data_9DL9
# 
_entry.id   9DL9 
# 
_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   9DL9         pdb_00009dl9 10.2210/pdb9dl9/pdb 
WWPDB D_1000287804 ?            ?                   
# 
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                        9DL9 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              tannerjj@missouri.edu 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tanner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8314-113X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanner, J.J.' 1 ? 
'Meeks, K.R.'  2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Molecules 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            29 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystallographic Fragment Screening of a Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates for Proline Dehydrogenase and L-Glutamate-gamma-semialdehyde Dehydrogenase.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/molecules29225408 
_citation.pdbx_database_id_PubMed   39598797 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Meeks, K.R.'  1 ? 
primary 'Bogner, A.N.' 2 ? 
primary 'Nix, J.C.'    3 ? 
primary 'Tanner, J.J.' 4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Bifunctional protein PutA'       131961.656 2    1.5.5.2,1.2.1.88 ? ? ? 
2  non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'     785.550    2    ?                ? ? ? 
3  non-polymer syn '(4-methoxyphenyl)methanol'       138.164    3    ?                ? ? ? 
4  non-polymer syn 'TRIETHYLENE GLYCOL'              150.173    3    ?                ? ? ? 
5  non-polymer syn 'FORMIC ACID'                     46.025     4    ?                ? ? ? 
6  non-polymer syn 'DI(HYDROXYETHYL)ETHER'           106.120    3    ?                ? ? ? 
7  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE 663.425    2    ?                ? ? ? 
8  non-polymer syn 'SULFATE ION'                     96.063     5    ?                ? ? ? 
9  non-polymer syn 'MAGNESIUM ION'                   24.305     2    ?                ? ? ? 
10 non-polymer syn 'PENTAETHYLENE GLYCOL'            238.278    1    ?                ? ? ? 
11 water       nat water                             18.015     2660 ?                ? ? ? 
# 
_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  '(4-methoxyphenyl)methanol'       A1BDD 
4  'TRIETHYLENE GLYCOL'              PGE   
5  'FORMIC ACID'                     FMT   
6  'DI(HYDROXYETHYL)ETHER'           PEG   
7  NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD   
8  'SULFATE ION'                     SO4   
9  'MAGNESIUM ION'                   MG    
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 
A1BDD non-polymer         . '(4-methoxyphenyl)methanol'       ?      'C8 H10 O2'         138.164 
ALA   'L-peptide linking' y ALANINE                           ?      'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                          ?      'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                        ?      'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                   ?      'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE                          ?      'C3 H7 N O2 S'      121.158 
FAD   non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'     ?      'C27 H33 N9 O15 P2' 785.550 
FMT   non-polymer         . 'FORMIC ACID'                     ?      'C H2 O2'           46.025  
GLN   'L-peptide linking' y GLUTAMINE                         ?      'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                   ?      'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                           ?      'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                         ?      'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                             ?      'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                        ?      'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                           ?      'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                            ?      'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                        ?      'C5 H11 N O2 S'     149.211 
MG    non-polymer         . 'MAGNESIUM ION'                   ?      'Mg 2'              24.305  
NAD   non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ?      'C21 H27 N7 O14 P2' 663.425 
PEG   non-polymer         . 'DI(HYDROXYETHYL)ETHER'           ?      'C4 H10 O3'         106.120 
PGE   non-polymer         . 'TRIETHYLENE GLYCOL'              ?      'C6 H14 O4'         150.173 
PHE   'L-peptide linking' y PHENYLALANINE                     ?      'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                           ?      'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                            ?      'C3 H7 N O3'        105.093 
SO4   non-polymer         . 'SULFATE ION'                     ?      'O4 S -2'           96.063  
THR   'L-peptide linking' y THREONINE                         ?      'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                        ?      'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                          ?      'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                            ?      'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    SER 1    -1   ?    ?   ?   A . n 
A 1 2    MET 2    0    ?    ?   ?   A . n 
A 1 3    MET 3    1    ?    ?   ?   A . n 
A 1 4    SER 4    2    ?    ?   ?   A . n 
A 1 5    PRO 5    3    ?    ?   ?   A . n 
A 1 6    ASN 6    4    ?    ?   ?   A . n 
A 1 7    PRO 7    5    ?    ?   ?   A . n 
A 1 8    LEU 8    6    ?    ?   ?   A . n 
A 1 9    GLN 9    7    ?    ?   ?   A . n 
A 1 10   LYS 10   8    ?    ?   ?   A . n 
A 1 11   PRO 11   9    ?    ?   ?   A . n 
A 1 12   ALA 12   10   ?    ?   ?   A . n 
A 1 13   ILE 13   11   ?    ?   ?   A . n 
A 1 14   ASP 14   12   ?    ?   ?   A . n 
A 1 15   ALA 15   13   ?    ?   ?   A . n 
A 1 16   ALA 16   14   14   ALA ALA A . n 
A 1 17   PRO 17   15   15   PRO PRO A . n 
A 1 18   ALA 18   16   16   ALA ALA A . n 
A 1 19   PRO 19   17   17   PRO PRO A . n 
A 1 20   PHE 20   18   18   PHE PHE A . n 
A 1 21   ALA 21   19   19   ALA ALA A . n 
A 1 22   ASP 22   20   20   ASP ASP A . n 
A 1 23   PHE 23   21   21   PHE PHE A . n 
A 1 24   ALA 24   22   22   ALA ALA A . n 
A 1 25   PRO 25   23   23   PRO PRO A . n 
A 1 26   PRO 26   24   24   PRO PRO A . n 
A 1 27   VAL 27   25   25   VAL VAL A . n 
A 1 28   ARG 28   26   26   ARG ARG A . n 
A 1 29   PRO 29   27   27   PRO PRO A . n 
A 1 30   GLN 30   28   28   GLN GLN A . n 
A 1 31   SER 31   29   29   SER SER A . n 
A 1 32   THR 32   30   30   THR THR A . n 
A 1 33   LEU 33   31   31   LEU LEU A . n 
A 1 34   ARG 34   32   32   ARG ARG A . n 
A 1 35   ARG 35   33   33   ARG ARG A . n 
A 1 36   ALA 36   34   34   ALA ALA A . n 
A 1 37   ILE 37   35   35   ILE ILE A . n 
A 1 38   THR 38   36   36   THR THR A . n 
A 1 39   ALA 39   37   37   ALA ALA A . n 
A 1 40   ALA 40   38   38   ALA ALA A . n 
A 1 41   TYR 41   39   39   TYR TYR A . n 
A 1 42   ARG 42   40   40   ARG ARG A . n 
A 1 43   ARG 43   41   41   ARG ARG A . n 
A 1 44   PRO 44   42   42   PRO PRO A . n 
A 1 45   GLU 45   43   43   GLU GLU A . n 
A 1 46   THR 46   44   44   THR THR A . n 
A 1 47   GLU 47   45   45   GLU GLU A . n 
A 1 48   CYS 48   46   46   CYS CYS A . n 
A 1 49   LEU 49   47   47   LEU LEU A . n 
A 1 50   PRO 50   48   48   PRO PRO A . n 
A 1 51   PRO 51   49   49   PRO PRO A . n 
A 1 52   LEU 52   50   50   LEU LEU A . n 
A 1 53   VAL 53   51   51   VAL VAL A . n 
A 1 54   GLU 54   52   52   GLU GLU A . n 
A 1 55   ALA 55   53   53   ALA ALA A . n 
A 1 56   ALA 56   54   54   ALA ALA A . n 
A 1 57   THR 57   55   55   THR THR A . n 
A 1 58   GLN 58   56   56   GLN GLN A . n 
A 1 59   SER 59   57   57   SER SER A . n 
A 1 60   LYS 60   58   58   LYS LYS A . n 
A 1 61   GLU 61   59   59   GLU GLU A . n 
A 1 62   ILE 62   60   60   ILE ILE A . n 
A 1 63   ARG 63   61   61   ARG ARG A . n 
A 1 64   ASP 64   62   62   ASP ASP A . n 
A 1 65   ALA 65   63   63   ALA ALA A . n 
A 1 66   ALA 66   64   64   ALA ALA A . n 
A 1 67   ALA 67   65   65   ALA ALA A . n 
A 1 68   SER 68   66   66   SER SER A . n 
A 1 69   THR 69   67   67   THR THR A . n 
A 1 70   ALA 70   68   68   ALA ALA A . n 
A 1 71   ARG 71   69   69   ARG ARG A . n 
A 1 72   LYS 72   70   70   LYS LYS A . n 
A 1 73   LEU 73   71   71   LEU LEU A . n 
A 1 74   ILE 74   72   72   ILE ILE A . n 
A 1 75   GLU 75   73   73   GLU GLU A . n 
A 1 76   ALA 76   74   74   ALA ALA A . n 
A 1 77   LEU 77   75   75   LEU LEU A . n 
A 1 78   ARG 78   76   76   ARG ARG A . n 
A 1 79   GLY 79   77   77   GLY GLY A . n 
A 1 80   LYS 80   78   78   LYS LYS A . n 
A 1 81   HIS 81   79   79   HIS HIS A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   82   SER SER A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  ?    ?   ?   A . n 
A 1 495  ASN 495  493  ?    ?   ?   A . n 
A 1 496  GLY 496  494  ?    ?   ?   A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU A . n 
A 1 1232 MET 1232 1230 1230 MET MET A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ILE 1234 1232 1232 ILE ILE A . n 
A 1 1235 GLY 1235 1233 1233 GLY GLY A . n 
B 1 1    SER 1    -1   ?    ?   ?   B . n 
B 1 2    MET 2    0    ?    ?   ?   B . n 
B 1 3    MET 3    1    ?    ?   ?   B . n 
B 1 4    SER 4    2    ?    ?   ?   B . n 
B 1 5    PRO 5    3    ?    ?   ?   B . n 
B 1 6    ASN 6    4    ?    ?   ?   B . n 
B 1 7    PRO 7    5    ?    ?   ?   B . n 
B 1 8    LEU 8    6    ?    ?   ?   B . n 
B 1 9    GLN 9    7    ?    ?   ?   B . n 
B 1 10   LYS 10   8    ?    ?   ?   B . n 
B 1 11   PRO 11   9    ?    ?   ?   B . n 
B 1 12   ALA 12   10   ?    ?   ?   B . n 
B 1 13   ILE 13   11   ?    ?   ?   B . n 
B 1 14   ASP 14   12   ?    ?   ?   B . n 
B 1 15   ALA 15   13   ?    ?   ?   B . n 
B 1 16   ALA 16   14   14   ALA ALA B . n 
B 1 17   PRO 17   15   15   PRO PRO B . n 
B 1 18   ALA 18   16   16   ALA ALA B . n 
B 1 19   PRO 19   17   17   PRO PRO B . n 
B 1 20   PHE 20   18   18   PHE PHE B . n 
B 1 21   ALA 21   19   19   ALA ALA B . n 
B 1 22   ASP 22   20   20   ASP ASP B . n 
B 1 23   PHE 23   21   21   PHE PHE B . n 
B 1 24   ALA 24   22   22   ALA ALA B . n 
B 1 25   PRO 25   23   23   PRO PRO B . n 
B 1 26   PRO 26   24   24   PRO PRO B . n 
B 1 27   VAL 27   25   25   VAL VAL B . n 
B 1 28   ARG 28   26   26   ARG ARG B . n 
B 1 29   PRO 29   27   27   PRO PRO B . n 
B 1 30   GLN 30   28   28   GLN GLN B . n 
B 1 31   SER 31   29   29   SER SER B . n 
B 1 32   THR 32   30   30   THR THR B . n 
B 1 33   LEU 33   31   31   LEU LEU B . n 
B 1 34   ARG 34   32   32   ARG ARG B . n 
B 1 35   ARG 35   33   33   ARG ARG B . n 
B 1 36   ALA 36   34   34   ALA ALA B . n 
B 1 37   ILE 37   35   35   ILE ILE B . n 
B 1 38   THR 38   36   36   THR THR B . n 
B 1 39   ALA 39   37   37   ALA ALA B . n 
B 1 40   ALA 40   38   38   ALA ALA B . n 
B 1 41   TYR 41   39   39   TYR TYR B . n 
B 1 42   ARG 42   40   40   ARG ARG B . n 
B 1 43   ARG 43   41   41   ARG ARG B . n 
B 1 44   PRO 44   42   42   PRO PRO B . n 
B 1 45   GLU 45   43   43   GLU GLU B . n 
B 1 46   THR 46   44   44   THR THR B . n 
B 1 47   GLU 47   45   45   GLU GLU B . n 
B 1 48   CYS 48   46   46   CYS CYS B . n 
B 1 49   LEU 49   47   47   LEU LEU B . n 
B 1 50   PRO 50   48   48   PRO PRO B . n 
B 1 51   PRO 51   49   49   PRO PRO B . n 
B 1 52   LEU 52   50   50   LEU LEU B . n 
B 1 53   VAL 53   51   51   VAL VAL B . n 
B 1 54   GLU 54   52   52   GLU GLU B . n 
B 1 55   ALA 55   53   53   ALA ALA B . n 
B 1 56   ALA 56   54   54   ALA ALA B . n 
B 1 57   THR 57   55   55   THR THR B . n 
B 1 58   GLN 58   56   56   GLN GLN B . n 
B 1 59   SER 59   57   57   SER SER B . n 
B 1 60   LYS 60   58   58   LYS LYS B . n 
B 1 61   GLU 61   59   59   GLU GLU B . n 
B 1 62   ILE 62   60   60   ILE ILE B . n 
B 1 63   ARG 63   61   61   ARG ARG B . n 
B 1 64   ASP 64   62   62   ASP ASP B . n 
B 1 65   ALA 65   63   63   ALA ALA B . n 
B 1 66   ALA 66   64   64   ALA ALA B . n 
B 1 67   ALA 67   65   65   ALA ALA B . n 
B 1 68   SER 68   66   66   SER SER B . n 
B 1 69   THR 69   67   67   THR THR B . n 
B 1 70   ALA 70   68   68   ALA ALA B . n 
B 1 71   ARG 71   69   69   ARG ARG B . n 
B 1 72   LYS 72   70   70   LYS LYS B . n 
B 1 73   LEU 73   71   71   LEU LEU B . n 
B 1 74   ILE 74   72   72   ILE ILE B . n 
B 1 75   GLU 75   73   73   GLU GLU B . n 
B 1 76   ALA 76   74   74   ALA ALA B . n 
B 1 77   LEU 77   75   75   LEU LEU B . n 
B 1 78   ARG 78   76   76   ARG ARG B . n 
B 1 79   GLY 79   77   77   GLY GLY B . n 
B 1 80   LYS 80   78   78   LYS LYS B . n 
B 1 81   HIS 81   79   ?    ?   ?   B . n 
B 1 82   SER 82   80   ?    ?   ?   B . n 
B 1 83   GLY 83   81   ?    ?   ?   B . n 
B 1 84   SER 84   82   ?    ?   ?   B . n 
B 1 85   GLY 85   83   83   GLY GLY B . n 
B 1 86   VAL 86   84   84   VAL VAL B . n 
B 1 87   GLU 87   85   85   GLU GLU B . n 
B 1 88   GLY 88   86   86   GLY GLY B . n 
B 1 89   LEU 89   87   87   LEU LEU B . n 
B 1 90   VAL 90   88   88   VAL VAL B . n 
B 1 91   GLN 91   89   89   GLN GLN B . n 
B 1 92   GLU 92   90   90   GLU GLU B . n 
B 1 93   TYR 93   91   91   TYR TYR B . n 
B 1 94   SER 94   92   92   SER SER B . n 
B 1 95   LEU 95   93   93   LEU LEU B . n 
B 1 96   SER 96   94   94   SER SER B . n 
B 1 97   SER 97   95   95   SER SER B . n 
B 1 98   GLN 98   96   96   GLN GLN B . n 
B 1 99   GLU 99   97   97   GLU GLU B . n 
B 1 100  GLY 100  98   98   GLY GLY B . n 
B 1 101  VAL 101  99   99   VAL VAL B . n 
B 1 102  ALA 102  100  100  ALA ALA B . n 
B 1 103  LEU 103  101  101  LEU LEU B . n 
B 1 104  MET 104  102  102  MET MET B . n 
B 1 105  CYS 105  103  103  CYS CYS B . n 
B 1 106  LEU 106  104  104  LEU LEU B . n 
B 1 107  ALA 107  105  105  ALA ALA B . n 
B 1 108  GLU 108  106  106  GLU GLU B . n 
B 1 109  ALA 109  107  107  ALA ALA B . n 
B 1 110  LEU 110  108  108  LEU LEU B . n 
B 1 111  LEU 111  109  109  LEU LEU B . n 
B 1 112  ARG 112  110  110  ARG ARG B . n 
B 1 113  ILE 113  111  111  ILE ILE B . n 
B 1 114  PRO 114  112  112  PRO PRO B . n 
B 1 115  ASP 115  113  113  ASP ASP B . n 
B 1 116  THR 116  114  114  THR THR B . n 
B 1 117  ALA 117  115  115  ALA ALA B . n 
B 1 118  THR 118  116  116  THR THR B . n 
B 1 119  ARG 119  117  117  ARG ARG B . n 
B 1 120  ASP 120  118  118  ASP ASP B . n 
B 1 121  ALA 121  119  119  ALA ALA B . n 
B 1 122  LEU 122  120  120  LEU LEU B . n 
B 1 123  ILE 123  121  121  ILE ILE B . n 
B 1 124  ARG 124  122  122  ARG ARG B . n 
B 1 125  ASP 125  123  123  ASP ASP B . n 
B 1 126  LYS 126  124  124  LYS LYS B . n 
B 1 127  ILE 127  125  125  ILE ILE B . n 
B 1 128  ALA 128  126  126  ALA ALA B . n 
B 1 129  ASP 129  127  127  ASP ASP B . n 
B 1 130  GLY 130  128  128  GLY GLY B . n 
B 1 131  ASN 131  129  129  ASN ASN B . n 
B 1 132  TRP 132  130  130  TRP TRP B . n 
B 1 133  LYS 133  131  131  LYS LYS B . n 
B 1 134  SER 134  132  132  SER SER B . n 
B 1 135  HIS 135  133  133  HIS HIS B . n 
B 1 136  LEU 136  134  134  LEU LEU B . n 
B 1 137  GLY 137  135  ?    ?   ?   B . n 
B 1 138  GLY 138  136  ?    ?   ?   B . n 
B 1 139  SER 139  137  ?    ?   ?   B . n 
B 1 140  ARG 140  138  138  ARG ARG B . n 
B 1 141  SER 141  139  139  SER SER B . n 
B 1 142  LEU 142  140  140  LEU LEU B . n 
B 1 143  PHE 143  141  141  PHE PHE B . n 
B 1 144  VAL 144  142  142  VAL VAL B . n 
B 1 145  ASN 145  143  143  ASN ASN B . n 
B 1 146  ALA 146  144  144  ALA ALA B . n 
B 1 147  ALA 147  145  145  ALA ALA B . n 
B 1 148  THR 148  146  146  THR THR B . n 
B 1 149  TRP 149  147  147  TRP TRP B . n 
B 1 150  GLY 150  148  148  GLY GLY B . n 
B 1 151  LEU 151  149  149  LEU LEU B . n 
B 1 152  VAL 152  150  150  VAL VAL B . n 
B 1 153  VAL 153  151  151  VAL VAL B . n 
B 1 154  THR 154  152  152  THR THR B . n 
B 1 155  GLY 155  153  153  GLY GLY B . n 
B 1 156  LYS 156  154  154  LYS LYS B . n 
B 1 157  LEU 157  155  155  LEU LEU B . n 
B 1 158  THR 158  156  156  THR THR B . n 
B 1 159  SER 159  157  157  SER SER B . n 
B 1 160  THR 160  158  158  THR THR B . n 
B 1 161  VAL 161  159  159  VAL VAL B . n 
B 1 162  ASN 162  160  160  ASN ASN B . n 
B 1 163  ASP 163  161  161  ASP ASP B . n 
B 1 164  ARG 164  162  162  ARG ARG B . n 
B 1 165  SER 165  163  163  SER SER B . n 
B 1 166  LEU 166  164  164  LEU LEU B . n 
B 1 167  ALA 167  165  165  ALA ALA B . n 
B 1 168  ALA 168  166  166  ALA ALA B . n 
B 1 169  ALA 169  167  167  ALA ALA B . n 
B 1 170  LEU 170  168  168  LEU LEU B . n 
B 1 171  THR 171  169  169  THR THR B . n 
B 1 172  ARG 172  170  170  ARG ARG B . n 
B 1 173  LEU 173  171  171  LEU LEU B . n 
B 1 174  ILE 174  172  172  ILE ILE B . n 
B 1 175  SER 175  173  173  SER SER B . n 
B 1 176  ARG 176  174  174  ARG ARG B . n 
B 1 177  CYS 177  175  175  CYS CYS B . n 
B 1 178  GLY 178  176  176  GLY GLY B . n 
B 1 179  GLU 179  177  177  GLU GLU B . n 
B 1 180  PRO 180  178  178  PRO PRO B . n 
B 1 181  VAL 181  179  179  VAL VAL B . n 
B 1 182  ILE 182  180  180  ILE ILE B . n 
B 1 183  ARG 183  181  181  ARG ARG B . n 
B 1 184  ARG 184  182  182  ARG ARG B . n 
B 1 185  GLY 185  183  183  GLY GLY B . n 
B 1 186  VAL 186  184  184  VAL VAL B . n 
B 1 187  ASP 187  185  185  ASP ASP B . n 
B 1 188  MET 188  186  186  MET MET B . n 
B 1 189  ALA 189  187  187  ALA ALA B . n 
B 1 190  MET 190  188  188  MET MET B . n 
B 1 191  ARG 191  189  189  ARG ARG B . n 
B 1 192  MET 192  190  190  MET MET B . n 
B 1 193  MET 193  191  191  MET MET B . n 
B 1 194  GLY 194  192  192  GLY GLY B . n 
B 1 195  GLU 195  193  193  GLU GLU B . n 
B 1 196  GLN 196  194  194  GLN GLN B . n 
B 1 197  PHE 197  195  195  PHE PHE B . n 
B 1 198  VAL 198  196  196  VAL VAL B . n 
B 1 199  THR 199  197  197  THR THR B . n 
B 1 200  GLY 200  198  198  GLY GLY B . n 
B 1 201  GLU 201  199  199  GLU GLU B . n 
B 1 202  THR 202  200  200  THR THR B . n 
B 1 203  ILE 203  201  201  ILE ILE B . n 
B 1 204  ARG 204  202  202  ARG ARG B . n 
B 1 205  GLU 205  203  203  GLU GLU B . n 
B 1 206  ALA 206  204  204  ALA ALA B . n 
B 1 207  LEU 207  205  205  LEU LEU B . n 
B 1 208  LYS 208  206  206  LYS LYS B . n 
B 1 209  ARG 209  207  207  ARG ARG B . n 
B 1 210  SER 210  208  208  SER SER B . n 
B 1 211  LYS 211  209  209  LYS LYS B . n 
B 1 212  GLU 212  210  210  GLU GLU B . n 
B 1 213  LEU 213  211  211  LEU LEU B . n 
B 1 214  GLU 214  212  212  GLU GLU B . n 
B 1 215  GLU 215  213  213  GLU GLU B . n 
B 1 216  LYS 216  214  214  LYS LYS B . n 
B 1 217  GLY 217  215  215  GLY GLY B . n 
B 1 218  PHE 218  216  216  PHE PHE B . n 
B 1 219  SER 219  217  217  SER SER B . n 
B 1 220  TYR 220  218  218  TYR TYR B . n 
B 1 221  SER 221  219  219  SER SER B . n 
B 1 222  TYR 222  220  220  TYR TYR B . n 
B 1 223  ASP 223  221  221  ASP ASP B . n 
B 1 224  MET 224  222  222  MET MET B . n 
B 1 225  LEU 225  223  223  LEU LEU B . n 
B 1 226  GLY 226  224  224  GLY GLY B . n 
B 1 227  GLU 227  225  225  GLU GLU B . n 
B 1 228  ALA 228  226  226  ALA ALA B . n 
B 1 229  ALA 229  227  227  ALA ALA B . n 
B 1 230  THR 230  228  228  THR THR B . n 
B 1 231  THR 231  229  229  THR THR B . n 
B 1 232  ALA 232  230  230  ALA ALA B . n 
B 1 233  ALA 233  231  231  ALA ALA B . n 
B 1 234  ASP 234  232  232  ASP ASP B . n 
B 1 235  ALA 235  233  233  ALA ALA B . n 
B 1 236  GLU 236  234  234  GLU GLU B . n 
B 1 237  ARG 237  235  235  ARG ARG B . n 
B 1 238  TYR 238  236  236  TYR TYR B . n 
B 1 239  TYR 239  237  237  TYR TYR B . n 
B 1 240  ARG 240  238  238  ARG ARG B . n 
B 1 241  ASP 241  239  239  ASP ASP B . n 
B 1 242  TYR 242  240  240  TYR TYR B . n 
B 1 243  GLU 243  241  241  GLU GLU B . n 
B 1 244  SER 244  242  242  SER SER B . n 
B 1 245  ALA 245  243  243  ALA ALA B . n 
B 1 246  ILE 246  244  244  ILE ILE B . n 
B 1 247  HIS 247  245  245  HIS HIS B . n 
B 1 248  ALA 248  246  246  ALA ALA B . n 
B 1 249  ILE 249  247  247  ILE ILE B . n 
B 1 250  GLY 250  248  248  GLY GLY B . n 
B 1 251  LYS 251  249  249  LYS LYS B . n 
B 1 252  ALA 252  250  250  ALA ALA B . n 
B 1 253  SER 253  251  251  SER SER B . n 
B 1 254  ALA 254  252  252  ALA ALA B . n 
B 1 255  GLY 255  253  253  GLY GLY B . n 
B 1 256  ARG 256  254  254  ARG ARG B . n 
B 1 257  GLY 257  255  255  GLY GLY B . n 
B 1 258  ILE 258  256  256  ILE ILE B . n 
B 1 259  TYR 259  257  257  TYR TYR B . n 
B 1 260  GLU 260  258  258  GLU GLU B . n 
B 1 261  GLY 261  259  259  GLY GLY B . n 
B 1 262  PRO 262  260  260  PRO PRO B . n 
B 1 263  GLY 263  261  261  GLY GLY B . n 
B 1 264  ILE 264  262  262  ILE ILE B . n 
B 1 265  SER 265  263  263  SER SER B . n 
B 1 266  ILE 266  264  264  ILE ILE B . n 
B 1 267  LYS 267  265  265  LYS LYS B . n 
B 1 268  LEU 268  266  266  LEU LEU B . n 
B 1 269  SER 269  267  267  SER SER B . n 
B 1 270  ALA 270  268  268  ALA ALA B . n 
B 1 271  LEU 271  269  269  LEU LEU B . n 
B 1 272  HIS 272  270  270  HIS HIS B . n 
B 1 273  PRO 273  271  271  PRO PRO B . n 
B 1 274  ARG 274  272  272  ARG ARG B . n 
B 1 275  TYR 275  273  273  TYR TYR B . n 
B 1 276  SER 276  274  274  SER SER B . n 
B 1 277  ARG 277  275  275  ARG ARG B . n 
B 1 278  ALA 278  276  276  ALA ALA B . n 
B 1 279  GLN 279  277  277  GLN GLN B . n 
B 1 280  ALA 280  278  278  ALA ALA B . n 
B 1 281  ALA 281  279  279  ALA ALA B . n 
B 1 282  ARG 282  280  280  ARG ARG B . n 
B 1 283  VAL 283  281  281  VAL VAL B . n 
B 1 284  MET 284  282  282  MET MET B . n 
B 1 285  GLY 285  283  283  GLY GLY B . n 
B 1 286  GLU 286  284  284  GLU GLU B . n 
B 1 287  LEU 287  285  285  LEU LEU B . n 
B 1 288  LEU 288  286  286  LEU LEU B . n 
B 1 289  PRO 289  287  287  PRO PRO B . n 
B 1 290  ARG 290  288  288  ARG ARG B . n 
B 1 291  VAL 291  289  289  VAL VAL B . n 
B 1 292  LYS 292  290  290  LYS LYS B . n 
B 1 293  ALA 293  291  291  ALA ALA B . n 
B 1 294  LEU 294  292  292  LEU LEU B . n 
B 1 295  ALA 295  293  293  ALA ALA B . n 
B 1 296  LEU 296  294  294  LEU LEU B . n 
B 1 297  LEU 297  295  295  LEU LEU B . n 
B 1 298  ALA 298  296  296  ALA ALA B . n 
B 1 299  LYS 299  297  297  LYS LYS B . n 
B 1 300  ASN 300  298  298  ASN ASN B . n 
B 1 301  TYR 301  299  299  TYR TYR B . n 
B 1 302  ASP 302  300  300  ASP ASP B . n 
B 1 303  ILE 303  301  301  ILE ILE B . n 
B 1 304  GLY 304  302  302  GLY GLY B . n 
B 1 305  LEU 305  303  303  LEU LEU B . n 
B 1 306  ASN 306  304  304  ASN ASN B . n 
B 1 307  ILE 307  305  305  ILE ILE B . n 
B 1 308  ASP 308  306  306  ASP ASP B . n 
B 1 309  ALA 309  307  307  ALA ALA B . n 
B 1 310  GLU 310  308  308  GLU GLU B . n 
B 1 311  GLU 311  309  309  GLU GLU B . n 
B 1 312  ALA 312  310  310  ALA ALA B . n 
B 1 313  ASP 313  311  311  ASP ASP B . n 
B 1 314  ARG 314  312  312  ARG ARG B . n 
B 1 315  LEU 315  313  313  LEU LEU B . n 
B 1 316  GLU 316  314  314  GLU GLU B . n 
B 1 317  LEU 317  315  315  LEU LEU B . n 
B 1 318  SER 318  316  316  SER SER B . n 
B 1 319  LEU 319  317  317  LEU LEU B . n 
B 1 320  ASP 320  318  318  ASP ASP B . n 
B 1 321  LEU 321  319  319  LEU LEU B . n 
B 1 322  LEU 322  320  320  LEU LEU B . n 
B 1 323  GLU 323  321  321  GLU GLU B . n 
B 1 324  VAL 324  322  322  VAL VAL B . n 
B 1 325  LEU 325  323  323  LEU LEU B . n 
B 1 326  CYS 326  324  324  CYS CYS B . n 
B 1 327  LEU 327  325  325  LEU LEU B . n 
B 1 328  ASP 328  326  326  ASP ASP B . n 
B 1 329  GLY 329  327  327  GLY GLY B . n 
B 1 330  ASP 330  328  328  ASP ASP B . n 
B 1 331  LEU 331  329  329  LEU LEU B . n 
B 1 332  SER 332  330  330  SER SER B . n 
B 1 333  GLY 333  331  331  GLY GLY B . n 
B 1 334  TRP 334  332  332  TRP TRP B . n 
B 1 335  ASN 335  333  333  ASN ASN B . n 
B 1 336  GLY 336  334  334  GLY GLY B . n 
B 1 337  MET 337  335  335  MET MET B . n 
B 1 338  GLY 338  336  336  GLY GLY B . n 
B 1 339  PHE 339  337  337  PHE PHE B . n 
B 1 340  VAL 340  338  338  VAL VAL B . n 
B 1 341  VAL 341  339  339  VAL VAL B . n 
B 1 342  GLN 342  340  340  GLN GLN B . n 
B 1 343  ALA 343  341  341  ALA ALA B . n 
B 1 344  TYR 344  342  342  TYR TYR B . n 
B 1 345  GLY 345  343  343  GLY GLY B . n 
B 1 346  LYS 346  344  344  LYS LYS B . n 
B 1 347  ARG 347  345  345  ARG ARG B . n 
B 1 348  CYS 348  346  346  CYS CYS B . n 
B 1 349  PRO 349  347  347  PRO PRO B . n 
B 1 350  PHE 350  348  348  PHE PHE B . n 
B 1 351  VAL 351  349  349  VAL VAL B . n 
B 1 352  LEU 352  350  350  LEU LEU B . n 
B 1 353  ASP 353  351  351  ASP ASP B . n 
B 1 354  PHE 354  352  352  PHE PHE B . n 
B 1 355  ILE 355  353  353  ILE ILE B . n 
B 1 356  ILE 356  354  354  ILE ILE B . n 
B 1 357  ASP 357  355  355  ASP ASP B . n 
B 1 358  LEU 358  356  356  LEU LEU B . n 
B 1 359  ALA 359  357  357  ALA ALA B . n 
B 1 360  ARG 360  358  358  ARG ARG B . n 
B 1 361  ARG 361  359  359  ARG ARG B . n 
B 1 362  SER 362  360  360  SER SER B . n 
B 1 363  GLY 363  361  361  GLY GLY B . n 
B 1 364  ARG 364  362  362  ARG ARG B . n 
B 1 365  ARG 365  363  363  ARG ARG B . n 
B 1 366  ILE 366  364  364  ILE ILE B . n 
B 1 367  MET 367  365  365  MET MET B . n 
B 1 368  VAL 368  366  366  VAL VAL B . n 
B 1 369  ARG 369  367  367  ARG ARG B . n 
B 1 370  LEU 370  368  368  LEU LEU B . n 
B 1 371  VAL 371  369  369  VAL VAL B . n 
B 1 372  LYS 372  370  370  LYS LYS B . n 
B 1 373  GLY 373  371  371  GLY GLY B . n 
B 1 374  ALA 374  372  372  ALA ALA B . n 
B 1 375  TYR 375  373  373  TYR TYR B . n 
B 1 376  TRP 376  374  374  TRP TRP B . n 
B 1 377  ASP 377  375  375  ASP ASP B . n 
B 1 378  ALA 378  376  376  ALA ALA B . n 
B 1 379  GLU 379  377  377  GLU GLU B . n 
B 1 380  ILE 380  378  378  ILE ILE B . n 
B 1 381  LYS 381  379  379  LYS LYS B . n 
B 1 382  ARG 382  380  380  ARG ARG B . n 
B 1 383  ALA 383  381  381  ALA ALA B . n 
B 1 384  GLN 384  382  382  GLN GLN B . n 
B 1 385  LEU 385  383  383  LEU LEU B . n 
B 1 386  ASP 386  384  384  ASP ASP B . n 
B 1 387  GLY 387  385  385  GLY GLY B . n 
B 1 388  LEU 388  386  386  LEU LEU B . n 
B 1 389  ALA 389  387  387  ALA ALA B . n 
B 1 390  ASP 390  388  388  ASP ASP B . n 
B 1 391  PHE 391  389  389  PHE PHE B . n 
B 1 392  PRO 392  390  390  PRO PRO B . n 
B 1 393  VAL 393  391  391  VAL VAL B . n 
B 1 394  PHE 394  392  392  PHE PHE B . n 
B 1 395  THR 395  393  393  THR THR B . n 
B 1 396  ARG 396  394  394  ARG ARG B . n 
B 1 397  LYS 397  395  395  LYS LYS B . n 
B 1 398  ILE 398  396  396  ILE ILE B . n 
B 1 399  HIS 399  397  397  HIS HIS B . n 
B 1 400  THR 400  398  398  THR THR B . n 
B 1 401  ASP 401  399  399  ASP ASP B . n 
B 1 402  VAL 402  400  400  VAL VAL B . n 
B 1 403  SER 403  401  401  SER SER B . n 
B 1 404  TYR 404  402  402  TYR TYR B . n 
B 1 405  ILE 405  403  403  ILE ILE B . n 
B 1 406  ALA 406  404  404  ALA ALA B . n 
B 1 407  CYS 407  405  405  CYS CYS B . n 
B 1 408  ALA 408  406  406  ALA ALA B . n 
B 1 409  ALA 409  407  407  ALA ALA B . n 
B 1 410  LYS 410  408  408  LYS LYS B . n 
B 1 411  LEU 411  409  409  LEU LEU B . n 
B 1 412  LEU 412  410  410  LEU LEU B . n 
B 1 413  ALA 413  411  411  ALA ALA B . n 
B 1 414  ALA 414  412  412  ALA ALA B . n 
B 1 415  THR 415  413  413  THR THR B . n 
B 1 416  ASP 416  414  414  ASP ASP B . n 
B 1 417  VAL 417  415  415  VAL VAL B . n 
B 1 418  VAL 418  416  416  VAL VAL B . n 
B 1 419  PHE 419  417  417  PHE PHE B . n 
B 1 420  PRO 420  418  418  PRO PRO B . n 
B 1 421  GLN 421  419  419  GLN GLN B . n 
B 1 422  PHE 422  420  420  PHE PHE B . n 
B 1 423  ALA 423  421  421  ALA ALA B . n 
B 1 424  THR 424  422  422  THR THR B . n 
B 1 425  HIS 425  423  423  HIS HIS B . n 
B 1 426  ASN 426  424  424  ASN ASN B . n 
B 1 427  ALA 427  425  425  ALA ALA B . n 
B 1 428  GLN 428  426  426  GLN GLN B . n 
B 1 429  THR 429  427  427  THR THR B . n 
B 1 430  LEU 430  428  428  LEU LEU B . n 
B 1 431  ALA 431  429  429  ALA ALA B . n 
B 1 432  ALA 432  430  430  ALA ALA B . n 
B 1 433  ILE 433  431  431  ILE ILE B . n 
B 1 434  TYR 434  432  432  TYR TYR B . n 
B 1 435  HIS 435  433  433  HIS HIS B . n 
B 1 436  MET 436  434  434  MET MET B . n 
B 1 437  ALA 437  435  435  ALA ALA B . n 
B 1 438  GLY 438  436  436  GLY GLY B . n 
B 1 439  LYS 439  437  437  LYS LYS B . n 
B 1 440  ASP 440  438  438  ASP ASP B . n 
B 1 441  PHE 441  439  439  PHE PHE B . n 
B 1 442  HIS 442  440  440  HIS HIS B . n 
B 1 443  VAL 443  441  441  VAL VAL B . n 
B 1 444  GLY 444  442  442  GLY GLY B . n 
B 1 445  LYS 445  443  443  LYS LYS B . n 
B 1 446  TYR 446  444  444  TYR TYR B . n 
B 1 447  GLU 447  445  445  GLU GLU B . n 
B 1 448  PHE 448  446  446  PHE PHE B . n 
B 1 449  GLN 449  447  447  GLN GLN B . n 
B 1 450  CYS 450  448  448  CYS CYS B . n 
B 1 451  LEU 451  449  449  LEU LEU B . n 
B 1 452  HIS 452  450  450  HIS HIS B . n 
B 1 453  GLY 453  451  451  GLY GLY B . n 
B 1 454  MET 454  452  452  MET MET B . n 
B 1 455  GLY 455  453  453  GLY GLY B . n 
B 1 456  GLU 456  454  454  GLU GLU B . n 
B 1 457  PRO 457  455  455  PRO PRO B . n 
B 1 458  LEU 458  456  456  LEU LEU B . n 
B 1 459  TYR 459  457  457  TYR TYR B . n 
B 1 460  GLU 460  458  458  GLU GLU B . n 
B 1 461  GLU 461  459  459  GLU GLU B . n 
B 1 462  VAL 462  460  460  VAL VAL B . n 
B 1 463  VAL 463  461  461  VAL VAL B . n 
B 1 464  GLY 464  462  462  GLY GLY B . n 
B 1 465  ARG 465  463  463  ARG ARG B . n 
B 1 466  GLY 466  464  464  GLY GLY B . n 
B 1 467  LYS 467  465  465  LYS LYS B . n 
B 1 468  LEU 468  466  466  LEU LEU B . n 
B 1 469  ASP 469  467  467  ASP ASP B . n 
B 1 470  ARG 470  468  468  ARG ARG B . n 
B 1 471  PRO 471  469  469  PRO PRO B . n 
B 1 472  CYS 472  470  470  CYS CYS B . n 
B 1 473  ARG 473  471  471  ARG ARG B . n 
B 1 474  ILE 474  472  472  ILE ILE B . n 
B 1 475  TYR 475  473  473  TYR TYR B . n 
B 1 476  ALA 476  474  474  ALA ALA B . n 
B 1 477  PRO 477  475  475  PRO PRO B . n 
B 1 478  VAL 478  476  476  VAL VAL B . n 
B 1 479  GLY 479  477  477  GLY GLY B . n 
B 1 480  THR 480  478  478  THR THR B . n 
B 1 481  HIS 481  479  479  HIS HIS B . n 
B 1 482  GLU 482  480  480  GLU GLU B . n 
B 1 483  THR 483  481  481  THR THR B . n 
B 1 484  LEU 484  482  482  LEU LEU B . n 
B 1 485  LEU 485  483  483  LEU LEU B . n 
B 1 486  ALA 486  484  484  ALA ALA B . n 
B 1 487  TYR 487  485  485  TYR TYR B . n 
B 1 488  LEU 488  486  486  LEU LEU B . n 
B 1 489  VAL 489  487  487  VAL VAL B . n 
B 1 490  ARG 490  488  488  ARG ARG B . n 
B 1 491  ARG 491  489  489  ARG ARG B . n 
B 1 492  LEU 492  490  490  LEU LEU B . n 
B 1 493  LEU 493  491  491  LEU LEU B . n 
B 1 494  GLU 494  492  492  GLU GLU B . n 
B 1 495  ASN 495  493  493  ASN ASN B . n 
B 1 496  GLY 496  494  494  GLY GLY B . n 
B 1 497  ALA 497  495  495  ALA ALA B . n 
B 1 498  ASN 498  496  496  ASN ASN B . n 
B 1 499  SER 499  497  497  SER SER B . n 
B 1 500  SER 500  498  498  SER SER B . n 
B 1 501  PHE 501  499  499  PHE PHE B . n 
B 1 502  VAL 502  500  500  VAL VAL B . n 
B 1 503  HIS 503  501  501  HIS HIS B . n 
B 1 504  ARG 504  502  502  ARG ARG B . n 
B 1 505  ILE 505  503  503  ILE ILE B . n 
B 1 506  ASN 506  504  504  ASN ASN B . n 
B 1 507  ASP 507  505  505  ASP ASP B . n 
B 1 508  PRO 508  506  506  PRO PRO B . n 
B 1 509  LYS 509  507  507  LYS LYS B . n 
B 1 510  VAL 510  508  508  VAL VAL B . n 
B 1 511  SER 511  509  509  SER SER B . n 
B 1 512  ILE 512  510  510  ILE ILE B . n 
B 1 513  ASP 513  511  511  ASP ASP B . n 
B 1 514  GLU 514  512  512  GLU GLU B . n 
B 1 515  LEU 515  513  513  LEU LEU B . n 
B 1 516  ILE 516  514  514  ILE ILE B . n 
B 1 517  ALA 517  515  515  ALA ALA B . n 
B 1 518  ASP 518  516  516  ASP ASP B . n 
B 1 519  PRO 519  517  517  PRO PRO B . n 
B 1 520  VAL 520  518  518  VAL VAL B . n 
B 1 521  GLU 521  519  519  GLU GLU B . n 
B 1 522  VAL 522  520  520  VAL VAL B . n 
B 1 523  VAL 523  521  521  VAL VAL B . n 
B 1 524  ARG 524  522  522  ARG ARG B . n 
B 1 525  ALA 525  523  523  ALA ALA B . n 
B 1 526  MET 526  524  524  MET MET B . n 
B 1 527  PRO 527  525  525  PRO PRO B . n 
B 1 528  VAL 528  526  526  VAL VAL B . n 
B 1 529  VAL 529  527  527  VAL VAL B . n 
B 1 530  GLY 530  528  528  GLY GLY B . n 
B 1 531  ALA 531  529  529  ALA ALA B . n 
B 1 532  LYS 532  530  530  LYS LYS B . n 
B 1 533  HIS 533  531  531  HIS HIS B . n 
B 1 534  ASP 534  532  532  ASP ASP B . n 
B 1 535  ARG 535  533  533  ARG ARG B . n 
B 1 536  ILE 536  534  534  ILE ILE B . n 
B 1 537  ALA 537  535  535  ALA ALA B . n 
B 1 538  LEU 538  536  536  LEU LEU B . n 
B 1 539  PRO 539  537  537  PRO PRO B . n 
B 1 540  ALA 540  538  538  ALA ALA B . n 
B 1 541  GLU 541  539  539  GLU GLU B . n 
B 1 542  LEU 542  540  540  LEU LEU B . n 
B 1 543  PHE 543  541  541  PHE PHE B . n 
B 1 544  GLY 544  542  542  GLY GLY B . n 
B 1 545  ASP 545  543  543  ASP ASP B . n 
B 1 546  ALA 546  544  544  ALA ALA B . n 
B 1 547  ARG 547  545  545  ARG ARG B . n 
B 1 548  THR 548  546  546  THR THR B . n 
B 1 549  ASN 549  547  547  ASN ASN B . n 
B 1 550  SER 550  548  548  SER SER B . n 
B 1 551  ALA 551  549  549  ALA ALA B . n 
B 1 552  GLY 552  550  550  GLY GLY B . n 
B 1 553  LEU 553  551  551  LEU LEU B . n 
B 1 554  ASP 554  552  552  ASP ASP B . n 
B 1 555  LEU 555  553  553  LEU LEU B . n 
B 1 556  SER 556  554  554  SER SER B . n 
B 1 557  ASN 557  555  555  ASN ASN B . n 
B 1 558  GLU 558  556  556  GLU GLU B . n 
B 1 559  GLU 559  557  557  GLU GLU B . n 
B 1 560  THR 560  558  558  THR THR B . n 
B 1 561  LEU 561  559  559  LEU LEU B . n 
B 1 562  ALA 562  560  560  ALA ALA B . n 
B 1 563  SER 563  561  561  SER SER B . n 
B 1 564  LEU 564  562  562  LEU LEU B . n 
B 1 565  THR 565  563  563  THR THR B . n 
B 1 566  GLU 566  564  564  GLU GLU B . n 
B 1 567  ALA 567  565  565  ALA ALA B . n 
B 1 568  LEU 568  566  566  LEU LEU B . n 
B 1 569  ARG 569  567  567  ARG ARG B . n 
B 1 570  GLU 570  568  568  GLU GLU B . n 
B 1 571  SER 571  569  569  SER SER B . n 
B 1 572  ALA 572  570  570  ALA ALA B . n 
B 1 573  ALA 573  571  571  ALA ALA B . n 
B 1 574  MET 574  572  572  MET MET B . n 
B 1 575  LYS 575  573  573  LYS LYS B . n 
B 1 576  TRP 576  574  574  TRP TRP B . n 
B 1 577  THR 577  575  575  THR THR B . n 
B 1 578  ALA 578  576  576  ALA ALA B . n 
B 1 579  LEU 579  577  577  LEU LEU B . n 
B 1 580  PRO 580  578  578  PRO PRO B . n 
B 1 581  GLN 581  579  579  GLN GLN B . n 
B 1 582  LEU 582  580  580  LEU LEU B . n 
B 1 583  ALA 583  581  581  ALA ALA B . n 
B 1 584  THR 584  582  582  THR THR B . n 
B 1 585  GLY 585  583  583  GLY GLY B . n 
B 1 586  PRO 586  584  584  PRO PRO B . n 
B 1 587  ALA 587  585  585  ALA ALA B . n 
B 1 588  ALA 588  586  586  ALA ALA B . n 
B 1 589  GLY 589  587  587  GLY GLY B . n 
B 1 590  GLU 590  588  588  GLU GLU B . n 
B 1 591  THR 591  589  589  THR THR B . n 
B 1 592  ARG 592  590  590  ARG ARG B . n 
B 1 593  THR 593  591  591  THR THR B . n 
B 1 594  VAL 594  592  592  VAL VAL B . n 
B 1 595  LEU 595  593  593  LEU LEU B . n 
B 1 596  ASN 596  594  594  ASN ASN B . n 
B 1 597  PRO 597  595  595  PRO PRO B . n 
B 1 598  GLY 598  596  596  GLY GLY B . n 
B 1 599  ASP 599  597  597  ASP ASP B . n 
B 1 600  HIS 600  598  598  HIS HIS B . n 
B 1 601  ARG 601  599  599  ARG ARG B . n 
B 1 602  ASP 602  600  600  ASP ASP B . n 
B 1 603  VAL 603  601  601  VAL VAL B . n 
B 1 604  VAL 604  602  602  VAL VAL B . n 
B 1 605  GLY 605  603  603  GLY GLY B . n 
B 1 606  SER 606  604  604  SER SER B . n 
B 1 607  VAL 607  605  605  VAL VAL B . n 
B 1 608  THR 608  606  606  THR THR B . n 
B 1 609  GLU 609  607  607  GLU GLU B . n 
B 1 610  THR 610  608  608  THR THR B . n 
B 1 611  SER 611  609  609  SER SER B . n 
B 1 612  GLU 612  610  610  GLU GLU B . n 
B 1 613  GLU 613  611  611  GLU GLU B . n 
B 1 614  ASP 614  612  612  ASP ASP B . n 
B 1 615  ALA 615  613  613  ALA ALA B . n 
B 1 616  ARG 616  614  614  ARG ARG B . n 
B 1 617  ARG 617  615  615  ARG ARG B . n 
B 1 618  ALA 618  616  616  ALA ALA B . n 
B 1 619  VAL 619  617  617  VAL VAL B . n 
B 1 620  ARG 620  618  618  ARG ARG B . n 
B 1 621  LEU 621  619  619  LEU LEU B . n 
B 1 622  ALA 622  620  620  ALA ALA B . n 
B 1 623  ALA 623  621  621  ALA ALA B . n 
B 1 624  ASP 624  622  622  ASP ASP B . n 
B 1 625  ALA 625  623  623  ALA ALA B . n 
B 1 626  ALA 626  624  624  ALA ALA B . n 
B 1 627  PRO 627  625  625  PRO PRO B . n 
B 1 628  ASP 628  626  626  ASP ASP B . n 
B 1 629  TRP 629  627  627  TRP TRP B . n 
B 1 630  ALA 630  628  628  ALA ALA B . n 
B 1 631  ALA 631  629  629  ALA ALA B . n 
B 1 632  VAL 632  630  630  VAL VAL B . n 
B 1 633  PRO 633  631  631  PRO PRO B . n 
B 1 634  PRO 634  632  632  PRO PRO B . n 
B 1 635  SER 635  633  633  SER SER B . n 
B 1 636  GLU 636  634  634  GLU GLU B . n 
B 1 637  ARG 637  635  635  ARG ARG B . n 
B 1 638  ALA 638  636  636  ALA ALA B . n 
B 1 639  ALA 639  637  637  ALA ALA B . n 
B 1 640  CYS 640  638  638  CYS CYS B . n 
B 1 641  LEU 641  639  639  LEU LEU B . n 
B 1 642  ASP 642  640  640  ASP ASP B . n 
B 1 643  ARG 643  641  641  ARG ARG B . n 
B 1 644  ALA 644  642  642  ALA ALA B . n 
B 1 645  ALA 645  643  643  ALA ALA B . n 
B 1 646  GLU 646  644  644  GLU GLU B . n 
B 1 647  LEU 647  645  645  LEU LEU B . n 
B 1 648  MET 648  646  646  MET MET B . n 
B 1 649  GLN 649  647  647  GLN GLN B . n 
B 1 650  ALA 650  648  648  ALA ALA B . n 
B 1 651  ARG 651  649  649  ARG ARG B . n 
B 1 652  MET 652  650  650  MET MET B . n 
B 1 653  PRO 653  651  651  PRO PRO B . n 
B 1 654  THR 654  652  652  THR THR B . n 
B 1 655  LEU 655  653  653  LEU LEU B . n 
B 1 656  LEU 656  654  654  LEU LEU B . n 
B 1 657  GLY 657  655  655  GLY GLY B . n 
B 1 658  LEU 658  656  656  LEU LEU B . n 
B 1 659  ILE 659  657  657  ILE ILE B . n 
B 1 660  ILE 660  658  658  ILE ILE B . n 
B 1 661  ARG 661  659  659  ARG ARG B . n 
B 1 662  GLU 662  660  660  GLU GLU B . n 
B 1 663  ALA 663  661  661  ALA ALA B . n 
B 1 664  GLY 664  662  662  GLY GLY B . n 
B 1 665  LYS 665  663  663  LYS LYS B . n 
B 1 666  SER 666  664  664  SER SER B . n 
B 1 667  ALA 667  665  665  ALA ALA B . n 
B 1 668  LEU 668  666  666  LEU LEU B . n 
B 1 669  ASN 669  667  667  ASN ASN B . n 
B 1 670  ALA 670  668  668  ALA ALA B . n 
B 1 671  ILE 671  669  669  ILE ILE B . n 
B 1 672  ALA 672  670  670  ALA ALA B . n 
B 1 673  GLU 673  671  671  GLU GLU B . n 
B 1 674  VAL 674  672  672  VAL VAL B . n 
B 1 675  ARG 675  673  673  ARG ARG B . n 
B 1 676  GLU 676  674  674  GLU GLU B . n 
B 1 677  ALA 677  675  675  ALA ALA B . n 
B 1 678  ILE 678  676  676  ILE ILE B . n 
B 1 679  ASP 679  677  677  ASP ASP B . n 
B 1 680  PHE 680  678  678  PHE PHE B . n 
B 1 681  LEU 681  679  679  LEU LEU B . n 
B 1 682  ARG 682  680  680  ARG ARG B . n 
B 1 683  TYR 683  681  681  TYR TYR B . n 
B 1 684  TYR 684  682  682  TYR TYR B . n 
B 1 685  ALA 685  683  683  ALA ALA B . n 
B 1 686  GLU 686  684  684  GLU GLU B . n 
B 1 687  GLN 687  685  685  GLN GLN B . n 
B 1 688  THR 688  686  686  THR THR B . n 
B 1 689  ARG 689  687  687  ARG ARG B . n 
B 1 690  ARG 690  688  688  ARG ARG B . n 
B 1 691  THR 691  689  689  THR THR B . n 
B 1 692  LEU 692  690  690  LEU LEU B . n 
B 1 693  GLY 693  691  691  GLY GLY B . n 
B 1 694  PRO 694  692  692  PRO PRO B . n 
B 1 695  GLY 695  693  693  GLY GLY B . n 
B 1 696  HIS 696  694  694  HIS HIS B . n 
B 1 697  GLY 697  695  695  GLY GLY B . n 
B 1 698  PRO 698  696  696  PRO PRO B . n 
B 1 699  LEU 699  697  697  LEU LEU B . n 
B 1 700  GLY 700  698  698  GLY GLY B . n 
B 1 701  PRO 701  699  699  PRO PRO B . n 
B 1 702  ILE 702  700  700  ILE ILE B . n 
B 1 703  VAL 703  701  701  VAL VAL B . n 
B 1 704  CYS 704  702  702  CYS CYS B . n 
B 1 705  ILE 705  703  703  ILE ILE B . n 
B 1 706  SER 706  704  704  SER SER B . n 
B 1 707  PRO 707  705  705  PRO PRO B . n 
B 1 708  TRP 708  706  706  TRP TRP B . n 
B 1 709  ASN 709  707  707  ASN ASN B . n 
B 1 710  PHE 710  708  708  PHE PHE B . n 
B 1 711  PRO 711  709  709  PRO PRO B . n 
B 1 712  LEU 712  710  710  LEU LEU B . n 
B 1 713  ALA 713  711  711  ALA ALA B . n 
B 1 714  ILE 714  712  712  ILE ILE B . n 
B 1 715  PHE 715  713  713  PHE PHE B . n 
B 1 716  THR 716  714  714  THR THR B . n 
B 1 717  GLY 717  715  715  GLY GLY B . n 
B 1 718  GLN 718  716  716  GLN GLN B . n 
B 1 719  ILE 719  717  717  ILE ILE B . n 
B 1 720  ALA 720  718  718  ALA ALA B . n 
B 1 721  ALA 721  719  719  ALA ALA B . n 
B 1 722  ALA 722  720  720  ALA ALA B . n 
B 1 723  LEU 723  721  721  LEU LEU B . n 
B 1 724  VAL 724  722  722  VAL VAL B . n 
B 1 725  ALA 725  723  723  ALA ALA B . n 
B 1 726  GLY 726  724  724  GLY GLY B . n 
B 1 727  ASN 727  725  725  ASN ASN B . n 
B 1 728  PRO 728  726  726  PRO PRO B . n 
B 1 729  VAL 729  727  727  VAL VAL B . n 
B 1 730  LEU 730  728  728  LEU LEU B . n 
B 1 731  ALA 731  729  729  ALA ALA B . n 
B 1 732  LYS 732  730  730  LYS LYS B . n 
B 1 733  PRO 733  731  731  PRO PRO B . n 
B 1 734  ALA 734  732  732  ALA ALA B . n 
B 1 735  GLU 735  733  733  GLU GLU B . n 
B 1 736  GLU 736  734  734  GLU GLU B . n 
B 1 737  THR 737  735  735  THR THR B . n 
B 1 738  PRO 738  736  736  PRO PRO B . n 
B 1 739  LEU 739  737  737  LEU LEU B . n 
B 1 740  ILE 740  738  738  ILE ILE B . n 
B 1 741  ALA 741  739  739  ALA ALA B . n 
B 1 742  ALA 742  740  740  ALA ALA B . n 
B 1 743  GLU 743  741  741  GLU GLU B . n 
B 1 744  GLY 744  742  742  GLY GLY B . n 
B 1 745  VAL 745  743  743  VAL VAL B . n 
B 1 746  ARG 746  744  744  ARG ARG B . n 
B 1 747  ILE 747  745  745  ILE ILE B . n 
B 1 748  LEU 748  746  746  LEU LEU B . n 
B 1 749  ARG 749  747  747  ARG ARG B . n 
B 1 750  GLU 750  748  748  GLU GLU B . n 
B 1 751  ALA 751  749  749  ALA ALA B . n 
B 1 752  GLY 752  750  750  GLY GLY B . n 
B 1 753  ILE 753  751  751  ILE ILE B . n 
B 1 754  PRO 754  752  752  PRO PRO B . n 
B 1 755  ALA 755  753  753  ALA ALA B . n 
B 1 756  SER 756  754  754  SER SER B . n 
B 1 757  ALA 757  755  755  ALA ALA B . n 
B 1 758  LEU 758  756  756  LEU LEU B . n 
B 1 759  GLN 759  757  757  GLN GLN B . n 
B 1 760  LEU 760  758  758  LEU LEU B . n 
B 1 761  LEU 761  759  759  LEU LEU B . n 
B 1 762  PRO 762  760  760  PRO PRO B . n 
B 1 763  GLY 763  761  761  GLY GLY B . n 
B 1 764  ASP 764  762  762  ASP ASP B . n 
B 1 765  GLY 765  763  763  GLY GLY B . n 
B 1 766  ARG 766  764  764  ARG ARG B . n 
B 1 767  VAL 767  765  765  VAL VAL B . n 
B 1 768  GLY 768  766  766  GLY GLY B . n 
B 1 769  ALA 769  767  767  ALA ALA B . n 
B 1 770  ALA 770  768  768  ALA ALA B . n 
B 1 771  LEU 771  769  769  LEU LEU B . n 
B 1 772  VAL 772  770  770  VAL VAL B . n 
B 1 773  ALA 773  771  771  ALA ALA B . n 
B 1 774  ALA 774  772  772  ALA ALA B . n 
B 1 775  ALA 775  773  773  ALA ALA B . n 
B 1 776  GLU 776  774  774  GLU GLU B . n 
B 1 777  THR 777  775  775  THR THR B . n 
B 1 778  ALA 778  776  776  ALA ALA B . n 
B 1 779  GLY 779  777  777  GLY GLY B . n 
B 1 780  VAL 780  778  778  VAL VAL B . n 
B 1 781  MET 781  779  779  MET MET B . n 
B 1 782  PHE 782  780  780  PHE PHE B . n 
B 1 783  THR 783  781  781  THR THR B . n 
B 1 784  GLY 784  782  782  GLY GLY B . n 
B 1 785  SER 785  783  783  SER SER B . n 
B 1 786  THR 786  784  784  THR THR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  VAL 788  786  786  VAL VAL B . n 
B 1 789  ALA 789  787  787  ALA ALA B . n 
B 1 790  ARG 790  788  788  ARG ARG B . n 
B 1 791  LEU 791  789  789  LEU LEU B . n 
B 1 792  ILE 792  790  790  ILE ILE B . n 
B 1 793  GLN 793  791  791  GLN GLN B . n 
B 1 794  ALA 794  792  792  ALA ALA B . n 
B 1 795  GLN 795  793  793  GLN GLN B . n 
B 1 796  LEU 796  794  794  LEU LEU B . n 
B 1 797  ALA 797  795  795  ALA ALA B . n 
B 1 798  ASP 798  796  796  ASP ASP B . n 
B 1 799  ARG 799  797  797  ARG ARG B . n 
B 1 800  LEU 800  798  798  LEU LEU B . n 
B 1 801  SER 801  799  799  SER SER B . n 
B 1 802  PRO 802  800  800  PRO PRO B . n 
B 1 803  ALA 803  801  801  ALA ALA B . n 
B 1 804  GLY 804  802  802  GLY GLY B . n 
B 1 805  ARG 805  803  803  ARG ARG B . n 
B 1 806  PRO 806  804  804  PRO PRO B . n 
B 1 807  ILE 807  805  805  ILE ILE B . n 
B 1 808  PRO 808  806  806  PRO PRO B . n 
B 1 809  LEU 809  807  807  LEU LEU B . n 
B 1 810  ILE 810  808  808  ILE ILE B . n 
B 1 811  ALA 811  809  809  ALA ALA B . n 
B 1 812  GLU 812  810  810  GLU GLU B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  GLY 814  812  812  GLY GLY B . n 
B 1 815  GLY 815  813  813  GLY GLY B . n 
B 1 816  GLN 816  814  814  GLN GLN B . n 
B 1 817  ASN 817  815  815  ASN ASN B . n 
B 1 818  ALA 818  816  816  ALA ALA B . n 
B 1 819  MET 819  817  817  MET MET B . n 
B 1 820  ILE 820  818  818  ILE ILE B . n 
B 1 821  VAL 821  819  819  VAL VAL B . n 
B 1 822  ASP 822  820  820  ASP ASP B . n 
B 1 823  SER 823  821  821  SER SER B . n 
B 1 824  SER 824  822  822  SER SER B . n 
B 1 825  ALA 825  823  823  ALA ALA B . n 
B 1 826  LEU 826  824  824  LEU LEU B . n 
B 1 827  ALA 827  825  825  ALA ALA B . n 
B 1 828  GLU 828  826  826  GLU GLU B . n 
B 1 829  GLN 829  827  827  GLN GLN B . n 
B 1 830  VAL 830  828  828  VAL VAL B . n 
B 1 831  VAL 831  829  829  VAL VAL B . n 
B 1 832  GLY 832  830  830  GLY GLY B . n 
B 1 833  ASP 833  831  831  ASP ASP B . n 
B 1 834  VAL 834  832  832  VAL VAL B . n 
B 1 835  ILE 835  833  833  ILE ILE B . n 
B 1 836  THR 836  834  834  THR THR B . n 
B 1 837  SER 837  835  835  SER SER B . n 
B 1 838  ALA 838  836  836  ALA ALA B . n 
B 1 839  PHE 839  837  837  PHE PHE B . n 
B 1 840  ASP 840  838  838  ASP ASP B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  ALA 842  840  840  ALA ALA B . n 
B 1 843  GLY 843  841  841  GLY GLY B . n 
B 1 844  GLN 844  842  842  GLN GLN B . n 
B 1 845  ARG 845  843  843  ARG ARG B . n 
B 1 846  CYS 846  844  844  CYS CYS B . n 
B 1 847  SER 847  845  845  SER SER B . n 
B 1 848  ALA 848  846  846  ALA ALA B . n 
B 1 849  LEU 849  847  847  LEU LEU B . n 
B 1 850  ARG 850  848  848  ARG ARG B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LEU 852  850  850  LEU LEU B . n 
B 1 853  CYS 853  851  851  CYS CYS B . n 
B 1 854  LEU 854  852  852  LEU LEU B . n 
B 1 855  GLN 855  853  853  GLN GLN B . n 
B 1 856  GLU 856  854  854  GLU GLU B . n 
B 1 857  ASP 857  855  855  ASP ASP B . n 
B 1 858  VAL 858  856  856  VAL VAL B . n 
B 1 859  ALA 859  857  857  ALA ALA B . n 
B 1 860  ASP 860  858  858  ASP ASP B . n 
B 1 861  ARG 861  859  859  ARG ARG B . n 
B 1 862  ILE 862  860  860  ILE ILE B . n 
B 1 863  LEU 863  861  861  LEU LEU B . n 
B 1 864  THR 864  862  862  THR THR B . n 
B 1 865  MET 865  863  863  MET MET B . n 
B 1 866  LEU 866  864  864  LEU LEU B . n 
B 1 867  LYS 867  865  865  LYS LYS B . n 
B 1 868  GLY 868  866  866  GLY GLY B . n 
B 1 869  ALA 869  867  867  ALA ALA B . n 
B 1 870  LEU 870  868  868  LEU LEU B . n 
B 1 871  HIS 871  869  869  HIS HIS B . n 
B 1 872  GLU 872  870  870  GLU GLU B . n 
B 1 873  LEU 873  871  871  LEU LEU B . n 
B 1 874  HIS 874  872  872  HIS HIS B . n 
B 1 875  ILE 875  873  873  ILE ILE B . n 
B 1 876  GLY 876  874  874  GLY GLY B . n 
B 1 877  ARG 877  875  875  ARG ARG B . n 
B 1 878  THR 878  876  876  THR THR B . n 
B 1 879  ASP 879  877  877  ASP ASP B . n 
B 1 880  ARG 880  878  878  ARG ARG B . n 
B 1 881  LEU 881  879  879  LEU LEU B . n 
B 1 882  SER 882  880  880  SER SER B . n 
B 1 883  VAL 883  881  881  VAL VAL B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  VAL 885  883  883  VAL VAL B . n 
B 1 886  GLY 886  884  884  GLY GLY B . n 
B 1 887  PRO 887  885  885  PRO PRO B . n 
B 1 888  VAL 888  886  886  VAL VAL B . n 
B 1 889  ILE 889  887  887  ILE ILE B . n 
B 1 890  THR 890  888  888  THR THR B . n 
B 1 891  SER 891  889  889  SER SER B . n 
B 1 892  GLU 892  890  890  GLU GLU B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  LYS 894  892  892  LYS LYS B . n 
B 1 895  ASP 895  893  893  ASP ASP B . n 
B 1 896  ASN 896  894  894  ASN ASN B . n 
B 1 897  ILE 897  895  895  ILE ILE B . n 
B 1 898  GLU 898  896  896  GLU GLU B . n 
B 1 899  LYS 899  897  897  LYS LYS B . n 
B 1 900  HIS 900  898  898  HIS HIS B . n 
B 1 901  ILE 901  899  899  ILE ILE B . n 
B 1 902  GLU 902  900  900  GLU GLU B . n 
B 1 903  ARG 903  901  901  ARG ARG B . n 
B 1 904  MET 904  902  902  MET MET B . n 
B 1 905  ARG 905  903  903  ARG ARG B . n 
B 1 906  GLY 906  904  904  GLY GLY B . n 
B 1 907  LEU 907  905  905  LEU LEU B . n 
B 1 908  GLY 908  906  906  GLY GLY B . n 
B 1 909  ARG 909  907  907  ARG ARG B . n 
B 1 910  LYS 910  908  908  LYS LYS B . n 
B 1 911  VAL 911  909  909  VAL VAL B . n 
B 1 912  GLU 912  910  910  GLU GLU B . n 
B 1 913  GLN 913  911  911  GLN GLN B . n 
B 1 914  ILE 914  912  912  ILE ILE B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 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 A1BDD ? ? A1BDD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD   ? ? FAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2  FAD   1    2001 2001 FAD   FAD A . 
D  3  A1BDD 1    2002 2002 A1BDD 201 A . 
E  4  PGE   1    2003 2003 PGE   PGE A . 
F  5  FMT   1    2004 2004 FMT   FMT A . 
G  6  PEG   1    2005 2005 PEG   PEG A . 
H  6  PEG   1    2006 2007 PEG   PEG A . 
I  7  NAD   1    2007 2002 NAD   NAD A . 
J  8  SO4   1    2008 2    SO4   SO4 A . 
K  8  SO4   1    2009 3    SO4   SO4 A . 
L  8  SO4   1    2010 4    SO4   SO4 A . 
M  8  SO4   1    2011 5    SO4   SO4 A . 
N  9  MG    1    2012 2    MG    MG  A . 
O  2  FAD   1    2001 2001 FAD   FAD B . 
P  3  A1BDD 1    2002 2002 A1BDD 201 B . 
Q  6  PEG   1    2003 2003 PEG   PEG B . 
R  3  A1BDD 1    2004 2004 A1BDD 201 B . 
S  4  PGE   1    2005 2005 PGE   PGE B . 
T  5  FMT   1    2006 2006 FMT   FMT B . 
U  5  FMT   1    2007 2008 FMT   FMT B . 
V  5  FMT   1    2008 2015 FMT   FMT B . 
W  4  PGE   1    2009 2016 PGE   PGE B . 
X  10 1PE   1    2010 2018 1PE   1PE B . 
Y  7  NAD   1    2011 2002 NAD   NAD B . 
Z  8  SO4   1    2012 1    SO4   SO4 B . 
AA 9  MG    1    2013 1    MG    MG  B . 
BA 11 HOH   1    2101 1598 HOH   HOH A . 
BA 11 HOH   2    2102 634  HOH   HOH A . 
BA 11 HOH   3    2103 2619 HOH   HOH A . 
BA 11 HOH   4    2104 2692 HOH   HOH A . 
BA 11 HOH   5    2105 92   HOH   HOH A . 
BA 11 HOH   6    2106 2043 HOH   HOH A . 
BA 11 HOH   7    2107 938  HOH   HOH A . 
BA 11 HOH   8    2108 2348 HOH   HOH A . 
BA 11 HOH   9    2109 1273 HOH   HOH A . 
BA 11 HOH   10   2110 2328 HOH   HOH A . 
BA 11 HOH   11   2111 2022 HOH   HOH A . 
BA 11 HOH   12   2112 939  HOH   HOH A . 
BA 11 HOH   13   2113 2037 HOH   HOH A . 
BA 11 HOH   14   2114 1947 HOH   HOH A . 
BA 11 HOH   15   2115 2293 HOH   HOH A . 
BA 11 HOH   16   2116 609  HOH   HOH A . 
BA 11 HOH   17   2117 1060 HOH   HOH A . 
BA 11 HOH   18   2118 1615 HOH   HOH A . 
BA 11 HOH   19   2119 38   HOH   HOH A . 
BA 11 HOH   20   2120 2476 HOH   HOH A . 
BA 11 HOH   21   2121 9    HOH   HOH A . 
BA 11 HOH   22   2122 2256 HOH   HOH A . 
BA 11 HOH   23   2123 1683 HOH   HOH A . 
BA 11 HOH   24   2124 2235 HOH   HOH A . 
BA 11 HOH   25   2125 2188 HOH   HOH A . 
BA 11 HOH   26   2126 2057 HOH   HOH A . 
BA 11 HOH   27   2127 1971 HOH   HOH A . 
BA 11 HOH   28   2128 1980 HOH   HOH A . 
BA 11 HOH   29   2129 1989 HOH   HOH A . 
BA 11 HOH   30   2130 899  HOH   HOH A . 
BA 11 HOH   31   2131 1463 HOH   HOH A . 
BA 11 HOH   32   2132 2469 HOH   HOH A . 
BA 11 HOH   33   2133 2104 HOH   HOH A . 
BA 11 HOH   34   2134 1657 HOH   HOH A . 
BA 11 HOH   35   2135 76   HOH   HOH A . 
BA 11 HOH   36   2136 535  HOH   HOH A . 
BA 11 HOH   37   2137 1208 HOH   HOH A . 
BA 11 HOH   38   2138 932  HOH   HOH A . 
BA 11 HOH   39   2139 2369 HOH   HOH A . 
BA 11 HOH   40   2140 659  HOH   HOH A . 
BA 11 HOH   41   2141 652  HOH   HOH A . 
BA 11 HOH   42   2142 1239 HOH   HOH A . 
BA 11 HOH   43   2143 2151 HOH   HOH A . 
BA 11 HOH   44   2144 2067 HOH   HOH A . 
BA 11 HOH   45   2145 1013 HOH   HOH A . 
BA 11 HOH   46   2146 2130 HOH   HOH A . 
BA 11 HOH   47   2147 2016 HOH   HOH A . 
BA 11 HOH   48   2148 2508 HOH   HOH A . 
BA 11 HOH   49   2149 1779 HOH   HOH A . 
BA 11 HOH   50   2150 1812 HOH   HOH A . 
BA 11 HOH   51   2151 2439 HOH   HOH A . 
BA 11 HOH   52   2152 1621 HOH   HOH A . 
BA 11 HOH   53   2153 1055 HOH   HOH A . 
BA 11 HOH   54   2154 1506 HOH   HOH A . 
BA 11 HOH   55   2155 184  HOH   HOH A . 
BA 11 HOH   56   2156 2595 HOH   HOH A . 
BA 11 HOH   57   2157 1469 HOH   HOH A . 
BA 11 HOH   58   2158 2445 HOH   HOH A . 
BA 11 HOH   59   2159 1350 HOH   HOH A . 
BA 11 HOH   60   2160 519  HOH   HOH A . 
BA 11 HOH   61   2161 1027 HOH   HOH A . 
BA 11 HOH   62   2162 2305 HOH   HOH A . 
BA 11 HOH   63   2163 373  HOH   HOH A . 
BA 11 HOH   64   2164 2634 HOH   HOH A . 
BA 11 HOH   65   2165 1280 HOH   HOH A . 
BA 11 HOH   66   2166 1708 HOH   HOH A . 
BA 11 HOH   67   2167 2317 HOH   HOH A . 
BA 11 HOH   68   2168 982  HOH   HOH A . 
BA 11 HOH   69   2169 1323 HOH   HOH A . 
BA 11 HOH   70   2170 2455 HOH   HOH A . 
BA 11 HOH   71   2171 215  HOH   HOH A . 
BA 11 HOH   72   2172 1632 HOH   HOH A . 
BA 11 HOH   73   2173 1841 HOH   HOH A . 
BA 11 HOH   74   2174 110  HOH   HOH A . 
BA 11 HOH   75   2175 694  HOH   HOH A . 
BA 11 HOH   76   2176 2393 HOH   HOH A . 
BA 11 HOH   77   2177 2145 HOH   HOH A . 
BA 11 HOH   78   2178 887  HOH   HOH A . 
BA 11 HOH   79   2179 1656 HOH   HOH A . 
BA 11 HOH   80   2180 466  HOH   HOH A . 
BA 11 HOH   81   2181 1686 HOH   HOH A . 
BA 11 HOH   82   2182 2041 HOH   HOH A . 
BA 11 HOH   83   2183 221  HOH   HOH A . 
BA 11 HOH   84   2184 82   HOH   HOH A . 
BA 11 HOH   85   2185 1529 HOH   HOH A . 
BA 11 HOH   86   2186 1978 HOH   HOH A . 
BA 11 HOH   87   2187 346  HOH   HOH A . 
BA 11 HOH   88   2188 13   HOH   HOH A . 
BA 11 HOH   89   2189 2594 HOH   HOH A . 
BA 11 HOH   90   2190 171  HOH   HOH A . 
BA 11 HOH   91   2191 1767 HOH   HOH A . 
BA 11 HOH   92   2192 389  HOH   HOH A . 
BA 11 HOH   93   2193 1171 HOH   HOH A . 
BA 11 HOH   94   2194 62   HOH   HOH A . 
BA 11 HOH   95   2195 175  HOH   HOH A . 
BA 11 HOH   96   2196 290  HOH   HOH A . 
BA 11 HOH   97   2197 1071 HOH   HOH A . 
BA 11 HOH   98   2198 553  HOH   HOH A . 
BA 11 HOH   99   2199 1609 HOH   HOH A . 
BA 11 HOH   100  2200 54   HOH   HOH A . 
BA 11 HOH   101  2201 1440 HOH   HOH A . 
BA 11 HOH   102  2202 619  HOH   HOH A . 
BA 11 HOH   103  2203 1240 HOH   HOH A . 
BA 11 HOH   104  2204 1120 HOH   HOH A . 
BA 11 HOH   105  2205 2642 HOH   HOH A . 
BA 11 HOH   106  2206 1689 HOH   HOH A . 
BA 11 HOH   107  2207 376  HOH   HOH A . 
BA 11 HOH   108  2208 96   HOH   HOH A . 
BA 11 HOH   109  2209 1965 HOH   HOH A . 
BA 11 HOH   110  2210 739  HOH   HOH A . 
BA 11 HOH   111  2211 2312 HOH   HOH A . 
BA 11 HOH   112  2212 1080 HOH   HOH A . 
BA 11 HOH   113  2213 1301 HOH   HOH A . 
BA 11 HOH   114  2214 2531 HOH   HOH A . 
BA 11 HOH   115  2215 646  HOH   HOH A . 
BA 11 HOH   116  2216 2023 HOH   HOH A . 
BA 11 HOH   117  2217 2694 HOH   HOH A . 
BA 11 HOH   118  2218 670  HOH   HOH A . 
BA 11 HOH   119  2219 1336 HOH   HOH A . 
BA 11 HOH   120  2220 1483 HOH   HOH A . 
BA 11 HOH   121  2221 868  HOH   HOH A . 
BA 11 HOH   122  2222 1033 HOH   HOH A . 
BA 11 HOH   123  2223 339  HOH   HOH A . 
BA 11 HOH   124  2224 1596 HOH   HOH A . 
BA 11 HOH   125  2225 382  HOH   HOH A . 
BA 11 HOH   126  2226 661  HOH   HOH A . 
BA 11 HOH   127  2227 30   HOH   HOH A . 
BA 11 HOH   128  2228 1347 HOH   HOH A . 
BA 11 HOH   129  2229 1810 HOH   HOH A . 
BA 11 HOH   130  2230 1205 HOH   HOH A . 
BA 11 HOH   131  2231 2298 HOH   HOH A . 
BA 11 HOH   132  2232 999  HOH   HOH A . 
BA 11 HOH   133  2233 1764 HOH   HOH A . 
BA 11 HOH   134  2234 852  HOH   HOH A . 
BA 11 HOH   135  2235 429  HOH   HOH A . 
BA 11 HOH   136  2236 80   HOH   HOH A . 
BA 11 HOH   137  2237 898  HOH   HOH A . 
BA 11 HOH   138  2238 440  HOH   HOH A . 
BA 11 HOH   139  2239 724  HOH   HOH A . 
BA 11 HOH   140  2240 479  HOH   HOH A . 
BA 11 HOH   141  2241 1530 HOH   HOH A . 
BA 11 HOH   142  2242 447  HOH   HOH A . 
BA 11 HOH   143  2243 858  HOH   HOH A . 
BA 11 HOH   144  2244 2442 HOH   HOH A . 
BA 11 HOH   145  2245 351  HOH   HOH A . 
BA 11 HOH   146  2246 251  HOH   HOH A . 
BA 11 HOH   147  2247 408  HOH   HOH A . 
BA 11 HOH   148  2248 2100 HOH   HOH A . 
BA 11 HOH   149  2249 345  HOH   HOH A . 
BA 11 HOH   150  2250 1095 HOH   HOH A . 
BA 11 HOH   151  2251 51   HOH   HOH A . 
BA 11 HOH   152  2252 1022 HOH   HOH A . 
BA 11 HOH   153  2253 2217 HOH   HOH A . 
BA 11 HOH   154  2254 437  HOH   HOH A . 
BA 11 HOH   155  2255 236  HOH   HOH A . 
BA 11 HOH   156  2256 384  HOH   HOH A . 
BA 11 HOH   157  2257 1253 HOH   HOH A . 
BA 11 HOH   158  2258 1137 HOH   HOH A . 
BA 11 HOH   159  2259 1106 HOH   HOH A . 
BA 11 HOH   160  2260 1097 HOH   HOH A . 
BA 11 HOH   161  2261 1977 HOH   HOH A . 
BA 11 HOH   162  2262 1600 HOH   HOH A . 
BA 11 HOH   163  2263 762  HOH   HOH A . 
BA 11 HOH   164  2264 195  HOH   HOH A . 
BA 11 HOH   165  2265 1369 HOH   HOH A . 
BA 11 HOH   166  2266 1133 HOH   HOH A . 
BA 11 HOH   167  2267 1634 HOH   HOH A . 
BA 11 HOH   168  2268 2006 HOH   HOH A . 
BA 11 HOH   169  2269 57   HOH   HOH A . 
BA 11 HOH   170  2270 61   HOH   HOH A . 
BA 11 HOH   171  2271 2646 HOH   HOH A . 
BA 11 HOH   172  2272 988  HOH   HOH A . 
BA 11 HOH   173  2273 817  HOH   HOH A . 
BA 11 HOH   174  2274 2443 HOH   HOH A . 
BA 11 HOH   175  2275 53   HOH   HOH A . 
BA 11 HOH   176  2276 696  HOH   HOH A . 
BA 11 HOH   177  2277 2346 HOH   HOH A . 
BA 11 HOH   178  2278 737  HOH   HOH A . 
BA 11 HOH   179  2279 2480 HOH   HOH A . 
BA 11 HOH   180  2280 1182 HOH   HOH A . 
BA 11 HOH   181  2281 848  HOH   HOH A . 
BA 11 HOH   182  2282 1339 HOH   HOH A . 
BA 11 HOH   183  2283 1646 HOH   HOH A . 
BA 11 HOH   184  2284 200  HOH   HOH A . 
BA 11 HOH   185  2285 850  HOH   HOH A . 
BA 11 HOH   186  2286 2268 HOH   HOH A . 
BA 11 HOH   187  2287 1718 HOH   HOH A . 
BA 11 HOH   188  2288 1473 HOH   HOH A . 
BA 11 HOH   189  2289 1411 HOH   HOH A . 
BA 11 HOH   190  2290 462  HOH   HOH A . 
BA 11 HOH   191  2291 1545 HOH   HOH A . 
BA 11 HOH   192  2292 1118 HOH   HOH A . 
BA 11 HOH   193  2293 585  HOH   HOH A . 
BA 11 HOH   194  2294 1164 HOH   HOH A . 
BA 11 HOH   195  2295 308  HOH   HOH A . 
BA 11 HOH   196  2296 1188 HOH   HOH A . 
BA 11 HOH   197  2297 126  HOH   HOH A . 
BA 11 HOH   198  2298 525  HOH   HOH A . 
BA 11 HOH   199  2299 511  HOH   HOH A . 
BA 11 HOH   200  2300 630  HOH   HOH A . 
BA 11 HOH   201  2301 1979 HOH   HOH A . 
BA 11 HOH   202  2302 821  HOH   HOH A . 
BA 11 HOH   203  2303 931  HOH   HOH A . 
BA 11 HOH   204  2304 706  HOH   HOH A . 
BA 11 HOH   205  2305 79   HOH   HOH A . 
BA 11 HOH   206  2306 601  HOH   HOH A . 
BA 11 HOH   207  2307 1216 HOH   HOH A . 
BA 11 HOH   208  2308 540  HOH   HOH A . 
BA 11 HOH   209  2309 1163 HOH   HOH A . 
BA 11 HOH   210  2310 1467 HOH   HOH A . 
BA 11 HOH   211  2311 1805 HOH   HOH A . 
BA 11 HOH   212  2312 60   HOH   HOH A . 
BA 11 HOH   213  2313 2008 HOH   HOH A . 
BA 11 HOH   214  2314 69   HOH   HOH A . 
BA 11 HOH   215  2315 976  HOH   HOH A . 
BA 11 HOH   216  2316 837  HOH   HOH A . 
BA 11 HOH   217  2317 679  HOH   HOH A . 
BA 11 HOH   218  2318 2628 HOH   HOH A . 
BA 11 HOH   219  2319 185  HOH   HOH A . 
BA 11 HOH   220  2320 143  HOH   HOH A . 
BA 11 HOH   221  2321 1691 HOH   HOH A . 
BA 11 HOH   222  2322 864  HOH   HOH A . 
BA 11 HOH   223  2323 201  HOH   HOH A . 
BA 11 HOH   224  2324 2518 HOH   HOH A . 
BA 11 HOH   225  2325 825  HOH   HOH A . 
BA 11 HOH   226  2326 2120 HOH   HOH A . 
BA 11 HOH   227  2327 561  HOH   HOH A . 
BA 11 HOH   228  2328 1745 HOH   HOH A . 
BA 11 HOH   229  2329 965  HOH   HOH A . 
BA 11 HOH   230  2330 2132 HOH   HOH A . 
BA 11 HOH   231  2331 318  HOH   HOH A . 
BA 11 HOH   232  2332 402  HOH   HOH A . 
BA 11 HOH   233  2333 1068 HOH   HOH A . 
BA 11 HOH   234  2334 18   HOH   HOH A . 
BA 11 HOH   235  2335 399  HOH   HOH A . 
BA 11 HOH   236  2336 1025 HOH   HOH A . 
BA 11 HOH   237  2337 2547 HOH   HOH A . 
BA 11 HOH   238  2338 1442 HOH   HOH A . 
BA 11 HOH   239  2339 1518 HOH   HOH A . 
BA 11 HOH   240  2340 1639 HOH   HOH A . 
BA 11 HOH   241  2341 20   HOH   HOH A . 
BA 11 HOH   242  2342 2495 HOH   HOH A . 
BA 11 HOH   243  2343 2481 HOH   HOH A . 
BA 11 HOH   244  2344 248  HOH   HOH A . 
BA 11 HOH   245  2345 715  HOH   HOH A . 
BA 11 HOH   246  2346 1050 HOH   HOH A . 
BA 11 HOH   247  2347 681  HOH   HOH A . 
BA 11 HOH   248  2348 102  HOH   HOH A . 
BA 11 HOH   249  2349 210  HOH   HOH A . 
BA 11 HOH   250  2350 324  HOH   HOH A . 
BA 11 HOH   251  2351 395  HOH   HOH A . 
BA 11 HOH   252  2352 264  HOH   HOH A . 
BA 11 HOH   253  2353 2038 HOH   HOH A . 
BA 11 HOH   254  2354 2498 HOH   HOH A . 
BA 11 HOH   255  2355 231  HOH   HOH A . 
BA 11 HOH   256  2356 1334 HOH   HOH A . 
BA 11 HOH   257  2357 2092 HOH   HOH A . 
BA 11 HOH   258  2358 1026 HOH   HOH A . 
BA 11 HOH   259  2359 1754 HOH   HOH A . 
BA 11 HOH   260  2360 1941 HOH   HOH A . 
BA 11 HOH   261  2361 432  HOH   HOH A . 
BA 11 HOH   262  2362 412  HOH   HOH A . 
BA 11 HOH   263  2363 576  HOH   HOH A . 
BA 11 HOH   264  2364 669  HOH   HOH A . 
BA 11 HOH   265  2365 178  HOH   HOH A . 
BA 11 HOH   266  2366 2364 HOH   HOH A . 
BA 11 HOH   267  2367 1705 HOH   HOH A . 
BA 11 HOH   268  2368 1729 HOH   HOH A . 
BA 11 HOH   269  2369 2351 HOH   HOH A . 
BA 11 HOH   270  2370 1130 HOH   HOH A . 
BA 11 HOH   271  2371 446  HOH   HOH A . 
BA 11 HOH   272  2372 77   HOH   HOH A . 
BA 11 HOH   273  2373 814  HOH   HOH A . 
BA 11 HOH   274  2374 1010 HOH   HOH A . 
BA 11 HOH   275  2375 862  HOH   HOH A . 
BA 11 HOH   276  2376 979  HOH   HOH A . 
BA 11 HOH   277  2377 1093 HOH   HOH A . 
BA 11 HOH   278  2378 169  HOH   HOH A . 
BA 11 HOH   279  2379 1061 HOH   HOH A . 
BA 11 HOH   280  2380 1734 HOH   HOH A . 
BA 11 HOH   281  2381 1831 HOH   HOH A . 
BA 11 HOH   282  2382 731  HOH   HOH A . 
BA 11 HOH   283  2383 419  HOH   HOH A . 
BA 11 HOH   284  2384 572  HOH   HOH A . 
BA 11 HOH   285  2385 937  HOH   HOH A . 
BA 11 HOH   286  2386 1676 HOH   HOH A . 
BA 11 HOH   287  2387 2171 HOH   HOH A . 
BA 11 HOH   288  2388 1521 HOH   HOH A . 
BA 11 HOH   289  2389 1976 HOH   HOH A . 
BA 11 HOH   290  2390 2500 HOH   HOH A . 
BA 11 HOH   291  2391 1716 HOH   HOH A . 
BA 11 HOH   292  2392 1263 HOH   HOH A . 
BA 11 HOH   293  2393 205  HOH   HOH A . 
BA 11 HOH   294  2394 2337 HOH   HOH A . 
BA 11 HOH   295  2395 1348 HOH   HOH A . 
BA 11 HOH   296  2396 888  HOH   HOH A . 
BA 11 HOH   297  2397 816  HOH   HOH A . 
BA 11 HOH   298  2398 952  HOH   HOH A . 
BA 11 HOH   299  2399 192  HOH   HOH A . 
BA 11 HOH   300  2400 766  HOH   HOH A . 
BA 11 HOH   301  2401 465  HOH   HOH A . 
BA 11 HOH   302  2402 1238 HOH   HOH A . 
BA 11 HOH   303  2403 97   HOH   HOH A . 
BA 11 HOH   304  2404 705  HOH   HOH A . 
BA 11 HOH   305  2405 2042 HOH   HOH A . 
BA 11 HOH   306  2406 1275 HOH   HOH A . 
BA 11 HOH   307  2407 198  HOH   HOH A . 
BA 11 HOH   308  2408 180  HOH   HOH A . 
BA 11 HOH   309  2409 1479 HOH   HOH A . 
BA 11 HOH   310  2410 2158 HOH   HOH A . 
BA 11 HOH   311  2411 812  HOH   HOH A . 
BA 11 HOH   312  2412 1186 HOH   HOH A . 
BA 11 HOH   313  2413 558  HOH   HOH A . 
BA 11 HOH   314  2414 121  HOH   HOH A . 
BA 11 HOH   315  2415 2247 HOH   HOH A . 
BA 11 HOH   316  2416 1551 HOH   HOH A . 
BA 11 HOH   317  2417 2517 HOH   HOH A . 
BA 11 HOH   318  2418 1782 HOH   HOH A . 
BA 11 HOH   319  2419 612  HOH   HOH A . 
BA 11 HOH   320  2420 2165 HOH   HOH A . 
BA 11 HOH   321  2421 702  HOH   HOH A . 
BA 11 HOH   322  2422 1715 HOH   HOH A . 
BA 11 HOH   323  2423 393  HOH   HOH A . 
BA 11 HOH   324  2424 2665 HOH   HOH A . 
BA 11 HOH   325  2425 1418 HOH   HOH A . 
BA 11 HOH   326  2426 294  HOH   HOH A . 
BA 11 HOH   327  2427 901  HOH   HOH A . 
BA 11 HOH   328  2428 2726 HOH   HOH A . 
BA 11 HOH   329  2429 946  HOH   HOH A . 
BA 11 HOH   330  2430 142  HOH   HOH A . 
BA 11 HOH   331  2431 220  HOH   HOH A . 
BA 11 HOH   332  2432 843  HOH   HOH A . 
BA 11 HOH   333  2433 1181 HOH   HOH A . 
BA 11 HOH   334  2434 377  HOH   HOH A . 
BA 11 HOH   335  2435 76   HOH   HOH A . 
BA 11 HOH   336  2436 581  HOH   HOH A . 
BA 11 HOH   337  2437 849  HOH   HOH A . 
BA 11 HOH   338  2438 1842 HOH   HOH A . 
BA 11 HOH   339  2439 115  HOH   HOH A . 
BA 11 HOH   340  2440 348  HOH   HOH A . 
BA 11 HOH   341  2441 1383 HOH   HOH A . 
BA 11 HOH   342  2442 611  HOH   HOH A . 
BA 11 HOH   343  2443 273  HOH   HOH A . 
BA 11 HOH   344  2444 161  HOH   HOH A . 
BA 11 HOH   345  2445 33   HOH   HOH A . 
BA 11 HOH   346  2446 1889 HOH   HOH A . 
BA 11 HOH   347  2447 1698 HOH   HOH A . 
BA 11 HOH   348  2448 88   HOH   HOH A . 
BA 11 HOH   349  2449 1752 HOH   HOH A . 
BA 11 HOH   350  2450 89   HOH   HOH A . 
BA 11 HOH   351  2451 2248 HOH   HOH A . 
BA 11 HOH   352  2452 826  HOH   HOH A . 
BA 11 HOH   353  2453 714  HOH   HOH A . 
BA 11 HOH   354  2454 2549 HOH   HOH A . 
BA 11 HOH   355  2455 295  HOH   HOH A . 
BA 11 HOH   356  2456 268  HOH   HOH A . 
BA 11 HOH   357  2457 240  HOH   HOH A . 
BA 11 HOH   358  2458 407  HOH   HOH A . 
BA 11 HOH   359  2459 306  HOH   HOH A . 
BA 11 HOH   360  2460 304  HOH   HOH A . 
BA 11 HOH   361  2461 307  HOH   HOH A . 
BA 11 HOH   362  2462 1827 HOH   HOH A . 
BA 11 HOH   363  2463 1167 HOH   HOH A . 
BA 11 HOH   364  2464 1490 HOH   HOH A . 
BA 11 HOH   365  2465 2724 HOH   HOH A . 
BA 11 HOH   366  2466 1028 HOH   HOH A . 
BA 11 HOH   367  2467 1748 HOH   HOH A . 
BA 11 HOH   368  2468 1014 HOH   HOH A . 
BA 11 HOH   369  2469 450  HOH   HOH A . 
BA 11 HOH   370  2470 891  HOH   HOH A . 
BA 11 HOH   371  2471 1370 HOH   HOH A . 
BA 11 HOH   372  2472 1502 HOH   HOH A . 
BA 11 HOH   373  2473 657  HOH   HOH A . 
BA 11 HOH   374  2474 315  HOH   HOH A . 
BA 11 HOH   375  2475 917  HOH   HOH A . 
BA 11 HOH   376  2476 639  HOH   HOH A . 
BA 11 HOH   377  2477 238  HOH   HOH A . 
BA 11 HOH   378  2478 99   HOH   HOH A . 
BA 11 HOH   379  2479 262  HOH   HOH A . 
BA 11 HOH   380  2480 2473 HOH   HOH A . 
BA 11 HOH   381  2481 38   HOH   HOH A . 
BA 11 HOH   382  2482 50   HOH   HOH A . 
BA 11 HOH   383  2483 578  HOH   HOH A . 
BA 11 HOH   384  2484 1065 HOH   HOH A . 
BA 11 HOH   385  2485 2175 HOH   HOH A . 
BA 11 HOH   386  2486 785  HOH   HOH A . 
BA 11 HOH   387  2487 239  HOH   HOH A . 
BA 11 HOH   388  2488 309  HOH   HOH A . 
BA 11 HOH   389  2489 881  HOH   HOH A . 
BA 11 HOH   390  2490 2314 HOH   HOH A . 
BA 11 HOH   391  2491 445  HOH   HOH A . 
BA 11 HOH   392  2492 83   HOH   HOH A . 
BA 11 HOH   393  2493 173  HOH   HOH A . 
BA 11 HOH   394  2494 2097 HOH   HOH A . 
BA 11 HOH   395  2495 134  HOH   HOH A . 
BA 11 HOH   396  2496 840  HOH   HOH A . 
BA 11 HOH   397  2497 607  HOH   HOH A . 
BA 11 HOH   398  2498 322  HOH   HOH A . 
BA 11 HOH   399  2499 314  HOH   HOH A . 
BA 11 HOH   400  2500 689  HOH   HOH A . 
BA 11 HOH   401  2501 42   HOH   HOH A . 
BA 11 HOH   402  2502 604  HOH   HOH A . 
BA 11 HOH   403  2503 326  HOH   HOH A . 
BA 11 HOH   404  2504 1378 HOH   HOH A . 
BA 11 HOH   405  2505 473  HOH   HOH A . 
BA 11 HOH   406  2506 421  HOH   HOH A . 
BA 11 HOH   407  2507 2224 HOH   HOH A . 
BA 11 HOH   408  2508 1995 HOH   HOH A . 
BA 11 HOH   409  2509 78   HOH   HOH A . 
BA 11 HOH   410  2510 1338 HOH   HOH A . 
BA 11 HOH   411  2511 417  HOH   HOH A . 
BA 11 HOH   412  2512 2338 HOH   HOH A . 
BA 11 HOH   413  2513 708  HOH   HOH A . 
BA 11 HOH   414  2514 438  HOH   HOH A . 
BA 11 HOH   415  2515 2213 HOH   HOH A . 
BA 11 HOH   416  2516 1672 HOH   HOH A . 
BA 11 HOH   417  2517 1034 HOH   HOH A . 
BA 11 HOH   418  2518 2602 HOH   HOH A . 
BA 11 HOH   419  2519 22   HOH   HOH A . 
BA 11 HOH   420  2520 453  HOH   HOH A . 
BA 11 HOH   421  2521 2144 HOH   HOH A . 
BA 11 HOH   422  2522 451  HOH   HOH A . 
BA 11 HOH   423  2523 379  HOH   HOH A . 
BA 11 HOH   424  2524 131  HOH   HOH A . 
BA 11 HOH   425  2525 622  HOH   HOH A . 
BA 11 HOH   426  2526 606  HOH   HOH A . 
BA 11 HOH   427  2527 730  HOH   HOH A . 
BA 11 HOH   428  2528 796  HOH   HOH A . 
BA 11 HOH   429  2529 2143 HOH   HOH A . 
BA 11 HOH   430  2530 37   HOH   HOH A . 
BA 11 HOH   431  2531 485  HOH   HOH A . 
BA 11 HOH   432  2532 2448 HOH   HOH A . 
BA 11 HOH   433  2533 2353 HOH   HOH A . 
BA 11 HOH   434  2534 645  HOH   HOH A . 
BA 11 HOH   435  2535 618  HOH   HOH A . 
BA 11 HOH   436  2536 44   HOH   HOH A . 
BA 11 HOH   437  2537 1929 HOH   HOH A . 
BA 11 HOH   438  2538 624  HOH   HOH A . 
BA 11 HOH   439  2539 1685 HOH   HOH A . 
BA 11 HOH   440  2540 2635 HOH   HOH A . 
BA 11 HOH   441  2541 789  HOH   HOH A . 
BA 11 HOH   442  2542 1838 HOH   HOH A . 
BA 11 HOH   443  2543 1712 HOH   HOH A . 
BA 11 HOH   444  2544 486  HOH   HOH A . 
BA 11 HOH   445  2545 2154 HOH   HOH A . 
BA 11 HOH   446  2546 259  HOH   HOH A . 
BA 11 HOH   447  2547 1868 HOH   HOH A . 
BA 11 HOH   448  2548 597  HOH   HOH A . 
BA 11 HOH   449  2549 795  HOH   HOH A . 
BA 11 HOH   450  2550 808  HOH   HOH A . 
BA 11 HOH   451  2551 418  HOH   HOH A . 
BA 11 HOH   452  2552 1553 HOH   HOH A . 
BA 11 HOH   453  2553 926  HOH   HOH A . 
BA 11 HOH   454  2554 2591 HOH   HOH A . 
BA 11 HOH   455  2555 1637 HOH   HOH A . 
BA 11 HOH   456  2556 806  HOH   HOH A . 
BA 11 HOH   457  2557 2096 HOH   HOH A . 
BA 11 HOH   458  2558 549  HOH   HOH A . 
BA 11 HOH   459  2559 876  HOH   HOH A . 
BA 11 HOH   460  2560 241  HOH   HOH A . 
BA 11 HOH   461  2561 1784 HOH   HOH A . 
BA 11 HOH   462  2562 1038 HOH   HOH A . 
BA 11 HOH   463  2563 1059 HOH   HOH A . 
BA 11 HOH   464  2564 782  HOH   HOH A . 
BA 11 HOH   465  2565 559  HOH   HOH A . 
BA 11 HOH   466  2566 337  HOH   HOH A . 
BA 11 HOH   467  2567 1001 HOH   HOH A . 
BA 11 HOH   468  2568 2125 HOH   HOH A . 
BA 11 HOH   469  2569 2566 HOH   HOH A . 
BA 11 HOH   470  2570 456  HOH   HOH A . 
BA 11 HOH   471  2571 2360 HOH   HOH A . 
BA 11 HOH   472  2572 332  HOH   HOH A . 
BA 11 HOH   473  2573 2597 HOH   HOH A . 
BA 11 HOH   474  2574 277  HOH   HOH A . 
BA 11 HOH   475  2575 764  HOH   HOH A . 
BA 11 HOH   476  2576 717  HOH   HOH A . 
BA 11 HOH   477  2577 1679 HOH   HOH A . 
BA 11 HOH   478  2578 587  HOH   HOH A . 
BA 11 HOH   479  2579 1377 HOH   HOH A . 
BA 11 HOH   480  2580 2289 HOH   HOH A . 
BA 11 HOH   481  2581 222  HOH   HOH A . 
BA 11 HOH   482  2582 64   HOH   HOH A . 
BA 11 HOH   483  2583 510  HOH   HOH A . 
BA 11 HOH   484  2584 528  HOH   HOH A . 
BA 11 HOH   485  2585 1156 HOH   HOH A . 
BA 11 HOH   486  2586 1858 HOH   HOH A . 
BA 11 HOH   487  2587 75   HOH   HOH A . 
BA 11 HOH   488  2588 49   HOH   HOH A . 
BA 11 HOH   489  2589 577  HOH   HOH A . 
BA 11 HOH   490  2590 1514 HOH   HOH A . 
BA 11 HOH   491  2591 2627 HOH   HOH A . 
BA 11 HOH   492  2592 176  HOH   HOH A . 
BA 11 HOH   493  2593 747  HOH   HOH A . 
BA 11 HOH   494  2594 1057 HOH   HOH A . 
BA 11 HOH   495  2595 321  HOH   HOH A . 
BA 11 HOH   496  2596 1278 HOH   HOH A . 
BA 11 HOH   497  2597 1459 HOH   HOH A . 
BA 11 HOH   498  2598 595  HOH   HOH A . 
BA 11 HOH   499  2599 1183 HOH   HOH A . 
BA 11 HOH   500  2600 266  HOH   HOH A . 
BA 11 HOH   501  2601 1773 HOH   HOH A . 
BA 11 HOH   502  2602 1158 HOH   HOH A . 
BA 11 HOH   503  2603 642  HOH   HOH A . 
BA 11 HOH   504  2604 654  HOH   HOH A . 
BA 11 HOH   505  2605 227  HOH   HOH A . 
BA 11 HOH   506  2606 360  HOH   HOH A . 
BA 11 HOH   507  2607 425  HOH   HOH A . 
BA 11 HOH   508  2608 1875 HOH   HOH A . 
BA 11 HOH   509  2609 527  HOH   HOH A . 
BA 11 HOH   510  2610 1159 HOH   HOH A . 
BA 11 HOH   511  2611 127  HOH   HOH A . 
BA 11 HOH   512  2612 289  HOH   HOH A . 
BA 11 HOH   513  2613 285  HOH   HOH A . 
BA 11 HOH   514  2614 1196 HOH   HOH A . 
BA 11 HOH   515  2615 39   HOH   HOH A . 
BA 11 HOH   516  2616 2546 HOH   HOH A . 
BA 11 HOH   517  2617 1236 HOH   HOH A . 
BA 11 HOH   518  2618 2090 HOH   HOH A . 
BA 11 HOH   519  2619 356  HOH   HOH A . 
BA 11 HOH   520  2620 93   HOH   HOH A . 
BA 11 HOH   521  2621 732  HOH   HOH A . 
BA 11 HOH   522  2622 1346 HOH   HOH A . 
BA 11 HOH   523  2623 2304 HOH   HOH A . 
BA 11 HOH   524  2624 1175 HOH   HOH A . 
BA 11 HOH   525  2625 1399 HOH   HOH A . 
BA 11 HOH   526  2626 1441 HOH   HOH A . 
BA 11 HOH   527  2627 1713 HOH   HOH A . 
BA 11 HOH   528  2628 1642 HOH   HOH A . 
BA 11 HOH   529  2629 442  HOH   HOH A . 
BA 11 HOH   530  2630 392  HOH   HOH A . 
BA 11 HOH   531  2631 2691 HOH   HOH A . 
BA 11 HOH   532  2632 2253 HOH   HOH A . 
BA 11 HOH   533  2633 343  HOH   HOH A . 
BA 11 HOH   534  2634 2278 HOH   HOH A . 
BA 11 HOH   535  2635 741  HOH   HOH A . 
BA 11 HOH   536  2636 1031 HOH   HOH A . 
BA 11 HOH   537  2637 1324 HOH   HOH A . 
BA 11 HOH   538  2638 874  HOH   HOH A . 
BA 11 HOH   539  2639 1561 HOH   HOH A . 
BA 11 HOH   540  2640 2058 HOH   HOH A . 
BA 11 HOH   541  2641 772  HOH   HOH A . 
BA 11 HOH   542  2642 1154 HOH   HOH A . 
BA 11 HOH   543  2643 996  HOH   HOH A . 
BA 11 HOH   544  2644 2010 HOH   HOH A . 
BA 11 HOH   545  2645 336  HOH   HOH A . 
BA 11 HOH   546  2646 320  HOH   HOH A . 
BA 11 HOH   547  2647 2447 HOH   HOH A . 
BA 11 HOH   548  2648 40   HOH   HOH A . 
BA 11 HOH   549  2649 233  HOH   HOH A . 
BA 11 HOH   550  2650 592  HOH   HOH A . 
BA 11 HOH   551  2651 605  HOH   HOH A . 
BA 11 HOH   552  2652 2288 HOH   HOH A . 
BA 11 HOH   553  2653 797  HOH   HOH A . 
BA 11 HOH   554  2654 836  HOH   HOH A . 
BA 11 HOH   555  2655 331  HOH   HOH A . 
BA 11 HOH   556  2656 502  HOH   HOH A . 
BA 11 HOH   557  2657 352  HOH   HOH A . 
BA 11 HOH   558  2658 494  HOH   HOH A . 
BA 11 HOH   559  2659 2365 HOH   HOH A . 
BA 11 HOH   560  2660 650  HOH   HOH A . 
BA 11 HOH   561  2661 2218 HOH   HOH A . 
BA 11 HOH   562  2662 1802 HOH   HOH A . 
BA 11 HOH   563  2663 815  HOH   HOH A . 
BA 11 HOH   564  2664 798  HOH   HOH A . 
BA 11 HOH   565  2665 1110 HOH   HOH A . 
BA 11 HOH   566  2666 1150 HOH   HOH A . 
BA 11 HOH   567  2667 1300 HOH   HOH A . 
BA 11 HOH   568  2668 920  HOH   HOH A . 
BA 11 HOH   569  2669 2437 HOH   HOH A . 
BA 11 HOH   570  2670 468  HOH   HOH A . 
BA 11 HOH   571  2671 367  HOH   HOH A . 
BA 11 HOH   572  2672 1640 HOH   HOH A . 
BA 11 HOH   573  2673 2306 HOH   HOH A . 
BA 11 HOH   574  2674 160  HOH   HOH A . 
BA 11 HOH   575  2675 2544 HOH   HOH A . 
BA 11 HOH   576  2676 998  HOH   HOH A . 
BA 11 HOH   577  2677 2652 HOH   HOH A . 
BA 11 HOH   578  2678 2534 HOH   HOH A . 
BA 11 HOH   579  2679 1540 HOH   HOH A . 
BA 11 HOH   580  2680 1274 HOH   HOH A . 
BA 11 HOH   581  2681 673  HOH   HOH A . 
BA 11 HOH   582  2682 727  HOH   HOH A . 
BA 11 HOH   583  2683 430  HOH   HOH A . 
BA 11 HOH   584  2684 117  HOH   HOH A . 
BA 11 HOH   585  2685 350  HOH   HOH A . 
BA 11 HOH   586  2686 148  HOH   HOH A . 
BA 11 HOH   587  2687 664  HOH   HOH A . 
BA 11 HOH   588  2688 1098 HOH   HOH A . 
BA 11 HOH   589  2689 1818 HOH   HOH A . 
BA 11 HOH   590  2690 883  HOH   HOH A . 
BA 11 HOH   591  2691 95   HOH   HOH A . 
BA 11 HOH   592  2692 2350 HOH   HOH A . 
BA 11 HOH   593  2693 2239 HOH   HOH A . 
BA 11 HOH   594  2694 177  HOH   HOH A . 
BA 11 HOH   595  2695 831  HOH   HOH A . 
BA 11 HOH   596  2696 298  HOH   HOH A . 
BA 11 HOH   597  2697 1422 HOH   HOH A . 
BA 11 HOH   598  2698 2485 HOH   HOH A . 
BA 11 HOH   599  2699 1379 HOH   HOH A . 
BA 11 HOH   600  2700 1436 HOH   HOH A . 
BA 11 HOH   601  2701 115  HOH   HOH A . 
BA 11 HOH   602  2702 2493 HOH   HOH A . 
BA 11 HOH   603  2703 39   HOH   HOH A . 
BA 11 HOH   604  2704 1974 HOH   HOH A . 
BA 11 HOH   605  2705 614  HOH   HOH A . 
BA 11 HOH   606  2706 151  HOH   HOH A . 
BA 11 HOH   607  2707 1425 HOH   HOH A . 
BA 11 HOH   608  2708 90   HOH   HOH A . 
BA 11 HOH   609  2709 616  HOH   HOH A . 
BA 11 HOH   610  2710 1017 HOH   HOH A . 
BA 11 HOH   611  2711 487  HOH   HOH A . 
BA 11 HOH   612  2712 1487 HOH   HOH A . 
BA 11 HOH   613  2713 1176 HOH   HOH A . 
BA 11 HOH   614  2714 907  HOH   HOH A . 
BA 11 HOH   615  2715 1742 HOH   HOH A . 
BA 11 HOH   616  2716 293  HOH   HOH A . 
BA 11 HOH   617  2717 1659 HOH   HOH A . 
BA 11 HOH   618  2718 400  HOH   HOH A . 
BA 11 HOH   619  2719 372  HOH   HOH A . 
BA 11 HOH   620  2720 740  HOH   HOH A . 
BA 11 HOH   621  2721 488  HOH   HOH A . 
BA 11 HOH   622  2722 2596 HOH   HOH A . 
BA 11 HOH   623  2723 1434 HOH   HOH A . 
BA 11 HOH   624  2724 1053 HOH   HOH A . 
BA 11 HOH   625  2725 245  HOH   HOH A . 
BA 11 HOH   626  2726 871  HOH   HOH A . 
BA 11 HOH   627  2727 1792 HOH   HOH A . 
BA 11 HOH   628  2728 1525 HOH   HOH A . 
BA 11 HOH   629  2729 2679 HOH   HOH A . 
BA 11 HOH   630  2730 675  HOH   HOH A . 
BA 11 HOH   631  2731 374  HOH   HOH A . 
BA 11 HOH   632  2732 1228 HOH   HOH A . 
BA 11 HOH   633  2733 1433 HOH   HOH A . 
BA 11 HOH   634  2734 793  HOH   HOH A . 
BA 11 HOH   635  2735 1758 HOH   HOH A . 
BA 11 HOH   636  2736 56   HOH   HOH A . 
BA 11 HOH   637  2737 574  HOH   HOH A . 
BA 11 HOH   638  2738 1394 HOH   HOH A . 
BA 11 HOH   639  2739 2048 HOH   HOH A . 
BA 11 HOH   640  2740 967  HOH   HOH A . 
BA 11 HOH   641  2741 1907 HOH   HOH A . 
BA 11 HOH   642  2742 459  HOH   HOH A . 
BA 11 HOH   643  2743 995  HOH   HOH A . 
BA 11 HOH   644  2744 1126 HOH   HOH A . 
BA 11 HOH   645  2745 933  HOH   HOH A . 
BA 11 HOH   646  2746 844  HOH   HOH A . 
BA 11 HOH   647  2747 491  HOH   HOH A . 
BA 11 HOH   648  2748 2446 HOH   HOH A . 
BA 11 HOH   649  2749 297  HOH   HOH A . 
BA 11 HOH   650  2750 223  HOH   HOH A . 
BA 11 HOH   651  2751 2320 HOH   HOH A . 
BA 11 HOH   652  2752 1512 HOH   HOH A . 
BA 11 HOH   653  2753 1663 HOH   HOH A . 
BA 11 HOH   654  2754 2532 HOH   HOH A . 
BA 11 HOH   655  2755 722  HOH   HOH A . 
BA 11 HOH   656  2756 984  HOH   HOH A . 
BA 11 HOH   657  2757 1360 HOH   HOH A . 
BA 11 HOH   658  2758 1937 HOH   HOH A . 
BA 11 HOH   659  2759 1408 HOH   HOH A . 
BA 11 HOH   660  2760 2009 HOH   HOH A . 
BA 11 HOH   661  2761 2027 HOH   HOH A . 
BA 11 HOH   662  2762 536  HOH   HOH A . 
BA 11 HOH   663  2763 19   HOH   HOH A . 
BA 11 HOH   664  2764 2024 HOH   HOH A . 
BA 11 HOH   665  2765 1546 HOH   HOH A . 
BA 11 HOH   666  2766 1135 HOH   HOH A . 
BA 11 HOH   667  2767 966  HOH   HOH A . 
BA 11 HOH   668  2768 354  HOH   HOH A . 
BA 11 HOH   669  2769 515  HOH   HOH A . 
BA 11 HOH   670  2770 1452 HOH   HOH A . 
BA 11 HOH   671  2771 106  HOH   HOH A . 
BA 11 HOH   672  2772 42   HOH   HOH A . 
BA 11 HOH   673  2773 947  HOH   HOH A . 
BA 11 HOH   674  2774 504  HOH   HOH A . 
BA 11 HOH   675  2775 133  HOH   HOH A . 
BA 11 HOH   676  2776 460  HOH   HOH A . 
BA 11 HOH   677  2777 2424 HOH   HOH A . 
BA 11 HOH   678  2778 1382 HOH   HOH A . 
BA 11 HOH   679  2779 2000 HOH   HOH A . 
BA 11 HOH   680  2780 41   HOH   HOH A . 
BA 11 HOH   681  2781 1177 HOH   HOH A . 
BA 11 HOH   682  2782 1305 HOH   HOH A . 
BA 11 HOH   683  2783 1651 HOH   HOH A . 
BA 11 HOH   684  2784 495  HOH   HOH A . 
BA 11 HOH   685  2785 2331 HOH   HOH A . 
BA 11 HOH   686  2786 1063 HOH   HOH A . 
BA 11 HOH   687  2787 543  HOH   HOH A . 
BA 11 HOH   688  2788 878  HOH   HOH A . 
BA 11 HOH   689  2789 1954 HOH   HOH A . 
BA 11 HOH   690  2790 671  HOH   HOH A . 
BA 11 HOH   691  2791 2516 HOH   HOH A . 
BA 11 HOH   692  2792 1358 HOH   HOH A . 
BA 11 HOH   693  2793 2398 HOH   HOH A . 
BA 11 HOH   694  2794 2117 HOH   HOH A . 
BA 11 HOH   695  2795 834  HOH   HOH A . 
BA 11 HOH   696  2796 1227 HOH   HOH A . 
BA 11 HOH   697  2797 530  HOH   HOH A . 
BA 11 HOH   698  2798 2160 HOH   HOH A . 
BA 11 HOH   699  2799 683  HOH   HOH A . 
BA 11 HOH   700  2800 1304 HOH   HOH A . 
BA 11 HOH   701  2801 1975 HOH   HOH A . 
BA 11 HOH   702  2802 1616 HOH   HOH A . 
BA 11 HOH   703  2803 509  HOH   HOH A . 
BA 11 HOH   704  2804 924  HOH   HOH A . 
BA 11 HOH   705  2805 1302 HOH   HOH A . 
BA 11 HOH   706  2806 769  HOH   HOH A . 
BA 11 HOH   707  2807 388  HOH   HOH A . 
BA 11 HOH   708  2808 1250 HOH   HOH A . 
BA 11 HOH   709  2809 334  HOH   HOH A . 
BA 11 HOH   710  2810 1800 HOH   HOH A . 
BA 11 HOH   711  2811 760  HOH   HOH A . 
BA 11 HOH   712  2812 1719 HOH   HOH A . 
BA 11 HOH   713  2813 1478 HOH   HOH A . 
BA 11 HOH   714  2814 464  HOH   HOH A . 
BA 11 HOH   715  2815 1329 HOH   HOH A . 
BA 11 HOH   716  2816 788  HOH   HOH A . 
BA 11 HOH   717  2817 522  HOH   HOH A . 
BA 11 HOH   718  2818 865  HOH   HOH A . 
BA 11 HOH   719  2819 2452 HOH   HOH A . 
BA 11 HOH   720  2820 1062 HOH   HOH A . 
BA 11 HOH   721  2821 2503 HOH   HOH A . 
BA 11 HOH   722  2822 2126 HOH   HOH A . 
BA 11 HOH   723  2823 305  HOH   HOH A . 
BA 11 HOH   724  2824 1393 HOH   HOH A . 
BA 11 HOH   725  2825 1432 HOH   HOH A . 
BA 11 HOH   726  2826 1789 HOH   HOH A . 
BA 11 HOH   727  2827 686  HOH   HOH A . 
BA 11 HOH   728  2828 28   HOH   HOH A . 
BA 11 HOH   729  2829 1160 HOH   HOH A . 
BA 11 HOH   730  2830 1986 HOH   HOH A . 
BA 11 HOH   731  2831 1886 HOH   HOH A . 
BA 11 HOH   732  2832 1903 HOH   HOH A . 
BA 11 HOH   733  2833 2330 HOH   HOH A . 
BA 11 HOH   734  2834 375  HOH   HOH A . 
BA 11 HOH   735  2835 771  HOH   HOH A . 
BA 11 HOH   736  2836 1041 HOH   HOH A . 
BA 11 HOH   737  2837 2240 HOH   HOH A . 
BA 11 HOH   738  2838 2265 HOH   HOH A . 
BA 11 HOH   739  2839 701  HOH   HOH A . 
BA 11 HOH   740  2840 1012 HOH   HOH A . 
BA 11 HOH   741  2841 2536 HOH   HOH A . 
BA 11 HOH   742  2842 2367 HOH   HOH A . 
BA 11 HOH   743  2843 2062 HOH   HOH A . 
BA 11 HOH   744  2844 775  HOH   HOH A . 
BA 11 HOH   745  2845 1391 HOH   HOH A . 
BA 11 HOH   746  2846 1349 HOH   HOH A . 
BA 11 HOH   747  2847 159  HOH   HOH A . 
BA 11 HOH   748  2848 539  HOH   HOH A . 
BA 11 HOH   749  2849 610  HOH   HOH A . 
BA 11 HOH   750  2850 1511 HOH   HOH A . 
BA 11 HOH   751  2851 1661 HOH   HOH A . 
BA 11 HOH   752  2852 1004 HOH   HOH A . 
BA 11 HOH   753  2853 2425 HOH   HOH A . 
BA 11 HOH   754  2854 288  HOH   HOH A . 
BA 11 HOH   755  2855 404  HOH   HOH A . 
BA 11 HOH   756  2856 565  HOH   HOH A . 
BA 11 HOH   757  2857 603  HOH   HOH A . 
BA 11 HOH   758  2858 777  HOH   HOH A . 
BA 11 HOH   759  2859 2040 HOH   HOH A . 
BA 11 HOH   760  2860 1462 HOH   HOH A . 
BA 11 HOH   761  2861 299  HOH   HOH A . 
BA 11 HOH   762  2862 807  HOH   HOH A . 
BA 11 HOH   763  2863 934  HOH   HOH A . 
BA 11 HOH   764  2864 729  HOH   HOH A . 
BA 11 HOH   765  2865 2222 HOH   HOH A . 
BA 11 HOH   766  2866 74   HOH   HOH A . 
BA 11 HOH   767  2867 1252 HOH   HOH A . 
BA 11 HOH   768  2868 1623 HOH   HOH A . 
BA 11 HOH   769  2869 2047 HOH   HOH A . 
BA 11 HOH   770  2870 2501 HOH   HOH A . 
BA 11 HOH   771  2871 691  HOH   HOH A . 
BA 11 HOH   772  2872 1549 HOH   HOH A . 
BA 11 HOH   773  2873 1833 HOH   HOH A . 
BA 11 HOH   774  2874 560  HOH   HOH A . 
BA 11 HOH   775  2875 2721 HOH   HOH A . 
BA 11 HOH   776  2876 809  HOH   HOH A . 
BA 11 HOH   777  2877 1155 HOH   HOH A . 
BA 11 HOH   778  2878 949  HOH   HOH A . 
BA 11 HOH   779  2879 649  HOH   HOH A . 
BA 11 HOH   780  2880 589  HOH   HOH A . 
BA 11 HOH   781  2881 364  HOH   HOH A . 
BA 11 HOH   782  2882 2203 HOH   HOH A . 
BA 11 HOH   783  2883 1541 HOH   HOH A . 
BA 11 HOH   784  2884 2099 HOH   HOH A . 
BA 11 HOH   785  2885 370  HOH   HOH A . 
BA 11 HOH   786  2886 132  HOH   HOH A . 
BA 11 HOH   787  2887 870  HOH   HOH A . 
BA 11 HOH   788  2888 582  HOH   HOH A . 
BA 11 HOH   789  2889 1430 HOH   HOH A . 
BA 11 HOH   790  2890 830  HOH   HOH A . 
BA 11 HOH   791  2891 342  HOH   HOH A . 
BA 11 HOH   792  2892 1359 HOH   HOH A . 
BA 11 HOH   793  2893 1328 HOH   HOH A . 
BA 11 HOH   794  2894 1282 HOH   HOH A . 
BA 11 HOH   795  2895 780  HOH   HOH A . 
BA 11 HOH   796  2896 2460 HOH   HOH A . 
BA 11 HOH   797  2897 2420 HOH   HOH A . 
BA 11 HOH   798  2898 2072 HOH   HOH A . 
BA 11 HOH   799  2899 1070 HOH   HOH A . 
BA 11 HOH   800  2900 1772 HOH   HOH A . 
BA 11 HOH   801  2901 366  HOH   HOH A . 
BA 11 HOH   802  2902 1123 HOH   HOH A . 
BA 11 HOH   803  2903 1647 HOH   HOH A . 
BA 11 HOH   804  2904 531  HOH   HOH A . 
BA 11 HOH   805  2905 2600 HOH   HOH A . 
BA 11 HOH   806  2906 1020 HOH   HOH A . 
BA 11 HOH   807  2907 2693 HOH   HOH A . 
BA 11 HOH   808  2908 410  HOH   HOH A . 
BA 11 HOH   809  2909 1532 HOH   HOH A . 
BA 11 HOH   810  2910 2525 HOH   HOH A . 
BA 11 HOH   811  2911 2352 HOH   HOH A . 
BA 11 HOH   812  2912 1235 HOH   HOH A . 
BA 11 HOH   813  2913 1885 HOH   HOH A . 
BA 11 HOH   814  2914 2415 HOH   HOH A . 
BA 11 HOH   815  2915 2091 HOH   HOH A . 
BA 11 HOH   816  2916 1139 HOH   HOH A . 
BA 11 HOH   817  2917 1654 HOH   HOH A . 
BA 11 HOH   818  2918 463  HOH   HOH A . 
BA 11 HOH   819  2919 149  HOH   HOH A . 
BA 11 HOH   820  2920 900  HOH   HOH A . 
BA 11 HOH   821  2921 1677 HOH   HOH A . 
BA 11 HOH   822  2922 822  HOH   HOH A . 
BA 11 HOH   823  2923 596  HOH   HOH A . 
BA 11 HOH   824  2924 1395 HOH   HOH A . 
BA 11 HOH   825  2925 928  HOH   HOH A . 
BA 11 HOH   826  2926 208  HOH   HOH A . 
BA 11 HOH   827  2927 2161 HOH   HOH A . 
BA 11 HOH   828  2928 1009 HOH   HOH A . 
BA 11 HOH   829  2929 497  HOH   HOH A . 
BA 11 HOH   830  2930 1142 HOH   HOH A . 
BA 11 HOH   831  2931 1073 HOH   HOH A . 
BA 11 HOH   832  2932 433  HOH   HOH A . 
BA 11 HOH   833  2933 1113 HOH   HOH A . 
BA 11 HOH   834  2934 728  HOH   HOH A . 
BA 11 HOH   835  2935 36   HOH   HOH A . 
BA 11 HOH   836  2936 863  HOH   HOH A . 
BA 11 HOH   837  2937 83   HOH   HOH A . 
BA 11 HOH   838  2938 542  HOH   HOH A . 
BA 11 HOH   839  2939 2342 HOH   HOH A . 
BA 11 HOH   840  2940 2173 HOH   HOH A . 
BA 11 HOH   841  2941 1212 HOH   HOH A . 
BA 11 HOH   842  2942 1342 HOH   HOH A . 
BA 11 HOH   843  2943 2488 HOH   HOH A . 
BA 11 HOH   844  2944 1335 HOH   HOH A . 
BA 11 HOH   845  2945 2155 HOH   HOH A . 
BA 11 HOH   846  2946 2661 HOH   HOH A . 
BA 11 HOH   847  2947 1625 HOH   HOH A . 
BA 11 HOH   848  2948 2576 HOH   HOH A . 
BA 11 HOH   849  2949 1365 HOH   HOH A . 
BA 11 HOH   850  2950 68   HOH   HOH A . 
BA 11 HOH   851  2951 1728 HOH   HOH A . 
BA 11 HOH   852  2952 1923 HOH   HOH A . 
BA 11 HOH   853  2953 2542 HOH   HOH A . 
BA 11 HOH   854  2954 621  HOH   HOH A . 
BA 11 HOH   855  2955 1706 HOH   HOH A . 
BA 11 HOH   856  2956 1627 HOH   HOH A . 
BA 11 HOH   857  2957 1552 HOH   HOH A . 
BA 11 HOH   858  2958 2315 HOH   HOH A . 
BA 11 HOH   859  2959 2219 HOH   HOH A . 
BA 11 HOH   860  2960 454  HOH   HOH A . 
BA 11 HOH   861  2961 1361 HOH   HOH A . 
BA 11 HOH   862  2962 1590 HOH   HOH A . 
BA 11 HOH   863  2963 2124 HOH   HOH A . 
BA 11 HOH   864  2964 2362 HOH   HOH A . 
BA 11 HOH   865  2965 1125 HOH   HOH A . 
BA 11 HOH   866  2966 1917 HOH   HOH A . 
BA 11 HOH   867  2967 1864 HOH   HOH A . 
BA 11 HOH   868  2968 1863 HOH   HOH A . 
BA 11 HOH   869  2969 1877 HOH   HOH A . 
BA 11 HOH   870  2970 2162 HOH   HOH A . 
BA 11 HOH   871  2971 567  HOH   HOH A . 
BA 11 HOH   872  2972 2714 HOH   HOH A . 
BA 11 HOH   873  2973 2589 HOH   HOH A . 
BA 11 HOH   874  2974 1178 HOH   HOH A . 
BA 11 HOH   875  2975 2670 HOH   HOH A . 
BA 11 HOH   876  2976 1218 HOH   HOH A . 
BA 11 HOH   877  2977 2394 HOH   HOH A . 
BA 11 HOH   878  2978 557  HOH   HOH A . 
BA 11 HOH   879  2979 2479 HOH   HOH A . 
BA 11 HOH   880  2980 1311 HOH   HOH A . 
BA 11 HOH   881  2981 936  HOH   HOH A . 
BA 11 HOH   882  2982 886  HOH   HOH A . 
BA 11 HOH   883  2983 1673 HOH   HOH A . 
BA 11 HOH   884  2984 776  HOH   HOH A . 
BA 11 HOH   885  2985 2011 HOH   HOH A . 
BA 11 HOH   886  2986 1558 HOH   HOH A . 
BA 11 HOH   887  2987 2003 HOH   HOH A . 
BA 11 HOH   888  2988 1612 HOH   HOH A . 
BA 11 HOH   889  2989 2556 HOH   HOH A . 
BA 11 HOH   890  2990 2025 HOH   HOH A . 
BA 11 HOH   891  2991 1309 HOH   HOH A . 
BA 11 HOH   892  2992 667  HOH   HOH A . 
BA 11 HOH   893  2993 1243 HOH   HOH A . 
BA 11 HOH   894  2994 913  HOH   HOH A . 
BA 11 HOH   895  2995 600  HOH   HOH A . 
BA 11 HOH   896  2996 242  HOH   HOH A . 
BA 11 HOH   897  2997 1669 HOH   HOH A . 
BA 11 HOH   898  2998 2427 HOH   HOH A . 
BA 11 HOH   899  2999 2102 HOH   HOH A . 
BA 11 HOH   900  3000 1353 HOH   HOH A . 
BA 11 HOH   901  3001 2159 HOH   HOH A . 
BA 11 HOH   902  3002 1207 HOH   HOH A . 
BA 11 HOH   903  3003 688  HOH   HOH A . 
BA 11 HOH   904  3004 1836 HOH   HOH A . 
BA 11 HOH   905  3005 2095 HOH   HOH A . 
BA 11 HOH   906  3006 699  HOH   HOH A . 
BA 11 HOH   907  3007 4    HOH   HOH A . 
BA 11 HOH   908  3008 1488 HOH   HOH A . 
BA 11 HOH   909  3009 64   HOH   HOH A . 
BA 11 HOH   910  3010 2063 HOH   HOH A . 
BA 11 HOH   911  3011 2064 HOH   HOH A . 
BA 11 HOH   912  3012 2332 HOH   HOH A . 
BA 11 HOH   913  3013 23   HOH   HOH A . 
BA 11 HOH   914  3014 2359 HOH   HOH A . 
BA 11 HOH   915  3015 2444 HOH   HOH A . 
BA 11 HOH   916  3016 2477 HOH   HOH A . 
BA 11 HOH   917  3017 992  HOH   HOH A . 
BA 11 HOH   918  3018 2308 HOH   HOH A . 
BA 11 HOH   919  3019 1367 HOH   HOH A . 
BA 11 HOH   920  3020 1891 HOH   HOH A . 
BA 11 HOH   921  3021 1260 HOH   HOH A . 
BA 11 HOH   922  3022 2403 HOH   HOH A . 
BA 11 HOH   923  3023 2402 HOH   HOH A . 
BA 11 HOH   924  3024 2174 HOH   HOH A . 
BA 11 HOH   925  3025 2035 HOH   HOH A . 
BA 11 HOH   926  3026 1678 HOH   HOH A . 
BA 11 HOH   927  3027 2079 HOH   HOH A . 
BA 11 HOH   928  3028 103  HOH   HOH A . 
BA 11 HOH   929  3029 1269 HOH   HOH A . 
BA 11 HOH   930  3030 2244 HOH   HOH A . 
BA 11 HOH   931  3031 55   HOH   HOH A . 
BA 11 HOH   932  3032 1351 HOH   HOH A . 
BA 11 HOH   933  3033 1134 HOH   HOH A . 
BA 11 HOH   934  3034 916  HOH   HOH A . 
BA 11 HOH   935  3035 2717 HOH   HOH A . 
BA 11 HOH   936  3036 2723 HOH   HOH A . 
BA 11 HOH   937  3037 48   HOH   HOH A . 
BA 11 HOH   938  3038 2277 HOH   HOH A . 
BA 11 HOH   939  3039 2201 HOH   HOH A . 
BA 11 HOH   940  3040 2537 HOH   HOH A . 
BA 11 HOH   941  3041 2458 HOH   HOH A . 
BA 11 HOH   942  3042 2049 HOH   HOH A . 
BA 11 HOH   943  3043 2245 HOH   HOH A . 
BA 11 HOH   944  3044 2156 HOH   HOH A . 
BA 11 HOH   945  3045 819  HOH   HOH A . 
BA 11 HOH   946  3046 493  HOH   HOH A . 
BA 11 HOH   947  3047 1660 HOH   HOH A . 
BA 11 HOH   948  3048 2389 HOH   HOH A . 
BA 11 HOH   949  3049 1272 HOH   HOH A . 
BA 11 HOH   950  3050 1813 HOH   HOH A . 
BA 11 HOH   951  3051 1927 HOH   HOH A . 
BA 11 HOH   952  3052 1777 HOH   HOH A . 
BA 11 HOH   953  3053 100  HOH   HOH A . 
BA 11 HOH   954  3054 1076 HOH   HOH A . 
BA 11 HOH   955  3055 2459 HOH   HOH A . 
BA 11 HOH   956  3056 1876 HOH   HOH A . 
BA 11 HOH   957  3057 2533 HOH   HOH A . 
BA 11 HOH   958  3058 1404 HOH   HOH A . 
BA 11 HOH   959  3059 2491 HOH   HOH A . 
BA 11 HOH   960  3060 2637 HOH   HOH A . 
BA 11 HOH   961  3061 1224 HOH   HOH A . 
BA 11 HOH   962  3062 2657 HOH   HOH A . 
BA 11 HOH   963  3063 75   HOH   HOH A . 
BA 11 HOH   964  3064 2573 HOH   HOH A . 
BA 11 HOH   965  3065 22   HOH   HOH A . 
BA 11 HOH   966  3066 751  HOH   HOH A . 
BA 11 HOH   967  3067 2220 HOH   HOH A . 
BA 11 HOH   968  3068 56   HOH   HOH A . 
BA 11 HOH   969  3069 1486 HOH   HOH A . 
BA 11 HOH   970  3070 1132 HOH   HOH A . 
BA 11 HOH   971  3071 2094 HOH   HOH A . 
BA 11 HOH   972  3072 1624 HOH   HOH A . 
BA 11 HOH   973  3073 1731 HOH   HOH A . 
BA 11 HOH   974  3074 1709 HOH   HOH A . 
BA 11 HOH   975  3075 2157 HOH   HOH A . 
BA 11 HOH   976  3076 1681 HOH   HOH A . 
BA 11 HOH   977  3077 1023 HOH   HOH A . 
BA 11 HOH   978  3078 1317 HOH   HOH A . 
BA 11 HOH   979  3079 2318 HOH   HOH A . 
BA 11 HOH   980  3080 2730 HOH   HOH A . 
BA 11 HOH   981  3081 2438 HOH   HOH A . 
BA 11 HOH   982  3082 1190 HOH   HOH A . 
BA 11 HOH   983  3083 2465 HOH   HOH A . 
BA 11 HOH   984  3084 910  HOH   HOH A . 
BA 11 HOH   985  3085 550  HOH   HOH A . 
BA 11 HOH   986  3086 1631 HOH   HOH A . 
BA 11 HOH   987  3087 1161 HOH   HOH A . 
BA 11 HOH   988  3088 1791 HOH   HOH A . 
BA 11 HOH   989  3089 2475 HOH   HOH A . 
BA 11 HOH   990  3090 1797 HOH   HOH A . 
BA 11 HOH   991  3091 2163 HOH   HOH A . 
BA 11 HOH   992  3092 586  HOH   HOH A . 
BA 11 HOH   993  3093 955  HOH   HOH A . 
BA 11 HOH   994  3094 2216 HOH   HOH A . 
BA 11 HOH   995  3095 1039 HOH   HOH A . 
BA 11 HOH   996  3096 2326 HOH   HOH A . 
BA 11 HOH   997  3097 2701 HOH   HOH A . 
BA 11 HOH   998  3098 2678 HOH   HOH A . 
BA 11 HOH   999  3099 2211 HOH   HOH A . 
BA 11 HOH   1000 3100 1992 HOH   HOH A . 
BA 11 HOH   1001 3101 823  HOH   HOH A . 
BA 11 HOH   1002 3102 2407 HOH   HOH A . 
BA 11 HOH   1003 3103 1547 HOH   HOH A . 
BA 11 HOH   1004 3104 845  HOH   HOH A . 
BA 11 HOH   1005 3105 2123 HOH   HOH A . 
BA 11 HOH   1006 3106 1046 HOH   HOH A . 
BA 11 HOH   1007 3107 2177 HOH   HOH A . 
BA 11 HOH   1008 3108 1345 HOH   HOH A . 
BA 11 HOH   1009 3109 2080 HOH   HOH A . 
BA 11 HOH   1010 3110 1315 HOH   HOH A . 
BA 11 HOH   1011 3111 1289 HOH   HOH A . 
BA 11 HOH   1012 3112 2667 HOH   HOH A . 
BA 11 HOH   1013 3113 2391 HOH   HOH A . 
BA 11 HOH   1014 3114 2368 HOH   HOH A . 
BA 11 HOH   1015 3115 736  HOH   HOH A . 
BA 11 HOH   1016 3116 2663 HOH   HOH A . 
BA 11 HOH   1017 3117 2494 HOH   HOH A . 
BA 11 HOH   1018 3118 2567 HOH   HOH A . 
BA 11 HOH   1019 3119 2453 HOH   HOH A . 
BA 11 HOH   1020 3120 1517 HOH   HOH A . 
BA 11 HOH   1021 3121 1420 HOH   HOH A . 
BA 11 HOH   1022 3122 61   HOH   HOH A . 
BA 11 HOH   1023 3123 1454 HOH   HOH A . 
BA 11 HOH   1024 3124 2323 HOH   HOH A . 
BA 11 HOH   1025 3125 1928 HOH   HOH A . 
BA 11 HOH   1026 3126 1884 HOH   HOH A . 
BA 11 HOH   1027 3127 2366 HOH   HOH A . 
BA 11 HOH   1028 3128 554  HOH   HOH A . 
BA 11 HOH   1029 3129 1066 HOH   HOH A . 
BA 11 HOH   1030 3130 1861 HOH   HOH A . 
BA 11 HOH   1031 3131 1850 HOH   HOH A . 
BA 11 HOH   1032 3132 2212 HOH   HOH A . 
BA 11 HOH   1033 3133 1036 HOH   HOH A . 
BA 11 HOH   1034 3134 2347 HOH   HOH A . 
BA 11 HOH   1035 3135 1533 HOH   HOH A . 
BA 11 HOH   1036 3136 1435 HOH   HOH A . 
BA 11 HOH   1037 3137 1187 HOH   HOH A . 
BA 11 HOH   1038 3138 1    HOH   HOH A . 
BA 11 HOH   1039 3139 2486 HOH   HOH A . 
BA 11 HOH   1040 3140 2685 HOH   HOH A . 
BA 11 HOH   1041 3141 2152 HOH   HOH A . 
BA 11 HOH   1042 3142 1951 HOH   HOH A . 
BA 11 HOH   1043 3143 1730 HOH   HOH A . 
BA 11 HOH   1044 3144 1636 HOH   HOH A . 
BA 11 HOH   1045 3145 1499 HOH   HOH A . 
BA 11 HOH   1046 3146 2541 HOH   HOH A . 
BA 11 HOH   1047 3147 2254 HOH   HOH A . 
BA 11 HOH   1048 3148 1611 HOH   HOH A . 
BA 11 HOH   1049 3149 6    HOH   HOH A . 
BA 11 HOH   1050 3150 2325 HOH   HOH A . 
BA 11 HOH   1051 3151 413  HOH   HOH A . 
BA 11 HOH   1052 3152 2012 HOH   HOH A . 
BA 11 HOH   1053 3153 2081 HOH   HOH A . 
BA 11 HOH   1054 3154 2376 HOH   HOH A . 
BA 11 HOH   1055 3155 2611 HOH   HOH A . 
BA 11 HOH   1056 3156 52   HOH   HOH A . 
BA 11 HOH   1057 3157 1919 HOH   HOH A . 
BA 11 HOH   1058 3158 2555 HOH   HOH A . 
BA 11 HOH   1059 3159 92   HOH   HOH A . 
BA 11 HOH   1060 3160 1325 HOH   HOH A . 
BA 11 HOH   1061 3161 820  HOH   HOH A . 
BA 11 HOH   1062 3162 2722 HOH   HOH A . 
BA 11 HOH   1063 3163 2149 HOH   HOH A . 
BA 11 HOH   1064 3164 70   HOH   HOH A . 
BA 11 HOH   1065 3165 1407 HOH   HOH A . 
BA 11 HOH   1066 3166 1372 HOH   HOH A . 
BA 11 HOH   1067 3167 1316 HOH   HOH A . 
BA 11 HOH   1068 3168 2176 HOH   HOH A . 
BA 11 HOH   1069 3169 194  HOH   HOH A . 
BA 11 HOH   1070 3170 2252 HOH   HOH A . 
BA 11 HOH   1071 3171 1904 HOH   HOH A . 
BA 11 HOH   1072 3172 1471 HOH   HOH A . 
BA 11 HOH   1073 3173 2107 HOH   HOH A . 
BA 11 HOH   1074 3174 2280 HOH   HOH A . 
BA 11 HOH   1075 3175 2535 HOH   HOH A . 
BA 11 HOH   1076 3176 712  HOH   HOH A . 
BA 11 HOH   1077 3177 369  HOH   HOH A . 
BA 11 HOH   1078 3178 2153 HOH   HOH A . 
BA 11 HOH   1079 3179 2026 HOH   HOH A . 
BA 11 HOH   1080 3180 1332 HOH   HOH A . 
BA 11 HOH   1081 3181 1578 HOH   HOH A . 
BA 11 HOH   1082 3182 1926 HOH   HOH A . 
BA 11 HOH   1083 3183 1241 HOH   HOH A . 
BA 11 HOH   1084 3184 1373 HOH   HOH A . 
BA 11 HOH   1085 3185 1222 HOH   HOH A . 
BA 11 HOH   1086 3186 1444 HOH   HOH A . 
BA 11 HOH   1087 3187 1180 HOH   HOH A . 
BA 11 HOH   1088 3188 2572 HOH   HOH A . 
BA 11 HOH   1089 3189 1213 HOH   HOH A . 
BA 11 HOH   1090 3190 1557 HOH   HOH A . 
BA 11 HOH   1091 3191 1371 HOH   HOH A . 
BA 11 HOH   1092 3192 2098 HOH   HOH A . 
BA 11 HOH   1093 3193 2545 HOH   HOH A . 
BA 11 HOH   1094 3194 1855 HOH   HOH A . 
BA 11 HOH   1095 3195 1757 HOH   HOH A . 
BA 11 HOH   1096 3196 2422 HOH   HOH A . 
BA 11 HOH   1097 3197 2377 HOH   HOH A . 
BA 11 HOH   1098 3198 2116 HOH   HOH A . 
BA 11 HOH   1099 3199 2554 HOH   HOH A . 
BA 11 HOH   1100 3200 1337 HOH   HOH A . 
BA 11 HOH   1101 3201 119  HOH   HOH A . 
BA 11 HOH   1102 3202 2520 HOH   HOH A . 
BA 11 HOH   1103 3203 1562 HOH   HOH A . 
BA 11 HOH   1104 3204 1882 HOH   HOH A . 
BA 11 HOH   1105 3205 455  HOH   HOH A . 
BA 11 HOH   1106 3206 2671 HOH   HOH A . 
BA 11 HOH   1107 3207 1881 HOH   HOH A . 
BA 11 HOH   1108 3208 2251 HOH   HOH A . 
BA 11 HOH   1109 3209 20   HOH   HOH A . 
BA 11 HOH   1110 3210 1356 HOH   HOH A . 
BA 11 HOH   1111 3211 1419 HOH   HOH A . 
BA 11 HOH   1112 3212 32   HOH   HOH A . 
BA 11 HOH   1113 3213 1972 HOH   HOH A . 
BA 11 HOH   1114 3214 2509 HOH   HOH A . 
BA 11 HOH   1115 3215 2519 HOH   HOH A . 
BA 11 HOH   1116 3216 1675 HOH   HOH A . 
BA 11 HOH   1117 3217 35   HOH   HOH A . 
BA 11 HOH   1118 3218 420  HOH   HOH A . 
BA 11 HOH   1119 3219 1364 HOH   HOH A . 
BA 11 HOH   1120 3220 2388 HOH   HOH A . 
BA 11 HOH   1121 3221 1498 HOH   HOH A . 
BA 11 HOH   1122 3222 90   HOH   HOH A . 
BA 11 HOH   1123 3223 2496 HOH   HOH A . 
BA 11 HOH   1124 3224 2472 HOH   HOH A . 
BA 11 HOH   1125 3225 2603 HOH   HOH A . 
BA 11 HOH   1126 3226 1539 HOH   HOH A . 
BA 11 HOH   1127 3227 768  HOH   HOH A . 
BA 11 HOH   1128 3228 1837 HOH   HOH A . 
BA 11 HOH   1129 3229 1326 HOH   HOH A . 
BA 11 HOH   1130 3230 2103 HOH   HOH A . 
BA 11 HOH   1131 3231 2409 HOH   HOH A . 
BA 11 HOH   1132 3232 29   HOH   HOH A . 
BA 11 HOH   1133 3233 2109 HOH   HOH A . 
BA 11 HOH   1134 3234 1078 HOH   HOH A . 
BA 11 HOH   1135 3235 2577 HOH   HOH A . 
BA 11 HOH   1136 3236 2649 HOH   HOH A . 
BA 11 HOH   1137 3237 2209 HOH   HOH A . 
BA 11 HOH   1138 3238 2664 HOH   HOH A . 
BA 11 HOH   1139 3239 1140 HOH   HOH A . 
BA 11 HOH   1140 3240 2093 HOH   HOH A . 
BA 11 HOH   1141 3241 1550 HOH   HOH A . 
BA 11 HOH   1142 3242 2451 HOH   HOH A . 
BA 11 HOH   1143 3243 51   HOH   HOH A . 
BA 11 HOH   1144 3244 885  HOH   HOH A . 
BA 11 HOH   1145 3245 66   HOH   HOH A . 
BA 11 HOH   1146 3246 256  HOH   HOH A . 
BA 11 HOH   1147 3247 1888 HOH   HOH A . 
BA 11 HOH   1148 3248 833  HOH   HOH A . 
BA 11 HOH   1149 3249 1166 HOH   HOH A . 
BA 11 HOH   1150 3250 1924 HOH   HOH A . 
BA 11 HOH   1151 3251 1112 HOH   HOH A . 
BA 11 HOH   1152 3252 2082 HOH   HOH A . 
BA 11 HOH   1153 3253 2718 HOH   HOH A . 
BA 11 HOH   1154 3254 2131 HOH   HOH A . 
BA 11 HOH   1155 3255 774  HOH   HOH A . 
BA 11 HOH   1156 3256 1206 HOH   HOH A . 
BA 11 HOH   1157 3257 2598 HOH   HOH A . 
BA 11 HOH   1158 3258 1477 HOH   HOH A . 
BA 11 HOH   1159 3259 2110 HOH   HOH A . 
BA 11 HOH   1160 3260 2243 HOH   HOH A . 
BA 11 HOH   1161 3261 1149 HOH   HOH A . 
BA 11 HOH   1162 3262 2146 HOH   HOH A . 
BA 11 HOH   1163 3263 1638 HOH   HOH A . 
BA 11 HOH   1164 3264 617  HOH   HOH A . 
BA 11 HOH   1165 3265 106  HOH   HOH A . 
BA 11 HOH   1166 3266 1738 HOH   HOH A . 
BA 11 HOH   1167 3267 503  HOH   HOH A . 
BA 11 HOH   1168 3268 1457 HOH   HOH A . 
BA 11 HOH   1169 3269 1823 HOH   HOH A . 
BA 11 HOH   1170 3270 1199 HOH   HOH A . 
BA 11 HOH   1171 3271 87   HOH   HOH A . 
BA 11 HOH   1172 3272 1528 HOH   HOH A . 
BA 11 HOH   1173 3273 1935 HOH   HOH A . 
BA 11 HOH   1174 3274 1908 HOH   HOH A . 
BA 11 HOH   1175 3275 914  HOH   HOH A . 
BA 11 HOH   1176 3276 1572 HOH   HOH A . 
BA 11 HOH   1177 3277 1189 HOH   HOH A . 
BA 11 HOH   1178 3278 2073 HOH   HOH A . 
BA 11 HOH   1179 3279 5    HOH   HOH A . 
BA 11 HOH   1180 3280 1310 HOH   HOH A . 
BA 11 HOH   1181 3281 1958 HOH   HOH A . 
BA 11 HOH   1182 3282 2358 HOH   HOH A . 
BA 11 HOH   1183 3283 2121 HOH   HOH A . 
BA 11 HOH   1184 3284 1464 HOH   HOH A . 
BA 11 HOH   1185 3285 2610 HOH   HOH A . 
BA 11 HOH   1186 3286 1102 HOH   HOH A . 
BA 11 HOH   1187 3287 2303 HOH   HOH A . 
BA 11 HOH   1188 3288 2354 HOH   HOH A . 
BA 11 HOH   1189 3289 1217 HOH   HOH A . 
BA 11 HOH   1190 3290 1587 HOH   HOH A . 
BA 11 HOH   1191 3291 2512 HOH   HOH A . 
BA 11 HOH   1192 3292 1717 HOH   HOH A . 
BA 11 HOH   1193 3293 1460 HOH   HOH A . 
BA 11 HOH   1194 3294 1409 HOH   HOH A . 
BA 11 HOH   1195 3295 1955 HOH   HOH A . 
BA 11 HOH   1196 3296 1741 HOH   HOH A . 
BA 11 HOH   1197 3297 2108 HOH   HOH A . 
BA 11 HOH   1198 3298 1852 HOH   HOH A . 
BA 11 HOH   1199 3299 1247 HOH   HOH A . 
BA 11 HOH   1200 3300 594  HOH   HOH A . 
BA 11 HOH   1201 3301 2720 HOH   HOH A . 
BA 11 HOH   1202 3302 2170 HOH   HOH A . 
BA 11 HOH   1203 3303 2039 HOH   HOH A . 
BA 11 HOH   1204 3304 521  HOH   HOH A . 
BA 11 HOH   1205 3305 1828 HOH   HOH A . 
BA 11 HOH   1206 3306 1870 HOH   HOH A . 
BA 11 HOH   1207 3307 72   HOH   HOH A . 
BA 11 HOH   1208 3308 1839 HOH   HOH A . 
BA 11 HOH   1209 3309 1662 HOH   HOH A . 
BA 11 HOH   1210 3310 800  HOH   HOH A . 
BA 11 HOH   1211 3311 1497 HOH   HOH A . 
BA 11 HOH   1212 3312 19   HOH   HOH A . 
BA 11 HOH   1213 3313 2392 HOH   HOH A . 
BA 11 HOH   1214 3314 1555 HOH   HOH A . 
BA 11 HOH   1215 3315 2101 HOH   HOH A . 
BA 11 HOH   1216 3316 2668 HOH   HOH A . 
BA 11 HOH   1217 3317 1732 HOH   HOH A . 
BA 11 HOH   1218 3318 1961 HOH   HOH A . 
BA 11 HOH   1219 3319 994  HOH   HOH A . 
BA 11 HOH   1220 3320 1606 HOH   HOH A . 
BA 11 HOH   1221 3321 2478 HOH   HOH A . 
BA 11 HOH   1222 3322 1484 HOH   HOH A . 
BA 11 HOH   1223 3323 323  HOH   HOH A . 
BA 11 HOH   1224 3324 1963 HOH   HOH A . 
BA 11 HOH   1225 3325 986  HOH   HOH A . 
BA 11 HOH   1226 3326 1480 HOH   HOH A . 
BA 11 HOH   1227 3327 897  HOH   HOH A . 
BA 11 HOH   1228 3328 1680 HOH   HOH A . 
BA 11 HOH   1229 3329 1492 HOH   HOH A . 
BA 11 HOH   1230 3330 1901 HOH   HOH A . 
BA 11 HOH   1231 3331 2492 HOH   HOH A . 
BA 11 HOH   1232 3332 2302 HOH   HOH A . 
BA 11 HOH   1233 3333 2700 HOH   HOH A . 
BA 11 HOH   1234 3334 1044 HOH   HOH A . 
BA 11 HOH   1235 3335 2395 HOH   HOH A . 
BA 11 HOH   1236 3336 1330 HOH   HOH A . 
BA 11 HOH   1237 3337 2699 HOH   HOH A . 
BA 11 HOH   1238 3338 1075 HOH   HOH A . 
BA 11 HOH   1239 3339 980  HOH   HOH A . 
BA 11 HOH   1240 3340 1427 HOH   HOH A . 
BA 11 HOH   1241 3341 33   HOH   HOH A . 
BA 11 HOH   1242 3342 1202 HOH   HOH A . 
BA 11 HOH   1243 3343 2287 HOH   HOH A . 
BA 11 HOH   1244 3344 2609 HOH   HOH A . 
BA 11 HOH   1245 3345 45   HOH   HOH A . 
BA 11 HOH   1246 3346 2608 HOH   HOH A . 
BA 11 HOH   1247 3347 47   HOH   HOH A . 
BA 11 HOH   1248 3348 1853 HOH   HOH A . 
BA 11 HOH   1249 3349 1918 HOH   HOH A . 
BA 11 HOH   1250 3350 2015 HOH   HOH A . 
BA 11 HOH   1251 3351 1108 HOH   HOH A . 
BA 11 HOH   1252 3352 59   HOH   HOH A . 
BA 11 HOH   1253 3353 2621 HOH   HOH A . 
BA 11 HOH   1254 3354 1200 HOH   HOH A . 
BA 11 HOH   1255 3355 2333 HOH   HOH A . 
BA 11 HOH   1256 3356 1762 HOH   HOH A . 
BA 11 HOH   1257 3357 1225 HOH   HOH A . 
BA 11 HOH   1258 3358 2370 HOH   HOH A . 
BA 11 HOH   1259 3359 853  HOH   HOH A . 
BA 11 HOH   1260 3360 1538 HOH   HOH A . 
BA 11 HOH   1261 3361 2562 HOH   HOH A . 
BA 11 HOH   1262 3362 2115 HOH   HOH A . 
BA 11 HOH   1263 3363 46   HOH   HOH A . 
BA 11 HOH   1264 3364 1878 HOH   HOH A . 
BA 11 HOH   1265 3365 1476 HOH   HOH A . 
BA 11 HOH   1266 3366 1298 HOH   HOH A . 
BA 11 HOH   1267 3367 24   HOH   HOH A . 
BA 11 HOH   1268 3368 91   HOH   HOH A . 
BA 11 HOH   1269 3369 1664 HOH   HOH A . 
BA 11 HOH   1270 3370 1687 HOH   HOH A . 
BA 11 HOH   1271 3371 1283 HOH   HOH A . 
BA 11 HOH   1272 3372 2487 HOH   HOH A . 
BA 11 HOH   1273 3373 2113 HOH   HOH A . 
BA 11 HOH   1274 3374 2285 HOH   HOH A . 
BA 11 HOH   1275 3375 2638 HOH   HOH A . 
BA 11 HOH   1276 3376 2147 HOH   HOH A . 
BA 11 HOH   1277 3377 1834 HOH   HOH A . 
BA 11 HOH   1278 3378 34   HOH   HOH A . 
BA 11 HOH   1279 3379 12   HOH   HOH A . 
BA 11 HOH   1280 3380 1496 HOH   HOH A . 
BA 11 HOH   1281 3381 1209 HOH   HOH A . 
BA 11 HOH   1282 3382 1264 HOH   HOH A . 
BA 11 HOH   1283 3383 1002 HOH   HOH A . 
BA 11 HOH   1284 3384 1931 HOH   HOH A . 
BA 11 HOH   1285 3385 1504 HOH   HOH A . 
BA 11 HOH   1286 3386 2148 HOH   HOH A . 
BA 11 HOH   1287 3387 1794 HOH   HOH A . 
CA 11 HOH   1    2101 2030 HOH   HOH B . 
CA 11 HOH   2    2102 1626 HOH   HOH B . 
CA 11 HOH   3    2103 1577 HOH   HOH B . 
CA 11 HOH   4    2104 2406 HOH   HOH B . 
CA 11 HOH   5    2105 1674 HOH   HOH B . 
CA 11 HOH   6    2106 2538 HOH   HOH B . 
CA 11 HOH   7    2107 2258 HOH   HOH B . 
CA 11 HOH   8    2108 2129 HOH   HOH B . 
CA 11 HOH   9    2109 656  HOH   HOH B . 
CA 11 HOH   10   2110 2659 HOH   HOH B . 
CA 11 HOH   11   2111 2677 HOH   HOH B . 
CA 11 HOH   12   2112 1229 HOH   HOH B . 
CA 11 HOH   13   2113 773  HOH   HOH B . 
CA 11 HOH   14   2114 2416 HOH   HOH B . 
CA 11 HOH   15   2115 2260 HOH   HOH B . 
CA 11 HOH   16   2116 2135 HOH   HOH B . 
CA 11 HOH   17   2117 2361 HOH   HOH B . 
CA 11 HOH   18   2118 904  HOH   HOH B . 
CA 11 HOH   19   2119 2729 HOH   HOH B . 
CA 11 HOH   20   2120 2373 HOH   HOH B . 
CA 11 HOH   21   2121 2470 HOH   HOH B . 
CA 11 HOH   22   2122 2397 HOH   HOH B . 
CA 11 HOH   23   2123 1170 HOH   HOH B . 
CA 11 HOH   24   2124 1340 HOH   HOH B . 
CA 11 HOH   25   2125 1064 HOH   HOH B . 
CA 11 HOH   26   2126 2189 HOH   HOH B . 
CA 11 HOH   27   2127 2226 HOH   HOH B . 
CA 11 HOH   28   2128 973  HOH   HOH B . 
CA 11 HOH   29   2129 1030 HOH   HOH B . 
CA 11 HOH   30   2130 1819 HOH   HOH B . 
CA 11 HOH   31   2131 787  HOH   HOH B . 
CA 11 HOH   32   2132 1723 HOH   HOH B . 
CA 11 HOH   33   2133 801  HOH   HOH B . 
CA 11 HOH   34   2134 1277 HOH   HOH B . 
CA 11 HOH   35   2135 626  HOH   HOH B . 
CA 11 HOH   36   2136 564  HOH   HOH B . 
CA 11 HOH   37   2137 839  HOH   HOH B . 
CA 11 HOH   38   2138 2712 HOH   HOH B . 
CA 11 HOH   39   2139 10   HOH   HOH B . 
CA 11 HOH   40   2140 202  HOH   HOH B . 
CA 11 HOH   41   2141 1785 HOH   HOH B . 
CA 11 HOH   42   2142 1398 HOH   HOH B . 
CA 11 HOH   43   2143 2658 HOH   HOH B . 
CA 11 HOH   44   2144 2702 HOH   HOH B . 
CA 11 HOH   45   2145 2204 HOH   HOH B . 
CA 11 HOH   46   2146 1912 HOH   HOH B . 
CA 11 HOH   47   2147 94   HOH   HOH B . 
CA 11 HOH   48   2148 972  HOH   HOH B . 
CA 11 HOH   49   2149 501  HOH   HOH B . 
CA 11 HOH   50   2150 1644 HOH   HOH B . 
CA 11 HOH   51   2151 1116 HOH   HOH B . 
CA 11 HOH   52   2152 962  HOH   HOH B . 
CA 11 HOH   53   2153 1314 HOH   HOH B . 
CA 11 HOH   54   2154 2060 HOH   HOH B . 
CA 11 HOH   55   2155 2660 HOH   HOH B . 
CA 11 HOH   56   2156 1956 HOH   HOH B . 
CA 11 HOH   57   2157 2345 HOH   HOH B . 
CA 11 HOH   58   2158 2662 HOH   HOH B . 
CA 11 HOH   59   2159 2196 HOH   HOH B . 
CA 11 HOH   60   2160 79   HOH   HOH B . 
CA 11 HOH   61   2161 2190 HOH   HOH B . 
CA 11 HOH   62   2162 2467 HOH   HOH B . 
CA 11 HOH   63   2163 1210 HOH   HOH B . 
CA 11 HOH   64   2164 71   HOH   HOH B . 
CA 11 HOH   65   2165 2655 HOH   HOH B . 
CA 11 HOH   66   2166 313  HOH   HOH B . 
CA 11 HOH   67   2167 573  HOH   HOH B . 
CA 11 HOH   68   2168 2233 HOH   HOH B . 
CA 11 HOH   69   2169 363  HOH   HOH B . 
CA 11 HOH   70   2170 117  HOH   HOH B . 
CA 11 HOH   71   2171 1694 HOH   HOH B . 
CA 11 HOH   72   2172 1245 HOH   HOH B . 
CA 11 HOH   73   2173 2709 HOH   HOH B . 
CA 11 HOH   74   2174 59   HOH   HOH B . 
CA 11 HOH   75   2175 2225 HOH   HOH B . 
CA 11 HOH   76   2176 397  HOH   HOH B . 
CA 11 HOH   77   2177 2682 HOH   HOH B . 
CA 11 HOH   78   2178 631  HOH   HOH B . 
CA 11 HOH   79   2179 794  HOH   HOH B . 
CA 11 HOH   80   2180 287  HOH   HOH B . 
CA 11 HOH   81   2181 1174 HOH   HOH B . 
CA 11 HOH   82   2182 125  HOH   HOH B . 
CA 11 HOH   83   2183 292  HOH   HOH B . 
CA 11 HOH   84   2184 1248 HOH   HOH B . 
CA 11 HOH   85   2185 1109 HOH   HOH B . 
CA 11 HOH   86   2186 628  HOH   HOH B . 
CA 11 HOH   87   2187 2340 HOH   HOH B . 
CA 11 HOH   88   2188 1534 HOH   HOH B . 
CA 11 HOH   89   2189 193  HOH   HOH B . 
CA 11 HOH   90   2190 627  HOH   HOH B . 
CA 11 HOH   91   2191 953  HOH   HOH B . 
CA 11 HOH   92   2192 756  HOH   HOH B . 
CA 11 HOH   93   2193 935  HOH   HOH B . 
CA 11 HOH   94   2194 353  HOH   HOH B . 
CA 11 HOH   95   2195 879  HOH   HOH B . 
CA 11 HOH   96   2196 520  HOH   HOH B . 
CA 11 HOH   97   2197 1744 HOH   HOH B . 
CA 11 HOH   98   2198 13   HOH   HOH B . 
CA 11 HOH   99   2199 1449 HOH   HOH B . 
CA 11 HOH   100  2200 1508 HOH   HOH B . 
CA 11 HOH   101  2201 1042 HOH   HOH B . 
CA 11 HOH   102  2202 2683 HOH   HOH B . 
CA 11 HOH   103  2203 1822 HOH   HOH B . 
CA 11 HOH   104  2204 1893 HOH   HOH B . 
CA 11 HOH   105  2205 1548 HOH   HOH B . 
CA 11 HOH   106  2206 1585 HOH   HOH B . 
CA 11 HOH   107  2207 385  HOH   HOH B . 
CA 11 HOH   108  2208 1291 HOH   HOH B . 
CA 11 HOH   109  2209 2311 HOH   HOH B . 
CA 11 HOH   110  2210 2182 HOH   HOH B . 
CA 11 HOH   111  2211 478  HOH   HOH B . 
CA 11 HOH   112  2212 1456 HOH   HOH B . 
CA 11 HOH   113  2213 1172 HOH   HOH B . 
CA 11 HOH   114  2214 860  HOH   HOH B . 
CA 11 HOH   115  2215 1374 HOH   HOH B . 
CA 11 HOH   116  2216 867  HOH   HOH B . 
CA 11 HOH   117  2217 1220 HOH   HOH B . 
CA 11 HOH   118  2218 678  HOH   HOH B . 
CA 11 HOH   119  2219 72   HOH   HOH B . 
CA 11 HOH   120  2220 57   HOH   HOH B . 
CA 11 HOH   121  2221 230  HOH   HOH B . 
CA 11 HOH   122  2222 1388 HOH   HOH B . 
CA 11 HOH   123  2223 2418 HOH   HOH B . 
CA 11 HOH   124  2224 637  HOH   HOH B . 
CA 11 HOH   125  2225 1696 HOH   HOH B . 
CA 11 HOH   126  2226 632  HOH   HOH B . 
CA 11 HOH   127  2227 711  HOH   HOH B . 
CA 11 HOH   128  2228 1157 HOH   HOH B . 
CA 11 HOH   129  2229 27   HOH   HOH B . 
CA 11 HOH   130  2230 257  HOH   HOH B . 
CA 11 HOH   131  2231 1141 HOH   HOH B . 
CA 11 HOH   132  2232 1381 HOH   HOH B . 
CA 11 HOH   133  2233 2381 HOH   HOH B . 
CA 11 HOH   134  2234 1376 HOH   HOH B . 
CA 11 HOH   135  2235 146  HOH   HOH B . 
CA 11 HOH   136  2236 23   HOH   HOH B . 
CA 11 HOH   137  2237 383  HOH   HOH B . 
CA 11 HOH   138  2238 271  HOH   HOH B . 
CA 11 HOH   139  2239 44   HOH   HOH B . 
CA 11 HOH   140  2240 427  HOH   HOH B . 
CA 11 HOH   141  2241 1021 HOH   HOH B . 
CA 11 HOH   142  2242 1787 HOH   HOH B . 
CA 11 HOH   143  2243 1491 HOH   HOH B . 
CA 11 HOH   144  2244 1007 HOH   HOH B . 
CA 11 HOH   145  2245 508  HOH   HOH B . 
CA 11 HOH   146  2246 224  HOH   HOH B . 
CA 11 HOH   147  2247 742  HOH   HOH B . 
CA 11 HOH   148  2248 950  HOH   HOH B . 
CA 11 HOH   149  2249 2029 HOH   HOH B . 
CA 11 HOH   150  2250 1455 HOH   HOH B . 
CA 11 HOH   151  2251 2316 HOH   HOH B . 
CA 11 HOH   152  2252 1230 HOH   HOH B . 
CA 11 HOH   153  2253 2088 HOH   HOH B . 
CA 11 HOH   154  2254 225  HOH   HOH B . 
CA 11 HOH   155  2255 237  HOH   HOH B . 
CA 11 HOH   156  2256 2461 HOH   HOH B . 
CA 11 HOH   157  2257 753  HOH   HOH B . 
CA 11 HOH   158  2258 1416 HOH   HOH B . 
CA 11 HOH   159  2259 252  HOH   HOH B . 
CA 11 HOH   160  2260 1803 HOH   HOH B . 
CA 11 HOH   161  2261 91   HOH   HOH B . 
CA 11 HOH   162  2262 959  HOH   HOH B . 
CA 11 HOH   163  2263 300  HOH   HOH B . 
CA 11 HOH   164  2264 1197 HOH   HOH B . 
CA 11 HOH   165  2265 663  HOH   HOH B . 
CA 11 HOH   166  2266 813  HOH   HOH B . 
CA 11 HOH   167  2267 790  HOH   HOH B . 
CA 11 HOH   168  2268 1380 HOH   HOH B . 
CA 11 HOH   169  2269 104  HOH   HOH B . 
CA 11 HOH   170  2270 658  HOH   HOH B . 
CA 11 HOH   171  2271 2557 HOH   HOH B . 
CA 11 HOH   172  2272 32   HOH   HOH B . 
CA 11 HOH   173  2273 791  HOH   HOH B . 
CA 11 HOH   174  2274 338  HOH   HOH B . 
CA 11 HOH   175  2275 1072 HOH   HOH B . 
CA 11 HOH   176  2276 275  HOH   HOH B . 
CA 11 HOH   177  2277 2675 HOH   HOH B . 
CA 11 HOH   178  2278 1527 HOH   HOH B . 
CA 11 HOH   179  2279 894  HOH   HOH B . 
CA 11 HOH   180  2280 449  HOH   HOH B . 
CA 11 HOH   181  2281 890  HOH   HOH B . 
CA 11 HOH   182  2282 1415 HOH   HOH B . 
CA 11 HOH   183  2283 703  HOH   HOH B . 
CA 11 HOH   184  2284 1184 HOH   HOH B . 
CA 11 HOH   185  2285 443  HOH   HOH B . 
CA 11 HOH   186  2286 2632 HOH   HOH B . 
CA 11 HOH   187  2287 89   HOH   HOH B . 
CA 11 HOH   188  2288 2522 HOH   HOH B . 
CA 11 HOH   189  2289 344  HOH   HOH B . 
CA 11 HOH   190  2290 2202 HOH   HOH B . 
CA 11 HOH   191  2291 838  HOH   HOH B . 
CA 11 HOH   192  2292 2013 HOH   HOH B . 
CA 11 HOH   193  2293 111  HOH   HOH B . 
CA 11 HOH   194  2294 394  HOH   HOH B . 
CA 11 HOH   195  2295 128  HOH   HOH B . 
CA 11 HOH   196  2296 41   HOH   HOH B . 
CA 11 HOH   197  2297 197  HOH   HOH B . 
CA 11 HOH   198  2298 1089 HOH   HOH B . 
CA 11 HOH   199  2299 482  HOH   HOH B . 
CA 11 HOH   200  2300 26   HOH   HOH B . 
CA 11 HOH   201  2301 640  HOH   HOH B . 
CA 11 HOH   202  2302 713  HOH   HOH B . 
CA 11 HOH   203  2303 347  HOH   HOH B . 
CA 11 HOH   204  2304 1726 HOH   HOH B . 
CA 11 HOH   205  2305 114  HOH   HOH B . 
CA 11 HOH   206  2306 359  HOH   HOH B . 
CA 11 HOH   207  2307 1284 HOH   HOH B . 
CA 11 HOH   208  2308 105  HOH   HOH B . 
CA 11 HOH   209  2309 666  HOH   HOH B . 
CA 11 HOH   210  2310 1266 HOH   HOH B . 
CA 11 HOH   211  2311 167  HOH   HOH B . 
CA 11 HOH   212  2312 365  HOH   HOH B . 
CA 11 HOH   213  2313 2357 HOH   HOH B . 
CA 11 HOH   214  2314 69   HOH   HOH B . 
CA 11 HOH   215  2315 1510 HOH   HOH B . 
CA 11 HOH   216  2316 2417 HOH   HOH B . 
CA 11 HOH   217  2317 86   HOH   HOH B . 
CA 11 HOH   218  2318 1136 HOH   HOH B . 
CA 11 HOH   219  2319 1807 HOH   HOH B . 
CA 11 HOH   220  2320 538  HOH   HOH B . 
CA 11 HOH   221  2321 21   HOH   HOH B . 
CA 11 HOH   222  2322 872  HOH   HOH B . 
CA 11 HOH   223  2323 1608 HOH   HOH B . 
CA 11 HOH   224  2324 140  HOH   HOH B . 
CA 11 HOH   225  2325 166  HOH   HOH B . 
CA 11 HOH   226  2326 67   HOH   HOH B . 
CA 11 HOH   227  2327 1173 HOH   HOH B . 
CA 11 HOH   228  2328 674  HOH   HOH B . 
CA 11 HOH   229  2329 144  HOH   HOH B . 
CA 11 HOH   230  2330 150  HOH   HOH B . 
CA 11 HOH   231  2331 218  HOH   HOH B . 
CA 11 HOH   232  2332 1313 HOH   HOH B . 
CA 11 HOH   233  2333 475  HOH   HOH B . 
CA 11 HOH   234  2334 116  HOH   HOH B . 
CA 11 HOH   235  2335 1299 HOH   HOH B . 
CA 11 HOH   236  2336 2727 HOH   HOH B . 
CA 11 HOH   237  2337 1131 HOH   HOH B . 
CA 11 HOH   238  2338 1211 HOH   HOH B . 
CA 11 HOH   239  2339 588  HOH   HOH B . 
CA 11 HOH   240  2340 635  HOH   HOH B . 
CA 11 HOH   241  2341 906  HOH   HOH B . 
CA 11 HOH   242  2342 2604 HOH   HOH B . 
CA 11 HOH   243  2343 2363 HOH   HOH B . 
CA 11 HOH   244  2344 1604 HOH   HOH B . 
CA 11 HOH   245  2345 1847 HOH   HOH B . 
CA 11 HOH   246  2346 1086 HOH   HOH B . 
CA 11 HOH   247  2347 2433 HOH   HOH B . 
CA 11 HOH   248  2348 923  HOH   HOH B . 
CA 11 HOH   249  2349 851  HOH   HOH B . 
CA 11 HOH   250  2350 541  HOH   HOH B . 
CA 11 HOH   251  2351 930  HOH   HOH B . 
CA 11 HOH   252  2352 608  HOH   HOH B . 
CA 11 HOH   253  2353 244  HOH   HOH B . 
CA 11 HOH   254  2354 2550 HOH   HOH B . 
CA 11 HOH   255  2355 37   HOH   HOH B . 
CA 11 HOH   256  2356 2548 HOH   HOH B . 
CA 11 HOH   257  2357 1254 HOH   HOH B . 
CA 11 HOH   258  2358 2526 HOH   HOH B . 
CA 11 HOH   259  2359 98   HOH   HOH B . 
CA 11 HOH   260  2360 929  HOH   HOH B . 
CA 11 HOH   261  2361 269  HOH   HOH B . 
CA 11 HOH   262  2362 1453 HOH   HOH B . 
CA 11 HOH   263  2363 620  HOH   HOH B . 
CA 11 HOH   264  2364 1829 HOH   HOH B . 
CA 11 HOH   265  2365 170  HOH   HOH B . 
CA 11 HOH   266  2366 1821 HOH   HOH B . 
CA 11 HOH   267  2367 648  HOH   HOH B . 
CA 11 HOH   268  2368 492  HOH   HOH B . 
CA 11 HOH   269  2369 1005 HOH   HOH B . 
CA 11 HOH   270  2370 1564 HOH   HOH B . 
CA 11 HOH   271  2371 426  HOH   HOH B . 
CA 11 HOH   272  2372 190  HOH   HOH B . 
CA 11 HOH   273  2373 1119 HOH   HOH B . 
CA 11 HOH   274  2374 280  HOH   HOH B . 
CA 11 HOH   275  2375 1522 HOH   HOH B . 
CA 11 HOH   276  2376 2264 HOH   HOH B . 
CA 11 HOH   277  2377 1987 HOH   HOH B . 
CA 11 HOH   278  2378 15   HOH   HOH B . 
CA 11 HOH   279  2379 316  HOH   HOH B . 
CA 11 HOH   280  2380 55   HOH   HOH B . 
CA 11 HOH   281  2381 1035 HOH   HOH B . 
CA 11 HOH   282  2382 2052 HOH   HOH B . 
CA 11 HOH   283  2383 1281 HOH   HOH B . 
CA 11 HOH   284  2384 2482 HOH   HOH B . 
CA 11 HOH   285  2385 1824 HOH   HOH B . 
CA 11 HOH   286  2386 546  HOH   HOH B . 
CA 11 HOH   287  2387 1597 HOH   HOH B . 
CA 11 HOH   288  2388 1743 HOH   HOH B . 
CA 11 HOH   289  2389 804  HOH   HOH B . 
CA 11 HOH   290  2390 6    HOH   HOH B . 
CA 11 HOH   291  2391 10   HOH   HOH B . 
CA 11 HOH   292  2392 1321 HOH   HOH B . 
CA 11 HOH   293  2393 805  HOH   HOH B . 
CA 11 HOH   294  2394 158  HOH   HOH B . 
CA 11 HOH   295  2395 311  HOH   HOH B . 
CA 11 HOH   296  2396 317  HOH   HOH B . 
CA 11 HOH   297  2397 895  HOH   HOH B . 
CA 11 HOH   298  2398 1737 HOH   HOH B . 
CA 11 HOH   299  2399 716  HOH   HOH B . 
CA 11 HOH   300  2400 137  HOH   HOH B . 
CA 11 HOH   301  2401 1588 HOH   HOH B . 
CA 11 HOH   302  2402 1692 HOH   HOH B . 
CA 11 HOH   303  2403 2194 HOH   HOH B . 
CA 11 HOH   304  2404 529  HOH   HOH B . 
CA 11 HOH   305  2405 1756 HOH   HOH B . 
CA 11 HOH   306  2406 329  HOH   HOH B . 
CA 11 HOH   307  2407 1520 HOH   HOH B . 
CA 11 HOH   308  2408 1788 HOH   HOH B . 
CA 11 HOH   309  2409 1040 HOH   HOH B . 
CA 11 HOH   310  2410 249  HOH   HOH B . 
CA 11 HOH   311  2411 2002 HOH   HOH B . 
CA 11 HOH   312  2412 1746 HOH   HOH B . 
CA 11 HOH   313  2413 1936 HOH   HOH B . 
CA 11 HOH   314  2414 63   HOH   HOH B . 
CA 11 HOH   315  2415 153  HOH   HOH B . 
CA 11 HOH   316  2416 981  HOH   HOH B . 
CA 11 HOH   317  2417 250  HOH   HOH B . 
CA 11 HOH   318  2418 1763 HOH   HOH B . 
CA 11 HOH   319  2419 2629 HOH   HOH B . 
CA 11 HOH   320  2420 1232 HOH   HOH B . 
CA 11 HOH   321  2421 107  HOH   HOH B . 
CA 11 HOH   322  2422 957  HOH   HOH B . 
CA 11 HOH   323  2423 112  HOH   HOH B . 
CA 11 HOH   324  2424 767  HOH   HOH B . 
CA 11 HOH   325  2425 2379 HOH   HOH B . 
CA 11 HOH   326  2426 548  HOH   HOH B . 
CA 11 HOH   327  2427 2321 HOH   HOH B . 
CA 11 HOH   328  2428 882  HOH   HOH B . 
CA 11 HOH   329  2429 47   HOH   HOH B . 
CA 11 HOH   330  2430 763  HOH   HOH B . 
CA 11 HOH   331  2431 1806 HOH   HOH B . 
CA 11 HOH   332  2432 1306 HOH   HOH B . 
CA 11 HOH   333  2433 174  HOH   HOH B . 
CA 11 HOH   334  2434 2540 HOH   HOH B . 
CA 11 HOH   335  2435 209  HOH   HOH B . 
CA 11 HOH   336  2436 2071 HOH   HOH B . 
CA 11 HOH   337  2437 1318 HOH   HOH B . 
CA 11 HOH   338  2438 719  HOH   HOH B . 
CA 11 HOH   339  2439 2374 HOH   HOH B . 
CA 11 HOH   340  2440 1121 HOH   HOH B . 
CA 11 HOH   341  2441 643  HOH   HOH B . 
CA 11 HOH   342  2442 1312 HOH   HOH B . 
CA 11 HOH   343  2443 265  HOH   HOH B . 
CA 11 HOH   344  2444 697  HOH   HOH B . 
CA 11 HOH   345  2445 571  HOH   HOH B . 
CA 11 HOH   346  2446 272  HOH   HOH B . 
CA 11 HOH   347  2447 156  HOH   HOH B . 
CA 11 HOH   348  2448 903  HOH   HOH B . 
CA 11 HOH   349  2449 1721 HOH   HOH B . 
CA 11 HOH   350  2450 1879 HOH   HOH B . 
CA 11 HOH   351  2451 2412 HOH   HOH B . 
CA 11 HOH   352  2452 1103 HOH   HOH B . 
CA 11 HOH   353  2453 157  HOH   HOH B . 
CA 11 HOH   354  2454 357  HOH   HOH B . 
CA 11 HOH   355  2455 754  HOH   HOH B . 
CA 11 HOH   356  2456 1003 HOH   HOH B . 
CA 11 HOH   357  2457 204  HOH   HOH B . 
CA 11 HOH   358  2458 11   HOH   HOH B . 
CA 11 HOH   359  2459 291  HOH   HOH B . 
CA 11 HOH   360  2460 1006 HOH   HOH B . 
CA 11 HOH   361  2461 358  HOH   HOH B . 
CA 11 HOH   362  2462 2    HOH   HOH B . 
CA 11 HOH   363  2463 1494 HOH   HOH B . 
CA 11 HOH   364  2464 415  HOH   HOH B . 
CA 11 HOH   365  2465 591  HOH   HOH B . 
CA 11 HOH   366  2466 81   HOH   HOH B . 
CA 11 HOH   367  2467 103  HOH   HOH B . 
CA 11 HOH   368  2468 118  HOH   HOH B . 
CA 11 HOH   369  2469 499  HOH   HOH B . 
CA 11 HOH   370  2470 2706 HOH   HOH B . 
CA 11 HOH   371  2471 8    HOH   HOH B . 
CA 11 HOH   372  2472 46   HOH   HOH B . 
CA 11 HOH   373  2473 1437 HOH   HOH B . 
CA 11 HOH   374  2474 2564 HOH   HOH B . 
CA 11 HOH   375  2475 423  HOH   HOH B . 
CA 11 HOH   376  2476 1755 HOH   HOH B . 
CA 11 HOH   377  2477 2695 HOH   HOH B . 
CA 11 HOH   378  2478 477  HOH   HOH B . 
CA 11 HOH   379  2479 25   HOH   HOH B . 
CA 11 HOH   380  2480 854  HOH   HOH B . 
CA 11 HOH   381  2481 1472 HOH   HOH B . 
CA 11 HOH   382  2482 2647 HOH   HOH B . 
CA 11 HOH   383  2483 213  HOH   HOH B . 
CA 11 HOH   384  2484 203  HOH   HOH B . 
CA 11 HOH   385  2485 2172 HOH   HOH B . 
CA 11 HOH   386  2486 974  HOH   HOH B . 
CA 11 HOH   387  2487 1114 HOH   HOH B . 
CA 11 HOH   388  2488 1505 HOH   HOH B . 
CA 11 HOH   389  2489 1948 HOH   HOH B . 
CA 11 HOH   390  2490 1750 HOH   HOH B . 
CA 11 HOH   391  2491 662  HOH   HOH B . 
CA 11 HOH   392  2492 677  HOH   HOH B . 
CA 11 HOH   393  2493 1094 HOH   HOH B . 
CA 11 HOH   394  2494 116  HOH   HOH B . 
CA 11 HOH   395  2495 196  HOH   HOH B . 
CA 11 HOH   396  2496 165  HOH   HOH B . 
CA 11 HOH   397  2497 436  HOH   HOH B . 
CA 11 HOH   398  2498 1465 HOH   HOH B . 
CA 11 HOH   399  2499 270  HOH   HOH B . 
CA 11 HOH   400  2500 721  HOH   HOH B . 
CA 11 HOH   401  2501 2236 HOH   HOH B . 
CA 11 HOH   402  2502 2191 HOH   HOH B . 
CA 11 HOH   403  2503 1586 HOH   HOH B . 
CA 11 HOH   404  2504 340  HOH   HOH B . 
CA 11 HOH   405  2505 1405 HOH   HOH B . 
CA 11 HOH   406  2506 1105 HOH   HOH B . 
CA 11 HOH   407  2507 18   HOH   HOH B . 
CA 11 HOH   408  2508 303  HOH   HOH B . 
CA 11 HOH   409  2509 641  HOH   HOH B . 
CA 11 HOH   410  2510 9    HOH   HOH B . 
CA 11 HOH   411  2511 1560 HOH   HOH B . 
CA 11 HOH   412  2512 381  HOH   HOH B . 
CA 11 HOH   413  2513 1169 HOH   HOH B . 
CA 11 HOH   414  2514 349  HOH   HOH B . 
CA 11 HOH   415  2515 85   HOH   HOH B . 
CA 11 HOH   416  2516 532  HOH   HOH B . 
CA 11 HOH   417  2517 2464 HOH   HOH B . 
CA 11 HOH   418  2518 781  HOH   HOH B . 
CA 11 HOH   419  2519 2356 HOH   HOH B . 
CA 11 HOH   420  2520 2592 HOH   HOH B . 
CA 11 HOH   421  2521 422  HOH   HOH B . 
CA 11 HOH   422  2522 302  HOH   HOH B . 
CA 11 HOH   423  2523 107  HOH   HOH B . 
CA 11 HOH   424  2524 1256 HOH   HOH B . 
CA 11 HOH   425  2525 254  HOH   HOH B . 
CA 11 HOH   426  2526 1796 HOH   HOH B . 
CA 11 HOH   427  2527 723  HOH   HOH B . 
CA 11 HOH   428  2528 327  HOH   HOH B . 
CA 11 HOH   429  2529 516  HOH   HOH B . 
CA 11 HOH   430  2530 2266 HOH   HOH B . 
CA 11 HOH   431  2531 2181 HOH   HOH B . 
CA 11 HOH   432  2532 16   HOH   HOH B . 
CA 11 HOH   433  2533 2380 HOH   HOH B . 
CA 11 HOH   434  2534 1223 HOH   HOH B . 
CA 11 HOH   435  2535 1970 HOH   HOH B . 
CA 11 HOH   436  2536 2568 HOH   HOH B . 
CA 11 HOH   437  2537 1795 HOH   HOH B . 
CA 11 HOH   438  2538 1267 HOH   HOH B . 
CA 11 HOH   439  2539 2197 HOH   HOH B . 
CA 11 HOH   440  2540 765  HOH   HOH B . 
CA 11 HOH   441  2541 911  HOH   HOH B . 
CA 11 HOH   442  2542 31   HOH   HOH B . 
CA 11 HOH   443  2543 655  HOH   HOH B . 
CA 11 HOH   444  2544 1195 HOH   HOH B . 
CA 11 HOH   445  2545 613  HOH   HOH B . 
CA 11 HOH   446  2546 428  HOH   HOH B . 
CA 11 HOH   447  2547 1082 HOH   HOH B . 
CA 11 HOH   448  2548 1115 HOH   HOH B . 
CA 11 HOH   449  2549 2421 HOH   HOH B . 
CA 11 HOH   450  2550 232  HOH   HOH B . 
CA 11 HOH   451  2551 109  HOH   HOH B . 
CA 11 HOH   452  2552 101  HOH   HOH B . 
CA 11 HOH   453  2553 217  HOH   HOH B . 
CA 11 HOH   454  2554 778  HOH   HOH B . 
CA 11 HOH   455  2555 1296 HOH   HOH B . 
CA 11 HOH   456  2556 2616 HOH   HOH B . 
CA 11 HOH   457  2557 970  HOH   HOH B . 
CA 11 HOH   458  2558 70   HOH   HOH B . 
CA 11 HOH   459  2559 1628 HOH   HOH B . 
CA 11 HOH   460  2560 30   HOH   HOH B . 
CA 11 HOH   461  2561 130  HOH   HOH B . 
CA 11 HOH   462  2562 124  HOH   HOH B . 
CA 11 HOH   463  2563 633  HOH   HOH B . 
CA 11 HOH   464  2564 1162 HOH   HOH B . 
CA 11 HOH   465  2565 1501 HOH   HOH B . 
CA 11 HOH   466  2566 2716 HOH   HOH B . 
CA 11 HOH   467  2567 704  HOH   HOH B . 
CA 11 HOH   468  2568 2575 HOH   HOH B . 
CA 11 HOH   469  2569 139  HOH   HOH B . 
CA 11 HOH   470  2570 403  HOH   HOH B . 
CA 11 HOH   471  2571 2530 HOH   HOH B . 
CA 11 HOH   472  2572 1191 HOH   HOH B . 
CA 11 HOH   473  2573 471  HOH   HOH B . 
CA 11 HOH   474  2574 1    HOH   HOH B . 
CA 11 HOH   475  2575 470  HOH   HOH B . 
CA 11 HOH   476  2576 100  HOH   HOH B . 
CA 11 HOH   477  2577 2054 HOH   HOH B . 
CA 11 HOH   478  2578 1906 HOH   HOH B . 
CA 11 HOH   479  2579 915  HOH   HOH B . 
CA 11 HOH   480  2580 1203 HOH   HOH B . 
CA 11 HOH   481  2581 361  HOH   HOH B . 
CA 11 HOH   482  2582 1916 HOH   HOH B . 
CA 11 HOH   483  2583 1493 HOH   HOH B . 
CA 11 HOH   484  2584 87   HOH   HOH B . 
CA 11 HOH   485  2585 212  HOH   HOH B . 
CA 11 HOH   486  2586 1905 HOH   HOH B . 
CA 11 HOH   487  2587 752  HOH   HOH B . 
CA 11 HOH   488  2588 2387 HOH   HOH B . 
CA 11 HOH   489  2589 296  HOH   HOH B . 
CA 11 HOH   490  2590 615  HOH   HOH B . 
CA 11 HOH   491  2591 138  HOH   HOH B . 
CA 11 HOH   492  2592 120  HOH   HOH B . 
CA 11 HOH   493  2593 2672 HOH   HOH B . 
CA 11 HOH   494  2594 328  HOH   HOH B . 
CA 11 HOH   495  2595 88   HOH   HOH B . 
CA 11 HOH   496  2596 330  HOH   HOH B . 
CA 11 HOH   497  2597 733  HOH   HOH B . 
CA 11 HOH   498  2598 685  HOH   HOH B . 
CA 11 HOH   499  2599 644  HOH   HOH B . 
CA 11 HOH   500  2600 1665 HOH   HOH B . 
CA 11 HOH   501  2601 1015 HOH   HOH B . 
CA 11 HOH   502  2602 2014 HOH   HOH B . 
CA 11 HOH   503  2603 690  HOH   HOH B . 
CA 11 HOH   504  2604 283  HOH   HOH B . 
CA 11 HOH   505  2605 680  HOH   HOH B . 
CA 11 HOH   506  2606 387  HOH   HOH B . 
CA 11 HOH   507  2607 905  HOH   HOH B . 
CA 11 HOH   508  2608 1122 HOH   HOH B . 
CA 11 HOH   509  2609 14   HOH   HOH B . 
CA 11 HOH   510  2610 1029 HOH   HOH B . 
CA 11 HOH   511  2611 1215 HOH   HOH B . 
CA 11 HOH   512  2612 1233 HOH   HOH B . 
CA 11 HOH   513  2613 1083 HOH   HOH B . 
CA 11 HOH   514  2614 182  HOH   HOH B . 
CA 11 HOH   515  2615 12   HOH   HOH B . 
CA 11 HOH   516  2616 189  HOH   HOH B . 
CA 11 HOH   517  2617 73   HOH   HOH B . 
CA 11 HOH   518  2618 1543 HOH   HOH B . 
CA 11 HOH   519  2619 154  HOH   HOH B . 
CA 11 HOH   520  2620 1481 HOH   HOH B . 
CA 11 HOH   521  2621 668  HOH   HOH B . 
CA 11 HOH   522  2622 857  HOH   HOH B . 
CA 11 HOH   523  2623 625  HOH   HOH B . 
CA 11 HOH   524  2624 17   HOH   HOH B . 
CA 11 HOH   525  2625 1352 HOH   HOH B . 
CA 11 HOH   526  2626 112  HOH   HOH B . 
CA 11 HOH   527  2627 58   HOH   HOH B . 
CA 11 HOH   528  2628 1559 HOH   HOH B . 
CA 11 HOH   529  2629 28   HOH   HOH B . 
CA 11 HOH   530  2630 526  HOH   HOH B . 
CA 11 HOH   531  2631 45   HOH   HOH B . 
CA 11 HOH   532  2632 2179 HOH   HOH B . 
CA 11 HOH   533  2633 566  HOH   HOH B . 
CA 11 HOH   534  2634 396  HOH   HOH B . 
CA 11 HOH   535  2635 43   HOH   HOH B . 
CA 11 HOH   536  2636 398  HOH   HOH B . 
CA 11 HOH   537  2637 207  HOH   HOH B . 
CA 11 HOH   538  2638 684  HOH   HOH B . 
CA 11 HOH   539  2639 875  HOH   HOH B . 
CA 11 HOH   540  2640 989  HOH   HOH B . 
CA 11 HOH   541  2641 1770 HOH   HOH B . 
CA 11 HOH   542  2642 563  HOH   HOH B . 
CA 11 HOH   543  2643 700  HOH   HOH B . 
CA 11 HOH   544  2644 1362 HOH   HOH B . 
CA 11 HOH   545  2645 276  HOH   HOH B . 
CA 11 HOH   546  2646 483  HOH   HOH B . 
CA 11 HOH   547  2647 162  HOH   HOH B . 
CA 11 HOH   548  2648 958  HOH   HOH B . 
CA 11 HOH   549  2649 2269 HOH   HOH B . 
CA 11 HOH   550  2650 827  HOH   HOH B . 
CA 11 HOH   551  2651 226  HOH   HOH B . 
CA 11 HOH   552  2652 1271 HOH   HOH B . 
CA 11 HOH   553  2653 2085 HOH   HOH B . 
CA 11 HOH   554  2654 498  HOH   HOH B . 
CA 11 HOH   555  2655 1825 HOH   HOH B . 
CA 11 HOH   556  2656 2241 HOH   HOH B . 
CA 11 HOH   557  2657 893  HOH   HOH B . 
CA 11 HOH   558  2658 406  HOH   HOH B . 
CA 11 HOH   559  2659 325  HOH   HOH B . 
CA 11 HOH   560  2660 925  HOH   HOH B . 
CA 11 HOH   561  2661 1087 HOH   HOH B . 
CA 11 HOH   562  2662 1946 HOH   HOH B . 
CA 11 HOH   563  2663 842  HOH   HOH B . 
CA 11 HOH   564  2664 7    HOH   HOH B . 
CA 11 HOH   565  2665 1079 HOH   HOH B . 
CA 11 HOH   566  2666 534  HOH   HOH B . 
CA 11 HOH   567  2667 786  HOH   HOH B . 
CA 11 HOH   568  2668 3    HOH   HOH B . 
CA 11 HOH   569  2669 1526 HOH   HOH B . 
CA 11 HOH   570  2670 2725 HOH   HOH B . 
CA 11 HOH   571  2671 286  HOH   HOH B . 
CA 11 HOH   572  2672 918  HOH   HOH B . 
CA 11 HOH   573  2673 155  HOH   HOH B . 
CA 11 HOH   574  2674 489  HOH   HOH B . 
CA 11 HOH   575  2675 1286 HOH   HOH B . 
CA 11 HOH   576  2676 2684 HOH   HOH B . 
CA 11 HOH   577  2677 355  HOH   HOH B . 
CA 11 HOH   578  2678 77   HOH   HOH B . 
CA 11 HOH   579  2679 29   HOH   HOH B . 
CA 11 HOH   580  2680 1567 HOH   HOH B . 
CA 11 HOH   581  2681 599  HOH   HOH B . 
CA 11 HOH   582  2682 942  HOH   HOH B . 
CA 11 HOH   583  2683 274  HOH   HOH B . 
CA 11 HOH   584  2684 1413 HOH   HOH B . 
CA 11 HOH   585  2685 517  HOH   HOH B . 
CA 11 HOH   586  2686 78   HOH   HOH B . 
CA 11 HOH   587  2687 211  HOH   HOH B . 
CA 11 HOH   588  2688 368  HOH   HOH B . 
CA 11 HOH   589  2689 141  HOH   HOH B . 
CA 11 HOH   590  2690 2687 HOH   HOH B . 
CA 11 HOH   591  2691 147  HOH   HOH B . 
CA 11 HOH   592  2692 191  HOH   HOH B . 
CA 11 HOH   593  2693 214  HOH   HOH B . 
CA 11 HOH   594  2694 672  HOH   HOH B . 
CA 11 HOH   595  2695 2456 HOH   HOH B . 
CA 11 HOH   596  2696 884  HOH   HOH B . 
CA 11 HOH   597  2697 1285 HOH   HOH B . 
CA 11 HOH   598  2698 1811 HOH   HOH B . 
CA 11 HOH   599  2699 431  HOH   HOH B . 
CA 11 HOH   600  2700 748  HOH   HOH B . 
CA 11 HOH   601  2701 108  HOH   HOH B . 
CA 11 HOH   602  2702 179  HOH   HOH B . 
CA 11 HOH   603  2703 1085 HOH   HOH B . 
CA 11 HOH   604  2704 234  HOH   HOH B . 
CA 11 HOH   605  2705 281  HOH   HOH B . 
CA 11 HOH   606  2706 682  HOH   HOH B . 
CA 11 HOH   607  2707 1688 HOH   HOH B . 
CA 11 HOH   608  2708 260  HOH   HOH B . 
CA 11 HOH   609  2709 1390 HOH   HOH B . 
CA 11 HOH   610  2710 409  HOH   HOH B . 
CA 11 HOH   611  2711 1542 HOH   HOH B . 
CA 11 HOH   612  2712 48   HOH   HOH B . 
CA 11 HOH   613  2713 873  HOH   HOH B . 
CA 11 HOH   614  2714 52   HOH   HOH B . 
CA 11 HOH   615  2715 743  HOH   HOH B . 
CA 11 HOH   616  2716 246  HOH   HOH B . 
CA 11 HOH   617  2717 496  HOH   HOH B . 
CA 11 HOH   618  2718 629  HOH   HOH B . 
CA 11 HOH   619  2719 2449 HOH   HOH B . 
CA 11 HOH   620  2720 832  HOH   HOH B . 
CA 11 HOH   621  2721 902  HOH   HOH B . 
CA 11 HOH   622  2722 35   HOH   HOH B . 
CA 11 HOH   623  2723 1650 HOH   HOH B . 
CA 11 HOH   624  2724 692  HOH   HOH B . 
CA 11 HOH   625  2725 720  HOH   HOH B . 
CA 11 HOH   626  2726 301  HOH   HOH B . 
CA 11 HOH   627  2727 2273 HOH   HOH B . 
CA 11 HOH   628  2728 2231 HOH   HOH B . 
CA 11 HOH   629  2729 2322 HOH   HOH B . 
CA 11 HOH   630  2730 1257 HOH   HOH B . 
CA 11 HOH   631  2731 1292 HOH   HOH B . 
CA 11 HOH   632  2732 507  HOH   HOH B . 
CA 11 HOH   633  2733 2505 HOH   HOH B . 
CA 11 HOH   634  2734 1921 HOH   HOH B . 
CA 11 HOH   635  2735 2336 HOH   HOH B . 
CA 11 HOH   636  2736 1255 HOH   HOH B . 
CA 11 HOH   637  2737 653  HOH   HOH B . 
CA 11 HOH   638  2738 1658 HOH   HOH B . 
CA 11 HOH   639  2739 1052 HOH   HOH B . 
CA 11 HOH   640  2740 97   HOH   HOH B . 
CA 11 HOH   641  2741 709  HOH   HOH B . 
CA 11 HOH   642  2742 258  HOH   HOH B . 
CA 11 HOH   643  2743 927  HOH   HOH B . 
CA 11 HOH   644  2744 1759 HOH   HOH B . 
CA 11 HOH   645  2745 181  HOH   HOH B . 
CA 11 HOH   646  2746 783  HOH   HOH B . 
CA 11 HOH   647  2747 855  HOH   HOH B . 
CA 11 HOH   648  2748 1129 HOH   HOH B . 
CA 11 HOH   649  2749 95   HOH   HOH B . 
CA 11 HOH   650  2750 811  HOH   HOH B . 
CA 11 HOH   651  2751 484  HOH   HOH B . 
CA 11 HOH   652  2752 1898 HOH   HOH B . 
CA 11 HOH   653  2753 123  HOH   HOH B . 
CA 11 HOH   654  2754 533  HOH   HOH B . 
CA 11 HOH   655  2755 216  HOH   HOH B . 
CA 11 HOH   656  2756 310  HOH   HOH B . 
CA 11 HOH   657  2757 335  HOH   HOH B . 
CA 11 HOH   658  2758 759  HOH   HOH B . 
CA 11 HOH   659  2759 908  HOH   HOH B . 
CA 11 HOH   660  2760 85   HOH   HOH B . 
CA 11 HOH   661  2761 799  HOH   HOH B . 
CA 11 HOH   662  2762 5    HOH   HOH B . 
CA 11 HOH   663  2763 1288 HOH   HOH B . 
CA 11 HOH   664  2764 1320 HOH   HOH B . 
CA 11 HOH   665  2765 2708 HOH   HOH B . 
CA 11 HOH   666  2766 1054 HOH   HOH B . 
CA 11 HOH   667  2767 1448 HOH   HOH B . 
CA 11 HOH   668  2768 1019 HOH   HOH B . 
CA 11 HOH   669  2769 2432 HOH   HOH B . 
CA 11 HOH   670  2770 476  HOH   HOH B . 
CA 11 HOH   671  2771 255  HOH   HOH B . 
CA 11 HOH   672  2772 228  HOH   HOH B . 
CA 11 HOH   673  2773 1198 HOH   HOH B . 
CA 11 HOH   674  2774 341  HOH   HOH B . 
CA 11 HOH   675  2775 282  HOH   HOH B . 
CA 11 HOH   676  2776 889  HOH   HOH B . 
CA 11 HOH   677  2777 145  HOH   HOH B . 
CA 11 HOH   678  2778 111  HOH   HOH B . 
CA 11 HOH   679  2779 944  HOH   HOH B . 
CA 11 HOH   680  2780 1124 HOH   HOH B . 
CA 11 HOH   681  2781 1067 HOH   HOH B . 
CA 11 HOH   682  2782 651  HOH   HOH B . 
CA 11 HOH   683  2783 461  HOH   HOH B . 
CA 11 HOH   684  2784 1461 HOH   HOH B . 
CA 11 HOH   685  2785 2065 HOH   HOH B . 
CA 11 HOH   686  2786 2168 HOH   HOH B . 
CA 11 HOH   687  2787 4    HOH   HOH B . 
CA 11 HOH   688  2788 1576 HOH   HOH B . 
CA 11 HOH   689  2789 362  HOH   HOH B . 
CA 11 HOH   690  2790 118  HOH   HOH B . 
CA 11 HOH   691  2791 65   HOH   HOH B . 
CA 11 HOH   692  2792 1100 HOH   HOH B . 
CA 11 HOH   693  2793 279  HOH   HOH B . 
CA 11 HOH   694  2794 2484 HOH   HOH B . 
CA 11 HOH   695  2795 562  HOH   HOH B . 
CA 11 HOH   696  2796 1769 HOH   HOH B . 
CA 11 HOH   697  2797 735  HOH   HOH B . 
CA 11 HOH   698  2798 284  HOH   HOH B . 
CA 11 HOH   699  2799 579  HOH   HOH B . 
CA 11 HOH   700  2800 569  HOH   HOH B . 
CA 11 HOH   701  2801 43   HOH   HOH B . 
CA 11 HOH   702  2802 2483 HOH   HOH B . 
CA 11 HOH   703  2803 1671 HOH   HOH B . 
CA 11 HOH   704  2804 1354 HOH   HOH B . 
CA 11 HOH   705  2805 1515 HOH   HOH B . 
CA 11 HOH   706  2806 2166 HOH   HOH B . 
CA 11 HOH   707  2807 803  HOH   HOH B . 
CA 11 HOH   708  2808 405  HOH   HOH B . 
CA 11 HOH   709  2809 2579 HOH   HOH B . 
CA 11 HOH   710  2810 152  HOH   HOH B . 
CA 11 HOH   711  2811 263  HOH   HOH B . 
CA 11 HOH   712  2812 267  HOH   HOH B . 
CA 11 HOH   713  2813 746  HOH   HOH B . 
CA 11 HOH   714  2814 3    HOH   HOH B . 
CA 11 HOH   715  2815 518  HOH   HOH B . 
CA 11 HOH   716  2816 65   HOH   HOH B . 
CA 11 HOH   717  2817 136  HOH   HOH B . 
CA 11 HOH   718  2818 945  HOH   HOH B . 
CA 11 HOH   719  2819 824  HOH   HOH B . 
CA 11 HOH   720  2820 1695 HOH   HOH B . 
CA 11 HOH   721  2821 1386 HOH   HOH B . 
CA 11 HOH   722  2822 1400 HOH   HOH B . 
CA 11 HOH   723  2823 758  HOH   HOH B . 
CA 11 HOH   724  2824 1832 HOH   HOH B . 
CA 11 HOH   725  2825 2207 HOH   HOH B . 
CA 11 HOH   726  2826 1294 HOH   HOH B . 
CA 11 HOH   727  2827 119  HOH   HOH B . 
CA 11 HOH   728  2828 2429 HOH   HOH B . 
CA 11 HOH   729  2829 416  HOH   HOH B . 
CA 11 HOH   730  2830 168  HOH   HOH B . 
CA 11 HOH   731  2831 598  HOH   HOH B . 
CA 11 HOH   732  2832 1500 HOH   HOH B . 
CA 11 HOH   733  2833 1817 HOH   HOH B . 
CA 11 HOH   734  2834 2208 HOH   HOH B . 
CA 11 HOH   735  2835 590  HOH   HOH B . 
CA 11 HOH   736  2836 113  HOH   HOH B . 
CA 11 HOH   737  2837 472  HOH   HOH B . 
CA 11 HOH   738  2838 66   HOH   HOH B . 
CA 11 HOH   739  2839 1152 HOH   HOH B . 
CA 11 HOH   740  2840 544  HOH   HOH B . 
CA 11 HOH   741  2841 647  HOH   HOH B . 
CA 11 HOH   742  2842 750  HOH   HOH B . 
CA 11 HOH   743  2843 792  HOH   HOH B . 
CA 11 HOH   744  2844 199  HOH   HOH B . 
CA 11 HOH   745  2845 458  HOH   HOH B . 
CA 11 HOH   746  2846 547  HOH   HOH B . 
CA 11 HOH   747  2847 514  HOH   HOH B . 
CA 11 HOH   748  2848 2375 HOH   HOH B . 
CA 11 HOH   749  2849 1431 HOH   HOH B . 
CA 11 HOH   750  2850 1412 HOH   HOH B . 
CA 11 HOH   751  2851 129  HOH   HOH B . 
CA 11 HOH   752  2852 963  HOH   HOH B . 
CA 11 HOH   753  2853 710  HOH   HOH B . 
CA 11 HOH   754  2854 1993 HOH   HOH B . 
CA 11 HOH   755  2855 551  HOH   HOH B . 
CA 11 HOH   756  2856 1592 HOH   HOH B . 
CA 11 HOH   757  2857 638  HOH   HOH B . 
CA 11 HOH   758  2858 312  HOH   HOH B . 
CA 11 HOH   759  2859 500  HOH   HOH B . 
CA 11 HOH   760  2860 1341 HOH   HOH B . 
CA 11 HOH   761  2861 434  HOH   HOH B . 
CA 11 HOH   762  2862 84   HOH   HOH B . 
CA 11 HOH   763  2863 481  HOH   HOH B . 
CA 11 HOH   764  2864 206  HOH   HOH B . 
CA 11 HOH   765  2865 676  HOH   HOH B . 
CA 11 HOH   766  2866 1101 HOH   HOH B . 
CA 11 HOH   767  2867 623  HOH   HOH B . 
CA 11 HOH   768  2868 1147 HOH   HOH B . 
CA 11 HOH   769  2869 841  HOH   HOH B . 
CA 11 HOH   770  2870 513  HOH   HOH B . 
CA 11 HOH   771  2871 1268 HOH   HOH B . 
CA 11 HOH   772  2872 687  HOH   HOH B . 
CA 11 HOH   773  2873 135  HOH   HOH B . 
CA 11 HOH   774  2874 188  HOH   HOH B . 
CA 11 HOH   775  2875 1840 HOH   HOH B . 
CA 11 HOH   776  2876 24   HOH   HOH B . 
CA 11 HOH   777  2877 1892 HOH   HOH B . 
CA 11 HOH   778  2878 2728 HOH   HOH B . 
CA 11 HOH   779  2879 1991 HOH   HOH B . 
CA 11 HOH   780  2880 2078 HOH   HOH B . 
CA 11 HOH   781  2881 1107 HOH   HOH B . 
CA 11 HOH   782  2882 954  HOH   HOH B . 
CA 11 HOH   783  2883 2128 HOH   HOH B . 
CA 11 HOH   784  2884 172  HOH   HOH B . 
CA 11 HOH   785  2885 921  HOH   HOH B . 
CA 11 HOH   786  2886 380  HOH   HOH B . 
CA 11 HOH   787  2887 261  HOH   HOH B . 
CA 11 HOH   788  2888 34   HOH   HOH B . 
CA 11 HOH   789  2889 2506 HOH   HOH B . 
CA 11 HOH   790  2890 2711 HOH   HOH B . 
CA 11 HOH   791  2891 1403 HOH   HOH B . 
CA 11 HOH   792  2892 187  HOH   HOH B . 
CA 11 HOH   793  2893 1468 HOH   HOH B . 
CA 11 HOH   794  2894 2083 HOH   HOH B . 
CA 11 HOH   795  2895 1037 HOH   HOH B . 
CA 11 HOH   796  2896 401  HOH   HOH B . 
CA 11 HOH   797  2897 1096 HOH   HOH B . 
CA 11 HOH   798  2898 444  HOH   HOH B . 
CA 11 HOH   799  2899 2507 HOH   HOH B . 
CA 11 HOH   800  2900 2069 HOH   HOH B . 
CA 11 HOH   801  2901 1783 HOH   HOH B . 
CA 11 HOH   802  2902 448  HOH   HOH B . 
CA 11 HOH   803  2903 391  HOH   HOH B . 
CA 11 HOH   804  2904 1722 HOH   HOH B . 
CA 11 HOH   805  2905 58   HOH   HOH B . 
CA 11 HOH   806  2906 2428 HOH   HOH B . 
CA 11 HOH   807  2907 1816 HOH   HOH B . 
CA 11 HOH   808  2908 1724 HOH   HOH B . 
CA 11 HOH   809  2909 247  HOH   HOH B . 
CA 11 HOH   810  2910 1714 HOH   HOH B . 
CA 11 HOH   811  2911 1099 HOH   HOH B . 
CA 11 HOH   812  2912 163  HOH   HOH B . 
CA 11 HOH   813  2913 1582 HOH   HOH B . 
CA 11 HOH   814  2914 636  HOH   HOH B . 
CA 11 HOH   815  2915 570  HOH   HOH B . 
CA 11 HOH   816  2916 2276 HOH   HOH B . 
CA 11 HOH   817  2917 3    HOH   HOH B . 
CA 11 HOH   818  2918 1482 HOH   HOH B . 
CA 11 HOH   819  2919 1957 HOH   HOH B . 
CA 11 HOH   820  2920 2307 HOH   HOH B . 
CA 11 HOH   821  2921 1396 HOH   HOH B . 
CA 11 HOH   822  2922 1866 HOH   HOH B . 
CA 11 HOH   823  2923 580  HOH   HOH B . 
CA 11 HOH   824  2924 846  HOH   HOH B . 
CA 11 HOH   825  2925 1276 HOH   HOH B . 
CA 11 HOH   826  2926 828  HOH   HOH B . 
CA 11 HOH   827  2927 2355 HOH   HOH B . 
CA 11 HOH   828  2928 2612 HOH   HOH B . 
CA 11 HOH   829  2929 512  HOH   HOH B . 
CA 11 HOH   830  2930 2061 HOH   HOH B . 
CA 11 HOH   831  2931 1439 HOH   HOH B . 
CA 11 HOH   832  2932 414  HOH   HOH B . 
CA 11 HOH   833  2933 1565 HOH   HOH B . 
CA 11 HOH   834  2934 1000 HOH   HOH B . 
CA 11 HOH   835  2935 2001 HOH   HOH B . 
CA 11 HOH   836  2936 319  HOH   HOH B . 
CA 11 HOH   837  2937 2669 HOH   HOH B . 
CA 11 HOH   838  2938 1047 HOH   HOH B . 
CA 11 HOH   839  2939 435  HOH   HOH B . 
CA 11 HOH   840  2940 745  HOH   HOH B . 
CA 11 HOH   841  2941 1516 HOH   HOH B . 
CA 11 HOH   842  2942 113  HOH   HOH B . 
CA 11 HOH   843  2943 333  HOH   HOH B . 
CA 11 HOH   844  2944 1583 HOH   HOH B . 
CA 11 HOH   845  2945 506  HOH   HOH B . 
CA 11 HOH   846  2946 2528 HOH   HOH B . 
CA 11 HOH   847  2947 2585 HOH   HOH B . 
CA 11 HOH   848  2948 880  HOH   HOH B . 
CA 11 HOH   849  2949 1485 HOH   HOH B . 
CA 11 HOH   850  2950 1531 HOH   HOH B . 
CA 11 HOH   851  2951 219  HOH   HOH B . 
CA 11 HOH   852  2952 474  HOH   HOH B . 
CA 11 HOH   853  2953 31   HOH   HOH B . 
CA 11 HOH   854  2954 2310 HOH   HOH B . 
CA 11 HOH   855  2955 98   HOH   HOH B . 
CA 11 HOH   856  2956 1580 HOH   HOH B . 
CA 11 HOH   857  2957 1622 HOH   HOH B . 
CA 11 HOH   858  2958 1185 HOH   HOH B . 
CA 11 HOH   859  2959 2696 HOH   HOH B . 
CA 11 HOH   860  2960 2028 HOH   HOH B . 
CA 11 HOH   861  2961 2565 HOH   HOH B . 
CA 11 HOH   862  2962 537  HOH   HOH B . 
CA 11 HOH   863  2963 1458 HOH   HOH B . 
CA 11 HOH   864  2964 2045 HOH   HOH B . 
CA 11 HOH   865  2965 1475 HOH   HOH B . 
CA 11 HOH   866  2966 505  HOH   HOH B . 
CA 11 HOH   867  2967 229  HOH   HOH B . 
CA 11 HOH   868  2968 718  HOH   HOH B . 
CA 11 HOH   869  2969 1307 HOH   HOH B . 
CA 11 HOH   870  2970 2457 HOH   HOH B . 
CA 11 HOH   871  2971 1287 HOH   HOH B . 
CA 11 HOH   872  2972 856  HOH   HOH B . 
CA 11 HOH   873  2973 2434 HOH   HOH B . 
CA 11 HOH   874  2974 36   HOH   HOH B . 
CA 11 HOH   875  2975 2624 HOH   HOH B . 
CA 11 HOH   876  2976 186  HOH   HOH B . 
CA 11 HOH   877  2977 726  HOH   HOH B . 
CA 11 HOH   878  2978 16   HOH   HOH B . 
CA 11 HOH   879  2979 1117 HOH   HOH B . 
CA 11 HOH   880  2980 2650 HOH   HOH B . 
CA 11 HOH   881  2981 278  HOH   HOH B . 
CA 11 HOH   882  2982 1    HOH   HOH B . 
CA 11 HOH   883  2983 86   HOH   HOH B . 
CA 11 HOH   884  2984 1259 HOH   HOH B . 
CA 11 HOH   885  2985 2234 HOH   HOH B . 
CA 11 HOH   886  2986 593  HOH   HOH B . 
CA 11 HOH   887  2987 2349 HOH   HOH B . 
CA 11 HOH   888  2988 997  HOH   HOH B . 
CA 11 HOH   889  2989 2105 HOH   HOH B . 
CA 11 HOH   890  2990 755  HOH   HOH B . 
CA 11 HOH   891  2991 1655 HOH   HOH B . 
CA 11 HOH   892  2992 2466 HOH   HOH B . 
CA 11 HOH   893  2993 2502 HOH   HOH B . 
CA 11 HOH   894  2994 2018 HOH   HOH B . 
CA 11 HOH   895  2995 1569 HOH   HOH B . 
CA 11 HOH   896  2996 96   HOH   HOH B . 
CA 11 HOH   897  2997 2033 HOH   HOH B . 
CA 11 HOH   898  2998 2242 HOH   HOH B . 
CA 11 HOH   899  2999 68   HOH   HOH B . 
CA 11 HOH   900  3000 948  HOH   HOH B . 
CA 11 HOH   901  3001 2139 HOH   HOH B . 
CA 11 HOH   902  3002 784  HOH   HOH B . 
CA 11 HOH   903  3003 602  HOH   HOH B . 
CA 11 HOH   904  3004 725  HOH   HOH B . 
CA 11 HOH   905  3005 2423 HOH   HOH B . 
CA 11 HOH   906  3006 1934 HOH   HOH B . 
CA 11 HOH   907  3007 1851 HOH   HOH B . 
CA 11 HOH   908  3008 2435 HOH   HOH B . 
CA 11 HOH   909  3009 2527 HOH   HOH B . 
CA 11 HOH   910  3010 452  HOH   HOH B . 
CA 11 HOH   911  3011 1591 HOH   HOH B . 
CA 11 HOH   912  3012 2620 HOH   HOH B . 
CA 11 HOH   913  3013 2386 HOH   HOH B . 
CA 11 HOH   914  3014 2227 HOH   HOH B . 
CA 11 HOH   915  3015 1466 HOH   HOH B . 
CA 11 HOH   916  3016 2044 HOH   HOH B . 
CA 11 HOH   917  3017 1725 HOH   HOH B . 
CA 11 HOH   918  3018 1820 HOH   HOH B . 
CA 11 HOH   919  3019 1774 HOH   HOH B . 
CA 11 HOH   920  3020 2399 HOH   HOH B . 
CA 11 HOH   921  3021 1104 HOH   HOH B . 
CA 11 HOH   922  3022 371  HOH   HOH B . 
CA 11 HOH   923  3023 1614 HOH   HOH B . 
CA 11 HOH   924  3024 2249 HOH   HOH B . 
CA 11 HOH   925  3025 1869 HOH   HOH B . 
CA 11 HOH   926  3026 1739 HOH   HOH B . 
CA 11 HOH   927  3027 2625 HOH   HOH B . 
CA 11 HOH   928  3028 1633 HOH   HOH B . 
CA 11 HOH   929  3029 2623 HOH   HOH B . 
CA 11 HOH   930  3030 441  HOH   HOH B . 
CA 11 HOH   931  3031 896  HOH   HOH B . 
CA 11 HOH   932  3032 2341 HOH   HOH B . 
CA 11 HOH   933  3033 1470 HOH   HOH B . 
CA 11 HOH   934  3034 8    HOH   HOH B . 
CA 11 HOH   935  3035 1571 HOH   HOH B . 
CA 11 HOH   936  3036 2020 HOH   HOH B . 
CA 11 HOH   937  3037 2698 HOH   HOH B . 
CA 11 HOH   938  3038 2133 HOH   HOH B . 
CA 11 HOH   939  3039 1575 HOH   HOH B . 
CA 11 HOH   940  3040 1554 HOH   HOH B . 
CA 11 HOH   941  3041 2582 HOH   HOH B . 
CA 11 HOH   942  3042 2601 HOH   HOH B . 
CA 11 HOH   943  3043 1231 HOH   HOH B . 
CA 11 HOH   944  3044 1890 HOH   HOH B . 
CA 11 HOH   945  3045 951  HOH   HOH B . 
CA 11 HOH   946  3046 1146 HOH   HOH B . 
CA 11 HOH   947  3047 1998 HOH   HOH B . 
CA 11 HOH   948  3048 744  HOH   HOH B . 
CA 11 HOH   949  3049 524  HOH   HOH B . 
CA 11 HOH   950  3050 1016 HOH   HOH B . 
CA 11 HOH   951  3051 1786 HOH   HOH B . 
CA 11 HOH   952  3052 1056 HOH   HOH B . 
CA 11 HOH   953  3053 734  HOH   HOH B . 
CA 11 HOH   954  3054 1568 HOH   HOH B . 
CA 11 HOH   955  3055 2021 HOH   HOH B . 
CA 11 HOH   956  3056 1581 HOH   HOH B . 
CA 11 HOH   957  3057 1751 HOH   HOH B . 
CA 11 HOH   958  3058 2089 HOH   HOH B . 
CA 11 HOH   959  3059 1982 HOH   HOH B . 
CA 11 HOH   960  3060 2674 HOH   HOH B . 
CA 11 HOH   961  3061 1690 HOH   HOH B . 
CA 11 HOH   962  3062 969  HOH   HOH B . 
CA 11 HOH   963  3063 2385 HOH   HOH B . 
CA 11 HOH   964  3064 1653 HOH   HOH B . 
CA 11 HOH   965  3065 2261 HOH   HOH B . 
CA 11 HOH   966  3066 1489 HOH   HOH B . 
CA 11 HOH   967  3067 2697 HOH   HOH B . 
CA 11 HOH   968  3068 1011 HOH   HOH B . 
CA 11 HOH   969  3069 1048 HOH   HOH B . 
CA 11 HOH   970  3070 1703 HOH   HOH B . 
CA 11 HOH   971  3071 2019 HOH   HOH B . 
CA 11 HOH   972  3072 1242 HOH   HOH B . 
CA 11 HOH   973  3073 26   HOH   HOH B . 
CA 11 HOH   974  3074 1735 HOH   HOH B . 
CA 11 HOH   975  3075 2581 HOH   HOH B . 
CA 11 HOH   976  3076 2184 HOH   HOH B . 
CA 11 HOH   977  3077 1700 HOH   HOH B . 
CA 11 HOH   978  3078 1707 HOH   HOH B . 
CA 11 HOH   979  3079 2136 HOH   HOH B . 
CA 11 HOH   980  3080 2396 HOH   HOH B . 
CA 11 HOH   981  3081 2463 HOH   HOH B . 
CA 11 HOH   982  3082 2419 HOH   HOH B . 
CA 11 HOH   983  3083 1446 HOH   HOH B . 
CA 11 HOH   984  3084 1357 HOH   HOH B . 
CA 11 HOH   985  3085 2335 HOH   HOH B . 
CA 11 HOH   986  3086 1601 HOH   HOH B . 
CA 11 HOH   987  3087 1406 HOH   HOH B . 
CA 11 HOH   988  3088 2259 HOH   HOH B . 
CA 11 HOH   989  3089 2210 HOH   HOH B . 
CA 11 HOH   990  3090 1234 HOH   HOH B . 
CA 11 HOH   991  3091 2490 HOH   HOH B . 
CA 11 HOH   992  3092 2270 HOH   HOH B . 
CA 11 HOH   993  3093 2514 HOH   HOH B . 
CA 11 HOH   994  3094 2529 HOH   HOH B . 
CA 11 HOH   995  3095 987  HOH   HOH B . 
CA 11 HOH   996  3096 1949 HOH   HOH B . 
CA 11 HOH   997  3097 2313 HOH   HOH B . 
CA 11 HOH   998  3098 7    HOH   HOH B . 
CA 11 HOH   999  3099 2474 HOH   HOH B . 
CA 11 HOH   1000 3100 2510 HOH   HOH B . 
CA 11 HOH   1001 3101 1262 HOH   HOH B . 
CA 11 HOH   1002 3102 2515 HOH   HOH B . 
CA 11 HOH   1003 3103 2593 HOH   HOH B . 
CA 11 HOH   1004 3104 2344 HOH   HOH B . 
CA 11 HOH   1005 3105 1983 HOH   HOH B . 
CA 11 HOH   1006 3106 1090 HOH   HOH B . 
CA 11 HOH   1007 3107 54   HOH   HOH B . 
CA 11 HOH   1008 3108 1249 HOH   HOH B . 
CA 11 HOH   1009 3109 2703 HOH   HOH B . 
CA 11 HOH   1010 3110 2558 HOH   HOH B . 
CA 11 HOH   1011 3111 2644 HOH   HOH B . 
CA 11 HOH   1012 3112 1445 HOH   HOH B . 
CA 11 HOH   1013 3113 1344 HOH   HOH B . 
CA 11 HOH   1014 3114 1620 HOH   HOH B . 
CA 11 HOH   1015 3115 2626 HOH   HOH B . 
CA 11 HOH   1016 3116 1922 HOH   HOH B . 
CA 11 HOH   1017 3117 1049 HOH   HOH B . 
CA 11 HOH   1018 3118 424  HOH   HOH B . 
CA 11 HOH   1019 3119 1944 HOH   HOH B . 
CA 11 HOH   1020 3120 2271 HOH   HOH B . 
CA 11 HOH   1021 3121 2134 HOH   HOH B . 
CA 11 HOH   1022 3122 411  HOH   HOH B . 
CA 11 HOH   1023 3123 1088 HOH   HOH B . 
CA 11 HOH   1024 3124 847  HOH   HOH B . 
CA 11 HOH   1025 3125 2007 HOH   HOH B . 
CA 11 HOH   1026 3126 94   HOH   HOH B . 
CA 11 HOH   1027 3127 1423 HOH   HOH B . 
CA 11 HOH   1028 3128 1599 HOH   HOH B . 
CA 11 HOH   1029 3129 2032 HOH   HOH B . 
CA 11 HOH   1030 3130 2645 HOH   HOH B . 
CA 11 HOH   1031 3131 2705 HOH   HOH B . 
CA 11 HOH   1032 3132 1194 HOH   HOH B . 
CA 11 HOH   1033 3133 1964 HOH   HOH B . 
CA 11 HOH   1034 3134 1219 HOH   HOH B . 
CA 11 HOH   1035 3135 1693 HOH   HOH B . 
CA 11 HOH   1036 3136 1414 HOH   HOH B . 
CA 11 HOH   1037 3137 67   HOH   HOH B . 
CA 11 HOH   1038 3138 983  HOH   HOH B . 
CA 11 HOH   1039 3139 99   HOH   HOH B . 
CA 11 HOH   1040 3140 1091 HOH   HOH B . 
CA 11 HOH   1041 3141 968  HOH   HOH B . 
CA 11 HOH   1042 3142 575  HOH   HOH B . 
CA 11 HOH   1043 3143 1775 HOH   HOH B . 
CA 11 HOH   1044 3144 469  HOH   HOH B . 
CA 11 HOH   1045 3145 1610 HOH   HOH B . 
CA 11 HOH   1046 3146 698  HOH   HOH B . 
CA 11 HOH   1047 3147 568  HOH   HOH B . 
CA 11 HOH   1048 3148 2504 HOH   HOH B . 
CA 11 HOH   1049 3149 2106 HOH   HOH B . 
CA 11 HOH   1050 3150 2187 HOH   HOH B . 
CA 11 HOH   1051 3151 1856 HOH   HOH B . 
CA 11 HOH   1052 3152 53   HOH   HOH B . 
CA 11 HOH   1053 3153 1069 HOH   HOH B . 
CA 11 HOH   1054 3154 2651 HOH   HOH B . 
CA 11 HOH   1055 3155 82   HOH   HOH B . 
CA 11 HOH   1056 3156 1168 HOH   HOH B . 
CA 11 HOH   1057 3157 2237 HOH   HOH B . 
CA 11 HOH   1058 3158 1389 HOH   HOH B . 
CA 11 HOH   1059 3159 1594 HOH   HOH B . 
CA 11 HOH   1060 3160 1776 HOH   HOH B . 
CA 11 HOH   1061 3161 2468 HOH   HOH B . 
CA 11 HOH   1062 3162 2140 HOH   HOH B . 
CA 11 HOH   1063 3163 2704 HOH   HOH B . 
CA 11 HOH   1064 3164 2715 HOH   HOH B . 
CA 11 HOH   1065 3165 2031 HOH   HOH B . 
CA 11 HOH   1066 3166 1830 HOH   HOH B . 
CA 11 HOH   1067 3167 2138 HOH   HOH B . 
CA 11 HOH   1068 3168 964  HOH   HOH B . 
CA 11 HOH   1069 3169 1303 HOH   HOH B . 
CA 11 HOH   1070 3170 110  HOH   HOH B . 
CA 11 HOH   1071 3171 940  HOH   HOH B . 
CA 11 HOH   1072 3172 523  HOH   HOH B . 
CA 11 HOH   1073 3173 1914 HOH   HOH B . 
CA 11 HOH   1074 3174 1024 HOH   HOH B . 
CA 11 HOH   1075 3175 2382 HOH   HOH B . 
CA 11 HOH   1076 3176 1761 HOH   HOH B . 
CA 11 HOH   1077 3177 1999 HOH   HOH B . 
CA 11 HOH   1078 3178 1617 HOH   HOH B . 
CA 11 HOH   1079 3179 2440 HOH   HOH B . 
CA 11 HOH   1080 3180 2141 HOH   HOH B . 
CA 11 HOH   1081 3181 1165 HOH   HOH B . 
CA 11 HOH   1082 3182 1519 HOH   HOH B . 
CA 11 HOH   1083 3183 1387 HOH   HOH B . 
CA 11 HOH   1084 3184 2    HOH   HOH B . 
CA 11 HOH   1085 3185 2290 HOH   HOH B . 
CA 11 HOH   1086 3186 1074 HOH   HOH B . 
CA 11 HOH   1087 3187 1873 HOH   HOH B . 
CA 11 HOH   1088 3188 1214 HOH   HOH B . 
CA 11 HOH   1089 3189 556  HOH   HOH B . 
CA 11 HOH   1090 3190 912  HOH   HOH B . 
CA 11 HOH   1091 3191 2070 HOH   HOH B . 
CA 11 HOH   1092 3192 1915 HOH   HOH B . 
CA 11 HOH   1093 3193 1862 HOH   HOH B . 
CA 11 HOH   1094 3194 2539 HOH   HOH B . 
CA 11 HOH   1095 3195 1051 HOH   HOH B . 
CA 11 HOH   1096 3196 1966 HOH   HOH B . 
CA 11 HOH   1097 3197 1808 HOH   HOH B . 
CA 11 HOH   1098 3198 2372 HOH   HOH B . 
CA 11 HOH   1099 3199 761  HOH   HOH B . 
CA 11 HOH   1100 3200 1967 HOH   HOH B . 
CA 11 HOH   1101 3201 2324 HOH   HOH B . 
CA 11 HOH   1102 3202 1826 HOH   HOH B . 
CA 11 HOH   1103 3203 1902 HOH   HOH B . 
CA 11 HOH   1104 3204 1854 HOH   HOH B . 
CA 11 HOH   1105 3205 779  HOH   HOH B . 
CA 11 HOH   1106 3206 2569 HOH   HOH B . 
CA 11 HOH   1107 3207 2405 HOH   HOH B . 
CA 11 HOH   1108 3208 1867 HOH   HOH B . 
CA 11 HOH   1109 3209 1589 HOH   HOH B . 
CA 11 HOH   1110 3210 1201 HOH   HOH B . 
CA 11 HOH   1111 3211 1720 HOH   HOH B . 
CA 11 HOH   1112 3212 1447 HOH   HOH B . 
CA 11 HOH   1113 3213 707  HOH   HOH B . 
CA 11 HOH   1114 3214 1943 HOH   HOH B . 
CA 11 HOH   1115 3215 2283 HOH   HOH B . 
CA 11 HOH   1116 3216 1537 HOH   HOH B . 
CA 11 HOH   1117 3217 2055 HOH   HOH B . 
CA 11 HOH   1118 3218 1799 HOH   HOH B . 
CA 11 HOH   1119 3219 2056 HOH   HOH B . 
CA 11 HOH   1120 3220 2511 HOH   HOH B . 
CA 11 HOH   1121 3221 1985 HOH   HOH B . 
CA 11 HOH   1122 3222 2411 HOH   HOH B . 
CA 11 HOH   1123 3223 1417 HOH   HOH B . 
CA 11 HOH   1124 3224 2560 HOH   HOH B . 
CA 11 HOH   1125 3225 114  HOH   HOH B . 
CA 11 HOH   1126 3226 2343 HOH   HOH B . 
CA 11 HOH   1127 3227 1952 HOH   HOH B . 
CA 11 HOH   1128 3228 2292 HOH   HOH B . 
CA 11 HOH   1129 3229 991  HOH   HOH B . 
CA 11 HOH   1130 3230 922  HOH   HOH B . 
CA 11 HOH   1131 3231 1265 HOH   HOH B . 
CA 11 HOH   1132 3232 1421 HOH   HOH B . 
CA 11 HOH   1133 3233 1244 HOH   HOH B . 
CA 11 HOH   1134 3234 15   HOH   HOH B . 
CA 11 HOH   1135 3235 2068 HOH   HOH B . 
CA 11 HOH   1136 3236 2587 HOH   HOH B . 
CA 11 HOH   1137 3237 1649 HOH   HOH B . 
CA 11 HOH   1138 3238 1018 HOH   HOH B . 
CA 11 HOH   1139 3239 1251 HOH   HOH B . 
CA 11 HOH   1140 3240 2673 HOH   HOH B . 
CA 11 HOH   1141 3241 1697 HOH   HOH B . 
CA 11 HOH   1142 3242 2309 HOH   HOH B . 
CA 11 HOH   1143 3243 104  HOH   HOH B . 
CA 11 HOH   1144 3244 1384 HOH   HOH B . 
CA 11 HOH   1145 3245 1295 HOH   HOH B . 
CA 11 HOH   1146 3246 1652 HOH   HOH B . 
CA 11 HOH   1147 3247 2471 HOH   HOH B . 
CA 11 HOH   1148 3248 1573 HOH   HOH B . 
CA 11 HOH   1149 3249 4    HOH   HOH B . 
CA 11 HOH   1150 3250 2570 HOH   HOH B . 
CA 11 HOH   1151 3251 869  HOH   HOH B . 
CA 11 HOH   1152 3252 1428 HOH   HOH B . 
CA 11 HOH   1153 3253 2681 HOH   HOH B . 
CA 11 HOH   1154 3254 990  HOH   HOH B . 
CA 11 HOH   1155 3255 1896 HOH   HOH B . 
CA 11 HOH   1156 3256 1148 HOH   HOH B . 
CA 11 HOH   1157 3257 1045 HOH   HOH B . 
CA 11 HOH   1158 3258 2087 HOH   HOH B . 
CA 11 HOH   1159 3259 2378 HOH   HOH B . 
CA 11 HOH   1160 3260 1736 HOH   HOH B . 
CA 11 HOH   1161 3261 866  HOH   HOH B . 
CA 11 HOH   1162 3262 2571 HOH   HOH B . 
CA 11 HOH   1163 3263 1032 HOH   HOH B . 
CA 11 HOH   1164 3264 1844 HOH   HOH B . 
CA 11 HOH   1165 3265 1523 HOH   HOH B . 
CA 11 HOH   1166 3266 1450 HOH   HOH B . 
CA 11 HOH   1167 3267 2561 HOH   HOH B . 
CA 11 HOH   1168 3268 62   HOH   HOH B . 
CA 11 HOH   1169 3269 2232 HOH   HOH B . 
CA 11 HOH   1170 3270 2034 HOH   HOH B . 
CA 11 HOH   1171 3271 552  HOH   HOH B . 
CA 11 HOH   1172 3272 2551 HOH   HOH B . 
CA 11 HOH   1173 3273 27   HOH   HOH B . 
CA 11 HOH   1174 3274 1871 HOH   HOH B . 
CA 11 HOH   1175 3275 2648 HOH   HOH B . 
CA 11 HOH   1176 3276 1544 HOH   HOH B . 
CA 11 HOH   1177 3277 1204 HOH   HOH B . 
CA 11 HOH   1178 3278 378  HOH   HOH B . 
CA 11 HOH   1179 3279 2274 HOH   HOH B . 
CA 11 HOH   1180 3280 1397 HOH   HOH B . 
CA 11 HOH   1181 3281 2051 HOH   HOH B . 
CA 11 HOH   1182 3282 25   HOH   HOH B . 
CA 11 HOH   1183 3283 2450 HOH   HOH B . 
CA 11 HOH   1184 3284 1668 HOH   HOH B . 
CA 11 HOH   1185 3285 1872 HOH   HOH B . 
CA 11 HOH   1186 3286 105  HOH   HOH B . 
CA 11 HOH   1187 3287 1894 HOH   HOH B . 
CA 11 HOH   1188 3288 2297 HOH   HOH B . 
CA 11 HOH   1189 3289 1270 HOH   HOH B . 
CA 11 HOH   1190 3290 1699 HOH   HOH B . 
CA 11 HOH   1191 3291 1900 HOH   HOH B . 
CA 11 HOH   1192 3292 1701 HOH   HOH B . 
CA 11 HOH   1193 3293 1749 HOH   HOH B . 
CA 11 HOH   1194 3294 1290 HOH   HOH B . 
CA 11 HOH   1195 3295 1535 HOH   HOH B . 
CA 11 HOH   1196 3296 2441 HOH   HOH B . 
CA 11 HOH   1197 3297 1648 HOH   HOH B . 
CA 11 HOH   1198 3298 2371 HOH   HOH B . 
CA 11 HOH   1199 3299 1933 HOH   HOH B . 
CA 11 HOH   1200 3300 978  HOH   HOH B . 
CA 11 HOH   1201 3301 1138 HOH   HOH B . 
CA 11 HOH   1202 3302 2275 HOH   HOH B . 
CA 11 HOH   1203 3303 1127 HOH   HOH B . 
CA 11 HOH   1204 3304 818  HOH   HOH B . 
CA 11 HOH   1205 3305 1308 HOH   HOH B . 
CA 11 HOH   1206 3306 2114 HOH   HOH B . 
CA 11 HOH   1207 3307 2431 HOH   HOH B . 
CA 11 HOH   1208 3308 1322 HOH   HOH B . 
CA 11 HOH   1209 3309 2436 HOH   HOH B . 
CA 11 HOH   1210 3310 93   HOH   HOH B . 
CA 11 HOH   1211 3311 1938 HOH   HOH B . 
CA 11 HOH   1212 3312 1994 HOH   HOH B . 
CA 11 HOH   1213 3313 1144 HOH   HOH B . 
CA 11 HOH   1214 3314 749  HOH   HOH B . 
CA 11 HOH   1215 3315 1997 HOH   HOH B . 
CA 11 HOH   1216 3316 2710 HOH   HOH B . 
CA 11 HOH   1217 3317 1343 HOH   HOH B . 
CA 11 HOH   1218 3318 2255 HOH   HOH B . 
CA 11 HOH   1219 3319 122  HOH   HOH B . 
CA 11 HOH   1220 3320 1843 HOH   HOH B . 
CA 11 HOH   1221 3321 583  HOH   HOH B . 
CA 11 HOH   1222 3322 1909 HOH   HOH B . 
CA 11 HOH   1223 3323 1845 HOH   HOH B . 
CA 11 HOH   1224 3324 665  HOH   HOH B . 
CA 11 HOH   1225 3325 2300 HOH   HOH B . 
CA 11 HOH   1226 3326 1996 HOH   HOH B . 
CA 11 HOH   1227 3327 50   HOH   HOH B . 
CA 11 HOH   1228 3328 738  HOH   HOH B . 
CA 11 HOH   1229 3329 1402 HOH   HOH B . 
CA 11 HOH   1230 3330 1226 HOH   HOH B . 
CA 11 HOH   1231 3331 1451 HOH   HOH B . 
CA 11 HOH   1232 3332 183  HOH   HOH B . 
CA 11 HOH   1233 3333 1179 HOH   HOH B . 
CA 11 HOH   1234 3334 2111 HOH   HOH B . 
CA 11 HOH   1235 3335 17   HOH   HOH B . 
CA 11 HOH   1236 3336 2489 HOH   HOH B . 
CA 11 HOH   1237 3337 2050 HOH   HOH B . 
CA 11 HOH   1238 3338 480  HOH   HOH B . 
CA 11 HOH   1239 3339 467  HOH   HOH B . 
CA 11 HOH   1240 3340 2178 HOH   HOH B . 
CA 11 HOH   1241 3341 961  HOH   HOH B . 
CA 11 HOH   1242 3342 2636 HOH   HOH B . 
CA 11 HOH   1243 3343 1849 HOH   HOH B . 
CA 11 HOH   1244 3344 1968 HOH   HOH B . 
CA 11 HOH   1245 3345 1988 HOH   HOH B . 
CA 11 HOH   1246 3346 1221 HOH   HOH B . 
CA 11 HOH   1247 3347 1740 HOH   HOH B . 
CA 11 HOH   1248 3348 2578 HOH   HOH B . 
CA 11 HOH   1249 3349 1246 HOH   HOH B . 
CA 11 HOH   1250 3350 1081 HOH   HOH B . 
CA 11 HOH   1251 3351 21   HOH   HOH B . 
CA 11 HOH   1252 3352 660  HOH   HOH B . 
CA 11 HOH   1253 3353 2112 HOH   HOH B . 
CA 11 HOH   1254 3354 1897 HOH   HOH B . 
CA 11 HOH   1255 3355 1507 HOH   HOH B . 
CA 11 HOH   1256 3356 941  HOH   HOH B . 
CA 11 HOH   1257 3357 1145 HOH   HOH B . 
CA 11 HOH   1258 3358 1942 HOH   HOH B . 
CA 11 HOH   1259 3359 1429 HOH   HOH B . 
CA 11 HOH   1260 3360 2127 HOH   HOH B . 
CA 11 HOH   1261 3361 2513 HOH   HOH B . 
CA 11 HOH   1262 3362 1424 HOH   HOH B . 
CA 11 HOH   1263 3363 877  HOH   HOH B . 
CA 11 HOH   1264 3364 71   HOH   HOH B . 
CA 11 HOH   1265 3365 1438 HOH   HOH B . 
CA 11 HOH   1266 3366 1410 HOH   HOH B . 
CA 11 HOH   1267 3367 2206 HOH   HOH B . 
CA 11 HOH   1268 3368 2053 HOH   HOH B . 
CA 11 HOH   1269 3369 975  HOH   HOH B . 
CA 11 HOH   1270 3370 1153 HOH   HOH B . 
CA 11 HOH   1271 3371 770  HOH   HOH B . 
CA 11 HOH   1272 3372 1443 HOH   HOH B . 
CA 11 HOH   1273 3373 1392 HOH   HOH B . 
CA 11 HOH   1274 3374 1293 HOH   HOH B . 
CA 11 HOH   1275 3375 2291 HOH   HOH B . 
CA 11 HOH   1276 3376 164  HOH   HOH B . 
CA 11 HOH   1277 3377 1950 HOH   HOH B . 
CA 11 HOH   1278 3378 2    HOH   HOH B . 
CA 11 HOH   1279 3379 439  HOH   HOH B . 
CA 11 HOH   1280 3380 2084 HOH   HOH B . 
CA 11 HOH   1281 3381 993  HOH   HOH B . 
CA 11 HOH   1282 3382 2653 HOH   HOH B . 
CA 11 HOH   1283 3383 1279 HOH   HOH B . 
CA 11 HOH   1284 3384 1385 HOH   HOH B . 
CA 11 HOH   1285 3385 1910 HOH   HOH B . 
CA 11 HOH   1286 3386 1111 HOH   HOH B . 
CA 11 HOH   1287 3387 802  HOH   HOH B . 
CA 11 HOH   1288 3388 2199 HOH   HOH B . 
CA 11 HOH   1289 3389 1058 HOH   HOH B . 
CA 11 HOH   1290 3390 2631 HOH   HOH B . 
CA 11 HOH   1291 3391 695  HOH   HOH B . 
CA 11 HOH   1292 3392 1781 HOH   HOH B . 
CA 11 HOH   1293 3393 1962 HOH   HOH B . 
CA 11 HOH   1294 3394 1874 HOH   HOH B . 
CA 11 HOH   1295 3395 1426 HOH   HOH B . 
CA 11 HOH   1296 3396 1495 HOH   HOH B . 
CA 11 HOH   1297 3397 1092 HOH   HOH B . 
CA 11 HOH   1298 3398 1973 HOH   HOH B . 
CA 11 HOH   1299 3399 1846 HOH   HOH B . 
CA 11 HOH   1300 3400 1760 HOH   HOH B . 
CA 11 HOH   1301 3401 1702 HOH   HOH B . 
CA 11 HOH   1302 3402 1860 HOH   HOH B . 
CA 11 HOH   1303 3403 1366 HOH   HOH B . 
CA 11 HOH   1304 3404 1925 HOH   HOH B . 
CA 11 HOH   1305 3405 2198 HOH   HOH B . 
CA 11 HOH   1306 3406 1765 HOH   HOH B . 
CA 11 HOH   1307 3407 1911 HOH   HOH B . 
CA 11 HOH   1308 3408 2630 HOH   HOH B . 
CA 11 HOH   1309 3409 1981 HOH   HOH B . 
CA 11 HOH   1310 3410 490  HOH   HOH B . 
CA 11 HOH   1311 3411 2614 HOH   HOH B . 
CA 11 HOH   1312 3412 1798 HOH   HOH B . 
CA 11 HOH   1313 3413 243  HOH   HOH B . 
CA 11 HOH   1314 3414 2334 HOH   HOH B . 
CA 11 HOH   1315 3415 757  HOH   HOH B . 
CA 11 HOH   1316 3416 1643 HOH   HOH B . 
CA 11 HOH   1317 3417 2180 HOH   HOH B . 
CA 11 HOH   1318 3418 810  HOH   HOH B . 
CA 11 HOH   1319 3419 2639 HOH   HOH B . 
CA 11 HOH   1320 3420 2282 HOH   HOH B . 
CA 11 HOH   1321 3421 2250 HOH   HOH B . 
CA 11 HOH   1322 3422 1297 HOH   HOH B . 
CA 11 HOH   1323 3423 1556 HOH   HOH B . 
CA 11 HOH   1324 3424 1331 HOH   HOH B . 
CA 11 HOH   1325 3425 2296 HOH   HOH B . 
CA 11 HOH   1326 3426 909  HOH   HOH B . 
CA 11 HOH   1327 3427 1710 HOH   HOH B . 
CA 11 HOH   1328 3428 1768 HOH   HOH B . 
CA 11 HOH   1329 3429 1084 HOH   HOH B . 
CA 11 HOH   1330 3430 919  HOH   HOH B . 
CA 11 HOH   1331 3431 1128 HOH   HOH B . 
CA 11 HOH   1332 3432 1513 HOH   HOH B . 
CA 11 HOH   1333 3433 2410 HOH   HOH B . 
CA 11 HOH   1334 3434 40   HOH   HOH B . 
CA 11 HOH   1335 3435 2122 HOH   HOH B . 
CA 11 HOH   1336 3436 2707 HOH   HOH B . 
CA 11 HOH   1337 3437 2200 HOH   HOH B . 
CA 11 HOH   1338 3438 1959 HOH   HOH B . 
CA 11 HOH   1339 3439 1753 HOH   HOH B . 
CA 11 HOH   1340 3440 2284 HOH   HOH B . 
CA 11 HOH   1341 3441 102  HOH   HOH B . 
CA 11 HOH   1342 3442 1375 HOH   HOH B . 
CA 11 HOH   1343 3443 545  HOH   HOH B . 
CA 11 HOH   1344 3444 1509 HOH   HOH B . 
CA 11 HOH   1345 3445 1363 HOH   HOH B . 
CA 11 HOH   1346 3446 2294 HOH   HOH B . 
CA 11 HOH   1347 3447 101  HOH   HOH B . 
CA 11 HOH   1348 3448 1913 HOH   HOH B . 
CA 11 HOH   1349 3449 693  HOH   HOH B . 
CA 11 HOH   1350 3450 2137 HOH   HOH B . 
CA 11 HOH   1351 3451 2719 HOH   HOH B . 
CA 11 HOH   1352 3452 1930 HOH   HOH B . 
CA 11 HOH   1353 3453 1666 HOH   HOH B . 
CA 11 HOH   1354 3454 1355 HOH   HOH B . 
CA 11 HOH   1355 3455 1401 HOH   HOH B . 
CA 11 HOH   1356 3456 2075 HOH   HOH B . 
CA 11 HOH   1357 3457 1143 HOH   HOH B . 
CA 11 HOH   1358 3458 2462 HOH   HOH B . 
CA 11 HOH   1359 3459 2404 HOH   HOH B . 
CA 11 HOH   1360 3460 2299 HOH   HOH B . 
CA 11 HOH   1361 3461 1077 HOH   HOH B . 
CA 11 HOH   1362 3462 1368 HOH   HOH B . 
CA 11 HOH   1363 3463 2613 HOH   HOH B . 
CA 11 HOH   1364 3464 985  HOH   HOH B . 
CA 11 HOH   1365 3465 1809 HOH   HOH B . 
CA 11 HOH   1366 3466 1883 HOH   HOH B . 
CA 11 HOH   1367 3467 1536 HOH   HOH B . 
CA 11 HOH   1368 3468 1960 HOH   HOH B . 
CA 11 HOH   1369 3469 2301 HOH   HOH B . 
CA 11 HOH   1370 3470 2713 HOH   HOH B . 
CA 11 HOH   1371 3471 1815 HOH   HOH B . 
CA 11 HOH   1372 3472 2295 HOH   HOH B . 
CA 11 HOH   1373 3473 2414 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 52   ? CG  ? A GLU 54   CG  
2   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
3   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
4   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
5   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
6   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
7   1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
8   1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
9   1 Y 1 A HIS 79   ? CG  ? A HIS 81   CG  
10  1 Y 1 A HIS 79   ? ND1 ? A HIS 81   ND1 
11  1 Y 1 A HIS 79   ? CD2 ? A HIS 81   CD2 
12  1 Y 1 A HIS 79   ? CE1 ? A HIS 81   CE1 
13  1 Y 1 A HIS 79   ? NE2 ? A HIS 81   NE2 
14  1 Y 1 A SER 82   ? OG  ? A SER 84   OG  
15  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
16  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
17  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
18  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
19  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
20  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
21  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
22  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
23  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
24  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
25  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
26  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
27  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
28  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
29  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
30  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
31  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
32  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
33  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
34  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
35  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
36  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
37  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
38  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
39  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
40  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
41  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
42  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
43  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
44  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
45  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
46  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
47  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
48  1 Y 1 A THR 156  ? OG1 ? A THR 158  OG1 
49  1 Y 1 A THR 156  ? CG2 ? A THR 158  CG2 
50  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
51  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
52  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
53  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
54  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
55  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
56  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
57  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
58  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
59  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
60  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
61  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
62  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
63  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
64  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
65  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
66  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
67  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
68  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
69  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
70  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
71  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
72  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
73  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
74  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
75  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
76  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
77  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
78  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
79  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
80  1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
81  1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
82  1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
83  1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
84  1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
85  1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
86  1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
87  1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
88  1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
89  1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
90  1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
91  1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
92  1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
93  1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
94  1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
95  1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
96  1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
97  1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
98  1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
99  1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
100 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
101 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
102 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
103 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
104 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
105 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
106 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
107 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
108 1 Y 1 A GLU 674  ? CG  ? A GLU 676  CG  
109 1 Y 1 A GLU 674  ? CD  ? A GLU 676  CD  
110 1 Y 1 A GLU 674  ? OE1 ? A GLU 676  OE1 
111 1 Y 1 A GLU 674  ? OE2 ? A GLU 676  OE2 
112 1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
113 1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
114 1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
115 1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
116 1 Y 1 A LEU 824  ? CG  ? A LEU 826  CG  
117 1 Y 1 A LEU 824  ? CD1 ? A LEU 826  CD1 
118 1 Y 1 A LEU 824  ? CD2 ? A LEU 826  CD2 
119 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
120 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
121 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
122 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
123 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
124 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
125 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
126 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
127 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
128 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
129 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
130 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
131 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
132 1 Y 1 A GLU 932  ? CG  ? A GLU 934  CG  
133 1 Y 1 A GLU 932  ? CD  ? A GLU 934  CD  
134 1 Y 1 A GLU 932  ? OE1 ? A GLU 934  OE1 
135 1 Y 1 A GLU 932  ? OE2 ? A GLU 934  OE2 
136 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
137 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
138 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
139 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
140 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
141 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
142 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
143 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
144 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
145 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
146 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
147 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
148 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
149 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
150 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
151 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
152 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
153 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
154 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
155 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
156 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
157 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
158 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
159 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
160 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
161 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
162 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
163 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
164 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
165 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
166 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
167 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
168 1 Y 1 A MET 1230 ? CG  ? A MET 1232 CG  
169 1 Y 1 A MET 1230 ? SD  ? A MET 1232 SD  
170 1 Y 1 A MET 1230 ? CE  ? A MET 1232 CE  
171 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
172 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
173 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
174 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
175 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
176 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
177 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
178 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
179 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
180 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
181 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
182 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
183 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
184 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
185 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
186 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
187 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
188 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
189 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
190 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
191 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
192 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
193 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
194 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
195 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
196 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
197 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
198 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
199 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
200 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
201 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
202 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
203 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
204 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
205 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
206 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
207 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
208 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
209 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
210 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
211 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
212 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
213 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
214 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
215 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
216 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
217 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
218 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
219 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
220 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
221 1 Y 1 B LEU 155  ? CG  ? B LEU 157  CG  
222 1 Y 1 B LEU 155  ? CD1 ? B LEU 157  CD1 
223 1 Y 1 B LEU 155  ? CD2 ? B LEU 157  CD2 
224 1 Y 1 B GLU 199  ? CG  ? B GLU 201  CG  
225 1 Y 1 B GLU 199  ? CD  ? B GLU 201  CD  
226 1 Y 1 B GLU 199  ? OE1 ? B GLU 201  OE1 
227 1 Y 1 B GLU 199  ? OE2 ? B GLU 201  OE2 
228 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
229 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
230 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
231 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
232 1 Y 1 B LYS 214  ? CG  ? B LYS 216  CG  
233 1 Y 1 B LYS 214  ? CD  ? B LYS 216  CD  
234 1 Y 1 B LYS 214  ? CE  ? B LYS 216  CE  
235 1 Y 1 B LYS 214  ? NZ  ? B LYS 216  NZ  
236 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
237 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
238 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
239 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
240 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
241 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
242 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
243 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
244 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
245 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
246 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
247 1 Y 1 B GLU 458  ? CG  ? B GLU 460  CG  
248 1 Y 1 B GLU 458  ? CD  ? B GLU 460  CD  
249 1 Y 1 B GLU 458  ? OE1 ? B GLU 460  OE1 
250 1 Y 1 B GLU 458  ? OE2 ? B GLU 460  OE2 
251 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
252 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
253 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
254 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
255 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
256 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
257 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
258 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
259 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
260 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
261 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
262 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
263 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
264 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
265 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
266 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
267 1 Y 1 B LEU 490  ? CG  ? B LEU 492  CG  
268 1 Y 1 B LEU 490  ? CD1 ? B LEU 492  CD1 
269 1 Y 1 B LEU 490  ? CD2 ? B LEU 492  CD2 
270 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
271 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
272 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
273 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
274 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
275 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
276 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
277 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
278 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
279 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
280 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
281 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
282 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
283 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
284 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
285 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
286 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
287 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
288 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
289 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
290 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
291 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
292 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
293 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
294 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
295 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
296 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
297 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
298 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
299 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
300 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
301 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
302 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
303 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
304 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
305 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
306 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
307 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
308 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
309 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
310 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
311 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
312 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
313 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
314 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
315 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
316 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
317 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
318 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
319 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
320 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
321 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
322 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
323 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
324 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
325 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
326 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
327 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
328 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
329 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
330 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
331 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
332 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
333 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
334 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
335 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
336 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
337 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
338 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
339 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
340 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
341 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
342 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
343 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
344 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
345 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
346 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
347 1 Y 1 B SER 1228 ? OG  ? B SER 1230 OG  
348 1 Y 1 B MET 1230 ? CG  ? B MET 1232 CG  
349 1 Y 1 B MET 1230 ? SD  ? B MET 1232 SD  
350 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                   106.32 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DL9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.745 
_cell.length_a_esd                 ? 
_cell.length_b                     101.959 
_cell.length_b_esd                 ? 
_cell.length_c                     126.167 
_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                         9DL9 
_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                   9DL9 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.80 
_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 20 mM 4-Methoxybenzyl alcohol. Crystal was soaked in cryobuffer containing 67 mM 4-Methoxybenzyl alcohol and 20% PEG 200
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000090 
_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        1.000090 
_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                                       9DL9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.32 
_reflns.d_resolution_low                               48.34 
_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                                     1056665 
_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                           94.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.93 
_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                                0.056 
_reflns.pdbx_Rpim_I_all                                0.021 
_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                              0.052 
_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                           80807 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17661 
_reflns_shell.percent_possible_obs                          62.5 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.6 
_reflns_shell.pdbx_chi_squared                              0.65 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.7 
_reflns_shell.pdbx_Rrim_I_all                               1.942 
_reflns_shell.pdbx_Rpim_I_all                               0.886 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.352 
_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                                  1.720 
_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                                 9DL9 
_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                             46.99 
_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                     1056665 
_refine.ls_number_reflns_R_free                  53398 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.30 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1692 
_refine.ls_R_factor_R_free                       0.1878 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1682 
_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                          0.05 
_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                 22.08 
_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        17891 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         330 
_refine_hist.number_atoms_solvent             2660 
_refine_hist.number_atoms_total               20881 
_refine_hist.d_res_high                       1.32 
_refine_hist.d_res_low                        46.99 
# 
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  ? 18989 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.961  ? 25948 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.824 ? 7160  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.071  ? 3038  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3357  ? 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  . . 1097 21185 59.00  . . . . 0.3372 . . . . . . . . . . . 0.3677 
'X-RAY DIFFRACTION' 1.34 1.35  . . 1158 23403 65.00  . . . . 0.3272 . . . . . . . . . . . 0.3275 
'X-RAY DIFFRACTION' 1.35 1.37  . . 1324 25458 71.00  . . . . 0.3176 . . . . . . . . . . . 0.3480 
'X-RAY DIFFRACTION' 1.37 1.38  . . 1574 27669 77.00  . . . . 0.3036 . . . . . . . . . . . 0.3240 
'X-RAY DIFFRACTION' 1.38 1.40  . . 1523 29953 83.00  . . . . 0.2953 . . . . . . . . . . . 0.3028 
'X-RAY DIFFRACTION' 1.40 1.42  . . 1780 32233 90.00  . . . . 0.2862 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 1.42 1.44  . . 1820 35077 98.00  . . . . 0.2696 . . . . . . . . . . . 0.2948 
'X-RAY DIFFRACTION' 1.44 1.46  . . 1989 35703 99.00  . . . . 0.2525 . . . . . . . . . . . 0.2799 
'X-RAY DIFFRACTION' 1.46 1.49  . . 1896 35442 99.00  . . . . 0.2445 . . . . . . . . . . . 0.2523 
'X-RAY DIFFRACTION' 1.49 1.51  . . 2028 35440 99.00  . . . . 0.2313 . . . . . . . . . . . 0.2603 
'X-RAY DIFFRACTION' 1.51 1.54  . . 1876 35617 99.00  . . . . 0.2145 . . . . . . . . . . . 0.2414 
'X-RAY DIFFRACTION' 1.54 1.57  . . 1922 35493 99.00  . . . . 0.2068 . . . . . . . . . . . 0.2275 
'X-RAY DIFFRACTION' 1.57 1.60  . . 1918 35446 99.00  . . . . 0.1989 . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 1.60 1.63  . . 1806 35551 99.00  . . . . 0.1925 . . . . . . . . . . . 0.2239 
'X-RAY DIFFRACTION' 1.63 1.66  . . 1871 35202 98.00  . . . . 0.1845 . . . . . . . . . . . 0.2148 
'X-RAY DIFFRACTION' 1.66 1.70  . . 1942 35251 98.00  . . . . 0.1815 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 1.70 1.74  . . 1726 35337 98.00  . . . . 0.1808 . . . . . . . . . . . 0.2095 
'X-RAY DIFFRACTION' 1.74 1.79  . . 1776 35138 98.00  . . . . 0.1832 . . . . . . . . . . . 0.2014 
'X-RAY DIFFRACTION' 1.79 1.84  . . 1939 34546 97.00  . . . . 0.1920 . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 1.84 1.90  . . 1844 33440 93.00  . . . . 0.1863 . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 1.90 1.97  . . 1898 35041 98.00  . . . . 0.1754 . . . . . . . . . . . 0.1943 
'X-RAY DIFFRACTION' 1.97 2.05  . . 1767 35717 99.00  . . . . 0.1672 . . . . . . . . . . . 0.1902 
'X-RAY DIFFRACTION' 2.05 2.14  . . 1914 35469 99.00  . . . . 0.1633 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 2.14 2.26  . . 1871 35274 98.00  . . . . 0.1603 . . . . . . . . . . . 0.1834 
'X-RAY DIFFRACTION' 2.26 2.40  . . 1991 35273 99.00  . . . . 0.1588 . . . . . . . . . . . 0.1820 
'X-RAY DIFFRACTION' 2.40 2.58  . . 1854 35302 98.00  . . . . 0.1604 . . . . . . . . . . . 0.1761 
'X-RAY DIFFRACTION' 2.58 2.84  . . 1880 35118 98.00  . . . . 0.1606 . . . . . . . . . . . 0.1778 
'X-RAY DIFFRACTION' 2.84 3.26  . . 1698 34304 95.00  . . . . 0.1574 . . . . . . . . . . . 0.1732 
'X-RAY DIFFRACTION' 3.26 4.10  . . 1749 33515 93.00  . . . . 0.1375 . . . . . . . . . . . 0.1576 
'X-RAY DIFFRACTION' 4.10 46.99 . . 1967 35670 100.00 . . . . 0.1347 . . . . . . . . . . . 0.1475 
# 
_struct.entry_id                     9DL9 
_struct.title                        'Structure of proline utilization A co-crystallized with 4-methoxybenzyl alcohol' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DL9 
_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 6  ? 
I  N N 7  ? 
J  N N 8  ? 
K  N N 8  ? 
L  N N 8  ? 
M  N N 8  ? 
N  N N 9  ? 
O  N N 2  ? 
P  N N 3  ? 
Q  N N 6  ? 
R  N N 3  ? 
S  N N 4  ? 
T  N N 5  ? 
U  N N 5  ? 
V  N N 5  ? 
W  N N 4  ? 
X  N N 10 ? 
Y  N N 7  ? 
Z  N N 8  ? 
AA N N 9  ? 
BA N N 11 ? 
CA 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 9DL9 A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9DL9 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 9DL9 SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9DL9 MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9DL9 SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9DL9 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)' 13600 ? 
1 MORE         -124  ? 
1 'SSA (A^2)'  77170 ? 
# 
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 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,BA                                 
3 1 B,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,CA                              
# 
_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   ? HIS A 81   ? SER A 57   HIS A 79   1 ? 23 
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 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P8   AA8 ASN A 162  ? GLN A 196  ? ASN A 160  GLN A 194  1 ? 35 
HELX_P HELX_P9   AA9 THR A 202  ? LYS A 216  ? THR A 200  LYS A 214  1 ? 15 
HELX_P HELX_P10  AB1 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P11  AB2 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P12  AB3 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P13  AB4 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P14  AB5 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P15  AB6 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P16  AB7 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P17  AB8 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P18  AB9 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P19  AC1 TYR A 375  ? GLY A 387  ? TYR A 373  GLY A 385  1 ? 13 
HELX_P HELX_P20  AC2 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P21  AC3 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P22  AC4 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P23  AC5 THR A 480  ? ALA A 486  ? THR A 478  ALA A 484  1 ? 7  
HELX_P HELX_P24  AC6 TYR A 487  ? LEU A 493  ? TYR A 485  LEU A 491  1 ? 7  
HELX_P HELX_P25  AC7 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P26  AC8 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P27  AC9 ASP A 518  ? MET A 526  ? ASP A 516  MET A 524  1 ? 9  
HELX_P HELX_P28  AD1 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P29  AD2 PHE A 543  ? ARG A 547  ? PHE A 541  ARG A 545  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 ? LYS A 1062 ? ASP A 1047 LYS A 1060 1 ? 14 
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   ? SER B 94   ? VAL B 84   SER B 92   1 ? 9  
HELX_P HELX_P65  AH2 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P66  AH3 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P67  AH4 GLY B 130  ? HIS B 135  ? GLY B 128  HIS B 133  5 ? 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  ? GLU B 215  ? THR B 200  GLU B 213  1 ? 14 
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 LEU B 493  ? ALA B 497  ? LEU B 491  ALA B 495  5 ? 5  
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  ? MET B 574  ? ASN B 555  MET B 572  1 ? 18 
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  ? PHE B 839  ? LEU B 824  PHE B 837  1 ? 14 
HELX_P HELX_P102 AL3 ASP B 840  ? GLN B 844  ? ASP B 838  GLN B 842  5 ? 5  
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 ? ? I  NAD . O2A ? ? ? 1_555 N  MG  . MG ? ? A NAD 2007 A MG  2012 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
metalc2  metalc ? ? N  MG  . MG  ? ? ? 1_555 BA HOH . O  ? ? A MG  2012 A HOH 2299 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc3  metalc ? ? N  MG  . MG  ? ? ? 1_555 BA HOH . O  ? ? A MG  2012 A HOH 2404 1_555 ? ? ? ? ? ? ? 2.211 ? ? 
metalc4  metalc ? ? N  MG  . MG  ? ? ? 1_555 BA HOH . O  ? ? A MG  2012 A HOH 2644 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc5  metalc ? ? N  MG  . MG  ? ? ? 1_555 BA HOH . O  ? ? A MG  2012 A HOH 2985 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc6  metalc ? ? N  MG  . MG  ? ? ? 1_555 BA HOH . O  ? ? A MG  2012 A HOH 3152 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc7  metalc ? ? Y  NAD . O2A ? ? ? 1_555 AA MG  . MG ? ? B NAD 2011 B MG  2013 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc8  metalc ? ? AA MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? B MG  2013 B HOH 2370 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc9  metalc ? ? AA MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? B MG  2013 B HOH 2680 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc10 metalc ? ? AA MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? B MG  2013 B HOH 2855 1_555 ? ? ? ? ? ? ? 2.230 ? ? 
metalc11 metalc ? ? AA MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? B MG  2013 B HOH 3011 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc12 metalc ? ? AA MG  . MG  ? ? ? 1_555 CA HOH . O  ? ? B MG  2013 B HOH 3199 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
# 
_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 ? I  NAD . ? A NAD 2007 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2299 ? 1_555 85.5  ? 
2  O2A ? I  NAD . ? A NAD 2007 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2404 ? 1_555 90.4  ? 
3  O   ? BA HOH . ? A HOH 2299 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2404 ? 1_555 94.1  ? 
4  O2A ? I  NAD . ? A NAD 2007 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2644 ? 1_555 86.6  ? 
5  O   ? BA HOH . ? A HOH 2299 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2644 ? 1_555 91.4  ? 
6  O   ? BA HOH . ? A HOH 2404 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2644 ? 1_555 173.4 ? 
7  O2A ? I  NAD . ? A NAD 2007 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2985 ? 1_555 92.2  ? 
8  O   ? BA HOH . ? A HOH 2299 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2985 ? 1_555 174.9 ? 
9  O   ? BA HOH . ? A HOH 2404 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2985 ? 1_555 81.3  ? 
10 O   ? BA HOH . ? A HOH 2644 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 2985 ? 1_555 93.0  ? 
11 O2A ? I  NAD . ? A NAD 2007 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 3152 ? 1_555 172.1 ? 
12 O   ? BA HOH . ? A HOH 2299 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 3152 ? 1_555 86.7  ? 
13 O   ? BA HOH . ? A HOH 2404 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 3152 ? 1_555 91.2  ? 
14 O   ? BA HOH . ? A HOH 2644 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 3152 ? 1_555 92.6  ? 
15 O   ? BA HOH . ? A HOH 2985 ? 1_555 MG ? N  MG . ? A MG 2012 ? 1_555 O ? BA HOH . ? A HOH 3152 ? 1_555 95.6  ? 
16 O2A ? Y  NAD . ? B NAD 2011 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 2370 ? 1_555 93.4  ? 
17 O2A ? Y  NAD . ? B NAD 2011 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 2680 ? 1_555 94.6  ? 
18 O   ? CA HOH . ? B HOH 2370 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 2680 ? 1_555 103.4 ? 
19 O2A ? Y  NAD . ? B NAD 2011 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 2855 ? 1_555 85.4  ? 
20 O   ? CA HOH . ? B HOH 2370 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 2855 ? 1_555 88.1  ? 
21 O   ? CA HOH . ? B HOH 2680 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 2855 ? 1_555 168.5 ? 
22 O2A ? Y  NAD . ? B NAD 2011 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3011 ? 1_555 91.7  ? 
23 O   ? CA HOH . ? B HOH 2370 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3011 ? 1_555 167.9 ? 
24 O   ? CA HOH . ? B HOH 2680 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3011 ? 1_555 87.1  ? 
25 O   ? CA HOH . ? B HOH 2855 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3011 ? 1_555 81.4  ? 
26 O2A ? Y  NAD . ? B NAD 2011 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3199 ? 1_555 170.9 ? 
27 O   ? CA HOH . ? B HOH 2370 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3199 ? 1_555 89.4  ? 
28 O   ? CA HOH . ? B HOH 2680 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3199 ? 1_555 93.2  ? 
29 O   ? CA HOH . ? B HOH 2855 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3199 ? 1_555 86.0  ? 
30 O   ? CA HOH . ? B HOH 3011 ? 1_555 MG ? AA MG . ? B MG 2013 ? 1_555 O ? CA HOH . ? B HOH 3199 ? 1_555 84.0  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 1021 A . ? GLY 1019 A PRO 1022 A ? PRO 1020 A 1 -2.86 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 1.81  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -2.62 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 4.34  
# 
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 ILE A 366  ? N ILE A 364  O PHE A 419  ? O PHE A 417  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O 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 ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O ALA A 1218 ? O ALA A 1216 N LEU A 1095 ? N LEU A 1093 
AA5 9 10 O TYR A 1096 ? O TYR A 1094 N LEU A 1084 ? N LEU A 1082 
AA6 1 2  O SER A 1154 ? O SER A 1152 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                   9DL9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 2869 ? ? O A HOH 2907 ? ? 2.04 
2  1 O   A HOH 3160 ? ? O A HOH 3291 ? ? 2.09 
3  1 O   B HOH 2944 ? ? O B HOH 3136 ? ? 2.09 
4  1 O   A HOH 2448 ? ? O A HOH 3271 ? ? 2.11 
5  1 O   A HOH 2415 ? ? O A HOH 2451 ? ? 2.11 
6  1 OE1 B GLN 793  ? ? O B HOH 2101 ? ? 2.12 
7  1 OE1 A GLN 793  ? ? O A HOH 2101 ? ? 2.12 
8  1 OH  A TYR 995  ? ? O A HOH 2102 ? ? 2.12 
9  1 O4  A SO4 2011 ? ? O A HOH 2103 ? ? 2.13 
10 1 O   B SER 1075 ? ? O B HOH 2102 ? ? 2.14 
11 1 OE2 A GLU 234  ? ? O A HOH 2104 ? ? 2.14 
12 1 O   B HOH 2102 ? ? O B HOH 2422 ? ? 2.14 
13 1 O   B HOH 2347 ? ? O B HOH 2769 ? ? 2.15 
14 1 O   B HOH 2941 ? ? O B HOH 3300 ? ? 2.15 
15 1 O   B HOH 2104 ? ? O B HOH 3207 ? ? 2.15 
16 1 OE1 B GLU 539  ? ? O B HOH 2103 ? ? 2.15 
17 1 O   B HOH 3019 ? ? O B HOH 3125 ? ? 2.17 
18 1 O   B HOH 2593 ? ? O B HOH 3240 ? ? 2.17 
19 1 O   B HOH 2588 ? ? O B HOH 3013 ? ? 2.18 
20 1 O   A LEU 1183 ? ? O A HOH 2105 ? ? 2.18 
21 1 O   B HOH 2153 ? ? O B HOH 2969 ? ? 2.19 
22 1 OE2 B GLU 309  ? ? O B HOH 2104 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 3060 ? ? 1_555 O B HOH 2107 ? ? 1_455 2.09 
2 1 O A HOH 2112 ? ? 1_555 O B HOH 3106 ? ? 2_556 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 22   ? ? -156.71 56.84   
2  1 ASN A 129  ? ? -68.45  98.66   
3  1 GLU A 225  ? ? -173.30 145.39  
4  1 GLU A 308  ? ? -118.59 -136.12 
5  1 MET A 452  ? ? -148.26 -50.52  
6  1 LYS A 465  ? ? -118.99 -124.11 
7  1 ASP A 597  ? ? -172.58 98.34   
8  1 THR A 689  ? ? -130.60 -44.90  
9  1 THR A 811  ? ? -125.09 -157.85 
10 1 GLN A 842  ? ? -94.83  50.96   
11 1 GLN A 938  ? ? -101.21 -72.87  
12 1 LEU A 970  ? ? -97.95  -88.53  
13 1 GLN A 1008 ? ? -118.09 77.90   
14 1 ALA B 22   ? ? -157.94 59.44   
15 1 ASN B 129  ? ? -71.44  42.11   
16 1 SER B 132  ? ? -109.51 40.50   
17 1 HIS B 133  ? ? -149.75 -35.82  
18 1 LEU B 223  ? ? 78.53   -0.79   
19 1 GLU B 308  ? ? -115.74 -134.52 
20 1 MET B 452  ? ? -139.30 -45.92  
21 1 VAL B 460  ? ? -123.33 -52.73  
22 1 LYS B 465  ? ? -120.76 -125.20 
23 1 TYR B 485  ? ? -140.50 22.15   
24 1 ARG B 489  ? ? -91.07  -107.77 
25 1 ASP B 597  ? ? -167.46 99.03   
26 1 HIS B 694  ? ? -100.97 78.68   
27 1 THR B 811  ? ? -125.19 -153.42 
28 1 GLN B 842  ? ? -94.44  54.72   
29 1 LEU B 914  ? ? 175.96  70.50   
30 1 LEU B 970  ? ? -97.37  -88.02  
31 1 GLN B 1008 ? ? -116.99 77.18   
32 1 ASP B 1154 ? ? -159.69 88.99   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     744 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.077 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 -25.5445 65.9149 92.7467 0.1525 ? 0.0198 ? 0.0121  ? 0.1314 ? 0.0063  ? 0.1243 ? 0.6121 ? -0.0123 
? 0.1794 ? 0.0946 ? -0.0041 ? 0.1283 ? -0.0354 ? -0.1118 ? 0.0104  ? 0.0293 ? 0.0337 ? 0.0145  ? -0.0190 ? -0.0205 ? 0.0016  ? 
2 'X-RAY DIFFRACTION' ? refined 5.7734   31.1918 91.5254 0.1194 ? 0.0040 ? -0.0026 ? 0.1297 ? -0.0173 ? 0.1191 ? 0.1741 ? 0.0089  
? 0.0374 ? 0.2092 ? -0.0577 ? 0.2998 ? 0.0087  ? -0.0284 ? -0.0032 ? 0.0408 ? 0.0017 ? -0.0056 ? 0.0210  ? -0.0591 ? -0.0137 ? 
# 
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 3387 ? 5.85 . 
2 1 O ? B HOH 3470 ? 5.99 . 
3 1 O ? B HOH 3471 ? 6.13 . 
4 1 O ? B HOH 3472 ? 6.34 . 
5 1 O ? B HOH 3473 ? 6.35 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER -1  ? A SER 1   
2  1 Y 1 A MET 0   ? A MET 2   
3  1 Y 1 A MET 1   ? A MET 3   
4  1 Y 1 A SER 2   ? A SER 4   
5  1 Y 1 A PRO 3   ? A PRO 5   
6  1 Y 1 A ASN 4   ? A ASN 6   
7  1 Y 1 A PRO 5   ? A PRO 7   
8  1 Y 1 A LEU 6   ? A LEU 8   
9  1 Y 1 A GLN 7   ? A GLN 9   
10 1 Y 1 A LYS 8   ? A LYS 10  
11 1 Y 1 A PRO 9   ? A PRO 11  
12 1 Y 1 A ALA 10  ? A ALA 12  
13 1 Y 1 A ILE 11  ? A ILE 13  
14 1 Y 1 A ASP 12  ? A ASP 14  
15 1 Y 1 A ALA 13  ? A ALA 15  
16 1 Y 1 A SER 80  ? A SER 82  
17 1 Y 1 A GLY 81  ? A GLY 83  
18 1 Y 1 A GLY 135 ? A GLY 137 
19 1 Y 1 A GLY 136 ? A GLY 138 
20 1 Y 1 A GLU 492 ? A GLU 494 
21 1 Y 1 A ASN 493 ? A ASN 495 
22 1 Y 1 A GLY 494 ? A GLY 496 
23 1 Y 1 B SER -1  ? B SER 1   
24 1 Y 1 B MET 0   ? B MET 2   
25 1 Y 1 B MET 1   ? B MET 3   
26 1 Y 1 B SER 2   ? B SER 4   
27 1 Y 1 B PRO 3   ? B PRO 5   
28 1 Y 1 B ASN 4   ? B ASN 6   
29 1 Y 1 B PRO 5   ? B PRO 7   
30 1 Y 1 B LEU 6   ? B LEU 8   
31 1 Y 1 B GLN 7   ? B GLN 9   
32 1 Y 1 B LYS 8   ? B LYS 10  
33 1 Y 1 B PRO 9   ? B PRO 11  
34 1 Y 1 B ALA 10  ? B ALA 12  
35 1 Y 1 B ILE 11  ? B ILE 13  
36 1 Y 1 B ASP 12  ? B ASP 14  
37 1 Y 1 B ALA 13  ? B ALA 15  
38 1 Y 1 B HIS 79  ? B HIS 81  
39 1 Y 1 B SER 80  ? B SER 82  
40 1 Y 1 B GLY 81  ? B GLY 83  
41 1 Y 1 B SER 82  ? B SER 84  
42 1 Y 1 B GLY 135 ? B GLY 137 
43 1 Y 1 B GLY 136 ? B GLY 138 
44 1 Y 1 B SER 137 ? B SER 139 
# 
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  
A1BDD C01    C  N N 39  
A1BDD C03    C  Y N 40  
A1BDD C04    C  Y N 41  
A1BDD C05    C  Y N 42  
A1BDD C06    C  Y N 43  
A1BDD C07    C  N N 44  
A1BDD C09    C  Y N 45  
A1BDD C10    C  Y N 46  
A1BDD O02    O  N N 47  
A1BDD O08    O  N N 48  
A1BDD H1     H  N N 49  
A1BDD H2     H  N N 50  
A1BDD H3     H  N N 51  
A1BDD H4     H  N N 52  
A1BDD H5     H  N N 53  
A1BDD H6     H  N N 54  
A1BDD H7     H  N N 55  
A1BDD H8     H  N N 56  
A1BDD H9     H  N N 57  
A1BDD H10    H  N N 58  
ALA   N      N  N N 59  
ALA   CA     C  N S 60  
ALA   C      C  N N 61  
ALA   O      O  N N 62  
ALA   CB     C  N N 63  
ALA   OXT    O  N N 64  
ALA   H      H  N N 65  
ALA   H2     H  N N 66  
ALA   HA     H  N N 67  
ALA   HB1    H  N N 68  
ALA   HB2    H  N N 69  
ALA   HB3    H  N N 70  
ALA   HXT    H  N N 71  
ARG   N      N  N N 72  
ARG   CA     C  N S 73  
ARG   C      C  N N 74  
ARG   O      O  N N 75  
ARG   CB     C  N N 76  
ARG   CG     C  N N 77  
ARG   CD     C  N N 78  
ARG   NE     N  N N 79  
ARG   CZ     C  N N 80  
ARG   NH1    N  N N 81  
ARG   NH2    N  N N 82  
ARG   OXT    O  N N 83  
ARG   H      H  N N 84  
ARG   H2     H  N N 85  
ARG   HA     H  N N 86  
ARG   HB2    H  N N 87  
ARG   HB3    H  N N 88  
ARG   HG2    H  N N 89  
ARG   HG3    H  N N 90  
ARG   HD2    H  N N 91  
ARG   HD3    H  N N 92  
ARG   HE     H  N N 93  
ARG   HH11   H  N N 94  
ARG   HH12   H  N N 95  
ARG   HH21   H  N N 96  
ARG   HH22   H  N N 97  
ARG   HXT    H  N N 98  
ASN   N      N  N N 99  
ASN   CA     C  N S 100 
ASN   C      C  N N 101 
ASN   O      O  N N 102 
ASN   CB     C  N N 103 
ASN   CG     C  N N 104 
ASN   OD1    O  N N 105 
ASN   ND2    N  N N 106 
ASN   OXT    O  N N 107 
ASN   H      H  N N 108 
ASN   H2     H  N N 109 
ASN   HA     H  N N 110 
ASN   HB2    H  N N 111 
ASN   HB3    H  N N 112 
ASN   HD21   H  N N 113 
ASN   HD22   H  N N 114 
ASN   HXT    H  N N 115 
ASP   N      N  N N 116 
ASP   CA     C  N S 117 
ASP   C      C  N N 118 
ASP   O      O  N N 119 
ASP   CB     C  N N 120 
ASP   CG     C  N N 121 
ASP   OD1    O  N N 122 
ASP   OD2    O  N N 123 
ASP   OXT    O  N N 124 
ASP   H      H  N N 125 
ASP   H2     H  N N 126 
ASP   HA     H  N N 127 
ASP   HB2    H  N N 128 
ASP   HB3    H  N N 129 
ASP   HD2    H  N N 130 
ASP   HXT    H  N N 131 
CYS   N      N  N N 132 
CYS   CA     C  N R 133 
CYS   C      C  N N 134 
CYS   O      O  N N 135 
CYS   CB     C  N N 136 
CYS   SG     S  N N 137 
CYS   OXT    O  N N 138 
CYS   H      H  N N 139 
CYS   H2     H  N N 140 
CYS   HA     H  N N 141 
CYS   HB2    H  N N 142 
CYS   HB3    H  N N 143 
CYS   HG     H  N N 144 
CYS   HXT    H  N N 145 
FAD   PA     P  N R 146 
FAD   O1A    O  N N 147 
FAD   O2A    O  N N 148 
FAD   O5B    O  N N 149 
FAD   C5B    C  N N 150 
FAD   C4B    C  N R 151 
FAD   O4B    O  N N 152 
FAD   C3B    C  N S 153 
FAD   O3B    O  N N 154 
FAD   C2B    C  N R 155 
FAD   O2B    O  N N 156 
FAD   C1B    C  N R 157 
FAD   N9A    N  Y N 158 
FAD   C8A    C  Y N 159 
FAD   N7A    N  Y N 160 
FAD   C5A    C  Y N 161 
FAD   C6A    C  Y N 162 
FAD   N6A    N  N N 163 
FAD   N1A    N  Y N 164 
FAD   C2A    C  Y N 165 
FAD   N3A    N  Y N 166 
FAD   C4A    C  Y N 167 
FAD   N1     N  N N 168 
FAD   C2     C  N N 169 
FAD   O2     O  N N 170 
FAD   N3     N  N N 171 
FAD   C4     C  N N 172 
FAD   O4     O  N N 173 
FAD   C4X    C  N N 174 
FAD   N5     N  N N 175 
FAD   C5X    C  Y N 176 
FAD   C6     C  Y N 177 
FAD   C7     C  Y N 178 
FAD   C7M    C  N N 179 
FAD   C8     C  Y N 180 
FAD   C8M    C  N N 181 
FAD   C9     C  Y N 182 
FAD   C9A    C  Y N 183 
FAD   N10    N  N N 184 
FAD   C10    C  N N 185 
FAD   "C1'"  C  N N 186 
FAD   "C2'"  C  N S 187 
FAD   "O2'"  O  N N 188 
FAD   "C3'"  C  N S 189 
FAD   "O3'"  O  N N 190 
FAD   "C4'"  C  N R 191 
FAD   "O4'"  O  N N 192 
FAD   "C5'"  C  N N 193 
FAD   "O5'"  O  N N 194 
FAD   P      P  N R 195 
FAD   O1P    O  N N 196 
FAD   O2P    O  N N 197 
FAD   O3P    O  N N 198 
FAD   HOA2   H  N N 199 
FAD   H51A   H  N N 200 
FAD   H52A   H  N N 201 
FAD   H4B    H  N N 202 
FAD   H3B    H  N N 203 
FAD   HO3A   H  N N 204 
FAD   H2B    H  N N 205 
FAD   HO2A   H  N N 206 
FAD   H1B    H  N N 207 
FAD   H8A    H  N N 208 
FAD   H61A   H  N N 209 
FAD   H62A   H  N N 210 
FAD   H2A    H  N N 211 
FAD   HN3    H  N N 212 
FAD   H6     H  N N 213 
FAD   HM71   H  N N 214 
FAD   HM72   H  N N 215 
FAD   HM73   H  N N 216 
FAD   HM81   H  N N 217 
FAD   HM82   H  N N 218 
FAD   HM83   H  N N 219 
FAD   H9     H  N N 220 
FAD   "H1'1" H  N N 221 
FAD   "H1'2" H  N N 222 
FAD   "H2'"  H  N N 223 
FAD   "HO2'" H  N N 224 
FAD   "H3'"  H  N N 225 
FAD   "HO3'" H  N N 226 
FAD   "H4'"  H  N N 227 
FAD   "HO4'" H  N N 228 
FAD   "H5'1" H  N N 229 
FAD   "H5'2" H  N N 230 
FAD   HOP2   H  N N 231 
FMT   C      C  N N 232 
FMT   O1     O  N N 233 
FMT   O2     O  N N 234 
FMT   H      H  N N 235 
FMT   HO2    H  N N 236 
GLN   N      N  N N 237 
GLN   CA     C  N S 238 
GLN   C      C  N N 239 
GLN   O      O  N N 240 
GLN   CB     C  N N 241 
GLN   CG     C  N N 242 
GLN   CD     C  N N 243 
GLN   OE1    O  N N 244 
GLN   NE2    N  N N 245 
GLN   OXT    O  N N 246 
GLN   H      H  N N 247 
GLN   H2     H  N N 248 
GLN   HA     H  N N 249 
GLN   HB2    H  N N 250 
GLN   HB3    H  N N 251 
GLN   HG2    H  N N 252 
GLN   HG3    H  N N 253 
GLN   HE21   H  N N 254 
GLN   HE22   H  N N 255 
GLN   HXT    H  N N 256 
GLU   N      N  N N 257 
GLU   CA     C  N S 258 
GLU   C      C  N N 259 
GLU   O      O  N N 260 
GLU   CB     C  N N 261 
GLU   CG     C  N N 262 
GLU   CD     C  N N 263 
GLU   OE1    O  N N 264 
GLU   OE2    O  N N 265 
GLU   OXT    O  N N 266 
GLU   H      H  N N 267 
GLU   H2     H  N N 268 
GLU   HA     H  N N 269 
GLU   HB2    H  N N 270 
GLU   HB3    H  N N 271 
GLU   HG2    H  N N 272 
GLU   HG3    H  N N 273 
GLU   HE2    H  N N 274 
GLU   HXT    H  N N 275 
GLY   N      N  N N 276 
GLY   CA     C  N N 277 
GLY   C      C  N N 278 
GLY   O      O  N N 279 
GLY   OXT    O  N N 280 
GLY   H      H  N N 281 
GLY   H2     H  N N 282 
GLY   HA2    H  N N 283 
GLY   HA3    H  N N 284 
GLY   HXT    H  N N 285 
HIS   N      N  N N 286 
HIS   CA     C  N S 287 
HIS   C      C  N N 288 
HIS   O      O  N N 289 
HIS   CB     C  N N 290 
HIS   CG     C  Y N 291 
HIS   ND1    N  Y N 292 
HIS   CD2    C  Y N 293 
HIS   CE1    C  Y N 294 
HIS   NE2    N  Y N 295 
HIS   OXT    O  N N 296 
HIS   H      H  N N 297 
HIS   H2     H  N N 298 
HIS   HA     H  N N 299 
HIS   HB2    H  N N 300 
HIS   HB3    H  N N 301 
HIS   HD1    H  N N 302 
HIS   HD2    H  N N 303 
HIS   HE1    H  N N 304 
HIS   HE2    H  N N 305 
HIS   HXT    H  N N 306 
HOH   O      O  N N 307 
HOH   H1     H  N N 308 
HOH   H2     H  N N 309 
ILE   N      N  N N 310 
ILE   CA     C  N S 311 
ILE   C      C  N N 312 
ILE   O      O  N N 313 
ILE   CB     C  N S 314 
ILE   CG1    C  N N 315 
ILE   CG2    C  N N 316 
ILE   CD1    C  N N 317 
ILE   OXT    O  N N 318 
ILE   H      H  N N 319 
ILE   H2     H  N N 320 
ILE   HA     H  N N 321 
ILE   HB     H  N N 322 
ILE   HG12   H  N N 323 
ILE   HG13   H  N N 324 
ILE   HG21   H  N N 325 
ILE   HG22   H  N N 326 
ILE   HG23   H  N N 327 
ILE   HD11   H  N N 328 
ILE   HD12   H  N N 329 
ILE   HD13   H  N N 330 
ILE   HXT    H  N N 331 
LEU   N      N  N N 332 
LEU   CA     C  N S 333 
LEU   C      C  N N 334 
LEU   O      O  N N 335 
LEU   CB     C  N N 336 
LEU   CG     C  N N 337 
LEU   CD1    C  N N 338 
LEU   CD2    C  N N 339 
LEU   OXT    O  N N 340 
LEU   H      H  N N 341 
LEU   H2     H  N N 342 
LEU   HA     H  N N 343 
LEU   HB2    H  N N 344 
LEU   HB3    H  N N 345 
LEU   HG     H  N N 346 
LEU   HD11   H  N N 347 
LEU   HD12   H  N N 348 
LEU   HD13   H  N N 349 
LEU   HD21   H  N N 350 
LEU   HD22   H  N N 351 
LEU   HD23   H  N N 352 
LEU   HXT    H  N N 353 
LYS   N      N  N N 354 
LYS   CA     C  N S 355 
LYS   C      C  N N 356 
LYS   O      O  N N 357 
LYS   CB     C  N N 358 
LYS   CG     C  N N 359 
LYS   CD     C  N N 360 
LYS   CE     C  N N 361 
LYS   NZ     N  N N 362 
LYS   OXT    O  N N 363 
LYS   H      H  N N 364 
LYS   H2     H  N N 365 
LYS   HA     H  N N 366 
LYS   HB2    H  N N 367 
LYS   HB3    H  N N 368 
LYS   HG2    H  N N 369 
LYS   HG3    H  N N 370 
LYS   HD2    H  N N 371 
LYS   HD3    H  N N 372 
LYS   HE2    H  N N 373 
LYS   HE3    H  N N 374 
LYS   HZ1    H  N N 375 
LYS   HZ2    H  N N 376 
LYS   HZ3    H  N N 377 
LYS   HXT    H  N N 378 
MET   N      N  N N 379 
MET   CA     C  N S 380 
MET   C      C  N N 381 
MET   O      O  N N 382 
MET   CB     C  N N 383 
MET   CG     C  N N 384 
MET   SD     S  N N 385 
MET   CE     C  N N 386 
MET   OXT    O  N N 387 
MET   H      H  N N 388 
MET   H2     H  N N 389 
MET   HA     H  N N 390 
MET   HB2    H  N N 391 
MET   HB3    H  N N 392 
MET   HG2    H  N N 393 
MET   HG3    H  N N 394 
MET   HE1    H  N N 395 
MET   HE2    H  N N 396 
MET   HE3    H  N N 397 
MET   HXT    H  N N 398 
MG    MG     MG N N 399 
NAD   PA     P  N S 400 
NAD   O1A    O  N N 401 
NAD   O2A    O  N N 402 
NAD   O5B    O  N N 403 
NAD   C5B    C  N N 404 
NAD   C4B    C  N R 405 
NAD   O4B    O  N N 406 
NAD   C3B    C  N S 407 
NAD   O3B    O  N N 408 
NAD   C2B    C  N R 409 
NAD   O2B    O  N N 410 
NAD   C1B    C  N R 411 
NAD   N9A    N  Y N 412 
NAD   C8A    C  Y N 413 
NAD   N7A    N  Y N 414 
NAD   C5A    C  Y N 415 
NAD   C6A    C  Y N 416 
NAD   N6A    N  N N 417 
NAD   N1A    N  Y N 418 
NAD   C2A    C  Y N 419 
NAD   N3A    N  Y N 420 
NAD   C4A    C  Y N 421 
NAD   O3     O  N N 422 
NAD   PN     P  N N 423 
NAD   O1N    O  N N 424 
NAD   O2N    O  N N 425 
NAD   O5D    O  N N 426 
NAD   C5D    C  N N 427 
NAD   C4D    C  N R 428 
NAD   O4D    O  N N 429 
NAD   C3D    C  N S 430 
NAD   O3D    O  N N 431 
NAD   C2D    C  N R 432 
NAD   O2D    O  N N 433 
NAD   C1D    C  N R 434 
NAD   N1N    N  Y N 435 
NAD   C2N    C  Y N 436 
NAD   C3N    C  Y N 437 
NAD   C7N    C  N N 438 
NAD   O7N    O  N N 439 
NAD   N7N    N  N N 440 
NAD   C4N    C  Y N 441 
NAD   C5N    C  Y N 442 
NAD   C6N    C  Y N 443 
NAD   HOA2   H  N N 444 
NAD   H51A   H  N N 445 
NAD   H52A   H  N N 446 
NAD   H4B    H  N N 447 
NAD   H3B    H  N N 448 
NAD   HO3A   H  N N 449 
NAD   H2B    H  N N 450 
NAD   HO2A   H  N N 451 
NAD   H1B    H  N N 452 
NAD   H8A    H  N N 453 
NAD   H61A   H  N N 454 
NAD   H62A   H  N N 455 
NAD   H2A    H  N N 456 
NAD   H51N   H  N N 457 
NAD   H52N   H  N N 458 
NAD   H4D    H  N N 459 
NAD   H3D    H  N N 460 
NAD   HO3N   H  N N 461 
NAD   H2D    H  N N 462 
NAD   HO2N   H  N N 463 
NAD   H1D    H  N N 464 
NAD   H2N    H  N N 465 
NAD   H71N   H  N N 466 
NAD   H72N   H  N N 467 
NAD   H4N    H  N N 468 
NAD   H5N    H  N N 469 
NAD   H6N    H  N N 470 
PEG   C1     C  N N 471 
PEG   O1     O  N N 472 
PEG   C2     C  N N 473 
PEG   O2     O  N N 474 
PEG   C3     C  N N 475 
PEG   C4     C  N N 476 
PEG   O4     O  N N 477 
PEG   H11    H  N N 478 
PEG   H12    H  N N 479 
PEG   HO1    H  N N 480 
PEG   H21    H  N N 481 
PEG   H22    H  N N 482 
PEG   H31    H  N N 483 
PEG   H32    H  N N 484 
PEG   H41    H  N N 485 
PEG   H42    H  N N 486 
PEG   HO4    H  N N 487 
PGE   C1     C  N N 488 
PGE   O1     O  N N 489 
PGE   C2     C  N N 490 
PGE   O2     O  N N 491 
PGE   C3     C  N N 492 
PGE   C4     C  N N 493 
PGE   O4     O  N N 494 
PGE   C6     C  N N 495 
PGE   C5     C  N N 496 
PGE   O3     O  N N 497 
PGE   H1     H  N N 498 
PGE   H12    H  N N 499 
PGE   HO1    H  N N 500 
PGE   H2     H  N N 501 
PGE   H22    H  N N 502 
PGE   H3     H  N N 503 
PGE   H32    H  N N 504 
PGE   H4     H  N N 505 
PGE   H42    H  N N 506 
PGE   HO4    H  N N 507 
PGE   H6     H  N N 508 
PGE   H62    H  N N 509 
PGE   H5     H  N N 510 
PGE   H52    H  N N 511 
PHE   N      N  N N 512 
PHE   CA     C  N S 513 
PHE   C      C  N N 514 
PHE   O      O  N N 515 
PHE   CB     C  N N 516 
PHE   CG     C  Y N 517 
PHE   CD1    C  Y N 518 
PHE   CD2    C  Y N 519 
PHE   CE1    C  Y N 520 
PHE   CE2    C  Y N 521 
PHE   CZ     C  Y N 522 
PHE   OXT    O  N N 523 
PHE   H      H  N N 524 
PHE   H2     H  N N 525 
PHE   HA     H  N N 526 
PHE   HB2    H  N N 527 
PHE   HB3    H  N N 528 
PHE   HD1    H  N N 529 
PHE   HD2    H  N N 530 
PHE   HE1    H  N N 531 
PHE   HE2    H  N N 532 
PHE   HZ     H  N N 533 
PHE   HXT    H  N N 534 
PRO   N      N  N N 535 
PRO   CA     C  N S 536 
PRO   C      C  N N 537 
PRO   O      O  N N 538 
PRO   CB     C  N N 539 
PRO   CG     C  N N 540 
PRO   CD     C  N N 541 
PRO   OXT    O  N N 542 
PRO   H      H  N N 543 
PRO   HA     H  N N 544 
PRO   HB2    H  N N 545 
PRO   HB3    H  N N 546 
PRO   HG2    H  N N 547 
PRO   HG3    H  N N 548 
PRO   HD2    H  N N 549 
PRO   HD3    H  N N 550 
PRO   HXT    H  N N 551 
SER   N      N  N N 552 
SER   CA     C  N S 553 
SER   C      C  N N 554 
SER   O      O  N N 555 
SER   CB     C  N N 556 
SER   OG     O  N N 557 
SER   OXT    O  N N 558 
SER   H      H  N N 559 
SER   H2     H  N N 560 
SER   HA     H  N N 561 
SER   HB2    H  N N 562 
SER   HB3    H  N N 563 
SER   HG     H  N N 564 
SER   HXT    H  N N 565 
SO4   S      S  N N 566 
SO4   O1     O  N N 567 
SO4   O2     O  N N 568 
SO4   O3     O  N N 569 
SO4   O4     O  N N 570 
THR   N      N  N N 571 
THR   CA     C  N S 572 
THR   C      C  N N 573 
THR   O      O  N N 574 
THR   CB     C  N R 575 
THR   OG1    O  N N 576 
THR   CG2    C  N N 577 
THR   OXT    O  N N 578 
THR   H      H  N N 579 
THR   H2     H  N N 580 
THR   HA     H  N N 581 
THR   HB     H  N N 582 
THR   HG1    H  N N 583 
THR   HG21   H  N N 584 
THR   HG22   H  N N 585 
THR   HG23   H  N N 586 
THR   HXT    H  N N 587 
TRP   N      N  N N 588 
TRP   CA     C  N S 589 
TRP   C      C  N N 590 
TRP   O      O  N N 591 
TRP   CB     C  N N 592 
TRP   CG     C  Y N 593 
TRP   CD1    C  Y N 594 
TRP   CD2    C  Y N 595 
TRP   NE1    N  Y N 596 
TRP   CE2    C  Y N 597 
TRP   CE3    C  Y N 598 
TRP   CZ2    C  Y N 599 
TRP   CZ3    C  Y N 600 
TRP   CH2    C  Y N 601 
TRP   OXT    O  N N 602 
TRP   H      H  N N 603 
TRP   H2     H  N N 604 
TRP   HA     H  N N 605 
TRP   HB2    H  N N 606 
TRP   HB3    H  N N 607 
TRP   HD1    H  N N 608 
TRP   HE1    H  N N 609 
TRP   HE3    H  N N 610 
TRP   HZ2    H  N N 611 
TRP   HZ3    H  N N 612 
TRP   HH2    H  N N 613 
TRP   HXT    H  N N 614 
TYR   N      N  N N 615 
TYR   CA     C  N S 616 
TYR   C      C  N N 617 
TYR   O      O  N N 618 
TYR   CB     C  N N 619 
TYR   CG     C  Y N 620 
TYR   CD1    C  Y N 621 
TYR   CD2    C  Y N 622 
TYR   CE1    C  Y N 623 
TYR   CE2    C  Y N 624 
TYR   CZ     C  Y N 625 
TYR   OH     O  N N 626 
TYR   OXT    O  N N 627 
TYR   H      H  N N 628 
TYR   H2     H  N N 629 
TYR   HA     H  N N 630 
TYR   HB2    H  N N 631 
TYR   HB3    H  N N 632 
TYR   HD1    H  N N 633 
TYR   HD2    H  N N 634 
TYR   HE1    H  N N 635 
TYR   HE2    H  N N 636 
TYR   HH     H  N N 637 
TYR   HXT    H  N N 638 
VAL   N      N  N N 639 
VAL   CA     C  N S 640 
VAL   C      C  N N 641 
VAL   O      O  N N 642 
VAL   CB     C  N N 643 
VAL   CG1    C  N N 644 
VAL   CG2    C  N N 645 
VAL   OXT    O  N N 646 
VAL   H      H  N N 647 
VAL   H2     H  N N 648 
VAL   HA     H  N N 649 
VAL   HB     H  N N 650 
VAL   HG11   H  N N 651 
VAL   HG12   H  N N 652 
VAL   HG13   H  N N 653 
VAL   HG21   H  N N 654 
VAL   HG22   H  N N 655 
VAL   HG23   H  N N 656 
VAL   HXT    H  N N 657 
# 
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  
A1BDD O02   C01    sing N N 38  
A1BDD O02   C03    sing N N 39  
A1BDD C10   C03    doub Y N 40  
A1BDD C10   C09    sing Y N 41  
A1BDD C03   C04    sing Y N 42  
A1BDD C09   C06    doub Y N 43  
A1BDD C04   C05    doub Y N 44  
A1BDD C06   C05    sing Y N 45  
A1BDD C06   C07    sing N N 46  
A1BDD C07   O08    sing N N 47  
A1BDD C01   H1     sing N N 48  
A1BDD C01   H2     sing N N 49  
A1BDD C01   H3     sing N N 50  
A1BDD C04   H4     sing N N 51  
A1BDD C05   H5     sing N N 52  
A1BDD C07   H6     sing N N 53  
A1BDD C07   H7     sing N N 54  
A1BDD C09   H8     sing N N 55  
A1BDD C10   H9     sing N N 56  
A1BDD O08   H10    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                    9DL9 
_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]   0.009926 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002905 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009808 
_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]   0.008259 
_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   ? -48.931 93.541  103.846 1.00 51.98 ? 14   ALA   A N     1 
ATOM   2     C  CA    . ALA   A  1  16   ? -47.934 92.474  103.820 1.00 51.88 ? 14   ALA   A CA    1 
ATOM   3     C  C     . ALA   A  1  16   ? -48.597 91.106  103.940 1.00 48.77 ? 14   ALA   A C     1 
ATOM   4     O  O     . ALA   A  1  16   ? -49.376 90.868  104.860 1.00 48.65 ? 14   ALA   A O     1 
ATOM   5     C  CB    . ALA   A  1  16   ? -46.914 92.670  104.934 1.00 51.32 ? 14   ALA   A CB    1 
ATOM   6     N  N     . PRO   A  1  17   ? -48.286 90.201  103.012 1.00 45.64 ? 15   PRO   A N     1 
ATOM   7     C  CA    . PRO   A  1  17   ? -48.898 88.868  103.060 1.00 40.71 ? 15   PRO   A CA    1 
ATOM   8     C  C     . PRO   A  1  17   ? -48.387 88.082  104.257 1.00 39.14 ? 15   PRO   A C     1 
ATOM   9     O  O     . PRO   A  1  17   ? -47.209 88.159  104.618 1.00 39.40 ? 15   PRO   A O     1 
ATOM   10    C  CB    . PRO   A  1  17   ? -48.456 88.226  101.740 1.00 42.77 ? 15   PRO   A CB    1 
ATOM   11    C  CG    . PRO   A  1  17   ? -47.192 88.937  101.390 1.00 48.12 ? 15   PRO   A CG    1 
ATOM   12    C  CD    . PRO   A  1  17   ? -47.355 90.347  101.880 1.00 43.45 ? 15   PRO   A CD    1 
ATOM   13    N  N     . ALA   A  1  18   ? -49.292 87.333  104.879 1.00 36.63 ? 16   ALA   A N     1 
ATOM   14    C  CA    . ALA   A  1  18   ? -48.930 86.574  106.064 1.00 33.07 ? 16   ALA   A CA    1 
ATOM   15    C  C     . ALA   A  1  18   ? -47.874 85.535  105.700 1.00 28.96 ? 16   ALA   A C     1 
ATOM   16    O  O     . ALA   A  1  18   ? -47.945 84.932  104.624 1.00 29.60 ? 16   ALA   A O     1 
ATOM   17    C  CB    . ALA   A  1  18   ? -50.161 85.868  106.633 1.00 37.22 ? 16   ALA   A CB    1 
ATOM   18    N  N     . PRO   A  1  19   ? -46.893 85.303  106.563 1.00 27.68 ? 17   PRO   A N     1 
ATOM   19    C  CA    . PRO   A  1  19   ? -45.825 84.354  106.229 1.00 26.91 ? 17   PRO   A CA    1 
ATOM   20    C  C     . PRO   A  1  19   ? -46.387 82.959  106.033 1.00 25.70 ? 17   PRO   A C     1 
ATOM   21    O  O     . PRO   A  1  19   ? -47.191 82.474  106.832 1.00 28.23 ? 17   PRO   A O     1 
ATOM   22    C  CB    . PRO   A  1  19   ? -44.896 84.421  107.449 1.00 31.46 ? 17   PRO   A CB    1 
ATOM   23    C  CG    . PRO   A  1  19   ? -45.219 85.727  108.104 1.00 33.83 ? 17   PRO   A CG    1 
ATOM   24    C  CD    . PRO   A  1  19   ? -46.675 85.954  107.865 1.00 30.50 ? 17   PRO   A CD    1 
ATOM   25    N  N     . PHE   A  1  20   ? -45.976 82.331  104.934 1.00 24.49 ? 18   PHE   A N     1 
ATOM   26    C  CA    . PHE   A  1  20   ? -46.328 80.966  104.562 1.00 25.29 ? 18   PHE   A CA    1 
ATOM   27    C  C     . PHE   A  1  20   ? -47.808 80.778  104.275 1.00 25.55 ? 18   PHE   A C     1 
ATOM   28    O  O     . PHE   A  1  20   ? -48.265 79.637  104.188 1.00 26.74 ? 18   PHE   A O     1 
ATOM   29    C  CB    . PHE   A  1  20   ? -45.857 79.933  105.590 1.00 25.31 ? 18   PHE   A CB    1 
ATOM   30    C  CG    . PHE   A  1  20   ? -44.393 80.004  105.878 1.00 25.45 ? 18   PHE   A CG    1 
ATOM   31    C  CD1   . PHE   A  1  20   ? -43.483 79.498  104.974 1.00 23.67 ? 18   PHE   A CD1   1 
ATOM   32    C  CD2   . PHE   A  1  20   ? -43.926 80.580  107.053 1.00 26.15 ? 18   PHE   A CD2   1 
ATOM   33    C  CE1   . PHE   A  1  20   ? -42.121 79.560  105.231 1.00 24.42 ? 18   PHE   A CE1   1 
ATOM   34    C  CE2   . PHE   A  1  20   ? -42.571 80.638  107.317 1.00 27.90 ? 18   PHE   A CE2   1 
ATOM   35    C  CZ    . PHE   A  1  20   ? -41.670 80.127  106.406 1.00 27.89 ? 18   PHE   A CZ    1 
ATOM   36    N  N     . ALA   A  1  21   ? -48.569 81.860  104.130 1.00 26.74 ? 19   ALA   A N     1 
ATOM   37    C  CA    . ALA   A  1  21   ? -49.989 81.717  103.848 1.00 25.64 ? 19   ALA   A CA    1 
ATOM   38    C  C     . ALA   A  1  21   ? -50.248 81.147  102.462 1.00 30.20 ? 19   ALA   A C     1 
ATOM   39    O  O     . ALA   A  1  21   ? -51.347 80.648  102.208 1.00 31.70 ? 19   ALA   A O     1 
ATOM   40    C  CB    . ALA   A  1  21   ? -50.693 83.061  104.033 1.00 32.12 ? 19   ALA   A CB    1 
ATOM   41    N  N     . ASP   A  1  22   ? -49.270 81.199  101.566 1.00 25.44 ? 20   ASP   A N     1 
ATOM   42    C  CA    . ASP   A  1  22   ? -49.397 80.654  100.221 1.00 29.36 ? 20   ASP   A CA    1 
ATOM   43    C  C     . ASP   A  1  22   ? -48.231 79.728  99.916  1.00 24.38 ? 20   ASP   A C     1 
ATOM   44    O  O     . ASP   A  1  22   ? -47.713 79.699  98.796  1.00 25.28 ? 20   ASP   A O     1 
ATOM   45    C  CB    . ASP   A  1  22   ? -49.463 81.767  99.180  1.00 33.39 ? 20   ASP   A CB    1 
ATOM   46    C  CG    . ASP   A  1  22   ? -50.685 82.653  99.342  1.00 46.68 ? 20   ASP   A CG    1 
ATOM   47    O  OD1   . ASP   A  1  22   ? -51.722 82.175  99.848  1.00 46.99 ? 20   ASP   A OD1   1 
ATOM   48    O  OD2   . ASP   A  1  22   ? -50.602 83.837  98.953  1.00 58.83 ? 20   ASP   A OD2   1 
ATOM   49    N  N     . PHE   A  1  23   ? -47.788 78.965  100.917 1.00 21.73 ? 21   PHE   A N     1 
ATOM   50    C  CA    . PHE   A  1  23   ? -46.524 78.249  100.777 1.00 20.31 ? 21   PHE   A CA    1 
ATOM   51    C  C     . PHE   A  1  23   ? -46.575 77.228  99.646  1.00 20.51 ? 21   PHE   A C     1 
ATOM   52    O  O     . PHE   A  1  23   ? -45.751 77.257  98.727  1.00 19.24 ? 21   PHE   A O     1 
ATOM   53    C  CB    . PHE   A  1  23   ? -46.130 77.575  102.088 1.00 21.13 ? 21   PHE   A CB    1 
ATOM   54    C  CG    . PHE   A  1  23   ? -44.926 76.700  101.950 1.00 19.76 ? 21   PHE   A CG    1 
ATOM   55    C  CD1   . PHE   A  1  23   ? -43.702 77.249  101.612 1.00 20.91 ? 21   PHE   A CD1   1 
ATOM   56    C  CD2   . PHE   A  1  23   ? -45.016 75.329  102.123 1.00 21.94 ? 21   PHE   A CD2   1 
ATOM   57    C  CE1   . PHE   A  1  23   ? -42.578 76.449  101.457 1.00 20.33 ? 21   PHE   A CE1   1 
ATOM   58    C  CE2   . PHE   A  1  23   ? -43.900 74.519  101.978 1.00 24.13 ? 21   PHE   A CE2   1 
ATOM   59    C  CZ    . PHE   A  1  23   ? -42.679 75.079  101.638 1.00 21.32 ? 21   PHE   A CZ    1 
ATOM   60    N  N     . ALA   A  1  24   ? -47.532 76.304  99.702  1.00 20.33 ? 22   ALA   A N     1 
ATOM   61    C  CA    . ALA   A  1  24   ? -47.566 75.237  98.712  1.00 21.60 ? 22   ALA   A CA    1 
ATOM   62    C  C     . ALA   A  1  24   ? -48.969 74.660  98.584  1.00 19.35 ? 22   ALA   A C     1 
ATOM   63    O  O     . ALA   A  1  24   ? -49.160 73.446  98.741  1.00 20.45 ? 22   ALA   A O     1 
ATOM   64    C  CB    . ALA   A  1  24   ? -46.562 74.137  99.071  1.00 22.71 ? 22   ALA   A CB    1 
ATOM   65    N  N     . PRO   A  1  25   ? -49.969 75.478  98.278  1.00 22.13 ? 23   PRO   A N     1 
ATOM   66    C  CA    . PRO   A  1  25   ? -51.326 74.958  98.188  1.00 23.44 ? 23   PRO   A CA    1 
ATOM   67    C  C     . PRO   A  1  25   ? -51.420 73.960  97.052  1.00 22.46 ? 23   PRO   A C     1 
ATOM   68    O  O     . PRO   A  1  25   ? -50.859 74.186  95.971  1.00 21.90 ? 23   PRO   A O     1 
ATOM   69    C  CB    . PRO   A  1  25   ? -52.158 76.214  97.887  1.00 25.26 ? 23   PRO   A CB    1 
ATOM   70    C  CG    . PRO   A  1  25   ? -51.242 77.103  97.179  1.00 24.28 ? 23   PRO   A CG    1 
ATOM   71    C  CD    . PRO   A  1  25   ? -49.898 76.886  97.847  1.00 23.93 ? 23   PRO   A CD    1 
ATOM   72    N  N     . PRO   A  1  26   ? -52.104 72.841  97.262  1.00 20.53 ? 24   PRO   A N     1 
ATOM   73    C  CA    . PRO   A  1  26   ? -52.243 71.859  96.186  1.00 21.08 ? 24   PRO   A CA    1 
ATOM   74    C  C     . PRO   A  1  26   ? -53.078 72.418  95.045  1.00 19.83 ? 24   PRO   A C     1 
ATOM   75    O  O     . PRO   A  1  26   ? -53.883 73.341  95.213  1.00 23.11 ? 24   PRO   A O     1 
ATOM   76    C  CB    . PRO   A  1  26   ? -52.946 70.679  96.865  1.00 24.01 ? 24   PRO   A CB    1 
ATOM   77    C  CG    . PRO   A  1  26   ? -53.682 71.301  98.013  1.00 29.57 ? 24   PRO   A CG    1 
ATOM   78    C  CD    . PRO   A  1  26   ? -52.834 72.454  98.482  1.00 23.04 ? 24   PRO   A CD    1 
ATOM   79    N  N     . VAL   A  1  27   ? -52.861 71.830  93.864  1.00 19.68 ? 25   VAL   A N     1 
ATOM   80    C  CA    . VAL   A  1  27   ? -53.635 72.180  92.675  1.00 21.67 ? 25   VAL   A CA    1 
ATOM   81    C  C     . VAL   A  1  27   ? -55.120 72.058  92.946  1.00 21.94 ? 25   VAL   A C     1 
ATOM   82    O  O     . VAL   A  1  27   ? -55.914 72.918  92.545  1.00 25.57 ? 25   VAL   A O     1 
ATOM   83    C  CB    . VAL   A  1  27   ? -53.216 71.283  91.500  1.00 21.54 ? 25   VAL   A CB    1 
ATOM   84    C  CG1   . VAL   A  1  27   ? -54.165 71.474  90.340  1.00 23.21 ? 25   VAL   A CG1   1 
ATOM   85    C  CG2   . VAL   A  1  27   ? -51.793 71.595  91.081  1.00 21.27 ? 25   VAL   A CG2   1 
ATOM   86    N  N     . ARG   A  1  28   ? -55.522 70.996  93.633  1.00 23.68 ? 26   ARG   A N     1 
ATOM   87    C  CA    . ARG   A  1  28   ? -56.921 70.754  93.953  1.00 23.65 ? 26   ARG   A CA    1 
ATOM   88    C  C     . ARG   A  1  28   ? -56.984 70.087  95.318  1.00 27.81 ? 26   ARG   A C     1 
ATOM   89    O  O     . ARG   A  1  28   ? -55.976 69.552  95.796  1.00 24.29 ? 26   ARG   A O     1 
ATOM   90    C  CB    . ARG   A  1  28   ? -57.570 69.855  92.891  1.00 27.60 ? 26   ARG   A CB    1 
ATOM   91    C  CG    . ARG   A  1  28   ? -57.059 68.419  92.895  1.00 26.61 ? 26   ARG   A CG    1 
ATOM   92    C  CD    . ARG   A  1  28   ? -57.568 67.621  91.691  1.00 28.06 ? 26   ARG   A CD    1 
ATOM   93    N  NE    . ARG   A  1  28   ? -56.916 68.020  90.447  1.00 30.44 ? 26   ARG   A NE    1 
ATOM   94    C  CZ    . ARG   A  1  28   ? -57.431 68.870  89.570  1.00 33.84 ? 26   ARG   A CZ    1 
ATOM   95    N  NH1   . ARG   A  1  28   ? -58.640 69.384  89.730  1.00 31.71 ? 26   ARG   A NH1   1 
ATOM   96    N  NH2   . ARG   A  1  28   ? -56.710 69.225  88.515  1.00 29.47 ? 26   ARG   A NH2   1 
ATOM   97    N  N     . PRO   A  1  29   ? -58.140 70.113  95.982  1.00 23.82 ? 27   PRO   A N     1 
ATOM   98    C  CA    . PRO   A  1  29   ? -58.260 69.348  97.228  1.00 24.40 ? 27   PRO   A CA    1 
ATOM   99    C  C     . PRO   A  1  29   ? -58.075 67.869  96.930  1.00 25.04 ? 27   PRO   A C     1 
ATOM   100   O  O     . PRO   A  1  29   ? -58.554 67.355  95.920  1.00 26.71 ? 27   PRO   A O     1 
ATOM   101   C  CB    . PRO   A  1  29   ? -59.685 69.655  97.703  1.00 28.82 ? 27   PRO   A CB    1 
ATOM   102   C  CG    . PRO   A  1  29   ? -60.032 70.961  97.056  1.00 28.90 ? 27   PRO   A CG    1 
ATOM   103   C  CD    . PRO   A  1  29   ? -59.345 70.924  95.719  1.00 26.29 ? 27   PRO   A CD    1 
ATOM   104   N  N     . GLN   A  1  30   ? -57.353 67.189  97.807  1.00 25.92 ? 28   GLN   A N     1 
ATOM   105   C  CA    . GLN   A  1  30   ? -56.978 65.808  97.535  1.00 24.54 ? 28   GLN   A CA    1 
ATOM   106   C  C     . GLN   A  1  30   ? -58.139 64.883  97.886  1.00 24.63 ? 28   GLN   A C     1 
ATOM   107   O  O     . GLN   A  1  30   ? -58.550 64.808  99.048  1.00 26.80 ? 28   GLN   A O     1 
ATOM   108   C  CB    . GLN   A  1  30   ? -55.735 65.453  98.344  1.00 25.97 ? 28   GLN   A CB    1 
ATOM   109   C  CG    . GLN   A  1  30   ? -54.581 66.397  98.084  1.00 23.27 ? 28   GLN   A CG    1 
ATOM   110   C  CD    . GLN   A  1  30   ? -54.032 66.252  96.679  1.00 23.99 ? 28   GLN   A CD    1 
ATOM   111   O  OE1   . GLN   A  1  30   ? -53.340 65.285  96.374  1.00 21.97 ? 28   GLN   A OE1   1 
ATOM   112   N  NE2   . GLN   A  1  30   ? -54.349 67.204  95.815  1.00 21.80 ? 28   GLN   A NE2   1 
ATOM   113   N  N     . SER   A  1  31   ? -58.650 64.173  96.885  1.00 24.74 ? 29   SER   A N     1 
ATOM   114   C  CA    . SER   A  1  31   ? -59.739 63.232  97.110  1.00 22.98 ? 29   SER   A CA    1 
ATOM   115   C  C     . SER   A  1  31   ? -59.234 62.032  97.902  1.00 25.04 ? 29   SER   A C     1 
ATOM   116   O  O     . SER   A  1  31   ? -58.028 61.840  98.098  1.00 22.72 ? 29   SER   A O     1 
ATOM   117   C  CB    . SER   A  1  31   ? -60.274 62.725  95.776  1.00 23.01 ? 29   SER   A CB    1 
ATOM   118   O  OG    . SER   A  1  31   ? -59.268 61.957  95.124  1.00 21.56 ? 29   SER   A OG    1 
ATOM   119   N  N     . THR   A  1  32   ? -60.180 61.206  98.361  1.00 24.64 ? 30   THR   A N     1 
ATOM   120   C  CA    . THR   A  1  32   ? -59.818 59.963  99.029  1.00 21.44 ? 30   THR   A CA    1 
ATOM   121   C  C     . THR   A  1  32   ? -58.880 59.137  98.159  1.00 21.99 ? 30   THR   A C     1 
ATOM   122   O  O     . THR   A  1  32   ? -57.880 58.602  98.640  1.00 22.22 ? 30   THR   A O     1 
ATOM   123   C  CB    . THR   A  1  32   ? -61.086 59.169  99.361  1.00 25.18 ? 30   THR   A CB    1 
ATOM   124   O  OG1   . THR   A  1  32   ? -61.924 59.956  100.215 1.00 31.65 ? 30   THR   A OG1   1 
ATOM   125   C  CG2   . THR   A  1  32   ? -60.729 57.873  100.059 1.00 28.67 ? 30   THR   A CG2   1 
ATOM   126   N  N     . LEU   A  1  33   ? -59.186 59.035  96.870  1.00 20.81 ? 31   LEU   A N     1 
ATOM   127   C  CA    . LEU   A  1  33   ? -58.341 58.240  95.991  1.00 20.58 ? 31   LEU   A CA    1 
ATOM   128   C  C     . LEU   A  1  33   ? -56.967 58.869  95.831  1.00 21.37 ? 31   LEU   A C     1 
ATOM   129   O  O     . LEU   A  1  33   ? -55.959 58.158  95.782  1.00 20.08 ? 31   LEU   A O     1 
ATOM   130   C  CB    . LEU   A  1  33   ? -59.015 58.072  94.636  1.00 20.79 ? 31   LEU   A CB    1 
ATOM   131   C  CG    . LEU   A  1  33   ? -60.131 57.034  94.690  1.00 24.55 ? 31   LEU   A CG    1 
ATOM   132   C  CD1   . LEU   A  1  33   ? -60.999 57.135  93.460  1.00 22.54 ? 31   LEU   A CD1   1 
ATOM   133   C  CD2   . LEU   A  1  33   ? -59.571 55.626  94.837  1.00 29.50 ? 31   LEU   A CD2   1 
ATOM   134   N  N     . ARG   A  1  34   ? -56.902 60.196  95.733  1.00 19.14 ? 32   ARG   A N     1 
ATOM   135   C  CA    . ARG   A  1  34   ? -55.591 60.824  95.608  1.00 19.32 ? 32   ARG   A CA    1 
ATOM   136   C  C     . ARG   A  1  34   ? -54.792 60.658  96.883  1.00 19.18 ? 32   ARG   A C     1 
ATOM   137   O  O     . ARG   A  1  34   ? -53.574 60.458  96.835  1.00 20.36 ? 32   ARG   A O     1 
ATOM   138   C  CB    . ARG   A  1  34   ? -55.727 62.302  95.266  1.00 21.01 ? 32   ARG   A CB    1 
ATOM   139   C  CG    . ARG   A  1  34   ? -56.150 62.576  93.843  1.00 19.93 ? 32   ARG   A CG    1 
ATOM   140   C  CD    . ARG   A  1  34   ? -55.018 62.323  92.842  1.00 21.35 ? 32   ARG   A CD    1 
ATOM   141   N  NE    . ARG   A  1  34   ? -53.903 63.257  92.971  1.00 20.02 ? 32   ARG   A NE    1 
ATOM   142   C  CZ    . ARG   A  1  34   ? -53.820 64.425  92.338  1.00 20.81 ? 32   ARG   A CZ    1 
ATOM   143   N  NH1   . ARG   A  1  34   ? -54.787 64.850  91.536  1.00 21.83 ? 32   ARG   A NH1   1 
ATOM   144   N  NH2   . ARG   A  1  34   ? -52.740 65.185  92.511  1.00 22.48 ? 32   ARG   A NH2   1 
ATOM   145   N  N     . ARG   A  1  35   ? -55.462 60.734  98.037  1.00 19.90 ? 33   ARG   A N     1 
ATOM   146   C  CA    . ARG   A  1  35   ? -54.755 60.608  99.302  1.00 19.92 ? 33   ARG   A CA    1 
ATOM   147   C  C     . ARG   A  1  35   ? -54.184 59.211  99.481  1.00 19.28 ? 33   ARG   A C     1 
ATOM   148   O  O     . ARG   A  1  35   ? -53.111 59.056  100.076 1.00 21.53 ? 33   ARG   A O     1 
ATOM   149   C  CB    . ARG   A  1  35   ? -55.676 60.981  100.464 1.00 23.10 ? 33   ARG   A CB    1 
ATOM   150   C  CG    . ARG   A  1  35   ? -55.976 62.464  100.495 1.00 23.43 ? 33   ARG   A CG    1 
ATOM   151   C  CD    . ARG   A  1  35   ? -56.927 62.829  101.623 1.00 31.36 ? 33   ARG   A CD    1 
ATOM   152   N  NE    . ARG   A  1  35   ? -57.137 64.270  101.644 1.00 38.46 ? 33   ARG   A NE    1 
ATOM   153   C  CZ    . ARG   A  1  35   ? -56.324 65.130  102.243 1.00 47.53 ? 33   ARG   A CZ    1 
ATOM   154   N  NH1   . ARG   A  1  35   ? -55.267 64.720  102.924 1.00 51.11 ? 33   ARG   A NH1   1 
ATOM   155   N  NH2   . ARG   A  1  35   ? -56.573 66.434  102.148 1.00 46.10 ? 33   ARG   A NH2   1 
ATOM   156   N  N     . ALA   A  1  36   ? -54.874 58.197  98.953  1.00 19.87 ? 34   ALA   A N     1 
ATOM   157   C  CA    . ALA   A  1  36   ? -54.364 56.837  99.030  1.00 22.27 ? 34   ALA   A CA    1 
ATOM   158   C  C     . ALA   A  1  36   ? -53.109 56.680  98.198  1.00 20.02 ? 34   ALA   A C     1 
ATOM   159   O  O     . ALA   A  1  36   ? -52.219 55.910  98.561  1.00 22.45 ? 34   ALA   A O     1 
ATOM   160   C  CB    . ALA   A  1  36   ? -55.429 55.842  98.576  1.00 23.38 ? 34   ALA   A CB    1 
ATOM   161   N  N     . ILE   A  1  37   ? -53.011 57.419  97.091  1.00 18.61 ? 35   ILE   A N     1 
ATOM   162   C  CA    . ILE   A  1  37   ? -51.776 57.435  96.323  1.00 18.89 ? 35   ILE   A CA    1 
ATOM   163   C  C     . ILE   A  1  37   ? -50.649 58.018  97.156  1.00 18.51 ? 35   ILE   A C     1 
ATOM   164   O  O     . ILE   A  1  37   ? -49.597 57.397  97.338  1.00 18.52 ? 35   ILE   A O     1 
ATOM   165   C  CB    . ILE   A  1  37   ? -51.981 58.223  95.022  1.00 17.53 ? 35   ILE   A CB    1 
ATOM   166   C  CG1   . ILE   A  1  37   ? -52.933 57.482  94.096  1.00 18.06 ? 35   ILE   A CG1   1 
ATOM   167   C  CG2   . ILE   A  1  37   ? -50.653 58.398  94.332  1.00 17.77 ? 35   ILE   A CG2   1 
ATOM   168   C  CD1   . ILE   A  1  37   ? -53.417 58.340  92.949  1.00 17.86 ? 35   ILE   A CD1   1 
ATOM   169   N  N     . THR   A  1  38   ? -50.857 59.221  97.690  1.00 18.19 ? 36   THR   A N     1 
ATOM   170   C  CA    . THR   A  1  38   ? -49.789 59.875  98.428  1.00 19.07 ? 36   THR   A CA    1 
ATOM   171   C  C     . THR   A  1  38   ? -49.365 59.044  99.632  1.00 18.89 ? 36   THR   A C     1 
ATOM   172   O  O     . THR   A  1  38   ? -48.173 58.979  99.954  1.00 19.92 ? 36   THR   A O     1 
ATOM   173   C  CB    . THR   A  1  38   ? -50.247 61.263  98.859  1.00 19.77 ? 36   THR   A CB    1 
ATOM   174   O  OG1   . THR   A  1  38   ? -50.764 61.962  97.722  1.00 19.73 ? 36   THR   A OG1   1 
ATOM   175   C  CG2   . THR   A  1  38   ? -49.102 62.036  99.455  1.00 20.39 ? 36   THR   A CG2   1 
ATOM   176   N  N     . ALA   A  1  39   ? -50.323 58.367  100.267 1.00 20.02 ? 37   ALA   A N     1 
ATOM   177   C  CA    . ALA   A  1  39   ? -50.015 57.571  101.448 1.00 20.56 ? 37   ALA   A CA    1 
ATOM   178   C  C     . ALA   A  1  39   ? -49.066 56.426  101.136 1.00 22.88 ? 37   ALA   A C     1 
ATOM   179   O  O     . ALA   A  1  39   ? -48.349 55.962  102.029 1.00 24.43 ? 37   ALA   A O     1 
ATOM   180   C  CB    . ALA   A  1  39   ? -51.307 57.029  102.063 1.00 22.00 ? 37   ALA   A CB    1 
ATOM   181   N  N     . ALA   A  1  40   ? -49.038 55.959  99.892  1.00 19.25 ? 38   ALA   A N     1 
ATOM   182   C  CA    . ALA   A  1  40   ? -48.202 54.828  99.513  1.00 20.16 ? 38   ALA   A CA    1 
ATOM   183   C  C     . ALA   A  1  40   ? -46.839 55.242  98.988  1.00 20.05 ? 38   ALA   A C     1 
ATOM   184   O  O     . ALA   A  1  40   ? -46.031 54.366  98.657  1.00 20.95 ? 38   ALA   A O     1 
ATOM   185   C  CB    . ALA   A  1  40   ? -48.899 53.986  98.447  1.00 20.57 ? 38   ALA   A CB    1 
ATOM   186   N  N     . TYR   A  1  41   ? -46.565 56.549  98.923  1.00 17.90 ? 39   TYR   A N     1 
ATOM   187   C  CA    . TYR   A  1  41   ? -45.402 57.060  98.195  1.00 17.47 ? 39   TYR   A CA    1 
ATOM   188   C  C     . TYR   A  1  41   ? -44.117 56.331  98.576  1.00 19.61 ? 39   TYR   A C     1 
ATOM   189   O  O     . TYR   A  1  41   ? -43.366 55.880  97.707  1.00 19.19 ? 39   TYR   A O     1 
ATOM   190   C  CB    . TYR   A  1  41   ? -45.300 58.562  98.459  1.00 19.33 ? 39   TYR   A CB    1 
ATOM   191   C  CG    . TYR   A  1  41   ? -44.528 59.417  97.473  1.00 17.82 ? 39   TYR   A CG    1 
ATOM   192   C  CD1   . TYR   A  1  41   ? -43.456 58.925  96.748  1.00 18.86 ? 39   TYR   A CD1   1 
ATOM   193   C  CD2   . TYR   A  1  41   ? -44.877 60.749  97.299  1.00 18.77 ? 39   TYR   A CD2   1 
ATOM   194   C  CE1   . TYR   A  1  41   ? -42.758 59.742  95.872  1.00 17.40 ? 39   TYR   A CE1   1 
ATOM   195   C  CE2   . TYR   A  1  41   ? -44.197 61.566  96.433  1.00 19.68 ? 39   TYR   A CE2   1 
ATOM   196   C  CZ    . TYR   A  1  41   ? -43.133 61.063  95.727  1.00 17.86 ? 39   TYR   A CZ    1 
ATOM   197   O  OH    . TYR   A  1  41   ? -42.445 61.893  94.880  1.00 18.40 ? 39   TYR   A OH    1 
ATOM   198   N  N     . ARG   A  1  42   ? -43.857 56.182  99.869  1.00 20.16 ? 40   ARG   A N     1 
ATOM   199   C  CA    . ARG   A  1  42   ? -42.629 55.536  100.322 1.00 20.88 ? 40   ARG   A CA    1 
ATOM   200   C  C     . ARG   A  1  42   ? -42.943 54.443  101.325 1.00 19.98 ? 40   ARG   A C     1 
ATOM   201   O  O     . ARG   A  1  42   ? -42.184 54.197  102.275 1.00 24.12 ? 40   ARG   A O     1 
ATOM   202   C  CB    . ARG   A  1  42   ? -41.634 56.556  100.860 1.00 23.42 ? 40   ARG   A CB    1 
ATOM   203   C  CG    . ARG   A  1  42   ? -41.103 57.452  99.767  1.00 22.21 ? 40   ARG   A CG    1 
ATOM   204   C  CD    . ARG   A  1  42   ? -40.329 58.617  100.296 1.00 24.39 ? 40   ARG   A CD    1 
ATOM   205   N  NE    . ARG   A  1  42   ? -40.346 59.666  99.289  1.00 22.79 ? 40   ARG   A NE    1 
ATOM   206   C  CZ    . ARG   A  1  42   ? -39.529 59.718  98.249  1.00 20.27 ? 40   ARG   A CZ    1 
ATOM   207   N  NH1   . ARG   A  1  42   ? -38.522 58.862  98.112  1.00 20.72 ? 40   ARG   A NH1   1 
ATOM   208   N  NH2   . ARG   A  1  42   ? -39.722 60.651  97.322  1.00 20.02 ? 40   ARG   A NH2   1 
ATOM   209   N  N     . ARG   A  1  43   ? -44.060 53.765  101.103 1.00 21.02 ? 41   ARG   A N     1 
ATOM   210   C  CA    . ARG   A  1  43   ? -44.499 52.699  101.987 1.00 21.85 ? 41   ARG   A CA    1 
ATOM   211   C  C     . ARG   A  1  43   ? -43.425 51.619  102.057 1.00 24.11 ? 41   ARG   A C     1 
ATOM   212   O  O     . ARG   A  1  43   ? -42.851 51.245  101.030 1.00 22.75 ? 41   ARG   A O     1 
ATOM   213   C  CB    . ARG   A  1  43   ? -45.786 52.094  101.439 1.00 21.77 ? 41   ARG   A CB    1 
ATOM   214   C  CG    . ARG   A  1  43   ? -46.345 50.920  102.244 1.00 23.52 ? 41   ARG   A CG    1 
ATOM   215   C  CD    . ARG   A  1  43   ? -47.770 50.659  101.830 1.00 24.93 ? 41   ARG   A CD    1 
ATOM   216   N  NE    . ARG   A  1  43   ? -48.610 51.794  102.196 1.00 23.57 ? 41   ARG   A NE    1 
ATOM   217   C  CZ    . ARG   A  1  43   ? -49.748 52.116  101.599 1.00 23.50 ? 41   ARG   A CZ    1 
ATOM   218   N  NH1   . ARG   A  1  43   ? -50.218 51.414  100.582 1.00 23.51 ? 41   ARG   A NH1   1 
ATOM   219   N  NH2   . ARG   A  1  43   ? -50.423 53.178  102.027 1.00 25.68 ? 41   ARG   A NH2   1 
ATOM   220   N  N     . PRO   A  1  44   ? -43.114 51.111  103.245 1.00 24.80 ? 42   PRO   A N     1 
ATOM   221   C  CA    . PRO   A  1  44   ? -42.133 50.027  103.348 1.00 25.80 ? 42   PRO   A CA    1 
ATOM   222   C  C     . PRO   A  1  44   ? -42.465 48.891  102.392 1.00 22.62 ? 42   PRO   A C     1 
ATOM   223   O  O     . PRO   A  1  44   ? -43.625 48.543  102.176 1.00 24.69 ? 42   PRO   A O     1 
ATOM   224   C  CB    . PRO   A  1  44   ? -42.258 49.583  104.810 1.00 25.74 ? 42   PRO   A CB    1 
ATOM   225   C  CG    . PRO   A  1  44   ? -42.736 50.814  105.525 1.00 30.66 ? 42   PRO   A CG    1 
ATOM   226   C  CD    . PRO   A  1  44   ? -43.690 51.467  104.554 1.00 28.11 ? 42   PRO   A CD    1 
ATOM   227   N  N     . GLU   A  1  45   ? -41.413 48.345  101.778 1.00 23.09 ? 43   GLU   A N     1 
ATOM   228   C  CA    . GLU   A  1  45   ? -41.592 47.303  100.779 1.00 25.47 ? 43   GLU   A CA    1 
ATOM   229   C  C     . GLU   A  1  45   ? -42.309 46.075  101.338 1.00 25.61 ? 43   GLU   A C     1 
ATOM   230   O  O     . GLU   A  1  45   ? -43.105 45.443  100.634 1.00 26.43 ? 43   GLU   A O     1 
ATOM   231   C  CB    . GLU   A  1  45   ? -40.224 46.959  100.190 1.00 27.73 ? 43   GLU   A CB    1 
ATOM   232   C  CG    . GLU   A  1  45   ? -40.253 46.792  98.706  1.00 30.24 ? 43   GLU   A CG    1 
ATOM   233   C  CD    . GLU   A  1  45   ? -38.888 46.818  98.054  1.00 23.88 ? 43   GLU   A CD    1 
ATOM   234   O  OE1   . GLU   A  1  45   ? -37.944 47.449  98.588  1.00 23.07 ? 43   GLU   A OE1   1 
ATOM   235   O  OE2   . GLU   A  1  45   ? -38.780 46.181  96.994  1.00 22.42 ? 43   GLU   A OE2   1 
ATOM   236   N  N     . THR   A  1  46   ? -42.051 45.715  102.601 1.00 26.37 ? 44   THR   A N     1 
ATOM   237   C  CA    . THR   A  1  46   ? -42.756 44.581  103.195 1.00 30.24 ? 44   THR   A CA    1 
ATOM   238   C  C     . THR   A  1  46   ? -44.259 44.809  103.301 1.00 30.60 ? 44   THR   A C     1 
ATOM   239   O  O     . THR   A  1  46   ? -45.022 43.836  103.337 1.00 31.70 ? 44   THR   A O     1 
ATOM   240   C  CB    . THR   A  1  46   ? -42.187 44.264  104.578 1.00 28.41 ? 44   THR   A CB    1 
ATOM   241   O  OG1   . THR   A  1  46   ? -42.193 45.453  105.378 1.00 33.01 ? 44   THR   A OG1   1 
ATOM   242   C  CG2   . THR   A  1  46   ? -40.753 43.747  104.466 1.00 27.34 ? 44   THR   A CG2   1 
ATOM   243   N  N     . GLU   A  1  47   ? -44.701 46.064  103.351 1.00 25.49 ? 45   GLU   A N     1 
ATOM   244   C  CA    . GLU   A  1  47   ? -46.127 46.354  103.388 1.00 28.17 ? 45   GLU   A CA    1 
ATOM   245   C  C     . GLU   A  1  47   ? -46.747 46.340  101.995 1.00 27.77 ? 45   GLU   A C     1 
ATOM   246   O  O     . GLU   A  1  47   ? -47.930 46.014  101.844 1.00 27.60 ? 45   GLU   A O     1 
ATOM   247   C  CB    . GLU   A  1  47   ? -46.354 47.700  104.075 1.00 30.47 ? 45   GLU   A CB    1 
ATOM   248   C  CG    . GLU   A  1  47   ? -45.766 47.761  105.481 1.00 41.53 ? 45   GLU   A CG    1 
ATOM   249   C  CD    . GLU   A  1  47   ? -46.071 49.062  106.192 1.00 42.56 ? 45   GLU   A CD    1 
ATOM   250   O  OE1   . GLU   A  1  47   ? -47.002 49.772  105.755 1.00 47.38 ? 45   GLU   A OE1   1 
ATOM   251   O  OE2   . GLU   A  1  47   ? -45.378 49.374  107.186 1.00 51.46 ? 45   GLU   A OE2   1 
ATOM   252   N  N     . CYS   A  1  48   ? -45.960 46.665  100.968 1.00 24.09 ? 46   CYS   A N     1 
ATOM   253   C  CA    . CYS   A  1  48   ? -46.502 46.751  99.616  1.00 24.98 ? 46   CYS   A CA    1 
ATOM   254   C  C     . CYS   A  1  48   ? -46.787 45.376  99.031  1.00 19.80 ? 46   CYS   A C     1 
ATOM   255   O  O     . CYS   A  1  48   ? -47.763 45.197  98.295  1.00 23.92 ? 46   CYS   A O     1 
ATOM   256   C  CB    . CYS   A  1  48   ? -45.506 47.471  98.711  1.00 24.05 ? 46   CYS   A CB    1 
ATOM   257   S  SG    . CYS   A  1  48   ? -45.261 49.204  99.104  1.00 24.69 ? 46   CYS   A SG    1 
ATOM   258   N  N     . LEU   A  1  49   ? -45.913 44.406  99.291  1.00 24.50 ? 47   LEU   A N     1 
ATOM   259   C  CA    . LEU   A  1  49   ? -45.966 43.176  98.508  1.00 25.05 ? 47   LEU   A CA    1 
ATOM   260   C  C     . LEU   A  1  49   ? -47.155 42.246  98.766  1.00 22.29 ? 47   LEU   A C     1 
ATOM   261   O  O     . LEU   A  1  49   ? -47.691 41.681  97.804  1.00 25.65 ? 47   LEU   A O     1 
ATOM   262   C  CB    . LEU   A  1  49   ? -44.639 42.417  98.582  1.00 26.07 ? 47   LEU   A CB    1 
ATOM   263   C  CG    . LEU   A  1  49   ? -43.685 42.680  97.412  1.00 25.65 ? 47   LEU   A CG    1 
ATOM   264   C  CD1   . LEU   A  1  49   ? -44.314 42.244  96.096  1.00 25.81 ? 47   LEU   A CD1   1 
ATOM   265   C  CD2   . LEU   A  1  49   ? -43.279 44.144  97.360  1.00 26.01 ? 47   LEU   A CD2   1 
ATOM   266   N  N     . PRO   A  1  50   ? -47.576 42.011  100.011 1.00 28.15 ? 48   PRO   A N     1 
ATOM   267   C  CA    . PRO   A  1  50   ? -48.638 41.011  100.255 1.00 27.07 ? 48   PRO   A CA    1 
ATOM   268   C  C     . PRO   A  1  50   ? -49.903 41.262  99.448  1.00 27.74 ? 48   PRO   A C     1 
ATOM   269   O  O     . PRO   A  1  50   ? -50.416 40.320  98.822  1.00 28.76 ? 48   PRO   A O     1 
ATOM   270   C  CB    . PRO   A  1  50   ? -48.879 41.106  101.771 1.00 27.94 ? 48   PRO   A CB    1 
ATOM   271   C  CG    . PRO   A  1  50   ? -47.553 41.479  102.309 1.00 28.75 ? 48   PRO   A CG    1 
ATOM   272   C  CD    . PRO   A  1  50   ? -46.950 42.439  101.274 1.00 25.58 ? 48   PRO   A CD    1 
ATOM   273   N  N     . PRO   A  1  51   ? -50.446 42.492  99.404  1.00 26.53 ? 49   PRO   A N     1 
ATOM   274   C  CA    . PRO   A  1  51   ? -51.639 42.687  98.562  1.00 29.58 ? 49   PRO   A CA    1 
ATOM   275   C  C     . PRO   A  1  51   ? -51.365 42.487  97.081  1.00 24.89 ? 49   PRO   A C     1 
ATOM   276   O  O     . PRO   A  1  51   ? -52.271 42.080  96.337  1.00 27.79 ? 49   PRO   A O     1 
ATOM   277   C  CB    . PRO   A  1  51   ? -52.102 44.112  98.900  1.00 27.93 ? 49   PRO   A CB    1 
ATOM   278   C  CG    . PRO   A  1  51   ? -50.914 44.786  99.435  1.00 31.80 ? 49   PRO   A CG    1 
ATOM   279   C  CD    . PRO   A  1  51   ? -50.101 43.729  100.133 1.00 28.96 ? 49   PRO   A CD    1 
ATOM   280   N  N     . LEU   A  1  52   ? -50.139 42.763  96.625  1.00 27.06 ? 50   LEU   A N     1 
ATOM   281   C  CA    . LEU   A  1  52   ? -49.813 42.531  95.221  1.00 26.67 ? 50   LEU   A CA    1 
ATOM   282   C  C     . LEU   A  1  52   ? -49.739 41.040  94.929  1.00 22.03 ? 50   LEU   A C     1 
ATOM   283   O  O     . LEU   A  1  52   ? -50.250 40.569  93.905  1.00 25.11 ? 50   LEU   A O     1 
ATOM   284   C  CB    . LEU   A  1  52   ? -48.498 43.231  94.871  1.00 25.09 ? 50   LEU   A CB    1 
ATOM   285   C  CG    . LEU   A  1  52   ? -48.460 44.758  95.009  1.00 25.89 ? 50   LEU   A CG    1 
ATOM   286   C  CD1   . LEU   A  1  52   ? -47.038 45.283  94.813  1.00 23.63 ? 50   LEU   A CD1   1 
ATOM   287   C  CD2   . LEU   A  1  52   ? -49.404 45.432  94.018  1.00 24.52 ? 50   LEU   A CD2   1 
ATOM   288   N  N     . VAL   A  1  53   ? -49.140 40.277  95.843  1.00 25.72 ? 51   VAL   A N     1 
ATOM   289   C  CA    . VAL   A  1  53   ? -49.120 38.823  95.709  1.00 28.10 ? 51   VAL   A CA    1 
ATOM   290   C  C     . VAL   A  1  53   ? -50.539 38.278  95.644  1.00 24.80 ? 51   VAL   A C     1 
ATOM   291   O  O     . VAL   A  1  53   ? -50.868 37.454  94.779  1.00 27.29 ? 51   VAL   A O     1 
ATOM   292   C  CB    . VAL   A  1  53   ? -48.322 38.190  96.860  1.00 24.62 ? 51   VAL   A CB    1 
ATOM   293   C  CG1   . VAL   A  1  53   ? -48.486 36.677  96.845  1.00 29.35 ? 51   VAL   A CG1   1 
ATOM   294   C  CG2   . VAL   A  1  53   ? -46.860 38.578  96.764  1.00 24.30 ? 51   VAL   A CG2   1 
ATOM   295   N  N     . GLU   A  1  54   ? -51.411 38.759  96.536  1.00 26.69 ? 52   GLU   A N     1 
ATOM   296   C  CA    . GLU   A  1  54   ? -52.802 38.315  96.527  1.00 29.82 ? 52   GLU   A CA    1 
ATOM   297   C  C     . GLU   A  1  54   ? -53.467 38.630  95.193  1.00 27.30 ? 52   GLU   A C     1 
ATOM   298   O  O     . GLU   A  1  54   ? -54.090 37.758  94.577  1.00 29.40 ? 52   GLU   A O     1 
ATOM   299   C  CB    . GLU   A  1  54   ? -53.567 38.946  97.693  1.00 32.75 ? 52   GLU   A CB    1 
ATOM   300   N  N     . ALA   A  1  55   ? -53.292 39.864  94.695  1.00 26.16 ? 53   ALA   A N     1 
ATOM   301   C  CA    . ALA   A  1  55   ? -53.992 40.265  93.478  1.00 28.17 ? 53   ALA   A CA    1 
ATOM   302   C  C     . ALA   A  1  55   ? -53.443 39.553  92.249  1.00 23.61 ? 53   ALA   A C     1 
ATOM   303   O  O     . ALA   A  1  55   ? -54.162 39.372  91.259  1.00 26.84 ? 53   ALA   A O     1 
ATOM   304   C  CB    . ALA   A  1  55   ? -53.885 41.779  93.302  1.00 27.96 ? 53   ALA   A CB    1 
ATOM   305   N  N     . ALA   A  1  56   ? -52.180 39.145  92.291  1.00 23.75 ? 54   ALA   A N     1 
ATOM   306   C  CA    . ALA   A  1  56   ? -51.527 38.516  91.152  1.00 26.71 ? 54   ALA   A CA    1 
ATOM   307   C  C     . ALA   A  1  56   ? -51.664 36.998  91.146  1.00 30.88 ? 54   ALA   A C     1 
ATOM   308   O  O     . ALA   A  1  56   ? -51.213 36.354  90.193  1.00 26.95 ? 54   ALA   A O     1 
ATOM   309   C  CB    . ALA   A  1  56   ? -50.042 38.903  91.120  1.00 23.69 ? 54   ALA   A CB    1 
ATOM   310   N  N     . THR   A  1  57   ? -52.273 36.418  92.172  1.00 29.87 ? 55   THR   A N     1 
ATOM   311   C  CA    . THR   A  1  57   ? -52.386 34.969  92.258  1.00 29.94 ? 55   THR   A CA    1 
ATOM   312   C  C     . THR   A  1  57   ? -53.327 34.451  91.177  1.00 27.98 ? 55   THR   A C     1 
ATOM   313   O  O     . THR   A  1  57   ? -54.376 35.041  90.911  1.00 30.59 ? 55   THR   A O     1 
ATOM   314   C  CB    . THR   A  1  57   ? -52.912 34.595  93.642  1.00 31.38 ? 55   THR   A CB    1 
ATOM   315   O  OG1   . THR   A  1  57   ? -51.959 34.998  94.632  1.00 31.81 ? 55   THR   A OG1   1 
ATOM   316   C  CG2   . THR   A  1  57   ? -53.168 33.087  93.761  1.00 36.34 ? 55   THR   A CG2   1 
ATOM   317   N  N     . GLN   A  1  58   ? -52.938 33.349  90.538  1.00 28.79 ? 56   GLN   A N     1 
ATOM   318   C  CA    . GLN   A  1  58   ? -53.780 32.685  89.553  1.00 27.37 ? 56   GLN   A CA    1 
ATOM   319   C  C     . GLN   A  1  58   ? -53.820 31.194  89.862  1.00 27.28 ? 56   GLN   A C     1 
ATOM   320   O  O     . GLN   A  1  58   ? -53.004 30.676  90.624  1.00 31.26 ? 56   GLN   A O     1 
ATOM   321   C  CB    . GLN   A  1  58   ? -53.286 32.933  88.122  1.00 29.45 ? 56   GLN   A CB    1 
ATOM   322   C  CG    . GLN   A  1  58   ? -53.197 34.404  87.755  1.00 27.85 ? 56   GLN   A CG    1 
ATOM   323   C  CD    . GLN   A  1  58   ? -53.012 34.620  86.276  1.00 25.60 ? 56   GLN   A CD    1 
ATOM   324   O  OE1   . GLN   A  1  58   ? -53.970 34.559  85.510  1.00 28.74 ? 56   GLN   A OE1   1 
ATOM   325   N  NE2   . GLN   A  1  58   ? -51.773 34.870  85.858  1.00 28.14 ? 56   GLN   A NE2   1 
ATOM   326   N  N     . SER   A  1  59   ? -54.780 30.507  89.252  1.00 29.30 ? 57   SER   A N     1 
ATOM   327   C  CA    . SER   A  1  59   ? -54.956 29.086  89.502  1.00 28.89 ? 57   SER   A CA    1 
ATOM   328   C  C     . SER   A  1  59   ? -53.730 28.303  89.044  1.00 33.63 ? 57   SER   A C     1 
ATOM   329   O  O     . SER   A  1  59   ? -52.964 28.739  88.178  1.00 29.56 ? 57   SER   A O     1 
ATOM   330   C  CB    . SER   A  1  59   ? -56.159 28.571  88.729  1.00 31.95 ? 57   SER   A CB    1 
ATOM   331   O  OG    . SER   A  1  59   ? -55.888 28.572  87.340  1.00 32.39 ? 57   SER   A OG    1 
ATOM   332   N  N     . LYS   A  1  60   ? -53.562 27.114  89.630  1.00 33.17 ? 58   LYS   A N     1 
ATOM   333   C  CA    . LYS   A  1  60   ? -52.474 26.236  89.215  1.00 32.57 ? 58   LYS   A CA    1 
ATOM   334   C  C     . LYS   A  1  60   ? -52.553 25.928  87.724  1.00 33.64 ? 58   LYS   A C     1 
ATOM   335   O  O     . LYS   A  1  60   ? -51.526 25.903  87.036  1.00 35.62 ? 58   LYS   A O     1 
ATOM   336   C  CB    . LYS   A  1  60   ? -52.490 24.947  90.044  1.00 34.02 ? 58   LYS   A CB    1 
ATOM   337   C  CG    . LYS   A  1  60   ? -51.348 23.982  89.731  1.00 35.10 ? 58   LYS   A CG    1 
ATOM   338   C  CD    . LYS   A  1  60   ? -49.994 24.631  89.960  1.00 40.78 ? 58   LYS   A CD    1 
ATOM   339   C  CE    . LYS   A  1  60   ? -48.884 23.597  90.129  1.00 44.32 ? 58   LYS   A CE    1 
ATOM   340   N  NZ    . LYS   A  1  60   ? -48.628 22.827  88.882  1.00 45.30 ? 58   LYS   A NZ    1 
ATOM   341   N  N     . GLU   A  1  61   ? -53.764 25.705  87.204  1.00 33.74 ? 59   GLU   A N     1 
ATOM   342   C  CA    . GLU   A  1  61   ? -53.917 25.414  85.780  1.00 33.99 ? 59   GLU   A CA    1 
ATOM   343   C  C     . GLU   A  1  61   ? -53.443 26.582  84.925  1.00 32.71 ? 59   GLU   A C     1 
ATOM   344   O  O     . GLU   A  1  61   ? -52.790 26.381  83.894  1.00 36.17 ? 59   GLU   A O     1 
ATOM   345   C  CB    . GLU   A  1  61   ? -55.371 25.071  85.459  1.00 36.60 ? 59   GLU   A CB    1 
ATOM   346   N  N     . ILE   A  1  62   ? -53.767 27.811  85.333  1.00 32.56 ? 60   ILE   A N     1 
ATOM   347   C  CA    . ILE   A  1  62   ? -53.312 28.981  84.589  1.00 30.07 ? 60   ILE   A CA    1 
ATOM   348   C  C     . ILE   A  1  62   ? -51.801 29.126  84.672  1.00 32.22 ? 60   ILE   A C     1 
ATOM   349   O  O     . ILE   A  1  62   ? -51.139 29.406  83.666  1.00 30.08 ? 60   ILE   A O     1 
ATOM   350   C  CB    . ILE   A  1  62   ? -54.039 30.248  85.069  1.00 30.66 ? 60   ILE   A CB    1 
ATOM   351   C  CG1   . ILE   A  1  62   ? -55.453 30.272  84.508  1.00 33.86 ? 60   ILE   A CG1   1 
ATOM   352   C  CG2   . ILE   A  1  62   ? -53.275 31.502  84.657  1.00 30.68 ? 60   ILE   A CG2   1 
ATOM   353   C  CD1   . ILE   A  1  62   ? -56.204 31.470  84.912  1.00 37.56 ? 60   ILE   A CD1   1 
ATOM   354   N  N     . ARG   A  1  63   ? -51.234 28.954  85.868  1.00 28.93 ? 61   ARG   A N     1 
ATOM   355   C  CA    . ARG   A  1  63   ? -49.789 29.088  86.028  1.00 31.34 ? 61   ARG   A CA    1 
ATOM   356   C  C     . ARG   A  1  63   ? -49.040 28.069  85.180  1.00 31.89 ? 61   ARG   A C     1 
ATOM   357   O  O     . ARG   A  1  63   ? -47.998 28.385  84.591  1.00 31.52 ? 61   ARG   A O     1 
ATOM   358   C  CB    . ARG   A  1  63   ? -49.410 28.985  87.506  1.00 32.63 ? 61   ARG   A CB    1 
ATOM   359   C  CG    . ARG   A  1  63   ? -49.879 30.192  88.295  1.00 39.14 ? 61   ARG   A CG    1 
ATOM   360   C  CD    . ARG   A  1  63   ? -49.407 30.185  89.733  1.00 43.70 ? 61   ARG   A CD    1 
ATOM   361   N  NE    . ARG   A  1  63   ? -50.134 29.224  90.546  1.00 43.37 ? 61   ARG   A NE    1 
ATOM   362   C  CZ    . ARG   A  1  63   ? -49.625 28.079  90.972  1.00 45.80 ? 61   ARG   A CZ    1 
ATOM   363   N  NH1   . ARG   A  1  63   ? -48.385 27.727  90.680  1.00 45.03 ? 61   ARG   A NH1   1 
ATOM   364   N  NH2   . ARG   A  1  63   ? -50.375 27.273  91.715  1.00 44.61 ? 61   ARG   A NH2   1 
ATOM   365   N  N     . ASP   A  1  64   ? -49.561 26.844  85.092  1.00 35.75 ? 62   ASP   A N     1 
ATOM   366   C  CA    . ASP   A  1  64   ? -48.942 25.849  84.228  1.00 33.18 ? 62   ASP   A CA    1 
ATOM   367   C  C     . ASP   A  1  64   ? -49.089 26.225  82.758  1.00 33.27 ? 62   ASP   A C     1 
ATOM   368   O  O     . ASP   A  1  64   ? -48.151 26.057  81.972  1.00 32.72 ? 62   ASP   A O     1 
ATOM   369   C  CB    . ASP   A  1  64   ? -49.546 24.470  84.507  1.00 34.26 ? 62   ASP   A CB    1 
ATOM   370   C  CG    . ASP   A  1  64   ? -49.160 23.928  85.880  1.00 35.02 ? 62   ASP   A CG    1 
ATOM   371   O  OD1   . ASP   A  1  64   ? -48.308 24.539  86.559  1.00 37.25 ? 62   ASP   A OD1   1 
ATOM   372   O  OD2   . ASP   A  1  64   ? -49.714 22.878  86.282  1.00 44.86 ? 62   ASP   A OD2   1 
ATOM   373   N  N     . ALA   A  1  65   ? -50.261 26.727  82.364  1.00 29.32 ? 63   ALA   A N     1 
ATOM   374   C  CA    . ALA   A  1  65   ? -50.444 27.153  80.981  1.00 29.62 ? 63   ALA   A CA    1 
ATOM   375   C  C     . ALA   A  1  65   ? -49.576 28.361  80.664  1.00 33.66 ? 63   ALA   A C     1 
ATOM   376   O  O     . ALA   A  1  65   ? -49.023 28.464  79.562  1.00 31.10 ? 63   ALA   A O     1 
ATOM   377   C  CB    . ALA   A  1  65   ? -51.917 27.465  80.711  1.00 32.31 ? 63   ALA   A CB    1 
ATOM   378   N  N     . ALA   A  1  66   ? -49.444 29.280  81.622  1.00 29.98 ? 64   ALA   A N     1 
ATOM   379   C  CA    . ALA   A  1  66   ? -48.590 30.443  81.421  1.00 30.09 ? 64   ALA   A CA    1 
ATOM   380   C  C     . ALA   A  1  66   ? -47.135 30.028  81.258  1.00 30.78 ? 64   ALA   A C     1 
ATOM   381   O  O     . ALA   A  1  66   ? -46.434 30.537  80.374  1.00 28.28 ? 64   ALA   A O     1 
ATOM   382   C  CB    . ALA   A  1  66   ? -48.740 31.410  82.596  1.00 30.67 ? 64   ALA   A CB    1 
ATOM   383   N  N     . ALA   A  1  67   ? -46.669 29.096  82.094  1.00 27.93 ? 65   ALA   A N     1 
ATOM   384   C  CA    . ALA   A  1  67   ? -45.292 28.629  81.989  1.00 30.87 ? 65   ALA   A CA    1 
ATOM   385   C  C     . ALA   A  1  67   ? -45.046 27.951  80.648  1.00 30.45 ? 65   ALA   A C     1 
ATOM   386   O  O     . ALA   A  1  67   ? -43.983 28.127  80.039  1.00 31.89 ? 65   ALA   A O     1 
ATOM   387   C  CB    . ALA   A  1  67   ? -44.978 27.671  83.138  1.00 31.37 ? 65   ALA   A CB    1 
ATOM   388   N  N     . SER   A  1  68   ? -46.024 27.187  80.164  1.00 30.63 ? 66   SER   A N     1 
ATOM   389   C  CA    . SER   A  1  68   ? -45.878 26.541  78.865  1.00 33.08 ? 66   SER   A CA    1 
ATOM   390   C  C     . SER   A  1  68   ? -45.831 27.573  77.747  1.00 34.13 ? 66   SER   A C     1 
ATOM   391   O  O     . SER   A  1  68   ? -44.994 27.487  76.841  1.00 32.36 ? 66   SER   A O     1 
ATOM   392   C  CB    . SER   A  1  68   ? -47.020 25.544  78.651  1.00 36.78 ? 66   SER   A CB    1 
ATOM   393   O  OG    . SER   A  1  68   ? -47.013 25.032  77.332  1.00 42.50 ? 66   SER   A OG    1 
ATOM   394   N  N     . THR   A  1  69   ? -46.722 28.566  77.796  1.00 31.66 ? 67   THR   A N     1 
ATOM   395   C  CA    . THR   A  1  69   ? -46.690 29.620  76.793  1.00 27.63 ? 67   THR   A CA    1 
ATOM   396   C  C     . THR   A  1  69   ? -45.380 30.391  76.850  1.00 27.73 ? 67   THR   A C     1 
ATOM   397   O  O     . THR   A  1  69   ? -44.780 30.681  75.809  1.00 27.56 ? 67   THR   A O     1 
ATOM   398   C  CB    . THR   A  1  69   ? -47.869 30.566  76.996  1.00 27.57 ? 67   THR   A CB    1 
ATOM   399   O  OG1   . THR   A  1  69   ? -49.084 29.863  76.726  1.00 29.02 ? 67   THR   A OG1   1 
ATOM   400   C  CG2   . THR   A  1  69   ? -47.759 31.759  76.062  1.00 28.79 ? 67   THR   A CG2   1 
ATOM   401   N  N     . ALA   A  1  70   ? -44.922 30.727  78.057  1.00 27.83 ? 68   ALA   A N     1 
ATOM   402   C  CA    . ALA   A  1  70   ? -43.667 31.456  78.192  1.00 28.18 ? 68   ALA   A CA    1 
ATOM   403   C  C     . ALA   A  1  70   ? -42.505 30.644  77.641  1.00 30.24 ? 68   ALA   A C     1 
ATOM   404   O  O     . ALA   A  1  70   ? -41.650 31.182  76.928  1.00 28.88 ? 68   ALA   A O     1 
ATOM   405   C  CB    . ALA   A  1  70   ? -43.421 31.843  79.651  1.00 28.10 ? 68   ALA   A CB    1 
ATOM   406   N  N     . ARG   A  1  71   ? -42.464 29.345  77.955  1.00 29.19 ? 69   ARG   A N     1 
ATOM   407   C  CA    . ARG   A  1  71   ? -41.404 28.494  77.422  1.00 30.26 ? 69   ARG   A CA    1 
ATOM   408   C  C     . ARG   A  1  71   ? -41.443 28.472  75.901  1.00 31.74 ? 69   ARG   A C     1 
ATOM   409   O  O     . ARG   A  1  71   ? -40.406 28.630  75.245  1.00 30.42 ? 69   ARG   A O     1 
ATOM   410   C  CB    . ARG   A  1  71   ? -41.529 27.081  77.992  1.00 33.45 ? 69   ARG   A CB    1 
ATOM   411   C  CG    . ARG   A  1  71   ? -40.692 26.054  77.257  1.00 35.63 ? 69   ARG   A CG    1 
ATOM   412   C  CD    . ARG   A  1  71   ? -40.695 24.708  77.964  1.00 35.78 ? 69   ARG   A CD    1 
ATOM   413   N  NE    . ARG   A  1  71   ? -39.934 24.758  79.205  1.00 37.84 ? 69   ARG   A NE    1 
ATOM   414   C  CZ    . ARG   A  1  71   ? -38.610 24.714  79.268  1.00 37.44 ? 69   ARG   A CZ    1 
ATOM   415   N  NH1   . ARG   A  1  71   ? -37.868 24.634  78.173  1.00 38.00 ? 69   ARG   A NH1   1 
ATOM   416   N  NH2   . ARG   A  1  71   ? -38.015 24.765  80.456  1.00 36.42 ? 69   ARG   A NH2   1 
ATOM   417   N  N     . LYS   A  1  72   ? -42.638 28.314  75.325  1.00 30.22 ? 70   LYS   A N     1 
ATOM   418   C  CA    . LYS   A  1  72   ? -42.788 28.325  73.872  1.00 31.68 ? 70   LYS   A CA    1 
ATOM   419   C  C     . LYS   A  1  72   ? -42.262 29.628  73.274  1.00 34.71 ? 70   LYS   A C     1 
ATOM   420   O  O     . LYS   A  1  72   ? -41.514 29.615  72.289  1.00 31.40 ? 70   LYS   A O     1 
ATOM   421   C  CB    . LYS   A  1  72   ? -44.252 28.106  73.499  1.00 30.71 ? 70   LYS   A CB    1 
ATOM   422   C  CG    . LYS   A  1  72   ? -44.525 28.042  72.009  1.00 36.57 ? 70   LYS   A CG    1 
ATOM   423   C  CD    . LYS   A  1  72   ? -45.978 27.667  71.767  1.00 40.38 ? 70   LYS   A CD    1 
ATOM   424   C  CE    . LYS   A  1  72   ? -46.204 27.100  70.377  1.00 49.22 ? 70   LYS   A CE    1 
ATOM   425   N  NZ    . LYS   A  1  72   ? -46.229 28.160  69.339  1.00 54.17 ? 70   LYS   A NZ    1 
ATOM   426   N  N     . LEU   A  1  73   ? -42.637 30.767  73.866  1.00 30.91 ? 71   LEU   A N     1 
ATOM   427   C  CA    . LEU   A  1  73   ? -42.134 32.055  73.394  1.00 30.60 ? 71   LEU   A CA    1 
ATOM   428   C  C     . LEU   A  1  73   ? -40.618 32.140  73.513  1.00 29.62 ? 71   LEU   A C     1 
ATOM   429   O  O     . LEU   A  1  73   ? -39.941 32.626  72.600  1.00 30.14 ? 71   LEU   A O     1 
ATOM   430   C  CB    . LEU   A  1  73   ? -42.767 33.186  74.201  1.00 29.03 ? 71   LEU   A CB    1 
ATOM   431   C  CG    . LEU   A  1  73   ? -44.274 33.351  74.053  1.00 29.12 ? 71   LEU   A CG    1 
ATOM   432   C  CD1   . LEU   A  1  73   ? -44.767 34.400  75.024  1.00 25.38 ? 71   LEU   A CD1   1 
ATOM   433   C  CD2   . LEU   A  1  73   ? -44.632 33.728  72.628  1.00 32.14 ? 71   LEU   A CD2   1 
ATOM   434   N  N     . ILE   A  1  74   ? -40.071 31.692  74.642  1.00 28.25 ? 72   ILE   A N     1 
ATOM   435   C  CA    . ILE   A  1  74   ? -38.632 31.782  74.859  1.00 29.21 ? 72   ILE   A CA    1 
ATOM   436   C  C     . ILE   A  1  74   ? -37.883 30.842  73.924  1.00 32.99 ? 72   ILE   A C     1 
ATOM   437   O  O     . ILE   A  1  74   ? -36.808 31.181  73.411  1.00 32.52 ? 72   ILE   A O     1 
ATOM   438   C  CB    . ILE   A  1  74   ? -38.314 31.530  76.342  1.00 27.85 ? 72   ILE   A CB    1 
ATOM   439   C  CG1   . ILE   A  1  74   ? -38.819 32.713  77.175  1.00 30.29 ? 72   ILE   A CG1   1 
ATOM   440   C  CG2   . ILE   A  1  74   ? -36.818 31.312  76.555  1.00 29.08 ? 72   ILE   A CG2   1 
ATOM   441   C  CD1   . ILE   A  1  74   ? -38.948 32.429  78.644  1.00 28.67 ? 72   ILE   A CD1   1 
ATOM   442   N  N     . GLU   A  1  75   ? -38.437 29.653  73.679  1.00 32.10 ? 73   GLU   A N     1 
ATOM   443   C  CA    . GLU   A  1  75   ? -37.808 28.735  72.736  1.00 32.10 ? 73   GLU   A CA    1 
ATOM   444   C  C     . GLU   A  1  75   ? -37.786 29.323  71.331  1.00 36.68 ? 73   GLU   A C     1 
ATOM   445   O  O     . GLU   A  1  75   ? -36.770 29.239  70.631  1.00 34.22 ? 73   GLU   A O     1 
ATOM   446   C  CB    . GLU   A  1  75   ? -38.500 27.371  72.784  1.00 34.87 ? 73   GLU   A CB    1 
ATOM   447   C  CG    . GLU   A  1  75   ? -38.052 26.556  73.979  1.00 37.39 ? 73   GLU   A CG    1 
ATOM   448   C  CD    . GLU   A  1  75   ? -38.942 25.373  74.302  1.00 43.50 ? 73   GLU   A CD    1 
ATOM   449   O  OE1   . GLU   A  1  75   ? -40.021 25.228  73.685  1.00 44.42 ? 73   GLU   A OE1   1 
ATOM   450   O  OE2   . GLU   A  1  75   ? -38.553 24.588  75.195  1.00 45.68 ? 73   GLU   A OE2   1 
ATOM   451   N  N     . ALA   A  1  76   ? -38.884 29.955  70.914  1.00 35.25 ? 74   ALA   A N     1 
ATOM   452   C  CA    . ALA   A  1  76   ? -38.898 30.639  69.626  1.00 34.30 ? 74   ALA   A CA    1 
ATOM   453   C  C     . ALA   A  1  76   ? -37.884 31.777  69.590  1.00 35.81 ? 74   ALA   A C     1 
ATOM   454   O  O     . ALA   A  1  76   ? -37.202 31.972  68.578  1.00 36.66 ? 74   ALA   A O     1 
ATOM   455   C  CB    . ALA   A  1  76   ? -40.308 31.148  69.321  1.00 36.08 ? 74   ALA   A CB    1 
ATOM   456   N  N     . LEU   A  1  77   ? -37.767 32.538  70.683  1.00 34.04 ? 75   LEU   A N     1 
ATOM   457   C  CA    . LEU   A  1  77   ? -36.806 33.638  70.730  1.00 31.85 ? 75   LEU   A CA    1 
ATOM   458   C  C     . LEU   A  1  77   ? -35.380 33.129  70.581  1.00 39.32 ? 75   LEU   A C     1 
ATOM   459   O  O     . LEU   A  1  77   ? -34.624 33.597  69.721  1.00 41.13 ? 75   LEU   A O     1 
ATOM   460   C  CB    . LEU   A  1  77   ? -36.939 34.403  72.045  1.00 32.66 ? 75   LEU   A CB    1 
ATOM   461   C  CG    . LEU   A  1  77   ? -37.993 35.499  72.107  1.00 33.03 ? 75   LEU   A CG    1 
ATOM   462   C  CD1   . LEU   A  1  77   ? -37.977 36.136  73.482  1.00 31.52 ? 75   LEU   A CD1   1 
ATOM   463   C  CD2   . LEU   A  1  77   ? -37.726 36.530  71.026  1.00 33.39 ? 75   LEU   A CD2   1 
ATOM   464   N  N     . ARG   A  1  78   ? -34.990 32.176  71.429  1.00 32.78 ? 76   ARG   A N     1 
ATOM   465   C  CA    . ARG   A  1  78   ? -33.634 31.648  71.384  1.00 34.23 ? 76   ARG   A CA    1 
ATOM   466   C  C     . ARG   A  1  78   ? -33.355 30.869  70.109  1.00 37.22 ? 76   ARG   A C     1 
ATOM   467   O  O     . ARG   A  1  78   ? -32.189 30.740  69.721  1.00 41.63 ? 76   ARG   A O     1 
ATOM   468   C  CB    . ARG   A  1  78   ? -33.378 30.786  72.616  1.00 33.99 ? 76   ARG   A CB    1 
ATOM   469   C  CG    . ARG   A  1  78   ? -33.281 31.609  73.877  1.00 34.06 ? 76   ARG   A CG    1 
ATOM   470   C  CD    . ARG   A  1  78   ? -32.877 30.778  75.067  1.00 32.55 ? 76   ARG   A CD    1 
ATOM   471   N  NE    . ARG   A  1  78   ? -32.298 31.629  76.095  1.00 31.90 ? 76   ARG   A NE    1 
ATOM   472   C  CZ    . ARG   A  1  78   ? -31.863 31.199  77.268  1.00 32.16 ? 76   ARG   A CZ    1 
ATOM   473   N  NH1   . ARG   A  1  78   ? -31.984 29.931  77.627  1.00 33.94 ? 76   ARG   A NH1   1 
ATOM   474   N  NH2   . ARG   A  1  78   ? -31.283 32.060  78.100  1.00 33.73 ? 76   ARG   A NH2   1 
ATOM   475   N  N     . GLY   A  1  79   ? -34.394 30.361  69.444  1.00 36.89 ? 77   GLY   A N     1 
ATOM   476   C  CA    . GLY   A  1  79   ? -34.200 29.586  68.233  1.00 44.33 ? 77   GLY   A CA    1 
ATOM   477   C  C     . GLY   A  1  79   ? -33.923 30.406  66.993  1.00 46.38 ? 77   GLY   A C     1 
ATOM   478   O  O     . GLY   A  1  79   ? -33.381 29.873  66.021  1.00 50.11 ? 77   GLY   A O     1 
ATOM   479   N  N     . LYS   A  1  80   ? -34.279 31.688  66.998  1.00 43.77 ? 78   LYS   A N     1 
ATOM   480   C  CA    . LYS   A  1  80   ? -34.058 32.547  65.844  1.00 47.83 ? 78   LYS   A CA    1 
ATOM   481   C  C     . LYS   A  1  80   ? -33.010 33.623  66.089  1.00 46.89 ? 78   LYS   A C     1 
ATOM   482   O  O     . LYS   A  1  80   ? -32.731 34.411  65.179  1.00 51.41 ? 78   LYS   A O     1 
ATOM   483   C  CB    . LYS   A  1  80   ? -35.376 33.178  65.383  1.00 46.11 ? 78   LYS   A CB    1 
ATOM   484   C  CG    . LYS   A  1  80   ? -36.072 34.019  66.443  1.00 47.04 ? 78   LYS   A CG    1 
ATOM   485   C  CD    . LYS   A  1  80   ? -37.455 34.434  65.973  1.00 42.08 ? 78   LYS   A CD    1 
ATOM   486   C  CE    . LYS   A  1  80   ? -38.211 35.195  67.047  1.00 41.43 ? 78   LYS   A CE    1 
ATOM   487   N  NZ    . LYS   A  1  80   ? -39.581 35.566  66.588  1.00 31.71 ? 78   LYS   A NZ    1 
ATOM   488   N  N     . HIS   A  1  81   ? -32.421 33.670  67.281  1.00 46.48 ? 79   HIS   A N     1 
ATOM   489   C  CA    . HIS   A  1  81   ? -31.453 34.701  67.640  1.00 50.66 ? 79   HIS   A CA    1 
ATOM   490   C  C     . HIS   A  1  81   ? -30.233 34.690  66.723  1.00 53.93 ? 79   HIS   A C     1 
ATOM   491   O  O     . HIS   A  1  81   ? -29.829 33.638  66.231  1.00 61.68 ? 79   HIS   A O     1 
ATOM   492   C  CB    . HIS   A  1  81   ? -31.011 34.526  69.095  1.00 51.04 ? 79   HIS   A CB    1 
ATOM   493   N  N     . SER   A  1  84   ? -26.128 41.096  67.096  1.00 52.62 ? 82   SER   A N     1 
ATOM   494   C  CA    . SER   A  1  84   ? -25.373 40.202  66.228  1.00 50.17 ? 82   SER   A CA    1 
ATOM   495   C  C     . SER   A  1  84   ? -24.674 40.980  65.116  1.00 46.81 ? 82   SER   A C     1 
ATOM   496   O  O     . SER   A  1  84   ? -23.663 40.530  64.583  1.00 43.32 ? 82   SER   A O     1 
ATOM   497   C  CB    . SER   A  1  84   ? -26.283 39.125  65.631  1.00 49.14 ? 82   SER   A CB    1 
ATOM   498   N  N     . GLY   A  1  85   ? -25.222 42.144  64.762  1.00 44.00 ? 83   GLY   A N     1 
ATOM   499   C  CA    . GLY   A  1  85   ? -24.576 42.973  63.756  1.00 37.35 ? 83   GLY   A CA    1 
ATOM   500   C  C     . GLY   A  1  85   ? -23.225 43.486  64.220  1.00 29.40 ? 83   GLY   A C     1 
ATOM   501   O  O     . GLY   A  1  85   ? -22.205 43.296  63.547  1.00 32.57 ? 83   GLY   A O     1 
ATOM   502   N  N     . VAL   A  1  86   ? -23.201 44.148  65.379  1.00 32.41 ? 84   VAL   A N     1 
ATOM   503   C  CA    . VAL   A  1  86   ? -21.936 44.595  65.957  1.00 31.14 ? 84   VAL   A CA    1 
ATOM   504   C  C     . VAL   A  1  86   ? -21.059 43.399  66.296  1.00 34.01 ? 84   VAL   A C     1 
ATOM   505   O  O     . VAL   A  1  86   ? -19.846 43.404  66.043  1.00 26.31 ? 84   VAL   A O     1 
ATOM   506   C  CB    . VAL   A  1  86   ? -22.196 45.499  67.178  1.00 33.74 ? 84   VAL   A CB    1 
ATOM   507   C  CG1   . VAL   A  1  86   ? -20.936 45.629  68.030  1.00 34.95 ? 84   VAL   A CG1   1 
ATOM   508   C  CG2   . VAL   A  1  86   ? -22.670 46.866  66.724  1.00 34.92 ? 84   VAL   A CG2   1 
ATOM   509   N  N     . GLU   A  1  87   ? -21.661 42.350  66.861  1.00 32.07 ? 85   GLU   A N     1 
ATOM   510   C  CA    . GLU   A  1  87   ? -20.912 41.136  67.168  1.00 33.75 ? 85   GLU   A CA    1 
ATOM   511   C  C     . GLU   A  1  87   ? -20.268 40.554  65.917  1.00 33.31 ? 85   GLU   A C     1 
ATOM   512   O  O     . GLU   A  1  87   ? -19.101 40.145  65.942  1.00 34.45 ? 85   GLU   A O     1 
ATOM   513   C  CB    . GLU   A  1  87   ? -21.833 40.109  67.827  1.00 41.24 ? 85   GLU   A CB    1 
ATOM   514   N  N     . GLY   A  1  88   ? -21.007 40.521  64.808  1.00 31.30 ? 86   GLY   A N     1 
ATOM   515   C  CA    . GLY   A  1  88   ? -20.443 39.992  63.579  1.00 31.45 ? 86   GLY   A CA    1 
ATOM   516   C  C     . GLY   A  1  88   ? -19.281 40.823  63.076  1.00 29.36 ? 86   GLY   A C     1 
ATOM   517   O  O     . GLY   A  1  88   ? -18.303 40.289  62.549  1.00 31.75 ? 86   GLY   A O     1 
ATOM   518   N  N     . LEU   A  1  89   ? -19.368 42.143  63.248  1.00 29.45 ? 87   LEU   A N     1 
ATOM   519   C  CA    . LEU   A  1  89   ? -18.286 43.026  62.835  1.00 29.10 ? 87   LEU   A CA    1 
ATOM   520   C  C     . LEU   A  1  89   ? -17.055 42.804  63.705  1.00 26.27 ? 87   LEU   A C     1 
ATOM   521   O  O     . LEU   A  1  89   ? -15.941 42.647  63.192  1.00 24.85 ? 87   LEU   A O     1 
ATOM   522   C  CB    . LEU   A  1  89   ? -18.771 44.476  62.912  1.00 31.70 ? 87   LEU   A CB    1 
ATOM   523   C  CG    . LEU   A  1  89   ? -18.136 45.543  62.017  1.00 34.89 ? 87   LEU   A CG    1 
ATOM   524   C  CD1   . LEU   A  1  89   ? -18.875 46.857  62.197  1.00 34.90 ? 87   LEU   A CD1   1 
ATOM   525   C  CD2   . LEU   A  1  89   ? -16.663 45.726  62.318  1.00 37.85 ? 87   LEU   A CD2   1 
ATOM   526   N  N     . VAL   A  1  90   ? -17.247 42.775  65.027  1.00 24.42 ? 88   VAL   A N     1 
ATOM   527   C  CA    . VAL   A  1  90   ? -16.152 42.494  65.952  1.00 25.44 ? 88   VAL   A CA    1 
ATOM   528   C  C     . VAL   A  1  90   ? -15.468 41.181  65.594  1.00 28.54 ? 88   VAL   A C     1 
ATOM   529   O  O     . VAL   A  1  90   ? -14.232 41.084  65.597  1.00 25.84 ? 88   VAL   A O     1 
ATOM   530   C  CB    . VAL   A  1  90   ? -16.685 42.496  67.396  1.00 23.77 ? 88   VAL   A CB    1 
ATOM   531   C  CG1   . VAL   A  1  90   ? -15.666 41.904  68.345  1.00 29.39 ? 88   VAL   A CG1   1 
ATOM   532   C  CG2   . VAL   A  1  90   ? -17.055 43.907  67.822  1.00 27.06 ? 88   VAL   A CG2   1 
ATOM   533   N  N     . GLN   A  1  91   ? -16.259 40.153  65.279  1.00 29.95 ? 89   GLN   A N     1 
ATOM   534   C  CA    . GLN   A  1  91   ? -15.700 38.851  64.925  1.00 28.74 ? 89   GLN   A CA    1 
ATOM   535   C  C     . GLN   A  1  91   ? -14.914 38.918  63.622  1.00 31.14 ? 89   GLN   A C     1 
ATOM   536   O  O     . GLN   A  1  91   ? -13.775 38.440  63.546  1.00 31.83 ? 89   GLN   A O     1 
ATOM   537   C  CB    . GLN   A  1  91   ? -16.826 37.814  64.823  1.00 31.85 ? 89   GLN   A CB    1 
ATOM   538   N  N     . GLU   A  1  92   ? -15.503 39.512  62.582  1.00 29.48 ? 90   GLU   A N     1 
ATOM   539   C  CA    . GLU   A  1  92   ? -14.880 39.489  61.261  1.00 28.63 ? 90   GLU   A CA    1 
ATOM   540   C  C     . GLU   A  1  92   ? -13.512 40.162  61.265  1.00 29.73 ? 90   GLU   A C     1 
ATOM   541   O  O     . GLU   A  1  92   ? -12.572 39.686  60.615  1.00 28.68 ? 90   GLU   A O     1 
ATOM   542   C  CB    . GLU   A  1  92   ? -15.807 40.148  60.238  1.00 29.15 ? 90   GLU   A CB    1 
ATOM   543   C  CG    . GLU   A  1  92   ? -15.176 40.346  58.872  1.00 31.16 ? 90   GLU   A CG    1 
ATOM   544   C  CD    . GLU   A  1  92   ? -16.149 40.920  57.862  1.00 38.99 ? 90   GLU   A CD    1 
ATOM   545   O  OE1   . GLU   A  1  92   ? -17.286 41.248  58.258  1.00 41.24 ? 90   GLU   A OE1   1 
ATOM   546   O  OE2   . GLU   A  1  92   ? -15.777 41.043  56.677  1.00 39.52 ? 90   GLU   A OE2   1 
ATOM   547   N  N     . TYR   A  1  93   ? -13.376 41.264  61.998  1.00 25.78 ? 91   TYR   A N     1 
ATOM   548   C  CA    . TYR   A  1  93   ? -12.136 42.024  62.024  1.00 27.32 ? 91   TYR   A CA    1 
ATOM   549   C  C     . TYR   A  1  93   ? -11.324 41.803  63.295  1.00 23.96 ? 91   TYR   A C     1 
ATOM   550   O  O     . TYR   A  1  93   ? -10.345 42.525  63.523  1.00 24.86 ? 91   TYR   A O     1 
ATOM   551   C  CB    . TYR   A  1  93   ? -12.424 43.507  61.795  1.00 25.54 ? 91   TYR   A CB    1 
ATOM   552   C  CG    . TYR   A  1  93   ? -12.929 43.756  60.400  1.00 25.31 ? 91   TYR   A CG    1 
ATOM   553   C  CD1   . TYR   A  1  93   ? -12.039 43.925  59.343  1.00 24.37 ? 91   TYR   A CD1   1 
ATOM   554   C  CD2   . TYR   A  1  93   ? -14.290 43.776  60.127  1.00 25.01 ? 91   TYR   A CD2   1 
ATOM   555   C  CE1   . TYR   A  1  93   ? -12.496 44.132  58.056  1.00 27.56 ? 91   TYR   A CE1   1 
ATOM   556   C  CE2   . TYR   A  1  93   ? -14.754 43.984  58.837  1.00 30.84 ? 91   TYR   A CE2   1 
ATOM   557   C  CZ    . TYR   A  1  93   ? -13.848 44.167  57.814  1.00 26.47 ? 91   TYR   A CZ    1 
ATOM   558   O  OH    . TYR   A  1  93   ? -14.295 44.367  56.528  1.00 33.91 ? 91   TYR   A OH    1 
ATOM   559   N  N     . SER   A  1  94   ? -11.687 40.803  64.099  1.00 24.92 ? 92   SER   A N     1 
ATOM   560   C  CA    . SER   A  1  94   ? -10.940 40.460  65.311  1.00 24.33 ? 92   SER   A CA    1 
ATOM   561   C  C     . SER   A  1  94   ? -10.724 41.688  66.186  1.00 23.10 ? 92   SER   A C     1 
ATOM   562   O  O     . SER   A  1  94   ? -9.621  41.949  66.671  1.00 25.20 ? 92   SER   A O     1 
ATOM   563   C  CB    . SER   A  1  94   ? -9.618  39.767  64.988  1.00 27.22 ? 92   SER   A CB    1 
ATOM   564   O  OG    . SER   A  1  94   ? -9.829  38.679  64.099  1.00 28.79 ? 92   SER   A OG    1 
ATOM   565   N  N     . LEU   A  1  95   ? -11.783 42.465  66.363  1.00 20.95 ? 93   LEU   A N     1 
ATOM   566   C  CA    . LEU   A  1  95   ? -11.692 43.692  67.129  1.00 22.84 ? 93   LEU   A CA    1 
ATOM   567   C  C     . LEU   A  1  95   ? -11.726 43.388  68.616  1.00 21.42 ? 93   LEU   A C     1 
ATOM   568   O  O     . LEU   A  1  95   ? -12.512 42.560  69.085  1.00 22.28 ? 93   LEU   A O     1 
ATOM   569   C  CB    . LEU   A  1  95   ? -12.871 44.601  66.794  1.00 19.43 ? 93   LEU   A CB    1 
ATOM   570   C  CG    . LEU   A  1  95   ? -13.014 45.036  65.334  1.00 19.65 ? 93   LEU   A CG    1 
ATOM   571   C  CD1   . LEU   A  1  95   ? -14.147 46.060  65.232  1.00 23.27 ? 93   LEU   A CD1   1 
ATOM   572   C  CD2   . LEU   A  1  95   ? -11.724 45.592  64.790  1.00 21.61 ? 93   LEU   A CD2   1 
ATOM   573   N  N     . SER   A  1  96   ? -10.881 44.080  69.363  1.00 19.54 ? 94   SER   A N     1 
ATOM   574   C  CA    . SER   A  1  96   ? -11.080 44.145  70.800  1.00 18.02 ? 94   SER   A CA    1 
ATOM   575   C  C     . SER   A  1  96   ? -12.318 44.989  71.100  1.00 18.34 ? 94   SER   A C     1 
ATOM   576   O  O     . SER   A  1  96   ? -12.871 45.664  70.225  1.00 18.85 ? 94   SER   A O     1 
ATOM   577   C  CB    . SER   A  1  96   ? -9.883  44.819  71.454  1.00 19.34 ? 94   SER   A CB    1 
ATOM   578   O  OG    . SER   A  1  96   ? -9.827  46.183  71.064  1.00 17.69 ? 94   SER   A OG    1 
ATOM   579   N  N     . SER   A  1  97   ? -12.747 44.972  72.361  1.00 19.06 ? 95   SER   A N     1 
ATOM   580   C  CA    . SER   A  1  97   ? -13.901 45.784  72.738  1.00 19.68 ? 95   SER   A CA    1 
ATOM   581   C  C     . SER   A  1  97   ? -13.626 47.263  72.512  1.00 16.92 ? 95   SER   A C     1 
ATOM   582   O  O     . SER   A  1  97   ? -14.470 47.987  71.973  1.00 17.22 ? 95   SER   A O     1 
ATOM   583   C  CB    . SER   A  1  97   ? -14.259 45.537  74.203  1.00 23.78 ? 95   SER   A CB    1 
ATOM   584   O  OG    . SER   A  1  97   ? -14.866 44.270  74.344  1.00 31.77 ? 95   SER   A OG    1 
ATOM   585   N  N     . GLN   A  1  98   ? -12.450 47.732  72.910  1.00 16.67 ? 96   GLN   A N     1 
ATOM   586   C  CA    . GLN   A  1  98   ? -12.139 49.136  72.704  1.00 17.13 ? 96   GLN   A CA    1 
ATOM   587   C  C     . GLN   A  1  98   ? -12.102 49.475  71.223  1.00 14.62 ? 96   GLN   A C     1 
ATOM   588   O  O     . GLN   A  1  98   ? -12.521 50.565  70.825  1.00 15.78 ? 96   GLN   A O     1 
ATOM   589   C  CB    . GLN   A  1  98   ? -10.828 49.495  73.397  1.00 15.63 ? 96   GLN   A CB    1 
ATOM   590   C  CG    . GLN   A  1  98   ? -10.999 49.581  74.917  1.00 17.51 ? 96   GLN   A CG    1 
ATOM   591   C  CD    . GLN   A  1  98   ? -11.930 50.695  75.349  1.00 17.24 ? 96   GLN   A CD    1 
ATOM   592   O  OE1   . GLN   A  1  98   ? -13.150 50.523  75.371  1.00 19.61 ? 96   GLN   A OE1   1 
ATOM   593   N  NE2   . GLN   A  1  98   ? -11.367 51.840  75.714  1.00 19.26 ? 96   GLN   A NE2   1 
ATOM   594   N  N     . GLU   A  1  99   ? -11.594 48.559  70.392  1.00 14.69 ? 97   GLU   A N     1 
ATOM   595   C  CA    . GLU   A  1  99   ? -11.607 48.798  68.953  1.00 15.13 ? 97   GLU   A CA    1 
ATOM   596   C  C     . GLU   A  1  99   ? -13.027 48.872  68.430  1.00 16.27 ? 97   GLU   A C     1 
ATOM   597   O  O     . GLU   A  1  99   ? -13.345 49.743  67.613  1.00 16.56 ? 97   GLU   A O     1 
ATOM   598   C  CB    . GLU   A  1  99   ? -10.820 47.709  68.244  1.00 15.68 ? 97   GLU   A CB    1 
ATOM   599   C  CG    . GLU   A  1  99   ? -9.326  47.894  68.449  1.00 16.09 ? 97   GLU   A CG    1 
ATOM   600   C  CD    . GLU   A  1  99   ? -8.519  46.713  67.980  1.00 16.55 ? 97   GLU   A CD    1 
ATOM   601   O  OE1   . GLU   A  1  99   ? -9.119  45.711  67.556  1.00 19.17 ? 97   GLU   A OE1   1 
ATOM   602   O  OE2   . GLU   A  1  99   ? -7.265  46.774  68.037  1.00 17.88 ? 97   GLU   A OE2   1 
ATOM   603   N  N     . GLY   A  1  100  ? -13.902 47.977  68.889  1.00 15.58 ? 98   GLY   A N     1 
ATOM   604   C  CA    . GLY   A  1  100  ? -15.295 48.058  68.478  1.00 16.44 ? 98   GLY   A CA    1 
ATOM   605   C  C     . GLY   A  1  100  ? -15.924 49.387  68.850  1.00 18.13 ? 98   GLY   A C     1 
ATOM   606   O  O     . GLY   A  1  100  ? -16.609 50.016  68.042  1.00 16.50 ? 98   GLY   A O     1 
ATOM   607   N  N     . VAL   A  1  101  ? -15.706 49.830  70.089  1.00 15.19 ? 99   VAL   A N     1 
ATOM   608   C  CA    . VAL   A  1  101  ? -16.264 51.101  70.523  1.00 15.77 ? 99   VAL   A CA    1 
ATOM   609   C  C     . VAL   A  1  101  ? -15.691 52.241  69.700  1.00 15.11 ? 99   VAL   A C     1 
ATOM   610   O  O     . VAL   A  1  101  ? -16.431 53.108  69.214  1.00 16.42 ? 99   VAL   A O     1 
ATOM   611   C  CB    . VAL   A  1  101  ? -16.018 51.314  72.022  1.00 15.61 ? 99   VAL   A CB    1 
ATOM   612   C  CG1   . VAL   A  1  101  ? -16.445 52.706  72.410  1.00 17.57 ? 99   VAL   A CG1   1 
ATOM   613   C  CG2   . VAL   A  1  101  ? -16.782 50.264  72.816  1.00 16.69 ? 99   VAL   A CG2   1 
ATOM   614   N  N     . ALA   A  1  102  ? -14.367 52.238  69.499  1.00 14.53 ? 100  ALA   A N     1 
ATOM   615   C  CA    . ALA   A  1  102  ? -13.739 53.337  68.776  1.00 14.94 ? 100  ALA   A CA    1 
ATOM   616   C  C     . ALA   A  1  102  ? -14.229 53.381  67.346  1.00 15.18 ? 100  ALA   A C     1 
ATOM   617   O  O     . ALA   A  1  102  ? -14.461 54.466  66.801  1.00 15.96 ? 100  ALA   A O     1 
ATOM   618   C  CB    . ALA   A  1  102  ? -12.217 53.192  68.808  1.00 16.02 ? 100  ALA   A CB    1 
ATOM   619   N  N     . LEU   A  1  103  ? -14.400 52.210  66.738  1.00 14.66 ? 101  LEU   A N     1 
ATOM   620   C  CA    . LEU   A  1  103  ? -14.904 52.138  65.373  1.00 15.12 ? 101  LEU   A CA    1 
ATOM   621   C  C     . LEU   A  1  103  ? -16.292 52.743  65.278  1.00 16.05 ? 101  LEU   A C     1 
ATOM   622   O  O     . LEU   A  1  103  ? -16.586 53.495  64.340  1.00 17.86 ? 101  LEU   A O     1 
ATOM   623   C  CB    . LEU   A  1  103  ? -14.924 50.686  64.902  1.00 15.80 ? 101  LEU   A CB    1 
ATOM   624   C  CG    . LEU   A  1  103  ? -15.554 50.481  63.525  1.00 16.93 ? 101  LEU   A CG    1 
ATOM   625   C  CD1   . LEU   A  1  103  ? -14.734 51.182  62.462  1.00 19.93 ? 101  LEU   A CD1   1 
ATOM   626   C  CD2   . LEU   A  1  103  ? -15.671 49.012  63.250  1.00 19.82 ? 101  LEU   A CD2   1 
ATOM   627   N  N     . MET   A  1  104  ? -17.172 52.415  66.224  1.00 16.32 ? 102  MET   A N     1 
ATOM   628   C  CA    . MET   A  1  104  ? -18.515 52.977  66.160  1.00 15.86 ? 102  MET   A CA    1 
ATOM   629   C  C     . MET   A  1  104  ? -18.498 54.478  66.403  1.00 16.81 ? 102  MET   A C     1 
ATOM   630   O  O     . MET   A  1  104  ? -19.299 55.205  65.802  1.00 17.90 ? 102  MET   A O     1 
ATOM   631   C  CB    . MET   A  1  104  ? -19.448 52.253  67.140  1.00 16.89 ? 102  MET   A CB    1 
ATOM   632   C  CG    . MET   A  1  104  ? -19.546 50.762  66.845  1.00 18.46 ? 102  MET   A CG    1 
ATOM   633   S  SD    . MET   A  1  104  ? -20.005 50.385  65.118  1.00 25.62 ? 102  MET   A SD    1 
ATOM   634   C  CE    . MET   A  1  104  ? -21.663 51.034  65.071  1.00 27.14 ? 102  MET   A CE    1 
ATOM   635   N  N     . CYS   A  1  105  ? -17.587 54.967  67.249  1.00 15.87 ? 103  CYS   A N     1 
ATOM   636   C  CA    . CYS   A  1  105  ? -17.463 56.408  67.419  1.00 16.33 ? 103  CYS   A CA    1 
ATOM   637   C  C     . CYS   A  1  105  ? -17.010 57.068  66.131  1.00 18.92 ? 103  CYS   A C     1 
ATOM   638   O  O     . CYS   A  1  105  ? -17.537 58.116  65.740  1.00 19.96 ? 103  CYS   A O     1 
ATOM   639   C  CB    . CYS   A  1  105  ? -16.464 56.715  68.527  1.00 17.36 ? 103  CYS   A CB    1 
ATOM   640   S  SG    . CYS   A  1  105  ? -17.051 56.258  70.144  1.00 18.44 ? 103  CYS   A SG    1 
ATOM   641   N  N     . LEU   A  1  106  ? -16.027 56.471  65.458  1.00 16.61 ? 104  LEU   A N     1 
ATOM   642   C  CA    . LEU   A  1  106  ? -15.612 56.975  64.160  1.00 18.36 ? 104  LEU   A CA    1 
ATOM   643   C  C     . LEU   A  1  106  ? -16.776 56.961  63.187  1.00 19.72 ? 104  LEU   A C     1 
ATOM   644   O  O     . LEU   A  1  106  ? -16.984 57.927  62.441  1.00 19.63 ? 104  LEU   A O     1 
ATOM   645   C  CB    . LEU   A  1  106  ? -14.468 56.121  63.609  1.00 18.70 ? 104  LEU   A CB    1 
ATOM   646   C  CG    . LEU   A  1  106  ? -14.112 56.447  62.160  1.00 18.13 ? 104  LEU   A CG    1 
ATOM   647   C  CD1   . LEU   A  1  106  ? -13.577 57.871  62.067  1.00 22.66 ? 104  LEU   A CD1   1 
ATOM   648   C  CD2   . LEU   A  1  106  ? -13.119 55.420  61.651  1.00 21.33 ? 104  LEU   A CD2   1 
ATOM   649   N  N     . ALA   A  1  107  ? -17.523 55.857  63.146  1.00 17.33 ? 105  ALA   A N     1 
ATOM   650   C  CA    . ALA   A  1  107  ? -18.630 55.780  62.208  1.00 19.20 ? 105  ALA   A CA    1 
ATOM   651   C  C     . ALA   A  1  107  ? -19.643 56.870  62.509  1.00 22.15 ? 105  ALA   A C     1 
ATOM   652   O  O     . ALA   A  1  107  ? -20.118 57.550  61.592  1.00 21.24 ? 105  ALA   A O     1 
ATOM   653   C  CB    . ALA   A  1  107  ? -19.269 54.395  62.270  1.00 17.45 ? 105  ALA   A CB    1 
ATOM   654   N  N     . GLU   A  1  108  ? -19.951 57.073  63.792  1.00 19.54 ? 106  GLU   A N     1 
ATOM   655   C  CA    . GLU   A  1  108  ? -20.857 58.142  64.196  1.00 19.94 ? 106  GLU   A CA    1 
ATOM   656   C  C     . GLU   A  1  108  ? -20.378 59.490  63.672  1.00 26.17 ? 106  GLU   A C     1 
ATOM   657   O  O     . GLU   A  1  108  ? -21.162 60.271  63.117  1.00 25.87 ? 106  GLU   A O     1 
ATOM   658   C  CB    . GLU   A  1  108  ? -20.947 58.157  65.728  1.00 21.57 ? 106  GLU   A CB    1 
ATOM   659   C  CG    . GLU   A  1  108  ? -21.831 59.267  66.297  1.00 22.98 ? 106  GLU   A CG    1 
ATOM   660   C  CD    . GLU   A  1  108  ? -21.522 59.576  67.749  1.00 25.61 ? 106  GLU   A CD    1 
ATOM   661   O  OE1   . GLU   A  1  108  ? -21.006 58.687  68.472  1.00 23.74 ? 106  GLU   A OE1   1 
ATOM   662   O  OE2   . GLU   A  1  108  ? -21.793 60.721  68.168  1.00 26.87 ? 106  GLU   A OE2   1 
ATOM   663   N  N     . ALA   A  1  109  ? -19.079 59.769  63.825  1.00 22.92 ? 107  ALA   A N     1 
ATOM   664   C  CA    . ALA   A  1  109  ? -18.521 61.035  63.363  1.00 23.72 ? 107  ALA   A CA    1 
ATOM   665   C  C     . ALA   A  1  109  ? -18.605 61.157  61.849  1.00 26.53 ? 107  ALA   A C     1 
ATOM   666   O  O     . ALA   A  1  109  ? -18.949 62.223  61.325  1.00 29.55 ? 107  ALA   A O     1 
ATOM   667   C  CB    . ALA   A  1  109  ? -17.071 61.161  63.821  1.00 25.76 ? 107  ALA   A CB    1 
ATOM   668   N  N     . LEU   A  1  110  ? -18.284 60.079  61.132  1.00 23.10 ? 108  LEU   A N     1 
ATOM   669   C  CA    . LEU   A  1  110  ? -18.360 60.103  59.679  1.00 23.95 ? 108  LEU   A CA    1 
ATOM   670   C  C     . LEU   A  1  110  ? -19.778 60.350  59.198  1.00 24.75 ? 108  LEU   A C     1 
ATOM   671   O  O     . LEU   A  1  110  ? -19.974 60.964  58.140  1.00 26.98 ? 108  LEU   A O     1 
ATOM   672   C  CB    . LEU   A  1  110  ? -17.822 58.793  59.104  1.00 21.83 ? 108  LEU   A CB    1 
ATOM   673   C  CG    . LEU   A  1  110  ? -16.304 58.666  59.233  1.00 23.45 ? 108  LEU   A CG    1 
ATOM   674   C  CD1   . LEU   A  1  110  ? -15.844 57.253  58.932  1.00 22.74 ? 108  LEU   A CD1   1 
ATOM   675   C  CD2   . LEU   A  1  110  ? -15.637 59.657  58.279  1.00 28.56 ? 108  LEU   A CD2   1 
ATOM   676   N  N     . LEU   A  1  111  ? -20.775 59.876  59.945  1.00 23.93 ? 109  LEU   A N     1 
ATOM   677   C  CA    . LEU   A  1  111  ? -22.172 60.090  59.593  1.00 26.27 ? 109  LEU   A CA    1 
ATOM   678   C  C     . LEU   A  1  111  ? -22.647 61.504  59.893  1.00 32.47 ? 109  LEU   A C     1 
ATOM   679   O  O     . LEU   A  1  111  ? -23.734 61.880  59.442  1.00 34.10 ? 109  LEU   A O     1 
ATOM   680   C  CB    . LEU   A  1  111  ? -23.056 59.058  60.302  1.00 26.20 ? 109  LEU   A CB    1 
ATOM   681   C  CG    . LEU   A  1  111  ? -22.850 57.630  59.787  1.00 26.05 ? 109  LEU   A CG    1 
ATOM   682   C  CD1   . LEU   A  1  111  ? -23.551 56.621  60.664  1.00 28.40 ? 109  LEU   A CD1   1 
ATOM   683   C  CD2   . LEU   A  1  111  ? -23.302 57.498  58.341  1.00 26.84 ? 109  LEU   A CD2   1 
ATOM   684   N  N     . ARG   A  1  112  ? -21.874 62.288  60.647  1.00 31.57 ? 110  ARG   A N     1 
ATOM   685   C  CA    . ARG   A  1  112  ? -22.146 63.716  60.770  1.00 34.27 ? 110  ARG   A CA    1 
ATOM   686   C  C     . ARG   A  1  112  ? -21.782 64.484  59.504  1.00 37.85 ? 110  ARG   A C     1 
ATOM   687   O  O     . ARG   A  1  112  ? -22.176 65.647  59.373  1.00 39.34 ? 110  ARG   A O     1 
ATOM   688   C  CB    . ARG   A  1  112  ? -21.433 64.303  61.992  1.00 35.83 ? 110  ARG   A CB    1 
ATOM   689   C  CG    . ARG   A  1  112  ? -21.933 63.758  63.332  1.00 31.60 ? 110  ARG   A CG    1 
ATOM   690   C  CD    . ARG   A  1  112  ? -20.920 63.983  64.455  1.00 33.94 ? 110  ARG   A CD    1 
ATOM   691   N  NE    . ARG   A  1  112  ? -20.818 65.378  64.864  1.00 43.80 ? 110  ARG   A NE    1 
ATOM   692   C  CZ    . ARG   A  1  112  ? -21.518 65.931  65.848  1.00 50.39 ? 110  ARG   A CZ    1 
ATOM   693   N  NH1   . ARG   A  1  112  ? -22.405 65.237  66.544  1.00 45.97 ? 110  ARG   A NH1   1 
ATOM   694   N  NH2   . ARG   A  1  112  ? -21.324 67.215  66.141  1.00 51.13 ? 110  ARG   A NH2   1 
ATOM   695   N  N     . ILE   A  1  113  ? -21.043 63.872  58.583  1.00 34.55 ? 111  ILE   A N     1 
ATOM   696   C  CA    . ILE   A  1  113  ? -20.819 64.434  57.251  1.00 35.55 ? 111  ILE   A CA    1 
ATOM   697   C  C     . ILE   A  1  113  ? -22.042 64.134  56.393  1.00 38.21 ? 111  ILE   A C     1 
ATOM   698   O  O     . ILE   A  1  113  ? -22.302 62.965  56.075  1.00 40.20 ? 111  ILE   A O     1 
ATOM   699   C  CB    . ILE   A  1  113  ? -19.543 63.867  56.614  1.00 31.95 ? 111  ILE   A CB    1 
ATOM   700   C  CG1   . ILE   A  1  113  ? -18.322 64.273  57.433  1.00 35.01 ? 111  ILE   A CG1   1 
ATOM   701   C  CG2   . ILE   A  1  113  ? -19.418 64.338  55.170  1.00 37.87 ? 111  ILE   A CG2   1 
ATOM   702   C  CD1   . ILE   A  1  113  ? -17.082 63.529  57.053  1.00 36.69 ? 111  ILE   A CD1   1 
ATOM   703   N  N     . PRO   A  1  114  ? -22.819 65.148  55.989  1.00 45.59 ? 112  PRO   A N     1 
ATOM   704   C  CA    . PRO   A  1  114  ? -24.086 64.880  55.291  1.00 40.63 ? 112  PRO   A CA    1 
ATOM   705   C  C     . PRO   A  1  114  ? -23.941 64.257  53.910  1.00 43.12 ? 112  PRO   A C     1 
ATOM   706   O  O     . PRO   A  1  114  ? -24.651 63.300  53.582  1.00 48.98 ? 112  PRO   A O     1 
ATOM   707   C  CB    . PRO   A  1  114  ? -24.744 66.265  55.209  1.00 44.68 ? 112  PRO   A CB    1 
ATOM   708   C  CG    . PRO   A  1  114  ? -24.082 67.069  56.288  1.00 51.47 ? 112  PRO   A CG    1 
ATOM   709   C  CD    . PRO   A  1  114  ? -22.668 66.571  56.331  1.00 47.86 ? 112  PRO   A CD    1 
ATOM   710   N  N     . ASP   A  1  115  ? -23.041 64.785  53.085  1.00 46.36 ? 113  ASP   A N     1 
ATOM   711   C  CA    . ASP   A  1  115  ? -22.937 64.329  51.704  1.00 47.18 ? 113  ASP   A CA    1 
ATOM   712   C  C     . ASP   A  1  115  ? -22.216 62.988  51.647  1.00 43.82 ? 113  ASP   A C     1 
ATOM   713   O  O     . ASP   A  1  115  ? -21.073 62.871  52.102  1.00 42.30 ? 113  ASP   A O     1 
ATOM   714   C  CB    . ASP   A  1  115  ? -22.210 65.359  50.846  1.00 44.06 ? 113  ASP   A CB    1 
ATOM   715   C  CG    . ASP   A  1  115  ? -22.109 64.927  49.402  1.00 48.20 ? 113  ASP   A CG    1 
ATOM   716   O  OD1   . ASP   A  1  115  ? -23.167 64.670  48.787  1.00 55.98 ? 113  ASP   A OD1   1 
ATOM   717   O  OD2   . ASP   A  1  115  ? -20.976 64.833  48.885  1.00 50.21 ? 113  ASP   A OD2   1 
ATOM   718   N  N     . THR   A  1  116  ? -22.879 61.988  51.061  1.00 41.81 ? 114  THR   A N     1 
ATOM   719   C  CA    . THR   A  1  116  ? -22.329 60.637  51.027  1.00 37.54 ? 114  THR   A CA    1 
ATOM   720   C  C     . THR   A  1  116  ? -21.017 60.581  50.256  1.00 42.73 ? 114  THR   A C     1 
ATOM   721   O  O     . THR   A  1  116  ? -20.057 59.940  50.699  1.00 40.56 ? 114  THR   A O     1 
ATOM   722   C  CB    . THR   A  1  116  ? -23.351 59.681  50.419  1.00 43.51 ? 114  THR   A CB    1 
ATOM   723   O  OG1   . THR   A  1  116  ? -24.499 59.605  51.274  1.00 45.52 ? 114  THR   A OG1   1 
ATOM   724   C  CG2   . THR   A  1  116  ? -22.747 58.295  50.241  1.00 46.01 ? 114  THR   A CG2   1 
ATOM   725   N  N     . ALA   A  1  117  ? -20.955 61.242  49.098  1.00 40.96 ? 115  ALA   A N     1 
ATOM   726   C  CA    . ALA   A  1  117  ? -19.728 61.227  48.309  1.00 39.22 ? 115  ALA   A CA    1 
ATOM   727   C  C     . ALA   A  1  117  ? -18.578 61.885  49.058  1.00 34.85 ? 115  ALA   A C     1 
ATOM   728   O  O     . ALA   A  1  117  ? -17.435 61.420  48.986  1.00 38.92 ? 115  ALA   A O     1 
ATOM   729   C  CB    . ALA   A  1  117  ? -19.959 61.911  46.960  1.00 45.59 ? 115  ALA   A CB    1 
ATOM   730   N  N     . THR   A  1  118  ? -18.858 62.972  49.779  1.00 37.26 ? 116  THR   A N     1 
ATOM   731   C  CA    . THR   A  1  118  ? -17.814 63.613  50.570  1.00 38.21 ? 116  THR   A CA    1 
ATOM   732   C  C     . THR   A  1  118  ? -17.317 62.678  51.664  1.00 32.67 ? 116  THR   A C     1 
ATOM   733   O  O     . THR   A  1  118  ? -16.110 62.580  51.908  1.00 36.30 ? 116  THR   A O     1 
ATOM   734   C  CB    . THR   A  1  118  ? -18.346 64.905  51.191  1.00 36.55 ? 116  THR   A CB    1 
ATOM   735   O  OG1   . THR   A  1  118  ? -18.865 65.753  50.161  1.00 51.76 ? 116  THR   A OG1   1 
ATOM   736   C  CG2   . THR   A  1  118  ? -17.240 65.638  51.929  1.00 37.28 ? 116  THR   A CG2   1 
ATOM   737   N  N     . ARG   A  1  119  ? -18.238 61.985  52.330  1.00 35.59 ? 117  ARG   A N     1 
ATOM   738   C  CA    A ARG   A  1  119  ? -17.852 61.052  53.383  0.80 33.60 ? 117  ARG   A CA    1 
ATOM   739   C  CA    B ARG   A  1  119  ? -17.843 61.056  53.383  0.20 33.58 ? 117  ARG   A CA    1 
ATOM   740   C  C     . ARG   A  1  119  ? -16.978 59.932  52.827  1.00 31.05 ? 117  ARG   A C     1 
ATOM   741   O  O     . ARG   A  1  119  ? -15.924 59.611  53.388  1.00 33.42 ? 117  ARG   A O     1 
ATOM   742   C  CB    A ARG   A  1  119  ? -19.111 60.478  54.028  0.80 31.59 ? 117  ARG   A CB    1 
ATOM   743   C  CB    B ARG   A  1  119  ? -19.077 60.486  54.082  0.20 31.66 ? 117  ARG   A CB    1 
ATOM   744   C  CG    A ARG   A  1  119  ? -18.849 59.644  55.272  0.80 27.76 ? 117  ARG   A CG    1 
ATOM   745   C  CG    B ARG   A  1  119  ? -18.750 59.306  54.987  0.20 28.99 ? 117  ARG   A CG    1 
ATOM   746   C  CD    A ARG   A  1  119  ? -20.101 58.885  55.676  0.80 29.32 ? 117  ARG   A CD    1 
ATOM   747   C  CD    B ARG   A  1  119  ? -19.948 58.833  55.791  0.20 29.58 ? 117  ARG   A CD    1 
ATOM   748   N  NE    A ARG   A  1  119  ? -21.242 59.770  55.865  0.80 29.79 ? 117  ARG   A NE    1 
ATOM   749   N  NE    B ARG   A  1  119  ? -21.080 58.454  54.955  0.20 29.01 ? 117  ARG   A NE    1 
ATOM   750   C  CZ    A ARG   A  1  119  ? -22.427 59.601  55.293  0.80 30.42 ? 117  ARG   A CZ    1 
ATOM   751   C  CZ    B ARG   A  1  119  ? -22.206 59.148  54.865  0.20 31.22 ? 117  ARG   A CZ    1 
ATOM   752   N  NH1   A ARG   A  1  119  ? -22.676 58.566  54.508  0.80 30.78 ? 117  ARG   A NH1   1 
ATOM   753   N  NH1   B ARG   A  1  119  ? -22.381 60.270  55.543  0.20 31.82 ? 117  ARG   A NH1   1 
ATOM   754   N  NH2   A ARG   A  1  119  ? -23.394 60.483  55.531  0.80 36.40 ? 117  ARG   A NH2   1 
ATOM   755   N  NH2   B ARG   A  1  119  ? -23.183 58.700  54.083  0.20 32.63 ? 117  ARG   A NH2   1 
ATOM   756   N  N     . ASP   A  1  120  ? -17.407 59.325  51.718  1.00 33.02 ? 118  ASP   A N     1 
ATOM   757   C  CA    . ASP   A  1  120  ? -16.672 58.199  51.154  1.00 33.68 ? 118  ASP   A CA    1 
ATOM   758   C  C     . ASP   A  1  120  ? -15.280 58.615  50.698  1.00 36.62 ? 118  ASP   A C     1 
ATOM   759   O  O     . ASP   A  1  120  ? -14.319 57.849  50.835  1.00 34.99 ? 118  ASP   A O     1 
ATOM   760   C  CB    . ASP   A  1  120  ? -17.462 57.569  50.008  1.00 34.52 ? 118  ASP   A CB    1 
ATOM   761   C  CG    . ASP   A  1  120  ? -18.801 57.021  50.462  1.00 43.62 ? 118  ASP   A CG    1 
ATOM   762   O  OD1   . ASP   A  1  120  ? -19.055 57.032  51.683  1.00 41.05 ? 118  ASP   A OD1   1 
ATOM   763   O  OD2   . ASP   A  1  120  ? -19.600 56.583  49.603  1.00 40.99 ? 118  ASP   A OD2   1 
ATOM   764   N  N     . ALA   A  1  121  ? -15.151 59.825  50.146  1.00 35.54 ? 119  ALA   A N     1 
ATOM   765   C  CA    . ALA   A  1  121  ? -13.835 60.310  49.746  1.00 37.22 ? 119  ALA   A CA    1 
ATOM   766   C  C     . ALA   A  1  121  ? -12.937 60.530  50.957  1.00 37.41 ? 119  ALA   A C     1 
ATOM   767   O  O     . ALA   A  1  121  ? -11.744 60.197  50.927  1.00 37.29 ? 119  ALA   A O     1 
ATOM   768   C  CB    . ALA   A  1  121  ? -13.971 61.595  48.932  1.00 38.63 ? 119  ALA   A CB    1 
ATOM   769   N  N     . LEU   A  1  122  ? -13.487 61.098  52.032  1.00 35.83 ? 120  LEU   A N     1 
ATOM   770   C  CA    . LEU   A  1  122  ? -12.699 61.257  53.248  1.00 37.01 ? 120  LEU   A CA    1 
ATOM   771   C  C     . LEU   A  1  122  ? -12.242 59.903  53.776  1.00 36.79 ? 120  LEU   A C     1 
ATOM   772   O  O     . LEU   A  1  122  ? -11.086 59.747  54.188  1.00 34.75 ? 120  LEU   A O     1 
ATOM   773   C  CB    . LEU   A  1  122  ? -13.505 62.010  54.302  1.00 38.16 ? 120  LEU   A CB    1 
ATOM   774   C  CG    . LEU   A  1  122  ? -12.690 62.488  55.503  1.00 35.85 ? 120  LEU   A CG    1 
ATOM   775   C  CD1   . LEU   A  1  122  ? -11.655 63.510  55.064  1.00 43.00 ? 120  LEU   A CD1   1 
ATOM   776   C  CD2   . LEU   A  1  122  ? -13.587 63.057  56.579  1.00 34.84 ? 120  LEU   A CD2   1 
ATOM   777   N  N     . ILE   A  1  123  ? -13.129 58.906  53.741  1.00 34.74 ? 121  ILE   A N     1 
ATOM   778   C  CA    . ILE   A  1  123  ? -12.771 57.560  54.186  1.00 33.38 ? 121  ILE   A CA    1 
ATOM   779   C  C     . ILE   A  1  123  ? -11.656 56.990  53.319  1.00 35.44 ? 121  ILE   A C     1 
ATOM   780   O  O     . ILE   A  1  123  ? -10.607 56.570  53.821  1.00 34.57 ? 121  ILE   A O     1 
ATOM   781   C  CB    . ILE   A  1  123  ? -14.006 56.644  54.181  1.00 30.99 ? 121  ILE   A CB    1 
ATOM   782   C  CG1   . ILE   A  1  123  ? -14.998 57.075  55.265  1.00 30.43 ? 121  ILE   A CG1   1 
ATOM   783   C  CG2   . ILE   A  1  123  ? -13.583 55.175  54.325  1.00 27.55 ? 121  ILE   A CG2   1 
ATOM   784   C  CD1   . ILE   A  1  123  ? -16.354 56.459  55.116  1.00 29.92 ? 121  ILE   A CD1   1 
ATOM   785   N  N     . ARG   A  1  124  ? -11.874 56.965  52.001  1.00 33.93 ? 122  ARG   A N     1 
ATOM   786   C  CA    . ARG   A  1  124  ? -10.940 56.285  51.106  1.00 36.76 ? 122  ARG   A CA    1 
ATOM   787   C  C     . ARG   A  1  124  ? -9.592  56.992  51.055  1.00 41.54 ? 122  ARG   A C     1 
ATOM   788   O  O     . ARG   A  1  124  ? -8.542  56.340  51.102  1.00 42.28 ? 122  ARG   A O     1 
ATOM   789   C  CB    . ARG   A  1  124  ? -11.536 56.188  49.702  1.00 37.84 ? 122  ARG   A CB    1 
ATOM   790   N  N     . ASP   A  1  125  ? -9.599  58.320  50.973  1.00 42.51 ? 123  ASP   A N     1 
ATOM   791   C  CA    . ASP   A  1  125  ? -8.374  59.059  50.702  1.00 48.34 ? 123  ASP   A CA    1 
ATOM   792   C  C     . ASP   A  1  125  ? -7.649  59.513  51.960  1.00 47.86 ? 123  ASP   A C     1 
ATOM   793   O  O     . ASP   A  1  125  ? -6.418  59.636  51.938  1.00 50.61 ? 123  ASP   A O     1 
ATOM   794   C  CB    . ASP   A  1  125  ? -8.670  60.275  49.817  1.00 53.14 ? 123  ASP   A CB    1 
ATOM   795   C  CG    . ASP   A  1  125  ? -9.335  59.898  48.504  1.00 55.11 ? 123  ASP   A CG    1 
ATOM   796   O  OD1   . ASP   A  1  125  ? -8.996  58.832  47.944  1.00 58.94 ? 123  ASP   A OD1   1 
ATOM   797   O  OD2   . ASP   A  1  125  ? -10.200 60.667  48.031  1.00 55.91 ? 123  ASP   A OD2   1 
ATOM   798   N  N     . LYS   A  1  126  ? -8.370  59.762  53.054  1.00 41.51 ? 124  LYS   A N     1 
ATOM   799   C  CA    . LYS   A  1  126  ? -7.782  60.366  54.245  1.00 41.05 ? 124  LYS   A CA    1 
ATOM   800   C  C     . LYS   A  1  126  ? -7.844  59.474  55.477  1.00 45.29 ? 124  LYS   A C     1 
ATOM   801   O  O     . LYS   A  1  126  ? -6.804  59.222  56.097  1.00 49.38 ? 124  LYS   A O     1 
ATOM   802   C  CB    . LYS   A  1  126  ? -8.437  61.727  54.538  1.00 47.67 ? 124  LYS   A CB    1 
ATOM   803   N  N     . ILE   A  1  127  ? -9.033  58.995  55.858  1.00 39.26 ? 125  ILE   A N     1 
ATOM   804   C  CA    . ILE   A  1  127  ? -9.167  58.221  57.096  1.00 36.30 ? 125  ILE   A CA    1 
ATOM   805   C  C     . ILE   A  1  127  ? -8.406  56.906  56.991  1.00 37.96 ? 125  ILE   A C     1 
ATOM   806   O  O     . ILE   A  1  127  ? -7.631  56.540  57.883  1.00 42.31 ? 125  ILE   A O     1 
ATOM   807   C  CB    . ILE   A  1  127  ? -10.649 57.972  57.437  1.00 33.28 ? 125  ILE   A CB    1 
ATOM   808   C  CG1   . ILE   A  1  127  ? -11.463 59.269  57.396  1.00 40.15 ? 125  ILE   A CG1   1 
ATOM   809   C  CG2   . ILE   A  1  127  ? -10.773 57.307  58.813  1.00 34.19 ? 125  ILE   A CG2   1 
ATOM   810   C  CD1   . ILE   A  1  127  ? -10.982 60.323  58.350  1.00 34.67 ? 125  ILE   A CD1   1 
ATOM   811   N  N     . ALA   A  1  128  ? -8.640  56.162  55.910  1.00 32.85 ? 126  ALA   A N     1 
ATOM   812   C  CA    . ALA   A  1  128  ? -8.057  54.832  55.787  1.00 32.16 ? 126  ALA   A CA    1 
ATOM   813   C  C     . ALA   A  1  128  ? -6.542  54.900  55.669  1.00 42.29 ? 126  ALA   A C     1 
ATOM   814   O  O     . ALA   A  1  128  ? -5.835  54.050  56.222  1.00 42.35 ? 126  ALA   A O     1 
ATOM   815   C  CB    . ALA   A  1  128  ? -8.655  54.104  54.588  1.00 32.93 ? 126  ALA   A CB    1 
ATOM   816   N  N     . ASP   A  1  129  ? -6.030  55.915  54.967  1.00 55.32 ? 127  ASP   A N     1 
ATOM   817   C  CA    . ASP   A  1  129  ? -4.609  55.985  54.643  1.00 59.07 ? 127  ASP   A CA    1 
ATOM   818   C  C     . ASP   A  1  129  ? -3.739  56.291  55.854  1.00 58.99 ? 127  ASP   A C     1 
ATOM   819   O  O     . ASP   A  1  129  ? -2.538  56.000  55.824  1.00 64.19 ? 127  ASP   A O     1 
ATOM   820   C  CB    . ASP   A  1  129  ? -4.366  57.020  53.541  1.00 57.55 ? 127  ASP   A CB    1 
ATOM   821   N  N     . GLY   A  1  130  ? -4.302  56.869  56.911  1.00 56.72 ? 128  GLY   A N     1 
ATOM   822   C  CA    . GLY   A  1  130  ? -3.503  57.113  58.094  1.00 56.46 ? 128  GLY   A CA    1 
ATOM   823   C  C     . GLY   A  1  130  ? -4.173  57.906  59.195  1.00 58.80 ? 128  GLY   A C     1 
ATOM   824   O  O     . GLY   A  1  130  ? -5.085  57.413  59.867  1.00 58.24 ? 128  GLY   A O     1 
ATOM   825   N  N     . ASN   A  1  131  ? -3.717  59.142  59.385  1.00 60.59 ? 129  ASN   A N     1 
ATOM   826   C  CA    . ASN   A  1  131  ? -4.088  59.953  60.543  1.00 55.93 ? 129  ASN   A CA    1 
ATOM   827   C  C     . ASN   A  1  131  ? -5.560  60.335  60.458  1.00 49.17 ? 129  ASN   A C     1 
ATOM   828   O  O     . ASN   A  1  131  ? -5.933  61.282  59.764  1.00 52.74 ? 129  ASN   A O     1 
ATOM   829   C  CB    . ASN   A  1  131  ? -3.203  61.193  60.611  1.00 54.84 ? 129  ASN   A CB    1 
ATOM   830   N  N     . TRP   A  1  132  ? -6.406  59.592  61.175  1.00 45.59 ? 130  TRP   A N     1 
ATOM   831   C  CA    . TRP   A  1  132  ? -7.805  59.984  61.307  1.00 36.92 ? 130  TRP   A CA    1 
ATOM   832   C  C     . TRP   A  1  132  ? -7.949  61.233  62.163  1.00 35.20 ? 130  TRP   A C     1 
ATOM   833   O  O     . TRP   A  1  132  ? -8.921  61.982  62.011  1.00 41.45 ? 130  TRP   A O     1 
ATOM   834   C  CB    . TRP   A  1  132  ? -8.603  58.844  61.937  1.00 36.44 ? 130  TRP   A CB    1 
ATOM   835   C  CG    . TRP   A  1  132  ? -8.047  58.418  63.269  1.00 31.95 ? 130  TRP   A CG    1 
ATOM   836   C  CD1   . TRP   A  1  132  ? -7.132  57.432  63.494  1.00 31.17 ? 130  TRP   A CD1   1 
ATOM   837   C  CD2   . TRP   A  1  132  ? -8.368  58.970  64.554  1.00 25.02 ? 130  TRP   A CD2   1 
ATOM   838   N  NE1   . TRP   A  1  132  ? -6.868  57.330  64.839  1.00 27.84 ? 130  TRP   A NE1   1 
ATOM   839   C  CE2   . TRP   A  1  132  ? -7.603  58.270  65.512  1.00 24.31 ? 130  TRP   A CE2   1 
ATOM   840   C  CE3   . TRP   A  1  132  ? -9.218  59.989  64.986  1.00 26.72 ? 130  TRP   A CE3   1 
ATOM   841   C  CZ2   . TRP   A  1  132  ? -7.676  58.547  66.874  1.00 26.46 ? 130  TRP   A CZ2   1 
ATOM   842   C  CZ3   . TRP   A  1  132  ? -9.282  60.268  66.336  1.00 25.80 ? 130  TRP   A CZ3   1 
ATOM   843   C  CH2   . TRP   A  1  132  ? -8.518  59.549  67.266  1.00 26.04 ? 130  TRP   A CH2   1 
ATOM   844   N  N     . LYS   A  1  133  ? -7.001  61.462  63.076  1.00 38.95 ? 131  LYS   A N     1 
ATOM   845   C  CA    . LYS   A  1  133  ? -7.083  62.618  63.962  1.00 42.63 ? 131  LYS   A CA    1 
ATOM   846   C  C     . LYS   A  1  133  ? -7.013  63.920  63.176  1.00 50.70 ? 131  LYS   A C     1 
ATOM   847   O  O     . LYS   A  1  133  ? -7.705  64.891  63.504  1.00 55.61 ? 131  LYS   A O     1 
ATOM   848   C  CB    . LYS   A  1  133  ? -5.966  62.553  65.003  1.00 41.23 ? 131  LYS   A CB    1 
ATOM   849   N  N     . SER   A  1  134  ? -6.197  63.950  62.118  1.00 54.98 ? 132  SER   A N     1 
ATOM   850   C  CA    . SER   A  1  134  ? -6.005  65.171  61.342  1.00 57.87 ? 132  SER   A CA    1 
ATOM   851   C  C     . SER   A  1  134  ? -7.286  65.649  60.671  1.00 58.73 ? 132  SER   A C     1 
ATOM   852   O  O     . SER   A  1  134  ? -7.412  66.844  60.384  1.00 62.70 ? 132  SER   A O     1 
ATOM   853   C  CB    . SER   A  1  134  ? -4.921  64.949  60.286  1.00 56.32 ? 132  SER   A CB    1 
ATOM   854   O  OG    . SER   A  1  134  ? -3.746  64.415  60.870  1.00 59.29 ? 132  SER   A OG    1 
ATOM   855   N  N     . HIS   A  1  135  ? -8.243  64.753  60.422  1.00 57.77 ? 133  HIS   A N     1 
ATOM   856   C  CA    . HIS   A  1  135  ? -9.440  65.104  59.674  1.00 55.57 ? 133  HIS   A CA    1 
ATOM   857   C  C     . HIS   A  1  135  ? -10.718 65.090  60.500  1.00 58.49 ? 133  HIS   A C     1 
ATOM   858   O  O     . HIS   A  1  135  ? -11.710 65.694  60.078  1.00 59.79 ? 133  HIS   A O     1 
ATOM   859   C  CB    . HIS   A  1  135  ? -9.604  64.176  58.462  1.00 55.06 ? 133  HIS   A CB    1 
ATOM   860   C  CG    . HIS   A  1  135  ? -8.351  64.016  57.657  1.00 60.12 ? 133  HIS   A CG    1 
ATOM   861   N  ND1   . HIS   A  1  135  ? -7.345  63.141  58.012  1.00 59.77 ? 133  HIS   A ND1   1 
ATOM   862   C  CD2   . HIS   A  1  135  ? -7.936  64.625  56.520  1.00 56.38 ? 133  HIS   A CD2   1 
ATOM   863   C  CE1   . HIS   A  1  135  ? -6.368  63.214  57.127  1.00 64.47 ? 133  HIS   A CE1   1 
ATOM   864   N  NE2   . HIS   A  1  135  ? -6.701  64.107  56.211  1.00 65.62 ? 133  HIS   A NE2   1 
ATOM   865   N  N     . LEU   A  1  136  ? -10.724 64.429  61.653  1.00 54.98 ? 134  LEU   A N     1 
ATOM   866   C  CA    . LEU   A  1  136  ? -11.895 64.425  62.523  1.00 54.67 ? 134  LEU   A CA    1 
ATOM   867   C  C     . LEU   A  1  136  ? -11.488 64.617  63.984  1.00 60.39 ? 134  LEU   A C     1 
ATOM   868   O  O     . LEU   A  1  136  ? -12.261 65.131  64.796  1.00 62.59 ? 134  LEU   A O     1 
ATOM   869   C  CB    . LEU   A  1  136  ? -12.686 63.122  62.360  1.00 51.41 ? 134  LEU   A CB    1 
ATOM   870   C  CG    . LEU   A  1  136  ? -13.378 62.870  61.017  1.00 48.30 ? 134  LEU   A CG    1 
ATOM   871   C  CD1   . LEU   A  1  136  ? -13.849 61.434  60.934  1.00 43.39 ? 134  LEU   A CD1   1 
ATOM   872   C  CD2   . LEU   A  1  136  ? -14.544 63.823  60.826  1.00 43.16 ? 134  LEU   A CD2   1 
ATOM   873   N  N     . SER   A  1  139  ? -12.312 69.918  67.561  1.00 43.07 ? 137  SER   A N     1 
ATOM   874   C  CA    . SER   A  1  139  ? -13.117 70.692  68.508  1.00 43.26 ? 137  SER   A CA    1 
ATOM   875   C  C     . SER   A  1  139  ? -13.995 69.797  69.386  1.00 42.80 ? 137  SER   A C     1 
ATOM   876   O  O     . SER   A  1  139  ? -14.368 70.167  70.502  1.00 41.00 ? 137  SER   A O     1 
ATOM   877   C  CB    . SER   A  1  139  ? -13.986 71.710  67.763  1.00 43.82 ? 137  SER   A CB    1 
ATOM   878   N  N     . ARG   A  1  140  ? -14.327 68.617  68.873  1.00 31.14 ? 138  ARG   A N     1 
ATOM   879   C  CA    . ARG   A  1  140  ? -15.178 67.660  69.569  1.00 32.30 ? 138  ARG   A CA    1 
ATOM   880   C  C     . ARG   A  1  140  ? -14.497 66.307  69.481  1.00 30.66 ? 138  ARG   A C     1 
ATOM   881   O  O     . ARG   A  1  140  ? -14.183 65.841  68.380  1.00 30.30 ? 138  ARG   A O     1 
ATOM   882   C  CB    . ARG   A  1  140  ? -16.560 67.603  68.910  1.00 35.05 ? 138  ARG   A CB    1 
ATOM   883   C  CG    . ARG   A  1  140  ? -17.471 66.463  69.367  1.00 36.39 ? 138  ARG   A CG    1 
ATOM   884   C  CD    . ARG   A  1  140  ? -18.678 66.356  68.439  1.00 43.03 ? 138  ARG   A CD    1 
ATOM   885   N  NE    . ARG   A  1  140  ? -19.525 65.195  68.698  1.00 44.13 ? 138  ARG   A NE    1 
ATOM   886   C  CZ    . ARG   A  1  140  ? -19.390 64.016  68.101  1.00 47.69 ? 138  ARG   A CZ    1 
ATOM   887   N  NH1   . ARG   A  1  140  ? -18.399 63.777  67.253  1.00 45.26 ? 138  ARG   A NH1   1 
ATOM   888   N  NH2   . ARG   A  1  140  ? -20.273 63.054  68.356  1.00 43.54 ? 138  ARG   A NH2   1 
ATOM   889   N  N     . SER   A  1  141  ? -14.243 65.692  70.634  1.00 27.55 ? 139  SER   A N     1 
ATOM   890   C  CA    . SER   A  1  141  ? -13.662 64.362  70.643  1.00 22.32 ? 139  SER   A CA    1 
ATOM   891   C  C     . SER   A  1  141  ? -14.523 63.425  69.811  1.00 22.72 ? 139  SER   A C     1 
ATOM   892   O  O     . SER   A  1  141  ? -15.755 63.481  69.845  1.00 22.50 ? 139  SER   A O     1 
ATOM   893   C  CB    . SER   A  1  141  ? -13.595 63.840  72.076  1.00 23.48 ? 139  SER   A CB    1 
ATOM   894   O  OG    . SER   A  1  141  ? -13.146 62.490  72.107  1.00 22.33 ? 139  SER   A OG    1 
ATOM   895   N  N     . LEU   A  1  142  ? -13.862 62.556  69.049  1.00 22.39 ? 140  LEU   A N     1 
ATOM   896   C  CA    . LEU   A  1  142  ? -14.597 61.507  68.363  1.00 21.16 ? 140  LEU   A CA    1 
ATOM   897   C  C     . LEU   A  1  142  ? -15.392 60.650  69.335  1.00 19.06 ? 140  LEU   A C     1 
ATOM   898   O  O     . LEU   A  1  142  ? -16.383 60.015  68.956  1.00 20.46 ? 140  LEU   A O     1 
ATOM   899   C  CB    . LEU   A  1  142  ? -13.591 60.599  67.670  1.00 22.75 ? 140  LEU   A CB    1 
ATOM   900   C  CG    . LEU   A  1  142  ? -13.915 60.223  66.245  1.00 29.23 ? 140  LEU   A CG    1 
ATOM   901   C  CD1   . LEU   A  1  142  ? -13.859 61.455  65.370  1.00 31.41 ? 140  LEU   A CD1   1 
ATOM   902   C  CD2   . LEU   A  1  142  ? -12.899 59.214  65.815  1.00 28.11 ? 140  LEU   A CD2   1 
ATOM   903   N  N     . PHE   A  1  143  ? -14.989 60.643  70.598  1.00 17.95 ? 141  PHE   A N     1 
ATOM   904   C  CA    . PHE   A  1  143  ? -15.417 59.640  71.551  1.00 17.15 ? 141  PHE   A CA    1 
ATOM   905   C  C     . PHE   A  1  143  ? -16.423 60.187  72.557  1.00 18.49 ? 141  PHE   A C     1 
ATOM   906   O  O     . PHE   A  1  143  ? -16.672 59.547  73.574  1.00 18.60 ? 141  PHE   A O     1 
ATOM   907   C  CB    . PHE   A  1  143  ? -14.175 59.050  72.229  1.00 16.16 ? 141  PHE   A CB    1 
ATOM   908   C  CG    . PHE   A  1  143  ? -13.158 58.562  71.239  1.00 17.10 ? 141  PHE   A CG    1 
ATOM   909   C  CD1   . PHE   A  1  143  ? -13.496 57.573  70.330  1.00 16.70 ? 141  PHE   A CD1   1 
ATOM   910   C  CD2   . PHE   A  1  143  ? -11.893 59.117  71.177  1.00 17.41 ? 141  PHE   A CD2   1 
ATOM   911   C  CE1   . PHE   A  1  143  ? -12.592 57.126  69.404  1.00 17.47 ? 141  PHE   A CE1   1 
ATOM   912   C  CE2   . PHE   A  1  143  ? -10.985 58.667  70.247  1.00 17.78 ? 141  PHE   A CE2   1 
ATOM   913   C  CZ    . PHE   A  1  143  ? -11.326 57.679  69.363  1.00 16.39 ? 141  PHE   A CZ    1 
ATOM   914   N  N     . VAL   A  1  144  ? -17.051 61.329  72.254  1.00 18.64 ? 142  VAL   A N     1 
ATOM   915   C  CA    A VAL   A  1  144  ? -17.971 61.931  73.215  0.37 19.63 ? 142  VAL   A CA    1 
ATOM   916   C  CA    B VAL   A  1  144  ? -18.007 61.948  73.182  0.63 19.62 ? 142  VAL   A CA    1 
ATOM   917   C  C     . VAL   A  1  144  ? -19.076 60.957  73.611  1.00 20.03 ? 142  VAL   A C     1 
ATOM   918   O  O     . VAL   A  1  144  ? -19.497 60.930  74.772  1.00 22.18 ? 142  VAL   A O     1 
ATOM   919   C  CB    A VAL   A  1  144  ? -18.521 63.275  72.702  0.37 20.93 ? 142  VAL   A CB    1 
ATOM   920   C  CB    B VAL   A  1  144  ? -18.632 63.210  72.553  0.63 20.67 ? 142  VAL   A CB    1 
ATOM   921   C  CG1   A VAL   A  1  144  ? -17.392 64.272  72.531  0.37 22.92 ? 142  VAL   A CG1   1 
ATOM   922   C  CG1   B VAL   A  1  144  ? -19.832 63.715  73.382  0.63 20.42 ? 142  VAL   A CG1   1 
ATOM   923   C  CG2   A VAL   A  1  144  ? -19.266 63.086  71.405  0.37 21.83 ? 142  VAL   A CG2   1 
ATOM   924   C  CG2   B VAL   A  1  144  ? -17.593 64.297  72.422  0.63 22.75 ? 142  VAL   A CG2   1 
ATOM   925   N  N     . ASN   A  1  145  ? -19.556 60.141  72.675  1.00 19.40 ? 143  ASN   A N     1 
ATOM   926   C  CA    . ASN   A  1  145  ? -20.622 59.200  72.984  1.00 19.93 ? 143  ASN   A CA    1 
ATOM   927   C  C     . ASN   A  1  145  ? -20.119 57.781  73.188  1.00 19.76 ? 143  ASN   A C     1 
ATOM   928   O  O     . ASN   A  1  145  ? -20.897 56.827  73.092  1.00 19.74 ? 143  ASN   A O     1 
ATOM   929   C  CB    . ASN   A  1  145  ? -21.699 59.255  71.904  1.00 22.92 ? 143  ASN   A CB    1 
ATOM   930   C  CG    . ASN   A  1  145  ? -22.452 60.553  71.930  1.00 22.31 ? 143  ASN   A CG    1 
ATOM   931   O  OD1   . ASN   A  1  145  ? -22.966 60.950  72.975  1.00 26.73 ? 143  ASN   A OD1   1 
ATOM   932   N  ND2   . ASN   A  1  145  ? -22.497 61.236  70.799  1.00 25.92 ? 143  ASN   A ND2   1 
ATOM   933   N  N     . ALA   A  1  146  ? -18.833 57.616  73.499  1.00 18.12 ? 144  ALA   A N     1 
ATOM   934   C  CA    . ALA   A  1  146  ? -18.293 56.270  73.615  1.00 18.26 ? 144  ALA   A CA    1 
ATOM   935   C  C     . ALA   A  1  146  ? -18.923 55.465  74.743  1.00 17.33 ? 144  ALA   A C     1 
ATOM   936   O  O     . ALA   A  1  146  ? -18.931 54.236  74.680  1.00 20.64 ? 144  ALA   A O     1 
ATOM   937   C  CB    . ALA   A  1  146  ? -16.781 56.319  73.790  1.00 18.41 ? 144  ALA   A CB    1 
ATOM   938   N  N     . ALA   A  1  147  ? -19.447 56.115  75.787  1.00 18.71 ? 145  ALA   A N     1 
ATOM   939   C  CA    . ALA   A  1  147  ? -20.099 55.333  76.833  1.00 21.58 ? 145  ALA   A CA    1 
ATOM   940   C  C     . ALA   A  1  147  ? -21.321 54.621  76.280  1.00 19.41 ? 145  ALA   A C     1 
ATOM   941   O  O     . ALA   A  1  147  ? -21.600 53.467  76.630  1.00 21.55 ? 145  ALA   A O     1 
ATOM   942   C  CB    . ALA   A  1  147  ? -20.478 56.223  78.018  1.00 25.49 ? 145  ALA   A CB    1 
ATOM   943   N  N     . THR   A  1  148  ? -22.042 55.284  75.382  1.00 19.42 ? 146  THR   A N     1 
ATOM   944   C  CA    . THR   A  1  148  ? -23.194 54.658  74.753  1.00 19.14 ? 146  THR   A CA    1 
ATOM   945   C  C     . THR   A  1  148  ? -22.757 53.531  73.836  1.00 17.14 ? 146  THR   A C     1 
ATOM   946   O  O     . THR   A  1  148  ? -23.272 52.409  73.914  1.00 19.36 ? 146  THR   A O     1 
ATOM   947   C  CB    . THR   A  1  148  ? -23.961 55.715  73.969  1.00 23.84 ? 146  THR   A CB    1 
ATOM   948   O  OG1   . THR   A  1  148  ? -24.357 56.743  74.877  1.00 25.00 ? 146  THR   A OG1   1 
ATOM   949   C  CG2   . THR   A  1  148  ? -25.193 55.110  73.311  1.00 28.30 ? 146  THR   A CG2   1 
ATOM   950   N  N     . TRP   A  1  149  ? -21.782 53.800  72.965  1.00 18.89 ? 147  TRP   A N     1 
ATOM   951   C  CA    . TRP   A  1  149  ? -21.289 52.726  72.118  1.00 18.66 ? 147  TRP   A CA    1 
ATOM   952   C  C     . TRP   A  1  149  ? -20.676 51.599  72.930  1.00 17.76 ? 147  TRP   A C     1 
ATOM   953   O  O     . TRP   A  1  149  ? -20.742 50.442  72.509  1.00 18.51 ? 147  TRP   A O     1 
ATOM   954   C  CB    . TRP   A  1  149  ? -20.284 53.256  71.099  1.00 17.99 ? 147  TRP   A CB    1 
ATOM   955   C  CG    . TRP   A  1  149  ? -20.924 54.128  70.091  1.00 18.50 ? 147  TRP   A CG    1 
ATOM   956   C  CD1   . TRP   A  1  149  ? -20.693 55.451  69.897  1.00 21.18 ? 147  TRP   A CD1   1 
ATOM   957   C  CD2   . TRP   A  1  149  ? -21.923 53.744  69.150  1.00 20.56 ? 147  TRP   A CD2   1 
ATOM   958   N  NE1   . TRP   A  1  149  ? -21.475 55.921  68.866  1.00 20.80 ? 147  TRP   A NE1   1 
ATOM   959   C  CE2   . TRP   A  1  149  ? -22.242 54.888  68.393  1.00 21.41 ? 147  TRP   A CE2   1 
ATOM   960   C  CE3   . TRP   A  1  149  ? -22.561 52.538  68.854  1.00 20.28 ? 147  TRP   A CE3   1 
ATOM   961   C  CZ2   . TRP   A  1  149  ? -23.193 54.869  67.369  1.00 21.89 ? 147  TRP   A CZ2   1 
ATOM   962   C  CZ3   . TRP   A  1  149  ? -23.506 52.516  67.831  1.00 24.28 ? 147  TRP   A CZ3   1 
ATOM   963   C  CH2   . TRP   A  1  149  ? -23.809 53.677  67.103  1.00 26.47 ? 147  TRP   A CH2   1 
ATOM   964   N  N     . GLY   A  1  150  ? -20.069 51.913  74.078  1.00 17.42 ? 148  GLY   A N     1 
ATOM   965   C  CA    . GLY   A  1  150  ? -19.585 50.855  74.949  1.00 19.69 ? 148  GLY   A CA    1 
ATOM   966   C  C     . GLY   A  1  150  ? -20.703 49.945  75.411  1.00 20.59 ? 148  GLY   A C     1 
ATOM   967   O  O     . GLY   A  1  150  ? -20.542 48.725  75.470  1.00 20.83 ? 148  GLY   A O     1 
ATOM   968   N  N     . LEU   A  1  151  ? -21.860 50.529  75.739  1.00 20.79 ? 149  LEU   A N     1 
ATOM   969   C  CA    . LEU   A  1  151  ? -23.009 49.713  76.103  1.00 23.19 ? 149  LEU   A CA    1 
ATOM   970   C  C     . LEU   A  1  151  ? -23.424 48.825  74.939  1.00 21.38 ? 149  LEU   A C     1 
ATOM   971   O  O     . LEU   A  1  151  ? -23.695 47.636  75.122  1.00 25.23 ? 149  LEU   A O     1 
ATOM   972   C  CB    . LEU   A  1  151  ? -24.155 50.622  76.553  1.00 27.30 ? 149  LEU   A CB    1 
ATOM   973   C  CG    . LEU   A  1  151  ? -25.250 50.074  77.460  1.00 34.09 ? 149  LEU   A CG    1 
ATOM   974   C  CD1   . LEU   A  1  151  ? -24.678 49.326  78.656  1.00 25.38 ? 149  LEU   A CD1   1 
ATOM   975   C  CD2   . LEU   A  1  151  ? -26.083 51.249  77.937  1.00 35.26 ? 149  LEU   A CD2   1 
ATOM   976   N  N     . VAL   A  1  152  ? -23.427 49.378  73.722  1.00 20.37 ? 150  VAL   A N     1 
ATOM   977   C  CA    . VAL   A  1  152  ? -23.793 48.607  72.533  1.00 22.28 ? 150  VAL   A CA    1 
ATOM   978   C  C     . VAL   A  1  152  ? -22.816 47.462  72.295  1.00 24.34 ? 150  VAL   A C     1 
ATOM   979   O  O     . VAL   A  1  152  ? -23.217 46.329  71.998  1.00 26.36 ? 150  VAL   A O     1 
ATOM   980   C  CB    . VAL   A  1  152  ? -23.883 49.536  71.306  1.00 22.99 ? 150  VAL   A CB    1 
ATOM   981   C  CG1   . VAL   A  1  152  ? -23.971 48.722  70.027  1.00 25.79 ? 150  VAL   A CG1   1 
ATOM   982   C  CG2   . VAL   A  1  152  ? -25.064 50.487  71.431  1.00 25.98 ? 150  VAL   A CG2   1 
ATOM   983   N  N     . VAL   A  1  153  ? -21.517 47.745  72.393  1.00 22.26 ? 151  VAL   A N     1 
ATOM   984   C  CA    . VAL   A  1  153  ? -20.505 46.752  72.054  1.00 23.90 ? 151  VAL   A CA    1 
ATOM   985   C  C     . VAL   A  1  153  ? -20.320 45.735  73.176  1.00 23.81 ? 151  VAL   A C     1 
ATOM   986   O  O     . VAL   A  1  153  ? -20.223 44.531  72.920  1.00 27.81 ? 151  VAL   A O     1 
ATOM   987   C  CB    . VAL   A  1  153  ? -19.183 47.455  71.694  1.00 22.62 ? 151  VAL   A CB    1 
ATOM   988   C  CG1   . VAL   A  1  153  ? -18.060 46.438  71.506  1.00 25.03 ? 151  VAL   A CG1   1 
ATOM   989   C  CG2   . VAL   A  1  153  ? -19.356 48.305  70.450  1.00 22.99 ? 151  VAL   A CG2   1 
ATOM   990   N  N     . THR   A  1  154  ? -20.252 46.192  74.427  1.00 25.00 ? 152  THR   A N     1 
ATOM   991   C  CA    . THR   A  1  154  ? -19.828 45.338  75.528  1.00 25.57 ? 152  THR   A CA    1 
ATOM   992   C  C     . THR   A  1  154  ? -20.957 44.960  76.469  1.00 28.19 ? 152  THR   A C     1 
ATOM   993   O  O     . THR   A  1  154  ? -20.777 44.049  77.283  1.00 28.50 ? 152  THR   A O     1 
ATOM   994   C  CB    . THR   A  1  154  ? -18.732 46.016  76.363  1.00 27.38 ? 152  THR   A CB    1 
ATOM   995   O  OG1   . THR   A  1  154  ? -19.310 47.055  77.168  1.00 28.05 ? 152  THR   A OG1   1 
ATOM   996   C  CG2   . THR   A  1  154  ? -17.655 46.607  75.470  1.00 26.80 ? 152  THR   A CG2   1 
ATOM   997   N  N     . GLY   A  1  155  ? -22.094 45.643  76.404  1.00 26.83 ? 153  GLY   A N     1 
ATOM   998   C  CA    . GLY   A  1  155  ? -23.153 45.430  77.369  1.00 25.08 ? 153  GLY   A CA    1 
ATOM   999   C  C     . GLY   A  1  155  ? -22.911 46.054  78.724  1.00 29.19 ? 153  GLY   A C     1 
ATOM   1000  O  O     . GLY   A  1  155  ? -23.749 45.888  79.623  1.00 27.64 ? 153  GLY   A O     1 
ATOM   1001  N  N     . LYS   A  1  156  ? -21.799 46.759  78.901  1.00 26.88 ? 154  LYS   A N     1 
ATOM   1002  C  CA    . LYS   A  1  156  ? -21.433 47.370  80.168  1.00 28.04 ? 154  LYS   A CA    1 
ATOM   1003  C  C     . LYS   A  1  156  ? -21.416 48.884  80.014  1.00 30.12 ? 154  LYS   A C     1 
ATOM   1004  O  O     . LYS   A  1  156  ? -21.058 49.413  78.956  1.00 26.02 ? 154  LYS   A O     1 
ATOM   1005  C  CB    . LYS   A  1  156  ? -20.058 46.882  80.636  1.00 34.97 ? 154  LYS   A CB    1 
ATOM   1006  N  N     . LEU   A  1  157  ? -21.826 49.579  81.062  1.00 26.52 ? 155  LEU   A N     1 
ATOM   1007  C  CA    . LEU   A  1  157  ? -21.828 51.029  81.068  1.00 27.61 ? 155  LEU   A CA    1 
ATOM   1008  C  C     . LEU   A  1  157  ? -20.609 51.521  81.835  1.00 32.84 ? 155  LEU   A C     1 
ATOM   1009  O  O     . LEU   A  1  157  ? -20.347 51.066  82.953  1.00 34.24 ? 155  LEU   A O     1 
ATOM   1010  C  CB    . LEU   A  1  157  ? -23.099 51.544  81.730  1.00 29.30 ? 155  LEU   A CB    1 
ATOM   1011  C  CG    . LEU   A  1  157  ? -23.140 53.056  81.878  1.00 36.95 ? 155  LEU   A CG    1 
ATOM   1012  C  CD1   . LEU   A  1  157  ? -23.117 53.722  80.507  1.00 33.57 ? 155  LEU   A CD1   1 
ATOM   1013  C  CD2   . LEU   A  1  157  ? -24.382 53.431  82.658  1.00 36.09 ? 155  LEU   A CD2   1 
ATOM   1014  N  N     . THR   A  1  158  ? -19.854 52.426  81.220  1.00 37.31 ? 156  THR   A N     1 
ATOM   1015  C  CA    . THR   A  1  158  ? -18.748 53.118  81.869  1.00 38.01 ? 156  THR   A CA    1 
ATOM   1016  C  C     . THR   A  1  158  ? -19.046 54.608  81.796  1.00 42.21 ? 156  THR   A C     1 
ATOM   1017  O  O     . THR   A  1  158  ? -19.227 55.150  80.701  1.00 45.53 ? 156  THR   A O     1 
ATOM   1018  C  CB    . THR   A  1  158  ? -17.421 52.794  81.177  1.00 40.02 ? 156  THR   A CB    1 
ATOM   1019  N  N     . SER   A  1  159  ? -19.097 55.265  82.959  1.00 31.15 ? 157  SER   A N     1 
ATOM   1020  C  CA    . SER   A  1  159  ? -19.608 56.633  83.032  1.00 26.83 ? 157  SER   A CA    1 
ATOM   1021  C  C     . SER   A  1  159  ? -18.735 57.623  82.262  1.00 28.14 ? 157  SER   A C     1 
ATOM   1022  O  O     . SER   A  1  159  ? -19.241 58.590  81.684  1.00 32.75 ? 157  SER   A O     1 
ATOM   1023  C  CB    . SER   A  1  159  ? -19.744 57.058  84.493  1.00 35.37 ? 157  SER   A CB    1 
ATOM   1024  O  OG    . SER   A  1  159  ? -18.547 56.793  85.205  1.00 37.26 ? 157  SER   A OG    1 
ATOM   1025  N  N     . THR   A  1  160  ? -17.427 57.423  82.265  1.00 25.12 ? 158  THR   A N     1 
ATOM   1026  C  CA    . THR   A  1  160  ? -16.528 58.283  81.515  1.00 22.41 ? 158  THR   A CA    1 
ATOM   1027  C  C     . THR   A  1  160  ? -15.801 57.447  80.479  1.00 21.61 ? 158  THR   A C     1 
ATOM   1028  O  O     . THR   A  1  160  ? -15.806 56.216  80.518  1.00 25.23 ? 158  THR   A O     1 
ATOM   1029  C  CB    . THR   A  1  160  ? -15.521 58.985  82.432  1.00 25.06 ? 158  THR   A CB    1 
ATOM   1030  O  OG1   . THR   A  1  160  ? -14.689 57.999  83.054  1.00 26.84 ? 158  THR   A OG1   1 
ATOM   1031  C  CG2   . THR   A  1  160  ? -16.233 59.809  83.490  1.00 30.47 ? 158  THR   A CG2   1 
ATOM   1032  N  N     . VAL   A  1  161  ? -15.157 58.150  79.558  1.00 17.69 ? 159  VAL   A N     1 
ATOM   1033  C  CA    . VAL   A  1  161  ? -14.617 57.574  78.337  1.00 17.64 ? 159  VAL   A CA    1 
ATOM   1034  C  C     . VAL   A  1  161  ? -13.104 57.620  78.444  1.00 16.71 ? 159  VAL   A C     1 
ATOM   1035  O  O     . VAL   A  1  161  ? -12.535 58.687  78.672  1.00 17.04 ? 159  VAL   A O     1 
ATOM   1036  C  CB    . VAL   A  1  161  ? -15.079 58.411  77.133  1.00 19.50 ? 159  VAL   A CB    1 
ATOM   1037  C  CG1   . VAL   A  1  161  ? -14.381 57.989  75.888  1.00 20.56 ? 159  VAL   A CG1   1 
ATOM   1038  C  CG2   . VAL   A  1  161  ? -16.620 58.356  77.000  1.00 22.66 ? 159  VAL   A CG2   1 
ATOM   1039  N  N     . ASN   A  1  162  ? -12.447 56.480  78.232  1.00 15.57 ? 160  ASN   A N     1 
ATOM   1040  C  CA    . ASN   A  1  162  ? -10.985 56.494  78.178  1.00 15.49 ? 160  ASN   A CA    1 
ATOM   1041  C  C     . ASN   A  1  162  ? -10.620 56.835  76.744  1.00 15.29 ? 160  ASN   A C     1 
ATOM   1042  O  O     . ASN   A  1  162  ? -10.427 55.962  75.893  1.00 15.95 ? 160  ASN   A O     1 
ATOM   1043  C  CB    . ASN   A  1  162  ? -10.383 55.182  78.648  1.00 16.42 ? 160  ASN   A CB    1 
ATOM   1044  C  CG    . ASN   A  1  162  ? -8.870  55.253  78.701  1.00 16.81 ? 160  ASN   A CG    1 
ATOM   1045  O  OD1   . ASN   A  1  162  ? -8.279  56.098  78.043  1.00 17.27 ? 160  ASN   A OD1   1 
ATOM   1046  N  ND2   . ASN   A  1  162  ? -8.249  54.380  79.471  1.00 22.22 ? 160  ASN   A ND2   1 
ATOM   1047  N  N     . ASP   A  1  163  ? -10.543 58.137  76.471  1.00 14.13 ? 161  ASP   A N     1 
ATOM   1048  C  CA    . ASP   A  1  163  ? -10.366 58.603  75.106  1.00 15.40 ? 161  ASP   A CA    1 
ATOM   1049  C  C     . ASP   A  1  163  ? -8.977  58.299  74.579  1.00 15.28 ? 161  ASP   A C     1 
ATOM   1050  O  O     . ASP   A  1  163  ? -8.794  58.140  73.382  1.00 16.52 ? 161  ASP   A O     1 
ATOM   1051  C  CB    . ASP   A  1  163  ? -10.728 60.088  74.956  1.00 17.91 ? 161  ASP   A CB    1 
ATOM   1052  C  CG    . ASP   A  1  163  ? -10.086 60.997  75.998  1.00 19.20 ? 161  ASP   A CG    1 
ATOM   1053  O  OD1   . ASP   A  1  163  ? -9.943  60.623  77.187  1.00 18.02 ? 161  ASP   A OD1   1 
ATOM   1054  O  OD2   . ASP   A  1  163  ? -9.757  62.138  75.602  1.00 20.88 ? 161  ASP   A OD2   1 
ATOM   1055  N  N     . ARG   A  1  164  ? -7.996  58.173  75.462  1.00 15.52 ? 162  ARG   A N     1 
ATOM   1056  C  CA    A ARG   A  1  164  ? -6.672  57.793  74.991  0.59 15.09 ? 162  ARG   A CA    1 
ATOM   1057  C  CA    B ARG   A  1  164  ? -6.669  57.792  75.000  0.41 15.15 ? 162  ARG   A CA    1 
ATOM   1058  C  C     . ARG   A  1  164  ? -6.633  56.326  74.588  1.00 13.90 ? 162  ARG   A C     1 
ATOM   1059  O  O     . ARG   A  1  164  ? -5.985  55.967  73.596  1.00 15.26 ? 162  ARG   A O     1 
ATOM   1060  C  CB    A ARG   A  1  164  ? -5.616  58.133  76.045  0.59 17.15 ? 162  ARG   A CB    1 
ATOM   1061  C  CB    B ARG   A  1  164  ? -5.638  58.108  76.083  0.41 17.13 ? 162  ARG   A CB    1 
ATOM   1062  C  CG    A ARG   A  1  164  ? -5.438  59.631  76.278  0.59 17.64 ? 162  ARG   A CG    1 
ATOM   1063  C  CG    B ARG   A  1  164  ? -5.582  59.585  76.434  0.41 17.93 ? 162  ARG   A CG    1 
ATOM   1064  C  CD    A ARG   A  1  164  ? -5.503  60.446  74.992  0.59 21.45 ? 162  ARG   A CD    1 
ATOM   1065  C  CD    B ARG   A  1  164  ? -4.578  60.363  75.585  0.41 20.61 ? 162  ARG   A CD    1 
ATOM   1066  N  NE    A ARG   A  1  164  ? -4.553  60.007  73.973  0.59 25.76 ? 162  ARG   A NE    1 
ATOM   1067  N  NE    B ARG   A  1  164  ? -4.843  60.304  74.153  0.41 25.06 ? 162  ARG   A NE    1 
ATOM   1068  C  CZ    A ARG   A  1  164  ? -4.658  60.306  72.684  0.59 26.04 ? 162  ARG   A CZ    1 
ATOM   1069  C  CZ    B ARG   A  1  164  ? -5.856  60.907  73.543  0.41 24.61 ? 162  ARG   A CZ    1 
ATOM   1070  N  NH1   A ARG   A  1  164  ? -5.647  61.057  72.227  0.59 28.26 ? 162  ARG   A NH1   1 
ATOM   1071  N  NH1   B ARG   A  1  164  ? -6.763  61.594  74.219  0.41 26.04 ? 162  ARG   A NH1   1 
ATOM   1072  N  NH2   A ARG   A  1  164  ? -3.755  59.832  71.831  0.59 23.60 ? 162  ARG   A NH2   1 
ATOM   1073  N  NH2   B ARG   A  1  164  ? -5.969  60.809  72.222  0.41 28.02 ? 162  ARG   A NH2   1 
ATOM   1074  N  N     . SER   A  1  165  ? -7.326  55.467  75.339  1.00 13.33 ? 163  SER   A N     1 
ATOM   1075  C  CA    . SER   A  1  165  ? -7.427  54.065  74.941  1.00 12.86 ? 163  SER   A CA    1 
ATOM   1076  C  C     . SER   A  1  165  ? -8.181  53.921  73.635  1.00 14.66 ? 163  SER   A C     1 
ATOM   1077  O  O     . SER   A  1  165  ? -7.790  53.132  72.768  1.00 14.62 ? 163  SER   A O     1 
ATOM   1078  C  CB    . SER   A  1  165  ? -8.131  53.276  76.045  1.00 15.44 ? 163  SER   A CB    1 
ATOM   1079  O  OG    . SER   A  1  165  ? -8.484  51.978  75.595  1.00 17.29 ? 163  SER   A OG    1 
ATOM   1080  N  N     . LEU   A  1  166  ? -9.272  54.672  73.482  1.00 14.79 ? 164  LEU   A N     1 
ATOM   1081  C  CA    . LEU   A  1  166  ? -10.033 54.609  72.245  1.00 14.57 ? 164  LEU   A CA    1 
ATOM   1082  C  C     . LEU   A  1  166  ? -9.231  55.151  71.073  1.00 14.34 ? 164  LEU   A C     1 
ATOM   1083  O  O     . LEU   A  1  166  ? -9.300  54.599  69.974  1.00 15.01 ? 164  LEU   A O     1 
ATOM   1084  C  CB    . LEU   A  1  166  ? -11.328 55.385  72.413  1.00 14.19 ? 164  LEU   A CB    1 
ATOM   1085  C  CG    . LEU   A  1  166  ? -12.276 54.679  73.375  1.00 14.22 ? 164  LEU   A CG    1 
ATOM   1086  C  CD1   . LEU   A  1  166  ? -13.444 55.566  73.669  1.00 16.55 ? 164  LEU   A CD1   1 
ATOM   1087  C  CD2   . LEU   A  1  166  ? -12.749 53.350  72.802  1.00 17.15 ? 164  LEU   A CD2   1 
ATOM   1088  N  N     . ALA   A  1  167  ? -8.479  56.237  71.277  1.00 14.34 ? 165  ALA   A N     1 
ATOM   1089  C  CA    . ALA   A  1  167  ? -7.683  56.757  70.174  1.00 15.54 ? 165  ALA   A CA    1 
ATOM   1090  C  C     . ALA   A  1  167  ? -6.635  55.740  69.745  1.00 16.55 ? 165  ALA   A C     1 
ATOM   1091  O  O     . ALA   A  1  167  ? -6.403  55.541  68.548  1.00 16.91 ? 165  ALA   A O     1 
ATOM   1092  C  CB    . ALA   A  1  167  ? -7.025  58.074  70.570  1.00 17.53 ? 165  ALA   A CB    1 
ATOM   1093  N  N     . ALA   A  1  168  ? -5.966  55.109  70.718  1.00 15.21 ? 166  ALA   A N     1 
ATOM   1094  C  CA    . ALA   A  1  168  ? -5.001  54.070  70.373  1.00 15.31 ? 166  ALA   A CA    1 
ATOM   1095  C  C     . ALA   A  1  168  ? -5.667  52.926  69.626  1.00 15.25 ? 166  ALA   A C     1 
ATOM   1096  O  O     . ALA   A  1  168  ? -5.131  52.426  68.624  1.00 15.82 ? 166  ALA   A O     1 
ATOM   1097  C  CB    . ALA   A  1  168  ? -4.347  53.558  71.659  1.00 15.72 ? 166  ALA   A CB    1 
ATOM   1098  N  N     . ALA   A  1  169  ? -6.844  52.506  70.094  1.00 15.10 ? 167  ALA   A N     1 
ATOM   1099  C  CA    . ALA   A  1  169  ? -7.547  51.406  69.459  1.00 14.10 ? 167  ALA   A CA    1 
ATOM   1100  C  C     . ALA   A  1  169  ? -7.977  51.751  68.041  1.00 15.17 ? 167  ALA   A C     1 
ATOM   1101  O  O     . ALA   A  1  169  ? -7.913  50.901  67.157  1.00 15.49 ? 167  ALA   A O     1 
ATOM   1102  C  CB    . ALA   A  1  169  ? -8.773  51.058  70.299  1.00 15.73 ? 167  ALA   A CB    1 
ATOM   1103  N  N     . LEU   A  1  170  ? -8.429  52.984  67.818  1.00 14.63 ? 168  LEU   A N     1 
ATOM   1104  C  CA    . LEU   A  1  170  ? -8.831  53.392  66.480  1.00 15.12 ? 168  LEU   A CA    1 
ATOM   1105  C  C     . LEU   A  1  170  ? -7.637  53.411  65.537  1.00 15.89 ? 168  LEU   A C     1 
ATOM   1106  O  O     . LEU   A  1  170  ? -7.713  52.895  64.420  1.00 16.28 ? 168  LEU   A O     1 
ATOM   1107  C  CB    . LEU   A  1  170  ? -9.500  54.763  66.555  1.00 17.39 ? 168  LEU   A CB    1 
ATOM   1108  C  CG    . LEU   A  1  170  ? -10.122 55.207  65.242  1.00 16.48 ? 168  LEU   A CG    1 
ATOM   1109  C  CD1   . LEU   A  1  170  ? -11.096 54.146  64.774  1.00 18.17 ? 168  LEU   A CD1   1 
ATOM   1110  C  CD2   . LEU   A  1  170  ? -10.815 56.510  65.479  1.00 17.67 ? 168  LEU   A CD2   1 
ATOM   1111  N  N     . THR   A  1  171  ? -6.522  53.997  65.977  1.00 16.28 ? 169  THR   A N     1 
ATOM   1112  C  CA    . THR   A  1  171  ? -5.321  53.963  65.155  1.00 17.14 ? 169  THR   A CA    1 
ATOM   1113  C  C     . THR   A  1  171  ? -4.934  52.525  64.837  1.00 16.45 ? 169  THR   A C     1 
ATOM   1114  O  O     . THR   A  1  171  ? -4.623  52.183  63.687  1.00 18.03 ? 169  THR   A O     1 
ATOM   1115  C  CB    . THR   A  1  171  ? -4.192  54.660  65.896  1.00 18.56 ? 169  THR   A CB    1 
ATOM   1116  O  OG1   . THR   A  1  171  ? -4.549  56.034  66.117  1.00 21.35 ? 169  THR   A OG1   1 
ATOM   1117  C  CG2   . THR   A  1  171  ? -2.872  54.565  65.143  1.00 19.47 ? 169  THR   A CG2   1 
ATOM   1118  N  N     . ARG   A  1  172  ? -4.986  51.660  65.848  1.00 16.45 ? 170  ARG   A N     1 
ATOM   1119  C  CA    . ARG   A  1  172  ? -4.571  50.279  65.653  1.00 16.80 ? 170  ARG   A CA    1 
ATOM   1120  C  C     . ARG   A  1  172  ? -5.470  49.575  64.656  1.00 17.47 ? 170  ARG   A C     1 
ATOM   1121  O  O     . ARG   A  1  172  ? -4.993  48.886  63.747  1.00 17.28 ? 170  ARG   A O     1 
ATOM   1122  C  CB    . ARG   A  1  172  ? -4.590  49.545  66.994  1.00 15.68 ? 170  ARG   A CB    1 
ATOM   1123  C  CG    . ARG   A  1  172  ? -3.846  48.212  66.940  1.00 16.18 ? 170  ARG   A CG    1 
ATOM   1124  C  CD    . ARG   A  1  172  ? -4.051  47.413  68.221  1.00 18.09 ? 170  ARG   A CD    1 
ATOM   1125  N  NE    . ARG   A  1  172  ? -3.781  48.209  69.411  1.00 15.66 ? 170  ARG   A NE    1 
ATOM   1126  C  CZ    . ARG   A  1  172  ? -4.718  48.668  70.232  1.00 16.17 ? 170  ARG   A CZ    1 
ATOM   1127  N  NH1   . ARG   A  1  172  ? -6.006  48.437  70.020  1.00 16.09 ? 170  ARG   A NH1   1 
ATOM   1128  N  NH2   . ARG   A  1  172  ? -4.352  49.390  71.284  1.00 16.21 ? 170  ARG   A NH2   1 
ATOM   1129  N  N     . LEU   A  1  173  ? -6.781  49.748  64.792  1.00 16.84 ? 171  LEU   A N     1 
ATOM   1130  C  CA    . LEU   A  1  173  ? -7.674  48.992  63.929  1.00 16.38 ? 171  LEU   A CA    1 
ATOM   1131  C  C     . LEU   A  1  173  ? -7.629  49.513  62.501  1.00 16.85 ? 171  LEU   A C     1 
ATOM   1132  O  O     . LEU   A  1  173  ? -7.720  48.733  61.550  1.00 18.51 ? 171  LEU   A O     1 
ATOM   1133  C  CB    . LEU   A  1  173  ? -9.093  48.975  64.492  1.00 18.19 ? 171  LEU   A CB    1 
ATOM   1134  C  CG    . LEU   A  1  173  ? -9.983  50.218  64.393  1.00 18.46 ? 171  LEU   A CG    1 
ATOM   1135  C  CD1   . LEU   A  1  173  ? -10.766 50.277  63.087  1.00 19.68 ? 171  LEU   A CD1   1 
ATOM   1136  C  CD2   . LEU   A  1  173  ? -10.971 50.254  65.556  1.00 17.94 ? 171  LEU   A CD2   1 
ATOM   1137  N  N     . ILE   A  1  174  ? -7.482  50.828  62.335  1.00 17.31 ? 172  ILE   A N     1 
ATOM   1138  C  CA    . ILE   A  1  174  ? -7.405  51.367  60.981  1.00 16.83 ? 172  ILE   A CA    1 
ATOM   1139  C  C     . ILE   A  1  174  ? -6.104  50.941  60.324  1.00 18.25 ? 172  ILE   A C     1 
ATOM   1140  O  O     . ILE   A  1  174  ? -6.089  50.537  59.159  1.00 18.74 ? 172  ILE   A O     1 
ATOM   1141  C  CB    . ILE   A  1  174  ? -7.555  52.896  60.987  1.00 17.90 ? 172  ILE   A CB    1 
ATOM   1142  C  CG1   . ILE   A  1  174  ? -8.975  53.314  61.369  1.00 19.67 ? 172  ILE   A CG1   1 
ATOM   1143  C  CG2   . ILE   A  1  174  ? -7.212  53.447  59.587  1.00 21.58 ? 172  ILE   A CG2   1 
ATOM   1144  C  CD1   . ILE   A  1  174  ? -9.104  54.795  61.597  1.00 21.32 ? 172  ILE   A CD1   1 
ATOM   1145  N  N     . SER   A  1  175  ? -5.000  50.994  61.065  1.00 18.81 ? 173  SER   A N     1 
ATOM   1146  C  CA    . SER   A  1  175  ? -3.726  50.595  60.481  1.00 17.06 ? 173  SER   A CA    1 
ATOM   1147  C  C     . SER   A  1  175  ? -3.692  49.108  60.193  1.00 19.97 ? 173  SER   A C     1 
ATOM   1148  O  O     . SER   A  1  175  ? -2.962  48.671  59.300  1.00 22.60 ? 173  SER   A O     1 
ATOM   1149  C  CB    . SER   A  1  175  ? -2.576  50.972  61.401  1.00 21.63 ? 173  SER   A CB    1 
ATOM   1150  O  OG    . SER   A  1  175  ? -2.466  52.376  61.523  1.00 24.11 ? 173  SER   A OG    1 
ATOM   1151  N  N     . ARG   A  1  176  ? -4.473  48.320  60.923  1.00 19.57 ? 174  ARG   A N     1 
ATOM   1152  C  CA    . ARG   A  1  176  ? -4.466  46.885  60.683  1.00 19.45 ? 174  ARG   A CA    1 
ATOM   1153  C  C     . ARG   A  1  176  ? -5.425  46.505  59.563  1.00 23.04 ? 174  ARG   A C     1 
ATOM   1154  O  O     . ARG   A  1  176  ? -5.088  45.673  58.717  1.00 23.95 ? 174  ARG   A O     1 
ATOM   1155  C  CB    . ARG   A  1  176  ? -4.822  46.168  61.988  1.00 22.65 ? 174  ARG   A CB    1 
ATOM   1156  C  CG    . ARG   A  1  176  ? -4.694  44.656  61.942  1.00 20.91 ? 174  ARG   A CG    1 
ATOM   1157  C  CD    . ARG   A  1  176  ? -4.952  44.069  63.343  1.00 22.01 ? 174  ARG   A CD    1 
ATOM   1158  N  NE    . ARG   A  1  176  ? -6.369  44.098  63.698  1.00 21.40 ? 174  ARG   A NE    1 
ATOM   1159  C  CZ    . ARG   A  1  176  ? -6.923  44.810  64.683  1.00 21.86 ? 174  ARG   A CZ    1 
ATOM   1160  N  NH1   . ARG   A  1  176  ? -6.195  45.550  65.521  1.00 19.99 ? 174  ARG   A NH1   1 
ATOM   1161  N  NH2   . ARG   A  1  176  ? -8.246  44.774  64.842  1.00 24.35 ? 174  ARG   A NH2   1 
ATOM   1162  N  N     . CYS   A  1  177  ? -6.613  47.116  59.520  1.00 22.01 ? 175  CYS   A N     1 
ATOM   1163  C  CA    . CYS   A  1  177  ? -7.684  46.648  58.657  1.00 23.02 ? 175  CYS   A CA    1 
ATOM   1164  C  C     . CYS   A  1  177  ? -8.135  47.644  57.599  1.00 23.84 ? 175  CYS   A C     1 
ATOM   1165  O  O     . CYS   A  1  177  ? -8.859  47.246  56.684  1.00 26.78 ? 175  CYS   A O     1 
ATOM   1166  C  CB    . CYS   A  1  177  ? -8.915  46.258  59.486  1.00 24.64 ? 175  CYS   A CB    1 
ATOM   1167  S  SG    . CYS   A  1  177  ? -8.544  45.057  60.795  1.00 27.40 ? 175  CYS   A SG    1 
ATOM   1168  N  N     . GLY   A  1  178  ? -7.771  48.913  57.717  1.00 23.48 ? 176  GLY   A N     1 
ATOM   1169  C  CA    . GLY   A  1  178  ? -7.976  49.847  56.623  1.00 22.61 ? 176  GLY   A CA    1 
ATOM   1170  C  C     . GLY   A  1  178  ? -9.428  50.189  56.312  1.00 20.84 ? 176  GLY   A C     1 
ATOM   1171  O  O     . GLY   A  1  178  ? -10.349 50.061  57.125  1.00 22.46 ? 176  GLY   A O     1 
ATOM   1172  N  N     . GLU   A  1  179  ? -9.611  50.631  55.071  1.00 22.09 ? 177  GLU   A N     1 
ATOM   1173  C  CA    . GLU   A  1  179  ? -10.926 51.065  54.614  1.00 22.54 ? 177  GLU   A CA    1 
ATOM   1174  C  C     . GLU   A  1  179  ? -12.025 50.029  54.810  1.00 20.38 ? 177  GLU   A C     1 
ATOM   1175  O  O     . GLU   A  1  179  ? -13.135 50.424  55.200  1.00 22.85 ? 177  GLU   A O     1 
ATOM   1176  C  CB    . GLU   A  1  179  ? -10.833 51.534  53.151  1.00 24.95 ? 177  GLU   A CB    1 
ATOM   1177  C  CG    . GLU   A  1  179  ? -12.113 52.193  52.623  1.00 32.52 ? 177  GLU   A CG    1 
ATOM   1178  C  CD    . GLU   A  1  179  ? -13.100 51.204  52.013  1.00 42.14 ? 177  GLU   A CD    1 
ATOM   1179  O  OE1   . GLU   A  1  179  ? -12.692 50.076  51.652  1.00 42.62 ? 177  GLU   A OE1   1 
ATOM   1180  O  OE2   . GLU   A  1  179  ? -14.296 51.560  51.892  1.00 46.37 ? 177  GLU   A OE2   1 
ATOM   1181  N  N     . PRO   A  1  180  ? -11.817 48.732  54.557  1.00 21.55 ? 178  PRO   A N     1 
ATOM   1182  C  CA    . PRO   A  1  180  ? -12.934 47.790  54.722  1.00 22.47 ? 178  PRO   A CA    1 
ATOM   1183  C  C     . PRO   A  1  180  ? -13.578 47.811  56.095  1.00 21.39 ? 178  PRO   A C     1 
ATOM   1184  O  O     . PRO   A  1  180  ? -14.807 47.721  56.191  1.00 21.84 ? 178  PRO   A O     1 
ATOM   1185  C  CB    . PRO   A  1  180  ? -12.304 46.436  54.389  1.00 24.79 ? 178  PRO   A CB    1 
ATOM   1186  C  CG    . PRO   A  1  180  ? -11.212 46.774  53.433  1.00 24.85 ? 178  PRO   A CG    1 
ATOM   1187  C  CD    . PRO   A  1  180  ? -10.655 48.084  53.917  1.00 22.36 ? 178  PRO   A CD    1 
ATOM   1188  N  N     . VAL   A  1  181  ? -12.797 47.953  57.166  1.00 21.05 ? 179  VAL   A N     1 
ATOM   1189  C  CA    . VAL   A  1  181  ? -13.428 47.966  58.475  1.00 20.37 ? 179  VAL   A CA    1 
ATOM   1190  C  C     . VAL   A  1  181  ? -14.153 49.280  58.709  1.00 19.70 ? 179  VAL   A C     1 
ATOM   1191  O  O     . VAL   A  1  181  ? -15.185 49.307  59.379  1.00 18.44 ? 179  VAL   A O     1 
ATOM   1192  C  CB    . VAL   A  1  181  ? -12.409 47.634  59.583  1.00 19.43 ? 179  VAL   A CB    1 
ATOM   1193  C  CG1   . VAL   A  1  181  ? -11.430 48.782  59.782  1.00 20.05 ? 179  VAL   A CG1   1 
ATOM   1194  C  CG2   . VAL   A  1  181  ? -13.146 47.303  60.867  1.00 23.35 ? 179  VAL   A CG2   1 
ATOM   1195  N  N     . ILE   A  1  182  ? -13.637 50.384  58.172  1.00 19.98 ? 180  ILE   A N     1 
ATOM   1196  C  CA    . ILE   A  1  182  ? -14.315 51.662  58.331  1.00 20.39 ? 180  ILE   A CA    1 
ATOM   1197  C  C     . ILE   A  1  182  ? -15.650 51.623  57.618  1.00 22.06 ? 180  ILE   A C     1 
ATOM   1198  O  O     . ILE   A  1  182  ? -16.679 52.033  58.162  1.00 21.19 ? 180  ILE   A O     1 
ATOM   1199  C  CB    . ILE   A  1  182  ? -13.438 52.806  57.801  1.00 20.58 ? 180  ILE   A CB    1 
ATOM   1200  C  CG1   . ILE   A  1  182  ? -12.098 52.836  58.533  1.00 21.21 ? 180  ILE   A CG1   1 
ATOM   1201  C  CG2   . ILE   A  1  182  ? -14.191 54.133  57.931  1.00 20.95 ? 180  ILE   A CG2   1 
ATOM   1202  C  CD1   . ILE   A  1  182  ? -11.080 53.715  57.842  1.00 25.00 ? 180  ILE   A CD1   1 
ATOM   1203  N  N     . ARG   A  1  183  ? -15.640 51.115  56.389  1.00 21.02 ? 181  ARG   A N     1 
ATOM   1204  C  CA    A ARG   A  1  183  ? -16.871 50.981  55.620  0.40 22.73 ? 181  ARG   A CA    1 
ATOM   1205  C  CA    B ARG   A  1  183  ? -16.864 50.965  55.611  0.60 22.69 ? 181  ARG   A CA    1 
ATOM   1206  C  C     . ARG   A  1  183  ? -17.904 50.148  56.369  1.00 23.47 ? 181  ARG   A C     1 
ATOM   1207  O  O     . ARG   A  1  183  ? -19.086 50.519  56.435  1.00 23.37 ? 181  ARG   A O     1 
ATOM   1208  C  CB    A ARG   A  1  183  ? -16.552 50.362  54.261  0.40 23.34 ? 181  ARG   A CB    1 
ATOM   1209  C  CB    B ARG   A  1  183  ? -16.508 50.277  54.294  0.60 23.24 ? 181  ARG   A CB    1 
ATOM   1210  C  CG    A ARG   A  1  183  ? -17.768 49.996  53.417  0.40 29.20 ? 181  ARG   A CG    1 
ATOM   1211  C  CG    B ARG   A  1  183  ? -17.670 49.991  53.349  0.60 29.29 ? 181  ARG   A CG    1 
ATOM   1212  C  CD    A ARG   A  1  183  ? -18.728 51.169  53.267  0.40 30.85 ? 181  ARG   A CD    1 
ATOM   1213  C  CD    B ARG   A  1  183  ? -18.112 51.246  52.611  0.60 32.71 ? 181  ARG   A CD    1 
ATOM   1214  N  NE    A ARG   A  1  183  ? -18.050 52.397  52.866  0.40 28.32 ? 181  ARG   A NE    1 
ATOM   1215  N  NE    B ARG   A  1  183  ? -19.120 51.987  53.360  0.60 28.36 ? 181  ARG   A NE    1 
ATOM   1216  C  CZ    A ARG   A  1  183  ? -18.570 53.609  52.999  0.40 32.18 ? 181  ARG   A CZ    1 
ATOM   1217  C  CZ    B ARG   A  1  183  ? -19.294 53.299  53.284  0.60 31.84 ? 181  ARG   A CZ    1 
ATOM   1218  N  NH1   A ARG   A  1  183  ? -19.763 53.793  53.542  0.40 28.78 ? 181  ARG   A NH1   1 
ATOM   1219  N  NH1   B ARG   A  1  183  ? -18.501 54.060  52.547  0.60 33.91 ? 181  ARG   A NH1   1 
ATOM   1220  N  NH2   A ARG   A  1  183  ? -17.874 54.663  52.582  0.40 33.20 ? 181  ARG   A NH2   1 
ATOM   1221  N  NH2   B ARG   A  1  183  ? -20.281 53.862  53.972  0.60 27.82 ? 181  ARG   A NH2   1 
ATOM   1222  N  N     . ARG   A  1  184  ? -17.485 49.016  56.936  1.00 22.38 ? 182  ARG   A N     1 
ATOM   1223  C  CA    . ARG   A  1  184  ? -18.434 48.182  57.666  1.00 24.10 ? 182  ARG   A CA    1 
ATOM   1224  C  C     . ARG   A  1  184  ? -18.948 48.898  58.903  1.00 23.26 ? 182  ARG   A C     1 
ATOM   1225  O  O     . ARG   A  1  184  ? -20.127 48.781  59.256  1.00 23.73 ? 182  ARG   A O     1 
ATOM   1226  C  CB    . ARG   A  1  184  ? -17.787 46.857  58.051  1.00 23.95 ? 182  ARG   A CB    1 
ATOM   1227  C  CG    . ARG   A  1  184  ? -17.666 45.897  56.894  1.00 30.42 ? 182  ARG   A CG    1 
ATOM   1228  C  CD    . ARG   A  1  184  ? -18.885 44.988  56.814  1.00 30.80 ? 182  ARG   A CD    1 
ATOM   1229  N  NE    . ARG   A  1  184  ? -18.740 43.837  57.694  1.00 33.52 ? 182  ARG   A NE    1 
ATOM   1230  C  CZ    . ARG   A  1  184  ? -19.547 43.542  58.703  1.00 33.34 ? 182  ARG   A CZ    1 
ATOM   1231  N  NH1   . ARG   A  1  184  ? -20.595 44.297  58.997  1.00 33.63 ? 182  ARG   A NH1   1 
ATOM   1232  N  NH2   . ARG   A  1  184  ? -19.304 42.452  59.426  1.00 31.40 ? 182  ARG   A NH2   1 
ATOM   1233  N  N     . GLY   A  1  185  ? -18.072 49.632  59.588  1.00 21.44 ? 183  GLY   A N     1 
ATOM   1234  C  CA    . GLY   A  1  185  ? -18.518 50.370  60.757  1.00 19.82 ? 183  GLY   A CA    1 
ATOM   1235  C  C     . GLY   A  1  185  ? -19.523 51.450  60.401  1.00 20.43 ? 183  GLY   A C     1 
ATOM   1236  O  O     . GLY   A  1  185  ? -20.537 51.617  61.077  1.00 20.21 ? 183  GLY   A O     1 
ATOM   1237  N  N     . VAL   A  1  186  ? -19.247 52.198  59.330  1.00 19.97 ? 184  VAL   A N     1 
ATOM   1238  C  CA    . VAL   A  1  186  ? -20.164 53.250  58.893  1.00 22.01 ? 184  VAL   A CA    1 
ATOM   1239  C  C     . VAL   A  1  186  ? -21.521 52.664  58.549  1.00 21.86 ? 184  VAL   A C     1 
ATOM   1240  O  O     . VAL   A  1  186  ? -22.567 53.184  58.963  1.00 21.05 ? 184  VAL   A O     1 
ATOM   1241  C  CB    . VAL   A  1  186  ? -19.561 54.013  57.702  1.00 22.15 ? 184  VAL   A CB    1 
ATOM   1242  C  CG1   . VAL   A  1  186  ? -20.645 54.851  56.988  1.00 23.46 ? 184  VAL   A CG1   1 
ATOM   1243  C  CG2   . VAL   A  1  186  ? -18.424 54.880  58.181  1.00 22.03 ? 184  VAL   A CG2   1 
ATOM   1244  N  N     . ASP   A  1  187  ? -21.526 51.566  57.800  1.00 21.10 ? 185  ASP   A N     1 
ATOM   1245  C  CA    . ASP   A  1  187  ? -22.792 50.975  57.387  1.00 24.87 ? 185  ASP   A CA    1 
ATOM   1246  C  C     . ASP   A  1  187  ? -23.554 50.432  58.584  1.00 26.37 ? 185  ASP   A C     1 
ATOM   1247  O  O     . ASP   A  1  187  ? -24.783 50.552  58.651  1.00 25.58 ? 185  ASP   A O     1 
ATOM   1248  C  CB    . ASP   A  1  187  ? -22.546 49.887  56.350  1.00 25.02 ? 185  ASP   A CB    1 
ATOM   1249  C  CG    . ASP   A  1  187  ? -22.054 50.448  55.021  1.00 27.34 ? 185  ASP   A CG    1 
ATOM   1250  O  OD1   . ASP   A  1  187  ? -22.130 51.684  54.826  1.00 34.05 ? 185  ASP   A OD1   1 
ATOM   1251  O  OD2   . ASP   A  1  187  ? -21.585 49.661  54.181  1.00 31.51 ? 185  ASP   A OD2   1 
ATOM   1252  N  N     . MET   A  1  188  ? -22.841 49.843  59.543  1.00 24.18 ? 186  MET   A N     1 
ATOM   1253  C  CA    . MET   A  1  188  ? -23.485 49.351  60.756  1.00 23.53 ? 186  MET   A CA    1 
ATOM   1254  C  C     . MET   A  1  188  ? -24.077 50.494  61.563  1.00 25.47 ? 186  MET   A C     1 
ATOM   1255  O  O     . MET   A  1  188  ? -25.235 50.430  62.003  1.00 23.18 ? 186  MET   A O     1 
ATOM   1256  C  CB    . MET   A  1  188  ? -22.461 48.587  61.593  1.00 25.69 ? 186  MET   A CB    1 
ATOM   1257  C  CG    . MET   A  1  188  ? -23.023 47.973  62.857  1.00 31.47 ? 186  MET   A CG    1 
ATOM   1258  S  SD    . MET   A  1  188  ? -24.221 46.694  62.450  1.00 41.73 ? 186  MET   A SD    1 
ATOM   1259  C  CE    . MET   A  1  188  ? -23.189 45.645  61.413  1.00 36.47 ? 186  MET   A CE    1 
ATOM   1260  N  N     . ALA   A  1  189  ? -23.289 51.548  61.782  1.00 21.88 ? 187  ALA   A N     1 
ATOM   1261  C  CA    . ALA   A  1  189  ? -23.773 52.681  62.556  1.00 22.23 ? 187  ALA   A CA    1 
ATOM   1262  C  C     . ALA   A  1  189  ? -24.959 53.335  61.871  1.00 21.96 ? 187  ALA   A C     1 
ATOM   1263  O  O     . ALA   A  1  189  ? -25.913 53.753  62.533  1.00 21.94 ? 187  ALA   A O     1 
ATOM   1264  C  CB    . ALA   A  1  189  ? -22.653 53.695  62.781  1.00 24.48 ? 187  ALA   A CB    1 
ATOM   1265  N  N     . MET   A  1  190  ? -24.921 53.426  60.543  1.00 22.15 ? 188  MET   A N     1 
ATOM   1266  C  CA    . MET   A  1  190  ? -26.022 54.042  59.810  1.00 24.16 ? 188  MET   A CA    1 
ATOM   1267  C  C     . MET   A  1  190  ? -27.309 53.261  60.018  1.00 25.34 ? 188  MET   A C     1 
ATOM   1268  O  O     . MET   A  1  190  ? -28.370 53.839  60.285  1.00 25.98 ? 188  MET   A O     1 
ATOM   1269  C  CB    . MET   A  1  190  ? -25.670 54.085  58.329  1.00 25.56 ? 188  MET   A CB    1 
ATOM   1270  C  CG    . MET   A  1  190  ? -26.628 54.901  57.498  1.00 30.75 ? 188  MET   A CG    1 
ATOM   1271  S  SD    . MET   A  1  190  ? -26.201 54.785  55.748  1.00 36.63 ? 188  MET   A SD    1 
ATOM   1272  C  CE    . MET   A  1  190  ? -24.433 55.084  55.805  1.00 29.88 ? 188  MET   A CE    1 
ATOM   1273  N  N     . ARG   A  1  191  ? -27.228 51.939  59.903  1.00 22.03 ? 189  ARG   A N     1 
ATOM   1274  C  CA    . ARG   A  1  191  ? -28.388 51.087  60.137  1.00 26.72 ? 189  ARG   A CA    1 
ATOM   1275  C  C     . ARG   A  1  191  ? -28.883 51.206  61.572  1.00 26.59 ? 189  ARG   A C     1 
ATOM   1276  O  O     . ARG   A  1  191  ? -30.088 51.324  61.817  1.00 26.45 ? 189  ARG   A O     1 
ATOM   1277  C  CB    . ARG   A  1  191  ? -28.018 49.639  59.825  1.00 26.51 ? 189  ARG   A CB    1 
ATOM   1278  C  CG    . ARG   A  1  191  ? -29.186 48.664  59.852  1.00 33.34 ? 189  ARG   A CG    1 
ATOM   1279  C  CD    . ARG   A  1  191  ? -28.780 47.319  59.265  1.00 43.99 ? 189  ARG   A CD    1 
ATOM   1280  N  NE    . ARG   A  1  191  ? -27.887 46.582  60.152  1.00 53.86 ? 189  ARG   A NE    1 
ATOM   1281  C  CZ    . ARG   A  1  191  ? -28.263 45.563  60.914  1.00 58.34 ? 189  ARG   A CZ    1 
ATOM   1282  N  NH1   . ARG   A  1  191  ? -29.506 45.108  60.897  1.00 58.78 ? 189  ARG   A NH1   1 
ATOM   1283  N  NH2   . ARG   A  1  191  ? -27.369 44.985  61.712  1.00 54.93 ? 189  ARG   A NH2   1 
ATOM   1284  N  N     . MET   A  1  192  ? -27.973 51.153  62.543  1.00 21.92 ? 190  MET   A N     1 
ATOM   1285  C  CA    . MET   A  1  192  ? -28.413 51.172  63.934  1.00 23.27 ? 190  MET   A CA    1 
ATOM   1286  C  C     . MET   A  1  192  ? -29.060 52.498  64.288  1.00 25.34 ? 190  MET   A C     1 
ATOM   1287  O  O     . MET   A  1  192  ? -30.137 52.535  64.891  1.00 23.39 ? 190  MET   A O     1 
ATOM   1288  C  CB    . MET   A  1  192  ? -27.229 50.898  64.856  1.00 25.41 ? 190  MET   A CB    1 
ATOM   1289  C  CG    . MET   A  1  192  ? -26.738 49.484  64.769  1.00 23.56 ? 190  MET   A CG    1 
ATOM   1290  S  SD    . MET   A  1  192  ? -25.370 49.231  65.904  1.00 35.72 ? 190  MET   A SD    1 
ATOM   1291  C  CE    . MET   A  1  192  ? -26.292 48.908  67.391  1.00 34.81 ? 190  MET   A CE    1 
ATOM   1292  N  N     . MET   A  1  193  ? -28.420 53.602  63.923  1.00 21.64 ? 191  MET   A N     1 
ATOM   1293  C  CA    A MET   A  1  193  ? -28.919 54.921  64.288  0.58 23.90 ? 191  MET   A CA    1 
ATOM   1294  C  CA    B MET   A  1  193  ? -28.946 54.902  64.307  0.42 23.93 ? 191  MET   A CA    1 
ATOM   1295  C  C     . MET   A  1  193  ? -30.105 55.363  63.438  1.00 25.05 ? 191  MET   A C     1 
ATOM   1296  O  O     . MET   A  1  193  ? -30.861 56.239  63.865  1.00 28.57 ? 191  MET   A O     1 
ATOM   1297  C  CB    A MET   A  1  193  ? -27.797 55.957  64.180  0.58 25.07 ? 191  MET   A CB    1 
ATOM   1298  C  CB    B MET   A  1  193  ? -27.837 55.949  64.311  0.42 25.13 ? 191  MET   A CB    1 
ATOM   1299  C  CG    A MET   A  1  193  ? -26.507 55.572  64.908  0.58 23.54 ? 191  MET   A CG    1 
ATOM   1300  C  CG    B MET   A  1  193  ? -26.873 55.774  65.462  0.42 24.14 ? 191  MET   A CG    1 
ATOM   1301  S  SD    A MET   A  1  193  ? -25.211 56.829  64.774  0.58 26.06 ? 191  MET   A SD    1 
ATOM   1302  S  SD    B MET   A  1  193  ? -25.813 57.206  65.666  0.42 26.37 ? 191  MET   A SD    1 
ATOM   1303  C  CE    A MET   A  1  193  ? -25.790 58.023  65.979  0.58 29.67 ? 191  MET   A CE    1 
ATOM   1304  C  CE    B MET   A  1  193  ? -24.845 57.126  64.155  0.42 26.96 ? 191  MET   A CE    1 
ATOM   1305  N  N     . GLY   A  1  194  ? -30.278 54.788  62.259  1.00 24.48 ? 192  GLY   A N     1 
ATOM   1306  C  CA    . GLY   A  1  194  ? -31.348 55.216  61.382  1.00 26.70 ? 192  GLY   A CA    1 
ATOM   1307  C  C     . GLY   A  1  194  ? -32.537 54.283  61.358  1.00 28.25 ? 192  GLY   A C     1 
ATOM   1308  O  O     . GLY   A  1  194  ? -33.641 54.700  60.990  1.00 29.35 ? 192  GLY   A O     1 
ATOM   1309  N  N     . GLU   A  1  195  ? -32.335 53.022  61.749  1.00 23.68 ? 193  GLU   A N     1 
ATOM   1310  C  CA    . GLU   A  1  195  ? -33.367 52.003  61.615  1.00 23.04 ? 193  GLU   A CA    1 
ATOM   1311  C  C     . GLU   A  1  195  ? -33.620 51.172  62.859  1.00 23.81 ? 193  GLU   A C     1 
ATOM   1312  O  O     . GLU   A  1  195  ? -34.685 50.551  62.939  1.00 23.04 ? 193  GLU   A O     1 
ATOM   1313  C  CB    . GLU   A  1  195  ? -33.041 51.034  60.470  1.00 27.23 ? 193  GLU   A CB    1 
ATOM   1314  C  CG    . GLU   A  1  195  ? -32.614 51.692  59.185  1.00 34.56 ? 193  GLU   A CG    1 
ATOM   1315  C  CD    . GLU   A  1  195  ? -32.110 50.675  58.190  1.00 44.94 ? 193  GLU   A CD    1 
ATOM   1316  O  OE1   . GLU   A  1  195  ? -32.552 49.507  58.268  1.00 47.28 ? 193  GLU   A OE1   1 
ATOM   1317  O  OE2   . GLU   A  1  195  ? -31.266 51.034  57.344  1.00 52.90 ? 193  GLU   A OE2   1 
ATOM   1318  N  N     . GLN   A  1  196  ? -32.692 51.110  63.815  1.00 24.58 ? 194  GLN   A N     1 
ATOM   1319  C  CA    A GLN   A  1  196  ? -32.868 50.303  65.014  0.49 25.09 ? 194  GLN   A CA    1 
ATOM   1320  C  CA    B GLN   A  1  196  ? -32.865 50.302  65.018  0.51 25.09 ? 194  GLN   A CA    1 
ATOM   1321  C  C     . GLN   A  1  196  ? -33.169 51.131  66.255  1.00 25.57 ? 194  GLN   A C     1 
ATOM   1322  O  O     . GLN   A  1  196  ? -34.164 50.877  66.946  1.00 27.10 ? 194  GLN   A O     1 
ATOM   1323  C  CB    A GLN   A  1  196  ? -31.628 49.422  65.229  0.49 27.37 ? 194  GLN   A CB    1 
ATOM   1324  C  CB    B GLN   A  1  196  ? -31.635 49.422  65.290  0.51 27.37 ? 194  GLN   A CB    1 
ATOM   1325  C  CG    A GLN   A  1  196  ? -31.304 48.574  64.006  0.49 28.20 ? 194  GLN   A CG    1 
ATOM   1326  C  CG    B GLN   A  1  196  ? -31.768 48.629  66.587  0.51 30.54 ? 194  GLN   A CG    1 
ATOM   1327  C  CD    A GLN   A  1  196  ? -29.991 47.822  64.121  0.49 30.08 ? 194  GLN   A CD    1 
ATOM   1328  C  CD    B GLN   A  1  196  ? -30.503 47.902  66.981  0.51 29.42 ? 194  GLN   A CD    1 
ATOM   1329  O  OE1   A GLN   A  1  196  ? -29.388 47.452  63.114  0.49 31.31 ? 194  GLN   A OE1   1 
ATOM   1330  O  OE1   B GLN   A  1  196  ? -29.702 47.523  66.133  0.51 31.21 ? 194  GLN   A OE1   1 
ATOM   1331  N  NE2   A GLN   A  1  196  ? -29.549 47.583  65.348  0.49 32.45 ? 194  GLN   A NE2   1 
ATOM   1332  N  NE2   B GLN   A  1  196  ? -30.315 47.706  68.282  0.51 30.36 ? 194  GLN   A NE2   1 
ATOM   1333  N  N     . PHE   A  1  197  ? -32.333 52.116  66.565  1.00 23.39 ? 195  PHE   A N     1 
ATOM   1334  C  CA    . PHE   A  1  197  ? -32.576 52.957  67.728  1.00 24.33 ? 195  PHE   A CA    1 
ATOM   1335  C  C     . PHE   A  1  197  ? -33.740 53.899  67.493  1.00 24.71 ? 195  PHE   A C     1 
ATOM   1336  O  O     . PHE   A  1  197  ? -34.304 54.420  68.460  1.00 25.51 ? 195  PHE   A O     1 
ATOM   1337  C  CB    . PHE   A  1  197  ? -31.339 53.791  68.048  1.00 25.34 ? 195  PHE   A CB    1 
ATOM   1338  C  CG    . PHE   A  1  197  ? -30.124 52.979  68.379  1.00 29.43 ? 195  PHE   A CG    1 
ATOM   1339  C  CD1   . PHE   A  1  197  ? -30.235 51.771  69.043  1.00 35.01 ? 195  PHE   A CD1   1 
ATOM   1340  C  CD2   . PHE   A  1  197  ? -28.865 53.438  68.031  1.00 26.97 ? 195  PHE   A CD2   1 
ATOM   1341  C  CE1   . PHE   A  1  197  ? -29.105 51.029  69.353  1.00 34.17 ? 195  PHE   A CE1   1 
ATOM   1342  C  CE2   . PHE   A  1  197  ? -27.736 52.701  68.341  1.00 30.68 ? 195  PHE   A CE2   1 
ATOM   1343  C  CZ    . PHE   A  1  197  ? -27.868 51.496  69.004  1.00 29.98 ? 195  PHE   A CZ    1 
ATOM   1344  N  N     . VAL   A  1  198  ? -34.065 54.161  66.230  1.00 21.93 ? 196  VAL   A N     1 
ATOM   1345  C  CA    . VAL   A  1  198  ? -35.258 54.901  65.844  1.00 21.10 ? 196  VAL   A CA    1 
ATOM   1346  C  C     . VAL   A  1  198  ? -35.949 54.131  64.739  1.00 21.72 ? 196  VAL   A C     1 
ATOM   1347  O  O     . VAL   A  1  198  ? -35.324 53.366  63.998  1.00 25.46 ? 196  VAL   A O     1 
ATOM   1348  C  CB    . VAL   A  1  198  ? -34.972 56.360  65.394  1.00 20.64 ? 196  VAL   A CB    1 
ATOM   1349  C  CG1   . VAL   A  1  198  ? -34.339 57.166  66.524  1.00 22.02 ? 196  VAL   A CG1   1 
ATOM   1350  C  CG2   . VAL   A  1  198  ? -34.094 56.387  64.159  1.00 22.42 ? 196  VAL   A CG2   1 
ATOM   1351  N  N     . THR   A  1  199  ? -37.260 54.327  64.643  1.00 20.00 ? 197  THR   A N     1 
ATOM   1352  C  CA    . THR   A  1  199  ? -37.992 53.804  63.503  1.00 22.50 ? 197  THR   A CA    1 
ATOM   1353  C  C     . THR   A  1  199  ? -37.673 54.615  62.262  1.00 22.80 ? 197  THR   A C     1 
ATOM   1354  O  O     . THR   A  1  199  ? -37.632 54.071  61.156  1.00 27.84 ? 197  THR   A O     1 
ATOM   1355  C  CB    . THR   A  1  199  ? -39.487 53.825  63.823  1.00 22.23 ? 197  THR   A CB    1 
ATOM   1356  O  OG1   . THR   A  1  199  ? -39.695 53.120  65.057  1.00 23.95 ? 197  THR   A OG1   1 
ATOM   1357  C  CG2   . THR   A  1  199  ? -40.290 53.162  62.721  1.00 26.99 ? 197  THR   A CG2   1 
ATOM   1358  N  N     . GLY   A  1  200  ? -37.423 55.902  62.430  1.00 21.22 ? 198  GLY   A N     1 
ATOM   1359  C  CA    . GLY   A  1  200  ? -36.996 56.732  61.320  1.00 22.37 ? 198  GLY   A CA    1 
ATOM   1360  C  C     . GLY   A  1  200  ? -36.493 58.047  61.861  1.00 20.29 ? 198  GLY   A C     1 
ATOM   1361  O  O     . GLY   A  1  200  ? -36.715 58.391  63.023  1.00 19.88 ? 198  GLY   A O     1 
ATOM   1362  N  N     . GLU   A  1  201  ? -35.809 58.785  60.991  1.00 21.26 ? 199  GLU   A N     1 
ATOM   1363  C  CA    . GLU   A  1  201  ? -35.254 60.069  61.397  1.00 21.01 ? 199  GLU   A CA    1 
ATOM   1364  C  C     . GLU   A  1  201  ? -36.330 61.137  61.496  1.00 22.52 ? 199  GLU   A C     1 
ATOM   1365  O  O     . GLU   A  1  201  ? -36.199 62.082  62.279  1.00 24.67 ? 199  GLU   A O     1 
ATOM   1366  C  CB    . GLU   A  1  201  ? -34.189 60.493  60.385  1.00 26.13 ? 199  GLU   A CB    1 
ATOM   1367  C  CG    . GLU   A  1  201  ? -33.507 61.806  60.682  1.00 34.70 ? 199  GLU   A CG    1 
ATOM   1368  C  CD    . GLU   A  1  201  ? -32.412 62.108  59.678  1.00 47.53 ? 199  GLU   A CD    1 
ATOM   1369  O  OE1   . GLU   A  1  201  ? -32.435 61.508  58.582  1.00 49.17 ? 199  GLU   A OE1   1 
ATOM   1370  O  OE2   . GLU   A  1  201  ? -31.525 62.933  59.988  1.00 53.06 ? 199  GLU   A OE2   1 
ATOM   1371  N  N     . THR   A  1  202  ? -37.388 61.007  60.710  1.00 20.73 ? 200  THR   A N     1 
ATOM   1372  C  CA    . THR   A  1  202  ? -38.492 61.945  60.714  1.00 19.22 ? 200  THR   A CA    1 
ATOM   1373  C  C     . THR   A  1  202  ? -39.784 61.158  60.794  1.00 18.68 ? 200  THR   A C     1 
ATOM   1374  O  O     . THR   A  1  202  ? -39.826 59.957  60.523  1.00 19.21 ? 200  THR   A O     1 
ATOM   1375  C  CB    . THR   A  1  202  ? -38.547 62.716  59.402  1.00 22.18 ? 200  THR   A CB    1 
ATOM   1376  O  OG1   . THR   A  1  202  ? -38.784 61.781  58.345  1.00 24.37 ? 200  THR   A OG1   1 
ATOM   1377  C  CG2   . THR   A  1  202  ? -37.227 63.456  59.142  1.00 24.50 ? 200  THR   A CG2   1 
ATOM   1378  N  N     . ILE   A  1  203  ? -40.853 61.853  61.165  1.00 18.74 ? 201  ILE   A N     1 
ATOM   1379  C  CA    . ILE   A  1  203  ? -42.129 61.158  61.303  1.00 18.55 ? 201  ILE   A CA    1 
ATOM   1380  C  C     . ILE   A  1  203  ? -42.565 60.555  59.970  1.00 20.42 ? 201  ILE   A C     1 
ATOM   1381  O  O     . ILE   A  1  203  ? -43.083 59.438  59.928  1.00 19.47 ? 201  ILE   A O     1 
ATOM   1382  C  CB    . ILE   A  1  203  ? -43.196 62.056  61.961  1.00 19.93 ? 201  ILE   A CB    1 
ATOM   1383  C  CG1   . ILE   A  1  203  ? -44.444 61.241  62.316  1.00 17.78 ? 201  ILE   A CG1   1 
ATOM   1384  C  CG2   . ILE   A  1  203  ? -43.548 63.249  61.073  1.00 21.61 ? 201  ILE   A CG2   1 
ATOM   1385  C  CD1   . ILE   A  1  203  ? -44.193 60.065  63.229  1.00 18.81 ? 201  ILE   A CD1   1 
ATOM   1386  N  N     . ARG   A  1  204  ? -42.297 61.243  58.857  1.00 19.29 ? 202  ARG   A N     1 
ATOM   1387  C  CA    . ARG   A  1  204  ? -42.680 60.688  57.562  1.00 19.92 ? 202  ARG   A CA    1 
ATOM   1388  C  C     . ARG   A  1  204  ? -41.934 59.398  57.255  1.00 19.26 ? 202  ARG   A C     1 
ATOM   1389  O  O     . ARG   A  1  204  ? -42.528 58.437  56.759  1.00 21.19 ? 202  ARG   A O     1 
ATOM   1390  C  CB    . ARG   A  1  204  ? -42.465 61.717  56.456  1.00 25.83 ? 202  ARG   A CB    1 
ATOM   1391  C  CG    . ARG   A  1  204  ? -43.612 62.691  56.343  1.00 32.71 ? 202  ARG   A CG    1 
ATOM   1392  C  CD    . ARG   A  1  204  ? -43.203 63.954  55.603  1.00 35.81 ? 202  ARG   A CD    1 
ATOM   1393  N  NE    . ARG   A  1  204  ? -44.316 64.893  55.535  1.00 34.62 ? 202  ARG   A NE    1 
ATOM   1394  C  CZ    . ARG   A  1  204  ? -44.761 65.597  56.566  1.00 34.39 ? 202  ARG   A CZ    1 
ATOM   1395  N  NH1   . ARG   A  1  204  ? -44.200 65.503  57.764  1.00 27.31 ? 202  ARG   A NH1   1 
ATOM   1396  N  NH2   . ARG   A  1  204  ? -45.797 66.415  56.391  1.00 29.98 ? 202  ARG   A NH2   1 
ATOM   1397  N  N     . GLU   A  1  205  ? -40.628 59.365  57.524  1.00 21.00 ? 203  GLU   A N     1 
ATOM   1398  C  CA    . GLU   A  1  205  ? -39.863 58.138  57.330  1.00 22.84 ? 203  GLU   A CA    1 
ATOM   1399  C  C     . GLU   A  1  205  ? -40.359 57.032  58.247  1.00 21.28 ? 203  GLU   A C     1 
ATOM   1400  O  O     . GLU   A  1  205  ? -40.520 55.884  57.821  1.00 21.03 ? 203  GLU   A O     1 
ATOM   1401  C  CB    . GLU   A  1  205  ? -38.385 58.405  57.590  1.00 23.34 ? 203  GLU   A CB    1 
ATOM   1402  C  CG    . GLU   A  1  205  ? -37.480 57.249  57.237  1.00 27.54 ? 203  GLU   A CG    1 
ATOM   1403  C  CD    . GLU   A  1  205  ? -36.020 57.633  57.338  1.00 35.78 ? 203  GLU   A CD    1 
ATOM   1404  O  OE1   . GLU   A  1  205  ? -35.527 57.786  58.475  1.00 30.74 ? 203  GLU   A OE1   1 
ATOM   1405  O  OE2   . GLU   A  1  205  ? -35.372 57.801  56.281  1.00 38.95 ? 203  GLU   A OE2   1 
ATOM   1406  N  N     . ALA   A  1  206  ? -40.634 57.370  59.507  1.00 19.17 ? 204  ALA   A N     1 
ATOM   1407  C  CA    . ALA   A  1  206  ? -41.126 56.379  60.453  1.00 19.65 ? 204  ALA   A CA    1 
ATOM   1408  C  C     . ALA   A  1  206  ? -42.460 55.811  59.999  1.00 19.29 ? 204  ALA   A C     1 
ATOM   1409  O  O     . ALA   A  1  206  ? -42.685 54.598  60.082  1.00 21.70 ? 204  ALA   A O     1 
ATOM   1410  C  CB    . ALA   A  1  206  ? -41.263 57.019  61.835  1.00 19.22 ? 204  ALA   A CB    1 
ATOM   1411  N  N     . LEU   A  1  207  ? -43.353 56.674  59.510  1.00 19.29 ? 205  LEU   A N     1 
ATOM   1412  C  CA    . LEU   A  1  207  ? -44.652 56.208  59.042  1.00 19.34 ? 205  LEU   A CA    1 
ATOM   1413  C  C     . LEU   A  1  207  ? -44.515 55.293  57.834  1.00 22.54 ? 205  LEU   A C     1 
ATOM   1414  O  O     . LEU   A  1  207  ? -45.222 54.283  57.732  1.00 21.91 ? 205  LEU   A O     1 
ATOM   1415  C  CB    . LEU   A  1  207  ? -45.547 57.396  58.714  1.00 20.69 ? 205  LEU   A CB    1 
ATOM   1416  C  CG    . LEU   A  1  207  ? -46.053 58.153  59.930  1.00 19.41 ? 205  LEU   A CG    1 
ATOM   1417  C  CD1   . LEU   A  1  207  ? -46.627 59.488  59.488  1.00 20.21 ? 205  LEU   A CD1   1 
ATOM   1418  C  CD2   . LEU   A  1  207  ? -47.108 57.319  60.658  1.00 20.19 ? 205  LEU   A CD2   1 
ATOM   1419  N  N     . LYS   A  1  208  ? -43.611 55.627  56.910  1.00 21.66 ? 206  LYS   A N     1 
ATOM   1420  C  CA    . LYS   A  1  208  ? -43.396 54.760  55.757  1.00 24.16 ? 206  LYS   A CA    1 
ATOM   1421  C  C     . LYS   A  1  208  ? -42.916 53.383  56.190  1.00 24.97 ? 206  LYS   A C     1 
ATOM   1422  O  O     . LYS   A  1  208  ? -43.372 52.363  55.656  1.00 27.98 ? 206  LYS   A O     1 
ATOM   1423  C  CB    . LYS   A  1  208  ? -42.383 55.402  54.808  1.00 26.25 ? 206  LYS   A CB    1 
ATOM   1424  N  N     . ARG   A  1  209  ? -42.029 53.331  57.181  1.00 23.09 ? 207  ARG   A N     1 
ATOM   1425  C  CA    . ARG   A  1  209  ? -41.475 52.073  57.655  1.00 24.20 ? 207  ARG   A CA    1 
ATOM   1426  C  C     . ARG   A  1  209  ? -42.440 51.283  58.523  1.00 26.36 ? 207  ARG   A C     1 
ATOM   1427  O  O     . ARG   A  1  209  ? -42.161 50.122  58.824  1.00 28.84 ? 207  ARG   A O     1 
ATOM   1428  C  CB    . ARG   A  1  209  ? -40.175 52.333  58.400  1.00 24.44 ? 207  ARG   A CB    1 
ATOM   1429  C  CG    . ARG   A  1  209  ? -39.090 52.785  57.453  1.00 27.25 ? 207  ARG   A CG    1 
ATOM   1430  C  CD    . ARG   A  1  209  ? -37.889 53.233  58.200  1.00 27.70 ? 207  ARG   A CD    1 
ATOM   1431  N  NE    . ARG   A  1  209  ? -36.863 53.757  57.312  1.00 31.37 ? 207  ARG   A NE    1 
ATOM   1432  C  CZ    . ARG   A  1  209  ? -35.721 54.264  57.747  1.00 35.54 ? 207  ARG   A CZ    1 
ATOM   1433  N  NH1   . ARG   A  1  209  ? -35.453 54.342  59.039  1.00 28.33 ? 207  ARG   A NH1   1 
ATOM   1434  N  NH2   . ARG   A  1  209  ? -34.828 54.705  56.865  1.00 39.82 ? 207  ARG   A NH2   1 
ATOM   1435  N  N     . SER   A  1  210  ? -43.561 51.871  58.922  1.00 24.70 ? 208  SER   A N     1 
ATOM   1436  C  CA    . SER   A  1  210  ? -44.497 51.191  59.804  1.00 22.80 ? 208  SER   A CA    1 
ATOM   1437  C  C     . SER   A  1  210  ? -45.488 50.310  59.061  1.00 25.18 ? 208  SER   A C     1 
ATOM   1438  O  O     . SER   A  1  210  ? -46.125 49.462  59.690  1.00 24.36 ? 208  SER   A O     1 
ATOM   1439  C  CB    . SER   A  1  210  ? -45.260 52.219  60.642  1.00 23.76 ? 208  SER   A CB    1 
ATOM   1440  O  OG    . SER   A  1  210  ? -44.359 52.907  61.495  1.00 24.30 ? 208  SER   A OG    1 
ATOM   1441  N  N     . LYS   A  1  211  ? -45.622 50.479  57.745  1.00 25.46 ? 209  LYS   A N     1 
ATOM   1442  C  CA    . LYS   A  1  211  ? -46.667 49.768  57.016  1.00 25.32 ? 209  LYS   A CA    1 
ATOM   1443  C  C     . LYS   A  1  211  ? -46.472 48.257  57.091  1.00 25.42 ? 209  LYS   A C     1 
ATOM   1444  O  O     . LYS   A  1  211  ? -47.447 47.506  57.220  1.00 27.61 ? 209  LYS   A O     1 
ATOM   1445  C  CB    . LYS   A  1  211  ? -46.702 50.247  55.564  1.00 30.60 ? 209  LYS   A CB    1 
ATOM   1446  N  N     . GLU   A  1  212  ? -45.219 47.801  57.047  1.00 26.79 ? 210  GLU   A N     1 
ATOM   1447  C  CA    . GLU   A  1  212  ? -44.933 46.368  57.013  1.00 30.64 ? 210  GLU   A CA    1 
ATOM   1448  C  C     . GLU   A  1  212  ? -45.508 45.649  58.230  1.00 30.43 ? 210  GLU   A C     1 
ATOM   1449  O  O     . GLU   A  1  212  ? -46.216 44.647  58.092  1.00 31.08 ? 210  GLU   A O     1 
ATOM   1450  C  CB    . GLU   A  1  212  ? -43.427 46.141  56.910  1.00 33.87 ? 210  GLU   A CB    1 
ATOM   1451  C  CG    . GLU   A  1  212  ? -43.042 44.676  56.840  1.00 43.17 ? 210  GLU   A CG    1 
ATOM   1452  C  CD    . GLU   A  1  212  ? -41.546 44.466  56.893  1.00 53.98 ? 210  GLU   A CD    1 
ATOM   1453  O  OE1   . GLU   A  1  212  ? -40.800 45.415  56.572  1.00 59.08 ? 210  GLU   A OE1   1 
ATOM   1454  O  OE2   . GLU   A  1  212  ? -41.116 43.352  57.262  1.00 58.53 ? 210  GLU   A OE2   1 
ATOM   1455  N  N     . LEU   A  1  213  ? -45.225 46.147  59.435  1.00 27.82 ? 211  LEU   A N     1 
ATOM   1456  C  CA    . LEU   A  1  213  ? -45.738 45.468  60.621  1.00 25.98 ? 211  LEU   A CA    1 
ATOM   1457  C  C     . LEU   A  1  213  ? -47.201 45.794  60.895  1.00 25.39 ? 211  LEU   A C     1 
ATOM   1458  O  O     . LEU   A  1  213  ? -47.916 44.965  61.473  1.00 25.13 ? 211  LEU   A O     1 
ATOM   1459  C  CB    . LEU   A  1  213  ? -44.862 45.749  61.838  1.00 23.37 ? 211  LEU   A CB    1 
ATOM   1460  C  CG    . LEU   A  1  213  ? -43.476 45.092  61.766  1.00 26.40 ? 211  LEU   A CG    1 
ATOM   1461  C  CD1   . LEU   A  1  213  ? -42.659 45.352  63.022  1.00 27.53 ? 211  LEU   A CD1   1 
ATOM   1462  C  CD2   . LEU   A  1  213  ? -43.591 43.593  61.500  1.00 32.73 ? 211  LEU   A CD2   1 
ATOM   1463  N  N     . GLU   A  1  214  ? -47.685 46.965  60.477  1.00 23.40 ? 212  GLU   A N     1 
ATOM   1464  C  CA    . GLU   A  1  214  ? -49.117 47.218  60.602  1.00 23.75 ? 212  GLU   A CA    1 
ATOM   1465  C  C     . GLU   A  1  214  ? -49.923 46.194  59.814  1.00 27.37 ? 212  GLU   A C     1 
ATOM   1466  O  O     . GLU   A  1  214  ? -50.979 45.745  60.271  1.00 26.95 ? 212  GLU   A O     1 
ATOM   1467  C  CB    . GLU   A  1  214  ? -49.464 48.638  60.169  1.00 23.40 ? 212  GLU   A CB    1 
ATOM   1468  C  CG    . GLU   A  1  214  ? -49.013 49.669  61.185  1.00 22.93 ? 212  GLU   A CG    1 
ATOM   1469  C  CD    . GLU   A  1  214  ? -49.409 51.068  60.802  1.00 26.34 ? 212  GLU   A CD    1 
ATOM   1470  O  OE1   . GLU   A  1  214  ? -49.698 51.307  59.610  1.00 27.63 ? 212  GLU   A OE1   1 
ATOM   1471  O  OE2   . GLU   A  1  214  ? -49.434 51.934  61.698  1.00 27.70 ? 212  GLU   A OE2   1 
ATOM   1472  N  N     . GLU   A  1  215  ? -49.426 45.798  58.637  1.00 26.68 ? 213  GLU   A N     1 
ATOM   1473  C  CA    . GLU   A  1  215  ? -50.115 44.802  57.826  1.00 30.91 ? 213  GLU   A CA    1 
ATOM   1474  C  C     . GLU   A  1  215  ? -50.154 43.442  58.507  1.00 32.70 ? 213  GLU   A C     1 
ATOM   1475  O  O     . GLU   A  1  215  ? -51.027 42.625  58.190  1.00 35.93 ? 213  GLU   A O     1 
ATOM   1476  C  CB    . GLU   A  1  215  ? -49.446 44.686  56.454  1.00 33.57 ? 213  GLU   A CB    1 
ATOM   1477  N  N     . LYS   A  1  216  ? -49.246 43.193  59.443  1.00 31.34 ? 214  LYS   A N     1 
ATOM   1478  C  CA    . LYS   A  1  216  ? -49.211 41.952  60.200  1.00 31.98 ? 214  LYS   A CA    1 
ATOM   1479  C  C     . LYS   A  1  216  ? -50.039 42.009  61.479  1.00 32.98 ? 214  LYS   A C     1 
ATOM   1480  O  O     . LYS   A  1  216  ? -50.212 40.976  62.133  1.00 40.18 ? 214  LYS   A O     1 
ATOM   1481  C  CB    . LYS   A  1  216  ? -47.762 41.571  60.522  1.00 30.56 ? 214  LYS   A CB    1 
ATOM   1482  N  N     . GLY   A  1  217  ? -50.570 43.175  61.840  1.00 28.00 ? 215  GLY   A N     1 
ATOM   1483  C  CA    . GLY   A  1  217  ? -51.400 43.320  63.020  1.00 28.18 ? 215  GLY   A CA    1 
ATOM   1484  C  C     . GLY   A  1  217  ? -50.780 44.132  64.134  1.00 25.33 ? 215  GLY   A C     1 
ATOM   1485  O  O     . GLY   A  1  217  ? -51.388 44.246  65.205  1.00 26.66 ? 215  GLY   A O     1 
ATOM   1486  N  N     . PHE   A  1  218  ? -49.588 44.679  63.936  1.00 23.26 ? 216  PHE   A N     1 
ATOM   1487  C  CA    . PHE   A  1  218  ? -49.044 45.598  64.917  1.00 19.66 ? 216  PHE   A CA    1 
ATOM   1488  C  C     . PHE   A  1  218  ? -49.645 46.978  64.719  1.00 21.57 ? 216  PHE   A C     1 
ATOM   1489  O  O     . PHE   A  1  218  ? -50.197 47.307  63.665  1.00 21.57 ? 216  PHE   A O     1 
ATOM   1490  C  CB    . PHE   A  1  218  ? -47.529 45.725  64.764  1.00 21.37 ? 216  PHE   A CB    1 
ATOM   1491  C  CG    . PHE   A  1  218  ? -46.762 44.508  65.202  1.00 21.68 ? 216  PHE   A CG    1 
ATOM   1492  C  CD1   . PHE   A  1  218  ? -46.610 43.424  64.346  1.00 24.69 ? 216  PHE   A CD1   1 
ATOM   1493  C  CD2   . PHE   A  1  218  ? -46.162 44.462  66.443  1.00 21.86 ? 216  PHE   A CD2   1 
ATOM   1494  C  CE1   . PHE   A  1  218  ? -45.898 42.310  64.738  1.00 25.34 ? 216  PHE   A CE1   1 
ATOM   1495  C  CE2   . PHE   A  1  218  ? -45.444 43.347  66.841  1.00 24.10 ? 216  PHE   A CE2   1 
ATOM   1496  C  CZ    . PHE   A  1  218  ? -45.313 42.272  65.985  1.00 22.18 ? 216  PHE   A CZ    1 
ATOM   1497  N  N     . SER   A  1  219  ? -49.537 47.792  65.759  1.00 20.92 ? 217  SER   A N     1 
ATOM   1498  C  CA    . SER   A  1  219  ? -49.813 49.210  65.663  1.00 19.23 ? 217  SER   A CA    1 
ATOM   1499  C  C     . SER   A  1  219  ? -48.594 49.948  66.183  1.00 17.85 ? 217  SER   A C     1 
ATOM   1500  O  O     . SER   A  1  219  ? -47.615 49.334  66.605  1.00 16.98 ? 217  SER   A O     1 
ATOM   1501  C  CB    . SER   A  1  219  ? -51.063 49.601  66.454  1.00 20.10 ? 217  SER   A CB    1 
ATOM   1502  O  OG    . SER   A  1  219  ? -50.911 49.231  67.811  1.00 21.28 ? 217  SER   A OG    1 
ATOM   1503  N  N     . TYR   A  1  220  ? -48.670 51.278  66.170  1.00 16.60 ? 218  TYR   A N     1 
ATOM   1504  C  CA    . TYR   A  1  220  ? -47.532 52.111  66.525  1.00 16.58 ? 218  TYR   A CA    1 
ATOM   1505  C  C     . TYR   A  1  220  ? -47.947 53.249  67.440  1.00 16.89 ? 218  TYR   A C     1 
ATOM   1506  O  O     . TYR   A  1  220  ? -49.065 53.768  67.357  1.00 16.71 ? 218  TYR   A O     1 
ATOM   1507  C  CB    . TYR   A  1  220  ? -46.894 52.712  65.266  1.00 17.90 ? 218  TYR   A CB    1 
ATOM   1508  C  CG    . TYR   A  1  220  ? -45.981 51.744  64.592  1.00 17.26 ? 218  TYR   A CG    1 
ATOM   1509  C  CD1   . TYR   A  1  220  ? -46.476 50.775  63.721  1.00 21.19 ? 218  TYR   A CD1   1 
ATOM   1510  C  CD2   . TYR   A  1  220  ? -44.625 51.780  64.838  1.00 18.59 ? 218  TYR   A CD2   1 
ATOM   1511  C  CE1   . TYR   A  1  220  ? -45.629 49.869  63.117  1.00 20.02 ? 218  TYR   A CE1   1 
ATOM   1512  C  CE2   . TYR   A  1  220  ? -43.772 50.885  64.233  1.00 19.54 ? 218  TYR   A CE2   1 
ATOM   1513  C  CZ    . TYR   A  1  220  ? -44.279 49.937  63.381  1.00 21.22 ? 218  TYR   A CZ    1 
ATOM   1514  O  OH    . TYR   A  1  220  ? -43.410 49.048  62.801  1.00 21.34 ? 218  TYR   A OH    1 
ATOM   1515  N  N     . SER   A  1  221  ? -47.017 53.638  68.307  1.00 16.94 ? 219  SER   A N     1 
ATOM   1516  C  CA    . SER   A  1  221  ? -47.095 54.893  69.039  1.00 16.98 ? 219  SER   A CA    1 
ATOM   1517  C  C     . SER   A  1  221  ? -45.763 55.591  68.842  1.00 16.22 ? 219  SER   A C     1 
ATOM   1518  O  O     . SER   A  1  221  ? -44.722 55.055  69.231  1.00 19.59 ? 219  SER   A O     1 
ATOM   1519  C  CB    . SER   A  1  221  ? -47.326 54.659  70.532  1.00 18.30 ? 219  SER   A CB    1 
ATOM   1520  O  OG    . SER   A  1  221  ? -47.416 55.910  71.205  1.00 19.30 ? 219  SER   A OG    1 
ATOM   1521  N  N     . TYR   A  1  222  ? -45.786 56.778  68.271  1.00 14.45 ? 220  TYR   A N     1 
ATOM   1522  C  CA    . TYR   A  1  222  ? -44.534 57.436  67.911  1.00 15.68 ? 220  TYR   A CA    1 
ATOM   1523  C  C     . TYR   A  1  222  ? -44.051 58.351  69.020  1.00 18.90 ? 220  TYR   A C     1 
ATOM   1524  O  O     . TYR   A  1  222  ? -44.824 59.129  69.581  1.00 17.75 ? 220  TYR   A O     1 
ATOM   1525  C  CB    . TYR   A  1  222  ? -44.686 58.207  66.601  1.00 17.51 ? 220  TYR   A CB    1 
ATOM   1526  C  CG    . TYR   A  1  222  ? -45.004 57.271  65.481  1.00 16.48 ? 220  TYR   A CG    1 
ATOM   1527  C  CD1   . TYR   A  1  222  ? -44.010 56.516  64.867  1.00 16.47 ? 220  TYR   A CD1   1 
ATOM   1528  C  CD2   . TYR   A  1  222  ? -46.304 57.105  65.063  1.00 15.03 ? 220  TYR   A CD2   1 
ATOM   1529  C  CE1   . TYR   A  1  222  ? -44.324 55.627  63.861  1.00 17.48 ? 220  TYR   A CE1   1 
ATOM   1530  C  CE2   . TYR   A  1  222  ? -46.621 56.223  64.058  1.00 17.57 ? 220  TYR   A CE2   1 
ATOM   1531  C  CZ    . TYR   A  1  222  ? -45.634 55.491  63.467  1.00 17.38 ? 220  TYR   A CZ    1 
ATOM   1532  O  OH    . TYR   A  1  222  ? -45.967 54.615  62.465  1.00 19.47 ? 220  TYR   A OH    1 
ATOM   1533  N  N     . ASP   A  1  223  ? -42.760 58.271  69.301  1.00 19.04 ? 221  ASP   A N     1 
ATOM   1534  C  CA    . ASP   A  1  223  ? -42.096 59.078  70.314  1.00 23.29 ? 221  ASP   A CA    1 
ATOM   1535  C  C     . ASP   A  1  223  ? -41.121 60.008  69.608  1.00 22.44 ? 221  ASP   A C     1 
ATOM   1536  O  O     . ASP   A  1  223  ? -40.090 59.555  69.093  1.00 21.09 ? 221  ASP   A O     1 
ATOM   1537  C  CB    . ASP   A  1  223  ? -41.332 58.146  71.235  1.00 24.02 ? 221  ASP   A CB    1 
ATOM   1538  C  CG    . ASP   A  1  223  ? -40.395 58.884  72.179  1.00 27.18 ? 221  ASP   A CG    1 
ATOM   1539  O  OD1   . ASP   A  1  223  ? -40.631 60.076  72.470  1.00 28.13 ? 221  ASP   A OD1   1 
ATOM   1540  O  OD2   . ASP   A  1  223  ? -39.427 58.248  72.629  1.00 36.55 ? 221  ASP   A OD2   1 
ATOM   1541  N  N     . MET   A  1  224  ? -41.429 61.299  69.602  1.00 22.52 ? 222  MET   A N     1 
ATOM   1542  C  CA    . MET   A  1  224  ? -40.562 62.292  68.983  1.00 23.34 ? 222  MET   A CA    1 
ATOM   1543  C  C     . MET   A  1  224  ? -39.328 62.614  69.833  1.00 23.92 ? 222  MET   A C     1 
ATOM   1544  O  O     . MET   A  1  224  ? -38.557 63.501  69.463  1.00 31.01 ? 222  MET   A O     1 
ATOM   1545  C  CB    . MET   A  1  224  ? -41.355 63.556  68.620  1.00 23.40 ? 222  MET   A CB    1 
ATOM   1546  C  CG    . MET   A  1  224  ? -42.540 63.312  67.665  1.00 24.47 ? 222  MET   A CG    1 
ATOM   1547  S  SD    . MET   A  1  224  ? -42.101 62.471  66.126  1.00 30.68 ? 222  MET   A SD    1 
ATOM   1548  C  CE    . MET   A  1  224  ? -40.914 63.613  65.446  1.00 35.90 ? 222  MET   A CE    1 
ATOM   1549  N  N     . LEU   A  1  225  ? -39.130 61.910  70.942  1.00 29.53 ? 223  LEU   A N     1 
ATOM   1550  C  CA    . LEU   A  1  225  ? -37.892 61.911  71.715  1.00 28.74 ? 223  LEU   A CA    1 
ATOM   1551  C  C     . LEU   A  1  225  ? -37.641 63.212  72.471  1.00 35.25 ? 223  LEU   A C     1 
ATOM   1552  O  O     . LEU   A  1  225  ? -36.552 63.392  73.026  1.00 37.53 ? 223  LEU   A O     1 
ATOM   1553  C  CB    . LEU   A  1  225  ? -36.670 61.488  70.881  1.00 31.85 ? 223  LEU   A CB    1 
ATOM   1554  C  CG    . LEU   A  1  225  ? -36.540 60.009  70.484  1.00 25.66 ? 223  LEU   A CG    1 
ATOM   1555  C  CD1   . LEU   A  1  225  ? -35.380 59.815  69.510  1.00 32.28 ? 223  LEU   A CD1   1 
ATOM   1556  C  CD2   . LEU   A  1  225  ? -36.352 59.115  71.704  1.00 31.24 ? 223  LEU   A CD2   1 
ATOM   1557  N  N     . GLY   A  1  226  ? -38.615 64.116  72.523  1.00 30.51 ? 224  GLY   A N     1 
ATOM   1558  C  CA    . GLY   A  1  226  ? -38.461 65.307  73.333  1.00 33.77 ? 224  GLY   A CA    1 
ATOM   1559  C  C     . GLY   A  1  226  ? -38.611 64.996  74.808  1.00 28.11 ? 224  GLY   A C     1 
ATOM   1560  O  O     . GLY   A  1  226  ? -39.382 64.128  75.212  1.00 26.02 ? 224  GLY   A O     1 
ATOM   1561  N  N     . GLU   A  1  227  ? -37.860 65.726  75.627  1.00 26.47 ? 225  GLU   A N     1 
ATOM   1562  C  CA    . GLU   A  1  227  ? -37.853 65.436  77.049  1.00 24.50 ? 225  GLU   A CA    1 
ATOM   1563  C  C     . GLU   A  1  227  ? -37.051 66.519  77.742  1.00 23.13 ? 225  GLU   A C     1 
ATOM   1564  O  O     . GLU   A  1  227  ? -36.086 67.037  77.174  1.00 21.86 ? 225  GLU   A O     1 
ATOM   1565  C  CB    . GLU   A  1  227  ? -37.192 64.071  77.261  1.00 27.28 ? 225  GLU   A CB    1 
ATOM   1566  C  CG    . GLU   A  1  227  ? -37.033 63.588  78.658  1.00 34.54 ? 225  GLU   A CG    1 
ATOM   1567  C  CD    . GLU   A  1  227  ? -36.402 62.209  78.664  1.00 41.47 ? 225  GLU   A CD    1 
ATOM   1568  O  OE1   . GLU   A  1  227  ? -36.425 61.551  77.597  1.00 32.25 ? 225  GLU   A OE1   1 
ATOM   1569  O  OE2   . GLU   A  1  227  ? -35.871 61.792  79.710  1.00 42.51 ? 225  GLU   A OE2   1 
ATOM   1570  N  N     . ALA   A  1  228  ? -37.472 66.869  78.954  1.00 20.02 ? 226  ALA   A N     1 
ATOM   1571  C  CA    . ALA   A  1  228  ? -36.709 67.741  79.838  1.00 22.07 ? 226  ALA   A CA    1 
ATOM   1572  C  C     . ALA   A  1  228  ? -36.302 69.041  79.135  1.00 18.00 ? 226  ALA   A C     1 
ATOM   1573  O  O     . ALA   A  1  228  ? -35.119 69.365  78.991  1.00 22.14 ? 226  ALA   A O     1 
ATOM   1574  C  CB    . ALA   A  1  228  ? -35.498 67.000  80.409  1.00 25.62 ? 226  ALA   A CB    1 
ATOM   1575  N  N     . ALA   A  1  229  ? -37.310 69.797  78.712  1.00 17.88 ? 227  ALA   A N     1 
ATOM   1576  C  CA    . ALA   A  1  229  ? -37.069 71.144  78.217  1.00 16.55 ? 227  ALA   A CA    1 
ATOM   1577  C  C     . ALA   A  1  229  ? -36.323 71.956  79.264  1.00 18.06 ? 227  ALA   A C     1 
ATOM   1578  O  O     . ALA   A  1  229  ? -36.677 71.954  80.447  1.00 17.78 ? 227  ALA   A O     1 
ATOM   1579  C  CB    . ALA   A  1  229  ? -38.396 71.828  77.919  1.00 17.23 ? 227  ALA   A CB    1 
ATOM   1580  N  N     . THR   A  1  230  ? -35.296 72.658  78.810  1.00 17.98 ? 228  THR   A N     1 
ATOM   1581  C  CA    . THR   A  1  230  ? -34.518 73.530  79.680  1.00 18.46 ? 228  THR   A CA    1 
ATOM   1582  C  C     . THR   A  1  230  ? -34.930 74.987  79.560  1.00 17.40 ? 228  THR   A C     1 
ATOM   1583  O  O     . THR   A  1  230  ? -34.772 75.757  80.512  1.00 17.68 ? 228  THR   A O     1 
ATOM   1584  C  CB    . THR   A  1  230  ? -33.034 73.383  79.317  1.00 20.67 ? 228  THR   A CB    1 
ATOM   1585  O  OG1   . THR   A  1  230  ? -32.669 71.998  79.413  1.00 26.79 ? 228  THR   A OG1   1 
ATOM   1586  C  CG2   . THR   A  1  230  ? -32.155 74.171  80.261  1.00 23.57 ? 228  THR   A CG2   1 
ATOM   1587  N  N     . THR   A  1  231  ? -35.494 75.378  78.422  1.00 17.11 ? 229  THR   A N     1 
ATOM   1588  C  CA    . THR   A  1  231  ? -35.845 76.759  78.143  1.00 15.67 ? 229  THR   A CA    1 
ATOM   1589  C  C     . THR   A  1  231  ? -37.242 76.788  77.546  1.00 17.19 ? 229  THR   A C     1 
ATOM   1590  O  O     . THR   A  1  231  ? -37.764 75.766  77.083  1.00 15.94 ? 229  THR   A O     1 
ATOM   1591  C  CB    . THR   A  1  231  ? -34.885 77.391  77.124  1.00 17.15 ? 229  THR   A CB    1 
ATOM   1592  O  OG1   . THR   A  1  231  ? -35.116 76.789  75.846  1.00 18.86 ? 229  THR   A OG1   1 
ATOM   1593  C  CG2   . THR   A  1  231  ? -33.413 77.191  77.523  1.00 18.07 ? 229  THR   A CG2   1 
ATOM   1594  N  N     . ALA   A  1  232  ? -37.838 77.977  77.579  1.00 17.42 ? 230  ALA   A N     1 
ATOM   1595  C  CA    . ALA   A  1  232  ? -39.101 78.189  76.880  1.00 17.51 ? 230  ALA   A CA    1 
ATOM   1596  C  C     . ALA   A  1  232  ? -38.975 77.810  75.413  1.00 19.56 ? 230  ALA   A C     1 
ATOM   1597  O  O     . ALA   A  1  232  ? -39.879 77.179  74.848  1.00 18.77 ? 230  ALA   A O     1 
ATOM   1598  C  CB    . ALA   A  1  232  ? -39.521 79.646  77.015  1.00 18.23 ? 230  ALA   A CB    1 
ATOM   1599  N  N     . ALA   A  1  233  ? -37.856 78.162  74.778  1.00 18.65 ? 231  ALA   A N     1 
ATOM   1600  C  CA    . ALA   A  1  233  ? -37.697 77.840  73.361  1.00 22.11 ? 231  ALA   A CA    1 
ATOM   1601  C  C     . ALA   A  1  233  ? -37.661 76.338  73.126  1.00 19.41 ? 231  ALA   A C     1 
ATOM   1602  O  O     . ALA   A  1  233  ? -38.215 75.852  72.129  1.00 22.45 ? 231  ALA   A O     1 
ATOM   1603  C  CB    . ALA   A  1  233  ? -36.452 78.510  72.780  1.00 23.96 ? 231  ALA   A CB    1 
ATOM   1604  N  N     . ASP   A  1  234  ? -37.020 75.583  74.022  1.00 18.88 ? 232  ASP   A N     1 
ATOM   1605  C  CA    . ASP   A  1  234  ? -37.020 74.127  73.905  1.00 20.27 ? 232  ASP   A CA    1 
ATOM   1606  C  C     . ASP   A  1  234  ? -38.435 73.600  73.963  1.00 20.09 ? 232  ASP   A C     1 
ATOM   1607  O  O     . ASP   A  1  234  ? -38.814 72.703  73.205  1.00 20.17 ? 232  ASP   A O     1 
ATOM   1608  C  CB    . ASP   A  1  234  ? -36.320 73.484  75.097  1.00 24.26 ? 232  ASP   A CB    1 
ATOM   1609  C  CG    . ASP   A  1  234  ? -34.832 73.579  75.051  1.00 33.07 ? 232  ASP   A CG    1 
ATOM   1610  O  OD1   . ASP   A  1  234  ? -34.246 73.858  73.984  1.00 30.19 ? 232  ASP   A OD1   1 
ATOM   1611  O  OD2   . ASP   A  1  234  ? -34.248 73.326  76.128  1.00 26.74 ? 232  ASP   A OD2   1 
ATOM   1612  N  N     . ALA   A  1  235  ? -39.206 74.085  74.934  1.00 18.62 ? 233  ALA   A N     1 
ATOM   1613  C  CA    . ALA   A  1  235  ? -40.562 73.596  75.107  1.00 17.95 ? 233  ALA   A CA    1 
ATOM   1614  C  C     . ALA   A  1  235  ? -41.401 73.923  73.885  1.00 20.08 ? 233  ALA   A C     1 
ATOM   1615  O  O     . ALA   A  1  235  ? -42.248 73.123  73.469  1.00 17.68 ? 233  ALA   A O     1 
ATOM   1616  C  CB    . ALA   A  1  235  ? -41.170 74.215  76.363  1.00 18.84 ? 233  ALA   A CB    1 
ATOM   1617  N  N     . GLU   A  1  236  ? -41.183 75.100  73.297  1.00 18.45 ? 234  GLU   A N     1 
ATOM   1618  C  CA    . GLU   A  1  236  ? -41.907 75.452  72.081  1.00 17.34 ? 234  GLU   A CA    1 
ATOM   1619  C  C     . GLU   A  1  236  ? -41.504 74.547  70.931  1.00 18.91 ? 234  GLU   A C     1 
ATOM   1620  O  O     . GLU   A  1  236  ? -42.352 74.130  70.135  1.00 18.69 ? 234  GLU   A O     1 
ATOM   1621  C  CB    . GLU   A  1  236  ? -41.607 76.900  71.715  1.00 23.05 ? 234  GLU   A CB    1 
ATOM   1622  C  CG    . GLU   A  1  236  ? -42.217 77.909  72.633  1.00 27.91 ? 234  GLU   A CG    1 
ATOM   1623  C  CD    . GLU   A  1  236  ? -41.467 79.230  72.620  1.00 39.72 ? 234  GLU   A CD    1 
ATOM   1624  O  OE1   . GLU   A  1  236  ? -40.583 79.404  71.751  1.00 45.17 ? 234  GLU   A OE1   1 
ATOM   1625  O  OE2   . GLU   A  1  236  ? -41.756 80.091  73.478  1.00 45.07 ? 234  GLU   A OE2   1 
ATOM   1626  N  N     . ARG   A  1  237  ? -40.212 74.257  70.813  1.00 19.46 ? 235  ARG   A N     1 
ATOM   1627  C  CA    . ARG   A  1  237  ? -39.741 73.353  69.772  1.00 19.55 ? 235  ARG   A CA    1 
ATOM   1628  C  C     . ARG   A  1  237  ? -40.357 71.971  69.931  1.00 21.92 ? 235  ARG   A C     1 
ATOM   1629  O  O     . ARG   A  1  237  ? -40.816 71.366  68.958  1.00 19.10 ? 235  ARG   A O     1 
ATOM   1630  C  CB    . ARG   A  1  237  ? -38.209 73.284  69.772  1.00 22.16 ? 235  ARG   A CB    1 
ATOM   1631  C  CG    . ARG   A  1  237  ? -37.637 72.244  68.807  1.00 29.91 ? 235  ARG   A CG    1 
ATOM   1632  C  CD    . ARG   A  1  237  ? -36.124 72.391  68.654  1.00 36.25 ? 235  ARG   A CD    1 
ATOM   1633  N  NE    . ARG   A  1  237  ? -35.458 72.384  69.951  1.00 40.35 ? 235  ARG   A NE    1 
ATOM   1634  C  CZ    . ARG   A  1  237  ? -35.002 71.294  70.554  1.00 44.26 ? 235  ARG   A CZ    1 
ATOM   1635  N  NH1   . ARG   A  1  237  ? -35.089 70.101  69.987  1.00 45.33 ? 235  ARG   A NH1   1 
ATOM   1636  N  NH2   . ARG   A  1  237  ? -34.447 71.404  71.757  1.00 37.31 ? 235  ARG   A NH2   1 
ATOM   1637  N  N     . TYR   A  1  238  ? -40.403 71.459  71.155  1.00 17.63 ? 236  TYR   A N     1 
ATOM   1638  C  CA    . TYR   A  1  238  ? -40.974 70.137  71.337  1.00 16.95 ? 236  TYR   A CA    1 
ATOM   1639  C  C     . TYR   A  1  238  ? -42.464 70.157  71.048  1.00 17.13 ? 236  TYR   A C     1 
ATOM   1640  O  O     . TYR   A  1  238  ? -42.998 69.208  70.464  1.00 17.18 ? 236  TYR   A O     1 
ATOM   1641  C  CB    . TYR   A  1  238  ? -40.691 69.630  72.749  1.00 16.24 ? 236  TYR   A CB    1 
ATOM   1642  C  CG    . TYR   A  1  238  ? -39.243 69.301  73.008  1.00 17.02 ? 236  TYR   A CG    1 
ATOM   1643  C  CD1   . TYR   A  1  238  ? -38.456 68.687  72.046  1.00 23.05 ? 236  TYR   A CD1   1 
ATOM   1644  C  CD2   . TYR   A  1  238  ? -38.662 69.610  74.226  1.00 18.63 ? 236  TYR   A CD2   1 
ATOM   1645  C  CE1   . TYR   A  1  238  ? -37.116 68.385  72.302  1.00 26.13 ? 236  TYR   A CE1   1 
ATOM   1646  C  CE2   . TYR   A  1  238  ? -37.340 69.308  74.492  1.00 23.94 ? 236  TYR   A CE2   1 
ATOM   1647  C  CZ    . TYR   A  1  238  ? -36.575 68.697  73.535  1.00 25.19 ? 236  TYR   A CZ    1 
ATOM   1648  O  OH    . TYR   A  1  238  ? -35.252 68.410  73.816  1.00 25.79 ? 236  TYR   A OH    1 
ATOM   1649  N  N     . TYR   A  1  239  ? -43.142 71.230  71.443  1.00 15.35 ? 237  TYR   A N     1 
ATOM   1650  C  CA    . TYR   A  1  239  ? -44.554 71.375  71.114  1.00 15.74 ? 237  TYR   A CA    1 
ATOM   1651  C  C     . TYR   A  1  239  ? -44.769 71.296  69.613  1.00 16.79 ? 237  TYR   A C     1 
ATOM   1652  O  O     . TYR   A  1  239  ? -45.606 70.522  69.135  1.00 16.83 ? 237  TYR   A O     1 
ATOM   1653  C  CB    . TYR   A  1  239  ? -45.097 72.701  71.637  1.00 17.34 ? 237  TYR   A CB    1 
ATOM   1654  C  CG    . TYR   A  1  239  ? -46.546 72.831  71.294  1.00 18.10 ? 237  TYR   A CG    1 
ATOM   1655  C  CD1   . TYR   A  1  239  ? -46.948 73.332  70.063  1.00 20.33 ? 237  TYR   A CD1   1 
ATOM   1656  C  CD2   . TYR   A  1  239  ? -47.522 72.388  72.170  1.00 19.03 ? 237  TYR   A CD2   1 
ATOM   1657  C  CE1   . TYR   A  1  239  ? -48.280 73.410  69.723  1.00 22.44 ? 237  TYR   A CE1   1 
ATOM   1658  C  CE2   . TYR   A  1  239  ? -48.849 72.474  71.844  1.00 21.40 ? 237  TYR   A CE2   1 
ATOM   1659  C  CZ    . TYR   A  1  239  ? -49.227 72.980  70.621  1.00 21.22 ? 237  TYR   A CZ    1 
ATOM   1660  O  OH    . TYR   A  1  239  ? -50.554 73.061  70.275  1.00 26.33 ? 237  TYR   A OH    1 
ATOM   1661  N  N     . ARG   A  1  240  ? -44.052 72.121  68.853  1.00 16.42 ? 238  ARG   A N     1 
ATOM   1662  C  CA    . ARG   A  1  240  ? -44.328 72.122  67.420  1.00 16.11 ? 238  ARG   A CA    1 
ATOM   1663  C  C     . ARG   A  1  240  ? -43.924 70.802  66.779  1.00 15.70 ? 238  ARG   A C     1 
ATOM   1664  O  O     . ARG   A  1  240  ? -44.531 70.396  65.782  1.00 16.69 ? 238  ARG   A O     1 
ATOM   1665  C  CB    . ARG   A  1  240  ? -43.722 73.351  66.727  1.00 21.08 ? 238  ARG   A CB    1 
ATOM   1666  C  CG    . ARG   A  1  240  ? -42.241 73.333  66.632  1.00 23.61 ? 238  ARG   A CG    1 
ATOM   1667  C  CD    . ARG   A  1  240  ? -41.727 74.546  65.855  1.00 20.36 ? 238  ARG   A CD    1 
ATOM   1668  N  NE    . ARG   A  1  240  ? -40.288 74.673  66.042  1.00 23.50 ? 238  ARG   A NE    1 
ATOM   1669  C  CZ    . ARG   A  1  240  ? -39.709 75.448  66.953  1.00 26.55 ? 238  ARG   A CZ    1 
ATOM   1670  N  NH1   . ARG   A  1  240  ? -40.411 76.270  67.721  1.00 22.39 ? 238  ARG   A NH1   1 
ATOM   1671  N  NH2   . ARG   A  1  240  ? -38.386 75.404  67.094  1.00 29.83 ? 238  ARG   A NH2   1 
ATOM   1672  N  N     . ASP   A  1  241  ? -42.928 70.102  67.329  1.00 15.61 ? 239  ASP   A N     1 
ATOM   1673  C  CA    . ASP   A  1  241  ? -42.610 68.759  66.852  1.00 15.94 ? 239  ASP   A CA    1 
ATOM   1674  C  C     . ASP   A  1  241  ? -43.761 67.793  67.109  1.00 16.89 ? 239  ASP   A C     1 
ATOM   1675  O  O     . ASP   A  1  241  ? -44.117 66.983  66.245  1.00 17.85 ? 239  ASP   A O     1 
ATOM   1676  C  CB    . ASP   A  1  241  ? -41.347 68.219  67.522  1.00 21.05 ? 239  ASP   A CB    1 
ATOM   1677  C  CG    . ASP   A  1  241  ? -40.089 68.932  67.078  1.00 31.05 ? 239  ASP   A CG    1 
ATOM   1678  O  OD1   . ASP   A  1  241  ? -40.160 69.780  66.162  1.00 37.56 ? 239  ASP   A OD1   1 
ATOM   1679  O  OD2   . ASP   A  1  241  ? -39.027 68.645  67.670  1.00 41.52 ? 239  ASP   A OD2   1 
ATOM   1680  N  N     . TYR   A  1  242  ? -44.354 67.851  68.301  1.00 16.42 ? 240  TYR   A N     1 
ATOM   1681  C  CA    . TYR   A  1  242  ? -45.502 66.995  68.578  1.00 15.81 ? 240  TYR   A CA    1 
ATOM   1682  C  C     . TYR   A  1  242  ? -46.678 67.348  67.677  1.00 15.30 ? 240  TYR   A C     1 
ATOM   1683  O  O     . TYR   A  1  242  ? -47.358 66.458  67.150  1.00 15.67 ? 240  TYR   A O     1 
ATOM   1684  C  CB    . TYR   A  1  242  ? -45.935 67.146  70.032  1.00 14.75 ? 240  TYR   A CB    1 
ATOM   1685  C  CG    . TYR   A  1  242  ? -45.049 66.518  71.073  1.00 15.70 ? 240  TYR   A CG    1 
ATOM   1686  C  CD1   . TYR   A  1  242  ? -44.413 65.302  70.861  1.00 17.76 ? 240  TYR   A CD1   1 
ATOM   1687  C  CD2   . TYR   A  1  242  ? -44.918 67.121  72.303  1.00 16.49 ? 240  TYR   A CD2   1 
ATOM   1688  C  CE1   . TYR   A  1  242  ? -43.622 64.735  71.862  1.00 17.85 ? 240  TYR   A CE1   1 
ATOM   1689  C  CE2   . TYR   A  1  242  ? -44.141 66.565  73.291  1.00 15.45 ? 240  TYR   A CE2   1 
ATOM   1690  C  CZ    . TYR   A  1  242  ? -43.510 65.389  73.066  1.00 14.27 ? 240  TYR   A CZ    1 
ATOM   1691  O  OH    . TYR   A  1  242  ? -42.753 64.869  74.098  1.00 16.35 ? 240  TYR   A OH    1 
ATOM   1692  N  N     . GLU   A  1  243  ? -46.941 68.639  67.507  1.00 14.07 ? 241  GLU   A N     1 
ATOM   1693  C  CA    . GLU   A  1  243  ? -48.073 69.046  66.688  1.00 15.17 ? 241  GLU   A CA    1 
ATOM   1694  C  C     . GLU   A  1  243  ? -47.879 68.574  65.255  1.00 15.76 ? 241  GLU   A C     1 
ATOM   1695  O  O     . GLU   A  1  243  ? -48.786 67.994  64.651  1.00 15.87 ? 241  GLU   A O     1 
ATOM   1696  C  CB    . GLU   A  1  243  ? -48.229 70.564  66.771  1.00 16.70 ? 241  GLU   A CB    1 
ATOM   1697  C  CG    . GLU   A  1  243  ? -49.308 71.156  65.917  1.00 20.24 ? 241  GLU   A CG    1 
ATOM   1698  C  CD    . GLU   A  1  243  ? -49.140 72.663  65.805  1.00 23.85 ? 241  GLU   A CD    1 
ATOM   1699  O  OE1   . GLU   A  1  243  ? -47.989 73.177  65.854  1.00 29.99 ? 241  GLU   A OE1   1 
ATOM   1700  O  OE2   . GLU   A  1  243  ? -50.166 73.326  65.673  1.00 21.48 ? 241  GLU   A OE2   1 
ATOM   1701  N  N     . SER   A  1  244  ? -46.680 68.770  64.709  1.00 16.29 ? 242  SER   A N     1 
ATOM   1702  C  CA    . SER   A  1  244  ? -46.442 68.325  63.341  1.00 15.30 ? 242  SER   A CA    1 
ATOM   1703  C  C     . SER   A  1  244  ? -46.520 66.807  63.225  1.00 16.11 ? 242  SER   A C     1 
ATOM   1704  O  O     . SER   A  1  244  ? -47.032 66.280  62.232  1.00 18.12 ? 242  SER   A O     1 
ATOM   1705  C  CB    . SER   A  1  244  ? -45.096 68.844  62.835  1.00 18.21 ? 242  SER   A CB    1 
ATOM   1706  O  OG    . SER   A  1  244  ? -44.015 68.276  63.543  1.00 22.06 ? 242  SER   A OG    1 
ATOM   1707  N  N     . ALA   A  1  245  ? -46.045 66.076  64.236  1.00 15.47 ? 243  ALA   A N     1 
ATOM   1708  C  CA    . ALA   A  1  245  ? -46.164 64.623  64.194  1.00 14.85 ? 243  ALA   A CA    1 
ATOM   1709  C  C     . ALA   A  1  245  ? -47.622 64.184  64.266  1.00 15.29 ? 243  ALA   A C     1 
ATOM   1710  O  O     . ALA   A  1  245  ? -48.027 63.237  63.585  1.00 16.70 ? 243  ALA   A O     1 
ATOM   1711  C  CB    . ALA   A  1  245  ? -45.351 63.978  65.316  1.00 17.51 ? 243  ALA   A CB    1 
ATOM   1712  N  N     . ILE   A  1  246  ? -48.426 64.835  65.105  1.00 15.40 ? 244  ILE   A N     1 
ATOM   1713  C  CA    . ILE   A  1  246  ? -49.836 64.470  65.171  1.00 14.93 ? 244  ILE   A CA    1 
ATOM   1714  C  C     . ILE   A  1  246  ? -50.488 64.621  63.808  1.00 16.83 ? 244  ILE   A C     1 
ATOM   1715  O  O     . ILE   A  1  246  ? -51.265 63.762  63.389  1.00 17.05 ? 244  ILE   A O     1 
ATOM   1716  C  CB    . ILE   A  1  246  ? -50.568 65.282  66.247  1.00 14.93 ? 244  ILE   A CB    1 
ATOM   1717  C  CG1   . ILE   A  1  246  ? -50.114 64.823  67.633  1.00 15.26 ? 244  ILE   A CG1   1 
ATOM   1718  C  CG2   . ILE   A  1  246  ? -52.077 65.113  66.094  1.00 16.76 ? 244  ILE   A CG2   1 
ATOM   1719  C  CD1   . ILE   A  1  246  ? -50.514 65.786  68.742  1.00 17.24 ? 244  ILE   A CD1   1 
ATOM   1720  N  N     . HIS   A  1  247  ? -50.170 65.700  63.082  1.00 15.04 ? 245  HIS   A N     1 
ATOM   1721  C  CA    . HIS   A  1  247  ? -50.757 65.845  61.752  1.00 14.70 ? 245  HIS   A CA    1 
ATOM   1722  C  C     . HIS   A  1  247  ? -50.340 64.694  60.853  1.00 15.99 ? 245  HIS   A C     1 
ATOM   1723  O  O     . HIS   A  1  247  ? -51.172 64.104  60.160  1.00 17.16 ? 245  HIS   A O     1 
ATOM   1724  C  CB    . HIS   A  1  247  ? -50.344 67.170  61.125  1.00 17.05 ? 245  HIS   A CB    1 
ATOM   1725  C  CG    . HIS   A  1  247  ? -51.051 68.350  61.690  1.00 19.28 ? 245  HIS   A CG    1 
ATOM   1726  N  ND1   . HIS   A  1  247  ? -52.405 68.544  61.559  1.00 18.25 ? 245  HIS   A ND1   1 
ATOM   1727  C  CD2   . HIS   A  1  247  ? -50.583 69.409  62.391  1.00 19.37 ? 245  HIS   A CD2   1 
ATOM   1728  C  CE1   . HIS   A  1  247  ? -52.746 69.674  62.151  1.00 21.23 ? 245  HIS   A CE1   1 
ATOM   1729  N  NE2   . HIS   A  1  247  ? -51.657 70.216  62.660  1.00 19.04 ? 245  HIS   A NE2   1 
ATOM   1730  N  N     . ALA   A  1  248  ? -49.056 64.358  60.851  1.00 15.61 ? 246  ALA   A N     1 
ATOM   1731  C  CA    . ALA   A  1  248  ? -48.591 63.295  59.975  1.00 16.45 ? 246  ALA   A CA    1 
ATOM   1732  C  C     . ALA   A  1  248  ? -49.200 61.960  60.366  1.00 16.70 ? 246  ALA   A C     1 
ATOM   1733  O  O     . ALA   A  1  248  ? -49.652 61.200  59.505  1.00 17.40 ? 246  ALA   A O     1 
ATOM   1734  C  CB    . ALA   A  1  248  ? -47.066 63.229  59.990  1.00 16.97 ? 246  ALA   A CB    1 
ATOM   1735  N  N     . ILE   A  1  249  ? -49.231 61.669  61.668  1.00 16.19 ? 247  ILE   A N     1 
ATOM   1736  C  CA    . ILE   A  1  249  ? -49.793 60.418  62.156  1.00 15.74 ? 247  ILE   A CA    1 
ATOM   1737  C  C     . ILE   A  1  249  ? -51.287 60.372  61.885  1.00 15.86 ? 247  ILE   A C     1 
ATOM   1738  O  O     . ILE   A  1  249  ? -51.829 59.340  61.477  1.00 17.61 ? 247  ILE   A O     1 
ATOM   1739  C  CB    . ILE   A  1  249  ? -49.484 60.280  63.656  1.00 15.76 ? 247  ILE   A CB    1 
ATOM   1740  C  CG1   . ILE   A  1  249  ? -47.984 60.155  63.892  1.00 16.24 ? 247  ILE   A CG1   1 
ATOM   1741  C  CG2   . ILE   A  1  249  ? -50.198 59.063  64.242  1.00 16.99 ? 247  ILE   A CG2   1 
ATOM   1742  C  CD1   . ILE   A  1  249  ? -47.586 60.480  65.322  1.00 16.85 ? 247  ILE   A CD1   1 
ATOM   1743  N  N     . GLY   A  1  250  ? -51.979 61.482  62.117  1.00 15.13 ? 248  GLY   A N     1 
ATOM   1744  C  CA    . GLY   A  1  250  ? -53.409 61.505  61.875  1.00 16.63 ? 248  GLY   A CA    1 
ATOM   1745  C  C     . GLY   A  1  250  ? -53.763 61.395  60.404  1.00 16.64 ? 248  GLY   A C     1 
ATOM   1746  O  O     . GLY   A  1  250  ? -54.753 60.753  60.047  1.00 17.82 ? 248  GLY   A O     1 
ATOM   1747  N  N     . LYS   A  1  251  ? -52.977 62.036  59.536  1.00 16.52 ? 249  LYS   A N     1 
ATOM   1748  C  CA    . LYS   A  1  251  ? -53.205 61.872  58.105  1.00 18.01 ? 249  LYS   A CA    1 
ATOM   1749  C  C     . LYS   A  1  251  ? -53.019 60.422  57.705  1.00 18.64 ? 249  LYS   A C     1 
ATOM   1750  O  O     . LYS   A  1  251  ? -53.778 59.897  56.883  1.00 19.32 ? 249  LYS   A O     1 
ATOM   1751  C  CB    . LYS   A  1  251  ? -52.234 62.730  57.305  1.00 19.58 ? 249  LYS   A CB    1 
ATOM   1752  C  CG    . LYS   A  1  251  ? -52.485 64.218  57.348  1.00 18.98 ? 249  LYS   A CG    1 
ATOM   1753  C  CD    . LYS   A  1  251  ? -51.272 64.902  56.763  1.00 21.57 ? 249  LYS   A CD    1 
ATOM   1754  C  CE    . LYS   A  1  251  ? -51.376 66.407  56.773  1.00 21.24 ? 249  LYS   A CE    1 
ATOM   1755  N  NZ    . LYS   A  1  251  ? -50.109 66.958  56.198  1.00 20.65 ? 249  LYS   A NZ    1 
ATOM   1756  N  N     . ALA   A  1  252  ? -51.998 59.766  58.270  1.00 18.45 ? 250  ALA   A N     1 
ATOM   1757  C  CA    . ALA   A  1  252  ? -51.712 58.381  57.926  1.00 19.49 ? 250  ALA   A CA    1 
ATOM   1758  C  C     . ALA   A  1  252  ? -52.722 57.447  58.556  1.00 19.94 ? 250  ALA   A C     1 
ATOM   1759  O  O     . ALA   A  1  252  ? -53.087 56.428  57.961  1.00 20.73 ? 250  ALA   A O     1 
ATOM   1760  C  CB    . ALA   A  1  252  ? -50.315 58.004  58.398  1.00 22.88 ? 250  ALA   A CB    1 
ATOM   1761  N  N     . SER   A  1  253  ? -53.169 57.761  59.771  1.00 19.73 ? 251  SER   A N     1 
ATOM   1762  C  CA    . SER   A  1  253  ? -54.157 56.909  60.409  1.00 18.64 ? 251  SER   A CA    1 
ATOM   1763  C  C     . SER   A  1  253  ? -55.378 56.766  59.527  1.00 20.39 ? 251  SER   A C     1 
ATOM   1764  O  O     . SER   A  1  253  ? -55.920 55.668  59.383  1.00 20.73 ? 251  SER   A O     1 
ATOM   1765  C  CB    . SER   A  1  253  ? -54.550 57.505  61.753  1.00 18.44 ? 251  SER   A CB    1 
ATOM   1766  O  OG    . SER   A  1  253  ? -55.549 56.710  62.346  1.00 18.61 ? 251  SER   A OG    1 
ATOM   1767  N  N     . ALA   A  1  254  ? -55.797 57.868  58.910  1.00 19.80 ? 252  ALA   A N     1 
ATOM   1768  C  CA    . ALA   A  1  254  ? -56.852 57.865  57.902  1.00 21.71 ? 252  ALA   A CA    1 
ATOM   1769  C  C     . ALA   A  1  254  ? -58.110 57.168  58.410  1.00 23.80 ? 252  ALA   A C     1 
ATOM   1770  O  O     . ALA   A  1  254  ? -58.724 56.342  57.726  1.00 23.93 ? 252  ALA   A O     1 
ATOM   1771  C  CB    . ALA   A  1  254  ? -56.353 57.268  56.586  1.00 25.85 ? 252  ALA   A CB    1 
ATOM   1772  N  N     . GLY   A  1  255  ? -58.500 57.506  59.630  1.00 21.46 ? 253  GLY   A N     1 
ATOM   1773  C  CA    . GLY   A  1  255  ? -59.739 56.988  60.170  1.00 21.63 ? 253  GLY   A CA    1 
ATOM   1774  C  C     . GLY   A  1  255  ? -59.682 55.602  60.770  1.00 19.99 ? 253  GLY   A C     1 
ATOM   1775  O  O     . GLY   A  1  255  ? -60.730 55.055  61.118  1.00 25.12 ? 253  GLY   A O     1 
ATOM   1776  N  N     . ARG   A  1  256  ? -58.493 55.017  60.930  1.00 19.94 ? 254  ARG   A N     1 
ATOM   1777  C  CA    . ARG   A  1  256  ? -58.405 53.699  61.545  1.00 20.51 ? 254  ARG   A CA    1 
ATOM   1778  C  C     . ARG   A  1  256  ? -58.767 53.718  63.020  1.00 20.71 ? 254  ARG   A C     1 
ATOM   1779  O  O     . ARG   A  1  256  ? -59.025 52.654  63.592  1.00 21.93 ? 254  ARG   A O     1 
ATOM   1780  C  CB    . ARG   A  1  256  ? -57.009 53.110  61.370  1.00 19.90 ? 254  ARG   A CB    1 
ATOM   1781  C  CG    . ARG   A  1  256  ? -56.803 52.468  60.016  1.00 23.77 ? 254  ARG   A CG    1 
ATOM   1782  C  CD    . ARG   A  1  256  ? -55.386 51.987  59.889  1.00 25.63 ? 254  ARG   A CD    1 
ATOM   1783  N  NE    . ARG   A  1  256  ? -54.476 53.101  59.669  1.00 21.27 ? 254  ARG   A NE    1 
ATOM   1784  C  CZ    . ARG   A  1  256  ? -53.158 52.976  59.636  1.00 24.05 ? 254  ARG   A CZ    1 
ATOM   1785  N  NH1   . ARG   A  1  256  ? -52.571 51.820  59.910  1.00 24.96 ? 254  ARG   A NH1   1 
ATOM   1786  N  NH2   . ARG   A  1  256  ? -52.413 54.031  59.313  1.00 22.93 ? 254  ARG   A NH2   1 
ATOM   1787  N  N     . GLY   A  1  257  ? -58.772 54.886  63.651  1.00 17.79 ? 255  GLY   A N     1 
ATOM   1788  C  CA    . GLY   A  1  257  ? -59.157 54.972  65.044  1.00 18.46 ? 255  GLY   A CA    1 
ATOM   1789  C  C     . GLY   A  1  257  ? -58.015 54.668  65.990  1.00 17.40 ? 255  GLY   A C     1 
ATOM   1790  O  O     . GLY   A  1  257  ? -56.882 54.388  65.600  1.00 18.44 ? 255  GLY   A O     1 
ATOM   1791  N  N     . ILE   A  1  258  ? -58.342 54.691  67.278  1.00 16.66 ? 256  ILE   A N     1 
ATOM   1792  C  CA    . ILE   A  1  258  ? -57.295 54.721  68.296  1.00 15.96 ? 256  ILE   A CA    1 
ATOM   1793  C  C     . ILE   A  1  258  ? -56.703 53.360  68.601  1.00 19.06 ? 256  ILE   A C     1 
ATOM   1794  O  O     . ILE   A  1  258  ? -55.622 53.289  69.192  1.00 18.05 ? 256  ILE   A O     1 
ATOM   1795  C  CB    . ILE   A  1  258  ? -57.809 55.387  69.578  1.00 15.75 ? 256  ILE   A CB    1 
ATOM   1796  C  CG1   . ILE   A  1  258  ? -58.939 54.561  70.208  1.00 19.32 ? 256  ILE   A CG1   1 
ATOM   1797  C  CG2   . ILE   A  1  258  ? -58.228 56.824  69.301  1.00 17.81 ? 256  ILE   A CG2   1 
ATOM   1798  C  CD1   . ILE   A  1  258  ? -59.416 55.130  71.527  1.00 18.78 ? 256  ILE   A CD1   1 
ATOM   1799  N  N     . TYR   A  1  259  ? -57.375 52.272  68.242  1.00 19.16 ? 257  TYR   A N     1 
ATOM   1800  C  CA    . TYR   A  1  259  ? -56.849 50.951  68.561  1.00 17.96 ? 257  TYR   A CA    1 
ATOM   1801  C  C     . TYR   A  1  259  ? -56.060 50.360  67.403  1.00 22.18 ? 257  TYR   A C     1 
ATOM   1802  O  O     . TYR   A  1  259  ? -54.910 49.949  67.579  1.00 23.08 ? 257  TYR   A O     1 
ATOM   1803  C  CB    . TYR   A  1  259  ? -57.989 50.021  68.988  1.00 21.89 ? 257  TYR   A CB    1 
ATOM   1804  C  CG    . TYR   A  1  259  ? -58.805 50.614  70.102  1.00 20.12 ? 257  TYR   A CG    1 
ATOM   1805  C  CD1   . TYR   A  1  259  ? -58.221 50.921  71.322  1.00 21.93 ? 257  TYR   A CD1   1 
ATOM   1806  C  CD2   . TYR   A  1  259  ? -60.150 50.905  69.930  1.00 20.51 ? 257  TYR   A CD2   1 
ATOM   1807  C  CE1   . TYR   A  1  259  ? -58.954 51.487  72.344  1.00 21.28 ? 257  TYR   A CE1   1 
ATOM   1808  C  CE2   . TYR   A  1  259  ? -60.897 51.471  70.954  1.00 22.40 ? 257  TYR   A CE2   1 
ATOM   1809  C  CZ    . TYR   A  1  259  ? -60.284 51.763  72.158  1.00 21.30 ? 257  TYR   A CZ    1 
ATOM   1810  O  OH    . TYR   A  1  259  ? -60.991 52.332  73.186  1.00 20.74 ? 257  TYR   A OH    1 
ATOM   1811  N  N     . GLU   A  1  260  ? -56.645 50.339  66.208  1.00 19.36 ? 258  GLU   A N     1 
ATOM   1812  C  CA    . GLU   A  1  260  ? -55.925 49.828  65.051  1.00 22.57 ? 258  GLU   A CA    1 
ATOM   1813  C  C     . GLU   A  1  260  ? -54.905 50.830  64.542  1.00 23.82 ? 258  GLU   A C     1 
ATOM   1814  O  O     . GLU   A  1  260  ? -53.836 50.437  64.058  1.00 27.21 ? 258  GLU   A O     1 
ATOM   1815  C  CB    . GLU   A  1  260  ? -56.894 49.502  63.911  1.00 25.58 ? 258  GLU   A CB    1 
ATOM   1816  C  CG    . GLU   A  1  260  ? -56.174 48.954  62.680  1.00 33.64 ? 258  GLU   A CG    1 
ATOM   1817  C  CD    . GLU   A  1  260  ? -57.055 48.837  61.448  1.00 40.37 ? 258  GLU   A CD    1 
ATOM   1818  O  OE1   . GLU   A  1  260  ? -58.295 48.755  61.591  1.00 41.82 ? 258  GLU   A OE1   1 
ATOM   1819  O  OE2   . GLU   A  1  260  ? -56.493 48.829  60.329  1.00 37.20 ? 258  GLU   A OE2   1 
ATOM   1820  N  N     . GLY   A  1  261  ? -55.202 52.117  64.662  1.00 19.06 ? 259  GLY   A N     1 
ATOM   1821  C  CA    . GLY   A  1  261  ? -54.389 53.132  64.059  1.00 18.01 ? 259  GLY   A CA    1 
ATOM   1822  C  C     . GLY   A  1  261  ? -53.312 53.625  64.992  1.00 18.15 ? 259  GLY   A C     1 
ATOM   1823  O  O     . GLY   A  1  261  ? -53.320 53.372  66.199  1.00 17.40 ? 259  GLY   A O     1 
ATOM   1824  N  N     . PRO   A  1  262  ? -52.363 54.348  64.425  1.00 17.39 ? 260  PRO   A N     1 
ATOM   1825  C  CA    . PRO   A  1  262  ? -51.205 54.804  65.192  1.00 17.16 ? 260  PRO   A CA    1 
ATOM   1826  C  C     . PRO   A  1  262  ? -51.571 55.952  66.109  1.00 16.97 ? 260  PRO   A C     1 
ATOM   1827  O  O     . PRO   A  1  262  ? -52.555 56.662  65.905  1.00 19.54 ? 260  PRO   A O     1 
ATOM   1828  C  CB    . PRO   A  1  262  ? -50.245 55.282  64.105  1.00 17.47 ? 260  PRO   A CB    1 
ATOM   1829  C  CG    . PRO   A  1  262  ? -51.164 55.677  62.956  1.00 19.63 ? 260  PRO   A CG    1 
ATOM   1830  C  CD    . PRO   A  1  262  ? -52.268 54.686  62.998  1.00 18.76 ? 260  PRO   A CD    1 
ATOM   1831  N  N     . GLY   A  1  263  ? -50.747 56.128  67.139  1.00 16.35 ? 261  GLY   A N     1 
ATOM   1832  C  CA    . GLY   A  1  263  ? -50.883 57.276  68.016  1.00 16.17 ? 261  GLY   A CA    1 
ATOM   1833  C  C     . GLY   A  1  263  ? -49.545 57.919  68.313  1.00 14.37 ? 261  GLY   A C     1 
ATOM   1834  O  O     . GLY   A  1  263  ? -48.535 57.592  67.678  1.00 15.80 ? 261  GLY   A O     1 
ATOM   1835  N  N     . ILE   A  1  264  ? -49.541 58.850  69.259  1.00 15.28 ? 262  ILE   A N     1 
ATOM   1836  C  CA    . ILE   A  1  264  ? -48.328 59.550  69.650  1.00 15.59 ? 262  ILE   A CA    1 
ATOM   1837  C  C     . ILE   A  1  264  ? -48.156 59.410  71.154  1.00 15.20 ? 262  ILE   A C     1 
ATOM   1838  O  O     . ILE   A  1  264  ? -49.126 59.246  71.900  1.00 15.22 ? 262  ILE   A O     1 
ATOM   1839  C  CB    . ILE   A  1  264  ? -48.384 61.034  69.207  1.00 16.55 ? 262  ILE   A CB    1 
ATOM   1840  C  CG1   . ILE   A  1  264  ? -46.994 61.665  69.255  1.00 18.15 ? 262  ILE   A CG1   1 
ATOM   1841  C  CG2   . ILE   A  1  264  ? -49.414 61.835  70.030  1.00 17.07 ? 262  ILE   A CG2   1 
ATOM   1842  C  CD1   . ILE   A  1  264  ? -46.970 63.078  68.705  1.00 19.42 ? 262  ILE   A CD1   1 
ATOM   1843  N  N     . SER   A  1  265  ? -46.905 59.471  71.597  1.00 13.85 ? 263  SER   A N     1 
ATOM   1844  C  CA    . SER   A  1  265  ? -46.570 59.551  73.008  1.00 14.79 ? 263  SER   A CA    1 
ATOM   1845  C  C     . SER   A  1  265  ? -45.838 60.856  73.253  1.00 16.27 ? 263  SER   A C     1 
ATOM   1846  O  O     . SER   A  1  265  ? -44.991 61.258  72.445  1.00 19.40 ? 263  SER   A O     1 
ATOM   1847  C  CB    . SER   A  1  265  ? -45.673 58.400  73.444  1.00 17.00 ? 263  SER   A CB    1 
ATOM   1848  O  OG    . SER   A  1  265  ? -46.385 57.180  73.440  1.00 18.44 ? 263  SER   A OG    1 
ATOM   1849  N  N     . ILE   A  1  266  ? -46.160 61.514  74.363  1.00 14.94 ? 264  ILE   A N     1 
ATOM   1850  C  CA    . ILE   A  1  266  ? -45.525 62.768  74.737  1.00 15.48 ? 264  ILE   A CA    1 
ATOM   1851  C  C     . ILE   A  1  266  ? -44.979 62.650  76.148  1.00 14.56 ? 264  ILE   A C     1 
ATOM   1852  O  O     . ILE   A  1  266  ? -45.431 61.835  76.952  1.00 15.39 ? 264  ILE   A O     1 
ATOM   1853  C  CB    . ILE   A  1  266  ? -46.478 63.975  74.642  1.00 16.90 ? 264  ILE   A CB    1 
ATOM   1854  C  CG1   . ILE   A  1  266  ? -47.605 63.881  75.667  1.00 17.88 ? 264  ILE   A CG1   1 
ATOM   1855  C  CG2   . ILE   A  1  266  ? -47.087 64.070  73.243  1.00 17.15 ? 264  ILE   A CG2   1 
ATOM   1856  C  CD1   . ILE   A  1  266  ? -48.429 65.153  75.762  1.00 18.47 ? 264  ILE   A CD1   1 
ATOM   1857  N  N     . LYS   A  1  267  ? -44.017 63.503  76.451  1.00 15.43 ? 265  LYS   A N     1 
ATOM   1858  C  CA    . LYS   A  1  267  ? -43.526 63.664  77.808  1.00 14.24 ? 265  LYS   A CA    1 
ATOM   1859  C  C     . LYS   A  1  267  ? -43.846 65.067  78.273  1.00 14.20 ? 265  LYS   A C     1 
ATOM   1860  O  O     . LYS   A  1  267  ? -43.525 66.046  77.593  1.00 15.16 ? 265  LYS   A O     1 
ATOM   1861  C  CB    . LYS   A  1  267  ? -42.020 63.437  77.856  1.00 16.35 ? 265  LYS   A CB    1 
ATOM   1862  C  CG    . LYS   A  1  267  ? -41.633 61.982  77.755  1.00 19.48 ? 265  LYS   A CG    1 
ATOM   1863  C  CD    . LYS   A  1  267  ? -40.121 61.864  77.802  1.00 23.19 ? 265  LYS   A CD    1 
ATOM   1864  C  CE    . LYS   A  1  267  ? -39.663 60.440  77.732  1.00 31.49 ? 265  LYS   A CE    1 
ATOM   1865  N  NZ    . LYS   A  1  267  ? -40.369 59.705  76.645  1.00 32.31 ? 265  LYS   A NZ    1 
ATOM   1866  N  N     . LEU   A  1  268  ? -44.511 65.172  79.416  1.00 14.27 ? 266  LEU   A N     1 
ATOM   1867  C  CA    . LEU   A  1  268  ? -44.838 66.497  79.923  1.00 15.15 ? 266  LEU   A CA    1 
ATOM   1868  C  C     . LEU   A  1  268  ? -43.596 67.346  80.149  1.00 14.60 ? 266  LEU   A C     1 
ATOM   1869  O  O     . LEU   A  1  268  ? -43.655 68.570  79.984  1.00 15.96 ? 266  LEU   A O     1 
ATOM   1870  C  CB    . LEU   A  1  268  ? -45.667 66.397  81.203  1.00 15.76 ? 266  LEU   A CB    1 
ATOM   1871  C  CG    . LEU   A  1  268  ? -46.998 65.672  81.000  1.00 16.33 ? 266  LEU   A CG    1 
ATOM   1872  C  CD1   . LEU   A  1  268  ? -47.766 65.594  82.296  1.00 18.19 ? 266  LEU   A CD1   1 
ATOM   1873  C  CD2   . LEU   A  1  268  ? -47.816 66.359  79.918  1.00 19.87 ? 266  LEU   A CD2   1 
ATOM   1874  N  N     . SER   A  1  269  ? -42.468 66.730  80.513  1.00 14.78 ? 267  SER   A N     1 
ATOM   1875  C  CA    . SER   A  1  269  ? -41.271 67.523  80.746  1.00 15.39 ? 267  SER   A CA    1 
ATOM   1876  C  C     . SER   A  1  269  ? -40.762 68.171  79.478  1.00 16.67 ? 267  SER   A C     1 
ATOM   1877  O  O     . SER   A  1  269  ? -39.981 69.122  79.559  1.00 16.76 ? 267  SER   A O     1 
ATOM   1878  C  CB    . SER   A  1  269  ? -40.157 66.678  81.348  1.00 16.57 ? 267  SER   A CB    1 
ATOM   1879  O  OG    . SER   A  1  269  ? -39.652 65.743  80.420  1.00 16.78 ? 267  SER   A OG    1 
ATOM   1880  N  N     . ALA   A  1  270  ? -41.163 67.663  78.309  1.00 14.35 ? 268  ALA   A N     1 
ATOM   1881  C  CA    . ALA   A  1  270  ? -40.771 68.311  77.068  1.00 14.89 ? 268  ALA   A CA    1 
ATOM   1882  C  C     . ALA   A  1  270  ? -41.528 69.602  76.846  1.00 14.35 ? 268  ALA   A C     1 
ATOM   1883  O  O     . ALA   A  1  270  ? -41.087 70.438  76.056  1.00 15.57 ? 268  ALA   A O     1 
ATOM   1884  C  CB    . ALA   A  1  270  ? -41.051 67.372  75.893  1.00 16.77 ? 268  ALA   A CB    1 
ATOM   1885  N  N     . LEU   A  1  271  ? -42.663 69.791  77.508  1.00 14.53 ? 269  LEU   A N     1 
ATOM   1886  C  CA    . LEU   A  1  271  ? -43.567 70.864  77.150  1.00 15.78 ? 269  LEU   A CA    1 
ATOM   1887  C  C     . LEU   A  1  271  ? -43.492 72.045  78.090  1.00 16.26 ? 269  LEU   A C     1 
ATOM   1888  O  O     . LEU   A  1  271  ? -44.188 73.036  77.876  1.00 17.44 ? 269  LEU   A O     1 
ATOM   1889  C  CB    . LEU   A  1  271  ? -44.998 70.349  77.075  1.00 15.94 ? 269  LEU   A CB    1 
ATOM   1890  C  CG    . LEU   A  1  271  ? -45.195 69.395  75.900  1.00 17.75 ? 269  LEU   A CG    1 
ATOM   1891  C  CD1   . LEU   A  1  271  ? -46.576 68.765  75.979  1.00 20.36 ? 269  LEU   A CD1   1 
ATOM   1892  C  CD2   . LEU   A  1  271  ? -45.054 70.173  74.617  1.00 20.04 ? 269  LEU   A CD2   1 
ATOM   1893  N  N     . HIS   A  1  272  ? -42.660 71.962  79.126  1.00 16.02 ? 270  HIS   A N     1 
ATOM   1894  C  CA    . HIS   A  1  272  ? -42.504 73.128  79.965  1.00 15.16 ? 270  HIS   A CA    1 
ATOM   1895  C  C     . HIS   A  1  272  ? -41.163 73.005  80.648  1.00 15.30 ? 270  HIS   A C     1 
ATOM   1896  O  O     . HIS   A  1  272  ? -40.830 71.919  81.124  1.00 16.81 ? 270  HIS   A O     1 
ATOM   1897  C  CB    . HIS   A  1  272  ? -43.604 73.217  81.023  1.00 17.72 ? 270  HIS   A CB    1 
ATOM   1898  C  CG    . HIS   A  1  272  ? -43.710 74.575  81.632  1.00 18.62 ? 270  HIS   A CG    1 
ATOM   1899  N  ND1   . HIS   A  1  272  ? -42.773 75.075  82.515  1.00 19.91 ? 270  HIS   A ND1   1 
ATOM   1900  C  CD2   . HIS   A  1  272  ? -44.623 75.557  81.454  1.00 21.90 ? 270  HIS   A CD2   1 
ATOM   1901  C  CE1   . HIS   A  1  272  ? -43.106 76.309  82.848  1.00 21.73 ? 270  HIS   A CE1   1 
ATOM   1902  N  NE2   . HIS   A  1  272  ? -44.227 76.622  82.222  1.00 22.52 ? 270  HIS   A NE2   1 
ATOM   1903  N  N     . PRO   A  1  273  ? -40.377 74.079  80.717  1.00 17.72 ? 271  PRO   A N     1 
ATOM   1904  C  CA    . PRO   A  1  273  ? -39.064 73.989  81.362  1.00 16.66 ? 271  PRO   A CA    1 
ATOM   1905  C  C     . PRO   A  1  273  ? -39.111 73.896  82.871  1.00 17.07 ? 271  PRO   A C     1 
ATOM   1906  O  O     . PRO   A  1  273  ? -38.075 73.604  83.471  1.00 18.08 ? 271  PRO   A O     1 
ATOM   1907  C  CB    . PRO   A  1  273  ? -38.370 75.283  80.919  1.00 18.32 ? 271  PRO   A CB    1 
ATOM   1908  C  CG    . PRO   A  1  273  ? -39.496 76.246  80.733  1.00 19.92 ? 271  PRO   A CG    1 
ATOM   1909  C  CD    . PRO   A  1  273  ? -40.635 75.420  80.165  1.00 17.99 ? 271  PRO   A CD    1 
ATOM   1910  N  N     . ARG   A  1  274  ? -40.257 74.143  83.499  1.00 15.36 ? 272  ARG   A N     1 
ATOM   1911  C  CA    . ARG   A  1  274  ? -40.349 74.046  84.950  1.00 15.32 ? 272  ARG   A CA    1 
ATOM   1912  C  C     . ARG   A  1  274  ? -41.470 73.101  85.337  1.00 17.41 ? 272  ARG   A C     1 
ATOM   1913  O  O     . ARG   A  1  274  ? -42.387 73.455  86.086  1.00 18.37 ? 272  ARG   A O     1 
ATOM   1914  C  CB    . ARG   A  1  274  ? -40.569 75.418  85.576  1.00 17.43 ? 272  ARG   A CB    1 
ATOM   1915  C  CG    . ARG   A  1  274  ? -39.420 76.405  85.350  1.00 16.60 ? 272  ARG   A CG    1 
ATOM   1916  C  CD    . ARG   A  1  274  ? -38.084 75.869  85.873  1.00 18.02 ? 272  ARG   A CD    1 
ATOM   1917  N  NE    . ARG   A  1  274  ? -38.147 75.474  87.277  1.00 18.99 ? 272  ARG   A NE    1 
ATOM   1918  C  CZ    . ARG   A  1  274  ? -38.109 76.327  88.295  1.00 18.05 ? 272  ARG   A CZ    1 
ATOM   1919  N  NH1   . ARG   A  1  274  ? -38.059 77.633  88.094  1.00 19.05 ? 272  ARG   A NH1   1 
ATOM   1920  N  NH2   . ARG   A  1  274  ? -38.133 75.854  89.540  1.00 18.85 ? 272  ARG   A NH2   1 
ATOM   1921  N  N     . TYR   A  1  275  ? -41.402 71.887  84.815  1.00 15.90 ? 273  TYR   A N     1 
ATOM   1922  C  CA    . TYR   A  1  275  ? -42.408 70.879  85.098  1.00 15.52 ? 273  TYR   A CA    1 
ATOM   1923  C  C     . TYR   A  1  275  ? -42.028 70.216  86.412  1.00 15.65 ? 273  TYR   A C     1 
ATOM   1924  O  O     . TYR   A  1  275  ? -41.220 69.291  86.468  1.00 16.63 ? 273  TYR   A O     1 
ATOM   1925  C  CB    . TYR   A  1  275  ? -42.488 69.895  83.937  1.00 15.34 ? 273  TYR   A CB    1 
ATOM   1926  C  CG    . TYR   A  1  275  ? -43.422 68.760  84.215  1.00 14.51 ? 273  TYR   A CG    1 
ATOM   1927  C  CD1   . TYR   A  1  275  ? -44.719 68.995  84.634  1.00 16.44 ? 273  TYR   A CD1   1 
ATOM   1928  C  CD2   . TYR   A  1  275  ? -42.990 67.455  84.075  1.00 14.46 ? 273  TYR   A CD2   1 
ATOM   1929  C  CE1   . TYR   A  1  275  ? -45.566 67.937  84.911  1.00 16.96 ? 273  TYR   A CE1   1 
ATOM   1930  C  CE2   . TYR   A  1  275  ? -43.827 66.396  84.344  1.00 15.13 ? 273  TYR   A CE2   1 
ATOM   1931  C  CZ    . TYR   A  1  275  ? -45.108 66.650  84.764  1.00 17.24 ? 273  TYR   A CZ    1 
ATOM   1932  O  OH    . TYR   A  1  275  ? -45.938 65.603  85.048  1.00 17.54 ? 273  TYR   A OH    1 
ATOM   1933  N  N     . SER   A  1  276  ? -42.614 70.716  87.492  1.00 15.10 ? 274  SER   A N     1 
ATOM   1934  C  CA    . SER   A  1  276  ? -42.307 70.204  88.817  1.00 14.15 ? 274  SER   A CA    1 
ATOM   1935  C  C     . SER   A  1  276  ? -43.409 70.634  89.762  1.00 15.39 ? 274  SER   A C     1 
ATOM   1936  O  O     . SER   A  1  276  ? -44.116 71.611  89.515  1.00 15.85 ? 274  SER   A O     1 
ATOM   1937  C  CB    . SER   A  1  276  ? -40.967 70.741  89.325  1.00 19.54 ? 274  SER   A CB    1 
ATOM   1938  O  OG    . SER   A  1  276  ? -41.061 72.128  89.592  1.00 22.94 ? 274  SER   A OG    1 
ATOM   1939  N  N     . ARG   A  1  277  ? -43.553 69.871  90.849  1.00 15.58 ? 275  ARG   A N     1 
ATOM   1940  C  CA    . ARG   A  1  277  ? -44.534 70.229  91.866  1.00 15.64 ? 275  ARG   A CA    1 
ATOM   1941  C  C     . ARG   A  1  277  ? -44.295 71.627  92.423  1.00 16.12 ? 275  ARG   A C     1 
ATOM   1942  O  O     . ARG   A  1  277  ? -45.254 72.339  92.724  1.00 16.35 ? 275  ARG   A O     1 
ATOM   1943  C  CB    . ARG   A  1  277  ? -44.520 69.190  92.990  1.00 15.78 ? 275  ARG   A CB    1 
ATOM   1944  C  CG    . ARG   A  1  277  ? -45.369 69.550  94.214  1.00 16.74 ? 275  ARG   A CG    1 
ATOM   1945  C  CD    . ARG   A  1  277  ? -46.847 69.740  93.847  1.00 16.49 ? 275  ARG   A CD    1 
ATOM   1946  N  NE    . ARG   A  1  277  ? -47.668 70.070  95.012  1.00 16.33 ? 275  ARG   A NE    1 
ATOM   1947  C  CZ    . ARG   A  1  277  ? -47.854 71.303  95.470  1.00 16.11 ? 275  ARG   A CZ    1 
ATOM   1948  N  NH1   . ARG   A  1  277  ? -47.232 72.344  94.936  1.00 18.09 ? 275  ARG   A NH1   1 
ATOM   1949  N  NH2   . ARG   A  1  277  ? -48.678 71.496  96.505  1.00 17.12 ? 275  ARG   A NH2   1 
ATOM   1950  N  N     . ALA   A  1  278  ? -43.031 72.046  92.555  1.00 16.35 ? 276  ALA   A N     1 
ATOM   1951  C  CA    . ALA   A  1  278  ? -42.769 73.370  93.109  1.00 18.76 ? 276  ALA   A CA    1 
ATOM   1952  C  C     . ALA   A  1  278  ? -43.338 74.462  92.227  1.00 17.10 ? 276  ALA   A C     1 
ATOM   1953  O  O     . ALA   A  1  278  ? -43.649 75.556  92.706  1.00 20.00 ? 276  ALA   A O     1 
ATOM   1954  C  CB    . ALA   A  1  278  ? -41.264 73.571  93.279  1.00 19.05 ? 276  ALA   A CB    1 
ATOM   1955  N  N     . GLN   A  1  279  ? -43.464 74.187  90.935  1.00 16.63 ? 277  GLN   A N     1 
ATOM   1956  C  CA    . GLN   A  1  279  ? -44.001 75.133  89.968  1.00 16.32 ? 277  GLN   A CA    1 
ATOM   1957  C  C     . GLN   A  1  279  ? -45.383 74.714  89.485  1.00 17.45 ? 277  GLN   A C     1 
ATOM   1958  O  O     . GLN   A  1  279  ? -45.751 74.987  88.343  1.00 16.93 ? 277  GLN   A O     1 
ATOM   1959  C  CB    . GLN   A  1  279  ? -43.039 75.253  88.788  1.00 17.32 ? 277  GLN   A CB    1 
ATOM   1960  C  CG    . GLN   A  1  279  ? -41.661 75.753  89.189  1.00 18.68 ? 277  GLN   A CG    1 
ATOM   1961  C  CD    . GLN   A  1  279  ? -41.733 77.131  89.783  1.00 20.78 ? 277  GLN   A CD    1 
ATOM   1962  O  OE1   . GLN   A  1  279  ? -42.531 77.966  89.358  1.00 31.90 ? 277  GLN   A OE1   1 
ATOM   1963  N  NE2   . GLN   A  1  279  ? -40.934 77.369  90.811  1.00 20.09 ? 277  GLN   A NE2   1 
ATOM   1964  N  N     . ALA   A  1  280  ? -46.167 74.076  90.352  1.00 16.55 ? 278  ALA   A N     1 
ATOM   1965  C  CA    . ALA   A  1  280  ? -47.431 73.497  89.903  1.00 17.06 ? 278  ALA   A CA    1 
ATOM   1966  C  C     . ALA   A  1  280  ? -48.359 74.539  89.302  1.00 18.07 ? 278  ALA   A C     1 
ATOM   1967  O  O     . ALA   A  1  280  ? -49.071 74.243  88.340  1.00 16.67 ? 278  ALA   A O     1 
ATOM   1968  C  CB    . ALA   A  1  280  ? -48.126 72.772  91.050  1.00 18.96 ? 278  ALA   A CB    1 
ATOM   1969  N  N     . ALA   A  1  281  ? -48.393 75.753  89.853  1.00 17.78 ? 279  ALA   A N     1 
ATOM   1970  C  CA    . ALA   A  1  281  ? -49.276 76.773  89.292  1.00 18.60 ? 279  ALA   A CA    1 
ATOM   1971  C  C     . ALA   A  1  281  ? -48.889 77.105  87.856  1.00 18.12 ? 279  ALA   A C     1 
ATOM   1972  O  O     . ALA   A  1  281  ? -49.762 77.242  86.985  1.00 19.17 ? 279  ALA   A O     1 
ATOM   1973  C  CB    . ALA   A  1  281  ? -49.292 78.030  90.168  1.00 21.73 ? 279  ALA   A CB    1 
ATOM   1974  N  N     . ARG   A  1  282  ? -47.590 77.218  87.580  1.00 16.70 ? 280  ARG   A N     1 
ATOM   1975  C  CA    . ARG   A  1  282  ? -47.171 77.443  86.198  1.00 17.53 ? 280  ARG   A CA    1 
ATOM   1976  C  C     . ARG   A  1  282  ? -47.486 76.237  85.328  1.00 16.98 ? 280  ARG   A C     1 
ATOM   1977  O  O     . ARG   A  1  282  ? -47.838 76.388  84.153  1.00 17.14 ? 280  ARG   A O     1 
ATOM   1978  C  CB    . ARG   A  1  282  ? -45.678 77.758  86.121  1.00 19.72 ? 280  ARG   A CB    1 
ATOM   1979  C  CG    . ARG   A  1  282  ? -45.300 79.095  86.702  1.00 20.94 ? 280  ARG   A CG    1 
ATOM   1980  C  CD    . ARG   A  1  282  ? -43.850 79.399  86.340  1.00 20.17 ? 280  ARG   A CD    1 
ATOM   1981  N  NE    . ARG   A  1  282  ? -43.746 79.566  84.898  1.00 18.87 ? 280  ARG   A NE    1 
ATOM   1982  C  CZ    . ARG   A  1  282  ? -42.615 79.543  84.211  1.00 19.51 ? 280  ARG   A CZ    1 
ATOM   1983  N  NH1   . ARG   A  1  282  ? -41.441 79.387  84.813  1.00 19.27 ? 280  ARG   A NH1   1 
ATOM   1984  N  NH2   . ARG   A  1  282  ? -42.660 79.688  82.892  1.00 21.74 ? 280  ARG   A NH2   1 
ATOM   1985  N  N     . VAL   A  1  283  ? -47.344 75.033  85.871  1.00 16.17 ? 281  VAL   A N     1 
ATOM   1986  C  CA    . VAL   A  1  283  ? -47.658 73.830  85.108  1.00 16.22 ? 281  VAL   A CA    1 
ATOM   1987  C  C     . VAL   A  1  283  ? -49.127 73.832  84.703  1.00 16.47 ? 281  VAL   A C     1 
ATOM   1988  O  O     . VAL   A  1  283  ? -49.472 73.627  83.533  1.00 16.24 ? 281  VAL   A O     1 
ATOM   1989  C  CB    . VAL   A  1  283  ? -47.297 72.581  85.927  1.00 15.44 ? 281  VAL   A CB    1 
ATOM   1990  C  CG1   . VAL   A  1  283  ? -47.856 71.332  85.257  1.00 18.89 ? 281  VAL   A CG1   1 
ATOM   1991  C  CG2   . VAL   A  1  283  ? -45.793 72.495  86.059  1.00 16.85 ? 281  VAL   A CG2   1 
ATOM   1992  N  N     . MET   A  1  284  ? -50.016 74.093  85.654  1.00 16.00 ? 282  MET   A N     1 
ATOM   1993  C  CA    . MET   A  1  284  ? -51.437 74.099  85.320  1.00 17.41 ? 282  MET   A CA    1 
ATOM   1994  C  C     . MET   A  1  284  ? -51.792 75.256  84.404  1.00 17.92 ? 282  MET   A C     1 
ATOM   1995  O  O     . MET   A  1  284  ? -52.694 75.127  83.567  1.00 20.73 ? 282  MET   A O     1 
ATOM   1996  C  CB    . MET   A  1  284  ? -52.278 74.143  86.596  1.00 16.53 ? 282  MET   A CB    1 
ATOM   1997  C  CG    . MET   A  1  284  ? -52.021 72.957  87.512  1.00 19.43 ? 282  MET   A CG    1 
ATOM   1998  S  SD    . MET   A  1  284  ? -52.205 71.333  86.736  1.00 21.05 ? 282  MET   A SD    1 
ATOM   1999  C  CE    . MET   A  1  284  ? -53.951 71.320  86.343  1.00 22.43 ? 282  MET   A CE    1 
ATOM   2000  N  N     . GLY   A  1  285  ? -51.109 76.384  84.536  1.00 17.41 ? 283  GLY   A N     1 
ATOM   2001  C  CA    . GLY   A  1  285  ? -51.485 77.552  83.778  1.00 18.50 ? 283  GLY   A CA    1 
ATOM   2002  C  C     . GLY   A  1  285  ? -50.895 77.554  82.388  1.00 18.50 ? 283  GLY   A C     1 
ATOM   2003  O  O     . GLY   A  1  285  ? -51.495 78.093  81.453  1.00 20.55 ? 283  GLY   A O     1 
ATOM   2004  N  N     . GLU   A  1  286  ? -49.729 76.949  82.232  1.00 17.63 ? 284  GLU   A N     1 
ATOM   2005  C  CA    . GLU   A  1  286  ? -48.954 77.067  81.007  1.00 17.52 ? 284  GLU   A CA    1 
ATOM   2006  C  C     . GLU   A  1  286  ? -48.764 75.748  80.290  1.00 17.35 ? 284  GLU   A C     1 
ATOM   2007  O  O     . GLU   A  1  286  ? -48.814 75.709  79.056  1.00 19.97 ? 284  GLU   A O     1 
ATOM   2008  C  CB    . GLU   A  1  286  ? -47.575 77.668  81.311  1.00 17.15 ? 284  GLU   A CB    1 
ATOM   2009  C  CG    . GLU   A  1  286  ? -47.641 79.033  81.961  1.00 20.06 ? 284  GLU   A CG    1 
ATOM   2010  C  CD    . GLU   A  1  286  ? -46.297 79.481  82.506  1.00 21.97 ? 284  GLU   A CD    1 
ATOM   2011  O  OE1   . GLU   A  1  286  ? -45.269 79.098  81.924  1.00 23.19 ? 284  GLU   A OE1   1 
ATOM   2012  O  OE2   . GLU   A  1  286  ? -46.275 80.218  83.517  1.00 24.97 ? 284  GLU   A OE2   1 
ATOM   2013  N  N     . LEU   A  1  287  ? -48.501 74.667  81.016  1.00 16.00 ? 285  LEU   A N     1 
ATOM   2014  C  CA    . LEU   A  1  287  ? -48.294 73.379  80.378  1.00 15.93 ? 285  LEU   A CA    1 
ATOM   2015  C  C     . LEU   A  1  287  ? -49.628 72.776  79.968  1.00 17.62 ? 285  LEU   A C     1 
ATOM   2016  O  O     . LEU   A  1  287  ? -49.778 72.289  78.843  1.00 17.27 ? 285  LEU   A O     1 
ATOM   2017  C  CB    . LEU   A  1  287  ? -47.547 72.444  81.339  1.00 17.19 ? 285  LEU   A CB    1 
ATOM   2018  C  CG    . LEU   A  1  287  ? -46.670 71.340  80.750  1.00 21.75 ? 285  LEU   A CG    1 
ATOM   2019  C  CD1   . LEU   A  1  287  ? -45.987 70.572  81.854  1.00 22.70 ? 285  LEU   A CD1   1 
ATOM   2020  C  CD2   . LEU   A  1  287  ? -47.461 70.392  79.909  1.00 24.18 ? 285  LEU   A CD2   1 
ATOM   2021  N  N     . LEU   A  1  288  ? -50.601 72.790  80.871  1.00 16.80 ? 286  LEU   A N     1 
ATOM   2022  C  CA    . LEU   A  1  288  ? -51.901 72.189  80.589  1.00 17.79 ? 286  LEU   A CA    1 
ATOM   2023  C  C     . LEU   A  1  288  ? -52.517 72.664  79.276  1.00 17.85 ? 286  LEU   A C     1 
ATOM   2024  O  O     . LEU   A  1  288  ? -52.926 71.809  78.474  1.00 17.46 ? 286  LEU   A O     1 
ATOM   2025  C  CB    . LEU   A  1  288  ? -52.822 72.363  81.804  1.00 20.94 ? 286  LEU   A CB    1 
ATOM   2026  C  CG    . LEU   A  1  288  ? -54.287 72.017  81.544  1.00 24.66 ? 286  LEU   A CG    1 
ATOM   2027  C  CD1   . LEU   A  1  288  ? -54.435 70.537  81.246  1.00 22.70 ? 286  LEU   A CD1   1 
ATOM   2028  C  CD2   . LEU   A  1  288  ? -55.128 72.434  82.744  1.00 32.63 ? 286  LEU   A CD2   1 
ATOM   2029  N  N     . PRO   A  1  289  ? -52.604 73.965  78.980  1.00 16.90 ? 287  PRO   A N     1 
ATOM   2030  C  CA    . PRO   A  1  289  ? -53.191 74.367  77.691  1.00 17.38 ? 287  PRO   A CA    1 
ATOM   2031  C  C     . PRO   A  1  289  ? -52.458 73.807  76.497  1.00 18.32 ? 287  PRO   A C     1 
ATOM   2032  O  O     . PRO   A  1  289  ? -53.079 73.575  75.453  1.00 16.36 ? 287  PRO   A O     1 
ATOM   2033  C  CB    . PRO   A  1  289  ? -53.103 75.897  77.727  1.00 19.68 ? 287  PRO   A CB    1 
ATOM   2034  C  CG    . PRO   A  1  289  ? -53.060 76.232  79.185  1.00 23.06 ? 287  PRO   A CG    1 
ATOM   2035  C  CD    . PRO   A  1  289  ? -52.266 75.132  79.813  1.00 19.34 ? 287  PRO   A CD    1 
ATOM   2036  N  N     . ARG   A  1  290  ? -51.150 73.614  76.600  1.00 15.22 ? 288  ARG   A N     1 
ATOM   2037  C  CA    . ARG   A  1  290  ? -50.408 73.021  75.495  1.00 16.12 ? 288  ARG   A CA    1 
ATOM   2038  C  C     . ARG   A  1  290  ? -50.794 71.572  75.290  1.00 15.17 ? 288  ARG   A C     1 
ATOM   2039  O  O     . ARG   A  1  290  ? -50.989 71.132  74.149  1.00 15.60 ? 288  ARG   A O     1 
ATOM   2040  C  CB    . ARG   A  1  290  ? -48.905 73.151  75.729  1.00 17.25 ? 288  ARG   A CB    1 
ATOM   2041  C  CG    . ARG   A  1  290  ? -48.480 74.580  75.767  1.00 19.33 ? 288  ARG   A CG    1 
ATOM   2042  C  CD    . ARG   A  1  290  ? -47.057 74.712  76.255  1.00 23.43 ? 288  ARG   A CD    1 
ATOM   2043  N  NE    . ARG   A  1  290  ? -46.718 76.119  76.404  1.00 25.77 ? 288  ARG   A NE    1 
ATOM   2044  C  CZ    . ARG   A  1  290  ? -45.725 76.565  77.159  1.00 25.28 ? 288  ARG   A CZ    1 
ATOM   2045  N  NH1   . ARG   A  1  290  ? -44.936 75.734  77.819  1.00 23.07 ? 288  ARG   A NH1   1 
ATOM   2046  N  NH2   . ARG   A  1  290  ? -45.529 77.877  77.261  1.00 31.81 ? 288  ARG   A NH2   1 
ATOM   2047  N  N     . VAL   A  1  291  ? -50.897 70.804  76.370  1.00 14.60 ? 289  VAL   A N     1 
ATOM   2048  C  CA    . VAL   A  1  291  ? -51.357 69.429  76.224  1.00 15.36 ? 289  VAL   A CA    1 
ATOM   2049  C  C     . VAL   A  1  291  ? -52.765 69.403  75.666  1.00 15.03 ? 289  VAL   A C     1 
ATOM   2050  O  O     . VAL   A  1  291  ? -53.091 68.566  74.818  1.00 15.70 ? 289  VAL   A O     1 
ATOM   2051  C  CB    . VAL   A  1  291  ? -51.286 68.680  77.562  1.00 15.26 ? 289  VAL   A CB    1 
ATOM   2052  C  CG1   . VAL   A  1  291  ? -51.646 67.233  77.347  1.00 17.18 ? 289  VAL   A CG1   1 
ATOM   2053  C  CG2   . VAL   A  1  291  ? -49.901 68.781  78.112  1.00 18.10 ? 289  VAL   A CG2   1 
ATOM   2054  N  N     . LYS   A  1  292  ? -53.619 70.303  76.142  1.00 14.73 ? 290  LYS   A N     1 
ATOM   2055  C  CA    . LYS   A  1  292  ? -54.983 70.324  75.645  1.00 13.89 ? 290  LYS   A CA    1 
ATOM   2056  C  C     . LYS   A  1  292  ? -55.004 70.587  74.152  1.00 17.20 ? 290  LYS   A C     1 
ATOM   2057  O  O     . LYS   A  1  292  ? -55.766 69.953  73.415  1.00 14.55 ? 290  LYS   A O     1 
ATOM   2058  C  CB    . LYS   A  1  292  ? -55.802 71.378  76.375  1.00 15.77 ? 290  LYS   A CB    1 
ATOM   2059  C  CG    . LYS   A  1  292  ? -57.210 71.494  75.799  1.00 17.06 ? 290  LYS   A CG    1 
ATOM   2060  C  CD    . LYS   A  1  292  ? -58.078 72.505  76.494  1.00 18.90 ? 290  LYS   A CD    1 
ATOM   2061  C  CE    . LYS   A  1  292  ? -59.444 72.525  75.824  1.00 18.55 ? 290  LYS   A CE    1 
ATOM   2062  N  NZ    . LYS   A  1  292  ? -60.380 73.376  76.601  1.00 18.81 ? 290  LYS   A NZ    1 
ATOM   2063  N  N     . ALA   A  1  293  ? -54.169 71.512  73.682  1.00 14.22 ? 291  ALA   A N     1 
ATOM   2064  C  CA    . ALA   A  1  293  ? -54.178 71.811  72.254  1.00 15.55 ? 291  ALA   A CA    1 
ATOM   2065  C  C     . ALA   A  1  293  ? -53.720 70.608  71.438  1.00 14.08 ? 291  ALA   A C     1 
ATOM   2066  O  O     . ALA   A  1  293  ? -54.284 70.315  70.372  1.00 15.44 ? 291  ALA   A O     1 
ATOM   2067  C  CB    . ALA   A  1  293  ? -53.308 73.042  71.986  1.00 15.28 ? 291  ALA   A CB    1 
ATOM   2068  N  N     . LEU   A  1  294  ? -52.697 69.896  71.905  1.00 14.13 ? 292  LEU   A N     1 
ATOM   2069  C  CA    . LEU   A  1  294  ? -52.280 68.684  71.212  1.00 14.62 ? 292  LEU   A CA    1 
ATOM   2070  C  C     . LEU   A  1  294  ? -53.368 67.627  71.282  1.00 15.22 ? 292  LEU   A C     1 
ATOM   2071  O  O     . LEU   A  1  294  ? -53.636 66.937  70.294  1.00 14.49 ? 292  LEU   A O     1 
ATOM   2072  C  CB    . LEU   A  1  294  ? -50.988 68.149  71.833  1.00 16.01 ? 292  LEU   A CB    1 
ATOM   2073  C  CG    . LEU   A  1  294  ? -49.778 69.063  71.719  1.00 14.57 ? 292  LEU   A CG    1 
ATOM   2074  C  CD1   . LEU   A  1  294  ? -48.634 68.490  72.529  1.00 16.44 ? 292  LEU   A CD1   1 
ATOM   2075  C  CD2   . LEU   A  1  294  ? -49.363 69.204  70.257  1.00 16.03 ? 292  LEU   A CD2   1 
ATOM   2076  N  N     . ALA   A  1  295  ? -54.044 67.519  72.429  1.00 13.74 ? 293  ALA   A N     1 
ATOM   2077  C  CA    . ALA   A  1  295  ? -55.103 66.526  72.558  1.00 14.83 ? 293  ALA   A CA    1 
ATOM   2078  C  C     . ALA   A  1  295  ? -56.279 66.842  71.646  1.00 14.93 ? 293  ALA   A C     1 
ATOM   2079  O  O     . ALA   A  1  295  ? -56.890 65.930  71.089  1.00 15.17 ? 293  ALA   A O     1 
ATOM   2080  C  CB    . ALA   A  1  295  ? -55.551 66.427  74.016  1.00 15.51 ? 293  ALA   A CB    1 
ATOM   2081  N  N     . LEU   A  1  296  ? -56.604 68.120  71.480  1.00 14.22 ? 294  LEU   A N     1 
ATOM   2082  C  CA    . LEU   A  1  296  ? -57.679 68.495  70.569  1.00 15.01 ? 294  LEU   A CA    1 
ATOM   2083  C  C     . LEU   A  1  296  ? -57.361 68.064  69.152  1.00 15.54 ? 294  LEU   A C     1 
ATOM   2084  O  O     . LEU   A  1  296  ? -58.250 67.632  68.410  1.00 14.63 ? 294  LEU   A O     1 
ATOM   2085  C  CB    . LEU   A  1  296  ? -57.912 70.002  70.613  1.00 15.24 ? 294  LEU   A CB    1 
ATOM   2086  C  CG    . LEU   A  1  296  ? -58.611 70.513  71.865  1.00 16.14 ? 294  LEU   A CG    1 
ATOM   2087  C  CD1   . LEU   A  1  296  ? -58.519 72.022  71.923  1.00 17.21 ? 294  LEU   A CD1   1 
ATOM   2088  C  CD2   . LEU   A  1  296  ? -60.079 70.090  71.871  1.00 20.03 ? 294  LEU   A CD2   1 
ATOM   2089  N  N     . LEU   A  1  297  ? -56.099 68.180  68.754  1.00 14.85 ? 295  LEU   A N     1 
ATOM   2090  C  CA    . LEU   A  1  297  ? -55.729 67.750  67.412  1.00 15.49 ? 295  LEU   A CA    1 
ATOM   2091  C  C     . LEU   A  1  297  ? -55.772 66.234  67.306  1.00 14.51 ? 295  LEU   A C     1 
ATOM   2092  O  O     . LEU   A  1  297  ? -56.248 65.693  66.303  1.00 15.85 ? 295  LEU   A O     1 
ATOM   2093  C  CB    . LEU   A  1  297  ? -54.345 68.296  67.043  1.00 18.17 ? 295  LEU   A CB    1 
ATOM   2094  C  CG    . LEU   A  1  297  ? -53.971 68.155  65.558  1.00 20.39 ? 295  LEU   A CG    1 
ATOM   2095  C  CD1   . LEU   A  1  297  ? -54.925 68.923  64.631  1.00 22.80 ? 295  LEU   A CD1   1 
ATOM   2096  C  CD2   . LEU   A  1  297  ? -52.538 68.627  65.389  1.00 24.30 ? 295  LEU   A CD2   1 
ATOM   2097  N  N     . ALA   A  1  298  ? -55.286 65.527  68.333  1.00 13.85 ? 296  ALA   A N     1 
ATOM   2098  C  CA    . ALA   A  1  298  ? -55.383 64.074  68.315  1.00 14.67 ? 296  ALA   A CA    1 
ATOM   2099  C  C     . ALA   A  1  298  ? -56.835 63.632  68.255  1.00 15.43 ? 296  ALA   A C     1 
ATOM   2100  O  O     . ALA   A  1  298  ? -57.167 62.662  67.565  1.00 15.94 ? 296  ALA   A O     1 
ATOM   2101  C  CB    . ALA   A  1  298  ? -54.693 63.481  69.544  1.00 16.17 ? 296  ALA   A CB    1 
ATOM   2102  N  N     . LYS   A  1  299  ? -57.713 64.333  68.980  1.00 14.36 ? 297  LYS   A N     1 
ATOM   2103  C  CA    A LYS   A  1  299  ? -59.142 64.050  68.908  0.56 15.26 ? 297  LYS   A CA    1 
ATOM   2104  C  CA    B LYS   A  1  299  ? -59.140 64.047  68.908  0.44 15.27 ? 297  LYS   A CA    1 
ATOM   2105  C  C     . LYS   A  1  299  ? -59.660 64.221  67.489  1.00 15.88 ? 297  LYS   A C     1 
ATOM   2106  O  O     . LYS   A  1  299  ? -60.430 63.389  66.998  1.00 16.93 ? 297  LYS   A O     1 
ATOM   2107  C  CB    A LYS   A  1  299  ? -59.902 64.969  69.865  0.56 14.87 ? 297  LYS   A CB    1 
ATOM   2108  C  CB    B LYS   A  1  299  ? -59.886 64.964  69.875  0.44 14.89 ? 297  LYS   A CB    1 
ATOM   2109  C  CG    A LYS   A  1  299  ? -61.378 65.133  69.514  0.56 16.52 ? 297  LYS   A CG    1 
ATOM   2110  C  CG    B LYS   A  1  299  ? -61.385 65.014  69.663  0.44 16.55 ? 297  LYS   A CG    1 
ATOM   2111  C  CD    A LYS   A  1  299  ? -62.138 65.960  70.546  0.56 17.48 ? 297  LYS   A CD    1 
ATOM   2112  C  CD    B LYS   A  1  299  ? -62.070 65.749  70.806  0.44 16.98 ? 297  LYS   A CD    1 
ATOM   2113  C  CE    A LYS   A  1  299  ? -63.502 66.382  70.006  0.56 16.56 ? 297  LYS   A CE    1 
ATOM   2114  C  CE    B LYS   A  1  299  ? -63.503 66.086  70.452  0.44 19.44 ? 297  LYS   A CE    1 
ATOM   2115  N  NZ    A LYS   A  1  299  ? -64.336 67.019  71.062  0.56 18.60 ? 297  LYS   A NZ    1 
ATOM   2116  N  NZ    B LYS   A  1  299  ? -63.595 67.006  69.299  0.44 21.76 ? 297  LYS   A NZ    1 
ATOM   2117  N  N     . ASN   A  1  300  ? -59.239 65.285  66.806  1.00 15.39 ? 298  ASN   A N     1 
ATOM   2118  C  CA    . ASN   A  1  300  ? -59.798 65.509  65.482  1.00 14.99 ? 298  ASN   A CA    1 
ATOM   2119  C  C     . ASN   A  1  300  ? -59.401 64.413  64.503  1.00 17.25 ? 298  ASN   A C     1 
ATOM   2120  O  O     . ASN   A  1  300  ? -60.212 64.012  63.656  1.00 19.11 ? 298  ASN   A O     1 
ATOM   2121  C  CB    . ASN   A  1  300  ? -59.426 66.877  64.942  1.00 17.86 ? 298  ASN   A CB    1 
ATOM   2122  C  CG    . ASN   A  1  300  ? -60.227 67.213  63.716  1.00 25.10 ? 298  ASN   A CG    1 
ATOM   2123  O  OD1   . ASN   A  1  300  ? -61.395 67.611  63.810  1.00 30.21 ? 298  ASN   A OD1   1 
ATOM   2124  N  ND2   . ASN   A  1  300  ? -59.639 67.006  62.558  1.00 23.19 ? 298  ASN   A ND2   1 
ATOM   2125  N  N     . TYR   A  1  301  ? -58.179 63.904  64.612  1.00 15.99 ? 299  TYR   A N     1 
ATOM   2126  C  CA    . TYR   A  1  301  ? -57.749 62.792  63.785  1.00 15.82 ? 299  TYR   A CA    1 
ATOM   2127  C  C     . TYR   A  1  301  ? -58.148 61.440  64.354  1.00 16.36 ? 299  TYR   A C     1 
ATOM   2128  O  O     . TYR   A  1  301  ? -57.972 60.426  63.669  1.00 18.53 ? 299  TYR   A O     1 
ATOM   2129  C  CB    . TYR   A  1  301  ? -56.234 62.829  63.631  1.00 15.84 ? 299  TYR   A CB    1 
ATOM   2130  C  CG    . TYR   A  1  301  ? -55.703 63.908  62.732  1.00 15.94 ? 299  TYR   A CG    1 
ATOM   2131  C  CD1   . TYR   A  1  301  ? -55.894 63.848  61.358  1.00 18.43 ? 299  TYR   A CD1   1 
ATOM   2132  C  CD2   . TYR   A  1  301  ? -54.953 64.952  63.243  1.00 16.20 ? 299  TYR   A CD2   1 
ATOM   2133  C  CE1   . TYR   A  1  301  ? -55.355 64.812  60.524  1.00 17.97 ? 299  TYR   A CE1   1 
ATOM   2134  C  CE2   . TYR   A  1  301  ? -54.414 65.917  62.429  1.00 17.57 ? 299  TYR   A CE2   1 
ATOM   2135  C  CZ    . TYR   A  1  301  ? -54.617 65.849  61.060  1.00 18.12 ? 299  TYR   A CZ    1 
ATOM   2136  O  OH    . TYR   A  1  301  ? -54.063 66.813  60.240  1.00 18.29 ? 299  TYR   A OH    1 
ATOM   2137  N  N     . ASP   A  1  302  ? -58.644 61.403  65.589  1.00 16.14 ? 300  ASP   A N     1 
ATOM   2138  C  CA    . ASP   A  1  302  ? -58.997 60.173  66.291  1.00 15.44 ? 300  ASP   A CA    1 
ATOM   2139  C  C     . ASP   A  1  302  ? -57.807 59.228  66.396  1.00 15.51 ? 300  ASP   A C     1 
ATOM   2140  O  O     . ASP   A  1  302  ? -57.860 58.062  66.000  1.00 17.55 ? 300  ASP   A O     1 
ATOM   2141  C  CB    . ASP   A  1  302  ? -60.218 59.465  65.691  1.00 16.11 ? 300  ASP   A CB    1 
ATOM   2142  C  CG    . ASP   A  1  302  ? -60.870 58.535  66.680  1.00 20.71 ? 300  ASP   A CG    1 
ATOM   2143  O  OD1   . ASP   A  1  302  ? -60.831 58.852  67.885  1.00 19.44 ? 300  ASP   A OD1   1 
ATOM   2144  O  OD2   . ASP   A  1  302  ? -61.410 57.486  66.271  1.00 21.47 ? 300  ASP   A OD2   1 
ATOM   2145  N  N     . ILE   A  1  303  ? -56.730 59.751  66.974  1.00 14.46 ? 301  ILE   A N     1 
ATOM   2146  C  CA    . ILE   A  1  303  ? -55.538 58.967  67.268  1.00 15.44 ? 301  ILE   A CA    1 
ATOM   2147  C  C     . ILE   A  1  303  ? -55.298 58.979  68.768  1.00 15.85 ? 301  ILE   A C     1 
ATOM   2148  O  O     . ILE   A  1  303  ? -55.804 59.829  69.501  1.00 14.97 ? 301  ILE   A O     1 
ATOM   2149  C  CB    . ILE   A  1  303  ? -54.277 59.457  66.531  1.00 16.25 ? 301  ILE   A CB    1 
ATOM   2150  C  CG1   . ILE   A  1  303  ? -53.802 60.811  67.064  1.00 15.66 ? 301  ILE   A CG1   1 
ATOM   2151  C  CG2   . ILE   A  1  303  ? -54.550 59.550  65.029  1.00 17.41 ? 301  ILE   A CG2   1 
ATOM   2152  C  CD1   . ILE   A  1  303  ? -52.439 61.217  66.518  1.00 16.68 ? 301  ILE   A CD1   1 
ATOM   2153  N  N     . GLY   A  1  304  ? -54.502 58.015  69.218  1.00 15.76 ? 302  GLY   A N     1 
ATOM   2154  C  CA    . GLY   A  1  304  ? -54.107 57.980  70.621  1.00 16.40 ? 302  GLY   A CA    1 
ATOM   2155  C  C     . GLY   A  1  304  ? -53.071 59.051  70.930  1.00 15.13 ? 302  GLY   A C     1 
ATOM   2156  O  O     . GLY   A  1  304  ? -52.230 59.394  70.099  1.00 14.64 ? 302  GLY   A O     1 
ATOM   2157  N  N     . LEU   A  1  305  ? -53.159 59.606  72.134  1.00 14.14 ? 303  LEU   A N     1 
ATOM   2158  C  CA    . LEU   A  1  305  ? -52.158 60.534  72.648  1.00 14.51 ? 303  LEU   A CA    1 
ATOM   2159  C  C     . LEU   A  1  305  ? -51.843 60.083  74.062  1.00 14.52 ? 303  LEU   A C     1 
ATOM   2160  O  O     . LEU   A  1  305  ? -52.686 60.219  74.952  1.00 15.07 ? 303  LEU   A O     1 
ATOM   2161  C  CB    . LEU   A  1  305  ? -52.687 61.967  72.645  1.00 16.04 ? 303  LEU   A CB    1 
ATOM   2162  C  CG    . LEU   A  1  305  ? -51.641 63.007  73.069  1.00 18.84 ? 303  LEU   A CG    1 
ATOM   2163  C  CD1   . LEU   A  1  305  ? -51.843 64.301  72.335  1.00 21.62 ? 303  LEU   A CD1   1 
ATOM   2164  C  CD2   . LEU   A  1  305  ? -51.649 63.281  74.558  1.00 25.49 ? 303  LEU   A CD2   1 
ATOM   2165  N  N     . ASN   A  1  306  ? -50.644 59.551  74.265  1.00 15.15 ? 304  ASN   A N     1 
ATOM   2166  C  CA    . ASN   A  1  306  ? -50.252 58.951  75.526  1.00 14.99 ? 304  ASN   A CA    1 
ATOM   2167  C  C     . ASN   A  1  306  ? -49.294 59.878  76.258  1.00 14.76 ? 304  ASN   A C     1 
ATOM   2168  O  O     . ASN   A  1  306  ? -48.341 60.391  75.664  1.00 15.41 ? 304  ASN   A O     1 
ATOM   2169  C  CB    . ASN   A  1  306  ? -49.537 57.636  75.266  1.00 14.95 ? 304  ASN   A CB    1 
ATOM   2170  C  CG    . ASN   A  1  306  ? -48.908 57.092  76.506  1.00 16.61 ? 304  ASN   A CG    1 
ATOM   2171  O  OD1   . ASN   A  1  306  ? -47.707 57.288  76.760  1.00 19.36 ? 304  ASN   A OD1   1 
ATOM   2172  N  ND2   . ASN   A  1  306  ? -49.705 56.424  77.303  1.00 15.84 ? 304  ASN   A ND2   1 
ATOM   2173  N  N     . ILE   A  1  307  ? -49.521 60.045  77.557  1.00 14.60 ? 305  ILE   A N     1 
ATOM   2174  C  CA    . ILE   A  1  307  ? -48.602 60.774  78.425  1.00 15.53 ? 305  ILE   A CA    1 
ATOM   2175  C  C     . ILE   A  1  307  ? -47.648 59.774  79.061  1.00 13.89 ? 305  ILE   A C     1 
ATOM   2176  O  O     . ILE   A  1  307  ? -48.047 58.965  79.910  1.00 14.19 ? 305  ILE   A O     1 
ATOM   2177  C  CB    . ILE   A  1  307  ? -49.358 61.572  79.489  1.00 15.62 ? 305  ILE   A CB    1 
ATOM   2178  C  CG1   . ILE   A  1  307  ? -50.239 62.614  78.804  1.00 17.47 ? 305  ILE   A CG1   1 
ATOM   2179  C  CG2   . ILE   A  1  307  ? -48.364 62.219  80.458  1.00 18.14 ? 305  ILE   A CG2   1 
ATOM   2180  C  CD1   . ILE   A  1  307  ? -51.154 63.341  79.760  1.00 21.51 ? 305  ILE   A CD1   1 
ATOM   2181  N  N     . ASP   A  1  308  ? -46.380 59.824  78.659  1.00 15.26 ? 306  ASP   A N     1 
ATOM   2182  C  CA    . ASP   A  1  308  ? -45.364 58.943  79.217  1.00 14.02 ? 306  ASP   A CA    1 
ATOM   2183  C  C     . ASP   A  1  308  ? -45.109 59.302  80.679  1.00 14.61 ? 306  ASP   A C     1 
ATOM   2184  O  O     . ASP   A  1  308  ? -45.306 60.440  81.100  1.00 15.31 ? 306  ASP   A O     1 
ATOM   2185  C  CB    . ASP   A  1  308  ? -44.048 59.123  78.453  1.00 15.73 ? 306  ASP   A CB    1 
ATOM   2186  C  CG    . ASP   A  1  308  ? -44.061 58.503  77.061  1.00 20.26 ? 306  ASP   A CG    1 
ATOM   2187  O  OD1   . ASP   A  1  308  ? -44.995 57.755  76.706  1.00 18.65 ? 306  ASP   A OD1   1 
ATOM   2188  O  OD2   . ASP   A  1  308  ? -43.089 58.747  76.309  1.00 21.03 ? 306  ASP   A OD2   1 
ATOM   2189  N  N     . ALA   A  1  309  ? -44.702 58.310  81.465  1.00 14.25 ? 307  ALA   A N     1 
ATOM   2190  C  CA    . ALA   A  1  309  ? -44.419 58.526  82.878  1.00 14.88 ? 307  ALA   A CA    1 
ATOM   2191  C  C     . ALA   A  1  309  ? -42.935 58.780  83.082  1.00 14.10 ? 307  ALA   A C     1 
ATOM   2192  O  O     . ALA   A  1  309  ? -42.084 58.115  82.482  1.00 15.50 ? 307  ALA   A O     1 
ATOM   2193  C  CB    . ALA   A  1  309  ? -44.836 57.328  83.714  1.00 15.93 ? 307  ALA   A CB    1 
ATOM   2194  N  N     . GLU   A  1  310  ? -42.638 59.725  83.964  1.00 13.99 ? 308  GLU   A N     1 
ATOM   2195  C  CA    . GLU   A  1  310  ? -41.258 60.150  84.154  1.00 14.10 ? 308  GLU   A CA    1 
ATOM   2196  C  C     . GLU   A  1  310  ? -40.808 59.880  85.583  1.00 14.33 ? 308  GLU   A C     1 
ATOM   2197  O  O     . GLU   A  1  310  ? -41.098 58.811  86.122  1.00 15.53 ? 308  GLU   A O     1 
ATOM   2198  C  CB    . GLU   A  1  310  ? -41.120 61.593  83.695  1.00 15.42 ? 308  GLU   A CB    1 
ATOM   2199  C  CG    . GLU   A  1  310  ? -41.484 61.731  82.197  1.00 16.90 ? 308  GLU   A CG    1 
ATOM   2200  C  CD    . GLU   A  1  310  ? -41.217 63.114  81.665  1.00 17.65 ? 308  GLU   A CD    1 
ATOM   2201  O  OE1   . GLU   A  1  310  ? -40.025 63.435  81.435  1.00 20.14 ? 308  GLU   A OE1   1 
ATOM   2202  O  OE2   . GLU   A  1  310  ? -42.195 63.873  81.476  1.00 17.33 ? 308  GLU   A OE2   1 
ATOM   2203  N  N     . GLU   A  1  311  ? -40.121 60.829  86.205  1.00 14.96 ? 309  GLU   A N     1 
ATOM   2204  C  CA    . GLU   A  1  311  ? -39.604 60.605  87.545  1.00 16.01 ? 309  GLU   A CA    1 
ATOM   2205  C  C     . GLU   A  1  311  ? -40.734 60.499  88.561  1.00 14.83 ? 309  GLU   A C     1 
ATOM   2206  O  O     . GLU   A  1  311  ? -41.848 61.004  88.375  1.00 15.46 ? 309  GLU   A O     1 
ATOM   2207  C  CB    . GLU   A  1  311  ? -38.702 61.760  87.954  1.00 16.33 ? 309  GLU   A CB    1 
ATOM   2208  C  CG    . GLU   A  1  311  ? -37.412 61.854  87.145  1.00 17.77 ? 309  GLU   A CG    1 
ATOM   2209  C  CD    . GLU   A  1  311  ? -37.546 62.725  85.916  1.00 21.80 ? 309  GLU   A CD    1 
ATOM   2210  O  OE1   . GLU   A  1  311  ? -38.672 63.040  85.494  1.00 16.77 ? 309  GLU   A OE1   1 
ATOM   2211  O  OE2   . GLU   A  1  311  ? -36.499 63.110  85.359  1.00 27.67 ? 309  GLU   A OE2   1 
ATOM   2212  N  N     . ALA   A  1  312  ? -40.419 59.853  89.681  1.00 15.12 ? 310  ALA   A N     1 
ATOM   2213  C  CA    . ALA   A  1  312  ? -41.437 59.607  90.691  1.00 14.64 ? 310  ALA   A CA    1 
ATOM   2214  C  C     . ALA   A  1  312  ? -42.029 60.899  91.240  1.00 14.58 ? 310  ALA   A C     1 
ATOM   2215  O  O     . ALA   A  1  312  ? -43.214 60.939  91.583  1.00 15.79 ? 310  ALA   A O     1 
ATOM   2216  C  CB    . ALA   A  1  312  ? -40.844 58.763  91.820  1.00 15.78 ? 310  ALA   A CB    1 
ATOM   2217  N  N     . ASP   A  1  313  ? -41.236 61.972  91.317  1.00 15.46 ? 311  ASP   A N     1 
ATOM   2218  C  CA    . ASP   A  1  313  ? -41.749 63.226  91.860  1.00 16.19 ? 311  ASP   A CA    1 
ATOM   2219  C  C     . ASP   A  1  313  ? -42.618 64.000  90.884  1.00 14.50 ? 311  ASP   A C     1 
ATOM   2220  O  O     . ASP   A  1  313  ? -43.069 65.097  91.230  1.00 17.20 ? 311  ASP   A O     1 
ATOM   2221  C  CB    . ASP   A  1  313  ? -40.643 64.109  92.459  1.00 19.06 ? 311  ASP   A CB    1 
ATOM   2222  C  CG    . ASP   A  1  313  ? -39.659 64.626  91.422  1.00 21.57 ? 311  ASP   A CG    1 
ATOM   2223  O  OD1   . ASP   A  1  313  ? -39.834 64.377  90.212  1.00 19.49 ? 311  ASP   A OD1   1 
ATOM   2224  O  OD2   . ASP   A  1  313  ? -38.693 65.305  91.840  1.00 25.27 ? 311  ASP   A OD2   1 
ATOM   2225  N  N     . ARG   A  1  314  ? -42.881 63.440  89.710  1.00 14.47 ? 312  ARG   A N     1 
ATOM   2226  C  CA    . ARG   A  1  314  ? -43.774 64.035  88.742  1.00 14.97 ? 312  ARG   A CA    1 
ATOM   2227  C  C     . ARG   A  1  314  ? -45.061 63.253  88.592  1.00 15.33 ? 312  ARG   A C     1 
ATOM   2228  O  O     . ARG   A  1  314  ? -46.001 63.754  87.965  1.00 15.56 ? 312  ARG   A O     1 
ATOM   2229  C  CB    . ARG   A  1  314  ? -43.071 64.131  87.383  1.00 15.49 ? 312  ARG   A CB    1 
ATOM   2230  C  CG    . ARG   A  1  314  ? -42.085 65.286  87.361  1.00 16.70 ? 312  ARG   A CG    1 
ATOM   2231  C  CD    . ARG   A  1  314  ? -41.078 65.174  86.256  1.00 18.34 ? 312  ARG   A CD    1 
ATOM   2232  N  NE    . ARG   A  1  314  ? -40.509 66.486  85.994  1.00 19.41 ? 312  ARG   A NE    1 
ATOM   2233  C  CZ    . ARG   A  1  314  ? -39.521 66.696  85.140  1.00 16.76 ? 312  ARG   A CZ    1 
ATOM   2234  N  NH1   . ARG   A  1  314  ? -38.927 65.691  84.525  1.00 17.26 ? 312  ARG   A NH1   1 
ATOM   2235  N  NH2   . ARG   A  1  314  ? -39.135 67.946  84.887  1.00 18.87 ? 312  ARG   A NH2   1 
ATOM   2236  N  N     . LEU   A  1  315  ? -45.144 62.060  89.183  1.00 14.80 ? 313  LEU   A N     1 
ATOM   2237  C  CA    . LEU   A  1  315  ? -46.336 61.225  89.031  1.00 15.46 ? 313  LEU   A CA    1 
ATOM   2238  C  C     . LEU   A  1  315  ? -47.598 61.967  89.450  1.00 15.87 ? 313  LEU   A C     1 
ATOM   2239  O  O     . LEU   A  1  315  ? -48.546 62.114  88.668  1.00 15.53 ? 313  LEU   A O     1 
ATOM   2240  C  CB    . LEU   A  1  315  ? -46.178 59.970  89.877  1.00 16.56 ? 313  LEU   A CB    1 
ATOM   2241  C  CG    . LEU   A  1  315  ? -46.992 58.748  89.449  1.00 17.84 ? 313  LEU   A CG    1 
ATOM   2242  C  CD1   . LEU   A  1  315  ? -46.622 57.552  90.303  1.00 16.65 ? 313  LEU   A CD1   1 
ATOM   2243  C  CD2   . LEU   A  1  315  ? -48.486 58.957  89.506  1.00 19.71 ? 313  LEU   A CD2   1 
ATOM   2244  N  N     . GLU   A  1  316  ? -47.655 62.397  90.707  1.00 15.70 ? 314  GLU   A N     1 
ATOM   2245  C  CA    . GLU   A  1  316  ? -48.906 62.950  91.205  1.00 15.63 ? 314  GLU   A CA    1 
ATOM   2246  C  C     . GLU   A  1  316  ? -49.252 64.259  90.512  1.00 17.57 ? 314  GLU   A C     1 
ATOM   2247  O  O     . GLU   A  1  316  ? -50.420 64.508  90.206  1.00 17.46 ? 314  GLU   A O     1 
ATOM   2248  C  CB    . GLU   A  1  316  ? -48.875 63.047  92.727  1.00 16.56 ? 314  GLU   A CB    1 
ATOM   2249  C  CG    . GLU   A  1  316  ? -48.945 61.649  93.328  1.00 18.30 ? 314  GLU   A CG    1 
ATOM   2250  C  CD    . GLU   A  1  316  ? -48.919 61.635  94.832  1.00 18.62 ? 314  GLU   A CD    1 
ATOM   2251  O  OE1   . GLU   A  1  316  ? -49.647 62.437  95.429  1.00 20.40 ? 314  GLU   A OE1   1 
ATOM   2252  O  OE2   . GLU   A  1  316  ? -48.167 60.825  95.410  1.00 19.19 ? 314  GLU   A OE2   1 
ATOM   2253  N  N     . LEU   A  1  317  ? -48.249 65.075  90.186  1.00 16.71 ? 315  LEU   A N     1 
ATOM   2254  C  CA    . LEU   A  1  317  ? -48.513 66.291  89.425  1.00 17.72 ? 315  LEU   A CA    1 
ATOM   2255  C  C     . LEU   A  1  317  ? -49.163 65.967  88.082  1.00 16.71 ? 315  LEU   A C     1 
ATOM   2256  O  O     . LEU   A  1  317  ? -50.118 66.636  87.659  1.00 16.83 ? 315  LEU   A O     1 
ATOM   2257  C  CB    . LEU   A  1  317  ? -47.201 67.031  89.207  1.00 19.41 ? 315  LEU   A CB    1 
ATOM   2258  C  CG    . LEU   A  1  317  ? -47.318 68.310  88.379  1.00 19.70 ? 315  LEU   A CG    1 
ATOM   2259  C  CD1   . LEU   A  1  317  ? -48.328 69.277  89.010  1.00 23.84 ? 315  LEU   A CD1   1 
ATOM   2260  C  CD2   . LEU   A  1  317  ? -45.951 68.955  88.243  1.00 23.33 ? 315  LEU   A CD2   1 
ATOM   2261  N  N     . SER   A  1  318  ? -48.682 64.923  87.410  1.00 14.69 ? 316  SER   A N     1 
ATOM   2262  C  CA    . SER   A  1  318  ? -49.239 64.577  86.107  1.00 15.55 ? 316  SER   A CA    1 
ATOM   2263  C  C     . SER   A  1  318  ? -50.692 64.173  86.227  1.00 15.85 ? 316  SER   A C     1 
ATOM   2264  O  O     . SER   A  1  318  ? -51.469 64.371  85.283  1.00 15.44 ? 316  SER   A O     1 
ATOM   2265  C  CB    . SER   A  1  318  ? -48.431 63.466  85.439  1.00 14.49 ? 316  SER   A CB    1 
ATOM   2266  O  OG    . SER   A  1  318  ? -48.662 62.217  86.063  1.00 15.62 ? 316  SER   A OG    1 
ATOM   2267  N  N     . LEU   A  1  319  ? -51.082 63.628  87.379  1.00 15.90 ? 317  LEU   A N     1 
ATOM   2268  C  CA    . LEU   A  1  319  ? -52.480 63.265  87.585  1.00 16.10 ? 317  LEU   A CA    1 
ATOM   2269  C  C     . LEU   A  1  319  ? -53.386 64.482  87.583  1.00 16.81 ? 317  LEU   A C     1 
ATOM   2270  O  O     . LEU   A  1  319  ? -54.547 64.386  87.171  1.00 16.81 ? 317  LEU   A O     1 
ATOM   2271  C  CB    . LEU   A  1  319  ? -52.652 62.510  88.900  1.00 17.74 ? 317  LEU   A CB    1 
ATOM   2272  C  CG    . LEU   A  1  319  ? -51.964 61.150  88.935  1.00 16.92 ? 317  LEU   A CG    1 
ATOM   2273  C  CD1   . LEU   A  1  319  ? -52.138 60.540  90.334  1.00 18.61 ? 317  LEU   A CD1   1 
ATOM   2274  C  CD2   . LEU   A  1  319  ? -52.488 60.205  87.875  1.00 17.95 ? 317  LEU   A CD2   1 
ATOM   2275  N  N     . ASP   A  1  320  ? -52.895 65.626  88.048  1.00 17.28 ? 318  ASP   A N     1 
ATOM   2276  C  CA    . ASP   A  1  320  ? -53.712 66.829  87.996  1.00 18.75 ? 318  ASP   A CA    1 
ATOM   2277  C  C     . ASP   A  1  320  ? -53.987 67.255  86.568  1.00 18.39 ? 318  ASP   A C     1 
ATOM   2278  O  O     . ASP   A  1  320  ? -55.086 67.735  86.264  1.00 19.67 ? 318  ASP   A O     1 
ATOM   2279  C  CB    . ASP   A  1  320  ? -53.069 67.941  88.812  1.00 18.91 ? 318  ASP   A CB    1 
ATOM   2280  C  CG    . ASP   A  1  320  ? -53.224 67.703  90.286  1.00 22.08 ? 318  ASP   A CG    1 
ATOM   2281  O  OD1   . ASP   A  1  320  ? -54.397 67.569  90.714  1.00 24.27 ? 318  ASP   A OD1   1 
ATOM   2282  O  OD2   . ASP   A  1  320  ? -52.192 67.607  90.992  1.00 26.29 ? 318  ASP   A OD2   1 
ATOM   2283  N  N     . LEU   A  1  321  ? -53.024 67.056  85.673  1.00 17.10 ? 319  LEU   A N     1 
ATOM   2284  C  CA    . LEU   A  1  321  ? -53.281 67.349  84.272  1.00 16.47 ? 319  LEU   A CA    1 
ATOM   2285  C  C     . LEU   A  1  321  ? -54.227 66.325  83.670  1.00 17.11 ? 319  LEU   A C     1 
ATOM   2286  O  O     . LEU   A  1  321  ? -55.138 66.687  82.917  1.00 17.20 ? 319  LEU   A O     1 
ATOM   2287  C  CB    . LEU   A  1  321  ? -51.978 67.384  83.482  1.00 16.80 ? 319  LEU   A CB    1 
ATOM   2288  C  CG    . LEU   A  1  321  ? -51.141 68.640  83.705  1.00 20.34 ? 319  LEU   A CG    1 
ATOM   2289  C  CD1   . LEU   A  1  321  ? -50.206 68.466  84.874  1.00 23.52 ? 319  LEU   A CD1   1 
ATOM   2290  C  CD2   . LEU   A  1  321  ? -50.357 68.997  82.434  1.00 24.94 ? 319  LEU   A CD2   1 
ATOM   2291  N  N     . LEU   A  1  322  ? -54.014 65.043  83.971  1.00 16.42 ? 320  LEU   A N     1 
ATOM   2292  C  CA    . LEU   A  1  322  ? -54.898 64.015  83.437  1.00 17.26 ? 320  LEU   A CA    1 
ATOM   2293  C  C     . LEU   A  1  322  ? -56.329 64.272  83.867  1.00 17.04 ? 320  LEU   A C     1 
ATOM   2294  O  O     . LEU   A  1  322  ? -57.253 64.162  83.056  1.00 17.30 ? 320  LEU   A O     1 
ATOM   2295  C  CB    . LEU   A  1  322  ? -54.440 62.642  83.912  1.00 16.86 ? 320  LEU   A CB    1 
ATOM   2296  C  CG    . LEU   A  1  322  ? -55.290 61.484  83.386  1.00 17.63 ? 320  LEU   A CG    1 
ATOM   2297  C  CD1   . LEU   A  1  322  ? -55.091 61.279  81.903  1.00 17.61 ? 320  LEU   A CD1   1 
ATOM   2298  C  CD2   . LEU   A  1  322  ? -54.935 60.219  84.160  1.00 16.84 ? 320  LEU   A CD2   1 
ATOM   2299  N  N     . GLU   A  1  323  ? -56.522 64.673  85.121  1.00 15.87 ? 321  GLU   A N     1 
ATOM   2300  C  CA    . GLU   A  1  323  ? -57.862 64.958  85.634  1.00 18.30 ? 321  GLU   A CA    1 
ATOM   2301  C  C     . GLU   A  1  323  ? -58.525 66.075  84.842  1.00 18.65 ? 321  GLU   A C     1 
ATOM   2302  O  O     . GLU   A  1  323  ? -59.664 65.926  84.374  1.00 18.17 ? 321  GLU   A O     1 
ATOM   2303  C  CB    . GLU   A  1  323  ? -57.787 65.334  87.112  1.00 19.10 ? 321  GLU   A CB    1 
ATOM   2304  C  CG    . GLU   A  1  323  ? -59.086 65.898  87.685  1.00 24.35 ? 321  GLU   A CG    1 
ATOM   2305  C  CD    . GLU   A  1  323  ? -59.808 64.927  88.595  1.00 26.39 ? 321  GLU   A CD    1 
ATOM   2306  O  OE1   . GLU   A  1  323  ? -59.233 63.882  88.929  1.00 27.44 ? 321  GLU   A OE1   1 
ATOM   2307  O  OE2   . GLU   A  1  323  ? -60.969 65.202  88.967  1.00 28.47 ? 321  GLU   A OE2   1 
ATOM   2308  N  N     . VAL   A  1  324  ? -57.837 67.210  84.686  1.00 16.91 ? 322  VAL   A N     1 
ATOM   2309  C  CA    . VAL   A  1  324  ? -58.441 68.338  83.988  1.00 17.42 ? 322  VAL   A CA    1 
ATOM   2310  C  C     . VAL   A  1  324  ? -58.753 67.965  82.549  1.00 16.64 ? 322  VAL   A C     1 
ATOM   2311  O  O     . VAL   A  1  324  ? -59.826 68.287  82.031  1.00 16.90 ? 322  VAL   A O     1 
ATOM   2312  C  CB    . VAL   A  1  324  ? -57.541 69.583  84.067  1.00 18.63 ? 322  VAL   A CB    1 
ATOM   2313  C  CG1   . VAL   A  1  324  ? -58.153 70.713  83.231  1.00 20.82 ? 322  VAL   A CG1   1 
ATOM   2314  C  CG2   . VAL   A  1  324  ? -57.373 70.027  85.496  1.00 19.77 ? 322  VAL   A CG2   1 
ATOM   2315  N  N     . LEU   A  1  325  ? -57.836 67.260  81.888  1.00 15.60 ? 323  LEU   A N     1 
ATOM   2316  C  CA    . LEU   A  1  325  ? -58.060 66.926  80.483  1.00 15.69 ? 323  LEU   A CA    1 
ATOM   2317  C  C     . LEU   A  1  325  ? -59.250 65.996  80.332  1.00 15.48 ? 323  LEU   A C     1 
ATOM   2318  O  O     . LEU   A  1  325  ? -60.088 66.181  79.441  1.00 15.43 ? 323  LEU   A O     1 
ATOM   2319  C  CB    . LEU   A  1  325  ? -56.817 66.276  79.892  1.00 16.56 ? 323  LEU   A CB    1 
ATOM   2320  C  CG    . LEU   A  1  325  ? -55.630 67.235  79.765  1.00 17.38 ? 323  LEU   A CG    1 
ATOM   2321  C  CD1   . LEU   A  1  325  ? -54.339 66.428  79.642  1.00 19.07 ? 323  LEU   A CD1   1 
ATOM   2322  C  CD2   . LEU   A  1  325  ? -55.829 68.163  78.584  1.00 18.44 ? 323  LEU   A CD2   1 
ATOM   2323  N  N     . CYS   A  1  326  ? -59.352 64.996  81.202  1.00 16.02 ? 324  CYS   A N     1 
ATOM   2324  C  CA    . CYS   A  1  326  ? -60.444 64.044  81.065  1.00 15.62 ? 324  CYS   A CA    1 
ATOM   2325  C  C     . CYS   A  1  326  ? -61.790 64.649  81.418  1.00 17.49 ? 324  CYS   A C     1 
ATOM   2326  O  O     . CYS   A  1  326  ? -62.815 64.132  80.968  1.00 18.35 ? 324  CYS   A O     1 
ATOM   2327  C  CB    . CYS   A  1  326  ? -60.190 62.804  81.912  1.00 16.68 ? 324  CYS   A CB    1 
ATOM   2328  S  SG    . CYS   A  1  326  ? -58.852 61.783  81.259  1.00 19.35 ? 324  CYS   A SG    1 
ATOM   2329  N  N     . LEU   A  1  327  ? -61.816 65.712  82.212  1.00 16.54 ? 325  LEU   A N     1 
ATOM   2330  C  CA    . LEU   A  1  327  ? -63.055 66.393  82.554  1.00 16.32 ? 325  LEU   A CA    1 
ATOM   2331  C  C     . LEU   A  1  327  ? -63.372 67.542  81.611  1.00 17.64 ? 325  LEU   A C     1 
ATOM   2332  O  O     . LEU   A  1  327  ? -64.432 68.153  81.740  1.00 18.46 ? 325  LEU   A O     1 
ATOM   2333  C  CB    . LEU   A  1  327  ? -63.003 66.902  83.994  1.00 17.33 ? 325  LEU   A CB    1 
ATOM   2334  C  CG    . LEU   A  1  327  ? -62.868 65.794  85.041  1.00 21.90 ? 325  LEU   A CG    1 
ATOM   2335  C  CD1   . LEU   A  1  327  ? -62.735 66.409  86.431  1.00 24.58 ? 325  LEU   A CD1   1 
ATOM   2336  C  CD2   . LEU   A  1  327  ? -64.034 64.826  84.992  1.00 25.38 ? 325  LEU   A CD2   1 
ATOM   2337  N  N     . ASP   A  1  328  ? -62.502 67.826  80.651  1.00 16.18 ? 326  ASP   A N     1 
ATOM   2338  C  CA    . ASP   A  1  328  ? -62.680 68.974  79.772  1.00 16.97 ? 326  ASP   A CA    1 
ATOM   2339  C  C     . ASP   A  1  328  ? -63.627 68.601  78.642  1.00 18.00 ? 326  ASP   A C     1 
ATOM   2340  O  O     . ASP   A  1  328  ? -63.295 67.757  77.806  1.00 16.41 ? 326  ASP   A O     1 
ATOM   2341  C  CB    . ASP   A  1  328  ? -61.324 69.386  79.206  1.00 17.50 ? 326  ASP   A CB    1 
ATOM   2342  C  CG    . ASP   A  1  328  ? -61.379 70.709  78.491  1.00 20.60 ? 326  ASP   A CG    1 
ATOM   2343  O  OD1   . ASP   A  1  328  ? -62.364 70.968  77.774  1.00 20.83 ? 326  ASP   A OD1   1 
ATOM   2344  O  OD2   . ASP   A  1  328  ? -60.453 71.517  78.667  1.00 24.63 ? 326  ASP   A OD2   1 
ATOM   2345  N  N     . GLY   A  1  329  ? -64.786 69.263  78.598  1.00 17.06 ? 327  GLY   A N     1 
ATOM   2346  C  CA    . GLY   A  1  329  ? -65.799 68.925  77.605  1.00 17.17 ? 327  GLY   A CA    1 
ATOM   2347  C  C     . GLY   A  1  329  ? -65.333 69.098  76.175  1.00 19.29 ? 327  GLY   A C     1 
ATOM   2348  O  O     . GLY   A  1  329  ? -65.846 68.436  75.273  1.00 16.83 ? 327  GLY   A O     1 
ATOM   2349  N  N     . ASP   A  1  330  ? -64.338 69.957  75.945  1.00 17.78 ? 328  ASP   A N     1 
ATOM   2350  C  CA    . ASP   A  1  330  ? -63.850 70.149  74.585  1.00 18.54 ? 328  ASP   A CA    1 
ATOM   2351  C  C     . ASP   A  1  330  ? -63.210 68.888  74.022  1.00 15.75 ? 328  ASP   A C     1 
ATOM   2352  O  O     . ASP   A  1  330  ? -63.115 68.748  72.799  1.00 17.40 ? 328  ASP   A O     1 
ATOM   2353  C  CB    . ASP   A  1  330  ? -62.822 71.273  74.521  1.00 18.57 ? 328  ASP   A CB    1 
ATOM   2354  C  CG    . ASP   A  1  330  ? -63.426 72.631  74.742  1.00 25.06 ? 328  ASP   A CG    1 
ATOM   2355  O  OD1   . ASP   A  1  330  ? -64.642 72.799  74.524  1.00 27.22 ? 328  ASP   A OD1   1 
ATOM   2356  O  OD2   . ASP   A  1  330  ? -62.671 73.538  75.121  1.00 21.75 ? 328  ASP   A OD2   1 
ATOM   2357  N  N     . LEU   A  1  331  ? -62.792 67.960  74.881  1.00 15.34 ? 329  LEU   A N     1 
ATOM   2358  C  CA    . LEU   A  1  331  ? -62.161 66.730  74.437  1.00 15.59 ? 329  LEU   A CA    1 
ATOM   2359  C  C     . LEU   A  1  331  ? -63.127 65.567  74.400  1.00 15.86 ? 329  LEU   A C     1 
ATOM   2360  O  O     . LEU   A  1  331  ? -62.718 64.440  74.120  1.00 17.39 ? 329  LEU   A O     1 
ATOM   2361  C  CB    . LEU   A  1  331  ? -60.966 66.398  75.333  1.00 15.76 ? 329  LEU   A CB    1 
ATOM   2362  C  CG    . LEU   A  1  331  ? -59.764 67.319  75.118  1.00 15.61 ? 329  LEU   A CG    1 
ATOM   2363  C  CD1   . LEU   A  1  331  ? -58.749 67.121  76.211  1.00 16.64 ? 329  LEU   A CD1   1 
ATOM   2364  C  CD2   . LEU   A  1  331  ? -59.131 67.064  73.765  1.00 18.14 ? 329  LEU   A CD2   1 
ATOM   2365  N  N     . SER   A  1  332  ? -64.404 65.811  74.673  1.00 16.85 ? 330  SER   A N     1 
ATOM   2366  C  CA    . SER   A  1  332  ? -65.326 64.694  74.797  1.00 18.87 ? 330  SER   A CA    1 
ATOM   2367  C  C     . SER   A  1  332  ? -65.560 64.042  73.443  1.00 16.90 ? 330  SER   A C     1 
ATOM   2368  O  O     . SER   A  1  332  ? -65.386 64.660  72.385  1.00 19.77 ? 330  SER   A O     1 
ATOM   2369  C  CB    . SER   A  1  332  ? -66.653 65.154  75.383  1.00 19.19 ? 330  SER   A CB    1 
ATOM   2370  O  OG    . SER   A  1  332  ? -67.335 65.979  74.470  1.00 22.23 ? 330  SER   A OG    1 
ATOM   2371  N  N     . GLY   A  1  333  ? -65.904 62.765  73.485  1.00 16.62 ? 331  GLY   A N     1 
ATOM   2372  C  CA    . GLY   A  1  333  ? -66.124 62.007  72.278  1.00 17.18 ? 331  GLY   A CA    1 
ATOM   2373  C  C     . GLY   A  1  333  ? -64.900 61.280  71.784  1.00 17.25 ? 331  GLY   A C     1 
ATOM   2374  O  O     . GLY   A  1  333  ? -65.002 60.484  70.843  1.00 20.95 ? 331  GLY   A O     1 
ATOM   2375  N  N     . TRP   A  1  334  ? -63.752 61.505  72.408  1.00 16.55 ? 332  TRP   A N     1 
ATOM   2376  C  CA    . TRP   A  1  334  ? -62.495 60.910  71.994  1.00 16.49 ? 332  TRP   A CA    1 
ATOM   2377  C  C     . TRP   A  1  334  ? -61.964 60.098  73.158  1.00 15.92 ? 332  TRP   A C     1 
ATOM   2378  O  O     . TRP   A  1  334  ? -61.866 60.610  74.276  1.00 17.08 ? 332  TRP   A O     1 
ATOM   2379  C  CB    . TRP   A  1  334  ? -61.525 62.032  71.664  1.00 16.99 ? 332  TRP   A CB    1 
ATOM   2380  C  CG    . TRP   A  1  334  ? -60.103 61.663  71.478  1.00 16.04 ? 332  TRP   A CG    1 
ATOM   2381  C  CD1   . TRP   A  1  334  ? -59.569 60.911  70.476  1.00 15.77 ? 332  TRP   A CD1   1 
ATOM   2382  C  CD2   . TRP   A  1  334  ? -59.017 62.124  72.271  1.00 15.54 ? 332  TRP   A CD2   1 
ATOM   2383  N  NE1   . TRP   A  1  334  ? -58.195 60.862  70.608  1.00 16.26 ? 332  TRP   A NE1   1 
ATOM   2384  C  CE2   . TRP   A  1  334  ? -57.834 61.599  71.706  1.00 15.01 ? 332  TRP   A CE2   1 
ATOM   2385  C  CE3   . TRP   A  1  334  ? -58.925 62.921  73.418  1.00 16.59 ? 332  TRP   A CE3   1 
ATOM   2386  C  CZ2   . TRP   A  1  334  ? -56.570 61.844  72.250  1.00 15.44 ? 332  TRP   A CZ2   1 
ATOM   2387  C  CZ3   . TRP   A  1  334  ? -57.670 63.165  73.955  1.00 17.62 ? 332  TRP   A CZ3   1 
ATOM   2388  C  CH2   . TRP   A  1  334  ? -56.507 62.631  73.369  1.00 16.76 ? 332  TRP   A CH2   1 
ATOM   2389  N  N     . ASN   A  1  335  ? -61.610 58.843  72.895  1.00 15.23 ? 333  ASN   A N     1 
ATOM   2390  C  CA    . ASN   A  1  335  ? -61.085 57.945  73.913  1.00 15.78 ? 333  ASN   A CA    1 
ATOM   2391  C  C     . ASN   A  1  335  ? -59.591 57.724  73.762  1.00 16.55 ? 333  ASN   A C     1 
ATOM   2392  O  O     . ASN   A  1  335  ? -59.059 56.761  74.309  1.00 16.15 ? 333  ASN   A O     1 
ATOM   2393  C  CB    . ASN   A  1  335  ? -61.791 56.592  73.864  1.00 18.23 ? 333  ASN   A CB    1 
ATOM   2394  C  CG    . ASN   A  1  335  ? -63.141 56.624  74.516  1.00 19.68 ? 333  ASN   A CG    1 
ATOM   2395  O  OD1   . ASN   A  1  335  ? -63.393 57.408  75.431  1.00 17.76 ? 333  ASN   A OD1   1 
ATOM   2396  N  ND2   . ASN   A  1  335  ? -64.030 55.751  74.051  1.00 22.94 ? 333  ASN   A ND2   1 
ATOM   2397  N  N     . GLY   A  1  336  ? -58.916 58.587  73.006  1.00 15.61 ? 334  GLY   A N     1 
ATOM   2398  C  CA    . GLY   A  1  336  ? -57.514 58.379  72.740  1.00 14.24 ? 334  GLY   A CA    1 
ATOM   2399  C  C     . GLY   A  1  336  ? -56.549 58.862  73.803  1.00 15.21 ? 334  GLY   A C     1 
ATOM   2400  O  O     . GLY   A  1  336  ? -55.356 58.593  73.657  1.00 15.35 ? 334  GLY   A O     1 
ATOM   2401  N  N     . MET   A  1  337  ? -56.999 59.556  74.848  1.00 14.44 ? 335  MET   A N     1 
ATOM   2402  C  CA    A MET   A  1  337  ? -56.071 59.987  75.888  0.57 15.40 ? 335  MET   A CA    1 
ATOM   2403  C  CA    B MET   A  1  337  ? -56.069 59.984  75.886  0.43 15.42 ? 335  MET   A CA    1 
ATOM   2404  C  C     . MET   A  1  337  ? -55.503 58.774  76.615  1.00 14.76 ? 335  MET   A C     1 
ATOM   2405  O  O     . MET   A  1  337  ? -56.249 57.905  77.087  1.00 16.30 ? 335  MET   A O     1 
ATOM   2406  C  CB    A MET   A  1  337  ? -56.771 60.916  76.873  0.57 17.47 ? 335  MET   A CB    1 
ATOM   2407  C  CB    B MET   A  1  337  ? -56.756 60.910  76.876  0.43 17.46 ? 335  MET   A CB    1 
ATOM   2408  C  CG    A MET   A  1  337  ? -55.843 61.572  77.860  0.57 19.01 ? 335  MET   A CG    1 
ATOM   2409  C  CG    B MET   A  1  337  ? -55.914 61.228  78.085  0.43 20.49 ? 335  MET   A CG    1 
ATOM   2410  S  SD    A MET   A  1  337  ? -54.775 62.765  77.054  0.57 25.22 ? 335  MET   A SD    1 
ATOM   2411  S  SD    B MET   A  1  337  ? -55.931 62.991  78.372  0.43 20.69 ? 335  MET   A SD    1 
ATOM   2412  C  CE    A MET   A  1  337  ? -55.841 64.201  76.939  0.57 24.32 ? 335  MET   A CE    1 
ATOM   2413  C  CE    B MET   A  1  337  ? -55.234 63.548  76.819  0.43 15.95 ? 335  MET   A CE    1 
ATOM   2414  N  N     . GLY   A  1  338  ? -54.178 58.720  76.714  1.00 15.17 ? 336  GLY   A N     1 
ATOM   2415  C  CA    . GLY   A  1  338  ? -53.507 57.604  77.339  1.00 16.42 ? 336  GLY   A CA    1 
ATOM   2416  C  C     . GLY   A  1  338  ? -52.546 58.091  78.404  1.00 16.09 ? 336  GLY   A C     1 
ATOM   2417  O  O     . GLY   A  1  338  ? -52.165 59.257  78.438  1.00 14.74 ? 336  GLY   A O     1 
ATOM   2418  N  N     . PHE   A  1  339  ? -52.208 57.186  79.308  1.00 14.70 ? 337  PHE   A N     1 
ATOM   2419  C  CA    . PHE   A  1  339  ? -51.408 57.560  80.465  1.00 15.02 ? 337  PHE   A CA    1 
ATOM   2420  C  C     . PHE   A  1  339  ? -50.652 56.342  80.958  1.00 15.96 ? 337  PHE   A C     1 
ATOM   2421  O  O     . PHE   A  1  339  ? -51.228 55.257  81.097  1.00 15.81 ? 337  PHE   A O     1 
ATOM   2422  C  CB    . PHE   A  1  339  ? -52.366 58.054  81.547  1.00 14.76 ? 337  PHE   A CB    1 
ATOM   2423  C  CG    . PHE   A  1  339  ? -51.696 58.710  82.718  1.00 15.59 ? 337  PHE   A CG    1 
ATOM   2424  C  CD1   . PHE   A  1  339  ? -51.415 60.071  82.694  1.00 16.63 ? 337  PHE   A CD1   1 
ATOM   2425  C  CD2   . PHE   A  1  339  ? -51.387 57.979  83.855  1.00 15.00 ? 337  PHE   A CD2   1 
ATOM   2426  C  CE1   . PHE   A  1  339  ? -50.834 60.681  83.792  1.00 16.87 ? 337  PHE   A CE1   1 
ATOM   2427  C  CE2   . PHE   A  1  339  ? -50.797 58.594  84.956  1.00 18.38 ? 337  PHE   A CE2   1 
ATOM   2428  C  CZ    . PHE   A  1  339  ? -50.525 59.937  84.914  1.00 17.52 ? 337  PHE   A CZ    1 
ATOM   2429  N  N     . VAL   A  1  340  ? -49.370 56.517  81.195  1.00 15.46 ? 338  VAL   A N     1 
ATOM   2430  C  CA    . VAL   A  1  340  ? -48.505 55.437  81.646  1.00 14.43 ? 338  VAL   A CA    1 
ATOM   2431  C  C     . VAL   A  1  340  ? -48.503 55.365  83.160  1.00 13.81 ? 338  VAL   A C     1 
ATOM   2432  O  O     . VAL   A  1  340  ? -48.463 56.391  83.850  1.00 15.52 ? 338  VAL   A O     1 
ATOM   2433  C  CB    . VAL   A  1  340  ? -47.077 55.682  81.150  1.00 14.84 ? 338  VAL   A CB    1 
ATOM   2434  C  CG1   . VAL   A  1  340  ? -46.140 54.589  81.672  1.00 16.13 ? 338  VAL   A CG1   1 
ATOM   2435  C  CG2   . VAL   A  1  340  ? -47.071 55.724  79.647  1.00 16.58 ? 338  VAL   A CG2   1 
ATOM   2436  N  N     . VAL   A  1  341  ? -48.517 54.151  83.688  1.00 14.73 ? 339  VAL   A N     1 
ATOM   2437  C  CA    A VAL   A  1  341  ? -48.278 53.920  85.107  0.38 15.41 ? 339  VAL   A CA    1 
ATOM   2438  C  CA    B VAL   A  1  341  ? -48.272 53.925  85.103  0.62 15.39 ? 339  VAL   A CA    1 
ATOM   2439  C  C     . VAL   A  1  341  ? -47.141 52.923  85.249  1.00 15.57 ? 339  VAL   A C     1 
ATOM   2440  O  O     . VAL   A  1  341  ? -47.074 51.927  84.516  1.00 16.90 ? 339  VAL   A O     1 
ATOM   2441  C  CB    A VAL   A  1  341  ? -49.535 53.450  85.864  0.38 17.05 ? 339  VAL   A CB    1 
ATOM   2442  C  CB    B VAL   A  1  341  ? -49.529 53.464  85.854  0.62 17.05 ? 339  VAL   A CB    1 
ATOM   2443  C  CG1   A VAL   A  1  341  ? -50.599 54.529  85.816  0.38 16.99 ? 339  VAL   A CG1   1 
ATOM   2444  C  CG1   B VAL   A  1  341  ? -49.315 53.650  87.328  0.62 18.33 ? 339  VAL   A CG1   1 
ATOM   2445  C  CG2   A VAL   A  1  341  ? -50.051 52.153  85.283  0.38 16.69 ? 339  VAL   A CG2   1 
ATOM   2446  C  CG2   B VAL   A  1  341  ? -50.720 54.269  85.388  0.62 16.69 ? 339  VAL   A CG2   1 
ATOM   2447  N  N     . GLN   A  1  342  ? -46.245 53.206  86.186  1.00 15.12 ? 340  GLN   A N     1 
ATOM   2448  C  CA    . GLN   A  1  342  ? -45.009 52.451  86.369  1.00 15.26 ? 340  GLN   A CA    1 
ATOM   2449  C  C     . GLN   A  1  342  ? -45.171 51.471  87.525  1.00 15.52 ? 340  GLN   A C     1 
ATOM   2450  O  O     . GLN   A  1  342  ? -45.287 51.878  88.687  1.00 17.18 ? 340  GLN   A O     1 
ATOM   2451  C  CB    . GLN   A  1  342  ? -43.849 53.408  86.633  1.00 14.57 ? 340  GLN   A CB    1 
ATOM   2452  C  CG    . GLN   A  1  342  ? -43.600 54.403  85.497  1.00 14.57 ? 340  GLN   A CG    1 
ATOM   2453  C  CD    . GLN   A  1  342  ? -43.023 55.695  85.995  1.00 15.08 ? 340  GLN   A CD    1 
ATOM   2454  O  OE1   . GLN   A  1  342  ? -43.524 56.289  86.948  1.00 15.57 ? 340  GLN   A OE1   1 
ATOM   2455  N  NE2   . GLN   A  1  342  ? -41.968 56.158  85.341  1.00 14.59 ? 340  GLN   A NE2   1 
ATOM   2456  N  N     . ALA   A  1  343  ? -45.151 50.179  87.198  1.00 14.78 ? 341  ALA   A N     1 
ATOM   2457  C  CA    . ALA   A  1  343  ? -45.357 49.140  88.202  1.00 16.68 ? 341  ALA   A CA    1 
ATOM   2458  C  C     . ALA   A  1  343  ? -44.179 49.005  89.157  1.00 18.44 ? 341  ALA   A C     1 
ATOM   2459  O  O     . ALA   A  1  343  ? -44.334 48.405  90.227  1.00 18.04 ? 341  ALA   A O     1 
ATOM   2460  C  CB    . ALA   A  1  343  ? -45.608 47.803  87.523  1.00 18.88 ? 341  ALA   A CB    1 
ATOM   2461  N  N     . TYR   A  1  344  ? -43.012 49.553  88.821  1.00 16.75 ? 342  TYR   A N     1 
ATOM   2462  C  CA    . TYR   A  1  344  ? -41.956 49.575  89.820  1.00 16.17 ? 342  TYR   A CA    1 
ATOM   2463  C  C     . TYR   A  1  344  ? -42.241 50.554  90.940  1.00 19.17 ? 342  TYR   A C     1 
ATOM   2464  O  O     . TYR   A  1  344  ? -41.495 50.577  91.919  1.00 19.17 ? 342  TYR   A O     1 
ATOM   2465  C  CB    . TYR   A  1  344  ? -40.563 49.771  89.204  1.00 16.51 ? 342  TYR   A CB    1 
ATOM   2466  C  CG    . TYR   A  1  344  ? -40.139 51.148  88.700  1.00 14.73 ? 342  TYR   A CG    1 
ATOM   2467  C  CD1   . TYR   A  1  344  ? -40.983 52.246  88.657  1.00 15.64 ? 342  TYR   A CD1   1 
ATOM   2468  C  CD2   . TYR   A  1  344  ? -38.831 51.317  88.243  1.00 15.83 ? 342  TYR   A CD2   1 
ATOM   2469  C  CE1   . TYR   A  1  344  ? -40.532 53.470  88.160  1.00 16.20 ? 342  TYR   A CE1   1 
ATOM   2470  C  CE2   . TYR   A  1  344  ? -38.378 52.512  87.759  1.00 16.37 ? 342  TYR   A CE2   1 
ATOM   2471  C  CZ    . TYR   A  1  344  ? -39.211 53.588  87.716  1.00 15.96 ? 342  TYR   A CZ    1 
ATOM   2472  O  OH    . TYR   A  1  344  ? -38.723 54.771  87.223  1.00 15.48 ? 342  TYR   A OH    1 
ATOM   2473  N  N     . GLY   A  1  345  ? -43.294 51.355  90.823  1.00 16.70 ? 343  GLY   A N     1 
ATOM   2474  C  CA    . GLY   A  1  345  ? -43.600 52.343  91.829  1.00 17.18 ? 343  GLY   A CA    1 
ATOM   2475  C  C     . GLY   A  1  345  ? -44.594 51.806  92.845  1.00 17.98 ? 343  GLY   A C     1 
ATOM   2476  O  O     . GLY   A  1  345  ? -45.544 51.101  92.502  1.00 17.86 ? 343  GLY   A O     1 
ATOM   2477  N  N     . LYS   A  1  346  ? -44.358 52.169  94.104  1.00 17.46 ? 344  LYS   A N     1 
ATOM   2478  C  CA    . LYS   A  1  346  ? -45.202 51.696  95.189  1.00 17.28 ? 344  LYS   A CA    1 
ATOM   2479  C  C     . LYS   A  1  346  ? -46.621 52.234  95.109  1.00 19.08 ? 344  LYS   A C     1 
ATOM   2480  O  O     . LYS   A  1  346  ? -47.534 51.635  95.682  1.00 19.18 ? 344  LYS   A O     1 
ATOM   2481  C  CB    . LYS   A  1  346  ? -44.575 52.074  96.525  1.00 18.24 ? 344  LYS   A CB    1 
ATOM   2482  C  CG    . LYS   A  1  346  ? -43.221 51.436  96.728  1.00 19.22 ? 344  LYS   A CG    1 
ATOM   2483  C  CD    . LYS   A  1  346  ? -42.568 51.925  97.986  1.00 20.86 ? 344  LYS   A CD    1 
ATOM   2484  C  CE    . LYS   A  1  346  ? -41.362 51.084  98.273  1.00 20.68 ? 344  LYS   A CE    1 
ATOM   2485  N  NZ    . LYS   A  1  346  ? -40.594 51.651  99.411  1.00 21.97 ? 344  LYS   A NZ    1 
ATOM   2486  N  N     . ARG   A  1  347  ? -46.829 53.341  94.414  1.00 17.44 ? 345  ARG   A N     1 
ATOM   2487  C  CA    . ARG   A  1  347  ? -48.160 53.918  94.289  1.00 16.90 ? 345  ARG   A CA    1 
ATOM   2488  C  C     . ARG   A  1  347  ? -48.974 53.318  93.154  1.00 17.70 ? 345  ARG   A C     1 
ATOM   2489  O  O     . ARG   A  1  347  ? -50.168 53.612  93.063  1.00 17.56 ? 345  ARG   A O     1 
ATOM   2490  C  CB    . ARG   A  1  347  ? -48.057 55.433  94.114  1.00 18.95 ? 345  ARG   A CB    1 
ATOM   2491  C  CG    . ARG   A  1  347  ? -47.516 56.107  95.360  1.00 17.51 ? 345  ARG   A CG    1 
ATOM   2492  C  CD    . ARG   A  1  347  ? -47.107 57.527  95.073  1.00 16.84 ? 345  ARG   A CD    1 
ATOM   2493  N  NE    . ARG   A  1  347  ? -45.882 57.562  94.282  1.00 17.39 ? 345  ARG   A NE    1 
ATOM   2494  C  CZ    . ARG   A  1  347  ? -45.406 58.660  93.711  1.00 16.77 ? 345  ARG   A CZ    1 
ATOM   2495  N  NH1   . ARG   A  1  347  ? -46.004 59.828  93.860  1.00 16.94 ? 345  ARG   A NH1   1 
ATOM   2496  N  NH2   . ARG   A  1  347  ? -44.300 58.579  92.977  1.00 16.62 ? 345  ARG   A NH2   1 
ATOM   2497  N  N     . CYS   A  1  348  ? -48.382 52.468  92.326  1.00 16.88 ? 346  CYS   A N     1 
ATOM   2498  C  CA    . CYS   A  1  348  ? -49.017 52.012  91.094  1.00 17.07 ? 346  CYS   A CA    1 
ATOM   2499  C  C     . CYS   A  1  348  ? -50.466 51.548  91.241  1.00 17.06 ? 346  CYS   A C     1 
ATOM   2500  O  O     . CYS   A  1  348  ? -51.341 52.052  90.534  1.00 18.04 ? 346  CYS   A O     1 
ATOM   2501  C  CB    . CYS   A  1  348  ? -48.167 50.925  90.427  1.00 18.78 ? 346  CYS   A CB    1 
ATOM   2502  S  SG    . CYS   A  1  348  ? -48.656 50.646  88.720  1.00 22.02 ? 346  CYS   A SG    1 
ATOM   2503  N  N     . PRO   A  1  349  ? -50.780 50.595  92.114  1.00 17.43 ? 347  PRO   A N     1 
ATOM   2504  C  CA    . PRO   A  1  349  ? -52.181 50.154  92.187  1.00 18.59 ? 347  PRO   A CA    1 
ATOM   2505  C  C     . PRO   A  1  349  ? -53.133 51.254  92.619  1.00 18.90 ? 347  PRO   A C     1 
ATOM   2506  O  O     . PRO   A  1  349  ? -54.286 51.287  92.175  1.00 19.46 ? 347  PRO   A O     1 
ATOM   2507  C  CB    . PRO   A  1  349  ? -52.141 48.998  93.198  1.00 20.43 ? 347  PRO   A CB    1 
ATOM   2508  C  CG    . PRO   A  1  349  ? -50.924 49.238  94.005  1.00 22.84 ? 347  PRO   A CG    1 
ATOM   2509  C  CD    . PRO   A  1  349  ? -49.931 49.921  93.111  1.00 18.87 ? 347  PRO   A CD    1 
ATOM   2510  N  N     . PHE   A  1  350  ? -52.667 52.174  93.454  1.00 17.96 ? 348  PHE   A N     1 
ATOM   2511  C  CA    . PHE   A  1  350  ? -53.505 53.278  93.901  1.00 18.84 ? 348  PHE   A CA    1 
ATOM   2512  C  C     . PHE   A  1  350  ? -53.679 54.308  92.809  1.00 18.16 ? 348  PHE   A C     1 
ATOM   2513  O  O     . PHE   A  1  350  ? -54.754 54.907  92.675  1.00 18.12 ? 348  PHE   A O     1 
ATOM   2514  C  CB    . PHE   A  1  350  ? -52.900 53.882  95.158  1.00 19.32 ? 348  PHE   A CB    1 
ATOM   2515  C  CG    . PHE   A  1  350  ? -52.584 52.848  96.186  1.00 20.18 ? 348  PHE   A CG    1 
ATOM   2516  C  CD1   . PHE   A  1  350  ? -53.600 52.298  96.950  1.00 23.41 ? 348  PHE   A CD1   1 
ATOM   2517  C  CD2   . PHE   A  1  350  ? -51.295 52.367  96.333  1.00 20.98 ? 348  PHE   A CD2   1 
ATOM   2518  C  CE1   . PHE   A  1  350  ? -53.324 51.312  97.880  1.00 23.11 ? 348  PHE   A CE1   1 
ATOM   2519  C  CE2   . PHE   A  1  350  ? -51.010 51.374  97.257  1.00 24.67 ? 348  PHE   A CE2   1 
ATOM   2520  C  CZ    . PHE   A  1  350  ? -52.028 50.851  98.032  1.00 24.94 ? 348  PHE   A CZ    1 
ATOM   2521  N  N     . VAL   A  1  351  ? -52.645 54.495  91.995  1.00 17.43 ? 349  VAL   A N     1 
ATOM   2522  C  CA    . VAL   A  1  351  ? -52.770 55.349  90.823  1.00 17.30 ? 349  VAL   A CA    1 
ATOM   2523  C  C     . VAL   A  1  351  ? -53.792 54.761  89.866  1.00 17.88 ? 349  VAL   A C     1 
ATOM   2524  O  O     . VAL   A  1  351  ? -54.654 55.476  89.341  1.00 17.80 ? 349  VAL   A O     1 
ATOM   2525  C  CB    . VAL   A  1  351  ? -51.396 55.526  90.157  1.00 15.32 ? 349  VAL   A CB    1 
ATOM   2526  C  CG1   . VAL   A  1  351  ? -51.567 56.271  88.846  1.00 16.55 ? 349  VAL   A CG1   1 
ATOM   2527  C  CG2   . VAL   A  1  351  ? -50.455 56.291  91.080  1.00 17.80 ? 349  VAL   A CG2   1 
ATOM   2528  N  N     . LEU   A  1  352  ? -53.723 53.442  89.647  1.00 18.04 ? 350  LEU   A N     1 
ATOM   2529  C  CA    . LEU   A  1  352  ? -54.692 52.777  88.789  1.00 16.98 ? 350  LEU   A CA    1 
ATOM   2530  C  C     . LEU   A  1  352  ? -56.105 52.928  89.332  1.00 17.83 ? 350  LEU   A C     1 
ATOM   2531  O  O     . LEU   A  1  352  ? -57.038 53.176  88.566  1.00 18.43 ? 350  LEU   A O     1 
ATOM   2532  C  CB    . LEU   A  1  352  ? -54.330 51.305  88.617  1.00 18.53 ? 350  LEU   A CB    1 
ATOM   2533  C  CG    . LEU   A  1  352  ? -53.077 51.081  87.782  1.00 18.44 ? 350  LEU   A CG    1 
ATOM   2534  C  CD1   . LEU   A  1  352  ? -52.716 49.617  87.810  1.00 21.15 ? 350  LEU   A CD1   1 
ATOM   2535  C  CD2   . LEU   A  1  352  ? -53.325 51.551  86.367  1.00 21.12 ? 350  LEU   A CD2   1 
ATOM   2536  N  N     . ASP   A  1  353  ? -56.290 52.768  90.651  1.00 17.95 ? 351  ASP   A N     1 
ATOM   2537  C  CA    . ASP   A  1  353  ? -57.621 52.990  91.217  1.00 18.97 ? 351  ASP   A CA    1 
ATOM   2538  C  C     . ASP   A  1  353  ? -58.114 54.391  90.903  1.00 17.46 ? 351  ASP   A C     1 
ATOM   2539  O  O     . ASP   A  1  353  ? -59.289 54.587  90.572  1.00 18.54 ? 351  ASP   A O     1 
ATOM   2540  C  CB    . ASP   A  1  353  ? -57.587 52.807  92.733  1.00 19.44 ? 351  ASP   A CB    1 
ATOM   2541  C  CG    . ASP   A  1  353  ? -57.427 51.366  93.159  1.00 21.90 ? 351  ASP   A CG    1 
ATOM   2542  O  OD1   . ASP   A  1  353  ? -57.756 50.450  92.374  1.00 23.21 ? 351  ASP   A OD1   1 
ATOM   2543  O  OD2   . ASP   A  1  353  ? -56.978 51.164  94.301  1.00 26.52 ? 351  ASP   A OD2   1 
ATOM   2544  N  N     . PHE   A  1  354  ? -57.229 55.381  91.032  1.00 18.18 ? 352  PHE   A N     1 
ATOM   2545  C  CA    . PHE   A  1  354  ? -57.586 56.755  90.726  1.00 16.48 ? 352  PHE   A CA    1 
ATOM   2546  C  C     . PHE   A  1  354  ? -57.957 56.903  89.257  1.00 16.57 ? 352  PHE   A C     1 
ATOM   2547  O  O     . PHE   A  1  354  ? -58.965 57.530  88.928  1.00 17.56 ? 352  PHE   A O     1 
ATOM   2548  C  CB    . PHE   A  1  354  ? -56.431 57.698  91.095  1.00 17.24 ? 352  PHE   A CB    1 
ATOM   2549  C  CG    . PHE   A  1  354  ? -56.612 59.073  90.547  1.00 18.40 ? 352  PHE   A CG    1 
ATOM   2550  C  CD1   . PHE   A  1  354  ? -57.354 60.013  91.234  1.00 19.34 ? 352  PHE   A CD1   1 
ATOM   2551  C  CD2   . PHE   A  1  354  ? -56.071 59.409  89.318  1.00 19.48 ? 352  PHE   A CD2   1 
ATOM   2552  C  CE1   . PHE   A  1  354  ? -57.558 61.283  90.701  1.00 20.61 ? 352  PHE   A CE1   1 
ATOM   2553  C  CE2   . PHE   A  1  354  ? -56.268 60.664  88.777  1.00 19.49 ? 352  PHE   A CE2   1 
ATOM   2554  C  CZ    . PHE   A  1  354  ? -57.016 61.604  89.469  1.00 19.49 ? 352  PHE   A CZ    1 
ATOM   2555  N  N     . ILE   A  1  355  ? -57.158 56.317  88.363  1.00 15.67 ? 353  ILE   A N     1 
ATOM   2556  C  CA    . ILE   A  1  355  ? -57.399 56.466  86.932  1.00 15.82 ? 353  ILE   A CA    1 
ATOM   2557  C  C     . ILE   A  1  355  ? -58.676 55.764  86.524  1.00 18.13 ? 353  ILE   A C     1 
ATOM   2558  O  O     . ILE   A  1  355  ? -59.444 56.280  85.717  1.00 17.36 ? 353  ILE   A O     1 
ATOM   2559  C  CB    . ILE   A  1  355  ? -56.205 55.937  86.129  1.00 17.09 ? 353  ILE   A CB    1 
ATOM   2560  C  CG1   . ILE   A  1  355  ? -54.998 56.835  86.347  1.00 17.98 ? 353  ILE   A CG1   1 
ATOM   2561  C  CG2   . ILE   A  1  355  ? -56.565 55.845  84.653  1.00 17.83 ? 353  ILE   A CG2   1 
ATOM   2562  C  CD1   . ILE   A  1  355  ? -53.726 56.244  85.806  1.00 19.89 ? 353  ILE   A CD1   1 
ATOM   2563  N  N     . ILE   A  1  356  ? -58.895 54.552  87.034  1.00 17.88 ? 354  ILE   A N     1 
ATOM   2564  C  CA    . ILE   A  1  356  ? -60.117 53.832  86.705  1.00 17.37 ? 354  ILE   A CA    1 
ATOM   2565  C  C     . ILE   A  1  356  ? -61.336 54.616  87.165  1.00 18.05 ? 354  ILE   A C     1 
ATOM   2566  O  O     . ILE   A  1  356  ? -62.326 54.744  86.434  1.00 18.35 ? 354  ILE   A O     1 
ATOM   2567  C  CB    . ILE   A  1  356  ? -60.057 52.420  87.306  1.00 19.38 ? 354  ILE   A CB    1 
ATOM   2568  C  CG1   . ILE   A  1  356  ? -59.013 51.600  86.542  1.00 19.61 ? 354  ILE   A CG1   1 
ATOM   2569  C  CG2   . ILE   A  1  356  ? -61.435 51.764  87.304  1.00 21.40 ? 354  ILE   A CG2   1 
ATOM   2570  C  CD1   . ILE   A  1  356  ? -58.583 50.358  87.289  1.00 20.73 ? 354  ILE   A CD1   1 
ATOM   2571  N  N     . ASP   A  1  357  ? -61.261 55.201  88.359  1.00 18.52 ? 355  ASP   A N     1 
ATOM   2572  C  CA    . ASP   A  1  357  ? -62.369 56.027  88.821  1.00 18.29 ? 355  ASP   A CA    1 
ATOM   2573  C  C     . ASP   A  1  357  ? -62.531 57.285  87.970  1.00 17.22 ? 355  ASP   A C     1 
ATOM   2574  O  O     . ASP   A  1  357  ? -63.663 57.690  87.660  1.00 18.31 ? 355  ASP   A O     1 
ATOM   2575  C  CB    . ASP   A  1  357  ? -62.192 56.377  90.293  1.00 19.72 ? 355  ASP   A CB    1 
ATOM   2576  C  CG    . ASP   A  1  357  ? -63.218 57.372  90.762  1.00 21.85 ? 355  ASP   A CG    1 
ATOM   2577  O  OD1   . ASP   A  1  357  ? -64.346 56.946  91.070  1.00 24.81 ? 355  ASP   A OD1   1 
ATOM   2578  O  OD2   . ASP   A  1  357  ? -62.912 58.581  90.787  1.00 21.10 ? 355  ASP   A OD2   1 
ATOM   2579  N  N     . LEU   A  1  358  ? -61.417 57.908  87.570  1.00 17.18 ? 356  LEU   A N     1 
ATOM   2580  C  CA    . LEU   A  1  358  ? -61.509 59.068  86.694  1.00 17.16 ? 356  LEU   A CA    1 
ATOM   2581  C  C     . LEU   A  1  358  ? -62.136 58.691  85.364  1.00 16.80 ? 356  LEU   A C     1 
ATOM   2582  O  O     . LEU   A  1  358  ? -62.958 59.438  84.817  1.00 17.22 ? 356  LEU   A O     1 
ATOM   2583  C  CB    . LEU   A  1  358  ? -60.121 59.659  86.467  1.00 15.45 ? 356  LEU   A CB    1 
ATOM   2584  C  CG    . LEU   A  1  358  ? -60.023 60.767  85.423  1.00 16.16 ? 356  LEU   A CG    1 
ATOM   2585  C  CD1   . LEU   A  1  358  ? -60.862 61.965  85.813  1.00 19.45 ? 356  LEU   A CD1   1 
ATOM   2586  C  CD2   . LEU   A  1  358  ? -58.534 61.172  85.272  1.00 15.88 ? 356  LEU   A CD2   1 
ATOM   2587  N  N     . ALA   A  1  359  ? -61.777 57.520  84.836  1.00 16.70 ? 357  ALA   A N     1 
ATOM   2588  C  CA    . ALA   A  1  359  ? -62.393 57.053  83.602  1.00 17.51 ? 357  ALA   A CA    1 
ATOM   2589  C  C     . ALA   A  1  359  ? -63.889 56.856  83.778  1.00 17.28 ? 357  ALA   A C     1 
ATOM   2590  O  O     . ALA   A  1  359  ? -64.669 57.172  82.879  1.00 18.35 ? 357  ALA   A O     1 
ATOM   2591  C  CB    . ALA   A  1  359  ? -61.732 55.751  83.156  1.00 19.94 ? 357  ALA   A CB    1 
ATOM   2592  N  N     . ARG   A  1  360  ? -64.308 56.331  84.934  1.00 17.72 ? 358  ARG   A N     1 
ATOM   2593  C  CA    . ARG   A  1  360  ? -65.736 56.178  85.194  1.00 18.78 ? 358  ARG   A CA    1 
ATOM   2594  C  C     . ARG   A  1  360  ? -66.429 57.532  85.273  1.00 21.21 ? 358  ARG   A C     1 
ATOM   2595  O  O     . ARG   A  1  360  ? -67.484 57.740  84.663  1.00 22.26 ? 358  ARG   A O     1 
ATOM   2596  C  CB    . ARG   A  1  360  ? -65.949 55.388  86.484  1.00 20.23 ? 358  ARG   A CB    1 
ATOM   2597  C  CG    . ARG   A  1  360  ? -65.600 53.907  86.382  1.00 25.65 ? 358  ARG   A CG    1 
ATOM   2598  C  CD    . ARG   A  1  360  ? -66.141 53.118  87.576  1.00 30.63 ? 358  ARG   A CD    1 
ATOM   2599  N  NE    . ARG   A  1  360  ? -65.388 51.884  87.768  1.00 32.64 ? 358  ARG   A NE    1 
ATOM   2600  C  CZ    . ARG   A  1  360  ? -65.648 50.744  87.142  1.00 39.77 ? 358  ARG   A CZ    1 
ATOM   2601  N  NH1   . ARG   A  1  360  ? -66.688 50.621  86.332  1.00 45.13 ? 358  ARG   A NH1   1 
ATOM   2602  N  NH2   . ARG   A  1  360  ? -64.840 49.704  87.329  1.00 38.02 ? 358  ARG   A NH2   1 
ATOM   2603  N  N     . ARG   A  1  361  ? -65.852 58.466  86.030  1.00 19.98 ? 359  ARG   A N     1 
ATOM   2604  C  CA    . ARG   A  1  361  ? -66.457 59.784  86.211  1.00 20.44 ? 359  ARG   A CA    1 
ATOM   2605  C  C     . ARG   A  1  361  ? -66.551 60.535  84.892  1.00 20.10 ? 359  ARG   A C     1 
ATOM   2606  O  O     . ARG   A  1  361  ? -67.577 61.155  84.580  1.00 22.17 ? 359  ARG   A O     1 
ATOM   2607  C  CB    . ARG   A  1  361  ? -65.619 60.594  87.207  1.00 23.04 ? 359  ARG   A CB    1 
ATOM   2608  C  CG    . ARG   A  1  361  ? -65.751 60.154  88.645  1.00 24.94 ? 359  ARG   A CG    1 
ATOM   2609  C  CD    . ARG   A  1  361  ? -65.012 61.121  89.553  1.00 24.12 ? 359  ARG   A CD    1 
ATOM   2610  N  NE    . ARG   A  1  361  ? -63.560 61.009  89.472  1.00 22.56 ? 359  ARG   A NE    1 
ATOM   2611  C  CZ    . ARG   A  1  361  ? -62.738 62.016  89.210  1.00 21.69 ? 359  ARG   A CZ    1 
ATOM   2612  N  NH1   . ARG   A  1  361  ? -63.189 63.200  88.840  1.00 22.28 ? 359  ARG   A NH1   1 
ATOM   2613  N  NH2   . ARG   A  1  361  ? -61.428 61.839  89.355  1.00 20.78 ? 359  ARG   A NH2   1 
ATOM   2614  N  N     . SER   A  1  362  ? -65.476 60.507  84.111  1.00 18.93 ? 360  SER   A N     1 
ATOM   2615  C  CA    . SER   A  1  362  ? -65.412 61.272  82.877  1.00 18.02 ? 360  SER   A CA    1 
ATOM   2616  C  C     . SER   A  1  362  ? -66.106 60.567  81.724  1.00 18.51 ? 360  SER   A C     1 
ATOM   2617  O  O     . SER   A  1  362  ? -66.434 61.216  80.724  1.00 19.11 ? 360  SER   A O     1 
ATOM   2618  C  CB    . SER   A  1  362  ? -63.937 61.492  82.515  1.00 18.57 ? 360  SER   A CB    1 
ATOM   2619  O  OG    . SER   A  1  362  ? -63.327 60.255  82.171  1.00 17.53 ? 360  SER   A OG    1 
ATOM   2620  N  N     . GLY   A  1  363  ? -66.309 59.256  81.827  1.00 18.74 ? 361  GLY   A N     1 
ATOM   2621  C  CA    . GLY   A  1  363  ? -66.767 58.491  80.688  1.00 19.63 ? 361  GLY   A CA    1 
ATOM   2622  C  C     . GLY   A  1  363  ? -65.751 58.310  79.587  1.00 21.18 ? 361  GLY   A C     1 
ATOM   2623  O  O     . GLY   A  1  363  ? -66.127 57.875  78.492  1.00 22.69 ? 361  GLY   A O     1 
ATOM   2624  N  N     . ARG   A  1  364  ? -64.480 58.637  79.841  1.00 18.47 ? 362  ARG   A N     1 
ATOM   2625  C  CA    . ARG   A  1  364  ? -63.410 58.468  78.867  1.00 19.84 ? 362  ARG   A CA    1 
ATOM   2626  C  C     . ARG   A  1  364  ? -62.769 57.119  79.127  1.00 17.92 ? 362  ARG   A C     1 
ATOM   2627  O  O     . ARG   A  1  364  ? -62.404 56.813  80.266  1.00 19.74 ? 362  ARG   A O     1 
ATOM   2628  C  CB    . ARG   A  1  364  ? -62.326 59.530  79.060  1.00 20.88 ? 362  ARG   A CB    1 
ATOM   2629  C  CG    . ARG   A  1  364  ? -62.777 60.981  79.070  1.00 24.82 ? 362  ARG   A CG    1 
ATOM   2630  C  CD    . ARG   A  1  364  ? -62.811 61.631  77.700  1.00 19.39 ? 362  ARG   A CD    1 
ATOM   2631  N  NE    . ARG   A  1  364  ? -63.627 62.835  77.779  1.00 18.42 ? 362  ARG   A NE    1 
ATOM   2632  C  CZ    . ARG   A  1  364  ? -63.157 64.063  77.921  1.00 17.07 ? 362  ARG   A CZ    1 
ATOM   2633  N  NH1   . ARG   A  1  364  ? -61.858 64.321  77.868  1.00 16.62 ? 362  ARG   A NH1   1 
ATOM   2634  N  NH2   . ARG   A  1  364  ? -64.012 65.059  78.121  1.00 17.27 ? 362  ARG   A NH2   1 
ATOM   2635  N  N     . ARG   A  1  365  ? -62.630 56.314  78.083  1.00 18.14 ? 363  ARG   A N     1 
ATOM   2636  C  CA    . ARG   A  1  365  ? -61.990 55.017  78.231  1.00 16.67 ? 363  ARG   A CA    1 
ATOM   2637  C  C     . ARG   A  1  365  ? -60.486 55.253  78.152  1.00 17.32 ? 363  ARG   A C     1 
ATOM   2638  O  O     . ARG   A  1  365  ? -59.870 55.167  77.088  1.00 19.27 ? 363  ARG   A O     1 
ATOM   2639  C  CB    . ARG   A  1  365  ? -62.468 54.069  77.149  1.00 18.59 ? 363  ARG   A CB    1 
ATOM   2640  C  CG    . ARG   A  1  365  ? -61.924 52.693  77.339  1.00 19.30 ? 363  ARG   A CG    1 
ATOM   2641  C  CD    . ARG   A  1  365  ? -62.800 51.661  76.715  1.00 23.52 ? 363  ARG   A CD    1 
ATOM   2642  N  NE    . ARG   A  1  365  ? -62.272 50.343  77.027  1.00 20.90 ? 363  ARG   A NE    1 
ATOM   2643  C  CZ    . ARG   A  1  365  ? -61.572 49.605  76.180  1.00 19.77 ? 363  ARG   A CZ    1 
ATOM   2644  N  NH1   . ARG   A  1  365  ? -61.361 49.995  74.935  1.00 23.23 ? 363  ARG   A NH1   1 
ATOM   2645  N  NH2   . ARG   A  1  365  ? -61.063 48.458  76.597  1.00 18.85 ? 363  ARG   A NH2   1 
ATOM   2646  N  N     . ILE   A  1  366  ? -59.888 55.584  79.296  1.00 16.62 ? 364  ILE   A N     1 
ATOM   2647  C  CA    . ILE   A  1  366  ? -58.491 55.996  79.309  1.00 17.33 ? 364  ILE   A CA    1 
ATOM   2648  C  C     . ILE   A  1  366  ? -57.627 54.831  78.880  1.00 17.16 ? 364  ILE   A C     1 
ATOM   2649  O  O     . ILE   A  1  366  ? -57.808 53.700  79.350  1.00 16.77 ? 364  ILE   A O     1 
ATOM   2650  C  CB    . ILE   A  1  366  ? -58.112 56.509  80.704  1.00 16.57 ? 364  ILE   A CB    1 
ATOM   2651  C  CG1   . ILE   A  1  366  ? -58.958 57.735  81.053  1.00 19.12 ? 364  ILE   A CG1   1 
ATOM   2652  C  CG2   . ILE   A  1  366  ? -56.626 56.838  80.782  1.00 18.41 ? 364  ILE   A CG2   1 
ATOM   2653  C  CD1   . ILE   A  1  366  ? -58.773 58.206  82.490  1.00 19.00 ? 364  ILE   A CD1   1 
ATOM   2654  N  N     . MET   A  1  367  ? -56.672 55.104  77.995  1.00 16.49 ? 365  MET   A N     1 
ATOM   2655  C  CA    . MET   A  1  367  ? -55.713 54.094  77.576  1.00 15.43 ? 365  MET   A CA    1 
ATOM   2656  C  C     . MET   A  1  367  ? -54.606 54.074  78.614  1.00 17.26 ? 365  MET   A C     1 
ATOM   2657  O  O     . MET   A  1  367  ? -53.935 55.084  78.830  1.00 20.18 ? 365  MET   A O     1 
ATOM   2658  C  CB    . MET   A  1  367  ? -55.147 54.448  76.203  1.00 15.22 ? 365  MET   A CB    1 
ATOM   2659  C  CG    . MET   A  1  367  ? -56.256 54.685  75.193  1.00 16.53 ? 365  MET   A CG    1 
ATOM   2660  S  SD    . MET   A  1  367  ? -55.702 55.097  73.528  1.00 18.66 ? 365  MET   A SD    1 
ATOM   2661  C  CE    . MET   A  1  367  ? -55.500 53.502  72.728  1.00 22.31 ? 365  MET   A CE    1 
ATOM   2662  N  N     . VAL   A  1  368  ? -54.446 52.963  79.299  1.00 14.27 ? 366  VAL   A N     1 
ATOM   2663  C  CA    . VAL   A  1  368  ? -53.519 52.902  80.410  1.00 15.10 ? 366  VAL   A CA    1 
ATOM   2664  C  C     . VAL   A  1  368  ? -52.380 52.001  79.991  1.00 15.21 ? 366  VAL   A C     1 
ATOM   2665  O  O     . VAL   A  1  368  ? -52.563 50.791  79.831  1.00 16.96 ? 366  VAL   A O     1 
ATOM   2666  C  CB    . VAL   A  1  368  ? -54.182 52.395  81.693  1.00 16.50 ? 366  VAL   A CB    1 
ATOM   2667  C  CG1   . VAL   A  1  368  ? -53.132 52.310  82.800  1.00 17.87 ? 366  VAL   A CG1   1 
ATOM   2668  C  CG2   . VAL   A  1  368  ? -55.329 53.313  82.081  1.00 17.94 ? 366  VAL   A CG2   1 
ATOM   2669  N  N     . ARG   A  1  369  ? -51.192 52.573  79.834  1.00 14.45 ? 367  ARG   A N     1 
ATOM   2670  C  CA    . ARG   A  1  369  ? -50.022 51.772  79.512  1.00 15.85 ? 367  ARG   A CA    1 
ATOM   2671  C  C     . ARG   A  1  369  ? -49.344 51.393  80.813  1.00 15.85 ? 367  ARG   A C     1 
ATOM   2672  O  O     . ARG   A  1  369  ? -48.855 52.257  81.547  1.00 17.35 ? 367  ARG   A O     1 
ATOM   2673  C  CB    . ARG   A  1  369  ? -49.052 52.527  78.618  1.00 16.32 ? 367  ARG   A CB    1 
ATOM   2674  C  CG    . ARG   A  1  369  ? -47.866 51.640  78.247  1.00 16.90 ? 367  ARG   A CG    1 
ATOM   2675  C  CD    . ARG   A  1  369  ? -46.669 52.452  77.811  1.00 17.56 ? 367  ARG   A CD    1 
ATOM   2676  N  NE    . ARG   A  1  369  ? -46.975 53.129  76.566  1.00 16.86 ? 367  ARG   A NE    1 
ATOM   2677  C  CZ    . ARG   A  1  369  ? -46.396 54.247  76.155  1.00 18.46 ? 367  ARG   A CZ    1 
ATOM   2678  N  NH1   . ARG   A  1  369  ? -45.453 54.844  76.872  1.00 17.57 ? 367  ARG   A NH1   1 
ATOM   2679  N  NH2   . ARG   A  1  369  ? -46.797 54.791  75.009  1.00 16.98 ? 367  ARG   A NH2   1 
ATOM   2680  N  N     . LEU   A  1  370  ? -49.338 50.109  81.107  1.00 15.89 ? 368  LEU   A N     1 
ATOM   2681  C  CA    . LEU   A  1  370  ? -48.644 49.605  82.274  1.00 14.99 ? 368  LEU   A CA    1 
ATOM   2682  C  C     . LEU   A  1  370  ? -47.223 49.247  81.861  1.00 16.58 ? 368  LEU   A C     1 
ATOM   2683  O  O     . LEU   A  1  370  ? -47.013 48.416  80.968  1.00 15.95 ? 368  LEU   A O     1 
ATOM   2684  C  CB    . LEU   A  1  370  ? -49.380 48.379  82.810  1.00 17.73 ? 368  LEU   A CB    1 
ATOM   2685  C  CG    . LEU   A  1  370  ? -48.836 47.811  84.113  1.00 18.38 ? 368  LEU   A CG    1 
ATOM   2686  C  CD1   . LEU   A  1  370  ? -49.040 48.790  85.262  1.00 19.57 ? 368  LEU   A CD1   1 
ATOM   2687  C  CD2   . LEU   A  1  370  ? -49.501 46.487  84.416  1.00 19.12 ? 368  LEU   A CD2   1 
ATOM   2688  N  N     . VAL   A  1  371  ? -46.252 49.865  82.521  1.00 15.99 ? 369  VAL   A N     1 
ATOM   2689  C  CA    . VAL   A  1  371  ? -44.847 49.603  82.278  1.00 15.95 ? 369  VAL   A CA    1 
ATOM   2690  C  C     . VAL   A  1  371  ? -44.238 49.232  83.611  1.00 15.49 ? 369  VAL   A C     1 
ATOM   2691  O  O     . VAL   A  1  371  ? -44.851 49.402  84.659  1.00 17.68 ? 369  VAL   A O     1 
ATOM   2692  C  CB    . VAL   A  1  371  ? -44.121 50.826  81.695  1.00 15.73 ? 369  VAL   A CB    1 
ATOM   2693  C  CG1   . VAL   A  1  371  ? -44.807 51.324  80.439  1.00 17.08 ? 369  VAL   A CG1   1 
ATOM   2694  C  CG2   . VAL   A  1  371  ? -43.985 51.929  82.744  1.00 17.60 ? 369  VAL   A CG2   1 
ATOM   2695  N  N     . LYS   A  1  372  ? -43.003 48.738  83.573  1.00 16.36 ? 370  LYS   A N     1 
ATOM   2696  C  CA    . LYS   A  1  372  ? -42.300 48.572  84.839  1.00 17.42 ? 370  LYS   A CA    1 
ATOM   2697  C  C     . LYS   A  1  372  ? -41.701 49.895  85.314  1.00 17.25 ? 370  LYS   A C     1 
ATOM   2698  O  O     . LYS   A  1  372  ? -42.109 50.432  86.350  1.00 20.20 ? 370  LYS   A O     1 
ATOM   2699  C  CB    . LYS   A  1  372  ? -41.344 47.376  84.776  1.00 19.17 ? 370  LYS   A CB    1 
ATOM   2700  C  CG    . LYS   A  1  372  ? -42.181 46.088  84.692  1.00 17.96 ? 370  LYS   A CG    1 
ATOM   2701  C  CD    . LYS   A  1  372  ? -41.366 44.817  84.546  1.00 20.57 ? 370  LYS   A CD    1 
ATOM   2702  C  CE    . LYS   A  1  372  ? -42.306 43.680  84.169  1.00 19.46 ? 370  LYS   A CE    1 
ATOM   2703  N  NZ    . LYS   A  1  372  ? -41.553 42.400  83.972  1.00 20.53 ? 370  LYS   A NZ    1 
ATOM   2704  N  N     . GLY   A  1  373  ? -40.818 50.487  84.537  1.00 16.11 ? 371  GLY   A N     1 
ATOM   2705  C  CA    . GLY   A  1  373  ? -40.347 51.834  84.826  1.00 16.20 ? 371  GLY   A CA    1 
ATOM   2706  C  C     . GLY   A  1  373  ? -38.907 52.005  84.384  1.00 15.59 ? 371  GLY   A C     1 
ATOM   2707  O  O     . GLY   A  1  373  ? -38.100 51.088  84.447  1.00 17.39 ? 371  GLY   A O     1 
ATOM   2708  N  N     . ALA   A  1  374  ? -38.575 53.230  83.964  1.00 15.40 ? 372  ALA   A N     1 
ATOM   2709  C  CA    . ALA   A  1  374  ? -37.328 53.483  83.251  1.00 14.81 ? 372  ALA   A CA    1 
ATOM   2710  C  C     . ALA   A  1  374  ? -36.263 54.213  84.057  1.00 17.97 ? 372  ALA   A C     1 
ATOM   2711  O  O     . ALA   A  1  374  ? -35.151 54.404  83.546  1.00 17.89 ? 372  ALA   A O     1 
ATOM   2712  C  CB    . ALA   A  1  374  ? -37.604 54.269  81.964  1.00 17.16 ? 372  ALA   A CB    1 
ATOM   2713  N  N     . TYR   A  1  375  ? -36.557 54.646  85.278  1.00 16.09 ? 373  TYR   A N     1 
ATOM   2714  C  CA    . TYR   A  1  375  ? -35.674 55.542  86.014  1.00 15.27 ? 373  TYR   A CA    1 
ATOM   2715  C  C     . TYR   A  1  375  ? -35.184 54.918  87.313  1.00 14.98 ? 373  TYR   A C     1 
ATOM   2716  O  O     . TYR   A  1  375  ? -34.873 55.643  88.257  1.00 16.78 ? 373  TYR   A O     1 
ATOM   2717  C  CB    . TYR   A  1  375  ? -36.372 56.863  86.351  1.00 17.34 ? 373  TYR   A CB    1 
ATOM   2718  C  CG    . TYR   A  1  375  ? -36.965 57.592  85.185  1.00 15.71 ? 373  TYR   A CG    1 
ATOM   2719  C  CD1   . TYR   A  1  375  ? -38.168 57.180  84.615  1.00 16.22 ? 373  TYR   A CD1   1 
ATOM   2720  C  CD2   . TYR   A  1  375  ? -36.344 58.714  84.669  1.00 18.98 ? 373  TYR   A CD2   1 
ATOM   2721  C  CE1   . TYR   A  1  375  ? -38.709 57.858  83.540  1.00 18.11 ? 373  TYR   A CE1   1 
ATOM   2722  C  CE2   . TYR   A  1  375  ? -36.879 59.398  83.593  1.00 19.21 ? 373  TYR   A CE2   1 
ATOM   2723  C  CZ    . TYR   A  1  375  ? -38.064 58.973  83.050  1.00 22.61 ? 373  TYR   A CZ    1 
ATOM   2724  O  OH    . TYR   A  1  375  ? -38.594 59.673  81.986  1.00 22.95 ? 373  TYR   A OH    1 
ATOM   2725  N  N     . TRP   A  1  376  ? -35.108 53.593  87.365  1.00 14.95 ? 374  TRP   A N     1 
ATOM   2726  C  CA    . TRP   A  1  376  ? -34.891 52.920  88.645  1.00 16.66 ? 374  TRP   A CA    1 
ATOM   2727  C  C     . TRP   A  1  376  ? -33.625 53.405  89.345  1.00 17.40 ? 374  TRP   A C     1 
ATOM   2728  O  O     . TRP   A  1  376  ? -33.678 53.820  90.510  1.00 17.14 ? 374  TRP   A O     1 
ATOM   2729  C  CB    . TRP   A  1  376  ? -34.899 51.402  88.485  1.00 17.02 ? 374  TRP   A CB    1 
ATOM   2730  C  CG    . TRP   A  1  376  ? -34.741 50.707  89.797  1.00 17.95 ? 374  TRP   A CG    1 
ATOM   2731  C  CD1   . TRP   A  1  376  ? -35.720 50.466  90.722  1.00 17.79 ? 374  TRP   A CD1   1 
ATOM   2732  C  CD2   . TRP   A  1  376  ? -33.528 50.196  90.351  1.00 18.17 ? 374  TRP   A CD2   1 
ATOM   2733  N  NE1   . TRP   A  1  376  ? -35.186 49.824  91.813  1.00 18.52 ? 374  TRP   A NE1   1 
ATOM   2734  C  CE2   . TRP   A  1  376  ? -33.842 49.646  91.610  1.00 18.96 ? 374  TRP   A CE2   1 
ATOM   2735  C  CE3   . TRP   A  1  376  ? -32.209 50.138  89.901  1.00 20.49 ? 374  TRP   A CE3   1 
ATOM   2736  C  CZ2   . TRP   A  1  376  ? -32.882 49.043  92.426  1.00 19.35 ? 374  TRP   A CZ2   1 
ATOM   2737  C  CZ3   . TRP   A  1  376  ? -31.254 49.540  90.713  1.00 21.42 ? 374  TRP   A CZ3   1 
ATOM   2738  C  CH2   . TRP   A  1  376  ? -31.595 49.004  91.959  1.00 21.35 ? 374  TRP   A CH2   1 
ATOM   2739  N  N     . ASP   A  1  377  ? -32.472 53.358  88.659  1.00 17.95 ? 375  ASP   A N     1 
ATOM   2740  C  CA    A ASP   A  1  377  ? -31.204 53.759  89.281  0.51 17.66 ? 375  ASP   A CA    1 
ATOM   2741  C  CA    B ASP   A  1  377  ? -31.253 53.725  89.364  0.49 17.60 ? 375  ASP   A CA    1 
ATOM   2742  C  C     . ASP   A  1  377  ? -31.278 55.180  89.811  1.00 16.74 ? 375  ASP   A C     1 
ATOM   2743  O  O     . ASP   A  1  377  ? -30.768 55.494  90.890  1.00 17.60 ? 375  ASP   A O     1 
ATOM   2744  C  CB    A ASP   A  1  377  ? -30.069 53.737  88.248  0.51 20.71 ? 375  ASP   A CB    1 
ATOM   2745  C  CB    B ASP   A  1  377  ? -29.975 53.340  88.605  0.49 20.11 ? 375  ASP   A CB    1 
ATOM   2746  C  CG    A ASP   A  1  377  ? -29.686 52.349  87.799  0.51 23.20 ? 375  ASP   A CG    1 
ATOM   2747  C  CG    B ASP   A  1  377  ? -29.896 53.929  87.211  0.49 19.85 ? 375  ASP   A CG    1 
ATOM   2748  O  OD1   A ASP   A  1  377  ? -29.827 51.396  88.578  0.51 30.84 ? 375  ASP   A OD1   1 
ATOM   2749  O  OD1   B ASP   A  1  377  ? -30.366 55.063  86.995  0.49 25.68 ? 375  ASP   A OD1   1 
ATOM   2750  O  OD2   A ASP   A  1  377  ? -29.206 52.228  86.652  0.51 30.21 ? 375  ASP   A OD2   1 
ATOM   2751  O  OD2   B ASP   A  1  377  ? -29.318 53.253  86.332  0.49 23.55 ? 375  ASP   A OD2   1 
ATOM   2752  N  N     . ALA   A  1  378  ? -31.888 56.067  89.029  1.00 15.75 ? 376  ALA   A N     1 
ATOM   2753  C  CA    . ALA   A  1  378  ? -31.953 57.469  89.408  1.00 15.31 ? 376  ALA   A CA    1 
ATOM   2754  C  C     . ALA   A  1  378  ? -32.849 57.658  90.617  1.00 16.24 ? 376  ALA   A C     1 
ATOM   2755  O  O     . ALA   A  1  378  ? -32.578 58.523  91.459  1.00 16.19 ? 376  ALA   A O     1 
ATOM   2756  C  CB    . ALA   A  1  378  ? -32.457 58.307  88.236  1.00 16.69 ? 376  ALA   A CB    1 
ATOM   2757  N  N     . GLU   A  1  379  ? -33.932 56.878  90.713  1.00 16.21 ? 377  GLU   A N     1 
ATOM   2758  C  CA    . GLU   A  1  379  ? -34.799 56.991  91.878  1.00 15.13 ? 377  GLU   A CA    1 
ATOM   2759  C  C     . GLU   A  1  379  ? -34.081 56.546  93.138  1.00 15.97 ? 377  GLU   A C     1 
ATOM   2760  O  O     . GLU   A  1  379  ? -34.297 57.123  94.207  1.00 17.24 ? 377  GLU   A O     1 
ATOM   2761  C  CB    . GLU   A  1  379  ? -36.061 56.157  91.692  1.00 15.75 ? 377  GLU   A CB    1 
ATOM   2762  C  CG    . GLU   A  1  379  ? -36.940 56.564  90.504  1.00 16.95 ? 377  GLU   A CG    1 
ATOM   2763  C  CD    . GLU   A  1  379  ? -37.533 57.957  90.604  1.00 17.40 ? 377  GLU   A CD    1 
ATOM   2764  O  OE1   . GLU   A  1  379  ? -37.396 58.638  91.637  1.00 18.67 ? 377  GLU   A OE1   1 
ATOM   2765  O  OE2   . GLU   A  1  379  ? -38.168 58.367  89.608  1.00 17.39 ? 377  GLU   A OE2   1 
ATOM   2766  N  N     . ILE   A  1  380  ? -33.229 55.519  93.033  1.00 15.74 ? 378  ILE   A N     1 
ATOM   2767  C  CA    . ILE   A  1  380  ? -32.480 55.079  94.208  1.00 17.30 ? 378  ILE   A CA    1 
ATOM   2768  C  C     . ILE   A  1  380  ? -31.525 56.180  94.647  1.00 17.21 ? 378  ILE   A C     1 
ATOM   2769  O  O     . ILE   A  1  380  ? -31.476 56.565  95.822  1.00 16.57 ? 378  ILE   A O     1 
ATOM   2770  C  CB    . ILE   A  1  380  ? -31.719 53.777  93.910  1.00 17.54 ? 378  ILE   A CB    1 
ATOM   2771  C  CG1   . ILE   A  1  380  ? -32.662 52.651  93.497  1.00 17.19 ? 378  ILE   A CG1   1 
ATOM   2772  C  CG2   . ILE   A  1  380  ? -30.845 53.376  95.114  1.00 18.45 ? 378  ILE   A CG2   1 
ATOM   2773  C  CD1   . ILE   A  1  380  ? -33.769 52.370  94.492  1.00 18.60 ? 378  ILE   A CD1   1 
ATOM   2774  N  N     . LYS   A  1  381  ? -30.781 56.739  93.693  1.00 15.19 ? 379  LYS   A N     1 
ATOM   2775  C  CA    . LYS   A  1  381  ? -29.838 57.793  94.031  1.00 15.69 ? 379  LYS   A CA    1 
ATOM   2776  C  C     . LYS   A  1  381  ? -30.540 58.998  94.635  1.00 16.69 ? 379  LYS   A C     1 
ATOM   2777  O  O     . LYS   A  1  381  ? -30.094 59.542  95.651  1.00 15.98 ? 379  LYS   A O     1 
ATOM   2778  C  CB    . LYS   A  1  381  ? -29.033 58.205  92.801  1.00 16.51 ? 379  LYS   A CB    1 
ATOM   2779  C  CG    . LYS   A  1  381  ? -28.064 59.337  93.081  1.00 17.29 ? 379  LYS   A CG    1 
ATOM   2780  C  CD    . LYS   A  1  381  ? -27.153 59.596  91.876  1.00 16.37 ? 379  LYS   A CD    1 
ATOM   2781  C  CE    . LYS   A  1  381  ? -26.144 60.674  92.198  1.00 18.11 ? 379  LYS   A CE    1 
ATOM   2782  N  NZ    . LYS   A  1  381  ? -25.239 60.936  91.018  1.00 16.61 ? 379  LYS   A NZ    1 
ATOM   2783  N  N     . ARG   A  1  382  ? -31.652 59.424  94.029  1.00 16.07 ? 380  ARG   A N     1 
ATOM   2784  C  CA    . ARG   A  1  382  ? -32.311 60.636  94.493  1.00 16.46 ? 380  ARG   A CA    1 
ATOM   2785  C  C     . ARG   A  1  382  ? -32.801 60.478  95.918  1.00 16.14 ? 380  ARG   A C     1 
ATOM   2786  O  O     . ARG   A  1  382  ? -32.655 61.398  96.728  1.00 17.40 ? 380  ARG   A O     1 
ATOM   2787  C  CB    . ARG   A  1  382  ? -33.496 60.957  93.585  1.00 17.92 ? 380  ARG   A CB    1 
ATOM   2788  C  CG    . ARG   A  1  382  ? -34.178 62.266  93.901  1.00 21.17 ? 380  ARG   A CG    1 
ATOM   2789  C  CD    . ARG   A  1  382  ? -33.407 63.406  93.266  1.00 36.84 ? 380  ARG   A CD    1 
ATOM   2790  N  NE    . ARG   A  1  382  ? -32.678 64.180  94.261  1.00 39.46 ? 380  ARG   A NE    1 
ATOM   2791  C  CZ    . ARG   A  1  382  ? -31.679 65.011  93.995  1.00 43.56 ? 380  ARG   A CZ    1 
ATOM   2792  N  NH1   . ARG   A  1  382  ? -31.210 65.163  92.765  1.00 46.35 ? 380  ARG   A NH1   1 
ATOM   2793  N  NH2   . ARG   A  1  382  ? -31.135 65.709  94.990  1.00 35.74 ? 380  ARG   A NH2   1 
ATOM   2794  N  N     . ALA   A  1  383  ? -33.397 59.329  96.242  1.00 16.82 ? 381  ALA   A N     1 
ATOM   2795  C  CA    . ALA   A  1  383  ? -33.910 59.148  97.597  1.00 16.99 ? 381  ALA   A CA    1 
ATOM   2796  C  C     . ALA   A  1  383  ? -32.769 59.151  98.599  1.00 17.21 ? 381  ALA   A C     1 
ATOM   2797  O  O     . ALA   A  1  383  ? -32.897 59.711  99.696  1.00 18.63 ? 381  ALA   A O     1 
ATOM   2798  C  CB    . ALA   A  1  383  ? -34.711 57.851  97.694  1.00 18.73 ? 381  ALA   A CB    1 
ATOM   2799  N  N     . GLN   A  1  384  ? -31.633 58.559  98.227  1.00 16.55 ? 382  GLN   A N     1 
ATOM   2800  C  CA    . GLN   A  1  384  ? -30.486 58.564  99.130  1.00 17.14 ? 382  GLN   A CA    1 
ATOM   2801  C  C     . GLN   A  1  384  ? -29.960 59.978  99.309  1.00 17.40 ? 382  GLN   A C     1 
ATOM   2802  O  O     . GLN   A  1  384  ? -29.713 60.414  100.437 1.00 18.61 ? 382  GLN   A O     1 
ATOM   2803  C  CB    . GLN   A  1  384  ? -29.400 57.627  98.596  1.00 15.79 ? 382  GLN   A CB    1 
ATOM   2804  C  CG    . GLN   A  1  384  ? -29.788 56.170  98.669  1.00 17.13 ? 382  GLN   A CG    1 
ATOM   2805  C  CD    . GLN   A  1  384  ? -28.638 55.264  98.300  1.00 17.84 ? 382  GLN   A CD    1 
ATOM   2806  O  OE1   . GLN   A  1  384  ? -27.698 55.695  97.648  1.00 19.80 ? 382  GLN   A OE1   1 
ATOM   2807  N  NE2   . GLN   A  1  384  ? -28.697 54.011  98.730  1.00 19.78 ? 382  GLN   A NE2   1 
ATOM   2808  N  N     . LEU   A  1  385  ? -29.798 60.723  98.213  1.00 16.93 ? 383  LEU   A N     1 
ATOM   2809  C  CA    . LEU   A  1  385  ? -29.316 62.098  98.317  1.00 17.33 ? 383  LEU   A CA    1 
ATOM   2810  C  C     . LEU   A  1  385  ? -30.219 62.936  99.204  1.00 18.40 ? 383  LEU   A C     1 
ATOM   2811  O  O     . LEU   A  1  385  ? -29.742 63.761  99.992  1.00 20.15 ? 383  LEU   A O     1 
ATOM   2812  C  CB    . LEU   A  1  385  ? -29.243 62.745  96.937  1.00 16.28 ? 383  LEU   A CB    1 
ATOM   2813  C  CG    . LEU   A  1  385  ? -28.139 62.284  95.988  1.00 20.65 ? 383  LEU   A CG    1 
ATOM   2814  C  CD1   . LEU   A  1  385  ? -28.305 62.964  94.657  1.00 22.29 ? 383  LEU   A CD1   1 
ATOM   2815  C  CD2   . LEU   A  1  385  ? -26.793 62.617  96.576  1.00 22.98 ? 383  LEU   A CD2   1 
ATOM   2816  N  N     . ASP   A  1  386  ? -31.526 62.752  99.079  1.00 17.58 ? 384  ASP   A N     1 
ATOM   2817  C  CA    . ASP   A  1  386  ? -32.473 63.600  99.773  1.00 19.03 ? 384  ASP   A CA    1 
ATOM   2818  C  C     . ASP   A  1  386  ? -32.760 63.117  101.183 1.00 19.60 ? 384  ASP   A C     1 
ATOM   2819  O  O     . ASP   A  1  386  ? -33.528 63.767  101.899 1.00 19.92 ? 384  ASP   A O     1 
ATOM   2820  C  CB    . ASP   A  1  386  ? -33.760 63.723  98.949  1.00 19.67 ? 384  ASP   A CB    1 
ATOM   2821  C  CG    . ASP   A  1  386  ? -33.567 64.529  97.669  1.00 25.42 ? 384  ASP   A CG    1 
ATOM   2822  O  OD1   . ASP   A  1  386  ? -32.483 65.134  97.488  1.00 26.82 ? 384  ASP   A OD1   1 
ATOM   2823  O  OD2   . ASP   A  1  386  ? -34.493 64.547  96.823  1.00 26.93 ? 384  ASP   A OD2   1 
ATOM   2824  N  N     . GLY   A  1  387  ? -32.154 62.011  101.602 1.00 19.10 ? 385  GLY   A N     1 
ATOM   2825  C  CA    . GLY   A  1  387  ? -32.328 61.542  102.969 1.00 19.66 ? 385  GLY   A CA    1 
ATOM   2826  C  C     . GLY   A  1  387  ? -33.760 61.187  103.292 1.00 20.19 ? 385  GLY   A C     1 
ATOM   2827  O  O     . GLY   A  1  387  ? -34.233 61.472  104.397 1.00 20.56 ? 385  GLY   A O     1 
ATOM   2828  N  N     . LEU   A  1  388  ? -34.467 60.578  102.354 1.00 19.88 ? 386  LEU   A N     1 
ATOM   2829  C  CA    . LEU   A  1  388  ? -35.883 60.350  102.579 1.00 20.69 ? 386  LEU   A CA    1 
ATOM   2830  C  C     . LEU   A  1  388  ? -36.113 58.994  103.226 1.00 20.96 ? 386  LEU   A C     1 
ATOM   2831  O  O     . LEU   A  1  388  ? -35.207 58.170  103.369 1.00 22.89 ? 386  LEU   A O     1 
ATOM   2832  C  CB    . LEU   A  1  388  ? -36.672 60.537  101.282 1.00 19.45 ? 386  LEU   A CB    1 
ATOM   2833  C  CG    . LEU   A  1  388  ? -36.510 61.937  100.693 1.00 21.30 ? 386  LEU   A CG    1 
ATOM   2834  C  CD1   . LEU   A  1  388  ? -37.274 62.092  99.379  1.00 21.16 ? 386  LEU   A CD1   1 
ATOM   2835  C  CD2   . LEU   A  1  388  ? -36.953 63.000  101.680 1.00 22.64 ? 386  LEU   A CD2   1 
ATOM   2836  N  N     . ALA   A  1  389  ? -37.352 58.782  103.668 1.00 23.09 ? 387  ALA   A N     1 
ATOM   2837  C  CA    . ALA   A  1  389  ? -37.616 57.650  104.540 1.00 25.18 ? 387  ALA   A CA    1 
ATOM   2838  C  C     . ALA   A  1  389  ? -37.418 56.325  103.824 1.00 23.98 ? 387  ALA   A C     1 
ATOM   2839  O  O     . ALA   A  1  389  ? -36.984 55.345  104.433 1.00 24.50 ? 387  ALA   A O     1 
ATOM   2840  C  CB    . ALA   A  1  389  ? -39.035 57.758  105.094 1.00 27.55 ? 387  ALA   A CB    1 
ATOM   2841  N  N     . ASP   A  1  390  ? -37.733 56.270  102.538 1.00 20.79 ? 388  ASP   A N     1 
ATOM   2842  C  CA    . ASP   A  1  390  ? -37.683 55.026  101.786 1.00 21.53 ? 388  ASP   A CA    1 
ATOM   2843  C  C     . ASP   A  1  390  ? -37.700 55.412  100.314 1.00 19.97 ? 388  ASP   A C     1 
ATOM   2844  O  O     . ASP   A  1  390  ? -37.737 56.594  99.968  1.00 19.03 ? 388  ASP   A O     1 
ATOM   2845  C  CB    . ASP   A  1  390  ? -38.867 54.129  102.177 1.00 21.47 ? 388  ASP   A CB    1 
ATOM   2846  C  CG    . ASP   A  1  390  ? -38.596 52.646  101.975 1.00 23.42 ? 388  ASP   A CG    1 
ATOM   2847  O  OD1   . ASP   A  1  390  ? -37.953 52.253  100.984 1.00 23.90 ? 388  ASP   A OD1   1 
ATOM   2848  O  OD2   . ASP   A  1  390  ? -39.059 51.856  102.822 1.00 27.67 ? 388  ASP   A OD2   1 
ATOM   2849  N  N     . PHE   A  1  391  ? -37.644 54.431  99.475  1.00 18.96 ? 389  PHE   A N     1 
ATOM   2850  C  CA    . PHE   A  1  391  ? -37.662 54.646  98.040  1.00 18.46 ? 389  PHE   A CA    1 
ATOM   2851  C  C     . PHE   A  1  391  ? -39.096 54.677  97.539  1.00 18.82 ? 389  PHE   A C     1 
ATOM   2852  O  O     . PHE   A  1  391  ? -39.989 54.091  98.156  1.00 19.45 ? 389  PHE   A O     1 
ATOM   2853  C  CB    . PHE   A  1  391  ? -36.907 53.517  97.353  1.00 19.12 ? 389  PHE   A CB    1 
ATOM   2854  C  CG    . PHE   A  1  391  ? -35.494 53.421  97.817  1.00 17.11 ? 389  PHE   A CG    1 
ATOM   2855  C  CD1   . PHE   A  1  391  ? -34.588 54.361  97.414  1.00 18.19 ? 389  PHE   A CD1   1 
ATOM   2856  C  CD2   . PHE   A  1  391  ? -35.105 52.463  98.731  1.00 19.25 ? 389  PHE   A CD2   1 
ATOM   2857  C  CE1   . PHE   A  1  391  ? -33.289 54.326  97.858  1.00 20.46 ? 389  PHE   A CE1   1 
ATOM   2858  C  CE2   . PHE   A  1  391  ? -33.805 52.427  99.190  1.00 20.61 ? 389  PHE   A CE2   1 
ATOM   2859  C  CZ    . PHE   A  1  391  ? -32.906 53.353  98.759  1.00 19.63 ? 389  PHE   A CZ    1 
ATOM   2860  N  N     . PRO   A  1  392  ? -39.350 55.393  96.445  1.00 17.69 ? 390  PRO   A N     1 
ATOM   2861  C  CA    . PRO   A  1  392  ? -40.685 55.381  95.838  1.00 17.85 ? 390  PRO   A CA    1 
ATOM   2862  C  C     . PRO   A  1  392  ? -40.850 54.261  94.827  1.00 17.79 ? 390  PRO   A C     1 
ATOM   2863  O  O     . PRO   A  1  392  ? -41.881 54.193  94.139  1.00 18.98 ? 390  PRO   A O     1 
ATOM   2864  C  CB    . PRO   A  1  392  ? -40.725 56.743  95.145  1.00 16.97 ? 390  PRO   A CB    1 
ATOM   2865  C  CG    . PRO   A  1  392  ? -39.295 56.947  94.682  1.00 15.03 ? 390  PRO   A CG    1 
ATOM   2866  C  CD    . PRO   A  1  392  ? -38.421 56.300  95.750  1.00 16.54 ? 390  PRO   A CD    1 
ATOM   2867  N  N     . VAL   A  1  393  ? -39.836 53.408  94.709  1.00 17.00 ? 391  VAL   A N     1 
ATOM   2868  C  CA    . VAL   A  1  393  ? -39.850 52.267  93.817  1.00 17.42 ? 391  VAL   A CA    1 
ATOM   2869  C  C     . VAL   A  1  393  ? -39.413 51.055  94.625  1.00 18.32 ? 391  VAL   A C     1 
ATOM   2870  O  O     . VAL   A  1  393  ? -38.800 51.176  95.689  1.00 19.23 ? 391  VAL   A O     1 
ATOM   2871  C  CB    . VAL   A  1  393  ? -38.909 52.463  92.608  1.00 15.97 ? 391  VAL   A CB    1 
ATOM   2872  C  CG1   . VAL   A  1  393  ? -39.386 53.615  91.721  1.00 17.55 ? 391  VAL   A CG1   1 
ATOM   2873  C  CG2   . VAL   A  1  393  ? -37.489 52.728  93.075  1.00 18.14 ? 391  VAL   A CG2   1 
ATOM   2874  N  N     . PHE   A  1  394  ? -39.740 49.879  94.106  1.00 17.66 ? 392  PHE   A N     1 
ATOM   2875  C  CA    . PHE   A  1  394  ? -39.250 48.645  94.695  1.00 17.49 ? 392  PHE   A CA    1 
ATOM   2876  C  C     . PHE   A  1  394  ? -37.744 48.554  94.502  1.00 18.56 ? 392  PHE   A C     1 
ATOM   2877  O  O     . PHE   A  1  394  ? -37.153 49.244  93.670  1.00 19.16 ? 392  PHE   A O     1 
ATOM   2878  C  CB    . PHE   A  1  394  ? -39.975 47.461  94.067  1.00 19.96 ? 392  PHE   A CB    1 
ATOM   2879  C  CG    . PHE   A  1  394  ? -41.443 47.510  94.305  1.00 17.58 ? 392  PHE   A CG    1 
ATOM   2880  C  CD1   . PHE   A  1  394  ? -41.924 47.387  95.597  1.00 20.76 ? 392  PHE   A CD1   1 
ATOM   2881  C  CD2   . PHE   A  1  394  ? -42.327 47.733  93.282  1.00 19.36 ? 392  PHE   A CD2   1 
ATOM   2882  C  CE1   . PHE   A  1  394  ? -43.271 47.476  95.860  1.00 19.57 ? 392  PHE   A CE1   1 
ATOM   2883  C  CE2   . PHE   A  1  394  ? -43.685 47.806  93.538  1.00 20.17 ? 392  PHE   A CE2   1 
ATOM   2884  C  CZ    . PHE   A  1  394  ? -44.154 47.674  94.829  1.00 19.69 ? 392  PHE   A CZ    1 
ATOM   2885  N  N     . THR   A  1  395  ? -37.107 47.737  95.333  1.00 18.44 ? 393  THR   A N     1 
ATOM   2886  C  CA    . THR   A  1  395  ? -35.669 47.545  95.248  1.00 20.12 ? 393  THR   A CA    1 
ATOM   2887  C  C     . THR   A  1  395  ? -35.265 46.146  94.824  1.00 19.87 ? 393  THR   A C     1 
ATOM   2888  O  O     . THR   A  1  395  ? -34.077 45.918  94.569  1.00 20.92 ? 393  THR   A O     1 
ATOM   2889  C  CB    . THR   A  1  395  ? -34.978 47.866  96.578  1.00 19.64 ? 393  THR   A CB    1 
ATOM   2890  O  OG1   . THR   A  1  395  ? -35.500 47.018  97.607  1.00 20.67 ? 393  THR   A OG1   1 
ATOM   2891  C  CG2   . THR   A  1  395  ? -35.160 49.324  96.961  1.00 21.16 ? 393  THR   A CG2   1 
ATOM   2892  N  N     . ARG   A  1  396  ? -36.198 45.211  94.744  1.00 20.69 ? 394  ARG   A N     1 
ATOM   2893  C  CA    . ARG   A  1  396  ? -35.943 43.912  94.151  1.00 21.54 ? 394  ARG   A CA    1 
ATOM   2894  C  C     . ARG   A  1  396  ? -36.737 43.814  92.868  1.00 20.52 ? 394  ARG   A C     1 
ATOM   2895  O  O     . ARG   A  1  396  ? -37.929 44.138  92.838  1.00 20.54 ? 394  ARG   A O     1 
ATOM   2896  C  CB    . ARG   A  1  396  ? -36.332 42.770  95.083  1.00 22.32 ? 394  ARG   A CB    1 
ATOM   2897  C  CG    . ARG   A  1  396  ? -35.544 42.736  96.356  1.00 23.08 ? 394  ARG   A CG    1 
ATOM   2898  C  CD    . ARG   A  1  396  ? -35.838 41.456  97.104  1.00 28.59 ? 394  ARG   A CD    1 
ATOM   2899  N  NE    . ARG   A  1  396  ? -35.315 41.526  98.458  1.00 31.32 ? 394  ARG   A NE    1 
ATOM   2900  C  CZ    . ARG   A  1  396  ? -34.472 40.650  98.982  1.00 37.50 ? 394  ARG   A CZ    1 
ATOM   2901  N  NH1   . ARG   A  1  396  ? -34.090 39.574  98.312  1.00 38.94 ? 394  ARG   A NH1   1 
ATOM   2902  N  NH2   . ARG   A  1  396  ? -34.003 40.860  100.209 1.00 31.30 ? 394  ARG   A NH2   1 
ATOM   2903  N  N     . LYS   A  1  397  ? -36.062 43.391  91.808  1.00 21.89 ? 395  LYS   A N     1 
ATOM   2904  C  CA    . LYS   A  1  397  ? -36.702 43.340  90.505  1.00 21.57 ? 395  LYS   A CA    1 
ATOM   2905  C  C     . LYS   A  1  397  ? -37.945 42.464  90.540  1.00 21.03 ? 395  LYS   A C     1 
ATOM   2906  O  O     . LYS   A  1  397  ? -38.955 42.772  89.894  1.00 20.56 ? 395  LYS   A O     1 
ATOM   2907  C  CB    . LYS   A  1  397  ? -35.688 42.853  89.475  1.00 23.54 ? 395  LYS   A CB    1 
ATOM   2908  C  CG    . LYS   A  1  397  ? -36.085 43.130  88.053  1.00 24.29 ? 395  LYS   A CG    1 
ATOM   2909  C  CD    . LYS   A  1  397  ? -36.795 41.955  87.457  1.00 22.47 ? 395  LYS   A CD    1 
ATOM   2910  C  CE    . LYS   A  1  397  ? -37.258 42.283  86.053  1.00 22.49 ? 395  LYS   A CE    1 
ATOM   2911  N  NZ    . LYS   A  1  397  ? -37.866 41.105  85.397  1.00 24.63 ? 395  LYS   A NZ    1 
ATOM   2912  N  N     . ILE   A  1  398  ? -37.903 41.377  91.313  1.00 21.10 ? 396  ILE   A N     1 
ATOM   2913  C  CA    . ILE   A  1  398  ? -39.037 40.468  91.341  1.00 22.10 ? 396  ILE   A CA    1 
ATOM   2914  C  C     . ILE   A  1  398  ? -40.264 41.149  91.936  1.00 19.05 ? 396  ILE   A C     1 
ATOM   2915  O  O     . ILE   A  1  398  ? -41.404 40.793  91.608  1.00 22.45 ? 396  ILE   A O     1 
ATOM   2916  C  CB    . ILE   A  1  398  ? -38.632 39.181  92.084  1.00 25.17 ? 396  ILE   A CB    1 
ATOM   2917  C  CG1   . ILE   A  1  398  ? -39.641 38.072  91.813  1.00 27.62 ? 396  ILE   A CG1   1 
ATOM   2918  C  CG2   . ILE   A  1  398  ? -38.480 39.452  93.574  1.00 24.36 ? 396  ILE   A CG2   1 
ATOM   2919  C  CD1   . ILE   A  1  398  ? -39.125 36.700  92.189  1.00 29.24 ? 396  ILE   A CD1   1 
ATOM   2920  N  N     . HIS   A  1  399  ? -40.057 42.135  92.808  1.00 21.88 ? 397  HIS   A N     1 
ATOM   2921  C  CA    . HIS   A  1  399  ? -41.184 42.873  93.362  1.00 20.85 ? 397  HIS   A CA    1 
ATOM   2922  C  C     . HIS   A  1  399  ? -41.892 43.661  92.276  1.00 19.70 ? 397  HIS   A C     1 
ATOM   2923  O  O     . HIS   A  1  399  ? -43.124 43.669  92.208  1.00 20.55 ? 397  HIS   A O     1 
ATOM   2924  C  CB    . HIS   A  1  399  ? -40.701 43.802  94.471  1.00 21.09 ? 397  HIS   A CB    1 
ATOM   2925  C  CG    . HIS   A  1  399  ? -40.191 43.068  95.674  1.00 19.03 ? 397  HIS   A CG    1 
ATOM   2926  N  ND1   . HIS   A  1  399  ? -39.508 43.691  96.696  1.00 22.46 ? 397  HIS   A ND1   1 
ATOM   2927  C  CD2   . HIS   A  1  399  ? -40.245 41.755  96.000  1.00 26.34 ? 397  HIS   A CD2   1 
ATOM   2928  C  CE1   . HIS   A  1  399  ? -39.176 42.793  97.609  1.00 23.60 ? 397  HIS   A CE1   1 
ATOM   2929  N  NE2   . HIS   A  1  399  ? -39.608 41.611  97.208  1.00 25.46 ? 397  HIS   A NE2   1 
ATOM   2930  N  N     . THR   A  1  400  ? -41.122 44.305  91.404  1.00 19.99 ? 398  THR   A N     1 
ATOM   2931  C  CA    . THR   A  1  400  ? -41.712 44.990  90.264  1.00 17.76 ? 398  THR   A CA    1 
ATOM   2932  C  C     . THR   A  1  400  ? -42.501 44.030  89.381  1.00 19.25 ? 398  THR   A C     1 
ATOM   2933  O  O     . THR   A  1  400  ? -43.584 44.374  88.897  1.00 18.53 ? 398  THR   A O     1 
ATOM   2934  C  CB    . THR   A  1  400  ? -40.600 45.685  89.492  1.00 17.91 ? 398  THR   A CB    1 
ATOM   2935  O  OG1   . THR   A  1  400  ? -40.080 46.735  90.307  1.00 18.58 ? 398  THR   A OG1   1 
ATOM   2936  C  CG2   . THR   A  1  400  ? -41.116 46.280  88.173  1.00 16.40 ? 398  THR   A CG2   1 
ATOM   2937  N  N     . ASP   A  1  401  ? -41.994 42.812  89.179  1.00 18.44 ? 399  ASP   A N     1 
ATOM   2938  C  CA    . ASP   A  1  401  ? -42.716 41.852  88.349  1.00 20.35 ? 399  ASP   A CA    1 
ATOM   2939  C  C     . ASP   A  1  401  ? -44.053 41.486  88.974  1.00 19.59 ? 399  ASP   A C     1 
ATOM   2940  O  O     . ASP   A  1  401  ? -45.070 41.404  88.275  1.00 20.42 ? 399  ASP   A O     1 
ATOM   2941  C  CB    . ASP   A  1  401  ? -41.876 40.591  88.105  1.00 21.13 ? 399  ASP   A CB    1 
ATOM   2942  C  CG    . ASP   A  1  401  ? -40.673 40.854  87.221  1.00 23.72 ? 399  ASP   A CG    1 
ATOM   2943  O  OD1   . ASP   A  1  401  ? -40.711 41.813  86.426  1.00 25.11 ? 399  ASP   A OD1   1 
ATOM   2944  O  OD2   . ASP   A  1  401  ? -39.686 40.103  87.323  1.00 25.50 ? 399  ASP   A OD2   1 
ATOM   2945  N  N     . VAL   A  1  402  ? -44.065 41.235  90.286  1.00 20.22 ? 400  VAL   A N     1 
ATOM   2946  C  CA    . VAL   A  1  402  ? -45.319 40.914  90.959  1.00 21.96 ? 400  VAL   A CA    1 
ATOM   2947  C  C     . VAL   A  1  402  ? -46.258 42.105  90.914  1.00 19.25 ? 400  VAL   A C     1 
ATOM   2948  O  O     . VAL   A  1  402  ? -47.461 41.957  90.655  1.00 20.23 ? 400  VAL   A O     1 
ATOM   2949  C  CB    . VAL   A  1  402  ? -45.056 40.476  92.405  1.00 20.60 ? 400  VAL   A CB    1 
ATOM   2950  C  CG1   . VAL   A  1  402  ? -46.389 40.259  93.150  1.00 20.27 ? 400  VAL   A CG1   1 
ATOM   2951  C  CG2   . VAL   A  1  402  ? -44.225 39.209  92.421  1.00 24.16 ? 400  VAL   A CG2   1 
ATOM   2952  N  N     . SER   A  1  403  ? -45.719 43.303  91.169  1.00 20.32 ? 401  SER   A N     1 
ATOM   2953  C  CA    . SER   A  1  403  ? -46.515 44.519  91.067  1.00 19.40 ? 401  SER   A CA    1 
ATOM   2954  C  C     . SER   A  1  403  ? -47.162 44.624  89.694  1.00 20.86 ? 401  SER   A C     1 
ATOM   2955  O  O     . SER   A  1  403  ? -48.356 44.896  89.575  1.00 19.09 ? 401  SER   A O     1 
ATOM   2956  C  CB    . SER   A  1  403  ? -45.630 45.736  91.326  1.00 20.32 ? 401  SER   A CB    1 
ATOM   2957  O  OG    . SER   A  1  403  ? -46.365 46.931  91.127  1.00 20.21 ? 401  SER   A OG    1 
ATOM   2958  N  N     . TYR   A  1  404  ? -46.379 44.390  88.643  1.00 18.46 ? 402  TYR   A N     1 
ATOM   2959  C  CA    . TYR   A  1  404  ? -46.904 44.472  87.289  1.00 19.66 ? 402  TYR   A CA    1 
ATOM   2960  C  C     . TYR   A  1  404  ? -48.076 43.515  87.094  1.00 17.69 ? 402  TYR   A C     1 
ATOM   2961  O  O     . TYR   A  1  404  ? -49.130 43.900  86.580  1.00 19.14 ? 402  TYR   A O     1 
ATOM   2962  C  CB    . TYR   A  1  404  ? -45.768 44.183  86.307  1.00 18.14 ? 402  TYR   A CB    1 
ATOM   2963  C  CG    . TYR   A  1  404  ? -46.089 44.524  84.885  1.00 19.18 ? 402  TYR   A CG    1 
ATOM   2964  C  CD1   . TYR   A  1  404  ? -46.862 43.679  84.102  1.00 18.77 ? 402  TYR   A CD1   1 
ATOM   2965  C  CD2   . TYR   A  1  404  ? -45.612 45.690  84.315  1.00 17.24 ? 402  TYR   A CD2   1 
ATOM   2966  C  CE1   . TYR   A  1  404  ? -47.160 43.985  82.801  1.00 19.58 ? 402  TYR   A CE1   1 
ATOM   2967  C  CE2   . TYR   A  1  404  ? -45.901 46.000  82.989  1.00 17.48 ? 402  TYR   A CE2   1 
ATOM   2968  C  CZ    . TYR   A  1  404  ? -46.664 45.138  82.243  1.00 17.63 ? 402  TYR   A CZ    1 
ATOM   2969  O  OH    . TYR   A  1  404  ? -46.979 45.433  80.939  1.00 20.28 ? 402  TYR   A OH    1 
ATOM   2970  N  N     . ILE   A  1  405  ? -47.911 42.259  87.512  1.00 20.62 ? 403  ILE   A N     1 
ATOM   2971  C  CA    . ILE   A  1  405  ? -48.953 41.267  87.285  1.00 20.32 ? 403  ILE   A CA    1 
ATOM   2972  C  C     . ILE   A  1  405  ? -50.183 41.577  88.127  1.00 19.30 ? 403  ILE   A C     1 
ATOM   2973  O  O     . ILE   A  1  405  ? -51.318 41.453  87.658  1.00 21.45 ? 403  ILE   A O     1 
ATOM   2974  C  CB    . ILE   A  1  405  ? -48.394 39.860  87.546  1.00 22.70 ? 403  ILE   A CB    1 
ATOM   2975  C  CG1   . ILE   A  1  405  ? -47.287 39.581  86.535  1.00 25.20 ? 403  ILE   A CG1   1 
ATOM   2976  C  CG2   . ILE   A  1  405  ? -49.492 38.835  87.417  1.00 24.66 ? 403  ILE   A CG2   1 
ATOM   2977  C  CD1   . ILE   A  1  405  ? -46.379 38.450  86.935  1.00 27.80 ? 403  ILE   A CD1   1 
ATOM   2978  N  N     . ALA   A  1  406  ? -49.973 42.033  89.361  1.00 20.26 ? 404  ALA   A N     1 
ATOM   2979  C  CA    . ALA   A  1  406  ? -51.100 42.441  90.197  1.00 20.66 ? 404  ALA   A CA    1 
ATOM   2980  C  C     . ALA   A  1  406  ? -51.850 43.602  89.568  1.00 19.80 ? 404  ALA   A C     1 
ATOM   2981  O  O     . ALA   A  1  406  ? -53.089 43.638  89.575  1.00 22.37 ? 404  ALA   A O     1 
ATOM   2982  C  CB    . ALA   A  1  406  ? -50.599 42.872  91.565  1.00 20.22 ? 404  ALA   A CB    1 
ATOM   2983  N  N     . CYS   A  1  407  ? -51.111 44.583  89.044  1.00 18.81 ? 405  CYS   A N     1 
ATOM   2984  C  CA    . CYS   A  1  407  ? -51.751 45.731  88.418  1.00 19.75 ? 405  CYS   A CA    1 
ATOM   2985  C  C     . CYS   A  1  407  ? -52.454 45.339  87.128  1.00 19.68 ? 405  CYS   A C     1 
ATOM   2986  O  O     . CYS   A  1  407  ? -53.504 45.907  86.795  1.00 19.96 ? 405  CYS   A O     1 
ATOM   2987  C  CB    . CYS   A  1  407  ? -50.713 46.830  88.216  1.00 21.55 ? 405  CYS   A CB    1 
ATOM   2988  S  SG    . CYS   A  1  407  ? -50.284 47.573  89.807  1.00 24.45 ? 405  CYS   A SG    1 
ATOM   2989  N  N     . ALA   A  1  408  ? -51.916 44.345  86.411  1.00 19.31 ? 406  ALA   A N     1 
ATOM   2990  C  CA    . ALA   A  1  408  ? -52.597 43.837  85.229  1.00 21.57 ? 406  ALA   A CA    1 
ATOM   2991  C  C     . ALA   A  1  408  ? -53.922 43.187  85.591  1.00 18.88 ? 406  ALA   A C     1 
ATOM   2992  O  O     . ALA   A  1  408  ? -54.890 43.293  84.837  1.00 21.02 ? 406  ALA   A O     1 
ATOM   2993  C  CB    . ALA   A  1  408  ? -51.706 42.840  84.491  1.00 22.09 ? 406  ALA   A CB    1 
ATOM   2994  N  N     . ALA   A  1  409  ? -53.971 42.482  86.720  1.00 20.63 ? 407  ALA   A N     1 
ATOM   2995  C  CA    . ALA   A  1  409  ? -55.234 41.915  87.171  1.00 20.24 ? 407  ALA   A CA    1 
ATOM   2996  C  C     . ALA   A  1  409  ? -56.253 43.007  87.453  1.00 21.16 ? 407  ALA   A C     1 
ATOM   2997  O  O     . ALA   A  1  409  ? -57.432 42.860  87.126  1.00 22.87 ? 407  ALA   A O     1 
ATOM   2998  C  CB    . ALA   A  1  409  ? -55.004 41.052  88.412  1.00 24.45 ? 407  ALA   A CB    1 
ATOM   2999  N  N     . LYS   A  1  410  ? -55.812 44.113  88.060  1.00 20.21 ? 408  LYS   A N     1 
ATOM   3000  C  CA    . LYS   A  1  410  ? -56.722 45.226  88.304  1.00 20.40 ? 408  LYS   A CA    1 
ATOM   3001  C  C     . LYS   A  1  410  ? -57.231 45.811  86.991  1.00 20.07 ? 408  LYS   A C     1 
ATOM   3002  O  O     . LYS   A  1  410  ? -58.427 46.070  86.827  1.00 20.19 ? 408  LYS   A O     1 
ATOM   3003  C  CB    . LYS   A  1  410  ? -56.012 46.298  89.126  1.00 21.04 ? 408  LYS   A CB    1 
ATOM   3004  C  CG    . LYS   A  1  410  ? -56.886 47.505  89.469  1.00 21.48 ? 408  LYS   A CG    1 
ATOM   3005  C  CD    . LYS   A  1  410  ? -56.087 48.539  90.244  1.00 23.87 ? 408  LYS   A CD    1 
ATOM   3006  C  CE    . LYS   A  1  410  ? -55.601 48.020  91.584  1.00 25.02 ? 408  LYS   A CE    1 
ATOM   3007  N  NZ    . LYS   A  1  410  ? -56.714 48.031  92.560  1.00 26.77 ? 408  LYS   A NZ    1 
ATOM   3008  N  N     . LEU   A  1  411  ? -56.321 46.036  86.040  1.00 18.55 ? 409  LEU   A N     1 
ATOM   3009  C  CA    . LEU   A  1  411  ? -56.718 46.589  84.751  1.00 18.04 ? 409  LEU   A CA    1 
ATOM   3010  C  C     . LEU   A  1  411  ? -57.642 45.644  83.993  1.00 17.61 ? 409  LEU   A C     1 
ATOM   3011  O  O     . LEU   A  1  411  ? -58.608 46.085  83.364  1.00 18.67 ? 409  LEU   A O     1 
ATOM   3012  C  CB    . LEU   A  1  411  ? -55.464 46.899  83.929  1.00 18.12 ? 409  LEU   A CB    1 
ATOM   3013  C  CG    . LEU   A  1  411  ? -54.739 48.158  84.379  1.00 18.44 ? 409  LEU   A CG    1 
ATOM   3014  C  CD1   . LEU   A  1  411  ? -53.320 48.209  83.818  1.00 18.40 ? 409  LEU   A CD1   1 
ATOM   3015  C  CD2   . LEU   A  1  411  ? -55.513 49.392  83.982  1.00 18.35 ? 409  LEU   A CD2   1 
ATOM   3016  N  N     . LEU   A  1  412  ? -57.367 44.334  84.045  1.00 19.08 ? 410  LEU   A N     1 
ATOM   3017  C  CA    . LEU   A  1  412  ? -58.188 43.404  83.281  1.00 20.16 ? 410  LEU   A CA    1 
ATOM   3018  C  C     . LEU   A  1  412  ? -59.587 43.270  83.849  1.00 21.95 ? 410  LEU   A C     1 
ATOM   3019  O  O     . LEU   A  1  412  ? -60.485 42.822  83.133  1.00 24.86 ? 410  LEU   A O     1 
ATOM   3020  C  CB    . LEU   A  1  412  ? -57.512 42.034  83.169  1.00 21.95 ? 410  LEU   A CB    1 
ATOM   3021  C  CG    . LEU   A  1  412  ? -56.326 42.020  82.193  1.00 20.52 ? 410  LEU   A CG    1 
ATOM   3022  C  CD1   . LEU   A  1  412  ? -55.575 40.713  82.306  1.00 24.46 ? 410  LEU   A CD1   1 
ATOM   3023  C  CD2   . LEU   A  1  412  ? -56.802 42.226  80.784  1.00 23.60 ? 410  LEU   A CD2   1 
ATOM   3024  N  N     . ALA   A  1  413  ? -59.796 43.663  85.101  1.00 20.40 ? 411  ALA   A N     1 
ATOM   3025  C  CA    . ALA   A  1  413  ? -61.139 43.696  85.670  1.00 22.34 ? 411  ALA   A CA    1 
ATOM   3026  C  C     . ALA   A  1  413  ? -61.909 44.948  85.282  1.00 22.63 ? 411  ALA   A C     1 
ATOM   3027  O  O     . ALA   A  1  413  ? -63.087 45.076  85.627  1.00 25.17 ? 411  ALA   A O     1 
ATOM   3028  C  CB    . ALA   A  1  413  ? -61.068 43.598  87.196  1.00 23.78 ? 411  ALA   A CB    1 
ATOM   3029  N  N     . ALA   A  1  414  ? -61.274 45.864  84.560  1.00 19.96 ? 412  ALA   A N     1 
ATOM   3030  C  CA    . ALA   A  1  414  ? -61.826 47.181  84.284  1.00 22.34 ? 412  ALA   A CA    1 
ATOM   3031  C  C     . ALA   A  1  414  ? -61.771 47.522  82.800  1.00 20.06 ? 412  ALA   A C     1 
ATOM   3032  O  O     . ALA   A  1  414  ? -61.801 48.698  82.448  1.00 19.90 ? 412  ALA   A O     1 
ATOM   3033  C  CB    . ALA   A  1  414  ? -61.096 48.250  85.106  1.00 23.48 ? 412  ALA   A CB    1 
ATOM   3034  N  N     . THR   A  1  415  ? -61.715 46.510  81.921  1.00 20.77 ? 413  THR   A N     1 
ATOM   3035  C  CA    . THR   A  1  415  ? -61.631 46.774  80.487  1.00 20.40 ? 413  THR   A CA    1 
ATOM   3036  C  C     . THR   A  1  415  ? -62.863 47.472  79.933  1.00 20.90 ? 413  THR   A C     1 
ATOM   3037  O  O     . THR   A  1  415  ? -62.793 48.022  78.829  1.00 23.49 ? 413  THR   A O     1 
ATOM   3038  C  CB    . THR   A  1  415  ? -61.337 45.503  79.681  1.00 21.92 ? 413  THR   A CB    1 
ATOM   3039  O  OG1   . THR   A  1  415  ? -62.411 44.569  79.846  1.00 25.50 ? 413  THR   A OG1   1 
ATOM   3040  C  CG2   . THR   A  1  415  ? -60.055 44.855  80.153  1.00 24.81 ? 413  THR   A CG2   1 
ATOM   3041  N  N     . ASP   A  1  416  ? -63.988 47.471  80.657  1.00 22.33 ? 414  ASP   A N     1 
ATOM   3042  C  CA    . ASP   A  1  416  ? -65.110 48.271  80.182  1.00 21.25 ? 414  ASP   A CA    1 
ATOM   3043  C  C     . ASP   A  1  416  ? -64.845 49.764  80.322  1.00 21.90 ? 414  ASP   A C     1 
ATOM   3044  O  O     . ASP   A  1  416  ? -65.420 50.555  79.572  1.00 27.78 ? 414  ASP   A O     1 
ATOM   3045  C  CB    . ASP   A  1  416  ? -66.414 47.868  80.877  1.00 26.86 ? 414  ASP   A CB    1 
ATOM   3046  C  CG    . ASP   A  1  416  ? -66.341 48.016  82.375  1.00 35.12 ? 414  ASP   A CG    1 
ATOM   3047  O  OD1   . ASP   A  1  416  ? -65.294 47.657  82.962  1.00 34.37 ? 414  ASP   A OD1   1 
ATOM   3048  O  OD2   . ASP   A  1  416  ? -67.334 48.497  82.969  1.00 43.37 ? 414  ASP   A OD2   1 
ATOM   3049  N  N     . VAL   A  1  417  ? -63.975 50.172  81.243  1.00 21.76 ? 415  VAL   A N     1 
ATOM   3050  C  CA    . VAL   A  1  417  ? -63.786 51.589  81.512  1.00 22.83 ? 415  VAL   A CA    1 
ATOM   3051  C  C     . VAL   A  1  417  ? -62.399 52.107  81.160  1.00 19.38 ? 415  VAL   A C     1 
ATOM   3052  O  O     . VAL   A  1  417  ? -62.253 53.323  80.967  1.00 19.89 ? 415  VAL   A O     1 
ATOM   3053  C  CB    . VAL   A  1  417  ? -64.166 51.982  82.951  1.00 29.54 ? 415  VAL   A CB    1 
ATOM   3054  C  CG1   . VAL   A  1  417  ? -65.595 51.552  83.245  1.00 32.27 ? 415  VAL   A CG1   1 
ATOM   3055  C  CG2   . VAL   A  1  417  ? -63.229 51.359  83.916  1.00 25.27 ? 415  VAL   A CG2   1 
ATOM   3056  N  N     . VAL   A  1  418  ? -61.386 51.242  81.064  1.00 18.69 ? 416  VAL   A N     1 
ATOM   3057  C  CA    . VAL   A  1  418  ? -60.062 51.619  80.576  1.00 17.58 ? 416  VAL   A CA    1 
ATOM   3058  C  C     . VAL   A  1  418  ? -59.623 50.626  79.509  1.00 17.18 ? 416  VAL   A C     1 
ATOM   3059  O  O     . VAL   A  1  418  ? -60.144 49.515  79.400  1.00 18.56 ? 416  VAL   A O     1 
ATOM   3060  C  CB    . VAL   A  1  418  ? -58.996 51.717  81.694  1.00 17.46 ? 416  VAL   A CB    1 
ATOM   3061  C  CG1   . VAL   A  1  418  ? -59.336 52.846  82.668  1.00 20.31 ? 416  VAL   A CG1   1 
ATOM   3062  C  CG2   . VAL   A  1  418  ? -58.848 50.384  82.413  1.00 20.26 ? 416  VAL   A CG2   1 
ATOM   3063  N  N     . PHE   A  1  419  ? -58.619 51.031  78.737  1.00 16.68 ? 417  PHE   A N     1 
ATOM   3064  C  CA    . PHE   A  1  419  ? -58.018 50.176  77.719  1.00 18.69 ? 417  PHE   A CA    1 
ATOM   3065  C  C     . PHE   A  1  419  ? -56.618 49.837  78.193  1.00 16.93 ? 417  PHE   A C     1 
ATOM   3066  O  O     . PHE   A  1  419  ? -55.705 50.669  78.061  1.00 17.14 ? 417  PHE   A O     1 
ATOM   3067  C  CB    . PHE   A  1  419  ? -57.958 50.911  76.377  1.00 17.88 ? 417  PHE   A CB    1 
ATOM   3068  C  CG    . PHE   A  1  419  ? -57.252 50.146  75.288  1.00 17.30 ? 417  PHE   A CG    1 
ATOM   3069  C  CD1   . PHE   A  1  419  ? -57.704 48.902  74.876  1.00 18.88 ? 417  PHE   A CD1   1 
ATOM   3070  C  CD2   . PHE   A  1  419  ? -56.151 50.686  74.658  1.00 17.74 ? 417  PHE   A CD2   1 
ATOM   3071  C  CE1   . PHE   A  1  419  ? -57.073 48.216  73.848  1.00 19.25 ? 417  PHE   A CE1   1 
ATOM   3072  C  CE2   . PHE   A  1  419  ? -55.510 50.000  73.637  1.00 17.49 ? 417  PHE   A CE2   1 
ATOM   3073  C  CZ    . PHE   A  1  419  ? -55.962 48.777  73.238  1.00 17.81 ? 417  PHE   A CZ    1 
ATOM   3074  N  N     . PRO   A  1  420  ? -56.390 48.646  78.742  1.00 15.88 ? 418  PRO   A N     1 
ATOM   3075  C  CA    . PRO   A  1  420  ? -55.055 48.314  79.251  1.00 16.35 ? 418  PRO   A CA    1 
ATOM   3076  C  C     . PRO   A  1  420  ? -54.102 48.031  78.110  1.00 16.38 ? 418  PRO   A C     1 
ATOM   3077  O  O     . PRO   A  1  420  ? -54.458 47.403  77.113  1.00 17.21 ? 418  PRO   A O     1 
ATOM   3078  C  CB    . PRO   A  1  420  ? -55.293 47.051  80.090  1.00 16.55 ? 418  PRO   A CB    1 
ATOM   3079  C  CG    . PRO   A  1  420  ? -56.792 46.997  80.303  1.00 18.28 ? 418  PRO   A CG    1 
ATOM   3080  C  CD    . PRO   A  1  420  ? -57.366 47.591  79.056  1.00 17.28 ? 418  PRO   A CD    1 
ATOM   3081  N  N     . GLN   A  1  421  ? -52.874 48.508  78.280  1.00 15.57 ? 419  GLN   A N     1 
ATOM   3082  C  CA    . GLN   A  1  421  ? -51.811 48.336  77.297  1.00 15.41 ? 419  GLN   A CA    1 
ATOM   3083  C  C     . GLN   A  1  421  ? -50.609 47.812  78.060  1.00 16.97 ? 419  GLN   A C     1 
ATOM   3084  O  O     . GLN   A  1  421  ? -50.010 48.537  78.860  1.00 17.63 ? 419  GLN   A O     1 
ATOM   3085  C  CB    . GLN   A  1  421  ? -51.508 49.662  76.614  1.00 14.85 ? 419  GLN   A CB    1 
ATOM   3086  C  CG    . GLN   A  1  421  ? -52.734 50.283  75.985  1.00 17.00 ? 419  GLN   A CG    1 
ATOM   3087  C  CD    . GLN   A  1  421  ? -52.513 51.739  75.656  1.00 15.43 ? 419  GLN   A CD    1 
ATOM   3088  O  OE1   . GLN   A  1  421  ? -52.294 52.560  76.546  1.00 17.74 ? 419  GLN   A OE1   1 
ATOM   3089  N  NE2   . GLN   A  1  421  ? -52.580 52.072  74.376  1.00 17.33 ? 419  GLN   A NE2   1 
ATOM   3090  N  N     . PHE   A  1  422  ? -50.277 46.550  77.843  1.00 15.66 ? 420  PHE   A N     1 
ATOM   3091  C  CA    . PHE   A  1  422  ? -49.263 45.880  78.646  1.00 14.69 ? 420  PHE   A CA    1 
ATOM   3092  C  C     . PHE   A  1  422  ? -47.923 45.962  77.929  1.00 15.17 ? 420  PHE   A C     1 
ATOM   3093  O  O     . PHE   A  1  422  ? -47.620 45.148  77.053  1.00 17.58 ? 420  PHE   A O     1 
ATOM   3094  C  CB    . PHE   A  1  422  ? -49.694 44.455  78.947  1.00 17.29 ? 420  PHE   A CB    1 
ATOM   3095  C  CG    . PHE   A  1  422  ? -50.972 44.392  79.715  1.00 18.47 ? 420  PHE   A CG    1 
ATOM   3096  C  CD1   . PHE   A  1  422  ? -51.022 44.878  81.005  1.00 19.74 ? 420  PHE   A CD1   1 
ATOM   3097  C  CD2   . PHE   A  1  422  ? -52.120 43.882  79.141  1.00 18.00 ? 420  PHE   A CD2   1 
ATOM   3098  C  CE1   . PHE   A  1  422  ? -52.198 44.835  81.720  1.00 19.06 ? 420  PHE   A CE1   1 
ATOM   3099  C  CE2   . PHE   A  1  422  ? -53.300 43.834  79.858  1.00 20.15 ? 420  PHE   A CE2   1 
ATOM   3100  C  CZ    . PHE   A  1  422  ? -53.329 44.318  81.143  1.00 20.07 ? 420  PHE   A CZ    1 
ATOM   3101  N  N     . ALA   A  1  423  ? -47.128 46.949  78.317  1.00 15.84 ? 421  ALA   A N     1 
ATOM   3102  C  CA    . ALA   A  1  423  ? -45.825 47.173  77.704  1.00 15.66 ? 421  ALA   A CA    1 
ATOM   3103  C  C     . ALA   A  1  423  ? -44.803 46.320  78.438  1.00 17.75 ? 421  ALA   A C     1 
ATOM   3104  O  O     . ALA   A  1  423  ? -44.489 46.580  79.604  1.00 19.46 ? 421  ALA   A O     1 
ATOM   3105  C  CB    . ALA   A  1  423  ? -45.466 48.648  77.799  1.00 16.14 ? 421  ALA   A CB    1 
ATOM   3106  N  N     . THR   A  1  424  ? -44.287 45.301  77.764  1.00 17.08 ? 422  THR   A N     1 
ATOM   3107  C  CA    . THR   A  1  424  ? -43.252 44.479  78.377  1.00 17.83 ? 422  THR   A CA    1 
ATOM   3108  C  C     . THR   A  1  424  ? -42.554 43.666  77.301  1.00 18.60 ? 422  THR   A C     1 
ATOM   3109  O  O     . THR   A  1  424  ? -43.160 43.260  76.309  1.00 19.77 ? 422  THR   A O     1 
ATOM   3110  C  CB    . THR   A  1  424  ? -43.808 43.540  79.457  1.00 20.21 ? 422  THR   A CB    1 
ATOM   3111  O  OG1   . THR   A  1  424  ? -42.711 42.833  80.056  1.00 21.12 ? 422  THR   A OG1   1 
ATOM   3112  C  CG2   . THR   A  1  424  ? -44.764 42.540  78.850  1.00 22.90 ? 422  THR   A CG2   1 
ATOM   3113  N  N     . HIS   A  1  425  ? -41.268 43.435  77.517  1.00 18.75 ? 423  HIS   A N     1 
ATOM   3114  C  CA    . HIS   A  1  425  ? -40.507 42.519  76.690  1.00 18.94 ? 423  HIS   A CA    1 
ATOM   3115  C  C     . HIS   A  1  425  ? -40.281 41.192  77.376  1.00 21.19 ? 423  HIS   A C     1 
ATOM   3116  O  O     . HIS   A  1  425  ? -39.580 40.334  76.829  1.00 23.59 ? 423  HIS   A O     1 
ATOM   3117  C  CB    . HIS   A  1  425  ? -39.156 43.135  76.346  1.00 20.00 ? 423  HIS   A CB    1 
ATOM   3118  C  CG    . HIS   A  1  425  ? -39.271 44.393  75.560  1.00 18.95 ? 423  HIS   A CG    1 
ATOM   3119  N  ND1   . HIS   A  1  425  ? -38.524 45.515  75.844  1.00 21.25 ? 423  HIS   A ND1   1 
ATOM   3120  C  CD2   . HIS   A  1  425  ? -40.066 44.720  74.514  1.00 21.20 ? 423  HIS   A CD2   1 
ATOM   3121  C  CE1   . HIS   A  1  425  ? -38.844 46.477  74.995  1.00 21.86 ? 423  HIS   A CE1   1 
ATOM   3122  N  NE2   . HIS   A  1  425  ? -39.777 46.019  74.180  1.00 19.92 ? 423  HIS   A NE2   1 
ATOM   3123  N  N     . ASN   A  1  426  ? -40.860 40.999  78.551  1.00 20.23 ? 424  ASN   A N     1 
ATOM   3124  C  CA    . ASN   A  1  426  ? -40.605 39.810  79.357  1.00 22.63 ? 424  ASN   A CA    1 
ATOM   3125  C  C     . ASN   A  1  426  ? -41.655 38.758  79.001  1.00 22.23 ? 424  ASN   A C     1 
ATOM   3126  O  O     . ASN   A  1  426  ? -42.849 38.949  79.255  1.00 21.97 ? 424  ASN   A O     1 
ATOM   3127  C  CB    . ASN   A  1  426  ? -40.639 40.217  80.829  1.00 20.78 ? 424  ASN   A CB    1 
ATOM   3128  C  CG    . ASN   A  1  426  ? -40.270 39.090  81.762  1.00 21.48 ? 424  ASN   A CG    1 
ATOM   3129  O  OD1   . ASN   A  1  426  ? -40.698 37.959  81.568  1.00 24.31 ? 424  ASN   A OD1   1 
ATOM   3130  N  ND2   . ASN   A  1  426  ? -39.476 39.400  82.792  1.00 21.84 ? 424  ASN   A ND2   1 
ATOM   3131  N  N     . ALA   A  1  427  ? -41.211 37.644  78.401  1.00 20.77 ? 425  ALA   A N     1 
ATOM   3132  C  CA    . ALA   A  1  427  ? -42.139 36.608  77.953  1.00 21.75 ? 425  ALA   A CA    1 
ATOM   3133  C  C     . ALA   A  1  427  ? -42.898 35.970  79.112  1.00 21.29 ? 425  ALA   A C     1 
ATOM   3134  O  O     . ALA   A  1  427  ? -44.021 35.486  78.924  1.00 21.92 ? 425  ALA   A O     1 
ATOM   3135  C  CB    . ALA   A  1  427  ? -41.378 35.528  77.180  1.00 24.93 ? 425  ALA   A CB    1 
ATOM   3136  N  N     . GLN   A  1  428  ? -42.299 35.934  80.300  1.00 22.12 ? 426  GLN   A N     1 
ATOM   3137  C  CA    . GLN   A  1  428  ? -43.013 35.410  81.459  1.00 24.06 ? 426  GLN   A CA    1 
ATOM   3138  C  C     . GLN   A  1  428  ? -44.152 36.344  81.838  1.00 22.84 ? 426  GLN   A C     1 
ATOM   3139  O  O     . GLN   A  1  428  ? -45.293 35.902  82.036  1.00 23.36 ? 426  GLN   A O     1 
ATOM   3140  C  CB    . GLN   A  1  428  ? -42.045 35.230  82.630  1.00 21.77 ? 426  GLN   A CB    1 
ATOM   3141  C  CG    . GLN   A  1  428  ? -42.575 34.305  83.732  1.00 24.56 ? 426  GLN   A CG    1 
ATOM   3142  C  CD    . GLN   A  1  428  ? -43.676 34.930  84.568  1.00 29.38 ? 426  GLN   A CD    1 
ATOM   3143  O  OE1   . GLN   A  1  428  ? -43.636 36.121  84.884  1.00 28.84 ? 426  GLN   A OE1   1 
ATOM   3144  N  NE2   . GLN   A  1  428  ? -44.671 34.124  84.932  1.00 27.70 ? 426  GLN   A NE2   1 
ATOM   3145  N  N     . THR   A  1  429  ? -43.853 37.643  81.941  1.00 22.08 ? 427  THR   A N     1 
ATOM   3146  C  CA    . THR   A  1  429  ? -44.886 38.636  82.210  1.00 21.85 ? 427  THR   A CA    1 
ATOM   3147  C  C     . THR   A  1  429  ? -45.989 38.556  81.167  1.00 21.35 ? 427  THR   A C     1 
ATOM   3148  O  O     . THR   A  1  429  ? -47.182 38.534  81.499  1.00 21.48 ? 427  THR   A O     1 
ATOM   3149  C  CB    . THR   A  1  429  ? -44.262 40.032  82.188  1.00 21.29 ? 427  THR   A CB    1 
ATOM   3150  O  OG1   . THR   A  1  429  ? -43.091 40.054  83.007  1.00 22.19 ? 427  THR   A OG1   1 
ATOM   3151  C  CG2   . THR   A  1  429  ? -45.243 41.045  82.729  1.00 23.33 ? 427  THR   A CG2   1 
ATOM   3152  N  N     . LEU   A  1  430  ? -45.600 38.481  79.894  1.00 21.61 ? 428  LEU   A N     1 
ATOM   3153  C  CA    . LEU   A  1  430  ? -46.566 38.439  78.805  1.00 21.24 ? 428  LEU   A CA    1 
ATOM   3154  C  C     . LEU   A  1  430  ? -47.477 37.229  78.935  1.00 22.20 ? 428  LEU   A C     1 
ATOM   3155  O  O     . LEU   A  1  430  ? -48.706 37.343  78.854  1.00 22.30 ? 428  LEU   A O     1 
ATOM   3156  C  CB    . LEU   A  1  430  ? -45.798 38.384  77.481  1.00 20.48 ? 428  LEU   A CB    1 
ATOM   3157  C  CG    . LEU   A  1  430  ? -46.461 38.628  76.125  1.00 24.46 ? 428  LEU   A CG    1 
ATOM   3158  C  CD1   . LEU   A  1  430  ? -45.351 38.756  75.109  1.00 27.18 ? 428  LEU   A CD1   1 
ATOM   3159  C  CD2   . LEU   A  1  430  ? -47.408 37.511  75.708  1.00 26.20 ? 428  LEU   A CD2   1 
ATOM   3160  N  N     . ALA   A  1  431  ? -46.878 36.049  79.109  1.00 23.99 ? 429  ALA   A N     1 
ATOM   3161  C  CA    . ALA   A  1  431  ? -47.657 34.819  79.168  1.00 24.26 ? 429  ALA   A CA    1 
ATOM   3162  C  C     . ALA   A  1  431  ? -48.623 34.831  80.342  1.00 24.16 ? 429  ALA   A C     1 
ATOM   3163  O  O     . ALA   A  1  431  ? -49.766 34.379  80.219  1.00 23.00 ? 429  ALA   A O     1 
ATOM   3164  C  CB    . ALA   A  1  431  ? -46.708 33.630  79.287  1.00 23.92 ? 429  ALA   A CB    1 
ATOM   3165  N  N     . ALA   A  1  432  ? -48.179 35.355  81.485  1.00 22.79 ? 430  ALA   A N     1 
ATOM   3166  C  CA    . ALA   A  1  432  ? -49.040 35.420  82.660  1.00 24.04 ? 430  ALA   A CA    1 
ATOM   3167  C  C     . ALA   A  1  432  ? -50.276 36.260  82.385  1.00 25.55 ? 430  ALA   A C     1 
ATOM   3168  O  O     . ALA   A  1  432  ? -51.386 35.904  82.795  1.00 25.54 ? 430  ALA   A O     1 
ATOM   3169  C  CB    . ALA   A  1  432  ? -48.261 35.998  83.838  1.00 24.72 ? 430  ALA   A CB    1 
ATOM   3170  N  N     . ILE   A  1  433  ? -50.104 37.373  81.682  1.00 23.36 ? 431  ILE   A N     1 
ATOM   3171  C  CA    . ILE   A  1  433  ? -51.225 38.257  81.407  1.00 21.51 ? 431  ILE   A CA    1 
ATOM   3172  C  C     . ILE   A  1  433  ? -52.094 37.698  80.300  1.00 22.79 ? 431  ILE   A C     1 
ATOM   3173  O  O     . ILE   A  1  433  ? -53.325 37.787  80.356  1.00 22.04 ? 431  ILE   A O     1 
ATOM   3174  C  CB    . ILE   A  1  433  ? -50.668 39.648  81.070  1.00 22.37 ? 431  ILE   A CB    1 
ATOM   3175  C  CG1   . ILE   A  1  433  ? -50.032 40.232  82.332  1.00 25.30 ? 431  ILE   A CG1   1 
ATOM   3176  C  CG2   . ILE   A  1  433  ? -51.751 40.538  80.477  1.00 23.37 ? 431  ILE   A CG2   1 
ATOM   3177  C  CD1   . ILE   A  1  433  ? -49.337 41.518  82.105  1.00 26.90 ? 431  ILE   A CD1   1 
ATOM   3178  N  N     . TYR   A  1  434  ? -51.472 37.109  79.277  1.00 22.56 ? 432  TYR   A N     1 
ATOM   3179  C  CA    . TYR   A  1  434  ? -52.232 36.492  78.199  1.00 23.04 ? 432  TYR   A CA    1 
ATOM   3180  C  C     . TYR   A  1  434  ? -53.226 35.477  78.743  1.00 23.57 ? 432  TYR   A C     1 
ATOM   3181  O  O     . TYR   A  1  434  ? -54.383 35.429  78.308  1.00 25.02 ? 432  TYR   A O     1 
ATOM   3182  C  CB    . TYR   A  1  434  ? -51.252 35.830  77.232  1.00 26.02 ? 432  TYR   A CB    1 
ATOM   3183  C  CG    . TYR   A  1  434  ? -51.876 34.904  76.230  1.00 24.19 ? 432  TYR   A CG    1 
ATOM   3184  C  CD1   . TYR   A  1  434  ? -52.694 35.390  75.224  1.00 25.52 ? 432  TYR   A CD1   1 
ATOM   3185  C  CD2   . TYR   A  1  434  ? -51.637 33.532  76.283  1.00 27.61 ? 432  TYR   A CD2   1 
ATOM   3186  C  CE1   . TYR   A  1  434  ? -53.263 34.543  74.301  1.00 26.73 ? 432  TYR   A CE1   1 
ATOM   3187  C  CE2   . TYR   A  1  434  ? -52.193 32.678  75.363  1.00 30.48 ? 432  TYR   A CE2   1 
ATOM   3188  C  CZ    . TYR   A  1  434  ? -53.009 33.184  74.375  1.00 31.64 ? 432  TYR   A CZ    1 
ATOM   3189  O  OH    . TYR   A  1  434  ? -53.567 32.332  73.455  1.00 34.55 ? 432  TYR   A OH    1 
ATOM   3190  N  N     . HIS   A  1  435  ? -52.795 34.661  79.699  1.00 25.05 ? 433  HIS   A N     1 
ATOM   3191  C  CA    . HIS   A  1  435  ? -53.697 33.669  80.267  1.00 26.92 ? 433  HIS   A CA    1 
ATOM   3192  C  C     . HIS   A  1  435  ? -54.641 34.281  81.283  1.00 27.57 ? 433  HIS   A C     1 
ATOM   3193  O  O     . HIS   A  1  435  ? -55.801 33.863  81.369  1.00 27.20 ? 433  HIS   A O     1 
ATOM   3194  C  CB    . HIS   A  1  435  ? -52.907 32.516  80.865  1.00 28.84 ? 433  HIS   A CB    1 
ATOM   3195  C  CG    . HIS   A  1  435  ? -52.296 31.632  79.830  1.00 29.85 ? 433  HIS   A CG    1 
ATOM   3196  N  ND1   . HIS   A  1  435  ? -52.991 30.605  79.231  1.00 31.27 ? 433  HIS   A ND1   1 
ATOM   3197  C  CD2   . HIS   A  1  435  ? -51.079 31.660  79.239  1.00 25.76 ? 433  HIS   A CD2   1 
ATOM   3198  C  CE1   . HIS   A  1  435  ? -52.216 30.015  78.338  1.00 31.18 ? 433  HIS   A CE1   1 
ATOM   3199  N  NE2   . HIS   A  1  435  ? -51.050 30.635  78.324  1.00 28.48 ? 433  HIS   A NE2   1 
ATOM   3200  N  N     . MET   A  1  436  ? -54.171 35.273  82.039  1.00 25.68 ? 434  MET   A N     1 
ATOM   3201  C  CA    . MET   A  1  436  ? -55.055 35.988  82.953  1.00 26.91 ? 434  MET   A CA    1 
ATOM   3202  C  C     . MET   A  1  436  ? -56.223 36.623  82.212  1.00 23.63 ? 434  MET   A C     1 
ATOM   3203  O  O     . MET   A  1  436  ? -57.357 36.620  82.705  1.00 26.41 ? 434  MET   A O     1 
ATOM   3204  C  CB    . MET   A  1  436  ? -54.262 37.060  83.683  1.00 26.60 ? 434  MET   A CB    1 
ATOM   3205  C  CG    . MET   A  1  436  ? -55.048 37.765  84.750  1.00 26.03 ? 434  MET   A CG    1 
ATOM   3206  S  SD    . MET   A  1  436  ? -54.152 39.196  85.344  1.00 26.39 ? 434  MET   A SD    1 
ATOM   3207  C  CE    . MET   A  1  436  ? -52.900 38.411  86.353  1.00 29.39 ? 434  MET   A CE    1 
ATOM   3208  N  N     . ALA   A  1  437  ? -55.972 37.166  81.020  1.00 22.71 ? 435  ALA   A N     1 
ATOM   3209  C  CA    . ALA   A  1  437  ? -57.020 37.858  80.277  1.00 25.40 ? 435  ALA   A CA    1 
ATOM   3210  C  C     . ALA   A  1  437  ? -58.042 36.890  79.697  1.00 28.66 ? 435  ALA   A C     1 
ATOM   3211  O  O     . ALA   A  1  437  ? -59.188 37.277  79.455  1.00 27.63 ? 435  ALA   A O     1 
ATOM   3212  C  CB    . ALA   A  1  437  ? -56.406 38.716  79.175  1.00 26.38 ? 435  ALA   A CB    1 
ATOM   3213  N  N     . GLY   A  1  438  ? -57.652 35.641  79.458  1.00 31.92 ? 436  GLY   A N     1 
ATOM   3214  C  CA    . GLY   A  1  438  ? -58.602 34.635  79.032  1.00 33.45 ? 436  GLY   A CA    1 
ATOM   3215  C  C     . GLY   A  1  438  ? -58.844 34.618  77.540  1.00 31.44 ? 436  GLY   A C     1 
ATOM   3216  O  O     . GLY   A  1  438  ? -58.242 35.353  76.754  1.00 30.26 ? 436  GLY   A O     1 
ATOM   3217  N  N     . LYS   A  1  439  ? -59.785 33.755  77.148  1.00 37.70 ? 437  LYS   A N     1 
ATOM   3218  C  CA    . LYS   A  1  439  ? -59.997 33.445  75.740  1.00 38.87 ? 437  LYS   A CA    1 
ATOM   3219  C  C     . LYS   A  1  439  ? -60.893 34.449  75.031  1.00 34.15 ? 437  LYS   A C     1 
ATOM   3220  O  O     . LYS   A  1  439  ? -60.829 34.545  73.802  1.00 44.19 ? 437  LYS   A O     1 
ATOM   3221  C  CB    . LYS   A  1  439  ? -60.586 32.039  75.592  1.00 45.63 ? 437  LYS   A CB    1 
ATOM   3222  N  N     . ASP   A  1  440  ? -61.720 35.195  75.764  1.00 28.87 ? 438  ASP   A N     1 
ATOM   3223  C  CA    . ASP   A  1  440  ? -62.579 36.207  75.160  1.00 37.91 ? 438  ASP   A CA    1 
ATOM   3224  C  C     . ASP   A  1  440  ? -61.729 37.417  74.803  1.00 37.59 ? 438  ASP   A C     1 
ATOM   3225  O  O     . ASP   A  1  440  ? -61.238 38.124  75.690  1.00 38.27 ? 438  ASP   A O     1 
ATOM   3226  C  CB    . ASP   A  1  440  ? -63.693 36.606  76.121  1.00 40.08 ? 438  ASP   A CB    1 
ATOM   3227  C  CG    . ASP   A  1  440  ? -64.791 35.566  76.202  1.00 46.54 ? 438  ASP   A CG    1 
ATOM   3228  O  OD1   . ASP   A  1  440  ? -64.681 34.530  75.509  1.00 42.42 ? 438  ASP   A OD1   1 
ATOM   3229  O  OD2   . ASP   A  1  440  ? -65.760 35.788  76.959  1.00 45.74 ? 438  ASP   A OD2   1 
ATOM   3230  N  N     . PHE   A  1  441  ? -61.560 37.669  73.509  1.00 30.19 ? 439  PHE   A N     1 
ATOM   3231  C  CA    . PHE   A  1  441  ? -60.771 38.808  73.084  1.00 27.90 ? 439  PHE   A CA    1 
ATOM   3232  C  C     . PHE   A  1  441  ? -61.411 39.475  71.882  1.00 30.85 ? 439  PHE   A C     1 
ATOM   3233  O  O     . PHE   A  1  441  ? -61.993 38.821  71.016  1.00 31.29 ? 439  PHE   A O     1 
ATOM   3234  C  CB    . PHE   A  1  441  ? -59.312 38.458  72.744  1.00 24.64 ? 439  PHE   A CB    1 
ATOM   3235  C  CG    . PHE   A  1  441  ? -58.493 39.668  72.421  1.00 26.18 ? 439  PHE   A CG    1 
ATOM   3236  C  CD1   . PHE   A  1  441  ? -57.998 40.463  73.440  1.00 24.43 ? 439  PHE   A CD1   1 
ATOM   3237  C  CD2   . PHE   A  1  441  ? -58.289 40.063  71.104  1.00 25.01 ? 439  PHE   A CD2   1 
ATOM   3238  C  CE1   . PHE   A  1  441  ? -57.287 41.611  73.158  1.00 22.65 ? 439  PHE   A CE1   1 
ATOM   3239  C  CE2   . PHE   A  1  441  ? -57.575 41.215  70.818  1.00 25.15 ? 439  PHE   A CE2   1 
ATOM   3240  C  CZ    . PHE   A  1  441  ? -57.083 41.991  71.851  1.00 23.74 ? 439  PHE   A CZ    1 
ATOM   3241  N  N     . HIS   A  1  442  ? -61.292 40.794  71.848  1.00 24.94 ? 440  HIS   A N     1 
ATOM   3242  C  CA    . HIS   A  1  442  ? -61.635 41.570  70.673  1.00 26.38 ? 440  HIS   A CA    1 
ATOM   3243  C  C     . HIS   A  1  442  ? -60.678 42.744  70.646  1.00 30.88 ? 440  HIS   A C     1 
ATOM   3244  O  O     . HIS   A  1  442  ? -60.226 43.204  71.699  1.00 24.10 ? 440  HIS   A O     1 
ATOM   3245  C  CB    . HIS   A  1  442  ? -63.082 42.070  70.727  1.00 29.23 ? 440  HIS   A CB    1 
ATOM   3246  C  CG    . HIS   A  1  442  ? -63.376 42.955  71.898  1.00 27.02 ? 440  HIS   A CG    1 
ATOM   3247  N  ND1   . HIS   A  1  442  ? -63.774 42.464  73.124  1.00 27.37 ? 440  HIS   A ND1   1 
ATOM   3248  C  CD2   . HIS   A  1  442  ? -63.343 44.303  72.024  1.00 28.26 ? 440  HIS   A CD2   1 
ATOM   3249  C  CE1   . HIS   A  1  442  ? -63.965 43.472  73.956  1.00 26.19 ? 440  HIS   A CE1   1 
ATOM   3250  N  NE2   . HIS   A  1  442  ? -63.708 44.596  73.315  1.00 25.29 ? 440  HIS   A NE2   1 
ATOM   3251  N  N     . VAL   A  1  443  ? -60.349 43.210  69.438  1.00 30.98 ? 441  VAL   A N     1 
ATOM   3252  C  CA    . VAL   A  1  443  ? -59.489 44.378  69.335  1.00 31.59 ? 441  VAL   A CA    1 
ATOM   3253  C  C     . VAL   A  1  443  ? -60.188 45.542  70.011  1.00 27.06 ? 441  VAL   A C     1 
ATOM   3254  O  O     . VAL   A  1  443  ? -61.377 45.804  69.781  1.00 26.15 ? 441  VAL   A O     1 
ATOM   3255  C  CB    . VAL   A  1  443  ? -59.105 44.671  67.876  1.00 30.48 ? 441  VAL   A CB    1 
ATOM   3256  C  CG1   . VAL   A  1  443  ? -58.549 46.086  67.753  1.00 31.76 ? 441  VAL   A CG1   1 
ATOM   3257  C  CG2   . VAL   A  1  443  ? -58.062 43.669  67.399  1.00 34.45 ? 441  VAL   A CG2   1 
ATOM   3258  N  N     . GLY   A  1  444  ? -59.459 46.225  70.877  1.00 23.23 ? 442  GLY   A N     1 
ATOM   3259  C  CA    . GLY   A  1  444  ? -60.026 47.220  71.749  1.00 20.62 ? 442  GLY   A CA    1 
ATOM   3260  C  C     . GLY   A  1  444  ? -60.185 46.767  73.179  1.00 19.39 ? 442  GLY   A C     1 
ATOM   3261  O  O     . GLY   A  1  444  ? -60.417 47.608  74.050  1.00 21.02 ? 442  GLY   A O     1 
ATOM   3262  N  N     . LYS   A  1  445  ? -60.082 45.470  73.455  1.00 20.16 ? 443  LYS   A N     1 
ATOM   3263  C  CA    . LYS   A  1  445  ? -60.217 45.034  74.838  1.00 20.08 ? 443  LYS   A CA    1 
ATOM   3264  C  C     . LYS   A  1  445  ? -58.971 45.382  75.636  1.00 21.89 ? 443  LYS   A C     1 
ATOM   3265  O  O     . LYS   A  1  445  ? -59.054 46.019  76.692  1.00 19.74 ? 443  LYS   A O     1 
ATOM   3266  C  CB    . LYS   A  1  445  ? -60.498 43.544  74.913  1.00 23.76 ? 443  LYS   A CB    1 
ATOM   3267  C  CG    . LYS   A  1  445  ? -60.903 43.137  76.311  1.00 26.35 ? 443  LYS   A CG    1 
ATOM   3268  C  CD    . LYS   A  1  445  ? -61.211 41.665  76.430  1.00 32.65 ? 443  LYS   A CD    1 
ATOM   3269  C  CE    . LYS   A  1  445  ? -62.110 41.429  77.640  1.00 33.98 ? 443  LYS   A CE    1 
ATOM   3270  N  NZ    . LYS   A  1  445  ? -62.441 39.989  77.828  1.00 41.57 ? 443  LYS   A NZ    1 
ATOM   3271  N  N     . TYR   A  1  446  ? -57.810 44.966  75.138  1.00 20.03 ? 444  TYR   A N     1 
ATOM   3272  C  CA    . TYR   A  1  446  ? -56.511 45.360  75.664  1.00 19.51 ? 444  TYR   A CA    1 
ATOM   3273  C  C     . TYR   A  1  446  ? -55.508 45.124  74.548  1.00 18.86 ? 444  TYR   A C     1 
ATOM   3274  O  O     . TYR   A  1  446  ? -55.840 44.566  73.503  1.00 19.52 ? 444  TYR   A O     1 
ATOM   3275  C  CB    . TYR   A  1  446  ? -56.152 44.563  76.921  1.00 18.37 ? 444  TYR   A CB    1 
ATOM   3276  C  CG    . TYR   A  1  446  ? -55.744 43.124  76.679  1.00 21.20 ? 444  TYR   A CG    1 
ATOM   3277  C  CD1   . TYR   A  1  446  ? -56.682 42.090  76.674  1.00 29.96 ? 444  TYR   A CD1   1 
ATOM   3278  C  CD2   . TYR   A  1  446  ? -54.413 42.803  76.472  1.00 24.54 ? 444  TYR   A CD2   1 
ATOM   3279  C  CE1   . TYR   A  1  446  ? -56.279 40.770  76.458  1.00 24.64 ? 444  TYR   A CE1   1 
ATOM   3280  C  CE2   . TYR   A  1  446  ? -54.009 41.505  76.260  1.00 29.07 ? 444  TYR   A CE2   1 
ATOM   3281  C  CZ    . TYR   A  1  446  ? -54.937 40.499  76.251  1.00 28.70 ? 444  TYR   A CZ    1 
ATOM   3282  O  OH    . TYR   A  1  446  ? -54.474 39.215  76.037  1.00 34.00 ? 444  TYR   A OH    1 
ATOM   3283  N  N     . GLU   A  1  447  ? -54.268 45.539  74.780  1.00 16.71 ? 445  GLU   A N     1 
ATOM   3284  C  CA    . GLU   A  1  447  ? -53.205 45.206  73.845  1.00 17.87 ? 445  GLU   A CA    1 
ATOM   3285  C  C     . GLU   A  1  447  ? -51.922 45.041  74.633  1.00 19.57 ? 445  GLU   A C     1 
ATOM   3286  O  O     . GLU   A  1  447  ? -51.832 45.424  75.799  1.00 18.76 ? 445  GLU   A O     1 
ATOM   3287  C  CB    . GLU   A  1  447  ? -53.016 46.290  72.776  1.00 17.08 ? 445  GLU   A CB    1 
ATOM   3288  C  CG    . GLU   A  1  447  ? -52.556 47.609  73.357  1.00 18.30 ? 445  GLU   A CG    1 
ATOM   3289  C  CD    . GLU   A  1  447  ? -52.497 48.739  72.345  1.00 18.61 ? 445  GLU   A CD    1 
ATOM   3290  O  OE1   . GLU   A  1  447  ? -53.059 48.601  71.239  1.00 20.42 ? 445  GLU   A OE1   1 
ATOM   3291  O  OE2   . GLU   A  1  447  ? -51.888 49.786  72.667  1.00 17.99 ? 445  GLU   A OE2   1 
ATOM   3292  N  N     . PHE   A  1  448  ? -50.913 44.496  73.964  1.00 17.81 ? 446  PHE   A N     1 
ATOM   3293  C  CA    . PHE   A  1  448  ? -49.550 44.532  74.458  1.00 17.69 ? 446  PHE   A CA    1 
ATOM   3294  C  C     . PHE   A  1  448  ? -48.823 45.685  73.789  1.00 15.89 ? 446  PHE   A C     1 
ATOM   3295  O  O     . PHE   A  1  448  ? -49.293 46.253  72.803  1.00 16.97 ? 446  PHE   A O     1 
ATOM   3296  C  CB    . PHE   A  1  448  ? -48.850 43.209  74.149  1.00 19.81 ? 446  PHE   A CB    1 
ATOM   3297  C  CG    . PHE   A  1  448  ? -49.417 42.048  74.893  1.00 20.44 ? 446  PHE   A CG    1 
ATOM   3298  C  CD1   . PHE   A  1  448  ? -49.088 41.850  76.223  1.00 19.90 ? 446  PHE   A CD1   1 
ATOM   3299  C  CD2   . PHE   A  1  448  ? -50.288 41.162  74.270  1.00 21.17 ? 446  PHE   A CD2   1 
ATOM   3300  C  CE1   . PHE   A  1  448  ? -49.624 40.787  76.932  1.00 24.56 ? 446  PHE   A CE1   1 
ATOM   3301  C  CE2   . PHE   A  1  448  ? -50.821 40.093  74.970  1.00 24.38 ? 446  PHE   A CE2   1 
ATOM   3302  C  CZ    . PHE   A  1  448  ? -50.488 39.908  76.304  1.00 22.31 ? 446  PHE   A CZ    1 
ATOM   3303  N  N     . GLN   A  1  449  ? -47.669 46.037  74.341  1.00 16.13 ? 447  GLN   A N     1 
ATOM   3304  C  CA    . GLN   A  1  449  ? -46.811 47.028  73.706  1.00 16.59 ? 447  GLN   A CA    1 
ATOM   3305  C  C     . GLN   A  1  449  ? -45.364 46.610  73.830  1.00 18.65 ? 447  GLN   A C     1 
ATOM   3306  O  O     . GLN   A  1  449  ? -44.986 45.862  74.733  1.00 17.73 ? 447  GLN   A O     1 
ATOM   3307  C  CB    . GLN   A  1  449  ? -46.972 48.425  74.276  1.00 16.16 ? 447  GLN   A CB    1 
ATOM   3308  C  CG    . GLN   A  1  449  ? -48.386 48.922  74.194  1.00 15.47 ? 447  GLN   A CG    1 
ATOM   3309  C  CD    . GLN   A  1  449  ? -48.471 50.410  74.381  1.00 17.68 ? 447  GLN   A CD    1 
ATOM   3310  O  OE1   . GLN   A  1  449  ? -47.506 51.054  74.842  1.00 18.52 ? 447  GLN   A OE1   1 
ATOM   3311  N  NE2   . GLN   A  1  449  ? -49.607 50.981  74.024  1.00 16.85 ? 447  GLN   A NE2   1 
ATOM   3312  N  N     . CYS   A  1  450  ? -44.563 47.095  72.895  1.00 16.54 ? 448  CYS   A N     1 
ATOM   3313  C  CA    . CYS   A  1  450  ? -43.141 46.806  72.921  1.00 16.40 ? 448  CYS   A CA    1 
ATOM   3314  C  C     . CYS   A  1  450  ? -42.394 47.976  72.309  1.00 18.00 ? 448  CYS   A C     1 
ATOM   3315  O  O     . CYS   A  1  450  ? -42.987 48.889  71.731  1.00 17.73 ? 448  CYS   A O     1 
ATOM   3316  C  CB    . CYS   A  1  450  ? -42.825 45.497  72.202  1.00 18.12 ? 448  CYS   A CB    1 
ATOM   3317  S  SG    . CYS   A  1  450  ? -42.923 45.597  70.412  1.00 20.67 ? 448  CYS   A SG    1 
ATOM   3318  N  N     . LEU   A  1  451  ? -41.075 47.940  72.448  1.00 17.07 ? 449  LEU   A N     1 
ATOM   3319  C  CA    . LEU   A  1  451  ? -40.230 48.975  71.883  1.00 19.15 ? 449  LEU   A CA    1 
ATOM   3320  C  C     . LEU   A  1  451  ? -39.744 48.564  70.501  1.00 19.20 ? 449  LEU   A C     1 
ATOM   3321  O  O     . LEU   A  1  451  ? -39.385 47.404  70.275  1.00 19.49 ? 449  LEU   A O     1 
ATOM   3322  C  CB    . LEU   A  1  451  ? -39.027 49.199  72.796  1.00 19.38 ? 449  LEU   A CB    1 
ATOM   3323  C  CG    . LEU   A  1  451  ? -37.987 50.225  72.351  1.00 22.50 ? 449  LEU   A CG    1 
ATOM   3324  C  CD1   . LEU   A  1  451  ? -38.542 51.641  72.283  1.00 21.40 ? 449  LEU   A CD1   1 
ATOM   3325  C  CD2   . LEU   A  1  451  ? -36.797 50.155  73.312  1.00 24.25 ? 449  LEU   A CD2   1 
ATOM   3326  N  N     . HIS   A  1  452  ? -39.754 49.522  69.575  1.00 18.31 ? 450  HIS   A N     1 
ATOM   3327  C  CA    . HIS   A  1  452  ? -39.190 49.301  68.252  1.00 17.50 ? 450  HIS   A CA    1 
ATOM   3328  C  C     . HIS   A  1  452  ? -37.754 48.814  68.353  1.00 19.45 ? 450  HIS   A C     1 
ATOM   3329  O  O     . HIS   A  1  452  ? -36.980 49.295  69.178  1.00 21.79 ? 450  HIS   A O     1 
ATOM   3330  C  CB    . HIS   A  1  452  ? -39.200 50.621  67.483  1.00 18.04 ? 450  HIS   A CB    1 
ATOM   3331  C  CG    . HIS   A  1  452  ? -38.400 50.572  66.226  1.00 16.47 ? 450  HIS   A CG    1 
ATOM   3332  N  ND1   . HIS   A  1  452  ? -38.917 50.114  65.033  1.00 20.24 ? 450  HIS   A ND1   1 
ATOM   3333  C  CD2   . HIS   A  1  452  ? -37.102 50.875  65.988  1.00 20.50 ? 450  HIS   A CD2   1 
ATOM   3334  C  CE1   . HIS   A  1  452  ? -37.975 50.159  64.106  1.00 21.62 ? 450  HIS   A CE1   1 
ATOM   3335  N  NE2   . HIS   A  1  452  ? -36.866 50.612  64.663  1.00 20.79 ? 450  HIS   A NE2   1 
ATOM   3336  N  N     . GLY   A  1  453  ? -37.404 47.864  67.491  1.00 21.48 ? 451  GLY   A N     1 
ATOM   3337  C  CA    . GLY   A  1  453  ? -36.021 47.418  67.445  1.00 23.98 ? 451  GLY   A CA    1 
ATOM   3338  C  C     . GLY   A  1  453  ? -35.579 46.655  68.668  1.00 32.27 ? 451  GLY   A C     1 
ATOM   3339  O  O     . GLY   A  1  453  ? -34.376 46.548  68.927  1.00 34.23 ? 451  GLY   A O     1 
ATOM   3340  N  N     . MET   A  1  454  ? -36.526 46.122  69.431  1.00 24.84 ? 452  MET   A N     1 
ATOM   3341  C  CA    . MET   A  1  454  ? -36.221 45.361  70.630  1.00 22.17 ? 452  MET   A CA    1 
ATOM   3342  C  C     . MET   A  1  454  ? -37.275 44.287  70.836  1.00 25.05 ? 452  MET   A C     1 
ATOM   3343  O  O     . MET   A  1  454  ? -36.950 43.111  71.021  1.00 26.66 ? 452  MET   A O     1 
ATOM   3344  C  CB    . MET   A  1  454  ? -36.163 46.282  71.847  1.00 24.65 ? 452  MET   A CB    1 
ATOM   3345  C  CG    . MET   A  1  454  ? -35.980 45.542  73.156  1.00 25.63 ? 452  MET   A CG    1 
ATOM   3346  S  SD    . MET   A  1  454  ? -34.460 44.572  73.143  1.00 31.21 ? 452  MET   A SD    1 
ATOM   3347  C  CE    . MET   A  1  454  ? -33.237 45.880  73.093  1.00 32.93 ? 452  MET   A CE    1 
ATOM   3348  N  N     . GLY   A  1  455  ? -38.542 44.680  70.790  1.00 23.28 ? 453  GLY   A N     1 
ATOM   3349  C  CA    . GLY   A  1  455  ? -39.608 43.754  71.124  1.00 22.15 ? 453  GLY   A CA    1 
ATOM   3350  C  C     . GLY   A  1  455  ? -40.186 42.950  69.984  1.00 22.95 ? 453  GLY   A C     1 
ATOM   3351  O  O     . GLY   A  1  455  ? -40.954 42.015  70.232  1.00 24.57 ? 453  GLY   A O     1 
ATOM   3352  N  N     . GLU   A  1  456  ? -39.850 43.277  68.735  1.00 24.32 ? 454  GLU   A N     1 
ATOM   3353  C  CA    . GLU   A  1  456  ? -40.467 42.575  67.612  1.00 25.25 ? 454  GLU   A CA    1 
ATOM   3354  C  C     . GLU   A  1  456  ? -40.210 41.075  67.590  1.00 28.12 ? 454  GLU   A C     1 
ATOM   3355  O  O     . GLU   A  1  456  ? -41.149 40.332  67.253  1.00 27.59 ? 454  GLU   A O     1 
ATOM   3356  C  CB    . GLU   A  1  456  ? -40.087 43.210  66.269  1.00 27.82 ? 454  GLU   A CB    1 
ATOM   3357  C  CG    . GLU   A  1  456  ? -40.546 44.634  66.110  1.00 31.11 ? 454  GLU   A CG    1 
ATOM   3358  C  CD    . GLU   A  1  456  ? -39.453 45.599  66.458  1.00 30.28 ? 454  GLU   A CD    1 
ATOM   3359  O  OE1   . GLU   A  1  456  ? -38.578 45.227  67.275  1.00 29.44 ? 454  GLU   A OE1   1 
ATOM   3360  O  OE2   . GLU   A  1  456  ? -39.456 46.716  65.899  1.00 31.40 ? 454  GLU   A OE2   1 
ATOM   3361  N  N     . PRO   A  1  457  ? -39.004 40.567  67.881  1.00 26.99 ? 455  PRO   A N     1 
ATOM   3362  C  CA    . PRO   A  1  457  ? -38.839 39.104  67.884  1.00 27.90 ? 455  PRO   A CA    1 
ATOM   3363  C  C     . PRO   A  1  457  ? -39.814 38.398  68.807  1.00 27.30 ? 455  PRO   A C     1 
ATOM   3364  O  O     . PRO   A  1  457  ? -40.369 37.360  68.431  1.00 28.63 ? 455  PRO   A O     1 
ATOM   3365  C  CB    . PRO   A  1  457  ? -37.375 38.911  68.308  1.00 28.35 ? 455  PRO   A CB    1 
ATOM   3366  C  CG    . PRO   A  1  457  ? -36.702 40.157  67.845  1.00 29.12 ? 455  PRO   A CG    1 
ATOM   3367  C  CD    . PRO   A  1  457  ? -37.714 41.253  68.092  1.00 26.71 ? 455  PRO   A CD    1 
ATOM   3368  N  N     . LEU   A  1  458  ? -40.054 38.949  69.999  1.00 25.66 ? 456  LEU   A N     1 
ATOM   3369  C  CA    . LEU   A  1  458  ? -41.032 38.348  70.903  1.00 24.45 ? 456  LEU   A CA    1 
ATOM   3370  C  C     . LEU   A  1  458  ? -42.442 38.479  70.349  1.00 24.43 ? 456  LEU   A C     1 
ATOM   3371  O  O     . LEU   A  1  458  ? -43.185 37.495  70.269  1.00 24.59 ? 456  LEU   A O     1 
ATOM   3372  C  CB    . LEU   A  1  458  ? -40.939 39.004  72.280  1.00 24.97 ? 456  LEU   A CB    1 
ATOM   3373  C  CG    . LEU   A  1  458  ? -42.016 38.569  73.278  1.00 26.19 ? 456  LEU   A CG    1 
ATOM   3374  C  CD1   . LEU   A  1  458  ? -42.000 37.046  73.464  1.00 23.29 ? 456  LEU   A CD1   1 
ATOM   3375  C  CD2   . LEU   A  1  458  ? -41.791 39.285  74.593  1.00 25.29 ? 456  LEU   A CD2   1 
ATOM   3376  N  N     . TYR   A  1  459  ? -42.823 39.684  69.938  1.00 23.19 ? 457  TYR   A N     1 
ATOM   3377  C  CA    . TYR   A  1  459  ? -44.210 39.901  69.566  1.00 24.23 ? 457  TYR   A CA    1 
ATOM   3378  C  C     . TYR   A  1  459  ? -44.567 39.344  68.198  1.00 24.95 ? 457  TYR   A C     1 
ATOM   3379  O  O     . TYR   A  1  459  ? -45.757 39.158  67.911  1.00 25.01 ? 457  TYR   A O     1 
ATOM   3380  C  CB    . TYR   A  1  459  ? -44.587 41.365  69.776  1.00 21.80 ? 457  TYR   A CB    1 
ATOM   3381  C  CG    . TYR   A  1  459  ? -44.806 41.625  71.243  1.00 20.42 ? 457  TYR   A CG    1 
ATOM   3382  C  CD1   . TYR   A  1  459  ? -46.006 41.267  71.846  1.00 22.00 ? 457  TYR   A CD1   1 
ATOM   3383  C  CD2   . TYR   A  1  459  ? -43.804 42.168  72.032  1.00 21.42 ? 457  TYR   A CD2   1 
ATOM   3384  C  CE1   . TYR   A  1  459  ? -46.213 41.470  73.177  1.00 22.54 ? 457  TYR   A CE1   1 
ATOM   3385  C  CE2   . TYR   A  1  459  ? -44.009 42.383  73.388  1.00 19.73 ? 457  TYR   A CE2   1 
ATOM   3386  C  CZ    . TYR   A  1  459  ? -45.211 42.027  73.947  1.00 22.58 ? 457  TYR   A CZ    1 
ATOM   3387  O  OH    . TYR   A  1  459  ? -45.405 42.242  75.290  1.00 21.99 ? 457  TYR   A OH    1 
ATOM   3388  N  N     . GLU   A  1  460  ? -43.574 39.029  67.365  1.00 25.02 ? 458  GLU   A N     1 
ATOM   3389  C  CA    . GLU   A  1  460  ? -43.875 38.233  66.185  1.00 27.47 ? 458  GLU   A CA    1 
ATOM   3390  C  C     . GLU   A  1  460  ? -44.307 36.815  66.531  1.00 30.77 ? 458  GLU   A C     1 
ATOM   3391  O  O     . GLU   A  1  460  ? -44.837 36.118  65.661  1.00 30.13 ? 458  GLU   A O     1 
ATOM   3392  C  CB    . GLU   A  1  460  ? -42.714 38.263  65.193  1.00 33.64 ? 458  GLU   A CB    1 
ATOM   3393  C  CG    . GLU   A  1  460  ? -42.858 39.405  64.198  1.00 40.99 ? 458  GLU   A CG    1 
ATOM   3394  C  CD    . GLU   A  1  460  ? -41.603 39.661  63.397  1.00 51.44 ? 458  GLU   A CD    1 
ATOM   3395  O  OE1   . GLU   A  1  460  ? -40.579 38.994  63.661  1.00 53.45 ? 458  GLU   A OE1   1 
ATOM   3396  O  OE2   . GLU   A  1  460  ? -41.645 40.536  62.505  1.00 52.79 ? 458  GLU   A OE2   1 
ATOM   3397  N  N     . GLU   A  1  461  ? -44.119 36.388  67.779  1.00 27.56 ? 459  GLU   A N     1 
ATOM   3398  C  CA    . GLU   A  1  461  ? -44.667 35.135  68.282  1.00 30.78 ? 459  GLU   A CA    1 
ATOM   3399  C  C     . GLU   A  1  461  ? -46.013 35.329  68.967  1.00 29.62 ? 459  GLU   A C     1 
ATOM   3400  O  O     . GLU   A  1  461  ? -46.573 34.366  69.501  1.00 28.87 ? 459  GLU   A O     1 
ATOM   3401  C  CB    . GLU   A  1  461  ? -43.681 34.494  69.264  1.00 27.39 ? 459  GLU   A CB    1 
ATOM   3402  C  CG    . GLU   A  1  461  ? -42.280 34.348  68.707  1.00 29.75 ? 459  GLU   A CG    1 
ATOM   3403  C  CD    . GLU   A  1  461  ? -42.230 33.433  67.492  1.00 35.28 ? 459  GLU   A CD    1 
ATOM   3404  O  OE1   . GLU   A  1  461  ? -43.116 32.558  67.361  1.00 35.53 ? 459  GLU   A OE1   1 
ATOM   3405  O  OE2   . GLU   A  1  461  ? -41.296 33.585  66.671  1.00 35.78 ? 459  GLU   A OE2   1 
ATOM   3406  N  N     . VAL   A  1  462  ? -46.537 36.553  68.960  1.00 27.94 ? 460  VAL   A N     1 
ATOM   3407  C  CA    . VAL   A  1  462  ? -47.760 36.911  69.666  1.00 24.11 ? 460  VAL   A CA    1 
ATOM   3408  C  C     . VAL   A  1  462  ? -48.833 37.402  68.702  1.00 26.53 ? 460  VAL   A C     1 
ATOM   3409  O  O     . VAL   A  1  462  ? -49.962 36.896  68.690  1.00 27.28 ? 460  VAL   A O     1 
ATOM   3410  C  CB    . VAL   A  1  462  ? -47.481 37.961  70.765  1.00 26.57 ? 460  VAL   A CB    1 
ATOM   3411  C  CG1   . VAL   A  1  462  ? -48.764 38.390  71.433  1.00 24.36 ? 460  VAL   A CG1   1 
ATOM   3412  C  CG2   . VAL   A  1  462  ? -46.518 37.409  71.794  1.00 25.82 ? 460  VAL   A CG2   1 
ATOM   3413  N  N     . VAL   A  1  463  ? -48.485 38.373  67.860  1.00 26.09 ? 461  VAL   A N     1 
ATOM   3414  C  CA    . VAL   A  1  463  ? -49.446 38.982  66.955  1.00 26.53 ? 461  VAL   A CA    1 
ATOM   3415  C  C     . VAL   A  1  463  ? -49.809 38.006  65.846  1.00 32.19 ? 461  VAL   A C     1 
ATOM   3416  O  O     . VAL   A  1  463  ? -48.955 37.274  65.329  1.00 33.53 ? 461  VAL   A O     1 
ATOM   3417  C  CB    . VAL   A  1  463  ? -48.835 40.263  66.371  1.00 25.66 ? 461  VAL   A CB    1 
ATOM   3418  C  CG1   . VAL   A  1  463  ? -49.767 40.877  65.333  1.00 28.17 ? 461  VAL   A CG1   1 
ATOM   3419  C  CG2   . VAL   A  1  463  ? -48.522 41.253  67.489  1.00 24.98 ? 461  VAL   A CG2   1 
ATOM   3420  N  N     . GLY   A  1  464  ? -51.073 37.996  65.470  1.00 30.17 ? 462  GLY   A N     1 
ATOM   3421  C  CA    . GLY   A  1  464  ? -51.462 37.221  64.313  1.00 36.77 ? 462  GLY   A CA    1 
ATOM   3422  C  C     . GLY   A  1  464  ? -52.229 35.971  64.698  1.00 35.59 ? 462  GLY   A C     1 
ATOM   3423  O  O     . GLY   A  1  464  ? -51.987 35.352  65.743  1.00 34.12 ? 462  GLY   A O     1 
ATOM   3424  N  N     . ARG   A  1  465  ? -53.160 35.579  63.823  1.00 33.15 ? 463  ARG   A N     1 
ATOM   3425  C  CA    . ARG   A  1  465  ? -54.015 34.428  64.097  1.00 38.20 ? 463  ARG   A CA    1 
ATOM   3426  C  C     . ARG   A  1  465  ? -53.207 33.144  64.244  1.00 38.07 ? 463  ARG   A C     1 
ATOM   3427  O  O     . ARG   A  1  465  ? -53.616 32.234  64.974  1.00 42.99 ? 463  ARG   A O     1 
ATOM   3428  C  CB    . ARG   A  1  465  ? -55.062 34.280  62.992  1.00 37.33 ? 463  ARG   A CB    1 
ATOM   3429  N  N     . GLY   A  1  466  ? -52.064 33.052  63.573  1.00 33.23 ? 464  GLY   A N     1 
ATOM   3430  C  CA    . GLY   A  1  466  ? -51.215 31.887  63.710  1.00 36.06 ? 464  GLY   A CA    1 
ATOM   3431  C  C     . GLY   A  1  466  ? -50.365 31.851  64.954  1.00 39.24 ? 464  GLY   A C     1 
ATOM   3432  O  O     . GLY   A  1  466  ? -49.610 30.893  65.161  1.00 39.74 ? 464  GLY   A O     1 
ATOM   3433  N  N     . LYS   A  1  467  ? -50.466 32.879  65.807  1.00 33.10 ? 465  LYS   A N     1 
ATOM   3434  C  CA    . LYS   A  1  467  ? -49.704 32.937  67.049  1.00 29.70 ? 465  LYS   A CA    1 
ATOM   3435  C  C     . LYS   A  1  467  ? -50.713 32.980  68.197  1.00 31.67 ? 465  LYS   A C     1 
ATOM   3436  O  O     . LYS   A  1  467  ? -51.563 32.098  68.284  1.00 36.26 ? 465  LYS   A O     1 
ATOM   3437  C  CB    . LYS   A  1  467  ? -48.685 34.060  67.024  1.00 30.93 ? 465  LYS   A CB    1 
ATOM   3438  C  CG    . LYS   A  1  467  ? -47.644 33.948  65.923  1.00 32.10 ? 465  LYS   A CG    1 
ATOM   3439  C  CD    . LYS   A  1  467  ? -46.763 32.734  66.145  1.00 34.99 ? 465  LYS   A CD    1 
ATOM   3440  C  CE    . LYS   A  1  467  ? -45.609 32.754  65.178  1.00 37.07 ? 465  LYS   A CE    1 
ATOM   3441  N  NZ    . LYS   A  1  467  ? -44.696 31.615  65.409  1.00 34.31 ? 465  LYS   A NZ    1 
ATOM   3442  N  N     . LEU   A  1  468  ? -50.645 33.992  69.069  1.00 29.71 ? 466  LEU   A N     1 
ATOM   3443  C  CA    . LEU   A  1  468  ? -51.592 34.171  70.156  1.00 31.17 ? 466  LEU   A CA    1 
ATOM   3444  C  C     . LEU   A  1  468  ? -52.750 35.077  69.772  1.00 29.43 ? 466  LEU   A C     1 
ATOM   3445  O  O     . LEU   A  1  468  ? -53.690 35.221  70.559  1.00 29.45 ? 466  LEU   A O     1 
ATOM   3446  C  CB    . LEU   A  1  468  ? -50.877 34.746  71.381  1.00 30.58 ? 466  LEU   A CB    1 
ATOM   3447  C  CG    . LEU   A  1  468  ? -49.652 33.968  71.872  1.00 29.22 ? 466  LEU   A CG    1 
ATOM   3448  C  CD1   . LEU   A  1  468  ? -49.189 34.488  73.211  1.00 30.38 ? 466  LEU   A CD1   1 
ATOM   3449  C  CD2   . LEU   A  1  468  ? -49.966 32.481  71.950  1.00 35.63 ? 466  LEU   A CD2   1 
ATOM   3450  N  N     . ASP   A  1  469  ? -52.695 35.682  68.585  1.00 30.54 ? 467  ASP   A N     1 
ATOM   3451  C  CA    . ASP   A  1  469  ? -53.761 36.536  68.075  1.00 28.84 ? 467  ASP   A CA    1 
ATOM   3452  C  C     . ASP   A  1  469  ? -54.072 37.667  69.046  1.00 27.29 ? 467  ASP   A C     1 
ATOM   3453  O  O     . ASP   A  1  469  ? -55.234 37.958  69.343  1.00 25.33 ? 467  ASP   A O     1 
ATOM   3454  C  CB    . ASP   A  1  469  ? -55.016 35.735  67.723  1.00 31.19 ? 467  ASP   A CB    1 
ATOM   3455  C  CG    . ASP   A  1  469  ? -55.904 36.454  66.735  1.00 32.17 ? 467  ASP   A CG    1 
ATOM   3456  O  OD1   . ASP   A  1  469  ? -55.411 37.359  66.029  1.00 34.21 ? 467  ASP   A OD1   1 
ATOM   3457  O  OD2   . ASP   A  1  469  ? -57.102 36.119  66.664  1.00 37.53 ? 467  ASP   A OD2   1 
ATOM   3458  N  N     . ARG   A  1  470  ? -53.016 38.293  69.565  1.00 27.74 ? 468  ARG   A N     1 
ATOM   3459  C  CA    . ARG   A  1  470  ? -53.160 39.479  70.381  1.00 24.72 ? 468  ARG   A CA    1 
ATOM   3460  C  C     . ARG   A  1  470  ? -52.352 40.617  69.772  1.00 23.69 ? 468  ARG   A C     1 
ATOM   3461  O  O     . ARG   A  1  470  ? -51.236 40.394  69.283  1.00 23.82 ? 468  ARG   A O     1 
ATOM   3462  C  CB    . ARG   A  1  470  ? -52.682 39.231  71.819  1.00 24.08 ? 468  ARG   A CB    1 
ATOM   3463  C  CG    . ARG   A  1  470  ? -53.471 38.161  72.566  1.00 21.95 ? 468  ARG   A CG    1 
ATOM   3464  C  CD    . ARG   A  1  470  ? -54.920 38.578  72.782  1.00 22.52 ? 468  ARG   A CD    1 
ATOM   3465  N  NE    . ARG   A  1  470  ? -55.678 37.522  73.446  1.00 26.26 ? 468  ARG   A NE    1 
ATOM   3466  C  CZ    . ARG   A  1  470  ? -56.403 36.607  72.817  1.00 26.70 ? 468  ARG   A CZ    1 
ATOM   3467  N  NH1   . ARG   A  1  470  ? -56.526 36.607  71.499  1.00 27.35 ? 468  ARG   A NH1   1 
ATOM   3468  N  NH2   . ARG   A  1  470  ? -57.037 35.678  73.530  1.00 29.58 ? 468  ARG   A NH2   1 
ATOM   3469  N  N     . PRO   A  1  471  ? -52.889 41.832  69.776  1.00 21.58 ? 469  PRO   A N     1 
ATOM   3470  C  CA    . PRO   A  1  471  ? -52.206 42.956  69.131  1.00 20.97 ? 469  PRO   A CA    1 
ATOM   3471  C  C     . PRO   A  1  471  ? -51.082 43.502  69.992  1.00 21.12 ? 469  PRO   A C     1 
ATOM   3472  O  O     . PRO   A  1  471  ? -51.060 43.369  71.217  1.00 19.49 ? 469  PRO   A O     1 
ATOM   3473  C  CB    . PRO   A  1  471  ? -53.317 44.003  68.999  1.00 23.04 ? 469  PRO   A CB    1 
ATOM   3474  C  CG    . PRO   A  1  471  ? -54.192 43.723  70.168  1.00 24.33 ? 469  PRO   A CG    1 
ATOM   3475  C  CD    . PRO   A  1  471  ? -54.207 42.222  70.295  1.00 21.99 ? 469  PRO   A CD    1 
ATOM   3476  N  N     . CYS   A  1  472  ? -50.135 44.143  69.317  1.00 19.26 ? 470  CYS   A N     1 
ATOM   3477  C  CA    . CYS   A  1  472  ? -49.031 44.784  70.005  1.00 21.04 ? 470  CYS   A CA    1 
ATOM   3478  C  C     . CYS   A  1  472  ? -48.801 46.131  69.356  1.00 19.06 ? 470  CYS   A C     1 
ATOM   3479  O  O     . CYS   A  1  472  ? -48.715 46.219  68.127  1.00 20.21 ? 470  CYS   A O     1 
ATOM   3480  C  CB    . CYS   A  1  472  ? -47.757 43.953  69.875  1.00 20.38 ? 470  CYS   A CB    1 
ATOM   3481  S  SG    . CYS   A  1  472  ? -46.369 44.658  70.766  1.00 21.47 ? 470  CYS   A SG    1 
ATOM   3482  N  N     . ARG   A  1  473  ? -48.685 47.165  70.173  1.00 17.07 ? 471  ARG   A N     1 
ATOM   3483  C  CA    . ARG   A  1  473  ? -48.357 48.495  69.697  1.00 17.29 ? 471  ARG   A CA    1 
ATOM   3484  C  C     . ARG   A  1  473  ? -46.870 48.735  69.905  1.00 18.13 ? 471  ARG   A C     1 
ATOM   3485  O  O     . ARG   A  1  473  ? -46.354 48.579  71.015  1.00 18.77 ? 471  ARG   A O     1 
ATOM   3486  C  CB    . ARG   A  1  473  ? -49.151 49.554  70.454  1.00 18.21 ? 471  ARG   A CB    1 
ATOM   3487  C  CG    . ARG   A  1  473  ? -48.975 50.953  69.863  1.00 17.56 ? 471  ARG   A CG    1 
ATOM   3488  C  CD    . ARG   A  1  473  ? -49.869 51.951  70.565  1.00 17.68 ? 471  ARG   A CD    1 
ATOM   3489  N  NE    . ARG   A  1  473  ? -51.247 51.481  70.544  1.00 17.66 ? 471  ARG   A NE    1 
ATOM   3490  C  CZ    . ARG   A  1  473  ? -52.084 51.638  69.530  1.00 18.70 ? 471  ARG   A CZ    1 
ATOM   3491  N  NH1   . ARG   A  1  473  ? -51.770 52.373  68.474  1.00 18.59 ? 471  ARG   A NH1   1 
ATOM   3492  N  NH2   . ARG   A  1  473  ? -53.268 51.036  69.577  1.00 19.57 ? 471  ARG   A NH2   1 
ATOM   3493  N  N     . ILE   A  1  474  ? -46.195 49.137  68.841  1.00 16.40 ? 472  ILE   A N     1 
ATOM   3494  C  CA    . ILE   A  1  474  ? -44.757 49.350  68.876  1.00 16.83 ? 472  ILE   A CA    1 
ATOM   3495  C  C     . ILE   A  1  474  ? -44.491 50.803  69.231  1.00 17.50 ? 472  ILE   A C     1 
ATOM   3496  O  O     . ILE   A  1  474  ? -44.942 51.713  68.530  1.00 17.85 ? 472  ILE   A O     1 
ATOM   3497  C  CB    . ILE   A  1  474  ? -44.134 49.000  67.522  1.00 17.53 ? 472  ILE   A CB    1 
ATOM   3498  C  CG1   . ILE   A  1  474  ? -44.346 47.521  67.224  1.00 20.03 ? 472  ILE   A CG1   1 
ATOM   3499  C  CG2   . ILE   A  1  474  ? -42.655 49.353  67.530  1.00 18.67 ? 472  ILE   A CG2   1 
ATOM   3500  C  CD1   . ILE   A  1  474  ? -44.007 47.151  65.795  1.00 20.93 ? 472  ILE   A CD1   1 
ATOM   3501  N  N     . TYR   A  1  475  ? -43.737 51.023  70.309  1.00 17.00 ? 473  TYR   A N     1 
ATOM   3502  C  CA    . TYR   A  1  475  ? -43.312 52.364  70.688  1.00 17.37 ? 473  TYR   A CA    1 
ATOM   3503  C  C     . TYR   A  1  475  ? -42.119 52.721  69.817  1.00 16.83 ? 473  TYR   A C     1 
ATOM   3504  O  O     . TYR   A  1  475  ? -41.080 52.046  69.862  1.00 17.65 ? 473  TYR   A O     1 
ATOM   3505  C  CB    . TYR   A  1  475  ? -42.937 52.384  72.168  1.00 18.55 ? 473  TYR   A CB    1 
ATOM   3506  C  CG    . TYR   A  1  475  ? -42.642 53.747  72.767  1.00 19.03 ? 473  TYR   A CG    1 
ATOM   3507  C  CD1   . TYR   A  1  475  ? -41.359 54.285  72.717  1.00 23.04 ? 473  TYR   A CD1   1 
ATOM   3508  C  CD2   . TYR   A  1  475  ? -43.637 54.494  73.394  1.00 18.11 ? 473  TYR   A CD2   1 
ATOM   3509  C  CE1   . TYR   A  1  475  ? -41.076 55.519  73.264  1.00 24.15 ? 473  TYR   A CE1   1 
ATOM   3510  C  CE2   . TYR   A  1  475  ? -43.359 55.733  73.955  1.00 19.06 ? 473  TYR   A CE2   1 
ATOM   3511  C  CZ    . TYR   A  1  475  ? -42.079 56.239  73.883  1.00 24.58 ? 473  TYR   A CZ    1 
ATOM   3512  O  OH    . TYR   A  1  475  ? -41.800 57.473  74.426  1.00 24.06 ? 473  TYR   A OH    1 
ATOM   3513  N  N     . ALA   A  1  476  ? -42.285 53.744  68.989  1.00 17.23 ? 474  ALA   A N     1 
ATOM   3514  C  CA    . ALA   A  1  476  ? -41.393 53.983  67.858  1.00 16.32 ? 474  ALA   A CA    1 
ATOM   3515  C  C     . ALA   A  1  476  ? -40.695 55.311  68.045  1.00 16.70 ? 474  ALA   A C     1 
ATOM   3516  O  O     . ALA   A  1  476  ? -41.281 56.371  67.766  1.00 17.27 ? 474  ALA   A O     1 
ATOM   3517  C  CB    . ALA   A  1  476  ? -42.206 53.987  66.566  1.00 19.65 ? 474  ALA   A CB    1 
ATOM   3518  N  N     . PRO   A  1  477  ? -39.445 55.318  68.500  1.00 17.69 ? 475  PRO   A N     1 
ATOM   3519  C  CA    . PRO   A  1  477  ? -38.715 56.581  68.583  1.00 18.76 ? 475  PRO   A CA    1 
ATOM   3520  C  C     . PRO   A  1  477  ? -38.473 57.135  67.192  1.00 16.62 ? 475  PRO   A C     1 
ATOM   3521  O  O     . PRO   A  1  477  ? -38.258 56.394  66.232  1.00 17.83 ? 475  PRO   A O     1 
ATOM   3522  C  CB    . PRO   A  1  477  ? -37.391 56.182  69.250  1.00 17.56 ? 475  PRO   A CB    1 
ATOM   3523  C  CG    . PRO   A  1  477  ? -37.647 54.815  69.848  1.00 22.69 ? 475  PRO   A CG    1 
ATOM   3524  C  CD    . PRO   A  1  477  ? -38.620 54.172  68.908  1.00 19.05 ? 475  PRO   A CD    1 
ATOM   3525  N  N     . VAL   A  1  478  ? -38.528 58.450  67.090  1.00 16.15 ? 476  VAL   A N     1 
ATOM   3526  C  CA    . VAL   A  1  478  ? -38.354 59.138  65.823  1.00 18.35 ? 476  VAL   A CA    1 
ATOM   3527  C  C     . VAL   A  1  478  ? -37.416 60.300  66.085  1.00 20.64 ? 476  VAL   A C     1 
ATOM   3528  O  O     . VAL   A  1  478  ? -37.675 61.116  66.972  1.00 22.84 ? 476  VAL   A O     1 
ATOM   3529  C  CB    . VAL   A  1  478  ? -39.710 59.662  65.321  1.00 18.17 ? 476  VAL   A CB    1 
ATOM   3530  C  CG1   . VAL   A  1  478  ? -39.540 60.465  64.031  1.00 19.39 ? 476  VAL   A CG1   1 
ATOM   3531  C  CG2   . VAL   A  1  478  ? -40.695 58.508  65.130  1.00 19.44 ? 476  VAL   A CG2   1 
ATOM   3532  N  N     . GLY   A  1  479  ? -36.325 60.374  65.339  1.00 19.98 ? 477  GLY   A N     1 
ATOM   3533  C  CA    . GLY   A  1  479  ? -35.455 61.519  65.504  1.00 22.12 ? 477  GLY   A CA    1 
ATOM   3534  C  C     . GLY   A  1  479  ? -34.106 61.301  64.872  1.00 21.27 ? 477  GLY   A C     1 
ATOM   3535  O  O     . GLY   A  1  479  ? -33.774 60.218  64.391  1.00 21.51 ? 477  GLY   A O     1 
ATOM   3536  N  N     . THR   A  1  480  ? -33.321 62.371  64.901  1.00 26.11 ? 478  THR   A N     1 
ATOM   3537  C  CA    . THR   A  1  480  ? -31.996 62.386  64.303  1.00 25.42 ? 478  THR   A CA    1 
ATOM   3538  C  C     . THR   A  1  480  ? -31.003 61.683  65.220  1.00 31.44 ? 478  THR   A C     1 
ATOM   3539  O  O     . THR   A  1  480  ? -31.329 61.271  66.337  1.00 28.57 ? 478  THR   A O     1 
ATOM   3540  C  CB    . THR   A  1  480  ? -31.550 63.827  64.086  1.00 29.25 ? 478  THR   A CB    1 
ATOM   3541  O  OG1   . THR   A  1  480  ? -31.502 64.486  65.359  1.00 34.70 ? 478  THR   A OG1   1 
ATOM   3542  C  CG2   . THR   A  1  480  ? -32.525 64.549  63.185  1.00 30.59 ? 478  THR   A CG2   1 
ATOM   3543  N  N     . HIS   A  1  481  ? -29.760 61.571  64.743  1.00 33.41 ? 479  HIS   A N     1 
ATOM   3544  C  CA    . HIS   A  1  481  ? -28.698 60.969  65.544  1.00 37.24 ? 479  HIS   A CA    1 
ATOM   3545  C  C     . HIS   A  1  481  ? -28.480 61.741  66.839  1.00 38.32 ? 479  HIS   A C     1 
ATOM   3546  O  O     . HIS   A  1  481  ? -28.385 61.146  67.921  1.00 33.78 ? 479  HIS   A O     1 
ATOM   3547  C  CB    . HIS   A  1  481  ? -27.402 60.920  64.737  1.00 33.17 ? 479  HIS   A CB    1 
ATOM   3548  C  CG    . HIS   A  1  481  ? -27.468 60.032  63.534  1.00 34.78 ? 479  HIS   A CG    1 
ATOM   3549  N  ND1   . HIS   A  1  481  ? -26.383 59.821  62.707  1.00 33.74 ? 479  HIS   A ND1   1 
ATOM   3550  C  CD2   . HIS   A  1  481  ? -28.485 59.301  63.016  1.00 35.55 ? 479  HIS   A CD2   1 
ATOM   3551  C  CE1   . HIS   A  1  481  ? -26.730 59.000  61.732  1.00 36.12 ? 479  HIS   A CE1   1 
ATOM   3552  N  NE2   . HIS   A  1  481  ? -27.998 58.666  61.899  1.00 35.29 ? 479  HIS   A NE2   1 
ATOM   3553  N  N     . GLU   A  1  482  ? -28.388 63.072  66.746  1.00 41.22 ? 480  GLU   A N     1 
ATOM   3554  C  CA    . GLU   A  1  482  ? -28.190 63.891  67.940  1.00 45.48 ? 480  GLU   A CA    1 
ATOM   3555  C  C     . GLU   A  1  482  ? -29.291 63.649  68.961  1.00 41.28 ? 480  GLU   A C     1 
ATOM   3556  O  O     . GLU   A  1  482  ? -29.024 63.541  70.164  1.00 40.70 ? 480  GLU   A O     1 
ATOM   3557  C  CB    . GLU   A  1  482  ? -28.143 65.371  67.553  1.00 44.06 ? 480  GLU   A CB    1 
ATOM   3558  N  N     . THR   A  1  483  ? -30.537 63.543  68.496  1.00 36.64 ? 481  THR   A N     1 
ATOM   3559  C  CA    . THR   A  1  483  ? -31.662 63.394  69.410  1.00 36.12 ? 481  THR   A CA    1 
ATOM   3560  C  C     . THR   A  1  483  ? -31.662 62.025  70.081  1.00 36.90 ? 481  THR   A C     1 
ATOM   3561  O  O     . THR   A  1  483  ? -31.914 61.922  71.287  1.00 34.36 ? 481  THR   A O     1 
ATOM   3562  C  CB    . THR   A  1  483  ? -32.967 63.613  68.649  1.00 31.67 ? 481  THR   A CB    1 
ATOM   3563  O  OG1   . THR   A  1  483  ? -32.955 64.914  68.053  1.00 40.59 ? 481  THR   A OG1   1 
ATOM   3564  C  CG2   . THR   A  1  483  ? -34.151 63.515  69.589  1.00 40.53 ? 481  THR   A CG2   1 
ATOM   3565  N  N     . LEU   A  1  484  ? -31.395 60.961  69.320  1.00 32.65 ? 482  LEU   A N     1 
ATOM   3566  C  CA    . LEU   A  1  484  ? -31.501 59.622  69.890  1.00 31.35 ? 482  LEU   A CA    1 
ATOM   3567  C  C     . LEU   A  1  484  ? -30.365 59.331  70.863  1.00 32.20 ? 482  LEU   A C     1 
ATOM   3568  O  O     . LEU   A  1  484  ? -30.562 58.620  71.855  1.00 32.33 ? 482  LEU   A O     1 
ATOM   3569  C  CB    . LEU   A  1  484  ? -31.578 58.569  68.781  1.00 31.76 ? 482  LEU   A CB    1 
ATOM   3570  C  CG    . LEU   A  1  484  ? -30.356 58.371  67.879  1.00 32.47 ? 482  LEU   A CG    1 
ATOM   3571  C  CD1   . LEU   A  1  484  ? -29.453 57.277  68.433  1.00 33.21 ? 482  LEU   A CD1   1 
ATOM   3572  C  CD2   . LEU   A  1  484  ? -30.767 58.048  66.454  1.00 35.94 ? 482  LEU   A CD2   1 
ATOM   3573  N  N     . LEU   A  1  485  ? -29.170 59.863  70.602  1.00 35.67 ? 483  LEU   A N     1 
ATOM   3574  C  CA    . LEU   A  1  485  ? -28.042 59.585  71.484  1.00 28.60 ? 483  LEU   A CA    1 
ATOM   3575  C  C     . LEU   A  1  485  ? -28.214 60.210  72.862  1.00 34.18 ? 483  LEU   A C     1 
ATOM   3576  O  O     . LEU   A  1  485  ? -27.598 59.734  73.824  1.00 34.76 ? 483  LEU   A O     1 
ATOM   3577  C  CB    . LEU   A  1  485  ? -26.737 60.063  70.844  1.00 31.22 ? 483  LEU   A CB    1 
ATOM   3578  C  CG    . LEU   A  1  485  ? -26.264 59.280  69.615  1.00 33.70 ? 483  LEU   A CG    1 
ATOM   3579  C  CD1   . LEU   A  1  485  ? -25.130 60.021  68.938  1.00 33.70 ? 483  LEU   A CD1   1 
ATOM   3580  C  CD2   . LEU   A  1  485  ? -25.842 57.864  69.989  1.00 32.71 ? 483  LEU   A CD2   1 
ATOM   3581  N  N     . ALA   A  1  486  ? -29.057 61.242  72.974  1.00 36.34 ? 484  ALA   A N     1 
ATOM   3582  C  CA    . ALA   A  1  486  ? -29.157 62.019  74.205  1.00 36.87 ? 484  ALA   A CA    1 
ATOM   3583  C  C     . ALA   A  1  486  ? -29.481 61.138  75.408  1.00 39.25 ? 484  ALA   A C     1 
ATOM   3584  O  O     . ALA   A  1  486  ? -28.844 61.255  76.462  1.00 36.52 ? 484  ALA   A O     1 
ATOM   3585  C  CB    . ALA   A  1  486  ? -30.201 63.124  74.038  1.00 36.76 ? 484  ALA   A CB    1 
ATOM   3586  N  N     . TYR   A  1  487  ? -30.467 60.244  75.272  1.00 37.26 ? 485  TYR   A N     1 
ATOM   3587  C  CA    . TYR   A  1  487  ? -30.882 59.385  76.379  1.00 36.61 ? 485  TYR   A CA    1 
ATOM   3588  C  C     . TYR   A  1  487  ? -30.891 57.914  75.980  1.00 35.85 ? 485  TYR   A C     1 
ATOM   3589  O  O     . TYR   A  1  487  ? -31.646 57.113  76.540  1.00 30.09 ? 485  TYR   A O     1 
ATOM   3590  C  CB    . TYR   A  1  487  ? -32.229 59.822  76.959  1.00 40.34 ? 485  TYR   A CB    1 
ATOM   3591  C  CG    . TYR   A  1  487  ? -32.217 61.255  77.447  1.00 44.75 ? 485  TYR   A CG    1 
ATOM   3592  C  CD1   . TYR   A  1  487  ? -31.713 61.579  78.703  1.00 45.54 ? 485  TYR   A CD1   1 
ATOM   3593  C  CD2   . TYR   A  1  487  ? -32.689 62.286  76.642  1.00 43.74 ? 485  TYR   A CD2   1 
ATOM   3594  C  CE1   . TYR   A  1  487  ? -31.687 62.894  79.147  1.00 50.98 ? 485  TYR   A CE1   1 
ATOM   3595  C  CE2   . TYR   A  1  487  ? -32.668 63.600  77.075  1.00 45.76 ? 485  TYR   A CE2   1 
ATOM   3596  C  CZ    . TYR   A  1  487  ? -32.167 63.901  78.327  1.00 55.30 ? 485  TYR   A CZ    1 
ATOM   3597  O  OH    . TYR   A  1  487  ? -32.148 65.211  78.756  1.00 56.57 ? 485  TYR   A OH    1 
ATOM   3598  N  N     . LEU   A  1  488  ? -30.040 57.539  75.023  1.00 32.88 ? 486  LEU   A N     1 
ATOM   3599  C  CA    . LEU   A  1  488  ? -29.985 56.143  74.609  1.00 30.49 ? 486  LEU   A CA    1 
ATOM   3600  C  C     . LEU   A  1  488  ? -29.462 55.247  75.725  1.00 29.10 ? 486  LEU   A C     1 
ATOM   3601  O  O     . LEU   A  1  488  ? -29.833 54.069  75.800  1.00 28.36 ? 486  LEU   A O     1 
ATOM   3602  C  CB    . LEU   A  1  488  ? -29.122 56.003  73.358  1.00 28.82 ? 486  LEU   A CB    1 
ATOM   3603  C  CG    . LEU   A  1  488  ? -29.110 54.601  72.755  1.00 33.78 ? 486  LEU   A CG    1 
ATOM   3604  C  CD1   . LEU   A  1  488  ? -30.541 54.130  72.558  1.00 33.81 ? 486  LEU   A CD1   1 
ATOM   3605  C  CD2   . LEU   A  1  488  ? -28.363 54.597  71.441  1.00 31.65 ? 486  LEU   A CD2   1 
ATOM   3606  N  N     . VAL   A  1  489  ? -28.604 55.782  76.598  1.00 33.47 ? 487  VAL   A N     1 
ATOM   3607  C  CA    . VAL   A  1  489  ? -28.091 54.985  77.710  1.00 27.49 ? 487  VAL   A CA    1 
ATOM   3608  C  C     . VAL   A  1  489  ? -29.238 54.466  78.567  1.00 28.72 ? 487  VAL   A C     1 
ATOM   3609  O  O     . VAL   A  1  489  ? -29.308 53.271  78.875  1.00 28.00 ? 487  VAL   A O     1 
ATOM   3610  C  CB    . VAL   A  1  489  ? -27.070 55.785  78.537  1.00 28.61 ? 487  VAL   A CB    1 
ATOM   3611  C  CG1   . VAL   A  1  489  ? -26.805 55.080  79.866  1.00 32.72 ? 487  VAL   A CG1   1 
ATOM   3612  C  CG2   . VAL   A  1  489  ? -25.768 55.968  77.752  1.00 27.69 ? 487  VAL   A CG2   1 
ATOM   3613  N  N     . ARG   A  1  490  ? -30.159 55.354  78.958  1.00 33.03 ? 488  ARG   A N     1 
ATOM   3614  C  CA    . ARG   A  1  490  ? -31.305 54.921  79.755  1.00 33.69 ? 488  ARG   A CA    1 
ATOM   3615  C  C     . ARG   A  1  490  ? -32.117 53.859  79.021  1.00 34.35 ? 488  ARG   A C     1 
ATOM   3616  O  O     . ARG   A  1  490  ? -32.552 52.872  79.626  1.00 31.65 ? 488  ARG   A O     1 
ATOM   3617  C  CB    . ARG   A  1  490  ? -32.183 56.120  80.130  1.00 34.38 ? 488  ARG   A CB    1 
ATOM   3618  C  CG    . ARG   A  1  490  ? -33.351 55.769  81.058  1.00 34.02 ? 488  ARG   A CG    1 
ATOM   3619  C  CD    . ARG   A  1  490  ? -34.314 56.941  81.291  1.00 36.62 ? 488  ARG   A CD    1 
ATOM   3620  N  NE    . ARG   A  1  490  ? -35.091 57.273  80.098  1.00 37.51 ? 488  ARG   A NE    1 
ATOM   3621  C  CZ    . ARG   A  1  490  ? -35.238 58.499  79.612  1.00 36.33 ? 488  ARG   A CZ    1 
ATOM   3622  N  NH1   . ARG   A  1  490  ? -34.684 59.549  80.201  1.00 34.86 ? 488  ARG   A NH1   1 
ATOM   3623  N  NH2   . ARG   A  1  490  ? -35.961 58.677  78.509  1.00 32.65 ? 488  ARG   A NH2   1 
ATOM   3624  N  N     . ARG   A  1  491  ? -32.302 54.030  77.708  1.00 32.38 ? 489  ARG   A N     1 
ATOM   3625  C  CA    . ARG   A  1  491  ? -33.130 53.103  76.945  1.00 38.56 ? 489  ARG   A CA    1 
ATOM   3626  C  C     . ARG   A  1  491  ? -32.494 51.723  76.870  1.00 44.35 ? 489  ARG   A C     1 
ATOM   3627  O  O     . ARG   A  1  491  ? -33.198 50.708  76.921  1.00 42.69 ? 489  ARG   A O     1 
ATOM   3628  C  CB    . ARG   A  1  491  ? -33.375 53.660  75.542  1.00 40.99 ? 489  ARG   A CB    1 
ATOM   3629  N  N     . LEU   A  1  492  ? -31.162 51.666  76.760  1.00 40.34 ? 490  LEU   A N     1 
ATOM   3630  C  CA    . LEU   A  1  492  ? -30.478 50.381  76.641  1.00 39.83 ? 490  LEU   A CA    1 
ATOM   3631  C  C     . LEU   A  1  492  ? -30.499 49.610  77.958  1.00 41.79 ? 490  LEU   A C     1 
ATOM   3632  O  O     . LEU   A  1  492  ? -30.653 48.381  77.962  1.00 35.98 ? 490  LEU   A O     1 
ATOM   3633  C  CB    . LEU   A  1  492  ? -29.040 50.595  76.160  1.00 35.06 ? 490  LEU   A CB    1 
ATOM   3634  C  CG    . LEU   A  1  492  ? -28.854 51.151  74.745  1.00 36.84 ? 490  LEU   A CG    1 
ATOM   3635  C  CD1   . LEU   A  1  492  ? -27.423 51.651  74.518  1.00 36.73 ? 490  LEU   A CD1   1 
ATOM   3636  C  CD2   . LEU   A  1  492  ? -29.235 50.101  73.709  1.00 38.31 ? 490  LEU   A CD2   1 
ATOM   3637  N  N     . LEU   A  1  493  ? -30.337 50.306  79.080  1.00 36.10 ? 491  LEU   A N     1 
ATOM   3638  C  CA    . LEU   A  1  493  ? -30.344 49.648  80.381  1.00 29.20 ? 491  LEU   A CA    1 
ATOM   3639  C  C     . LEU   A  1  493  ? -31.699 48.997  80.653  1.00 37.76 ? 491  LEU   A C     1 
ATOM   3640  O  O     . LEU   A  1  493  ? -31.794 48.048  81.434  1.00 41.17 ? 491  LEU   A O     1 
ATOM   3641  C  CB    . LEU   A  1  493  ? -30.014 50.643  81.494  1.00 37.94 ? 491  LEU   A CB    1 
ATOM   3642  C  CG    . LEU   A  1  493  ? -28.632 51.288  81.438  1.00 40.94 ? 491  LEU   A CG    1 
ATOM   3643  C  CD1   . LEU   A  1  493  ? -28.366 52.061  82.728  1.00 39.27 ? 491  LEU   A CD1   1 
ATOM   3644  C  CD2   . LEU   A  1  493  ? -27.574 50.222  81.193  1.00 42.98 ? 491  LEU   A CD2   1 
ATOM   3645  N  N     . ALA   A  1  497  ? -29.318 45.478  81.613  1.00 40.67 ? 495  ALA   A N     1 
ATOM   3646  C  CA    . ALA   A  1  497  ? -28.901 45.171  82.980  1.00 37.36 ? 495  ALA   A CA    1 
ATOM   3647  C  C     . ALA   A  1  497  ? -28.972 43.673  83.232  1.00 34.07 ? 495  ALA   A C     1 
ATOM   3648  O  O     . ALA   A  1  497  ? -29.734 42.966  82.572  1.00 33.85 ? 495  ALA   A O     1 
ATOM   3649  C  CB    . ALA   A  1  497  ? -29.777 45.918  83.985  1.00 32.74 ? 495  ALA   A CB    1 
ATOM   3650  N  N     . ASN   A  1  498  ? -28.193 43.189  84.206  1.00 36.16 ? 496  ASN   A N     1 
ATOM   3651  C  CA    . ASN   A  1  498  ? -28.149 41.750  84.466  1.00 35.50 ? 496  ASN   A CA    1 
ATOM   3652  C  C     . ASN   A  1  498  ? -29.519 41.180  84.815  1.00 33.31 ? 496  ASN   A C     1 
ATOM   3653  O  O     . ASN   A  1  498  ? -29.794 40.012  84.519  1.00 36.15 ? 496  ASN   A O     1 
ATOM   3654  C  CB    . ASN   A  1  498  ? -27.150 41.436  85.579  1.00 40.97 ? 496  ASN   A CB    1 
ATOM   3655  C  CG    . ASN   A  1  498  ? -25.713 41.596  85.131  1.00 52.25 ? 496  ASN   A CG    1 
ATOM   3656  O  OD1   . ASN   A  1  498  ? -25.408 41.500  83.941  1.00 52.98 ? 496  ASN   A OD1   1 
ATOM   3657  N  ND2   . ASN   A  1  498  ? -24.818 41.836  86.085  1.00 54.75 ? 496  ASN   A ND2   1 
ATOM   3658  N  N     . SER   A  1  499  ? -30.383 41.973  85.451  1.00 32.64 ? 497  SER   A N     1 
ATOM   3659  C  CA    . SER   A  1  499  ? -31.711 41.500  85.819  1.00 34.31 ? 497  SER   A CA    1 
ATOM   3660  C  C     . SER   A  1  499  ? -32.722 41.608  84.684  1.00 27.04 ? 497  SER   A C     1 
ATOM   3661  O  O     . SER   A  1  499  ? -33.833 41.082  84.816  1.00 31.67 ? 497  SER   A O     1 
ATOM   3662  C  CB    . SER   A  1  499  ? -32.225 42.278  87.035  1.00 37.29 ? 497  SER   A CB    1 
ATOM   3663  O  OG    . SER   A  1  499  ? -32.080 43.674  86.833  1.00 40.90 ? 497  SER   A OG    1 
ATOM   3664  N  N     . SER   A  1  500  ? -32.364 42.258  83.579  1.00 27.56 ? 498  SER   A N     1 
ATOM   3665  C  CA    . SER   A  1  500  ? -33.309 42.484  82.494  1.00 24.49 ? 498  SER   A CA    1 
ATOM   3666  C  C     . SER   A  1  500  ? -33.571 41.206  81.714  1.00 30.88 ? 498  SER   A C     1 
ATOM   3667  O  O     . SER   A  1  500  ? -32.655 40.421  81.449  1.00 28.63 ? 498  SER   A O     1 
ATOM   3668  C  CB    . SER   A  1  500  ? -32.769 43.544  81.540  1.00 30.03 ? 498  SER   A CB    1 
ATOM   3669  O  OG    . SER   A  1  500  ? -32.758 44.806  82.164  1.00 33.03 ? 498  SER   A OG    1 
ATOM   3670  N  N     . PHE   A  1  501  ? -34.835 41.013  81.322  1.00 25.42 ? 499  PHE   A N     1 
ATOM   3671  C  CA    . PHE   A  1  501  ? -35.200 39.826  80.560  1.00 26.57 ? 499  PHE   A CA    1 
ATOM   3672  C  C     . PHE   A  1  501  ? -34.394 39.725  79.274  1.00 30.84 ? 499  PHE   A C     1 
ATOM   3673  O  O     . PHE   A  1  501  ? -33.925 38.642  78.908  1.00 30.61 ? 499  PHE   A O     1 
ATOM   3674  C  CB    . PHE   A  1  501  ? -36.694 39.839  80.232  1.00 25.79 ? 499  PHE   A CB    1 
ATOM   3675  C  CG    . PHE   A  1  501  ? -37.115 38.696  79.352  1.00 24.49 ? 499  PHE   A CG    1 
ATOM   3676  C  CD1   . PHE   A  1  501  ? -37.475 37.483  79.903  1.00 24.95 ? 499  PHE   A CD1   1 
ATOM   3677  C  CD2   . PHE   A  1  501  ? -37.137 38.833  77.972  1.00 29.47 ? 499  PHE   A CD2   1 
ATOM   3678  C  CE1   . PHE   A  1  501  ? -37.850 36.425  79.102  1.00 28.01 ? 499  PHE   A CE1   1 
ATOM   3679  C  CE2   . PHE   A  1  501  ? -37.511 37.774  77.162  1.00 27.29 ? 499  PHE   A CE2   1 
ATOM   3680  C  CZ    . PHE   A  1  501  ? -37.869 36.571  77.732  1.00 29.98 ? 499  PHE   A CZ    1 
ATOM   3681  N  N     . VAL   A  1  502  ? -34.248 40.843  78.561  1.00 30.00 ? 500  VAL   A N     1 
ATOM   3682  C  CA    . VAL   A  1  502  ? -33.588 40.812  77.260  1.00 32.41 ? 500  VAL   A CA    1 
ATOM   3683  C  C     . VAL   A  1  502  ? -32.118 40.453  77.415  1.00 33.99 ? 500  VAL   A C     1 
ATOM   3684  O  O     . VAL   A  1  502  ? -31.534 39.773  76.562  1.00 40.52 ? 500  VAL   A O     1 
ATOM   3685  C  CB    . VAL   A  1  502  ? -33.795 42.143  76.516  1.00 34.25 ? 500  VAL   A CB    1 
ATOM   3686  C  CG1   . VAL   A  1  502  ? -32.955 42.179  75.243  1.00 44.10 ? 500  VAL   A CG1   1 
ATOM   3687  C  CG2   . VAL   A  1  502  ? -35.272 42.337  76.192  1.00 34.60 ? 500  VAL   A CG2   1 
ATOM   3688  N  N     . HIS   A  1  503  ? -31.494 40.895  78.504  1.00 29.55 ? 501  HIS   A N     1 
ATOM   3689  C  CA    . HIS   A  1  503  ? -30.137 40.446  78.788  1.00 29.77 ? 501  HIS   A CA    1 
ATOM   3690  C  C     . HIS   A  1  503  ? -30.124 38.960  79.118  1.00 34.28 ? 501  HIS   A C     1 
ATOM   3691  O  O     . HIS   A  1  503  ? -29.297 38.202  78.598  1.00 31.12 ? 501  HIS   A O     1 
ATOM   3692  C  CB    . HIS   A  1  503  ? -29.542 41.271  79.930  1.00 32.52 ? 501  HIS   A CB    1 
ATOM   3693  C  CG    . HIS   A  1  503  ? -28.148 40.868  80.303  1.00 38.69 ? 501  HIS   A CG    1 
ATOM   3694  N  ND1   . HIS   A  1  503  ? -27.873 40.021  81.357  1.00 37.39 ? 501  HIS   A ND1   1 
ATOM   3695  C  CD2   . HIS   A  1  503  ? -26.951 41.193  79.760  1.00 39.72 ? 501  HIS   A CD2   1 
ATOM   3696  C  CE1   . HIS   A  1  503  ? -26.567 39.843  81.448  1.00 38.32 ? 501  HIS   A CE1   1 
ATOM   3697  N  NE2   . HIS   A  1  503  ? -25.984 40.543  80.489  1.00 37.27 ? 501  HIS   A NE2   1 
ATOM   3698  N  N     . ARG   A  1  504  ? -31.065 38.516  79.952  1.00 29.91 ? 502  ARG   A N     1 
ATOM   3699  C  CA    . ARG   A  1  504  ? -31.066 37.126  80.390  1.00 29.78 ? 502  ARG   A CA    1 
ATOM   3700  C  C     . ARG   A  1  504  ? -31.397 36.172  79.247  1.00 32.64 ? 502  ARG   A C     1 
ATOM   3701  O  O     . ARG   A  1  504  ? -30.833 35.073  79.171  1.00 33.13 ? 502  ARG   A O     1 
ATOM   3702  C  CB    . ARG   A  1  504  ? -32.022 36.952  81.571  1.00 31.06 ? 502  ARG   A CB    1 
ATOM   3703  C  CG    . ARG   A  1  504  ? -31.537 37.665  82.825  1.00 30.89 ? 502  ARG   A CG    1 
ATOM   3704  C  CD    . ARG   A  1  504  ? -32.668 37.900  83.815  1.00 31.32 ? 502  ARG   A CD    1 
ATOM   3705  N  NE    . ARG   A  1  504  ? -33.432 36.689  84.076  1.00 35.05 ? 502  ARG   A NE    1 
ATOM   3706  C  CZ    . ARG   A  1  504  ? -33.051 35.723  84.900  1.00 38.31 ? 502  ARG   A CZ    1 
ATOM   3707  N  NH1   . ARG   A  1  504  ? -31.883 35.765  85.519  1.00 40.10 ? 502  ARG   A NH1   1 
ATOM   3708  N  NH2   . ARG   A  1  504  ? -33.863 34.689  85.109  1.00 37.66 ? 502  ARG   A NH2   1 
ATOM   3709  N  N     . ILE   A  1  505  ? -32.299 36.571  78.343  1.00 33.51 ? 503  ILE   A N     1 
ATOM   3710  C  CA    . ILE   A  1  505  ? -32.643 35.713  77.208  1.00 33.62 ? 503  ILE   A CA    1 
ATOM   3711  C  C     . ILE   A  1  505  ? -31.409 35.404  76.368  1.00 36.88 ? 503  ILE   A C     1 
ATOM   3712  O  O     . ILE   A  1  505  ? -31.286 34.306  75.809  1.00 39.88 ? 503  ILE   A O     1 
ATOM   3713  C  CB    . ILE   A  1  505  ? -33.795 36.322  76.374  1.00 37.80 ? 503  ILE   A CB    1 
ATOM   3714  C  CG1   . ILE   A  1  505  ? -34.324 35.317  75.358  1.00 43.73 ? 503  ILE   A CG1   1 
ATOM   3715  C  CG2   . ILE   A  1  505  ? -33.345 37.546  75.620  1.00 39.36 ? 503  ILE   A CG2   1 
ATOM   3716  C  CD1   . ILE   A  1  505  ? -35.372 34.419  75.909  1.00 34.66 ? 503  ILE   A CD1   1 
ATOM   3717  N  N     . ASN   A  1  506  ? -30.466 36.341  76.293  1.00 33.36 ? 504  ASN   A N     1 
ATOM   3718  C  CA    . ASN   A  1  506  ? -29.240 36.173  75.525  1.00 37.71 ? 504  ASN   A CA    1 
ATOM   3719  C  C     . ASN   A  1  506  ? -28.109 35.542  76.324  1.00 37.66 ? 504  ASN   A C     1 
ATOM   3720  O  O     . ASN   A  1  506  ? -27.028 35.320  75.766  1.00 41.75 ? 504  ASN   A O     1 
ATOM   3721  C  CB    . ASN   A  1  506  ? -28.771 37.520  74.977  1.00 39.02 ? 504  ASN   A CB    1 
ATOM   3722  C  CG    . ASN   A  1  506  ? -29.681 38.056  73.900  1.00 39.75 ? 504  ASN   A CG    1 
ATOM   3723  O  OD1   . ASN   A  1  506  ? -30.318 37.294  73.173  1.00 48.46 ? 504  ASN   A OD1   1 
ATOM   3724  N  ND2   . ASN   A  1  506  ? -29.749 39.378  73.787  1.00 47.99 ? 504  ASN   A ND2   1 
ATOM   3725  N  N     . ASP   A  1  507  ? -28.315 35.260  77.609  1.00 35.15 ? 505  ASP   A N     1 
ATOM   3726  C  CA    . ASP   A  1  507  ? -27.274 34.659  78.431  1.00 36.02 ? 505  ASP   A CA    1 
ATOM   3727  C  C     . ASP   A  1  507  ? -27.440 33.147  78.389  1.00 42.36 ? 505  ASP   A C     1 
ATOM   3728  O  O     . ASP   A  1  507  ? -28.434 32.631  78.919  1.00 35.90 ? 505  ASP   A O     1 
ATOM   3729  C  CB    . ASP   A  1  507  ? -27.372 35.163  79.863  1.00 36.03 ? 505  ASP   A CB    1 
ATOM   3730  C  CG    . ASP   A  1  507  ? -26.217 34.690  80.734  1.00 42.25 ? 505  ASP   A CG    1 
ATOM   3731  O  OD1   . ASP   A  1  507  ? -25.492 33.758  80.325  1.00 46.12 ? 505  ASP   A OD1   1 
ATOM   3732  O  OD2   . ASP   A  1  507  ? -26.027 35.254  81.830  1.00 42.01 ? 505  ASP   A OD2   1 
ATOM   3733  N  N     . PRO   A  1  508  ? -26.501 32.398  77.800  1.00 45.94 ? 506  PRO   A N     1 
ATOM   3734  C  CA    . PRO   A  1  508  ? -26.647 30.933  77.769  1.00 45.93 ? 506  PRO   A CA    1 
ATOM   3735  C  C     . PRO   A  1  508  ? -26.595 30.292  79.142  1.00 43.93 ? 506  PRO   A C     1 
ATOM   3736  O  O     . PRO   A  1  508  ? -27.065 29.157  79.296  1.00 52.16 ? 506  PRO   A O     1 
ATOM   3737  C  CB    . PRO   A  1  508  ? -25.472 30.471  76.894  1.00 47.60 ? 506  PRO   A CB    1 
ATOM   3738  C  CG    . PRO   A  1  508  ? -24.972 31.717  76.201  1.00 52.98 ? 506  PRO   A CG    1 
ATOM   3739  C  CD    . PRO   A  1  508  ? -25.271 32.850  77.132  1.00 44.32 ? 506  PRO   A CD    1 
ATOM   3740  N  N     . LYS   A  1  509  ? -26.042 30.977  80.143  1.00 39.52 ? 507  LYS   A N     1 
ATOM   3741  C  CA    . LYS   A  1  509  ? -26.037 30.459  81.505  1.00 38.43 ? 507  LYS   A CA    1 
ATOM   3742  C  C     . LYS   A  1  509  ? -27.408 30.519  82.169  1.00 41.03 ? 507  LYS   A C     1 
ATOM   3743  O  O     . LYS   A  1  509  ? -27.575 29.945  83.250  1.00 43.27 ? 507  LYS   A O     1 
ATOM   3744  C  CB    . LYS   A  1  509  ? -25.020 31.229  82.349  1.00 44.38 ? 507  LYS   A CB    1 
ATOM   3745  N  N     . VAL   A  1  510  ? -28.384 31.195  81.568  1.00 38.22 ? 508  VAL   A N     1 
ATOM   3746  C  CA    . VAL   A  1  510  ? -29.727 31.307  82.131  1.00 35.65 ? 508  VAL   A CA    1 
ATOM   3747  C  C     . VAL   A  1  510  ? -30.632 30.313  81.413  1.00 33.89 ? 508  VAL   A C     1 
ATOM   3748  O  O     . VAL   A  1  510  ? -30.793 30.376  80.189  1.00 35.62 ? 508  VAL   A O     1 
ATOM   3749  C  CB    . VAL   A  1  510  ? -30.266 32.743  82.015  1.00 35.99 ? 508  VAL   A CB    1 
ATOM   3750  C  CG1   . VAL   A  1  510  ? -31.666 32.830  82.596  1.00 34.39 ? 508  VAL   A CG1   1 
ATOM   3751  C  CG2   . VAL   A  1  510  ? -29.342 33.728  82.720  1.00 32.38 ? 508  VAL   A CG2   1 
ATOM   3752  N  N     . SER   A  1  511  ? -31.220 29.388  82.166  1.00 32.02 ? 509  SER   A N     1 
ATOM   3753  C  CA    . SER   A  1  511  ? -32.063 28.368  81.569  1.00 31.78 ? 509  SER   A CA    1 
ATOM   3754  C  C     . SER   A  1  511  ? -33.457 28.920  81.303  1.00 30.40 ? 509  SER   A C     1 
ATOM   3755  O  O     . SER   A  1  511  ? -33.870 29.940  81.865  1.00 34.06 ? 509  SER   A O     1 
ATOM   3756  C  CB    . SER   A  1  511  ? -32.188 27.162  82.500  1.00 39.29 ? 509  SER   A CB    1 
ATOM   3757  O  OG    . SER   A  1  511  ? -32.901 27.506  83.676  1.00 36.68 ? 509  SER   A OG    1 
ATOM   3758  N  N     . ILE   A  1  512  ? -34.188 28.223  80.435  1.00 32.27 ? 510  ILE   A N     1 
ATOM   3759  C  CA    . ILE   A  1  512  ? -35.579 28.586  80.189  1.00 32.57 ? 510  ILE   A CA    1 
ATOM   3760  C  C     . ILE   A  1  512  ? -36.403 28.421  81.457  1.00 37.26 ? 510  ILE   A C     1 
ATOM   3761  O  O     . ILE   A  1  512  ? -37.302 29.221  81.739  1.00 32.94 ? 510  ILE   A O     1 
ATOM   3762  C  CB    . ILE   A  1  512  ? -36.140 27.777  79.008  1.00 34.37 ? 510  ILE   A CB    1 
ATOM   3763  C  CG1   . ILE   A  1  512  ? -35.382 28.143  77.731  1.00 35.42 ? 510  ILE   A CG1   1 
ATOM   3764  C  CG2   . ILE   A  1  512  ? -37.630 28.028  78.843  1.00 36.42 ? 510  ILE   A CG2   1 
ATOM   3765  C  CD1   . ILE   A  1  512  ? -35.826 27.379  76.521  1.00 38.51 ? 510  ILE   A CD1   1 
ATOM   3766  N  N     . ASP   A  1  513  ? -36.096 27.394  82.255  1.00 33.82 ? 511  ASP   A N     1 
ATOM   3767  C  CA    . ASP   A  1  513  ? -36.785 27.222  83.529  1.00 34.69 ? 511  ASP   A CA    1 
ATOM   3768  C  C     . ASP   A  1  513  ? -36.588 28.430  84.439  1.00 35.60 ? 511  ASP   A C     1 
ATOM   3769  O  O     . ASP   A  1  513  ? -37.529 28.862  85.115  1.00 34.93 ? 511  ASP   A O     1 
ATOM   3770  C  CB    . ASP   A  1  513  ? -36.325 25.935  84.212  1.00 40.79 ? 511  ASP   A CB    1 
ATOM   3771  C  CG    . ASP   A  1  513  ? -36.813 24.696  83.493  1.00 43.21 ? 511  ASP   A CG    1 
ATOM   3772  O  OD1   . ASP   A  1  513  ? -37.967 24.697  83.017  1.00 46.13 ? 511  ASP   A OD1   1 
ATOM   3773  O  OD2   . ASP   A  1  513  ? -36.039 23.723  83.397  1.00 56.23 ? 511  ASP   A OD2   1 
ATOM   3774  N  N     . GLU   A  1  514  ? -35.378 28.995  84.462  1.00 31.28 ? 512  GLU   A N     1 
ATOM   3775  C  CA    . GLU   A  1  514  ? -35.145 30.218  85.226  1.00 34.11 ? 512  GLU   A CA    1 
ATOM   3776  C  C     . GLU   A  1  514  ? -35.964 31.381  84.676  1.00 34.48 ? 512  GLU   A C     1 
ATOM   3777  O  O     . GLU   A  1  514  ? -36.478 32.208  85.440  1.00 31.52 ? 512  GLU   A O     1 
ATOM   3778  C  CB    . GLU   A  1  514  ? -33.658 30.578  85.204  1.00 35.18 ? 512  GLU   A CB    1 
ATOM   3779  C  CG    . GLU   A  1  514  ? -32.767 29.667  86.027  1.00 41.72 ? 512  GLU   A CG    1 
ATOM   3780  C  CD    . GLU   A  1  514  ? -31.289 29.925  85.770  1.00 47.25 ? 512  GLU   A CD    1 
ATOM   3781  O  OE1   . GLU   A  1  514  ? -30.783 29.484  84.718  1.00 47.17 ? 512  GLU   A OE1   1 
ATOM   3782  O  OE2   . GLU   A  1  514  ? -30.638 30.585  86.608  1.00 51.58 ? 512  GLU   A OE2   1 
ATOM   3783  N  N     . LEU   A  1  515  ? -36.088 31.464  83.349  1.00 34.00 ? 513  LEU   A N     1 
ATOM   3784  C  CA    . LEU   A  1  515  ? -36.792 32.583  82.732  1.00 29.99 ? 513  LEU   A CA    1 
ATOM   3785  C  C     . LEU   A  1  515  ? -38.294 32.472  82.914  1.00 29.41 ? 513  LEU   A C     1 
ATOM   3786  O  O     . LEU   A  1  515  ? -38.989 33.493  82.938  1.00 30.00 ? 513  LEU   A O     1 
ATOM   3787  C  CB    . LEU   A  1  515  ? -36.463 32.649  81.243  1.00 30.19 ? 513  LEU   A CB    1 
ATOM   3788  C  CG    . LEU   A  1  515  ? -35.032 33.063  80.907  1.00 30.10 ? 513  LEU   A CG    1 
ATOM   3789  C  CD1   . LEU   A  1  515  ? -34.752 32.854  79.423  1.00 32.47 ? 513  LEU   A CD1   1 
ATOM   3790  C  CD2   . LEU   A  1  515  ? -34.779 34.510  81.323  1.00 29.75 ? 513  LEU   A CD2   1 
ATOM   3791  N  N     . ILE   A  1  516  ? -38.817 31.247  83.018  1.00 28.52 ? 514  ILE   A N     1 
ATOM   3792  C  CA    . ILE   A  1  516  ? -40.250 31.066  83.208  1.00 27.41 ? 514  ILE   A CA    1 
ATOM   3793  C  C     . ILE   A  1  516  ? -40.637 30.965  84.673  1.00 30.46 ? 514  ILE   A C     1 
ATOM   3794  O  O     . ILE   A  1  516  ? -41.814 30.719  84.974  1.00 30.58 ? 514  ILE   A O     1 
ATOM   3795  C  CB    . ILE   A  1  516  ? -40.797 29.883  82.386  1.00 29.56 ? 514  ILE   A CB    1 
ATOM   3796  C  CG1   . ILE   A  1  516  ? -40.245 28.557  82.914  1.00 35.60 ? 514  ILE   A CG1   1 
ATOM   3797  C  CG2   . ILE   A  1  516  ? -40.476 30.088  80.911  1.00 31.35 ? 514  ILE   A CG2   1 
ATOM   3798  C  CD1   . ILE   A  1  516  ? -40.756 27.345  82.169  1.00 38.28 ? 514  ILE   A CD1   1 
ATOM   3799  N  N     . ALA   A  1  517  ? -39.690 31.144  85.592  1.00 28.78 ? 515  ALA   A N     1 
ATOM   3800  C  CA    . ALA   A  1  517  ? -40.021 31.168  87.008  1.00 33.23 ? 515  ALA   A CA    1 
ATOM   3801  C  C     . ALA   A  1  517  ? -41.113 32.196  87.258  1.00 32.47 ? 515  ALA   A C     1 
ATOM   3802  O  O     . ALA   A  1  517  ? -41.087 33.299  86.711  1.00 31.13 ? 515  ALA   A O     1 
ATOM   3803  C  CB    . ALA   A  1  517  ? -38.788 31.531  87.833  1.00 34.25 ? 515  ALA   A CB    1 
ATOM   3804  N  N     . ASP   A  1  518  ? -42.083 31.816  88.068  1.00 29.73 ? 516  ASP   A N     1 
ATOM   3805  C  CA    . ASP   A  1  518  ? -43.231 32.660  88.358  1.00 27.89 ? 516  ASP   A CA    1 
ATOM   3806  C  C     . ASP   A  1  518  ? -42.887 33.599  89.504  1.00 27.78 ? 516  ASP   A C     1 
ATOM   3807  O  O     . ASP   A  1  518  ? -42.744 33.153  90.647  1.00 31.27 ? 516  ASP   A O     1 
ATOM   3808  C  CB    . ASP   A  1  518  ? -44.409 31.776  88.746  1.00 30.35 ? 516  ASP   A CB    1 
ATOM   3809  C  CG    . ASP   A  1  518  ? -45.657 32.568  89.035  1.00 32.53 ? 516  ASP   A CG    1 
ATOM   3810  O  OD1   . ASP   A  1  518  ? -45.642 33.810  88.888  1.00 30.38 ? 516  ASP   A OD1   1 
ATOM   3811  O  OD2   . ASP   A  1  518  ? -46.660 31.938  89.413  1.00 38.65 ? 516  ASP   A OD2   1 
ATOM   3812  N  N     . PRO   A  1  519  ? -42.753 34.902  89.251  1.00 27.33 ? 517  PRO   A N     1 
ATOM   3813  C  CA    . PRO   A  1  519  ? -42.358 35.801  90.343  1.00 26.11 ? 517  PRO   A CA    1 
ATOM   3814  C  C     . PRO   A  1  519  ? -43.362 35.838  91.481  1.00 25.36 ? 517  PRO   A C     1 
ATOM   3815  O  O     . PRO   A  1  519  ? -42.965 36.072  92.628  1.00 26.14 ? 517  PRO   A O     1 
ATOM   3816  C  CB    . PRO   A  1  519  ? -42.213 37.166  89.649  1.00 27.01 ? 517  PRO   A CB    1 
ATOM   3817  C  CG    . PRO   A  1  519  ? -43.033 37.056  88.419  1.00 32.51 ? 517  PRO   A CG    1 
ATOM   3818  C  CD    . PRO   A  1  519  ? -42.964 35.620  87.985  1.00 25.73 ? 517  PRO   A CD    1 
ATOM   3819  N  N     . VAL   A  1  520  ? -44.645 35.616  91.194  1.00 28.95 ? 518  VAL   A N     1 
ATOM   3820  C  CA    . VAL   A  1  520  ? -45.664 35.655  92.239  1.00 24.75 ? 518  VAL   A CA    1 
ATOM   3821  C  C     . VAL   A  1  520  ? -45.417 34.550  93.253  1.00 32.21 ? 518  VAL   A C     1 
ATOM   3822  O  O     . VAL   A  1  520  ? -45.382 34.788  94.464  1.00 29.47 ? 518  VAL   A O     1 
ATOM   3823  C  CB    . VAL   A  1  520  ? -47.069 35.554  91.626  1.00 27.55 ? 518  VAL   A CB    1 
ATOM   3824  C  CG1   . VAL   A  1  520  ? -48.127 35.640  92.722  1.00 28.81 ? 518  VAL   A CG1   1 
ATOM   3825  C  CG2   . VAL   A  1  520  ? -47.268 36.654  90.592  1.00 28.27 ? 518  VAL   A CG2   1 
ATOM   3826  N  N     . GLU   A  1  521  ? -45.218 33.327  92.764  1.00 28.74 ? 519  GLU   A N     1 
ATOM   3827  C  CA    . GLU   A  1  521  ? -44.974 32.207  93.666  1.00 31.71 ? 519  GLU   A CA    1 
ATOM   3828  C  C     . GLU   A  1  521  ? -43.611 32.304  94.335  1.00 33.38 ? 519  GLU   A C     1 
ATOM   3829  O  O     . GLU   A  1  521  ? -43.459 31.879  95.486  1.00 34.40 ? 519  GLU   A O     1 
ATOM   3830  C  CB    . GLU   A  1  521  ? -45.142 30.887  92.919  1.00 35.09 ? 519  GLU   A CB    1 
ATOM   3831  C  CG    . GLU   A  1  521  ? -46.572 30.645  92.474  1.00 36.47 ? 519  GLU   A CG    1 
ATOM   3832  C  CD    . GLU   A  1  521  ? -47.557 30.763  93.623  1.00 41.03 ? 519  GLU   A CD    1 
ATOM   3833  O  OE1   . GLU   A  1  521  ? -47.251 30.263  94.728  1.00 46.23 ? 519  GLU   A OE1   1 
ATOM   3834  O  OE2   . GLU   A  1  521  ? -48.639 31.359  93.427  1.00 44.39 ? 519  GLU   A OE2   1 
ATOM   3835  N  N     . VAL   A  1  522  ? -42.612 32.861  93.647  1.00 28.96 ? 520  VAL   A N     1 
ATOM   3836  C  CA    . VAL   A  1  522  ? -41.301 33.021  94.266  1.00 27.62 ? 520  VAL   A CA    1 
ATOM   3837  C  C     . VAL   A  1  522  ? -41.374 34.009  95.423  1.00 36.96 ? 520  VAL   A C     1 
ATOM   3838  O  O     . VAL   A  1  522  ? -40.847 33.755  96.513  1.00 34.10 ? 520  VAL   A O     1 
ATOM   3839  C  CB    . VAL   A  1  522  ? -40.235 33.418  93.230  1.00 35.00 ? 520  VAL   A CB    1 
ATOM   3840  C  CG1   . VAL   A  1  522  ? -38.911 33.699  93.928  1.00 33.36 ? 520  VAL   A CG1   1 
ATOM   3841  C  CG2   . VAL   A  1  522  ? -40.073 32.324  92.178  1.00 35.52 ? 520  VAL   A CG2   1 
ATOM   3842  N  N     . VAL   A  1  523  ? -42.041 35.146  95.208  1.00 27.31 ? 521  VAL   A N     1 
ATOM   3843  C  CA    . VAL   A  1  523  ? -42.183 36.127  96.278  1.00 29.82 ? 521  VAL   A CA    1 
ATOM   3844  C  C     . VAL   A  1  523  ? -43.021 35.556  97.413  1.00 29.17 ? 521  VAL   A C     1 
ATOM   3845  O  O     . VAL   A  1  523  ? -42.709 35.754  98.592  1.00 30.52 ? 521  VAL   A O     1 
ATOM   3846  C  CB    . VAL   A  1  523  ? -42.762 37.444  95.729  1.00 24.68 ? 521  VAL   A CB    1 
ATOM   3847  C  CG1   . VAL   A  1  523  ? -43.190 38.349  96.870  1.00 30.31 ? 521  VAL   A CG1   1 
ATOM   3848  C  CG2   . VAL   A  1  523  ? -41.731 38.145  94.863  1.00 27.60 ? 521  VAL   A CG2   1 
ATOM   3849  N  N     . ARG   A  1  524  ? -44.094 34.837  97.070  1.00 28.94 ? 522  ARG   A N     1 
ATOM   3850  C  CA    . ARG   A  1  524  ? -44.971 34.262  98.087  1.00 31.02 ? 522  ARG   A CA    1 
ATOM   3851  C  C     . ARG   A  1  524  ? -44.200 33.377  99.061  1.00 37.57 ? 522  ARG   A C     1 
ATOM   3852  O  O     . ARG   A  1  524  ? -44.512 33.344  100.257 1.00 38.58 ? 522  ARG   A O     1 
ATOM   3853  C  CB    . ARG   A  1  524  ? -46.080 33.454  97.417  1.00 34.95 ? 522  ARG   A CB    1 
ATOM   3854  C  CG    . ARG   A  1  524  ? -47.005 32.762  98.406  1.00 35.79 ? 522  ARG   A CG    1 
ATOM   3855  C  CD    . ARG   A  1  524  ? -47.895 31.739  97.730  1.00 44.06 ? 522  ARG   A CD    1 
ATOM   3856  N  NE    . ARG   A  1  524  ? -48.516 32.254  96.517  1.00 41.98 ? 522  ARG   A NE    1 
ATOM   3857  C  CZ    . ARG   A  1  524  ? -49.558 33.074  96.497  1.00 34.57 ? 522  ARG   A CZ    1 
ATOM   3858  N  NH1   . ARG   A  1  524  ? -50.088 33.547  97.614  1.00 40.89 ? 522  ARG   A NH1   1 
ATOM   3859  N  NH2   . ARG   A  1  524  ? -50.081 33.429  95.327  1.00 40.30 ? 522  ARG   A NH2   1 
ATOM   3860  N  N     . ALA   A  1  525  ? -43.184 32.668  98.571  1.00 33.86 ? 523  ALA   A N     1 
ATOM   3861  C  CA    . ALA   A  1  525  ? -42.461 31.672  99.354  1.00 38.39 ? 523  ALA   A CA    1 
ATOM   3862  C  C     . ALA   A  1  525  ? -41.240 32.226  100.077 1.00 37.63 ? 523  ALA   A C     1 
ATOM   3863  O  O     . ALA   A  1  525  ? -40.603 31.484  100.835 1.00 41.50 ? 523  ALA   A O     1 
ATOM   3864  C  CB    . ALA   A  1  525  ? -42.038 30.505  98.455  1.00 37.59 ? 523  ALA   A CB    1 
ATOM   3865  N  N     . MET   A  1  526  ? -40.896 33.494  99.869  1.00 35.35 ? 524  MET   A N     1 
ATOM   3866  C  CA    A MET   A  1  526  ? -39.741 34.075  100.536 0.57 36.92 ? 524  MET   A CA    1 
ATOM   3867  C  CA    B MET   A  1  526  ? -39.737 34.061  100.536 0.43 36.93 ? 524  MET   A CA    1 
ATOM   3868  C  C     . MET   A  1  526  ? -39.970 34.119  102.046 1.00 38.72 ? 524  MET   A C     1 
ATOM   3869  O  O     . MET   A  1  526  ? -41.111 34.232  102.504 1.00 36.33 ? 524  MET   A O     1 
ATOM   3870  C  CB    A MET   A  1  526  ? -39.495 35.492  100.016 0.57 40.19 ? 524  MET   A CB    1 
ATOM   3871  C  CB    B MET   A  1  526  ? -39.450 35.460  99.993  0.43 40.17 ? 524  MET   A CB    1 
ATOM   3872  C  CG    A MET   A  1  526  ? -38.954 35.552  98.596  0.57 38.86 ? 524  MET   A CG    1 
ATOM   3873  C  CG    B MET   A  1  526  ? -38.345 35.495  98.942  0.43 38.28 ? 524  MET   A CG    1 
ATOM   3874  S  SD    A MET   A  1  526  ? -37.356 34.734  98.438  0.57 44.53 ? 524  MET   A SD    1 
ATOM   3875  S  SD    B MET   A  1  526  ? -38.481 36.878  97.793  0.43 37.00 ? 524  MET   A SD    1 
ATOM   3876  C  CE    A MET   A  1  526  ? -36.328 35.771  99.479  0.57 38.46 ? 524  MET   A CE    1 
ATOM   3877  C  CE    B MET   A  1  526  ? -36.840 36.882  97.073  0.43 37.08 ? 524  MET   A CE    1 
ATOM   3878  N  N     . PRO   A  1  527  ? -38.900 34.029  102.847 1.00 40.78 ? 525  PRO   A N     1 
ATOM   3879  C  CA    . PRO   A  1  527  ? -39.096 34.035  104.310 1.00 41.30 ? 525  PRO   A CA    1 
ATOM   3880  C  C     . PRO   A  1  527  ? -39.758 35.301  104.821 1.00 41.83 ? 525  PRO   A C     1 
ATOM   3881  O  O     . PRO   A  1  527  ? -40.674 35.235  105.654 1.00 38.30 ? 525  PRO   A O     1 
ATOM   3882  C  CB    . PRO   A  1  527  ? -37.672 33.839  104.858 1.00 43.18 ? 525  PRO   A CB    1 
ATOM   3883  C  CG    . PRO   A  1  527  ? -36.777 34.298  103.760 1.00 44.36 ? 525  PRO   A CG    1 
ATOM   3884  C  CD    . PRO   A  1  527  ? -37.477 33.914  102.486 1.00 41.03 ? 525  PRO   A CD    1 
ATOM   3885  N  N     . VAL   A  1  528  ? -39.327 36.459  104.331 1.00 40.86 ? 526  VAL   A N     1 
ATOM   3886  C  CA    . VAL   A  1  528  ? -39.991 37.728  104.592 1.00 34.04 ? 526  VAL   A CA    1 
ATOM   3887  C  C     . VAL   A  1  528  ? -40.480 38.246  103.251 1.00 33.40 ? 526  VAL   A C     1 
ATOM   3888  O  O     . VAL   A  1  528  ? -39.670 38.586  102.378 1.00 37.11 ? 526  VAL   A O     1 
ATOM   3889  C  CB    . VAL   A  1  528  ? -39.055 38.740  105.259 1.00 35.37 ? 526  VAL   A CB    1 
ATOM   3890  C  CG1   . VAL   A  1  528  ? -39.776 40.059  105.452 1.00 39.29 ? 526  VAL   A CG1   1 
ATOM   3891  C  CG2   . VAL   A  1  528  ? -38.565 38.196  106.588 1.00 39.38 ? 526  VAL   A CG2   1 
ATOM   3892  N  N     . VAL   A  1  529  ? -41.797 38.307  103.080 1.00 31.21 ? 527  VAL   A N     1 
ATOM   3893  C  CA    . VAL   A  1  529  ? -42.365 38.761  101.816 1.00 30.96 ? 527  VAL   A CA    1 
ATOM   3894  C  C     . VAL   A  1  529  ? -42.103 40.253  101.654 1.00 33.52 ? 527  VAL   A C     1 
ATOM   3895  O  O     . VAL   A  1  529  ? -42.471 41.064  102.512 1.00 32.69 ? 527  VAL   A O     1 
ATOM   3896  C  CB    . VAL   A  1  529  ? -43.862 38.439  101.741 1.00 30.45 ? 527  VAL   A CB    1 
ATOM   3897  C  CG1   . VAL   A  1  529  ? -44.473 39.110  100.526 1.00 29.57 ? 527  VAL   A CG1   1 
ATOM   3898  C  CG2   . VAL   A  1  529  ? -44.077 36.928  101.685 1.00 34.80 ? 527  VAL   A CG2   1 
ATOM   3899  N  N     . GLY   A  1  530  ? -41.453 40.620  100.552 1.00 28.65 ? 528  GLY   A N     1 
ATOM   3900  C  CA    . GLY   A  1  530  ? -41.249 42.020  100.241 1.00 30.08 ? 528  GLY   A CA    1 
ATOM   3901  C  C     . GLY   A  1  530  ? -40.082 42.696  100.917 1.00 26.94 ? 528  GLY   A C     1 
ATOM   3902  O  O     . GLY   A  1  530  ? -40.060 43.926  100.985 1.00 28.64 ? 528  GLY   A O     1 
ATOM   3903  N  N     . ALA   A  1  531  ? -39.103 41.942  101.420 1.00 28.13 ? 529  ALA   A N     1 
ATOM   3904  C  CA    . ALA   A  1  531  ? -37.947 42.570  102.048 1.00 26.41 ? 529  ALA   A CA    1 
ATOM   3905  C  C     . ALA   A  1  531  ? -37.168 43.422  101.048 1.00 24.71 ? 529  ALA   A C     1 
ATOM   3906  O  O     . ALA   A  1  531  ? -37.027 43.060  99.875  1.00 28.79 ? 529  ALA   A O     1 
ATOM   3907  C  CB    . ALA   A  1  531  ? -37.017 41.505  102.637 1.00 27.95 ? 529  ALA   A CB    1 
ATOM   3908  N  N     . LYS   A  1  532  ? -36.667 44.563  101.529 1.00 24.27 ? 530  LYS   A N     1 
ATOM   3909  C  CA    . LYS   A  1  532  ? -35.775 45.426  100.760 1.00 24.29 ? 530  LYS   A CA    1 
ATOM   3910  C  C     . LYS   A  1  532  ? -34.583 44.626  100.250 1.00 26.20 ? 530  LYS   A C     1 
ATOM   3911  O  O     . LYS   A  1  532  ? -34.163 43.637  100.859 1.00 25.61 ? 530  LYS   A O     1 
ATOM   3912  C  CB    . LYS   A  1  532  ? -35.265 46.551  101.676 1.00 29.63 ? 530  LYS   A CB    1 
ATOM   3913  C  CG    . LYS   A  1  532  ? -34.275 47.520  101.029 1.00 34.69 ? 530  LYS   A CG    1 
ATOM   3914  C  CD    . LYS   A  1  532  ? -33.762 48.571  101.999 1.00 27.43 ? 530  LYS   A CD    1 
ATOM   3915  C  CE    . LYS   A  1  532  ? -32.957 47.951  103.135 1.00 30.77 ? 530  LYS   A CE    1 
ATOM   3916  N  NZ    . LYS   A  1  532  ? -31.657 47.380  102.663 1.00 27.19 ? 530  LYS   A NZ    1 
ATOM   3917  N  N     . HIS   A  1  533  ? -34.036 45.050  99.114  1.00 24.35 ? 531  HIS   A N     1 
ATOM   3918  C  CA    . HIS   A  1  533  ? -32.803 44.456  98.630  1.00 23.98 ? 531  HIS   A CA    1 
ATOM   3919  C  C     . HIS   A  1  533  ? -31.703 44.631  99.668  1.00 27.96 ? 531  HIS   A C     1 
ATOM   3920  O  O     . HIS   A  1  533  ? -31.536 45.709  100.249 1.00 25.97 ? 531  HIS   A O     1 
ATOM   3921  C  CB    . HIS   A  1  533  ? -32.392 45.130  97.324  1.00 24.25 ? 531  HIS   A CB    1 
ATOM   3922  C  CG    . HIS   A  1  533  ? -31.406 44.341  96.530  1.00 25.78 ? 531  HIS   A CG    1 
ATOM   3923  N  ND1   . HIS   A  1  533  ? -30.116 44.111  96.965  1.00 24.52 ? 531  HIS   A ND1   1 
ATOM   3924  C  CD2   . HIS   A  1  533  ? -31.520 43.713  95.335  1.00 28.33 ? 531  HIS   A CD2   1 
ATOM   3925  C  CE1   . HIS   A  1  533  ? -29.475 43.386  96.065  1.00 32.60 ? 531  HIS   A CE1   1 
ATOM   3926  N  NE2   . HIS   A  1  533  ? -30.304 43.129  95.068  1.00 34.60 ? 531  HIS   A NE2   1 
ATOM   3927  N  N     . ASP   A  1  534  ? -30.944 43.556  99.895  1.00 26.26 ? 532  ASP   A N     1 
ATOM   3928  C  CA    . ASP   A  1  534  ? -29.904 43.572  100.919 1.00 26.23 ? 532  ASP   A CA    1 
ATOM   3929  C  C     . ASP   A  1  534  ? -28.778 44.535  100.580 1.00 28.48 ? 532  ASP   A C     1 
ATOM   3930  O  O     . ASP   A  1  534  ? -28.096 45.035  101.484 1.00 31.52 ? 532  ASP   A O     1 
ATOM   3931  C  CB    . ASP   A  1  534  ? -29.322 42.169  101.064 1.00 28.92 ? 532  ASP   A CB    1 
ATOM   3932  C  CG    . ASP   A  1  534  ? -30.349 41.161  101.507 1.00 45.11 ? 532  ASP   A CG    1 
ATOM   3933  O  OD1   . ASP   A  1  534  ? -31.211 41.523  102.335 1.00 53.04 ? 532  ASP   A OD1   1 
ATOM   3934  O  OD2   . ASP   A  1  534  ? -30.297 40.009  101.025 1.00 58.86 ? 532  ASP   A OD2   1 
ATOM   3935  N  N     . ARG   A  1  535  ? -28.552 44.796  99.298  1.00 25.53 ? 533  ARG   A N     1 
ATOM   3936  C  CA    . ARG   A  1  535  ? -27.403 45.573  98.864  1.00 25.41 ? 533  ARG   A CA    1 
ATOM   3937  C  C     . ARG   A  1  535  ? -27.739 47.030  98.561  1.00 23.49 ? 533  ARG   A C     1 
ATOM   3938  O  O     . ARG   A  1  535  ? -26.884 47.760  98.048  1.00 27.33 ? 533  ARG   A O     1 
ATOM   3939  C  CB    . ARG   A  1  535  ? -26.736 44.914  97.653  1.00 31.61 ? 533  ARG   A CB    1 
ATOM   3940  N  N     . ILE   A  1  536  ? -28.946 47.478  98.885  1.00 24.46 ? 534  ILE   A N     1 
ATOM   3941  C  CA    . ILE   A  1  536  ? -29.328 48.871  98.697  1.00 24.42 ? 534  ILE   A CA    1 
ATOM   3942  C  C     . ILE   A  1  536  ? -29.628 49.463  100.062 1.00 22.92 ? 534  ILE   A C     1 
ATOM   3943  O  O     . ILE   A  1  536  ? -30.529 48.990  100.762 1.00 24.71 ? 534  ILE   A O     1 
ATOM   3944  C  CB    . ILE   A  1  536  ? -30.532 49.003  97.760  1.00 23.14 ? 534  ILE   A CB    1 
ATOM   3945  C  CG1   . ILE   A  1  536  ? -30.185 48.375  96.412  1.00 26.77 ? 534  ILE   A CG1   1 
ATOM   3946  C  CG2   . ILE   A  1  536  ? -30.936 50.464  97.633  1.00 25.08 ? 534  ILE   A CG2   1 
ATOM   3947  C  CD1   . ILE   A  1  536  ? -31.309 48.428  95.441  1.00 27.13 ? 534  ILE   A CD1   1 
ATOM   3948  N  N     . ALA   A  1  537  ? -28.878 50.489  100.438 1.00 22.02 ? 535  ALA   A N     1 
ATOM   3949  C  CA    . ALA   A  1  537  ? -29.063 51.112  101.736 1.00 21.20 ? 535  ALA   A CA    1 
ATOM   3950  C  C     . ALA   A  1  537  ? -30.253 52.058  101.693 1.00 22.43 ? 535  ALA   A C     1 
ATOM   3951  O  O     . ALA   A  1  537  ? -30.387 52.858  100.760 1.00 20.90 ? 535  ALA   A O     1 
ATOM   3952  C  CB    . ALA   A  1  537  ? -27.810 51.901  102.105 1.00 25.06 ? 535  ALA   A CB    1 
ATOM   3953  N  N     . LEU   A  1  538  ? -31.116 51.973  102.702 1.00 20.48 ? 536  LEU   A N     1 
ATOM   3954  C  CA    . LEU   A  1  538  ? -32.051 53.053  102.930 1.00 20.79 ? 536  LEU   A CA    1 
ATOM   3955  C  C     . LEU   A  1  538  ? -31.257 54.340  103.146 1.00 23.66 ? 536  LEU   A C     1 
ATOM   3956  O  O     . LEU   A  1  538  ? -30.115 54.306  103.618 1.00 22.04 ? 536  LEU   A O     1 
ATOM   3957  C  CB    . LEU   A  1  538  ? -32.907 52.767  104.163 1.00 22.61 ? 536  LEU   A CB    1 
ATOM   3958  C  CG    . LEU   A  1  538  ? -33.942 51.651  104.038 1.00 23.85 ? 536  LEU   A CG    1 
ATOM   3959  C  CD1   . LEU   A  1  538  ? -34.565 51.405  105.398 1.00 29.05 ? 536  LEU   A CD1   1 
ATOM   3960  C  CD2   . LEU   A  1  538  ? -35.011 52.021  103.028 1.00 25.32 ? 536  LEU   A CD2   1 
ATOM   3961  N  N     . PRO   A  1  539  ? -31.818 55.482  102.782 1.00 19.91 ? 537  PRO   A N     1 
ATOM   3962  C  CA    . PRO   A  1  539  ? -31.076 56.738  102.950 1.00 20.63 ? 537  PRO   A CA    1 
ATOM   3963  C  C     . PRO   A  1  539  ? -30.556 56.949  104.362 1.00 21.59 ? 537  PRO   A C     1 
ATOM   3964  O  O     . PRO   A  1  539  ? -29.418 57.403  104.525 1.00 20.88 ? 537  PRO   A O     1 
ATOM   3965  C  CB    . PRO   A  1  539  ? -32.084 57.797  102.493 1.00 19.71 ? 537  PRO   A CB    1 
ATOM   3966  C  CG    . PRO   A  1  539  ? -32.930 57.051  101.489 1.00 20.62 ? 537  PRO   A CG    1 
ATOM   3967  C  CD    . PRO   A  1  539  ? -33.083 55.676  102.052 1.00 19.05 ? 537  PRO   A CD    1 
ATOM   3968  N  N     . ALA   A  1  540  ? -31.327 56.575  105.384 1.00 21.27 ? 538  ALA   A N     1 
ATOM   3969  C  CA    . ALA   A  1  540  ? -30.860 56.759  106.753 1.00 22.86 ? 538  ALA   A CA    1 
ATOM   3970  C  C     . ALA   A  1  540  ? -29.621 55.929  107.063 1.00 25.61 ? 538  ALA   A C     1 
ATOM   3971  O  O     . ALA   A  1  540  ? -28.911 56.232  108.031 1.00 25.13 ? 538  ALA   A O     1 
ATOM   3972  C  CB    . ALA   A  1  540  ? -31.964 56.398  107.744 1.00 23.99 ? 538  ALA   A CB    1 
ATOM   3973  N  N     . GLU   A  1  541  ? -29.341 54.892  106.272 1.00 23.18 ? 539  GLU   A N     1 
ATOM   3974  C  CA    . GLU   A  1  541  ? -28.288 53.934  106.589 1.00 23.07 ? 539  GLU   A CA    1 
ATOM   3975  C  C     . GLU   A  1  541  ? -27.069 54.076  105.686 1.00 23.79 ? 539  GLU   A C     1 
ATOM   3976  O  O     . GLU   A  1  541  ? -26.223 53.173  105.644 1.00 23.80 ? 539  GLU   A O     1 
ATOM   3977  C  CB    . GLU   A  1  541  ? -28.849 52.510  106.572 1.00 28.14 ? 539  GLU   A CB    1 
ATOM   3978  C  CG    . GLU   A  1  541  ? -30.055 52.367  107.488 1.00 32.08 ? 539  GLU   A CG    1 
ATOM   3979  C  CD    . GLU   A  1  541  ? -30.524 50.939  107.639 1.00 42.30 ? 539  GLU   A CD    1 
ATOM   3980  O  OE1   . GLU   A  1  541  ? -29.667 50.040  107.768 1.00 53.86 ? 539  GLU   A OE1   1 
ATOM   3981  O  OE2   . GLU   A  1  541  ? -31.753 50.717  107.627 1.00 49.59 ? 539  GLU   A OE2   1 
ATOM   3982  N  N     . LEU   A  1  542  ? -26.953 55.202  104.973 1.00 22.48 ? 540  LEU   A N     1 
ATOM   3983  C  CA    . LEU   A  1  542  ? -25.842 55.396  104.048 1.00 23.22 ? 540  LEU   A CA    1 
ATOM   3984  C  C     . LEU   A  1  542  ? -24.487 55.200  104.705 1.00 22.84 ? 540  LEU   A C     1 
ATOM   3985  O  O     . LEU   A  1  542  ? -23.531 54.774  104.049 1.00 25.15 ? 540  LEU   A O     1 
ATOM   3986  C  CB    . LEU   A  1  542  ? -25.871 56.808  103.479 1.00 26.15 ? 540  LEU   A CB    1 
ATOM   3987  C  CG    . LEU   A  1  542  ? -26.746 57.075  102.267 1.00 31.13 ? 540  LEU   A CG    1 
ATOM   3988  C  CD1   . LEU   A  1  542  ? -26.282 58.383  101.664 1.00 26.19 ? 540  LEU   A CD1   1 
ATOM   3989  C  CD2   . LEU   A  1  542  ? -26.684 55.935  101.253 1.00 27.35 ? 540  LEU   A CD2   1 
ATOM   3990  N  N     . PHE   A  1  543  ? -24.369 55.531  105.986 1.00 22.45 ? 541  PHE   A N     1 
ATOM   3991  C  CA    . PHE   A  1  543  ? -23.088 55.441  106.663 1.00 24.15 ? 541  PHE   A CA    1 
ATOM   3992  C  C     . PHE   A  1  543  ? -23.000 54.233  107.579 1.00 23.44 ? 541  PHE   A C     1 
ATOM   3993  O  O     . PHE   A  1  543  ? -22.026 54.103  108.329 1.00 23.93 ? 541  PHE   A O     1 
ATOM   3994  C  CB    . PHE   A  1  543  ? -22.797 56.745  107.401 1.00 22.52 ? 541  PHE   A CB    1 
ATOM   3995  C  CG    . PHE   A  1  543  ? -23.035 57.953  106.556 1.00 21.63 ? 541  PHE   A CG    1 
ATOM   3996  C  CD1   . PHE   A  1  543  ? -22.341 58.110  105.366 1.00 25.94 ? 541  PHE   A CD1   1 
ATOM   3997  C  CD2   . PHE   A  1  543  ? -23.973 58.910  106.912 1.00 20.71 ? 541  PHE   A CD2   1 
ATOM   3998  C  CE1   . PHE   A  1  543  ? -22.559 59.197  104.560 1.00 23.71 ? 541  PHE   A CE1   1 
ATOM   3999  C  CE2   . PHE   A  1  543  ? -24.192 60.010  106.105 1.00 21.86 ? 541  PHE   A CE2   1 
ATOM   4000  C  CZ    . PHE   A  1  543  ? -23.488 60.158  104.929 1.00 23.56 ? 541  PHE   A CZ    1 
ATOM   4001  N  N     . GLY   A  1  544  ? -23.994 53.352  107.535 1.00 22.58 ? 542  GLY   A N     1 
ATOM   4002  C  CA    . GLY   A  1  544  ? -23.920 52.115  108.291 1.00 28.27 ? 542  GLY   A CA    1 
ATOM   4003  C  C     . GLY   A  1  544  ? -23.769 52.377  109.775 1.00 27.08 ? 542  GLY   A C     1 
ATOM   4004  O  O     . GLY   A  1  544  ? -24.430 53.247  110.351 1.00 26.39 ? 542  GLY   A O     1 
ATOM   4005  N  N     . ASP   A  1  545  ? -22.863 51.626  110.400 1.00 28.59 ? 543  ASP   A N     1 
ATOM   4006  C  CA    . ASP   A  1  545  ? -22.678 51.697  111.846 1.00 31.21 ? 543  ASP   A CA    1 
ATOM   4007  C  C     . ASP   A  1  545  ? -22.005 52.983  112.309 1.00 31.86 ? 543  ASP   A C     1 
ATOM   4008  O  O     . ASP   A  1  545  ? -22.027 53.264  113.514 1.00 33.67 ? 543  ASP   A O     1 
ATOM   4009  C  CB    . ASP   A  1  545  ? -21.850 50.502  112.327 1.00 34.84 ? 543  ASP   A CB    1 
ATOM   4010  C  CG    . ASP   A  1  545  ? -22.556 49.180  112.115 1.00 45.58 ? 543  ASP   A CG    1 
ATOM   4011  O  OD1   . ASP   A  1  545  ? -23.750 49.199  111.751 1.00 45.45 ? 543  ASP   A OD1   1 
ATOM   4012  O  OD2   . ASP   A  1  545  ? -21.916 48.123  112.314 1.00 54.74 ? 543  ASP   A OD2   1 
ATOM   4013  N  N     . ALA   A  1  546  ? -21.409 53.761  111.403 1.00 26.83 ? 544  ALA   A N     1 
ATOM   4014  C  CA    . ALA   A  1  546  ? -20.674 54.950  111.828 1.00 28.25 ? 544  ALA   A CA    1 
ATOM   4015  C  C     . ALA   A  1  546  ? -21.604 55.996  112.422 1.00 29.51 ? 544  ALA   A C     1 
ATOM   4016  O  O     . ALA   A  1  546  ? -21.296 56.593  113.458 1.00 29.68 ? 544  ALA   A O     1 
ATOM   4017  C  CB    . ALA   A  1  546  ? -19.882 55.541  110.668 1.00 26.81 ? 544  ALA   A CB    1 
ATOM   4018  N  N     . ARG   A  1  547  ? -22.743 56.238  111.782 1.00 24.39 ? 545  ARG   A N     1 
ATOM   4019  C  CA    . ARG   A  1  547  ? -23.685 57.225  112.281 1.00 26.78 ? 545  ARG   A CA    1 
ATOM   4020  C  C     . ARG   A  1  547  ? -24.932 57.154  111.425 1.00 21.39 ? 545  ARG   A C     1 
ATOM   4021  O  O     . ARG   A  1  547  ? -24.936 56.576  110.335 1.00 23.10 ? 545  ARG   A O     1 
ATOM   4022  C  CB    . ARG   A  1  547  ? -23.134 58.650  112.266 1.00 29.07 ? 545  ARG   A CB    1 
ATOM   4023  C  CG    . ARG   A  1  547  ? -22.838 59.161  110.898 1.00 27.78 ? 545  ARG   A CG    1 
ATOM   4024  C  CD    . ARG   A  1  547  ? -22.217 60.535  110.951 1.00 26.24 ? 545  ARG   A CD    1 
ATOM   4025  N  NE    . ARG   A  1  547  ? -21.360 60.728  109.791 1.00 23.17 ? 545  ARG   A NE    1 
ATOM   4026  C  CZ    . ARG   A  1  547  ? -21.707 61.385  108.691 1.00 22.21 ? 545  ARG   A CZ    1 
ATOM   4027  N  NH1   . ARG   A  1  547  ? -22.864 62.018  108.597 1.00 22.25 ? 545  ARG   A NH1   1 
ATOM   4028  N  NH2   . ARG   A  1  547  ? -20.866 61.414  107.664 1.00 23.22 ? 545  ARG   A NH2   1 
ATOM   4029  N  N     . THR   A  1  548  ? -25.981 57.777  111.937 1.00 22.59 ? 546  THR   A N     1 
ATOM   4030  C  CA    . THR   A  1  548  ? -27.259 57.837  111.254 1.00 21.07 ? 546  THR   A CA    1 
ATOM   4031  C  C     . THR   A  1  548  ? -27.263 59.058  110.350 1.00 20.10 ? 546  THR   A C     1 
ATOM   4032  O  O     . THR   A  1  548  ? -26.971 60.174  110.793 1.00 20.93 ? 546  THR   A O     1 
ATOM   4033  C  CB    . THR   A  1  548  ? -28.369 57.948  112.290 1.00 24.45 ? 546  THR   A CB    1 
ATOM   4034  O  OG1   . THR   A  1  548  ? -28.271 56.838  113.195 1.00 29.93 ? 546  THR   A OG1   1 
ATOM   4035  C  CG2   . THR   A  1  548  ? -29.717 57.944  111.611 1.00 25.91 ? 546  THR   A CG2   1 
ATOM   4036  N  N     . ASN   A  1  549  ? -27.596 58.843  109.081 1.00 19.48 ? 547  ASN   A N     1 
ATOM   4037  C  CA    . ASN   A  1  549  ? -27.707 59.950  108.150 1.00 19.72 ? 547  ASN   A CA    1 
ATOM   4038  C  C     . ASN   A  1  549  ? -28.847 60.862  108.586 1.00 20.59 ? 547  ASN   A C     1 
ATOM   4039  O  O     . ASN   A  1  549  ? -29.844 60.411  109.147 1.00 21.26 ? 547  ASN   A O     1 
ATOM   4040  C  CB    . ASN   A  1  549  ? -27.982 59.388  106.753 1.00 19.01 ? 547  ASN   A CB    1 
ATOM   4041  C  CG    . ASN   A  1  549  ? -27.822 60.412  105.666 1.00 19.29 ? 547  ASN   A CG    1 
ATOM   4042  O  OD1   . ASN   A  1  549  ? -27.302 61.500  105.880 1.00 19.58 ? 547  ASN   A OD1   1 
ATOM   4043  N  ND2   . ASN   A  1  549  ? -28.275 60.064  104.472 1.00 20.31 ? 547  ASN   A ND2   1 
ATOM   4044  N  N     . SER   A  1  550  ? -28.684 62.163  108.364 1.00 19.75 ? 548  SER   A N     1 
ATOM   4045  C  CA    . SER   A  1  550  ? -29.803 63.069  108.593 1.00 19.87 ? 548  SER   A CA    1 
ATOM   4046  C  C     . SER   A  1  550  ? -30.907 62.777  107.587 1.00 18.88 ? 548  SER   A C     1 
ATOM   4047  O  O     . SER   A  1  550  ? -30.657 62.273  106.489 1.00 20.82 ? 548  SER   A O     1 
ATOM   4048  C  CB    . SER   A  1  550  ? -29.359 64.515  108.434 1.00 19.25 ? 548  SER   A CB    1 
ATOM   4049  O  OG    . SER   A  1  550  ? -28.861 64.743  107.131 1.00 19.96 ? 548  SER   A OG    1 
ATOM   4050  N  N     . ALA   A  1  551  ? -32.137 63.091  107.978 1.00 20.09 ? 549  ALA   A N     1 
ATOM   4051  C  CA    . ALA   A  1  551  ? -33.305 62.882  107.138 1.00 22.41 ? 549  ALA   A CA    1 
ATOM   4052  C  C     . ALA   A  1  551  ? -33.783 64.212  106.587 1.00 21.29 ? 549  ALA   A C     1 
ATOM   4053  O  O     . ALA   A  1  551  ? -33.813 65.220  107.300 1.00 20.19 ? 549  ALA   A O     1 
ATOM   4054  C  CB    . ALA   A  1  551  ? -34.443 62.254  107.943 1.00 23.26 ? 549  ALA   A CB    1 
ATOM   4055  N  N     . GLY   A  1  552  ? -34.199 64.199  105.326 1.00 20.30 ? 550  GLY   A N     1 
ATOM   4056  C  CA    . GLY   A  1  552  ? -34.791 65.346  104.700 1.00 20.82 ? 550  GLY   A CA    1 
ATOM   4057  C  C     . GLY   A  1  552  ? -36.299 65.261  104.699 1.00 21.96 ? 550  GLY   A C     1 
ATOM   4058  O  O     . GLY   A  1  552  ? -36.912 64.541  105.494 1.00 23.27 ? 550  GLY   A O     1 
ATOM   4059  N  N     . LEU   A  1  553  ? -36.902 66.024  103.795 1.00 21.05 ? 551  LEU   A N     1 
ATOM   4060  C  CA    . LEU   A  1  553  ? -38.346 66.096  103.651 1.00 19.39 ? 551  LEU   A CA    1 
ATOM   4061  C  C     . LEU   A  1  553  ? -38.647 66.091  102.166 1.00 21.22 ? 551  LEU   A C     1 
ATOM   4062  O  O     . LEU   A  1  553  ? -37.905 66.682  101.383 1.00 22.24 ? 551  LEU   A O     1 
ATOM   4063  C  CB    . LEU   A  1  553  ? -38.881 67.391  104.246 1.00 23.72 ? 551  LEU   A CB    1 
ATOM   4064  C  CG    . LEU   A  1  553  ? -38.786 67.499  105.761 1.00 23.88 ? 551  LEU   A CG    1 
ATOM   4065  C  CD1   . LEU   A  1  553  ? -39.260 68.872  106.195 1.00 29.96 ? 551  LEU   A CD1   1 
ATOM   4066  C  CD2   . LEU   A  1  553  ? -39.602 66.399  106.439 1.00 27.34 ? 551  LEU   A CD2   1 
ATOM   4067  N  N     . ASP   A  1  554  ? -39.734 65.425  101.791 1.00 21.01 ? 552  ASP   A N     1 
ATOM   4068  C  CA    . ASP   A  1  554  ? -40.085 65.272  100.379 1.00 22.14 ? 552  ASP   A CA    1 
ATOM   4069  C  C     . ASP   A  1  554  ? -41.050 66.388  100.017 1.00 20.35 ? 552  ASP   A C     1 
ATOM   4070  O  O     . ASP   A  1  554  ? -42.245 66.314  100.323 1.00 18.97 ? 552  ASP   A O     1 
ATOM   4071  C  CB    . ASP   A  1  554  ? -40.730 63.913  100.132 1.00 20.73 ? 552  ASP   A CB    1 
ATOM   4072  C  CG    . ASP   A  1  554  ? -41.036 63.682  98.669  1.00 20.67 ? 552  ASP   A CG    1 
ATOM   4073  O  OD1   . ASP   A  1  554  ? -40.780 64.595  97.858  1.00 21.86 ? 552  ASP   A OD1   1 
ATOM   4074  O  OD2   . ASP   A  1  554  ? -41.501 62.581  98.332  1.00 23.14 ? 552  ASP   A OD2   1 
ATOM   4075  N  N     . LEU   A  1  555  ? -40.545 67.408  99.329  1.00 19.68 ? 553  LEU   A N     1 
ATOM   4076  C  CA    . LEU   A  1  555  ? -41.391 68.534  98.958  1.00 19.23 ? 553  LEU   A CA    1 
ATOM   4077  C  C     . LEU   A  1  555  ? -42.271 68.237  97.752  1.00 18.86 ? 553  LEU   A C     1 
ATOM   4078  O  O     . LEU   A  1  555  ? -42.958 69.142  97.272  1.00 21.44 ? 553  LEU   A O     1 
ATOM   4079  C  CB    . LEU   A  1  555  ? -40.556 69.802  98.767  1.00 19.16 ? 553  LEU   A CB    1 
ATOM   4080  C  CG    . LEU   A  1  555  ? -39.739 70.191  100.011 1.00 19.34 ? 553  LEU   A CG    1 
ATOM   4081  C  CD1   . LEU   A  1  555  ? -39.009 71.488  99.781  1.00 25.35 ? 553  LEU   A CD1   1 
ATOM   4082  C  CD2   . LEU   A  1  555  ? -40.664 70.312  101.208 1.00 24.38 ? 553  LEU   A CD2   1 
ATOM   4083  N  N     . SER   A  1  556  ? -42.280 67.000  97.267  1.00 18.35 ? 554  SER   A N     1 
ATOM   4084  C  CA    . SER   A  1  556  ? -43.275 66.573  96.290  1.00 18.93 ? 554  SER   A CA    1 
ATOM   4085  C  C     . SER   A  1  556  ? -44.423 65.800  96.925  1.00 21.05 ? 554  SER   A C     1 
ATOM   4086  O  O     . SER   A  1  556  ? -45.359 65.418  96.220  1.00 20.94 ? 554  SER   A O     1 
ATOM   4087  C  CB    . SER   A  1  556  ? -42.616 65.709  95.207  1.00 19.89 ? 554  SER   A CB    1 
ATOM   4088  O  OG    . SER   A  1  556  ? -42.362 64.391  95.685  1.00 22.32 ? 554  SER   A OG    1 
ATOM   4089  N  N     . ASN   A  1  557  ? -44.388 65.570  98.232  1.00 18.65 ? 555  ASN   A N     1 
ATOM   4090  C  CA    . ASN   A  1  557  ? -45.393 64.769  98.916  1.00 19.19 ? 555  ASN   A CA    1 
ATOM   4091  C  C     . ASN   A  1  557  ? -46.430 65.716  99.502  1.00 21.27 ? 555  ASN   A C     1 
ATOM   4092  O  O     . ASN   A  1  557  ? -46.091 66.571  100.327 1.00 19.21 ? 555  ASN   A O     1 
ATOM   4093  C  CB    . ASN   A  1  557  ? -44.688 63.956  100.005 1.00 19.60 ? 555  ASN   A CB    1 
ATOM   4094  C  CG    . ASN   A  1  557  ? -45.634 63.086  100.792 1.00 20.01 ? 555  ASN   A CG    1 
ATOM   4095  O  OD1   . ASN   A  1  557  ? -46.650 63.553  101.275 1.00 22.10 ? 555  ASN   A OD1   1 
ATOM   4096  N  ND2   . ASN   A  1  557  ? -45.306 61.810  100.914 1.00 22.93 ? 555  ASN   A ND2   1 
ATOM   4097  N  N     . GLU   A  1  558  ? -47.697 65.564  99.085  1.00 19.30 ? 556  GLU   A N     1 
ATOM   4098  C  CA    . GLU   A  1  558  ? -48.726 66.501  99.531  1.00 22.00 ? 556  GLU   A CA    1 
ATOM   4099  C  C     . GLU   A  1  558  ? -48.927 66.458  101.035 1.00 19.57 ? 556  GLU   A C     1 
ATOM   4100  O  O     . GLU   A  1  558  ? -49.248 67.487  101.642 1.00 21.61 ? 556  GLU   A O     1 
ATOM   4101  C  CB    . GLU   A  1  558  ? -50.066 66.258  98.832  1.00 21.36 ? 556  GLU   A CB    1 
ATOM   4102  C  CG    . GLU   A  1  558  ? -50.079 66.607  97.367  1.00 22.78 ? 556  GLU   A CG    1 
ATOM   4103  C  CD    . GLU   A  1  558  ? -49.810 68.080  97.028  1.00 19.64 ? 556  GLU   A CD    1 
ATOM   4104  O  OE1   . GLU   A  1  558  ? -49.840 68.985  97.886  1.00 21.48 ? 556  GLU   A OE1   1 
ATOM   4105  O  OE2   . GLU   A  1  558  ? -49.587 68.332  95.828  1.00 21.02 ? 556  GLU   A OE2   1 
ATOM   4106  N  N     . GLU   A  1  559  ? -48.794 65.277  101.652 1.00 20.05 ? 557  GLU   A N     1 
ATOM   4107  C  CA    . GLU   A  1  559  ? -48.904 65.203  103.107 1.00 21.72 ? 557  GLU   A CA    1 
ATOM   4108  C  C     . GLU   A  1  559  ? -47.791 66.011  103.752 1.00 21.32 ? 557  GLU   A C     1 
ATOM   4109  O  O     . GLU   A  1  559  ? -48.024 66.780  104.688 1.00 22.56 ? 557  GLU   A O     1 
ATOM   4110  C  CB    . GLU   A  1  559  ? -48.825 63.753  103.592 1.00 25.45 ? 557  GLU   A CB    1 
ATOM   4111  C  CG    . GLU   A  1  559  ? -49.958 62.830  103.172 1.00 26.41 ? 557  GLU   A CG    1 
ATOM   4112  C  CD    . GLU   A  1  559  ? -49.696 61.386  103.588 1.00 36.27 ? 557  GLU   A CD    1 
ATOM   4113  O  OE1   . GLU   A  1  559  ? -48.759 61.158  104.386 1.00 43.79 ? 557  GLU   A OE1   1 
ATOM   4114  O  OE2   . GLU   A  1  559  ? -50.411 60.476  103.119 1.00 33.80 ? 557  GLU   A OE2   1 
ATOM   4115  N  N     . THR   A  1  560  ? -46.570 65.863  103.238 1.00 20.61 ? 558  THR   A N     1 
ATOM   4116  C  CA    . THR   A  1  560  ? -45.453 66.626  103.780 1.00 21.72 ? 558  THR   A CA    1 
ATOM   4117  C  C     . THR   A  1  560  ? -45.665 68.115  103.578 1.00 19.85 ? 558  THR   A C     1 
ATOM   4118  O  O     . THR   A  1  560  ? -45.446 68.912  104.492 1.00 21.68 ? 558  THR   A O     1 
ATOM   4119  C  CB    . THR   A  1  560  ? -44.161 66.177  103.110 1.00 20.82 ? 558  THR   A CB    1 
ATOM   4120  O  OG1   . THR   A  1  560  ? -44.005 64.766  103.303 1.00 23.97 ? 558  THR   A OG1   1 
ATOM   4121  C  CG2   . THR   A  1  560  ? -42.959 66.931  103.690 1.00 23.02 ? 558  THR   A CG2   1 
ATOM   4122  N  N     . LEU   A  1  561  ? -46.129 68.513  102.392 1.00 19.13 ? 559  LEU   A N     1 
ATOM   4123  C  CA    . LEU   A  1  561  ? -46.346 69.931  102.148 1.00 18.34 ? 559  LEU   A CA    1 
ATOM   4124  C  C     . LEU   A  1  561  ? -47.426 70.489  103.062 1.00 21.69 ? 559  LEU   A C     1 
ATOM   4125  O  O     . LEU   A  1  561  ? -47.313 71.621  103.544 1.00 21.59 ? 559  LEU   A O     1 
ATOM   4126  C  CB    . LEU   A  1  561  ? -46.722 70.159  100.685 1.00 17.58 ? 559  LEU   A CB    1 
ATOM   4127  C  CG    . LEU   A  1  561  ? -45.571 69.887  99.721  1.00 17.60 ? 559  LEU   A CG    1 
ATOM   4128  C  CD1   . LEU   A  1  561  ? -46.094 70.053  98.309  1.00 19.45 ? 559  LEU   A CD1   1 
ATOM   4129  C  CD2   . LEU   A  1  561  ? -44.409 70.849  99.984  1.00 19.85 ? 559  LEU   A CD2   1 
ATOM   4130  N  N     . ALA   A  1  562  ? -48.489 69.715  103.300 1.00 21.61 ? 560  ALA   A N     1 
ATOM   4131  C  CA    . ALA   A  1  562  ? -49.557 70.209  104.163 1.00 21.48 ? 560  ALA   A CA    1 
ATOM   4132  C  C     . ALA   A  1  562  ? -49.084 70.331  105.604 1.00 22.34 ? 560  ALA   A C     1 
ATOM   4133  O  O     . ALA   A  1  562  ? -49.361 71.336  106.274 1.00 22.72 ? 560  ALA   A O     1 
ATOM   4134  C  CB    . ALA   A  1  562  ? -50.786 69.302  104.069 1.00 24.53 ? 560  ALA   A CB    1 
ATOM   4135  N  N     . SER   A  1  563  ? -48.360 69.327  106.094 1.00 22.47 ? 561  SER   A N     1 
ATOM   4136  C  CA    A SER   A  1  563  ? -47.841 69.386  107.455 0.44 23.34 ? 561  SER   A CA    1 
ATOM   4137  C  CA    B SER   A  1  563  ? -47.863 69.408  107.461 0.56 23.33 ? 561  SER   A CA    1 
ATOM   4138  C  C     . SER   A  1  563  ? -46.793 70.482  107.590 1.00 23.93 ? 561  SER   A C     1 
ATOM   4139  O  O     . SER   A  1  563  ? -46.766 71.214  108.583 1.00 25.76 ? 561  SER   A O     1 
ATOM   4140  C  CB    A SER   A  1  563  ? -47.254 68.026  107.829 0.44 25.26 ? 561  SER   A CB    1 
ATOM   4141  C  CB    B SER   A  1  563  ? -47.358 68.045  107.935 0.56 25.34 ? 561  SER   A CB    1 
ATOM   4142  O  OG    A SER   A  1  563  ? -46.703 68.050  109.128 0.44 24.80 ? 561  SER   A OG    1 
ATOM   4143  O  OG    B SER   A  1  563  ? -46.206 67.649  107.227 0.56 28.14 ? 561  SER   A OG    1 
ATOM   4144  N  N     . LEU   A  1  564  ? -45.927 70.614  106.589 1.00 23.27 ? 562  LEU   A N     1 
ATOM   4145  C  CA    . LEU   A  1  564  ? -44.913 71.658  106.629 1.00 23.06 ? 562  LEU   A CA    1 
ATOM   4146  C  C     . LEU   A  1  564  ? -45.546 73.042  106.594 1.00 23.67 ? 562  LEU   A C     1 
ATOM   4147  O  O     . LEU   A  1  564  ? -45.122 73.943  107.324 1.00 23.73 ? 562  LEU   A O     1 
ATOM   4148  C  CB    . LEU   A  1  564  ? -43.957 71.482  105.455 1.00 23.53 ? 562  LEU   A CB    1 
ATOM   4149  C  CG    . LEU   A  1  564  ? -42.648 72.250  105.461 1.00 27.84 ? 562  LEU   A CG    1 
ATOM   4150  C  CD1   . LEU   A  1  564  ? -41.876 71.931  106.732 1.00 26.49 ? 562  LEU   A CD1   1 
ATOM   4151  C  CD2   . LEU   A  1  564  ? -41.851 71.863  104.237 1.00 23.70 ? 562  LEU   A CD2   1 
ATOM   4152  N  N     . THR   A  1  565  ? -46.582 73.229  105.773 1.00 22.49 ? 563  THR   A N     1 
ATOM   4153  C  CA    . THR   A  1  565  ? -47.262 74.517  105.740 1.00 23.76 ? 563  THR   A CA    1 
ATOM   4154  C  C     . THR   A  1  565  ? -47.681 74.942  107.140 1.00 23.41 ? 563  THR   A C     1 
ATOM   4155  O  O     . THR   A  1  565  ? -47.464 76.088  107.549 1.00 25.62 ? 563  THR   A O     1 
ATOM   4156  C  CB    . THR   A  1  565  ? -48.483 74.447  104.829 1.00 23.32 ? 563  THR   A CB    1 
ATOM   4157  O  OG1   . THR   A  1  565  ? -48.062 74.203  103.476 1.00 23.64 ? 563  THR   A OG1   1 
ATOM   4158  C  CG2   . THR   A  1  565  ? -49.248 75.763  104.886 1.00 26.77 ? 563  THR   A CG2   1 
ATOM   4159  N  N     . GLU   A  1  566  ? -48.267 74.017  107.899 1.00 23.95 ? 564  GLU   A N     1 
ATOM   4160  C  CA    . GLU   A  1  566  ? -48.748 74.370  109.228 1.00 24.69 ? 564  GLU   A CA    1 
ATOM   4161  C  C     . GLU   A  1  566  ? -47.588 74.637  110.171 1.00 25.35 ? 564  GLU   A C     1 
ATOM   4162  O  O     . GLU   A  1  566  ? -47.613 75.611  110.931 1.00 24.46 ? 564  GLU   A O     1 
ATOM   4163  C  CB    . GLU   A  1  566  ? -49.659 73.268  109.763 1.00 28.30 ? 564  GLU   A CB    1 
ATOM   4164  C  CG    . GLU   A  1  566  ? -50.885 73.050  108.890 1.00 32.91 ? 564  GLU   A CG    1 
ATOM   4165  C  CD    . GLU   A  1  566  ? -51.690 74.330  108.670 1.00 40.12 ? 564  GLU   A CD    1 
ATOM   4166  O  OE1   . GLU   A  1  566  ? -51.942 75.058  109.657 1.00 44.25 ? 564  GLU   A OE1   1 
ATOM   4167  O  OE2   . GLU   A  1  566  ? -52.066 74.609  107.507 1.00 42.27 ? 564  GLU   A OE2   1 
ATOM   4168  N  N     . ALA   A  1  567  ? -46.557 73.795  110.122 1.00 24.68 ? 565  ALA   A N     1 
ATOM   4169  C  CA    . ALA   A  1  567  ? -45.402 74.005  110.986 1.00 25.69 ? 565  ALA   A CA    1 
ATOM   4170  C  C     . ALA   A  1  567  ? -44.691 75.309  110.643 1.00 22.08 ? 565  ALA   A C     1 
ATOM   4171  O  O     . ALA   A  1  567  ? -44.214 76.020  111.539 1.00 24.61 ? 565  ALA   A O     1 
ATOM   4172  C  CB    . ALA   A  1  567  ? -44.456 72.812  110.873 1.00 25.43 ? 565  ALA   A CB    1 
ATOM   4173  N  N     . LEU   A  1  568  ? -44.607 75.643  109.353 1.00 22.57 ? 566  LEU   A N     1 
ATOM   4174  C  CA    . LEU   A  1  568  ? -43.969 76.894  108.957 1.00 21.62 ? 566  LEU   A CA    1 
ATOM   4175  C  C     . LEU   A  1  568  ? -44.772 78.092  109.434 1.00 22.82 ? 566  LEU   A C     1 
ATOM   4176  O  O     . LEU   A  1  568  ? -44.214 79.039  109.996 1.00 24.85 ? 566  LEU   A O     1 
ATOM   4177  C  CB    . LEU   A  1  568  ? -43.793 76.948  107.438 1.00 21.81 ? 566  LEU   A CB    1 
ATOM   4178  C  CG    . LEU   A  1  568  ? -42.857 75.901  106.849 1.00 20.84 ? 566  LEU   A CG    1 
ATOM   4179  C  CD1   . LEU   A  1  568  ? -42.898 75.913  105.323 1.00 21.64 ? 566  LEU   A CD1   1 
ATOM   4180  C  CD2   . LEU   A  1  568  ? -41.437 76.108  107.356 1.00 24.56 ? 566  LEU   A CD2   1 
ATOM   4181  N  N     . ARG   A  1  569  ? -46.092 78.066  109.227 1.00 22.95 ? 567  ARG   A N     1 
ATOM   4182  C  CA    . ARG   A  1  569  ? -46.936 79.128  109.764 1.00 25.64 ? 567  ARG   A CA    1 
ATOM   4183  C  C     . ARG   A  1  569  ? -46.762 79.245  111.270 1.00 26.60 ? 567  ARG   A C     1 
ATOM   4184  O  O     . ARG   A  1  569  ? -46.620 80.351  111.808 1.00 27.88 ? 567  ARG   A O     1 
ATOM   4185  C  CB    . ARG   A  1  569  ? -48.397 78.860  109.413 1.00 26.33 ? 567  ARG   A CB    1 
ATOM   4186  C  CG    . ARG   A  1  569  ? -48.684 79.006  107.934 1.00 28.20 ? 567  ARG   A CG    1 
ATOM   4187  C  CD    . ARG   A  1  569  ? -50.146 78.668  107.623 1.00 34.00 ? 567  ARG   A CD    1 
ATOM   4188  N  NE    . ARG   A  1  569  ? -50.423 78.716  106.191 1.00 33.84 ? 567  ARG   A NE    1 
ATOM   4189  C  CZ    . ARG   A  1  569  ? -51.528 78.245  105.628 1.00 41.47 ? 567  ARG   A CZ    1 
ATOM   4190  N  NH1   . ARG   A  1  569  ? -52.473 77.658  106.346 1.00 46.95 ? 567  ARG   A NH1   1 
ATOM   4191  N  NH2   . ARG   A  1  569  ? -51.688 78.365  104.312 1.00 46.16 ? 567  ARG   A NH2   1 
ATOM   4192  N  N     . GLU   A  1  570  ? -46.759 78.107  111.967 1.00 23.77 ? 568  GLU   A N     1 
ATOM   4193  C  CA    . GLU   A  1  570  ? -46.598 78.136  113.417 1.00 25.42 ? 568  GLU   A CA    1 
ATOM   4194  C  C     . GLU   A  1  570  ? -45.250 78.723  113.807 1.00 28.84 ? 568  GLU   A C     1 
ATOM   4195  O  O     . GLU   A  1  570  ? -45.143 79.446  114.804 1.00 30.25 ? 568  GLU   A O     1 
ATOM   4196  C  CB    . GLU   A  1  570  ? -46.780 76.730  113.991 1.00 29.78 ? 568  GLU   A CB    1 
ATOM   4197  C  CG    . GLU   A  1  570  ? -48.242 76.274  114.013 1.00 30.85 ? 568  GLU   A CG    1 
ATOM   4198  C  CD    . GLU   A  1  570  ? -48.402 74.795  114.328 1.00 45.07 ? 568  GLU   A CD    1 
ATOM   4199  O  OE1   . GLU   A  1  570  ? -47.386 74.069  114.324 1.00 51.30 ? 568  GLU   A OE1   1 
ATOM   4200  O  OE2   . GLU   A  1  570  ? -49.547 74.355  114.578 1.00 54.84 ? 568  GLU   A OE2   1 
ATOM   4201  N  N     . SER   A  1  571  ? -44.210 78.441  113.023 1.00 26.36 ? 569  SER   A N     1 
ATOM   4202  C  CA    . SER   A  1  571  ? -42.899 78.992  113.342 1.00 28.78 ? 569  SER   A CA    1 
ATOM   4203  C  C     . SER   A  1  571  ? -42.884 80.508  113.203 1.00 28.10 ? 569  SER   A C     1 
ATOM   4204  O  O     . SER   A  1  571  ? -42.159 81.188  113.935 1.00 29.84 ? 569  SER   A O     1 
ATOM   4205  C  CB    . SER   A  1  571  ? -41.836 78.370  112.440 1.00 25.25 ? 569  SER   A CB    1 
ATOM   4206  O  OG    . SER   A  1  571  ? -41.837 78.987  111.162 1.00 25.88 ? 569  SER   A OG    1 
ATOM   4207  N  N     . ALA   A  1  572  ? -43.680 81.057  112.285 1.00 29.44 ? 570  ALA   A N     1 
ATOM   4208  C  CA    . ALA   A  1  572  ? -43.717 82.501  112.085 1.00 29.03 ? 570  ALA   A CA    1 
ATOM   4209  C  C     . ALA   A  1  572  ? -44.488 83.224  113.178 1.00 36.54 ? 570  ALA   A C     1 
ATOM   4210  O  O     . ALA   A  1  572  ? -44.415 84.453  113.256 1.00 37.58 ? 570  ALA   A O     1 
ATOM   4211  C  CB    . ALA   A  1  572  ? -44.302 82.843  110.712 1.00 33.74 ? 570  ALA   A CB    1 
ATOM   4212  N  N     . ALA   A  1  573  ? -45.215 82.494  114.015 1.00 30.62 ? 571  ALA   A N     1 
ATOM   4213  C  CA    . ALA   A  1  573  ? -45.915 83.062  115.157 1.00 37.56 ? 571  ALA   A CA    1 
ATOM   4214  C  C     . ALA   A  1  573  ? -45.091 82.997  116.437 1.00 43.02 ? 571  ALA   A C     1 
ATOM   4215  O  O     . ALA   A  1  573  ? -45.543 83.486  117.477 1.00 40.05 ? 571  ALA   A O     1 
ATOM   4216  C  CB    . ALA   A  1  573  ? -47.259 82.350  115.355 1.00 35.68 ? 571  ALA   A CB    1 
ATOM   4217  N  N     . MET   A  1  574  ? -43.897 82.412  116.388 1.00 35.61 ? 572  MET   A N     1 
ATOM   4218  C  CA    . MET   A  1  574  ? -43.056 82.312  117.570 1.00 35.66 ? 572  MET   A CA    1 
ATOM   4219  C  C     . MET   A  1  574  ? -42.308 83.619  117.804 1.00 37.68 ? 572  MET   A C     1 
ATOM   4220  O  O     . MET   A  1  574  ? -42.043 84.385  116.872 1.00 32.15 ? 572  MET   A O     1 
ATOM   4221  C  CB    . MET   A  1  574  ? -42.084 81.141  117.434 1.00 38.43 ? 572  MET   A CB    1 
ATOM   4222  C  CG    . MET   A  1  574  ? -42.775 79.779  117.525 1.00 39.41 ? 572  MET   A CG    1 
ATOM   4223  S  SD    . MET   A  1  574  ? -41.730 78.383  117.083 1.00 38.93 ? 572  MET   A SD    1 
ATOM   4224  C  CE    . MET   A  1  574  ? -42.872 77.013  117.277 1.00 49.50 ? 572  MET   A CE    1 
ATOM   4225  N  N     . LYS   A  1  575  ? -42.015 83.891  119.078 1.00 37.91 ? 573  LYS   A N     1 
ATOM   4226  C  CA    . LYS   A  1  575  ? -41.314 85.114  119.478 1.00 39.91 ? 573  LYS   A CA    1 
ATOM   4227  C  C     . LYS   A  1  575  ? -39.816 84.825  119.584 1.00 34.47 ? 573  LYS   A C     1 
ATOM   4228  O  O     . LYS   A  1  575  ? -39.232 84.716  120.665 1.00 35.90 ? 573  LYS   A O     1 
ATOM   4229  C  CB    . LYS   A  1  575  ? -41.886 85.663  120.780 1.00 40.87 ? 573  LYS   A CB    1 
ATOM   4230  N  N     . TRP   A  1  576  ? -39.204 84.694  118.411 1.00 29.83 ? 574  TRP   A N     1 
ATOM   4231  C  CA    . TRP   A  1  576  ? -37.794 84.346  118.313 1.00 27.06 ? 574  TRP   A CA    1 
ATOM   4232  C  C     . TRP   A  1  576  ? -36.939 85.463  118.889 1.00 26.39 ? 574  TRP   A C     1 
ATOM   4233  O  O     . TRP   A  1  576  ? -37.121 86.636  118.554 1.00 29.18 ? 574  TRP   A O     1 
ATOM   4234  C  CB    . TRP   A  1  576  ? -37.421 84.138  116.850 1.00 26.54 ? 574  TRP   A CB    1 
ATOM   4235  C  CG    . TRP   A  1  576  ? -38.114 82.983  116.203 1.00 25.04 ? 574  TRP   A CG    1 
ATOM   4236  C  CD1   . TRP   A  1  576  ? -39.105 83.040  115.254 1.00 25.84 ? 574  TRP   A CD1   1 
ATOM   4237  C  CD2   . TRP   A  1  576  ? -37.887 81.592  116.459 1.00 24.62 ? 574  TRP   A CD2   1 
ATOM   4238  N  NE1   . TRP   A  1  576  ? -39.491 81.773  114.901 1.00 27.62 ? 574  TRP   A NE1   1 
ATOM   4239  C  CE2   . TRP   A  1  576  ? -38.759 80.865  115.621 1.00 26.25 ? 574  TRP   A CE2   1 
ATOM   4240  C  CE3   . TRP   A  1  576  ? -37.025 80.888  117.310 1.00 25.53 ? 574  TRP   A CE3   1 
ATOM   4241  C  CZ2   . TRP   A  1  576  ? -38.794 79.471  115.605 1.00 25.45 ? 574  TRP   A CZ2   1 
ATOM   4242  C  CZ3   . TRP   A  1  576  ? -37.058 79.506  117.292 1.00 25.88 ? 574  TRP   A CZ3   1 
ATOM   4243  C  CH2   . TRP   A  1  576  ? -37.941 78.810  116.449 1.00 27.29 ? 574  TRP   A CH2   1 
ATOM   4244  N  N     . THR   A  1  577  ? -35.999 85.103  119.756 1.00 26.42 ? 575  THR   A N     1 
ATOM   4245  C  CA    . THR   A  1  577  ? -35.061 86.080  120.278 1.00 25.36 ? 575  THR   A CA    1 
ATOM   4246  C  C     . THR   A  1  577  ? -33.672 85.478  120.313 1.00 27.95 ? 575  THR   A C     1 
ATOM   4247  O  O     . THR   A  1  577  ? -33.495 84.258  120.292 1.00 28.72 ? 575  THR   A O     1 
ATOM   4248  C  CB    . THR   A  1  577  ? -35.407 86.554  121.702 1.00 29.23 ? 575  THR   A CB    1 
ATOM   4249  O  OG1   . THR   A  1  577  ? -35.290 85.450  122.606 1.00 31.92 ? 575  THR   A OG1   1 
ATOM   4250  C  CG2   . THR   A  1  577  ? -36.815 87.134  121.760 1.00 31.80 ? 575  THR   A CG2   1 
ATOM   4251  N  N     . ALA   A  1  578  ? -32.685 86.366  120.367 1.00 28.28 ? 576  ALA   A N     1 
ATOM   4252  C  CA    . ALA   A  1  578  ? -31.296 85.996  120.580 1.00 26.99 ? 576  ALA   A CA    1 
ATOM   4253  C  C     . ALA   A  1  578  ? -30.748 86.965  121.605 1.00 30.51 ? 576  ALA   A C     1 
ATOM   4254  O  O     . ALA   A  1  578  ? -30.866 88.181  121.428 1.00 28.99 ? 576  ALA   A O     1 
ATOM   4255  C  CB    . ALA   A  1  578  ? -30.485 86.125  119.289 1.00 25.83 ? 576  ALA   A CB    1 
ATOM   4256  N  N     . LEU   A  1  579  ? -30.169 86.429  122.668 1.00 28.15 ? 577  LEU   A N     1 
ATOM   4257  C  CA    . LEU   A  1  579  ? -29.673 87.214  123.784 1.00 30.33 ? 577  LEU   A CA    1 
ATOM   4258  C  C     . LEU   A  1  579  ? -28.235 86.825  124.057 1.00 31.89 ? 577  LEU   A C     1 
ATOM   4259  O  O     . LEU   A  1  579  ? -27.806 85.720  123.710 1.00 28.27 ? 577  LEU   A O     1 
ATOM   4260  C  CB    . LEU   A  1  579  ? -30.497 86.937  125.052 1.00 29.56 ? 577  LEU   A CB    1 
ATOM   4261  C  CG    . LEU   A  1  579  ? -32.015 87.043  124.934 1.00 34.05 ? 577  LEU   A CG    1 
ATOM   4262  C  CD1   . LEU   A  1  579  ? -32.644 86.767  126.288 1.00 35.11 ? 577  LEU   A CD1   1 
ATOM   4263  C  CD2   . LEU   A  1  579  ? -32.424 88.414  124.422 1.00 37.89 ? 577  LEU   A CD2   1 
ATOM   4264  N  N     . PRO   A  1  580  ? -27.459 87.711  124.686 1.00 29.83 ? 578  PRO   A N     1 
ATOM   4265  C  CA    . PRO   A  1  580  ? -26.145 87.303  125.187 1.00 26.19 ? 578  PRO   A CA    1 
ATOM   4266  C  C     . PRO   A  1  580  ? -26.334 86.316  126.322 1.00 33.63 ? 578  PRO   A C     1 
ATOM   4267  O  O     . PRO   A  1  580  ? -26.695 86.703  127.438 1.00 35.81 ? 578  PRO   A O     1 
ATOM   4268  C  CB    . PRO   A  1  580  ? -25.526 88.621  125.675 1.00 32.43 ? 578  PRO   A CB    1 
ATOM   4269  C  CG    . PRO   A  1  580  ? -26.425 89.719  125.130 1.00 30.99 ? 578  PRO   A CG    1 
ATOM   4270  C  CD    . PRO   A  1  580  ? -27.772 89.098  125.065 1.00 29.73 ? 578  PRO   A CD    1 
ATOM   4271  N  N     . GLN   A  1  581  ? -26.139 85.034  126.032 1.00 27.73 ? 579  GLN   A N     1 
ATOM   4272  C  CA    . GLN   A  1  581  ? -26.334 83.960  127.002 1.00 29.09 ? 579  GLN   A CA    1 
ATOM   4273  C  C     . GLN   A  1  581  ? -24.989 83.639  127.638 1.00 29.20 ? 579  GLN   A C     1 
ATOM   4274  O  O     . GLN   A  1  581  ? -24.263 82.735  127.223 1.00 31.13 ? 579  GLN   A O     1 
ATOM   4275  C  CB    . GLN   A  1  581  ? -26.928 82.735  126.322 1.00 28.36 ? 579  GLN   A CB    1 
ATOM   4276  C  CG    . GLN   A  1  581  ? -28.280 82.974  125.673 1.00 27.10 ? 579  GLN   A CG    1 
ATOM   4277  C  CD    . GLN   A  1  581  ? -29.376 83.126  126.700 1.00 30.03 ? 579  GLN   A CD    1 
ATOM   4278  O  OE1   . GLN   A  1  581  ? -29.140 82.959  127.899 1.00 30.44 ? 579  GLN   A OE1   1 
ATOM   4279  N  NE2   . GLN   A  1  581  ? -30.586 83.442  126.240 1.00 32.69 ? 579  GLN   A NE2   1 
ATOM   4280  N  N     . LEU   A  1  582  ? -24.662 84.413  128.668 1.00 30.21 ? 580  LEU   A N     1 
ATOM   4281  C  CA    . LEU   A  1  582  ? -23.457 84.197  129.441 1.00 30.89 ? 580  LEU   A CA    1 
ATOM   4282  C  C     . LEU   A  1  582  ? -23.643 83.000  130.371 1.00 32.60 ? 580  LEU   A C     1 
ATOM   4283  O  O     . LEU   A  1  582  ? -24.759 82.521  130.597 1.00 36.01 ? 580  LEU   A O     1 
ATOM   4284  C  CB    . LEU   A  1  582  ? -23.106 85.458  130.230 1.00 33.04 ? 580  LEU   A CB    1 
ATOM   4285  C  CG    . LEU   A  1  582  ? -22.237 86.498  129.508 1.00 40.38 ? 580  LEU   A CG    1 
ATOM   4286  C  CD1   . LEU   A  1  582  ? -22.856 86.963  128.208 1.00 39.02 ? 580  LEU   A CD1   1 
ATOM   4287  C  CD2   . LEU   A  1  582  ? -22.001 87.690  130.415 1.00 42.13 ? 580  LEU   A CD2   1 
ATOM   4288  N  N     . ALA   A  1  583  ? -22.530 82.507  130.914 1.00 31.03 ? 581  ALA   A N     1 
ATOM   4289  C  CA    . ALA   A  1  583  ? -22.610 81.387  131.841 1.00 34.44 ? 581  ALA   A CA    1 
ATOM   4290  C  C     . ALA   A  1  583  ? -23.486 81.730  133.033 1.00 35.36 ? 581  ALA   A C     1 
ATOM   4291  O  O     . ALA   A  1  583  ? -24.105 80.841  133.625 1.00 41.86 ? 581  ALA   A O     1 
ATOM   4292  C  CB    . ALA   A  1  583  ? -21.212 81.004  132.321 1.00 34.87 ? 581  ALA   A CB    1 
ATOM   4293  N  N     . THR   A  1  584  ? -23.557 83.013  133.383 1.00 34.75 ? 582  THR   A N     1 
ATOM   4294  C  CA    . THR   A  1  584  ? -24.330 83.497  134.518 1.00 37.30 ? 582  THR   A CA    1 
ATOM   4295  C  C     . THR   A  1  584  ? -25.783 83.766  134.169 1.00 40.60 ? 582  THR   A C     1 
ATOM   4296  O  O     . THR   A  1  584  ? -26.555 84.144  135.057 1.00 41.63 ? 582  THR   A O     1 
ATOM   4297  C  CB    . THR   A  1  584  ? -23.702 84.786  135.063 1.00 39.63 ? 582  THR   A CB    1 
ATOM   4298  O  OG1   . THR   A  1  584  ? -23.553 85.737  133.998 1.00 45.83 ? 582  THR   A OG1   1 
ATOM   4299  C  CG2   . THR   A  1  584  ? -22.342 84.505  135.686 1.00 38.83 ? 582  THR   A CG2   1 
ATOM   4300  N  N     . GLY   A  1  585  ? -26.173 83.594  132.909 1.00 37.86 ? 583  GLY   A N     1 
ATOM   4301  C  CA    . GLY   A  1  585  ? -27.526 83.871  132.486 1.00 38.87 ? 583  GLY   A CA    1 
ATOM   4302  C  C     . GLY   A  1  585  ? -27.568 84.936  131.409 1.00 38.70 ? 583  GLY   A C     1 
ATOM   4303  O  O     . GLY   A  1  585  ? -26.541 85.515  131.042 1.00 38.99 ? 583  GLY   A O     1 
ATOM   4304  N  N     . PRO   A  1  586  ? -28.760 85.220  130.885 1.00 35.59 ? 584  PRO   A N     1 
ATOM   4305  C  CA    . PRO   A  1  586  ? -28.879 86.249  129.846 1.00 36.12 ? 584  PRO   A CA    1 
ATOM   4306  C  C     . PRO   A  1  586  ? -28.413 87.601  130.361 1.00 41.68 ? 584  PRO   A C     1 
ATOM   4307  O  O     . PRO   A  1  586  ? -28.650 87.963  131.515 1.00 40.11 ? 584  PRO   A O     1 
ATOM   4308  C  CB    . PRO   A  1  586  ? -30.380 86.271  129.530 1.00 42.17 ? 584  PRO   A CB    1 
ATOM   4309  C  CG    . PRO   A  1  586  ? -30.960 85.056  130.194 1.00 46.35 ? 584  PRO   A CG    1 
ATOM   4310  C  CD    . PRO   A  1  586  ? -30.074 84.737  131.341 1.00 39.82 ? 584  PRO   A CD    1 
ATOM   4311  N  N     . ALA   A  1  587  ? -27.749 88.349  129.487 1.00 35.24 ? 585  ALA   A N     1 
ATOM   4312  C  CA    . ALA   A  1  587  ? -27.225 89.668  129.803 1.00 38.28 ? 585  ALA   A CA    1 
ATOM   4313  C  C     . ALA   A  1  587  ? -28.014 90.729  129.048 1.00 40.07 ? 585  ALA   A C     1 
ATOM   4314  O  O     . ALA   A  1  587  ? -28.580 90.466  127.985 1.00 38.73 ? 585  ALA   A O     1 
ATOM   4315  C  CB    . ALA   A  1  587  ? -25.742 89.770  129.432 1.00 40.30 ? 585  ALA   A CB    1 
ATOM   4316  N  N     . ALA   A  1  588  ? -28.065 91.930  129.612 1.00 38.58 ? 586  ALA   A N     1 
ATOM   4317  C  CA    . ALA   A  1  588  ? -28.732 93.025  128.934 1.00 34.52 ? 586  ALA   A CA    1 
ATOM   4318  C  C     . ALA   A  1  588  ? -27.826 93.597  127.848 1.00 37.21 ? 586  ALA   A C     1 
ATOM   4319  O  O     . ALA   A  1  588  ? -26.612 93.372  127.830 1.00 41.57 ? 586  ALA   A O     1 
ATOM   4320  C  CB    . ALA   A  1  588  ? -29.101 94.127  129.929 1.00 36.22 ? 586  ALA   A CB    1 
ATOM   4321  N  N     . GLY   A  1  589  ? -28.430 94.353  126.941 1.00 37.22 ? 587  GLY   A N     1 
ATOM   4322  C  CA    . GLY   A  1  589  ? -27.662 94.976  125.880 1.00 35.90 ? 587  GLY   A CA    1 
ATOM   4323  C  C     . GLY   A  1  589  ? -28.573 95.719  124.931 1.00 39.22 ? 587  GLY   A C     1 
ATOM   4324  O  O     . GLY   A  1  589  ? -29.776 95.855  125.173 1.00 42.25 ? 587  GLY   A O     1 
ATOM   4325  N  N     . GLU   A  1  590  ? -27.982 96.204  123.841 1.00 41.68 ? 588  GLU   A N     1 
ATOM   4326  C  CA    . GLU   A  1  590  ? -28.754 96.897  122.818 1.00 37.74 ? 588  GLU   A CA    1 
ATOM   4327  C  C     . GLU   A  1  590  ? -29.621 95.902  122.055 1.00 35.26 ? 588  GLU   A C     1 
ATOM   4328  O  O     . GLU   A  1  590  ? -29.120 94.920  121.494 1.00 34.49 ? 588  GLU   A O     1 
ATOM   4329  C  CB    . GLU   A  1  590  ? -27.820 97.621  121.850 1.00 42.71 ? 588  GLU   A CB    1 
ATOM   4330  N  N     . THR   A  1  591  ? -30.920 96.171  122.014 1.00 34.33 ? 589  THR   A N     1 
ATOM   4331  C  CA    . THR   A  1  591  ? -31.890 95.286  121.389 1.00 36.19 ? 589  THR   A CA    1 
ATOM   4332  C  C     . THR   A  1  591  ? -32.425 95.913  120.108 1.00 35.66 ? 589  THR   A C     1 
ATOM   4333  O  O     . THR   A  1  591  ? -32.710 97.113  120.063 1.00 37.33 ? 589  THR   A O     1 
ATOM   4334  C  CB    . THR   A  1  591  ? -33.040 95.016  122.362 1.00 36.50 ? 589  THR   A CB    1 
ATOM   4335  O  OG1   . THR   A  1  591  ? -32.533 94.362  123.535 1.00 39.17 ? 589  THR   A OG1   1 
ATOM   4336  C  CG2   . THR   A  1  591  ? -34.102 94.151  121.721 1.00 36.42 ? 589  THR   A CG2   1 
ATOM   4337  N  N     . ARG   A  1  592  ? -32.552 95.097  119.063 1.00 30.23 ? 590  ARG   A N     1 
ATOM   4338  C  CA    . ARG   A  1  592  ? -33.132 95.547  117.808 1.00 34.57 ? 590  ARG   A CA    1 
ATOM   4339  C  C     . ARG   A  1  592  ? -33.886 94.391  117.172 1.00 31.76 ? 590  ARG   A C     1 
ATOM   4340  O  O     . ARG   A  1  592  ? -33.690 93.226  117.528 1.00 31.94 ? 590  ARG   A O     1 
ATOM   4341  C  CB    . ARG   A  1  592  ? -32.071 96.075  116.835 1.00 35.18 ? 590  ARG   A CB    1 
ATOM   4342  C  CG    . ARG   A  1  592  ? -31.125 95.014  116.334 1.00 38.42 ? 590  ARG   A CG    1 
ATOM   4343  C  CD    . ARG   A  1  592  ? -30.364 95.476  115.099 1.00 38.51 ? 590  ARG   A CD    1 
ATOM   4344  N  NE    . ARG   A  1  592  ? -29.289 94.549  114.766 1.00 40.11 ? 590  ARG   A NE    1 
ATOM   4345  C  CZ    . ARG   A  1  592  ? -29.458 93.417  114.099 1.00 40.02 ? 590  ARG   A CZ    1 
ATOM   4346  N  NH1   . ARG   A  1  592  ? -30.649 93.048  113.653 1.00 38.01 ? 590  ARG   A NH1   1 
ATOM   4347  N  NH2   . ARG   A  1  592  ? -28.407 92.632  113.876 1.00 40.70 ? 590  ARG   A NH2   1 
ATOM   4348  N  N     . THR   A  1  593  ? -34.759 94.726  116.227 1.00 31.55 ? 591  THR   A N     1 
ATOM   4349  C  CA    . THR   A  1  593  ? -35.483 93.687  115.523 1.00 31.01 ? 591  THR   A CA    1 
ATOM   4350  C  C     . THR   A  1  593  ? -34.609 93.049  114.451 1.00 32.99 ? 591  THR   A C     1 
ATOM   4351  O  O     . THR   A  1  593  ? -33.626 93.624  113.974 1.00 33.06 ? 591  THR   A O     1 
ATOM   4352  C  CB    . THR   A  1  593  ? -36.729 94.259  114.861 1.00 34.52 ? 591  THR   A CB    1 
ATOM   4353  O  OG1   . THR   A  1  593  ? -36.339 95.320  113.981 1.00 34.78 ? 591  THR   A OG1   1 
ATOM   4354  C  CG2   . THR   A  1  593  ? -37.687 94.786  115.915 1.00 37.84 ? 591  THR   A CG2   1 
ATOM   4355  N  N     . VAL   A  1  594  ? -34.988 91.834  114.085 1.00 27.94 ? 592  VAL   A N     1 
ATOM   4356  C  CA    . VAL   A  1  594  ? -34.396 91.107  112.971 1.00 27.51 ? 592  VAL   A CA    1 
ATOM   4357  C  C     . VAL   A  1  594  ? -35.469 91.041  111.893 1.00 30.32 ? 592  VAL   A C     1 
ATOM   4358  O  O     . VAL   A  1  594  ? -36.573 90.545  112.147 1.00 29.39 ? 592  VAL   A O     1 
ATOM   4359  C  CB    . VAL   A  1  594  ? -33.956 89.701  113.400 1.00 27.19 ? 592  VAL   A CB    1 
ATOM   4360  C  CG1   . VAL   A  1  594  ? -33.412 88.929  112.212 1.00 28.59 ? 592  VAL   A CG1   1 
ATOM   4361  C  CG2   . VAL   A  1  594  ? -32.899 89.778  114.517 1.00 30.24 ? 592  VAL   A CG2   1 
ATOM   4362  N  N     . LEU   A  1  595  ? -35.163 91.557  110.704 1.00 27.87 ? 593  LEU   A N     1 
ATOM   4363  C  CA    . LEU   A  1  595  ? -36.146 91.665  109.634 1.00 28.35 ? 593  LEU   A CA    1 
ATOM   4364  C  C     . LEU   A  1  595  ? -35.869 90.639  108.540 1.00 27.05 ? 593  LEU   A C     1 
ATOM   4365  O  O     . LEU   A  1  595  ? -34.718 90.319  108.237 1.00 27.80 ? 593  LEU   A O     1 
ATOM   4366  C  CB    . LEU   A  1  595  ? -36.150 93.074  109.021 1.00 28.24 ? 593  LEU   A CB    1 
ATOM   4367  C  CG    . LEU   A  1  595  ? -36.286 94.276  109.956 1.00 30.23 ? 593  LEU   A CG    1 
ATOM   4368  C  CD1   . LEU   A  1  595  ? -36.304 95.579  109.172 1.00 34.12 ? 593  LEU   A CD1   1 
ATOM   4369  C  CD2   . LEU   A  1  595  ? -37.534 94.153  110.812 1.00 31.93 ? 593  LEU   A CD2   1 
ATOM   4370  N  N     . ASN   A  1  596  ? -36.944 90.135  107.947 1.00 25.75 ? 594  ASN   A N     1 
ATOM   4371  C  CA    . ASN   A  1  596  ? -36.846 89.222  106.817 1.00 24.62 ? 594  ASN   A CA    1 
ATOM   4372  C  C     . ASN   A  1  596  ? -36.178 89.940  105.649 1.00 23.40 ? 594  ASN   A C     1 
ATOM   4373  O  O     . ASN   A  1  596  ? -36.704 90.960  105.183 1.00 24.54 ? 594  ASN   A O     1 
ATOM   4374  C  CB    . ASN   A  1  596  ? -38.274 88.830  106.437 1.00 25.20 ? 594  ASN   A CB    1 
ATOM   4375  C  CG    . ASN   A  1  596  ? -38.335 87.724  105.392 1.00 25.75 ? 594  ASN   A CG    1 
ATOM   4376  O  OD1   . ASN   A  1  596  ? -37.479 87.619  104.523 1.00 24.93 ? 594  ASN   A OD1   1 
ATOM   4377  N  ND2   . ASN   A  1  596  ? -39.372 86.899  105.478 1.00 28.35 ? 594  ASN   A ND2   1 
ATOM   4378  N  N     . PRO   A  1  597  ? -35.053 89.440  105.129 1.00 22.55 ? 595  PRO   A N     1 
ATOM   4379  C  CA    . PRO   A  1  597  ? -34.388 90.136  104.016 1.00 22.25 ? 595  PRO   A CA    1 
ATOM   4380  C  C     . PRO   A  1  597  ? -35.245 90.213  102.772 1.00 25.34 ? 595  PRO   A C     1 
ATOM   4381  O  O     . PRO   A  1  597  ? -35.023 91.091  101.928 1.00 22.66 ? 595  PRO   A O     1 
ATOM   4382  C  CB    . PRO   A  1  597  ? -33.115 89.301  103.775 1.00 22.98 ? 595  PRO   A CB    1 
ATOM   4383  C  CG    . PRO   A  1  597  ? -33.423 87.963  104.340 1.00 24.18 ? 595  PRO   A CG    1 
ATOM   4384  C  CD    . PRO   A  1  597  ? -34.339 88.212  105.519 1.00 20.81 ? 595  PRO   A CD    1 
ATOM   4385  N  N     . GLY   A  1  598  ? -36.225 89.328  102.634 1.00 21.87 ? 596  GLY   A N     1 
ATOM   4386  C  CA    . GLY   A  1  598  ? -37.099 89.361  101.483 1.00 22.65 ? 596  GLY   A CA    1 
ATOM   4387  C  C     . GLY   A  1  598  ? -38.285 90.273  101.618 1.00 25.90 ? 596  GLY   A C     1 
ATOM   4388  O  O     . GLY   A  1  598  ? -39.010 90.465  100.644 1.00 25.49 ? 596  GLY   A O     1 
ATOM   4389  N  N     . ASP   A  1  599  ? -38.494 90.846  102.801 1.00 24.24 ? 597  ASP   A N     1 
ATOM   4390  C  CA    . ASP   A  1  599  ? -39.617 91.736  103.048 1.00 25.86 ? 597  ASP   A CA    1 
ATOM   4391  C  C     . ASP   A  1  599  ? -39.402 92.318  104.430 1.00 23.97 ? 597  ASP   A C     1 
ATOM   4392  O  O     . ASP   A  1  599  ? -39.709 91.669  105.438 1.00 26.38 ? 597  ASP   A O     1 
ATOM   4393  C  CB    . ASP   A  1  599  ? -40.930 90.963  103.015 1.00 27.00 ? 597  ASP   A CB    1 
ATOM   4394  C  CG    . ASP   A  1  599  ? -42.137 91.861  103.119 1.00 28.79 ? 597  ASP   A CG    1 
ATOM   4395  O  OD1   . ASP   A  1  599  ? -41.994 93.008  103.593 1.00 28.33 ? 597  ASP   A OD1   1 
ATOM   4396  O  OD2   . ASP   A  1  599  ? -43.227 91.405  102.725 1.00 32.69 ? 597  ASP   A OD2   1 
ATOM   4397  N  N     . HIS   A  1  600  ? -38.859 93.530  104.480 1.00 24.37 ? 598  HIS   A N     1 
ATOM   4398  C  CA    . HIS   A  1  600  ? -38.489 94.136  105.753 1.00 27.67 ? 598  HIS   A CA    1 
ATOM   4399  C  C     . HIS   A  1  600  ? -39.684 94.406  106.659 1.00 30.91 ? 598  HIS   A C     1 
ATOM   4400  O  O     . HIS   A  1  600  ? -39.483 94.659  107.851 1.00 31.94 ? 598  HIS   A O     1 
ATOM   4401  C  CB    . HIS   A  1  600  ? -37.680 95.410  105.515 1.00 30.77 ? 598  HIS   A CB    1 
ATOM   4402  C  CG    . HIS   A  1  600  ? -36.304 95.152  104.984 1.00 32.08 ? 598  HIS   A CG    1 
ATOM   4403  N  ND1   . HIS   A  1  600  ? -35.457 96.161  104.576 1.00 35.86 ? 598  HIS   A ND1   1 
ATOM   4404  C  CD2   . HIS   A  1  600  ? -35.626 93.993  104.795 1.00 30.51 ? 598  HIS   A CD2   1 
ATOM   4405  C  CE1   . HIS   A  1  600  ? -34.319 95.635  104.157 1.00 37.93 ? 598  HIS   A CE1   1 
ATOM   4406  N  NE2   . HIS   A  1  600  ? -34.394 94.322  104.284 1.00 34.09 ? 598  HIS   A NE2   1 
ATOM   4407  N  N     . ARG   A  1  601  ? -40.907 94.346  106.131 1.00 29.75 ? 599  ARG   A N     1 
ATOM   4408  C  CA    . ARG   A  1  601  ? -42.096 94.470  106.964 1.00 31.58 ? 599  ARG   A CA    1 
ATOM   4409  C  C     . ARG   A  1  601  ? -42.315 93.243  107.839 1.00 35.25 ? 599  ARG   A C     1 
ATOM   4410  O  O     . ARG   A  1  601  ? -43.057 93.328  108.823 1.00 32.45 ? 599  ARG   A O     1 
ATOM   4411  C  CB    . ARG   A  1  601  ? -43.323 94.685  106.080 1.00 31.61 ? 599  ARG   A CB    1 
ATOM   4412  C  CG    . ARG   A  1  601  ? -43.194 95.848  105.118 1.00 31.79 ? 599  ARG   A CG    1 
ATOM   4413  C  CD    . ARG   A  1  601  ? -44.308 95.823  104.087 1.00 33.36 ? 599  ARG   A CD    1 
ATOM   4414  N  NE    . ARG   A  1  601  ? -44.293 94.595  103.302 1.00 31.36 ? 599  ARG   A NE    1 
ATOM   4415  C  CZ    . ARG   A  1  601  ? -45.185 94.288  102.371 1.00 35.24 ? 599  ARG   A CZ    1 
ATOM   4416  N  NH1   . ARG   A  1  601  ? -46.188 95.103  102.075 1.00 35.15 ? 599  ARG   A NH1   1 
ATOM   4417  N  NH2   . ARG   A  1  601  ? -45.071 93.133  101.721 1.00 31.52 ? 599  ARG   A NH2   1 
ATOM   4418  N  N     . ASP   A  1  602  ? -41.688 92.115  107.503 1.00 29.22 ? 600  ASP   A N     1 
ATOM   4419  C  CA    . ASP   A  1  602  ? -41.837 90.866  108.248 1.00 30.26 ? 600  ASP   A CA    1 
ATOM   4420  C  C     . ASP   A  1  602  ? -40.766 90.836  109.330 1.00 31.35 ? 600  ASP   A C     1 
ATOM   4421  O  O     . ASP   A  1  602  ? -39.606 90.520  109.062 1.00 31.21 ? 600  ASP   A O     1 
ATOM   4422  C  CB    . ASP   A  1  602  ? -41.707 89.669  107.310 1.00 30.00 ? 600  ASP   A CB    1 
ATOM   4423  C  CG    . ASP   A  1  602  ? -41.904 88.342  108.022 1.00 31.20 ? 600  ASP   A CG    1 
ATOM   4424  O  OD1   . ASP   A  1  602  ? -42.500 88.337  109.119 1.00 31.99 ? 600  ASP   A OD1   1 
ATOM   4425  O  OD2   . ASP   A  1  602  ? -41.449 87.305  107.488 1.00 30.52 ? 600  ASP   A OD2   1 
ATOM   4426  N  N     . VAL   A  1  603  ? -41.153 91.173  110.556 1.00 29.90 ? 601  VAL   A N     1 
ATOM   4427  C  CA    . VAL   A  1  603  ? -40.245 91.118  111.693 1.00 30.14 ? 601  VAL   A CA    1 
ATOM   4428  C  C     . VAL   A  1  603  ? -40.160 89.669  112.150 1.00 30.95 ? 601  VAL   A C     1 
ATOM   4429  O  O     . VAL   A  1  603  ? -41.176 89.050  112.483 1.00 32.41 ? 601  VAL   A O     1 
ATOM   4430  C  CB    . VAL   A  1  603  ? -40.729 92.033  112.825 1.00 34.50 ? 601  VAL   A CB    1 
ATOM   4431  C  CG1   . VAL   A  1  603  ? -39.823 91.905  114.032 1.00 33.50 ? 601  VAL   A CG1   1 
ATOM   4432  C  CG2   . VAL   A  1  603  ? -40.775 93.469  112.347 1.00 33.48 ? 601  VAL   A CG2   1 
ATOM   4433  N  N     . VAL   A  1  604  ? -38.955 89.118  112.140 1.00 26.85 ? 602  VAL   A N     1 
ATOM   4434  C  CA    . VAL   A  1  604  ? -38.775 87.713  112.477 1.00 28.33 ? 602  VAL   A CA    1 
ATOM   4435  C  C     . VAL   A  1  604  ? -38.528 87.538  113.962 1.00 27.26 ? 602  VAL   A C     1 
ATOM   4436  O  O     . VAL   A  1  604  ? -38.973 86.562  114.568 1.00 28.83 ? 602  VAL   A O     1 
ATOM   4437  C  CB    . VAL   A  1  604  ? -37.629 87.120  111.634 1.00 25.85 ? 602  VAL   A CB    1 
ATOM   4438  C  CG1   . VAL   A  1  604  ? -37.474 85.640  111.925 1.00 24.24 ? 602  VAL   A CG1   1 
ATOM   4439  C  CG2   . VAL   A  1  604  ? -37.892 87.352  110.153 1.00 26.62 ? 602  VAL   A CG2   1 
ATOM   4440  N  N     . GLY   A  1  605  ? -37.824 88.480  114.564 1.00 26.40 ? 603  GLY   A N     1 
ATOM   4441  C  CA    . GLY   A  1  605  ? -37.563 88.384  115.982 1.00 27.04 ? 603  GLY   A CA    1 
ATOM   4442  C  C     . GLY   A  1  605  ? -36.776 89.571  116.463 1.00 27.64 ? 603  GLY   A C     1 
ATOM   4443  O  O     . GLY   A  1  605  ? -36.741 90.621  115.820 1.00 29.81 ? 603  GLY   A O     1 
ATOM   4444  N  N     . SER   A  1  606  ? -36.131 89.382  117.606 1.00 27.03 ? 604  SER   A N     1 
ATOM   4445  C  CA    A SER   A  1  606  ? -35.377 90.446  118.236 0.59 27.79 ? 604  SER   A CA    1 
ATOM   4446  C  CA    B SER   A  1  606  ? -35.397 90.442  118.271 0.41 27.84 ? 604  SER   A CA    1 
ATOM   4447  C  C     . SER   A  1  606  ? -34.064 89.896  118.750 1.00 29.85 ? 604  SER   A C     1 
ATOM   4448  O  O     . SER   A  1  606  ? -33.999 88.780  119.277 1.00 30.32 ? 604  SER   A O     1 
ATOM   4449  C  CB    A SER   A  1  606  ? -36.159 91.069  119.391 0.59 29.33 ? 604  SER   A CB    1 
ATOM   4450  C  CB    B SER   A  1  606  ? -36.197 90.952  119.473 0.41 29.25 ? 604  SER   A CB    1 
ATOM   4451  O  OG    A SER   A  1  606  ? -37.294 91.755  118.899 0.59 30.69 ? 604  SER   A OG    1 
ATOM   4452  O  OG    B SER   A  1  606  ? -35.446 91.870  120.238 0.41 29.01 ? 604  SER   A OG    1 
ATOM   4453  N  N     . VAL   A  1  607  ? -33.009 90.677  118.570 1.00 27.80 ? 605  VAL   A N     1 
ATOM   4454  C  CA    . VAL   A  1  607  ? -31.685 90.301  119.038 1.00 27.21 ? 605  VAL   A CA    1 
ATOM   4455  C  C     . VAL   A  1  607  ? -31.220 91.352  120.024 1.00 29.47 ? 605  VAL   A C     1 
ATOM   4456  O  O     . VAL   A  1  607  ? -31.354 92.553  119.769 1.00 28.92 ? 605  VAL   A O     1 
ATOM   4457  C  CB    . VAL   A  1  607  ? -30.676 90.128  117.886 1.00 27.63 ? 605  VAL   A CB    1 
ATOM   4458  C  CG1   . VAL   A  1  607  ? -30.595 91.375  117.021 1.00 29.57 ? 605  VAL   A CG1   1 
ATOM   4459  C  CG2   . VAL   A  1  607  ? -29.299 89.786  118.445 1.00 27.28 ? 605  VAL   A CG2   1 
ATOM   4460  N  N     . THR   A  1  608  ? -30.702 90.895  121.154 1.00 29.96 ? 606  THR   A N     1 
ATOM   4461  C  CA    . THR   A  1  608  ? -29.993 91.740  122.097 1.00 32.71 ? 606  THR   A CA    1 
ATOM   4462  C  C     . THR   A  1  608  ? -28.512 91.461  121.903 1.00 30.16 ? 606  THR   A C     1 
ATOM   4463  O  O     . THR   A  1  608  ? -28.065 90.321  122.064 1.00 29.01 ? 606  THR   A O     1 
ATOM   4464  C  CB    . THR   A  1  608  ? -30.428 91.395  123.516 1.00 30.80 ? 606  THR   A CB    1 
ATOM   4465  O  OG1   . THR   A  1  608  ? -31.837 91.632  123.639 1.00 31.99 ? 606  THR   A OG1   1 
ATOM   4466  C  CG2   . THR   A  1  608  ? -29.678 92.250  124.522 1.00 35.57 ? 606  THR   A CG2   1 
ATOM   4467  N  N     . GLU   A  1  609  ? -27.762 92.489  121.535 1.00 30.03 ? 607  GLU   A N     1 
ATOM   4468  C  CA    . GLU   A  1  609  ? -26.361 92.296  121.208 1.00 33.58 ? 607  GLU   A CA    1 
ATOM   4469  C  C     . GLU   A  1  609  ? -25.462 92.463  122.434 1.00 30.69 ? 607  GLU   A C     1 
ATOM   4470  O  O     . GLU   A  1  609  ? -25.824 93.086  123.436 1.00 29.57 ? 607  GLU   A O     1 
ATOM   4471  C  CB    . GLU   A  1  609  ? -25.965 93.183  120.021 1.00 35.90 ? 607  GLU   A CB    1 
ATOM   4472  C  CG    . GLU   A  1  609  ? -26.680 92.706  118.740 1.00 35.86 ? 607  GLU   A CG    1 
ATOM   4473  C  CD    . GLU   A  1  609  ? -26.362 93.521  117.496 1.00 43.23 ? 607  GLU   A CD    1 
ATOM   4474  O  OE1   . GLU   A  1  609  ? -26.219 94.757  117.609 1.00 48.13 ? 607  GLU   A OE1   1 
ATOM   4475  O  OE2   . GLU   A  1  609  ? -26.272 92.915  116.397 1.00 40.05 ? 607  GLU   A OE2   1 
ATOM   4476  N  N     . THR   A  1  610  ? -24.289 91.853  122.350 1.00 30.58 ? 608  THR   A N     1 
ATOM   4477  C  CA    . THR   A  1  610  ? -23.379 91.728  123.477 1.00 30.24 ? 608  THR   A CA    1 
ATOM   4478  C  C     . THR   A  1  610  ? -22.485 92.955  123.542 1.00 36.27 ? 608  THR   A C     1 
ATOM   4479  O  O     . THR   A  1  610  ? -21.905 93.364  122.530 1.00 35.39 ? 608  THR   A O     1 
ATOM   4480  C  CB    . THR   A  1  610  ? -22.505 90.485  123.286 1.00 29.55 ? 608  THR   A CB    1 
ATOM   4481  O  OG1   . THR   A  1  610  ? -23.343 89.353  123.011 1.00 29.73 ? 608  THR   A OG1   1 
ATOM   4482  C  CG2   . THR   A  1  610  ? -21.655 90.213  124.528 1.00 32.10 ? 608  THR   A CG2   1 
ATOM   4483  N  N     . SER   A  1  611  ? -22.366 93.537  124.729 1.00 32.26 ? 609  SER   A N     1 
ATOM   4484  C  CA    . SER   A  1  611  ? -21.386 94.591  124.918 1.00 36.45 ? 609  SER   A CA    1 
ATOM   4485  C  C     . SER   A  1  611  ? -19.988 93.992  124.881 1.00 37.51 ? 609  SER   A C     1 
ATOM   4486  O  O     . SER   A  1  611  ? -19.788 92.807  125.166 1.00 32.96 ? 609  SER   A O     1 
ATOM   4487  C  CB    . SER   A  1  611  ? -21.601 95.269  126.267 1.00 37.42 ? 609  SER   A CB    1 
ATOM   4488  O  OG    . SER   A  1  611  ? -21.136 94.442  127.316 1.00 39.29 ? 609  SER   A OG    1 
ATOM   4489  N  N     . GLU   A  1  612  ? -19.011 94.818  124.510 1.00 36.74 ? 610  GLU   A N     1 
ATOM   4490  C  CA    . GLU   A  1  612  ? -17.640 94.327  124.475 1.00 37.36 ? 610  GLU   A CA    1 
ATOM   4491  C  C     . GLU   A  1  612  ? -17.146 93.959  125.866 1.00 36.61 ? 610  GLU   A C     1 
ATOM   4492  O  O     . GLU   A  1  612  ? -16.309 93.061  126.009 1.00 36.60 ? 610  GLU   A O     1 
ATOM   4493  C  CB    . GLU   A  1  612  ? -16.730 95.332  123.766 1.00 46.33 ? 610  GLU   A CB    1 
ATOM   4494  C  CG    . GLU   A  1  612  ? -16.861 95.252  122.242 1.00 44.81 ? 610  GLU   A CG    1 
ATOM   4495  C  CD    . GLU   A  1  612  ? -16.456 96.529  121.533 1.00 49.50 ? 610  GLU   A CD    1 
ATOM   4496  O  OE1   . GLU   A  1  612  ? -15.241 96.783  121.399 1.00 54.20 ? 610  GLU   A OE1   1 
ATOM   4497  O  OE2   . GLU   A  1  612  ? -17.359 97.278  121.106 1.00 55.42 ? 610  GLU   A OE2   1 
ATOM   4498  N  N     . GLU   A  1  613  ? -17.687 94.605  126.902 1.00 36.33 ? 611  GLU   A N     1 
ATOM   4499  C  CA    . GLU   A  1  613  ? -17.356 94.216  128.269 1.00 41.48 ? 611  GLU   A CA    1 
ATOM   4500  C  C     . GLU   A  1  613  ? -17.885 92.822  128.590 1.00 34.80 ? 611  GLU   A C     1 
ATOM   4501  O  O     . GLU   A  1  613  ? -17.173 92.006  129.185 1.00 33.95 ? 611  GLU   A O     1 
ATOM   4502  C  CB    . GLU   A  1  613  ? -17.897 95.250  129.258 1.00 42.57 ? 611  GLU   A CB    1 
ATOM   4503  N  N     . ASP   A  1  614  ? -19.130 92.526  128.200 1.00 34.99 ? 612  ASP   A N     1 
ATOM   4504  C  CA    . ASP   A  1  614  ? -19.690 91.208  128.483 1.00 28.59 ? 612  ASP   A CA    1 
ATOM   4505  C  C     . ASP   A  1  614  ? -19.026 90.125  127.639 1.00 29.75 ? 612  ASP   A C     1 
ATOM   4506  O  O     . ASP   A  1  614  ? -18.933 88.971  128.074 1.00 30.84 ? 612  ASP   A O     1 
ATOM   4507  C  CB    . ASP   A  1  614  ? -21.198 91.208  128.251 1.00 33.77 ? 612  ASP   A CB    1 
ATOM   4508  C  CG    . ASP   A  1  614  ? -21.951 91.996  129.314 1.00 34.17 ? 612  ASP   A CG    1 
ATOM   4509  O  OD1   . ASP   A  1  614  ? -21.474 92.039  130.466 1.00 37.65 ? 612  ASP   A OD1   1 
ATOM   4510  O  OD2   . ASP   A  1  614  ? -23.011 92.571  128.995 1.00 39.34 ? 612  ASP   A OD2   1 
ATOM   4511  N  N     . ALA   A  1  615  ? -18.551 90.476  126.445 1.00 29.57 ? 613  ALA   A N     1 
ATOM   4512  C  CA    . ALA   A  1  615  ? -17.801 89.513  125.648 1.00 30.54 ? 613  ALA   A CA    1 
ATOM   4513  C  C     . ALA   A  1  615  ? -16.526 89.104  126.368 1.00 28.62 ? 613  ALA   A C     1 
ATOM   4514  O  O     . ALA   A  1  615  ? -16.215 87.912  126.481 1.00 28.23 ? 613  ALA   A O     1 
ATOM   4515  C  CB    . ALA   A  1  615  ? -17.485 90.099  124.274 1.00 28.99 ? 613  ALA   A CB    1 
ATOM   4516  N  N     . ARG   A  1  616  ? -15.785 90.085  126.888 1.00 32.74 ? 614  ARG   A N     1 
ATOM   4517  C  CA    . ARG   A  1  616  ? -14.599 89.768  127.677 1.00 34.64 ? 614  ARG   A CA    1 
ATOM   4518  C  C     . ARG   A  1  616  ? -14.969 88.978  128.923 1.00 29.21 ? 614  ARG   A C     1 
ATOM   4519  O  O     . ARG   A  1  616  ? -14.278 88.020  129.287 1.00 31.10 ? 614  ARG   A O     1 
ATOM   4520  C  CB    . ARG   A  1  616  ? -13.856 91.052  128.049 1.00 36.00 ? 614  ARG   A CB    1 
ATOM   4521  C  CG    . ARG   A  1  616  ? -13.005 91.605  126.920 1.00 42.45 ? 614  ARG   A CG    1 
ATOM   4522  C  CD    . ARG   A  1  616  ? -12.372 92.942  127.286 1.00 48.82 ? 614  ARG   A CD    1 
ATOM   4523  N  NE    . ARG   A  1  616  ? -13.045 94.045  126.613 1.00 53.03 ? 614  ARG   A NE    1 
ATOM   4524  C  CZ    . ARG   A  1  616  ? -13.730 95.002  127.223 1.00 46.81 ? 614  ARG   A CZ    1 
ATOM   4525  N  NH1   . ARG   A  1  616  ? -13.825 95.057  128.544 1.00 52.01 ? 614  ARG   A NH1   1 
ATOM   4526  N  NH2   . ARG   A  1  616  ? -14.327 95.937  126.489 1.00 49.87 ? 614  ARG   A NH2   1 
ATOM   4527  N  N     . ARG   A  1  617  ? -16.074 89.347  129.577 1.00 27.82 ? 615  ARG   A N     1 
ATOM   4528  C  CA    . ARG   A  1  617  ? -16.507 88.593  130.746 1.00 30.67 ? 615  ARG   A CA    1 
ATOM   4529  C  C     . ARG   A  1  617  ? -16.830 87.150  130.376 1.00 31.14 ? 615  ARG   A C     1 
ATOM   4530  O  O     . ARG   A  1  617  ? -16.499 86.220  131.120 1.00 30.67 ? 615  ARG   A O     1 
ATOM   4531  C  CB    . ARG   A  1  617  ? -17.708 89.277  131.397 1.00 33.29 ? 615  ARG   A CB    1 
ATOM   4532  C  CG    . ARG   A  1  617  ? -18.167 88.620  132.674 1.00 41.00 ? 615  ARG   A CG    1 
ATOM   4533  C  CD    . ARG   A  1  617  ? -18.868 89.628  133.567 1.00 43.23 ? 615  ARG   A CD    1 
ATOM   4534  N  NE    . ARG   A  1  617  ? -20.081 90.162  132.961 1.00 48.16 ? 615  ARG   A NE    1 
ATOM   4535  C  CZ    . ARG   A  1  617  ? -21.290 89.649  133.141 1.00 51.02 ? 615  ARG   A CZ    1 
ATOM   4536  N  NH1   . ARG   A  1  617  ? -21.479 88.568  133.883 1.00 52.14 ? 615  ARG   A NH1   1 
ATOM   4537  N  NH2   . ARG   A  1  617  ? -22.338 90.240  132.571 1.00 46.42 ? 615  ARG   A NH2   1 
ATOM   4538  N  N     . ALA   A  1  618  ? -17.464 86.942  129.220 1.00 29.94 ? 616  ALA   A N     1 
ATOM   4539  C  CA    . ALA   A  1  618  ? -17.808 85.584  128.813 1.00 30.06 ? 616  ALA   A CA    1 
ATOM   4540  C  C     . ALA   A  1  618  ? -16.562 84.725  128.649 1.00 26.78 ? 616  ALA   A C     1 
ATOM   4541  O  O     . ALA   A  1  618  ? -16.549 83.550  129.038 1.00 27.73 ? 616  ALA   A O     1 
ATOM   4542  C  CB    . ALA   A  1  618  ? -18.621 85.616  127.518 1.00 30.22 ? 616  ALA   A CB    1 
ATOM   4543  N  N     . VAL   A  1  619  ? -15.495 85.297  128.093 1.00 26.69 ? 617  VAL   A N     1 
ATOM   4544  C  CA    . VAL   A  1  619  ? -14.269 84.524  127.926 1.00 27.48 ? 617  VAL   A CA    1 
ATOM   4545  C  C     . VAL   A  1  619  ? -13.699 84.134  129.280 1.00 28.06 ? 617  VAL   A C     1 
ATOM   4546  O  O     . VAL   A  1  619  ? -13.250 83.001  129.476 1.00 28.81 ? 617  VAL   A O     1 
ATOM   4547  C  CB    . VAL   A  1  619  ? -13.243 85.280  127.061 1.00 27.22 ? 617  VAL   A CB    1 
ATOM   4548  C  CG1   . VAL   A  1  619  ? -11.965 84.458  126.926 1.00 29.69 ? 617  VAL   A CG1   1 
ATOM   4549  C  CG2   . VAL   A  1  619  ? -13.812 85.567  125.689 1.00 27.30 ? 617  VAL   A CG2   1 
ATOM   4550  N  N     . ARG   A  1  620  ? -13.738 85.055  130.246 1.00 27.40 ? 618  ARG   A N     1 
ATOM   4551  C  CA    . ARG   A  1  620  ? -13.253 84.718  131.578 1.00 32.08 ? 618  ARG   A CA    1 
ATOM   4552  C  C     . ARG   A  1  620  ? -14.101 83.621  132.204 1.00 29.68 ? 618  ARG   A C     1 
ATOM   4553  O  O     . ARG   A  1  620  ? -13.566 82.698  132.830 1.00 31.27 ? 618  ARG   A O     1 
ATOM   4554  C  CB    . ARG   A  1  620  ? -13.207 85.964  132.461 1.00 33.58 ? 618  ARG   A CB    1 
ATOM   4555  C  CG    . ARG   A  1  620  ? -12.095 86.919  132.067 1.00 37.68 ? 618  ARG   A CG    1 
ATOM   4556  C  CD    . ARG   A  1  620  ? -11.974 88.096  133.024 1.00 44.91 ? 618  ARG   A CD    1 
ATOM   4557  N  NE    . ARG   A  1  620  ? -12.433 89.329  132.396 1.00 53.61 ? 618  ARG   A NE    1 
ATOM   4558  C  CZ    . ARG   A  1  620  ? -13.528 89.991  132.744 1.00 47.47 ? 618  ARG   A CZ    1 
ATOM   4559  N  NH1   . ARG   A  1  620  ? -14.276 89.606  133.767 1.00 51.67 ? 618  ARG   A NH1   1 
ATOM   4560  N  NH2   . ARG   A  1  620  ? -13.874 91.075  132.056 1.00 46.86 ? 618  ARG   A NH2   1 
ATOM   4561  N  N     . LEU   A  1  621  ? -15.422 83.683  132.016 1.00 27.80 ? 619  LEU   A N     1 
ATOM   4562  C  CA    . LEU   A  1  621  ? -16.282 82.627  132.542 1.00 30.54 ? 619  LEU   A CA    1 
ATOM   4563  C  C     . LEU   A  1  621  ? -15.987 81.298  131.858 1.00 28.61 ? 619  LEU   A C     1 
ATOM   4564  O  O     . LEU   A  1  621  ? -15.957 80.248  132.512 1.00 31.19 ? 619  LEU   A O     1 
ATOM   4565  C  CB    . LEU   A  1  621  ? -17.749 83.008  132.364 1.00 31.24 ? 619  LEU   A CB    1 
ATOM   4566  C  CG    . LEU   A  1  621  ? -18.260 84.219  133.150 1.00 31.24 ? 619  LEU   A CG    1 
ATOM   4567  C  CD1   . LEU   A  1  621  ? -19.602 84.694  132.607 1.00 32.37 ? 619  LEU   A CD1   1 
ATOM   4568  C  CD2   . LEU   A  1  621  ? -18.392 83.871  134.625 1.00 34.61 ? 619  LEU   A CD2   1 
ATOM   4569  N  N     . ALA   A  1  622  ? -15.763 81.326  130.541 1.00 28.94 ? 620  ALA   A N     1 
ATOM   4570  C  CA    . ALA   A  1  622  ? -15.380 80.115  129.826 1.00 29.02 ? 620  ALA   A CA    1 
ATOM   4571  C  C     . ALA   A  1  622  ? -14.074 79.549  130.365 1.00 26.73 ? 620  ALA   A C     1 
ATOM   4572  O  O     . ALA   A  1  622  ? -13.938 78.331  130.533 1.00 27.88 ? 620  ALA   A O     1 
ATOM   4573  C  CB    . ALA   A  1  622  ? -15.252 80.405  128.331 1.00 27.35 ? 620  ALA   A CB    1 
ATOM   4574  N  N     . ALA   A  1  623  ? -13.092 80.418  130.628 1.00 28.35 ? 621  ALA   A N     1 
ATOM   4575  C  CA    . ALA   A  1  623  ? -11.816 79.947  131.157 1.00 28.59 ? 621  ALA   A CA    1 
ATOM   4576  C  C     . ALA   A  1  623  ? -11.992 79.306  132.527 1.00 28.84 ? 621  ALA   A C     1 
ATOM   4577  O  O     . ALA   A  1  623  ? -11.397 78.263  132.812 1.00 30.00 ? 621  ALA   A O     1 
ATOM   4578  C  CB    . ALA   A  1  623  ? -10.814 81.098  131.221 1.00 33.45 ? 621  ALA   A CB    1 
ATOM   4579  N  N     . ASP   A  1  624  ? -12.831 79.900  133.374 1.00 29.63 ? 622  ASP   A N     1 
ATOM   4580  C  CA    . ASP   A  1  624  ? -13.074 79.325  134.696 1.00 34.30 ? 622  ASP   A CA    1 
ATOM   4581  C  C     . ASP   A  1  624  ? -13.779 77.981  134.580 1.00 36.03 ? 622  ASP   A C     1 
ATOM   4582  O  O     . ASP   A  1  624  ? -13.530 77.069  135.378 1.00 40.35 ? 622  ASP   A O     1 
ATOM   4583  C  CB    . ASP   A  1  624  ? -13.928 80.279  135.534 1.00 40.29 ? 622  ASP   A CB    1 
ATOM   4584  C  CG    . ASP   A  1  624  ? -13.224 81.590  135.837 1.00 47.93 ? 622  ASP   A CG    1 
ATOM   4585  O  OD1   . ASP   A  1  624  ? -11.976 81.638  135.766 1.00 51.12 ? 622  ASP   A OD1   1 
ATOM   4586  O  OD2   . ASP   A  1  624  ? -13.928 82.574  136.156 1.00 50.42 ? 622  ASP   A OD2   1 
ATOM   4587  N  N     . ALA   A  1  625  ? -14.653 77.845  133.586 1.00 35.88 ? 623  ALA   A N     1 
ATOM   4588  C  CA    . ALA   A  1  625  ? -15.444 76.644  133.370 1.00 39.04 ? 623  ALA   A CA    1 
ATOM   4589  C  C     . ALA   A  1  625  ? -14.712 75.584  132.571 1.00 38.04 ? 623  ALA   A C     1 
ATOM   4590  O  O     . ALA   A  1  625  ? -15.219 74.463  132.451 1.00 40.78 ? 623  ALA   A O     1 
ATOM   4591  C  CB    . ALA   A  1  625  ? -16.704 77.007  132.589 1.00 39.87 ? 623  ALA   A CB    1 
ATOM   4592  N  N     . ALA   A  1  626  ? -13.561 75.912  132.000 1.00 32.81 ? 624  ALA   A N     1 
ATOM   4593  C  CA    . ALA   A  1  626  ? -12.876 74.973  131.114 1.00 29.31 ? 624  ALA   A CA    1 
ATOM   4594  C  C     . ALA   A  1  626  ? -12.564 73.634  131.769 1.00 34.48 ? 624  ALA   A C     1 
ATOM   4595  O  O     . ALA   A  1  626  ? -12.817 72.596  131.140 1.00 33.70 ? 624  ALA   A O     1 
ATOM   4596  C  CB    . ALA   A  1  626  ? -11.651 75.647  130.483 1.00 31.96 ? 624  ALA   A CB    1 
ATOM   4597  N  N     . PRO   A  1  627  ? -12.037 73.567  132.999 1.00 33.76 ? 625  PRO   A N     1 
ATOM   4598  C  CA    . PRO   A  1  627  ? -11.748 72.241  133.571 1.00 32.37 ? 625  PRO   A CA    1 
ATOM   4599  C  C     . PRO   A  1  627  ? -12.981 71.367  133.730 1.00 31.91 ? 625  PRO   A C     1 
ATOM   4600  O  O     . PRO   A  1  627  ? -12.914 70.155  133.477 1.00 35.57 ? 625  PRO   A O     1 
ATOM   4601  C  CB    . PRO   A  1  627  ? -11.094 72.578  134.923 1.00 33.49 ? 625  PRO   A CB    1 
ATOM   4602  C  CG    . PRO   A  1  627  ? -10.553 73.965  134.739 1.00 36.34 ? 625  PRO   A CG    1 
ATOM   4603  C  CD    . PRO   A  1  627  ? -11.581 74.650  133.888 1.00 35.48 ? 625  PRO   A CD    1 
ATOM   4604  N  N     . ASP   A  1  628  ? -14.108 71.949  134.136 1.00 34.26 ? 626  ASP   A N     1 
ATOM   4605  C  CA    . ASP   A  1  628  ? -15.304 71.150  134.370 1.00 34.58 ? 626  ASP   A CA    1 
ATOM   4606  C  C     . ASP   A  1  628  ? -15.828 70.556  133.076 1.00 35.59 ? 626  ASP   A C     1 
ATOM   4607  O  O     . ASP   A  1  628  ? -16.436 69.480  133.085 1.00 35.74 ? 626  ASP   A O     1 
ATOM   4608  C  CB    . ASP   A  1  628  ? -16.398 72.006  135.008 1.00 33.71 ? 626  ASP   A CB    1 
ATOM   4609  C  CG    . ASP   A  1  628  ? -16.003 72.531  136.371 1.00 39.04 ? 626  ASP   A CG    1 
ATOM   4610  O  OD1   . ASP   A  1  628  ? -14.927 72.136  136.856 1.00 43.26 ? 626  ASP   A OD1   1 
ATOM   4611  O  OD2   . ASP   A  1  628  ? -16.761 73.339  136.942 1.00 49.53 ? 626  ASP   A OD2   1 
ATOM   4612  N  N     . TRP   A  1  629  ? -15.621 71.248  131.961 1.00 30.56 ? 627  TRP   A N     1 
ATOM   4613  C  CA    . TRP   A  1  629  ? -16.108 70.720  130.696 1.00 31.10 ? 627  TRP   A CA    1 
ATOM   4614  C  C     . TRP   A  1  629  ? -15.125 69.716  130.113 1.00 31.99 ? 627  TRP   A C     1 
ATOM   4615  O  O     . TRP   A  1  629  ? -15.537 68.690  129.559 1.00 29.26 ? 627  TRP   A O     1 
ATOM   4616  C  CB    . TRP   A  1  629  ? -16.387 71.859  129.717 1.00 28.50 ? 627  TRP   A CB    1 
ATOM   4617  C  CG    . TRP   A  1  629  ? -16.853 71.354  128.387 1.00 26.66 ? 627  TRP   A CG    1 
ATOM   4618  C  CD1   . TRP   A  1  629  ? -16.241 71.534  127.175 1.00 25.01 ? 627  TRP   A CD1   1 
ATOM   4619  C  CD2   . TRP   A  1  629  ? -18.003 70.537  128.139 1.00 24.37 ? 627  TRP   A CD2   1 
ATOM   4620  N  NE1   . TRP   A  1  629  ? -16.955 70.900  126.190 1.00 25.81 ? 627  TRP   A NE1   1 
ATOM   4621  C  CE2   . TRP   A  1  629  ? -18.042 70.284  126.753 1.00 24.86 ? 627  TRP   A CE2   1 
ATOM   4622  C  CE3   . TRP   A  1  629  ? -19.008 70.008  128.946 1.00 27.55 ? 627  TRP   A CE3   1 
ATOM   4623  C  CZ2   . TRP   A  1  629  ? -19.040 69.516  126.161 1.00 25.52 ? 627  TRP   A CZ2   1 
ATOM   4624  C  CZ3   . TRP   A  1  629  ? -20.003 69.246  128.349 1.00 28.24 ? 627  TRP   A CZ3   1 
ATOM   4625  C  CH2   . TRP   A  1  629  ? -20.009 69.007  126.972 1.00 27.26 ? 627  TRP   A CH2   1 
ATOM   4626  N  N     . ALA   A  1  630  ? -13.823 69.990  130.246 1.00 28.43 ? 628  ALA   A N     1 
ATOM   4627  C  CA    . ALA   A  1  630  ? -12.813 69.036  129.802 1.00 31.18 ? 628  ALA   A CA    1 
ATOM   4628  C  C     . ALA   A  1  630  ? -12.934 67.711  130.539 1.00 32.98 ? 628  ALA   A C     1 
ATOM   4629  O  O     . ALA   A  1  630  ? -12.563 66.662  129.997 1.00 32.24 ? 628  ALA   A O     1 
ATOM   4630  C  CB    . ALA   A  1  630  ? -11.415 69.621  130.004 1.00 31.60 ? 628  ALA   A CB    1 
ATOM   4631  N  N     . ALA   A  1  631  ? -13.445 67.738  131.770 1.00 31.38 ? 629  ALA   A N     1 
ATOM   4632  C  CA    . ALA   A  1  631  ? -13.586 66.528  132.568 1.00 31.33 ? 629  ALA   A CA    1 
ATOM   4633  C  C     . ALA   A  1  631  ? -14.795 65.688  132.184 1.00 32.29 ? 629  ALA   A C     1 
ATOM   4634  O  O     . ALA   A  1  631  ? -14.902 64.543  132.639 1.00 33.38 ? 629  ALA   A O     1 
ATOM   4635  C  CB    . ALA   A  1  631  ? -13.642 66.869  134.059 1.00 32.12 ? 629  ALA   A CB    1 
ATOM   4636  N  N     . VAL   A  1  632  ? -15.715 66.216  131.385 1.00 30.38 ? 630  VAL   A N     1 
ATOM   4637  C  CA    . VAL   A  1  632  ? -16.798 65.388  130.866 1.00 29.15 ? 630  VAL   A CA    1 
ATOM   4638  C  C     . VAL   A  1  632  ? -16.154 64.461  129.846 1.00 27.39 ? 630  VAL   A C     1 
ATOM   4639  O  O     . VAL   A  1  632  ? -15.520 64.951  128.906 1.00 29.84 ? 630  VAL   A O     1 
ATOM   4640  C  CB    . VAL   A  1  632  ? -17.911 66.245  130.246 1.00 29.34 ? 630  VAL   A CB    1 
ATOM   4641  C  CG1   . VAL   A  1  632  ? -19.009 65.365  129.653 1.00 32.08 ? 630  VAL   A CG1   1 
ATOM   4642  C  CG2   . VAL   A  1  632  ? -18.481 67.165  131.316 1.00 30.86 ? 630  VAL   A CG2   1 
ATOM   4643  N  N     . PRO   A  1  633  ? -16.255 63.143  130.011 1.00 28.16 ? 631  PRO   A N     1 
ATOM   4644  C  CA    . PRO   A  1  633  ? -15.529 62.239  129.125 1.00 27.34 ? 631  PRO   A CA    1 
ATOM   4645  C  C     . PRO   A  1  633  ? -15.939 62.460  127.679 1.00 26.58 ? 631  PRO   A C     1 
ATOM   4646  O  O     . PRO   A  1  633  ? -17.087 62.841  127.393 1.00 26.49 ? 631  PRO   A O     1 
ATOM   4647  C  CB    . PRO   A  1  633  ? -15.954 60.849  129.612 1.00 31.40 ? 631  PRO   A CB    1 
ATOM   4648  C  CG    . PRO   A  1  633  ? -16.396 61.055  131.016 1.00 32.91 ? 631  PRO   A CG    1 
ATOM   4649  C  CD    . PRO   A  1  633  ? -16.989 62.424  131.064 1.00 31.41 ? 631  PRO   A CD    1 
ATOM   4650  N  N     . PRO   A  1  634  ? -15.025 62.243  126.740 1.00 23.19 ? 632  PRO   A N     1 
ATOM   4651  C  CA    . PRO   A  1  634  ? -15.374 62.444  125.324 1.00 25.49 ? 632  PRO   A CA    1 
ATOM   4652  C  C     . PRO   A  1  634  ? -16.635 61.718  124.896 1.00 22.95 ? 632  PRO   A C     1 
ATOM   4653  O  O     . PRO   A  1  634  ? -17.422 62.270  124.119 1.00 23.32 ? 632  PRO   A O     1 
ATOM   4654  C  CB    . PRO   A  1  634  ? -14.137 61.925  124.580 1.00 25.72 ? 632  PRO   A CB    1 
ATOM   4655  C  CG    . PRO   A  1  634  ? -13.024 62.058  125.554 1.00 28.01 ? 632  PRO   A CG    1 
ATOM   4656  C  CD    . PRO   A  1  634  ? -13.611 61.882  126.931 1.00 26.50 ? 632  PRO   A CD    1 
ATOM   4657  N  N     . SER   A  1  635  ? -16.848 60.488  125.366 1.00 25.46 ? 633  SER   A N     1 
ATOM   4658  C  CA    . SER   A  1  635  ? -18.048 59.754  124.966 1.00 27.54 ? 633  SER   A CA    1 
ATOM   4659  C  C     . SER   A  1  635  ? -19.311 60.489  125.395 1.00 25.53 ? 633  SER   A C     1 
ATOM   4660  O  O     . SER   A  1  635  ? -20.308 60.502  124.663 1.00 26.26 ? 633  SER   A O     1 
ATOM   4661  C  CB    . SER   A  1  635  ? -18.025 58.359  125.583 1.00 35.34 ? 633  SER   A CB    1 
ATOM   4662  O  OG    . SER   A  1  635  ? -18.108 58.450  126.994 1.00 45.23 ? 633  SER   A OG    1 
ATOM   4663  N  N     . GLU   A  1  636  ? -19.288 61.109  126.577 1.00 25.50 ? 634  GLU   A N     1 
ATOM   4664  C  CA    . GLU   A  1  636  ? -20.460 61.848  127.034 1.00 26.15 ? 634  GLU   A CA    1 
ATOM   4665  C  C     . GLU   A  1  636  ? -20.609 63.177  126.299 1.00 25.54 ? 634  GLU   A C     1 
ATOM   4666  O  O     . GLU   A  1  636  ? -21.734 63.595  125.991 1.00 26.75 ? 634  GLU   A O     1 
ATOM   4667  C  CB    . GLU   A  1  636  ? -20.409 62.047  128.550 1.00 29.09 ? 634  GLU   A CB    1 
ATOM   4668  C  CG    . GLU   A  1  636  ? -21.578 62.851  129.087 1.00 37.35 ? 634  GLU   A CG    1 
ATOM   4669  C  CD    . GLU   A  1  636  ? -22.927 62.321  128.619 1.00 43.23 ? 634  GLU   A CD    1 
ATOM   4670  O  OE1   . GLU   A  1  636  ? -23.131 61.088  128.657 1.00 42.22 ? 634  GLU   A OE1   1 
ATOM   4671  O  OE2   . GLU   A  1  636  ? -23.780 63.138  128.198 1.00 41.21 ? 634  GLU   A OE2   1 
ATOM   4672  N  N     . ARG   A  1  637  ? -19.500 63.858  125.999 1.00 24.70 ? 635  ARG   A N     1 
ATOM   4673  C  CA    . ARG   A  1  637  ? -19.600 65.046  125.159 1.00 23.43 ? 635  ARG   A CA    1 
ATOM   4674  C  C     . ARG   A  1  637  ? -20.216 64.690  123.815 1.00 22.03 ? 635  ARG   A C     1 
ATOM   4675  O  O     . ARG   A  1  637  ? -21.092 65.401  123.311 1.00 22.73 ? 635  ARG   A O     1 
ATOM   4676  C  CB    . ARG   A  1  637  ? -18.227 65.705  124.983 1.00 22.72 ? 635  ARG   A CB    1 
ATOM   4677  C  CG    . ARG   A  1  637  ? -17.594 66.068  126.328 1.00 23.38 ? 635  ARG   A CG    1 
ATOM   4678  C  CD    . ARG   A  1  637  ? -16.399 66.995  126.185 1.00 25.25 ? 635  ARG   A CD    1 
ATOM   4679  N  NE    . ARG   A  1  637  ? -15.356 66.449  125.335 1.00 25.67 ? 635  ARG   A NE    1 
ATOM   4680  C  CZ    . ARG   A  1  637  ? -14.172 66.026  125.764 1.00 26.04 ? 635  ARG   A CZ    1 
ATOM   4681  N  NH1   . ARG   A  1  637  ? -13.856 66.025  127.048 1.00 28.65 ? 635  ARG   A NH1   1 
ATOM   4682  N  NH2   . ARG   A  1  637  ? -13.276 65.619  124.877 1.00 25.04 ? 635  ARG   A NH2   1 
ATOM   4683  N  N     . ALA   A  1  638  ? -19.768 63.580  123.224 1.00 22.05 ? 636  ALA   A N     1 
ATOM   4684  C  CA    . ALA   A  1  638  ? -20.319 63.137  121.951 1.00 22.96 ? 636  ALA   A CA    1 
ATOM   4685  C  C     . ALA   A  1  638  ? -21.796 62.791  122.084 1.00 21.95 ? 636  ALA   A C     1 
ATOM   4686  O  O     . ALA   A  1  638  ? -22.581 63.003  121.149 1.00 21.62 ? 636  ALA   A O     1 
ATOM   4687  C  CB    . ALA   A  1  638  ? -19.520 61.938  121.442 1.00 23.36 ? 636  ALA   A CB    1 
ATOM   4688  N  N     . ALA   A  1  639  ? -22.193 62.248  123.235 1.00 22.30 ? 637  ALA   A N     1 
ATOM   4689  C  CA    . ALA   A  1  639  ? -23.606 61.955  123.441 1.00 24.33 ? 637  ALA   A CA    1 
ATOM   4690  C  C     . ALA   A  1  639  ? -24.442 63.230  123.452 1.00 24.70 ? 637  ALA   A C     1 
ATOM   4691  O  O     . ALA   A  1  639  ? -25.590 63.224  122.991 1.00 24.68 ? 637  ALA   A O     1 
ATOM   4692  C  CB    . ALA   A  1  639  ? -23.805 61.146  124.724 1.00 24.16 ? 637  ALA   A CB    1 
ATOM   4693  N  N     . CYS   A  1  640  ? -23.883 64.334  123.961 1.00 23.27 ? 638  CYS   A N     1 
ATOM   4694  C  CA    . CYS   A  1  640  ? -24.584 65.611  123.882 1.00 24.43 ? 638  CYS   A CA    1 
ATOM   4695  C  C     . CYS   A  1  640  ? -24.799 66.014  122.438 1.00 23.02 ? 638  CYS   A C     1 
ATOM   4696  O  O     . CYS   A  1  640  ? -25.891 66.464  122.070 1.00 22.84 ? 638  CYS   A O     1 
ATOM   4697  C  CB    . CYS   A  1  640  ? -23.786 66.708  124.574 1.00 23.90 ? 638  CYS   A CB    1 
ATOM   4698  S  SG    . CYS   A  1  640  ? -23.686 66.566  126.352 1.00 27.09 ? 638  CYS   A SG    1 
ATOM   4699  N  N     . LEU   A  1  641  ? -23.765 65.862  121.607 1.00 21.90 ? 639  LEU   A N     1 
ATOM   4700  C  CA    . LEU   A  1  641  ? -23.911 66.185  120.198 1.00 22.10 ? 639  LEU   A CA    1 
ATOM   4701  C  C     . LEU   A  1  641  ? -24.973 65.312  119.556 1.00 21.01 ? 639  LEU   A C     1 
ATOM   4702  O  O     . LEU   A  1  641  ? -25.800 65.801  118.774 1.00 20.82 ? 639  LEU   A O     1 
ATOM   4703  C  CB    . LEU   A  1  641  ? -22.573 66.013  119.483 1.00 21.43 ? 639  LEU   A CB    1 
ATOM   4704  C  CG    . LEU   A  1  641  ? -21.645 67.227  119.464 1.00 22.01 ? 639  LEU   A CG    1 
ATOM   4705  C  CD1   . LEU   A  1  641  ? -21.233 67.679  120.838 1.00 24.34 ? 639  LEU   A CD1   1 
ATOM   4706  C  CD2   . LEU   A  1  641  ? -20.426 66.918  118.614 1.00 19.86 ? 639  LEU   A CD2   1 
ATOM   4707  N  N     . ASP   A  1  642  ? -24.964 64.013  119.856 1.00 21.59 ? 640  ASP   A N     1 
ATOM   4708  C  CA    . ASP   A  1  642  ? -25.965 63.137  119.254 1.00 21.48 ? 640  ASP   A CA    1 
ATOM   4709  C  C     . ASP   A  1  642  ? -27.373 63.506  119.714 1.00 22.21 ? 640  ASP   A C     1 
ATOM   4710  O  O     . ASP   A  1  642  ? -28.320 63.478  118.918 1.00 21.79 ? 640  ASP   A O     1 
ATOM   4711  C  CB    . ASP   A  1  642  ? -25.655 61.672  119.559 1.00 22.34 ? 640  ASP   A CB    1 
ATOM   4712  C  CG    . ASP   A  1  642  ? -24.563 61.108  118.669 1.00 23.98 ? 640  ASP   A CG    1 
ATOM   4713  O  OD1   . ASP   A  1  642  ? -24.317 61.670  117.579 1.00 24.43 ? 640  ASP   A OD1   1 
ATOM   4714  O  OD2   . ASP   A  1  642  ? -23.957 60.096  119.070 1.00 27.00 ? 640  ASP   A OD2   1 
ATOM   4715  N  N     . ARG   A  1  643  ? -27.533 63.883  120.981 1.00 22.13 ? 641  ARG   A N     1 
ATOM   4716  C  CA    . ARG   A  1  643  ? -28.851 64.320  121.431 1.00 22.97 ? 641  ARG   A CA    1 
ATOM   4717  C  C     . ARG   A  1  643  ? -29.257 65.616  120.750 1.00 24.14 ? 641  ARG   A C     1 
ATOM   4718  O  O     . ARG   A  1  643  ? -30.429 65.798  120.399 1.00 24.06 ? 641  ARG   A O     1 
ATOM   4719  C  CB    . ARG   A  1  643  ? -28.892 64.483  122.952 1.00 24.05 ? 641  ARG   A CB    1 
ATOM   4720  C  CG    . ARG   A  1  643  ? -29.005 63.171  123.709 1.00 24.20 ? 641  ARG   A CG    1 
ATOM   4721  C  CD    . ARG   A  1  643  ? -29.181 63.401  125.203 1.00 28.47 ? 641  ARG   A CD    1 
ATOM   4722  N  NE    . ARG   A  1  643  ? -28.050 64.096  125.800 1.00 26.77 ? 641  ARG   A NE    1 
ATOM   4723  C  CZ    . ARG   A  1  643  ? -27.034 63.485  126.397 1.00 25.96 ? 641  ARG   A CZ    1 
ATOM   4724  N  NH1   . ARG   A  1  643  ? -26.940 62.167  126.419 1.00 29.94 ? 641  ARG   A NH1   1 
ATOM   4725  N  NH2   . ARG   A  1  643  ? -26.093 64.217  126.990 1.00 29.27 ? 641  ARG   A NH2   1 
ATOM   4726  N  N     . ALA   A  1  644  ? -28.309 66.532  120.548 1.00 21.09 ? 642  ALA   A N     1 
ATOM   4727  C  CA    . ALA   A  1  644  ? -28.642 67.759  119.837 1.00 22.00 ? 642  ALA   A CA    1 
ATOM   4728  C  C     . ALA   A  1  644  ? -29.078 67.453  118.416 1.00 21.23 ? 642  ALA   A C     1 
ATOM   4729  O  O     . ALA   A  1  644  ? -30.005 68.083  117.892 1.00 21.85 ? 642  ALA   A O     1 
ATOM   4730  C  CB    . ALA   A  1  644  ? -27.465 68.730  119.855 1.00 22.96 ? 642  ALA   A CB    1 
ATOM   4731  N  N     . ALA   A  1  645  ? -28.437 66.472  117.780 1.00 20.01 ? 643  ALA   A N     1 
ATOM   4732  C  CA    . ALA   A  1  645  ? -28.817 66.118  116.418 1.00 20.50 ? 643  ALA   A CA    1 
ATOM   4733  C  C     . ALA   A  1  645  ? -30.238 65.566  116.369 1.00 20.83 ? 643  ALA   A C     1 
ATOM   4734  O  O     . ALA   A  1  645  ? -30.999 65.878  115.443 1.00 21.75 ? 643  ALA   A O     1 
ATOM   4735  C  CB    . ALA   A  1  645  ? -27.801 65.128  115.847 1.00 21.62 ? 643  ALA   A CB    1 
ATOM   4736  N  N     . GLU   A  1  646  ? -30.589 64.704  117.320 1.00 21.31 ? 644  GLU   A N     1 
ATOM   4737  C  CA    . GLU   A  1  646  ? -31.963 64.218  117.412 1.00 22.84 ? 644  GLU   A CA    1 
ATOM   4738  C  C     . GLU   A  1  646  ? -32.945 65.367  117.596 1.00 23.61 ? 644  GLU   A C     1 
ATOM   4739  O  O     . GLU   A  1  646  ? -34.005 65.391  116.958 1.00 23.81 ? 644  GLU   A O     1 
ATOM   4740  C  CB    . GLU   A  1  646  ? -32.110 63.248  118.578 1.00 26.99 ? 644  GLU   A CB    1 
ATOM   4741  C  CG    . GLU   A  1  646  ? -31.374 61.947  118.417 1.00 31.81 ? 644  GLU   A CG    1 
ATOM   4742  C  CD    . GLU   A  1  646  ? -31.871 61.135  117.245 1.00 41.83 ? 644  GLU   A CD    1 
ATOM   4743  O  OE1   . GLU   A  1  646  ? -33.085 61.181  116.954 1.00 47.96 ? 644  GLU   A OE1   1 
ATOM   4744  O  OE2   . GLU   A  1  646  ? -31.037 60.457  116.611 1.00 38.29 ? 644  GLU   A OE2   1 
ATOM   4745  N  N     . LEU   A  1  647  ? -32.612 66.322  118.467 1.00 24.14 ? 645  LEU   A N     1 
ATOM   4746  C  CA    . LEU   A  1  647  ? -33.497 67.462  118.697 1.00 23.04 ? 645  LEU   A CA    1 
ATOM   4747  C  C     . LEU   A  1  647  ? -33.640 68.301  117.434 1.00 25.06 ? 645  LEU   A C     1 
ATOM   4748  O  O     . LEU   A  1  647  ? -34.744 68.745  117.100 1.00 26.48 ? 645  LEU   A O     1 
ATOM   4749  C  CB    . LEU   A  1  647  ? -32.973 68.312  119.851 1.00 25.25 ? 645  LEU   A CB    1 
ATOM   4750  C  CG    . LEU   A  1  647  ? -33.026 67.640  121.221 1.00 25.44 ? 645  LEU   A CG    1 
ATOM   4751  C  CD1   . LEU   A  1  647  ? -32.308 68.472  122.272 1.00 26.60 ? 645  LEU   A CD1   1 
ATOM   4752  C  CD2   . LEU   A  1  647  ? -34.467 67.371  121.655 1.00 32.05 ? 645  LEU   A CD2   1 
ATOM   4753  N  N     . MET   A  1  648  ? -32.540 68.521  116.709 1.00 23.04 ? 646  MET   A N     1 
ATOM   4754  C  CA    . MET   A  1  648  ? -32.638 69.297  115.479 1.00 22.29 ? 646  MET   A CA    1 
ATOM   4755  C  C     . MET   A  1  648  ? -33.457 68.567  114.437 1.00 22.27 ? 646  MET   A C     1 
ATOM   4756  O  O     . MET   A  1  648  ? -34.231 69.191  113.706 1.00 23.93 ? 646  MET   A O     1 
ATOM   4757  C  CB    . MET   A  1  648  ? -31.256 69.622  114.921 1.00 21.14 ? 646  MET   A CB    1 
ATOM   4758  C  CG    . MET   A  1  648  ? -30.590 70.690  115.721 1.00 22.07 ? 646  MET   A CG    1 
ATOM   4759  S  SD    . MET   A  1  648  ? -29.195 71.339  114.812 1.00 25.87 ? 646  MET   A SD    1 
ATOM   4760  C  CE    . MET   A  1  648  ? -28.555 72.493  116.014 1.00 27.34 ? 646  MET   A CE    1 
ATOM   4761  N  N     . GLN   A  1  649  ? -33.289 67.248  114.342 1.00 22.59 ? 647  GLN   A N     1 
ATOM   4762  C  CA    . GLN   A  1  649  ? -34.082 66.482  113.391 1.00 22.59 ? 647  GLN   A CA    1 
ATOM   4763  C  C     . GLN   A  1  649  ? -35.568 66.593  113.704 1.00 23.16 ? 647  GLN   A C     1 
ATOM   4764  O  O     . GLN   A  1  649  ? -36.389 66.810  112.803 1.00 24.41 ? 647  GLN   A O     1 
ATOM   4765  C  CB    . GLN   A  1  649  ? -33.641 65.020  113.386 1.00 22.21 ? 647  GLN   A CB    1 
ATOM   4766  C  CG    . GLN   A  1  649  ? -34.360 64.189  112.334 1.00 22.31 ? 647  GLN   A CG    1 
ATOM   4767  C  CD    . GLN   A  1  649  ? -33.812 64.428  110.952 1.00 22.58 ? 647  GLN   A CD    1 
ATOM   4768  O  OE1   . GLN   A  1  649  ? -32.726 63.962  110.617 1.00 20.95 ? 647  GLN   A OE1   1 
ATOM   4769  N  NE2   . GLN   A  1  649  ? -34.564 65.145  110.127 1.00 24.64 ? 647  GLN   A NE2   1 
ATOM   4770  N  N     . ALA   A  1  650  ? -35.930 66.456  114.976 1.00 23.52 ? 648  ALA   A N     1 
ATOM   4771  C  CA    . ALA   A  1  650  ? -37.338 66.534  115.344 1.00 24.79 ? 648  ALA   A CA    1 
ATOM   4772  C  C     . ALA   A  1  650  ? -37.894 67.928  115.115 1.00 29.71 ? 648  ALA   A C     1 
ATOM   4773  O  O     . ALA   A  1  650  ? -39.075 68.075  114.774 1.00 29.29 ? 648  ALA   A O     1 
ATOM   4774  C  CB    . ALA   A  1  650  ? -37.508 66.143  116.811 1.00 27.60 ? 648  ALA   A CB    1 
ATOM   4775  N  N     . ARG   A  1  651  ? -37.070 68.951  115.297 1.00 23.68 ? 649  ARG   A N     1 
ATOM   4776  C  CA    . ARG   A  1  651  ? -37.495 70.337  115.207 1.00 23.62 ? 649  ARG   A CA    1 
ATOM   4777  C  C     . ARG   A  1  651  ? -37.299 70.905  113.812 1.00 23.20 ? 649  ARG   A C     1 
ATOM   4778  O  O     . ARG   A  1  651  ? -37.512 72.102  113.608 1.00 25.91 ? 649  ARG   A O     1 
ATOM   4779  C  CB    . ARG   A  1  651  ? -36.750 71.185  116.245 1.00 28.08 ? 649  ARG   A CB    1 
ATOM   4780  C  CG    . ARG   A  1  651  ? -37.367 72.556  116.531 1.00 32.28 ? 649  ARG   A CG    1 
ATOM   4781  C  CD    . ARG   A  1  651  ? -37.077 73.027  117.958 1.00 32.46 ? 649  ARG   A CD    1 
ATOM   4782  N  NE    . ARG   A  1  651  ? -37.596 74.367  118.220 1.00 34.58 ? 649  ARG   A NE    1 
ATOM   4783  C  CZ    . ARG   A  1  651  ? -38.876 74.656  118.418 1.00 35.56 ? 649  ARG   A CZ    1 
ATOM   4784  N  NH1   . ARG   A  1  651  ? -39.818 73.733  118.315 1.00 38.47 ? 649  ARG   A NH1   1 
ATOM   4785  N  NH2   . ARG   A  1  651  ? -39.220 75.906  118.718 1.00 37.46 ? 649  ARG   A NH2   1 
ATOM   4786  N  N     . MET   A  1  652  ? -36.879 70.077  112.861 1.00 23.48 ? 650  MET   A N     1 
ATOM   4787  C  CA    . MET   A  1  652  ? -36.561 70.576  111.526 1.00 23.10 ? 650  MET   A CA    1 
ATOM   4788  C  C     . MET   A  1  652  ? -37.636 71.476  110.936 1.00 23.28 ? 650  MET   A C     1 
ATOM   4789  O  O     . MET   A  1  652  ? -37.290 72.564  110.454 1.00 24.17 ? 650  MET   A O     1 
ATOM   4790  C  CB    . MET   A  1  652  ? -36.194 69.425  110.583 1.00 23.24 ? 650  MET   A CB    1 
ATOM   4791  C  CG    . MET   A  1  652  ? -36.008 69.882  109.146 1.00 22.73 ? 650  MET   A CG    1 
ATOM   4792  S  SD    . MET   A  1  652  ? -35.530 68.554  108.021 1.00 25.63 ? 650  MET   A SD    1 
ATOM   4793  C  CE    . MET   A  1  652  ? -33.827 68.320  108.490 1.00 23.77 ? 650  MET   A CE    1 
ATOM   4794  N  N     . PRO   A  1  653  ? -38.929 71.121  110.955 1.00 23.88 ? 651  PRO   A N     1 
ATOM   4795  C  CA    . PRO   A  1  653  ? -39.910 72.001  110.301 1.00 26.89 ? 651  PRO   A CA    1 
ATOM   4796  C  C     . PRO   A  1  653  ? -39.908 73.404  110.867 1.00 25.88 ? 651  PRO   A C     1 
ATOM   4797  O  O     . PRO   A  1  653  ? -39.934 74.384  110.110 1.00 24.65 ? 651  PRO   A O     1 
ATOM   4798  C  CB    . PRO   A  1  653  ? -41.234 71.271  110.545 1.00 24.40 ? 651  PRO   A CB    1 
ATOM   4799  C  CG    . PRO   A  1  653  ? -40.841 69.834  110.605 1.00 27.29 ? 651  PRO   A CG    1 
ATOM   4800  C  CD    . PRO   A  1  653  ? -39.546 69.857  111.386 1.00 25.05 ? 651  PRO   A CD    1 
ATOM   4801  N  N     . THR   A  1  654  ? -39.827 73.522  112.190 1.00 23.33 ? 652  THR   A N     1 
ATOM   4802  C  CA    . THR   A  1  654  ? -39.776 74.837  112.805 1.00 23.93 ? 652  THR   A CA    1 
ATOM   4803  C  C     . THR   A  1  654  ? -38.480 75.550  112.454 1.00 24.19 ? 652  THR   A C     1 
ATOM   4804  O  O     . THR   A  1  654  ? -38.487 76.745  112.131 1.00 24.48 ? 652  THR   A O     1 
ATOM   4805  C  CB    . THR   A  1  654  ? -39.925 74.684  114.316 1.00 25.96 ? 652  THR   A CB    1 
ATOM   4806  O  OG1   . THR   A  1  654  ? -41.180 74.051  114.587 1.00 27.27 ? 652  THR   A OG1   1 
ATOM   4807  C  CG2   . THR   A  1  654  ? -39.877 76.035  114.996 1.00 29.29 ? 652  THR   A CG2   1 
ATOM   4808  N  N     . LEU   A  1  655  ? -37.360 74.825  112.487 1.00 23.02 ? 653  LEU   A N     1 
ATOM   4809  C  CA    . LEU   A  1  655  ? -36.089 75.417  112.098 1.00 23.45 ? 653  LEU   A CA    1 
ATOM   4810  C  C     . LEU   A  1  655  ? -36.117 75.905  110.656 1.00 24.21 ? 653  LEU   A C     1 
ATOM   4811  O  O     . LEU   A  1  655  ? -35.560 76.964  110.345 1.00 23.80 ? 653  LEU   A O     1 
ATOM   4812  C  CB    . LEU   A  1  655  ? -34.963 74.403  112.293 1.00 24.17 ? 653  LEU   A CB    1 
ATOM   4813  C  CG    . LEU   A  1  655  ? -34.794 73.926  113.731 1.00 23.87 ? 653  LEU   A CG    1 
ATOM   4814  C  CD1   . LEU   A  1  655  ? -33.658 72.926  113.827 1.00 23.57 ? 653  LEU   A CD1   1 
ATOM   4815  C  CD2   . LEU   A  1  655  ? -34.536 75.106  114.635 1.00 28.68 ? 653  LEU   A CD2   1 
ATOM   4816  N  N     . LEU   A  1  656  ? -36.761 75.145  109.758 1.00 25.04 ? 654  LEU   A N     1 
ATOM   4817  C  CA    . LEU   A  1  656  ? -36.882 75.588  108.371 1.00 24.26 ? 654  LEU   A CA    1 
ATOM   4818  C  C     . LEU   A  1  656  ? -37.533 76.955  108.290 1.00 24.27 ? 654  LEU   A C     1 
ATOM   4819  O  O     . LEU   A  1  656  ? -37.060 77.842  107.572 1.00 24.46 ? 654  LEU   A O     1 
ATOM   4820  C  CB    . LEU   A  1  656  ? -37.736 74.612  107.561 1.00 25.34 ? 654  LEU   A CB    1 
ATOM   4821  C  CG    . LEU   A  1  656  ? -37.279 73.173  107.420 1.00 26.16 ? 654  LEU   A CG    1 
ATOM   4822  C  CD1   . LEU   A  1  656  ? -38.187 72.456  106.440 1.00 28.07 ? 654  LEU   A CD1   1 
ATOM   4823  C  CD2   . LEU   A  1  656  ? -35.835 73.117  106.990 1.00 24.40 ? 654  LEU   A CD2   1 
ATOM   4824  N  N     . GLY   A  1  657  ? -38.647 77.126  108.998 1.00 24.27 ? 655  GLY   A N     1 
ATOM   4825  C  CA    . GLY   A  1  657  ? -39.369 78.378  108.916 1.00 25.79 ? 655  GLY   A CA    1 
ATOM   4826  C  C     . GLY   A  1  657  ? -38.528 79.549  109.366 1.00 23.07 ? 655  GLY   A C     1 
ATOM   4827  O  O     . GLY   A  1  657  ? -38.581 80.628  108.776 1.00 25.47 ? 655  GLY   A O     1 
ATOM   4828  N  N     . LEU   A  1  658  ? -37.740 79.354  110.424 1.00 23.45 ? 656  LEU   A N     1 
ATOM   4829  C  CA    . LEU   A  1  658  ? -36.895 80.436  110.907 1.00 24.73 ? 656  LEU   A CA    1 
ATOM   4830  C  C     . LEU   A  1  658  ? -35.807 80.755  109.889 1.00 21.56 ? 656  LEU   A C     1 
ATOM   4831  O  O     . LEU   A  1  658  ? -35.571 81.922  109.561 1.00 24.39 ? 656  LEU   A O     1 
ATOM   4832  C  CB    . LEU   A  1  658  ? -36.307 80.067  112.270 1.00 23.64 ? 656  LEU   A CB    1 
ATOM   4833  C  CG    . LEU   A  1  658  ? -35.409 81.118  112.916 1.00 26.48 ? 656  LEU   A CG    1 
ATOM   4834  C  CD1   . LEU   A  1  658  ? -36.143 82.446  113.044 1.00 27.29 ? 656  LEU   A CD1   1 
ATOM   4835  C  CD2   . LEU   A  1  658  ? -34.951 80.624  114.275 1.00 26.03 ? 656  LEU   A CD2   1 
ATOM   4836  N  N     . ILE   A  1  659  ? -35.148 79.724  109.361 1.00 22.11 ? 657  ILE   A N     1 
ATOM   4837  C  CA    . ILE   A  1  659  ? -34.097 79.936  108.373 1.00 21.70 ? 657  ILE   A CA    1 
ATOM   4838  C  C     . ILE   A  1  659  ? -34.654 80.596  107.122 1.00 23.00 ? 657  ILE   A C     1 
ATOM   4839  O  O     . ILE   A  1  659  ? -34.039 81.509  106.555 1.00 21.63 ? 657  ILE   A O     1 
ATOM   4840  C  CB    . ILE   A  1  659  ? -33.409 78.600  108.052 1.00 20.46 ? 657  ILE   A CB    1 
ATOM   4841  C  CG1   . ILE   A  1  659  ? -32.701 78.103  109.309 1.00 22.13 ? 657  ILE   A CG1   1 
ATOM   4842  C  CG2   . ILE   A  1  659  ? -32.456 78.771  106.895 1.00 22.83 ? 657  ILE   A CG2   1 
ATOM   4843  C  CD1   . ILE   A  1  659  ? -32.250 76.682  109.220 1.00 24.50 ? 657  ILE   A CD1   1 
ATOM   4844  N  N     . ILE   A  1  660  ? -35.823 80.138  106.670 1.00 20.40 ? 658  ILE   A N     1 
ATOM   4845  C  CA    . ILE   A  1  660  ? -36.457 80.731  105.494 1.00 23.83 ? 658  ILE   A CA    1 
ATOM   4846  C  C     . ILE   A  1  660  ? -36.643 82.230  105.684 1.00 24.58 ? 658  ILE   A C     1 
ATOM   4847  O  O     . ILE   A  1  660  ? -36.302 83.033  104.807 1.00 24.66 ? 658  ILE   A O     1 
ATOM   4848  C  CB    . ILE   A  1  660  ? -37.790 80.019  105.205 1.00 21.29 ? 658  ILE   A CB    1 
ATOM   4849  C  CG1   . ILE   A  1  660  ? -37.516 78.639  104.609 1.00 21.04 ? 658  ILE   A CG1   1 
ATOM   4850  C  CG2   . ILE   A  1  660  ? -38.667 80.857  104.276 1.00 24.63 ? 658  ILE   A CG2   1 
ATOM   4851  C  CD1   . ILE   A  1  660  ? -38.761 77.782  104.545 1.00 24.90 ? 658  ILE   A CD1   1 
ATOM   4852  N  N     . ARG   A  1  661  ? -37.177 82.632  106.839 1.00 22.16 ? 659  ARG   A N     1 
ATOM   4853  C  CA    . ARG   A  1  661  ? -37.515 84.032  107.042 1.00 23.68 ? 659  ARG   A CA    1 
ATOM   4854  C  C     . ARG   A  1  661  ? -36.318 84.867  107.466 1.00 27.16 ? 659  ARG   A C     1 
ATOM   4855  O  O     . ARG   A  1  661  ? -36.244 86.049  107.111 1.00 25.56 ? 659  ARG   A O     1 
ATOM   4856  C  CB    . ARG   A  1  661  ? -38.644 84.156  108.060 1.00 25.06 ? 659  ARG   A CB    1 
ATOM   4857  C  CG    . ARG   A  1  661  ? -39.982 83.740  107.467 1.00 24.24 ? 659  ARG   A CG    1 
ATOM   4858  C  CD    . ARG   A  1  661  ? -41.093 83.688  108.496 1.00 25.73 ? 659  ARG   A CD    1 
ATOM   4859  N  NE    . ARG   A  1  661  ? -41.348 84.983  109.107 1.00 27.26 ? 659  ARG   A NE    1 
ATOM   4860  C  CZ    . ARG   A  1  661  ? -41.303 85.215  110.411 1.00 27.27 ? 659  ARG   A CZ    1 
ATOM   4861  N  NH1   . ARG   A  1  661  ? -40.964 84.269  111.273 1.00 30.09 ? 659  ARG   A NH1   1 
ATOM   4862  N  NH2   . ARG   A  1  661  ? -41.620 86.424  110.866 1.00 27.16 ? 659  ARG   A NH2   1 
ATOM   4863  N  N     . GLU   A  1  662  ? -35.388 84.293  108.233 1.00 24.83 ? 660  GLU   A N     1 
ATOM   4864  C  CA    . GLU   A  1  662  ? -34.275 85.094  108.725 1.00 23.98 ? 660  GLU   A CA    1 
ATOM   4865  C  C     . GLU   A  1  662  ? -33.180 85.254  107.678 1.00 22.93 ? 660  GLU   A C     1 
ATOM   4866  O  O     . GLU   A  1  662  ? -32.577 86.327  107.573 1.00 25.43 ? 660  GLU   A O     1 
ATOM   4867  C  CB    . GLU   A  1  662  ? -33.701 84.494  110.014 1.00 25.01 ? 660  GLU   A CB    1 
ATOM   4868  C  CG    . GLU   A  1  662  ? -32.613 85.365  110.642 1.00 25.04 ? 660  GLU   A CG    1 
ATOM   4869  C  CD    . GLU   A  1  662  ? -32.022 84.804  111.927 1.00 25.32 ? 660  GLU   A CD    1 
ATOM   4870  O  OE1   . GLU   A  1  662  ? -31.972 83.566  112.100 1.00 27.16 ? 660  GLU   A OE1   1 
ATOM   4871  O  OE2   . GLU   A  1  662  ? -31.605 85.618  112.767 1.00 26.22 ? 660  GLU   A OE2   1 
ATOM   4872  N  N     . ALA   A  1  663  ? -32.910 84.210  106.901 1.00 23.27 ? 661  ALA   A N     1 
ATOM   4873  C  CA    . ALA   A  1  663  ? -31.716 84.168  106.069 1.00 22.22 ? 661  ALA   A CA    1 
ATOM   4874  C  C     . ALA   A  1  663  ? -32.014 84.159  104.577 1.00 24.14 ? 661  ALA   A C     1 
ATOM   4875  O  O     . ALA   A  1  663  ? -31.092 83.974  103.776 1.00 28.43 ? 661  ALA   A O     1 
ATOM   4876  C  CB    . ALA   A  1  663  ? -30.836 82.975  106.452 1.00 24.13 ? 661  ALA   A CB    1 
ATOM   4877  N  N     . GLY   A  1  664  ? -33.274 84.341  104.187 1.00 25.79 ? 662  GLY   A N     1 
ATOM   4878  C  CA    . GLY   A  1  664  ? -33.611 84.380  102.774 1.00 26.66 ? 662  GLY   A CA    1 
ATOM   4879  C  C     . GLY   A  1  664  ? -33.477 83.060  102.055 1.00 25.13 ? 662  GLY   A C     1 
ATOM   4880  O  O     . GLY   A  1  664  ? -33.243 83.040  100.844 1.00 28.10 ? 662  GLY   A O     1 
ATOM   4881  N  N     . LYS   A  1  665  ? -33.612 81.948  102.764 1.00 22.39 ? 663  LYS   A N     1 
ATOM   4882  C  CA    . LYS   A  1  665  ? -33.418 80.647  102.144 1.00 22.29 ? 663  LYS   A CA    1 
ATOM   4883  C  C     . LYS   A  1  665  ? -34.741 80.089  101.651 1.00 19.56 ? 663  LYS   A C     1 
ATOM   4884  O  O     . LYS   A  1  665  ? -35.793 80.304  102.250 1.00 20.16 ? 663  LYS   A O     1 
ATOM   4885  C  CB    . LYS   A  1  665  ? -32.843 79.657  103.150 1.00 21.90 ? 663  LYS   A CB    1 
ATOM   4886  C  CG    . LYS   A  1  665  ? -31.515 80.069  103.742 1.00 23.03 ? 663  LYS   A CG    1 
ATOM   4887  C  CD    . LYS   A  1  665  ? -30.469 80.273  102.678 1.00 29.13 ? 663  LYS   A CD    1 
ATOM   4888  C  CE    . LYS   A  1  665  ? -29.115 80.544  103.328 1.00 27.96 ? 663  LYS   A CE    1 
ATOM   4889  N  NZ    . LYS   A  1  665  ? -28.091 81.042  102.347 1.00 29.58 ? 663  LYS   A NZ    1 
ATOM   4890  N  N     . SER   A  1  666  ? -34.670 79.350  100.552 1.00 22.53 ? 664  SER   A N     1 
ATOM   4891  C  CA    . SER   A  1  666  ? -35.815 78.569  100.127 1.00 22.99 ? 664  SER   A CA    1 
ATOM   4892  C  C     . SER   A  1  666  ? -35.977 77.366  101.050 1.00 23.21 ? 664  SER   A C     1 
ATOM   4893  O  O     . SER   A  1  666  ? -35.078 77.016  101.821 1.00 22.69 ? 664  SER   A O     1 
ATOM   4894  C  CB    . SER   A  1  666  ? -35.573 78.042  98.724  1.00 24.04 ? 664  SER   A CB    1 
ATOM   4895  O  OG    . SER   A  1  666  ? -34.569 77.052  98.790  1.00 24.56 ? 664  SER   A OG    1 
ATOM   4896  N  N     . ALA   A  1  667  ? -37.145 76.725  100.981 1.00 22.48 ? 665  ALA   A N     1 
ATOM   4897  C  CA    . ALA   A  1  667  ? -37.380 75.540  101.802 1.00 21.07 ? 665  ALA   A CA    1 
ATOM   4898  C  C     . ALA   A  1  667  ? -36.351 74.448  101.517 1.00 22.40 ? 665  ALA   A C     1 
ATOM   4899  O  O     . ALA   A  1  667  ? -35.817 73.835  102.449 1.00 21.03 ? 665  ALA   A O     1 
ATOM   4900  C  CB    . ALA   A  1  667  ? -38.805 75.018  101.599 1.00 25.61 ? 665  ALA   A CB    1 
ATOM   4901  N  N     . LEU   A  1  668  ? -36.077 74.169  100.236 1.00 21.80 ? 666  LEU   A N     1 
ATOM   4902  C  CA    . LEU   A  1  668  ? -35.076 73.158  99.896  1.00 21.39 ? 666  LEU   A CA    1 
ATOM   4903  C  C     . LEU   A  1  668  ? -33.735 73.486  100.521 1.00 24.19 ? 666  LEU   A C     1 
ATOM   4904  O  O     . LEU   A  1  668  ? -33.067 72.606  101.076 1.00 22.98 ? 666  LEU   A O     1 
ATOM   4905  C  CB    . LEU   A  1  668  ? -34.897 73.061  98.379  1.00 25.21 ? 666  LEU   A CB    1 
ATOM   4906  C  CG    . LEU   A  1  668  ? -35.881 72.197  97.609  1.00 32.14 ? 666  LEU   A CG    1 
ATOM   4907  C  CD1   . LEU   A  1  668  ? -35.536 72.251  96.128  1.00 27.86 ? 666  LEU   A CD1   1 
ATOM   4908  C  CD2   . LEU   A  1  668  ? -35.819 70.774  98.132  1.00 33.79 ? 666  LEU   A CD2   1 
ATOM   4909  N  N     . ASN   A  1  669  ? -33.325 74.750  100.448 1.00 19.72 ? 667  ASN   A N     1 
ATOM   4910  C  CA    . ASN   A  1  669  ? -32.024 75.107  100.997 1.00 21.63 ? 667  ASN   A CA    1 
ATOM   4911  C  C     . ASN   A  1  669  ? -32.030 75.099  102.516 1.00 21.50 ? 667  ASN   A C     1 
ATOM   4912  O  O     . ASN   A  1  669  ? -31.007 74.774  103.127 1.00 21.93 ? 667  ASN   A O     1 
ATOM   4913  C  CB    . ASN   A  1  669  ? -31.572 76.448  100.439 1.00 23.92 ? 667  ASN   A CB    1 
ATOM   4914  C  CG    . ASN   A  1  669  ? -31.236 76.368  98.960  1.00 30.39 ? 667  ASN   A CG    1 
ATOM   4915  O  OD1   . ASN   A  1  669  ? -30.752 75.341  98.478  1.00 35.15 ? 667  ASN   A OD1   1 
ATOM   4916  N  ND2   . ASN   A  1  669  ? -31.488 77.443  98.240  1.00 33.40 ? 667  ASN   A ND2   1 
ATOM   4917  N  N     . ALA   A  1  670  ? -33.161 75.415  103.140 1.00 20.52 ? 668  ALA   A N     1 
ATOM   4918  C  CA    . ALA   A  1  670  ? -33.251 75.327  104.590 1.00 21.49 ? 668  ALA   A CA    1 
ATOM   4919  C  C     . ALA   A  1  670  ? -33.201 73.878  105.057 1.00 20.78 ? 668  ALA   A C     1 
ATOM   4920  O  O     . ALA   A  1  670  ? -32.604 73.575  106.095 1.00 20.00 ? 668  ALA   A O     1 
ATOM   4921  C  CB    . ALA   A  1  670  ? -34.525 76.019  105.074 1.00 20.06 ? 668  ALA   A CB    1 
ATOM   4922  N  N     . ILE   A  1  671  ? -33.837 72.966  104.322 1.00 19.32 ? 669  ILE   A N     1 
ATOM   4923  C  CA    . ILE   A  1  671  ? -33.732 71.550  104.661 1.00 19.34 ? 669  ILE   A CA    1 
ATOM   4924  C  C     . ILE   A  1  671  ? -32.279 71.111  104.624 1.00 20.31 ? 669  ILE   A C     1 
ATOM   4925  O  O     . ILE   A  1  671  ? -31.791 70.434  105.538 1.00 21.90 ? 669  ILE   A O     1 
ATOM   4926  C  CB    . ILE   A  1  671  ? -34.581 70.702  103.701 1.00 21.57 ? 669  ILE   A CB    1 
ATOM   4927  C  CG1   . ILE   A  1  671  ? -36.062 70.958  103.936 1.00 20.81 ? 669  ILE   A CG1   1 
ATOM   4928  C  CG2   . ILE   A  1  671  ? -34.200 69.235  103.837 1.00 23.09 ? 669  ILE   A CG2   1 
ATOM   4929  C  CD1   . ILE   A  1  671  ? -36.926 70.391  102.826 1.00 23.36 ? 669  ILE   A CD1   1 
ATOM   4930  N  N     . ALA   A  1  672  ? -31.570 71.483  103.558 1.00 17.89 ? 670  ALA   A N     1 
ATOM   4931  C  CA    . ALA   A  1  672  ? -30.168 71.122  103.448 1.00 19.11 ? 670  ALA   A CA    1 
ATOM   4932  C  C     . ALA   A  1  672  ? -29.371 71.720  104.588 1.00 19.61 ? 670  ALA   A C     1 
ATOM   4933  O  O     . ALA   A  1  672  ? -28.464 71.076  105.115 1.00 20.66 ? 670  ALA   A O     1 
ATOM   4934  C  CB    . ALA   A  1  672  ? -29.617 71.608  102.114 1.00 20.35 ? 670  ALA   A CB    1 
ATOM   4935  N  N     . GLU   A  1  673  ? -29.713 72.940  104.998 1.00 18.97 ? 671  GLU   A N     1 
ATOM   4936  C  CA    . GLU   A  1  673  ? -28.994 73.610  106.073 1.00 19.40 ? 671  GLU   A CA    1 
ATOM   4937  C  C     . GLU   A  1  673  ? -29.152 72.853  107.387 1.00 20.57 ? 671  GLU   A C     1 
ATOM   4938  O  O     . GLU   A  1  673  ? -28.176 72.613  108.107 1.00 19.59 ? 671  GLU   A O     1 
ATOM   4939  C  CB    . GLU   A  1  673  ? -29.546 75.025  106.213 1.00 20.01 ? 671  GLU   A CB    1 
ATOM   4940  C  CG    . GLU   A  1  673  ? -28.945 75.835  107.340 1.00 24.59 ? 671  GLU   A CG    1 
ATOM   4941  C  CD    . GLU   A  1  673  ? -27.663 76.477  106.928 1.00 26.93 ? 671  GLU   A CD    1 
ATOM   4942  O  OE1   . GLU   A  1  673  ? -27.357 76.503  105.710 1.00 28.62 ? 671  GLU   A OE1   1 
ATOM   4943  O  OE2   . GLU   A  1  673  ? -26.948 76.951  107.824 1.00 24.71 ? 671  GLU   A OE2   1 
ATOM   4944  N  N     . VAL   A  1  674  ? -30.380 72.455  107.711 1.00 17.77 ? 672  VAL   A N     1 
ATOM   4945  C  CA    . VAL   A  1  674  ? -30.622 71.722  108.947 1.00 18.64 ? 672  VAL   A CA    1 
ATOM   4946  C  C     . VAL   A  1  674  ? -30.006 70.334  108.878 1.00 19.49 ? 672  VAL   A C     1 
ATOM   4947  O  O     . VAL   A  1  674  ? -29.406 69.856  109.851 1.00 18.21 ? 672  VAL   A O     1 
ATOM   4948  C  CB    . VAL   A  1  674  ? -32.125 71.669  109.258 1.00 18.69 ? 672  VAL   A CB    1 
ATOM   4949  C  CG1   . VAL   A  1  674  ? -32.357 70.887  110.546 1.00 21.00 ? 672  VAL   A CG1   1 
ATOM   4950  C  CG2   . VAL   A  1  674  ? -32.688 73.082  109.398 1.00 20.99 ? 672  VAL   A CG2   1 
ATOM   4951  N  N     . ARG   A  1  675  ? -30.125 69.668  107.729 1.00 18.30 ? 673  ARG   A N     1 
ATOM   4952  C  CA    . ARG   A  1  675  ? -29.474 68.380  107.570 1.00 17.98 ? 673  ARG   A CA    1 
ATOM   4953  C  C     . ARG   A  1  675  ? -27.986 68.496  107.827 1.00 17.77 ? 673  ARG   A C     1 
ATOM   4954  O  O     . ARG   A  1  675  ? -27.410 67.651  108.508 1.00 18.54 ? 673  ARG   A O     1 
ATOM   4955  C  CB    . ARG   A  1  675  ? -29.722 67.826  106.175 1.00 18.26 ? 673  ARG   A CB    1 
ATOM   4956  C  CG    . ARG   A  1  675  ? -31.145 67.335  105.975 1.00 18.82 ? 673  ARG   A CG    1 
ATOM   4957  C  CD    . ARG   A  1  675  ? -31.204 66.556  104.673 1.00 19.62 ? 673  ARG   A CD    1 
ATOM   4958  N  NE    . ARG   A  1  675  ? -30.474 65.300  104.800 1.00 19.20 ? 673  ARG   A NE    1 
ATOM   4959  C  CZ    . ARG   A  1  675  ? -30.086 64.558  103.774 1.00 20.08 ? 673  ARG   A CZ    1 
ATOM   4960  N  NH1   . ARG   A  1  675  ? -30.335 64.926  102.526 1.00 20.17 ? 673  ARG   A NH1   1 
ATOM   4961  N  NH2   . ARG   A  1  675  ? -29.463 63.407  104.007 1.00 19.19 ? 673  ARG   A NH2   1 
ATOM   4962  N  N     . GLU   A  1  676  ? -27.349 69.530  107.271 1.00 16.77 ? 674  GLU   A N     1 
ATOM   4963  C  CA    . GLU   A  1  676  ? -25.909 69.689  107.459 1.00 17.88 ? 674  GLU   A CA    1 
ATOM   4964  C  C     . GLU   A  1  676  ? -25.569 69.851  108.932 1.00 18.32 ? 674  GLU   A C     1 
ATOM   4965  O  O     . GLU   A  1  676  ? -24.577 69.292  109.419 1.00 18.21 ? 674  GLU   A O     1 
ATOM   4966  C  CB    . GLU   A  1  676  ? -25.407 70.886  106.662 1.00 19.10 ? 674  GLU   A CB    1 
ATOM   4967  N  N     . ALA   A  1  677  ? -26.371 70.620  109.658 1.00 17.76 ? 675  ALA   A N     1 
ATOM   4968  C  CA    . ALA   A  1  677  ? -26.117 70.793  111.083 1.00 17.12 ? 675  ALA   A CA    1 
ATOM   4969  C  C     . ALA   A  1  677  ? -26.208 69.461  111.819 1.00 19.59 ? 675  ALA   A C     1 
ATOM   4970  O  O     . ALA   A  1  677  ? -25.352 69.134  112.657 1.00 18.40 ? 675  ALA   A O     1 
ATOM   4971  C  CB    . ALA   A  1  677  ? -27.110 71.810  111.649 1.00 18.76 ? 675  ALA   A CB    1 
ATOM   4972  N  N     . ILE   A  1  678  ? -27.262 68.696  111.542 1.00 18.64 ? 676  ILE   A N     1 
ATOM   4973  C  CA    . ILE   A  1  678  ? -27.424 67.372  112.124 1.00 19.16 ? 676  ILE   A CA    1 
ATOM   4974  C  C     . ILE   A  1  678  ? -26.225 66.500  111.802 1.00 19.13 ? 676  ILE   A C     1 
ATOM   4975  O  O     . ILE   A  1  678  ? -25.699 65.789  112.671 1.00 19.23 ? 676  ILE   A O     1 
ATOM   4976  C  CB    . ILE   A  1  678  ? -28.727 66.752  111.594 1.00 19.23 ? 676  ILE   A CB    1 
ATOM   4977  C  CG1   . ILE   A  1  678  ? -29.922 67.532  112.127 1.00 19.53 ? 676  ILE   A CG1   1 
ATOM   4978  C  CG2   . ILE   A  1  678  ? -28.838 65.289  111.946 1.00 20.21 ? 676  ILE   A CG2   1 
ATOM   4979  C  CD1   . ILE   A  1  678  ? -31.223 67.189  111.416 1.00 20.41 ? 676  ILE   A CD1   1 
ATOM   4980  N  N     . ASP   A  1  679  ? -25.775 66.544  110.546 1.00 17.38 ? 677  ASP   A N     1 
ATOM   4981  C  CA    . ASP   A  1  679  ? -24.659 65.711  110.124 1.00 16.41 ? 677  ASP   A CA    1 
ATOM   4982  C  C     . ASP   A  1  679  ? -23.363 66.131  110.795 1.00 18.29 ? 677  ASP   A C     1 
ATOM   4983  O  O     . ASP   A  1  679  ? -22.575 65.271  111.189 1.00 17.66 ? 677  ASP   A O     1 
ATOM   4984  C  CB    . ASP   A  1  679  ? -24.504 65.768  108.602 1.00 17.26 ? 677  ASP   A CB    1 
ATOM   4985  C  CG    . ASP   A  1  679  ? -25.667 65.125  107.869 1.00 19.93 ? 677  ASP   A CG    1 
ATOM   4986  O  OD1   . ASP   A  1  679  ? -26.262 64.184  108.409 1.00 21.66 ? 677  ASP   A OD1   1 
ATOM   4987  O  OD2   . ASP   A  1  679  ? -25.949 65.532  106.726 1.00 22.78 ? 677  ASP   A OD2   1 
ATOM   4988  N  N     . PHE   A  1  680  ? -23.123 67.439  110.941 1.00 17.49 ? 678  PHE   A N     1 
ATOM   4989  C  CA    . PHE   A  1  680  ? -21.946 67.878  111.695 1.00 17.81 ? 678  PHE   A CA    1 
ATOM   4990  C  C     . PHE   A  1  680  ? -21.971 67.314  113.106 1.00 18.12 ? 678  PHE   A C     1 
ATOM   4991  O  O     . PHE   A  1  680  ? -20.969 66.788  113.603 1.00 18.56 ? 678  PHE   A O     1 
ATOM   4992  C  CB    . PHE   A  1  680  ? -21.891 69.397  111.795 1.00 18.54 ? 678  PHE   A CB    1 
ATOM   4993  C  CG    . PHE   A  1  680  ? -21.263 70.084  110.628 1.00 17.95 ? 678  PHE   A CG    1 
ATOM   4994  C  CD1   . PHE   A  1  680  ? -20.037 69.696  110.135 1.00 18.48 ? 678  PHE   A CD1   1 
ATOM   4995  C  CD2   . PHE   A  1  680  ? -21.899 71.166  110.054 1.00 18.53 ? 678  PHE   A CD2   1 
ATOM   4996  C  CE1   . PHE   A  1  680  ? -19.467 70.367  109.077 1.00 18.54 ? 678  PHE   A CE1   1 
ATOM   4997  C  CE2   . PHE   A  1  680  ? -21.352 71.837  109.009 1.00 17.81 ? 678  PHE   A CE2   1 
ATOM   4998  C  CZ    . PHE   A  1  680  ? -20.134 71.440  108.499 1.00 18.76 ? 678  PHE   A CZ    1 
ATOM   4999  N  N     . LEU   A  1  681  ? -23.101 67.458  113.787 1.00 17.36 ? 679  LEU   A N     1 
ATOM   5000  C  CA    . LEU   A  1  681  ? -23.203 66.961  115.153 1.00 17.17 ? 679  LEU   A CA    1 
ATOM   5001  C  C     . LEU   A  1  681  ? -22.884 65.476  115.217 1.00 19.90 ? 679  LEU   A C     1 
ATOM   5002  O  O     . LEU   A  1  681  ? -22.074 65.038  116.046 1.00 18.93 ? 679  LEU   A O     1 
ATOM   5003  C  CB    . LEU   A  1  681  ? -24.605 67.245  115.696 1.00 20.30 ? 679  LEU   A CB    1 
ATOM   5004  C  CG    . LEU   A  1  681  ? -24.909 68.723  115.942 1.00 20.85 ? 679  LEU   A CG    1 
ATOM   5005  C  CD1   . LEU   A  1  681  ? -26.407 68.994  115.985 1.00 20.93 ? 679  LEU   A CD1   1 
ATOM   5006  C  CD2   . LEU   A  1  681  ? -24.275 69.193  117.239 1.00 21.63 ? 679  LEU   A CD2   1 
ATOM   5007  N  N     . ARG   A  1  682  ? -23.493 64.681  114.336 1.00 17.80 ? 680  ARG   A N     1 
ATOM   5008  C  CA    . ARG   A  1  682  ? -23.283 63.242  114.410 1.00 19.49 ? 680  ARG   A CA    1 
ATOM   5009  C  C     . ARG   A  1  682  ? -21.899 62.849  113.921 1.00 19.20 ? 680  ARG   A C     1 
ATOM   5010  O  O     . ARG   A  1  682  ? -21.326 61.881  114.428 1.00 19.15 ? 680  ARG   A O     1 
ATOM   5011  C  CB    . ARG   A  1  682  ? -24.359 62.518  113.613 1.00 18.92 ? 680  ARG   A CB    1 
ATOM   5012  C  CG    . ARG   A  1  682  ? -25.720 62.665  114.230 1.00 19.40 ? 680  ARG   A CG    1 
ATOM   5013  C  CD    . ARG   A  1  682  ? -26.750 62.019  113.354 1.00 20.22 ? 680  ARG   A CD    1 
ATOM   5014  N  NE    . ARG   A  1  682  ? -28.043 62.010  114.018 1.00 20.85 ? 680  ARG   A NE    1 
ATOM   5015  C  CZ    . ARG   A  1  682  ? -29.188 61.821  113.383 1.00 21.25 ? 680  ARG   A CZ    1 
ATOM   5016  N  NH1   . ARG   A  1  682  ? -29.226 61.599  112.084 1.00 22.80 ? 680  ARG   A NH1   1 
ATOM   5017  N  NH2   . ARG   A  1  682  ? -30.322 61.851  114.075 1.00 24.45 ? 680  ARG   A NH2   1 
ATOM   5018  N  N     . TYR   A  1  683  ? -21.352 63.586  112.955 1.00 18.17 ? 681  TYR   A N     1 
ATOM   5019  C  CA    . TYR   A  1  683  ? -20.025 63.262  112.445 1.00 16.41 ? 681  TYR   A CA    1 
ATOM   5020  C  C     . TYR   A  1  683  ? -18.961 63.570  113.482 1.00 20.20 ? 681  TYR   A C     1 
ATOM   5021  O  O     . TYR   A  1  683  ? -18.091 62.739  113.749 1.00 19.20 ? 681  TYR   A O     1 
ATOM   5022  C  CB    . TYR   A  1  683  ? -19.768 64.044  111.165 1.00 18.00 ? 681  TYR   A CB    1 
ATOM   5023  C  CG    . TYR   A  1  683  ? -18.386 63.828  110.624 1.00 17.88 ? 681  TYR   A CG    1 
ATOM   5024  C  CD1   . TYR   A  1  683  ? -18.073 62.661  109.951 1.00 17.23 ? 681  TYR   A CD1   1 
ATOM   5025  C  CD2   . TYR   A  1  683  ? -17.396 64.782  110.805 1.00 17.50 ? 681  TYR   A CD2   1 
ATOM   5026  C  CE1   . TYR   A  1  683  ? -16.801 62.447  109.457 1.00 18.00 ? 681  TYR   A CE1   1 
ATOM   5027  C  CE2   . TYR   A  1  683  ? -16.126 64.583  110.338 1.00 17.43 ? 681  TYR   A CE2   1 
ATOM   5028  C  CZ    . TYR   A  1  683  ? -15.833 63.415  109.666 1.00 17.56 ? 681  TYR   A CZ    1 
ATOM   5029  O  OH    . TYR   A  1  683  ? -14.554 63.217  109.193 1.00 18.84 ? 681  TYR   A OH    1 
ATOM   5030  N  N     . TYR   A  1  684  ? -19.025 64.749  114.104 1.00 17.65 ? 682  TYR   A N     1 
ATOM   5031  C  CA    . TYR   A  1  684  ? -18.015 65.049  115.115 1.00 17.34 ? 682  TYR   A CA    1 
ATOM   5032  C  C     . TYR   A  1  684  ? -18.187 64.169  116.343 1.00 20.32 ? 682  TYR   A C     1 
ATOM   5033  O  O     . TYR   A  1  684  ? -17.197 63.816  116.989 1.00 19.42 ? 682  TYR   A O     1 
ATOM   5034  C  CB    . TYR   A  1  684  ? -18.021 66.528  115.493 1.00 18.18 ? 682  TYR   A CB    1 
ATOM   5035  C  CG    . TYR   A  1  684  ? -17.643 67.432  114.348 1.00 17.35 ? 682  TYR   A CG    1 
ATOM   5036  C  CD1   . TYR   A  1  684  ? -16.589 67.110  113.499 1.00 17.94 ? 682  TYR   A CD1   1 
ATOM   5037  C  CD2   . TYR   A  1  684  ? -18.360 68.592  114.090 1.00 18.71 ? 682  TYR   A CD2   1 
ATOM   5038  C  CE1   . TYR   A  1  684  ? -16.253 67.936  112.436 1.00 19.63 ? 682  TYR   A CE1   1 
ATOM   5039  C  CE2   . TYR   A  1  684  ? -18.024 69.424  113.047 1.00 17.80 ? 682  TYR   A CE2   1 
ATOM   5040  C  CZ    . TYR   A  1  684  ? -16.982 69.086  112.203 1.00 17.67 ? 682  TYR   A CZ    1 
ATOM   5041  O  OH    . TYR   A  1  684  ? -16.660 69.917  111.162 1.00 18.75 ? 682  TYR   A OH    1 
ATOM   5042  N  N     . ALA   A  1  685  ? -19.417 63.779  116.671 1.00 18.09 ? 683  ALA   A N     1 
ATOM   5043  C  CA    . ALA   A  1  685  ? -19.609 62.817  117.746 1.00 19.32 ? 683  ALA   A CA    1 
ATOM   5044  C  C     . ALA   A  1  685  ? -18.913 61.503  117.420 1.00 20.28 ? 683  ALA   A C     1 
ATOM   5045  O  O     . ALA   A  1  685  ? -18.195 60.945  118.256 1.00 20.30 ? 683  ALA   A O     1 
ATOM   5046  C  CB    . ALA   A  1  685  ? -21.102 62.593  117.995 1.00 20.66 ? 683  ALA   A CB    1 
ATOM   5047  N  N     . GLU   A  1  686  ? -19.116 60.995  116.205 1.00 19.38 ? 684  GLU   A N     1 
ATOM   5048  C  CA    . GLU   A  1  686  ? -18.495 59.725  115.841 1.00 20.46 ? 684  GLU   A CA    1 
ATOM   5049  C  C     . GLU   A  1  686  ? -16.978 59.846  115.769 1.00 18.89 ? 684  GLU   A C     1 
ATOM   5050  O  O     . GLU   A  1  686  ? -16.258 58.964  116.252 1.00 20.08 ? 684  GLU   A O     1 
ATOM   5051  C  CB    . GLU   A  1  686  ? -19.055 59.197  114.528 1.00 23.58 ? 684  GLU   A CB    1 
ATOM   5052  C  CG    . GLU   A  1  686  ? -18.337 57.931  114.034 1.00 26.29 ? 684  GLU   A CG    1 
ATOM   5053  C  CD    . GLU   A  1  686  ? -18.458 56.728  114.979 1.00 30.92 ? 684  GLU   A CD    1 
ATOM   5054  O  OE1   . GLU   A  1  686  ? -19.317 56.719  115.899 1.00 29.66 ? 684  GLU   A OE1   1 
ATOM   5055  O  OE2   . GLU   A  1  686  ? -17.683 55.765  114.788 1.00 33.23 ? 684  GLU   A OE2   1 
ATOM   5056  N  N     . GLN   A  1  687  ? -16.474 60.937  115.196 1.00 17.35 ? 685  GLN   A N     1 
ATOM   5057  C  CA    . GLN   A  1  687  ? -15.027 61.117  115.134 1.00 18.57 ? 685  GLN   A CA    1 
ATOM   5058  C  C     . GLN   A  1  687  ? -14.438 61.178  116.534 1.00 19.77 ? 685  GLN   A C     1 
ATOM   5059  O  O     . GLN   A  1  687  ? -13.328 60.688  116.776 1.00 20.77 ? 685  GLN   A O     1 
ATOM   5060  C  CB    . GLN   A  1  687  ? -14.698 62.384  114.360 1.00 18.41 ? 685  GLN   A CB    1 
ATOM   5061  C  CG    . GLN   A  1  687  ? -15.033 62.263  112.872 1.00 18.76 ? 685  GLN   A CG    1 
ATOM   5062  C  CD    . GLN   A  1  687  ? -14.284 61.120  112.221 1.00 22.36 ? 685  GLN   A CD    1 
ATOM   5063  O  OE1   . GLN   A  1  687  ? -13.065 61.058  112.304 1.00 21.09 ? 685  GLN   A OE1   1 
ATOM   5064  N  NE2   . GLN   A  1  687  ? -15.009 60.204  111.589 1.00 25.30 ? 685  GLN   A NE2   1 
ATOM   5065  N  N     . THR   A  1  688  ? -15.166 61.783  117.467 1.00 18.36 ? 686  THR   A N     1 
ATOM   5066  C  CA    . THR   A  1  688  ? -14.715 61.815  118.848 1.00 17.86 ? 686  THR   A CA    1 
ATOM   5067  C  C     . THR   A  1  688  ? -14.620 60.408  119.413 1.00 20.80 ? 686  THR   A C     1 
ATOM   5068  O  O     . THR   A  1  688  ? -13.614 60.041  120.031 1.00 21.24 ? 686  THR   A O     1 
ATOM   5069  C  CB    . THR   A  1  688  ? -15.681 62.658  119.679 1.00 19.86 ? 686  THR   A CB    1 
ATOM   5070  O  OG1   . THR   A  1  688  ? -15.524 64.025  119.305 1.00 20.39 ? 686  THR   A OG1   1 
ATOM   5071  C  CG2   . THR   A  1  688  ? -15.376 62.514  121.158 1.00 20.82 ? 686  THR   A CG2   1 
ATOM   5072  N  N     . ARG   A  1  689  ? -15.657 59.602  119.202 1.00 20.95 ? 687  ARG   A N     1 
ATOM   5073  C  CA    . ARG   A  1  689  ? -15.650 58.242  119.724 1.00 22.17 ? 687  ARG   A CA    1 
ATOM   5074  C  C     . ARG   A  1  689  ? -14.546 57.413  119.098 1.00 21.36 ? 687  ARG   A C     1 
ATOM   5075  O  O     . ARG   A  1  689  ? -14.088 56.441  119.707 1.00 23.96 ? 687  ARG   A O     1 
ATOM   5076  C  CB    . ARG   A  1  689  ? -16.998 57.574  119.480 1.00 20.68 ? 687  ARG   A CB    1 
ATOM   5077  C  CG    . ARG   A  1  689  ? -18.112 58.157  120.331 1.00 23.34 ? 687  ARG   A CG    1 
ATOM   5078  C  CD    . ARG   A  1  689  ? -19.383 57.341  120.169 1.00 26.38 ? 687  ARG   A CD    1 
ATOM   5079  N  NE    . ARG   A  1  689  ? -19.932 57.463  118.826 1.00 27.28 ? 687  ARG   A NE    1 
ATOM   5080  C  CZ    . ARG   A  1  689  ? -20.920 58.282  118.498 1.00 28.36 ? 687  ARG   A CZ    1 
ATOM   5081  N  NH1   . ARG   A  1  689  ? -21.498 59.060  119.398 1.00 27.34 ? 687  ARG   A NH1   1 
ATOM   5082  N  NH2   . ARG   A  1  689  ? -21.341 58.317  117.239 1.00 27.85 ? 687  ARG   A NH2   1 
ATOM   5083  N  N     . ARG   A  1  690  ? -14.109 57.775  117.895 1.00 19.77 ? 688  ARG   A N     1 
ATOM   5084  C  CA    . ARG   A  1  690  ? -13.006 57.066  117.265 1.00 21.67 ? 688  ARG   A CA    1 
ATOM   5085  C  C     . ARG   A  1  690  ? -11.636 57.502  117.768 1.00 21.22 ? 688  ARG   A C     1 
ATOM   5086  O  O     . ARG   A  1  690  ? -10.672 56.749  117.594 1.00 22.08 ? 688  ARG   A O     1 
ATOM   5087  C  CB    . ARG   A  1  690  ? -13.039 57.280  115.752 1.00 21.49 ? 688  ARG   A CB    1 
ATOM   5088  C  CG    . ARG   A  1  690  ? -14.254 56.664  115.077 1.00 22.69 ? 688  ARG   A CG    1 
ATOM   5089  C  CD    . ARG   A  1  690  ? -14.149 55.145  114.984 1.00 25.19 ? 688  ARG   A CD    1 
ATOM   5090  N  NE    . ARG   A  1  690  ? -12.980 54.723  114.213 1.00 24.31 ? 688  ARG   A NE    1 
ATOM   5091  C  CZ    . ARG   A  1  690  ? -11.948 54.070  114.724 1.00 28.06 ? 688  ARG   A CZ    1 
ATOM   5092  N  NH1   . ARG   A  1  690  ? -11.912 53.724  116.001 1.00 26.04 ? 688  ARG   A NH1   1 
ATOM   5093  N  NH2   . ARG   A  1  690  ? -10.930 53.755  113.933 1.00 24.87 ? 688  ARG   A NH2   1 
ATOM   5094  N  N     . THR   A  1  691  ? -11.511 58.694  118.364 1.00 19.87 ? 689  THR   A N     1 
ATOM   5095  C  CA    . THR   A  1  691  ? -10.175 59.261  118.539 1.00 20.74 ? 689  THR   A CA    1 
ATOM   5096  C  C     . THR   A  1  691  ? -9.813  59.773  119.924 1.00 22.70 ? 689  THR   A C     1 
ATOM   5097  O  O     . THR   A  1  691  ? -8.703  59.510  120.393 1.00 25.78 ? 689  THR   A O     1 
ATOM   5098  C  CB    . THR   A  1  691  ? -9.929  60.415  117.571 1.00 20.36 ? 689  THR   A CB    1 
ATOM   5099  O  OG1   . THR   A  1  691  ? -10.937 61.417  117.756 1.00 20.94 ? 689  THR   A OG1   1 
ATOM   5100  C  CG2   . THR   A  1  691  ? -9.942  59.924  116.128 1.00 21.68 ? 689  THR   A CG2   1 
ATOM   5101  N  N     . LEU   A  1  692  ? -10.694 60.517  120.590 1.00 20.46 ? 690  LEU   A N     1 
ATOM   5102  C  CA    . LEU   A  1  692  ? -10.234 61.348  121.700 1.00 23.11 ? 690  LEU   A CA    1 
ATOM   5103  C  C     . LEU   A  1  692  ? -10.030 60.550  122.984 1.00 24.33 ? 690  LEU   A C     1 
ATOM   5104  O  O     . LEU   A  1  692  ? -10.909 59.797  123.415 1.00 25.60 ? 690  LEU   A O     1 
ATOM   5105  C  CB    . LEU   A  1  692  ? -11.183 62.527  121.926 1.00 22.86 ? 690  LEU   A CB    1 
ATOM   5106  C  CG    . LEU   A  1  692  ? -11.223 63.540  120.778 1.00 23.83 ? 690  LEU   A CG    1 
ATOM   5107  C  CD1   . LEU   A  1  692  ? -12.001 64.773  121.198 1.00 27.14 ? 690  LEU   A CD1   1 
ATOM   5108  C  CD2   . LEU   A  1  692  ? -9.821  63.923  120.338 1.00 25.47 ? 690  LEU   A CD2   1 
ATOM   5109  N  N     . GLY   A  1  693  ? -8.858  60.729  123.583 1.00 24.80 ? 691  GLY   A N     1 
ATOM   5110  C  CA    . GLY   A  1  693  ? -8.508  60.099  124.829 1.00 28.25 ? 691  GLY   A CA    1 
ATOM   5111  C  C     . GLY   A  1  693  ? -7.914  61.103  125.796 1.00 27.33 ? 691  GLY   A C     1 
ATOM   5112  O  O     . GLY   A  1  693  ? -7.845  62.306  125.515 1.00 28.15 ? 691  GLY   A O     1 
ATOM   5113  N  N     . PRO   A  1  694  ? -7.452  60.615  126.949 1.00 29.21 ? 692  PRO   A N     1 
ATOM   5114  C  CA    . PRO   A  1  694  ? -6.978  61.526  128.009 1.00 29.11 ? 692  PRO   A CA    1 
ATOM   5115  C  C     . PRO   A  1  694  ? -5.830  62.427  127.587 1.00 31.63 ? 692  PRO   A C     1 
ATOM   5116  O  O     . PRO   A  1  694  ? -5.718  63.552  128.094 1.00 35.44 ? 692  PRO   A O     1 
ATOM   5117  C  CB    . PRO   A  1  694  ? -6.548  60.567  129.127 1.00 34.93 ? 692  PRO   A CB    1 
ATOM   5118  C  CG    . PRO   A  1  694  ? -7.311  59.307  128.879 1.00 31.87 ? 692  PRO   A CG    1 
ATOM   5119  C  CD    . PRO   A  1  694  ? -7.511  59.209  127.386 1.00 30.25 ? 692  PRO   A CD    1 
ATOM   5120  N  N     . GLY   A  1  695  ? -4.971  61.969  126.677 1.00 28.46 ? 693  GLY   A N     1 
ATOM   5121  C  CA    . GLY   A  1  695  ? -3.831  62.755  126.256 1.00 31.99 ? 693  GLY   A CA    1 
ATOM   5122  C  C     . GLY   A  1  695  ? -4.118  63.832  125.238 1.00 30.59 ? 693  GLY   A C     1 
ATOM   5123  O  O     . GLY   A  1  695  ? -3.214  64.602  124.907 1.00 30.32 ? 693  GLY   A O     1 
ATOM   5124  N  N     . HIS   A  1  696  ? -5.344  63.907  124.713 1.00 28.95 ? 694  HIS   A N     1 
ATOM   5125  C  CA    . HIS   A  1  696  ? -5.694  64.938  123.737 1.00 26.37 ? 694  HIS   A CA    1 
ATOM   5126  C  C     . HIS   A  1  696  ? -6.435  66.027  124.497 1.00 28.48 ? 694  HIS   A C     1 
ATOM   5127  O  O     . HIS   A  1  696  ? -7.664  66.100  124.517 1.00 32.44 ? 694  HIS   A O     1 
ATOM   5128  C  CB    . HIS   A  1  696  ? -6.515  64.349  122.596 1.00 27.86 ? 694  HIS   A CB    1 
ATOM   5129  C  CG    . HIS   A  1  696  ? -5.949  63.072  122.065 1.00 23.80 ? 694  HIS   A CG    1 
ATOM   5130  N  ND1   . HIS   A  1  696  ? -6.593  61.862  122.204 1.00 25.52 ? 694  HIS   A ND1   1 
ATOM   5131  C  CD2   . HIS   A  1  696  ? -4.773  62.807  121.450 1.00 26.07 ? 694  HIS   A CD2   1 
ATOM   5132  C  CE1   . HIS   A  1  696  ? -5.850  60.910  121.667 1.00 24.48 ? 694  HIS   A CE1   1 
ATOM   5133  N  NE2   . HIS   A  1  696  ? -4.740  61.457  121.207 1.00 26.82 ? 694  HIS   A NE2   1 
ATOM   5134  N  N     . GLY   A  1  697  ? -5.654  66.864  125.169 1.00 28.89 ? 695  GLY   A N     1 
ATOM   5135  C  CA    . GLY   A  1  697  ? -6.222  67.872  126.027 1.00 27.22 ? 695  GLY   A CA    1 
ATOM   5136  C  C     . GLY   A  1  697  ? -6.808  69.008  125.221 1.00 24.07 ? 695  GLY   A C     1 
ATOM   5137  O  O     . GLY   A  1  697  ? -6.295  69.373  124.163 1.00 25.25 ? 695  GLY   A O     1 
ATOM   5138  N  N     . PRO   A  1  698  ? -7.889  69.598  125.707 1.00 26.74 ? 696  PRO   A N     1 
ATOM   5139  C  CA    . PRO   A  1  698  ? -8.482  70.730  124.992 1.00 26.93 ? 696  PRO   A CA    1 
ATOM   5140  C  C     . PRO   A  1  698  ? -7.546  71.929  124.984 1.00 24.02 ? 696  PRO   A C     1 
ATOM   5141  O  O     . PRO   A  1  698  ? -6.671  72.074  125.841 1.00 26.11 ? 696  PRO   A O     1 
ATOM   5142  C  CB    . PRO   A  1  698  ? -9.746  71.029  125.802 1.00 29.09 ? 696  PRO   A CB    1 
ATOM   5143  C  CG    . PRO   A  1  698  ? -9.444  70.539  127.151 1.00 36.19 ? 696  PRO   A CG    1 
ATOM   5144  C  CD    . PRO   A  1  698  ? -8.606  69.303  126.955 1.00 34.46 ? 696  PRO   A CD    1 
ATOM   5145  N  N     . LEU   A  1  699  ? -7.719  72.782  123.976 1.00 24.03 ? 697  LEU   A N     1 
ATOM   5146  C  CA    . LEU   A  1  699  ? -6.995  74.050  123.952 1.00 24.75 ? 697  LEU   A CA    1 
ATOM   5147  C  C     . LEU   A  1  699  ? -7.419  74.959  125.093 1.00 25.08 ? 697  LEU   A C     1 
ATOM   5148  O  O     . LEU   A  1  699  ? -6.580  75.619  125.713 1.00 27.14 ? 697  LEU   A O     1 
ATOM   5149  C  CB    . LEU   A  1  699  ? -7.245  74.768  122.633 1.00 22.02 ? 697  LEU   A CB    1 
ATOM   5150  C  CG    . LEU   A  1  699  ? -6.754  74.084  121.368 1.00 25.28 ? 697  LEU   A CG    1 
ATOM   5151  C  CD1   . LEU   A  1  699  ? -7.177  74.937  120.179 1.00 23.37 ? 697  LEU   A CD1   1 
ATOM   5152  C  CD2   . LEU   A  1  699  ? -5.243  73.897  121.419 1.00 26.67 ? 697  LEU   A CD2   1 
ATOM   5153  N  N     . GLY   A  1  700  ? -8.716  75.015  125.381 1.00 24.26 ? 698  GLY   A N     1 
ATOM   5154  C  CA    . GLY   A  1  700  ? -9.263  76.007  126.276 1.00 23.90 ? 698  GLY   A CA    1 
ATOM   5155  C  C     . GLY   A  1  700  ? -10.406 76.721  125.588 1.00 23.38 ? 698  GLY   A C     1 
ATOM   5156  O  O     . GLY   A  1  700  ? -10.977 76.215  124.614 1.00 25.52 ? 698  GLY   A O     1 
ATOM   5157  N  N     . PRO   A  1  701  ? -10.766 77.911  126.067 1.00 24.49 ? 699  PRO   A N     1 
ATOM   5158  C  CA    . PRO   A  1  701  ? -11.889 78.633  125.455 1.00 25.74 ? 699  PRO   A CA    1 
ATOM   5159  C  C     . PRO   A  1  701  ? -11.637 78.872  123.976 1.00 23.85 ? 699  PRO   A C     1 
ATOM   5160  O  O     . PRO   A  1  701  ? -10.579 79.360  123.572 1.00 23.70 ? 699  PRO   A O     1 
ATOM   5161  C  CB    . PRO   A  1  701  ? -11.930 79.948  126.238 1.00 26.61 ? 699  PRO   A CB    1 
ATOM   5162  C  CG    . PRO   A  1  701  ? -11.338 79.591  127.579 1.00 26.42 ? 699  PRO   A CG    1 
ATOM   5163  C  CD    . PRO   A  1  701  ? -10.249 78.603  127.260 1.00 23.56 ? 699  PRO   A CD    1 
ATOM   5164  N  N     . ILE   A  1  702  ? -12.606 78.491  123.162 1.00 22.85 ? 700  ILE   A N     1 
ATOM   5165  C  CA    A ILE   A  1  702  ? -12.521 78.672  121.723 0.57 22.20 ? 700  ILE   A CA    1 
ATOM   5166  C  CA    B ILE   A  1  702  ? -12.537 78.648  121.715 0.43 22.20 ? 700  ILE   A CA    1 
ATOM   5167  C  C     . ILE   A  1  702  ? -13.586 79.665  121.294 1.00 21.35 ? 700  ILE   A C     1 
ATOM   5168  O  O     . ILE   A  1  702  ? -14.753 79.555  121.686 1.00 22.60 ? 700  ILE   A O     1 
ATOM   5169  C  CB    A ILE   A  1  702  ? -12.627 77.335  120.975 0.57 21.72 ? 700  ILE   A CB    1 
ATOM   5170  C  CB    B ILE   A  1  702  ? -12.770 77.309  120.999 0.43 21.54 ? 700  ILE   A CB    1 
ATOM   5171  C  CG1   A ILE   A  1  702  ? -11.326 76.548  121.169 0.57 21.37 ? 700  ILE   A CG1   1 
ATOM   5172  C  CG1   B ILE   A  1  702  ? -11.717 76.288  121.428 0.43 22.89 ? 700  ILE   A CG1   1 
ATOM   5173  C  CG2   A ILE   A  1  702  ? -12.885 77.569  119.491 0.57 22.74 ? 700  ILE   A CG2   1 
ATOM   5174  C  CG2   B ILE   A  1  702  ? -12.730 77.498  119.487 0.43 22.76 ? 700  ILE   A CG2   1 
ATOM   5175  C  CD1   A ILE   A  1  702  ? -11.285 75.236  120.450 0.57 20.55 ? 700  ILE   A CD1   1 
ATOM   5176  C  CD1   B ILE   A  1  702  ? -10.320 76.659  121.043 0.43 22.45 ? 700  ILE   A CD1   1 
ATOM   5177  N  N     . VAL   A  1  703  ? -13.175 80.648  120.512 1.00 22.34 ? 701  VAL   A N     1 
ATOM   5178  C  CA    . VAL   A  1  703  ? -14.083 81.637  119.956 1.00 21.79 ? 701  VAL   A CA    1 
ATOM   5179  C  C     . VAL   A  1  703  ? -14.516 81.114  118.598 1.00 20.81 ? 701  VAL   A C     1 
ATOM   5180  O  O     . VAL   A  1  703  ? -13.673 80.846  117.744 1.00 21.01 ? 701  VAL   A O     1 
ATOM   5181  C  CB    . VAL   A  1  703  ? -13.372 82.992  119.839 1.00 22.69 ? 701  VAL   A CB    1 
ATOM   5182  C  CG1   . VAL   A  1  703  ? -14.204 83.970  119.062 1.00 23.17 ? 701  VAL   A CG1   1 
ATOM   5183  C  CG2   . VAL   A  1  703  ? -13.099 83.534  121.244 1.00 24.79 ? 701  VAL   A CG2   1 
ATOM   5184  N  N     . CYS   A  1  704  ? -15.817 80.910  118.417 1.00 18.94 ? 702  CYS   A N     1 
ATOM   5185  C  CA    . CYS   A  1  704  ? -16.377 80.428  117.159 1.00 20.67 ? 702  CYS   A CA    1 
ATOM   5186  C  C     . CYS   A  1  704  ? -17.133 81.580  116.526 1.00 21.16 ? 702  CYS   A C     1 
ATOM   5187  O  O     . CYS   A  1  704  ? -18.145 82.042  117.063 1.00 20.84 ? 702  CYS   A O     1 
ATOM   5188  C  CB    . CYS   A  1  704  ? -17.300 79.233  117.371 1.00 21.73 ? 702  CYS   A CB    1 
ATOM   5189  S  SG    . CYS   A  1  704  ? -16.471 77.829  118.102 1.00 21.69 ? 702  CYS   A SG    1 
ATOM   5190  N  N     . ILE   A  1  705  ? -16.625 82.049  115.399 1.00 21.00 ? 703  ILE   A N     1 
ATOM   5191  C  CA    . ILE   A  1  705  ? -17.197 83.160  114.666 1.00 21.68 ? 703  ILE   A CA    1 
ATOM   5192  C  C     . ILE   A  1  705  ? -17.682 82.614  113.334 1.00 20.45 ? 703  ILE   A C     1 
ATOM   5193  O  O     . ILE   A  1  705  ? -16.919 81.964  112.602 1.00 19.83 ? 703  ILE   A O     1 
ATOM   5194  C  CB    . ILE   A  1  705  ? -16.147 84.264  114.478 1.00 21.50 ? 703  ILE   A CB    1 
ATOM   5195  C  CG1   . ILE   A  1  705  ? -15.780 84.887  115.826 1.00 21.99 ? 703  ILE   A CG1   1 
ATOM   5196  C  CG2   . ILE   A  1  705  ? -16.661 85.319  113.532 1.00 22.69 ? 703  ILE   A CG2   1 
ATOM   5197  C  CD1   . ILE   A  1  705  ? -14.551 85.761  115.747 1.00 23.93 ? 703  ILE   A CD1   1 
ATOM   5198  N  N     . SER   A  1  706  ? -18.945 82.851  113.032 1.00 21.14 ? 704  SER   A N     1 
ATOM   5199  C  CA    . SER   A  1  706  ? -19.583 82.166  111.922 1.00 19.54 ? 704  SER   A CA    1 
ATOM   5200  C  C     . SER   A  1  706  ? -20.214 83.168  110.973 1.00 19.50 ? 704  SER   A C     1 
ATOM   5201  O  O     . SER   A  1  706  ? -20.535 84.297  111.361 1.00 21.58 ? 704  SER   A O     1 
ATOM   5202  C  CB    . SER   A  1  706  ? -20.636 81.178  112.442 1.00 20.28 ? 704  SER   A CB    1 
ATOM   5203  O  OG    . SER   A  1  706  ? -21.545 81.835  113.294 1.00 21.19 ? 704  SER   A OG    1 
ATOM   5204  N  N     . PRO   A  1  707  ? -20.441 82.763  109.727 1.00 19.88 ? 705  PRO   A N     1 
ATOM   5205  C  CA    . PRO   A  1  707  ? -20.992 83.662  108.714 1.00 20.59 ? 705  PRO   A CA    1 
ATOM   5206  C  C     . PRO   A  1  707  ? -22.518 83.610  108.707 1.00 19.62 ? 705  PRO   A C     1 
ATOM   5207  O  O     . PRO   A  1  707  ? -23.142 82.719  109.282 1.00 21.70 ? 705  PRO   A O     1 
ATOM   5208  C  CB    . PRO   A  1  707  ? -20.447 83.037  107.424 1.00 20.20 ? 705  PRO   A CB    1 
ATOM   5209  C  CG    . PRO   A  1  707  ? -20.491 81.572  107.704 1.00 19.39 ? 705  PRO   A CG    1 
ATOM   5210  C  CD    . PRO   A  1  707  ? -20.086 81.449  109.160 1.00 19.89 ? 705  PRO   A CD    1 
ATOM   5211  N  N     . TRP   A  1  708  ? -23.114 84.575  108.016 1.00 19.64 ? 706  TRP   A N     1 
ATOM   5212  C  CA    . TRP   A  1  708  ? -24.574 84.606  107.990 1.00 20.11 ? 706  TRP   A CA    1 
ATOM   5213  C  C     . TRP   A  1  708  ? -25.163 83.566  107.044 1.00 21.67 ? 706  TRP   A C     1 
ATOM   5214  O  O     . TRP   A  1  708  ? -26.311 83.149  107.237 1.00 22.89 ? 706  TRP   A O     1 
ATOM   5215  C  CB    . TRP   A  1  708  ? -25.092 86.006  107.609 1.00 19.77 ? 706  TRP   A CB    1 
ATOM   5216  C  CG    . TRP   A  1  708  ? -24.946 86.252  106.150 1.00 20.90 ? 706  TRP   A CG    1 
ATOM   5217  C  CD1   . TRP   A  1  708  ? -23.910 86.869  105.530 1.00 23.57 ? 706  TRP   A CD1   1 
ATOM   5218  C  CD2   . TRP   A  1  708  ? -25.840 85.822  105.114 1.00 21.67 ? 706  TRP   A CD2   1 
ATOM   5219  N  NE1   . TRP   A  1  708  ? -24.096 86.856  104.170 1.00 21.92 ? 706  TRP   A NE1   1 
ATOM   5220  C  CE2   . TRP   A  1  708  ? -25.279 86.219  103.891 1.00 21.00 ? 706  TRP   A CE2   1 
ATOM   5221  C  CE3   . TRP   A  1  708  ? -27.071 85.156  105.112 1.00 20.63 ? 706  TRP   A CE3   1 
ATOM   5222  C  CZ2   . TRP   A  1  708  ? -25.892 85.962  102.667 1.00 21.57 ? 706  TRP   A CZ2   1 
ATOM   5223  C  CZ3   . TRP   A  1  708  ? -27.673 84.882  103.893 1.00 21.45 ? 706  TRP   A CZ3   1 
ATOM   5224  C  CH2   . TRP   A  1  708  ? -27.085 85.298  102.689 1.00 20.86 ? 706  TRP   A CH2   1 
ATOM   5225  N  N     . ASN   A  1  709  ? -24.412 83.126  106.041 1.00 19.61 ? 707  ASN   A N     1 
ATOM   5226  C  CA    . ASN   A  1  709  ? -25.058 82.510  104.888 1.00 20.55 ? 707  ASN   A CA    1 
ATOM   5227  C  C     . ASN   A  1  709  ? -25.410 81.047  105.100 1.00 23.51 ? 707  ASN   A C     1 
ATOM   5228  O  O     . ASN   A  1  709  ? -26.293 80.531  104.408 1.00 21.37 ? 707  ASN   A O     1 
ATOM   5229  C  CB    . ASN   A  1  709  ? -24.180 82.672  103.658 1.00 21.88 ? 707  ASN   A CB    1 
ATOM   5230  C  CG    . ASN   A  1  709  ? -22.961 81.815  103.725 1.00 22.41 ? 707  ASN   A CG    1 
ATOM   5231  O  OD1   . ASN   A  1  709  ? -22.100 82.024  104.570 1.00 23.30 ? 707  ASN   A OD1   1 
ATOM   5232  N  ND2   . ASN   A  1  709  ? -22.876 80.832  102.842 1.00 22.18 ? 707  ASN   A ND2   1 
ATOM   5233  N  N     . PHE   A  1  710  ? -24.725 80.364  106.007 1.00 21.61 ? 708  PHE   A N     1 
ATOM   5234  C  CA    . PHE   A  1  710  ? -25.111 79.037  106.469 1.00 21.29 ? 708  PHE   A CA    1 
ATOM   5235  C  C     . PHE   A  1  710  ? -25.315 79.201  107.966 1.00 21.93 ? 708  PHE   A C     1 
ATOM   5236  O  O     . PHE   A  1  710  ? -24.493 78.747  108.775 1.00 22.26 ? 708  PHE   A O     1 
ATOM   5237  C  CB    . PHE   A  1  710  ? -24.038 77.993  106.169 1.00 20.91 ? 708  PHE   A CB    1 
ATOM   5238  C  CG    . PHE   A  1  710  ? -23.771 77.785  104.693 1.00 24.84 ? 708  PHE   A CG    1 
ATOM   5239  C  CD1   . PHE   A  1  710  ? -24.804 77.769  103.775 1.00 25.13 ? 708  PHE   A CD1   1 
ATOM   5240  C  CD2   . PHE   A  1  710  ? -22.471 77.597  104.233 1.00 23.93 ? 708  PHE   A CD2   1 
ATOM   5241  C  CE1   . PHE   A  1  710  ? -24.554 77.570  102.425 1.00 25.94 ? 708  PHE   A CE1   1 
ATOM   5242  C  CE2   . PHE   A  1  710  ? -22.212 77.394  102.878 1.00 26.11 ? 708  PHE   A CE2   1 
ATOM   5243  C  CZ    . PHE   A  1  710  ? -23.257 77.385  101.977 1.00 29.47 ? 708  PHE   A CZ    1 
ATOM   5244  N  N     . PRO   A  1  711  ? -26.404 79.866  108.364 1.00 21.32 ? 709  PRO   A N     1 
ATOM   5245  C  CA    . PRO   A  1  711  ? -26.493 80.415  109.723 1.00 22.10 ? 709  PRO   A CA    1 
ATOM   5246  C  C     . PRO   A  1  711  ? -26.736 79.384  110.798 1.00 21.69 ? 709  PRO   A C     1 
ATOM   5247  O  O     . PRO   A  1  711  ? -26.601 79.710  111.985 1.00 23.10 ? 709  PRO   A O     1 
ATOM   5248  C  CB    . PRO   A  1  711  ? -27.681 81.373  109.622 1.00 22.86 ? 709  PRO   A CB    1 
ATOM   5249  C  CG    . PRO   A  1  711  ? -28.545 80.736  108.583 1.00 21.78 ? 709  PRO   A CG    1 
ATOM   5250  C  CD    . PRO   A  1  711  ? -27.594 80.184  107.558 1.00 21.11 ? 709  PRO   A CD    1 
ATOM   5251  N  N     . LEU   A  1  712  ? -27.137 78.172  110.440 1.00 21.61 ? 710  LEU   A N     1 
ATOM   5252  C  CA    . LEU   A  1  712  ? -27.220 77.090  111.402 1.00 20.77 ? 710  LEU   A CA    1 
ATOM   5253  C  C     . LEU   A  1  712  ? -26.131 76.055  111.206 1.00 20.15 ? 710  LEU   A C     1 
ATOM   5254  O  O     . LEU   A  1  712  ? -25.529 75.617  112.179 1.00 19.71 ? 710  LEU   A O     1 
ATOM   5255  C  CB    . LEU   A  1  712  ? -28.590 76.408  111.337 1.00 20.76 ? 710  LEU   A CB    1 
ATOM   5256  C  CG    . LEU   A  1  712  ? -28.734 75.292  112.369 1.00 22.94 ? 710  LEU   A CG    1 
ATOM   5257  C  CD1   . LEU   A  1  712  ? -28.705 75.856  113.795 1.00 22.21 ? 710  LEU   A CD1   1 
ATOM   5258  C  CD2   . LEU   A  1  712  ? -30.011 74.499  112.113 1.00 22.47 ? 710  LEU   A CD2   1 
ATOM   5259  N  N     . ALA   A  1  713  ? -25.827 75.689  109.964 1.00 19.17 ? 711  ALA   A N     1 
ATOM   5260  C  CA    . ALA   A  1  713  ? -24.943 74.550  109.750 1.00 18.19 ? 711  ALA   A CA    1 
ATOM   5261  C  C     . ALA   A  1  713  ? -23.510 74.864  110.146 1.00 19.20 ? 711  ALA   A C     1 
ATOM   5262  O  O     . ALA   A  1  713  ? -22.897 74.115  110.912 1.00 20.31 ? 711  ALA   A O     1 
ATOM   5263  C  CB    . ALA   A  1  713  ? -25.009 74.099  108.300 1.00 20.10 ? 711  ALA   A CB    1 
ATOM   5264  N  N     . ILE   A  1  714  ? -22.943 75.942  109.615 1.00 18.42 ? 712  ILE   A N     1 
ATOM   5265  C  CA    . ILE   A  1  714  ? -21.553 76.240  109.954 1.00 19.72 ? 712  ILE   A CA    1 
ATOM   5266  C  C     . ILE   A  1  714  ? -21.456 76.659  111.406 1.00 19.86 ? 712  ILE   A C     1 
ATOM   5267  O  O     . ILE   A  1  714  ? -20.525 76.277  112.127 1.00 20.98 ? 712  ILE   A O     1 
ATOM   5268  C  CB    . ILE   A  1  714  ? -20.981 77.297  109.001 1.00 19.96 ? 712  ILE   A CB    1 
ATOM   5269  C  CG1   . ILE   A  1  714  ? -20.887 76.677  107.599 1.00 22.14 ? 712  ILE   A CG1   1 
ATOM   5270  C  CG2   . ILE   A  1  714  ? -19.625 77.819  109.513 1.00 21.89 ? 712  ILE   A CG2   1 
ATOM   5271  C  CD1   . ILE   A  1  714  ? -19.857 77.282  106.722 1.00 31.31 ? 712  ILE   A CD1   1 
ATOM   5272  N  N     . PHE   A  1  715  ? -22.419 77.453  111.854 1.00 19.15 ? 713  PHE   A N     1 
ATOM   5273  C  CA    . PHE   A  1  715  ? -22.497 77.815  113.259 1.00 20.05 ? 713  PHE   A CA    1 
ATOM   5274  C  C     . PHE   A  1  715  ? -22.425 76.575  114.141 1.00 22.15 ? 713  PHE   A C     1 
ATOM   5275  O  O     . PHE   A  1  715  ? -21.597 76.488  115.058 1.00 20.55 ? 713  PHE   A O     1 
ATOM   5276  C  CB    . PHE   A  1  715  ? -23.822 78.540  113.469 1.00 21.67 ? 713  PHE   A CB    1 
ATOM   5277  C  CG    . PHE   A  1  715  ? -24.065 78.932  114.874 1.00 19.81 ? 713  PHE   A CG    1 
ATOM   5278  C  CD1   . PHE   A  1  715  ? -23.450 80.053  115.393 1.00 21.53 ? 713  PHE   A CD1   1 
ATOM   5279  C  CD2   . PHE   A  1  715  ? -24.893 78.169  115.700 1.00 20.71 ? 713  PHE   A CD2   1 
ATOM   5280  C  CE1   . PHE   A  1  715  ? -23.670 80.428  116.710 1.00 23.47 ? 713  PHE   A CE1   1 
ATOM   5281  C  CE2   . PHE   A  1  715  ? -25.105 78.528  117.005 1.00 22.30 ? 713  PHE   A CE2   1 
ATOM   5282  C  CZ    . PHE   A  1  715  ? -24.501 79.667  117.518 1.00 24.62 ? 713  PHE   A CZ    1 
ATOM   5283  N  N     . THR   A  1  716  ? -23.282 75.592  113.864 1.00 19.49 ? 714  THR   A N     1 
ATOM   5284  C  CA    . THR   A  1  716  ? -23.325 74.386  114.685 1.00 20.62 ? 714  THR   A CA    1 
ATOM   5285  C  C     . THR   A  1  716  ? -22.054 73.573  114.523 1.00 20.76 ? 714  THR   A C     1 
ATOM   5286  O  O     . THR   A  1  716  ? -21.528 73.040  115.504 1.00 19.32 ? 714  THR   A O     1 
ATOM   5287  C  CB    . THR   A  1  716  ? -24.531 73.543  114.271 1.00 20.57 ? 714  THR   A CB    1 
ATOM   5288  O  OG1   . THR   A  1  716  ? -25.730 74.285  114.525 1.00 22.03 ? 714  THR   A OG1   1 
ATOM   5289  C  CG2   . THR   A  1  716  ? -24.587 72.246  115.056 1.00 22.04 ? 714  THR   A CG2   1 
ATOM   5290  N  N     . GLY   A  1  717  ? -21.545 73.480  113.298 1.00 17.91 ? 715  GLY   A N     1 
ATOM   5291  C  CA    . GLY   A  1  717  ? -20.373 72.657  113.059 1.00 18.97 ? 715  GLY   A CA    1 
ATOM   5292  C  C     . GLY   A  1  717  ? -19.175 73.111  113.869 1.00 18.35 ? 715  GLY   A C     1 
ATOM   5293  O  O     . GLY   A  1  717  ? -18.535 72.314  114.547 1.00 19.66 ? 715  GLY   A O     1 
ATOM   5294  N  N     . GLN   A  1  718  ? -18.864 74.407  113.817 1.00 18.88 ? 716  GLN   A N     1 
ATOM   5295  C  CA    . GLN   A  1  718  ? -17.691 74.890  114.548 1.00 19.27 ? 716  GLN   A CA    1 
ATOM   5296  C  C     . GLN   A  1  718  ? -17.856 74.668  116.037 1.00 21.03 ? 716  GLN   A C     1 
ATOM   5297  O  O     . GLN   A  1  718  ? -16.940 74.200  116.722 1.00 20.23 ? 716  GLN   A O     1 
ATOM   5298  C  CB    . GLN   A  1  718  ? -17.467 76.373  114.275 1.00 18.33 ? 716  GLN   A CB    1 
ATOM   5299  C  CG    . GLN   A  1  718  ? -17.127 76.661  112.844 1.00 18.23 ? 716  GLN   A CG    1 
ATOM   5300  C  CD    . GLN   A  1  718  ? -16.728 78.096  112.595 1.00 21.16 ? 716  GLN   A CD    1 
ATOM   5301  O  OE1   . GLN   A  1  718  ? -15.778 78.352  111.854 1.00 21.63 ? 716  GLN   A OE1   1 
ATOM   5302  N  NE2   . GLN   A  1  718  ? -17.444 79.042  113.199 1.00 21.00 ? 716  GLN   A NE2   1 
ATOM   5303  N  N     . ILE   A  1  719  ? -19.016 75.036  116.565 1.00 19.98 ? 717  ILE   A N     1 
ATOM   5304  C  CA    . ILE   A  1  719  ? -19.249 74.927  117.998 1.00 19.88 ? 717  ILE   A CA    1 
ATOM   5305  C  C     . ILE   A  1  719  ? -19.242 73.472  118.440 1.00 20.15 ? 717  ILE   A C     1 
ATOM   5306  O  O     . ILE   A  1  719  ? -18.691 73.138  119.498 1.00 21.11 ? 717  ILE   A O     1 
ATOM   5307  C  CB    . ILE   A  1  719  ? -20.580 75.611  118.353 1.00 23.08 ? 717  ILE   A CB    1 
ATOM   5308  C  CG1   . ILE   A  1  719  ? -20.483 77.119  118.170 1.00 22.12 ? 717  ILE   A CG1   1 
ATOM   5309  C  CG2   . ILE   A  1  719  ? -21.020 75.248  119.747 1.00 28.13 ? 717  ILE   A CG2   1 
ATOM   5310  C  CD1   . ILE   A  1  719  ? -21.836 77.738  118.005 1.00 27.94 ? 717  ILE   A CD1   1 
ATOM   5311  N  N     . ALA   A  1  720  ? -19.878 72.592  117.663 1.00 20.55 ? 718  ALA   A N     1 
ATOM   5312  C  CA    . ALA   A  1  720  ? -19.945 71.190  118.053 1.00 20.89 ? 718  ALA   A CA    1 
ATOM   5313  C  C     . ALA   A  1  720  ? -18.555 70.589  118.109 1.00 19.66 ? 718  ALA   A C     1 
ATOM   5314  O  O     . ALA   A  1  720  ? -18.230 69.854  119.041 1.00 20.37 ? 718  ALA   A O     1 
ATOM   5315  C  CB    . ALA   A  1  720  ? -20.809 70.414  117.050 1.00 20.68 ? 718  ALA   A CB    1 
ATOM   5316  N  N     . ALA   A  1  721  ? -17.733 70.890  117.109 1.00 18.94 ? 719  ALA   A N     1 
ATOM   5317  C  CA    . ALA   A  1  721  ? -16.375 70.370  117.079 1.00 17.37 ? 719  ALA   A CA    1 
ATOM   5318  C  C     . ALA   A  1  721  ? -15.584 70.854  118.284 1.00 19.58 ? 719  ALA   A C     1 
ATOM   5319  O  O     . ALA   A  1  721  ? -14.953 70.058  118.989 1.00 19.76 ? 719  ALA   A O     1 
ATOM   5320  C  CB    . ALA   A  1  721  ? -15.690 70.832  115.802 1.00 19.16 ? 719  ALA   A CB    1 
ATOM   5321  N  N     . ALA   A  1  722  ? -15.647 72.158  118.564 1.00 19.33 ? 720  ALA   A N     1 
ATOM   5322  C  CA    . ALA   A  1  722  ? -14.886 72.698  119.684 1.00 19.53 ? 720  ALA   A CA    1 
ATOM   5323  C  C     . ALA   A  1  722  ? -15.359 72.093  120.999 1.00 21.39 ? 720  ALA   A C     1 
ATOM   5324  O  O     . ALA   A  1  722  ? -14.548 71.672  121.838 1.00 21.37 ? 720  ALA   A O     1 
ATOM   5325  C  CB    . ALA   A  1  722  ? -15.003 74.223  119.704 1.00 20.57 ? 720  ALA   A CB    1 
ATOM   5326  N  N     . LEU   A  1  723  ? -16.680 72.029  121.190 1.00 20.44 ? 721  LEU   A N     1 
ATOM   5327  C  CA    . LEU   A  1  723  ? -17.232 71.468  122.413 1.00 20.23 ? 721  LEU   A CA    1 
ATOM   5328  C  C     . LEU   A  1  723  ? -16.844 70.009  122.581 1.00 21.51 ? 721  LEU   A C     1 
ATOM   5329  O  O     . LEU   A  1  723  ? -16.465 69.575  123.674 1.00 21.49 ? 721  LEU   A O     1 
ATOM   5330  C  CB    . LEU   A  1  723  ? -18.752 71.584  122.393 1.00 22.00 ? 721  LEU   A CB    1 
ATOM   5331  C  CG    . LEU   A  1  723  ? -19.360 72.963  122.581 1.00 20.30 ? 721  LEU   A CG    1 
ATOM   5332  C  CD1   . LEU   A  1  723  ? -20.858 72.850  122.290 1.00 22.80 ? 721  LEU   A CD1   1 
ATOM   5333  C  CD2   . LEU   A  1  723  ? -19.102 73.451  123.994 1.00 22.77 ? 721  LEU   A CD2   1 
ATOM   5334  N  N     . VAL   A  1  724  ? -16.984 69.217  121.524 1.00 22.09 ? 722  VAL   A N     1 
ATOM   5335  C  CA    . VAL   A  1  724  ? -16.769 67.795  121.711 1.00 21.06 ? 722  VAL   A CA    1 
ATOM   5336  C  C     . VAL   A  1  724  ? -15.294 67.511  121.930 1.00 20.57 ? 722  VAL   A C     1 
ATOM   5337  O  O     . VAL   A  1  724  ? -14.937 66.527  122.585 1.00 22.04 ? 722  VAL   A O     1 
ATOM   5338  C  CB    . VAL   A  1  724  ? -17.383 66.994  120.555 1.00 19.93 ? 722  VAL   A CB    1 
ATOM   5339  C  CG1   . VAL   A  1  724  ? -16.458 67.010  119.336 1.00 20.13 ? 722  VAL   A CG1   1 
ATOM   5340  C  CG2   . VAL   A  1  724  ? -17.751 65.597  121.010 1.00 21.15 ? 722  VAL   A CG2   1 
ATOM   5341  N  N     . ALA   A  1  725  ? -14.424 68.383  121.430 1.00 20.61 ? 723  ALA   A N     1 
ATOM   5342  C  CA    . ALA   A  1  725  ? -13.002 68.281  121.725 1.00 21.82 ? 723  ALA   A CA    1 
ATOM   5343  C  C     . ALA   A  1  725  ? -12.677 68.689  123.149 1.00 23.03 ? 723  ALA   A C     1 
ATOM   5344  O  O     . ALA   A  1  725  ? -11.495 68.660  123.526 1.00 23.90 ? 723  ALA   A O     1 
ATOM   5345  C  CB    . ALA   A  1  725  ? -12.202 69.122  120.739 1.00 20.86 ? 723  ALA   A CB    1 
ATOM   5346  N  N     . GLY   A  1  726  ? -13.673 69.073  123.944 1.00 21.81 ? 724  GLY   A N     1 
ATOM   5347  C  CA    . GLY   A  1  726  ? -13.452 69.415  125.331 1.00 22.07 ? 724  GLY   A CA    1 
ATOM   5348  C  C     . GLY   A  1  726  ? -13.246 70.882  125.634 1.00 24.00 ? 724  GLY   A C     1 
ATOM   5349  O  O     . GLY   A  1  726  ? -12.859 71.215  126.770 1.00 25.23 ? 724  GLY   A O     1 
ATOM   5350  N  N     . ASN   A  1  727  ? -13.501 71.766  124.682 1.00 23.22 ? 725  ASN   A N     1 
ATOM   5351  C  CA    . ASN   A  1  727  ? -13.288 73.192  124.849 1.00 23.08 ? 725  ASN   A CA    1 
ATOM   5352  C  C     . ASN   A  1  727  ? -14.602 73.896  125.129 1.00 24.09 ? 725  ASN   A C     1 
ATOM   5353  O  O     . ASN   A  1  727  ? -15.592 73.659  124.432 1.00 24.50 ? 725  ASN   A O     1 
ATOM   5354  C  CB    . ASN   A  1  727  ? -12.726 73.786  123.561 1.00 22.45 ? 725  ASN   A CB    1 
ATOM   5355  C  CG    . ASN   A  1  727  ? -11.501 73.078  123.087 1.00 22.19 ? 725  ASN   A CG    1 
ATOM   5356  O  OD1   . ASN   A  1  727  ? -10.409 73.293  123.610 1.00 24.22 ? 725  ASN   A OD1   1 
ATOM   5357  N  ND2   . ASN   A  1  727  ? -11.662 72.232  122.087 1.00 21.78 ? 725  ASN   A ND2   1 
ATOM   5358  N  N     . PRO   A  1  728  ? -14.643 74.810  126.082 1.00 23.06 ? 726  PRO   A N     1 
ATOM   5359  C  CA    . PRO   A  1  728  ? -15.810 75.681  126.196 1.00 23.69 ? 726  PRO   A CA    1 
ATOM   5360  C  C     . PRO   A  1  728  ? -15.778 76.690  125.067 1.00 22.29 ? 726  PRO   A C     1 
ATOM   5361  O  O     . PRO   A  1  728  ? -14.714 77.058  124.563 1.00 25.39 ? 726  PRO   A O     1 
ATOM   5362  C  CB    . PRO   A  1  728  ? -15.609 76.367  127.548 1.00 23.15 ? 726  PRO   A CB    1 
ATOM   5363  C  CG    . PRO   A  1  728  ? -14.142 76.395  127.722 1.00 24.88 ? 726  PRO   A CG    1 
ATOM   5364  C  CD    . PRO   A  1  728  ? -13.575 75.189  127.018 1.00 23.28 ? 726  PRO   A CD    1 
ATOM   5365  N  N     . VAL   A  1  729  ? -16.962 77.129  124.660 1.00 25.33 ? 727  VAL   A N     1 
ATOM   5366  C  CA    . VAL   A  1  729  ? -17.124 77.875  123.424 1.00 23.21 ? 727  VAL   A CA    1 
ATOM   5367  C  C     . VAL   A  1  729  ? -17.779 79.218  123.690 1.00 22.87 ? 727  VAL   A C     1 
ATOM   5368  O  O     . VAL   A  1  729  ? -18.751 79.314  124.444 1.00 25.08 ? 727  VAL   A O     1 
ATOM   5369  C  CB    . VAL   A  1  729  ? -17.951 77.060  122.413 1.00 22.27 ? 727  VAL   A CB    1 
ATOM   5370  C  CG1   . VAL   A  1  729  ? -18.366 77.927  121.231 1.00 22.51 ? 727  VAL   A CG1   1 
ATOM   5371  C  CG2   . VAL   A  1  729  ? -17.121 75.898  121.921 1.00 24.81 ? 727  VAL   A CG2   1 
ATOM   5372  N  N     . LEU   A  1  730  ? -17.251 80.246  123.038 1.00 22.20 ? 728  LEU   A N     1 
ATOM   5373  C  CA    . LEU   A  1  730  ? -17.907 81.535  122.900 1.00 23.62 ? 728  LEU   A CA    1 
ATOM   5374  C  C     . LEU   A  1  730  ? -18.394 81.580  121.464 1.00 21.33 ? 728  LEU   A C     1 
ATOM   5375  O  O     . LEU   A  1  730  ? -17.583 81.593  120.532 1.00 21.98 ? 728  LEU   A O     1 
ATOM   5376  C  CB    . LEU   A  1  730  ? -16.917 82.670  123.161 1.00 25.57 ? 728  LEU   A CB    1 
ATOM   5377  C  CG    . LEU   A  1  730  ? -16.257 82.750  124.550 1.00 23.03 ? 728  LEU   A CG    1 
ATOM   5378  C  CD1   . LEU   A  1  730  ? -17.290 82.495  125.639 1.00 25.42 ? 728  LEU   A CD1   1 
ATOM   5379  C  CD2   . LEU   A  1  730  ? -15.097 81.802  124.700 1.00 24.53 ? 728  LEU   A CD2   1 
ATOM   5380  N  N     . ALA   A  1  731  ? -19.706 81.559  121.287 1.00 22.64 ? 729  ALA   A N     1 
ATOM   5381  C  CA    . ALA   A  1  731  ? -20.319 81.452  119.970 1.00 23.22 ? 729  ALA   A CA    1 
ATOM   5382  C  C     . ALA   A  1  731  ? -20.763 82.843  119.544 1.00 23.26 ? 729  ALA   A C     1 
ATOM   5383  O  O     . ALA   A  1  731  ? -21.676 83.420  120.139 1.00 24.38 ? 729  ALA   A O     1 
ATOM   5384  C  CB    . ALA   A  1  731  ? -21.502 80.489  120.006 1.00 22.87 ? 729  ALA   A CB    1 
ATOM   5385  N  N     . LYS   A  1  732  ? -20.126 83.373  118.501 1.00 21.65 ? 730  LYS   A N     1 
ATOM   5386  C  CA    . LYS   A  1  732  ? -20.439 84.706  118.000 1.00 21.83 ? 730  LYS   A CA    1 
ATOM   5387  C  C     . LYS   A  1  732  ? -21.041 84.548  116.615 1.00 22.85 ? 730  LYS   A C     1 
ATOM   5388  O  O     . LYS   A  1  732  ? -20.308 84.469  115.623 1.00 22.35 ? 730  LYS   A O     1 
ATOM   5389  C  CB    . LYS   A  1  732  ? -19.174 85.566  117.955 1.00 24.04 ? 730  LYS   A CB    1 
ATOM   5390  C  CG    . LYS   A  1  732  ? -19.396 87.037  118.266 1.00 25.86 ? 730  LYS   A CG    1 
ATOM   5391  C  CD    . LYS   A  1  732  ? -20.382 87.674  117.278 1.00 22.94 ? 730  LYS   A CD    1 
ATOM   5392  C  CE    . LYS   A  1  732  ? -19.743 87.863  115.913 1.00 23.87 ? 730  LYS   A CE    1 
ATOM   5393  N  NZ    . LYS   A  1  732  ? -20.723 88.419  114.934 1.00 24.15 ? 730  LYS   A NZ    1 
ATOM   5394  N  N     . PRO   A  1  733  ? -22.362 84.501  116.492 1.00 21.56 ? 731  PRO   A N     1 
ATOM   5395  C  CA    . PRO   A  1  733  ? -22.971 84.334  115.172 1.00 21.54 ? 731  PRO   A CA    1 
ATOM   5396  C  C     . PRO   A  1  733  ? -22.956 85.651  114.418 1.00 20.92 ? 731  PRO   A C     1 
ATOM   5397  O  O     . PRO   A  1  733  ? -22.841 86.732  114.997 1.00 23.09 ? 731  PRO   A O     1 
ATOM   5398  C  CB    . PRO   A  1  733  ? -24.409 83.942  115.508 1.00 22.47 ? 731  PRO   A CB    1 
ATOM   5399  C  CG    . PRO   A  1  733  ? -24.684 84.687  116.802 1.00 23.77 ? 731  PRO   A CG    1 
ATOM   5400  C  CD    . PRO   A  1  733  ? -23.369 84.642  117.561 1.00 22.94 ? 731  PRO   A CD    1 
ATOM   5401  N  N     . ALA   A  1  734  ? -23.090 85.539  113.100 1.00 20.56 ? 732  ALA   A N     1 
ATOM   5402  C  CA    . ALA   A  1  734  ? -23.144 86.722  112.259 1.00 21.11 ? 732  ALA   A CA    1 
ATOM   5403  C  C     . ALA   A  1  734  ? -24.271 87.644  112.710 1.00 23.13 ? 732  ALA   A C     1 
ATOM   5404  O  O     . ALA   A  1  734  ? -25.337 87.194  113.146 1.00 24.04 ? 732  ALA   A O     1 
ATOM   5405  C  CB    . ALA   A  1  734  ? -23.387 86.297  110.815 1.00 21.83 ? 732  ALA   A CB    1 
ATOM   5406  N  N     . GLU   A  1  735  ? -24.041 88.947  112.587 1.00 24.05 ? 733  GLU   A N     1 
ATOM   5407  C  CA    . GLU   A  1  735  ? -25.045 89.902  113.038 1.00 26.46 ? 733  GLU   A CA    1 
ATOM   5408  C  C     . GLU   A  1  735  ? -26.347 89.786  112.257 1.00 26.96 ? 733  GLU   A C     1 
ATOM   5409  O  O     . GLU   A  1  735  ? -27.405 90.155  112.780 1.00 26.43 ? 733  GLU   A O     1 
ATOM   5410  C  CB    . GLU   A  1  735  ? -24.502 91.329  112.977 1.00 30.20 ? 733  GLU   A CB    1 
ATOM   5411  C  CG    . GLU   A  1  735  ? -23.965 91.767  111.621 1.00 29.48 ? 733  GLU   A CG    1 
ATOM   5412  C  CD    . GLU   A  1  735  ? -22.481 91.460  111.437 1.00 32.52 ? 733  GLU   A CD    1 
ATOM   5413  O  OE1   . GLU   A  1  735  ? -21.972 90.510  112.072 1.00 28.29 ? 733  GLU   A OE1   1 
ATOM   5414  O  OE2   . GLU   A  1  735  ? -21.828 92.175  110.651 1.00 29.52 ? 733  GLU   A OE2   1 
ATOM   5415  N  N     . GLU   A  1  736  ? -26.304 89.264  111.033 1.00 25.42 ? 734  GLU   A N     1 
ATOM   5416  C  CA    . GLU   A  1  736  ? -27.514 89.199  110.230 1.00 22.80 ? 734  GLU   A CA    1 
ATOM   5417  C  C     . GLU   A  1  736  ? -28.442 88.085  110.683 1.00 25.74 ? 734  GLU   A C     1 
ATOM   5418  O  O     . GLU   A  1  736  ? -29.660 88.195  110.503 1.00 26.41 ? 734  GLU   A O     1 
ATOM   5419  C  CB    . GLU   A  1  736  ? -27.149 88.982  108.761 1.00 24.25 ? 734  GLU   A CB    1 
ATOM   5420  C  CG    . GLU   A  1  736  ? -26.323 90.090  108.120 1.00 28.15 ? 734  GLU   A CG    1 
ATOM   5421  C  CD    . GLU   A  1  736  ? -24.825 89.847  108.199 1.00 30.88 ? 734  GLU   A CD    1 
ATOM   5422  O  OE1   . GLU   A  1  736  ? -24.384 89.033  109.039 1.00 26.50 ? 734  GLU   A OE1   1 
ATOM   5423  O  OE2   . GLU   A  1  736  ? -24.083 90.467  107.410 1.00 27.84 ? 734  GLU   A OE2   1 
ATOM   5424  N  N     . THR   A  1  737  ? -27.904 87.008  111.255 1.00 23.90 ? 735  THR   A N     1 
ATOM   5425  C  CA    . THR   A  1  737  ? -28.673 85.787  111.506 1.00 24.03 ? 735  THR   A CA    1 
ATOM   5426  C  C     . THR   A  1  737  ? -28.504 85.275  112.937 1.00 23.11 ? 735  THR   A C     1 
ATOM   5427  O  O     . THR   A  1  737  ? -28.168 84.109  113.158 1.00 23.88 ? 735  THR   A O     1 
ATOM   5428  C  CB    . THR   A  1  737  ? -28.297 84.716  110.484 1.00 21.15 ? 735  THR   A CB    1 
ATOM   5429  O  OG1   . THR   A  1  737  ? -26.872 84.505  110.525 1.00 22.68 ? 735  THR   A OG1   1 
ATOM   5430  C  CG2   . THR   A  1  737  ? -28.704 85.153  109.086 1.00 22.09 ? 735  THR   A CG2   1 
ATOM   5431  N  N     . PRO   A  1  738  ? -28.793 86.109  113.941 1.00 22.81 ? 736  PRO   A N     1 
ATOM   5432  C  CA    . PRO   A  1  738  ? -28.634 85.656  115.330 1.00 22.99 ? 736  PRO   A CA    1 
ATOM   5433  C  C     . PRO   A  1  738  ? -29.719 84.715  115.819 1.00 24.63 ? 736  PRO   A C     1 
ATOM   5434  O  O     . PRO   A  1  738  ? -29.464 83.957  116.767 1.00 25.19 ? 736  PRO   A O     1 
ATOM   5435  C  CB    . PRO   A  1  738  ? -28.677 86.968  116.127 1.00 27.35 ? 736  PRO   A CB    1 
ATOM   5436  C  CG    . PRO   A  1  738  ? -29.618 87.808  115.333 1.00 24.52 ? 736  PRO   A CG    1 
ATOM   5437  C  CD    . PRO   A  1  738  ? -29.317 87.486  113.885 1.00 25.74 ? 736  PRO   A CD    1 
ATOM   5438  N  N     . LEU   A  1  739  ? -30.919 84.743  115.230 1.00 22.77 ? 737  LEU   A N     1 
ATOM   5439  C  CA    . LEU   A  1  739  ? -32.035 84.004  115.817 1.00 23.71 ? 737  LEU   A CA    1 
ATOM   5440  C  C     . LEU   A  1  739  ? -31.843 82.504  115.676 1.00 20.57 ? 737  LEU   A C     1 
ATOM   5441  O  O     . LEU   A  1  739  ? -32.041 81.750  116.634 1.00 23.95 ? 737  LEU   A O     1 
ATOM   5442  C  CB    . LEU   A  1  739  ? -33.354 84.423  115.178 1.00 23.32 ? 737  LEU   A CB    1 
ATOM   5443  C  CG    . LEU   A  1  739  ? -33.651 85.902  115.306 1.00 24.16 ? 737  LEU   A CG    1 
ATOM   5444  C  CD1   . LEU   A  1  739  ? -34.936 86.191  114.533 1.00 23.37 ? 737  LEU   A CD1   1 
ATOM   5445  C  CD2   . LEU   A  1  739  ? -33.795 86.288  116.779 1.00 27.16 ? 737  LEU   A CD2   1 
ATOM   5446  N  N     . ILE   A  1  740  ? -31.503 82.044  114.476 1.00 21.19 ? 738  ILE   A N     1 
ATOM   5447  C  CA    . ILE   A  1  740  ? -31.324 80.609  114.297 1.00 22.21 ? 738  ILE   A CA    1 
ATOM   5448  C  C     . ILE   A  1  740  ? -30.127 80.134  115.104 1.00 21.16 ? 738  ILE   A C     1 
ATOM   5449  O  O     . ILE   A  1  740  ? -30.123 79.013  115.624 1.00 23.01 ? 738  ILE   A O     1 
ATOM   5450  C  CB    . ILE   A  1  740  ? -31.246 80.248  112.803 1.00 22.19 ? 738  ILE   A CB    1 
ATOM   5451  C  CG1   . ILE   A  1  740  ? -31.213 78.734  112.606 1.00 22.43 ? 738  ILE   A CG1   1 
ATOM   5452  C  CG2   . ILE   A  1  740  ? -30.012 80.845  112.188 1.00 23.10 ? 738  ILE   A CG2   1 
ATOM   5453  C  CD1   . ILE   A  1  740  ? -32.424 78.022  113.148 1.00 24.58 ? 738  ILE   A CD1   1 
ATOM   5454  N  N     . ALA   A  1  741  ? -29.129 81.002  115.279 1.00 21.70 ? 739  ALA   A N     1 
ATOM   5455  C  CA    . ALA   A  1  741  ? -27.992 80.664  116.119 1.00 22.86 ? 739  ALA   A CA    1 
ATOM   5456  C  C     . ALA   A  1  741  ? -28.417 80.508  117.570 1.00 24.20 ? 739  ALA   A C     1 
ATOM   5457  O  O     . ALA   A  1  741  ? -28.008 79.552  118.238 1.00 25.52 ? 739  ALA   A O     1 
ATOM   5458  C  CB    . ALA   A  1  741  ? -26.922 81.740  115.984 1.00 26.61 ? 739  ALA   A CB    1 
ATOM   5459  N  N     . ALA   A  1  742  ? -29.259 81.416  118.061 1.00 23.75 ? 740  ALA   A N     1 
ATOM   5460  C  CA    . ALA   A  1  742  ? -29.750 81.292  119.428 1.00 22.40 ? 740  ALA   A CA    1 
ATOM   5461  C  C     . ALA   A  1  742  ? -30.550 80.012  119.600 1.00 24.46 ? 740  ALA   A C     1 
ATOM   5462  O  O     . ALA   A  1  742  ? -30.455 79.345  120.636 1.00 25.77 ? 740  ALA   A O     1 
ATOM   5463  C  CB    . ALA   A  1  742  ? -30.598 82.506  119.810 1.00 23.93 ? 740  ALA   A CB    1 
ATOM   5464  N  N     . GLU   A  1  743  ? -31.329 79.642  118.585 1.00 23.14 ? 741  GLU   A N     1 
ATOM   5465  C  CA    . GLU   A  1  743  ? -32.078 78.398  118.668 1.00 25.91 ? 741  GLU   A CA    1 
ATOM   5466  C  C     . GLU   A  1  743  ? -31.142 77.192  118.672 1.00 23.54 ? 741  GLU   A C     1 
ATOM   5467  O  O     . GLU   A  1  743  ? -31.357 76.237  119.431 1.00 24.67 ? 741  GLU   A O     1 
ATOM   5468  C  CB    . GLU   A  1  743  ? -33.097 78.346  117.531 1.00 25.39 ? 741  GLU   A CB    1 
ATOM   5469  C  CG    . GLU   A  1  743  ? -33.874 77.055  117.420 1.00 26.99 ? 741  GLU   A CG    1 
ATOM   5470  C  CD    . GLU   A  1  743  ? -34.797 76.772  118.593 1.00 25.16 ? 741  GLU   A CD    1 
ATOM   5471  O  OE1   . GLU   A  1  743  ? -34.980 77.635  119.478 1.00 26.08 ? 741  GLU   A OE1   1 
ATOM   5472  O  OE2   . GLU   A  1  743  ? -35.329 75.645  118.618 1.00 28.58 ? 741  GLU   A OE2   1 
ATOM   5473  N  N     . GLY   A  1  744  ? -30.082 77.230  117.857 1.00 23.71 ? 742  GLY   A N     1 
ATOM   5474  C  CA    . GLY   A  1  744  ? -29.093 76.161  117.887 1.00 22.53 ? 742  GLY   A CA    1 
ATOM   5475  C  C     . GLY   A  1  744  ? -28.425 76.037  119.244 1.00 22.51 ? 742  GLY   A C     1 
ATOM   5476  O  O     . GLY   A  1  744  ? -28.234 74.930  119.754 1.00 24.81 ? 742  GLY   A O     1 
ATOM   5477  N  N     . VAL   A  1  745  ? -28.080 77.172  119.857 1.00 23.27 ? 743  VAL   A N     1 
ATOM   5478  C  CA    . VAL   A  1  745  ? -27.520 77.147  121.207 1.00 22.99 ? 743  VAL   A CA    1 
ATOM   5479  C  C     . VAL   A  1  745  ? -28.541 76.599  122.201 1.00 26.45 ? 743  VAL   A C     1 
ATOM   5480  O  O     . VAL   A  1  745  ? -28.206 75.799  123.083 1.00 26.21 ? 743  VAL   A O     1 
ATOM   5481  C  CB    . VAL   A  1  745  ? -27.016 78.548  121.607 1.00 25.26 ? 743  VAL   A CB    1 
ATOM   5482  C  CG1   . VAL   A  1  745  ? -26.759 78.620  123.115 1.00 30.13 ? 743  VAL   A CG1   1 
ATOM   5483  C  CG2   . VAL   A  1  745  ? -25.743 78.880  120.844 1.00 27.45 ? 743  VAL   A CG2   1 
ATOM   5484  N  N     . ARG   A  1  746  ? -29.807 77.009  122.069 1.00 24.67 ? 744  ARG   A N     1 
ATOM   5485  C  CA    . ARG   A  1  746  ? -30.837 76.478  122.959 1.00 25.76 ? 744  ARG   A CA    1 
ATOM   5486  C  C     . ARG   A  1  746  ? -30.931 74.960  122.837 1.00 24.70 ? 744  ARG   A C     1 
ATOM   5487  O  O     . ARG   A  1  746  ? -31.044 74.248  123.842 1.00 26.37 ? 744  ARG   A O     1 
ATOM   5488  C  CB    . ARG   A  1  746  ? -32.189 77.126  122.645 1.00 27.74 ? 744  ARG   A CB    1 
ATOM   5489  C  CG    . ARG   A  1  746  ? -33.260 76.799  123.673 1.00 28.39 ? 744  ARG   A CG    1 
ATOM   5490  C  CD    . ARG   A  1  746  ? -34.661 77.049  123.135 1.00 28.00 ? 744  ARG   A CD    1 
ATOM   5491  N  NE    . ARG   A  1  746  ? -34.968 76.175  122.014 1.00 29.07 ? 744  ARG   A NE    1 
ATOM   5492  C  CZ    . ARG   A  1  746  ? -35.279 74.891  122.126 1.00 32.71 ? 744  ARG   A CZ    1 
ATOM   5493  N  NH1   . ARG   A  1  746  ? -35.334 74.292  123.305 1.00 35.61 ? 744  ARG   A NH1   1 
ATOM   5494  N  NH2   . ARG   A  1  746  ? -35.527 74.185  121.027 1.00 32.25 ? 744  ARG   A NH2   1 
ATOM   5495  N  N     . ILE   A  1  747  ? -30.845 74.444  121.613 1.00 23.22 ? 745  ILE   A N     1 
ATOM   5496  C  CA    . ILE   A  1  747  ? -30.912 73.003  121.398 1.00 25.11 ? 745  ILE   A CA    1 
ATOM   5497  C  C     . ILE   A  1  747  ? -29.700 72.303  122.002 1.00 23.38 ? 745  ILE   A C     1 
ATOM   5498  O  O     . ILE   A  1  747  ? -29.830 71.259  122.653 1.00 23.92 ? 745  ILE   A O     1 
ATOM   5499  C  CB    . ILE   A  1  747  ? -31.082 72.713  119.898 1.00 24.66 ? 745  ILE   A CB    1 
ATOM   5500  C  CG1   . ILE   A  1  747  ? -32.510 73.075  119.478 1.00 24.28 ? 745  ILE   A CG1   1 
ATOM   5501  C  CG2   . ILE   A  1  747  ? -30.718 71.264  119.587 1.00 26.29 ? 745  ILE   A CG2   1 
ATOM   5502  C  CD1   . ILE   A  1  747  ? -32.709 73.128  117.978 1.00 26.31 ? 745  ILE   A CD1   1 
ATOM   5503  N  N     . LEU   A  1  748  ? -28.502 72.850  121.782 1.00 23.33 ? 746  LEU   A N     1 
ATOM   5504  C  CA    . LEU   A  1  748  ? -27.299 72.246  122.349 1.00 24.51 ? 746  LEU   A CA    1 
ATOM   5505  C  C     . LEU   A  1  748  ? -27.357 72.234  123.870 1.00 25.24 ? 746  LEU   A C     1 
ATOM   5506  O  O     . LEU   A  1  748  ? -27.000 71.237  124.509 1.00 25.12 ? 746  LEU   A O     1 
ATOM   5507  C  CB    . LEU   A  1  748  ? -26.062 72.998  121.862 1.00 23.32 ? 746  LEU   A CB    1 
ATOM   5508  C  CG    . LEU   A  1  748  ? -25.561 72.524  120.502 1.00 25.48 ? 746  LEU   A CG    1 
ATOM   5509  C  CD1   . LEU   A  1  748  ? -24.579 73.525  119.921 1.00 28.36 ? 746  LEU   A CD1   1 
ATOM   5510  C  CD2   . LEU   A  1  748  ? -24.893 71.183  120.651 1.00 25.08 ? 746  LEU   A CD2   1 
ATOM   5511  N  N     . ARG   A  1  749  ? -27.836 73.322  124.464 1.00 22.40 ? 747  ARG   A N     1 
ATOM   5512  C  CA    . ARG   A  1  749  ? -27.986 73.353  125.913 1.00 24.07 ? 747  ARG   A CA    1 
ATOM   5513  C  C     . ARG   A  1  749  ? -29.024 72.336  126.381 1.00 24.81 ? 747  ARG   A C     1 
ATOM   5514  O  O     . ARG   A  1  749  ? -28.794 71.613  127.359 1.00 27.64 ? 747  ARG   A O     1 
ATOM   5515  C  CB    . ARG   A  1  749  ? -28.307 74.776  126.366 1.00 27.60 ? 747  ARG   A CB    1 
ATOM   5516  C  CG    . ARG   A  1  749  ? -27.072 75.690  126.386 1.00 33.07 ? 747  ARG   A CG    1 
ATOM   5517  C  CD    . ARG   A  1  749  ? -27.430 77.110  126.810 1.00 36.86 ? 747  ARG   A CD    1 
ATOM   5518  N  NE    . ARG   A  1  749  ? -26.261 77.952  127.054 1.00 32.03 ? 747  ARG   A NE    1 
ATOM   5519  C  CZ    . ARG   A  1  749  ? -26.299 79.065  127.779 1.00 34.92 ? 747  ARG   A CZ    1 
ATOM   5520  N  NH1   . ARG   A  1  749  ? -27.427 79.499  128.317 1.00 35.71 ? 747  ARG   A NH1   1 
ATOM   5521  N  NH2   . ARG   A  1  749  ? -25.175 79.749  127.986 1.00 32.78 ? 747  ARG   A NH2   1 
ATOM   5522  N  N     . GLU   A  1  750  ? -30.154 72.235  125.675 1.00 24.73 ? 748  GLU   A N     1 
ATOM   5523  C  CA    . GLU   A  1  750  ? -31.138 71.213  126.026 1.00 27.32 ? 748  GLU   A CA    1 
ATOM   5524  C  C     . GLU   A  1  750  ? -30.534 69.814  125.943 1.00 27.21 ? 748  GLU   A C     1 
ATOM   5525  O  O     . GLU   A  1  750  ? -30.840 68.940  126.766 1.00 28.06 ? 748  GLU   A O     1 
ATOM   5526  C  CB    . GLU   A  1  750  ? -32.362 71.325  125.120 1.00 28.38 ? 748  GLU   A CB    1 
ATOM   5527  C  CG    . GLU   A  1  750  ? -33.440 70.313  125.447 1.00 29.96 ? 748  GLU   A CG    1 
ATOM   5528  C  CD    . GLU   A  1  750  ? -34.621 70.383  124.504 1.00 32.16 ? 748  GLU   A CD    1 
ATOM   5529  O  OE1   . GLU   A  1  750  ? -34.811 71.430  123.850 1.00 40.10 ? 748  GLU   A OE1   1 
ATOM   5530  O  OE2   . GLU   A  1  750  ? -35.342 69.373  124.402 1.00 32.13 ? 748  GLU   A OE2   1 
ATOM   5531  N  N     . ALA   A  1  751  ? -29.648 69.593  124.973 1.00 26.02 ? 749  ALA   A N     1 
ATOM   5532  C  CA    . ALA   A  1  751  ? -29.025 68.291  124.773 1.00 25.17 ? 749  ALA   A CA    1 
ATOM   5533  C  C     . ALA   A  1  751  ? -28.001 67.968  125.846 1.00 26.97 ? 749  ALA   A C     1 
ATOM   5534  O  O     . ALA   A  1  751  ? -27.471 66.850  125.864 1.00 29.09 ? 749  ALA   A O     1 
ATOM   5535  C  CB    . ALA   A  1  751  ? -28.351 68.248  123.402 1.00 23.40 ? 749  ALA   A CB    1 
ATOM   5536  N  N     . GLY   A  1  752  ? -27.682 68.922  126.712 1.00 25.76 ? 750  GLY   A N     1 
ATOM   5537  C  CA    . GLY   A  1  752  ? -26.817 68.659  127.845 1.00 28.11 ? 750  GLY   A CA    1 
ATOM   5538  C  C     . GLY   A  1  752  ? -25.552 69.482  127.882 1.00 27.28 ? 750  GLY   A C     1 
ATOM   5539  O  O     . GLY   A  1  752  ? -24.760 69.310  128.819 1.00 28.55 ? 750  GLY   A O     1 
ATOM   5540  N  N     . ILE   A  1  753  ? -25.296 70.356  126.914 1.00 28.07 ? 751  ILE   A N     1 
ATOM   5541  C  CA    . ILE   A  1  753  ? -24.114 71.212  126.980 1.00 27.14 ? 751  ILE   A CA    1 
ATOM   5542  C  C     . ILE   A  1  753  ? -24.354 72.226  128.091 1.00 25.58 ? 751  ILE   A C     1 
ATOM   5543  O  O     . ILE   A  1  753  ? -25.316 72.998  128.015 1.00 27.12 ? 751  ILE   A O     1 
ATOM   5544  C  CB    . ILE   A  1  753  ? -23.852 71.919  125.644 1.00 25.17 ? 751  ILE   A CB    1 
ATOM   5545  C  CG1   . ILE   A  1  753  ? -23.648 70.905  124.519 1.00 24.77 ? 751  ILE   A CG1   1 
ATOM   5546  C  CG2   . ILE   A  1  753  ? -22.661 72.845  125.789 1.00 26.71 ? 751  ILE   A CG2   1 
ATOM   5547  C  CD1   . ILE   A  1  753  ? -22.364 70.131  124.593 1.00 23.59 ? 751  ILE   A CD1   1 
ATOM   5548  N  N     . PRO   A  1  754  ? -23.519 72.270  129.125 1.00 27.88 ? 752  PRO   A N     1 
ATOM   5549  C  CA    . PRO   A  1  754  ? -23.731 73.249  130.194 1.00 27.92 ? 752  PRO   A CA    1 
ATOM   5550  C  C     . PRO   A  1  754  ? -23.616 74.677  129.680 1.00 26.50 ? 752  PRO   A C     1 
ATOM   5551  O  O     . PRO   A  1  754  ? -22.888 74.963  128.727 1.00 26.34 ? 752  PRO   A O     1 
ATOM   5552  C  CB    . PRO   A  1  754  ? -22.610 72.935  131.194 1.00 30.42 ? 752  PRO   A CB    1 
ATOM   5553  C  CG    . PRO   A  1  754  ? -22.083 71.592  130.814 1.00 29.88 ? 752  PRO   A CG    1 
ATOM   5554  C  CD    . PRO   A  1  754  ? -22.330 71.438  129.349 1.00 28.07 ? 752  PRO   A CD    1 
ATOM   5555  N  N     . ALA   A  1  755  ? -24.348 75.583  130.338 1.00 28.80 ? 753  ALA   A N     1 
ATOM   5556  C  CA    . ALA   A  1  755  ? -24.289 76.999  129.977 1.00 27.12 ? 753  ALA   A CA    1 
ATOM   5557  C  C     . ALA   A  1  755  ? -22.869 77.546  130.068 1.00 27.59 ? 753  ALA   A C     1 
ATOM   5558  O  O     . ALA   A  1  755  ? -22.487 78.427  129.287 1.00 30.11 ? 753  ALA   A O     1 
ATOM   5559  C  CB    . ALA   A  1  755  ? -25.210 77.807  130.892 1.00 34.11 ? 753  ALA   A CB    1 
ATOM   5560  N  N     . SER   A  1  756  ? -22.073 77.038  131.007 1.00 28.51 ? 754  SER   A N     1 
ATOM   5561  C  CA    . SER   A  1  756  ? -20.709 77.524  131.139 1.00 28.80 ? 754  SER   A CA    1 
ATOM   5562  C  C     . SER   A  1  756  ? -19.851 77.097  129.959 1.00 29.13 ? 754  SER   A C     1 
ATOM   5563  O  O     . SER   A  1  756  ? -18.872 77.778  129.630 1.00 29.89 ? 754  SER   A O     1 
ATOM   5564  C  CB    . SER   A  1  756  ? -20.103 77.020  132.442 1.00 30.16 ? 754  SER   A CB    1 
ATOM   5565  O  OG    . SER   A  1  756  ? -20.031 75.603  132.471 1.00 33.29 ? 754  SER   A OG    1 
ATOM   5566  N  N     . ALA   A  1  757  ? -20.208 75.991  129.300 1.00 28.65 ? 755  ALA   A N     1 
ATOM   5567  C  CA    . ALA   A  1  757  ? -19.429 75.488  128.176 1.00 25.23 ? 755  ALA   A CA    1 
ATOM   5568  C  C     . ALA   A  1  757  ? -19.863 76.079  126.850 1.00 26.68 ? 755  ALA   A C     1 
ATOM   5569  O  O     . ALA   A  1  757  ? -19.119 75.972  125.872 1.00 25.74 ? 755  ALA   A O     1 
ATOM   5570  C  CB    . ALA   A  1  757  ? -19.541 73.963  128.087 1.00 27.45 ? 755  ALA   A CB    1 
ATOM   5571  N  N     . LEU   A  1  758  ? -21.037 76.701  126.783 1.00 25.17 ? 756  LEU   A N     1 
ATOM   5572  C  CA    . LEU   A  1  758  ? -21.531 77.232  125.516 1.00 25.56 ? 756  LEU   A CA    1 
ATOM   5573  C  C     . LEU   A  1  758  ? -22.249 78.544  125.791 1.00 26.35 ? 756  LEU   A C     1 
ATOM   5574  O  O     . LEU   A  1  758  ? -23.381 78.554  126.279 1.00 30.08 ? 756  LEU   A O     1 
ATOM   5575  C  CB    . LEU   A  1  758  ? -22.442 76.244  124.816 1.00 24.71 ? 756  LEU   A CB    1 
ATOM   5576  C  CG    . LEU   A  1  758  ? -23.052 76.763  123.518 1.00 26.03 ? 756  LEU   A CG    1 
ATOM   5577  C  CD1   . LEU   A  1  758  ? -21.970 77.286  122.565 1.00 25.79 ? 756  LEU   A CD1   1 
ATOM   5578  C  CD2   . LEU   A  1  758  ? -23.858 75.656  122.882 1.00 26.28 ? 756  LEU   A CD2   1 
ATOM   5579  N  N     . GLN   A  1  759  ? -21.583 79.642  125.468 1.00 24.05 ? 757  GLN   A N     1 
ATOM   5580  C  CA    . GLN   A  1  759  ? -22.128 80.971  125.651 1.00 26.77 ? 757  GLN   A CA    1 
ATOM   5581  C  C     . GLN   A  1  759  ? -22.369 81.593  124.288 1.00 26.21 ? 757  GLN   A C     1 
ATOM   5582  O  O     . GLN   A  1  759  ? -21.501 81.547  123.411 1.00 28.85 ? 757  GLN   A O     1 
ATOM   5583  C  CB    . GLN   A  1  759  ? -21.172 81.826  126.481 1.00 26.27 ? 757  GLN   A CB    1 
ATOM   5584  C  CG    . GLN   A  1  759  ? -21.039 81.355  127.898 1.00 27.94 ? 757  GLN   A CG    1 
ATOM   5585  C  CD    . GLN   A  1  759  ? -20.025 82.171  128.652 1.00 27.54 ? 757  GLN   A CD    1 
ATOM   5586  O  OE1   . GLN   A  1  759  ? -20.373 83.133  129.338 1.00 28.19 ? 757  GLN   A OE1   1 
ATOM   5587  N  NE2   . GLN   A  1  759  ? -18.754 81.814  128.503 1.00 27.58 ? 757  GLN   A NE2   1 
ATOM   5588  N  N     . LEU   A  1  760  ? -23.558 82.140  124.107 1.00 26.36 ? 758  LEU   A N     1 
ATOM   5589  C  CA    . LEU   A  1  760  ? -23.945 82.779  122.861 1.00 27.30 ? 758  LEU   A CA    1 
ATOM   5590  C  C     . LEU   A  1  760  ? -23.752 84.275  123.019 1.00 24.87 ? 758  LEU   A C     1 
ATOM   5591  O  O     . LEU   A  1  760  ? -24.264 84.869  123.971 1.00 25.37 ? 758  LEU   A O     1 
ATOM   5592  C  CB    . LEU   A  1  760  ? -25.412 82.500  122.560 1.00 25.35 ? 758  LEU   A CB    1 
ATOM   5593  C  CG    . LEU   A  1  760  ? -25.912 83.211  121.308 1.00 26.39 ? 758  LEU   A CG    1 
ATOM   5594  C  CD1   . LEU   A  1  760  ? -25.420 82.519  120.043 1.00 27.08 ? 758  LEU   A CD1   1 
ATOM   5595  C  CD2   . LEU   A  1  760  ? -27.422 83.281  121.327 1.00 27.94 ? 758  LEU   A CD2   1 
ATOM   5596  N  N     . LEU   A  1  761  ? -23.012 84.882  122.100 1.00 26.33 ? 759  LEU   A N     1 
ATOM   5597  C  CA    A LEU   A  1  761  ? -22.700 86.307  122.156 0.51 27.20 ? 759  LEU   A CA    1 
ATOM   5598  C  CA    B LEU   A  1  761  ? -22.695 86.309  122.155 0.49 27.20 ? 759  LEU   A CA    1 
ATOM   5599  C  C     . LEU   A  1  761  ? -23.106 86.959  120.846 1.00 26.55 ? 759  LEU   A C     1 
ATOM   5600  O  O     . LEU   A  1  761  ? -22.281 87.156  119.949 1.00 26.58 ? 759  LEU   A O     1 
ATOM   5601  C  CB    A LEU   A  1  761  ? -21.226 86.529  122.482 0.51 25.68 ? 759  LEU   A CB    1 
ATOM   5602  C  CB    B LEU   A  1  761  ? -21.211 86.555  122.432 0.49 25.69 ? 759  LEU   A CB    1 
ATOM   5603  C  CG    A LEU   A  1  761  ? -20.830 85.803  123.767 0.51 27.04 ? 759  LEU   A CG    1 
ATOM   5604  C  CG    B LEU   A  1  761  ? -20.579 86.035  123.725 0.49 26.72 ? 759  LEU   A CG    1 
ATOM   5605  C  CD1   A LEU   A  1  761  ? -19.331 85.655  123.884 0.51 26.44 ? 759  LEU   A CD1   1 
ATOM   5606  C  CD1   B LEU   A  1  761  ? -21.511 86.243  124.914 0.49 27.44 ? 759  LEU   A CD1   1 
ATOM   5607  C  CD2   A LEU   A  1  761  ? -21.404 86.531  124.970 0.51 27.89 ? 759  LEU   A CD2   1 
ATOM   5608  C  CD2   B LEU   A  1  761  ? -20.167 84.573  123.586 0.49 25.44 ? 759  LEU   A CD2   1 
ATOM   5609  N  N     . PRO   A  1  762  ? -24.374 87.310  120.701 1.00 24.53 ? 760  PRO   A N     1 
ATOM   5610  C  CA    . PRO   A  1  762  ? -24.810 87.981  119.474 1.00 25.98 ? 760  PRO   A CA    1 
ATOM   5611  C  C     . PRO   A  1  762  ? -24.162 89.350  119.344 1.00 30.08 ? 760  PRO   A C     1 
ATOM   5612  O  O     . PRO   A  1  762  ? -23.812 89.997  120.335 1.00 29.64 ? 760  PRO   A O     1 
ATOM   5613  C  CB    . PRO   A  1  762  ? -26.324 88.123  119.670 1.00 25.83 ? 760  PRO   A CB    1 
ATOM   5614  C  CG    . PRO   A  1  762  ? -26.672 87.161  120.764 1.00 27.14 ? 760  PRO   A CG    1 
ATOM   5615  C  CD    . PRO   A  1  762  ? -25.480 87.082  121.642 1.00 25.59 ? 760  PRO   A CD    1 
ATOM   5616  N  N     . GLY   A  1  763  ? -24.022 89.794  118.112 1.00 25.76 ? 761  GLY   A N     1 
ATOM   5617  C  CA    . GLY   A  1  763  ? -23.481 91.112  117.853 1.00 29.76 ? 761  GLY   A CA    1 
ATOM   5618  C  C     . GLY   A  1  763  ? -22.688 91.109  116.566 1.00 28.23 ? 761  GLY   A C     1 
ATOM   5619  O  O     . GLY   A  1  763  ? -22.637 90.120  115.840 1.00 26.56 ? 761  GLY   A O     1 
ATOM   5620  N  N     . ASP   A  1  764  ? -22.051 92.248  116.314 1.00 30.51 ? 762  ASP   A N     1 
ATOM   5621  C  CA    . ASP   A  1  764  ? -21.371 92.456  115.044 1.00 30.01 ? 762  ASP   A CA    1 
ATOM   5622  C  C     . ASP   A  1  764  ? -19.893 92.077  115.170 1.00 30.91 ? 762  ASP   A C     1 
ATOM   5623  O  O     . ASP   A  1  764  ? -19.484 91.392  116.113 1.00 26.88 ? 762  ASP   A O     1 
ATOM   5624  C  CB    . ASP   A  1  764  ? -21.631 93.876  114.522 1.00 35.76 ? 762  ASP   A CB    1 
ATOM   5625  C  CG    . ASP   A  1  764  ? -21.095 94.956  115.449 1.00 38.63 ? 762  ASP   A CG    1 
ATOM   5626  O  OD1   . ASP   A  1  764  ? -20.196 94.664  116.262 1.00 37.12 ? 762  ASP   A OD1   1 
ATOM   5627  O  OD2   . ASP   A  1  764  ? -21.584 96.107  115.377 1.00 47.91 ? 762  ASP   A OD2   1 
ATOM   5628  N  N     . GLY   A  1  765  ? -19.077 92.532  114.219 1.00 27.85 ? 763  GLY   A N     1 
ATOM   5629  C  CA    . GLY   A  1  765  ? -17.671 92.175  114.209 1.00 27.21 ? 763  GLY   A CA    1 
ATOM   5630  C  C     . GLY   A  1  765  ? -16.916 92.663  115.422 1.00 29.95 ? 763  GLY   A C     1 
ATOM   5631  O  O     . GLY   A  1  765  ? -15.869 92.101  115.758 1.00 31.13 ? 763  GLY   A O     1 
ATOM   5632  N  N     . ARG   A  1  766  ? -17.429 93.700  116.094 1.00 29.88 ? 764  ARG   A N     1 
ATOM   5633  C  CA    . ARG   A  1  766  ? -16.792 94.187  117.313 1.00 29.62 ? 764  ARG   A CA    1 
ATOM   5634  C  C     . ARG   A  1  766  ? -16.830 93.139  118.408 1.00 31.22 ? 764  ARG   A C     1 
ATOM   5635  O  O     . ARG   A  1  766  ? -15.894 93.031  119.207 1.00 31.37 ? 764  ARG   A O     1 
ATOM   5636  C  CB    . ARG   A  1  766  ? -17.515 95.425  117.831 1.00 36.13 ? 764  ARG   A CB    1 
ATOM   5637  C  CG    . ARG   A  1  766  ? -17.342 96.675  117.028 1.00 43.85 ? 764  ARG   A CG    1 
ATOM   5638  C  CD    . ARG   A  1  766  ? -18.215 97.739  117.654 1.00 39.15 ? 764  ARG   A CD    1 
ATOM   5639  N  NE    . ARG   A  1  766  ? -19.624 97.372  117.570 1.00 43.16 ? 764  ARG   A NE    1 
ATOM   5640  C  CZ    . ARG   A  1  766  ? -20.529 97.656  118.495 1.00 44.51 ? 764  ARG   A CZ    1 
ATOM   5641  N  NH1   . ARG   A  1  766  ? -20.198 98.267  119.621 1.00 52.18 ? 764  ARG   A NH1   1 
ATOM   5642  N  NH2   . ARG   A  1  766  ? -21.798 97.316  118.288 1.00 47.91 ? 764  ARG   A NH2   1 
ATOM   5643  N  N     . VAL   A  1  767  ? -17.936 92.402  118.502 1.00 26.57 ? 765  VAL   A N     1 
ATOM   5644  C  CA    . VAL   A  1  767  ? -18.025 91.339  119.493 1.00 28.50 ? 765  VAL   A CA    1 
ATOM   5645  C  C     . VAL   A  1  767  ? -17.066 90.220  119.137 1.00 26.10 ? 765  VAL   A C     1 
ATOM   5646  O  O     . VAL   A  1  767  ? -16.367 89.685  120.005 1.00 27.73 ? 765  VAL   A O     1 
ATOM   5647  C  CB    . VAL   A  1  767  ? -19.479 90.852  119.627 1.00 26.11 ? 765  VAL   A CB    1 
ATOM   5648  C  CG1   . VAL   A  1  767  ? -19.598 89.779  120.701 1.00 29.51 ? 765  VAL   A CG1   1 
ATOM   5649  C  CG2   . VAL   A  1  767  ? -20.392 92.025  119.935 1.00 29.72 ? 765  VAL   A CG2   1 
ATOM   5650  N  N     . GLY   A  1  768  ? -17.009 89.858  117.849 1.00 25.93 ? 766  GLY   A N     1 
ATOM   5651  C  CA    . GLY   A  1  768  ? -16.029 88.879  117.414 1.00 23.98 ? 766  GLY   A CA    1 
ATOM   5652  C  C     . GLY   A  1  768  ? -14.615 89.306  117.747 1.00 25.61 ? 766  GLY   A C     1 
ATOM   5653  O  O     . GLY   A  1  768  ? -13.829 88.524  118.277 1.00 25.57 ? 766  GLY   A O     1 
ATOM   5654  N  N     . ALA   A  1  769  ? -14.283 90.568  117.463 1.00 25.06 ? 767  ALA   A N     1 
ATOM   5655  C  CA    . ALA   A  1  769  ? -12.921 91.040  117.691 1.00 26.43 ? 767  ALA   A CA    1 
ATOM   5656  C  C     . ALA   A  1  769  ? -12.597 91.068  119.177 1.00 27.37 ? 767  ALA   A C     1 
ATOM   5657  O  O     . ALA   A  1  769  ? -11.481 90.716  119.581 1.00 28.66 ? 767  ALA   A O     1 
ATOM   5658  C  CB    . ALA   A  1  769  ? -12.737 92.428  117.081 1.00 28.64 ? 767  ALA   A CB    1 
ATOM   5659  N  N     . ALA   A  1  770  ? -13.563 91.481  120.000 1.00 28.05 ? 768  ALA   A N     1 
ATOM   5660  C  CA    . ALA   A  1  770  ? -13.328 91.523  121.439 1.00 29.66 ? 768  ALA   A CA    1 
ATOM   5661  C  C     . ALA   A  1  770  ? -13.064 90.127  121.974 1.00 28.15 ? 768  ALA   A C     1 
ATOM   5662  O  O     . ALA   A  1  770  ? -12.232 89.937  122.870 1.00 29.27 ? 768  ALA   A O     1 
ATOM   5663  C  CB    . ALA   A  1  770  ? -14.533 92.146  122.139 1.00 29.23 ? 768  ALA   A CB    1 
ATOM   5664  N  N     . LEU   A  1  771  ? -13.756 89.133  121.416 1.00 27.14 ? 769  LEU   A N     1 
ATOM   5665  C  CA    . LEU   A  1  771  ? -13.546 87.752  121.827 1.00 26.76 ? 769  LEU   A CA    1 
ATOM   5666  C  C     . LEU   A  1  771  ? -12.177 87.260  121.391 1.00 27.14 ? 769  LEU   A C     1 
ATOM   5667  O  O     . LEU   A  1  771  ? -11.458 86.623  122.171 1.00 28.39 ? 769  LEU   A O     1 
ATOM   5668  C  CB    . LEU   A  1  771  ? -14.651 86.875  121.230 1.00 25.00 ? 769  LEU   A CB    1 
ATOM   5669  C  CG    . LEU   A  1  771  ? -16.060 87.107  121.784 1.00 26.69 ? 769  LEU   A CG    1 
ATOM   5670  C  CD1   . LEU   A  1  771  ? -17.086 86.283  120.992 1.00 25.99 ? 769  LEU   A CD1   1 
ATOM   5671  C  CD2   . LEU   A  1  771  ? -16.110 86.790  123.277 1.00 28.09 ? 769  LEU   A CD2   1 
ATOM   5672  N  N     . VAL   A  1  772  ? -11.804 87.541  120.140 1.00 24.83 ? 770  VAL   A N     1 
ATOM   5673  C  CA    . VAL   A  1  772  ? -10.500 87.133  119.631 1.00 24.94 ? 770  VAL   A CA    1 
ATOM   5674  C  C     . VAL   A  1  772  ? -9.384  87.722  120.482 1.00 27.28 ? 770  VAL   A C     1 
ATOM   5675  O  O     . VAL   A  1  772  ? -8.395  87.046  120.781 1.00 29.49 ? 770  VAL   A O     1 
ATOM   5676  C  CB    . VAL   A  1  772  ? -10.363 87.522  118.148 1.00 25.96 ? 770  VAL   A CB    1 
ATOM   5677  C  CG1   . VAL   A  1  772  ? -8.929  87.337  117.675 1.00 26.55 ? 770  VAL   A CG1   1 
ATOM   5678  C  CG2   . VAL   A  1  772  ? -11.300 86.680  117.302 1.00 23.76 ? 770  VAL   A CG2   1 
ATOM   5679  N  N     . ALA   A  1  773  ? -9.521  88.986  120.876 1.00 28.04 ? 771  ALA   A N     1 
ATOM   5680  C  CA    . ALA   A  1  773  ? -8.470  89.681  121.617 1.00 26.66 ? 771  ALA   A CA    1 
ATOM   5681  C  C     . ALA   A  1  773  ? -8.422  89.301  123.090 1.00 33.64 ? 771  ALA   A C     1 
ATOM   5682  O  O     . ALA   A  1  773  ? -7.448  89.658  123.767 1.00 34.49 ? 771  ALA   A O     1 
ATOM   5683  C  CB    . ALA   A  1  773  ? -8.659  91.191  121.489 1.00 30.88 ? 771  ALA   A CB    1 
ATOM   5684  N  N     . ALA   A  1  774  ? -9.429  88.591  123.595 1.00 30.87 ? 772  ALA   A N     1 
ATOM   5685  C  CA    . ALA   A  1  774  ? -9.500  88.295  125.022 1.00 33.56 ? 772  ALA   A CA    1 
ATOM   5686  C  C     . ALA   A  1  774  ? -8.349  87.387  125.430 1.00 29.67 ? 772  ALA   A C     1 
ATOM   5687  O  O     . ALA   A  1  774  ? -7.964  86.468  124.705 1.00 31.45 ? 772  ALA   A O     1 
ATOM   5688  C  CB    . ALA   A  1  774  ? -10.837 87.641  125.359 1.00 33.07 ? 772  ALA   A CB    1 
ATOM   5689  N  N     . ALA   A  1  775  ? -7.792  87.653  126.613 1.00 38.33 ? 773  ALA   A N     1 
ATOM   5690  C  CA    . ALA   A  1  775  ? -6.537  87.013  126.974 1.00 33.92 ? 773  ALA   A CA    1 
ATOM   5691  C  C     . ALA   A  1  775  ? -6.671  85.503  127.106 1.00 28.06 ? 773  ALA   A C     1 
ATOM   5692  O  O     . ALA   A  1  775  ? -5.717  84.775  126.822 1.00 32.91 ? 773  ALA   A O     1 
ATOM   5693  C  CB    . ALA   A  1  775  ? -5.976  87.622  128.260 1.00 35.66 ? 773  ALA   A CB    1 
ATOM   5694  N  N     . GLU   A  1  776  ? -7.826  85.011  127.546 1.00 28.13 ? 774  GLU   A N     1 
ATOM   5695  C  CA    . GLU   A  1  776  ? -7.975  83.582  127.783 1.00 28.20 ? 774  GLU   A CA    1 
ATOM   5696  C  C     . GLU   A  1  776  ? -8.421  82.820  126.545 1.00 28.18 ? 774  GLU   A C     1 
ATOM   5697  O  O     . GLU   A  1  776  ? -8.583  81.596  126.608 1.00 29.41 ? 774  GLU   A O     1 
ATOM   5698  C  CB    . GLU   A  1  776  ? -8.945  83.317  128.931 1.00 30.93 ? 774  GLU   A CB    1 
ATOM   5699  C  CG    . GLU   A  1  776  ? -8.562  84.012  130.232 1.00 34.91 ? 774  GLU   A CG    1 
ATOM   5700  C  CD    . GLU   A  1  776  ? -9.196  85.392  130.398 1.00 39.48 ? 774  GLU   A CD    1 
ATOM   5701  O  OE1   . GLU   A  1  776  ? -9.689  85.985  129.407 1.00 33.24 ? 774  GLU   A OE1   1 
ATOM   5702  O  OE2   . GLU   A  1  776  ? -9.195  85.892  131.543 1.00 45.78 ? 774  GLU   A OE2   1 
ATOM   5703  N  N     . THR   A  1  777  ? -8.607  83.503  125.427 1.00 25.39 ? 775  THR   A N     1 
ATOM   5704  C  CA    . THR   A  1  777  ? -9.007  82.822  124.206 1.00 25.15 ? 775  THR   A CA    1 
ATOM   5705  C  C     . THR   A  1  777  ? -7.869  81.938  123.732 1.00 26.57 ? 775  THR   A C     1 
ATOM   5706  O  O     . THR   A  1  777  ? -6.746  82.410  123.516 1.00 28.13 ? 775  THR   A O     1 
ATOM   5707  C  CB    . THR   A  1  777  ? -9.376  83.847  123.149 1.00 27.10 ? 775  THR   A CB    1 
ATOM   5708  O  OG1   . THR   A  1  777  ? -10.597 84.474  123.544 1.00 25.65 ? 775  THR   A OG1   1 
ATOM   5709  C  CG2   . THR   A  1  777  ? -9.529  83.157  121.789 1.00 25.45 ? 775  THR   A CG2   1 
ATOM   5710  N  N     . ALA   A  1  778  ? -8.147  80.647  123.624 1.00 23.85 ? 776  ALA   A N     1 
ATOM   5711  C  CA    . ALA   A  1  778  ? -7.119  79.662  123.348 1.00 22.67 ? 776  ALA   A CA    1 
ATOM   5712  C  C     . ALA   A  1  778  ? -7.141  79.178  121.911 1.00 23.41 ? 776  ALA   A C     1 
ATOM   5713  O  O     . ALA   A  1  778  ? -6.234  78.453  121.504 1.00 23.68 ? 776  ALA   A O     1 
ATOM   5714  C  CB    . ALA   A  1  778  ? -7.271  78.471  124.304 1.00 24.28 ? 776  ALA   A CB    1 
ATOM   5715  N  N     . GLY   A  1  779  ? -8.157  79.554  121.145 1.00 21.72 ? 777  GLY   A N     1 
ATOM   5716  C  CA    . GLY   A  1  779  ? -8.245  79.156  119.763 1.00 21.44 ? 777  GLY   A CA    1 
ATOM   5717  C  C     . GLY   A  1  779  ? -9.408  79.874  119.130 1.00 20.31 ? 777  GLY   A C     1 
ATOM   5718  O  O     . GLY   A  1  779  ? -10.340 80.311  119.815 1.00 21.30 ? 777  GLY   A O     1 
ATOM   5719  N  N     . VAL   A  1  780  ? -9.348  80.017  117.817 1.00 20.26 ? 778  VAL   A N     1 
ATOM   5720  C  CA    . VAL   A  1  780  ? -10.358 80.745  117.070 1.00 21.18 ? 778  VAL   A CA    1 
ATOM   5721  C  C     . VAL   A  1  780  ? -10.757 79.894  115.879 1.00 19.96 ? 778  VAL   A C     1 
ATOM   5722  O  O     . VAL   A  1  780  ? -9.894  79.408  115.137 1.00 20.28 ? 778  VAL   A O     1 
ATOM   5723  C  CB    . VAL   A  1  780  ? -9.852  82.128  116.618 1.00 20.99 ? 778  VAL   A CB    1 
ATOM   5724  C  CG1   . VAL   A  1  780  ? -10.924 82.868  115.851 1.00 21.52 ? 778  VAL   A CG1   1 
ATOM   5725  C  CG2   . VAL   A  1  780  ? -9.435  82.952  117.844 1.00 21.81 ? 778  VAL   A CG2   1 
ATOM   5726  N  N     . MET   A  1  781  ? -12.057 79.693  115.711 1.00 18.98 ? 779  MET   A N     1 
ATOM   5727  C  CA    . MET   A  1  781  ? -12.613 79.038  114.537 1.00 18.03 ? 779  MET   A CA    1 
ATOM   5728  C  C     . MET   A  1  781  ? -13.421 80.099  113.822 1.00 19.08 ? 779  MET   A C     1 
ATOM   5729  O  O     . MET   A  1  781  ? -14.426 80.583  114.353 1.00 19.92 ? 779  MET   A O     1 
ATOM   5730  C  CB    . MET   A  1  781  ? -13.495 77.869  114.947 1.00 19.99 ? 779  MET   A CB    1 
ATOM   5731  C  CG    . MET   A  1  781  ? -12.737 76.848  115.747 1.00 20.30 ? 779  MET   A CG    1 
ATOM   5732  S  SD    . MET   A  1  781  ? -13.821 75.578  116.367 1.00 21.21 ? 779  MET   A SD    1 
ATOM   5733  C  CE    . MET   A  1  781  ? -14.044 74.609  114.887 1.00 20.96 ? 779  MET   A CE    1 
ATOM   5734  N  N     . PHE   A  1  782  ? -12.951 80.488  112.650 1.00 20.17 ? 780  PHE   A N     1 
ATOM   5735  C  CA    . PHE   A  1  782  ? -13.564 81.539  111.866 1.00 20.06 ? 780  PHE   A CA    1 
ATOM   5736  C  C     . PHE   A  1  782  ? -13.988 80.979  110.523 1.00 19.67 ? 780  PHE   A C     1 
ATOM   5737  O  O     . PHE   A  1  782  ? -13.184 80.353  109.824 1.00 19.21 ? 780  PHE   A O     1 
ATOM   5738  C  CB    . PHE   A  1  782  ? -12.564 82.658  111.597 1.00 20.01 ? 780  PHE   A CB    1 
ATOM   5739  C  CG    . PHE   A  1  782  ? -13.114 83.722  110.717 1.00 20.54 ? 780  PHE   A CG    1 
ATOM   5740  C  CD1   . PHE   A  1  782  ? -13.973 84.671  111.233 1.00 19.52 ? 780  PHE   A CD1   1 
ATOM   5741  C  CD2   . PHE   A  1  782  ? -12.827 83.750  109.356 1.00 19.12 ? 780  PHE   A CD2   1 
ATOM   5742  C  CE1   . PHE   A  1  782  ? -14.523 85.637  110.434 1.00 20.04 ? 780  PHE   A CE1   1 
ATOM   5743  C  CE2   . PHE   A  1  782  ? -13.372 84.724  108.558 1.00 19.64 ? 780  PHE   A CE2   1 
ATOM   5744  C  CZ    . PHE   A  1  782  ? -14.213 85.672  109.099 1.00 18.76 ? 780  PHE   A CZ    1 
ATOM   5745  N  N     . THR   A  1  783  ? -15.232 81.244  110.157 1.00 18.09 ? 781  THR   A N     1 
ATOM   5746  C  CA    . THR   A  1  783  ? -15.680 81.063  108.787 1.00 19.34 ? 781  THR   A CA    1 
ATOM   5747  C  C     . THR   A  1  783  ? -16.312 82.369  108.359 1.00 18.99 ? 781  THR   A C     1 
ATOM   5748  O  O     . THR   A  1  783  ? -17.166 82.904  109.065 1.00 20.02 ? 781  THR   A O     1 
ATOM   5749  C  CB    . THR   A  1  783  ? -16.652 79.891  108.665 1.00 19.80 ? 781  THR   A CB    1 
ATOM   5750  O  OG1   . THR   A  1  783  ? -16.006 78.709  109.151 1.00 19.44 ? 781  THR   A OG1   1 
ATOM   5751  C  CG2   . THR   A  1  783  ? -17.027 79.667  107.210 1.00 21.07 ? 781  THR   A CG2   1 
ATOM   5752  N  N     . GLY   A  1  784  ? -15.867 82.898  107.227 1.00 19.62 ? 782  GLY   A N     1 
ATOM   5753  C  CA    . GLY   A  1  784  ? -16.292 84.218  106.819 1.00 19.81 ? 782  GLY   A CA    1 
ATOM   5754  C  C     . GLY   A  1  784  ? -15.423 84.688  105.679 1.00 17.75 ? 782  GLY   A C     1 
ATOM   5755  O  O     . GLY   A  1  784  ? -14.785 83.881  104.997 1.00 20.58 ? 782  GLY   A O     1 
ATOM   5756  N  N     . SER   A  1  785  ? -15.400 85.997  105.480 1.00 19.87 ? 783  SER   A N     1 
ATOM   5757  C  CA    . SER   A  1  785  ? -14.656 86.532  104.350 1.00 20.56 ? 783  SER   A CA    1 
ATOM   5758  C  C     . SER   A  1  785  ? -13.154 86.513  104.613 1.00 22.67 ? 783  SER   A C     1 
ATOM   5759  O  O     . SER   A  1  785  ? -12.689 86.583  105.755 1.00 22.12 ? 783  SER   A O     1 
ATOM   5760  C  CB    . SER   A  1  785  ? -15.101 87.959  104.058 1.00 22.70 ? 783  SER   A CB    1 
ATOM   5761  O  OG    . SER   A  1  785  ? -14.840 88.801  105.165 1.00 24.29 ? 783  SER   A OG    1 
ATOM   5762  N  N     . THR   A  1  786  ? -12.392 86.404  103.523 1.00 21.78 ? 784  THR   A N     1 
ATOM   5763  C  CA    . THR   A  1  786  ? -10.940 86.420  103.633 1.00 23.17 ? 784  THR   A CA    1 
ATOM   5764  C  C     . THR   A  1  786  ? -10.439 87.704  104.283 1.00 21.16 ? 784  THR   A C     1 
ATOM   5765  O  O     . THR   A  1  786  ? -9.497  87.675  105.086 1.00 22.61 ? 784  THR   A O     1 
ATOM   5766  C  CB    . THR   A  1  786  ? -10.328 86.210  102.248 1.00 23.60 ? 784  THR   A CB    1 
ATOM   5767  O  OG1   . THR   A  1  786  ? -10.850 84.997  101.701 1.00 24.06 ? 784  THR   A OG1   1 
ATOM   5768  C  CG2   . THR   A  1  786  ? -8.819  86.125  102.345 1.00 25.05 ? 784  THR   A CG2   1 
ATOM   5769  N  N     . GLU   A  1  787  ? -11.071 88.837  103.971 1.00 23.65 ? 785  GLU   A N     1 
ATOM   5770  C  CA    . GLU   A  1  787  ? -10.614 90.113  104.507 1.00 22.67 ? 785  GLU   A CA    1 
ATOM   5771  C  C     . GLU   A  1  787  ? -10.791 90.177  106.021 1.00 22.01 ? 785  GLU   A C     1 
ATOM   5772  O  O     . GLU   A  1  787  ? -9.924  90.691  106.733 1.00 23.41 ? 785  GLU   A O     1 
ATOM   5773  C  CB    . GLU   A  1  787  ? -11.359 91.266  103.829 1.00 29.32 ? 785  GLU   A CB    1 
ATOM   5774  N  N     . VAL   A  1  788  ? -11.900 89.638  106.529 1.00 22.81 ? 786  VAL   A N     1 
ATOM   5775  C  CA    . VAL   A  1  788  ? -12.081 89.612  107.979 1.00 21.88 ? 786  VAL   A CA    1 
ATOM   5776  C  C     . VAL   A  1  788  ? -11.118 88.621  108.622 1.00 23.11 ? 786  VAL   A C     1 
ATOM   5777  O  O     . VAL   A  1  788  ? -10.539 88.895  109.680 1.00 22.73 ? 786  VAL   A O     1 
ATOM   5778  C  CB    . VAL   A  1  788  ? -13.547 89.320  108.340 1.00 22.30 ? 786  VAL   A CB    1 
ATOM   5779  C  CG1   . VAL   A  1  788  ? -13.671 89.020  109.824 1.00 23.56 ? 786  VAL   A CG1   1 
ATOM   5780  C  CG2   . VAL   A  1  788  ? -14.426 90.519  107.991 1.00 23.57 ? 786  VAL   A CG2   1 
ATOM   5781  N  N     . ALA   A  1  789  ? -10.923 87.458  107.994 1.00 20.38 ? 787  ALA   A N     1 
ATOM   5782  C  CA    . ALA   A  1  789  ? -9.955  86.501  108.516 1.00 21.35 ? 787  ALA   A CA    1 
ATOM   5783  C  C     . ALA   A  1  789  ? -8.588  87.145  108.654 1.00 19.78 ? 787  ALA   A C     1 
ATOM   5784  O  O     . ALA   A  1  789  ? -7.866  86.893  109.625 1.00 20.35 ? 787  ALA   A O     1 
ATOM   5785  C  CB    . ALA   A  1  789  ? -9.876  85.287  107.590 1.00 18.98 ? 787  ALA   A CB    1 
ATOM   5786  N  N     . ARG   A  1  790  ? -8.222  88.001  107.698 1.00 21.53 ? 788  ARG   A N     1 
ATOM   5787  C  CA    . ARG   A  1  790  ? -6.923  88.660  107.743 1.00 21.71 ? 788  ARG   A CA    1 
ATOM   5788  C  C     . ARG   A  1  790  ? -6.824  89.610  108.934 1.00 22.74 ? 788  ARG   A C     1 
ATOM   5789  O  O     . ARG   A  1  790  ? -5.761  89.730  109.553 1.00 23.41 ? 788  ARG   A O     1 
ATOM   5790  C  CB    . ARG   A  1  790  ? -6.680  89.383  106.418 1.00 25.14 ? 788  ARG   A CB    1 
ATOM   5791  C  CG    . ARG   A  1  790  ? -5.327  90.067  106.304 1.00 24.34 ? 788  ARG   A CG    1 
ATOM   5792  C  CD    . ARG   A  1  790  ? -5.114  90.604  104.880 1.00 21.99 ? 788  ARG   A CD    1 
ATOM   5793  N  NE    . ARG   A  1  790  ? -5.055  89.520  103.905 1.00 23.05 ? 788  ARG   A NE    1 
ATOM   5794  C  CZ    . ARG   A  1  790  ? -5.886  89.361  102.881 1.00 22.16 ? 788  ARG   A CZ    1 
ATOM   5795  N  NH1   . ARG   A  1  790  ? -6.849  90.231  102.619 1.00 26.87 ? 788  ARG   A NH1   1 
ATOM   5796  N  NH2   . ARG   A  1  790  ? -5.743  88.302  102.089 1.00 26.62 ? 788  ARG   A NH2   1 
ATOM   5797  N  N     . LEU   A  1  791  ? -7.929  90.287  109.278 1.00 23.52 ? 789  LEU   A N     1 
ATOM   5798  C  CA    . LEU   A  1  791  ? -7.941  91.124  110.473 1.00 23.87 ? 789  LEU   A CA    1 
ATOM   5799  C  C     . LEU   A  1  791  ? -7.766  90.279  111.730 1.00 24.34 ? 789  LEU   A C     1 
ATOM   5800  O  O     . LEU   A  1  791  ? -7.042  90.668  112.655 1.00 24.11 ? 789  LEU   A O     1 
ATOM   5801  C  CB    . LEU   A  1  791  ? -9.254  91.898  110.543 1.00 23.92 ? 789  LEU   A CB    1 
ATOM   5802  C  CG    . LEU   A  1  791  ? -9.494  92.943  109.450 1.00 29.21 ? 789  LEU   A CG    1 
ATOM   5803  C  CD1   . LEU   A  1  791  ? -10.899 93.498  109.541 1.00 29.31 ? 789  LEU   A CD1   1 
ATOM   5804  C  CD2   . LEU   A  1  791  ? -8.474  94.047  109.546 1.00 30.54 ? 789  LEU   A CD2   1 
ATOM   5805  N  N     . ILE   A  1  792  ? -8.423  89.117  111.773 1.00 21.21 ? 790  ILE   A N     1 
ATOM   5806  C  CA    . ILE   A  1  792  ? -8.258  88.209  112.907 1.00 22.70 ? 790  ILE   A CA    1 
ATOM   5807  C  C     . ILE   A  1  792  ? -6.833  87.674  112.983 1.00 24.29 ? 790  ILE   A C     1 
ATOM   5808  O  O     . ILE   A  1  792  ? -6.241  87.595  114.069 1.00 23.59 ? 790  ILE   A O     1 
ATOM   5809  C  CB    . ILE   A  1  792  ? -9.302  87.083  112.833 1.00 22.00 ? 790  ILE   A CB    1 
ATOM   5810  C  CG1   . ILE   A  1  792  ? -10.683 87.668  113.056 1.00 22.90 ? 790  ILE   A CG1   1 
ATOM   5811  C  CG2   . ILE   A  1  792  ? -8.998  85.975  113.846 1.00 22.95 ? 790  ILE   A CG2   1 
ATOM   5812  C  CD1   . ILE   A  1  792  ? -11.808 86.708  112.773 1.00 22.52 ? 790  ILE   A CD1   1 
ATOM   5813  N  N     . GLN   A  1  793  ? -6.269  87.284  111.841 1.00 21.13 ? 791  GLN   A N     1 
ATOM   5814  C  CA    . GLN   A  1  793  ? -4.876  86.858  111.799 1.00 22.34 ? 791  GLN   A CA    1 
ATOM   5815  C  C     . GLN   A  1  793  ? -3.960  87.925  112.386 1.00 22.19 ? 791  GLN   A C     1 
ATOM   5816  O  O     . GLN   A  1  793  ? -3.038  87.618  113.151 1.00 23.27 ? 791  GLN   A O     1 
ATOM   5817  C  CB    . GLN   A  1  793  ? -4.504  86.542  110.346 1.00 24.04 ? 791  GLN   A CB    1 
ATOM   5818  C  CG    . GLN   A  1  793  ? -3.059  86.161  110.118 1.00 23.33 ? 791  GLN   A CG    1 
ATOM   5819  C  CD    . GLN   A  1  793  ? -2.681  86.219  108.642 1.00 24.21 ? 791  GLN   A CD    1 
ATOM   5820  O  OE1   . GLN   A  1  793  ? -3.119  87.110  107.908 1.00 27.27 ? 791  GLN   A OE1   1 
ATOM   5821  N  NE2   . GLN   A  1  793  ? -1.895  85.248  108.192 1.00 26.49 ? 791  GLN   A NE2   1 
ATOM   5822  N  N     . ALA   A  1  794  ? -4.219  89.193  112.059 1.00 24.16 ? 792  ALA   A N     1 
ATOM   5823  C  CA    . ALA   A  1  794  ? -3.402  90.269  112.606 1.00 27.37 ? 792  ALA   A CA    1 
ATOM   5824  C  C     . ALA   A  1  794  ? -3.565  90.380  114.119 1.00 25.96 ? 792  ALA   A C     1 
ATOM   5825  O  O     . ALA   A  1  794  ? -2.574  90.537  114.837 1.00 29.31 ? 792  ALA   A O     1 
ATOM   5826  C  CB    . ALA   A  1  794  ? -3.749  91.585  111.915 1.00 26.68 ? 792  ALA   A CB    1 
ATOM   5827  N  N     . GLN   A  1  795  ? -4.803  90.279  114.615 1.00 24.97 ? 793  GLN   A N     1 
ATOM   5828  C  CA    . GLN   A  1  795  ? -5.040  90.318  116.058 1.00 24.99 ? 793  GLN   A CA    1 
ATOM   5829  C  C     . GLN   A  1  795  ? -4.280  89.210  116.765 1.00 27.74 ? 793  GLN   A C     1 
ATOM   5830  O  O     . GLN   A  1  795  ? -3.655  89.430  117.812 1.00 28.08 ? 793  GLN   A O     1 
ATOM   5831  C  CB    . GLN   A  1  795  ? -6.523  90.121  116.355 1.00 31.10 ? 793  GLN   A CB    1 
ATOM   5832  C  CG    . GLN   A  1  795  ? -7.440  91.304  116.197 1.00 34.55 ? 793  GLN   A CG    1 
ATOM   5833  C  CD    . GLN   A  1  795  ? -8.847  90.967  116.688 1.00 36.00 ? 793  GLN   A CD    1 
ATOM   5834  O  OE1   . GLN   A  1  795  ? -9.612  90.287  115.997 1.00 37.51 ? 793  GLN   A OE1   1 
ATOM   5835  N  NE2   . GLN   A  1  795  ? -9.181  91.408  117.893 1.00 30.02 ? 793  GLN   A NE2   1 
ATOM   5836  N  N     . LEU   A  1  796  ? -4.352  87.995  116.225 1.00 24.68 ? 794  LEU   A N     1 
ATOM   5837  C  CA    . LEU   A  1  796  ? -3.739  86.861  116.894 1.00 26.28 ? 794  LEU   A CA    1 
ATOM   5838  C  C     . LEU   A  1  796  ? -2.222  86.885  116.815 1.00 24.90 ? 794  LEU   A C     1 
ATOM   5839  O  O     . LEU   A  1  796  ? -1.562  86.267  117.658 1.00 29.13 ? 794  LEU   A O     1 
ATOM   5840  C  CB    . LEU   A  1  796  ? -4.279  85.562  116.313 1.00 23.60 ? 794  LEU   A CB    1 
ATOM   5841  C  CG    . LEU   A  1  796  ? -5.726  85.250  116.670 1.00 24.15 ? 794  LEU   A CG    1 
ATOM   5842  C  CD1   . LEU   A  1  796  ? -6.146  83.933  116.036 1.00 25.46 ? 794  LEU   A CD1   1 
ATOM   5843  C  CD2   . LEU   A  1  796  ? -5.867  85.205  118.193 1.00 27.50 ? 794  LEU   A CD2   1 
ATOM   5844  N  N     . ALA   A  1  797  ? -1.649  87.585  115.839 1.00 26.34 ? 795  ALA   A N     1 
ATOM   5845  C  CA    . ALA   A  1  797  ? -0.197  87.619  115.745 1.00 29.49 ? 795  ALA   A CA    1 
ATOM   5846  C  C     . ALA   A  1  797  ? 0.427   88.306  116.954 1.00 30.35 ? 795  ALA   A C     1 
ATOM   5847  O  O     . ALA   A  1  797  ? 1.593   88.052  117.272 1.00 36.67 ? 795  ALA   A O     1 
ATOM   5848  C  CB    . ALA   A  1  797  ? 0.235   88.285  114.439 1.00 27.26 ? 795  ALA   A CB    1 
ATOM   5849  N  N     . ASP   A  1  798  ? -0.340  89.141  117.655 1.00 29.23 ? 796  ASP   A N     1 
ATOM   5850  C  CA    . ASP   A  1  798  ? 0.139   89.760  118.885 1.00 33.82 ? 796  ASP   A CA    1 
ATOM   5851  C  C     . ASP   A  1  798  ? 0.244   88.762  120.023 1.00 39.44 ? 796  ASP   A C     1 
ATOM   5852  O  O     . ASP   A  1  798  ? 0.917   89.046  121.020 1.00 35.32 ? 796  ASP   A O     1 
ATOM   5853  C  CB    . ASP   A  1  798  ? -0.835  90.854  119.325 1.00 29.83 ? 796  ASP   A CB    1 
ATOM   5854  C  CG    . ASP   A  1  798  ? -0.831  92.040  118.396 1.00 46.94 ? 796  ASP   A CG    1 
ATOM   5855  O  OD1   . ASP   A  1  798  ? 0.220   92.288  117.766 1.00 46.00 ? 796  ASP   A OD1   1 
ATOM   5856  O  OD2   . ASP   A  1  798  ? -1.876  92.721  118.295 1.00 49.25 ? 796  ASP   A OD2   1 
ATOM   5857  N  N     . ARG   A  1  799  ? -0.395  87.607  119.892 1.00 30.59 ? 797  ARG   A N     1 
ATOM   5858  C  CA    . ARG   A  1  799  ? -0.758  86.777  121.025 1.00 28.87 ? 797  ARG   A CA    1 
ATOM   5859  C  C     . ARG   A  1  799  ? 0.022   85.469  121.035 1.00 26.33 ? 797  ARG   A C     1 
ATOM   5860  O  O     . ARG   A  1  799  ? 0.327   84.891  119.992 1.00 27.21 ? 797  ARG   A O     1 
ATOM   5861  C  CB    . ARG   A  1  799  ? -2.244  86.454  120.935 1.00 33.11 ? 797  ARG   A CB    1 
ATOM   5862  C  CG    . ARG   A  1  799  ? -3.084  87.687  120.673 1.00 37.85 ? 797  ARG   A CG    1 
ATOM   5863  C  CD    . ARG   A  1  799  ? -3.474  88.299  121.979 1.00 43.04 ? 797  ARG   A CD    1 
ATOM   5864  N  NE    . ARG   A  1  799  ? -4.093  87.281  122.813 1.00 45.47 ? 797  ARG   A NE    1 
ATOM   5865  C  CZ    . ARG   A  1  799  ? -5.293  86.767  122.591 1.00 40.64 ? 797  ARG   A CZ    1 
ATOM   5866  N  NH1   . ARG   A  1  799  ? -6.055  87.195  121.597 1.00 45.65 ? 797  ARG   A NH1   1 
ATOM   5867  N  NH2   . ARG   A  1  799  ? -5.737  85.793  123.380 1.00 48.09 ? 797  ARG   A NH2   1 
ATOM   5868  N  N     . LEU   A  1  800  ? 0.340   85.013  122.244 1.00 26.42 ? 798  LEU   A N     1 
ATOM   5869  C  CA    . LEU   A  1  800  ? 0.836   83.666  122.462 1.00 30.01 ? 798  LEU   A CA    1 
ATOM   5870  C  C     . LEU   A  1  800  ? 0.035   83.032  123.588 1.00 26.14 ? 798  LEU   A C     1 
ATOM   5871  O  O     . LEU   A  1  800  ? -0.493  83.720  124.461 1.00 31.29 ? 798  LEU   A O     1 
ATOM   5872  C  CB    . LEU   A  1  800  ? 2.298   83.679  122.889 1.00 27.62 ? 798  LEU   A CB    1 
ATOM   5873  C  CG    . LEU   A  1  800  ? 3.318   84.167  121.866 1.00 29.58 ? 798  LEU   A CG    1 
ATOM   5874  C  CD1   . LEU   A  1  800  ? 4.691   84.243  122.520 1.00 31.51 ? 798  LEU   A CD1   1 
ATOM   5875  C  CD2   . LEU   A  1  800  ? 3.332   83.237  120.667 1.00 30.89 ? 798  LEU   A CD2   1 
ATOM   5876  N  N     . SER   A  1  801  ? -0.050  81.707  123.545 1.00 28.52 ? 799  SER   A N     1 
ATOM   5877  C  CA    . SER   A  1  801  ? -0.643  80.948  124.630 1.00 30.65 ? 799  SER   A CA    1 
ATOM   5878  C  C     . SER   A  1  801  ? 0.230   81.070  125.877 1.00 36.13 ? 799  SER   A C     1 
ATOM   5879  O  O     . SER   A  1  801  ? 1.368   81.540  125.812 1.00 32.23 ? 799  SER   A O     1 
ATOM   5880  C  CB    . SER   A  1  801  ? -0.721  79.480  124.224 1.00 32.50 ? 799  SER   A CB    1 
ATOM   5881  O  OG    . SER   A  1  801  ? 0.576   78.909  124.258 1.00 30.36 ? 799  SER   A OG    1 
ATOM   5882  N  N     . PRO   A  1  802  ? -0.285  80.657  127.040 1.00 30.66 ? 800  PRO   A N     1 
ATOM   5883  C  CA    . PRO   A  1  802  ? 0.561   80.617  128.244 1.00 31.73 ? 800  PRO   A CA    1 
ATOM   5884  C  C     . PRO   A  1  802  ? 1.798   79.759  128.089 1.00 34.65 ? 800  PRO   A C     1 
ATOM   5885  O  O     . PRO   A  1  802  ? 2.786   79.989  128.799 1.00 39.50 ? 800  PRO   A O     1 
ATOM   5886  C  CB    . PRO   A  1  802  ? -0.385  80.062  129.313 1.00 36.66 ? 800  PRO   A CB    1 
ATOM   5887  C  CG    . PRO   A  1  802  ? -1.732  80.516  128.871 1.00 37.04 ? 800  PRO   A CG    1 
ATOM   5888  C  CD    . PRO   A  1  802  ? -1.707  80.434  127.364 1.00 33.33 ? 800  PRO   A CD    1 
ATOM   5889  N  N     . ALA   A  1  803  ? 1.778   78.781  127.189 1.00 37.19 ? 801  ALA   A N     1 
ATOM   5890  C  CA    . ALA   A  1  803  ? 2.964   78.011  126.855 1.00 34.39 ? 801  ALA   A CA    1 
ATOM   5891  C  C     . ALA   A  1  803  ? 3.868   78.727  125.859 1.00 41.24 ? 801  ALA   A C     1 
ATOM   5892  O  O     . ALA   A  1  803  ? 4.893   78.162  125.467 1.00 38.17 ? 801  ALA   A O     1 
ATOM   5893  C  CB    . ALA   A  1  803  ? 2.562   76.643  126.293 1.00 40.97 ? 801  ALA   A CB    1 
ATOM   5894  N  N     . GLY   A  1  804  ? 3.504   79.933  125.425 1.00 38.03 ? 802  GLY   A N     1 
ATOM   5895  C  CA    . GLY   A  1  804  ? 4.323   80.670  124.481 1.00 31.38 ? 802  GLY   A CA    1 
ATOM   5896  C  C     . GLY   A  1  804  ? 4.239   80.212  123.038 1.00 30.75 ? 802  GLY   A C     1 
ATOM   5897  O  O     . GLY   A  1  804  ? 5.225   80.321  122.306 1.00 33.20 ? 802  GLY   A O     1 
ATOM   5898  N  N     . ARG   A  1  805  ? 3.087   79.726  122.591 1.00 30.65 ? 803  ARG   A N     1 
ATOM   5899  C  CA    . ARG   A  1  805  ? 2.921   79.238  121.230 1.00 31.94 ? 803  ARG   A CA    1 
ATOM   5900  C  C     . ARG   A  1  805  ? 1.738   79.931  120.568 1.00 23.98 ? 803  ARG   A C     1 
ATOM   5901  O  O     . ARG   A  1  805  ? 0.880   80.490  121.256 1.00 25.99 ? 803  ARG   A O     1 
ATOM   5902  C  CB    . ARG   A  1  805  ? 2.722   77.715  121.220 1.00 33.32 ? 803  ARG   A CB    1 
ATOM   5903  C  CG    . ARG   A  1  805  ? 3.901   76.945  121.828 1.00 31.53 ? 803  ARG   A CG    1 
ATOM   5904  C  CD    . ARG   A  1  805  ? 5.222   77.263  121.109 1.00 36.37 ? 803  ARG   A CD    1 
ATOM   5905  N  NE    . ARG   A  1  805  ? 6.357   76.560  121.707 1.00 33.13 ? 803  ARG   A NE    1 
ATOM   5906  C  CZ    . ARG   A  1  805  ? 7.210   77.098  122.570 1.00 37.04 ? 803  ARG   A CZ    1 
ATOM   5907  N  NH1   . ARG   A  1  805  ? 7.126   78.369  122.932 1.00 36.40 ? 803  ARG   A NH1   1 
ATOM   5908  N  NH2   . ARG   A  1  805  ? 8.170   76.337  123.091 1.00 42.34 ? 803  ARG   A NH2   1 
ATOM   5909  N  N     . PRO   A  1  806  ? 1.687   79.953  119.229 1.00 26.94 ? 804  PRO   A N     1 
ATOM   5910  C  CA    . PRO   A  1  806  ? 0.605   80.678  118.551 1.00 25.35 ? 804  PRO   A CA    1 
ATOM   5911  C  C     . PRO   A  1  806  ? -0.758  80.107  118.904 1.00 23.78 ? 804  PRO   A C     1 
ATOM   5912  O  O     . PRO   A  1  806  ? -0.917  78.900  119.110 1.00 24.68 ? 804  PRO   A O     1 
ATOM   5913  C  CB    . PRO   A  1  806  ? 0.911   80.469  117.064 1.00 25.36 ? 804  PRO   A CB    1 
ATOM   5914  C  CG    . PRO   A  1  806  ? 2.382   80.208  117.013 1.00 27.69 ? 804  PRO   A CG    1 
ATOM   5915  C  CD    . PRO   A  1  806  ? 2.681   79.442  118.272 1.00 28.36 ? 804  PRO   A CD    1 
ATOM   5916  N  N     . ILE   A  1  807  ? -1.741  81.001  118.972 1.00 22.65 ? 805  ILE   A N     1 
ATOM   5917  C  CA    . ILE   A  1  807  ? -3.136  80.628  119.185 1.00 22.73 ? 805  ILE   A CA    1 
ATOM   5918  C  C     . ILE   A  1  807  ? -3.679  80.028  117.899 1.00 22.73 ? 805  ILE   A C     1 
ATOM   5919  O  O     . ILE   A  1  807  ? -3.682  80.703  116.862 1.00 23.22 ? 805  ILE   A O     1 
ATOM   5920  C  CB    . ILE   A  1  807  ? -3.974  81.855  119.556 1.00 23.65 ? 805  ILE   A CB    1 
ATOM   5921  C  CG1   . ILE   A  1  807  ? -3.408  82.533  120.795 1.00 26.26 ? 805  ILE   A CG1   1 
ATOM   5922  C  CG2   . ILE   A  1  807  ? -5.443  81.469  119.745 1.00 25.08 ? 805  ILE   A CG2   1 
ATOM   5923  C  CD1   . ILE   A  1  807  ? -3.352  81.645  122.013 1.00 29.19 ? 805  ILE   A CD1   1 
ATOM   5924  N  N     . PRO   A  1  808  ? -4.128  78.775  117.909 1.00 21.27 ? 806  PRO   A N     1 
ATOM   5925  C  CA    . PRO   A  1  808  ? -4.602  78.153  116.667 1.00 21.13 ? 806  PRO   A CA    1 
ATOM   5926  C  C     . PRO   A  1  808  ? -5.788  78.900  116.069 1.00 20.72 ? 806  PRO   A C     1 
ATOM   5927  O  O     . PRO   A  1  808  ? -6.717  79.304  116.774 1.00 21.21 ? 806  PRO   A O     1 
ATOM   5928  C  CB    . PRO   A  1  808  ? -4.997  76.742  117.117 1.00 23.36 ? 806  PRO   A CB    1 
ATOM   5929  C  CG    . PRO   A  1  808  ? -4.136  76.488  118.316 1.00 25.46 ? 806  PRO   A CG    1 
ATOM   5930  C  CD    . PRO   A  1  808  ? -4.098  77.815  119.026 1.00 22.35 ? 806  PRO   A CD    1 
ATOM   5931  N  N     . LEU   A  1  809  ? -5.741  79.073  114.752 1.00 20.52 ? 807  LEU   A N     1 
ATOM   5932  C  CA    . LEU   A  1  809  ? -6.808  79.710  113.997 1.00 20.36 ? 807  LEU   A CA    1 
ATOM   5933  C  C     . LEU   A  1  809  ? -7.185  78.786  112.855 1.00 21.05 ? 807  LEU   A C     1 
ATOM   5934  O  O     . LEU   A  1  809  ? -6.326  78.410  112.051 1.00 21.41 ? 807  LEU   A O     1 
ATOM   5935  C  CB    . LEU   A  1  809  ? -6.336  81.045  113.422 1.00 21.24 ? 807  LEU   A CB    1 
ATOM   5936  C  CG    . LEU   A  1  809  ? -7.292  81.713  112.433 1.00 20.24 ? 807  LEU   A CG    1 
ATOM   5937  C  CD1   . LEU   A  1  809  ? -8.626  82.053  113.097 1.00 22.16 ? 807  LEU   A CD1   1 
ATOM   5938  C  CD2   . LEU   A  1  809  ? -6.648  82.964  111.861 1.00 24.72 ? 807  LEU   A CD2   1 
ATOM   5939  N  N     . ILE   A  1  810  ? -8.453  78.395  112.796 1.00 18.70 ? 808  ILE   A N     1 
ATOM   5940  C  CA    . ILE   A  1  810  ? -9.025  77.805  111.599 1.00 19.26 ? 808  ILE   A CA    1 
ATOM   5941  C  C     . ILE   A  1  810  ? -9.788  78.926  110.931 1.00 18.69 ? 808  ILE   A C     1 
ATOM   5942  O  O     . ILE   A  1  810  ? -10.686 79.513  111.544 1.00 20.94 ? 808  ILE   A O     1 
ATOM   5943  C  CB    . ILE   A  1  810  ? -9.964  76.637  111.925 1.00 18.02 ? 808  ILE   A CB    1 
ATOM   5944  C  CG1   . ILE   A  1  810  ? -9.261  75.558  112.740 1.00 21.42 ? 808  ILE   A CG1   1 
ATOM   5945  C  CG2   . ILE   A  1  810  ? -10.486 76.038  110.620 1.00 20.87 ? 808  ILE   A CG2   1 
ATOM   5946  C  CD1   . ILE   A  1  810  ? -10.127 74.318  112.970 1.00 23.99 ? 808  ILE   A CD1   1 
ATOM   5947  N  N     . ALA   A  1  811  ? -9.414  79.252  109.700 1.00 18.45 ? 809  ALA   A N     1 
ATOM   5948  C  CA    . ALA   A  1  811  ? -10.027 80.366  108.984 1.00 18.23 ? 809  ALA   A CA    1 
ATOM   5949  C  C     . ALA   A  1  811  ? -10.446 79.846  107.619 1.00 18.28 ? 809  ALA   A C     1 
ATOM   5950  O  O     . ALA   A  1  811  ? -9.600  79.608  106.751 1.00 19.24 ? 809  ALA   A O     1 
ATOM   5951  C  CB    . ALA   A  1  811  ? -9.078  81.547  108.862 1.00 20.33 ? 809  ALA   A CB    1 
ATOM   5952  N  N     . GLU   A  1  812  ? -11.741 79.637  107.455 1.00 16.65 ? 810  GLU   A N     1 
ATOM   5953  C  CA    . GLU   A  1  812  ? -12.316 79.074  106.244 1.00 17.01 ? 810  GLU   A CA    1 
ATOM   5954  C  C     . GLU   A  1  812  ? -13.019 80.220  105.540 1.00 17.17 ? 810  GLU   A C     1 
ATOM   5955  O  O     . GLU   A  1  812  ? -13.945 80.817  106.092 1.00 18.72 ? 810  GLU   A O     1 
ATOM   5956  C  CB    . GLU   A  1  812  ? -13.245 77.927  106.624 1.00 19.89 ? 810  GLU   A CB    1 
ATOM   5957  C  CG    . GLU   A  1  812  ? -12.489 76.808  107.348 1.00 21.80 ? 810  GLU   A CG    1 
ATOM   5958  C  CD    . GLU   A  1  812  ? -11.327 76.247  106.524 1.00 24.45 ? 810  GLU   A CD    1 
ATOM   5959  O  OE1   . GLU   A  1  812  ? -11.588 75.419  105.627 1.00 21.23 ? 810  GLU   A OE1   1 
ATOM   5960  O  OE2   . GLU   A  1  812  ? -10.157 76.631  106.758 1.00 23.24 ? 810  GLU   A OE2   1 
ATOM   5961  N  N     . THR   A  1  813  ? -12.536 80.569  104.351 1.00 17.56 ? 811  THR   A N     1 
ATOM   5962  C  CA    . THR   A  1  813  ? -12.804 81.874  103.767 1.00 19.30 ? 811  THR   A CA    1 
ATOM   5963  C  C     . THR   A  1  813  ? -13.418 81.724  102.374 1.00 18.77 ? 811  THR   A C     1 
ATOM   5964  O  O     . THR   A  1  813  ? -14.035 80.712  102.030 1.00 19.96 ? 811  THR   A O     1 
ATOM   5965  C  CB    . THR   A  1  813  ? -11.572 82.766  103.906 1.00 19.26 ? 811  THR   A CB    1 
ATOM   5966  O  OG1   . THR   A  1  813  ? -10.424 82.089  103.376 1.00 20.44 ? 811  THR   A OG1   1 
ATOM   5967  C  CG2   . THR   A  1  813  ? -11.327 83.062  105.379 1.00 19.48 ? 811  THR   A CG2   1 
ATOM   5968  N  N     . GLY   A  1  814  ? -13.296 82.765  101.559 1.00 20.30 ? 812  GLY   A N     1 
ATOM   5969  C  CA    . GLY   A  1  814  ? -14.084 82.858  100.345 1.00 20.15 ? 812  GLY   A CA    1 
ATOM   5970  C  C     . GLY   A  1  814  ? -13.536 82.048  99.183  1.00 19.79 ? 812  GLY   A C     1 
ATOM   5971  O  O     . GLY   A  1  814  ? -12.494 81.401  99.256  1.00 20.19 ? 812  GLY   A O     1 
ATOM   5972  N  N     . GLY   A  1  815  ? -14.263 82.108  98.071  1.00 18.30 ? 813  GLY   A N     1 
ATOM   5973  C  CA    . GLY   A  1  815  ? -13.882 81.381  96.880  1.00 19.91 ? 813  GLY   A CA    1 
ATOM   5974  C  C     . GLY   A  1  815  ? -14.049 82.258  95.658  1.00 20.73 ? 813  GLY   A C     1 
ATOM   5975  O  O     . GLY   A  1  815  ? -14.730 83.284  95.685  1.00 22.29 ? 813  GLY   A O     1 
ATOM   5976  N  N     . GLN   A  1  816  ? -13.386 81.851  94.586  1.00 18.54 ? 814  GLN   A N     1 
ATOM   5977  C  CA    . GLN   A  1  816  ? -13.625 82.405  93.258  1.00 18.72 ? 814  GLN   A CA    1 
ATOM   5978  C  C     . GLN   A  1  816  ? -13.783 81.195  92.351  1.00 19.38 ? 814  GLN   A C     1 
ATOM   5979  O  O     . GLN   A  1  816  ? -12.913 80.869  91.545  1.00 20.97 ? 814  GLN   A O     1 
ATOM   5980  C  CB    . GLN   A  1  816  ? -12.476 83.297  92.808  1.00 20.49 ? 814  GLN   A CB    1 
ATOM   5981  C  CG    . GLN   A  1  816  ? -12.772 84.096  91.559  1.00 23.04 ? 814  GLN   A CG    1 
ATOM   5982  C  CD    . GLN   A  1  816  ? -13.848 85.128  91.796  1.00 26.61 ? 814  GLN   A CD    1 
ATOM   5983  O  OE1   . GLN   A  1  816  ? -15.034 84.809  91.830  1.00 23.44 ? 814  GLN   A OE1   1 
ATOM   5984  N  NE2   . GLN   A  1  816  ? -13.433 86.376  91.990  1.00 27.47 ? 814  GLN   A NE2   1 
ATOM   5985  N  N     . ASN   A  1  817  ? -14.888 80.497  92.533  1.00 17.38 ? 815  ASN   A N     1 
ATOM   5986  C  CA    . ASN   A  1  817  ? -14.980 79.112  92.105  1.00 16.99 ? 815  ASN   A CA    1 
ATOM   5987  C  C     . ASN   A  1  817  ? -15.330 79.023  90.629  1.00 16.52 ? 815  ASN   A C     1 
ATOM   5988  O  O     . ASN   A  1  817  ? -16.262 79.686  90.153  1.00 17.27 ? 815  ASN   A O     1 
ATOM   5989  C  CB    . ASN   A  1  817  ? -16.035 78.397  92.940  1.00 15.84 ? 815  ASN   A CB    1 
ATOM   5990  C  CG    . ASN   A  1  817  ? -15.833 78.632  94.419  1.00 15.71 ? 815  ASN   A CG    1 
ATOM   5991  O  OD1   . ASN   A  1  817  ? -14.747 78.379  94.948  1.00 16.28 ? 815  ASN   A OD1   1 
ATOM   5992  N  ND2   . ASN   A  1  817  ? -16.847 79.153  95.087  1.00 16.22 ? 815  ASN   A ND2   1 
ATOM   5993  N  N     . ALA   A  1  818  ? -14.594 78.178  89.915  1.00 15.18 ? 816  ALA   A N     1 
ATOM   5994  C  CA    . ALA   A  1  818  ? -14.766 77.995  88.487  1.00 16.36 ? 816  ALA   A CA    1 
ATOM   5995  C  C     . ALA   A  1  818  ? -15.332 76.623  88.184  1.00 14.08 ? 816  ALA   A C     1 
ATOM   5996  O  O     . ALA   A  1  818  ? -15.191 75.667  88.952  1.00 15.45 ? 816  ALA   A O     1 
ATOM   5997  C  CB    . ALA   A  1  818  ? -13.424 78.113  87.782  1.00 16.50 ? 816  ALA   A CB    1 
ATOM   5998  N  N     . MET   A  1  819  ? -15.981 76.544  87.024  1.00 15.97 ? 817  MET   A N     1 
ATOM   5999  C  CA    . MET   A  1  819  ? -16.370 75.285  86.423  1.00 15.06 ? 817  MET   A CA    1 
ATOM   6000  C  C     . MET   A  1  819  ? -15.898 75.312  84.984  1.00 15.99 ? 817  MET   A C     1 
ATOM   6001  O  O     . MET   A  1  819  ? -16.164 76.281  84.269  1.00 16.66 ? 817  MET   A O     1 
ATOM   6002  C  CB    . MET   A  1  819  ? -17.884 75.107  86.441  1.00 16.50 ? 817  MET   A CB    1 
ATOM   6003  C  CG    . MET   A  1  819  ? -18.299 73.830  85.725  1.00 17.03 ? 817  MET   A CG    1 
ATOM   6004  S  SD    . MET   A  1  819  ? -20.094 73.682  85.603  1.00 18.80 ? 817  MET   A SD    1 
ATOM   6005  C  CE    . MET   A  1  819  ? -20.535 73.423  87.310  1.00 22.03 ? 817  MET   A CE    1 
ATOM   6006  N  N     . ILE   A  1  820  ? -15.198 74.263  84.569  1.00 15.27 ? 818  ILE   A N     1 
ATOM   6007  C  CA    . ILE   A  1  820  ? -14.723 74.138  83.197  1.00 16.65 ? 818  ILE   A CA    1 
ATOM   6008  C  C     . ILE   A  1  820  ? -15.606 73.129  82.500  1.00 14.40 ? 818  ILE   A C     1 
ATOM   6009  O  O     . ILE   A  1  820  ? -15.851 72.038  83.022  1.00 16.26 ? 818  ILE   A O     1 
ATOM   6010  C  CB    . ILE   A  1  820  ? -13.252 73.705  83.153  1.00 15.41 ? 818  ILE   A CB    1 
ATOM   6011  C  CG1   . ILE   A  1  820  ? -12.394 74.801  83.766  1.00 18.78 ? 818  ILE   A CG1   1 
ATOM   6012  C  CG2   . ILE   A  1  820  ? -12.849 73.412  81.707  1.00 17.99 ? 818  ILE   A CG2   1 
ATOM   6013  C  CD1   . ILE   A  1  820  ? -10.907 74.475  83.792  1.00 17.24 ? 818  ILE   A CD1   1 
ATOM   6014  N  N     . VAL   A  1  821  ? -16.097 73.499  81.323  1.00 16.06 ? 819  VAL   A N     1 
ATOM   6015  C  CA    . VAL   A  1  821  ? -16.995 72.662  80.540  1.00 16.83 ? 819  VAL   A CA    1 
ATOM   6016  C  C     . VAL   A  1  821  ? -16.366 72.501  79.175  1.00 17.76 ? 819  VAL   A C     1 
ATOM   6017  O  O     . VAL   A  1  821  ? -16.018 73.496  78.533  1.00 19.47 ? 819  VAL   A O     1 
ATOM   6018  C  CB    . VAL   A  1  821  ? -18.372 73.326  80.384  1.00 17.36 ? 819  VAL   A CB    1 
ATOM   6019  C  CG1   . VAL   A  1  821  ? -19.304 72.460  79.523  1.00 19.75 ? 819  VAL   A CG1   1 
ATOM   6020  C  CG2   . VAL   A  1  821  ? -18.977 73.598  81.750  1.00 16.34 ? 819  VAL   A CG2   1 
ATOM   6021  N  N     . ASP   A  1  822  ? -16.227 71.263  78.730  1.00 17.59 ? 820  ASP   A N     1 
ATOM   6022  C  CA    . ASP   A  1  822  ? -15.668 71.040  77.406  1.00 18.68 ? 820  ASP   A CA    1 
ATOM   6023  C  C     . ASP   A  1  822  ? -16.771 70.618  76.450  1.00 18.63 ? 820  ASP   A C     1 
ATOM   6024  O  O     . ASP   A  1  822  ? -17.936 70.516  76.827  1.00 18.57 ? 820  ASP   A O     1 
ATOM   6025  C  CB    . ASP   A  1  822  ? -14.445 70.115  77.450  1.00 19.79 ? 820  ASP   A CB    1 
ATOM   6026  C  CG    . ASP   A  1  822  ? -14.790 68.642  77.638  1.00 17.85 ? 820  ASP   A CG    1 
ATOM   6027  O  OD1   . ASP   A  1  822  ? -15.970 68.228  77.563  1.00 18.93 ? 820  ASP   A OD1   1 
ATOM   6028  O  OD2   . ASP   A  1  822  ? -13.824 67.879  77.878  1.00 20.14 ? 820  ASP   A OD2   1 
ATOM   6029  N  N     . SER   A  1  823  ? -16.392 70.379  75.192  1.00 18.72 ? 821  SER   A N     1 
ATOM   6030  C  CA    . SER   A  1  823  ? -17.399 70.065  74.192  1.00 19.67 ? 821  SER   A CA    1 
ATOM   6031  C  C     . SER   A  1  823  ? -17.990 68.665  74.326  1.00 21.64 ? 821  SER   A C     1 
ATOM   6032  O  O     . SER   A  1  823  ? -18.909 68.336  73.564  1.00 23.60 ? 821  SER   A O     1 
ATOM   6033  C  CB    . SER   A  1  823  ? -16.807 70.256  72.794  1.00 21.31 ? 821  SER   A CB    1 
ATOM   6034  O  OG    . SER   A  1  823  ? -15.683 69.412  72.617  1.00 24.47 ? 821  SER   A OG    1 
ATOM   6035  N  N     . SER   A  1  824  ? -17.514 67.823  75.249  1.00 18.67 ? 822  SER   A N     1 
ATOM   6036  C  CA    . SER   A  1  824  ? -18.100 66.506  75.443  1.00 19.44 ? 822  SER   A CA    1 
ATOM   6037  C  C     . SER   A  1  824  ? -19.222 66.506  76.473  1.00 19.76 ? 822  SER   A C     1 
ATOM   6038  O  O     . SER   A  1  824  ? -19.932 65.502  76.602  1.00 21.52 ? 822  SER   A O     1 
ATOM   6039  C  CB    . SER   A  1  824  ? -17.031 65.499  75.879  1.00 19.26 ? 822  SER   A CB    1 
ATOM   6040  O  OG    . SER   A  1  824  ? -16.626 65.739  77.222  1.00 18.60 ? 822  SER   A OG    1 
ATOM   6041  N  N     . ALA   A  1  825  ? -19.365 67.592  77.234  1.00 20.34 ? 823  ALA   A N     1 
ATOM   6042  C  CA    . ALA   A  1  825  ? -20.379 67.658  78.269  1.00 20.20 ? 823  ALA   A CA    1 
ATOM   6043  C  C     . ALA   A  1  825  ? -21.763 67.793  77.646  1.00 20.61 ? 823  ALA   A C     1 
ATOM   6044  O  O     . ALA   A  1  825  ? -21.921 68.302  76.534  1.00 21.73 ? 823  ALA   A O     1 
ATOM   6045  C  CB    . ALA   A  1  825  ? -20.115 68.869  79.159  1.00 19.98 ? 823  ALA   A CB    1 
ATOM   6046  N  N     . LEU   A  1  826  ? -22.769 67.329  78.372  1.00 21.56 ? 824  LEU   A N     1 
ATOM   6047  C  CA    . LEU   A  1  826  ? -24.150 67.429  77.922  1.00 21.69 ? 824  LEU   A CA    1 
ATOM   6048  C  C     . LEU   A  1  826  ? -24.707 68.778  78.362  1.00 23.39 ? 824  LEU   A C     1 
ATOM   6049  O  O     . LEU   A  1  826  ? -24.738 69.082  79.560  1.00 22.35 ? 824  LEU   A O     1 
ATOM   6050  C  CB    . LEU   A  1  826  ? -24.979 66.280  78.493  1.00 25.95 ? 824  LEU   A CB    1 
ATOM   6051  N  N     . ALA   A  1  827  ? -25.142 69.584  77.394  1.00 21.91 ? 825  ALA   A N     1 
ATOM   6052  C  CA    . ALA   A  1  827  ? -25.494 70.970  77.685  1.00 19.75 ? 825  ALA   A CA    1 
ATOM   6053  C  C     . ALA   A  1  827  ? -26.584 71.070  78.745  1.00 21.03 ? 825  ALA   A C     1 
ATOM   6054  O  O     . ALA   A  1  827  ? -26.478 71.891  79.666  1.00 19.25 ? 825  ALA   A O     1 
ATOM   6055  C  CB    . ALA   A  1  827  ? -25.917 71.686  76.402  1.00 22.62 ? 825  ALA   A CB    1 
ATOM   6056  N  N     . GLU   A  1  828  ? -27.628 70.240  78.645  1.00 20.77 ? 826  GLU   A N     1 
ATOM   6057  C  CA    . GLU   A  1  828  ? -28.726 70.312  79.605  1.00 21.31 ? 826  GLU   A CA    1 
ATOM   6058  C  C     . GLU   A  1  828  ? -28.234 70.032  81.015  1.00 20.65 ? 826  GLU   A C     1 
ATOM   6059  O  O     . GLU   A  1  828  ? -28.671 70.677  81.977  1.00 21.63 ? 826  GLU   A O     1 
ATOM   6060  C  CB    . GLU   A  1  828  ? -29.833 69.319  79.232  1.00 23.76 ? 826  GLU   A CB    1 
ATOM   6061  C  CG    . GLU   A  1  828  ? -30.672 69.726  78.018  1.00 27.65 ? 826  GLU   A CG    1 
ATOM   6062  C  CD    . GLU   A  1  828  ? -29.982 69.473  76.681  1.00 35.70 ? 826  GLU   A CD    1 
ATOM   6063  O  OE1   . GLU   A  1  828  ? -28.834 68.974  76.667  1.00 33.90 ? 826  GLU   A OE1   1 
ATOM   6064  O  OE2   . GLU   A  1  828  ? -30.601 69.776  75.637  1.00 40.46 ? 826  GLU   A OE2   1 
ATOM   6065  N  N     . GLN   A  1  829  ? -27.323 69.072  81.153  1.00 21.39 ? 827  GLN   A N     1 
ATOM   6066  C  CA    . GLN   A  1  829  ? -26.758 68.748  82.457  1.00 21.92 ? 827  GLN   A CA    1 
ATOM   6067  C  C     . GLN   A  1  829  ? -25.923 69.905  82.982  1.00 19.39 ? 827  GLN   A C     1 
ATOM   6068  O  O     . GLN   A  1  829  ? -26.039 70.298  84.153  1.00 20.24 ? 827  GLN   A O     1 
ATOM   6069  C  CB    . GLN   A  1  829  ? -25.888 67.506  82.300  1.00 23.53 ? 827  GLN   A CB    1 
ATOM   6070  C  CG    . GLN   A  1  829  ? -25.776 66.622  83.494  1.00 34.59 ? 827  GLN   A CG    1 
ATOM   6071  C  CD    . GLN   A  1  829  ? -25.145 65.306  83.106  1.00 36.04 ? 827  GLN   A CD    1 
ATOM   6072  O  OE1   . GLN   A  1  829  ? -24.131 65.281  82.405  1.00 31.56 ? 827  GLN   A OE1   1 
ATOM   6073  N  NE2   . GLN   A  1  829  ? -25.763 64.203  83.518  1.00 39.53 ? 827  GLN   A NE2   1 
ATOM   6074  N  N     . VAL   A  1  830  ? -25.063 70.458  82.130  1.00 18.84 ? 828  VAL   A N     1 
ATOM   6075  C  CA    . VAL   A  1  830  ? -24.271 71.620  82.506  1.00 19.68 ? 828  VAL   A CA    1 
ATOM   6076  C  C     . VAL   A  1  830  ? -25.171 72.741  82.985  1.00 18.51 ? 828  VAL   A C     1 
ATOM   6077  O  O     . VAL   A  1  830  ? -24.946 73.330  84.045  1.00 17.94 ? 828  VAL   A O     1 
ATOM   6078  C  CB    . VAL   A  1  830  ? -23.414 72.082  81.319  1.00 17.89 ? 828  VAL   A CB    1 
ATOM   6079  C  CG1   . VAL   A  1  830  ? -22.789 73.436  81.605  1.00 18.79 ? 828  VAL   A CG1   1 
ATOM   6080  C  CG2   . VAL   A  1  830  ? -22.341 71.034  80.990  1.00 19.19 ? 828  VAL   A CG2   1 
ATOM   6081  N  N     . VAL   A  1  831  ? -26.197 73.065  82.199  1.00 16.91 ? 829  VAL   A N     1 
ATOM   6082  C  CA    . VAL   A  1  831  ? -27.021 74.215  82.534  1.00 17.31 ? 829  VAL   A CA    1 
ATOM   6083  C  C     . VAL   A  1  831  ? -27.702 74.011  83.872  1.00 16.34 ? 829  VAL   A C     1 
ATOM   6084  O  O     . VAL   A  1  831  ? -27.729 74.924  84.703  1.00 16.51 ? 829  VAL   A O     1 
ATOM   6085  C  CB    . VAL   A  1  831  ? -28.021 74.517  81.409  1.00 18.42 ? 829  VAL   A CB    1 
ATOM   6086  C  CG1   . VAL   A  1  831  ? -29.018 75.545  81.870  1.00 17.71 ? 829  VAL   A CG1   1 
ATOM   6087  C  CG2   . VAL   A  1  831  ? -27.258 75.025  80.194  1.00 20.35 ? 829  VAL   A CG2   1 
ATOM   6088  N  N     . GLY   A  1  832  ? -28.245 72.817  84.111  1.00 17.61 ? 830  GLY   A N     1 
ATOM   6089  C  CA    . GLY   A  1  832  ? -28.850 72.559  85.408  1.00 17.72 ? 830  GLY   A CA    1 
ATOM   6090  C  C     . GLY   A  1  832  ? -27.864 72.744  86.547  1.00 17.27 ? 830  GLY   A C     1 
ATOM   6091  O  O     . GLY   A  1  832  ? -28.165 73.399  87.554  1.00 17.69 ? 830  GLY   A O     1 
ATOM   6092  N  N     . ASP   A  1  833  ? -26.649 72.226  86.381  1.00 17.10 ? 831  ASP   A N     1 
ATOM   6093  C  CA    . ASP   A  1  833  ? -25.671 72.341  87.456  1.00 16.83 ? 831  ASP   A CA    1 
ATOM   6094  C  C     . ASP   A  1  833  ? -25.163 73.763  87.613  1.00 17.78 ? 831  ASP   A C     1 
ATOM   6095  O  O     . ASP   A  1  833  ? -24.801 74.172  88.720  1.00 17.26 ? 831  ASP   A O     1 
ATOM   6096  C  CB    . ASP   A  1  833  ? -24.511 71.391  87.198  1.00 17.67 ? 831  ASP   A CB    1 
ATOM   6097  C  CG    . ASP   A  1  833  ? -24.918 69.966  87.343  1.00 17.43 ? 831  ASP   A CG    1 
ATOM   6098  O  OD1   . ASP   A  1  833  ? -25.986 69.717  87.940  1.00 22.08 ? 831  ASP   A OD1   1 
ATOM   6099  O  OD2   . ASP   A  1  833  ? -24.191 69.084  86.852  1.00 19.09 ? 831  ASP   A OD2   1 
ATOM   6100  N  N     . VAL   A  1  834  ? -25.113 74.521  86.524  1.00 16.01 ? 832  VAL   A N     1 
ATOM   6101  C  CA    . VAL   A  1  834  ? -24.693 75.914  86.589  1.00 16.09 ? 832  VAL   A CA    1 
ATOM   6102  C  C     . VAL   A  1  834  ? -25.751 76.765  87.275  1.00 18.48 ? 832  VAL   A C     1 
ATOM   6103  O  O     . VAL   A  1  834  ? -25.446 77.570  88.163  1.00 18.02 ? 832  VAL   A O     1 
ATOM   6104  C  CB    . VAL   A  1  834  ? -24.398 76.427  85.171  1.00 16.56 ? 832  VAL   A CB    1 
ATOM   6105  C  CG1   . VAL   A  1  834  ? -24.235 77.919  85.160  1.00 18.07 ? 832  VAL   A CG1   1 
ATOM   6106  C  CG2   . VAL   A  1  834  ? -23.147 75.744  84.642  1.00 18.29 ? 832  VAL   A CG2   1 
ATOM   6107  N  N     . ILE   A  1  835  ? -27.013 76.610  86.859  1.00 17.05 ? 833  ILE   A N     1 
ATOM   6108  C  CA    . ILE   A  1  835  ? -28.103 77.364  87.469  1.00 18.36 ? 833  ILE   A CA    1 
ATOM   6109  C  C     . ILE   A  1  835  ? -28.137 77.103  88.964  1.00 18.41 ? 833  ILE   A C     1 
ATOM   6110  O  O     . ILE   A  1  835  ? -28.251 78.032  89.773  1.00 21.45 ? 833  ILE   A O     1 
ATOM   6111  C  CB    . ILE   A  1  835  ? -29.442 77.022  86.794  1.00 19.57 ? 833  ILE   A CB    1 
ATOM   6112  C  CG1   . ILE   A  1  835  ? -29.497 77.568  85.360  1.00 21.77 ? 833  ILE   A CG1   1 
ATOM   6113  C  CG2   . ILE   A  1  835  ? -30.615 77.541  87.634  1.00 21.94 ? 833  ILE   A CG2   1 
ATOM   6114  C  CD1   . ILE   A  1  835  ? -29.762 79.050  85.248  1.00 24.01 ? 833  ILE   A CD1   1 
ATOM   6115  N  N     . THR   A  1  836  ? -28.007 75.842  89.355  1.00 18.78 ? 834  THR   A N     1 
ATOM   6116  C  CA    . THR   A  1  836  ? -27.986 75.512  90.771  1.00 20.00 ? 834  THR   A CA    1 
ATOM   6117  C  C     . THR   A  1  836  ? -26.752 76.097  91.441  1.00 19.15 ? 834  THR   A C     1 
ATOM   6118  O  O     . THR   A  1  836  ? -26.856 76.788  92.456  1.00 21.38 ? 834  THR   A O     1 
ATOM   6119  C  CB    . THR   A  1  836  ? -28.028 73.991  90.927  1.00 23.99 ? 834  THR   A CB    1 
ATOM   6120  O  OG1   . THR   A  1  836  ? -29.289 73.516  90.446  1.00 29.34 ? 834  THR   A OG1   1 
ATOM   6121  C  CG2   . THR   A  1  836  ? -27.865 73.590  92.373  1.00 28.72 ? 834  THR   A CG2   1 
ATOM   6122  N  N     . SER   A  1  837  ? -25.575 75.869  90.866  1.00 18.95 ? 835  SER   A N     1 
ATOM   6123  C  CA    . SER   A  1  837  ? -24.357 76.270  91.557  1.00 17.35 ? 835  SER   A CA    1 
ATOM   6124  C  C     . SER   A  1  837  ? -24.218 77.780  91.647  1.00 17.05 ? 835  SER   A C     1 
ATOM   6125  O  O     . SER   A  1  837  ? -23.670 78.291  92.627  1.00 17.93 ? 835  SER   A O     1 
ATOM   6126  C  CB    . SER   A  1  837  ? -23.124 75.683  90.863  1.00 18.33 ? 835  SER   A CB    1 
ATOM   6127  O  OG    . SER   A  1  837  ? -23.170 74.271  90.845  1.00 17.53 ? 835  SER   A OG    1 
ATOM   6128  N  N     . ALA   A  1  838  ? -24.667 78.510  90.630  1.00 16.60 ? 836  ALA   A N     1 
ATOM   6129  C  CA    . ALA   A  1  838  ? -24.443 79.943  90.620  1.00 16.71 ? 836  ALA   A CA    1 
ATOM   6130  C  C     . ALA   A  1  838  ? -25.527 80.718  91.339  1.00 18.71 ? 836  ALA   A C     1 
ATOM   6131  O  O     . ALA   A  1  838  ? -25.243 81.763  91.932  1.00 18.89 ? 836  ALA   A O     1 
ATOM   6132  C  CB    . ALA   A  1  838  ? -24.337 80.460  89.182  1.00 19.00 ? 836  ALA   A CB    1 
ATOM   6133  N  N     . PHE   A  1  839  ? -26.768 80.254  91.279  1.00 17.62 ? 837  PHE   A N     1 
ATOM   6134  C  CA    . PHE   A  1  839  ? -27.890 81.089  91.673  1.00 19.74 ? 837  PHE   A CA    1 
ATOM   6135  C  C     . PHE   A  1  839  ? -28.708 80.559  92.827  1.00 19.74 ? 837  PHE   A C     1 
ATOM   6136  O  O     . PHE   A  1  839  ? -29.472 81.340  93.408  1.00 20.73 ? 837  PHE   A O     1 
ATOM   6137  C  CB    . PHE   A  1  839  ? -28.805 81.365  90.474  1.00 20.12 ? 837  PHE   A CB    1 
ATOM   6138  C  CG    . PHE   A  1  839  ? -28.082 81.968  89.338  1.00 18.69 ? 837  PHE   A CG    1 
ATOM   6139  C  CD1   . PHE   A  1  839  ? -27.380 83.145  89.505  1.00 21.38 ? 837  PHE   A CD1   1 
ATOM   6140  C  CD2   . PHE   A  1  839  ? -28.057 81.338  88.103  1.00 21.51 ? 837  PHE   A CD2   1 
ATOM   6141  C  CE1   . PHE   A  1  839  ? -26.685 83.707  88.460  1.00 20.49 ? 837  PHE   A CE1   1 
ATOM   6142  C  CE2   . PHE   A  1  839  ? -27.362 81.893  87.054  1.00 25.79 ? 837  PHE   A CE2   1 
ATOM   6143  C  CZ    . PHE   A  1  839  ? -26.676 83.084  87.230  1.00 23.13 ? 837  PHE   A CZ    1 
ATOM   6144  N  N     . ASP   A  1  840  ? -28.583 79.281  93.177  1.00 21.11 ? 838  ASP   A N     1 
ATOM   6145  C  CA    . ASP   A  1  840  ? -29.166 78.792  94.417  1.00 22.77 ? 838  ASP   A CA    1 
ATOM   6146  C  C     . ASP   A  1  840  ? -28.733 79.690  95.565  1.00 21.43 ? 838  ASP   A C     1 
ATOM   6147  O  O     . ASP   A  1  840  ? -27.571 80.107  95.648  1.00 21.32 ? 838  ASP   A O     1 
ATOM   6148  C  CB    . ASP   A  1  840  ? -28.680 77.361  94.666  1.00 26.45 ? 838  ASP   A CB    1 
ATOM   6149  C  CG    . ASP   A  1  840  ? -29.301 76.724  95.881  1.00 32.17 ? 838  ASP   A CG    1 
ATOM   6150  O  OD1   . ASP   A  1  840  ? -28.771 76.932  96.997  1.00 33.44 ? 838  ASP   A OD1   1 
ATOM   6151  O  OD2   . ASP   A  1  840  ? -30.310 76.005  95.710  1.00 38.89 ? 838  ASP   A OD2   1 
ATOM   6152  N  N     . SER   A  1  841  ? -29.683 80.015  96.436  1.00 20.96 ? 839  SER   A N     1 
ATOM   6153  C  CA    . SER   A  1  841  ? -29.416 80.890  97.576  1.00 20.25 ? 839  SER   A CA    1 
ATOM   6154  C  C     . SER   A  1  841  ? -28.926 82.257  97.121  1.00 19.50 ? 839  SER   A C     1 
ATOM   6155  O  O     . SER   A  1  841  ? -28.185 82.931  97.834  1.00 19.06 ? 839  SER   A O     1 
ATOM   6156  C  CB    . SER   A  1  841  ? -28.431 80.251  98.560  1.00 23.64 ? 839  SER   A CB    1 
ATOM   6157  O  OG    . SER   A  1  841  ? -28.861 78.952  98.932  1.00 28.55 ? 839  SER   A OG    1 
ATOM   6158  N  N     . ALA   A  1  842  ? -29.313 82.658  95.911  1.00 20.05 ? 840  ALA   A N     1 
ATOM   6159  C  CA    . ALA   A  1  842  ? -28.857 83.904  95.314  1.00 17.19 ? 840  ALA   A CA    1 
ATOM   6160  C  C     . ALA   A  1  842  ? -27.334 83.997  95.285  1.00 18.26 ? 840  ALA   A C     1 
ATOM   6161  O  O     . ALA   A  1  842  ? -26.763 85.069  95.461  1.00 20.26 ? 840  ALA   A O     1 
ATOM   6162  C  CB    . ALA   A  1  842  ? -29.493 85.135  95.970  1.00 20.97 ? 840  ALA   A CB    1 
ATOM   6163  N  N     . GLY   A  1  843  ? -26.677 82.867  95.014  1.00 17.54 ? 841  GLY   A N     1 
ATOM   6164  C  CA    . GLY   A  1  843  ? -25.226 82.857  94.952  1.00 17.49 ? 841  GLY   A CA    1 
ATOM   6165  C  C     . GLY   A  1  843  ? -24.548 83.090  96.278  1.00 17.80 ? 841  GLY   A C     1 
ATOM   6166  O  O     . GLY   A  1  843  ? -23.336 83.310  96.313  1.00 18.63 ? 841  GLY   A O     1 
ATOM   6167  N  N     . GLN   A  1  844  ? -25.290 83.030  97.371  1.00 17.76 ? 842  GLN   A N     1 
ATOM   6168  C  CA    . GLN   A  1  844  ? -24.734 83.298  98.690  1.00 16.05 ? 842  GLN   A CA    1 
ATOM   6169  C  C     . GLN   A  1  844  ? -24.313 82.004  99.372  1.00 20.17 ? 842  GLN   A C     1 
ATOM   6170  O  O     . GLN   A  1  844  ? -24.689 81.683  100.497 1.00 20.41 ? 842  GLN   A O     1 
ATOM   6171  C  CB    . GLN   A  1  844  ? -25.725 84.106  99.513  1.00 18.48 ? 842  GLN   A CB    1 
ATOM   6172  C  CG    . GLN   A  1  844  ? -25.956 85.480  98.899  1.00 19.75 ? 842  GLN   A CG    1 
ATOM   6173  C  CD    . GLN   A  1  844  ? -27.154 86.203  99.481  1.00 19.80 ? 842  GLN   A CD    1 
ATOM   6174  O  OE1   . GLN   A  1  844  ? -27.025 87.314  99.976  1.00 20.07 ? 842  GLN   A OE1   1 
ATOM   6175  N  NE2   . GLN   A  1  844  ? -28.331 85.589  99.385  1.00 21.19 ? 842  GLN   A NE2   1 
ATOM   6176  N  N     . ARG   A  1  845  ? -23.537 81.223  98.633  1.00 18.52 ? 843  ARG   A N     1 
ATOM   6177  C  CA    . ARG   A  1  845  ? -22.831 80.071  99.157  1.00 19.38 ? 843  ARG   A CA    1 
ATOM   6178  C  C     . ARG   A  1  845  ? -21.363 80.315  98.886  1.00 18.79 ? 843  ARG   A C     1 
ATOM   6179  O  O     . ARG   A  1  845  ? -21.001 80.834  97.828  1.00 20.19 ? 843  ARG   A O     1 
ATOM   6180  C  CB    . ARG   A  1  845  ? -23.234 78.787  98.431  1.00 21.83 ? 843  ARG   A CB    1 
ATOM   6181  C  CG    . ARG   A  1  845  ? -24.668 78.335  98.649  1.00 20.88 ? 843  ARG   A CG    1 
ATOM   6182  C  CD    . ARG   A  1  845  ? -24.938 77.070  97.856  1.00 28.08 ? 843  ARG   A CD    1 
ATOM   6183  N  NE    . ARG   A  1  845  ? -26.287 76.563  98.063  1.00 30.41 ? 843  ARG   A NE    1 
ATOM   6184  C  CZ    . ARG   A  1  845  ? -26.604 75.625  98.944  1.00 33.63 ? 843  ARG   A CZ    1 
ATOM   6185  N  NH1   . ARG   A  1  845  ? -25.687 75.067  99.722  1.00 33.99 ? 843  ARG   A NH1   1 
ATOM   6186  N  NH2   . ARG   A  1  845  ? -27.872 75.235  99.048  1.00 37.19 ? 843  ARG   A NH2   1 
ATOM   6187  N  N     . CYS   A  1  846  ? -20.513 79.977  99.848  1.00 18.60 ? 844  CYS   A N     1 
ATOM   6188  C  CA    . CYS   A  1  846  ? -19.091 80.145  99.602  1.00 19.68 ? 844  CYS   A CA    1 
ATOM   6189  C  C     . CYS   A  1  846  ? -18.631 79.288  98.429  1.00 16.89 ? 844  CYS   A C     1 
ATOM   6190  O  O     . CYS   A  1  846  ? -17.665 79.638  97.746  1.00 16.40 ? 844  CYS   A O     1 
ATOM   6191  C  CB    . CYS   A  1  846  ? -18.316 79.787  100.864 1.00 18.20 ? 844  CYS   A CB    1 
ATOM   6192  S  SG    . CYS   A  1  846  ? -18.679 78.161  101.550 1.00 23.01 ? 844  CYS   A SG    1 
ATOM   6193  N  N     . SER   A  1  847  ? -19.295 78.164  98.212  1.00 17.09 ? 845  SER   A N     1 
ATOM   6194  C  CA    . SER   A  1  847  ? -19.012 77.216  97.138  1.00 15.03 ? 845  SER   A CA    1 
ATOM   6195  C  C     . SER   A  1  847  ? -19.618 77.612  95.798  1.00 17.44 ? 845  SER   A C     1 
ATOM   6196  O  O     . SER   A  1  847  ? -19.405 76.890  94.808  1.00 17.26 ? 845  SER   A O     1 
ATOM   6197  C  CB    . SER   A  1  847  ? -19.628 75.885  97.529  1.00 16.93 ? 845  SER   A CB    1 
ATOM   6198  O  OG    . SER   A  1  847  ? -20.993 76.117  97.869  1.00 19.38 ? 845  SER   A OG    1 
ATOM   6199  N  N     . ALA   A  1  848  ? -20.351 78.722  95.736  1.00 17.35 ? 846  ALA   A N     1 
ATOM   6200  C  CA    . ALA   A  1  848  ? -21.131 79.041  94.547  1.00 15.04 ? 846  ALA   A CA    1 
ATOM   6201  C  C     . ALA   A  1  848  ? -20.237 79.205  93.331  1.00 15.98 ? 846  ALA   A C     1 
ATOM   6202  O  O     . ALA   A  1  848  ? -19.107 79.686  93.406  1.00 16.44 ? 846  ALA   A O     1 
ATOM   6203  C  CB    . ALA   A  1  848  ? -21.932 80.328  94.765  1.00 17.31 ? 846  ALA   A CB    1 
ATOM   6204  N  N     . LEU   A  1  849  ? -20.782 78.829  92.186  1.00 16.64 ? 847  LEU   A N     1 
ATOM   6205  C  CA    . LEU   A  1  849  ? -20.057 78.972  90.937  1.00 16.80 ? 847  LEU   A CA    1 
ATOM   6206  C  C     . LEU   A  1  849  ? -19.982 80.444  90.566  1.00 16.08 ? 847  LEU   A C     1 
ATOM   6207  O  O     . LEU   A  1  849  ? -21.015 81.108  90.437  1.00 17.78 ? 847  LEU   A O     1 
ATOM   6208  C  CB    . LEU   A  1  849  ? -20.805 78.208  89.858  1.00 17.59 ? 847  LEU   A CB    1 
ATOM   6209  C  CG    . LEU   A  1  849  ? -20.199 78.373  88.471  1.00 16.82 ? 847  LEU   A CG    1 
ATOM   6210  C  CD1   . LEU   A  1  849  ? -18.771 77.853  88.439  1.00 16.99 ? 847  LEU   A CD1   1 
ATOM   6211  C  CD2   . LEU   A  1  849  ? -21.065 77.642  87.454  1.00 16.91 ? 847  LEU   A CD2   1 
ATOM   6212  N  N     . ARG   A  1  850  ? -18.761 80.951  90.407  1.00 16.56 ? 848  ARG   A N     1 
ATOM   6213  C  CA    . ARG   A  1  850  ? -18.532 82.343  90.062  1.00 17.84 ? 848  ARG   A CA    1 
ATOM   6214  C  C     . ARG   A  1  850  ? -18.079 82.524  88.629  1.00 18.96 ? 848  ARG   A C     1 
ATOM   6215  O  O     . ARG   A  1  850  ? -18.348 83.565  88.034  1.00 18.60 ? 848  ARG   A O     1 
ATOM   6216  C  CB    . ARG   A  1  850  ? -17.458 82.955  90.976  1.00 18.93 ? 848  ARG   A CB    1 
ATOM   6217  C  CG    . ARG   A  1  850  ? -17.731 82.792  92.453  1.00 19.23 ? 848  ARG   A CG    1 
ATOM   6218  C  CD    . ARG   A  1  850  ? -19.118 83.296  92.822  1.00 19.11 ? 848  ARG   A CD    1 
ATOM   6219  N  NE    . ARG   A  1  850  ? -19.308 83.224  94.263  1.00 19.63 ? 848  ARG   A NE    1 
ATOM   6220  C  CZ    . ARG   A  1  850  ? -20.452 83.479  94.875  1.00 19.42 ? 848  ARG   A CZ    1 
ATOM   6221  N  NH1   . ARG   A  1  850  ? -21.539 83.827  94.196  1.00 19.15 ? 848  ARG   A NH1   1 
ATOM   6222  N  NH2   . ARG   A  1  850  ? -20.507 83.389  96.202  1.00 20.44 ? 848  ARG   A NH2   1 
ATOM   6223  N  N     . VAL   A  1  851  ? -17.367 81.546  88.075  1.00 17.45 ? 849  VAL   A N     1 
ATOM   6224  C  CA    . VAL   A  1  851  ? -16.758 81.676  86.754  1.00 19.86 ? 849  VAL   A CA    1 
ATOM   6225  C  C     . VAL   A  1  851  ? -17.016 80.385  85.997  1.00 18.09 ? 849  VAL   A C     1 
ATOM   6226  O  O     . VAL   A  1  851  ? -16.434 79.346  86.320  1.00 19.06 ? 849  VAL   A O     1 
ATOM   6227  C  CB    . VAL   A  1  851  ? -15.249 81.948  86.813  1.00 23.68 ? 849  VAL   A CB    1 
ATOM   6228  C  CG1   . VAL   A  1  851  ? -14.719 82.194  85.400  1.00 25.06 ? 849  VAL   A CG1   1 
ATOM   6229  C  CG2   . VAL   A  1  851  ? -14.925 83.117  87.729  1.00 27.61 ? 849  VAL   A CG2   1 
ATOM   6230  N  N     . LEU   A  1  852  ? -17.873 80.448  84.987  1.00 17.01 ? 850  LEU   A N     1 
ATOM   6231  C  CA    . LEU   A  1  852  ? -18.120 79.321  84.099  1.00 17.19 ? 850  LEU   A CA    1 
ATOM   6232  C  C     . LEU   A  1  852  ? -17.230 79.476  82.876  1.00 16.66 ? 850  LEU   A C     1 
ATOM   6233  O  O     . LEU   A  1  852  ? -17.233 80.528  82.229  1.00 17.44 ? 850  LEU   A O     1 
ATOM   6234  C  CB    . LEU   A  1  852  ? -19.584 79.356  83.665  1.00 17.58 ? 850  LEU   A CB    1 
ATOM   6235  C  CG    . LEU   A  1  852  ? -20.009 78.290  82.660  1.00 17.49 ? 850  LEU   A CG    1 
ATOM   6236  C  CD1   . LEU   A  1  852  ? -19.885 76.899  83.251  1.00 18.09 ? 850  LEU   A CD1   1 
ATOM   6237  C  CD2   . LEU   A  1  852  ? -21.456 78.559  82.242  1.00 18.96 ? 850  LEU   A CD2   1 
ATOM   6238  N  N     . CYS   A  1  853  ? -16.455 78.436  82.576  1.00 16.72 ? 851  CYS   A N     1 
ATOM   6239  C  CA    . CYS   A  1  853  ? -15.494 78.469  81.483  1.00 17.63 ? 851  CYS   A CA    1 
ATOM   6240  C  C     . CYS   A  1  853  ? -15.942 77.473  80.436  1.00 16.26 ? 851  CYS   A C     1 
ATOM   6241  O  O     . CYS   A  1  853  ? -15.995 76.276  80.703  1.00 17.15 ? 851  CYS   A O     1 
ATOM   6242  C  CB    . CYS   A  1  853  ? -14.096 78.104  81.974  1.00 18.94 ? 851  CYS   A CB    1 
ATOM   6243  S  SG    . CYS   A  1  853  ? -13.564 79.027  83.421  1.00 20.42 ? 851  CYS   A SG    1 
ATOM   6244  N  N     . LEU   A  1  854  ? -16.282 77.975  79.257  1.00 17.07 ? 852  LEU   A N     1 
ATOM   6245  C  CA    . LEU   A  1  854  ? -16.924 77.185  78.216  1.00 17.65 ? 852  LEU   A CA    1 
ATOM   6246  C  C     . LEU   A  1  854  ? -15.975 77.034  77.040  1.00 17.64 ? 852  LEU   A C     1 
ATOM   6247  O  O     . LEU   A  1  854  ? -15.471 78.029  76.508  1.00 18.32 ? 852  LEU   A O     1 
ATOM   6248  C  CB    . LEU   A  1  854  ? -18.200 77.873  77.729  1.00 17.60 ? 852  LEU   A CB    1 
ATOM   6249  C  CG    . LEU   A  1  854  ? -19.280 78.065  78.791  1.00 18.46 ? 852  LEU   A CG    1 
ATOM   6250  C  CD1   . LEU   A  1  854  ? -20.480 78.808  78.197  1.00 17.73 ? 852  LEU   A CD1   1 
ATOM   6251  C  CD2   . LEU   A  1  854  ? -19.705 76.715  79.363  1.00 19.24 ? 852  LEU   A CD2   1 
ATOM   6252  N  N     . GLN   A  1  855  ? -15.772 75.797  76.608  1.00 17.41 ? 853  GLN   A N     1 
ATOM   6253  C  CA    . GLN   A  1  855  ? -14.969 75.594  75.414  1.00 17.39 ? 853  GLN   A CA    1 
ATOM   6254  C  C     . GLN   A  1  855  ? -15.642 76.291  74.235  1.00 19.40 ? 853  GLN   A C     1 
ATOM   6255  O  O     . GLN   A  1  855  ? -16.862 76.237  74.070  1.00 18.94 ? 853  GLN   A O     1 
ATOM   6256  C  CB    . GLN   A  1  855  ? -14.799 74.109  75.148  1.00 18.04 ? 853  GLN   A CB    1 
ATOM   6257  C  CG    . GLN   A  1  855  ? -13.751 73.863  74.081  1.00 19.79 ? 853  GLN   A CG    1 
ATOM   6258  C  CD    . GLN   A  1  855  ? -13.684 72.419  73.666  1.00 21.48 ? 853  GLN   A CD    1 
ATOM   6259  O  OE1   . GLN   A  1  855  ? -13.749 71.517  74.495  1.00 23.52 ? 853  GLN   A OE1   1 
ATOM   6260  N  NE2   . GLN   A  1  855  ? -13.539 72.190  72.364  1.00 25.87 ? 853  GLN   A NE2   1 
ATOM   6261  N  N     . GLU   A  1  856  ? -14.822 76.955  73.419  1.00 19.89 ? 854  GLU   A N     1 
ATOM   6262  C  CA    . GLU   A  1  856  ? -15.332 77.907  72.436  1.00 22.33 ? 854  GLU   A CA    1 
ATOM   6263  C  C     . GLU   A  1  856  ? -16.379 77.287  71.521  1.00 22.37 ? 854  GLU   A C     1 
ATOM   6264  O  O     . GLU   A  1  856  ? -17.399 77.918  71.226  1.00 23.86 ? 854  GLU   A O     1 
ATOM   6265  C  CB    . GLU   A  1  856  ? -14.161 78.464  71.627  1.00 23.93 ? 854  GLU   A CB    1 
ATOM   6266  C  CG    . GLU   A  1  856  ? -14.574 79.375  70.482  1.00 27.73 ? 854  GLU   A CG    1 
ATOM   6267  C  CD    . GLU   A  1  856  ? -15.350 80.588  70.942  1.00 36.68 ? 854  GLU   A CD    1 
ATOM   6268  O  OE1   . GLU   A  1  856  ? -15.019 81.133  72.018  1.00 32.10 ? 854  GLU   A OE1   1 
ATOM   6269  O  OE2   . GLU   A  1  856  ? -16.291 80.998  70.224  1.00 37.27 ? 854  GLU   A OE2   1 
ATOM   6270  N  N     . ASP   A  1  857  ? -16.165 76.038  71.094  1.00 22.32 ? 855  ASP   A N     1 
ATOM   6271  C  CA    . ASP   A  1  857  ? -17.047 75.395  70.122  1.00 24.30 ? 855  ASP   A CA    1 
ATOM   6272  C  C     . ASP   A  1  857  ? -18.464 75.185  70.643  1.00 24.87 ? 855  ASP   A C     1 
ATOM   6273  O  O     . ASP   A  1  857  ? -19.397 75.076  69.841  1.00 28.83 ? 855  ASP   A O     1 
ATOM   6274  C  CB    . ASP   A  1  857  ? -16.467 74.049  69.682  1.00 30.73 ? 855  ASP   A CB    1 
ATOM   6275  N  N     . VAL   A  1  858  ? -18.655 75.114  71.956  1.00 21.07 ? 856  VAL   A N     1 
ATOM   6276  C  CA    . VAL   A  1  858  ? -19.975 74.880  72.524  1.00 21.18 ? 856  VAL   A CA    1 
ATOM   6277  C  C     . VAL   A  1  858  ? -20.491 76.068  73.304  1.00 19.25 ? 856  VAL   A C     1 
ATOM   6278  O  O     . VAL   A  1  858  ? -21.628 76.015  73.811  1.00 20.51 ? 856  VAL   A O     1 
ATOM   6279  C  CB    . VAL   A  1  858  ? -20.012 73.601  73.374  1.00 21.86 ? 856  VAL   A CB    1 
ATOM   6280  C  CG1   . VAL   A  1  858  ? -19.755 72.394  72.490  1.00 23.58 ? 856  VAL   A CG1   1 
ATOM   6281  C  CG2   . VAL   A  1  858  ? -18.986 73.688  74.512  1.00 20.82 ? 856  VAL   A CG2   1 
ATOM   6282  N  N     . ALA   A  1  859  ? -19.712 77.147  73.397  1.00 19.64 ? 857  ALA   A N     1 
ATOM   6283  C  CA    . ALA   A  1  859  ? -20.041 78.232  74.316  1.00 18.70 ? 857  ALA   A CA    1 
ATOM   6284  C  C     . ALA   A  1  859  ? -21.349 78.911  73.945  1.00 20.61 ? 857  ALA   A C     1 
ATOM   6285  O  O     . ALA   A  1  859  ? -22.167 79.199  74.822  1.00 20.22 ? 857  ALA   A O     1 
ATOM   6286  C  CB    . ALA   A  1  859  ? -18.912 79.255  74.354  1.00 20.34 ? 857  ALA   A CB    1 
ATOM   6287  N  N     . ASP   A  1  860  ? -21.563 79.179  72.654  1.00 21.52 ? 858  ASP   A N     1 
ATOM   6288  C  CA    . ASP   A  1  860  ? -22.777 79.884  72.260  1.00 20.67 ? 858  ASP   A CA    1 
ATOM   6289  C  C     . ASP   A  1  860  ? -24.019 79.060  72.557  1.00 20.84 ? 858  ASP   A C     1 
ATOM   6290  O  O     . ASP   A  1  860  ? -25.008 79.583  73.080  1.00 22.12 ? 858  ASP   A O     1 
ATOM   6291  C  CB    . ASP   A  1  860  ? -22.715 80.259  70.784  1.00 22.72 ? 858  ASP   A CB    1 
ATOM   6292  C  CG    . ASP   A  1  860  ? -21.752 81.392  70.523  1.00 30.53 ? 858  ASP   A CG    1 
ATOM   6293  O  OD1   . ASP   A  1  860  ? -21.633 82.277  71.394  1.00 35.78 ? 858  ASP   A OD1   1 
ATOM   6294  O  OD2   . ASP   A  1  860  ? -21.113 81.394  69.451  1.00 46.76 ? 858  ASP   A OD2   1 
ATOM   6295  N  N     . ARG   A  1  861  ? -23.992 77.766  72.234  1.00 20.47 ? 859  ARG   A N     1 
ATOM   6296  C  CA    . ARG   A  1  861  ? -25.153 76.928  72.491  1.00 21.65 ? 859  ARG   A CA    1 
ATOM   6297  C  C     . ARG   A  1  861  ? -25.437 76.835  73.985  1.00 18.20 ? 859  ARG   A C     1 
ATOM   6298  O  O     . ARG   A  1  861  ? -26.588 76.946  74.415  1.00 20.92 ? 859  ARG   A O     1 
ATOM   6299  C  CB    . ARG   A  1  861  ? -24.948 75.539  71.891  1.00 28.64 ? 859  ARG   A CB    1 
ATOM   6300  C  CG    . ARG   A  1  861  ? -26.047 74.571  72.271  1.00 35.26 ? 859  ARG   A CG    1 
ATOM   6301  C  CD    . ARG   A  1  861  ? -26.038 73.309  71.431  1.00 45.21 ? 859  ARG   A CD    1 
ATOM   6302  N  NE    . ARG   A  1  861  ? -27.225 72.513  71.721  1.00 55.95 ? 859  ARG   A NE    1 
ATOM   6303  C  CZ    . ARG   A  1  861  ? -27.256 71.496  72.571  1.00 49.73 ? 859  ARG   A CZ    1 
ATOM   6304  N  NH1   . ARG   A  1  861  ? -26.162 71.075  73.184  1.00 52.23 ? 859  ARG   A NH1   1 
ATOM   6305  N  NH2   . ARG   A  1  861  ? -28.412 70.884  72.809  1.00 44.08 ? 859  ARG   A NH2   1 
ATOM   6306  N  N     . ILE   A  1  862  ? -24.394 76.658  74.795  1.00 17.99 ? 860  ILE   A N     1 
ATOM   6307  C  CA    . ILE   A  1  862  ? -24.608 76.537  76.232  1.00 19.18 ? 860  ILE   A CA    1 
ATOM   6308  C  C     . ILE   A  1  862  ? -25.081 77.858  76.815  1.00 19.06 ? 860  ILE   A C     1 
ATOM   6309  O  O     . ILE   A  1  862  ? -25.995 77.889  77.650  1.00 17.54 ? 860  ILE   A O     1 
ATOM   6310  C  CB    . ILE   A  1  862  ? -23.335 76.018  76.921  1.00 17.27 ? 860  ILE   A CB    1 
ATOM   6311  C  CG1   . ILE   A  1  862  ? -23.135 74.557  76.538  1.00 19.79 ? 860  ILE   A CG1   1 
ATOM   6312  C  CG2   . ILE   A  1  862  ? -23.442 76.184  78.439  1.00 21.05 ? 860  ILE   A CG2   1 
ATOM   6313  C  CD1   . ILE   A  1  862  ? -21.830 73.961  77.041  1.00 21.89 ? 860  ILE   A CD1   1 
ATOM   6314  N  N     . LEU   A  1  863  ? -24.497 78.966  76.359  1.00 18.08 ? 861  LEU   A N     1 
ATOM   6315  C  CA    A LEU   A  1  863  ? -24.904 80.280  76.854  0.48 18.38 ? 861  LEU   A CA    1 
ATOM   6316  C  CA    B LEU   A  1  863  ? -24.900 80.278  76.850  0.52 18.38 ? 861  LEU   A CA    1 
ATOM   6317  C  C     . LEU   A  1  863  ? -26.356 80.573  76.514  1.00 17.54 ? 861  LEU   A C     1 
ATOM   6318  O  O     . LEU   A  1  863  ? -27.099 81.105  77.345  1.00 17.53 ? 861  LEU   A O     1 
ATOM   6319  C  CB    A LEU   A  1  863  ? -23.999 81.372  76.283  0.48 20.23 ? 861  LEU   A CB    1 
ATOM   6320  C  CB    B LEU   A  1  863  ? -23.985 81.331  76.237  0.52 20.24 ? 861  LEU   A CB    1 
ATOM   6321  C  CG    A LEU   A  1  863  ? -22.694 81.658  77.022  0.48 22.57 ? 861  LEU   A CG    1 
ATOM   6322  C  CG    B LEU   A  1  863  ? -24.053 82.738  76.792  0.52 22.65 ? 861  LEU   A CG    1 
ATOM   6323  C  CD1   A LEU   A  1  863  ? -21.855 82.660  76.251  0.48 21.66 ? 861  LEU   A CD1   1 
ATOM   6324  C  CD1   B LEU   A  1  863  ? -23.924 82.700  78.309  0.52 21.54 ? 861  LEU   A CD1   1 
ATOM   6325  C  CD2   A LEU   A  1  863  ? -23.002 82.187  78.406  0.48 24.13 ? 861  LEU   A CD2   1 
ATOM   6326  C  CD2   B LEU   A  1  863  ? -22.940 83.550  76.160  0.52 24.94 ? 861  LEU   A CD2   1 
ATOM   6327  N  N     . THR   A  1  864  ? -26.779 80.247  75.293  1.00 18.52 ? 862  THR   A N     1 
ATOM   6328  C  CA    . THR   A  1  864  ? -28.182 80.436  74.945  1.00 19.53 ? 862  THR   A CA    1 
ATOM   6329  C  C     . THR   A  1  864  ? -29.078 79.627  75.867  1.00 17.16 ? 862  THR   A C     1 
ATOM   6330  O  O     . THR   A  1  864  ? -30.085 80.129  76.377  1.00 16.64 ? 862  THR   A O     1 
ATOM   6331  C  CB    . THR   A  1  864  ? -28.409 80.023  73.501  1.00 19.76 ? 862  THR   A CB    1 
ATOM   6332  O  OG1   . THR   A  1  864  ? -27.711 80.935  72.660  1.00 22.34 ? 862  THR   A OG1   1 
ATOM   6333  C  CG2   . THR   A  1  864  ? -29.906 80.062  73.148  1.00 21.20 ? 862  THR   A CG2   1 
ATOM   6334  N  N     . MET   A  1  865  ? -28.728 78.362  76.090  1.00 16.32 ? 863  MET   A N     1 
ATOM   6335  C  CA    . MET   A  1  865  ? -29.535 77.534  76.970  1.00 17.83 ? 863  MET   A CA    1 
ATOM   6336  C  C     . MET   A  1  865  ? -29.514 78.078  78.386  1.00 16.18 ? 863  MET   A C     1 
ATOM   6337  O  O     . MET   A  1  865  ? -30.541 78.102  79.063  1.00 15.75 ? 863  MET   A O     1 
ATOM   6338  C  CB    . MET   A  1  865  ? -29.018 76.103  76.929  1.00 17.86 ? 863  MET   A CB    1 
ATOM   6339  C  CG    . MET   A  1  865  ? -29.870 75.132  77.696  1.00 20.36 ? 863  MET   A CG    1 
ATOM   6340  S  SD    . MET   A  1  865  ? -29.208 73.466  77.568  1.00 23.69 ? 863  MET   A SD    1 
ATOM   6341  C  CE    . MET   A  1  865  ? -29.029 73.415  75.778  1.00 26.61 ? 863  MET   A CE    1 
ATOM   6342  N  N     . LEU   A  1  866  ? -28.346 78.526  78.845  1.00 16.39 ? 864  LEU   A N     1 
ATOM   6343  C  CA    . LEU   A  1  866  ? -28.237 79.044  80.197  1.00 15.96 ? 864  LEU   A CA    1 
ATOM   6344  C  C     . LEU   A  1  866  ? -29.103 80.285  80.381  1.00 15.27 ? 864  LEU   A C     1 
ATOM   6345  O  O     . LEU   A  1  866  ? -29.797 80.432  81.391  1.00 16.97 ? 864  LEU   A O     1 
ATOM   6346  C  CB    . LEU   A  1  866  ? -26.776 79.381  80.460  1.00 17.51 ? 864  LEU   A CB    1 
ATOM   6347  C  CG    . LEU   A  1  866  ? -26.497 79.998  81.823  1.00 18.55 ? 864  LEU   A CG    1 
ATOM   6348  C  CD1   . LEU   A  1  866  ? -26.966 79.040  82.902  1.00 20.34 ? 864  LEU   A CD1   1 
ATOM   6349  C  CD2   . LEU   A  1  866  ? -25.014 80.303  81.963  1.00 21.79 ? 864  LEU   A CD2   1 
ATOM   6350  N  N     . LYS   A  1  867  ? -29.064 81.202  79.414  1.00 16.85 ? 865  LYS   A N     1 
ATOM   6351  C  CA    . LYS   A  1  867  ? -29.901 82.391  79.515  1.00 18.02 ? 865  LYS   A CA    1 
ATOM   6352  C  C     . LYS   A  1  867  ? -31.379 82.023  79.498  1.00 17.31 ? 865  LYS   A C     1 
ATOM   6353  O  O     . LYS   A  1  867  ? -32.188 82.616  80.222  1.00 17.45 ? 865  LYS   A O     1 
ATOM   6354  C  CB    . LYS   A  1  867  ? -29.561 83.363  78.387  1.00 20.69 ? 865  LYS   A CB    1 
ATOM   6355  C  CG    . LYS   A  1  867  ? -28.173 83.985  78.564  1.00 21.28 ? 865  LYS   A CG    1 
ATOM   6356  C  CD    . LYS   A  1  867  ? -27.743 84.738  77.315  1.00 22.17 ? 865  LYS   A CD    1 
ATOM   6357  C  CE    . LYS   A  1  867  ? -26.338 85.302  77.497  1.00 27.59 ? 865  LYS   A CE    1 
ATOM   6358  N  NZ    . LYS   A  1  867  ? -25.809 85.913  76.245  1.00 32.80 ? 865  LYS   A NZ    1 
ATOM   6359  N  N     . GLY   A  1  868  ? -31.758 81.041  78.680  1.00 17.52 ? 866  GLY   A N     1 
ATOM   6360  C  CA    . GLY   A  1  868  ? -33.146 80.613  78.672  1.00 17.58 ? 866  GLY   A CA    1 
ATOM   6361  C  C     . GLY   A  1  868  ? -33.564 80.040  80.010  1.00 16.50 ? 866  GLY   A C     1 
ATOM   6362  O  O     . GLY   A  1  868  ? -34.658 80.317  80.507  1.00 18.10 ? 866  GLY   A O     1 
ATOM   6363  N  N     . ALA   A  1  869  ? -32.684 79.257  80.621  1.00 15.74 ? 867  ALA   A N     1 
ATOM   6364  C  CA    . ALA   A  1  869  ? -32.981 78.683  81.925  1.00 15.35 ? 867  ALA   A CA    1 
ATOM   6365  C  C     . ALA   A  1  869  ? -33.041 79.762  82.998  1.00 17.64 ? 867  ALA   A C     1 
ATOM   6366  O  O     . ALA   A  1  869  ? -33.880 79.700  83.907  1.00 17.67 ? 867  ALA   A O     1 
ATOM   6367  C  CB    . ALA   A  1  869  ? -31.911 77.662  82.288  1.00 16.11 ? 867  ALA   A CB    1 
ATOM   6368  N  N     . LEU   A  1  870  ? -32.148 80.754  82.911  1.00 16.60 ? 868  LEU   A N     1 
ATOM   6369  C  CA    . LEU   A  1  870  ? -32.149 81.859  83.864  1.00 17.41 ? 868  LEU   A CA    1 
ATOM   6370  C  C     . LEU   A  1  870  ? -33.516 82.510  83.918  1.00 20.35 ? 868  LEU   A C     1 
ATOM   6371  O  O     . LEU   A  1  870  ? -34.023 82.835  84.998  1.00 20.73 ? 868  LEU   A O     1 
ATOM   6372  C  CB    . LEU   A  1  870  ? -31.100 82.892  83.442  1.00 19.40 ? 868  LEU   A CB    1 
ATOM   6373  C  CG    . LEU   A  1  870  ? -30.791 84.091  84.347  1.00 21.89 ? 868  LEU   A CG    1 
ATOM   6374  C  CD1   . LEU   A  1  870  ? -29.768 83.707  85.398  1.00 26.20 ? 868  LEU   A CD1   1 
ATOM   6375  C  CD2   . LEU   A  1  870  ? -30.309 85.303  83.549  1.00 27.13 ? 868  LEU   A CD2   1 
ATOM   6376  N  N     . HIS   A  1  871  ? -34.143 82.683  82.761  1.00 17.69 ? 869  HIS   A N     1 
ATOM   6377  C  CA    . HIS   A  1  871  ? -35.403 83.418  82.736  1.00 19.15 ? 869  HIS   A CA    1 
ATOM   6378  C  C     . HIS   A  1  871  ? -36.576 82.624  83.270  1.00 21.81 ? 869  HIS   A C     1 
ATOM   6379  O  O     . HIS   A  1  871  ? -37.663 83.191  83.416  1.00 21.81 ? 869  HIS   A O     1 
ATOM   6380  C  CB    . HIS   A  1  871  ? -35.666 83.991  81.349  1.00 24.20 ? 869  HIS   A CB    1 
ATOM   6381  C  CG    . HIS   A  1  871  ? -34.752 85.127  81.020  1.00 25.28 ? 869  HIS   A CG    1 
ATOM   6382  N  ND1   . HIS   A  1  871  ? -34.868 86.367  81.612  1.00 30.62 ? 869  HIS   A ND1   1 
ATOM   6383  C  CD2   . HIS   A  1  871  ? -33.664 85.195  80.217  1.00 24.73 ? 869  HIS   A CD2   1 
ATOM   6384  C  CE1   . HIS   A  1  871  ? -33.909 87.158  81.166  1.00 30.18 ? 869  HIS   A CE1   1 
ATOM   6385  N  NE2   . HIS   A  1  871  ? -33.166 86.472  80.316  1.00 29.41 ? 869  HIS   A NE2   1 
ATOM   6386  N  N     . GLU   A  1  872  ? -36.376 81.358  83.601  1.00 17.66 ? 870  GLU   A N     1 
ATOM   6387  C  CA    . GLU   A  1  872  ? -37.424 80.554  84.206  1.00 19.16 ? 870  GLU   A CA    1 
ATOM   6388  C  C     . GLU   A  1  872  ? -37.372 80.566  85.723  1.00 18.56 ? 870  GLU   A C     1 
ATOM   6389  O  O     . GLU   A  1  872  ? -38.197 79.907  86.363  1.00 19.41 ? 870  GLU   A O     1 
ATOM   6390  C  CB    . GLU   A  1  872  ? -37.328 79.114  83.707  1.00 18.48 ? 870  GLU   A CB    1 
ATOM   6391  C  CG    . GLU   A  1  872  ? -37.513 78.999  82.202  1.00 19.37 ? 870  GLU   A CG    1 
ATOM   6392  C  CD    . GLU   A  1  872  ? -38.887 79.442  81.755  1.00 23.07 ? 870  GLU   A CD    1 
ATOM   6393  O  OE1   . GLU   A  1  872  ? -39.833 79.371  82.571  1.00 22.66 ? 870  GLU   A OE1   1 
ATOM   6394  O  OE2   . GLU   A  1  872  ? -39.027 79.862  80.586  1.00 22.19 ? 870  GLU   A OE2   1 
ATOM   6395  N  N     . LEU   A  1  873  ? -36.425 81.290  86.313  1.00 18.06 ? 871  LEU   A N     1 
ATOM   6396  C  CA    . LEU   A  1  873  ? -36.303 81.334  87.760  1.00 18.08 ? 871  LEU   A CA    1 
ATOM   6397  C  C     . LEU   A  1  873  ? -37.283 82.332  88.356  1.00 19.09 ? 871  LEU   A C     1 
ATOM   6398  O  O     . LEU   A  1  873  ? -37.513 83.409  87.803  1.00 21.81 ? 871  LEU   A O     1 
ATOM   6399  C  CB    . LEU   A  1  873  ? -34.886 81.738  88.153  1.00 18.55 ? 871  LEU   A CB    1 
ATOM   6400  C  CG    . LEU   A  1  873  ? -33.817 80.767  87.679  1.00 18.81 ? 871  LEU   A CG    1 
ATOM   6401  C  CD1   . LEU   A  1  873  ? -32.441 81.309  88.082  1.00 19.64 ? 871  LEU   A CD1   1 
ATOM   6402  C  CD2   . LEU   A  1  873  ? -34.058 79.407  88.301  1.00 23.07 ? 871  LEU   A CD2   1 
ATOM   6403  N  N     . HIS   A  1  874  ? -37.852 81.962  89.495  1.00 19.47 ? 872  HIS   A N     1 
ATOM   6404  C  CA    . HIS   A  1  874  ? -38.761 82.814  90.240  1.00 18.82 ? 872  HIS   A CA    1 
ATOM   6405  C  C     . HIS   A  1  874  ? -37.997 83.375  91.432  1.00 17.26 ? 872  HIS   A C     1 
ATOM   6406  O  O     . HIS   A  1  874  ? -37.528 82.618  92.294  1.00 19.17 ? 872  HIS   A O     1 
ATOM   6407  C  CB    . HIS   A  1  874  ? -39.959 81.984  90.696  1.00 19.64 ? 872  HIS   A CB    1 
ATOM   6408  C  CG    . HIS   A  1  874  ? -40.994 82.753  91.454  1.00 23.14 ? 872  HIS   A CG    1 
ATOM   6409  N  ND1   . HIS   A  1  874  ? -42.190 82.185  91.836  1.00 29.46 ? 872  HIS   A ND1   1 
ATOM   6410  C  CD2   . HIS   A  1  874  ? -41.026 84.032  91.898  1.00 29.87 ? 872  HIS   A CD2   1 
ATOM   6411  C  CE1   . HIS   A  1  874  ? -42.910 83.077  92.492  1.00 26.37 ? 872  HIS   A CE1   1 
ATOM   6412  N  NE2   . HIS   A  1  874  ? -42.229 84.208  92.543  1.00 24.64 ? 872  HIS   A NE2   1 
ATOM   6413  N  N     . ILE   A  1  875  ? -37.876 84.696  91.466  1.00 18.97 ? 873  ILE   A N     1 
ATOM   6414  C  CA    . ILE   A  1  875  ? -37.192 85.420  92.527  1.00 19.49 ? 873  ILE   A CA    1 
ATOM   6415  C  C     . ILE   A  1  875  ? -38.250 86.068  93.404  1.00 23.68 ? 873  ILE   A C     1 
ATOM   6416  O  O     . ILE   A  1  875  ? -39.147 86.762  92.906  1.00 22.93 ? 873  ILE   A O     1 
ATOM   6417  C  CB    . ILE   A  1  875  ? -36.252 86.488  91.946  1.00 23.59 ? 873  ILE   A CB    1 
ATOM   6418  C  CG1   . ILE   A  1  875  ? -35.042 85.853  91.262  1.00 29.41 ? 873  ILE   A CG1   1 
ATOM   6419  C  CG2   . ILE   A  1  875  ? -35.752 87.399  93.049  1.00 25.28 ? 873  ILE   A CG2   1 
ATOM   6420  C  CD1   . ILE   A  1  875  ? -35.307 85.242  89.907  1.00 34.83 ? 873  ILE   A CD1   1 
ATOM   6421  N  N     . GLY   A  1  876  ? -38.145 85.861  94.707  1.00 21.48 ? 874  GLY   A N     1 
ATOM   6422  C  CA    . GLY   A  1  876  ? -39.099 86.495  95.590  1.00 20.94 ? 874  GLY   A CA    1 
ATOM   6423  C  C     . GLY   A  1  876  ? -38.877 86.098  97.028  1.00 21.15 ? 874  GLY   A C     1 
ATOM   6424  O  O     . GLY   A  1  876  ? -37.901 85.425  97.371  1.00 20.87 ? 874  GLY   A O     1 
ATOM   6425  N  N     . ARG   A  1  877  ? -39.796 86.558  97.873  1.00 22.80 ? 875  ARG   A N     1 
ATOM   6426  C  CA    . ARG   A  1  877  ? -39.781 86.165  99.271  1.00 21.58 ? 875  ARG   A CA    1 
ATOM   6427  C  C     . ARG   A  1  877  ? -39.950 84.656  99.367  1.00 20.42 ? 875  ARG   A C     1 
ATOM   6428  O  O     . ARG   A  1  877  ? -40.789 84.066  98.682  1.00 22.28 ? 875  ARG   A O     1 
ATOM   6429  C  CB    . ARG   A  1  877  ? -40.906 86.882  100.012 1.00 29.52 ? 875  ARG   A CB    1 
ATOM   6430  C  CG    . ARG   A  1  877  ? -40.712 86.907  101.503 1.00 26.60 ? 875  ARG   A CG    1 
ATOM   6431  C  CD    . ARG   A  1  877  ? -41.799 87.727  102.153 1.00 30.50 ? 875  ARG   A CD    1 
ATOM   6432  N  NE    . ARG   A  1  877  ? -43.002 86.948  102.396 1.00 29.08 ? 875  ARG   A NE    1 
ATOM   6433  C  CZ    . ARG   A  1  877  ? -44.064 87.419  103.034 1.00 38.28 ? 875  ARG   A CZ    1 
ATOM   6434  N  NH1   . ARG   A  1  877  ? -44.119 88.675  103.443 1.00 37.19 ? 875  ARG   A NH1   1 
ATOM   6435  N  NH2   . ARG   A  1  877  ? -45.090 86.607  103.275 1.00 34.07 ? 875  ARG   A NH2   1 
ATOM   6436  N  N     . THR   A  1  878  ? -39.128 84.023  100.200 1.00 21.24 ? 876  THR   A N     1 
ATOM   6437  C  CA    . THR   A  1  878  ? -38.901 82.588  100.100 1.00 19.48 ? 876  THR   A CA    1 
ATOM   6438  C  C     . THR   A  1  878  ? -39.913 81.746  100.858 1.00 21.17 ? 876  THR   A C     1 
ATOM   6439  O  O     . THR   A  1  878  ? -39.732 80.529  100.948 1.00 21.77 ? 876  THR   A O     1 
ATOM   6440  C  CB    . THR   A  1  878  ? -37.489 82.243  100.575 1.00 21.55 ? 876  THR   A CB    1 
ATOM   6441  O  OG1   . THR   A  1  878  ? -37.255 82.855  101.846 1.00 23.99 ? 876  THR   A OG1   1 
ATOM   6442  C  CG2   . THR   A  1  878  ? -36.471 82.736  99.581  1.00 26.11 ? 876  THR   A CG2   1 
ATOM   6443  N  N     . ASP   A  1  879  ? -40.963 82.347  101.397 1.00 20.74 ? 877  ASP   A N     1 
ATOM   6444  C  CA    . ASP   A  1  879  ? -42.005 81.569  102.052 1.00 23.77 ? 877  ASP   A CA    1 
ATOM   6445  C  C     . ASP   A  1  879  ? -43.043 81.024  101.073 1.00 22.27 ? 877  ASP   A C     1 
ATOM   6446  O  O     . ASP   A  1  879  ? -44.182 80.747  101.462 1.00 22.76 ? 877  ASP   A O     1 
ATOM   6447  C  CB    . ASP   A  1  879  ? -42.654 82.369  103.184 1.00 21.82 ? 877  ASP   A CB    1 
ATOM   6448  C  CG    . ASP   A  1  879  ? -43.355 83.623  102.693 1.00 28.97 ? 877  ASP   A CG    1 
ATOM   6449  O  OD1   . ASP   A  1  879  ? -42.893 84.235  101.705 1.00 30.80 ? 877  ASP   A OD1   1 
ATOM   6450  O  OD2   . ASP   A  1  879  ? -44.384 83.994  103.298 1.00 29.26 ? 877  ASP   A OD2   1 
ATOM   6451  N  N     . ARG   A  1  880  ? -42.658 80.865  99.810  1.00 22.00 ? 878  ARG   A N     1 
ATOM   6452  C  CA    . ARG   A  1  880  ? -43.463 80.185  98.806  1.00 21.24 ? 878  ARG   A CA    1 
ATOM   6453  C  C     . ARG   A  1  880  ? -42.591 79.127  98.161  1.00 19.37 ? 878  ARG   A C     1 
ATOM   6454  O  O     . ARG   A  1  880  ? -41.456 79.413  97.765  1.00 20.09 ? 878  ARG   A O     1 
ATOM   6455  C  CB    . ARG   A  1  880  ? -43.935 81.142  97.711  1.00 25.08 ? 878  ARG   A CB    1 
ATOM   6456  C  CG    . ARG   A  1  880  ? -44.972 82.152  98.162  1.00 27.85 ? 878  ARG   A CG    1 
ATOM   6457  C  CD    . ARG   A  1  880  ? -45.358 83.045  96.980  1.00 32.73 ? 878  ARG   A CD    1 
ATOM   6458  N  NE    . ARG   A  1  880  ? -46.292 84.090  97.376  1.00 50.79 ? 878  ARG   A NE    1 
ATOM   6459  C  CZ    . ARG   A  1  880  ? -47.559 84.139  96.988  1.00 52.47 ? 878  ARG   A CZ    1 
ATOM   6460  N  NH1   . ARG   A  1  880  ? -48.066 83.232  96.169  1.00 55.47 ? 878  ARG   A NH1   1 
ATOM   6461  N  NH2   . ARG   A  1  880  ? -48.334 85.126  97.429  1.00 55.55 ? 878  ARG   A NH2   1 
ATOM   6462  N  N     . LEU   A  1  881  ? -43.122 77.908  98.055  1.00 18.30 ? 879  LEU   A N     1 
ATOM   6463  C  CA    . LEU   A  1  881  ? -42.380 76.815  97.435  1.00 17.14 ? 879  LEU   A CA    1 
ATOM   6464  C  C     . LEU   A  1  881  ? -41.963 77.148  96.003  1.00 18.79 ? 879  LEU   A C     1 
ATOM   6465  O  O     . LEU   A  1  881  ? -40.918 76.674  95.526  1.00 18.45 ? 879  LEU   A O     1 
ATOM   6466  C  CB    . LEU   A  1  881  ? -43.233 75.548  97.466  1.00 20.18 ? 879  LEU   A CB    1 
ATOM   6467  C  CG    . LEU   A  1  881  ? -42.607 74.266  96.934  1.00 20.27 ? 879  LEU   A CG    1 
ATOM   6468  C  CD1   . LEU   A  1  881  ? -41.482 73.789  97.854  1.00 21.27 ? 879  LEU   A CD1   1 
ATOM   6469  C  CD2   . LEU   A  1  881  ? -43.667 73.202  96.774  1.00 21.96 ? 879  LEU   A CD2   1 
ATOM   6470  N  N     . SER   A  1  882  ? -42.743 77.976  95.307  1.00 18.87 ? 880  SER   A N     1 
ATOM   6471  C  CA    . SER   A  1  882  ? -42.431 78.284  93.919  1.00 18.47 ? 880  SER   A CA    1 
ATOM   6472  C  C     . SER   A  1  882  ? -41.247 79.217  93.763  1.00 21.16 ? 880  SER   A C     1 
ATOM   6473  O  O     . SER   A  1  882  ? -40.820 79.456  92.628  1.00 21.42 ? 880  SER   A O     1 
ATOM   6474  C  CB    . SER   A  1  882  ? -43.634 78.935  93.242  1.00 19.26 ? 880  SER   A CB    1 
ATOM   6475  O  OG    . SER   A  1  882  ? -43.957 80.138  93.907  1.00 23.45 ? 880  SER   A OG    1 
ATOM   6476  N  N     . VAL   A  1  883  ? -40.698 79.751  94.853  1.00 19.61 ? 881  VAL   A N     1 
ATOM   6477  C  CA    . VAL   A  1  883  ? -39.575 80.674  94.735  1.00 20.14 ? 881  VAL   A CA    1 
ATOM   6478  C  C     . VAL   A  1  883  ? -38.274 79.895  94.617  1.00 19.48 ? 881  VAL   A C     1 
ATOM   6479  O  O     . VAL   A  1  883  ? -37.972 79.017  95.437  1.00 22.40 ? 881  VAL   A O     1 
ATOM   6480  C  CB    . VAL   A  1  883  ? -39.539 81.659  95.909  1.00 21.55 ? 881  VAL   A CB    1 
ATOM   6481  C  CG1   . VAL   A  1  883  ? -38.234 82.447  95.886  1.00 20.46 ? 881  VAL   A CG1   1 
ATOM   6482  C  CG2   . VAL   A  1  883  ? -40.707 82.595  95.810  1.00 20.63 ? 881  VAL   A CG2   1 
ATOM   6483  N  N     . ASP   A  1  884  ? -37.495 80.224  93.598  1.00 17.73 ? 882  ASP   A N     1 
ATOM   6484  C  CA    . ASP   A  1  884  ? -36.213 79.579  93.360  1.00 20.30 ? 882  ASP   A CA    1 
ATOM   6485  C  C     . ASP   A  1  884  ? -35.063 80.345  93.975  1.00 22.47 ? 882  ASP   A C     1 
ATOM   6486  O  O     . ASP   A  1  884  ? -34.121 79.734  94.496  1.00 25.36 ? 882  ASP   A O     1 
ATOM   6487  C  CB    . ASP   A  1  884  ? -35.965 79.470  91.859  1.00 18.76 ? 882  ASP   A CB    1 
ATOM   6488  C  CG    . ASP   A  1  884  ? -37.057 78.712  91.170  1.00 17.95 ? 882  ASP   A CG    1 
ATOM   6489  O  OD1   . ASP   A  1  884  ? -37.276 77.553  91.566  1.00 20.52 ? 882  ASP   A OD1   1 
ATOM   6490  O  OD2   . ASP   A  1  884  ? -37.694 79.293  90.275  1.00 19.42 ? 882  ASP   A OD2   1 
ATOM   6491  N  N     . VAL   A  1  885  ? -35.120 81.670  93.911  1.00 19.31 ? 883  VAL   A N     1 
ATOM   6492  C  CA    . VAL   A  1  885  ? -34.014 82.526  94.313  1.00 21.52 ? 883  VAL   A CA    1 
ATOM   6493  C  C     . VAL   A  1  885  ? -34.570 83.548  95.286  1.00 20.29 ? 883  VAL   A C     1 
ATOM   6494  O  O     . VAL   A  1  885  ? -35.500 84.289  94.948  1.00 19.53 ? 883  VAL   A O     1 
ATOM   6495  C  CB    . VAL   A  1  885  ? -33.376 83.226  93.105  1.00 21.19 ? 883  VAL   A CB    1 
ATOM   6496  C  CG1   . VAL   A  1  885  ? -32.223 84.130  93.550  1.00 22.43 ? 883  VAL   A CG1   1 
ATOM   6497  C  CG2   . VAL   A  1  885  ? -32.876 82.195  92.101  1.00 23.39 ? 883  VAL   A CG2   1 
ATOM   6498  N  N     . GLY   A  1  886  ? -34.015 83.583  96.489  1.00 19.88 ? 884  GLY   A N     1 
ATOM   6499  C  CA    . GLY   A  1  886  ? -34.424 84.549  97.474  1.00 18.65 ? 884  GLY   A CA    1 
ATOM   6500  C  C     . GLY   A  1  886  ? -33.619 85.825  97.435  1.00 18.32 ? 884  GLY   A C     1 
ATOM   6501  O  O     . GLY   A  1  886  ? -32.915 86.135  96.462  1.00 19.90 ? 884  GLY   A O     1 
ATOM   6502  N  N     . PRO   A  1  887  ? -33.707 86.592  98.515  1.00 19.35 ? 885  PRO   A N     1 
ATOM   6503  C  CA    . PRO   A  1  887  ? -33.065 87.904  98.558  1.00 19.55 ? 885  PRO   A CA    1 
ATOM   6504  C  C     . PRO   A  1  887  ? -31.593 87.758  98.902  1.00 19.18 ? 885  PRO   A C     1 
ATOM   6505  O  O     . PRO   A  1  887  ? -31.126 86.709  99.344  1.00 20.23 ? 885  PRO   A O     1 
ATOM   6506  C  CB    . PRO   A  1  887  ? -33.807 88.593  99.710  1.00 19.36 ? 885  PRO   A CB    1 
ATOM   6507  C  CG    . PRO   A  1  887  ? -34.132 87.458  100.655 1.00 21.68 ? 885  PRO   A CG    1 
ATOM   6508  C  CD    . PRO   A  1  887  ? -34.499 86.315  99.731  1.00 21.56 ? 885  PRO   A CD    1 
ATOM   6509  N  N     . VAL   A  1  888  ? -30.869 88.844  98.684  1.00 19.03 ? 886  VAL   A N     1 
ATOM   6510  C  CA    . VAL   A  1  888  ? -29.574 88.990  99.321  1.00 19.90 ? 886  VAL   A CA    1 
ATOM   6511  C  C     . VAL   A  1  888  ? -29.775 89.511  100.740 1.00 20.19 ? 886  VAL   A C     1 
ATOM   6512  O  O     . VAL   A  1  888  ? -30.808 90.097  101.074 1.00 21.29 ? 886  VAL   A O     1 
ATOM   6513  C  CB    . VAL   A  1  888  ? -28.627 89.870  98.493  1.00 21.88 ? 886  VAL   A CB    1 
ATOM   6514  C  CG1   . VAL   A  1  888  ? -28.441 89.258  97.100  1.00 22.21 ? 886  VAL   A CG1   1 
ATOM   6515  C  CG2   . VAL   A  1  888  ? -29.143 91.270  98.379  1.00 25.42 ? 886  VAL   A CG2   1 
ATOM   6516  N  N     . ILE   A  1  889  ? -28.780 89.273  101.596 1.00 21.10 ? 887  ILE   A N     1 
ATOM   6517  C  CA    . ILE   A  1  889  ? -29.033 89.335  103.035 1.00 21.74 ? 887  ILE   A CA    1 
ATOM   6518  C  C     . ILE   A  1  889  ? -29.304 90.760  103.507 1.00 20.86 ? 887  ILE   A C     1 
ATOM   6519  O  O     . ILE   A  1  889  ? -30.095 90.971  104.434 1.00 22.37 ? 887  ILE   A O     1 
ATOM   6520  C  CB    . ILE   A  1  889  ? -27.904 88.645  103.824 1.00 23.03 ? 887  ILE   A CB    1 
ATOM   6521  C  CG1   . ILE   A  1  889  ? -28.268 88.551  105.312 1.00 23.00 ? 887  ILE   A CG1   1 
ATOM   6522  C  CG2   . ILE   A  1  889  ? -26.568 89.370  103.621 1.00 22.91 ? 887  ILE   A CG2   1 
ATOM   6523  C  CD1   . ILE   A  1  889  ? -29.536 87.765  105.587 1.00 23.76 ? 887  ILE   A CD1   1 
ATOM   6524  N  N     . THR   A  1  890  ? -28.657 91.759  102.912 1.00 21.99 ? 888  THR   A N     1 
ATOM   6525  C  CA    . THR   A  1  890  ? -28.817 93.128  103.394 1.00 22.46 ? 888  THR   A CA    1 
ATOM   6526  C  C     . THR   A  1  890  ? -28.745 94.094  102.227 1.00 22.59 ? 888  THR   A C     1 
ATOM   6527  O  O     . THR   A  1  890  ? -28.278 93.757  101.139 1.00 22.72 ? 888  THR   A O     1 
ATOM   6528  C  CB    . THR   A  1  890  ? -27.690 93.550  104.349 1.00 25.83 ? 888  THR   A CB    1 
ATOM   6529  O  OG1   . THR   A  1  890  ? -26.440 93.466  103.655 1.00 26.29 ? 888  THR   A OG1   1 
ATOM   6530  C  CG2   . THR   A  1  890  ? -27.651 92.693  105.611 1.00 25.93 ? 888  THR   A CG2   1 
ATOM   6531  N  N     . SER   A  1  891  ? -29.166 95.331  102.490 1.00 25.52 ? 889  SER   A N     1 
ATOM   6532  C  CA    A SER   A  1  891  ? -29.028 96.393  101.498 0.40 27.27 ? 889  SER   A CA    1 
ATOM   6533  C  CA    B SER   A  1  891  ? -29.028 96.372  101.480 0.60 27.26 ? 889  SER   A CA    1 
ATOM   6534  C  C     . SER   A  1  891  ? -27.565 96.636  101.157 1.00 26.83 ? 889  SER   A C     1 
ATOM   6535  O  O     . SER   A  1  891  ? -27.231 96.948  100.009 1.00 26.78 ? 889  SER   A O     1 
ATOM   6536  C  CB    A SER   A  1  891  ? -29.659 97.687  102.016 0.40 27.11 ? 889  SER   A CB    1 
ATOM   6537  C  CB    B SER   A  1  891  ? -29.705 97.657  101.954 0.60 27.09 ? 889  SER   A CB    1 
ATOM   6538  O  OG    A SER   A  1  891  ? -31.060 97.564  102.167 0.40 27.82 ? 889  SER   A OG    1 
ATOM   6539  O  OG    B SER   A  1  891  ? -29.069 98.150  103.117 0.60 31.26 ? 889  SER   A OG    1 
ATOM   6540  N  N     . GLU   A  1  892  ? -26.679 96.512  102.146 1.00 25.08 ? 890  GLU   A N     1 
ATOM   6541  C  CA    . GLU   A  1  892  ? -25.260 96.729  101.882 1.00 27.08 ? 890  GLU   A CA    1 
ATOM   6542  C  C     . GLU   A  1  892  ? -24.717 95.661  100.948 1.00 29.13 ? 890  GLU   A C     1 
ATOM   6543  O  O     . GLU   A  1  892  ? -23.936 95.961  100.038 1.00 27.68 ? 890  GLU   A O     1 
ATOM   6544  C  CB    . GLU   A  1  892  ? -24.470 96.746  103.188 1.00 27.63 ? 890  GLU   A CB    1 
ATOM   6545  C  CG    . GLU   A  1  892  ? -24.995 97.730  104.222 1.00 38.04 ? 890  GLU   A CG    1 
ATOM   6546  C  CD    . GLU   A  1  892  ? -25.943 97.081  105.218 1.00 40.77 ? 890  GLU   A CD    1 
ATOM   6547  O  OE1   . GLU   A  1  892  ? -27.153 96.997  104.932 1.00 34.53 ? 890  GLU   A OE1   1 
ATOM   6548  O  OE2   . GLU   A  1  892  ? -25.469 96.647  106.290 1.00 54.07 ? 890  GLU   A OE2   1 
ATOM   6549  N  N     . ALA   A  1  893  ? -25.110 94.407  101.173 1.00 25.40 ? 891  ALA   A N     1 
ATOM   6550  C  CA    . ALA   A  1  893  ? -24.717 93.339  100.261 1.00 25.30 ? 891  ALA   A CA    1 
ATOM   6551  C  C     . ALA   A  1  893  ? -25.250 93.611  98.863  1.00 26.69 ? 891  ALA   A C     1 
ATOM   6552  O  O     . ALA   A  1  893  ? -24.516 93.503  97.875  1.00 24.92 ? 891  ALA   A O     1 
ATOM   6553  C  CB    . ALA   A  1  893  ? -25.202 91.990  100.795 1.00 24.74 ? 891  ALA   A CB    1 
ATOM   6554  N  N     . LYS   A  1  894  ? -26.527 93.996  98.766  1.00 23.40 ? 892  LYS   A N     1 
ATOM   6555  C  CA    . LYS   A  1  894  ? -27.117 94.355  97.481  1.00 24.51 ? 892  LYS   A CA    1 
ATOM   6556  C  C     . LYS   A  1  894  ? -26.331 95.468  96.797  1.00 27.14 ? 892  LYS   A C     1 
ATOM   6557  O  O     . LYS   A  1  894  ? -26.026 95.383  95.603  1.00 29.03 ? 892  LYS   A O     1 
ATOM   6558  C  CB    . LYS   A  1  894  ? -28.574 94.767  97.689  1.00 25.59 ? 892  LYS   A CB    1 
ATOM   6559  C  CG    . LYS   A  1  894  ? -29.280 95.254  96.439  1.00 26.18 ? 892  LYS   A CG    1 
ATOM   6560  C  CD    . LYS   A  1  894  ? -30.732 95.583  96.746  1.00 28.20 ? 892  LYS   A CD    1 
ATOM   6561  C  CE    . LYS   A  1  894  ? -31.471 96.103  95.519  1.00 32.77 ? 892  LYS   A CE    1 
ATOM   6562  N  NZ    . LYS   A  1  894  ? -32.790 96.680  95.892  1.00 43.56 ? 892  LYS   A NZ    1 
ATOM   6563  N  N     . ASP   A  1  895  ? -25.995 96.527  97.541  1.00 26.14 ? 893  ASP   A N     1 
ATOM   6564  C  CA    . ASP   A  1  895  ? -25.242 97.632  96.954  1.00 31.25 ? 893  ASP   A CA    1 
ATOM   6565  C  C     . ASP   A  1  895  ? -23.881 97.171  96.454  1.00 28.37 ? 893  ASP   A C     1 
ATOM   6566  O  O     . ASP   A  1  895  ? -23.423 97.599  95.387  1.00 29.23 ? 893  ASP   A O     1 
ATOM   6567  C  CB    . ASP   A  1  895  ? -25.066 98.757  97.976  1.00 30.63 ? 893  ASP   A CB    1 
ATOM   6568  C  CG    . ASP   A  1  895  ? -26.361 99.465  98.302  1.00 36.92 ? 893  ASP   A CG    1 
ATOM   6569  O  OD1   . ASP   A  1  895  ? -27.335 99.329  97.530  1.00 42.66 ? 893  ASP   A OD1   1 
ATOM   6570  O  OD2   . ASP   A  1  895  ? -26.401 100.173 99.333  1.00 40.98 ? 893  ASP   A OD2   1 
ATOM   6571  N  N     . ASN   A  1  896  ? -23.210 96.315  97.223  1.00 25.52 ? 894  ASN   A N     1 
ATOM   6572  C  CA    . ASN   A  1  896  ? -21.896 95.840  96.821  1.00 25.88 ? 894  ASN   A CA    1 
ATOM   6573  C  C     . ASN   A  1  896  ? -21.980 95.009  95.553  1.00 29.54 ? 894  ASN   A C     1 
ATOM   6574  O  O     . ASN   A  1  896  ? -21.148 95.156  94.653  1.00 26.94 ? 894  ASN   A O     1 
ATOM   6575  C  CB    . ASN   A  1  896  ? -21.285 95.010  97.947  1.00 27.85 ? 894  ASN   A CB    1 
ATOM   6576  C  CG    . ASN   A  1  896  ? -19.938 94.436  97.574  1.00 39.72 ? 894  ASN   A CG    1 
ATOM   6577  O  OD1   . ASN   A  1  896  ? -19.829 93.267  97.186  1.00 43.22 ? 894  ASN   A OD1   1 
ATOM   6578  N  ND2   . ASN   A  1  896  ? -18.900 95.258  97.675  1.00 41.08 ? 894  ASN   A ND2   1 
ATOM   6579  N  N     . ILE   A  1  897  ? -22.973 94.124  95.475  1.00 26.96 ? 895  ILE   A N     1 
ATOM   6580  C  CA    . ILE   A  1  897  ? -23.130 93.294  94.289  1.00 25.19 ? 895  ILE   A CA    1 
ATOM   6581  C  C     . ILE   A  1  897  ? -23.485 94.157  93.090  1.00 28.72 ? 895  ILE   A C     1 
ATOM   6582  O  O     . ILE   A  1  897  ? -22.932 93.989  91.998  1.00 27.77 ? 895  ILE   A O     1 
ATOM   6583  C  CB    . ILE   A  1  897  ? -24.195 92.215  94.540  1.00 21.84 ? 895  ILE   A CB    1 
ATOM   6584  C  CG1   . ILE   A  1  897  ? -23.766 91.285  95.681  1.00 23.82 ? 895  ILE   A CG1   1 
ATOM   6585  C  CG2   . ILE   A  1  897  ? -24.432 91.404  93.273  1.00 23.70 ? 895  ILE   A CG2   1 
ATOM   6586  C  CD1   . ILE   A  1  897  ? -24.952 90.603  96.361  1.00 23.44 ? 895  ILE   A CD1   1 
ATOM   6587  N  N     . GLU   A  1  898  ? -24.412 95.099  93.270  1.00 27.16 ? 896  GLU   A N     1 
ATOM   6588  C  CA    . GLU   A  1  898  ? -24.838 95.917  92.142  1.00 28.25 ? 896  GLU   A CA    1 
ATOM   6589  C  C     . GLU   A  1  898  ? -23.722 96.820  91.638  1.00 30.50 ? 896  GLU   A C     1 
ATOM   6590  O  O     . GLU   A  1  898  ? -23.636 97.077  90.433  1.00 30.88 ? 896  GLU   A O     1 
ATOM   6591  C  CB    . GLU   A  1  898  ? -26.093 96.711  92.500  1.00 28.23 ? 896  GLU   A CB    1 
ATOM   6592  C  CG    . GLU   A  1  898  ? -27.316 95.826  92.669  1.00 32.39 ? 896  GLU   A CG    1 
ATOM   6593  C  CD    . GLU   A  1  898  ? -28.557 96.603  93.050  1.00 39.12 ? 896  GLU   A CD    1 
ATOM   6594  O  OE1   . GLU   A  1  898  ? -28.421 97.715  93.603  1.00 40.78 ? 896  GLU   A OE1   1 
ATOM   6595  O  OE2   . GLU   A  1  898  ? -29.668 96.096  92.797  1.00 47.39 ? 896  GLU   A OE2   1 
ATOM   6596  N  N     . LYS   A  1  899  ? -22.861 97.307  92.535  1.00 29.15 ? 897  LYS   A N     1 
ATOM   6597  C  CA    . LYS   A  1  899  ? -21.726 98.109  92.097  1.00 30.68 ? 897  LYS   A CA    1 
ATOM   6598  C  C     . LYS   A  1  899  ? -20.811 97.293  91.199  1.00 34.37 ? 897  LYS   A C     1 
ATOM   6599  O  O     . LYS   A  1  899  ? -20.264 97.811  90.218  1.00 31.61 ? 897  LYS   A O     1 
ATOM   6600  C  CB    . LYS   A  1  899  ? -20.955 98.636  93.309  1.00 32.20 ? 897  LYS   A CB    1 
ATOM   6601  N  N     . HIS   A  1  900  ? -20.631 96.013  91.523  1.00 28.34 ? 898  HIS   A N     1 
ATOM   6602  C  CA    . HIS   A  1  900  ? -19.841 95.140  90.662  1.00 29.04 ? 898  HIS   A CA    1 
ATOM   6603  C  C     . HIS   A  1  900  ? -20.522 94.940  89.315  1.00 30.07 ? 898  HIS   A C     1 
ATOM   6604  O  O     . HIS   A  1  900  ? -19.876 95.032  88.266  1.00 32.58 ? 898  HIS   A O     1 
ATOM   6605  C  CB    . HIS   A  1  900  ? -19.612 93.796  91.344  1.00 26.56 ? 898  HIS   A CB    1 
ATOM   6606  C  CG    . HIS   A  1  900  ? -19.018 92.766  90.439  1.00 27.99 ? 898  HIS   A CG    1 
ATOM   6607  N  ND1   . HIS   A  1  900  ? -17.683 92.756  90.105  1.00 29.53 ? 898  HIS   A ND1   1 
ATOM   6608  C  CD2   . HIS   A  1  900  ? -19.582 91.731  89.774  1.00 28.34 ? 898  HIS   A CD2   1 
ATOM   6609  C  CE1   . HIS   A  1  900  ? -17.444 91.745  89.289  1.00 28.10 ? 898  HIS   A CE1   1 
ATOM   6610  N  NE2   . HIS   A  1  900  ? -18.580 91.109  89.070  1.00 27.58 ? 898  HIS   A NE2   1 
ATOM   6611  N  N     . ILE   A  1  901  ? -21.824 94.652  89.324  1.00 26.07 ? 899  ILE   A N     1 
ATOM   6612  C  CA    . ILE   A  1  901  ? -22.544 94.458  88.070  1.00 28.54 ? 899  ILE   A CA    1 
ATOM   6613  C  C     . ILE   A  1  901  ? -22.424 95.692  87.189  1.00 32.58 ? 899  ILE   A C     1 
ATOM   6614  O  O     . ILE   A  1  901  ? -22.258 95.588  85.968  1.00 34.14 ? 899  ILE   A O     1 
ATOM   6615  C  CB    . ILE   A  1  901  ? -24.014 94.084  88.335  1.00 25.40 ? 899  ILE   A CB    1 
ATOM   6616  C  CG1   . ILE   A  1  901  ? -24.104 92.735  89.052  1.00 27.84 ? 899  ILE   A CG1   1 
ATOM   6617  C  CG2   . ILE   A  1  901  ? -24.808 94.069  87.028  1.00 27.81 ? 899  ILE   A CG2   1 
ATOM   6618  C  CD1   . ILE   A  1  901  ? -25.500 92.428  89.576  1.00 26.35 ? 899  ILE   A CD1   1 
ATOM   6619  N  N     . GLU   A  1  902  ? -22.491 96.881  87.793  1.00 32.90 ? 900  GLU   A N     1 
ATOM   6620  C  CA    . GLU   A  1  902  ? -22.445 98.111  87.006  1.00 38.34 ? 900  GLU   A CA    1 
ATOM   6621  C  C     . GLU   A  1  902  ? -21.043 98.419  86.494  1.00 36.11 ? 900  GLU   A C     1 
ATOM   6622  O  O     . GLU   A  1  902  ? -20.893 98.932  85.379  1.00 41.41 ? 900  GLU   A O     1 
ATOM   6623  C  CB    . GLU   A  1  902  ? -23.019 99.285  87.800  1.00 42.31 ? 900  GLU   A CB    1 
ATOM   6624  C  CG    . GLU   A  1  902  ? -24.524 99.206  87.955  1.00 47.66 ? 900  GLU   A CG    1 
ATOM   6625  C  CD    . GLU   A  1  902  ? -25.221 98.946  86.633  1.00 46.90 ? 900  GLU   A CD    1 
ATOM   6626  O  OE1   . GLU   A  1  902  ? -25.021 99.741  85.689  1.00 50.93 ? 900  GLU   A OE1   1 
ATOM   6627  O  OE2   . GLU   A  1  902  ? -25.957 97.939  86.532  1.00 47.17 ? 900  GLU   A OE2   1 
ATOM   6628  N  N     . ARG   A  1  903  ? -20.009 98.131  87.287  1.00 34.92 ? 901  ARG   A N     1 
ATOM   6629  C  CA    . ARG   A  1  903  ? -18.644 98.259  86.786  1.00 39.55 ? 901  ARG   A CA    1 
ATOM   6630  C  C     . ARG   A  1  903  ? -18.437 97.380  85.559  1.00 44.89 ? 901  ARG   A C     1 
ATOM   6631  O  O     . ARG   A  1  903  ? -17.894 97.828  84.542  1.00 44.01 ? 901  ARG   A O     1 
ATOM   6632  C  CB    . ARG   A  1  903  ? -17.639 97.902  87.880  1.00 39.40 ? 901  ARG   A CB    1 
ATOM   6633  N  N     . MET   A  1  904  ? -18.883 96.124  85.634  1.00 40.27 ? 902  MET   A N     1 
ATOM   6634  C  CA    . MET   A  1  904  ? -18.795 95.230  84.482  1.00 37.97 ? 902  MET   A CA    1 
ATOM   6635  C  C     . MET   A  1  904  ? -19.604 95.765  83.310  1.00 38.74 ? 902  MET   A C     1 
ATOM   6636  O  O     . MET   A  1  904  ? -19.134 95.773  82.167  1.00 40.22 ? 902  MET   A O     1 
ATOM   6637  C  CB    . MET   A  1  904  ? -19.288 93.837  84.870  1.00 32.05 ? 902  MET   A CB    1 
ATOM   6638  C  CG    . MET   A  1  904  ? -18.470 93.167  85.941  1.00 34.29 ? 902  MET   A CG    1 
ATOM   6639  S  SD    . MET   A  1  904  ? -16.792 92.836  85.380  1.00 46.01 ? 902  MET   A SD    1 
ATOM   6640  C  CE    . MET   A  1  904  ? -15.864 94.107  86.243  1.00 42.14 ? 902  MET   A CE    1 
ATOM   6641  N  N     . ARG   A  1  905  ? -20.837 96.204  83.574  1.00 34.86 ? 903  ARG   A N     1 
ATOM   6642  C  CA    . ARG   A  1  905  ? -21.664 96.755  82.509  1.00 38.09 ? 903  ARG   A CA    1 
ATOM   6643  C  C     . ARG   A  1  905  ? -21.014 97.985  81.898  1.00 42.93 ? 903  ARG   A C     1 
ATOM   6644  O  O     . ARG   A  1  905  ? -21.090 98.196  80.682  1.00 37.45 ? 903  ARG   A O     1 
ATOM   6645  C  CB    . ARG   A  1  905  ? -23.049 97.105  83.047  1.00 37.58 ? 903  ARG   A CB    1 
ATOM   6646  C  CG    . ARG   A  1  905  ? -24.087 97.305  81.965  1.00 39.56 ? 903  ARG   A CG    1 
ATOM   6647  C  CD    . ARG   A  1  905  ? -25.365 97.885  82.529  1.00 45.18 ? 903  ARG   A CD    1 
ATOM   6648  N  NE    . ARG   A  1  905  ? -25.903 97.101  83.634  1.00 39.81 ? 903  ARG   A NE    1 
ATOM   6649  C  CZ    . ARG   A  1  905  ? -26.770 96.106  83.497  1.00 40.60 ? 903  ARG   A CZ    1 
ATOM   6650  N  NH1   . ARG   A  1  905  ? -27.162 95.687  82.304  1.00 37.61 ? 903  ARG   A NH1   1 
ATOM   6651  N  NH2   . ARG   A  1  905  ? -27.259 95.518  84.586  1.00 43.39 ? 903  ARG   A NH2   1 
ATOM   6652  N  N     . GLY   A  1  906  ? -20.368 98.807  82.727  1.00 40.47 ? 904  GLY   A N     1 
ATOM   6653  C  CA    . GLY   A  1  906  ? -19.707 99.992  82.216  1.00 47.59 ? 904  GLY   A CA    1 
ATOM   6654  C  C     . GLY   A  1  906  ? -18.516 99.678  81.335  1.00 51.31 ? 904  GLY   A C     1 
ATOM   6655  O  O     . GLY   A  1  906  ? -18.159 100.476 80.464  1.00 57.80 ? 904  GLY   A O     1 
ATOM   6656  N  N     . LEU   A  1  907  ? -17.888 98.523  81.542  1.00 48.26 ? 905  LEU   A N     1 
ATOM   6657  C  CA    . LEU   A  1  907  ? -16.760 98.104  80.718  1.00 44.98 ? 905  LEU   A CA    1 
ATOM   6658  C  C     . LEU   A  1  907  ? -17.186 97.491  79.391  1.00 46.28 ? 905  LEU   A C     1 
ATOM   6659  O  O     . LEU   A  1  907  ? -16.321 97.027  78.642  1.00 48.64 ? 905  LEU   A O     1 
ATOM   6660  C  CB    . LEU   A  1  907  ? -15.876 97.117  81.483  1.00 43.18 ? 905  LEU   A CB    1 
ATOM   6661  C  CG    . LEU   A  1  907  ? -15.194 97.679  82.731  1.00 45.31 ? 905  LEU   A CG    1 
ATOM   6662  C  CD1   . LEU   A  1  907  ? -14.243 96.664  83.346  1.00 50.54 ? 905  LEU   A CD1   1 
ATOM   6663  C  CD2   . LEU   A  1  907  ? -14.467 98.966  82.389  1.00 50.62 ? 905  LEU   A CD2   1 
ATOM   6664  N  N     . GLY   A  1  908  ? -18.482 97.465  79.085  1.00 42.27 ? 906  GLY   A N     1 
ATOM   6665  C  CA    . GLY   A  1  908  ? -18.964 96.909  77.841  1.00 40.53 ? 906  GLY   A CA    1 
ATOM   6666  C  C     . GLY   A  1  908  ? -19.310 95.435  77.880  1.00 36.22 ? 906  GLY   A C     1 
ATOM   6667  O  O     . GLY   A  1  908  ? -19.712 94.885  76.848  1.00 35.24 ? 906  GLY   A O     1 
ATOM   6668  N  N     . ARG   A  1  909  ? -19.188 94.784  79.031  1.00 35.56 ? 907  ARG   A N     1 
ATOM   6669  C  CA    . ARG   A  1  909  ? -19.462 93.357  79.115  1.00 30.64 ? 907  ARG   A CA    1 
ATOM   6670  C  C     . ARG   A  1  909  ? -20.957 93.087  78.976  1.00 34.33 ? 907  ARG   A C     1 
ATOM   6671  O  O     . ARG   A  1  909  ? -21.794 93.835  79.490  1.00 36.18 ? 907  ARG   A O     1 
ATOM   6672  C  CB    . ARG   A  1  909  ? -18.954 92.813  80.447  1.00 30.95 ? 907  ARG   A CB    1 
ATOM   6673  C  CG    . ARG   A  1  909  ? -17.512 93.189  80.772  1.00 33.13 ? 907  ARG   A CG    1 
ATOM   6674  C  CD    . ARG   A  1  909  ? -16.521 92.519  79.833  1.00 35.44 ? 907  ARG   A CD    1 
ATOM   6675  N  NE    . ARG   A  1  909  ? -15.148 92.626  80.323  1.00 39.36 ? 907  ARG   A NE    1 
ATOM   6676  C  CZ    . ARG   A  1  909  ? -14.269 93.538  79.922  1.00 49.92 ? 907  ARG   A CZ    1 
ATOM   6677  N  NH1   . ARG   A  1  909  ? -14.583 94.453  79.018  1.00 47.04 ? 907  ARG   A NH1   1 
ATOM   6678  N  NH2   . ARG   A  1  909  ? -13.044 93.530  80.441  1.00 42.66 ? 907  ARG   A NH2   1 
ATOM   6679  N  N     . LYS   A  1  910  ? -21.285 92.011  78.266  1.00 26.53 ? 908  LYS   A N     1 
ATOM   6680  C  CA    . LYS   A  1  910  ? -22.673 91.613  78.080  1.00 28.33 ? 908  LYS   A CA    1 
ATOM   6681  C  C     . LYS   A  1  910  ? -23.254 91.106  79.400  1.00 26.87 ? 908  LYS   A C     1 
ATOM   6682  O  O     . LYS   A  1  910  ? -22.684 90.220  80.045  1.00 27.01 ? 908  LYS   A O     1 
ATOM   6683  C  CB    . LYS   A  1  910  ? -22.736 90.525  77.010  1.00 31.90 ? 908  LYS   A CB    1 
ATOM   6684  C  CG    . LYS   A  1  910  ? -24.051 90.424  76.272  1.00 40.45 ? 908  LYS   A CG    1 
ATOM   6685  C  CD    . LYS   A  1  910  ? -23.917 89.481  75.088  1.00 37.09 ? 908  LYS   A CD    1 
ATOM   6686  C  CE    . LYS   A  1  910  ? -25.186 89.464  74.257  1.00 46.29 ? 908  LYS   A CE    1 
ATOM   6687  N  NZ    . LYS   A  1  910  ? -25.112 88.490  73.136  1.00 47.82 ? 908  LYS   A NZ    1 
ATOM   6688  N  N     . VAL   A  1  911  ? -24.392 91.670  79.803  1.00 25.37 ? 909  VAL   A N     1 
ATOM   6689  C  CA    . VAL   A  1  911  ? -25.007 91.396  81.100  1.00 24.45 ? 909  VAL   A CA    1 
ATOM   6690  C  C     . VAL   A  1  911  ? -26.445 90.959  80.859  1.00 25.43 ? 909  VAL   A C     1 
ATOM   6691  O  O     . VAL   A  1  911  ? -27.237 91.713  80.281  1.00 30.55 ? 909  VAL   A O     1 
ATOM   6692  C  CB    . VAL   A  1  911  ? -24.969 92.634  82.014  1.00 26.35 ? 909  VAL   A CB    1 
ATOM   6693  C  CG1   . VAL   A  1  911  ? -25.729 92.370  83.310  1.00 31.24 ? 909  VAL   A CG1   1 
ATOM   6694  C  CG2   . VAL   A  1  911  ? -23.528 93.055  82.300  1.00 27.35 ? 909  VAL   A CG2   1 
ATOM   6695  N  N     . GLU   A  1  912  ? -26.769 89.740  81.272  1.00 26.04 ? 910  GLU   A N     1 
ATOM   6696  C  CA    . GLU   A  1  912  ? -28.116 89.194  81.196  1.00 26.57 ? 910  GLU   A CA    1 
ATOM   6697  C  C     . GLU   A  1  912  ? -28.692 89.172  82.603  1.00 26.37 ? 910  GLU   A C     1 
ATOM   6698  O  O     . GLU   A  1  912  ? -28.054 88.656  83.527  1.00 24.82 ? 910  GLU   A O     1 
ATOM   6699  C  CB    . GLU   A  1  912  ? -28.078 87.764  80.650  1.00 26.60 ? 910  GLU   A CB    1 
ATOM   6700  C  CG    . GLU   A  1  912  ? -29.450 87.157  80.365  1.00 25.82 ? 910  GLU   A CG    1 
ATOM   6701  C  CD    . GLU   A  1  912  ? -30.058 87.693  79.083  1.00 31.32 ? 910  GLU   A CD    1 
ATOM   6702  O  OE1   . GLU   A  1  912  ? -29.304 88.271  78.277  1.00 31.39 ? 910  GLU   A OE1   1 
ATOM   6703  O  OE2   . GLU   A  1  912  ? -31.285 87.543  78.882  1.00 30.73 ? 910  GLU   A OE2   1 
ATOM   6704  N  N     . GLN   A  1  913  ? -29.889 89.736  82.772  1.00 25.89 ? 911  GLN   A N     1 
ATOM   6705  C  CA    . GLN   A  1  913  ? -30.506 89.801  84.087  1.00 26.14 ? 911  GLN   A CA    1 
ATOM   6706  C  C     . GLN   A  1  913  ? -31.982 89.450  84.002  1.00 32.85 ? 911  GLN   A C     1 
ATOM   6707  O  O     . GLN   A  1  913  ? -32.672 89.849  83.062  1.00 32.60 ? 911  GLN   A O     1 
ATOM   6708  C  CB    . GLN   A  1  913  ? -30.352 91.196  84.714  1.00 29.58 ? 911  GLN   A CB    1 
ATOM   6709  C  CG    . GLN   A  1  913  ? -28.937 91.550  85.125  1.00 29.43 ? 911  GLN   A CG    1 
ATOM   6710  C  CD    . GLN   A  1  913  ? -28.882 92.772  86.031  1.00 29.54 ? 911  GLN   A CD    1 
ATOM   6711  O  OE1   . GLN   A  1  913  ? -29.343 93.855  85.662  1.00 32.97 ? 911  GLN   A OE1   1 
ATOM   6712  N  NE2   . GLN   A  1  913  ? -28.333 92.600  87.224  1.00 26.65 ? 911  GLN   A NE2   1 
ATOM   6713  N  N     . ILE   A  1  914  ? -32.448 88.690  84.992  1.00 32.41 ? 912  ILE   A N     1 
ATOM   6714  C  CA    . ILE   A  1  914  ? -33.872 88.438  85.176  1.00 28.88 ? 912  ILE   A CA    1 
ATOM   6715  C  C     . ILE   A  1  914  ? -34.568 89.731  85.575  1.00 31.21 ? 912  ILE   A C     1 
ATOM   6716  O  O     . ILE   A  1  914  ? -34.009 90.561  86.305  1.00 30.19 ? 912  ILE   A O     1 
ATOM   6717  C  CB    . ILE   A  1  914  ? -34.015 87.388  86.290  1.00 35.80 ? 912  ILE   A CB    1 
ATOM   6718  C  CG1   . ILE   A  1  914  ? -33.603 86.015  85.781  1.00 35.26 ? 912  ILE   A CG1   1 
ATOM   6719  C  CG2   . ILE   A  1  914  ? -35.413 87.388  86.891  1.00 47.08 ? 912  ILE   A CG2   1 
ATOM   6720  C  CD1   . ILE   A  1  914  ? -33.538 85.021  86.875  1.00 32.04 ? 912  ILE   A CD1   1 
ATOM   6721  N  N     . GLY   A  1  915  ? -35.798 89.914  85.099  1.00 37.11 ? 913  GLY   A N     1 
ATOM   6722  C  CA    . GLY   A  1  915  ? -36.613 91.021  85.569  1.00 35.76 ? 913  GLY   A CA    1 
ATOM   6723  C  C     . GLY   A  1  915  ? -37.242 90.667  86.904  1.00 39.01 ? 913  GLY   A C     1 
ATOM   6724  O  O     . GLY   A  1  915  ? -37.796 89.575  87.073  1.00 44.56 ? 913  GLY   A O     1 
ATOM   6725  N  N     . LEU   A  1  916  ? -37.150 91.586  87.860  1.00 34.42 ? 914  LEU   A N     1 
ATOM   6726  C  CA    . LEU   A  1  916  ? -37.654 91.351  89.205  1.00 39.82 ? 914  LEU   A CA    1 
ATOM   6727  C  C     . LEU   A  1  916  ? -39.084 91.856  89.336  1.00 40.50 ? 914  LEU   A C     1 
ATOM   6728  O  O     . LEU   A  1  916  ? -39.426 92.930  88.832  1.00 41.14 ? 914  LEU   A O     1 
ATOM   6729  C  CB    . LEU   A  1  916  ? -36.778 92.072  90.227  1.00 38.40 ? 914  LEU   A CB    1 
ATOM   6730  C  CG    . LEU   A  1  916  ? -35.338 91.582  90.332  1.00 39.25 ? 914  LEU   A CG    1 
ATOM   6731  C  CD1   . LEU   A  1  916  ? -34.628 92.341  91.432  1.00 37.19 ? 914  LEU   A CD1   1 
ATOM   6732  C  CD2   . LEU   A  1  916  ? -35.315 90.087  90.599  1.00 41.03 ? 914  LEU   A CD2   1 
ATOM   6733  N  N     . ALA   A  1  917  ? -39.910 91.082  90.032  1.00 33.82 ? 915  ALA   A N     1 
ATOM   6734  C  CA    . ALA   A  1  917  ? -41.285 91.485  90.269  1.00 36.28 ? 915  ALA   A CA    1 
ATOM   6735  C  C     . ALA   A  1  917  ? -41.329 92.690  91.205  1.00 36.08 ? 915  ALA   A C     1 
ATOM   6736  O  O     . ALA   A  1  917  ? -40.401 92.948  91.980  1.00 36.09 ? 915  ALA   A O     1 
ATOM   6737  C  CB    . ALA   A  1  917  ? -42.081 90.328  90.872  1.00 38.67 ? 915  ALA   A CB    1 
ATOM   6738  N  N     . SER   A  1  918  ? -42.432 93.439  91.121  1.00 36.19 ? 916  SER   A N     1 
ATOM   6739  C  CA    . SER   A  1  918  ? -42.602 94.607  91.982  1.00 39.65 ? 916  SER   A CA    1 
ATOM   6740  C  C     . SER   A  1  918  ? -42.577 94.228  93.458  1.00 34.41 ? 916  SER   A C     1 
ATOM   6741  O  O     . SER   A  1  918  ? -42.148 95.031  94.295  1.00 32.08 ? 916  SER   A O     1 
ATOM   6742  C  CB    . SER   A  1  918  ? -43.912 95.315  91.641  1.00 37.18 ? 916  SER   A CB    1 
ATOM   6743  O  OG    . SER   A  1  918  ? -44.994 94.400  91.710  1.00 44.87 ? 916  SER   A OG    1 
ATOM   6744  N  N     . GLU   A  1  919  ? -43.019 93.009  93.792  1.00 36.32 ? 917  GLU   A N     1 
ATOM   6745  C  CA    . GLU   A  1  919  ? -43.074 92.561  95.181  1.00 35.37 ? 917  GLU   A CA    1 
ATOM   6746  C  C     . GLU   A  1  919  ? -41.702 92.524  95.842  1.00 37.25 ? 917  GLU   A C     1 
ATOM   6747  O  O     . GLU   A  1  919  ? -41.622 92.517  97.075  1.00 33.46 ? 917  GLU   A O     1 
ATOM   6748  C  CB    . GLU   A  1  919  ? -43.706 91.168  95.268  1.00 37.58 ? 917  GLU   A CB    1 
ATOM   6749  C  CG    . GLU   A  1  919  ? -45.224 91.132  95.118  1.00 42.84 ? 917  GLU   A CG    1 
ATOM   6750  C  CD    . GLU   A  1  919  ? -45.685 91.260  93.677  1.00 50.95 ? 917  GLU   A CD    1 
ATOM   6751  O  OE1   . GLU   A  1  919  ? -44.829 91.257  92.766  1.00 48.94 ? 917  GLU   A OE1   1 
ATOM   6752  O  OE2   . GLU   A  1  919  ? -46.910 91.360  93.456  1.00 57.08 ? 917  GLU   A OE2   1 
ATOM   6753  N  N     . THR   A  1  920  ? -40.625 92.491  95.058  1.00 34.89 ? 918  THR   A N     1 
ATOM   6754  C  CA    . THR   A  1  920  ? -39.293 92.428  95.645  1.00 31.77 ? 918  THR   A CA    1 
ATOM   6755  C  C     . THR   A  1  920  ? -38.876 93.743  96.294  1.00 29.59 ? 918  THR   A C     1 
ATOM   6756  O  O     . THR   A  1  920  ? -37.958 93.744  97.121  1.00 29.06 ? 918  THR   A O     1 
ATOM   6757  C  CB    . THR   A  1  920  ? -38.273 91.993  94.588  1.00 26.93 ? 918  THR   A CB    1 
ATOM   6758  O  OG1   . THR   A  1  920  ? -38.273 92.928  93.505  1.00 30.66 ? 918  THR   A OG1   1 
ATOM   6759  C  CG2   . THR   A  1  920  ? -38.600 90.601  94.062  1.00 28.00 ? 918  THR   A CG2   1 
ATOM   6760  N  N     . GLY   A  1  921  ? -39.541 94.854  95.962  1.00 30.87 ? 919  GLY   A N     1 
ATOM   6761  C  CA    . GLY   A  1  921  ? -39.138 96.152  96.476  1.00 32.06 ? 919  GLY   A CA    1 
ATOM   6762  C  C     . GLY   A  1  921  ? -39.148 96.267  97.988  1.00 28.78 ? 919  GLY   A C     1 
ATOM   6763  O  O     . GLY   A  1  921  ? -38.426 97.102  98.541  1.00 32.99 ? 919  GLY   A O     1 
ATOM   6764  N  N     . VAL   A  1  922  ? -39.948 95.448  98.674  1.00 30.59 ? 920  VAL   A N     1 
ATOM   6765  C  CA    . VAL   A  1  922  ? -39.967 95.484  100.135 1.00 28.69 ? 920  VAL   A CA    1 
ATOM   6766  C  C     . VAL   A  1  922  ? -38.785 94.757  100.755 1.00 29.45 ? 920  VAL   A C     1 
ATOM   6767  O  O     . VAL   A  1  922  ? -38.577 94.863  101.970 1.00 29.28 ? 920  VAL   A O     1 
ATOM   6768  C  CB    . VAL   A  1  922  ? -41.290 94.932  100.694 1.00 26.99 ? 920  VAL   A CB    1 
ATOM   6769  C  CG1   . VAL   A  1  922  ? -42.443 95.871  100.350 1.00 29.98 ? 920  VAL   A CG1   1 
ATOM   6770  C  CG2   . VAL   A  1  922  ? -41.556 93.552  100.139 1.00 27.70 ? 920  VAL   A CG2   1 
ATOM   6771  N  N     . GLY   A  1  923  ? -38.012 94.019  99.957  1.00 27.50 ? 921  GLY   A N     1 
ATOM   6772  C  CA    . GLY   A  1  923  ? -36.819 93.352  100.440 1.00 25.67 ? 921  GLY   A CA    1 
ATOM   6773  C  C     . GLY   A  1  923  ? -35.585 93.794  99.684  1.00 25.11 ? 921  GLY   A C     1 
ATOM   6774  O  O     . GLY   A  1  923  ? -35.614 94.804  98.975  1.00 27.57 ? 921  GLY   A O     1 
ATOM   6775  N  N     . THR   A  1  924  ? -34.488 93.060  99.829  1.00 23.55 ? 922  THR   A N     1 
ATOM   6776  C  CA    . THR   A  1  924  ? -33.241 93.399  99.150  1.00 23.11 ? 922  THR   A CA    1 
ATOM   6777  C  C     . THR   A  1  924  ? -32.897 92.260  98.201  1.00 23.07 ? 922  THR   A C     1 
ATOM   6778  O  O     . THR   A  1  924  ? -32.361 91.229  98.618  1.00 24.31 ? 922  THR   A O     1 
ATOM   6779  C  CB    . THR   A  1  924  ? -32.119 93.664  100.145 1.00 21.88 ? 922  THR   A CB    1 
ATOM   6780  O  OG1   . THR   A  1  924  ? -32.046 92.594  101.095 1.00 23.70 ? 922  THR   A OG1   1 
ATOM   6781  C  CG2   . THR   A  1  924  ? -32.391 94.964  100.883 1.00 26.76 ? 922  THR   A CG2   1 
ATOM   6782  N  N     . PHE   A  1  925  ? -33.203 92.451  96.926  1.00 22.83 ? 923  PHE   A N     1 
ATOM   6783  C  CA    . PHE   A  1  925  ? -33.023 91.416  95.925  1.00 20.10 ? 923  PHE   A CA    1 
ATOM   6784  C  C     . PHE   A  1  925  ? -32.076 91.900  94.840  1.00 21.94 ? 923  PHE   A C     1 
ATOM   6785  O  O     . PHE   A  1  925  ? -32.089 93.077  94.459  1.00 24.55 ? 923  PHE   A O     1 
ATOM   6786  C  CB    . PHE   A  1  925  ? -34.357 91.068  95.265  1.00 20.17 ? 923  PHE   A CB    1 
ATOM   6787  C  CG    . PHE   A  1  925  ? -35.311 90.344  96.158  1.00 22.65 ? 923  PHE   A CG    1 
ATOM   6788  C  CD1   . PHE   A  1  925  ? -36.146 91.043  97.013  1.00 21.92 ? 923  PHE   A CD1   1 
ATOM   6789  C  CD2   . PHE   A  1  925  ? -35.383 88.963  96.133  1.00 20.83 ? 923  PHE   A CD2   1 
ATOM   6790  C  CE1   . PHE   A  1  925  ? -37.047 90.374  97.822  1.00 23.13 ? 923  PHE   A CE1   1 
ATOM   6791  C  CE2   . PHE   A  1  925  ? -36.271 88.284  96.944  1.00 21.72 ? 923  PHE   A CE2   1 
ATOM   6792  C  CZ    . PHE   A  1  925  ? -37.107 88.993  97.786  1.00 20.44 ? 923  PHE   A CZ    1 
ATOM   6793  N  N     . VAL   A  1  926  ? -31.261 90.974  94.350  1.00 22.52 ? 924  VAL   A N     1 
ATOM   6794  C  CA    . VAL   A  1  926  ? -30.443 91.165  93.162  1.00 22.00 ? 924  VAL   A CA    1 
ATOM   6795  C  C     . VAL   A  1  926  ? -30.869 90.089  92.175  1.00 21.95 ? 924  VAL   A C     1 
ATOM   6796  O  O     . VAL   A  1  926  ? -30.894 88.912  92.537  1.00 23.01 ? 924  VAL   A O     1 
ATOM   6797  C  CB    . VAL   A  1  926  ? -28.939 91.041  93.464  1.00 21.75 ? 924  VAL   A CB    1 
ATOM   6798  C  CG1   . VAL   A  1  926  ? -28.136 91.134  92.179  1.00 23.03 ? 924  VAL   A CG1   1 
ATOM   6799  C  CG2   . VAL   A  1  926  ? -28.519 92.132  94.446  1.00 24.91 ? 924  VAL   A CG2   1 
ATOM   6800  N  N     . PRO   A  1  927  ? -31.223 90.430  90.942  1.00 21.71 ? 925  PRO   A N     1 
ATOM   6801  C  CA    . PRO   A  1  927  ? -31.622 89.400  89.998  1.00 23.68 ? 925  PRO   A CA    1 
ATOM   6802  C  C     . PRO   A  1  927  ? -30.434 88.542  89.623  1.00 22.25 ? 925  PRO   A C     1 
ATOM   6803  O  O     . PRO   A  1  927  ? -29.301 89.042  89.515  1.00 23.47 ? 925  PRO   A O     1 
ATOM   6804  C  CB    . PRO   A  1  927  ? -32.118 90.198  88.787  1.00 27.54 ? 925  PRO   A CB    1 
ATOM   6805  C  CG    . PRO   A  1  927  ? -31.386 91.485  88.863  1.00 29.53 ? 925  PRO   A CG    1 
ATOM   6806  C  CD    . PRO   A  1  927  ? -31.213 91.774  90.332  1.00 25.30 ? 925  PRO   A CD    1 
ATOM   6807  N  N     . PRO   A  1  928  ? -30.649 87.242  89.469  1.00 23.60 ? 926  PRO   A N     1 
ATOM   6808  C  CA    . PRO   A  1  928  ? -29.621 86.392  88.873  1.00 23.81 ? 926  PRO   A CA    1 
ATOM   6809  C  C     . PRO   A  1  928  ? -29.096 87.043  87.608  1.00 20.10 ? 926  PRO   A C     1 
ATOM   6810  O  O     . PRO   A  1  928  ? -29.862 87.546  86.775  1.00 22.71 ? 926  PRO   A O     1 
ATOM   6811  C  CB    . PRO   A  1  928  ? -30.381 85.095  88.585  1.00 21.91 ? 926  PRO   A CB    1 
ATOM   6812  C  CG    . PRO   A  1  928  ? -31.378 85.041  89.697  1.00 24.89 ? 926  PRO   A CG    1 
ATOM   6813  C  CD    . PRO   A  1  928  ? -31.837 86.467  89.866  1.00 25.21 ? 926  PRO   A CD    1 
ATOM   6814  N  N     . THR   A  1  929  ? -27.778 87.069  87.492  1.00 22.19 ? 927  THR   A N     1 
ATOM   6815  C  CA    . THR   A  1  929  ? -27.075 87.857  86.503  1.00 21.60 ? 927  THR   A CA    1 
ATOM   6816  C  C     . THR   A  1  929  ? -26.012 86.982  85.873  1.00 21.52 ? 927  THR   A C     1 
ATOM   6817  O  O     . THR   A  1  929  ? -25.318 86.238  86.569  1.00 21.64 ? 927  THR   A O     1 
ATOM   6818  C  CB    . THR   A  1  929  ? -26.422 89.067  87.182  1.00 25.08 ? 927  THR   A CB    1 
ATOM   6819  O  OG1   . THR   A  1  929  ? -27.440 89.853  87.813  1.00 24.78 ? 927  THR   A OG1   1 
ATOM   6820  C  CG2   . THR   A  1  929  ? -25.667 89.941  86.172  1.00 26.88 ? 927  THR   A CG2   1 
ATOM   6821  N  N     . ILE   A  1  930  ? -25.898 87.066  84.553  1.00 21.21 ? 928  ILE   A N     1 
ATOM   6822  C  CA    . ILE   A  1  930  ? -24.818 86.425  83.819  1.00 23.52 ? 928  ILE   A CA    1 
ATOM   6823  C  C     . ILE   A  1  930  ? -24.011 87.527  83.164  1.00 22.81 ? 928  ILE   A C     1 
ATOM   6824  O  O     . ILE   A  1  930  ? -24.575 88.374  82.459  1.00 25.46 ? 928  ILE   A O     1 
ATOM   6825  C  CB    . ILE   A  1  930  ? -25.354 85.456  82.755  1.00 20.77 ? 928  ILE   A CB    1 
ATOM   6826  C  CG1   . ILE   A  1  930  ? -26.090 84.290  83.406  1.00 24.54 ? 928  ILE   A CG1   1 
ATOM   6827  C  CG2   . ILE   A  1  930  ? -24.194 84.963  81.879  1.00 25.93 ? 928  ILE   A CG2   1 
ATOM   6828  C  CD1   . ILE   A  1  930  ? -26.959 83.505  82.428  1.00 25.81 ? 928  ILE   A CD1   1 
ATOM   6829  N  N     . ILE   A  1  931  ? -22.702 87.516  83.387  1.00 22.07 ? 929  ILE   A N     1 
ATOM   6830  C  CA    . ILE   A  1  931  ? -21.784 88.519  82.866  1.00 24.25 ? 929  ILE   A CA    1 
ATOM   6831  C  C     . ILE   A  1  931  ? -20.741 87.794  82.035  1.00 27.87 ? 929  ILE   A C     1 
ATOM   6832  O  O     . ILE   A  1  931  ? -20.036 86.918  82.542  1.00 25.67 ? 929  ILE   A O     1 
ATOM   6833  C  CB    . ILE   A  1  931  ? -21.106 89.307  83.996  1.00 28.40 ? 929  ILE   A CB    1 
ATOM   6834  C  CG1   . ILE   A  1  931  ? -22.152 90.043  84.843  1.00 28.27 ? 929  ILE   A CG1   1 
ATOM   6835  C  CG2   . ILE   A  1  931  ? -20.089 90.282  83.428  1.00 27.56 ? 929  ILE   A CG2   1 
ATOM   6836  C  CD1   . ILE   A  1  931  ? -21.546 90.922  85.920  1.00 28.32 ? 929  ILE   A CD1   1 
ATOM   6837  N  N     . GLU   A  1  932  ? -20.631 88.158  80.767  1.00 25.56 ? 930  GLU   A N     1 
ATOM   6838  C  CA    . GLU   A  1  932  ? -19.664 87.522  79.887  1.00 26.06 ? 930  GLU   A CA    1 
ATOM   6839  C  C     . GLU   A  1  932  ? -18.362 88.305  79.951  1.00 21.84 ? 930  GLU   A C     1 
ATOM   6840  O  O     . GLU   A  1  932  ? -18.330 89.493  79.616  1.00 27.37 ? 930  GLU   A O     1 
ATOM   6841  C  CB    . GLU   A  1  932  ? -20.221 87.460  78.471  1.00 23.90 ? 930  GLU   A CB    1 
ATOM   6842  C  CG    . GLU   A  1  932  ? -21.419 86.529  78.389  1.00 25.00 ? 930  GLU   A CG    1 
ATOM   6843  C  CD    . GLU   A  1  932  ? -22.152 86.656  77.083  1.00 31.65 ? 930  GLU   A CD    1 
ATOM   6844  O  OE1   . GLU   A  1  932  ? -21.485 86.596  76.028  1.00 29.68 ? 930  GLU   A OE1   1 
ATOM   6845  O  OE2   . GLU   A  1  932  ? -23.391 86.822  77.114  1.00 30.18 ? 930  GLU   A OE2   1 
ATOM   6846  N  N     . LEU   A  1  933  ? -17.303 87.649  80.406  1.00 26.44 ? 931  LEU   A N     1 
ATOM   6847  C  CA    . LEU   A  1  933  ? -16.001 88.276  80.567  1.00 27.01 ? 931  LEU   A CA    1 
ATOM   6848  C  C     . LEU   A  1  933  ? -15.071 87.911  79.418  1.00 33.92 ? 931  LEU   A C     1 
ATOM   6849  O  O     . LEU   A  1  933  ? -15.265 86.910  78.724  1.00 30.25 ? 931  LEU   A O     1 
ATOM   6850  C  CB    . LEU   A  1  933  ? -15.344 87.837  81.876  1.00 30.17 ? 931  LEU   A CB    1 
ATOM   6851  C  CG    . LEU   A  1  933  ? -16.043 88.228  83.177  1.00 30.52 ? 931  LEU   A CG    1 
ATOM   6852  C  CD1   . LEU   A  1  933  ? -15.160 87.847  84.343  1.00 36.22 ? 931  LEU   A CD1   1 
ATOM   6853  C  CD2   . LEU   A  1  933  ? -16.341 89.715  83.187  1.00 36.10 ? 931  LEU   A CD2   1 
ATOM   6854  N  N     . GLU   A  1  934  ? -14.035 88.738  79.244  1.00 33.16 ? 932  GLU   A N     1 
ATOM   6855  C  CA    . GLU   A  1  934  ? -12.950 88.493  78.301  1.00 42.10 ? 932  GLU   A CA    1 
ATOM   6856  C  C     . GLU   A  1  934  ? -11.867 87.591  78.892  1.00 40.88 ? 932  GLU   A C     1 
ATOM   6857  O  O     . GLU   A  1  934  ? -11.484 86.593  78.273  1.00 47.67 ? 932  GLU   A O     1 
ATOM   6858  C  CB    . GLU   A  1  934  ? -12.344 89.823  77.838  1.00 44.39 ? 932  GLU   A CB    1 
ATOM   6859  N  N     . LYS   A  1  935  ? -11.370 87.926  80.083  1.00 42.40 ? 933  LYS   A N     1 
ATOM   6860  C  CA    . LYS   A  1  935  ? -10.342 87.147  80.760  1.00 42.78 ? 933  LYS   A CA    1 
ATOM   6861  C  C     . LYS   A  1  935  ? -10.739 86.945  82.215  1.00 47.64 ? 933  LYS   A C     1 
ATOM   6862  O  O     . LYS   A  1  935  ? -11.512 87.721  82.781  1.00 43.45 ? 933  LYS   A O     1 
ATOM   6863  C  CB    . LYS   A  1  935  ? -8.975  87.843  80.711  1.00 45.67 ? 933  LYS   A CB    1 
ATOM   6864  N  N     . LEU   A  1  936  ? -10.192 85.887  82.823  1.00 45.11 ? 934  LEU   A N     1 
ATOM   6865  C  CA    . LEU   A  1  936  ? -10.470 85.628  84.234  1.00 46.56 ? 934  LEU   A CA    1 
ATOM   6866  C  C     . LEU   A  1  936  ? -9.882  86.717  85.119  1.00 48.69 ? 934  LEU   A C     1 
ATOM   6867  O  O     . LEU   A  1  936  ? -10.378 86.959  86.226  1.00 47.93 ? 934  LEU   A O     1 
ATOM   6868  C  CB    . LEU   A  1  936  ? -9.944  84.253  84.641  1.00 42.13 ? 934  LEU   A CB    1 
ATOM   6869  C  CG    . LEU   A  1  936  ? -10.903 83.384  85.465  1.00 46.72 ? 934  LEU   A CG    1 
ATOM   6870  C  CD1   . LEU   A  1  936  ? -10.452 81.933  85.459  1.00 39.12 ? 934  LEU   A CD1   1 
ATOM   6871  C  CD2   . LEU   A  1  936  ? -11.022 83.895  86.892  1.00 43.76 ? 934  LEU   A CD2   1 
ATOM   6872  N  N     . SER   A  1  937  ? -8.837  87.394  84.644  1.00 50.98 ? 935  SER   A N     1 
ATOM   6873  C  CA    . SER   A  1  937  ? -8.264  88.516  85.375  1.00 51.09 ? 935  SER   A CA    1 
ATOM   6874  C  C     . SER   A  1  937  ? -9.210  89.708  85.470  1.00 47.95 ? 935  SER   A C     1 
ATOM   6875  O  O     . SER   A  1  937  ? -8.915  90.649  86.216  1.00 52.93 ? 935  SER   A O     1 
ATOM   6876  C  CB    . SER   A  1  937  ? -6.939  88.928  84.731  1.00 52.10 ? 935  SER   A CB    1 
ATOM   6877  O  OG    . SER   A  1  937  ? -7.043  88.915  83.317  1.00 56.61 ? 935  SER   A OG    1 
ATOM   6878  N  N     . ASP   A  1  938  ? -10.332 89.696  84.742  1.00 50.14 ? 936  ASP   A N     1 
ATOM   6879  C  CA    . ASP   A  1  938  ? -11.324 90.757  84.887  1.00 48.37 ? 936  ASP   A CA    1 
ATOM   6880  C  C     . ASP   A  1  938  ? -11.976 90.753  86.264  1.00 52.37 ? 936  ASP   A C     1 
ATOM   6881  O  O     . ASP   A  1  938  ? -12.637 91.731  86.629  1.00 50.33 ? 936  ASP   A O     1 
ATOM   6882  C  CB    . ASP   A  1  938  ? -12.416 90.623  83.824  1.00 53.53 ? 936  ASP   A CB    1 
ATOM   6883  C  CG    . ASP   A  1  938  ? -11.887 90.799  82.417  1.00 55.05 ? 936  ASP   A CG    1 
ATOM   6884  O  OD1   . ASP   A  1  938  ? -10.678 91.078  82.260  1.00 59.48 ? 936  ASP   A OD1   1 
ATOM   6885  O  OD2   . ASP   A  1  938  ? -12.686 90.654  81.465  1.00 52.31 ? 936  ASP   A OD2   1 
ATOM   6886  N  N     . LEU   A  1  939  ? -11.823 89.675  87.024  1.00 46.49 ? 937  LEU   A N     1 
ATOM   6887  C  CA    . LEU   A  1  939  ? -12.370 89.584  88.367  1.00 43.57 ? 937  LEU   A CA    1 
ATOM   6888  C  C     . LEU   A  1  939  ? -11.293 89.910  89.389  1.00 49.22 ? 937  LEU   A C     1 
ATOM   6889  O  O     . LEU   A  1  939  ? -10.145 89.476  89.260  1.00 49.94 ? 937  LEU   A O     1 
ATOM   6890  C  CB    . LEU   A  1  939  ? -12.905 88.182  88.638  1.00 39.56 ? 937  LEU   A CB    1 
ATOM   6891  C  CG    . LEU   A  1  939  ? -14.151 87.765  87.867  1.00 38.69 ? 937  LEU   A CG    1 
ATOM   6892  C  CD1   . LEU   A  1  939  ? -14.745 86.534  88.516  1.00 38.70 ? 937  LEU   A CD1   1 
ATOM   6893  C  CD2   . LEU   A  1  939  ? -15.165 88.899  87.826  1.00 41.63 ? 937  LEU   A CD2   1 
ATOM   6894  N  N     . GLN   A  1  940  ? -11.674 90.674  90.409  1.00 41.76 ? 938  GLN   A N     1 
ATOM   6895  C  CA    . GLN   A  1  940  ? -10.744 91.031  91.470  1.00 44.60 ? 938  GLN   A CA    1 
ATOM   6896  C  C     . GLN   A  1  940  ? -10.980 90.164  92.701  1.00 47.20 ? 938  GLN   A C     1 
ATOM   6897  O  O     . GLN   A  1  940  ? -10.181 89.269  92.994  1.00 54.21 ? 938  GLN   A O     1 
ATOM   6898  C  CB    . GLN   A  1  940  ? -10.856 92.518  91.810  1.00 43.62 ? 938  GLN   A CB    1 
ATOM   6899  N  N     . ARG   A  1  941  ? -12.071 90.409  93.422  1.00 45.38 ? 939  ARG   A N     1 
ATOM   6900  C  CA    . ARG   A  1  941  ? -12.382 89.679  94.643  1.00 37.50 ? 939  ARG   A CA    1 
ATOM   6901  C  C     . ARG   A  1  941  ? -13.698 88.927  94.482  1.00 30.22 ? 939  ARG   A C     1 
ATOM   6902  O  O     . ARG   A  1  941  ? -14.444 89.124  93.520  1.00 34.81 ? 939  ARG   A O     1 
ATOM   6903  C  CB    . ARG   A  1  941  ? -12.450 90.624  95.852  1.00 42.06 ? 939  ARG   A CB    1 
ATOM   6904  N  N     . GLU   A  1  942  ? -13.957 88.034  95.436  1.00 28.80 ? 940  GLU   A N     1 
ATOM   6905  C  CA    . GLU   A  1  942  ? -15.218 87.301  95.484  1.00 25.23 ? 940  GLU   A CA    1 
ATOM   6906  C  C     . GLU   A  1  942  ? -16.385 88.279  95.522  1.00 23.62 ? 940  GLU   A C     1 
ATOM   6907  O  O     . GLU   A  1  942  ? -16.366 89.249  96.284  1.00 26.01 ? 940  GLU   A O     1 
ATOM   6908  C  CB    . GLU   A  1  942  ? -15.225 86.454  96.754  1.00 27.74 ? 940  GLU   A CB    1 
ATOM   6909  C  CG    . GLU   A  1  942  ? -16.507 85.692  97.031  1.00 25.53 ? 940  GLU   A CG    1 
ATOM   6910  C  CD    . GLU   A  1  942  ? -16.514 85.121  98.433  1.00 25.34 ? 940  GLU   A CD    1 
ATOM   6911  O  OE1   . GLU   A  1  942  ? -16.272 85.898  99.381  1.00 27.83 ? 940  GLU   A OE1   1 
ATOM   6912  O  OE2   . GLU   A  1  942  ? -16.736 83.908  98.596  1.00 21.79 ? 940  GLU   A OE2   1 
ATOM   6913  N  N     . VAL   A  1  943  ? -17.391 88.034  94.685  1.00 24.36 ? 941  VAL   A N     1 
ATOM   6914  C  CA    . VAL   A  1  943  ? -18.629 88.809  94.667  1.00 23.31 ? 941  VAL   A CA    1 
ATOM   6915  C  C     . VAL   A  1  943  ? -19.726 87.875  95.153  1.00 25.57 ? 941  VAL   A C     1 
ATOM   6916  O  O     . VAL   A  1  943  ? -20.127 86.945  94.444  1.00 22.88 ? 941  VAL   A O     1 
ATOM   6917  C  CB    . VAL   A  1  943  ? -18.940 89.364  93.272  1.00 26.78 ? 941  VAL   A CB    1 
ATOM   6918  C  CG1   . VAL   A  1  943  ? -20.248 90.153  93.274  1.00 29.24 ? 941  VAL   A CG1   1 
ATOM   6919  C  CG2   . VAL   A  1  943  ? -17.787 90.233  92.794  1.00 29.18 ? 941  VAL   A CG2   1 
ATOM   6920  N  N     . PHE   A  1  944  ? -20.192 88.103  96.377  1.00 23.31 ? 942  PHE   A N     1 
ATOM   6921  C  CA    . PHE   A  1  944  ? -20.993 87.114  97.088  1.00 21.52 ? 942  PHE   A CA    1 
ATOM   6922  C  C     . PHE   A  1  944  ? -22.459 87.393  96.789  1.00 21.42 ? 942  PHE   A C     1 
ATOM   6923  O  O     . PHE   A  1  944  ? -23.205 87.946  97.598  1.00 23.46 ? 942  PHE   A O     1 
ATOM   6924  C  CB    . PHE   A  1  944  ? -20.677 87.177  98.578  1.00 21.32 ? 942  PHE   A CB    1 
ATOM   6925  C  CG    . PHE   A  1  944  ? -21.046 85.938  99.333  1.00 19.50 ? 942  PHE   A CG    1 
ATOM   6926  C  CD1   . PHE   A  1  944  ? -20.342 84.768  99.151  1.00 18.84 ? 942  PHE   A CD1   1 
ATOM   6927  C  CD2   . PHE   A  1  944  ? -22.069 85.962  100.268 1.00 19.96 ? 942  PHE   A CD2   1 
ATOM   6928  C  CE1   . PHE   A  1  944  ? -20.684 83.624  99.869  1.00 17.88 ? 942  PHE   A CE1   1 
ATOM   6929  C  CE2   . PHE   A  1  944  ? -22.401 84.818  100.988 1.00 19.94 ? 942  PHE   A CE2   1 
ATOM   6930  C  CZ    . PHE   A  1  944  ? -21.719 83.653  100.775 1.00 19.16 ? 942  PHE   A CZ    1 
ATOM   6931  N  N     . GLY   A  1  945  ? -22.873 87.013  95.585  1.00 20.97 ? 943  GLY   A N     1 
ATOM   6932  C  CA    . GLY   A  1  945  ? -24.220 87.266  95.143  1.00 22.39 ? 943  GLY   A CA    1 
ATOM   6933  C  C     . GLY   A  1  945  ? -24.509 86.472  93.895  1.00 21.76 ? 943  GLY   A C     1 
ATOM   6934  O  O     . GLY   A  1  945  ? -23.704 85.644  93.459  1.00 21.28 ? 943  GLY   A O     1 
ATOM   6935  N  N     . PRO   A  1  946  ? -25.666 86.707  93.296  1.00 20.31 ? 944  PRO   A N     1 
ATOM   6936  C  CA    . PRO   A  1  946  ? -26.118 85.856  92.187  1.00 21.76 ? 944  PRO   A CA    1 
ATOM   6937  C  C     . PRO   A  1  946  ? -25.554 86.326  90.850  1.00 20.87 ? 944  PRO   A C     1 
ATOM   6938  O  O     . PRO   A  1  946  ? -26.292 86.702  89.933  1.00 21.94 ? 944  PRO   A O     1 
ATOM   6939  C  CB    . PRO   A  1  946  ? -27.639 86.012  92.263  1.00 20.28 ? 944  PRO   A CB    1 
ATOM   6940  C  CG    . PRO   A  1  946  ? -27.819 87.442  92.726  1.00 22.63 ? 944  PRO   A CG    1 
ATOM   6941  C  CD    . PRO   A  1  946  ? -26.688 87.683  93.715  1.00 20.38 ? 944  PRO   A CD    1 
ATOM   6942  N  N     . VAL   A  1  947  ? -24.229 86.301  90.735  1.00 22.28 ? 945  VAL   A N     1 
ATOM   6943  C  CA    . VAL   A  1  947  ? -23.531 86.877  89.593  1.00 22.51 ? 945  VAL   A CA    1 
ATOM   6944  C  C     . VAL   A  1  947  ? -22.588 85.834  89.026  1.00 22.22 ? 945  VAL   A C     1 
ATOM   6945  O  O     . VAL   A  1  947  ? -21.540 85.546  89.617  1.00 20.81 ? 945  VAL   A O     1 
ATOM   6946  C  CB    . VAL   A  1  947  ? -22.778 88.163  89.945  1.00 25.27 ? 945  VAL   A CB    1 
ATOM   6947  C  CG1   . VAL   A  1  947  ? -22.160 88.741  88.702  1.00 25.73 ? 945  VAL   A CG1   1 
ATOM   6948  C  CG2   . VAL   A  1  947  ? -23.741 89.166  90.573  1.00 23.04 ? 945  VAL   A CG2   1 
ATOM   6949  N  N     . LEU   A  1  948  ? -22.958 85.276  87.881  1.00 20.36 ? 946  LEU   A N     1 
ATOM   6950  C  CA    . LEU   A  1  948  ? -22.158 84.280  87.194  1.00 19.20 ? 946  LEU   A CA    1 
ATOM   6951  C  C     . LEU   A  1  948  ? -21.374 84.969  86.093  1.00 21.46 ? 946  LEU   A C     1 
ATOM   6952  O  O     . LEU   A  1  948  ? -21.941 85.716  85.290  1.00 23.96 ? 946  LEU   A O     1 
ATOM   6953  C  CB    . LEU   A  1  948  ? -23.066 83.227  86.574  1.00 20.87 ? 946  LEU   A CB    1 
ATOM   6954  C  CG    . LEU   A  1  948  ? -22.288 82.192  85.767  1.00 18.68 ? 946  LEU   A CG    1 
ATOM   6955  C  CD1   . LEU   A  1  948  ? -21.341 81.404  86.684  1.00 19.39 ? 946  LEU   A CD1   1 
ATOM   6956  C  CD2   . LEU   A  1  948  ? -23.279 81.315  85.041  1.00 21.90 ? 946  LEU   A CD2   1 
ATOM   6957  N  N     . HIS   A  1  949  ? -20.079 84.711  86.051  1.00 21.21 ? 947  HIS   A N     1 
ATOM   6958  C  CA    . HIS   A  1  949  ? -19.235 85.217  84.987  1.00 21.15 ? 947  HIS   A CA    1 
ATOM   6959  C  C     . HIS   A  1  949  ? -18.913 84.075  84.043  1.00 21.27 ? 947  HIS   A C     1 
ATOM   6960  O  O     . HIS   A  1  949  ? -18.762 82.930  84.472  1.00 21.30 ? 947  HIS   A O     1 
ATOM   6961  C  CB    . HIS   A  1  949  ? -17.963 85.821  85.557  1.00 23.53 ? 947  HIS   A CB    1 
ATOM   6962  C  CG    . HIS   A  1  949  ? -18.229 86.851  86.606  1.00 22.68 ? 947  HIS   A CG    1 
ATOM   6963  N  ND1   . HIS   A  1  949  ? -18.429 86.526  87.932  1.00 22.22 ? 947  HIS   A ND1   1 
ATOM   6964  C  CD2   . HIS   A  1  949  ? -18.378 88.192  86.516  1.00 27.19 ? 947  HIS   A CD2   1 
ATOM   6965  C  CE1   . HIS   A  1  949  ? -18.660 87.634  88.618  1.00 25.07 ? 947  HIS   A CE1   1 
ATOM   6966  N  NE2   . HIS   A  1  949  ? -18.638 88.656  87.781  1.00 26.12 ? 947  HIS   A NE2   1 
ATOM   6967  N  N     . VAL   A  1  950  ? -18.873 84.382  82.752  1.00 20.57 ? 948  VAL   A N     1 
ATOM   6968  C  CA    . VAL   A  1  950  ? -18.683 83.378  81.719  1.00 21.84 ? 948  VAL   A CA    1 
ATOM   6969  C  C     . VAL   A  1  950  ? -17.477 83.771  80.895  1.00 24.81 ? 948  VAL   A C     1 
ATOM   6970  O  O     . VAL   A  1  950  ? -17.404 84.898  80.387  1.00 26.48 ? 948  VAL   A O     1 
ATOM   6971  C  CB    . VAL   A  1  950  ? -19.927 83.231  80.829  1.00 22.32 ? 948  VAL   A CB    1 
ATOM   6972  C  CG1   . VAL   A  1  950  ? -19.667 82.197  79.723  1.00 22.73 ? 948  VAL   A CG1   1 
ATOM   6973  C  CG2   . VAL   A  1  950  ? -21.123 82.828  81.665  1.00 22.66 ? 948  VAL   A CG2   1 
ATOM   6974  N  N     . ILE   A  1  951  ? -16.530 82.849  80.773  1.00 21.54 ? 949  ILE   A N     1 
ATOM   6975  C  CA    . ILE   A  1  951  ? -15.400 83.031  79.879  1.00 23.18 ? 949  ILE   A CA    1 
ATOM   6976  C  C     . ILE   A  1  951  ? -15.355 81.853  78.921  1.00 24.46 ? 949  ILE   A C     1 
ATOM   6977  O  O     . ILE   A  1  951  ? -15.882 80.772  79.194  1.00 21.82 ? 949  ILE   A O     1 
ATOM   6978  C  CB    . ILE   A  1  951  ? -14.066 83.210  80.610  1.00 26.56 ? 949  ILE   A CB    1 
ATOM   6979  C  CG1   . ILE   A  1  951  ? -13.710 81.957  81.379  1.00 26.30 ? 949  ILE   A CG1   1 
ATOM   6980  C  CG2   . ILE   A  1  951  ? -14.140 84.407  81.553  1.00 31.75 ? 949  ILE   A CG2   1 
ATOM   6981  C  CD1   . ILE   A  1  951  ? -12.373 82.071  82.064  1.00 39.51 ? 949  ILE   A CD1   1 
ATOM   6982  N  N     . ARG   A  1  952  ? -14.735 82.088  77.772  1.00 22.87 ? 950  ARG   A N     1 
ATOM   6983  C  CA    . ARG   A  1  952  ? -14.637 81.088  76.726  1.00 20.77 ? 950  ARG   A CA    1 
ATOM   6984  C  C     . ARG   A  1  952  ? -13.175 80.727  76.548  1.00 20.75 ? 950  ARG   A C     1 
ATOM   6985  O  O     . ARG   A  1  952  ? -12.288 81.560  76.754  1.00 23.37 ? 950  ARG   A O     1 
ATOM   6986  C  CB    . ARG   A  1  952  ? -15.162 81.654  75.411  1.00 23.67 ? 950  ARG   A CB    1 
ATOM   6987  C  CG    . ARG   A  1  952  ? -16.559 82.234  75.531  1.00 24.54 ? 950  ARG   A CG    1 
ATOM   6988  C  CD    . ARG   A  1  952  ? -16.851 83.181  74.380  1.00 28.51 ? 950  ARG   A CD    1 
ATOM   6989  N  NE    . ARG   A  1  952  ? -17.203 82.473  73.154  1.00 30.82 ? 950  ARG   A NE    1 
ATOM   6990  C  CZ    . ARG   A  1  952  ? -18.440 82.345  72.696  1.00 31.71 ? 950  ARG   A CZ    1 
ATOM   6991  N  NH1   . ARG   A  1  952  ? -19.472 82.882  73.329  1.00 31.02 ? 950  ARG   A NH1   1 
ATOM   6992  N  NH2   . ARG   A  1  952  ? -18.650 81.661  71.576  1.00 29.08 ? 950  ARG   A NH2   1 
ATOM   6993  N  N     . TYR   A  1  953  ? -12.922 79.483  76.160  1.00 20.51 ? 951  TYR   A N     1 
ATOM   6994  C  CA    . TYR   A  1  953  ? -11.540 79.070  75.973  1.00 21.09 ? 951  TYR   A CA    1 
ATOM   6995  C  C     . TYR   A  1  953  ? -11.443 78.106  74.802  1.00 19.38 ? 951  TYR   A C     1 
ATOM   6996  O  O     . TYR   A  1  953  ? -12.363 77.333  74.531  1.00 21.07 ? 951  TYR   A O     1 
ATOM   6997  C  CB    . TYR   A  1  953  ? -10.953 78.438  77.250  1.00 19.46 ? 951  TYR   A CB    1 
ATOM   6998  C  CG    . TYR   A  1  953  ? -11.491 77.060  77.536  1.00 18.77 ? 951  TYR   A CG    1 
ATOM   6999  C  CD1   . TYR   A  1  953  ? -12.701 76.882  78.202  1.00 18.49 ? 951  TYR   A CD1   1 
ATOM   7000  C  CD2   . TYR   A  1  953  ? -10.797 75.923  77.116  1.00 19.80 ? 951  TYR   A CD2   1 
ATOM   7001  C  CE1   . TYR   A  1  953  ? -13.194 75.635  78.446  1.00 18.47 ? 951  TYR   A CE1   1 
ATOM   7002  C  CE2   . TYR   A  1  953  ? -11.289 74.664  77.356  1.00 17.78 ? 951  TYR   A CE2   1 
ATOM   7003  C  CZ    . TYR   A  1  953  ? -12.490 74.523  78.031  1.00 18.11 ? 951  TYR   A CZ    1 
ATOM   7004  O  OH    . TYR   A  1  953  ? -12.994 73.274  78.269  1.00 19.46 ? 951  TYR   A OH    1 
ATOM   7005  N  N     . ARG   A  1  954  ? -10.300 78.159  74.123  1.00 22.91 ? 952  ARG   A N     1 
ATOM   7006  C  CA    . ARG   A  1  954  ? -9.986  77.191  73.085  1.00 24.12 ? 952  ARG   A CA    1 
ATOM   7007  C  C     . ARG   A  1  954  ? -9.383  75.956  73.734  1.00 19.59 ? 952  ARG   A C     1 
ATOM   7008  O  O     . ARG   A  1  954  ? -8.643  76.057  74.715  1.00 21.03 ? 952  ARG   A O     1 
ATOM   7009  C  CB    . ARG   A  1  954  ? -8.998  77.794  72.089  1.00 27.84 ? 952  ARG   A CB    1 
ATOM   7010  C  CG    . ARG   A  1  954  ? -9.435  79.143  71.533  1.00 32.41 ? 952  ARG   A CG    1 
ATOM   7011  C  CD    . ARG   A  1  954  ? -9.362  79.167  70.013  1.00 47.35 ? 952  ARG   A CD    1 
ATOM   7012  N  NE    . ARG   A  1  954  ? -10.509 78.511  69.393  1.00 49.08 ? 952  ARG   A NE    1 
ATOM   7013  C  CZ    . ARG   A  1  954  ? -11.390 79.123  68.611  1.00 51.46 ? 952  ARG   A CZ    1 
ATOM   7014  N  NH1   . ARG   A  1  954  ? -11.276 80.407  68.310  1.00 53.93 ? 952  ARG   A NH1   1 
ATOM   7015  N  NH2   . ARG   A  1  954  ? -12.407 78.426  68.110  1.00 47.80 ? 952  ARG   A NH2   1 
ATOM   7016  N  N     . ARG   A  1  955  ? -9.734  74.783  73.197  1.00 23.39 ? 953  ARG   A N     1 
ATOM   7017  C  CA    . ARG   A  1  955  ? -9.349  73.524  73.828  1.00 24.68 ? 953  ARG   A CA    1 
ATOM   7018  C  C     . ARG   A  1  955  ? -7.848  73.444  74.085  1.00 20.44 ? 953  ARG   A C     1 
ATOM   7019  O  O     . ARG   A  1  955  ? -7.412  72.961  75.137  1.00 24.43 ? 953  ARG   A O     1 
ATOM   7020  C  CB    . ARG   A  1  955  ? -9.812  72.340  72.975  1.00 30.21 ? 953  ARG   A CB    1 
ATOM   7021  C  CG    . ARG   A  1  955  ? -9.332  70.974  73.481  1.00 37.22 ? 953  ARG   A CG    1 
ATOM   7022  C  CD    . ARG   A  1  955  ? -9.653  70.829  74.957  1.00 40.62 ? 953  ARG   A CD    1 
ATOM   7023  N  NE    . ARG   A  1  955  ? -9.290  69.552  75.561  1.00 47.17 ? 953  ARG   A NE    1 
ATOM   7024  C  CZ    . ARG   A  1  955  ? -8.139  69.309  76.175  1.00 41.44 ? 953  ARG   A CZ    1 
ATOM   7025  N  NH1   . ARG   A  1  955  ? -7.169  70.211  76.210  1.00 33.54 ? 953  ARG   A NH1   1 
ATOM   7026  N  NH2   . ARG   A  1  955  ? -7.957  68.133  76.770  1.00 40.51 ? 953  ARG   A NH2   1 
ATOM   7027  N  N     . ASP   A  1  956  ? -7.036  73.915  73.142  1.00 23.04 ? 954  ASP   A N     1 
ATOM   7028  C  CA    . ASP   A  1  956  ? -5.595  73.820  73.339  1.00 23.05 ? 954  ASP   A CA    1 
ATOM   7029  C  C     . ASP   A  1  956  ? -5.111  74.691  74.484  1.00 24.66 ? 954  ASP   A C     1 
ATOM   7030  O  O     . ASP   A  1  956  ? -3.987  74.493  74.964  1.00 25.52 ? 954  ASP   A O     1 
ATOM   7031  C  CB    . ASP   A  1  956  ? -4.847  74.207  72.070  1.00 23.65 ? 954  ASP   A CB    1 
ATOM   7032  C  CG    . ASP   A  1  956  ? -4.994  73.180  70.973  1.00 27.87 ? 954  ASP   A CG    1 
ATOM   7033  O  OD1   . ASP   A  1  956  ? -5.362  72.030  71.286  1.00 31.04 ? 954  ASP   A OD1   1 
ATOM   7034  O  OD2   . ASP   A  1  956  ? -4.726  73.525  69.802  1.00 36.98 ? 954  ASP   A OD2   1 
ATOM   7035  N  N     . ASP   A  1  957  ? -5.922  75.653  74.921  1.00 21.66 ? 955  ASP   A N     1 
ATOM   7036  C  CA    . ASP   A  1  957  ? -5.559  76.546  76.009  1.00 23.14 ? 955  ASP   A CA    1 
ATOM   7037  C  C     . ASP   A  1  957  ? -6.097  76.073  77.347  1.00 22.32 ? 955  ASP   A C     1 
ATOM   7038  O  O     . ASP   A  1  957  ? -6.116  76.847  78.303  1.00 23.09 ? 955  ASP   A O     1 
ATOM   7039  C  CB    . ASP   A  1  957  ? -6.049  77.964  75.719  1.00 25.39 ? 955  ASP   A CB    1 
ATOM   7040  C  CG    . ASP   A  1  957  ? -5.381  78.571  74.507  1.00 33.24 ? 955  ASP   A CG    1 
ATOM   7041  O  OD1   . ASP   A  1  957  ? -4.206  78.239  74.251  1.00 32.56 ? 955  ASP   A OD1   1 
ATOM   7042  O  OD2   . ASP   A  1  957  ? -6.030  79.371  73.808  1.00 34.43 ? 955  ASP   A OD2   1 
ATOM   7043  N  N     . LEU   A  1  958  ? -6.541  74.821  77.432  1.00 20.48 ? 956  LEU   A N     1 
ATOM   7044  C  CA    . LEU   A  1  958  ? -7.126  74.331  78.678  1.00 19.48 ? 956  LEU   A CA    1 
ATOM   7045  C  C     . LEU   A  1  958  ? -6.128  74.403  79.831  1.00 20.98 ? 956  LEU   A C     1 
ATOM   7046  O  O     . LEU   A  1  958  ? -6.480  74.809  80.947  1.00 19.71 ? 956  LEU   A O     1 
ATOM   7047  C  CB    . LEU   A  1  958  ? -7.617  72.899  78.489  1.00 21.57 ? 956  LEU   A CB    1 
ATOM   7048  C  CG    . LEU   A  1  958  ? -8.130  72.219  79.757  1.00 20.30 ? 956  LEU   A CG    1 
ATOM   7049  C  CD1   . LEU   A  1  958  ? -9.301  72.989  80.355  1.00 20.46 ? 956  LEU   A CD1   1 
ATOM   7050  C  CD2   . LEU   A  1  958  ? -8.504  70.769  79.480  1.00 23.97 ? 956  LEU   A CD2   1 
ATOM   7051  N  N     . ASP   A  1  959  ? -4.872  74.029  79.586  1.00 17.79 ? 957  ASP   A N     1 
ATOM   7052  C  CA    . ASP   A  1  959  ? -3.889  74.066  80.661  1.00 19.71 ? 957  ASP   A CA    1 
ATOM   7053  C  C     . ASP   A  1  959  ? -3.643  75.493  81.124  1.00 19.76 ? 957  ASP   A C     1 
ATOM   7054  O  O     . ASP   A  1  959  ? -3.525  75.750  82.327  1.00 20.29 ? 957  ASP   A O     1 
ATOM   7055  C  CB    . ASP   A  1  959  ? -2.577  73.412  80.230  1.00 20.60 ? 957  ASP   A CB    1 
ATOM   7056  C  CG    . ASP   A  1  959  ? -1.700  73.095  81.410  1.00 24.58 ? 957  ASP   A CG    1 
ATOM   7057  O  OD1   . ASP   A  1  959  ? -2.183  72.408  82.326  1.00 23.62 ? 957  ASP   A OD1   1 
ATOM   7058  O  OD2   . ASP   A  1  959  ? -0.540  73.544  81.446  1.00 30.13 ? 957  ASP   A OD2   1 
ATOM   7059  N  N     . ARG   A  1  960  ? -3.565  76.432  80.183  1.00 19.73 ? 958  ARG   A N     1 
ATOM   7060  C  CA    . ARG   A  1  960  ? -3.419  77.838  80.545  1.00 22.84 ? 958  ARG   A CA    1 
ATOM   7061  C  C     . ARG   A  1  960  ? -4.613  78.302  81.363  1.00 20.97 ? 958  ARG   A C     1 
ATOM   7062  O  O     . ARG   A  1  960  ? -4.461  79.057  82.334  1.00 23.25 ? 958  ARG   A O     1 
ATOM   7063  C  CB    . ARG   A  1  960  ? -3.281  78.669  79.267  1.00 23.18 ? 958  ARG   A CB    1 
ATOM   7064  C  CG    . ARG   A  1  960  ? -3.022  80.160  79.467  1.00 26.88 ? 958  ARG   A CG    1 
ATOM   7065  C  CD    . ARG   A  1  960  ? -4.320  80.983  79.507  1.00 39.81 ? 958  ARG   A CD    1 
ATOM   7066  N  NE    . ARG   A  1  960  ? -5.338  80.479  78.592  1.00 40.24 ? 958  ARG   A NE    1 
ATOM   7067  C  CZ    . ARG   A  1  960  ? -6.641  80.699  78.722  1.00 41.85 ? 958  ARG   A CZ    1 
ATOM   7068  N  NH1   . ARG   A  1  960  ? -7.123  81.439  79.707  1.00 43.34 ? 958  ARG   A NH1   1 
ATOM   7069  N  NH2   . ARG   A  1  960  ? -7.483  80.152  77.849  1.00 44.42 ? 958  ARG   A NH2   1 
ATOM   7070  N  N     . LEU   A  1  961  ? -5.807  77.848  80.990  1.00 19.57 ? 959  LEU   A N     1 
ATOM   7071  C  CA    . LEU   A  1  961  ? -7.018  78.220  81.712  1.00 20.25 ? 959  LEU   A CA    1 
ATOM   7072  C  C     . LEU   A  1  961  ? -6.969  77.730  83.152  1.00 20.61 ? 959  LEU   A C     1 
ATOM   7073  O  O     . LEU   A  1  961  ? -7.335  78.462  84.078  1.00 20.24 ? 959  LEU   A O     1 
ATOM   7074  C  CB    . LEU   A  1  961  ? -8.237  77.649  81.000  1.00 19.53 ? 959  LEU   A CB    1 
ATOM   7075  C  CG    . LEU   A  1  961  ? -9.535  77.791  81.783  1.00 19.39 ? 959  LEU   A CG    1 
ATOM   7076  C  CD1   . LEU   A  1  961  ? -9.910  79.262  81.902  1.00 26.66 ? 959  LEU   A CD1   1 
ATOM   7077  C  CD2   . LEU   A  1  961  ? -10.620 76.994  81.093  1.00 23.41 ? 959  LEU   A CD2   1 
ATOM   7078  N  N     . VAL   A  1  962  ? -6.559  76.477  83.362  1.00 18.58 ? 960  VAL   A N     1 
ATOM   7079  C  CA    . VAL   A  1  962  ? -6.410  75.985  84.729  1.00 19.52 ? 960  VAL   A CA    1 
ATOM   7080  C  C     . VAL   A  1  962  ? -5.432  76.852  85.507  1.00 22.27 ? 960  VAL   A C     1 
ATOM   7081  O  O     . VAL   A  1  962  ? -5.672  77.180  86.676  1.00 19.80 ? 960  VAL   A O     1 
ATOM   7082  C  CB    . VAL   A  1  962  ? -6.026  74.496  84.744  1.00 19.81 ? 960  VAL   A CB    1 
ATOM   7083  C  CG1   . VAL   A  1  962  ? -5.730  74.030  86.178  1.00 22.63 ? 960  VAL   A CG1   1 
ATOM   7084  C  CG2   . VAL   A  1  962  ? -7.140  73.670  84.131  1.00 22.51 ? 960  VAL   A CG2   1 
ATOM   7085  N  N     . ASP   A  1  963  ? -4.321  77.246  84.876  1.00 21.87 ? 961  ASP   A N     1 
ATOM   7086  C  CA    . ASP   A  1  963  ? -3.410  78.190  85.517  1.00 21.43 ? 961  ASP   A CA    1 
ATOM   7087  C  C     . ASP   A  1  963  ? -4.129  79.478  85.889  1.00 22.91 ? 961  ASP   A C     1 
ATOM   7088  O  O     . ASP   A  1  963  ? -3.922  80.013  86.986  1.00 24.87 ? 961  ASP   A O     1 
ATOM   7089  C  CB    . ASP   A  1  963  ? -2.253  78.532  84.582  1.00 23.69 ? 961  ASP   A CB    1 
ATOM   7090  C  CG    . ASP   A  1  963  ? -1.275  77.405  84.418  1.00 29.03 ? 961  ASP   A CG    1 
ATOM   7091  O  OD1   . ASP   A  1  963  ? -1.173  76.555  85.321  1.00 40.76 ? 961  ASP   A OD1   1 
ATOM   7092  O  OD2   . ASP   A  1  963  ? -0.592  77.387  83.368  1.00 41.02 ? 961  ASP   A OD2   1 
ATOM   7093  N  N     . ASP   A  1  964  ? -4.959  80.001  84.981  1.00 22.57 ? 962  ASP   A N     1 
ATOM   7094  C  CA    . ASP   A  1  964  ? -5.690  81.233  85.264  1.00 25.72 ? 962  ASP   A CA    1 
ATOM   7095  C  C     . ASP   A  1  964  ? -6.616  81.060  86.461  1.00 26.88 ? 962  ASP   A C     1 
ATOM   7096  O  O     . ASP   A  1  964  ? -6.755  81.973  87.285  1.00 26.83 ? 962  ASP   A O     1 
ATOM   7097  C  CB    . ASP   A  1  964  ? -6.499  81.666  84.041  1.00 28.07 ? 962  ASP   A CB    1 
ATOM   7098  C  CG    . ASP   A  1  964  ? -5.623  82.156  82.906  1.00 31.52 ? 962  ASP   A CG    1 
ATOM   7099  O  OD1   . ASP   A  1  964  ? -4.421  82.408  83.142  1.00 34.34 ? 962  ASP   A OD1   1 
ATOM   7100  O  OD2   . ASP   A  1  964  ? -6.146  82.281  81.778  1.00 38.27 ? 962  ASP   A OD2   1 
ATOM   7101  N  N     . VAL   A  1  965  ? -7.282  79.910  86.563  1.00 22.65 ? 963  VAL   A N     1 
ATOM   7102  C  CA    . VAL   A  1  965  ? -8.145  79.668  87.716  1.00 22.58 ? 963  VAL   A CA    1 
ATOM   7103  C  C     . VAL   A  1  965  ? -7.316  79.656  88.990  1.00 25.64 ? 963  VAL   A C     1 
ATOM   7104  O  O     . VAL   A  1  965  ? -7.671  80.291  89.991  1.00 25.01 ? 963  VAL   A O     1 
ATOM   7105  C  CB    . VAL   A  1  965  ? -8.938  78.362  87.537  1.00 19.44 ? 963  VAL   A CB    1 
ATOM   7106  C  CG1   . VAL   A  1  965  ? -9.708  78.029  88.811  1.00 21.65 ? 963  VAL   A CG1   1 
ATOM   7107  C  CG2   . VAL   A  1  965  ? -9.893  78.471  86.345  1.00 22.11 ? 963  VAL   A CG2   1 
ATOM   7108  N  N     . ASN   A  1  966  ? -6.186  78.948  88.962  1.00 20.52 ? 964  ASN   A N     1 
ATOM   7109  C  CA    . ASN   A  1  966  ? -5.317  78.892  90.132  1.00 21.60 ? 964  ASN   A CA    1 
ATOM   7110  C  C     . ASN   A  1  966  ? -4.763  80.269  90.473  1.00 24.31 ? 964  ASN   A C     1 
ATOM   7111  O  O     . ASN   A  1  966  ? -4.539  80.580  91.651  1.00 24.60 ? 964  ASN   A O     1 
ATOM   7112  C  CB    . ASN   A  1  966  ? -4.163  77.913  89.883  1.00 21.12 ? 964  ASN   A CB    1 
ATOM   7113  C  CG    . ASN   A  1  966  ? -4.607  76.450  89.890  1.00 20.80 ? 964  ASN   A CG    1 
ATOM   7114  O  OD1   . ASN   A  1  966  ? -5.654  76.106  90.441  1.00 21.72 ? 964  ASN   A OD1   1 
ATOM   7115  N  ND2   . ASN   A  1  966  ? -3.807  75.587  89.270  1.00 21.66 ? 964  ASN   A ND2   1 
ATOM   7116  N  N     . ALA   A  1  967  ? -4.565  81.115  89.460  1.00 24.32 ? 965  ALA   A N     1 
ATOM   7117  C  CA    . ALA   A  1  967  ? -3.872  82.386  89.649  1.00 27.80 ? 965  ALA   A CA    1 
ATOM   7118  C  C     . ALA   A  1  967  ? -4.659  83.383  90.488  1.00 26.11 ? 965  ALA   A C     1 
ATOM   7119  O  O     . ALA   A  1  967  ? -4.070  84.360  90.964  1.00 30.72 ? 965  ALA   A O     1 
ATOM   7120  C  CB    . ALA   A  1  967  ? -3.519  83.007  88.296  1.00 31.86 ? 965  ALA   A CB    1 
ATOM   7121  N  N     . THR   A  1  968  ? -5.958  83.167  90.697  1.00 23.69 ? 966  THR   A N     1 
ATOM   7122  C  CA    . THR   A  1  968  ? -6.705  84.069  91.572  1.00 23.60 ? 966  THR   A CA    1 
ATOM   7123  C  C     . THR   A  1  968  ? -6.220  83.995  93.010  1.00 24.42 ? 966  THR   A C     1 
ATOM   7124  O  O     . THR   A  1  968  ? -6.462  84.935  93.775  1.00 26.15 ? 966  THR   A O     1 
ATOM   7125  C  CB    . THR   A  1  968  ? -8.196  83.735  91.586  1.00 25.27 ? 966  THR   A CB    1 
ATOM   7126  O  OG1   . THR   A  1  968  ? -8.400  82.495  92.279  1.00 23.60 ? 966  THR   A OG1   1 
ATOM   7127  C  CG2   . THR   A  1  968  ? -8.769  83.648  90.169  1.00 22.58 ? 966  THR   A CG2   1 
ATOM   7128  N  N     . GLY   A  1  969  ? -5.577  82.895  93.401  1.00 23.16 ? 967  GLY   A N     1 
ATOM   7129  C  CA    . GLY   A  1  969  ? -5.179  82.677  94.775  1.00 22.29 ? 967  GLY   A CA    1 
ATOM   7130  C  C     . GLY   A  1  969  ? -6.218  81.971  95.617  1.00 20.17 ? 967  GLY   A C     1 
ATOM   7131  O  O     . GLY   A  1  969  ? -5.889  81.486  96.707  1.00 19.98 ? 967  GLY   A O     1 
ATOM   7132  N  N     . TYR   A  1  970  ? -7.459  81.906  95.143  1.00 19.88 ? 968  TYR   A N     1 
ATOM   7133  C  CA    . TYR   A  1  970  ? -8.483  81.139  95.817  1.00 20.06 ? 968  TYR   A CA    1 
ATOM   7134  C  C     . TYR   A  1  970  ? -8.316  79.661  95.491  1.00 17.23 ? 968  TYR   A C     1 
ATOM   7135  O  O     . TYR   A  1  970  ? -7.508  79.264  94.644  1.00 21.99 ? 968  TYR   A O     1 
ATOM   7136  C  CB    . TYR   A  1  970  ? -9.868  81.626  95.401  1.00 20.04 ? 968  TYR   A CB    1 
ATOM   7137  C  CG    . TYR   A  1  970  ? -10.181 83.028  95.867  1.00 20.78 ? 968  TYR   A CG    1 
ATOM   7138  C  CD1   . TYR   A  1  970  ? -10.679 83.261  97.144  1.00 22.48 ? 968  TYR   A CD1   1 
ATOM   7139  C  CD2   . TYR   A  1  970  ? -9.989  84.117  95.026  1.00 23.28 ? 968  TYR   A CD2   1 
ATOM   7140  C  CE1   . TYR   A  1  970  ? -10.991 84.550  97.569  1.00 24.36 ? 968  TYR   A CE1   1 
ATOM   7141  C  CE2   . TYR   A  1  970  ? -10.288 85.405  95.443  1.00 26.11 ? 968  TYR   A CE2   1 
ATOM   7142  C  CZ    . TYR   A  1  970  ? -10.784 85.613  96.714  1.00 27.25 ? 968  TYR   A CZ    1 
ATOM   7143  O  OH    . TYR   A  1  970  ? -11.083 86.893  97.130  1.00 34.55 ? 968  TYR   A OH    1 
ATOM   7144  N  N     . GLY   A  1  971  ? -9.096  78.841  96.164  1.00 16.62 ? 969  GLY   A N     1 
ATOM   7145  C  CA    . GLY   A  1  971  ? -8.964  77.415  95.975  1.00 16.08 ? 969  GLY   A CA    1 
ATOM   7146  C  C     . GLY   A  1  971  ? -10.005 76.658  96.753  1.00 15.91 ? 969  GLY   A C     1 
ATOM   7147  O  O     . GLY   A  1  971  ? -9.685  75.740  97.513  1.00 16.43 ? 969  GLY   A O     1 
ATOM   7148  N  N     . LEU   A  1  972  ? -11.270 77.034  96.559  1.00 15.37 ? 970  LEU   A N     1 
ATOM   7149  C  CA    . LEU   A  1  972  ? -12.347 76.450  97.354  1.00 15.66 ? 970  LEU   A CA    1 
ATOM   7150  C  C     . LEU   A  1  972  ? -13.020 75.326  96.573  1.00 16.07 ? 970  LEU   A C     1 
ATOM   7151  O  O     . LEU   A  1  972  ? -12.596 74.173  96.673  1.00 16.92 ? 970  LEU   A O     1 
ATOM   7152  C  CB    . LEU   A  1  972  ? -13.309 77.527  97.846  1.00 16.22 ? 970  LEU   A CB    1 
ATOM   7153  C  CG    . LEU   A  1  972  ? -14.357 77.044  98.855  1.00 16.26 ? 970  LEU   A CG    1 
ATOM   7154  C  CD1   . LEU   A  1  972  ? -13.700 76.306  100.031 1.00 17.20 ? 970  LEU   A CD1   1 
ATOM   7155  C  CD2   . LEU   A  1  972  ? -15.172 78.234  99.365  1.00 19.08 ? 970  LEU   A CD2   1 
ATOM   7156  N  N     . THR   A  1  973  ? -14.038 75.632  95.766  1.00 16.14 ? 971  THR   A N     1 
ATOM   7157  C  CA    . THR   A  1  973  ? -14.678 74.607  94.957  1.00 15.77 ? 971  THR   A CA    1 
ATOM   7158  C  C     . THR   A  1  973  ? -14.296 74.773  93.497  1.00 15.37 ? 971  THR   A C     1 
ATOM   7159  O  O     . THR   A  1  973  ? -13.926 75.854  93.043  1.00 15.40 ? 971  THR   A O     1 
ATOM   7160  C  CB    . THR   A  1  973  ? -16.202 74.622  95.098  1.00 15.02 ? 971  THR   A CB    1 
ATOM   7161  O  OG1   . THR   A  1  973  ? -16.685 75.898  94.696  1.00 16.24 ? 971  THR   A OG1   1 
ATOM   7162  C  CG2   . THR   A  1  973  ? -16.611 74.331  96.533  1.00 15.34 ? 971  THR   A CG2   1 
ATOM   7163  N  N     . PHE   A  1  974  ? -14.382 73.663  92.772  1.00 14.99 ? 972  PHE   A N     1 
ATOM   7164  C  CA    . PHE   A  1  974  ? -14.055 73.647  91.358  1.00 15.32 ? 972  PHE   A CA    1 
ATOM   7165  C  C     . PHE   A  1  974  ? -14.849 72.542  90.699  1.00 14.17 ? 972  PHE   A C     1 
ATOM   7166  O  O     . PHE   A  1  974  ? -14.934 71.436  91.226  1.00 16.01 ? 972  PHE   A O     1 
ATOM   7167  C  CB    . PHE   A  1  974  ? -12.568 73.349  91.159  1.00 15.90 ? 972  PHE   A CB    1 
ATOM   7168  C  CG    . PHE   A  1  974  ? -12.210 73.166  89.724  1.00 16.21 ? 972  PHE   A CG    1 
ATOM   7169  C  CD1   . PHE   A  1  974  ? -12.050 74.263  88.913  1.00 14.92 ? 972  PHE   A CD1   1 
ATOM   7170  C  CD2   . PHE   A  1  974  ? -12.127 71.891  89.171  1.00 15.10 ? 972  PHE   A CD2   1 
ATOM   7171  C  CE1   . PHE   A  1  974  ? -11.764 74.106  87.564  1.00 16.93 ? 972  PHE   A CE1   1 
ATOM   7172  C  CE2   . PHE   A  1  974  ? -11.831 71.722  87.821  1.00 15.11 ? 972  PHE   A CE2   1 
ATOM   7173  C  CZ    . PHE   A  1  974  ? -11.645 72.829  87.030  1.00 15.76 ? 972  PHE   A CZ    1 
ATOM   7174  N  N     . GLY   A  1  975  ? -15.426 72.840  89.545  1.00 15.03 ? 973  GLY   A N     1 
ATOM   7175  C  CA    . GLY   A  1  975  ? -16.191 71.865  88.803  1.00 15.02 ? 973  GLY   A CA    1 
ATOM   7176  C  C     . GLY   A  1  975  ? -15.617 71.612  87.425  1.00 14.39 ? 973  GLY   A C     1 
ATOM   7177  O  O     . GLY   A  1  975  ? -15.061 72.503  86.788  1.00 14.21 ? 973  GLY   A O     1 
ATOM   7178  N  N     . LEU   A  1  976  ? -15.797 70.390  86.962  1.00 15.31 ? 974  LEU   A N     1 
ATOM   7179  C  CA    . LEU   A  1  976  ? -15.395 70.026  85.612  1.00 15.30 ? 974  LEU   A CA    1 
ATOM   7180  C  C     . LEU   A  1  976  ? -16.490 69.169  85.020  1.00 14.10 ? 974  LEU   A C     1 
ATOM   7181  O  O     . LEU   A  1  976  ? -16.898 68.174  85.624  1.00 15.20 ? 974  LEU   A O     1 
ATOM   7182  C  CB    . LEU   A  1  976  ? -14.101 69.221  85.654  1.00 14.86 ? 974  LEU   A CB    1 
ATOM   7183  C  CG    . LEU   A  1  976  ? -13.654 68.611  84.334  1.00 15.16 ? 974  LEU   A CG    1 
ATOM   7184  C  CD1   . LEU   A  1  976  ? -13.282 69.730  83.365  1.00 17.98 ? 974  LEU   A CD1   1 
ATOM   7185  C  CD2   . LEU   A  1  976  ? -12.486 67.700  84.606  1.00 18.63 ? 974  LEU   A CD2   1 
ATOM   7186  N  N     . HIS   A  1  977  ? -16.962 69.559  83.842  1.00 14.99 ? 975  HIS   A N     1 
ATOM   7187  C  CA    . HIS   A  1  977  ? -17.941 68.784  83.092  1.00 15.30 ? 975  HIS   A CA    1 
ATOM   7188  C  C     . HIS   A  1  977  ? -17.257 68.301  81.826  1.00 13.78 ? 975  HIS   A C     1 
ATOM   7189  O  O     . HIS   A  1  977  ? -16.954 69.095  80.925  1.00 15.32 ? 975  HIS   A O     1 
ATOM   7190  C  CB    . HIS   A  1  977  ? -19.186 69.607  82.753  1.00 15.93 ? 975  HIS   A CB    1 
ATOM   7191  C  CG    . HIS   A  1  977  ? -20.263 69.506  83.779  1.00 17.86 ? 975  HIS   A CG    1 
ATOM   7192  N  ND1   . HIS   A  1  977  ? -21.393 68.738  83.593  1.00 23.98 ? 975  HIS   A ND1   1 
ATOM   7193  C  CD2   . HIS   A  1  977  ? -20.366 70.041  85.018  1.00 24.07 ? 975  HIS   A CD2   1 
ATOM   7194  C  CE1   . HIS   A  1  977  ? -22.157 68.830  84.667  1.00 21.19 ? 975  HIS   A CE1   1 
ATOM   7195  N  NE2   . HIS   A  1  977  ? -21.562 69.618  85.540  1.00 24.28 ? 975  HIS   A NE2   1 
ATOM   7196  N  N     . THR   A  1  978  ? -17.032 66.998  81.773  1.00 13.88 ? 976  THR   A N     1 
ATOM   7197  C  CA    . THR   A  1  978  ? -16.430 66.347  80.624  1.00 15.61 ? 976  THR   A CA    1 
ATOM   7198  C  C     . THR   A  1  978  ? -16.709 64.868  80.740  1.00 16.06 ? 976  THR   A C     1 
ATOM   7199  O  O     . THR   A  1  978  ? -16.865 64.329  81.836  1.00 17.75 ? 976  THR   A O     1 
ATOM   7200  C  CB    . THR   A  1  978  ? -14.912 66.566  80.577  1.00 16.34 ? 976  THR   A CB    1 
ATOM   7201  O  OG1   . THR   A  1  978  ? -14.382 65.884  79.435  1.00 16.58 ? 976  THR   A OG1   1 
ATOM   7202  C  CG2   . THR   A  1  978  ? -14.244 65.988  81.796  1.00 17.37 ? 976  THR   A CG2   1 
ATOM   7203  N  N     . ARG   A  1  979  ? -16.740 64.207  79.596  1.00 16.51 ? 977  ARG   A N     1 
ATOM   7204  C  CA    . ARG   A  1  979  ? -16.824 62.760  79.585  1.00 18.36 ? 977  ARG   A CA    1 
ATOM   7205  C  C     . ARG   A  1  979  ? -15.470 62.108  79.394  1.00 16.68 ? 977  ARG   A C     1 
ATOM   7206  O  O     . ARG   A  1  979  ? -15.386 60.877  79.405  1.00 19.94 ? 977  ARG   A O     1 
ATOM   7207  C  CB    . ARG   A  1  979  ? -17.763 62.312  78.478  1.00 18.13 ? 977  ARG   A CB    1 
ATOM   7208  C  CG    . ARG   A  1  979  ? -19.167 62.810  78.690  1.00 22.22 ? 977  ARG   A CG    1 
ATOM   7209  C  CD    . ARG   A  1  979  ? -20.029 62.493  77.509  1.00 31.28 ? 977  ARG   A CD    1 
ATOM   7210  N  NE    . ARG   A  1  979  ? -21.428 62.766  77.802  1.00 34.39 ? 977  ARG   A NE    1 
ATOM   7211  C  CZ    . ARG   A  1  979  ? -22.431 62.409  77.016  1.00 40.17 ? 977  ARG   A CZ    1 
ATOM   7212  N  NH1   . ARG   A  1  979  ? -22.217 61.784  75.869  1.00 32.34 ? 977  ARG   A NH1   1 
ATOM   7213  N  NH2   . ARG   A  1  979  ? -23.677 62.677  77.395  1.00 35.54 ? 977  ARG   A NH2   1 
ATOM   7214  N  N     . LEU   A  1  980  ? -14.412 62.893  79.242  1.00 15.26 ? 978  LEU   A N     1 
ATOM   7215  C  CA    . LEU   A  1  980  ? -13.148 62.384  78.719  1.00 15.29 ? 978  LEU   A CA    1 
ATOM   7216  C  C     . LEU   A  1  980  ? -12.131 62.194  79.841  1.00 16.37 ? 978  LEU   A C     1 
ATOM   7217  O  O     . LEU   A  1  980  ? -11.742 63.159  80.506  1.00 16.95 ? 978  LEU   A O     1 
ATOM   7218  C  CB    . LEU   A  1  980  ? -12.592 63.339  77.671  1.00 16.08 ? 978  LEU   A CB    1 
ATOM   7219  C  CG    . LEU   A  1  980  ? -13.546 63.702  76.548  1.00 15.73 ? 978  LEU   A CG    1 
ATOM   7220  C  CD1   . LEU   A  1  980  ? -12.890 64.707  75.634  1.00 18.75 ? 978  LEU   A CD1   1 
ATOM   7221  C  CD2   . LEU   A  1  980  ? -13.958 62.432  75.793  1.00 18.95 ? 978  LEU   A CD2   1 
ATOM   7222  N  N     . ASP   A  1  981  ? -11.675 60.951  80.021  1.00 16.11 ? 979  ASP   A N     1 
ATOM   7223  C  CA    . ASP   A  1  981  ? -10.732 60.647  81.097  1.00 17.34 ? 979  ASP   A CA    1 
ATOM   7224  C  C     . ASP   A  1  981  ? -9.455  61.464  80.984  1.00 17.22 ? 979  ASP   A C     1 
ATOM   7225  O  O     . ASP   A  1  981  ? -8.871  61.844  82.008  1.00 16.42 ? 979  ASP   A O     1 
ATOM   7226  C  CB    . ASP   A  1  981  ? -10.356 59.173  81.061  1.00 17.97 ? 979  ASP   A CB    1 
ATOM   7227  C  CG    . ASP   A  1  981  ? -11.452 58.278  81.544  1.00 19.13 ? 979  ASP   A CG    1 
ATOM   7228  O  OD1   . ASP   A  1  981  ? -12.406 58.773  82.166  1.00 21.46 ? 979  ASP   A OD1   1 
ATOM   7229  O  OD2   . ASP   A  1  981  ? -11.347 57.061  81.302  1.00 22.05 ? 979  ASP   A OD2   1 
ATOM   7230  N  N     . GLU   A  1  982  ? -8.951  61.685  79.771  1.00 16.60 ? 980  GLU   A N     1 
ATOM   7231  C  CA    . GLU   A  1  982  ? -7.714  62.448  79.660  1.00 16.52 ? 980  GLU   A CA    1 
ATOM   7232  C  C     . GLU   A  1  982  ? -7.909  63.851  80.214  1.00 16.20 ? 980  GLU   A C     1 
ATOM   7233  O  O     . GLU   A  1  982  ? -7.037  64.385  80.911  1.00 16.89 ? 980  GLU   A O     1 
ATOM   7234  C  CB    . GLU   A  1  982  ? -7.245  62.502  78.206  1.00 17.79 ? 980  GLU   A CB    1 
ATOM   7235  C  CG    . GLU   A  1  982  ? -5.999  63.375  78.027  1.00 19.49 ? 980  GLU   A CG    1 
ATOM   7236  C  CD    . GLU   A  1  982  ? -5.738  63.765  76.588  1.00 25.43 ? 980  GLU   A CD    1 
ATOM   7237  O  OE1   . GLU   A  1  982  ? -6.663  64.267  75.922  1.00 27.89 ? 980  GLU   A OE1   1 
ATOM   7238  O  OE2   . GLU   A  1  982  ? -4.597  63.583  76.115  1.00 22.40 ? 980  GLU   A OE2   1 
ATOM   7239  N  N     . THR   A  1  983  ? -9.071  64.441  79.947  1.00 15.23 ? 981  THR   A N     1 
ATOM   7240  C  CA    . THR   A  1  983  ? -9.328  65.792  80.416  1.00 16.09 ? 981  THR   A CA    1 
ATOM   7241  C  C     . THR   A  1  983  ? -9.517  65.799  81.923  1.00 15.04 ? 981  THR   A C     1 
ATOM   7242  O  O     . THR   A  1  983  ? -9.003  66.690  82.611  1.00 16.36 ? 981  THR   A O     1 
ATOM   7243  C  CB    . THR   A  1  983  ? -10.551 66.349  79.693  1.00 15.50 ? 981  THR   A CB    1 
ATOM   7244  O  OG1   . THR   A  1  983  ? -10.252 66.439  78.291  1.00 18.71 ? 981  THR   A OG1   1 
ATOM   7245  C  CG2   . THR   A  1  983  ? -10.935 67.724  80.243  1.00 18.28 ? 981  THR   A CG2   1 
ATOM   7246  N  N     . ILE   A  1  984  ? -10.199 64.782  82.455  1.00 15.17 ? 982  ILE   A N     1 
ATOM   7247  C  CA    . ILE   A  1  984  ? -10.345 64.662  83.905  1.00 16.19 ? 982  ILE   A CA    1 
ATOM   7248  C  C     . ILE   A  1  984  ? -8.983  64.561  84.568  1.00 16.16 ? 982  ILE   A C     1 
ATOM   7249  O  O     . ILE   A  1  984  ? -8.703  65.247  85.558  1.00 15.63 ? 982  ILE   A O     1 
ATOM   7250  C  CB    . ILE   A  1  984  ? -11.228 63.457  84.262  1.00 16.14 ? 982  ILE   A CB    1 
ATOM   7251  C  CG1   . ILE   A  1  984  ? -12.654 63.707  83.791  1.00 17.74 ? 982  ILE   A CG1   1 
ATOM   7252  C  CG2   . ILE   A  1  984  ? -11.202 63.196  85.763  1.00 18.76 ? 982  ILE   A CG2   1 
ATOM   7253  C  CD1   . ILE   A  1  984  ? -13.541 62.487  83.921  1.00 21.06 ? 982  ILE   A CD1   1 
ATOM   7254  N  N     . ALA   A  1  985  ? -8.126  63.682  84.046  1.00 14.81 ? 983  ALA   A N     1 
ATOM   7255  C  CA    . ALA   A  1  985  ? -6.828  63.476  84.672  1.00 17.06 ? 983  ALA   A CA    1 
ATOM   7256  C  C     . ALA   A  1  985  ? -6.002  64.747  84.607  1.00 15.71 ? 983  ALA   A C     1 
ATOM   7257  O  O     . ALA   A  1  985  ? -5.379  65.138  85.604  1.00 17.56 ? 983  ALA   A O     1 
ATOM   7258  C  CB    . ALA   A  1  985  ? -6.106  62.327  83.968  1.00 17.74 ? 983  ALA   A CB    1 
ATOM   7259  N  N     . HIS   A  1  986  ? -5.994  65.404  83.451  1.00 16.57 ? 984  HIS   A N     1 
ATOM   7260  C  CA    . HIS   A  1  986  ? -5.238  66.640  83.293  1.00 17.51 ? 984  HIS   A CA    1 
ATOM   7261  C  C     . HIS   A  1  986  ? -5.741  67.706  84.254  1.00 17.15 ? 984  HIS   A C     1 
ATOM   7262  O  O     . HIS   A  1  986  ? -4.992  68.230  85.083  1.00 17.60 ? 984  HIS   A O     1 
ATOM   7263  C  CB    . HIS   A  1  986  ? -5.381  67.101  81.847  1.00 18.03 ? 984  HIS   A CB    1 
ATOM   7264  C  CG    . HIS   A  1  986  ? -4.819  68.459  81.560  1.00 20.66 ? 984  HIS   A CG    1 
ATOM   7265  N  ND1   . HIS   A  1  986  ? -5.013  69.089  80.351  1.00 25.73 ? 984  HIS   A ND1   1 
ATOM   7266  C  CD2   . HIS   A  1  986  ? -4.067  69.303  82.306  1.00 20.14 ? 984  HIS   A CD2   1 
ATOM   7267  C  CE1   . HIS   A  1  986  ? -4.410  70.265  80.367  1.00 27.70 ? 984  HIS   A CE1   1 
ATOM   7268  N  NE2   . HIS   A  1  986  ? -3.841  70.426  81.548  1.00 20.11 ? 984  HIS   A NE2   1 
ATOM   7269  N  N     . VAL   A  1  987  ? -7.031  68.016  84.175  1.00 17.07 ? 985  VAL   A N     1 
ATOM   7270  C  CA    . VAL   A  1  987  ? -7.549  69.135  84.948  1.00 16.32 ? 985  VAL   A CA    1 
ATOM   7271  C  C     . VAL   A  1  987  ? -7.448  68.866  86.439  1.00 17.42 ? 985  VAL   A C     1 
ATOM   7272  O  O     . VAL   A  1  987  ? -7.053  69.750  87.213  1.00 17.41 ? 985  VAL   A O     1 
ATOM   7273  C  CB    . VAL   A  1  987  ? -8.982  69.453  84.513  1.00 15.63 ? 985  VAL   A CB    1 
ATOM   7274  C  CG1   . VAL   A  1  987  ? -9.605  70.462  85.482  1.00 16.94 ? 985  VAL   A CG1   1 
ATOM   7275  C  CG2   . VAL   A  1  987  ? -8.960  70.000  83.111  1.00 19.31 ? 985  VAL   A CG2   1 
ATOM   7276  N  N     . THR   A  1  988  ? -7.799  67.658  86.884  1.00 16.27 ? 986  THR   A N     1 
ATOM   7277  C  CA    . THR   A  1  988  ? -7.788  67.443  88.328  1.00 18.45 ? 986  THR   A CA    1 
ATOM   7278  C  C     . THR   A  1  988  ? -6.374  67.365  88.875  1.00 22.98 ? 986  THR   A C     1 
ATOM   7279  O  O     . THR   A  1  988  ? -6.162  67.639  90.060  1.00 23.41 ? 986  THR   A O     1 
ATOM   7280  C  CB    . THR   A  1  988  ? -8.579  66.200  88.733  1.00 19.99 ? 986  THR   A CB    1 
ATOM   7281  O  OG1   . THR   A  1  988  ? -7.996  65.039  88.137  1.00 20.65 ? 986  THR   A OG1   1 
ATOM   7282  C  CG2   . THR   A  1  988  ? -10.025 66.324  88.295  1.00 20.21 ? 986  THR   A CG2   1 
ATOM   7283  N  N     . SER   A  1  989  ? -5.406  67.019  88.042  1.00 17.76 ? 987  SER   A N     1 
ATOM   7284  C  CA    . SER   A  1  989  ? -4.032  66.995  88.511  1.00 21.57 ? 987  SER   A CA    1 
ATOM   7285  C  C     . SER   A  1  989  ? -3.442  68.394  88.602  1.00 23.51 ? 987  SER   A C     1 
ATOM   7286  O  O     . SER   A  1  989  ? -2.519  68.608  89.393  1.00 30.51 ? 987  SER   A O     1 
ATOM   7287  C  CB    . SER   A  1  989  ? -3.179  66.091  87.615  1.00 22.15 ? 987  SER   A CB    1 
ATOM   7288  O  OG    . SER   A  1  989  ? -2.944  66.677  86.355  1.00 28.88 ? 987  SER   A OG    1 
ATOM   7289  N  N     . ARG   A  1  990  ? -3.979  69.356  87.855  1.00 18.67 ? 988  ARG   A N     1 
ATOM   7290  C  CA    . ARG   A  1  990  ? -3.402  70.693  87.779  1.00 21.36 ? 988  ARG   A CA    1 
ATOM   7291  C  C     . ARG   A  1  990  ? -4.164  71.736  88.581  1.00 19.34 ? 988  ARG   A C     1 
ATOM   7292  O  O     . ARG   A  1  990  ? -3.565  72.729  89.002  1.00 20.76 ? 988  ARG   A O     1 
ATOM   7293  C  CB    . ARG   A  1  990  ? -3.314  71.151  86.320  1.00 21.84 ? 988  ARG   A CB    1 
ATOM   7294  C  CG    . ARG   A  1  990  ? -2.564  70.171  85.437  1.00 31.29 ? 988  ARG   A CG    1 
ATOM   7295  C  CD    . ARG   A  1  990  ? -1.067  70.351  85.530  1.00 31.84 ? 988  ARG   A CD    1 
ATOM   7296  N  NE    . ARG   A  1  990  ? -0.587  71.304  84.535  1.00 29.02 ? 988  ARG   A NE    1 
ATOM   7297  C  CZ    . ARG   A  1  990  ? 0.671   71.707  84.442  1.00 28.51 ? 988  ARG   A CZ    1 
ATOM   7298  N  NH1   . ARG   A  1  990  ? 1.587   71.319  85.315  1.00 32.00 ? 988  ARG   A NH1   1 
ATOM   7299  N  NH2   . ARG   A  1  990  ? 1.020   72.512  83.442  1.00 30.37 ? 988  ARG   A NH2   1 
ATOM   7300  N  N     . ILE   A  1  991  ? -5.464  71.552  88.793  1.00 17.77 ? 989  ILE   A N     1 
ATOM   7301  C  CA    . ILE   A  1  991  ? -6.220  72.501  89.592  1.00 16.89 ? 989  ILE   A CA    1 
ATOM   7302  C  C     . ILE   A  1  991  ? -5.773  72.395  91.038  1.00 19.30 ? 989  ILE   A C     1 
ATOM   7303  O  O     . ILE   A  1  991  ? -5.390  71.321  91.516  1.00 19.66 ? 989  ILE   A O     1 
ATOM   7304  C  CB    . ILE   A  1  991  ? -7.723  72.205  89.449  1.00 17.89 ? 989  ILE   A CB    1 
ATOM   7305  C  CG1   . ILE   A  1  991  ? -8.543  73.367  90.008  1.00 19.17 ? 989  ILE   A CG1   1 
ATOM   7306  C  CG2   . ILE   A  1  991  ? -8.065  70.896  90.122  1.00 18.33 ? 989  ILE   A CG2   1 
ATOM   7307  C  CD1   . ILE   A  1  991  ? -8.469  74.585  89.125  1.00 22.51 ? 989  ILE   A CD1   1 
ATOM   7308  N  N     . LYS   A  1  992  ? -5.802  73.528  91.739  1.00 17.47 ? 990  LYS   A N     1 
ATOM   7309  C  CA    . LYS   A  1  992  ? -5.448  73.600  93.154  1.00 18.79 ? 990  LYS   A CA    1 
ATOM   7310  C  C     . LYS   A  1  992  ? -6.654  74.123  93.916  1.00 17.39 ? 990  LYS   A C     1 
ATOM   7311  O  O     . LYS   A  1  992  ? -6.778  75.325  94.166  1.00 20.53 ? 990  LYS   A O     1 
ATOM   7312  C  CB    . LYS   A  1  992  ? -4.255  74.503  93.338  1.00 19.97 ? 990  LYS   A CB    1 
ATOM   7313  C  CG    . LYS   A  1  992  ? -2.981  74.032  92.645  1.00 22.98 ? 990  LYS   A CG    1 
ATOM   7314  C  CD    . LYS   A  1  992  ? -1.932  75.151  92.719  1.00 34.63 ? 990  LYS   A CD    1 
ATOM   7315  C  CE    . LYS   A  1  992  ? -0.658  74.815  91.959  1.00 42.93 ? 990  LYS   A CE    1 
ATOM   7316  N  NZ    . LYS   A  1  992  ? 0.235   76.010  91.813  1.00 50.10 ? 990  LYS   A NZ    1 
ATOM   7317  N  N     . ALA   A  1  993  ? -7.547  73.215  94.279  1.00 18.08 ? 991  ALA   A N     1 
ATOM   7318  C  CA    . ALA   A  1  993  ? -8.739  73.577  95.033  1.00 16.56 ? 991  ALA   A CA    1 
ATOM   7319  C  C     . ALA   A  1  993  ? -9.085  72.440  95.975  1.00 17.75 ? 991  ALA   A C     1 
ATOM   7320  O  O     . ALA   A  1  993  ? -8.758  71.278  95.732  1.00 19.06 ? 991  ALA   A O     1 
ATOM   7321  C  CB    . ALA   A  1  993  ? -9.914  73.890  94.104  1.00 17.26 ? 991  ALA   A CB    1 
ATOM   7322  N  N     . GLY   A  1  994  ? -9.790  72.779  97.049  1.00 15.35 ? 992  GLY   A N     1 
ATOM   7323  C  CA    . GLY   A  1  994  ? -10.021 71.793  98.081  1.00 16.66 ? 992  GLY   A CA    1 
ATOM   7324  C  C     . GLY   A  1  994  ? -11.190 70.872  97.810  1.00 14.10 ? 992  GLY   A C     1 
ATOM   7325  O  O     . GLY   A  1  994  ? -11.234 69.759  98.337  1.00 15.19 ? 992  GLY   A O     1 
ATOM   7326  N  N     . ASN   A  1  995  ? -12.147 71.303  96.996  1.00 14.35 ? 993  ASN   A N     1 
ATOM   7327  C  CA    . ASN   A  1  995  ? -13.336 70.504  96.729  1.00 15.79 ? 993  ASN   A CA    1 
ATOM   7328  C  C     . ASN   A  1  995  ? -13.570 70.493  95.236  1.00 15.62 ? 993  ASN   A C     1 
ATOM   7329  O  O     . ASN   A  1  995  ? -13.869 71.533  94.646  1.00 15.49 ? 993  ASN   A O     1 
ATOM   7330  C  CB    . ASN   A  1  995  ? -14.557 71.041  97.467  1.00 15.07 ? 993  ASN   A CB    1 
ATOM   7331  C  CG    . ASN   A  1  995  ? -14.569 70.608  98.902  1.00 15.07 ? 993  ASN   A CG    1 
ATOM   7332  O  OD1   . ASN   A  1  995  ? -13.921 71.223  99.746  1.00 16.74 ? 993  ASN   A OD1   1 
ATOM   7333  N  ND2   . ASN   A  1  995  ? -15.266 69.528  99.187  1.00 16.24 ? 993  ASN   A ND2   1 
ATOM   7334  N  N     . LEU   A  1  996  ? -13.392 69.328  94.636  1.00 14.20 ? 994  LEU   A N     1 
ATOM   7335  C  CA    . LEU   A  1  996  ? -13.558 69.169  93.205  1.00 15.07 ? 994  LEU   A CA    1 
ATOM   7336  C  C     . LEU   A  1  996  ? -14.829 68.389  92.950  1.00 13.58 ? 994  LEU   A C     1 
ATOM   7337  O  O     . LEU   A  1  996  ? -15.199 67.505  93.725  1.00 14.20 ? 994  LEU   A O     1 
ATOM   7338  C  CB    . LEU   A  1  996  ? -12.398 68.367  92.622  1.00 16.14 ? 994  LEU   A CB    1 
ATOM   7339  C  CG    . LEU   A  1  996  ? -11.005 68.796  93.071  1.00 16.53 ? 994  LEU   A CG    1 
ATOM   7340  C  CD1   . LEU   A  1  996  ? -9.970  67.933  92.362  1.00 21.17 ? 994  LEU   A CD1   1 
ATOM   7341  C  CD2   . LEU   A  1  996  ? -10.779 70.264  92.791  1.00 18.36 ? 994  LEU   A CD2   1 
ATOM   7342  N  N     . TYR   A  1  997  ? -15.470 68.698  91.826  1.00 14.50 ? 995  TYR   A N     1 
ATOM   7343  C  CA    . TYR   A  1  997  ? -16.738 68.072  91.480  1.00 14.28 ? 995  TYR   A CA    1 
ATOM   7344  C  C     . TYR   A  1  997  ? -16.710 67.791  89.994  1.00 14.79 ? 995  TYR   A C     1 
ATOM   7345  O  O     . TYR   A  1  997  ? -16.410 68.683  89.193  1.00 16.36 ? 995  TYR   A O     1 
ATOM   7346  C  CB    . TYR   A  1  997  ? -17.913 68.997  91.796  1.00 14.85 ? 995  TYR   A CB    1 
ATOM   7347  C  CG    . TYR   A  1  997  ? -17.935 69.439  93.233  1.00 14.81 ? 995  TYR   A CG    1 
ATOM   7348  C  CD1   . TYR   A  1  997  ? -17.254 70.577  93.629  1.00 16.46 ? 995  TYR   A CD1   1 
ATOM   7349  C  CD2   . TYR   A  1  997  ? -18.630 68.717  94.179  1.00 16.75 ? 995  TYR   A CD2   1 
ATOM   7350  C  CE1   . TYR   A  1  997  ? -17.264 70.989  94.946  1.00 18.57 ? 995  TYR   A CE1   1 
ATOM   7351  C  CE2   . TYR   A  1  997  ? -18.652 69.130  95.509  1.00 15.85 ? 995  TYR   A CE2   1 
ATOM   7352  C  CZ    . TYR   A  1  997  ? -17.956 70.267  95.864  1.00 18.42 ? 995  TYR   A CZ    1 
ATOM   7353  O  OH    . TYR   A  1  997  ? -17.965 70.708  97.181  1.00 20.96 ? 995  TYR   A OH    1 
ATOM   7354  N  N     . ILE   A  1  998  ? -17.006 66.554  89.633  1.00 14.02 ? 996  ILE   A N     1 
ATOM   7355  C  CA    A ILE   A  1  998  ? -16.949 66.121  88.243  0.52 14.20 ? 996  ILE   A CA    1 
ATOM   7356  C  CA    B ILE   A  1  998  ? -16.953 66.125  88.245  0.48 14.20 ? 996  ILE   A CA    1 
ATOM   7357  C  C     . ILE   A  1  998  ? -18.354 65.757  87.802  1.00 14.08 ? 996  ILE   A C     1 
ATOM   7358  O  O     . ILE   A  1  998  ? -18.975 64.858  88.373  1.00 14.18 ? 996  ILE   A O     1 
ATOM   7359  C  CB    A ILE   A  1  998  ? -15.992 64.936  88.052  0.52 14.72 ? 996  ILE   A CB    1 
ATOM   7360  C  CB    B ILE   A  1  998  ? -15.985 64.951  88.055  0.48 14.72 ? 996  ILE   A CB    1 
ATOM   7361  C  CG1   A ILE   A  1  998  ? -14.649 65.197  88.737  0.52 16.70 ? 996  ILE   A CG1   1 
ATOM   7362  C  CG1   B ILE   A  1  998  ? -14.560 65.424  88.335  0.48 16.12 ? 996  ILE   A CG1   1 
ATOM   7363  C  CG2   A ILE   A  1  998  ? -15.770 64.693  86.556  0.52 15.39 ? 996  ILE   A CG2   1 
ATOM   7364  C  CG2   B ILE   A  1  998  ? -16.123 64.380  86.641  0.48 15.94 ? 996  ILE   A CG2   1 
ATOM   7365  C  CD1   A ILE   A  1  998  ? -13.912 66.377  88.168  0.52 16.20 ? 996  ILE   A CD1   1 
ATOM   7366  C  CD1   B ILE   A  1  998  ? -13.559 64.323  88.376  0.48 17.47 ? 996  ILE   A CD1   1 
ATOM   7367  N  N     . ASN   A  1  999  ? -18.837 66.455  86.777  1.00 14.72 ? 997  ASN   A N     1 
ATOM   7368  C  CA    . ASN   A  1  999  ? -20.129 66.166  86.146  1.00 14.89 ? 997  ASN   A CA    1 
ATOM   7369  C  C     . ASN   A  1  999  ? -21.309 66.317  87.097  1.00 13.79 ? 997  ASN   A C     1 
ATOM   7370  O  O     . ASN   A  1  999  ? -22.272 65.552  87.047  1.00 15.95 ? 997  ASN   A O     1 
ATOM   7371  C  CB    . ASN   A  1  999  ? -20.111 64.806  85.457  1.00 14.78 ? 997  ASN   A CB    1 
ATOM   7372  C  CG    . ASN   A  1  999  ? -19.158 64.792  84.304  1.00 13.80 ? 997  ASN   A CG    1 
ATOM   7373  O  OD1   . ASN   A  1  999  ? -18.946 65.820  83.659  1.00 16.42 ? 997  ASN   A OD1   1 
ATOM   7374  N  ND2   . ASN   A  1  999  ? -18.544 63.657  84.058  1.00 15.79 ? 997  ASN   A ND2   1 
ATOM   7375  N  N     . ARG   A  1  1000 ? -21.223 67.317  87.965  1.00 14.47 ? 998  ARG   A N     1 
ATOM   7376  C  CA    . ARG   A  1  1000 ? -22.284 67.593  88.925  1.00 15.49 ? 998  ARG   A CA    1 
ATOM   7377  C  C     . ARG   A  1  1000 ? -22.139 69.045  89.349  1.00 15.18 ? 998  ARG   A C     1 
ATOM   7378  O  O     . ARG   A  1  1000 ? -21.246 69.757  88.890  1.00 16.78 ? 998  ARG   A O     1 
ATOM   7379  C  CB    . ARG   A  1  1000 ? -22.219 66.625  90.104  1.00 14.84 ? 998  ARG   A CB    1 
ATOM   7380  C  CG    . ARG   A  1  1000 ? -20.824 66.555  90.734  1.00 15.54 ? 998  ARG   A CG    1 
ATOM   7381  C  CD    . ARG   A  1  1000 ? -20.899 66.191  92.203  1.00 16.42 ? 998  ARG   A CD    1 
ATOM   7382  N  NE    . ARG   A  1  1000 ? -21.562 67.242  92.959  1.00 15.22 ? 998  ARG   A NE    1 
ATOM   7383  C  CZ    . ARG   A  1  1000 ? -21.892 67.138  94.233  1.00 16.72 ? 998  ARG   A CZ    1 
ATOM   7384  N  NH1   . ARG   A  1  1000 ? -21.611 66.046  94.930  1.00 17.86 ? 998  ARG   A NH1   1 
ATOM   7385  N  NH2   . ARG   A  1  1000 ? -22.491 68.163  94.828  1.00 17.23 ? 998  ARG   A NH2   1 
ATOM   7386  N  N     . ASN   A  1  1001 ? -23.051 69.499  90.203  1.00 15.17 ? 999  ASN   A N     1 
ATOM   7387  C  CA    . ASN   A  1  1001 ? -22.899 70.856  90.694  1.00 15.25 ? 999  ASN   A CA    1 
ATOM   7388  C  C     . ASN   A  1  1001 ? -21.718 70.922  91.666  1.00 16.53 ? 999  ASN   A C     1 
ATOM   7389  O  O     . ASN   A  1  1001 ? -21.147 69.904  92.058  1.00 16.55 ? 999  ASN   A O     1 
ATOM   7390  C  CB    . ASN   A  1  1001 ? -24.211 71.358  91.304  1.00 18.27 ? 999  ASN   A CB    1 
ATOM   7391  C  CG    . ASN   A  1  1001 ? -24.575 70.658  92.589  1.00 19.33 ? 999  ASN   A CG    1 
ATOM   7392  O  OD1   . ASN   A  1  1001 ? -23.735 70.446  93.445  1.00 18.88 ? 999  ASN   A OD1   1 
ATOM   7393  N  ND2   . ASN   A  1  1001 ? -25.857 70.336  92.745  1.00 27.05 ? 999  ASN   A ND2   1 
ATOM   7394  N  N     A ILE   A  1  1002 ? -21.341 72.143  92.038  0.54 14.88 ? 1000 ILE   A N     1 
ATOM   7395  N  N     B ILE   A  1  1002 ? -21.378 72.132  92.082  0.46 14.86 ? 1000 ILE   A N     1 
ATOM   7396  C  CA    A ILE   A  1  1002 ? -20.126 72.367  92.818  0.54 15.09 ? 1000 ILE   A CA    1 
ATOM   7397  C  CA    B ILE   A  1  1002 ? -20.241 72.317  92.967  0.46 15.05 ? 1000 ILE   A CA    1 
ATOM   7398  C  C     A ILE   A  1  1002 ? -20.431 72.865  94.223  0.54 16.36 ? 1000 ILE   A C     1 
ATOM   7399  C  C     B ILE   A  1  1002 ? -20.674 72.738  94.366  0.46 15.87 ? 1000 ILE   A C     1 
ATOM   7400  O  O     A ILE   A  1  1002 ? -19.584 73.496  94.837  0.54 16.14 ? 1000 ILE   A O     1 
ATOM   7401  O  O     B ILE   A  1  1002 ? -19.859 73.232  95.128  0.46 18.23 ? 1000 ILE   A O     1 
ATOM   7402  C  CB    A ILE   A  1  1002 ? -19.129 73.289  92.099  0.54 15.25 ? 1000 ILE   A CB    1 
ATOM   7403  C  CB    B ILE   A  1  1002 ? -19.191 73.266  92.369  0.46 14.54 ? 1000 ILE   A CB    1 
ATOM   7404  C  CG1   A ILE   A  1  1002 ? -19.654 74.728  92.028  0.54 16.51 ? 1000 ILE   A CG1   1 
ATOM   7405  C  CG1   B ILE   A  1  1002 ? -19.749 74.682  92.214  0.46 16.54 ? 1000 ILE   A CG1   1 
ATOM   7406  C  CG2   A ILE   A  1  1002 ? -18.853 72.766  90.711  0.54 15.25 ? 1000 ILE   A CG2   1 
ATOM   7407  C  CG2   B ILE   A  1  1002 ? -18.717 72.736  91.023  0.46 14.83 ? 1000 ILE   A CG2   1 
ATOM   7408  C  CD1   A ILE   A  1  1002 ? -18.586 75.740  91.683  0.54 17.28 ? 1000 ILE   A CD1   1 
ATOM   7409  C  CD1   B ILE   A  1  1002 ? -18.721 75.675  91.731  0.46 17.16 ? 1000 ILE   A CD1   1 
ATOM   7410  N  N     A ILE   A  1  1003 ? -21.626 72.590  94.737  0.54 16.27 ? 1001 ILE   A N     1 
ATOM   7411  N  N     B ILE   A  1  1003 ? -21.942 72.535  94.721  0.46 16.31 ? 1001 ILE   A N     1 
ATOM   7412  C  CA    A ILE   A  1  1003 ? -22.035 73.109  96.038  0.54 18.34 ? 1001 ILE   A CA    1 
ATOM   7413  C  CA    B ILE   A  1  1003 ? -22.478 73.063  95.969  0.46 17.80 ? 1001 ILE   A CA    1 
ATOM   7414  C  C     A ILE   A  1  1003 ? -22.105 72.016  97.095  0.54 21.52 ? 1001 ILE   A C     1 
ATOM   7415  C  C     B ILE   A  1  1003 ? -23.099 71.940  96.791  0.46 17.36 ? 1001 ILE   A C     1 
ATOM   7416  O  O     A ILE   A  1  1003 ? -22.607 72.257  98.202  0.54 20.65 ? 1001 ILE   A O     1 
ATOM   7417  O  O     B ILE   A  1  1003 ? -23.242 70.806  96.338  0.46 19.34 ? 1001 ILE   A O     1 
ATOM   7418  C  CB    A ILE   A  1  1003 ? -23.333 73.937  95.961  0.54 18.13 ? 1001 ILE   A CB    1 
ATOM   7419  C  CB    B ILE   A  1  1003 ? -23.471 74.226  95.759  0.46 18.55 ? 1001 ILE   A CB    1 
ATOM   7420  C  CG1   A ILE   A  1  1003 ? -24.501 73.115  95.411  0.54 18.79 ? 1001 ILE   A CG1   1 
ATOM   7421  C  CG1   B ILE   A  1  1003 ? -24.704 73.755  94.996  0.46 18.28 ? 1001 ILE   A CG1   1 
ATOM   7422  C  CG2   A ILE   A  1  1003 ? -23.124 75.199  95.123  0.54 17.18 ? 1001 ILE   A CG2   1 
ATOM   7423  C  CG2   B ILE   A  1  1003 ? -22.797 75.382  95.032  0.46 17.45 ? 1001 ILE   A CG2   1 
ATOM   7424  C  CD1   A ILE   A  1  1003 ? -25.826 73.870  95.433  0.54 24.23 ? 1001 ILE   A CD1   1 
ATOM   7425  C  CD1   B ILE   A  1  1003 ? -25.885 74.712  95.115  0.46 22.59 ? 1001 ILE   A CD1   1 
ATOM   7426  N  N     A GLY   A  1  1004 ? -21.580 70.827  96.798  0.54 18.51 ? 1002 GLY   A N     1 
ATOM   7427  N  N     B GLY   A  1  1004 ? -23.447 72.275  98.029  0.46 18.59 ? 1002 GLY   A N     1 
ATOM   7428  C  CA    A GLY   A  1  1004 ? -21.680 69.709  97.720  0.54 17.99 ? 1002 GLY   A CA    1 
ATOM   7429  C  CA    B GLY   A  1  1004 ? -24.053 71.304  98.923  0.46 20.45 ? 1002 GLY   A CA    1 
ATOM   7430  C  C     A GLY   A  1  1004 ? -20.752 69.865  98.908  0.54 17.72 ? 1002 GLY   A C     1 
ATOM   7431  C  C     B GLY   A  1  1004 ? -23.140 70.177  99.364  0.46 18.52 ? 1002 GLY   A C     1 
ATOM   7432  O  O     A GLY   A  1  1004 ? -19.547 70.080  98.755  0.54 18.64 ? 1002 GLY   A O     1 
ATOM   7433  O  O     B GLY   A  1  1004 ? -23.575 69.017  99.417  0.46 20.71 ? 1002 GLY   A O     1 
ATOM   7434  N  N     A ALA   A  1  1005 ? -21.313 69.757  100.100 0.54 16.93 ? 1003 ALA   A N     1 
ATOM   7435  N  N     B ALA   A  1  1005 ? -21.888 70.487  99.698  0.46 19.51 ? 1003 ALA   A N     1 
ATOM   7436  C  CA    A ALA   A  1  1005 ? -20.507 69.789  101.313 0.54 17.06 ? 1003 ALA   A CA    1 
ATOM   7437  C  CA    B ALA   A  1  1005 ? -20.971 69.464  100.184 0.46 18.92 ? 1003 ALA   A CA    1 
ATOM   7438  C  C     A ALA   A  1  1005 ? -21.025 68.756  102.293 0.54 20.35 ? 1003 ALA   A C     1 
ATOM   7439  C  C     B ALA   A  1  1005 ? -21.549 68.773  101.413 0.46 18.91 ? 1003 ALA   A C     1 
ATOM   7440  O  O     A ALA   A  1  1005 ? -21.035 68.975  103.507 0.54 18.20 ? 1003 ALA   A O     1 
ATOM   7441  O  O     B ALA   A  1  1005 ? -22.152 69.414  102.276 0.46 21.19 ? 1003 ALA   A O     1 
ATOM   7442  C  CB    A ALA   A  1  1005 ? -20.490 71.185  101.930 0.54 19.15 ? 1003 ALA   A CB    1 
ATOM   7443  C  CB    B ALA   A  1  1005 ? -19.633 70.101  100.555 0.46 18.80 ? 1003 ALA   A CB    1 
ATOM   7444  N  N     A VAL   A  1  1006 ? -21.458 67.609  101.765 0.54 18.79 ? 1004 VAL   A N     1 
ATOM   7445  N  N     B VAL   A  1  1006 ? -21.359 67.452  101.490 0.46 18.74 ? 1004 VAL   A N     1 
ATOM   7446  C  CA    A VAL   A  1  1006 ? -22.034 66.546  102.575 0.54 17.31 ? 1004 VAL   A CA    1 
ATOM   7447  C  CA    B VAL   A  1  1006 ? -21.958 66.624  102.533 0.46 17.31 ? 1004 VAL   A CA    1 
ATOM   7448  C  C     A VAL   A  1  1006 ? -21.004 66.098  103.592 0.54 17.47 ? 1004 VAL   A C     1 
ATOM   7449  C  C     B VAL   A  1  1006 ? -20.905 66.298  103.583 0.46 17.63 ? 1004 VAL   A C     1 
ATOM   7450  O  O     A VAL   A  1  1006 ? -19.964 65.534  103.241 0.54 16.37 ? 1004 VAL   A O     1 
ATOM   7451  O  O     B VAL   A  1  1006 ? -19.758 65.985  103.252 0.46 17.83 ? 1004 VAL   A O     1 
ATOM   7452  C  CB    A VAL   A  1  1006 ? -22.520 65.364  101.725 0.54 17.69 ? 1004 VAL   A CB    1 
ATOM   7453  C  CB    B VAL   A  1  1006 ? -22.567 65.344  101.926 0.46 17.53 ? 1004 VAL   A CB    1 
ATOM   7454  C  CG1   A VAL   A  1  1006 ? -23.016 64.258  102.634 0.54 19.24 ? 1004 VAL   A CG1   1 
ATOM   7455  C  CG1   B VAL   A  1  1006 ? -23.058 64.407  103.015 0.46 18.99 ? 1004 VAL   A CG1   1 
ATOM   7456  C  CG2   A VAL   A  1  1006 ? -23.622 65.822  100.765 0.54 19.99 ? 1004 VAL   A CG2   1 
ATOM   7457  C  CG2   B VAL   A  1  1006 ? -23.706 65.701  100.966 0.46 20.07 ? 1004 VAL   A CG2   1 
ATOM   7458  N  N     . VAL   A  1  1007 ? -21.294 66.373  104.858 1.00 17.35 ? 1005 VAL   A N     1 
ATOM   7459  C  CA    . VAL   A  1  1007 ? -20.356 66.111  105.931 1.00 17.49 ? 1005 VAL   A CA    1 
ATOM   7460  C  C     . VAL   A  1  1007 ? -19.871 64.676  105.861 1.00 16.84 ? 1005 VAL   A C     1 
ATOM   7461  O  O     . VAL   A  1  1007 ? -20.666 63.740  105.706 1.00 18.40 ? 1005 VAL   A O     1 
ATOM   7462  C  CB    . VAL   A  1  1007 ? -21.055 66.407  107.264 1.00 17.42 ? 1005 VAL   A CB    1 
ATOM   7463  C  CG1   . VAL   A  1  1007 ? -20.174 65.996  108.403 1.00 17.62 ? 1005 VAL   A CG1   1 
ATOM   7464  C  CG2   . VAL   A  1  1007 ? -21.400 67.879  107.340 1.00 19.02 ? 1005 VAL   A CG2   1 
ATOM   7465  N  N     . GLY   A  1  1008 ? -18.550 64.492  105.976 1.00 16.78 ? 1006 GLY   A N     1 
ATOM   7466  C  CA    . GLY   A  1  1008 ? -17.965 63.165  105.960 1.00 17.52 ? 1006 GLY   A CA    1 
ATOM   7467  C  C     . GLY   A  1  1008 ? -18.002 62.484  104.613 1.00 17.70 ? 1006 GLY   A C     1 
ATOM   7468  O  O     . GLY   A  1  1008 ? -17.587 61.328  104.503 1.00 19.45 ? 1006 GLY   A O     1 
ATOM   7469  N  N     . VAL   A  1  1009 ? -18.497 63.159  103.587 1.00 17.21 ? 1007 VAL   A N     1 
ATOM   7470  C  CA    . VAL   A  1  1009 ? -18.585 62.610  102.243 1.00 18.21 ? 1007 VAL   A CA    1 
ATOM   7471  C  C     . VAL   A  1  1009 ? -17.851 63.494  101.258 1.00 16.24 ? 1007 VAL   A C     1 
ATOM   7472  O  O     . VAL   A  1  1009 ? -17.009 63.022  100.493 1.00 17.77 ? 1007 VAL   A O     1 
ATOM   7473  C  CB    . VAL   A  1  1009 ? -20.049 62.397  101.813 1.00 16.44 ? 1007 VAL   A CB    1 
ATOM   7474  C  CG1   . VAL   A  1  1009 ? -20.089 61.800  100.428 1.00 18.29 ? 1007 VAL   A CG1   1 
ATOM   7475  C  CG2   . VAL   A  1  1009 ? -20.745 61.458  102.769 1.00 18.14 ? 1007 VAL   A CG2   1 
ATOM   7476  N  N     . GLN   A  1  1010 ? -18.128 64.796  101.295 1.00 16.12 ? 1008 GLN   A N     1 
ATOM   7477  C  CA    . GLN   A  1  1010 ? -17.254 65.811  100.720 1.00 16.37 ? 1008 GLN   A CA    1 
ATOM   7478  C  C     . GLN   A  1  1010 ? -16.812 66.702  101.872 1.00 16.23 ? 1008 GLN   A C     1 
ATOM   7479  O  O     . GLN   A  1  1010 ? -17.358 67.798  102.054 1.00 19.27 ? 1008 GLN   A O     1 
ATOM   7480  C  CB    . GLN   A  1  1010 ? -17.930 66.641  99.631  1.00 18.76 ? 1008 GLN   A CB    1 
ATOM   7481  C  CG    . GLN   A  1  1010 ? -18.481 65.812  98.474  1.00 17.90 ? 1008 GLN   A CG    1 
ATOM   7482  C  CD    . GLN   A  1  1010 ? -19.969 65.583  98.569  1.00 18.42 ? 1008 GLN   A CD    1 
ATOM   7483  O  OE1   . GLN   A  1  1010 ? -20.712 66.433  99.073  1.00 18.42 ? 1008 GLN   A OE1   1 
ATOM   7484  N  NE2   . GLN   A  1  1010 ? -20.424 64.433  98.078  1.00 18.32 ? 1008 GLN   A NE2   1 
ATOM   7485  N  N     . PRO   A  1  1011 ? -15.856 66.255  102.682 1.00 16.52 ? 1009 PRO   A N     1 
ATOM   7486  C  CA    . PRO   A  1  1011 ? -15.234 67.160  103.660 1.00 18.05 ? 1009 PRO   A CA    1 
ATOM   7487  C  C     . PRO   A  1  1011 ? -14.871 68.448  102.948 1.00 16.70 ? 1009 PRO   A C     1 
ATOM   7488  O  O     . PRO   A  1  1011 ? -14.343 68.436  101.834 1.00 16.00 ? 1009 PRO   A O     1 
ATOM   7489  C  CB    . PRO   A  1  1011 ? -13.982 66.395  104.089 1.00 18.47 ? 1009 PRO   A CB    1 
ATOM   7490  C  CG    . PRO   A  1  1011 ? -14.358 64.955  103.924 1.00 19.75 ? 1009 PRO   A CG    1 
ATOM   7491  C  CD    . PRO   A  1  1011 ? -15.233 64.917  102.687 1.00 16.55 ? 1009 PRO   A CD    1 
ATOM   7492  N  N     . PHE   A  1  1012 ? -15.228 69.568  103.552 1.00 16.81 ? 1010 PHE   A N     1 
ATOM   7493  C  CA    . PHE   A  1  1012 ? -15.311 70.817  102.823 1.00 15.69 ? 1010 PHE   A CA    1 
ATOM   7494  C  C     . PHE   A  1  1012 ? -14.284 71.803  103.331 1.00 16.72 ? 1010 PHE   A C     1 
ATOM   7495  O  O     . PHE   A  1  1012 ? -14.175 72.028  104.539 1.00 17.81 ? 1010 PHE   A O     1 
ATOM   7496  C  CB    . PHE   A  1  1012 ? -16.696 71.451  102.945 1.00 16.91 ? 1010 PHE   A CB    1 
ATOM   7497  C  CG    . PHE   A  1  1012 ? -16.852 72.641  102.069 1.00 15.94 ? 1010 PHE   A CG    1 
ATOM   7498  C  CD1   . PHE   A  1  1012 ? -17.131 72.478  100.720 1.00 17.70 ? 1010 PHE   A CD1   1 
ATOM   7499  C  CD2   . PHE   A  1  1012 ? -16.662 73.929  102.567 1.00 18.68 ? 1010 PHE   A CD2   1 
ATOM   7500  C  CE1   . PHE   A  1  1012 ? -17.240 73.574  99.886  1.00 17.40 ? 1010 PHE   A CE1   1 
ATOM   7501  C  CE2   . PHE   A  1  1012 ? -16.782 75.039  101.728 1.00 20.21 ? 1010 PHE   A CE2   1 
ATOM   7502  C  CZ    . PHE   A  1  1012 ? -17.072 74.858  100.397 1.00 18.39 ? 1010 PHE   A CZ    1 
ATOM   7503  N  N     . GLY   A  1  1013 ? -13.565 72.415  102.410 1.00 15.97 ? 1011 GLY   A N     1 
ATOM   7504  C  CA    . GLY   A  1  1013 ? -12.669 73.482  102.776 1.00 18.68 ? 1011 GLY   A CA    1 
ATOM   7505  C  C     . GLY   A  1  1013 ? -11.584 73.615  101.749 1.00 16.49 ? 1011 GLY   A C     1 
ATOM   7506  O  O     . GLY   A  1  1013 ? -11.181 72.614  101.161 1.00 17.61 ? 1011 GLY   A O     1 
ATOM   7507  N  N     . GLY   A  1  1014 ? -11.100 74.828  101.544 1.00 16.85 ? 1012 GLY   A N     1 
ATOM   7508  C  CA    . GLY   A  1  1014 ? -10.134 75.062  100.508 1.00 19.21 ? 1012 GLY   A CA    1 
ATOM   7509  C  C     . GLY   A  1  1014 ? -8.793  75.545  100.995 1.00 18.98 ? 1012 GLY   A C     1 
ATOM   7510  O  O     . GLY   A  1  1014 ? -8.475  75.486  102.188 1.00 19.26 ? 1012 GLY   A O     1 
ATOM   7511  N  N     . ARG   A  1  1015 ? -8.022  76.059  100.053 1.00 16.57 ? 1013 ARG   A N     1 
ATOM   7512  C  CA    . ARG   A  1  1015 ? -6.632  76.419  100.281 1.00 18.15 ? 1013 ARG   A CA    1 
ATOM   7513  C  C     . ARG   A  1  1015 ? -6.406  77.828  99.763  1.00 17.05 ? 1013 ARG   A C     1 
ATOM   7514  O  O     . ARG   A  1  1015 ? -7.305  78.458  99.205  1.00 17.77 ? 1013 ARG   A O     1 
ATOM   7515  C  CB    . ARG   A  1  1015 ? -5.711  75.446  99.545  1.00 19.12 ? 1013 ARG   A CB    1 
ATOM   7516  C  CG    . ARG   A  1  1015 ? -5.961  75.483  98.030  1.00 18.32 ? 1013 ARG   A CG    1 
ATOM   7517  C  CD    . ARG   A  1  1015 ? -4.850  74.816  97.215  1.00 21.99 ? 1013 ARG   A CD    1 
ATOM   7518  N  NE    . ARG   A  1  1015 ? -3.541  74.971  97.827  1.00 25.99 ? 1013 ARG   A NE    1 
ATOM   7519  C  CZ    . ARG   A  1  1015 ? -2.809  76.073  97.753  1.00 28.69 ? 1013 ARG   A CZ    1 
ATOM   7520  N  NH1   . ARG   A  1  1015 ? -3.195  77.107  97.026  1.00 26.30 ? 1013 ARG   A NH1   1 
ATOM   7521  N  NH2   . ARG   A  1  1015 ? -1.669  76.144  98.437  1.00 24.76 ? 1013 ARG   A NH2   1 
ATOM   7522  N  N     . GLY   A  1  1016 ? -5.185  78.323  99.943  1.00 18.61 ? 1014 GLY   A N     1 
ATOM   7523  C  CA    . GLY   A  1  1016 ? -4.898  79.659  99.467  1.00 18.67 ? 1014 GLY   A CA    1 
ATOM   7524  C  C     . GLY   A  1  1016 ? -5.751  80.662  100.213 1.00 18.41 ? 1014 GLY   A C     1 
ATOM   7525  O  O     . GLY   A  1  1016 ? -5.953  80.566  101.430 1.00 19.38 ? 1014 GLY   A O     1 
ATOM   7526  N  N     . LEU   A  1  1017 ? -6.313  81.608  99.463  1.00 18.38 ? 1015 LEU   A N     1 
ATOM   7527  C  CA    . LEU   A  1  1017 ? -7.187  82.619  100.044 1.00 18.73 ? 1015 LEU   A CA    1 
ATOM   7528  C  C     . LEU   A  1  1017 ? -8.494  82.034  100.542 1.00 18.37 ? 1015 LEU   A C     1 
ATOM   7529  O  O     . LEU   A  1  1017 ? -9.292  82.766  101.134 1.00 19.35 ? 1015 LEU   A O     1 
ATOM   7530  C  CB    . LEU   A  1  1017 ? -7.511  83.680  98.994  1.00 19.55 ? 1015 LEU   A CB    1 
ATOM   7531  C  CG    . LEU   A  1  1017 ? -6.320  84.469  98.464  1.00 19.96 ? 1015 LEU   A CG    1 
ATOM   7532  C  CD1   . LEU   A  1  1017 ? -6.786  85.379  97.342  1.00 21.24 ? 1015 LEU   A CD1   1 
ATOM   7533  C  CD2   . LEU   A  1  1017 ? -5.676  85.273  99.592  1.00 21.45 ? 1015 LEU   A CD2   1 
ATOM   7534  N  N     . SER   A  1  1018 ? -8.739  80.747  100.305 1.00 16.48 ? 1016 SER   A N     1 
ATOM   7535  C  CA    . SER   A  1  1018 ? -9.995  80.113  100.680 1.00 18.84 ? 1016 SER   A CA    1 
ATOM   7536  C  C     . SER   A  1  1018 ? -9.946  79.393  102.018 1.00 16.63 ? 1016 SER   A C     1 
ATOM   7537  O  O     . SER   A  1  1018 ? -10.995 78.962  102.502 1.00 17.90 ? 1016 SER   A O     1 
ATOM   7538  C  CB    . SER   A  1  1018 ? -10.425 79.108  99.608  1.00 17.97 ? 1016 SER   A CB    1 
ATOM   7539  O  OG    . SER   A  1  1018 ? -10.617 79.778  98.376  1.00 17.37 ? 1016 SER   A OG    1 
ATOM   7540  N  N     . GLY   A  1  1019 ? -8.773  79.218  102.612 1.00 17.14 ? 1017 GLY   A N     1 
ATOM   7541  C  CA    . GLY   A  1  1019 ? -8.782  78.509  103.869 1.00 18.49 ? 1017 GLY   A CA    1 
ATOM   7542  C  C     . GLY   A  1  1019 ? -7.422  78.161  104.396 1.00 17.53 ? 1017 GLY   A C     1 
ATOM   7543  O  O     . GLY   A  1  1019 ? -6.464  78.069  103.635 1.00 19.26 ? 1017 GLY   A O     1 
ATOM   7544  N  N     . THR   A  1  1020 ? -7.342  77.975  105.702 1.00 18.73 ? 1018 THR   A N     1 
ATOM   7545  C  CA    . THR   A  1  1020 ? -6.175  77.385  106.328 1.00 18.70 ? 1018 THR   A CA    1 
ATOM   7546  C  C     . THR   A  1  1020 ? -6.318  75.886  106.454 1.00 18.25 ? 1018 THR   A C     1 
ATOM   7547  O  O     . THR   A  1  1020 ? -5.309  75.190  106.617 1.00 18.80 ? 1018 THR   A O     1 
ATOM   7548  C  CB    . THR   A  1  1020 ? -6.026  77.931  107.753 1.00 19.01 ? 1018 THR   A CB    1 
ATOM   7549  O  OG1   . THR   A  1  1020 ? -7.221  77.653  108.515 1.00 19.10 ? 1018 THR   A OG1   1 
ATOM   7550  C  CG2   . THR   A  1  1020 ? -5.797  79.419  107.725 1.00 22.38 ? 1018 THR   A CG2   1 
ATOM   7551  N  N     . GLY   A  1  1021 ? -7.546  75.390  106.459 1.00 19.47 ? 1019 GLY   A N     1 
ATOM   7552  C  CA    . GLY   A  1  1021 ? -7.807  74.047  106.891 1.00 19.82 ? 1019 GLY   A CA    1 
ATOM   7553  C  C     . GLY   A  1  1021 ? -7.559  73.924  108.379 1.00 19.98 ? 1019 GLY   A C     1 
ATOM   7554  O  O     . GLY   A  1  1021 ? -7.262  74.906  109.063 1.00 19.82 ? 1019 GLY   A O     1 
ATOM   7555  N  N     . PRO   A  1  1022 ? -7.763  72.731  108.921 1.00 18.92 ? 1020 PRO   A N     1 
ATOM   7556  C  CA    . PRO   A  1  1022 ? -8.260  71.523  108.250 1.00 19.13 ? 1020 PRO   A CA    1 
ATOM   7557  C  C     . PRO   A  1  1022 ? -9.718  71.660  107.841 1.00 19.04 ? 1020 PRO   A C     1 
ATOM   7558  O  O     . PRO   A  1  1022 ? -10.435 72.565  108.278 1.00 21.23 ? 1020 PRO   A O     1 
ATOM   7559  C  CB    . PRO   A  1  1022 ? -8.108  70.449  109.330 1.00 19.94 ? 1020 PRO   A CB    1 
ATOM   7560  C  CG    . PRO   A  1  1022 ? -8.290  71.203  110.618 1.00 22.55 ? 1020 PRO   A CG    1 
ATOM   7561  C  CD    . PRO   A  1  1022 ? -7.613  72.527  110.374 1.00 18.72 ? 1020 PRO   A CD    1 
ATOM   7562  N  N     . LYS   A  1  1023 ? -10.174 70.742  106.998 1.00 18.14 ? 1021 LYS   A N     1 
ATOM   7563  C  CA    . LYS   A  1  1023 ? -11.536 70.806  106.484 1.00 16.87 ? 1021 LYS   A CA    1 
ATOM   7564  C  C     . LYS   A  1  1023 ? -12.562 70.521  107.564 1.00 18.18 ? 1021 LYS   A C     1 
ATOM   7565  O  O     . LYS   A  1  1023 ? -12.472 69.518  108.275 1.00 18.62 ? 1021 LYS   A O     1 
ATOM   7566  C  CB    . LYS   A  1  1023 ? -11.733 69.751  105.406 1.00 16.63 ? 1021 LYS   A CB    1 
ATOM   7567  C  CG    . LYS   A  1  1023 ? -11.077 70.042  104.087 1.00 16.81 ? 1021 LYS   A CG    1 
ATOM   7568  C  CD    . LYS   A  1  1023 ? -11.283 68.842  103.201 1.00 16.94 ? 1021 LYS   A CD    1 
ATOM   7569  C  CE    . LYS   A  1  1023 ? -10.872 69.088  101.756 1.00 17.77 ? 1021 LYS   A CE    1 
ATOM   7570  N  NZ    . LYS   A  1  1023 ? -11.885 69.873  101.021 1.00 17.35 ? 1021 LYS   A NZ    1 
ATOM   7571  N  N     . ALA   A  1  1024 ? -13.579 71.376  107.629 1.00 19.03 ? 1022 ALA   A N     1 
ATOM   7572  C  CA    . ALA   A  1  1024 ? -14.794 71.036  108.343 1.00 20.23 ? 1022 ALA   A CA    1 
ATOM   7573  C  C     . ALA   A  1  1024 ? -15.423 69.794  107.724 1.00 18.13 ? 1022 ALA   A C     1 
ATOM   7574  O  O     . ALA   A  1  1024 ? -15.372 69.578  106.504 1.00 18.31 ? 1022 ALA   A O     1 
ATOM   7575  C  CB    . ALA   A  1  1024 ? -15.775 72.208  108.271 1.00 19.46 ? 1022 ALA   A CB    1 
ATOM   7576  N  N     . GLY   A  1  1025 ? -16.022 68.967  108.577 1.00 18.89 ? 1023 GLY   A N     1 
ATOM   7577  C  CA    . GLY   A  1  1025 ? -16.678 67.775  108.090 1.00 19.52 ? 1023 GLY   A CA    1 
ATOM   7578  C  C     . GLY   A  1  1025 ? -15.711 66.719  107.627 1.00 18.97 ? 1023 GLY   A C     1 
ATOM   7579  O  O     . GLY   A  1  1025 ? -16.099 65.804  106.884 1.00 17.86 ? 1023 GLY   A O     1 
ATOM   7580  N  N     . GLY   A  1  1026 ? -14.450 66.837  108.050 1.00 16.73 ? 1024 GLY   A N     1 
ATOM   7581  C  CA    . GLY   A  1  1026 ? -13.417 65.899  107.698 1.00 16.66 ? 1024 GLY   A CA    1 
ATOM   7582  C  C     . GLY   A  1  1026 ? -12.678 65.440  108.936 1.00 17.33 ? 1024 GLY   A C     1 
ATOM   7583  O  O     . GLY   A  1  1026 ? -12.876 65.962  110.034 1.00 17.82 ? 1024 GLY   A O     1 
ATOM   7584  N  N     . PRO   A  1  1027 ? -11.788 64.458  108.763 1.00 16.57 ? 1025 PRO   A N     1 
ATOM   7585  C  CA    . PRO   A  1  1027 ? -11.244 63.729  109.909 1.00 18.02 ? 1025 PRO   A CA    1 
ATOM   7586  C  C     . PRO   A  1  1027 ? -10.089 64.424  110.600 1.00 14.70 ? 1025 PRO   A C     1 
ATOM   7587  O  O     . PRO   A  1  1027 ? -9.672  63.959  111.661 1.00 17.58 ? 1025 PRO   A O     1 
ATOM   7588  C  CB    . PRO   A  1  1027 ? -10.786 62.407  109.278 1.00 19.45 ? 1025 PRO   A CB    1 
ATOM   7589  C  CG    . PRO   A  1  1027 ? -10.463 62.773  107.861 1.00 18.99 ? 1025 PRO   A CG    1 
ATOM   7590  C  CD    . PRO   A  1  1027 ? -11.500 63.789  107.482 1.00 16.31 ? 1025 PRO   A CD    1 
ATOM   7591  N  N     . LEU   A  1  1028 ? -9.548  65.494  110.025 1.00 16.57 ? 1026 LEU   A N     1 
ATOM   7592  C  CA    . LEU   A  1  1028 ? -8.460  66.225  110.668 1.00 17.21 ? 1026 LEU   A CA    1 
ATOM   7593  C  C     . LEU   A  1  1028 ? -8.951  67.367  111.531 1.00 17.25 ? 1026 LEU   A C     1 
ATOM   7594  O  O     . LEU   A  1  1028 ? -8.152  67.973  112.251 1.00 19.00 ? 1026 LEU   A O     1 
ATOM   7595  C  CB    . LEU   A  1  1028 ? -7.487  66.782  109.626 1.00 17.51 ? 1026 LEU   A CB    1 
ATOM   7596  C  CG    . LEU   A  1  1028 ? -6.637  65.718  108.929 1.00 20.90 ? 1026 LEU   A CG    1 
ATOM   7597  C  CD1   . LEU   A  1  1028 ? -5.866  66.333  107.789 1.00 21.76 ? 1026 LEU   A CD1   1 
ATOM   7598  C  CD2   . LEU   A  1  1028 ? -5.702  65.104  109.943 1.00 28.49 ? 1026 LEU   A CD2   1 
ATOM   7599  N  N     . TYR   A  1  1029 ? -10.254 67.628  111.521 1.00 17.18 ? 1027 TYR   A N     1 
ATOM   7600  C  CA    . TYR   A  1  1029 ? -10.779 68.846  112.120 1.00 17.93 ? 1027 TYR   A CA    1 
ATOM   7601  C  C     . TYR   A  1  1029 ? -10.628 68.839  113.629 1.00 17.47 ? 1027 TYR   A C     1 
ATOM   7602  O  O     . TYR   A  1  1029 ? -10.117 69.800  114.214 1.00 18.95 ? 1027 TYR   A O     1 
ATOM   7603  C  CB    . TYR   A  1  1029 ? -12.240 68.931  111.743 1.00 18.73 ? 1027 TYR   A CB    1 
ATOM   7604  C  CG    . TYR   A  1  1029 ? -12.888 70.271  111.842 1.00 17.93 ? 1027 TYR   A CG    1 
ATOM   7605  C  CD1   . TYR   A  1  1029 ? -12.499 71.317  111.020 1.00 18.02 ? 1027 TYR   A CD1   1 
ATOM   7606  C  CD2   . TYR   A  1  1029 ? -13.958 70.467  112.703 1.00 18.50 ? 1027 TYR   A CD2   1 
ATOM   7607  C  CE1   . TYR   A  1  1029 ? -13.140 72.531  111.068 1.00 18.40 ? 1027 TYR   A CE1   1 
ATOM   7608  C  CE2   . TYR   A  1  1029 ? -14.606 71.676  112.757 1.00 19.60 ? 1027 TYR   A CE2   1 
ATOM   7609  C  CZ    . TYR   A  1  1029 ? -14.201 72.702  111.933 1.00 19.13 ? 1027 TYR   A CZ    1 
ATOM   7610  O  OH    . TYR   A  1  1029 ? -14.890 73.898  111.965 1.00 20.93 ? 1027 TYR   A OH    1 
ATOM   7611  N  N     . LEU   A  1  1030 ? -11.107 67.785  114.286 1.00 17.80 ? 1028 LEU   A N     1 
ATOM   7612  C  CA    . LEU   A  1  1030 ? -11.083 67.800  115.744 1.00 18.03 ? 1028 LEU   A CA    1 
ATOM   7613  C  C     . LEU   A  1  1030 ? -9.662  67.874  116.261 1.00 19.88 ? 1028 LEU   A C     1 
ATOM   7614  O  O     . LEU   A  1  1030 ? -9.424  68.462  117.323 1.00 20.04 ? 1028 LEU   A O     1 
ATOM   7615  C  CB    . LEU   A  1  1030 ? -11.762 66.564  116.316 1.00 19.71 ? 1028 LEU   A CB    1 
ATOM   7616  C  CG    . LEU   A  1  1030 ? -13.238 66.419  115.999 1.00 19.85 ? 1028 LEU   A CG    1 
ATOM   7617  C  CD1   . LEU   A  1  1030 ? -13.752 65.159  116.668 1.00 24.38 ? 1028 LEU   A CD1   1 
ATOM   7618  C  CD2   . LEU   A  1  1030 ? -14.030 67.641  116.459 1.00 22.88 ? 1028 LEU   A CD2   1 
ATOM   7619  N  N     . GLY   A  1  1031 ? -8.708  67.294  115.534 1.00 18.62 ? 1029 GLY   A N     1 
ATOM   7620  C  CA    . GLY   A  1  1031 ? -7.337  67.289  116.002 1.00 20.27 ? 1029 GLY   A CA    1 
ATOM   7621  C  C     . GLY   A  1  1031 ? -6.731  68.663  116.137 1.00 20.02 ? 1029 GLY   A C     1 
ATOM   7622  O  O     . GLY   A  1  1031 ? -5.748  68.828  116.870 1.00 21.25 ? 1029 GLY   A O     1 
ATOM   7623  N  N     . ARG   A  1  1032 ? -7.284  69.656  115.448 1.00 18.75 ? 1030 ARG   A N     1 
ATOM   7624  C  CA    . ARG   A  1  1032 ? -6.793  71.017  115.555 1.00 18.06 ? 1030 ARG   A CA    1 
ATOM   7625  C  C     . ARG   A  1  1032 ? -7.269  71.685  116.838 1.00 19.32 ? 1030 ARG   A C     1 
ATOM   7626  O  O     . ARG   A  1  1032 ? -6.727  72.722  117.235 1.00 22.65 ? 1030 ARG   A O     1 
ATOM   7627  C  CB    . ARG   A  1  1032 ? -7.285  71.807  114.345 1.00 21.20 ? 1030 ARG   A CB    1 
ATOM   7628  C  CG    . ARG   A  1  1032 ? -6.655  73.164  114.165 1.00 20.13 ? 1030 ARG   A CG    1 
ATOM   7629  C  CD    . ARG   A  1  1032 ? -5.215  73.042  113.736 1.00 20.99 ? 1030 ARG   A CD    1 
ATOM   7630  N  NE    . ARG   A  1  1032 ? -4.704  74.351  113.365 1.00 21.06 ? 1030 ARG   A NE    1 
ATOM   7631  C  CZ    . ARG   A  1  1032 ? -3.630  74.919  113.897 1.00 23.72 ? 1030 ARG   A CZ    1 
ATOM   7632  N  NH1   . ARG   A  1  1032 ? -2.958  74.345  114.883 1.00 24.57 ? 1030 ARG   A NH1   1 
ATOM   7633  N  NH2   . ARG   A  1  1032 ? -3.228  76.096  113.430 1.00 24.85 ? 1030 ARG   A NH2   1 
ATOM   7634  N  N     . LEU   A  1  1033 ? -8.269  71.106  117.492 1.00 18.55 ? 1031 LEU   A N     1 
ATOM   7635  C  CA    . LEU   A  1  1033 ? -8.927  71.716  118.633 1.00 19.84 ? 1031 LEU   A CA    1 
ATOM   7636  C  C     . LEU   A  1  1033 ? -8.461  71.130  119.954 1.00 20.19 ? 1031 LEU   A C     1 
ATOM   7637  O  O     . LEU   A  1  1033 ? -9.072  71.389  120.993 1.00 21.59 ? 1031 LEU   A O     1 
ATOM   7638  C  CB    . LEU   A  1  1033 ? -10.440 71.560  118.472 1.00 19.58 ? 1031 LEU   A CB    1 
ATOM   7639  C  CG    . LEU   A  1  1033 ? -10.937 72.028  117.109 1.00 20.95 ? 1031 LEU   A CG    1 
ATOM   7640  C  CD1   . LEU   A  1  1033 ? -12.443 71.834  116.974 1.00 20.59 ? 1031 LEU   A CD1   1 
ATOM   7641  C  CD2   . LEU   A  1  1033 ? -10.558 73.483  116.869 1.00 21.92 ? 1031 LEU   A CD2   1 
ATOM   7642  N  N     . VAL   A  1  1034 ? -7.383  70.351  119.924 1.00 19.83 ? 1032 VAL   A N     1 
ATOM   7643  C  CA    . VAL   A  1  1034 ? -6.753  69.793  121.105 1.00 21.01 ? 1032 VAL   A CA    1 
ATOM   7644  C  C     . VAL   A  1  1034 ? -5.268  70.102  121.023 1.00 23.06 ? 1032 VAL   A C     1 
ATOM   7645  O  O     . VAL   A  1  1034 ? -4.738  70.432  119.962 1.00 22.62 ? 1032 VAL   A O     1 
ATOM   7646  C  CB    . VAL   A  1  1034 ? -7.000  68.280  121.232 1.00 22.33 ? 1032 VAL   A CB    1 
ATOM   7647  C  CG1   . VAL   A  1  1034 ? -8.483  68.012  121.544 1.00 22.43 ? 1032 VAL   A CG1   1 
ATOM   7648  C  CG2   . VAL   A  1  1034 ? -6.550  67.550  119.945 1.00 20.74 ? 1032 VAL   A CG2   1 
ATOM   7649  N  N     . THR   A  1  1035 ? -4.592  70.002  122.167 1.00 23.43 ? 1033 THR   A N     1 
ATOM   7650  C  CA    . THR   A  1  1035 ? -3.183  70.374  122.196 1.00 24.13 ? 1033 THR   A CA    1 
ATOM   7651  C  C     . THR   A  1  1035 ? -2.299  69.327  121.533 1.00 29.42 ? 1033 THR   A C     1 
ATOM   7652  O  O     . THR   A  1  1035 ? -1.278  69.677  120.936 1.00 32.92 ? 1033 THR   A O     1 
ATOM   7653  C  CB    . THR   A  1  1035 ? -2.743  70.650  123.630 1.00 28.48 ? 1033 THR   A CB    1 
ATOM   7654  O  OG1   . THR   A  1  1035 ? -3.059  69.523  124.454 1.00 39.02 ? 1033 THR   A OG1   1 
ATOM   7655  C  CG2   . THR   A  1  1035 ? -3.471  71.849  124.161 1.00 28.26 ? 1033 THR   A CG2   1 
ATOM   7656  N  N     . THR   A  1  1036 ? -2.667  68.052  121.629 1.00 24.46 ? 1034 THR   A N     1 
ATOM   7657  C  CA    . THR   A  1  1036 ? -1.954  66.963  120.975 1.00 24.95 ? 1034 THR   A CA    1 
ATOM   7658  C  C     . THR   A  1  1036 ? -2.947  66.257  120.068 1.00 26.21 ? 1034 THR   A C     1 
ATOM   7659  O  O     . THR   A  1  1036 ? -3.928  65.684  120.553 1.00 26.89 ? 1034 THR   A O     1 
ATOM   7660  C  CB    . THR   A  1  1036 ? -1.418  65.973  122.011 1.00 30.41 ? 1034 THR   A CB    1 
ATOM   7661  O  OG1   . THR   A  1  1036 ? -0.520  66.646  122.901 1.00 33.18 ? 1034 THR   A OG1   1 
ATOM   7662  C  CG2   . THR   A  1  1036 ? -0.678  64.832  121.306 1.00 31.78 ? 1034 THR   A CG2   1 
ATOM   7663  N  N     . ALA   A  1  1037 ? -2.691  66.288  118.771 1.00 25.65 ? 1035 ALA   A N     1 
ATOM   7664  C  CA    . ALA   A  1  1037 ? -3.672  65.781  117.826 1.00 25.27 ? 1035 ALA   A CA    1 
ATOM   7665  C  C     . ALA   A  1  1037 ? -3.713  64.257  117.871 1.00 23.66 ? 1035 ALA   A C     1 
ATOM   7666  O  O     . ALA   A  1  1037 ? -2.666  63.608  117.919 1.00 24.95 ? 1035 ALA   A O     1 
ATOM   7667  C  CB    . ALA   A  1  1037 ? -3.346  66.243  116.406 1.00 26.00 ? 1035 ALA   A CB    1 
ATOM   7668  N  N     . PRO   A  1  1038 ? -4.900  63.662  117.884 1.00 22.05 ? 1036 PRO   A N     1 
ATOM   7669  C  CA    . PRO   A  1  1038 ? -5.003  62.205  117.766 1.00 20.54 ? 1036 PRO   A CA    1 
ATOM   7670  C  C     . PRO   A  1  1038 ? -4.721  61.782  116.337 1.00 21.63 ? 1036 PRO   A C     1 
ATOM   7671  O  O     . PRO   A  1  1038 ? -4.608  62.593  115.421 1.00 20.51 ? 1036 PRO   A O     1 
ATOM   7672  C  CB    . PRO   A  1  1038 ? -6.467  61.938  118.103 1.00 24.90 ? 1036 PRO   A CB    1 
ATOM   7673  C  CG    . PRO   A  1  1038 ? -7.164  63.156  117.572 1.00 25.44 ? 1036 PRO   A CG    1 
ATOM   7674  C  CD    . PRO   A  1  1038 ? -6.227  64.303  117.914 1.00 22.02 ? 1036 PRO   A CD    1 
ATOM   7675  N  N     . VAL   A  1  1039 ? -4.612  60.470  116.159 1.00 21.86 ? 1037 VAL   A N     1 
ATOM   7676  C  CA    . VAL   A  1  1039 ? -4.497  59.867  114.835 1.00 20.01 ? 1037 VAL   A CA    1 
ATOM   7677  C  C     . VAL   A  1  1039 ? -5.913  59.686  114.296 1.00 19.55 ? 1037 VAL   A C     1 
ATOM   7678  O  O     . VAL   A  1  1039 ? -6.667  58.877  114.851 1.00 20.12 ? 1037 VAL   A O     1 
ATOM   7679  C  CB    . VAL   A  1  1039 ? -3.768  58.521  114.901 1.00 21.00 ? 1037 VAL   A CB    1 
ATOM   7680  C  CG1   . VAL   A  1  1039 ? -3.645  57.927  113.515 1.00 23.36 ? 1037 VAL   A CG1   1 
ATOM   7681  C  CG2   . VAL   A  1  1039 ? -2.400  58.696  115.546 1.00 24.85 ? 1037 VAL   A CG2   1 
ATOM   7682  N  N     . PRO   A  1  1040 ? -6.308  60.396  113.244 1.00 19.52 ? 1038 PRO   A N     1 
ATOM   7683  C  CA    . PRO   A  1  1040 ? -7.665  60.250  112.742 1.00 20.17 ? 1038 PRO   A CA    1 
ATOM   7684  C  C     . PRO   A  1  1040 ? -7.902  58.847  112.213 1.00 18.96 ? 1038 PRO   A C     1 
ATOM   7685  O  O     . PRO   A  1  1040 ? -6.956  58.137  111.837 1.00 18.49 ? 1038 PRO   A O     1 
ATOM   7686  C  CB    . PRO   A  1  1040 ? -7.743  61.281  111.599 1.00 20.47 ? 1038 PRO   A CB    1 
ATOM   7687  C  CG    . PRO   A  1  1040 ? -6.637  62.230  111.864 1.00 22.25 ? 1038 PRO   A CG    1 
ATOM   7688  C  CD    . PRO   A  1  1040 ? -5.551  61.427  112.517 1.00 20.65 ? 1038 PRO   A CD    1 
ATOM   7689  N  N     . PRO   A  1  1041 ? -9.158  58.421  112.137 1.00 18.56 ? 1039 PRO   A N     1 
ATOM   7690  C  CA    . PRO   A  1  1041 ? -9.455  57.146  111.488 1.00 18.53 ? 1039 PRO   A CA    1 
ATOM   7691  C  C     . PRO   A  1  1041 ? -8.925  57.159  110.071 1.00 18.01 ? 1039 PRO   A C     1 
ATOM   7692  O  O     . PRO   A  1  1041 ? -8.980  58.180  109.381 1.00 19.26 ? 1039 PRO   A O     1 
ATOM   7693  C  CB    . PRO   A  1  1041 ? -10.985 57.105  111.476 1.00 20.91 ? 1039 PRO   A CB    1 
ATOM   7694  C  CG    . PRO   A  1  1041 ? -11.400 58.030  112.565 1.00 24.40 ? 1039 PRO   A CG    1 
ATOM   7695  C  CD    . PRO   A  1  1041 ? -10.381 59.118  112.580 1.00 22.03 ? 1039 PRO   A CD    1 
ATOM   7696  N  N     . GLN   A  1  1042 ? -8.374  56.020  109.653 1.00 16.50 ? 1040 GLN   A N     1 
ATOM   7697  C  CA    . GLN   A  1  1042 ? -7.917  55.775  108.291 1.00 17.50 ? 1040 GLN   A CA    1 
ATOM   7698  C  C     . GLN   A  1  1042 ? -6.754  56.659  107.878 1.00 17.66 ? 1040 GLN   A C     1 
ATOM   7699  O  O     . GLN   A  1  1042 ? -6.388  56.670  106.705 1.00 19.07 ? 1040 GLN   A O     1 
ATOM   7700  C  CB    . GLN   A  1  1042 ? -9.049  55.897  107.265 1.00 20.76 ? 1040 GLN   A CB    1 
ATOM   7701  C  CG    . GLN   A  1  1042 ? -10.235 55.001  107.564 1.00 27.26 ? 1040 GLN   A CG    1 
ATOM   7702  C  CD    . GLN   A  1  1042 ? -11.298 55.102  106.481 1.00 32.50 ? 1040 GLN   A CD    1 
ATOM   7703  O  OE1   . GLN   A  1  1042 ? -12.148 55.988  106.515 1.00 39.29 ? 1040 GLN   A OE1   1 
ATOM   7704  N  NE2   . GLN   A  1  1042 ? -11.229 54.213  105.502 1.00 39.05 ? 1040 GLN   A NE2   1 
ATOM   7705  N  N     . HIS   A  1  1043 ? -6.136  57.371  108.815 1.00 17.03 ? 1041 HIS   A N     1 
ATOM   7706  C  CA    . HIS   A  1  1043 ? -5.140  58.384  108.483 1.00 16.84 ? 1041 HIS   A CA    1 
ATOM   7707  C  C     . HIS   A  1  1043 ? -3.752  57.760  108.541 1.00 17.75 ? 1041 HIS   A C     1 
ATOM   7708  O  O     . HIS   A  1  1043 ? -3.162  57.636  109.613 1.00 17.22 ? 1041 HIS   A O     1 
ATOM   7709  C  CB    . HIS   A  1  1043 ? -5.263  59.545  109.459 1.00 17.84 ? 1041 HIS   A CB    1 
ATOM   7710  C  CG    . HIS   A  1  1043 ? -4.301  60.657  109.201 1.00 17.04 ? 1041 HIS   A CG    1 
ATOM   7711  N  ND1   . HIS   A  1  1043 ? -4.573  61.701  108.347 1.00 17.14 ? 1041 HIS   A ND1   1 
ATOM   7712  C  CD2   . HIS   A  1  1043 ? -3.072  60.901  109.715 1.00 17.87 ? 1041 HIS   A CD2   1 
ATOM   7713  C  CE1   . HIS   A  1  1043 ? -3.549  62.535  108.331 1.00 18.64 ? 1041 HIS   A CE1   1 
ATOM   7714  N  NE2   . HIS   A  1  1043 ? -2.627  62.072  109.155 1.00 18.61 ? 1041 HIS   A NE2   1 
ATOM   7715  N  N     . SER   A  1  1044 ? -3.246  57.346  107.385 1.00 17.14 ? 1042 SER   A N     1 
ATOM   7716  C  CA    . SER   A  1  1044 ? -1.891  56.817  107.246 1.00 15.32 ? 1042 SER   A CA    1 
ATOM   7717  C  C     . SER   A  1  1044 ? -1.609  56.761  105.756 1.00 15.91 ? 1042 SER   A C     1 
ATOM   7718  O  O     . SER   A  1  1044 ? -2.509  56.909  104.931 1.00 17.80 ? 1042 SER   A O     1 
ATOM   7719  C  CB    . SER   A  1  1044 ? -1.760  55.419  107.845 1.00 17.79 ? 1042 SER   A CB    1 
ATOM   7720  O  OG    . SER   A  1  1044 ? -2.580  54.502  107.155 1.00 18.39 ? 1042 SER   A OG    1 
ATOM   7721  N  N     . SER   A  1  1045 ? -0.347  56.525  105.421 1.00 16.34 ? 1043 SER   A N     1 
ATOM   7722  C  CA    . SER   A  1  1045 ? 0.005   56.327  104.028 1.00 16.28 ? 1043 SER   A CA    1 
ATOM   7723  C  C     . SER   A  1  1045 ? 1.206   55.408  103.974 1.00 15.98 ? 1043 SER   A C     1 
ATOM   7724  O  O     . SER   A  1  1045 ? 2.149   55.568  104.752 1.00 16.15 ? 1043 SER   A O     1 
ATOM   7725  C  CB    . SER   A  1  1045 ? 0.369   57.650  103.360 1.00 18.07 ? 1043 SER   A CB    1 
ATOM   7726  O  OG    . SER   A  1  1045 ? 0.824   57.399  102.034 1.00 17.48 ? 1043 SER   A OG    1 
ATOM   7727  N  N     . VAL   A  1  1046 ? 1.176   54.451  103.040 1.00 16.69 ? 1044 VAL   A N     1 
ATOM   7728  C  CA    . VAL   A  1  1046 ? 2.338   53.587  102.853 1.00 18.35 ? 1044 VAL   A CA    1 
ATOM   7729  C  C     . VAL   A  1  1046 ? 3.402   54.221  101.986 1.00 17.17 ? 1044 VAL   A C     1 
ATOM   7730  O  O     . VAL   A  1  1046 ? 4.472   53.626  101.813 1.00 18.67 ? 1044 VAL   A O     1 
ATOM   7731  C  CB    . VAL   A  1  1046 ? 2.011   52.201  102.272 1.00 18.83 ? 1044 VAL   A CB    1 
ATOM   7732  C  CG1   . VAL   A  1  1046 ? 1.059   51.455  103.214 1.00 21.10 ? 1044 VAL   A CG1   1 
ATOM   7733  C  CG2   . VAL   A  1  1046 ? 1.423   52.326  100.893 1.00 20.35 ? 1044 VAL   A CG2   1 
ATOM   7734  N  N     . HIS   A  1  1047 ? 3.151   55.404  101.458 1.00 16.32 ? 1045 HIS   A N     1 
ATOM   7735  C  CA    . HIS   A  1  1047 ? 4.073   56.032  100.530 1.00 18.05 ? 1045 HIS   A CA    1 
ATOM   7736  C  C     . HIS   A  1  1047 ? 5.020   56.953  101.266 1.00 17.86 ? 1045 HIS   A C     1 
ATOM   7737  O  O     . HIS   A  1  1047 ? 4.642   57.609  102.239 1.00 17.62 ? 1045 HIS   A O     1 
ATOM   7738  C  CB    . HIS   A  1  1047 ? 3.265   56.789  99.493  1.00 20.34 ? 1045 HIS   A CB    1 
ATOM   7739  C  CG    . HIS   A  1  1047 ? 2.280   55.905  98.806  1.00 22.45 ? 1045 HIS   A CG    1 
ATOM   7740  N  ND1   . HIS   A  1  1047 ? 2.667   54.919  97.920  1.00 24.75 ? 1045 HIS   A ND1   1 
ATOM   7741  C  CD2   . HIS   A  1  1047 ? 0.935   55.805  98.921  1.00 25.70 ? 1045 HIS   A CD2   1 
ATOM   7742  C  CE1   . HIS   A  1  1047 ? 1.593   54.283  97.483  1.00 26.75 ? 1045 HIS   A CE1   1 
ATOM   7743  N  NE2   . HIS   A  1  1047 ? 0.532   54.799  98.079  1.00 26.70 ? 1045 HIS   A NE2   1 
ATOM   7744  N  N     . THR   A  1  1048 ? 6.261   56.979  100.816 1.00 16.93 ? 1046 THR   A N     1 
ATOM   7745  C  CA    . THR   A  1  1048 ? 7.279   57.816  101.425 1.00 17.19 ? 1046 THR   A CA    1 
ATOM   7746  C  C     . THR   A  1  1048 ? 7.764   58.799  100.383 1.00 17.68 ? 1046 THR   A C     1 
ATOM   7747  O  O     . THR   A  1  1048 ? 8.097   58.405  99.264  1.00 19.50 ? 1046 THR   A O     1 
ATOM   7748  C  CB    . THR   A  1  1048 ? 8.431   56.974  101.928 1.00 16.79 ? 1046 THR   A CB    1 
ATOM   7749  O  OG1   . THR   A  1  1048 ? 7.922   55.943  102.781 1.00 19.78 ? 1046 THR   A OG1   1 
ATOM   7750  C  CG2   . THR   A  1  1048 ? 9.383   57.848  102.748 1.00 19.38 ? 1046 THR   A CG2   1 
ATOM   7751  N  N     . ASP   A  1  1049 ? 7.787   60.065  100.744 1.00 17.24 ? 1047 ASP   A N     1 
ATOM   7752  C  CA    . ASP   A  1  1049 ? 8.224   61.067  99.800  1.00 15.98 ? 1047 ASP   A CA    1 
ATOM   7753  C  C     . ASP   A  1  1049 ? 9.685   60.804  99.431  1.00 16.76 ? 1047 ASP   A C     1 
ATOM   7754  O  O     . ASP   A  1  1049 ? 10.525  60.609  100.322 1.00 16.83 ? 1047 ASP   A O     1 
ATOM   7755  C  CB    . ASP   A  1  1049 ? 8.056   62.449  100.420 1.00 15.93 ? 1047 ASP   A CB    1 
ATOM   7756  C  CG    . ASP   A  1  1049 ? 8.491   63.542  99.489  1.00 17.74 ? 1047 ASP   A CG    1 
ATOM   7757  O  OD1   . ASP   A  1  1049 ? 9.719   63.780  99.409  1.00 17.89 ? 1047 ASP   A OD1   1 
ATOM   7758  O  OD2   . ASP   A  1  1049 ? 7.616   64.142  98.819  1.00 18.57 ? 1047 ASP   A OD2   1 
ATOM   7759  N  N     . PRO   A  1  1050 ? 10.016  60.755  98.141  1.00 15.11 ? 1048 PRO   A N     1 
ATOM   7760  C  CA    . PRO   A  1  1050 ? 11.380  60.381  97.757  1.00 16.37 ? 1048 PRO   A CA    1 
ATOM   7761  C  C     . PRO   A  1  1050 ? 12.396  61.467  98.034  1.00 16.21 ? 1048 PRO   A C     1 
ATOM   7762  O  O     . PRO   A  1  1050 ? 13.583  61.161  98.216  1.00 17.50 ? 1048 PRO   A O     1 
ATOM   7763  C  CB    . PRO   A  1  1050 ? 11.257  60.093  96.258  1.00 18.97 ? 1048 PRO   A CB    1 
ATOM   7764  C  CG    . PRO   A  1  1050 ? 10.095  60.923  95.827  1.00 17.89 ? 1048 PRO   A CG    1 
ATOM   7765  C  CD    . PRO   A  1  1050 ? 9.136   60.949  96.978  1.00 16.97 ? 1048 PRO   A CD    1 
ATOM   7766  N  N     . VAL   A  1  1051 ? 11.967  62.725  98.061  1.00 15.46 ? 1049 VAL   A N     1 
ATOM   7767  C  CA    . VAL   A  1  1051 ? 12.890  63.801  98.383  1.00 17.16 ? 1049 VAL   A CA    1 
ATOM   7768  C  C     . VAL   A  1  1051 ? 13.210  63.771  99.862  1.00 16.22 ? 1049 VAL   A C     1 
ATOM   7769  O  O     . VAL   A  1  1051 ? 14.352  64.012  100.265 1.00 17.57 ? 1049 VAL   A O     1 
ATOM   7770  C  CB    . VAL   A  1  1051 ? 12.316  65.154  97.949  1.00 16.32 ? 1049 VAL   A CB    1 
ATOM   7771  C  CG1   . VAL   A  1  1051 ? 13.301  66.257  98.268  1.00 20.62 ? 1049 VAL   A CG1   1 
ATOM   7772  C  CG2   . VAL   A  1  1051 ? 11.997  65.131  96.458  1.00 16.78 ? 1049 VAL   A CG2   1 
ATOM   7773  N  N     . LEU   A  1  1052 ? 12.212  63.463  100.694 1.00 15.58 ? 1050 LEU   A N     1 
ATOM   7774  C  CA    . LEU   A  1  1052 ? 12.487  63.185  102.095 1.00 15.61 ? 1050 LEU   A CA    1 
ATOM   7775  C  C     . LEU   A  1  1052 ? 13.542  62.096  102.225 1.00 17.58 ? 1050 LEU   A C     1 
ATOM   7776  O  O     . LEU   A  1  1052 ? 14.509  62.240  102.977 1.00 15.60 ? 1050 LEU   A O     1 
ATOM   7777  C  CB    . LEU   A  1  1052 ? 11.185  62.781  102.788 1.00 16.54 ? 1050 LEU   A CB    1 
ATOM   7778  C  CG    . LEU   A  1  1052 ? 11.233  62.370  104.262 1.00 16.50 ? 1050 LEU   A CG    1 
ATOM   7779  C  CD1   . LEU   A  1  1052 ? 11.821  60.961  104.500 1.00 16.76 ? 1050 LEU   A CD1   1 
ATOM   7780  C  CD2   . LEU   A  1  1052 ? 11.976  63.425  105.101 1.00 17.04 ? 1050 LEU   A CD2   1 
ATOM   7781  N  N     . LEU   A  1  1053 ? 13.363  60.984  101.498 1.00 16.66 ? 1051 LEU   A N     1 
ATOM   7782  C  CA    . LEU   A  1  1053 ? 14.346  59.907  101.562 1.00 16.65 ? 1051 LEU   A CA    1 
ATOM   7783  C  C     . LEU   A  1  1053 ? 15.724  60.390  101.146 1.00 15.39 ? 1051 LEU   A C     1 
ATOM   7784  O  O     . LEU   A  1  1053 ? 16.713  60.072  101.810 1.00 16.81 ? 1051 LEU   A O     1 
ATOM   7785  C  CB    . LEU   A  1  1053 ? 13.909  58.719  100.703 1.00 18.16 ? 1051 LEU   A CB    1 
ATOM   7786  C  CG    . LEU   A  1  1053 ? 12.715  57.939  101.252 1.00 18.91 ? 1051 LEU   A CG    1 
ATOM   7787  C  CD1   . LEU   A  1  1053 ? 12.231  56.900  100.240 1.00 19.44 ? 1051 LEU   A CD1   1 
ATOM   7788  C  CD2   . LEU   A  1  1053 ? 13.041  57.272  102.573 1.00 21.22 ? 1051 LEU   A CD2   1 
ATOM   7789  N  N     . ASP   A  1  1054 ? 15.812  61.188  100.079 1.00 16.41 ? 1052 ASP   A N     1 
ATOM   7790  C  CA    . ASP   A  1  1054 ? 17.116  61.704  99.664  1.00 17.04 ? 1052 ASP   A CA    1 
ATOM   7791  C  C     . ASP   A  1  1054 ? 17.700  62.614  100.733 1.00 16.77 ? 1052 ASP   A C     1 
ATOM   7792  O  O     . ASP   A  1  1054 ? 18.910  62.602  100.977 1.00 18.22 ? 1052 ASP   A O     1 
ATOM   7793  C  CB    . ASP   A  1  1054 ? 16.991  62.470  98.349  1.00 17.63 ? 1052 ASP   A CB    1 
ATOM   7794  C  CG    . ASP   A  1  1054 ? 16.728  61.566  97.170  1.00 21.75 ? 1052 ASP   A CG    1 
ATOM   7795  O  OD1   . ASP   A  1  1054 ? 16.860  60.336  97.328  1.00 19.75 ? 1052 ASP   A OD1   1 
ATOM   7796  O  OD2   . ASP   A  1  1054 ? 16.391  62.102  96.098  1.00 24.68 ? 1052 ASP   A OD2   1 
ATOM   7797  N  N     . PHE   A  1  1055 ? 16.852  63.417  101.374 1.00 15.94 ? 1053 PHE   A N     1 
ATOM   7798  C  CA    . PHE   A  1  1055 ? 17.329  64.294  102.433 1.00 16.35 ? 1053 PHE   A CA    1 
ATOM   7799  C  C     . PHE   A  1  1055 ? 17.857  63.484  103.605 1.00 16.09 ? 1053 PHE   A C     1 
ATOM   7800  O  O     . PHE   A  1  1055 ? 18.911  63.808  104.176 1.00 17.35 ? 1053 PHE   A O     1 
ATOM   7801  C  CB    . PHE   A  1  1055 ? 16.195  65.225  102.863 1.00 16.14 ? 1053 PHE   A CB    1 
ATOM   7802  C  CG    . PHE   A  1  1055 ? 16.577  66.180  103.944 1.00 16.24 ? 1053 PHE   A CG    1 
ATOM   7803  C  CD1   . PHE   A  1  1055 ? 17.648  67.048  103.776 1.00 19.67 ? 1053 PHE   A CD1   1 
ATOM   7804  C  CD2   . PHE   A  1  1055 ? 15.850  66.224  105.114 1.00 17.48 ? 1053 PHE   A CD2   1 
ATOM   7805  C  CE1   . PHE   A  1  1055 ? 18.002  67.944  104.787 1.00 21.05 ? 1053 PHE   A CE1   1 
ATOM   7806  C  CE2   . PHE   A  1  1055 ? 16.198  67.121  106.124 1.00 18.51 ? 1053 PHE   A CE2   1 
ATOM   7807  C  CZ    . PHE   A  1  1055 ? 17.273  67.972  105.952 1.00 20.13 ? 1053 PHE   A CZ    1 
ATOM   7808  N  N     . ALA   A  1  1056 ? 17.135  62.432  103.991 1.00 16.73 ? 1054 ALA   A N     1 
ATOM   7809  C  CA    . ALA   A  1  1056 ? 17.604  61.581  105.081 1.00 17.75 ? 1054 ALA   A CA    1 
ATOM   7810  C  C     . ALA   A  1  1056 ? 18.974  60.989  104.771 1.00 18.75 ? 1054 ALA   A C     1 
ATOM   7811  O  O     . ALA   A  1  1056 ? 19.845  60.925  105.647 1.00 18.37 ? 1054 ALA   A O     1 
ATOM   7812  C  CB    . ALA   A  1  1056 ? 16.579  60.487  105.381 1.00 18.25 ? 1054 ALA   A CB    1 
ATOM   7813  N  N     . LYS   A  1  1057 ? 19.193  60.552  103.531 1.00 18.55 ? 1055 LYS   A N     1 
ATOM   7814  C  CA    . LYS   A  1  1057 ? 20.509  60.021  103.184 1.00 21.04 ? 1055 LYS   A CA    1 
ATOM   7815  C  C     . LYS   A  1  1057 ? 21.567  61.110  103.225 1.00 19.02 ? 1055 LYS   A C     1 
ATOM   7816  O  O     . LYS   A  1  1057 ? 22.703  60.864  103.656 1.00 21.00 ? 1055 LYS   A O     1 
ATOM   7817  C  CB    . LYS   A  1  1057 ? 20.472  59.375  101.802 1.00 22.88 ? 1055 LYS   A CB    1 
ATOM   7818  C  CG    . LYS   A  1  1057 ? 19.756  58.043  101.791 1.00 22.37 ? 1055 LYS   A CG    1 
ATOM   7819  C  CD    . LYS   A  1  1057 ? 19.941  57.342  100.457 1.00 22.21 ? 1055 LYS   A CD    1 
ATOM   7820  C  CE    . LYS   A  1  1057 ? 19.338  58.150  99.330  1.00 22.78 ? 1055 LYS   A CE    1 
ATOM   7821  N  NZ    . LYS   A  1  1057 ? 19.186  57.295  98.118  1.00 25.83 ? 1055 LYS   A NZ    1 
ATOM   7822  N  N     . TRP   A  1  1058 ? 21.217  62.309  102.767 1.00 18.15 ? 1056 TRP   A N     1 
ATOM   7823  C  CA    . TRP   A  1  1058 ? 22.138  63.435  102.840 1.00 20.43 ? 1056 TRP   A CA    1 
ATOM   7824  C  C     . TRP   A  1  1058 ? 22.489  63.758  104.287 1.00 19.06 ? 1056 TRP   A C     1 
ATOM   7825  O  O     . TRP   A  1  1058 ? 23.659  63.992  104.609 1.00 20.96 ? 1056 TRP   A O     1 
ATOM   7826  C  CB    . TRP   A  1  1058 ? 21.525  64.641  102.129 1.00 21.43 ? 1056 TRP   A CB    1 
ATOM   7827  C  CG    . TRP   A  1  1058 ? 22.356  65.892  102.223 1.00 21.05 ? 1056 TRP   A CG    1 
ATOM   7828  C  CD1   . TRP   A  1  1058 ? 23.360  66.278  101.373 1.00 24.30 ? 1056 TRP   A CD1   1 
ATOM   7829  C  CD2   . TRP   A  1  1058 ? 22.249  66.919  103.213 1.00 22.49 ? 1056 TRP   A CD2   1 
ATOM   7830  N  NE1   . TRP   A  1  1058 ? 23.880  67.487  101.781 1.00 26.61 ? 1056 TRP   A NE1   1 
ATOM   7831  C  CE2   . TRP   A  1  1058 ? 23.215  67.900  102.906 1.00 26.82 ? 1056 TRP   A CE2   1 
ATOM   7832  C  CE3   . TRP   A  1  1058 ? 21.428  67.106  104.329 1.00 22.22 ? 1056 TRP   A CE3   1 
ATOM   7833  C  CZ2   . TRP   A  1  1058 ? 23.385  69.050  103.679 1.00 25.36 ? 1056 TRP   A CZ2   1 
ATOM   7834  C  CZ3   . TRP   A  1  1058 ? 21.598  68.246  105.095 1.00 24.42 ? 1056 TRP   A CZ3   1 
ATOM   7835  C  CH2   . TRP   A  1  1058 ? 22.572  69.201  104.768 1.00 25.63 ? 1056 TRP   A CH2   1 
ATOM   7836  N  N     . LEU   A  1  1059 ? 21.494  63.736  105.177 1.00 18.58 ? 1057 LEU   A N     1 
ATOM   7837  C  CA    . LEU   A  1  1059 ? 21.749  63.987  106.589 1.00 20.29 ? 1057 LEU   A CA    1 
ATOM   7838  C  C     . LEU   A  1  1059 ? 22.727  62.973  107.146 1.00 20.83 ? 1057 LEU   A C     1 
ATOM   7839  O  O     . LEU   A  1  1059 ? 23.661  63.331  107.872 1.00 21.87 ? 1057 LEU   A O     1 
ATOM   7840  C  CB    . LEU   A  1  1059 ? 20.438  63.936  107.371 1.00 18.26 ? 1057 LEU   A CB    1 
ATOM   7841  C  CG    . LEU   A  1  1059 ? 19.580  65.178  107.230 1.00 19.40 ? 1057 LEU   A CG    1 
ATOM   7842  C  CD1   . LEU   A  1  1059 ? 18.189  64.925  107.812 1.00 18.80 ? 1057 LEU   A CD1   1 
ATOM   7843  C  CD2   . LEU   A  1  1059 ? 20.254  66.323  107.966 1.00 22.00 ? 1057 LEU   A CD2   1 
ATOM   7844  N  N     . ASP   A  1  1060 ? 22.523  61.694  106.831 1.00 19.61 ? 1058 ASP   A N     1 
ATOM   7845  C  CA    . ASP   A  1  1060 ? 23.459  60.672  107.285 1.00 25.67 ? 1058 ASP   A CA    1 
ATOM   7846  C  C     . ASP   A  1  1060 ? 24.853  60.911  106.724 1.00 23.77 ? 1058 ASP   A C     1 
ATOM   7847  O  O     . ASP   A  1  1060 ? 25.848  60.764  107.444 1.00 27.78 ? 1058 ASP   A O     1 
ATOM   7848  C  CB    . ASP   A  1  1060 ? 22.963  59.282  106.904 1.00 24.08 ? 1058 ASP   A CB    1 
ATOM   7849  C  CG    . ASP   A  1  1060 ? 22.139  58.642  107.999 1.00 23.39 ? 1058 ASP   A CG    1 
ATOM   7850  O  OD1   . ASP   A  1  1060 ? 22.410  58.918  109.199 1.00 29.46 ? 1058 ASP   A OD1   1 
ATOM   7851  O  OD2   . ASP   A  1  1060 ? 21.226  57.864  107.670 1.00 30.85 ? 1058 ASP   A OD2   1 
ATOM   7852  N  N     . GLY   A  1  1061 ? 24.954  61.285  105.449 1.00 23.94 ? 1059 GLY   A N     1 
ATOM   7853  C  CA    . GLY   A  1  1061 ? 26.265  61.560  104.881 1.00 24.53 ? 1059 GLY   A CA    1 
ATOM   7854  C  C     . GLY   A  1  1061 ? 26.949  62.749  105.526 1.00 26.72 ? 1059 GLY   A C     1 
ATOM   7855  O  O     . GLY   A  1  1061 ? 28.185  62.805  105.587 1.00 27.90 ? 1059 GLY   A O     1 
ATOM   7856  N  N     . LYS   A  1  1062 ? 26.168  63.707  106.027 1.00 25.29 ? 1060 LYS   A N     1 
ATOM   7857  C  CA    . LYS   A  1  1062 ? 26.710  64.851  106.746 1.00 26.64 ? 1060 LYS   A CA    1 
ATOM   7858  C  C     . LYS   A  1  1062 ? 27.059  64.521  108.189 1.00 26.99 ? 1060 LYS   A C     1 
ATOM   7859  O  O     . LYS   A  1  1062 ? 27.662  65.357  108.870 1.00 33.05 ? 1060 LYS   A O     1 
ATOM   7860  C  CB    . LYS   A  1  1062 ? 25.714  66.013  106.717 1.00 27.66 ? 1060 LYS   A CB    1 
ATOM   7861  C  CG    . LYS   A  1  1062 ? 25.573  66.692  105.361 1.00 28.68 ? 1060 LYS   A CG    1 
ATOM   7862  C  CD    . LYS   A  1  1062 ? 26.907  67.289  104.912 1.00 37.78 ? 1060 LYS   A CD    1 
ATOM   7863  C  CE    . LYS   A  1  1062 ? 26.820  67.901  103.523 1.00 38.92 ? 1060 LYS   A CE    1 
ATOM   7864  N  NZ    . LYS   A  1  1062 ? 28.127  68.475  103.082 1.00 42.40 ? 1060 LYS   A NZ    1 
ATOM   7865  N  N     . GLY   A  1  1063 ? 26.706  63.331  108.665 1.00 23.47 ? 1061 GLY   A N     1 
ATOM   7866  C  CA    . GLY   A  1  1063 ? 26.895  62.964  110.050 1.00 27.67 ? 1061 GLY   A CA    1 
ATOM   7867  C  C     . GLY   A  1  1063 ? 25.784  63.374  110.991 1.00 30.53 ? 1061 GLY   A C     1 
ATOM   7868  O  O     . GLY   A  1  1063 ? 25.933  63.196  112.209 1.00 29.51 ? 1061 GLY   A O     1 
ATOM   7869  N  N     . ALA   A  1  1064 ? 24.676  63.912  110.477 1.00 24.76 ? 1062 ALA   A N     1 
ATOM   7870  C  CA    . ALA   A  1  1064 ? 23.539  64.304  111.316 1.00 24.67 ? 1062 ALA   A CA    1 
ATOM   7871  C  C     . ALA   A  1  1064 ? 22.653  63.082  111.557 1.00 26.02 ? 1062 ALA   A C     1 
ATOM   7872  O  O     . ALA   A  1  1064 ? 21.537  62.958  111.054 1.00 21.64 ? 1062 ALA   A O     1 
ATOM   7873  C  CB    . ALA   A  1  1064 ? 22.784  65.467  110.686 1.00 26.18 ? 1062 ALA   A CB    1 
ATOM   7874  N  N     . ARG   A  1  1065 ? 23.190  62.148  112.338 1.00 22.86 ? 1063 ARG   A N     1 
ATOM   7875  C  CA    . ARG   A  1  1065 ? 22.572  60.833  112.447 1.00 20.68 ? 1063 ARG   A CA    1 
ATOM   7876  C  C     . ARG   A  1  1065 ? 21.200  60.903  113.114 1.00 24.03 ? 1063 ARG   A C     1 
ATOM   7877  O  O     . ARG   A  1  1065 ? 20.242  60.272  112.650 1.00 23.75 ? 1063 ARG   A O     1 
ATOM   7878  C  CB    . ARG   A  1  1065 ? 23.504  59.874  113.189 1.00 24.80 ? 1063 ARG   A CB    1 
ATOM   7879  N  N     . ALA   A  1  1066 ? 21.077  61.650  114.214 1.00 22.10 ? 1064 ALA   A N     1 
ATOM   7880  C  CA    . ALA   A  1  1066 ? 19.775  61.749  114.866 1.00 20.71 ? 1064 ALA   A CA    1 
ATOM   7881  C  C     . ALA   A  1  1066 ? 18.751  62.432  113.964 1.00 20.46 ? 1064 ALA   A C     1 
ATOM   7882  O  O     . ALA   A  1  1066 ? 17.586  62.027  113.926 1.00 21.21 ? 1064 ALA   A O     1 
ATOM   7883  C  CB    . ALA   A  1  1066 ? 19.890  62.480  116.203 1.00 24.34 ? 1064 ALA   A CB    1 
ATOM   7884  N  N     . GLU   A  1  1067 ? 19.169  63.470  113.233 1.00 20.84 ? 1065 GLU   A N     1 
ATOM   7885  C  CA    . GLU   A  1  1067 ? 18.248  64.142  112.319 1.00 19.27 ? 1065 GLU   A CA    1 
ATOM   7886  C  C     . GLU   A  1  1067 ? 17.849  63.240  111.159 1.00 20.77 ? 1065 GLU   A C     1 
ATOM   7887  O  O     . GLU   A  1  1067 ? 16.701  63.281  110.708 1.00 19.68 ? 1065 GLU   A O     1 
ATOM   7888  C  CB    . GLU   A  1  1067 ? 18.849  65.457  111.826 1.00 20.95 ? 1065 GLU   A CB    1 
ATOM   7889  C  CG    . GLU   A  1  1067 ? 18.918  66.529  112.919 1.00 20.36 ? 1065 GLU   A CG    1 
ATOM   7890  C  CD    . GLU   A  1  1067 ? 20.105  66.373  113.846 1.00 28.23 ? 1065 GLU   A CD    1 
ATOM   7891  O  OE1   . GLU   A  1  1067 ? 21.018  65.550  113.578 1.00 22.69 ? 1065 GLU   A OE1   1 
ATOM   7892  O  OE2   . GLU   A  1  1067 ? 20.121  67.096  114.861 1.00 30.78 ? 1065 GLU   A OE2   1 
ATOM   7893  N  N     . ALA   A  1  1068 ? 18.779  62.416  110.668 1.00 19.85 ? 1066 ALA   A N     1 
ATOM   7894  C  CA    . ALA   A  1  1068 ? 18.433  61.480  109.602 1.00 18.88 ? 1066 ALA   A CA    1 
ATOM   7895  C  C     . ALA   A  1  1068 ? 17.391  60.484  110.074 1.00 20.67 ? 1066 ALA   A C     1 
ATOM   7896  O  O     . ALA   A  1  1068 ? 16.468  60.138  109.326 1.00 19.23 ? 1066 ALA   A O     1 
ATOM   7897  C  CB    . ALA   A  1  1068 ? 19.682  60.744  109.123 1.00 21.18 ? 1066 ALA   A CB    1 
ATOM   7898  N  N     . GLU   A  1  1069 ? 17.524  60.009  111.311 1.00 20.71 ? 1067 GLU   A N     1 
ATOM   7899  C  CA    . GLU   A  1  1069 ? 16.524  59.111  111.867 1.00 19.78 ? 1067 GLU   A CA    1 
ATOM   7900  C  C     . GLU   A  1  1069 ? 15.189  59.822  112.017 1.00 20.51 ? 1067 GLU   A C     1 
ATOM   7901  O  O     . GLU   A  1  1069 ? 14.134  59.256  111.699 1.00 21.19 ? 1067 GLU   A O     1 
ATOM   7902  C  CB    . GLU   A  1  1069 ? 17.010  58.570  113.210 1.00 23.47 ? 1067 GLU   A CB    1 
ATOM   7903  C  CG    . GLU   A  1  1069 ? 15.947  57.807  113.974 1.00 27.40 ? 1067 GLU   A CG    1 
ATOM   7904  C  CD    . GLU   A  1  1069 ? 15.706  56.416  113.422 1.00 36.43 ? 1067 GLU   A CD    1 
ATOM   7905  O  OE1   . GLU   A  1  1069 ? 16.354  56.045  112.417 1.00 41.48 ? 1067 GLU   A OE1   1 
ATOM   7906  O  OE2   . GLU   A  1  1069 ? 14.866  55.689  114.000 1.00 46.24 ? 1067 GLU   A OE2   1 
ATOM   7907  N  N     . ALA   A  1  1070 ? 15.210  61.065  112.504 1.00 20.68 ? 1068 ALA   A N     1 
ATOM   7908  C  CA    . ALA   A  1  1070 ? 13.975  61.831  112.612 1.00 19.46 ? 1068 ALA   A CA    1 
ATOM   7909  C  C     . ALA   A  1  1070 ? 13.358  62.048  111.239 1.00 18.47 ? 1068 ALA   A C     1 
ATOM   7910  O  O     . ALA   A  1  1070 ? 12.128  62.029  111.084 1.00 18.54 ? 1068 ALA   A O     1 
ATOM   7911  C  CB    . ALA   A  1  1070 ? 14.246  63.175  113.290 1.00 22.80 ? 1068 ALA   A CB    1 
ATOM   7912  N  N     . ALA   A  1  1071 ? 14.202  62.249  110.228 1.00 18.28 ? 1069 ALA   A N     1 
ATOM   7913  C  CA    . ALA   A  1  1071 ? 13.696  62.427  108.876 1.00 16.69 ? 1069 ALA   A CA    1 
ATOM   7914  C  C     . ALA   A  1  1071 ? 13.020  61.158  108.379 1.00 17.66 ? 1069 ALA   A C     1 
ATOM   7915  O  O     . ALA   A  1  1071 ? 11.910  61.212  107.842 1.00 16.82 ? 1069 ALA   A O     1 
ATOM   7916  C  CB    . ALA   A  1  1071 ? 14.842  62.837  107.956 1.00 17.62 ? 1069 ALA   A CB    1 
ATOM   7917  N  N     . ARG   A  1  1072 ? 13.660  59.999  108.573 1.00 17.56 ? 1070 ARG   A N     1 
ATOM   7918  C  CA    . ARG   A  1  1072 ? 13.012  58.746  108.193 1.00 17.75 ? 1070 ARG   A CA    1 
ATOM   7919  C  C     . ARG   A  1  1072 ? 11.701  58.549  108.944 1.00 18.07 ? 1070 ARG   A C     1 
ATOM   7920  O  O     . ARG   A  1  1072 ? 10.710  58.098  108.360 1.00 18.61 ? 1070 ARG   A O     1 
ATOM   7921  C  CB    . ARG   A  1  1072 ? 13.945  57.558  108.427 1.00 20.25 ? 1070 ARG   A CB    1 
ATOM   7922  C  CG    . ARG   A  1  1072 ? 15.093  57.491  107.435 1.00 22.13 ? 1070 ARG   A CG    1 
ATOM   7923  C  CD    . ARG   A  1  1072 ? 15.885  56.214  107.626 1.00 24.71 ? 1070 ARG   A CD    1 
ATOM   7924  N  NE    . ARG   A  1  1072 ? 16.631  56.237  108.876 1.00 26.06 ? 1070 ARG   A NE    1 
ATOM   7925  C  CZ    . ARG   A  1  1072 ? 17.850  56.741  109.007 1.00 27.29 ? 1070 ARG   A CZ    1 
ATOM   7926  N  NH1   . ARG   A  1  1072 ? 18.499  57.264  107.975 1.00 28.24 ? 1070 ARG   A NH1   1 
ATOM   7927  N  NH2   . ARG   A  1  1072 ? 18.433  56.721  110.203 1.00 26.92 ? 1070 ARG   A NH2   1 
ATOM   7928  N  N     . ASN   A  1  1073 ? 11.669  58.890  110.235 1.00 18.47 ? 1071 ASN   A N     1 
ATOM   7929  C  CA    . ASN   A  1  1073 ? 10.435  58.767  110.998 1.00 18.44 ? 1071 ASN   A CA    1 
ATOM   7930  C  C     . ASN   A  1  1073 ? 9.358   59.684  110.443 1.00 18.34 ? 1071 ASN   A C     1 
ATOM   7931  O  O     . ASN   A  1  1073 ? 8.191   59.288  110.347 1.00 19.86 ? 1071 ASN   A O     1 
ATOM   7932  C  CB    . ASN   A  1  1073 ? 10.679  59.043  112.482 1.00 18.76 ? 1071 ASN   A CB    1 
ATOM   7933  C  CG    . ASN   A  1  1073 ? 11.471  57.940  113.147 1.00 25.80 ? 1071 ASN   A CG    1 
ATOM   7934  O  OD1   . ASN   A  1  1073 ? 11.592  56.837  112.614 1.00 29.28 ? 1071 ASN   A OD1   1 
ATOM   7935  N  ND2   . ASN   A  1  1073 ? 12.017  58.235  114.307 1.00 27.87 ? 1071 ASN   A ND2   1 
ATOM   7936  N  N     . ALA   A  1  1074 ? 9.734   60.911  110.062 1.00 17.72 ? 1072 ALA   A N     1 
ATOM   7937  C  CA    . ALA   A  1  1074 ? 8.768   61.812  109.446 1.00 18.45 ? 1072 ALA   A CA    1 
ATOM   7938  C  C     . ALA   A  1  1074 ? 8.257   61.238  108.139 1.00 17.43 ? 1072 ALA   A C     1 
ATOM   7939  O  O     . ALA   A  1  1074 ? 7.064   61.343  107.835 1.00 16.36 ? 1072 ALA   A O     1 
ATOM   7940  C  CB    . ALA   A  1  1074 ? 9.409   63.179  109.206 1.00 21.00 ? 1072 ALA   A CB    1 
ATOM   7941  N  N     . GLY   A  1  1075 ? 9.143   60.625  107.357 1.00 16.75 ? 1073 GLY   A N     1 
ATOM   7942  C  CA    . GLY   A  1  1075 ? 8.712   60.030  106.105 1.00 17.37 ? 1073 GLY   A CA    1 
ATOM   7943  C  C     . GLY   A  1  1075 ? 7.652   58.971  106.310 1.00 16.66 ? 1073 GLY   A C     1 
ATOM   7944  O  O     . GLY   A  1  1075 ? 6.704   58.875  105.531 1.00 17.40 ? 1073 GLY   A O     1 
ATOM   7945  N  N     . SER   A  1  1076 ? 7.806   58.156  107.354 1.00 18.59 ? 1074 SER   A N     1 
ATOM   7946  C  CA    . SER   A  1  1076 ? 6.836   57.106  107.646 1.00 17.80 ? 1074 SER   A CA    1 
ATOM   7947  C  C     . SER   A  1  1076 ? 5.566   57.676  108.252 1.00 18.54 ? 1074 SER   A C     1 
ATOM   7948  O  O     . SER   A  1  1076 ? 4.459   57.231  107.922 1.00 20.85 ? 1074 SER   A O     1 
ATOM   7949  C  CB    . SER   A  1  1076 ? 7.440   56.109  108.629 1.00 21.84 ? 1074 SER   A CB    1 
ATOM   7950  O  OG    . SER   A  1  1076 ? 8.406   55.308  108.001 1.00 29.69 ? 1074 SER   A OG    1 
ATOM   7951  N  N     . SER   A  1  1077 ? 5.706   58.658  109.145 1.00 18.83 ? 1075 SER   A N     1 
ATOM   7952  C  CA    A SER   A  1  1077 ? 4.550   59.202  109.847 0.50 19.65 ? 1075 SER   A CA    1 
ATOM   7953  C  CA    B SER   A  1  1077 ? 4.566   59.223  109.861 0.50 19.66 ? 1075 SER   A CA    1 
ATOM   7954  C  C     . SER   A  1  1077 ? 3.674   60.058  108.949 1.00 17.97 ? 1075 SER   A C     1 
ATOM   7955  O  O     . SER   A  1  1077 ? 2.472   60.209  109.216 1.00 20.41 ? 1075 SER   A O     1 
ATOM   7956  C  CB    A SER   A  1  1077 ? 5.010   60.032  111.043 0.50 19.71 ? 1075 SER   A CB    1 
ATOM   7957  C  CB    B SER   A  1  1077 ? 5.083   60.078  111.019 0.50 19.68 ? 1075 SER   A CB    1 
ATOM   7958  O  OG    A SER   A  1  1077 ? 5.552   59.193  112.039 0.50 24.01 ? 1075 SER   A OG    1 
ATOM   7959  O  OG    B SER   A  1  1077 ? 4.028   60.712  111.721 0.50 23.93 ? 1075 SER   A OG    1 
ATOM   7960  N  N     . SER   A  1  1078 ? 4.241   60.631  107.906 1.00 16.65 ? 1076 SER   A N     1 
ATOM   7961  C  CA    . SER   A  1  1078 ? 3.474   61.455  106.994 1.00 17.19 ? 1076 SER   A CA    1 
ATOM   7962  C  C     . SER   A  1  1078 ? 2.332   60.655  106.379 1.00 17.12 ? 1076 SER   A C     1 
ATOM   7963  O  O     . SER   A  1  1078 ? 2.487   59.492  106.008 1.00 17.73 ? 1076 SER   A O     1 
ATOM   7964  C  CB    . SER   A  1  1078 ? 4.392   61.930  105.884 1.00 16.83 ? 1076 SER   A CB    1 
ATOM   7965  O  OG    . SER   A  1  1078 ? 3.634   62.609  104.897 1.00 16.04 ? 1076 SER   A OG    1 
ATOM   7966  N  N     . ALA   A  1  1079 ? 1.171   61.282  106.262 1.00 15.92 ? 1077 ALA   A N     1 
ATOM   7967  C  CA    . ALA   A  1  1079 ? 0.054   60.657  105.578 1.00 16.08 ? 1077 ALA   A CA    1 
ATOM   7968  C  C     . ALA   A  1  1079 ? -0.093  61.160  104.151 1.00 15.69 ? 1077 ALA   A C     1 
ATOM   7969  O  O     . ALA   A  1  1079 ? -1.105  60.889  103.499 1.00 16.12 ? 1077 ALA   A O     1 
ATOM   7970  C  CB    . ALA   A  1  1079 ? -1.240  60.841  106.371 1.00 16.76 ? 1077 ALA   A CB    1 
ATOM   7971  N  N     . LEU   A  1  1080 ? 0.895   61.888  103.648 1.00 15.07 ? 1078 LEU   A N     1 
ATOM   7972  C  CA    . LEU   A  1  1080 ? 0.918   62.263  102.243 1.00 16.05 ? 1078 LEU   A CA    1 
ATOM   7973  C  C     . LEU   A  1  1080 ? 0.672   61.042  101.373 1.00 14.69 ? 1078 LEU   A C     1 
ATOM   7974  O  O     . LEU   A  1  1080 ? 1.331   60.010  101.530 1.00 15.30 ? 1078 LEU   A O     1 
ATOM   7975  C  CB    . LEU   A  1  1080 ? 2.304   62.823  101.923 1.00 15.32 ? 1078 LEU   A CB    1 
ATOM   7976  C  CG    . LEU   A  1  1080 ? 2.521   63.137  100.454 1.00 16.41 ? 1078 LEU   A CG    1 
ATOM   7977  C  CD1   . LEU   A  1  1080 ? 1.647   64.326  100.056 1.00 18.05 ? 1078 LEU   A CD1   1 
ATOM   7978  C  CD2   . LEU   A  1  1080 ? 3.987   63.428  100.214 1.00 16.47 ? 1078 LEU   A CD2   1 
ATOM   7979  N  N     . GLY   A  1  1081 ? -0.274  61.157  100.441 1.00 14.32 ? 1079 GLY   A N     1 
ATOM   7980  C  CA    . GLY   A  1  1081 ? -0.573  60.037  99.572  1.00 15.81 ? 1079 GLY   A CA    1 
ATOM   7981  C  C     . GLY   A  1  1081 ? -1.763  59.215  100.014 1.00 17.03 ? 1079 GLY   A C     1 
ATOM   7982  O  O     . GLY   A  1  1081 ? -2.184  58.316  99.269  1.00 17.59 ? 1079 GLY   A O     1 
ATOM   7983  N  N     . LEU   A  1  1082 ? -2.312  59.488  101.192 1.00 14.88 ? 1080 LEU   A N     1 
ATOM   7984  C  CA    A LEU   A  1  1082 ? -3.578  58.884  101.582 0.48 14.92 ? 1080 LEU   A CA    1 
ATOM   7985  C  CA    B LEU   A  1  1082 ? -3.583  58.890  101.586 0.52 14.92 ? 1080 LEU   A CA    1 
ATOM   7986  C  C     . LEU   A  1  1082 ? -4.595  59.108  100.474 1.00 16.63 ? 1080 LEU   A C     1 
ATOM   7987  O  O     . LEU   A  1  1082 ? -4.683  60.195  99.906  1.00 16.08 ? 1080 LEU   A O     1 
ATOM   7988  C  CB    A LEU   A  1  1082 ? -4.079  59.534  102.871 0.48 15.85 ? 1080 LEU   A CB    1 
ATOM   7989  C  CB    B LEU   A  1  1082 ? -4.083  59.557  102.872 0.52 15.84 ? 1080 LEU   A CB    1 
ATOM   7990  C  CG    A LEU   A  1  1082 ? -5.427  59.037  103.393 0.48 16.13 ? 1080 LEU   A CG    1 
ATOM   7991  C  CG    B LEU   A  1  1082 ? -5.429  59.121  103.462 0.52 16.11 ? 1080 LEU   A CG    1 
ATOM   7992  C  CD1   A LEU   A  1  1082 ? -5.391  57.544  103.656 0.48 17.20 ? 1080 LEU   A CD1   1 
ATOM   7993  C  CD1   B LEU   A  1  1082 ? -5.423  59.274  104.972 0.52 16.27 ? 1080 LEU   A CD1   1 
ATOM   7994  C  CD2   A LEU   A  1  1082 ? -5.828  59.795  104.641 0.48 16.83 ? 1080 LEU   A CD2   1 
ATOM   7995  C  CD2   B LEU   A  1  1082 ? -6.584  59.923  102.855 0.52 16.65 ? 1080 LEU   A CD2   1 
ATOM   7996  N  N     . ASP   A  1  1083 ? -5.346  58.062  100.155 1.00 15.88 ? 1081 ASP   A N     1 
ATOM   7997  C  CA    . ASP   A  1  1083 ? -6.278  58.135  99.030  1.00 16.95 ? 1081 ASP   A CA    1 
ATOM   7998  C  C     . ASP   A  1  1083 ? -7.437  57.196  99.350  1.00 19.70 ? 1081 ASP   A C     1 
ATOM   7999  O  O     . ASP   A  1  1083 ? -7.295  55.978  99.229  1.00 22.13 ? 1081 ASP   A O     1 
ATOM   8000  C  CB    . ASP   A  1  1083 ? -5.559  57.721  97.752  1.00 20.95 ? 1081 ASP   A CB    1 
ATOM   8001  C  CG    . ASP   A  1  1083 ? -6.423  57.835  96.520  1.00 30.07 ? 1081 ASP   A CG    1 
ATOM   8002  O  OD1   . ASP   A  1  1083 ? -7.492  58.471  96.580  1.00 30.63 ? 1081 ASP   A OD1   1 
ATOM   8003  O  OD2   . ASP   A  1  1083 ? -6.016  57.278  95.478  1.00 34.72 ? 1081 ASP   A OD2   1 
ATOM   8004  N  N     . LEU   A  1  1084 ? -8.564  57.767  99.769  1.00 17.79 ? 1082 LEU   A N     1 
ATOM   8005  C  CA    . LEU   A  1  1084 ? -9.675  56.997  100.291 1.00 18.61 ? 1082 LEU   A CA    1 
ATOM   8006  C  C     . LEU   A  1  1084 ? -10.928 57.291  99.492  1.00 18.64 ? 1082 LEU   A C     1 
ATOM   8007  O  O     . LEU   A  1  1084 ? -11.093 58.378  98.933  1.00 19.29 ? 1082 LEU   A O     1 
ATOM   8008  C  CB    . LEU   A  1  1084 ? -9.982  57.391  101.733 1.00 19.31 ? 1082 LEU   A CB    1 
ATOM   8009  C  CG    . LEU   A  1  1084 ? -8.898  57.153  102.770 1.00 22.33 ? 1082 LEU   A CG    1 
ATOM   8010  C  CD1   . LEU   A  1  1084 ? -9.334  57.793  104.070 1.00 23.35 ? 1082 LEU   A CD1   1 
ATOM   8011  C  CD2   . LEU   A  1  1084 ? -8.663  55.668  102.948 1.00 23.82 ? 1082 LEU   A CD2   1 
ATOM   8012  N  N     . GLU   A  1  1085 ? -11.819 56.315  99.459  1.00 18.00 ? 1083 GLU   A N     1 
ATOM   8013  C  CA    . GLU   A  1  1085 ? -13.172 56.540  98.978  1.00 18.39 ? 1083 GLU   A CA    1 
ATOM   8014  C  C     . GLU   A  1  1085 ? -14.089 56.546  100.187 1.00 18.94 ? 1083 GLU   A C     1 
ATOM   8015  O  O     . GLU   A  1  1085 ? -14.052 55.616  101.000 1.00 20.56 ? 1083 GLU   A O     1 
ATOM   8016  C  CB    . GLU   A  1  1085 ? -13.625 55.474  97.984  1.00 20.43 ? 1083 GLU   A CB    1 
ATOM   8017  C  CG    . GLU   A  1  1085 ? -15.065 55.763  97.550  1.00 21.78 ? 1083 GLU   A CG    1 
ATOM   8018  C  CD    . GLU   A  1  1085 ? -15.581 54.931  96.387  1.00 30.72 ? 1083 GLU   A CD    1 
ATOM   8019  O  OE1   . GLU   A  1  1085 ? -14.773 54.292  95.679  1.00 31.62 ? 1083 GLU   A OE1   1 
ATOM   8020  O  OE2   . GLU   A  1  1085 ? -16.823 54.933  96.194  1.00 27.85 ? 1083 GLU   A OE2   1 
ATOM   8021  N  N     . LEU   A  1  1086 ? -14.895 57.590  100.308 1.00 18.39 ? 1084 LEU   A N     1 
ATOM   8022  C  CA    . LEU   A  1  1086 ? -15.775 57.750  101.451 1.00 17.26 ? 1084 LEU   A CA    1 
ATOM   8023  C  C     . LEU   A  1  1086 ? -17.173 57.231  101.126 1.00 20.65 ? 1084 LEU   A C     1 
ATOM   8024  O  O     . LEU   A  1  1086 ? -17.670 57.449  100.022 1.00 20.53 ? 1084 LEU   A O     1 
ATOM   8025  C  CB    . LEU   A  1  1086 ? -15.854 59.228  101.836 1.00 18.51 ? 1084 LEU   A CB    1 
ATOM   8026  C  CG    . LEU   A  1  1086 ? -14.489 59.869  102.160 1.00 20.10 ? 1084 LEU   A CG    1 
ATOM   8027  C  CD1   . LEU   A  1  1086 ? -14.680 61.317  102.553 1.00 22.64 ? 1084 LEU   A CD1   1 
ATOM   8028  C  CD2   . LEU   A  1  1086 ? -13.755 59.110  103.258 1.00 23.42 ? 1084 LEU   A CD2   1 
ATOM   8029  N  N     . PRO   A  1  1087 ? -17.788 56.519  102.067 1.00 19.78 ? 1085 PRO   A N     1 
ATOM   8030  C  CA    . PRO   A  1  1087 ? -19.148 56.014  101.851 1.00 22.68 ? 1085 PRO   A CA    1 
ATOM   8031  C  C     . PRO   A  1  1087 ? -20.103 57.147  101.543 1.00 21.62 ? 1085 PRO   A C     1 
ATOM   8032  O  O     . PRO   A  1  1087 ? -20.062 58.210  102.165 1.00 23.92 ? 1085 PRO   A O     1 
ATOM   8033  C  CB    . PRO   A  1  1087 ? -19.506 55.372  103.194 1.00 26.13 ? 1085 PRO   A CB    1 
ATOM   8034  C  CG    . PRO   A  1  1087 ? -18.208 55.079  103.839 1.00 25.38 ? 1085 PRO   A CG    1 
ATOM   8035  C  CD    . PRO   A  1  1087 ? -17.232 56.106  103.364 1.00 18.80 ? 1085 PRO   A CD    1 
ATOM   8036  N  N     . GLY   A  1  1088 ? -20.994 56.899  100.591 1.00 21.62 ? 1086 GLY   A N     1 
ATOM   8037  C  CA    . GLY   A  1  1088 ? -21.975 57.881  100.222 1.00 22.80 ? 1086 GLY   A CA    1 
ATOM   8038  C  C     . GLY   A  1  1088 ? -23.075 57.264  99.394  1.00 19.11 ? 1086 GLY   A C     1 
ATOM   8039  O  O     . GLY   A  1  1088 ? -23.278 56.051  99.374  1.00 18.90 ? 1086 GLY   A O     1 
ATOM   8040  N  N     . PRO   A  1  1089 ? -23.802 58.105  98.682  1.00 20.90 ? 1087 PRO   A N     1 
ATOM   8041  C  CA    . PRO   A  1  1089 ? -24.921 57.611  97.883  1.00 19.37 ? 1087 PRO   A CA    1 
ATOM   8042  C  C     . PRO   A  1  1089 ? -24.420 56.835  96.676  1.00 21.62 ? 1087 PRO   A C     1 
ATOM   8043  O  O     . PRO   A  1  1089 ? -23.286 56.990  96.216  1.00 20.25 ? 1087 PRO   A O     1 
ATOM   8044  C  CB    . PRO   A  1  1089 ? -25.615 58.899  97.443  1.00 22.27 ? 1087 PRO   A CB    1 
ATOM   8045  C  CG    . PRO   A  1  1089 ? -24.467 59.895  97.357  1.00 24.00 ? 1087 PRO   A CG    1 
ATOM   8046  C  CD    . PRO   A  1  1089 ? -23.583 59.551  98.518  1.00 21.40 ? 1087 PRO   A CD    1 
ATOM   8047  N  N     . VAL   A  1  1090 ? -25.304 55.990  96.153  1.00 18.83 ? 1088 VAL   A N     1 
ATOM   8048  C  CA    . VAL   A  1  1090 ? -25.035 55.344  94.883  1.00 17.91 ? 1088 VAL   A CA    1 
ATOM   8049  C  C     . VAL   A  1  1090 ? -24.908 56.388  93.778  1.00 17.27 ? 1088 VAL   A C     1 
ATOM   8050  O  O     . VAL   A  1  1090 ? -25.383 57.525  93.884  1.00 17.50 ? 1088 VAL   A O     1 
ATOM   8051  C  CB    . VAL   A  1  1090 ? -26.093 54.296  94.510  1.00 18.82 ? 1088 VAL   A CB    1 
ATOM   8052  C  CG1   . VAL   A  1  1090 ? -26.188 53.217  95.578  1.00 20.62 ? 1088 VAL   A CG1   1 
ATOM   8053  C  CG2   . VAL   A  1  1090 ? -27.463 54.958  94.268  1.00 20.85 ? 1088 VAL   A CG2   1 
ATOM   8054  N  N     . GLY   A  1  1091 ? -24.230 55.995  92.708  1.00 17.14 ? 1089 GLY   A N     1 
ATOM   8055  C  CA    . GLY   A  1  1091 ? -24.144 56.878  91.564  1.00 18.15 ? 1089 GLY   A CA    1 
ATOM   8056  C  C     . GLY   A  1  1091 ? -23.191 58.028  91.756  1.00 15.91 ? 1089 GLY   A C     1 
ATOM   8057  O  O     . GLY   A  1  1091 ? -23.208 58.995  90.987  1.00 16.59 ? 1089 GLY   A O     1 
ATOM   8058  N  N     . GLU   A  1  1092 ? -22.345 57.940  92.770  1.00 16.38 ? 1090 GLU   A N     1 
ATOM   8059  C  CA    . GLU   A  1  1092 ? -21.353 58.962  93.020  1.00 17.46 ? 1090 GLU   A CA    1 
ATOM   8060  C  C     . GLU   A  1  1092 ? -20.138 58.279  93.622  1.00 16.72 ? 1090 GLU   A C     1 
ATOM   8061  O  O     . GLU   A  1  1092 ? -20.257 57.281  94.334  1.00 18.51 ? 1090 GLU   A O     1 
ATOM   8062  C  CB    . GLU   A  1  1092 ? -21.912 59.957  94.033  1.00 21.87 ? 1090 GLU   A CB    1 
ATOM   8063  C  CG    . GLU   A  1  1092 ? -21.307 61.338  94.025  1.00 24.54 ? 1090 GLU   A CG    1 
ATOM   8064  C  CD    . GLU   A  1  1092 ? -22.151 62.272  94.862  1.00 27.20 ? 1090 GLU   A CD    1 
ATOM   8065  O  OE1   . GLU   A  1  1092 ? -22.031 62.189  96.094  1.00 22.04 ? 1090 GLU   A OE1   1 
ATOM   8066  O  OE2   . GLU   A  1  1092 ? -22.970 63.042  94.301  1.00 26.75 ? 1090 GLU   A OE2   1 
ATOM   8067  N  N     . ARG   A  1  1093 ? -18.961 58.798  93.308  1.00 15.09 ? 1091 ARG   A N     1 
ATOM   8068  C  CA    . ARG   A  1  1093 ? -17.735 58.369  93.966  1.00 16.34 ? 1091 ARG   A CA    1 
ATOM   8069  C  C     . ARG   A  1  1093 ? -17.152 59.584  94.663  1.00 15.48 ? 1091 ARG   A C     1 
ATOM   8070  O  O     . ARG   A  1  1093 ? -16.940 60.630  94.039  1.00 17.02 ? 1091 ARG   A O     1 
ATOM   8071  C  CB    . ARG   A  1  1093 ? -16.736 57.785  92.972  1.00 19.70 ? 1091 ARG   A CB    1 
ATOM   8072  C  CG    . ARG   A  1  1093 ? -16.889 56.300  92.751  1.00 31.13 ? 1091 ARG   A CG    1 
ATOM   8073  C  CD    . ARG   A  1  1093 ? -15.556 55.676  92.325  1.00 39.02 ? 1091 ARG   A CD    1 
ATOM   8074  N  NE    . ARG   A  1  1093 ? -14.950 56.423  91.230  1.00 50.93 ? 1091 ARG   A NE    1 
ATOM   8075  C  CZ    . ARG   A  1  1093 ? -15.256 56.254  89.950  1.00 52.24 ? 1091 ARG   A CZ    1 
ATOM   8076  N  NH1   . ARG   A  1  1093 ? -16.140 55.348  89.565  1.00 48.06 ? 1091 ARG   A NH1   1 
ATOM   8077  N  NH2   . ARG   A  1  1093 ? -14.664 57.018  89.035  1.00 48.03 ? 1091 ARG   A NH2   1 
ATOM   8078  N  N     . ASN   A  1  1094 ? -16.912 59.446  95.952  1.00 15.77 ? 1092 ASN   A N     1 
ATOM   8079  C  CA    . ASN   A  1  1094 ? -16.479 60.559  96.774  1.00 15.18 ? 1092 ASN   A CA    1 
ATOM   8080  C  C     . ASN   A  1  1094 ? -15.122 60.199  97.336  1.00 16.70 ? 1092 ASN   A C     1 
ATOM   8081  O  O     . ASN   A  1  1094 ? -15.001 59.235  98.096  1.00 17.91 ? 1092 ASN   A O     1 
ATOM   8082  C  CB    . ASN   A  1  1094 ? -17.520 60.823  97.846  1.00 15.52 ? 1092 ASN   A CB    1 
ATOM   8083  C  CG    . ASN   A  1  1094 ? -18.734 61.483  97.255  1.00 14.55 ? 1092 ASN   A CG    1 
ATOM   8084  O  OD1   . ASN   A  1  1094 ? -18.638 62.612  96.803  1.00 16.90 ? 1092 ASN   A OD1   1 
ATOM   8085  N  ND2   . ASN   A  1  1094 ? -19.877 60.780  97.232  1.00 18.42 ? 1092 ASN   A ND2   1 
ATOM   8086  N  N     . LEU   A  1  1095 ? -14.116 60.947  96.916  1.00 15.93 ? 1093 LEU   A N     1 
ATOM   8087  C  CA    . LEU   A  1  1095 ? -12.731 60.610  97.190  1.00 15.34 ? 1093 LEU   A CA    1 
ATOM   8088  C  C     . LEU   A  1  1095 ? -12.122 61.659  98.094  1.00 17.13 ? 1093 LEU   A C     1 
ATOM   8089  O  O     . LEU   A  1  1095 ? -12.490 62.830  98.060  1.00 17.12 ? 1093 LEU   A O     1 
ATOM   8090  C  CB    . LEU   A  1  1095 ? -11.923 60.566  95.895  1.00 17.91 ? 1093 LEU   A CB    1 
ATOM   8091  C  CG    . LEU   A  1  1095 ? -12.532 59.623  94.856  1.00 19.61 ? 1093 LEU   A CG    1 
ATOM   8092  C  CD1   . LEU   A  1  1095 ? -11.701 59.662  93.584  1.00 24.25 ? 1093 LEU   A CD1   1 
ATOM   8093  C  CD2   . LEU   A  1  1095 ? -12.678 58.197  95.394  1.00 23.75 ? 1093 LEU   A CD2   1 
ATOM   8094  N  N     . TYR   A  1  1096 ? -11.153 61.221  98.883  1.00 16.35 ? 1094 TYR   A N     1 
ATOM   8095  C  CA    . TYR   A  1  1096 ? -10.511 62.083  99.862  1.00 15.00 ? 1094 TYR   A CA    1 
ATOM   8096  C  C     . TYR   A  1  1096 ? -9.041  61.738  99.830  1.00 15.66 ? 1094 TYR   A C     1 
ATOM   8097  O  O     . TYR   A  1  1096 ? -8.684  60.567  99.982  1.00 16.48 ? 1094 TYR   A O     1 
ATOM   8098  C  CB    . TYR   A  1  1096 ? -11.101 61.811  101.237 1.00 15.76 ? 1094 TYR   A CB    1 
ATOM   8099  C  CG    . TYR   A  1  1096 ? -10.404 62.500  102.379 1.00 16.15 ? 1094 TYR   A CG    1 
ATOM   8100  C  CD1   . TYR   A  1  1096 ? -10.746 63.794  102.760 1.00 17.09 ? 1094 TYR   A CD1   1 
ATOM   8101  C  CD2   . TYR   A  1  1096 ? -9.419  61.846  103.104 1.00 18.41 ? 1094 TYR   A CD2   1 
ATOM   8102  C  CE1   . TYR   A  1  1096 ? -10.111 64.416  103.827 1.00 15.98 ? 1094 TYR   A CE1   1 
ATOM   8103  C  CE2   . TYR   A  1  1096 ? -8.780  62.463  104.179 1.00 18.15 ? 1094 TYR   A CE2   1 
ATOM   8104  C  CZ    . TYR   A  1  1096 ? -9.127  63.742  104.529 1.00 16.31 ? 1094 TYR   A CZ    1 
ATOM   8105  O  OH    . TYR   A  1  1096 ? -8.514  64.348  105.605 1.00 17.44 ? 1094 TYR   A OH    1 
ATOM   8106  N  N     . THR   A  1  1097 ? -8.204  62.739  99.589  1.00 15.30 ? 1095 THR   A N     1 
ATOM   8107  C  CA    . THR   A  1  1097 ? -6.787  62.500  99.380  1.00 16.24 ? 1095 THR   A CA    1 
ATOM   8108  C  C     . THR   A  1  1097 ? -5.984  63.565  100.107 1.00 17.60 ? 1095 THR   A C     1 
ATOM   8109  O  O     . THR   A  1  1097 ? -6.447  64.690  100.318 1.00 17.67 ? 1095 THR   A O     1 
ATOM   8110  C  CB    . THR   A  1  1097 ? -6.435  62.560  97.888  1.00 21.06 ? 1095 THR   A CB    1 
ATOM   8111  O  OG1   . THR   A  1  1097 ? -6.815  63.833  97.356  1.00 23.44 ? 1095 THR   A OG1   1 
ATOM   8112  C  CG2   . THR   A  1  1097 ? -7.181  61.505  97.110  1.00 21.03 ? 1095 THR   A CG2   1 
ATOM   8113  N  N     . LEU   A  1  1098 ? -4.766  63.202  100.488 1.00 16.15 ? 1096 LEU   A N     1 
ATOM   8114  C  CA    . LEU   A  1  1098 ? -3.848  64.127  101.137 1.00 16.73 ? 1096 LEU   A CA    1 
ATOM   8115  C  C     . LEU   A  1  1098 ? -2.687  64.421  100.207 1.00 14.08 ? 1096 LEU   A C     1 
ATOM   8116  O  O     . LEU   A  1  1098 ? -1.977  63.504  99.767  1.00 15.28 ? 1096 LEU   A O     1 
ATOM   8117  C  CB    . LEU   A  1  1098 ? -3.336  63.574  102.461 1.00 15.55 ? 1096 LEU   A CB    1 
ATOM   8118  C  CG    . LEU   A  1  1098 ? -4.444  63.360  103.488 1.00 14.89 ? 1096 LEU   A CG    1 
ATOM   8119  C  CD1   . LEU   A  1  1098 ? -3.778  62.850  104.728 1.00 16.58 ? 1096 LEU   A CD1   1 
ATOM   8120  C  CD2   . LEU   A  1  1098 ? -5.220  64.637  103.787 1.00 16.43 ? 1096 LEU   A CD2   1 
ATOM   8121  N  N     . HIS   A  1  1099 ? -2.486  65.696  99.934  1.00 14.85 ? 1097 HIS   A N     1 
ATOM   8122  C  CA    . HIS   A  1  1099 ? -1.453  66.173  99.037  1.00 15.48 ? 1097 HIS   A CA    1 
ATOM   8123  C  C     . HIS   A  1  1099 ? -0.529  67.095  99.802  1.00 15.79 ? 1097 HIS   A C     1 
ATOM   8124  O  O     . HIS   A  1  1099 ? -0.787  67.461  100.943 1.00 16.62 ? 1097 HIS   A O     1 
ATOM   8125  C  CB    . HIS   A  1  1099 ? -2.088  66.983  97.904  1.00 18.09 ? 1097 HIS   A CB    1 
ATOM   8126  C  CG    . HIS   A  1  1099 ? -3.050  66.199  97.079  1.00 18.96 ? 1097 HIS   A CG    1 
ATOM   8127  N  ND1   . HIS   A  1  1099 ? -2.745  65.758  95.813  1.00 25.66 ? 1097 HIS   A ND1   1 
ATOM   8128  C  CD2   . HIS   A  1  1099 ? -4.298  65.751  97.350  1.00 21.04 ? 1097 HIS   A CD2   1 
ATOM   8129  C  CE1   . HIS   A  1  1099 ? -3.774  65.087  95.327  1.00 23.40 ? 1097 HIS   A CE1   1 
ATOM   8130  N  NE2   . HIS   A  1  1099 ? -4.731  65.074  96.237  1.00 22.28 ? 1097 HIS   A NE2   1 
ATOM   8131  N  N     . ALA   A  1  1100 ? 0.547   67.494  99.140  1.00 16.14 ? 1098 ALA   A N     1 
ATOM   8132  C  CA    . ALA   A  1  1100 ? 1.374   68.547  99.685  1.00 17.36 ? 1098 ALA   A CA    1 
ATOM   8133  C  C     . ALA   A  1  1100 ? 0.591   69.850  99.717  1.00 18.66 ? 1098 ALA   A C     1 
ATOM   8134  O  O     . ALA   A  1  1100 ? -0.313  70.082  98.908  1.00 18.75 ? 1098 ALA   A O     1 
ATOM   8135  C  CB    . ALA   A  1  1100 ? 2.615   68.714  98.815  1.00 18.35 ? 1098 ALA   A CB    1 
ATOM   8136  N  N     . ARG   A  1  1101 ? 0.932   70.699  100.680 1.00 18.49 ? 1099 ARG   A N     1 
ATOM   8137  C  CA    A ARG   A  1  1101 ? 0.328   72.025  100.740 0.58 18.70 ? 1099 ARG   A CA    1 
ATOM   8138  C  CA    B ARG   A  1  1101 ? 0.333   72.026  100.745 0.42 18.73 ? 1099 ARG   A CA    1 
ATOM   8139  C  C     . ARG   A  1  1101 ? 0.919   72.959  99.695  1.00 17.84 ? 1099 ARG   A C     1 
ATOM   8140  O  O     . ARG   A  1  1101 ? 0.190   73.748  99.088  1.00 18.95 ? 1099 ARG   A O     1 
ATOM   8141  C  CB    A ARG   A  1  1101 ? 0.509   72.636  102.128 0.58 21.03 ? 1099 ARG   A CB    1 
ATOM   8142  C  CB    B ARG   A  1  1101 ? 0.546   72.616  102.134 0.42 21.01 ? 1099 ARG   A CB    1 
ATOM   8143  C  CG    A ARG   A  1  1101 ? -0.181  71.881  103.240 0.58 20.41 ? 1099 ARG   A CG    1 
ATOM   8144  C  CG    B ARG   A  1  1101 ? -0.348  72.029  103.194 0.42 20.88 ? 1099 ARG   A CG    1 
ATOM   8145  C  CD    A ARG   A  1  1101 ? -0.054  72.593  104.576 0.58 18.77 ? 1099 ARG   A CD    1 
ATOM   8146  C  CD    B ARG   A  1  1101 ? -1.157  73.132  103.832 0.42 22.26 ? 1099 ARG   A CD    1 
ATOM   8147  N  NE    A ARG   A  1  1101 ? -0.900  73.772  104.713 0.58 17.99 ? 1099 ARG   A NE    1 
ATOM   8148  N  NE    B ARG   A  1  1101 ? -2.201  72.625  104.712 0.42 19.97 ? 1099 ARG   A NE    1 
ATOM   8149  C  CZ    A ARG   A  1  1101 ? -2.164  73.751  105.121 0.58 21.54 ? 1099 ARG   A CZ    1 
ATOM   8150  C  CZ    B ARG   A  1  1101 ? -2.895  73.383  105.549 0.42 21.94 ? 1099 ARG   A CZ    1 
ATOM   8151  N  NH1   A ARG   A  1  1101 ? -2.778  72.616  105.417 0.58 22.58 ? 1099 ARG   A NH1   1 
ATOM   8152  N  NH1   B ARG   A  1  1101 ? -2.681  74.687  105.642 0.42 20.18 ? 1099 ARG   A NH1   1 
ATOM   8153  N  NH2   A ARG   A  1  1101 ? -2.831  74.897  105.230 0.58 20.81 ? 1099 ARG   A NH2   1 
ATOM   8154  N  NH2   B ARG   A  1  1101 ? -3.818  72.819  106.317 0.42 20.55 ? 1099 ARG   A NH2   1 
ATOM   8155  N  N     . GLY   A  1  1102 ? 2.219   72.886  99.474  1.00 18.00 ? 1100 GLY   A N     1 
ATOM   8156  C  CA    . GLY   A  1  1102 ? 2.842   73.773  98.520  1.00 20.59 ? 1100 GLY   A CA    1 
ATOM   8157  C  C     . GLY   A  1  1102 ? 4.213   74.158  99.010  1.00 17.55 ? 1100 GLY   A C     1 
ATOM   8158  O  O     . GLY   A  1  1102 ? 5.032   73.281  99.299  1.00 19.03 ? 1100 GLY   A O     1 
ATOM   8159  N  N     . ARG   A  1  1103 ? 4.486   75.452  99.110  1.00 17.61 ? 1101 ARG   A N     1 
ATOM   8160  C  CA    . ARG   A  1  1103 ? 5.778   75.914  99.597  1.00 17.73 ? 1101 ARG   A CA    1 
ATOM   8161  C  C     . ARG   A  1  1103 ? 5.622   76.388  101.034 1.00 16.33 ? 1101 ARG   A C     1 
ATOM   8162  O  O     . ARG   A  1  1103 ? 4.811   77.280  101.320 1.00 18.08 ? 1101 ARG   A O     1 
ATOM   8163  C  CB    . ARG   A  1  1103 ? 6.356   77.017  98.711  1.00 19.52 ? 1101 ARG   A CB    1 
ATOM   8164  C  CG    . ARG   A  1  1103 ? 7.806   77.329  99.096  1.00 21.43 ? 1101 ARG   A CG    1 
ATOM   8165  C  CD    . ARG   A  1  1103 ? 8.530   78.198  98.079  1.00 24.05 ? 1101 ARG   A CD    1 
ATOM   8166  N  NE    . ARG   A  1  1103 ? 8.583   77.558  96.768  1.00 28.14 ? 1101 ARG   A NE    1 
ATOM   8167  C  CZ    . ARG   A  1  1103 ? 9.603   76.860  96.281  1.00 34.18 ? 1101 ARG   A CZ    1 
ATOM   8168  N  NH1   . ARG   A  1  1103 ? 10.718  76.650  96.981  1.00 26.34 ? 1101 ARG   A NH1   1 
ATOM   8169  N  NH2   . ARG   A  1  1103 ? 9.505   76.356  95.054  1.00 33.54 ? 1101 ARG   A NH2   1 
ATOM   8170  N  N     . ILE   A  1  1104 ? 6.361   75.762  101.933 1.00 16.43 ? 1102 ILE   A N     1 
ATOM   8171  C  CA    . ILE   A  1  1104 ? 6.292   76.075  103.353 1.00 15.87 ? 1102 ILE   A CA    1 
ATOM   8172  C  C     . ILE   A  1  1104 ? 7.424   77.033  103.670 1.00 16.77 ? 1102 ILE   A C     1 
ATOM   8173  O  O     . ILE   A  1  1104 ? 8.575   76.785  103.294 1.00 17.38 ? 1102 ILE   A O     1 
ATOM   8174  C  CB    . ILE   A  1  1104 ? 6.418   74.800  104.204 1.00 18.04 ? 1102 ILE   A CB    1 
ATOM   8175  C  CG1   . ILE   A  1  1104 ? 5.391   73.751  103.766 1.00 17.41 ? 1102 ILE   A CG1   1 
ATOM   8176  C  CG2   . ILE   A  1  1104 ? 6.278   75.121  105.688 1.00 16.94 ? 1102 ILE   A CG2   1 
ATOM   8177  C  CD1   . ILE   A  1  1104 ? 3.984   74.162  103.949 1.00 19.00 ? 1102 ILE   A CD1   1 
ATOM   8178  N  N     . LEU   A  1  1105 ? 7.100   78.128  104.352 1.00 16.87 ? 1103 LEU   A N     1 
ATOM   8179  C  CA    . LEU   A  1  1105 ? 8.119   79.029  104.867 1.00 17.40 ? 1103 LEU   A CA    1 
ATOM   8180  C  C     . LEU   A  1  1105 ? 8.757   78.408  106.103 1.00 16.75 ? 1103 LEU   A C     1 
ATOM   8181  O  O     . LEU   A  1  1105 ? 8.061   78.094  107.072 1.00 18.15 ? 1103 LEU   A O     1 
ATOM   8182  C  CB    . LEU   A  1  1105 ? 7.464   80.354  105.241 1.00 19.90 ? 1103 LEU   A CB    1 
ATOM   8183  C  CG    . LEU   A  1  1105 ? 8.386   81.399  105.871 1.00 20.51 ? 1103 LEU   A CG    1 
ATOM   8184  C  CD1   . LEU   A  1  1105 ? 9.492   81.790  104.897 1.00 22.68 ? 1103 LEU   A CD1   1 
ATOM   8185  C  CD2   . LEU   A  1  1105 ? 7.570   82.614  106.278 1.00 22.05 ? 1103 LEU   A CD2   1 
ATOM   8186  N  N     . LEU   A  1  1106 ? 10.070  78.241  106.083 1.00 15.96 ? 1104 LEU   A N     1 
ATOM   8187  C  CA    . LEU   A  1  1106 ? 10.808  77.748  107.237 1.00 17.39 ? 1104 LEU   A CA    1 
ATOM   8188  C  C     . LEU   A  1  1106 ? 11.553  78.906  107.867 1.00 20.63 ? 1104 LEU   A C     1 
ATOM   8189  O  O     . LEU   A  1  1106 ? 12.314  79.601  107.190 1.00 18.98 ? 1104 LEU   A O     1 
ATOM   8190  C  CB    . LEU   A  1  1106 ? 11.827  76.691  106.831 1.00 18.07 ? 1104 LEU   A CB    1 
ATOM   8191  C  CG    . LEU   A  1  1106 ? 11.312  75.453  106.121 1.00 23.52 ? 1104 LEU   A CG    1 
ATOM   8192  C  CD1   . LEU   A  1  1106 ? 12.344  74.343  106.181 1.00 20.28 ? 1104 LEU   A CD1   1 
ATOM   8193  C  CD2   . LEU   A  1  1106 ? 9.980   74.966  106.634 1.00 21.52 ? 1104 LEU   A CD2   1 
ATOM   8194  N  N     . VAL   A  1  1107 ? 11.342  79.100  109.159 1.00 18.60 ? 1105 VAL   A N     1 
ATOM   8195  C  CA    . VAL   A  1  1107 ? 12.033  80.146  109.899 1.00 19.48 ? 1105 VAL   A CA    1 
ATOM   8196  C  C     . VAL   A  1  1107 ? 12.802  79.437  111.005 1.00 19.41 ? 1105 VAL   A C     1 
ATOM   8197  O  O     . VAL   A  1  1107 ? 12.321  79.341  112.140 1.00 19.43 ? 1105 VAL   A O     1 
ATOM   8198  C  CB    . VAL   A  1  1107 ? 11.046  81.196  110.428 1.00 18.66 ? 1105 VAL   A CB    1 
ATOM   8199  C  CG1   . VAL   A  1  1107 ? 11.801  82.365  111.030 1.00 21.73 ? 1105 VAL   A CG1   1 
ATOM   8200  C  CG2   . VAL   A  1  1107 ? 10.132  81.669  109.291 1.00 20.84 ? 1105 VAL   A CG2   1 
ATOM   8201  N  N     . PRO   A  1  1108 ? 13.972  78.895  110.722 1.00 17.57 ? 1106 PRO   A N     1 
ATOM   8202  C  CA    . PRO   A  1  1108 ? 14.717  78.156  111.739 1.00 18.81 ? 1106 PRO   A CA    1 
ATOM   8203  C  C     . PRO   A  1  1108 ? 15.584  79.096  112.565 1.00 21.09 ? 1106 PRO   A C     1 
ATOM   8204  O  O     . PRO   A  1  1108 ? 15.818  80.249  112.204 1.00 22.96 ? 1106 PRO   A O     1 
ATOM   8205  C  CB    . PRO   A  1  1108 ? 15.616  77.255  110.892 1.00 20.99 ? 1106 PRO   A CB    1 
ATOM   8206  C  CG    . PRO   A  1  1108 ? 15.901  78.093  109.683 1.00 20.98 ? 1106 PRO   A CG    1 
ATOM   8207  C  CD    . PRO   A  1  1108 ? 14.604  78.808  109.392 1.00 21.31 ? 1106 PRO   A CD    1 
ATOM   8208  N  N     . ALA   A  1  1109 ? 16.043  78.571  113.692 1.00 19.14 ? 1107 ALA   A N     1 
ATOM   8209  C  CA    . ALA   A  1  1109 ? 17.028  79.235  114.530 1.00 20.67 ? 1107 ALA   A CA    1 
ATOM   8210  C  C     . ALA   A  1  1109 ? 18.334  78.470  114.642 1.00 23.84 ? 1107 ALA   A C     1 
ATOM   8211  O  O     . ALA   A  1  1109 ? 19.391  79.088  114.812 1.00 26.54 ? 1107 ALA   A O     1 
ATOM   8212  C  CB    . ALA   A  1  1109 ? 16.465  79.452  115.946 1.00 22.07 ? 1107 ALA   A CB    1 
ATOM   8213  N  N     . THR   A  1  1110 ? 18.292  77.144  114.592 1.00 20.74 ? 1108 THR   A N     1 
ATOM   8214  C  CA    . THR   A  1  1110 ? 19.461  76.304  114.760 1.00 20.63 ? 1108 THR   A CA    1 
ATOM   8215  C  C     . THR   A  1  1110 ? 19.530  75.320  113.605 1.00 20.46 ? 1108 THR   A C     1 
ATOM   8216  O  O     . THR   A  1  1110 ? 18.531  75.024  112.944 1.00 19.77 ? 1108 THR   A O     1 
ATOM   8217  C  CB    . THR   A  1  1110 ? 19.425  75.510  116.072 1.00 22.48 ? 1108 THR   A CB    1 
ATOM   8218  O  OG1   . THR   A  1  1110 ? 18.331  74.586  116.043 1.00 21.46 ? 1108 THR   A OG1   1 
ATOM   8219  C  CG2   . THR   A  1  1110 ? 19.250  76.441  117.256 1.00 21.76 ? 1108 THR   A CG2   1 
ATOM   8220  N  N     . GLU   A  1  1111 ? 20.730  74.798  113.384 1.00 21.10 ? 1109 GLU   A N     1 
ATOM   8221  C  CA    . GLU   A  1  1111 ? 20.916  73.801  112.339 1.00 21.26 ? 1109 GLU   A CA    1 
ATOM   8222  C  C     . GLU   A  1  1111 ? 20.020  72.590  112.563 1.00 20.70 ? 1109 GLU   A C     1 
ATOM   8223  O  O     . GLU   A  1  1111 ? 19.342  72.131  111.634 1.00 19.78 ? 1109 GLU   A O     1 
ATOM   8224  C  CB    . GLU   A  1  1111 ? 22.375  73.383  112.292 1.00 23.28 ? 1109 GLU   A CB    1 
ATOM   8225  C  CG    . GLU   A  1  1111 ? 22.603  72.201  111.382 1.00 23.62 ? 1109 GLU   A CG    1 
ATOM   8226  C  CD    . GLU   A  1  1111 ? 24.069  71.895  111.207 1.00 27.39 ? 1109 GLU   A CD    1 
ATOM   8227  O  OE1   . GLU   A  1  1111 ? 24.755  72.720  110.569 1.00 28.00 ? 1109 GLU   A OE1   1 
ATOM   8228  O  OE2   . GLU   A  1  1111 ? 24.525  70.843  111.697 1.00 30.55 ? 1109 GLU   A OE2   1 
ATOM   8229  N  N     . SER   A  1  1112 ? 19.993  72.055  113.786 1.00 20.71 ? 1110 SER   A N     1 
ATOM   8230  C  CA    . SER   A  1  1112 ? 19.134  70.903  114.052 1.00 19.92 ? 1110 SER   A CA    1 
ATOM   8231  C  C     . SER   A  1  1112 ? 17.673  71.254  113.842 1.00 21.13 ? 1110 SER   A C     1 
ATOM   8232  O  O     . SER   A  1  1112 ? 16.912  70.461  113.275 1.00 20.23 ? 1110 SER   A O     1 
ATOM   8233  C  CB    . SER   A  1  1112 ? 19.357  70.363  115.459 1.00 23.52 ? 1110 SER   A CB    1 
ATOM   8234  O  OG    . SER   A  1  1112 ? 18.574  69.198  115.650 1.00 23.53 ? 1110 SER   A OG    1 
ATOM   8235  N  N     . GLY   A  1  1113 ? 17.268  72.449  114.272 1.00 19.50 ? 1111 GLY   A N     1 
ATOM   8236  C  CA    . GLY   A  1  1113 ? 15.907  72.886  114.016 1.00 17.36 ? 1111 GLY   A CA    1 
ATOM   8237  C  C     . GLY   A  1  1113 ? 15.597  72.952  112.536 1.00 17.60 ? 1111 GLY   A C     1 
ATOM   8238  O  O     . GLY   A  1  1113 ? 14.539  72.499  112.093 1.00 17.89 ? 1111 GLY   A O     1 
ATOM   8239  N  N     . LEU   A  1  1114 ? 16.524  73.496  111.748 1.00 19.23 ? 1112 LEU   A N     1 
ATOM   8240  C  CA    . LEU   A  1  1114 ? 16.332  73.539  110.302 1.00 18.60 ? 1112 LEU   A CA    1 
ATOM   8241  C  C     . LEU   A  1  1114 ? 16.175  72.142  109.727 1.00 17.48 ? 1112 LEU   A C     1 
ATOM   8242  O  O     . LEU   A  1  1114 ? 15.287  71.911  108.900 1.00 17.02 ? 1112 LEU   A O     1 
ATOM   8243  C  CB    . LEU   A  1  1114 ? 17.502  74.257  109.627 1.00 20.30 ? 1112 LEU   A CB    1 
ATOM   8244  C  CG    . LEU   A  1  1114 ? 17.476  74.209  108.102 1.00 20.58 ? 1112 LEU   A CG    1 
ATOM   8245  C  CD1   . LEU   A  1  1114 ? 16.164  74.775  107.577 1.00 21.95 ? 1112 LEU   A CD1   1 
ATOM   8246  C  CD2   . LEU   A  1  1114 ? 18.662  74.973  107.528 1.00 21.79 ? 1112 LEU   A CD2   1 
ATOM   8247  N  N     . TYR   A  1  1115 ? 17.011  71.201  110.160 1.00 18.17 ? 1113 TYR   A N     1 
ATOM   8248  C  CA    . TYR   A  1  1115 ? 16.919  69.848  109.625 1.00 18.58 ? 1113 TYR   A CA    1 
ATOM   8249  C  C     . TYR   A  1  1115 ? 15.583  69.212  109.986 1.00 17.48 ? 1113 TYR   A C     1 
ATOM   8250  O  O     . TYR   A  1  1115 ? 14.982  68.517  109.161 1.00 17.87 ? 1113 TYR   A O     1 
ATOM   8251  C  CB    . TYR   A  1  1115 ? 18.072  68.992  110.136 1.00 18.15 ? 1113 TYR   A CB    1 
ATOM   8252  C  CG    . TYR   A  1  1115 ? 19.441  69.397  109.637 1.00 18.47 ? 1113 TYR   A CG    1 
ATOM   8253  C  CD1   . TYR   A  1  1115 ? 19.593  70.246  108.554 1.00 17.95 ? 1113 TYR   A CD1   1 
ATOM   8254  C  CD2   . TYR   A  1  1115 ? 20.578  68.931  110.267 1.00 20.91 ? 1113 TYR   A CD2   1 
ATOM   8255  C  CE1   . TYR   A  1  1115 ? 20.860  70.605  108.091 1.00 21.56 ? 1113 TYR   A CE1   1 
ATOM   8256  C  CE2   . TYR   A  1  1115 ? 21.838  69.280  109.815 1.00 20.74 ? 1113 TYR   A CE2   1 
ATOM   8257  C  CZ    . TYR   A  1  1115 ? 21.962  70.120  108.725 1.00 23.96 ? 1113 TYR   A CZ    1 
ATOM   8258  O  OH    . TYR   A  1  1115 ? 23.218  70.485  108.280 1.00 23.68 ? 1113 TYR   A OH    1 
ATOM   8259  N  N     . HIS   A  1  1116 ? 15.092  69.452  111.200 1.00 18.14 ? 1114 HIS   A N     1 
ATOM   8260  C  CA    . HIS   A  1  1116 ? 13.791  68.921  111.593 1.00 18.02 ? 1114 HIS   A CA    1 
ATOM   8261  C  C     . HIS   A  1  1116 ? 12.666  69.584  110.811 1.00 17.40 ? 1114 HIS   A C     1 
ATOM   8262  O  O     . HIS   A  1  1116 ? 11.699  68.920  110.413 1.00 17.33 ? 1114 HIS   A O     1 
ATOM   8263  C  CB    . HIS   A  1  1116 ? 13.573  69.126  113.088 1.00 19.71 ? 1114 HIS   A CB    1 
ATOM   8264  C  CG    . HIS   A  1  1116 ? 14.200  68.072  113.942 1.00 19.17 ? 1114 HIS   A CG    1 
ATOM   8265  N  ND1   . HIS   A  1  1116 ? 15.497  68.152  114.406 1.00 22.86 ? 1114 HIS   A ND1   1 
ATOM   8266  C  CD2   . HIS   A  1  1116 ? 13.696  66.915  114.428 1.00 21.43 ? 1114 HIS   A CD2   1 
ATOM   8267  C  CE1   . HIS   A  1  1116 ? 15.760  67.087  115.145 1.00 22.33 ? 1114 HIS   A CE1   1 
ATOM   8268  N  NE2   . HIS   A  1  1116 ? 14.686  66.321  115.171 1.00 25.37 ? 1114 HIS   A NE2   1 
ATOM   8269  N  N     . GLN   A  1  1117 ? 12.753  70.897  110.604 1.00 17.03 ? 1115 GLN   A N     1 
ATOM   8270  C  CA    . GLN   A  1  1117 ? 11.725  71.575  109.829 1.00 17.42 ? 1115 GLN   A CA    1 
ATOM   8271  C  C     . GLN   A  1  1117 ? 11.716  71.058  108.405 1.00 15.47 ? 1115 GLN   A C     1 
ATOM   8272  O  O     . GLN   A  1  1117 ? 10.655  70.804  107.827 1.00 15.87 ? 1115 GLN   A O     1 
ATOM   8273  C  CB    . GLN   A  1  1117 ? 11.984  73.075  109.809 1.00 16.91 ? 1115 GLN   A CB    1 
ATOM   8274  C  CG    . GLN   A  1  1117 ? 11.814  73.753  111.134 1.00 18.25 ? 1115 GLN   A CG    1 
ATOM   8275  C  CD    . GLN   A  1  1117 ? 12.052  75.236  111.033 1.00 22.22 ? 1115 GLN   A CD    1 
ATOM   8276  O  OE1   . GLN   A  1  1117 ? 12.613  75.722  110.045 1.00 19.80 ? 1115 GLN   A OE1   1 
ATOM   8277  N  NE2   . GLN   A  1  1117 ? 11.635  75.970  112.055 1.00 18.47 ? 1115 GLN   A NE2   1 
ATOM   8278  N  N     . LEU   A  1  1118 ? 12.901  70.914  107.812 1.00 16.00 ? 1116 LEU   A N     1 
ATOM   8279  C  CA    A LEU   A  1  1118 ? 12.969  70.445  106.437 0.53 16.93 ? 1116 LEU   A CA    1 
ATOM   8280  C  CA    B LEU   A  1  1118 ? 12.994  70.427  106.439 0.47 16.95 ? 1116 LEU   A CA    1 
ATOM   8281  C  C     . LEU   A  1  1118 ? 12.444  69.020  106.323 1.00 16.44 ? 1116 LEU   A C     1 
ATOM   8282  O  O     . LEU   A  1  1118 ? 11.717  68.700  105.372 1.00 16.56 ? 1116 LEU   A O     1 
ATOM   8283  C  CB    A LEU   A  1  1118 ? 14.403  70.574  105.922 0.53 18.04 ? 1116 LEU   A CB    1 
ATOM   8284  C  CB    B LEU   A  1  1118 ? 14.453  70.432  105.993 0.47 18.14 ? 1116 LEU   A CB    1 
ATOM   8285  C  CG    A LEU   A  1  1118 ? 14.676  70.381  104.435 0.53 17.92 ? 1116 LEU   A CG    1 
ATOM   8286  C  CG    B LEU   A  1  1118 ? 15.014  71.766  105.542 0.47 18.58 ? 1116 LEU   A CG    1 
ATOM   8287  C  CD1   A LEU   A  1  1118 ? 13.696  71.173  103.584 0.53 18.49 ? 1116 LEU   A CD1   1 
ATOM   8288  C  CD1   B LEU   A  1  1118 ? 16.503  71.617  105.368 0.47 17.26 ? 1116 LEU   A CD1   1 
ATOM   8289  C  CD2   A LEU   A  1  1118 ? 16.107  70.823  104.161 0.53 19.98 ? 1116 LEU   A CD2   1 
ATOM   8290  C  CD2   B LEU   A  1  1118 ? 14.362  72.171  104.241 0.47 19.19 ? 1116 LEU   A CD2   1 
ATOM   8291  N  N     . ALA   A  1  1119 ? 12.774  68.166  107.287 1.00 17.06 ? 1117 ALA   A N     1 
ATOM   8292  C  CA    . ALA   A  1  1119 ? 12.269  66.798  107.254 1.00 18.35 ? 1117 ALA   A CA    1 
ATOM   8293  C  C     . ALA   A  1  1119 ? 10.754  66.787  107.300 1.00 18.04 ? 1117 ALA   A C     1 
ATOM   8294  O  O     . ALA   A  1  1119 ? 10.110  66.065  106.533 1.00 17.60 ? 1117 ALA   A O     1 
ATOM   8295  C  CB    . ALA   A  1  1119 ? 12.837  65.989  108.413 1.00 20.04 ? 1117 ALA   A CB    1 
ATOM   8296  N  N     . ALA   A  1  1120 ? 10.165  67.600  108.177 1.00 16.71 ? 1118 ALA   A N     1 
ATOM   8297  C  CA    . ALA   A  1  1120 ? 8.708   67.635  108.291 1.00 16.10 ? 1118 ALA   A CA    1 
ATOM   8298  C  C     . ALA   A  1  1120 ? 8.080   68.091  106.988 1.00 16.26 ? 1118 ALA   A C     1 
ATOM   8299  O  O     . ALA   A  1  1120 ? 7.125   67.479  106.488 1.00 16.44 ? 1118 ALA   A O     1 
ATOM   8300  C  CB    . ALA   A  1  1120 ? 8.298   68.575  109.422 1.00 16.33 ? 1118 ALA   A CB    1 
ATOM   8301  N  N     . ALA   A  1  1121 ? 8.627   69.152  106.403 1.00 15.81 ? 1119 ALA   A N     1 
ATOM   8302  C  CA    . ALA   A  1  1121 ? 8.066   69.699  105.176 1.00 16.53 ? 1119 ALA   A CA    1 
ATOM   8303  C  C     . ALA   A  1  1121 ? 8.262   68.758  103.996 1.00 15.13 ? 1119 ALA   A C     1 
ATOM   8304  O  O     . ALA   A  1  1121 ? 7.350   68.582  103.177 1.00 15.79 ? 1119 ALA   A O     1 
ATOM   8305  C  CB    . ALA   A  1  1121 ? 8.707   71.056  104.886 1.00 18.06 ? 1119 ALA   A CB    1 
ATOM   8306  N  N     . LEU   A  1  1122 ? 9.454   68.174  103.866 1.00 15.54 ? 1120 LEU   A N     1 
ATOM   8307  C  CA    . LEU   A  1  1122 ? 9.705   67.283  102.737 1.00 14.92 ? 1120 LEU   A CA    1 
ATOM   8308  C  C     . LEU   A  1  1122 ? 8.894   66.002  102.860 1.00 15.32 ? 1120 LEU   A C     1 
ATOM   8309  O  O     . LEU   A  1  1122 ? 8.402   65.479  101.857 1.00 15.00 ? 1120 LEU   A O     1 
ATOM   8310  C  CB    . LEU   A  1  1122 ? 11.189  66.950  102.623 1.00 17.10 ? 1120 LEU   A CB    1 
ATOM   8311  C  CG    . LEU   A  1  1122 ? 12.102  68.133  102.323 1.00 16.58 ? 1120 LEU   A CG    1 
ATOM   8312  C  CD1   . LEU   A  1  1122 ? 13.523  67.651  102.366 1.00 17.74 ? 1120 LEU   A CD1   1 
ATOM   8313  C  CD2   . LEU   A  1  1122 ? 11.745  68.781  100.975 1.00 17.81 ? 1120 LEU   A CD2   1 
ATOM   8314  N  N     . ALA   A  1  1123 ? 8.756   65.479  104.081 1.00 15.50 ? 1121 ALA   A N     1 
ATOM   8315  C  CA    . ALA   A  1  1123 ? 8.011   64.243  104.287 1.00 15.67 ? 1121 ALA   A CA    1 
ATOM   8316  C  C     . ALA   A  1  1123 ? 6.563   64.398  103.877 1.00 16.01 ? 1121 ALA   A C     1 
ATOM   8317  O  O     . ALA   A  1  1123 ? 5.907   63.401  103.579 1.00 16.08 ? 1121 ALA   A O     1 
ATOM   8318  C  CB    . ALA   A  1  1123 ? 8.052   63.826  105.763 1.00 15.53 ? 1121 ALA   A CB    1 
ATOM   8319  N  N     . THR   A  1  1124 ? 6.052   65.625  103.887 1.00 14.14 ? 1122 THR   A N     1 
ATOM   8320  C  CA    . THR   A  1  1124 ? 4.681   65.913  103.501 1.00 14.40 ? 1122 THR   A CA    1 
ATOM   8321  C  C     . THR   A  1  1124 ? 4.597   66.473  102.090 1.00 14.34 ? 1122 THR   A C     1 
ATOM   8322  O  O     . THR   A  1  1124 ? 3.552   66.997  101.688 1.00 16.09 ? 1122 THR   A O     1 
ATOM   8323  C  CB    . THR   A  1  1124 ? 4.034   66.823  104.543 1.00 15.07 ? 1122 THR   A CB    1 
ATOM   8324  O  OG1   . THR   A  1  1124 ? 4.930   67.901  104.846 1.00 15.34 ? 1122 THR   A OG1   1 
ATOM   8325  C  CG2   . THR   A  1  1124 ? 3.768   66.027  105.823 1.00 17.01 ? 1122 THR   A CG2   1 
ATOM   8326  N  N     . GLY   A  1  1125 ? 5.671   66.319  101.312 1.00 14.19 ? 1123 GLY   A N     1 
ATOM   8327  C  CA    . GLY   A  1  1125 ? 5.666   66.584  99.885  1.00 16.54 ? 1123 GLY   A CA    1 
ATOM   8328  C  C     . GLY   A  1  1125 ? 5.881   68.024  99.491  1.00 15.76 ? 1123 GLY   A C     1 
ATOM   8329  O  O     . GLY   A  1  1125 ? 5.767   68.352  98.301  1.00 16.61 ? 1123 GLY   A O     1 
ATOM   8330  N  N     . ASN   A  1  1126 ? 6.179   68.895  100.447 1.00 15.29 ? 1124 ASN   A N     1 
ATOM   8331  C  CA    . ASN   A  1  1126 ? 6.238   70.318  100.170 1.00 15.64 ? 1124 ASN   A CA    1 
ATOM   8332  C  C     . ASN   A  1  1126 ? 7.612   70.733  99.695  1.00 15.31 ? 1124 ASN   A C     1 
ATOM   8333  O  O     . ASN   A  1  1126 ? 8.617   70.056  99.932  1.00 17.05 ? 1124 ASN   A O     1 
ATOM   8334  C  CB    . ASN   A  1  1126 ? 5.961   71.088  101.456 1.00 15.96 ? 1124 ASN   A CB    1 
ATOM   8335  C  CG    . ASN   A  1  1126 ? 4.590   70.808  101.983 1.00 16.54 ? 1124 ASN   A CG    1 
ATOM   8336  O  OD1   . ASN   A  1  1126 ? 3.606   71.190  101.377 1.00 16.94 ? 1124 ASN   A OD1   1 
ATOM   8337  N  ND2   . ASN   A  1  1126 ? 4.515   70.105  103.094 1.00 15.66 ? 1124 ASN   A ND2   1 
ATOM   8338  N  N     . SER   A  1  1127 ? 7.641   71.883  99.032  1.00 17.01 ? 1125 SER   A N     1 
ATOM   8339  C  CA    . SER   A  1  1127 ? 8.885   72.619  98.884  1.00 17.85 ? 1125 SER   A CA    1 
ATOM   8340  C  C     . SER   A  1  1127 ? 8.982   73.604  100.036 1.00 17.01 ? 1125 SER   A C     1 
ATOM   8341  O  O     . SER   A  1  1127 ? 8.052   73.761  100.827 1.00 17.29 ? 1125 SER   A O     1 
ATOM   8342  C  CB    . SER   A  1  1127 ? 8.923   73.368  97.553  1.00 18.66 ? 1125 SER   A CB    1 
ATOM   8343  O  OG    . SER   A  1  1127 ? 7.857   74.290  97.457  1.00 23.31 ? 1125 SER   A OG    1 
ATOM   8344  N  N     . VAL   A  1  1128 ? 10.124  74.272  100.144 1.00 18.28 ? 1126 VAL   A N     1 
ATOM   8345  C  CA    . VAL   A  1  1128 ? 10.344  75.181  101.259 1.00 18.85 ? 1126 VAL   A CA    1 
ATOM   8346  C  C     . VAL   A  1  1128 ? 11.019  76.446  100.777 1.00 18.27 ? 1126 VAL   A C     1 
ATOM   8347  O  O     . VAL   A  1  1128 ? 11.774  76.443  99.801  1.00 20.34 ? 1126 VAL   A O     1 
ATOM   8348  C  CB    . VAL   A  1  1128 ? 11.180  74.552  102.392 1.00 18.57 ? 1126 VAL   A CB    1 
ATOM   8349  C  CG1   . VAL   A  1  1128 ? 10.508  73.315  102.931 1.00 19.00 ? 1126 VAL   A CG1   1 
ATOM   8350  C  CG2   . VAL   A  1  1128 ? 12.596  74.243  101.894 1.00 19.91 ? 1126 VAL   A CG2   1 
ATOM   8351  N  N     . ALA   A  1  1129 ? 10.746  77.535  101.483 1.00 17.02 ? 1127 ALA   A N     1 
ATOM   8352  C  CA    . ALA   A  1  1129 ? 11.553  78.741  101.406 1.00 19.79 ? 1127 ALA   A CA    1 
ATOM   8353  C  C     . ALA   A  1  1129 ? 12.108  78.972  102.800 1.00 17.49 ? 1127 ALA   A C     1 
ATOM   8354  O  O     . ALA   A  1  1129 ? 11.341  79.145  103.755 1.00 20.44 ? 1127 ALA   A O     1 
ATOM   8355  C  CB    . ALA   A  1  1129 ? 10.718  79.940  100.964 1.00 24.31 ? 1127 ALA   A CB    1 
ATOM   8356  N  N     . ILE   A  1  1130 ? 13.426  78.959  102.918 1.00 17.64 ? 1128 ILE   A N     1 
ATOM   8357  C  CA    . ILE   A  1  1130 ? 14.086  79.072  104.211 1.00 18.31 ? 1128 ILE   A CA    1 
ATOM   8358  C  C     . ILE   A  1  1130 ? 14.490  80.518  104.425 1.00 24.11 ? 1128 ILE   A C     1 
ATOM   8359  O  O     . ILE   A  1  1130 ? 15.104  81.138  103.550 1.00 21.98 ? 1128 ILE   A O     1 
ATOM   8360  C  CB    . ILE   A  1  1130 ? 15.314  78.157  104.304 1.00 17.79 ? 1128 ILE   A CB    1 
ATOM   8361  C  CG1   . ILE   A  1  1130 ? 14.938  76.735  103.899 1.00 20.78 ? 1128 ILE   A CG1   1 
ATOM   8362  C  CG2   . ILE   A  1  1130 ? 15.872  78.179  105.723 1.00 20.74 ? 1128 ILE   A CG2   1 
ATOM   8363  C  CD1   . ILE   A  1  1130 ? 16.145  75.864  103.712 1.00 20.65 ? 1128 ILE   A CD1   1 
ATOM   8364  N  N     . ASP   A  1  1131 ? 14.163  81.044  105.597 1.00 21.31 ? 1129 ASP   A N     1 
ATOM   8365  C  CA    . ASP   A  1  1131 ? 14.548  82.399  105.959 1.00 21.93 ? 1129 ASP   A CA    1 
ATOM   8366  C  C     . ASP   A  1  1131 ? 16.056  82.582  105.850 1.00 22.59 ? 1129 ASP   A C     1 
ATOM   8367  O  O     . ASP   A  1  1131 ? 16.814  81.983  106.614 1.00 21.73 ? 1129 ASP   A O     1 
ATOM   8368  C  CB    . ASP   A  1  1131 ? 14.122  82.675  107.396 1.00 20.06 ? 1129 ASP   A CB    1 
ATOM   8369  C  CG    . ASP   A  1  1131 ? 14.483  84.055  107.843 1.00 27.41 ? 1129 ASP   A CG    1 
ATOM   8370  O  OD1   . ASP   A  1  1131 ? 14.585  84.943  106.974 1.00 22.96 ? 1129 ASP   A OD1   1 
ATOM   8371  O  OD2   . ASP   A  1  1131 ? 14.678  84.246  109.054 1.00 24.51 ? 1129 ASP   A OD2   1 
ATOM   8372  N  N     . ALA   A  1  1132 ? 16.499  83.428  104.920 1.00 23.39 ? 1130 ALA   A N     1 
ATOM   8373  C  CA    . ALA   A  1  1132 ? 17.928  83.661  104.763 1.00 25.92 ? 1130 ALA   A CA    1 
ATOM   8374  C  C     . ALA   A  1  1132 ? 18.522  84.409  105.943 1.00 28.39 ? 1130 ALA   A C     1 
ATOM   8375  O  O     . ALA   A  1  1132 ? 19.725  84.288  106.193 1.00 29.02 ? 1130 ALA   A O     1 
ATOM   8376  C  CB    . ALA   A  1  1132 ? 18.199  84.418  103.461 1.00 28.21 ? 1130 ALA   A CB    1 
ATOM   8377  N  N     . ALA   A  1  1133 ? 17.706  85.162  106.684 1.00 23.99 ? 1131 ALA   A N     1 
ATOM   8378  C  CA    . ALA   A  1  1133 ? 18.207  85.889  107.844 1.00 25.76 ? 1131 ALA   A CA    1 
ATOM   8379  C  C     . ALA   A  1  1133 ? 18.599  84.964  108.986 1.00 26.49 ? 1131 ALA   A C     1 
ATOM   8380  O  O     . ALA   A  1  1133 ? 19.197  85.426  109.959 1.00 30.37 ? 1131 ALA   A O     1 
ATOM   8381  C  CB    . ALA   A  1  1133 ? 17.180  86.919  108.321 1.00 27.86 ? 1131 ALA   A CB    1 
ATOM   8382  N  N     . SER   A  1  1134 ? 18.282  83.674  108.890 1.00 27.37 ? 1132 SER   A N     1 
ATOM   8383  C  CA    . SER   A  1  1134 ? 18.698  82.719  109.900 1.00 24.86 ? 1132 SER   A CA    1 
ATOM   8384  C  C     . SER   A  1  1134 ? 20.201  82.510  109.900 1.00 24.51 ? 1132 SER   A C     1 
ATOM   8385  O  O     . SER   A  1  1134 ? 20.744  82.023  110.896 1.00 25.79 ? 1132 SER   A O     1 
ATOM   8386  C  CB    . SER   A  1  1134 ? 18.039  81.368  109.620 1.00 24.05 ? 1132 SER   A CB    1 
ATOM   8387  O  OG    . SER   A  1  1134 ? 18.540  80.799  108.410 1.00 23.99 ? 1132 SER   A OG    1 
ATOM   8388  N  N     . GLY   A  1  1135 ? 20.868  82.836  108.794 1.00 26.82 ? 1133 GLY   A N     1 
ATOM   8389  C  CA    . GLY   A  1  1135 ? 22.292  82.614  108.679 1.00 25.29 ? 1133 GLY   A CA    1 
ATOM   8390  C  C     . GLY   A  1  1135 ? 22.697  81.163  108.609 1.00 28.56 ? 1133 GLY   A C     1 
ATOM   8391  O  O     . GLY   A  1  1135 ? 23.862  80.844  108.849 1.00 29.22 ? 1133 GLY   A O     1 
ATOM   8392  N  N     . LEU   A  1  1136 ? 21.770  80.264  108.280 1.00 23.95 ? 1134 LEU   A N     1 
ATOM   8393  C  CA    . LEU   A  1  1136 ? 22.049  78.836  108.319 1.00 25.84 ? 1134 LEU   A CA    1 
ATOM   8394  C  C     . LEU   A  1  1136 ? 22.403  78.263  106.949 1.00 23.77 ? 1134 LEU   A C     1 
ATOM   8395  O  O     . LEU   A  1  1136 ? 22.413  77.037  106.782 1.00 24.35 ? 1134 LEU   A O     1 
ATOM   8396  C  CB    . LEU   A  1  1136 ? 20.881  78.082  108.954 1.00 25.65 ? 1134 LEU   A CB    1 
ATOM   8397  C  CG    . LEU   A  1  1136 ? 20.637  78.383  110.433 1.00 23.76 ? 1134 LEU   A CG    1 
ATOM   8398  C  CD1   . LEU   A  1  1136 ? 19.322  77.752  110.890 1.00 23.84 ? 1134 LEU   A CD1   1 
ATOM   8399  C  CD2   . LEU   A  1  1136 ? 21.787  77.857  111.250 1.00 25.13 ? 1134 LEU   A CD2   1 
ATOM   8400  N  N     . GLN   A  1  1137 ? 22.720  79.127  105.977 1.00 25.05 ? 1135 GLN   A N     1 
ATOM   8401  C  CA    . GLN   A  1  1137 ? 23.031  78.662  104.626 1.00 27.89 ? 1135 GLN   A CA    1 
ATOM   8402  C  C     . GLN   A  1  1137 ? 24.092  77.564  104.622 1.00 25.10 ? 1135 GLN   A C     1 
ATOM   8403  O  O     . GLN   A  1  1137 ? 23.969  76.581  103.880 1.00 25.80 ? 1135 GLN   A O     1 
ATOM   8404  C  CB    . GLN   A  1  1137 ? 23.460  79.833  103.735 1.00 28.44 ? 1135 GLN   A CB    1 
ATOM   8405  C  CG    . GLN   A  1  1137 ? 22.326  80.737  103.271 1.00 26.41 ? 1135 GLN   A CG    1 
ATOM   8406  C  CD    . GLN   A  1  1137 ? 21.961  81.790  104.302 1.00 26.91 ? 1135 GLN   A CD    1 
ATOM   8407  O  OE1   . GLN   A  1  1137 ? 22.411  81.737  105.445 1.00 29.56 ? 1135 GLN   A OE1   1 
ATOM   8408  N  NE2   . GLN   A  1  1137 ? 21.149  82.756  103.895 1.00 31.60 ? 1135 GLN   A NE2   1 
ATOM   8409  N  N     . ALA   A  1  1138 ? 25.133  77.698  105.452 1.00 26.35 ? 1136 ALA   A N     1 
ATOM   8410  C  CA    . ALA   A  1  1138 ? 26.208  76.709  105.457 1.00 26.69 ? 1136 ALA   A CA    1 
ATOM   8411  C  C     . ALA   A  1  1138 ? 25.777  75.348  105.987 1.00 30.61 ? 1136 ALA   A C     1 
ATOM   8412  O  O     . ALA   A  1  1138 ? 26.533  74.381  105.846 1.00 32.42 ? 1136 ALA   A O     1 
ATOM   8413  C  CB    . ALA   A  1  1138 ? 27.417  77.214  106.255 1.00 28.73 ? 1136 ALA   A CB    1 
ATOM   8414  N  N     . SER   A  1  1139 ? 24.588  75.242  106.585 1.00 27.28 ? 1137 SER   A N     1 
ATOM   8415  C  CA    . SER   A  1  1139 ? 24.109  73.956  107.069 1.00 25.74 ? 1137 SER   A CA    1 
ATOM   8416  C  C     . SER   A  1  1139 ? 23.520  73.092  105.964 1.00 24.57 ? 1137 SER   A C     1 
ATOM   8417  O  O     . SER   A  1  1139 ? 23.253  71.912  106.208 1.00 27.81 ? 1137 SER   A O     1 
ATOM   8418  C  CB    . SER   A  1  1139 ? 23.050  74.168  108.157 1.00 25.08 ? 1137 SER   A CB    1 
ATOM   8419  O  OG    . SER   A  1  1139 ? 23.620  74.727  109.326 1.00 29.41 ? 1137 SER   A OG    1 
ATOM   8420  N  N     . LEU   A  1  1140 ? 23.302  73.645  104.776 1.00 24.90 ? 1138 LEU   A N     1 
ATOM   8421  C  CA    . LEU   A  1  1140 ? 22.655  72.931  103.682 1.00 25.49 ? 1138 LEU   A CA    1 
ATOM   8422  C  C     . LEU   A  1  1140 ? 23.549  72.856  102.456 1.00 26.42 ? 1138 LEU   A C     1 
ATOM   8423  O  O     . LEU   A  1  1140 ? 23.088  73.016  101.326 1.00 32.13 ? 1138 LEU   A O     1 
ATOM   8424  C  CB    . LEU   A  1  1140 ? 21.314  73.560  103.309 1.00 30.05 ? 1138 LEU   A CB    1 
ATOM   8425  C  CG    . LEU   A  1  1140 ? 20.090  73.252  104.162 1.00 32.85 ? 1138 LEU   A CG    1 
ATOM   8426  C  CD1   . LEU   A  1  1140 ? 18.862  73.647  103.365 1.00 29.64 ? 1138 LEU   A CD1   1 
ATOM   8427  C  CD2   . LEU   A  1  1140 ? 20.022  71.788  104.585 1.00 25.73 ? 1138 LEU   A CD2   1 
ATOM   8428  N  N     . LYS   A  1  1141 ? 24.836  72.616  102.666 1.00 27.59 ? 1139 LYS   A N     1 
ATOM   8429  C  CA    . LYS   A  1  1141 ? 25.772  72.530  101.554 1.00 34.99 ? 1139 LYS   A CA    1 
ATOM   8430  C  C     . LYS   A  1  1141 ? 25.671  71.173  100.864 1.00 29.45 ? 1139 LYS   A C     1 
ATOM   8431  O  O     . LYS   A  1  1141 ? 25.481  70.139  101.510 1.00 29.94 ? 1139 LYS   A O     1 
ATOM   8432  C  CB    . LYS   A  1  1141 ? 27.200  72.751  102.053 1.00 33.18 ? 1139 LYS   A CB    1 
ATOM   8433  N  N     . ASN   A  1  1142 ? 25.793  71.189  99.537  1.00 29.02 ? 1140 ASN   A N     1 
ATOM   8434  C  CA    . ASN   A  1  1142 ? 25.909  69.968  98.738  1.00 29.39 ? 1140 ASN   A CA    1 
ATOM   8435  C  C     . ASN   A  1  1142 ? 24.640  69.112  98.772  1.00 27.97 ? 1140 ASN   A C     1 
ATOM   8436  O  O     . ASN   A  1  1142 ? 24.715  67.883  98.759  1.00 27.18 ? 1140 ASN   A O     1 
ATOM   8437  C  CB    . ASN   A  1  1142 ? 27.135  69.135  99.126  1.00 35.29 ? 1140 ASN   A CB    1 
ATOM   8438  C  CG    . ASN   A  1  1142 ? 28.398  69.973  99.250  1.00 39.78 ? 1140 ASN   A CG    1 
ATOM   8439  O  OD1   . ASN   A  1  1142 ? 29.008  70.044  100.318 1.00 43.46 ? 1140 ASN   A OD1   1 
ATOM   8440  N  ND2   . ASN   A  1  1142 ? 28.794  70.612  98.156  1.00 38.98 ? 1140 ASN   A ND2   1 
ATOM   8441  N  N     . LEU   A  1  1143 ? 23.468  69.747  98.818  1.00 28.51 ? 1141 LEU   A N     1 
ATOM   8442  C  CA    . LEU   A  1  1143 ? 22.240  68.970  98.783  1.00 26.04 ? 1141 LEU   A CA    1 
ATOM   8443  C  C     . LEU   A  1  1143 ? 22.164  68.165  97.489  1.00 29.27 ? 1141 LEU   A C     1 
ATOM   8444  O  O     . LEU   A  1  1143 ? 22.624  68.619  96.437  1.00 28.17 ? 1141 LEU   A O     1 
ATOM   8445  C  CB    . LEU   A  1  1143 ? 21.014  69.878  98.848  1.00 25.07 ? 1141 LEU   A CB    1 
ATOM   8446  C  CG    . LEU   A  1  1143 ? 20.625  70.433  100.209 1.00 26.88 ? 1141 LEU   A CG    1 
ATOM   8447  C  CD1   . LEU   A  1  1143 ? 19.461  71.393  100.039 1.00 25.91 ? 1141 LEU   A CD1   1 
ATOM   8448  C  CD2   . LEU   A  1  1143 ? 20.283  69.303  101.176 1.00 24.84 ? 1141 LEU   A CD2   1 
ATOM   8449  N  N     . PRO   A  1  1144 ? 21.582  66.969  97.537  1.00 24.53 ? 1142 PRO   A N     1 
ATOM   8450  C  CA    . PRO   A  1  1144 ? 21.230  66.278  96.292  1.00 25.10 ? 1142 PRO   A CA    1 
ATOM   8451  C  C     . PRO   A  1  1144 ? 20.327  67.173  95.462  1.00 24.59 ? 1142 PRO   A C     1 
ATOM   8452  O  O     . PRO   A  1  1144 ? 19.518  67.939  95.997  1.00 23.43 ? 1142 PRO   A O     1 
ATOM   8453  C  CB    . PRO   A  1  1144 ? 20.463  65.041  96.778  1.00 29.81 ? 1142 PRO   A CB    1 
ATOM   8454  C  CG    . PRO   A  1  1144 ? 20.778  64.917  98.240  1.00 30.75 ? 1142 PRO   A CG    1 
ATOM   8455  C  CD    . PRO   A  1  1144 ? 21.044  66.295  98.731  1.00 27.88 ? 1142 PRO   A CD    1 
ATOM   8456  N  N     . GLN   A  1  1145 ? 20.460  67.070  94.137  1.00 26.79 ? 1143 GLN   A N     1 
ATOM   8457  C  CA    . GLN   A  1  1145 ? 19.649  67.905  93.260  1.00 26.81 ? 1143 GLN   A CA    1 
ATOM   8458  C  C     . GLN   A  1  1145 ? 18.155  67.746  93.526  1.00 23.31 ? 1143 GLN   A C     1 
ATOM   8459  O  O     . GLN   A  1  1145 ? 17.408  68.723  93.427  1.00 23.54 ? 1143 GLN   A O     1 
ATOM   8460  C  CB    . GLN   A  1  1145 ? 19.963  67.601  91.793  1.00 30.41 ? 1143 GLN   A CB    1 
ATOM   8461  N  N     . THR   A  1  1146 ? 17.697  66.540  93.875  1.00 24.76 ? 1144 THR   A N     1 
ATOM   8462  C  CA    . THR   A  1  1146 ? 16.269  66.362  94.133  1.00 23.94 ? 1144 THR   A CA    1 
ATOM   8463  C  C     . THR   A  1  1146 ? 15.806  67.229  95.293  1.00 21.62 ? 1144 THR   A C     1 
ATOM   8464  O  O     . THR   A  1  1146 ? 14.690  67.762  95.271  1.00 23.20 ? 1144 THR   A O     1 
ATOM   8465  C  CB    . THR   A  1  1146 ? 15.959  64.908  94.465  1.00 24.00 ? 1144 THR   A CB    1 
ATOM   8466  O  OG1   . THR   A  1  1146 ? 16.857  64.464  95.489  1.00 24.91 ? 1144 THR   A OG1   1 
ATOM   8467  C  CG2   . THR   A  1  1146 ? 16.101  64.036  93.237  1.00 22.48 ? 1144 THR   A CG2   1 
ATOM   8468  N  N     . VAL   A  1  1147 ? 16.639  67.351  96.328  1.00 22.22 ? 1145 VAL   A N     1 
ATOM   8469  C  CA    . VAL   A  1  1147 ? 16.284  68.184  97.471  1.00 21.44 ? 1145 VAL   A CA    1 
ATOM   8470  C  C     . VAL   A  1  1147 ? 16.483  69.658  97.144  1.00 21.25 ? 1145 VAL   A C     1 
ATOM   8471  O  O     . VAL   A  1  1147 ? 15.645  70.500  97.482  1.00 20.43 ? 1145 VAL   A O     1 
ATOM   8472  C  CB    . VAL   A  1  1147 ? 17.075  67.767  98.723  1.00 20.22 ? 1145 VAL   A CB    1 
ATOM   8473  C  CG1   . VAL   A  1  1147 ? 16.593  68.571  99.912  1.00 18.96 ? 1145 VAL   A CG1   1 
ATOM   8474  C  CG2   . VAL   A  1  1147 ? 16.953  66.264  98.982  1.00 21.91 ? 1145 VAL   A CG2   1 
ATOM   8475  N  N     . GLY   A  1  1148 ? 17.587  69.996  96.471  1.00 20.84 ? 1146 GLY   A N     1 
ATOM   8476  C  CA    . GLY   A  1  1148 ? 17.793  71.374  96.058  1.00 21.17 ? 1146 GLY   A CA    1 
ATOM   8477  C  C     . GLY   A  1  1148 ? 16.635  71.945  95.262  1.00 22.94 ? 1146 GLY   A C     1 
ATOM   8478  O  O     . GLY   A  1  1148 ? 16.304  73.126  95.394  1.00 23.34 ? 1146 GLY   A O     1 
ATOM   8479  N  N     . LEU   A  1  1149 ? 15.993  71.115  94.428  1.00 20.40 ? 1147 LEU   A N     1 
ATOM   8480  C  CA    . LEU   A  1  1149 ? 14.855  71.585  93.645  1.00 23.48 ? 1147 LEU   A CA    1 
ATOM   8481  C  C     . LEU   A  1  1149 ? 13.706  72.035  94.532  1.00 21.97 ? 1147 LEU   A C     1 
ATOM   8482  O  O     . LEU   A  1  1149 ? 12.904  72.885  94.126  1.00 25.11 ? 1147 LEU   A O     1 
ATOM   8483  C  CB    . LEU   A  1  1149 ? 14.364  70.483  92.707  1.00 24.50 ? 1147 LEU   A CB    1 
ATOM   8484  C  CG    . LEU   A  1  1149 ? 15.220  70.203  91.474  1.00 31.61 ? 1147 LEU   A CG    1 
ATOM   8485  C  CD1   . LEU   A  1  1149 ? 14.644  69.019  90.714  1.00 35.43 ? 1147 LEU   A CD1   1 
ATOM   8486  C  CD2   . LEU   A  1  1149 ? 15.273  71.440  90.587  1.00 32.54 ? 1147 LEU   A CD2   1 
ATOM   8487  N  N     . ARG   A  1  1150 ? 13.606  71.472  95.736  1.00 21.11 ? 1148 ARG   A N     1 
ATOM   8488  C  CA    . ARG   A  1  1150 ? 12.550  71.824  96.669  1.00 20.52 ? 1148 ARG   A CA    1 
ATOM   8489  C  C     . ARG   A  1  1150 ? 12.942  72.946  97.614  1.00 20.97 ? 1148 ARG   A C     1 
ATOM   8490  O  O     . ARG   A  1  1150 ? 12.088  73.411  98.370  1.00 20.99 ? 1148 ARG   A O     1 
ATOM   8491  C  CB    . ARG   A  1  1150 ? 12.205  70.602  97.509  1.00 21.87 ? 1148 ARG   A CB    1 
ATOM   8492  C  CG    . ARG   A  1  1150 ? 11.529  69.494  96.740  1.00 24.83 ? 1148 ARG   A CG    1 
ATOM   8493  C  CD    . ARG   A  1  1150 ? 10.179  69.217  97.335  1.00 24.22 ? 1148 ARG   A CD    1 
ATOM   8494  N  NE    . ARG   A  1  1150 ? 9.629   67.967  96.837  1.00 21.54 ? 1148 ARG   A NE    1 
ATOM   8495  C  CZ    . ARG   A  1  1150 ? 9.151   67.011  97.613  1.00 21.08 ? 1148 ARG   A CZ    1 
ATOM   8496  N  NH1   . ARG   A  1  1150 ? 9.085   67.157  98.924  1.00 18.06 ? 1148 ARG   A NH1   1 
ATOM   8497  N  NH2   . ARG   A  1  1150 ? 8.714   65.885  97.061  1.00 18.55 ? 1148 ARG   A NH2   1 
ATOM   8498  N  N     . VAL   A  1  1151 ? 14.197  73.379  97.606  1.00 19.73 ? 1149 VAL   A N     1 
ATOM   8499  C  CA    . VAL   A  1  1151 ? 14.717  74.304  98.610  1.00 19.95 ? 1149 VAL   A CA    1 
ATOM   8500  C  C     . VAL   A  1  1151 ? 15.017  75.639  97.943  1.00 24.41 ? 1149 VAL   A C     1 
ATOM   8501  O  O     . VAL   A  1  1151 ? 15.731  75.697  96.938  1.00 26.20 ? 1149 VAL   A O     1 
ATOM   8502  C  CB    . VAL   A  1  1151 ? 15.975  73.744  99.299  1.00 22.56 ? 1149 VAL   A CB    1 
ATOM   8503  C  CG1   . VAL   A  1  1151 ? 16.623  74.803  100.204 1.00 23.30 ? 1149 VAL   A CG1   1 
ATOM   8504  C  CG2   . VAL   A  1  1151 ? 15.638  72.509  100.107 1.00 20.62 ? 1149 VAL   A CG2   1 
ATOM   8505  N  N     . SER   A  1  1152 ? 14.478  76.709  98.501  1.00 22.11 ? 1150 SER   A N     1 
ATOM   8506  C  CA    . SER   A  1  1152 ? 14.913  78.046  98.149  1.00 24.21 ? 1150 SER   A CA    1 
ATOM   8507  C  C     . SER   A  1  1152 ? 15.191  78.793  99.440  1.00 22.97 ? 1150 SER   A C     1 
ATOM   8508  O  O     . SER   A  1  1152 ? 14.737  78.401  100.517 1.00 22.95 ? 1150 SER   A O     1 
ATOM   8509  C  CB    . SER   A  1  1152 ? 13.876  78.796  97.309  1.00 23.97 ? 1150 SER   A CB    1 
ATOM   8510  O  OG    . SER   A  1  1152 ? 12.657  78.939  98.009  1.00 29.22 ? 1150 SER   A OG    1 
ATOM   8511  N  N     . TRP   A  1  1153 ? 15.966  79.861  99.331  1.00 23.26 ? 1151 TRP   A N     1 
ATOM   8512  C  CA    . TRP   A  1  1153 ? 16.254  80.728  100.459 1.00 22.76 ? 1151 TRP   A CA    1 
ATOM   8513  C  C     . TRP   A  1  1153 ? 15.602  82.073  100.200 1.00 25.26 ? 1151 TRP   A C     1 
ATOM   8514  O  O     . TRP   A  1  1153 ? 15.609  82.569  99.067  1.00 28.43 ? 1151 TRP   A O     1 
ATOM   8515  C  CB    . TRP   A  1  1153 ? 17.757  80.896  100.621 1.00 23.73 ? 1151 TRP   A CB    1 
ATOM   8516  C  CG    . TRP   A  1  1153 ? 18.411  79.673  101.119 1.00 25.86 ? 1151 TRP   A CG    1 
ATOM   8517  C  CD1   . TRP   A  1  1153 ? 18.840  78.608  100.379 1.00 25.84 ? 1151 TRP   A CD1   1 
ATOM   8518  C  CD2   . TRP   A  1  1153 ? 18.698  79.361  102.478 1.00 23.63 ? 1151 TRP   A CD2   1 
ATOM   8519  N  NE1   . TRP   A  1  1153 ? 19.396  77.659  101.202 1.00 27.99 ? 1151 TRP   A NE1   1 
ATOM   8520  C  CE2   . TRP   A  1  1153 ? 19.320  78.098  102.498 1.00 26.50 ? 1151 TRP   A CE2   1 
ATOM   8521  C  CE3   . TRP   A  1  1153 ? 18.503  80.035  103.687 1.00 22.71 ? 1151 TRP   A CE3   1 
ATOM   8522  C  CZ2   . TRP   A  1  1153 ? 19.739  77.493  103.683 1.00 23.62 ? 1151 TRP   A CZ2   1 
ATOM   8523  C  CZ3   . TRP   A  1  1153 ? 18.927  79.436  104.861 1.00 25.91 ? 1151 TRP   A CZ3   1 
ATOM   8524  C  CH2   . TRP   A  1  1153 ? 19.535  78.178  104.852 1.00 27.57 ? 1151 TRP   A CH2   1 
ATOM   8525  N  N     . SER   A  1  1154 ? 15.010  82.655  101.239 1.00 23.99 ? 1152 SER   A N     1 
ATOM   8526  C  CA    . SER   A  1  1154 ? 14.197  83.849  101.071 1.00 25.31 ? 1152 SER   A CA    1 
ATOM   8527  C  C     . SER   A  1  1154 ? 14.688  84.940  102.002 1.00 26.32 ? 1152 SER   A C     1 
ATOM   8528  O  O     . SER   A  1  1154 ? 14.654  84.778  103.228 1.00 25.69 ? 1152 SER   A O     1 
ATOM   8529  C  CB    . SER   A  1  1154 ? 12.719  83.559  101.329 1.00 23.44 ? 1152 SER   A CB    1 
ATOM   8530  O  OG    . SER   A  1  1154 ? 11.959  84.748  101.228 1.00 26.03 ? 1152 SER   A OG    1 
ATOM   8531  N  N     . LYS   A  1  1155 ? 15.149  86.045  101.419 1.00 26.23 ? 1153 LYS   A N     1 
ATOM   8532  C  CA    . LYS   A  1  1155 ? 15.459  87.234  102.200 1.00 31.40 ? 1153 LYS   A CA    1 
ATOM   8533  C  C     . LYS   A  1  1155 ? 14.249  88.139  102.371 1.00 32.02 ? 1153 LYS   A C     1 
ATOM   8534  O  O     . LYS   A  1  1155 ? 14.120  88.805  103.405 1.00 43.42 ? 1153 LYS   A O     1 
ATOM   8535  C  CB    . LYS   A  1  1155 ? 16.618  88.003  101.555 1.00 32.45 ? 1153 LYS   A CB    1 
ATOM   8536  N  N     . ASP   A  1  1156 ? 13.348  88.163  101.397 1.00 28.59 ? 1154 ASP   A N     1 
ATOM   8537  C  CA    . ASP   A  1  1156 ? 12.153  88.998  101.427 1.00 28.65 ? 1154 ASP   A CA    1 
ATOM   8538  C  C     . ASP   A  1  1156 ? 10.983  88.032  101.319 1.00 28.57 ? 1154 ASP   A C     1 
ATOM   8539  O  O     . ASP   A  1  1156 ? 10.584  87.656  100.216 1.00 28.75 ? 1154 ASP   A O     1 
ATOM   8540  C  CB    . ASP   A  1  1156 ? 12.172  89.983  100.252 1.00 30.97 ? 1154 ASP   A CB    1 
ATOM   8541  C  CG    . ASP   A  1  1156 ? 10.958  90.902  100.231 1.00 42.93 ? 1154 ASP   A CG    1 
ATOM   8542  O  OD1   . ASP   A  1  1156 ? 10.107  90.803  101.143 1.00 42.28 ? 1154 ASP   A OD1   1 
ATOM   8543  O  OD2   . ASP   A  1  1156 ? 10.856  91.731  99.300  1.00 42.37 ? 1154 ASP   A OD2   1 
ATOM   8544  N  N     . TRP   A  1  1157 ? 10.428  87.629  102.464 1.00 26.20 ? 1155 TRP   A N     1 
ATOM   8545  C  CA    . TRP   A  1  1157 ? 9.387   86.604  102.444 1.00 23.36 ? 1155 TRP   A CA    1 
ATOM   8546  C  C     . TRP   A  1  1157 ? 8.185   87.043  101.621 1.00 27.59 ? 1155 TRP   A C     1 
ATOM   8547  O  O     . TRP   A  1  1157 ? 7.543   86.216  100.970 1.00 26.95 ? 1155 TRP   A O     1 
ATOM   8548  C  CB    . TRP   A  1  1157 ? 8.929   86.275  103.861 1.00 26.54 ? 1155 TRP   A CB    1 
ATOM   8549  C  CG    . TRP   A  1  1157 ? 9.993   85.855  104.815 1.00 23.20 ? 1155 TRP   A CG    1 
ATOM   8550  C  CD1   . TRP   A  1  1157 ? 11.274  85.487  104.534 1.00 22.48 ? 1155 TRP   A CD1   1 
ATOM   8551  C  CD2   . TRP   A  1  1157 ? 9.854   85.778  106.232 1.00 21.97 ? 1155 TRP   A CD2   1 
ATOM   8552  N  NE1   . TRP   A  1  1157 ? 11.944  85.177  105.697 1.00 25.32 ? 1155 TRP   A NE1   1 
ATOM   8553  C  CE2   . TRP   A  1  1157 ? 11.087  85.353  106.753 1.00 24.02 ? 1155 TRP   A CE2   1 
ATOM   8554  C  CE3   . TRP   A  1  1157 ? 8.795   86.031  107.114 1.00 22.44 ? 1155 TRP   A CE3   1 
ATOM   8555  C  CZ2   . TRP   A  1  1157 ? 11.295  85.169  108.116 1.00 23.58 ? 1155 TRP   A CZ2   1 
ATOM   8556  C  CZ3   . TRP   A  1  1157 ? 9.005   85.851  108.467 1.00 23.26 ? 1155 TRP   A CZ3   1 
ATOM   8557  C  CH2   . TRP   A  1  1157 ? 10.243  85.429  108.955 1.00 27.15 ? 1155 TRP   A CH2   1 
ATOM   8558  N  N     . ALA   A  1  1158 ? 7.852   88.335  101.647 1.00 27.59 ? 1156 ALA   A N     1 
ATOM   8559  C  CA    . ALA   A  1  1158 ? 6.666   88.800  100.929 1.00 28.48 ? 1156 ALA   A CA    1 
ATOM   8560  C  C     . ALA   A  1  1158 ? 6.841   88.689  99.423  1.00 34.09 ? 1156 ALA   A C     1 
ATOM   8561  O  O     . ALA   A  1  1158 ? 5.851   88.584  98.689  1.00 39.16 ? 1156 ALA   A O     1 
ATOM   8562  C  CB    . ALA   A  1  1158 ? 6.332   90.237  101.326 1.00 31.54 ? 1156 ALA   A CB    1 
ATOM   8563  N  N     . ALA   A  1  1159 ? 8.082   88.713  98.943  1.00 29.52 ? 1157 ALA   A N     1 
ATOM   8564  C  CA    . ALA   A  1  1159 ? 8.334   88.593  97.514  1.00 34.75 ? 1157 ALA   A CA    1 
ATOM   8565  C  C     . ALA   A  1  1159 ? 8.274   87.155  97.024  1.00 33.82 ? 1157 ALA   A C     1 
ATOM   8566  O  O     . ALA   A  1  1159 ? 8.015   86.929  95.837  1.00 35.60 ? 1157 ALA   A O     1 
ATOM   8567  C  CB    . ALA   A  1  1159 ? 9.710   89.172  97.177  1.00 32.01 ? 1157 ALA   A CB    1 
ATOM   8568  N  N     . ASP   A  1  1160 ? 8.494   86.183  97.904  1.00 31.89 ? 1158 ASP   A N     1 
ATOM   8569  C  CA    . ASP   A  1  1160 ? 8.699   84.799  97.504  1.00 31.76 ? 1158 ASP   A CA    1 
ATOM   8570  C  C     . ASP   A  1  1160 ? 7.502   83.903  97.791  1.00 26.11 ? 1158 ASP   A C     1 
ATOM   8571  O  O     . ASP   A  1  1160 ? 7.603   82.684  97.628  1.00 27.83 ? 1158 ASP   A O     1 
ATOM   8572  C  CB    . ASP   A  1  1160 ? 9.961   84.245  98.165  1.00 28.69 ? 1158 ASP   A CB    1 
ATOM   8573  C  CG    . ASP   A  1  1160 ? 11.193  85.042  97.805  1.00 34.05 ? 1158 ASP   A CG    1 
ATOM   8574  O  OD1   . ASP   A  1  1160 ? 11.195  85.665  96.719  1.00 40.14 ? 1158 ASP   A OD1   1 
ATOM   8575  O  OD2   . ASP   A  1  1160 ? 12.152  85.053  98.601  1.00 32.73 ? 1158 ASP   A OD2   1 
ATOM   8576  N  N     . GLY   A  1  1161 ? 6.379   84.472  98.212  1.00 25.14 ? 1159 GLY   A N     1 
ATOM   8577  C  CA    . GLY   A  1  1161 ? 5.180   83.704  98.417  1.00 27.25 ? 1159 GLY   A CA    1 
ATOM   8578  C  C     . GLY   A  1  1161 ? 4.390   83.565  97.131  1.00 28.98 ? 1159 GLY   A C     1 
ATOM   8579  O  O     . GLY   A  1  1161 ? 4.878   83.888  96.046  1.00 32.03 ? 1159 GLY   A O     1 
ATOM   8580  N  N     . PRO   A  1  1162 ? 3.143   83.094  97.229  1.00 25.81 ? 1160 PRO   A N     1 
ATOM   8581  C  CA    . PRO   A  1  1162 ? 2.430   82.726  98.455  1.00 25.57 ? 1160 PRO   A CA    1 
ATOM   8582  C  C     . PRO   A  1  1162 ? 2.968   81.443  99.048  1.00 27.24 ? 1160 PRO   A C     1 
ATOM   8583  O  O     . PRO   A  1  1162 ? 3.392   80.518  98.362  1.00 25.68 ? 1160 PRO   A O     1 
ATOM   8584  C  CB    . PRO   A  1  1162 ? 0.981   82.552  97.979  1.00 27.02 ? 1160 PRO   A CB    1 
ATOM   8585  C  CG    . PRO   A  1  1162 ? 1.116   82.129  96.547  1.00 29.93 ? 1160 PRO   A CG    1 
ATOM   8586  C  CD    . PRO   A  1  1162 ? 2.296   82.918  96.034  1.00 26.89 ? 1160 PRO   A CD    1 
ATOM   8587  N  N     . PHE   A  1  1163 ? 2.984   81.380  100.365 1.00 22.06 ? 1161 PHE   A N     1 
ATOM   8588  C  CA    . PHE   A  1  1163 ? 3.316   80.147  101.043 1.00 19.01 ? 1161 PHE   A CA    1 
ATOM   8589  C  C     . PHE   A  1  1163 ? 2.033   79.426  101.412 1.00 20.34 ? 1161 PHE   A C     1 
ATOM   8590  O  O     . PHE   A  1  1163 ? 0.926   79.970  101.309 1.00 23.94 ? 1161 PHE   A O     1 
ATOM   8591  C  CB    . PHE   A  1  1163 ? 4.179   80.448  102.263 1.00 18.30 ? 1161 PHE   A CB    1 
ATOM   8592  C  CG    . PHE   A  1  1163 ? 5.422   81.203  101.918 1.00 19.46 ? 1161 PHE   A CG    1 
ATOM   8593  C  CD1   . PHE   A  1  1163 ? 6.384   80.623  101.101 1.00 22.51 ? 1161 PHE   A CD1   1 
ATOM   8594  C  CD2   . PHE   A  1  1163 ? 5.633   82.487  102.388 1.00 20.71 ? 1161 PHE   A CD2   1 
ATOM   8595  C  CE1   . PHE   A  1  1163 ? 7.540   81.312  100.771 1.00 24.95 ? 1161 PHE   A CE1   1 
ATOM   8596  C  CE2   . PHE   A  1  1163 ? 6.790   83.177  102.056 1.00 23.34 ? 1161 PHE   A CE2   1 
ATOM   8597  C  CZ    . PHE   A  1  1163 ? 7.740   82.591  101.250 1.00 22.81 ? 1161 PHE   A CZ    1 
ATOM   8598  N  N     . ALA   A  1  1164 ? 2.182   78.164  101.805 1.00 18.57 ? 1162 ALA   A N     1 
ATOM   8599  C  CA    . ALA   A  1  1164 ? 1.034   77.349  102.173 1.00 18.54 ? 1162 ALA   A CA    1 
ATOM   8600  C  C     . ALA   A  1  1164 ? 1.081   76.936  103.630 1.00 17.85 ? 1162 ALA   A C     1 
ATOM   8601  O  O     . ALA   A  1  1164 ? 0.247   76.143  104.070 1.00 21.22 ? 1162 ALA   A O     1 
ATOM   8602  C  CB    . ALA   A  1  1164 ? 0.924   76.125  101.259 1.00 21.51 ? 1162 ALA   A CB    1 
ATOM   8603  N  N     . GLY   A  1  1165 ? 2.059   77.430  104.371 1.00 18.60 ? 1163 GLY   A N     1 
ATOM   8604  C  CA    . GLY   A  1  1165 ? 2.193   77.154  105.786 1.00 18.51 ? 1163 GLY   A CA    1 
ATOM   8605  C  C     . GLY   A  1  1165 ? 3.553   77.650  106.214 1.00 17.33 ? 1163 GLY   A C     1 
ATOM   8606  O  O     . GLY   A  1  1165 ? 4.338   78.128  105.398 1.00 17.59 ? 1163 GLY   A O     1 
ATOM   8607  N  N     . ALA   A  1  1166 ? 3.823   77.542  107.509 1.00 17.55 ? 1164 ALA   A N     1 
ATOM   8608  C  CA    . ALA   A  1  1166 ? 5.111   77.989  108.009 1.00 17.66 ? 1164 ALA   A CA    1 
ATOM   8609  C  C     . ALA   A  1  1166 ? 5.508   77.131  109.194 1.00 17.31 ? 1164 ALA   A C     1 
ATOM   8610  O  O     . ALA   A  1  1166 ? 4.652   76.666  109.956 1.00 20.29 ? 1164 ALA   A O     1 
ATOM   8611  C  CB    . ALA   A  1  1166 ? 5.081   79.464  108.420 1.00 19.65 ? 1164 ALA   A CB    1 
ATOM   8612  N  N     . LEU   A  1  1167 ? 6.814   76.942  109.342 1.00 16.39 ? 1165 LEU   A N     1 
ATOM   8613  C  CA    . LEU   A  1  1167 ? 7.402   76.295  110.504 1.00 15.44 ? 1165 LEU   A CA    1 
ATOM   8614  C  C     . LEU   A  1  1167 ? 8.392   77.271  111.107 1.00 18.97 ? 1165 LEU   A C     1 
ATOM   8615  O  O     . LEU   A  1  1167 ? 9.249   77.808  110.396 1.00 18.82 ? 1165 LEU   A O     1 
ATOM   8616  C  CB    . LEU   A  1  1167 ? 8.116   75.007  110.120 1.00 17.40 ? 1165 LEU   A CB    1 
ATOM   8617  C  CG    . LEU   A  1  1167 ? 7.209   73.957  109.481 1.00 16.91 ? 1165 LEU   A CG    1 
ATOM   8618  C  CD1   . LEU   A  1  1167 ? 8.045   72.755  109.042 1.00 20.93 ? 1165 LEU   A CD1   1 
ATOM   8619  C  CD2   . LEU   A  1  1167 ? 6.109   73.533  110.435 1.00 19.02 ? 1165 LEU   A CD2   1 
ATOM   8620  N  N     . VAL   A  1  1168 ? 8.270   77.503  112.406 1.00 18.07 ? 1166 VAL   A N     1 
ATOM   8621  C  CA    . VAL   A  1  1168 ? 9.052   78.517  113.093 1.00 18.67 ? 1166 VAL   A CA    1 
ATOM   8622  C  C     . VAL   A  1  1168 ? 9.746   77.874  114.277 1.00 18.95 ? 1166 VAL   A C     1 
ATOM   8623  O  O     . VAL   A  1  1168 ? 9.139   77.091  115.017 1.00 18.62 ? 1166 VAL   A O     1 
ATOM   8624  C  CB    . VAL   A  1  1168 ? 8.155   79.690  113.548 1.00 18.65 ? 1166 VAL   A CB    1 
ATOM   8625  C  CG1   . VAL   A  1  1168 ? 9.003   80.773  114.223 1.00 20.00 ? 1166 VAL   A CG1   1 
ATOM   8626  C  CG2   . VAL   A  1  1168 ? 7.387   80.261  112.363 1.00 18.96 ? 1166 VAL   A CG2   1 
ATOM   8627  N  N     . GLU   A  1  1169 ? 11.015  78.216  114.469 1.00 17.90 ? 1167 GLU   A N     1 
ATOM   8628  C  CA    . GLU   A  1  1169 ? 11.786  77.794  115.632 1.00 17.36 ? 1167 GLU   A CA    1 
ATOM   8629  C  C     . GLU   A  1  1169 ? 12.240  79.034  116.380 1.00 21.61 ? 1167 GLU   A C     1 
ATOM   8630  O  O     . GLU   A  1  1169 ? 12.772  79.966  115.773 1.00 21.16 ? 1167 GLU   A O     1 
ATOM   8631  C  CB    . GLU   A  1  1169 ? 13.019  77.001  115.210 1.00 17.42 ? 1167 GLU   A CB    1 
ATOM   8632  C  CG    . GLU   A  1  1169 ? 13.902  76.562  116.367 1.00 18.67 ? 1167 GLU   A CG    1 
ATOM   8633  C  CD    . GLU   A  1  1169 ? 15.228  75.990  115.897 1.00 19.76 ? 1167 GLU   A CD    1 
ATOM   8634  O  OE1   . GLU   A  1  1169 ? 15.528  76.097  114.682 1.00 19.89 ? 1167 GLU   A OE1   1 
ATOM   8635  O  OE2   . GLU   A  1  1169 ? 15.957  75.429  116.742 1.00 21.37 ? 1167 GLU   A OE2   1 
ATOM   8636  N  N     . GLY   A  1  1170 ? 12.037  79.048  117.686 1.00 19.31 ? 1168 GLY   A N     1 
ATOM   8637  C  CA    . GLY   A  1  1170 ? 12.582  80.136  118.470 1.00 21.38 ? 1168 GLY   A CA    1 
ATOM   8638  C  C     . GLY   A  1  1170 ? 11.997  80.139  119.859 1.00 20.00 ? 1168 GLY   A C     1 
ATOM   8639  O  O     . GLY   A  1  1170 ? 11.074  79.382  120.171 1.00 23.98 ? 1168 GLY   A O     1 
ATOM   8640  N  N     . ASP   A  1  1171 ? 12.524  81.042  120.680 1.00 21.39 ? 1169 ASP   A N     1 
ATOM   8641  C  CA    . ASP   A  1  1171 ? 11.899  81.286  121.973 1.00 22.26 ? 1169 ASP   A CA    1 
ATOM   8642  C  C     . ASP   A  1  1171 ? 10.596  82.057  121.774 1.00 22.96 ? 1169 ASP   A C     1 
ATOM   8643  O  O     . ASP   A  1  1171 ? 10.230  82.429  120.656 1.00 22.17 ? 1169 ASP   A O     1 
ATOM   8644  C  CB    . ASP   A  1  1171 ? 12.885  81.918  122.961 1.00 23.82 ? 1169 ASP   A CB    1 
ATOM   8645  C  CG    . ASP   A  1  1171 ? 13.365  83.304  122.546 1.00 31.01 ? 1169 ASP   A CG    1 
ATOM   8646  O  OD1   . ASP   A  1  1171 ? 12.733  83.961  121.697 1.00 26.87 ? 1169 ASP   A OD1   1 
ATOM   8647  O  OD2   . ASP   A  1  1171 ? 14.395  83.750  123.102 1.00 32.91 ? 1169 ASP   A OD2   1 
ATOM   8648  N  N     . ALA   A  1  1172 ? 9.877   82.291  122.876 1.00 23.69 ? 1170 ALA   A N     1 
ATOM   8649  C  CA    . ALA   A  1  1172 ? 8.535   82.846  122.772 1.00 27.09 ? 1170 ALA   A CA    1 
ATOM   8650  C  C     . ALA   A  1  1172 ? 8.535   84.187  122.053 1.00 22.86 ? 1170 ALA   A C     1 
ATOM   8651  O  O     . ALA   A  1  1172 ? 7.681   84.434  121.196 1.00 23.73 ? 1170 ALA   A O     1 
ATOM   8652  C  CB    . ALA   A  1  1172 ? 7.902   82.974  124.156 1.00 26.16 ? 1170 ALA   A CB    1 
ATOM   8653  N  N     . GLU   A  1  1173 ? 9.490   85.064  122.369 1.00 24.49 ? 1171 GLU   A N     1 
ATOM   8654  C  CA    . GLU   A  1  1173 ? 9.460   86.378  121.738 1.00 28.01 ? 1171 GLU   A CA    1 
ATOM   8655  C  C     . GLU   A  1  1173 ? 9.882   86.319  120.277 1.00 25.63 ? 1171 GLU   A C     1 
ATOM   8656  O  O     . GLU   A  1  1173 ? 9.352   87.077  119.455 1.00 25.39 ? 1171 GLU   A O     1 
ATOM   8657  C  CB    . GLU   A  1  1173 ? 10.244  87.408  122.548 1.00 30.40 ? 1171 GLU   A CB    1 
ATOM   8658  C  CG    . GLU   A  1  1173 ? 9.586   87.723  123.888 1.00 33.12 ? 1171 GLU   A CG    1 
ATOM   8659  C  CD    . GLU   A  1  1173 ? 8.108   88.103  123.758 1.00 35.42 ? 1171 GLU   A CD    1 
ATOM   8660  O  OE1   . GLU   A  1  1173 ? 7.739   88.792  122.781 1.00 36.16 ? 1171 GLU   A OE1   1 
ATOM   8661  O  OE2   . GLU   A  1  1173 ? 7.309   87.713  124.639 1.00 36.05 ? 1171 GLU   A OE2   1 
ATOM   8662  N  N     . ARG   A  1  1174 ? 10.802  85.413  119.932 1.00 22.67 ? 1172 ARG   A N     1 
ATOM   8663  C  CA    . ARG   A  1  1174 ? 11.109  85.174  118.526 1.00 24.53 ? 1172 ARG   A CA    1 
ATOM   8664  C  C     . ARG   A  1  1174 ? 9.881   84.672  117.786 1.00 23.02 ? 1172 ARG   A C     1 
ATOM   8665  O  O     . ARG   A  1  1174 ? 9.579   85.139  116.683 1.00 22.49 ? 1172 ARG   A O     1 
ATOM   8666  C  CB    . ARG   A  1  1174 ? 12.241  84.154  118.399 1.00 23.30 ? 1172 ARG   A CB    1 
ATOM   8667  C  CG    . ARG   A  1  1174 ? 12.552  83.757  116.957 1.00 22.95 ? 1172 ARG   A CG    1 
ATOM   8668  C  CD    . ARG   A  1  1174 ? 13.010  84.952  116.147 1.00 25.89 ? 1172 ARG   A CD    1 
ATOM   8669  N  NE    . ARG   A  1  1174 ? 13.330  84.573  114.776 1.00 24.45 ? 1172 ARG   A NE    1 
ATOM   8670  C  CZ    . ARG   A  1  1174 ? 13.416  85.425  113.765 1.00 26.74 ? 1172 ARG   A CZ    1 
ATOM   8671  N  NH1   . ARG   A  1  1174 ? 13.197  86.723  113.929 1.00 27.76 ? 1172 ARG   A NH1   1 
ATOM   8672  N  NH2   . ARG   A  1  1174 ? 13.729  84.965  112.559 1.00 24.79 ? 1172 ARG   A NH2   1 
ATOM   8673  N  N     . ILE   A  1  1175 ? 9.151   83.728  118.380 1.00 20.73 ? 1173 ILE   A N     1 
ATOM   8674  C  CA    . ILE   A  1  1175 ? 7.931   83.225  117.753 1.00 22.07 ? 1173 ILE   A CA    1 
ATOM   8675  C  C     . ILE   A  1  1175 ? 6.932   84.350  117.551 1.00 21.15 ? 1173 ILE   A C     1 
ATOM   8676  O  O     . ILE   A  1  1175 ? 6.324   84.475  116.483 1.00 21.82 ? 1173 ILE   A O     1 
ATOM   8677  C  CB    . ILE   A  1  1175 ? 7.334   82.076  118.586 1.00 23.75 ? 1173 ILE   A CB    1 
ATOM   8678  C  CG1   . ILE   A  1  1175 ? 8.278   80.871  118.560 1.00 22.22 ? 1173 ILE   A CG1   1 
ATOM   8679  C  CG2   . ILE   A  1  1175 ? 5.921   81.741  118.111 1.00 23.07 ? 1173 ILE   A CG2   1 
ATOM   8680  C  CD1   . ILE   A  1  1175 ? 7.918   79.760  119.542 1.00 24.78 ? 1173 ILE   A CD1   1 
ATOM   8681  N  N     . ARG   A  1  1176 ? 6.756   85.200  118.564 1.00 23.74 ? 1174 ARG   A N     1 
ATOM   8682  C  CA    . ARG   A  1  1176 ? 5.798   86.291  118.443 1.00 24.47 ? 1174 ARG   A CA    1 
ATOM   8683  C  C     . ARG   A  1  1176 ? 6.190   87.228  117.308 1.00 21.61 ? 1174 ARG   A C     1 
ATOM   8684  O  O     . ARG   A  1  1176 ? 5.351   87.613  116.482 1.00 23.07 ? 1174 ARG   A O     1 
ATOM   8685  C  CB    . ARG   A  1  1176 ? 5.693   87.056  119.766 1.00 21.92 ? 1174 ARG   A CB    1 
ATOM   8686  C  CG    . ARG   A  1  1176 ? 4.432   87.892  119.836 1.00 28.11 ? 1174 ARG   A CG    1 
ATOM   8687  C  CD    . ARG   A  1  1176 ? 4.519   88.923  120.943 1.00 28.61 ? 1174 ARG   A CD    1 
ATOM   8688  N  NE    . ARG   A  1  1176 ? 4.826   88.322  122.235 1.00 28.40 ? 1174 ARG   A NE    1 
ATOM   8689  C  CZ    . ARG   A  1  1176 ? 3.917   87.873  123.091 1.00 31.03 ? 1174 ARG   A CZ    1 
ATOM   8690  N  NH1   . ARG   A  1  1176 ? 2.628   87.869  122.795 1.00 29.41 ? 1174 ARG   A NH1   1 
ATOM   8691  N  NH2   . ARG   A  1  1176 ? 4.311   87.435  124.287 1.00 31.32 ? 1174 ARG   A NH2   1 
ATOM   8692  N  N     . ALA   A  1  1177 ? 7.471   87.583  117.240 1.00 23.34 ? 1175 ALA   A N     1 
ATOM   8693  C  CA    . ALA   A  1  1177 ? 7.944   88.486  116.195 1.00 24.67 ? 1175 ALA   A CA    1 
ATOM   8694  C  C     . ALA   A  1  1177 ? 7.756   87.872  114.820 1.00 22.00 ? 1175 ALA   A C     1 
ATOM   8695  O  O     . ALA   A  1  1177 ? 7.280   88.531  113.890 1.00 23.46 ? 1175 ALA   A O     1 
ATOM   8696  C  CB    . ALA   A  1  1177 ? 9.415   88.823  116.425 1.00 25.39 ? 1175 ALA   A CB    1 
ATOM   8697  N  N     . VAL   A  1  1178 ? 8.121   86.600  114.671 1.00 22.03 ? 1176 VAL   A N     1 
ATOM   8698  C  CA    . VAL   A  1  1178 ? 7.961   85.940  113.381 1.00 20.39 ? 1176 VAL   A CA    1 
ATOM   8699  C  C     . VAL   A  1  1178 ? 6.493   85.858  113.003 1.00 21.60 ? 1176 VAL   A C     1 
ATOM   8700  O  O     . VAL   A  1  1178 ? 6.126   86.067  111.839 1.00 22.38 ? 1176 VAL   A O     1 
ATOM   8701  C  CB    . VAL   A  1  1178 ? 8.636   84.559  113.393 1.00 20.02 ? 1176 VAL   A CB    1 
ATOM   8702  C  CG1   . VAL   A  1  1178 ? 8.257   83.789  112.130 1.00 21.05 ? 1176 VAL   A CG1   1 
ATOM   8703  C  CG2   . VAL   A  1  1178 ? 10.131  84.721  113.468 1.00 20.54 ? 1176 VAL   A CG2   1 
ATOM   8704  N  N     . ASN   A  1  1179 ? 5.628   85.570  113.977 1.00 21.49 ? 1177 ASN   A N     1 
ATOM   8705  C  CA    . ASN   A  1  1179 ? 4.203   85.452  113.697 1.00 20.92 ? 1177 ASN   A CA    1 
ATOM   8706  C  C     . ASN   A  1  1179 ? 3.653   86.773  113.179 1.00 22.28 ? 1177 ASN   A C     1 
ATOM   8707  O  O     . ASN   A  1  1179 ? 2.825   86.794  112.262 1.00 22.36 ? 1177 ASN   A O     1 
ATOM   8708  C  CB    . ASN   A  1  1179 ? 3.481   85.031  114.982 1.00 27.41 ? 1177 ASN   A CB    1 
ATOM   8709  C  CG    . ASN   A  1  1179 ? 2.308   84.108  114.736 1.00 31.76 ? 1177 ASN   A CG    1 
ATOM   8710  O  OD1   . ASN   A  1  1179 ? 2.126   83.565  113.640 1.00 33.39 ? 1177 ASN   A OD1   1 
ATOM   8711  N  ND2   . ASN   A  1  1179 ? 1.490   83.922  115.771 1.00 35.71 ? 1177 ASN   A ND2   1 
ATOM   8712  N  N     . LYS   A  1  1180 ? 4.131   87.892  113.733 1.00 22.69 ? 1178 LYS   A N     1 
ATOM   8713  C  CA    . LYS   A  1  1180 ? 3.735   89.203  113.227 1.00 24.27 ? 1178 LYS   A CA    1 
ATOM   8714  C  C     . LYS   A  1  1180 ? 4.233   89.414  111.802 1.00 22.59 ? 1178 LYS   A C     1 
ATOM   8715  O  O     . LYS   A  1  1180 ? 3.493   89.915  110.947 1.00 23.37 ? 1178 LYS   A O     1 
ATOM   8716  C  CB    . LYS   A  1  1180 ? 4.276   90.297  114.150 1.00 26.33 ? 1178 LYS   A CB    1 
ATOM   8717  C  CG    . LYS   A  1  1180 ? 3.636   90.295  115.533 1.00 27.73 ? 1178 LYS   A CG    1 
ATOM   8718  C  CD    . LYS   A  1  1180 ? 4.420   91.160  116.537 1.00 27.25 ? 1178 LYS   A CD    1 
ATOM   8719  C  CE    . LYS   A  1  1180 ? 4.498   92.628  116.104 1.00 36.86 ? 1178 LYS   A CE    1 
ATOM   8720  N  NZ    . LYS   A  1  1180 ? 5.256   93.486  117.075 1.00 41.04 ? 1178 LYS   A NZ    1 
ATOM   8721  N  N     . ALA   A  1  1181 ? 5.480   89.033  111.528 1.00 21.98 ? 1179 ALA   A N     1 
ATOM   8722  C  CA    . ALA   A  1  1181 ? 6.012   89.176  110.178 1.00 23.45 ? 1179 ALA   A CA    1 
ATOM   8723  C  C     . ALA   A  1  1181 ? 5.253   88.299  109.197 1.00 23.14 ? 1179 ALA   A C     1 
ATOM   8724  O  O     . ALA   A  1  1181 ? 4.991   88.709  108.063 1.00 22.93 ? 1179 ALA   A O     1 
ATOM   8725  C  CB    . ALA   A  1  1181 ? 7.502   88.847  110.155 1.00 23.36 ? 1179 ALA   A CB    1 
ATOM   8726  N  N     . ILE   A  1  1182 ? 4.867   87.096  109.625 1.00 20.21 ? 1180 ILE   A N     1 
ATOM   8727  C  CA    . ILE   A  1  1182 ? 4.138   86.199  108.738 1.00 21.77 ? 1180 ILE   A CA    1 
ATOM   8728  C  C     . ILE   A  1  1182 ? 2.746   86.739  108.468 1.00 22.66 ? 1180 ILE   A C     1 
ATOM   8729  O  O     . ILE   A  1  1182 ? 2.266   86.712  107.327 1.00 21.19 ? 1180 ILE   A O     1 
ATOM   8730  C  CB    . ILE   A  1  1182 ? 4.109   84.775  109.317 1.00 22.13 ? 1180 ILE   A CB    1 
ATOM   8731  C  CG1   . ILE   A  1  1182 ? 5.497   84.152  109.229 1.00 22.29 ? 1180 ILE   A CG1   1 
ATOM   8732  C  CG2   . ILE   A  1  1182 ? 3.063   83.936  108.591 1.00 22.84 ? 1180 ILE   A CG2   1 
ATOM   8733  C  CD1   . ILE   A  1  1182 ? 5.602   82.770  109.868 1.00 24.28 ? 1180 ILE   A CD1   1 
ATOM   8734  N  N     . ALA   A  1  1183 ? 2.083   87.257  109.501 1.00 22.72 ? 1181 ALA   A N     1 
ATOM   8735  C  CA    . ALA   A  1  1183 ? 0.743   87.794  109.303 1.00 22.22 ? 1181 ALA   A CA    1 
ATOM   8736  C  C     . ALA   A  1  1183 ? 0.762   88.964  108.331 1.00 21.49 ? 1181 ALA   A C     1 
ATOM   8737  O  O     . ALA   A  1  1183 ? -0.222  89.202  107.619 1.00 22.22 ? 1181 ALA   A O     1 
ATOM   8738  C  CB    . ALA   A  1  1183 ? 0.134   88.191  110.647 1.00 21.35 ? 1181 ALA   A CB    1 
ATOM   8739  N  N     . ALA   A  1  1184 ? 1.893   89.670  108.244 1.00 21.93 ? 1182 ALA   A N     1 
ATOM   8740  C  CA    . ALA   A  1  1184 ? 1.987   90.817  107.350 1.00 22.44 ? 1182 ALA   A CA    1 
ATOM   8741  C  C     . ALA   A  1  1184 ? 2.205   90.415  105.901 1.00 23.83 ? 1182 ALA   A C     1 
ATOM   8742  O  O     . ALA   A  1  1184 ? 2.111   91.275  105.019 1.00 23.34 ? 1182 ALA   A O     1 
ATOM   8743  C  CB    . ALA   A  1  1184 ? 3.113   91.753  107.801 1.00 24.60 ? 1182 ALA   A CB    1 
ATOM   8744  N  N     . LEU   A  1  1185 ? 2.499   89.150  105.637 1.00 21.41 ? 1183 LEU   A N     1 
ATOM   8745  C  CA    . LEU   A  1  1185 ? 2.705   88.734  104.259 1.00 22.83 ? 1183 LEU   A CA    1 
ATOM   8746  C  C     . LEU   A  1  1185 ? 1.412   88.892  103.468 1.00 21.44 ? 1183 LEU   A C     1 
ATOM   8747  O  O     . LEU   A  1  1185 ? 0.323   88.614  103.984 1.00 23.03 ? 1183 LEU   A O     1 
ATOM   8748  C  CB    . LEU   A  1  1185 ? 3.158   87.283  104.193 1.00 21.56 ? 1183 LEU   A CB    1 
ATOM   8749  C  CG    . LEU   A  1  1185 ? 4.472   87.011  104.911 1.00 22.23 ? 1183 LEU   A CG    1 
ATOM   8750  C  CD1   . LEU   A  1  1185 ? 4.795   85.535  104.851 1.00 22.16 ? 1183 LEU   A CD1   1 
ATOM   8751  C  CD2   . LEU   A  1  1185 ? 5.610   87.846  104.328 1.00 24.86 ? 1183 LEU   A CD2   1 
ATOM   8752  N  N     . PRO   A  1  1186 ? 1.489   89.326  102.218 1.00 23.07 ? 1184 PRO   A N     1 
ATOM   8753  C  CA    . PRO   A  1  1186 ? 0.271   89.459  101.419 1.00 23.08 ? 1184 PRO   A CA    1 
ATOM   8754  C  C     . PRO   A  1  1186 ? -0.339  88.100  101.129 1.00 19.76 ? 1184 PRO   A C     1 
ATOM   8755  O  O     . PRO   A  1  1186 ? 0.343   87.073  101.104 1.00 23.74 ? 1184 PRO   A O     1 
ATOM   8756  C  CB    . PRO   A  1  1186 ? 0.768   90.117  100.127 1.00 26.36 ? 1184 PRO   A CB    1 
ATOM   8757  C  CG    . PRO   A  1  1186 ? 2.202   89.707  100.032 1.00 29.24 ? 1184 PRO   A CG    1 
ATOM   8758  C  CD    . PRO   A  1  1186 ? 2.705   89.654  101.460 1.00 25.06 ? 1184 PRO   A CD    1 
ATOM   8759  N  N     . GLY   A  1  1187 ? -1.647  88.103  100.930 1.00 20.29 ? 1185 GLY   A N     1 
ATOM   8760  C  CA    . GLY   A  1  1187 ? -2.307  86.933  100.410 1.00 23.34 ? 1185 GLY   A CA    1 
ATOM   8761  C  C     . GLY   A  1  1187 ? -2.873  86.026  101.482 1.00 20.03 ? 1185 GLY   A C     1 
ATOM   8762  O  O     . GLY   A  1  1187 ? -3.550  86.471  102.418 1.00 23.26 ? 1185 GLY   A O     1 
ATOM   8763  N  N     . PRO   A  1  1188 ? -2.607  84.730  101.356 1.00 19.99 ? 1186 PRO   A N     1 
ATOM   8764  C  CA    . PRO   A  1  1188 ? -3.334  83.753  102.167 1.00 18.90 ? 1186 PRO   A CA    1 
ATOM   8765  C  C     . PRO   A  1  1188 ? -2.890  83.783  103.614 1.00 18.55 ? 1186 PRO   A C     1 
ATOM   8766  O  O     . PRO   A  1  1188 ? -1.744  84.103  103.939 1.00 19.83 ? 1186 PRO   A O     1 
ATOM   8767  C  CB    . PRO   A  1  1188 ? -2.973  82.415  101.520 1.00 20.93 ? 1186 PRO   A CB    1 
ATOM   8768  C  CG    . PRO   A  1  1188 ? -1.617  82.655  100.932 1.00 21.41 ? 1186 PRO   A CG    1 
ATOM   8769  C  CD    . PRO   A  1  1188 ? -1.652  84.094  100.442 1.00 20.79 ? 1186 PRO   A CD    1 
ATOM   8770  N  N     . LEU   A  1  1189 ? -3.824  83.446  104.487 1.00 19.64 ? 1187 LEU   A N     1 
ATOM   8771  C  CA    . LEU   A  1  1189 ? -3.458  83.182  105.866 1.00 19.31 ? 1187 LEU   A CA    1 
ATOM   8772  C  C     . LEU   A  1  1189 ? -2.620  81.915  105.901 1.00 19.64 ? 1187 LEU   A C     1 
ATOM   8773  O  O     . LEU   A  1  1189 ? -2.908  80.944  105.199 1.00 23.37 ? 1187 LEU   A O     1 
ATOM   8774  C  CB    . LEU   A  1  1189 ? -4.713  83.004  106.715 1.00 20.51 ? 1187 LEU   A CB    1 
ATOM   8775  C  CG    . LEU   A  1  1189 ? -5.441  84.278  107.168 1.00 21.36 ? 1187 LEU   A CG    1 
ATOM   8776  C  CD1   . LEU   A  1  1189 ? -6.142  84.977  106.002 1.00 22.35 ? 1187 LEU   A CD1   1 
ATOM   8777  C  CD2   . LEU   A  1  1189 ? -6.432  83.945  108.266 1.00 27.33 ? 1187 LEU   A CD2   1 
ATOM   8778  N  N     . LEU   A  1  1190 ? -1.537  81.941  106.661 1.00 20.13 ? 1188 LEU   A N     1 
ATOM   8779  C  CA    . LEU   A  1  1190 ? -0.658  80.785  106.747 1.00 21.02 ? 1188 LEU   A CA    1 
ATOM   8780  C  C     . LEU   A  1  1190 ? -0.920  80.045  108.045 1.00 18.15 ? 1188 LEU   A C     1 
ATOM   8781  O  O     . LEU   A  1  1190 ? -1.002  80.662  109.110 1.00 21.26 ? 1188 LEU   A O     1 
ATOM   8782  C  CB    . LEU   A  1  1190 ? 0.808   81.200  106.692 1.00 22.28 ? 1188 LEU   A CB    1 
ATOM   8783  C  CG    . LEU   A  1  1190 ? 1.230   81.943  105.430 1.00 21.55 ? 1188 LEU   A CG    1 
ATOM   8784  C  CD1   . LEU   A  1  1190 ? 2.738   82.012  105.426 1.00 28.34 ? 1188 LEU   A CD1   1 
ATOM   8785  C  CD2   . LEU   A  1  1190 ? 0.738   81.216  104.184 1.00 23.48 ? 1188 LEU   A CD2   1 
ATOM   8786  N  N     . LEU   A  1  1191 ? -1.047  78.727  107.951 1.00 19.14 ? 1189 LEU   A N     1 
ATOM   8787  C  CA    . LEU   A  1  1191 ? -1.075  77.892  109.147 1.00 18.14 ? 1189 LEU   A CA    1 
ATOM   8788  C  C     . LEU   A  1  1191 ? 0.361   77.762  109.624 1.00 19.07 ? 1189 LEU   A C     1 
ATOM   8789  O  O     . LEU   A  1  1191 ? 1.179   77.086  108.985 1.00 19.60 ? 1189 LEU   A O     1 
ATOM   8790  C  CB    . LEU   A  1  1191 ? -1.688  76.535  108.814 1.00 18.71 ? 1189 LEU   A CB    1 
ATOM   8791  C  CG    . LEU   A  1  1191 ? -2.226  75.707  109.977 1.00 18.89 ? 1189 LEU   A CG    1 
ATOM   8792  C  CD1   . LEU   A  1  1191 ? -3.051  74.566  109.417 1.00 19.75 ? 1189 LEU   A CD1   1 
ATOM   8793  C  CD2   . LEU   A  1  1191 ? -1.070  75.143  110.815 1.00 19.46 ? 1189 LEU   A CD2   1 
ATOM   8794  N  N     . VAL   A  1  1192 ? 0.666   78.421  110.735 1.00 19.51 ? 1190 VAL   A N     1 
ATOM   8795  C  CA    . VAL   A  1  1192 ? 2.003   78.492  111.301 1.00 18.25 ? 1190 VAL   A CA    1 
ATOM   8796  C  C     . VAL   A  1  1192 ? 2.092   77.505  112.450 1.00 18.47 ? 1190 VAL   A C     1 
ATOM   8797  O  O     . VAL   A  1  1192 ? 1.200   77.448  113.308 1.00 21.17 ? 1190 VAL   A O     1 
ATOM   8798  C  CB    . VAL   A  1  1192 ? 2.278   79.913  111.825 1.00 22.00 ? 1190 VAL   A CB    1 
ATOM   8799  C  CG1   . VAL   A  1  1192 ? 3.679   80.000  112.436 1.00 22.64 ? 1190 VAL   A CG1   1 
ATOM   8800  C  CG2   . VAL   A  1  1192 ? 2.101   80.948  110.730 1.00 22.27 ? 1190 VAL   A CG2   1 
ATOM   8801  N  N     . GLN   A  1  1193 ? 3.188   76.760  112.502 1.00 18.08 ? 1191 GLN   A N     1 
ATOM   8802  C  CA    . GLN   A  1  1193 ? 3.511   75.943  113.657 1.00 16.79 ? 1191 GLN   A CA    1 
ATOM   8803  C  C     . GLN   A  1  1193 ? 4.850   76.401  114.191 1.00 17.63 ? 1191 GLN   A C     1 
ATOM   8804  O  O     . GLN   A  1  1193 ? 5.807   76.559  113.423 1.00 18.59 ? 1191 GLN   A O     1 
ATOM   8805  C  CB    . GLN   A  1  1193 ? 3.615   74.478  113.276 1.00 17.02 ? 1191 GLN   A CB    1 
ATOM   8806  C  CG    . GLN   A  1  1193 ? 2.326   73.900  112.737 1.00 20.02 ? 1191 GLN   A CG    1 
ATOM   8807  C  CD    . GLN   A  1  1193 ? 2.398   72.398  112.652 1.00 21.07 ? 1191 GLN   A CD    1 
ATOM   8808  O  OE1   . GLN   A  1  1193 ? 2.326   71.711  113.664 1.00 21.65 ? 1191 GLN   A OE1   1 
ATOM   8809  N  NE2   . GLN   A  1  1193 ? 2.554   71.878  111.441 1.00 19.64 ? 1191 GLN   A NE2   1 
ATOM   8810  N  N     . ALA   A  1  1194 ? 4.928   76.592  115.495 1.00 17.15 ? 1192 ALA   A N     1 
ATOM   8811  C  CA    . ALA   A  1  1194 ? 6.145   77.076  116.105 1.00 16.64 ? 1192 ALA   A CA    1 
ATOM   8812  C  C     . ALA   A  1  1194 ? 6.580   76.112  117.194 1.00 18.47 ? 1192 ALA   A C     1 
ATOM   8813  O  O     . ALA   A  1  1194 ? 5.758   75.429  117.812 1.00 20.49 ? 1192 ALA   A O     1 
ATOM   8814  C  CB    . ALA   A  1  1194 ? 5.907   78.450  116.711 1.00 19.61 ? 1192 ALA   A CB    1 
ATOM   8815  N  N     . ALA   A  1  1195 ? 7.877   76.104  117.454 1.00 18.02 ? 1193 ALA   A N     1 
ATOM   8816  C  CA    . ALA   A  1  1195 ? 8.427   75.287  118.522 1.00 19.06 ? 1193 ALA   A CA    1 
ATOM   8817  C  C     . ALA   A  1  1195 ? 9.734   75.917  118.960 1.00 19.86 ? 1193 ALA   A C     1 
ATOM   8818  O  O     . ALA   A  1  1195 ? 10.413  76.574  118.173 1.00 20.76 ? 1193 ALA   A O     1 
ATOM   8819  C  CB    . ALA   A  1  1195 ? 8.686   73.860  118.031 1.00 20.16 ? 1193 ALA   A CB    1 
ATOM   8820  N  N     . SER   A  1  1196 ? 10.077  75.715  120.220 1.00 20.43 ? 1194 SER   A N     1 
ATOM   8821  C  CA    . SER   A  1  1196 ? 11.396  76.115  120.670 1.00 21.60 ? 1194 SER   A CA    1 
ATOM   8822  C  C     . SER   A  1  1196 ? 12.425  75.070  120.245 1.00 20.15 ? 1194 SER   A C     1 
ATOM   8823  O  O     . SER   A  1  1196 ? 12.091  73.948  119.867 1.00 20.51 ? 1194 SER   A O     1 
ATOM   8824  C  CB    . SER   A  1  1196 ? 11.421  76.230  122.189 1.00 23.83 ? 1194 SER   A CB    1 
ATOM   8825  O  OG    . SER   A  1  1196 ? 11.237  74.950  122.759 1.00 23.27 ? 1194 SER   A OG    1 
ATOM   8826  N  N     . SER   A  1  1197 ? 13.701  75.447  120.310 1.00 21.74 ? 1195 SER   A N     1 
ATOM   8827  C  CA    . SER   A  1  1197 ? 14.740  74.467  120.019 1.00 22.23 ? 1195 SER   A CA    1 
ATOM   8828  C  C     . SER   A  1  1197 ? 14.651  73.285  120.977 1.00 20.71 ? 1195 SER   A C     1 
ATOM   8829  O  O     . SER   A  1  1197 ? 14.803  72.127  120.564 1.00 23.57 ? 1195 SER   A O     1 
ATOM   8830  C  CB    . SER   A  1  1197 ? 16.115  75.116  120.116 1.00 22.84 ? 1195 SER   A CB    1 
ATOM   8831  O  OG    . SER   A  1  1197 ? 16.235  76.195  119.215 1.00 23.62 ? 1195 SER   A OG    1 
ATOM   8832  N  N     . GLY   A  1  1198 ? 14.379  73.558  122.250 1.00 21.89 ? 1196 GLY   A N     1 
ATOM   8833  C  CA    . GLY   A  1  1198 ? 14.238  72.481  123.220 1.00 23.91 ? 1196 GLY   A CA    1 
ATOM   8834  C  C     . GLY   A  1  1198 ? 13.050  71.582  122.935 1.00 25.54 ? 1196 GLY   A C     1 
ATOM   8835  O  O     . GLY   A  1  1198 ? 13.132  70.361  123.092 1.00 25.29 ? 1196 GLY   A O     1 
ATOM   8836  N  N     . GLU   A  1  1199 ? 11.935  72.170  122.491 1.00 21.30 ? 1197 GLU   A N     1 
ATOM   8837  C  CA    . GLU   A  1  1199 ? 10.783  71.367  122.109 1.00 23.33 ? 1197 GLU   A CA    1 
ATOM   8838  C  C     . GLU   A  1  1199 ? 11.113  70.467  120.930 1.00 23.76 ? 1197 GLU   A C     1 
ATOM   8839  O  O     . GLU   A  1  1199 ? 10.709  69.299  120.892 1.00 23.25 ? 1197 GLU   A O     1 
ATOM   8840  C  CB    . GLU   A  1  1199 ? 9.623   72.299  121.792 1.00 21.66 ? 1197 GLU   A CB    1 
ATOM   8841  C  CG    . GLU   A  1  1199 ? 8.313   71.634  121.515 1.00 30.63 ? 1197 GLU   A CG    1 
ATOM   8842  C  CD    . GLU   A  1  1199 ? 7.230   72.670  121.327 1.00 40.59 ? 1197 GLU   A CD    1 
ATOM   8843  O  OE1   . GLU   A  1  1199 ? 7.530   73.876  121.530 1.00 33.35 ? 1197 GLU   A OE1   1 
ATOM   8844  O  OE2   . GLU   A  1  1199 ? 6.094   72.286  120.976 1.00 43.54 ? 1197 GLU   A OE2   1 
ATOM   8845  N  N     . ILE   A  1  1200 ? 11.833  70.996  119.940 1.00 20.94 ? 1198 ILE   A N     1 
ATOM   8846  C  CA    . ILE   A  1  1200 ? 12.242  70.166  118.812 1.00 21.82 ? 1198 ILE   A CA    1 
ATOM   8847  C  C     . ILE   A  1  1200 ? 13.075  68.988  119.296 1.00 24.31 ? 1198 ILE   A C     1 
ATOM   8848  O  O     . ILE   A  1  1200 ? 12.915  67.860  118.818 1.00 23.49 ? 1198 ILE   A O     1 
ATOM   8849  C  CB    . ILE   A  1  1200 ? 12.988  71.014  117.765 1.00 20.97 ? 1198 ILE   A CB    1 
ATOM   8850  C  CG1   . ILE   A  1  1200 ? 12.032  72.030  117.142 1.00 20.57 ? 1198 ILE   A CG1   1 
ATOM   8851  C  CG2   . ILE   A  1  1200 ? 13.615  70.124  116.680 1.00 21.99 ? 1198 ILE   A CG2   1 
ATOM   8852  C  CD1   . ILE   A  1  1200 ? 12.716  73.039  116.264 1.00 22.24 ? 1198 ILE   A CD1   1 
ATOM   8853  N  N     . ALA   A  1  1201 ? 13.954  69.223  120.273 1.00 22.07 ? 1199 ALA   A N     1 
ATOM   8854  C  CA    . ALA   A  1  1201 ? 14.789  68.145  120.796 1.00 23.98 ? 1199 ALA   A CA    1 
ATOM   8855  C  C     . ALA   A  1  1201 ? 13.969  67.135  121.590 1.00 25.40 ? 1199 ALA   A C     1 
ATOM   8856  O  O     . ALA   A  1  1201 ? 14.257  65.931  121.555 1.00 25.60 ? 1199 ALA   A O     1 
ATOM   8857  C  CB    . ALA   A  1  1201 ? 15.913  68.718  121.657 1.00 24.42 ? 1199 ALA   A CB    1 
ATOM   8858  N  N     . ARG   A  1  1202 ? 12.961  67.599  122.327 1.00 22.10 ? 1200 ARG   A N     1 
ATOM   8859  C  CA    . ARG   A  1  1202 ? 12.232  66.716  123.224 1.00 22.86 ? 1200 ARG   A CA    1 
ATOM   8860  C  C     . ARG   A  1  1202 ? 11.079  66.001  122.542 1.00 24.61 ? 1200 ARG   A C     1 
ATOM   8861  O  O     . ARG   A  1  1202 ? 10.762  64.866  122.911 1.00 27.57 ? 1200 ARG   A O     1 
ATOM   8862  C  CB    . ARG   A  1  1202 ? 11.681  67.504  124.413 1.00 24.25 ? 1200 ARG   A CB    1 
ATOM   8863  C  CG    . ARG   A  1  1202 ? 12.750  68.013  125.369 1.00 23.96 ? 1200 ARG   A CG    1 
ATOM   8864  C  CD    . ARG   A  1  1202 ? 12.126  68.660  126.599 1.00 27.36 ? 1200 ARG   A CD    1 
ATOM   8865  N  NE    . ARG   A  1  1202 ? 11.320  69.810  126.222 1.00 28.84 ? 1200 ARG   A NE    1 
ATOM   8866  C  CZ    . ARG   A  1  1202 ? 11.736  71.070  126.249 1.00 30.95 ? 1200 ARG   A CZ    1 
ATOM   8867  N  NH1   . ARG   A  1  1202 ? 12.917  71.403  126.750 1.00 26.69 ? 1200 ARG   A NH1   1 
ATOM   8868  N  NH2   . ARG   A  1  1202 ? 10.945  72.020  125.753 1.00 29.86 ? 1200 ARG   A NH2   1 
ATOM   8869  N  N     . ASN   A  1  1203 ? 10.441  66.631  121.566 1.00 23.41 ? 1201 ASN   A N     1 
ATOM   8870  C  CA    . ASN   A  1  1203 ? 9.170   66.132  121.053 1.00 23.71 ? 1201 ASN   A CA    1 
ATOM   8871  C  C     . ASN   A  1  1203 ? 9.280   65.851  119.569 1.00 27.76 ? 1201 ASN   A C     1 
ATOM   8872  O  O     . ASN   A  1  1203 ? 9.326   66.801  118.765 1.00 24.26 ? 1201 ASN   A O     1 
ATOM   8873  C  CB    . ASN   A  1  1203 ? 8.060   67.148  121.310 1.00 25.91 ? 1201 ASN   A CB    1 
ATOM   8874  C  CG    . ASN   A  1  1203 ? 6.712   66.664  120.829 1.00 29.40 ? 1201 ASN   A CG    1 
ATOM   8875  O  OD1   . ASN   A  1  1203 ? 6.575   65.528  120.371 1.00 28.21 ? 1201 ASN   A OD1   1 
ATOM   8876  N  ND2   . ASN   A  1  1203 ? 5.706   67.523  120.932 1.00 30.02 ? 1201 ASN   A ND2   1 
ATOM   8877  N  N     . PRO   A  1  1204 ? 9.280   64.585  119.154 1.00 27.01 ? 1202 PRO   A N     1 
ATOM   8878  C  CA    . PRO   A  1  1204 ? 9.350   64.283  117.717 1.00 28.95 ? 1202 PRO   A CA    1 
ATOM   8879  C  C     . PRO   A  1  1204 ? 8.207   64.874  116.922 1.00 27.13 ? 1202 PRO   A C     1 
ATOM   8880  O  O     . PRO   A  1  1204 ? 8.363   65.099  115.719 1.00 26.60 ? 1202 PRO   A O     1 
ATOM   8881  C  CB    . PRO   A  1  1204 ? 9.333   62.748  117.677 1.00 34.40 ? 1202 PRO   A CB    1 
ATOM   8882  C  CG    . PRO   A  1  1204 ? 9.773   62.326  119.042 1.00 36.90 ? 1202 PRO   A CG    1 
ATOM   8883  C  CD    . PRO   A  1  1204 ? 9.213   63.365  119.972 1.00 31.83 ? 1202 PRO   A CD    1 
ATOM   8884  N  N     . ASP   A  1  1205 ? 7.073   65.153  117.565 1.00 26.61 ? 1203 ASP   A N     1 
ATOM   8885  C  CA    . ASP   A  1  1205 ? 5.918   65.750  116.906 1.00 24.55 ? 1203 ASP   A CA    1 
ATOM   8886  C  C     . ASP   A  1  1205 ? 5.806   67.242  117.180 1.00 26.44 ? 1203 ASP   A C     1 
ATOM   8887  O  O     . ASP   A  1  1205 ? 4.701   67.796  117.101 1.00 30.20 ? 1203 ASP   A O     1 
ATOM   8888  C  CB    . ASP   A  1  1205 ? 4.636   65.044  117.350 1.00 32.96 ? 1203 ASP   A CB    1 
ATOM   8889  C  CG    . ASP   A  1  1205 ? 4.658   63.563  117.058 1.00 38.67 ? 1203 ASP   A CG    1 
ATOM   8890  O  OD1   . ASP   A  1  1205 ? 5.400   63.148  116.147 1.00 33.44 ? 1203 ASP   A OD1   1 
ATOM   8891  O  OD2   . ASP   A  1  1205 ? 3.931   62.814  117.745 1.00 44.30 ? 1203 ASP   A OD2   1 
ATOM   8892  N  N     . ALA   A  1  1206 ? 6.919   67.892  117.531 1.00 22.98 ? 1204 ALA   A N     1 
ATOM   8893  C  CA    . ALA   A  1  1206 ? 6.914   69.335  117.752 1.00 23.32 ? 1204 ALA   A CA    1 
ATOM   8894  C  C     . ALA   A  1  1206 ? 6.209   70.053  116.615 1.00 23.63 ? 1204 ALA   A C     1 
ATOM   8895  O  O     . ALA   A  1  1206 ? 5.409   70.966  116.846 1.00 26.62 ? 1204 ALA   A O     1 
ATOM   8896  C  CB    . ALA   A  1  1206 ? 8.350   69.838  117.860 1.00 23.68 ? 1204 ALA   A CB    1 
ATOM   8897  N  N     . TYR   A  1  1207 ? 6.486   69.648  115.383 1.00 21.60 ? 1205 TYR   A N     1 
ATOM   8898  C  CA    . TYR   A  1  1207 ? 5.730   70.096  114.223 1.00 22.81 ? 1205 TYR   A CA    1 
ATOM   8899  C  C     . TYR   A  1  1207 ? 4.833   68.955  113.778 1.00 22.81 ? 1205 TYR   A C     1 
ATOM   8900  O  O     . TYR   A  1  1207 ? 5.318   67.871  113.440 1.00 29.34 ? 1205 TYR   A O     1 
ATOM   8901  C  CB    . TYR   A  1  1207 ? 6.664   70.498  113.088 1.00 21.69 ? 1205 TYR   A CB    1 
ATOM   8902  C  CG    . TYR   A  1  1207 ? 7.599   71.611  113.456 1.00 18.11 ? 1205 TYR   A CG    1 
ATOM   8903  C  CD1   . TYR   A  1  1207 ? 7.110   72.861  113.819 1.00 21.11 ? 1205 TYR   A CD1   1 
ATOM   8904  C  CD2   . TYR   A  1  1207 ? 8.967   71.419  113.433 1.00 20.44 ? 1205 TYR   A CD2   1 
ATOM   8905  C  CE1   . TYR   A  1  1207 ? 7.971   73.886  114.151 1.00 19.04 ? 1205 TYR   A CE1   1 
ATOM   8906  C  CE2   . TYR   A  1  1207 ? 9.837   72.436  113.769 1.00 20.75 ? 1205 TYR   A CE2   1 
ATOM   8907  C  CZ    . TYR   A  1  1207 ? 9.327   73.669  114.115 1.00 19.26 ? 1205 TYR   A CZ    1 
ATOM   8908  O  OH    . TYR   A  1  1207 ? 10.192  74.677  114.444 1.00 21.73 ? 1205 TYR   A OH    1 
ATOM   8909  N  N     . CYS   A  1  1208 ? 3.538   69.197  113.766 1.00 20.79 ? 1206 CYS   A N     1 
ATOM   8910  C  CA    . CYS   A  1  1208 ? 2.581   68.146  113.479 1.00 22.32 ? 1206 CYS   A CA    1 
ATOM   8911  C  C     . CYS   A  1  1208 ? 2.407   68.018  111.973 1.00 20.86 ? 1206 CYS   A C     1 
ATOM   8912  O  O     . CYS   A  1  1208 ? 2.140   69.007  111.284 1.00 19.26 ? 1206 CYS   A O     1 
ATOM   8913  C  CB    . CYS   A  1  1208 ? 1.256   68.491  114.148 1.00 23.98 ? 1206 CYS   A CB    1 
ATOM   8914  S  SG    . CYS   A  1  1208 ? -0.040  67.295  113.857 1.00 27.81 ? 1206 CYS   A SG    1 
ATOM   8915  N  N     . LEU   A  1  1209 ? 2.574   66.797  111.466 1.00 18.26 ? 1207 LEU   A N     1 
ATOM   8916  C  CA    . LEU   A  1  1209 ? 2.490   66.579  110.033 1.00 17.53 ? 1207 LEU   A CA    1 
ATOM   8917  C  C     . LEU   A  1  1209 ? 1.061   66.702  109.507 1.00 17.98 ? 1207 LEU   A C     1 
ATOM   8918  O  O     . LEU   A  1  1209 ? 0.886   66.869  108.295 1.00 19.19 ? 1207 LEU   A O     1 
ATOM   8919  C  CB    . LEU   A  1  1209 ? 3.087   65.220  109.670 1.00 18.15 ? 1207 LEU   A CB    1 
ATOM   8920  C  CG    . LEU   A  1  1209 ? 4.536   65.033  110.110 1.00 18.99 ? 1207 LEU   A CG    1 
ATOM   8921  C  CD1   . LEU   A  1  1209 ? 5.030   63.696  109.599 1.00 20.41 ? 1207 LEU   A CD1   1 
ATOM   8922  C  CD2   . LEU   A  1  1209 ? 5.411   66.155  109.580 1.00 21.12 ? 1207 LEU   A CD2   1 
ATOM   8923  N  N     . ASN   A  1  1210 ? 0.052   66.627  110.391 1.00 19.12 ? 1208 ASN   A N     1 
ATOM   8924  C  CA    . ASN   A  1  1210 ? -1.335  66.813  109.971 1.00 20.10 ? 1208 ASN   A CA    1 
ATOM   8925  C  C     . ASN   A  1  1210 ? -1.515  68.135  109.238 1.00 18.91 ? 1208 ASN   A C     1 
ATOM   8926  O  O     . ASN   A  1  1210 ? -2.320  68.231  108.315 1.00 21.05 ? 1208 ASN   A O     1 
ATOM   8927  C  CB    . ASN   A  1  1210 ? -2.287  66.830  111.179 1.00 23.12 ? 1208 ASN   A CB    1 
ATOM   8928  C  CG    . ASN   A  1  1210 ? -2.438  65.478  111.864 1.00 24.83 ? 1208 ASN   A CG    1 
ATOM   8929  O  OD1   . ASN   A  1  1210 ? -1.683  64.542  111.626 1.00 33.27 ? 1208 ASN   A OD1   1 
ATOM   8930  N  ND2   . ASN   A  1  1210 ? -3.426  65.390  112.754 1.00 33.27 ? 1208 ASN   A ND2   1 
ATOM   8931  N  N     . TRP   A  1  1211 ? -0.819  69.183  109.680 1.00 18.03 ? 1209 TRP   A N     1 
ATOM   8932  C  CA    . TRP   A  1  1211 ? -1.045  70.525  109.160 1.00 19.43 ? 1209 TRP   A CA    1 
ATOM   8933  C  C     . TRP   A  1  1211 ? -0.097  70.884  108.031 1.00 19.04 ? 1209 TRP   A C     1 
ATOM   8934  O  O     . TRP   A  1  1211 ? -0.103  72.028  107.572 1.00 22.00 ? 1209 TRP   A O     1 
ATOM   8935  C  CB    . TRP   A  1  1211 ? -0.966  71.557  110.297 1.00 19.38 ? 1209 TRP   A CB    1 
ATOM   8936  C  CG    . TRP   A  1  1211 ? -1.562  71.047  111.579 1.00 20.25 ? 1209 TRP   A CG    1 
ATOM   8937  C  CD1   . TRP   A  1  1211 ? -0.956  70.999  112.809 1.00 21.07 ? 1209 TRP   A CD1   1 
ATOM   8938  C  CD2   . TRP   A  1  1211 ? -2.864  70.463  111.756 1.00 19.95 ? 1209 TRP   A CD2   1 
ATOM   8939  N  NE1   . TRP   A  1  1211 ? -1.802  70.433  113.729 1.00 23.21 ? 1209 TRP   A NE1   1 
ATOM   8940  C  CE2   . TRP   A  1  1211 ? -2.979  70.102  113.109 1.00 20.07 ? 1209 TRP   A CE2   1 
ATOM   8941  C  CE3   . TRP   A  1  1211 ? -3.942  70.215  110.899 1.00 20.98 ? 1209 TRP   A CE3   1 
ATOM   8942  C  CZ2   . TRP   A  1  1211 ? -4.127  69.502  113.629 1.00 22.58 ? 1209 TRP   A CZ2   1 
ATOM   8943  C  CZ3   . TRP   A  1  1211 ? -5.082  69.623  111.422 1.00 20.86 ? 1209 TRP   A CZ3   1 
ATOM   8944  C  CH2   . TRP   A  1  1211 ? -5.164  69.270  112.766 1.00 22.01 ? 1209 TRP   A CH2   1 
ATOM   8945  N  N     . LEU   A  1  1212 ? 0.706   69.930  107.567 1.00 16.86 ? 1210 LEU   A N     1 
ATOM   8946  C  CA    . LEU   A  1  1212 ? 1.634   70.139  106.472 1.00 17.82 ? 1210 LEU   A CA    1 
ATOM   8947  C  C     . LEU   A  1  1212 ? 1.180   69.444  105.200 1.00 15.25 ? 1210 LEU   A C     1 
ATOM   8948  O  O     . LEU   A  1  1212 ? 1.871   69.515  104.185 1.00 16.38 ? 1210 LEU   A O     1 
ATOM   8949  C  CB    . LEU   A  1  1212 ? 3.027   69.659  106.878 1.00 16.16 ? 1210 LEU   A CB    1 
ATOM   8950  C  CG    . LEU   A  1  1212 ? 3.725   70.642  107.820 1.00 17.59 ? 1210 LEU   A CG    1 
ATOM   8951  C  CD1   . LEU   A  1  1212 ? 4.898   69.977  108.529 1.00 18.41 ? 1210 LEU   A CD1   1 
ATOM   8952  C  CD2   . LEU   A  1  1212 ? 4.173   71.898  107.059 1.00 20.54 ? 1210 LEU   A CD2   1 
ATOM   8953  N  N     . VAL   A  1  1213 ? 0.036   68.771  105.244 1.00 16.82 ? 1211 VAL   A N     1 
ATOM   8954  C  CA    . VAL   A  1  1213 ? -0.607  68.229  104.060 1.00 17.59 ? 1211 VAL   A CA    1 
ATOM   8955  C  C     . VAL   A  1  1213 ? -1.873  69.020  103.808 1.00 16.71 ? 1211 VAL   A C     1 
ATOM   8956  O  O     . VAL   A  1  1213 ? -2.385  69.732  104.670 1.00 17.83 ? 1211 VAL   A O     1 
ATOM   8957  C  CB    . VAL   A  1  1213 ? -0.929  66.721  104.166 1.00 16.96 ? 1211 VAL   A CB    1 
ATOM   8958  C  CG1   . VAL   A  1  1213 ? 0.353   65.892  104.165 1.00 19.18 ? 1211 VAL   A CG1   1 
ATOM   8959  C  CG2   . VAL   A  1  1213 ? -1.786  66.424  105.391 1.00 18.43 ? 1211 VAL   A CG2   1 
ATOM   8960  N  N     . GLU   A  1  1214 ? -2.382  68.876  102.599 1.00 16.61 ? 1212 GLU   A N     1 
ATOM   8961  C  CA    . GLU   A  1  1214 ? -3.582  69.558  102.159 1.00 19.16 ? 1212 GLU   A CA    1 
ATOM   8962  C  C     . GLU   A  1  1214 ? -4.599  68.493  101.798 1.00 17.10 ? 1212 GLU   A C     1 
ATOM   8963  O  O     . GLU   A  1  1214 ? -4.292  67.570  101.038 1.00 16.21 ? 1212 GLU   A O     1 
ATOM   8964  C  CB    . GLU   A  1  1214 ? -3.224  70.354  100.918 1.00 23.27 ? 1212 GLU   A CB    1 
ATOM   8965  C  CG    . GLU   A  1  1214 ? -4.300  71.213  100.350 1.00 30.82 ? 1212 GLU   A CG    1 
ATOM   8966  C  CD    . GLU   A  1  1214 ? -3.706  72.120  99.302  1.00 33.03 ? 1212 GLU   A CD    1 
ATOM   8967  O  OE1   . GLU   A  1  1214 ? -3.021  73.093  99.690  1.00 34.03 ? 1212 GLU   A OE1   1 
ATOM   8968  O  OE2   . GLU   A  1  1214 ? -3.871  71.825  98.102  1.00 35.50 ? 1212 GLU   A OE2   1 
ATOM   8969  N  N     . GLU   A  1  1215 ? -5.793  68.614  102.348 1.00 17.31 ? 1213 GLU   A N     1 
ATOM   8970  C  CA    . GLU   A  1  1215 ? -6.873  67.701  102.010 1.00 15.03 ? 1213 GLU   A CA    1 
ATOM   8971  C  C     . GLU   A  1  1215 ? -7.541  68.132  100.713 1.00 14.82 ? 1213 GLU   A C     1 
ATOM   8972  O  O     . GLU   A  1  1215 ? -7.791  69.319  100.484 1.00 16.47 ? 1213 GLU   A O     1 
ATOM   8973  C  CB    . GLU   A  1  1215 ? -7.924  67.737  103.105 1.00 15.75 ? 1213 GLU   A CB    1 
ATOM   8974  C  CG    . GLU   A  1  1215 ? -7.433  67.290  104.461 1.00 17.14 ? 1213 GLU   A CG    1 
ATOM   8975  C  CD    . GLU   A  1  1215 ? -8.395  67.697  105.555 1.00 17.32 ? 1213 GLU   A CD    1 
ATOM   8976  O  OE1   . GLU   A  1  1215 ? -8.365  68.882  105.951 1.00 19.05 ? 1213 GLU   A OE1   1 
ATOM   8977  O  OE2   . GLU   A  1  1215 ? -9.187  66.840  105.986 1.00 18.93 ? 1213 GLU   A OE2   1 
ATOM   8978  N  N     . VAL   A  1  1216 ? -7.836  67.156  99.869  1.00 15.40 ? 1214 VAL   A N     1 
ATOM   8979  C  CA    . VAL   A  1  1216 ? -8.617  67.400  98.666  1.00 16.63 ? 1214 VAL   A CA    1 
ATOM   8980  C  C     . VAL   A  1  1216 ? -9.763  66.405  98.632  1.00 16.78 ? 1214 VAL   A C     1 
ATOM   8981  O  O     . VAL   A  1  1216 ? -9.559  65.201  98.803  1.00 17.33 ? 1214 VAL   A O     1 
ATOM   8982  C  CB    . VAL   A  1  1216 ? -7.768  67.287  97.397  1.00 15.55 ? 1214 VAL   A CB    1 
ATOM   8983  C  CG1   . VAL   A  1  1216 ? -8.655  67.474  96.186  1.00 17.02 ? 1214 VAL   A CG1   1 
ATOM   8984  C  CG2   . VAL   A  1  1216 ? -6.670  68.350  97.413  1.00 18.67 ? 1214 VAL   A CG2   1 
ATOM   8985  N  N     . SER   A  1  1217 ? -10.970 66.911  98.439  1.00 15.25 ? 1215 SER   A N     1 
ATOM   8986  C  CA    . SER   A  1  1217 ? -12.157 66.093  98.255  1.00 15.96 ? 1215 SER   A CA    1 
ATOM   8987  C  C     . SER   A  1  1217 ? -12.568 66.190  96.802  1.00 15.55 ? 1215 SER   A C     1 
ATOM   8988  O  O     . SER   A  1  1217 ? -12.498 67.264  96.212  1.00 15.64 ? 1215 SER   A O     1 
ATOM   8989  C  CB    . SER   A  1  1217 ? -13.291 66.655  99.097  1.00 17.54 ? 1215 SER   A CB    1 
ATOM   8990  O  OG    . SER   A  1  1217 ? -14.553 66.190  98.646  1.00 19.47 ? 1215 SER   A OG    1 
ATOM   8991  N  N     . ALA   A  1  1218 ? -12.925 65.058  96.216  1.00 14.54 ? 1216 ALA   A N     1 
ATOM   8992  C  CA    . ALA   A  1  1218 ? -13.411 65.034  94.843  1.00 15.06 ? 1216 ALA   A CA    1 
ATOM   8993  C  C     . ALA   A  1  1218 ? -14.672 64.198  94.801  1.00 15.81 ? 1216 ALA   A C     1 
ATOM   8994  O  O     . ALA   A  1  1218 ? -14.691 63.062  95.283  1.00 17.91 ? 1216 ALA   A O     1 
ATOM   8995  C  CB    . ALA   A  1  1218 ? -12.353 64.473  93.890  1.00 15.89 ? 1216 ALA   A CB    1 
ATOM   8996  N  N     . SER   A  1  1219 ? -15.729 64.768  94.236  1.00 14.75 ? 1217 SER   A N     1 
ATOM   8997  C  CA    . SER   A  1  1219 ? -17.014 64.100  94.121  1.00 16.22 ? 1217 SER   A CA    1 
ATOM   8998  C  C     . SER   A  1  1219 ? -17.319 63.939  92.647  1.00 14.67 ? 1217 SER   A C     1 
ATOM   8999  O  O     . SER   A  1  1219 ? -17.421 64.934  91.921  1.00 15.49 ? 1217 SER   A O     1 
ATOM   9000  C  CB    . SER   A  1  1219 ? -18.117 64.901  94.798  1.00 17.87 ? 1217 SER   A CB    1 
ATOM   9001  O  OG    . SER   A  1  1219 ? -19.342 64.194  94.683  1.00 16.57 ? 1217 SER   A OG    1 
ATOM   9002  N  N     . ILE   A  1  1220 ? -17.462 62.694  92.224  1.00 15.49 ? 1218 ILE   A N     1 
ATOM   9003  C  CA    . ILE   A  1  1220 ? -17.644 62.347  90.823  1.00 15.22 ? 1218 ILE   A CA    1 
ATOM   9004  C  C     . ILE   A  1  1220 ? -19.032 61.760  90.669  1.00 15.23 ? 1218 ILE   A C     1 
ATOM   9005  O  O     . ILE   A  1  1220 ? -19.354 60.745  91.292  1.00 16.34 ? 1218 ILE   A O     1 
ATOM   9006  C  CB    . ILE   A  1  1220 ? -16.593 61.327  90.367  1.00 18.09 ? 1218 ILE   A CB    1 
ATOM   9007  C  CG1   . ILE   A  1  1220 ? -15.194 61.875  90.640  1.00 20.56 ? 1218 ILE   A CG1   1 
ATOM   9008  C  CG2   . ILE   A  1  1220 ? -16.791 60.994  88.897  1.00 19.53 ? 1218 ILE   A CG2   1 
ATOM   9009  C  CD1   . ILE   A  1  1220 ? -14.102 60.837  90.557  1.00 31.18 ? 1218 ILE   A CD1   1 
ATOM   9010  N  N     . ASN   A  1  1221 ? -19.841 62.374  89.810  1.00 15.46 ? 1219 ASN   A N     1 
ATOM   9011  C  CA    . ASN   A  1  1221 ? -21.161 61.846  89.485  1.00 16.27 ? 1219 ASN   A CA    1 
ATOM   9012  C  C     . ASN   A  1  1221 ? -20.964 60.719  88.477  1.00 15.04 ? 1219 ASN   A C     1 
ATOM   9013  O  O     . ASN   A  1  1221 ? -20.698 60.965  87.303  1.00 20.30 ? 1219 ASN   A O     1 
ATOM   9014  C  CB    . ASN   A  1  1221 ? -22.016 62.963  88.906  1.00 17.19 ? 1219 ASN   A CB    1 
ATOM   9015  C  CG    . ASN   A  1  1221 ? -23.332 62.467  88.398  1.00 17.53 ? 1219 ASN   A CG    1 
ATOM   9016  O  OD1   . ASN   A  1  1221 ? -23.725 61.327  88.656  1.00 16.75 ? 1219 ASN   A OD1   1 
ATOM   9017  N  ND2   . ASN   A  1  1221 ? -24.024 63.318  87.650  1.00 20.22 ? 1219 ASN   A ND2   1 
ATOM   9018  N  N     . THR   A  1  1222 ? -21.105 59.480  88.931  1.00 15.71 ? 1220 THR   A N     1 
ATOM   9019  C  CA    . THR   A  1  1222 ? -20.873 58.337  88.058  1.00 18.53 ? 1220 THR   A CA    1 
ATOM   9020  C  C     . THR   A  1  1222 ? -22.144 57.891  87.363  1.00 21.06 ? 1220 THR   A C     1 
ATOM   9021  O  O     . THR   A  1  1222 ? -22.119 56.915  86.609  1.00 26.64 ? 1220 THR   A O     1 
ATOM   9022  C  CB    . THR   A  1  1222 ? -20.261 57.179  88.838  1.00 20.31 ? 1220 THR   A CB    1 
ATOM   9023  O  OG1   . THR   A  1  1222 ? -21.135 56.824  89.918  1.00 20.38 ? 1220 THR   A OG1   1 
ATOM   9024  C  CG2   . THR   A  1  1222 ? -18.904 57.577  89.387  1.00 19.31 ? 1220 THR   A CG2   1 
ATOM   9025  N  N     . ALA   A  1  1223 ? -23.250 58.577  87.606  1.00 17.77 ? 1221 ALA   A N     1 
ATOM   9026  C  CA    . ALA   A  1  1223 ? -24.480 58.363  86.872  1.00 20.99 ? 1221 ALA   A CA    1 
ATOM   9027  C  C     . ALA   A  1  1223 ? -24.636 59.342  85.717  1.00 24.57 ? 1221 ALA   A C     1 
ATOM   9028  O  O     . ALA   A  1  1223 ? -25.675 59.327  85.050  1.00 28.57 ? 1221 ALA   A O     1 
ATOM   9029  C  CB    . ALA   A  1  1223 ? -25.671 58.510  87.818  1.00 23.22 ? 1221 ALA   A CB    1 
ATOM   9030  N  N     . ALA   A  1  1224 ? -23.635 60.198  85.469  0.67 19.75 ? 1222 ALA   A N     1 
ATOM   9031  C  CA    . ALA   A  1  1224 ? -23.805 61.300  84.524  0.67 22.96 ? 1222 ALA   A CA    1 
ATOM   9032  C  C     . ALA   A  1  1224 ? -24.025 60.810  83.099  0.67 24.37 ? 1222 ALA   A C     1 
ATOM   9033  O  O     . ALA   A  1  1224 ? -24.641 61.517  82.296  0.67 27.62 ? 1222 ALA   A O     1 
ATOM   9034  C  CB    . ALA   A  1  1224 ? -22.602 62.245  84.581  0.67 22.52 ? 1222 ALA   A CB    1 
ATOM   9035  N  N     . ALA   A  1  1225 ? -23.537 59.615  82.762  0.67 22.58 ? 1223 ALA   A N     1 
ATOM   9036  C  CA    . ALA   A  1  1225 ? -23.731 59.110  81.408  0.67 23.91 ? 1223 ALA   A CA    1 
ATOM   9037  C  C     . ALA   A  1  1225 ? -25.163 58.673  81.146  0.67 27.78 ? 1223 ALA   A C     1 
ATOM   9038  O  O     . ALA   A  1  1225 ? -25.511 58.417  79.990  0.67 27.60 ? 1223 ALA   A O     1 
ATOM   9039  C  CB    . ALA   A  1  1225 ? -22.757 57.967  81.104  0.67 28.11 ? 1223 ALA   A CB    1 
ATOM   9040  N  N     . GLY   A  1  1226 ? -25.996 58.591  82.178  0.67 24.42 ? 1224 GLY   A N     1 
ATOM   9041  C  CA    . GLY   A  1  1226 ? -27.401 58.251  82.014  0.67 23.42 ? 1224 GLY   A CA    1 
ATOM   9042  C  C     . GLY   A  1  1226 ? -27.836 57.029  82.786  0.67 28.07 ? 1224 GLY   A C     1 
ATOM   9043  O  O     . GLY   A  1  1226 ? -29.028 56.692  82.764  0.67 27.64 ? 1224 GLY   A O     1 
ATOM   9044  N  N     . GLY   A  1  1227 ? -26.925 56.345  83.465  0.67 23.16 ? 1225 GLY   A N     1 
ATOM   9045  C  CA    . GLY   A  1  1227 ? -27.292 55.188  84.256  0.67 27.88 ? 1225 GLY   A CA    1 
ATOM   9046  C  C     . GLY   A  1  1227 ? -26.188 54.877  85.236  0.67 24.30 ? 1225 GLY   A C     1 
ATOM   9047  O  O     . GLY   A  1  1227 ? -25.120 55.493  85.226  0.67 24.83 ? 1225 GLY   A O     1 
ATOM   9048  N  N     . ASN   A  1  1228 ? -26.457 53.892  86.078  0.67 21.97 ? 1226 ASN   A N     1 
ATOM   9049  C  CA    . ASN   A  1  1228 ? -25.559 53.503  87.157  0.67 22.83 ? 1226 ASN   A CA    1 
ATOM   9050  C  C     . ASN   A  1  1228 ? -25.065 52.090  86.865  0.67 24.73 ? 1226 ASN   A C     1 
ATOM   9051  O  O     . ASN   A  1  1228 ? -25.832 51.126  86.960  0.67 25.40 ? 1226 ASN   A O     1 
ATOM   9052  C  CB    . ASN   A  1  1228 ? -26.310 53.571  88.484  0.67 24.98 ? 1226 ASN   A CB    1 
ATOM   9053  C  CG    . ASN   A  1  1228 ? -25.417 53.332  89.686  0.67 26.75 ? 1226 ASN   A CG    1 
ATOM   9054  O  OD1   . ASN   A  1  1228 ? -24.506 52.503  89.655  0.67 28.32 ? 1226 ASN   A OD1   1 
ATOM   9055  N  ND2   . ASN   A  1  1228 ? -25.694 54.046  90.770  0.67 27.58 ? 1226 ASN   A ND2   1 
ATOM   9056  N  N     . ALA   A  1  1229 ? -23.781 51.975  86.519  0.67 24.48 ? 1227 ALA   A N     1 
ATOM   9057  C  CA    . ALA   A  1  1229 ? -23.227 50.679  86.140  0.67 24.28 ? 1227 ALA   A CA    1 
ATOM   9058  C  C     . ALA   A  1  1229 ? -23.316 49.676  87.283  0.67 26.62 ? 1227 ALA   A C     1 
ATOM   9059  O  O     . ALA   A  1  1229 ? -23.719 48.524  87.084  0.67 25.67 ? 1227 ALA   A O     1 
ATOM   9060  C  CB    . ALA   A  1  1229 ? -21.775 50.850  85.697  0.67 26.36 ? 1227 ALA   A CB    1 
ATOM   9061  N  N     . SER   A  1  1230 ? -22.927 50.093  88.490  0.67 26.61 ? 1228 SER   A N     1 
ATOM   9062  C  CA    . SER   A  1  1230 ? -22.939 49.174  89.624  0.67 28.12 ? 1228 SER   A CA    1 
ATOM   9063  C  C     . SER   A  1  1230 ? -24.345 48.662  89.912  0.67 29.34 ? 1228 SER   A C     1 
ATOM   9064  O  O     . SER   A  1  1230 ? -24.534 47.476  90.211  0.67 29.04 ? 1228 SER   A O     1 
ATOM   9065  C  CB    . SER   A  1  1230 ? -22.342 49.849  90.857  0.67 32.42 ? 1228 SER   A CB    1 
ATOM   9066  O  OG    . SER   A  1  1230 ? -20.969 50.124  90.660  0.67 36.87 ? 1228 SER   A OG    1 
ATOM   9067  N  N     . LEU   A  1  1231 ? -25.348 49.535  89.806  0.67 27.74 ? 1229 LEU   A N     1 
ATOM   9068  C  CA    . LEU   A  1  1231 ? -26.719 49.111  90.064  0.67 27.59 ? 1229 LEU   A CA    1 
ATOM   9069  C  C     . LEU   A  1  1231 ? -27.299 48.244  88.951  0.67 29.68 ? 1229 LEU   A C     1 
ATOM   9070  O  O     . LEU   A  1  1231 ? -28.342 47.615  89.162  0.67 31.76 ? 1229 LEU   A O     1 
ATOM   9071  C  CB    . LEU   A  1  1231 ? -27.618 50.315  90.356  0.67 25.42 ? 1229 LEU   A CB    1 
ATOM   9072  C  CG    . LEU   A  1  1231 ? -27.514 50.949  91.751  0.67 30.23 ? 1229 LEU   A CG    1 
ATOM   9073  C  CD1   . LEU   A  1  1231 ? -28.628 51.961  91.957  0.67 25.90 ? 1229 LEU   A CD1   1 
ATOM   9074  C  CD2   . LEU   A  1  1231 ? -27.549 49.900  92.840  0.67 35.84 ? 1229 LEU   A CD2   1 
ATOM   9075  N  N     . MET   A  1  1232 ? -26.655 48.180  87.782  0.67 31.05 ? 1230 MET   A N     1 
ATOM   9076  C  CA    . MET   A  1  1232 ? -27.065 47.200  86.781  0.67 28.62 ? 1230 MET   A CA    1 
ATOM   9077  C  C     . MET   A  1  1232 ? -26.923 45.770  87.294  0.67 31.61 ? 1230 MET   A C     1 
ATOM   9078  O  O     . MET   A  1  1232 ? -27.600 44.869  86.786  0.67 34.07 ? 1230 MET   A O     1 
ATOM   9079  C  CB    . MET   A  1  1232 ? -26.264 47.383  85.488  0.67 30.59 ? 1230 MET   A CB    1 
ATOM   9080  N  N     . ALA   A  1  1233 ? -26.071 45.548  88.293  0.67 33.64 ? 1231 ALA   A N     1 
ATOM   9081  C  CA    . ALA   A  1  1233 ? -25.892 44.237  88.905  0.67 36.78 ? 1231 ALA   A CA    1 
ATOM   9082  C  C     . ALA   A  1  1233 ? -26.793 44.011  90.112  0.67 38.92 ? 1231 ALA   A C     1 
ATOM   9083  O  O     . ALA   A  1  1233 ? -26.750 42.926  90.703  0.67 39.03 ? 1231 ALA   A O     1 
ATOM   9084  C  CB    . ALA   A  1  1233 ? -24.429 44.040  89.315  0.67 35.89 ? 1231 ALA   A CB    1 
ATOM   9085  N  N     . ILE   A  1  1234 ? -27.603 44.993  90.495  0.67 37.11 ? 1232 ILE   A N     1 
ATOM   9086  C  CA    . ILE   A  1  1234 ? -28.483 44.874  91.652  0.67 38.83 ? 1232 ILE   A CA    1 
ATOM   9087  C  C     . ILE   A  1  1234 ? -29.908 44.651  91.159  0.67 35.29 ? 1232 ILE   A C     1 
ATOM   9088  O  O     . ILE   A  1  1234 ? -30.552 45.567  90.634  0.67 33.70 ? 1232 ILE   A O     1 
ATOM   9089  C  CB    . ILE   A  1  1234 ? -28.379 46.084  92.589  0.67 34.19 ? 1232 ILE   A CB    1 
ATOM   9090  C  CG1   . ILE   A  1  1234 ? -26.969 46.170  93.177  0.67 37.94 ? 1232 ILE   A CG1   1 
ATOM   9091  C  CG2   . ILE   A  1  1234 ? -29.403 45.976  93.699  0.67 32.12 ? 1232 ILE   A CG2   1 
ATOM   9092  C  CD1   . ILE   A  1  1234 ? -26.898 46.865  94.522  0.67 36.83 ? 1232 ILE   A CD1   1 
ATOM   9093  N  N     . GLY   A  1  1235 ? -30.393 43.426  91.322  0.67 36.96 ? 1233 GLY   A N     1 
ATOM   9094  C  CA    . GLY   A  1  1235 ? -31.763 43.082  91.006  0.67 30.94 ? 1233 GLY   A CA    1 
ATOM   9095  C  C     . GLY   A  1  1235 ? -32.329 42.248  92.134  0.67 28.28 ? 1233 GLY   A C     1 
ATOM   9096  O  O     . GLY   A  1  1235 ? -31.606 41.477  92.765  0.67 31.24 ? 1233 GLY   A O     1 
ATOM   9097  O  OXT   . GLY   A  1  1235 ? -33.502 42.310  92.462  0.67 22.27 ? 1233 GLY   A OXT   1 
ATOM   9098  N  N     . ALA   B  1  16   ? 30.141  4.543   81.281  1.00 43.95 ? 14   ALA   B N     1 
ATOM   9099  C  CA    . ALA   B  1  16   ? 29.170  5.616   81.486  1.00 43.13 ? 14   ALA   B CA    1 
ATOM   9100  C  C     . ALA   B  1  16   ? 27.751  5.067   81.448  1.00 41.95 ? 14   ALA   B C     1 
ATOM   9101  O  O     . ALA   B  1  16   ? 27.397  4.324   80.532  1.00 44.47 ? 14   ALA   B O     1 
ATOM   9102  C  CB    . ALA   B  1  16   ? 29.339  6.707   80.433  1.00 39.56 ? 14   ALA   B CB    1 
ATOM   9103  N  N     . PRO   B  1  17   ? 26.940  5.434   82.438  1.00 39.87 ? 15   PRO   B N     1 
ATOM   9104  C  CA    . PRO   B  1  17   ? 25.548  4.971   82.455  1.00 39.45 ? 15   PRO   B CA    1 
ATOM   9105  C  C     . PRO   B  1  17   ? 24.803  5.440   81.214  1.00 33.31 ? 15   PRO   B C     1 
ATOM   9106  O  O     . PRO   B  1  17   ? 24.991  6.563   80.739  1.00 34.59 ? 15   PRO   B O     1 
ATOM   9107  C  CB    . PRO   B  1  17   ? 24.978  5.606   83.730  1.00 41.21 ? 15   PRO   B CB    1 
ATOM   9108  C  CG    . PRO   B  1  17   ? 25.872  6.771   84.010  1.00 42.14 ? 15   PRO   B CG    1 
ATOM   9109  C  CD    . PRO   B  1  17   ? 27.236  6.347   83.555  1.00 38.56 ? 15   PRO   B CD    1 
ATOM   9110  N  N     . ALA   B  1  18   ? 23.969  4.553   80.679  1.00 32.49 ? 16   ALA   B N     1 
ATOM   9111  C  CA    . ALA   B  1  18   ? 23.187  4.883   79.499  1.00 29.96 ? 16   ALA   B CA    1 
ATOM   9112  C  C     . ALA   B  1  18   ? 22.271  6.063   79.810  1.00 26.88 ? 16   ALA   B C     1 
ATOM   9113  O  O     . ALA   B  1  18   ? 21.709  6.138   80.909  1.00 28.50 ? 16   ALA   B O     1 
ATOM   9114  C  CB    . ALA   B  1  18   ? 22.335  3.683   79.087  1.00 28.26 ? 16   ALA   B CB    1 
ATOM   9115  N  N     . PRO   B  1  19   ? 22.099  6.997   78.878  1.00 22.58 ? 17   PRO   B N     1 
ATOM   9116  C  CA    . PRO   B  1  19   ? 21.254  8.167   79.157  1.00 23.21 ? 17   PRO   B CA    1 
ATOM   9117  C  C     . PRO   B  1  19   ? 19.836  7.757   79.524  1.00 21.60 ? 17   PRO   B C     1 
ATOM   9118  O  O     . PRO   B  1  19   ? 19.212  6.935   78.851  1.00 23.10 ? 17   PRO   B O     1 
ATOM   9119  C  CB    . PRO   B  1  19   ? 21.287  8.951   77.839  1.00 24.02 ? 17   PRO   B CB    1 
ATOM   9120  C  CG    . PRO   B  1  19   ? 22.568  8.548   77.201  1.00 25.31 ? 17   PRO   B CG    1 
ATOM   9121  C  CD    . PRO   B  1  19   ? 22.775  7.100   77.571  1.00 25.05 ? 17   PRO   B CD    1 
ATOM   9122  N  N     . PHE   B  1  20   ? 19.342  8.325   80.625  1.00 20.95 ? 18   PHE   B N     1 
ATOM   9123  C  CA    . PHE   B  1  20   ? 17.967  8.161   81.090  1.00 19.15 ? 18   PHE   B CA    1 
ATOM   9124  C  C     . PHE   B  1  20   ? 17.634  6.745   81.535  1.00 23.41 ? 18   PHE   B C     1 
ATOM   9125  O  O     . PHE   B  1  20   ? 16.458  6.443   81.747  1.00 25.26 ? 18   PHE   B O     1 
ATOM   9126  C  CB    . PHE   B  1  20   ? 16.942  8.636   80.057  1.00 19.92 ? 18   PHE   B CB    1 
ATOM   9127  C  CG    . PHE   B  1  20   ? 17.126  10.056  79.643  1.00 17.40 ? 18   PHE   B CG    1 
ATOM   9128  C  CD1   . PHE   B  1  20   ? 16.785  11.088  80.499  1.00 18.33 ? 18   PHE   B CD1   1 
ATOM   9129  C  CD2   . PHE   B  1  20   ? 17.646  10.361  78.392  1.00 19.82 ? 18   PHE   B CD2   1 
ATOM   9130  C  CE1   . PHE   B  1  20   ? 16.951  12.406  80.125  1.00 20.57 ? 18   PHE   B CE1   1 
ATOM   9131  C  CE2   . PHE   B  1  20   ? 17.813  11.683  78.011  1.00 18.58 ? 18   PHE   B CE2   1 
ATOM   9132  C  CZ    . PHE   B  1  20   ? 17.462  12.702  78.875  1.00 19.54 ? 18   PHE   B CZ    1 
ATOM   9133  N  N     . ALA   B  1  21   ? 18.630  5.872   81.691  1.00 26.76 ? 19   ALA   B N     1 
ATOM   9134  C  CA    . ALA   B  1  21   ? 18.357  4.496   82.091  1.00 26.90 ? 19   ALA   B CA    1 
ATOM   9135  C  C     . ALA   B  1  21   ? 17.811  4.404   83.507  1.00 31.30 ? 19   ALA   B C     1 
ATOM   9136  O  O     . ALA   B  1  21   ? 17.208  3.387   83.866  1.00 35.12 ? 19   ALA   B O     1 
ATOM   9137  C  CB    . ALA   B  1  21   ? 19.624  3.651   81.966  1.00 32.91 ? 19   ALA   B CB    1 
ATOM   9138  N  N     . ASP   B  1  22   ? 18.002  5.436   84.314  1.00 23.53 ? 20   ASP   B N     1 
ATOM   9139  C  CA    . ASP   B  1  22   ? 17.485  5.447   85.672  1.00 25.09 ? 20   ASP   B CA    1 
ATOM   9140  C  C     . ASP   B  1  22   ? 16.737  6.738   85.919  1.00 21.47 ? 20   ASP   B C     1 
ATOM   9141  O  O     . ASP   B  1  22   ? 16.838  7.342   86.992  1.00 22.95 ? 20   ASP   B O     1 
ATOM   9142  C  CB    . ASP   B  1  22   ? 18.606  5.250   86.686  1.00 30.91 ? 20   ASP   B CB    1 
ATOM   9143  N  N     . PHE   B  1  23   ? 15.982  7.190   84.917  1.00 19.22 ? 21   PHE   B N     1 
ATOM   9144  C  CA    . PHE   B  1  23   ? 15.408  8.530   84.997  1.00 18.45 ? 21   PHE   B CA    1 
ATOM   9145  C  C     . PHE   B  1  23   ? 14.455  8.666   86.179  1.00 17.92 ? 21   PHE   B C     1 
ATOM   9146  O  O     . PHE   B  1  23   ? 14.620  9.554   87.019  1.00 17.88 ? 21   PHE   B O     1 
ATOM   9147  C  CB    . PHE   B  1  23   ? 14.715  8.911   83.697  1.00 18.33 ? 21   PHE   B CB    1 
ATOM   9148  C  CG    . PHE   B  1  23   ? 14.033  10.228  83.771  1.00 16.83 ? 21   PHE   B CG    1 
ATOM   9149  C  CD1   . PHE   B  1  23   ? 14.776  11.384  83.894  1.00 17.53 ? 21   PHE   B CD1   1 
ATOM   9150  C  CD2   . PHE   B  1  23   ? 12.651  10.312  83.751  1.00 19.09 ? 21   PHE   B CD2   1 
ATOM   9151  C  CE1   . PHE   B  1  23   ? 14.151  12.623  83.992  1.00 17.90 ? 21   PHE   B CE1   1 
ATOM   9152  C  CE2   . PHE   B  1  23   ? 12.026  11.542  83.853  1.00 18.08 ? 21   PHE   B CE2   1 
ATOM   9153  C  CZ    . PHE   B  1  23   ? 12.780  12.694  83.974  1.00 18.80 ? 21   PHE   B CZ    1 
ATOM   9154  N  N     . ALA   B  1  24   ? 13.446  7.810   86.247  1.00 17.91 ? 22   ALA   B N     1 
ATOM   9155  C  CA    . ALA   B  1  24   ? 12.467  7.932   87.325  1.00 18.51 ? 22   ALA   B CA    1 
ATOM   9156  C  C     . ALA   B  1  24   ? 11.745  6.614   87.558  1.00 17.18 ? 22   ALA   B C     1 
ATOM   9157  O  O     . ALA   B  1  24   ? 10.515  6.556   87.445  1.00 18.98 ? 22   ALA   B O     1 
ATOM   9158  C  CB    . ALA   B  1  24   ? 11.445  9.017   86.985  1.00 21.04 ? 22   ALA   B CB    1 
ATOM   9159  N  N     . PRO   B  1  25   ? 12.454  5.542   87.889  1.00 18.87 ? 23   PRO   B N     1 
ATOM   9160  C  CA    . PRO   B  1  25   ? 11.790  4.258   88.079  1.00 21.88 ? 23   PRO   B CA    1 
ATOM   9161  C  C     . PRO   B  1  25   ? 10.818  4.345   89.239  1.00 21.49 ? 23   PRO   B C     1 
ATOM   9162  O  O     . PRO   B  1  25   ? 11.119  4.976   90.258  1.00 20.52 ? 23   PRO   B O     1 
ATOM   9163  C  CB    . PRO   B  1  25   ? 12.954  3.311   88.403  1.00 24.52 ? 23   PRO   B CB    1 
ATOM   9164  C  CG    . PRO   B  1  25   ? 14.002  4.181   88.974  1.00 23.88 ? 23   PRO   B CG    1 
ATOM   9165  C  CD    . PRO   B  1  25   ? 13.885  5.482   88.231  1.00 21.48 ? 23   PRO   B CD    1 
ATOM   9166  N  N     . PRO   B  1  26   ? 9.635   3.759   89.112  1.00 19.36 ? 24   PRO   B N     1 
ATOM   9167  C  CA    . PRO   B  1  26   ? 8.672   3.811   90.214  1.00 19.87 ? 24   PRO   B CA    1 
ATOM   9168  C  C     . PRO   B  1  26   ? 9.153   2.989   91.394  1.00 21.69 ? 24   PRO   B C     1 
ATOM   9169  O  O     . PRO   B  1  26   ? 9.978   2.082   91.266  1.00 21.58 ? 24   PRO   B O     1 
ATOM   9170  C  CB    . PRO   B  1  26   ? 7.402   3.205   89.607  1.00 23.11 ? 24   PRO   B CB    1 
ATOM   9171  C  CG    . PRO   B  1  26   ? 7.894   2.315   88.533  1.00 23.27 ? 24   PRO   B CG    1 
ATOM   9172  C  CD    . PRO   B  1  26   ? 9.123   2.990   87.966  1.00 22.48 ? 24   PRO   B CD    1 
ATOM   9173  N  N     . VAL   B  1  27   ? 8.622   3.338   92.565  1.00 21.80 ? 25   VAL   B N     1 
ATOM   9174  C  CA    . VAL   B  1  27   ? 8.961   2.605   93.780  1.00 21.01 ? 25   VAL   B CA    1 
ATOM   9175  C  C     . VAL   B  1  27   ? 8.612   1.133   93.629  1.00 20.35 ? 25   VAL   B C     1 
ATOM   9176  O  O     . VAL   B  1  27   ? 9.352   0.252   94.089  1.00 23.44 ? 25   VAL   B O     1 
ATOM   9177  C  CB    . VAL   B  1  27   ? 8.242   3.232   94.985  1.00 20.79 ? 25   VAL   B CB    1 
ATOM   9178  C  CG1   . VAL   B  1  27   ? 8.383   2.324   96.198  1.00 24.31 ? 25   VAL   B CG1   1 
ATOM   9179  C  CG2   . VAL   B  1  27   ? 8.811   4.596   95.273  1.00 22.16 ? 25   VAL   B CG2   1 
ATOM   9180  N  N     . ARG   B  1  28   ? 7.495   0.840   92.984  1.00 20.59 ? 26   ARG   B N     1 
ATOM   9181  C  CA    . ARG   B  1  28   ? 7.067   -0.537  92.808  1.00 22.02 ? 26   ARG   B CA    1 
ATOM   9182  C  C     . ARG   B  1  28   ? 6.272   -0.623  91.519  1.00 24.06 ? 26   ARG   B C     1 
ATOM   9183  O  O     . ARG   B  1  28   ? 5.785   0.397   91.017  1.00 22.22 ? 26   ARG   B O     1 
ATOM   9184  C  CB    . ARG   B  1  28   ? 6.205   -0.998  93.992  1.00 23.38 ? 26   ARG   B CB    1 
ATOM   9185  C  CG    . ARG   B  1  28   ? 4.844   -0.313  94.051  1.00 24.45 ? 26   ARG   B CG    1 
ATOM   9186  C  CD    . ARG   B  1  28   ? 4.088   -0.671  95.330  1.00 26.31 ? 26   ARG   B CD    1 
ATOM   9187  N  NE    . ARG   B  1  28   ? 4.712   -0.073  96.504  1.00 26.25 ? 26   ARG   B NE    1 
ATOM   9188  C  CZ    . ARG   B  1  28   ? 5.474   -0.732  97.368  1.00 31.61 ? 26   ARG   B CZ    1 
ATOM   9189  N  NH1   . ARG   B  1  28   ? 5.724   -2.023  97.227  1.00 32.33 ? 26   ARG   B NH1   1 
ATOM   9190  N  NH2   . ARG   B  1  28   ? 5.996   -0.078  98.401  1.00 28.97 ? 26   ARG   B NH2   1 
ATOM   9191  N  N     . PRO   B  1  29   ? 6.141   -1.815  90.941  1.00 23.21 ? 27   PRO   B N     1 
ATOM   9192  C  CA    . PRO   B  1  29   ? 5.263   -1.956  89.778  1.00 22.39 ? 27   PRO   B CA    1 
ATOM   9193  C  C     . PRO   B  1  29   ? 3.848   -1.547  90.150  1.00 21.72 ? 27   PRO   B C     1 
ATOM   9194  O  O     . PRO   B  1  29   ? 3.352   -1.861  91.234  1.00 24.17 ? 27   PRO   B O     1 
ATOM   9195  C  CB    . PRO   B  1  29   ? 5.362   -3.446  89.432  1.00 25.61 ? 27   PRO   B CB    1 
ATOM   9196  C  CG    . PRO   B  1  29   ? 6.707   -3.859  89.998  1.00 28.34 ? 27   PRO   B CG    1 
ATOM   9197  C  CD    . PRO   B  1  29   ? 6.837   -3.073  91.267  1.00 25.90 ? 27   PRO   B CD    1 
ATOM   9198  N  N     . GLN   B  1  30   ? 3.211   -0.809  89.251  1.00 22.74 ? 28   GLN   B N     1 
ATOM   9199  C  CA    . GLN   B  1  30   ? 1.908   -0.224  89.540  1.00 23.64 ? 28   GLN   B CA    1 
ATOM   9200  C  C     . GLN   B  1  30   ? 0.817   -1.260  89.303  1.00 21.20 ? 28   GLN   B C     1 
ATOM   9201  O  O     . GLN   B  1  30   ? 0.631   -1.729  88.171  1.00 24.32 ? 28   GLN   B O     1 
ATOM   9202  C  CB    . GLN   B  1  30   ? 1.690   0.999   88.652  1.00 21.36 ? 28   GLN   B CB    1 
ATOM   9203  C  CG    . GLN   B  1  30   ? 2.774   2.056   88.804  1.00 21.07 ? 28   GLN   B CG    1 
ATOM   9204  C  CD    . GLN   B  1  30   ? 2.746   2.726   90.168  1.00 20.93 ? 28   GLN   B CD    1 
ATOM   9205  O  OE1   . GLN   B  1  30   ? 1.850   3.520   90.459  1.00 22.23 ? 28   GLN   B OE1   1 
ATOM   9206  N  NE2   . GLN   B  1  30   ? 3.725   2.410   91.013  1.00 20.34 ? 28   GLN   B NE2   1 
ATOM   9207  N  N     . SER   B  1  31   ? 0.093   -1.607  90.365  1.00 21.68 ? 29   SER   B N     1 
ATOM   9208  C  CA    . SER   B  1  31   ? -1.002  -2.555  90.278  1.00 21.40 ? 29   SER   B CA    1 
ATOM   9209  C  C     . SER   B  1  31   ? -2.175  -1.946  89.514  1.00 21.34 ? 29   SER   B C     1 
ATOM   9210  O  O     . SER   B  1  31   ? -2.211  -0.751  89.217  1.00 21.05 ? 29   SER   B O     1 
ATOM   9211  C  CB    . SER   B  1  31   ? -1.487  -2.914  91.677  1.00 22.62 ? 29   SER   B CB    1 
ATOM   9212  O  OG    . SER   B  1  31   ? -2.096  -1.783  92.276  1.00 22.51 ? 29   SER   B OG    1 
ATOM   9213  N  N     . THR   B  1  32   ? -3.143  -2.801  89.181  1.00 22.02 ? 30   THR   B N     1 
ATOM   9214  C  CA    . THR   B  1  32   ? -4.375  -2.323  88.558  1.00 21.73 ? 30   THR   B CA    1 
ATOM   9215  C  C     . THR   B  1  32   ? -5.022  -1.223  89.392  1.00 20.56 ? 30   THR   B C     1 
ATOM   9216  O  O     . THR   B  1  32   ? -5.413  -0.177  88.859  1.00 22.14 ? 30   THR   B O     1 
ATOM   9217  C  CB    . THR   B  1  32   ? -5.334  -3.499  88.383  1.00 24.31 ? 30   THR   B CB    1 
ATOM   9218  O  OG1   . THR   B  1  32   ? -4.735  -4.459  87.504  1.00 30.28 ? 30   THR   B OG1   1 
ATOM   9219  C  CG2   . THR   B  1  32   ? -6.672  -3.038  87.808  1.00 26.05 ? 30   THR   B CG2   1 
ATOM   9220  N  N     . LEU   B  1  33   ? -5.104  -1.418  90.710  1.00 21.87 ? 31   LEU   B N     1 
ATOM   9221  C  CA    . LEU   B  1  33   ? -5.716  -0.394  91.547  1.00 20.32 ? 31   LEU   B CA    1 
ATOM   9222  C  C     . LEU   B  1  33   ? -4.883  0.879   91.584  1.00 20.55 ? 31   LEU   B C     1 
ATOM   9223  O  O     . LEU   B  1  33   ? -5.438  1.982   91.592  1.00 19.18 ? 31   LEU   B O     1 
ATOM   9224  C  CB    . LEU   B  1  33   ? -5.958  -0.935  92.954  1.00 20.72 ? 31   LEU   B CB    1 
ATOM   9225  C  CG    . LEU   B  1  33   ? -7.039  -2.004  92.953  1.00 22.55 ? 31   LEU   B CG    1 
ATOM   9226  C  CD1   . LEU   B  1  33   ? -7.105  -2.692  94.301  1.00 23.64 ? 31   LEU   B CD1   1 
ATOM   9227  C  CD2   . LEU   B  1  33   ? -8.378  -1.381  92.593  1.00 27.73 ? 31   LEU   B CD2   1 
ATOM   9228  N  N     . ARG   B  1  34   ? -3.554  0.759   91.635  1.00 18.89 ? 32   ARG   B N     1 
ATOM   9229  C  CA    . ARG   B  1  34   ? -2.737  1.970   91.612  1.00 18.27 ? 32   ARG   B CA    1 
ATOM   9230  C  C     . ARG   B  1  34   ? -2.873  2.688   90.279  1.00 18.39 ? 32   ARG   B C     1 
ATOM   9231  O  O     . ARG   B  1  34   ? -2.902  3.921   90.232  1.00 18.52 ? 32   ARG   B O     1 
ATOM   9232  C  CB    . ARG   B  1  34   ? -1.269  1.657   91.899  1.00 17.73 ? 32   ARG   B CB    1 
ATOM   9233  C  CG    . ARG   B  1  34   ? -0.975  1.225   93.334  1.00 19.83 ? 32   ARG   B CG    1 
ATOM   9234  C  CD    . ARG   B  1  34   ? -1.044  2.395   94.310  1.00 20.34 ? 32   ARG   B CD    1 
ATOM   9235  N  NE    . ARG   B  1  34   ? -0.016  3.387   94.035  1.00 19.75 ? 32   ARG   B NE    1 
ATOM   9236  C  CZ    . ARG   B  1  34   ? 1.199   3.375   94.564  1.00 20.84 ? 32   ARG   B CZ    1 
ATOM   9237  N  NH1   . ARG   B  1  34   ? 1.561   2.451   95.441  1.00 21.70 ? 32   ARG   B NH1   1 
ATOM   9238  N  NH2   . ARG   B  1  34   ? 2.068   4.315   94.210  1.00 21.06 ? 32   ARG   B NH2   1 
ATOM   9239  N  N     . ARG   B  1  35   ? -2.957  1.931   89.187  1.00 18.61 ? 33   ARG   B N     1 
ATOM   9240  C  CA    . ARG   B  1  35   ? -3.092  2.555   87.878  1.00 20.09 ? 33   ARG   B CA    1 
ATOM   9241  C  C     . ARG   B  1  35   ? -4.414  3.287   87.750  1.00 18.69 ? 33   ARG   B C     1 
ATOM   9242  O  O     . ARG   B  1  35   ? -4.480  4.336   87.105  1.00 18.57 ? 33   ARG   B O     1 
ATOM   9243  C  CB    . ARG   B  1  35   ? -2.971  1.495   86.790  1.00 20.27 ? 33   ARG   B CB    1 
ATOM   9244  C  CG    . ARG   B  1  35   ? -1.548  1.044   86.620  1.00 21.81 ? 33   ARG   B CG    1 
ATOM   9245  C  CD    . ARG   B  1  35   ? -1.436  0.001   85.518  1.00 27.73 ? 33   ARG   B CD    1 
ATOM   9246  N  NE    . ARG   B  1  35   ? -0.076  -0.515  85.447  1.00 36.02 ? 33   ARG   B NE    1 
ATOM   9247  C  CZ    . ARG   B  1  35   ? 0.936   0.119   84.868  1.00 43.10 ? 33   ARG   B CZ    1 
ATOM   9248  N  NH1   . ARG   B  1  35   ? 0.768   1.284   84.263  1.00 43.83 ? 33   ARG   B NH1   1 
ATOM   9249  N  NH2   . ARG   B  1  35   ? 2.150   -0.425  84.908  1.00 40.71 ? 33   ARG   B NH2   1 
ATOM   9250  N  N     . ALA   B  1  36   ? -5.471  2.754   88.365  1.00 18.24 ? 34   ALA   B N     1 
ATOM   9251  C  CA    . ALA   B  1  36   ? -6.760  3.430   88.315  1.00 19.41 ? 34   ALA   B CA    1 
ATOM   9252  C  C     . ALA   B  1  36   ? -6.721  4.747   89.079  1.00 19.43 ? 34   ALA   B C     1 
ATOM   9253  O  O     . ALA   B  1  36   ? -7.394  5.707   88.695  1.00 20.97 ? 34   ALA   B O     1 
ATOM   9254  C  CB    . ALA   B  1  36   ? -7.871  2.513   88.832  1.00 20.00 ? 34   ALA   B CB    1 
ATOM   9255  N  N     . ILE   B  1  37   ? -5.928  4.817   90.150  1.00 17.86 ? 35   ILE   B N     1 
ATOM   9256  C  CA    . ILE   B  1  37   ? -5.709  6.092   90.821  1.00 18.25 ? 35   ILE   B CA    1 
ATOM   9257  C  C     . ILE   B  1  37   ? -5.041  7.076   89.876  1.00 19.31 ? 35   ILE   B C     1 
ATOM   9258  O  O     . ILE   B  1  37   ? -5.531  8.189   89.657  1.00 16.59 ? 35   ILE   B O     1 
ATOM   9259  C  CB    . ILE   B  1  37   ? -4.871  5.878   92.091  1.00 17.11 ? 35   ILE   B CB    1 
ATOM   9260  C  CG1   . ILE   B  1  37   ? -5.658  5.051   93.112  1.00 17.32 ? 35   ILE   B CG1   1 
ATOM   9261  C  CG2   . ILE   B  1  37   ? -4.399  7.231   92.650  1.00 17.27 ? 35   ILE   B CG2   1 
ATOM   9262  C  CD1   . ILE   B  1  37   ? -4.746  4.463   94.203  1.00 18.17 ? 35   ILE   B CD1   1 
ATOM   9263  N  N     . THR   B  1  38   ? -3.906  6.681   89.297  1.00 16.17 ? 36   THR   B N     1 
ATOM   9264  C  CA    . THR   B  1  38   ? -3.163  7.608   88.457  1.00 17.38 ? 36   THR   B CA    1 
ATOM   9265  C  C     . THR   B  1  38   ? -4.003  8.069   87.280  1.00 18.11 ? 36   THR   B C     1 
ATOM   9266  O  O     . THR   B  1  38   ? -3.939  9.238   86.888  1.00 18.07 ? 36   THR   B O     1 
ATOM   9267  C  CB    . THR   B  1  38   ? -1.881  6.937   87.969  1.00 16.94 ? 36   THR   B CB    1 
ATOM   9268  O  OG1   . THR   B  1  38   ? -1.193  6.402   89.108  1.00 17.33 ? 36   THR   B OG1   1 
ATOM   9269  C  CG2   . THR   B  1  38   ? -0.989  7.942   87.252  1.00 21.57 ? 36   THR   B CG2   1 
ATOM   9270  N  N     . ALA   B  1  39   ? -4.807  7.166   86.722  1.00 16.93 ? 37   ALA   B N     1 
ATOM   9271  C  CA    . ALA   B  1  39   ? -5.622  7.508   85.562  1.00 17.08 ? 37   ALA   B CA    1 
ATOM   9272  C  C     . ALA   B  1  39   ? -6.599  8.632   85.873  1.00 19.48 ? 37   ALA   B C     1 
ATOM   9273  O  O     . ALA   B  1  39   ? -7.005  9.369   84.967  1.00 20.42 ? 37   ALA   B O     1 
ATOM   9274  C  CB    . ALA   B  1  39   ? -6.374  6.267   85.081  1.00 20.13 ? 37   ALA   B CB    1 
ATOM   9275  N  N     . ALA   B  1  40   ? -6.985  8.787   87.134  1.00 17.66 ? 38   ALA   B N     1 
ATOM   9276  C  CA    . ALA   B  1  40   ? -7.984  9.772   87.518  1.00 18.45 ? 38   ALA   B CA    1 
ATOM   9277  C  C     . ALA   B  1  40   ? -7.370  11.110  87.890  1.00 16.94 ? 38   ALA   B C     1 
ATOM   9278  O  O     . ALA   B  1  40   ? -8.114  12.055  88.169  1.00 17.66 ? 38   ALA   B O     1 
ATOM   9279  C  CB    . ALA   B  1  40   ? -8.805  9.250   88.699  1.00 20.16 ? 38   ALA   B CB    1 
ATOM   9280  N  N     . TYR   B  1  41   ? -6.038  11.207  87.890  1.00 17.53 ? 39   TYR   B N     1 
ATOM   9281  C  CA    . TYR   B  1  41   ? -5.344  12.338  88.505  1.00 17.19 ? 39   TYR   B CA    1 
ATOM   9282  C  C     . TYR   B  1  41   ? -5.941  13.675  88.072  1.00 16.20 ? 39   TYR   B C     1 
ATOM   9283  O  O     . TYR   B  1  41   ? -6.276  14.518  88.913  1.00 16.87 ? 39   TYR   B O     1 
ATOM   9284  C  CB    . TYR   B  1  41   ? -3.864  12.241  88.131  1.00 16.38 ? 39   TYR   B CB    1 
ATOM   9285  C  CG    . TYR   B  1  41   ? -2.872  12.944  89.022  1.00 16.74 ? 39   TYR   B CG    1 
ATOM   9286  C  CD1   . TYR   B  1  41   ? -3.198  14.086  89.746  1.00 17.33 ? 39   TYR   B CD1   1 
ATOM   9287  C  CD2   . TYR   B  1  41   ? -1.582  12.460  89.118  1.00 17.88 ? 39   TYR   B CD2   1 
ATOM   9288  C  CE1   . TYR   B  1  41   ? -2.246  14.731  90.534  1.00 16.72 ? 39   TYR   B CE1   1 
ATOM   9289  C  CE2   . TYR   B  1  41   ? -0.630  13.086  89.899  1.00 17.10 ? 39   TYR   B CE2   1 
ATOM   9290  C  CZ    . TYR   B  1  41   ? -0.961  14.225  90.600  1.00 16.77 ? 39   TYR   B CZ    1 
ATOM   9291  O  OH    . TYR   B  1  41   ? -0.005  14.841  91.374  1.00 17.12 ? 39   TYR   B OH    1 
ATOM   9292  N  N     . ARG   B  1  42   ? -6.105  13.881  86.764  1.00 17.29 ? 40   ARG   B N     1 
ATOM   9293  C  CA    . ARG   B  1  42   ? -6.603  15.152  86.244  1.00 16.78 ? 40   ARG   B CA    1 
ATOM   9294  C  C     . ARG   B  1  42   ? -7.797  14.932  85.345  1.00 18.52 ? 40   ARG   B C     1 
ATOM   9295  O  O     . ARG   B  1  42   ? -7.991  15.642  84.357  1.00 20.08 ? 40   ARG   B O     1 
ATOM   9296  C  CB    . ARG   B  1  42   ? -5.503  15.952  85.559  1.00 18.62 ? 40   ARG   B CB    1 
ATOM   9297  C  CG    . ARG   B  1  42   ? -4.421  16.332  86.558  1.00 18.77 ? 40   ARG   B CG    1 
ATOM   9298  C  CD    . ARG   B  1  42   ? -3.213  16.985  85.940  1.00 18.05 ? 40   ARG   B CD    1 
ATOM   9299  N  NE    . ARG   B  1  42   ? -2.117  16.906  86.890  1.00 18.10 ? 40   ARG   B NE    1 
ATOM   9300  C  CZ    . ARG   B  1  42   ? -1.905  17.756  87.882  1.00 18.67 ? 40   ARG   B CZ    1 
ATOM   9301  N  NH1   . ARG   B  1  42   ? -2.647  18.842  88.036  1.00 18.11 ? 40   ARG   B NH1   1 
ATOM   9302  N  NH2   . ARG   B  1  42   ? -0.931  17.503  88.748  1.00 17.00 ? 40   ARG   B NH2   1 
ATOM   9303  N  N     . ARG   B  1  43   ? -8.618  13.951  85.695  1.00 17.03 ? 41   ARG   B N     1 
ATOM   9304  C  CA    . ARG   B  1  43   ? -9.769  13.601  84.875  1.00 18.58 ? 41   ARG   B CA    1 
ATOM   9305  C  C     . ARG   B  1  43   ? -10.705 14.800  84.777  1.00 19.40 ? 41   ARG   B C     1 
ATOM   9306  O  O     . ARG   B  1  43   ? -10.892 15.521  85.758  1.00 18.51 ? 41   ARG   B O     1 
ATOM   9307  C  CB    . ARG   B  1  43   ? -10.512 12.426  85.518  1.00 17.24 ? 41   ARG   B CB    1 
ATOM   9308  C  CG    . ARG   B  1  43   ? -11.767 11.981  84.784  1.00 18.62 ? 41   ARG   B CG    1 
ATOM   9309  C  CD    . ARG   B  1  43   ? -12.203 10.625  85.295  1.00 21.31 ? 41   ARG   B CD    1 
ATOM   9310  N  NE    . ARG   B  1  43   ? -11.220 9.617   84.914  1.00 21.09 ? 41   ARG   B NE    1 
ATOM   9311  C  CZ    . ARG   B  1  43   ? -10.979 8.506   85.598  1.00 24.46 ? 41   ARG   B CZ    1 
ATOM   9312  N  NH1   . ARG   B  1  43   ? -11.635 8.223   86.708  1.00 22.34 ? 41   ARG   B NH1   1 
ATOM   9313  N  NH2   . ARG   B  1  43   ? -10.052 7.662   85.156  1.00 21.16 ? 41   ARG   B NH2   1 
ATOM   9314  N  N     . PRO   B  1  44   ? -11.295 15.054  83.618  1.00 18.55 ? 42   PRO   B N     1 
ATOM   9315  C  CA    . PRO   B  1  44   ? -12.207 16.192  83.502  1.00 19.10 ? 42   PRO   B CA    1 
ATOM   9316  C  C     . PRO   B  1  44   ? -13.307 16.117  84.543  1.00 18.59 ? 42   PRO   B C     1 
ATOM   9317  O  O     . PRO   B  1  44   ? -13.830 15.047  84.867  1.00 18.29 ? 42   PRO   B O     1 
ATOM   9318  C  CB    . PRO   B  1  44   ? -12.767 16.048  82.086  1.00 20.09 ? 42   PRO   B CB    1 
ATOM   9319  C  CG    . PRO   B  1  44   ? -11.608 15.443  81.341  1.00 24.54 ? 42   PRO   B CG    1 
ATOM   9320  C  CD    . PRO   B  1  44   ? -11.020 14.442  82.310  1.00 20.48 ? 42   PRO   B CD    1 
ATOM   9321  N  N     . GLU   B  1  45   ? -13.649 17.286  85.073  1.00 19.95 ? 43   GLU   B N     1 
ATOM   9322  C  CA    . GLU   B  1  45   ? -14.651 17.362  86.114  1.00 19.05 ? 43   GLU   B CA    1 
ATOM   9323  C  C     . GLU   B  1  45   ? -15.982 16.778  85.649  1.00 20.02 ? 43   GLU   B C     1 
ATOM   9324  O  O     . GLU   B  1  45   ? -16.673 16.104  86.417  1.00 21.38 ? 43   GLU   B O     1 
ATOM   9325  C  CB    . GLU   B  1  45   ? -14.776 18.818  86.540  1.00 24.06 ? 43   GLU   B CB    1 
ATOM   9326  C  CG    . GLU   B  1  45   ? -15.186 18.971  87.954  1.00 25.58 ? 43   GLU   B CG    1 
ATOM   9327  C  CD    . GLU   B  1  45   ? -14.647 20.230  88.592  1.00 18.69 ? 43   GLU   B CD    1 
ATOM   9328  O  OE1   . GLU   B  1  45   ? -13.826 20.956  87.989  1.00 18.58 ? 43   GLU   B OE1   1 
ATOM   9329  O  OE2   . GLU   B  1  45   ? -15.094 20.487  89.714  1.00 19.10 ? 43   GLU   B OE2   1 
ATOM   9330  N  N     . THR   B  1  46   ? -16.338 16.984  84.375  1.00 20.14 ? 44   THR   B N     1 
ATOM   9331  C  CA    . THR   B  1  46   ? -17.576 16.427  83.842  1.00 20.60 ? 44   THR   B CA    1 
ATOM   9332  C  C     . THR   B  1  46   ? -17.560 14.905  83.773  1.00 20.35 ? 44   THR   B C     1 
ATOM   9333  O  O     . THR   B  1  46   ? -18.629 14.290  83.739  1.00 23.78 ? 44   THR   B O     1 
ATOM   9334  C  CB    . THR   B  1  46   ? -17.848 16.982  82.448  1.00 21.41 ? 44   THR   B CB    1 
ATOM   9335  O  OG1   . THR   B  1  46   ? -16.684 16.801  81.631  1.00 21.87 ? 44   THR   B OG1   1 
ATOM   9336  C  CG2   . THR   B  1  46   ? -18.182 18.458  82.520  1.00 23.16 ? 44   THR   B CG2   1 
ATOM   9337  N  N     . GLU   B  1  47   ? -16.380 14.286  83.726  1.00 20.93 ? 45   GLU   B N     1 
ATOM   9338  C  CA    . GLU   B  1  47   ? -16.307 12.834  83.806  1.00 20.86 ? 45   GLU   B CA    1 
ATOM   9339  C  C     . GLU   B  1  47   ? -16.316 12.334  85.241  1.00 21.81 ? 45   GLU   B C     1 
ATOM   9340  O  O     . GLU   B  1  47   ? -16.814 11.237  85.505  1.00 24.22 ? 45   GLU   B O     1 
ATOM   9341  C  CB    . GLU   B  1  47   ? -15.047 12.326  83.098  1.00 21.10 ? 45   GLU   B CB    1 
ATOM   9342  C  CG    . GLU   B  1  47   ? -15.036 12.571  81.604  1.00 27.95 ? 45   GLU   B CG    1 
ATOM   9343  C  CD    . GLU   B  1  47   ? -13.727 12.165  80.969  1.00 30.22 ? 45   GLU   B CD    1 
ATOM   9344  O  OE1   . GLU   B  1  47   ? -13.074 11.235  81.493  1.00 32.88 ? 45   GLU   B OE1   1 
ATOM   9345  O  OE2   . GLU   B  1  47   ? -13.353 12.787  79.956  1.00 36.10 ? 45   GLU   B OE2   1 
ATOM   9346  N  N     . CYS   B  1  48   ? -15.780 13.125  86.173  1.00 19.13 ? 46   CYS   B N     1 
ATOM   9347  C  CA    . CYS   B  1  48   ? -15.703 12.676  87.559  1.00 20.92 ? 46   CYS   B CA    1 
ATOM   9348  C  C     . CYS   B  1  48   ? -17.065 12.658  88.222  1.00 19.66 ? 46   CYS   B C     1 
ATOM   9349  O  O     . CYS   B  1  48   ? -17.363 11.763  89.023  1.00 20.44 ? 46   CYS   B O     1 
ATOM   9350  C  CB    . CYS   B  1  48   ? -14.810 13.610  88.363  1.00 18.61 ? 46   CYS   B CB    1 
ATOM   9351  S  SG    . CYS   B  1  48   ? -13.078 13.554  87.906  1.00 20.05 ? 46   CYS   B SG    1 
ATOM   9352  N  N     . LEU   B  1  49   ? -17.878 13.656  87.942  1.00 18.99 ? 47   LEU   B N     1 
ATOM   9353  C  CA    . LEU   B  1  49   ? -19.076 13.870  88.744  1.00 20.91 ? 47   LEU   B CA    1 
ATOM   9354  C  C     . LEU   B  1  49   ? -20.177 12.826  88.594  1.00 20.26 ? 47   LEU   B C     1 
ATOM   9355  O  O     . LEU   B  1  49   ? -20.757 12.429  89.604  1.00 21.21 ? 47   LEU   B O     1 
ATOM   9356  C  CB    . LEU   B  1  49   ? -19.619 15.296  88.603  1.00 21.21 ? 47   LEU   B CB    1 
ATOM   9357  C  CG    . LEU   B  1  49   ? -19.132 16.222  89.732  1.00 19.65 ? 47   LEU   B CG    1 
ATOM   9358  C  CD1   . LEU   B  1  49   ? -19.617 15.747  91.114  1.00 22.01 ? 47   LEU   B CD1   1 
ATOM   9359  C  CD2   . LEU   B  1  49   ? -17.615 16.324  89.717  1.00 20.95 ? 47   LEU   B CD2   1 
ATOM   9360  N  N     . PRO   B  1  50   ? -20.528 12.367  87.392  1.00 21.48 ? 48   PRO   B N     1 
ATOM   9361  C  CA    . PRO   B  1  50   ? -21.679 11.449  87.279  1.00 22.73 ? 48   PRO   B CA    1 
ATOM   9362  C  C     . PRO   B  1  50   ? -21.548 10.196  88.136  1.00 23.65 ? 48   PRO   B C     1 
ATOM   9363  O  O     . PRO   B  1  50   ? -22.506 9.840   88.831  1.00 23.53 ? 48   PRO   B O     1 
ATOM   9364  C  CB    . PRO   B  1  50   ? -21.735 11.136  85.775  1.00 22.23 ? 48   PRO   B CB    1 
ATOM   9365  C  CG    . PRO   B  1  50   ? -21.250 12.398  85.159  1.00 21.28 ? 48   PRO   B CG    1 
ATOM   9366  C  CD    . PRO   B  1  50   ? -20.121 12.874  86.069  1.00 20.19 ? 48   PRO   B CD    1 
ATOM   9367  N  N     . PRO   B  1  51   ? -20.399 9.501   88.167  1.00 22.64 ? 49   PRO   B N     1 
ATOM   9368  C  CA    . PRO   B  1  51   ? -20.337 8.339   89.070  1.00 22.74 ? 49   PRO   B CA    1 
ATOM   9369  C  C     . PRO   B  1  51   ? -20.436 8.708   90.539  1.00 21.03 ? 49   PRO   B C     1 
ATOM   9370  O  O     . PRO   B  1  51   ? -20.974 7.921   91.328  1.00 22.94 ? 49   PRO   B O     1 
ATOM   9371  C  CB    . PRO   B  1  51   ? -19.003 7.662   88.731  1.00 25.33 ? 49   PRO   B CB    1 
ATOM   9372  C  CG    . PRO   B  1  51   ? -18.209 8.694   88.020  1.00 27.50 ? 49   PRO   B CG    1 
ATOM   9373  C  CD    . PRO   B  1  51   ? -19.197 9.578   87.312  1.00 22.75 ? 49   PRO   B CD    1 
ATOM   9374  N  N     . LEU   B  1  52   ? -19.942 9.887   90.925  1.00 22.84 ? 50   LEU   B N     1 
ATOM   9375  C  CA    . LEU   B  1  52   ? -20.061 10.321  92.311  1.00 20.85 ? 50   LEU   B CA    1 
ATOM   9376  C  C     . LEU   B  1  52   ? -21.509 10.638  92.662  1.00 24.10 ? 50   LEU   B C     1 
ATOM   9377  O  O     . LEU   B  1  52   ? -21.984 10.276  93.742  1.00 21.90 ? 50   LEU   B O     1 
ATOM   9378  C  CB    . LEU   B  1  52   ? -19.177 11.545  92.544  1.00 21.11 ? 50   LEU   B CB    1 
ATOM   9379  C  CG    . LEU   B  1  52   ? -17.681 11.347  92.321  1.00 18.83 ? 50   LEU   B CG    1 
ATOM   9380  C  CD1   . LEU   B  1  52   ? -16.966 12.681  92.377  1.00 20.70 ? 50   LEU   B CD1   1 
ATOM   9381  C  CD2   . LEU   B  1  52   ? -17.134 10.399  93.368  1.00 21.71 ? 50   LEU   B CD2   1 
ATOM   9382  N  N     . VAL   B  1  53   ? -22.226 11.314  91.760  1.00 22.41 ? 51   VAL   B N     1 
ATOM   9383  C  CA    . VAL   B  1  53   ? -23.651 11.567  91.989  1.00 22.01 ? 51   VAL   B CA    1 
ATOM   9384  C  C     . VAL   B  1  53   ? -24.392 10.253  92.198  1.00 24.42 ? 51   VAL   B C     1 
ATOM   9385  O  O     . VAL   B  1  53   ? -25.204 10.113  93.121  1.00 23.91 ? 51   VAL   B O     1 
ATOM   9386  C  CB    . VAL   B  1  53   ? -24.248 12.371  90.818  1.00 23.16 ? 51   VAL   B CB    1 
ATOM   9387  C  CG1   . VAL   B  1  53   ? -25.786 12.355  90.874  1.00 23.46 ? 51   VAL   B CG1   1 
ATOM   9388  C  CG2   . VAL   B  1  53   ? -23.726 13.785  90.817  1.00 22.29 ? 51   VAL   B CG2   1 
ATOM   9389  N  N     . GLU   B  1  54   ? -24.103 9.263   91.348  1.00 23.63 ? 52   GLU   B N     1 
ATOM   9390  C  CA    . GLU   B  1  54   ? -24.747 7.961   91.486  1.00 26.63 ? 52   GLU   B CA    1 
ATOM   9391  C  C     . GLU   B  1  54   ? -24.424 7.329   92.831  1.00 26.09 ? 52   GLU   B C     1 
ATOM   9392  O  O     . GLU   B  1  54   ? -25.322 6.862   93.540  1.00 27.00 ? 52   GLU   B O     1 
ATOM   9393  C  CB    . GLU   B  1  54   ? -24.330 7.043   90.336  1.00 30.35 ? 52   GLU   B CB    1 
ATOM   9394  N  N     . ALA   B  1  55   ? -23.141 7.329   93.217  1.00 24.04 ? 53   ALA   B N     1 
ATOM   9395  C  CA    . ALA   B  1  55   ? -22.755 6.709   94.483  1.00 26.28 ? 53   ALA   B CA    1 
ATOM   9396  C  C     . ALA   B  1  55   ? -23.321 7.456   95.686  1.00 24.90 ? 53   ALA   B C     1 
ATOM   9397  O  O     . ALA   B  1  55   ? -23.574 6.841   96.728  1.00 27.50 ? 53   ALA   B O     1 
ATOM   9398  C  CB    . ALA   B  1  55   ? -21.229 6.620   94.585  1.00 27.54 ? 53   ALA   B CB    1 
ATOM   9399  N  N     . ALA   B  1  56   ? -23.514 8.769   95.570  1.00 24.40 ? 54   ALA   B N     1 
ATOM   9400  C  CA    . ALA   B  1  56   ? -24.005 9.590   96.670  1.00 24.53 ? 54   ALA   B CA    1 
ATOM   9401  C  C     . ALA   B  1  56   ? -25.521 9.637   96.756  1.00 25.74 ? 54   ALA   B C     1 
ATOM   9402  O  O     . ALA   B  1  56   ? -26.053 10.267  97.676  1.00 27.97 ? 54   ALA   B O     1 
ATOM   9403  C  CB    . ALA   B  1  56   ? -23.481 11.021  96.534  1.00 26.60 ? 54   ALA   B CB    1 
ATOM   9404  N  N     . THR   B  1  57   ? -26.227 9.001   95.827  1.00 25.95 ? 55   THR   B N     1 
ATOM   9405  C  CA    . THR   B  1  57   ? -27.681 9.069   95.818  1.00 29.66 ? 55   THR   B CA    1 
ATOM   9406  C  C     . THR   B  1  57   ? -28.264 8.337   97.017  1.00 30.77 ? 55   THR   B C     1 
ATOM   9407  O  O     . THR   B  1  57   ? -27.831 7.237   97.364  1.00 31.70 ? 55   THR   B O     1 
ATOM   9408  C  CB    . THR   B  1  57   ? -28.205 8.458   94.524  1.00 31.15 ? 55   THR   B CB    1 
ATOM   9409  O  OG1   . THR   B  1  57   ? -27.786 9.272   93.428  1.00 31.27 ? 55   THR   B OG1   1 
ATOM   9410  C  CG2   . THR   B  1  57   ? -29.727 8.384   94.544  1.00 29.89 ? 55   THR   B CG2   1 
ATOM   9411  N  N     . GLN   B  1  58   ? -29.242 8.971   97.662  1.00 32.21 ? 56   GLN   B N     1 
ATOM   9412  C  CA    . GLN   B  1  58   ? -29.975 8.374   98.765  1.00 29.62 ? 56   GLN   B CA    1 
ATOM   9413  C  C     . GLN   B  1  58   ? -31.469 8.513   98.500  1.00 33.45 ? 56   GLN   B C     1 
ATOM   9414  O  O     . GLN   B  1  58   ? -31.910 9.391   97.751  1.00 31.66 ? 56   GLN   B O     1 
ATOM   9415  C  CB    . GLN   B  1  58   ? -29.612 9.032   100.102 1.00 33.06 ? 56   GLN   B CB    1 
ATOM   9416  C  CG    . GLN   B  1  58   ? -28.108 9.155   100.340 1.00 30.16 ? 56   GLN   B CG    1 
ATOM   9417  C  CD    . GLN   B  1  58   ? -27.759 9.178   101.816 1.00 34.53 ? 56   GLN   B CD    1 
ATOM   9418  O  OE1   . GLN   B  1  58   ? -27.883 8.165   102.504 1.00 38.87 ? 56   GLN   B OE1   1 
ATOM   9419  N  NE2   . GLN   B  1  58   ? -27.327 10.332  102.312 1.00 33.48 ? 56   GLN   B NE2   1 
ATOM   9420  N  N     . SER   B  1  59   ? -32.242 7.631   99.131  1.00 38.43 ? 57   SER   B N     1 
ATOM   9421  C  CA    . SER   B  1  59   ? -33.689 7.612   98.960  1.00 35.29 ? 57   SER   B CA    1 
ATOM   9422  C  C     . SER   B  1  59   ? -34.312 8.910   99.461  1.00 37.13 ? 57   SER   B C     1 
ATOM   9423  O  O     . SER   B  1  59   ? -33.717 9.659   100.238 1.00 34.73 ? 57   SER   B O     1 
ATOM   9424  C  CB    . SER   B  1  59   ? -34.295 6.466   99.769  1.00 36.06 ? 57   SER   B CB    1 
ATOM   9425  O  OG    . SER   B  1  59   ? -34.085 6.676   101.159 1.00 38.94 ? 57   SER   B OG    1 
ATOM   9426  N  N     . LYS   B  1  60   ? -35.547 9.162   99.020  1.00 35.11 ? 58   LYS   B N     1 
ATOM   9427  C  CA    . LYS   B  1  60   ? -36.262 10.348  99.480  1.00 39.12 ? 58   LYS   B CA    1 
ATOM   9428  C  C     . LYS   B  1  60   ? -36.400 10.343  100.993 1.00 35.95 ? 58   LYS   B C     1 
ATOM   9429  O  O     . LYS   B  1  60   ? -36.268 11.389  101.639 1.00 36.06 ? 58   LYS   B O     1 
ATOM   9430  C  CB    . LYS   B  1  60   ? -37.648 10.413  98.833  1.00 36.34 ? 58   LYS   B CB    1 
ATOM   9431  N  N     . GLU   B  1  61   ? -36.664 9.173   101.574 1.00 35.03 ? 59   GLU   B N     1 
ATOM   9432  C  CA    . GLU   B  1  61   ? -36.855 9.089   103.017 1.00 35.55 ? 59   GLU   B CA    1 
ATOM   9433  C  C     . GLU   B  1  61   ? -35.598 9.531   103.752 1.00 36.18 ? 59   GLU   B C     1 
ATOM   9434  O  O     . GLU   B  1  61   ? -35.654 10.369  104.658 1.00 37.04 ? 59   GLU   B O     1 
ATOM   9435  C  CB    . GLU   B  1  61   ? -37.239 7.663   103.410 1.00 41.20 ? 59   GLU   B CB    1 
ATOM   9436  N  N     . ILE   B  1  62   ? -34.447 8.991   103.351 1.00 35.30 ? 60   ILE   B N     1 
ATOM   9437  C  CA    . ILE   B  1  62   ? -33.190 9.336   104.009 1.00 34.41 ? 60   ILE   B CA    1 
ATOM   9438  C  C     . ILE   B  1  62   ? -32.847 10.804  103.784 1.00 31.98 ? 60   ILE   B C     1 
ATOM   9439  O  O     . ILE   B  1  62   ? -32.352 11.488  104.690 1.00 36.03 ? 60   ILE   B O     1 
ATOM   9440  C  CB    . ILE   B  1  62   ? -32.073 8.386   103.538 1.00 39.71 ? 60   ILE   B CB    1 
ATOM   9441  C  CG1   . ILE   B  1  62   ? -32.313 6.986   104.103 1.00 43.61 ? 60   ILE   B CG1   1 
ATOM   9442  C  CG2   . ILE   B  1  62   ? -30.702 8.914   103.932 1.00 41.21 ? 60   ILE   B CG2   1 
ATOM   9443  C  CD1   . ILE   B  1  62   ? -31.340 5.954   103.598 1.00 41.43 ? 60   ILE   B CD1   1 
ATOM   9444  N  N     . ARG   B  1  63   ? -33.114 11.317  102.580 1.00 31.61 ? 61   ARG   B N     1 
ATOM   9445  C  CA    . ARG   B  1  63   ? -32.822 12.718  102.296 1.00 31.09 ? 61   ARG   B CA    1 
ATOM   9446  C  C     . ARG   B  1  63   ? -33.664 13.649  103.154 1.00 33.51 ? 61   ARG   B C     1 
ATOM   9447  O  O     . ARG   B  1  63   ? -33.158 14.654  103.665 1.00 36.18 ? 61   ARG   B O     1 
ATOM   9448  C  CB    . ARG   B  1  63   ? -33.014 13.015  100.809 1.00 34.24 ? 61   ARG   B CB    1 
ATOM   9449  C  CG    . ARG   B  1  63   ? -31.940 12.381  99.948  1.00 36.27 ? 61   ARG   B CG    1 
ATOM   9450  C  CD    . ARG   B  1  63   ? -32.007 12.828  98.501  1.00 41.99 ? 61   ARG   B CD    1 
ATOM   9451  N  NE    . ARG   B  1  63   ? -33.168 12.307  97.791  1.00 37.58 ? 61   ARG   B NE    1 
ATOM   9452  C  CZ    . ARG   B  1  63   ? -34.146 13.062  97.313  1.00 43.63 ? 61   ARG   B CZ    1 
ATOM   9453  N  NH1   . ARG   B  1  63   ? -34.156 14.374  97.492  1.00 45.04 ? 61   ARG   B NH1   1 
ATOM   9454  N  NH2   . ARG   B  1  63   ? -35.132 12.490  96.629  1.00 46.38 ? 61   ARG   B NH2   1 
ATOM   9455  N  N     . ASP   B  1  64   ? -34.957 13.351  103.307 1.00 31.33 ? 62   ASP   B N     1 
ATOM   9456  C  CA    . ASP   B  1  64   ? -35.781 14.168  104.190 1.00 33.39 ? 62   ASP   B CA    1 
ATOM   9457  C  C     . ASP   B  1  64   ? -35.302 14.062  105.631 1.00 27.65 ? 62   ASP   B C     1 
ATOM   9458  O  O     . ASP   B  1  64   ? -35.243 15.067  106.347 1.00 38.97 ? 62   ASP   B O     1 
ATOM   9459  C  CB    . ASP   B  1  64   ? -37.250 13.752  104.097 1.00 33.53 ? 62   ASP   B CB    1 
ATOM   9460  C  CG    . ASP   B  1  64   ? -37.837 13.976  102.720 1.00 39.80 ? 62   ASP   B CG    1 
ATOM   9461  O  OD1   . ASP   B  1  64   ? -37.258 14.749  101.926 1.00 41.92 ? 62   ASP   B OD1   1 
ATOM   9462  O  OD2   . ASP   B  1  64   ? -38.905 13.384  102.445 1.00 41.88 ? 62   ASP   B OD2   1 
ATOM   9463  N  N     . ALA   B  1  65   ? -34.982 12.846  106.081 1.00 30.86 ? 63   ALA   B N     1 
ATOM   9464  C  CA    . ALA   B  1  65   ? -34.512 12.665  107.451 1.00 31.06 ? 63   ALA   B CA    1 
ATOM   9465  C  C     . ALA   B  1  65   ? -33.195 13.396  107.684 1.00 36.10 ? 63   ALA   B C     1 
ATOM   9466  O  O     . ALA   B  1  65   ? -33.004 14.028  108.730 1.00 38.12 ? 63   ALA   B O     1 
ATOM   9467  C  CB    . ALA   B  1  65   ? -34.378 11.175  107.771 1.00 33.32 ? 63   ALA   B CB    1 
ATOM   9468  N  N     . ALA   B  1  66   ? -32.279 13.329  106.716 1.00 34.03 ? 64   ALA   B N     1 
ATOM   9469  C  CA    . ALA   B  1  66   ? -31.010 14.042  106.845 1.00 32.00 ? 64   ALA   B CA    1 
ATOM   9470  C  C     . ALA   B  1  66   ? -31.218 15.551  106.831 1.00 32.78 ? 64   ALA   B C     1 
ATOM   9471  O  O     . ALA   B  1  66   ? -30.565 16.280  107.586 1.00 35.39 ? 64   ALA   B O     1 
ATOM   9472  C  CB    . ALA   B  1  66   ? -30.054 13.611  105.737 1.00 30.96 ? 64   ALA   B CB    1 
ATOM   9473  N  N     . ALA   B  1  67   ? -32.148 16.036  106.006 1.00 33.42 ? 65   ALA   B N     1 
ATOM   9474  C  CA    . ALA   B  1  67   ? -32.415 17.470  105.973 1.00 32.11 ? 65   ALA   B CA    1 
ATOM   9475  C  C     . ALA   B  1  67   ? -32.951 17.959  107.314 1.00 37.28 ? 65   ALA   B C     1 
ATOM   9476  O  O     . ALA   B  1  67   ? -32.623 19.069  107.754 1.00 35.87 ? 65   ALA   B O     1 
ATOM   9477  C  CB    . ALA   B  1  67   ? -33.401 17.790  104.849 1.00 34.97 ? 65   ALA   B CB    1 
ATOM   9478  N  N     . SER   B  1  68   ? -33.777 17.143  107.979 1.00 37.29 ? 66   SER   B N     1 
ATOM   9479  C  CA    A SER   B  1  68   ? -34.296 17.522  109.290 0.37 36.44 ? 66   SER   B CA    1 
ATOM   9480  C  CA    B SER   B  1  68   ? -34.297 17.520  109.291 0.63 36.39 ? 66   SER   B CA    1 
ATOM   9481  C  C     . SER   B  1  68   ? -33.212 17.441  110.359 1.00 37.71 ? 66   SER   B C     1 
ATOM   9482  O  O     . SER   B  1  68   ? -33.148 18.294  111.252 1.00 35.23 ? 66   SER   B O     1 
ATOM   9483  C  CB    A SER   B  1  68   ? -35.490 16.644  109.660 0.37 42.23 ? 66   SER   B CB    1 
ATOM   9484  C  CB    B SER   B  1  68   ? -35.481 16.630  109.664 0.63 42.30 ? 66   SER   B CB    1 
ATOM   9485  O  OG    A SER   B  1  68   ? -35.116 15.280  109.745 0.37 40.94 ? 66   SER   B OG    1 
ATOM   9486  O  OG    B SER   B  1  68   ? -36.537 16.767  108.732 0.63 44.50 ? 66   SER   B OG    1 
ATOM   9487  N  N     . THR   B  1  69   ? -32.358 16.416  110.295 1.00 36.39 ? 67   THR   B N     1 
ATOM   9488  C  CA    . THR   B  1  69   ? -31.251 16.331  111.241 1.00 33.76 ? 67   THR   B CA    1 
ATOM   9489  C  C     . THR   B  1  69   ? -30.301 17.505  111.063 1.00 33.76 ? 67   THR   B C     1 
ATOM   9490  O  O     . THR   B  1  69   ? -29.844 18.101  112.048 1.00 31.50 ? 67   THR   B O     1 
ATOM   9491  C  CB    . THR   B  1  69   ? -30.507 15.009  111.066 1.00 33.37 ? 67   THR   B CB    1 
ATOM   9492  O  OG1   . THR   B  1  69   ? -31.316 13.933  111.550 1.00 35.45 ? 67   THR   B OG1   1 
ATOM   9493  C  CG2   . THR   B  1  69   ? -29.193 15.027  111.839 1.00 32.58 ? 67   THR   B CG2   1 
ATOM   9494  N  N     . ALA   B  1  70   ? -29.986 17.847  109.809 1.00 32.03 ? 68   ALA   B N     1 
ATOM   9495  C  CA    . ALA   B  1  70   ? -29.143 19.008  109.549 1.00 34.63 ? 68   ALA   B CA    1 
ATOM   9496  C  C     . ALA   B  1  70   ? -29.788 20.284  110.071 1.00 33.63 ? 68   ALA   B C     1 
ATOM   9497  O  O     . ALA   B  1  70   ? -29.103 21.141  110.638 1.00 33.31 ? 68   ALA   B O     1 
ATOM   9498  C  CB    . ALA   B  1  70   ? -28.828 19.120  108.054 1.00 32.89 ? 68   ALA   B CB    1 
ATOM   9499  N  N     . ARG   B  1  71   ? -31.108 20.425  109.900 1.00 35.61 ? 69   ARG   B N     1 
ATOM   9500  C  CA    A ARG   B  1  71   ? -31.805 21.600  110.417 0.49 37.37 ? 69   ARG   B CA    1 
ATOM   9501  C  CA    B ARG   B  1  71   ? -31.788 21.608  110.415 0.51 37.38 ? 69   ARG   B CA    1 
ATOM   9502  C  C     . ARG   B  1  71   ? -31.657 21.694  111.929 1.00 28.99 ? 69   ARG   B C     1 
ATOM   9503  O  O     . ARG   B  1  71   ? -31.343 22.759  112.472 1.00 35.80 ? 69   ARG   B O     1 
ATOM   9504  C  CB    A ARG   B  1  71   ? -33.283 21.533  110.032 0.49 37.22 ? 69   ARG   B CB    1 
ATOM   9505  C  CB    B ARG   B  1  71   ? -33.259 21.617  109.993 0.51 37.23 ? 69   ARG   B CB    1 
ATOM   9506  C  CG    A ARG   B  1  71   ? -34.181 22.463  110.835 0.49 37.68 ? 69   ARG   B CG    1 
ATOM   9507  C  CG    B ARG   B  1  71   ? -34.082 22.671  110.722 0.51 37.66 ? 69   ARG   B CG    1 
ATOM   9508  C  CD    A ARG   B  1  71   ? -34.589 23.681  110.024 0.49 37.52 ? 69   ARG   B CD    1 
ATOM   9509  C  CD    B ARG   B  1  71   ? -35.469 22.851  110.117 0.51 36.77 ? 69   ARG   B CD    1 
ATOM   9510  N  NE    A ARG   B  1  71   ? -35.338 23.313  108.829 0.49 36.98 ? 69   ARG   B NE    1 
ATOM   9511  N  NE    B ARG   B  1  71   ? -35.421 23.541  108.832 0.51 37.05 ? 69   ARG   B NE    1 
ATOM   9512  C  CZ    A ARG   B  1  71   ? -35.629 24.149  107.842 0.49 38.73 ? 69   ARG   B CZ    1 
ATOM   9513  C  CZ    B ARG   B  1  71   ? -35.281 24.852  108.689 0.51 39.92 ? 69   ARG   B CZ    1 
ATOM   9514  N  NH1   A ARG   B  1  71   ? -35.257 25.419  107.880 0.49 40.97 ? 69   ARG   B NH1   1 
ATOM   9515  N  NH1   B ARG   B  1  71   ? -35.157 25.653  109.735 0.51 34.15 ? 69   ARG   B NH1   1 
ATOM   9516  N  NH2   A ARG   B  1  71   ? -36.304 23.699  106.789 0.49 37.75 ? 69   ARG   B NH2   1 
ATOM   9517  N  NH2   B ARG   B  1  71   ? -35.258 25.373  107.464 0.51 41.22 ? 69   ARG   B NH2   1 
ATOM   9518  N  N     . LYS   B  1  72   ? -31.877 20.575  112.621 1.00 32.59 ? 70   LYS   B N     1 
ATOM   9519  C  CA    . LYS   B  1  72   ? -31.756 20.551  114.074 1.00 32.38 ? 70   LYS   B CA    1 
ATOM   9520  C  C     . LYS   B  1  72   ? -30.351 20.945  114.514 1.00 35.89 ? 70   LYS   B C     1 
ATOM   9521  O  O     . LYS   B  1  72   ? -30.181 21.717  115.465 1.00 35.98 ? 70   LYS   B O     1 
ATOM   9522  C  CB    . LYS   B  1  72   ? -32.119 19.159  114.588 1.00 33.60 ? 70   LYS   B CB    1 
ATOM   9523  C  CG    . LYS   B  1  72   ? -32.044 18.975  116.101 1.00 36.46 ? 70   LYS   B CG    1 
ATOM   9524  C  CD    . LYS   B  1  72   ? -32.599 17.601  116.494 1.00 31.37 ? 70   LYS   B CD    1 
ATOM   9525  C  CE    . LYS   B  1  72   ? -32.458 17.316  117.980 1.00 39.70 ? 70   LYS   B CE    1 
ATOM   9526  N  NZ    . LYS   B  1  72   ? -33.287 18.206  118.831 1.00 38.14 ? 70   LYS   B NZ    1 
ATOM   9527  N  N     . LEU   B  1  73   ? -29.327 20.447  113.815 1.00 34.21 ? 71   LEU   B N     1 
ATOM   9528  C  CA    . LEU   B  1  73   ? -27.960 20.797  114.184 1.00 32.11 ? 71   LEU   B CA    1 
ATOM   9529  C  C     . LEU   B  1  73   ? -27.693 22.282  113.978 1.00 28.67 ? 71   LEU   B C     1 
ATOM   9530  O  O     . LEU   B  1  73   ? -27.068 22.928  114.826 1.00 32.79 ? 71   LEU   B O     1 
ATOM   9531  C  CB    . LEU   B  1  73   ? -26.972 19.962  113.372 1.00 29.65 ? 71   LEU   B CB    1 
ATOM   9532  C  CG    . LEU   B  1  73   ? -27.045 18.455  113.604 1.00 31.73 ? 71   LEU   B CG    1 
ATOM   9533  C  CD1   . LEU   B  1  73   ? -26.205 17.720  112.555 1.00 29.46 ? 71   LEU   B CD1   1 
ATOM   9534  C  CD2   . LEU   B  1  73   ? -26.580 18.110  115.007 1.00 32.75 ? 71   LEU   B CD2   1 
ATOM   9535  N  N     . ILE   B  1  74   ? -28.171 22.839  112.863 1.00 31.64 ? 72   ILE   B N     1 
ATOM   9536  C  CA    . ILE   B  1  74   ? -27.854 24.218  112.505 1.00 32.17 ? 72   ILE   B CA    1 
ATOM   9537  C  C     . ILE   B  1  74   ? -28.567 25.195  113.429 1.00 41.74 ? 72   ILE   B C     1 
ATOM   9538  O  O     . ILE   B  1  74   ? -27.972 26.169  113.909 1.00 37.09 ? 72   ILE   B O     1 
ATOM   9539  C  CB    . ILE   B  1  74   ? -28.174 24.470  111.020 1.00 34.13 ? 72   ILE   B CB    1 
ATOM   9540  C  CG1   . ILE   B  1  74   ? -27.189 23.688  110.142 1.00 36.77 ? 72   ILE   B CG1   1 
ATOM   9541  C  CG2   . ILE   B  1  74   ? -28.098 25.954  110.698 1.00 34.10 ? 72   ILE   B CG2   1 
ATOM   9542  C  CD1   . ILE   B  1  74   ? -27.575 23.620  108.695 1.00 34.10 ? 72   ILE   B CD1   1 
ATOM   9543  N  N     . GLU   B  1  75   ? -29.853 24.957  113.688 1.00 40.57 ? 73   GLU   B N     1 
ATOM   9544  C  CA    . GLU   B  1  75   ? -30.567 25.774  114.663 1.00 42.10 ? 73   GLU   B CA    1 
ATOM   9545  C  C     . GLU   B  1  75   ? -29.887 25.721  116.027 1.00 39.43 ? 73   GLU   B C     1 
ATOM   9546  O  O     . GLU   B  1  75   ? -29.721 26.755  116.686 1.00 44.29 ? 73   GLU   B O     1 
ATOM   9547  C  CB    . GLU   B  1  75   ? -32.030 25.341  114.731 1.00 42.78 ? 73   GLU   B CB    1 
ATOM   9548  C  CG    . GLU   B  1  75   ? -32.786 25.593  113.431 1.00 45.76 ? 73   GLU   B CG    1 
ATOM   9549  C  CD    . GLU   B  1  75   ? -34.229 25.124  113.481 1.00 46.83 ? 73   GLU   B CD    1 
ATOM   9550  O  OE1   . GLU   B  1  75   ? -34.546 24.254  114.320 1.00 52.12 ? 73   GLU   B OE1   1 
ATOM   9551  O  OE2   . GLU   B  1  75   ? -35.044 25.626  112.677 1.00 45.56 ? 73   GLU   B OE2   1 
ATOM   9552  N  N     . ALA   B  1  76   ? -29.453 24.529  116.450 1.00 35.11 ? 74   ALA   B N     1 
ATOM   9553  C  CA    . ALA   B  1  76   ? -28.674 24.412  117.680 1.00 35.07 ? 74   ALA   B CA    1 
ATOM   9554  C  C     . ALA   B  1  76   ? -27.393 25.240  117.622 1.00 36.83 ? 74   ALA   B C     1 
ATOM   9555  O  O     . ALA   B  1  76   ? -27.020 25.888  118.608 1.00 39.61 ? 74   ALA   B O     1 
ATOM   9556  C  CB    . ALA   B  1  76   ? -28.367 22.944  117.976 1.00 38.28 ? 74   ALA   B CB    1 
ATOM   9557  N  N     . LEU   B  1  77   ? -26.703 25.231  116.476 1.00 33.50 ? 75   LEU   B N     1 
ATOM   9558  C  CA    . LEU   B  1  77   ? -25.488 26.026  116.325 1.00 38.25 ? 75   LEU   B CA    1 
ATOM   9559  C  C     . LEU   B  1  77   ? -25.788 27.520  116.378 1.00 35.98 ? 75   LEU   B C     1 
ATOM   9560  O  O     . LEU   B  1  77   ? -25.127 28.272  117.104 1.00 41.70 ? 75   LEU   B O     1 
ATOM   9561  C  CB    . LEU   B  1  77   ? -24.789 25.667  115.009 1.00 32.85 ? 75   LEU   B CB    1 
ATOM   9562  C  CG    . LEU   B  1  77   ? -24.008 24.355  114.970 1.00 37.32 ? 75   LEU   B CG    1 
ATOM   9563  C  CD1   . LEU   B  1  77   ? -23.490 24.082  113.566 1.00 32.70 ? 75   LEU   B CD1   1 
ATOM   9564  C  CD2   . LEU   B  1  77   ? -22.857 24.418  115.949 1.00 37.06 ? 75   LEU   B CD2   1 
ATOM   9565  N  N     . ARG   B  1  78   ? -26.767 27.975  115.597 1.00 37.11 ? 76   ARG   B N     1 
ATOM   9566  C  CA    . ARG   B  1  78   ? -27.059 29.402  115.537 1.00 36.09 ? 76   ARG   B CA    1 
ATOM   9567  C  C     . ARG   B  1  78   ? -27.753 29.917  116.788 1.00 36.66 ? 76   ARG   B C     1 
ATOM   9568  O  O     . ARG   B  1  78   ? -27.819 31.136  116.978 1.00 40.83 ? 76   ARG   B O     1 
ATOM   9569  C  CB    . ARG   B  1  78   ? -27.921 29.705  114.320 1.00 39.83 ? 76   ARG   B CB    1 
ATOM   9570  C  CG    . ARG   B  1  78   ? -27.223 29.366  113.028 1.00 37.56 ? 76   ARG   B CG    1 
ATOM   9571  C  CD    . ARG   B  1  78   ? -28.047 29.763  111.833 1.00 43.39 ? 76   ARG   B CD    1 
ATOM   9572  N  NE    . ARG   B  1  78   ? -27.198 30.352  110.807 1.00 39.00 ? 76   ARG   B NE    1 
ATOM   9573  C  CZ    . ARG   B  1  78   ? -27.615 30.713  109.603 1.00 43.92 ? 76   ARG   B CZ    1 
ATOM   9574  N  NH1   . ARG   B  1  78   ? -28.865 30.513  109.217 1.00 43.97 ? 76   ARG   B NH1   1 
ATOM   9575  N  NH2   . ARG   B  1  78   ? -26.758 31.291  108.767 1.00 42.74 ? 76   ARG   B NH2   1 
ATOM   9576  N  N     . GLY   B  1  79   ? -28.274 29.029  117.628 1.00 39.03 ? 77   GLY   B N     1 
ATOM   9577  C  CA    . GLY   B  1  79   ? -28.940 29.459  118.839 1.00 40.43 ? 77   GLY   B CA    1 
ATOM   9578  C  C     . GLY   B  1  79   ? -28.026 29.768  119.998 1.00 46.24 ? 77   GLY   B C     1 
ATOM   9579  O  O     . GLY   B  1  79   ? -28.499 30.288  121.011 1.00 40.17 ? 77   GLY   B O     1 
ATOM   9580  N  N     . LYS   B  1  80   ? -26.732 29.484  119.874 1.00 45.54 ? 78   LYS   B N     1 
ATOM   9581  C  CA    . LYS   B  1  80   ? -25.818 29.621  121.003 1.00 43.43 ? 78   LYS   B CA    1 
ATOM   9582  C  C     . LYS   B  1  80   ? -24.570 30.451  120.689 1.00 40.38 ? 78   LYS   B C     1 
ATOM   9583  O  O     . LYS   B  1  80   ? -24.257 30.723  119.526 1.00 44.50 ? 78   LYS   B O     1 
ATOM   9584  C  CB    . LYS   B  1  80   ? -25.427 28.235  121.529 1.00 46.87 ? 78   LYS   B CB    1 
ATOM   9585  C  CG    . LYS   B  1  80   ? -24.710 27.354  120.512 1.00 40.33 ? 78   LYS   B CG    1 
ATOM   9586  C  CD    . LYS   B  1  80   ? -24.711 25.892  120.951 1.00 39.13 ? 78   LYS   B CD    1 
ATOM   9587  C  CE    . LYS   B  1  80   ? -23.793 25.035  120.070 1.00 33.67 ? 78   LYS   B CE    1 
ATOM   9588  N  NZ    . LYS   B  1  80   ? -23.871 23.582  120.427 1.00 36.36 ? 78   LYS   B NZ    1 
ATOM   9589  N  N     . GLY   B  1  85   ? -15.074 35.740  121.235 1.00 44.18 ? 83   GLY   B N     1 
ATOM   9590  C  CA    . GLY   B  1  85   ? -14.364 36.545  122.210 1.00 40.05 ? 83   GLY   B CA    1 
ATOM   9591  C  C     . GLY   B  1  85   ? -13.795 37.817  121.609 1.00 38.64 ? 83   GLY   B C     1 
ATOM   9592  O  O     . GLY   B  1  85   ? -13.865 38.888  122.217 1.00 37.74 ? 83   GLY   B O     1 
ATOM   9593  N  N     . VAL   B  1  86   ? -13.225 37.694  120.408 1.00 40.17 ? 84   VAL   B N     1 
ATOM   9594  C  CA    . VAL   B  1  86   ? -12.689 38.864  119.720 1.00 40.83 ? 84   VAL   B CA    1 
ATOM   9595  C  C     . VAL   B  1  86   ? -13.802 39.852  119.391 1.00 36.85 ? 84   VAL   B C     1 
ATOM   9596  O  O     . VAL   B  1  86   ? -13.637 41.068  119.549 1.00 34.70 ? 84   VAL   B O     1 
ATOM   9597  C  CB    . VAL   B  1  86   ? -11.886 38.443  118.477 1.00 39.54 ? 84   VAL   B CB    1 
ATOM   9598  C  CG1   . VAL   B  1  86   ? -11.637 39.634  117.565 1.00 41.02 ? 84   VAL   B CG1   1 
ATOM   9599  C  CG2   . VAL   B  1  86   ? -10.570 37.843  118.899 1.00 44.83 ? 84   VAL   B CG2   1 
ATOM   9600  N  N     . GLU   B  1  87   ? -14.955 39.349  118.941 1.00 39.14 ? 85   GLU   B N     1 
ATOM   9601  C  CA    . GLU   B  1  87   ? -16.076 40.233  118.635 1.00 40.24 ? 85   GLU   B CA    1 
ATOM   9602  C  C     . GLU   B  1  87   ? -16.502 41.027  119.863 1.00 35.67 ? 85   GLU   B C     1 
ATOM   9603  O  O     . GLU   B  1  87   ? -16.808 42.221  119.766 1.00 37.01 ? 85   GLU   B O     1 
ATOM   9604  C  CB    . GLU   B  1  87   ? -17.249 39.421  118.083 1.00 46.81 ? 85   GLU   B CB    1 
ATOM   9605  N  N     . GLY   B  1  88   ? -16.518 40.386  121.033 1.00 35.02 ? 86   GLY   B N     1 
ATOM   9606  C  CA    . GLY   B  1  88   ? -16.884 41.099  122.246 1.00 36.53 ? 86   GLY   B CA    1 
ATOM   9607  C  C     . GLY   B  1  88   ? -15.863 42.154  122.625 1.00 31.79 ? 86   GLY   B C     1 
ATOM   9608  O  O     . GLY   B  1  88   ? -16.215 43.218  123.139 1.00 34.16 ? 86   GLY   B O     1 
ATOM   9609  N  N     . LEU   B  1  89   ? -14.583 41.876  122.366 1.00 32.81 ? 87   LEU   B N     1 
ATOM   9610  C  CA    . LEU   B  1  89   ? -13.541 42.862  122.630 1.00 32.74 ? 87   LEU   B CA    1 
ATOM   9611  C  C     . LEU   B  1  89   ? -13.681 44.056  121.694 1.00 28.71 ? 87   LEU   B C     1 
ATOM   9612  O  O     . LEU   B  1  89   ? -13.616 45.213  122.128 1.00 27.73 ? 87   LEU   B O     1 
ATOM   9613  C  CB    . LEU   B  1  89   ? -12.172 42.201  122.479 1.00 34.70 ? 87   LEU   B CB    1 
ATOM   9614  C  CG    . LEU   B  1  89   ? -10.936 43.095  122.512 1.00 36.22 ? 87   LEU   B CG    1 
ATOM   9615  C  CD1   . LEU   B  1  89   ? -10.834 43.795  123.847 1.00 41.06 ? 87   LEU   B CD1   1 
ATOM   9616  C  CD2   . LEU   B  1  89   ? -9.686  42.267  122.222 1.00 40.56 ? 87   LEU   B CD2   1 
ATOM   9617  N  N     . VAL   B  1  90   ? -13.908 43.786  120.408 1.00 30.73 ? 88   VAL   B N     1 
ATOM   9618  C  CA    . VAL   B  1  90   ? -14.115 44.852  119.432 1.00 31.94 ? 88   VAL   B CA    1 
ATOM   9619  C  C     . VAL   B  1  90   ? -15.327 45.693  119.808 1.00 34.60 ? 88   VAL   B C     1 
ATOM   9620  O  O     . VAL   B  1  90   ? -15.299 46.928  119.719 1.00 32.35 ? 88   VAL   B O     1 
ATOM   9621  C  CB    . VAL   B  1  90   ? -14.240 44.252  118.019 1.00 34.10 ? 88   VAL   B CB    1 
ATOM   9622  C  CG1   . VAL   B  1  90   ? -14.673 45.313  117.017 1.00 35.46 ? 88   VAL   B CG1   1 
ATOM   9623  C  CG2   . VAL   B  1  90   ? -12.930 43.613  117.596 1.00 30.68 ? 88   VAL   B CG2   1 
ATOM   9624  N  N     . GLN   B  1  91   ? -16.402 45.044  120.259 1.00 33.58 ? 89   GLN   B N     1 
ATOM   9625  C  CA    . GLN   B  1  91   ? -17.595 45.790  120.642 1.00 37.68 ? 89   GLN   B CA    1 
ATOM   9626  C  C     . GLN   B  1  91   ? -17.352 46.639  121.885 1.00 34.66 ? 89   GLN   B C     1 
ATOM   9627  O  O     . GLN   B  1  91   ? -17.761 47.804  121.936 1.00 36.69 ? 89   GLN   B O     1 
ATOM   9628  C  CB    . GLN   B  1  91   ? -18.769 44.833  120.847 1.00 43.40 ? 89   GLN   B CB    1 
ATOM   9629  N  N     . GLU   B  1  92   ? -16.669 46.085  122.891 1.00 33.54 ? 90   GLU   B N     1 
ATOM   9630  C  CA    . GLU   B  1  92   ? -16.515 46.795  124.157 1.00 34.05 ? 90   GLU   B CA    1 
ATOM   9631  C  C     . GLU   B  1  92   ? -15.676 48.056  124.004 1.00 30.89 ? 90   GLU   B C     1 
ATOM   9632  O  O     . GLU   B  1  92   ? -15.965 49.081  124.630 1.00 32.80 ? 90   GLU   B O     1 
ATOM   9633  C  CB    . GLU   B  1  92   ? -15.902 45.883  125.219 1.00 36.79 ? 90   GLU   B CB    1 
ATOM   9634  C  CG    . GLU   B  1  92   ? -15.659 46.609  126.533 1.00 36.61 ? 90   GLU   B CG    1 
ATOM   9635  C  CD    . GLU   B  1  92   ? -15.069 45.732  127.621 1.00 39.78 ? 90   GLU   B CD    1 
ATOM   9636  O  OE1   . GLU   B  1  92   ? -14.697 44.573  127.332 1.00 45.35 ? 90   GLU   B OE1   1 
ATOM   9637  O  OE2   . GLU   B  1  92   ? -14.977 46.216  128.767 1.00 38.32 ? 90   GLU   B OE2   1 
ATOM   9638  N  N     . TYR   B  1  93   ? -14.629 48.004  123.185 1.00 29.63 ? 91   TYR   B N     1 
ATOM   9639  C  CA    . TYR   B  1  93   ? -13.745 49.147  123.025 1.00 32.17 ? 91   TYR   B CA    1 
ATOM   9640  C  C     . TYR   B  1  93   ? -13.974 49.890  121.722 1.00 29.86 ? 91   TYR   B C     1 
ATOM   9641  O  O     . TYR   B  1  93   ? -13.180 50.773  121.382 1.00 29.60 ? 91   TYR   B O     1 
ATOM   9642  C  CB    . TYR   B  1  93   ? -12.285 48.733  123.189 1.00 28.95 ? 91   TYR   B CB    1 
ATOM   9643  C  CG    . TYR   B  1  93   ? -12.007 48.345  124.611 1.00 27.97 ? 91   TYR   B CG    1 
ATOM   9644  C  CD1   . TYR   B  1  93   ? -11.730 49.311  125.566 1.00 26.67 ? 91   TYR   B CD1   1 
ATOM   9645  C  CD2   . TYR   B  1  93   ? -12.068 47.019  125.009 1.00 29.98 ? 91   TYR   B CD2   1 
ATOM   9646  C  CE1   . TYR   B  1  93   ? -11.496 48.967  126.880 1.00 26.76 ? 91   TYR   B CE1   1 
ATOM   9647  C  CE2   . TYR   B  1  93   ? -11.835 46.663  126.327 1.00 31.65 ? 91   TYR   B CE2   1 
ATOM   9648  C  CZ    . TYR   B  1  93   ? -11.548 47.641  127.253 1.00 29.71 ? 91   TYR   B CZ    1 
ATOM   9649  O  OH    . TYR   B  1  93   ? -11.317 47.293  128.569 1.00 33.74 ? 91   TYR   B OH    1 
ATOM   9650  N  N     . SER   B  1  94   ? -15.051 49.566  121.007 1.00 26.35 ? 92   SER   B N     1 
ATOM   9651  C  CA    . SER   B  1  94   ? -15.413 50.251  119.774 1.00 27.30 ? 92   SER   B CA    1 
ATOM   9652  C  C     . SER   B  1  94   ? -14.240 50.267  118.807 1.00 26.68 ? 92   SER   B C     1 
ATOM   9653  O  O     . SER   B  1  94   ? -13.878 51.301  118.239 1.00 26.89 ? 92   SER   B O     1 
ATOM   9654  C  CB    . SER   B  1  94   ? -15.919 51.662  120.052 1.00 27.38 ? 92   SER   B CB    1 
ATOM   9655  O  OG    . SER   B  1  94   ? -17.025 51.621  120.931 1.00 31.83 ? 92   SER   B OG    1 
ATOM   9656  N  N     . LEU   B  1  95   ? -13.623 49.102  118.642 1.00 23.31 ? 93   LEU   B N     1 
ATOM   9657  C  CA    . LEU   B  1  95   ? -12.457 49.003  117.791 1.00 22.50 ? 93   LEU   B CA    1 
ATOM   9658  C  C     . LEU   B  1  95   ? -12.876 48.920  116.332 1.00 24.99 ? 93   LEU   B C     1 
ATOM   9659  O  O     . LEU   B  1  95   ? -13.853 48.252  115.981 1.00 26.31 ? 93   LEU   B O     1 
ATOM   9660  C  CB    . LEU   B  1  95   ? -11.657 47.754  118.145 1.00 24.60 ? 93   LEU   B CB    1 
ATOM   9661  C  CG    . LEU   B  1  95   ? -11.150 47.665  119.578 1.00 24.73 ? 93   LEU   B CG    1 
ATOM   9662  C  CD1   . LEU   B  1  95   ? -10.229 46.474  119.728 1.00 25.32 ? 93   LEU   B CD1   1 
ATOM   9663  C  CD2   . LEU   B  1  95   ? -10.454 48.962  119.961 1.00 24.85 ? 93   LEU   B CD2   1 
ATOM   9664  N  N     . SER   B  1  96   ? -12.117 49.589  115.473 1.00 21.53 ? 94   SER   B N     1 
ATOM   9665  C  CA    . SER   B  1  96   ? -12.201 49.298  114.062 1.00 22.23 ? 94   SER   B CA    1 
ATOM   9666  C  C     . SER   B  1  96   ? -11.511 47.965  113.790 1.00 23.39 ? 94   SER   B C     1 
ATOM   9667  O  O     . SER   B  1  96   ? -10.810 47.413  114.645 1.00 21.25 ? 94   SER   B O     1 
ATOM   9668  C  CB    . SER   B  1  96   ? -11.483 50.386  113.277 1.00 21.78 ? 94   SER   B CB    1 
ATOM   9669  O  OG    . SER   B  1  96   ? -10.088 50.310  113.533 1.00 19.86 ? 94   SER   B OG    1 
ATOM   9670  N  N     . SER   B  1  97   ? -11.699 47.443  112.582 1.00 21.37 ? 95   SER   B N     1 
ATOM   9671  C  CA    . SER   B  1  97   ? -11.040 46.195  112.226 1.00 22.12 ? 95   SER   B CA    1 
ATOM   9672  C  C     . SER   B  1  97   ? -9.530  46.322  112.358 1.00 21.21 ? 95   SER   B C     1 
ATOM   9673  O  O     . SER   B  1  97   ? -8.877  45.461  112.952 1.00 20.35 ? 95   SER   B O     1 
ATOM   9674  C  CB    . SER   B  1  97   ? -11.418 45.767  110.810 1.00 25.09 ? 95   SER   B CB    1 
ATOM   9675  O  OG    . SER   B  1  97   ? -12.810 45.512  110.755 1.00 30.58 ? 95   SER   B OG    1 
ATOM   9676  N  N     . GLN   B  1  98   ? -8.958  47.398  111.809 1.00 20.14 ? 96   GLN   B N     1 
ATOM   9677  C  CA    . GLN   B  1  98   ? -7.511  47.581  111.884 1.00 18.72 ? 96   GLN   B CA    1 
ATOM   9678  C  C     . GLN   B  1  98   ? -7.052  47.712  113.328 1.00 17.81 ? 96   GLN   B C     1 
ATOM   9679  O  O     . GLN   B  1  98   ? -5.972  47.231  113.687 1.00 18.97 ? 96   GLN   B O     1 
ATOM   9680  C  CB    . GLN   B  1  98   ? -7.079  48.808  111.075 1.00 19.23 ? 96   GLN   B CB    1 
ATOM   9681  C  CG    . GLN   B  1  98   ? -7.113  48.607  109.570 1.00 18.58 ? 96   GLN   B CG    1 
ATOM   9682  C  CD    . GLN   B  1  98   ? -6.148  47.541  109.113 1.00 19.98 ? 96   GLN   B CD    1 
ATOM   9683  O  OE1   . GLN   B  1  98   ? -6.448  46.347  109.176 1.00 24.03 ? 96   GLN   B OE1   1 
ATOM   9684  N  NE2   . GLN   B  1  98   ? -4.971  47.961  108.649 1.00 20.52 ? 96   GLN   B NE2   1 
ATOM   9685  N  N     . GLU   B  1  99   ? -7.851  48.363  114.170 1.00 18.41 ? 97   GLU   B N     1 
ATOM   9686  C  CA    . GLU   B  1  99   ? -7.496  48.450  115.580 1.00 19.33 ? 97   GLU   B CA    1 
ATOM   9687  C  C     . GLU   B  1  99   ? -7.539  47.083  116.237 1.00 22.10 ? 97   GLU   B C     1 
ATOM   9688  O  O     . GLU   B  1  99   ? -6.662  46.752  117.037 1.00 20.66 ? 97   GLU   B O     1 
ATOM   9689  C  CB    . GLU   B  1  99   ? -8.437  49.416  116.289 1.00 20.19 ? 97   GLU   B CB    1 
ATOM   9690  C  CG    . GLU   B  1  99   ? -8.138  50.867  115.965 1.00 19.95 ? 97   GLU   B CG    1 
ATOM   9691  C  CD    . GLU   B  1  99   ? -9.234  51.805  116.433 1.00 20.39 ? 97   GLU   B CD    1 
ATOM   9692  O  OE1   . GLU   B  1  99   ? -10.250 51.343  117.021 1.00 23.19 ? 97   GLU   B OE1   1 
ATOM   9693  O  OE2   . GLU   B  1  99   ? -9.073  53.029  116.264 1.00 21.46 ? 97   GLU   B OE2   1 
ATOM   9694  N  N     . GLY   B  1  100  ? -8.547  46.274  115.908 1.00 19.55 ? 98   GLY   B N     1 
ATOM   9695  C  CA    . GLY   B  1  100  ? -8.583  44.918  116.424 1.00 20.72 ? 98   GLY   B CA    1 
ATOM   9696  C  C     . GLY   B  1  100  ? -7.369  44.111  116.010 1.00 20.99 ? 98   GLY   B C     1 
ATOM   9697  O  O     . GLY   B  1  100  ? -6.775  43.406  116.829 1.00 20.07 ? 98   GLY   B O     1 
ATOM   9698  N  N     . VAL   B  1  101  ? -6.974  44.216  114.739 1.00 19.28 ? 99   VAL   B N     1 
ATOM   9699  C  CA    . VAL   B  1  101  ? -5.797  43.493  114.265 1.00 18.30 ? 99   VAL   B CA    1 
ATOM   9700  C  C     . VAL   B  1  101  ? -4.552  44.000  114.976 1.00 19.25 ? 99   VAL   B C     1 
ATOM   9701  O  O     . VAL   B  1  101  ? -3.717  43.216  115.458 1.00 19.91 ? 99   VAL   B O     1 
ATOM   9702  C  CB    . VAL   B  1  101  ? -5.664  43.631  112.738 1.00 19.38 ? 99   VAL   B CB    1 
ATOM   9703  C  CG1   . VAL   B  1  101  ? -4.369  43.015  112.256 1.00 21.37 ? 99   VAL   B CG1   1 
ATOM   9704  C  CG2   . VAL   B  1  101  ? -6.848  42.981  112.055 1.00 20.21 ? 99   VAL   B CG2   1 
ATOM   9705  N  N     . ALA   B  1  102  ? -4.396  45.324  115.031 1.00 18.09 ? 100  ALA   B N     1 
ATOM   9706  C  CA    . ALA   B  1  102  ? -3.201  45.897  115.638 1.00 18.89 ? 100  ALA   B CA    1 
ATOM   9707  C  C     . ALA   B  1  102  ? -3.102  45.488  117.093 1.00 19.25 ? 100  ALA   B C     1 
ATOM   9708  O  O     . ALA   B  1  102  ? -2.011  45.170  117.586 1.00 19.35 ? 100  ALA   B O     1 
ATOM   9709  C  CB    . ALA   B  1  102  ? -3.239  47.422  115.536 1.00 18.88 ? 100  ALA   B CB    1 
ATOM   9710  N  N     . LEU   B  1  103  ? -4.232  45.491  117.794 1.00 18.57 ? 101  LEU   B N     1 
ATOM   9711  C  CA    . LEU   B  1  103  ? -4.234  45.108  119.199 1.00 18.46 ? 101  LEU   B CA    1 
ATOM   9712  C  C     . LEU   B  1  103  ? -3.798  43.663  119.374 1.00 21.14 ? 101  LEU   B C     1 
ATOM   9713  O  O     . LEU   B  1  103  ? -3.029  43.346  120.295 1.00 20.75 ? 101  LEU   B O     1 
ATOM   9714  C  CB    . LEU   B  1  103  ? -5.633  45.304  119.774 1.00 19.44 ? 101  LEU   B CB    1 
ATOM   9715  C  CG    . LEU   B  1  103  ? -5.818  44.835  121.208 1.00 19.26 ? 101  LEU   B CG    1 
ATOM   9716  C  CD1   . LEU   B  1  103  ? -4.949  45.668  122.128 1.00 24.42 ? 101  LEU   B CD1   1 
ATOM   9717  C  CD2   . LEU   B  1  103  ? -7.282  44.944  121.593 1.00 21.86 ? 101  LEU   B CD2   1 
ATOM   9718  N  N     . MET   B  1  104  ? -4.301  42.768  118.531 1.00 19.77 ? 102  MET   B N     1 
ATOM   9719  C  CA    . MET   B  1  104  ? -3.912  41.368  118.648 1.00 22.21 ? 102  MET   B CA    1 
ATOM   9720  C  C     . MET   B  1  104  ? -2.439  41.178  118.334 1.00 20.69 ? 102  MET   B C     1 
ATOM   9721  O  O     . MET   B  1  104  ? -1.772  40.351  118.961 1.00 21.81 ? 102  MET   B O     1 
ATOM   9722  C  CB    . MET   B  1  104  ? -4.797  40.482  117.770 1.00 23.34 ? 102  MET   B CB    1 
ATOM   9723  C  CG    . MET   B  1  104  ? -6.263  40.535  118.175 1.00 24.07 ? 102  MET   B CG    1 
ATOM   9724  S  SD    . MET   B  1  104  ? -6.537  40.175  119.936 1.00 32.62 ? 102  MET   B SD    1 
ATOM   9725  C  CE    . MET   B  1  104  ? -6.279  38.408  119.913 1.00 41.24 ? 102  MET   B CE    1 
ATOM   9726  N  N     . CYS   B  1  105  ? -1.909  41.943  117.384 1.00 18.51 ? 103  CYS   B N     1 
ATOM   9727  C  CA    . CYS   B  1  105  ? -0.476  41.902  117.117 1.00 20.12 ? 103  CYS   B CA    1 
ATOM   9728  C  C     . CYS   B  1  105  ? 0.308   42.369  118.326 1.00 20.02 ? 103  CYS   B C     1 
ATOM   9729  O  O     . CYS   B  1  105  ? 1.328   41.771  118.691 1.00 21.85 ? 103  CYS   B O     1 
ATOM   9730  C  CB    . CYS   B  1  105  ? -0.140  42.803  115.941 1.00 18.46 ? 103  CYS   B CB    1 
ATOM   9731  S  SG    . CYS   B  1  105  ? -0.723  42.184  114.379 1.00 20.19 ? 103  CYS   B SG    1 
ATOM   9732  N  N     . LEU   B  1  106  ? -0.127  43.469  118.939 1.00 19.36 ? 104  LEU   B N     1 
ATOM   9733  C  CA    . LEU   B  1  106  ? 0.516   43.921  120.161 1.00 19.12 ? 104  LEU   B CA    1 
ATOM   9734  C  C     . LEU   B  1  106  ? 0.421   42.858  121.241 1.00 19.58 ? 104  LEU   B C     1 
ATOM   9735  O  O     . LEU   B  1  106  ? 1.405   42.593  121.946 1.00 22.32 ? 104  LEU   B O     1 
ATOM   9736  C  CB    . LEU   B  1  106  ? -0.123  45.225  120.640 1.00 20.34 ? 104  LEU   B CB    1 
ATOM   9737  C  CG    . LEU   B  1  106  ? 0.360   45.680  122.024 1.00 20.27 ? 104  LEU   B CG    1 
ATOM   9738  C  CD1   . LEU   B  1  106  ? 1.822   46.080  121.969 1.00 24.53 ? 104  LEU   B CD1   1 
ATOM   9739  C  CD2   . LEU   B  1  106  ? -0.488  46.801  122.586 1.00 23.72 ? 104  LEU   B CD2   1 
ATOM   9740  N  N     . ALA   B  1  107  ? -0.754  42.239  121.390 1.00 20.04 ? 105  ALA   B N     1 
ATOM   9741  C  CA    . ALA   B  1  107  ? -0.915  41.202  122.405 1.00 21.78 ? 105  ALA   B CA    1 
ATOM   9742  C  C     . ALA   B  1  107  ? 0.012   40.029  122.132 1.00 22.92 ? 105  ALA   B C     1 
ATOM   9743  O  O     . ALA   B  1  107  ? 0.667   39.530  123.053 1.00 23.93 ? 105  ALA   B O     1 
ATOM   9744  C  CB    . ALA   B  1  107  ? -2.362  40.725  122.433 1.00 22.51 ? 105  ALA   B CB    1 
ATOM   9745  N  N     . GLU   B  1  108  ? 0.098   39.592  120.872 1.00 23.15 ? 106  GLU   B N     1 
ATOM   9746  C  CA    . GLU   B  1  108  ? 1.008   38.512  120.504 1.00 23.53 ? 106  GLU   B CA    1 
ATOM   9747  C  C     . GLU   B  1  108  ? 2.436   38.842  120.914 1.00 27.38 ? 106  GLU   B C     1 
ATOM   9748  O  O     . GLU   B  1  108  ? 3.139   38.009  121.501 1.00 27.47 ? 106  GLU   B O     1 
ATOM   9749  C  CB    . GLU   B  1  108  ? 0.921   38.274  118.992 1.00 25.29 ? 106  GLU   B CB    1 
ATOM   9750  C  CG    . GLU   B  1  108  ? 2.015   37.369  118.412 1.00 29.14 ? 106  GLU   B CG    1 
ATOM   9751  C  CD    . GLU   B  1  108  ? 2.140   37.468  116.887 1.00 32.20 ? 106  GLU   B CD    1 
ATOM   9752  O  OE1   . GLU   B  1  108  ? 1.215   37.993  116.227 1.00 28.30 ? 106  GLU   B OE1   1 
ATOM   9753  O  OE2   . GLU   B  1  108  ? 3.183   37.038  116.339 1.00 32.75 ? 106  GLU   B OE2   1 
ATOM   9754  N  N     . ALA   B  1  109  ? 2.876   40.069  120.636 1.00 23.27 ? 107  ALA   B N     1 
ATOM   9755  C  CA    . ALA   B  1  109  ? 4.234   40.458  120.993 1.00 24.49 ? 107  ALA   B CA    1 
ATOM   9756  C  C     . ALA   B  1  109  ? 4.420   40.467  122.506 1.00 25.63 ? 107  ALA   B C     1 
ATOM   9757  O  O     . ALA   B  1  109  ? 5.443   39.992  123.017 1.00 26.53 ? 107  ALA   B O     1 
ATOM   9758  C  CB    . ALA   B  1  109  ? 4.566   41.821  120.386 1.00 24.78 ? 107  ALA   B CB    1 
ATOM   9759  N  N     . LEU   B  1  110  ? 3.440   40.995  123.241 1.00 24.03 ? 108  LEU   B N     1 
ATOM   9760  C  CA    . LEU   B  1  110  ? 3.553   41.021  124.694 1.00 23.50 ? 108  LEU   B CA    1 
ATOM   9761  C  C     . LEU   B  1  110  ? 3.595   39.617  125.282 1.00 23.97 ? 108  LEU   B C     1 
ATOM   9762  O  O     . LEU   B  1  110  ? 4.245   39.396  126.314 1.00 28.49 ? 108  LEU   B O     1 
ATOM   9763  C  CB    . LEU   B  1  110  ? 2.406   41.829  125.300 1.00 22.97 ? 108  LEU   B CB    1 
ATOM   9764  C  CG    . LEU   B  1  110  ? 2.534   43.333  125.056 1.00 22.82 ? 108  LEU   B CG    1 
ATOM   9765  C  CD1   . LEU   B  1  110  ? 1.203   44.007  125.338 1.00 23.12 ? 108  LEU   B CD1   1 
ATOM   9766  C  CD2   . LEU   B  1  110  ? 3.634   43.936  125.925 1.00 26.24 ? 108  LEU   B CD2   1 
ATOM   9767  N  N     . LEU   B  1  111  ? 2.931   38.656  124.641 1.00 25.46 ? 109  LEU   B N     1 
ATOM   9768  C  CA    . LEU   B  1  111  ? 2.944   37.282  125.123 1.00 30.25 ? 109  LEU   B CA    1 
ATOM   9769  C  C     . LEU   B  1  111  ? 4.256   36.567  124.841 1.00 33.16 ? 109  LEU   B C     1 
ATOM   9770  O  O     . LEU   B  1  111  ? 4.495   35.501  125.420 1.00 35.83 ? 109  LEU   B O     1 
ATOM   9771  C  CB    . LEU   B  1  111  ? 1.774   36.497  124.543 1.00 30.58 ? 109  LEU   B CB    1 
ATOM   9772  C  CG    . LEU   B  1  111  ? 0.429   36.959  125.092 1.00 28.75 ? 109  LEU   B CG    1 
ATOM   9773  C  CD1   . LEU   B  1  111  ? -0.675  36.320  124.293 1.00 31.04 ? 109  LEU   B CD1   1 
ATOM   9774  C  CD2   . LEU   B  1  111  ? 0.302   36.613  126.564 1.00 31.50 ? 109  LEU   B CD2   1 
ATOM   9775  N  N     . ARG   B  1  112  ? 5.108   37.124  123.982 1.00 29.14 ? 110  ARG   B N     1 
ATOM   9776  C  CA    . ARG   B  1  112  ? 6.464   36.611  123.847 1.00 32.35 ? 110  ARG   B CA    1 
ATOM   9777  C  C     . ARG   B  1  112  ? 7.324   36.942  125.058 1.00 32.73 ? 110  ARG   B C     1 
ATOM   9778  O  O     . ARG   B  1  112  ? 8.394   36.348  125.215 1.00 36.91 ? 110  ARG   B O     1 
ATOM   9779  C  CB    . ARG   B  1  112  ? 7.108   37.115  122.553 1.00 33.16 ? 110  ARG   B CB    1 
ATOM   9780  C  CG    . ARG   B  1  112  ? 6.391   36.639  121.292 1.00 33.44 ? 110  ARG   B CG    1 
ATOM   9781  C  CD    . ARG   B  1  112  ? 7.195   36.895  120.023 1.00 42.29 ? 110  ARG   B CD    1 
ATOM   9782  N  NE    . ARG   B  1  112  ? 7.084   38.270  119.548 1.00 39.90 ? 110  ARG   B NE    1 
ATOM   9783  C  CZ    . ARG   B  1  112  ? 6.228   38.678  118.620 1.00 40.68 ? 110  ARG   B CZ    1 
ATOM   9784  N  NH1   . ARG   B  1  112  ? 5.373   37.843  118.051 1.00 45.05 ? 110  ARG   B NH1   1 
ATOM   9785  N  NH2   . ARG   B  1  112  ? 6.233   39.955  118.248 1.00 43.84 ? 110  ARG   B NH2   1 
ATOM   9786  N  N     . ILE   B  1  113  ? 6.890   37.865  125.910 1.00 29.89 ? 111  ILE   B N     1 
ATOM   9787  C  CA    . ILE   B  1  113  ? 7.559   38.107  127.183 1.00 32.12 ? 111  ILE   B CA    1 
ATOM   9788  C  C     . ILE   B  1  113  ? 7.065   37.033  128.142 1.00 34.74 ? 111  ILE   B C     1 
ATOM   9789  O  O     . ILE   B  1  113  ? 5.892   37.055  128.541 1.00 36.62 ? 111  ILE   B O     1 
ATOM   9790  C  CB    . ILE   B  1  113  ? 7.264   39.515  127.722 1.00 31.08 ? 111  ILE   B CB    1 
ATOM   9791  C  CG1   . ILE   B  1  113  ? 7.741   40.577  126.730 1.00 32.18 ? 111  ILE   B CG1   1 
ATOM   9792  C  CG2   . ILE   B  1  113  ? 7.901   39.703  129.104 1.00 32.97 ? 111  ILE   B CG2   1 
ATOM   9793  C  CD1   . ILE   B  1  113  ? 7.289   41.974  127.081 1.00 31.65 ? 111  ILE   B CD1   1 
ATOM   9794  N  N     . PRO   B  1  114  ? 7.909   36.074  128.531 1.00 41.02 ? 112  PRO   B N     1 
ATOM   9795  C  CA    . PRO   B  1  114  ? 7.406   34.954  129.341 1.00 38.68 ? 112  PRO   B CA    1 
ATOM   9796  C  C     . PRO   B  1  114  ? 7.066   35.334  130.771 1.00 37.54 ? 112  PRO   B C     1 
ATOM   9797  O  O     . PRO   B  1  114  ? 6.146   34.745  131.352 1.00 41.13 ? 112  PRO   B O     1 
ATOM   9798  C  CB    . PRO   B  1  114  ? 8.548   33.930  129.274 1.00 35.84 ? 112  PRO   B CB    1 
ATOM   9799  C  CG    . PRO   B  1  114  ? 9.763   34.748  129.014 1.00 40.56 ? 112  PRO   B CG    1 
ATOM   9800  C  CD    . PRO   B  1  114  ? 9.330   35.917  128.178 1.00 37.89 ? 112  PRO   B CD    1 
ATOM   9801  N  N     . ASP   B  1  115  ? 7.766   36.302  131.354 1.00 37.49 ? 113  ASP   B N     1 
ATOM   9802  C  CA    . ASP   B  1  115  ? 7.545   36.670  132.748 1.00 43.74 ? 113  ASP   B CA    1 
ATOM   9803  C  C     . ASP   B  1  115  ? 6.345   37.605  132.851 1.00 43.81 ? 113  ASP   B C     1 
ATOM   9804  O  O     . ASP   B  1  115  ? 6.361   38.708  132.294 1.00 38.79 ? 113  ASP   B O     1 
ATOM   9805  C  CB    . ASP   B  1  115  ? 8.797   37.337  133.315 1.00 40.63 ? 113  ASP   B CB    1 
ATOM   9806  C  CG    . ASP   B  1  115  ? 8.626   37.763  134.759 1.00 45.45 ? 113  ASP   B CG    1 
ATOM   9807  O  OD1   . ASP   B  1  115  ? 8.241   36.917  135.594 1.00 50.86 ? 113  ASP   B OD1   1 
ATOM   9808  O  OD2   . ASP   B  1  115  ? 8.885   38.946  135.063 1.00 43.66 ? 113  ASP   B OD2   1 
ATOM   9809  N  N     . THR   B  1  116  ? 5.311   37.163  133.574 1.00 40.69 ? 114  THR   B N     1 
ATOM   9810  C  CA    . THR   B  1  116  ? 4.102   37.967  133.730 1.00 44.23 ? 114  THR   B CA    1 
ATOM   9811  C  C     . THR   B  1  116  ? 4.409   39.339  134.322 1.00 40.77 ? 114  THR   B C     1 
ATOM   9812  O  O     . THR   B  1  116  ? 3.868   40.355  133.868 1.00 38.42 ? 114  THR   B O     1 
ATOM   9813  C  CB    . THR   B  1  116  ? 3.084   37.216  134.593 1.00 47.96 ? 114  THR   B CB    1 
ATOM   9814  O  OG1   . THR   B  1  116  ? 2.704   36.001  133.935 1.00 53.61 ? 114  THR   B OG1   1 
ATOM   9815  C  CG2   . THR   B  1  116  ? 1.836   38.064  134.834 1.00 47.36 ? 114  THR   B CG2   1 
ATOM   9816  N  N     . ALA   B  1  117  ? 5.277   39.397  135.334 1.00 40.00 ? 115  ALA   B N     1 
ATOM   9817  C  CA    . ALA   B  1  117  ? 5.532   40.677  135.984 1.00 39.33 ? 115  ALA   B CA    1 
ATOM   9818  C  C     . ALA   B  1  117  ? 6.266   41.634  135.056 1.00 35.24 ? 115  ALA   B C     1 
ATOM   9819  O  O     . ALA   B  1  117  ? 5.969   42.835  135.035 1.00 40.26 ? 115  ALA   B O     1 
ATOM   9820  C  CB    . ALA   B  1  117  ? 6.314   40.471  137.282 1.00 35.64 ? 115  ALA   B CB    1 
ATOM   9821  N  N     . THR   B  1  118  ? 7.234   41.127  134.291 1.00 34.93 ? 116  THR   B N     1 
ATOM   9822  C  CA    . THR   B  1  118  ? 7.928   41.976  133.331 1.00 34.24 ? 116  THR   B CA    1 
ATOM   9823  C  C     . THR   B  1  118  ? 6.965   42.473  132.264 1.00 33.36 ? 116  THR   B C     1 
ATOM   9824  O  O     . THR   B  1  118  ? 7.006   43.645  131.874 1.00 37.01 ? 116  THR   B O     1 
ATOM   9825  C  CB    . THR   B  1  118  ? 9.081   41.202  132.691 1.00 35.97 ? 116  THR   B CB    1 
ATOM   9826  O  OG1   . THR   B  1  118  ? 10.019  40.818  133.707 1.00 38.69 ? 116  THR   B OG1   1 
ATOM   9827  C  CG2   . THR   B  1  118  ? 9.796   42.054  131.660 1.00 37.57 ? 116  THR   B CG2   1 
ATOM   9828  N  N     . ARG   B  1  119  ? 6.079   41.593  131.800 1.00 36.19 ? 117  ARG   B N     1 
ATOM   9829  C  CA    . ARG   B  1  119  ? 5.114   41.963  130.770 1.00 32.11 ? 117  ARG   B CA    1 
ATOM   9830  C  C     . ARG   B  1  119  ? 4.118   42.986  131.299 1.00 35.61 ? 117  ARG   B C     1 
ATOM   9831  O  O     . ARG   B  1  119  ? 3.852   44.003  130.647 1.00 32.78 ? 117  ARG   B O     1 
ATOM   9832  C  CB    . ARG   B  1  119  ? 4.382   40.710  130.305 1.00 33.25 ? 117  ARG   B CB    1 
ATOM   9833  C  CG    . ARG   B  1  119  ? 3.466   40.954  129.125 1.00 29.20 ? 117  ARG   B CG    1 
ATOM   9834  C  CD    . ARG   B  1  119  ? 2.492   39.818  128.964 1.00 29.02 ? 117  ARG   B CD    1 
ATOM   9835  N  NE    . ARG   B  1  119  ? 3.172   38.540  128.790 1.00 32.46 ? 117  ARG   B NE    1 
ATOM   9836  C  CZ    . ARG   B  1  119  ? 2.850   37.427  129.435 1.00 40.41 ? 117  ARG   B CZ    1 
ATOM   9837  N  NH1   . ARG   B  1  119  ? 1.834   37.388  130.284 1.00 35.74 ? 117  ARG   B NH1   1 
ATOM   9838  N  NH2   . ARG   B  1  119  ? 3.555   36.321  129.213 1.00 43.16 ? 117  ARG   B NH2   1 
ATOM   9839  N  N     . ASP   B  1  120  ? 3.567   42.738  132.489 1.00 31.86 ? 118  ASP   B N     1 
ATOM   9840  C  CA    . ASP   B  1  120  ? 2.615   43.675  133.076 1.00 33.61 ? 118  ASP   B CA    1 
ATOM   9841  C  C     . ASP   B  1  120  ? 3.268   45.016  133.381 1.00 39.76 ? 118  ASP   B C     1 
ATOM   9842  O  O     . ASP   B  1  120  ? 2.633   46.068  133.235 1.00 35.81 ? 118  ASP   B O     1 
ATOM   9843  C  CB    . ASP   B  1  120  ? 1.974   43.071  134.323 1.00 36.93 ? 118  ASP   B CB    1 
ATOM   9844  C  CG    . ASP   B  1  120  ? 1.074   41.892  133.998 1.00 43.55 ? 118  ASP   B CG    1 
ATOM   9845  O  OD1   . ASP   B  1  120  ? 0.857   41.628  132.793 1.00 43.75 ? 118  ASP   B OD1   1 
ATOM   9846  O  OD2   . ASP   B  1  120  ? 0.586   41.229  134.937 1.00 49.69 ? 118  ASP   B OD2   1 
ATOM   9847  N  N     . ALA   B  1  121  ? 4.538   45.007  133.795 1.00 33.68 ? 119  ALA   B N     1 
ATOM   9848  C  CA    . ALA   B  1  121  ? 5.212   46.274  134.054 1.00 40.82 ? 119  ALA   B CA    1 
ATOM   9849  C  C     . ALA   B  1  121  ? 5.417   47.058  132.766 1.00 37.76 ? 119  ALA   B C     1 
ATOM   9850  O  O     . ALA   B  1  121  ? 5.227   48.279  132.740 1.00 39.51 ? 119  ALA   B O     1 
ATOM   9851  C  CB    . ALA   B  1  121  ? 6.538   46.045  134.780 1.00 39.20 ? 119  ALA   B CB    1 
ATOM   9852  N  N     . LEU   B  1  122  ? 5.786   46.371  131.681 1.00 34.27 ? 120  LEU   B N     1 
ATOM   9853  C  CA    . LEU   B  1  122  ? 5.973   47.051  130.405 1.00 33.74 ? 120  LEU   B CA    1 
ATOM   9854  C  C     . LEU   B  1  122  ? 4.669   47.671  129.923 1.00 35.61 ? 120  LEU   B C     1 
ATOM   9855  O  O     . LEU   B  1  122  ? 4.662   48.786  129.389 1.00 34.45 ? 120  LEU   B O     1 
ATOM   9856  C  CB    . LEU   B  1  122  ? 6.510   46.067  129.368 1.00 33.77 ? 120  LEU   B CB    1 
ATOM   9857  C  CG    . LEU   B  1  122  ? 6.901   46.697  128.032 1.00 38.42 ? 120  LEU   B CG    1 
ATOM   9858  C  CD1   . LEU   B  1  122  ? 8.123   47.592  128.219 1.00 40.07 ? 120  LEU   B CD1   1 
ATOM   9859  C  CD2   . LEU   B  1  122  ? 7.148   45.639  126.969 1.00 37.12 ? 120  LEU   B CD2   1 
ATOM   9860  N  N     . ILE   B  1  123  ? 3.556   46.961  130.113 1.00 31.52 ? 121  ILE   B N     1 
ATOM   9861  C  CA    . ILE   B  1  123  ? 2.250   47.474  129.704 1.00 35.28 ? 121  ILE   B CA    1 
ATOM   9862  C  C     . ILE   B  1  123  ? 1.910   48.742  130.476 1.00 36.52 ? 121  ILE   B C     1 
ATOM   9863  O  O     . ILE   B  1  123  ? 1.559   49.773  129.889 1.00 36.43 ? 121  ILE   B O     1 
ATOM   9864  C  CB    . ILE   B  1  123  ? 1.172   46.392  129.889 1.00 31.14 ? 121  ILE   B CB    1 
ATOM   9865  C  CG1   . ILE   B  1  123  ? 1.377   45.255  128.891 1.00 27.14 ? 121  ILE   B CG1   1 
ATOM   9866  C  CG2   . ILE   B  1  123  ? -0.229  46.990  129.749 1.00 33.65 ? 121  ILE   B CG2   1 
ATOM   9867  C  CD1   . ILE   B  1  123  ? 0.566   44.042  129.229 1.00 25.50 ? 121  ILE   B CD1   1 
ATOM   9868  N  N     . ARG   B  1  124  ? 2.008   48.682  131.807 1.00 34.47 ? 122  ARG   B N     1 
ATOM   9869  C  CA    . ARG   B  1  124  ? 1.608   49.815  132.638 1.00 40.13 ? 122  ARG   B CA    1 
ATOM   9870  C  C     . ARG   B  1  124  ? 2.570   50.989  132.493 1.00 44.64 ? 122  ARG   B C     1 
ATOM   9871  O  O     . ARG   B  1  124  ? 2.140   52.149  132.480 1.00 49.51 ? 122  ARG   B O     1 
ATOM   9872  C  CB    . ARG   B  1  124  ? 1.498   49.382  134.100 1.00 44.66 ? 122  ARG   B CB    1 
ATOM   9873  N  N     . ASP   B  1  125  ? 3.872   50.716  132.375 1.00 40.97 ? 123  ASP   B N     1 
ATOM   9874  C  CA    . ASP   B  1  125  ? 4.879   51.771  132.400 1.00 48.91 ? 123  ASP   B CA    1 
ATOM   9875  C  C     . ASP   B  1  125  ? 5.306   52.262  131.023 1.00 50.16 ? 123  ASP   B C     1 
ATOM   9876  O  O     . ASP   B  1  125  ? 5.797   53.391  130.918 1.00 55.18 ? 123  ASP   B O     1 
ATOM   9877  C  CB    . ASP   B  1  125  ? 6.132   51.317  133.162 1.00 48.40 ? 123  ASP   B CB    1 
ATOM   9878  C  CG    . ASP   B  1  125  ? 5.835   50.910  134.592 1.00 54.22 ? 123  ASP   B CG    1 
ATOM   9879  O  OD1   . ASP   B  1  125  ? 4.792   51.332  135.134 1.00 52.89 ? 123  ASP   B OD1   1 
ATOM   9880  O  OD2   . ASP   B  1  125  ? 6.655   50.169  135.176 1.00 57.29 ? 123  ASP   B OD2   1 
ATOM   9881  N  N     . LYS   B  1  126  ? 5.144   51.465  129.976 1.00 39.48 ? 124  LYS   B N     1 
ATOM   9882  C  CA    . LYS   B  1  126  ? 5.657   51.902  128.683 1.00 45.36 ? 124  LYS   B CA    1 
ATOM   9883  C  C     . LYS   B  1  126  ? 4.628   51.848  127.563 1.00 42.53 ? 124  LYS   B C     1 
ATOM   9884  O  O     . LYS   B  1  126  ? 4.614   52.740  126.712 1.00 47.45 ? 124  LYS   B O     1 
ATOM   9885  C  CB    . LYS   B  1  126  ? 6.896   51.079  128.298 1.00 46.76 ? 124  LYS   B CB    1 
ATOM   9886  N  N     . ILE   B  1  127  ? 3.773   50.826  127.533 1.00 39.29 ? 125  ILE   B N     1 
ATOM   9887  C  CA    . ILE   B  1  127  ? 2.879   50.660  126.389 1.00 36.56 ? 125  ILE   B CA    1 
ATOM   9888  C  C     . ILE   B  1  127  ? 1.621   51.505  126.543 1.00 40.24 ? 125  ILE   B C     1 
ATOM   9889  O  O     . ILE   B  1  127  ? 1.165   52.134  125.581 1.00 35.89 ? 125  ILE   B O     1 
ATOM   9890  C  CB    . ILE   B  1  127  ? 2.544   49.179  126.145 1.00 32.40 ? 125  ILE   B CB    1 
ATOM   9891  C  CG1   . ILE   B  1  127  ? 3.815   48.324  126.123 1.00 37.60 ? 125  ILE   B CG1   1 
ATOM   9892  C  CG2   . ILE   B  1  127  ? 1.766   49.033  124.835 1.00 29.33 ? 125  ILE   B CG2   1 
ATOM   9893  C  CD1   . ILE   B  1  127  ? 4.801   48.720  125.060 1.00 43.85 ? 125  ILE   B CD1   1 
ATOM   9894  N  N     . ALA   B  1  128  ? 1.030   51.518  127.741 1.00 32.37 ? 126  ALA   B N     1 
ATOM   9895  C  CA    . ALA   B  1  128  ? -0.198  52.276  127.960 1.00 33.24 ? 126  ALA   B CA    1 
ATOM   9896  C  C     . ALA   B  1  128  ? 0.011   53.770  127.773 1.00 44.46 ? 126  ALA   B C     1 
ATOM   9897  O  O     . ALA   B  1  128  ? -0.957  54.499  127.529 1.00 41.11 ? 126  ALA   B O     1 
ATOM   9898  C  CB    . ALA   B  1  128  ? -0.761  51.986  129.350 1.00 36.90 ? 126  ALA   B CB    1 
ATOM   9899  N  N     . ASP   B  1  129  ? 1.253   54.237  127.874 1.00 44.09 ? 127  ASP   B N     1 
ATOM   9900  C  CA    . ASP   B  1  129  ? 1.599   55.624  127.615 1.00 52.93 ? 127  ASP   B CA    1 
ATOM   9901  C  C     . ASP   B  1  129  ? 1.988   55.869  126.161 1.00 54.37 ? 127  ASP   B C     1 
ATOM   9902  O  O     . ASP   B  1  129  ? 2.726   56.818  125.876 1.00 62.28 ? 127  ASP   B O     1 
ATOM   9903  C  CB    . ASP   B  1  129  ? 2.704   56.076  128.571 1.00 57.89 ? 127  ASP   B CB    1 
ATOM   9904  C  CG    . ASP   B  1  129  ? 2.338   55.843  130.026 1.00 65.33 ? 127  ASP   B CG    1 
ATOM   9905  O  OD1   . ASP   B  1  129  ? 1.145   55.993  130.371 1.00 66.20 ? 127  ASP   B OD1   1 
ATOM   9906  O  OD2   . ASP   B  1  129  ? 3.240   55.503  130.822 1.00 68.27 ? 127  ASP   B OD2   1 
ATOM   9907  N  N     . GLY   B  1  130  ? 1.525   55.022  125.243 1.00 50.68 ? 128  GLY   B N     1 
ATOM   9908  C  CA    . GLY   B  1  130  ? 1.659   55.277  123.822 1.00 53.22 ? 128  GLY   B CA    1 
ATOM   9909  C  C     . GLY   B  1  130  ? 3.014   54.994  123.207 1.00 55.66 ? 128  GLY   B C     1 
ATOM   9910  O  O     . GLY   B  1  130  ? 3.101   54.707  122.010 1.00 57.24 ? 128  GLY   B O     1 
ATOM   9911  N  N     . ASN   B  1  131  ? 4.083   55.062  123.998 1.00 61.74 ? 129  ASN   B N     1 
ATOM   9912  C  CA    . ASN   B  1  131  ? 5.427   54.902  123.452 1.00 60.91 ? 129  ASN   B CA    1 
ATOM   9913  C  C     . ASN   B  1  131  ? 5.705   53.459  123.038 1.00 58.53 ? 129  ASN   B C     1 
ATOM   9914  O  O     . ASN   B  1  131  ? 6.801   52.941  123.276 1.00 61.66 ? 129  ASN   B O     1 
ATOM   9915  C  CB    . ASN   B  1  131  ? 6.471   55.380  124.465 1.00 60.04 ? 129  ASN   B CB    1 
ATOM   9916  N  N     . TRP   B  1  132  ? 4.725   52.809  122.401 1.00 46.89 ? 130  TRP   B N     1 
ATOM   9917  C  CA    . TRP   B  1  132  ? 4.857   51.395  122.063 1.00 42.91 ? 130  TRP   B CA    1 
ATOM   9918  C  C     . TRP   B  1  132  ? 5.877   51.164  120.955 1.00 41.16 ? 130  TRP   B C     1 
ATOM   9919  O  O     . TRP   B  1  132  ? 6.485   50.090  120.891 1.00 44.37 ? 130  TRP   B O     1 
ATOM   9920  C  CB    . TRP   B  1  132  ? 3.493   50.816  121.667 1.00 40.71 ? 130  TRP   B CB    1 
ATOM   9921  C  CG    . TRP   B  1  132  ? 2.922   51.390  120.384 1.00 31.76 ? 130  TRP   B CG    1 
ATOM   9922  C  CD1   . TRP   B  1  132  ? 2.038   52.423  120.268 1.00 33.16 ? 130  TRP   B CD1   1 
ATOM   9923  C  CD2   . TRP   B  1  132  ? 3.208   50.957  119.046 1.00 29.35 ? 130  TRP   B CD2   1 
ATOM   9924  N  NE1   . TRP   B  1  132  ? 1.751   52.656  118.942 1.00 28.87 ? 130  TRP   B NE1   1 
ATOM   9925  C  CE2   . TRP   B  1  132  ? 2.457   51.770  118.174 1.00 25.36 ? 130  TRP   B CE2   1 
ATOM   9926  C  CE3   . TRP   B  1  132  ? 4.016   49.954  118.505 1.00 26.38 ? 130  TRP   B CE3   1 
ATOM   9927  C  CZ2   . TRP   B  1  132  ? 2.504   51.620  116.793 1.00 25.48 ? 130  TRP   B CZ2   1 
ATOM   9928  C  CZ3   . TRP   B  1  132  ? 4.064   49.810  117.135 1.00 25.47 ? 130  TRP   B CZ3   1 
ATOM   9929  C  CH2   . TRP   B  1  132  ? 3.307   50.634  116.293 1.00 25.27 ? 130  TRP   B CH2   1 
ATOM   9930  N  N     . LYS   B  1  133  ? 6.076   52.149  120.075 1.00 43.40 ? 131  LYS   B N     1 
ATOM   9931  C  CA    . LYS   B  1  133  ? 6.949   51.948  118.922 1.00 43.71 ? 131  LYS   B CA    1 
ATOM   9932  C  C     . LYS   B  1  133  ? 8.400   51.743  119.327 1.00 56.71 ? 131  LYS   B C     1 
ATOM   9933  O  O     . LYS   B  1  133  ? 9.180   51.185  118.547 1.00 58.00 ? 131  LYS   B O     1 
ATOM   9934  C  CB    . LYS   B  1  133  ? 6.836   53.133  117.960 1.00 45.97 ? 131  LYS   B CB    1 
ATOM   9935  N  N     . SER   B  1  134  ? 8.773   52.168  120.528 1.00 61.12 ? 132  SER   B N     1 
ATOM   9936  C  CA    . SER   B  1  134  ? 10.146  52.105  121.010 1.00 59.54 ? 132  SER   B CA    1 
ATOM   9937  C  C     . SER   B  1  134  ? 10.309  51.059  122.109 1.00 61.30 ? 132  SER   B C     1 
ATOM   9938  O  O     . SER   B  1  134  ? 11.016  51.282  123.092 1.00 67.85 ? 132  SER   B O     1 
ATOM   9939  C  CB    . SER   B  1  134  ? 10.603  53.478  121.495 1.00 56.02 ? 132  SER   B CB    1 
ATOM   9940  O  OG    . SER   B  1  134  ? 9.637   54.056  122.359 1.00 63.67 ? 132  SER   B OG    1 
ATOM   9941  N  N     . HIS   B  1  135  ? 9.661   49.903  121.956 1.00 61.94 ? 133  HIS   B N     1 
ATOM   9942  C  CA    . HIS   B  1  135  ? 9.701   48.894  123.010 1.00 64.28 ? 133  HIS   B CA    1 
ATOM   9943  C  C     . HIS   B  1  135  ? 9.594   47.469  122.483 1.00 65.13 ? 133  HIS   B C     1 
ATOM   9944  O  O     . HIS   B  1  135  ? 10.213  46.553  123.035 1.00 71.40 ? 133  HIS   B O     1 
ATOM   9945  C  CB    . HIS   B  1  135  ? 8.606   49.155  124.047 1.00 60.55 ? 133  HIS   B CB    1 
ATOM   9946  C  CG    . HIS   B  1  135  ? 8.897   50.310  124.952 1.00 64.63 ? 133  HIS   B CG    1 
ATOM   9947  N  ND1   . HIS   B  1  135  ? 8.246   51.521  124.848 1.00 69.94 ? 133  HIS   B ND1   1 
ATOM   9948  C  CD2   . HIS   B  1  135  ? 9.781   50.444  125.969 1.00 67.41 ? 133  HIS   B CD2   1 
ATOM   9949  C  CE1   . HIS   B  1  135  ? 8.712   52.349  125.767 1.00 71.90 ? 133  HIS   B CE1   1 
ATOM   9950  N  NE2   . HIS   B  1  135  ? 9.642   51.719  126.461 1.00 71.49 ? 133  HIS   B NE2   1 
ATOM   9951  N  N     . LEU   B  1  136  ? 8.807   47.263  121.434 1.00 56.70 ? 134  LEU   B N     1 
ATOM   9952  C  CA    . LEU   B  1  136  ? 8.582   45.917  120.923 1.00 56.87 ? 134  LEU   B CA    1 
ATOM   9953  C  C     . LEU   B  1  136  ? 8.894   45.825  119.433 1.00 52.15 ? 134  LEU   B C     1 
ATOM   9954  O  O     . LEU   B  1  136  ? 8.798   44.753  118.838 1.00 54.92 ? 134  LEU   B O     1 
ATOM   9955  C  CB    . LEU   B  1  136  ? 7.140   45.483  121.191 1.00 49.39 ? 134  LEU   B CB    1 
ATOM   9956  C  CG    . LEU   B  1  136  ? 6.690   45.479  122.651 1.00 43.02 ? 134  LEU   B CG    1 
ATOM   9957  C  CD1   . LEU   B  1  136  ? 5.188   45.304  122.731 1.00 39.56 ? 134  LEU   B CD1   1 
ATOM   9958  C  CD2   . LEU   B  1  136  ? 7.398   44.380  123.425 1.00 47.07 ? 134  LEU   B CD2   1 
ATOM   9959  N  N     . ARG   B  1  140  ? 12.063  43.875  114.539 1.00 37.97 ? 138  ARG   B N     1 
ATOM   9960  C  CA    . ARG   B  1  140  ? 11.005  43.138  113.857 1.00 46.09 ? 138  ARG   B CA    1 
ATOM   9961  C  C     . ARG   B  1  140  ? 9.647   43.799  114.085 1.00 42.64 ? 138  ARG   B C     1 
ATOM   9962  O  O     . ARG   B  1  140  ? 9.283   44.132  115.215 1.00 32.83 ? 138  ARG   B O     1 
ATOM   9963  C  CB    . ARG   B  1  140  ? 10.973  41.675  114.313 1.00 44.25 ? 138  ARG   B CB    1 
ATOM   9964  N  N     . SER   B  1  141  ? 8.905   43.980  112.996 1.00 32.86 ? 139  SER   B N     1 
ATOM   9965  C  CA    . SER   B  1  141  ? 7.628   44.672  113.062 1.00 27.85 ? 139  SER   B CA    1 
ATOM   9966  C  C     . SER   B  1  141  ? 6.690   43.961  114.028 1.00 27.17 ? 139  SER   B C     1 
ATOM   9967  O  O     . SER   B  1  141  ? 6.640   42.730  114.092 1.00 29.06 ? 139  SER   B O     1 
ATOM   9968  C  CB    . SER   B  1  141  ? 7.000   44.701  111.664 1.00 29.64 ? 139  SER   B CB    1 
ATOM   9969  O  OG    . SER   B  1  141  ? 5.710   45.310  111.671 1.00 30.46 ? 139  SER   B OG    1 
ATOM   9970  N  N     . LEU   B  1  142  ? 5.957   44.751  114.806 1.00 25.57 ? 140  LEU   B N     1 
ATOM   9971  C  CA    . LEU   B  1  142  ? 4.866   44.199  115.588 1.00 24.68 ? 140  LEU   B CA    1 
ATOM   9972  C  C     . LEU   B  1  142  ? 3.855   43.480  114.710 1.00 22.34 ? 140  LEU   B C     1 
ATOM   9973  O  O     . LEU   B  1  142  ? 3.133   42.601  115.193 1.00 21.60 ? 140  LEU   B O     1 
ATOM   9974  C  CB    . LEU   B  1  142  ? 4.142   45.356  116.269 1.00 23.47 ? 140  LEU   B CB    1 
ATOM   9975  C  CG    . LEU   B  1  142  ? 3.583   45.078  117.647 1.00 28.23 ? 140  LEU   B CG    1 
ATOM   9976  C  CD1   . LEU   B  1  142  ? 4.727   44.828  118.579 1.00 28.37 ? 140  LEU   B CD1   1 
ATOM   9977  C  CD2   . LEU   B  1  142  ? 2.797   46.258  118.111 1.00 30.23 ? 140  LEU   B CD2   1 
ATOM   9978  N  N     . PHE   B  1  143  ? 3.777   43.840  113.434 1.00 20.96 ? 141  PHE   B N     1 
ATOM   9979  C  CA    . PHE   B  1  143  ? 2.676   43.437  112.580 1.00 19.49 ? 141  PHE   B CA    1 
ATOM   9980  C  C     . PHE   B  1  143  ? 3.036   42.298  111.634 1.00 20.02 ? 141  PHE   B C     1 
ATOM   9981  O  O     . PHE   B  1  143  ? 2.295   42.043  110.681 1.00 20.54 ? 141  PHE   B O     1 
ATOM   9982  C  CB    . PHE   B  1  143  ? 2.129   44.670  111.860 1.00 21.32 ? 141  PHE   B CB    1 
ATOM   9983  C  CG    . PHE   B  1  143  ? 1.822   45.806  112.803 1.00 18.95 ? 141  PHE   B CG    1 
ATOM   9984  C  CD1   . PHE   B  1  143  ? 0.905   45.642  113.828 1.00 18.95 ? 141  PHE   B CD1   1 
ATOM   9985  C  CD2   . PHE   B  1  143  ? 2.454   47.033  112.681 1.00 18.20 ? 141  PHE   B CD2   1 
ATOM   9986  C  CE1   . PHE   B  1  143  ? 0.626   46.665  114.686 1.00 19.89 ? 141  PHE   B CE1   1 
ATOM   9987  C  CE2   . PHE   B  1  143  ? 2.185   48.064  113.547 1.00 20.26 ? 141  PHE   B CE2   1 
ATOM   9988  C  CZ    . PHE   B  1  143  ? 1.264   47.886  114.558 1.00 19.57 ? 141  PHE   B CZ    1 
ATOM   9989  N  N     . VAL   B  1  144  ? 4.138   41.584  111.902 1.00 21.47 ? 142  VAL   B N     1 
ATOM   9990  C  CA    . VAL   B  1  144  ? 4.575   40.481  111.042 1.00 22.83 ? 142  VAL   B CA    1 
ATOM   9991  C  C     . VAL   B  1  144  ? 3.457   39.477  110.789 1.00 24.09 ? 142  VAL   B C     1 
ATOM   9992  O  O     . VAL   B  1  144  ? 3.292   38.987  109.667 1.00 24.61 ? 142  VAL   B O     1 
ATOM   9993  C  CB    . VAL   B  1  144  ? 5.846   39.813  111.605 1.00 24.96 ? 142  VAL   B CB    1 
ATOM   9994  C  CG1   . VAL   B  1  144  ? 6.202   38.564  110.806 1.00 28.88 ? 142  VAL   B CG1   1 
ATOM   9995  C  CG2   . VAL   B  1  144  ? 6.996   40.791  111.585 1.00 26.45 ? 142  VAL   B CG2   1 
ATOM   9996  N  N     . ASN   B  1  145  ? 2.675   39.145  111.818 1.00 21.96 ? 143  ASN   B N     1 
ATOM   9997  C  CA    . ASN   B  1  145  ? 1.605   38.167  111.672 1.00 23.72 ? 143  ASN   B CA    1 
ATOM   9998  C  C     . ASN   B  1  145  ? 0.232   38.805  111.536 1.00 22.52 ? 143  ASN   B C     1 
ATOM   9999  O  O     . ASN   B  1  145  ? -0.781  38.149  111.806 1.00 22.65 ? 143  ASN   B O     1 
ATOM   10000 C  CB    . ASN   B  1  145  ? 1.628   37.162  112.821 1.00 25.24 ? 143  ASN   B CB    1 
ATOM   10001 C  CG    . ASN   B  1  145  ? 2.807   36.226  112.731 1.00 32.04 ? 143  ASN   B CG    1 
ATOM   10002 O  OD1   . ASN   B  1  145  ? 3.087   35.664  111.669 1.00 34.65 ? 143  ASN   B OD1   1 
ATOM   10003 N  ND2   . ASN   B  1  145  ? 3.513   36.059  113.837 1.00 30.97 ? 143  ASN   B ND2   1 
ATOM   10004 N  N     . ALA   B  1  146  ? 0.173   40.064  111.099 1.00 19.49 ? 144  ALA   B N     1 
ATOM   10005 C  CA    . ALA   B  1  146  ? -1.111  40.751  111.030 1.00 23.60 ? 144  ALA   B CA    1 
ATOM   10006 C  C     . ALA   B  1  146  ? -2.054  40.136  110.001 1.00 21.28 ? 144  ALA   B C     1 
ATOM   10007 O  O     . ALA   B  1  146  ? -3.276  40.267  110.138 1.00 22.33 ? 144  ALA   B O     1 
ATOM   10008 C  CB    . ALA   B  1  146  ? -0.907  42.242  110.762 1.00 21.79 ? 144  ALA   B CB    1 
ATOM   10009 N  N     . ALA   B  1  147  ? -1.537  39.476  108.965 1.00 22.06 ? 145  ALA   B N     1 
ATOM   10010 C  CA    . ALA   B  1  147  ? -2.456  38.831  108.031 1.00 22.51 ? 145  ALA   B CA    1 
ATOM   10011 C  C     . ALA   B  1  147  ? -3.237  37.731  108.731 1.00 23.07 ? 145  ALA   B C     1 
ATOM   10012 O  O     . ALA   B  1  147  ? -4.437  37.548  108.490 1.00 24.27 ? 145  ALA   B O     1 
ATOM   10013 C  CB    . ALA   B  1  147  ? -1.707  38.278  106.823 1.00 23.67 ? 145  ALA   B CB    1 
ATOM   10014 N  N     . THR   B  1  148  ? -2.576  37.015  109.633 1.00 23.00 ? 146  THR   B N     1 
ATOM   10015 C  CA    . THR   B  1  148  ? -3.264  35.988  110.401 1.00 22.51 ? 146  THR   B CA    1 
ATOM   10016 C  C     . THR   B  1  148  ? -4.277  36.607  111.355 1.00 24.16 ? 146  THR   B C     1 
ATOM   10017 O  O     . THR   B  1  148  ? -5.428  36.160  111.423 1.00 24.49 ? 146  THR   B O     1 
ATOM   10018 C  CB    . THR   B  1  148  ? -2.233  35.131  111.135 1.00 30.50 ? 146  THR   B CB    1 
ATOM   10019 O  OG1   . THR   B  1  148  ? -1.394  34.489  110.166 1.00 33.87 ? 146  THR   B OG1   1 
ATOM   10020 C  CG2   . THR   B  1  148  ? -2.921  34.079  111.989 1.00 36.58 ? 146  THR   B CG2   1 
ATOM   10021 N  N     . TRP   B  1  149  ? -3.887  37.661  112.076 1.00 22.32 ? 147  TRP   B N     1 
ATOM   10022 C  CA    . TRP   B  1  149  ? -4.851  38.308  112.954 1.00 22.38 ? 147  TRP   B CA    1 
ATOM   10023 C  C     . TRP   B  1  149  ? -5.963  38.981  112.163 1.00 20.91 ? 147  TRP   B C     1 
ATOM   10024 O  O     . TRP   B  1  149  ? -7.101  39.053  112.644 1.00 22.14 ? 147  TRP   B O     1 
ATOM   10025 C  CB    . TRP   B  1  149  ? -4.167  39.289  113.904 1.00 22.42 ? 147  TRP   B CB    1 
ATOM   10026 C  CG    . TRP   B  1  149  ? -3.273  38.611  114.892 1.00 22.01 ? 147  TRP   B CG    1 
ATOM   10027 C  CD1   . TRP   B  1  149  ? -1.917  38.697  114.955 1.00 24.48 ? 147  TRP   B CD1   1 
ATOM   10028 C  CD2   . TRP   B  1  149  ? -3.674  37.716  115.937 1.00 24.74 ? 147  TRP   B CD2   1 
ATOM   10029 N  NE1   . TRP   B  1  149  ? -1.447  37.921  115.986 1.00 23.59 ? 147  TRP   B NE1   1 
ATOM   10030 C  CE2   . TRP   B  1  149  ? -2.505  37.312  116.608 1.00 26.21 ? 147  TRP   B CE2   1 
ATOM   10031 C  CE3   . TRP   B  1  149  ? -4.909  37.227  116.377 1.00 28.07 ? 147  TRP   B CE3   1 
ATOM   10032 C  CZ2   . TRP   B  1  149  ? -2.530  36.438  117.700 1.00 29.75 ? 147  TRP   B CZ2   1 
ATOM   10033 C  CZ3   . TRP   B  1  149  ? -4.935  36.363  117.468 1.00 30.92 ? 147  TRP   B CZ3   1 
ATOM   10034 C  CH2   . TRP   B  1  149  ? -3.751  35.978  118.112 1.00 31.97 ? 147  TRP   B CH2   1 
ATOM   10035 N  N     . GLY   B  1  150  ? -5.658  39.471  110.959 1.00 21.24 ? 148  GLY   B N     1 
ATOM   10036 C  CA    . GLY   B  1  150  ? -6.711  39.991  110.103 1.00 23.85 ? 148  GLY   B CA    1 
ATOM   10037 C  C     . GLY   B  1  150  ? -7.764  38.944  109.810 1.00 22.72 ? 148  GLY   B C     1 
ATOM   10038 O  O     . GLY   B  1  150  ? -8.964  39.228  109.831 1.00 23.65 ? 148  GLY   B O     1 
ATOM   10039 N  N     . LEU   B  1  151  ? -7.332  37.708  109.558 1.00 23.10 ? 149  LEU   B N     1 
ATOM   10040 C  CA    A LEU   B  1  151  ? -8.290  36.623  109.369 0.52 28.19 ? 149  LEU   B CA    1 
ATOM   10041 C  CA    B LEU   B  1  151  ? -8.291  36.626  109.366 0.48 28.18 ? 149  LEU   B CA    1 
ATOM   10042 C  C     . LEU   B  1  151  ? -9.124  36.406  110.623 1.00 28.00 ? 149  LEU   B C     1 
ATOM   10043 O  O     . LEU   B  1  151  ? -10.344 36.223  110.546 1.00 30.04 ? 149  LEU   B O     1 
ATOM   10044 C  CB    A LEU   B  1  151  ? -7.556  35.339  108.990 0.52 27.91 ? 149  LEU   B CB    1 
ATOM   10045 C  CB    B LEU   B  1  151  ? -7.556  35.348  108.967 0.48 27.91 ? 149  LEU   B CB    1 
ATOM   10046 C  CG    A LEU   B  1  151  ? -7.583  34.953  107.515 0.52 27.85 ? 149  LEU   B CG    1 
ATOM   10047 C  CG    B LEU   B  1  151  ? -8.428  34.181  108.511 0.48 28.38 ? 149  LEU   B CG    1 
ATOM   10048 C  CD1   A LEU   B  1  151  ? -6.782  33.680  107.307 0.52 31.11 ? 149  LEU   B CD1   1 
ATOM   10049 C  CD1   B LEU   B  1  151  ? -9.321  34.621  107.360 0.48 29.56 ? 149  LEU   B CD1   1 
ATOM   10050 C  CD2   A LEU   B  1  151  ? -9.024  34.780  107.035 0.52 30.03 ? 149  LEU   B CD2   1 
ATOM   10051 C  CD2   B LEU   B  1  151  ? -7.550  33.012  108.098 0.48 32.70 ? 149  LEU   B CD2   1 
ATOM   10052 N  N     . VAL   B  1  152  ? -8.482  36.433  111.793 1.00 25.26 ? 150  VAL   B N     1 
ATOM   10053 C  CA    . VAL   B  1  152  ? -9.208  36.237  113.044 1.00 26.42 ? 150  VAL   B CA    1 
ATOM   10054 C  C     . VAL   B  1  152  ? -10.230 37.342  113.255 1.00 28.00 ? 150  VAL   B C     1 
ATOM   10055 O  O     . VAL   B  1  152  ? -11.378 37.086  113.635 1.00 30.85 ? 150  VAL   B O     1 
ATOM   10056 C  CB    . VAL   B  1  152  ? -8.224  36.158  114.224 1.00 24.36 ? 150  VAL   B CB    1 
ATOM   10057 C  CG1   . VAL   B  1  152  ? -8.980  36.180  115.547 1.00 32.57 ? 150  VAL   B CG1   1 
ATOM   10058 C  CG2   . VAL   B  1  152  ? -7.362  34.921  114.109 1.00 28.03 ? 150  VAL   B CG2   1 
ATOM   10059 N  N     . VAL   B  1  153  ? -9.831  38.587  113.011 1.00 24.64 ? 151  VAL   B N     1 
ATOM   10060 C  CA    . VAL   B  1  153  ? -10.672 39.726  113.348 1.00 25.77 ? 151  VAL   B CA    1 
ATOM   10061 C  C     . VAL   B  1  153  ? -11.752 39.953  112.301 1.00 25.70 ? 151  VAL   B C     1 
ATOM   10062 O  O     . VAL   B  1  153  ? -12.906 40.229  112.642 1.00 27.97 ? 151  VAL   B O     1 
ATOM   10063 C  CB    . VAL   B  1  153  ? -9.792  40.971  113.535 1.00 26.49 ? 151  VAL   B CB    1 
ATOM   10064 C  CG1   . VAL   B  1  153  ? -10.655 42.220  113.716 1.00 26.79 ? 151  VAL   B CG1   1 
ATOM   10065 C  CG2   . VAL   B  1  153  ? -8.847  40.771  114.709 1.00 23.96 ? 151  VAL   B CG2   1 
ATOM   10066 N  N     . THR   B  1  154  ? -11.399 39.875  111.018 1.00 25.41 ? 152  THR   B N     1 
ATOM   10067 C  CA    . THR   B  1  154  ? -12.310 40.258  109.947 1.00 28.10 ? 152  THR   B CA    1 
ATOM   10068 C  C     . THR   B  1  154  ? -12.817 39.090  109.126 1.00 31.46 ? 152  THR   B C     1 
ATOM   10069 O  O     . THR   B  1  154  ? -13.768 39.269  108.361 1.00 32.86 ? 152  THR   B O     1 
ATOM   10070 C  CB    . THR   B  1  154  ? -11.625 41.229  108.968 1.00 28.29 ? 152  THR   B CB    1 
ATOM   10071 O  OG1   . THR   B  1  154  ? -10.708 40.511  108.135 1.00 28.19 ? 152  THR   B OG1   1 
ATOM   10072 C  CG2   . THR   B  1  154  ? -10.878 42.318  109.707 1.00 31.95 ? 152  THR   B CG2   1 
ATOM   10073 N  N     . GLY   B  1  155  ? -12.194 37.921  109.232 1.00 26.54 ? 153  GLY   B N     1 
ATOM   10074 C  CA    . GLY   B  1  155  ? -12.558 36.809  108.382 1.00 30.33 ? 153  GLY   B CA    1 
ATOM   10075 C  C     . GLY   B  1  155  ? -12.031 36.904  106.974 1.00 30.14 ? 153  GLY   B C     1 
ATOM   10076 O  O     . GLY   B  1  155  ? -12.384 36.064  106.137 1.00 34.05 ? 153  GLY   B O     1 
ATOM   10077 N  N     . LYS   B  1  156  ? -11.198 37.898  106.683 1.00 28.19 ? 154  LYS   B N     1 
ATOM   10078 C  CA    . LYS   B  1  156  ? -10.645 38.108  105.355 1.00 30.08 ? 154  LYS   B CA    1 
ATOM   10079 C  C     . LYS   B  1  156  ? -9.129  38.008  105.433 1.00 29.22 ? 154  LYS   B C     1 
ATOM   10080 O  O     . LYS   B  1  156  ? -8.523  38.430  106.421 1.00 29.58 ? 154  LYS   B O     1 
ATOM   10081 C  CB    . LYS   B  1  156  ? -11.046 39.489  104.826 1.00 37.30 ? 154  LYS   B CB    1 
ATOM   10082 N  N     . LEU   B  1  157  ? -8.519  37.443  104.400 1.00 27.35 ? 155  LEU   B N     1 
ATOM   10083 C  CA    . LEU   B  1  157  ? -7.075  37.290  104.336 1.00 28.86 ? 155  LEU   B CA    1 
ATOM   10084 C  C     . LEU   B  1  157  ? -6.512  38.298  103.348 1.00 34.60 ? 155  LEU   B C     1 
ATOM   10085 O  O     . LEU   B  1  157  ? -7.022  38.433  102.232 1.00 37.21 ? 155  LEU   B O     1 
ATOM   10086 C  CB    . LEU   B  1  157  ? -6.688  35.876  103.897 1.00 32.48 ? 155  LEU   B CB    1 
ATOM   10087 N  N     . THR   B  1  158  ? -5.473  39.010  103.763 1.00 35.95 ? 156  THR   B N     1 
ATOM   10088 C  CA    . THR   B  1  158  ? -4.647  39.775  102.846 1.00 38.38 ? 156  THR   B CA    1 
ATOM   10089 C  C     . THR   B  1  158  ? -3.281  39.110  102.773 1.00 36.88 ? 156  THR   B C     1 
ATOM   10090 O  O     . THR   B  1  158  ? -2.848  38.435  103.712 1.00 39.17 ? 156  THR   B O     1 
ATOM   10091 C  CB    . THR   B  1  158  ? -4.487  41.224  103.310 1.00 44.57 ? 156  THR   B CB    1 
ATOM   10092 O  OG1   . THR   B  1  158  ? -3.663  41.261  104.481 1.00 46.42 ? 156  THR   B OG1   1 
ATOM   10093 C  CG2   . THR   B  1  158  ? -5.843  41.837  103.632 1.00 39.71 ? 156  THR   B CG2   1 
ATOM   10094 N  N     . SER   B  1  159  ? -2.604  39.292  101.646 1.00 31.85 ? 157  SER   B N     1 
ATOM   10095 C  CA    . SER   B  1  159  ? -1.293  38.675  101.502 1.00 29.75 ? 157  SER   B CA    1 
ATOM   10096 C  C     . SER   B  1  159  ? -0.225  39.477  102.233 1.00 33.66 ? 157  SER   B C     1 
ATOM   10097 O  O     . SER   B  1  159  ? 0.723   38.907  102.785 1.00 31.74 ? 157  SER   B O     1 
ATOM   10098 C  CB    . SER   B  1  159  ? -0.947  38.540  100.020 1.00 36.35 ? 157  SER   B CB    1 
ATOM   10099 O  OG    . SER   B  1  159  ? -1.461  39.644  99.294  1.00 42.50 ? 157  SER   B OG    1 
ATOM   10100 N  N     . THR   B  1  160  ? -0.363  40.794  102.244 1.00 28.92 ? 158  THR   B N     1 
ATOM   10101 C  CA    . THR   B  1  160  ? 0.583   41.666  102.916 1.00 22.83 ? 158  THR   B CA    1 
ATOM   10102 C  C     . THR   B  1  160  ? -0.182  42.591  103.845 1.00 22.91 ? 158  THR   B C     1 
ATOM   10103 O  O     . THR   B  1  160  ? -1.415  42.662  103.823 1.00 27.56 ? 158  THR   B O     1 
ATOM   10104 C  CB    . THR   B  1  160  ? 1.403   42.484  101.911 1.00 26.27 ? 158  THR   B CB    1 
ATOM   10105 O  OG1   . THR   B  1  160  ? 0.515   43.288  101.133 1.00 29.94 ? 158  THR   B OG1   1 
ATOM   10106 C  CG2   . THR   B  1  160  ? 2.220   41.566  100.994 1.00 29.40 ? 158  THR   B CG2   1 
ATOM   10107 N  N     . VAL   B  1  161  ? 0.587   43.321  104.645 1.00 18.24 ? 159  VAL   B N     1 
ATOM   10108 C  CA    . VAL   B  1  161  ? 0.115   44.006  105.836 1.00 22.00 ? 159  VAL   B CA    1 
ATOM   10109 C  C     . VAL   B  1  161  ? 0.303   45.495  105.606 1.00 19.40 ? 159  VAL   B C     1 
ATOM   10110 O  O     . VAL   B  1  161  ? 1.397   45.928  105.231 1.00 18.62 ? 159  VAL   B O     1 
ATOM   10111 C  CB    . VAL   B  1  161  ? 0.944   43.529  107.048 1.00 24.31 ? 159  VAL   B CB    1 
ATOM   10112 C  CG1   . VAL   B  1  161  ? 0.861   44.487  108.192 1.00 27.27 ? 159  VAL   B CG1   1 
ATOM   10113 C  CG2   . VAL   B  1  161  ? 0.511   42.128  107.454 1.00 33.75 ? 159  VAL   B CG2   1 
ATOM   10114 N  N     . ASN   B  1  162  ? -0.748  46.281  105.831 1.00 17.93 ? 160  ASN   B N     1 
ATOM   10115 C  CA    . ASN   B  1  162  ? -0.562  47.725  105.780 1.00 17.79 ? 160  ASN   B CA    1 
ATOM   10116 C  C     . ASN   B  1  162  ? -0.064  48.156  107.147 1.00 17.82 ? 160  ASN   B C     1 
ATOM   10117 O  O     . ASN   B  1  162  ? -0.831  48.493  108.042 1.00 18.39 ? 160  ASN   B O     1 
ATOM   10118 C  CB    . ASN   B  1  162  ? -1.825  48.462  105.367 1.00 18.78 ? 160  ASN   B CB    1 
ATOM   10119 C  CG    . ASN   B  1  162  ? -1.585  49.954  105.226 1.00 17.49 ? 160  ASN   B CG    1 
ATOM   10120 O  OD1   . ASN   B  1  162  ? -0.632  50.486  105.782 1.00 18.35 ? 160  ASN   B OD1   1 
ATOM   10121 N  ND2   . ASN   B  1  162  ? -2.447  50.631  104.494 1.00 20.72 ? 160  ASN   B ND2   1 
ATOM   10122 N  N     . ASP   B  1  163  ? 1.255   48.150  107.300 1.00 16.88 ? 161  ASP   B N     1 
ATOM   10123 C  CA    . ASP   B  1  163  ? 1.853   48.428  108.587 1.00 17.76 ? 161  ASP   B CA    1 
ATOM   10124 C  C     . ASP   B  1  163  ? 1.700   49.877  109.003 1.00 17.66 ? 161  ASP   B C     1 
ATOM   10125 O  O     . ASP   B  1  163  ? 1.738   50.162  110.192 1.00 17.23 ? 161  ASP   B O     1 
ATOM   10126 C  CB    . ASP   B  1  163  ? 3.320   47.969  108.613 1.00 17.44 ? 161  ASP   B CB    1 
ATOM   10127 C  CG    . ASP   B  1  163  ? 4.140   48.495  107.449 1.00 20.40 ? 161  ASP   B CG    1 
ATOM   10128 O  OD1   . ASP   B  1  163  ? 3.695   48.437  106.290 1.00 19.43 ? 161  ASP   B OD1   1 
ATOM   10129 O  OD2   . ASP   B  1  163  ? 5.279   48.927  107.716 1.00 22.02 ? 161  ASP   B OD2   1 
ATOM   10130 N  N     . ARG   B  1  164  ? 1.549   50.808  108.061 1.00 16.31 ? 162  ARG   B N     1 
ATOM   10131 C  CA    . ARG   B  1  164  ? 1.302   52.180  108.472 1.00 16.42 ? 162  ARG   B CA    1 
ATOM   10132 C  C     . ARG   B  1  164  ? -0.102  52.339  109.022 1.00 15.76 ? 162  ARG   B C     1 
ATOM   10133 O  O     . ARG   B  1  164  ? -0.310  53.063  109.994 1.00 15.84 ? 162  ARG   B O     1 
ATOM   10134 C  CB    . ARG   B  1  164  ? 1.542   53.142  107.310 1.00 17.37 ? 162  ARG   B CB    1 
ATOM   10135 C  CG    . ARG   B  1  164  ? 2.987   53.142  106.814 1.00 17.57 ? 162  ARG   B CG    1 
ATOM   10136 C  CD    . ARG   B  1  164  ? 3.984   53.275  107.951 1.00 23.34 ? 162  ARG   B CD    1 
ATOM   10137 N  NE    . ARG   B  1  164  ? 3.679   54.378  108.847 1.00 31.95 ? 162  ARG   B NE    1 
ATOM   10138 C  CZ    . ARG   B  1  164  ? 4.122   54.474  110.092 1.00 37.84 ? 162  ARG   B CZ    1 
ATOM   10139 N  NH1   . ARG   B  1  164  ? 4.884   53.532  110.631 1.00 38.59 ? 162  ARG   B NH1   1 
ATOM   10140 N  NH2   . ARG   B  1  164  ? 3.792   55.539  110.814 1.00 31.71 ? 162  ARG   B NH2   1 
ATOM   10141 N  N     . SER   B  1  165  ? -1.073  51.675  108.395 1.00 16.93 ? 163  SER   B N     1 
ATOM   10142 C  CA    . SER   B  1  165  ? -2.436  51.703  108.903 1.00 14.91 ? 163  SER   B CA    1 
ATOM   10143 C  C     . SER   B  1  165  ? -2.514  51.053  110.274 1.00 16.65 ? 163  SER   B C     1 
ATOM   10144 O  O     . SER   B  1  165  ? -3.205  51.554  111.168 1.00 16.16 ? 163  SER   B O     1 
ATOM   10145 C  CB    . SER   B  1  165  ? -3.331  50.952  107.918 1.00 16.15 ? 163  SER   B CB    1 
ATOM   10146 O  OG    . SER   B  1  165  ? -4.630  50.781  108.456 1.00 18.72 ? 163  SER   B OG    1 
ATOM   10147 N  N     . LEU   B  1  166  ? -1.821  49.923  110.435 1.00 16.75 ? 164  LEU   B N     1 
ATOM   10148 C  CA    . LEU   B  1  166  ? -1.835  49.235  111.720 1.00 16.22 ? 164  LEU   B CA    1 
ATOM   10149 C  C     . LEU   B  1  166  ? -1.146  50.054  112.798 1.00 17.53 ? 164  LEU   B C     1 
ATOM   10150 O  O     . LEU   B  1  166  ? -1.624  50.104  113.926 1.00 17.43 ? 164  LEU   B O     1 
ATOM   10151 C  CB    . LEU   B  1  166  ? -1.181  47.864  111.563 1.00 16.46 ? 164  LEU   B CB    1 
ATOM   10152 C  CG    . LEU   B  1  166  ? -2.083  46.913  110.787 1.00 16.65 ? 164  LEU   B CG    1 
ATOM   10153 C  CD1   . LEU   B  1  166  ? -1.374  45.647  110.442 1.00 21.66 ? 164  LEU   B CD1   1 
ATOM   10154 C  CD2   . LEU   B  1  166  ? -3.338  46.609  111.596 1.00 17.92 ? 164  LEU   B CD2   1 
ATOM   10155 N  N     . ALA   B  1  167  ? -0.019  50.692  112.468 1.00 16.12 ? 165  ALA   B N     1 
ATOM   10156 C  CA    . ALA   B  1  167  ? 0.650   51.539  113.444 1.00 16.19 ? 165  ALA   B CA    1 
ATOM   10157 C  C     . ALA   B  1  167  ? -0.244  52.694  113.870 1.00 17.79 ? 165  ALA   B C     1 
ATOM   10158 O  O     . ALA   B  1  167  ? -0.349  53.003  115.054 1.00 18.62 ? 165  ALA   B O     1 
ATOM   10159 C  CB    . ALA   B  1  167  ? 1.955   52.067  112.856 1.00 18.19 ? 165  ALA   B CB    1 
ATOM   10160 N  N     . ALA   B  1  168  ? -0.918  53.329  112.903 1.00 17.12 ? 166  ALA   B N     1 
ATOM   10161 C  CA    . ALA   B  1  168  ? -1.856  54.388  113.232 1.00 16.76 ? 166  ALA   B CA    1 
ATOM   10162 C  C     . ALA   B  1  168  ? -2.981  53.864  114.113 1.00 15.51 ? 166  ALA   B C     1 
ATOM   10163 O  O     . ALA   B  1  168  ? -3.371  54.506  115.084 1.00 17.88 ? 166  ALA   B O     1 
ATOM   10164 C  CB    . ALA   B  1  168  ? -2.436  54.960  111.934 1.00 18.00 ? 166  ALA   B CB    1 
ATOM   10165 N  N     . ALA   B  1  169  ? -3.497  52.676  113.777 1.00 15.71 ? 167  ALA   B N     1 
ATOM   10166 C  CA    . ALA   B  1  169  ? -4.609  52.122  114.540 1.00 17.25 ? 167  ALA   B CA    1 
ATOM   10167 C  C     . ALA   B  1  169  ? -4.188  51.775  115.962 1.00 18.18 ? 167  ALA   B C     1 
ATOM   10168 O  O     . ALA   B  1  169  ? -4.961  51.968  116.900 1.00 17.86 ? 167  ALA   B O     1 
ATOM   10169 C  CB    . ALA   B  1  169  ? -5.132  50.882  113.830 1.00 17.76 ? 167  ALA   B CB    1 
ATOM   10170 N  N     . LEU   B  1  170  ? -2.971  51.254  116.132 1.00 16.96 ? 168  LEU   B N     1 
ATOM   10171 C  CA    . LEU   B  1  170  ? -2.507  50.907  117.472 1.00 16.87 ? 168  LEU   B CA    1 
ATOM   10172 C  C     . LEU   B  1  170  ? -2.310  52.155  118.312 1.00 18.13 ? 168  LEU   B C     1 
ATOM   10173 O  O     . LEU   B  1  170  ? -2.720  52.206  119.473 1.00 18.83 ? 168  LEU   B O     1 
ATOM   10174 C  CB    . LEU   B  1  170  ? -1.211  50.110  117.376 1.00 18.30 ? 168  LEU   B CB    1 
ATOM   10175 C  CG    . LEU   B  1  170  ? -0.749  49.554  118.721 1.00 18.63 ? 168  LEU   B CG    1 
ATOM   10176 C  CD1   . LEU   B  1  170  ? -1.832  48.685  119.359 1.00 21.23 ? 168  LEU   B CD1   1 
ATOM   10177 C  CD2   . LEU   B  1  170  ? 0.502   48.763  118.492 1.00 21.46 ? 168  LEU   B CD2   1 
ATOM   10178 N  N     . THR   B  1  171  ? -1.664  53.174  117.746 1.00 18.88 ? 169  THR   B N     1 
ATOM   10179 C  CA    . THR   B  1  171  ? -1.541  54.444  118.448 1.00 19.84 ? 169  THR   B CA    1 
ATOM   10180 C  C     . THR   B  1  171  ? -2.908  54.985  118.828 1.00 19.58 ? 169  THR   B C     1 
ATOM   10181 O  O     . THR   B  1  171  ? -3.128  55.446  119.954 1.00 20.05 ? 169  THR   B O     1 
ATOM   10182 C  CB    . THR   B  1  171  ? -0.811  55.444  117.565 1.00 20.93 ? 169  THR   B CB    1 
ATOM   10183 O  OG1   . THR   B  1  171  ? 0.508   54.954  117.308 1.00 24.16 ? 169  THR   B OG1   1 
ATOM   10184 C  CG2   . THR   B  1  171  ? -0.732  56.792  118.223 1.00 22.53 ? 169  THR   B CG2   1 
ATOM   10185 N  N     . ARG   B  1  172  ? -3.850  54.931  117.882 1.00 18.27 ? 170  ARG   B N     1 
ATOM   10186 C  CA    . ARG   B  1  172  ? -5.160  55.496  118.151 1.00 18.42 ? 170  ARG   B CA    1 
ATOM   10187 C  C     . ARG   B  1  172  ? -5.849  54.746  119.282 1.00 18.21 ? 170  ARG   B C     1 
ATOM   10188 O  O     . ARG   B  1  172  ? -6.396  55.353  120.201 1.00 19.14 ? 170  ARG   B O     1 
ATOM   10189 C  CB    . ARG   B  1  172  ? -6.005  55.465  116.880 1.00 19.05 ? 170  ARG   B CB    1 
ATOM   10190 C  CG    . ARG   B  1  172  ? -7.292  56.269  117.016 1.00 17.99 ? 170  ARG   B CG    1 
ATOM   10191 C  CD    . ARG   B  1  172  ? -8.178  56.092  115.774 1.00 17.87 ? 170  ARG   B CD    1 
ATOM   10192 N  NE    . ARG   B  1  172  ? -7.451  56.205  114.518 1.00 17.69 ? 170  ARG   B NE    1 
ATOM   10193 C  CZ    . ARG   B  1  172  ? -7.155  55.177  113.740 1.00 17.87 ? 170  ARG   B CZ    1 
ATOM   10194 N  NH1   . ARG   B  1  172  ? -7.497  53.940  114.062 1.00 18.87 ? 170  ARG   B NH1   1 
ATOM   10195 N  NH2   . ARG   B  1  172  ? -6.482  55.386  112.613 1.00 17.39 ? 170  ARG   B NH2   1 
ATOM   10196 N  N     . LEU   B  1  173  ? -5.834  53.412  119.225 1.00 20.00 ? 171  LEU   B N     1 
ATOM   10197 C  CA    . LEU   B  1  173  ? -6.577  52.673  120.242 1.00 18.50 ? 171  LEU   B CA    1 
ATOM   10198 C  C     . LEU   B  1  173  ? -5.938  52.805  121.614 1.00 20.83 ? 171  LEU   B C     1 
ATOM   10199 O  O     . LEU   B  1  173  ? -6.647  52.879  122.615 1.00 20.28 ? 171  LEU   B O     1 
ATOM   10200 C  CB    . LEU   B  1  173  ? -6.745  51.212  119.844 1.00 20.73 ? 171  LEU   B CB    1 
ATOM   10201 C  CG    . LEU   B  1  173  ? -5.567  50.237  119.881 1.00 20.20 ? 171  LEU   B CG    1 
ATOM   10202 C  CD1   . LEU   B  1  173  ? -5.504  49.561  121.249 1.00 22.70 ? 171  LEU   B CD1   1 
ATOM   10203 C  CD2   . LEU   B  1  173  ? -5.741  49.200  118.808 1.00 20.67 ? 171  LEU   B CD2   1 
ATOM   10204 N  N     . ILE   B  1  174  ? -4.607  52.828  121.684 1.00 20.41 ? 172  ILE   B N     1 
ATOM   10205 C  CA    . ILE   B  1  174  ? -3.974  52.973  122.991 1.00 19.99 ? 172  ILE   B CA    1 
ATOM   10206 C  C     . ILE   B  1  174  ? -4.217  54.364  123.551 1.00 22.26 ? 172  ILE   B C     1 
ATOM   10207 O  O     . ILE   B  1  174  ? -4.494  54.528  124.745 1.00 23.42 ? 172  ILE   B O     1 
ATOM   10208 C  CB    . ILE   B  1  174  ? -2.475  52.656  122.904 1.00 20.60 ? 172  ILE   B CB    1 
ATOM   10209 C  CG1   . ILE   B  1  174  ? -2.253  51.190  122.567 1.00 21.91 ? 172  ILE   B CG1   1 
ATOM   10210 C  CG2   . ILE   B  1  174  ? -1.792  53.001  124.228 1.00 22.70 ? 172  ILE   B CG2   1 
ATOM   10211 C  CD1   . ILE   B  1  174  ? -0.813  50.854  122.276 1.00 22.99 ? 172  ILE   B CD1   1 
ATOM   10212 N  N     . SER   B  1  175  ? -4.099  55.392  122.706 1.00 22.31 ? 173  SER   B N     1 
ATOM   10213 C  CA    . SER   B  1  175  ? -4.337  56.741  123.195 1.00 22.01 ? 173  SER   B CA    1 
ATOM   10214 C  C     . SER   B  1  175  ? -5.791  56.945  123.589 1.00 20.04 ? 173  SER   B C     1 
ATOM   10215 O  O     . SER   B  1  175  ? -6.084  57.795  124.426 1.00 24.80 ? 173  SER   B O     1 
ATOM   10216 C  CB    . SER   B  1  175  ? -3.928  57.767  122.138 1.00 23.83 ? 173  SER   B CB    1 
ATOM   10217 O  OG    . SER   B  1  175  ? -2.540  57.671  121.866 1.00 29.06 ? 173  SER   B OG    1 
ATOM   10218 N  N     . ARG   B  1  176  ? -6.705  56.183  122.989 1.00 21.42 ? 174  ARG   B N     1 
ATOM   10219 C  CA    . ARG   B  1  176  ? -8.115  56.333  123.310 1.00 21.20 ? 174  ARG   B CA    1 
ATOM   10220 C  C     . ARG   B  1  176  ? -8.491  55.521  124.548 1.00 23.37 ? 174  ARG   B C     1 
ATOM   10221 O  O     . ARG   B  1  176  ? -9.249  55.997  125.393 1.00 25.18 ? 174  ARG   B O     1 
ATOM   10222 C  CB    . ARG   B  1  176  ? -8.959  55.908  122.102 1.00 22.59 ? 174  ARG   B CB    1 
ATOM   10223 C  CG    . ARG   B  1  176  ? -10.457 56.201  122.242 1.00 23.83 ? 174  ARG   B CG    1 
ATOM   10224 C  CD    . ARG   B  1  176  ? -11.185 55.866  120.927 1.00 22.19 ? 174  ARG   B CD    1 
ATOM   10225 N  NE    . ARG   B  1  176  ? -11.297 54.429  120.685 1.00 22.73 ? 174  ARG   B NE    1 
ATOM   10226 C  CZ    . ARG   B  1  176  ? -10.723 53.757  119.690 1.00 23.49 ? 174  ARG   B CZ    1 
ATOM   10227 N  NH1   . ARG   B  1  176  ? -10.006 54.365  118.743 1.00 22.15 ? 174  ARG   B NH1   1 
ATOM   10228 N  NH2   . ARG   B  1  176  ? -10.870 52.436  119.635 1.00 26.65 ? 174  ARG   B NH2   1 
ATOM   10229 N  N     . CYS   B  1  177  ? -7.985  54.286  124.655 1.00 23.11 ? 175  CYS   B N     1 
ATOM   10230 C  CA    . CYS   B  1  177  ? -8.482  53.356  125.659 1.00 24.55 ? 175  CYS   B CA    1 
ATOM   10231 C  C     . CYS   B  1  177  ? -7.447  52.913  126.677 1.00 26.96 ? 175  CYS   B C     1 
ATOM   10232 O  O     . CYS   B  1  177  ? -7.834  52.350  127.705 1.00 28.29 ? 175  CYS   B O     1 
ATOM   10233 C  CB    . CYS   B  1  177  ? -9.068  52.103  124.997 1.00 24.88 ? 175  CYS   B CB    1 
ATOM   10234 S  SG    . CYS   B  1  177  ? -10.334 52.450  123.728 1.00 31.52 ? 175  CYS   B SG    1 
ATOM   10235 N  N     . GLY   B  1  178  ? -6.158  53.111  126.411 1.00 25.96 ? 176  GLY   B N     1 
ATOM   10236 C  CA    . GLY   B  1  178  ? -5.199  52.947  127.493 1.00 26.33 ? 176  GLY   B CA    1 
ATOM   10237 C  C     . GLY   B  1  178  ? -4.949  51.501  127.894 1.00 25.99 ? 176  GLY   B C     1 
ATOM   10238 O  O     . GLY   B  1  178  ? -5.212  50.551  127.161 1.00 25.20 ? 176  GLY   B O     1 
ATOM   10239 N  N     . GLU   B  1  179  ? -4.427  51.351  129.108 1.00 25.64 ? 177  GLU   B N     1 
ATOM   10240 C  CA    . GLU   B  1  179  ? -4.098  50.019  129.605 1.00 27.98 ? 177  GLU   B CA    1 
ATOM   10241 C  C     . GLU   B  1  179  ? -5.265  49.037  129.596 1.00 22.81 ? 177  GLU   B C     1 
ATOM   10242 O  O     . GLU   B  1  179  ? -5.035  47.865  129.253 1.00 24.16 ? 177  GLU   B O     1 
ATOM   10243 C  CB    . GLU   B  1  179  ? -3.434  50.098  130.989 1.00 30.57 ? 177  GLU   B CB    1 
ATOM   10244 C  CG    . GLU   B  1  179  ? -3.148  48.719  131.582 1.00 32.16 ? 177  GLU   B CG    1 
ATOM   10245 C  CD    . GLU   B  1  179  ? -2.294  48.766  132.830 1.00 48.54 ? 177  GLU   B CD    1 
ATOM   10246 O  OE1   . GLU   B  1  179  ? -1.716  49.834  133.122 1.00 50.49 ? 177  GLU   B OE1   1 
ATOM   10247 O  OE2   . GLU   B  1  179  ? -2.199  47.725  133.515 1.00 55.64 ? 177  GLU   B OE2   1 
ATOM   10248 N  N     . PRO   B  1  180  ? -6.505  49.418  129.927 1.00 24.76 ? 178  PRO   B N     1 
ATOM   10249 C  CA    . PRO   B  1  180  ? -7.579  48.413  129.926 1.00 26.04 ? 178  PRO   B CA    1 
ATOM   10250 C  C     . PRO   B  1  180  ? -7.737  47.668  128.613 1.00 27.50 ? 178  PRO   B C     1 
ATOM   10251 O  O     . PRO   B  1  180  ? -7.984  46.457  128.625 1.00 27.87 ? 178  PRO   B O     1 
ATOM   10252 C  CB    . PRO   B  1  180  ? -8.822  49.227  130.296 1.00 27.70 ? 178  PRO   B CB    1 
ATOM   10253 C  CG    . PRO   B  1  180  ? -8.289  50.316  131.163 1.00 30.73 ? 178  PRO   B CG    1 
ATOM   10254 C  CD    . PRO   B  1  180  ? -6.961  50.682  130.538 1.00 28.07 ? 178  PRO   B CD    1 
ATOM   10255 N  N     . VAL   B  1  181  ? -7.587  48.337  127.470 1.00 22.97 ? 179  VAL   B N     1 
ATOM   10256 C  CA    . VAL   B  1  181  ? -7.748  47.593  126.229 1.00 22.41 ? 179  VAL   B CA    1 
ATOM   10257 C  C     . VAL   B  1  181  ? -6.548  46.695  125.963 1.00 21.47 ? 179  VAL   B C     1 
ATOM   10258 O  O     . VAL   B  1  181  ? -6.694  45.605  125.394 1.00 22.62 ? 179  VAL   B O     1 
ATOM   10259 C  CB    . VAL   B  1  181  ? -8.074  48.512  125.034 1.00 22.54 ? 179  VAL   B CB    1 
ATOM   10260 C  CG1   . VAL   B  1  181  ? -6.845  49.309  124.601 1.00 23.64 ? 179  VAL   B CG1   1 
ATOM   10261 C  CG2   . VAL   B  1  181  ? -8.596  47.681  123.877 1.00 26.83 ? 179  VAL   B CG2   1 
ATOM   10262 N  N     . ILE   B  1  182  ? -5.346  47.134  126.347 1.00 21.74 ? 180  ILE   B N     1 
ATOM   10263 C  CA    . ILE   B  1  182  ? -4.166  46.288  126.204 1.00 23.56 ? 180  ILE   B CA    1 
ATOM   10264 C  C     . ILE   B  1  182  ? -4.321  45.030  127.042 1.00 24.23 ? 180  ILE   B C     1 
ATOM   10265 O  O     . ILE   B  1  182  ? -4.056  43.918  126.570 1.00 24.20 ? 180  ILE   B O     1 
ATOM   10266 C  CB    . ILE   B  1  182  ? -2.893  47.073  126.569 1.00 23.69 ? 180  ILE   B CB    1 
ATOM   10267 C  CG1   . ILE   B  1  182  ? -2.736  48.281  125.647 1.00 23.03 ? 180  ILE   B CG1   1 
ATOM   10268 C  CG2   . ILE   B  1  182  ? -1.665  46.165  126.484 1.00 24.90 ? 180  ILE   B CG2   1 
ATOM   10269 C  CD1   . ILE   B  1  182  ? -1.705  49.274  126.136 1.00 26.00 ? 180  ILE   B CD1   1 
ATOM   10270 N  N     . ARG   B  1  183  ? -4.772  45.188  128.292 1.00 26.51 ? 181  ARG   B N     1 
ATOM   10271 C  CA    . ARG   B  1  183  ? -4.992  44.040  129.164 1.00 26.90 ? 181  ARG   B CA    1 
ATOM   10272 C  C     . ARG   B  1  183  ? -6.005  43.073  128.562 1.00 27.92 ? 181  ARG   B C     1 
ATOM   10273 O  O     . ARG   B  1  183  ? -5.772  41.859  128.527 1.00 28.80 ? 181  ARG   B O     1 
ATOM   10274 C  CB    . ARG   B  1  183  ? -5.428  44.526  130.549 1.00 27.92 ? 181  ARG   B CB    1 
ATOM   10275 C  CG    . ARG   B  1  183  ? -5.970  43.442  131.485 1.00 38.58 ? 181  ARG   B CG    1 
ATOM   10276 C  CD    . ARG   B  1  183  ? -5.042  42.241  131.546 1.00 39.91 ? 181  ARG   B CD    1 
ATOM   10277 N  NE    . ARG   B  1  183  ? -3.685  42.618  131.907 1.00 44.04 ? 181  ARG   B NE    1 
ATOM   10278 C  CZ    . ARG   B  1  183  ? -2.616  41.885  131.642 1.00 39.48 ? 181  ARG   B CZ    1 
ATOM   10279 N  NH1   . ARG   B  1  183  ? -2.708  40.747  130.971 1.00 39.54 ? 181  ARG   B NH1   1 
ATOM   10280 N  NH2   . ARG   B  1  183  ? -1.424  42.305  132.056 1.00 40.23 ? 181  ARG   B NH2   1 
ATOM   10281 N  N     . ARG   B  1  184  ? -7.135  43.595  128.074 1.00 28.30 ? 182  ARG   B N     1 
ATOM   10282 C  CA    . ARG   B  1  184  ? -8.133  42.737  127.438 1.00 28.31 ? 182  ARG   B CA    1 
ATOM   10283 C  C     . ARG   B  1  184  ? -7.564  42.031  126.214 1.00 27.97 ? 182  ARG   B C     1 
ATOM   10284 O  O     . ARG   B  1  184  ? -7.831  40.844  125.996 1.00 28.60 ? 182  ARG   B O     1 
ATOM   10285 C  CB    . ARG   B  1  184  ? -9.372  43.549  127.058 1.00 29.34 ? 182  ARG   B CB    1 
ATOM   10286 C  CG    . ARG   B  1  184  ? -10.275 43.892  128.235 1.00 34.61 ? 182  ARG   B CG    1 
ATOM   10287 C  CD    . ARG   B  1  184  ? -11.267 42.768  128.525 1.00 39.29 ? 182  ARG   B CD    1 
ATOM   10288 N  NE    . ARG   B  1  184  ? -12.455 42.849  127.681 1.00 33.23 ? 182  ARG   B NE    1 
ATOM   10289 C  CZ    . ARG   B  1  184  ? -12.858 41.906  126.839 1.00 33.87 ? 182  ARG   B CZ    1 
ATOM   10290 N  NH1   . ARG   B  1  184  ? -12.197 40.768  126.703 1.00 37.25 ? 182  ARG   B NH1   1 
ATOM   10291 N  NH2   . ARG   B  1  184  ? -13.957 42.109  126.118 1.00 37.37 ? 182  ARG   B NH2   1 
ATOM   10292 N  N     . GLY   B  1  185  ? -6.788  42.741  125.394 1.00 27.38 ? 183  GLY   B N     1 
ATOM   10293 C  CA    . GLY   B  1  185  ? -6.206  42.103  124.226 1.00 25.34 ? 183  GLY   B CA    1 
ATOM   10294 C  C     . GLY   B  1  185  ? -5.233  40.999  124.592 1.00 27.45 ? 183  GLY   B C     1 
ATOM   10295 O  O     . GLY   B  1  185  ? -5.235  39.927  123.982 1.00 25.52 ? 183  GLY   B O     1 
ATOM   10296 N  N     . VAL   B  1  186  ? -4.389  41.249  125.594 1.00 25.74 ? 184  VAL   B N     1 
ATOM   10297 C  CA    . VAL   B  1  186  ? -3.417  40.246  126.024 1.00 28.40 ? 184  VAL   B CA    1 
ATOM   10298 C  C     . VAL   B  1  186  ? -4.131  39.003  126.540 1.00 27.63 ? 184  VAL   B C     1 
ATOM   10299 O  O     . VAL   B  1  186  ? -3.807  37.872  126.158 1.00 27.80 ? 184  VAL   B O     1 
ATOM   10300 C  CB    . VAL   B  1  186  ? -2.466  40.844  127.077 1.00 26.12 ? 184  VAL   B CB    1 
ATOM   10301 C  CG1   . VAL   B  1  186  ? -1.722  39.740  127.811 1.00 29.19 ? 184  VAL   B CG1   1 
ATOM   10302 C  CG2   . VAL   B  1  186  ? -1.486  41.793  126.408 1.00 26.46 ? 184  VAL   B CG2   1 
ATOM   10303 N  N     . ASP   B  1  187  ? -5.120  39.198  127.408 1.00 26.86 ? 185  ASP   B N     1 
ATOM   10304 C  CA    . ASP   B  1  187  ? -5.872  38.064  127.932 1.00 32.05 ? 185  ASP   B CA    1 
ATOM   10305 C  C     . ASP   B  1  187  ? -6.575  37.313  126.815 1.00 33.21 ? 185  ASP   B C     1 
ATOM   10306 O  O     . ASP   B  1  187  ? -6.621  36.077  126.821 1.00 29.95 ? 185  ASP   B O     1 
ATOM   10307 C  CB    . ASP   B  1  187  ? -6.878  38.546  128.970 1.00 30.03 ? 185  ASP   B CB    1 
ATOM   10308 C  CG    . ASP   B  1  187  ? -6.206  39.076  130.223 1.00 32.79 ? 185  ASP   B CG    1 
ATOM   10309 O  OD1   . ASP   B  1  187  ? -4.985  38.856  130.386 1.00 36.99 ? 185  ASP   B OD1   1 
ATOM   10310 O  OD2   . ASP   B  1  187  ? -6.893  39.721  131.039 1.00 35.17 ? 185  ASP   B OD2   1 
ATOM   10311 N  N     . MET   B  1  188  ? -7.107  38.045  125.834 1.00 30.65 ? 186  MET   B N     1 
ATOM   10312 C  CA    . MET   B  1  188  ? -7.793  37.415  124.715 1.00 30.39 ? 186  MET   B CA    1 
ATOM   10313 C  C     . MET   B  1  188  ? -6.824  36.586  123.883 1.00 28.66 ? 186  MET   B C     1 
ATOM   10314 O  O     . MET   B  1  188  ? -7.100  35.425  123.559 1.00 30.91 ? 186  MET   B O     1 
ATOM   10315 C  CB    . MET   B  1  188  ? -8.459  38.491  123.859 1.00 30.01 ? 186  MET   B CB    1 
ATOM   10316 C  CG    . MET   B  1  188  ? -9.259  37.954  122.702 1.00 36.32 ? 186  MET   B CG    1 
ATOM   10317 S  SD    . MET   B  1  188  ? -10.509 36.791  123.268 1.00 51.25 ? 186  MET   B SD    1 
ATOM   10318 C  CE    . MET   B  1  188  ? -11.399 37.789  124.466 1.00 46.06 ? 186  MET   B CE    1 
ATOM   10319 N  N     . ALA   B  1  189  ? -5.679  37.167  123.521 1.00 28.71 ? 187  ALA   B N     1 
ATOM   10320 C  CA    . ALA   B  1  189  ? -4.721  36.429  122.703 1.00 28.62 ? 187  ALA   B CA    1 
ATOM   10321 C  C     . ALA   B  1  189  ? -4.169  35.229  123.461 1.00 29.10 ? 187  ALA   B C     1 
ATOM   10322 O  O     . ALA   B  1  189  ? -3.943  34.164  122.876 1.00 29.26 ? 187  ALA   B O     1 
ATOM   10323 C  CB    . ALA   B  1  189  ? -3.592  37.350  122.245 1.00 30.59 ? 187  ALA   B CB    1 
ATOM   10324 N  N     . MET   B  1  190  ? -3.943  35.386  124.765 1.00 27.30 ? 188  MET   B N     1 
ATOM   10325 C  CA    . MET   B  1  190  ? -3.472  34.268  125.576 1.00 30.35 ? 188  MET   B CA    1 
ATOM   10326 C  C     . MET   B  1  190  ? -4.454  33.104  125.515 1.00 32.21 ? 188  MET   B C     1 
ATOM   10327 O  O     . MET   B  1  190  ? -4.058  31.949  125.325 1.00 31.28 ? 188  MET   B O     1 
ATOM   10328 C  CB    . MET   B  1  190  ? -3.274  34.727  127.020 1.00 32.09 ? 188  MET   B CB    1 
ATOM   10329 C  CG    . MET   B  1  190  ? -2.540  33.725  127.874 1.00 36.82 ? 188  MET   B CG    1 
ATOM   10330 S  SD    . MET   B  1  190  ? -2.469  34.242  129.596 1.00 45.50 ? 188  MET   B SD    1 
ATOM   10331 C  CE    . MET   B  1  190  ? -2.011  35.968  129.424 1.00 34.60 ? 188  MET   B CE    1 
ATOM   10332 N  N     . ARG   B  1  191  ? -5.747  33.394  125.673 1.00 28.77 ? 189  ARG   B N     1 
ATOM   10333 C  CA    . ARG   B  1  191  ? -6.754  32.341  125.601 1.00 31.60 ? 189  ARG   B CA    1 
ATOM   10334 C  C     . ARG   B  1  191  ? -6.807  31.737  124.204 1.00 35.24 ? 189  ARG   B C     1 
ATOM   10335 O  O     . ARG   B  1  191  ? -6.818  30.510  124.044 1.00 30.96 ? 189  ARG   B O     1 
ATOM   10336 C  CB    . ARG   B  1  191  ? -8.123  32.887  126.011 1.00 32.70 ? 189  ARG   B CB    1 
ATOM   10337 C  CG    . ARG   B  1  191  ? -9.206  31.823  126.101 1.00 42.31 ? 189  ARG   B CG    1 
ATOM   10338 C  CD    . ARG   B  1  191  ? -10.571 32.422  126.452 1.00 48.64 ? 189  ARG   B CD    1 
ATOM   10339 N  NE    . ARG   B  1  191  ? -11.155 33.166  125.340 1.00 54.23 ? 189  ARG   B NE    1 
ATOM   10340 C  CZ    . ARG   B  1  191  ? -12.294 33.845  125.405 1.00 54.78 ? 189  ARG   B CZ    1 
ATOM   10341 N  NH1   . ARG   B  1  191  ? -13.006 33.898  126.520 1.00 58.62 ? 189  ARG   B NH1   1 
ATOM   10342 N  NH2   . ARG   B  1  191  ? -12.728 34.489  124.326 1.00 58.37 ? 189  ARG   B NH2   1 
ATOM   10343 N  N     . MET   B  1  192  ? -6.825  32.584  123.176 1.00 29.76 ? 190  MET   B N     1 
ATOM   10344 C  CA    . MET   B  1  192  ? -6.910  32.074  121.813 1.00 28.66 ? 190  MET   B CA    1 
ATOM   10345 C  C     . MET   B  1  192  ? -5.714  31.198  121.476 1.00 32.23 ? 190  MET   B C     1 
ATOM   10346 O  O     . MET   B  1  192  ? -5.869  30.076  120.979 1.00 29.44 ? 190  MET   B O     1 
ATOM   10347 C  CB    . MET   B  1  192  ? -7.015  33.234  120.826 1.00 30.31 ? 190  MET   B CB    1 
ATOM   10348 C  CG    . MET   B  1  192  ? -8.243  34.091  121.034 1.00 36.17 ? 190  MET   B CG    1 
ATOM   10349 S  SD    . MET   B  1  192  ? -8.458  35.229  119.664 1.00 44.19 ? 190  MET   B SD    1 
ATOM   10350 C  CE    . MET   B  1  192  ? -9.049  34.081  118.432 1.00 36.03 ? 190  MET   B CE    1 
ATOM   10351 N  N     . MET   B  1  193  ? -4.508  31.692  121.738 1.00 28.28 ? 191  MET   B N     1 
ATOM   10352 C  CA    A MET   B  1  193  ? -3.302  30.974  121.349 0.49 31.39 ? 191  MET   B CA    1 
ATOM   10353 C  CA    B MET   B  1  193  ? -3.324  30.952  121.334 0.51 31.37 ? 191  MET   B CA    1 
ATOM   10354 C  C     . MET   B  1  193  ? -2.978  29.813  122.277 1.00 31.20 ? 191  MET   B C     1 
ATOM   10355 O  O     . MET   B  1  193  ? -2.226  28.916  121.884 1.00 31.22 ? 191  MET   B O     1 
ATOM   10356 C  CB    A MET   B  1  193  ? -2.109  31.934  121.304 0.49 31.81 ? 191  MET   B CB    1 
ATOM   10357 C  CB    B MET   B  1  193  ? -2.135  31.896  121.176 0.51 31.84 ? 191  MET   B CB    1 
ATOM   10358 C  CG    A MET   B  1  193  ? -2.322  33.157  120.423 0.49 29.91 ? 191  MET   B CG    1 
ATOM   10359 C  CG    B MET   B  1  193  ? -2.246  32.765  119.946 0.51 31.80 ? 191  MET   B CG    1 
ATOM   10360 S  SD    A MET   B  1  193  ? -0.933  34.311  120.487 0.49 31.06 ? 191  MET   B SD    1 
ATOM   10361 S  SD    B MET   B  1  193  ? -0.713  33.613  119.570 0.51 33.14 ? 191  MET   B SD    1 
ATOM   10362 C  CE    A MET   B  1  193  ? 0.134   33.622  119.227 0.49 37.50 ? 191  MET   B CE    1 
ATOM   10363 C  CE    B MET   B  1  193  ? -0.603  34.748  120.952 0.51 32.24 ? 191  MET   B CE    1 
ATOM   10364 N  N     . GLY   B  1  194  ? -3.517  29.813  123.490 1.00 30.02 ? 192  GLY   B N     1 
ATOM   10365 C  CA    . GLY   B  1  194  ? -3.178  28.782  124.447 1.00 31.87 ? 192  GLY   B CA    1 
ATOM   10366 C  C     . GLY   B  1  194  ? -4.230  27.706  124.593 1.00 29.59 ? 192  GLY   B C     1 
ATOM   10367 O  O     . GLY   B  1  194  ? -3.920  26.593  125.029 1.00 30.38 ? 192  GLY   B O     1 
ATOM   10368 N  N     . GLU   B  1  195  ? -5.476  28.020  124.234 1.00 28.45 ? 193  GLU   B N     1 
ATOM   10369 C  CA    . GLU   B  1  195  ? -6.593  27.121  124.506 1.00 32.87 ? 193  GLU   B CA    1 
ATOM   10370 C  C     . GLU   B  1  195  ? -7.503  26.875  123.319 1.00 30.08 ? 193  GLU   B C     1 
ATOM   10371 O  O     . GLU   B  1  195  ? -8.233  25.878  123.327 1.00 27.85 ? 193  GLU   B O     1 
ATOM   10372 C  CB    . GLU   B  1  195  ? -7.457  27.652  125.659 1.00 33.93 ? 193  GLU   B CB    1 
ATOM   10373 C  CG    . GLU   B  1  195  ? -6.694  28.047  126.901 1.00 43.77 ? 193  GLU   B CG    1 
ATOM   10374 C  CD    . GLU   B  1  195  ? -7.561  28.827  127.862 1.00 46.77 ? 193  GLU   B CD    1 
ATOM   10375 O  OE1   . GLU   B  1  195  ? -8.758  28.489  127.986 1.00 50.70 ? 193  GLU   B OE1   1 
ATOM   10376 O  OE2   . GLU   B  1  195  ? -7.052  29.788  128.479 1.00 52.31 ? 193  GLU   B OE2   1 
ATOM   10377 N  N     . GLN   B  1  196  ? -7.505  27.738  122.314 1.00 30.41 ? 194  GLN   B N     1 
ATOM   10378 C  CA    . GLN   B  1  196  ? -8.400  27.590  121.178 1.00 31.34 ? 194  GLN   B CA    1 
ATOM   10379 C  C     . GLN   B  1  196  ? -7.670  27.120  119.931 1.00 33.43 ? 194  GLN   B C     1 
ATOM   10380 O  O     . GLN   B  1  196  ? -8.062  26.122  119.321 1.00 35.80 ? 194  GLN   B O     1 
ATOM   10381 C  CB    . GLN   B  1  196  ? -9.109  28.924  120.924 1.00 35.60 ? 194  GLN   B CB    1 
ATOM   10382 C  CG    . GLN   B  1  196  ? -10.092 28.927  119.778 1.00 44.46 ? 194  GLN   B CG    1 
ATOM   10383 C  CD    . GLN   B  1  196  ? -10.704 30.295  119.586 1.00 48.56 ? 194  GLN   B CD    1 
ATOM   10384 O  OE1   . GLN   B  1  196  ? -10.738 31.106  120.516 1.00 52.02 ? 194  GLN   B OE1   1 
ATOM   10385 N  NE2   . GLN   B  1  196  ? -11.179 30.570  118.377 1.00 52.72 ? 194  GLN   B NE2   1 
ATOM   10386 N  N     . PHE   B  1  197  ? -6.593  27.802  119.548 1.00 30.20 ? 195  PHE   B N     1 
ATOM   10387 C  CA    . PHE   B  1  197  ? -5.832  27.368  118.383 1.00 31.09 ? 195  PHE   B CA    1 
ATOM   10388 C  C     . PHE   B  1  197  ? -5.089  26.071  118.658 1.00 31.19 ? 195  PHE   B C     1 
ATOM   10389 O  O     . PHE   B  1  197  ? -4.778  25.321  117.724 1.00 33.19 ? 195  PHE   B O     1 
ATOM   10390 C  CB    . PHE   B  1  197  ? -4.847  28.455  117.961 1.00 33.76 ? 195  PHE   B CB    1 
ATOM   10391 C  CG    . PHE   B  1  197  ? -5.505  29.737  117.545 1.00 30.65 ? 195  PHE   B CG    1 
ATOM   10392 C  CD1   . PHE   B  1  197  ? -6.771  29.729  116.985 1.00 37.49 ? 195  PHE   B CD1   1 
ATOM   10393 C  CD2   . PHE   B  1  197  ? -4.860  30.948  117.725 1.00 34.21 ? 195  PHE   B CD2   1 
ATOM   10394 C  CE1   . PHE   B  1  197  ? -7.380  30.910  116.598 1.00 40.94 ? 195  PHE   B CE1   1 
ATOM   10395 C  CE2   . PHE   B  1  197  ? -5.465  32.134  117.340 1.00 35.92 ? 195  PHE   B CE2   1 
ATOM   10396 C  CZ    . PHE   B  1  197  ? -6.723  32.112  116.780 1.00 37.13 ? 195  PHE   B CZ    1 
ATOM   10397 N  N     . VAL   B  1  198  ? -4.773  25.807  119.921 1.00 30.76 ? 196  VAL   B N     1 
ATOM   10398 C  CA    . VAL   B  1  198  ? -4.157  24.555  120.328 1.00 28.35 ? 196  VAL   B CA    1 
ATOM   10399 C  C     . VAL   B  1  198  ? -4.913  24.040  121.538 1.00 27.89 ? 196  VAL   B C     1 
ATOM   10400 O  O     . VAL   B  1  198  ? -5.533  24.803  122.288 1.00 29.51 ? 196  VAL   B O     1 
ATOM   10401 C  CB    . VAL   B  1  198  ? -2.658  24.701  120.674 1.00 26.02 ? 196  VAL   B CB    1 
ATOM   10402 C  CG1   . VAL   B  1  198  ? -1.874  25.173  119.483 1.00 29.56 ? 196  VAL   B CG1   1 
ATOM   10403 C  CG2   . VAL   B  1  198  ? -2.482  25.648  121.854 1.00 30.38 ? 196  VAL   B CG2   1 
ATOM   10404 N  N     . THR   B  1  199  ? -4.876  22.728  121.715 1.00 26.28 ? 197  THR   B N     1 
ATOM   10405 C  CA    A THR   B  1  199  ? -5.415  22.133  122.927 0.64 27.15 ? 197  THR   B CA    1 
ATOM   10406 C  CA    B THR   B  1  199  ? -5.423  22.152  122.933 0.36 27.16 ? 197  THR   B CA    1 
ATOM   10407 C  C     . THR   B  1  199  ? -4.488  22.334  124.117 1.00 29.11 ? 197  THR   B C     1 
ATOM   10408 O  O     . THR   B  1  199  ? -4.944  22.308  125.259 1.00 30.67 ? 197  THR   B O     1 
ATOM   10409 C  CB    A THR   B  1  199  ? -5.697  20.650  122.679 0.64 27.34 ? 197  THR   B CB    1 
ATOM   10410 C  CB    B THR   B  1  199  ? -5.736  20.669  122.731 0.36 27.33 ? 197  THR   B CB    1 
ATOM   10411 O  OG1   A THR   B  1  199  ? -6.459  20.521  121.469 0.64 26.94 ? 197  THR   B OG1   1 
ATOM   10412 O  OG1   B THR   B  1  199  ? -6.246  20.115  123.949 0.36 30.99 ? 197  THR   B OG1   1 
ATOM   10413 C  CG2   A THR   B  1  199  ? -6.494  20.047  123.820 0.64 30.92 ? 197  THR   B CG2   1 
ATOM   10414 C  CG2   B THR   B  1  199  ? -4.490  19.929  122.331 0.36 24.06 ? 197  THR   B CG2   1 
ATOM   10415 N  N     . GLY   B  1  200  ? -3.208  22.545  123.868 1.00 25.76 ? 198  GLY   B N     1 
ATOM   10416 C  CA    . GLY   B  1  200  ? -2.266  22.821  124.927 1.00 25.57 ? 198  GLY   B CA    1 
ATOM   10417 C  C     . GLY   B  1  200  ? -0.933  23.152  124.298 1.00 26.28 ? 198  GLY   B C     1 
ATOM   10418 O  O     . GLY   B  1  200  ? -0.699  22.876  123.115 1.00 25.00 ? 198  GLY   B O     1 
ATOM   10419 N  N     . GLU   B  1  201  ? -0.066  23.762  125.110 1.00 28.85 ? 199  GLU   B N     1 
ATOM   10420 C  CA    . GLU   B  1  201  ? 1.282   24.081  124.649 1.00 30.23 ? 199  GLU   B CA    1 
ATOM   10421 C  C     . GLU   B  1  201  ? 2.183   22.855  124.632 1.00 28.57 ? 199  GLU   B C     1 
ATOM   10422 O  O     . GLU   B  1  201  ? 3.104   22.781  123.812 1.00 35.81 ? 199  GLU   B O     1 
ATOM   10423 C  CB    . GLU   B  1  201  ? 1.904   25.180  125.516 1.00 34.43 ? 199  GLU   B CB    1 
ATOM   10424 N  N     . THR   B  1  202  ? 1.949   21.901  125.527 1.00 24.70 ? 200  THR   B N     1 
ATOM   10425 C  CA    . THR   B  1  202  ? 2.707   20.663  125.593 1.00 25.22 ? 200  THR   B CA    1 
ATOM   10426 C  C     . THR   B  1  202  ? 1.735   19.495  125.543 1.00 26.48 ? 200  THR   B C     1 
ATOM   10427 O  O     . THR   B  1  202  ? 0.537   19.654  125.801 1.00 24.28 ? 200  THR   B O     1 
ATOM   10428 C  CB    . THR   B  1  202  ? 3.473   20.546  126.908 1.00 28.34 ? 200  THR   B CB    1 
ATOM   10429 O  OG1   . THR   B  1  202  ? 2.540   20.446  127.989 1.00 28.79 ? 200  THR   B OG1   1 
ATOM   10430 C  CG2   . THR   B  1  202  ? 4.357   21.759  127.125 1.00 34.74 ? 200  THR   B CG2   1 
ATOM   10431 N  N     . ILE   B  1  203  ? 2.269   18.313  125.227 1.00 22.86 ? 201  ILE   B N     1 
ATOM   10432 C  CA    . ILE   B  1  203  ? 1.415   17.132  125.156 1.00 22.08 ? 201  ILE   B CA    1 
ATOM   10433 C  C     . ILE   B  1  203  ? 0.840   16.824  126.528 1.00 26.07 ? 201  ILE   B C     1 
ATOM   10434 O  O     . ILE   B  1  203  ? -0.324  16.426  126.648 1.00 24.06 ? 201  ILE   B O     1 
ATOM   10435 C  CB    . ILE   B  1  203  ? 2.136   15.930  124.507 1.00 22.58 ? 201  ILE   B CB    1 
ATOM   10436 C  CG1   . ILE   B  1  203  ? 1.145   14.793  124.228 1.00 23.02 ? 201  ILE   B CG1   1 
ATOM   10437 C  CG2   . ILE   B  1  203  ? 3.270   15.411  125.400 1.00 24.91 ? 201  ILE   B CG2   1 
ATOM   10438 C  CD1   . ILE   B  1  203  ? 0.029   15.169  123.243 1.00 23.00 ? 201  ILE   B CD1   1 
ATOM   10439 N  N     . ARG   B  1  204  ? 1.624   17.060  127.584 1.00 25.35 ? 202  ARG   B N     1 
ATOM   10440 C  CA    . ARG   B  1  204  ? 1.153   16.900  128.957 1.00 27.80 ? 202  ARG   B CA    1 
ATOM   10441 C  C     . ARG   B  1  204  ? -0.109  17.712  129.201 1.00 22.73 ? 202  ARG   B C     1 
ATOM   10442 O  O     . ARG   B  1  204  ? -1.102  17.200  129.742 1.00 27.40 ? 202  ARG   B O     1 
ATOM   10443 C  CB    . ARG   B  1  204  ? 2.256   17.387  129.902 1.00 33.17 ? 202  ARG   B CB    1 
ATOM   10444 C  CG    . ARG   B  1  204  ? 2.495   16.529  131.096 1.00 46.07 ? 202  ARG   B CG    1 
ATOM   10445 C  CD    . ARG   B  1  204  ? 3.797   16.930  131.785 1.00 33.79 ? 202  ARG   B CD    1 
ATOM   10446 N  NE    . ARG   B  1  204  ? 3.854   18.348  132.136 1.00 31.79 ? 202  ARG   B NE    1 
ATOM   10447 C  CZ    . ARG   B  1  204  ? 3.176   18.903  133.131 1.00 36.25 ? 202  ARG   B CZ    1 
ATOM   10448 N  NH1   . ARG   B  1  204  ? 2.313   18.206  133.855 1.00 35.64 ? 202  ARG   B NH1   1 
ATOM   10449 N  NH2   . ARG   B  1  204  ? 3.380   20.187  133.421 1.00 34.44 ? 202  ARG   B NH2   1 
ATOM   10450 N  N     . GLU   B  1  205  ? -0.070  18.999  128.846 1.00 25.94 ? 203  GLU   B N     1 
ATOM   10451 C  CA    . GLU   B  1  205  ? -1.204  19.884  129.072 1.00 26.19 ? 203  GLU   B CA    1 
ATOM   10452 C  C     . GLU   B  1  205  ? -2.380  19.480  128.201 1.00 25.62 ? 203  GLU   B C     1 
ATOM   10453 O  O     . GLU   B  1  205  ? -3.528  19.465  128.662 1.00 26.43 ? 203  GLU   B O     1 
ATOM   10454 C  CB    . GLU   B  1  205  ? -0.797  21.323  128.759 1.00 29.72 ? 203  GLU   B CB    1 
ATOM   10455 C  CG    . GLU   B  1  205  ? -1.897  22.345  128.974 1.00 29.10 ? 203  GLU   B CG    1 
ATOM   10456 C  CD    . GLU   B  1  205  ? -1.428  23.777  128.767 1.00 40.85 ? 203  GLU   B CD    1 
ATOM   10457 O  OE1   . GLU   B  1  205  ? -0.902  24.087  127.680 1.00 39.24 ? 203  GLU   B OE1   1 
ATOM   10458 O  OE2   . GLU   B  1  205  ? -1.579  24.596  129.699 1.00 57.54 ? 203  GLU   B OE2   1 
ATOM   10459 N  N     . ALA   B  1  206  ? -2.104  19.138  126.949 1.00 23.16 ? 204  ALA   B N     1 
ATOM   10460 C  CA    . ALA   B  1  206  ? -3.158  18.733  126.030 1.00 20.93 ? 204  ALA   B CA    1 
ATOM   10461 C  C     . ALA   B  1  206  ? -3.873  17.496  126.547 1.00 24.12 ? 204  ALA   B C     1 
ATOM   10462 O  O     . ALA   B  1  206  ? -5.108  17.434  126.544 1.00 23.29 ? 204  ALA   B O     1 
ATOM   10463 C  CB    . ALA   B  1  206  ? -2.543  18.458  124.665 1.00 22.67 ? 204  ALA   B CB    1 
ATOM   10464 N  N     . LEU   B  1  207  ? -3.106  16.499  127.003 1.00 21.36 ? 205  LEU   B N     1 
ATOM   10465 C  CA    . LEU   B  1  207  ? -3.701  15.285  127.552 1.00 24.39 ? 205  LEU   B CA    1 
ATOM   10466 C  C     . LEU   B  1  207  ? -4.549  15.589  128.777 1.00 27.36 ? 205  LEU   B C     1 
ATOM   10467 O  O     . LEU   B  1  207  ? -5.640  15.027  128.943 1.00 25.71 ? 205  LEU   B O     1 
ATOM   10468 C  CB    . LEU   B  1  207  ? -2.609  14.264  127.884 1.00 26.65 ? 205  LEU   B CB    1 
ATOM   10469 C  CG    . LEU   B  1  207  ? -1.979  13.616  126.648 1.00 28.24 ? 205  LEU   B CG    1 
ATOM   10470 C  CD1   . LEU   B  1  207  ? -0.673  12.920  127.014 1.00 29.97 ? 205  LEU   B CD1   1 
ATOM   10471 C  CD2   . LEU   B  1  207  ? -2.942  12.635  126.002 1.00 24.77 ? 205  LEU   B CD2   1 
ATOM   10472 N  N     . LYS   B  1  208  ? -4.064  16.467  129.659 1.00 22.41 ? 206  LYS   B N     1 
ATOM   10473 C  CA    . LYS   B  1  208  ? -4.847  16.817  130.839 1.00 25.09 ? 206  LYS   B CA    1 
ATOM   10474 C  C     . LYS   B  1  208  ? -6.154  17.502  130.449 1.00 25.98 ? 206  LYS   B C     1 
ATOM   10475 O  O     . LYS   B  1  208  ? -7.212  17.219  131.022 1.00 27.47 ? 206  LYS   B O     1 
ATOM   10476 C  CB    . LYS   B  1  208  ? -4.015  17.700  131.778 1.00 27.87 ? 206  LYS   B CB    1 
ATOM   10477 N  N     . ARG   B  1  209  ? -6.107  18.384  129.456 1.00 27.03 ? 207  ARG   B N     1 
ATOM   10478 C  CA    . ARG   B  1  209  ? -7.301  19.100  129.033 1.00 26.25 ? 207  ARG   B CA    1 
ATOM   10479 C  C     . ARG   B  1  209  ? -8.270  18.228  128.254 1.00 30.84 ? 207  ARG   B C     1 
ATOM   10480 O  O     . ARG   B  1  209  ? -9.426  18.627  128.070 1.00 30.15 ? 207  ARG   B O     1 
ATOM   10481 C  CB    . ARG   B  1  209  ? -6.914  20.312  128.197 1.00 28.29 ? 207  ARG   B CB    1 
ATOM   10482 C  CG    . ARG   B  1  209  ? -6.203  21.379  129.016 1.00 28.03 ? 207  ARG   B CG    1 
ATOM   10483 C  CD    . ARG   B  1  209  ? -5.854  22.546  128.137 1.00 30.77 ? 207  ARG   B CD    1 
ATOM   10484 N  NE    . ARG   B  1  209  ? -5.234  23.646  128.861 1.00 41.71 ? 207  ARG   B NE    1 
ATOM   10485 C  CZ    . ARG   B  1  209  ? -4.756  24.736  128.277 1.00 44.79 ? 207  ARG   B CZ    1 
ATOM   10486 N  NH1   . ARG   B  1  209  ? -4.789  24.885  126.963 1.00 33.54 ? 207  ARG   B NH1   1 
ATOM   10487 N  NH2   . ARG   B  1  209  ? -4.236  25.702  129.031 1.00 49.70 ? 207  ARG   B NH2   1 
ATOM   10488 N  N     . SER   B  1  210  ? -7.841  17.046  127.823 1.00 24.38 ? 208  SER   B N     1 
ATOM   10489 C  CA    . SER   B  1  210  ? -8.694  16.197  127.007 1.00 24.80 ? 208  SER   B CA    1 
ATOM   10490 C  C     . SER   B  1  210  ? -9.677  15.394  127.840 1.00 24.84 ? 208  SER   B C     1 
ATOM   10491 O  O     . SER   B  1  210  ? -10.663 14.890  127.296 1.00 26.99 ? 208  SER   B O     1 
ATOM   10492 C  CB    . SER   B  1  210  ? -7.816  15.269  126.175 1.00 21.59 ? 208  SER   B CB    1 
ATOM   10493 O  OG    . SER   B  1  210  ? -7.015  16.034  125.275 1.00 28.84 ? 208  SER   B OG    1 
ATOM   10494 N  N     . LYS   B  1  211  ? -9.449  15.283  129.149 1.00 25.06 ? 209  LYS   B N     1 
ATOM   10495 C  CA    . LYS   B  1  211  ? -10.279 14.405  129.964 1.00 24.56 ? 209  LYS   B CA    1 
ATOM   10496 C  C     . LYS   B  1  211  ? -11.740 14.841  129.946 1.00 25.99 ? 209  LYS   B C     1 
ATOM   10497 O  O     . LYS   B  1  211  ? -12.641 13.998  129.946 1.00 29.76 ? 209  LYS   B O     1 
ATOM   10498 C  CB    . LYS   B  1  211  ? -9.754  14.368  131.396 1.00 28.24 ? 209  LYS   B CB    1 
ATOM   10499 C  CG    . LYS   B  1  211  ? -8.258  14.134  131.498 1.00 33.57 ? 209  LYS   B CG    1 
ATOM   10500 C  CD    . LYS   B  1  211  ? -7.804  12.886  130.742 1.00 35.01 ? 209  LYS   B CD    1 
ATOM   10501 C  CE    . LYS   B  1  211  ? -6.337  12.590  131.035 1.00 44.61 ? 209  LYS   B CE    1 
ATOM   10502 N  NZ    . LYS   B  1  211  ? -5.758  11.473  130.225 1.00 42.95 ? 209  LYS   B NZ    1 
ATOM   10503 N  N     . GLU   B  1  212  ? -11.991 16.154  129.910 1.00 27.20 ? 210  GLU   B N     1 
ATOM   10504 C  CA    . GLU   B  1  212  ? -13.359 16.655  130.025 1.00 32.53 ? 210  GLU   B CA    1 
ATOM   10505 C  C     . GLU   B  1  212  ? -14.241 16.127  128.898 1.00 27.36 ? 210  GLU   B C     1 
ATOM   10506 O  O     . GLU   B  1  212  ? -15.332 15.599  129.146 1.00 27.29 ? 210  GLU   B O     1 
ATOM   10507 C  CB    . GLU   B  1  212  ? -13.357 18.183  130.024 1.00 37.07 ? 210  GLU   B CB    1 
ATOM   10508 C  CG    . GLU   B  1  212  ? -14.747 18.791  130.090 1.00 45.60 ? 210  GLU   B CG    1 
ATOM   10509 C  CD    . GLU   B  1  212  ? -14.769 20.251  129.678 1.00 53.78 ? 210  GLU   B CD    1 
ATOM   10510 O  OE1   . GLU   B  1  212  ? -13.719 20.920  129.792 1.00 61.89 ? 210  GLU   B OE1   1 
ATOM   10511 O  OE2   . GLU   B  1  212  ? -15.835 20.727  129.227 1.00 57.71 ? 210  GLU   B OE2   1 
ATOM   10512 N  N     . LEU   B  1  213  ? -13.783 16.259  127.652 1.00 25.92 ? 211  LEU   B N     1 
ATOM   10513 C  CA    . LEU   B  1  213  ? -14.573 15.788  126.515 1.00 25.88 ? 211  LEU   B CA    1 
ATOM   10514 C  C     . LEU   B  1  213  ? -14.479 14.278  126.326 1.00 25.48 ? 211  LEU   B C     1 
ATOM   10515 O  O     . LEU   B  1  213  ? -15.428 13.665  125.824 1.00 25.76 ? 211  LEU   B O     1 
ATOM   10516 C  CB    . LEU   B  1  213  ? -14.232 16.558  125.234 1.00 25.42 ? 211  LEU   B CB    1 
ATOM   10517 C  CG    . LEU   B  1  213  ? -14.662 18.031  125.255 1.00 27.95 ? 211  LEU   B CG    1 
ATOM   10518 C  CD1   . LEU   B  1  213  ? -14.418 18.732  123.923 1.00 28.48 ? 211  LEU   B CD1   1 
ATOM   10519 C  CD2   . LEU   B  1  213  ? -16.128 18.157  125.660 1.00 31.97 ? 211  LEU   B CD2   1 
ATOM   10520 N  N     . GLU   B  1  214  ? -13.369 13.654  126.731 1.00 24.20 ? 212  GLU   B N     1 
ATOM   10521 C  CA    . GLU   B  1  214  ? -13.302 12.197  126.679 1.00 22.56 ? 212  GLU   B CA    1 
ATOM   10522 C  C     . GLU   B  1  214  ? -14.375 11.570  127.556 1.00 26.32 ? 212  GLU   B C     1 
ATOM   10523 O  O     . GLU   B  1  214  ? -15.034 10.605  127.147 1.00 28.12 ? 212  GLU   B O     1 
ATOM   10524 C  CB    . GLU   B  1  214  ? -11.911 11.699  127.066 1.00 24.40 ? 212  GLU   B CB    1 
ATOM   10525 C  CG    . GLU   B  1  214  ? -10.912 11.944  125.966 1.00 23.09 ? 212  GLU   B CG    1 
ATOM   10526 C  CD    . GLU   B  1  214  ? -9.560  11.350  126.246 1.00 26.44 ? 212  GLU   B CD    1 
ATOM   10527 O  OE1   . GLU   B  1  214  ? -9.254  11.079  127.422 1.00 28.67 ? 212  GLU   B OE1   1 
ATOM   10528 O  OE2   . GLU   B  1  214  ? -8.795  11.171  125.272 1.00 25.96 ? 212  GLU   B OE2   1 
ATOM   10529 N  N     . GLU   B  1  215  ? -14.592 12.128  128.753 1.00 26.74 ? 213  GLU   B N     1 
ATOM   10530 C  CA    . GLU   B  1  215  ? -15.658 11.643  129.621 1.00 26.13 ? 213  GLU   B CA    1 
ATOM   10531 C  C     . GLU   B  1  215  ? -17.035 11.764  128.980 1.00 29.39 ? 213  GLU   B C     1 
ATOM   10532 O  O     . GLU   B  1  215  ? -17.947 11.026  129.368 1.00 32.43 ? 213  GLU   B O     1 
ATOM   10533 C  CB    . GLU   B  1  215  ? -15.633 12.376  130.966 1.00 29.12 ? 213  GLU   B CB    1 
ATOM   10534 C  CG    . GLU   B  1  215  ? -14.428 12.028  131.820 1.00 35.10 ? 213  GLU   B CG    1 
ATOM   10535 C  CD    . GLU   B  1  215  ? -14.439 12.728  133.162 1.00 44.38 ? 213  GLU   B CD    1 
ATOM   10536 O  OE1   . GLU   B  1  215  ? -15.504 12.749  133.817 1.00 55.45 ? 213  GLU   B OE1   1 
ATOM   10537 O  OE2   . GLU   B  1  215  ? -13.378 13.257  133.557 1.00 51.98 ? 213  GLU   B OE2   1 
ATOM   10538 N  N     . LYS   B  1  216  ? -17.209 12.676  128.022 1.00 26.99 ? 214  LYS   B N     1 
ATOM   10539 C  CA    . LYS   B  1  216  ? -18.478 12.820  127.322 1.00 27.29 ? 214  LYS   B CA    1 
ATOM   10540 C  C     . LYS   B  1  216  ? -18.593 11.900  126.115 1.00 31.84 ? 214  LYS   B C     1 
ATOM   10541 O  O     . LYS   B  1  216  ? -19.691 11.757  125.562 1.00 31.07 ? 214  LYS   B O     1 
ATOM   10542 C  CB    . LYS   B  1  216  ? -18.700 14.276  126.893 1.00 28.81 ? 214  LYS   B CB    1 
ATOM   10543 N  N     . GLY   B  1  217  ? -17.504 11.256  125.708 1.00 25.75 ? 215  GLY   B N     1 
ATOM   10544 C  CA    . GLY   B  1  217  ? -17.530 10.344  124.585 1.00 24.64 ? 215  GLY   B CA    1 
ATOM   10545 C  C     . GLY   B  1  217  ? -16.728 10.812  123.391 1.00 26.84 ? 215  GLY   B C     1 
ATOM   10546 O  O     . GLY   B  1  217  ? -16.766 10.155  122.343 1.00 26.37 ? 215  GLY   B O     1 
ATOM   10547 N  N     . PHE   B  1  218  ? -16.042 11.945  123.491 1.00 23.71 ? 216  PHE   B N     1 
ATOM   10548 C  CA    . PHE   B  1  218  ? -15.106 12.321  122.448 1.00 21.49 ? 216  PHE   B CA    1 
ATOM   10549 C  C     . PHE   B  1  218  ? -13.822 11.527  122.609 1.00 21.65 ? 216  PHE   B C     1 
ATOM   10550 O  O     . PHE   B  1  218  ? -13.517 10.996  123.677 1.00 22.77 ? 216  PHE   B O     1 
ATOM   10551 C  CB    . PHE   B  1  218  ? -14.762 13.809  122.529 1.00 22.29 ? 216  PHE   B CB    1 
ATOM   10552 C  CG    . PHE   B  1  218  ? -15.890 14.720  122.139 1.00 23.02 ? 216  PHE   B CG    1 
ATOM   10553 C  CD1   . PHE   B  1  218  ? -16.891 15.039  123.045 1.00 24.55 ? 216  PHE   B CD1   1 
ATOM   10554 C  CD2   . PHE   B  1  218  ? -15.937 15.274  120.877 1.00 24.43 ? 216  PHE   B CD2   1 
ATOM   10555 C  CE1   . PHE   B  1  218  ? -17.918 15.891  122.681 1.00 27.32 ? 216  PHE   B CE1   1 
ATOM   10556 C  CE2   . PHE   B  1  218  ? -16.959 16.122  120.514 1.00 26.76 ? 216  PHE   B CE2   1 
ATOM   10557 C  CZ    . PHE   B  1  218  ? -17.946 16.432  121.417 1.00 25.70 ? 216  PHE   B CZ    1 
ATOM   10558 N  N     . SER   B  1  219  ? -13.068 11.451  121.520 1.00 21.42 ? 217  SER   B N     1 
ATOM   10559 C  CA    . SER   B  1  219  ? -11.699 10.963  121.550 1.00 22.32 ? 217  SER   B CA    1 
ATOM   10560 C  C     . SER   B  1  219  ? -10.810 12.026  120.931 1.00 21.59 ? 217  SER   B C     1 
ATOM   10561 O  O     . SER   B  1  219  ? -11.280 13.082  120.495 1.00 19.04 ? 217  SER   B O     1 
ATOM   10562 C  CB    . SER   B  1  219  ? -11.566 9.629   120.814 1.00 21.42 ? 217  SER   B CB    1 
ATOM   10563 O  OG    . SER   B  1  219  ? -11.976 9.780   119.469 1.00 25.48 ? 217  SER   B OG    1 
ATOM   10564 N  N     . TYR   B  1  220  ? -9.507  11.750  120.881 1.00 20.73 ? 218  TYR   B N     1 
ATOM   10565 C  CA    . TYR   B  1  220  ? -8.557  12.746  120.415 1.00 18.80 ? 218  TYR   B CA    1 
ATOM   10566 C  C     . TYR   B  1  220  ? -7.535  12.147  119.466 1.00 18.16 ? 218  TYR   B C     1 
ATOM   10567 O  O     . TYR   B  1  220  ? -7.185  10.970  119.557 1.00 20.34 ? 218  TYR   B O     1 
ATOM   10568 C  CB    . TYR   B  1  220  ? -7.805  13.364  121.601 1.00 19.15 ? 218  TYR   B CB    1 
ATOM   10569 C  CG    . TYR   B  1  220  ? -8.598  14.447  122.279 1.00 19.09 ? 218  TYR   B CG    1 
ATOM   10570 C  CD1   . TYR   B  1  220  ? -9.561  14.141  123.229 1.00 21.22 ? 218  TYR   B CD1   1 
ATOM   10571 C  CD2   . TYR   B  1  220  ? -8.420  15.772  121.919 1.00 19.08 ? 218  TYR   B CD2   1 
ATOM   10572 C  CE1   . TYR   B  1  220  ? -10.302 15.135  123.826 1.00 21.26 ? 218  TYR   B CE1   1 
ATOM   10573 C  CE2   . TYR   B  1  220  ? -9.148  16.774  122.517 1.00 21.78 ? 218  TYR   B CE2   1 
ATOM   10574 C  CZ    . TYR   B  1  220  ? -10.096 16.441  123.459 1.00 19.47 ? 218  TYR   B CZ    1 
ATOM   10575 O  OH    . TYR   B  1  220  ? -10.825 17.436  124.058 1.00 24.93 ? 218  TYR   B OH    1 
ATOM   10576 N  N     . SER   B  1  221  ? -7.031  13.002  118.586 1.00 17.40 ? 219  SER   B N     1 
ATOM   10577 C  CA    . SER   B  1  221  ? -5.857  12.719  117.774 1.00 17.58 ? 219  SER   B CA    1 
ATOM   10578 C  C     . SER   B  1  221  ? -4.973  13.949  117.849 1.00 18.52 ? 219  SER   B C     1 
ATOM   10579 O  O     . SER   B  1  221  ? -5.390  15.033  117.439 1.00 20.17 ? 219  SER   B O     1 
ATOM   10580 C  CB    . SER   B  1  221  ? -6.255  12.453  116.325 1.00 18.29 ? 219  SER   B CB    1 
ATOM   10581 O  OG    . SER   B  1  221  ? -5.104  12.193  115.538 1.00 19.45 ? 219  SER   B OG    1 
ATOM   10582 N  N     . TYR   B  1  222  ? -3.767  13.789  118.388 1.00 17.93 ? 220  TYR   B N     1 
ATOM   10583 C  CA    . TYR   B  1  222  ? -2.899  14.933  118.639 1.00 18.03 ? 220  TYR   B CA    1 
ATOM   10584 C  C     . TYR   B  1  222  ? -1.977  15.243  117.475 1.00 19.42 ? 220  TYR   B C     1 
ATOM   10585 O  O     . TYR   B  1  222  ? -1.403  14.348  116.853 1.00 20.10 ? 220  TYR   B O     1 
ATOM   10586 C  CB    . TYR   B  1  222  ? -2.074  14.705  119.899 1.00 17.68 ? 220  TYR   B CB    1 
ATOM   10587 C  CG    . TYR   B  1  222  ? -2.993  14.586  121.078 1.00 16.10 ? 220  TYR   B CG    1 
ATOM   10588 C  CD1   . TYR   B  1  222  ? -3.578  15.717  121.622 1.00 18.97 ? 220  TYR   B CD1   1 
ATOM   10589 C  CD2   . TYR   B  1  222  ? -3.321  13.350  121.615 1.00 18.79 ? 220  TYR   B CD2   1 
ATOM   10590 C  CE1   . TYR   B  1  222  ? -4.446  15.628  122.685 1.00 18.51 ? 220  TYR   B CE1   1 
ATOM   10591 C  CE2   . TYR   B  1  222  ? -4.180  13.249  122.686 1.00 18.11 ? 220  TYR   B CE2   1 
ATOM   10592 C  CZ    . TYR   B  1  222  ? -4.736  14.392  123.219 1.00 18.06 ? 220  TYR   B CZ    1 
ATOM   10593 O  OH    . TYR   B  1  222  ? -5.626  14.293  124.258 1.00 20.08 ? 220  TYR   B OH    1 
ATOM   10594 N  N     . ASP   B  1  223  ? -1.838  16.532  117.195 1.00 19.22 ? 221  ASP   B N     1 
ATOM   10595 C  CA    . ASP   B  1  223  ? -1.014  17.041  116.106 1.00 21.34 ? 221  ASP   B CA    1 
ATOM   10596 C  C     . ASP   B  1  223  ? 0.079   17.895  116.731 1.00 20.71 ? 221  ASP   B C     1 
ATOM   10597 O  O     . ASP   B  1  223  ? -0.200  18.987  117.237 1.00 23.12 ? 221  ASP   B O     1 
ATOM   10598 C  CB    . ASP   B  1  223  ? -1.890  17.879  115.188 1.00 22.03 ? 221  ASP   B CB    1 
ATOM   10599 C  CG    . ASP   B  1  223  ? -1.090  18.749  114.232 1.00 27.16 ? 221  ASP   B CG    1 
ATOM   10600 O  OD1   . ASP   B  1  223  ? 0.056   18.393  113.898 1.00 25.61 ? 221  ASP   B OD1   1 
ATOM   10601 O  OD2   . ASP   B  1  223  ? -1.622  19.804  113.834 1.00 29.27 ? 221  ASP   B OD2   1 
ATOM   10602 N  N     . MET   B  1  224  ? 1.320   17.406  116.694 1.00 19.61 ? 222  MET   B N     1 
ATOM   10603 C  CA    . MET   B  1  224  ? 2.450   18.116  117.277 1.00 23.92 ? 222  MET   B CA    1 
ATOM   10604 C  C     . MET   B  1  224  ? 2.983   19.223  116.380 1.00 25.24 ? 222  MET   B C     1 
ATOM   10605 O  O     . MET   B  1  224  ? 4.043   19.788  116.678 1.00 27.35 ? 222  MET   B O     1 
ATOM   10606 C  CB    . MET   B  1  224  ? 3.573   17.141  117.653 1.00 24.56 ? 222  MET   B CB    1 
ATOM   10607 C  CG    . MET   B  1  224  ? 3.151   16.050  118.620 1.00 21.33 ? 222  MET   B CG    1 
ATOM   10608 S  SD    . MET   B  1  224  ? 2.293   16.695  120.076 1.00 26.58 ? 222  MET   B SD    1 
ATOM   10609 C  CE    . MET   B  1  224  ? 3.581   17.731  120.752 1.00 27.61 ? 222  MET   B CE    1 
ATOM   10610 N  N     . LEU   B  1  225  ? 2.286   19.517  115.295 1.00 28.09 ? 223  LEU   B N     1 
ATOM   10611 C  CA    . LEU   B  1  225  ? 2.477   20.675  114.428 1.00 26.68 ? 223  LEU   B CA    1 
ATOM   10612 C  C     . LEU   B  1  225  ? 3.650   20.547  113.454 1.00 31.75 ? 223  LEU   B C     1 
ATOM   10613 O  O     . LEU   B  1  225  ? 3.857   21.471  112.664 1.00 32.96 ? 223  LEU   B O     1 
ATOM   10614 C  CB    . LEU   B  1  225  ? 2.551   22.009  115.187 1.00 31.23 ? 223  LEU   B CB    1 
ATOM   10615 C  CG    . LEU   B  1  225  ? 1.379   22.315  116.123 1.00 35.90 ? 223  LEU   B CG    1 
ATOM   10616 C  CD1   . LEU   B  1  225  ? 1.632   23.601  116.882 1.00 39.82 ? 223  LEU   B CD1   1 
ATOM   10617 C  CD2   . LEU   B  1  225  ? 0.073   22.395  115.364 1.00 31.43 ? 223  LEU   B CD2   1 
ATOM   10618 N  N     . GLY   B  1  226  ? 4.403   19.450  113.462 1.00 28.38 ? 224  GLY   B N     1 
ATOM   10619 C  CA    . GLY   B  1  226  ? 5.495   19.316  112.506 1.00 27.58 ? 224  GLY   B CA    1 
ATOM   10620 C  C     . GLY   B  1  226  ? 4.979   19.247  111.077 1.00 23.57 ? 224  GLY   B C     1 
ATOM   10621 O  O     . GLY   B  1  226  ? 3.978   18.588  110.785 1.00 24.89 ? 224  GLY   B O     1 
ATOM   10622 N  N     . GLU   B  1  227  ? 5.682   19.928  110.173 1.00 23.56 ? 225  GLU   B N     1 
ATOM   10623 C  CA    . GLU   B  1  227  ? 5.268   19.931  108.780 1.00 21.93 ? 225  GLU   B CA    1 
ATOM   10624 C  C     . GLU   B  1  227  ? 6.388   20.529  107.947 1.00 20.05 ? 225  GLU   B C     1 
ATOM   10625 O  O     . GLU   B  1  227  ? 7.074   21.445  108.400 1.00 21.75 ? 225  GLU   B O     1 
ATOM   10626 C  CB    . GLU   B  1  227  ? 3.996   20.778  108.636 1.00 23.57 ? 225  GLU   B CB    1 
ATOM   10627 C  CG    . GLU   B  1  227  ? 3.415   20.823  107.268 1.00 26.54 ? 225  GLU   B CG    1 
ATOM   10628 C  CD    . GLU   B  1  227  ? 2.077   21.541  107.244 1.00 28.89 ? 225  GLU   B CD    1 
ATOM   10629 O  OE1   . GLU   B  1  227  ? 1.519   21.849  108.325 1.00 27.77 ? 225  GLU   B OE1   1 
ATOM   10630 O  OE2   . GLU   B  1  227  ? 1.588   21.802  106.134 1.00 31.43 ? 225  GLU   B OE2   1 
ATOM   10631 N  N     . ALA   B  1  228  ? 6.559   20.015  106.731 1.00 18.46 ? 226  ALA   B N     1 
ATOM   10632 C  CA    . ALA   B  1  228  ? 7.409   20.660  105.733 1.00 20.06 ? 226  ALA   B CA    1 
ATOM   10633 C  C     . ALA   B  1  228  ? 8.801   20.958  106.284 1.00 18.92 ? 226  ALA   B C     1 
ATOM   10634 O  O     . ALA   B  1  228  ? 9.266   22.102  106.293 1.00 20.70 ? 226  ALA   B O     1 
ATOM   10635 C  CB    . ALA   B  1  228  ? 6.748   21.934  105.209 1.00 21.10 ? 226  ALA   B CB    1 
ATOM   10636 N  N     . ALA   B  1  229  ? 9.462   19.907  106.772 1.00 16.83 ? 227  ALA   B N     1 
ATOM   10637 C  CA    . ALA   B  1  229  ? 10.861  20.039  107.153 1.00 16.89 ? 227  ALA   B CA    1 
ATOM   10638 C  C     . ALA   B  1  229  ? 11.654  20.652  106.004 1.00 15.51 ? 227  ALA   B C     1 
ATOM   10639 O  O     . ALA   B  1  229  ? 11.491  20.261  104.847 1.00 17.58 ? 227  ALA   B O     1 
ATOM   10640 C  CB    . ALA   B  1  229  ? 11.416  18.658  107.483 1.00 17.32 ? 227  ALA   B CB    1 
ATOM   10641 N  N     . THR   B  1  230  ? 12.496  21.634  106.333 1.00 16.92 ? 228  THR   B N     1 
ATOM   10642 C  CA    . THR   B  1  230  ? 13.375  22.265  105.355 1.00 16.05 ? 228  THR   B CA    1 
ATOM   10643 C  C     . THR   B  1  230  ? 14.775  21.690  105.406 1.00 15.99 ? 228  THR   B C     1 
ATOM   10644 O  O     . THR   B  1  230  ? 15.462  21.644  104.379 1.00 17.32 ? 228  THR   B O     1 
ATOM   10645 C  CB    . THR   B  1  230  ? 13.443  23.772  105.638 1.00 17.85 ? 228  THR   B CB    1 
ATOM   10646 O  OG1   . THR   B  1  230  ? 12.107  24.283  105.723 1.00 21.49 ? 228  THR   B OG1   1 
ATOM   10647 C  CG2   . THR   B  1  230  ? 14.188  24.518  104.524 1.00 17.40 ? 228  THR   B CG2   1 
ATOM   10648 N  N     . THR   B  1  231  ? 15.199  21.233  106.576 1.00 15.66 ? 229  THR   B N     1 
ATOM   10649 C  CA    . THR   B  1  231  ? 16.542  20.722  106.776 1.00 15.92 ? 229  THR   B CA    1 
ATOM   10650 C  C     . THR   B  1  231  ? 16.460  19.360  107.449 1.00 15.44 ? 229  THR   B C     1 
ATOM   10651 O  O     . THR   B  1  231  ? 15.435  18.982  108.023 1.00 16.10 ? 229  THR   B O     1 
ATOM   10652 C  CB    . THR   B  1  231  ? 17.363  21.657  107.665 1.00 16.66 ? 229  THR   B CB    1 
ATOM   10653 O  OG1   . THR   B  1  231  ? 16.862  21.569  109.005 1.00 17.14 ? 229  THR   B OG1   1 
ATOM   10654 C  CG2   . THR   B  1  231  ? 17.269  23.099  107.173 1.00 17.79 ? 229  THR   B CG2   1 
ATOM   10655 N  N     . ALA   B  1  232  ? 17.586  18.650  107.416 1.00 16.37 ? 230  ALA   B N     1 
ATOM   10656 C  CA    . ALA   B  1  232  ? 17.674  17.391  108.145 1.00 16.96 ? 230  ALA   B CA    1 
ATOM   10657 C  C     . ALA   B  1  232  ? 17.406  17.597  109.625 1.00 16.49 ? 230  ALA   B C     1 
ATOM   10658 O  O     . ALA   B  1  232  ? 16.740  16.772  110.261 1.00 18.24 ? 230  ALA   B O     1 
ATOM   10659 C  CB    . ALA   B  1  232  ? 19.052  16.767  107.939 1.00 18.69 ? 230  ALA   B CB    1 
ATOM   10660 N  N     . ALA   B  1  233  ? 17.912  18.692  110.196 1.00 17.57 ? 231  ALA   B N     1 
ATOM   10661 C  CA    . ALA   B  1  233  ? 17.687  18.950  111.614 1.00 18.17 ? 231  ALA   B CA    1 
ATOM   10662 C  C     . ALA   B  1  233  ? 16.209  19.154  111.912 1.00 18.10 ? 231  ALA   B C     1 
ATOM   10663 O  O     . ALA   B  1  233  ? 15.724  18.726  112.965 1.00 18.37 ? 231  ALA   B O     1 
ATOM   10664 C  CB    . ALA   B  1  233  ? 18.514  20.145  112.084 1.00 20.66 ? 231  ALA   B CB    1 
ATOM   10665 N  N     . ASP   B  1  234  ? 15.473  19.802  111.002 1.00 16.73 ? 232  ASP   B N     1 
ATOM   10666 C  CA    . ASP   B  1  234  ? 14.035  19.949  111.205 1.00 17.95 ? 232  ASP   B CA    1 
ATOM   10667 C  C     . ASP   B  1  234  ? 13.382  18.586  111.274 1.00 16.62 ? 232  ASP   B C     1 
ATOM   10668 O  O     . ASP   B  1  234  ? 12.594  18.302  112.185 1.00 16.57 ? 232  ASP   B O     1 
ATOM   10669 C  CB    . ASP   B  1  234  ? 13.384  20.667  110.025 1.00 19.01 ? 232  ASP   B CB    1 
ATOM   10670 C  CG    . ASP   B  1  234  ? 13.729  22.121  109.940 1.00 22.95 ? 232  ASP   B CG    1 
ATOM   10671 O  OD1   . ASP   B  1  234  ? 14.069  22.747  110.963 1.00 23.20 ? 232  ASP   B OD1   1 
ATOM   10672 O  OD2   . ASP   B  1  234  ? 13.616  22.645  108.813 1.00 22.19 ? 232  ASP   B OD2   1 
ATOM   10673 N  N     . ALA   B  1  235  ? 13.687  17.733  110.297 1.00 16.13 ? 233  ALA   B N     1 
ATOM   10674 C  CA    . ALA   B  1  235  ? 13.045  16.432  110.222 1.00 16.52 ? 233  ALA   B CA    1 
ATOM   10675 C  C     . ALA   B  1  235  ? 13.394  15.588  111.436 1.00 16.06 ? 233  ALA   B C     1 
ATOM   10676 O  O     . ALA   B  1  235  ? 12.539  14.868  111.968 1.00 17.55 ? 233  ALA   B O     1 
ATOM   10677 C  CB    . ALA   B  1  235  ? 13.437  15.722  108.927 1.00 16.62 ? 233  ALA   B CB    1 
ATOM   10678 N  N     . GLU   B  1  236  ? 14.643  15.670  111.895 1.00 16.41 ? 234  GLU   B N     1 
ATOM   10679 C  CA    . GLU   B  1  236  ? 15.036  14.891  113.059 1.00 18.31 ? 234  GLU   B CA    1 
ATOM   10680 C  C     . GLU   B  1  236  ? 14.299  15.377  114.295 1.00 18.66 ? 234  GLU   B C     1 
ATOM   10681 O  O     . GLU   B  1  236  ? 13.837  14.570  115.115 1.00 18.59 ? 234  GLU   B O     1 
ATOM   10682 C  CB    . GLU   B  1  236  ? 16.552  14.966  113.235 1.00 19.18 ? 234  GLU   B CB    1 
ATOM   10683 C  CG    . GLU   B  1  236  ? 17.083  14.007  114.275 1.00 24.06 ? 234  GLU   B CG    1 
ATOM   10684 C  CD    . GLU   B  1  236  ? 18.599  14.013  114.349 1.00 31.91 ? 234  GLU   B CD    1 
ATOM   10685 O  OE1   . GLU   B  1  236  ? 19.239  14.806  113.622 1.00 37.63 ? 234  GLU   B OE1   1 
ATOM   10686 O  OE2   . GLU   B  1  236  ? 19.144  13.214  115.136 1.00 34.54 ? 234  GLU   B OE2   1 
ATOM   10687 N  N     . ARG   B  1  237  ? 14.158  16.693  114.433 1.00 17.18 ? 235  ARG   B N     1 
ATOM   10688 C  CA    . ARG   B  1  237  ? 13.430  17.242  115.564 1.00 20.04 ? 235  ARG   B CA    1 
ATOM   10689 C  C     . ARG   B  1  237  ? 11.969  16.827  115.525 1.00 19.46 ? 235  ARG   B C     1 
ATOM   10690 O  O     . ARG   B  1  237  ? 11.404  16.414  116.543 1.00 18.94 ? 235  ARG   B O     1 
ATOM   10691 C  CB    . ARG   B  1  237  ? 13.553  18.763  115.575 1.00 21.92 ? 235  ARG   B CB    1 
ATOM   10692 C  CG    . ARG   B  1  237  ? 12.887  19.358  116.788 1.00 23.18 ? 235  ARG   B CG    1 
ATOM   10693 C  CD    . ARG   B  1  237  ? 12.741  20.843  116.704 1.00 26.99 ? 235  ARG   B CD    1 
ATOM   10694 N  NE    . ARG   B  1  237  ? 12.106  21.311  117.931 1.00 31.25 ? 235  ARG   B NE    1 
ATOM   10695 C  CZ    . ARG   B  1  237  ? 12.135  22.561  118.366 1.00 35.17 ? 235  ARG   B CZ    1 
ATOM   10696 N  NH1   . ARG   B  1  237  ? 12.771  23.509  117.697 1.00 39.13 ? 235  ARG   B NH1   1 
ATOM   10697 N  NH2   . ARG   B  1  237  ? 11.516  22.863  119.503 1.00 33.63 ? 235  ARG   B NH2   1 
ATOM   10698 N  N     . TYR   B  1  238  ? 11.332  16.939  114.358 1.00 17.80 ? 236  TYR   B N     1 
ATOM   10699 C  CA    . TYR   B  1  238  ? 9.923   16.567  114.271 1.00 17.00 ? 236  TYR   B CA    1 
ATOM   10700 C  C     . TYR   B  1  238  ? 9.737   15.090  114.582 1.00 16.39 ? 236  TYR   B C     1 
ATOM   10701 O  O     . TYR   B  1  238  ? 8.768   14.704  115.255 1.00 17.05 ? 236  TYR   B O     1 
ATOM   10702 C  CB    . TYR   B  1  238  ? 9.363   16.889  112.888 1.00 16.58 ? 236  TYR   B CB    1 
ATOM   10703 C  CG    . TYR   B  1  238  ? 9.249   18.362  112.578 1.00 20.15 ? 236  TYR   B CG    1 
ATOM   10704 C  CD1   . TYR   B  1  238  ? 8.983   19.300  113.565 1.00 22.88 ? 236  TYR   B CD1   1 
ATOM   10705 C  CD2   . TYR   B  1  238  ? 9.419   18.809  111.285 1.00 19.25 ? 236  TYR   B CD2   1 
ATOM   10706 C  CE1   . TYR   B  1  238  ? 8.884   20.658  113.253 1.00 27.55 ? 236  TYR   B CE1   1 
ATOM   10707 C  CE2   . TYR   B  1  238  ? 9.316   20.140  110.962 1.00 20.68 ? 236  TYR   B CE2   1 
ATOM   10708 C  CZ    . TYR   B  1  238  ? 9.054   21.064  111.939 1.00 28.63 ? 236  TYR   B CZ    1 
ATOM   10709 O  OH    . TYR   B  1  238  ? 8.975   22.394  111.582 1.00 30.14 ? 236  TYR   B OH    1 
ATOM   10710 N  N     . TYR   B  1  239  ? 10.664  14.252  114.118 1.00 16.49 ? 237  TYR   B N     1 
ATOM   10711 C  CA    . TYR   B  1  239  ? 10.605  12.837  114.461 1.00 18.58 ? 237  TYR   B CA    1 
ATOM   10712 C  C     . TYR   B  1  239  ? 10.655  12.650  115.966 1.00 19.87 ? 237  TYR   B C     1 
ATOM   10713 O  O     . TYR   B  1  239  ? 9.861   11.895  116.542 1.00 18.93 ? 237  TYR   B O     1 
ATOM   10714 C  CB    . TYR   B  1  239  ? 11.772  12.081  113.828 1.00 18.01 ? 237  TYR   B CB    1 
ATOM   10715 C  CG    . TYR   B  1  239  ? 11.860  10.648  114.311 1.00 21.17 ? 237  TYR   B CG    1 
ATOM   10716 C  CD1   . TYR   B  1  239  ? 11.107  9.659   113.718 1.00 20.37 ? 237  TYR   B CD1   1 
ATOM   10717 C  CD2   . TYR   B  1  239  ? 12.671  10.289  115.386 1.00 28.62 ? 237  TYR   B CD2   1 
ATOM   10718 C  CE1   . TYR   B  1  239  ? 11.167  8.369   114.135 1.00 20.80 ? 237  TYR   B CE1   1 
ATOM   10719 C  CE2   . TYR   B  1  239  ? 12.727  8.974   115.830 1.00 28.23 ? 237  TYR   B CE2   1 
ATOM   10720 C  CZ    . TYR   B  1  239  ? 11.964  8.021   115.190 1.00 26.56 ? 237  TYR   B CZ    1 
ATOM   10721 O  OH    . TYR   B  1  239  ? 11.984  6.706   115.581 1.00 33.84 ? 237  TYR   B OH    1 
ATOM   10722 N  N     . ARG   B  1  240  ? 11.623  13.295  116.620 1.00 18.33 ? 238  ARG   B N     1 
ATOM   10723 C  CA    . ARG   B  1  240  ? 11.752  13.119  118.056 1.00 19.57 ? 238  ARG   B CA    1 
ATOM   10724 C  C     . ARG   B  1  240  ? 10.542  13.661  118.784 1.00 19.98 ? 238  ARG   B C     1 
ATOM   10725 O  O     . ARG   B  1  240  ? 10.132  13.102  119.804 1.00 20.44 ? 238  ARG   B O     1 
ATOM   10726 C  CB    . ARG   B  1  240  ? 13.017  13.819  118.546 1.00 21.35 ? 238  ARG   B CB    1 
ATOM   10727 C  CG    . ARG   B  1  240  ? 14.278  13.159  118.077 1.00 22.07 ? 238  ARG   B CG    1 
ATOM   10728 C  CD    . ARG   B  1  240  ? 14.375  11.726  118.556 1.00 25.85 ? 238  ARG   B CD    1 
ATOM   10729 N  NE    . ARG   B  1  240  ? 15.560  11.089  117.996 1.00 29.45 ? 238  ARG   B NE    1 
ATOM   10730 C  CZ    . ARG   B  1  240  ? 15.792  9.784   118.009 1.00 40.10 ? 238  ARG   B CZ    1 
ATOM   10731 N  NH1   . ARG   B  1  240  ? 14.937  8.935   118.558 1.00 33.82 ? 238  ARG   B NH1   1 
ATOM   10732 N  NH2   . ARG   B  1  240  ? 16.911  9.320   117.461 1.00 39.79 ? 238  ARG   B NH2   1 
ATOM   10733 N  N     . ASP   B  1  241  ? 9.941   14.728  118.261 1.00 20.22 ? 239  ASP   B N     1 
ATOM   10734 C  CA    . ASP   B  1  241  ? 8.747   15.276  118.881 1.00 21.74 ? 239  ASP   B CA    1 
ATOM   10735 C  C     . ASP   B  1  241  ? 7.578   14.305  118.764 1.00 18.31 ? 239  ASP   B C     1 
ATOM   10736 O  O     . ASP   B  1  241  ? 6.820   14.125  119.719 1.00 20.01 ? 239  ASP   B O     1 
ATOM   10737 C  CB    . ASP   B  1  241  ? 8.415   16.647  118.286 1.00 23.98 ? 239  ASP   B CB    1 
ATOM   10738 C  CG    . ASP   B  1  241  ? 9.419   17.743  118.695 1.00 30.10 ? 239  ASP   B CG    1 
ATOM   10739 O  OD1   . ASP   B  1  241  ? 10.300  17.513  119.559 1.00 31.30 ? 239  ASP   B OD1   1 
ATOM   10740 O  OD2   . ASP   B  1  241  ? 9.324   18.853  118.133 1.00 39.45 ? 239  ASP   B OD2   1 
ATOM   10741 N  N     . TYR   B  1  242  ? 7.412   13.666  117.602 1.00 17.62 ? 240  TYR   B N     1 
ATOM   10742 C  CA    . TYR   B  1  242  ? 6.383   12.646  117.478 1.00 17.32 ? 240  TYR   B CA    1 
ATOM   10743 C  C     . TYR   B  1  242  ? 6.660   11.473  118.404 1.00 17.34 ? 240  TYR   B C     1 
ATOM   10744 O  O     . TYR   B  1  242  ? 5.742   10.925  119.025 1.00 16.88 ? 240  TYR   B O     1 
ATOM   10745 C  CB    . TYR   B  1  242  ? 6.357   12.119  116.053 1.00 17.68 ? 240  TYR   B CB    1 
ATOM   10746 C  CG    . TYR   B  1  242  ? 5.769   13.029  115.004 1.00 16.34 ? 240  TYR   B CG    1 
ATOM   10747 C  CD1   . TYR   B  1  242  ? 4.687   13.864  115.270 1.00 18.08 ? 240  TYR   B CD1   1 
ATOM   10748 C  CD2   . TYR   B  1  242  ? 6.298   13.025  113.731 1.00 17.76 ? 240  TYR   B CD2   1 
ATOM   10749 C  CE1   . TYR   B  1  242  ? 4.140   14.665  114.267 1.00 18.44 ? 240  TYR   B CE1   1 
ATOM   10750 C  CE2   . TYR   B  1  242  ? 5.772   13.812  112.737 1.00 17.37 ? 240  TYR   B CE2   1 
ATOM   10751 C  CZ    . TYR   B  1  242  ? 4.711   14.635  113.008 1.00 18.33 ? 240  TYR   B CZ    1 
ATOM   10752 O  OH    . TYR   B  1  242  ? 4.220   15.392  111.958 1.00 19.00 ? 240  TYR   B OH    1 
ATOM   10753 N  N     . GLU   B  1  243  ? 7.921   11.051  118.480 1.00 17.54 ? 241  GLU   B N     1 
ATOM   10754 C  CA    . GLU   B  1  243  ? 8.263   9.906   119.312 1.00 19.18 ? 241  GLU   B CA    1 
ATOM   10755 C  C     . GLU   B  1  243  ? 7.920   10.183  120.766 1.00 17.98 ? 241  GLU   B C     1 
ATOM   10756 O  O     . GLU   B  1  243  ? 7.308   9.353   121.448 1.00 17.58 ? 241  GLU   B O     1 
ATOM   10757 C  CB    . GLU   B  1  243  ? 9.755   9.626   119.163 1.00 18.92 ? 241  GLU   B CB    1 
ATOM   10758 C  CG    . GLU   B  1  243  ? 10.266  8.502   120.032 1.00 23.82 ? 241  GLU   B CG    1 
ATOM   10759 C  CD    . GLU   B  1  243  ? 11.778  8.380   119.969 1.00 27.02 ? 241  GLU   B CD    1 
ATOM   10760 O  OE1   . GLU   B  1  243  ? 12.457  9.411   119.788 1.00 30.32 ? 241  GLU   B OE1   1 
ATOM   10761 O  OE2   . GLU   B  1  243  ? 12.290  7.252   120.087 1.00 31.20 ? 241  GLU   B OE2   1 
ATOM   10762 N  N     . SER   B  1  244  ? 8.313   11.358  121.258 1.00 17.30 ? 242  SER   B N     1 
ATOM   10763 C  CA    A SER   B  1  244  ? 8.008   11.737  122.630 0.61 18.64 ? 242  SER   B CA    1 
ATOM   10764 C  CA    B SER   B  1  244  ? 8.004   11.720  122.636 0.39 18.67 ? 242  SER   B CA    1 
ATOM   10765 C  C     . SER   B  1  244  ? 6.504   11.822  122.850 1.00 17.06 ? 242  SER   B C     1 
ATOM   10766 O  O     . SER   B  1  244  ? 5.986   11.378  123.881 1.00 18.23 ? 242  SER   B O     1 
ATOM   10767 C  CB    A SER   B  1  244  ? 8.661   13.089  122.902 0.61 21.44 ? 242  SER   B CB    1 
ATOM   10768 C  CB    B SER   B  1  244  ? 8.666   13.047  122.987 0.39 21.43 ? 242  SER   B CB    1 
ATOM   10769 O  OG    A SER   B  1  244  ? 8.439   13.534  124.217 0.61 22.47 ? 242  SER   B OG    1 
ATOM   10770 O  OG    B SER   B  1  244  ? 10.071  12.941  122.892 0.39 20.55 ? 242  SER   B OG    1 
ATOM   10771 N  N     . ALA   B  1  245  ? 5.790   12.401  121.885 1.00 17.82 ? 243  ALA   B N     1 
ATOM   10772 C  CA    . ALA   B  1  245  ? 4.345   12.496  122.014 1.00 18.37 ? 243  ALA   B CA    1 
ATOM   10773 C  C     . ALA   B  1  245  ? 3.705   11.116  122.044 1.00 19.10 ? 243  ALA   B C     1 
ATOM   10774 O  O     . ALA   B  1  245  ? 2.763   10.884  122.804 1.00 19.42 ? 243  ALA   B O     1 
ATOM   10775 C  CB    . ALA   B  1  245  ? 3.756   13.329  120.878 1.00 19.05 ? 243  ALA   B CB    1 
ATOM   10776 N  N     . ILE   B  1  246  ? 4.187   10.187  121.213 1.00 17.88 ? 244  ILE   B N     1 
ATOM   10777 C  CA    . ILE   B  1  246  ? 3.607   8.845   121.226 1.00 18.82 ? 244  ILE   B CA    1 
ATOM   10778 C  C     . ILE   B  1  246  ? 3.752   8.205   122.596 1.00 20.32 ? 244  ILE   B C     1 
ATOM   10779 O  O     . ILE   B  1  246  ? 2.821   7.566   123.097 1.00 20.43 ? 244  ILE   B O     1 
ATOM   10780 C  CB    . ILE   B  1  246  ? 4.201   7.961   120.120 1.00 18.96 ? 244  ILE   B CB    1 
ATOM   10781 C  CG1   . ILE   B  1  246  ? 3.738   8.458   118.762 1.00 19.58 ? 244  ILE   B CG1   1 
ATOM   10782 C  CG2   . ILE   B  1  246  ? 3.773   6.503   120.324 1.00 18.94 ? 244  ILE   B CG2   1 
ATOM   10783 C  CD1   . ILE   B  1  246  ? 4.446   7.770   117.610 1.00 21.90 ? 244  ILE   B CD1   1 
ATOM   10784 N  N     . HIS   B  1  247  ? 4.912   8.356   123.228 1.00 19.32 ? 245  HIS   B N     1 
ATOM   10785 C  CA    . HIS   B  1  247  ? 5.049   7.808   124.572 1.00 19.17 ? 245  HIS   B CA    1 
ATOM   10786 C  C     . HIS   B  1  247  ? 4.037   8.420   125.520 1.00 19.52 ? 245  HIS   B C     1 
ATOM   10787 O  O     . HIS   B  1  247  ? 3.415   7.705   126.315 1.00 20.48 ? 245  HIS   B O     1 
ATOM   10788 C  CB    . HIS   B  1  247  ? 6.472   8.001   125.094 1.00 20.43 ? 245  HIS   B CB    1 
ATOM   10789 C  CG    . HIS   B  1  247  ? 7.461   7.079   124.458 1.00 21.82 ? 245  HIS   B CG    1 
ATOM   10790 N  ND1   . HIS   B  1  247  ? 7.442   5.719   124.673 1.00 21.37 ? 245  HIS   B ND1   1 
ATOM   10791 C  CD2   . HIS   B  1  247  ? 8.495   7.317   123.620 1.00 22.53 ? 245  HIS   B CD2   1 
ATOM   10792 C  CE1   . HIS   B  1  247  ? 8.417   5.154   123.983 1.00 23.10 ? 245  HIS   B CE1   1 
ATOM   10793 N  NE2   . HIS   B  1  247  ? 9.075   6.103   123.340 1.00 24.74 ? 245  HIS   B NE2   1 
ATOM   10794 N  N     . ALA   B  1  248  ? 3.853   9.738   125.449 1.00 18.27 ? 246  ALA   B N     1 
ATOM   10795 C  CA    . ALA   B  1  248  ? 2.923   10.386  126.365 1.00 19.52 ? 246  ALA   B CA    1 
ATOM   10796 C  C     . ALA   B  1  248  ? 1.491   9.968   126.058 1.00 18.14 ? 246  ALA   B C     1 
ATOM   10797 O  O     . ALA   B  1  248  ? 0.719   9.634   126.966 1.00 20.07 ? 246  ALA   B O     1 
ATOM   10798 C  CB    . ALA   B  1  248  ? 3.064   11.902  126.253 1.00 20.54 ? 246  ALA   B CB    1 
ATOM   10799 N  N     . ILE   B  1  249  ? 1.122   9.988   124.777 1.00 19.20 ? 247  ILE   B N     1 
ATOM   10800 C  CA    . ILE   B  1  249  ? -0.237  9.624   124.392 1.00 19.75 ? 247  ILE   B CA    1 
ATOM   10801 C  C     . ILE   B  1  249  ? -0.500  8.158   124.688 1.00 19.52 ? 247  ILE   B C     1 
ATOM   10802 O  O     . ILE   B  1  249  ? -1.587  7.786   125.153 1.00 20.33 ? 247  ILE   B O     1 
ATOM   10803 C  CB    . ILE   B  1  249  ? -0.458  9.933   122.908 1.00 18.12 ? 247  ILE   B CB    1 
ATOM   10804 C  CG1   . ILE   B  1  249  ? -0.340  11.425  122.656 1.00 18.31 ? 247  ILE   B CG1   1 
ATOM   10805 C  CG2   . ILE   B  1  249  ? -1.811  9.360   122.449 1.00 21.40 ? 247  ILE   B CG2   1 
ATOM   10806 C  CD1   . ILE   B  1  249  ? -0.039  11.754  121.214 1.00 19.48 ? 247  ILE   B CD1   1 
ATOM   10807 N  N     . GLY   B  1  250  ? 0.486   7.302   124.413 1.00 20.46 ? 248  GLY   B N     1 
ATOM   10808 C  CA    . GLY   B  1  250  ? 0.313   5.882   124.645 1.00 20.93 ? 248  GLY   B CA    1 
ATOM   10809 C  C     . GLY   B  1  250  ? 0.167   5.555   126.113 1.00 24.18 ? 248  GLY   B C     1 
ATOM   10810 O  O     . GLY   B  1  250  ? -0.652  4.717   126.495 1.00 22.88 ? 248  GLY   B O     1 
ATOM   10811 N  N     . LYS   B  1  251  ? 0.958   6.206   126.961 1.00 21.63 ? 249  LYS   B N     1 
ATOM   10812 C  CA    . LYS   B  1  251  ? 0.796   5.986   128.391 1.00 25.70 ? 249  LYS   B CA    1 
ATOM   10813 C  C     . LYS   B  1  251  ? -0.560  6.489   128.866 1.00 21.13 ? 249  LYS   B C     1 
ATOM   10814 O  O     . LYS   B  1  251  ? -1.237  5.813   129.654 1.00 24.40 ? 249  LYS   B O     1 
ATOM   10815 C  CB    . LYS   B  1  251  ? 1.944   6.643   129.163 1.00 24.19 ? 249  LYS   B CB    1 
ATOM   10816 N  N     . ALA   B  1  252  ? -0.987  7.651   128.363 1.00 23.32 ? 250  ALA   B N     1 
ATOM   10817 C  CA    . ALA   B  1  252  ? -2.285  8.197   128.747 1.00 23.45 ? 250  ALA   B CA    1 
ATOM   10818 C  C     . ALA   B  1  252  ? -3.425  7.332   128.232 1.00 23.76 ? 250  ALA   B C     1 
ATOM   10819 O  O     . ALA   B  1  252  ? -4.454  7.202   128.901 1.00 25.74 ? 250  ALA   B O     1 
ATOM   10820 C  CB    . ALA   B  1  252  ? -2.430  9.628   128.234 1.00 22.49 ? 250  ALA   B CB    1 
ATOM   10821 N  N     . SER   B  1  253  ? -3.269  6.751   127.042 1.00 23.55 ? 251  SER   B N     1 
ATOM   10822 C  CA    . SER   B  1  253  ? -4.299  5.860   126.522 1.00 22.88 ? 251  SER   B CA    1 
ATOM   10823 C  C     . SER   B  1  253  ? -4.573  4.727   127.496 1.00 22.72 ? 251  SER   B C     1 
ATOM   10824 O  O     . SER   B  1  253  ? -5.732  4.361   127.724 1.00 25.18 ? 251  SER   B O     1 
ATOM   10825 C  CB    . SER   B  1  253  ? -3.854  5.281   125.192 1.00 21.88 ? 251  SER   B CB    1 
ATOM   10826 O  OG    . SER   B  1  253  ? -4.843  4.390   124.719 1.00 23.73 ? 251  SER   B OG    1 
ATOM   10827 N  N     . ALA   B  1  254  ? -3.512  4.155   128.073 1.00 23.07 ? 252  ALA   B N     1 
ATOM   10828 C  CA    . ALA   B  1  254  ? -3.620  3.177   129.153 1.00 26.39 ? 252  ALA   B CA    1 
ATOM   10829 C  C     . ALA   B  1  254  ? -4.478  1.981   128.751 1.00 28.00 ? 252  ALA   B C     1 
ATOM   10830 O  O     . ALA   B  1  254  ? -5.307  1.498   129.524 1.00 29.77 ? 252  ALA   B O     1 
ATOM   10831 C  CB    . ALA   B  1  254  ? -4.089  3.812   130.467 1.00 27.75 ? 252  ALA   B CB    1 
ATOM   10832 N  N     . GLY   B  1  255  ? -4.285  1.506   127.522 1.00 28.73 ? 253  GLY   B N     1 
ATOM   10833 C  CA    . GLY   B  1  255  ? -5.010  0.346   127.054 1.00 29.42 ? 253  GLY   B CA    1 
ATOM   10834 C  C     . GLY   B  1  255  ? -6.428  0.598   126.594 1.00 26.65 ? 253  GLY   B C     1 
ATOM   10835 O  O     . GLY   B  1  255  ? -7.176  -0.367  126.410 1.00 28.76 ? 253  GLY   B O     1 
ATOM   10836 N  N     . ARG   B  1  256  ? -6.835  1.855   126.408 1.00 23.98 ? 254  ARG   B N     1 
ATOM   10837 C  CA    . ARG   B  1  256  ? -8.193  2.101   125.935 1.00 25.86 ? 254  ARG   B CA    1 
ATOM   10838 C  C     . ARG   B  1  256  ? -8.404  1.668   124.496 1.00 25.06 ? 254  ARG   B C     1 
ATOM   10839 O  O     . ARG   B  1  256  ? -9.556  1.583   124.054 1.00 27.20 ? 254  ARG   B O     1 
ATOM   10840 C  CB    . ARG   B  1  256  ? -8.578  3.570   126.092 1.00 24.13 ? 254  ARG   B CB    1 
ATOM   10841 C  CG    . ARG   B  1  256  ? -9.007  3.928   127.510 1.00 25.35 ? 254  ARG   B CG    1 
ATOM   10842 C  CD    . ARG   B  1  256  ? -9.313  5.404   127.619 1.00 26.42 ? 254  ARG   B CD    1 
ATOM   10843 N  NE    . ARG   B  1  256  ? -8.086  6.194   127.638 1.00 23.45 ? 254  ARG   B NE    1 
ATOM   10844 C  CZ    . ARG   B  1  256  ? -8.045  7.509   127.503 1.00 25.60 ? 254  ARG   B CZ    1 
ATOM   10845 N  NH1   . ARG   B  1  256  ? -9.135  8.209   127.239 1.00 27.08 ? 254  ARG   B NH1   1 
ATOM   10846 N  NH2   . ARG   B  1  256  ? -6.878  8.139   127.640 1.00 26.23 ? 254  ARG   B NH2   1 
ATOM   10847 N  N     . GLY   B  1  257  ? -7.334  1.393   123.762 1.00 24.35 ? 255  GLY   B N     1 
ATOM   10848 C  CA    . GLY   B  1  257  ? -7.468  0.958   122.387 1.00 23.73 ? 255  GLY   B CA    1 
ATOM   10849 C  C     . GLY   B  1  257  ? -7.589  2.115   121.424 1.00 23.23 ? 255  GLY   B C     1 
ATOM   10850 O  O     . GLY   B  1  257  ? -7.654  3.288   121.788 1.00 22.34 ? 255  GLY   B O     1 
ATOM   10851 N  N     . ILE   B  1  258  ? -7.664  1.756   120.144 1.00 22.77 ? 256  ILE   B N     1 
ATOM   10852 C  CA    . ILE   B  1  258  ? -7.569  2.764   119.096 1.00 21.16 ? 256  ILE   B CA    1 
ATOM   10853 C  C     . ILE   B  1  258  ? -8.854  3.557   118.882 1.00 22.03 ? 256  ILE   B C     1 
ATOM   10854 O  O     . ILE   B  1  258  ? -8.809  4.620   118.256 1.00 23.64 ? 256  ILE   B O     1 
ATOM   10855 C  CB    . ILE   B  1  258  ? -7.123  2.135   117.768 1.00 23.59 ? 256  ILE   B CB    1 
ATOM   10856 C  CG1   . ILE   B  1  258  ? -8.173  1.138   117.284 1.00 24.31 ? 256  ILE   B CG1   1 
ATOM   10857 C  CG2   . ILE   B  1  258  ? -5.778  1.448   117.932 1.00 24.29 ? 256  ILE   B CG2   1 
ATOM   10858 C  CD1   . ILE   B  1  258  ? -7.822  0.487   115.963 1.00 26.24 ? 256  ILE   B CD1   1 
ATOM   10859 N  N     . TYR   B  1  259  ? -9.994  3.080   119.379 1.00 22.64 ? 257  TYR   B N     1 
ATOM   10860 C  CA    . TYR   B  1  259  ? -11.263 3.773   119.166 1.00 24.00 ? 257  TYR   B CA    1 
ATOM   10861 C  C     . TYR   B  1  259  ? -11.596 4.727   120.308 1.00 25.23 ? 257  TYR   B C     1 
ATOM   10862 O  O     . TYR   B  1  259  ? -11.794 5.928   120.085 1.00 24.12 ? 257  TYR   B O     1 
ATOM   10863 C  CB    . TYR   B  1  259  ? -12.385 2.751   118.938 1.00 23.72 ? 257  TYR   B CB    1 
ATOM   10864 C  CG    . TYR   B  1  259  ? -12.026 1.784   117.846 1.00 26.07 ? 257  TYR   B CG    1 
ATOM   10865 C  CD1   . TYR   B  1  259  ? -11.899 2.224   116.542 1.00 25.29 ? 257  TYR   B CD1   1 
ATOM   10866 C  CD2   . TYR   B  1  259  ? -11.780 0.447   118.112 1.00 27.97 ? 257  TYR   B CD2   1 
ATOM   10867 C  CE1   . TYR   B  1  259  ? -11.554 1.362   115.519 1.00 23.98 ? 257  TYR   B CE1   1 
ATOM   10868 C  CE2   . TYR   B  1  259  ? -11.429 -0.426  117.095 1.00 24.65 ? 257  TYR   B CE2   1 
ATOM   10869 C  CZ    . TYR   B  1  259  ? -11.316 0.045   115.800 1.00 25.21 ? 257  TYR   B CZ    1 
ATOM   10870 O  OH    . TYR   B  1  259  ? -10.965 -0.801  114.775 1.00 26.57 ? 257  TYR   B OH    1 
ATOM   10871 N  N     . GLU   B  1  260  ? -11.665 4.207   121.534 1.00 24.32 ? 258  GLU   B N     1 
ATOM   10872 C  CA    . GLU   B  1  260  ? -11.934 5.079   122.668 1.00 25.13 ? 258  GLU   B CA    1 
ATOM   10873 C  C     . GLU   B  1  260  ? -10.722 5.940   122.995 1.00 29.33 ? 258  GLU   B C     1 
ATOM   10874 O  O     . GLU   B  1  260  ? -10.865 7.116   123.359 1.00 27.39 ? 258  GLU   B O     1 
ATOM   10875 C  CB    . GLU   B  1  260  ? -12.343 4.252   123.884 1.00 27.68 ? 258  GLU   B CB    1 
ATOM   10876 C  CG    . GLU   B  1  260  ? -12.595 5.106   125.116 1.00 34.81 ? 258  GLU   B CG    1 
ATOM   10877 C  CD    . GLU   B  1  260  ? -12.745 4.283   126.374 1.00 37.03 ? 258  GLU   B CD    1 
ATOM   10878 O  OE1   . GLU   B  1  260  ? -12.965 3.057   126.255 1.00 40.15 ? 258  GLU   B OE1   1 
ATOM   10879 O  OE2   . GLU   B  1  260  ? -12.637 4.864   127.479 1.00 37.40 ? 258  GLU   B OE2   1 
ATOM   10880 N  N     . GLY   B  1  261  ? -9.528  5.379   122.860 1.00 23.83 ? 259  GLY   B N     1 
ATOM   10881 C  CA    . GLY   B  1  261  ? -8.332  6.033   123.319 1.00 22.38 ? 259  GLY   B CA    1 
ATOM   10882 C  C     . GLY   B  1  261  ? -7.758  6.981   122.286 1.00 22.45 ? 259  GLY   B C     1 
ATOM   10883 O  O     . GLY   B  1  261  ? -8.105  6.952   121.099 1.00 22.29 ? 259  GLY   B O     1 
ATOM   10884 N  N     . PRO   B  1  262  ? -6.854  7.845   122.734 1.00 20.48 ? 260  PRO   B N     1 
ATOM   10885 C  CA    . PRO   B  1  262  ? -6.301  8.874   121.851 1.00 19.20 ? 260  PRO   B CA    1 
ATOM   10886 C  C     . PRO   B  1  262  ? -5.317  8.304   120.843 1.00 21.30 ? 260  PRO   B C     1 
ATOM   10887 O  O     . PRO   B  1  262  ? -4.745  7.223   121.005 1.00 23.17 ? 260  PRO   B O     1 
ATOM   10888 C  CB    . PRO   B  1  262  ? -5.587  9.821   122.820 1.00 21.72 ? 260  PRO   B CB    1 
ATOM   10889 C  CG    . PRO   B  1  262  ? -5.218  8.934   123.988 1.00 23.29 ? 260  PRO   B CG    1 
ATOM   10890 C  CD    . PRO   B  1  262  ? -6.399  8.003   124.127 1.00 21.90 ? 260  PRO   B CD    1 
ATOM   10891 N  N     . GLY   B  1  263  ? -5.112  9.075   119.792 1.00 18.38 ? 261  GLY   B N     1 
ATOM   10892 C  CA    . GLY   B  1  263  ? -4.085  8.731   118.837 1.00 20.46 ? 261  GLY   B CA    1 
ATOM   10893 C  C     . GLY   B  1  263  ? -3.246  9.932   118.464 1.00 18.23 ? 261  GLY   B C     1 
ATOM   10894 O  O     . GLY   B  1  263  ? -3.363  11.005  119.071 1.00 19.09 ? 261  GLY   B O     1 
ATOM   10895 N  N     . ILE   B  1  264  ? -2.409  9.763   117.452 1.00 19.00 ? 262  ILE   B N     1 
ATOM   10896 C  CA    . ILE   B  1  264  ? -1.536  10.826  116.977 1.00 17.56 ? 262  ILE   B CA    1 
ATOM   10897 C  C     . ILE   B  1  264  ? -1.696  10.939  115.475 1.00 17.78 ? 262  ILE   B C     1 
ATOM   10898 O  O     . ILE   B  1  264  ? -2.014  9.960   114.795 1.00 19.40 ? 262  ILE   B O     1 
ATOM   10899 C  CB    . ILE   B  1  264  ? -0.065  10.566  117.376 1.00 19.08 ? 262  ILE   B CB    1 
ATOM   10900 C  CG1   . ILE   B  1  264  ? 0.768   11.829  117.172 1.00 19.30 ? 262  ILE   B CG1   1 
ATOM   10901 C  CG2   . ILE   B  1  264  ? 0.510   9.399   116.586 1.00 19.63 ? 262  ILE   B CG2   1 
ATOM   10902 C  CD1   . ILE   B  1  264  ? 2.211   11.708  117.645 1.00 20.36 ? 262  ILE   B CD1   1 
ATOM   10903 N  N     . SER   B  1  265  ? -1.513  12.149  114.962 1.00 15.66 ? 263  SER   B N     1 
ATOM   10904 C  CA    . SER   B  1  265  ? -1.495  12.403  113.530 1.00 17.22 ? 263  SER   B CA    1 
ATOM   10905 C  C     . SER   B  1  265  ? -0.128  12.952  113.157 1.00 18.85 ? 263  SER   B C     1 
ATOM   10906 O  O     . SER   B  1  265  ? 0.427   13.783  113.877 1.00 20.58 ? 263  SER   B O     1 
ATOM   10907 C  CB    . SER   B  1  265  ? -2.544  13.435  113.168 1.00 19.36 ? 263  SER   B CB    1 
ATOM   10908 O  OG    . SER   B  1  265  ? -3.841  12.865  113.188 1.00 19.96 ? 263  SER   B OG    1 
ATOM   10909 N  N     . ILE   B  1  266  ? 0.419   12.485  112.038 1.00 16.26 ? 264  ILE   B N     1 
ATOM   10910 C  CA    . ILE   B  1  266  ? 1.725   12.926  111.575 1.00 16.30 ? 264  ILE   B CA    1 
ATOM   10911 C  C     . ILE   B  1  266  ? 1.606   13.392  110.137 1.00 16.24 ? 264  ILE   B C     1 
ATOM   10912 O  O     . ILE   B  1  266  ? 0.665   13.052  109.423 1.00 16.94 ? 264  ILE   B O     1 
ATOM   10913 C  CB    . ILE   B  1  266  ? 2.799   11.824  111.693 1.00 17.98 ? 264  ILE   B CB    1 
ATOM   10914 C  CG1   . ILE   B  1  266  ? 2.494   10.661  110.748 1.00 20.65 ? 264  ILE   B CG1   1 
ATOM   10915 C  CG2   . ILE   B  1  266  ? 2.892   11.340  113.137 1.00 18.95 ? 264  ILE   B CG2   1 
ATOM   10916 C  CD1   . ILE   B  1  266  ? 3.650   9.694   110.538 1.00 22.80 ? 264  ILE   B CD1   1 
ATOM   10917 N  N     . LYS   B  1  267  ? 2.592   14.167  109.710 1.00 16.06 ? 265  LYS   B N     1 
ATOM   10918 C  CA    . LYS   B  1  267  ? 2.715   14.571  108.320 1.00 16.63 ? 265  LYS   B CA    1 
ATOM   10919 C  C     . LYS   B  1  267  ? 4.034   14.031  107.806 1.00 15.44 ? 265  LYS   B C     1 
ATOM   10920 O  O     . LYS   B  1  267  ? 5.087   14.270  108.410 1.00 17.07 ? 265  LYS   B O     1 
ATOM   10921 C  CB    . LYS   B  1  267  ? 2.681   16.088  108.200 1.00 16.69 ? 265  LYS   B CB    1 
ATOM   10922 C  CG    . LYS   B  1  267  ? 1.296   16.663  108.397 1.00 21.62 ? 265  LYS   B CG    1 
ATOM   10923 C  CD    . LYS   B  1  267  ? 1.354   18.171  108.425 1.00 25.94 ? 265  LYS   B CD    1 
ATOM   10924 C  CE    . LYS   B  1  267  ? -0.022  18.782  108.635 1.00 29.49 ? 265  LYS   B CE    1 
ATOM   10925 N  NZ    . LYS   B  1  267  ? -0.737  18.175  109.787 1.00 31.03 ? 265  LYS   B NZ    1 
ATOM   10926 N  N     . LEU   B  1  268  ? 3.974   13.285  106.707 1.00 15.07 ? 266  LEU   B N     1 
ATOM   10927 C  CA    . LEU   B  1  268  ? 5.213   12.770  106.138 1.00 15.43 ? 266  LEU   B CA    1 
ATOM   10928 C  C     . LEU   B  1  268  ? 6.188   13.884  105.778 1.00 17.22 ? 266  LEU   B C     1 
ATOM   10929 O  O     . LEU   B  1  268  ? 7.399   13.694  105.916 1.00 16.35 ? 266  LEU   B O     1 
ATOM   10930 C  CB    . LEU   B  1  268  ? 4.934   11.874  104.939 1.00 15.52 ? 266  LEU   B CB    1 
ATOM   10931 C  CG    . LEU   B  1  268  ? 4.030   10.689  105.261 1.00 16.28 ? 266  LEU   B CG    1 
ATOM   10932 C  CD1   . LEU   B  1  268  ? 3.852   9.851   104.014 1.00 18.97 ? 266  LEU   B CD1   1 
ATOM   10933 C  CD2   . LEU   B  1  268  ? 4.597   9.846   106.383 1.00 19.52 ? 266  LEU   B CD2   1 
ATOM   10934 N  N     . SER   B  1  269  ? 5.697   15.067  105.383 1.00 15.51 ? 267  SER   B N     1 
ATOM   10935 C  CA    . SER   B  1  269  ? 6.622   16.147  105.047 1.00 15.02 ? 267  SER   B CA    1 
ATOM   10936 C  C     . SER   B  1  269  ? 7.398   16.625  106.262 1.00 16.60 ? 267  SER   B C     1 
ATOM   10937 O  O     . SER   B  1  269  ? 8.446   17.253  106.105 1.00 15.90 ? 267  SER   B O     1 
ATOM   10938 C  CB    . SER   B  1  269  ? 5.894   17.334  104.423 1.00 16.28 ? 267  SER   B CB    1 
ATOM   10939 O  OG    . SER   B  1  269  ? 5.076   17.965  105.392 1.00 17.06 ? 267  SER   B OG    1 
ATOM   10940 N  N     . ALA   B  1  270  ? 6.910   16.351  107.468 1.00 14.83 ? 268  ALA   B N     1 
ATOM   10941 C  CA    . ALA   B  1  270  ? 7.677   16.697  108.652 1.00 15.41 ? 268  ALA   B CA    1 
ATOM   10942 C  C     . ALA   B  1  270  ? 8.896   15.810  108.819 1.00 17.28 ? 268  ALA   B C     1 
ATOM   10943 O  O     . ALA   B  1  270  ? 9.832   16.193  109.531 1.00 16.57 ? 268  ALA   B O     1 
ATOM   10944 C  CB    . ALA   B  1  270  ? 6.809   16.538  109.902 1.00 16.80 ? 268  ALA   B CB    1 
ATOM   10945 N  N     . LEU   B  1  271  ? 8.896   14.627  108.208 1.00 15.73 ? 269  LEU   B N     1 
ATOM   10946 C  CA    . LEU   B  1  271  ? 9.879   13.606  108.541 1.00 17.57 ? 269  LEU   B CA    1 
ATOM   10947 C  C     . LEU   B  1  271  ? 11.016  13.520  107.549 1.00 15.92 ? 269  LEU   B C     1 
ATOM   10948 O  O     . LEU   B  1  271  ? 11.929  12.718  107.753 1.00 17.34 ? 269  LEU   B O     1 
ATOM   10949 C  CB    . LEU   B  1  271  ? 9.204   12.246  108.675 1.00 16.42 ? 269  LEU   B CB    1 
ATOM   10950 C  CG    . LEU   B  1  271  ? 8.218   12.208  109.843 1.00 17.83 ? 269  LEU   B CG    1 
ATOM   10951 C  CD1   . LEU   B  1  271  ? 7.496   10.880  109.837 1.00 21.99 ? 269  LEU   B CD1   1 
ATOM   10952 C  CD2   . LEU   B  1  271  ? 8.968   12.407  111.140 1.00 18.42 ? 269  LEU   B CD2   1 
ATOM   10953 N  N     . HIS   B  1  272  ? 10.994  14.333  106.492 1.00 16.38 ? 270  HIS   B N     1 
ATOM   10954 C  CA    . HIS   B  1  272  ? 12.114  14.334  105.574 1.00 16.97 ? 270  HIS   B CA    1 
ATOM   10955 C  C     . HIS   B  1  272  ? 12.106  15.654  104.830 1.00 15.27 ? 270  HIS   B C     1 
ATOM   10956 O  O     . HIS   B  1  272  ? 11.030  16.108  104.436 1.00 16.68 ? 270  HIS   B O     1 
ATOM   10957 C  CB    . HIS   B  1  272  ? 11.982  13.181  104.576 1.00 18.06 ? 270  HIS   B CB    1 
ATOM   10958 C  CG    . HIS   B  1  272  ? 13.267  12.863  103.898 1.00 17.56 ? 270  HIS   B CG    1 
ATOM   10959 N  ND1   . HIS   B  1  272  ? 13.759  13.619  102.859 1.00 20.40 ? 270  HIS   B ND1   1 
ATOM   10960 C  CD2   . HIS   B  1  272  ? 14.208  11.932  104.173 1.00 22.66 ? 270  HIS   B CD2   1 
ATOM   10961 C  CE1   . HIS   B  1  272  ? 14.933  13.138  102.491 1.00 21.66 ? 270  HIS   B CE1   1 
ATOM   10962 N  NE2   . HIS   B  1  272  ? 15.229  12.115  103.273 1.00 23.03 ? 270  HIS   B NE2   1 
ATOM   10963 N  N     . PRO   B  1  273  ? 13.264  16.279  104.595 1.00 16.23 ? 271  PRO   B N     1 
ATOM   10964 C  CA    . PRO   B  1  273  ? 13.284  17.564  103.871 1.00 16.04 ? 271  PRO   B CA    1 
ATOM   10965 C  C     . PRO   B  1  273  ? 13.061  17.437  102.377 1.00 15.04 ? 271  PRO   B C     1 
ATOM   10966 O  O     . PRO   B  1  273  ? 12.869  18.466  101.723 1.00 17.46 ? 271  PRO   B O     1 
ATOM   10967 C  CB    . PRO   B  1  273  ? 14.684  18.114  104.168 1.00 18.18 ? 271  PRO   B CB    1 
ATOM   10968 C  CG    . PRO   B  1  273  ? 15.498  16.896  104.451 1.00 18.80 ? 271  PRO   B CG    1 
ATOM   10969 C  CD    . PRO   B  1  273  ? 14.582  15.923  105.138 1.00 17.20 ? 271  PRO   B CD    1 
ATOM   10970 N  N     . ARG   B  1  274  ? 13.073  16.231  101.819 1.00 16.02 ? 272  ARG   B N     1 
ATOM   10971 C  CA    . ARG   B  1  274  ? 12.887  16.016  100.390 1.00 15.59 ? 272  ARG   B CA    1 
ATOM   10972 C  C     . ARG   B  1  274  ? 11.785  15.001  100.168 1.00 16.35 ? 272  ARG   B C     1 
ATOM   10973 O  O     . ARG   B  1  274  ? 11.932  14.002  99.459  1.00 17.79 ? 272  ARG   B O     1 
ATOM   10974 C  CB    . ARG   B  1  274  ? 14.188  15.576  99.717  1.00 15.78 ? 272  ARG   B CB    1 
ATOM   10975 C  CG    . ARG   B  1  274  ? 15.322  16.601  99.765  1.00 18.05 ? 272  ARG   B CG    1 
ATOM   10976 C  CD    . ARG   B  1  274  ? 14.931  17.950  99.162  1.00 17.13 ? 272  ARG   B CD    1 
ATOM   10977 N  NE    . ARG   B  1  274  ? 14.443  17.853  97.792  1.00 17.27 ? 272  ARG   B NE    1 
ATOM   10978 C  CZ    . ARG   B  1  274  ? 15.229  17.765  96.726  1.00 17.09 ? 272  ARG   B CZ    1 
ATOM   10979 N  NH1   . ARG   B  1  274  ? 16.543  17.679  96.844  1.00 16.63 ? 272  ARG   B NH1   1 
ATOM   10980 N  NH2   . ARG   B  1  274  ? 14.685  17.774  95.517  1.00 18.10 ? 272  ARG   B NH2   1 
ATOM   10981 N  N     . TYR   B  1  275  ? 10.642  15.244  100.799 1.00 16.06 ? 273  TYR   B N     1 
ATOM   10982 C  CA    . TYR   B  1  275  ? 9.486   14.374  100.626 1.00 17.29 ? 273  TYR   B CA    1 
ATOM   10983 C  C     . TYR   B  1  275  ? 8.813   14.724  99.306  1.00 16.85 ? 273  TYR   B C     1 
ATOM   10984 O  O     . TYR   B  1  275  ? 7.979   15.620  99.217  1.00 16.81 ? 273  TYR   B O     1 
ATOM   10985 C  CB    . TYR   B  1  275  ? 8.544   14.509  101.814 1.00 16.06 ? 273  TYR   B CB    1 
ATOM   10986 C  CG    . TYR   B  1  275  ? 7.289   13.704  101.667 1.00 14.88 ? 273  TYR   B CG    1 
ATOM   10987 C  CD1   . TYR   B  1  275  ? 7.342   12.373  101.270 1.00 17.15 ? 273  TYR   B CD1   1 
ATOM   10988 C  CD2   . TYR   B  1  275  ? 6.055   14.276  101.908 1.00 16.60 ? 273  TYR   B CD2   1 
ATOM   10989 C  CE1   . TYR   B  1  275  ? 6.194   11.634  101.113 1.00 17.61 ? 273  TYR   B CE1   1 
ATOM   10990 C  CE2   . TYR   B  1  275  ? 4.906   13.548  101.765 1.00 15.88 ? 273  TYR   B CE2   1 
ATOM   10991 C  CZ    . TYR   B  1  275  ? 4.979   12.225  101.369 1.00 16.02 ? 273  TYR   B CZ    1 
ATOM   10992 O  OH    . TYR   B  1  275  ? 3.835   11.499  101.197 1.00 18.10 ? 273  TYR   B OH    1 
ATOM   10993 N  N     . SER   B  1  276  ? 9.205   14.024  98.248  1.00 15.20 ? 274  SER   B N     1 
ATOM   10994 C  CA    . SER   B  1  276  ? 8.648   14.314  96.933  1.00 16.18 ? 274  SER   B CA    1 
ATOM   10995 C  C     . SER   B  1  276  ? 8.892   13.118  96.036  1.00 15.37 ? 274  SER   B C     1 
ATOM   10996 O  O     . SER   B  1  276  ? 9.803   12.323  96.269  1.00 15.53 ? 274  SER   B O     1 
ATOM   10997 C  CB    . SER   B  1  276  ? 9.282   15.562  96.322  1.00 20.25 ? 274  SER   B CB    1 
ATOM   10998 O  OG    . SER   B  1  276  ? 10.624  15.298  95.986  1.00 24.42 ? 274  SER   B OG    1 
ATOM   10999 N  N     . ARG   B  1  277  ? 8.058   13.002  95.001  1.00 14.93 ? 275  ARG   B N     1 
ATOM   11000 C  CA    . ARG   B  1  277  ? 8.244   11.924  94.044  1.00 14.56 ? 275  ARG   B CA    1 
ATOM   11001 C  C     . ARG   B  1  277  ? 9.616   11.986  93.395  1.00 15.03 ? 275  ARG   B C     1 
ATOM   11002 O  O     . ARG   B  1  277  ? 10.196  10.941  93.092  1.00 16.25 ? 275  ARG   B O     1 
ATOM   11003 C  CB    . ARG   B  1  277  ? 7.130   11.972  92.997  1.00 16.18 ? 275  ARG   B CB    1 
ATOM   11004 C  CG    . ARG   B  1  277  ? 7.299   11.007  91.825  1.00 16.83 ? 275  ARG   B CG    1 
ATOM   11005 C  CD    . ARG   B  1  277  ? 7.317   9.554   92.293  1.00 16.58 ? 275  ARG   B CD    1 
ATOM   11006 N  NE    . ARG   B  1  277  ? 7.491   8.629   91.179  1.00 16.67 ? 275  ARG   B NE    1 
ATOM   11007 C  CZ    . ARG   B  1  277  ? 8.665   8.265   90.681  1.00 17.09 ? 275  ARG   B CZ    1 
ATOM   11008 N  NH1   . ARG   B  1  277  ? 9.799   8.800   91.111  1.00 19.21 ? 275  ARG   B NH1   1 
ATOM   11009 N  NH2   . ARG   B  1  277  ? 8.701   7.319   89.745  1.00 17.59 ? 275  ARG   B NH2   1 
ATOM   11010 N  N     . ALA   B  1  278  ? 10.143  13.191  93.175  1.00 15.08 ? 276  ALA   B N     1 
ATOM   11011 C  CA    . ALA   B  1  278  ? 11.458  13.307  92.556  1.00 16.89 ? 276  ALA   B CA    1 
ATOM   11012 C  C     . ALA   B  1  278  ? 12.530  12.647  93.404  1.00 16.84 ? 276  ALA   B C     1 
ATOM   11013 O  O     . ALA   B  1  278  ? 13.564  12.213  92.880  1.00 18.05 ? 276  ALA   B O     1 
ATOM   11014 C  CB    . ALA   B  1  278  ? 11.801  14.776  92.310  1.00 17.58 ? 276  ALA   B CB    1 
ATOM   11015 N  N     . GLN   B  1  279  ? 12.312  12.571  94.714  1.00 16.08 ? 277  GLN   B N     1 
ATOM   11016 C  CA    . GLN   B  1  279  ? 13.253  11.941  95.630  1.00 15.75 ? 277  GLN   B CA    1 
ATOM   11017 C  C     . GLN   B  1  279  ? 12.695  10.660  96.238  1.00 15.28 ? 277  GLN   B C     1 
ATOM   11018 O  O     . GLN   B  1  279  ? 12.975  10.341  97.394  1.00 16.55 ? 277  GLN   B O     1 
ATOM   11019 C  CB    . GLN   B  1  279  ? 13.675  12.914  96.725  1.00 17.82 ? 277  GLN   B CB    1 
ATOM   11020 C  CG    . GLN   B  1  279  ? 14.287  14.180  96.166  1.00 18.50 ? 277  GLN   B CG    1 
ATOM   11021 C  CD    . GLN   B  1  279  ? 15.585  13.896  95.439  1.00 21.07 ? 277  GLN   B CD    1 
ATOM   11022 O  OE1   . GLN   B  1  279  ? 16.271  12.908  95.718  1.00 23.18 ? 277  GLN   B OE1   1 
ATOM   11023 N  NE2   . GLN   B  1  279  ? 15.918  14.748  94.485  1.00 18.02 ? 277  GLN   B NE2   1 
ATOM   11024 N  N     . ALA   B  1  280  ? 11.927  9.902   95.453  1.00 16.74 ? 278  ALA   B N     1 
ATOM   11025 C  CA    . ALA   B  1  280  ? 11.239  8.741   95.998  1.00 16.82 ? 278  ALA   B CA    1 
ATOM   11026 C  C     . ALA   B  1  280  ? 12.210  7.754   96.627  1.00 18.07 ? 278  ALA   B C     1 
ATOM   11027 O  O     . ALA   B  1  280  ? 11.890  7.139   97.640  1.00 17.30 ? 278  ALA   B O     1 
ATOM   11028 C  CB    . ALA   B  1  280  ? 10.431  8.046   94.904  1.00 19.39 ? 278  ALA   B CB    1 
ATOM   11029 N  N     . ALA   B  1  281  ? 13.391  7.572   96.037  1.00 16.96 ? 279  ALA   B N     1 
ATOM   11030 C  CA    . ALA   B  1  281  ? 14.338  6.626   96.620  1.00 18.29 ? 279  ALA   B CA    1 
ATOM   11031 C  C     . ALA   B  1  281  ? 14.746  7.050   98.027  1.00 17.33 ? 279  ALA   B C     1 
ATOM   11032 O  O     . ALA   B  1  281  ? 14.818  6.216   98.938  1.00 19.32 ? 279  ALA   B O     1 
ATOM   11033 C  CB    . ALA   B  1  281  ? 15.567  6.467   95.723  1.00 19.61 ? 279  ALA   B CB    1 
ATOM   11034 N  N     . ARG   B  1  282  ? 14.999  8.343   98.225  1.00 16.14 ? 280  ARG   B N     1 
ATOM   11035 C  CA    . ARG   B  1  282  ? 15.340  8.822   99.560  1.00 16.37 ? 280  ARG   B CA    1 
ATOM   11036 C  C     . ARG   B  1  282  ? 14.149  8.725   100.493 1.00 17.19 ? 280  ARG   B C     1 
ATOM   11037 O  O     . ARG   B  1  282  ? 14.314  8.443   101.681 1.00 17.91 ? 280  ARG   B O     1 
ATOM   11038 C  CB    . ARG   B  1  282  ? 15.854  10.259  99.506  1.00 19.00 ? 280  ARG   B CB    1 
ATOM   11039 C  CG    . ARG   B  1  282  ? 17.191  10.400  98.807  1.00 20.42 ? 280  ARG   B CG    1 
ATOM   11040 C  CD    . ARG   B  1  282  ? 17.735  11.792  99.053  1.00 20.47 ? 280  ARG   B CD    1 
ATOM   11041 N  NE    . ARG   B  1  282  ? 18.047  11.975  100.464 1.00 19.60 ? 280  ARG   B NE    1 
ATOM   11042 C  CZ    . ARG   B  1  282  ? 18.200  13.152  101.051 1.00 19.29 ? 280  ARG   B CZ    1 
ATOM   11043 N  NH1   . ARG   B  1  282  ? 18.068  14.283  100.379 1.00 20.10 ? 280  ARG   B NH1   1 
ATOM   11044 N  NH2   . ARG   B  1  282  ? 18.502  13.196  102.347 1.00 19.51 ? 280  ARG   B NH2   1 
ATOM   11045 N  N     . VAL   B  1  283  ? 12.944  8.961   99.976  1.00 16.90 ? 281  VAL   B N     1 
ATOM   11046 C  CA    . VAL   B  1  283  ? 11.745  8.816   100.795 1.00 17.36 ? 281  VAL   B CA    1 
ATOM   11047 C  C     . VAL   B  1  283  ? 11.619  7.391   101.305 1.00 17.72 ? 281  VAL   B C     1 
ATOM   11048 O  O     . VAL   B  1  283  ? 11.432  7.161   102.505 1.00 18.09 ? 281  VAL   B O     1 
ATOM   11049 C  CB    . VAL   B  1  283  ? 10.507  9.273   100.013 1.00 16.72 ? 281  VAL   B CB    1 
ATOM   11050 C  CG1   . VAL   B  1  283  ? 9.236   8.882   100.753 1.00 18.63 ? 281  VAL   B CG1   1 
ATOM   11051 C  CG2   . VAL   B  1  283  ? 10.583  10.782  99.810  1.00 17.27 ? 281  VAL   B CG2   1 
ATOM   11052 N  N     . MET   B  1  284  ? 11.754  6.412   100.411 1.00 16.90 ? 282  MET   B N     1 
ATOM   11053 C  CA    . MET   B  1  284  ? 11.605  5.033   100.842 1.00 18.86 ? 282  MET   B CA    1 
ATOM   11054 C  C     . MET   B  1  284  ? 12.766  4.601   101.718 1.00 19.26 ? 282  MET   B C     1 
ATOM   11055 O  O     . MET   B  1  284  ? 12.576  3.808   102.645 1.00 20.44 ? 282  MET   B O     1 
ATOM   11056 C  CB    . MET   B  1  284  ? 11.454  4.104   99.637  1.00 18.66 ? 282  MET   B CB    1 
ATOM   11057 C  CG    . MET   B  1  284  ? 10.255  4.425   98.766  1.00 19.96 ? 282  MET   B CG    1 
ATOM   11058 S  SD    . MET   B  1  284  ? 8.679   4.360   99.641  1.00 22.04 ? 282  MET   B SD    1 
ATOM   11059 C  CE    . MET   B  1  284  ? 8.568   2.608   99.951  1.00 24.74 ? 282  MET   B CE    1 
ATOM   11060 N  N     . GLY   B  1  285  ? 13.964  5.116   101.450 1.00 18.28 ? 283  GLY   B N     1 
ATOM   11061 C  CA    . GLY   B  1  285  ? 15.128  4.678   102.199 1.00 20.42 ? 283  GLY   B CA    1 
ATOM   11062 C  C     . GLY   B  1  285  ? 15.293  5.351   103.541 1.00 20.24 ? 283  GLY   B C     1 
ATOM   11063 O  O     . GLY   B  1  285  ? 15.847  4.751   104.466 1.00 21.83 ? 283  GLY   B O     1 
ATOM   11064 N  N     . GLU   B  1  286  ? 14.833  6.588   103.672 1.00 18.48 ? 284  GLU   B N     1 
ATOM   11065 C  CA    . GLU   B  1  286  ? 15.093  7.423   104.836 1.00 16.63 ? 284  GLU   B CA    1 
ATOM   11066 C  C     . GLU   B  1  286  ? 13.840  7.841   105.582 1.00 21.13 ? 284  GLU   B C     1 
ATOM   11067 O  O     . GLU   B  1  286  ? 13.841  7.847   106.818 1.00 23.50 ? 284  GLU   B O     1 
ATOM   11068 C  CB    . GLU   B  1  286  ? 15.851  8.691   104.421 1.00 18.86 ? 284  GLU   B CB    1 
ATOM   11069 C  CG    . GLU   B  1  286  ? 17.141  8.395   103.645 1.00 19.27 ? 284  GLU   B CG    1 
ATOM   11070 C  CD    . GLU   B  1  286  ? 17.739  9.635   102.999 1.00 24.30 ? 284  GLU   B CD    1 
ATOM   11071 O  OE1   . GLU   B  1  286  ? 17.572  10.747  103.544 1.00 23.54 ? 284  GLU   B OE1   1 
ATOM   11072 O  OE2   . GLU   B  1  286  ? 18.383  9.488   101.941 1.00 25.55 ? 284  GLU   B OE2   1 
ATOM   11073 N  N     . LEU   B  1  287  ? 12.781  8.218   104.870 1.00 19.00 ? 285  LEU   B N     1 
ATOM   11074 C  CA    . LEU   B  1  287  ? 11.550  8.625   105.534 1.00 18.26 ? 285  LEU   B CA    1 
ATOM   11075 C  C     . LEU   B  1  287  ? 10.788  7.414   106.050 1.00 20.99 ? 285  LEU   B C     1 
ATOM   11076 O  O     . LEU   B  1  287  ? 10.365  7.389   107.211 1.00 18.32 ? 285  LEU   B O     1 
ATOM   11077 C  CB    . LEU   B  1  287  ? 10.693  9.456   104.576 1.00 17.43 ? 285  LEU   B CB    1 
ATOM   11078 C  CG    . LEU   B  1  287  ? 9.663   10.438  105.155 1.00 19.73 ? 285  LEU   B CG    1 
ATOM   11079 C  CD1   . LEU   B  1  287  ? 9.059   11.249  104.049 1.00 18.62 ? 285  LEU   B CD1   1 
ATOM   11080 C  CD2   . LEU   B  1  287  ? 8.560   9.738   105.901 1.00 20.67 ? 285  LEU   B CD2   1 
ATOM   11081 N  N     . LEU   B  1  288  ? 10.604  6.403   105.204 1.00 18.60 ? 286  LEU   B N     1 
ATOM   11082 C  CA    . LEU   B  1  288  ? 9.843   5.221   105.603 1.00 18.56 ? 286  LEU   B CA    1 
ATOM   11083 C  C     . LEU   B  1  288  ? 10.327  4.588   106.901 1.00 19.44 ? 286  LEU   B C     1 
ATOM   11084 O  O     . LEU   B  1  288  ? 9.485   4.290   107.759 1.00 19.25 ? 286  LEU   B O     1 
ATOM   11085 C  CB    . LEU   B  1  288  ? 9.761   4.223   104.440 1.00 21.29 ? 286  LEU   B CB    1 
ATOM   11086 C  CG    . LEU   B  1  288  ? 9.136   2.873   104.777 1.00 22.76 ? 286  LEU   B CG    1 
ATOM   11087 C  CD1   . LEU   B  1  288  ? 7.694   3.024   105.239 1.00 21.72 ? 286  LEU   B CD1   1 
ATOM   11088 C  CD2   . LEU   B  1  288  ? 9.217   1.964   103.564 1.00 29.37 ? 286  LEU   B CD2   1 
ATOM   11089 N  N     . PRO   B  1  289  ? 11.624  4.362   107.122 1.00 19.21 ? 287  PRO   B N     1 
ATOM   11090 C  CA    . PRO   B  1  289  ? 12.034  3.779   108.412 1.00 19.62 ? 287  PRO   B CA    1 
ATOM   11091 C  C     . PRO   B  1  289  ? 11.623  4.617   109.611 1.00 18.27 ? 287  PRO   B C     1 
ATOM   11092 O  O     . PRO   B  1  289  ? 11.336  4.058   110.675 1.00 19.65 ? 287  PRO   B O     1 
ATOM   11093 C  CB    . PRO   B  1  289  ? 13.559  3.670   108.285 1.00 22.74 ? 287  PRO   B CB    1 
ATOM   11094 C  CG    . PRO   B  1  289  ? 13.784  3.539   106.800 1.00 24.21 ? 287  PRO   B CG    1 
ATOM   11095 C  CD    . PRO   B  1  289  ? 12.747  4.421   106.163 1.00 20.79 ? 287  PRO   B CD    1 
ATOM   11096 N  N     . ARG   B  1  290  ? 11.566  5.941   109.461 1.00 17.76 ? 288  ARG   B N     1 
ATOM   11097 C  CA    A ARG   B  1  290  ? 11.096  6.787   110.552 0.47 18.75 ? 288  ARG   B CA    1 
ATOM   11098 C  CA    B ARG   B  1  290  ? 11.094  6.796   110.545 0.53 18.74 ? 288  ARG   B CA    1 
ATOM   11099 C  C     . ARG   B  1  290  ? 9.619   6.560   110.830 1.00 17.07 ? 288  ARG   B C     1 
ATOM   11100 O  O     . ARG   B  1  290  ? 9.214   6.432   111.992 1.00 18.26 ? 288  ARG   B O     1 
ATOM   11101 C  CB    A ARG   B  1  290  ? 11.382  8.252   110.237 0.47 19.98 ? 288  ARG   B CB    1 
ATOM   11102 C  CB    B ARG   B  1  290  ? 11.346  8.259   110.197 0.53 19.95 ? 288  ARG   B CB    1 
ATOM   11103 C  CG    A ARG   B  1  290  ? 12.865  8.561   110.291 0.47 22.72 ? 288  ARG   B CG    1 
ATOM   11104 C  CG    B ARG   B  1  290  ? 12.819  8.615   110.193 0.53 22.75 ? 288  ARG   B CG    1 
ATOM   11105 C  CD    A ARG   B  1  290  ? 13.228  9.735   109.413 0.47 24.64 ? 288  ARG   B CD    1 
ATOM   11106 C  CD    B ARG   B  1  290  ? 13.037  10.068  109.822 0.53 23.32 ? 288  ARG   B CD    1 
ATOM   11107 N  NE    A ARG   B  1  290  ? 14.671  9.836   109.228 0.47 22.80 ? 288  ARG   B NE    1 
ATOM   11108 N  NE    B ARG   B  1  290  ? 14.267  10.590  110.405 0.53 20.94 ? 288  ARG   B NE    1 
ATOM   11109 C  CZ    A ARG   B  1  290  ? 15.255  10.647  108.356 0.47 23.09 ? 288  ARG   B CZ    1 
ATOM   11110 C  CZ    B ARG   B  1  290  ? 14.852  11.722  110.035 0.53 26.63 ? 288  ARG   B CZ    1 
ATOM   11111 N  NH1   A ARG   B  1  290  ? 14.547  11.459  107.588 0.47 18.94 ? 288  ARG   B NH1   1 
ATOM   11112 N  NH1   B ARG   B  1  290  ? 14.384  12.449  109.033 0.53 24.36 ? 288  ARG   B NH1   1 
ATOM   11113 N  NH2   A ARG   B  1  290  ? 16.580  10.640  108.250 0.47 23.77 ? 288  ARG   B NH2   1 
ATOM   11114 N  NH2   B ARG   B  1  290  ? 15.931  12.136  110.688 0.53 28.42 ? 288  ARG   B NH2   1 
ATOM   11115 N  N     . VAL   B  1  291  ? 8.799   6.494   109.781 1.00 18.52 ? 289  VAL   B N     1 
ATOM   11116 C  CA    . VAL   B  1  291  ? 7.387   6.232   110.011 1.00 17.86 ? 289  VAL   B CA    1 
ATOM   11117 C  C     . VAL   B  1  291  ? 7.206   4.861   110.629 1.00 18.52 ? 289  VAL   B C     1 
ATOM   11118 O  O     . VAL   B  1  291  ? 6.383   4.673   111.539 1.00 18.83 ? 289  VAL   B O     1 
ATOM   11119 C  CB    . VAL   B  1  291  ? 6.581   6.362   108.712 1.00 18.19 ? 289  VAL   B CB    1 
ATOM   11120 C  CG1   . VAL   B  1  291  ? 5.095   6.200   109.029 1.00 21.12 ? 289  VAL   B CG1   1 
ATOM   11121 C  CG2   . VAL   B  1  291  ? 6.840   7.689   108.068 1.00 21.85 ? 289  VAL   B CG2   1 
ATOM   11122 N  N     . LYS   B  1  292  ? 7.962   3.870   110.144 1.00 17.52 ? 290  LYS   B N     1 
ATOM   11123 C  CA    A LYS   B  1  292  ? 7.837   2.535   110.715 0.60 19.86 ? 290  LYS   B CA    1 
ATOM   11124 C  CA    B LYS   B  1  292  ? 7.857   2.531   110.709 0.40 19.88 ? 290  LYS   B CA    1 
ATOM   11125 C  C     . LYS   B  1  292  ? 8.156   2.550   112.201 1.00 18.93 ? 290  LYS   B C     1 
ATOM   11126 O  O     . LYS   B  1  292  ? 7.448   1.923   112.999 1.00 20.59 ? 290  LYS   B O     1 
ATOM   11127 C  CB    A LYS   B  1  292  ? 8.720   1.533   109.966 0.60 20.95 ? 290  LYS   B CB    1 
ATOM   11128 C  CB    B LYS   B  1  292  ? 8.808   1.587   109.969 0.40 20.97 ? 290  LYS   B CB    1 
ATOM   11129 C  CG    A LYS   B  1  292  ? 8.547   0.084   110.445 0.60 19.49 ? 290  LYS   B CG    1 
ATOM   11130 C  CG    B LYS   B  1  292  ? 9.196   0.336   110.745 0.40 22.65 ? 290  LYS   B CG    1 
ATOM   11131 C  CD    A LYS   B  1  292  ? 9.559   -0.288  111.526 0.60 24.69 ? 290  LYS   B CD    1 
ATOM   11132 C  CD    B LYS   B  1  292  ? 8.005   -0.564  111.008 0.40 21.82 ? 290  LYS   B CD    1 
ATOM   11133 C  CE    A LYS   B  1  292  ? 9.353   -1.718  112.021 0.60 27.20 ? 290  LYS   B CE    1 
ATOM   11134 C  CE    B LYS   B  1  292  ? 8.420   -1.765  111.845 0.40 29.33 ? 290  LYS   B CE    1 
ATOM   11135 N  NZ    A LYS   B  1  292  ? 9.540   -2.723  110.934 0.60 27.69 ? 290  LYS   B NZ    1 
ATOM   11136 N  NZ    B LYS   B  1  292  ? 9.396   -2.635  111.125 0.40 27.61 ? 290  LYS   B NZ    1 
ATOM   11137 N  N     . ALA   B  1  293  ? 9.206   3.266   112.594 1.00 17.95 ? 291  ALA   B N     1 
ATOM   11138 C  CA    . ALA   B  1  293  ? 9.555   3.301   114.007 1.00 19.20 ? 291  ALA   B CA    1 
ATOM   11139 C  C     . ALA   B  1  293  ? 8.442   3.933   114.829 1.00 20.89 ? 291  ALA   B C     1 
ATOM   11140 O  O     . ALA   B  1  293  ? 8.112   3.452   115.921 1.00 20.26 ? 291  ALA   B O     1 
ATOM   11141 C  CB    . ALA   B  1  293  ? 10.864  4.060   114.193 1.00 21.08 ? 291  ALA   B CB    1 
ATOM   11142 N  N     . LEU   B  1  294  ? 7.862   5.024   114.328 1.00 17.84 ? 292  LEU   B N     1 
ATOM   11143 C  CA    . LEU   B  1  294  ? 6.761   5.647   115.045 1.00 19.74 ? 292  LEU   B CA    1 
ATOM   11144 C  C     . LEU   B  1  294  ? 5.554   4.725   115.095 1.00 18.99 ? 292  LEU   B C     1 
ATOM   11145 O  O     . LEU   B  1  294  ? 4.900   4.602   116.134 1.00 19.13 ? 292  LEU   B O     1 
ATOM   11146 C  CB    . LEU   B  1  294  ? 6.384   6.974   114.393 1.00 17.69 ? 292  LEU   B CB    1 
ATOM   11147 C  CG    . LEU   B  1  294  ? 7.481   8.040   114.373 1.00 18.13 ? 292  LEU   B CG    1 
ATOM   11148 C  CD1   . LEU   B  1  294  ? 6.997   9.221   113.584 1.00 19.56 ? 292  LEU   B CD1   1 
ATOM   11149 C  CD2   . LEU   B  1  294  ? 7.872   8.447   115.800 1.00 18.80 ? 292  LEU   B CD2   1 
ATOM   11150 N  N     . ALA   B  1  295  ? 5.254   4.054   113.986 1.00 18.80 ? 293  ALA   B N     1 
ATOM   11151 C  CA    . ALA   B  1  295  ? 4.127   3.134   113.958 1.00 18.64 ? 293  ALA   B CA    1 
ATOM   11152 C  C     . ALA   B  1  295  ? 4.333   1.987   114.935 1.00 19.46 ? 293  ALA   B C     1 
ATOM   11153 O  O     . ALA   B  1  295  ? 3.393   1.558   115.613 1.00 19.70 ? 293  ALA   B O     1 
ATOM   11154 C  CB    . ALA   B  1  295  ? 3.946   2.609   112.532 1.00 19.55 ? 293  ALA   B CB    1 
ATOM   11155 N  N     . LEU   B  1  296  ? 5.566   1.494   115.041 1.00 19.37 ? 294  LEU   B N     1 
ATOM   11156 C  CA    . LEU   B  1  296  ? 5.843   0.416   115.978 1.00 20.60 ? 294  LEU   B CA    1 
ATOM   11157 C  C     . LEU   B  1  296  ? 5.600   0.875   117.406 1.00 20.22 ? 294  LEU   B C     1 
ATOM   11158 O  O     . LEU   B  1  296  ? 5.025   0.138   118.215 1.00 20.97 ? 294  LEU   B O     1 
ATOM   11159 C  CB    . LEU   B  1  296  ? 7.277   -0.062  115.785 1.00 23.51 ? 294  LEU   B CB    1 
ATOM   11160 C  CG    . LEU   B  1  296  ? 7.729   -1.257  116.622 1.00 28.36 ? 294  LEU   B CG    1 
ATOM   11161 C  CD1   . LEU   B  1  296  ? 6.784   -2.450  116.430 1.00 29.13 ? 294  LEU   B CD1   1 
ATOM   11162 C  CD2   . LEU   B  1  296  ? 9.164   -1.627  116.257 1.00 31.48 ? 294  LEU   B CD2   1 
ATOM   11163 N  N     . LEU   B  1  297  ? 6.008   2.101   117.732 1.00 20.15 ? 295  LEU   B N     1 
ATOM   11164 C  CA    . LEU   B  1  297  ? 5.693   2.642   119.051 1.00 22.38 ? 295  LEU   B CA    1 
ATOM   11165 C  C     . LEU   B  1  297  ? 4.187   2.735   119.256 1.00 20.55 ? 295  LEU   B C     1 
ATOM   11166 O  O     . LEU   B  1  297  ? 3.662   2.349   120.309 1.00 20.73 ? 295  LEU   B O     1 
ATOM   11167 C  CB    . LEU   B  1  297  ? 6.335   4.018   119.211 1.00 21.32 ? 295  LEU   B CB    1 
ATOM   11168 C  CG    . LEU   B  1  297  ? 7.848   4.089   119.402 1.00 27.89 ? 295  LEU   B CG    1 
ATOM   11169 C  CD1   . LEU   B  1  297  ? 8.287   5.550   119.450 1.00 25.52 ? 295  LEU   B CD1   1 
ATOM   11170 C  CD2   . LEU   B  1  297  ? 8.266   3.352   120.659 1.00 30.83 ? 295  LEU   B CD2   1 
ATOM   11171 N  N     . ALA   B  1  298  ? 3.467   3.255   118.262 1.00 20.90 ? 296  ALA   B N     1 
ATOM   11172 C  CA    . ALA   B  1  298  ? 2.018   3.363   118.398 1.00 19.44 ? 296  ALA   B CA    1 
ATOM   11173 C  C     . ALA   B  1  298  ? 1.389   1.993   118.567 1.00 22.91 ? 296  ALA   B C     1 
ATOM   11174 O  O     . ALA   B  1  298  ? 0.473   1.811   119.377 1.00 23.27 ? 296  ALA   B O     1 
ATOM   11175 C  CB    . ALA   B  1  298  ? 1.428   4.063   117.175 1.00 20.32 ? 296  ALA   B CB    1 
ATOM   11176 N  N     . LYS   B  1  299  ? 1.864   1.018   117.795 1.00 21.38 ? 297  LYS   B N     1 
ATOM   11177 C  CA    A LYS   B  1  299  ? 1.371   -0.345  117.938 0.50 21.14 ? 297  LYS   B CA    1 
ATOM   11178 C  CA    B LYS   B  1  299  ? 1.369   -0.344  117.942 0.50 21.14 ? 297  LYS   B CA    1 
ATOM   11179 C  C     . LYS   B  1  299  ? 1.596   -0.861  119.352 1.00 24.60 ? 297  LYS   B C     1 
ATOM   11180 O  O     . LYS   B  1  299  ? 0.707   -1.487  119.944 1.00 25.03 ? 297  LYS   B O     1 
ATOM   11181 C  CB    A LYS   B  1  299  ? 2.067   -1.244  116.917 0.50 25.39 ? 297  LYS   B CB    1 
ATOM   11182 C  CB    B LYS   B  1  299  ? 2.066   -1.265  116.945 0.50 25.39 ? 297  LYS   B CB    1 
ATOM   11183 C  CG    A LYS   B  1  299  ? 1.663   -2.705  116.984 0.50 27.11 ? 297  LYS   B CG    1 
ATOM   11184 C  CG    B LYS   B  1  299  ? 1.779   -2.733  117.202 0.50 26.87 ? 297  LYS   B CG    1 
ATOM   11185 C  CD    A LYS   B  1  299  ? 2.733   -3.549  117.648 0.50 25.33 ? 297  LYS   B CD    1 
ATOM   11186 C  CD    B LYS   B  1  299  ? 2.800   -3.618  116.527 0.50 29.40 ? 297  LYS   B CD    1 
ATOM   11187 C  CE    A LYS   B  1  299  ? 2.315   -5.011  117.714 0.50 29.09 ? 297  LYS   B CE    1 
ATOM   11188 C  CE    B LYS   B  1  299  ? 2.445   -5.084  116.679 0.50 30.93 ? 297  LYS   B CE    1 
ATOM   11189 N  NZ    A LYS   B  1  299  ? 2.135   -5.609  116.363 0.50 33.71 ? 297  LYS   B NZ    1 
ATOM   11190 N  NZ    B LYS   B  1  299  ? 2.501   -5.553  118.086 0.50 31.15 ? 297  LYS   B NZ    1 
ATOM   11191 N  N     . ASN   B  1  300  ? 2.780   -0.614  119.906 1.00 22.27 ? 298  ASN   B N     1 
ATOM   11192 C  CA    . ASN   B  1  300  ? 3.086   -1.159  121.221 1.00 25.59 ? 298  ASN   B CA    1 
ATOM   11193 C  C     . ASN   B  1  300  ? 2.165   -0.592  122.287 1.00 25.97 ? 298  ASN   B C     1 
ATOM   11194 O  O     . ASN   B  1  300  ? 1.816   -1.298  123.239 1.00 26.91 ? 298  ASN   B O     1 
ATOM   11195 C  CB    . ASN   B  1  300  ? 4.562   -0.941  121.559 1.00 26.32 ? 298  ASN   B CB    1 
ATOM   11196 C  CG    . ASN   B  1  300  ? 5.479   -1.837  120.732 1.00 29.84 ? 298  ASN   B CG    1 
ATOM   11197 O  OD1   . ASN   B  1  300  ? 5.066   -2.899  120.269 1.00 35.65 ? 298  ASN   B OD1   1 
ATOM   11198 N  ND2   . ASN   B  1  300  ? 6.724   -1.412  120.549 1.00 40.09 ? 298  ASN   B ND2   1 
ATOM   11199 N  N     . TYR   B  1  301  ? 1.731   0.654   122.129 1.00 22.80 ? 299  TYR   B N     1 
ATOM   11200 C  CA    . TYR   B  1  301  ? 0.763   1.248   123.039 1.00 24.49 ? 299  TYR   B CA    1 
ATOM   11201 C  C     . TYR   B  1  301  ? -0.672  1.025   122.599 1.00 20.63 ? 299  TYR   B C     1 
ATOM   11202 O  O     . TYR   B  1  301  ? -1.587  1.417   123.328 1.00 23.14 ? 299  TYR   B O     1 
ATOM   11203 C  CB    . TYR   B  1  301  ? 0.994   2.753   123.147 1.00 21.91 ? 299  TYR   B CB    1 
ATOM   11204 C  CG    . TYR   B  1  301  ? 2.240   3.147   123.898 1.00 22.40 ? 299  TYR   B CG    1 
ATOM   11205 C  CD1   . TYR   B  1  301  ? 2.322   2.982   125.274 1.00 22.15 ? 299  TYR   B CD1   1 
ATOM   11206 C  CD2   . TYR   B  1  301  ? 3.320   3.706   123.238 1.00 22.37 ? 299  TYR   B CD2   1 
ATOM   11207 C  CE1   . TYR   B  1  301  ? 3.466   3.352   125.972 1.00 22.12 ? 299  TYR   B CE1   1 
ATOM   11208 C  CE2   . TYR   B  1  301  ? 4.461   4.084   123.918 1.00 21.30 ? 299  TYR   B CE2   1 
ATOM   11209 C  CZ    . TYR   B  1  301  ? 4.521   3.908   125.282 1.00 21.22 ? 299  TYR   B CZ    1 
ATOM   11210 O  OH    . TYR   B  1  301  ? 5.653   4.283   125.952 1.00 23.34 ? 299  TYR   B OH    1 
ATOM   11211 N  N     . ASP   B  1  302  ? -0.878  0.419   121.432 1.00 21.15 ? 300  ASP   B N     1 
ATOM   11212 C  CA    . ASP   B  1  302  ? -2.186  0.246   120.809 1.00 23.28 ? 300  ASP   B CA    1 
ATOM   11213 C  C     . ASP   B  1  302  ? -2.959  1.561   120.718 1.00 20.60 ? 300  ASP   B C     1 
ATOM   11214 O  O     . ASP   B  1  302  ? -4.083  1.692   121.200 1.00 22.57 ? 300  ASP   B O     1 
ATOM   11215 C  CB    . ASP   B  1  302  ? -3.017  -0.853  121.470 1.00 22.59 ? 300  ASP   B CB    1 
ATOM   11216 C  CG    . ASP   B  1  302  ? -4.113  -1.366  120.546 1.00 26.66 ? 300  ASP   B CG    1 
ATOM   11217 O  OD1   . ASP   B  1  302  ? -3.907  -1.346  119.304 1.00 27.72 ? 300  ASP   B OD1   1 
ATOM   11218 O  OD2   . ASP   B  1  302  ? -5.183  -1.756  121.051 1.00 32.32 ? 300  ASP   B OD2   1 
ATOM   11219 N  N     . ILE   B  1  303  ? -2.330  2.542   120.075 1.00 20.15 ? 301  ILE   B N     1 
ATOM   11220 C  CA    . ILE   B  1  303  ? -2.994  3.795   119.748 1.00 19.43 ? 301  ILE   B CA    1 
ATOM   11221 C  C     . ILE   B  1  303  ? -3.043  3.923   118.235 1.00 21.01 ? 301  ILE   B C     1 
ATOM   11222 O  O     . ILE   B  1  303  ? -2.325  3.238   117.501 1.00 20.87 ? 301  ILE   B O     1 
ATOM   11223 C  CB    . ILE   B  1  303  ? -2.304  5.032   120.369 1.00 18.90 ? 301  ILE   B CB    1 
ATOM   11224 C  CG1   . ILE   B  1  303  ? -0.948  5.277   119.703 1.00 21.01 ? 301  ILE   B CG1   1 
ATOM   11225 C  CG2   . ILE   B  1  303  ? -2.128  4.867   121.852 1.00 20.97 ? 301  ILE   B CG2   1 
ATOM   11226 C  CD1   . ILE   B  1  303  ? -0.299  6.617   120.091 1.00 23.54 ? 301  ILE   B CD1   1 
ATOM   11227 N  N     . GLY   B  1  304  ? -3.894  4.835   117.774 1.00 17.81 ? 302  GLY   B N     1 
ATOM   11228 C  CA    . GLY   B  1  304  ? -3.936  5.154   116.355 1.00 19.38 ? 302  GLY   B CA    1 
ATOM   11229 C  C     . GLY   B  1  304  ? -2.792  6.078   115.959 1.00 20.28 ? 302  GLY   B C     1 
ATOM   11230 O  O     . GLY   B  1  304  ? -2.387  6.969   116.708 1.00 20.38 ? 302  GLY   B O     1 
ATOM   11231 N  N     . LEU   B  1  305  ? -2.255  5.843   114.767 1.00 16.94 ? 303  LEU   B N     1 
ATOM   11232 C  CA    . LEU   B  1  305  ? -1.273  6.737   114.173 1.00 18.37 ? 303  LEU   B CA    1 
ATOM   11233 C  C     . LEU   B  1  305  ? -1.751  7.021   112.766 1.00 18.34 ? 303  LEU   B C     1 
ATOM   11234 O  O     . LEU   B  1  305  ? -1.806  6.108   111.935 1.00 18.72 ? 303  LEU   B O     1 
ATOM   11235 C  CB    . LEU   B  1  305  ? 0.125   6.113   114.143 1.00 19.49 ? 303  LEU   B CB    1 
ATOM   11236 C  CG    . LEU   B  1  305  ? 1.195   7.042   113.552 1.00 19.35 ? 303  LEU   B CG    1 
ATOM   11237 C  CD1   . LEU   B  1  305  ? 2.495   6.925   114.297 1.00 22.88 ? 303  LEU   B CD1   1 
ATOM   11238 C  CD2   . LEU   B  1  305  ? 1.437   6.732   112.090 1.00 22.88 ? 303  LEU   B CD2   1 
ATOM   11239 N  N     . ASN   B  1  306  ? -2.059  8.279   112.501 1.00 17.18 ? 304  ASN   B N     1 
ATOM   11240 C  CA    . ASN   B  1  306  ? -2.689  8.697   111.264 1.00 16.75 ? 304  ASN   B CA    1 
ATOM   11241 C  C     . ASN   B  1  306  ? -1.712  9.507   110.432 1.00 16.89 ? 304  ASN   B C     1 
ATOM   11242 O  O     . ASN   B  1  306  ? -1.027  10.391  110.954 1.00 17.06 ? 304  ASN   B O     1 
ATOM   11243 C  CB    . ASN   B  1  306  ? -3.895  9.579   111.569 1.00 18.07 ? 304  ASN   B CB    1 
ATOM   11244 C  CG    . ASN   B  1  306  ? -4.486  10.157  110.335 1.00 17.97 ? 304  ASN   B CG    1 
ATOM   11245 O  OD1   . ASN   B  1  306  ? -5.218  9.475   109.614 1.00 21.08 ? 304  ASN   B OD1   1 
ATOM   11246 N  ND2   . ASN   B  1  306  ? -4.137  11.401  110.028 1.00 18.94 ? 304  ASN   B ND2   1 
ATOM   11247 N  N     . ILE   B  1  307  ? -1.671  9.210   109.141 1.00 17.29 ? 305  ILE   B N     1 
ATOM   11248 C  CA    . ILE   B  1  307  ? -0.890  9.986   108.189 1.00 16.23 ? 305  ILE   B CA    1 
ATOM   11249 C  C     . ILE   B  1  307  ? -1.807  11.023  107.554 1.00 18.13 ? 305  ILE   B C     1 
ATOM   11250 O  O     . ILE   B  1  307  ? -2.716  10.684  106.786 1.00 16.38 ? 305  ILE   B O     1 
ATOM   11251 C  CB    . ILE   B  1  307  ? -0.265  9.093   107.113 1.00 16.91 ? 305  ILE   B CB    1 
ATOM   11252 C  CG1   . ILE   B  1  307  ? 0.687   8.100   107.766 1.00 19.72 ? 305  ILE   B CG1   1 
ATOM   11253 C  CG2   . ILE   B  1  307  ? 0.429   9.951   106.048 1.00 19.53 ? 305  ILE   B CG2   1 
ATOM   11254 C  CD1   . ILE   B  1  307  ? 1.276   7.147   106.749 1.00 20.69 ? 305  ILE   B CD1   1 
ATOM   11255 N  N     . ASP   B  1  308  ? -1.569  12.290  107.867 1.00 16.45 ? 306  ASP   B N     1 
ATOM   11256 C  CA    . ASP   B  1  308  ? -2.338  13.373  107.280 1.00 17.07 ? 306  ASP   B CA    1 
ATOM   11257 C  C     . ASP   B  1  308  ? -2.042  13.461  105.792 1.00 16.61 ? 306  ASP   B C     1 
ATOM   11258 O  O     . ASP   B  1  308  ? -0.954  13.106  105.334 1.00 17.75 ? 306  ASP   B O     1 
ATOM   11259 C  CB    . ASP   B  1  308  ? -1.949  14.703  107.930 1.00 17.19 ? 306  ASP   B CB    1 
ATOM   11260 C  CG    . ASP   B  1  308  ? -2.431  14.833  109.370 1.00 18.70 ? 306  ASP   B CG    1 
ATOM   11261 O  OD1   . ASP   B  1  308  ? -3.249  14.016  109.833 1.00 18.77 ? 306  ASP   B OD1   1 
ATOM   11262 O  OD2   . ASP   B  1  308  ? -1.970  15.777  110.052 1.00 19.81 ? 306  ASP   B OD2   1 
ATOM   11263 N  N     . ALA   B  1  309  ? -3.010  13.953  105.030 1.00 15.05 ? 307  ALA   B N     1 
ATOM   11264 C  CA    . ALA   B  1  309  ? -2.850  14.072  103.589 1.00 15.59 ? 307  ALA   B CA    1 
ATOM   11265 C  C     . ALA   B  1  309  ? -2.433  15.485  103.238 1.00 15.01 ? 307  ALA   B C     1 
ATOM   11266 O  O     . ALA   B  1  309  ? -2.944  16.454  103.805 1.00 16.86 ? 307  ALA   B O     1 
ATOM   11267 C  CB    . ALA   B  1  309  ? -4.161  13.741  102.885 1.00 16.18 ? 307  ALA   B CB    1 
ATOM   11268 N  N     . GLU   B  1  310  ? -1.464  15.595  102.336 1.00 14.79 ? 308  GLU   B N     1 
ATOM   11269 C  CA    . GLU   B  1  310  ? -0.889  16.898  102.025 1.00 14.86 ? 308  GLU   B CA    1 
ATOM   11270 C  C     . GLU   B  1  310  ? -1.167  17.294  100.578 1.00 14.29 ? 308  GLU   B C     1 
ATOM   11271 O  O     . GLU   B  1  310  ? -2.301  17.144  100.112 1.00 14.67 ? 308  GLU   B O     1 
ATOM   11272 C  CB    . GLU   B  1  310  ? 0.593   16.910  102.414 1.00 15.54 ? 308  GLU   B CB    1 
ATOM   11273 C  CG    . GLU   B  1  310  ? 0.770   16.593  103.899 1.00 17.14 ? 308  GLU   B CG    1 
ATOM   11274 C  CD    . GLU   B  1  310  ? 2.207   16.694  104.360 1.00 18.08 ? 308  GLU   B CD    1 
ATOM   11275 O  OE1   . GLU   B  1  310  ? 2.681   17.832  104.498 1.00 19.10 ? 308  GLU   B OE1   1 
ATOM   11276 O  OE2   . GLU   B  1  310  ? 2.839   15.641  104.596 1.00 17.75 ? 308  GLU   B OE2   1 
ATOM   11277 N  N     . GLU   B  1  311  ? -0.173  17.791  99.856  1.00 15.18 ? 309  GLU   B N     1 
ATOM   11278 C  CA    . GLU   B  1  311  ? -0.439  18.269  98.510  1.00 14.16 ? 309  GLU   B CA    1 
ATOM   11279 C  C     . GLU   B  1  311  ? -0.745  17.106  97.574  1.00 14.80 ? 309  GLU   B C     1 
ATOM   11280 O  O     . GLU   B  1  311  ? -0.386  15.952  97.830  1.00 15.51 ? 309  GLU   B O     1 
ATOM   11281 C  CB    . GLU   B  1  311  ? 0.774   19.034  97.976  1.00 14.75 ? 309  GLU   B CB    1 
ATOM   11282 C  CG    . GLU   B  1  311  ? 1.075   20.321  98.747  1.00 17.67 ? 309  GLU   B CG    1 
ATOM   11283 C  CD    . GLU   B  1  311  ? 2.022   20.135  99.912  1.00 20.93 ? 309  GLU   B CD    1 
ATOM   11284 O  OE1   . GLU   B  1  311  ? 2.194   19.001  100.418 1.00 17.67 ? 309  GLU   B OE1   1 
ATOM   11285 O  OE2   . GLU   B  1  311  ? 2.612   21.159  100.331 1.00 25.99 ? 309  GLU   B OE2   1 
ATOM   11286 N  N     . ALA   B  1  312  ? -1.438  17.430  96.473  1.00 14.49 ? 310  ALA   B N     1 
ATOM   11287 C  CA    . ALA   B  1  312  ? -1.870  16.395  95.547  1.00 15.84 ? 310  ALA   B CA    1 
ATOM   11288 C  C     . ALA   B  1  312  ? -0.697  15.609  94.988  1.00 14.13 ? 310  ALA   B C     1 
ATOM   11289 O  O     . ALA   B  1  312  ? -0.825  14.405  94.759  1.00 15.33 ? 310  ALA   B O     1 
ATOM   11290 C  CB    . ALA   B  1  312  ? -2.659  17.024  94.398  1.00 15.71 ? 310  ALA   B CB    1 
ATOM   11291 N  N     . ASP   B  1  313  ? 0.460   16.255  94.798  1.00 14.99 ? 311  ASP   B N     1 
ATOM   11292 C  CA    . ASP   B  1  313  ? 1.600   15.534  94.236  1.00 14.40 ? 311  ASP   B CA    1 
ATOM   11293 C  C     . ASP   B  1  313  ? 2.306   14.634  95.236  1.00 16.39 ? 311  ASP   B C     1 
ATOM   11294 O  O     . ASP   B  1  313  ? 3.307   14.013  94.875  1.00 16.15 ? 311  ASP   B O     1 
ATOM   11295 C  CB    . ASP   B  1  313  ? 2.582   16.456  93.492  1.00 16.82 ? 311  ASP   B CB    1 
ATOM   11296 C  CG    . ASP   B  1  313  ? 3.274   17.462  94.384  1.00 18.91 ? 311  ASP   B CG    1 
ATOM   11297 O  OD1   . ASP   B  1  313  ? 3.124   17.427  95.623  1.00 19.18 ? 311  ASP   B OD1   1 
ATOM   11298 O  OD2   . ASP   B  1  313  ? 4.010   18.307  93.816  1.00 21.59 ? 311  ASP   B OD2   1 
ATOM   11299 N  N     . ARG   B  1  314  ? 1.807   14.543  96.463  1.00 15.07 ? 312  ARG   B N     1 
ATOM   11300 C  CA    . ARG   B  1  314  ? 2.341   13.614  97.450  1.00 15.56 ? 312  ARG   B CA    1 
ATOM   11301 C  C     . ARG   B  1  314  ? 1.403   12.452  97.717  1.00 15.24 ? 312  ARG   B C     1 
ATOM   11302 O  O     . ARG   B  1  314  ? 1.783   11.515  98.418  1.00 16.38 ? 312  ARG   B O     1 
ATOM   11303 C  CB    . ARG   B  1  314  ? 2.633   14.360  98.759  1.00 15.56 ? 312  ARG   B CB    1 
ATOM   11304 C  CG    . ARG   B  1  314  ? 3.899   15.178  98.633  1.00 15.49 ? 312  ARG   B CG    1 
ATOM   11305 C  CD    . ARG   B  1  314  ? 3.977   16.255  99.700  1.00 16.46 ? 312  ARG   B CD    1 
ATOM   11306 N  NE    . ARG   B  1  314  ? 5.347   16.740  99.833  1.00 17.25 ? 312  ARG   B NE    1 
ATOM   11307 C  CZ    . ARG   B  1  314  ? 5.705   17.752  100.604 1.00 16.49 ? 312  ARG   B CZ    1 
ATOM   11308 N  NH1   . ARG   B  1  314  ? 4.809   18.492  101.238 1.00 17.48 ? 312  ARG   B NH1   1 
ATOM   11309 N  NH2   . ARG   B  1  314  ? 7.001   18.004  100.778 1.00 18.52 ? 312  ARG   B NH2   1 
ATOM   11310 N  N     . LEU   B  1  315  ? 0.195   12.485  97.160  1.00 15.41 ? 313  LEU   B N     1 
ATOM   11311 C  CA    . LEU   B  1  315  ? -0.791  11.460  97.466  1.00 16.41 ? 313  LEU   B CA    1 
ATOM   11312 C  C     . LEU   B  1  315  ? -0.267  10.072  97.108  1.00 17.04 ? 313  LEU   B C     1 
ATOM   11313 O  O     . LEU   B  1  315  ? -0.200  9.177   97.960  1.00 16.19 ? 313  LEU   B O     1 
ATOM   11314 C  CB    . LEU   B  1  315  ? -2.085  11.771  96.715  1.00 15.63 ? 313  LEU   B CB    1 
ATOM   11315 C  CG    . LEU   B  1  315  ? -3.363  11.107  97.207  1.00 16.73 ? 313  LEU   B CG    1 
ATOM   11316 C  CD1   . LEU   B  1  315  ? -4.522  11.612  96.379  1.00 17.99 ? 313  LEU   B CD1   1 
ATOM   11317 C  CD2   . LEU   B  1  315  ? -3.334  9.578   97.155  1.00 20.94 ? 313  LEU   B CD2   1 
ATOM   11318 N  N     . GLU   B  1  316  ? 0.093   9.861   95.843  1.00 15.94 ? 314  GLU   B N     1 
ATOM   11319 C  CA    . GLU   B  1  316  ? 0.444   8.508   95.432  1.00 16.29 ? 314  GLU   B CA    1 
ATOM   11320 C  C     . GLU   B  1  316  ? 1.746   8.043   96.068  1.00 17.36 ? 314  GLU   B C     1 
ATOM   11321 O  O     . GLU   B  1  316  ? 1.873   6.876   96.450  1.00 17.71 ? 314  GLU   B O     1 
ATOM   11322 C  CB    . GLU   B  1  316  ? 0.458   8.412   93.912  1.00 16.25 ? 314  GLU   B CB    1 
ATOM   11323 C  CG    . GLU   B  1  316  ? -0.960  8.561   93.367  1.00 16.01 ? 314  GLU   B CG    1 
ATOM   11324 C  CD    . GLU   B  1  316  ? -1.053  8.455   91.856  1.00 19.95 ? 314  GLU   B CD    1 
ATOM   11325 O  OE1   . GLU   B  1  316  ? -0.408  7.558   91.274  1.00 19.26 ? 314  GLU   B OE1   1 
ATOM   11326 O  OE2   . GLU   B  1  316  ? -1.800  9.252   91.255  1.00 18.52 ? 314  GLU   B OE2   1 
ATOM   11327 N  N     . LEU   B  1  317  ? 2.704   8.949   96.237  1.00 17.00 ? 315  LEU   B N     1 
ATOM   11328 C  CA    . LEU   B  1  317  ? 3.919   8.596   96.964  1.00 18.61 ? 315  LEU   B CA    1 
ATOM   11329 C  C     . LEU   B  1  317  ? 3.601   8.092   98.365  1.00 17.53 ? 315  LEU   B C     1 
ATOM   11330 O  O     . LEU   B  1  317  ? 4.156   7.082   98.812  1.00 19.10 ? 315  LEU   B O     1 
ATOM   11331 C  CB    . LEU   B  1  317  ? 4.842   9.805   97.014  1.00 20.31 ? 315  LEU   B CB    1 
ATOM   11332 C  CG    . LEU   B  1  317  ? 6.145   9.598   97.772  1.00 20.75 ? 315  LEU   B CG    1 
ATOM   11333 C  CD1   . LEU   B  1  317  ? 6.926   8.406   97.216  1.00 23.76 ? 315  LEU   B CD1   1 
ATOM   11334 C  CD2   . LEU   B  1  317  ? 6.967   10.864  97.690  1.00 22.13 ? 315  LEU   B CD2   1 
ATOM   11335 N  N     . SER   B  1  318  ? 2.662   8.743   99.057  1.00 16.34 ? 316  SER   B N     1 
ATOM   11336 C  CA    . SER   B  1  318  ? 2.316   8.289   100.402 1.00 16.41 ? 316  SER   B CA    1 
ATOM   11337 C  C     . SER   B  1  318  ? 1.746   6.872   100.397 1.00 16.82 ? 316  SER   B C     1 
ATOM   11338 O  O     . SER   B  1  318  ? 1.931   6.132   101.370 1.00 17.48 ? 316  SER   B O     1 
ATOM   11339 C  CB    . SER   B  1  318  ? 1.348   9.265   101.080 1.00 17.71 ? 316  SER   B CB    1 
ATOM   11340 O  OG    . SER   B  1  318  ? 0.051   9.160   100.526 1.00 17.50 ? 316  SER   B OG    1 
ATOM   11341 N  N     . LEU   B  1  319  ? 1.075   6.468   99.315  1.00 16.39 ? 317  LEU   B N     1 
ATOM   11342 C  CA    . LEU   B  1  319  ? 0.536   5.116   99.252  1.00 16.74 ? 317  LEU   B CA    1 
ATOM   11343 C  C     . LEU   B  1  319  ? 1.634   4.068   99.239  1.00 17.71 ? 317  LEU   B C     1 
ATOM   11344 O  O     . LEU   B  1  319  ? 1.422   2.947   99.719  1.00 18.29 ? 317  LEU   B O     1 
ATOM   11345 C  CB    . LEU   B  1  319  ? -0.325  4.951   98.003  1.00 16.77 ? 317  LEU   B CB    1 
ATOM   11346 C  CG    . LEU   B  1  319  ? -1.552  5.857   97.915  1.00 16.43 ? 317  LEU   B CG    1 
ATOM   11347 C  CD1   . LEU   B  1  319  ? -2.192  5.638   96.544  1.00 17.98 ? 317  LEU   B CD1   1 
ATOM   11348 C  CD2   . LEU   B  1  319  ? -2.542  5.583   99.029  1.00 21.22 ? 317  LEU   B CD2   1 
ATOM   11349 N  N     . ASP   B  1  320  ? 2.797   4.397   98.682  1.00 18.87 ? 318  ASP   B N     1 
ATOM   11350 C  CA    . ASP   B  1  320  ? 3.893   3.442   98.714  1.00 20.38 ? 318  ASP   B CA    1 
ATOM   11351 C  C     . ASP   B  1  320  ? 4.369   3.185   100.131 1.00 18.83 ? 318  ASP   B C     1 
ATOM   11352 O  O     . ASP   B  1  320  ? 4.795   2.072   100.447 1.00 22.10 ? 318  ASP   B O     1 
ATOM   11353 C  CB    . ASP   B  1  320  ? 5.019   3.933   97.829  1.00 20.27 ? 318  ASP   B CB    1 
ATOM   11354 C  CG    . ASP   B  1  320  ? 4.699   3.735   96.385  1.00 19.28 ? 318  ASP   B CG    1 
ATOM   11355 O  OD1   . ASP   B  1  320  ? 4.385   2.587   96.017  1.00 22.04 ? 318  ASP   B OD1   1 
ATOM   11356 O  OD2   . ASP   B  1  320  ? 4.708   4.716   95.623  1.00 22.27 ? 318  ASP   B OD2   1 
ATOM   11357 N  N     . LEU   B  1  321  ? 4.301   4.192   100.998 1.00 16.79 ? 319  LEU   B N     1 
ATOM   11358 C  CA    . LEU   B  1  321  ? 4.634   3.961   102.395 1.00 19.74 ? 319  LEU   B CA    1 
ATOM   11359 C  C     . LEU   B  1  321  ? 3.537   3.184   103.095 1.00 19.03 ? 319  LEU   B C     1 
ATOM   11360 O  O     . LEU   B  1  321  ? 3.818   2.252   103.857 1.00 20.91 ? 319  LEU   B O     1 
ATOM   11361 C  CB    . LEU   B  1  321  ? 4.894   5.287   103.111 1.00 19.87 ? 319  LEU   B CB    1 
ATOM   11362 C  CG    . LEU   B  1  321  ? 6.243   5.928   102.785 1.00 19.72 ? 319  LEU   B CG    1 
ATOM   11363 C  CD1   . LEU   B  1  321  ? 6.177   6.770   101.518 1.00 22.44 ? 319  LEU   B CD1   1 
ATOM   11364 C  CD2   . LEU   B  1  321  ? 6.735   6.754   103.963 1.00 21.73 ? 319  LEU   B CD2   1 
ATOM   11365 N  N     . LEU   B  1  322  ? 2.282   3.554   102.858 1.00 18.69 ? 320  LEU   B N     1 
ATOM   11366 C  CA    . LEU   B  1  322  ? 1.187   2.831   103.488 1.00 19.50 ? 320  LEU   B CA    1 
ATOM   11367 C  C     . LEU   B  1  322  ? 1.253   1.352   103.156 1.00 19.30 ? 320  LEU   B C     1 
ATOM   11368 O  O     . LEU   B  1  322  ? 1.010   0.501   104.025 1.00 20.21 ? 320  LEU   B O     1 
ATOM   11369 C  CB    . LEU   B  1  322  ? -0.142  3.408   103.016 1.00 18.48 ? 320  LEU   B CB    1 
ATOM   11370 C  CG    . LEU   B  1  322  ? -1.386  2.750   103.605 1.00 19.04 ? 320  LEU   B CG    1 
ATOM   11371 C  CD1   . LEU   B  1  322  ? -1.426  3.016   105.099 1.00 20.99 ? 320  LEU   B CD1   1 
ATOM   11372 C  CD2   . LEU   B  1  322  ? -2.639  3.273   102.913 1.00 18.99 ? 320  LEU   B CD2   1 
ATOM   11373 N  N     . GLU   B  1  323  ? 1.571   1.028   101.897 1.00 20.12 ? 321  GLU   B N     1 
ATOM   11374 C  CA    . GLU   B  1  323  ? 1.661   -0.361  101.465 1.00 20.29 ? 321  GLU   B CA    1 
ATOM   11375 C  C     . GLU   B  1  323  ? 2.687   -1.128  102.286 1.00 19.42 ? 321  GLU   B C     1 
ATOM   11376 O  O     . GLU   B  1  323  ? 2.401   -2.219  102.787 1.00 22.81 ? 321  GLU   B O     1 
ATOM   11377 C  CB    . GLU   B  1  323  ? 2.021   -0.411  99.981  1.00 23.60 ? 321  GLU   B CB    1 
ATOM   11378 C  CG    . GLU   B  1  323  ? 2.356   -1.801  99.454  1.00 28.18 ? 321  GLU   B CG    1 
ATOM   11379 C  CD    . GLU   B  1  323  ? 1.165   -2.491  98.821  1.00 29.34 ? 321  GLU   B CD    1 
ATOM   11380 O  OE1   . GLU   B  1  323  ? 0.142   -1.810  98.588  1.00 27.71 ? 321  GLU   B OE1   1 
ATOM   11381 O  OE2   . GLU   B  1  323  ? 1.243   -3.714  98.567  1.00 27.21 ? 321  GLU   B OE2   1 
ATOM   11382 N  N     . VAL   B  1  324  ? 3.891   -0.567  102.438 1.00 18.63 ? 322  VAL   B N     1 
ATOM   11383 C  CA    . VAL   B  1  324  ? 4.927   -1.247  103.210 1.00 21.22 ? 322  VAL   B CA    1 
ATOM   11384 C  C     . VAL   B  1  324  ? 4.481   -1.433  104.654 1.00 18.43 ? 322  VAL   B C     1 
ATOM   11385 O  O     . VAL   B  1  324  ? 4.617   -2.519  105.230 1.00 21.78 ? 322  VAL   B O     1 
ATOM   11386 C  CB    . VAL   B  1  324  ? 6.262   -0.487  103.120 1.00 20.90 ? 322  VAL   B CB    1 
ATOM   11387 C  CG1   . VAL   B  1  324  ? 7.289   -1.112  104.056 1.00 22.79 ? 322  VAL   B CG1   1 
ATOM   11388 C  CG2   . VAL   B  1  324  ? 6.767   -0.476  101.689 1.00 22.97 ? 322  VAL   B CG2   1 
ATOM   11389 N  N     . LEU   B  1  325  ? 3.933   -0.382  105.260 1.00 19.77 ? 323  LEU   B N     1 
ATOM   11390 C  CA    . LEU   B  1  325  ? 3.555   -0.471  106.665 1.00 21.55 ? 323  LEU   B CA    1 
ATOM   11391 C  C     . LEU   B  1  325  ? 2.493   -1.537  106.888 1.00 19.46 ? 323  LEU   B C     1 
ATOM   11392 O  O     . LEU   B  1  325  ? 2.556   -2.292  107.862 1.00 20.45 ? 323  LEU   B O     1 
ATOM   11393 C  CB    . LEU   B  1  325  ? 3.077   0.893   107.162 1.00 20.44 ? 323  LEU   B CB    1 
ATOM   11394 C  CG    . LEU   B  1  325  ? 4.180   1.945   107.104 1.00 22.02 ? 323  LEU   B CG    1 
ATOM   11395 C  CD1   . LEU   B  1  325  ? 3.602   3.331   107.283 1.00 24.17 ? 323  LEU   B CD1   1 
ATOM   11396 C  CD2   . LEU   B  1  325  ? 5.216   1.645   108.171 1.00 21.56 ? 323  LEU   B CD2   1 
ATOM   11397 N  N     . CYS   B  1  326  ? 1.512   -1.628  105.984 1.00 21.05 ? 324  CYS   B N     1 
ATOM   11398 C  CA    . CYS   B  1  326  ? 0.450   -2.614  106.149 1.00 19.88 ? 324  CYS   B CA    1 
ATOM   11399 C  C     . CYS   B  1  326  ? 0.939   -4.043  105.943 1.00 21.35 ? 324  CYS   B C     1 
ATOM   11400 O  O     . CYS   B  1  326  ? 0.312   -4.973  106.457 1.00 21.15 ? 324  CYS   B O     1 
ATOM   11401 C  CB    . CYS   B  1  326  ? -0.708  -2.321  105.200 1.00 21.00 ? 324  CYS   B CB    1 
ATOM   11402 S  SG    . CYS   B  1  326  ? -1.617  -0.842  105.670 1.00 23.00 ? 324  CYS   B SG    1 
ATOM   11403 N  N     . LEU   B  1  327  ? 2.052   -4.230  105.234 1.00 21.99 ? 325  LEU   B N     1 
ATOM   11404 C  CA    . LEU   B  1  327  ? 2.616   -5.555  105.013 1.00 23.95 ? 325  LEU   B CA    1 
ATOM   11405 C  C     . LEU   B  1  327  ? 3.740   -5.891  105.982 1.00 25.64 ? 325  LEU   B C     1 
ATOM   11406 O  O     . LEU   B  1  327  ? 4.302   -6.987  105.905 1.00 26.98 ? 325  LEU   B O     1 
ATOM   11407 C  CB    . LEU   B  1  327  ? 3.124   -5.676  103.576 1.00 23.13 ? 325  LEU   B CB    1 
ATOM   11408 C  CG    . LEU   B  1  327  ? 2.052   -5.503  102.500 1.00 29.09 ? 325  LEU   B CG    1 
ATOM   11409 C  CD1   . LEU   B  1  327  ? 2.668   -5.619  101.120 1.00 33.93 ? 325  LEU   B CD1   1 
ATOM   11410 C  CD2   . LEU   B  1  327  ? 0.956   -6.513  102.687 1.00 32.31 ? 325  LEU   B CD2   1 
ATOM   11411 N  N     . ASP   B  1  328  ? 4.083   -4.979  106.882 1.00 22.05 ? 326  ASP   B N     1 
ATOM   11412 C  CA    . ASP   B  1  328  ? 5.211   -5.169  107.789 1.00 21.85 ? 326  ASP   B CA    1 
ATOM   11413 C  C     . ASP   B  1  328  ? 4.754   -5.994  108.985 1.00 22.94 ? 326  ASP   B C     1 
ATOM   11414 O  O     . ASP   B  1  328  ? 3.959   -5.525  109.806 1.00 23.56 ? 326  ASP   B O     1 
ATOM   11415 C  CB    . ASP   B  1  328  ? 5.712   -3.801  108.234 1.00 22.89 ? 326  ASP   B CB    1 
ATOM   11416 C  CG    . ASP   B  1  328  ? 6.988   -3.884  109.045 1.00 29.95 ? 326  ASP   B CG    1 
ATOM   11417 O  OD1   . ASP   B  1  328  ? 7.222   -4.918  109.704 1.00 27.40 ? 326  ASP   B OD1   1 
ATOM   11418 O  OD2   . ASP   B  1  328  ? 7.758   -2.905  109.019 1.00 32.54 ? 326  ASP   B OD2   1 
ATOM   11419 N  N     . GLY   B  1  329  ? 5.276   -7.220  109.104 1.00 25.60 ? 327  GLY   B N     1 
ATOM   11420 C  CA    . GLY   B  1  329  ? 4.877   -8.105  110.187 1.00 26.43 ? 327  GLY   B CA    1 
ATOM   11421 C  C     . GLY   B  1  329  ? 5.181   -7.583  111.579 1.00 26.29 ? 327  GLY   B C     1 
ATOM   11422 O  O     . GLY   B  1  329  ? 4.559   -8.032  112.549 1.00 24.57 ? 327  GLY   B O     1 
ATOM   11423 N  N     . ASP   B  1  330  ? 6.120   -6.642  111.707 1.00 25.48 ? 328  ASP   B N     1 
ATOM   11424 C  CA    . ASP   B  1  330  ? 6.350   -6.028  113.013 1.00 23.47 ? 328  ASP   B CA    1 
ATOM   11425 C  C     . ASP   B  1  330  ? 5.110   -5.315  113.531 1.00 27.63 ? 328  ASP   B C     1 
ATOM   11426 O  O     . ASP   B  1  330  ? 4.982   -5.116  114.744 1.00 29.54 ? 328  ASP   B O     1 
ATOM   11427 C  CB    . ASP   B  1  330  ? 7.531   -5.047  112.965 1.00 25.33 ? 328  ASP   B CB    1 
ATOM   11428 C  CG    . ASP   B  1  330  ? 8.874   -5.741  112.785 1.00 31.45 ? 328  ASP   B CG    1 
ATOM   11429 O  OD1   . ASP   B  1  330  ? 8.967   -6.960  113.048 1.00 34.69 ? 328  ASP   B OD1   1 
ATOM   11430 O  OD2   . ASP   B  1  330  ? 9.847   -5.065  112.385 1.00 31.27 ? 328  ASP   B OD2   1 
ATOM   11431 N  N     . LEU   B  1  331  ? 4.192   -4.928  112.638 1.00 23.28 ? 329  LEU   B N     1 
ATOM   11432 C  CA    . LEU   B  1  331  ? 2.960   -4.256  113.018 1.00 24.18 ? 329  LEU   B CA    1 
ATOM   11433 C  C     . LEU   B  1  331  ? 1.767   -5.200  113.034 1.00 23.21 ? 329  LEU   B C     1 
ATOM   11434 O  O     . LEU   B  1  331  ? 0.621   -4.740  113.013 1.00 24.50 ? 329  LEU   B O     1 
ATOM   11435 C  CB    . LEU   B  1  331  ? 2.703   -3.074  112.087 1.00 23.53 ? 329  LEU   B CB    1 
ATOM   11436 C  CG    . LEU   B  1  331  ? 3.847   -2.062  112.028 1.00 22.07 ? 329  LEU   B CG    1 
ATOM   11437 C  CD1   . LEU   B  1  331  ? 3.578   -0.981  110.985 1.00 20.67 ? 329  LEU   B CD1   1 
ATOM   11438 C  CD2   . LEU   B  1  331  ? 4.061   -1.452  113.414 1.00 20.67 ? 329  LEU   B CD2   1 
ATOM   11439 N  N     . SER   B  1  332  ? 2.026   -6.506  113.091 1.00 25.99 ? 330  SER   B N     1 
ATOM   11440 C  CA    . SER   B  1  332  ? 0.992   -7.533  113.008 1.00 25.82 ? 330  SER   B CA    1 
ATOM   11441 C  C     . SER   B  1  332  ? -0.180  -7.266  113.946 1.00 25.92 ? 330  SER   B C     1 
ATOM   11442 O  O     . SER   B  1  332  ? 0.000   -7.018  115.143 1.00 28.99 ? 330  SER   B O     1 
ATOM   11443 C  CB    . SER   B  1  332  ? 1.618   -8.879  113.365 1.00 31.25 ? 330  SER   B CB    1 
ATOM   11444 O  OG    . SER   B  1  332  ? 0.644   -9.905  113.307 1.00 35.75 ? 330  SER   B OG    1 
ATOM   11445 N  N     . GLY   B  1  333  ? -1.389  -7.335  113.394 1.00 24.73 ? 331  GLY   B N     1 
ATOM   11446 C  CA    . GLY   B  1  333  ? -2.604  -7.236  114.176 1.00 25.28 ? 331  GLY   B CA    1 
ATOM   11447 C  C     . GLY   B  1  333  ? -2.963  -5.848  114.658 1.00 26.92 ? 331  GLY   B C     1 
ATOM   11448 O  O     . GLY   B  1  333  ? -3.984  -5.694  115.339 1.00 28.20 ? 331  GLY   B O     1 
ATOM   11449 N  N     . TRP   B  1  334  ? -2.168  -4.838  114.336 1.00 25.98 ? 332  TRP   B N     1 
ATOM   11450 C  CA    . TRP   B  1  334  ? -2.448  -3.478  114.774 1.00 24.16 ? 332  TRP   B CA    1 
ATOM   11451 C  C     . TRP   B  1  334  ? -3.415  -2.831  113.802 1.00 22.14 ? 332  TRP   B C     1 
ATOM   11452 O  O     . TRP   B  1  334  ? -3.136  -2.734  112.601 1.00 23.79 ? 332  TRP   B O     1 
ATOM   11453 C  CB    . TRP   B  1  334  ? -1.148  -2.694  114.838 1.00 26.33 ? 332  TRP   B CB    1 
ATOM   11454 C  CG    . TRP   B  1  334  ? -1.268  -1.238  115.168 1.00 23.69 ? 332  TRP   B CG    1 
ATOM   11455 C  CD1   . TRP   B  1  334  ? -1.830  -0.676  116.285 1.00 25.77 ? 332  TRP   B CD1   1 
ATOM   11456 C  CD2   . TRP   B  1  334  ? -0.736  -0.165  114.400 1.00 21.84 ? 332  TRP   B CD2   1 
ATOM   11457 N  NE1   . TRP   B  1  334  ? -1.698  0.694   116.238 1.00 22.12 ? 332  TRP   B NE1   1 
ATOM   11458 C  CE2   . TRP   B  1  334  ? -1.027  1.031   115.091 1.00 21.90 ? 332  TRP   B CE2   1 
ATOM   11459 C  CE3   . TRP   B  1  334  ? -0.053  -0.094  113.179 1.00 22.62 ? 332  TRP   B CE3   1 
ATOM   11460 C  CZ2   . TRP   B  1  334  ? -0.657  2.280   114.600 1.00 20.34 ? 332  TRP   B CZ2   1 
ATOM   11461 C  CZ3   . TRP   B  1  334  ? 0.315   1.141   112.698 1.00 25.30 ? 332  TRP   B CZ3   1 
ATOM   11462 C  CH2   . TRP   B  1  334  ? 0.017   2.317   113.410 1.00 23.66 ? 332  TRP   B CH2   1 
ATOM   11463 N  N     . ASN   B  1  335  ? -4.562  -2.403  114.306 1.00 22.82 ? 333  ASN   B N     1 
ATOM   11464 C  CA    . ASN   B  1  335  ? -5.569  -1.781  113.463 1.00 22.84 ? 333  ASN   B CA    1 
ATOM   11465 C  C     . ASN   B  1  335  ? -5.537  -0.267  113.557 1.00 21.90 ? 333  ASN   B C     1 
ATOM   11466 O  O     . ASN   B  1  335  ? -6.470  0.405   113.109 1.00 23.00 ? 333  ASN   B O     1 
ATOM   11467 C  CB    . ASN   B  1  335  ? -6.950  -2.341  113.787 1.00 25.45 ? 333  ASN   B CB    1 
ATOM   11468 C  CG    . ASN   B  1  335  ? -7.089  -3.782  113.365 1.00 26.54 ? 333  ASN   B CG    1 
ATOM   11469 O  OD1   . ASN   B  1  335  ? -6.451  -4.212  112.401 1.00 24.61 ? 333  ASN   B OD1   1 
ATOM   11470 N  ND2   . ASN   B  1  335  ? -7.925  -4.536  114.073 1.00 28.73 ? 333  ASN   B ND2   1 
ATOM   11471 N  N     . GLY   B  1  336  ? -4.469  0.279   114.111 1.00 20.98 ? 334  GLY   B N     1 
ATOM   11472 C  CA    . GLY   B  1  336  ? -4.388  1.704   114.319 1.00 21.71 ? 334  GLY   B CA    1 
ATOM   11473 C  C     . GLY   B  1  336  ? -3.725  2.503   113.234 1.00 20.51 ? 334  GLY   B C     1 
ATOM   11474 O  O     . GLY   B  1  336  ? -3.605  3.717   113.388 1.00 19.76 ? 334  GLY   B O     1 
ATOM   11475 N  N     . MET   B  1  337  ? -3.295  1.892   112.133 1.00 20.97 ? 335  MET   B N     1 
ATOM   11476 C  CA    . MET   B  1  337  ? -2.742  2.685   111.046 1.00 19.11 ? 335  MET   B CA    1 
ATOM   11477 C  C     . MET   B  1  337  ? -3.859  3.514   110.431 1.00 20.01 ? 335  MET   B C     1 
ATOM   11478 O  O     . MET   B  1  337  ? -4.880  2.968   109.999 1.00 19.96 ? 335  MET   B O     1 
ATOM   11479 C  CB    . MET   B  1  337  ? -2.153  1.774   109.979 1.00 23.78 ? 335  MET   B CB    1 
ATOM   11480 C  CG    . MET   B  1  337  ? -1.512  2.541   108.835 1.00 23.30 ? 335  MET   B CG    1 
ATOM   11481 S  SD    . MET   B  1  337  ? 0.082   3.201   109.346 1.00 33.17 ? 335  MET   B SD    1 
ATOM   11482 C  CE    . MET   B  1  337  ? -0.196  4.952   109.131 1.00 28.10 ? 335  MET   B CE    1 
ATOM   11483 N  N     . GLY   B  1  338  ? -3.655  4.823   110.367 1.00 17.86 ? 336  GLY   B N     1 
ATOM   11484 C  CA    . GLY   B  1  338  ? -4.647  5.735   109.840 1.00 19.56 ? 336  GLY   B CA    1 
ATOM   11485 C  C     . GLY   B  1  338  ? -4.125  6.466   108.619 1.00 17.97 ? 336  GLY   B C     1 
ATOM   11486 O  O     . GLY   B  1  338  ? -2.928  6.731   108.492 1.00 18.23 ? 336  GLY   B O     1 
ATOM   11487 N  N     . PHE   B  1  339  ? -5.036  6.791   107.715 1.00 17.26 ? 337  PHE   B N     1 
ATOM   11488 C  CA    . PHE   B  1  339  ? -4.620  7.409   106.472 1.00 17.22 ? 337  PHE   B CA    1 
ATOM   11489 C  C     . PHE   B  1  339  ? -5.740  8.318   106.005 1.00 16.07 ? 337  PHE   B C     1 
ATOM   11490 O  O     . PHE   B  1  339  ? -6.900  7.898   105.950 1.00 18.17 ? 337  PHE   B O     1 
ATOM   11491 C  CB    . PHE   B  1  339  ? -4.359  6.323   105.429 1.00 18.07 ? 337  PHE   B CB    1 
ATOM   11492 C  CG    . PHE   B  1  339  ? -3.643  6.810   104.209 1.00 18.00 ? 337  PHE   B CG    1 
ATOM   11493 C  CD1   . PHE   B  1  339  ? -2.262  6.879   104.178 1.00 20.05 ? 337  PHE   B CD1   1 
ATOM   11494 C  CD2   . PHE   B  1  339  ? -4.355  7.169   103.083 1.00 17.39 ? 337  PHE   B CD2   1 
ATOM   11495 C  CE1   . PHE   B  1  339  ? -1.604  7.314   103.027 1.00 20.78 ? 337  PHE   B CE1   1 
ATOM   11496 C  CE2   . PHE   B  1  339  ? -3.705  7.602   101.928 1.00 20.06 ? 337  PHE   B CE2   1 
ATOM   11497 C  CZ    . PHE   B  1  339  ? -2.336  7.675   101.907 1.00 20.83 ? 337  PHE   B CZ    1 
ATOM   11498 N  N     . VAL   B  1  340  ? -5.401  9.555   105.697 1.00 16.48 ? 338  VAL   B N     1 
ATOM   11499 C  CA    . VAL   B  1  340  ? -6.376  10.544  105.254 1.00 15.89 ? 338  VAL   B CA    1 
ATOM   11500 C  C     . VAL   B  1  340  ? -6.531  10.442  103.752 1.00 17.29 ? 338  VAL   B C     1 
ATOM   11501 O  O     . VAL   B  1  340  ? -5.547  10.305  103.025 1.00 15.95 ? 338  VAL   B O     1 
ATOM   11502 C  CB    . VAL   B  1  340  ? -5.911  11.963  105.622 1.00 16.23 ? 338  VAL   B CB    1 
ATOM   11503 C  CG1   . VAL   B  1  340  ? -6.911  13.003  105.123 1.00 18.43 ? 338  VAL   B CG1   1 
ATOM   11504 C  CG2   . VAL   B  1  340  ? -5.724  12.077  107.117 1.00 16.94 ? 338  VAL   B CG2   1 
ATOM   11505 N  N     . VAL   B  1  341  ? -7.758  10.571  103.279 1.00 16.06 ? 339  VAL   B N     1 
ATOM   11506 C  CA    A VAL   B  1  341  ? -8.038  10.727  101.859 0.51 16.86 ? 339  VAL   B CA    1 
ATOM   11507 C  CA    B VAL   B  1  341  ? -8.039  10.725  101.858 0.49 16.86 ? 339  VAL   B CA    1 
ATOM   11508 C  C     . VAL   B  1  341  ? -8.882  11.977  101.674 1.00 15.65 ? 339  VAL   B C     1 
ATOM   11509 O  O     . VAL   B  1  341  ? -9.826  12.222  102.439 1.00 16.93 ? 339  VAL   B O     1 
ATOM   11510 C  CB    A VAL   B  1  341  ? -8.709  9.477   101.262 0.51 17.52 ? 339  VAL   B CB    1 
ATOM   11511 C  CB    B VAL   B  1  341  ? -8.728  9.486   101.255 0.49 17.52 ? 339  VAL   B CB    1 
ATOM   11512 C  CG1   A VAL   B  1  341  ? -7.755  8.305   101.341 0.51 19.06 ? 339  VAL   B CG1   1 
ATOM   11513 C  CG1   B VAL   B  1  341  ? -8.587  9.498   99.733  0.49 16.63 ? 339  VAL   B CG1   1 
ATOM   11514 C  CG2   A VAL   B  1  341  ? -10.003 9.167   101.991 0.51 21.02 ? 339  VAL   B CG2   1 
ATOM   11515 C  CG2   B VAL   B  1  341  ? -8.145  8.215   101.847 0.49 19.60 ? 339  VAL   B CG2   1 
ATOM   11516 N  N     . GLN   B  1  342  ? -8.524  12.780  100.677 1.00 15.35 ? 340  GLN   B N     1 
ATOM   11517 C  CA    . GLN   B  1  342  ? -9.123  14.093  100.447 1.00 16.88 ? 340  GLN   B CA    1 
ATOM   11518 C  C     . GLN   B  1  342  ? -10.197 13.997  99.370  1.00 16.40 ? 340  GLN   B C     1 
ATOM   11519 O  O     . GLN   B  1  342  ? -9.891  13.770  98.193  1.00 16.13 ? 340  GLN   B O     1 
ATOM   11520 C  CB    . GLN   B  1  342  ? -8.044  15.087  100.039 1.00 14.24 ? 340  GLN   B CB    1 
ATOM   11521 C  CG    . GLN   B  1  342  ? -7.015  15.296  101.118 1.00 14.60 ? 340  GLN   B CG    1 
ATOM   11522 C  CD    . GLN   B  1  342  ? -5.644  15.639  100.541 1.00 14.32 ? 340  GLN   B CD    1 
ATOM   11523 O  OE1   . GLN   B  1  342  ? -5.178  15.002  99.606  1.00 15.34 ? 340  GLN   B OE1   1 
ATOM   11524 N  NE2   . GLN   B  1  342  ? -4.999  16.650  101.099 1.00 14.62 ? 340  GLN   B NE2   1 
ATOM   11525 N  N     . ALA   B  1  343  ? -11.445 14.211  99.771  1.00 16.13 ? 341  ALA   B N     1 
ATOM   11526 C  CA    . ALA   B  1  343  ? -12.550 14.097  98.840  1.00 15.11 ? 341  ALA   B CA    1 
ATOM   11527 C  C     . ALA   B  1  343  ? -12.600 15.234  97.835  1.00 16.20 ? 341  ALA   B C     1 
ATOM   11528 O  O     . ALA   B  1  343  ? -13.302 15.100  96.824  1.00 17.15 ? 341  ALA   B O     1 
ATOM   11529 C  CB    . ALA   B  1  343  ? -13.859 14.006  99.616  1.00 16.98 ? 341  ALA   B CB    1 
ATOM   11530 N  N     . TYR   B  1  344  ? -11.871 16.335  98.053  1.00 16.56 ? 342  TYR   B N     1 
ATOM   11531 C  CA    . TYR   B  1  344  ? -11.787 17.309  96.977  1.00 15.68 ? 342  TYR   B CA    1 
ATOM   11532 C  C     . TYR   B  1  344  ? -10.927 16.830  95.827  1.00 16.61 ? 342  TYR   B C     1 
ATOM   11533 O  O     . TYR   B  1  344  ? -10.845 17.525  94.822  1.00 16.59 ? 342  TYR   B O     1 
ATOM   11534 C  CB    . TYR   B  1  344  ? -11.377 18.718  97.453  1.00 16.49 ? 342  TYR   B CB    1 
ATOM   11535 C  CG    . TYR   B  1  344  ? -9.930  18.981  97.867  1.00 16.04 ? 342  TYR   B CG    1 
ATOM   11536 C  CD1   . TYR   B  1  344  ? -8.963  17.981  97.915  1.00 15.21 ? 342  TYR   B CD1   1 
ATOM   11537 C  CD2   . TYR   B  1  344  ? -9.560  20.256  98.240  1.00 15.83 ? 342  TYR   B CD2   1 
ATOM   11538 C  CE1   . TYR   B  1  344  ? -7.649  18.271  98.299  1.00 14.87 ? 342  TYR   B CE1   1 
ATOM   11539 C  CE2   . TYR   B  1  344  ? -8.286  20.549  98.628  1.00 15.94 ? 342  TYR   B CE2   1 
ATOM   11540 C  CZ    . TYR   B  1  344  ? -7.332  19.564  98.668  1.00 15.59 ? 342  TYR   B CZ    1 
ATOM   11541 O  OH    . TYR   B  1  344  ? -6.064  19.924  99.088  1.00 14.83 ? 342  TYR   B OH    1 
ATOM   11542 N  N     . GLY   B  1  345  ? -10.284 15.679  95.966  1.00 16.15 ? 343  GLY   B N     1 
ATOM   11543 C  CA    . GLY   B  1  345  ? -9.387  15.172  94.954  1.00 15.81 ? 343  GLY   B CA    1 
ATOM   11544 C  C     . GLY   B  1  345  ? -10.126 14.206  94.046  1.00 16.25 ? 343  GLY   B C     1 
ATOM   11545 O  O     . GLY   B  1  345  ? -10.923 13.390  94.503  1.00 16.76 ? 343  GLY   B O     1 
ATOM   11546 N  N     . LYS   B  1  346  ? -9.791  14.274  92.759  1.00 15.74 ? 344  LYS   B N     1 
ATOM   11547 C  CA    . LYS   B  1  346  ? -10.438 13.429  91.764  1.00 16.29 ? 344  LYS   B CA    1 
ATOM   11548 C  C     . LYS   B  1  346  ? -10.093 11.961  91.937  1.00 15.83 ? 344  LYS   B C     1 
ATOM   11549 O  O     . LYS   B  1  346  ? -10.824 11.101  91.437  1.00 16.99 ? 344  LYS   B O     1 
ATOM   11550 C  CB    . LYS   B  1  346  ? -10.028 13.901  90.378  1.00 16.85 ? 344  LYS   B CB    1 
ATOM   11551 C  CG    . LYS   B  1  346  ? -10.511 15.300  90.089  1.00 17.52 ? 344  LYS   B CG    1 
ATOM   11552 C  CD    . LYS   B  1  346  ? -10.038 15.781  88.756  1.00 17.57 ? 344  LYS   B CD    1 
ATOM   11553 C  CE    . LYS   B  1  346  ? -10.673 17.124  88.455  1.00 17.51 ? 344  LYS   B CE    1 
ATOM   11554 N  NZ    . LYS   B  1  346  ? -10.059 17.733  87.230  1.00 16.90 ? 344  LYS   B NZ    1 
ATOM   11555 N  N     . ARG   B  1  347  ? -8.980  11.658  92.592  1.00 15.89 ? 345  ARG   B N     1 
ATOM   11556 C  CA    . ARG   B  1  347  ? -8.587  10.276  92.753  1.00 17.35 ? 345  ARG   B CA    1 
ATOM   11557 C  C     . ARG   B  1  347  ? -9.220  9.626   93.961  1.00 16.54 ? 345  ARG   B C     1 
ATOM   11558 O  O     . ARG   B  1  347  ? -9.085  8.411   94.125  1.00 17.57 ? 345  ARG   B O     1 
ATOM   11559 C  CB    . ARG   B  1  347  ? -7.070  10.178  92.848  1.00 16.57 ? 345  ARG   B CB    1 
ATOM   11560 C  CG    . ARG   B  1  347  ? -6.410  10.537  91.529  1.00 15.37 ? 345  ARG   B CG    1 
ATOM   11561 C  CD    . ARG   B  1  347  ? -4.939  10.810  91.726  1.00 16.95 ? 345  ARG   B CD    1 
ATOM   11562 N  NE    . ARG   B  1  347  ? -4.710  12.074  92.418  1.00 14.86 ? 345  ARG   B NE    1 
ATOM   11563 C  CZ    . ARG   B  1  347  ? -3.528  12.425  92.898  1.00 16.39 ? 345  ARG   B CZ    1 
ATOM   11564 N  NH1   . ARG   B  1  347  ? -2.461  11.656  92.730  1.00 15.62 ? 345  ARG   B NH1   1 
ATOM   11565 N  NH2   . ARG   B  1  347  ? -3.404  13.583  93.541  1.00 15.33 ? 345  ARG   B NH2   1 
ATOM   11566 N  N     . CYS   B  1  348  ? -9.932  10.399  94.788  1.00 17.00 ? 346  CYS   B N     1 
ATOM   11567 C  CA    . CYS   B  1  348  ? -10.395 9.932   96.088  1.00 17.49 ? 346  CYS   B CA    1 
ATOM   11568 C  C     . CYS   B  1  348  ? -11.056 8.553   96.055  1.00 17.94 ? 346  CYS   B C     1 
ATOM   11569 O  O     . CYS   B  1  348  ? -10.625 7.664   96.794  1.00 19.39 ? 346  CYS   B O     1 
ATOM   11570 C  CB    . CYS   B  1  348  ? -11.280 10.986  96.745  1.00 16.30 ? 346  CYS   B CB    1 
ATOM   11571 S  SG    . CYS   B  1  348  ? -11.586 10.624  98.485  1.00 22.27 ? 346  CYS   B SG    1 
ATOM   11572 N  N     . PRO   B  1  349  ? -12.091 8.311   95.241  1.00 18.03 ? 347  PRO   B N     1 
ATOM   11573 C  CA    . PRO   B  1  349  ? -12.722 6.982   95.282  1.00 19.36 ? 347  PRO   B CA    1 
ATOM   11574 C  C     . PRO   B  1  349  ? -11.787 5.862   94.867  1.00 17.62 ? 347  PRO   B C     1 
ATOM   11575 O  O     . PRO   B  1  349  ? -11.878 4.750   95.405  1.00 18.33 ? 347  PRO   B O     1 
ATOM   11576 C  CB    . PRO   B  1  349  ? -13.924 7.115   94.335  1.00 22.64 ? 347  PRO   B CB    1 
ATOM   11577 C  CG    . PRO   B  1  349  ? -13.632 8.267   93.493  1.00 20.63 ? 347  PRO   B CG    1 
ATOM   11578 C  CD    . PRO   B  1  349  ? -12.727 9.194   94.250  1.00 18.83 ? 347  PRO   B CD    1 
ATOM   11579 N  N     . PHE   B  1  350  ? -10.867 6.140   93.943  1.00 18.04 ? 348  PHE   B N     1 
ATOM   11580 C  CA    . PHE   B  1  350  ? -9.909  5.130   93.505  1.00 18.51 ? 348  PHE   B CA    1 
ATOM   11581 C  C     . PHE   B  1  350  ? -8.866  4.869   94.575  1.00 17.80 ? 348  PHE   B C     1 
ATOM   11582 O  O     . PHE   B  1  350  ? -8.447  3.720   94.776  1.00 19.17 ? 348  PHE   B O     1 
ATOM   11583 C  CB    . PHE   B  1  350  ? -9.302  5.561   92.175  1.00 17.53 ? 348  PHE   B CB    1 
ATOM   11584 C  CG    . PHE   B  1  350  ? -10.343 5.941   91.202  1.00 18.71 ? 348  PHE   B CG    1 
ATOM   11585 C  CD1   . PHE   B  1  350  ? -11.068 4.959   90.563  1.00 21.61 ? 348  PHE   B CD1   1 
ATOM   11586 C  CD2   . PHE   B  1  350  ? -10.668 7.270   90.991  1.00 18.79 ? 348  PHE   B CD2   1 
ATOM   11587 C  CE1   . PHE   B  1  350  ? -12.090 5.298   89.681  1.00 23.08 ? 348  PHE   B CE1   1 
ATOM   11588 C  CE2   . PHE   B  1  350  ? -11.681 7.612   90.130  1.00 20.82 ? 348  PHE   B CE2   1 
ATOM   11589 C  CZ    . PHE   B  1  350  ? -12.391 6.626   89.468  1.00 21.60 ? 348  PHE   B CZ    1 
ATOM   11590 N  N     . VAL   B  1  351  ? -8.475  5.914   95.305  1.00 17.59 ? 349  VAL   B N     1 
ATOM   11591 C  CA    . VAL   B  1  351  ? -7.587  5.721   96.446  1.00 17.77 ? 349  VAL   B CA    1 
ATOM   11592 C  C     . VAL   B  1  351  ? -8.273  4.869   97.498  1.00 17.93 ? 349  VAL   B C     1 
ATOM   11593 O  O     . VAL   B  1  351  ? -7.670  3.960   98.077  1.00 18.18 ? 349  VAL   B O     1 
ATOM   11594 C  CB    . VAL   B  1  351  ? -7.165  7.081   97.010  1.00 16.36 ? 349  VAL   B CB    1 
ATOM   11595 C  CG1   . VAL   B  1  351  ? -6.325  6.872   98.273  1.00 18.89 ? 349  VAL   B CG1   1 
ATOM   11596 C  CG2   . VAL   B  1  351  ? -6.360  7.837   95.981  1.00 17.73 ? 349  VAL   B CG2   1 
ATOM   11597 N  N     . LEU   B  1  352  ? -9.550  5.143   97.756  1.00 17.33 ? 350  LEU   B N     1 
ATOM   11598 C  CA    . LEU   B  1  352  ? -10.294 4.341   98.714  1.00 18.31 ? 350  LEU   B CA    1 
ATOM   11599 C  C     . LEU   B  1  352  ? -10.349 2.882   98.283  1.00 18.56 ? 350  LEU   B C     1 
ATOM   11600 O  O     . LEU   B  1  352  ? -10.165 1.980   99.108  1.00 19.69 ? 350  LEU   B O     1 
ATOM   11601 C  CB    . LEU   B  1  352  ? -11.700 4.909   98.888  1.00 18.77 ? 350  LEU   B CB    1 
ATOM   11602 C  CG    . LEU   B  1  352  ? -11.748 6.227   99.662  1.00 19.83 ? 350  LEU   B CG    1 
ATOM   11603 C  CD1   . LEU   B  1  352  ? -13.174 6.728   99.674  1.00 20.77 ? 350  LEU   B CD1   1 
ATOM   11604 C  CD2   . LEU   B  1  352  ? -11.249 6.024   101.094 1.00 22.06 ? 350  LEU   B CD2   1 
ATOM   11605 N  N     . ASP   B  1  353  ? -10.604 2.631   96.991  1.00 18.93 ? 351  ASP   B N     1 
ATOM   11606 C  CA    . ASP   B  1  353  ? -10.595 1.254   96.497  1.00 20.04 ? 351  ASP   B CA    1 
ATOM   11607 C  C     . ASP   B  1  353  ? -9.255  0.596   96.775  1.00 18.18 ? 351  ASP   B C     1 
ATOM   11608 O  O     . ASP   B  1  353  ? -9.198  -0.573  97.185  1.00 20.61 ? 351  ASP   B O     1 
ATOM   11609 C  CB    . ASP   B  1  353  ? -10.836 1.222   94.987  1.00 19.81 ? 351  ASP   B CB    1 
ATOM   11610 C  CG    . ASP   B  1  353  ? -12.244 1.602   94.596  1.00 24.68 ? 351  ASP   B CG    1 
ATOM   11611 O  OD1   . ASP   B  1  353  ? -13.163 1.460   95.423  1.00 25.30 ? 351  ASP   B OD1   1 
ATOM   11612 O  OD2   . ASP   B  1  353  ? -12.407 2.047   93.433  1.00 25.75 ? 351  ASP   B OD2   1 
ATOM   11613 N  N     . PHE   B  1  354  ? -8.167  1.330   96.540  1.00 19.18 ? 352  PHE   B N     1 
ATOM   11614 C  CA    . PHE   B  1  354  ? -6.837  0.803   96.815  1.00 19.05 ? 352  PHE   B CA    1 
ATOM   11615 C  C     . PHE   B  1  354  ? -6.656  0.490   98.295  1.00 19.32 ? 352  PHE   B C     1 
ATOM   11616 O  O     . PHE   B  1  354  ? -6.121  -0.567  98.648  1.00 19.41 ? 352  PHE   B O     1 
ATOM   11617 C  CB    . PHE   B  1  354  ? -5.773  1.799   96.359  1.00 19.50 ? 352  PHE   B CB    1 
ATOM   11618 C  CG    . PHE   B  1  354  ? -4.405  1.459   96.865  1.00 18.74 ? 352  PHE   B CG    1 
ATOM   11619 C  CD1   . PHE   B  1  354  ? -3.620  0.532   96.197  1.00 19.97 ? 352  PHE   B CD1   1 
ATOM   11620 C  CD2   . PHE   B  1  354  ? -3.922  2.028   98.041  1.00 19.47 ? 352  PHE   B CD2   1 
ATOM   11621 C  CE1   . PHE   B  1  354  ? -2.359  0.192   96.685  1.00 19.80 ? 352  PHE   B CE1   1 
ATOM   11622 C  CE2   . PHE   B  1  354  ? -2.684  1.683   98.536  1.00 21.56 ? 352  PHE   B CE2   1 
ATOM   11623 C  CZ    . PHE   B  1  354  ? -1.903  0.766   97.870  1.00 19.79 ? 352  PHE   B CZ    1 
ATOM   11624 N  N     . ILE   B  1  355  ? -7.097  1.394   99.174  1.00 18.61 ? 353  ILE   B N     1 
ATOM   11625 C  CA    . ILE   B  1  355  ? -6.918  1.196   100.612 1.00 18.98 ? 353  ILE   B CA    1 
ATOM   11626 C  C     . ILE   B  1  355  ? -7.772  0.042   101.109 1.00 18.67 ? 353  ILE   B C     1 
ATOM   11627 O  O     . ILE   B  1  355  ? -7.328  -0.779  101.921 1.00 19.32 ? 353  ILE   B O     1 
ATOM   11628 C  CB    . ILE   B  1  355  ? -7.242  2.497   101.366 1.00 19.81 ? 353  ILE   B CB    1 
ATOM   11629 C  CG1   . ILE   B  1  355  ? -6.212  3.566   101.037 1.00 21.00 ? 353  ILE   B CG1   1 
ATOM   11630 C  CG2   . ILE   B  1  355  ? -7.297  2.252   102.886 1.00 20.53 ? 353  ILE   B CG2   1 
ATOM   11631 C  CD1   . ILE   B  1  355  ? -6.600  4.926   101.570 1.00 22.50 ? 353  ILE   B CD1   1 
ATOM   11632 N  N     . ILE   B  1  356  ? -9.018  -0.036  100.646 1.00 19.51 ? 354  ILE   B N     1 
ATOM   11633 C  CA    . ILE   B  1  356  ? -9.884  -1.121  101.080 1.00 21.83 ? 354  ILE   B CA    1 
ATOM   11634 C  C     . ILE   B  1  356  ? -9.300  -2.459  100.662 1.00 20.64 ? 354  ILE   B C     1 
ATOM   11635 O  O     . ILE   B  1  356  ? -9.320  -3.434  101.428 1.00 21.14 ? 354  ILE   B O     1 
ATOM   11636 C  CB    . ILE   B  1  356  ? -11.299 -0.915  100.517 1.00 21.50 ? 354  ILE   B CB    1 
ATOM   11637 C  CG1   . ILE   B  1  356  ? -11.985 0.243   101.249 1.00 22.98 ? 354  ILE   B CG1   1 
ATOM   11638 C  CG2   . ILE   B  1  356  ? -12.093 -2.203  100.615 1.00 22.32 ? 354  ILE   B CG2   1 
ATOM   11639 C  CD1   . ILE   B  1  356  ? -13.180 0.815   100.496 1.00 21.40 ? 354  ILE   B CD1   1 
ATOM   11640 N  N     . ASP   B  1  357  ? -8.773  -2.529  99.438  1.00 20.87 ? 355  ASP   B N     1 
ATOM   11641 C  CA    . ASP   B  1  357  ? -8.156  -3.766  98.992  1.00 21.11 ? 355  ASP   B CA    1 
ATOM   11642 C  C     . ASP   B  1  357  ? -6.904  -4.076  99.796  1.00 19.46 ? 355  ASP   B C     1 
ATOM   11643 O  O     . ASP   B  1  357  ? -6.683  -5.233  100.164 1.00 20.10 ? 355  ASP   B O     1 
ATOM   11644 C  CB    . ASP   B  1  357  ? -7.842  -3.695  97.501  1.00 21.99 ? 355  ASP   B CB    1 
ATOM   11645 C  CG    . ASP   B  1  357  ? -6.992  -4.858  97.043  1.00 22.17 ? 355  ASP   B CG    1 
ATOM   11646 O  OD1   . ASP   B  1  357  ? -7.556  -5.961  96.862  1.00 25.28 ? 355  ASP   B OD1   1 
ATOM   11647 O  OD2   . ASP   B  1  357  ? -5.764  -4.681  96.913  1.00 21.60 ? 355  ASP   B OD2   1 
ATOM   11648 N  N     . LEU   B  1  358  ? -6.069  -3.062  100.058 1.00 20.14 ? 356  LEU   B N     1 
ATOM   11649 C  CA    . LEU   B  1  358  ? -4.884  -3.273  100.881 1.00 19.57 ? 356  LEU   B CA    1 
ATOM   11650 C  C     . LEU   B  1  358  ? -5.270  -3.794  102.252 1.00 18.39 ? 356  LEU   B C     1 
ATOM   11651 O  O     . LEU   B  1  358  ? -4.642  -4.723  102.775 1.00 20.02 ? 356  LEU   B O     1 
ATOM   11652 C  CB    . LEU   B  1  358  ? -4.115  -1.962  101.025 1.00 17.81 ? 356  LEU   B CB    1 
ATOM   11653 C  CG    . LEU   B  1  358  ? -2.873  -1.947  101.935 1.00 17.55 ? 356  LEU   B CG    1 
ATOM   11654 C  CD1   . LEU   B  1  358  ? -1.873  -2.984  101.478 1.00 20.71 ? 356  LEU   B CD1   1 
ATOM   11655 C  CD2   . LEU   B  1  358  ? -2.257  -0.558  101.903 1.00 20.05 ? 356  LEU   B CD2   1 
ATOM   11656 N  N     . ALA   B  1  359  ? -6.316  -3.221  102.844 1.00 19.45 ? 357  ALA   B N     1 
ATOM   11657 C  CA    . ALA   B  1  359  ? -6.765  -3.691  104.148 1.00 18.83 ? 357  ALA   B CA    1 
ATOM   11658 C  C     . ALA   B  1  359  ? -7.168  -5.159  104.080 1.00 21.75 ? 357  ALA   B C     1 
ATOM   11659 O  O     . ALA   B  1  359  ? -6.766  -5.969  104.919 1.00 21.79 ? 357  ALA   B O     1 
ATOM   11660 C  CB    . ALA   B  1  359  ? -7.944  -2.836  104.610 1.00 22.08 ? 357  ALA   B CB    1 
ATOM   11661 N  N     . ARG   B  1  360  ? -7.929  -5.523  103.043 1.00 21.35 ? 358  ARG   B N     1 
ATOM   11662 C  CA    A ARG   B  1  360  ? -8.405  -6.894  102.904 0.48 23.41 ? 358  ARG   B CA    1 
ATOM   11663 C  CA    B ARG   B  1  360  ? -8.405  -6.895  102.910 0.52 23.41 ? 358  ARG   B CA    1 
ATOM   11664 C  C     . ARG   B  1  360  ? -7.253  -7.873  102.742 1.00 21.68 ? 358  ARG   B C     1 
ATOM   11665 O  O     . ARG   B  1  360  ? -7.242  -8.942  103.364 1.00 23.46 ? 358  ARG   B O     1 
ATOM   11666 C  CB    A ARG   B  1  360  ? -9.349  -6.992  101.709 0.48 23.98 ? 358  ARG   B CB    1 
ATOM   11667 C  CB    B ARG   B  1  360  ? -9.358  -7.005  101.722 0.52 23.98 ? 358  ARG   B CB    1 
ATOM   11668 C  CG    A ARG   B  1  360  ? -10.756 -6.601  102.047 0.48 28.48 ? 358  ARG   B CG    1 
ATOM   11669 C  CG    B ARG   B  1  360  ? -10.819 -6.973  102.103 0.52 30.49 ? 358  ARG   B CG    1 
ATOM   11670 C  CD    A ARG   B  1  360  ? -11.614 -6.439  100.814 0.48 28.26 ? 358  ARG   B CD    1 
ATOM   11671 C  CD    B ARG   B  1  360  ? -11.695 -7.396  100.932 0.52 27.69 ? 358  ARG   B CD    1 
ATOM   11672 N  NE    A ARG   B  1  360  ? -13.006 -6.235  101.192 0.48 28.41 ? 358  ARG   B NE    1 
ATOM   11673 N  NE    B ARG   B  1  360  ? -12.237 -6.252  100.209 0.52 30.05 ? 358  ARG   B NE    1 
ATOM   11674 C  CZ    A ARG   B  1  360  ? -13.910 -5.633  100.432 0.48 30.77 ? 358  ARG   B CZ    1 
ATOM   11675 C  CZ    B ARG   B  1  360  ? -13.426 -5.716  100.449 0.52 29.90 ? 358  ARG   B CZ    1 
ATOM   11676 N  NH1   A ARG   B  1  360  ? -13.600 -5.155  99.237  0.48 35.60 ? 358  ARG   B NH1   1 
ATOM   11677 N  NH1   B ARG   B  1  360  ? -14.211 -6.177  101.411 0.52 36.72 ? 358  ARG   B NH1   1 
ATOM   11678 N  NH2   A ARG   B  1  360  ? -15.156 -5.507  100.882 0.48 35.16 ? 358  ARG   B NH2   1 
ATOM   11679 N  NH2   B ARG   B  1  360  ? -13.845 -4.703  99.698  0.52 36.19 ? 358  ARG   B NH2   1 
ATOM   11680 N  N     . ARG   B  1  361  ? -6.280  -7.536  101.904 1.00 22.72 ? 359  ARG   B N     1 
ATOM   11681 C  CA    . ARG   B  1  361  ? -5.221  -8.502  101.646 1.00 24.44 ? 359  ARG   B CA    1 
ATOM   11682 C  C     . ARG   B  1  361  ? -4.156  -8.537  102.729 1.00 20.09 ? 359  ARG   B C     1 
ATOM   11683 O  O     . ARG   B  1  361  ? -3.445  -9.538  102.837 1.00 23.70 ? 359  ARG   B O     1 
ATOM   11684 C  CB    . ARG   B  1  361  ? -4.603  -8.293  100.268 1.00 28.20 ? 359  ARG   B CB    1 
ATOM   11685 C  CG    . ARG   B  1  361  ? -3.854  -7.008  100.110 1.00 24.67 ? 359  ARG   B CG    1 
ATOM   11686 C  CD    . ARG   B  1  361  ? -3.491  -6.844  98.629  1.00 22.50 ? 359  ARG   B CD    1 
ATOM   11687 N  NE    . ARG   B  1  361  ? -3.283  -5.443  98.295  1.00 20.59 ? 359  ARG   B NE    1 
ATOM   11688 C  CZ    . ARG   B  1  361  ? -2.119  -4.816  98.356  1.00 19.21 ? 359  ARG   B CZ    1 
ATOM   11689 N  NH1   . ARG   B  1  361  ? -1.019  -5.428  98.758  1.00 23.03 ? 359  ARG   B NH1   1 
ATOM   11690 N  NH2   . ARG   B  1  361  ? -2.053  -3.536  98.000  1.00 21.18 ? 359  ARG   B NH2   1 
ATOM   11691 N  N     . SER   B  1  362  ? -4.045  -7.487  103.548 1.00 21.07 ? 360  SER   B N     1 
ATOM   11692 C  CA    . SER   B  1  362  ? -3.028  -7.433  104.585 1.00 21.44 ? 360  SER   B CA    1 
ATOM   11693 C  C     . SER   B  1  362  ? -3.549  -7.847  105.954 1.00 20.93 ? 360  SER   B C     1 
ATOM   11694 O  O     . SER   B  1  362  ? -2.748  -7.984  106.888 1.00 22.87 ? 360  SER   B O     1 
ATOM   11695 C  CB    . SER   B  1  362  ? -2.429  -6.021  104.666 1.00 22.93 ? 360  SER   B CB    1 
ATOM   11696 O  OG    . SER   B  1  362  ? -3.387  -5.104  105.162 1.00 22.48 ? 360  SER   B OG    1 
ATOM   11697 N  N     . GLY   B  1  363  ? -4.854  -8.029  106.111 1.00 21.19 ? 361  GLY   B N     1 
ATOM   11698 C  CA    . GLY   B  1  363  ? -5.368  -8.377  107.425 1.00 23.75 ? 361  GLY   B CA    1 
ATOM   11699 C  C     . GLY   B  1  363  ? -5.245  -7.250  108.425 1.00 24.14 ? 361  GLY   B C     1 
ATOM   11700 O  O     . GLY   B  1  363  ? -4.992  -7.498  109.604 1.00 26.59 ? 361  GLY   B O     1 
ATOM   11701 N  N     . ARG   B  1  364  ? -5.398  -6.015  107.971 1.00 22.38 ? 362  ARG   B N     1 
ATOM   11702 C  CA    . ARG   B  1  364  ? -5.298  -4.832  108.813 1.00 24.23 ? 362  ARG   B CA    1 
ATOM   11703 C  C     . ARG   B  1  364  ? -6.576  -4.054  108.595 1.00 23.51 ? 362  ARG   B C     1 
ATOM   11704 O  O     . ARG   B  1  364  ? -6.946  -3.788  107.447 1.00 24.38 ? 362  ARG   B O     1 
ATOM   11705 C  CB    . ARG   B  1  364  ? -4.152  -3.926  108.342 1.00 24.08 ? 362  ARG   B CB    1 
ATOM   11706 C  CG    . ARG   B  1  364  ? -2.756  -4.511  108.435 1.00 22.04 ? 362  ARG   B CG    1 
ATOM   11707 C  CD    . ARG   B  1  364  ? -2.269  -4.578  109.872 1.00 21.52 ? 362  ARG   B CD    1 
ATOM   11708 N  NE    . ARG   B  1  364  ? -0.985  -5.264  109.939 1.00 23.28 ? 362  ARG   B NE    1 
ATOM   11709 C  CZ    . ARG   B  1  364  ? 0.191   -4.692  109.722 1.00 21.78 ? 362  ARG   B CZ    1 
ATOM   11710 N  NH1   . ARG   B  1  364  ? 0.299   -3.390  109.494 1.00 21.37 ? 362  ARG   B NH1   1 
ATOM   11711 N  NH2   . ARG   B  1  364  ? 1.288   -5.441  109.750 1.00 24.16 ? 362  ARG   B NH2   1 
ATOM   11712 N  N     . ARG   B  1  365  ? -7.251  -3.679  109.667 1.00 23.55 ? 363  ARG   B N     1 
ATOM   11713 C  CA    . ARG   B  1  365  ? -8.264  -2.655  109.514 1.00 21.86 ? 363  ARG   B CA    1 
ATOM   11714 C  C     . ARG   B  1  365  ? -7.521  -1.336  109.466 1.00 22.61 ? 363  ARG   B C     1 
ATOM   11715 O  O     . ARG   B  1  365  ? -6.679  -1.067  110.321 1.00 23.43 ? 363  ARG   B O     1 
ATOM   11716 C  CB    . ARG   B  1  365  ? -9.250  -2.664  110.671 1.00 22.89 ? 363  ARG   B CB    1 
ATOM   11717 C  CG    . ARG   B  1  365  ? -10.538 -1.923  110.325 1.00 23.44 ? 363  ARG   B CG    1 
ATOM   11718 C  CD    . ARG   B  1  365  ? -11.585 -2.164  111.406 1.00 26.87 ? 363  ARG   B CD    1 
ATOM   11719 N  NE    . ARG   B  1  365  ? -12.878 -1.598  111.047 1.00 27.42 ? 363  ARG   B NE    1 
ATOM   11720 C  CZ    . ARG   B  1  365  ? -13.634 -0.872  111.861 1.00 26.15 ? 363  ARG   B CZ    1 
ATOM   11721 N  NH1   . ARG   B  1  365  ? -13.264 -0.619  113.105 1.00 24.98 ? 363  ARG   B NH1   1 
ATOM   11722 N  NH2   . ARG   B  1  365  ? -14.791 -0.394  111.419 1.00 23.56 ? 363  ARG   B NH2   1 
ATOM   11723 N  N     . ILE   B  1  366  ? -7.759  -0.556  108.432 1.00 20.46 ? 364  ILE   B N     1 
ATOM   11724 C  CA    . ILE   B  1  366  ? -7.094  0.722   108.264 1.00 21.17 ? 364  ILE   B CA    1 
ATOM   11725 C  C     . ILE   B  1  366  ? -8.091  1.795   108.646 1.00 20.63 ? 364  ILE   B C     1 
ATOM   11726 O  O     . ILE   B  1  366  ? -9.260  1.744   108.229 1.00 20.42 ? 364  ILE   B O     1 
ATOM   11727 C  CB    . ILE   B  1  366  ? -6.591  0.893   106.819 1.00 19.95 ? 364  ILE   B CB    1 
ATOM   11728 C  CG1   . ILE   B  1  366  ? -5.560  -0.196  106.500 1.00 20.82 ? 364  ILE   B CG1   1 
ATOM   11729 C  CG2   . ILE   B  1  366  ? -6.021  2.291   106.599 1.00 18.32 ? 364  ILE   B CG2   1 
ATOM   11730 C  CD1   . ILE   B  1  366  ? -5.141  -0.260  105.048 1.00 22.51 ? 364  ILE   B CD1   1 
ATOM   11731 N  N     . MET   B  1  367  ? -7.655  2.736   109.484 1.00 20.04 ? 365  MET   B N     1 
ATOM   11732 C  CA    . MET   B  1  367  ? -8.504  3.857   109.850 1.00 20.96 ? 365  MET   B CA    1 
ATOM   11733 C  C     . MET   B  1  367  ? -8.395  4.863   108.722 1.00 21.69 ? 365  MET   B C     1 
ATOM   11734 O  O     . MET   B  1  367  ? -7.289  5.257   108.347 1.00 21.36 ? 365  MET   B O     1 
ATOM   11735 C  CB    . MET   B  1  367  ? -8.026  4.458   111.167 1.00 20.25 ? 365  MET   B CB    1 
ATOM   11736 C  CG    . MET   B  1  367  ? -7.809  3.402   112.234 1.00 19.81 ? 365  MET   B CG    1 
ATOM   11737 S  SD    . MET   B  1  367  ? -7.346  4.120   113.820 1.00 22.59 ? 365  MET   B SD    1 
ATOM   11738 C  CE    . MET   B  1  367  ? -8.884  4.429   114.676 1.00 29.70 ? 365  MET   B CE    1 
ATOM   11739 N  N     . VAL   B  1  368  ? -9.522  5.239   108.139 1.00 17.91 ? 366  VAL   B N     1 
ATOM   11740 C  CA    . VAL   B  1  368  ? -9.506  6.097   106.969 1.00 18.06 ? 366  VAL   B CA    1 
ATOM   11741 C  C     . VAL   B  1  368  ? -10.221 7.382   107.325 1.00 20.24 ? 366  VAL   B C     1 
ATOM   11742 O  O     . VAL   B  1  368  ? -11.440 7.384   107.512 1.00 19.45 ? 366  VAL   B O     1 
ATOM   11743 C  CB    . VAL   B  1  368  ? -10.168 5.440   105.753 1.00 20.07 ? 366  VAL   B CB    1 
ATOM   11744 C  CG1   . VAL   B  1  368  ? -10.153 6.422   104.606 1.00 19.18 ? 366  VAL   B CG1   1 
ATOM   11745 C  CG2   . VAL   B  1  368  ? -9.431  4.155   105.365 1.00 21.75 ? 366  VAL   B CG2   1 
ATOM   11746 N  N     . ARG   B  1  369  ? -9.481  8.483   107.387 1.00 18.16 ? 367  ARG   B N     1 
ATOM   11747 C  CA    . ARG   B  1  369  ? -10.088 9.778   107.649 1.00 17.69 ? 367  ARG   B CA    1 
ATOM   11748 C  C     . ARG   B  1  369  ? -10.471 10.373  106.313 1.00 17.39 ? 367  ARG   B C     1 
ATOM   11749 O  O     . ARG   B  1  369  ? -9.604  10.684  105.496 1.00 18.17 ? 367  ARG   B O     1 
ATOM   11750 C  CB    . ARG   B  1  369  ? -9.142  10.712  108.402 1.00 17.80 ? 367  ARG   B CB    1 
ATOM   11751 C  CG    . ARG   B  1  369  ? -9.828  12.025  108.757 1.00 20.37 ? 367  ARG   B CG    1 
ATOM   11752 C  CD    . ARG   B  1  369  ? -8.826  13.090  109.107 1.00 19.04 ? 367  ARG   B CD    1 
ATOM   11753 N  NE    . ARG   B  1  369  ? -8.124  12.768  110.335 1.00 18.39 ? 367  ARG   B NE    1 
ATOM   11754 C  CZ    . ARG   B  1  369  ? -6.903  13.187  110.630 1.00 19.09 ? 367  ARG   B CZ    1 
ATOM   11755 N  NH1   . ARG   B  1  369  ? -6.213  13.955  109.795 1.00 18.24 ? 367  ARG   B NH1   1 
ATOM   11756 N  NH2   . ARG   B  1  369  ? -6.353  12.799  111.779 1.00 19.23 ? 367  ARG   B NH2   1 
ATOM   11757 N  N     . LEU   B  1  370  ? -11.764 10.527  106.091 1.00 17.76 ? 368  LEU   B N     1 
ATOM   11758 C  CA    . LEU   B  1  370  ? -12.255 11.215  104.914 1.00 17.46 ? 368  LEU   B CA    1 
ATOM   11759 C  C     . LEU   B  1  370  ? -12.370 12.692  105.253 1.00 17.19 ? 368  LEU   B C     1 
ATOM   11760 O  O     . LEU   B  1  370  ? -13.075 13.068  106.203 1.00 18.93 ? 368  LEU   B O     1 
ATOM   11761 C  CB    . LEU   B  1  370  ? -13.605 10.633  104.506 1.00 17.92 ? 368  LEU   B CB    1 
ATOM   11762 C  CG    . LEU   B  1  370  ? -14.128 11.203  103.196 1.00 18.66 ? 368  LEU   B CG    1 
ATOM   11763 C  CD1   . LEU   B  1  370  ? -13.224 10.791  102.059 1.00 20.57 ? 368  LEU   B CD1   1 
ATOM   11764 C  CD2   . LEU   B  1  370  ? -15.534 10.683  102.993 1.00 19.75 ? 368  LEU   B CD2   1 
ATOM   11765 N  N     . VAL   B  1  371  ? -11.643 13.515  104.520 1.00 15.86 ? 369  VAL   B N     1 
ATOM   11766 C  CA    . VAL   B  1  371  ? -11.698 14.958  104.655 1.00 17.55 ? 369  VAL   B CA    1 
ATOM   11767 C  C     . VAL   B  1  371  ? -12.089 15.504  103.308 1.00 17.69 ? 369  VAL   B C     1 
ATOM   11768 O  O     . VAL   B  1  371  ? -12.055 14.797  102.304 1.00 17.82 ? 369  VAL   B O     1 
ATOM   11769 C  CB    . VAL   B  1  371  ? -10.353 15.560  105.100 1.00 16.00 ? 369  VAL   B CB    1 
ATOM   11770 C  CG1   . VAL   B  1  371  ? -9.891  14.903  106.367 1.00 18.15 ? 369  VAL   B CG1   1 
ATOM   11771 C  CG2   . VAL   B  1  371  ? -9.317  15.418  103.986 1.00 17.69 ? 369  VAL   B CG2   1 
ATOM   11772 N  N     . LYS   B  1  372  ? -12.406 16.792  103.277 1.00 16.35 ? 370  LYS   B N     1 
ATOM   11773 C  CA    . LYS   B  1  372  ? -12.532 17.450  101.990 1.00 16.95 ? 370  LYS   B CA    1 
ATOM   11774 C  C     . LYS   B  1  372  ? -11.155 17.817  101.442 1.00 16.66 ? 370  LYS   B C     1 
ATOM   11775 O  O     . LYS   B  1  372  ? -10.716 17.268  100.428 1.00 18.34 ? 370  LYS   B O     1 
ATOM   11776 C  CB    . LYS   B  1  372  ? -13.550 18.598  102.066 1.00 18.45 ? 370  LYS   B CB    1 
ATOM   11777 C  CG    . LYS   B  1  372  ? -14.935 18.006  102.275 1.00 18.60 ? 370  LYS   B CG    1 
ATOM   11778 C  CD    . LYS   B  1  372  ? -16.039 19.032  102.419 1.00 20.06 ? 370  LYS   B CD    1 
ATOM   11779 C  CE    . LYS   B  1  372  ? -17.319 18.325  102.876 1.00 21.22 ? 370  LYS   B CE    1 
ATOM   11780 N  NZ    . LYS   B  1  372  ? -18.410 19.311  103.101 1.00 21.22 ? 370  LYS   B NZ    1 
ATOM   11781 N  N     . GLY   B  1  373  ? -10.426 18.686  102.126 1.00 16.40 ? 371  GLY   B N     1 
ATOM   11782 C  CA    . GLY   B  1  373  ? -9.046  18.930  101.743 1.00 15.82 ? 371  GLY   B CA    1 
ATOM   11783 C  C     . GLY   B  1  373  ? -8.609  20.339  102.058 1.00 16.94 ? 371  GLY   B C     1 
ATOM   11784 O  O     . GLY   B  1  373  ? -9.402  21.270  101.925 1.00 17.94 ? 371  GLY   B O     1 
ATOM   11785 N  N     . ALA   B  1  374  ? -7.349  20.516  102.465 1.00 14.87 ? 372  ALA   B N     1 
ATOM   11786 C  CA    . ALA   B  1  374  ? -6.897  21.772  103.042 1.00 16.10 ? 372  ALA   B CA    1 
ATOM   11787 C  C     . ALA   B  1  374  ? -6.067  22.627  102.106 1.00 16.59 ? 372  ALA   B C     1 
ATOM   11788 O  O     . ALA   B  1  374  ? -5.643  23.710  102.517 1.00 19.39 ? 372  ALA   B O     1 
ATOM   11789 C  CB    . ALA   B  1  374  ? -6.058  21.505  104.291 1.00 18.34 ? 372  ALA   B CB    1 
ATOM   11790 N  N     . TYR   B  1  375  ? -5.802  22.183  100.873 1.00 15.94 ? 373  TYR   B N     1 
ATOM   11791 C  CA    . TYR   B  1  375  ? -4.858  22.891  100.022 1.00 15.07 ? 373  TYR   B CA    1 
ATOM   11792 C  C     . TYR   B  1  375  ? -5.508  23.425  98.757  1.00 14.31 ? 373  TYR   B C     1 
ATOM   11793 O  O     . TYR   B  1  375  ? -4.829  23.613  97.757  1.00 15.33 ? 373  TYR   B O     1 
ATOM   11794 C  CB    . TYR   B  1  375  ? -3.685  21.996  99.640  1.00 17.26 ? 373  TYR   B CB    1 
ATOM   11795 C  CG    . TYR   B  1  375  ? -2.942  21.397  100.803 1.00 17.01 ? 373  TYR   B CG    1 
ATOM   11796 C  CD1   . TYR   B  1  375  ? -3.465  20.325  101.529 1.00 17.29 ? 373  TYR   B CD1   1 
ATOM   11797 C  CD2   . TYR   B  1  375  ? -1.670  21.853  101.135 1.00 18.98 ? 373  TYR   B CD2   1 
ATOM   11798 C  CE1   . TYR   B  1  375  ? -2.765  19.778  102.599 1.00 18.28 ? 373  TYR   B CE1   1 
ATOM   11799 C  CE2   . TYR   B  1  375  ? -0.963  21.305  102.174 1.00 19.95 ? 373  TYR   B CE2   1 
ATOM   11800 C  CZ    . TYR   B  1  375  ? -1.511  20.273  102.896 1.00 18.78 ? 373  TYR   B CZ    1 
ATOM   11801 O  OH    . TYR   B  1  375  ? -0.778  19.722  103.912 1.00 22.00 ? 373  TYR   B OH    1 
ATOM   11802 N  N     . TRP   B  1  376  ? -6.814  23.679  98.782  1.00 15.22 ? 374  TRP   B N     1 
ATOM   11803 C  CA    . TRP   B  1  376  ? -7.539  23.913  97.540  1.00 14.61 ? 374  TRP   B CA    1 
ATOM   11804 C  C     . TRP   B  1  376  ? -6.939  25.051  96.714  1.00 14.79 ? 374  TRP   B C     1 
ATOM   11805 O  O     . TRP   B  1  376  ? -6.621  24.868  95.534  1.00 15.86 ? 374  TRP   B O     1 
ATOM   11806 C  CB    . TRP   B  1  376  ? -9.019  24.128  97.827  1.00 15.38 ? 374  TRP   B CB    1 
ATOM   11807 C  CG    . TRP   B  1  376  ? -9.770  24.285  96.552  1.00 16.64 ? 374  TRP   B CG    1 
ATOM   11808 C  CD1   . TRP   B  1  376  ? -10.139 23.292  95.691  1.00 15.21 ? 374  TRP   B CD1   1 
ATOM   11809 C  CD2   . TRP   B  1  376  ? -10.180 25.509  95.959  1.00 16.31 ? 374  TRP   B CD2   1 
ATOM   11810 N  NE1   . TRP   B  1  376  ? -10.785 23.831  94.606  1.00 16.06 ? 374  TRP   B NE1   1 
ATOM   11811 C  CE2   . TRP   B  1  376  ? -10.823 25.191  94.746  1.00 16.46 ? 374  TRP   B CE2   1 
ATOM   11812 C  CE3   . TRP   B  1  376  ? -10.097 26.847  96.355  1.00 19.42 ? 374  TRP   B CE3   1 
ATOM   11813 C  CZ2   . TRP   B  1  376  ? -11.347 26.161  93.900  1.00 16.43 ? 374  TRP   B CZ2   1 
ATOM   11814 C  CZ3   . TRP   B  1  376  ? -10.636 27.815  95.535  1.00 19.51 ? 374  TRP   B CZ3   1 
ATOM   11815 C  CH2   . TRP   B  1  376  ? -11.261 27.469  94.314  1.00 19.39 ? 374  TRP   B CH2   1 
ATOM   11816 N  N     . ASP   B  1  377  ? -6.817  26.246  97.304  1.00 16.63 ? 375  ASP   B N     1 
ATOM   11817 C  CA    . ASP   B  1  377  ? -6.327  27.395  96.547  1.00 17.68 ? 375  ASP   B CA    1 
ATOM   11818 C  C     . ASP   B  1  377  ? -4.958  27.103  95.966  1.00 15.10 ? 375  ASP   B C     1 
ATOM   11819 O  O     . ASP   B  1  377  ? -4.649  27.518  94.844  1.00 16.31 ? 375  ASP   B O     1 
ATOM   11820 C  CB    . ASP   B  1  377  ? -6.200  28.629  97.447  1.00 21.38 ? 375  ASP   B CB    1 
ATOM   11821 C  CG    . ASP   B  1  377  ? -7.516  29.138  97.961  1.00 31.68 ? 375  ASP   B CG    1 
ATOM   11822 O  OD1   . ASP   B  1  377  ? -8.437  29.301  97.155  1.00 43.65 ? 375  ASP   B OD1   1 
ATOM   11823 O  OD2   . ASP   B  1  377  ? -7.610  29.406  99.176  1.00 46.45 ? 375  ASP   B OD2   1 
ATOM   11824 N  N     . ALA   B  1  378  ? -4.104  26.435  96.740  1.00 15.15 ? 376  ALA   B N     1 
ATOM   11825 C  CA    . ALA   B  1  378  ? -2.752  26.175  96.280  1.00 15.02 ? 376  ALA   B CA    1 
ATOM   11826 C  C     . ALA   B  1  378  ? -2.747  25.174  95.141  1.00 16.04 ? 376  ALA   B C     1 
ATOM   11827 O  O     . ALA   B  1  378  ? -1.903  25.266  94.244  1.00 15.53 ? 376  ALA   B O     1 
ATOM   11828 C  CB    . ALA   B  1  378  ? -1.890  25.657  97.432  1.00 16.52 ? 376  ALA   B CB    1 
ATOM   11829 N  N     . GLU   B  1  379  ? -3.675  24.220  95.156  1.00 14.88 ? 377  GLU   B N     1 
ATOM   11830 C  CA    . GLU   B  1  379  ? -3.727  23.255  94.065  1.00 14.50 ? 377  GLU   B CA    1 
ATOM   11831 C  C     . GLU   B  1  379  ? -4.197  23.919  92.783  1.00 15.73 ? 377  GLU   B C     1 
ATOM   11832 O  O     . GLU   B  1  379  ? -3.723  23.578  91.694  1.00 15.23 ? 377  GLU   B O     1 
ATOM   11833 C  CB    . GLU   B  1  379  ? -4.654  22.084  94.408  1.00 15.46 ? 377  GLU   B CB    1 
ATOM   11834 C  CG    . GLU   B  1  379  ? -4.251  21.250  95.626  1.00 16.77 ? 377  GLU   B CG    1 
ATOM   11835 C  CD    . GLU   B  1  379  ? -2.964  20.467  95.483  1.00 17.01 ? 377  GLU   B CD    1 
ATOM   11836 O  OE1   . GLU   B  1  379  ? -2.344  20.433  94.397  1.00 18.42 ? 377  GLU   B OE1   1 
ATOM   11837 O  OE2   . GLU   B  1  379  ? -2.569  19.855  96.492  1.00 17.26 ? 377  GLU   B OE2   1 
ATOM   11838 N  N     . ILE   B  1  380  ? -5.129  24.867  92.880  1.00 14.91 ? 378  ILE   B N     1 
ATOM   11839 C  CA    . ILE   B  1  380  ? -5.537  25.595  91.682  1.00 15.32 ? 378  ILE   B CA    1 
ATOM   11840 C  C     . ILE   B  1  380  ? -4.355  26.353  91.105  1.00 14.53 ? 378  ILE   B C     1 
ATOM   11841 O  O     . ILE   B  1  380  ? -4.054  26.262  89.907  1.00 14.87 ? 378  ILE   B O     1 
ATOM   11842 C  CB    . ILE   B  1  380  ? -6.701  26.546  91.995  1.00 14.72 ? 378  ILE   B CB    1 
ATOM   11843 C  CG1   . ILE   B  1  380  ? -7.892  25.779  92.555  1.00 15.31 ? 378  ILE   B CG1   1 
ATOM   11844 C  CG2   . ILE   B  1  380  ? -7.088  27.317  90.755  1.00 16.20 ? 378  ILE   B CG2   1 
ATOM   11845 C  CD1   . ILE   B  1  380  ? -8.394  24.654  91.643  1.00 17.52 ? 378  ILE   B CD1   1 
ATOM   11846 N  N     . LYS   B  1  381  ? -3.652  27.099  91.961  1.00 15.11 ? 379  LYS   B N     1 
ATOM   11847 C  CA    . LYS   B  1  381  ? -2.526  27.892  91.493  1.00 13.94 ? 379  LYS   B CA    1 
ATOM   11848 C  C     . LYS   B  1  381  ? -1.463  27.004  90.878  1.00 14.34 ? 379  LYS   B C     1 
ATOM   11849 O  O     . LYS   B  1  381  ? -0.932  27.310  89.804  1.00 14.93 ? 379  LYS   B O     1 
ATOM   11850 C  CB    . LYS   B  1  381  ? -1.925  28.702  92.642  1.00 14.40 ? 379  LYS   B CB    1 
ATOM   11851 C  CG    . LYS   B  1  381  ? -0.714  29.503  92.212  1.00 16.38 ? 379  LYS   B CG    1 
ATOM   11852 C  CD    . LYS   B  1  381  ? -0.251  30.398  93.348  1.00 14.59 ? 379  LYS   B CD    1 
ATOM   11853 C  CE    . LYS   B  1  381  ? 0.872   31.299  92.863  1.00 16.78 ? 379  LYS   B CE    1 
ATOM   11854 N  NZ    . LYS   B  1  381  ? 1.333   32.216  93.956  1.00 15.37 ? 379  LYS   B NZ    1 
ATOM   11855 N  N     . ARG   B  1  382  ? -1.152  25.887  91.534  1.00 14.23 ? 380  ARG   B N     1 
ATOM   11856 C  CA    . ARG   B  1  382  ? -0.038  25.069  91.069  1.00 14.47 ? 380  ARG   B CA    1 
ATOM   11857 C  C     . ARG   B  1  382  ? -0.335  24.460  89.706  1.00 14.25 ? 380  ARG   B C     1 
ATOM   11858 O  O     . ARG   B  1  382  ? 0.533   24.442  88.823  1.00 15.38 ? 380  ARG   B O     1 
ATOM   11859 C  CB    . ARG   B  1  382  ? 0.236   23.974  92.101  1.00 15.53 ? 380  ARG   B CB    1 
ATOM   11860 C  CG    . ARG   B  1  382  ? 1.390   23.052  91.741  1.00 18.63 ? 380  ARG   B CG    1 
ATOM   11861 C  CD    . ARG   B  1  382  ? 2.698   23.811  91.492  1.00 23.75 ? 380  ARG   B CD    1 
ATOM   11862 N  NE    . ARG   B  1  382  ? 3.787   22.869  91.250  1.00 26.76 ? 380  ARG   B NE    1 
ATOM   11863 C  CZ    . ARG   B  1  382  ? 4.503   22.286  92.203  1.00 38.90 ? 380  ARG   B CZ    1 
ATOM   11864 N  NH1   . ARG   B  1  382  ? 4.291   22.544  93.487  1.00 34.54 ? 380  ARG   B NH1   1 
ATOM   11865 N  NH2   . ARG   B  1  382  ? 5.455   21.422  91.862  1.00 38.77 ? 380  ARG   B NH2   1 
ATOM   11866 N  N     . ALA   B  1  383  ? -1.551  23.973  89.502  1.00 14.28 ? 381  ALA   B N     1 
ATOM   11867 C  CA    . ALA   B  1  383  ? -1.882  23.394  88.207  1.00 14.76 ? 381  ALA   B CA    1 
ATOM   11868 C  C     . ALA   B  1  383  ? -1.818  24.450  87.114  1.00 14.93 ? 381  ALA   B C     1 
ATOM   11869 O  O     . ALA   B  1  383  ? -1.372  24.168  85.995  1.00 15.35 ? 381  ALA   B O     1 
ATOM   11870 C  CB    . ALA   B  1  383  ? -3.272  22.772  88.270  1.00 15.51 ? 381  ALA   B CB    1 
ATOM   11871 N  N     . GLN   B  1  384  ? -2.262  25.670  87.424  1.00 13.85 ? 382  GLN   B N     1 
ATOM   11872 C  CA    . GLN   B  1  384  ? -2.177  26.754  86.456  1.00 15.24 ? 382  GLN   B CA    1 
ATOM   11873 C  C     . GLN   B  1  384  ? -0.732  27.105  86.154  1.00 14.89 ? 382  GLN   B C     1 
ATOM   11874 O  O     . GLN   B  1  384  ? -0.352  27.225  84.986  1.00 15.22 ? 382  GLN   B O     1 
ATOM   11875 C  CB    . GLN   B  1  384  ? -2.940  27.976  86.955  1.00 14.25 ? 382  GLN   B CB    1 
ATOM   11876 C  CG    . GLN   B  1  384  ? -4.432  27.769  86.930  1.00 14.96 ? 382  GLN   B CG    1 
ATOM   11877 C  CD    . GLN   B  1  384  ? -5.153  29.011  87.298  1.00 15.27 ? 382  GLN   B CD    1 
ATOM   11878 O  OE1   . GLN   B  1  384  ? -4.572  29.899  87.916  1.00 17.73 ? 382  GLN   B OE1   1 
ATOM   11879 N  NE2   . GLN   B  1  384  ? -6.435  29.092  86.951  1.00 15.85 ? 382  GLN   B NE2   1 
ATOM   11880 N  N     . LEU   B  1  385  ? 0.096   27.257  87.192  1.00 14.43 ? 383  LEU   B N     1 
ATOM   11881 C  CA    . LEU   B  1  385  ? 1.502   27.569  86.965  1.00 13.98 ? 383  LEU   B CA    1 
ATOM   11882 C  C     . LEU   B  1  385  ? 2.165   26.512  86.111  1.00 15.70 ? 383  LEU   B C     1 
ATOM   11883 O  O     . LEU   B  1  385  ? 3.027   26.829  85.274  1.00 15.27 ? 383  LEU   B O     1 
ATOM   11884 C  CB    . LEU   B  1  385  ? 2.250   27.662  88.290  1.00 15.71 ? 383  LEU   B CB    1 
ATOM   11885 C  CG    . LEU   B  1  385  ? 1.948   28.855  89.175  1.00 18.59 ? 383  LEU   B CG    1 
ATOM   11886 C  CD1   . LEU   B  1  385  ? 2.784   28.708  90.416  1.00 20.13 ? 383  LEU   B CD1   1 
ATOM   11887 C  CD2   . LEU   B  1  385  ? 2.286   30.131  88.432  1.00 20.68 ? 383  LEU   B CD2   1 
ATOM   11888 N  N     . ASP   B  1  386  ? 1.821   25.249  86.337  1.00 14.70 ? 384  ASP   B N     1 
ATOM   11889 C  CA    . ASP   B  1  386  ? 2.514   24.154  85.671  1.00 14.42 ? 384  ASP   B CA    1 
ATOM   11890 C  C     . ASP   B  1  386  ? 1.932   23.824  84.311  1.00 16.39 ? 384  ASP   B C     1 
ATOM   11891 O  O     . ASP   B  1  386  ? 2.452   22.938  83.632  1.00 16.71 ? 384  ASP   B O     1 
ATOM   11892 C  CB    . ASP   B  1  386  ? 2.590   22.915  86.584  1.00 16.90 ? 384  ASP   B CB    1 
ATOM   11893 C  CG    . ASP   B  1  386  ? 3.491   23.133  87.807  1.00 20.78 ? 384  ASP   B CG    1 
ATOM   11894 O  OD1   . ASP   B  1  386  ? 4.212   24.156  87.870  1.00 22.42 ? 384  ASP   B OD1   1 
ATOM   11895 O  OD2   . ASP   B  1  386  ? 3.494   22.264  88.713  1.00 22.78 ? 384  ASP   B OD2   1 
ATOM   11896 N  N     . GLY   B  1  387  ? 0.864   24.501  83.905  1.00 14.53 ? 385  GLY   B N     1 
ATOM   11897 C  CA    . GLY   B  1  387  ? 0.275   24.261  82.608  1.00 14.53 ? 385  GLY   B CA    1 
ATOM   11898 C  C     . GLY   B  1  387  ? -0.229  22.849  82.431  1.00 16.74 ? 385  GLY   B C     1 
ATOM   11899 O  O     . GLY   B  1  387  ? -0.119  22.284  81.334  1.00 17.19 ? 385  GLY   B O     1 
ATOM   11900 N  N     . LEU   B  1  388  ? -0.781  22.259  83.486  1.00 16.47 ? 386  LEU   B N     1 
ATOM   11901 C  CA    . LEU   B  1  388  ? -1.163  20.860  83.400  1.00 17.52 ? 386  LEU   B CA    1 
ATOM   11902 C  C     . LEU   B  1  388  ? -2.570  20.712  82.829  1.00 17.51 ? 386  LEU   B C     1 
ATOM   11903 O  O     . LEU   B  1  388  ? -3.309  21.684  82.652  1.00 16.54 ? 386  LEU   B O     1 
ATOM   11904 C  CB    . LEU   B  1  388  ? -0.981  20.162  84.743  1.00 17.42 ? 386  LEU   B CB    1 
ATOM   11905 C  CG    . LEU   B  1  388  ? 0.477   20.258  85.175  1.00 16.76 ? 386  LEU   B CG    1 
ATOM   11906 C  CD1   . LEU   B  1  388  ? 0.692   19.589  86.524  1.00 20.01 ? 386  LEU   B CD1   1 
ATOM   11907 C  CD2   . LEU   B  1  388  ? 1.422   19.645  84.141  1.00 19.09 ? 386  LEU   B CD2   1 
ATOM   11908 N  N     . ALA   B  1  389  ? -2.941  19.465  82.530  1.00 17.41 ? 387  ALA   B N     1 
ATOM   11909 C  CA    . ALA   B  1  389  ? -4.135  19.249  81.717  1.00 17.97 ? 387  ALA   B CA    1 
ATOM   11910 C  C     . ALA   B  1  389  ? -5.400  19.702  82.422  1.00 16.61 ? 387  ALA   B C     1 
ATOM   11911 O  O     . ALA   B  1  389  ? -6.340  20.179  81.778  1.00 19.82 ? 387  ALA   B O     1 
ATOM   11912 C  CB    . ALA   B  1  389  ? -4.262  17.776  81.325  1.00 21.15 ? 387  ALA   B CB    1 
ATOM   11913 N  N     . ASP   B  1  390  ? -5.444  19.545  83.733  1.00 16.85 ? 388  ASP   B N     1 
ATOM   11914 C  CA    . ASP   B  1  390  ? -6.613  19.906  84.516  1.00 15.90 ? 388  ASP   B CA    1 
ATOM   11915 C  C     . ASP   B  1  390  ? -6.137  19.970  85.953  1.00 14.82 ? 388  ASP   B C     1 
ATOM   11916 O  O     . ASP   B  1  390  ? -4.962  19.734  86.251  1.00 16.17 ? 388  ASP   B O     1 
ATOM   11917 C  CB    . ASP   B  1  390  ? -7.717  18.851  84.331  1.00 17.23 ? 388  ASP   B CB    1 
ATOM   11918 C  CG    . ASP   B  1  390  ? -9.123  19.400  84.524  1.00 18.48 ? 388  ASP   B CG    1 
ATOM   11919 O  OD1   . ASP   B  1  390  ? -9.373  20.147  85.490  1.00 18.12 ? 388  ASP   B OD1   1 
ATOM   11920 O  OD2   . ASP   B  1  390  ? -9.993  19.065  83.694  1.00 22.15 ? 388  ASP   B OD2   1 
ATOM   11921 N  N     . PHE   B  1  391  ? -7.058  20.292  86.839  1.00 16.51 ? 389  PHE   B N     1 
ATOM   11922 C  CA    . PHE   B  1  391  ? -6.764  20.308  88.253  1.00 15.33 ? 389  PHE   B CA    1 
ATOM   11923 C  C     . PHE   B  1  391  ? -6.859  18.905  88.839  1.00 15.44 ? 389  PHE   B C     1 
ATOM   11924 O  O     . PHE   B  1  391  ? -7.582  18.051  88.320  1.00 16.32 ? 389  PHE   B O     1 
ATOM   11925 C  CB    . PHE   B  1  391  ? -7.760  21.225  88.949  1.00 16.45 ? 389  PHE   B CB    1 
ATOM   11926 C  CG    . PHE   B  1  391  ? -7.730  22.606  88.392  1.00 14.67 ? 389  PHE   B CG    1 
ATOM   11927 C  CD1   . PHE   B  1  391  ? -6.669  23.422  88.694  1.00 14.63 ? 389  PHE   B CD1   1 
ATOM   11928 C  CD2   . PHE   B  1  391  ? -8.686  23.045  87.499  1.00 15.72 ? 389  PHE   B CD2   1 
ATOM   11929 C  CE1   . PHE   B  1  391  ? -6.575  24.689  88.174  1.00 15.35 ? 389  PHE   B CE1   1 
ATOM   11930 C  CE2   . PHE   B  1  391  ? -8.607  24.319  86.967  1.00 15.14 ? 389  PHE   B CE2   1 
ATOM   11931 C  CZ    . PHE   B  1  391  ? -7.543  25.139  87.300  1.00 15.34 ? 389  PHE   B CZ    1 
ATOM   11932 N  N     . PRO   B  1  392  ? -6.144  18.645  89.931  1.00 14.20 ? 390  PRO   B N     1 
ATOM   11933 C  CA    . PRO   B  1  392  ? -6.282  17.365  90.626  1.00 14.07 ? 390  PRO   B CA    1 
ATOM   11934 C  C     . PRO   B  1  392  ? -7.341  17.417  91.705  1.00 15.86 ? 390  PRO   B C     1 
ATOM   11935 O  O     . PRO   B  1  392  ? -7.503  16.444  92.444  1.00 15.89 ? 390  PRO   B O     1 
ATOM   11936 C  CB    . PRO   B  1  392  ? -4.896  17.202  91.260  1.00 15.96 ? 390  PRO   B CB    1 
ATOM   11937 C  CG    . PRO   B  1  392  ? -4.519  18.622  91.631  1.00 16.85 ? 390  PRO   B CG    1 
ATOM   11938 C  CD    . PRO   B  1  392  ? -5.070  19.477  90.507  1.00 14.16 ? 390  PRO   B CD    1 
ATOM   11939 N  N     . VAL   B  1  393  ? -8.022  18.550  91.801  1.00 16.73 ? 391  VAL   B N     1 
ATOM   11940 C  CA    . VAL   B  1  393  ? -9.112  18.760  92.736  1.00 15.82 ? 391  VAL   B CA    1 
ATOM   11941 C  C     . VAL   B  1  393  ? -10.288 19.311  91.946  1.00 16.16 ? 391  VAL   B C     1 
ATOM   11942 O  O     . VAL   B  1  393  ? -10.137 19.812  90.827  1.00 16.12 ? 391  VAL   B O     1 
ATOM   11943 C  CB    . VAL   B  1  393  ? -8.728  19.737  93.869  1.00 15.64 ? 391  VAL   B CB    1 
ATOM   11944 C  CG1   . VAL   B  1  393  ? -7.605  19.169  94.704  1.00 15.23 ? 391  VAL   B CG1   1 
ATOM   11945 C  CG2   . VAL   B  1  393  ? -8.325  21.086  93.296  1.00 14.94 ? 391  VAL   B CG2   1 
ATOM   11946 N  N     . PHE   B  1  394  ? -11.467 19.232  92.555  1.00 15.87 ? 392  PHE   B N     1 
ATOM   11947 C  CA    . PHE   B  1  394  ? -12.638 19.859  91.965  1.00 14.57 ? 392  PHE   B CA    1 
ATOM   11948 C  C     . PHE   B  1  394  ? -12.530 21.374  92.051  1.00 16.25 ? 392  PHE   B C     1 
ATOM   11949 O  O     . PHE   B  1  394  ? -11.740 21.925  92.825  1.00 16.54 ? 392  PHE   B O     1 
ATOM   11950 C  CB    . PHE   B  1  394  ? -13.906 19.345  92.645  1.00 15.82 ? 392  PHE   B CB    1 
ATOM   11951 C  CG    . PHE   B  1  394  ? -14.042 17.877  92.522  1.00 15.85 ? 392  PHE   B CG    1 
ATOM   11952 C  CD1   . PHE   B  1  394  ? -14.294 17.313  91.286  1.00 17.10 ? 392  PHE   B CD1   1 
ATOM   11953 C  CD2   . PHE   B  1  394  ? -13.848 17.046  93.605  1.00 17.43 ? 392  PHE   B CD2   1 
ATOM   11954 C  CE1   . PHE   B  1  394  ? -14.365 15.951  91.138  1.00 17.20 ? 392  PHE   B CE1   1 
ATOM   11955 C  CE2   . PHE   B  1  394  ? -13.914 15.687  93.460  1.00 16.68 ? 392  PHE   B CE2   1 
ATOM   11956 C  CZ    . PHE   B  1  394  ? -14.173 15.136  92.225  1.00 17.03 ? 392  PHE   B CZ    1 
ATOM   11957 N  N     . THR   B  1  395  ? -13.317 22.052  91.209  1.00 17.12 ? 393  THR   B N     1 
ATOM   11958 C  CA    . THR   B  1  395  ? -13.318 23.508  91.164  1.00 16.08 ? 393  THR   B CA    1 
ATOM   11959 C  C     . THR   B  1  395  ? -14.618 24.130  91.637  1.00 15.16 ? 393  THR   B C     1 
ATOM   11960 O  O     . THR   B  1  395  ? -14.652 25.346  91.820  1.00 18.46 ? 393  THR   B O     1 
ATOM   11961 C  CB    . THR   B  1  395  ? -13.007 24.038  89.763  1.00 16.46 ? 393  THR   B CB    1 
ATOM   11962 O  OG1   . THR   B  1  395  ? -14.010 23.575  88.858  1.00 16.66 ? 393  THR   B OG1   1 
ATOM   11963 C  CG2   . THR   B  1  395  ? -11.636 23.586  89.302  1.00 17.81 ? 393  THR   B CG2   1 
ATOM   11964 N  N     . ARG   B  1  396  ? -15.681 23.352  91.808  1.00 16.20 ? 394  ARG   B N     1 
ATOM   11965 C  CA    . ARG   B  1  396  ? -16.886 23.835  92.470  1.00 17.56 ? 394  ARG   B CA    1 
ATOM   11966 C  C     . ARG   B  1  396  ? -16.985 23.152  93.818  1.00 18.35 ? 394  ARG   B C     1 
ATOM   11967 O  O     . ARG   B  1  396  ? -16.824 21.930  93.920  1.00 18.63 ? 394  ARG   B O     1 
ATOM   11968 C  CB    . ARG   B  1  396  ? -18.153 23.546  91.662  1.00 18.46 ? 394  ARG   B CB    1 
ATOM   11969 C  CG    . ARG   B  1  396  ? -18.170 24.207  90.319  1.00 20.10 ? 394  ARG   B CG    1 
ATOM   11970 C  CD    . ARG   B  1  396  ? -19.543 24.052  89.677  1.00 21.47 ? 394  ARG   B CD    1 
ATOM   11971 N  NE    . ARG   B  1  396  ? -19.462 24.504  88.296  1.00 23.78 ? 394  ARG   B NE    1 
ATOM   11972 C  CZ    . ARG   B  1  396  ? -20.319 25.336  87.722  1.00 25.64 ? 394  ARG   B CZ    1 
ATOM   11973 N  NH1   . ARG   B  1  396  ? -21.386 25.778  88.368  1.00 26.26 ? 394  ARG   B NH1   1 
ATOM   11974 N  NH2   . ARG   B  1  396  ? -20.101 25.729  86.468  1.00 26.62 ? 394  ARG   B NH2   1 
ATOM   11975 N  N     . LYS   B  1  397  ? -17.278 23.942  94.850  1.00 18.72 ? 395  LYS   B N     1 
ATOM   11976 C  CA    . LYS   B  1  397  ? -17.291 23.406  96.199  1.00 18.64 ? 395  LYS   B CA    1 
ATOM   11977 C  C     . LYS   B  1  397  ? -18.339 22.312  96.334  1.00 17.87 ? 395  LYS   B C     1 
ATOM   11978 O  O     . LYS   B  1  397  ? -18.131 21.312  97.028  1.00 19.81 ? 395  LYS   B O     1 
ATOM   11979 C  CB    . LYS   B  1  397  ? -17.537 24.551  97.170  1.00 22.10 ? 395  LYS   B CB    1 
ATOM   11980 C  CG    . LYS   B  1  397  ? -17.217 24.225  98.581  1.00 22.55 ? 395  LYS   B CG    1 
ATOM   11981 C  CD    . LYS   B  1  397  ? -18.453 23.776  99.294  1.00 23.82 ? 395  LYS   B CD    1 
ATOM   11982 C  CE    . LYS   B  1  397  ? -18.113 23.420  100.712 1.00 22.34 ? 395  LYS   B CE    1 
ATOM   11983 N  NZ    . LYS   B  1  397  ? -19.318 22.920  101.405 1.00 22.61 ? 395  LYS   B NZ    1 
ATOM   11984 N  N     . ILE   B  1  398  ? -19.468 22.474  95.645  1.00 19.35 ? 396  ILE   B N     1 
ATOM   11985 C  CA    . ILE   B  1  398  ? -20.522 21.469  95.704  1.00 23.20 ? 396  ILE   B CA    1 
ATOM   11986 C  C     . ILE   B  1  398  ? -20.048 20.135  95.128  1.00 18.14 ? 396  ILE   B C     1 
ATOM   11987 O  O     . ILE   B  1  398  ? -20.517 19.065  95.543  1.00 20.01 ? 396  ILE   B O     1 
ATOM   11988 C  CB    . ILE   B  1  398  ? -21.775 22.025  95.001  1.00 25.08 ? 396  ILE   B CB    1 
ATOM   11989 C  CG1   . ILE   B  1  398  ? -22.986 21.179  95.321  1.00 30.52 ? 396  ILE   B CG1   1 
ATOM   11990 C  CG2   . ILE   B  1  398  ? -21.567 22.108  93.505  1.00 22.96 ? 396  ILE   B CG2   1 
ATOM   11991 C  CD1   . ILE   B  1  398  ? -24.265 21.894  95.010  1.00 30.59 ? 396  ILE   B CD1   1 
ATOM   11992 N  N     . HIS   B  1  399  ? -19.070 20.167  94.217  1.00 19.26 ? 397  HIS   B N     1 
ATOM   11993 C  CA    . HIS   B  1  399  ? -18.524 18.915  93.706  1.00 18.24 ? 397  HIS   B CA    1 
ATOM   11994 C  C     . HIS   B  1  399  ? -17.741 18.176  94.776  1.00 17.33 ? 397  HIS   B C     1 
ATOM   11995 O  O     . HIS   B  1  399  ? -17.854 16.951  94.904  1.00 19.14 ? 397  HIS   B O     1 
ATOM   11996 C  CB    . HIS   B  1  399  ? -17.626 19.200  92.515  1.00 18.14 ? 397  HIS   B CB    1 
ATOM   11997 C  CG    . HIS   B  1  399  ? -18.375 19.697  91.324  1.00 18.71 ? 397  HIS   B CG    1 
ATOM   11998 N  ND1   . HIS   B  1  399  ? -17.743 20.244  90.233  1.00 19.41 ? 397  HIS   B ND1   1 
ATOM   11999 C  CD2   . HIS   B  1  399  ? -19.703 19.727  91.052  1.00 22.16 ? 397  HIS   B CD2   1 
ATOM   12000 C  CE1   . HIS   B  1  399  ? -18.648 20.590  89.333  1.00 20.72 ? 397  HIS   B CE1   1 
ATOM   12001 N  NE2   . HIS   B  1  399  ? -19.845 20.287  89.805  1.00 21.76 ? 397  HIS   B NE2   1 
ATOM   12002 N  N     . THR   B  1  400  ? -16.939 18.904  95.549  1.00 17.95 ? 398  THR   B N     1 
ATOM   12003 C  CA    . THR   B  1  400  ? -16.259 18.279  96.672  1.00 18.17 ? 398  THR   B CA    1 
ATOM   12004 C  C     . THR   B  1  400  ? -17.258 17.687  97.652  1.00 16.65 ? 398  THR   B C     1 
ATOM   12005 O  O     . THR   B  1  400  ? -17.039 16.599  98.194  1.00 19.49 ? 398  THR   B O     1 
ATOM   12006 C  CB    . THR   B  1  400  ? -15.367 19.306  97.356  1.00 17.62 ? 398  THR   B CB    1 
ATOM   12007 O  OG1   . THR   B  1  400  ? -14.289 19.593  96.470  1.00 16.69 ? 398  THR   B OG1   1 
ATOM   12008 C  CG2   . THR   B  1  400  ? -14.822 18.755  98.663  1.00 19.57 ? 398  THR   B CG2   1 
ATOM   12009 N  N     . ASP   B  1  401  ? -18.379 18.386  97.882  1.00 19.04 ? 399  ASP   B N     1 
ATOM   12010 C  CA    . ASP   B  1  401  ? -19.389 17.870  98.801  1.00 21.38 ? 399  ASP   B CA    1 
ATOM   12011 C  C     . ASP   B  1  401  ? -19.992 16.578  98.277  1.00 19.91 ? 399  ASP   B C     1 
ATOM   12012 O  O     . ASP   B  1  401  ? -20.176 15.620  99.030  1.00 20.95 ? 399  ASP   B O     1 
ATOM   12013 C  CB    . ASP   B  1  401  ? -20.497 18.906  99.005  1.00 22.12 ? 399  ASP   B CB    1 
ATOM   12014 C  CG    . ASP   B  1  401  ? -20.052 20.086  99.845  1.00 26.04 ? 399  ASP   B CG    1 
ATOM   12015 O  OD1   . ASP   B  1  401  ? -19.085 19.941  100.633 1.00 23.01 ? 399  ASP   B OD1   1 
ATOM   12016 O  OD2   . ASP   B  1  401  ? -20.673 21.163  99.732  1.00 25.60 ? 399  ASP   B OD2   1 
ATOM   12017 N  N     . VAL   B  1  402  ? -20.280 16.526  96.975  1.00 19.66 ? 400  VAL   B N     1 
ATOM   12018 C  CA    . VAL   B  1  402  ? -20.827 15.304  96.401  1.00 21.78 ? 400  VAL   B CA    1 
ATOM   12019 C  C     . VAL   B  1  402  ? -19.803 14.191  96.464  1.00 17.87 ? 400  VAL   B C     1 
ATOM   12020 O  O     . VAL   B  1  402  ? -20.122 13.050  96.825  1.00 20.65 ? 400  VAL   B O     1 
ATOM   12021 C  CB    . VAL   B  1  402  ? -21.288 15.552  94.961  1.00 19.96 ? 400  VAL   B CB    1 
ATOM   12022 C  CG1   . VAL   B  1  402  ? -21.642 14.224  94.293  1.00 23.28 ? 400  VAL   B CG1   1 
ATOM   12023 C  CG2   . VAL   B  1  402  ? -22.466 16.523  94.958  1.00 21.64 ? 400  VAL   B CG2   1 
ATOM   12024 N  N     . SER   B  1  403  ? -18.548 14.515  96.142  1.00 17.84 ? 401  SER   B N     1 
ATOM   12025 C  CA    . SER   B  1  403  ? -17.468 13.541  96.238  1.00 19.47 ? 401  SER   B CA    1 
ATOM   12026 C  C     . SER   B  1  403  ? -17.345 12.978  97.648  1.00 16.83 ? 401  SER   B C     1 
ATOM   12027 O  O     . SER   B  1  403  ? -17.218 11.766  97.834  1.00 18.24 ? 401  SER   B O     1 
ATOM   12028 C  CB    . SER   B  1  403  ? -16.162 14.210  95.813  1.00 17.88 ? 401  SER   B CB    1 
ATOM   12029 O  OG    . SER   B  1  403  ? -15.069 13.336  96.007  1.00 18.59 ? 401  SER   B OG    1 
ATOM   12030 N  N     . TYR   B  1  404  ? -17.438 13.844  98.655  1.00 18.40 ? 402  TYR   B N     1 
ATOM   12031 C  CA    . TYR   B  1  404  ? -17.337 13.397  100.039 1.00 19.26 ? 402  TYR   B CA    1 
ATOM   12032 C  C     . TYR   B  1  404  ? -18.448 12.411  100.365 1.00 18.71 ? 402  TYR   B C     1 
ATOM   12033 O  O     . TYR   B  1  404  ? -18.206 11.346  100.942 1.00 20.67 ? 402  TYR   B O     1 
ATOM   12034 C  CB    . TYR   B  1  404  ? -17.414 14.615  100.955 1.00 20.25 ? 402  TYR   B CB    1 
ATOM   12035 C  CG    . TYR   B  1  404  ? -17.054 14.339  102.387 1.00 18.35 ? 402  TYR   B CG    1 
ATOM   12036 C  CD1   . TYR   B  1  404  ? -17.968 13.768  103.257 1.00 20.05 ? 402  TYR   B CD1   1 
ATOM   12037 C  CD2   . TYR   B  1  404  ? -15.795 14.648  102.866 1.00 18.14 ? 402  TYR   B CD2   1 
ATOM   12038 C  CE1   . TYR   B  1  404  ? -17.640 13.531  104.586 1.00 20.98 ? 402  TYR   B CE1   1 
ATOM   12039 C  CE2   . TYR   B  1  404  ? -15.451 14.410  104.176 1.00 18.59 ? 402  TYR   B CE2   1 
ATOM   12040 C  CZ    . TYR   B  1  404  ? -16.376 13.846  105.028 1.00 20.25 ? 402  TYR   B CZ    1 
ATOM   12041 O  OH    . TYR   B  1  404  ? -16.053 13.600  106.349 1.00 22.34 ? 402  TYR   B OH    1 
ATOM   12042 N  N     . ILE   B  1  405  ? -19.679 12.752  99.987  1.00 20.44 ? 403  ILE   B N     1 
ATOM   12043 C  CA    . ILE   B  1  405  ? -20.812 11.882  100.278 1.00 21.77 ? 403  ILE   B CA    1 
ATOM   12044 C  C     . ILE   B  1  405  ? -20.697 10.565  99.518  1.00 20.43 ? 403  ILE   B C     1 
ATOM   12045 O  O     . ILE   B  1  405  ? -20.971 9.492   100.067 1.00 23.27 ? 403  ILE   B O     1 
ATOM   12046 C  CB    . ILE   B  1  405  ? -22.135 12.624  100.011 1.00 23.73 ? 403  ILE   B CB    1 
ATOM   12047 C  CG1   . ILE   B  1  405  ? -22.249 13.820  100.962 1.00 27.43 ? 403  ILE   B CG1   1 
ATOM   12048 C  CG2   . ILE   B  1  405  ? -23.314 11.685  100.172 1.00 24.71 ? 403  ILE   B CG2   1 
ATOM   12049 C  CD1   . ILE   B  1  405  ? -23.337 14.799  100.614 1.00 35.38 ? 403  ILE   B CD1   1 
ATOM   12050 N  N     . ALA   B  1  406  ? -20.265 10.619  98.253  1.00 21.33 ? 404  ALA   B N     1 
ATOM   12051 C  CA    . ALA   B  1  406  ? -20.071 9.388   97.491  1.00 23.07 ? 404  ALA   B CA    1 
ATOM   12052 C  C     . ALA   B  1  406  ? -18.991 8.522   98.111  1.00 21.20 ? 404  ALA   B C     1 
ATOM   12053 O  O     . ALA   B  1  406  ? -19.127 7.295   98.182  1.00 23.59 ? 404  ALA   B O     1 
ATOM   12054 C  CB    . ALA   B  1  406  ? -19.690 9.725   96.050  1.00 21.92 ? 404  ALA   B CB    1 
ATOM   12055 N  N     . CYS   B  1  407  ? -17.909 9.146   98.577  1.00 20.02 ? 405  CYS   B N     1 
ATOM   12056 C  CA    . CYS   B  1  407  ? -16.835 8.386   99.199  1.00 21.19 ? 405  CYS   B CA    1 
ATOM   12057 C  C     . CYS   B  1  407  ? -17.251 7.855   100.561 1.00 18.31 ? 405  CYS   B C     1 
ATOM   12058 O  O     . CYS   B  1  407  ? -16.840 6.755   100.944 1.00 22.98 ? 405  CYS   B O     1 
ATOM   12059 C  CB    . CYS   B  1  407  ? -15.571 9.237   99.253  1.00 20.24 ? 405  CYS   B CB    1 
ATOM   12060 S  SG    . CYS   B  1  407  ? -14.873 9.471   97.576  1.00 24.31 ? 405  CYS   B SG    1 
ATOM   12061 N  N     . ALA   B  1  408  ? -18.104 8.597   101.277 1.00 19.43 ? 406  ALA   B N     1 
ATOM   12062 C  CA    . ALA   B  1  408  ? -18.662 8.087   102.523 1.00 20.56 ? 406  ALA   B CA    1 
ATOM   12063 C  C     . ALA   B  1  408  ? -19.521 6.861   102.268 1.00 21.15 ? 406  ALA   B C     1 
ATOM   12064 O  O     . ALA   B  1  408  ? -19.485 5.900   103.037 1.00 24.50 ? 406  ALA   B O     1 
ATOM   12065 C  CB    . ALA   B  1  408  ? -19.489 9.175   103.200 1.00 23.64 ? 406  ALA   B CB    1 
ATOM   12066 N  N     . ALA   B  1  409  ? -20.284 6.869   101.173 1.00 23.44 ? 407  ALA   B N     1 
ATOM   12067 C  CA    . ALA   B  1  409  ? -21.073 5.690   100.844 1.00 24.88 ? 407  ALA   B CA    1 
ATOM   12068 C  C     . ALA   B  1  409  ? -20.175 4.483   100.630 1.00 22.38 ? 407  ALA   B C     1 
ATOM   12069 O  O     . ALA   B  1  409  ? -20.478 3.383   101.107 1.00 27.73 ? 407  ALA   B O     1 
ATOM   12070 C  CB    . ALA   B  1  409  ? -21.949 5.959   99.620  1.00 23.06 ? 407  ALA   B CB    1 
ATOM   12071 N  N     . LYS   B  1  410  ? -19.050 4.680   99.937  1.00 22.77 ? 408  LYS   B N     1 
ATOM   12072 C  CA    . LYS   B  1  410  ? -18.101 3.595   99.732  1.00 20.36 ? 408  LYS   B CA    1 
ATOM   12073 C  C     . LYS   B  1  410  ? -17.508 3.135   101.053 1.00 24.64 ? 408  LYS   B C     1 
ATOM   12074 O  O     . LYS   B  1  410  ? -17.388 1.930   101.303 1.00 26.80 ? 408  LYS   B O     1 
ATOM   12075 C  CB    . LYS   B  1  410  ? -16.992 4.051   98.784  1.00 24.49 ? 408  LYS   B CB    1 
ATOM   12076 C  CG    . LYS   B  1  410  ? -15.963 2.973   98.461  1.00 24.93 ? 408  LYS   B CG    1 
ATOM   12077 C  CD    . LYS   B  1  410  ? -14.789 3.503   97.656  1.00 25.08 ? 408  LYS   B CD    1 
ATOM   12078 C  CE    . LYS   B  1  410  ? -15.194 3.969   96.269  1.00 26.34 ? 408  LYS   B CE    1 
ATOM   12079 N  NZ    . LYS   B  1  410  ? -15.478 2.822   95.351  1.00 28.69 ? 408  LYS   B NZ    1 
ATOM   12080 N  N     . LEU   B  1  411  ? -17.131 4.085   101.910 1.00 24.45 ? 409  LEU   B N     1 
ATOM   12081 C  CA    . LEU   B  1  411  ? -16.563 3.722   103.203 1.00 23.90 ? 409  LEU   B CA    1 
ATOM   12082 C  C     . LEU   B  1  411  ? -17.587 3.028   104.086 1.00 23.65 ? 409  LEU   B C     1 
ATOM   12083 O  O     . LEU   B  1  411  ? -17.267 2.032   104.734 1.00 24.20 ? 409  LEU   B O     1 
ATOM   12084 C  CB    . LEU   B  1  411  ? -16.000 4.959   103.892 1.00 21.71 ? 409  LEU   B CB    1 
ATOM   12085 C  CG    . LEU   B  1  411  ? -14.652 5.410   103.338 1.00 22.86 ? 409  LEU   B CG    1 
ATOM   12086 C  CD1   . LEU   B  1  411  ? -14.334 6.817   103.814 1.00 23.32 ? 409  LEU   B CD1   1 
ATOM   12087 C  CD2   . LEU   B  1  411  ? -13.542 4.445   103.741 1.00 24.62 ? 409  LEU   B CD2   1 
ATOM   12088 N  N     . LEU   B  1  412  ? -18.828 3.530   104.112 1.00 24.98 ? 410  LEU   B N     1 
ATOM   12089 C  CA    . LEU   B  1  412  ? -19.840 2.926   104.973 1.00 24.40 ? 410  LEU   B CA    1 
ATOM   12090 C  C     . LEU   B  1  412  ? -20.196 1.519   104.517 1.00 25.51 ? 410  LEU   B C     1 
ATOM   12091 O  O     . LEU   B  1  412  ? -20.637 0.705   105.330 1.00 30.81 ? 410  LEU   B O     1 
ATOM   12092 C  CB    . LEU   B  1  412  ? -21.077 3.818   105.071 1.00 27.79 ? 410  LEU   B CB    1 
ATOM   12093 C  CG    . LEU   B  1  412  ? -20.865 5.064   105.942 1.00 25.10 ? 410  LEU   B CG    1 
ATOM   12094 C  CD1   . LEU   B  1  412  ? -21.993 6.066   105.780 1.00 35.15 ? 410  LEU   B CD1   1 
ATOM   12095 C  CD2   . LEU   B  1  412  ? -20.680 4.674   107.411 1.00 30.30 ? 410  LEU   B CD2   1 
ATOM   12096 N  N     . ALA   B  1  413  ? -20.001 1.209   103.238 1.00 26.76 ? 411  ALA   B N     1 
ATOM   12097 C  CA    . ALA   B  1  413  ? -20.200 -0.158  102.778 1.00 31.22 ? 411  ALA   B CA    1 
ATOM   12098 C  C     . ALA   B  1  413  ? -19.016 -1.052  103.095 1.00 31.47 ? 411  ALA   B C     1 
ATOM   12099 O  O     . ALA   B  1  413  ? -19.086 -2.261  102.859 1.00 31.95 ? 411  ALA   B O     1 
ATOM   12100 C  CB    . ALA   B  1  413  ? -20.468 -0.176  101.273 1.00 28.32 ? 411  ALA   B CB    1 
ATOM   12101 N  N     . ALA   B  1  414  ? -17.938 -0.494  103.645 1.00 27.32 ? 412  ALA   B N     1 
ATOM   12102 C  CA    . ALA   B  1  414  ? -16.726 -1.257  103.905 1.00 23.08 ? 412  ALA   B CA    1 
ATOM   12103 C  C     . ALA   B  1  414  ? -16.309 -1.198  105.374 1.00 27.58 ? 412  ALA   B C     1 
ATOM   12104 O  O     . ALA   B  1  414  ? -15.132 -1.409  105.680 1.00 26.45 ? 412  ALA   B O     1 
ATOM   12105 C  CB    . ALA   B  1  414  ? -15.583 -0.786  103.001 1.00 26.82 ? 412  ALA   B CB    1 
ATOM   12106 N  N     . THR   B  1  415  ? -17.252 -0.939  106.292 1.00 25.95 ? 413  THR   B N     1 
ATOM   12107 C  CA    . THR   B  1  415  ? -16.885 -0.785  107.700 1.00 26.43 ? 413  THR   B CA    1 
ATOM   12108 C  C     . THR   B  1  415  ? -16.374 -2.079  108.298 1.00 27.31 ? 413  THR   B C     1 
ATOM   12109 O  O     . THR   B  1  415  ? -15.723 -2.050  109.351 1.00 28.04 ? 413  THR   B O     1 
ATOM   12110 C  CB    . THR   B  1  415  ? -18.060 -0.275  108.533 1.00 27.14 ? 413  THR   B CB    1 
ATOM   12111 O  OG1   . THR   B  1  415  ? -19.135 -1.215  108.466 1.00 32.08 ? 413  THR   B OG1   1 
ATOM   12112 C  CG2   . THR   B  1  415  ? -18.529 1.065   108.022 1.00 30.66 ? 413  THR   B CG2   1 
ATOM   12113 N  N     . ASP   B  1  416  ? -16.654 -3.212  107.656 1.00 28.50 ? 414  ASP   B N     1 
ATOM   12114 C  CA    . ASP   B  1  416  ? -16.052 -4.475  108.047 1.00 31.24 ? 414  ASP   B CA    1 
ATOM   12115 C  C     . ASP   B  1  416  ? -14.569 -4.541  107.712 1.00 26.85 ? 414  ASP   B C     1 
ATOM   12116 O  O     . ASP   B  1  416  ? -13.879 -5.426  108.224 1.00 31.63 ? 414  ASP   B O     1 
ATOM   12117 C  CB    . ASP   B  1  416  ? -16.812 -5.640  107.388 1.00 28.10 ? 414  ASP   B CB    1 
ATOM   12118 C  CG    . ASP   B  1  416  ? -16.942 -5.485  105.862 1.00 45.15 ? 414  ASP   B CG    1 
ATOM   12119 O  OD1   . ASP   B  1  416  ? -17.281 -4.380  105.379 1.00 37.62 ? 414  ASP   B OD1   1 
ATOM   12120 O  OD2   . ASP   B  1  416  ? -16.709 -6.481  105.141 1.00 47.75 ? 414  ASP   B OD2   1 
ATOM   12121 N  N     . VAL   B  1  417  ? -14.050 -3.613  106.904 1.00 25.94 ? 415  VAL   B N     1 
ATOM   12122 C  CA    . VAL   B  1  417  ? -12.697 -3.717  106.358 1.00 24.44 ? 415  VAL   B CA    1 
ATOM   12123 C  C     . VAL   B  1  417  ? -11.835 -2.516  106.744 1.00 24.56 ? 415  VAL   B C     1 
ATOM   12124 O  O     . VAL   B  1  417  ? -10.613 -2.626  106.888 1.00 25.34 ? 415  VAL   B O     1 
ATOM   12125 C  CB    . VAL   B  1  417  ? -12.768 -3.877  104.827 1.00 30.69 ? 415  VAL   B CB    1 
ATOM   12126 C  CG1   . VAL   B  1  417  ? -11.388 -3.911  104.219 1.00 26.74 ? 415  VAL   B CG1   1 
ATOM   12127 C  CG2   . VAL   B  1  417  ? -13.556 -5.139  104.469 1.00 31.24 ? 415  VAL   B CG2   1 
ATOM   12128 N  N     . VAL   B  1  418  ? -12.456 -1.348  106.855 1.00 22.60 ? 416  VAL   B N     1 
ATOM   12129 C  CA    . VAL   B  1  418  ? -11.764 -0.129  107.238 1.00 21.42 ? 416  VAL   B CA    1 
ATOM   12130 C  C     . VAL   B  1  418  ? -12.608 0.546   108.301 1.00 23.77 ? 416  VAL   B C     1 
ATOM   12131 O  O     . VAL   B  1  418  ? -13.783 0.219   108.496 1.00 23.23 ? 416  VAL   B O     1 
ATOM   12132 C  CB    . VAL   B  1  418  ? -11.524 0.824   106.048 1.00 22.10 ? 416  VAL   B CB    1 
ATOM   12133 C  CG1   . VAL   B  1  418  ? -10.553 0.197   105.054 1.00 22.27 ? 416  VAL   B CG1   1 
ATOM   12134 C  CG2   . VAL   B  1  418  ? -12.850 1.167   105.361 1.00 23.83 ? 416  VAL   B CG2   1 
ATOM   12135 N  N     . PHE   B  1  419  ? -11.981 1.483   109.011 1.00 20.17 ? 417  PHE   B N     1 
ATOM   12136 C  CA    . PHE   B  1  419  ? -12.664 2.242   110.048 1.00 20.21 ? 417  PHE   B CA    1 
ATOM   12137 C  C     . PHE   B  1  419  ? -12.860 3.651   109.521 1.00 19.87 ? 417  PHE   B C     1 
ATOM   12138 O  O     . PHE   B  1  419  ? -11.912 4.454   109.526 1.00 20.38 ? 417  PHE   B O     1 
ATOM   12139 C  CB    . PHE   B  1  419  ? -11.828 2.267   111.329 1.00 21.02 ? 417  PHE   B CB    1 
ATOM   12140 C  CG    . PHE   B  1  419  ? -12.435 3.092   112.415 1.00 22.11 ? 417  PHE   B CG    1 
ATOM   12141 C  CD1   . PHE   B  1  419  ? -13.705 2.814   112.892 1.00 22.85 ? 417  PHE   B CD1   1 
ATOM   12142 C  CD2   . PHE   B  1  419  ? -11.740 4.153   112.961 1.00 22.26 ? 417  PHE   B CD2   1 
ATOM   12143 C  CE1   . PHE   B  1  419  ? -14.270 3.584   113.889 1.00 23.99 ? 417  PHE   B CE1   1 
ATOM   12144 C  CE2   . PHE   B  1  419  ? -12.297 4.922   113.963 1.00 22.00 ? 417  PHE   B CE2   1 
ATOM   12145 C  CZ    . PHE   B  1  419  ? -13.558 4.642   114.430 1.00 21.66 ? 417  PHE   B CZ    1 
ATOM   12146 N  N     . PRO   B  1  420  ? -14.041 3.994   109.024 1.00 19.93 ? 418  PRO   B N     1 
ATOM   12147 C  CA    . PRO   B  1  420  ? -14.228 5.319   108.423 1.00 19.43 ? 418  PRO   B CA    1 
ATOM   12148 C  C     . PRO   B  1  420  ? -14.294 6.399   109.489 1.00 18.94 ? 418  PRO   B C     1 
ATOM   12149 O  O     . PRO   B  1  420  ? -14.941 6.243   110.525 1.00 19.39 ? 418  PRO   B O     1 
ATOM   12150 C  CB    . PRO   B  1  420  ? -15.574 5.185   107.698 1.00 22.18 ? 418  PRO   B CB    1 
ATOM   12151 C  CG    . PRO   B  1  420  ? -15.800 3.703   107.571 1.00 22.09 ? 418  PRO   B CG    1 
ATOM   12152 C  CD    . PRO   B  1  420  ? -15.211 3.131   108.820 1.00 21.62 ? 418  PRO   B CD    1 
ATOM   12153 N  N     . GLN   B  1  421  ? -13.599 7.501   109.230 1.00 19.91 ? 419  GLN   B N     1 
ATOM   12154 C  CA    . GLN   B  1  421  ? -13.559 8.630   110.152 1.00 20.38 ? 419  GLN   B CA    1 
ATOM   12155 C  C     . GLN   B  1  421  ? -13.952 9.861   109.357 1.00 19.14 ? 419  GLN   B C     1 
ATOM   12156 O  O     . GLN   B  1  421  ? -13.197 10.320  108.497 1.00 18.37 ? 419  GLN   B O     1 
ATOM   12157 C  CB    . GLN   B  1  421  ? -12.163 8.776   110.749 1.00 20.28 ? 419  GLN   B CB    1 
ATOM   12158 C  CG    . GLN   B  1  421  ? -11.694 7.501   111.404 1.00 20.14 ? 419  GLN   B CG    1 
ATOM   12159 C  CD    . GLN   B  1  421  ? -10.201 7.487   111.626 1.00 19.28 ? 419  GLN   B CD    1 
ATOM   12160 O  OE1   . GLN   B  1  421  ? -9.432  7.573   110.685 1.00 20.97 ? 419  GLN   B OE1   1 
ATOM   12161 N  NE2   . GLN   B  1  421  ? -9.784  7.401   112.884 1.00 18.80 ? 419  GLN   B NE2   1 
ATOM   12162 N  N     . PHE   B  1  422  ? -15.152 10.374  109.599 1.00 19.72 ? 420  PHE   B N     1 
ATOM   12163 C  CA    . PHE   B  1  422  ? -15.701 11.427  108.754 1.00 18.96 ? 420  PHE   B CA    1 
ATOM   12164 C  C     . PHE   B  1  422  ? -15.390 12.779  109.378 1.00 17.89 ? 420  PHE   B C     1 
ATOM   12165 O  O     . PHE   B  1  422  ? -16.114 13.252  110.258 1.00 19.63 ? 420  PHE   B O     1 
ATOM   12166 C  CB    . PHE   B  1  422  ? -17.193 11.203  108.535 1.00 19.68 ? 420  PHE   B CB    1 
ATOM   12167 C  CG    . PHE   B  1  422  ? -17.495 9.898   107.868 1.00 22.06 ? 420  PHE   B CG    1 
ATOM   12168 C  CD1   . PHE   B  1  422  ? -17.104 9.685   106.564 1.00 21.76 ? 420  PHE   B CD1   1 
ATOM   12169 C  CD2   . PHE   B  1  422  ? -18.149 8.882   108.540 1.00 20.66 ? 420  PHE   B CD2   1 
ATOM   12170 C  CE1   . PHE   B  1  422  ? -17.370 8.477   105.938 1.00 22.66 ? 420  PHE   B CE1   1 
ATOM   12171 C  CE2   . PHE   B  1  422  ? -18.406 7.671   107.914 1.00 24.95 ? 420  PHE   B CE2   1 
ATOM   12172 C  CZ    . PHE   B  1  422  ? -18.022 7.481   106.611 1.00 24.18 ? 420  PHE   B CZ    1 
ATOM   12173 N  N     . ALA   B  1  423  ? -14.302 13.392  108.923 1.00 18.39 ? 421  ALA   B N     1 
ATOM   12174 C  CA    . ALA   B  1  423  ? -13.902 14.709  109.395 1.00 19.70 ? 421  ALA   B CA    1 
ATOM   12175 C  C     . ALA   B  1  423  ? -14.659 15.768  108.613 1.00 19.86 ? 421  ALA   B C     1 
ATOM   12176 O  O     . ALA   B  1  423  ? -14.441 15.935  107.407 1.00 22.88 ? 421  ALA   B O     1 
ATOM   12177 C  CB    . ALA   B  1  423  ? -12.401 14.889  109.193 1.00 19.01 ? 421  ALA   B CB    1 
ATOM   12178 N  N     . THR   B  1  424  ? -15.519 16.514  109.298 1.00 21.44 ? 422  THR   B N     1 
ATOM   12179 C  CA    . THR   B  1  424  ? -16.229 17.610  108.655 1.00 20.39 ? 422  THR   B CA    1 
ATOM   12180 C  C     . THR   B  1  424  ? -16.848 18.485  109.731 1.00 19.53 ? 422  THR   B C     1 
ATOM   12181 O  O     . THR   B  1  424  ? -17.243 17.999  110.798 1.00 21.70 ? 422  THR   B O     1 
ATOM   12182 C  CB    . THR   B  1  424  ? -17.328 17.108  107.701 1.00 24.24 ? 422  THR   B CB    1 
ATOM   12183 O  OG1   . THR   B  1  424  ? -17.975 18.233  107.099 1.00 24.03 ? 422  THR   B OG1   1 
ATOM   12184 C  CG2   . THR   B  1  424  ? -18.375 16.277  108.452 1.00 22.08 ? 422  THR   B CG2   1 
ATOM   12185 N  N     . HIS   B  1  425  ? -16.909 19.779  109.443 1.00 21.14 ? 423  HIS   B N     1 
ATOM   12186 C  CA    . HIS   B  1  425  ? -17.641 20.720  110.281 1.00 20.87 ? 423  HIS   B CA    1 
ATOM   12187 C  C     . HIS   B  1  425  ? -18.979 21.101  109.682 1.00 24.16 ? 423  HIS   B C     1 
ATOM   12188 O  O     . HIS   B  1  425  ? -19.684 21.937  110.249 1.00 24.33 ? 423  HIS   B O     1 
ATOM   12189 C  CB    . HIS   B  1  425  ? -16.801 21.970  110.516 1.00 21.78 ? 423  HIS   B CB    1 
ATOM   12190 C  CG    . HIS   B  1  425  ? -15.545 21.700  111.274 1.00 22.60 ? 423  HIS   B CG    1 
ATOM   12191 N  ND1   . HIS   B  1  425  ? -14.327 22.213  110.890 1.00 24.08 ? 423  HIS   B ND1   1 
ATOM   12192 C  CD2   . HIS   B  1  425  ? -15.311 20.943  112.371 1.00 23.31 ? 423  HIS   B CD2   1 
ATOM   12193 C  CE1   . HIS   B  1  425  ? -13.398 21.808  111.739 1.00 21.53 ? 423  HIS   B CE1   1 
ATOM   12194 N  NE2   . HIS   B  1  425  ? -13.966 21.028  112.639 1.00 21.28 ? 423  HIS   B NE2   1 
ATOM   12195 N  N     . ASN   B  1  426  ? -19.336 20.509  108.549 1.00 23.19 ? 424  ASN   B N     1 
ATOM   12196 C  CA    . ASN   B  1  426  ? -20.538 20.862  107.814 1.00 23.39 ? 424  ASN   B CA    1 
ATOM   12197 C  C     . ASN   B  1  426  ? -21.689 19.992  108.305 1.00 24.92 ? 424  ASN   B C     1 
ATOM   12198 O  O     . ASN   B  1  426  ? -21.668 18.769  108.135 1.00 22.29 ? 424  ASN   B O     1 
ATOM   12199 C  CB    . ASN   B  1  426  ? -20.260 20.604  106.339 1.00 23.26 ? 424  ASN   B CB    1 
ATOM   12200 C  CG    . ASN   B  1  426  ? -21.350 21.121  105.439 1.00 24.33 ? 424  ASN   B CG    1 
ATOM   12201 O  OD1   . ASN   B  1  426  ? -22.537 20.896  105.683 1.00 26.03 ? 424  ASN   B OD1   1 
ATOM   12202 N  ND2   . ASN   B  1  426  ? -20.950 21.819  104.380 1.00 23.37 ? 424  ASN   B ND2   1 
ATOM   12203 N  N     . ALA   B  1  427  ? -22.692 20.627  108.929 1.00 25.52 ? 425  ALA   B N     1 
ATOM   12204 C  CA    . ALA   B  1  427  ? -23.815 19.887  109.494 1.00 27.82 ? 425  ALA   B CA    1 
ATOM   12205 C  C     . ALA   B  1  427  ? -24.631 19.182  108.422 1.00 22.54 ? 425  ALA   B C     1 
ATOM   12206 O  O     . ALA   B  1  427  ? -25.241 18.139  108.696 1.00 26.02 ? 425  ALA   B O     1 
ATOM   12207 C  CB    . ALA   B  1  427  ? -24.713 20.830  110.296 1.00 29.86 ? 425  ALA   B CB    1 
ATOM   12208 N  N     . GLN   B  1  428  ? -24.657 19.730  107.208 1.00 24.76 ? 426  GLN   B N     1 
ATOM   12209 C  CA    . GLN   B  1  428  ? -25.355 19.042  106.131 1.00 26.27 ? 426  GLN   B CA    1 
ATOM   12210 C  C     . GLN   B  1  428  ? -24.617 17.767  105.744 1.00 24.84 ? 426  GLN   B C     1 
ATOM   12211 O  O     . GLN   B  1  428  ? -25.226 16.699  105.610 1.00 26.37 ? 426  GLN   B O     1 
ATOM   12212 C  CB    . GLN   B  1  428  ? -25.549 19.976  104.938 1.00 26.00 ? 426  GLN   B CB    1 
ATOM   12213 C  CG    . GLN   B  1  428  ? -26.590 19.483  103.944 1.00 27.95 ? 426  GLN   B CG    1 
ATOM   12214 C  CD    . GLN   B  1  428  ? -26.078 18.349  103.077 1.00 27.54 ? 426  GLN   B CD    1 
ATOM   12215 O  OE1   . GLN   B  1  428  ? -24.891 18.298  102.745 1.00 29.32 ? 426  GLN   B OE1   1 
ATOM   12216 N  NE2   . GLN   B  1  428  ? -26.965 17.424  102.719 1.00 31.92 ? 426  GLN   B NE2   1 
ATOM   12217 N  N     . THR   B  1  429  ? -23.291 17.856  105.591 1.00 25.69 ? 427  THR   B N     1 
ATOM   12218 C  CA    . THR   B  1  429  ? -22.506 16.666  105.285 1.00 25.41 ? 427  THR   B CA    1 
ATOM   12219 C  C     . THR   B  1  429  ? -22.656 15.626  106.382 1.00 22.75 ? 427  THR   B C     1 
ATOM   12220 O  O     . THR   B  1  429  ? -22.871 14.438  106.108 1.00 25.74 ? 427  THR   B O     1 
ATOM   12221 C  CB    . THR   B  1  429  ? -21.033 17.045  105.151 1.00 22.62 ? 427  THR   B CB    1 
ATOM   12222 O  OG1   . THR   B  1  429  ? -20.888 18.165  104.273 1.00 23.85 ? 427  THR   B OG1   1 
ATOM   12223 C  CG2   . THR   B  1  429  ? -20.250 15.874  104.609 1.00 26.87 ? 427  THR   B CG2   1 
ATOM   12224 N  N     . LEU   B  1  430  ? -22.523 16.060  107.637 1.00 25.34 ? 428  LEU   B N     1 
ATOM   12225 C  CA    . LEU   B  1  430  ? -22.655 15.158  108.774 1.00 24.97 ? 428  LEU   B CA    1 
ATOM   12226 C  C     . LEU   B  1  430  ? -24.010 14.460  108.764 1.00 27.40 ? 428  LEU   B C     1 
ATOM   12227 O  O     . LEU   B  1  430  ? -24.090 13.238  108.922 1.00 25.99 ? 428  LEU   B O     1 
ATOM   12228 C  CB    . LEU   B  1  430  ? -22.482 15.957  110.067 1.00 27.78 ? 428  LEU   B CB    1 
ATOM   12229 C  CG    . LEU   B  1  430  ? -22.326 15.279  111.437 1.00 27.29 ? 428  LEU   B CG    1 
ATOM   12230 C  CD1   . LEU   B  1  430  ? -21.949 16.347  112.434 1.00 29.50 ? 428  LEU   B CD1   1 
ATOM   12231 C  CD2   . LEU   B  1  430  ? -23.564 14.538  111.915 1.00 31.14 ? 428  LEU   B CD2   1 
ATOM   12232 N  N     . ALA   B  1  431  ? -25.089 15.232  108.594 1.00 28.70 ? 429  ALA   B N     1 
ATOM   12233 C  CA    . ALA   B  1  431  ? -26.435 14.664  108.628 1.00 30.25 ? 429  ALA   B CA    1 
ATOM   12234 C  C     . ALA   B  1  431  ? -26.620 13.628  107.530 1.00 27.87 ? 429  ALA   B C     1 
ATOM   12235 O  O     . ALA   B  1  431  ? -27.210 12.566  107.762 1.00 28.97 ? 429  ALA   B O     1 
ATOM   12236 C  CB    . ALA   B  1  431  ? -27.471 15.776  108.482 1.00 28.81 ? 429  ALA   B CB    1 
ATOM   12237 N  N     . ALA   B  1  432  ? -26.093 13.910  106.334 1.00 28.72 ? 430  ALA   B N     1 
ATOM   12238 C  CA    . ALA   B  1  432  ? -26.210 12.966  105.227 1.00 26.84 ? 430  ALA   B CA    1 
ATOM   12239 C  C     . ALA   B  1  432  ? -25.539 11.646  105.571 1.00 28.01 ? 430  ALA   B C     1 
ATOM   12240 O  O     . ALA   B  1  432  ? -26.087 10.572  105.320 1.00 29.80 ? 430  ALA   B O     1 
ATOM   12241 C  CB    . ALA   B  1  432  ? -25.597 13.570  103.961 1.00 28.80 ? 430  ALA   B CB    1 
ATOM   12242 N  N     . ILE   B  1  433  ? -24.339 11.710  106.152 1.00 26.56 ? 431  ILE   B N     1 
ATOM   12243 C  CA    . ILE   B  1  433  ? -23.632 10.484  106.507 1.00 30.31 ? 431  ILE   B CA    1 
ATOM   12244 C  C     . ILE   B  1  433  ? -24.289 9.790   107.692 1.00 26.47 ? 431  ILE   B C     1 
ATOM   12245 O  O     . ILE   B  1  433  ? -24.385 8.557   107.732 1.00 26.70 ? 431  ILE   B O     1 
ATOM   12246 C  CB    . ILE   B  1  433  ? -22.154 10.801  106.766 1.00 27.92 ? 431  ILE   B CB    1 
ATOM   12247 C  CG1   . ILE   B  1  433  ? -21.488 11.151  105.445 1.00 33.02 ? 431  ILE   B CG1   1 
ATOM   12248 C  CG2   . ILE   B  1  433  ? -21.459 9.644   107.465 1.00 32.43 ? 431  ILE   B CG2   1 
ATOM   12249 C  CD1   . ILE   B  1  433  ? -20.148 11.681  105.621 1.00 32.68 ? 431  ILE   B CD1   1 
ATOM   12250 N  N     . TYR   B  1  434  ? -24.723 10.566  108.688 1.00 26.74 ? 432  TYR   B N     1 
ATOM   12251 C  CA    . TYR   B  1  434  ? -25.403 9.992   109.841 1.00 27.90 ? 432  TYR   B CA    1 
ATOM   12252 C  C     . TYR   B  1  434  ? -26.573 9.113   109.414 1.00 28.60 ? 432  TYR   B C     1 
ATOM   12253 O  O     . TYR   B  1  434  ? -26.730 7.992   109.906 1.00 28.46 ? 432  TYR   B O     1 
ATOM   12254 C  CB    . TYR   B  1  434  ? -25.849 11.131  110.758 1.00 29.83 ? 432  TYR   B CB    1 
ATOM   12255 C  CG    . TYR   B  1  434  ? -26.767 10.723  111.878 1.00 29.56 ? 432  TYR   B CG    1 
ATOM   12256 C  CD1   . TYR   B  1  434  ? -26.301 9.982   112.958 1.00 28.71 ? 432  TYR   B CD1   1 
ATOM   12257 C  CD2   . TYR   B  1  434  ? -28.107 11.090  111.863 1.00 32.21 ? 432  TYR   B CD2   1 
ATOM   12258 C  CE1   . TYR   B  1  434  ? -27.146 9.619   113.998 1.00 32.79 ? 432  TYR   B CE1   1 
ATOM   12259 C  CE2   . TYR   B  1  434  ? -28.954 10.735  112.892 1.00 30.02 ? 432  TYR   B CE2   1 
ATOM   12260 C  CZ    . TYR   B  1  434  ? -28.471 9.996   113.952 1.00 33.60 ? 432  TYR   B CZ    1 
ATOM   12261 O  OH    . TYR   B  1  434  ? -29.319 9.639   114.971 1.00 34.41 ? 432  TYR   B OH    1 
ATOM   12262 N  N     . HIS   B  1  435  ? -27.361 9.574   108.448 1.00 31.92 ? 433  HIS   B N     1 
ATOM   12263 C  CA    . HIS   B  1  435  ? -28.487 8.765   108.002 1.00 31.44 ? 433  HIS   B CA    1 
ATOM   12264 C  C     . HIS   B  1  435  ? -28.080 7.698   107.000 1.00 30.68 ? 433  HIS   B C     1 
ATOM   12265 O  O     . HIS   B  1  435  ? -28.641 6.596   107.010 1.00 31.18 ? 433  HIS   B O     1 
ATOM   12266 C  CB    . HIS   B  1  435  ? -29.585 9.664   107.454 1.00 35.62 ? 433  HIS   B CB    1 
ATOM   12267 C  CG    . HIS   B  1  435  ? -30.310 10.403  108.526 1.00 30.82 ? 433  HIS   B CG    1 
ATOM   12268 N  ND1   . HIS   B  1  435  ? -31.312 9.824   109.272 1.00 32.35 ? 433  HIS   B ND1   1 
ATOM   12269 C  CD2   . HIS   B  1  435  ? -30.146 11.652  109.021 1.00 32.92 ? 433  HIS   B CD2   1 
ATOM   12270 C  CE1   . HIS   B  1  435  ? -31.755 10.693  110.162 1.00 37.25 ? 433  HIS   B CE1   1 
ATOM   12271 N  NE2   . HIS   B  1  435  ? -31.071 11.813  110.025 1.00 27.96 ? 433  HIS   B NE2   1 
ATOM   12272 N  N     . MET   B  1  436  ? -27.105 7.998   106.142 1.00 28.94 ? 434  MET   B N     1 
ATOM   12273 C  CA    . MET   B  1  436  ? -26.608 6.983   105.230 1.00 28.11 ? 434  MET   B CA    1 
ATOM   12274 C  C     . MET   B  1  436  ? -26.100 5.759   105.976 1.00 31.05 ? 434  MET   B C     1 
ATOM   12275 O  O     . MET   B  1  436  ? -26.210 4.635   105.473 1.00 32.17 ? 434  MET   B O     1 
ATOM   12276 C  CB    . MET   B  1  436  ? -25.485 7.582   104.394 1.00 29.79 ? 434  MET   B CB    1 
ATOM   12277 C  CG    . MET   B  1  436  ? -24.779 6.593   103.510 1.00 30.36 ? 434  MET   B CG    1 
ATOM   12278 S  SD    . MET   B  1  436  ? -23.396 7.408   102.706 1.00 34.97 ? 434  MET   B SD    1 
ATOM   12279 C  CE    . MET   B  1  436  ? -24.262 8.467   101.558 1.00 31.65 ? 434  MET   B CE    1 
ATOM   12280 N  N     . ALA   B  1  437  ? -25.546 5.953   107.178 1.00 27.51 ? 435  ALA   B N     1 
ATOM   12281 C  CA    . ALA   B  1  437  ? -24.970 4.839   107.921 1.00 29.26 ? 435  ALA   B CA    1 
ATOM   12282 C  C     . ALA   B  1  437  ? -26.030 3.909   108.494 1.00 33.94 ? 435  ALA   B C     1 
ATOM   12283 O  O     . ALA   B  1  437  ? -25.704 2.784   108.886 1.00 36.62 ? 435  ALA   B O     1 
ATOM   12284 C  CB    . ALA   B  1  437  ? -24.076 5.366   109.045 1.00 31.17 ? 435  ALA   B CB    1 
ATOM   12285 N  N     . GLY   B  1  438  ? -27.279 4.349   108.549 1.00 34.27 ? 436  GLY   B N     1 
ATOM   12286 C  CA    . GLY   B  1  438  ? -28.359 3.508   109.021 1.00 36.38 ? 436  GLY   B CA    1 
ATOM   12287 C  C     . GLY   B  1  438  ? -28.495 3.536   110.526 1.00 42.58 ? 436  GLY   B C     1 
ATOM   12288 O  O     . GLY   B  1  438  ? -27.763 4.216   111.253 1.00 38.13 ? 436  GLY   B O     1 
ATOM   12289 N  N     . LYS   B  1  439  ? -29.466 2.755   110.999 1.00 40.63 ? 437  LYS   B N     1 
ATOM   12290 C  CA    . LYS   B  1  439  ? -29.808 2.742   112.415 1.00 40.18 ? 437  LYS   B CA    1 
ATOM   12291 C  C     . LYS   B  1  439  ? -28.826 1.949   113.269 1.00 38.92 ? 437  LYS   B C     1 
ATOM   12292 O  O     . LYS   B  1  439  ? -28.761 2.181   114.481 1.00 46.42 ? 437  LYS   B O     1 
ATOM   12293 C  CB    . LYS   B  1  439  ? -31.219 2.178   112.608 1.00 38.22 ? 437  LYS   B CB    1 
ATOM   12294 N  N     . ASP   B  1  440  ? -28.071 1.022   112.681 1.00 37.39 ? 438  ASP   B N     1 
ATOM   12295 C  CA    . ASP   B  1  440  ? -27.207 0.130   113.446 1.00 41.19 ? 438  ASP   B CA    1 
ATOM   12296 C  C     . ASP   B  1  440  ? -25.870 0.819   113.686 1.00 35.70 ? 438  ASP   B C     1 
ATOM   12297 O  O     . ASP   B  1  440  ? -25.189 1.207   112.731 1.00 42.37 ? 438  ASP   B O     1 
ATOM   12298 C  CB    . ASP   B  1  440  ? -26.990 -1.180  112.691 1.00 42.17 ? 438  ASP   B CB    1 
ATOM   12299 N  N     . PHE   B  1  441  ? -25.497 0.975   114.954 1.00 37.05 ? 439  PHE   B N     1 
ATOM   12300 C  CA    . PHE   B  1  441  ? -24.224 1.606   115.269 1.00 33.25 ? 439  PHE   B CA    1 
ATOM   12301 C  C     . PHE   B  1  441  ? -23.620 1.023   116.535 1.00 34.55 ? 439  PHE   B C     1 
ATOM   12302 O  O     . PHE   B  1  441  ? -24.326 0.712   117.498 1.00 34.48 ? 439  PHE   B O     1 
ATOM   12303 C  CB    . PHE   B  1  441  ? -24.332 3.122   115.439 1.00 32.05 ? 439  PHE   B CB    1 
ATOM   12304 C  CG    . PHE   B  1  441  ? -23.001 3.770   115.682 1.00 30.58 ? 439  PHE   B CG    1 
ATOM   12305 C  CD1   . PHE   B  1  441  ? -22.162 4.048   114.617 1.00 29.10 ? 439  PHE   B CD1   1 
ATOM   12306 C  CD2   . PHE   B  1  441  ? -22.556 4.035   116.973 1.00 28.22 ? 439  PHE   B CD2   1 
ATOM   12307 C  CE1   . PHE   B  1  441  ? -20.911 4.618   114.824 1.00 27.94 ? 439  PHE   B CE1   1 
ATOM   12308 C  CE2   . PHE   B  1  441  ? -21.310 4.601   117.189 1.00 29.25 ? 439  PHE   B CE2   1 
ATOM   12309 C  CZ    . PHE   B  1  441  ? -20.484 4.887   116.110 1.00 28.52 ? 439  PHE   B CZ    1 
ATOM   12310 N  N     . HIS   B  1  442  ? -22.298 0.909   116.527 1.00 34.09 ? 440  HIS   B N     1 
ATOM   12311 C  CA    . HIS   B  1  442  ? -21.528 0.610   117.718 1.00 31.58 ? 440  HIS   B CA    1 
ATOM   12312 C  C     . HIS   B  1  442  ? -20.208 1.350   117.592 1.00 29.21 ? 440  HIS   B C     1 
ATOM   12313 O  O     . HIS   B  1  442  ? -19.744 1.623   116.481 1.00 30.57 ? 440  HIS   B O     1 
ATOM   12314 C  CB    . HIS   B  1  442  ? -21.262 -0.889  117.816 1.00 33.18 ? 440  HIS   B CB    1 
ATOM   12315 C  CG    . HIS   B  1  442  ? -20.671 -1.468  116.571 1.00 38.39 ? 440  HIS   B CG    1 
ATOM   12316 N  ND1   . HIS   B  1  442  ? -19.312 -1.502  116.338 1.00 42.03 ? 440  HIS   B ND1   1 
ATOM   12317 C  CD2   . HIS   B  1  442  ? -21.257 -2.013  115.477 1.00 37.78 ? 440  HIS   B CD2   1 
ATOM   12318 C  CE1   . HIS   B  1  442  ? -19.085 -2.056  115.160 1.00 41.47 ? 440  HIS   B CE1   1 
ATOM   12319 N  NE2   . HIS   B  1  442  ? -20.248 -2.378  114.619 1.00 42.24 ? 440  HIS   B NE2   1 
ATOM   12320 N  N     . VAL   B  1  443  ? -19.608 1.684   118.736 1.00 30.00 ? 441  VAL   B N     1 
ATOM   12321 C  CA    . VAL   B  1  443  ? -18.282 2.287   118.698 1.00 29.63 ? 441  VAL   B CA    1 
ATOM   12322 C  C     . VAL   B  1  443  ? -17.324 1.328   118.013 1.00 27.72 ? 441  VAL   B C     1 
ATOM   12323 O  O     . VAL   B  1  443  ? -17.315 0.123   118.289 1.00 31.75 ? 441  VAL   B O     1 
ATOM   12324 C  CB    . VAL   B  1  443  ? -17.805 2.659   120.108 1.00 32.82 ? 441  VAL   B CB    1 
ATOM   12325 C  CG1   . VAL   B  1  443  ? -16.323 2.994   120.074 1.00 30.97 ? 441  VAL   B CG1   1 
ATOM   12326 C  CG2   . VAL   B  1  443  ? -18.606 3.839   120.640 1.00 33.87 ? 441  VAL   B CG2   1 
ATOM   12327 N  N     . GLY   B  1  444  ? -16.521 1.860   117.100 1.00 27.80 ? 442  GLY   B N     1 
ATOM   12328 C  CA    . GLY   B  1  444  ? -15.668 1.048   116.267 1.00 27.88 ? 442  GLY   B CA    1 
ATOM   12329 C  C     . GLY   B  1  444  ? -16.202 0.822   114.870 1.00 27.32 ? 442  GLY   B C     1 
ATOM   12330 O  O     . GLY   B  1  444  ? -15.443 0.370   114.006 1.00 26.51 ? 442  GLY   B O     1 
ATOM   12331 N  N     . LYS   B  1  445  ? -17.480 1.119   114.623 1.00 26.48 ? 443  LYS   B N     1 
ATOM   12332 C  CA    . LYS   B  1  445  ? -18.004 0.999   113.266 1.00 25.37 ? 443  LYS   B CA    1 
ATOM   12333 C  C     . LYS   B  1  445  ? -17.483 2.133   112.391 1.00 26.00 ? 443  LYS   B C     1 
ATOM   12334 O  O     . LYS   B  1  445  ? -16.924 1.899   111.315 1.00 25.74 ? 443  LYS   B O     1 
ATOM   12335 C  CB    . LYS   B  1  445  ? -19.534 0.975   113.278 1.00 26.73 ? 443  LYS   B CB    1 
ATOM   12336 C  CG    . LYS   B  1  445  ? -20.140 0.737   111.900 1.00 30.61 ? 443  LYS   B CG    1 
ATOM   12337 C  CD    . LYS   B  1  445  ? -21.657 0.667   111.961 1.00 35.75 ? 443  LYS   B CD    1 
ATOM   12338 C  CE    . LYS   B  1  445  ? -22.259 0.460   110.581 1.00 41.30 ? 443  LYS   B CE    1 
ATOM   12339 N  NZ    . LYS   B  1  445  ? -23.737 0.260   110.672 1.00 41.18 ? 443  LYS   B NZ    1 
ATOM   12340 N  N     . TYR   B  1  446  ? -17.675 3.368   112.838 1.00 23.09 ? 444  TYR   B N     1 
ATOM   12341 C  CA    . TYR   B  1  446  ? -17.139 4.557   112.194 1.00 22.44 ? 444  TYR   B CA    1 
ATOM   12342 C  C     . TYR   B  1  446  ? -17.199 5.659   113.238 1.00 24.44 ? 444  TYR   B C     1 
ATOM   12343 O  O     . TYR   B  1  446  ? -17.823 5.502   114.288 1.00 23.39 ? 444  TYR   B O     1 
ATOM   12344 C  CB    . TYR   B  1  446  ? -17.936 4.929   110.938 1.00 23.06 ? 444  TYR   B CB    1 
ATOM   12345 C  CG    . TYR   B  1  446  ? -19.341 5.436   111.207 1.00 28.05 ? 444  TYR   B CG    1 
ATOM   12346 C  CD1   . TYR   B  1  446  ? -19.584 6.790   111.421 1.00 24.57 ? 444  TYR   B CD1   1 
ATOM   12347 C  CD2   . TYR   B  1  446  ? -20.426 4.566   111.209 1.00 27.44 ? 444  TYR   B CD2   1 
ATOM   12348 C  CE1   . TYR   B  1  446  ? -20.861 7.256   111.665 1.00 32.69 ? 444  TYR   B CE1   1 
ATOM   12349 C  CE2   . TYR   B  1  446  ? -21.701 5.021   111.454 1.00 31.23 ? 444  TYR   B CE2   1 
ATOM   12350 C  CZ    . TYR   B  1  446  ? -21.913 6.368   111.676 1.00 28.32 ? 444  TYR   B CZ    1 
ATOM   12351 O  OH    . TYR   B  1  446  ? -23.194 6.818   111.912 1.00 41.02 ? 444  TYR   B OH    1 
ATOM   12352 N  N     . GLU   B  1  447  ? -16.553 6.776   112.946 1.00 21.76 ? 445  GLU   B N     1 
ATOM   12353 C  CA    . GLU   B  1  447  ? -16.664 7.919   113.834 1.00 21.64 ? 445  GLU   B CA    1 
ATOM   12354 C  C     . GLU   B  1  447  ? -16.683 9.176   112.995 1.00 19.18 ? 445  GLU   B C     1 
ATOM   12355 O  O     . GLU   B  1  447  ? -16.394 9.159   111.791 1.00 20.79 ? 445  GLU   B O     1 
ATOM   12356 C  CB    . GLU   B  1  447  ? -15.510 7.980   114.840 1.00 20.98 ? 445  GLU   B CB    1 
ATOM   12357 C  CG    . GLU   B  1  447  ? -14.194 8.231   114.148 1.00 20.09 ? 445  GLU   B CG    1 
ATOM   12358 C  CD    . GLU   B  1  447  ? -13.016 8.164   115.086 1.00 20.36 ? 445  GLU   B CD    1 
ATOM   12359 O  OE1   . GLU   B  1  447  ? -13.192 7.744   116.240 1.00 22.38 ? 445  GLU   B OE1   1 
ATOM   12360 O  OE2   . GLU   B  1  447  ? -11.903 8.536   114.653 1.00 20.36 ? 445  GLU   B OE2   1 
ATOM   12361 N  N     . PHE   B  1  448  ? -17.050 10.272  113.629 1.00 21.03 ? 446  PHE   B N     1 
ATOM   12362 C  CA    . PHE   B  1  448  ? -16.824 11.585  113.064 1.00 19.93 ? 446  PHE   B CA    1 
ATOM   12363 C  C     . PHE   B  1  448  ? -15.535 12.145  113.636 1.00 17.78 ? 446  PHE   B C     1 
ATOM   12364 O  O     . PHE   B  1  448  ? -14.994 11.631  114.614 1.00 20.17 ? 446  PHE   B O     1 
ATOM   12365 C  CB    . PHE   B  1  448  ? -17.995 12.505  113.383 1.00 24.04 ? 446  PHE   B CB    1 
ATOM   12366 C  CG    . PHE   B  1  448  ? -19.260 12.082  112.729 1.00 21.43 ? 446  PHE   B CG    1 
ATOM   12367 C  CD1   . PHE   B  1  448  ? -19.500 12.410  111.405 1.00 24.38 ? 446  PHE   B CD1   1 
ATOM   12368 C  CD2   . PHE   B  1  448  ? -20.190 11.324  113.418 1.00 24.31 ? 446  PHE   B CD2   1 
ATOM   12369 C  CE1   . PHE   B  1  448  ? -20.668 12.007  110.779 1.00 23.51 ? 446  PHE   B CE1   1 
ATOM   12370 C  CE2   . PHE   B  1  448  ? -21.355 10.914  112.802 1.00 29.06 ? 446  PHE   B CE2   1 
ATOM   12371 C  CZ    . PHE   B  1  448  ? -21.595 11.257  111.485 1.00 25.88 ? 446  PHE   B CZ    1 
ATOM   12372 N  N     . GLN   B  1  449  ? -15.032 13.190  112.989 1.00 19.45 ? 447  GLN   B N     1 
ATOM   12373 C  CA    . GLN   B  1  449  ? -13.882 13.921  113.503 1.00 18.38 ? 447  GLN   B CA    1 
ATOM   12374 C  C     . GLN   B  1  449  ? -14.095 15.408  113.295 1.00 19.23 ? 447  GLN   B C     1 
ATOM   12375 O  O     . GLN   B  1  449  ? -14.803 15.836  112.376 1.00 19.18 ? 447  GLN   B O     1 
ATOM   12376 C  CB    . GLN   B  1  449  ? -12.566 13.491  112.855 1.00 17.98 ? 447  GLN   B CB    1 
ATOM   12377 C  CG    . GLN   B  1  449  ? -12.303 12.016  112.938 1.00 20.27 ? 447  GLN   B CG    1 
ATOM   12378 C  CD    . GLN   B  1  449  ? -10.847 11.717  112.767 1.00 18.24 ? 447  GLN   B CD    1 
ATOM   12379 O  OE1   . GLN   B  1  449  ? -10.106 12.560  112.268 1.00 22.03 ? 447  GLN   B OE1   1 
ATOM   12380 N  NE2   . GLN   B  1  449  ? -10.422 10.534  113.180 1.00 19.86 ? 447  GLN   B NE2   1 
ATOM   12381 N  N     . CYS   B  1  450  ? -13.463 16.199  114.155 1.00 18.74 ? 448  CYS   B N     1 
ATOM   12382 C  CA    . CYS   B  1  450  ? -13.534 17.641  114.012 1.00 19.11 ? 448  CYS   B CA    1 
ATOM   12383 C  C     . CYS   B  1  450  ? -12.238 18.225  114.532 1.00 18.60 ? 448  CYS   B C     1 
ATOM   12384 O  O     . CYS   B  1  450  ? -11.408 17.524  115.115 1.00 20.18 ? 448  CYS   B O     1 
ATOM   12385 C  CB    . CYS   B  1  450  ? -14.715 18.227  114.799 1.00 19.36 ? 448  CYS   B CB    1 
ATOM   12386 S  SG    . CYS   B  1  450  ? -14.523 18.167  116.610 1.00 22.71 ? 448  CYS   B SG    1 
ATOM   12387 N  N     . LEU   B  1  451  ? -12.088 19.521  114.327 1.00 19.79 ? 449  LEU   B N     1 
ATOM   12388 C  CA    . LEU   B  1  451  ? -10.912 20.239  114.790 1.00 20.78 ? 449  LEU   B CA    1 
ATOM   12389 C  C     . LEU   B  1  451  ? -11.184 20.848  116.156 1.00 23.56 ? 449  LEU   B C     1 
ATOM   12390 O  O     . LEU   B  1  451  ? -12.255 21.406  116.399 1.00 24.33 ? 449  LEU   B O     1 
ATOM   12391 C  CB    . LEU   B  1  451  ? -10.577 21.348  113.799 1.00 21.94 ? 449  LEU   B CB    1 
ATOM   12392 C  CG    . LEU   B  1  451  ? -9.359  22.225  114.050 1.00 25.34 ? 449  LEU   B CG    1 
ATOM   12393 C  CD1   . LEU   B  1  451  ? -8.064  21.402  114.118 1.00 25.22 ? 449  LEU   B CD1   1 
ATOM   12394 C  CD2   . LEU   B  1  451  ? -9.292  23.260  112.949 1.00 29.10 ? 449  LEU   B CD2   1 
ATOM   12395 N  N     . HIS   B  1  452  ? -10.210 20.717  117.055 1.00 19.68 ? 450  HIS   B N     1 
ATOM   12396 C  CA    . HIS   B  1  452  ? -10.286 21.386  118.343 1.00 22.49 ? 450  HIS   B CA    1 
ATOM   12397 C  C     . HIS   B  1  452  ? -10.573 22.867  118.149 1.00 22.90 ? 450  HIS   B C     1 
ATOM   12398 O  O     . HIS   B  1  452  ? -9.998  23.511  117.274 1.00 25.00 ? 450  HIS   B O     1 
ATOM   12399 C  CB    . HIS   B  1  452  ? -8.929  21.269  119.036 1.00 20.41 ? 450  HIS   B CB    1 
ATOM   12400 C  CG    . HIS   B  1  452  ? -8.826  22.120  120.253 1.00 22.33 ? 450  HIS   B CG    1 
ATOM   12401 N  ND1   . HIS   B  1  452  ? -9.359  21.740  121.463 1.00 25.87 ? 450  HIS   B ND1   1 
ATOM   12402 C  CD2   . HIS   B  1  452  ? -8.307  23.355  120.436 1.00 25.08 ? 450  HIS   B CD2   1 
ATOM   12403 C  CE1   . HIS   B  1  452  ? -9.146  22.694  122.353 1.00 26.84 ? 450  HIS   B CE1   1 
ATOM   12404 N  NE2   . HIS   B  1  452  ? -8.518  23.689  121.753 1.00 23.54 ? 450  HIS   B NE2   1 
ATOM   12405 N  N     . GLY   B  1  453  ? -11.440 23.414  119.004 1.00 28.62 ? 451  GLY   B N     1 
ATOM   12406 C  CA    . GLY   B  1  453  ? -11.667 24.850  118.990 1.00 36.37 ? 451  GLY   B CA    1 
ATOM   12407 C  C     . GLY   B  1  453  ? -12.381 25.366  117.763 1.00 40.40 ? 451  GLY   B C     1 
ATOM   12408 O  O     . GLY   B  1  453  ? -12.363 26.573  117.499 1.00 39.89 ? 451  GLY   B O     1 
ATOM   12409 N  N     . MET   B  1  454  ? -12.992 24.475  116.987 1.00 28.33 ? 452  MET   B N     1 
ATOM   12410 C  CA    . MET   B  1  454  ? -13.822 24.858  115.856 1.00 29.17 ? 452  MET   B CA    1 
ATOM   12411 C  C     . MET   B  1  454  ? -15.043 23.956  115.836 1.00 28.62 ? 452  MET   B C     1 
ATOM   12412 O  O     . MET   B  1  454  ? -16.175 24.427  115.685 1.00 30.01 ? 452  MET   B O     1 
ATOM   12413 C  CB    . MET   B  1  454  ? -13.051 24.700  114.541 1.00 24.31 ? 452  MET   B CB    1 
ATOM   12414 C  CG    . MET   B  1  454  ? -13.907 24.931  113.297 1.00 29.28 ? 452  MET   B CG    1 
ATOM   12415 S  SD    . MET   B  1  454  ? -14.777 26.511  113.351 1.00 38.13 ? 452  MET   B SD    1 
ATOM   12416 C  CE    . MET   B  1  454  ? -13.382 27.636  113.363 1.00 39.37 ? 452  MET   B CE    1 
ATOM   12417 N  N     . GLY   B  1  455  ? -14.823 22.653  116.007 1.00 24.06 ? 453  GLY   B N     1 
ATOM   12418 C  CA    . GLY   B  1  455  ? -15.878 21.684  115.790 1.00 25.97 ? 453  GLY   B CA    1 
ATOM   12419 C  C     . GLY   B  1  455  ? -16.704 21.316  116.996 1.00 29.19 ? 453  GLY   B C     1 
ATOM   12420 O  O     . GLY   B  1  455  ? -17.718 20.632  116.843 1.00 28.24 ? 453  GLY   B O     1 
ATOM   12421 N  N     . GLU   B  1  456  ? -16.293 21.717  118.201 1.00 29.56 ? 454  GLU   B N     1 
ATOM   12422 C  CA    . GLU   B  1  456  ? -17.043 21.326  119.395 1.00 30.86 ? 454  GLU   B CA    1 
ATOM   12423 C  C     . GLU   B  1  456  ? -18.495 21.775  119.382 1.00 31.64 ? 454  GLU   B C     1 
ATOM   12424 O  O     . GLU   B  1  456  ? -19.364 20.961  119.734 1.00 32.12 ? 454  GLU   B O     1 
ATOM   12425 C  CB    . GLU   B  1  456  ? -16.327 21.765  120.675 1.00 35.59 ? 454  GLU   B CB    1 
ATOM   12426 C  CG    . GLU   B  1  456  ? -15.034 21.039  120.935 1.00 40.55 ? 454  GLU   B CG    1 
ATOM   12427 C  CD    . GLU   B  1  456  ? -13.855 21.784  120.375 1.00 40.02 ? 454  GLU   B CD    1 
ATOM   12428 O  OE1   . GLU   B  1  456  ? -14.049 22.577  119.425 1.00 37.97 ? 454  GLU   B OE1   1 
ATOM   12429 O  OE2   . GLU   B  1  456  ? -12.742 21.586  120.896 1.00 31.85 ? 454  GLU   B OE2   1 
ATOM   12430 N  N     . PRO   B  1  457  ? -18.832 23.021  119.022 1.00 31.22 ? 455  PRO   B N     1 
ATOM   12431 C  CA    . PRO   B  1  457  ? -20.254 23.404  119.018 1.00 32.38 ? 455  PRO   B CA    1 
ATOM   12432 C  C     . PRO   B  1  457  ? -21.128 22.478  118.193 1.00 34.01 ? 455  PRO   B C     1 
ATOM   12433 O  O     . PRO   B  1  457  ? -22.251 22.160  118.602 1.00 31.74 ? 455  PRO   B O     1 
ATOM   12434 C  CB    . PRO   B  1  457  ? -20.225 24.826  118.451 1.00 31.99 ? 455  PRO   B CB    1 
ATOM   12435 C  CG    . PRO   B  1  457  ? -18.897 25.347  118.855 1.00 34.82 ? 455  PRO   B CG    1 
ATOM   12436 C  CD    . PRO   B  1  457  ? -17.965 24.177  118.728 1.00 34.12 ? 455  PRO   B CD    1 
ATOM   12437 N  N     . LEU   B  1  458  ? -20.641 22.029  117.040 1.00 31.31 ? 456  LEU   B N     1 
ATOM   12438 C  CA    . LEU   B  1  458  ? -21.417 21.087  116.247 1.00 26.87 ? 456  LEU   B CA    1 
ATOM   12439 C  C     . LEU   B  1  458  ? -21.480 19.733  116.928 1.00 28.57 ? 456  LEU   B C     1 
ATOM   12440 O  O     . LEU   B  1  458  ? -22.559 19.154  117.092 1.00 28.21 ? 456  LEU   B O     1 
ATOM   12441 C  CB    . LEU   B  1  458  ? -20.816 20.960  114.849 1.00 27.09 ? 456  LEU   B CB    1 
ATOM   12442 C  CG    . LEU   B  1  458  ? -21.505 19.951  113.933 1.00 26.59 ? 456  LEU   B CG    1 
ATOM   12443 C  CD1   . LEU   B  1  458  ? -22.980 20.309  113.771 1.00 31.48 ? 456  LEU   B CD1   1 
ATOM   12444 C  CD2   . LEU   B  1  458  ? -20.814 19.897  112.577 1.00 29.05 ? 456  LEU   B CD2   1 
ATOM   12445 N  N     . TYR   B  1  459  ? -20.337 19.225  117.367 1.00 24.28 ? 457  TYR   B N     1 
ATOM   12446 C  CA    . TYR   B  1  459  ? -20.299 17.853  117.830 1.00 23.77 ? 457  TYR   B CA    1 
ATOM   12447 C  C     . TYR   B  1  459  ? -20.813 17.684  119.248 1.00 24.44 ? 457  TYR   B C     1 
ATOM   12448 O  O     . TYR   B  1  459  ? -21.115 16.558  119.638 1.00 25.91 ? 457  TYR   B O     1 
ATOM   12449 C  CB    . TYR   B  1  459  ? -18.910 17.263  117.594 1.00 24.16 ? 457  TYR   B CB    1 
ATOM   12450 C  CG    . TYR   B  1  459  ? -18.764 16.910  116.141 1.00 23.85 ? 457  TYR   B CG    1 
ATOM   12451 C  CD1   . TYR   B  1  459  ? -19.316 15.733  115.655 1.00 22.85 ? 457  TYR   B CD1   1 
ATOM   12452 C  CD2   . TYR   B  1  459  ? -18.141 17.773  115.242 1.00 23.08 ? 457  TYR   B CD2   1 
ATOM   12453 C  CE1   . TYR   B  1  459  ? -19.223 15.399  114.316 1.00 22.81 ? 457  TYR   B CE1   1 
ATOM   12454 C  CE2   . TYR   B  1  459  ? -18.044 17.439  113.882 1.00 23.44 ? 457  TYR   B CE2   1 
ATOM   12455 C  CZ    . TYR   B  1  459  ? -18.583 16.246  113.439 1.00 20.32 ? 457  TYR   B CZ    1 
ATOM   12456 O  OH    . TYR   B  1  459  ? -18.500 15.892  112.104 1.00 22.82 ? 457  TYR   B OH    1 
ATOM   12457 N  N     . GLU   B  1  460  ? -20.931 18.771  120.008 1.00 27.30 ? 458  GLU   B N     1 
ATOM   12458 C  CA    . GLU   B  1  460  ? -21.697 18.720  121.246 1.00 28.15 ? 458  GLU   B CA    1 
ATOM   12459 C  C     . GLU   B  1  460  ? -23.153 18.359  120.983 1.00 33.40 ? 458  GLU   B C     1 
ATOM   12460 O  O     . GLU   B  1  460  ? -23.832 17.866  121.892 1.00 31.67 ? 458  GLU   B O     1 
ATOM   12461 C  CB    . GLU   B  1  460  ? -21.578 20.052  121.994 1.00 32.80 ? 458  GLU   B CB    1 
ATOM   12462 N  N     . GLU   B  1  461  ? -23.640 18.584  119.758 1.00 31.21 ? 459  GLU   B N     1 
ATOM   12463 C  CA    . GLU   B  1  461  ? -24.983 18.187  119.351 1.00 32.83 ? 459  GLU   B CA    1 
ATOM   12464 C  C     . GLU   B  1  461  ? -25.020 16.798  118.734 1.00 34.51 ? 459  GLU   B C     1 
ATOM   12465 O  O     . GLU   B  1  461  ? -26.059 16.392  118.198 1.00 30.08 ? 459  GLU   B O     1 
ATOM   12466 C  CB    . GLU   B  1  461  ? -25.554 19.196  118.357 1.00 30.02 ? 459  GLU   B CB    1 
ATOM   12467 C  CG    . GLU   B  1  461  ? -25.415 20.641  118.779 1.00 32.18 ? 459  GLU   B CG    1 
ATOM   12468 C  CD    . GLU   B  1  461  ? -26.206 20.945  120.035 1.00 41.65 ? 459  GLU   B CD    1 
ATOM   12469 O  OE1   . GLU   B  1  461  ? -27.146 20.178  120.340 1.00 39.73 ? 459  GLU   B OE1   1 
ATOM   12470 O  OE2   . GLU   B  1  461  ? -25.885 21.945  120.712 1.00 44.04 ? 459  GLU   B OE2   1 
ATOM   12471 N  N     . VAL   B  1  462  ? -23.907 16.071  118.780 1.00 31.25 ? 460  VAL   B N     1 
ATOM   12472 C  CA    . VAL   B  1  462  ? -23.767 14.778  118.126 1.00 28.49 ? 460  VAL   B CA    1 
ATOM   12473 C  C     . VAL   B  1  462  ? -23.375 13.696  119.119 1.00 28.00 ? 460  VAL   B C     1 
ATOM   12474 O  O     . VAL   B  1  462  ? -24.023 12.648  119.204 1.00 30.73 ? 460  VAL   B O     1 
ATOM   12475 C  CB    . VAL   B  1  462  ? -22.754 14.849  116.956 1.00 26.08 ? 460  VAL   B CB    1 
ATOM   12476 C  CG1   . VAL   B  1  462  ? -22.523 13.471  116.345 1.00 27.35 ? 460  VAL   B CG1   1 
ATOM   12477 C  CG2   . VAL   B  1  462  ? -23.235 15.840  115.906 1.00 29.32 ? 460  VAL   B CG2   1 
ATOM   12478 N  N     . VAL   B  1  463  ? -22.305 13.934  119.883 1.00 26.49 ? 461  VAL   B N     1 
ATOM   12479 C  CA    . VAL   B  1  463  ? -21.821 12.957  120.847 1.00 26.45 ? 461  VAL   B CA    1 
ATOM   12480 C  C     . VAL   B  1  463  ? -22.776 12.881  122.030 1.00 28.41 ? 461  VAL   B C     1 
ATOM   12481 O  O     . VAL   B  1  463  ? -23.303 13.900  122.500 1.00 31.40 ? 461  VAL   B O     1 
ATOM   12482 C  CB    . VAL   B  1  463  ? -20.393 13.327  121.292 1.00 26.06 ? 461  VAL   B CB    1 
ATOM   12483 C  CG1   . VAL   B  1  463  ? -19.894 12.365  122.345 1.00 32.15 ? 461  VAL   B CG1   1 
ATOM   12484 C  CG2   . VAL   B  1  463  ? -19.440 13.347  120.082 1.00 26.02 ? 461  VAL   B CG2   1 
ATOM   12485 N  N     . GLY   B  1  464  ? -22.993 11.677  122.521 1.00 31.52 ? 462  GLY   B N     1 
ATOM   12486 C  CA    . GLY   B  1  464  ? -23.776 11.507  123.733 1.00 32.21 ? 462  GLY   B CA    1 
ATOM   12487 C  C     . GLY   B  1  464  ? -25.097 10.816  123.455 1.00 36.20 ? 462  GLY   B C     1 
ATOM   12488 O  O     . GLY   B  1  464  ? -25.717 11.014  122.403 1.00 33.50 ? 462  GLY   B O     1 
ATOM   12489 N  N     . ARG   B  1  465  ? -25.539 10.001  124.418 1.00 35.69 ? 463  ARG   B N     1 
ATOM   12490 C  CA    . ARG   B  1  465  ? -26.796 9.275   124.270 1.00 40.38 ? 463  ARG   B CA    1 
ATOM   12491 C  C     . ARG   B  1  465  ? -27.975 10.222  124.091 1.00 40.84 ? 463  ARG   B C     1 
ATOM   12492 O  O     . ARG   B  1  465  ? -28.963 9.865   123.440 1.00 47.42 ? 463  ARG   B O     1 
ATOM   12493 C  CB    . ARG   B  1  465  ? -27.015 8.364   125.479 1.00 45.72 ? 463  ARG   B CB    1 
ATOM   12494 N  N     . GLY   B  1  466  ? -27.887 11.430  124.646 1.00 38.30 ? 464  GLY   B N     1 
ATOM   12495 C  CA    . GLY   B  1  466  ? -28.914 12.439  124.502 1.00 44.29 ? 464  GLY   B CA    1 
ATOM   12496 C  C     . GLY   B  1  466  ? -28.838 13.256  123.236 1.00 45.46 ? 464  GLY   B C     1 
ATOM   12497 O  O     . GLY   B  1  466  ? -29.626 14.188  123.050 1.00 42.98 ? 464  GLY   B O     1 
ATOM   12498 N  N     . LYS   B  1  467  ? -27.895 12.937  122.353 1.00 38.17 ? 465  LYS   B N     1 
ATOM   12499 C  CA    . LYS   B  1  467  ? -27.790 13.601  121.065 1.00 36.73 ? 465  LYS   B CA    1 
ATOM   12500 C  C     . LYS   B  1  467  ? -27.924 12.566  119.957 1.00 38.86 ? 465  LYS   B C     1 
ATOM   12501 O  O     . LYS   B  1  467  ? -28.909 11.827  119.912 1.00 38.76 ? 465  LYS   B O     1 
ATOM   12502 C  CB    . LYS   B  1  467  ? -26.468 14.364  120.962 1.00 32.00 ? 465  LYS   B CB    1 
ATOM   12503 C  CG    . LYS   B  1  467  ? -26.300 15.431  122.044 1.00 38.91 ? 465  LYS   B CG    1 
ATOM   12504 C  CD    . LYS   B  1  467  ? -27.316 16.554  121.862 1.00 40.64 ? 465  LYS   B CD    1 
ATOM   12505 C  CE    . LYS   B  1  467  ? -27.219 17.626  122.949 1.00 39.28 ? 465  LYS   B CE    1 
ATOM   12506 N  NZ    . LYS   B  1  467  ? -27.977 18.859  122.562 1.00 43.31 ? 465  LYS   B NZ    1 
ATOM   12507 N  N     . LEU   B  1  468  ? -26.954 12.500  119.050 1.00 33.42 ? 466  LEU   B N     1 
ATOM   12508 C  CA    . LEU   B  1  468  ? -27.014 11.475  118.020 1.00 32.58 ? 466  LEU   B CA    1 
ATOM   12509 C  C     . LEU   B  1  468  ? -26.312 10.192  118.427 1.00 31.32 ? 466  LEU   B C     1 
ATOM   12510 O  O     . LEU   B  1  468  ? -26.381 9.205   117.686 1.00 31.16 ? 466  LEU   B O     1 
ATOM   12511 C  CB    . LEU   B  1  468  ? -26.446 11.990  116.696 1.00 32.87 ? 466  LEU   B CB    1 
ATOM   12512 C  CG    . LEU   B  1  468  ? -27.082 13.277  116.174 1.00 34.19 ? 466  LEU   B CG    1 
ATOM   12513 C  CD1   . LEU   B  1  468  ? -26.490 13.672  114.835 1.00 35.60 ? 466  LEU   B CD1   1 
ATOM   12514 C  CD2   . LEU   B  1  468  ? -28.600 13.113  116.084 1.00 35.41 ? 466  LEU   B CD2   1 
ATOM   12515 N  N     . ASP   B  1  469  ? -25.646 10.185  119.583 1.00 28.59 ? 467  ASP   B N     1 
ATOM   12516 C  CA    . ASP   B  1  469  ? -24.961 8.995   120.084 1.00 34.18 ? 467  ASP   B CA    1 
ATOM   12517 C  C     . ASP   B  1  469  ? -23.932 8.492   119.077 1.00 27.98 ? 467  ASP   B C     1 
ATOM   12518 O  O     . ASP   B  1  469  ? -23.817 7.294   118.817 1.00 29.28 ? 467  ASP   B O     1 
ATOM   12519 C  CB    . ASP   B  1  469  ? -25.945 7.897   120.494 1.00 34.11 ? 467  ASP   B CB    1 
ATOM   12520 C  CG    . ASP   B  1  469  ? -25.347 6.913   121.472 1.00 42.26 ? 467  ASP   B CG    1 
ATOM   12521 O  OD1   . ASP   B  1  469  ? -24.262 7.200   122.029 1.00 41.31 ? 467  ASP   B OD1   1 
ATOM   12522 O  OD2   . ASP   B  1  469  ? -25.961 5.846   121.680 1.00 43.24 ? 467  ASP   B OD2   1 
ATOM   12523 N  N     . ARG   B  1  470  ? -23.185 9.429   118.502 1.00 31.59 ? 468  ARG   B N     1 
ATOM   12524 C  CA    . ARG   B  1  470  ? -22.107 9.113   117.595 1.00 29.62 ? 468  ARG   B CA    1 
ATOM   12525 C  C     . ARG   B  1  470  ? -20.815 9.732   118.103 1.00 27.80 ? 468  ARG   B C     1 
ATOM   12526 O  O     . ARG   B  1  470  ? -20.808 10.890  118.533 1.00 26.79 ? 468  ARG   B O     1 
ATOM   12527 C  CB    . ARG   B  1  470  ? -22.392 9.665   116.197 1.00 27.07 ? 468  ARG   B CB    1 
ATOM   12528 C  CG    . ARG   B  1  470  ? -23.603 9.030   115.520 1.00 28.11 ? 468  ARG   B CG    1 
ATOM   12529 C  CD    . ARG   B  1  470  ? -23.431 7.524   115.370 1.00 25.12 ? 468  ARG   B CD    1 
ATOM   12530 N  NE    . ARG   B  1  470  ? -24.590 6.886   114.748 1.00 29.64 ? 468  ARG   B NE    1 
ATOM   12531 C  CZ    . ARG   B  1  470  ? -25.570 6.297   115.418 1.00 34.83 ? 468  ARG   B CZ    1 
ATOM   12532 N  NH1   . ARG   B  1  470  ? -25.588 6.276   116.741 1.00 33.85 ? 468  ARG   B NH1   1 
ATOM   12533 N  NH2   . ARG   B  1  470  ? -26.558 5.711   114.743 1.00 34.79 ? 468  ARG   B NH2   1 
ATOM   12534 N  N     . PRO   B  1  471  ? -19.715 8.996   118.059 1.00 25.45 ? 469  PRO   B N     1 
ATOM   12535 C  CA    . PRO   B  1  471  ? -18.461 9.507   118.607 1.00 24.97 ? 469  PRO   B CA    1 
ATOM   12536 C  C     . PRO   B  1  471  ? -17.814 10.488  117.647 1.00 22.56 ? 469  PRO   B C     1 
ATOM   12537 O  O     . PRO   B  1  471  ? -18.063 10.496  116.438 1.00 21.95 ? 469  PRO   B O     1 
ATOM   12538 C  CB    . PRO   B  1  471  ? -17.607 8.244   118.733 1.00 24.86 ? 469  PRO   B CB    1 
ATOM   12539 C  CG    . PRO   B  1  471  ? -18.077 7.395   117.621 1.00 27.57 ? 469  PRO   B CG    1 
ATOM   12540 C  CD    . PRO   B  1  471  ? -19.560 7.640   117.519 1.00 27.32 ? 469  PRO   B CD    1 
ATOM   12541 N  N     . CYS   B  1  472  ? -16.955 11.323  118.218 1.00 22.05 ? 470  CYS   B N     1 
ATOM   12542 C  CA    . CYS   B  1  472  ? -16.204 12.282  117.433 1.00 21.63 ? 470  CYS   B CA    1 
ATOM   12543 C  C     . CYS   B  1  472  ? -14.797 12.356  117.996 1.00 20.75 ? 470  CYS   B C     1 
ATOM   12544 O  O     . CYS   B  1  472  ? -14.611 12.483  119.214 1.00 22.40 ? 470  CYS   B O     1 
ATOM   12545 C  CB    . CYS   B  1  472  ? -16.857 13.663  117.467 1.00 24.61 ? 470  CYS   B CB    1 
ATOM   12546 S  SG    . CYS   B  1  472  ? -15.958 14.863  116.488 1.00 25.17 ? 470  CYS   B SG    1 
ATOM   12547 N  N     . ARG   B  1  473  ? -13.816 12.250  117.109 1.00 20.52 ? 471  ARG   B N     1 
ATOM   12548 C  CA    . ARG   B  1  473  ? -12.417 12.395  117.473 1.00 19.89 ? 471  ARG   B CA    1 
ATOM   12549 C  C     . ARG   B  1  473  ? -11.969 13.810  117.150 1.00 19.59 ? 471  ARG   B C     1 
ATOM   12550 O  O     . ARG   B  1  473  ? -12.124 14.284  116.019 1.00 22.52 ? 471  ARG   B O     1 
ATOM   12551 C  CB    . ARG   B  1  473  ? -11.546 11.391  116.725 1.00 18.97 ? 471  ARG   B CB    1 
ATOM   12552 C  CG    . ARG   B  1  473  ? -10.085 11.434  117.189 1.00 20.11 ? 471  ARG   B CG    1 
ATOM   12553 C  CD    . ARG   B  1  473  ? -9.284  10.311  116.561 1.00 17.96 ? 471  ARG   B CD    1 
ATOM   12554 N  NE    . ARG   B  1  473  ? -9.967  9.031   116.688 1.00 19.93 ? 471  ARG   B NE    1 
ATOM   12555 C  CZ    . ARG   B  1  473  ? -9.896  8.244   117.752 1.00 22.16 ? 471  ARG   B CZ    1 
ATOM   12556 N  NH1   . ARG   B  1  473  ? -9.059  8.501   118.747 1.00 21.54 ? 471  ARG   B NH1   1 
ATOM   12557 N  NH2   . ARG   B  1  473  ? -10.675 7.167   117.818 1.00 23.82 ? 471  ARG   B NH2   1 
ATOM   12558 N  N     . ILE   B  1  474  ? -11.404 14.472  118.150 1.00 20.06 ? 472  ILE   B N     1 
ATOM   12559 C  CA    . ILE   B  1  474  ? -10.976 15.854  118.028 1.00 19.35 ? 472  ILE   B CA    1 
ATOM   12560 C  C     . ILE   B  1  474  ? -9.519  15.867  117.596 1.00 20.09 ? 472  ILE   B C     1 
ATOM   12561 O  O     . ILE   B  1  474  ? -8.657  15.308  118.283 1.00 20.23 ? 472  ILE   B O     1 
ATOM   12562 C  CB    . ILE   B  1  474  ? -11.153 16.576  119.367 1.00 19.79 ? 472  ILE   B CB    1 
ATOM   12563 C  CG1   . ILE   B  1  474  ? -12.643 16.617  119.726 1.00 20.22 ? 472  ILE   B CG1   1 
ATOM   12564 C  CG2   . ILE   B  1  474  ? -10.557 17.954  119.280 1.00 20.31 ? 472  ILE   B CG2   1 
ATOM   12565 C  CD1   . ILE   B  1  474  ? -12.899 17.141  121.121 1.00 23.71 ? 472  ILE   B CD1   1 
ATOM   12566 N  N     . TYR   B  1  475  ? -9.250  16.506  116.468 1.00 18.11 ? 473  TYR   B N     1 
ATOM   12567 C  CA    . TYR   B  1  475  ? -7.889  16.746  116.012 1.00 18.67 ? 473  TYR   B CA    1 
ATOM   12568 C  C     . TYR   B  1  475  ? -7.357  17.906  116.828 1.00 19.21 ? 473  TYR   B C     1 
ATOM   12569 O  O     . TYR   B  1  475  ? -7.901  19.015  116.781 1.00 19.98 ? 473  TYR   B O     1 
ATOM   12570 C  CB    . TYR   B  1  475  ? -7.922  17.085  114.526 1.00 19.55 ? 473  TYR   B CB    1 
ATOM   12571 C  CG    . TYR   B  1  475  ? -6.579  17.143  113.844 1.00 19.11 ? 473  TYR   B CG    1 
ATOM   12572 C  CD1   . TYR   B  1  475  ? -5.833  18.316  113.836 1.00 20.44 ? 473  TYR   B CD1   1 
ATOM   12573 C  CD2   . TYR   B  1  475  ? -6.064  16.035  113.187 1.00 19.21 ? 473  TYR   B CD2   1 
ATOM   12574 C  CE1   . TYR   B  1  475  ? -4.605  18.384  113.198 1.00 19.66 ? 473  TYR   B CE1   1 
ATOM   12575 C  CE2   . TYR   B  1  475  ? -4.845  16.096  112.536 1.00 17.66 ? 473  TYR   B CE2   1 
ATOM   12576 C  CZ    . TYR   B  1  475  ? -4.122  17.270  112.558 1.00 21.12 ? 473  TYR   B CZ    1 
ATOM   12577 O  OH    . TYR   B  1  475  ? -2.901  17.347  111.938 1.00 21.83 ? 473  TYR   B OH    1 
ATOM   12578 N  N     . ALA   B  1  476  ? -6.322  17.633  117.612 1.00 18.37 ? 474  ALA   B N     1 
ATOM   12579 C  CA    . ALA   B  1  476  ? -5.886  18.532  118.675 1.00 21.18 ? 474  ALA   B CA    1 
ATOM   12580 C  C     . ALA   B  1  476  ? -4.466  19.006  118.416 1.00 20.03 ? 474  ALA   B C     1 
ATOM   12581 O  O     . ALA   B  1  476  ? -3.497  18.274  118.697 1.00 19.28 ? 474  ALA   B O     1 
ATOM   12582 C  CB    . ALA   B  1  476  ? -5.990  17.807  120.013 1.00 22.64 ? 474  ALA   B CB    1 
ATOM   12583 N  N     . PRO   B  1  477  ? -4.296  20.213  117.885 1.00 20.78 ? 475  PRO   B N     1 
ATOM   12584 C  CA    . PRO   B  1  477  ? -2.953  20.777  117.751 1.00 21.17 ? 475  PRO   B CA    1 
ATOM   12585 C  C     . PRO   B  1  477  ? -2.337  21.005  119.115 1.00 20.72 ? 475  PRO   B C     1 
ATOM   12586 O  O     . PRO   B  1  477  ? -3.013  21.395  120.066 1.00 21.13 ? 475  PRO   B O     1 
ATOM   12587 C  CB    . PRO   B  1  477  ? -3.195  22.113  117.043 1.00 22.79 ? 475  PRO   B CB    1 
ATOM   12588 C  CG    . PRO   B  1  477  ? -4.557  21.996  116.422 1.00 23.28 ? 475  PRO   B CG    1 
ATOM   12589 C  CD    . PRO   B  1  477  ? -5.335  21.115  117.358 1.00 21.02 ? 475  PRO   B CD    1 
ATOM   12590 N  N     . VAL   B  1  478  ? -1.039  20.758  119.202 1.00 19.57 ? 476  VAL   B N     1 
ATOM   12591 C  CA    . VAL   B  1  478  ? -0.283  20.901  120.431 1.00 19.91 ? 476  VAL   B CA    1 
ATOM   12592 C  C     . VAL   B  1  478  ? 0.991   21.641  120.072 1.00 23.14 ? 476  VAL   B C     1 
ATOM   12593 O  O     . VAL   B  1  478  ? 1.755   21.178  119.222 1.00 24.75 ? 476  VAL   B O     1 
ATOM   12594 C  CB    . VAL   B  1  478  ? 0.053   19.531  121.041 1.00 21.10 ? 476  VAL   B CB    1 
ATOM   12595 C  CG1   . VAL   B  1  478  ? 0.852   19.701  122.309 1.00 23.90 ? 476  VAL   B CG1   1 
ATOM   12596 C  CG2   . VAL   B  1  478  ? -1.219  18.731  121.307 1.00 21.44 ? 476  VAL   B CG2   1 
ATOM   12597 N  N     . GLY   B  1  479  ? 1.216   22.782  120.698 1.00 27.24 ? 477  GLY   B N     1 
ATOM   12598 C  CA    . GLY   B  1  479  ? 2.457   23.487  120.455 1.00 31.13 ? 477  GLY   B CA    1 
ATOM   12599 C  C     . GLY   B  1  479  ? 2.396   24.923  120.920 1.00 29.19 ? 477  GLY   B C     1 
ATOM   12600 O  O     . GLY   B  1  479  ? 1.372   25.415  121.398 1.00 27.17 ? 477  GLY   B O     1 
ATOM   12601 N  N     . THR   B  1  480  ? 3.530   25.592  120.735 1.00 35.66 ? 478  THR   B N     1 
ATOM   12602 C  CA    . THR   B  1  480  ? 3.750   26.946  121.204 1.00 39.92 ? 478  THR   B CA    1 
ATOM   12603 C  C     . THR   B  1  480  ? 3.116   27.952  120.246 1.00 42.22 ? 478  THR   B C     1 
ATOM   12604 O  O     . THR   B  1  480  ? 2.607   27.605  119.175 1.00 44.17 ? 478  THR   B O     1 
ATOM   12605 C  CB    . THR   B  1  480  ? 5.249   27.215  121.304 1.00 36.35 ? 478  THR   B CB    1 
ATOM   12606 O  OG1   . THR   B  1  480  ? 5.826   27.121  119.996 1.00 52.70 ? 478  THR   B OG1   1 
ATOM   12607 C  CG2   . THR   B  1  480  ? 5.906   26.193  122.199 1.00 39.57 ? 478  THR   B CG2   1 
ATOM   12608 N  N     . HIS   B  1  481  ? 3.170   29.225  120.645 1.00 50.01 ? 479  HIS   B N     1 
ATOM   12609 C  CA    . HIS   B  1  481  ? 2.601   30.293  119.829 1.00 49.24 ? 479  HIS   B CA    1 
ATOM   12610 C  C     . HIS   B  1  481  ? 3.280   30.374  118.469 1.00 53.22 ? 479  HIS   B C     1 
ATOM   12611 O  O     . HIS   B  1  481  ? 2.610   30.449  117.432 1.00 50.42 ? 479  HIS   B O     1 
ATOM   12612 C  CB    . HIS   B  1  481  ? 2.725   31.626  120.563 1.00 44.26 ? 479  HIS   B CB    1 
ATOM   12613 C  CG    . HIS   B  1  481  ? 1.883   31.711  121.796 1.00 46.03 ? 479  HIS   B CG    1 
ATOM   12614 N  ND1   . HIS   B  1  481  ? 1.720   32.880  122.508 1.00 50.55 ? 479  HIS   B ND1   1 
ATOM   12615 C  CD2   . HIS   B  1  481  ? 1.153   30.771  122.441 1.00 42.06 ? 479  HIS   B CD2   1 
ATOM   12616 C  CE1   . HIS   B  1  481  ? 0.925   32.657  123.539 1.00 51.57 ? 479  HIS   B CE1   1 
ATOM   12617 N  NE2   . HIS   B  1  481  ? 0.567   31.385  123.521 1.00 52.60 ? 479  HIS   B NE2   1 
ATOM   12618 N  N     . GLU   B  1  482  ? 4.616   30.364  118.455 1.00 51.95 ? 480  GLU   B N     1 
ATOM   12619 C  CA    . GLU   B  1  482  ? 5.346   30.514  117.200 1.00 49.94 ? 480  GLU   B CA    1 
ATOM   12620 C  C     . GLU   B  1  482  ? 5.011   29.391  116.228 1.00 45.07 ? 480  GLU   B C     1 
ATOM   12621 O  O     . GLU   B  1  482  ? 4.920   29.614  115.015 1.00 53.45 ? 480  GLU   B O     1 
ATOM   12622 C  CB    . GLU   B  1  482  ? 6.850   30.565  117.476 1.00 54.14 ? 480  GLU   B CB    1 
ATOM   12623 N  N     . THR   B  1  483  ? 4.794   28.183  116.746 1.00 50.20 ? 481  THR   B N     1 
ATOM   12624 C  CA    . THR   B  1  483  ? 4.527   27.042  115.880 1.00 51.69 ? 481  THR   B CA    1 
ATOM   12625 C  C     . THR   B  1  483  ? 3.096   27.048  115.350 1.00 51.86 ? 481  THR   B C     1 
ATOM   12626 O  O     . THR   B  1  483  ? 2.870   26.740  114.173 1.00 54.95 ? 481  THR   B O     1 
ATOM   12627 C  CB    . THR   B  1  483  ? 4.832   25.741  116.626 1.00 56.16 ? 481  THR   B CB    1 
ATOM   12628 O  OG1   . THR   B  1  483  ? 6.107   25.851  117.270 1.00 59.33 ? 481  THR   B OG1   1 
ATOM   12629 C  CG2   . THR   B  1  483  ? 4.875   24.578  115.655 1.00 55.55 ? 481  THR   B CG2   1 
ATOM   12630 N  N     . LEU   B  1  484  ? 2.117   27.390  116.193 1.00 49.01 ? 482  LEU   B N     1 
ATOM   12631 C  CA    . LEU   B  1  484  ? 0.730   27.376  115.732 1.00 47.29 ? 482  LEU   B CA    1 
ATOM   12632 C  C     . LEU   B  1  484  ? 0.475   28.477  114.708 1.00 45.22 ? 482  LEU   B C     1 
ATOM   12633 O  O     . LEU   B  1  484  ? -0.316  28.296  113.773 1.00 43.35 ? 482  LEU   B O     1 
ATOM   12634 C  CB    . LEU   B  1  484  ? -0.237  27.475  116.917 1.00 44.75 ? 482  LEU   B CB    1 
ATOM   12635 C  CG    . LEU   B  1  484  ? -0.413  28.809  117.652 1.00 44.44 ? 482  LEU   B CG    1 
ATOM   12636 C  CD1   . LEU   B  1  484  ? -1.491  29.676  117.008 1.00 42.83 ? 482  LEU   B CD1   1 
ATOM   12637 C  CD2   . LEU   B  1  484  ? -0.729  28.577  119.117 1.00 42.44 ? 482  LEU   B CD2   1 
ATOM   12638 N  N     . LEU   B  1  485  ? 1.135   29.626  114.867 1.00 42.74 ? 483  LEU   B N     1 
ATOM   12639 C  CA    . LEU   B  1  485  ? 0.931   30.721  113.926 1.00 49.59 ? 483  LEU   B CA    1 
ATOM   12640 C  C     . LEU   B  1  485  ? 1.389   30.350  112.521 1.00 44.86 ? 483  LEU   B C     1 
ATOM   12641 O  O     . LEU   B  1  485  ? 0.908   30.928  111.540 1.00 44.24 ? 483  LEU   B O     1 
ATOM   12642 C  CB    . LEU   B  1  485  ? 1.660   31.975  114.420 1.00 44.65 ? 483  LEU   B CB    1 
ATOM   12643 C  CG    . LEU   B  1  485  ? 1.011   32.726  115.584 1.00 40.22 ? 483  LEU   B CG    1 
ATOM   12644 C  CD1   . LEU   B  1  485  ? 1.926   33.826  116.074 1.00 41.34 ? 483  LEU   B CD1   1 
ATOM   12645 C  CD2   . LEU   B  1  485  ? -0.343  33.302  115.182 1.00 43.17 ? 483  LEU   B CD2   1 
ATOM   12646 N  N     . ALA   B  1  486  ? 2.285   29.365  112.407 1.00 44.21 ? 484  ALA   B N     1 
ATOM   12647 C  CA    . ALA   B  1  486  ? 2.970   29.113  111.141 1.00 39.28 ? 484  ALA   B CA    1 
ATOM   12648 C  C     . ALA   B  1  486  ? 2.020   28.633  110.047 1.00 49.08 ? 484  ALA   B C     1 
ATOM   12649 O  O     . ALA   B  1  486  ? 2.307   28.812  108.857 1.00 50.81 ? 484  ALA   B O     1 
ATOM   12650 C  CB    . ALA   B  1  486  ? 4.118   28.125  111.350 1.00 45.43 ? 484  ALA   B CB    1 
ATOM   12651 N  N     . TYR   B  1  487  ? 0.890   28.021  110.417 1.00 47.86 ? 485  TYR   B N     1 
ATOM   12652 C  CA    . TYR   B  1  487  ? -0.066  27.573  109.409 1.00 45.85 ? 485  TYR   B CA    1 
ATOM   12653 C  C     . TYR   B  1  487  ? -1.515  27.805  109.832 1.00 45.26 ? 485  TYR   B C     1 
ATOM   12654 O  O     . TYR   B  1  487  ? -2.422  27.142  109.305 1.00 33.83 ? 485  TYR   B O     1 
ATOM   12655 C  CB    . TYR   B  1  487  ? 0.155   26.104  109.018 1.00 45.68 ? 485  TYR   B CB    1 
ATOM   12656 C  CG    . TYR   B  1  487  ? 1.437   25.845  108.249 1.00 51.00 ? 485  TYR   B CG    1 
ATOM   12657 C  CD1   . TYR   B  1  487  ? 1.517   26.097  106.881 1.00 54.86 ? 485  TYR   B CD1   1 
ATOM   12658 C  CD2   . TYR   B  1  487  ? 2.563   25.336  108.887 1.00 50.25 ? 485  TYR   B CD2   1 
ATOM   12659 C  CE1   . TYR   B  1  487  ? 2.688   25.857  106.172 1.00 54.28 ? 485  TYR   B CE1   1 
ATOM   12660 C  CE2   . TYR   B  1  487  ? 3.736   25.093  108.188 1.00 50.83 ? 485  TYR   B CE2   1 
ATOM   12661 C  CZ    . TYR   B  1  487  ? 3.794   25.355  106.832 1.00 54.70 ? 485  TYR   B CZ    1 
ATOM   12662 O  OH    . TYR   B  1  487  ? 4.961   25.112  106.140 1.00 60.18 ? 485  TYR   B OH    1 
ATOM   12663 N  N     . LEU   B  1  488  ? -1.756  28.735  110.760 1.00 46.54 ? 486  LEU   B N     1 
ATOM   12664 C  CA    . LEU   B  1  488  ? -3.126  29.059  111.144 1.00 42.05 ? 486  LEU   B CA    1 
ATOM   12665 C  C     . LEU   B  1  488  ? -3.915  29.622  109.971 1.00 42.18 ? 486  LEU   B C     1 
ATOM   12666 O  O     . LEU   B  1  488  ? -5.132  29.421  109.891 1.00 31.32 ? 486  LEU   B O     1 
ATOM   12667 C  CB    . LEU   B  1  488  ? -3.120  30.057  112.301 1.00 42.02 ? 486  LEU   B CB    1 
ATOM   12668 C  CG    . LEU   B  1  488  ? -4.426  30.324  113.051 1.00 40.78 ? 486  LEU   B CG    1 
ATOM   12669 C  CD1   . LEU   B  1  488  ? -4.062  30.753  114.435 1.00 35.99 ? 486  LEU   B CD1   1 
ATOM   12670 C  CD2   . LEU   B  1  488  ? -5.298  31.397  112.407 1.00 39.58 ? 486  LEU   B CD2   1 
ATOM   12671 N  N     . VAL   B  1  489  ? -3.249  30.344  109.066 1.00 40.60 ? 487  VAL   B N     1 
ATOM   12672 C  CA    . VAL   B  1  489  ? -3.934  30.882  107.891 1.00 33.11 ? 487  VAL   B CA    1 
ATOM   12673 C  C     . VAL   B  1  489  ? -4.711  29.780  107.187 1.00 35.84 ? 487  VAL   B C     1 
ATOM   12674 O  O     . VAL   B  1  489  ? -5.930  29.870  106.999 1.00 47.06 ? 487  VAL   B O     1 
ATOM   12675 C  CB    . VAL   B  1  489  ? -2.932  31.562  106.945 1.00 36.89 ? 487  VAL   B CB    1 
ATOM   12676 C  CG1   . VAL   B  1  489  ? -3.603  31.901  105.612 1.00 37.33 ? 487  VAL   B CG1   1 
ATOM   12677 C  CG2   . VAL   B  1  489  ? -2.345  32.805  107.613 1.00 37.63 ? 487  VAL   B CG2   1 
ATOM   12678 N  N     . ARG   B  1  490  ? -4.014  28.700  106.827 1.00 43.35 ? 488  ARG   B N     1 
ATOM   12679 C  CA    . ARG   B  1  490  ? -4.651  27.596  106.118 1.00 45.16 ? 488  ARG   B CA    1 
ATOM   12680 C  C     . ARG   B  1  490  ? -5.715  26.910  106.971 1.00 42.09 ? 488  ARG   B C     1 
ATOM   12681 O  O     . ARG   B  1  490  ? -6.674  26.348  106.431 1.00 43.35 ? 488  ARG   B O     1 
ATOM   12682 C  CB    . ARG   B  1  490  ? -3.572  26.593  105.682 1.00 41.88 ? 488  ARG   B CB    1 
ATOM   12683 C  CG    . ARG   B  1  490  ? -4.066  25.385  104.886 1.00 40.96 ? 488  ARG   B CG    1 
ATOM   12684 C  CD    . ARG   B  1  490  ? -2.976  24.307  104.784 1.00 39.21 ? 488  ARG   B CD    1 
ATOM   12685 N  NE    . ARG   B  1  490  ? -2.691  23.688  106.078 1.00 40.44 ? 488  ARG   B NE    1 
ATOM   12686 C  CZ    . ARG   B  1  490  ? -1.543  23.098  106.390 1.00 34.84 ? 488  ARG   B CZ    1 
ATOM   12687 N  NH1   . ARG   B  1  490  ? -0.530  23.070  105.541 1.00 34.46 ? 488  ARG   B NH1   1 
ATOM   12688 N  NH2   . ARG   B  1  490  ? -1.404  22.536  107.587 1.00 29.73 ? 488  ARG   B NH2   1 
ATOM   12689 N  N     . ARG   B  1  491  ? -5.604  26.997  108.296 1.00 34.78 ? 489  ARG   B N     1 
ATOM   12690 C  CA    . ARG   B  1  491  ? -6.219  25.996  109.160 1.00 44.49 ? 489  ARG   B CA    1 
ATOM   12691 C  C     . ARG   B  1  491  ? -7.639  26.310  109.615 1.00 37.78 ? 489  ARG   B C     1 
ATOM   12692 O  O     . ARG   B  1  491  ? -8.593  26.223  108.833 1.00 37.73 ? 489  ARG   B O     1 
ATOM   12693 C  CB    . ARG   B  1  491  ? -5.339  25.759  110.393 1.00 46.98 ? 489  ARG   B CB    1 
ATOM   12694 N  N     . LEU   B  1  492  ? -7.770  26.655  110.900 1.00 39.26 ? 490  LEU   B N     1 
ATOM   12695 C  CA    . LEU   B  1  492  ? -9.065  26.620  111.576 1.00 37.43 ? 490  LEU   B CA    1 
ATOM   12696 C  C     . LEU   B  1  492  ? -10.114 27.456  110.856 1.00 42.56 ? 490  LEU   B C     1 
ATOM   12697 O  O     . LEU   B  1  492  ? -11.292 27.079  110.808 1.00 38.52 ? 490  LEU   B O     1 
ATOM   12698 C  CB    . LEU   B  1  492  ? -8.906  27.073  113.032 1.00 42.31 ? 490  LEU   B CB    1 
ATOM   12699 N  N     . LEU   B  1  493  ? -9.706  28.580  110.270 1.00 38.57 ? 491  LEU   B N     1 
ATOM   12700 C  CA    . LEU   B  1  493  ? -10.639 29.530  109.681 1.00 41.08 ? 491  LEU   B CA    1 
ATOM   12701 C  C     . LEU   B  1  493  ? -10.871 29.299  108.192 1.00 36.21 ? 491  LEU   B C     1 
ATOM   12702 O  O     . LEU   B  1  493  ? -11.578 30.092  107.558 1.00 44.49 ? 491  LEU   B O     1 
ATOM   12703 C  CB    . LEU   B  1  493  ? -10.175 30.962  109.961 1.00 39.49 ? 491  LEU   B CB    1 
ATOM   12704 C  CG    . LEU   B  1  493  ? -9.975  31.222  111.459 1.00 39.23 ? 491  LEU   B CG    1 
ATOM   12705 C  CD1   . LEU   B  1  493  ? -9.401  32.604  111.706 1.00 40.60 ? 491  LEU   B CD1   1 
ATOM   12706 C  CD2   . LEU   B  1  493  ? -11.280 31.030  112.233 1.00 42.92 ? 491  LEU   B CD2   1 
ATOM   12707 N  N     . GLU   B  1  494  ? -10.312 28.224  107.633 1.00 41.18 ? 492  GLU   B N     1 
ATOM   12708 C  CA    . GLU   B  1  494  ? -10.532 27.853  106.235 1.00 36.17 ? 492  GLU   B CA    1 
ATOM   12709 C  C     . GLU   B  1  494  ? -10.226 29.014  105.298 1.00 38.76 ? 492  GLU   B C     1 
ATOM   12710 O  O     . GLU   B  1  494  ? -10.960 29.277  104.342 1.00 43.32 ? 492  GLU   B O     1 
ATOM   12711 C  CB    . GLU   B  1  494  ? -11.946 27.304  106.009 1.00 37.57 ? 492  GLU   B CB    1 
ATOM   12712 C  CG    . GLU   B  1  494  ? -12.387 26.271  107.035 1.00 30.38 ? 492  GLU   B CG    1 
ATOM   12713 C  CD    . GLU   B  1  494  ? -11.634 24.951  106.931 1.00 36.53 ? 492  GLU   B CD    1 
ATOM   12714 O  OE1   . GLU   B  1  494  ? -10.751 24.821  106.055 1.00 34.11 ? 492  GLU   B OE1   1 
ATOM   12715 O  OE2   . GLU   B  1  494  ? -11.929 24.041  107.739 1.00 34.10 ? 492  GLU   B OE2   1 
ATOM   12716 N  N     . ASN   B  1  495  ? -9.144  29.734  105.602 1.00 36.91 ? 493  ASN   B N     1 
ATOM   12717 C  CA    . ASN   B  1  495  ? -8.685  30.874  104.802 1.00 43.28 ? 493  ASN   B CA    1 
ATOM   12718 C  C     . ASN   B  1  495  ? -9.763  31.937  104.634 1.00 43.17 ? 493  ASN   B C     1 
ATOM   12719 O  O     . ASN   B  1  495  ? -9.741  32.703  103.666 1.00 44.93 ? 493  ASN   B O     1 
ATOM   12720 C  CB    . ASN   B  1  495  ? -8.153  30.448  103.433 1.00 43.79 ? 493  ASN   B CB    1 
ATOM   12721 C  CG    . ASN   B  1  495  ? -7.065  29.416  103.531 1.00 52.76 ? 493  ASN   B CG    1 
ATOM   12722 O  OD1   . ASN   B  1  495  ? -5.895  29.749  103.709 1.00 52.67 ? 493  ASN   B OD1   1 
ATOM   12723 N  ND2   . ASN   B  1  495  ? -7.441  28.146  103.404 1.00 51.77 ? 493  ASN   B ND2   1 
ATOM   12724 N  N     . GLY   B  1  496  ? -10.715 31.983  105.565 1.00 41.63 ? 494  GLY   B N     1 
ATOM   12725 C  CA    . GLY   B  1  496  ? -11.835 32.897  105.462 1.00 46.37 ? 494  GLY   B CA    1 
ATOM   12726 C  C     . GLY   B  1  496  ? -12.578 32.790  104.145 1.00 53.39 ? 494  GLY   B C     1 
ATOM   12727 O  O     . GLY   B  1  496  ? -12.897 33.807  103.522 1.00 52.98 ? 494  GLY   B O     1 
ATOM   12728 N  N     . ALA   B  1  497  ? -12.844 31.562  103.702 1.00 43.04 ? 495  ALA   B N     1 
ATOM   12729 C  CA    . ALA   B  1  497  ? -13.586 31.349  102.468 1.00 43.93 ? 495  ALA   B CA    1 
ATOM   12730 C  C     . ALA   B  1  497  ? -15.075 31.538  102.717 1.00 35.26 ? 495  ALA   B C     1 
ATOM   12731 O  O     . ALA   B  1  497  ? -15.640 30.948  103.644 1.00 37.08 ? 495  ALA   B O     1 
ATOM   12732 C  CB    . ALA   B  1  497  ? -13.329 29.947  101.923 1.00 35.22 ? 495  ALA   B CB    1 
ATOM   12733 N  N     . ASN   B  1  498  ? -15.712 32.348  101.868 1.00 39.39 ? 496  ASN   B N     1 
ATOM   12734 C  CA    . ASN   B  1  498  ? -17.152 32.563  101.974 1.00 40.27 ? 496  ASN   B CA    1 
ATOM   12735 C  C     . ASN   B  1  498  ? -17.943 31.294  101.682 1.00 38.72 ? 496  ASN   B C     1 
ATOM   12736 O  O     . ASN   B  1  498  ? -19.071 31.143  102.164 1.00 39.02 ? 496  ASN   B O     1 
ATOM   12737 C  CB    . ASN   B  1  498  ? -17.582 33.684  101.027 1.00 43.43 ? 496  ASN   B CB    1 
ATOM   12738 C  CG    . ASN   B  1  498  ? -17.044 35.038  101.446 1.00 50.48 ? 496  ASN   B CG    1 
ATOM   12739 O  OD1   . ASN   B  1  498  ? -16.807 35.286  102.628 1.00 53.31 ? 496  ASN   B OD1   1 
ATOM   12740 N  ND2   . ASN   B  1  498  ? -16.852 35.927  100.476 1.00 59.29 ? 496  ASN   B ND2   1 
ATOM   12741 N  N     . SER   B  1  499  ? -17.379 30.378  100.894 1.00 34.79 ? 497  SER   B N     1 
ATOM   12742 C  CA    . SER   B  1  499  ? -18.054 29.127  100.575 1.00 31.78 ? 497  SER   B CA    1 
ATOM   12743 C  C     . SER   B  1  499  ? -18.025 28.133  101.725 1.00 27.53 ? 497  SER   B C     1 
ATOM   12744 O  O     . SER   B  1  499  ? -18.686 27.095  101.640 1.00 30.90 ? 497  SER   B O     1 
ATOM   12745 C  CB    . SER   B  1  499  ? -17.372 28.482  99.369  1.00 34.38 ? 497  SER   B CB    1 
ATOM   12746 O  OG    . SER   B  1  499  ? -15.996 28.276  99.641  1.00 36.94 ? 497  SER   B OG    1 
ATOM   12747 N  N     . SER   B  1  500  ? -17.263 28.409  102.776 1.00 29.93 ? 498  SER   B N     1 
ATOM   12748 C  CA    . SER   B  1  500  ? -17.073 27.434  103.831 1.00 27.98 ? 498  SER   B CA    1 
ATOM   12749 C  C     . SER   B  1  500  ? -18.239 27.462  104.812 1.00 32.94 ? 498  SER   B C     1 
ATOM   12750 O  O     . SER   B  1  500  ? -18.833 28.510  105.079 1.00 35.57 ? 498  SER   B O     1 
ATOM   12751 C  CB    . SER   B  1  500  ? -15.751 27.688  104.562 1.00 34.44 ? 498  SER   B CB    1 
ATOM   12752 O  OG    . SER   B  1  500  ? -15.723 28.986  105.136 1.00 40.43 ? 498  SER   B OG    1 
ATOM   12753 N  N     . PHE   B  1  501  ? -18.576 26.283  105.333 1.00 28.59 ? 499  PHE   B N     1 
ATOM   12754 C  CA    . PHE   B  1  501  ? -19.597 26.205  106.370 1.00 31.35 ? 499  PHE   B CA    1 
ATOM   12755 C  C     . PHE   B  1  501  ? -19.228 27.048  107.587 1.00 37.43 ? 499  PHE   B C     1 
ATOM   12756 O  O     . PHE   B  1  501  ? -20.113 27.651  108.203 1.00 43.96 ? 499  PHE   B O     1 
ATOM   12757 C  CB    . PHE   B  1  501  ? -19.854 24.740  106.745 1.00 31.79 ? 499  PHE   B CB    1 
ATOM   12758 C  CG    . PHE   B  1  501  ? -21.057 24.538  107.636 1.00 32.72 ? 499  PHE   B CG    1 
ATOM   12759 C  CD1   . PHE   B  1  501  ? -20.940 24.627  109.012 1.00 36.53 ? 499  PHE   B CD1   1 
ATOM   12760 C  CD2   . PHE   B  1  501  ? -22.294 24.239  107.092 1.00 32.57 ? 499  PHE   B CD2   1 
ATOM   12761 C  CE1   . PHE   B  1  501  ? -22.050 24.437  109.834 1.00 37.09 ? 499  PHE   B CE1   1 
ATOM   12762 C  CE2   . PHE   B  1  501  ? -23.405 24.050  107.904 1.00 38.43 ? 499  PHE   B CE2   1 
ATOM   12763 C  CZ    . PHE   B  1  501  ? -23.279 24.151  109.275 1.00 36.38 ? 499  PHE   B CZ    1 
ATOM   12764 N  N     . VAL   B  1  502  ? -17.936 27.138  107.926 1.00 39.42 ? 500  VAL   B N     1 
ATOM   12765 C  CA    . VAL   B  1  502  ? -17.526 27.905  109.106 1.00 46.08 ? 500  VAL   B CA    1 
ATOM   12766 C  C     . VAL   B  1  502  ? -17.864 29.383  108.958 1.00 46.39 ? 500  VAL   B C     1 
ATOM   12767 O  O     . VAL   B  1  502  ? -18.157 30.064  109.948 1.00 46.59 ? 500  VAL   B O     1 
ATOM   12768 C  CB    . VAL   B  1  502  ? -16.034 27.688  109.436 1.00 46.02 ? 500  VAL   B CB    1 
ATOM   12769 C  CG1   . VAL   B  1  502  ? -15.773 26.237  109.800 1.00 48.14 ? 500  VAL   B CG1   1 
ATOM   12770 C  CG2   . VAL   B  1  502  ? -15.155 28.142  108.279 1.00 41.16 ? 500  VAL   B CG2   1 
ATOM   12771 N  N     . HIS   B  1  503  ? -17.815 29.908  107.735 1.00 39.69 ? 501  HIS   B N     1 
ATOM   12772 C  CA    . HIS   B  1  503  ? -18.220 31.288  107.499 1.00 39.58 ? 501  HIS   B CA    1 
ATOM   12773 C  C     . HIS   B  1  503  ? -19.733 31.397  107.350 1.00 43.36 ? 501  HIS   B C     1 
ATOM   12774 O  O     . HIS   B  1  503  ? -20.352 32.312  107.907 1.00 37.56 ? 501  HIS   B O     1 
ATOM   12775 C  CB    . HIS   B  1  503  ? -17.507 31.825  106.256 1.00 40.12 ? 501  HIS   B CB    1 
ATOM   12776 C  CG    . HIS   B  1  503  ? -17.998 33.163  105.798 1.00 37.13 ? 501  HIS   B CG    1 
ATOM   12777 N  ND1   . HIS   B  1  503  ? -19.035 33.308  104.900 1.00 42.76 ? 501  HIS   B ND1   1 
ATOM   12778 C  CD2   . HIS   B  1  503  ? -17.586 34.417  106.103 1.00 42.49 ? 501  HIS   B CD2   1 
ATOM   12779 C  CE1   . HIS   B  1  503  ? -19.244 34.594  104.677 1.00 42.29 ? 501  HIS   B CE1   1 
ATOM   12780 N  NE2   . HIS   B  1  503  ? -18.379 35.287  105.394 1.00 42.67 ? 501  HIS   B NE2   1 
ATOM   12781 N  N     . ARG   B  1  504  ? -20.346 30.447  106.637 1.00 36.28 ? 502  ARG   B N     1 
ATOM   12782 C  CA    . ARG   B  1  504  ? -21.759 30.561  106.294 1.00 32.69 ? 502  ARG   B CA    1 
ATOM   12783 C  C     . ARG   B  1  504  ? -22.665 30.419  107.512 1.00 39.51 ? 502  ARG   B C     1 
ATOM   12784 O  O     . ARG   B  1  504  ? -23.711 31.073  107.576 1.00 37.71 ? 502  ARG   B O     1 
ATOM   12785 C  CB    . ARG   B  1  504  ? -22.120 29.544  105.211 1.00 38.42 ? 502  ARG   B CB    1 
ATOM   12786 C  CG    . ARG   B  1  504  ? -21.493 29.872  103.865 1.00 38.01 ? 502  ARG   B CG    1 
ATOM   12787 C  CD    . ARG   B  1  504  ? -21.476 28.677  102.906 1.00 31.28 ? 502  ARG   B CD    1 
ATOM   12788 N  NE    . ARG   B  1  504  ? -22.800 28.130  102.652 1.00 32.40 ? 502  ARG   B NE    1 
ATOM   12789 C  CZ    . ARG   B  1  504  ? -23.735 28.736  101.934 1.00 36.88 ? 502  ARG   B CZ    1 
ATOM   12790 N  NH1   . ARG   B  1  504  ? -23.546 29.947  101.433 1.00 36.10 ? 502  ARG   B NH1   1 
ATOM   12791 N  NH2   . ARG   B  1  504  ? -24.888 28.112  101.711 1.00 36.75 ? 502  ARG   B NH2   1 
ATOM   12792 N  N     . ILE   B  1  505  ? -22.287 29.580  108.479 1.00 39.13 ? 503  ILE   B N     1 
ATOM   12793 C  CA    . ILE   B  1  505  ? -23.105 29.414  109.679 1.00 39.07 ? 503  ILE   B CA    1 
ATOM   12794 C  C     . ILE   B  1  505  ? -23.260 30.734  110.427 1.00 43.33 ? 503  ILE   B C     1 
ATOM   12795 O  O     . ILE   B  1  505  ? -24.291 30.977  111.069 1.00 38.36 ? 503  ILE   B O     1 
ATOM   12796 C  CB    . ILE   B  1  505  ? -22.532 28.295  110.574 1.00 36.12 ? 503  ILE   B CB    1 
ATOM   12797 N  N     . ASN   B  1  506  ? -22.261 31.612  110.343 1.00 38.69 ? 504  ASN   B N     1 
ATOM   12798 C  CA    . ASN   B  1  506  ? -22.283 32.895  111.032 1.00 45.11 ? 504  ASN   B CA    1 
ATOM   12799 C  C     . ASN   B  1  506  ? -22.731 34.045  110.141 1.00 46.62 ? 504  ASN   B C     1 
ATOM   12800 O  O     . ASN   B  1  506  ? -22.703 35.200  110.578 1.00 47.93 ? 504  ASN   B O     1 
ATOM   12801 C  CB    . ASN   B  1  506  ? -20.916 33.194  111.650 1.00 45.38 ? 504  ASN   B CB    1 
ATOM   12802 C  CG    . ASN   B  1  506  ? -20.593 32.276  112.810 1.00 46.79 ? 504  ASN   B CG    1 
ATOM   12803 O  OD1   . ASN   B  1  506  ? -21.431 32.038  113.679 1.00 50.83 ? 504  ASN   B OD1   1 
ATOM   12804 N  ND2   . ASN   B  1  506  ? -19.380 31.737  112.819 1.00 53.75 ? 504  ASN   B ND2   1 
ATOM   12805 N  N     . ASP   B  1  507  ? -23.146 33.761  108.908 1.00 42.17 ? 505  ASP   B N     1 
ATOM   12806 C  CA    . ASP   B  1  507  ? -23.629 34.802  108.017 1.00 45.38 ? 505  ASP   B CA    1 
ATOM   12807 C  C     . ASP   B  1  507  ? -25.147 34.839  108.089 1.00 50.52 ? 505  ASP   B C     1 
ATOM   12808 O  O     . ASP   B  1  507  ? -25.800 33.874  107.662 1.00 46.41 ? 505  ASP   B O     1 
ATOM   12809 C  CB    . ASP   B  1  507  ? -23.174 34.528  106.587 1.00 44.17 ? 505  ASP   B CB    1 
ATOM   12810 C  CG    . ASP   B  1  507  ? -23.259 35.756  105.706 1.00 50.63 ? 505  ASP   B CG    1 
ATOM   12811 O  OD1   . ASP   B  1  507  ? -24.164 36.590  105.930 1.00 57.17 ? 505  ASP   B OD1   1 
ATOM   12812 O  OD2   . ASP   B  1  507  ? -22.415 35.892  104.796 1.00 59.68 ? 505  ASP   B OD2   1 
ATOM   12813 N  N     . PRO   B  1  508  ? -25.752 35.911  108.611 1.00 55.14 ? 506  PRO   B N     1 
ATOM   12814 C  CA    . PRO   B  1  508  ? -27.219 35.944  108.722 1.00 54.18 ? 506  PRO   B CA    1 
ATOM   12815 C  C     . PRO   B  1  508  ? -27.930 36.022  107.385 1.00 52.80 ? 506  PRO   B C     1 
ATOM   12816 O  O     . PRO   B  1  508  ? -29.136 35.753  107.328 1.00 58.99 ? 506  PRO   B O     1 
ATOM   12817 C  CB    . PRO   B  1  508  ? -27.487 37.197  109.572 1.00 60.29 ? 506  PRO   B CB    1 
ATOM   12818 C  CG    . PRO   B  1  508  ? -26.149 37.588  110.147 1.00 57.95 ? 506  PRO   B CG    1 
ATOM   12819 C  CD    . PRO   B  1  508  ? -25.129 37.123  109.162 1.00 51.79 ? 506  PRO   B CD    1 
ATOM   12820 N  N     . LYS   B  1  509  ? -27.229 36.387  106.310 1.00 53.02 ? 507  LYS   B N     1 
ATOM   12821 C  CA    . LYS   B  1  509  ? -27.827 36.385  104.982 1.00 52.44 ? 507  LYS   B CA    1 
ATOM   12822 C  C     . LYS   B  1  509  ? -28.045 34.980  104.440 1.00 57.36 ? 507  LYS   B C     1 
ATOM   12823 O  O     . LYS   B  1  509  ? -28.707 34.828  103.408 1.00 62.11 ? 507  LYS   B O     1 
ATOM   12824 C  CB    . LYS   B  1  509  ? -26.953 37.184  104.013 1.00 49.95 ? 507  LYS   B CB    1 
ATOM   12825 N  N     . VAL   B  1  510  ? -27.515 33.959  105.108 1.00 57.07 ? 508  VAL   B N     1 
ATOM   12826 C  CA    . VAL   B  1  510  ? -27.626 32.575  104.664 1.00 50.87 ? 508  VAL   B CA    1 
ATOM   12827 C  C     . VAL   B  1  510  ? -28.668 31.882  105.530 1.00 51.10 ? 508  VAL   B C     1 
ATOM   12828 O  O     . VAL   B  1  510  ? -28.488 31.752  106.746 1.00 53.34 ? 508  VAL   B O     1 
ATOM   12829 C  CB    . VAL   B  1  510  ? -26.270 31.857  104.749 1.00 46.54 ? 508  VAL   B CB    1 
ATOM   12830 C  CG1   . VAL   B  1  510  ? -26.379 30.450  104.188 1.00 47.57 ? 508  VAL   B CG1   1 
ATOM   12831 C  CG2   . VAL   B  1  510  ? -25.202 32.656  104.017 1.00 44.78 ? 508  VAL   B CG2   1 
ATOM   12832 N  N     . SER   B  1  511  ? -29.756 31.437  104.910 1.00 48.75 ? 509  SER   B N     1 
ATOM   12833 C  CA    . SER   B  1  511  ? -30.812 30.773  105.654 1.00 49.98 ? 509  SER   B CA    1 
ATOM   12834 C  C     . SER   B  1  511  ? -30.400 29.348  106.007 1.00 49.09 ? 509  SER   B C     1 
ATOM   12835 O  O     . SER   B  1  511  ? -29.443 28.788  105.462 1.00 46.74 ? 509  SER   B O     1 
ATOM   12836 C  CB    . SER   B  1  511  ? -32.105 30.740  104.840 1.00 48.23 ? 509  SER   B CB    1 
ATOM   12837 O  OG    . SER   B  1  511  ? -32.030 29.782  103.796 1.00 49.84 ? 509  SER   B OG    1 
ATOM   12838 N  N     . ILE   B  1  512  ? -31.148 28.756  106.938 1.00 47.20 ? 510  ILE   B N     1 
ATOM   12839 C  CA    . ILE   B  1  512  ? -30.966 27.341  107.232 1.00 44.66 ? 510  ILE   B CA    1 
ATOM   12840 C  C     . ILE   B  1  512  ? -31.355 26.489  106.028 1.00 50.68 ? 510  ILE   B C     1 
ATOM   12841 O  O     . ILE   B  1  512  ? -30.748 25.438  105.780 1.00 45.26 ? 510  ILE   B O     1 
ATOM   12842 C  CB    . ILE   B  1  512  ? -31.712 26.962  108.524 1.00 43.30 ? 510  ILE   B CB    1 
ATOM   12843 C  CG1   . ILE   B  1  512  ? -31.023 27.615  109.725 1.00 46.44 ? 510  ILE   B CG1   1 
ATOM   12844 C  CG2   . ILE   B  1  512  ? -31.772 25.455  108.698 1.00 42.46 ? 510  ILE   B CG2   1 
ATOM   12845 C  CD1   . ILE   B  1  512  ? -31.939 28.431  110.611 1.00 47.44 ? 510  ILE   B CD1   1 
ATOM   12846 N  N     . ASP   B  1  513  ? -32.338 26.938  105.241 1.00 45.15 ? 511  ASP   B N     1 
ATOM   12847 C  CA    . ASP   B  1  513  ? -32.703 26.220  104.023 1.00 45.72 ? 511  ASP   B CA    1 
ATOM   12848 C  C     . ASP   B  1  513  ? -31.518 26.108  103.071 1.00 40.27 ? 511  ASP   B C     1 
ATOM   12849 O  O     . ASP   B  1  513  ? -31.250 25.034  102.521 1.00 41.41 ? 511  ASP   B O     1 
ATOM   12850 C  CB    . ASP   B  1  513  ? -33.888 26.903  103.335 1.00 48.94 ? 511  ASP   B CB    1 
ATOM   12851 C  CG    . ASP   B  1  513  ? -35.223 26.558  103.978 1.00 54.35 ? 511  ASP   B CG    1 
ATOM   12852 O  OD1   . ASP   B  1  513  ? -35.334 25.481  104.607 1.00 52.82 ? 511  ASP   B OD1   1 
ATOM   12853 O  OD2   . ASP   B  1  513  ? -36.169 27.362  103.843 1.00 60.61 ? 511  ASP   B OD2   1 
ATOM   12854 N  N     . GLU   B  1  514  ? -30.799 27.214  102.858 1.00 40.75 ? 512  GLU   B N     1 
ATOM   12855 C  CA    . GLU   B  1  514  ? -29.617 27.172  102.000 1.00 43.20 ? 512  GLU   B CA    1 
ATOM   12856 C  C     . GLU   B  1  514  ? -28.560 26.225  102.556 1.00 42.38 ? 512  GLU   B C     1 
ATOM   12857 O  O     . GLU   B  1  514  ? -27.921 25.484  101.802 1.00 38.54 ? 512  GLU   B O     1 
ATOM   12858 C  CB    . GLU   B  1  514  ? -29.032 28.575  101.843 1.00 41.25 ? 512  GLU   B CB    1 
ATOM   12859 C  CG    . GLU   B  1  514  ? -29.929 29.554  101.112 1.00 52.25 ? 512  GLU   B CG    1 
ATOM   12860 C  CD    . GLU   B  1  514  ? -29.380 30.967  101.135 1.00 56.16 ? 512  GLU   B CD    1 
ATOM   12861 O  OE1   . GLU   B  1  514  ? -29.719 31.724  102.069 1.00 54.24 ? 512  GLU   B OE1   1 
ATOM   12862 O  OE2   . GLU   B  1  514  ? -28.598 31.316  100.225 1.00 64.25 ? 512  GLU   B OE2   1 
ATOM   12863 N  N     . LEU   B  1  515  ? -28.363 26.235  103.876 1.00 37.40 ? 513  LEU   B N     1 
ATOM   12864 C  CA    . LEU   B  1  515  ? -27.322 25.409  104.477 1.00 37.51 ? 513  LEU   B CA    1 
ATOM   12865 C  C     . LEU   B  1  515  ? -27.659 23.927  104.410 1.00 34.25 ? 513  LEU   B C     1 
ATOM   12866 O  O     . LEU   B  1  515  ? -26.751 23.088  104.400 1.00 35.77 ? 513  LEU   B O     1 
ATOM   12867 C  CB    . LEU   B  1  515  ? -27.101 25.823  105.928 1.00 33.80 ? 513  LEU   B CB    1 
ATOM   12868 C  CG    . LEU   B  1  515  ? -26.492 27.202  106.160 1.00 35.79 ? 513  LEU   B CG    1 
ATOM   12869 C  CD1   . LEU   B  1  515  ? -26.545 27.522  107.646 1.00 39.76 ? 513  LEU   B CD1   1 
ATOM   12870 C  CD2   . LEU   B  1  515  ? -25.065 27.266  105.651 1.00 35.74 ? 513  LEU   B CD2   1 
ATOM   12871 N  N     . ILE   B  1  516  ? -28.949 23.580  104.379 1.00 34.30 ? 514  ILE   B N     1 
ATOM   12872 C  CA    . ILE   B  1  516  ? -29.350 22.180  104.319 1.00 30.62 ? 514  ILE   B CA    1 
ATOM   12873 C  C     . ILE   B  1  516  ? -29.601 21.713  102.897 1.00 30.59 ? 514  ILE   B C     1 
ATOM   12874 O  O     . ILE   B  1  516  ? -30.011 20.561  102.701 1.00 30.05 ? 514  ILE   B O     1 
ATOM   12875 C  CB    . ILE   B  1  516  ? -30.550 21.868  105.237 1.00 33.63 ? 514  ILE   B CB    1 
ATOM   12876 C  CG1   . ILE   B  1  516  ? -31.827 22.515  104.688 1.00 36.54 ? 514  ILE   B CG1   1 
ATOM   12877 C  CG2   . ILE   B  1  516  ? -30.256 22.327  106.655 1.00 35.07 ? 514  ILE   B CG2   1 
ATOM   12878 C  CD1   . ILE   B  1  516  ? -33.058 22.305  105.563 1.00 39.59 ? 514  ILE   B CD1   1 
ATOM   12879 N  N     . ALA   B  1  517  ? -29.377 22.570  101.905 1.00 33.86 ? 515  ALA   B N     1 
ATOM   12880 C  CA    . ALA   B  1  517  ? -29.475 22.150  100.515 1.00 34.70 ? 515  ALA   B CA    1 
ATOM   12881 C  C     . ALA   B  1  517  ? -28.607 20.921  100.287 1.00 32.09 ? 515  ALA   B C     1 
ATOM   12882 O  O     . ALA   B  1  517  ? -27.481 20.834  100.787 1.00 30.67 ? 515  ALA   B O     1 
ATOM   12883 C  CB    . ALA   B  1  517  ? -29.022 23.281  99.593  1.00 31.80 ? 515  ALA   B CB    1 
ATOM   12884 N  N     . ASP   B  1  518  ? -29.159 19.957  99.559  1.00 31.27 ? 516  ASP   B N     1 
ATOM   12885 C  CA    . ASP   B  1  518  ? -28.500 18.691  99.288  1.00 30.53 ? 516  ASP   B CA    1 
ATOM   12886 C  C     . ASP   B  1  518  ? -27.597 18.871  98.074  1.00 26.57 ? 516  ASP   B C     1 
ATOM   12887 O  O     . ASP   B  1  518  ? -28.084 19.027  96.949  1.00 29.05 ? 516  ASP   B O     1 
ATOM   12888 C  CB    . ASP   B  1  518  ? -29.558 17.613  99.040  1.00 29.21 ? 516  ASP   B CB    1 
ATOM   12889 C  CG    . ASP   B  1  518  ? -28.958 16.245  98.767  1.00 33.36 ? 516  ASP   B CG    1 
ATOM   12890 O  OD1   . ASP   B  1  518  ? -27.716 16.120  98.675  1.00 27.59 ? 516  ASP   B OD1   1 
ATOM   12891 O  OD2   . ASP   B  1  518  ? -29.736 15.281  98.637  1.00 36.41 ? 516  ASP   B OD2   1 
ATOM   12892 N  N     . PRO   B  1  519  ? -26.277 18.857  98.256  1.00 24.44 ? 517  PRO   B N     1 
ATOM   12893 C  CA    . PRO   B  1  519  ? -25.385 19.025  97.102  1.00 26.28 ? 517  PRO   B CA    1 
ATOM   12894 C  C     . PRO   B  1  519  ? -25.617 17.998  96.013  1.00 24.10 ? 517  PRO   B C     1 
ATOM   12895 O  O     . PRO   B  1  519  ? -25.492 18.330  94.831  1.00 24.67 ? 517  PRO   B O     1 
ATOM   12896 C  CB    . PRO   B  1  519  ? -23.979 18.913  97.716  1.00 26.08 ? 517  PRO   B CB    1 
ATOM   12897 C  CG    . PRO   B  1  519  ? -24.172 18.251  99.024  1.00 29.51 ? 517  PRO   B CG    1 
ATOM   12898 C  CD    . PRO   B  1  519  ? -25.548 18.602  99.509  1.00 24.77 ? 517  PRO   B CD    1 
ATOM   12899 N  N     . VAL   B  1  520  ? -25.956 16.762  96.383  1.00 24.72 ? 518  VAL   B N     1 
ATOM   12900 C  CA    . VAL   B  1  520  ? -26.144 15.701  95.395  1.00 25.05 ? 518  VAL   B CA    1 
ATOM   12901 C  C     . VAL   B  1  520  ? -27.271 16.061  94.436  1.00 26.92 ? 518  VAL   B C     1 
ATOM   12902 O  O     . VAL   B  1  520  ? -27.119 15.981  93.210  1.00 26.52 ? 518  VAL   B O     1 
ATOM   12903 C  CB    . VAL   B  1  520  ? -26.407 14.355  96.094  1.00 26.04 ? 518  VAL   B CB    1 
ATOM   12904 C  CG1   . VAL   B  1  520  ? -26.486 13.229  95.067  1.00 30.68 ? 518  VAL   B CG1   1 
ATOM   12905 C  CG2   . VAL   B  1  520  ? -25.336 14.081  97.144  1.00 27.39 ? 518  VAL   B CG2   1 
ATOM   12906 N  N     . GLU   B  1  521  ? -28.416 16.479  94.979  1.00 27.34 ? 519  GLU   B N     1 
ATOM   12907 C  CA    . GLU   B  1  521  ? -29.535 16.819  94.110  1.00 25.95 ? 519  GLU   B CA    1 
ATOM   12908 C  C     . GLU   B  1  521  ? -29.292 18.112  93.349  1.00 28.22 ? 519  GLU   B C     1 
ATOM   12909 O  O     . GLU   B  1  521  ? -29.766 18.256  92.217  1.00 30.62 ? 519  GLU   B O     1 
ATOM   12910 C  CB    . GLU   B  1  521  ? -30.839 16.851  94.907  1.00 29.83 ? 519  GLU   B CB    1 
ATOM   12911 C  CG    . GLU   B  1  521  ? -31.203 15.500  95.473  1.00 33.23 ? 519  GLU   B CG    1 
ATOM   12912 C  CD    . GLU   B  1  521  ? -31.254 14.415  94.410  1.00 38.33 ? 519  GLU   B CD    1 
ATOM   12913 O  OE1   . GLU   B  1  521  ? -31.641 14.717  93.260  1.00 38.59 ? 519  GLU   B OE1   1 
ATOM   12914 O  OE2   . GLU   B  1  521  ? -30.910 13.255  94.726  1.00 45.22 ? 519  GLU   B OE2   1 
ATOM   12915 N  N     . VAL   B  1  522  ? -28.554 19.056  93.929  1.00 27.92 ? 520  VAL   B N     1 
ATOM   12916 C  CA    . VAL   B  1  522  ? -28.246 20.276  93.195  1.00 26.36 ? 520  VAL   B CA    1 
ATOM   12917 C  C     . VAL   B  1  522  ? -27.362 19.963  91.995  1.00 29.42 ? 520  VAL   B C     1 
ATOM   12918 O  O     . VAL   B  1  522  ? -27.610 20.437  90.881  1.00 30.91 ? 520  VAL   B O     1 
ATOM   12919 C  CB    . VAL   B  1  522  ? -27.621 21.334  94.122  1.00 30.59 ? 520  VAL   B CB    1 
ATOM   12920 C  CG1   . VAL   B  1  522  ? -27.216 22.563  93.322  1.00 30.82 ? 520  VAL   B CG1   1 
ATOM   12921 C  CG2   . VAL   B  1  522  ? -28.592 21.707  95.236  1.00 37.63 ? 520  VAL   B CG2   1 
ATOM   12922 N  N     . VAL   B  1  523  ? -26.321 19.146  92.200  1.00 24.38 ? 521  VAL   B N     1 
ATOM   12923 C  CA    . VAL   B  1  523  ? -25.441 18.769  91.097  1.00 25.93 ? 521  VAL   B CA    1 
ATOM   12924 C  C     . VAL   B  1  523  ? -26.199 17.967  90.047  1.00 25.90 ? 521  VAL   B C     1 
ATOM   12925 O  O     . VAL   B  1  523  ? -25.995 18.151  88.842  1.00 27.09 ? 521  VAL   B O     1 
ATOM   12926 C  CB    . VAL   B  1  523  ? -24.209 18.008  91.622  1.00 26.77 ? 521  VAL   B CB    1 
ATOM   12927 C  CG1   . VAL   B  1  523  ? -23.433 17.412  90.473  1.00 25.23 ? 521  VAL   B CG1   1 
ATOM   12928 C  CG2   . VAL   B  1  523  ? -23.322 18.932  92.441  1.00 27.29 ? 521  VAL   B CG2   1 
ATOM   12929 N  N     . ARG   B  1  524  ? -27.065 17.053  90.485  1.00 27.07 ? 522  ARG   B N     1 
ATOM   12930 C  CA    . ARG   B  1  524  ? -27.797 16.224  89.534  1.00 28.05 ? 522  ARG   B CA    1 
ATOM   12931 C  C     . ARG   B  1  524  ? -28.622 17.072  88.575  1.00 29.84 ? 522  ARG   B C     1 
ATOM   12932 O  O     . ARG   B  1  524  ? -28.773 16.717  87.401  1.00 34.17 ? 522  ARG   B O     1 
ATOM   12933 C  CB    . ARG   B  1  524  ? -28.701 15.250  90.288  1.00 30.21 ? 522  ARG   B CB    1 
ATOM   12934 C  CG    . ARG   B  1  524  ? -29.414 14.256  89.398  1.00 33.41 ? 522  ARG   B CG    1 
ATOM   12935 C  CD    . ARG   B  1  524  ? -30.574 13.594  90.124  1.00 36.86 ? 522  ARG   B CD    1 
ATOM   12936 N  NE    . ARG   B  1  524  ? -30.182 13.053  91.420  1.00 33.82 ? 522  ARG   B NE    1 
ATOM   12937 C  CZ    . ARG   B  1  524  ? -29.514 11.918  91.589  1.00 33.37 ? 522  ARG   B CZ    1 
ATOM   12938 N  NH1   . ARG   B  1  524  ? -29.108 11.192  90.559  1.00 33.65 ? 522  ARG   B NH1   1 
ATOM   12939 N  NH2   . ARG   B  1  524  ? -29.240 11.504  92.823  1.00 34.53 ? 522  ARG   B NH2   1 
ATOM   12940 N  N     . ALA   B  1  525  ? -29.122 18.212  89.041  1.00 31.49 ? 523  ALA   B N     1 
ATOM   12941 C  CA    . ALA   B  1  525  ? -30.049 19.027  88.269  1.00 32.64 ? 523  ALA   B CA    1 
ATOM   12942 C  C     . ALA   B  1  525  ? -29.355 20.072  87.410  1.00 37.69 ? 523  ALA   B C     1 
ATOM   12943 O  O     . ALA   B  1  525  ? -30.032 20.777  86.653  1.00 35.71 ? 523  ALA   B O     1 
ATOM   12944 C  CB    . ALA   B  1  525  ? -31.055 19.704  89.204  1.00 35.28 ? 523  ALA   B CB    1 
ATOM   12945 N  N     . MET   B  1  526  ? -28.035 20.184  87.497  1.00 32.79 ? 524  MET   B N     1 
ATOM   12946 C  CA    A MET   B  1  526  ? -27.313 21.152  86.688  0.56 31.72 ? 524  MET   B CA    1 
ATOM   12947 C  CA    B MET   B  1  526  ? -27.326 21.158  86.688  0.44 31.76 ? 524  MET   B CA    1 
ATOM   12948 C  C     . MET   B  1  526  ? -27.393 20.769  85.212  1.00 31.41 ? 524  MET   B C     1 
ATOM   12949 O  O     . MET   B  1  526  ? -27.468 19.585  84.873  1.00 31.42 ? 524  MET   B O     1 
ATOM   12950 C  CB    A MET   B  1  526  ? -25.854 21.205  87.121  0.56 33.41 ? 524  MET   B CB    1 
ATOM   12951 C  CB    B MET   B  1  526  ? -25.875 21.260  87.140  0.44 33.41 ? 524  MET   B CB    1 
ATOM   12952 C  CG    A MET   B  1  526  ? -25.676 21.784  88.503  0.56 34.88 ? 524  MET   B CG    1 
ATOM   12953 C  CG    B MET   B  1  526  ? -25.649 22.353  88.167  0.44 35.44 ? 524  MET   B CG    1 
ATOM   12954 S  SD    A MET   B  1  526  ? -26.444 23.412  88.621  0.56 39.58 ? 524  MET   B SD    1 
ATOM   12955 S  SD    B MET   B  1  526  ? -24.227 22.029  89.218  0.44 36.87 ? 524  MET   B SD    1 
ATOM   12956 C  CE    A MET   B  1  526  ? -25.404 24.375  87.523  0.56 35.90 ? 524  MET   B CE    1 
ATOM   12957 C  CE    B MET   B  1  526  ? -23.619 23.687  89.510  0.44 38.12 ? 524  MET   B CE    1 
ATOM   12958 N  N     . PRO   B  1  527  ? -27.383 21.757  84.310  1.00 34.57 ? 525  PRO   B N     1 
ATOM   12959 C  CA    . PRO   B  1  527  ? -27.507 21.427  82.880  1.00 38.40 ? 525  PRO   B CA    1 
ATOM   12960 C  C     . PRO   B  1  527  ? -26.368 20.569  82.366  1.00 35.25 ? 525  PRO   B C     1 
ATOM   12961 O  O     . PRO   B  1  527  ? -26.595 19.660  81.557  1.00 32.66 ? 525  PRO   B O     1 
ATOM   12962 C  CB    . PRO   B  1  527  ? -27.558 22.805  82.205  1.00 41.97 ? 525  PRO   B CB    1 
ATOM   12963 C  CG    . PRO   B  1  527  ? -26.862 23.711  83.159  1.00 38.74 ? 525  PRO   B CG    1 
ATOM   12964 C  CD    . PRO   B  1  527  ? -27.201 23.202  84.530  1.00 38.15 ? 525  PRO   B CD    1 
ATOM   12965 N  N     . VAL   B  1  528  ? -25.146 20.826  82.821  1.00 31.48 ? 526  VAL   B N     1 
ATOM   12966 C  CA    . VAL   B  1  528  ? -23.992 20.001  82.497  1.00 28.22 ? 526  VAL   B CA    1 
ATOM   12967 C  C     . VAL   B  1  528  ? -23.441 19.515  83.832  1.00 25.76 ? 526  VAL   B C     1 
ATOM   12968 O  O     . VAL   B  1  528  ? -22.780 20.272  84.550  1.00 31.70 ? 526  VAL   B O     1 
ATOM   12969 C  CB    . VAL   B  1  528  ? -22.934 20.770  81.703  1.00 28.98 ? 526  VAL   B CB    1 
ATOM   12970 C  CG1   . VAL   B  1  528  ? -21.709 19.908  81.472  1.00 27.72 ? 526  VAL   B CG1   1 
ATOM   12971 C  CG2   . VAL   B  1  528  ? -23.512 21.221  80.369  1.00 30.92 ? 526  VAL   B CG2   1 
ATOM   12972 N  N     . VAL   B  1  529  ? -23.705 18.252  84.170  1.00 25.28 ? 527  VAL   B N     1 
ATOM   12973 C  CA    . VAL   B  1  529  ? -23.256 17.726  85.456  1.00 23.39 ? 527  VAL   B CA    1 
ATOM   12974 C  C     . VAL   B  1  529  ? -21.738 17.755  85.527  1.00 23.71 ? 527  VAL   B C     1 
ATOM   12975 O  O     . VAL   B  1  529  ? -21.040 17.239  84.645  1.00 24.42 ? 527  VAL   B O     1 
ATOM   12976 C  CB    . VAL   B  1  529  ? -23.794 16.308  85.678  1.00 23.83 ? 527  VAL   B CB    1 
ATOM   12977 C  CG1   . VAL   B  1  529  ? -23.171 15.690  86.927  1.00 23.79 ? 527  VAL   B CG1   1 
ATOM   12978 C  CG2   . VAL   B  1  529  ? -25.316 16.330  85.793  1.00 27.69 ? 527  VAL   B CG2   1 
ATOM   12979 N  N     . GLY   B  1  530  ? -21.215 18.385  86.573  1.00 22.75 ? 528  GLY   B N     1 
ATOM   12980 C  CA    . GLY   B  1  530  ? -19.784 18.395  86.777  1.00 22.60 ? 528  GLY   B CA    1 
ATOM   12981 C  C     . GLY   B  1  530  ? -19.019 19.434  85.996  1.00 21.07 ? 528  GLY   B C     1 
ATOM   12982 O  O     . GLY   B  1  530  ? -17.800 19.327  85.888  1.00 20.27 ? 528  GLY   B O     1 
ATOM   12983 N  N     . ALA   B  1  531  ? -19.685 20.439  85.441  1.00 20.62 ? 529  ALA   B N     1 
ATOM   12984 C  CA    . ALA   B  1  531  ? -18.958 21.475  84.728  1.00 20.02 ? 529  ALA   B CA    1 
ATOM   12985 C  C     . ALA   B  1  531  ? -18.011 22.201  85.670  1.00 20.98 ? 529  ALA   B C     1 
ATOM   12986 O  O     . ALA   B  1  531  ? -18.332 22.445  86.835  1.00 21.79 ? 529  ALA   B O     1 
ATOM   12987 C  CB    . ALA   B  1  531  ? -19.924 22.480  84.109  1.00 24.24 ? 529  ALA   B CB    1 
ATOM   12988 N  N     . LYS   B  1  532  ? -16.837 22.538  85.156  1.00 19.56 ? 530  LYS   B N     1 
ATOM   12989 C  CA    . LYS   B  1  532  ? -15.857 23.317  85.902  1.00 19.41 ? 530  LYS   B CA    1 
ATOM   12990 C  C     . LYS   B  1  532  ? -16.477 24.634  86.348  1.00 19.42 ? 530  LYS   B C     1 
ATOM   12991 O  O     . LYS   B  1  532  ? -17.414 25.152  85.729  1.00 20.41 ? 530  LYS   B O     1 
ATOM   12992 C  CB    . LYS   B  1  532  ? -14.658 23.594  84.980  1.00 23.35 ? 530  LYS   B CB    1 
ATOM   12993 C  CG    . LYS   B  1  532  ? -13.574 24.547  85.495  1.00 22.61 ? 530  LYS   B CG    1 
ATOM   12994 C  CD    . LYS   B  1  532  ? -12.526 24.826  84.407  1.00 23.74 ? 530  LYS   B CD    1 
ATOM   12995 C  CE    . LYS   B  1  532  ? -13.078 25.621  83.223  1.00 22.64 ? 530  LYS   B CE    1 
ATOM   12996 N  NZ    . LYS   B  1  532  ? -13.547 26.991  83.600  1.00 21.80 ? 530  LYS   B NZ    1 
ATOM   12997 N  N     . HIS   B  1  533  ? -15.963 25.166  87.447  1.00 18.27 ? 531  HIS   B N     1 
ATOM   12998 C  CA    . HIS   B  1  533  ? -16.327 26.509  87.862  1.00 19.18 ? 531  HIS   B CA    1 
ATOM   12999 C  C     . HIS   B  1  533  ? -16.138 27.483  86.706  1.00 19.54 ? 531  HIS   B C     1 
ATOM   13000 O  O     . HIS   B  1  533  ? -15.110 27.467  86.027  1.00 19.90 ? 531  HIS   B O     1 
ATOM   13001 C  CB    . HIS   B  1  533  ? -15.435 26.925  89.025  1.00 19.46 ? 531  HIS   B CB    1 
ATOM   13002 C  CG    . HIS   B  1  533  ? -15.981 28.068  89.813  1.00 22.23 ? 531  HIS   B CG    1 
ATOM   13003 N  ND1   . HIS   B  1  533  ? -16.116 29.334  89.287  1.00 21.62 ? 531  HIS   B ND1   1 
ATOM   13004 C  CD2   . HIS   B  1  533  ? -16.435 28.137  91.086  1.00 26.05 ? 531  HIS   B CD2   1 
ATOM   13005 C  CE1   . HIS   B  1  533  ? -16.646 30.131  90.199  1.00 27.52 ? 531  HIS   B CE1   1 
ATOM   13006 N  NE2   . HIS   B  1  533  ? -16.844 29.430  91.301  1.00 34.11 ? 531  HIS   B NE2   1 
ATOM   13007 N  N     . ASP   B  1  534  ? -17.148 28.332  86.493  1.00 20.49 ? 532  ASP   B N     1 
ATOM   13008 C  CA    . ASP   B  1  534  ? -17.124 29.303  85.401  1.00 23.17 ? 532  ASP   B CA    1 
ATOM   13009 C  C     . ASP   B  1  534  ? -15.993 30.310  85.544  1.00 23.42 ? 532  ASP   B C     1 
ATOM   13010 O  O     . ASP   B  1  534  ? -15.541 30.878  84.545  1.00 26.93 ? 532  ASP   B O     1 
ATOM   13011 C  CB    . ASP   B  1  534  ? -18.444 30.080  85.380  1.00 29.67 ? 532  ASP   B CB    1 
ATOM   13012 C  CG    . ASP   B  1  534  ? -19.596 29.266  84.854  1.00 39.88 ? 532  ASP   B CG    1 
ATOM   13013 O  OD1   . ASP   B  1  534  ? -19.353 28.383  84.005  1.00 45.82 ? 532  ASP   B OD1   1 
ATOM   13014 O  OD2   . ASP   B  1  534  ? -20.746 29.520  85.282  1.00 45.72 ? 532  ASP   B OD2   1 
ATOM   13015 N  N     . ARG   B  1  535  ? -15.528 30.559  86.764  1.00 21.26 ? 533  ARG   B N     1 
ATOM   13016 C  CA    . ARG   B  1  535  ? -14.593 31.645  87.013  1.00 21.17 ? 533  ARG   B CA    1 
ATOM   13017 C  C     . ARG   B  1  535  ? -13.197 31.151  87.351  1.00 21.21 ? 533  ARG   B C     1 
ATOM   13018 O  O     . ARG   B  1  535  ? -12.381 31.933  87.839  1.00 24.15 ? 533  ARG   B O     1 
ATOM   13019 C  CB    . ARG   B  1  535  ? -15.117 32.564  88.120  1.00 26.02 ? 533  ARG   B CB    1 
ATOM   13020 N  N     . ILE   B  1  536  ? -12.914 29.873  87.132  1.00 18.60 ? 534  ILE   B N     1 
ATOM   13021 C  CA    . ILE   B  1  536  ? -11.580 29.318  87.311  1.00 17.39 ? 534  ILE   B CA    1 
ATOM   13022 C  C     . ILE   B  1  536  ? -11.133 28.786  85.967  1.00 17.74 ? 534  ILE   B C     1 
ATOM   13023 O  O     . ILE   B  1  536  ? -11.778 27.897  85.398  1.00 19.60 ? 534  ILE   B O     1 
ATOM   13024 C  CB    . ILE   B  1  536  ? -11.568 28.200  88.355  1.00 18.12 ? 534  ILE   B CB    1 
ATOM   13025 C  CG1   . ILE   B  1  536  ? -11.982 28.774  89.704  1.00 18.51 ? 534  ILE   B CG1   1 
ATOM   13026 C  CG2   . ILE   B  1  536  ? -10.167 27.601  88.469  1.00 18.98 ? 534  ILE   B CG2   1 
ATOM   13027 C  CD1   . ILE   B  1  536  ? -12.114 27.715  90.755  1.00 24.02 ? 534  ILE   B CD1   1 
ATOM   13028 N  N     . ALA   B  1  537  ? -10.047 29.336  85.453  1.00 16.89 ? 535  ALA   B N     1 
ATOM   13029 C  CA    . ALA   B  1  537  ? -9.567  28.926  84.146  1.00 17.74 ? 535  ALA   B CA    1 
ATOM   13030 C  C     . ALA   B  1  537  ? -8.787  27.623  84.244  1.00 16.00 ? 535  ALA   B C     1 
ATOM   13031 O  O     . ALA   B  1  537  ? -7.952  27.445  85.138  1.00 16.37 ? 535  ALA   B O     1 
ATOM   13032 C  CB    . ALA   B  1  537  ? -8.668  30.013  83.564  1.00 18.60 ? 535  ALA   B CB    1 
ATOM   13033 N  N     . LEU   B  1  538  ? -9.057  26.710  83.313  1.00 16.04 ? 536  LEU   B N     1 
ATOM   13034 C  CA    . LEU   B  1  538  ? -8.128  25.612  83.121  1.00 16.11 ? 536  LEU   B CA    1 
ATOM   13035 C  C     . LEU   B  1  538  ? -6.754  26.195  82.815  1.00 16.47 ? 536  LEU   B C     1 
ATOM   13036 O  O     . LEU   B  1  538  ? -6.651  27.296  82.262  1.00 18.02 ? 536  LEU   B O     1 
ATOM   13037 C  CB    . LEU   B  1  538  ? -8.555  24.746  81.942  1.00 18.68 ? 536  LEU   B CB    1 
ATOM   13038 C  CG    . LEU   B  1  538  ? -9.741  23.818  82.174  1.00 20.48 ? 536  LEU   B CG    1 
ATOM   13039 C  CD1   . LEU   B  1  538  ? -10.136 23.159  80.855  1.00 23.93 ? 536  LEU   B CD1   1 
ATOM   13040 C  CD2   . LEU   B  1  538  ? -9.399  22.775  83.227  1.00 21.15 ? 536  LEU   B CD2   1 
ATOM   13041 N  N     . PRO   B  1  539  ? -5.682  25.487  83.165  1.00 15.34 ? 537  PRO   B N     1 
ATOM   13042 C  CA    . PRO   B  1  539  ? -4.343  26.001  82.849  1.00 15.42 ? 537  PRO   B CA    1 
ATOM   13043 C  C     . PRO   B  1  539  ? -4.194  26.379  81.394  1.00 16.06 ? 537  PRO   B C     1 
ATOM   13044 O  O     . PRO   B  1  539  ? -3.633  27.436  81.098  1.00 16.19 ? 537  PRO   B O     1 
ATOM   13045 C  CB    . PRO   B  1  539  ? -3.418  24.862  83.291  1.00 16.04 ? 537  PRO   B CB    1 
ATOM   13046 C  CG    . PRO   B  1  539  ? -4.197  24.212  84.421  1.00 15.77 ? 537  PRO   B CG    1 
ATOM   13047 C  CD    . PRO   B  1  539  ? -5.636  24.262  83.979  1.00 17.42 ? 537  PRO   B CD    1 
ATOM   13048 N  N     . ALA   B  1  540  ? -4.754  25.587  80.489  1.00 15.27 ? 538  ALA   B N     1 
ATOM   13049 C  CA    . ALA   B  1  540  ? -4.635  25.898  79.068  1.00 16.32 ? 538  ALA   B CA    1 
ATOM   13050 C  C     . ALA   B  1  540  ? -5.315  27.208  78.702  1.00 17.80 ? 538  ALA   B C     1 
ATOM   13051 O  O     . ALA   B  1  540  ? -4.989  27.802  77.661  1.00 17.23 ? 538  ALA   B O     1 
ATOM   13052 C  CB    . ALA   B  1  540  ? -5.240  24.773  78.224  1.00 18.55 ? 538  ALA   B CB    1 
ATOM   13053 N  N     . GLU   B  1  541  ? -6.244  27.671  79.534  1.00 17.77 ? 539  GLU   B N     1 
ATOM   13054 C  CA    . GLU   B  1  541  ? -7.139  28.765  79.177  1.00 17.10 ? 539  GLU   B CA    1 
ATOM   13055 C  C     . GLU   B  1  541  ? -6.827  30.039  79.958  1.00 16.06 ? 539  GLU   B C     1 
ATOM   13056 O  O     . GLU   B  1  541  ? -7.630  30.969  79.967  1.00 18.00 ? 539  GLU   B O     1 
ATOM   13057 C  CB    . GLU   B  1  541  ? -8.601  28.307  79.301  1.00 21.00 ? 539  GLU   B CB    1 
ATOM   13058 C  CG    . GLU   B  1  541  ? -8.841  27.071  78.384  1.00 23.30 ? 539  GLU   B CG    1 
ATOM   13059 C  CD    . GLU   B  1  541  ? -10.242 26.450  78.397  1.00 35.64 ? 539  GLU   B CD    1 
ATOM   13060 O  OE1   . GLU   B  1  541  ? -11.111 26.875  79.175  1.00 32.34 ? 539  GLU   B OE1   1 
ATOM   13061 O  OE2   . GLU   B  1  541  ? -10.464 25.504  77.607  1.00 35.74 ? 539  GLU   B OE2   1 
ATOM   13062 N  N     . LEU   B  1  542  ? -5.637  30.129  80.563  1.00 15.44 ? 540  LEU   B N     1 
ATOM   13063 C  CA    . LEU   B  1  542  ? -5.313  31.309  81.368  1.00 16.54 ? 540  LEU   B CA    1 
ATOM   13064 C  C     . LEU   B  1  542  ? -5.436  32.605  80.586  1.00 16.39 ? 540  LEU   B C     1 
ATOM   13065 O  O     . LEU   B  1  542  ? -5.732  33.655  81.168  1.00 18.94 ? 540  LEU   B O     1 
ATOM   13066 C  CB    . LEU   B  1  542  ? -3.878  31.244  81.873  1.00 18.74 ? 540  LEU   B CB    1 
ATOM   13067 C  CG    . LEU   B  1  542  ? -3.534  30.304  83.007  1.00 21.04 ? 540  LEU   B CG    1 
ATOM   13068 C  CD1   . LEU   B  1  542  ? -2.120  30.609  83.466  1.00 18.45 ? 540  LEU   B CD1   1 
ATOM   13069 C  CD2   . LEU   B  1  542  ? -4.539  30.431  84.141  1.00 19.34 ? 540  LEU   B CD2   1 
ATOM   13070 N  N     . PHE   B  1  543  ? -5.198  32.567  79.277  1.00 16.47 ? 541  PHE   B N     1 
ATOM   13071 C  CA    . PHE   B  1  543  ? -5.196  33.773  78.464  1.00 17.42 ? 541  PHE   B CA    1 
ATOM   13072 C  C     . PHE   B  1  543  ? -6.468  33.911  77.651  1.00 17.68 ? 541  PHE   B C     1 
ATOM   13073 O  O     . PHE   B  1  543  ? -6.555  34.778  76.775  1.00 19.07 ? 541  PHE   B O     1 
ATOM   13074 C  CB    . PHE   B  1  543  ? -3.944  33.803  77.592  1.00 16.07 ? 541  PHE   B CB    1 
ATOM   13075 C  CG    . PHE   B  1  543  ? -2.706  33.551  78.381  1.00 15.71 ? 541  PHE   B CG    1 
ATOM   13076 C  CD1   . PHE   B  1  543  ? -2.397  34.363  79.458  1.00 19.41 ? 541  PHE   B CD1   1 
ATOM   13077 C  CD2   . PHE   B  1  543  ? -1.885  32.474  78.102  1.00 16.11 ? 541  PHE   B CD2   1 
ATOM   13078 C  CE1   . PHE   B  1  543  ? -1.267  34.128  80.221  1.00 18.40 ? 541  PHE   B CE1   1 
ATOM   13079 C  CE2   . PHE   B  1  543  ? -0.751  32.242  78.854  1.00 16.46 ? 541  PHE   B CE2   1 
ATOM   13080 C  CZ    . PHE   B  1  543  ? -0.444  33.068  79.923  1.00 17.94 ? 541  PHE   B CZ    1 
ATOM   13081 N  N     . GLY   B  1  544  ? -7.452  33.065  77.924  1.00 17.55 ? 542  GLY   B N     1 
ATOM   13082 C  CA    . GLY   B  1  544  ? -8.729  33.184  77.249  1.00 17.47 ? 542  GLY   B CA    1 
ATOM   13083 C  C     . GLY   B  1  544  ? -8.584  33.069  75.747  1.00 20.33 ? 542  GLY   B C     1 
ATOM   13084 O  O     . GLY   B  1  544  ? -7.857  32.216  75.222  1.00 21.87 ? 542  GLY   B O     1 
ATOM   13085 N  N     . ASP   B  1  545  ? -9.298  33.944  75.034  1.00 22.10 ? 543  ASP   B N     1 
ATOM   13086 C  CA    . ASP   B  1  545  ? -9.342  33.875  73.580  1.00 25.05 ? 543  ASP   B CA    1 
ATOM   13087 C  C     . ASP   B  1  545  ? -8.055  34.348  72.923  1.00 24.25 ? 543  ASP   B C     1 
ATOM   13088 O  O     . ASP   B  1  545  ? -7.891  34.135  71.716  1.00 23.40 ? 543  ASP   B O     1 
ATOM   13089 C  CB    . ASP   B  1  545  ? -10.504 34.718  73.038  1.00 25.70 ? 543  ASP   B CB    1 
ATOM   13090 C  CG    . ASP   B  1  545  ? -11.844 34.299  73.603  1.00 39.60 ? 543  ASP   B CG    1 
ATOM   13091 O  OD1   . ASP   B  1  545  ? -12.031 33.092  73.868  1.00 41.14 ? 543  ASP   B OD1   1 
ATOM   13092 O  OD2   . ASP   B  1  545  ? -12.713 35.183  73.774  1.00 55.02 ? 543  ASP   B OD2   1 
ATOM   13093 N  N     . ALA   B  1  546  ? -7.156  34.992  73.668  1.00 21.11 ? 544  ALA   B N     1 
ATOM   13094 C  CA    . ALA   B  1  546  ? -5.946  35.536  73.054  1.00 19.49 ? 544  ALA   B CA    1 
ATOM   13095 C  C     . ALA   B  1  546  ? -5.044  34.438  72.516  1.00 19.05 ? 544  ALA   B C     1 
ATOM   13096 O  O     . ALA   B  1  546  ? -4.502  34.564  71.417  1.00 18.85 ? 544  ALA   B O     1 
ATOM   13097 C  CB    . ALA   B  1  546  ? -5.174  36.390  74.060  1.00 22.17 ? 544  ALA   B CB    1 
ATOM   13098 N  N     . ARG   B  1  547  ? -4.840  33.374  73.285  1.00 18.46 ? 545  ARG   B N     1 
ATOM   13099 C  CA    . ARG   B  1  547  ? -3.937  32.312  72.866  1.00 17.71 ? 545  ARG   B CA    1 
ATOM   13100 C  C     . ARG   B  1  547  ? -4.053  31.183  73.865  1.00 16.47 ? 545  ARG   B C     1 
ATOM   13101 O  O     . ARG   B  1  547  ? -4.592  31.354  74.958  1.00 16.96 ? 545  ARG   B O     1 
ATOM   13102 C  CB    . ARG   B  1  547  ? -2.473  32.760  72.785  1.00 19.60 ? 545  ARG   B CB    1 
ATOM   13103 C  CG    . ARG   B  1  547  ? -1.943  33.255  74.091  1.00 18.19 ? 545  ARG   B CG    1 
ATOM   13104 C  CD    . ARG   B  1  547  ? -0.502  33.732  73.931  1.00 18.19 ? 545  ARG   B CD    1 
ATOM   13105 N  NE    . ARG   B  1  547  ? -0.186  34.624  75.029  1.00 16.25 ? 545  ARG   B NE    1 
ATOM   13106 C  CZ    . ARG   B  1  547  ? 0.581   34.299  76.058  1.00 17.28 ? 545  ARG   B CZ    1 
ATOM   13107 N  NH1   . ARG   B  1  547  ? 1.199   33.129  76.118  1.00 16.63 ? 545  ARG   B NH1   1 
ATOM   13108 N  NH2   . ARG   B  1  547  ? 0.741   35.178  77.037  1.00 17.70 ? 545  ARG   B NH2   1 
ATOM   13109 N  N     . THR   B  1  548  ? -3.581  30.023  73.455  1.00 16.29 ? 546  THR   B N     1 
ATOM   13110 C  CA    . THR   B  1  548  ? -3.580  28.851  74.305  1.00 16.06 ? 546  THR   B CA    1 
ATOM   13111 C  C     . THR   B  1  548  ? -2.282  28.823  75.095  1.00 14.90 ? 546  THR   B C     1 
ATOM   13112 O  O     . THR   B  1  548  ? -1.201  28.970  74.529  1.00 15.36 ? 546  THR   B O     1 
ATOM   13113 C  CB    . THR   B  1  548  ? -3.653  27.628  73.411  1.00 15.20 ? 546  THR   B CB    1 
ATOM   13114 O  OG1   . THR   B  1  548  ? -4.866  27.702  72.637  1.00 20.70 ? 546  THR   B OG1   1 
ATOM   13115 C  CG2   . THR   B  1  548  ? -3.634  26.372  74.231  1.00 17.87 ? 546  THR   B CG2   1 
ATOM   13116 N  N     . ASN   B  1  549  ? -2.384  28.634  76.400  1.00 14.48 ? 547  ASN   B N     1 
ATOM   13117 C  CA    . ASN   B  1  549  ? -1.209  28.556  77.238  1.00 13.55 ? 547  ASN   B CA    1 
ATOM   13118 C  C     . ASN   B  1  549  ? -0.432  27.291  76.900  1.00 13.74 ? 547  ASN   B C     1 
ATOM   13119 O  O     . ASN   B  1  549  ? -1.009  26.257  76.546  1.00 15.87 ? 547  ASN   B O     1 
ATOM   13120 C  CB    . ASN   B  1  549  ? -1.687  28.521  78.683  1.00 15.38 ? 547  ASN   B CB    1 
ATOM   13121 C  CG    . ASN   B  1  549  ? -0.574  28.676  79.662  1.00 14.86 ? 547  ASN   B CG    1 
ATOM   13122 O  OD1   . ASN   B  1  549  ? 0.516   29.139  79.326  1.00 14.93 ? 547  ASN   B OD1   1 
ATOM   13123 N  ND2   . ASN   B  1  549  ? -0.844  28.301  80.900  1.00 14.93 ? 547  ASN   B ND2   1 
ATOM   13124 N  N     . SER   B  1  550  ? 0.889   27.381  76.953  1.00 13.37 ? 548  SER   B N     1 
ATOM   13125 C  CA    . SER   B  1  550  ? 1.674   26.170  76.791  1.00 14.30 ? 548  SER   B CA    1 
ATOM   13126 C  C     . SER   B  1  550  ? 1.333   25.187  77.902  1.00 14.73 ? 548  SER   B C     1 
ATOM   13127 O  O     . SER   B  1  550  ? 0.926   25.574  79.002  1.00 15.67 ? 548  SER   B O     1 
ATOM   13128 C  CB    . SER   B  1  550  ? 3.157   26.496  76.856  1.00 14.83 ? 548  SER   B CB    1 
ATOM   13129 O  OG    . SER   B  1  550  ? 3.496   27.009  78.127  1.00 14.44 ? 548  SER   B OG    1 
ATOM   13130 N  N     . ALA   B  1  551  ? 1.486   23.906  77.602  1.00 15.60 ? 549  ALA   B N     1 
ATOM   13131 C  CA    . ALA   B  1  551  ? 1.244   22.851  78.572  1.00 16.56 ? 549  ALA   B CA    1 
ATOM   13132 C  C     . ALA   B  1  551  ? 2.555   22.239  79.025  1.00 15.75 ? 549  ALA   B C     1 
ATOM   13133 O  O     . ALA   B  1  551  ? 3.492   22.097  78.238  1.00 16.38 ? 549  ALA   B O     1 
ATOM   13134 C  CB    . ALA   B  1  551  ? 0.366   21.765  77.973  1.00 16.81 ? 549  ALA   B CB    1 
ATOM   13135 N  N     . GLY   B  1  552  ? 2.620   21.886  80.299  1.00 16.21 ? 550  GLY   B N     1 
ATOM   13136 C  CA    . GLY   B  1  552  ? 3.745   21.181  80.850  1.00 16.41 ? 550  GLY   B CA    1 
ATOM   13137 C  C     . GLY   B  1  552  ? 3.497   19.694  80.921  1.00 16.69 ? 550  GLY   B C     1 
ATOM   13138 O  O     . GLY   B  1  552  ? 2.650   19.136  80.217  1.00 18.44 ? 550  GLY   B O     1 
ATOM   13139 N  N     . LEU   B  1  553  ? 4.253   19.041  81.793  1.00 16.98 ? 551  LEU   B N     1 
ATOM   13140 C  CA    . LEU   B  1  553  ? 4.137   17.611  82.008  1.00 18.06 ? 551  LEU   B CA    1 
ATOM   13141 C  C     . LEU   B  1  553  ? 4.183   17.405  83.505  1.00 16.86 ? 551  LEU   B C     1 
ATOM   13142 O  O     . LEU   B  1  553  ? 4.918   18.100  84.202  1.00 18.68 ? 551  LEU   B O     1 
ATOM   13143 C  CB    . LEU   B  1  553  ? 5.307   16.854  81.366  1.00 17.26 ? 551  LEU   B CB    1 
ATOM   13144 C  CG    . LEU   B  1  553  ? 5.330   16.883  79.836  1.00 20.06 ? 551  LEU   B CG    1 
ATOM   13145 C  CD1   . LEU   B  1  553  ? 6.652   16.377  79.325  1.00 22.25 ? 551  LEU   B CD1   1 
ATOM   13146 C  CD2   . LEU   B  1  553  ? 4.194   16.048  79.273  1.00 22.66 ? 551  LEU   B CD2   1 
ATOM   13147 N  N     . ASP   B  1  554  ? 3.364   16.483  83.998  1.00 17.32 ? 552  ASP   B N     1 
ATOM   13148 C  CA    . ASP   B  1  554  ? 3.248   16.262  85.435  1.00 17.39 ? 552  ASP   B CA    1 
ATOM   13149 C  C     . ASP   B  1  554  ? 4.258   15.194  85.840  1.00 16.34 ? 552  ASP   B C     1 
ATOM   13150 O  O     . ASP   B  1  554  ? 4.031   14.003  85.625  1.00 17.74 ? 552  ASP   B O     1 
ATOM   13151 C  CB    . ASP   B  1  554  ? 1.833   15.825  85.768  1.00 19.32 ? 552  ASP   B CB    1 
ATOM   13152 C  CG    . ASP   B  1  554  ? 1.625   15.621  87.236  1.00 18.98 ? 552  ASP   B CG    1 
ATOM   13153 O  OD1   . ASP   B  1  554  ? 2.580   15.814  88.008  1.00 18.85 ? 552  ASP   B OD1   1 
ATOM   13154 O  OD2   . ASP   B  1  554  ? 0.496   15.267  87.612  1.00 20.28 ? 552  ASP   B OD2   1 
ATOM   13155 N  N     . LEU   B  1  555  ? 5.366   15.624  86.424  1.00 16.37 ? 553  LEU   B N     1 
ATOM   13156 C  CA    . LEU   B  1  555  ? 6.408   14.692  86.817  1.00 17.85 ? 553  LEU   B CA    1 
ATOM   13157 C  C     . LEU   B  1  555  ? 6.094   13.965  88.113  1.00 18.75 ? 553  LEU   B C     1 
ATOM   13158 O  O     . LEU   B  1  555  ? 6.953   13.258  88.638  1.00 18.44 ? 553  LEU   B O     1 
ATOM   13159 C  CB    . LEU   B  1  555  ? 7.747   15.411  86.913  1.00 17.25 ? 553  LEU   B CB    1 
ATOM   13160 C  CG    . LEU   B  1  555  ? 8.165   16.121  85.629  1.00 17.79 ? 553  LEU   B CG    1 
ATOM   13161 C  CD1   . LEU   B  1  555  ? 9.571   16.662  85.805  1.00 21.31 ? 553  LEU   B CD1   1 
ATOM   13162 C  CD2   . LEU   B  1  555  ? 8.070   15.172  84.428  1.00 21.86 ? 553  LEU   B CD2   1 
ATOM   13163 N  N     . SER   B  1  556  ? 4.882   14.114  88.641  1.00 16.64 ? 554  SER   B N     1 
ATOM   13164 C  CA    . SER   B  1  556  ? 4.418   13.266  89.727  1.00 18.09 ? 554  SER   B CA    1 
ATOM   13165 C  C     . SER   B  1  556  ? 3.467   12.190  89.238  1.00 18.82 ? 554  SER   B C     1 
ATOM   13166 O  O     . SER   B  1  556  ? 3.021   11.356  90.028  1.00 19.61 ? 554  SER   B O     1 
ATOM   13167 C  CB    . SER   B  1  556  ? 3.733   14.103  90.813  1.00 17.41 ? 554  SER   B CB    1 
ATOM   13168 O  OG    . SER   B  1  556  ? 2.480   14.567  90.340  1.00 18.74 ? 554  SER   B OG    1 
ATOM   13169 N  N     . ASN   B  1  557  ? 3.164   12.171  87.948  1.00 17.34 ? 555  ASN   B N     1 
ATOM   13170 C  CA    . ASN   B  1  557  ? 2.228   11.220  87.375  1.00 16.60 ? 555  ASN   B CA    1 
ATOM   13171 C  C     . ASN   B  1  557  ? 3.012   10.025  86.835  1.00 18.34 ? 555  ASN   B C     1 
ATOM   13172 O  O     . ASN   B  1  557  ? 3.842   10.187  85.937  1.00 17.86 ? 555  ASN   B O     1 
ATOM   13173 C  CB    . ASN   B  1  557  ? 1.435   11.915  86.267  1.00 17.31 ? 555  ASN   B CB    1 
ATOM   13174 C  CG    . ASN   B  1  557  ? 0.422   11.012  85.618  1.00 17.44 ? 555  ASN   B CG    1 
ATOM   13175 O  OD1   . ASN   B  1  557  ? 0.741   9.910   85.197  1.00 18.79 ? 555  ASN   B OD1   1 
ATOM   13176 N  ND2   . ASN   B  1  557  ? -0.829  11.470  85.535  1.00 19.47 ? 555  ASN   B ND2   1 
ATOM   13177 N  N     . GLU   B  1  558  ? 2.752   8.823   87.370  1.00 19.11 ? 556  GLU   B N     1 
ATOM   13178 C  CA    . GLU   B  1  558  ? 3.552   7.666   86.953  1.00 19.54 ? 556  GLU   B CA    1 
ATOM   13179 C  C     . GLU   B  1  558  ? 3.365   7.328   85.487  1.00 20.59 ? 556  GLU   B C     1 
ATOM   13180 O  O     . GLU   B  1  558  ? 4.291   6.815   84.859  1.00 19.69 ? 556  GLU   B O     1 
ATOM   13181 C  CB    . GLU   B  1  558  ? 3.236   6.406   87.761  1.00 21.22 ? 556  GLU   B CB    1 
ATOM   13182 C  CG    . GLU   B  1  558  ? 3.638   6.457   89.191  1.00 20.92 ? 556  GLU   B CG    1 
ATOM   13183 C  CD    . GLU   B  1  558  ? 5.138   6.602   89.459  1.00 21.51 ? 556  GLU   B CD    1 
ATOM   13184 O  OE1   . GLU   B  1  558  ? 6.005   6.416   88.573  1.00 21.33 ? 556  GLU   B OE1   1 
ATOM   13185 O  OE2   . GLU   B  1  558  ? 5.450   6.903   90.615  1.00 21.03 ? 556  GLU   B OE2   1 
ATOM   13186 N  N     . GLU   B  1  559  ? 2.176   7.551   84.927  1.00 19.01 ? 557  GLU   B N     1 
ATOM   13187 C  CA    . GLU   B  1  559  ? 2.019   7.333   83.494  1.00 19.13 ? 557  GLU   B CA    1 
ATOM   13188 C  C     . GLU   B  1  559  ? 2.930   8.269   82.731  1.00 19.19 ? 557  GLU   B C     1 
ATOM   13189 O  O     . GLU   B  1  559  ? 3.608   7.866   81.779  1.00 19.16 ? 557  GLU   B O     1 
ATOM   13190 C  CB    . GLU   B  1  559  ? 0.581   7.598   83.057  1.00 23.09 ? 557  GLU   B CB    1 
ATOM   13191 C  CG    . GLU   B  1  559  ? -0.452  6.655   83.576  1.00 26.47 ? 557  GLU   B CG    1 
ATOM   13192 C  CD    . GLU   B  1  559  ? -1.830  6.997   83.036  1.00 34.85 ? 557  GLU   B CD    1 
ATOM   13193 O  OE1   . GLU   B  1  559  ? -1.914  7.607   81.944  1.00 38.80 ? 557  GLU   B OE1   1 
ATOM   13194 O  OE2   . GLU   B  1  559  ? -2.825  6.665   83.706  1.00 30.71 ? 557  GLU   B OE2   1 
ATOM   13195 N  N     . THR   B  1  560  ? 2.943   9.535   83.131  1.00 18.42 ? 558  THR   B N     1 
ATOM   13196 C  CA    . THR   B  1  560  ? 3.790   10.508  82.461  1.00 17.85 ? 558  THR   B CA    1 
ATOM   13197 C  C     . THR   B  1  560  ? 5.249   10.138  82.616  1.00 17.33 ? 558  THR   B C     1 
ATOM   13198 O  O     . THR   B  1  560  ? 6.019   10.206  81.650  1.00 18.40 ? 558  THR   B O     1 
ATOM   13199 C  CB    . THR   B  1  560  ? 3.548   11.889  83.052  1.00 16.84 ? 558  THR   B CB    1 
ATOM   13200 O  OG1   . THR   B  1  560  ? 2.158   12.202  82.914  1.00 19.44 ? 558  THR   B OG1   1 
ATOM   13201 C  CG2   . THR   B  1  560  ? 4.369   12.939  82.317  1.00 19.13 ? 558  THR   B CG2   1 
ATOM   13202 N  N     . LEU   B  1  561  ? 5.659   9.748   83.820  1.00 16.37 ? 559  LEU   B N     1 
ATOM   13203 C  CA    . LEU   B  1  561  ? 7.060   9.404   84.020  1.00 14.84 ? 559  LEU   B CA    1 
ATOM   13204 C  C     . LEU   B  1  561  ? 7.454   8.200   83.179  1.00 17.84 ? 559  LEU   B C     1 
ATOM   13205 O  O     . LEU   B  1  561  ? 8.553   8.165   82.611  1.00 17.88 ? 559  LEU   B O     1 
ATOM   13206 C  CB    . LEU   B  1  561  ? 7.345   9.146   85.498  1.00 17.27 ? 559  LEU   B CB    1 
ATOM   13207 C  CG    . LEU   B  1  561  ? 7.256   10.396  86.364  1.00 15.97 ? 559  LEU   B CG    1 
ATOM   13208 C  CD1   . LEU   B  1  561  ? 7.396   10.025  87.839  1.00 18.93 ? 559  LEU   B CD1   1 
ATOM   13209 C  CD2   . LEU   B  1  561  ? 8.321   11.398  85.959  1.00 18.30 ? 559  LEU   B CD2   1 
ATOM   13210 N  N     . ALA   B  1  562  ? 6.570   7.211   83.073  1.00 16.98 ? 560  ALA   B N     1 
ATOM   13211 C  CA    . ALA   B  1  562  ? 6.895   6.030   82.284  1.00 18.18 ? 560  ALA   B CA    1 
ATOM   13212 C  C     . ALA   B  1  562  ? 6.990   6.374   80.804  1.00 20.83 ? 560  ALA   B C     1 
ATOM   13213 O  O     . ALA   B  1  562  ? 7.912   5.929   80.110  1.00 20.27 ? 560  ALA   B O     1 
ATOM   13214 C  CB    . ALA   B  1  562  ? 5.851   4.932   82.519  1.00 19.19 ? 560  ALA   B CB    1 
ATOM   13215 N  N     . SER   B  1  563  ? 6.041   7.154   80.294  1.00 17.99 ? 561  SER   B N     1 
ATOM   13216 C  CA    . SER   B  1  563  ? 6.104   7.503   78.881  1.00 16.97 ? 561  SER   B CA    1 
ATOM   13217 C  C     . SER   B  1  563  ? 7.256   8.457   78.607  1.00 18.26 ? 561  SER   B C     1 
ATOM   13218 O  O     . SER   B  1  563  ? 7.939   8.344   77.575  1.00 20.22 ? 561  SER   B O     1 
ATOM   13219 C  CB    . SER   B  1  563  ? 4.773   8.084   78.407  1.00 20.29 ? 561  SER   B CB    1 
ATOM   13220 O  OG    . SER   B  1  563  ? 4.506   9.327   79.014  1.00 24.55 ? 561  SER   B OG    1 
ATOM   13221 N  N     . LEU   B  1  564  ? 7.511   9.382   79.533  1.00 17.74 ? 562  LEU   B N     1 
ATOM   13222 C  CA    . LEU   B  1  564  ? 8.620   10.301  79.353  1.00 18.49 ? 562  LEU   B CA    1 
ATOM   13223 C  C     . LEU   B  1  564  ? 9.940   9.554   79.362  1.00 18.82 ? 562  LEU   B C     1 
ATOM   13224 O  O     . LEU   B  1  564  ? 10.814  9.820   78.526  1.00 18.55 ? 562  LEU   B O     1 
ATOM   13225 C  CB    . LEU   B  1  564  ? 8.577   11.386  80.430  1.00 18.37 ? 562  LEU   B CB    1 
ATOM   13226 C  CG    . LEU   B  1  564  ? 9.650   12.454  80.375  1.00 19.54 ? 562  LEU   B CG    1 
ATOM   13227 C  CD1   . LEU   B  1  564  ? 9.568   13.176  79.048  1.00 21.05 ? 562  LEU   B CD1   1 
ATOM   13228 C  CD2   . LEU   B  1  564  ? 9.461   13.422  81.530  1.00 21.82 ? 562  LEU   B CD2   1 
ATOM   13229 N  N     . THR   B  1  565  ? 10.105  8.610   80.293  1.00 18.18 ? 563  THR   B N     1 
ATOM   13230 C  CA    . THR   B  1  565  ? 11.313  7.795   80.308  1.00 17.68 ? 563  THR   B CA    1 
ATOM   13231 C  C     . THR   B  1  565  ? 11.590  7.215   78.932  1.00 19.67 ? 563  THR   B C     1 
ATOM   13232 O  O     . THR   B  1  565  ? 12.714  7.297   78.430  1.00 19.62 ? 563  THR   B O     1 
ATOM   13233 C  CB    . THR   B  1  565  ? 11.159  6.658   81.320  1.00 19.13 ? 563  THR   B CB    1 
ATOM   13234 O  OG1   . THR   B  1  565  ? 11.089  7.197   82.647  1.00 20.28 ? 563  THR   B OG1   1 
ATOM   13235 C  CG2   . THR   B  1  565  ? 12.365  5.736   81.251  1.00 20.41 ? 563  THR   B CG2   1 
ATOM   13236 N  N     . GLU   B  1  566  ? 10.567  6.639   78.297  1.00 18.39 ? 564  GLU   B N     1 
ATOM   13237 C  CA    . GLU   B  1  566  ? 10.766  6.032   76.984  1.00 18.41 ? 564  GLU   B CA    1 
ATOM   13238 C  C     . GLU   B  1  566  ? 11.141  7.077   75.944  1.00 18.05 ? 564  GLU   B C     1 
ATOM   13239 O  O     . GLU   B  1  566  ? 12.056  6.869   75.142  1.00 18.64 ? 564  GLU   B O     1 
ATOM   13240 C  CB    . GLU   B  1  566  ? 9.522   5.244   76.577  1.00 20.50 ? 564  GLU   B CB    1 
ATOM   13241 C  CG    . GLU   B  1  566  ? 9.315   4.009   77.456  1.00 28.97 ? 564  GLU   B CG    1 
ATOM   13242 C  CD    . GLU   B  1  566  ? 10.627  3.318   77.833  1.00 38.27 ? 564  GLU   B CD    1 
ATOM   13243 O  OE1   . GLU   B  1  566  ? 11.395  2.931   76.922  1.00 42.19 ? 564  GLU   B OE1   1 
ATOM   13244 O  OE2   . GLU   B  1  566  ? 10.892  3.159   79.047  1.00 36.85 ? 564  GLU   B OE2   1 
ATOM   13245 N  N     . ALA   B  1  567  ? 10.441  8.210   75.938  1.00 17.40 ? 565  ALA   B N     1 
ATOM   13246 C  CA    . ALA   B  1  567  ? 10.739  9.256   74.965  1.00 19.56 ? 565  ALA   B CA    1 
ATOM   13247 C  C     . ALA   B  1  567  ? 12.130  9.833   75.185  1.00 17.51 ? 565  ALA   B C     1 
ATOM   13248 O  O     . ALA   B  1  567  ? 12.841  10.146  74.222  1.00 17.66 ? 565  ALA   B O     1 
ATOM   13249 C  CB    . ALA   B  1  567  ? 9.684   10.356  75.052  1.00 19.23 ? 565  ALA   B CB    1 
ATOM   13250 N  N     . LEU   B  1  568  ? 12.554  9.944   76.441  1.00 16.58 ? 566  LEU   B N     1 
ATOM   13251 C  CA    . LEU   B  1  568  ? 13.885  10.466  76.725  1.00 16.54 ? 566  LEU   B CA    1 
ATOM   13252 C  C     . LEU   B  1  568  ? 14.943  9.484   76.260  1.00 17.29 ? 566  LEU   B C     1 
ATOM   13253 O  O     . LEU   B  1  568  ? 15.927  9.870   75.616  1.00 17.37 ? 566  LEU   B O     1 
ATOM   13254 C  CB    . LEU   B  1  568  ? 14.032  10.741  78.222  1.00 17.67 ? 566  LEU   B CB    1 
ATOM   13255 C  CG    . LEU   B  1  568  ? 13.107  11.837  78.752  1.00 16.34 ? 566  LEU   B CG    1 
ATOM   13256 C  CD1   . LEU   B  1  568  ? 13.214  11.897  80.269  1.00 19.08 ? 566  LEU   B CD1   1 
ATOM   13257 C  CD2   . LEU   B  1  568  ? 13.445  13.175  78.119  1.00 20.06 ? 566  LEU   B CD2   1 
ATOM   13258 N  N     . ARG   B  1  569  ? 14.753  8.206   76.581  1.00 17.66 ? 567  ARG   B N     1 
ATOM   13259 C  CA    . ARG   B  1  569  ? 15.680  7.189   76.106  1.00 18.28 ? 567  ARG   B CA    1 
ATOM   13260 C  C     . ARG   B  1  569  ? 15.766  7.210   74.590  1.00 18.20 ? 567  ARG   B C     1 
ATOM   13261 O  O     . ARG   B  1  569  ? 16.864  7.185   74.018  1.00 21.95 ? 567  ARG   B O     1 
ATOM   13262 C  CB    . ARG   B  1  569  ? 15.234  5.812   76.598  1.00 19.85 ? 567  ARG   B CB    1 
ATOM   13263 C  CG    . ARG   B  1  569  ? 15.521  5.607   78.067  1.00 26.66 ? 567  ARG   B CG    1 
ATOM   13264 C  CD    . ARG   B  1  569  ? 15.089  4.233   78.553  1.00 30.39 ? 567  ARG   B CD    1 
ATOM   13265 N  NE    . ARG   B  1  569  ? 15.203  4.150   80.005  1.00 33.89 ? 567  ARG   B NE    1 
ATOM   13266 C  CZ    . ARG   B  1  569  ? 14.612  3.227   80.754  1.00 33.83 ? 567  ARG   B CZ    1 
ATOM   13267 N  NH1   . ARG   B  1  569  ? 13.835  2.299   80.220  1.00 39.71 ? 567  ARG   B NH1   1 
ATOM   13268 N  NH2   . ARG   B  1  569  ? 14.796  3.246   82.072  1.00 38.81 ? 567  ARG   B NH2   1 
ATOM   13269 N  N     . GLU   B  1  570  ? 14.617  7.287   73.924  1.00 17.86 ? 568  GLU   B N     1 
ATOM   13270 C  CA    . GLU   B  1  570  ? 14.611  7.307   72.469  1.00 20.03 ? 568  GLU   B CA    1 
ATOM   13271 C  C     . GLU   B  1  570  ? 15.292  8.548   71.927  1.00 21.16 ? 568  GLU   B C     1 
ATOM   13272 O  O     . GLU   B  1  570  ? 15.921  8.488   70.869  1.00 22.44 ? 568  GLU   B O     1 
ATOM   13273 C  CB    . GLU   B  1  570  ? 13.175  7.228   71.955  1.00 22.66 ? 568  GLU   B CB    1 
ATOM   13274 C  CG    . GLU   B  1  570  ? 12.529  5.862   72.149  1.00 25.23 ? 568  GLU   B CG    1 
ATOM   13275 C  CD    . GLU   B  1  570  ? 11.006  5.923   72.173  1.00 36.69 ? 568  GLU   B CD    1 
ATOM   13276 O  OE1   . GLU   B  1  570  ? 10.437  6.968   71.786  1.00 34.40 ? 568  GLU   B OE1   1 
ATOM   13277 O  OE2   . GLU   B  1  570  ? 10.377  4.929   72.595  1.00 38.10 ? 568  GLU   B OE2   1 
ATOM   13278 N  N     . SER   B  1  571  ? 15.184  9.677   72.632  1.00 20.01 ? 569  SER   B N     1 
ATOM   13279 C  CA    . SER   B  1  571  ? 15.813  10.897  72.150  1.00 19.93 ? 569  SER   B CA    1 
ATOM   13280 C  C     . SER   B  1  571  ? 17.316  10.745  72.137  1.00 23.56 ? 569  SER   B C     1 
ATOM   13281 O  O     . SER   B  1  571  ? 17.994  11.306  71.268  1.00 24.53 ? 569  SER   B O     1 
ATOM   13282 C  CB    . SER   B  1  571  ? 15.415  12.094  73.014  1.00 20.92 ? 569  SER   B CB    1 
ATOM   13283 O  OG    . SER   B  1  571  ? 16.127  12.121  74.252  1.00 21.31 ? 569  SER   B OG    1 
ATOM   13284 N  N     . ALA   B  1  572  ? 17.852  9.959   73.064  1.00 20.53 ? 570  ALA   B N     1 
ATOM   13285 C  CA    . ALA   B  1  572  ? 19.292  9.785   73.114  1.00 20.20 ? 570  ALA   B CA    1 
ATOM   13286 C  C     . ALA   B  1  572  ? 19.792  8.854   72.015  1.00 25.47 ? 570  ALA   B C     1 
ATOM   13287 O  O     . ALA   B  1  572  ? 20.990  8.869   71.702  1.00 30.79 ? 570  ALA   B O     1 
ATOM   13288 C  CB    . ALA   B  1  572  ? 19.717  9.306   74.500  1.00 22.68 ? 570  ALA   B CB    1 
ATOM   13289 N  N     . ALA   B  1  573  ? 18.910  8.066   71.404  1.00 21.43 ? 571  ALA   B N     1 
ATOM   13290 C  CA    . ALA   B  1  573  ? 19.320  7.202   70.303  1.00 26.87 ? 571  ALA   B CA    1 
ATOM   13291 C  C     . ALA   B  1  573  ? 19.270  7.891   68.940  1.00 26.98 ? 571  ALA   B C     1 
ATOM   13292 O  O     . ALA   B  1  573  ? 19.751  7.318   67.955  1.00 26.59 ? 571  ALA   B O     1 
ATOM   13293 C  CB    . ALA   B  1  573  ? 18.464  5.932   70.285  1.00 27.63 ? 571  ALA   B CB    1 
ATOM   13294 N  N     . MET   B  1  574  ? 18.721  9.100   68.861  1.00 23.98 ? 572  MET   B N     1 
ATOM   13295 C  CA    . MET   B  1  574  ? 18.627  9.817   67.602  1.00 22.66 ? 572  MET   B CA    1 
ATOM   13296 C  C     . MET   B  1  574  ? 19.959  10.450  67.244  1.00 22.22 ? 572  MET   B C     1 
ATOM   13297 O  O     . MET   B  1  574  ? 20.748  10.827  68.114  1.00 22.79 ? 572  MET   B O     1 
ATOM   13298 C  CB    . MET   B  1  574  ? 17.594  10.932  67.724  1.00 22.13 ? 572  MET   B CB    1 
ATOM   13299 C  CG    . MET   B  1  574  ? 16.184  10.403  67.846  1.00 25.10 ? 572  MET   B CG    1 
ATOM   13300 S  SD    . MET   B  1  574  ? 15.043  11.669  68.408  1.00 24.92 ? 572  MET   B SD    1 
ATOM   13301 C  CE    . MET   B  1  574  ? 13.543  10.691  68.528  1.00 24.62 ? 572  MET   B CE    1 
ATOM   13302 N  N     . LYS   B  1  575  ? 20.196  10.589  65.944  1.00 20.69 ? 573  LYS   B N     1 
ATOM   13303 C  CA    . LYS   B  1  575  ? 21.376  11.301  65.455  1.00 20.01 ? 573  LYS   B CA    1 
ATOM   13304 C  C     . LYS   B  1  575  ? 21.039  12.782  65.388  1.00 20.28 ? 573  LYS   B C     1 
ATOM   13305 O  O     . LYS   B  1  575  ? 20.306  13.227  64.497  1.00 21.33 ? 573  LYS   B O     1 
ATOM   13306 C  CB    . LYS   B  1  575  ? 21.776  10.756  64.090  1.00 21.54 ? 573  LYS   B CB    1 
ATOM   13307 C  CG    . LYS   B  1  575  ? 22.969  11.446  63.461  1.00 26.94 ? 573  LYS   B CG    1 
ATOM   13308 C  CD    . LYS   B  1  575  ? 23.332  10.739  62.170  1.00 30.86 ? 573  LYS   B CD    1 
ATOM   13309 C  CE    . LYS   B  1  575  ? 24.628  11.258  61.570  1.00 40.70 ? 573  LYS   B CE    1 
ATOM   13310 N  NZ    . LYS   B  1  575  ? 24.417  12.526  60.822  1.00 40.74 ? 573  LYS   B NZ    1 
ATOM   13311 N  N     . TRP   B  1  576  ? 21.541  13.535  66.365  1.00 19.95 ? 574  TRP   B N     1 
ATOM   13312 C  CA    . TRP   B  1  576  ? 21.315  14.963  66.460  1.00 17.48 ? 574  TRP   B CA    1 
ATOM   13313 C  C     . TRP   B  1  576  ? 22.460  15.699  65.794  1.00 17.59 ? 574  TRP   B C     1 
ATOM   13314 O  O     . TRP   B  1  576  ? 23.628  15.506  66.143  1.00 19.07 ? 574  TRP   B O     1 
ATOM   13315 C  CB    . TRP   B  1  576  ? 21.237  15.402  67.919  1.00 16.18 ? 574  TRP   B CB    1 
ATOM   13316 C  CG    . TRP   B  1  576  ? 20.059  14.863  68.661  1.00 16.89 ? 574  TRP   B CG    1 
ATOM   13317 C  CD1   . TRP   B  1  576  ? 20.069  13.895  69.618  1.00 20.57 ? 574  TRP   B CD1   1 
ATOM   13318 C  CD2   . TRP   B  1  576  ? 18.704  15.252  68.488  1.00 16.44 ? 574  TRP   B CD2   1 
ATOM   13319 N  NE1   . TRP   B  1  576  ? 18.791  13.678  70.079  1.00 19.74 ? 574  TRP   B NE1   1 
ATOM   13320 C  CE2   . TRP   B  1  576  ? 17.933  14.498  69.395  1.00 19.36 ? 574  TRP   B CE2   1 
ATOM   13321 C  CE3   . TRP   B  1  576  ? 18.070  16.187  67.675  1.00 16.41 ? 574  TRP   B CE3   1 
ATOM   13322 C  CZ2   . TRP   B  1  576  ? 16.552  14.647  69.509  1.00 20.17 ? 574  TRP   B CZ2   1 
ATOM   13323 C  CZ3   . TRP   B  1  576  ? 16.692  16.339  67.784  1.00 17.24 ? 574  TRP   B CZ3   1 
ATOM   13324 C  CH2   . TRP   B  1  576  ? 15.950  15.569  68.695  1.00 19.43 ? 574  TRP   B CH2   1 
ATOM   13325 N  N     . THR   B  1  577  ? 22.116  16.554  64.853  1.00 18.93 ? 575  THR   B N     1 
ATOM   13326 C  CA    . THR   B  1  577  ? 23.105  17.318  64.123  1.00 17.25 ? 575  THR   B CA    1 
ATOM   13327 C  C     . THR   B  1  577  ? 22.654  18.763  64.082  1.00 17.09 ? 575  THR   B C     1 
ATOM   13328 O  O     . THR   B  1  577  ? 21.480  19.081  64.268  1.00 16.74 ? 575  THR   B O     1 
ATOM   13329 C  CB    . THR   B  1  577  ? 23.252  16.813  62.684  1.00 19.04 ? 575  THR   B CB    1 
ATOM   13330 O  OG1   . THR   B  1  577  ? 22.004  17.003  62.007  1.00 22.68 ? 575  THR   B OG1   1 
ATOM   13331 C  CG2   . THR   B  1  577  ? 23.619  15.343  62.673  1.00 19.91 ? 575  THR   B CG2   1 
ATOM   13332 N  N     . ALA   B  1  578  ? 23.607  19.645  63.831  1.00 16.80 ? 576  ALA   B N     1 
ATOM   13333 C  CA    . ALA   B  1  578  ? 23.311  21.042  63.573  1.00 16.76 ? 576  ALA   B CA    1 
ATOM   13334 C  C     . ALA   B  1  578  ? 24.250  21.453  62.461  1.00 15.31 ? 576  ALA   B C     1 
ATOM   13335 O  O     . ALA   B  1  578  ? 25.460  21.256  62.585  1.00 17.32 ? 576  ALA   B O     1 
ATOM   13336 C  CB    . ALA   B  1  578  ? 23.568  21.882  64.824  1.00 15.39 ? 576  ALA   B CB    1 
ATOM   13337 N  N     . LEU   B  1  579  ? 23.699  21.969  61.372  1.00 16.01 ? 577  LEU   B N     1 
ATOM   13338 C  CA    . LEU   B  1  579  ? 24.468  22.295  60.184  1.00 15.89 ? 577  LEU   B CA    1 
ATOM   13339 C  C     . LEU   B  1  579  ? 24.215  23.745  59.817  1.00 15.78 ? 577  LEU   B C     1 
ATOM   13340 O  O     . LEU   B  1  579  ? 23.192  24.323  60.194  1.00 15.49 ? 577  LEU   B O     1 
ATOM   13341 C  CB    . LEU   B  1  579  ? 24.004  21.422  59.002  1.00 19.89 ? 577  LEU   B CB    1 
ATOM   13342 C  CG    . LEU   B  1  579  ? 23.830  19.933  59.276  1.00 23.97 ? 577  LEU   B CG    1 
ATOM   13343 C  CD1   . LEU   B  1  579  ? 23.245  19.178  58.066  1.00 24.26 ? 577  LEU   B CD1   1 
ATOM   13344 C  CD2   . LEU   B  1  579  ? 25.182  19.405  59.636  1.00 22.01 ? 577  LEU   B CD2   1 
ATOM   13345 N  N     . PRO   B  1  580  ? 25.103  24.347  59.034  1.00 16.47 ? 578  PRO   B N     1 
ATOM   13346 C  CA    . PRO   B  1  580  ? 24.757  25.635  58.428  1.00 15.56 ? 578  PRO   B CA    1 
ATOM   13347 C  C     . PRO   B  1  580  ? 23.667  25.410  57.403  1.00 14.92 ? 578  PRO   B C     1 
ATOM   13348 O  O     . PRO   B  1  580  ? 23.935  24.879  56.323  1.00 18.24 ? 578  PRO   B O     1 
ATOM   13349 C  CB    . PRO   B  1  580  ? 26.078  26.111  57.802  1.00 17.66 ? 578  PRO   B CB    1 
ATOM   13350 C  CG    . PRO   B  1  580  ? 27.152  25.201  58.406  1.00 18.82 ? 578  PRO   B CG    1 
ATOM   13351 C  CD    . PRO   B  1  580  ? 26.447  23.900  58.634  1.00 16.36 ? 578  PRO   B CD    1 
ATOM   13352 N  N     . GLN   B  1  581  ? 22.442  25.741  57.758  1.00 15.53 ? 579  GLN   B N     1 
ATOM   13353 C  CA    . GLN   B  1  581  ? 21.274  25.495  56.917  1.00 16.19 ? 579  GLN   B CA    1 
ATOM   13354 C  C     . GLN   B  1  581  ? 20.985  26.782  56.173  1.00 18.37 ? 579  GLN   B C     1 
ATOM   13355 O  O     . GLN   B  1  581  ? 20.282  27.664  56.666  1.00 17.89 ? 579  GLN   B O     1 
ATOM   13356 C  CB    . GLN   B  1  581  ? 20.095  25.083  57.773  1.00 16.74 ? 579  GLN   B CB    1 
ATOM   13357 C  CG    . GLN   B  1  581  ? 20.321  23.796  58.485  1.00 17.56 ? 579  GLN   B CG    1 
ATOM   13358 C  CD    . GLN   B  1  581  ? 20.280  22.590  57.569  1.00 20.48 ? 579  GLN   B CD    1 
ATOM   13359 O  OE1   . GLN   B  1  581  ? 20.058  22.705  56.346  1.00 21.62 ? 579  GLN   B OE1   1 
ATOM   13360 N  NE2   . GLN   B  1  581  ? 20.478  21.414  58.150  1.00 27.92 ? 579  GLN   B NE2   1 
ATOM   13361 N  N     . LEU   B  1  582  ? 21.561  26.902  54.987  1.00 17.04 ? 580  LEU   B N     1 
ATOM   13362 C  CA    . LEU   B  1  582  ? 21.314  28.056  54.148  1.00 17.23 ? 580  LEU   B CA    1 
ATOM   13363 C  C     . LEU   B  1  582  ? 20.065  27.808  53.300  1.00 17.60 ? 580  LEU   B C     1 
ATOM   13364 O  O     . LEU   B  1  582  ? 19.508  26.706  53.271  1.00 19.79 ? 580  LEU   B O     1 
ATOM   13365 C  CB    . LEU   B  1  582  ? 22.542  28.363  53.284  1.00 19.64 ? 580  LEU   B CB    1 
ATOM   13366 C  CG    . LEU   B  1  582  ? 23.622  29.208  54.000  1.00 22.69 ? 580  LEU   B CG    1 
ATOM   13367 C  CD1   . LEU   B  1  582  ? 24.295  28.494  55.178  1.00 21.93 ? 580  LEU   B CD1   1 
ATOM   13368 C  CD2   . LEU   B  1  582  ? 24.659  29.694  53.012  1.00 27.53 ? 580  LEU   B CD2   1 
ATOM   13369 N  N     . ALA   B  1  583  ? 19.601  28.867  52.639  1.00 18.68 ? 581  ALA   B N     1 
ATOM   13370 C  CA    . ALA   B  1  583  ? 18.383  28.761  51.845  1.00 21.88 ? 581  ALA   B CA    1 
ATOM   13371 C  C     . ALA   B  1  583  ? 18.505  27.678  50.792  1.00 24.55 ? 581  ALA   B C     1 
ATOM   13372 O  O     . ALA   B  1  583  ? 17.517  27.005  50.477  1.00 25.97 ? 581  ALA   B O     1 
ATOM   13373 C  CB    . ALA   B  1  583  ? 18.078  30.104  51.192  1.00 23.13 ? 581  ALA   B CB    1 
ATOM   13374 N  N     . THR   B  1  584  ? 19.712  27.468  50.281  1.00 20.60 ? 582  THR   B N     1 
ATOM   13375 C  CA    . THR   B  1  584  ? 19.987  26.527  49.206  1.00 22.58 ? 582  THR   B CA    1 
ATOM   13376 C  C     . THR   B  1  584  ? 20.344  25.138  49.712  1.00 20.20 ? 582  THR   B C     1 
ATOM   13377 O  O     . THR   B  1  584  ? 20.641  24.254  48.905  1.00 20.90 ? 582  THR   B O     1 
ATOM   13378 C  CB    . THR   B  1  584  ? 21.130  27.072  48.354  1.00 24.40 ? 582  THR   B CB    1 
ATOM   13379 O  OG1   . THR   B  1  584  ? 22.213  27.457  49.216  1.00 26.02 ? 582  THR   B OG1   1 
ATOM   13380 C  CG2   . THR   B  1  584  ? 20.660  28.278  47.573  1.00 31.68 ? 582  THR   B CG2   1 
ATOM   13381 N  N     . GLY   B  1  585  ? 20.330  24.924  51.021  1.00 21.37 ? 583  GLY   B N     1 
ATOM   13382 C  CA    . GLY   B  1  585  ? 20.629  23.631  51.586  1.00 18.54 ? 583  GLY   B CA    1 
ATOM   13383 C  C     . GLY   B  1  585  ? 21.759  23.746  52.585  1.00 19.93 ? 583  GLY   B C     1 
ATOM   13384 O  O     . GLY   B  1  585  ? 22.324  24.825  52.787  1.00 20.72 ? 583  GLY   B O     1 
ATOM   13385 N  N     . PRO   B  1  586  ? 22.101  22.639  53.237  1.00 18.56 ? 584  PRO   B N     1 
ATOM   13386 C  CA    . PRO   B  1  586  ? 23.184  22.680  54.222  1.00 17.42 ? 584  PRO   B CA    1 
ATOM   13387 C  C     . PRO   B  1  586  ? 24.534  22.859  53.572  1.00 21.26 ? 584  PRO   B C     1 
ATOM   13388 O  O     . PRO   B  1  586  ? 24.825  22.283  52.520  1.00 20.78 ? 584  PRO   B O     1 
ATOM   13389 C  CB    . PRO   B  1  586  ? 23.084  21.321  54.917  1.00 21.93 ? 584  PRO   B CB    1 
ATOM   13390 C  CG    . PRO   B  1  586  ? 22.502  20.439  53.888  1.00 23.83 ? 584  PRO   B CG    1 
ATOM   13391 C  CD    . PRO   B  1  586  ? 21.470  21.312  53.204  1.00 21.54 ? 584  PRO   B CD    1 
ATOM   13392 N  N     . ALA   B  1  587  ? 25.372  23.642  54.224  1.00 18.50 ? 585  ALA   B N     1 
ATOM   13393 C  CA    . ALA   B  1  587  ? 26.707  23.921  53.735  1.00 18.77 ? 585  ALA   B CA    1 
ATOM   13394 C  C     . ALA   B  1  587  ? 27.715  23.082  54.497  1.00 19.53 ? 585  ALA   B C     1 
ATOM   13395 O  O     . ALA   B  1  587  ? 27.488  22.668  55.633  1.00 19.78 ? 585  ALA   B O     1 
ATOM   13396 C  CB    . ALA   B  1  587  ? 27.020  25.408  53.906  1.00 20.89 ? 585  ALA   B CB    1 
ATOM   13397 N  N     . ALA   B  1  588  ? 28.843  22.832  53.839  1.00 20.86 ? 586  ALA   B N     1 
ATOM   13398 C  CA    . ALA   B  1  588  ? 29.948  22.158  54.495  1.00 19.16 ? 586  ALA   B CA    1 
ATOM   13399 C  C     . ALA   B  1  588  ? 30.619  23.095  55.492  1.00 20.42 ? 586  ALA   B C     1 
ATOM   13400 O  O     . ALA   B  1  588  ? 30.573  24.323  55.367  1.00 22.54 ? 586  ALA   B O     1 
ATOM   13401 C  CB    . ALA   B  1  588  ? 30.988  21.719  53.467  1.00 19.54 ? 586  ALA   B CB    1 
ATOM   13402 N  N     . GLY   B  1  589  ? 31.279  22.501  56.476  1.00 19.57 ? 587  GLY   B N     1 
ATOM   13403 C  CA    . GLY   B  1  589  ? 32.030  23.299  57.425  1.00 20.88 ? 587  GLY   B CA    1 
ATOM   13404 C  C     . GLY   B  1  589  ? 32.805  22.412  58.370  1.00 22.18 ? 587  GLY   B C     1 
ATOM   13405 O  O     . GLY   B  1  589  ? 32.846  21.190  58.209  1.00 23.79 ? 587  GLY   B O     1 
ATOM   13406 N  N     . GLU   B  1  590  ? 33.423  23.047  59.369  1.00 21.27 ? 588  GLU   B N     1 
ATOM   13407 C  CA    . GLU   B  1  590  ? 34.178  22.310  60.373  1.00 23.00 ? 588  GLU   B CA    1 
ATOM   13408 C  C     . GLU   B  1  590  ? 33.219  21.669  61.365  1.00 20.64 ? 588  GLU   B C     1 
ATOM   13409 O  O     . GLU   B  1  590  ? 32.353  22.338  61.936  1.00 20.23 ? 588  GLU   B O     1 
ATOM   13410 C  CB    . GLU   B  1  590  ? 35.122  23.244  61.126  1.00 24.92 ? 588  GLU   B CB    1 
ATOM   13411 C  CG    . GLU   B  1  590  ? 36.217  23.842  60.267  1.00 34.54 ? 588  GLU   B CG    1 
ATOM   13412 C  CD    . GLU   B  1  590  ? 37.133  22.784  59.687  1.00 42.08 ? 588  GLU   B CD    1 
ATOM   13413 O  OE1   . GLU   B  1  590  ? 37.484  21.830  60.416  1.00 45.54 ? 588  GLU   B OE1   1 
ATOM   13414 O  OE2   . GLU   B  1  590  ? 37.490  22.900  58.496  1.00 52.04 ? 588  GLU   B OE2   1 
ATOM   13415 N  N     . THR   B  1  591  ? 33.388  20.376  61.588  1.00 20.82 ? 589  THR   B N     1 
ATOM   13416 C  CA    . THR   B  1  591  ? 32.460  19.599  62.393  1.00 21.30 ? 589  THR   B CA    1 
ATOM   13417 C  C     . THR   B  1  591  ? 33.130  19.142  63.680  1.00 20.15 ? 589  THR   B C     1 
ATOM   13418 O  O     . THR   B  1  591  ? 34.308  18.760  63.685  1.00 23.05 ? 589  THR   B O     1 
ATOM   13419 C  CB    . THR   B  1  591  ? 31.982  18.394  61.590  1.00 22.88 ? 589  THR   B CB    1 
ATOM   13420 O  OG1   . THR   B  1  591  ? 31.358  18.861  60.388  1.00 23.36 ? 589  THR   B OG1   1 
ATOM   13421 C  CG2   . THR   B  1  591  ? 30.977  17.584  62.384  1.00 23.32 ? 589  THR   B CG2   1 
ATOM   13422 N  N     . ARG   B  1  592  ? 32.381  19.205  64.773  1.00 20.36 ? 590  ARG   B N     1 
ATOM   13423 C  CA    . ARG   B  1  592  ? 32.868  18.689  66.037  1.00 23.66 ? 590  ARG   B CA    1 
ATOM   13424 C  C     . ARG   B  1  592  ? 31.709  18.078  66.804  1.00 21.34 ? 590  ARG   B C     1 
ATOM   13425 O  O     . ARG   B  1  592  ? 30.534  18.303  66.496  1.00 20.03 ? 590  ARG   B O     1 
ATOM   13426 C  CB    . ARG   B  1  592  ? 33.532  19.787  66.869  1.00 23.64 ? 590  ARG   B CB    1 
ATOM   13427 C  CG    . ARG   B  1  592  ? 32.580  20.877  67.272  1.00 24.04 ? 590  ARG   B CG    1 
ATOM   13428 C  CD    . ARG   B  1  592  ? 33.152  21.708  68.390  1.00 32.09 ? 590  ARG   B CD    1 
ATOM   13429 N  NE    . ARG   B  1  592  ? 32.308  22.865  68.656  1.00 29.11 ? 590  ARG   B NE    1 
ATOM   13430 C  CZ    . ARG   B  1  592  ? 31.290  22.867  69.502  1.00 28.41 ? 590  ARG   B CZ    1 
ATOM   13431 N  NH1   . ARG   B  1  592  ? 30.945  21.777  70.173  1.00 27.63 ? 590  ARG   B NH1   1 
ATOM   13432 N  NH2   . ARG   B  1  592  ? 30.603  23.992  69.680  1.00 28.79 ? 590  ARG   B NH2   1 
ATOM   13433 N  N     . THR   B  1  593  ? 32.050  17.300  67.821  1.00 23.36 ? 591  THR   B N     1 
ATOM   13434 C  CA    . THR   B  1  593  ? 31.029  16.697  68.647  1.00 21.22 ? 591  THR   B CA    1 
ATOM   13435 C  C     . THR   B  1  593  ? 30.520  17.698  69.669  1.00 20.28 ? 591  THR   B C     1 
ATOM   13436 O  O     . THR   B  1  593  ? 31.185  18.675  70.026  1.00 21.73 ? 591  THR   B O     1 
ATOM   13437 C  CB    . THR   B  1  593  ? 31.587  15.489  69.388  1.00 22.76 ? 591  THR   B CB    1 
ATOM   13438 O  OG1   . THR   B  1  593  ? 32.713  15.908  70.164  1.00 27.77 ? 591  THR   B OG1   1 
ATOM   13439 C  CG2   . THR   B  1  593  ? 32.011  14.418  68.398  1.00 31.46 ? 591  THR   B CG2   1 
ATOM   13440 N  N     . VAL   B  1  594  ? 29.299  17.450  70.110  1.00 18.81 ? 592  VAL   B N     1 
ATOM   13441 C  CA    . VAL   B  1  594  ? 28.661  18.180  71.191  1.00 17.50 ? 592  VAL   B CA    1 
ATOM   13442 C  C     . VAL   B  1  594  ? 28.540  17.188  72.331  1.00 20.37 ? 592  VAL   B C     1 
ATOM   13443 O  O     . VAL   B  1  594  ? 27.956  16.113  72.156  1.00 20.55 ? 592  VAL   B O     1 
ATOM   13444 C  CB    . VAL   B  1  594  ? 27.283  18.687  70.745  1.00 18.66 ? 592  VAL   B CB    1 
ATOM   13445 C  CG1   . VAL   B  1  594  ? 26.576  19.417  71.868  1.00 19.59 ? 592  VAL   B CG1   1 
ATOM   13446 C  CG2   . VAL   B  1  594  ? 27.442  19.588  69.523  1.00 21.40 ? 592  VAL   B CG2   1 
ATOM   13447 N  N     . LEU   B  1  595  ? 29.143  17.514  73.476  1.00 19.39 ? 593  LEU   B N     1 
ATOM   13448 C  CA    . LEU   B  1  595  ? 29.226  16.607  74.611  1.00 19.54 ? 593  LEU   B CA    1 
ATOM   13449 C  C     . LEU   B  1  595  ? 28.332  17.096  75.738  1.00 18.80 ? 593  LEU   B C     1 
ATOM   13450 O  O     . LEU   B  1  595  ? 28.139  18.299  75.927  1.00 21.49 ? 593  LEU   B O     1 
ATOM   13451 C  CB    . LEU   B  1  595  ? 30.659  16.521  75.133  1.00 19.53 ? 593  LEU   B CB    1 
ATOM   13452 C  CG    . LEU   B  1  595  ? 31.688  16.117  74.089  1.00 20.24 ? 593  LEU   B CG    1 
ATOM   13453 C  CD1   . LEU   B  1  595  ? 33.064  16.106  74.740  1.00 22.57 ? 593  LEU   B CD1   1 
ATOM   13454 C  CD2   . LEU   B  1  595  ? 31.367  14.761  73.453  1.00 22.06 ? 593  LEU   B CD2   1 
ATOM   13455 N  N     . ASN   B  1  596  ? 27.803  16.150  76.490  1.00 17.39 ? 594  ASN   B N     1 
ATOM   13456 C  CA    . ASN   B  1  596  ? 26.965  16.473  77.634  1.00 16.49 ? 594  ASN   B CA    1 
ATOM   13457 C  C     . ASN   B  1  596  ? 27.829  17.186  78.666  1.00 16.71 ? 594  ASN   B C     1 
ATOM   13458 O  O     . ASN   B  1  596  ? 28.845  16.628  79.099  1.00 16.55 ? 594  ASN   B O     1 
ATOM   13459 C  CB    . ASN   B  1  596  ? 26.453  15.147  78.197  1.00 15.91 ? 594  ASN   B CB    1 
ATOM   13460 C  CG    . ASN   B  1  596  ? 25.435  15.318  79.289  1.00 16.94 ? 594  ASN   B CG    1 
ATOM   13461 O  OD1   . ASN   B  1  596  ? 25.473  16.277  80.062  1.00 17.88 ? 594  ASN   B OD1   1 
ATOM   13462 N  ND2   . ASN   B  1  596  ? 24.512  14.369  79.376  1.00 20.30 ? 594  ASN   B ND2   1 
ATOM   13463 N  N     . PRO   B  1  597  ? 27.492  18.408  79.072  1.00 15.21 ? 595  PRO   B N     1 
ATOM   13464 C  CA    . PRO   B  1  597  ? 28.330  19.096  80.068  1.00 16.66 ? 595  PRO   B CA    1 
ATOM   13465 C  C     . PRO   B  1  597  ? 28.404  18.372  81.390  1.00 16.84 ? 595  PRO   B C     1 
ATOM   13466 O  O     . PRO   B  1  597  ? 29.364  18.582  82.137  1.00 16.72 ? 595  PRO   B O     1 
ATOM   13467 C  CB    . PRO   B  1  597  ? 27.668  20.476  80.216  1.00 16.98 ? 595  PRO   B CB    1 
ATOM   13468 C  CG    . PRO   B  1  597  ? 26.222  20.251  79.753  1.00 16.25 ? 595  PRO   B CG    1 
ATOM   13469 C  CD    . PRO   B  1  597  ? 26.347  19.230  78.641  1.00 15.80 ? 595  PRO   B CD    1 
ATOM   13470 N  N     . GLY   B  1  598  ? 27.426  17.529  81.710  1.00 16.77 ? 596  GLY   B N     1 
ATOM   13471 C  CA    . GLY   B  1  598  ? 27.499  16.785  82.948  1.00 16.65 ? 596  GLY   B CA    1 
ATOM   13472 C  C     . GLY   B  1  598  ? 28.250  15.492  82.855  1.00 16.78 ? 596  GLY   B C     1 
ATOM   13473 O  O     . GLY   B  1  598  ? 28.506  14.851  83.879  1.00 19.62 ? 596  GLY   B O     1 
ATOM   13474 N  N     . ASP   B  1  599  ? 28.639  15.089  81.653  1.00 17.44 ? 597  ASP   B N     1 
ATOM   13475 C  CA    . ASP   B  1  599  ? 29.407  13.869  81.459  1.00 18.12 ? 597  ASP   B CA    1 
ATOM   13476 C  C     . ASP   B  1  599  ? 29.935  13.887  80.038  1.00 18.42 ? 597  ASP   B C     1 
ATOM   13477 O  O     . ASP   B  1  599  ? 29.215  13.542  79.092  1.00 18.78 ? 597  ASP   B O     1 
ATOM   13478 C  CB    . ASP   B  1  599  ? 28.527  12.643  81.675  1.00 18.28 ? 597  ASP   B CB    1 
ATOM   13479 C  CG    . ASP   B  1  599  ? 29.308  11.356  81.681  1.00 20.58 ? 597  ASP   B CG    1 
ATOM   13480 O  OD1   . ASP   B  1  599  ? 30.467  11.337  81.201  1.00 21.00 ? 597  ASP   B OD1   1 
ATOM   13481 O  OD2   . ASP   B  1  599  ? 28.747  10.363  82.185  1.00 22.89 ? 597  ASP   B OD2   1 
ATOM   13482 N  N     . HIS   B  1  600  ? 31.196  14.282  79.880  1.00 17.86 ? 598  HIS   B N     1 
ATOM   13483 C  CA    . HIS   B  1  600  ? 31.734  14.418  78.538  1.00 18.39 ? 598  HIS   B CA    1 
ATOM   13484 C  C     . HIS   B  1  600  ? 31.828  13.094  77.796  1.00 18.94 ? 598  HIS   B C     1 
ATOM   13485 O  O     . HIS   B  1  600  ? 32.056  13.110  76.588  1.00 23.24 ? 598  HIS   B O     1 
ATOM   13486 C  CB    . HIS   B  1  600  ? 33.087  15.132  78.559  1.00 22.00 ? 598  HIS   B CB    1 
ATOM   13487 C  CG    . HIS   B  1  600  ? 32.991  16.583  78.907  1.00 21.05 ? 598  HIS   B CG    1 
ATOM   13488 N  ND1   . HIS   B  1  600  ? 34.100  17.387  79.064  1.00 26.31 ? 598  HIS   B ND1   1 
ATOM   13489 C  CD2   . HIS   B  1  600  ? 31.916  17.375  79.126  1.00 19.53 ? 598  HIS   B CD2   1 
ATOM   13490 C  CE1   . HIS   B  1  600  ? 33.712  18.612  79.375  1.00 28.40 ? 598  HIS   B CE1   1 
ATOM   13491 N  NE2   . HIS   B  1  600  ? 32.390  18.634  79.413  1.00 23.10 ? 598  HIS   B NE2   1 
ATOM   13492 N  N     . ARG   B  1  601  ? 31.655  11.956  78.474  1.00 19.31 ? 599  ARG   B N     1 
ATOM   13493 C  CA    . ARG   B  1  601  ? 31.611  10.686  77.765  1.00 20.77 ? 599  ARG   B CA    1 
ATOM   13494 C  C     . ARG   B  1  601  ? 30.332  10.533  76.959  1.00 19.60 ? 599  ARG   B C     1 
ATOM   13495 O  O     . ARG   B  1  601  ? 30.283  9.698   76.051  1.00 23.35 ? 599  ARG   B O     1 
ATOM   13496 C  CB    . ARG   B  1  601  ? 31.735  9.536   78.755  1.00 24.07 ? 599  ARG   B CB    1 
ATOM   13497 C  CG    . ARG   B  1  601  ? 33.018  9.586   79.559  1.00 25.13 ? 599  ARG   B CG    1 
ATOM   13498 C  CD    . ARG   B  1  601  ? 32.963  8.612   80.707  1.00 26.00 ? 599  ARG   B CD    1 
ATOM   13499 N  NE    . ARG   B  1  601  ? 31.875  8.918   81.623  1.00 26.40 ? 599  ARG   B NE    1 
ATOM   13500 C  CZ    . ARG   B  1  601  ? 31.553  8.172   82.668  1.00 28.39 ? 599  ARG   B CZ    1 
ATOM   13501 N  NH1   . ARG   B  1  601  ? 32.245  7.084   82.979  1.00 31.15 ? 599  ARG   B NH1   1 
ATOM   13502 N  NH2   . ARG   B  1  601  ? 30.511  8.520   83.417  1.00 27.67 ? 599  ARG   B NH2   1 
ATOM   13503 N  N     . ASP   B  1  602  ? 29.299  11.315  77.279  1.00 18.69 ? 600  ASP   B N     1 
ATOM   13504 C  CA    . ASP   B  1  602  ? 27.989  11.196  76.651  1.00 20.05 ? 600  ASP   B CA    1 
ATOM   13505 C  C     . ASP   B  1  602  ? 27.981  12.151  75.464  1.00 20.69 ? 600  ASP   B C     1 
ATOM   13506 O  O     . ASP   B  1  602  ? 27.868  13.367  75.627  1.00 20.24 ? 600  ASP   B O     1 
ATOM   13507 C  CB    . ASP   B  1  602  ? 26.902  11.518  77.670  1.00 20.16 ? 600  ASP   B CB    1 
ATOM   13508 C  CG    . ASP   B  1  602  ? 25.518  11.459  77.074  1.00 23.18 ? 600  ASP   B CG    1 
ATOM   13509 O  OD1   . ASP   B  1  602  ? 25.349  10.764  76.043  1.00 23.51 ? 600  ASP   B OD1   1 
ATOM   13510 O  OD2   . ASP   B  1  602  ? 24.612  12.119  77.632  1.00 23.05 ? 600  ASP   B OD2   1 
ATOM   13511 N  N     . VAL   B  1  603  ? 28.150  11.599  74.268  1.00 20.28 ? 601  VAL   B N     1 
ATOM   13512 C  CA    . VAL   B  1  603  ? 28.148  12.384  73.040  1.00 18.62 ? 601  VAL   B CA    1 
ATOM   13513 C  C     . VAL   B  1  603  ? 26.701  12.629  72.643  1.00 19.84 ? 601  VAL   B C     1 
ATOM   13514 O  O     . VAL   B  1  603  ? 25.938  11.685  72.407  1.00 23.24 ? 601  VAL   B O     1 
ATOM   13515 C  CB    . VAL   B  1  603  ? 28.908  11.656  71.924  1.00 20.85 ? 601  VAL   B CB    1 
ATOM   13516 C  CG1   . VAL   B  1  603  ? 28.843  12.465  70.629  1.00 22.57 ? 601  VAL   B CG1   1 
ATOM   13517 C  CG2   . VAL   B  1  603  ? 30.359  11.385  72.349  1.00 23.46 ? 601  VAL   B CG2   1 
ATOM   13518 N  N     . VAL   B  1  604  ? 26.317  13.897  72.595  1.00 17.43 ? 602  VAL   B N     1 
ATOM   13519 C  CA    . VAL   B  1  604  ? 24.940  14.237  72.287  1.00 16.00 ? 602  VAL   B CA    1 
ATOM   13520 C  C     . VAL   B  1  604  ? 24.715  14.323  70.790  1.00 17.15 ? 602  VAL   B C     1 
ATOM   13521 O  O     . VAL   B  1  604  ? 23.688  13.866  70.291  1.00 18.68 ? 602  VAL   B O     1 
ATOM   13522 C  CB    . VAL   B  1  604  ? 24.555  15.538  72.997  1.00 16.60 ? 602  VAL   B CB    1 
ATOM   13523 C  CG1   . VAL   B  1  604  ? 23.080  15.795  72.815  1.00 17.84 ? 602  VAL   B CG1   1 
ATOM   13524 C  CG2   . VAL   B  1  604  ? 24.903  15.433  74.486  1.00 18.65 ? 602  VAL   B CG2   1 
ATOM   13525 N  N     . GLY   B  1  605  ? 25.672  14.863  70.052  1.00 17.16 ? 603  GLY   B N     1 
ATOM   13526 C  CA    . GLY   B  1  605  ? 25.478  15.025  68.630  1.00 18.09 ? 603  GLY   B CA    1 
ATOM   13527 C  C     . GLY   B  1  605  ? 26.681  15.689  68.027  1.00 17.75 ? 603  GLY   B C     1 
ATOM   13528 O  O     . GLY   B  1  605  ? 27.758  15.683  68.616  1.00 18.34 ? 603  GLY   B O     1 
ATOM   13529 N  N     . SER   B  1  606  ? 26.492  16.252  66.845  1.00 17.60 ? 604  SER   B N     1 
ATOM   13530 C  CA    A SER   B  1  606  ? 27.590  16.873  66.128  0.43 19.19 ? 604  SER   B CA    1 
ATOM   13531 C  CA    B SER   B  1  606  ? 27.584  16.858  66.100  0.57 19.16 ? 604  SER   B CA    1 
ATOM   13532 C  C     . SER   B  1  606  ? 27.111  18.173  65.516  1.00 18.76 ? 604  SER   B C     1 
ATOM   13533 O  O     . SER   B  1  606  ? 25.957  18.287  65.080  1.00 19.84 ? 604  SER   B O     1 
ATOM   13534 C  CB    A SER   B  1  606  ? 28.134  15.959  65.031  0.43 25.36 ? 604  SER   B CB    1 
ATOM   13535 C  CB    B SER   B  1  606  ? 28.055  15.944  64.964  0.57 25.37 ? 604  SER   B CB    1 
ATOM   13536 O  OG    A SER   B  1  606  ? 27.154  15.728  64.043  0.43 24.32 ? 604  SER   B OG    1 
ATOM   13537 O  OG    B SER   B  1  606  ? 28.640  14.761  65.478  0.57 33.06 ? 604  SER   B OG    1 
ATOM   13538 N  N     . VAL   B  1  607  ? 28.004  19.149  65.486  1.00 17.02 ? 605  VAL   B N     1 
ATOM   13539 C  CA    . VAL   B  1  607  ? 27.710  20.449  64.921  1.00 15.41 ? 605  VAL   B CA    1 
ATOM   13540 C  C     . VAL   B  1  607  ? 28.714  20.734  63.821  1.00 17.88 ? 605  VAL   B C     1 
ATOM   13541 O  O     . VAL   B  1  607  ? 29.926  20.526  63.990  1.00 17.64 ? 605  VAL   B O     1 
ATOM   13542 C  CB    . VAL   B  1  607  ? 27.697  21.562  65.986  1.00 16.28 ? 605  VAL   B CB    1 
ATOM   13543 C  CG1   . VAL   B  1  607  ? 29.022  21.645  66.742  1.00 18.32 ? 605  VAL   B CG1   1 
ATOM   13544 C  CG2   . VAL   B  1  607  ? 27.359  22.885  65.336  1.00 17.05 ? 605  VAL   B CG2   1 
ATOM   13545 N  N     . THR   B  1  608  ? 28.210  21.181  62.690  1.00 16.24 ? 606  THR   B N     1 
ATOM   13546 C  CA    . THR   B  1  608  ? 29.033  21.692  61.618  1.00 17.32 ? 606  THR   B CA    1 
ATOM   13547 C  C     . THR   B  1  608  ? 28.914  23.207  61.647  1.00 16.20 ? 606  THR   B C     1 
ATOM   13548 O  O     . THR   B  1  608  ? 27.813  23.754  61.543  1.00 17.95 ? 606  THR   B O     1 
ATOM   13549 C  CB    . THR   B  1  608  ? 28.554  21.116  60.290  1.00 18.54 ? 606  THR   B CB    1 
ATOM   13550 O  OG1   . THR   B  1  608  ? 28.690  19.692  60.333  1.00 19.49 ? 606  THR   B OG1   1 
ATOM   13551 C  CG2   . THR   B  1  608  ? 29.382  21.661  59.140  1.00 18.66 ? 606  THR   B CG2   1 
ATOM   13552 N  N     . GLU   B  1  609  ? 30.031  23.880  61.843  1.00 17.22 ? 607  GLU   B N     1 
ATOM   13553 C  CA    . GLU   B  1  609  ? 29.967  25.309  62.043  1.00 18.72 ? 607  GLU   B CA    1 
ATOM   13554 C  C     . GLU   B  1  609  ? 30.158  26.056  60.728  1.00 17.21 ? 607  GLU   B C     1 
ATOM   13555 O  O     . GLU   B  1  609  ? 30.687  25.526  59.750  1.00 18.94 ? 607  GLU   B O     1 
ATOM   13556 C  CB    . GLU   B  1  609  ? 30.940  25.736  63.141  1.00 20.92 ? 607  GLU   B CB    1 
ATOM   13557 C  CG    . GLU   B  1  609  ? 30.466  25.192  64.493  1.00 23.82 ? 607  GLU   B CG    1 
ATOM   13558 C  CD    . GLU   B  1  609  ? 31.344  25.592  65.660  1.00 27.11 ? 607  GLU   B CD    1 
ATOM   13559 O  OE1   . GLU   B  1  609  ? 32.551  25.820  65.443  1.00 34.36 ? 607  GLU   B OE1   1 
ATOM   13560 O  OE2   . GLU   B  1  609  ? 30.824  25.686  66.796  1.00 25.37 ? 607  GLU   B OE2   1 
ATOM   13561 N  N     . THR   B  1  610  ? 29.689  27.293  60.718  1.00 17.17 ? 608  THR   B N     1 
ATOM   13562 C  CA    . THR   B  1  610  ? 29.514  28.074  59.505  1.00 15.88 ? 608  THR   B CA    1 
ATOM   13563 C  C     . THR   B  1  610  ? 30.781  28.860  59.225  1.00 17.83 ? 608  THR   B C     1 
ATOM   13564 O  O     . THR   B  1  610  ? 31.316  29.514  60.122  1.00 19.47 ? 608  THR   B O     1 
ATOM   13565 C  CB    . THR   B  1  610  ? 28.372  29.064  59.734  1.00 17.91 ? 608  THR   B CB    1 
ATOM   13566 O  OG1   . THR   B  1  610  ? 27.201  28.370  60.192  1.00 17.26 ? 608  THR   B OG1   1 
ATOM   13567 C  CG2   . THR   B  1  610  ? 28.037  29.772  58.434  1.00 18.52 ? 608  THR   B CG2   1 
ATOM   13568 N  N     . SER   B  1  611  ? 31.252  28.816  57.985  1.00 17.54 ? 609  SER   B N     1 
ATOM   13569 C  CA    . SER   B  1  611  ? 32.343  29.705  57.608  1.00 18.79 ? 609  SER   B CA    1 
ATOM   13570 C  C     . SER   B  1  611  ? 31.844  31.141  57.528  1.00 22.40 ? 609  SER   B C     1 
ATOM   13571 O  O     . SER   B  1  611  ? 30.659  31.399  57.302  1.00 18.80 ? 609  SER   B O     1 
ATOM   13572 C  CB    . SER   B  1  611  ? 32.904  29.303  56.248  1.00 20.42 ? 609  SER   B CB    1 
ATOM   13573 O  OG    . SER   B  1  611  ? 31.994  29.627  55.220  1.00 20.94 ? 609  SER   B OG    1 
ATOM   13574 N  N     . GLU   B  1  612  ? 32.757  32.095  57.724  1.00 21.73 ? 610  GLU   B N     1 
ATOM   13575 C  CA    . GLU   B  1  612  ? 32.354  33.489  57.602  1.00 22.50 ? 610  GLU   B CA    1 
ATOM   13576 C  C     . GLU   B  1  612  ? 31.859  33.801  56.194  1.00 23.20 ? 610  GLU   B C     1 
ATOM   13577 O  O     . GLU   B  1  612  ? 30.916  34.588  56.027  1.00 23.47 ? 610  GLU   B O     1 
ATOM   13578 C  CB    . GLU   B  1  612  ? 33.476  34.418  58.081  1.00 26.29 ? 610  GLU   B CB    1 
ATOM   13579 C  CG    . GLU   B  1  612  ? 33.816  34.169  59.558  1.00 27.45 ? 610  GLU   B CG    1 
ATOM   13580 C  CD    . GLU   B  1  612  ? 34.968  35.015  60.079  1.00 38.73 ? 610  GLU   B CD    1 
ATOM   13581 O  OE1   . GLU   B  1  612  ? 35.131  36.163  59.615  1.00 45.70 ? 610  GLU   B OE1   1 
ATOM   13582 O  OE2   . GLU   B  1  612  ? 35.706  34.529  60.963  1.00 41.06 ? 610  GLU   B OE2   1 
ATOM   13583 N  N     . GLU   B  1  613  ? 32.432  33.149  55.181  1.00 21.66 ? 611  GLU   B N     1 
ATOM   13584 C  CA    . GLU   B  1  613  ? 31.930  33.321  53.824  1.00 21.90 ? 611  GLU   B CA    1 
ATOM   13585 C  C     . GLU   B  1  613  ? 30.486  32.848  53.704  1.00 21.71 ? 611  GLU   B C     1 
ATOM   13586 O  O     . GLU   B  1  613  ? 29.662  33.510  53.067  1.00 22.13 ? 611  GLU   B O     1 
ATOM   13587 C  CB    . GLU   B  1  613  ? 32.830  32.578  52.836  1.00 27.70 ? 611  GLU   B CB    1 
ATOM   13588 N  N     . ASP   B  1  614  ? 30.161  31.697  54.295  1.00 18.48 ? 612  ASP   B N     1 
ATOM   13589 C  CA    . ASP   B  1  614  ? 28.786  31.226  54.195  1.00 18.34 ? 612  ASP   B CA    1 
ATOM   13590 C  C     . ASP   B  1  614  ? 27.851  32.066  55.041  1.00 19.08 ? 612  ASP   B C     1 
ATOM   13591 O  O     . ASP   B  1  614  ? 26.672  32.192  54.705  1.00 18.41 ? 612  ASP   B O     1 
ATOM   13592 C  CB    . ASP   B  1  614  ? 28.688  29.753  54.561  1.00 20.61 ? 612  ASP   B CB    1 
ATOM   13593 C  CG    . ASP   B  1  614  ? 29.147  28.852  53.428  1.00 24.07 ? 612  ASP   B CG    1 
ATOM   13594 O  OD1   . ASP   B  1  614  ? 29.081  29.287  52.253  1.00 28.81 ? 612  ASP   B OD1   1 
ATOM   13595 O  OD2   . ASP   B  1  614  ? 29.580  27.722  53.711  1.00 25.04 ? 612  ASP   B OD2   1 
ATOM   13596 N  N     . ALA   B  1  615  ? 28.349  32.650  56.130  1.00 18.48 ? 613  ALA   B N     1 
ATOM   13597 C  CA    . ALA   B  1  615  ? 27.526  33.582  56.887  1.00 17.33 ? 613  ALA   B CA    1 
ATOM   13598 C  C     . ALA   B  1  615  ? 27.125  34.764  56.017  1.00 18.13 ? 613  ALA   B C     1 
ATOM   13599 O  O     . ALA   B  1  615  ? 25.952  35.143  55.960  1.00 17.20 ? 613  ALA   B O     1 
ATOM   13600 C  CB    . ALA   B  1  615  ? 28.267  34.045  58.138  1.00 20.36 ? 613  ALA   B CB    1 
ATOM   13601 N  N     . ARG   B  1  616  ? 28.084  35.332  55.287  1.00 19.69 ? 614  ARG   B N     1 
ATOM   13602 C  CA    . ARG   B  1  616  ? 27.745  36.435  54.395  1.00 19.37 ? 614  ARG   B CA    1 
ATOM   13603 C  C     . ARG   B  1  616  ? 26.835  35.971  53.267  1.00 17.99 ? 614  ARG   B C     1 
ATOM   13604 O  O     . ARG   B  1  616  ? 25.916  36.697  52.859  1.00 19.04 ? 614  ARG   B O     1 
ATOM   13605 C  CB    . ARG   B  1  616  ? 29.020  37.078  53.858  1.00 23.70 ? 614  ARG   B CB    1 
ATOM   13606 C  CG    . ARG   B  1  616  ? 29.671  37.962  54.899  1.00 24.33 ? 614  ARG   B CG    1 
ATOM   13607 C  CD    . ARG   B  1  616  ? 30.844  38.707  54.301  1.00 30.10 ? 614  ARG   B CD    1 
ATOM   13608 N  NE    . ARG   B  1  616  ? 31.961  37.807  54.068  1.00 31.93 ? 614  ARG   B NE    1 
ATOM   13609 C  CZ    . ARG   B  1  616  ? 32.805  37.419  55.013  1.00 32.00 ? 614  ARG   B CZ    1 
ATOM   13610 N  NH1   . ARG   B  1  616  ? 32.679  37.834  56.266  1.00 29.85 ? 614  ARG   B NH1   1 
ATOM   13611 N  NH2   . ARG   B  1  616  ? 33.794  36.590  54.696  1.00 31.14 ? 614  ARG   B NH2   1 
ATOM   13612 N  N     . ARG   B  1  617  ? 27.079  34.768  52.743  1.00 18.02 ? 615  ARG   B N     1 
ATOM   13613 C  CA    . ARG   B  1  617  ? 26.191  34.241  51.713  1.00 19.43 ? 615  ARG   B CA    1 
ATOM   13614 C  C     . ARG   B  1  617  ? 24.768  34.125  52.236  1.00 18.66 ? 615  ARG   B C     1 
ATOM   13615 O  O     . ARG   B  1  617  ? 23.809  34.488  51.548  1.00 18.62 ? 615  ARG   B O     1 
ATOM   13616 C  CB    . ARG   B  1  617  ? 26.687  32.881  51.215  1.00 22.10 ? 615  ARG   B CB    1 
ATOM   13617 C  CG    . ARG   B  1  617  ? 25.825  32.299  50.093  1.00 22.58 ? 615  ARG   B CG    1 
ATOM   13618 C  CD    . ARG   B  1  617  ? 26.603  31.292  49.256  1.00 29.11 ? 615  ARG   B CD    1 
ATOM   13619 N  NE    . ARG   B  1  617  ? 26.873  30.049  49.966  1.00 32.41 ? 615  ARG   B NE    1 
ATOM   13620 C  CZ    . ARG   B  1  617  ? 26.054  29.006  49.983  1.00 38.90 ? 615  ARG   B CZ    1 
ATOM   13621 N  NH1   . ARG   B  1  617  ? 24.882  29.036  49.363  1.00 32.97 ? 615  ARG   B NH1   1 
ATOM   13622 N  NH2   . ARG   B  1  617  ? 26.413  27.910  50.647  1.00 38.90 ? 615  ARG   B NH2   1 
ATOM   13623 N  N     . ALA   B  1  618  ? 24.615  33.644  53.471  1.00 17.42 ? 616  ALA   B N     1 
ATOM   13624 C  CA    . ALA   B  1  618  ? 23.283  33.510  54.038  1.00 15.31 ? 616  ALA   B CA    1 
ATOM   13625 C  C     . ALA   B  1  618  ? 22.580  34.857  54.090  1.00 15.96 ? 616  ALA   B C     1 
ATOM   13626 O  O     . ALA   B  1  618  ? 21.384  34.950  53.799  1.00 17.08 ? 616  ALA   B O     1 
ATOM   13627 C  CB    . ALA   B  1  618  ? 23.389  32.912  55.439  1.00 16.61 ? 616  ALA   B CB    1 
ATOM   13628 N  N     . VAL   B  1  619  ? 23.297  35.912  54.467  1.00 17.19 ? 617  VAL   B N     1 
ATOM   13629 C  CA    . VAL   B  1  619  ? 22.650  37.216  54.540  1.00 16.68 ? 617  VAL   B CA    1 
ATOM   13630 C  C     . VAL   B  1  619  ? 22.199  37.661  53.164  1.00 18.22 ? 617  VAL   B C     1 
ATOM   13631 O  O     . VAL   B  1  619  ? 21.111  38.221  53.004  1.00 18.73 ? 617  VAL   B O     1 
ATOM   13632 C  CB    . VAL   B  1  619  ? 23.539  38.250  55.244  1.00 17.14 ? 617  VAL   B CB    1 
ATOM   13633 C  CG1   . VAL   B  1  619  ? 22.851  39.605  55.292  1.00 19.48 ? 617  VAL   B CG1   1 
ATOM   13634 C  CG2   . VAL   B  1  619  ? 23.837  37.770  56.661  1.00 18.47 ? 617  VAL   B CG2   1 
ATOM   13635 N  N     . ARG   B  1  620  ? 23.013  37.392  52.145  1.00 18.59 ? 618  ARG   B N     1 
ATOM   13636 C  CA    . ARG   B  1  620  ? 22.606  37.723  50.787  1.00 21.24 ? 618  ARG   B CA    1 
ATOM   13637 C  C     . ARG   B  1  620  ? 21.373  36.939  50.377  1.00 17.25 ? 618  ARG   B C     1 
ATOM   13638 O  O     . ARG   B  1  620  ? 20.450  37.495  49.770  1.00 18.93 ? 618  ARG   B O     1 
ATOM   13639 C  CB    . ARG   B  1  620  ? 23.759  37.456  49.827  1.00 23.47 ? 618  ARG   B CB    1 
ATOM   13640 C  CG    . ARG   B  1  620  ? 24.549  38.701  49.505  1.00 38.14 ? 618  ARG   B CG    1 
ATOM   13641 C  CD    . ARG   B  1  620  ? 25.667  38.424  48.514  1.00 39.02 ? 618  ARG   B CD    1 
ATOM   13642 N  NE    . ARG   B  1  620  ? 26.839  37.882  49.187  1.00 45.22 ? 618  ARG   B NE    1 
ATOM   13643 C  CZ    . ARG   B  1  620  ? 27.273  36.636  49.061  1.00 41.01 ? 618  ARG   B CZ    1 
ATOM   13644 N  NH1   . ARG   B  1  620  ? 26.680  35.772  48.249  1.00 41.64 ? 618  ARG   B NH1   1 
ATOM   13645 N  NH2   . ARG   B  1  620  ? 28.335  36.251  49.760  1.00 36.33 ? 618  ARG   B NH2   1 
ATOM   13646 N  N     . LEU   B  1  621  ? 21.325  35.650  50.717  1.00 18.19 ? 619  LEU   B N     1 
ATOM   13647 C  CA    . LEU   B  1  621  ? 20.139  34.850  50.415  1.00 17.73 ? 619  LEU   B CA    1 
ATOM   13648 C  C     . LEU   B  1  621  ? 18.911  35.374  51.146  1.00 20.63 ? 619  LEU   B C     1 
ATOM   13649 O  O     . LEU   B  1  621  ? 17.802  35.369  50.593  1.00 20.24 ? 619  LEU   B O     1 
ATOM   13650 C  CB    . LEU   B  1  621  ? 20.390  33.388  50.774  1.00 19.10 ? 619  LEU   B CB    1 
ATOM   13651 C  CG    . LEU   B  1  621  ? 21.434  32.691  49.893  1.00 19.69 ? 619  LEU   B CG    1 
ATOM   13652 C  CD1   . LEU   B  1  621  ? 21.839  31.354  50.496  1.00 21.45 ? 619  LEU   B CD1   1 
ATOM   13653 C  CD2   . LEU   B  1  621  ? 20.897  32.493  48.483  1.00 25.11 ? 619  LEU   B CD2   1 
ATOM   13654 N  N     . ALA   B  1  622  ? 19.083  35.821  52.392  1.00 17.37 ? 620  ALA   B N     1 
ATOM   13655 C  CA    . ALA   B  1  622  ? 17.954  36.384  53.127  1.00 17.88 ? 620  ALA   B CA    1 
ATOM   13656 C  C     . ALA   B  1  622  ? 17.486  37.675  52.476  1.00 17.20 ? 620  ALA   B C     1 
ATOM   13657 O  O     . ALA   B  1  622  ? 16.279  37.905  52.350  1.00 17.54 ? 620  ALA   B O     1 
ATOM   13658 C  CB    . ALA   B  1  622  ? 18.327  36.615  54.595  1.00 17.45 ? 620  ALA   B CB    1 
ATOM   13659 N  N     . ALA   B  1  623  ? 18.427  38.517  52.037  1.00 17.23 ? 621  ALA   B N     1 
ATOM   13660 C  CA    . ALA   B  1  623  ? 18.036  39.762  51.388  1.00 17.33 ? 621  ALA   B CA    1 
ATOM   13661 C  C     . ALA   B  1  623  ? 17.266  39.485  50.105  1.00 19.18 ? 621  ALA   B C     1 
ATOM   13662 O  O     . ALA   B  1  623  ? 16.242  40.129  49.830  1.00 18.78 ? 621  ALA   B O     1 
ATOM   13663 C  CB    . ALA   B  1  623  ? 19.272  40.613  51.105  1.00 18.13 ? 621  ALA   B CB    1 
ATOM   13664 N  N     . ASP   B  1  624  ? 17.698  38.480  49.342  1.00 19.59 ? 622  ASP   B N     1 
ATOM   13665 C  CA    . ASP   B  1  624  ? 16.988  38.126  48.117  1.00 19.73 ? 622  ASP   B CA    1 
ATOM   13666 C  C     . ASP   B  1  624  ? 15.562  37.684  48.410  1.00 22.27 ? 622  ASP   B C     1 
ATOM   13667 O  O     . ASP   B  1  624  ? 14.635  38.002  47.653  1.00 27.83 ? 622  ASP   B O     1 
ATOM   13668 C  CB    . ASP   B  1  624  ? 17.733  36.997  47.397  1.00 22.70 ? 622  ASP   B CB    1 
ATOM   13669 C  CG    . ASP   B  1  624  ? 19.090  37.419  46.871  1.00 30.90 ? 622  ASP   B CG    1 
ATOM   13670 O  OD1   . ASP   B  1  624  ? 19.336  38.634  46.712  1.00 34.74 ? 622  ASP   B OD1   1 
ATOM   13671 O  OD2   . ASP   B  1  624  ? 19.917  36.518  46.605  1.00 35.27 ? 622  ASP   B OD2   1 
ATOM   13672 N  N     . ALA   B  1  625  ? 15.369  36.955  49.504  1.00 23.66 ? 623  ALA   B N     1 
ATOM   13673 C  CA    . ALA   B  1  625  ? 14.077  36.401  49.872  1.00 28.23 ? 623  ALA   B CA    1 
ATOM   13674 C  C     . ALA   B  1  625  ? 13.209  37.372  50.650  1.00 25.10 ? 623  ALA   B C     1 
ATOM   13675 O  O     . ALA   B  1  625  ? 12.034  37.073  50.906  1.00 23.51 ? 623  ALA   B O     1 
ATOM   13676 C  CB    . ALA   B  1  625  ? 14.296  35.180  50.752  1.00 32.70 ? 623  ALA   B CB    1 
ATOM   13677 N  N     . ALA   B  1  626  ? 13.756  38.507  51.057  1.00 20.12 ? 624  ALA   B N     1 
ATOM   13678 C  CA    . ALA   B  1  626  ? 13.017  39.381  51.957  1.00 18.97 ? 624  ALA   B CA    1 
ATOM   13679 C  C     . ALA   B  1  626  ? 11.682  39.848  51.395  1.00 19.05 ? 624  ALA   B C     1 
ATOM   13680 O  O     . ALA   B  1  626  ? 10.689  39.810  52.145  1.00 19.75 ? 624  ALA   B O     1 
ATOM   13681 C  CB    . ALA   B  1  626  ? 13.903  40.536  52.427  1.00 18.35 ? 624  ALA   B CB    1 
ATOM   13682 N  N     . PRO   B  1  627  ? 11.563  40.263  50.128  1.00 19.37 ? 625  PRO   B N     1 
ATOM   13683 C  CA    . PRO   B  1  627  ? 10.237  40.671  49.642  1.00 19.09 ? 625  PRO   B CA    1 
ATOM   13684 C  C     . PRO   B  1  627  ? 9.216   39.553  49.666  1.00 20.95 ? 625  PRO   B C     1 
ATOM   13685 O  O     . PRO   B  1  627  ? 8.048   39.802  49.983  1.00 20.16 ? 625  PRO   B O     1 
ATOM   13686 C  CB    . PRO   B  1  627  ? 10.503  41.154  48.204  1.00 24.74 ? 625  PRO   B CB    1 
ATOM   13687 C  CG    . PRO   B  1  627  ? 11.950  41.447  48.154  1.00 26.84 ? 625  PRO   B CG    1 
ATOM   13688 C  CD    . PRO   B  1  627  ? 12.615  40.515  49.127  1.00 21.61 ? 625  PRO   B CD    1 
ATOM   13689 N  N     . ASP   B  1  628  ? 9.608   38.324  49.336  1.00 19.76 ? 626  ASP   B N     1 
ATOM   13690 C  CA    . ASP   B  1  628  ? 8.622   37.248  49.298  1.00 21.68 ? 626  ASP   B CA    1 
ATOM   13691 C  C     . ASP   B  1  628  ? 8.098   36.933  50.690  1.00 21.55 ? 626  ASP   B C     1 
ATOM   13692 O  O     . ASP   B  1  628  ? 6.911   36.637  50.858  1.00 21.99 ? 626  ASP   B O     1 
ATOM   13693 C  CB    . ASP   B  1  628  ? 9.200   35.982  48.668  1.00 23.39 ? 626  ASP   B CB    1 
ATOM   13694 C  CG    . ASP   B  1  628  ? 9.514   36.145  47.198  1.00 29.98 ? 626  ASP   B CG    1 
ATOM   13695 O  OD1   . ASP   B  1  628  ? 8.860   36.968  46.524  1.00 32.17 ? 626  ASP   B OD1   1 
ATOM   13696 O  OD2   . ASP   B  1  628  ? 10.427  35.440  46.733  1.00 35.98 ? 626  ASP   B OD2   1 
ATOM   13697 N  N     . TRP   B  1  629  ? 8.963   36.974  51.701  1.00 17.49 ? 627  TRP   B N     1 
ATOM   13698 C  CA    . TRP   B  1  629  ? 8.479   36.704  53.043  1.00 17.74 ? 627  TRP   B CA    1 
ATOM   13699 C  C     . TRP   B  1  629  ? 7.645   37.865  53.566  1.00 16.88 ? 627  TRP   B C     1 
ATOM   13700 O  O     . TRP   B  1  629  ? 6.612   37.647  54.201  1.00 17.28 ? 627  TRP   B O     1 
ATOM   13701 C  CB    . TRP   B  1  629  ? 9.656   36.383  53.957  1.00 17.21 ? 627  TRP   B CB    1 
ATOM   13702 C  CG    . TRP   B  1  629  ? 9.213   36.103  55.346  1.00 14.57 ? 627  TRP   B CG    1 
ATOM   13703 C  CD1   . TRP   B  1  629  ? 9.570   36.794  56.482  1.00 17.99 ? 627  TRP   B CD1   1 
ATOM   13704 C  CD2   . TRP   B  1  629  ? 8.312   35.079  55.767  1.00 16.96 ? 627  TRP   B CD2   1 
ATOM   13705 N  NE1   . TRP   B  1  629  ? 8.951   36.254  57.568  1.00 16.00 ? 627  TRP   B NE1   1 
ATOM   13706 C  CE2   . TRP   B  1  629  ? 8.175   35.198  57.168  1.00 15.64 ? 627  TRP   B CE2   1 
ATOM   13707 C  CE3   . TRP   B  1  629  ? 7.602   34.068  55.104  1.00 17.28 ? 627  TRP   B CE3   1 
ATOM   13708 C  CZ2   . TRP   B  1  629  ? 7.351   34.355  57.909  1.00 17.29 ? 627  TRP   B CZ2   1 
ATOM   13709 C  CZ3   . TRP   B  1  629  ? 6.788   33.230  55.849  1.00 17.49 ? 627  TRP   B CZ3   1 
ATOM   13710 C  CH2   . TRP   B  1  629  ? 6.674   33.376  57.238  1.00 18.60 ? 627  TRP   B CH2   1 
ATOM   13711 N  N     . ALA   B  1  630  ? 8.053   39.100  53.271  1.00 16.98 ? 628  ALA   B N     1 
ATOM   13712 C  CA    . ALA   B  1  630  ? 7.273   40.257  53.695  1.00 18.11 ? 628  ALA   B CA    1 
ATOM   13713 C  C     . ALA   B  1  630  ? 5.883   40.222  53.086  1.00 18.89 ? 628  ALA   B C     1 
ATOM   13714 O  O     . ALA   B  1  630  ? 4.927   40.711  53.695  1.00 20.84 ? 628  ALA   B O     1 
ATOM   13715 C  CB    . ALA   B  1  630  ? 7.977   41.548  53.293  1.00 19.98 ? 628  ALA   B CB    1 
ATOM   13716 N  N     . ALA   B  1  631  ? 5.749   39.642  51.893  1.00 18.30 ? 629  ALA   B N     1 
ATOM   13717 C  CA    . ALA   B  1  631  ? 4.459   39.560  51.230  1.00 19.08 ? 629  ALA   B CA    1 
ATOM   13718 C  C     . ALA   B  1  631  ? 3.551   38.484  51.806  1.00 20.70 ? 629  ALA   B C     1 
ATOM   13719 O  O     . ALA   B  1  631  ? 2.366   38.444  51.451  1.00 21.55 ? 629  ALA   B O     1 
ATOM   13720 C  CB    . ALA   B  1  631  ? 4.667   39.306  49.733  1.00 19.90 ? 629  ALA   B CB    1 
ATOM   13721 N  N     . VAL   B  1  632  ? 4.054   37.609  52.665  1.00 18.70 ? 630  VAL   B N     1 
ATOM   13722 C  CA    . VAL   B  1  632  ? 3.143   36.663  53.309  1.00 18.26 ? 630  VAL   B CA    1 
ATOM   13723 C  C     . VAL   B  1  632  ? 2.342   37.427  54.352  1.00 19.03 ? 630  VAL   B C     1 
ATOM   13724 O  O     . VAL   B  1  632  ? 2.946   38.125  55.192  1.00 19.09 ? 630  VAL   B O     1 
ATOM   13725 C  CB    . VAL   B  1  632  ? 3.939   35.532  53.968  1.00 18.63 ? 630  VAL   B CB    1 
ATOM   13726 C  CG1   . VAL   B  1  632  ? 2.972   34.632  54.739  1.00 18.86 ? 630  VAL   B CG1   1 
ATOM   13727 C  CG2   . VAL   B  1  632  ? 4.708   34.748  52.930  1.00 19.13 ? 630  VAL   B CG2   1 
ATOM   13728 N  N     . PRO   B  1  633  ? 1.014   37.383  54.312  1.00 17.83 ? 631  PRO   B N     1 
ATOM   13729 C  CA    . PRO   B  1  633  ? 0.239   38.252  55.179  1.00 18.34 ? 631  PRO   B CA    1 
ATOM   13730 C  C     . PRO   B  1  633  ? 0.565   37.978  56.636  1.00 18.18 ? 631  PRO   B C     1 
ATOM   13731 O  O     . PRO   B  1  633  ? 0.839   36.829  57.018  1.00 17.13 ? 631  PRO   B O     1 
ATOM   13732 C  CB    . PRO   B  1  633  ? -1.208  37.863  54.863  1.00 17.63 ? 631  PRO   B CB    1 
ATOM   13733 C  CG    . PRO   B  1  633  ? -1.159  37.373  53.449  1.00 22.53 ? 631  PRO   B CG    1 
ATOM   13734 C  CD    . PRO   B  1  633  ? 0.175   36.661  53.339  1.00 17.72 ? 631  PRO   B CD    1 
ATOM   13735 N  N     . PRO   B  1  634  ? 0.534   39.007  57.476  1.00 17.84 ? 632  PRO   B N     1 
ATOM   13736 C  CA    . PRO   B  1  634  ? 0.849   38.802  58.902  1.00 18.58 ? 632  PRO   B CA    1 
ATOM   13737 C  C     . PRO   B  1  634  ? 0.070   37.674  59.536  1.00 17.15 ? 632  PRO   B C     1 
ATOM   13738 O  O     . PRO   B  1  634  ? 0.650   36.915  60.319  1.00 17.08 ? 632  PRO   B O     1 
ATOM   13739 C  CB    . PRO   B  1  634  ? 0.548   40.168  59.534  1.00 19.58 ? 632  PRO   B CB    1 
ATOM   13740 C  CG    . PRO   B  1  634  ? 0.718   41.147  58.419  1.00 22.21 ? 632  PRO   B CG    1 
ATOM   13741 C  CD    . PRO   B  1  634  ? 0.432   40.431  57.118  1.00 18.44 ? 632  PRO   B CD    1 
ATOM   13742 N  N     . SER   B  1  635  ? -1.214  37.519  59.216  1.00 18.36 ? 633  SER   B N     1 
ATOM   13743 C  CA    . SER   B  1  635  ? -1.974  36.438  59.835  1.00 19.61 ? 633  SER   B CA    1 
ATOM   13744 C  C     . SER   B  1  635  ? -1.439  35.077  59.429  1.00 17.09 ? 633  SER   B C     1 
ATOM   13745 O  O     . SER   B  1  635  ? -1.495  34.132  60.221  1.00 17.17 ? 633  SER   B O     1 
ATOM   13746 C  CB    . SER   B  1  635  ? -3.452  36.546  59.468  1.00 23.19 ? 633  SER   B CB    1 
ATOM   13747 O  OG    . SER   B  1  635  ? -3.629  36.396  58.078  1.00 32.32 ? 633  SER   B OG    1 
ATOM   13748 N  N     . GLU   B  1  636  ? -0.924  34.952  58.201  1.00 18.07 ? 634  GLU   B N     1 
ATOM   13749 C  CA    . GLU   B  1  636  ? -0.372  33.675  57.769  1.00 17.15 ? 634  GLU   B CA    1 
ATOM   13750 C  C     . GLU   B  1  636  ? 1.010   33.451  58.365  1.00 16.36 ? 634  GLU   B C     1 
ATOM   13751 O  O     . GLU   B  1  636  ? 1.363   32.316  58.708  1.00 16.45 ? 634  GLU   B O     1 
ATOM   13752 C  CB    . GLU   B  1  636  ? -0.314  33.588  56.243  1.00 18.78 ? 634  GLU   B CB    1 
ATOM   13753 C  CG    . GLU   B  1  636  ? 0.322   32.284  55.750  1.00 27.40 ? 634  GLU   B CG    1 
ATOM   13754 C  CD    . GLU   B  1  636  ? -0.277  31.038  56.412  1.00 36.59 ? 634  GLU   B CD    1 
ATOM   13755 O  OE1   . GLU   B  1  636  ? -1.525  30.948  56.519  1.00 31.77 ? 634  GLU   B OE1   1 
ATOM   13756 O  OE2   . GLU   B  1  636  ? 0.505   30.151  56.837  1.00 32.02 ? 634  GLU   B OE2   1 
ATOM   13757 N  N     . ARG   B  1  637  ? 1.804   34.515  58.519  1.00 14.40 ? 635  ARG   B N     1 
ATOM   13758 C  CA    . ARG   B  1  637  ? 3.062   34.360  59.241  1.00 14.90 ? 635  ARG   B CA    1 
ATOM   13759 C  C     . ARG   B  1  637  ? 2.789   33.932  60.673  1.00 15.28 ? 635  ARG   B C     1 
ATOM   13760 O  O     . ARG   B  1  637  ? 3.456   33.033  61.204  1.00 15.98 ? 635  ARG   B O     1 
ATOM   13761 C  CB    . ARG   B  1  637  ? 3.852   35.660  59.201  1.00 14.77 ? 635  ARG   B CB    1 
ATOM   13762 C  CG    . ARG   B  1  637  ? 4.119   36.147  57.793  1.00 15.75 ? 635  ARG   B CG    1 
ATOM   13763 C  CD    . ARG   B  1  637  ? 5.159   37.241  57.749  1.00 16.54 ? 635  ARG   B CD    1 
ATOM   13764 N  NE    . ARG   B  1  637  ? 4.787   38.405  58.542  1.00 16.82 ? 635  ARG   B NE    1 
ATOM   13765 C  CZ    . ARG   B  1  637  ? 4.558   39.617  58.060  1.00 17.06 ? 635  ARG   B CZ    1 
ATOM   13766 N  NH1   . ARG   B  1  637  ? 4.439   39.839  56.760  1.00 21.82 ? 635  ARG   B NH1   1 
ATOM   13767 N  NH2   . ARG   B  1  637  ? 4.459   40.638  58.901  1.00 17.03 ? 635  ARG   B NH2   1 
ATOM   13768 N  N     . ALA   B  1  638  ? 1.774   34.536  61.297  1.00 14.05 ? 636  ALA   B N     1 
ATOM   13769 C  CA    . ALA   B  1  638  ? 1.387   34.152  62.652  1.00 13.80 ? 636  ALA   B CA    1 
ATOM   13770 C  C     . ALA   B  1  638  ? 0.911   32.708  62.695  1.00 15.19 ? 636  ALA   B C     1 
ATOM   13771 O  O     . ALA   B  1  638  ? 1.180   31.989  63.663  1.00 15.20 ? 636  ALA   B O     1 
ATOM   13772 C  CB    . ALA   B  1  638  ? 0.314   35.112  63.178  1.00 14.40 ? 636  ALA   B CB    1 
ATOM   13773 N  N     . ALA   B  1  639  ? 0.212   32.253  61.649  1.00 15.16 ? 637  ALA   B N     1 
ATOM   13774 C  CA    . ALA   B  1  639  ? -0.232  30.862  61.637  1.00 14.95 ? 637  ALA   B CA    1 
ATOM   13775 C  C     . ALA   B  1  639  ? 0.949   29.902  61.600  1.00 14.70 ? 637  ALA   B C     1 
ATOM   13776 O  O     . ALA   B  1  639  ? 0.872   28.808  62.165  1.00 15.46 ? 637  ALA   B O     1 
ATOM   13777 C  CB    . ALA   B  1  639  ? -1.145  30.612  60.438  1.00 15.68 ? 637  ALA   B CB    1 
ATOM   13778 N  N     . CYS   B  1  640  ? 2.051   30.296  60.955  1.00 14.42 ? 638  CYS   B N     1 
ATOM   13779 C  CA    . CYS   B  1  640  ? 3.260   29.478  61.000  1.00 15.10 ? 638  CYS   B CA    1 
ATOM   13780 C  C     . CYS   B  1  640  ? 3.778   29.356  62.419  1.00 13.84 ? 638  CYS   B C     1 
ATOM   13781 O  O     . CYS   B  1  640  ? 4.152   28.267  62.865  1.00 14.65 ? 638  CYS   B O     1 
ATOM   13782 C  CB    . CYS   B  1  640  ? 4.369   30.080  60.138  1.00 14.29 ? 638  CYS   B CB    1 
ATOM   13783 S  SG    . CYS   B  1  640  ? 4.059   30.027  58.390  1.00 17.19 ? 638  CYS   B SG    1 
ATOM   13784 N  N     . LEU   B  1  641  ? 3.835   30.478  63.138  1.00 13.33 ? 639  LEU   B N     1 
ATOM   13785 C  CA    . LEU   B  1  641  ? 4.283   30.421  64.525  1.00 13.33 ? 639  LEU   B CA    1 
ATOM   13786 C  C     . LEU   B  1  641  ? 3.387   29.506  65.339  1.00 14.01 ? 639  LEU   B C     1 
ATOM   13787 O  O     . LEU   B  1  641  ? 3.873   28.712  66.159  1.00 13.31 ? 639  LEU   B O     1 
ATOM   13788 C  CB    . LEU   B  1  641  ? 4.278   31.818  65.144  1.00 14.72 ? 639  LEU   B CB    1 
ATOM   13789 C  CG    . LEU   B  1  641  ? 5.541   32.664  64.962  1.00 15.75 ? 639  LEU   B CG    1 
ATOM   13790 C  CD1   . LEU   B  1  641  ? 5.953   32.879  63.504  1.00 19.14 ? 639  LEU   B CD1   1 
ATOM   13791 C  CD2   . LEU   B  1  641  ? 5.367   33.988  65.674  1.00 14.56 ? 639  LEU   B CD2   1 
ATOM   13792 N  N     . ASP   B  1  642  ? 2.063   29.637  65.161  1.00 13.17 ? 640  ASP   B N     1 
ATOM   13793 C  CA    . ASP   B  1  642  ? 1.151   28.792  65.922  1.00 15.11 ? 640  ASP   B CA    1 
ATOM   13794 C  C     . ASP   B  1  642  ? 1.337   27.328  65.565  1.00 13.76 ? 640  ASP   B C     1 
ATOM   13795 O  O     . ASP   B  1  642  ? 1.281   26.457  66.434  1.00 14.94 ? 640  ASP   B O     1 
ATOM   13796 C  CB    . ASP   B  1  642  ? -0.296  29.210  65.686  1.00 14.17 ? 640  ASP   B CB    1 
ATOM   13797 C  CG    . ASP   B  1  642  ? -0.701  30.407  66.497  1.00 16.96 ? 640  ASP   B CG    1 
ATOM   13798 O  OD1   . ASP   B  1  642  ? -0.070  30.699  67.524  1.00 17.43 ? 640  ASP   B OD1   1 
ATOM   13799 O  OD2   . ASP   B  1  642  ? -1.697  31.042  66.107  1.00 17.84 ? 640  ASP   B OD2   1 
ATOM   13800 N  N     . ARG   B  1  643  ? 1.585   27.030  64.292  1.00 14.22 ? 641  ARG   B N     1 
ATOM   13801 C  CA    . ARG   B  1  643  ? 1.825   25.636  63.939  1.00 15.63 ? 641  ARG   B CA    1 
ATOM   13802 C  C     . ARG   B  1  643  ? 3.117   25.136  64.556  1.00 14.30 ? 641  ARG   B C     1 
ATOM   13803 O  O     . ARG   B  1  643  ? 3.188   23.998  65.025  1.00 14.99 ? 641  ARG   B O     1 
ATOM   13804 C  CB    . ARG   B  1  643  ? 1.876   25.472  62.425  1.00 15.11 ? 641  ARG   B CB    1 
ATOM   13805 C  CG    . ARG   B  1  643  ? 0.504   25.352  61.799  1.00 17.07 ? 641  ARG   B CG    1 
ATOM   13806 C  CD    . ARG   B  1  643  ? 0.608   24.967  60.334  1.00 19.87 ? 641  ARG   B CD    1 
ATOM   13807 N  NE    . ARG   B  1  643  ? 1.289   25.999  59.561  1.00 18.81 ? 641  ARG   B NE    1 
ATOM   13808 C  CZ    . ARG   B  1  643  ? 0.684   27.008  58.951  1.00 19.13 ? 641  ARG   B CZ    1 
ATOM   13809 N  NH1   . ARG   B  1  643  ? -0.631  27.162  59.006  1.00 19.94 ? 641  ARG   B NH1   1 
ATOM   13810 N  NH2   . ARG   B  1  643  ? 1.415   27.894  58.278  1.00 21.74 ? 641  ARG   B NH2   1 
ATOM   13811 N  N     . ALA   B  1  644  ? 4.144   25.986  64.596  1.00 12.81 ? 642  ALA   B N     1 
ATOM   13812 C  CA    . ALA   B  1  644  ? 5.391   25.586  65.232  1.00 13.98 ? 642  ALA   B CA    1 
ATOM   13813 C  C     . ALA   B  1  644  ? 5.172   25.294  66.705  1.00 14.52 ? 642  ALA   B C     1 
ATOM   13814 O  O     . ALA   B  1  644  ? 5.758   24.360  67.264  1.00 14.76 ? 642  ALA   B O     1 
ATOM   13815 C  CB    . ALA   B  1  644  ? 6.437   26.675  65.031  1.00 13.99 ? 642  ALA   B CB    1 
ATOM   13816 N  N     . ALA   B  1  645  ? 4.332   26.099  67.356  1.00 13.92 ? 643  ALA   B N     1 
ATOM   13817 C  CA    . ALA   B  1  645  ? 4.074   25.884  68.770  1.00 14.19 ? 643  ALA   B CA    1 
ATOM   13818 C  C     . ALA   B  1  645  ? 3.385   24.551  69.004  1.00 13.34 ? 643  ALA   B C     1 
ATOM   13819 O  O     . ALA   B  1  645  ? 3.709   23.848  69.976  1.00 15.24 ? 643  ALA   B O     1 
ATOM   13820 C  CB    . ALA   B  1  645  ? 3.246   27.041  69.316  1.00 15.48 ? 643  ALA   B CB    1 
ATOM   13821 N  N     . GLU   B  1  646  ? 2.438   24.186  68.122  1.00 15.04 ? 644  GLU   B N     1 
ATOM   13822 C  CA    . GLU   B  1  646  ? 1.774   22.891  68.236  1.00 15.97 ? 644  GLU   B CA    1 
ATOM   13823 C  C     . GLU   B  1  646  ? 2.777   21.760  68.101  1.00 14.82 ? 644  GLU   B C     1 
ATOM   13824 O  O     . GLU   B  1  646  ? 2.698   20.756  68.816  1.00 15.70 ? 644  GLU   B O     1 
ATOM   13825 C  CB    . GLU   B  1  646  ? 0.719   22.738  67.137  1.00 18.17 ? 644  GLU   B CB    1 
ATOM   13826 C  CG    . GLU   B  1  646  ? -0.462  23.651  67.268  1.00 21.14 ? 644  GLU   B CG    1 
ATOM   13827 C  CD    . GLU   B  1  646  ? -1.199  23.454  68.570  1.00 30.41 ? 644  GLU   B CD    1 
ATOM   13828 O  OE1   . GLU   B  1  646  ? -1.537  22.297  68.905  1.00 39.23 ? 644  GLU   B OE1   1 
ATOM   13829 O  OE2   . GLU   B  1  646  ? -1.432  24.462  69.265  1.00 33.05 ? 644  GLU   B OE2   1 
ATOM   13830 N  N     . LEU   B  1  647  ? 3.733   21.907  67.181  1.00 15.61 ? 645  LEU   B N     1 
ATOM   13831 C  CA    . LEU   B  1  647  ? 4.739   20.866  66.994  1.00 17.17 ? 645  LEU   B CA    1 
ATOM   13832 C  C     . LEU   B  1  647  ? 5.656   20.768  68.202  1.00 16.09 ? 645  LEU   B C     1 
ATOM   13833 O  O     . LEU   B  1  647  ? 5.965   19.665  68.665  1.00 16.59 ? 645  LEU   B O     1 
ATOM   13834 C  CB    . LEU   B  1  647  ? 5.553   21.148  65.736  1.00 15.82 ? 645  LEU   B CB    1 
ATOM   13835 C  CG    . LEU   B  1  647  ? 4.803   21.079  64.412  1.00 15.98 ? 645  LEU   B CG    1 
ATOM   13836 C  CD1   . LEU   B  1  647  ? 5.768   21.359  63.279  1.00 18.04 ? 645  LEU   B CD1   1 
ATOM   13837 C  CD2   . LEU   B  1  647  ? 4.142   19.720  64.236  1.00 20.02 ? 645  LEU   B CD2   1 
ATOM   13838 N  N     . MET   B  1  648  ? 6.091   21.908  68.740  1.00 14.47 ? 646  MET   B N     1 
ATOM   13839 C  CA    . MET   B  1  648  ? 6.943   21.858  69.923  1.00 15.12 ? 646  MET   B CA    1 
ATOM   13840 C  C     . MET   B  1  648  ? 6.186   21.254  71.095  1.00 15.39 ? 646  MET   B C     1 
ATOM   13841 O  O     . MET   B  1  648  ? 6.757   20.511  71.896  1.00 16.32 ? 646  MET   B O     1 
ATOM   13842 C  CB    . MET   B  1  648  ? 7.451   23.245  70.300  1.00 16.52 ? 646  MET   B CB    1 
ATOM   13843 C  CG    . MET   B  1  648  ? 8.494   23.764  69.355  1.00 16.62 ? 646  MET   B CG    1 
ATOM   13844 S  SD    . MET   B  1  648  ? 9.278   25.167  70.129  1.00 17.77 ? 646  MET   B SD    1 
ATOM   13845 C  CE    . MET   B  1  648  ? 10.342  25.643  68.773  1.00 19.41 ? 646  MET   B CE    1 
ATOM   13846 N  N     . GLN   B  1  649  ? 4.897   21.570  71.218  1.00 13.80 ? 647  GLN   B N     1 
ATOM   13847 C  CA    . GLN   B  1  649  ? 4.113   20.994  72.302  1.00 15.35 ? 647  GLN   B CA    1 
ATOM   13848 C  C     . GLN   B  1  649  ? 4.035   19.481  72.165  1.00 15.31 ? 647  GLN   B C     1 
ATOM   13849 O  O     . GLN   B  1  649  ? 4.219   18.746  73.147  1.00 17.65 ? 647  GLN   B O     1 
ATOM   13850 C  CB    . GLN   B  1  649  ? 2.712   21.599  72.296  1.00 15.30 ? 647  GLN   B CB    1 
ATOM   13851 C  CG    . GLN   B  1  649  ? 1.853   21.171  73.472  1.00 16.64 ? 647  GLN   B CG    1 
ATOM   13852 C  CD    . GLN   B  1  649  ? 2.299   21.827  74.749  1.00 16.68 ? 647  GLN   B CD    1 
ATOM   13853 O  OE1   . GLN   B  1  649  ? 2.010   23.003  74.988  1.00 16.46 ? 647  GLN   B OE1   1 
ATOM   13854 N  NE2   . GLN   B  1  649  ? 3.045   21.093  75.562  1.00 17.13 ? 647  GLN   B NE2   1 
ATOM   13855 N  N     . ALA   B  1  650  ? 3.739   18.996  70.959  1.00 15.66 ? 648  ALA   B N     1 
ATOM   13856 C  CA    . ALA   B  1  650  ? 3.595   17.560  70.766  1.00 16.86 ? 648  ALA   B CA    1 
ATOM   13857 C  C     . ALA   B  1  650  ? 4.922   16.834  70.924  1.00 18.51 ? 648  ALA   B C     1 
ATOM   13858 O  O     . ALA   B  1  650  ? 4.945   15.683  71.372  1.00 20.07 ? 648  ALA   B O     1 
ATOM   13859 C  CB    . ALA   B  1  650  ? 2.963   17.271  69.404  1.00 19.09 ? 648  ALA   B CB    1 
ATOM   13860 N  N     . ARG   B  1  651  ? 6.029   17.493  70.598  1.00 16.01 ? 649  ARG   B N     1 
ATOM   13861 C  CA    . ARG   B  1  651  ? 7.348   16.877  70.646  1.00 15.40 ? 649  ARG   B CA    1 
ATOM   13862 C  C     . ARG   B  1  651  ? 8.108   17.230  71.907  1.00 15.64 ? 649  ARG   B C     1 
ATOM   13863 O  O     . ARG   B  1  651  ? 9.299   16.918  72.021  1.00 16.93 ? 649  ARG   B O     1 
ATOM   13864 C  CB    . ARG   B  1  651  ? 8.133   17.285  69.411  1.00 17.19 ? 649  ARG   B CB    1 
ATOM   13865 C  CG    . ARG   B  1  651  ? 7.447   16.759  68.184  1.00 18.15 ? 649  ARG   B CG    1 
ATOM   13866 C  CD    . ARG   B  1  651  ? 8.029   17.304  66.917  1.00 18.03 ? 649  ARG   B CD    1 
ATOM   13867 N  NE    . ARG   B  1  651  ? 7.158   16.928  65.819  1.00 19.81 ? 649  ARG   B NE    1 
ATOM   13868 C  CZ    . ARG   B  1  651  ? 7.317   17.340  64.574  1.00 18.78 ? 649  ARG   B CZ    1 
ATOM   13869 N  NH1   . ARG   B  1  651  ? 8.369   18.070  64.220  1.00 19.19 ? 649  ARG   B NH1   1 
ATOM   13870 N  NH2   . ARG   B  1  651  ? 6.398   17.020  63.665  1.00 19.47 ? 649  ARG   B NH2   1 
ATOM   13871 N  N     . MET   B  1  652  ? 7.447   17.877  72.856  1.00 15.06 ? 650  MET   B N     1 
ATOM   13872 C  CA    . MET   B  1  652  ? 8.125   18.276  74.083  1.00 15.48 ? 650  MET   B CA    1 
ATOM   13873 C  C     . MET   B  1  652  ? 8.932   17.154  74.722  1.00 15.56 ? 650  MET   B C     1 
ATOM   13874 O  O     . MET   B  1  652  ? 10.074  17.417  75.122  1.00 17.22 ? 650  MET   B O     1 
ATOM   13875 C  CB    . MET   B  1  652  ? 7.106   18.887  75.056  1.00 15.66 ? 650  MET   B CB    1 
ATOM   13876 C  CG    . MET   B  1  652  ? 7.734   19.283  76.370  1.00 15.11 ? 650  MET   B CG    1 
ATOM   13877 S  SD    . MET   B  1  652  ? 6.539   19.988  77.523  1.00 18.65 ? 650  MET   B SD    1 
ATOM   13878 C  CE    . MET   B  1  652  ? 6.328   21.585  76.791  1.00 17.99 ? 650  MET   B CE    1 
ATOM   13879 N  N     . PRO   B  1  653  ? 8.437   15.917  74.847  1.00 15.70 ? 651  PRO   B N     1 
ATOM   13880 C  CA    . PRO   B  1  653  ? 9.268   14.883  75.485  1.00 18.57 ? 651  PRO   B CA    1 
ATOM   13881 C  C     . PRO   B  1  653  ? 10.611  14.673  74.811  1.00 17.70 ? 651  PRO   B C     1 
ATOM   13882 O  O     . PRO   B  1  653  ? 11.629  14.556  75.507  1.00 17.90 ? 651  PRO   B O     1 
ATOM   13883 C  CB    . PRO   B  1  653  ? 8.373   13.635  75.433  1.00 18.70 ? 651  PRO   B CB    1 
ATOM   13884 C  CG    . PRO   B  1  653  ? 6.977   14.197  75.491  1.00 17.01 ? 651  PRO   B CG    1 
ATOM   13885 C  CD    . PRO   B  1  653  ? 7.066   15.428  74.604  1.00 17.77 ? 651  PRO   B CD    1 
ATOM   13886 N  N     . THR   B  1  654  ? 10.642  14.653  73.476  1.00 16.79 ? 652  THR   B N     1 
ATOM   13887 C  CA    . THR   B  1  654  ? 11.902  14.506  72.760  1.00 17.74 ? 652  THR   B CA    1 
ATOM   13888 C  C     . THR   B  1  654  ? 12.776  15.739  72.943  1.00 19.35 ? 652  THR   B C     1 
ATOM   13889 O  O     . THR   B  1  654  ? 13.982  15.623  73.198  1.00 17.78 ? 652  THR   B O     1 
ATOM   13890 C  CB    . THR   B  1  654  ? 11.611  14.267  71.281  1.00 18.50 ? 652  THR   B CB    1 
ATOM   13891 O  OG1   . THR   B  1  654  ? 10.837  13.070  71.145  1.00 20.23 ? 652  THR   B OG1   1 
ATOM   13892 C  CG2   . THR   B  1  654  ? 12.911  14.114  70.496  1.00 19.95 ? 652  THR   B CG2   1 
ATOM   13893 N  N     . LEU   B  1  655  ? 12.186  16.927  72.827  1.00 16.59 ? 653  LEU   B N     1 
ATOM   13894 C  CA    . LEU   B  1  655  ? 12.959  18.151  72.993  1.00 15.62 ? 653  LEU   B CA    1 
ATOM   13895 C  C     . LEU   B  1  655  ? 13.555  18.230  74.383  1.00 16.95 ? 653  LEU   B C     1 
ATOM   13896 O  O     . LEU   B  1  655  ? 14.693  18.687  74.548  1.00 17.22 ? 653  LEU   B O     1 
ATOM   13897 C  CB    . LEU   B  1  655  ? 12.073  19.370  72.753  1.00 16.07 ? 653  LEU   B CB    1 
ATOM   13898 C  CG    . LEU   B  1  655  ? 11.438  19.452  71.370  1.00 17.26 ? 653  LEU   B CG    1 
ATOM   13899 C  CD1   . LEU   B  1  655  ? 10.527  20.659  71.318  1.00 18.48 ? 653  LEU   B CD1   1 
ATOM   13900 C  CD2   . LEU   B  1  655  ? 12.525  19.548  70.337  1.00 22.46 ? 653  LEU   B CD2   1 
ATOM   13901 N  N     . LEU   B  1  656  ? 12.801  17.790  75.396  1.00 17.74 ? 654  LEU   B N     1 
ATOM   13902 C  CA    . LEU   B  1  656  ? 13.321  17.774  76.763  1.00 18.82 ? 654  LEU   B CA    1 
ATOM   13903 C  C     . LEU   B  1  656  ? 14.589  16.966  76.837  1.00 17.64 ? 654  LEU   B C     1 
ATOM   13904 O  O     . LEU   B  1  656  ? 15.561  17.365  77.493  1.00 19.19 ? 654  LEU   B O     1 
ATOM   13905 C  CB    . LEU   B  1  656  ? 12.327  17.096  77.708  1.00 22.03 ? 654  LEU   B CB    1 
ATOM   13906 C  CG    . LEU   B  1  656  ? 10.974  17.723  77.887  1.00 26.83 ? 654  LEU   B CG    1 
ATOM   13907 C  CD1   . LEU   B  1  656  ? 10.259  17.041  79.022  1.00 21.43 ? 654  LEU   B CD1   1 
ATOM   13908 C  CD2   . LEU   B  1  656  ? 11.155  19.191  78.113  1.00 23.38 ? 654  LEU   B CD2   1 
ATOM   13909 N  N     . GLY   B  1  657  ? 14.569  15.788  76.234  1.00 18.62 ? 655  GLY   B N     1 
ATOM   13910 C  CA    . GLY   B  1  657  ? 15.719  14.919  76.301  1.00 22.48 ? 655  GLY   B CA    1 
ATOM   13911 C  C     . GLY   B  1  657  ? 16.944  15.580  75.727  1.00 20.15 ? 655  GLY   B C     1 
ATOM   13912 O  O     . GLY   B  1  657  ? 18.039  15.461  76.275  1.00 19.90 ? 655  GLY   B O     1 
ATOM   13913 N  N     . LEU   B  1  658  ? 16.778  16.293  74.615  1.00 18.06 ? 656  LEU   B N     1 
ATOM   13914 C  CA    . LEU   B  1  658  ? 17.918  16.972  74.029  1.00 15.57 ? 656  LEU   B CA    1 
ATOM   13915 C  C     . LEU   B  1  658  ? 18.401  18.101  74.922  1.00 17.33 ? 656  LEU   B C     1 
ATOM   13916 O  O     . LEU   B  1  658  ? 19.602  18.248  75.152  1.00 16.76 ? 656  LEU   B O     1 
ATOM   13917 C  CB    . LEU   B  1  658  ? 17.534  17.497  72.650  1.00 16.75 ? 656  LEU   B CB    1 
ATOM   13918 C  CG    . LEU   B  1  658  ? 18.689  18.142  71.892  1.00 16.09 ? 656  LEU   B CG    1 
ATOM   13919 C  CD1   . LEU   B  1  658  ? 19.902  17.216  71.766  1.00 17.45 ? 656  LEU   B CD1   1 
ATOM   13920 C  CD2   . LEU   B  1  658  ? 18.180  18.553  70.523  1.00 17.00 ? 656  LEU   B CD2   1 
ATOM   13921 N  N     . ILE   B  1  659  ? 17.484  18.895  75.461  1.00 15.21 ? 657  ILE   B N     1 
ATOM   13922 C  CA    . ILE   B  1  659  ? 17.881  20.014  76.303  1.00 14.85 ? 657  ILE   B CA    1 
ATOM   13923 C  C     . ILE   B  1  659  ? 18.576  19.521  77.560  1.00 15.28 ? 657  ILE   B C     1 
ATOM   13924 O  O     . ILE   B  1  659  ? 19.575  20.107  78.014  1.00 15.59 ? 657  ILE   B O     1 
ATOM   13925 C  CB    . ILE   B  1  659  ? 16.638  20.853  76.627  1.00 14.75 ? 657  ILE   B CB    1 
ATOM   13926 C  CG1   . ILE   B  1  659  ? 16.150  21.525  75.346  1.00 15.04 ? 657  ILE   B CG1   1 
ATOM   13927 C  CG2   . ILE   B  1  659  ? 16.930  21.872  77.705  1.00 16.29 ? 657  ILE   B CG2   1 
ATOM   13928 C  CD1   . ILE   B  1  659  ? 14.714  22.025  75.448  1.00 15.52 ? 657  ILE   B CD1   1 
ATOM   13929 N  N     . ILE   B  1  660  ? 18.048  18.452  78.154  1.00 15.60 ? 658  ILE   B N     1 
ATOM   13930 C  CA    . ILE   B  1  660  ? 18.646  17.896  79.365  1.00 15.45 ? 658  ILE   B CA    1 
ATOM   13931 C  C     . ILE   B  1  660  ? 20.101  17.546  79.119  1.00 16.55 ? 658  ILE   B C     1 
ATOM   13932 O  O     . ILE   B  1  660  ? 20.980  17.856  79.938  1.00 17.26 ? 658  ILE   B O     1 
ATOM   13933 C  CB    . ILE   B  1  660  ? 17.847  16.668  79.829  1.00 15.14 ? 658  ILE   B CB    1 
ATOM   13934 C  CG1   . ILE   B  1  660  ? 16.539  17.111  80.478  1.00 16.30 ? 658  ILE   B CG1   1 
ATOM   13935 C  CG2   . ILE   B  1  660  ? 18.675  15.815  80.799  1.00 17.22 ? 658  ILE   B CG2   1 
ATOM   13936 C  CD1   . ILE   B  1  660  ? 15.634  15.943  80.796  1.00 17.54 ? 658  ILE   B CD1   1 
ATOM   13937 N  N     . ARG   B  1  661  ? 20.376  16.893  77.993  1.00 15.78 ? 659  ARG   B N     1 
ATOM   13938 C  CA    . ARG   B  1  661  ? 21.708  16.372  77.738  1.00 15.00 ? 659  ARG   B CA    1 
ATOM   13939 C  C     . ARG   B  1  661  ? 22.632  17.419  77.136  1.00 16.60 ? 659  ARG   B C     1 
ATOM   13940 O  O     . ARG   B  1  661  ? 23.838  17.388  77.393  1.00 17.67 ? 659  ARG   B O     1 
ATOM   13941 C  CB    . ARG   B  1  661  ? 21.625  15.118  76.874  1.00 17.31 ? 659  ARG   B CB    1 
ATOM   13942 C  CG    . ARG   B  1  661  ? 21.129  13.926  77.672  1.00 18.61 ? 659  ARG   B CG    1 
ATOM   13943 C  CD    . ARG   B  1  661  ? 20.959  12.681  76.824  1.00 20.89 ? 659  ARG   B CD    1 
ATOM   13944 N  NE    . ARG   B  1  661  ? 22.190  12.256  76.160  1.00 20.69 ? 659  ARG   B NE    1 
ATOM   13945 C  CZ    . ARG   B  1  661  ? 22.330  12.163  74.845  1.00 21.46 ? 659  ARG   B CZ    1 
ATOM   13946 N  NH1   . ARG   B  1  661  ? 21.348  12.482  74.016  1.00 23.24 ? 659  ARG   B NH1   1 
ATOM   13947 N  NH2   . ARG   B  1  661  ? 23.484  11.723  74.341  1.00 22.24 ? 659  ARG   B NH2   1 
ATOM   13948 N  N     . GLU   B  1  662  ? 22.106  18.340  76.340  1.00 16.00 ? 660  GLU   B N     1 
ATOM   13949 C  CA    . GLU   B  1  662  ? 22.983  19.312  75.700  1.00 17.18 ? 660  GLU   B CA    1 
ATOM   13950 C  C     . GLU   B  1  662  ? 23.300  20.492  76.608  1.00 17.49 ? 660  GLU   B C     1 
ATOM   13951 O  O     . GLU   B  1  662  ? 24.427  20.993  76.599  1.00 17.22 ? 660  GLU   B O     1 
ATOM   13952 C  CB    . GLU   B  1  662  ? 22.352  19.812  74.395  1.00 18.51 ? 660  GLU   B CB    1 
ATOM   13953 C  CG    . GLU   B  1  662  ? 23.235  20.828  73.671  1.00 18.53 ? 660  GLU   B CG    1 
ATOM   13954 C  CD    . GLU   B  1  662  ? 22.679  21.322  72.336  1.00 18.07 ? 660  GLU   B CD    1 
ATOM   13955 O  OE1   . GLU   B  1  662  ? 21.449  21.505  72.199  1.00 19.40 ? 660  GLU   B OE1   1 
ATOM   13956 O  OE2   . GLU   B  1  662  ? 23.508  21.548  71.443  1.00 18.83 ? 660  GLU   B OE2   1 
ATOM   13957 N  N     . ALA   B  1  663  ? 22.334  20.947  77.402  1.00 15.92 ? 661  ALA   B N     1 
ATOM   13958 C  CA    . ALA   B  1  663  ? 22.479  22.198  78.124  1.00 16.26 ? 661  ALA   B CA    1 
ATOM   13959 C  C     . ALA   B  1  663  ? 22.528  22.019  79.629  1.00 17.88 ? 661  ALA   B C     1 
ATOM   13960 O  O     . ALA   B  1  663  ? 22.502  23.015  80.355  1.00 21.82 ? 661  ALA   B O     1 
ATOM   13961 C  CB    . ALA   B  1  663  ? 21.374  23.176  77.731  1.00 17.54 ? 661  ALA   B CB    1 
ATOM   13962 N  N     . GLY   B  1  664  ? 22.560  20.783  80.111  1.00 18.74 ? 662  GLY   B N     1 
ATOM   13963 C  CA    . GLY   B  1  664  ? 22.700  20.570  81.543  1.00 19.64 ? 662  GLY   B CA    1 
ATOM   13964 C  C     . GLY   B  1  664  ? 21.473  20.905  82.359  1.00 19.17 ? 662  GLY   B C     1 
ATOM   13965 O  O     . GLY   B  1  664  ? 21.594  21.221  83.545  1.00 20.12 ? 662  GLY   B O     1 
ATOM   13966 N  N     . LYS   B  1  665  ? 20.295  20.858  81.757  1.00 16.32 ? 663  LYS   B N     1 
ATOM   13967 C  CA    . LYS   B  1  665  ? 19.080  21.221  82.459  1.00 16.72 ? 663  LYS   B CA    1 
ATOM   13968 C  C     . LYS   B  1  665  ? 18.451  19.998  83.089  1.00 15.13 ? 663  LYS   B C     1 
ATOM   13969 O  O     . LYS   B  1  665  ? 18.522  18.889  82.557  1.00 16.38 ? 663  LYS   B O     1 
ATOM   13970 C  CB    . LYS   B  1  665  ? 18.059  21.807  81.488  1.00 17.09 ? 663  LYS   B CB    1 
ATOM   13971 C  CG    . LYS   B  1  665  ? 18.544  22.998  80.690  1.00 20.90 ? 663  LYS   B CG    1 
ATOM   13972 C  CD    . LYS   B  1  665  ? 19.005  24.122  81.585  1.00 20.82 ? 663  LYS   B CD    1 
ATOM   13973 C  CE    . LYS   B  1  665  ? 19.333  25.370  80.768  1.00 23.46 ? 663  LYS   B CE    1 
ATOM   13974 N  NZ    . LYS   B  1  665  ? 19.888  26.441  81.658  1.00 22.48 ? 663  LYS   B NZ    1 
ATOM   13975 N  N     . SER   B  1  666  ? 17.796  20.225  84.222  1.00 17.18 ? 664  SER   B N     1 
ATOM   13976 C  CA    . SER   B  1  666  ? 16.929  19.219  84.798  1.00 17.05 ? 664  SER   B CA    1 
ATOM   13977 C  C     . SER   B  1  666  ? 15.640  19.122  83.986  1.00 17.62 ? 664  SER   B C     1 
ATOM   13978 O  O     . SER   B  1  666  ? 15.305  19.990  83.173  1.00 18.14 ? 664  SER   B O     1 
ATOM   13979 C  CB    . SER   B  1  666  ? 16.543  19.629  86.210  1.00 19.54 ? 664  SER   B CB    1 
ATOM   13980 O  OG    . SER   B  1  666  ? 15.696  20.772  86.152  1.00 21.11 ? 664  SER   B OG    1 
ATOM   13981 N  N     . ALA   B  1  667  ? 14.897  18.049  84.230  1.00 17.10 ? 665  ALA   B N     1 
ATOM   13982 C  CA    . ALA   B  1  667  ? 13.650  17.851  83.504  1.00 17.33 ? 665  ALA   B CA    1 
ATOM   13983 C  C     . ALA   B  1  667  ? 12.690  19.013  83.712  1.00 17.62 ? 665  ALA   B C     1 
ATOM   13984 O  O     . ALA   B  1  667  ? 12.071  19.478  82.754  1.00 16.45 ? 665  ALA   B O     1 
ATOM   13985 C  CB    . ALA   B  1  667  ? 12.996  16.543  83.939  1.00 19.25 ? 665  ALA   B CB    1 
ATOM   13986 N  N     . LEU   B  1  668  ? 12.524  19.487  84.952  1.00 17.34 ? 666  LEU   B N     1 
ATOM   13987 C  CA    . LEU   B  1  668  ? 11.587  20.589  85.161  1.00 18.57 ? 666  LEU   B CA    1 
ATOM   13988 C  C     . LEU   B  1  668  ? 12.010  21.832  84.395  1.00 16.82 ? 666  LEU   B C     1 
ATOM   13989 O  O     . LEU   B  1  668  ? 11.170  22.546  83.832  1.00 16.15 ? 666  LEU   B O     1 
ATOM   13990 C  CB    . LEU   B  1  668  ? 11.434  20.921  86.646  1.00 19.86 ? 666  LEU   B CB    1 
ATOM   13991 C  CG    . LEU   B  1  668  ? 10.499  19.985  87.405  1.00 24.62 ? 666  LEU   B CG    1 
ATOM   13992 C  CD1   . LEU   B  1  668  ? 10.502  20.328  88.888  1.00 29.12 ? 666  LEU   B CD1   1 
ATOM   13993 C  CD2   . LEU   B  1  668  ? 9.086   20.059  86.832  1.00 27.04 ? 666  LEU   B CD2   1 
ATOM   13994 N  N     . ASN   B  1  669  ? 13.302  22.117  84.366  1.00 16.34 ? 667  ASN   B N     1 
ATOM   13995 C  CA    . ASN   B  1  669  ? 13.720  23.324  83.673  1.00 16.55 ? 667  ASN   B CA    1 
ATOM   13996 C  C     . ASN   B  1  669  ? 13.731  23.149  82.170  1.00 16.00 ? 667  ASN   B C     1 
ATOM   13997 O  O     . ASN   B  1  669  ? 13.559  24.135  81.443  1.00 16.88 ? 667  ASN   B O     1 
ATOM   13998 C  CB    . ASN   B  1  669  ? 15.027  23.837  84.251  1.00 21.22 ? 667  ASN   B CB    1 
ATOM   13999 C  CG    . ASN   B  1  669  ? 14.835  24.345  85.654  1.00 21.37 ? 667  ASN   B CG    1 
ATOM   14000 O  OD1   . ASN   B  1  669  ? 13.792  24.935  85.968  1.00 23.84 ? 667  ASN   B OD1   1 
ATOM   14001 N  ND2   . ASN   B  1  669  ? 15.789  24.070  86.519  1.00 24.72 ? 667  ASN   B ND2   1 
ATOM   14002 N  N     . ALA   B  1  670  ? 13.900  21.916  81.688  1.00 15.32 ? 668  ALA   B N     1 
ATOM   14003 C  CA    . ALA   B  1  670  ? 13.741  21.663  80.265  1.00 16.03 ? 668  ALA   B CA    1 
ATOM   14004 C  C     . ALA   B  1  670  ? 12.286  21.818  79.849  1.00 14.89 ? 668  ALA   B C     1 
ATOM   14005 O  O     . ALA   B  1  670  ? 11.999  22.361  78.780  1.00 14.76 ? 668  ALA   B O     1 
ATOM   14006 C  CB    . ALA   B  1  670  ? 14.261  20.267  79.914  1.00 16.52 ? 668  ALA   B CB    1 
ATOM   14007 N  N     . ILE   B  1  671  ? 11.350  21.351  80.683  1.00 14.50 ? 669  ILE   B N     1 
ATOM   14008 C  CA    . ILE   B  1  671  ? 9.935   21.610  80.428  1.00 14.54 ? 669  ILE   B CA    1 
ATOM   14009 C  C     . ILE   B  1  671  ? 9.681   23.102  80.345  1.00 14.58 ? 669  ILE   B C     1 
ATOM   14010 O  O     . ILE   B  1  671  ? 9.013   23.582  79.421  1.00 15.09 ? 669  ILE   B O     1 
ATOM   14011 C  CB    . ILE   B  1  671  ? 9.055   20.954  81.506  1.00 14.48 ? 669  ILE   B CB    1 
ATOM   14012 C  CG1   . ILE   B  1  671  ? 9.093   19.441  81.346  1.00 16.60 ? 669  ILE   B CG1   1 
ATOM   14013 C  CG2   . ILE   B  1  671  ? 7.632   21.472  81.369  1.00 16.49 ? 669  ILE   B CG2   1 
ATOM   14014 C  CD1   . ILE   B  1  671  ? 8.556   18.679  82.553  1.00 18.60 ? 669  ILE   B CD1   1 
ATOM   14015 N  N     . ALA   B  1  672  ? 10.192  23.855  81.313  1.00 14.22 ? 670  ALA   B N     1 
ATOM   14016 C  CA    . ALA   B  1  672  ? 9.993   25.299  81.303  1.00 15.37 ? 670  ALA   B CA    1 
ATOM   14017 C  C     . ALA   B  1  672  ? 10.569  25.919  80.044  1.00 15.40 ? 670  ALA   B C     1 
ATOM   14018 O  O     . ALA   B  1  672  ? 9.977   26.847  79.482  1.00 15.12 ? 670  ALA   B O     1 
ATOM   14019 C  CB    . ALA   B  1  672  ? 10.625  25.931  82.546  1.00 16.85 ? 670  ALA   B CB    1 
ATOM   14020 N  N     . GLU   B  1  673  ? 11.727  25.424  79.595  1.00 14.68 ? 671  GLU   B N     1 
ATOM   14021 C  CA    . GLU   B  1  673  ? 12.359  25.931  78.389  1.00 14.14 ? 671  GLU   B CA    1 
ATOM   14022 C  C     . GLU   B  1  673  ? 11.450  25.747  77.186  1.00 14.89 ? 671  GLU   B C     1 
ATOM   14023 O  O     . GLU   B  1  673  ? 11.251  26.677  76.395  1.00 15.04 ? 671  GLU   B O     1 
ATOM   14024 C  CB    . GLU   B  1  673  ? 13.650  25.152  78.167  1.00 15.71 ? 671  GLU   B CB    1 
ATOM   14025 C  CG    . GLU   B  1  673  ? 14.497  25.657  77.038  1.00 17.23 ? 671  GLU   B CG    1 
ATOM   14026 C  CD    . GLU   B  1  673  ? 15.271  26.904  77.381  1.00 18.39 ? 671  GLU   B CD    1 
ATOM   14027 O  OE1   . GLU   B  1  673  ? 15.529  27.190  78.588  1.00 18.84 ? 671  GLU   B OE1   1 
ATOM   14028 O  OE2   . GLU   B  1  673  ? 15.668  27.584  76.422  1.00 16.65 ? 671  GLU   B OE2   1 
ATOM   14029 N  N     . VAL   B  1  674  ? 10.917  24.538  77.011  1.00 13.34 ? 672  VAL   B N     1 
ATOM   14030 C  CA    . VAL   B  1  674  ? 10.071  24.281  75.852  1.00 13.37 ? 672  VAL   B CA    1 
ATOM   14031 C  C     . VAL   B  1  674  ? 8.767   25.056  75.963  1.00 14.01 ? 672  VAL   B C     1 
ATOM   14032 O  O     . VAL   B  1  674  ? 8.293   25.633  74.981  1.00 13.71 ? 672  VAL   B O     1 
ATOM   14033 C  CB    . VAL   B  1  674  ? 9.828   22.774  75.660  1.00 13.06 ? 672  VAL   B CB    1 
ATOM   14034 C  CG1   . VAL   B  1  674  ? 8.940   22.543  74.455  1.00 14.42 ? 672  VAL   B CG1   1 
ATOM   14035 C  CG2   . VAL   B  1  674  ? 11.138  22.044  75.473  1.00 15.19 ? 672  VAL   B CG2   1 
ATOM   14036 N  N     . ARG   B  1  675  ? 8.187   25.119  77.165  1.00 13.62 ? 673  ARG   B N     1 
ATOM   14037 C  CA    . ARG   B  1  675  ? 6.967   25.893  77.342  1.00 13.12 ? 673  ARG   B CA    1 
ATOM   14038 C  C     . ARG   B  1  675  ? 7.183   27.342  76.967  1.00 12.05 ? 673  ARG   B C     1 
ATOM   14039 O  O     . ARG   B  1  675  ? 6.343   27.943  76.298  1.00 13.08 ? 673  ARG   B O     1 
ATOM   14040 C  CB    . ARG   B  1  675  ? 6.481   25.817  78.778  1.00 13.32 ? 673  ARG   B CB    1 
ATOM   14041 C  CG    . ARG   B  1  675  ? 5.913   24.472  79.171  1.00 14.77 ? 673  ARG   B CG    1 
ATOM   14042 C  CD    . ARG   B  1  675  ? 5.267   24.591  80.547  1.00 14.53 ? 673  ARG   B CD    1 
ATOM   14043 N  NE    . ARG   B  1  675  ? 4.108   25.466  80.458  1.00 14.68 ? 673  ARG   B NE    1 
ATOM   14044 C  CZ    . ARG   B  1  675  ? 3.524   26.028  81.503  1.00 14.16 ? 673  ARG   B CZ    1 
ATOM   14045 N  NH1   . ARG   B  1  675  ? 3.983   25.844  82.727  1.00 16.73 ? 673  ARG   B NH1   1 
ATOM   14046 N  NH2   . ARG   B  1  675  ? 2.456   26.790  81.308  1.00 14.69 ? 673  ARG   B NH2   1 
ATOM   14047 N  N     . GLU   B  1  676  ? 8.317   27.908  77.358  1.00 12.81 ? 674  GLU   B N     1 
ATOM   14048 C  CA    . GLU   B  1  676  ? 8.583   29.303  77.054  1.00 12.08 ? 674  GLU   B CA    1 
ATOM   14049 C  C     . GLU   B  1  676  ? 8.686   29.532  75.557  1.00 12.92 ? 674  GLU   B C     1 
ATOM   14050 O  O     . GLU   B  1  676  ? 8.199   30.544  75.047  1.00 13.18 ? 674  GLU   B O     1 
ATOM   14051 C  CB    . GLU   B  1  676  ? 9.867   29.732  77.760  1.00 14.30 ? 674  GLU   B CB    1 
ATOM   14052 C  CG    . GLU   B  1  676  ? 10.165  31.209  77.635  1.00 13.99 ? 674  GLU   B CG    1 
ATOM   14053 C  CD    . GLU   B  1  676  ? 9.554   32.037  78.717  1.00 18.88 ? 674  GLU   B CD    1 
ATOM   14054 O  OE1   . GLU   B  1  676  ? 8.676   31.539  79.449  1.00 21.62 ? 674  GLU   B OE1   1 
ATOM   14055 O  OE2   . GLU   B  1  676  ? 9.960   33.209  78.842  1.00 18.68 ? 674  GLU   B OE2   1 
ATOM   14056 N  N     . ALA   B  1  677  ? 9.333   28.610  74.838  1.00 12.58 ? 675  ALA   B N     1 
ATOM   14057 C  CA    . ALA   B  1  677  ? 9.397   28.718  73.385  1.00 12.68 ? 675  ALA   B CA    1 
ATOM   14058 C  C     . ALA   B  1  677  ? 8.000   28.686  72.781  1.00 12.25 ? 675  ALA   B C     1 
ATOM   14059 O  O     . ALA   B  1  677  ? 7.669   29.504  71.917  1.00 13.53 ? 675  ALA   B O     1 
ATOM   14060 C  CB    . ALA   B  1  677  ? 10.247  27.577  72.832  1.00 13.49 ? 675  ALA   B CB    1 
ATOM   14061 N  N     . ILE   B  1  678  ? 7.159   27.764  73.256  1.00 12.51 ? 676  ILE   B N     1 
ATOM   14062 C  CA    . ILE   B  1  678  ? 5.783   27.674  72.783  1.00 12.74 ? 676  ILE   B CA    1 
ATOM   14063 C  C     . ILE   B  1  678  ? 5.052   28.972  73.055  1.00 12.75 ? 676  ILE   B C     1 
ATOM   14064 O  O     . ILE   B  1  678  ? 4.328   29.488  72.198  1.00 13.32 ? 676  ILE   B O     1 
ATOM   14065 C  CB    . ILE   B  1  678  ? 5.082   26.487  73.463  1.00 12.64 ? 676  ILE   B CB    1 
ATOM   14066 C  CG1   . ILE   B  1  678  ? 5.658   25.168  72.958  1.00 13.21 ? 676  ILE   B CG1   1 
ATOM   14067 C  CG2   . ILE   B  1  678  ? 3.538   26.547  73.290  1.00 14.04 ? 676  ILE   B CG2   1 
ATOM   14068 C  CD1   . ILE   B  1  678  ? 5.370   24.001  73.909  1.00 14.47 ? 676  ILE   B CD1   1 
ATOM   14069 N  N     . ASP   B  1  679  ? 5.225   29.520  74.249  1.00 12.64 ? 677  ASP   B N     1 
ATOM   14070 C  CA    . ASP   B  1  679  ? 4.544   30.751  74.603  1.00 12.71 ? 677  ASP   B CA    1 
ATOM   14071 C  C     . ASP   B  1  679  ? 5.037   31.928  73.781  1.00 12.71 ? 677  ASP   B C     1 
ATOM   14072 O  O     . ASP   B  1  679  ? 4.242   32.766  73.383  1.00 13.14 ? 677  ASP   B O     1 
ATOM   14073 C  CB    . ASP   B  1  679  ? 4.692   31.029  76.093  1.00 12.98 ? 677  ASP   B CB    1 
ATOM   14074 C  CG    . ASP   B  1  679  ? 3.939   30.035  76.948  1.00 15.28 ? 677  ASP   B CG    1 
ATOM   14075 O  OD1   . ASP   B  1  679  ? 2.853   29.584  76.542  1.00 15.95 ? 677  ASP   B OD1   1 
ATOM   14076 O  OD2   . ASP   B  1  679  ? 4.421   29.745  78.062  1.00 16.05 ? 677  ASP   B OD2   1 
ATOM   14077 N  N     . PHE   B  1  680  ? 6.340   32.019  73.518  1.00 13.03 ? 678  PHE   B N     1 
ATOM   14078 C  CA    . PHE   B  1  680  ? 6.801   33.078  72.624  1.00 12.59 ? 678  PHE   B CA    1 
ATOM   14079 C  C     . PHE   B  1  680  ? 6.131   32.965  71.271  1.00 13.31 ? 678  PHE   B C     1 
ATOM   14080 O  O     . PHE   B  1  680  ? 5.674   33.963  70.701  1.00 13.04 ? 678  PHE   B O     1 
ATOM   14081 C  CB    . PHE   B  1  680  ? 8.304   32.979  72.412  1.00 12.56 ? 678  PHE   B CB    1 
ATOM   14082 C  CG    . PHE   B  1  680  ? 9.143   33.634  73.480  1.00 12.07 ? 678  PHE   B CG    1 
ATOM   14083 C  CD1   . PHE   B  1  680  ? 8.888   34.928  73.911  1.00 12.76 ? 678  PHE   B CD1   1 
ATOM   14084 C  CD2   . PHE   B  1  680  ? 10.206  32.936  74.018  1.00 12.95 ? 678  PHE   B CD2   1 
ATOM   14085 C  CE1   . PHE   B  1  680  ? 9.719   35.517  74.886  1.00 13.47 ? 678  PHE   B CE1   1 
ATOM   14086 C  CE2   . PHE   B  1  680  ? 11.012  33.504  74.985  1.00 13.14 ? 678  PHE   B CE2   1 
ATOM   14087 C  CZ    . PHE   B  1  680  ? 10.777  34.791  75.415  1.00 14.00 ? 678  PHE   B CZ    1 
ATOM   14088 N  N     . LEU   B  1  681  ? 6.123   31.757  70.710  1.00 12.05 ? 679  LEU   B N     1 
ATOM   14089 C  CA    . LEU   B  1  681  ? 5.507   31.568  69.406  1.00 11.59 ? 679  LEU   B CA    1 
ATOM   14090 C  C     . LEU   B  1  681  ? 4.069   32.046  69.420  1.00 12.42 ? 679  LEU   B C     1 
ATOM   14091 O  O     . LEU   B  1  681  ? 3.644   32.803  68.544  1.00 13.52 ? 679  LEU   B O     1 
ATOM   14092 C  CB    . LEU   B  1  681  ? 5.586   30.095  69.007  1.00 13.00 ? 679  LEU   B CB    1 
ATOM   14093 C  CG    . LEU   B  1  681  ? 6.999   29.623  68.677  1.00 12.29 ? 679  LEU   B CG    1 
ATOM   14094 C  CD1   . LEU   B  1  681  ? 7.076   28.123  68.738  1.00 14.22 ? 679  LEU   B CD1   1 
ATOM   14095 C  CD2   . LEU   B  1  681  ? 7.398   30.134  67.301  1.00 13.30 ? 679  LEU   B CD2   1 
ATOM   14096 N  N     . ARG   B  1  682  ? 3.295   31.595  70.403  1.00 13.05 ? 680  ARG   B N     1 
ATOM   14097 C  CA    . ARG   B  1  682  ? 1.880   31.922  70.415  1.00 12.43 ? 680  ARG   B CA    1 
ATOM   14098 C  C     . ARG   B  1  682  ? 1.644   33.376  70.772  1.00 12.63 ? 680  ARG   B C     1 
ATOM   14099 O  O     . ARG   B  1  682  ? 0.687   33.984  70.288  1.00 13.18 ? 680  ARG   B O     1 
ATOM   14100 C  CB    . ARG   B  1  682  ? 1.140   30.997  71.362  1.00 13.21 ? 680  ARG   B CB    1 
ATOM   14101 C  CG    . ARG   B  1  682  ? 1.097   29.588  70.844  1.00 14.09 ? 680  ARG   B CG    1 
ATOM   14102 C  CD    . ARG   B  1  682  ? 0.433   28.717  71.875  1.00 14.96 ? 680  ARG   B CD    1 
ATOM   14103 N  NE    . ARG   B  1  682  ? 0.228   27.371  71.365  1.00 14.54 ? 680  ARG   B NE    1 
ATOM   14104 C  CZ    . ARG   B  1  682  ? 0.003   26.312  72.123  1.00 15.59 ? 680  ARG   B CZ    1 
ATOM   14105 N  NH1   . ARG   B  1  682  ? -0.041  26.404  73.439  1.00 16.16 ? 680  ARG   B NH1   1 
ATOM   14106 N  NH2   . ARG   B  1  682  ? -0.135  25.123  71.546  1.00 17.97 ? 680  ARG   B NH2   1 
ATOM   14107 N  N     . TYR   B  1  683  ? 2.481   33.937  71.630  1.00 12.49 ? 681  TYR   B N     1 
ATOM   14108 C  CA    . TYR   B  1  683  ? 2.311   35.331  72.011  1.00 13.23 ? 681  TYR   B CA    1 
ATOM   14109 C  C     . TYR   B  1  683  ? 2.631   36.257  70.847  1.00 12.78 ? 681  TYR   B C     1 
ATOM   14110 O  O     . TYR   B  1  683  ? 1.862   37.174  70.549  1.00 13.39 ? 681  TYR   B O     1 
ATOM   14111 C  CB    . TYR   B  1  683  ? 3.197   35.636  73.211  1.00 12.94 ? 681  TYR   B CB    1 
ATOM   14112 C  CG    . TYR   B  1  683  ? 3.151   37.082  73.624  1.00 12.42 ? 681  TYR   B CG    1 
ATOM   14113 C  CD1   . TYR   B  1  683  ? 2.085   37.583  74.348  1.00 14.10 ? 681  TYR   B CD1   1 
ATOM   14114 C  CD2   . TYR   B  1  683  ? 4.177   37.933  73.287  1.00 12.98 ? 681  TYR   B CD2   1 
ATOM   14115 C  CE1   . TYR   B  1  683  ? 2.047   38.903  74.727  1.00 13.87 ? 681  TYR   B CE1   1 
ATOM   14116 C  CE2   . TYR   B  1  683  ? 4.155   39.257  73.654  1.00 13.35 ? 681  TYR   B CE2   1 
ATOM   14117 C  CZ    . TYR   B  1  683  ? 3.086   39.734  74.378  1.00 12.80 ? 681  TYR   B CZ    1 
ATOM   14118 O  OH    . TYR   B  1  683  ? 3.064   41.064  74.725  1.00 16.27 ? 681  TYR   B OH    1 
ATOM   14119 N  N     . TYR   B  1  684  ? 3.768   36.036  70.175  1.00 12.21 ? 682  TYR   B N     1 
ATOM   14120 C  CA    . TYR   B  1  684  ? 4.071   36.912  69.051  1.00 12.71 ? 682  TYR   B CA    1 
ATOM   14121 C  C     . TYR   B  1  684  ? 3.085   36.709  67.912  1.00 13.67 ? 682  TYR   B C     1 
ATOM   14122 O  O     . TYR   B  1  684  ? 2.780   37.664  67.199  1.00 13.67 ? 682  TYR   B O     1 
ATOM   14123 C  CB    . TYR   B  1  684  ? 5.515   36.726  68.598  1.00 12.66 ? 682  TYR   B CB    1 
ATOM   14124 C  CG    . TYR   B  1  684  ? 6.514   37.107  69.651  1.00 12.16 ? 682  TYR   B CG    1 
ATOM   14125 C  CD1   . TYR   B  1  684  ? 6.349   38.254  70.405  1.00 13.47 ? 682  TYR   B CD1   1 
ATOM   14126 C  CD2   . TYR   B  1  684  ? 7.634   36.323  69.884  1.00 11.82 ? 682  TYR   B CD2   1 
ATOM   14127 C  CE1   . TYR   B  1  684  ? 7.274   38.604  71.393  1.00 13.59 ? 682  TYR   B CE1   1 
ATOM   14128 C  CE2   . TYR   B  1  684  ? 8.560   36.666  70.845  1.00 12.91 ? 682  TYR   B CE2   1 
ATOM   14129 C  CZ    . TYR   B  1  684  ? 8.379   37.797  71.600  1.00 12.82 ? 682  TYR   B CZ    1 
ATOM   14130 O  OH    . TYR   B  1  684  ? 9.301   38.104  72.574  1.00 13.19 ? 682  TYR   B OH    1 
ATOM   14131 N  N     . ALA   B  1  685  ? 2.539   35.500  67.760  1.00 12.75 ? 683  ALA   B N     1 
ATOM   14132 C  CA    . ALA   B  1  685  ? 1.478   35.289  66.779  1.00 12.62 ? 683  ALA   B CA    1 
ATOM   14133 C  C     . ALA   B  1  685  ? 0.264   36.132  67.128  1.00 14.38 ? 683  ALA   B C     1 
ATOM   14134 O  O     . ALA   B  1  685  ? -0.285  36.843  66.274  1.00 14.21 ? 683  ALA   B O     1 
ATOM   14135 C  CB    . ALA   B  1  685  ? 1.102   33.809  66.733  1.00 13.87 ? 683  ALA   B CB    1 
ATOM   14136 N  N     . GLU   B  1  686  ? -0.175  36.070  68.383  1.00 13.27 ? 684  GLU   B N     1 
ATOM   14137 C  CA    . GLU   B  1  686  ? -1.337  36.865  68.751  1.00 15.01 ? 684  GLU   B CA    1 
ATOM   14138 C  C     . GLU   B  1  686  ? -1.051  38.359  68.677  1.00 16.67 ? 684  GLU   B C     1 
ATOM   14139 O  O     . GLU   B  1  686  ? -1.884  39.124  68.175  1.00 15.08 ? 684  GLU   B O     1 
ATOM   14140 C  CB    . GLU   B  1  686  ? -1.835  36.476  70.129  1.00 16.96 ? 684  GLU   B CB    1 
ATOM   14141 C  CG    . GLU   B  1  686  ? -2.980  37.380  70.628  1.00 19.08 ? 684  GLU   B CG    1 
ATOM   14142 C  CD    . GLU   B  1  686  ? -4.276  37.290  69.814  1.00 21.73 ? 684  GLU   B CD    1 
ATOM   14143 O  OE1   . GLU   B  1  686  ? -4.440  36.418  68.922  1.00 20.79 ? 684  GLU   B OE1   1 
ATOM   14144 O  OE2   . GLU   B  1  686  ? -5.173  38.116  70.088  1.00 24.17 ? 684  GLU   B OE2   1 
ATOM   14145 N  N     . GLN   B  1  687  ? 0.118   38.800  69.147  1.00 13.43 ? 685  GLN   B N     1 
ATOM   14146 C  CA    . GLN   B  1  687  ? 0.415   40.223  69.042  1.00 14.56 ? 685  GLN   B CA    1 
ATOM   14147 C  C     . GLN   B  1  687  ? 0.426   40.671  67.593  1.00 15.04 ? 685  GLN   B C     1 
ATOM   14148 O  O     . GLN   B  1  687  ? -0.036  41.772  67.273  1.00 15.41 ? 685  GLN   B O     1 
ATOM   14149 C  CB    . GLN   B  1  687  ? 1.751   40.535  69.706  1.00 14.45 ? 685  GLN   B CB    1 
ATOM   14150 C  CG    . GLN   B  1  687  ? 1.707   40.336  71.224  1.00 15.13 ? 685  GLN   B CG    1 
ATOM   14151 C  CD    . GLN   B  1  687  ? 0.668   41.226  71.882  1.00 16.56 ? 685  GLN   B CD    1 
ATOM   14152 O  OE1   . GLN   B  1  687  ? 0.709   42.447  71.739  1.00 16.89 ? 685  GLN   B OE1   1 
ATOM   14153 N  NE2   . GLN   B  1  687  ? -0.282  40.616  72.600  1.00 20.25 ? 685  GLN   B NE2   1 
ATOM   14154 N  N     . THR   B  1  688  ? 0.903   39.808  66.694  1.00 13.19 ? 686  THR   B N     1 
ATOM   14155 C  CA    . THR   B  1  688  ? 0.845   40.123  65.274  1.00 14.69 ? 686  THR   B CA    1 
ATOM   14156 C  C     . THR   B  1  688  ? -0.589  40.294  64.811  1.00 14.37 ? 686  THR   B C     1 
ATOM   14157 O  O     . THR   B  1  688  ? -0.918  41.271  64.132  1.00 15.34 ? 686  THR   B O     1 
ATOM   14158 C  CB    . THR   B  1  688  ? 1.525   39.026  64.478  1.00 13.28 ? 686  THR   B CB    1 
ATOM   14159 O  OG1   . THR   B  1  688  ? 2.915   39.083  64.771  1.00 14.91 ? 686  THR   B OG1   1 
ATOM   14160 C  CG2   . THR   B  1  688  ? 1.318   39.267  62.996  1.00 15.52 ? 686  THR   B CG2   1 
ATOM   14161 N  N     . ARG   B  1  689  ? -1.452  39.344  65.155  1.00 13.98 ? 687  ARG   B N     1 
ATOM   14162 C  CA    . ARG   B  1  689  ? -2.853  39.442  64.743  1.00 14.35 ? 687  ARG   B CA    1 
ATOM   14163 C  C     . ARG   B  1  689  ? -3.524  40.687  65.294  1.00 15.17 ? 687  ARG   B C     1 
ATOM   14164 O  O     . ARG   B  1  689  ? -4.485  41.185  64.700  1.00 17.45 ? 687  ARG   B O     1 
ATOM   14165 C  CB    . ARG   B  1  689  ? -3.613  38.189  65.176  1.00 15.94 ? 687  ARG   B CB    1 
ATOM   14166 C  CG    . ARG   B  1  689  ? -3.209  36.946  64.397  1.00 18.21 ? 687  ARG   B CG    1 
ATOM   14167 C  CD    . ARG   B  1  689  ? -4.120  35.801  64.756  1.00 17.96 ? 687  ARG   B CD    1 
ATOM   14168 N  NE    . ARG   B  1  689  ? -3.948  35.390  66.139  1.00 18.81 ? 687  ARG   B NE    1 
ATOM   14169 C  CZ    . ARG   B  1  689  ? -3.184  34.379  66.527  1.00 19.77 ? 687  ARG   B CZ    1 
ATOM   14170 N  NH1   . ARG   B  1  689  ? -2.496  33.663  65.651  1.00 18.85 ? 687  ARG   B NH1   1 
ATOM   14171 N  NH2   . ARG   B  1  689  ? -3.129  34.068  67.817  1.00 19.07 ? 687  ARG   B NH2   1 
ATOM   14172 N  N     . ARG   B  1  690  ? -3.062  41.193  66.430  1.00 15.25 ? 688  ARG   B N     1 
ATOM   14173 C  CA    . ARG   B  1  690  ? -3.635  42.404  66.992  1.00 14.59 ? 688  ARG   B CA    1 
ATOM   14174 C  C     . ARG   B  1  690  ? -3.109  43.676  66.353  1.00 15.76 ? 688  ARG   B C     1 
ATOM   14175 O  O     . ARG   B  1  690  ? -3.742  44.726  66.514  1.00 16.37 ? 688  ARG   B O     1 
ATOM   14176 C  CB    . ARG   B  1  690  ? -3.303  42.478  68.485  1.00 16.57 ? 688  ARG   B CB    1 
ATOM   14177 C  CG    . ARG   B  1  690  ? -3.936  41.385  69.317  1.00 17.12 ? 688  ARG   B CG    1 
ATOM   14178 C  CD    . ARG   B  1  690  ? -5.445  41.618  69.543  1.00 21.09 ? 688  ARG   B CD    1 
ATOM   14179 N  NE    . ARG   B  1  690  ? -5.708  42.874  70.245  1.00 24.05 ? 688  ARG   B NE    1 
ATOM   14180 C  CZ    . ARG   B  1  690  ? -6.317  43.922  69.713  1.00 23.95 ? 688  ARG   B CZ    1 
ATOM   14181 N  NH1   . ARG   B  1  690  ? -6.824  43.881  68.490  1.00 23.62 ? 688  ARG   B NH1   1 
ATOM   14182 N  NH2   . ARG   B  1  690  ? -6.450  45.031  70.438  1.00 21.88 ? 688  ARG   B NH2   1 
ATOM   14183 N  N     . THR   B  1  691  ? -1.960  43.633  65.685  1.00 15.54 ? 689  THR   B N     1 
ATOM   14184 C  CA    . THR   B  1  691  ? -1.328  44.904  65.336  1.00 16.08 ? 689  THR   B CA    1 
ATOM   14185 C  C     . THR   B  1  691  ? -0.924  45.070  63.880  1.00 16.32 ? 689  THR   B C     1 
ATOM   14186 O  O     . THR   B  1  691  ? -1.110  46.152  63.334  1.00 19.82 ? 689  THR   B O     1 
ATOM   14187 C  CB    . THR   B  1  691  ? -0.083  45.141  66.195  1.00 15.32 ? 689  THR   B CB    1 
ATOM   14188 O  OG1   . THR   B  1  691  ? 0.823   44.033  66.054  1.00 17.04 ? 689  THR   B OG1   1 
ATOM   14189 C  CG2   . THR   B  1  691  ? -0.464  45.332  67.645  1.00 18.65 ? 689  THR   B CG2   1 
ATOM   14190 N  N     . LEU   B  1  692  ? -0.315  44.068  63.254  1.00 15.03 ? 690  LEU   B N     1 
ATOM   14191 C  CA    . LEU   B  1  692  ? 0.444   44.359  62.044  1.00 15.91 ? 690  LEU   B CA    1 
ATOM   14192 C  C     . LEU   B  1  692  ? -0.450  44.504  60.820  1.00 16.77 ? 690  LEU   B C     1 
ATOM   14193 O  O     . LEU   B  1  692  ? -1.289  43.648  60.546  1.00 18.92 ? 690  LEU   B O     1 
ATOM   14194 C  CB    . LEU   B  1  692  ? 1.505   43.294  61.796  1.00 16.54 ? 690  LEU   B CB    1 
ATOM   14195 C  CG    . LEU   B  1  692  ? 2.581   43.252  62.882  1.00 18.40 ? 690  LEU   B CG    1 
ATOM   14196 C  CD1   . LEU   B  1  692  ? 3.703   42.322  62.447  1.00 20.99 ? 690  LEU   B CD1   1 
ATOM   14197 C  CD2   . LEU   B  1  692  ? 3.130   44.630  63.221  1.00 19.85 ? 690  LEU   B CD2   1 
ATOM   14198 N  N     . GLY   B  1  693  ? -0.251  45.599  60.104  1.00 16.89 ? 691  GLY   B N     1 
ATOM   14199 C  CA    . GLY   B  1  693  ? -0.964  45.891  58.892  1.00 18.08 ? 691  GLY   B CA    1 
ATOM   14200 C  C     . GLY   B  1  693  ? 0.005   46.294  57.804  1.00 20.11 ? 691  GLY   B C     1 
ATOM   14201 O  O     . GLY   B  1  693  ? 1.231   46.262  57.966  1.00 20.29 ? 691  GLY   B O     1 
ATOM   14202 N  N     . PRO   B  1  694  ? -0.544  46.710  56.669  1.00 19.89 ? 692  PRO   B N     1 
ATOM   14203 C  CA    . PRO   B  1  694  ? 0.305   46.914  55.484  1.00 21.26 ? 692  PRO   B CA    1 
ATOM   14204 C  C     . PRO   B  1  694  ? 1.364   47.981  55.665  1.00 21.93 ? 692  PRO   B C     1 
ATOM   14205 O  O     . PRO   B  1  694  ? 2.440   47.883  55.059  1.00 26.89 ? 692  PRO   B O     1 
ATOM   14206 C  CB    . PRO   B  1  694  ? -0.700  47.252  54.370  1.00 25.57 ? 692  PRO   B CB    1 
ATOM   14207 C  CG    . PRO   B  1  694  ? -2.019  47.486  55.056  1.00 28.09 ? 692  PRO   B CG    1 
ATOM   14208 C  CD    . PRO   B  1  694  ? -1.986  46.795  56.383  1.00 21.35 ? 692  PRO   B CD    1 
ATOM   14209 N  N     . GLY   B  1  695  ? 1.113   48.987  56.491  1.00 22.22 ? 693  GLY   B N     1 
ATOM   14210 C  CA    . GLY   B  1  695  ? 2.056   50.055  56.707  1.00 21.96 ? 693  GLY   B CA    1 
ATOM   14211 C  C     . GLY   B  1  695  ? 3.147   49.759  57.708  1.00 21.85 ? 693  GLY   B C     1 
ATOM   14212 O  O     . GLY   B  1  695  ? 3.991   50.624  57.966  1.00 25.92 ? 693  GLY   B O     1 
ATOM   14213 N  N     . HIS   B  1  696  ? 3.157   48.568  58.310  1.00 21.60 ? 694  HIS   B N     1 
ATOM   14214 C  CA    . HIS   B  1  696  ? 4.227   48.194  59.237  1.00 19.26 ? 694  HIS   B CA    1 
ATOM   14215 C  C     . HIS   B  1  696  ? 5.201   47.289  58.498  1.00 18.79 ? 694  HIS   B C     1 
ATOM   14216 O  O     . HIS   B  1  696  ? 5.194   46.069  58.634  1.00 24.93 ? 694  HIS   B O     1 
ATOM   14217 C  CB    . HIS   B  1  696  ? 3.648   47.519  60.467  1.00 19.40 ? 694  HIS   B CB    1 
ATOM   14218 C  CG    . HIS   B  1  696  ? 2.543   48.299  61.086  1.00 18.86 ? 694  HIS   B CG    1 
ATOM   14219 N  ND1   . HIS   B  1  696  ? 1.253   47.826  61.151  1.00 18.86 ? 694  HIS   B ND1   1 
ATOM   14220 C  CD2   . HIS   B  1  696  ? 2.521   49.543  61.615  1.00 19.06 ? 694  HIS   B CD2   1 
ATOM   14221 C  CE1   . HIS   B  1  696  ? 0.487   48.736  61.725  1.00 18.45 ? 694  HIS   B CE1   1 
ATOM   14222 N  NE2   . HIS   B  1  696  ? 1.228   49.792  62.002  1.00 20.39 ? 694  HIS   B NE2   1 
ATOM   14223 N  N     . GLY   B  1  697  ? 6.047   47.918  57.696  1.00 21.24 ? 695  GLY   B N     1 
ATOM   14224 C  CA    . GLY   B  1  697  ? 6.957   47.193  56.840  1.00 19.74 ? 695  GLY   B CA    1 
ATOM   14225 C  C     . GLY   B  1  697  ? 8.091   46.576  57.623  1.00 17.92 ? 695  GLY   B C     1 
ATOM   14226 O  O     . GLY   B  1  697  ? 8.543   47.117  58.627  1.00 19.64 ? 695  GLY   B O     1 
ATOM   14227 N  N     . PRO   B  1  698  ? 8.587   45.436  57.172  1.00 19.98 ? 696  PRO   B N     1 
ATOM   14228 C  CA    . PRO   B  1  698  ? 9.709   44.809  57.875  1.00 17.61 ? 696  PRO   B CA    1 
ATOM   14229 C  C     . PRO   B  1  698  ? 10.999  45.587  57.675  1.00 17.71 ? 696  PRO   B C     1 
ATOM   14230 O  O     . PRO   B  1  698  ? 11.148  46.404  56.761  1.00 19.00 ? 696  PRO   B O     1 
ATOM   14231 C  CB    . PRO   B  1  698  ? 9.815   43.429  57.224  1.00 22.53 ? 696  PRO   B CB    1 
ATOM   14232 C  CG    . PRO   B  1  698  ? 9.295   43.652  55.854  1.00 28.96 ? 696  PRO   B CG    1 
ATOM   14233 C  CD    . PRO   B  1  698  ? 8.142   44.631  56.025  1.00 24.00 ? 696  PRO   B CD    1 
ATOM   14234 N  N     . LEU   B  1  699  ? 11.944  45.329  58.576  1.00 16.28 ? 697  LEU   B N     1 
ATOM   14235 C  CA    . LEU   B  1  699  ? 13.280  45.903  58.413  1.00 16.56 ? 697  LEU   B CA    1 
ATOM   14236 C  C     . LEU   B  1  699  ? 14.025  45.268  57.251  1.00 16.21 ? 697  LEU   B C     1 
ATOM   14237 O  O     . LEU   B  1  699  ? 14.733  45.960  56.515  1.00 18.57 ? 697  LEU   B O     1 
ATOM   14238 C  CB    . LEU   B  1  699  ? 14.086  45.694  59.686  1.00 17.07 ? 697  LEU   B CB    1 
ATOM   14239 C  CG    . LEU   B  1  699  ? 13.486  46.315  60.943  1.00 17.94 ? 697  LEU   B CG    1 
ATOM   14240 C  CD1   . LEU   B  1  699  ? 14.351  45.930  62.124  1.00 18.88 ? 697  LEU   B CD1   1 
ATOM   14241 C  CD2   . LEU   B  1  699  ? 13.410  47.818  60.796  1.00 22.60 ? 697  LEU   B CD2   1 
ATOM   14242 N  N     . GLY   B  1  700  ? 13.912  43.952  57.098  1.00 15.90 ? 698  GLY   B N     1 
ATOM   14243 C  CA    . GLY   B  1  700  ? 14.768  43.194  56.215  1.00 16.31 ? 698  GLY   B CA    1 
ATOM   14244 C  C     . GLY   B  1  700  ? 15.450  42.089  57.001  1.00 15.72 ? 698  GLY   B C     1 
ATOM   14245 O  O     . GLY   B  1  700  ? 14.997  41.709  58.081  1.00 16.19 ? 698  GLY   B O     1 
ATOM   14246 N  N     . PRO   B  1  701  ? 16.558  41.560  56.492  1.00 15.52 ? 699  PRO   B N     1 
ATOM   14247 C  CA    . PRO   B  1  701  ? 17.218  40.438  57.173  1.00 15.44 ? 699  PRO   B CA    1 
ATOM   14248 C  C     . PRO   B  1  701  ? 17.605  40.817  58.590  1.00 14.87 ? 699  PRO   B C     1 
ATOM   14249 O  O     . PRO   B  1  701  ? 18.266  41.829  58.826  1.00 16.27 ? 699  PRO   B O     1 
ATOM   14250 C  CB    . PRO   B  1  701  ? 18.458  40.175  56.310  1.00 16.47 ? 699  PRO   B CB    1 
ATOM   14251 C  CG    . PRO   B  1  701  ? 18.053  40.678  54.946  1.00 18.53 ? 699  PRO   B CG    1 
ATOM   14252 C  CD    . PRO   B  1  701  ? 17.252  41.919  55.247  1.00 16.76 ? 699  PRO   B CD    1 
ATOM   14253 N  N     . ILE   B  1  702  ? 17.183  39.995  59.537  1.00 13.89 ? 700  ILE   B N     1 
ATOM   14254 C  CA    A ILE   B  1  702  ? 17.509  40.209  60.937  0.66 14.45 ? 700  ILE   B CA    1 
ATOM   14255 C  CA    B ILE   B  1  702  ? 17.485  40.198  60.948  0.34 14.44 ? 700  ILE   B CA    1 
ATOM   14256 C  C     . ILE   B  1  702  ? 18.419  39.089  61.398  1.00 14.82 ? 700  ILE   B C     1 
ATOM   14257 O  O     . ILE   B  1  702  ? 18.146  37.905  61.166  1.00 14.58 ? 700  ILE   B O     1 
ATOM   14258 C  CB    A ILE   B  1  702  ? 16.255  40.309  61.812  0.66 12.94 ? 700  ILE   B CB    1 
ATOM   14259 C  CB    B ILE   B  1  702  ? 16.209  40.200  61.804  0.34 13.03 ? 700  ILE   B CB    1 
ATOM   14260 C  CG1   A ILE   B  1  702  ? 15.564  41.642  61.539  0.66 15.31 ? 700  ILE   B CG1   1 
ATOM   14261 C  CG1   B ILE   B  1  702  ? 15.244  41.273  61.310  0.34 13.40 ? 700  ILE   B CG1   1 
ATOM   14262 C  CG2   A ILE   B  1  702  ? 16.633  40.129  63.279  0.66 13.95 ? 700  ILE   B CG2   1 
ATOM   14263 C  CG2   B ILE   B  1  702  ? 16.565  40.403  63.270  0.34 14.34 ? 700  ILE   B CG2   1 
ATOM   14264 C  CD1   A ILE   B  1  702  ? 14.302  41.838  62.325  0.66 13.42 ? 700  ILE   B CD1   1 
ATOM   14265 C  CD1   B ILE   B  1  702  ? 15.819  42.655  61.314  0.34 16.76 ? 700  ILE   B CD1   1 
ATOM   14266 N  N     . VAL   B  1  703  ? 19.507  39.467  62.036  1.00 13.74 ? 701  VAL   B N     1 
ATOM   14267 C  CA    . VAL   B  1  703  ? 20.435  38.515  62.612  1.00 15.03 ? 701  VAL   B CA    1 
ATOM   14268 C  C     . VAL   B  1  703  ? 20.018  38.310  64.059  1.00 13.39 ? 701  VAL   B C     1 
ATOM   14269 O  O     . VAL   B  1  703  ? 19.908  39.277  64.817  1.00 13.78 ? 701  VAL   B O     1 
ATOM   14270 C  CB    . VAL   B  1  703  ? 21.859  39.067  62.520  1.00 14.47 ? 701  VAL   B CB    1 
ATOM   14271 C  CG1   . VAL   B  1  703  ? 22.824  38.222  63.347  1.00 15.35 ? 701  VAL   B CG1   1 
ATOM   14272 C  CG2   . VAL   B  1  703  ? 22.278  39.109  61.063  1.00 15.14 ? 701  VAL   B CG2   1 
ATOM   14273 N  N     . CYS   B  1  704  ? 19.742  37.068  64.431  1.00 13.24 ? 702  CYS   B N     1 
ATOM   14274 C  CA    . CYS   B  1  704  ? 19.311  36.736  65.779  1.00 13.08 ? 702  CYS   B CA    1 
ATOM   14275 C  C     . CYS   B  1  704  ? 20.427  35.947  66.424  1.00 13.54 ? 702  CYS   B C     1 
ATOM   14276 O  O     . CYS   B  1  704  ? 20.747  34.846  65.971  1.00 13.75 ? 702  CYS   B O     1 
ATOM   14277 C  CB    . CYS   B  1  704  ? 18.026  35.914  65.760  1.00 13.29 ? 702  CYS   B CB    1 
ATOM   14278 S  SG    . CYS   B  1  704  ? 16.632  36.785  65.052  1.00 14.15 ? 702  CYS   B SG    1 
ATOM   14279 N  N     . ILE   B  1  705  ? 21.021  36.518  67.468  1.00 13.34 ? 703  ILE   B N     1 
ATOM   14280 C  CA    . ILE   B  1  705  ? 22.153  35.918  68.155  1.00 13.37 ? 703  ILE   B CA    1 
ATOM   14281 C  C     . ILE   B  1  705  ? 21.699  35.631  69.575  1.00 13.17 ? 703  ILE   B C     1 
ATOM   14282 O  O     . ILE   B  1  705  ? 21.191  36.525  70.259  1.00 13.72 ? 703  ILE   B O     1 
ATOM   14283 C  CB    . ILE   B  1  705  ? 23.367  36.857  68.123  1.00 14.02 ? 703  ILE   B CB    1 
ATOM   14284 C  CG1   . ILE   B  1  705  ? 23.917  36.931  66.703  1.00 14.80 ? 703  ILE   B CG1   1 
ATOM   14285 C  CG2   . ILE   B  1  705  ? 24.418  36.364  69.087  1.00 14.24 ? 703  ILE   B CG2   1 
ATOM   14286 C  CD1   . ILE   B  1  705  ? 24.867  38.087  66.508  1.00 15.76 ? 703  ILE   B CD1   1 
ATOM   14287 N  N     . SER   B  1  706  ? 21.844  34.388  69.999  1.00 13.87 ? 704  SER   B N     1 
ATOM   14288 C  CA    . SER   B  1  706  ? 21.205  33.937  71.221  1.00 15.42 ? 704  SER   B CA    1 
ATOM   14289 C  C     . SER   B  1  706  ? 22.210  33.297  72.158  1.00 13.16 ? 704  SER   B C     1 
ATOM   14290 O  O     . SER   B  1  706  ? 23.281  32.853  71.735  1.00 14.45 ? 704  SER   B O     1 
ATOM   14291 C  CB    . SER   B  1  706  ? 20.079  32.950  70.880  1.00 13.41 ? 704  SER   B CB    1 
ATOM   14292 O  OG    . SER   B  1  706  ? 20.542  31.893  70.055  1.00 13.72 ? 704  SER   B OG    1 
ATOM   14293 N  N     . PRO   B  1  707  ? 21.893  33.255  73.442  1.00 13.30 ? 705  PRO   B N     1 
ATOM   14294 C  CA    . PRO   B  1  707  ? 22.807  32.721  74.448  1.00 13.98 ? 705  PRO   B CA    1 
ATOM   14295 C  C     . PRO   B  1  707  ? 22.591  31.224  74.621  1.00 14.27 ? 705  PRO   B C     1 
ATOM   14296 O  O     . PRO   B  1  707  ? 21.596  30.653  74.169  1.00 14.92 ? 705  PRO   B O     1 
ATOM   14297 C  CB    . PRO   B  1  707  ? 22.340  33.465  75.705  1.00 15.42 ? 705  PRO   B CB    1 
ATOM   14298 C  CG    . PRO   B  1  707  ? 20.856  33.569  75.525  1.00 15.04 ? 705  PRO   B CG    1 
ATOM   14299 C  CD    . PRO   B  1  707  ? 20.678  33.838  74.043  1.00 15.32 ? 705  PRO   B CD    1 
ATOM   14300 N  N     . TRP   B  1  708  ? 23.535  30.589  75.306  1.00 13.36 ? 706  TRP   B N     1 
ATOM   14301 C  CA    . TRP   B  1  708  ? 23.399  29.147  75.465  1.00 14.54 ? 706  TRP   B CA    1 
ATOM   14302 C  C     . TRP   B  1  708  ? 22.394  28.769  76.536  1.00 14.88 ? 706  TRP   B C     1 
ATOM   14303 O  O     . TRP   B  1  708  ? 21.895  27.648  76.522  1.00 15.61 ? 706  TRP   B O     1 
ATOM   14304 C  CB    . TRP   B  1  708  ? 24.746  28.488  75.808  1.00 13.66 ? 706  TRP   B CB    1 
ATOM   14305 C  CG    . TRP   B  1  708  ? 25.151  28.751  77.218  1.00 13.69 ? 706  TRP   B CG    1 
ATOM   14306 C  CD1   . TRP   B  1  708  ? 25.927  29.771  77.671  1.00 18.41 ? 706  TRP   B CD1   1 
ATOM   14307 C  CD2   . TRP   B  1  708  ? 24.732  28.007  78.365  1.00 15.55 ? 706  TRP   B CD2   1 
ATOM   14308 N  NE1   . TRP   B  1  708  ? 26.012  29.708  79.042  1.00 16.64 ? 706  TRP   B NE1   1 
ATOM   14309 C  CE2   . TRP   B  1  708  ? 25.293  28.627  79.486  1.00 15.01 ? 706  TRP   B CE2   1 
ATOM   14310 C  CE3   . TRP   B  1  708  ? 23.952  26.860  78.542  1.00 16.47 ? 706  TRP   B CE3   1 
ATOM   14311 C  CZ2   . TRP   B  1  708  ? 25.093  28.149  80.773  1.00 16.27 ? 706  TRP   B CZ2   1 
ATOM   14312 C  CZ3   . TRP   B  1  708  ? 23.747  26.383  79.819  1.00 15.63 ? 706  TRP   B CZ3   1 
ATOM   14313 C  CH2   . TRP   B  1  708  ? 24.313  27.027  80.917  1.00 16.26 ? 706  TRP   B CH2   1 
ATOM   14314 N  N     . ASN   B  1  709  ? 22.111  29.658  77.487  1.00 13.74 ? 707  ASN   B N     1 
ATOM   14315 C  CA    . ASN   B  1  709  ? 21.562  29.188  78.751  1.00 14.03 ? 707  ASN   B CA    1 
ATOM   14316 C  C     . ASN   B  1  709  ? 20.071  28.962  78.712  1.00 15.77 ? 707  ASN   B C     1 
ATOM   14317 O  O     . ASN   B  1  709  ? 19.567  28.183  79.520  1.00 16.67 ? 707  ASN   B O     1 
ATOM   14318 C  CB    . ASN   B  1  709  ? 21.918  30.152  79.875  1.00 14.58 ? 707  ASN   B CB    1 
ATOM   14319 C  CG    . ASN   B  1  709  ? 21.150  31.439  79.776  1.00 14.02 ? 707  ASN   B CG    1 
ATOM   14320 O  OD1   . ASN   B  1  709  ? 21.393  32.247  78.882  1.00 17.91 ? 707  ASN   B OD1   1 
ATOM   14321 N  ND2   . ASN   B  1  709  ? 20.196  31.636  80.685  1.00 16.59 ? 707  ASN   B ND2   1 
ATOM   14322 N  N     . PHE   B  1  710  ? 19.368  29.614  77.792  1.00 15.07 ? 708  PHE   B N     1 
ATOM   14323 C  CA    . PHE   B  1  710  ? 17.981  29.308  77.479  1.00 15.59 ? 708  PHE   B CA    1 
ATOM   14324 C  C     . PHE   B  1  710  ? 18.017  28.937  76.007  1.00 15.43 ? 708  PHE   B C     1 
ATOM   14325 O  O     . PHE   B  1  710  ? 17.614  29.725  75.141  1.00 15.65 ? 708  PHE   B O     1 
ATOM   14326 C  CB    . PHE   B  1  710  ? 17.057  30.493  77.743  1.00 15.71 ? 708  PHE   B CB    1 
ATOM   14327 C  CG    . PHE   B  1  710  ? 16.984  30.915  79.192  1.00 16.14 ? 708  PHE   B CG    1 
ATOM   14328 C  CD1   . PHE   B  1  710  ? 16.901  29.980  80.220  1.00 18.84 ? 708  PHE   B CD1   1 
ATOM   14329 C  CD2   . PHE   B  1  710  ? 16.974  32.253  79.513  1.00 17.45 ? 708  PHE   B CD2   1 
ATOM   14330 C  CE1   . PHE   B  1  710  ? 16.812  30.387  81.542  1.00 18.32 ? 708  PHE   B CE1   1 
ATOM   14331 C  CE2   . PHE   B  1  710  ? 16.880  32.675  80.830  1.00 18.35 ? 708  PHE   B CE2   1 
ATOM   14332 C  CZ    . PHE   B  1  710  ? 16.805  31.738  81.849  1.00 17.95 ? 708  PHE   B CZ    1 
ATOM   14333 N  N     . PRO   B  1  711  ? 18.508  27.738  75.694  1.00 14.63 ? 709  PRO   B N     1 
ATOM   14334 C  CA    . PRO   B  1  711  ? 18.963  27.447  74.327  1.00 15.34 ? 709  PRO   B CA    1 
ATOM   14335 C  C     . PRO   B  1  711  ? 17.850  27.229  73.322  1.00 14.92 ? 709  PRO   B C     1 
ATOM   14336 O  O     . PRO   B  1  711  ? 18.122  27.232  72.117  1.00 15.18 ? 709  PRO   B O     1 
ATOM   14337 C  CB    . PRO   B  1  711  ? 19.783  26.164  74.512  1.00 16.64 ? 709  PRO   B CB    1 
ATOM   14338 C  CG    . PRO   B  1  711  ? 19.096  25.488  75.668  1.00 17.82 ? 709  PRO   B CG    1 
ATOM   14339 C  CD    . PRO   B  1  711  ? 18.785  26.622  76.616  1.00 15.41 ? 709  PRO   B CD    1 
ATOM   14340 N  N     . LEU   B  1  712  ? 16.628  26.986  73.766  1.00 13.80 ? 710  LEU   B N     1 
ATOM   14341 C  CA    . LEU   B  1  712  ? 15.505  26.951  72.850  1.00 14.56 ? 710  LEU   B CA    1 
ATOM   14342 C  C     . LEU   B  1  712  ? 14.598  28.144  73.024  1.00 13.78 ? 710  LEU   B C     1 
ATOM   14343 O  O     . LEU   B  1  712  ? 14.086  28.666  72.042  1.00 14.66 ? 710  LEU   B O     1 
ATOM   14344 C  CB    . LEU   B  1  712  ? 14.702  25.659  73.036  1.00 14.57 ? 710  LEU   B CB    1 
ATOM   14345 C  CG    . LEU   B  1  712  ? 13.520  25.515  72.082  1.00 13.33 ? 710  LEU   B CG    1 
ATOM   14346 C  CD1   . LEU   B  1  712  ? 13.975  25.417  70.633  1.00 15.39 ? 710  LEU   B CD1   1 
ATOM   14347 C  CD2   . LEU   B  1  712  ? 12.681  24.297  72.459  1.00 17.45 ? 710  LEU   B CD2   1 
ATOM   14348 N  N     . ALA   B  1  713  ? 14.398  28.609  74.255  1.00 13.66 ? 711  ALA   B N     1 
ATOM   14349 C  CA    . ALA   B  1  713  ? 13.368  29.618  74.473  1.00 13.77 ? 711  ALA   B CA    1 
ATOM   14350 C  C     . ALA   B  1  713  ? 13.771  30.976  73.915  1.00 13.53 ? 711  ALA   B C     1 
ATOM   14351 O  O     . ALA   B  1  713  ? 13.022  31.571  73.145  1.00 13.59 ? 711  ALA   B O     1 
ATOM   14352 C  CB    . ALA   B  1  713  ? 13.037  29.712  75.959  1.00 15.12 ? 711  ALA   B CB    1 
ATOM   14353 N  N     . ILE   B  1  714  ? 14.934  31.500  74.294  1.00 14.64 ? 712  ILE   B N     1 
ATOM   14354 C  CA    . ILE   B  1  714  ? 15.321  32.801  73.748  1.00 15.08 ? 712  ILE   B CA    1 
ATOM   14355 C  C     . ILE   B  1  714  ? 15.604  32.683  72.264  1.00 14.66 ? 712  ILE   B C     1 
ATOM   14356 O  O     . ILE   B  1  714  ? 15.222  33.554  71.470  1.00 14.18 ? 712  ILE   B O     1 
ATOM   14357 C  CB    . ILE   B  1  714  ? 16.514  33.370  74.524  1.00 14.28 ? 712  ILE   B CB    1 
ATOM   14358 C  CG1   . ILE   B  1  714  ? 16.012  33.721  75.925  1.00 16.41 ? 712  ILE   B CG1   1 
ATOM   14359 C  CG2   . ILE   B  1  714  ? 17.104  34.583  73.784  1.00 15.45 ? 712  ILE   B CG2   1 
ATOM   14360 C  CD1   . ILE   B  1  714  ? 17.001  34.434  76.758  1.00 24.89 ? 712  ILE   B CD1   1 
ATOM   14361 N  N     . PHE   B  1  715  ? 16.271  31.600  71.877  1.00 14.10 ? 713  PHE   B N     1 
ATOM   14362 C  CA    . PHE   B  1  715  ? 16.505  31.307  70.473  1.00 14.01 ? 713  PHE   B CA    1 
ATOM   14363 C  C     . PHE   B  1  715  ? 15.214  31.435  69.678  1.00 13.73 ? 713  PHE   B C     1 
ATOM   14364 O  O     . PHE   B  1  715  ? 15.150  32.176  68.688  1.00 13.66 ? 713  PHE   B O     1 
ATOM   14365 C  CB    . PHE   B  1  715  ? 17.066  29.890  70.354  1.00 13.74 ? 713  PHE   B CB    1 
ATOM   14366 C  CG    . PHE   B  1  715  ? 17.309  29.476  68.944  1.00 13.43 ? 713  PHE   B CG    1 
ATOM   14367 C  CD1   . PHE   B  1  715  ? 18.417  29.933  68.271  1.00 13.50 ? 713  PHE   B CD1   1 
ATOM   14368 C  CD2   . PHE   B  1  715  ? 16.398  28.669  68.277  1.00 13.77 ? 713  PHE   B CD2   1 
ATOM   14369 C  CE1   . PHE   B  1  715  ? 18.646  29.563  66.957  1.00 14.46 ? 713  PHE   B CE1   1 
ATOM   14370 C  CE2   . PHE   B  1  715  ? 16.613  28.302  66.956  1.00 15.73 ? 713  PHE   B CE2   1 
ATOM   14371 C  CZ    . PHE   B  1  715  ? 17.729  28.748  66.297  1.00 14.61 ? 713  PHE   B CZ    1 
ATOM   14372 N  N     . THR   B  1  716  ? 14.168  30.724  70.108  1.00 12.58 ? 714  THR   B N     1 
ATOM   14373 C  CA    . THR   B  1  716  ? 12.901  30.728  69.382  1.00 13.48 ? 714  THR   B CA    1 
ATOM   14374 C  C     . THR   B  1  716  ? 12.217  32.076  69.474  1.00 13.97 ? 714  THR   B C     1 
ATOM   14375 O  O     . THR   B  1  716  ? 11.635  32.550  68.495  1.00 13.61 ? 714  THR   B O     1 
ATOM   14376 C  CB    . THR   B  1  716  ? 11.987  29.649  69.961  1.00 12.88 ? 714  THR   B CB    1 
ATOM   14377 O  OG1   . THR   B  1  716  ? 12.577  28.368  69.761  1.00 15.47 ? 714  THR   B OG1   1 
ATOM   14378 C  CG2   . THR   B  1  716  ? 10.629  29.672  69.293  1.00 15.17 ? 714  THR   B CG2   1 
ATOM   14379 N  N     . GLY   B  1  717  ? 12.222  32.690  70.651  1.00 13.89 ? 715  GLY   B N     1 
ATOM   14380 C  CA    . GLY   B  1  717  ? 11.545  33.967  70.818  1.00 14.04 ? 715  GLY   B CA    1 
ATOM   14381 C  C     . GLY   B  1  717  ? 12.050  35.029  69.859  1.00 13.60 ? 715  GLY   B C     1 
ATOM   14382 O  O     . GLY   B  1  717  ? 11.265  35.690  69.177  1.00 13.48 ? 715  GLY   B O     1 
ATOM   14383 N  N     . GLN   B  1  718  ? 13.371  35.191  69.766  1.00 13.01 ? 716  GLN   B N     1 
ATOM   14384 C  CA    . GLN   B  1  718  ? 13.879  36.253  68.907  1.00 12.78 ? 716  GLN   B CA    1 
ATOM   14385 C  C     . GLN   B  1  718  ? 13.525  35.973  67.456  1.00 13.61 ? 716  GLN   B C     1 
ATOM   14386 O  O     . GLN   B  1  718  ? 13.066  36.855  66.718  1.00 13.10 ? 716  GLN   B O     1 
ATOM   14387 C  CB    . GLN   B  1  718  ? 15.392  36.382  69.041  1.00 13.49 ? 716  GLN   B CB    1 
ATOM   14388 C  CG    . GLN   B  1  718  ? 15.825  36.811  70.442  1.00 13.23 ? 716  GLN   B CG    1 
ATOM   14389 C  CD    . GLN   B  1  718  ? 17.304  37.091  70.549  1.00 13.63 ? 716  GLN   B CD    1 
ATOM   14390 O  OE1   . GLN   B  1  718  ? 17.693  38.075  71.174  1.00 15.49 ? 716  GLN   B OE1   1 
ATOM   14391 N  NE2   . GLN   B  1  718  ? 18.137  36.244  69.945  1.00 14.20 ? 716  GLN   B NE2   1 
ATOM   14392 N  N     . ILE   B  1  719  ? 13.741  34.732  67.032  1.00 13.48 ? 717  ILE   B N     1 
ATOM   14393 C  CA    . ILE   B  1  719  ? 13.495  34.344  65.649  1.00 13.27 ? 717  ILE   B CA    1 
ATOM   14394 C  C     . ILE   B  1  719  ? 12.024  34.497  65.316  1.00 13.73 ? 717  ILE   B C     1 
ATOM   14395 O  O     . ILE   B  1  719  ? 11.664  35.006  64.251  1.00 13.55 ? 717  ILE   B O     1 
ATOM   14396 C  CB    . ILE   B  1  719  ? 13.970  32.907  65.427  1.00 14.49 ? 717  ILE   B CB    1 
ATOM   14397 C  CG1   . ILE   B  1  719  ? 15.483  32.864  65.506  1.00 14.96 ? 717  ILE   B CG1   1 
ATOM   14398 C  CG2   . ILE   B  1  719  ? 13.445  32.374  64.125  1.00 18.37 ? 717  ILE   B CG2   1 
ATOM   14399 C  CD1   . ILE   B  1  719  ? 15.933  31.451  65.646  1.00 22.07 ? 717  ILE   B CD1   1 
ATOM   14400 N  N     . ALA   B  1  720  ? 11.156  34.022  66.205  1.00 13.32 ? 718  ALA   B N     1 
ATOM   14401 C  CA    . ALA   B  1  720  ? 9.728   34.061  65.937  1.00 12.45 ? 718  ALA   B CA    1 
ATOM   14402 C  C     . ALA   B  1  720  ? 9.258   35.485  65.765  1.00 13.09 ? 718  ALA   B C     1 
ATOM   14403 O  O     . ALA   B  1  720  ? 8.442   35.780  64.874  1.00 14.04 ? 718  ALA   B O     1 
ATOM   14404 C  CB    . ALA   B  1  720  ? 8.963   33.410  67.085  1.00 14.44 ? 718  ALA   B CB    1 
ATOM   14405 N  N     . ALA   B  1  721  ? 9.710   36.370  66.649  1.00 13.03 ? 719  ALA   B N     1 
ATOM   14406 C  CA    . ALA   B  1  721  ? 9.304   37.762  66.557  1.00 13.38 ? 719  ALA   B CA    1 
ATOM   14407 C  C     . ALA   B  1  721  ? 9.785   38.375  65.258  1.00 12.48 ? 719  ALA   B C     1 
ATOM   14408 O  O     . ALA   B  1  721  ? 9.023   39.047  64.557  1.00 13.14 ? 719  ALA   B O     1 
ATOM   14409 C  CB    . ALA   B  1  721  ? 9.845   38.530  67.756  1.00 13.54 ? 719  ALA   B CB    1 
ATOM   14410 N  N     . ALA   B  1  722  ? 11.056  38.170  64.926  1.00 12.36 ? 720  ALA   B N     1 
ATOM   14411 C  CA    . ALA   B  1  722  ? 11.563  38.723  63.674  1.00 12.00 ? 720  ALA   B CA    1 
ATOM   14412 C  C     . ALA   B  1  722  ? 10.788  38.194  62.473  1.00 12.57 ? 720  ALA   B C     1 
ATOM   14413 O  O     . ALA   B  1  722  ? 10.381  38.970  61.594  1.00 13.45 ? 720  ALA   B O     1 
ATOM   14414 C  CB    . ALA   B  1  722  ? 13.042  38.399  63.539  1.00 12.57 ? 720  ALA   B CB    1 
ATOM   14415 N  N     . LEU   B  1  723  ? 10.563  36.879  62.435  1.00 12.59 ? 721  LEU   B N     1 
ATOM   14416 C  CA    . LEU   B  1  723  ? 9.851   36.270  61.309  1.00 13.21 ? 721  LEU   B CA    1 
ATOM   14417 C  C     . LEU   B  1  723  ? 8.442   36.803  61.207  1.00 14.13 ? 721  LEU   B C     1 
ATOM   14418 O  O     . LEU   B  1  723  ? 7.960   37.111  60.107  1.00 13.91 ? 721  LEU   B O     1 
ATOM   14419 C  CB    . LEU   B  1  723  ? 9.774   34.762  61.494  1.00 13.78 ? 721  LEU   B CB    1 
ATOM   14420 C  CG    . LEU   B  1  723  ? 11.057  33.989  61.247  1.00 14.28 ? 721  LEU   B CG    1 
ATOM   14421 C  CD1   . LEU   B  1  723  ? 10.839  32.554  61.699  1.00 15.06 ? 721  LEU   B CD1   1 
ATOM   14422 C  CD2   . LEU   B  1  723  ? 11.495  34.071  59.797  1.00 14.98 ? 721  LEU   B CD2   1 
ATOM   14423 N  N     . VAL   B  1  724  ? 7.734   36.856  62.332  1.00 12.60 ? 722  VAL   B N     1 
ATOM   14424 C  CA    . VAL   B  1  724  ? 6.327   37.209  62.239  1.00 12.83 ? 722  VAL   B CA    1 
ATOM   14425 C  C     . VAL   B  1  724  ? 6.163   38.676  61.882  1.00 13.32 ? 722  VAL   B C     1 
ATOM   14426 O  O     . VAL   B  1  724  ? 5.160   39.061  61.266  1.00 14.16 ? 722  VAL   B O     1 
ATOM   14427 C  CB    . VAL   B  1  724  ? 5.541   36.787  63.497  1.00 12.33 ? 722  VAL   B CB    1 
ATOM   14428 C  CG1   . VAL   B  1  724  ? 5.743   37.776  64.635  1.00 14.49 ? 722  VAL   B CG1   1 
ATOM   14429 C  CG2   . VAL   B  1  724  ? 4.090   36.600  63.158  1.00 14.12 ? 722  VAL   B CG2   1 
ATOM   14430 N  N     . ALA   B  1  725  ? 7.149   39.502  62.227  1.00 14.31 ? 723  ALA   B N     1 
ATOM   14431 C  CA    . ALA   B  1  725  ? 7.188   40.890  61.783  1.00 13.83 ? 723  ALA   B CA    1 
ATOM   14432 C  C     . ALA   B  1  725  ? 7.532   41.019  60.306  1.00 15.87 ? 723  ALA   B C     1 
ATOM   14433 O  O     . ALA   B  1  725  ? 7.564   42.140  59.788  1.00 17.47 ? 723  ALA   B O     1 
ATOM   14434 C  CB    . ALA   B  1  725  ? 8.146   41.705  62.663  1.00 14.95 ? 723  ALA   B CB    1 
ATOM   14435 N  N     . GLY   B  1  726  ? 7.774   39.915  59.614  1.00 14.00 ? 724  GLY   B N     1 
ATOM   14436 C  CA    . GLY   B  1  726  ? 7.980   39.945  58.179  1.00 14.65 ? 724  GLY   B CA    1 
ATOM   14437 C  C     . GLY   B  1  726  ? 9.423   39.947  57.742  1.00 15.54 ? 724  GLY   B C     1 
ATOM   14438 O  O     . GLY   B  1  726  ? 9.696   40.220  56.565  1.00 16.65 ? 724  GLY   B O     1 
ATOM   14439 N  N     . ASN   B  1  727  ? 10.353  39.662  58.641  1.00 13.87 ? 725  ASN   B N     1 
ATOM   14440 C  CA    . ASN   B  1  727  ? 11.770  39.708  58.339  1.00 14.22 ? 725  ASN   B CA    1 
ATOM   14441 C  C     . ASN   B  1  727  ? 12.312  38.308  58.180  1.00 13.94 ? 725  ASN   B C     1 
ATOM   14442 O  O     . ASN   B  1  727  ? 12.030  37.442  59.014  1.00 16.18 ? 725  ASN   B O     1 
ATOM   14443 C  CB    . ASN   B  1  727  ? 12.514  40.356  59.500  1.00 14.24 ? 725  ASN   B CB    1 
ATOM   14444 C  CG    . ASN   B  1  727  ? 11.966  41.701  59.863  1.00 15.97 ? 725  ASN   B CG    1 
ATOM   14445 O  OD1   . ASN   B  1  727  ? 12.255  42.702  59.206  1.00 15.57 ? 725  ASN   B OD1   1 
ATOM   14446 N  ND2   . ASN   B  1  727  ? 11.184  41.749  60.928  1.00 14.40 ? 725  ASN   B ND2   1 
ATOM   14447 N  N     . PRO   B  1  728  ? 13.122  38.053  57.166  1.00 13.76 ? 726  PRO   B N     1 
ATOM   14448 C  CA    . PRO   B  1  728  ? 13.847  36.789  57.124  1.00 14.48 ? 726  PRO   B CA    1 
ATOM   14449 C  C     . PRO   B  1  728  ? 14.931  36.843  58.179  1.00 16.07 ? 726  PRO   B C     1 
ATOM   14450 O  O     . PRO   B  1  728  ? 15.415  37.918  58.536  1.00 15.72 ? 726  PRO   B O     1 
ATOM   14451 C  CB    . PRO   B  1  728  ? 14.453  36.777  55.718  1.00 16.38 ? 726  PRO   B CB    1 
ATOM   14452 C  CG    . PRO   B  1  728  ? 14.641  38.220  55.385  1.00 17.46 ? 726  PRO   B CG    1 
ATOM   14453 C  CD    . PRO   B  1  728  ? 13.512  38.971  56.083  1.00 14.88 ? 726  PRO   B CD    1 
ATOM   14454 N  N     . VAL   B  1  729  ? 15.304  35.675  58.677  1.00 13.56 ? 727  VAL   B N     1 
ATOM   14455 C  CA    . VAL   B  1  729  ? 16.144  35.573  59.860  1.00 14.06 ? 727  VAL   B CA    1 
ATOM   14456 C  C     . VAL   B  1  729  ? 17.390  34.758  59.564  1.00 14.69 ? 727  VAL   B C     1 
ATOM   14457 O  O     . VAL   B  1  729  ? 17.337  33.703  58.914  1.00 14.75 ? 727  VAL   B O     1 
ATOM   14458 C  CB    . VAL   B  1  729  ? 15.358  34.945  61.016  1.00 14.34 ? 727  VAL   B CB    1 
ATOM   14459 C  CG1   . VAL   B  1  729  ? 16.316  34.557  62.143  1.00 14.82 ? 727  VAL   B CG1   1 
ATOM   14460 C  CG2   . VAL   B  1  729  ? 14.344  35.937  61.520  1.00 14.66 ? 727  VAL   B CG2   1 
ATOM   14461 N  N     . LEU   B  1  730  ? 18.516  35.240  60.076  1.00 13.06 ? 728  LEU   B N     1 
ATOM   14462 C  CA    . LEU   B  1  730  ? 19.752  34.480  60.167  1.00 13.48 ? 728  LEU   B CA    1 
ATOM   14463 C  C     . LEU   B  1  730  ? 19.921  34.141  61.638  1.00 13.23 ? 728  LEU   B C     1 
ATOM   14464 O  O     . LEU   B  1  730  ? 20.134  35.037  62.460  1.00 14.74 ? 728  LEU   B O     1 
ATOM   14465 C  CB    . LEU   B  1  730  ? 20.935  35.321  59.698  1.00 14.75 ? 728  LEU   B CB    1 
ATOM   14466 C  CG    . LEU   B  1  730  ? 20.958  35.859  58.267  1.00 16.23 ? 728  LEU   B CG    1 
ATOM   14467 C  CD1   . LEU   B  1  730  ? 20.579  34.737  57.305  1.00 16.02 ? 728  LEU   B CD1   1 
ATOM   14468 C  CD2   . LEU   B  1  730  ? 20.092  37.097  58.054  1.00 15.69 ? 728  LEU   B CD2   1 
ATOM   14469 N  N     . ALA   B  1  731  ? 19.783  32.872  61.971  1.00 13.56 ? 729  ALA   B N     1 
ATOM   14470 C  CA    . ALA   B  1  731  ? 19.771  32.432  63.357  1.00 12.83 ? 729  ALA   B CA    1 
ATOM   14471 C  C     . ALA   B  1  731  ? 21.141  31.890  63.724  1.00 15.00 ? 729  ALA   B C     1 
ATOM   14472 O  O     . ALA   B  1  731  ? 21.580  30.890  63.163  1.00 14.00 ? 729  ALA   B O     1 
ATOM   14473 C  CB    . ALA   B  1  731  ? 18.684  31.378  63.574  1.00 15.19 ? 729  ALA   B CB    1 
ATOM   14474 N  N     . LYS   B  1  732  ? 21.803  32.545  64.674  1.00 14.10 ? 730  LYS   B N     1 
ATOM   14475 C  CA    . LYS   B  1  732  ? 23.156  32.194  65.094  1.00 14.03 ? 730  LYS   B CA    1 
ATOM   14476 C  C     . LYS   B  1  732  ? 23.070  31.773  66.551  1.00 14.15 ? 730  LYS   B C     1 
ATOM   14477 O  O     . LYS   B  1  732  ? 23.103  32.624  67.462  1.00 13.87 ? 730  LYS   B O     1 
ATOM   14478 C  CB    . LYS   B  1  732  ? 24.116  33.363  64.890  1.00 13.87 ? 730  LYS   B CB    1 
ATOM   14479 C  CG    . LYS   B  1  732  ? 25.545  32.962  64.593  1.00 14.50 ? 730  LYS   B CG    1 
ATOM   14480 C  CD    . LYS   B  1  732  ? 26.156  32.064  65.668  1.00 14.67 ? 730  LYS   B CD    1 
ATOM   14481 C  CE    . LYS   B  1  732  ? 26.508  32.840  66.934  1.00 14.33 ? 730  LYS   B CE    1 
ATOM   14482 N  NZ    . LYS   B  1  732  ? 27.079  31.916  67.943  1.00 15.79 ? 730  LYS   B NZ    1 
ATOM   14483 N  N     . PRO   B  1  733  ? 22.941  30.484  66.817  1.00 13.09 ? 731  PRO   B N     1 
ATOM   14484 C  CA    . PRO   B  1  733  ? 22.812  30.031  68.205  1.00 14.34 ? 731  PRO   B CA    1 
ATOM   14485 C  C     . PRO   B  1  733  ? 24.174  29.993  68.862  1.00 12.83 ? 731  PRO   B C     1 
ATOM   14486 O  O     . PRO   B  1  733  ? 25.217  29.966  68.210  1.00 13.85 ? 731  PRO   B O     1 
ATOM   14487 C  CB    . PRO   B  1  733  ? 22.271  28.609  68.059  1.00 15.02 ? 731  PRO   B CB    1 
ATOM   14488 C  CG    . PRO   B  1  733  ? 22.873  28.142  66.752  1.00 14.49 ? 731  PRO   B CG    1 
ATOM   14489 C  CD    . PRO   B  1  733  ? 22.890  29.370  65.849  1.00 14.75 ? 731  PRO   B CD    1 
ATOM   14490 N  N     . ALA   B  1  734  ? 24.134  30.004  70.183  1.00 13.38 ? 732  ALA   B N     1 
ATOM   14491 C  CA    . ALA   B  1  734  ? 25.359  29.913  70.960  1.00 14.13 ? 732  ALA   B CA    1 
ATOM   14492 C  C     . ALA   B  1  734  ? 26.150  28.670  70.574  1.00 14.67 ? 732  ALA   B C     1 
ATOM   14493 O  O     . ALA   B  1  734  ? 25.590  27.611  70.265  1.00 15.65 ? 732  ALA   B O     1 
ATOM   14494 C  CB    . ALA   B  1  734  ? 24.983  29.840  72.437  1.00 14.87 ? 732  ALA   B CB    1 
ATOM   14495 N  N     . GLU   B  1  735  ? 27.471  28.790  70.616  1.00 14.48 ? 733  GLU   B N     1 
ATOM   14496 C  CA    . GLU   B  1  735  ? 28.296  27.661  70.207  1.00 15.31 ? 733  GLU   B CA    1 
ATOM   14497 C  C     . GLU   B  1  735  ? 28.117  26.456  71.116  1.00 16.44 ? 733  GLU   B C     1 
ATOM   14498 O  O     . GLU   B  1  735  ? 28.317  25.321  70.679  1.00 17.15 ? 733  GLU   B O     1 
ATOM   14499 C  CB    . GLU   B  1  735  ? 29.765  28.061  70.121  1.00 17.42 ? 733  GLU   B CB    1 
ATOM   14500 C  CG    . GLU   B  1  735  ? 30.336  28.670  71.381  1.00 21.18 ? 733  GLU   B CG    1 
ATOM   14501 C  CD    . GLU   B  1  735  ? 30.223  30.193  71.429  1.00 20.73 ? 733  GLU   B CD    1 
ATOM   14502 O  OE1   . GLU   B  1  735  ? 29.273  30.768  70.856  1.00 21.88 ? 733  GLU   B OE1   1 
ATOM   14503 O  OE2   . GLU   B  1  735  ? 31.113  30.823  72.046  1.00 22.92 ? 733  GLU   B OE2   1 
ATOM   14504 N  N     . GLU   B  1  736  ? 27.707  26.677  72.363  1.00 14.92 ? 734  GLU   B N     1 
ATOM   14505 C  CA    . GLU   B  1  736  ? 27.571  25.569  73.293  1.00 16.78 ? 734  GLU   B CA    1 
ATOM   14506 C  C     . GLU   B  1  736  ? 26.335  24.724  73.018  1.00 15.92 ? 734  GLU   B C     1 
ATOM   14507 O  O     . GLU   B  1  736  ? 26.316  23.540  73.372  1.00 18.07 ? 734  GLU   B O     1 
ATOM   14508 C  CB    . GLU   B  1  736  ? 27.463  26.096  74.724  1.00 16.12 ? 734  GLU   B CB    1 
ATOM   14509 C  CG    . GLU   B  1  736  ? 28.700  26.820  75.246  1.00 18.05 ? 734  GLU   B CG    1 
ATOM   14510 C  CD    . GLU   B  1  736  ? 28.688  28.325  75.002  1.00 20.33 ? 734  GLU   B CD    1 
ATOM   14511 O  OE1   . GLU   B  1  736  ? 27.927  28.818  74.138  1.00 17.93 ? 734  GLU   B OE1   1 
ATOM   14512 O  OE2   . GLU   B  1  736  ? 29.444  29.026  75.708  1.00 23.85 ? 734  GLU   B OE2   1 
ATOM   14513 N  N     . THR   B  1  737  ? 25.291  25.299  72.408  1.00 15.19 ? 735  THR   B N     1 
ATOM   14514 C  CA    . THR   B  1  737  ? 23.982  24.636  72.343  1.00 15.47 ? 735  THR   B CA    1 
ATOM   14515 C  C     . THR   B  1  737  ? 23.379  24.692  70.945  1.00 14.95 ? 735  THR   B C     1 
ATOM   14516 O  O     . THR   B  1  737  ? 22.239  25.111  70.763  1.00 15.59 ? 735  THR   B O     1 
ATOM   14517 C  CB    . THR   B  1  737  ? 23.026  25.236  73.371  1.00 15.30 ? 735  THR   B CB    1 
ATOM   14518 O  OG1   . THR   B  1  737  ? 22.999  26.659  73.211  1.00 15.72 ? 735  THR   B OG1   1 
ATOM   14519 C  CG2   . THR   B  1  737  ? 23.487  24.890  74.790  1.00 15.94 ? 735  THR   B CG2   1 
ATOM   14520 N  N     . PRO   B  1  738  ? 24.106  24.226  69.934  1.00 14.07 ? 736  PRO   B N     1 
ATOM   14521 C  CA    . PRO   B  1  738  ? 23.569  24.284  68.567  1.00 13.98 ? 736  PRO   B CA    1 
ATOM   14522 C  C     . PRO   B  1  738  ? 22.507  23.243  68.275  1.00 14.57 ? 736  PRO   B C     1 
ATOM   14523 O  O     . PRO   B  1  738  ? 21.724  23.450  67.343  1.00 14.98 ? 736  PRO   B O     1 
ATOM   14524 C  CB    . PRO   B  1  738  ? 24.807  24.009  67.704  1.00 14.67 ? 736  PRO   B CB    1 
ATOM   14525 C  CG    . PRO   B  1  738  ? 25.618  23.076  68.573  1.00 15.43 ? 736  PRO   B CG    1 
ATOM   14526 C  CD    . PRO   B  1  738  ? 25.452  23.619  69.971  1.00 14.44 ? 736  PRO   B CD    1 
ATOM   14527 N  N     . LEU   B  1  739  ? 22.463  22.129  69.003  1.00 13.61 ? 737  LEU   B N     1 
ATOM   14528 C  CA    . LEU   B  1  739  ? 21.596  21.036  68.572  1.00 14.27 ? 737  LEU   B CA    1 
ATOM   14529 C  C     . LEU   B  1  739  ? 20.136  21.384  68.783  1.00 14.18 ? 737  LEU   B C     1 
ATOM   14530 O  O     . LEU   B  1  739  ? 19.306  21.192  67.885  1.00 14.64 ? 737  LEU   B O     1 
ATOM   14531 C  CB    . LEU   B  1  739  ? 21.951  19.736  69.278  1.00 14.96 ? 737  LEU   B CB    1 
ATOM   14532 C  CG    . LEU   B  1  739  ? 23.397  19.297  69.080  1.00 15.11 ? 737  LEU   B CG    1 
ATOM   14533 C  CD1   . LEU   B  1  739  ? 23.621  18.064  69.920  1.00 17.23 ? 737  LEU   B CD1   1 
ATOM   14534 C  CD2   . LEU   B  1  739  ? 23.684  19.012  67.605  1.00 16.43 ? 737  LEU   B CD2   1 
ATOM   14535 N  N     . ILE   B  1  740  ? 19.789  21.900  69.962  1.00 14.94 ? 738  ILE   B N     1 
ATOM   14536 C  CA    . ILE   B  1  740  ? 18.388  22.234  70.168  1.00 14.10 ? 738  ILE   B CA    1 
ATOM   14537 C  C     . ILE   B  1  740  ? 17.984  23.388  69.268  1.00 13.05 ? 738  ILE   B C     1 
ATOM   14538 O  O     . ILE   B  1  740  ? 16.830  23.469  68.836  1.00 14.68 ? 738  ILE   B O     1 
ATOM   14539 C  CB    . ILE   B  1  740  ? 18.063  22.496  71.653  1.00 15.95 ? 738  ILE   B CB    1 
ATOM   14540 C  CG1   . ILE   B  1  740  ? 16.557  22.650  71.858  1.00 16.55 ? 738  ILE   B CG1   1 
ATOM   14541 C  CG2   . ILE   B  1  740  ? 18.791  23.744  72.131  1.00 17.19 ? 738  ILE   B CG2   1 
ATOM   14542 C  CD1   . ILE   B  1  740  ? 15.775  21.374  71.613  1.00 17.87 ? 738  ILE   B CD1   1 
ATOM   14543 N  N     . ALA   B  1  741  ? 18.913  24.297  68.964  1.00 13.95 ? 739  ALA   B N     1 
ATOM   14544 C  CA    . ALA   B  1  741  ? 18.607  25.377  68.038  1.00 14.07 ? 739  ALA   B CA    1 
ATOM   14545 C  C     . ALA   B  1  741  ? 18.302  24.828  66.662  1.00 14.27 ? 739  ALA   B C     1 
ATOM   14546 O  O     . ALA   B  1  741  ? 17.333  25.248  66.022  1.00 14.58 ? 739  ALA   B O     1 
ATOM   14547 C  CB    . ALA   B  1  741  ? 19.784  26.348  67.983  1.00 15.62 ? 739  ALA   B CB    1 
ATOM   14548 N  N     . ALA   B  1  742  ? 19.102  23.865  66.206  1.00 14.10 ? 740  ALA   B N     1 
ATOM   14549 C  CA    . ALA   B  1  742  ? 18.836  23.249  64.919  1.00 14.32 ? 740  ALA   B CA    1 
ATOM   14550 C  C     . ALA   B  1  742  ? 17.461  22.613  64.916  1.00 14.38 ? 740  ALA   B C     1 
ATOM   14551 O  O     . ALA   B  1  742  ? 16.733  22.682  63.915  1.00 14.73 ? 740  ALA   B O     1 
ATOM   14552 C  CB    . ALA   B  1  742  ? 19.911  22.215  64.603  1.00 14.89 ? 740  ALA   B CB    1 
ATOM   14553 N  N     . GLU   B  1  743  ? 17.073  22.008  66.034  1.00 14.52 ? 741  GLU   B N     1 
ATOM   14554 C  CA    . GLU   B  1  743  ? 15.756  21.389  66.097  1.00 14.94 ? 741  GLU   B CA    1 
ATOM   14555 C  C     . GLU   B  1  743  ? 14.664  22.444  66.072  1.00 13.82 ? 741  GLU   B C     1 
ATOM   14556 O  O     . GLU   B  1  743  ? 13.633  22.262  65.410  1.00 15.03 ? 741  GLU   B O     1 
ATOM   14557 C  CB    . GLU   B  1  743  ? 15.682  20.516  67.343  1.00 16.18 ? 741  GLU   B CB    1 
ATOM   14558 C  CG    . GLU   B  1  743  ? 14.347  19.861  67.515  1.00 16.99 ? 741  GLU   B CG    1 
ATOM   14559 C  CD    . GLU   B  1  743  ? 14.046  18.809  66.487  1.00 18.31 ? 741  GLU   B CD    1 
ATOM   14560 O  OE1   . GLU   B  1  743  ? 14.914  18.478  65.647  1.00 18.23 ? 741  GLU   B OE1   1 
ATOM   14561 O  OE2   . GLU   B  1  743  ? 12.901  18.310  66.515  1.00 22.37 ? 741  GLU   B OE2   1 
ATOM   14562 N  N     . GLY   B  1  744  ? 14.888  23.580  66.731  1.00 14.59 ? 742  GLY   B N     1 
ATOM   14563 C  CA    . GLY   B  1  744  ? 13.940  24.680  66.631  1.00 15.40 ? 742  GLY   B CA    1 
ATOM   14564 C  C     . GLY   B  1  744  ? 13.743  25.142  65.194  1.00 13.65 ? 742  GLY   B C     1 
ATOM   14565 O  O     . GLY   B  1  744  ? 12.614  25.379  64.754  1.00 13.95 ? 742  GLY   B O     1 
ATOM   14566 N  N     . VAL   B  1  745  ? 14.832  25.246  64.433  1.00 14.35 ? 743  VAL   B N     1 
ATOM   14567 C  CA    . VAL   B  1  745  ? 14.712  25.648  63.035  1.00 13.56 ? 743  VAL   B CA    1 
ATOM   14568 C  C     . VAL   B  1  745  ? 13.996  24.582  62.223  1.00 15.25 ? 743  VAL   B C     1 
ATOM   14569 O  O     . VAL   B  1  745  ? 13.162  24.908  61.370  1.00 14.73 ? 743  VAL   B O     1 
ATOM   14570 C  CB    . VAL   B  1  745  ? 16.087  26.016  62.461  1.00 15.16 ? 743  VAL   B CB    1 
ATOM   14571 C  CG1   . VAL   B  1  745  ? 16.012  26.164  60.936  1.00 15.29 ? 743  VAL   B CG1   1 
ATOM   14572 C  CG2   . VAL   B  1  745  ? 16.522  27.309  63.091  1.00 15.98 ? 743  VAL   B CG2   1 
ATOM   14573 N  N     . ARG   B  1  746  ? 14.274  23.295  62.487  1.00 14.06 ? 744  ARG   B N     1 
ATOM   14574 C  CA    . ARG   B  1  746  ? 13.544  22.241  61.779  1.00 14.74 ? 744  ARG   B CA    1 
ATOM   14575 C  C     . ARG   B  1  746  ? 12.056  22.394  62.012  1.00 14.59 ? 744  ARG   B C     1 
ATOM   14576 O  O     . ARG   B  1  746  ? 11.250  22.234  61.087  1.00 14.90 ? 744  ARG   B O     1 
ATOM   14577 C  CB    . ARG   B  1  746  ? 13.942  20.857  62.293  1.00 14.87 ? 744  ARG   B CB    1 
ATOM   14578 C  CG    . ARG   B  1  746  ? 15.335  20.408  61.946  1.00 16.39 ? 744  ARG   B CG    1 
ATOM   14579 C  CD    . ARG   B  1  746  ? 15.545  18.978  62.433  1.00 16.51 ? 744  ARG   B CD    1 
ATOM   14580 N  NE    . ARG   B  1  746  ? 16.942  18.602  62.292  1.00 17.84 ? 744  ARG   B NE    1 
ATOM   14581 C  CZ    . ARG   B  1  746  ? 17.862  18.716  63.239  1.00 16.14 ? 744  ARG   B CZ    1 
ATOM   14582 N  NH1   . ARG   B  1  746  ? 17.534  18.916  64.509  1.00 17.47 ? 744  ARG   B NH1   1 
ATOM   14583 N  NH2   . ARG   B  1  746  ? 19.145  18.647  62.896  1.00 17.81 ? 744  ARG   B NH2   1 
ATOM   14584 N  N     . ILE   B  1  747  ? 11.674  22.690  63.250  1.00 13.62 ? 745  ILE   B N     1 
ATOM   14585 C  CA    . ILE   B  1  747  ? 10.260  22.776  63.585  1.00 13.85 ? 745  ILE   B CA    1 
ATOM   14586 C  C     . ILE   B  1  747  ? 9.622   23.994  62.934  1.00 14.03 ? 745  ILE   B C     1 
ATOM   14587 O  O     . ILE   B  1  747  ? 8.518   23.912  62.376  1.00 14.09 ? 745  ILE   B O     1 
ATOM   14588 C  CB    . ILE   B  1  747  ? 10.072  22.755  65.110  1.00 14.32 ? 745  ILE   B CB    1 
ATOM   14589 C  CG1   . ILE   B  1  747  ? 10.289  21.329  65.593  1.00 15.66 ? 745  ILE   B CG1   1 
ATOM   14590 C  CG2   . ILE   B  1  747  ? 8.682   23.238  65.469  1.00 15.49 ? 745  ILE   B CG2   1 
ATOM   14591 C  CD1   . ILE   B  1  747  ? 10.400  21.217  67.066  1.00 17.50 ? 745  ILE   B CD1   1 
ATOM   14592 N  N     . LEU   B  1  748  ? 10.309  25.138  62.957  1.00 13.38 ? 746  LEU   B N     1 
ATOM   14593 C  CA    . LEU   B  1  748  ? 9.750   26.319  62.302  1.00 13.48 ? 746  LEU   B CA    1 
ATOM   14594 C  C     . LEU   B  1  748  ? 9.619   26.124  60.804  1.00 13.28 ? 746  LEU   B C     1 
ATOM   14595 O  O     . LEU   B  1  748  ? 8.639   26.570  60.209  1.00 14.36 ? 746  LEU   B O     1 
ATOM   14596 C  CB    . LEU   B  1  748  ? 10.578  27.559  62.600  1.00 14.55 ? 746  LEU   B CB    1 
ATOM   14597 C  CG    . LEU   B  1  748  ? 10.265  28.168  63.968  1.00 17.48 ? 746  LEU   B CG    1 
ATOM   14598 C  CD1   . LEU   B  1  748  ? 11.426  29.048  64.413  1.00 19.51 ? 746  LEU   B CD1   1 
ATOM   14599 C  CD2   . LEU   B  1  748  ? 9.015   28.979  63.847  1.00 19.56 ? 746  LEU   B CD2   1 
ATOM   14600 N  N     . ARG   B  1  749  ? 10.609  25.497  60.177  1.00 13.24 ? 747  ARG   B N     1 
ATOM   14601 C  CA    . ARG   B  1  749  ? 10.492  25.219  58.754  1.00 14.19 ? 747  ARG   B CA    1 
ATOM   14602 C  C     . ARG   B  1  749  ? 9.359   24.245  58.490  1.00 13.44 ? 747  ARG   B C     1 
ATOM   14603 O  O     . ARG   B  1  749  ? 8.574   24.443  57.550  1.00 14.91 ? 747  ARG   B O     1 
ATOM   14604 C  CB    . ARG   B  1  749  ? 11.815  24.687  58.213  1.00 14.57 ? 747  ARG   B CB    1 
ATOM   14605 C  CG    . ARG   B  1  749  ? 12.855  25.760  58.085  1.00 15.46 ? 747  ARG   B CG    1 
ATOM   14606 C  CD    . ARG   B  1  749  ? 14.054  25.187  57.368  1.00 18.07 ? 747  ARG   B CD    1 
ATOM   14607 N  NE    . ARG   B  1  749  ? 15.070  26.186  57.067  1.00 18.15 ? 747  ARG   B NE    1 
ATOM   14608 C  CZ    . ARG   B  1  749  ? 16.123  25.938  56.307  1.00 22.25 ? 747  ARG   B CZ    1 
ATOM   14609 N  NH1   . ARG   B  1  749  ? 16.290  24.756  55.730  1.00 23.42 ? 747  ARG   B NH1   1 
ATOM   14610 N  NH2   . ARG   B  1  749  ? 17.024  26.898  56.113  1.00 22.86 ? 747  ARG   B NH2   1 
ATOM   14611 N  N     . GLU   B  1  750  ? 9.229   23.208  59.330  1.00 13.52 ? 748  GLU   B N     1 
ATOM   14612 C  CA    . GLU   B  1  750  ? 8.134   22.262  59.140  1.00 14.93 ? 748  GLU   B CA    1 
ATOM   14613 C  C     . GLU   B  1  750  ? 6.790   22.963  59.259  1.00 12.84 ? 748  GLU   B C     1 
ATOM   14614 O  O     . GLU   B  1  750  ? 5.837   22.629  58.542  1.00 16.09 ? 748  GLU   B O     1 
ATOM   14615 C  CB    . GLU   B  1  750  ? 8.245   21.139  60.176  1.00 15.29 ? 748  GLU   B CB    1 
ATOM   14616 C  CG    . GLU   B  1  750  ? 7.184   20.089  60.008  1.00 17.13 ? 748  GLU   B CG    1 
ATOM   14617 C  CD    . GLU   B  1  750  ? 7.378   18.908  60.927  1.00 19.86 ? 748  GLU   B CD    1 
ATOM   14618 O  OE1   . GLU   B  1  750  ? 8.456   18.808  61.547  1.00 20.00 ? 748  GLU   B OE1   1 
ATOM   14619 O  OE2   . GLU   B  1  750  ? 6.433   18.101  61.037  1.00 23.53 ? 748  GLU   B OE2   1 
ATOM   14620 N  N     . ALA   B  1  751  ? 6.713   23.965  60.124  1.00 15.25 ? 749  ALA   B N     1 
ATOM   14621 C  CA    . ALA   B  1  751  ? 5.492   24.713  60.365  1.00 15.87 ? 749  ALA   B CA    1 
ATOM   14622 C  C     . ALA   B  1  751  ? 5.178   25.708  59.268  1.00 15.26 ? 749  ALA   B C     1 
ATOM   14623 O  O     . ALA   B  1  751  ? 4.118   26.340  59.323  1.00 17.31 ? 749  ALA   B O     1 
ATOM   14624 C  CB    . ALA   B  1  751  ? 5.633   25.475  61.678  1.00 15.72 ? 749  ALA   B CB    1 
ATOM   14625 N  N     . GLY   B  1  752  ? 6.047   25.878  58.281  1.00 14.05 ? 750  GLY   B N     1 
ATOM   14626 C  CA    . GLY   B  1  752  ? 5.740   26.732  57.144  1.00 16.05 ? 750  GLY   B CA    1 
ATOM   14627 C  C     . GLY   B  1  752  ? 6.709   27.871  56.918  1.00 15.79 ? 750  GLY   B C     1 
ATOM   14628 O  O     . GLY   B  1  752  ? 6.541   28.602  55.936  1.00 17.95 ? 750  GLY   B O     1 
ATOM   14629 N  N     . ILE   B  1  753  ? 7.721   28.089  57.757  1.00 14.35 ? 751  ILE   B N     1 
ATOM   14630 C  CA    . ILE   B  1  753  ? 8.665   29.167  57.486  1.00 15.33 ? 751  ILE   B CA    1 
ATOM   14631 C  C     . ILE   B  1  753  ? 9.566   28.715  56.347  1.00 16.39 ? 751  ILE   B C     1 
ATOM   14632 O  O     . ILE   B  1  753  ? 10.227  27.680  56.465  1.00 16.43 ? 751  ILE   B O     1 
ATOM   14633 C  CB    . ILE   B  1  753  ? 9.514   29.486  58.723  1.00 13.41 ? 751  ILE   B CB    1 
ATOM   14634 C  CG1   . ILE   B  1  753  ? 8.624   29.843  59.921  1.00 15.45 ? 751  ILE   B CG1   1 
ATOM   14635 C  CG2   . ILE   B  1  753  ? 10.486  30.599  58.386  1.00 16.01 ? 751  ILE   B CG2   1 
ATOM   14636 C  CD1   . ILE   B  1  753  ? 7.795   31.092  59.704  1.00 15.39 ? 751  ILE   B CD1   1 
ATOM   14637 N  N     . PRO   B  1  754  ? 9.616   29.451  55.240  1.00 15.63 ? 752  PRO   B N     1 
ATOM   14638 C  CA    . PRO   B  1  754  ? 10.432  29.024  54.101  1.00 16.43 ? 752  PRO   B CA    1 
ATOM   14639 C  C     . PRO   B  1  754  ? 11.904  28.975  54.464  1.00 18.03 ? 752  PRO   B C     1 
ATOM   14640 O  O     . PRO   B  1  754  ? 12.383  29.710  55.327  1.00 16.67 ? 752  PRO   B O     1 
ATOM   14641 C  CB    . PRO   B  1  754  ? 10.169  30.111  53.051  1.00 18.21 ? 752  PRO   B CB    1 
ATOM   14642 C  CG    . PRO   B  1  754  ? 8.892   30.780  53.475  1.00 23.01 ? 752  PRO   B CG    1 
ATOM   14643 C  CD    . PRO   B  1  754  ? 8.808   30.649  54.968  1.00 17.50 ? 752  PRO   B CD    1 
ATOM   14644 N  N     . ALA   B  1  755  ? 12.631  28.093  53.780  1.00 21.05 ? 753  ALA   B N     1 
ATOM   14645 C  CA    . ALA   B  1  755  ? 14.053  27.972  54.067  1.00 19.58 ? 753  ALA   B CA    1 
ATOM   14646 C  C     . ALA   B  1  755  ? 14.786  29.288  53.847  1.00 17.48 ? 753  ALA   B C     1 
ATOM   14647 O  O     . ALA   B  1  755  ? 15.729  29.601  54.580  1.00 20.15 ? 753  ALA   B O     1 
ATOM   14648 C  CB    . ALA   B  1  755  ? 14.674  26.862  53.220  1.00 24.45 ? 753  ALA   B CB    1 
ATOM   14649 N  N     . SER   B  1  756  ? 14.355  30.090  52.877  1.00 17.08 ? 754  SER   B N     1 
ATOM   14650 C  CA    . SER   B  1  756  ? 15.028  31.359  52.647  1.00 17.71 ? 754  SER   B CA    1 
ATOM   14651 C  C     . SER   B  1  756  ? 14.721  32.378  53.730  1.00 16.29 ? 754  SER   B C     1 
ATOM   14652 O  O     . SER   B  1  756  ? 15.471  33.349  53.880  1.00 17.72 ? 754  SER   B O     1 
ATOM   14653 C  CB    . SER   B  1  756  ? 14.611  31.923  51.305  1.00 20.01 ? 754  SER   B CB    1 
ATOM   14654 O  OG    . SER   B  1  756  ? 13.208  32.073  51.282  1.00 23.25 ? 754  SER   B OG    1 
ATOM   14655 N  N     . ALA   B  1  757  ? 13.634  32.190  54.475  1.00 14.32 ? 755  ALA   B N     1 
ATOM   14656 C  CA    . ALA   B  1  757  ? 13.299  33.093  55.551  1.00 13.32 ? 755  ALA   B CA    1 
ATOM   14657 C  C     . ALA   B  1  757  ? 13.934  32.703  56.865  1.00 14.67 ? 755  ALA   B C     1 
ATOM   14658 O  O     . ALA   B  1  757  ? 13.899  33.503  57.798  1.00 15.54 ? 755  ALA   B O     1 
ATOM   14659 C  CB    . ALA   B  1  757  ? 11.778  33.160  55.720  1.00 15.49 ? 755  ALA   B CB    1 
ATOM   14660 N  N     . LEU   B  1  758  ? 14.484  31.497  56.984  1.00 14.64 ? 756  LEU   B N     1 
ATOM   14661 C  CA    . LEU   B  1  758  ? 15.050  31.089  58.270  1.00 14.22 ? 756  LEU   B CA    1 
ATOM   14662 C  C     . LEU   B  1  758  ? 16.233  30.179  57.998  1.00 14.55 ? 756  LEU   B C     1 
ATOM   14663 O  O     . LEU   B  1  758  ? 16.063  29.012  57.639  1.00 16.78 ? 756  LEU   B O     1 
ATOM   14664 C  CB    . LEU   B  1  758  ? 14.020  30.390  59.143  1.00 14.66 ? 756  LEU   B CB    1 
ATOM   14665 C  CG    . LEU   B  1  758  ? 14.583  29.851  60.465  1.00 14.24 ? 756  LEU   B CG    1 
ATOM   14666 C  CD1   . LEU   B  1  758  ? 15.194  30.962  61.315  1.00 15.88 ? 756  LEU   B CD1   1 
ATOM   14667 C  CD2   . LEU   B  1  758  ? 13.473  29.166  61.247  1.00 16.39 ? 756  LEU   B CD2   1 
ATOM   14668 N  N     . GLN   B  1  759  ? 17.420  30.724  58.173  1.00 13.67 ? 757  GLN   B N     1 
ATOM   14669 C  CA    . GLN   B  1  759  ? 18.657  29.998  57.973  1.00 14.22 ? 757  GLN   B CA    1 
ATOM   14670 C  C     . GLN   B  1  759  ? 19.362  29.884  59.315  1.00 14.21 ? 757  GLN   B C     1 
ATOM   14671 O  O     . GLN   B  1  759  ? 19.337  30.823  60.119  1.00 15.46 ? 757  GLN   B O     1 
ATOM   14672 C  CB    . GLN   B  1  759  ? 19.525  30.755  56.976  1.00 14.16 ? 757  GLN   B CB    1 
ATOM   14673 C  CG    . GLN   B  1  759  ? 18.907  30.787  55.572  1.00 15.68 ? 757  GLN   B CG    1 
ATOM   14674 C  CD    . GLN   B  1  759  ? 19.698  31.643  54.635  1.00 14.65 ? 757  GLN   B CD    1 
ATOM   14675 O  OE1   . GLN   B  1  759  ? 20.535  31.143  53.894  1.00 17.87 ? 757  GLN   B OE1   1 
ATOM   14676 N  NE2   . GLN   B  1  759  ? 19.459  32.938  54.668  1.00 15.89 ? 757  GLN   B NE2   1 
ATOM   14677 N  N     . LEU   B  1  760  ? 19.975  28.735  59.552  1.00 14.43 ? 758  LEU   B N     1 
ATOM   14678 C  CA    . LEU   B  1  760  ? 20.682  28.453  60.792  1.00 13.40 ? 758  LEU   B CA    1 
ATOM   14679 C  C     . LEU   B  1  760  ? 22.170  28.489  60.509  1.00 15.12 ? 758  LEU   B C     1 
ATOM   14680 O  O     . LEU   B  1  760  ? 22.646  27.791  59.614  1.00 15.62 ? 758  LEU   B O     1 
ATOM   14681 C  CB    . LEU   B  1  760  ? 20.327  27.062  61.310  1.00 15.47 ? 758  LEU   B CB    1 
ATOM   14682 C  CG    . LEU   B  1  760  ? 21.022  26.700  62.625  1.00 14.02 ? 758  LEU   B CG    1 
ATOM   14683 C  CD1   . LEU   B  1  760  ? 20.301  27.373  63.776  1.00 17.20 ? 758  LEU   B CD1   1 
ATOM   14684 C  CD2   . LEU   B  1  760  ? 21.090  25.195  62.819  1.00 17.55 ? 758  LEU   B CD2   1 
ATOM   14685 N  N     . LEU   B  1  761  ? 22.912  29.272  61.288  1.00 15.52 ? 759  LEU   B N     1 
ATOM   14686 C  CA    . LEU   B  1  761  ? 24.352  29.422  61.117  1.00 15.03 ? 759  LEU   B CA    1 
ATOM   14687 C  C     . LEU   B  1  761  ? 25.031  29.072  62.433  1.00 14.12 ? 759  LEU   B C     1 
ATOM   14688 O  O     . LEU   B  1  761  ? 25.311  29.967  63.246  1.00 15.55 ? 759  LEU   B O     1 
ATOM   14689 C  CB    . LEU   B  1  761  ? 24.732  30.836  60.682  1.00 16.10 ? 759  LEU   B CB    1 
ATOM   14690 C  CG    . LEU   B  1  761  ? 24.196  31.389  59.356  1.00 16.57 ? 759  LEU   B CG    1 
ATOM   14691 C  CD1   . LEU   B  1  761  ? 24.256  30.351  58.223  1.00 18.54 ? 759  LEU   B CD1   1 
ATOM   14692 C  CD2   . LEU   B  1  761  ? 22.811  31.961  59.513  1.00 19.81 ? 759  LEU   B CD2   1 
ATOM   14693 N  N     . PRO   B  1  762  ? 25.273  27.798  62.705  1.00 14.19 ? 760  PRO   B N     1 
ATOM   14694 C  CA    . PRO   B  1  762  ? 25.982  27.451  63.944  1.00 14.65 ? 760  PRO   B CA    1 
ATOM   14695 C  C     . PRO   B  1  762  ? 27.400  27.978  63.908  1.00 15.22 ? 760  PRO   B C     1 
ATOM   14696 O  O     . PRO   B  1  762  ? 28.001  28.156  62.844  1.00 15.57 ? 760  PRO   B O     1 
ATOM   14697 C  CB    . PRO   B  1  762  ? 25.988  25.917  63.945  1.00 14.86 ? 760  PRO   B CB    1 
ATOM   14698 C  CG    . PRO   B  1  762  ? 24.957  25.511  62.932  1.00 14.99 ? 760  PRO   B CG    1 
ATOM   14699 C  CD    . PRO   B  1  762  ? 24.963  26.601  61.908  1.00 14.05 ? 760  PRO   B CD    1 
ATOM   14700 N  N     . GLY   B  1  763  ? 27.947  28.196  65.095  1.00 14.60 ? 761  GLY   B N     1 
ATOM   14701 C  CA    . GLY   B  1  763  ? 29.337  28.576  65.222  1.00 15.36 ? 761  GLY   B CA    1 
ATOM   14702 C  C     . GLY   B  1  763  ? 29.501  29.515  66.390  1.00 14.18 ? 761  GLY   B C     1 
ATOM   14703 O  O     . GLY   B  1  763  ? 28.591  29.718  67.188  1.00 15.94 ? 761  GLY   B O     1 
ATOM   14704 N  N     . ASP   B  1  764  ? 30.708  30.038  66.500  1.00 17.20 ? 762  ASP   B N     1 
ATOM   14705 C  CA    . ASP   B  1  764  ? 31.050  30.826  67.666  1.00 17.96 ? 762  ASP   B CA    1 
ATOM   14706 C  C     . ASP   B  1  764  ? 30.802  32.303  67.376  1.00 19.60 ? 762  ASP   B C     1 
ATOM   14707 O  O     . ASP   B  1  764  ? 30.084  32.665  66.435  1.00 17.14 ? 762  ASP   B O     1 
ATOM   14708 C  CB    . ASP   B  1  764  ? 32.453  30.464  68.156  1.00 20.98 ? 762  ASP   B CB    1 
ATOM   14709 C  CG    . ASP   B  1  764  ? 33.556  30.887  67.199  1.00 25.24 ? 762  ASP   B CG    1 
ATOM   14710 O  OD1   . ASP   B  1  764  ? 33.329  31.678  66.265  1.00 20.96 ? 762  ASP   B OD1   1 
ATOM   14711 O  OD2   . ASP   B  1  764  ? 34.700  30.418  67.396  1.00 32.70 ? 762  ASP   B OD2   1 
ATOM   14712 N  N     . GLY   B  1  765  ? 31.386  33.172  68.198  1.00 18.16 ? 763  GLY   B N     1 
ATOM   14713 C  CA    . GLY   B  1  765  ? 31.144  34.590  68.052  1.00 17.54 ? 763  GLY   B CA    1 
ATOM   14714 C  C     . GLY   B  1  765  ? 31.631  35.169  66.747  1.00 17.41 ? 763  GLY   B C     1 
ATOM   14715 O  O     . GLY   B  1  765  ? 31.129  36.215  66.334  1.00 18.84 ? 763  GLY   B O     1 
ATOM   14716 N  N     . ARG   B  1  766  ? 32.603  34.527  66.090  1.00 18.31 ? 764  ARG   B N     1 
ATOM   14717 C  CA    . ARG   B  1  766  ? 33.051  35.030  64.793  1.00 19.86 ? 764  ARG   B CA    1 
ATOM   14718 C  C     . ARG   B  1  766  ? 31.956  34.904  63.748  1.00 16.99 ? 764  ARG   B C     1 
ATOM   14719 O  O     . ARG   B  1  766  ? 31.866  35.742  62.843  1.00 18.40 ? 764  ARG   B O     1 
ATOM   14720 C  CB    . ARG   B  1  766  ? 34.287  34.270  64.314  1.00 20.92 ? 764  ARG   B CB    1 
ATOM   14721 C  CG    . ARG   B  1  766  ? 35.483  34.376  65.236  1.00 23.28 ? 764  ARG   B CG    1 
ATOM   14722 C  CD    . ARG   B  1  766  ? 36.551  33.338  64.867  1.00 32.88 ? 764  ARG   B CD    1 
ATOM   14723 N  NE    . ARG   B  1  766  ? 36.032  31.979  64.984  1.00 37.16 ? 764  ARG   B NE    1 
ATOM   14724 C  CZ    . ARG   B  1  766  ? 36.689  30.884  64.623  1.00 43.87 ? 764  ARG   B CZ    1 
ATOM   14725 N  NH1   . ARG   B  1  766  ? 37.907  30.945  64.112  1.00 41.11 ? 764  ARG   B NH1   1 
ATOM   14726 N  NH2   . ARG   B  1  766  ? 36.105  29.698  64.775  1.00 41.03 ? 764  ARG   B NH2   1 
ATOM   14727 N  N     . VAL   B  1  767  ? 31.115  33.878  63.871  1.00 15.96 ? 765  VAL   B N     1 
ATOM   14728 C  CA    . VAL   B  1  767  ? 29.987  33.743  62.963  1.00 17.01 ? 765  VAL   B CA    1 
ATOM   14729 C  C     . VAL   B  1  767  ? 28.963  34.822  63.259  1.00 15.77 ? 765  VAL   B C     1 
ATOM   14730 O  O     . VAL   B  1  767  ? 28.443  35.472  62.342  1.00 16.73 ? 765  VAL   B O     1 
ATOM   14731 C  CB    . VAL   B  1  767  ? 29.395  32.330  63.063  1.00 16.37 ? 765  VAL   B CB    1 
ATOM   14732 C  CG1   . VAL   B  1  767  ? 28.201  32.196  62.145  1.00 16.01 ? 765  VAL   B CG1   1 
ATOM   14733 C  CG2   . VAL   B  1  767  ? 30.429  31.309  62.714  1.00 17.26 ? 765  VAL   B CG2   1 
ATOM   14734 N  N     . GLY   B  1  768  ? 28.683  35.060  64.543  1.00 15.78 ? 766  GLY   B N     1 
ATOM   14735 C  CA    . GLY   B  1  768  ? 27.801  36.158  64.887  1.00 15.93 ? 766  GLY   B CA    1 
ATOM   14736 C  C     . GLY   B  1  768  ? 28.314  37.482  64.359  1.00 15.43 ? 766  GLY   B C     1 
ATOM   14737 O  O     . GLY   B  1  768  ? 27.559  38.278  63.793  1.00 15.95 ? 766  GLY   B O     1 
ATOM   14738 N  N     . ALA   B  1  769  ? 29.617  37.730  64.525  1.00 16.75 ? 767  ALA   B N     1 
ATOM   14739 C  CA    . ALA   B  1  769  ? 30.170  39.002  64.075  1.00 16.55 ? 767  ALA   B CA    1 
ATOM   14740 C  C     . ALA   B  1  769  ? 30.105  39.137  62.559  1.00 17.01 ? 767  ALA   B C     1 
ATOM   14741 O  O     . ALA   B  1  769  ? 29.809  40.222  62.045  1.00 17.68 ? 767  ALA   B O     1 
ATOM   14742 C  CB    . ALA   B  1  769  ? 31.601  39.156  64.590  1.00 17.79 ? 767  ALA   B CB    1 
ATOM   14743 N  N     . ALA   B  1  770  ? 30.335  38.042  61.830  1.00 16.67 ? 768  ALA   B N     1 
ATOM   14744 C  CA    . ALA   B  1  770  ? 30.263  38.107  60.376  1.00 16.80 ? 768  ALA   B CA    1 
ATOM   14745 C  C     . ALA   B  1  770  ? 28.846  38.405  59.918  1.00 16.93 ? 768  ALA   B C     1 
ATOM   14746 O  O     . ALA   B  1  770  ? 28.641  39.140  58.949  1.00 18.86 ? 768  ALA   B O     1 
ATOM   14747 C  CB    . ALA   B  1  770  ? 30.749  36.801  59.759  1.00 18.63 ? 768  ALA   B CB    1 
ATOM   14748 N  N     . LEU   B  1  771  ? 27.852  37.845  60.606  1.00 16.07 ? 769  LEU   B N     1 
ATOM   14749 C  CA    . LEU   B  1  771  ? 26.468  38.141  60.258  1.00 15.80 ? 769  LEU   B CA    1 
ATOM   14750 C  C     . LEU   B  1  771  ? 26.138  39.597  60.536  1.00 15.52 ? 769  LEU   B C     1 
ATOM   14751 O  O     . LEU   B  1  771  ? 25.501  40.264  59.719  1.00 17.55 ? 769  LEU   B O     1 
ATOM   14752 C  CB    . LEU   B  1  771  ? 25.521  37.237  61.053  1.00 14.36 ? 769  LEU   B CB    1 
ATOM   14753 C  CG    . LEU   B  1  771  ? 25.605  35.768  60.657  1.00 14.27 ? 769  LEU   B CG    1 
ATOM   14754 C  CD1   . LEU   B  1  771  ? 24.813  34.936  61.637  1.00 16.61 ? 769  LEU   B CD1   1 
ATOM   14755 C  CD2   . LEU   B  1  771  ? 25.076  35.575  59.226  1.00 16.99 ? 769  LEU   B CD2   1 
ATOM   14756 N  N     . VAL   B  1  772  ? 26.566  40.104  61.688  1.00 15.94 ? 770  VAL   B N     1 
ATOM   14757 C  CA    . VAL   B  1  772  ? 26.261  41.478  62.074  1.00 15.88 ? 770  VAL   B CA    1 
ATOM   14758 C  C     . VAL   B  1  772  ? 26.848  42.456  61.079  1.00 18.56 ? 770  VAL   B C     1 
ATOM   14759 O  O     . VAL   B  1  772  ? 26.226  43.474  60.741  1.00 20.54 ? 770  VAL   B O     1 
ATOM   14760 C  CB    . VAL   B  1  772  ? 26.792  41.744  63.493  1.00 16.59 ? 770  VAL   B CB    1 
ATOM   14761 C  CG1   . VAL   B  1  772  ? 26.802  43.228  63.804  1.00 19.01 ? 770  VAL   B CG1   1 
ATOM   14762 C  CG2   . VAL   B  1  772  ? 25.962  40.992  64.521  1.00 16.58 ? 770  VAL   B CG2   1 
ATOM   14763 N  N     . ALA   B  1  773  ? 28.060  42.171  60.599  1.00 18.39 ? 771  ALA   B N     1 
ATOM   14764 C  CA    . ALA   B  1  773  ? 28.756  43.095  59.718  1.00 18.70 ? 771  ALA   B CA    1 
ATOM   14765 C  C     . ALA   B  1  773  ? 28.282  43.013  58.277  1.00 22.00 ? 771  ALA   B C     1 
ATOM   14766 O  O     . ALA   B  1  773  ? 28.656  43.875  57.472  1.00 22.95 ? 771  ALA   B O     1 
ATOM   14767 C  CB    . ALA   B  1  773  ? 30.258  42.816  59.766  1.00 21.71 ? 771  ALA   B CB    1 
ATOM   14768 N  N     . ALA   B  1  774  ? 27.492  42.000  57.929  1.00 19.45 ? 772  ALA   B N     1 
ATOM   14769 C  CA    . ALA   B  1  774  ? 27.106  41.783  56.540  1.00 19.20 ? 772  ALA   B CA    1 
ATOM   14770 C  C     . ALA   B  1  774  ? 26.295  42.958  56.013  1.00 22.09 ? 772  ALA   B C     1 
ATOM   14771 O  O     . ALA   B  1  774  ? 25.487  43.553  56.731  1.00 22.31 ? 772  ALA   B O     1 
ATOM   14772 C  CB    . ALA   B  1  774  ? 26.308  40.485  56.404  1.00 20.74 ? 772  ALA   B CB    1 
ATOM   14773 N  N     . ALA   B  1  775  ? 26.494  43.264  54.727  1.00 23.30 ? 773  ALA   B N     1 
ATOM   14774 C  CA    . ALA   B  1  775  ? 25.964  44.496  54.152  1.00 25.83 ? 773  ALA   B CA    1 
ATOM   14775 C  C     . ALA   B  1  775  ? 24.447  44.581  54.260  1.00 22.90 ? 773  ALA   B C     1 
ATOM   14776 O  O     . ALA   B  1  775  ? 23.894  45.664  54.474  1.00 24.03 ? 773  ALA   B O     1 
ATOM   14777 C  CB    . ALA   B  1  775  ? 26.391  44.592  52.689  1.00 26.69 ? 773  ALA   B CB    1 
ATOM   14778 N  N     . GLU   B  1  776  ? 23.757  43.460  54.104  1.00 20.44 ? 774  GLU   B N     1 
ATOM   14779 C  CA    . GLU   B  1  776  ? 22.306  43.477  54.016  1.00 19.08 ? 774  GLU   B CA    1 
ATOM   14780 C  C     . GLU   B  1  776  ? 21.618  43.279  55.359  1.00 17.63 ? 774  GLU   B C     1 
ATOM   14781 O  O     . GLU   B  1  776  ? 20.389  43.277  55.409  1.00 18.33 ? 774  GLU   B O     1 
ATOM   14782 C  CB    . GLU   B  1  776  ? 21.823  42.408  53.034  1.00 19.08 ? 774  GLU   B CB    1 
ATOM   14783 C  CG    . GLU   B  1  776  ? 22.405  42.537  51.615  1.00 26.44 ? 774  GLU   B CG    1 
ATOM   14784 C  CD    . GLU   B  1  776  ? 23.772  41.849  51.444  1.00 32.54 ? 774  GLU   B CD    1 
ATOM   14785 O  OE1   . GLU   B  1  776  ? 24.300  41.247  52.411  1.00 25.55 ? 774  GLU   B OE1   1 
ATOM   14786 O  OE2   . GLU   B  1  776  ? 24.330  41.916  50.324  1.00 35.45 ? 774  GLU   B OE2   1 
ATOM   14787 N  N     . THR   B  1  777  ? 22.369  43.115  56.438  1.00 16.42 ? 775  THR   B N     1 
ATOM   14788 C  CA    . THR   B  1  777  ? 21.755  42.970  57.750  1.00 16.29 ? 775  THR   B CA    1 
ATOM   14789 C  C     . THR   B  1  777  ? 21.024  44.248  58.106  1.00 17.42 ? 775  THR   B C     1 
ATOM   14790 O  O     . THR   B  1  777  ? 21.600  45.339  58.061  1.00 18.34 ? 775  THR   B O     1 
ATOM   14791 C  CB    . THR   B  1  777  ? 22.844  42.650  58.759  1.00 16.37 ? 775  THR   B CB    1 
ATOM   14792 O  OG1   . THR   B  1  777  ? 23.342  41.348  58.449  1.00 18.71 ? 775  THR   B OG1   1 
ATOM   14793 C  CG2   . THR   B  1  777  ? 22.286  42.665  60.175  1.00 17.03 ? 775  THR   B CG2   1 
ATOM   14794 N  N     . ALA   B  1  778  ? 19.731  44.115  58.413  1.00 14.68 ? 776  ALA   B N     1 
ATOM   14795 C  CA    . ALA   B  1  778  ? 18.865  45.257  58.636  1.00 15.66 ? 776  ALA   B CA    1 
ATOM   14796 C  C     . ALA   B  1  778  ? 18.477  45.418  60.091  1.00 15.05 ? 776  ALA   B C     1 
ATOM   14797 O  O     . ALA   B  1  778  ? 17.846  46.419  60.445  1.00 16.78 ? 776  ALA   B O     1 
ATOM   14798 C  CB    . ALA   B  1  778  ? 17.604  45.123  57.774  1.00 16.12 ? 776  ALA   B CB    1 
ATOM   14799 N  N     . GLY   B  1  779  ? 18.842  44.470  60.938  1.00 14.23 ? 777  GLY   B N     1 
ATOM   14800 C  CA    . GLY   B  1  779  ? 18.531  44.582  62.347  1.00 14.69 ? 777  GLY   B CA    1 
ATOM   14801 C  C     . GLY   B  1  779  ? 19.196  43.427  63.048  1.00 14.97 ? 777  GLY   B C     1 
ATOM   14802 O  O     . GLY   B  1  779  ? 19.478  42.398  62.424  1.00 14.38 ? 777  GLY   B O     1 
ATOM   14803 N  N     . VAL   B  1  780  ? 19.482  43.591  64.335  1.00 14.42 ? 778  VAL   B N     1 
ATOM   14804 C  CA    . VAL   B  1  780  ? 20.118  42.553  65.126  1.00 13.78 ? 778  VAL   B CA    1 
ATOM   14805 C  C     . VAL   B  1  780  ? 19.337  42.393  66.419  1.00 13.93 ? 778  VAL   B C     1 
ATOM   14806 O  O     . VAL   B  1  780  ? 19.028  43.383  67.096  1.00 14.70 ? 778  VAL   B O     1 
ATOM   14807 C  CB    . VAL   B  1  780  ? 21.596  42.879  65.417  1.00 14.44 ? 778  VAL   B CB    1 
ATOM   14808 C  CG1   . VAL   B  1  780  ? 22.199  41.817  66.303  1.00 14.89 ? 778  VAL   B CG1   1 
ATOM   14809 C  CG2   . VAL   B  1  780  ? 22.366  42.990  64.128  1.00 15.84 ? 778  VAL   B CG2   1 
ATOM   14810 N  N     . MET   B  1  781  ? 19.036  41.157  66.762  1.00 13.01 ? 779  MET   B N     1 
ATOM   14811 C  CA    . MET   B  1  781  ? 18.441  40.809  68.045  1.00 12.73 ? 779  MET   B CA    1 
ATOM   14812 C  C     . MET   B  1  781  ? 19.480  39.988  68.773  1.00 12.91 ? 779  MET   B C     1 
ATOM   14813 O  O     . MET   B  1  781  ? 19.863  38.900  68.315  1.00 13.95 ? 779  MET   B O     1 
ATOM   14814 C  CB    . MET   B  1  781  ? 17.161  40.008  67.845  1.00 12.63 ? 779  MET   B CB    1 
ATOM   14815 C  CG    . MET   B  1  781  ? 16.173  40.783  67.011  1.00 14.32 ? 779  MET   B CG    1 
ATOM   14816 S  SD    . MET   B  1  781  ? 14.720  39.827  66.633  1.00 14.63 ? 779  MET   B SD    1 
ATOM   14817 C  CE    . MET   B  1  781  ? 13.863  39.893  68.195  1.00 14.65 ? 779  MET   B CE    1 
ATOM   14818 N  N     . PHE   B  1  782  ? 19.995  40.537  69.861  1.00 13.18 ? 780  PHE   B N     1 
ATOM   14819 C  CA    . PHE   B  1  782  ? 21.067  39.918  70.612  1.00 13.51 ? 780  PHE   B CA    1 
ATOM   14820 C  C     . PHE   B  1  782  ? 20.606  39.697  72.040  1.00 13.32 ? 780  PHE   B C     1 
ATOM   14821 O  O     . PHE   B  1  782  ? 20.061  40.604  72.670  1.00 13.98 ? 780  PHE   B O     1 
ATOM   14822 C  CB    . PHE   B  1  782  ? 22.291  40.823  70.674  1.00 14.00 ? 780  PHE   B CB    1 
ATOM   14823 C  CG    . PHE   B  1  782  ? 23.357  40.287  71.560  1.00 13.39 ? 780  PHE   B CG    1 
ATOM   14824 C  CD1   . PHE   B  1  782  ? 24.176  39.258  71.115  1.00 13.41 ? 780  PHE   B CD1   1 
ATOM   14825 C  CD2   . PHE   B  1  782  ? 23.533  40.783  72.849  1.00 14.28 ? 780  PHE   B CD2   1 
ATOM   14826 C  CE1   . PHE   B  1  782  ? 25.142  38.731  71.906  1.00 14.02 ? 780  PHE   B CE1   1 
ATOM   14827 C  CE2   . PHE   B  1  782  ? 24.527  40.249  73.666  1.00 15.12 ? 780  PHE   B CE2   1 
ATOM   14828 C  CZ    . PHE   B  1  782  ? 25.348  39.237  73.175  1.00 14.54 ? 780  PHE   B CZ    1 
ATOM   14829 N  N     . THR   B  1  783  ? 20.845  38.502  72.548  1.00 12.95 ? 781  THR   B N     1 
ATOM   14830 C  CA    . THR   B  1  783  ? 20.721  38.248  73.969  1.00 14.15 ? 781  THR   B CA    1 
ATOM   14831 C  C     . THR   B  1  783  ? 21.988  37.534  74.383  1.00 14.47 ? 781  THR   B C     1 
ATOM   14832 O  O     . THR   B  1  783  ? 22.400  36.568  73.739  1.00 14.59 ? 781  THR   B O     1 
ATOM   14833 C  CB    . THR   B  1  783  ? 19.470  37.419  74.293  1.00 14.31 ? 781  THR   B CB    1 
ATOM   14834 O  OG1   . THR   B  1  783  ? 18.307  38.102  73.817  1.00 14.22 ? 781  THR   B OG1   1 
ATOM   14835 C  CG2   . THR   B  1  783  ? 19.360  37.250  75.807  1.00 14.79 ? 781  THR   B CG2   1 
ATOM   14836 N  N     . GLY   B  1  784  ? 22.628  38.031  75.428  1.00 13.71 ? 782  GLY   B N     1 
ATOM   14837 C  CA    . GLY   B  1  784  ? 23.933  37.534  75.800  1.00 13.90 ? 782  GLY   B CA    1 
ATOM   14838 C  C     . GLY   B  1  784  ? 24.586  38.509  76.751  1.00 14.65 ? 782  GLY   B C     1 
ATOM   14839 O  O     . GLY   B  1  784  ? 23.914  39.332  77.371  1.00 15.41 ? 782  GLY   B O     1 
ATOM   14840 N  N     . SER   B  1  785  ? 25.896  38.404  76.837  1.00 15.35 ? 783  SER   B N     1 
ATOM   14841 C  CA    . SER   B  1  785  ? 26.604  39.231  77.799  1.00 16.51 ? 783  SER   B CA    1 
ATOM   14842 C  C     . SER   B  1  785  ? 26.687  40.670  77.322  1.00 18.14 ? 783  SER   B C     1 
ATOM   14843 O  O     . SER   B  1  785  ? 26.725  40.961  76.120  1.00 16.66 ? 783  SER   B O     1 
ATOM   14844 C  CB    . SER   B  1  785  ? 28.007  38.684  78.023  1.00 17.86 ? 783  SER   B CB    1 
ATOM   14845 O  OG    . SER   B  1  785  ? 28.771  38.765  76.840  1.00 17.57 ? 783  SER   B OG    1 
ATOM   14846 N  N     . THR   B  1  786  ? 26.743  41.589  78.293  1.00 17.72 ? 784  THR   B N     1 
ATOM   14847 C  CA    . THR   B  1  786  ? 26.860  43.003  77.968  1.00 18.68 ? 784  THR   B CA    1 
ATOM   14848 C  C     . THR   B  1  786  ? 28.129  43.265  77.162  1.00 17.41 ? 784  THR   B C     1 
ATOM   14849 O  O     . THR   B  1  786  ? 28.131  44.059  76.216  1.00 19.81 ? 784  THR   B O     1 
ATOM   14850 C  CB    . THR   B  1  786  ? 26.811  43.827  79.270  1.00 18.95 ? 784  THR   B CB    1 
ATOM   14851 O  OG1   . THR   B  1  786  ? 25.636  43.467  80.016  1.00 20.44 ? 784  THR   B OG1   1 
ATOM   14852 C  CG2   . THR   B  1  786  ? 26.758  45.304  78.959  1.00 23.73 ? 784  THR   B CG2   1 
ATOM   14853 N  N     . GLU   B  1  787  ? 29.218  42.572  77.507  1.00 20.30 ? 785  GLU   B N     1 
ATOM   14854 C  CA    . GLU   B  1  787  ? 30.486  42.756  76.810  1.00 19.53 ? 785  GLU   B CA    1 
ATOM   14855 C  C     . GLU   B  1  787  ? 30.356  42.462  75.317  1.00 19.40 ? 785  GLU   B C     1 
ATOM   14856 O  O     . GLU   B  1  787  ? 30.857  43.216  74.468  1.00 19.10 ? 785  GLU   B O     1 
ATOM   14857 C  CB    . GLU   B  1  787  ? 31.544  41.836  77.431  1.00 21.94 ? 785  GLU   B CB    1 
ATOM   14858 N  N     . VAL   B  1  788  ? 29.678  41.363  74.979  1.00 17.56 ? 786  VAL   B N     1 
ATOM   14859 C  CA    . VAL   B  1  788  ? 29.507  41.012  73.575  1.00 18.12 ? 786  VAL   B CA    1 
ATOM   14860 C  C     . VAL   B  1  788  ? 28.565  41.995  72.894  1.00 15.81 ? 786  VAL   B C     1 
ATOM   14861 O  O     . VAL   B  1  788  ? 28.793  42.405  71.759  1.00 16.79 ? 786  VAL   B O     1 
ATOM   14862 C  CB    . VAL   B  1  788  ? 29.027  39.557  73.448  1.00 17.76 ? 786  VAL   B CB    1 
ATOM   14863 C  CG1   . VAL   B  1  788  ? 28.623  39.271  72.018  1.00 16.82 ? 786  VAL   B CG1   1 
ATOM   14864 C  CG2   . VAL   B  1  788  ? 30.154  38.598  73.857  1.00 18.89 ? 786  VAL   B CG2   1 
ATOM   14865 N  N     . ALA   B  1  789  ? 27.512  42.415  73.595  1.00 15.87 ? 787  ALA   B N     1 
ATOM   14866 C  CA    . ALA   B  1  789  ? 26.582  43.368  73.004  1.00 15.35 ? 787  ALA   B CA    1 
ATOM   14867 C  C     . ALA   B  1  789  ? 27.298  44.640  72.586  1.00 15.00 ? 787  ALA   B C     1 
ATOM   14868 O  O     . ALA   B  1  789  ? 26.971  45.234  71.559  1.00 16.11 ? 787  ALA   B O     1 
ATOM   14869 C  CB    . ALA   B  1  789  ? 25.474  43.705  73.992  1.00 15.17 ? 787  ALA   B CB    1 
ATOM   14870 N  N     . ARG   B  1  790  ? 28.271  45.090  73.392  1.00 16.47 ? 788  ARG   B N     1 
ATOM   14871 C  CA    . ARG   B  1  790  ? 28.992  46.310  73.035  1.00 18.62 ? 788  ARG   B CA    1 
ATOM   14872 C  C     . ARG   B  1  790  ? 29.762  46.140  71.744  1.00 17.71 ? 788  ARG   B C     1 
ATOM   14873 O  O     . ARG   B  1  790  ? 29.876  47.084  70.955  1.00 19.79 ? 788  ARG   B O     1 
ATOM   14874 C  CB    . ARG   B  1  790  ? 30.004  46.670  74.117  1.00 21.36 ? 788  ARG   B CB    1 
ATOM   14875 C  CG    . ARG   B  1  790  ? 29.425  47.161  75.375  1.00 23.30 ? 788  ARG   B CG    1 
ATOM   14876 C  CD    . ARG   B  1  790  ? 30.549  47.682  76.263  1.00 28.42 ? 788  ARG   B CD    1 
ATOM   14877 N  NE    . ARG   B  1  790  ? 30.032  47.899  77.597  1.00 38.27 ? 788  ARG   B NE    1 
ATOM   14878 C  CZ    . ARG   B  1  790  ? 29.294  48.943  77.934  1.00 36.77 ? 788  ARG   B CZ    1 
ATOM   14879 N  NH1   . ARG   B  1  790  ? 29.007  49.899  77.058  1.00 32.47 ? 788  ARG   B NH1   1 
ATOM   14880 N  NH2   . ARG   B  1  790  ? 28.835  49.031  79.178  1.00 41.44 ? 788  ARG   B NH2   1 
ATOM   14881 N  N     . LEU   B  1  791  ? 30.328  44.951  71.521  1.00 17.85 ? 789  LEU   B N     1 
ATOM   14882 C  CA    . LEU   B  1  791  ? 31.050  44.723  70.278  1.00 17.53 ? 789  LEU   B CA    1 
ATOM   14883 C  C     . LEU   B  1  791  ? 30.107  44.796  69.093  1.00 19.42 ? 789  LEU   B C     1 
ATOM   14884 O  O     . LEU   B  1  791  ? 30.432  45.381  68.055  1.00 20.47 ? 789  LEU   B O     1 
ATOM   14885 C  CB    . LEU   B  1  791  ? 31.733  43.362  70.314  1.00 19.84 ? 789  LEU   B CB    1 
ATOM   14886 C  CG    . LEU   B  1  791  ? 32.770  43.181  71.417  1.00 21.09 ? 789  LEU   B CG    1 
ATOM   14887 C  CD1   . LEU   B  1  791  ? 33.331  41.771  71.323  1.00 22.06 ? 789  LEU   B CD1   1 
ATOM   14888 C  CD2   . LEU   B  1  791  ? 33.882  44.253  71.312  1.00 24.16 ? 789  LEU   B CD2   1 
ATOM   14889 N  N     . ILE   B  1  792  ? 28.915  44.221  69.246  1.00 18.92 ? 790  ILE   B N     1 
ATOM   14890 C  CA    . ILE   B  1  792  ? 27.936  44.242  68.169  1.00 17.82 ? 790  ILE   B CA    1 
ATOM   14891 C  C     . ILE   B  1  792  ? 27.475  45.663  67.909  1.00 17.03 ? 790  ILE   B C     1 
ATOM   14892 O  O     . ILE   B  1  792  ? 27.351  46.097  66.757  1.00 18.35 ? 790  ILE   B O     1 
ATOM   14893 C  CB    . ILE   B  1  792  ? 26.765  43.326  68.554  1.00 16.07 ? 790  ILE   B CB    1 
ATOM   14894 C  CG1   . ILE   B  1  792  ? 27.234  41.871  68.550  1.00 15.50 ? 790  ILE   B CG1   1 
ATOM   14895 C  CG2   . ILE   B  1  792  ? 25.555  43.599  67.652  1.00 16.15 ? 790  ILE   B CG2   1 
ATOM   14896 C  CD1   . ILE   B  1  792  ? 26.241  40.926  69.124  1.00 16.61 ? 790  ILE   B CD1   1 
ATOM   14897 N  N     . GLN   B  1  793  ? 27.202  46.402  68.980  1.00 17.45 ? 791  GLN   B N     1 
ATOM   14898 C  CA    . GLN   B  1  793  ? 26.794  47.792  68.853  1.00 17.68 ? 791  GLN   B CA    1 
ATOM   14899 C  C     . GLN   B  1  793  ? 27.832  48.602  68.095  1.00 17.13 ? 791  GLN   B C     1 
ATOM   14900 O  O     . GLN   B  1  793  ? 27.483  49.421  67.233  1.00 18.91 ? 791  GLN   B O     1 
ATOM   14901 C  CB    . GLN   B  1  793  ? 26.605  48.365  70.253  1.00 18.05 ? 791  GLN   B CB    1 
ATOM   14902 C  CG    . GLN   B  1  793  ? 26.207  49.796  70.283  1.00 19.57 ? 791  GLN   B CG    1 
ATOM   14903 C  CD    . GLN   B  1  793  ? 26.498  50.416  71.616  1.00 22.53 ? 791  GLN   B CD    1 
ATOM   14904 O  OE1   . GLN   B  1  793  ? 27.523  50.124  72.244  1.00 24.33 ? 791  GLN   B OE1   1 
ATOM   14905 N  NE2   . GLN   B  1  793  ? 25.599  51.268  72.073  1.00 27.05 ? 791  GLN   B NE2   1 
ATOM   14906 N  N     . ALA   B  1  794  ? 29.113  48.375  68.391  1.00 18.67 ? 792  ALA   B N     1 
ATOM   14907 C  CA    . ALA   B  1  794  ? 30.171  49.079  67.675  1.00 19.38 ? 792  ALA   B CA    1 
ATOM   14908 C  C     . ALA   B  1  794  ? 30.174  48.722  66.193  1.00 20.04 ? 792  ALA   B C     1 
ATOM   14909 O  O     . ALA   B  1  794  ? 30.332  49.605  65.340  1.00 22.15 ? 792  ALA   B O     1 
ATOM   14910 C  CB    . ALA   B  1  794  ? 31.528  48.792  68.323  1.00 22.84 ? 792  ALA   B CB    1 
ATOM   14911 N  N     . GLN   B  1  795  ? 30.008  47.435  65.865  1.00 19.83 ? 793  GLN   B N     1 
ATOM   14912 C  CA    . GLN   B  1  795  ? 29.939  47.035  64.458  1.00 20.99 ? 793  GLN   B CA    1 
ATOM   14913 C  C     . GLN   B  1  795  ? 28.809  47.763  63.749  1.00 20.59 ? 793  GLN   B C     1 
ATOM   14914 O  O     . GLN   B  1  795  ? 28.972  48.266  62.632  1.00 21.61 ? 793  GLN   B O     1 
ATOM   14915 C  CB    . GLN   B  1  795  ? 29.701  45.524  64.322  1.00 22.94 ? 793  GLN   B CB    1 
ATOM   14916 C  CG    . GLN   B  1  795  ? 30.824  44.574  64.665  1.00 25.89 ? 793  GLN   B CG    1 
ATOM   14917 C  CD    . GLN   B  1  795  ? 30.408  43.110  64.462  1.00 27.87 ? 793  GLN   B CD    1 
ATOM   14918 O  OE1   . GLN   B  1  795  ? 29.785  42.502  65.332  1.00 28.89 ? 793  GLN   B OE1   1 
ATOM   14919 N  NE2   . GLN   B  1  795  ? 30.753  42.548  63.317  1.00 25.00 ? 793  GLN   B NE2   1 
ATOM   14920 N  N     . LEU   B  1  796  ? 27.638  47.818  64.385  1.00 18.01 ? 794  LEU   B N     1 
ATOM   14921 C  CA    . LEU   B  1  796  ? 26.467  48.350  63.703  1.00 17.77 ? 794  LEU   B CA    1 
ATOM   14922 C  C     . LEU   B  1  796  ? 26.545  49.856  63.535  1.00 20.51 ? 794  LEU   B C     1 
ATOM   14923 O  O     . LEU   B  1  796  ? 25.983  50.399  62.580  1.00 22.17 ? 794  LEU   B O     1 
ATOM   14924 C  CB    . LEU   B  1  796  ? 25.213  48.016  64.497  1.00 18.11 ? 794  LEU   B CB    1 
ATOM   14925 C  CG    . LEU   B  1  796  ? 24.792  46.557  64.455  1.00 18.41 ? 794  LEU   B CG    1 
ATOM   14926 C  CD1   . LEU   B  1  796  ? 23.537  46.409  65.293  1.00 19.62 ? 794  LEU   B CD1   1 
ATOM   14927 C  CD2   . LEU   B  1  796  ? 24.495  46.144  63.027  1.00 17.63 ? 794  LEU   B CD2   1 
ATOM   14928 N  N     . ALA   B  1  797  ? 27.209  50.543  64.462  1.00 19.98 ? 795  ALA   B N     1 
ATOM   14929 C  CA    . ALA   B  1  797  ? 27.285  51.996  64.392  1.00 25.27 ? 795  ALA   B CA    1 
ATOM   14930 C  C     . ALA   B  1  797  ? 28.112  52.467  63.209  1.00 26.09 ? 795  ALA   B C     1 
ATOM   14931 O  O     . ALA   B  1  797  ? 27.999  53.630  62.816  1.00 28.05 ? 795  ALA   B O     1 
ATOM   14932 C  CB    . ALA   B  1  797  ? 27.865  52.558  65.687  1.00 24.77 ? 795  ALA   B CB    1 
ATOM   14933 N  N     . ASP   B  1  798  ? 28.911  51.584  62.615  1.00 23.83 ? 796  ASP   B N     1 
ATOM   14934 C  CA    . ASP   B  1  798  ? 29.630  51.944  61.400  1.00 28.65 ? 796  ASP   B CA    1 
ATOM   14935 C  C     . ASP   B  1  798  ? 28.713  51.991  60.190  1.00 29.44 ? 796  ASP   B C     1 
ATOM   14936 O  O     . ASP   B  1  798  ? 29.101  52.543  59.156  1.00 30.22 ? 796  ASP   B O     1 
ATOM   14937 C  CB    . ASP   B  1  798  ? 30.738  50.926  61.122  1.00 26.50 ? 796  ASP   B CB    1 
ATOM   14938 C  CG    . ASP   B  1  798  ? 31.883  51.003  62.125  1.00 40.56 ? 796  ASP   B CG    1 
ATOM   14939 O  OD1   . ASP   B  1  798  ? 32.120  52.095  62.688  1.00 48.58 ? 796  ASP   B OD1   1 
ATOM   14940 O  OD2   . ASP   B  1  798  ? 32.555  49.969  62.343  1.00 45.43 ? 796  ASP   B OD2   1 
ATOM   14941 N  N     . ARG   B  1  799  ? 27.505  51.450  60.300  1.00 24.78 ? 797  ARG   B N     1 
ATOM   14942 C  CA    A ARG   B  1  799  ? 26.626  51.185  59.173  0.45 29.16 ? 797  ARG   B CA    1 
ATOM   14943 C  CA    B ARG   B  1  799  ? 26.662  51.251  59.137  0.55 29.18 ? 797  ARG   B CA    1 
ATOM   14944 C  C     . ARG   B  1  799  ? 25.351  52.009  59.287  1.00 25.39 ? 797  ARG   B C     1 
ATOM   14945 O  O     . ARG   B  1  799  ? 24.976  52.471  60.367  1.00 23.61 ? 797  ARG   B O     1 
ATOM   14946 C  CB    A ARG   B  1  799  ? 26.232  49.698  59.144  0.45 29.92 ? 797  ARG   B CB    1 
ATOM   14947 C  CB    B ARG   B  1  799  ? 26.409  49.757  58.894  0.55 30.91 ? 797  ARG   B CB    1 
ATOM   14948 C  CG    A ARG   B  1  799  ? 27.395  48.721  59.327  0.45 31.54 ? 797  ARG   B CG    1 
ATOM   14949 C  CG    B ARG   B  1  799  ? 27.658  48.890  59.069  0.55 31.52 ? 797  ARG   B CG    1 
ATOM   14950 C  CD    A ARG   B  1  799  ? 26.924  47.271  59.213  0.45 30.17 ? 797  ARG   B CD    1 
ATOM   14951 C  CD    B ARG   B  1  799  ? 27.711  47.769  58.047  0.55 29.32 ? 797  ARG   B CD    1 
ATOM   14952 N  NE    A ARG   B  1  799  ? 25.815  47.154  58.275  0.45 32.72 ? 797  ARG   B NE    1 
ATOM   14953 N  NE    B ARG   B  1  799  ? 26.378  47.276  57.733  0.55 32.34 ? 797  ARG   B NE    1 
ATOM   14954 C  CZ    A ARG   B  1  799  ? 24.691  46.490  58.507  0.45 28.28 ? 797  ARG   B CZ    1 
ATOM   14955 C  CZ    B ARG   B  1  799  ? 25.778  46.275  58.360  0.55 29.52 ? 797  ARG   B CZ    1 
ATOM   14956 N  NH1   A ARG   B  1  799  ? 24.527  45.761  59.600  0.45 24.29 ? 797  ARG   B NH1   1 
ATOM   14957 N  NH1   B ARG   B  1  799  ? 26.381  45.605  59.327  0.55 28.50 ? 797  ARG   B NH1   1 
ATOM   14958 N  NH2   A ARG   B  1  799  ? 23.712  46.542  57.611  0.45 25.89 ? 797  ARG   B NH2   1 
ATOM   14959 N  NH2   B ARG   B  1  799  ? 24.537  45.943  58.011  0.55 30.37 ? 797  ARG   B NH2   1 
ATOM   14960 N  N     . LEU   B  1  800  ? 24.668  52.153  58.160  1.00 23.47 ? 798  LEU   B N     1 
ATOM   14961 C  CA    . LEU   B  1  800  ? 23.345  52.737  58.095  1.00 23.71 ? 798  LEU   B CA    1 
ATOM   14962 C  C     . LEU   B  1  800  ? 22.513  51.874  57.164  1.00 27.37 ? 798  LEU   B C     1 
ATOM   14963 O  O     . LEU   B  1  800  ? 23.050  51.185  56.293  1.00 27.79 ? 798  LEU   B O     1 
ATOM   14964 C  CB    . LEU   B  1  800  ? 23.375  54.157  57.527  1.00 24.67 ? 798  LEU   B CB    1 
ATOM   14965 C  CG    . LEU   B  1  800  ? 23.957  55.262  58.403  1.00 27.25 ? 798  LEU   B CG    1 
ATOM   14966 C  CD1   . LEU   B  1  800  ? 23.880  56.564  57.627  1.00 31.77 ? 798  LEU   B CD1   1 
ATOM   14967 C  CD2   . LEU   B  1  800  ? 23.211  55.356  59.727  1.00 24.26 ? 798  LEU   B CD2   1 
ATOM   14968 N  N     . SER   B  1  801  ? 21.201  51.910  57.359  1.00 24.84 ? 799  SER   B N     1 
ATOM   14969 C  CA    . SER   B  1  801  ? 20.304  51.263  56.423  1.00 26.38 ? 799  SER   B CA    1 
ATOM   14970 C  C     . SER   B  1  801  ? 20.392  51.977  55.078  1.00 30.69 ? 799  SER   B C     1 
ATOM   14971 O  O     . SER   B  1  801  ? 20.940  53.078  54.987  1.00 29.57 ? 799  SER   B O     1 
ATOM   14972 C  CB    . SER   B  1  801  ? 18.879  51.379  56.938  1.00 29.83 ? 799  SER   B CB    1 
ATOM   14973 O  OG    . SER   B  1  801  ? 18.453  52.725  56.839  1.00 28.37 ? 799  SER   B OG    1 
ATOM   14974 N  N     . PRO   B  1  802  ? 19.881  51.363  54.007  1.00 32.33 ? 800  PRO   B N     1 
ATOM   14975 C  CA    . PRO   B  1  802  ? 19.813  52.097  52.731  1.00 34.44 ? 800  PRO   B CA    1 
ATOM   14976 C  C     . PRO   B  1  802  ? 19.028  53.397  52.828  1.00 33.78 ? 800  PRO   B C     1 
ATOM   14977 O  O     . PRO   B  1  802  ? 19.259  54.315  52.029  1.00 34.13 ? 800  PRO   B O     1 
ATOM   14978 C  CB    . PRO   B  1  802  ? 19.161  51.086  51.779  1.00 30.67 ? 800  PRO   B CB    1 
ATOM   14979 C  CG    . PRO   B  1  802  ? 19.576  49.757  52.330  1.00 33.26 ? 800  PRO   B CG    1 
ATOM   14980 C  CD    . PRO   B  1  802  ? 19.553  49.935  53.838  1.00 30.78 ? 800  PRO   B CD    1 
ATOM   14981 N  N     . ALA   B  1  803  ? 18.110  53.504  53.786  1.00 31.16 ? 801  ALA   B N     1 
ATOM   14982 C  CA    . ALA   B  1  803  ? 17.404  54.747  54.060  1.00 33.24 ? 801  ALA   B CA    1 
ATOM   14983 C  C     . ALA   B  1  803  ? 18.236  55.737  54.869  1.00 36.70 ? 801  ALA   B C     1 
ATOM   14984 O  O     . ALA   B  1  803  ? 17.756  56.839  55.152  1.00 36.78 ? 801  ALA   B O     1 
ATOM   14985 C  CB    . ALA   B  1  803  ? 16.089  54.452  54.784  1.00 30.59 ? 801  ALA   B CB    1 
ATOM   14986 N  N     . GLY   B  1  804  ? 19.460  55.379  55.245  1.00 30.04 ? 802  GLY   B N     1 
ATOM   14987 C  CA    . GLY   B  1  804  ? 20.309  56.288  55.987  1.00 28.79 ? 802  GLY   B CA    1 
ATOM   14988 C  C     . GLY   B  1  804  ? 20.004  56.384  57.463  1.00 27.89 ? 802  GLY   B C     1 
ATOM   14989 O  O     . GLY   B  1  804  ? 20.199  57.445  58.059  1.00 28.70 ? 802  GLY   B O     1 
ATOM   14990 N  N     . ARG   B  1  805  ? 19.538  55.308  58.080  1.00 28.38 ? 803  ARG   B N     1 
ATOM   14991 C  CA    . ARG   B  1  805  ? 19.152  55.327  59.481  1.00 25.16 ? 803  ARG   B CA    1 
ATOM   14992 C  C     . ARG   B  1  805  ? 19.864  54.218  60.236  1.00 21.57 ? 803  ARG   B C     1 
ATOM   14993 O  O     . ARG   B  1  805  ? 20.317  53.239  59.636  1.00 23.08 ? 803  ARG   B O     1 
ATOM   14994 C  CB    . ARG   B  1  805  ? 17.635  55.156  59.619  1.00 26.41 ? 803  ARG   B CB    1 
ATOM   14995 C  CG    . ARG   B  1  805  ? 16.851  56.291  59.002  1.00 30.89 ? 803  ARG   B CG    1 
ATOM   14996 C  CD    . ARG   B  1  805  ? 17.233  57.628  59.628  1.00 33.14 ? 803  ARG   B CD    1 
ATOM   14997 N  NE    . ARG   B  1  805  ? 16.479  58.720  59.021  1.00 38.44 ? 803  ARG   B NE    1 
ATOM   14998 C  CZ    . ARG   B  1  805  ? 16.939  59.513  58.063  1.00 31.87 ? 803  ARG   B CZ    1 
ATOM   14999 N  NH1   . ARG   B  1  805  ? 18.184  59.418  57.620  1.00 33.05 ? 803  ARG   B NH1   1 
ATOM   15000 N  NH2   . ARG   B  1  805  ? 16.127  60.421  57.527  1.00 39.31 ? 803  ARG   B NH2   1 
ATOM   15001 N  N     . PRO   B  1  806  ? 19.986  54.342  61.558  1.00 20.70 ? 804  PRO   B N     1 
ATOM   15002 C  CA    . PRO   B  1  806  ? 20.689  53.310  62.323  1.00 20.02 ? 804  PRO   B CA    1 
ATOM   15003 C  C     . PRO   B  1  806  ? 20.013  51.956  62.187  1.00 18.68 ? 804  PRO   B C     1 
ATOM   15004 O  O     . PRO   B  1  806  ? 18.788  51.850  62.086  1.00 19.26 ? 804  PRO   B O     1 
ATOM   15005 C  CB    . PRO   B  1  806  ? 20.618  53.824  63.765  1.00 22.05 ? 804  PRO   B CB    1 
ATOM   15006 C  CG    . PRO   B  1  806  ? 20.458  55.303  63.615  1.00 26.22 ? 804  PRO   B CG    1 
ATOM   15007 C  CD    . PRO   B  1  806  ? 19.577  55.468  62.416  1.00 23.51 ? 804  PRO   B CD    1 
ATOM   15008 N  N     . ILE   B  1  807  ? 20.844  50.920  62.165  1.00 19.29 ? 805  ILE   B N     1 
ATOM   15009 C  CA    . ILE   B  1  807  ? 20.371  49.540  62.179  1.00 17.39 ? 805  ILE   B CA    1 
ATOM   15010 C  C     . ILE   B  1  807  ? 19.884  49.249  63.594  1.00 16.41 ? 805  ILE   B C     1 
ATOM   15011 O  O     . ILE   B  1  807  ? 20.671  49.374  64.545  1.00 17.64 ? 805  ILE   B O     1 
ATOM   15012 C  CB    . ILE   B  1  807  ? 21.499  48.575  61.802  1.00 16.87 ? 805  ILE   B CB    1 
ATOM   15013 C  CG1   . ILE   B  1  807  ? 22.107  48.930  60.437  1.00 21.35 ? 805  ILE   B CG1   1 
ATOM   15014 C  CG2   . ILE   B  1  807  ? 21.004  47.136  61.872  1.00 19.00 ? 805  ILE   B CG2   1 
ATOM   15015 C  CD1   . ILE   B  1  807  ? 21.167  48.728  59.295  1.00 25.78 ? 805  ILE   B CD1   1 
ATOM   15016 N  N     . PRO   B  1  808  ? 18.623  48.860  63.777  1.00 15.88 ? 806  PRO   B N     1 
ATOM   15017 C  CA    . PRO   B  1  808  ? 18.117  48.595  65.131  1.00 17.36 ? 806  PRO   B CA    1 
ATOM   15018 C  C     . PRO   B  1  808  ? 18.826  47.413  65.770  1.00 17.51 ? 806  PRO   B C     1 
ATOM   15019 O  O     . PRO   B  1  808  ? 19.069  46.384  65.132  1.00 15.88 ? 806  PRO   B O     1 
ATOM   15020 C  CB    . PRO   B  1  808  ? 16.638  48.266  64.899  1.00 17.90 ? 806  PRO   B CB    1 
ATOM   15021 C  CG    . PRO   B  1  808  ? 16.301  48.920  63.586  1.00 20.77 ? 806  PRO   B CG    1 
ATOM   15022 C  CD    . PRO   B  1  808  ? 17.561  48.766  62.765  1.00 16.03 ? 806  PRO   B CD    1 
ATOM   15023 N  N     . LEU   B  1  809  ? 19.132  47.568  67.056  1.00 15.37 ? 807  LEU   B N     1 
ATOM   15024 C  CA    . LEU   B  1  809  ? 19.712  46.512  67.865  1.00 14.39 ? 807  LEU   B CA    1 
ATOM   15025 C  C     . LEU   B  1  809  ? 18.847  46.365  69.103  1.00 14.30 ? 807  LEU   B C     1 
ATOM   15026 O  O     . LEU   B  1  809  ? 18.638  47.338  69.832  1.00 17.20 ? 807  LEU   B O     1 
ATOM   15027 C  CB    . LEU   B  1  809  ? 21.131  46.900  68.272  1.00 16.02 ? 807  LEU   B CB    1 
ATOM   15028 C  CG    . LEU   B  1  809  ? 21.786  46.005  69.315  1.00 15.55 ? 807  LEU   B CG    1 
ATOM   15029 C  CD1   . LEU   B  1  809  ? 21.983  44.571  68.829  1.00 16.36 ? 807  LEU   B CD1   1 
ATOM   15030 C  CD2   . LEU   B  1  809  ? 23.125  46.621  69.688  1.00 17.23 ? 807  LEU   B CD2   1 
ATOM   15031 N  N     . ILE   B  1  810  ? 18.339  45.163  69.345  1.00 13.79 ? 808  ILE   B N     1 
ATOM   15032 C  CA    . ILE   B  1  810  ? 17.800  44.813  70.648  1.00 13.21 ? 808  ILE   B CA    1 
ATOM   15033 C  C     . ILE   B  1  810  ? 18.901  44.037  71.325  1.00 14.67 ? 808  ILE   B C     1 
ATOM   15034 O  O     . ILE   B  1  810  ? 19.378  43.033  70.786  1.00 16.13 ? 808  ILE   B O     1 
ATOM   15035 C  CB    . ILE   B  1  810  ? 16.526  43.968  70.539  1.00 14.88 ? 808  ILE   B CB    1 
ATOM   15036 C  CG1   . ILE   B  1  810  ? 15.487  44.680  69.687  1.00 15.11 ? 808  ILE   B CG1   1 
ATOM   15037 C  CG2   . ILE   B  1  810  ? 15.948  43.743  71.941  1.00 18.45 ? 808  ILE   B CG2   1 
ATOM   15038 C  CD1   . ILE   B  1  810  ? 14.164  43.927  69.630  1.00 17.98 ? 808  ILE   B CD1   1 
ATOM   15039 N  N     . ALA   B  1  811  ? 19.360  44.527  72.469  1.00 14.59 ? 809  ALA   B N     1 
ATOM   15040 C  CA    . ALA   B  1  811  ? 20.472  43.890  73.166  1.00 14.59 ? 809  ALA   B CA    1 
ATOM   15041 C  C     . ALA   B  1  811  ? 20.051  43.669  74.604  1.00 16.22 ? 809  ALA   B C     1 
ATOM   15042 O  O     . ALA   B  1  811  ? 20.001  44.618  75.393  1.00 16.01 ? 809  ALA   B O     1 
ATOM   15043 C  CB    . ALA   B  1  811  ? 21.744  44.730  73.097  1.00 16.57 ? 809  ALA   B CB    1 
ATOM   15044 N  N     . GLU   B  1  812  ? 19.741  42.432  74.925  1.00 13.07 ? 810  GLU   B N     1 
ATOM   15045 C  CA    . GLU   B  1  812  ? 19.234  42.052  76.233  1.00 14.07 ? 810  GLU   B CA    1 
ATOM   15046 C  C     . GLU   B  1  812  ? 20.347  41.296  76.919  1.00 14.67 ? 810  GLU   B C     1 
ATOM   15047 O  O     . GLU   B  1  812  ? 20.804  40.256  76.425  1.00 15.87 ? 810  GLU   B O     1 
ATOM   15048 C  CB    . GLU   B  1  812  ? 17.967  41.220  76.068  1.00 15.86 ? 810  GLU   B CB    1 
ATOM   15049 C  CG    . GLU   B  1  812  ? 16.893  42.033  75.332  1.00 16.46 ? 810  GLU   B CG    1 
ATOM   15050 C  CD    . GLU   B  1  812  ? 16.517  43.308  76.101  1.00 18.16 ? 810  GLU   B CD    1 
ATOM   15051 O  OE1   . GLU   B  1  812  ? 15.778  43.199  77.099  1.00 17.43 ? 810  GLU   B OE1   1 
ATOM   15052 O  OE2   . GLU   B  1  812  ? 16.945  44.416  75.705  1.00 18.57 ? 810  GLU   B OE2   1 
ATOM   15053 N  N     . THR   B  1  813  ? 20.843  41.867  78.010  1.00 14.52 ? 811  THR   B N     1 
ATOM   15054 C  CA    . THR   B  1  813  ? 22.159  41.517  78.489  1.00 14.55 ? 811  THR   B CA    1 
ATOM   15055 C  C     . THR   B  1  813  ? 22.113  41.066  79.946  1.00 15.39 ? 811  THR   B C     1 
ATOM   15056 O  O     . THR   B  1  813  ? 21.092  40.554  80.399  1.00 15.33 ? 811  THR   B O     1 
ATOM   15057 C  CB    . THR   B  1  813  ? 23.128  42.660  78.180  1.00 15.74 ? 811  THR   B CB    1 
ATOM   15058 O  OG1   . THR   B  1  813  ? 22.574  43.915  78.598  1.00 15.98 ? 811  THR   B OG1   1 
ATOM   15059 C  CG2   . THR   B  1  813  ? 23.336  42.746  76.665  1.00 17.82 ? 811  THR   B CG2   1 
ATOM   15060 N  N     . GLY   B  1  814  ? 23.199  41.221  80.685  1.00 15.79 ? 812  GLY   B N     1 
ATOM   15061 C  CA    . GLY   B  1  814  ? 23.320  40.523  81.954  1.00 16.02 ? 812  GLY   B CA    1 
ATOM   15062 C  C     . GLY   B  1  814  ? 22.616  41.211  83.104  1.00 15.62 ? 812  GLY   B C     1 
ATOM   15063 O  O     . GLY   B  1  814  ? 21.958  42.235  82.960  1.00 17.74 ? 812  GLY   B O     1 
ATOM   15064 N  N     . GLY   B  1  815  ? 22.747  40.596  84.275  1.00 16.05 ? 813  GLY   B N     1 
ATOM   15065 C  CA    . GLY   B  1  815  ? 22.169  41.153  85.479  1.00 16.33 ? 813  GLY   B CA    1 
ATOM   15066 C  C     . GLY   B  1  815  ? 23.118  40.963  86.642  1.00 14.76 ? 813  GLY   B C     1 
ATOM   15067 O  O     . GLY   B  1  815  ? 24.084  40.201  86.573  1.00 17.98 ? 813  GLY   B O     1 
ATOM   15068 N  N     . GLN   B  1  816  ? 22.871  41.728  87.692  1.00 15.01 ? 814  GLN   B N     1 
ATOM   15069 C  CA    . GLN   B  1  816  ? 23.546  41.538  88.971  1.00 15.51 ? 814  GLN   B CA    1 
ATOM   15070 C  C     . GLN   B  1  816  ? 22.444  41.578  90.023  1.00 14.57 ? 814  GLN   B C     1 
ATOM   15071 O  O     . GLN   B  1  816  ? 22.283  42.544  90.771  1.00 15.69 ? 814  GLN   B O     1 
ATOM   15072 C  CB    . GLN   B  1  816  ? 24.610  42.604  89.205  1.00 15.79 ? 814  GLN   B CB    1 
ATOM   15073 C  CG    . GLN   B  1  816  ? 25.490  42.298  90.398  1.00 16.08 ? 814  GLN   B CG    1 
ATOM   15074 C  CD    . GLN   B  1  816  ? 26.362  41.090  90.147  1.00 15.52 ? 814  GLN   B CD    1 
ATOM   15075 O  OE1   . GLN   B  1  816  ? 25.911  39.949  90.277  1.00 17.43 ? 814  GLN   B OE1   1 
ATOM   15076 N  NE2   . GLN   B  1  816  ? 27.631  41.331  89.769  1.00 16.61 ? 814  GLN   B NE2   1 
ATOM   15077 N  N     . ASN   B  1  817  ? 21.661  40.517  90.065  1.00 12.80 ? 815  ASN   B N     1 
ATOM   15078 C  CA    . ASN   B  1  817  ? 20.313  40.605  90.596  1.00 12.86 ? 815  ASN   B CA    1 
ATOM   15079 C  C     . ASN   B  1  817  ? 20.308  40.371  92.088  1.00 13.26 ? 815  ASN   B C     1 
ATOM   15080 O  O     . ASN   B  1  817  ? 20.912  39.410  92.578  1.00 14.50 ? 815  ASN   B O     1 
ATOM   15081 C  CB    . ASN   B  1  817  ? 19.431  39.565  89.921  1.00 14.98 ? 815  ASN   B CB    1 
ATOM   15082 C  CG    . ASN   B  1  817  ? 19.556  39.616  88.422  1.00 14.07 ? 815  ASN   B CG    1 
ATOM   15083 O  OD1   . ASN   B  1  817  ? 19.371  40.666  87.804  1.00 13.55 ? 815  ASN   B OD1   1 
ATOM   15084 N  ND2   . ASN   B  1  817  ? 19.920  38.500  87.840  1.00 13.92 ? 815  ASN   B ND2   1 
ATOM   15085 N  N     . ALA   B  1  818  ? 19.574  41.219  92.793  1.00 12.97 ? 816  ALA   B N     1 
ATOM   15086 C  CA    . ALA   B  1  818  ? 19.492  41.154  94.240  1.00 13.21 ? 816  ALA   B CA    1 
ATOM   15087 C  C     . ALA   B  1  818  ? 18.108  40.736  94.693  1.00 13.18 ? 816  ALA   B C     1 
ATOM   15088 O  O     . ALA   B  1  818  ? 17.111  40.906  93.989  1.00 13.59 ? 816  ALA   B O     1 
ATOM   15089 C  CB    . ALA   B  1  818  ? 19.817  42.519  94.844  1.00 15.22 ? 816  ALA   B CB    1 
ATOM   15090 N  N     . MET   B  1  819  ? 18.062  40.182  95.897  1.00 13.98 ? 817  MET   B N     1 
ATOM   15091 C  CA    . MET   B  1  819  ? 16.830  39.968  96.624  1.00 14.00 ? 817  MET   B CA    1 
ATOM   15092 C  C     . MET   B  1  819  ? 17.032  40.560  98.005  1.00 13.05 ? 817  MET   B C     1 
ATOM   15093 O  O     . MET   B  1  819  ? 18.028  40.254  98.671  1.00 14.91 ? 817  MET   B O     1 
ATOM   15094 C  CB    . MET   B  1  819  ? 16.512  38.490  96.754  1.00 15.45 ? 817  MET   B CB    1 
ATOM   15095 C  CG    . MET   B  1  819  ? 15.265  38.242  97.596  1.00 16.15 ? 817  MET   B CG    1 
ATOM   15096 S  SD    . MET   B  1  819  ? 14.969  36.487  97.901  1.00 17.87 ? 817  MET   B SD    1 
ATOM   15097 C  CE    . MET   B  1  819  ? 14.369  35.991  96.297  1.00 20.05 ? 817  MET   B CE    1 
ATOM   15098 N  N     . ILE   B  1  820  ? 16.119  41.430  98.406  1.00 14.04 ? 818  ILE   B N     1 
ATOM   15099 C  CA    . ILE   B  1  820  ? 16.140  42.011  99.740  1.00 13.31 ? 818  ILE   B CA    1 
ATOM   15100 C  C     . ILE   B  1  820  ? 15.108  41.300  100.588 1.00 14.13 ? 818  ILE   B C     1 
ATOM   15101 O  O     . ILE   B  1  820  ? 13.958  41.135  100.174 1.00 15.20 ? 818  ILE   B O     1 
ATOM   15102 C  CB    . ILE   B  1  820  ? 15.875  43.518  99.690  1.00 14.25 ? 818  ILE   B CB    1 
ATOM   15103 C  CG1   . ILE   B  1  820  ? 16.986  44.195  98.903  1.00 15.08 ? 818  ILE   B CG1   1 
ATOM   15104 C  CG2   . ILE   B  1  820  ? 15.806  44.080  101.112 1.00 15.96 ? 818  ILE   B CG2   1 
ATOM   15105 C  CD1   . ILE   B  1  820  ? 16.797  45.684  98.796  1.00 17.95 ? 818  ILE   B CD1   1 
ATOM   15106 N  N     . VAL   B  1  821  ? 15.522  40.877  101.779 1.00 14.65 ? 819  VAL   B N     1 
ATOM   15107 C  CA    . VAL   B  1  821  ? 14.687  40.108  102.689 1.00 15.89 ? 819  VAL   B CA    1 
ATOM   15108 C  C     . VAL   B  1  821  ? 14.684  40.856  104.008 1.00 15.65 ? 819  VAL   B C     1 
ATOM   15109 O  O     . VAL   B  1  821  ? 15.752  41.095  104.582 1.00 16.49 ? 819  VAL   B O     1 
ATOM   15110 C  CB    . VAL   B  1  821  ? 15.265  38.705  102.910 1.00 15.59 ? 819  VAL   B CB    1 
ATOM   15111 C  CG1   . VAL   B  1  821  ? 14.397  37.932  103.897 1.00 17.68 ? 819  VAL   B CG1   1 
ATOM   15112 C  CG2   . VAL   B  1  821  ? 15.404  37.956  101.575 1.00 15.45 ? 819  VAL   B CG2   1 
ATOM   15113 N  N     . ASP   B  1  822  ? 13.507  41.211  104.497 1.00 15.90 ? 820  ASP   B N     1 
ATOM   15114 C  CA    . ASP   B  1  822  ? 13.449  41.851  105.798 1.00 16.92 ? 820  ASP   B CA    1 
ATOM   15115 C  C     . ASP   B  1  822  ? 13.040  40.845  106.868 1.00 17.68 ? 820  ASP   B C     1 
ATOM   15116 O  O     . ASP   B  1  822  ? 12.815  39.659  106.614 1.00 18.01 ? 820  ASP   B O     1 
ATOM   15117 C  CB    . ASP   B  1  822  ? 12.638  43.158  105.779 1.00 17.41 ? 820  ASP   B CB    1 
ATOM   15118 C  CG    . ASP   B  1  822  ? 11.143  42.940  105.715 1.00 18.17 ? 820  ASP   B CG    1 
ATOM   15119 O  OD1   . ASP   B  1  822  ? 10.665  41.813  105.906 1.00 17.61 ? 820  ASP   B OD1   1 
ATOM   15120 O  OD2   . ASP   B  1  822  ? 10.430  43.945  105.482 1.00 20.03 ? 820  ASP   B OD2   1 
ATOM   15121 N  N     . SER   B  1  823  ? 12.939  41.339  108.097 1.00 18.44 ? 821  SER   B N     1 
ATOM   15122 C  CA    . SER   B  1  823  ? 12.664  40.443  109.206 1.00 19.89 ? 821  SER   B CA    1 
ATOM   15123 C  C     . SER   B  1  823  ? 11.216  39.978  109.263 1.00 19.98 ? 821  SER   B C     1 
ATOM   15124 O  O     . SER   B  1  823  ? 10.890  39.142  110.111 1.00 23.67 ? 821  SER   B O     1 
ATOM   15125 C  CB    . SER   B  1  823  ? 13.055  41.106  110.523 1.00 21.09 ? 821  SER   B CB    1 
ATOM   15126 O  OG    . SER   B  1  823  ? 12.300  42.289  110.719 1.00 22.89 ? 821  SER   B OG    1 
ATOM   15127 N  N     . SER   B  1  824  ? 10.337  40.481  108.398 1.00 17.21 ? 822  SER   B N     1 
ATOM   15128 C  CA    . SER   B  1  824  ? 8.967   40.002  108.372 1.00 17.61 ? 822  SER   B CA    1 
ATOM   15129 C  C     . SER   B  1  824  ? 8.774   38.825  107.434 1.00 18.78 ? 822  SER   B C     1 
ATOM   15130 O  O     . SER   B  1  824  ? 7.720   38.181  107.466 1.00 21.17 ? 822  SER   B O     1 
ATOM   15131 C  CB    . SER   B  1  824  ? 8.006   41.129  107.981 1.00 19.24 ? 822  SER   B CB    1 
ATOM   15132 O  OG    . SER   B  1  824  ? 8.103   41.440  106.602 1.00 17.67 ? 822  SER   B OG    1 
ATOM   15133 N  N     . ALA   B  1  825  ? 9.764   38.538  106.602 1.00 17.63 ? 823  ALA   B N     1 
ATOM   15134 C  CA    . ALA   B  1  825  ? 9.637   37.483  105.615 1.00 17.61 ? 823  ALA   B CA    1 
ATOM   15135 C  C     . ALA   B  1  825  ? 9.666   36.126  106.303 1.00 18.04 ? 823  ALA   B C     1 
ATOM   15136 O  O     . ALA   B  1  825  ? 10.219  35.972  107.396 1.00 20.25 ? 823  ALA   B O     1 
ATOM   15137 C  CB    . ALA   B  1  825  ? 10.800  37.586  104.636 1.00 18.67 ? 823  ALA   B CB    1 
ATOM   15138 N  N     . LEU   B  1  826  ? 9.048   35.144  105.673 1.00 20.79 ? 824  LEU   B N     1 
ATOM   15139 C  CA    . LEU   B  1  826  ? 9.015   33.791  106.207 1.00 19.45 ? 824  LEU   B CA    1 
ATOM   15140 C  C     . LEU   B  1  826  ? 10.253  33.053  105.718 1.00 19.57 ? 824  LEU   B C     1 
ATOM   15141 O  O     . LEU   B  1  826  ? 10.413  32.850  104.511 1.00 18.98 ? 824  LEU   B O     1 
ATOM   15142 C  CB    . LEU   B  1  826  ? 7.761   33.068  105.729 1.00 23.83 ? 824  LEU   B CB    1 
ATOM   15143 C  CG    . LEU   B  1  826  ? 7.593   31.650  106.273 1.00 28.12 ? 824  LEU   B CG    1 
ATOM   15144 C  CD1   . LEU   B  1  826  ? 7.480   31.655  107.794 1.00 32.07 ? 824  LEU   B CD1   1 
ATOM   15145 C  CD2   . LEU   B  1  826  ? 6.359   31.028  105.651 1.00 34.61 ? 824  LEU   B CD2   1 
ATOM   15146 N  N     . ALA   B  1  827  ? 11.102  32.620  106.649 1.00 20.61 ? 825  ALA   B N     1 
ATOM   15147 C  CA    . ALA   B  1  827  ? 12.399  32.064  106.276 1.00 18.25 ? 825  ALA   B CA    1 
ATOM   15148 C  C     . ALA   B  1  827  ? 12.268  30.899  105.301 1.00 18.77 ? 825  ALA   B C     1 
ATOM   15149 O  O     . ALA   B  1  827  ? 13.028  30.815  104.329 1.00 17.82 ? 825  ALA   B O     1 
ATOM   15150 C  CB    . ALA   B  1  827  ? 13.163  31.641  107.529 1.00 18.92 ? 825  ALA   B CB    1 
ATOM   15151 N  N     . GLU   B  1  828  ? 11.331  29.983  105.548 1.00 19.21 ? 826  GLU   B N     1 
ATOM   15152 C  CA    . GLU   B  1  828  ? 11.190  28.824  104.669 1.00 20.35 ? 826  GLU   B CA    1 
ATOM   15153 C  C     . GLU   B  1  828  ? 10.866  29.247  103.243 1.00 20.60 ? 826  GLU   B C     1 
ATOM   15154 O  O     . GLU   B  1  828  ? 11.353  28.645  102.276 1.00 17.89 ? 826  GLU   B O     1 
ATOM   15155 C  CB    . GLU   B  1  828  ? 10.089  27.900  105.189 1.00 21.84 ? 826  GLU   B CB    1 
ATOM   15156 C  CG    . GLU   B  1  828  ? 10.472  27.071  106.399 1.00 25.36 ? 826  GLU   B CG    1 
ATOM   15157 C  CD    . GLU   B  1  828  ? 10.339  27.814  107.721 1.00 26.35 ? 826  GLU   B CD    1 
ATOM   15158 O  OE1   . GLU   B  1  828  ? 9.973   29.017  107.733 1.00 26.27 ? 826  GLU   B OE1   1 
ATOM   15159 O  OE2   . GLU   B  1  828  ? 10.604  27.176  108.763 1.00 28.81 ? 826  GLU   B OE2   1 
ATOM   15160 N  N     . GLN   B  1  829  ? 10.019  30.265  103.091 1.00 18.08 ? 827  GLN   B N     1 
ATOM   15161 C  CA    A GLN   B  1  829  ? 9.687   30.741  101.753 0.51 18.87 ? 827  GLN   B CA    1 
ATOM   15162 C  CA    B GLN   B  1  829  ? 9.683   30.744  101.756 0.49 18.87 ? 827  GLN   B CA    1 
ATOM   15163 C  C     . GLN   B  1  829  ? 10.889  31.397  101.099 1.00 18.51 ? 827  GLN   B C     1 
ATOM   15164 O  O     . GLN   B  1  829  ? 11.173  31.154  99.921  1.00 18.18 ? 827  GLN   B O     1 
ATOM   15165 C  CB    A GLN   B  1  829  ? 8.532   31.735  101.824 0.51 22.41 ? 827  GLN   B CB    1 
ATOM   15166 C  CB    B GLN   B  1  829  ? 8.516   31.727  101.850 0.49 22.41 ? 827  GLN   B CB    1 
ATOM   15167 C  CG    A GLN   B  1  829  ? 7.185   31.125  102.116 0.51 20.97 ? 827  GLN   B CG    1 
ATOM   15168 C  CG    B GLN   B  1  829  ? 8.050   32.286  100.523 0.49 17.62 ? 827  GLN   B CG    1 
ATOM   15169 C  CD    A GLN   B  1  829  ? 6.084   32.157  102.007 0.51 26.47 ? 827  GLN   B CD    1 
ATOM   15170 C  CD    B GLN   B  1  829  ? 6.891   33.255  100.682 0.49 24.53 ? 827  GLN   B CD    1 
ATOM   15171 O  OE1   A GLN   B  1  829  ? 6.327   33.353  102.176 0.51 26.16 ? 827  GLN   B OE1   1 
ATOM   15172 O  OE1   B GLN   B  1  829  ? 6.669   33.810  101.763 0.49 27.23 ? 827  GLN   B OE1   1 
ATOM   15173 N  NE2   A GLN   B  1  829  ? 4.871   31.705  101.724 0.51 29.24 ? 827  GLN   B NE2   1 
ATOM   15174 N  NE2   B GLN   B  1  829  ? 6.144   33.459  99.609  0.49 22.94 ? 827  GLN   B NE2   1 
ATOM   15175 N  N     . VAL   B  1  830  ? 11.611  32.218  101.854 1.00 17.10 ? 828  VAL   B N     1 
ATOM   15176 C  CA    . VAL   B  1  830  ? 12.833  32.825  101.356 1.00 15.75 ? 828  VAL   B CA    1 
ATOM   15177 C  C     . VAL   B  1  830  ? 13.791  31.752  100.882 1.00 17.84 ? 828  VAL   B C     1 
ATOM   15178 O  O     . VAL   B  1  830  ? 14.346  31.829  99.785  1.00 16.77 ? 828  VAL   B O     1 
ATOM   15179 C  CB    . VAL   B  1  830  ? 13.484  33.682  102.453 1.00 16.50 ? 828  VAL   B CB    1 
ATOM   15180 C  CG1   . VAL   B  1  830  ? 14.845  34.155  101.995 1.00 17.08 ? 828  VAL   B CG1   1 
ATOM   15181 C  CG2   . VAL   B  1  830  ? 12.587  34.846  102.803 1.00 18.44 ? 828  VAL   B CG2   1 
ATOM   15182 N  N     . VAL   B  1  831  ? 14.028  30.746  101.723 1.00 16.31 ? 829  VAL   B N     1 
ATOM   15183 C  CA    . VAL   B  1  831  ? 15.022  29.734  101.390 1.00 15.74 ? 829  VAL   B CA    1 
ATOM   15184 C  C     . VAL   B  1  831  ? 14.644  29.008  100.102 1.00 16.06 ? 829  VAL   B C     1 
ATOM   15185 O  O     . VAL   B  1  831  ? 15.484  28.822  99.214  1.00 16.25 ? 829  VAL   B O     1 
ATOM   15186 C  CB    . VAL   B  1  831  ? 15.237  28.780  102.575 1.00 16.89 ? 829  VAL   B CB    1 
ATOM   15187 C  CG1   . VAL   B  1  831  ? 15.980  27.531  102.122 1.00 16.98 ? 829  VAL   B CG1   1 
ATOM   15188 C  CG2   . VAL   B  1  831  ? 15.994  29.508  103.657 1.00 18.18 ? 829  VAL   B CG2   1 
ATOM   15189 N  N     . GLY   B  1  832  ? 13.382  28.603  99.966  1.00 16.08 ? 830  GLY   B N     1 
ATOM   15190 C  CA    . GLY   B  1  832  ? 12.978  27.945  98.729  1.00 15.83 ? 830  GLY   B CA    1 
ATOM   15191 C  C     . GLY   B  1  832  ? 13.182  28.832  97.521  1.00 16.08 ? 830  GLY   B C     1 
ATOM   15192 O  O     . GLY   B  1  832  ? 13.661  28.382  96.477  1.00 17.20 ? 830  GLY   B O     1 
ATOM   15193 N  N     . ASP   B  1  833  ? 12.850  30.113  97.658  1.00 15.02 ? 831  ASP   B N     1 
ATOM   15194 C  CA    . ASP   B  1  833  ? 12.975  31.023  96.526  1.00 16.07 ? 831  ASP   B CA    1 
ATOM   15195 C  C     . ASP   B  1  833  ? 14.423  31.359  96.230  1.00 16.72 ? 831  ASP   B C     1 
ATOM   15196 O  O     . ASP   B  1  833  ? 14.774  31.594  95.072  1.00 15.77 ? 831  ASP   B O     1 
ATOM   15197 C  CB    . ASP   B  1  833  ? 12.163  32.288  96.798  1.00 15.89 ? 831  ASP   B CB    1 
ATOM   15198 C  CG    . ASP   B  1  833  ? 10.678  32.019  96.782  1.00 16.90 ? 831  ASP   B CG    1 
ATOM   15199 O  OD1   . ASP   B  1  833  ? 10.274  30.961  96.257  1.00 18.90 ? 831  ASP   B OD1   1 
ATOM   15200 O  OD2   . ASP   B  1  833  ? 9.903   32.864  97.271  1.00 18.46 ? 831  ASP   B OD2   1 
ATOM   15201 N  N     . VAL   B  1  834  ? 15.281  31.377  97.250  1.00 14.94 ? 832  VAL   B N     1 
ATOM   15202 C  CA    . VAL   B  1  834  ? 16.705  31.588  97.026  1.00 14.53 ? 832  VAL   B CA    1 
ATOM   15203 C  C     . VAL   B  1  834  ? 17.306  30.402  96.296  1.00 15.44 ? 832  VAL   B C     1 
ATOM   15204 O  O     . VAL   B  1  834  ? 18.103  30.557  95.358  1.00 15.47 ? 832  VAL   B O     1 
ATOM   15205 C  CB    . VAL   B  1  834  ? 17.417  31.851  98.364  1.00 15.17 ? 832  VAL   B CB    1 
ATOM   15206 C  CG1   . VAL   B  1  834  ? 18.909  31.694  98.207  1.00 16.16 ? 832  VAL   B CG1   1 
ATOM   15207 C  CG2   . VAL   B  1  834  ? 17.060  33.234  98.874  1.00 17.23 ? 832  VAL   B CG2   1 
ATOM   15208 N  N     . ILE   B  1  835  ? 16.959  29.196  96.726  1.00 15.39 ? 833  ILE   B N     1 
ATOM   15209 C  CA    . ILE   B  1  835  ? 17.506  28.026  96.055  1.00 18.20 ? 833  ILE   B CA    1 
ATOM   15210 C  C     . ILE   B  1  835  ? 17.080  28.007  94.597  1.00 18.01 ? 833  ILE   B C     1 
ATOM   15211 O  O     . ILE   B  1  835  ? 17.908  27.849  93.690  1.00 18.65 ? 833  ILE   B O     1 
ATOM   15212 C  CB    . ILE   B  1  835  ? 17.121  26.749  96.804  1.00 18.87 ? 833  ILE   B CB    1 
ATOM   15213 C  CG1   . ILE   B  1  835  ? 17.840  26.753  98.141  1.00 22.71 ? 833  ILE   B CG1   1 
ATOM   15214 C  CG2   . ILE   B  1  835  ? 17.497  25.515  95.976  1.00 22.35 ? 833  ILE   B CG2   1 
ATOM   15215 C  CD1   . ILE   B  1  835  ? 17.581  25.548  98.944  1.00 24.14 ? 833  ILE   B CD1   1 
ATOM   15216 N  N     . THR   B  1  836  ? 15.797  28.234  94.344  1.00 15.71 ? 834  THR   B N     1 
ATOM   15217 C  CA    . THR   B  1  836  ? 15.317  28.288  92.969  1.00 15.91 ? 834  THR   B CA    1 
ATOM   15218 C  C     . THR   B  1  836  ? 16.054  29.357  92.176  1.00 17.78 ? 834  THR   B C     1 
ATOM   15219 O  O     . THR   B  1  836  ? 16.510  29.123  91.047  1.00 22.30 ? 834  THR   B O     1 
ATOM   15220 C  CB    . THR   B  1  836  ? 13.828  28.614  93.000  1.00 18.04 ? 834  THR   B CB    1 
ATOM   15221 O  OG1   . THR   B  1  836  ? 13.117  27.529  93.614  1.00 22.60 ? 834  THR   B OG1   1 
ATOM   15222 C  CG2   . THR   B  1  836  ? 13.297  28.836  91.582  1.00 21.66 ? 834  THR   B CG2   1 
ATOM   15223 N  N     . SER   B  1  837  ? 16.177  30.541  92.750  1.00 15.51 ? 835  SER   B N     1 
ATOM   15224 C  CA    . SER   B  1  837  ? 16.679  31.671  91.988  1.00 15.94 ? 835  SER   B CA    1 
ATOM   15225 C  C     . SER   B  1  837  ? 18.189  31.639  91.828  1.00 15.10 ? 835  SER   B C     1 
ATOM   15226 O  O     . SER   B  1  837  ? 18.709  32.051  90.793  1.00 15.69 ? 835  SER   B O     1 
ATOM   15227 C  CB    . SER   B  1  837  ? 16.283  32.973  92.657  1.00 15.19 ? 835  SER   B CB    1 
ATOM   15228 O  OG    . SER   B  1  837  ? 14.876  33.044  92.801  1.00 15.40 ? 835  SER   B OG    1 
ATOM   15229 N  N     . ALA   B  1  838  ? 18.916  31.203  92.852  1.00 15.15 ? 836  ALA   B N     1 
ATOM   15230 C  CA    . ALA   B  1  838  ? 20.363  31.289  92.828  1.00 15.50 ? 836  ALA   B CA    1 
ATOM   15231 C  C     . ALA   B  1  838  ? 21.018  30.034  92.295  1.00 15.97 ? 836  ALA   B C     1 
ATOM   15232 O  O     . ALA   B  1  838  ? 22.072  30.125  91.666  1.00 18.32 ? 836  ALA   B O     1 
ATOM   15233 C  CB    . ALA   B  1  838  ? 20.888  31.525  94.248  1.00 15.17 ? 836  ALA   B CB    1 
ATOM   15234 N  N     . PHE   B  1  839  ? 20.468  28.861  92.594  1.00 16.64 ? 837  PHE   B N     1 
ATOM   15235 C  CA    . PHE   B  1  839  ? 21.226  27.638  92.397  1.00 17.90 ? 837  PHE   B CA    1 
ATOM   15236 C  C     . PHE   B  1  839  ? 20.606  26.687  91.407  1.00 20.51 ? 837  PHE   B C     1 
ATOM   15237 O  O     . PHE   B  1  839  ? 21.327  25.856  90.849  1.00 19.62 ? 837  PHE   B O     1 
ATOM   15238 C  CB    . PHE   B  1  839  ? 21.436  26.914  93.729  1.00 17.64 ? 837  PHE   B CB    1 
ATOM   15239 C  CG    . PHE   B  1  839  ? 22.143  27.754  94.741  1.00 17.15 ? 837  PHE   B CG    1 
ATOM   15240 C  CD1   . PHE   B  1  839  ? 23.428  28.225  94.488  1.00 17.32 ? 837  PHE   B CD1   1 
ATOM   15241 C  CD2   . PHE   B  1  839  ? 21.540  28.094  95.937  1.00 18.71 ? 837  PHE   B CD2   1 
ATOM   15242 C  CE1   . PHE   B  1  839  ? 24.078  29.016  95.398  1.00 17.14 ? 837  PHE   B CE1   1 
ATOM   15243 C  CE2   . PHE   B  1  839  ? 22.207  28.875  96.866  1.00 18.34 ? 837  PHE   B CE2   1 
ATOM   15244 C  CZ    . PHE   B  1  839  ? 23.486  29.330  96.597  1.00 17.21 ? 837  PHE   B CZ    1 
ATOM   15245 N  N     . ASP   B  1  840  ? 19.309  26.771  91.180  1.00 17.91 ? 838  ASP   B N     1 
ATOM   15246 C  CA    . ASP   B  1  840  ? 18.722  26.010  90.099  1.00 19.33 ? 838  ASP   B CA    1 
ATOM   15247 C  C     . ASP   B  1  840  ? 19.409  26.396  88.793  1.00 21.30 ? 838  ASP   B C     1 
ATOM   15248 O  O     . ASP   B  1  840  ? 19.833  27.541  88.600  1.00 19.25 ? 838  ASP   B O     1 
ATOM   15249 C  CB    . ASP   B  1  840  ? 17.230  26.306  90.035  1.00 25.94 ? 838  ASP   B CB    1 
ATOM   15250 C  CG    . ASP   B  1  840  ? 16.452  25.230  89.347  1.00 32.91 ? 838  ASP   B CG    1 
ATOM   15251 O  OD1   . ASP   B  1  840  ? 16.965  24.092  89.245  1.00 36.45 ? 838  ASP   B OD1   1 
ATOM   15252 O  OD2   . ASP   B  1  840  ? 15.328  25.531  88.896  1.00 35.89 ? 838  ASP   B OD2   1 
ATOM   15253 N  N     . SER   B  1  841  ? 19.570  25.414  87.909  1.00 18.52 ? 839  SER   B N     1 
ATOM   15254 C  CA    . SER   B  1  841  ? 20.320  25.595  86.660  1.00 18.30 ? 839  SER   B CA    1 
ATOM   15255 C  C     . SER   B  1  841  ? 21.749  26.021  86.919  1.00 17.19 ? 839  SER   B C     1 
ATOM   15256 O  O     . SER   B  1  841  ? 22.392  26.625  86.057  1.00 16.30 ? 839  SER   B O     1 
ATOM   15257 C  CB    . SER   B  1  841  ? 19.645  26.575  85.694  1.00 22.36 ? 839  SER   B CB    1 
ATOM   15258 O  OG    . SER   B  1  841  ? 18.331  26.152  85.399  1.00 22.01 ? 839  SER   B OG    1 
ATOM   15259 N  N     . ALA   B  1  842  ? 22.249  25.686  88.105  1.00 16.11 ? 840  ALA   B N     1 
ATOM   15260 C  CA    . ALA   B  1  842  ? 23.567  26.105  88.552  1.00 16.46 ? 840  ALA   B CA    1 
ATOM   15261 C  C     . ALA   B  1  842  ? 23.757  27.608  88.375  1.00 15.22 ? 840  ALA   B C     1 
ATOM   15262 O  O     . ALA   B  1  842  ? 24.837  28.086  88.029  1.00 15.71 ? 840  ALA   B O     1 
ATOM   15263 C  CB    . ALA   B  1  842  ? 24.684  25.280  87.905  1.00 16.96 ? 840  ALA   B CB    1 
ATOM   15264 N  N     . GLY   B  1  843  ? 22.683  28.360  88.625  1.00 14.62 ? 841  GLY   B N     1 
ATOM   15265 C  CA    . GLY   B  1  843  ? 22.785  29.803  88.550  1.00 14.15 ? 841  GLY   B CA    1 
ATOM   15266 C  C     . GLY   B  1  843  ? 22.944  30.332  87.154  1.00 15.10 ? 841  GLY   B C     1 
ATOM   15267 O  O     . GLY   B  1  843  ? 23.283  31.505  86.989  1.00 15.38 ? 841  GLY   B O     1 
ATOM   15268 N  N     . GLN   B  1  844  ? 22.715  29.495  86.149  1.00 14.32 ? 842  GLN   B N     1 
ATOM   15269 C  CA    . GLN   B  1  844  ? 22.961  29.875  84.757  1.00 13.94 ? 842  GLN   B CA    1 
ATOM   15270 C  C     . GLN   B  1  844  ? 21.690  30.404  84.101  1.00 14.99 ? 842  GLN   B C     1 
ATOM   15271 O  O     . GLN   B  1  844  ? 21.216  29.930  83.074  1.00 15.94 ? 842  GLN   B O     1 
ATOM   15272 C  CB    . GLN   B  1  844  ? 23.582  28.716  83.999  1.00 14.55 ? 842  GLN   B CB    1 
ATOM   15273 C  CG    . GLN   B  1  844  ? 24.948  28.407  84.555  1.00 14.40 ? 842  GLN   B CG    1 
ATOM   15274 C  CD    . GLN   B  1  844  ? 25.504  27.107  84.050  1.00 15.03 ? 842  GLN   B CD    1 
ATOM   15275 O  OE1   . GLN   B  1  844  ? 26.571  27.085  83.452  1.00 15.05 ? 842  GLN   B OE1   1 
ATOM   15276 N  NE2   . GLN   B  1  844  ? 24.809  26.011  84.332  1.00 16.76 ? 842  GLN   B NE2   1 
ATOM   15277 N  N     . ARG   B  1  845  ? 21.126  31.404  84.759  1.00 14.84 ? 843  ARG   B N     1 
ATOM   15278 C  CA    . ARG   B  1  845  ? 20.013  32.180  84.242  1.00 13.22 ? 843  ARG   B CA    1 
ATOM   15279 C  C     . ARG   B  1  845  ? 20.417  33.639  84.345  1.00 13.28 ? 843  ARG   B C     1 
ATOM   15280 O  O     . ARG   B  1  845  ? 20.984  34.064  85.351  1.00 14.00 ? 843  ARG   B O     1 
ATOM   15281 C  CB    . ARG   B  1  845  ? 18.763  31.980  85.080  1.00 15.18 ? 843  ARG   B CB    1 
ATOM   15282 C  CG    . ARG   B  1  845  ? 18.237  30.568  85.084  1.00 17.16 ? 843  ARG   B CG    1 
ATOM   15283 C  CD    . ARG   B  1  845  ? 16.855  30.610  85.686  1.00 23.02 ? 843  ARG   B CD    1 
ATOM   15284 N  NE    . ARG   B  1  845  ? 16.144  29.346  85.576  1.00 22.42 ? 843  ARG   B NE    1 
ATOM   15285 C  CZ    . ARG   B  1  845  ? 15.947  28.524  86.591  1.00 24.02 ? 843  ARG   B CZ    1 
ATOM   15286 N  NH1   . ARG   B  1  845  ? 16.491  28.751  87.777  1.00 26.46 ? 843  ARG   B NH1   1 
ATOM   15287 N  NH2   . ARG   B  1  845  ? 15.159  27.464  86.422  1.00 28.12 ? 843  ARG   B NH2   1 
ATOM   15288 N  N     . CYS   B  1  846  ? 20.087  34.435  83.335  1.00 14.59 ? 844  CYS   B N     1 
ATOM   15289 C  CA    . CYS   B  1  846  ? 20.371  35.856  83.458  1.00 15.13 ? 844  CYS   B CA    1 
ATOM   15290 C  C     . CYS   B  1  846  ? 19.649  36.458  84.650  1.00 12.06 ? 844  CYS   B C     1 
ATOM   15291 O  O     . CYS   B  1  846  ? 20.132  37.428  85.250  1.00 14.78 ? 844  CYS   B O     1 
ATOM   15292 C  CB    . CYS   B  1  846  ? 19.931  36.563  82.185  1.00 15.56 ? 844  CYS   B CB    1 
ATOM   15293 S  SG    . CYS   B  1  846  ? 18.280  36.166  81.624  1.00 15.05 ? 844  CYS   B SG    1 
ATOM   15294 N  N     . SER   B  1  847  ? 18.492  35.907  84.983  1.00 12.85 ? 845  SER   B N     1 
ATOM   15295 C  CA    . SER   B  1  847  ? 17.640  36.356  86.073  1.00 12.33 ? 845  SER   B CA    1 
ATOM   15296 C  C     . SER   B  1  847  ? 18.084  35.840  87.432  1.00 13.48 ? 845  SER   B C     1 
ATOM   15297 O  O     . SER   B  1  847  ? 17.453  36.189  88.439  1.00 13.64 ? 845  SER   B O     1 
ATOM   15298 C  CB    . SER   B  1  847  ? 16.246  35.807  85.797  1.00 13.99 ? 845  SER   B CB    1 
ATOM   15299 O  OG    . SER   B  1  847  ? 16.369  34.418  85.554  1.00 14.49 ? 845  SER   B OG    1 
ATOM   15300 N  N     . ALA   B  1  848  ? 19.134  35.024  87.489  1.00 12.98 ? 846  ALA   B N     1 
ATOM   15301 C  CA    . ALA   B  1  848  ? 19.465  34.328  88.720  1.00 13.25 ? 846  ALA   B CA    1 
ATOM   15302 C  C     . ALA   B  1  848  ? 19.809  35.302  89.834  1.00 13.86 ? 846  ALA   B C     1 
ATOM   15303 O  O     . ALA   B  1  848  ? 20.360  36.387  89.620  1.00 14.54 ? 846  ALA   B O     1 
ATOM   15304 C  CB    . ALA   B  1  848  ? 20.678  33.421  88.487  1.00 14.20 ? 846  ALA   B CB    1 
ATOM   15305 N  N     . LEU   B  1  849  ? 19.495  34.878  91.051  1.00 13.46 ? 847  LEU   B N     1 
ATOM   15306 C  CA    . LEU   B  1  849  ? 19.825  35.665  92.228  1.00 13.74 ? 847  LEU   B CA    1 
ATOM   15307 C  C     . LEU   B  1  849  ? 21.323  35.638  92.483  1.00 13.54 ? 847  LEU   B C     1 
ATOM   15308 O  O     . LEU   B  1  849  ? 21.902  34.567  92.660  1.00 15.26 ? 847  LEU   B O     1 
ATOM   15309 C  CB    . LEU   B  1  849  ? 19.069  35.077  93.405  1.00 14.94 ? 847  LEU   B CB    1 
ATOM   15310 C  CG    . LEU   B  1  849  ? 19.444  35.698  94.734  1.00 15.01 ? 847  LEU   B CG    1 
ATOM   15311 C  CD1   . LEU   B  1  849  ? 19.179  37.192  94.739  1.00 16.26 ? 847  LEU   B CD1   1 
ATOM   15312 C  CD2   . LEU   B  1  849  ? 18.665  34.993  95.844  1.00 16.36 ? 847  LEU   B CD2   1 
ATOM   15313 N  N     . ARG   B  1  850  ? 21.941  36.813  92.487  1.00 13.79 ? 848  ARG   B N     1 
ATOM   15314 C  CA    . ARG   B  1  850  ? 23.370  36.944  92.701  1.00 14.83 ? 848  ARG   B CA    1 
ATOM   15315 C  C     . ARG   B  1  850  ? 23.709  37.515  94.062  1.00 14.92 ? 848  ARG   B C     1 
ATOM   15316 O  O     . ARG   B  1  850  ? 24.769  37.208  94.603  1.00 14.73 ? 848  ARG   B O     1 
ATOM   15317 C  CB    . ARG   B  1  850  ? 23.987  37.870  91.640  1.00 14.62 ? 848  ARG   B CB    1 
ATOM   15318 C  CG    . ARG   B  1  850  ? 23.658  37.491  90.218  1.00 14.17 ? 848  ARG   B CG    1 
ATOM   15319 C  CD    . ARG   B  1  850  ? 24.043  36.078  89.943  1.00 14.05 ? 848  ARG   B CD    1 
ATOM   15320 N  NE    . ARG   B  1  850  ? 23.843  35.759  88.540  1.00 14.78 ? 848  ARG   B NE    1 
ATOM   15321 C  CZ    . ARG   B  1  850  ? 23.940  34.533  88.049  1.00 14.74 ? 848  ARG   B CZ    1 
ATOM   15322 N  NH1   . ARG   B  1  850  ? 24.183  33.490  88.826  1.00 15.37 ? 848  ARG   B NH1   1 
ATOM   15323 N  NH2   . ARG   B  1  850  ? 23.728  34.339  86.749  1.00 15.23 ? 848  ARG   B NH2   1 
ATOM   15324 N  N     . VAL   B  1  851  ? 22.848  38.353  94.623  1.00 15.24 ? 849  VAL   B N     1 
ATOM   15325 C  CA    . VAL   B  1  851  ? 23.130  39.032  95.881  1.00 15.38 ? 849  VAL   B CA    1 
ATOM   15326 C  C     . VAL   B  1  851  ? 21.902  38.931  96.769  1.00 15.01 ? 849  VAL   B C     1 
ATOM   15327 O  O     . VAL   B  1  851  ? 20.875  39.558  96.492  1.00 15.38 ? 849  VAL   B O     1 
ATOM   15328 C  CB    . VAL   B  1  851  ? 23.522  40.500  95.676  1.00 16.78 ? 849  VAL   B CB    1 
ATOM   15329 C  CG1   . VAL   B  1  851  ? 23.910  41.102  97.029  1.00 18.23 ? 849  VAL   B CG1   1 
ATOM   15330 C  CG2   . VAL   B  1  851  ? 24.671  40.634  94.663  1.00 18.95 ? 849  VAL   B CG2   1 
ATOM   15331 N  N     . LEU   B  1  852  ? 22.004  38.144  97.835  1.00 14.61 ? 850  LEU   B N     1 
ATOM   15332 C  CA    . LEU   B  1  852  ? 20.942  38.013  98.819  1.00 15.29 ? 850  LEU   B CA    1 
ATOM   15333 C  C     . LEU   B  1  852  ? 21.225  38.984  99.954  1.00 14.67 ? 850  LEU   B C     1 
ATOM   15334 O  O     . LEU   B  1  852  ? 22.282  38.902  100.591 1.00 14.98 ? 850  LEU   B O     1 
ATOM   15335 C  CB    . LEU   B  1  852  ? 20.911  36.575  99.329  1.00 15.28 ? 850  LEU   B CB    1 
ATOM   15336 C  CG    . LEU   B  1  852  ? 19.896  36.297  100.433 1.00 14.99 ? 850  LEU   B CG    1 
ATOM   15337 C  CD1   . LEU   B  1  852  ? 18.471  36.606  99.958  1.00 16.53 ? 850  LEU   B CD1   1 
ATOM   15338 C  CD2   . LEU   B  1  852  ? 19.990  34.853  100.883 1.00 17.15 ? 850  LEU   B CD2   1 
ATOM   15339 N  N     . CYS   B  1  853  ? 20.306  39.908  100.187 1.00 14.62 ? 851  CYS   B N     1 
ATOM   15340 C  CA    . CYS   B  1  853  ? 20.474  40.944  101.201 1.00 15.08 ? 851  CYS   B CA    1 
ATOM   15341 C  C     . CYS   B  1  853  ? 19.531  40.630  102.346 1.00 14.44 ? 851  CYS   B C     1 
ATOM   15342 O  O     . CYS   B  1  853  ? 18.310  40.682  102.188 1.00 15.34 ? 851  CYS   B O     1 
ATOM   15343 C  CB    . CYS   B  1  853  ? 20.169  42.322  100.631 1.00 15.88 ? 851  CYS   B CB    1 
ATOM   15344 S  SG    . CYS   B  1  853  ? 21.117  42.673  99.149  1.00 18.15 ? 851  CYS   B SG    1 
ATOM   15345 N  N     . LEU   B  1  854  ? 20.094  40.296  103.498 1.00 14.97 ? 852  LEU   B N     1 
ATOM   15346 C  CA    . LEU   B  1  854  ? 19.314  39.818  104.627 1.00 16.62 ? 852  LEU   B CA    1 
ATOM   15347 C  C     . LEU   B  1  854  ? 19.359  40.852  105.736 1.00 15.80 ? 852  LEU   B C     1 
ATOM   15348 O  O     . LEU   B  1  854  ? 20.440  41.303  106.123 1.00 15.90 ? 852  LEU   B O     1 
ATOM   15349 C  CB    . LEU   B  1  854  ? 19.919  38.522  105.157 1.00 17.37 ? 852  LEU   B CB    1 
ATOM   15350 C  CG    . LEU   B  1  854  ? 19.930  37.386  104.136 1.00 15.85 ? 852  LEU   B CG    1 
ATOM   15351 C  CD1   . LEU   B  1  854  ? 20.660  36.183  104.742 1.00 18.29 ? 852  LEU   B CD1   1 
ATOM   15352 C  CD2   . LEU   B  1  854  ? 18.509  37.034  103.755 1.00 18.48 ? 852  LEU   B CD2   1 
ATOM   15353 N  N     . GLN   B  1  855  ? 18.197  41.206  106.268 1.00 16.36 ? 853  GLN   B N     1 
ATOM   15354 C  CA    . GLN   B  1  855  ? 18.208  42.096  107.421 1.00 16.01 ? 853  GLN   B CA    1 
ATOM   15355 C  C     . GLN   B  1  855  ? 18.994  41.427  108.543 1.00 18.74 ? 853  GLN   B C     1 
ATOM   15356 O  O     . GLN   B  1  855  ? 18.883  40.217  108.756 1.00 17.82 ? 853  GLN   B O     1 
ATOM   15357 C  CB    . GLN   B  1  855  ? 16.790  42.399  107.872 1.00 17.14 ? 853  GLN   B CB    1 
ATOM   15358 C  CG    . GLN   B  1  855  ? 16.710  43.571  108.831 1.00 19.49 ? 853  GLN   B CG    1 
ATOM   15359 C  CD    . GLN   B  1  855  ? 15.303  43.872  109.272 1.00 25.07 ? 853  GLN   B CD    1 
ATOM   15360 O  OE1   . GLN   B  1  855  ? 14.374  43.856  108.476 1.00 25.42 ? 853  GLN   B OE1   1 
ATOM   15361 N  NE2   . GLN   B  1  855  ? 15.134  44.150  110.553 1.00 27.02 ? 853  GLN   B NE2   1 
ATOM   15362 N  N     . GLU   B  1  856  ? 19.816  42.224  109.232 1.00 18.21 ? 854  GLU   B N     1 
ATOM   15363 C  CA    . GLU   B  1  856  ? 20.818  41.675  110.143 1.00 20.03 ? 854  GLU   B CA    1 
ATOM   15364 C  C     . GLU   B  1  856  ? 20.203  40.737  111.174 1.00 19.34 ? 854  GLU   B C     1 
ATOM   15365 O  O     . GLU   B  1  856  ? 20.801  39.711  111.522 1.00 21.88 ? 854  GLU   B O     1 
ATOM   15366 C  CB    . GLU   B  1  856  ? 21.565  42.820  110.838 1.00 25.78 ? 854  GLU   B CB    1 
ATOM   15367 N  N     . ASP   B  1  857  ? 19.011  41.066  111.671 1.00 19.94 ? 855  ASP   B N     1 
ATOM   15368 C  CA    . ASP   B  1  857  ? 18.430  40.319  112.785 1.00 23.04 ? 855  ASP   B CA    1 
ATOM   15369 C  C     . ASP   B  1  857  ? 17.964  38.924  112.394 1.00 22.06 ? 855  ASP   B C     1 
ATOM   15370 O  O     . ASP   B  1  857  ? 17.813  38.068  113.271 1.00 24.61 ? 855  ASP   B O     1 
ATOM   15371 C  CB    . ASP   B  1  857  ? 17.259  41.096  113.389 1.00 29.84 ? 855  ASP   B CB    1 
ATOM   15372 N  N     . VAL   B  1  858  ? 17.710  38.674  111.114 1.00 17.65 ? 856  VAL   B N     1 
ATOM   15373 C  CA    . VAL   B  1  858  ? 17.265  37.365  110.657 1.00 18.44 ? 856  VAL   B CA    1 
ATOM   15374 C  C     . VAL   B  1  858  ? 18.309  36.654  109.829 1.00 15.31 ? 856  VAL   B C     1 
ATOM   15375 O  O     . VAL   B  1  858  ? 18.082  35.504  109.426 1.00 17.62 ? 856  VAL   B O     1 
ATOM   15376 C  CB    . VAL   B  1  858  ? 15.927  37.429  109.900 1.00 18.32 ? 856  VAL   B CB    1 
ATOM   15377 C  CG1   . VAL   B  1  858  ? 14.831  37.924  110.825 1.00 22.41 ? 856  VAL   B CG1   1 
ATOM   15378 C  CG2   . VAL   B  1  858  ? 16.053  38.333  108.678 1.00 19.08 ? 856  VAL   B CG2   1 
ATOM   15379 N  N     . ALA   B  1  859  ? 19.447  37.295  109.560 1.00 16.72 ? 857  ALA   B N     1 
ATOM   15380 C  CA    . ALA   B  1  859  ? 20.412  36.739  108.616 1.00 17.82 ? 857  ALA   B CA    1 
ATOM   15381 C  C     . ALA   B  1  859  ? 20.902  35.365  109.049 1.00 17.75 ? 857  ALA   B C     1 
ATOM   15382 O  O     . ALA   B  1  859  ? 20.931  34.431  108.246 1.00 18.22 ? 857  ALA   B O     1 
ATOM   15383 C  CB    . ALA   B  1  859  ? 21.587  37.696  108.423 1.00 17.86 ? 857  ALA   B CB    1 
ATOM   15384 N  N     . ASP   B  1  860  ? 21.322  35.229  110.306 1.00 18.68 ? 858  ASP   B N     1 
ATOM   15385 C  CA    . ASP   B  1  860  ? 21.900  33.965  110.746 1.00 18.65 ? 858  ASP   B CA    1 
ATOM   15386 C  C     . ASP   B  1  860  ? 20.904  32.825  110.638 1.00 18.80 ? 858  ASP   B C     1 
ATOM   15387 O  O     . ASP   B  1  860  ? 21.255  31.735  110.172 1.00 18.68 ? 858  ASP   B O     1 
ATOM   15388 C  CB    . ASP   B  1  860  ? 22.395  34.073  112.189 1.00 18.40 ? 858  ASP   B CB    1 
ATOM   15389 C  CG    . ASP   B  1  860  ? 23.610  34.955  112.325 1.00 26.14 ? 858  ASP   B CG    1 
ATOM   15390 O  OD1   . ASP   B  1  860  ? 24.398  35.045  111.361 1.00 29.20 ? 858  ASP   B OD1   1 
ATOM   15391 O  OD2   . ASP   B  1  860  ? 23.777  35.562  113.403 1.00 30.63 ? 858  ASP   B OD2   1 
ATOM   15392 N  N     . ARG   B  1  861  ? 19.654  33.053  111.055 1.00 17.04 ? 859  ARG   B N     1 
ATOM   15393 C  CA    . ARG   B  1  861  ? 18.671  31.981  110.990 1.00 19.35 ? 859  ARG   B CA    1 
ATOM   15394 C  C     . ARG   B  1  861  ? 18.360  31.605  109.550 1.00 16.96 ? 859  ARG   B C     1 
ATOM   15395 O  O     . ARG   B  1  861  ? 18.233  30.420  109.224 1.00 18.21 ? 859  ARG   B O     1 
ATOM   15396 C  CB    . ARG   B  1  861  ? 17.400  32.354  111.750 1.00 22.20 ? 859  ARG   B CB    1 
ATOM   15397 C  CG    . ARG   B  1  861  ? 16.364  31.260  111.704 1.00 30.95 ? 859  ARG   B CG    1 
ATOM   15398 C  CD    . ARG   B  1  861  ? 15.241  31.474  112.691 1.00 35.99 ? 859  ARG   B CD    1 
ATOM   15399 N  NE    . ARG   B  1  861  ? 14.174  30.518  112.426 1.00 46.01 ? 859  ARG   B NE    1 
ATOM   15400 C  CZ    . ARG   B  1  861  ? 13.124  30.773  111.659 1.00 41.74 ? 859  ARG   B CZ    1 
ATOM   15401 N  NH1   . ARG   B  1  861  ? 12.931  31.972  111.131 1.00 38.47 ? 859  ARG   B NH1   1 
ATOM   15402 N  NH2   . ARG   B  1  861  ? 12.248  29.802  111.413 1.00 42.06 ? 859  ARG   B NH2   1 
ATOM   15403 N  N     . ILE   B  1  862  ? 18.254  32.598  108.669 1.00 15.88 ? 860  ILE   B N     1 
ATOM   15404 C  CA    . ILE   B  1  862  ? 18.002  32.285  107.269 1.00 16.36 ? 860  ILE   B CA    1 
ATOM   15405 C  C     . ILE   B  1  862  ? 19.180  31.550  106.657 1.00 15.34 ? 860  ILE   B C     1 
ATOM   15406 O  O     . ILE   B  1  862  ? 18.991  30.581  105.913 1.00 16.76 ? 860  ILE   B O     1 
ATOM   15407 C  CB    . ILE   B  1  862  ? 17.637  33.563  106.507 1.00 16.59 ? 860  ILE   B CB    1 
ATOM   15408 C  CG1   . ILE   B  1  862  ? 16.262  34.034  106.983 1.00 19.90 ? 860  ILE   B CG1   1 
ATOM   15409 C  CG2   . ILE   B  1  862  ? 17.686  33.324  104.996 1.00 15.80 ? 860  ILE   B CG2   1 
ATOM   15410 C  CD1   . ILE   B  1  862  ? 15.863  35.401  106.470 1.00 22.26 ? 860  ILE   B CD1   1 
ATOM   15411 N  N     . LEU   B  1  863  ? 20.405  31.983  106.955 1.00 16.55 ? 861  LEU   B N     1 
ATOM   15412 C  CA    . LEU   B  1  863  ? 21.560  31.313  106.372 1.00 17.27 ? 861  LEU   B CA    1 
ATOM   15413 C  C     . LEU   B  1  863  ? 21.683  29.885  106.876 1.00 19.20 ? 861  LEU   B C     1 
ATOM   15414 O  O     . LEU   B  1  863  ? 22.051  28.985  106.116 1.00 17.38 ? 861  LEU   B O     1 
ATOM   15415 C  CB    . LEU   B  1  863  ? 22.828  32.098  106.666 1.00 17.84 ? 861  LEU   B CB    1 
ATOM   15416 C  CG    . LEU   B  1  863  ? 22.876  33.399  105.875 1.00 19.15 ? 861  LEU   B CG    1 
ATOM   15417 C  CD1   . LEU   B  1  863  ? 24.002  34.251  106.424 1.00 21.91 ? 861  LEU   B CD1   1 
ATOM   15418 C  CD2   . LEU   B  1  863  ? 23.071  33.136  104.384 1.00 20.95 ? 861  LEU   B CD2   1 
ATOM   15419 N  N     . THR   B  1  864  ? 21.388  29.651  108.151 1.00 16.97 ? 862  THR   B N     1 
ATOM   15420 C  CA    . THR   B  1  864  ? 21.435  28.284  108.642 1.00 19.12 ? 862  THR   B CA    1 
ATOM   15421 C  C     . THR   B  1  864  ? 20.434  27.422  107.904 1.00 18.24 ? 862  THR   B C     1 
ATOM   15422 O  O     . THR   B  1  864  ? 20.744  26.295  107.501 1.00 18.81 ? 862  THR   B O     1 
ATOM   15423 C  CB    . THR   B  1  864  ? 21.130  28.274  110.134 1.00 21.08 ? 862  THR   B CB    1 
ATOM   15424 O  OG1   . THR   B  1  864  ? 22.183  28.951  110.817 1.00 23.90 ? 862  THR   B OG1   1 
ATOM   15425 C  CG2   . THR   B  1  864  ? 20.998  26.835  110.657 1.00 24.07 ? 862  THR   B CG2   1 
ATOM   15426 N  N     . MET   B  1  865  ? 19.230  27.949  107.690 1.00 16.33 ? 863  MET   B N     1 
ATOM   15427 C  CA    . MET   B  1  865  ? 18.214  27.180  106.999 1.00 17.44 ? 863  MET   B CA    1 
ATOM   15428 C  C     . MET   B  1  865  ? 18.604  26.971  105.545 1.00 16.93 ? 863  MET   B C     1 
ATOM   15429 O  O     . MET   B  1  865  ? 18.413  25.885  104.993 1.00 16.76 ? 863  MET   B O     1 
ATOM   15430 C  CB    . MET   B  1  865  ? 16.878  27.910  107.099 1.00 17.62 ? 863  MET   B CB    1 
ATOM   15431 C  CG    . MET   B  1  865  ? 15.737  27.116  106.550 1.00 19.05 ? 863  MET   B CG    1 
ATOM   15432 S  SD    . MET   B  1  865  ? 14.202  28.023  106.690 1.00 20.73 ? 863  MET   B SD    1 
ATOM   15433 C  CE    . MET   B  1  865  ? 14.060  28.161  108.472 1.00 24.41 ? 863  MET   B CE    1 
ATOM   15434 N  N     . LEU   B  1  866  ? 19.145  28.010  104.916 1.00 16.50 ? 864  LEU   B N     1 
ATOM   15435 C  CA    . LEU   B  1  866  ? 19.572  27.896  103.526 1.00 16.09 ? 864  LEU   B CA    1 
ATOM   15436 C  C     . LEU   B  1  866  ? 20.636  26.821  103.381 1.00 16.19 ? 864  LEU   B C     1 
ATOM   15437 O  O     . LEU   B  1  866  ? 20.563  25.966  102.493 1.00 15.96 ? 864  LEU   B O     1 
ATOM   15438 C  CB    . LEU   B  1  866  ? 20.109  29.243  103.057 1.00 17.33 ? 864  LEU   B CB    1 
ATOM   15439 C  CG    . LEU   B  1  866  ? 20.711  29.205  101.651 1.00 14.94 ? 864  LEU   B CG    1 
ATOM   15440 C  CD1   . LEU   B  1  866  ? 19.687  28.756  100.623 1.00 17.74 ? 864  LEU   B CD1   1 
ATOM   15441 C  CD2   . LEU   B  1  866  ? 21.257  30.596  101.318 1.00 19.05 ? 864  LEU   B CD2   1 
ATOM   15442 N  N     . LYS   B  1  867  ? 21.621  26.828  104.277 1.00 16.41 ? 865  LYS   B N     1 
ATOM   15443 C  CA    . LYS   B  1  867  ? 22.689  25.845  104.178 1.00 16.94 ? 865  LYS   B CA    1 
ATOM   15444 C  C     . LYS   B  1  867  ? 22.163  24.441  104.435 1.00 16.87 ? 865  LYS   B C     1 
ATOM   15445 O  O     . LYS   B  1  867  ? 22.561  23.490  103.754 1.00 17.18 ? 865  LYS   B O     1 
ATOM   15446 C  CB    . LYS   B  1  867  ? 23.841  26.232  105.106 1.00 19.32 ? 865  LYS   B CB    1 
ATOM   15447 C  CG    . LYS   B  1  867  ? 24.545  27.503  104.611 1.00 20.35 ? 865  LYS   B CG    1 
ATOM   15448 C  CD    . LYS   B  1  867  ? 25.436  28.128  105.667 1.00 22.78 ? 865  LYS   B CD    1 
ATOM   15449 C  CE    . LYS   B  1  867  ? 25.966  29.473  105.179 1.00 30.76 ? 865  LYS   B CE    1 
ATOM   15450 N  NZ    . LYS   B  1  867  ? 26.739  30.190  106.239 1.00 33.34 ? 865  LYS   B NZ    1 
ATOM   15451 N  N     . GLY   B  1  868  ? 21.225  24.295  105.370 1.00 17.59 ? 866  GLY   B N     1 
ATOM   15452 C  CA    . GLY   B  1  868  ? 20.635  22.987  105.584 1.00 18.08 ? 866  GLY   B CA    1 
ATOM   15453 C  C     . GLY   B  1  868  ? 19.861  22.501  104.374 1.00 16.99 ? 866  GLY   B C     1 
ATOM   15454 O  O     . GLY   B  1  868  ? 19.910  21.319  104.020 1.00 18.83 ? 866  GLY   B O     1 
ATOM   15455 N  N     . ALA   B  1  869  ? 19.125  23.404  103.724 1.00 17.44 ? 867  ALA   B N     1 
ATOM   15456 C  CA    . ALA   B  1  869  ? 18.400  23.040  102.515 1.00 16.58 ? 867  ALA   B CA    1 
ATOM   15457 C  C     . ALA   B  1  869  ? 19.365  22.696  101.385 1.00 15.09 ? 867  ALA   B C     1 
ATOM   15458 O  O     . ALA   B  1  869  ? 19.127  21.753  100.621 1.00 16.63 ? 867  ALA   B O     1 
ATOM   15459 C  CB    . ALA   B  1  869  ? 17.470  24.182  102.123 1.00 17.18 ? 867  ALA   B CB    1 
ATOM   15460 N  N     . LEU   B  1  870  ? 20.484  23.427  101.289 1.00 15.08 ? 868  LEU   B N     1 
ATOM   15461 C  CA    . LEU   B  1  870  ? 21.453  23.139  100.232 1.00 16.32 ? 868  LEU   B CA    1 
ATOM   15462 C  C     . LEU   B  1  870  ? 22.068  21.763  100.403 1.00 16.98 ? 868  LEU   B C     1 
ATOM   15463 O  O     . LEU   B  1  870  ? 22.416  21.116  99.417  1.00 17.89 ? 868  LEU   B O     1 
ATOM   15464 C  CB    . LEU   B  1  870  ? 22.564  24.183  100.210 1.00 17.91 ? 868  LEU   B CB    1 
ATOM   15465 C  CG    . LEU   B  1  870  ? 22.145  25.522  99.620  1.00 18.72 ? 868  LEU   B CG    1 
ATOM   15466 C  CD1   . LEU   B  1  870  ? 23.257  26.525  99.769  1.00 20.37 ? 868  LEU   B CD1   1 
ATOM   15467 C  CD2   . LEU   B  1  870  ? 21.765  25.344  98.134  1.00 20.06 ? 868  LEU   B CD2   1 
ATOM   15468 N  N     . HIS   B  1  871  ? 22.202  21.301  101.643 1.00 16.44 ? 869  HIS   B N     1 
ATOM   15469 C  CA    A HIS   B  1  871  ? 22.772  19.981  101.867 0.52 17.46 ? 869  HIS   B CA    1 
ATOM   15470 C  CA    B HIS   B  1  871  ? 22.750  19.978  101.912 0.48 17.46 ? 869  HIS   B CA    1 
ATOM   15471 C  C     . HIS   B  1  871  ? 21.877  18.869  101.345 1.00 19.35 ? 869  HIS   B C     1 
ATOM   15472 O  O     . HIS   B  1  871  ? 22.348  17.738  101.173 1.00 19.86 ? 869  HIS   B O     1 
ATOM   15473 C  CB    A HIS   B  1  871  ? 23.107  19.778  103.346 0.52 18.78 ? 869  HIS   B CB    1 
ATOM   15474 C  CB    B HIS   B  1  871  ? 22.896  19.790  103.424 0.48 18.50 ? 869  HIS   B CB    1 
ATOM   15475 C  CG    A HIS   B  1  871  ? 24.449  20.314  103.736 0.52 21.55 ? 869  HIS   B CG    1 
ATOM   15476 C  CG    B HIS   B  1  871  ? 23.548  18.502  103.811 0.48 21.10 ? 869  HIS   B CG    1 
ATOM   15477 N  ND1   A HIS   B  1  871  ? 24.628  21.582  104.247 0.52 24.67 ? 869  HIS   B ND1   1 
ATOM   15478 N  ND1   B HIS   B  1  871  ? 24.901  18.286  103.672 0.48 25.46 ? 869  HIS   B ND1   1 
ATOM   15479 C  CD2   A HIS   B  1  871  ? 25.681  19.754  103.678 0.52 25.53 ? 869  HIS   B CD2   1 
ATOM   15480 C  CD2   B HIS   B  1  871  ? 23.032  17.356  104.317 0.48 23.57 ? 869  HIS   B CD2   1 
ATOM   15481 C  CE1   A HIS   B  1  871  ? 25.910  21.777  104.493 0.52 25.43 ? 869  HIS   B CE1   1 
ATOM   15482 C  CE1   B HIS   B  1  871  ? 25.194  17.065  104.084 0.48 23.84 ? 869  HIS   B CE1   1 
ATOM   15483 N  NE2   A HIS   B  1  871  ? 26.571  20.686  104.151 0.52 22.16 ? 869  HIS   B NE2   1 
ATOM   15484 N  NE2   B HIS   B  1  871  ? 24.078  16.480  104.481 0.48 25.59 ? 869  HIS   B NE2   1 
ATOM   15485 N  N     . GLU   B  1  872  ? 20.616  19.162  101.061 1.00 15.54 ? 870  GLU   B N     1 
ATOM   15486 C  CA    . GLU   B  1  872  ? 19.701  18.153  100.562 1.00 17.14 ? 870  GLU   B CA    1 
ATOM   15487 C  C     . GLU   B  1  872  ? 19.626  18.105  99.051  1.00 16.10 ? 870  GLU   B C     1 
ATOM   15488 O  O     . GLU   B  1  872  ? 18.862  17.296  98.518  1.00 18.36 ? 870  GLU   B O     1 
ATOM   15489 C  CB    . GLU   B  1  872  ? 18.309  18.385  101.139 1.00 17.75 ? 870  GLU   B CB    1 
ATOM   15490 C  CG    . GLU   B  1  872  ? 18.331  18.401  102.642 1.00 17.21 ? 870  GLU   B CG    1 
ATOM   15491 C  CD    . GLU   B  1  872  ? 18.718  17.071  103.228 1.00 20.36 ? 870  GLU   B CD    1 
ATOM   15492 O  OE1   . GLU   B  1  872  ? 18.525  16.041  102.549 1.00 22.03 ? 870  GLU   B OE1   1 
ATOM   15493 O  OE2   . GLU   B  1  872  ? 19.205  17.037  104.370 1.00 22.05 ? 870  GLU   B OE2   1 
ATOM   15494 N  N     . LEU   B  1  873  ? 20.392  18.936  98.351  1.00 16.49 ? 871  LEU   B N     1 
ATOM   15495 C  CA    . LEU   B  1  873  ? 20.322  18.954  96.902  1.00 16.72 ? 871  LEU   B CA    1 
ATOM   15496 C  C     . LEU   B  1  873  ? 21.229  17.890  96.317  1.00 17.13 ? 871  LEU   B C     1 
ATOM   15497 O  O     . LEU   B  1  873  ? 22.288  17.576  96.855  1.00 20.20 ? 871  LEU   B O     1 
ATOM   15498 C  CB    . LEU   B  1  873  ? 20.751  20.308  96.356  1.00 17.77 ? 871  LEU   B CB    1 
ATOM   15499 C  CG    . LEU   B  1  873  ? 19.860  21.475  96.760  1.00 18.82 ? 871  LEU   B CG    1 
ATOM   15500 C  CD1   . LEU   B  1  873  ? 20.298  22.716  95.982  1.00 21.95 ? 871  LEU   B CD1   1 
ATOM   15501 C  CD2   . LEU   B  1  873  ? 18.387  21.173  96.528  1.00 18.96 ? 871  LEU   B CD2   1 
ATOM   15502 N  N     . HIS   B  1  874  ? 20.802  17.347  95.195  1.00 16.77 ? 872  HIS   B N     1 
ATOM   15503 C  CA    . HIS   B  1  874  ? 21.570  16.364  94.455  1.00 18.97 ? 872  HIS   B CA    1 
ATOM   15504 C  C     . HIS   B  1  874  ? 22.144  17.065  93.227  1.00 16.98 ? 872  HIS   B C     1 
ATOM   15505 O  O     . HIS   B  1  874  ? 21.388  17.609  92.409  1.00 16.58 ? 872  HIS   B O     1 
ATOM   15506 C  CB    . HIS   B  1  874  ? 20.628  15.226  94.075  1.00 19.48 ? 872  HIS   B CB    1 
ATOM   15507 C  CG    . HIS   B  1  874  ? 21.267  14.128  93.290  1.00 20.27 ? 872  HIS   B CG    1 
ATOM   15508 N  ND1   . HIS   B  1  874  ? 20.560  13.022  92.871  1.00 25.72 ? 872  HIS   B ND1   1 
ATOM   15509 C  CD2   . HIS   B  1  874  ? 22.535  13.959  92.844  1.00 26.33 ? 872  HIS   B CD2   1 
ATOM   15510 C  CE1   . HIS   B  1  874  ? 21.365  12.220  92.193  1.00 26.92 ? 872  HIS   B CE1   1 
ATOM   15511 N  NE2   . HIS   B  1  874  ? 22.568  12.766  92.162  1.00 26.68 ? 872  HIS   B NE2   1 
ATOM   15512 N  N     . ILE   B  1  875  ? 23.470  17.097  93.134  1.00 17.53 ? 873  ILE   B N     1 
ATOM   15513 C  CA    . ILE   B  1  875  ? 24.185  17.706  92.016  1.00 17.26 ? 873  ILE   B CA    1 
ATOM   15514 C  C     . ILE   B  1  875  ? 24.689  16.575  91.140  1.00 17.86 ? 873  ILE   B C     1 
ATOM   15515 O  O     . ILE   B  1  875  ? 25.356  15.663  91.634  1.00 19.46 ? 873  ILE   B O     1 
ATOM   15516 C  CB    . ILE   B  1  875  ? 25.376  18.538  92.511  1.00 19.45 ? 873  ILE   B CB    1 
ATOM   15517 C  CG1   . ILE   B  1  875  ? 24.933  19.616  93.500  1.00 21.57 ? 873  ILE   B CG1   1 
ATOM   15518 C  CG2   . ILE   B  1  875  ? 26.115  19.156  91.326  1.00 20.82 ? 873  ILE   B CG2   1 
ATOM   15519 C  CD1   . ILE   B  1  875  ? 26.043  20.063  94.425  1.00 26.93 ? 873  ILE   B CD1   1 
ATOM   15520 N  N     . GLY   B  1  876  ? 24.389  16.624  89.849  1.00 16.52 ? 874  GLY   B N     1 
ATOM   15521 C  CA    . GLY   B  1  876  ? 24.877  15.558  89.000  1.00 17.49 ? 874  GLY   B CA    1 
ATOM   15522 C  C     . GLY   B  1  876  ? 24.381  15.709  87.584  1.00 16.92 ? 874  GLY   B C     1 
ATOM   15523 O  O     . GLY   B  1  876  ? 23.778  16.713  87.217  1.00 16.86 ? 874  GLY   B O     1 
ATOM   15524 N  N     . ARG   B  1  877  ? 24.667  14.681  86.791  1.00 18.93 ? 875  ARG   B N     1 
ATOM   15525 C  CA    . ARG   B  1  877  ? 24.167  14.628  85.432  1.00 18.11 ? 875  ARG   B CA    1 
ATOM   15526 C  C     . ARG   B  1  877  ? 22.646  14.613  85.465  1.00 17.48 ? 875  ARG   B C     1 
ATOM   15527 O  O     . ARG   B  1  877  ? 22.038  13.877  86.241  1.00 19.02 ? 875  ARG   B O     1 
ATOM   15528 C  CB    . ARG   B  1  877  ? 24.713  13.376  84.759  1.00 20.64 ? 875  ARG   B CB    1 
ATOM   15529 C  CG    . ARG   B  1  877  ? 24.611  13.431  83.263  1.00 22.57 ? 875  ARG   B CG    1 
ATOM   15530 C  CD    . ARG   B  1  877  ? 25.290  12.229  82.669  1.00 26.32 ? 875  ARG   B CD    1 
ATOM   15531 N  NE    . ARG   B  1  877  ? 24.427  11.065  82.634  1.00 24.67 ? 875  ARG   B NE    1 
ATOM   15532 C  CZ    . ARG   B  1  877  ? 24.759  9.926   82.047  1.00 29.71 ? 875  ARG   B CZ    1 
ATOM   15533 N  NH1   . ARG   B  1  877  ? 25.964  9.748   81.522  1.00 26.73 ? 875  ARG   B NH1   1 
ATOM   15534 N  NH2   . ARG   B  1  877  ? 23.859  8.948   81.970  1.00 31.23 ? 875  ARG   B NH2   1 
ATOM   15535 N  N     . THR   B  1  878  ? 22.027  15.426  84.615  1.00 16.73 ? 876  THR   B N     1 
ATOM   15536 C  CA    . THR   B  1  878  ? 20.624  15.784  84.793  1.00 18.62 ? 876  THR   B CA    1 
ATOM   15537 C  C     . THR   B  1  878  ? 19.628  14.796  84.196  1.00 16.28 ? 876  THR   B C     1 
ATOM   15538 O  O     . THR   B  1  878  ? 18.429  15.073  84.215  1.00 17.83 ? 876  THR   B O     1 
ATOM   15539 C  CB    . THR   B  1  878  ? 20.370  17.178  84.241  1.00 17.73 ? 876  THR   B CB    1 
ATOM   15540 O  OG1   . THR   B  1  878  ? 20.898  17.261  82.913  1.00 21.31 ? 876  THR   B OG1   1 
ATOM   15541 C  CG2   . THR   B  1  878  ? 21.069  18.202  85.111  1.00 20.45 ? 876  THR   B CG2   1 
ATOM   15542 N  N     . ASP   B  1  879  ? 20.078  13.647  83.706  1.00 16.27 ? 877  ASP   B N     1 
ATOM   15543 C  CA    . ASP   B  1  879  ? 19.173  12.649  83.153  1.00 16.58 ? 877  ASP   B CA    1 
ATOM   15544 C  C     . ASP   B  1  879  ? 18.601  11.733  84.222  1.00 18.03 ? 877  ASP   B C     1 
ATOM   15545 O  O     . ASP   B  1  879  ? 18.231  10.589  83.933  1.00 19.14 ? 877  ASP   B O     1 
ATOM   15546 C  CB    . ASP   B  1  879  ? 19.846  11.862  82.029  1.00 18.80 ? 877  ASP   B CB    1 
ATOM   15547 C  CG    . ASP   B  1  879  ? 21.025  11.040  82.516  1.00 21.82 ? 877  ASP   B CG    1 
ATOM   15548 O  OD1   . ASP   B  1  879  ? 21.719  11.461  83.469  1.00 24.39 ? 877  ASP   B OD1   1 
ATOM   15549 O  OD2   . ASP   B  1  879  ? 21.256  9.960   81.942  1.00 22.67 ? 877  ASP   B OD2   1 
ATOM   15550 N  N     . ARG   B  1  880  ? 18.529  12.215  85.457  1.00 18.98 ? 878  ARG   B N     1 
ATOM   15551 C  CA    . ARG   B  1  880  ? 17.812  11.544  86.535  1.00 19.03 ? 878  ARG   B CA    1 
ATOM   15552 C  C     . ARG   B  1  880  ? 16.878  12.567  87.152  1.00 17.45 ? 878  ARG   B C     1 
ATOM   15553 O  O     . ARG   B  1  880  ? 17.290  13.700  87.428  1.00 17.92 ? 878  ARG   B O     1 
ATOM   15554 C  CB    . ARG   B  1  880  ? 18.769  11.047  87.619  1.00 21.48 ? 878  ARG   B CB    1 
ATOM   15555 C  CG    . ARG   B  1  880  ? 19.610  9.840   87.254  1.00 27.93 ? 878  ARG   B CG    1 
ATOM   15556 C  CD    . ARG   B  1  880  ? 20.516  9.451   88.426  1.00 31.66 ? 878  ARG   B CD    1 
ATOM   15557 N  NE    . ARG   B  1  880  ? 21.498  8.443   88.046  1.00 48.36 ? 878  ARG   B NE    1 
ATOM   15558 C  CZ    . ARG   B  1  880  ? 21.394  7.153   88.331  1.00 52.55 ? 878  ARG   B CZ    1 
ATOM   15559 N  NH1   . ARG   B  1  880  ? 20.381  6.682   89.041  1.00 52.66 ? 878  ARG   B NH1   1 
ATOM   15560 N  NH2   . ARG   B  1  880  ? 22.328  6.314   87.890  1.00 48.93 ? 878  ARG   B NH2   1 
ATOM   15561 N  N     . LEU   B  1  881  ? 15.625  12.161  87.381  1.00 17.07 ? 879  LEU   B N     1 
ATOM   15562 C  CA    . LEU   B  1  881  ? 14.655  13.063  87.994  1.00 16.99 ? 879  LEU   B CA    1 
ATOM   15563 C  C     . LEU   B  1  881  ? 15.117  13.544  89.368  1.00 16.93 ? 879  LEU   B C     1 
ATOM   15564 O  O     . LEU   B  1  881  ? 14.798  14.670  89.781  1.00 16.99 ? 879  LEU   B O     1 
ATOM   15565 C  CB    . LEU   B  1  881  ? 13.310  12.353  88.102  1.00 16.96 ? 879  LEU   B CB    1 
ATOM   15566 C  CG    . LEU   B  1  881  ? 12.141  13.146  88.679  1.00 18.59 ? 879  LEU   B CG    1 
ATOM   15567 C  CD1   . LEU   B  1  881  ? 11.737  14.251  87.739  1.00 21.81 ? 879  LEU   B CD1   1 
ATOM   15568 C  CD2   . LEU   B  1  881  ? 10.993  12.190  88.950  1.00 19.60 ? 879  LEU   B CD2   1 
ATOM   15569 N  N     . SER   B  1  882  ? 15.896  12.733  90.072  1.00 16.03 ? 880  SER   B N     1 
ATOM   15570 C  CA    . SER   B  1  882  ? 16.352  13.101  91.403  1.00 16.33 ? 880  SER   B CA    1 
ATOM   15571 C  C     . SER   B  1  882  ? 17.441  14.168  91.402  1.00 16.74 ? 880  SER   B C     1 
ATOM   15572 O  O     . SER   B  1  882  ? 17.860  14.592  92.481  1.00 17.67 ? 880  SER   B O     1 
ATOM   15573 C  CB    . SER   B  1  882  ? 16.876  11.858  92.115  1.00 16.92 ? 880  SER   B CB    1 
ATOM   15574 O  OG    . SER   B  1  882  ? 18.089  11.450  91.507  1.00 20.82 ? 880  SER   B OG    1 
ATOM   15575 N  N     . VAL   B  1  883  ? 17.927  14.619  90.255  1.00 16.38 ? 881  VAL   B N     1 
ATOM   15576 C  CA    . VAL   B  1  883  ? 18.982  15.625  90.225  1.00 16.76 ? 881  VAL   B CA    1 
ATOM   15577 C  C     . VAL   B  1  883  ? 18.380  17.017  90.301  1.00 17.86 ? 881  VAL   B C     1 
ATOM   15578 O  O     . VAL   B  1  883  ? 17.458  17.353  89.557  1.00 19.68 ? 881  VAL   B O     1 
ATOM   15579 C  CB    . VAL   B  1  883  ? 19.878  15.464  88.991  1.00 18.68 ? 881  VAL   B CB    1 
ATOM   15580 C  CG1   . VAL   B  1  883  ? 20.809  16.664  88.868  1.00 18.68 ? 881  VAL   B CG1   1 
ATOM   15581 C  CG2   . VAL   B  1  883  ? 20.682  14.194  89.127  1.00 20.61 ? 881  VAL   B CG2   1 
ATOM   15582 N  N     . ASP   B  1  884  ? 18.896  17.823  91.212  1.00 16.30 ? 882  ASP   B N     1 
ATOM   15583 C  CA    . ASP   B  1  884  ? 18.429  19.181  91.418  1.00 16.74 ? 882  ASP   B CA    1 
ATOM   15584 C  C     . ASP   B  1  884  ? 19.279  20.219  90.711  1.00 19.39 ? 882  ASP   B C     1 
ATOM   15585 O  O     . ASP   B  1  884  ? 18.732  21.179  90.166  1.00 23.73 ? 882  ASP   B O     1 
ATOM   15586 C  CB    . ASP   B  1  884  ? 18.448  19.478  92.912  1.00 18.14 ? 882  ASP   B CB    1 
ATOM   15587 C  CG    . ASP   B  1  884  ? 17.591  18.510  93.690  1.00 17.31 ? 882  ASP   B CG    1 
ATOM   15588 O  OD1   . ASP   B  1  884  ? 16.389  18.390  93.355  1.00 18.26 ? 882  ASP   B OD1   1 
ATOM   15589 O  OD2   . ASP   B  1  884  ? 18.123  17.849  94.603  1.00 17.37 ? 882  ASP   B OD2   1 
ATOM   15590 N  N     . VAL   B  1  885  ? 20.596  20.048  90.732  1.00 16.98 ? 883  VAL   B N     1 
ATOM   15591 C  CA    . VAL   B  1  885  ? 21.546  21.028  90.218  1.00 16.78 ? 883  VAL   B CA    1 
ATOM   15592 C  C     . VAL   B  1  885  ? 22.413  20.304  89.198  1.00 15.50 ? 883  VAL   B C     1 
ATOM   15593 O  O     . VAL   B  1  885  ? 23.098  19.322  89.531  1.00 16.81 ? 883  VAL   B O     1 
ATOM   15594 C  CB    . VAL   B  1  885  ? 22.409  21.637  91.339  1.00 17.44 ? 883  VAL   B CB    1 
ATOM   15595 C  CG1   . VAL   B  1  885  ? 23.434  22.611  90.770  1.00 19.56 ? 883  VAL   B CG1   1 
ATOM   15596 C  CG2   . VAL   B  1  885  ? 21.526  22.348  92.378  1.00 22.48 ? 883  VAL   B CG2   1 
ATOM   15597 N  N     . GLY   B  1  886  ? 22.400  20.801  87.971  1.00 16.09 ? 884  GLY   B N     1 
ATOM   15598 C  CA    . GLY   B  1  886  ? 23.212  20.262  86.912  1.00 15.63 ? 884  GLY   B CA    1 
ATOM   15599 C  C     . GLY   B  1  886  ? 24.554  20.945  86.793  1.00 15.30 ? 884  GLY   B C     1 
ATOM   15600 O  O     . GLY   B  1  886  ? 24.976  21.732  87.646  1.00 15.67 ? 884  GLY   B O     1 
ATOM   15601 N  N     . PRO   B  1  887  ? 25.246  20.641  85.703  1.00 15.83 ? 885  PRO   B N     1 
ATOM   15602 C  CA    . PRO   B  1  887  ? 26.600  21.144  85.489  1.00 15.39 ? 885  PRO   B CA    1 
ATOM   15603 C  C     . PRO   B  1  887  ? 26.607  22.582  85.006  1.00 13.91 ? 885  PRO   B C     1 
ATOM   15604 O  O     . PRO   B  1  887  ? 25.615  23.126  84.519  1.00 15.46 ? 885  PRO   B O     1 
ATOM   15605 C  CB    . PRO   B  1  887  ? 27.106  20.233  84.368  1.00 15.46 ? 885  PRO   B CB    1 
ATOM   15606 C  CG    . PRO   B  1  887  ? 25.851  19.937  83.572  1.00 16.12 ? 885  PRO   B CG    1 
ATOM   15607 C  CD    . PRO   B  1  887  ? 24.789  19.756  84.619  1.00 15.96 ? 885  PRO   B CD    1 
ATOM   15608 N  N     . VAL   B  1  888  ? 27.784  23.178  85.098  1.00 15.03 ? 886  VAL   B N     1 
ATOM   15609 C  CA    . VAL   B  1  888  ? 28.030  24.391  84.344  1.00 15.75 ? 886  VAL   B CA    1 
ATOM   15610 C  C     . VAL   B  1  888  ? 28.393  24.008  82.912  1.00 14.88 ? 886  VAL   B C     1 
ATOM   15611 O  O     . VAL   B  1  888  ? 28.839  22.891  82.627  1.00 15.60 ? 886  VAL   B O     1 
ATOM   15612 C  CB    . VAL   B  1  888  ? 29.097  25.281  85.007  1.00 18.03 ? 886  VAL   B CB    1 
ATOM   15613 C  CG1   . VAL   B  1  888  ? 28.634  25.682  86.428  1.00 18.50 ? 886  VAL   B CG1   1 
ATOM   15614 C  CG2   . VAL   B  1  888  ? 30.418  24.603  85.045  1.00 24.91 ? 886  VAL   B CG2   1 
ATOM   15615 N  N     . ILE   B  1  889  ? 28.167  24.943  81.993  1.00 14.83 ? 887  ILE   B N     1 
ATOM   15616 C  CA    . ILE   B  1  889  ? 28.078  24.555  80.587  1.00 15.30 ? 887  ILE   B CA    1 
ATOM   15617 C  C     . ILE   B  1  889  ? 29.420  24.098  80.021  1.00 17.02 ? 887  ILE   B C     1 
ATOM   15618 O  O     . ILE   B  1  889  ? 29.466  23.203  79.176  1.00 16.17 ? 887  ILE   B O     1 
ATOM   15619 C  CB    . ILE   B  1  889  ? 27.439  25.673  79.751  1.00 15.35 ? 887  ILE   B CB    1 
ATOM   15620 C  CG1   . ILE   B  1  889  ? 27.191  25.189  78.312  1.00 16.31 ? 887  ILE   B CG1   1 
ATOM   15621 C  CG2   . ILE   B  1  889  ? 28.288  26.928  79.760  1.00 17.96 ? 887  ILE   B CG2   1 
ATOM   15622 C  CD1   . ILE   B  1  889  ? 26.236  24.014  78.197  1.00 16.83 ? 887  ILE   B CD1   1 
ATOM   15623 N  N     . THR   B  1  890  ? 30.524  24.706  80.439  1.00 14.73 ? 888  THR   B N     1 
ATOM   15624 C  CA    . THR   B  1  890  ? 31.816  24.362  79.859  1.00 16.77 ? 888  THR   B CA    1 
ATOM   15625 C  C     . THR   B  1  890  ? 32.889  24.475  80.916  1.00 16.40 ? 888  THR   B C     1 
ATOM   15626 O  O     . THR   B  1  890  ? 32.700  25.077  81.975  1.00 16.70 ? 888  THR   B O     1 
ATOM   15627 C  CB    . THR   B  1  890  ? 32.256  25.328  78.749  1.00 17.26 ? 888  THR   B CB    1 
ATOM   15628 O  OG1   . THR   B  1  890  ? 32.284  26.665  79.270  1.00 18.67 ? 888  THR   B OG1   1 
ATOM   15629 C  CG2   . THR   B  1  890  ? 31.326  25.238  77.525  1.00 18.96 ? 888  THR   B CG2   1 
ATOM   15630 N  N     . SER   B  1  891  ? 34.047  23.915  80.584  1.00 16.89 ? 889  SER   B N     1 
ATOM   15631 C  CA    A SER   B  1  891  ? 35.212  24.066  81.447  0.30 17.16 ? 889  SER   B CA    1 
ATOM   15632 C  CA    B SER   B  1  891  ? 35.198  24.066  81.463  0.40 17.14 ? 889  SER   B CA    1 
ATOM   15633 C  CA    C SER   B  1  891  ? 35.214  24.063  81.445  0.30 17.16 ? 889  SER   B CA    1 
ATOM   15634 C  C     . SER   B  1  891  ? 35.618  25.528  81.558  1.00 17.58 ? 889  SER   B C     1 
ATOM   15635 O  O     . SER   B  1  891  ? 36.035  25.987  82.627  1.00 18.48 ? 889  SER   B O     1 
ATOM   15636 C  CB    A SER   B  1  891  ? 36.370  23.233  80.902  0.30 19.38 ? 889  SER   B CB    1 
ATOM   15637 C  CB    B SER   B  1  891  ? 36.349  23.184  80.984  0.40 19.40 ? 889  SER   B CB    1 
ATOM   15638 C  CB    C SER   B  1  891  ? 36.363  23.227  80.883  0.30 19.38 ? 889  SER   B CB    1 
ATOM   15639 O  OG    A SER   B  1  891  ? 36.066  21.853  80.949  0.30 19.99 ? 889  SER   B OG    1 
ATOM   15640 O  OG    B SER   B  1  891  ? 36.858  23.639  79.750  0.40 20.46 ? 889  SER   B OG    1 
ATOM   15641 O  OG    C SER   B  1  891  ? 37.490  23.263  81.737  0.30 20.47 ? 889  SER   B OG    1 
ATOM   15642 N  N     . GLU   B  1  892  ? 35.503  26.278  80.457  1.00 16.90 ? 890  GLU   B N     1 
ATOM   15643 C  CA    . GLU   B  1  892  ? 35.840  27.695  80.504  1.00 18.86 ? 890  GLU   B CA    1 
ATOM   15644 C  C     . GLU   B  1  892  ? 34.932  28.432  81.473  1.00 17.87 ? 890  GLU   B C     1 
ATOM   15645 O  O     . GLU   B  1  892  ? 35.400  29.268  82.254  1.00 19.82 ? 890  GLU   B O     1 
ATOM   15646 C  CB    . GLU   B  1  892  ? 35.732  28.323  79.111  1.00 21.34 ? 890  GLU   B CB    1 
ATOM   15647 N  N     . ALA   B  1  893  ? 33.629  28.137  81.435  1.00 17.22 ? 891  ALA   B N     1 
ATOM   15648 C  CA    . ALA   B  1  893  ? 32.709  28.764  82.376  1.00 16.90 ? 891  ALA   B CA    1 
ATOM   15649 C  C     . ALA   B  1  893  ? 33.065  28.382  83.803  1.00 17.20 ? 891  ALA   B C     1 
ATOM   15650 O  O     . ALA   B  1  893  ? 33.109  29.236  84.696  1.00 18.02 ? 891  ALA   B O     1 
ATOM   15651 C  CB    . ALA   B  1  893  ? 31.269  28.364  82.053  1.00 18.79 ? 891  ALA   B CB    1 
ATOM   15652 N  N     . LYS   B  1  894  ? 33.325  27.100  84.033  1.00 16.62 ? 892  LYS   B N     1 
ATOM   15653 C  CA    . LYS   B  1  894  ? 33.734  26.645  85.354  1.00 18.69 ? 892  LYS   B CA    1 
ATOM   15654 C  C     . LYS   B  1  894  ? 34.967  27.400  85.835  1.00 18.09 ? 892  LYS   B C     1 
ATOM   15655 O  O     . LYS   B  1  894  ? 35.012  27.875  86.974  1.00 17.70 ? 892  LYS   B O     1 
ATOM   15656 C  CB    . LYS   B  1  894  ? 34.001  25.146  85.318  1.00 16.66 ? 892  LYS   B CB    1 
ATOM   15657 C  CG    . LYS   B  1  894  ? 34.499  24.570  86.623  1.00 17.66 ? 892  LYS   B CG    1 
ATOM   15658 C  CD    . LYS   B  1  894  ? 34.588  23.058  86.494  1.00 21.37 ? 892  LYS   B CD    1 
ATOM   15659 C  CE    . LYS   B  1  894  ? 35.444  22.433  87.580  1.00 28.35 ? 892  LYS   B CE    1 
ATOM   15660 N  NZ    . LYS   B  1  894  ? 34.771  22.399  88.890  1.00 39.12 ? 892  LYS   B NZ    1 
ATOM   15661 N  N     . ASP   B  1  895  ? 35.974  27.538  84.973  1.00 17.67 ? 893  ASP   B N     1 
ATOM   15662 C  CA    . ASP   B  1  895  ? 37.184  28.258  85.367  1.00 17.91 ? 893  ASP   B CA    1 
ATOM   15663 C  C     . ASP   B  1  895  ? 36.891  29.715  85.694  1.00 17.25 ? 893  ASP   B C     1 
ATOM   15664 O  O     . ASP   B  1  895  ? 37.487  30.284  86.610  1.00 19.48 ? 893  ASP   B O     1 
ATOM   15665 C  CB    . ASP   B  1  895  ? 38.214  28.195  84.246  1.00 19.37 ? 893  ASP   B CB    1 
ATOM   15666 C  CG    . ASP   B  1  895  ? 38.794  26.826  84.076  1.00 22.58 ? 893  ASP   B CG    1 
ATOM   15667 O  OD1   . ASP   B  1  895  ? 38.687  26.014  85.014  1.00 25.60 ? 893  ASP   B OD1   1 
ATOM   15668 O  OD2   . ASP   B  1  895  ? 39.382  26.573  83.001  1.00 25.47 ? 893  ASP   B OD2   1 
ATOM   15669 N  N     . ASN   B  1  896  ? 36.002  30.342  84.931  1.00 17.26 ? 894  ASN   B N     1 
ATOM   15670 C  CA    . ASN   B  1  896  ? 35.663  31.742  85.155  1.00 18.36 ? 894  ASN   B CA    1 
ATOM   15671 C  C     . ASN   B  1  896  ? 34.982  31.912  86.510  1.00 19.96 ? 894  ASN   B C     1 
ATOM   15672 O  O     . ASN   B  1  896  ? 35.310  32.823  87.285  1.00 18.84 ? 894  ASN   B O     1 
ATOM   15673 C  CB    . ASN   B  1  896  ? 34.750  32.168  84.004  1.00 20.55 ? 894  ASN   B CB    1 
ATOM   15674 C  CG    . ASN   B  1  896  ? 34.307  33.599  84.083  1.00 28.23 ? 894  ASN   B CG    1 
ATOM   15675 O  OD1   . ASN   B  1  896  ? 33.616  33.997  85.009  1.00 28.23 ? 894  ASN   B OD1   1 
ATOM   15676 N  ND2   . ASN   B  1  896  ? 34.639  34.370  83.056  1.00 36.01 ? 894  ASN   B ND2   1 
ATOM   15677 N  N     . ILE   B  1  897  ? 34.047  31.018  86.818  1.00 17.61 ? 895  ILE   B N     1 
ATOM   15678 C  CA    . ILE   B  1  897  ? 33.356  31.060  88.098  1.00 16.81 ? 895  ILE   B CA    1 
ATOM   15679 C  C     . ILE   B  1  897  ? 34.346  30.810  89.221  1.00 17.43 ? 895  ILE   B C     1 
ATOM   15680 O  O     . ILE   B  1  897  ? 34.365  31.516  90.238  1.00 17.83 ? 895  ILE   B O     1 
ATOM   15681 C  CB    . ILE   B  1  897  ? 32.237  30.007  88.106  1.00 16.93 ? 895  ILE   B CB    1 
ATOM   15682 C  CG1   . ILE   B  1  897  ? 31.182  30.330  87.047  1.00 16.13 ? 895  ILE   B CG1   1 
ATOM   15683 C  CG2   . ILE   B  1  897  ? 31.625  29.890  89.516  1.00 18.59 ? 895  ILE   B CG2   1 
ATOM   15684 C  CD1   . ILE   B  1  897  ? 30.378  29.117  86.623  1.00 17.20 ? 895  ILE   B CD1   1 
ATOM   15685 N  N     . GLU   B  1  898  ? 35.183  29.795  89.053  1.00 17.63 ? 896  GLU   B N     1 
ATOM   15686 C  CA    . GLU   B  1  898  ? 36.134  29.458  90.103  1.00 16.75 ? 896  GLU   B CA    1 
ATOM   15687 C  C     . GLU   B  1  898  ? 37.154  30.561  90.315  1.00 18.05 ? 896  GLU   B C     1 
ATOM   15688 O  O     . GLU   B  1  898  ? 37.594  30.777  91.452  1.00 17.81 ? 896  GLU   B O     1 
ATOM   15689 C  CB    . GLU   B  1  898  ? 36.791  28.114  89.809  1.00 20.74 ? 896  GLU   B CB    1 
ATOM   15690 C  CG    . GLU   B  1  898  ? 35.809  26.974  90.040  1.00 21.46 ? 896  GLU   B CG    1 
ATOM   15691 C  CD    . GLU   B  1  898  ? 36.381  25.613  89.721  1.00 30.25 ? 896  GLU   B CD    1 
ATOM   15692 O  OE1   . GLU   B  1  898  ? 37.474  25.551  89.132  1.00 31.72 ? 896  GLU   B OE1   1 
ATOM   15693 O  OE2   . GLU   B  1  898  ? 35.725  24.607  90.061  1.00 37.32 ? 896  GLU   B OE2   1 
ATOM   15694 N  N     . LYS   B  1  899  ? 37.529  31.284  89.257  1.00 18.25 ? 897  LYS   B N     1 
ATOM   15695 C  CA    . LYS   B  1  899  ? 38.443  32.403  89.438  1.00 19.12 ? 897  LYS   B CA    1 
ATOM   15696 C  C     . LYS   B  1  899  ? 37.823  33.452  90.346  1.00 17.01 ? 897  LYS   B C     1 
ATOM   15697 O  O     . LYS   B  1  899  ? 38.501  34.025  91.208  1.00 18.11 ? 897  LYS   B O     1 
ATOM   15698 C  CB    . LYS   B  1  899  ? 38.810  33.013  88.085  1.00 20.68 ? 897  LYS   B CB    1 
ATOM   15699 C  CG    . LYS   B  1  899  ? 39.770  34.176  88.206  1.00 23.23 ? 897  LYS   B CG    1 
ATOM   15700 C  CD    . LYS   B  1  899  ? 40.293  34.601  86.848  1.00 31.35 ? 897  LYS   B CD    1 
ATOM   15701 C  CE    . LYS   B  1  899  ? 39.386  35.608  86.187  1.00 30.15 ? 897  LYS   B CE    1 
ATOM   15702 N  NZ    . LYS   B  1  899  ? 40.089  36.338  85.085  1.00 30.85 ? 897  LYS   B NZ    1 
ATOM   15703 N  N     . HIS   B  1  900  ? 36.530  33.699  90.186  1.00 17.61 ? 898  HIS   B N     1 
ATOM   15704 C  CA    . HIS   B  1  900  ? 35.868  34.656  91.055  1.00 17.85 ? 898  HIS   B CA    1 
ATOM   15705 C  C     . HIS   B  1  900  ? 35.836  34.142  92.485  1.00 18.01 ? 898  HIS   B C     1 
ATOM   15706 O  O     . HIS   B  1  900  ? 36.117  34.887  93.428  1.00 17.70 ? 898  HIS   B O     1 
ATOM   15707 C  CB    . HIS   B  1  900  ? 34.452  34.897  90.569  1.00 15.76 ? 898  HIS   B CB    1 
ATOM   15708 C  CG    . HIS   B  1  900  ? 33.621  35.635  91.559  1.00 17.11 ? 898  HIS   B CG    1 
ATOM   15709 N  ND1   . HIS   B  1  900  ? 33.801  36.972  91.814  1.00 21.18 ? 898  HIS   B ND1   1 
ATOM   15710 C  CD2   . HIS   B  1  900  ? 32.609  35.225  92.363  1.00 17.73 ? 898  HIS   B CD2   1 
ATOM   15711 C  CE1   . HIS   B  1  900  ? 32.932  37.360  92.732  1.00 19.84 ? 898  HIS   B CE1   1 
ATOM   15712 N  NE2   . HIS   B  1  900  ? 32.201  36.319  93.083  1.00 18.58 ? 898  HIS   B NE2   1 
ATOM   15713 N  N     . ILE   B  1  901  ? 35.475  32.873  92.662  1.00 17.26 ? 899  ILE   B N     1 
ATOM   15714 C  CA    . ILE   B  1  901  ? 35.395  32.312  94.005  1.00 17.85 ? 899  ILE   B CA    1 
ATOM   15715 C  C     . ILE   B  1  901  ? 36.744  32.405  94.697  1.00 19.02 ? 899  ILE   B C     1 
ATOM   15716 O  O     . ILE   B  1  901  ? 36.838  32.811  95.862  1.00 19.68 ? 899  ILE   B O     1 
ATOM   15717 C  CB    . ILE   B  1  901  ? 34.881  30.866  93.939  1.00 16.98 ? 899  ILE   B CB    1 
ATOM   15718 C  CG1   . ILE   B  1  901  ? 33.447  30.837  93.416  1.00 16.81 ? 899  ILE   B CG1   1 
ATOM   15719 C  CG2   . ILE   B  1  901  ? 34.993  30.203  95.292  1.00 19.37 ? 899  ILE   B CG2   1 
ATOM   15720 C  CD1   . ILE   B  1  901  ? 32.964  29.423  93.119  1.00 19.43 ? 899  ILE   B CD1   1 
ATOM   15721 N  N     . GLU   B  1  902  ? 37.814  32.069  93.980  1.00 19.64 ? 900  GLU   B N     1 
ATOM   15722 C  CA    . GLU   B  1  902  ? 39.138  32.102  94.584  1.00 20.19 ? 900  GLU   B CA    1 
ATOM   15723 C  C     . GLU   B  1  902  ? 39.602  33.530  94.812  1.00 19.98 ? 900  GLU   B C     1 
ATOM   15724 O  O     . GLU   B  1  902  ? 40.360  33.784  95.755  1.00 21.16 ? 900  GLU   B O     1 
ATOM   15725 C  CB    . GLU   B  1  902  ? 40.124  31.310  93.725  1.00 20.90 ? 900  GLU   B CB    1 
ATOM   15726 C  CG    . GLU   B  1  902  ? 39.815  29.815  93.678  1.00 28.97 ? 900  GLU   B CG    1 
ATOM   15727 C  CD    . GLU   B  1  902  ? 39.558  29.207  95.061  1.00 30.80 ? 900  GLU   B CD    1 
ATOM   15728 O  OE1   . GLU   B  1  902  ? 40.415  29.376  95.959  1.00 32.05 ? 900  GLU   B OE1   1 
ATOM   15729 O  OE2   . GLU   B  1  902  ? 38.496  28.567  95.245  1.00 33.06 ? 900  GLU   B OE2   1 
ATOM   15730 N  N     . ARG   B  1  903  ? 39.176  34.474  93.975  1.00 21.26 ? 901  ARG   B N     1 
ATOM   15731 C  CA    . ARG   B  1  903  ? 39.506  35.866  94.249  1.00 21.84 ? 901  ARG   B CA    1 
ATOM   15732 C  C     . ARG   B  1  903  ? 38.843  36.329  95.537  1.00 21.08 ? 901  ARG   B C     1 
ATOM   15733 O  O     . ARG   B  1  903  ? 39.479  36.987  96.368  1.00 22.67 ? 901  ARG   B O     1 
ATOM   15734 C  CB    . ARG   B  1  903  ? 39.088  36.757  93.080  1.00 23.41 ? 901  ARG   B CB    1 
ATOM   15735 C  CG    . ARG   B  1  903  ? 39.467  38.215  93.283  1.00 30.81 ? 901  ARG   B CG    1 
ATOM   15736 C  CD    . ARG   B  1  903  ? 39.100  39.066  92.085  1.00 37.97 ? 901  ARG   B CD    1 
ATOM   15737 N  NE    . ARG   B  1  903  ? 37.729  39.558  92.137  1.00 43.10 ? 901  ARG   B NE    1 
ATOM   15738 C  CZ    . ARG   B  1  903  ? 37.371  40.725  92.657  1.00 41.10 ? 901  ARG   B CZ    1 
ATOM   15739 N  NH1   . ARG   B  1  903  ? 38.254  41.529  93.221  1.00 45.61 ? 901  ARG   B NH1   1 
ATOM   15740 N  NH2   . ARG   B  1  903  ? 36.092  41.093  92.608  1.00 43.24 ? 901  ARG   B NH2   1 
ATOM   15741 N  N     . MET   B  1  904  ? 37.571  35.981  95.726  1.00 20.93 ? 902  MET   B N     1 
ATOM   15742 C  CA    . MET   B  1  904  ? 36.891  36.332  96.965  1.00 19.37 ? 902  MET   B CA    1 
ATOM   15743 C  C     . MET   B  1  904  ? 37.546  35.656  98.155  1.00 23.52 ? 902  MET   B C     1 
ATOM   15744 O  O     . MET   B  1  904  ? 37.736  36.282  99.206  1.00 23.41 ? 902  MET   B O     1 
ATOM   15745 C  CB    . MET   B  1  904  ? 35.425  35.927  96.877  1.00 20.77 ? 902  MET   B CB    1 
ATOM   15746 C  CG    . MET   B  1  904  ? 34.682  36.616  95.764  1.00 20.91 ? 902  MET   B CG    1 
ATOM   15747 S  SD    . MET   B  1  904  ? 34.515  38.373  96.132  1.00 30.20 ? 902  MET   B SD    1 
ATOM   15748 C  CE    . MET   B  1  904  ? 35.713  39.042  94.997  1.00 30.59 ? 902  MET   B CE    1 
ATOM   15749 N  N     . ARG   B  1  905  ? 37.890  34.377  98.014  1.00 20.70 ? 903  ARG   B N     1 
ATOM   15750 C  CA    . ARG   B  1  905  ? 38.539  33.673  99.112  1.00 24.97 ? 903  ARG   B CA    1 
ATOM   15751 C  C     . ARG   B  1  905  ? 39.867  34.329  99.457  1.00 24.47 ? 903  ARG   B C     1 
ATOM   15752 O  O     . ARG   B  1  905  ? 40.180  34.536  100.637 1.00 25.12 ? 903  ARG   B O     1 
ATOM   15753 C  CB    . ARG   B  1  905  ? 38.729  32.203  98.742  1.00 24.66 ? 903  ARG   B CB    1 
ATOM   15754 C  CG    . ARG   B  1  905  ? 38.920  31.285  99.925  1.00 30.65 ? 903  ARG   B CG    1 
ATOM   15755 C  CD    . ARG   B  1  905  ? 39.358  29.907  99.465  1.00 33.55 ? 903  ARG   B CD    1 
ATOM   15756 N  NE    . ARG   B  1  905  ? 38.500  29.340  98.431  1.00 30.96 ? 903  ARG   B NE    1 
ATOM   15757 C  CZ    . ARG   B  1  905  ? 37.419  28.606  98.666  1.00 28.09 ? 903  ARG   B CZ    1 
ATOM   15758 N  NH1   . ARG   B  1  905  ? 36.951  28.435  99.892  1.00 32.61 ? 903  ARG   B NH1   1 
ATOM   15759 N  NH2   . ARG   B  1  905  ? 36.802  28.016  97.647  1.00 30.06 ? 903  ARG   B NH2   1 
ATOM   15760 N  N     . GLY   B  1  906  ? 40.641  34.712  98.442  1.00 22.97 ? 904  GLY   B N     1 
ATOM   15761 C  CA    . GLY   B  1  906  ? 41.942  35.310  98.694  1.00 24.42 ? 904  GLY   B CA    1 
ATOM   15762 C  C     . GLY   B  1  906  ? 41.868  36.691  99.302  1.00 25.55 ? 904  GLY   B C     1 
ATOM   15763 O  O     . GLY   B  1  906  ? 42.834  37.122  99.942  1.00 31.23 ? 904  GLY   B O     1 
ATOM   15764 N  N     . LEU   B  1  907  ? 40.747  37.388  99.126  1.00 26.34 ? 905  LEU   B N     1 
ATOM   15765 C  CA    . LEU   B  1  907  ? 40.486  38.671  99.765  1.00 29.59 ? 905  LEU   B CA    1 
ATOM   15766 C  C     . LEU   B  1  907  ? 39.973  38.519  101.187 1.00 26.89 ? 905  LEU   B C     1 
ATOM   15767 O  O     . LEU   B  1  907  ? 39.738  39.532  101.853 1.00 29.23 ? 905  LEU   B O     1 
ATOM   15768 C  CB    . LEU   B  1  907  ? 39.479  39.477  98.953  1.00 31.22 ? 905  LEU   B CB    1 
ATOM   15769 C  CG    . LEU   B  1  907  ? 39.931  39.939  97.569  1.00 36.72 ? 905  LEU   B CG    1 
ATOM   15770 C  CD1   . LEU   B  1  907  ? 38.842  40.777  96.930  1.00 38.33 ? 905  LEU   B CD1   1 
ATOM   15771 C  CD2   . LEU   B  1  907  ? 41.237  40.712  97.665  1.00 37.62 ? 905  LEU   B CD2   1 
ATOM   15772 N  N     . GLY   B  1  908  ? 39.795  37.292  101.656 1.00 26.41 ? 906  GLY   B N     1 
ATOM   15773 C  CA    . GLY   B  1  908  ? 39.387  37.047  103.021 1.00 28.37 ? 906  GLY   B CA    1 
ATOM   15774 C  C     . GLY   B  1  908  ? 37.898  36.929  103.232 1.00 29.56 ? 906  GLY   B C     1 
ATOM   15775 O  O     . GLY   B  1  908  ? 37.459  36.834  104.383 1.00 28.14 ? 906  GLY   B O     1 
ATOM   15776 N  N     . ARG   B  1  909  ? 37.106  36.927  102.165 1.00 23.01 ? 907  ARG   B N     1 
ATOM   15777 C  CA    . ARG   B  1  909  ? 35.672  36.774  102.325 1.00 22.90 ? 907  ARG   B CA    1 
ATOM   15778 C  C     . ARG   B  1  909  ? 35.344  35.352  102.744 1.00 22.44 ? 907  ARG   B C     1 
ATOM   15779 O  O     . ARG   B  1  909  ? 36.013  34.389  102.355 1.00 26.59 ? 907  ARG   B O     1 
ATOM   15780 C  CB    . ARG   B  1  909  ? 34.961  37.055  101.007 1.00 23.22 ? 907  ARG   B CB    1 
ATOM   15781 C  CG    . ARG   B  1  909  ? 35.381  38.345  100.355 1.00 30.02 ? 907  ARG   B CG    1 
ATOM   15782 C  CD    . ARG   B  1  909  ? 34.913  39.552  101.132 1.00 38.46 ? 907  ARG   B CD    1 
ATOM   15783 N  NE    . ARG   B  1  909  ? 35.602  40.755  100.678 1.00 46.21 ? 907  ARG   B NE    1 
ATOM   15784 C  CZ    . ARG   B  1  909  ? 35.177  41.989  100.902 1.00 52.01 ? 907  ARG   B CZ    1 
ATOM   15785 N  NH1   . ARG   B  1  909  ? 34.038  42.222  101.535 1.00 49.16 ? 907  ARG   B NH1   1 
ATOM   15786 N  NH2   . ARG   B  1  909  ? 35.906  43.016  100.473 1.00 52.93 ? 907  ARG   B NH2   1 
ATOM   15787 N  N     . LYS   B  1  910  ? 34.280  35.216  103.516 1.00 20.83 ? 908  LYS   B N     1 
ATOM   15788 C  CA    . LYS   B  1  910  ? 33.828  33.888  103.890 1.00 22.26 ? 908  LYS   B CA    1 
ATOM   15789 C  C     . LYS   B  1  910  ? 33.192  33.223  102.675 1.00 21.74 ? 908  LYS   B C     1 
ATOM   15790 O  O     . LYS   B  1  910  ? 32.238  33.750  102.091 1.00 20.22 ? 908  LYS   B O     1 
ATOM   15791 C  CB    . LYS   B  1  910  ? 32.833  33.976  105.042 1.00 24.46 ? 908  LYS   B CB    1 
ATOM   15792 C  CG    . LYS   B  1  910  ? 32.391  32.615  105.560 1.00 26.75 ? 908  LYS   B CG    1 
ATOM   15793 C  CD    . LYS   B  1  910  ? 31.355  32.745  106.665 1.00 34.45 ? 908  LYS   B CD    1 
ATOM   15794 C  CE    . LYS   B  1  910  ? 31.059  31.388  107.289 1.00 43.75 ? 908  LYS   B CE    1 
ATOM   15795 N  NZ    . LYS   B  1  910  ? 29.794  31.385  108.074 1.00 46.93 ? 908  LYS   B NZ    1 
ATOM   15796 N  N     . VAL   B  1  911  ? 33.732  32.078  102.284 1.00 19.43 ? 909  VAL   B N     1 
ATOM   15797 C  CA    . VAL   B  1  911  ? 33.268  31.308  101.140 1.00 18.87 ? 909  VAL   B CA    1 
ATOM   15798 C  C     . VAL   B  1  911  ? 32.904  29.923  101.643 1.00 20.42 ? 909  VAL   B C     1 
ATOM   15799 O  O     . VAL   B  1  911  ? 33.720  29.262  102.301 1.00 21.94 ? 909  VAL   B O     1 
ATOM   15800 C  CB    . VAL   B  1  911  ? 34.362  31.209  100.065 1.00 18.93 ? 909  VAL   B CB    1 
ATOM   15801 C  CG1   . VAL   B  1  911  ? 33.949  30.246  98.962  1.00 20.06 ? 909  VAL   B CG1   1 
ATOM   15802 C  CG2   . VAL   B  1  911  ? 34.718  32.599  99.525  1.00 20.03 ? 909  VAL   B CG2   1 
ATOM   15803 N  N     . GLU   B  1  912  ? 31.687  29.487  101.350 1.00 17.59 ? 910  GLU   B N     1 
ATOM   15804 C  CA    . GLU   B  1  912  ? 31.237  28.155  101.720 1.00 18.97 ? 910  GLU   B CA    1 
ATOM   15805 C  C     . GLU   B  1  912  ? 30.676  27.461  100.492 1.00 19.32 ? 910  GLU   B C     1 
ATOM   15806 O  O     . GLU   B  1  912  ? 29.951  28.074  99.705  1.00 19.58 ? 910  GLU   B O     1 
ATOM   15807 C  CB    . GLU   B  1  912  ? 30.168  28.222  102.806 1.00 24.00 ? 910  GLU   B CB    1 
ATOM   15808 C  CG    . GLU   B  1  912  ? 30.686  28.792  104.121 1.00 25.23 ? 910  GLU   B CG    1 
ATOM   15809 C  CD    . GLU   B  1  912  ? 29.575  28.981  105.133 1.00 38.41 ? 910  GLU   B CD    1 
ATOM   15810 O  OE1   . GLU   B  1  912  ? 29.180  27.987  105.777 1.00 42.83 ? 910  GLU   B OE1   1 
ATOM   15811 O  OE2   . GLU   B  1  912  ? 29.085  30.121  105.263 1.00 45.14 ? 910  GLU   B OE2   1 
ATOM   15812 N  N     . GLN   B  1  913  ? 31.012  26.184  100.320 1.00 18.10 ? 911  GLN   B N     1 
ATOM   15813 C  CA    . GLN   B  1  913  ? 30.495  25.403  99.206  1.00 19.69 ? 911  GLN   B CA    1 
ATOM   15814 C  C     . GLN   B  1  913  ? 29.895  24.122  99.740  1.00 22.17 ? 911  GLN   B C     1 
ATOM   15815 O  O     . GLN   B  1  913  ? 30.465  23.483  100.630 1.00 24.92 ? 911  GLN   B O     1 
ATOM   15816 C  CB    . GLN   B  1  913  ? 31.574  25.089  98.179  1.00 22.57 ? 911  GLN   B CB    1 
ATOM   15817 C  CG    . GLN   B  1  913  ? 32.170  26.346  97.590  1.00 21.87 ? 911  GLN   B CG    1 
ATOM   15818 C  CD    . GLN   B  1  913  ? 33.154  26.038  96.499  1.00 26.28 ? 911  GLN   B CD    1 
ATOM   15819 O  OE1   . GLN   B  1  913  ? 34.199  25.444  96.751  1.00 33.89 ? 911  GLN   B OE1   1 
ATOM   15820 N  NE2   . GLN   B  1  913  ? 32.828  26.428  95.277  1.00 22.76 ? 911  GLN   B NE2   1 
ATOM   15821 N  N     . ILE   B  1  914  ? 28.741  23.752  99.195  1.00 21.96 ? 912  ILE   B N     1 
ATOM   15822 C  CA    . ILE   B  1  914  ? 27.945  22.655  99.730  1.00 29.58 ? 912  ILE   B CA    1 
ATOM   15823 C  C     . ILE   B  1  914  ? 27.578  21.733  98.580  1.00 27.47 ? 912  ILE   B C     1 
ATOM   15824 O  O     . ILE   B  1  914  ? 26.894  22.162  97.644  1.00 25.87 ? 912  ILE   B O     1 
ATOM   15825 C  CB    . ILE   B  1  914  ? 26.680  23.173  100.434 1.00 28.65 ? 912  ILE   B CB    1 
ATOM   15826 C  CG1   . ILE   B  1  914  ? 27.063  24.005  101.667 1.00 32.48 ? 912  ILE   B CG1   1 
ATOM   15827 C  CG2   . ILE   B  1  914  ? 25.771  22.013  100.793 1.00 27.72 ? 912  ILE   B CG2   1 
ATOM   15828 C  CD1   . ILE   B  1  914  ? 25.927  24.820  102.259 1.00 28.79 ? 912  ILE   B CD1   1 
ATOM   15829 N  N     . GLY   B  1  915  ? 28.035  20.481  98.647  1.00 32.97 ? 913  GLY   B N     1 
ATOM   15830 C  CA    . GLY   B  1  915  ? 27.819  19.400  97.693  1.00 40.34 ? 913  GLY   B CA    1 
ATOM   15831 C  C     . GLY   B  1  915  ? 29.051  19.127  96.840  1.00 40.81 ? 913  GLY   B C     1 
ATOM   15832 O  O     . GLY   B  1  915  ? 29.821  20.036  96.510  1.00 43.32 ? 913  GLY   B O     1 
ATOM   15833 N  N     . LEU   B  1  916  ? 29.242  17.846  96.461  1.00 53.82 ? 914  LEU   B N     1 
ATOM   15834 C  CA    . LEU   B  1  916  ? 30.426  17.445  95.688  1.00 50.21 ? 914  LEU   B CA    1 
ATOM   15835 C  C     . LEU   B  1  916  ? 30.573  15.946  95.403  1.00 56.55 ? 914  LEU   B C     1 
ATOM   15836 O  O     . LEU   B  1  916  ? 31.501  15.318  95.924  1.00 55.29 ? 914  LEU   B O     1 
ATOM   15837 C  CB    . LEU   B  1  916  ? 31.700  17.877  96.425  1.00 52.72 ? 914  LEU   B CB    1 
ATOM   15838 C  CG    . LEU   B  1  916  ? 32.718  18.692  95.626  1.00 60.33 ? 914  LEU   B CG    1 
ATOM   15839 C  CD1   . LEU   B  1  916  ? 33.435  19.684  96.533  1.00 60.80 ? 914  LEU   B CD1   1 
ATOM   15840 C  CD2   . LEU   B  1  916  ? 33.716  17.775  94.925  1.00 63.62 ? 914  LEU   B CD2   1 
ATOM   15841 N  N     . ALA   B  1  917  ? 29.736  15.365  94.542  1.00 51.43 ? 915  ALA   B N     1 
ATOM   15842 C  CA    . ALA   B  1  917  ? 29.815  13.928  94.277  1.00 50.46 ? 915  ALA   B CA    1 
ATOM   15843 C  C     . ALA   B  1  917  ? 30.987  13.580  93.359  1.00 50.75 ? 915  ALA   B C     1 
ATOM   15844 O  O     . ALA   B  1  917  ? 31.390  14.370  92.501  1.00 45.90 ? 915  ALA   B O     1 
ATOM   15845 C  CB    . ALA   B  1  917  ? 28.515  13.421  93.648  1.00 51.05 ? 915  ALA   B CB    1 
ATOM   15846 N  N     . SER   B  1  918  ? 31.527  12.366  93.538  1.00 49.66 ? 916  SER   B N     1 
ATOM   15847 C  CA    . SER   B  1  918  ? 32.648  11.924  92.707  1.00 48.81 ? 916  SER   B CA    1 
ATOM   15848 C  C     . SER   B  1  918  ? 32.245  11.760  91.245  1.00 47.24 ? 916  SER   B C     1 
ATOM   15849 O  O     . SER   B  1  918  ? 33.063  12.005  90.348  1.00 40.33 ? 916  SER   B O     1 
ATOM   15850 C  CB    . SER   B  1  918  ? 33.237  10.616  93.248  1.00 49.67 ? 916  SER   B CB    1 
ATOM   15851 O  OG    . SER   B  1  918  ? 32.305  9.552   93.156  1.00 57.01 ? 916  SER   B OG    1 
ATOM   15852 N  N     . GLU   B  1  919  ? 30.996  11.360  90.987  1.00 42.14 ? 917  GLU   B N     1 
ATOM   15853 C  CA    . GLU   B  1  919  ? 30.501  11.230  89.623  1.00 41.33 ? 917  GLU   B CA    1 
ATOM   15854 C  C     . GLU   B  1  919  ? 30.538  12.541  88.857  1.00 41.11 ? 917  GLU   B C     1 
ATOM   15855 O  O     . GLU   B  1  919  ? 30.371  12.527  87.633  1.00 35.51 ? 917  GLU   B O     1 
ATOM   15856 C  CB    . GLU   B  1  919  ? 29.065  10.696  89.616  1.00 42.12 ? 917  GLU   B CB    1 
ATOM   15857 C  CG    . GLU   B  1  919  ? 28.927  9.223   89.979  1.00 52.35 ? 917  GLU   B CG    1 
ATOM   15858 C  CD    . GLU   B  1  919  ? 29.119  8.957   91.464  1.00 55.63 ? 917  GLU   B CD    1 
ATOM   15859 O  OE1   . GLU   B  1  919  ? 29.044  9.920   92.260  1.00 51.75 ? 917  GLU   B OE1   1 
ATOM   15860 O  OE2   . GLU   B  1  919  ? 29.344  7.782   91.832  1.00 54.53 ? 917  GLU   B OE2   1 
ATOM   15861 N  N     . THR   B  1  920  ? 30.742  13.669  89.538  1.00 36.06 ? 918  THR   B N     1 
ATOM   15862 C  CA    . THR   B  1  920  ? 30.815  14.937  88.829  1.00 33.07 ? 918  THR   B CA    1 
ATOM   15863 C  C     . THR   B  1  920  ? 32.100  15.080  88.023  1.00 34.72 ? 918  THR   B C     1 
ATOM   15864 O  O     . THR   B  1  920  ? 32.127  15.877  87.082  1.00 31.16 ? 918  THR   B O     1 
ATOM   15865 C  CB    . THR   B  1  920  ? 30.638  16.118  89.797  1.00 36.41 ? 918  THR   B CB    1 
ATOM   15866 O  OG1   . THR   B  1  920  ? 31.641  16.065  90.820  1.00 34.56 ? 918  THR   B OG1   1 
ATOM   15867 C  CG2   . THR   B  1  920  ? 29.239  16.115  90.431  1.00 27.13 ? 918  THR   B CG2   1 
ATOM   15868 N  N     . GLY   B  1  921  ? 33.146  14.309  88.350  1.00 31.29 ? 919  GLY   B N     1 
ATOM   15869 C  CA    . GLY   B  1  921  ? 34.457  14.484  87.731  1.00 33.04 ? 919  GLY   B CA    1 
ATOM   15870 C  C     . GLY   B  1  921  ? 34.475  14.308  86.223  1.00 32.37 ? 919  GLY   B C     1 
ATOM   15871 O  O     . GLY   B  1  921  ? 35.390  14.807  85.561  1.00 35.39 ? 919  GLY   B O     1 
ATOM   15872 N  N     . VAL   B  1  922  ? 33.486  13.604  85.667  1.00 24.32 ? 920  VAL   B N     1 
ATOM   15873 C  CA    . VAL   B  1  922  ? 33.400  13.404  84.223  1.00 22.76 ? 920  VAL   B CA    1 
ATOM   15874 C  C     . VAL   B  1  922  ? 32.748  14.578  83.504  1.00 21.68 ? 920  VAL   B C     1 
ATOM   15875 O  O     . VAL   B  1  922  ? 32.780  14.628  82.264  1.00 21.49 ? 920  VAL   B O     1 
ATOM   15876 C  CB    . VAL   B  1  922  ? 32.650  12.102  83.878  1.00 25.49 ? 920  VAL   B CB    1 
ATOM   15877 C  CG1   . VAL   B  1  922  ? 33.461  10.884  84.317  1.00 26.26 ? 920  VAL   B CG1   1 
ATOM   15878 C  CG2   . VAL   B  1  922  ? 31.267  12.089  84.517  1.00 22.99 ? 920  VAL   B CG2   1 
ATOM   15879 N  N     . GLY   B  1  923  ? 32.154  15.511  84.236  1.00 19.75 ? 921  GLY   B N     1 
ATOM   15880 C  CA    . GLY   B  1  923  ? 31.575  16.701  83.647  1.00 19.09 ? 921  GLY   B CA    1 
ATOM   15881 C  C     . GLY   B  1  923  ? 32.136  17.944  84.300  1.00 19.71 ? 921  GLY   B C     1 
ATOM   15882 O  O     . GLY   B  1  923  ? 33.123  17.864  85.046  1.00 21.46 ? 921  GLY   B O     1 
ATOM   15883 N  N     . THR   B  1  924  ? 31.515  19.089  84.074  1.00 16.80 ? 922  THR   B N     1 
ATOM   15884 C  CA    . THR   B  1  924  ? 31.997  20.360  84.610  1.00 16.94 ? 922  THR   B CA    1 
ATOM   15885 C  C     . THR   B  1  924  ? 30.961  20.878  85.593  1.00 16.52 ? 922  THR   B C     1 
ATOM   15886 O  O     . THR   B  1  924  ? 29.919  21.393  85.187  1.00 18.44 ? 922  THR   B O     1 
ATOM   15887 C  CB    . THR   B  1  924  ? 32.255  21.373  83.497  1.00 15.55 ? 922  THR   B CB    1 
ATOM   15888 O  OG1   . THR   B  1  924  ? 31.124  21.425  82.632  1.00 17.89 ? 922  THR   B OG1   1 
ATOM   15889 C  CG2   . THR   B  1  924  ? 33.466  20.966  82.669  1.00 20.05 ? 922  THR   B CG2   1 
ATOM   15890 N  N     . PHE   B  1  925  ? 31.244  20.730  86.881  1.00 16.83 ? 923  PHE   B N     1 
ATOM   15891 C  CA    . PHE   B  1  925  ? 30.322  21.140  87.923  1.00 17.22 ? 923  PHE   B CA    1 
ATOM   15892 C  C     . PHE   B  1  925  ? 30.979  22.148  88.843  1.00 17.29 ? 923  PHE   B C     1 
ATOM   15893 O  O     . PHE   B  1  925  ? 32.174  22.064  89.131  1.00 18.00 ? 923  PHE   B O     1 
ATOM   15894 C  CB    . PHE   B  1  925  ? 29.870  19.945  88.760  1.00 16.89 ? 923  PHE   B CB    1 
ATOM   15895 C  CG    . PHE   B  1  925  ? 28.997  18.985  88.021  1.00 16.56 ? 923  PHE   B CG    1 
ATOM   15896 C  CD1   . PHE   B  1  925  ? 29.559  18.006  87.222  1.00 16.64 ? 923  PHE   B CD1   1 
ATOM   15897 C  CD2   . PHE   B  1  925  ? 27.615  19.055  88.121  1.00 16.77 ? 923  PHE   B CD2   1 
ATOM   15898 C  CE1   . PHE   B  1  925  ? 28.766  17.111  86.533  1.00 18.15 ? 923  PHE   B CE1   1 
ATOM   15899 C  CE2   . PHE   B  1  925  ? 26.809  18.163  87.430  1.00 16.67 ? 923  PHE   B CE2   1 
ATOM   15900 C  CZ    . PHE   B  1  925  ? 27.384  17.185  86.646  1.00 17.61 ? 923  PHE   B CZ    1 
ATOM   15901 N  N     . VAL   B  1  926  ? 30.172  23.084  89.318  1.00 16.75 ? 924  VAL   B N     1 
ATOM   15902 C  CA    . VAL   B  1  926  ? 30.518  23.966  90.421  1.00 16.28 ? 924  VAL   B CA    1 
ATOM   15903 C  C     . VAL   B  1  926  ? 29.411  23.801  91.451  1.00 16.14 ? 924  VAL   B C     1 
ATOM   15904 O  O     . VAL   B  1  926  ? 28.237  23.893  91.094  1.00 16.72 ? 924  VAL   B O     1 
ATOM   15905 C  CB    . VAL   B  1  926  ? 30.609  25.434  89.968  1.00 17.17 ? 924  VAL   B CB    1 
ATOM   15906 C  CG1   . VAL   B  1  926  ? 30.867  26.352  91.161  1.00 17.24 ? 924  VAL   B CG1   1 
ATOM   15907 C  CG2   . VAL   B  1  926  ? 31.707  25.600  88.935  1.00 18.92 ? 924  VAL   B CG2   1 
ATOM   15908 N  N     . PRO   B  1  927  ? 29.720  23.534  92.716  1.00 18.03 ? 925  PRO   B N     1 
ATOM   15909 C  CA    . PRO   B  1  927  ? 28.663  23.359  93.695  1.00 18.39 ? 925  PRO   B CA    1 
ATOM   15910 C  C     . PRO   B  1  927  ? 28.103  24.700  94.120  1.00 17.55 ? 925  PRO   B C     1 
ATOM   15911 O  O     . PRO   B  1  927  ? 28.787  25.730  94.007  1.00 17.83 ? 925  PRO   B O     1 
ATOM   15912 C  CB    . PRO   B  1  927  ? 29.386  22.687  94.869  1.00 22.04 ? 925  PRO   B CB    1 
ATOM   15913 C  CG    . PRO   B  1  927  ? 30.770  23.238  94.791  1.00 20.61 ? 925  PRO   B CG    1 
ATOM   15914 C  CD    . PRO   B  1  927  ? 31.063  23.417  93.299  1.00 18.80 ? 925  PRO   B CD    1 
ATOM   15915 N  N     . PRO   B  1  928  ? 26.867  24.720  94.603  1.00 18.25 ? 926  PRO   B N     1 
ATOM   15916 C  CA    . PRO   B  1  928  ? 26.331  25.930  95.224  1.00 17.24 ? 926  PRO   B CA    1 
ATOM   15917 C  C     . PRO   B  1  928  ? 27.326  26.530  96.199  1.00 16.98 ? 926  PRO   B C     1 
ATOM   15918 O  O     . PRO   B  1  928  ? 27.895  25.842  97.056  1.00 17.94 ? 926  PRO   B O     1 
ATOM   15919 C  CB    . PRO   B  1  928  ? 25.083  25.421  95.952  1.00 18.15 ? 926  PRO   B CB    1 
ATOM   15920 C  CG    . PRO   B  1  928  ? 24.632  24.274  95.124  1.00 21.29 ? 926  PRO   B CG    1 
ATOM   15921 C  CD    . PRO   B  1  928  ? 25.893  23.613  94.632  1.00 18.26 ? 926  PRO   B CD    1 
ATOM   15922 N  N     . THR   B  1  929  ? 27.553  27.819  96.038  1.00 16.82 ? 927  THR   B N     1 
ATOM   15923 C  CA    . THR   B  1  929  ? 28.586  28.549  96.740  1.00 16.44 ? 927  THR   B CA    1 
ATOM   15924 C  C     . THR   B  1  929  ? 27.946  29.785  97.336  1.00 16.69 ? 927  THR   B C     1 
ATOM   15925 O  O     . THR   B  1  929  ? 27.144  30.451  96.687  1.00 17.38 ? 927  THR   B O     1 
ATOM   15926 C  CB    . THR   B  1  929  ? 29.690  28.949  95.757  1.00 16.35 ? 927  THR   B CB    1 
ATOM   15927 O  OG1   . THR   B  1  929  ? 30.264  27.763  95.190  1.00 17.63 ? 927  THR   B OG1   1 
ATOM   15928 C  CG2   . THR   B  1  929  ? 30.786  29.762  96.442  1.00 18.01 ? 927  THR   B CG2   1 
ATOM   15929 N  N     . ILE   B  1  930  ? 28.290  30.077  98.584  1.00 16.30 ? 928  ILE   B N     1 
ATOM   15930 C  CA    . ILE   B  1  930  ? 27.804  31.251  99.288  1.00 17.57 ? 928  ILE   B CA    1 
ATOM   15931 C  C     . ILE   B  1  930  ? 29.016  32.047  99.723  1.00 16.76 ? 928  ILE   B C     1 
ATOM   15932 O  O     . ILE   B  1  930  ? 29.919  31.511  100.383 1.00 17.72 ? 928  ILE   B O     1 
ATOM   15933 C  CB    . ILE   B  1  930  ? 26.944  30.873  100.504 1.00 16.91 ? 928  ILE   B CB    1 
ATOM   15934 C  CG1   . ILE   B  1  930  ? 25.732  30.057  100.059 1.00 17.77 ? 928  ILE   B CG1   1 
ATOM   15935 C  CG2   . ILE   B  1  930  ? 26.520  32.143  101.242 1.00 18.03 ? 928  ILE   B CG2   1 
ATOM   15936 C  CD1   . ILE   B  1  930  ? 24.939  29.470  101.215 1.00 22.55 ? 928  ILE   B CD1   1 
ATOM   15937 N  N     . ILE   B  1  931  ? 29.039  33.322  99.363  1.00 17.45 ? 929  ILE   B N     1 
ATOM   15938 C  CA    . ILE   B  1  931  ? 30.145  34.210  99.672  1.00 15.78 ? 929  ILE   B CA    1 
ATOM   15939 C  C     . ILE   B  1  931  ? 29.595  35.405  100.421 1.00 17.74 ? 929  ILE   B C     1 
ATOM   15940 O  O     . ILE   B  1  931  ? 28.683  36.077  99.934  1.00 18.61 ? 929  ILE   B O     1 
ATOM   15941 C  CB    . ILE   B  1  931  ? 30.847  34.684  98.394  1.00 16.42 ? 929  ILE   B CB    1 
ATOM   15942 C  CG1   . ILE   B  1  931  ? 31.314  33.478  97.573  1.00 18.84 ? 929  ILE   B CG1   1 
ATOM   15943 C  CG2   . ILE   B  1  931  ? 32.006  35.615  98.758  1.00 18.62 ? 929  ILE   B CG2   1 
ATOM   15944 C  CD1   . ILE   B  1  931  ? 32.119  33.854  96.344  1.00 19.04 ? 929  ILE   B CD1   1 
ATOM   15945 N  N     . GLU   B  1  932  ? 30.150  35.686  101.589 1.00 17.47 ? 930  GLU   B N     1 
ATOM   15946 C  CA    . GLU   B  1  932  ? 29.695  36.831  102.351 1.00 18.35 ? 930  GLU   B CA    1 
ATOM   15947 C  C     . GLU   B  1  932  ? 30.479  38.052  101.915 1.00 18.39 ? 930  GLU   B C     1 
ATOM   15948 O  O     . GLU   B  1  932  ? 31.716  38.031  101.896 1.00 19.76 ? 930  GLU   B O     1 
ATOM   15949 C  CB    . GLU   B  1  932  ? 29.863  36.583  103.851 1.00 23.94 ? 930  GLU   B CB    1 
ATOM   15950 C  CG    . GLU   B  1  932  ? 29.003  35.443  104.336 1.00 26.65 ? 930  GLU   B CG    1 
ATOM   15951 C  CD    . GLU   B  1  932  ? 28.681  35.527  105.810 1.00 40.48 ? 930  GLU   B CD    1 
ATOM   15952 O  OE1   . GLU   B  1  932  ? 29.320  36.334  106.523 1.00 41.12 ? 930  GLU   B OE1   1 
ATOM   15953 O  OE2   . GLU   B  1  932  ? 27.783  34.781  106.251 1.00 35.03 ? 930  GLU   B OE2   1 
ATOM   15954 N  N     . LEU   B  1  933  ? 29.764  39.102  101.541 1.00 19.41 ? 931  LEU   B N     1 
ATOM   15955 C  CA    . LEU   B  1  933  ? 30.399  40.350  101.170 1.00 19.35 ? 931  LEU   B CA    1 
ATOM   15956 C  C     . LEU   B  1  933  ? 30.230  41.375  102.281 1.00 23.66 ? 931  LEU   B C     1 
ATOM   15957 O  O     . LEU   B  1  933  ? 29.250  41.350  103.029 1.00 27.49 ? 931  LEU   B O     1 
ATOM   15958 C  CB    . LEU   B  1  933  ? 29.776  40.907  99.894  1.00 21.49 ? 931  LEU   B CB    1 
ATOM   15959 C  CG    . LEU   B  1  933  ? 29.790  40.020  98.653  1.00 23.39 ? 931  LEU   B CG    1 
ATOM   15960 C  CD1   . LEU   B  1  933  ? 29.115  40.783  97.529  1.00 27.45 ? 931  LEU   B CD1   1 
ATOM   15961 C  CD2   . LEU   B  1  933  ? 31.217  39.637  98.290  1.00 32.30 ? 931  LEU   B CD2   1 
ATOM   15962 N  N     . GLU   B  1  934  ? 31.184  42.299  102.356 1.00 27.75 ? 932  GLU   B N     1 
ATOM   15963 C  CA    . GLU   B  1  934  ? 31.008  43.458  103.223 1.00 29.38 ? 932  GLU   B CA    1 
ATOM   15964 C  C     . GLU   B  1  934  ? 30.155  44.519  102.542 1.00 30.74 ? 932  GLU   B C     1 
ATOM   15965 O  O     . GLU   B  1  934  ? 29.330  45.173  103.189 1.00 33.75 ? 932  GLU   B O     1 
ATOM   15966 C  CB    . GLU   B  1  934  ? 32.370  44.033  103.621 1.00 34.83 ? 932  GLU   B CB    1 
ATOM   15967 N  N     . LYS   B  1  935  ? 30.312  44.677  101.233 1.00 25.68 ? 933  LYS   B N     1 
ATOM   15968 C  CA    . LYS   B  1  935  ? 29.600  45.699  100.491 1.00 28.15 ? 933  LYS   B CA    1 
ATOM   15969 C  C     . LYS   B  1  935  ? 29.301  45.143  99.113  1.00 25.27 ? 933  LYS   B C     1 
ATOM   15970 O  O     . LYS   B  1  935  ? 30.056  44.322  98.584  1.00 27.05 ? 933  LYS   B O     1 
ATOM   15971 C  CB    . LYS   B  1  935  ? 30.451  46.971  100.365 1.00 33.36 ? 933  LYS   B CB    1 
ATOM   15972 N  N     . LEU   B  1  936  ? 28.183  45.587  98.537  1.00 23.32 ? 934  LEU   B N     1 
ATOM   15973 C  CA    . LEU   B  1  936  ? 27.840  45.121  97.203  1.00 23.63 ? 934  LEU   B CA    1 
ATOM   15974 C  C     . LEU   B  1  936  ? 28.925  45.480  96.197  1.00 25.12 ? 934  LEU   B C     1 
ATOM   15975 O  O     . LEU   B  1  936  ? 29.146  44.735  95.238  1.00 25.57 ? 934  LEU   B O     1 
ATOM   15976 C  CB    . LEU   B  1  936  ? 26.475  45.665  96.794  1.00 26.58 ? 934  LEU   B CB    1 
ATOM   15977 C  CG    . LEU   B  1  936  ? 25.581  44.685  96.039  1.00 27.80 ? 934  LEU   B CG    1 
ATOM   15978 C  CD1   . LEU   B  1  936  ? 24.128  45.028  96.289  1.00 29.76 ? 934  LEU   B CD1   1 
ATOM   15979 C  CD2   . LEU   B  1  936  ? 25.907  44.732  94.571  1.00 30.12 ? 934  LEU   B CD2   1 
ATOM   15980 N  N     . SER   B  1  937  ? 29.638  46.584  96.417  1.00 23.51 ? 935  SER   B N     1 
ATOM   15981 C  CA    . SER   B  1  937  ? 30.692  46.988  95.496  1.00 26.42 ? 935  SER   B CA    1 
ATOM   15982 C  C     . SER   B  1  937  ? 31.886  46.042  95.498  1.00 28.11 ? 935  SER   B C     1 
ATOM   15983 O  O     . SER   B  1  937  ? 32.766  46.197  94.645  1.00 26.25 ? 935  SER   B O     1 
ATOM   15984 C  CB    . SER   B  1  937  ? 31.143  48.418  95.798  1.00 27.56 ? 935  SER   B CB    1 
ATOM   15985 O  OG    . SER   B  1  937  ? 31.561  48.524  97.146  1.00 32.14 ? 935  SER   B OG    1 
ATOM   15986 N  N     . ASP   B  1  938  ? 31.941  45.071  96.421  1.00 25.66 ? 936  ASP   B N     1 
ATOM   15987 C  CA    . ASP   B  1  938  ? 32.945  44.016  96.313  1.00 26.95 ? 936  ASP   B CA    1 
ATOM   15988 C  C     . ASP   B  1  938  ? 32.768  43.208  95.039  1.00 24.84 ? 936  ASP   B C     1 
ATOM   15989 O  O     . ASP   B  1  938  ? 33.720  42.583  94.569  1.00 27.36 ? 936  ASP   B O     1 
ATOM   15990 C  CB    . ASP   B  1  938  ? 32.835  43.024  97.475  1.00 31.00 ? 936  ASP   B CB    1 
ATOM   15991 C  CG    . ASP   B  1  938  ? 33.079  43.661  98.828  1.00 39.63 ? 936  ASP   B CG    1 
ATOM   15992 O  OD1   . ASP   B  1  938  ? 33.716  44.732  98.893  1.00 35.37 ? 936  ASP   B OD1   1 
ATOM   15993 O  OD2   . ASP   B  1  938  ? 32.620  43.074  99.833  1.00 42.65 ? 936  ASP   B OD2   1 
ATOM   15994 N  N     . LEU   B  1  939  ? 31.567  43.198  94.481  1.00 21.98 ? 937  LEU   B N     1 
ATOM   15995 C  CA    . LEU   B  1  939  ? 31.244  42.394  93.318  1.00 27.69 ? 937  LEU   B CA    1 
ATOM   15996 C  C     . LEU   B  1  939  ? 31.283  43.320  92.110  1.00 26.00 ? 937  LEU   B C     1 
ATOM   15997 O  O     . LEU   B  1  939  ? 30.531  44.302  92.058  1.00 33.32 ? 937  LEU   B O     1 
ATOM   15998 C  CB    . LEU   B  1  939  ? 29.843  41.822  93.524  1.00 25.03 ? 937  LEU   B CB    1 
ATOM   15999 C  CG    . LEU   B  1  939  ? 29.274  40.769  92.587  1.00 30.57 ? 937  LEU   B CG    1 
ATOM   16000 C  CD1   . LEU   B  1  939  ? 30.168  39.547  92.500  1.00 32.68 ? 937  LEU   B CD1   1 
ATOM   16001 C  CD2   . LEU   B  1  939  ? 27.919  40.398  93.137  1.00 24.54 ? 937  LEU   B CD2   1 
ATOM   16002 N  N     . GLN   B  1  940  ? 32.137  43.000  91.136  1.00 22.33 ? 938  GLN   B N     1 
ATOM   16003 C  CA    . GLN   B  1  940  ? 32.401  43.890  90.011  1.00 28.73 ? 938  GLN   B CA    1 
ATOM   16004 C  C     . GLN   B  1  940  ? 31.960  43.354  88.658  1.00 25.87 ? 938  GLN   B C     1 
ATOM   16005 O  O     . GLN   B  1  940  ? 32.065  44.078  87.663  1.00 24.92 ? 938  GLN   B O     1 
ATOM   16006 C  CB    . GLN   B  1  940  ? 33.899  44.237  89.932  1.00 36.61 ? 938  GLN   B CB    1 
ATOM   16007 N  N     . ARG   B  1  941  ? 31.480  42.120  88.584  1.00 20.08 ? 939  ARG   B N     1 
ATOM   16008 C  CA    . ARG   B  1  941  ? 31.090  41.554  87.307  1.00 20.93 ? 939  ARG   B CA    1 
ATOM   16009 C  C     . ARG   B  1  941  ? 30.023  40.505  87.558  1.00 17.83 ? 939  ARG   B C     1 
ATOM   16010 O  O     . ARG   B  1  941  ? 29.932  39.934  88.645  1.00 17.83 ? 939  ARG   B O     1 
ATOM   16011 C  CB    . ARG   B  1  941  ? 32.291  40.937  86.562  1.00 23.37 ? 939  ARG   B CB    1 
ATOM   16012 C  CG    . ARG   B  1  941  ? 32.904  39.699  87.231  1.00 25.16 ? 939  ARG   B CG    1 
ATOM   16013 C  CD    . ARG   B  1  941  ? 34.232  39.327  86.558  1.00 23.52 ? 939  ARG   B CD    1 
ATOM   16014 N  NE    . ARG   B  1  941  ? 34.850  38.126  87.121  1.00 25.43 ? 939  ARG   B NE    1 
ATOM   16015 C  CZ    . ARG   B  1  941  ? 34.611  36.887  86.704  1.00 25.34 ? 939  ARG   B CZ    1 
ATOM   16016 N  NH1   . ARG   B  1  941  ? 33.699  36.633  85.776  1.00 23.80 ? 939  ARG   B NH1   1 
ATOM   16017 N  NH2   . ARG   B  1  941  ? 35.314  35.880  87.223  1.00 24.01 ? 939  ARG   B NH2   1 
ATOM   16018 N  N     . GLU   B  1  942  ? 29.231  40.247  86.525  1.00 19.17 ? 940  GLU   B N     1 
ATOM   16019 C  CA    . GLU   B  1  942  ? 28.257  39.168  86.576  1.00 17.18 ? 940  GLU   B CA    1 
ATOM   16020 C  C     . GLU   B  1  942  ? 29.002  37.848  86.539  1.00 17.11 ? 940  GLU   B C     1 
ATOM   16021 O  O     . GLU   B  1  942  ? 29.776  37.591  85.613  1.00 20.90 ? 940  GLU   B O     1 
ATOM   16022 C  CB    . GLU   B  1  942  ? 27.318  39.274  85.378  1.00 18.67 ? 940  GLU   B CB    1 
ATOM   16023 C  CG    . GLU   B  1  942  ? 26.315  38.137  85.288  1.00 17.36 ? 940  GLU   B CG    1 
ATOM   16024 C  CD    . GLU   B  1  942  ? 25.591  38.096  83.951  1.00 18.12 ? 940  GLU   B CD    1 
ATOM   16025 O  OE1   . GLU   B  1  942  ? 26.276  38.261  82.907  1.00 20.95 ? 940  GLU   B OE1   1 
ATOM   16026 O  OE2   . GLU   B  1  942  ? 24.360  37.885  83.937  1.00 16.03 ? 940  GLU   B OE2   1 
ATOM   16027 N  N     . VAL   B  1  943  ? 28.787  37.016  87.543  1.00 15.47 ? 941  VAL   B N     1 
ATOM   16028 C  CA    . VAL   B  1  943  ? 29.422  35.711  87.637  1.00 16.10 ? 941  VAL   B CA    1 
ATOM   16029 C  C     . VAL   B  1  943  ? 28.329  34.688  87.377  1.00 16.68 ? 941  VAL   B C     1 
ATOM   16030 O  O     . VAL   B  1  943  ? 27.430  34.479  88.201  1.00 15.90 ? 941  VAL   B O     1 
ATOM   16031 C  CB    . VAL   B  1  943  ? 30.100  35.507  88.997  1.00 17.81 ? 941  VAL   B CB    1 
ATOM   16032 C  CG1   . VAL   B  1  943  ? 30.715  34.107  89.075  1.00 18.91 ? 941  VAL   B CG1   1 
ATOM   16033 C  CG2   . VAL   B  1  943  ? 31.151  36.581  89.224  1.00 20.76 ? 941  VAL   B CG2   1 
ATOM   16034 N  N     . PHE   B  1  944  ? 28.391  34.064  86.207  1.00 15.91 ? 942  PHE   B N     1 
ATOM   16035 C  CA    . PHE   B  1  944  ? 27.272  33.304  85.673  1.00 15.21 ? 942  PHE   B CA    1 
ATOM   16036 C  C     . PHE   B  1  944  ? 27.408  31.849  86.111  1.00 15.32 ? 942  PHE   B C     1 
ATOM   16037 O  O     . PHE   B  1  944  ? 27.752  30.947  85.354  1.00 17.10 ? 942  PHE   B O     1 
ATOM   16038 C  CB    . PHE   B  1  944  ? 27.255  33.454  84.158  1.00 15.61 ? 942  PHE   B CB    1 
ATOM   16039 C  CG    . PHE   B  1  944  ? 25.929  33.200  83.541  1.00 15.66 ? 942  PHE   B CG    1 
ATOM   16040 C  CD1   . PHE   B  1  944  ? 24.896  34.098  83.709  1.00 15.86 ? 942  PHE   B CD1   1 
ATOM   16041 C  CD2   . PHE   B  1  944  ? 25.714  32.065  82.786  1.00 15.83 ? 942  PHE   B CD2   1 
ATOM   16042 C  CE1   . PHE   B  1  944  ? 23.667  33.872  83.123  1.00 16.78 ? 942  PHE   B CE1   1 
ATOM   16043 C  CE2   . PHE   B  1  944  ? 24.481  31.834  82.195  1.00 15.82 ? 942  PHE   B CE2   1 
ATOM   16044 C  CZ    . PHE   B  1  944  ? 23.454  32.739  82.385  1.00 16.57 ? 942  PHE   B CZ    1 
ATOM   16045 N  N     . GLY   B  1  945  ? 27.154  31.635  87.389  1.00 15.46 ? 943  GLY   B N     1 
ATOM   16046 C  CA    . GLY   B  1  945  ? 27.263  30.322  87.959  1.00 16.04 ? 943  GLY   B CA    1 
ATOM   16047 C  C     . GLY   B  1  945  ? 26.563  30.291  89.294  1.00 16.60 ? 943  GLY   B C     1 
ATOM   16048 O  O     . GLY   B  1  945  ? 25.876  31.239  89.686  1.00 16.09 ? 943  GLY   B O     1 
ATOM   16049 N  N     . PRO   B  1  946  ? 26.728  29.206  90.031  1.00 15.48 ? 944  PRO   B N     1 
ATOM   16050 C  CA    . PRO   B  1  946  ? 25.921  29.012  91.254  1.00 15.78 ? 944  PRO   B CA    1 
ATOM   16051 C  C     . PRO   B  1  946  ? 26.577  29.665  92.466  1.00 14.90 ? 944  PRO   B C     1 
ATOM   16052 O  O     . PRO   B  1  946  ? 26.938  29.005  93.439  1.00 17.28 ? 944  PRO   B O     1 
ATOM   16053 C  CB    . PRO   B  1  946  ? 25.873  27.486  91.372  1.00 16.07 ? 944  PRO   B CB    1 
ATOM   16054 C  CG    . PRO   B  1  946  ? 27.221  27.057  90.829  1.00 17.58 ? 944  PRO   B CG    1 
ATOM   16055 C  CD    . PRO   B  1  946  ? 27.547  28.029  89.693  1.00 16.35 ? 944  PRO   B CD    1 
ATOM   16056 N  N     . VAL   B  1  947  ? 26.769  30.970  92.391  1.00 15.84 ? 945  VAL   B N     1 
ATOM   16057 C  CA    . VAL   B  1  947  ? 27.526  31.702  93.395  1.00 15.60 ? 945  VAL   B CA    1 
ATOM   16058 C  C     . VAL   B  1  947  ? 26.626  32.787  93.945  1.00 17.83 ? 945  VAL   B C     1 
ATOM   16059 O  O     . VAL   B  1  947  ? 26.346  33.781  93.261  1.00 17.99 ? 945  VAL   B O     1 
ATOM   16060 C  CB    . VAL   B  1  947  ? 28.823  32.287  92.834  1.00 17.40 ? 945  VAL   B CB    1 
ATOM   16061 C  CG1   . VAL   B  1  947  ? 29.599  32.956  93.957  1.00 16.66 ? 945  VAL   B CG1   1 
ATOM   16062 C  CG2   . VAL   B  1  947  ? 29.644  31.189  92.177  1.00 17.90 ? 945  VAL   B CG2   1 
ATOM   16063 N  N     . LEU   B  1  948  ? 26.158  32.591  95.171  1.00 15.59 ? 946  LEU   B N     1 
ATOM   16064 C  CA    . LEU   B  1  948  ? 25.285  33.538  95.838  1.00 15.82 ? 946  LEU   B CA    1 
ATOM   16065 C  C     . LEU   B  1  948  ? 26.124  34.380  96.780  1.00 15.23 ? 946  LEU   B C     1 
ATOM   16066 O  O     . LEU   B  1  948  ? 26.889  33.842  97.591  1.00 16.41 ? 946  LEU   B O     1 
ATOM   16067 C  CB    . LEU   B  1  948  ? 24.250  32.773  96.649  1.00 14.91 ? 946  LEU   B CB    1 
ATOM   16068 C  CG    . LEU   B  1  948  ? 23.284  33.671  97.407  1.00 14.99 ? 946  LEU   B CG    1 
ATOM   16069 C  CD1   . LEU   B  1  948  ? 22.441  34.457  96.427  1.00 15.32 ? 946  LEU   B CD1   1 
ATOM   16070 C  CD2   . LEU   B  1  948  ? 22.411  32.795  98.288  1.00 20.81 ? 946  LEU   B CD2   1 
ATOM   16071 N  N     . HIS   B  1  949  ? 25.985  35.689  96.681  1.00 14.80 ? 947  HIS   B N     1 
ATOM   16072 C  CA    . HIS   B  1  949  ? 26.675  36.599  97.570  1.00 14.49 ? 947  HIS   B CA    1 
ATOM   16073 C  C     . HIS   B  1  949  ? 25.698  37.095  98.605  1.00 15.63 ? 947  HIS   B C     1 
ATOM   16074 O  O     . HIS   B  1  949  ? 24.523  37.306  98.305  1.00 18.82 ? 947  HIS   B O     1 
ATOM   16075 C  CB    . HIS   B  1  949  ? 27.261  37.762  96.784  1.00 16.19 ? 947  HIS   B CB    1 
ATOM   16076 C  CG    . HIS   B  1  949  ? 28.142  37.300  95.673  1.00 15.73 ? 947  HIS   B CG    1 
ATOM   16077 N  ND1   . HIS   B  1  949  ? 27.642  36.947  94.440  1.00 16.63 ? 947  HIS   B ND1   1 
ATOM   16078 C  CD2   . HIS   B  1  949  ? 29.471  37.044  95.632  1.00 15.82 ? 947  HIS   B CD2   1 
ATOM   16079 C  CE1   . HIS   B  1  949  ? 28.634  36.534  93.670  1.00 16.44 ? 947  HIS   B CE1   1 
ATOM   16080 N  NE2   . HIS   B  1  949  ? 29.752  36.584  94.367  1.00 16.88 ? 947  HIS   B NE2   1 
ATOM   16081 N  N     . VAL   B  1  950  ? 26.165  37.231  99.835  1.00 17.00 ? 948  VAL   B N     1 
ATOM   16082 C  CA    . VAL   B  1  950  ? 25.282  37.569  100.935 1.00 16.89 ? 948  VAL   B CA    1 
ATOM   16083 C  C     . VAL   B  1  950  ? 25.725  38.883  101.543 1.00 17.12 ? 948  VAL   B C     1 
ATOM   16084 O  O     . VAL   B  1  950  ? 26.907  39.068  101.863 1.00 18.57 ? 948  VAL   B O     1 
ATOM   16085 C  CB    . VAL   B  1  950  ? 25.241  36.454  101.990 1.00 17.27 ? 948  VAL   B CB    1 
ATOM   16086 C  CG1   . VAL   B  1  950  ? 24.468  36.948  103.228 1.00 19.49 ? 948  VAL   B CG1   1 
ATOM   16087 C  CG2   . VAL   B  1  950  ? 24.612  35.207  101.412 1.00 19.44 ? 948  VAL   B CG2   1 
ATOM   16088 N  N     . ILE   B  1  951  ? 24.774  39.781  101.717 1.00 17.22 ? 949  ILE   B N     1 
ATOM   16089 C  CA    . ILE   B  1  951  ? 24.983  41.050  102.391 1.00 17.34 ? 949  ILE   B CA    1 
ATOM   16090 C  C     . ILE   B  1  951  ? 24.006  41.110  103.553 1.00 17.22 ? 949  ILE   B C     1 
ATOM   16091 O  O     . ILE   B  1  951  ? 22.853  40.691  103.428 1.00 18.21 ? 949  ILE   B O     1 
ATOM   16092 C  CB    . ILE   B  1  951  ? 24.715  42.213  101.417 1.00 20.76 ? 949  ILE   B CB    1 
ATOM   16093 C  CG1   . ILE   B  1  951  ? 25.784  42.238  100.329 1.00 24.93 ? 949  ILE   B CG1   1 
ATOM   16094 C  CG2   . ILE   B  1  951  ? 24.655  43.550  102.165 1.00 29.53 ? 949  ILE   B CG2   1 
ATOM   16095 C  CD1   . ILE   B  1  951  ? 25.574  43.327  99.341  1.00 33.06 ? 949  ILE   B CD1   1 
ATOM   16096 N  N     . ARG   B  1  952  ? 24.481  41.577  104.693 1.00 17.26 ? 950  ARG   B N     1 
ATOM   16097 C  CA    A ARG   B  1  952  ? 23.622  41.841  105.834 0.69 17.37 ? 950  ARG   B CA    1 
ATOM   16098 C  CA    B ARG   B  1  952  ? 23.635  41.844  105.847 0.31 17.46 ? 950  ARG   B CA    1 
ATOM   16099 C  C     . ARG   B  1  952  ? 23.404  43.344  105.930 1.00 18.64 ? 950  ARG   B C     1 
ATOM   16100 O  O     . ARG   B  1  952  ? 24.320  44.132  105.694 1.00 22.99 ? 950  ARG   B O     1 
ATOM   16101 C  CB    A ARG   B  1  952  ? 24.287  41.317  107.109 0.69 18.86 ? 950  ARG   B CB    1 
ATOM   16102 C  CB    B ARG   B  1  952  ? 24.331  41.390  107.131 0.31 18.89 ? 950  ARG   B CB    1 
ATOM   16103 C  CG    A ARG   B  1  952  ? 24.618  39.837  107.016 0.69 20.22 ? 950  ARG   B CG    1 
ATOM   16104 C  CG    B ARG   B  1  952  ? 24.381  39.892  107.334 0.31 21.35 ? 950  ARG   B CG    1 
ATOM   16105 C  CD    A ARG   B  1  952  ? 25.678  39.437  108.028 0.69 25.46 ? 950  ARG   B CD    1 
ATOM   16106 C  CD    B ARG   B  1  952  ? 25.295  39.552  108.502 0.31 24.75 ? 950  ARG   B CD    1 
ATOM   16107 N  NE    A ARG   B  1  952  ? 26.097  38.054  107.845 0.69 27.88 ? 950  ARG   B NE    1 
ATOM   16108 N  NE    B ARG   B  1  952  ? 25.157  38.170  108.941 0.31 27.60 ? 950  ARG   B NE    1 
ATOM   16109 C  CZ    A ARG   B  1  952  ? 25.741  37.048  108.635 0.69 27.48 ? 950  ARG   B CZ    1 
ATOM   16110 C  CZ    B ARG   B  1  952  ? 25.649  37.121  108.295 0.31 27.91 ? 950  ARG   B CZ    1 
ATOM   16111 N  NH1   A ARG   B  1  952  ? 24.932  37.231  109.663 0.69 22.17 ? 950  ARG   B NH1   1 
ATOM   16112 N  NH1   B ARG   B  1  952  ? 26.269  37.250  107.131 0.31 27.75 ? 950  ARG   B NH1   1 
ATOM   16113 N  NH2   A ARG   B  1  952  ? 26.217  35.830  108.390 0.69 29.37 ? 950  ARG   B NH2   1 
ATOM   16114 N  NH2   B ARG   B  1  952  ? 25.517  35.911  108.830 0.31 28.57 ? 950  ARG   B NH2   1 
ATOM   16115 N  N     . TYR   B  1  953  ? 22.183  43.747  106.270 1.00 17.60 ? 951  TYR   B N     1 
ATOM   16116 C  CA    . TYR   B  1  953  ? 21.925  45.175  106.361 1.00 18.09 ? 951  TYR   B CA    1 
ATOM   16117 C  C     . TYR   B  1  953  ? 21.066  45.490  107.572 1.00 18.20 ? 951  TYR   B C     1 
ATOM   16118 O  O     . TYR   B  1  953  ? 20.285  44.656  108.038 1.00 18.92 ? 951  TYR   B O     1 
ATOM   16119 C  CB    . TYR   B  1  953  ? 21.260  45.719  105.081 1.00 18.22 ? 951  TYR   B CB    1 
ATOM   16120 C  CG    . TYR   B  1  953  ? 19.827  45.288  104.924 1.00 16.36 ? 951  TYR   B CG    1 
ATOM   16121 C  CD1   . TYR   B  1  953  ? 19.498  44.046  104.383 1.00 14.55 ? 951  TYR   B CD1   1 
ATOM   16122 C  CD2   . TYR   B  1  953  ? 18.800  46.115  105.329 1.00 15.90 ? 951  TYR   B CD2   1 
ATOM   16123 C  CE1   . TYR   B  1  953  ? 18.190  43.660  104.266 1.00 16.11 ? 951  TYR   B CE1   1 
ATOM   16124 C  CE2   . TYR   B  1  953  ? 17.493  45.734  105.200 1.00 18.40 ? 951  TYR   B CE2   1 
ATOM   16125 C  CZ    . TYR   B  1  953  ? 17.193  44.508  104.665 1.00 17.96 ? 951  TYR   B CZ    1 
ATOM   16126 O  OH    . TYR   B  1  953  ? 15.886  44.124  104.551 1.00 18.60 ? 951  TYR   B OH    1 
ATOM   16127 N  N     . ARG   B  1  954  ? 21.218  46.715  108.068 1.00 21.29 ? 952  ARG   B N     1 
ATOM   16128 C  CA    . ARG   B  1  954  ? 20.343  47.242  109.105 1.00 25.84 ? 952  ARG   B CA    1 
ATOM   16129 C  C     . ARG   B  1  954  ? 19.151  47.895  108.429 1.00 24.05 ? 952  ARG   B C     1 
ATOM   16130 O  O     . ARG   B  1  954  ? 19.303  48.554  107.400 1.00 21.37 ? 952  ARG   B O     1 
ATOM   16131 C  CB    . ARG   B  1  954  ? 21.077  48.283  109.957 1.00 26.36 ? 952  ARG   B CB    1 
ATOM   16132 N  N     . ARG   B  1  955  ? 17.960  47.702  109.009 1.00 22.60 ? 953  ARG   B N     1 
ATOM   16133 C  CA    . ARG   B  1  955  ? 16.744  48.204  108.375 1.00 24.78 ? 953  ARG   B CA    1 
ATOM   16134 C  C     . ARG   B  1  955  ? 16.821  49.704  108.106 1.00 23.27 ? 953  ARG   B C     1 
ATOM   16135 O  O     . ARG   B  1  955  ? 16.308  50.186  107.088 1.00 23.33 ? 953  ARG   B O     1 
ATOM   16136 C  CB    . ARG   B  1  955  ? 15.509  47.851  109.203 1.00 29.32 ? 953  ARG   B CB    1 
ATOM   16137 C  CG    . ARG   B  1  955  ? 14.174  48.281  108.575 1.00 29.36 ? 953  ARG   B CG    1 
ATOM   16138 C  CD    . ARG   B  1  955  ? 14.024  47.837  107.115 1.00 28.40 ? 953  ARG   B CD    1 
ATOM   16139 N  NE    . ARG   B  1  955  ? 12.731  48.232  106.567 1.00 30.67 ? 953  ARG   B NE    1 
ATOM   16140 C  CZ    . ARG   B  1  955  ? 12.409  49.471  106.218 1.00 34.21 ? 953  ARG   B CZ    1 
ATOM   16141 N  NH1   . ARG   B  1  955  ? 13.274  50.468  106.327 1.00 33.60 ? 953  ARG   B NH1   1 
ATOM   16142 N  NH2   . ARG   B  1  955  ? 11.185  49.716  105.747 1.00 29.29 ? 953  ARG   B NH2   1 
ATOM   16143 N  N     . ASP   B  1  956  ? 17.459  50.468  108.994 1.00 23.78 ? 954  ASP   B N     1 
ATOM   16144 C  CA    A ASP   B  1  956  ? 17.579  51.906  108.765 0.46 24.75 ? 954  ASP   B CA    1 
ATOM   16145 C  CA    B ASP   B  1  956  ? 17.549  51.903  108.742 0.54 24.72 ? 954  ASP   B CA    1 
ATOM   16146 C  C     . ASP   B  1  956  ? 18.455  52.241  107.566 1.00 25.17 ? 954  ASP   B C     1 
ATOM   16147 O  O     . ASP   B  1  956  ? 18.462  53.396  107.124 1.00 29.87 ? 954  ASP   B O     1 
ATOM   16148 C  CB    A ASP   B  1  956  ? 18.116  52.602  110.015 0.46 26.54 ? 954  ASP   B CB    1 
ATOM   16149 C  CB    B ASP   B  1  956  ? 17.892  52.710  110.010 0.54 26.50 ? 954  ASP   B CB    1 
ATOM   16150 C  CG    A ASP   B  1  956  ? 17.161  52.509  111.185 0.46 30.99 ? 954  ASP   B CG    1 
ATOM   16151 C  CG    B ASP   B  1  956  ? 19.194  52.276  110.682 0.54 25.06 ? 954  ASP   B CG    1 
ATOM   16152 O  OD1   A ASP   B  1  956  ? 15.947  52.330  110.950 0.46 34.86 ? 954  ASP   B OD1   1 
ATOM   16153 O  OD1   B ASP   B  1  956  ? 20.035  51.596  110.062 0.54 28.71 ? 954  ASP   B OD1   1 
ATOM   16154 O  OD2   A ASP   B  1  956  ? 17.624  52.620  112.339 0.46 32.36 ? 954  ASP   B OD2   1 
ATOM   16155 O  OD2   B ASP   B  1  956  ? 19.374  52.638  111.867 0.54 30.37 ? 954  ASP   B OD2   1 
ATOM   16156 N  N     . ASP   B  1  957  ? 19.184  51.268  107.037 1.00 22.23 ? 955  ASP   B N     1 
ATOM   16157 C  CA    . ASP   B  1  957  ? 20.032  51.462  105.877 1.00 23.45 ? 955  ASP   B CA    1 
ATOM   16158 C  C     . ASP   B  1  957  ? 19.380  50.942  104.601 1.00 20.14 ? 955  ASP   B C     1 
ATOM   16159 O  O     . ASP   B  1  957  ? 20.054  50.829  103.581 1.00 21.04 ? 955  ASP   B O     1 
ATOM   16160 C  CB    . ASP   B  1  957  ? 21.381  50.769  106.086 1.00 24.18 ? 955  ASP   B CB    1 
ATOM   16161 C  CG    . ASP   B  1  957  ? 22.255  51.478  107.104 1.00 35.27 ? 955  ASP   B CG    1 
ATOM   16162 O  OD1   . ASP   B  1  957  ? 22.049  52.689  107.337 1.00 32.53 ? 955  ASP   B OD1   1 
ATOM   16163 O  OD2   . ASP   B  1  957  ? 23.155  50.816  107.664 1.00 39.79 ? 955  ASP   B OD2   1 
ATOM   16164 N  N     . LEU   B  1  958  ? 18.087  50.613  104.649 1.00 19.26 ? 956  LEU   B N     1 
ATOM   16165 C  CA    . LEU   B  1  958  ? 17.431  50.015  103.491 1.00 18.08 ? 956  LEU   B CA    1 
ATOM   16166 C  C     . LEU   B  1  958  ? 17.547  50.903  102.261 1.00 18.79 ? 956  LEU   B C     1 
ATOM   16167 O  O     . LEU   B  1  958  ? 17.838  50.419  101.161 1.00 17.76 ? 956  LEU   B O     1 
ATOM   16168 C  CB    . LEU   B  1  958  ? 15.965  49.759  103.806 1.00 18.54 ? 956  LEU   B CB    1 
ATOM   16169 C  CG    . LEU   B  1  958  ? 15.132  49.181  102.664 1.00 17.77 ? 956  LEU   B CG    1 
ATOM   16170 C  CD1   . LEU   B  1  958  ? 15.743  47.883  102.155 1.00 19.53 ? 956  LEU   B CD1   1 
ATOM   16171 C  CD2   . LEU   B  1  958  ? 13.720  48.948  103.130 1.00 22.29 ? 956  LEU   B CD2   1 
ATOM   16172 N  N     . ASP   B  1  959  ? 17.335  52.207  102.416 1.00 17.66 ? 957  ASP   B N     1 
ATOM   16173 C  CA    . ASP   B  1  959  ? 17.371  53.072  101.243 1.00 16.87 ? 957  ASP   B CA    1 
ATOM   16174 C  C     . ASP   B  1  959  ? 18.758  53.078  100.615 1.00 17.74 ? 957  ASP   B C     1 
ATOM   16175 O  O     . ASP   B  1  959  ? 18.894  53.048  99.385  1.00 17.74 ? 957  ASP   B O     1 
ATOM   16176 C  CB    . ASP   B  1  959  ? 16.918  54.482  101.610 1.00 18.88 ? 957  ASP   B CB    1 
ATOM   16177 C  CG    . ASP   B  1  959  ? 16.456  55.261  100.407 1.00 19.71 ? 957  ASP   B CG    1 
ATOM   16178 O  OD1   . ASP   B  1  959  ? 15.698  54.701  99.585  1.00 19.32 ? 957  ASP   B OD1   1 
ATOM   16179 O  OD2   . ASP   B  1  959  ? 16.832  56.437  100.285 1.00 21.04 ? 957  ASP   B OD2   1 
ATOM   16180 N  N     . ARG   B  1  960  ? 19.796  53.113  101.442 1.00 17.92 ? 958  ARG   B N     1 
ATOM   16181 C  CA    . ARG   B  1  960  ? 21.158  53.054  100.936 1.00 17.73 ? 958  ARG   B CA    1 
ATOM   16182 C  C     . ARG   B  1  960  ? 21.438  51.706  100.295 1.00 17.26 ? 958  ARG   B C     1 
ATOM   16183 O  O     . ARG   B  1  960  ? 22.173  51.625  99.305  1.00 17.66 ? 958  ARG   B O     1 
ATOM   16184 C  CB    . ARG   B  1  960  ? 22.130  53.307  102.082 1.00 21.25 ? 958  ARG   B CB    1 
ATOM   16185 N  N     . LEU   B  1  961  ? 20.871  50.634  100.846 1.00 16.51 ? 959  LEU   B N     1 
ATOM   16186 C  CA    . LEU   B  1  961  ? 21.034  49.323  100.229 1.00 15.79 ? 959  LEU   B CA    1 
ATOM   16187 C  C     . LEU   B  1  961  ? 20.438  49.296  98.833  1.00 16.01 ? 959  LEU   B C     1 
ATOM   16188 O  O     . LEU   B  1  961  ? 21.051  48.760  97.902  1.00 16.40 ? 959  LEU   B O     1 
ATOM   16189 C  CB    . LEU   B  1  961  ? 20.394  48.252  101.099 1.00 17.49 ? 959  LEU   B CB    1 
ATOM   16190 C  CG    . LEU   B  1  961  ? 20.419  46.849  100.499 1.00 17.19 ? 959  LEU   B CG    1 
ATOM   16191 C  CD1   . LEU   B  1  961  ? 21.857  46.363  100.370 1.00 21.39 ? 959  LEU   B CD1   1 
ATOM   16192 C  CD2   . LEU   B  1  961  ? 19.583  45.900  101.330 1.00 19.11 ? 959  LEU   B CD2   1 
ATOM   16193 N  N     . VAL   B  1  962  ? 19.263  49.898  98.661  1.00 15.25 ? 960  VAL   B N     1 
ATOM   16194 C  CA    . VAL   B  1  962  ? 18.677  49.976  97.330  1.00 16.38 ? 960  VAL   B CA    1 
ATOM   16195 C  C     . VAL   B  1  962  ? 19.609  50.726  96.391  1.00 16.80 ? 960  VAL   B C     1 
ATOM   16196 O  O     . VAL   B  1  962  ? 19.819  50.308  95.250  1.00 16.26 ? 960  VAL   B O     1 
ATOM   16197 C  CB    . VAL   B  1  962  ? 17.277  50.601  97.394  1.00 17.16 ? 960  VAL   B CB    1 
ATOM   16198 C  CG1   . VAL   B  1  962  ? 16.783  50.872  96.003  1.00 19.57 ? 960  VAL   B CG1   1 
ATOM   16199 C  CG2   . VAL   B  1  962  ? 16.335  49.667  98.134  1.00 17.48 ? 960  VAL   B CG2   1 
ATOM   16200 N  N     . ASP   B  1  963  ? 20.219  51.816  96.864  1.00 15.75 ? 961  ASP   B N     1 
ATOM   16201 C  CA    . ASP   B  1  963  ? 21.205  52.515  96.040  1.00 17.28 ? 961  ASP   B CA    1 
ATOM   16202 C  C     . ASP   B  1  963  ? 22.345  51.591  95.660  1.00 18.52 ? 961  ASP   B C     1 
ATOM   16203 O  O     . ASP   B  1  963  ? 22.826  51.620  94.519  1.00 18.29 ? 961  ASP   B O     1 
ATOM   16204 C  CB    . ASP   B  1  963  ? 21.809  53.685  96.810  1.00 18.07 ? 961  ASP   B CB    1 
ATOM   16205 C  CG    . ASP   B  1  963  ? 20.865  54.804  96.995  1.00 21.66 ? 961  ASP   B CG    1 
ATOM   16206 O  OD1   . ASP   B  1  963  ? 19.894  54.898  96.222  1.00 22.92 ? 961  ASP   B OD1   1 
ATOM   16207 O  OD2   . ASP   B  1  963  ? 21.125  55.603  97.921  1.00 23.28 ? 961  ASP   B OD2   1 
ATOM   16208 N  N     . ASP   B  1  964  ? 22.822  50.796  96.619  1.00 16.67 ? 962  ASP   B N     1 
ATOM   16209 C  CA    . ASP   B  1  964  ? 23.918  49.875  96.340  1.00 17.74 ? 962  ASP   B CA    1 
ATOM   16210 C  C     . ASP   B  1  964  ? 23.528  48.879  95.265  1.00 17.55 ? 962  ASP   B C     1 
ATOM   16211 O  O     . ASP   B  1  964  ? 24.331  48.570  94.381  1.00 17.69 ? 962  ASP   B O     1 
ATOM   16212 C  CB    . ASP   B  1  964  ? 24.317  49.126  97.608  1.00 18.42 ? 962  ASP   B CB    1 
ATOM   16213 C  CG    . ASP   B  1  964  ? 24.982  50.017  98.636  1.00 23.49 ? 962  ASP   B CG    1 
ATOM   16214 O  OD1   . ASP   B  1  964  ? 25.323  51.175  98.314  1.00 23.55 ? 962  ASP   B OD1   1 
ATOM   16215 O  OD2   . ASP   B  1  964  ? 25.156  49.540  99.782  1.00 27.86 ? 962  ASP   B OD2   1 
ATOM   16216 N  N     . VAL   B  1  965  ? 22.294  48.374  95.311  1.00 15.29 ? 963  VAL   B N     1 
ATOM   16217 C  CA    . VAL   B  1  965  ? 21.832  47.470  94.264  1.00 14.32 ? 963  VAL   B CA    1 
ATOM   16218 C  C     . VAL   B  1  965  ? 21.825  48.186  92.923  1.00 16.02 ? 963  VAL   B C     1 
ATOM   16219 O  O     . VAL   B  1  965  ? 22.351  47.674  91.926  1.00 17.17 ? 963  VAL   B O     1 
ATOM   16220 C  CB    . VAL   B  1  965  ? 20.458  46.882  94.622  1.00 14.94 ? 963  VAL   B CB    1 
ATOM   16221 C  CG1   . VAL   B  1  965  ? 19.923  46.076  93.457  1.00 15.49 ? 963  VAL   B CG1   1 
ATOM   16222 C  CG2   . VAL   B  1  965  ? 20.580  46.008  95.875  1.00 17.71 ? 963  VAL   B CG2   1 
ATOM   16223 N  N     . ASN   B  1  966  ? 21.296  49.406  92.891  1.00 16.14 ? 964  ASN   B N     1 
ATOM   16224 C  CA    . ASN   B  1  966  ? 21.225  50.135  91.624  1.00 16.31 ? 964  ASN   B CA    1 
ATOM   16225 C  C     . ASN   B  1  966  ? 22.613  50.522  91.125  1.00 16.91 ? 964  ASN   B C     1 
ATOM   16226 O  O     . ASN   B  1  966  ? 22.822  50.680  89.918  1.00 18.39 ? 964  ASN   B O     1 
ATOM   16227 C  CB    . ASN   B  1  966  ? 20.393  51.401  91.798  1.00 16.53 ? 964  ASN   B CB    1 
ATOM   16228 C  CG    . ASN   B  1  966  ? 18.917  51.126  91.985  1.00 15.35 ? 964  ASN   B CG    1 
ATOM   16229 O  OD1   . ASN   B  1  966  ? 18.404  50.101  91.549  1.00 16.96 ? 964  ASN   B OD1   1 
ATOM   16230 N  ND2   . ASN   B  1  966  ? 18.223  52.063  92.612  1.00 16.98 ? 964  ASN   B ND2   1 
ATOM   16231 N  N     . ALA   B  1  967  ? 23.575  50.656  92.026  1.00 16.24 ? 965  ALA   B N     1 
ATOM   16232 C  CA    . ALA   B  1  967  ? 24.867  51.211  91.667  1.00 16.69 ? 965  ALA   B CA    1 
ATOM   16233 C  C     . ALA   B  1  967  ? 25.706  50.277  90.821  1.00 17.37 ? 965  ALA   B C     1 
ATOM   16234 O  O     . ALA   B  1  967  ? 26.727  50.719  90.287  1.00 19.24 ? 965  ALA   B O     1 
ATOM   16235 C  CB    . ALA   B  1  967  ? 25.636  51.574  92.938  1.00 18.59 ? 965  ALA   B CB    1 
ATOM   16236 N  N     . THR   B  1  968  ? 25.321  49.006  90.693  1.00 16.08 ? 966  THR   B N     1 
ATOM   16237 C  CA    . THR   B  1  968  ? 26.069  48.121  89.813  1.00 16.87 ? 966  THR   B CA    1 
ATOM   16238 C  C     . THR   B  1  968  ? 25.926  48.528  88.356  1.00 17.31 ? 966  THR   B C     1 
ATOM   16239 O  O     . THR   B  1  968  ? 26.754  48.127  87.527  1.00 18.38 ? 966  THR   B O     1 
ATOM   16240 C  CB    . THR   B  1  968  ? 25.585  46.682  89.942  1.00 17.16 ? 966  THR   B CB    1 
ATOM   16241 O  OG1   . THR   B  1  968  ? 24.285  46.576  89.344  1.00 17.02 ? 966  THR   B OG1   1 
ATOM   16242 C  CG2   . THR   B  1  968  ? 25.525  46.241  91.389  1.00 18.19 ? 966  THR   B CG2   1 
ATOM   16243 N  N     . GLY   B  1  969  ? 24.888  49.302  88.032  1.00 16.67 ? 967  GLY   B N     1 
ATOM   16244 C  CA    . GLY   B  1  969  ? 24.573  49.650  86.674  1.00 17.11 ? 967  GLY   B CA    1 
ATOM   16245 C  C     . GLY   B  1  969  ? 23.675  48.664  85.978  1.00 16.46 ? 967  GLY   B C     1 
ATOM   16246 O  O     . GLY   B  1  969  ? 23.138  48.993  84.916  1.00 16.42 ? 967  GLY   B O     1 
ATOM   16247 N  N     . TYR   B  1  970  ? 23.477  47.480  86.556  1.00 15.77 ? 968  TYR   B N     1 
ATOM   16248 C  CA    . TYR   B  1  970  ? 22.542  46.505  86.024  1.00 14.20 ? 968  TYR   B CA    1 
ATOM   16249 C  C     . TYR   B  1  970  ? 21.137  46.809  86.525  1.00 14.26 ? 968  TYR   B C     1 
ATOM   16250 O  O     . TYR   B  1  970  ? 20.935  47.619  87.433  1.00 17.27 ? 968  TYR   B O     1 
ATOM   16251 C  CB    . TYR   B  1  970  ? 22.982  45.119  86.472  1.00 15.44 ? 968  TYR   B CB    1 
ATOM   16252 C  CG    . TYR   B  1  970  ? 24.178  44.603  85.720  1.00 17.08 ? 968  TYR   B CG    1 
ATOM   16253 C  CD1   . TYR   B  1  970  ? 24.017  44.124  84.432  1.00 18.96 ? 968  TYR   B CD1   1 
ATOM   16254 C  CD2   . TYR   B  1  970  ? 25.455  44.575  86.288  1.00 19.69 ? 968  TYR   B CD2   1 
ATOM   16255 C  CE1   . TYR   B  1  970  ? 25.079  43.623  83.705  1.00 23.45 ? 968  TYR   B CE1   1 
ATOM   16256 C  CE2   . TYR   B  1  970  ? 26.546  44.060  85.544  1.00 21.31 ? 968  TYR   B CE2   1 
ATOM   16257 C  CZ    . TYR   B  1  970  ? 26.325  43.594  84.252  1.00 23.92 ? 968  TYR   B CZ    1 
ATOM   16258 O  OH    . TYR   B  1  970  ? 27.337  43.073  83.460  1.00 29.11 ? 968  TYR   B OH    1 
ATOM   16259 N  N     . GLY   B  1  971  ? 20.154  46.164  85.915  1.00 14.18 ? 969  GLY   B N     1 
ATOM   16260 C  CA    . GLY   B  1  971  ? 18.790  46.387  86.321  1.00 14.54 ? 969  GLY   B CA    1 
ATOM   16261 C  C     . GLY   B  1  971  ? 17.881  45.376  85.664  1.00 13.37 ? 969  GLY   B C     1 
ATOM   16262 O  O     . GLY   B  1  971  ? 16.942  45.748  84.956  1.00 14.00 ? 969  GLY   B O     1 
ATOM   16263 N  N     . LEU   B  1  972  ? 18.144  44.100  85.914  1.00 12.79 ? 970  LEU   B N     1 
ATOM   16264 C  CA    . LEU   B  1  972  ? 17.380  43.026  85.299  1.00 13.43 ? 970  LEU   B CA    1 
ATOM   16265 C  C     . LEU   B  1  972  ? 16.295  42.537  86.249  1.00 12.57 ? 970  LEU   B C     1 
ATOM   16266 O  O     . LEU   B  1  972  ? 15.169  43.032  86.183  1.00 13.93 ? 970  LEU   B O     1 
ATOM   16267 C  CB    . LEU   B  1  972  ? 18.319  41.923  84.794  1.00 14.46 ? 970  LEU   B CB    1 
ATOM   16268 C  CG    . LEU   B  1  972  ? 17.646  40.858  83.947  1.00 13.45 ? 970  LEU   B CG    1 
ATOM   16269 C  CD1   . LEU   B  1  972  ? 16.933  41.488  82.746  1.00 16.70 ? 970  LEU   B CD1   1 
ATOM   16270 C  CD2   . LEU   B  1  972  ? 18.691  39.872  83.484  1.00 16.42 ? 970  LEU   B CD2   1 
ATOM   16271 N  N     . THR   B  1  973  ? 16.599  41.575  87.119  1.00 12.63 ? 971  THR   B N     1 
ATOM   16272 C  CA    . THR   B  1  973  ? 15.594  41.100  88.057  1.00 12.74 ? 971  THR   B CA    1 
ATOM   16273 C  C     . THR   B  1  973  ? 15.923  41.563  89.463  1.00 11.98 ? 971  THR   B C     1 
ATOM   16274 O  O     . THR   B  1  973  ? 17.070  41.845  89.791  1.00 13.76 ? 971  THR   B O     1 
ATOM   16275 C  CB    . THR   B  1  973  ? 15.484  39.578  88.054  1.00 12.11 ? 971  THR   B CB    1 
ATOM   16276 O  OG1   . THR   B  1  973  ? 16.752  39.003  88.386  1.00 13.26 ? 971  THR   B OG1   1 
ATOM   16277 C  CG2   . THR   B  1  973  ? 15.021  39.082  86.692  1.00 14.14 ? 971  THR   B CG2   1 
ATOM   16278 N  N     . PHE   B  1  974  ? 14.877  41.631  90.278  1.00 12.39 ? 972  PHE   B N     1 
ATOM   16279 C  CA    . PHE   B  1  974  ? 15.028  42.059  91.656  1.00 11.71 ? 972  PHE   B CA    1 
ATOM   16280 C  C     . PHE   B  1  974  ? 13.890  41.464  92.463  1.00 12.95 ? 972  PHE   B C     1 
ATOM   16281 O  O     . PHE   B  1  974  ? 12.741  41.501  92.032  1.00 12.62 ? 972  PHE   B O     1 
ATOM   16282 C  CB    . PHE   B  1  974  ? 14.950  43.577  91.755  1.00 13.25 ? 972  PHE   B CB    1 
ATOM   16283 C  CG    . PHE   B  1  974  ? 14.867  44.051  93.174  1.00 12.90 ? 972  PHE   B CG    1 
ATOM   16284 C  CD1   . PHE   B  1  974  ? 16.017  44.177  93.919  1.00 14.20 ? 972  PHE   B CD1   1 
ATOM   16285 C  CD2   . PHE   B  1  974  ? 13.647  44.311  93.757  1.00 14.06 ? 972  PHE   B CD2   1 
ATOM   16286 C  CE1   . PHE   B  1  974  ? 15.959  44.564  95.243  1.00 14.92 ? 972  PHE   B CE1   1 
ATOM   16287 C  CE2   . PHE   B  1  974  ? 13.570  44.693  95.077  1.00 14.61 ? 972  PHE   B CE2   1 
ATOM   16288 C  CZ    . PHE   B  1  974  ? 14.721  44.826  95.814  1.00 15.16 ? 972  PHE   B CZ    1 
ATOM   16289 N  N     . GLY   B  1  975  ? 14.216  40.939  93.638  1.00 13.07 ? 973  GLY   B N     1 
ATOM   16290 C  CA    . GLY   B  1  975  ? 13.225  40.355  94.519  1.00 13.30 ? 973  GLY   B CA    1 
ATOM   16291 C  C     . GLY   B  1  975  ? 13.159  41.053  95.861  1.00 12.96 ? 973  GLY   B C     1 
ATOM   16292 O  O     . GLY   B  1  975  ? 14.154  41.560  96.371  1.00 14.08 ? 973  GLY   B O     1 
ATOM   16293 N  N     . LEU   B  1  976  ? 11.972  41.039  96.437  1.00 13.23 ? 974  LEU   B N     1 
ATOM   16294 C  CA    . LEU   B  1  976  ? 11.768  41.586  97.764  1.00 13.42 ? 974  LEU   B CA    1 
ATOM   16295 C  C     . LEU   B  1  976  ? 10.882  40.611  98.512  1.00 14.35 ? 974  LEU   B C     1 
ATOM   16296 O  O     . LEU   B  1  976  ? 9.796   40.261  98.037  1.00 15.03 ? 974  LEU   B O     1 
ATOM   16297 C  CB    . LEU   B  1  976  ? 11.094  42.954  97.671  1.00 15.35 ? 974  LEU   B CB    1 
ATOM   16298 C  CG    . LEU   B  1  976  ? 10.705  43.583  99.013  1.00 16.05 ? 974  LEU   B CG    1 
ATOM   16299 C  CD1   . LEU   B  1  976  ? 11.943  43.882  99.841  1.00 18.42 ? 974  LEU   B CD1   1 
ATOM   16300 C  CD2   . LEU   B  1  976  ? 9.883   44.843  98.772  1.00 17.57 ? 974  LEU   B CD2   1 
ATOM   16301 N  N     . HIS   B  1  977  ? 11.341  40.175  99.681  1.00 14.75 ? 975  HIS   B N     1 
ATOM   16302 C  CA    . HIS   B  1  977  ? 10.531  39.342  100.559 1.00 15.16 ? 975  HIS   B CA    1 
ATOM   16303 C  C     . HIS   B  1  977  ? 10.223  40.164  101.797 1.00 14.87 ? 975  HIS   B C     1 
ATOM   16304 O  O     . HIS   B  1  977  ? 11.119  40.472  102.591 1.00 15.18 ? 975  HIS   B O     1 
ATOM   16305 C  CB    . HIS   B  1  977  ? 11.230  38.041  100.938 1.00 17.07 ? 975  HIS   B CB    1 
ATOM   16306 C  CG    . HIS   B  1  977  ? 10.956  36.913  100.002 1.00 16.25 ? 975  HIS   B CG    1 
ATOM   16307 N  ND1   . HIS   B  1  977  ? 10.134  35.858  100.335 1.00 23.22 ? 975  HIS   B ND1   1 
ATOM   16308 C  CD2   . HIS   B  1  977  ? 11.379  36.684  98.740  1.00 24.06 ? 975  HIS   B CD2   1 
ATOM   16309 C  CE1   . HIS   B  1  977  ? 10.090  35.011  99.323  1.00 20.48 ? 975  HIS   B CE1   1 
ATOM   16310 N  NE2   . HIS   B  1  977  ? 10.827  35.493  98.342  1.00 22.17 ? 975  HIS   B NE2   1 
ATOM   16311 N  N     . THR   B  1  978  ? 8.959   40.522  101.948 1.00 14.62 ? 976  THR   B N     1 
ATOM   16312 C  CA    . THR   B  1  978  ? 8.492   41.276  103.095 1.00 15.09 ? 976  THR   B CA    1 
ATOM   16313 C  C     . THR   B  1  978  ? 6.990   41.130  103.132 1.00 14.94 ? 976  THR   B C     1 
ATOM   16314 O  O     . THR   B  1  978  ? 6.349   40.913  102.104 1.00 17.34 ? 976  THR   B O     1 
ATOM   16315 C  CB    . THR   B  1  978  ? 8.857   42.759  102.991 1.00 16.70 ? 976  THR   B CB    1 
ATOM   16316 O  OG1   . THR   B  1  978  ? 8.339   43.446  104.130 1.00 16.81 ? 976  THR   B OG1   1 
ATOM   16317 C  CG2   . THR   B  1  978  ? 8.238   43.378  101.774 1.00 20.45 ? 976  THR   B CG2   1 
ATOM   16318 N  N     . ARG   B  1  979  ? 6.438   41.245  104.326 1.00 17.25 ? 977  ARG   B N     1 
ATOM   16319 C  CA    . ARG   B  1  979  ? 4.999   41.287  104.469 1.00 18.22 ? 977  ARG   B CA    1 
ATOM   16320 C  C     . ARG   B  1  979  ? 4.481   42.704  104.590 1.00 18.81 ? 977  ARG   B C     1 
ATOM   16321 O  O     . ARG   B  1  979  ? 3.272   42.887  104.709 1.00 19.65 ? 977  ARG   B O     1 
ATOM   16322 C  CB    . ARG   B  1  979  ? 4.569   40.469  105.683 1.00 21.62 ? 977  ARG   B CB    1 
ATOM   16323 C  CG    . ARG   B  1  979  ? 4.813   38.998  105.483 1.00 26.37 ? 977  ARG   B CG    1 
ATOM   16324 C  CD    . ARG   B  1  979  ? 4.654   38.242  106.775 1.00 33.58 ? 977  ARG   B CD    1 
ATOM   16325 N  NE    . ARG   B  1  979  ? 4.638   36.805  106.548 1.00 37.85 ? 977  ARG   B NE    1 
ATOM   16326 C  CZ    . ARG   B  1  979  ? 4.357   35.909  107.483 1.00 43.17 ? 977  ARG   B CZ    1 
ATOM   16327 N  NH1   . ARG   B  1  979  ? 4.063   36.274  108.721 1.00 35.09 ? 977  ARG   B NH1   1 
ATOM   16328 N  NH2   . ARG   B  1  979  ? 4.370   34.616  107.168 1.00 41.81 ? 977  ARG   B NH2   1 
ATOM   16329 N  N     . LEU   B  1  980  ? 5.355   43.705  104.566 1.00 16.73 ? 978  LEU   B N     1 
ATOM   16330 C  CA    . LEU   B  1  980  ? 5.007   45.055  104.996 1.00 15.92 ? 978  LEU   B CA    1 
ATOM   16331 C  C     . LEU   B  1  980  ? 4.800   45.967  103.799 1.00 16.79 ? 978  LEU   B C     1 
ATOM   16332 O  O     . LEU   B  1  980  ? 5.738   46.205  103.029 1.00 16.70 ? 978  LEU   B O     1 
ATOM   16333 C  CB    . LEU   B  1  980  ? 6.116   45.617  105.877 1.00 16.08 ? 978  LEU   B CB    1 
ATOM   16334 C  CG    . LEU   B  1  980  ? 6.445   44.715  107.064 1.00 18.76 ? 978  LEU   B CG    1 
ATOM   16335 C  CD1   . LEU   B  1  980  ? 7.554   45.343  107.911 1.00 19.39 ? 978  LEU   B CD1   1 
ATOM   16336 C  CD2   . LEU   B  1  980  ? 5.210   44.445  107.901 1.00 18.66 ? 978  LEU   B CD2   1 
ATOM   16337 N  N     . ASP   B  1  981  ? 3.586   46.511  103.674 1.00 16.93 ? 979  ASP   B N     1 
ATOM   16338 C  CA    . ASP   B  1  981  ? 3.265   47.347  102.520 1.00 17.31 ? 979  ASP   B CA    1 
ATOM   16339 C  C     . ASP   B  1  981  ? 4.175   48.560  102.422 1.00 17.99 ? 979  ASP   B C     1 
ATOM   16340 O  O     . ASP   B  1  981  ? 4.507   48.987  101.315 1.00 16.53 ? 979  ASP   B O     1 
ATOM   16341 C  CB    . ASP   B  1  981  ? 1.812   47.813  102.565 1.00 18.98 ? 979  ASP   B CB    1 
ATOM   16342 C  CG    . ASP   B  1  981  ? 0.829   46.716  102.262 1.00 20.92 ? 979  ASP   B CG    1 
ATOM   16343 O  OD1   . ASP   B  1  981  ? 1.205   45.675  101.687 1.00 22.28 ? 979  ASP   B OD1   1 
ATOM   16344 O  OD2   . ASP   B  1  981  ? -0.355  46.926  102.617 1.00 23.73 ? 979  ASP   B OD2   1 
ATOM   16345 N  N     . GLU   B  1  982  ? 4.565   49.156  103.547 1.00 16.73 ? 980  GLU   B N     1 
ATOM   16346 C  CA    . GLU   B  1  982  ? 5.431   50.330  103.461 1.00 17.35 ? 980  GLU   B CA    1 
ATOM   16347 C  C     . GLU   B  1  982  ? 6.779   49.964  102.865 1.00 17.10 ? 980  GLU   B C     1 
ATOM   16348 O  O     . GLU   B  1  982  ? 7.355   50.733  102.089 1.00 17.19 ? 980  GLU   B O     1 
ATOM   16349 C  CB    . GLU   B  1  982  ? 5.628   50.972  104.832 1.00 18.35 ? 980  GLU   B CB    1 
ATOM   16350 C  CG    . GLU   B  1  982  ? 6.569   52.171  104.784 1.00 22.07 ? 980  GLU   B CG    1 
ATOM   16351 C  CD    . GLU   B  1  982  ? 7.065   52.613  106.151 1.00 25.60 ? 980  GLU   B CD    1 
ATOM   16352 O  OE1   . GLU   B  1  982  ? 7.401   51.747  106.991 1.00 31.04 ? 980  GLU   B OE1   1 
ATOM   16353 O  OE2   . GLU   B  1  982  ? 7.126   53.832  106.388 1.00 25.96 ? 980  GLU   B OE2   1 
ATOM   16354 N  N     . THR   B  1  983  ? 7.298   48.796  103.229 1.00 15.68 ? 981  THR   B N     1 
ATOM   16355 C  CA    . THR   B  1  983  ? 8.581   48.376  102.691 1.00 15.74 ? 981  THR   B CA    1 
ATOM   16356 C  C     . THR   B  1  983  ? 8.458   48.074  101.208 1.00 14.98 ? 981  THR   B C     1 
ATOM   16357 O  O     . THR   B  1  983  ? 9.333   48.448  100.418 1.00 16.25 ? 981  THR   B O     1 
ATOM   16358 C  CB    . THR   B  1  983  ? 9.077   47.167  103.471 1.00 18.00 ? 981  THR   B CB    1 
ATOM   16359 O  OG1   . THR   B  1  983  ? 9.296   47.568  104.825 1.00 18.43 ? 981  THR   B OG1   1 
ATOM   16360 C  CG2   . THR   B  1  983  ? 10.389  46.675  102.890 1.00 17.39 ? 981  THR   B CG2   1 
ATOM   16361 N  N     . ILE   B  1  984  ? 7.349   47.449  100.810 1.00 15.25 ? 982  ILE   B N     1 
ATOM   16362 C  CA    . ILE   B  1  984  ? 7.109   47.185  99.397  1.00 15.25 ? 982  ILE   B CA    1 
ATOM   16363 C  C     . ILE   B  1  984  ? 7.047   48.486  98.618  1.00 14.93 ? 982  ILE   B C     1 
ATOM   16364 O  O     . ILE   B  1  984  ? 7.686   48.628  97.566  1.00 16.10 ? 982  ILE   B O     1 
ATOM   16365 C  CB    . ILE   B  1  984  ? 5.826   46.361  99.212  1.00 15.28 ? 982  ILE   B CB    1 
ATOM   16366 C  CG1   . ILE   B  1  984  ? 6.002   44.967  99.788  1.00 18.70 ? 982  ILE   B CG1   1 
ATOM   16367 C  CG2   . ILE   B  1  984  ? 5.471   46.265  97.741  1.00 17.86 ? 982  ILE   B CG2   1 
ATOM   16368 C  CD1   . ILE   B  1  984  ? 4.709   44.207  99.904  1.00 18.79 ? 982  ILE   B CD1   1 
ATOM   16369 N  N     . ALA   B  1  985  ? 6.300   49.468  99.131  1.00 15.76 ? 983  ALA   B N     1 
ATOM   16370 C  CA    . ALA   B  1  985  ? 6.178   50.728  98.407  1.00 16.76 ? 983  ALA   B CA    1 
ATOM   16371 C  C     . ALA   B  1  985  ? 7.521   51.426  98.314  1.00 15.35 ? 983  ALA   B C     1 
ATOM   16372 O  O     . ALA   B  1  985  ? 7.909   51.900  97.238  1.00 16.94 ? 983  ALA   B O     1 
ATOM   16373 C  CB    . ALA   B  1  985  ? 5.149   51.633  99.090  1.00 16.67 ? 983  ALA   B CB    1 
ATOM   16374 N  N     . HIS   B  1  986  ? 8.262   51.465  99.424  1.00 16.02 ? 984  HIS   B N     1 
ATOM   16375 C  CA    . HIS   B  1  986  ? 9.565   52.113  99.426  1.00 16.71 ? 984  HIS   B CA    1 
ATOM   16376 C  C     . HIS   B  1  986  ? 10.485  51.438  98.421  1.00 15.82 ? 984  HIS   B C     1 
ATOM   16377 O  O     . HIS   B  1  986  ? 11.023  52.077  97.508  1.00 17.33 ? 984  HIS   B O     1 
ATOM   16378 C  CB    . HIS   B  1  986  ? 10.154  52.030  100.835 1.00 18.24 ? 984  HIS   B CB    1 
ATOM   16379 C  CG    . HIS   B  1  986  ? 11.537  52.589  100.969 1.00 18.70 ? 984  HIS   B CG    1 
ATOM   16380 N  ND1   . HIS   B  1  986  ? 12.142  52.751  102.195 1.00 24.95 ? 984  HIS   B ND1   1 
ATOM   16381 C  CD2   . HIS   B  1  986  ? 12.431  53.021  100.050 1.00 19.66 ? 984  HIS   B CD2   1 
ATOM   16382 C  CE1   . HIS   B  1  986  ? 13.352  53.256  102.026 1.00 23.45 ? 984  HIS   B CE1   1 
ATOM   16383 N  NE2   . HIS   B  1  986  ? 13.554  53.425  100.733 1.00 20.53 ? 984  HIS   B NE2   1 
ATOM   16384 N  N     . VAL   B  1  987  ? 10.672  50.134  98.570  1.00 15.57 ? 985  VAL   B N     1 
ATOM   16385 C  CA    . VAL   B  1  987  ? 11.681  49.456  97.769  1.00 15.87 ? 985  VAL   B CA    1 
ATOM   16386 C  C     . VAL   B  1  987  ? 11.310  49.476  96.297  1.00 16.56 ? 985  VAL   B C     1 
ATOM   16387 O  O     . VAL   B  1  987  ? 12.159  49.751  95.444  1.00 17.24 ? 985  VAL   B O     1 
ATOM   16388 C  CB    . VAL   B  1  987  ? 11.915  48.033  98.286  1.00 16.34 ? 985  VAL   B CB    1 
ATOM   16389 C  CG1   . VAL   B  1  987  ? 12.784  47.263  97.317  1.00 17.34 ? 985  VAL   B CG1   1 
ATOM   16390 C  CG2   . VAL   B  1  987  ? 12.575  48.086  99.650  1.00 15.94 ? 985  VAL   B CG2   1 
ATOM   16391 N  N     . THR   B  1  988  ? 10.049  49.192  95.965  1.00 15.36 ? 986  THR   B N     1 
ATOM   16392 C  CA    . THR   B  1  988  ? 9.686   49.170  94.548  1.00 16.81 ? 986  THR   B CA    1 
ATOM   16393 C  C     . THR   B  1  988  ? 9.727   50.568  93.939  1.00 18.07 ? 986  THR   B C     1 
ATOM   16394 O  O     . THR   B  1  988  ? 9.957   50.698  92.732  1.00 24.53 ? 986  THR   B O     1 
ATOM   16395 C  CB    . THR   B  1  988  ? 8.341   48.470  94.304  1.00 19.31 ? 986  THR   B CB    1 
ATOM   16396 O  OG1   . THR   B  1  988  ? 7.301   49.174  94.969  1.00 21.06 ? 986  THR   B OG1   1 
ATOM   16397 C  CG2   . THR   B  1  988  ? 8.366   47.046  94.791  1.00 21.01 ? 986  THR   B CG2   1 
ATOM   16398 N  N     . SER   B  1  989  ? 9.551   51.616  94.743  1.00 19.13 ? 987  SER   B N     1 
ATOM   16399 C  CA    . SER   B  1  989  ? 9.641   52.974  94.217  1.00 20.86 ? 987  SER   B CA    1 
ATOM   16400 C  C     . SER   B  1  989  ? 11.078  53.382  93.922  1.00 21.41 ? 987  SER   B C     1 
ATOM   16401 O  O     . SER   B  1  989  ? 11.292  54.288  93.109  1.00 28.38 ? 987  SER   B O     1 
ATOM   16402 C  CB    . SER   B  1  989  ? 8.972   53.990  95.158  1.00 24.39 ? 987  SER   B CB    1 
ATOM   16403 O  OG    . SER   B  1  989  ? 9.714   54.219  96.345  1.00 30.76 ? 987  SER   B OG    1 
ATOM   16404 N  N     . ARG   B  1  990  ? 12.065  52.728  94.535  1.00 18.01 ? 988  ARG   B N     1 
ATOM   16405 C  CA    . ARG   B  1  990  ? 13.452  53.174  94.460  1.00 18.31 ? 988  ARG   B CA    1 
ATOM   16406 C  C     . ARG   B  1  990  ? 14.348  52.234  93.672  1.00 16.57 ? 988  ARG   B C     1 
ATOM   16407 O  O     . ARG   B  1  990  ? 15.377  52.665  93.147  1.00 16.78 ? 988  ARG   B O     1 
ATOM   16408 C  CB    . ARG   B  1  990  ? 14.032  53.339  95.868  1.00 20.40 ? 988  ARG   B CB    1 
ATOM   16409 C  CG    . ARG   B  1  990  ? 13.180  54.183  96.802  1.00 29.87 ? 988  ARG   B CG    1 
ATOM   16410 C  CD    . ARG   B  1  990  ? 13.380  55.659  96.576  1.00 26.32 ? 988  ARG   B CD    1 
ATOM   16411 N  NE    . ARG   B  1  990  ? 14.513  56.188  97.330  1.00 19.68 ? 988  ARG   B NE    1 
ATOM   16412 C  CZ    . ARG   B  1  990  ? 14.912  57.448  97.249  1.00 22.08 ? 988  ARG   B CZ    1 
ATOM   16413 N  NH1   . ARG   B  1  990  ? 14.325  58.306  96.431  1.00 24.08 ? 988  ARG   B NH1   1 
ATOM   16414 N  NH2   . ARG   B  1  990  ? 15.924  57.856  98.003  1.00 21.87 ? 988  ARG   B NH2   1 
ATOM   16415 N  N     . ILE   B  1  991  ? 14.004  50.954  93.587  1.00 15.11 ? 989  ILE   B N     1 
ATOM   16416 C  CA    . ILE   B  1  991  ? 14.792  50.025  92.788  1.00 16.45 ? 989  ILE   B CA    1 
ATOM   16417 C  C     . ILE   B  1  991  ? 14.629  50.369  91.313  1.00 16.29 ? 989  ILE   B C     1 
ATOM   16418 O  O     . ILE   B  1  991  ? 13.584  50.865  90.879  1.00 17.71 ? 989  ILE   B O     1 
ATOM   16419 C  CB    . ILE   B  1  991  ? 14.330  48.589  93.094  1.00 16.77 ? 989  ILE   B CB    1 
ATOM   16420 C  CG1   . ILE   B  1  991  ? 15.315  47.565  92.550  1.00 19.13 ? 989  ILE   B CG1   1 
ATOM   16421 C  CG2   . ILE   B  1  991  ? 12.956  48.326  92.507  1.00 19.79 ? 989  ILE   B CG2   1 
ATOM   16422 C  CD1   . ILE   B  1  991  ? 16.658  47.674  93.201  1.00 22.04 ? 989  ILE   B CD1   1 
ATOM   16423 N  N     . LYS   B  1  992  ? 15.670  50.126  90.534  1.00 14.91 ? 990  LYS   B N     1 
ATOM   16424 C  CA    . LYS   B  1  992  ? 15.622  50.413  89.101  1.00 15.69 ? 990  LYS   B CA    1 
ATOM   16425 C  C     . LYS   B  1  992  ? 15.941  49.113  88.383  1.00 16.12 ? 990  LYS   B C     1 
ATOM   16426 O  O     . LYS   B  1  992  ? 17.074  48.871  87.977  1.00 20.99 ? 990  LYS   B O     1 
ATOM   16427 C  CB    . LYS   B  1  992  ? 16.639  51.510  88.780  1.00 17.67 ? 990  LYS   B CB    1 
ATOM   16428 C  CG    . LYS   B  1  992  ? 16.310  52.840  89.455  1.00 19.45 ? 990  LYS   B CG    1 
ATOM   16429 C  CD    . LYS   B  1  992  ? 17.386  53.891  89.157  1.00 27.55 ? 990  LYS   B CD    1 
ATOM   16430 C  CE    . LYS   B  1  992  ? 17.672  53.989  87.659  1.00 36.45 ? 990  LYS   B CE    1 
ATOM   16431 N  NZ    . LYS   B  1  992  ? 18.912  54.762  87.336  1.00 40.29 ? 990  LYS   B NZ    1 
ATOM   16432 N  N     . ALA   B  1  993  ? 14.944  48.255  88.250  1.00 15.95 ? 991  ALA   B N     1 
ATOM   16433 C  CA    . ALA   B  1  993  ? 15.125  46.995  87.554  1.00 14.80 ? 991  ALA   B CA    1 
ATOM   16434 C  C     . ALA   B  1  993  ? 13.885  46.723  86.726  1.00 15.25 ? 991  ALA   B C     1 
ATOM   16435 O  O     . ALA   B  1  993  ? 12.787  47.188  87.054  1.00 16.34 ? 991  ALA   B O     1 
ATOM   16436 C  CB    . ALA   B  1  993  ? 15.337  45.829  88.520  1.00 17.02 ? 991  ALA   B CB    1 
ATOM   16437 N  N     . GLY   B  1  994  ? 14.066  45.962  85.646  1.00 13.76 ? 992  GLY   B N     1 
ATOM   16438 C  CA    . GLY   B  1  994  ? 12.946  45.763  84.744  1.00 13.40 ? 992  GLY   B CA    1 
ATOM   16439 C  C     . GLY   B  1  994  ? 11.950  44.715  85.177  1.00 13.02 ? 992  GLY   B C     1 
ATOM   16440 O  O     . GLY   B  1  994  ? 10.809  44.754  84.725  1.00 12.72 ? 992  GLY   B O     1 
ATOM   16441 N  N     . ASN   B  1  995  ? 12.341  43.791  86.046  1.00 13.25 ? 993  ASN   B N     1 
ATOM   16442 C  CA    . ASN   B  1  995  ? 11.469  42.706  86.470  1.00 12.57 ? 993  ASN   B CA    1 
ATOM   16443 C  C     . ASN   B  1  995  ? 11.581  42.608  87.973  1.00 12.05 ? 993  ASN   B C     1 
ATOM   16444 O  O     . ASN   B  1  995  ? 12.647  42.274  88.498  1.00 13.10 ? 993  ASN   B O     1 
ATOM   16445 C  CB    . ASN   B  1  995  ? 11.856  41.387  85.810  1.00 13.10 ? 993  ASN   B CB    1 
ATOM   16446 C  CG    . ASN   B  1  995  ? 11.305  41.284  84.428  1.00 13.09 ? 993  ASN   B CG    1 
ATOM   16447 O  OD1   . ASN   B  1  995  ? 11.905  41.786  83.472  1.00 13.10 ? 993  ASN   B OD1   1 
ATOM   16448 N  ND2   . ASN   B  1  995  ? 10.130  40.680  84.311  1.00 13.97 ? 993  ASN   B ND2   1 
ATOM   16449 N  N     . LEU   B  1  996  ? 10.489  42.910  88.645  1.00 12.81 ? 994  LEU   B N     1 
ATOM   16450 C  CA    . LEU   B  1  996  ? 10.413  42.891  90.094  1.00 12.46 ? 994  LEU   B CA    1 
ATOM   16451 C  C     . LEU   B  1  996  ? 9.562   41.713  90.511  1.00 13.18 ? 994  LEU   B C     1 
ATOM   16452 O  O     . LEU   B  1  996  ? 8.598   41.354  89.823  1.00 13.10 ? 994  LEU   B O     1 
ATOM   16453 C  CB    . LEU   B  1  996  ? 9.757   44.159  90.618  1.00 13.57 ? 994  LEU   B CB    1 
ATOM   16454 C  CG    . LEU   B  1  996  ? 10.325  45.454  90.043  1.00 14.78 ? 994  LEU   B CG    1 
ATOM   16455 C  CD1   . LEU   B  1  996  ? 9.614   46.663  90.648  1.00 18.07 ? 994  LEU   B CD1   1 
ATOM   16456 C  CD2   . LEU   B  1  996  ? 11.830  45.534  90.226  1.00 16.22 ? 994  LEU   B CD2   1 
ATOM   16457 N  N     . TYR   B  1  997  ? 9.886   41.146  91.673  1.00 12.86 ? 995  TYR   B N     1 
ATOM   16458 C  CA    . TYR   B  1  997  ? 9.201   39.966  92.181  1.00 13.14 ? 995  TYR   B CA    1 
ATOM   16459 C  C     . TYR   B  1  997  ? 9.037   40.135  93.673  1.00 12.91 ? 995  TYR   B C     1 
ATOM   16460 O  O     . TYR   B  1  997  ? 10.013  40.415  94.369  1.00 14.78 ? 995  TYR   B O     1 
ATOM   16461 C  CB    . TYR   B  1  997  ? 10.004  38.695  91.915  1.00 13.50 ? 995  TYR   B CB    1 
ATOM   16462 C  CG    . TYR   B  1  997  ? 10.382  38.532  90.451  1.00 13.40 ? 995  TYR   B CG    1 
ATOM   16463 C  CD1   . TYR   B  1  997  ? 11.502  39.152  89.934  1.00 13.73 ? 995  TYR   B CD1   1 
ATOM   16464 C  CD2   . TYR   B  1  997  ? 9.609   37.772  89.600  1.00 14.91 ? 995  TYR   B CD2   1 
ATOM   16465 C  CE1   . TYR   B  1  997  ? 11.844  39.022  88.617  1.00 14.59 ? 995  TYR   B CE1   1 
ATOM   16466 C  CE2   . TYR   B  1  997  ? 9.946   37.642  88.264  1.00 12.85 ? 995  TYR   B CE2   1 
ATOM   16467 C  CZ    . TYR   B  1  997  ? 11.067  38.260  87.795  1.00 13.58 ? 995  TYR   B CZ    1 
ATOM   16468 O  OH    . TYR   B  1  997  ? 11.436  38.144  86.463  1.00 15.86 ? 995  TYR   B OH    1 
ATOM   16469 N  N     . ILE   B  1  998  ? 7.812   39.998  94.151  1.00 13.34 ? 996  ILE   B N     1 
ATOM   16470 C  CA    . ILE   B  1  998  ? 7.502   40.210  95.556  1.00 13.36 ? 996  ILE   B CA    1 
ATOM   16471 C  C     . ILE   B  1  998  ? 7.062   38.883  96.144  1.00 13.75 ? 996  ILE   B C     1 
ATOM   16472 O  O     . ILE   B  1  998  ? 6.055   38.304  95.723  1.00 14.34 ? 996  ILE   B O     1 
ATOM   16473 C  CB    . ILE   B  1  998  ? 6.409   41.269  95.748  1.00 15.54 ? 996  ILE   B CB    1 
ATOM   16474 C  CG1   . ILE   B  1  998  ? 6.788   42.598  95.084  1.00 18.30 ? 996  ILE   B CG1   1 
ATOM   16475 C  CG2   . ILE   B  1  998  ? 6.134   41.464  97.232  1.00 17.71 ? 996  ILE   B CG2   1 
ATOM   16476 C  CD1   . ILE   B  1  998  ? 8.102   43.158  95.487  1.00 23.48 ? 996  ILE   B CD1   1 
ATOM   16477 N  N     . ASN   B  1  999  ? 7.812   38.420  97.141  1.00 13.01 ? 997  ASN   B N     1 
ATOM   16478 C  CA    . ASN   B  1  999  ? 7.457   37.221  97.905  1.00 14.58 ? 997  ASN   B CA    1 
ATOM   16479 C  C     . ASN   B  1  999  ? 7.428   35.971  97.040  1.00 14.00 ? 997  ASN   B C     1 
ATOM   16480 O  O     . ASN   B  1  999  ? 6.615   35.073  97.236  1.00 15.31 ? 997  ASN   B O     1 
ATOM   16481 C  CB    . ASN   B  1  999  ? 6.172   37.427  98.697  1.00 14.24 ? 997  ASN   B CB    1 
ATOM   16482 C  CG    . ASN   B  1  999  ? 6.349   38.460  99.767  1.00 14.43 ? 997  ASN   B CG    1 
ATOM   16483 O  OD1   . ASN   B  1  999  ? 7.435   38.584  100.329 1.00 15.78 ? 997  ASN   B OD1   1 
ATOM   16484 N  ND2   . ASN   B  1  999  ? 5.298   39.210  100.060 1.00 15.32 ? 997  ASN   B ND2   1 
ATOM   16485 N  N     . ARG   B  1  1000 ? 8.350   35.905  96.093  1.00 14.07 ? 998  ARG   B N     1 
ATOM   16486 C  CA    . ARG   B  1  1000 ? 8.463   34.750  95.217  1.00 12.83 ? 998  ARG   B CA    1 
ATOM   16487 C  C     . ARG   B  1  1000 ? 9.881   34.717  94.668  1.00 14.67 ? 998  ARG   B C     1 
ATOM   16488 O  O     . ARG   B  1  1000 ? 10.715  35.560  94.998  1.00 16.03 ? 998  ARG   B O     1 
ATOM   16489 C  CB    . ARG   B  1  1000 ? 7.435   34.818  94.087  1.00 13.60 ? 998  ARG   B CB    1 
ATOM   16490 C  CG    . ARG   B  1  1000 ? 7.464   36.165  93.350  1.00 14.56 ? 998  ARG   B CG    1 
ATOM   16491 C  CD    . ARG   B  1  1000 ? 6.929   36.014  91.926  1.00 14.93 ? 998  ARG   B CD    1 
ATOM   16492 N  NE    . ARG   B  1  1000 ? 7.823   35.176  91.146  1.00 13.90 ? 998  ARG   B NE    1 
ATOM   16493 C  CZ    . ARG   B  1  1000 ? 7.510   34.698  89.955  1.00 13.59 ? 998  ARG   B CZ    1 
ATOM   16494 N  NH1   . ARG   B  1  1000 ? 6.361   35.011  89.374  1.00 15.54 ? 998  ARG   B NH1   1 
ATOM   16495 N  NH2   . ARG   B  1  1000 ? 8.364   33.885  89.343  1.00 14.98 ? 998  ARG   B NH2   1 
ATOM   16496 N  N     . ASN   B  1  1001 ? 10.168  33.706  93.857  1.00 13.71 ? 999  ASN   B N     1 
ATOM   16497 C  CA    . ASN   B  1  1001 ? 11.470  33.660  93.208  1.00 14.85 ? 999  ASN   B CA    1 
ATOM   16498 C  C     . ASN   B  1  1001 ? 11.595  34.796  92.187  1.00 13.80 ? 999  ASN   B C     1 
ATOM   16499 O  O     . ASN   B  1  1001 ? 10.613  35.446  91.821  1.00 14.22 ? 999  ASN   B O     1 
ATOM   16500 C  CB    . ASN   B  1  1001 ? 11.719  32.276  92.600  1.00 15.15 ? 999  ASN   B CB    1 
ATOM   16501 C  CG    . ASN   B  1  1001 ? 10.868  31.994  91.382  1.00 16.64 ? 999  ASN   B CG    1 
ATOM   16502 O  OD1   . ASN   B  1  1001 ? 10.758  32.806  90.483  1.00 15.55 ? 999  ASN   B OD1   1 
ATOM   16503 N  ND2   . ASN   B  1  1001 ? 10.274  30.814  91.352  1.00 25.19 ? 999  ASN   B ND2   1 
ATOM   16504 N  N     . ILE   B  1  1002 ? 12.814  35.022  91.713  1.00 13.74 ? 1000 ILE   B N     1 
ATOM   16505 C  CA    . ILE   B  1  1002 ? 13.067  36.135  90.801  1.00 13.32 ? 1000 ILE   B CA    1 
ATOM   16506 C  C     . ILE   B  1  1002 ? 13.369  35.668  89.382  1.00 14.91 ? 1000 ILE   B C     1 
ATOM   16507 O  O     . ILE   B  1  1002 ? 13.981  36.403  88.615  1.00 14.80 ? 1000 ILE   B O     1 
ATOM   16508 C  CB    . ILE   B  1  1002 ? 14.148  37.090  91.328  1.00 13.80 ? 1000 ILE   B CB    1 
ATOM   16509 C  CG1   . ILE   B  1  1002 ? 15.533  36.428  91.337  1.00 14.08 ? 1000 ILE   B CG1   1 
ATOM   16510 C  CG2   . ILE   B  1  1002 ? 13.754  37.617  92.696  1.00 14.07 ? 1000 ILE   B CG2   1 
ATOM   16511 C  CD1   . ILE   B  1  1002 ? 16.636  37.421  91.600  1.00 13.80 ? 1000 ILE   B CD1   1 
ATOM   16512 N  N     . ILE   B  1  1003 ? 12.935  34.474  89.012  1.00 15.35 ? 1001 ILE   B N     1 
ATOM   16513 C  CA    . ILE   B  1  1003 ? 13.303  33.940  87.709  1.00 15.02 ? 1001 ILE   B CA    1 
ATOM   16514 C  C     . ILE   B  1  1003 ? 12.116  33.883  86.754  1.00 17.49 ? 1001 ILE   B C     1 
ATOM   16515 O  O     . ILE   B  1  1003 ? 12.229  33.320  85.660  1.00 18.94 ? 1001 ILE   B O     1 
ATOM   16516 C  CB    . ILE   B  1  1003 ? 14.045  32.607  87.844  1.00 17.40 ? 1001 ILE   B CB    1 
ATOM   16517 C  CG1   . ILE   B  1  1003 ? 13.188  31.597  88.592  1.00 21.71 ? 1001 ILE   B CG1   1 
ATOM   16518 C  CG2   . ILE   B  1  1003 ? 15.369  32.844  88.565  1.00 17.95 ? 1001 ILE   B CG2   1 
ATOM   16519 C  CD1   . ILE   B  1  1003 ? 13.580  30.193  88.290  1.00 28.32 ? 1001 ILE   B CD1   1 
ATOM   16520 N  N     . GLY   B  1  1004 ? 10.995  34.508  87.110  1.00 15.37 ? 1002 GLY   B N     1 
ATOM   16521 C  CA    . GLY   B  1  1004 ? 9.796   34.425  86.292  1.00 17.61 ? 1002 GLY   B CA    1 
ATOM   16522 C  C     . GLY   B  1  1004 ? 9.925   35.220  85.009  1.00 16.78 ? 1002 GLY   B C     1 
ATOM   16523 O  O     . GLY   B  1  1004 ? 10.251  36.412  85.014  1.00 17.38 ? 1002 GLY   B O     1 
ATOM   16524 N  N     . ALA   B  1  1005 ? 9.650   34.564  83.896  1.00 16.25 ? 1003 ALA   B N     1 
ATOM   16525 C  CA    . ALA   B  1  1005 ? 9.684   35.229  82.612  1.00 16.24 ? 1003 ALA   B CA    1 
ATOM   16526 C  C     . ALA   B  1  1005 ? 8.520   34.745  81.787  1.00 17.37 ? 1003 ALA   B C     1 
ATOM   16527 O  O     . ALA   B  1  1005 ? 8.627   34.594  80.567  1.00 16.29 ? 1003 ALA   B O     1 
ATOM   16528 C  CB    . ALA   B  1  1005 ? 11.010  34.991  81.891  1.00 15.34 ? 1003 ALA   B CB    1 
ATOM   16529 N  N     . VAL   B  1  1006 ? 7.376   34.507  82.434  1.00 13.88 ? 1004 VAL   B N     1 
ATOM   16530 C  CA    . VAL   B  1  1006 ? 6.233   33.957  81.716  1.00 14.47 ? 1004 VAL   B CA    1 
ATOM   16531 C  C     . VAL   B  1  1006 ? 5.827   34.945  80.638  1.00 14.35 ? 1004 VAL   B C     1 
ATOM   16532 O  O     . VAL   B  1  1006 ? 5.563   36.121  80.918  1.00 14.48 ? 1004 VAL   B O     1 
ATOM   16533 C  CB    . VAL   B  1  1006 ? 5.091   33.623  82.674  1.00 15.23 ? 1004 VAL   B CB    1 
ATOM   16534 C  CG1   . VAL   B  1  1006 ? 3.887   33.136  81.868  1.00 16.40 ? 1004 VAL   B CG1   1 
ATOM   16535 C  CG2   . VAL   B  1  1006 ? 5.533   32.538  83.653  1.00 17.06 ? 1004 VAL   B CG2   1 
ATOM   16536 N  N     . VAL   B  1  1007 ? 5.805   34.465  79.392  1.00 14.63 ? 1005 VAL   B N     1 
ATOM   16537 C  CA    . VAL   B  1  1007 ? 5.567   35.335  78.255  1.00 14.38 ? 1005 VAL   B CA    1 
ATOM   16538 C  C     . VAL   B  1  1007 ? 4.216   36.017  78.398  1.00 14.50 ? 1005 VAL   B C     1 
ATOM   16539 O  O     . VAL   B  1  1007 ? 3.203   35.383  78.710  1.00 14.76 ? 1005 VAL   B O     1 
ATOM   16540 C  CB    . VAL   B  1  1007 ? 5.655   34.508  76.973  1.00 14.65 ? 1005 VAL   B CB    1 
ATOM   16541 C  CG1   . VAL   B  1  1007 ? 5.339   35.384  75.795  1.00 15.42 ? 1005 VAL   B CG1   1 
ATOM   16542 C  CG2   . VAL   B  1  1007 ? 7.033   33.911  76.817  1.00 15.01 ? 1005 VAL   B CG2   1 
ATOM   16543 N  N     . GLY   B  1  1008 ? 4.208   37.331  78.216  1.00 13.95 ? 1006 GLY   B N     1 
ATOM   16544 C  CA    . GLY   B  1  1008 ? 2.982   38.100  78.314  1.00 14.86 ? 1006 GLY   B CA    1 
ATOM   16545 C  C     . GLY   B  1  1008 ? 2.404   38.209  79.702  1.00 14.94 ? 1006 GLY   B C     1 
ATOM   16546 O  O     . GLY   B  1  1008 ? 1.305   38.746  79.857  1.00 16.76 ? 1006 GLY   B O     1 
ATOM   16547 N  N     . VAL   B  1  1009 ? 3.113   37.699  80.700  1.00 13.97 ? 1007 VAL   B N     1 
ATOM   16548 C  CA    . VAL   B  1  1009 ? 2.701   37.768  82.097  1.00 15.14 ? 1007 VAL   B CA    1 
ATOM   16549 C  C     . VAL   B  1  1009 ? 3.756   38.471  82.935  1.00 15.27 ? 1007 VAL   B C     1 
ATOM   16550 O  O     . VAL   B  1  1009 ? 3.451   39.412  83.672  1.00 15.67 ? 1007 VAL   B O     1 
ATOM   16551 C  CB    . VAL   B  1  1009 ? 2.389   36.365  82.667  1.00 15.48 ? 1007 VAL   B CB    1 
ATOM   16552 C  CG1   . VAL   B  1  1009 ? 1.898   36.484  84.091  1.00 15.42 ? 1007 VAL   B CG1   1 
ATOM   16553 C  CG2   . VAL   B  1  1009 ? 1.321   35.678  81.822  1.00 15.33 ? 1007 VAL   B CG2   1 
ATOM   16554 N  N     . GLN   B  1  1010 ? 5.017   38.051  82.800  1.00 14.39 ? 1008 GLN   B N     1 
ATOM   16555 C  CA    . GLN   B  1  1010 ? 6.177   38.855  83.193  1.00 14.31 ? 1008 GLN   B CA    1 
ATOM   16556 C  C     . GLN   B  1  1010 ? 6.987   39.138  81.935  1.00 14.34 ? 1008 GLN   B C     1 
ATOM   16557 O  O     . GLN   B  1  1010 ? 8.012   38.490  81.704  1.00 15.85 ? 1008 GLN   B O     1 
ATOM   16558 C  CB    . GLN   B  1  1010 ? 7.063   38.161  84.230  1.00 14.63 ? 1008 GLN   B CB    1 
ATOM   16559 C  CG    . GLN   B  1  1010 ? 6.354   37.788  85.520  1.00 16.72 ? 1008 GLN   B CG    1 
ATOM   16560 C  CD    . GLN   B  1  1010 ? 5.945   36.340  85.566  1.00 15.76 ? 1008 GLN   B CD    1 
ATOM   16561 O  OE1   . GLN   B  1  1010 ? 6.654   35.458  85.095  1.00 15.80 ? 1008 GLN   B OE1   1 
ATOM   16562 N  NE2   . GLN   B  1  1010 ? 4.791   36.081  86.169  1.00 15.26 ? 1008 GLN   B NE2   1 
ATOM   16563 N  N     . PRO   B  1  1011 ? 6.546   40.079  81.096  1.00 13.26 ? 1009 PRO   B N     1 
ATOM   16564 C  CA    . PRO   B  1  1011 ? 7.403   40.557  80.005  1.00 15.29 ? 1009 PRO   B CA    1 
ATOM   16565 C  C     . PRO   B  1  1011 ? 8.773   40.838  80.587  1.00 13.48 ? 1009 PRO   B C     1 
ATOM   16566 O  O     . PRO   B  1  1011 ? 8.894   41.459  81.642  1.00 12.61 ? 1009 PRO   B O     1 
ATOM   16567 C  CB    . PRO   B  1  1011 ? 6.711   41.848  79.565  1.00 14.82 ? 1009 PRO   B CB    1 
ATOM   16568 C  CG    . PRO   B  1  1011 ? 5.277   41.603  79.877  1.00 16.25 ? 1009 PRO   B CG    1 
ATOM   16569 C  CD    . PRO   B  1  1011 ? 5.305   40.855  81.194  1.00 16.27 ? 1009 PRO   B CD    1 
ATOM   16570 N  N     . PHE   B  1  1012 ? 9.801   40.321  79.945  1.00 13.10 ? 1010 PHE   B N     1 
ATOM   16571 C  CA    . PHE   B  1  1012 ? 11.075  40.169  80.608  1.00 12.68 ? 1010 PHE   B CA    1 
ATOM   16572 C  C     . PHE   B  1  1012 ? 12.128  41.024  79.929  1.00 13.55 ? 1010 PHE   B C     1 
ATOM   16573 O  O     . PHE   B  1  1012 ? 12.284  40.982  78.708  1.00 14.13 ? 1010 PHE   B O     1 
ATOM   16574 C  CB    . PHE   B  1  1012 ? 11.527  38.707  80.603  1.00 13.79 ? 1010 PHE   B CB    1 
ATOM   16575 C  CG    . PHE   B  1  1012 ? 12.739  38.497  81.435  1.00 12.50 ? 1010 PHE   B CG    1 
ATOM   16576 C  CD1   . PHE   B  1  1012 ? 12.619  38.293  82.799  1.00 14.24 ? 1010 PHE   B CD1   1 
ATOM   16577 C  CD2   . PHE   B  1  1012 ? 14.000  38.575  80.875  1.00 14.20 ? 1010 PHE   B CD2   1 
ATOM   16578 C  CE1   . PHE   B  1  1012 ? 13.737  38.133  83.580  1.00 14.37 ? 1010 PHE   B CE1   1 
ATOM   16579 C  CE2   . PHE   B  1  1012 ? 15.132  38.436  81.665  1.00 14.73 ? 1010 PHE   B CE2   1 
ATOM   16580 C  CZ    . PHE   B  1  1012 ? 14.984  38.202  83.019  1.00 14.06 ? 1010 PHE   B CZ    1 
ATOM   16581 N  N     . GLY   B  1  1013 ? 12.836  41.794  80.726  1.00 12.81 ? 1011 GLY   B N     1 
ATOM   16582 C  CA    . GLY   B  1  1013 ? 13.945  42.556  80.201  1.00 13.73 ? 1011 GLY   B CA    1 
ATOM   16583 C  C     . GLY   B  1  1013 ? 14.241  43.725  81.097  1.00 13.26 ? 1011 GLY   B C     1 
ATOM   16584 O  O     . GLY   B  1  1013 ? 13.344  44.247  81.765  1.00 14.55 ? 1011 GLY   B O     1 
ATOM   16585 N  N     . GLY   B  1  1014 ? 15.494  44.130  81.120  1.00 14.44 ? 1012 GLY   B N     1 
ATOM   16586 C  CA    . GLY   B  1  1014 ? 15.889  45.176  82.023  1.00 16.46 ? 1012 GLY   B CA    1 
ATOM   16587 C  C     . GLY   B  1  1014 ? 16.478  46.390  81.371  1.00 14.98 ? 1012 GLY   B C     1 
ATOM   16588 O  O     . GLY   B  1  1014 ? 16.374  46.582  80.153  1.00 17.65 ? 1012 GLY   B O     1 
ATOM   16589 N  N     . ARG   B  1  1015 ? 17.105  47.212  82.198  1.00 15.78 ? 1013 ARG   B N     1 
ATOM   16590 C  CA    . ARG   B  1  1015 ? 17.588  48.523  81.821  1.00 16.11 ? 1013 ARG   B CA    1 
ATOM   16591 C  C     . ARG   B  1  1015 ? 19.044  48.629  82.224  1.00 14.68 ? 1013 ARG   B C     1 
ATOM   16592 O  O     . ARG   B  1  1015 ? 19.622  47.699  82.784  1.00 14.98 ? 1013 ARG   B O     1 
ATOM   16593 C  CB    . ARG   B  1  1015 ? 16.770  49.610  82.531  1.00 17.02 ? 1013 ARG   B CB    1 
ATOM   16594 C  CG    . ARG   B  1  1015 ? 16.813  49.468  84.061  1.00 17.27 ? 1013 ARG   B CG    1 
ATOM   16595 C  CD    . ARG   B  1  1015 ? 16.738  50.823  84.794  1.00 21.38 ? 1013 ARG   B CD    1 
ATOM   16596 N  NE    . ARG   B  1  1015 ? 18.044  51.481  84.797  1.00 22.65 ? 1013 ARG   B NE    1 
ATOM   16597 C  CZ    . ARG   B  1  1015 ? 19.057  51.121  85.573  1.00 22.98 ? 1013 ARG   B CZ    1 
ATOM   16598 N  NH1   . ARG   B  1  1015 ? 18.936  50.160  86.477  1.00 21.87 ? 1013 ARG   B NH1   1 
ATOM   16599 N  NH2   . ARG   B  1  1015 ? 20.235  51.725  85.426  1.00 24.90 ? 1013 ARG   B NH2   1 
ATOM   16600 N  N     . GLY   B  1  1016 ? 19.626  49.791  81.949  1.00 15.91 ? 1014 GLY   B N     1 
ATOM   16601 C  CA    . GLY   B  1  1016 ? 21.035  49.986  82.237  1.00 16.01 ? 1014 GLY   B CA    1 
ATOM   16602 C  C     . GLY   B  1  1016 ? 21.876  48.977  81.486  1.00 15.23 ? 1014 GLY   B C     1 
ATOM   16603 O  O     . GLY   B  1  1016 ? 21.661  48.734  80.294  1.00 17.04 ? 1014 GLY   B O     1 
ATOM   16604 N  N     . LEU   B  1  1017 ? 22.829  48.368  82.182  1.00 15.48 ? 1015 LEU   B N     1 
ATOM   16605 C  CA    . LEU   B  1  1017 ? 23.674  47.354  81.579  1.00 16.08 ? 1015 LEU   B CA    1 
ATOM   16606 C  C     . LEU   B  1  1017 ? 22.926  46.085  81.254  1.00 15.67 ? 1015 LEU   B C     1 
ATOM   16607 O  O     . LEU   B  1  1017 ? 23.534  45.175  80.674  1.00 15.40 ? 1015 LEU   B O     1 
ATOM   16608 C  CB    . LEU   B  1  1017 ? 24.831  47.016  82.515  1.00 15.10 ? 1015 LEU   B CB    1 
ATOM   16609 C  CG    . LEU   B  1  1017 ? 25.770  48.174  82.848  1.00 17.37 ? 1015 LEU   B CG    1 
ATOM   16610 C  CD1   . LEU   B  1  1017 ? 26.798  47.704  83.858  1.00 19.29 ? 1015 LEU   B CD1   1 
ATOM   16611 C  CD2   . LEU   B  1  1017 ? 26.461  48.653  81.593  1.00 19.82 ? 1015 LEU   B CD2   1 
ATOM   16612 N  N     . SER   B  1  1018 ? 21.655  45.988  81.631  1.00 13.67 ? 1016 SER   B N     1 
ATOM   16613 C  CA    . SER   B  1  1018 ? 20.887  44.778  81.410  1.00 14.07 ? 1016 SER   B CA    1 
ATOM   16614 C  C     . SER   B  1  1018 ? 20.078  44.791  80.129  1.00 13.09 ? 1016 SER   B C     1 
ATOM   16615 O  O     . SER   B  1  1018 ? 19.555  43.739  79.767  1.00 14.76 ? 1016 SER   B O     1 
ATOM   16616 C  CB    . SER   B  1  1018 ? 19.913  44.550  82.563  1.00 13.91 ? 1016 SER   B CB    1 
ATOM   16617 O  OG    . SER   B  1  1018 ? 20.664  44.330  83.744  1.00 14.43 ? 1016 SER   B OG    1 
ATOM   16618 N  N     . GLY   B  1  1019 ? 19.921  45.917  79.451  1.00 14.25 ? 1017 GLY   B N     1 
ATOM   16619 C  CA    . GLY   B  1  1019 ? 19.117  45.849  78.247  1.00 14.89 ? 1017 GLY   B CA    1 
ATOM   16620 C  C     . GLY   B  1  1019 ? 18.909  47.186  77.588  1.00 16.20 ? 1017 GLY   B C     1 
ATOM   16621 O  O     . GLY   B  1  1019 ? 18.940  48.235  78.227  1.00 16.64 ? 1017 GLY   B O     1 
ATOM   16622 N  N     . THR   B  1  1020 ? 18.638  47.116  76.287  1.00 15.31 ? 1018 THR   B N     1 
ATOM   16623 C  CA    . THR   B  1  1020 ? 18.095  48.246  75.556  1.00 15.45 ? 1018 THR   B CA    1 
ATOM   16624 C  C     . THR   B  1  1020 ? 16.584  48.274  75.594  1.00 14.91 ? 1018 THR   B C     1 
ATOM   16625 O  O     . THR   B  1  1020 ? 15.991  49.334  75.380  1.00 16.49 ? 1018 THR   B O     1 
ATOM   16626 C  CB    . THR   B  1  1020 ? 18.493  48.161  74.075  1.00 15.03 ? 1018 THR   B CB    1 
ATOM   16627 O  OG1   . THR   B  1  1020 ? 18.053  46.906  73.540  1.00 14.33 ? 1018 THR   B OG1   1 
ATOM   16628 C  CG2   . THR   B  1  1020 ? 20.009  48.245  73.912  1.00 15.84 ? 1018 THR   B CG2   1 
ATOM   16629 N  N     . GLY   B  1  1021 ? 15.959  47.129  75.814  1.00 14.99 ? 1019 GLY   B N     1 
ATOM   16630 C  CA    . GLY   B  1  1021 ? 14.560  46.984  75.528  1.00 14.84 ? 1019 GLY   B CA    1 
ATOM   16631 C  C     . GLY   B  1  1021 ? 14.332  47.016  74.031  1.00 14.61 ? 1019 GLY   B C     1 
ATOM   16632 O  O     . GLY   B  1  1021 ? 15.264  47.177  73.240  1.00 14.69 ? 1019 GLY   B O     1 
ATOM   16633 N  N     . PRO   B  1  1022 ? 13.097  46.848  73.617  1.00 14.19 ? 1020 PRO   B N     1 
ATOM   16634 C  CA    . PRO   B  1  1022 ? 11.923  46.580  74.445  1.00 15.25 ? 1020 PRO   B CA    1 
ATOM   16635 C  C     . PRO   B  1  1022 ? 11.967  45.159  74.991  1.00 15.81 ? 1020 PRO   B C     1 
ATOM   16636 O  O     . PRO   B  1  1022 ? 12.761  44.326  74.568  1.00 16.67 ? 1020 PRO   B O     1 
ATOM   16637 C  CB    . PRO   B  1  1022 ? 10.775  46.749  73.449  1.00 16.73 ? 1020 PRO   B CB    1 
ATOM   16638 C  CG    . PRO   B  1  1022 ? 11.361  46.288  72.160  1.00 16.05 ? 1020 PRO   B CG    1 
ATOM   16639 C  CD    . PRO   B  1  1022 ? 12.771  46.838  72.182  1.00 15.32 ? 1020 PRO   B CD    1 
ATOM   16640 N  N     . LYS   B  1  1023 ? 11.112  44.873  75.966  1.00 13.95 ? 1021 LYS   B N     1 
ATOM   16641 C  CA    . LYS   B  1  1023 ? 11.118  43.572  76.610  1.00 14.54 ? 1021 LYS   B CA    1 
ATOM   16642 C  C     . LYS   B  1  1023 ? 10.629  42.483  75.676  1.00 13.29 ? 1021 LYS   B C     1 
ATOM   16643 O  O     . LYS   B  1  1023 ? 9.562   42.591  75.060  1.00 14.14 ? 1021 LYS   B O     1 
ATOM   16644 C  CB    . LYS   B  1  1023 ? 10.162  43.587  77.783  1.00 13.07 ? 1021 LYS   B CB    1 
ATOM   16645 C  CG    . LYS   B  1  1023 ? 10.601  44.388  78.976  1.00 13.61 ? 1021 LYS   B CG    1 
ATOM   16646 C  CD    . LYS   B  1  1023 ? 9.483   44.349  79.971  1.00 12.68 ? 1021 LYS   B CD    1 
ATOM   16647 C  CE    . LYS   B  1  1023 ? 9.870   44.885  81.336  1.00 15.46 ? 1021 LYS   B CE    1 
ATOM   16648 N  NZ    . LYS   B  1  1023 ? 10.587  43.848  82.107  1.00 14.18 ? 1021 LYS   B NZ    1 
ATOM   16649 N  N     . ALA   B  1  1024 ? 11.375  41.399  75.627  1.00 14.22 ? 1022 ALA   B N     1 
ATOM   16650 C  CA    . ALA   B  1  1024 ? 10.859  40.170  75.058  1.00 13.27 ? 1022 ALA   B CA    1 
ATOM   16651 C  C     . ALA   B  1  1024 ? 9.628   39.713  75.817  1.00 14.80 ? 1022 ALA   B C     1 
ATOM   16652 O  O     . ALA   B  1  1024 ? 9.496   39.920  77.029  1.00 15.17 ? 1022 ALA   B O     1 
ATOM   16653 C  CB    . ALA   B  1  1024 ? 11.938  39.087  75.121  1.00 15.20 ? 1022 ALA   B CB    1 
ATOM   16654 N  N     . GLY   B  1  1025 ? 8.693   39.115  75.090  1.00 12.98 ? 1023 GLY   B N     1 
ATOM   16655 C  CA    . GLY   B  1  1025 ? 7.498   38.628  75.743  1.00 14.39 ? 1023 GLY   B CA    1 
ATOM   16656 C  C     . GLY   B  1  1025 ? 6.586   39.733  76.190  1.00 14.21 ? 1023 GLY   B C     1 
ATOM   16657 O  O     . GLY   B  1  1025 ? 5.709   39.502  77.018  1.00 14.49 ? 1023 GLY   B O     1 
ATOM   16658 N  N     . GLY   B  1  1026 ? 6.778   40.931  75.649  1.00 14.12 ? 1024 GLY   B N     1 
ATOM   16659 C  CA    . GLY   B  1  1026 ? 5.961   42.070  75.968  1.00 14.19 ? 1024 GLY   B CA    1 
ATOM   16660 C  C     . GLY   B  1  1026 ? 5.452   42.715  74.698  1.00 14.03 ? 1024 GLY   B C     1 
ATOM   16661 O  O     . GLY   B  1  1026 ? 5.860   42.377  73.578  1.00 13.49 ? 1024 GLY   B O     1 
ATOM   16662 N  N     . PRO   B  1  1027 ? 4.558   43.684  74.862  1.00 13.98 ? 1025 PRO   B N     1 
ATOM   16663 C  CA    . PRO   B  1  1027 ? 3.789   44.191  73.727  1.00 12.12 ? 1025 PRO   B CA    1 
ATOM   16664 C  C     . PRO   B  1  1027 ? 4.523   45.211  72.892  1.00 13.01 ? 1025 PRO   B C     1 
ATOM   16665 O  O     . PRO   B  1  1027 ? 4.006   45.575  71.838  1.00 13.97 ? 1025 PRO   B O     1 
ATOM   16666 C  CB    . PRO   B  1  1027 ? 2.558   44.807  74.402  1.00 14.46 ? 1025 PRO   B CB    1 
ATOM   16667 C  CG    . PRO   B  1  1027 ? 3.058   45.200  75.759  1.00 16.32 ? 1025 PRO   B CG    1 
ATOM   16668 C  CD    . PRO   B  1  1027 ? 4.060   44.172  76.155  1.00 15.21 ? 1025 PRO   B CD    1 
ATOM   16669 N  N     . LEU   B  1  1028 ? 5.688   45.689  73.309  1.00 13.23 ? 1026 LEU   B N     1 
ATOM   16670 C  CA    . LEU   B  1  1028 ? 6.433   46.649  72.505  1.00 13.94 ? 1026 LEU   B CA    1 
ATOM   16671 C  C     . LEU   B  1  1028 ? 7.426   45.978  71.583  1.00 14.43 ? 1026 LEU   B C     1 
ATOM   16672 O  O     . LEU   B  1  1028 ? 8.004   46.651  70.727  1.00 15.45 ? 1026 LEU   B O     1 
ATOM   16673 C  CB    . LEU   B  1  1028 ? 7.214   47.616  73.399  1.00 14.28 ? 1026 LEU   B CB    1 
ATOM   16674 C  CG    . LEU   B  1  1028 ? 6.380   48.435  74.369  1.00 17.61 ? 1026 LEU   B CG    1 
ATOM   16675 C  CD1   . LEU   B  1  1028 ? 7.255   49.440  75.086  1.00 18.79 ? 1026 LEU   B CD1   1 
ATOM   16676 C  CD2   . LEU   B  1  1028 ? 5.298   49.119  73.634  1.00 21.37 ? 1026 LEU   B CD2   1 
ATOM   16677 N  N     . TYR   B  1  1029 ? 7.612   44.674  71.726  1.00 13.28 ? 1027 TYR   B N     1 
ATOM   16678 C  CA    . TYR   B  1  1029 ? 8.735   43.996  71.099  1.00 13.88 ? 1027 TYR   B CA    1 
ATOM   16679 C  C     . TYR   B  1  1029 ? 8.606   43.985  69.587  1.00 12.91 ? 1027 TYR   B C     1 
ATOM   16680 O  O     . TYR   B  1  1029 ? 9.558   44.331  68.886  1.00 13.84 ? 1027 TYR   B O     1 
ATOM   16681 C  CB    . TYR   B  1  1029 ? 8.748   42.570  71.609  1.00 14.27 ? 1027 TYR   B CB    1 
ATOM   16682 C  CG    . TYR   B  1  1029 ? 10.006  41.772  71.445  1.00 13.47 ? 1027 TYR   B CG    1 
ATOM   16683 C  CD1   . TYR   B  1  1029 ? 11.150  42.103  72.148  1.00 14.29 ? 1027 TYR   B CD1   1 
ATOM   16684 C  CD2   . TYR   B  1  1029 ? 10.012  40.606  70.689  1.00 13.75 ? 1027 TYR   B CD2   1 
ATOM   16685 C  CE1   . TYR   B  1  1029 ? 12.290  41.314  72.065  1.00 14.33 ? 1027 TYR   B CE1   1 
ATOM   16686 C  CE2   . TYR   B  1  1029 ? 11.138  39.819  70.614  1.00 13.01 ? 1027 TYR   B CE2   1 
ATOM   16687 C  CZ    . TYR   B  1  1029 ? 12.267  40.175  71.299  1.00 13.78 ? 1027 TYR   B CZ    1 
ATOM   16688 O  OH    . TYR   B  1  1029 ? 13.348  39.335  71.241  1.00 14.92 ? 1027 TYR   B OH    1 
ATOM   16689 N  N     . LEU   B  1  1030 ? 7.449   43.567  69.058  1.00 12.74 ? 1028 LEU   B N     1 
ATOM   16690 C  CA    . LEU   B  1  1030 ? 7.348   43.424  67.606  1.00 13.34 ? 1028 LEU   B CA    1 
ATOM   16691 C  C     . LEU   B  1  1030 ? 7.542   44.756  66.915  1.00 14.33 ? 1028 LEU   B C     1 
ATOM   16692 O  O     . LEU   B  1  1030 ? 8.080   44.813  65.797  1.00 14.14 ? 1028 LEU   B O     1 
ATOM   16693 C  CB    . LEU   B  1  1030 ? 6.003   42.823  67.210  1.00 14.09 ? 1028 LEU   B CB    1 
ATOM   16694 C  CG    . LEU   B  1  1030 ? 5.765   41.376  67.640  1.00 15.10 ? 1028 LEU   B CG    1 
ATOM   16695 C  CD1   . LEU   B  1  1030 ? 4.432   40.865  67.131  1.00 17.74 ? 1028 LEU   B CD1   1 
ATOM   16696 C  CD2   . LEU   B  1  1030 ? 6.899   40.462  67.144  1.00 18.20 ? 1028 LEU   B CD2   1 
ATOM   16697 N  N     . GLY   B  1  1031 ? 7.156   45.844  67.573  1.00 14.69 ? 1029 GLY   B N     1 
ATOM   16698 C  CA    . GLY   B  1  1031 ? 7.226   47.150  66.952  1.00 15.79 ? 1029 GLY   B CA    1 
ATOM   16699 C  C     . GLY   B  1  1031 ? 8.634   47.613  66.676  1.00 14.46 ? 1029 GLY   B C     1 
ATOM   16700 O  O     . GLY   B  1  1031 ? 8.827   48.526  65.871  1.00 16.32 ? 1029 GLY   B O     1 
ATOM   16701 N  N     . ARG   B  1  1032 ? 9.618   47.003  67.318  1.00 13.97 ? 1030 ARG   B N     1 
ATOM   16702 C  CA    . ARG   B  1  1032 ? 11.000  47.341  67.037  1.00 13.73 ? 1030 ARG   B CA    1 
ATOM   16703 C  C     . ARG   B  1  1032 ? 11.495  46.680  65.763  1.00 14.37 ? 1030 ARG   B C     1 
ATOM   16704 O  O     . ARG   B  1  1032 ? 12.561  47.058  65.254  1.00 16.34 ? 1030 ARG   B O     1 
ATOM   16705 C  CB    . ARG   B  1  1032 ? 11.847  46.915  68.239  1.00 14.81 ? 1030 ARG   B CB    1 
ATOM   16706 C  CG    . ARG   B  1  1032 ? 13.270  47.407  68.220  1.00 16.04 ? 1030 ARG   B CG    1 
ATOM   16707 C  CD    . ARG   B  1  1032 ? 13.338  48.904  68.428  1.00 16.38 ? 1030 ARG   B CD    1 
ATOM   16708 N  NE    . ARG   B  1  1032 ? 14.716  49.314  68.652  1.00 17.81 ? 1030 ARG   B NE    1 
ATOM   16709 C  CZ    . ARG   B  1  1032 ? 15.338  50.272  67.983  1.00 20.61 ? 1030 ARG   B CZ    1 
ATOM   16710 N  NH1   . ARG   B  1  1032 ? 14.743  50.926  66.997  1.00 20.68 ? 1030 ARG   B NH1   1 
ATOM   16711 N  NH2   . ARG   B  1  1032 ? 16.588  50.582  68.316  1.00 20.73 ? 1030 ARG   B NH2   1 
ATOM   16712 N  N     . LEU   B  1  1033 ? 10.744  45.713  65.237  1.00 13.59 ? 1031 LEU   B N     1 
ATOM   16713 C  CA    . LEU   B  1  1033 ? 11.187  44.869  64.139  1.00 14.31 ? 1031 LEU   B CA    1 
ATOM   16714 C  C     . LEU   B  1  1033 ? 10.518  45.243  62.829  1.00 14.46 ? 1031 LEU   B C     1 
ATOM   16715 O  O     . LEU   B  1  1033 ? 10.570  44.464  61.876  1.00 15.12 ? 1031 LEU   B O     1 
ATOM   16716 C  CB    . LEU   B  1  1033 ? 10.927  43.401  64.482  1.00 15.39 ? 1031 LEU   B CB    1 
ATOM   16717 C  CG    . LEU   B  1  1033 ? 11.488  43.009  65.852  1.00 14.47 ? 1031 LEU   B CG    1 
ATOM   16718 C  CD1   . LEU   B  1  1033 ? 11.157  41.566  66.159  1.00 15.02 ? 1031 LEU   B CD1   1 
ATOM   16719 C  CD2   . LEU   B  1  1033 ? 12.996  43.241  65.933  1.00 16.37 ? 1031 LEU   B CD2   1 
ATOM   16720 N  N     . VAL   B  1  1034 ? 9.848   46.386  62.791  1.00 14.95 ? 1032 VAL   B N     1 
ATOM   16721 C  CA    . VAL   B  1  1034 ? 9.242   46.940  61.592  1.00 16.23 ? 1032 VAL   B CA    1 
ATOM   16722 C  C     . VAL   B  1  1034 ? 9.680   48.393  61.508  1.00 17.27 ? 1032 VAL   B C     1 
ATOM   16723 O  O     . VAL   B  1  1034 ? 10.158  48.972  62.483  1.00 18.42 ? 1032 VAL   B O     1 
ATOM   16724 C  CB    . VAL   B  1  1034 ? 7.708   46.839  61.636  1.00 16.26 ? 1032 VAL   B CB    1 
ATOM   16725 C  CG1   . VAL   B  1  1034 ? 7.245   45.391  61.501  1.00 18.57 ? 1032 VAL   B CG1   1 
ATOM   16726 C  CG2   . VAL   B  1  1034 ? 7.178   47.423  62.944  1.00 16.34 ? 1032 VAL   B CG2   1 
ATOM   16727 N  N     . THR   B  1  1035 ? 9.537   48.991  60.323  1.00 19.21 ? 1033 THR   B N     1 
ATOM   16728 C  CA    . THR   B  1  1035 ? 10.053  50.347  60.177  1.00 20.80 ? 1033 THR   B CA    1 
ATOM   16729 C  C     . THR   B  1  1035 ? 9.117   51.407  60.729  1.00 21.82 ? 1033 THR   B C     1 
ATOM   16730 O  O     . THR   B  1  1035 ? 9.568   52.525  60.993  1.00 26.74 ? 1033 THR   B O     1 
ATOM   16731 C  CB    . THR   B  1  1035 ? 10.399  50.650  58.720  1.00 26.24 ? 1033 THR   B CB    1 
ATOM   16732 O  OG1   . THR   B  1  1035 ? 9.311   50.250  57.890  1.00 29.10 ? 1033 THR   B OG1   1 
ATOM   16733 C  CG2   . THR   B  1  1035 ? 11.650  49.893  58.318  1.00 28.45 ? 1033 THR   B CG2   1 
ATOM   16734 N  N     . THR   B  1  1036 ? 7.840   51.082  60.906  1.00 18.88 ? 1034 THR   B N     1 
ATOM   16735 C  CA    . THR   B  1  1036 ? 6.873   51.959  61.547  1.00 20.49 ? 1034 THR   B CA    1 
ATOM   16736 C  C     . THR   B  1  1036 ? 6.206   51.128  62.629  1.00 20.52 ? 1034 THR   B C     1 
ATOM   16737 O  O     . THR   B  1  1036 ? 5.588   50.109  62.325  1.00 19.37 ? 1034 THR   B O     1 
ATOM   16738 C  CB    . THR   B  1  1036 ? 5.822   52.419  60.540  1.00 25.83 ? 1034 THR   B CB    1 
ATOM   16739 O  OG1   . THR   B  1  1036 ? 6.468   53.012  59.405  1.00 31.44 ? 1034 THR   B OG1   1 
ATOM   16740 C  CG2   . THR   B  1  1036 ? 4.883   53.436  61.178  1.00 30.88 ? 1034 THR   B CG2   1 
ATOM   16741 N  N     . ALA   B  1  1037 ? 6.348   51.542  63.884  1.00 20.04 ? 1035 ALA   B N     1 
ATOM   16742 C  CA    . ALA   B  1  1037 ? 5.822   50.732  64.973  1.00 19.11 ? 1035 ALA   B CA    1 
ATOM   16743 C  C     . ALA   B  1  1037 ? 4.303   50.854  65.040  1.00 17.97 ? 1035 ALA   B C     1 
ATOM   16744 O  O     . ALA   B  1  1037 ? 3.760   51.953  64.904  1.00 19.94 ? 1035 ALA   B O     1 
ATOM   16745 C  CB    . ALA   B  1  1037 ? 6.429   51.179  66.300  1.00 21.80 ? 1035 ALA   B CB    1 
ATOM   16746 N  N     . PRO   B  1  1038 ? 3.598   49.750  65.239  1.00 16.08 ? 1036 PRO   B N     1 
ATOM   16747 C  CA    . PRO   B  1  1038 ? 2.160   49.815  65.482  1.00 16.59 ? 1036 PRO   B CA    1 
ATOM   16748 C  C     . PRO   B  1  1038 ? 1.880   50.294  66.898  1.00 16.34 ? 1036 PRO   B C     1 
ATOM   16749 O  O     . PRO   B  1  1038 ? 2.760   50.407  67.741  1.00 16.90 ? 1036 PRO   B O     1 
ATOM   16750 C  CB    . PRO   B  1  1038 ? 1.715   48.361  65.331  1.00 18.37 ? 1036 PRO   B CB    1 
ATOM   16751 C  CG    . PRO   B  1  1038 ? 2.898   47.572  65.772  1.00 19.98 ? 1036 PRO   B CG    1 
ATOM   16752 C  CD    . PRO   B  1  1038 ? 4.110   48.372  65.308  1.00 17.04 ? 1036 PRO   B CD    1 
ATOM   16753 N  N     . VAL   B  1  1039 ? 0.603   50.545  67.157  1.00 16.21 ? 1037 VAL   B N     1 
ATOM   16754 C  CA    . VAL   B  1  1039 ? 0.121   50.833  68.502  1.00 16.80 ? 1037 VAL   B CA    1 
ATOM   16755 C  C     . VAL   B  1  1039 ? -0.177  49.494  69.173  1.00 16.04 ? 1037 VAL   B C     1 
ATOM   16756 O  O     . VAL   B  1  1039 ? -1.086  48.787  68.728  1.00 17.04 ? 1037 VAL   B O     1 
ATOM   16757 C  CB    . VAL   B  1  1039 ? -1.130  51.711  68.454  1.00 17.09 ? 1037 VAL   B CB    1 
ATOM   16758 C  CG1   . VAL   B  1  1039 ? -1.599  51.979  69.874  1.00 20.76 ? 1037 VAL   B CG1   1 
ATOM   16759 C  CG2   . VAL   B  1  1039 ? -0.810  53.003  67.724  1.00 20.90 ? 1037 VAL   B CG2   1 
ATOM   16760 N  N     . PRO   B  1  1040 ? 0.569   49.097  70.190  1.00 16.31 ? 1038 PRO   B N     1 
ATOM   16761 C  CA    . PRO   B  1  1040 ? 0.338   47.791  70.782  1.00 16.53 ? 1038 PRO   B CA    1 
ATOM   16762 C  C     . PRO   B  1  1040 ? -1.005  47.729  71.483  1.00 16.38 ? 1038 PRO   B C     1 
ATOM   16763 O  O     . PRO   B  1  1040 ? -1.566  48.767  71.862  1.00 16.35 ? 1038 PRO   B O     1 
ATOM   16764 C  CB    . PRO   B  1  1040 ? 1.489   47.661  71.795  1.00 18.76 ? 1038 PRO   B CB    1 
ATOM   16765 C  CG    . PRO   B  1  1040 ? 2.535   48.642  71.335  1.00 20.77 ? 1038 PRO   B CG    1 
ATOM   16766 C  CD    . PRO   B  1  1040 ? 1.752   49.777  70.750  1.00 18.01 ? 1038 PRO   B CD    1 
ATOM   16767 N  N     . PRO   B  1  1041 ? -1.555  46.531  71.669  1.00 17.45 ? 1039 PRO   B N     1 
ATOM   16768 C  CA    . PRO   B  1  1041 ? -2.763  46.382  72.482  1.00 17.68 ? 1039 PRO   B CA    1 
ATOM   16769 C  C     . PRO   B  1  1041 ? -2.580  47.048  73.837  1.00 15.54 ? 1039 PRO   B C     1 
ATOM   16770 O  O     . PRO   B  1  1041 ? -1.511  46.960  74.446  1.00 17.70 ? 1039 PRO   B O     1 
ATOM   16771 C  CB    . PRO   B  1  1041 ? -2.902  44.864  72.637  1.00 18.49 ? 1039 PRO   B CB    1 
ATOM   16772 C  CG    . PRO   B  1  1041 ? -2.101  44.283  71.491  1.00 21.82 ? 1039 PRO   B CG    1 
ATOM   16773 C  CD    . PRO   B  1  1041 ? -0.977  45.233  71.266  1.00 19.41 ? 1039 PRO   B CD    1 
ATOM   16774 N  N     . GLN   B  1  1042 ? -3.622  47.737  74.287  1.00 16.27 ? 1040 GLN   B N     1 
ATOM   16775 C  CA    . GLN   B  1  1042 ? -3.696  48.348  75.612  1.00 17.19 ? 1040 GLN   B CA    1 
ATOM   16776 C  C     . GLN   B  1  1042 ? -2.674  49.454  75.831  1.00 16.92 ? 1040 GLN   B C     1 
ATOM   16777 O  O     . GLN   B  1  1042 ? -2.486  49.904  76.967  1.00 17.55 ? 1040 GLN   B O     1 
ATOM   16778 C  CB    . GLN   B  1  1042 ? -3.576  47.308  76.733  1.00 19.50 ? 1040 GLN   B CB    1 
ATOM   16779 C  CG    . GLN   B  1  1042 ? -4.588  46.178  76.644  1.00 23.28 ? 1040 GLN   B CG    1 
ATOM   16780 C  CD    . GLN   B  1  1042 ? -4.461  45.243  77.832  1.00 29.70 ? 1040 GLN   B CD    1 
ATOM   16781 O  OE1   . GLN   B  1  1042 ? -3.511  44.467  77.923  1.00 44.83 ? 1040 GLN   B OE1   1 
ATOM   16782 N  NE2   . GLN   B  1  1042 ? -5.388  45.354  78.768  1.00 40.52 ? 1040 GLN   B NE2   1 
ATOM   16783 N  N     . HIS   B  1  1043 ? -1.993  49.911  74.788  1.00 15.78 ? 1041 HIS   B N     1 
ATOM   16784 C  CA    . HIS   B  1  1043 ? -0.882  50.844  74.948  1.00 15.48 ? 1041 HIS   B CA    1 
ATOM   16785 C  C     . HIS   B  1  1043 ? -1.403  52.271  74.858  1.00 17.07 ? 1041 HIS   B C     1 
ATOM   16786 O  O     . HIS   B  1  1043 ? -1.501  52.858  73.778  1.00 18.96 ? 1041 HIS   B O     1 
ATOM   16787 C  CB    . HIS   B  1  1043 ? 0.161   50.569  73.876  1.00 15.75 ? 1041 HIS   B CB    1 
ATOM   16788 C  CG    . HIS   B  1  1043 ? 1.362   51.452  73.955  1.00 16.08 ? 1041 HIS   B CG    1 
ATOM   16789 N  ND1   . HIS   B  1  1043 ? 2.447   51.163  74.756  1.00 16.55 ? 1041 HIS   B ND1   1 
ATOM   16790 C  CD2   . HIS   B  1  1043 ? 1.661   52.609  73.319  1.00 18.59 ? 1041 HIS   B CD2   1 
ATOM   16791 C  CE1   . HIS   B  1  1043 ? 3.368   52.099  74.600  1.00 15.74 ? 1041 HIS   B CE1   1 
ATOM   16792 N  NE2   . HIS   B  1  1043 ? 2.920   52.984  73.727  1.00 16.00 ? 1041 HIS   B NE2   1 
ATOM   16793 N  N     . SER   B  1  1044 ? -1.766  52.834  76.005  1.00 14.36 ? 1042 SER   B N     1 
ATOM   16794 C  CA    . SER   B  1  1044 ? -2.181  54.225  76.078  1.00 14.75 ? 1042 SER   B CA    1 
ATOM   16795 C  C     . SER   B  1  1044 ? -2.111  54.631  77.533  1.00 15.52 ? 1042 SER   B C     1 
ATOM   16796 O  O     . SER   B  1  1044 ? -1.951  53.794  78.421  1.00 16.64 ? 1042 SER   B O     1 
ATOM   16797 C  CB    . SER   B  1  1044 ? -3.611  54.420  75.577  1.00 15.82 ? 1042 SER   B CB    1 
ATOM   16798 O  OG    . SER   B  1  1044 ? -4.520  53.766  76.435  1.00 17.08 ? 1042 SER   B OG    1 
ATOM   16799 N  N     . SER   B  1  1045 ? -2.267  55.924  77.767  1.00 14.68 ? 1043 SER   B N     1 
ATOM   16800 C  CA    . SER   B  1  1045 ? -2.316  56.431  79.124  1.00 14.01 ? 1043 SER   B CA    1 
ATOM   16801 C  C     . SER   B  1  1045 ? -3.166  57.682  79.136  1.00 15.86 ? 1043 SER   B C     1 
ATOM   16802 O  O     . SER   B  1  1045 ? -3.100  58.488  78.208  1.00 16.55 ? 1043 SER   B O     1 
ATOM   16803 C  CB    . SER   B  1  1045 ? -0.903  56.812  79.550  1.00 15.55 ? 1043 SER   B CB    1 
ATOM   16804 O  OG    . SER   B  1  1045 ? -0.927  57.391  80.834  1.00 16.39 ? 1043 SER   B OG    1 
ATOM   16805 N  N     . VAL   B  1  1046 ? -3.961  57.849  80.200  1.00 15.46 ? 1044 VAL   B N     1 
ATOM   16806 C  CA    . VAL   B  1  1046 ? -4.728  59.080  80.360  1.00 17.23 ? 1044 VAL   B CA    1 
ATOM   16807 C  C     . VAL   B  1  1046 ? -3.909  60.206  80.956  1.00 17.92 ? 1044 VAL   B C     1 
ATOM   16808 O  O     . VAL   B  1  1046 ? -4.382  61.345  81.008  1.00 17.97 ? 1044 VAL   B O     1 
ATOM   16809 C  CB    . VAL   B  1  1046 ? -6.010  58.867  81.186  1.00 20.23 ? 1044 VAL   B CB    1 
ATOM   16810 C  CG1   . VAL   B  1  1046 ? -6.863  57.808  80.508  1.00 22.37 ? 1044 VAL   B CG1   1 
ATOM   16811 C  CG2   . VAL   B  1  1046 ? -5.676  58.471  82.597  1.00 18.98 ? 1044 VAL   B CG2   1 
ATOM   16812 N  N     . HIS   B  1  1047 ? -2.685  59.926  81.372  1.00 16.70 ? 1045 HIS   B N     1 
ATOM   16813 C  CA    A HIS   B  1  1047 ? -1.886  60.925  82.046  0.57 17.68 ? 1045 HIS   B CA    1 
ATOM   16814 C  CA    B HIS   B  1  1047 ? -1.822  60.878  82.066  0.43 17.67 ? 1045 HIS   B CA    1 
ATOM   16815 C  C     . HIS   B  1  1047 ? -1.064  61.713  81.049  1.00 16.61 ? 1045 HIS   B C     1 
ATOM   16816 O  O     . HIS   B  1  1047 ? -0.596  61.182  80.044  1.00 17.90 ? 1045 HIS   B O     1 
ATOM   16817 C  CB    A HIS   B  1  1047 ? -1.007  60.230  83.065  0.57 18.31 ? 1045 HIS   B CB    1 
ATOM   16818 C  CB    B HIS   B  1  1047 ? -0.797  60.102  82.897  0.43 17.35 ? 1045 HIS   B CB    1 
ATOM   16819 C  CG    A HIS   B  1  1047 ? -1.800  59.383  83.998  0.57 16.35 ? 1045 HIS   B CG    1 
ATOM   16820 C  CG    B HIS   B  1  1047 ? 0.373   60.921  83.357  0.43 20.54 ? 1045 HIS   B CG    1 
ATOM   16821 N  ND1   A HIS   B  1  1047 ? -2.637  59.924  84.949  0.57 19.51 ? 1045 HIS   B ND1   1 
ATOM   16822 N  ND1   B HIS   B  1  1047 ? 0.281   61.851  84.370  0.43 21.23 ? 1045 HIS   B ND1   1 
ATOM   16823 C  CD2   A HIS   B  1  1047 ? -1.955  58.040  84.078  0.57 19.16 ? 1045 HIS   B CD2   1 
ATOM   16824 C  CD2   B HIS   B  1  1047 ? 1.667   60.936  82.950  0.43 20.62 ? 1045 HIS   B CD2   1 
ATOM   16825 C  CE1   A HIS   B  1  1047 ? -3.242  58.949  85.605  0.57 24.06 ? 1045 HIS   B CE1   1 
ATOM   16826 C  CE1   B HIS   B  1  1047 ? 1.462   62.412  84.560  0.43 20.22 ? 1045 HIS   B CE1   1 
ATOM   16827 N  NE2   A HIS   B  1  1047 ? -2.848  57.796  85.092  0.57 21.37 ? 1045 HIS   B NE2   1 
ATOM   16828 N  NE2   B HIS   B  1  1047 ? 2.321   61.874  83.712  0.43 22.35 ? 1045 HIS   B NE2   1 
ATOM   16829 N  N     . THR   B  1  1048 ? -0.934  63.002  81.320  1.00 17.12 ? 1046 THR   B N     1 
ATOM   16830 C  CA    . THR   B  1  1048 ? -0.131  63.883  80.489  1.00 17.08 ? 1046 THR   B CA    1 
ATOM   16831 C  C     . THR   B  1  1048 ? 0.997   64.435  81.343  1.00 17.96 ? 1046 THR   B C     1 
ATOM   16832 O  O     . THR   B  1  1048 ? 0.760   64.967  82.429  1.00 18.97 ? 1046 THR   B O     1 
ATOM   16833 C  CB    . THR   B  1  1048 ? -0.950  65.038  79.939  1.00 18.33 ? 1046 THR   B CB    1 
ATOM   16834 O  OG1   . THR   B  1  1048 ? -2.129  64.525  79.303  1.00 20.26 ? 1046 THR   B OG1   1 
ATOM   16835 C  CG2   . THR   B  1  1048 ? -0.128  65.807  78.898  1.00 21.45 ? 1046 THR   B CG2   1 
ATOM   16836 N  N     . ASP   B  1  1049 ? 2.213   64.298  80.856  1.00 17.03 ? 1047 ASP   B N     1 
ATOM   16837 C  CA    . ASP   B  1  1049 ? 3.338   64.786  81.619  1.00 16.30 ? 1047 ASP   B CA    1 
ATOM   16838 C  C     . ASP   B  1  1049 ? 3.182   66.286  81.842  1.00 16.58 ? 1047 ASP   B C     1 
ATOM   16839 O  O     . ASP   B  1  1049 ? 2.926   67.027  80.886  1.00 17.95 ? 1047 ASP   B O     1 
ATOM   16840 C  CB    . ASP   B  1  1049 ? 4.626   64.498  80.859  1.00 15.82 ? 1047 ASP   B CB    1 
ATOM   16841 C  CG    . ASP   B  1  1049 ? 5.834   64.931  81.632  1.00 17.98 ? 1047 ASP   B CG    1 
ATOM   16842 O  OD1   . ASP   B  1  1049 ? 6.169   66.124  81.544  1.00 18.55 ? 1047 ASP   B OD1   1 
ATOM   16843 O  OD2   . ASP   B  1  1049 ? 6.375   64.097  82.380  1.00 18.09 ? 1047 ASP   B OD2   1 
ATOM   16844 N  N     . PRO   B  1  1050 ? 3.310   66.771  83.084  1.00 18.32 ? 1048 PRO   B N     1 
ATOM   16845 C  CA    . PRO   B  1  1050 ? 3.061   68.195  83.335  1.00 19.37 ? 1048 PRO   B CA    1 
ATOM   16846 C  C     . PRO   B  1  1050 ? 4.130   69.096  82.756  1.00 18.93 ? 1048 PRO   B C     1 
ATOM   16847 O  O     . PRO   B  1  1050 ? 3.840   70.244  82.408  1.00 20.94 ? 1048 PRO   B O     1 
ATOM   16848 C  CB    . PRO   B  1  1050 ? 3.022   68.276  84.869  1.00 21.89 ? 1048 PRO   B CB    1 
ATOM   16849 C  CG    . PRO   B  1  1050 ? 3.857   67.149  85.320  1.00 22.43 ? 1048 PRO   B CG    1 
ATOM   16850 C  CD    . PRO   B  1  1050 ? 3.598   66.035  84.325  1.00 20.95 ? 1048 PRO   B CD    1 
ATOM   16851 N  N     . VAL   B  1  1051 ? 5.368   68.612  82.666  1.00 19.54 ? 1049 VAL   B N     1 
ATOM   16852 C  CA    . VAL   B  1  1051 ? 6.428   69.422  82.075  1.00 18.24 ? 1049 VAL   B CA    1 
ATOM   16853 C  C     . VAL   B  1  1051 ? 6.210   69.550  80.579  1.00 17.58 ? 1049 VAL   B C     1 
ATOM   16854 O  O     . VAL   B  1  1051 ? 6.413   70.621  79.997  1.00 19.62 ? 1049 VAL   B O     1 
ATOM   16855 C  CB    . VAL   B  1  1051 ? 7.807   68.838  82.419  1.00 21.38 ? 1049 VAL   B CB    1 
ATOM   16856 C  CG1   . VAL   B  1  1051 ? 8.919   69.667  81.764  1.00 22.14 ? 1049 VAL   B CG1   1 
ATOM   16857 C  CG2   . VAL   B  1  1051 ? 7.982   68.801  83.935  1.00 20.53 ? 1049 VAL   B CG2   1 
ATOM   16858 N  N     . LEU   B  1  1052 ? 5.781   68.463  79.936  1.00 17.24 ? 1050 LEU   B N     1 
ATOM   16859 C  CA    . LEU   B  1  1052 ? 5.335   68.555  78.552  1.00 18.21 ? 1050 LEU   B CA    1 
ATOM   16860 C  C     . LEU   B  1  1052 ? 4.302   69.661  78.389  1.00 19.50 ? 1050 LEU   B C     1 
ATOM   16861 O  O     . LEU   B  1  1052 ? 4.392   70.474  77.466  1.00 18.84 ? 1050 LEU   B O     1 
ATOM   16862 C  CB    . LEU   B  1  1052 ? 4.784   67.209  78.082  1.00 17.15 ? 1050 LEU   B CB    1 
ATOM   16863 C  CG    . LEU   B  1  1052 ? 4.283   67.066  76.634  1.00 15.89 ? 1050 LEU   B CG    1 
ATOM   16864 C  CD1   . LEU   B  1  1052 ? 2.904   67.677  76.392  1.00 18.31 ? 1050 LEU   B CD1   1 
ATOM   16865 C  CD2   . LEU   B  1  1052 ? 5.291   67.629  75.636  1.00 17.53 ? 1050 LEU   B CD2   1 
ATOM   16866 N  N     . LEU   B  1  1053 ? 3.307   69.704  79.285  1.00 18.37 ? 1051 LEU   B N     1 
ATOM   16867 C  CA    . LEU   B  1  1053 ? 2.269   70.723  79.179  1.00 20.84 ? 1051 LEU   B CA    1 
ATOM   16868 C  C     . LEU   B  1  1053 ? 2.855   72.124  79.271  1.00 20.59 ? 1051 LEU   B C     1 
ATOM   16869 O  O     . LEU   B  1  1053 ? 2.498   73.007  78.484  1.00 22.38 ? 1051 LEU   B O     1 
ATOM   16870 C  CB    . LEU   B  1  1053 ? 1.217   70.520  80.274  1.00 23.30 ? 1051 LEU   B CB    1 
ATOM   16871 C  CG    . LEU   B  1  1053 ? 0.301   69.309  80.068  1.00 26.91 ? 1051 LEU   B CG    1 
ATOM   16872 C  CD1   . LEU   B  1  1053 ? -0.543  69.080  81.312  1.00 23.58 ? 1051 LEU   B CD1   1 
ATOM   16873 C  CD2   . LEU   B  1  1053 ? -0.579  69.522  78.860  1.00 28.04 ? 1051 LEU   B CD2   1 
ATOM   16874 N  N     . ASP   B  1  1054 ? 3.759   72.344  80.226  1.00 22.03 ? 1052 ASP   B N     1 
ATOM   16875 C  CA    . ASP   B  1  1054 ? 4.406   73.646  80.346  1.00 24.60 ? 1052 ASP   B CA    1 
ATOM   16876 C  C     . ASP   B  1  1054 ? 5.228   73.967  79.104  1.00 20.35 ? 1052 ASP   B C     1 
ATOM   16877 O  O     . ASP   B  1  1054 ? 5.286   75.121  78.671  1.00 22.76 ? 1052 ASP   B O     1 
ATOM   16878 C  CB    . ASP   B  1  1054 ? 5.293   73.667  81.588  1.00 24.35 ? 1052 ASP   B CB    1 
ATOM   16879 C  CG    . ASP   B  1  1054 ? 4.495   73.612  82.875  1.00 29.87 ? 1052 ASP   B CG    1 
ATOM   16880 O  OD1   . ASP   B  1  1054 ? 3.290   73.911  82.832  1.00 29.10 ? 1052 ASP   B OD1   1 
ATOM   16881 O  OD2   . ASP   B  1  1054 ? 5.075   73.282  83.930  1.00 32.70 ? 1052 ASP   B OD2   1 
ATOM   16882 N  N     . PHE   B  1  1055 ? 5.863   72.956  78.513  1.00 19.22 ? 1053 PHE   B N     1 
ATOM   16883 C  CA    . PHE   B  1  1055 ? 6.645   73.187  77.307  1.00 18.89 ? 1053 PHE   B CA    1 
ATOM   16884 C  C     . PHE   B  1  1055 ? 5.753   73.610  76.154  1.00 21.67 ? 1053 PHE   B C     1 
ATOM   16885 O  O     . PHE   B  1  1055 ? 6.093   74.528  75.397  1.00 21.31 ? 1053 PHE   B O     1 
ATOM   16886 C  CB    . PHE   B  1  1055 ? 7.413   71.919  76.956  1.00 20.73 ? 1053 PHE   B CB    1 
ATOM   16887 C  CG    . PHE   B  1  1055 ? 8.335   72.068  75.781  1.00 18.83 ? 1053 PHE   B CG    1 
ATOM   16888 C  CD1   . PHE   B  1  1055 ? 9.313   73.049  75.774  1.00 21.10 ? 1053 PHE   B CD1   1 
ATOM   16889 C  CD2   . PHE   B  1  1055 ? 8.234   71.205  74.699  1.00 18.91 ? 1053 PHE   B CD2   1 
ATOM   16890 C  CE1   . PHE   B  1  1055 ? 10.175  73.186  74.690  1.00 21.65 ? 1053 PHE   B CE1   1 
ATOM   16891 C  CE2   . PHE   B  1  1055 ? 9.080   71.343  73.603  1.00 20.30 ? 1053 PHE   B CE2   1 
ATOM   16892 C  CZ    . PHE   B  1  1055 ? 10.057  72.332  73.613  1.00 20.26 ? 1053 PHE   B CZ    1 
ATOM   16893 N  N     . ALA   B  1  1056 ? 4.594   72.963  76.012  1.00 20.36 ? 1054 ALA   B N     1 
ATOM   16894 C  CA    . ALA   B  1  1056 ? 3.684   73.323  74.931  1.00 20.08 ? 1054 ALA   B CA    1 
ATOM   16895 C  C     . ALA   B  1  1056 ? 3.180   74.753  75.087  1.00 21.49 ? 1054 ALA   B C     1 
ATOM   16896 O  O     . ALA   B  1  1056 ? 3.067   75.488  74.099  1.00 23.21 ? 1054 ALA   B O     1 
ATOM   16897 C  CB    . ALA   B  1  1056 ? 2.509   72.345  74.883  1.00 20.76 ? 1054 ALA   B CB    1 
ATOM   16898 N  N     . LYS   B  1  1057 ? 2.873   75.165  76.319  1.00 23.03 ? 1055 LYS   B N     1 
ATOM   16899 C  CA    . LYS   B  1  1057 ? 2.457   76.546  76.543  1.00 25.47 ? 1055 LYS   B CA    1 
ATOM   16900 C  C     . LYS   B  1  1057 ? 3.577   77.511  76.192  1.00 27.41 ? 1055 LYS   B C     1 
ATOM   16901 O  O     . LYS   B  1  1057 ? 3.331   78.576  75.610  1.00 27.14 ? 1055 LYS   B O     1 
ATOM   16902 C  CB    . LYS   B  1  1057 ? 2.034   76.747  77.995  1.00 28.11 ? 1055 LYS   B CB    1 
ATOM   16903 C  CG    . LYS   B  1  1057 ? 0.663   76.198  78.322  1.00 31.47 ? 1055 LYS   B CG    1 
ATOM   16904 C  CD    . LYS   B  1  1057 ? 0.297   76.497  79.758  1.00 27.05 ? 1055 LYS   B CD    1 
ATOM   16905 C  CE    . LYS   B  1  1057 ? 1.345   75.974  80.719  1.00 28.83 ? 1055 LYS   B CE    1 
ATOM   16906 N  NZ    . LYS   B  1  1057 ? 0.842   75.923  82.122  1.00 34.67 ? 1055 LYS   B NZ    1 
ATOM   16907 N  N     . TRP   B  1  1058 ? 4.816   77.158  76.547  1.00 24.27 ? 1056 TRP   B N     1 
ATOM   16908 C  CA    . TRP   B  1  1058 ? 5.946   78.014  76.201  1.00 27.88 ? 1056 TRP   B CA    1 
ATOM   16909 C  C     . TRP   B  1  1058 ? 6.099   78.131  74.693  1.00 25.35 ? 1056 TRP   B C     1 
ATOM   16910 O  O     . TRP   B  1  1058 ? 6.317   79.230  74.171  1.00 28.39 ? 1056 TRP   B O     1 
ATOM   16911 C  CB    . TRP   B  1  1058 ? 7.218   77.475  76.852  1.00 24.66 ? 1056 TRP   B CB    1 
ATOM   16912 C  CG    . TRP   B  1  1058 ? 8.478   78.220  76.491  1.00 27.27 ? 1056 TRP   B CG    1 
ATOM   16913 C  CD1   . TRP   B  1  1058 ? 8.905   79.414  77.007  1.00 32.46 ? 1056 TRP   B CD1   1 
ATOM   16914 C  CD2   . TRP   B  1  1058 ? 9.476   77.809  75.551  1.00 25.52 ? 1056 TRP   B CD2   1 
ATOM   16915 N  NE1   . TRP   B  1  1058 ? 10.103  79.771  76.439  1.00 31.79 ? 1056 TRP   B NE1   1 
ATOM   16916 C  CE2   . TRP   B  1  1058 ? 10.477  78.805  75.543  1.00 31.35 ? 1056 TRP   B CE2   1 
ATOM   16917 C  CE3   . TRP   B  1  1058 ? 9.622   76.699  74.713  1.00 26.95 ? 1056 TRP   B CE3   1 
ATOM   16918 C  CZ2   . TRP   B  1  1058 ? 11.611  78.717  74.736  1.00 29.09 ? 1056 TRP   B CZ2   1 
ATOM   16919 C  CZ3   . TRP   B  1  1058 ? 10.750  76.620  73.899  1.00 30.79 ? 1056 TRP   B CZ3   1 
ATOM   16920 C  CH2   . TRP   B  1  1058 ? 11.728  77.623  73.924  1.00 26.78 ? 1056 TRP   B CH2   1 
ATOM   16921 N  N     . LEU   B  1  1059 ? 5.961   77.013  73.974  1.00 22.87 ? 1057 LEU   B N     1 
ATOM   16922 C  CA    . LEU   B  1  1059 ? 6.053   77.042  72.521  1.00 25.88 ? 1057 LEU   B CA    1 
ATOM   16923 C  C     . LEU   B  1  1059 ? 4.980   77.936  71.918  1.00 31.58 ? 1057 LEU   B C     1 
ATOM   16924 O  O     . LEU   B  1  1059 ? 5.252   78.728  71.008  1.00 31.34 ? 1057 LEU   B O     1 
ATOM   16925 C  CB    . LEU   B  1  1059 ? 5.934   75.629  71.962  1.00 23.48 ? 1057 LEU   B CB    1 
ATOM   16926 C  CG    . LEU   B  1  1059 ? 7.133   74.725  72.221  1.00 21.63 ? 1057 LEU   B CG    1 
ATOM   16927 C  CD1   . LEU   B  1  1059 ? 6.823   73.332  71.747  1.00 22.29 ? 1057 LEU   B CD1   1 
ATOM   16928 C  CD2   . LEU   B  1  1059 ? 8.364   75.277  71.503  1.00 26.35 ? 1057 LEU   B CD2   1 
ATOM   16929 N  N     . ASP   B  1  1060 ? 3.743   77.819  72.402  1.00 27.40 ? 1058 ASP   B N     1 
ATOM   16930 C  CA    . ASP   B  1  1060 ? 2.693   78.676  71.858  1.00 29.63 ? 1058 ASP   B CA    1 
ATOM   16931 C  C     . ASP   B  1  1060 ? 2.954   80.138  72.181  1.00 35.47 ? 1058 ASP   B C     1 
ATOM   16932 O  O     . ASP   B  1  1060 ? 2.699   81.018  71.350  1.00 36.78 ? 1058 ASP   B O     1 
ATOM   16933 C  CB    . ASP   B  1  1060 ? 1.327   78.245  72.368  1.00 34.17 ? 1058 ASP   B CB    1 
ATOM   16934 C  CG    . ASP   B  1  1060 ? 0.651   77.267  71.439  1.00 36.11 ? 1058 ASP   B CG    1 
ATOM   16935 O  OD1   . ASP   B  1  1060 ? 0.650   77.497  70.203  1.00 41.91 ? 1058 ASP   B OD1   1 
ATOM   16936 O  OD2   . ASP   B  1  1060 ? 0.135   76.257  71.945  1.00 34.65 ? 1058 ASP   B OD2   1 
ATOM   16937 N  N     . GLY   B  1  1061 ? 3.468   80.413  73.381  1.00 33.06 ? 1059 GLY   B N     1 
ATOM   16938 C  CA    . GLY   B  1  1061 ? 3.802   81.780  73.738  1.00 33.27 ? 1059 GLY   B CA    1 
ATOM   16939 C  C     . GLY   B  1  1061 ? 4.771   82.422  72.763  1.00 36.94 ? 1059 GLY   B C     1 
ATOM   16940 O  O     . GLY   B  1  1061 ? 4.673   83.617  72.474  1.00 38.24 ? 1059 GLY   B O     1 
ATOM   16941 N  N     . LYS   B  1  1062 ? 5.709   81.642  72.232  1.00 34.65 ? 1060 LYS   B N     1 
ATOM   16942 C  CA    . LYS   B  1  1062 ? 6.682   82.171  71.288  1.00 33.89 ? 1060 LYS   B CA    1 
ATOM   16943 C  C     . LYS   B  1  1062 ? 6.276   81.969  69.830  1.00 40.50 ? 1060 LYS   B C     1 
ATOM   16944 O  O     . LYS   B  1  1062 ? 7.080   82.238  68.933  1.00 41.34 ? 1060 LYS   B O     1 
ATOM   16945 C  CB    . LYS   B  1  1062 ? 8.078   81.600  71.564  1.00 37.32 ? 1060 LYS   B CB    1 
ATOM   16946 C  CG    . LYS   B  1  1062 ? 8.228   80.125  71.302  1.00 40.53 ? 1060 LYS   B CG    1 
ATOM   16947 C  CD    . LYS   B  1  1062 ? 9.620   79.662  71.723  1.00 35.94 ? 1060 LYS   B CD    1 
ATOM   16948 C  CE    . LYS   B  1  1062 ? 10.700  80.406  70.944  1.00 35.63 ? 1060 LYS   B CE    1 
ATOM   16949 N  NZ    . LYS   B  1  1062 ? 12.040  80.273  71.574  1.00 39.87 ? 1060 LYS   B NZ    1 
ATOM   16950 N  N     . GLY   B  1  1063 ? 5.053   81.509  69.574  1.00 39.05 ? 1061 GLY   B N     1 
ATOM   16951 C  CA    . GLY   B  1  1063 ? 4.553   81.412  68.219  1.00 38.11 ? 1061 GLY   B CA    1 
ATOM   16952 C  C     . GLY   B  1  1063 ? 4.954   80.174  67.453  1.00 42.78 ? 1061 GLY   B C     1 
ATOM   16953 O  O     . GLY   B  1  1063 ? 4.641   80.078  66.260  1.00 41.10 ? 1061 GLY   B O     1 
ATOM   16954 N  N     . ALA   B  1  1064 ? 5.629   79.216  68.091  1.00 35.48 ? 1062 ALA   B N     1 
ATOM   16955 C  CA    . ALA   B  1  1064 ? 6.026   77.978  67.419  1.00 35.20 ? 1062 ALA   B CA    1 
ATOM   16956 C  C     . ALA   B  1  1064 ? 4.816   77.044  67.362  1.00 34.46 ? 1062 ALA   B C     1 
ATOM   16957 O  O     . ALA   B  1  1064 ? 4.711   76.048  68.081  1.00 29.55 ? 1062 ALA   B O     1 
ATOM   16958 C  CB    . ALA   B  1  1064 ? 7.216   77.339  68.125  1.00 32.49 ? 1062 ALA   B CB    1 
ATOM   16959 N  N     . ARG   B  1  1065 ? 3.886   77.387  66.466  1.00 33.53 ? 1063 ARG   B N     1 
ATOM   16960 C  CA    . ARG   B  1  1065 ? 2.578   76.734  66.451  1.00 31.24 ? 1063 ARG   B CA    1 
ATOM   16961 C  C     . ARG   B  1  1065 ? 2.688   75.261  66.080  1.00 30.25 ? 1063 ARG   B C     1 
ATOM   16962 O  O     . ARG   B  1  1065 ? 2.086   74.400  66.736  1.00 31.01 ? 1063 ARG   B O     1 
ATOM   16963 C  CB    . ARG   B  1  1065 ? 1.642   77.466  65.486  1.00 37.63 ? 1063 ARG   B CB    1 
ATOM   16964 N  N     . ALA   B  1  1066 ? 3.440   74.946  65.024  1.00 27.71 ? 1064 ALA   B N     1 
ATOM   16965 C  CA    . ALA   B  1  1066 ? 3.595   73.551  64.639  1.00 27.10 ? 1064 ALA   B CA    1 
ATOM   16966 C  C     . ALA   B  1  1066 ? 4.233   72.750  65.762  1.00 27.08 ? 1064 ALA   B C     1 
ATOM   16967 O  O     . ALA   B  1  1066 ? 3.821   71.619  66.042  1.00 27.08 ? 1064 ALA   B O     1 
ATOM   16968 C  CB    . ALA   B  1  1066 ? 4.438   73.440  63.369  1.00 30.06 ? 1064 ALA   B CB    1 
ATOM   16969 N  N     . GLU   B  1  1067 ? 5.240   73.322  66.423  1.00 24.41 ? 1065 GLU   B N     1 
ATOM   16970 C  CA    . GLU   B  1  1067 ? 5.924   72.579  67.472  1.00 26.28 ? 1065 GLU   B CA    1 
ATOM   16971 C  C     . GLU   B  1  1067 ? 5.030   72.390  68.690  1.00 22.72 ? 1065 GLU   B C     1 
ATOM   16972 O  O     . GLU   B  1  1067 ? 5.048   71.323  69.314  1.00 22.48 ? 1065 GLU   B O     1 
ATOM   16973 C  CB    . GLU   B  1  1067 ? 7.234   73.276  67.842  1.00 26.34 ? 1065 GLU   B CB    1 
ATOM   16974 C  CG    . GLU   B  1  1067 ? 8.306   73.164  66.767  1.00 26.03 ? 1065 GLU   B CG    1 
ATOM   16975 C  CD    . GLU   B  1  1067 ? 8.128   74.174  65.662  1.00 30.10 ? 1065 GLU   B CD    1 
ATOM   16976 O  OE1   . GLU   B  1  1067 ? 7.249   75.056  65.786  1.00 30.55 ? 1065 GLU   B OE1   1 
ATOM   16977 O  OE2   . GLU   B  1  1067 ? 8.873   74.085  64.660  1.00 32.42 ? 1065 GLU   B OE2   1 
ATOM   16978 N  N     . ALA   B  1  1068 ? 4.247   73.411  69.038  1.00 23.15 ? 1066 ALA   B N     1 
ATOM   16979 C  CA    . ALA   B  1  1068 ? 3.324   73.286  70.161  1.00 24.97 ? 1066 ALA   B CA    1 
ATOM   16980 C  C     . ALA   B  1  1068 ? 2.288   72.206  69.892  1.00 22.18 ? 1066 ALA   B C     1 
ATOM   16981 O  O     . ALA   B  1  1068 ? 1.940   71.432  70.791  1.00 21.36 ? 1066 ALA   B O     1 
ATOM   16982 C  CB    . ALA   B  1  1068 ? 2.640   74.625  70.421  1.00 23.45 ? 1066 ALA   B CB    1 
ATOM   16983 N  N     . GLU   B  1  1069 ? 1.791   72.129  68.653  1.00 21.45 ? 1067 GLU   B N     1 
ATOM   16984 C  CA    . GLU   B  1  1069 ? 0.871   71.058  68.285  1.00 25.62 ? 1067 GLU   B CA    1 
ATOM   16985 C  C     . GLU   B  1  1069 ? 1.539   69.691  68.377  1.00 25.57 ? 1067 GLU   B C     1 
ATOM   16986 O  O     . GLU   B  1  1069 ? 0.942   68.731  68.885  1.00 23.81 ? 1067 GLU   B O     1 
ATOM   16987 C  CB    . GLU   B  1  1069 ? 0.335   71.305  66.871  1.00 29.88 ? 1067 GLU   B CB    1 
ATOM   16988 C  CG    . GLU   B  1  1069 ? -0.538  70.188  66.317  1.00 30.51 ? 1067 GLU   B CG    1 
ATOM   16989 C  CD    . GLU   B  1  1069 ? -1.891  70.086  67.014  1.00 39.29 ? 1067 GLU   B CD    1 
ATOM   16990 O  OE1   . GLU   B  1  1069 ? -2.246  71.001  67.787  1.00 38.29 ? 1067 GLU   B OE1   1 
ATOM   16991 O  OE2   . GLU   B  1  1069 ? -2.601  69.084  66.787  1.00 47.24 ? 1067 GLU   B OE2   1 
ATOM   16992 N  N     . ALA   B  1  1070 ? 2.775   69.578  67.890  1.00 23.17 ? 1068 ALA   B N     1 
ATOM   16993 C  CA    . ALA   B  1  1070 ? 3.499   68.324  68.043  1.00 25.09 ? 1068 ALA   B CA    1 
ATOM   16994 C  C     . ALA   B  1  1070 ? 3.695   67.996  69.516  1.00 18.61 ? 1068 ALA   B C     1 
ATOM   16995 O  O     . ALA   B  1  1070 ? 3.605   66.831  69.914  1.00 21.88 ? 1068 ALA   B O     1 
ATOM   16996 C  CB    . ALA   B  1  1070 ? 4.850   68.401  67.326  1.00 26.72 ? 1068 ALA   B CB    1 
ATOM   16997 N  N     . ALA   B  1  1071 ? 3.947   69.013  70.339  1.00 19.93 ? 1069 ALA   B N     1 
ATOM   16998 C  CA    . ALA   B  1  1071 ? 4.128   68.761  71.764  1.00 18.61 ? 1069 ALA   B CA    1 
ATOM   16999 C  C     . ALA   B  1  1071 ? 2.844   68.225  72.387  1.00 19.25 ? 1069 ALA   B C     1 
ATOM   17000 O  O     . ALA   B  1  1071 ? 2.866   67.221  73.116  1.00 19.71 ? 1069 ALA   B O     1 
ATOM   17001 C  CB    . ALA   B  1  1071 ? 4.609   70.020  72.485  1.00 17.70 ? 1069 ALA   B CB    1 
ATOM   17002 N  N     . ARG   B  1  1072 ? 1.707   68.868  72.100  1.00 19.19 ? 1070 ARG   B N     1 
ATOM   17003 C  CA    A ARG   B  1  1072 ? 0.437   68.383  72.639  0.58 20.04 ? 1070 ARG   B CA    1 
ATOM   17004 C  CA    B ARG   B  1  1072 ? 0.450   68.377  72.654  0.42 20.06 ? 1070 ARG   B CA    1 
ATOM   17005 C  C     . ARG   B  1  1072 ? 0.137   66.976  72.147  1.00 21.01 ? 1070 ARG   B C     1 
ATOM   17006 O  O     . ARG   B  1  1072 ? -0.329  66.125  72.914  1.00 19.27 ? 1070 ARG   B O     1 
ATOM   17007 C  CB    A ARG   B  1  1072 ? -0.701  69.324  72.244  0.58 21.89 ? 1070 ARG   B CB    1 
ATOM   17008 C  CB    B ARG   B  1  1072 ? -0.687  69.353  72.353  0.42 21.92 ? 1070 ARG   B CB    1 
ATOM   17009 C  CG    A ARG   B  1  1072 ? -0.735  70.620  73.015  0.58 25.21 ? 1070 ARG   B CG    1 
ATOM   17010 C  CG    B ARG   B  1  1072 ? -0.425  70.731  72.914  0.42 24.62 ? 1070 ARG   B CG    1 
ATOM   17011 C  CD    A ARG   B  1  1072 ? -1.957  71.436  72.614  0.58 22.81 ? 1070 ARG   B CD    1 
ATOM   17012 C  CD    B ARG   B  1  1072 ? -1.678  71.590  72.967  0.42 23.08 ? 1070 ARG   B CD    1 
ATOM   17013 N  NE    A ARG   B  1  1072 ? -1.886  71.878  71.226  0.58 25.02 ? 1070 ARG   B NE    1 
ATOM   17014 N  NE    B ARG   B  1  1072 ? -1.355  72.917  73.472  0.42 25.35 ? 1070 ARG   B NE    1 
ATOM   17015 C  CZ    A ARG   B  1  1072 ? -1.389  73.047  70.846  0.58 27.78 ? 1070 ARG   B CZ    1 
ATOM   17016 C  CZ    B ARG   B  1  1072 ? -1.159  73.201  74.751  0.42 24.52 ? 1070 ARG   B CZ    1 
ATOM   17017 N  NH1   A ARG   B  1  1072 ? -0.937  73.923  71.727  0.58 25.76 ? 1070 ARG   B NH1   1 
ATOM   17018 N  NH1   B ARG   B  1  1072 ? -1.330  72.290  75.697  0.42 27.72 ? 1070 ARG   B NH1   1 
ATOM   17019 N  NH2   A ARG   B  1  1072 ? -1.342  73.342  69.551  0.58 23.86 ? 1070 ARG   B NH2   1 
ATOM   17020 N  NH2   B ARG   B  1  1072 ? -0.765  74.422  75.089  0.42 25.61 ? 1070 ARG   B NH2   1 
ATOM   17021 N  N     . ASN   B  1  1073 ? 0.404   66.710  70.864  1.00 18.82 ? 1071 ASN   B N     1 
ATOM   17022 C  CA    . ASN   B  1  1073 ? 0.142   65.383  70.327  1.00 20.01 ? 1071 ASN   B CA    1 
ATOM   17023 C  C     . ASN   B  1  1073 ? 1.010   64.338  71.002  1.00 20.53 ? 1071 ASN   B C     1 
ATOM   17024 O  O     . ASN   B  1  1073 ? 0.545   63.226  71.286  1.00 21.71 ? 1071 ASN   B O     1 
ATOM   17025 C  CB    . ASN   B  1  1073 ? 0.357   65.376  68.817  1.00 21.85 ? 1071 ASN   B CB    1 
ATOM   17026 C  CG    . ASN   B  1  1073 ? -0.737  66.111  68.092  1.00 29.51 ? 1071 ASN   B CG    1 
ATOM   17027 O  OD1   . ASN   B  1  1073 ? -1.843  66.265  68.617  1.00 30.42 ? 1071 ASN   B OD1   1 
ATOM   17028 N  ND2   . ASN   B  1  1073 ? -0.444  66.578  66.888  1.00 32.78 ? 1071 ASN   B ND2   1 
ATOM   17029 N  N     . ALA   B  1  1074 ? 2.281   64.670  71.252  1.00 18.56 ? 1072 ALA   B N     1 
ATOM   17030 C  CA    . ALA   B  1  1074 ? 3.149   63.743  71.969  1.00 20.18 ? 1072 ALA   B CA    1 
ATOM   17031 C  C     . ALA   B  1  1074 ? 2.650   63.517  73.388  1.00 15.90 ? 1072 ALA   B C     1 
ATOM   17032 O  O     . ALA   B  1  1074 ? 2.673   62.386  73.888  1.00 18.37 ? 1072 ALA   B O     1 
ATOM   17033 C  CB    . ALA   B  1  1074 ? 4.582   64.278  71.987  1.00 19.08 ? 1072 ALA   B CB    1 
ATOM   17034 N  N     . GLY   B  1  1075 ? 2.203   64.579  74.052  1.00 16.81 ? 1073 GLY   B N     1 
ATOM   17035 C  CA    . GLY   B  1  1075 ? 1.684   64.419  75.399  1.00 19.39 ? 1073 GLY   B CA    1 
ATOM   17036 C  C     . GLY   B  1  1075 ? 0.532   63.436  75.447  1.00 20.52 ? 1073 GLY   B C     1 
ATOM   17037 O  O     . GLY   B  1  1075 ? 0.412   62.644  76.390  1.00 20.15 ? 1073 GLY   B O     1 
ATOM   17038 N  N     . SER   B  1  1076 ? -0.304  63.447  74.411  1.00 20.56 ? 1074 SER   B N     1 
ATOM   17039 C  CA    . SER   B  1  1076 ? -1.470  62.576  74.396  1.00 19.21 ? 1074 SER   B CA    1 
ATOM   17040 C  C     . SER   B  1  1076 ? -1.103  61.160  73.983  1.00 19.57 ? 1074 SER   B C     1 
ATOM   17041 O  O     . SER   B  1  1076 ? -1.567  60.197  74.600  1.00 22.21 ? 1074 SER   B O     1 
ATOM   17042 C  CB    . SER   B  1  1076 ? -2.532  63.152  73.468  1.00 22.25 ? 1074 SER   B CB    1 
ATOM   17043 O  OG    . SER   B  1  1076 ? -3.116  64.300  74.057  1.00 25.04 ? 1074 SER   B OG    1 
ATOM   17044 N  N     . SER   B  1  1077 ? -0.239  61.007  72.979  1.00 18.58 ? 1075 SER   B N     1 
ATOM   17045 C  CA    A SER   B  1  1077 ? 0.106   59.685  72.461  0.31 22.63 ? 1075 SER   B CA    1 
ATOM   17046 C  CA    B SER   B  1  1077 ? 0.049   59.663  72.505  0.69 22.65 ? 1075 SER   B CA    1 
ATOM   17047 C  C     . SER   B  1  1077 ? 1.046   58.925  73.385  1.00 20.14 ? 1075 SER   B C     1 
ATOM   17048 O  O     . SER   B  1  1077 ? 1.100   57.690  73.323  1.00 24.63 ? 1075 SER   B O     1 
ATOM   17049 C  CB    A SER   B  1  1077 ? 0.759   59.816  71.087  0.31 25.14 ? 1075 SER   B CB    1 
ATOM   17050 C  CB    B SER   B  1  1077 ? 0.520   59.683  71.054  0.69 25.59 ? 1075 SER   B CB    1 
ATOM   17051 O  OG    A SER   B  1  1077 ? -0.108  60.444  70.161  0.31 24.90 ? 1075 SER   B OG    1 
ATOM   17052 O  OG    B SER   B  1  1077 ? 1.832   60.184  70.961  0.69 24.32 ? 1075 SER   B OG    1 
ATOM   17053 N  N     . SER   B  1  1078 ? 1.800   59.637  74.210  1.00 17.52 ? 1076 SER   B N     1 
ATOM   17054 C  CA    . SER   B  1  1078 ? 2.688   58.986  75.159  1.00 16.98 ? 1076 SER   B CA    1 
ATOM   17055 C  C     . SER   B  1  1078 ? 1.895   58.025  76.025  1.00 16.61 ? 1076 SER   B C     1 
ATOM   17056 O  O     . SER   B  1  1078 ? 0.780   58.332  76.460  1.00 17.27 ? 1076 SER   B O     1 
ATOM   17057 C  CB    . SER   B  1  1078 ? 3.291   60.043  76.068  1.00 17.07 ? 1076 SER   B CB    1 
ATOM   17058 O  OG    . SER   B  1  1078 ? 3.993   59.416  77.131  1.00 15.64 ? 1076 SER   B OG    1 
ATOM   17059 N  N     . ALA   B  1  1079 ? 2.463   56.854  76.276  1.00 14.72 ? 1077 ALA   B N     1 
ATOM   17060 C  CA    . ALA   B  1  1079 ? 1.833   55.885  77.155  1.00 15.07 ? 1077 ALA   B CA    1 
ATOM   17061 C  C     . ALA   B  1  1079 ? 2.469   55.895  78.530  1.00 15.30 ? 1077 ALA   B C     1 
ATOM   17062 O  O     . ALA   B  1  1079 ? 2.231   54.983  79.322  1.00 14.88 ? 1077 ALA   B O     1 
ATOM   17063 C  CB    . ALA   B  1  1079 ? 1.854   54.481  76.541  1.00 15.74 ? 1077 ALA   B CB    1 
ATOM   17064 N  N     . LEU   B  1  1080 ? 3.286   56.901  78.821  1.00 14.00 ? 1078 LEU   B N     1 
ATOM   17065 C  CA    . LEU   B  1  1080 ? 3.834   57.058  80.157  1.00 14.27 ? 1078 LEU   B CA    1 
ATOM   17066 C  C     . LEU   B  1  1080 ? 2.706   57.025  81.172  1.00 14.29 ? 1078 LEU   B C     1 
ATOM   17067 O  O     . LEU   B  1  1080 ? 1.709   57.740  81.038  1.00 15.78 ? 1078 LEU   B O     1 
ATOM   17068 C  CB    . LEU   B  1  1080 ? 4.534   58.409  80.227  1.00 14.96 ? 1078 LEU   B CB    1 
ATOM   17069 C  CG    . LEU   B  1  1080 ? 4.979   58.826  81.621  1.00 15.37 ? 1078 LEU   B CG    1 
ATOM   17070 C  CD1   . LEU   B  1  1080 ? 6.129   57.956  82.079  1.00 17.09 ? 1078 LEU   B CD1   1 
ATOM   17071 C  CD2   . LEU   B  1  1080 ? 5.354   60.292  81.629  1.00 16.67 ? 1078 LEU   B CD2   1 
ATOM   17072 N  N     . GLY   B  1  1081 ? 2.873   56.197  82.200  1.00 13.60 ? 1079 GLY   B N     1 
ATOM   17073 C  CA    . GLY   B  1  1081 ? 1.860   56.072  83.223  1.00 14.78 ? 1079 GLY   B CA    1 
ATOM   17074 C  C     . GLY   B  1  1081 ? 0.910   54.916  83.009  1.00 16.45 ? 1079 GLY   B C     1 
ATOM   17075 O  O     . GLY   B  1  1081 ? 0.048   54.680  83.868  1.00 17.92 ? 1079 GLY   B O     1 
ATOM   17076 N  N     . LEU   B  1  1082 ? 1.022   54.206  81.894  1.00 15.44 ? 1080 LEU   B N     1 
ATOM   17077 C  CA    A LEU   B  1  1082 ? 0.274   52.969  81.725  0.45 16.52 ? 1080 LEU   B CA    1 
ATOM   17078 C  CA    B LEU   B  1  1082 ? 0.274   52.968  81.726  0.55 16.52 ? 1080 LEU   B CA    1 
ATOM   17079 C  C     . LEU   B  1  1082 ? 0.542   52.058  82.911  1.00 16.01 ? 1080 LEU   B C     1 
ATOM   17080 O  O     . LEU   B  1  1082 ? 1.675   51.936  83.370  1.00 16.58 ? 1080 LEU   B O     1 
ATOM   17081 C  CB    A LEU   B  1  1082 ? 0.728   52.283  80.436  0.45 16.19 ? 1080 LEU   B CB    1 
ATOM   17082 C  CB    B LEU   B  1  1082 ? 0.732   52.280  80.441  0.55 16.19 ? 1080 LEU   B CB    1 
ATOM   17083 C  CG    A LEU   B  1  1082 ? 0.123   50.918  80.104  0.45 16.30 ? 1080 LEU   B CG    1 
ATOM   17084 C  CG    B LEU   B  1  1082 ? 0.180   50.896  80.087  0.55 16.29 ? 1080 LEU   B CG    1 
ATOM   17085 C  CD1   A LEU   B  1  1082 ? -1.368  51.005  80.064  0.45 19.19 ? 1080 LEU   B CD1   1 
ATOM   17086 C  CD1   B LEU   B  1  1082 ? 0.222   50.715  78.579  0.55 16.47 ? 1080 LEU   B CD1   1 
ATOM   17087 C  CD2   A LEU   B  1  1082 ? 0.628   50.404  78.768  0.45 17.44 ? 1080 LEU   B CD2   1 
ATOM   17088 C  CD2   B LEU   B  1  1082 ? 0.957   49.761  80.769  0.55 14.45 ? 1080 LEU   B CD2   1 
ATOM   17089 N  N     . ASP   B  1  1083 ? -0.506  51.413  83.404  1.00 17.20 ? 1081 ASP   B N     1 
ATOM   17090 C  CA    . ASP   B  1  1083 ? -0.392  50.627  84.627  1.00 20.77 ? 1081 ASP   B CA    1 
ATOM   17091 C  C     . ASP   B  1  1083 ? -1.466  49.549  84.524  1.00 19.37 ? 1081 ASP   B C     1 
ATOM   17092 O  O     . ASP   B  1  1083 ? -2.644  49.808  84.806  1.00 23.21 ? 1081 ASP   B O     1 
ATOM   17093 C  CB    . ASP   B  1  1083 ? -0.618  51.540  85.820  1.00 21.20 ? 1081 ASP   B CB    1 
ATOM   17094 C  CG    . ASP   B  1  1083 ? -0.480  50.829  87.147  1.00 32.59 ? 1081 ASP   B CG    1 
ATOM   17095 O  OD1   . ASP   B  1  1083 ? 0.112   49.735  87.189  1.00 34.58 ? 1081 ASP   B OD1   1 
ATOM   17096 O  OD2   . ASP   B  1  1083 ? -0.972  51.376  88.158  1.00 36.93 ? 1081 ASP   B OD2   1 
ATOM   17097 N  N     . LEU   B  1  1084 ? -1.056  48.357  84.113  1.00 17.21 ? 1082 LEU   B N     1 
ATOM   17098 C  CA    . LEU   B  1  1084 ? -1.960  47.281  83.746  1.00 19.05 ? 1082 LEU   B CA    1 
ATOM   17099 C  C     . LEU   B  1  1084 ? -1.700  46.080  84.637  1.00 17.56 ? 1082 LEU   B C     1 
ATOM   17100 O  O     . LEU   B  1  1084 ? -0.571  45.832  85.062  1.00 17.60 ? 1082 LEU   B O     1 
ATOM   17101 C  CB    . LEU   B  1  1084 ? -1.705  46.820  82.305  1.00 21.66 ? 1082 LEU   B CB    1 
ATOM   17102 C  CG    . LEU   B  1  1084 ? -2.022  47.777  81.159  1.00 25.22 ? 1082 LEU   B CG    1 
ATOM   17103 C  CD1   . LEU   B  1  1084 ? -1.640  47.155  79.832  1.00 25.49 ? 1082 LEU   B CD1   1 
ATOM   17104 C  CD2   . LEU   B  1  1084 ? -3.491  48.186  81.188  1.00 27.53 ? 1082 LEU   B CD2   1 
ATOM   17105 N  N     . GLU   B  1  1085 ? -2.746  45.324  84.914  1.00 16.68 ? 1083 GLU   B N     1 
ATOM   17106 C  CA    . GLU   B  1  1085 ? -2.590  43.977  85.427  1.00 16.14 ? 1083 GLU   B CA    1 
ATOM   17107 C  C     . GLU   B  1  1085 ? -2.777  43.006  84.277  1.00 16.97 ? 1083 GLU   B C     1 
ATOM   17108 O  O     . GLU   B  1  1085 ? -3.780  43.076  83.552  1.00 19.61 ? 1083 GLU   B O     1 
ATOM   17109 C  CB    . GLU   B  1  1085 ? -3.589  43.669  86.544  1.00 18.11 ? 1083 GLU   B CB    1 
ATOM   17110 C  CG    . GLU   B  1  1085 ? -3.332  42.262  87.064  1.00 19.17 ? 1083 GLU   B CG    1 
ATOM   17111 C  CD    . GLU   B  1  1085 ? -4.112  41.881  88.284  1.00 25.32 ? 1083 GLU   B CD    1 
ATOM   17112 O  OE1   . GLU   B  1  1085 ? -4.695  42.771  88.938  1.00 28.80 ? 1083 GLU   B OE1   1 
ATOM   17113 O  OE2   . GLU   B  1  1085 ? -4.141  40.669  88.583  1.00 23.85 ? 1083 GLU   B OE2   1 
ATOM   17114 N  N     . LEU   B  1  1086 ? -1.820  42.132  84.096  1.00 15.91 ? 1084 LEU   B N     1 
ATOM   17115 C  CA    . LEU   B  1  1086 ? -1.830  41.165  83.013  1.00 15.36 ? 1084 LEU   B CA    1 
ATOM   17116 C  C     . LEU   B  1  1086 ? -2.489  39.866  83.474  1.00 19.26 ? 1084 LEU   B C     1 
ATOM   17117 O  O     . LEU   B  1  1086 ? -2.296  39.445  84.617  1.00 20.31 ? 1084 LEU   B O     1 
ATOM   17118 C  CB    . LEU   B  1  1086 ? -0.407  40.880  82.548  1.00 17.08 ? 1084 LEU   B CB    1 
ATOM   17119 C  CG    . LEU   B  1  1086 ? 0.324   42.128  82.059  1.00 16.13 ? 1084 LEU   B CG    1 
ATOM   17120 C  CD1   . LEU   B  1  1086 ? 1.728   41.776  81.617  1.00 19.53 ? 1084 LEU   B CD1   1 
ATOM   17121 C  CD2   . LEU   B  1  1086 ? -0.424  42.787  80.906  1.00 21.49 ? 1084 LEU   B CD2   1 
ATOM   17122 N  N     . PRO   B  1  1087 ? -3.266  39.223  82.607  1.00 16.89 ? 1085 PRO   B N     1 
ATOM   17123 C  CA    . PRO   B  1  1087 ? -3.864  37.934  82.966  1.00 19.44 ? 1085 PRO   B CA    1 
ATOM   17124 C  C     . PRO   B  1  1087 ? -2.796  36.901  83.257  1.00 19.27 ? 1085 PRO   B C     1 
ATOM   17125 O  O     . PRO   B  1  1087 ? -1.784  36.807  82.563  1.00 19.73 ? 1085 PRO   B O     1 
ATOM   17126 C  CB    . PRO   B  1  1087 ? -4.652  37.548  81.708  1.00 20.57 ? 1085 PRO   B CB    1 
ATOM   17127 C  CG    . PRO   B  1  1087 ? -4.949  38.828  81.040  1.00 22.30 ? 1085 PRO   B CG    1 
ATOM   17128 C  CD    . PRO   B  1  1087 ? -3.770  39.722  81.311  1.00 19.96 ? 1085 PRO   B CD    1 
ATOM   17129 N  N     . GLY   B  1  1088 ? -3.026  36.119  84.289  1.00 19.08 ? 1086 GLY   B N     1 
ATOM   17130 C  CA    . GLY   B  1  1088 ? -2.092  35.088  84.650  1.00 18.08 ? 1086 GLY   B CA    1 
ATOM   17131 C  C     . GLY   B  1  1088 ? -2.737  34.144  85.634  1.00 15.74 ? 1086 GLY   B C     1 
ATOM   17132 O  O     . GLY   B  1  1088 ? -3.959  34.086  85.772  1.00 17.40 ? 1086 GLY   B O     1 
ATOM   17133 N  N     . PRO   B  1  1089 ? -1.913  33.408  86.360  1.00 16.55 ? 1087 PRO   B N     1 
ATOM   17134 C  CA    . PRO   B  1  1089 ? -2.442  32.438  87.321  1.00 15.80 ? 1087 PRO   B CA    1 
ATOM   17135 C  C     . PRO   B  1  1089 ? -3.063  33.117  88.527  1.00 16.52 ? 1087 PRO   B C     1 
ATOM   17136 O  O     . PRO   B  1  1089 ? -2.750  34.258  88.876  1.00 17.71 ? 1087 PRO   B O     1 
ATOM   17137 C  CB    . PRO   B  1  1089 ? -1.197  31.649  87.727  1.00 19.66 ? 1087 PRO   B CB    1 
ATOM   17138 C  CG    . PRO   B  1  1089 ? -0.070  32.655  87.558  1.00 21.48 ? 1087 PRO   B CG    1 
ATOM   17139 C  CD    . PRO   B  1  1089 ? -0.441  33.469  86.364  1.00 17.46 ? 1087 PRO   B CD    1 
ATOM   17140 N  N     . VAL   B  1  1090 ? -3.963  32.376  89.176  1.00 15.48 ? 1088 VAL   B N     1 
ATOM   17141 C  CA    . VAL   B  1  1090 ? -4.474  32.824  90.455  1.00 16.90 ? 1088 VAL   B CA    1 
ATOM   17142 C  C     . VAL   B  1  1090 ? -3.341  32.876  91.465  1.00 16.65 ? 1088 VAL   B C     1 
ATOM   17143 O  O     . VAL   B  1  1090 ? -2.298  32.231  91.315  1.00 16.73 ? 1088 VAL   B O     1 
ATOM   17144 C  CB    . VAL   B  1  1090 ? -5.603  31.928  90.978  1.00 16.44 ? 1088 VAL   B CB    1 
ATOM   17145 C  CG1   . VAL   B  1  1090 ? -6.745  31.879  89.981  1.00 17.39 ? 1088 VAL   B CG1   1 
ATOM   17146 C  CG2   . VAL   B  1  1090 ? -5.088  30.528  91.324  1.00 18.51 ? 1088 VAL   B CG2   1 
ATOM   17147 N  N     . GLY   B  1  1091 ? -3.557  33.667  92.511  1.00 16.05 ? 1089 GLY   B N     1 
ATOM   17148 C  CA    . GLY   B  1  1091 ? -2.571  33.751  93.576  1.00 16.19 ? 1089 GLY   B CA    1 
ATOM   17149 C  C     . GLY   B  1  1091 ? -1.350  34.544  93.210  1.00 16.43 ? 1089 GLY   B C     1 
ATOM   17150 O  O     . GLY   B  1  1091 ? -0.324  34.456  93.892  1.00 15.56 ? 1089 GLY   B O     1 
ATOM   17151 N  N     . GLU   B  1  1092 ? -1.426  35.311  92.136  1.00 16.90 ? 1090 GLU   B N     1 
ATOM   17152 C  CA    . GLU   B  1  1092 ? -0.345  36.165  91.704  1.00 15.71 ? 1090 GLU   B CA    1 
ATOM   17153 C  C     . GLU   B  1  1092 ? -0.986  37.385  91.082  1.00 16.52 ? 1090 GLU   B C     1 
ATOM   17154 O  O     . GLU   B  1  1092 ? -2.060  37.287  90.478  1.00 18.62 ? 1090 GLU   B O     1 
ATOM   17155 C  CB    . GLU   B  1  1092 ? 0.473   35.450  90.628  1.00 19.87 ? 1090 GLU   B CB    1 
ATOM   17156 C  CG    . GLU   B  1  1092 ? 1.932   35.409  90.877  1.00 26.46 ? 1090 GLU   B CG    1 
ATOM   17157 C  CD    . GLU   B  1  1092 ? 2.653   34.564  89.850  1.00 24.11 ? 1090 GLU   B CD    1 
ATOM   17158 O  OE1   . GLU   B  1  1092 ? 2.504   34.840  88.639  1.00 20.54 ? 1090 GLU   B OE1   1 
ATOM   17159 O  OE2   . GLU   B  1  1092 ? 3.357   33.617  90.258  1.00 24.71 ? 1090 GLU   B OE2   1 
ATOM   17160 N  N     . ARG   B  1  1093 ? -0.359  38.535  91.263  1.00 16.35 ? 1091 ARG   B N     1 
ATOM   17161 C  CA    . ARG   B  1  1093 ? -0.723  39.735  90.527  1.00 14.90 ? 1091 ARG   B CA    1 
ATOM   17162 C  C     . ARG   B  1  1093 ? 0.475   40.130  89.688  1.00 15.75 ? 1091 ARG   B C     1 
ATOM   17163 O  O     . ARG   B  1  1093 ? 1.581   40.321  90.208  1.00 16.34 ? 1091 ARG   B O     1 
ATOM   17164 C  CB    . ARG   B  1  1093 ? -1.127  40.881  91.456  1.00 17.97 ? 1091 ARG   B CB    1 
ATOM   17165 C  CG    . ARG   B  1  1093 ? -2.570  40.820  91.888  1.00 27.45 ? 1091 ARG   B CG    1 
ATOM   17166 C  CD    . ARG   B  1  1093 ? -3.046  42.194  92.351  1.00 34.38 ? 1091 ARG   B CD    1 
ATOM   17167 N  NE    . ARG   B  1  1093 ? -2.247  42.670  93.469  1.00 38.13 ? 1091 ARG   B NE    1 
ATOM   17168 C  CZ    . ARG   B  1  1093 ? -2.497  42.382  94.739  1.00 48.97 ? 1091 ARG   B CZ    1 
ATOM   17169 N  NH1   . ARG   B  1  1093 ? -3.539  41.641  95.086  1.00 45.67 ? 1091 ARG   B NH1   1 
ATOM   17170 N  NH2   . ARG   B  1  1093 ? -1.679  42.842  95.684  1.00 46.29 ? 1091 ARG   B NH2   1 
ATOM   17171 N  N     . ASN   B  1  1094 ? 0.259   40.228  88.393  1.00 13.52 ? 1092 ASN   B N     1 
ATOM   17172 C  CA    . ASN   B  1  1094 ? 1.343   40.464  87.457  1.00 13.16 ? 1092 ASN   B CA    1 
ATOM   17173 C  C     . ASN   B  1  1094 ? 1.058   41.792  86.793  1.00 14.54 ? 1092 ASN   B C     1 
ATOM   17174 O  O     . ASN   B  1  1094 ? 0.052   41.933  86.082  1.00 16.24 ? 1092 ASN   B O     1 
ATOM   17175 C  CB    . ASN   B  1  1094 ? 1.426   39.316  86.472  1.00 14.39 ? 1092 ASN   B CB    1 
ATOM   17176 C  CG    . ASN   B  1  1094 ? 2.021   38.112  87.108  1.00 14.94 ? 1092 ASN   B CG    1 
ATOM   17177 O  OD1   . ASN   B  1  1094 ? 3.203   38.111  87.393  1.00 15.25 ? 1092 ASN   B OD1   1 
ATOM   17178 N  ND2   . ASN   B  1  1094 ? 1.215   37.103  87.384  1.00 16.26 ? 1092 ASN   B ND2   1 
ATOM   17179 N  N     . LEU   B  1  1095 ? 1.897   42.771  87.081  1.00 14.19 ? 1093 LEU   B N     1 
ATOM   17180 C  CA    . LEU   B  1  1095 ? 1.649   44.156  86.735  1.00 15.12 ? 1093 LEU   B CA    1 
ATOM   17181 C  C     . LEU   B  1  1095 ? 2.669   44.602  85.705  1.00 13.25 ? 1093 LEU   B C     1 
ATOM   17182 O  O     . LEU   B  1  1095 ? 3.807   44.123  85.673  1.00 15.01 ? 1093 LEU   B O     1 
ATOM   17183 C  CB    . LEU   B  1  1095 ? 1.774   45.056  87.956  1.00 16.25 ? 1093 LEU   B CB    1 
ATOM   17184 C  CG    . LEU   B  1  1095 ? 0.939   44.559  89.135  1.00 18.15 ? 1093 LEU   B CG    1 
ATOM   17185 C  CD1   . LEU   B  1  1095 ? 1.227   45.429  90.355  1.00 23.59 ? 1093 LEU   B CD1   1 
ATOM   17186 C  CD2   . LEU   B  1  1095 ? -0.552  44.515  88.797  1.00 20.42 ? 1093 LEU   B CD2   1 
ATOM   17187 N  N     . TYR   B  1  1096 ? 2.238   45.526  84.857  1.00 13.96 ? 1094 TYR   B N     1 
ATOM   17188 C  CA    . TYR   B  1  1096 ? 3.079   46.002  83.778  1.00 13.43 ? 1094 TYR   B CA    1 
ATOM   17189 C  C     . TYR   B  1  1096 ? 2.853   47.494  83.701  1.00 13.12 ? 1094 TYR   B C     1 
ATOM   17190 O  O     . TYR   B  1  1096 ? 1.715   47.952  83.580  1.00 14.77 ? 1094 TYR   B O     1 
ATOM   17191 C  CB    . TYR   B  1  1096 ? 2.682   45.316  82.479  1.00 14.53 ? 1094 TYR   B CB    1 
ATOM   17192 C  CG    . TYR   B  1  1096 ? 3.339   45.844  81.228  1.00 13.83 ? 1094 TYR   B CG    1 
ATOM   17193 C  CD1   . TYR   B  1  1096 ? 4.569   45.371  80.798  1.00 14.39 ? 1094 TYR   B CD1   1 
ATOM   17194 C  CD2   . TYR   B  1  1096 ? 2.690   46.778  80.456  1.00 15.75 ? 1094 TYR   B CD2   1 
ATOM   17195 C  CE1   . TYR   B  1  1096 ? 5.142   45.841  79.620  1.00 14.46 ? 1094 TYR   B CE1   1 
ATOM   17196 C  CE2   . TYR   B  1  1096 ? 3.255   47.250  79.273  1.00 16.45 ? 1094 TYR   B CE2   1 
ATOM   17197 C  CZ    . TYR   B  1  1096 ? 4.470   46.780  78.877  1.00 15.52 ? 1094 TYR   B CZ    1 
ATOM   17198 O  OH    . TYR   B  1  1096 ? 5.022   47.265  77.717  1.00 16.44 ? 1094 TYR   B OH    1 
ATOM   17199 N  N     . THR   B  1  1097 ? 3.928   48.260  83.776  1.00 14.37 ? 1095 THR   B N     1 
ATOM   17200 C  CA    A THR   B  1  1097 ? 3.834   49.702  83.891  0.74 14.18 ? 1095 THR   B CA    1 
ATOM   17201 C  CA    B THR   B  1  1097 ? 3.810   49.700  83.864  0.26 14.25 ? 1095 THR   B CA    1 
ATOM   17202 C  C     . THR   B  1  1097 ? 4.876   50.355  83.003  1.00 14.14 ? 1095 THR   B C     1 
ATOM   17203 O  O     . THR   B  1  1097 ? 5.950   49.798  82.774  1.00 16.25 ? 1095 THR   B O     1 
ATOM   17204 C  CB    A THR   B  1  1097 ? 4.071   50.142  85.337  0.74 16.71 ? 1095 THR   B CB    1 
ATOM   17205 C  CB    B THR   B  1  1097 ? 3.960   50.135  85.317  0.26 16.80 ? 1095 THR   B CB    1 
ATOM   17206 O  OG1   A THR   B  1  1097 ? 5.386   49.767  85.755  0.74 20.56 ? 1095 THR   B OG1   1 
ATOM   17207 O  OG1   B THR   B  1  1097 ? 3.957   51.561  85.412  0.26 17.16 ? 1095 THR   B OG1   1 
ATOM   17208 C  CG2   A THR   B  1  1097 ? 3.093   49.472  86.264  0.74 16.29 ? 1095 THR   B CG2   1 
ATOM   17209 C  CG2   B THR   B  1  1097 ? 5.246   49.636  85.830  0.26 19.73 ? 1095 THR   B CG2   1 
ATOM   17210 N  N     . LEU   B  1  1098 ? 4.553   51.548  82.518  1.00 13.61 ? 1096 LEU   B N     1 
ATOM   17211 C  CA    . LEU   B  1  1098 ? 5.471   52.320  81.687  1.00 13.68 ? 1096 LEU   B CA    1 
ATOM   17212 C  C     . LEU   B  1  1098 ? 5.894   53.564  82.444  1.00 13.73 ? 1096 LEU   B C     1 
ATOM   17213 O  O     . LEU   B  1  1098 ? 5.064   54.388  82.837  1.00 15.09 ? 1096 LEU   B O     1 
ATOM   17214 C  CB    . LEU   B  1  1098 ? 4.835   52.699  80.354  1.00 13.77 ? 1096 LEU   B CB    1 
ATOM   17215 C  CG    . LEU   B  1  1098 ? 4.468   51.488  79.502  1.00 13.61 ? 1096 LEU   B CG    1 
ATOM   17216 C  CD1   . LEU   B  1  1098 ? 3.843   51.987  78.207  1.00 14.06 ? 1096 LEU   B CD1   1 
ATOM   17217 C  CD2   . LEU   B  1  1098 ? 5.668   50.607  79.198  1.00 15.16 ? 1096 LEU   B CD2   1 
ATOM   17218 N  N     . HIS   B  1  1099 ? 7.198   53.701  82.616  1.00 13.90 ? 1097 HIS   B N     1 
ATOM   17219 C  CA    . HIS   B  1  1099 ? 7.823   54.802  83.317  1.00 14.18 ? 1097 HIS   B CA    1 
ATOM   17220 C  C     . HIS   B  1  1099 ? 8.695   55.557  82.340  1.00 14.35 ? 1097 HIS   B C     1 
ATOM   17221 O  O     . HIS   B  1  1099 ? 8.932   55.106  81.214  1.00 14.52 ? 1097 HIS   B O     1 
ATOM   17222 C  CB    . HIS   B  1  1099 ? 8.742   54.251  84.398  1.00 16.09 ? 1097 HIS   B CB    1 
ATOM   17223 C  CG    . HIS   B  1  1099 ? 8.026   53.428  85.404  1.00 16.80 ? 1097 HIS   B CG    1 
ATOM   17224 N  ND1   . HIS   B  1  1099 ? 7.671   53.924  86.637  1.00 21.40 ? 1097 HIS   B ND1   1 
ATOM   17225 C  CD2   . HIS   B  1  1099 ? 7.564   52.159  85.355  1.00 21.43 ? 1097 HIS   B CD2   1 
ATOM   17226 C  CE1   . HIS   B  1  1099 ? 7.045   52.981  87.320  1.00 22.76 ? 1097 HIS   B CE1   1 
ATOM   17227 N  NE2   . HIS   B  1  1099 ? 6.968   51.902  86.566  1.00 21.51 ? 1097 HIS   B NE2   1 
ATOM   17228 N  N     . ALA   B  1  1100 ? 9.182   56.707  82.781  1.00 15.64 ? 1098 ALA   B N     1 
ATOM   17229 C  CA    . ALA   B  1  1100 ? 10.195  57.390  81.991  1.00 16.24 ? 1098 ALA   B CA    1 
ATOM   17230 C  C     . ALA   B  1  1100 ? 11.437  56.521  81.868  1.00 16.65 ? 1098 ALA   B C     1 
ATOM   17231 O  O     . ALA   B  1  1100 ? 11.757  55.727  82.759  1.00 18.09 ? 1098 ALA   B O     1 
ATOM   17232 C  CB    . ALA   B  1  1100 ? 10.571  58.705  82.659  1.00 17.33 ? 1098 ALA   B CB    1 
ATOM   17233 N  N     . ARG   B  1  1101 ? 12.129  56.660  80.732  1.00 16.29 ? 1099 ARG   B N     1 
ATOM   17234 C  CA    . ARG   B  1  1101 ? 13.434  56.015  80.580  1.00 17.82 ? 1099 ARG   B CA    1 
ATOM   17235 C  C     . ARG   B  1  1101 ? 14.476  56.611  81.515  1.00 15.68 ? 1099 ARG   B C     1 
ATOM   17236 O  O     . ARG   B  1  1101 ? 15.305  55.880  82.068  1.00 18.10 ? 1099 ARG   B O     1 
ATOM   17237 C  CB    . ARG   B  1  1101 ? 13.922  56.113  79.131  1.00 18.79 ? 1099 ARG   B CB    1 
ATOM   17238 C  CG    . ARG   B  1  1101 ? 13.318  55.094  78.181  1.00 20.70 ? 1099 ARG   B CG    1 
ATOM   17239 C  CD    . ARG   B  1  1101 ? 14.101  53.796  78.204  1.00 21.58 ? 1099 ARG   B CD    1 
ATOM   17240 N  NE    . ARG   B  1  1101 ? 13.547  52.820  77.275  1.00 21.06 ? 1099 ARG   B NE    1 
ATOM   17241 C  CZ    . ARG   B  1  1101 ? 14.272  51.940  76.605  1.00 18.77 ? 1099 ARG   B CZ    1 
ATOM   17242 N  NH1   . ARG   B  1  1101 ? 15.589  51.863  76.754  1.00 18.64 ? 1099 ARG   B NH1   1 
ATOM   17243 N  NH2   . ARG   B  1  1101 ? 13.666  51.115  75.762  1.00 22.42 ? 1099 ARG   B NH2   1 
ATOM   17244 N  N     . GLY   B  1  1102 ? 14.474  57.928  81.690  1.00 16.01 ? 1100 GLY   B N     1 
ATOM   17245 C  CA    . GLY   B  1  1102 ? 15.506  58.576  82.479  1.00 18.38 ? 1100 GLY   B CA    1 
ATOM   17246 C  C     . GLY   B  1  1102 ? 15.973  59.839  81.794  1.00 17.85 ? 1100 GLY   B C     1 
ATOM   17247 O  O     . GLY   B  1  1102 ? 15.164  60.715  81.478  1.00 18.88 ? 1100 GLY   B O     1 
ATOM   17248 N  N     . ARG   B  1  1103 ? 17.271  59.962  81.555  1.00 16.37 ? 1101 ARG   B N     1 
ATOM   17249 C  CA    . ARG   B  1  1103 ? 17.782  61.126  80.851  1.00 18.03 ? 1101 ARG   B CA    1 
ATOM   17250 C  C     . ARG   B  1  1103 ? 18.132  60.752  79.418  1.00 17.22 ? 1101 ARG   B C     1 
ATOM   17251 O  O     . ARG   B  1  1103 ? 18.886  59.806  79.180  1.00 18.43 ? 1101 ARG   B O     1 
ATOM   17252 C  CB    . ARG   B  1  1103 ? 19.011  61.717  81.541  1.00 18.07 ? 1101 ARG   B CB    1 
ATOM   17253 C  CG    . ARG   B  1  1103 ? 19.471  63.012  80.862  1.00 19.30 ? 1101 ARG   B CG    1 
ATOM   17254 C  CD    . ARG   B  1  1103 ? 20.479  63.793  81.704  1.00 23.67 ? 1101 ARG   B CD    1 
ATOM   17255 N  NE    . ARG   B  1  1103 ? 19.837  64.491  82.812  1.00 29.48 ? 1101 ARG   B NE    1 
ATOM   17256 C  CZ    . ARG   B  1  1103 ? 20.014  64.206  84.091  1.00 37.17 ? 1101 ARG   B CZ    1 
ATOM   17257 N  NH1   . ARG   B  1  1103 ? 20.829  63.234  84.478  1.00 43.28 ? 1101 ARG   B NH1   1 
ATOM   17258 N  NH2   . ARG   B  1  1103 ? 19.366  64.923  85.008  1.00 39.13 ? 1101 ARG   B NH2   1 
ATOM   17259 N  N     . ILE   B  1  1104 ? 17.577  61.487  78.477  1.00 15.61 ? 1102 ILE   B N     1 
ATOM   17260 C  CA    . ILE   B  1  1104 ? 17.745  61.188  77.063  1.00 15.48 ? 1102 ILE   B CA    1 
ATOM   17261 C  C     . ILE   B  1  1104 ? 18.763  62.162  76.503  1.00 16.48 ? 1102 ILE   B C     1 
ATOM   17262 O  O     . ILE   B  1  1104 ? 18.673  63.372  76.739  1.00 16.57 ? 1102 ILE   B O     1 
ATOM   17263 C  CB    . ILE   B  1  1104 ? 16.408  61.310  76.317  1.00 15.43 ? 1102 ILE   B CB    1 
ATOM   17264 C  CG1   . ILE   B  1  1104 ? 15.330  60.447  77.002  1.00 15.81 ? 1102 ILE   B CG1   1 
ATOM   17265 C  CG2   . ILE   B  1  1104 ? 16.575  60.957  74.832  1.00 16.37 ? 1102 ILE   B CG2   1 
ATOM   17266 C  CD1   . ILE   B  1  1104 ? 15.610  58.977  77.005  1.00 17.40 ? 1102 ILE   B CD1   1 
ATOM   17267 N  N     . LEU   B  1  1105 ? 19.725  61.638  75.764  1.00 15.78 ? 1103 LEU   B N     1 
ATOM   17268 C  CA    . LEU   B  1  1105 ? 20.673  62.480  75.052  1.00 16.51 ? 1103 LEU   B CA    1 
ATOM   17269 C  C     . LEU   B  1  1105 ? 20.006  63.014  73.790  1.00 16.20 ? 1103 LEU   B C     1 
ATOM   17270 O  O     . LEU   B  1  1105 ? 19.498  62.242  72.971  1.00 15.57 ? 1103 LEU   B O     1 
ATOM   17271 C  CB    . LEU   B  1  1105 ? 21.902  61.649  74.697  1.00 17.04 ? 1103 LEU   B CB    1 
ATOM   17272 C  CG    . LEU   B  1  1105 ? 22.954  62.360  73.842  1.00 16.99 ? 1103 LEU   B CG    1 
ATOM   17273 C  CD1   . LEU   B  1  1105 ? 23.577  63.536  74.587  1.00 16.89 ? 1103 LEU   B CD1   1 
ATOM   17274 C  CD2   . LEU   B  1  1105 ? 24.000  61.343  73.421  1.00 18.59 ? 1103 LEU   B CD2   1 
ATOM   17275 N  N     . LEU   B  1  1106 ? 19.968  64.328  73.657  1.00 15.74 ? 1104 LEU   B N     1 
ATOM   17276 C  CA    . LEU   B  1  1106 ? 19.390  64.978  72.495  1.00 16.41 ? 1104 LEU   B CA    1 
ATOM   17277 C  C     . LEU   B  1  1106 ? 20.522  65.529  71.648  1.00 16.19 ? 1104 LEU   B C     1 
ATOM   17278 O  O     . LEU   B  1  1106 ? 21.370  66.277  72.149  1.00 17.22 ? 1104 LEU   B O     1 
ATOM   17279 C  CB    . LEU   B  1  1106 ? 18.453  66.119  72.905  1.00 16.59 ? 1104 LEU   B CB    1 
ATOM   17280 C  CG    . LEU   B  1  1106 ? 16.976  65.778  73.058  1.00 22.02 ? 1104 LEU   B CG    1 
ATOM   17281 C  CD1   . LEU   B  1  1106 ? 16.744  64.464  73.766  1.00 23.00 ? 1104 LEU   B CD1   1 
ATOM   17282 C  CD2   . LEU   B  1  1106 ? 16.207  66.935  73.699  1.00 17.67 ? 1104 LEU   B CD2   1 
ATOM   17283 N  N     . VAL   B  1  1107 ? 20.527  65.152  70.378  1.00 16.71 ? 1105 VAL   B N     1 
ATOM   17284 C  CA    . VAL   B  1  1107 ? 21.540  65.640  69.450  1.00 16.69 ? 1105 VAL   B CA    1 
ATOM   17285 C  C     . VAL   B  1  1107 ? 20.786  66.328  68.322  1.00 16.71 ? 1105 VAL   B C     1 
ATOM   17286 O  O     . VAL   B  1  1107 ? 20.568  65.731  67.261  1.00 18.07 ? 1105 VAL   B O     1 
ATOM   17287 C  CB    . VAL   B  1  1107 ? 22.435  64.498  68.952  1.00 16.39 ? 1105 VAL   B CB    1 
ATOM   17288 C  CG1   . VAL   B  1  1107 ? 23.612  65.074  68.155  1.00 18.09 ? 1105 VAL   B CG1   1 
ATOM   17289 C  CG2   . VAL   B  1  1107 ? 22.956  63.683  70.121  1.00 17.14 ? 1105 VAL   B CG2   1 
ATOM   17290 N  N     . PRO   B  1  1108 ? 20.332  67.556  68.522  1.00 16.77 ? 1106 PRO   B N     1 
ATOM   17291 C  CA    . PRO   B  1  1108 ? 19.591  68.251  67.477  1.00 18.27 ? 1106 PRO   B CA    1 
ATOM   17292 C  C     . PRO   B  1  1108 ? 20.538  68.868  66.468  1.00 17.49 ? 1106 PRO   B C     1 
ATOM   17293 O  O     . PRO   B  1  1108 ? 21.738  69.033  66.710  1.00 21.71 ? 1106 PRO   B O     1 
ATOM   17294 C  CB    . PRO   B  1  1108 ? 18.884  69.361  68.257  1.00 17.97 ? 1106 PRO   B CB    1 
ATOM   17295 C  CG    . PRO   B  1  1108 ? 19.871  69.688  69.352  1.00 18.03 ? 1106 PRO   B CG    1 
ATOM   17296 C  CD    . PRO   B  1  1108 ? 20.416  68.353  69.763  1.00 18.30 ? 1106 PRO   B CD    1 
ATOM   17297 N  N     . ALA   B  1  1109 ? 19.961  69.231  65.334  1.00 18.71 ? 1107 ALA   B N     1 
ATOM   17298 C  CA    . ALA   B  1  1109 ? 20.628  70.050  64.335  1.00 20.83 ? 1107 ALA   B CA    1 
ATOM   17299 C  C     . ALA   B  1  1109 ? 19.986  71.417  64.193  1.00 23.64 ? 1107 ALA   B C     1 
ATOM   17300 O  O     . ALA   B  1  1109 ? 20.689  72.415  64.006  1.00 23.87 ? 1107 ALA   B O     1 
ATOM   17301 C  CB    . ALA   B  1  1109 ? 20.594  69.336  62.980  1.00 20.50 ? 1107 ALA   B CB    1 
ATOM   17302 N  N     . THR   B  1  1110 ? 18.662  71.487  64.295  1.00 20.09 ? 1108 THR   B N     1 
ATOM   17303 C  CA    . THR   B  1  1110 ? 17.928  72.724  64.098  1.00 19.83 ? 1108 THR   B CA    1 
ATOM   17304 C  C     . THR   B  1  1110 ? 17.067  73.024  65.314  1.00 20.78 ? 1108 THR   B C     1 
ATOM   17305 O  O     . THR   B  1  1110 ? 16.747  72.136  66.113  1.00 19.58 ? 1108 THR   B O     1 
ATOM   17306 C  CB    . THR   B  1  1110 ? 17.004  72.644  62.868  1.00 22.91 ? 1108 THR   B CB    1 
ATOM   17307 O  OG1   . THR   B  1  1110 ? 15.998  71.639  63.075  1.00 22.15 ? 1108 THR   B OG1   1 
ATOM   17308 C  CG2   . THR   B  1  1110 ? 17.796  72.303  61.603  1.00 25.51 ? 1108 THR   B CG2   1 
ATOM   17309 N  N     . GLU   B  1  1111 ? 16.675  74.291  65.427  1.00 22.25 ? 1109 GLU   B N     1 
ATOM   17310 C  CA    . GLU   B  1  1111 ? 15.803  74.693  66.523  1.00 21.98 ? 1109 GLU   B CA    1 
ATOM   17311 C  C     . GLU   B  1  1111 ? 14.510  73.887  66.520  1.00 23.36 ? 1109 GLU   B C     1 
ATOM   17312 O  O     . GLU   B  1  1111 ? 14.099  73.354  67.557  1.00 20.79 ? 1109 GLU   B O     1 
ATOM   17313 C  CB    . GLU   B  1  1111 ? 15.509  76.186  66.425  1.00 22.68 ? 1109 GLU   B CB    1 
ATOM   17314 C  CG    . GLU   B  1  1111 ? 14.437  76.640  67.382  1.00 24.67 ? 1109 GLU   B CG    1 
ATOM   17315 C  CD    . GLU   B  1  1111 ? 14.261  78.137  67.350  1.00 25.88 ? 1109 GLU   B CD    1 
ATOM   17316 O  OE1   . GLU   B  1  1111 ? 15.088  78.834  67.964  1.00 28.15 ? 1109 GLU   B OE1   1 
ATOM   17317 O  OE2   . GLU   B  1  1111 ? 13.303  78.609  66.703  1.00 29.85 ? 1109 GLU   B OE2   1 
ATOM   17318 N  N     . SER   B  1  1112 ? 13.852  73.786  65.363  1.00 22.84 ? 1110 SER   B N     1 
ATOM   17319 C  CA    . SER   B  1  1112 ? 12.616  73.012  65.301  1.00 20.97 ? 1110 SER   B CA    1 
ATOM   17320 C  C     . SER   B  1  1112 ? 12.863  71.558  65.669  1.00 21.55 ? 1110 SER   B C     1 
ATOM   17321 O  O     . SER   B  1  1112 ? 12.065  70.947  66.393  1.00 21.16 ? 1110 SER   B O     1 
ATOM   17322 C  CB    . SER   B  1  1112 ? 12.000  73.095  63.908  1.00 24.52 ? 1110 SER   B CB    1 
ATOM   17323 O  OG    . SER   B  1  1112 ? 10.795  72.341  63.860  1.00 24.25 ? 1110 SER   B OG    1 
ATOM   17324 N  N     . GLY   B  1  1113 ? 13.965  70.983  65.180  1.00 20.75 ? 1111 GLY   B N     1 
ATOM   17325 C  CA    . GLY   B  1  1113 ? 14.289  69.615  65.545  1.00 18.59 ? 1111 GLY   B CA    1 
ATOM   17326 C  C     . GLY   B  1  1113 ? 14.444  69.453  67.041  1.00 19.47 ? 1111 GLY   B C     1 
ATOM   17327 O  O     . GLY   B  1  1113 ? 13.932  68.497  67.630  1.00 18.62 ? 1111 GLY   B O     1 
ATOM   17328 N  N     . LEU   B  1  1114 ? 15.144  70.389  67.679  1.00 18.07 ? 1112 LEU   B N     1 
ATOM   17329 C  CA    . LEU   B  1  1114 ? 15.284  70.352  69.129  1.00 17.18 ? 1112 LEU   B CA    1 
ATOM   17330 C  C     . LEU   B  1  1114 ? 13.929  70.429  69.819  1.00 17.88 ? 1112 LEU   B C     1 
ATOM   17331 O  O     . LEU   B  1  1114 ? 13.680  69.693  70.777  1.00 16.99 ? 1112 LEU   B O     1 
ATOM   17332 C  CB    . LEU   B  1  1114 ? 16.187  71.490  69.600  1.00 19.81 ? 1112 LEU   B CB    1 
ATOM   17333 C  CG    . LEU   B  1  1114 ? 16.246  71.721  71.103  1.00 20.24 ? 1112 LEU   B CG    1 
ATOM   17334 C  CD1   . LEU   B  1  1114 ? 16.768  70.480  71.786  1.00 19.04 ? 1112 LEU   B CD1   1 
ATOM   17335 C  CD2   . LEU   B  1  1114 ? 17.118  72.928  71.444  1.00 22.50 ? 1112 LEU   B CD2   1 
ATOM   17336 N  N     . TYR   B  1  1115 ? 13.047  71.313  69.357  1.00 19.30 ? 1113 TYR   B N     1 
ATOM   17337 C  CA    . TYR   B  1  1115 ? 11.733  71.400  69.986  1.00 19.09 ? 1113 TYR   B CA    1 
ATOM   17338 C  C     . TYR   B  1  1115 ? 10.975  70.088  69.840  1.00 18.92 ? 1113 TYR   B C     1 
ATOM   17339 O  O     . TYR   B  1  1115 ? 10.304  69.648  70.778  1.00 18.99 ? 1113 TYR   B O     1 
ATOM   17340 C  CB    . TYR   B  1  1115 ? 10.927  72.540  69.377  1.00 19.16 ? 1113 TYR   B CB    1 
ATOM   17341 C  CG    . TYR   B  1  1115 ? 11.437  73.927  69.675  1.00 18.94 ? 1113 TYR   B CG    1 
ATOM   17342 C  CD1   . TYR   B  1  1115 ? 12.371  74.161  70.669  1.00 20.15 ? 1113 TYR   B CD1   1 
ATOM   17343 C  CD2   . TYR   B  1  1115 ? 10.964  75.008  68.950  1.00 24.31 ? 1113 TYR   B CD2   1 
ATOM   17344 C  CE1   . TYR   B  1  1115 ? 12.827  75.447  70.926  1.00 23.56 ? 1113 TYR   B CE1   1 
ATOM   17345 C  CE2   . TYR   B  1  1115 ? 11.409  76.289  69.206  1.00 24.38 ? 1113 TYR   B CE2   1 
ATOM   17346 C  CZ    . TYR   B  1  1115 ? 12.343  76.501  70.191  1.00 26.79 ? 1113 TYR   B CZ    1 
ATOM   17347 O  OH    . TYR   B  1  1115 ? 12.795  77.779  70.435  1.00 30.76 ? 1113 TYR   B OH    1 
ATOM   17348 N  N     . HIS   B  1  1116 ? 11.077  69.442  68.679  1.00 17.29 ? 1114 HIS   B N     1 
ATOM   17349 C  CA    . HIS   B  1  1116 ? 10.420  68.154  68.501  1.00 17.96 ? 1114 HIS   B CA    1 
ATOM   17350 C  C     . HIS   B  1  1116 ? 11.045  67.083  69.381  1.00 18.57 ? 1114 HIS   B C     1 
ATOM   17351 O  O     . HIS   B  1  1116 ? 10.330  66.257  69.962  1.00 18.34 ? 1114 HIS   B O     1 
ATOM   17352 C  CB    . HIS   B  1  1116 ? 10.459  67.725  67.037  1.00 16.88 ? 1114 HIS   B CB    1 
ATOM   17353 C  CG    . HIS   B  1  1116 ? 9.416   68.379  66.184  1.00 21.40 ? 1114 HIS   B CG    1 
ATOM   17354 N  ND1   . HIS   B  1  1116 ? 9.603   69.609  65.589  1.00 23.67 ? 1114 HIS   B ND1   1 
ATOM   17355 C  CD2   . HIS   B  1  1116 ? 8.183   67.962  65.804  1.00 21.38 ? 1114 HIS   B CD2   1 
ATOM   17356 C  CE1   . HIS   B  1  1116 ? 8.528   69.925  64.887  1.00 24.94 ? 1114 HIS   B CE1   1 
ATOM   17357 N  NE2   . HIS   B  1  1116 ? 7.653   68.944  65.002  1.00 24.95 ? 1114 HIS   B NE2   1 
ATOM   17358 N  N     . GLN   B  1  1117 ? 12.379  67.070  69.493  1.00 16.48 ? 1115 GLN   B N     1 
ATOM   17359 C  CA    . GLN   B  1  1117 ? 13.019  66.098  70.368  1.00 16.36 ? 1115 GLN   B CA    1 
ATOM   17360 C  C     . GLN   B  1  1117 ? 12.612  66.333  71.806  1.00 16.45 ? 1115 GLN   B C     1 
ATOM   17361 O  O     . GLN   B  1  1117 ? 12.362  65.379  72.548  1.00 16.21 ? 1115 GLN   B O     1 
ATOM   17362 C  CB    . GLN   B  1  1117 ? 14.541  66.196  70.242  1.00 16.68 ? 1115 GLN   B CB    1 
ATOM   17363 C  CG    . GLN   B  1  1117 ? 15.075  65.762  68.890  1.00 16.01 ? 1115 GLN   B CG    1 
ATOM   17364 C  CD    . GLN   B  1  1117 ? 16.584  65.947  68.793  1.00 16.52 ? 1115 GLN   B CD    1 
ATOM   17365 O  OE1   . GLN   B  1  1117 ? 17.197  66.610  69.625  1.00 18.70 ? 1115 GLN   B OE1   1 
ATOM   17366 N  NE2   . GLN   B  1  1117 ? 17.183  65.333  67.792  1.00 18.46 ? 1115 GLN   B NE2   1 
ATOM   17367 N  N     . LEU   B  1  1118 ? 12.596  67.595  72.232  1.00 16.68 ? 1116 LEU   B N     1 
ATOM   17368 C  CA    . LEU   B  1  1118 ? 12.177  67.894  73.591  1.00 17.75 ? 1116 LEU   B CA    1 
ATOM   17369 C  C     . LEU   B  1  1118 ? 10.752  67.444  73.825  1.00 17.20 ? 1116 LEU   B C     1 
ATOM   17370 O  O     . LEU   B  1  1118 ? 10.447  66.858  74.867  1.00 18.00 ? 1116 LEU   B O     1 
ATOM   17371 C  CB    . LEU   B  1  1118 ? 12.266  69.388  73.857  1.00 19.49 ? 1116 LEU   B CB    1 
ATOM   17372 C  CG    . LEU   B  1  1118 ? 13.671  69.882  74.103  1.00 23.78 ? 1116 LEU   B CG    1 
ATOM   17373 C  CD1   . LEU   B  1  1118 ? 13.663  71.386  74.027  1.00 22.83 ? 1116 LEU   B CD1   1 
ATOM   17374 C  CD2   . LEU   B  1  1118 ? 14.146  69.411  75.465  1.00 22.10 ? 1116 LEU   B CD2   1 
ATOM   17375 N  N     . ALA   B  1  1119 ? 9.865   67.706  72.869  1.00 18.41 ? 1117 ALA   B N     1 
ATOM   17376 C  CA    . ALA   B  1  1119 ? 8.479   67.288  73.036  1.00 18.37 ? 1117 ALA   B CA    1 
ATOM   17377 C  C     . ALA   B  1  1119 ? 8.399   65.788  73.267  1.00 17.73 ? 1117 ALA   B C     1 
ATOM   17378 O  O     . ALA   B  1  1119 ? 7.730   65.330  74.202  1.00 17.76 ? 1117 ALA   B O     1 
ATOM   17379 C  CB    . ALA   B  1  1119 ? 7.655   67.691  71.815  1.00 19.15 ? 1117 ALA   B CB    1 
ATOM   17380 N  N     . ALA   B  1  1120 ? 9.092   65.011  72.438  1.00 15.30 ? 1118 ALA   B N     1 
ATOM   17381 C  CA    . ALA   B  1  1120 ? 9.035   63.558  72.562  1.00 14.64 ? 1118 ALA   B CA    1 
ATOM   17382 C  C     . ALA   B  1  1120 ? 9.578   63.110  73.908  1.00 17.01 ? 1118 ALA   B C     1 
ATOM   17383 O  O     . ALA   B  1  1120 ? 8.980   62.265  74.587  1.00 16.71 ? 1118 ALA   B O     1 
ATOM   17384 C  CB    . ALA   B  1  1120 ? 9.819   62.902  71.428  1.00 16.67 ? 1118 ALA   B CB    1 
ATOM   17385 N  N     . ALA   B  1  1121 ? 10.727  63.658  74.309  1.00 14.45 ? 1119 ALA   B N     1 
ATOM   17386 C  CA    . ALA   B  1  1121 ? 11.337  63.244  75.569  1.00 15.52 ? 1119 ALA   B CA    1 
ATOM   17387 C  C     . ALA   B  1  1121 ? 10.523  63.687  76.780  1.00 14.26 ? 1119 ALA   B C     1 
ATOM   17388 O  O     . ALA   B  1  1121 ? 10.354  62.908  77.726  1.00 15.18 ? 1119 ALA   B O     1 
ATOM   17389 C  CB    . ALA   B  1  1121 ? 12.767  63.783  75.655  1.00 16.80 ? 1119 ALA   B CB    1 
ATOM   17390 N  N     . LEU   B  1  1122 ? 10.046  64.934  76.792  1.00 15.73 ? 1120 LEU   B N     1 
ATOM   17391 C  CA    . LEU   B  1  1122 ? 9.259   65.410  77.930  1.00 15.56 ? 1120 LEU   B CA    1 
ATOM   17392 C  C     . LEU   B  1  1122 ? 7.937   64.666  78.038  1.00 15.84 ? 1120 LEU   B C     1 
ATOM   17393 O  O     . LEU   B  1  1122 ? 7.488   64.356  79.149  1.00 15.90 ? 1120 LEU   B O     1 
ATOM   17394 C  CB    . LEU   B  1  1122 ? 9.002   66.906  77.831  1.00 15.73 ? 1120 LEU   B CB    1 
ATOM   17395 C  CG    . LEU   B  1  1122 ? 10.267  67.757  77.877  1.00 19.14 ? 1120 LEU   B CG    1 
ATOM   17396 C  CD1   . LEU   B  1  1122 ? 9.932   69.195  77.564  1.00 19.73 ? 1120 LEU   B CD1   1 
ATOM   17397 C  CD2   . LEU   B  1  1122 ? 10.977  67.645  79.231  1.00 20.08 ? 1120 LEU   B CD2   1 
ATOM   17398 N  N     . ALA   B  1  1123 ? 7.311   64.366  76.904  1.00 14.76 ? 1121 ALA   B N     1 
ATOM   17399 C  CA    . ALA   B  1  1123 ? 6.005   63.717  76.927  1.00 16.66 ? 1121 ALA   B CA    1 
ATOM   17400 C  C     . ALA   B  1  1123 ? 6.092   62.340  77.542  1.00 16.65 ? 1121 ALA   B C     1 
ATOM   17401 O  O     . ALA   B  1  1123 ? 5.088   61.823  78.051  1.00 15.72 ? 1121 ALA   B O     1 
ATOM   17402 C  CB    . ALA   B  1  1123 ? 5.456   63.587  75.515  1.00 16.26 ? 1121 ALA   B CB    1 
ATOM   17403 N  N     . THR   B  1  1124 ? 7.265   61.719  77.479  1.00 15.01 ? 1122 THR   B N     1 
ATOM   17404 C  CA    . THR   B  1  1124 ? 7.496   60.409  78.048  1.00 13.06 ? 1122 THR   B CA    1 
ATOM   17405 C  C     . THR   B  1  1124 ? 8.183   60.492  79.407  1.00 13.56 ? 1122 THR   B C     1 
ATOM   17406 O  O     . THR   B  1  1124 ? 8.697   59.482  79.900  1.00 15.32 ? 1122 THR   B O     1 
ATOM   17407 C  CB    . THR   B  1  1124 ? 8.273   59.542  77.057  1.00 14.35 ? 1122 THR   B CB    1 
ATOM   17408 O  OG1   . THR   B  1  1124 ? 9.375   60.293  76.516  1.00 15.46 ? 1122 THR   B OG1   1 
ATOM   17409 C  CG2   . THR   B  1  1124 ? 7.345   59.107  75.906  1.00 14.23 ? 1122 THR   B CG2   1 
ATOM   17410 N  N     . GLY   B  1  1125 ? 8.181   61.675  80.019  1.00 14.56 ? 1123 GLY   B N     1 
ATOM   17411 C  CA    . GLY   B  1  1125 ? 8.591   61.850  81.401  1.00 14.26 ? 1123 GLY   B CA    1 
ATOM   17412 C  C     . GLY   B  1  1125 ? 10.078  61.983  81.616  1.00 14.85 ? 1123 GLY   B C     1 
ATOM   17413 O  O     . GLY   B  1  1125 ? 10.531  61.982  82.765  1.00 15.27 ? 1123 GLY   B O     1 
ATOM   17414 N  N     . ASN   B  1  1126 ? 10.843  62.122  80.555  1.00 15.27 ? 1124 ASN   B N     1 
ATOM   17415 C  CA    . ASN   B  1  1126 ? 12.288  62.091  80.662  1.00 14.43 ? 1124 ASN   B CA    1 
ATOM   17416 C  C     . ASN   B  1  1126 ? 12.847  63.475  80.912  1.00 15.53 ? 1124 ASN   B C     1 
ATOM   17417 O  O     . ASN   B  1  1126 ? 12.229  64.498  80.619  1.00 17.01 ? 1124 ASN   B O     1 
ATOM   17418 C  CB    . ASN   B  1  1126 ? 12.887  61.538  79.379  1.00 14.48 ? 1124 ASN   B CB    1 
ATOM   17419 C  CG    . ASN   B  1  1126 ? 12.419  60.152  79.100  1.00 14.60 ? 1124 ASN   B CG    1 
ATOM   17420 O  OD1   . ASN   B  1  1126 ? 12.771  59.217  79.811  1.00 15.58 ? 1124 ASN   B OD1   1 
ATOM   17421 N  ND2   . ASN   B  1  1126 ? 11.609  59.998  78.067  1.00 15.33 ? 1124 ASN   B ND2   1 
ATOM   17422 N  N     . SER   B  1  1127 ? 14.056  63.479  81.465  1.00 15.32 ? 1125 SER   B N     1 
ATOM   17423 C  CA    . SER   B  1  1127 ? 14.905  64.654  81.399  1.00 16.39 ? 1125 SER   B CA    1 
ATOM   17424 C  C     . SER   B  1  1127 ? 15.804  64.505  80.177  1.00 16.02 ? 1125 SER   B C     1 
ATOM   17425 O  O     . SER   B  1  1127 ? 15.821  63.460  79.521  1.00 16.24 ? 1125 SER   B O     1 
ATOM   17426 C  CB    . SER   B  1  1127 ? 15.757  64.774  82.657  1.00 17.80 ? 1125 SER   B CB    1 
ATOM   17427 O  OG    . SER   B  1  1127 ? 16.557  63.617  82.837  1.00 21.66 ? 1125 SER   B OG    1 
ATOM   17428 N  N     . VAL   B  1  1128 ? 16.529  65.567  79.847  1.00 17.16 ? 1126 VAL   B N     1 
ATOM   17429 C  CA    . VAL   B  1  1128 ? 17.340  65.552  78.636  1.00 17.08 ? 1126 VAL   B CA    1 
ATOM   17430 C  C     . VAL   B  1  1128 ? 18.696  66.169  78.906  1.00 17.62 ? 1126 VAL   B C     1 
ATOM   17431 O  O     . VAL   B  1  1128 ? 18.847  67.048  79.761  1.00 19.49 ? 1126 VAL   B O     1 
ATOM   17432 C  CB    . VAL   B  1  1128 ? 16.678  66.269  77.438  1.00 17.29 ? 1126 VAL   B CB    1 
ATOM   17433 C  CG1   . VAL   B  1  1128 ? 15.346  65.604  77.084  1.00 16.89 ? 1126 VAL   B CG1   1 
ATOM   17434 C  CG2   . VAL   B  1  1128 ? 16.476  67.747  77.729  1.00 18.66 ? 1126 VAL   B CG2   1 
ATOM   17435 N  N     . ALA   B  1  1129 ? 19.681  65.712  78.148  1.00 16.67 ? 1127 ALA   B N     1 
ATOM   17436 C  CA    . ALA   B  1  1129 ? 20.946  66.417  78.008  1.00 17.80 ? 1127 ALA   B CA    1 
ATOM   17437 C  C     . ALA   B  1  1129 ? 21.075  66.761  76.538  1.00 16.15 ? 1127 ALA   B C     1 
ATOM   17438 O  O     . ALA   B  1  1129 ? 21.073  65.863  75.690  1.00 17.27 ? 1127 ALA   B O     1 
ATOM   17439 C  CB    . ALA   B  1  1129 ? 22.105  65.533  78.450  1.00 18.99 ? 1127 ALA   B CB    1 
ATOM   17440 N  N     . ILE   B  1  1130 ? 21.159  68.046  76.233  1.00 16.12 ? 1128 ILE   B N     1 
ATOM   17441 C  CA    . ILE   B  1  1130 ? 21.213  68.508  74.856  1.00 16.83 ? 1128 ILE   B CA    1 
ATOM   17442 C  C     . ILE   B  1  1130 ? 22.660  68.743  74.471  1.00 17.55 ? 1128 ILE   B C     1 
ATOM   17443 O  O     . ILE   B  1  1130 ? 23.413  69.400  75.203  1.00 17.68 ? 1128 ILE   B O     1 
ATOM   17444 C  CB    . ILE   B  1  1130 ? 20.402  69.792  74.646  1.00 17.10 ? 1128 ILE   B CB    1 
ATOM   17445 C  CG1   . ILE   B  1  1130 ? 18.999  69.649  75.249  1.00 19.17 ? 1128 ILE   B CG1   1 
ATOM   17446 C  CG2   . ILE   B  1  1130 ? 20.320  70.099  73.154  1.00 17.67 ? 1128 ILE   B CG2   1 
ATOM   17447 C  CD1   . ILE   B  1  1130 ? 18.276  70.967  75.351  1.00 18.19 ? 1128 ILE   B CD1   1 
ATOM   17448 N  N     . ASP   B  1  1131 ? 23.031  68.231  73.308  1.00 17.09 ? 1129 ASP   B N     1 
ATOM   17449 C  CA    . ASP   B  1  1131 ? 24.379  68.419  72.795  1.00 17.88 ? 1129 ASP   B CA    1 
ATOM   17450 C  C     . ASP   B  1  1131 ? 24.704  69.900  72.659  1.00 18.37 ? 1129 ASP   B C     1 
ATOM   17451 O  O     . ASP   B  1  1131 ? 24.098  70.608  71.849  1.00 18.79 ? 1129 ASP   B O     1 
ATOM   17452 C  CB    . ASP   B  1  1131 ? 24.492  67.721  71.451  1.00 17.60 ? 1129 ASP   B CB    1 
ATOM   17453 C  CG    . ASP   B  1  1131 ? 25.832  67.917  70.820  1.00 19.54 ? 1129 ASP   B CG    1 
ATOM   17454 O  OD1   . ASP   B  1  1131 ? 26.813  68.043  71.575  1.00 20.20 ? 1129 ASP   B OD1   1 
ATOM   17455 O  OD2   . ASP   B  1  1131 ? 25.876  67.965  69.586  1.00 20.53 ? 1129 ASP   B OD2   1 
ATOM   17456 N  N     . ALA   B  1  1132 ? 25.675  70.373  73.448  1.00 19.14 ? 1130 ALA   B N     1 
ATOM   17457 C  CA    . ALA   B  1  1132 ? 26.047  71.782  73.393  1.00 19.06 ? 1130 ALA   B CA    1 
ATOM   17458 C  C     . ALA   B  1  1132 ? 26.645  72.150  72.047  1.00 21.25 ? 1130 ALA   B C     1 
ATOM   17459 O  O     . ALA   B  1  1132 ? 26.524  73.301  71.612  1.00 21.69 ? 1130 ALA   B O     1 
ATOM   17460 C  CB    . ALA   B  1  1132 ? 27.022  72.108  74.525  1.00 19.87 ? 1130 ALA   B CB    1 
ATOM   17461 N  N     . ALA   B  1  1133 ? 27.266  71.189  71.360  1.00 19.52 ? 1131 ALA   B N     1 
ATOM   17462 C  CA    . ALA   B  1  1133 ? 27.866  71.502  70.070  1.00 23.83 ? 1131 ALA   B CA    1 
ATOM   17463 C  C     . ALA   B  1  1133 ? 26.828  71.839  69.017  1.00 23.70 ? 1131 ALA   B C     1 
ATOM   17464 O  O     . ALA   B  1  1133 ? 27.193  72.298  67.930  1.00 23.85 ? 1131 ALA   B O     1 
ATOM   17465 C  CB    . ALA   B  1  1133 ? 28.756  70.350  69.590  1.00 22.84 ? 1131 ALA   B CB    1 
ATOM   17466 N  N     . SER   B  1  1134 ? 25.543  71.618  69.307  1.00 20.57 ? 1132 SER   B N     1 
ATOM   17467 C  CA    . SER   B  1  1134 ? 24.497  72.034  68.384  1.00 20.72 ? 1132 SER   B CA    1 
ATOM   17468 C  C     . SER   B  1  1134 ? 24.430  73.551  68.249  1.00 20.72 ? 1132 SER   B C     1 
ATOM   17469 O  O     . SER   B  1  1134 ? 23.930  74.042  67.239  1.00 22.33 ? 1132 SER   B O     1 
ATOM   17470 C  CB    . SER   B  1  1134 ? 23.137  71.509  68.860  1.00 19.84 ? 1132 SER   B CB    1 
ATOM   17471 O  OG    . SER   B  1  1134 ? 22.744  72.157  70.057  1.00 20.98 ? 1132 SER   B OG    1 
ATOM   17472 N  N     . GLY   B  1  1135 ? 24.899  74.295  69.245  1.00 20.53 ? 1133 GLY   B N     1 
ATOM   17473 C  CA    . GLY   B  1  1135 ? 24.843  75.743  69.184  1.00 21.78 ? 1133 GLY   B CA    1 
ATOM   17474 C  C     . GLY   B  1  1135 ? 23.455  76.323  69.342  1.00 24.06 ? 1133 GLY   B C     1 
ATOM   17475 O  O     . GLY   B  1  1135 ? 23.242  77.494  69.025  1.00 26.13 ? 1133 GLY   B O     1 
ATOM   17476 N  N     . LEU   B  1  1136 ? 22.502  75.541  69.850  1.00 22.43 ? 1134 LEU   B N     1 
ATOM   17477 C  CA    . LEU   B  1  1136 ? 21.103  75.941  69.876  1.00 22.66 ? 1134 LEU   B CA    1 
ATOM   17478 C  C     . LEU   B  1  1136 ? 20.672  76.507  71.223  1.00 25.55 ? 1134 LEU   B C     1 
ATOM   17479 O  O     . LEU   B  1  1136 ? 19.468  76.586  71.492  1.00 23.86 ? 1134 LEU   B O     1 
ATOM   17480 C  CB    . LEU   B  1  1136 ? 20.223  74.755  69.484  1.00 20.45 ? 1134 LEU   B CB    1 
ATOM   17481 C  CG    . LEU   B  1  1136 ? 20.407  74.248  68.056  1.00 21.93 ? 1134 LEU   B CG    1 
ATOM   17482 C  CD1   . LEU   B  1  1136 ? 19.611  72.980  67.835  1.00 23.85 ? 1134 LEU   B CD1   1 
ATOM   17483 C  CD2   . LEU   B  1  1136 ? 19.989  75.321  67.065  1.00 23.99 ? 1134 LEU   B CD2   1 
ATOM   17484 N  N     . GLN   B  1  1137 ? 21.625  76.908  72.065  1.00 22.73 ? 1135 GLN   B N     1 
ATOM   17485 C  CA    . GLN   B  1  1137 ? 21.303  77.353  73.417  1.00 23.56 ? 1135 GLN   B CA    1 
ATOM   17486 C  C     . GLN   B  1  1137 ? 20.312  78.512  73.419  1.00 27.92 ? 1135 GLN   B C     1 
ATOM   17487 O  O     . GLN   B  1  1137 ? 19.427  78.574  74.282  1.00 27.67 ? 1135 GLN   B O     1 
ATOM   17488 C  CB    . GLN   B  1  1137 ? 22.582  77.744  74.159  1.00 25.72 ? 1135 GLN   B CB    1 
ATOM   17489 C  CG    . GLN   B  1  1137 ? 23.465  76.571  74.559  1.00 25.55 ? 1135 GLN   B CG    1 
ATOM   17490 C  CD    . GLN   B  1  1137 ? 24.423  76.126  73.460  1.00 23.87 ? 1135 GLN   B CD    1 
ATOM   17491 O  OE1   . GLN   B  1  1137 ? 24.289  76.509  72.300  1.00 25.50 ? 1135 GLN   B OE1   1 
ATOM   17492 N  NE2   . GLN   B  1  1137 ? 25.395  75.299  73.834  1.00 26.45 ? 1135 GLN   B NE2   1 
ATOM   17493 N  N     . ALA   B  1  1138 ? 20.436  79.437  72.465  1.00 24.14 ? 1136 ALA   B N     1 
ATOM   17494 C  CA    . ALA   B  1  1138 ? 19.540  80.589  72.432  1.00 28.33 ? 1136 ALA   B CA    1 
ATOM   17495 C  C     . ALA   B  1  1138 ? 18.099  80.187  72.157  1.00 29.62 ? 1136 ALA   B C     1 
ATOM   17496 O  O     . ALA   B  1  1138 ? 17.183  80.965  72.445  1.00 31.24 ? 1136 ALA   B O     1 
ATOM   17497 C  CB    . ALA   B  1  1138 ? 20.000  81.597  71.380  1.00 27.51 ? 1136 ALA   B CB    1 
ATOM   17498 N  N     . SER   B  1  1139 ? 17.882  78.993  71.608  1.00 26.74 ? 1137 SER   B N     1 
ATOM   17499 C  CA    . SER   B  1  1139 ? 16.538  78.529  71.298  1.00 26.75 ? 1137 SER   B CA    1 
ATOM   17500 C  C     . SER   B  1  1139 ? 15.719  78.232  72.547  1.00 28.56 ? 1137 SER   B C     1 
ATOM   17501 O  O     . SER   B  1  1139 ? 14.488  78.173  72.462  1.00 26.44 ? 1137 SER   B O     1 
ATOM   17502 C  CB    . SER   B  1  1139 ? 16.629  77.278  70.426  1.00 25.26 ? 1137 SER   B CB    1 
ATOM   17503 O  OG    . SER   B  1  1139 ? 17.136  77.597  69.144  1.00 28.70 ? 1137 SER   B OG    1 
ATOM   17504 N  N     . LEU   B  1  1140 ? 16.368  78.038  73.692  1.00 26.47 ? 1138 LEU   B N     1 
ATOM   17505 C  CA    . LEU   B  1  1140 ? 15.674  77.799  74.950  1.00 28.17 ? 1138 LEU   B CA    1 
ATOM   17506 C  C     . LEU   B  1  1140 ? 15.698  79.009  75.876  1.00 32.64 ? 1138 LEU   B C     1 
ATOM   17507 O  O     . LEU   B  1  1140 ? 15.560  78.852  77.092  1.00 33.06 ? 1138 LEU   B O     1 
ATOM   17508 C  CB    . LEU   B  1  1140 ? 16.226  76.561  75.658  1.00 27.50 ? 1138 LEU   B CB    1 
ATOM   17509 C  CG    . LEU   B  1  1140 ? 16.045  75.260  74.877  1.00 26.84 ? 1138 LEU   B CG    1 
ATOM   17510 C  CD1   . LEU   B  1  1140 ? 16.402  74.042  75.721  1.00 25.95 ? 1138 LEU   B CD1   1 
ATOM   17511 C  CD2   . LEU   B  1  1140 ? 14.623  75.149  74.330  1.00 31.09 ? 1138 LEU   B CD2   1 
ATOM   17512 N  N     . LYS   B  1  1141 ? 15.864  80.212  75.334  1.00 34.65 ? 1139 LYS   B N     1 
ATOM   17513 C  CA    . LYS   B  1  1141 ? 15.796  81.404  76.170  1.00 36.20 ? 1139 LYS   B CA    1 
ATOM   17514 C  C     . LYS   B  1  1141 ? 14.398  81.543  76.764  1.00 39.13 ? 1139 LYS   B C     1 
ATOM   17515 O  O     . LYS   B  1  1141 ? 13.393  81.289  76.094  1.00 35.35 ? 1139 LYS   B O     1 
ATOM   17516 C  CB    . LYS   B  1  1141 ? 16.135  82.646  75.344  1.00 35.73 ? 1139 LYS   B CB    1 
ATOM   17517 N  N     . ASN   B  1  1142 ? 14.340  81.930  78.039  1.00 37.20 ? 1140 ASN   B N     1 
ATOM   17518 C  CA    . ASN   B  1  1142 ? 13.089  82.173  78.757  1.00 35.64 ? 1140 ASN   B CA    1 
ATOM   17519 C  C     . ASN   B  1  1142 ? 12.260  80.908  78.967  1.00 36.85 ? 1140 ASN   B C     1 
ATOM   17520 O  O     . ASN   B  1  1142 ? 11.042  80.985  79.150  1.00 34.63 ? 1140 ASN   B O     1 
ATOM   17521 C  CB    . ASN   B  1  1142 ? 12.243  83.276  78.105  1.00 40.41 ? 1140 ASN   B CB    1 
ATOM   17522 C  CG    . ASN   B  1  1142 ? 13.030  84.556  77.869  1.00 49.77 ? 1140 ASN   B CG    1 
ATOM   17523 O  OD1   . ASN   B  1  1142 ? 13.795  84.997  78.727  1.00 47.46 ? 1140 ASN   B OD1   1 
ATOM   17524 N  ND2   . ASN   B  1  1142 ? 12.849  85.154  76.695  1.00 52.45 ? 1140 ASN   B ND2   1 
ATOM   17525 N  N     . LEU   B  1  1143 ? 12.891  79.742  78.937  1.00 33.98 ? 1141 LEU   B N     1 
ATOM   17526 C  CA    . LEU   B  1  1143 ? 12.169  78.508  79.193  1.00 29.98 ? 1141 LEU   B CA    1 
ATOM   17527 C  C     . LEU   B  1  1143 ? 11.604  78.536  80.613  1.00 31.32 ? 1141 LEU   B C     1 
ATOM   17528 O  O     . LEU   B  1  1143 ? 12.289  78.978  81.540  1.00 39.46 ? 1141 LEU   B O     1 
ATOM   17529 C  CB    . LEU   B  1  1143 ? 13.139  77.336  79.051  1.00 28.72 ? 1141 LEU   B CB    1 
ATOM   17530 C  CG    . LEU   B  1  1143 ? 12.618  75.923  78.858  1.00 29.60 ? 1141 LEU   B CG    1 
ATOM   17531 C  CD1   . LEU   B  1  1143 ? 11.866  75.809  77.550  1.00 29.21 ? 1141 LEU   B CD1   1 
ATOM   17532 C  CD2   . LEU   B  1  1143 ? 13.792  74.967  78.888  1.00 27.05 ? 1141 LEU   B CD2   1 
ATOM   17533 N  N     . PRO   B  1  1144 ? 10.365  78.085  80.816  1.00 31.58 ? 1142 PRO   B N     1 
ATOM   17534 C  CA    . PRO   B  1  1144 ? 9.843   77.945  82.183  1.00 35.14 ? 1142 PRO   B CA    1 
ATOM   17535 C  C     . PRO   B  1  1144 ? 10.757  77.069  83.029  1.00 31.83 ? 1142 PRO   B C     1 
ATOM   17536 O  O     . PRO   B  1  1144 ? 11.311  76.079  82.546  1.00 26.50 ? 1142 PRO   B O     1 
ATOM   17537 C  CB    . PRO   B  1  1144 ? 8.482   77.262  81.975  1.00 34.70 ? 1142 PRO   B CB    1 
ATOM   17538 C  CG    . PRO   B  1  1144 ? 8.133   77.488  80.545  1.00 35.61 ? 1142 PRO   B CG    1 
ATOM   17539 C  CD    . PRO   B  1  1144 ? 9.434   77.565  79.803  1.00 30.77 ? 1142 PRO   B CD    1 
ATOM   17540 N  N     . GLN   B  1  1145 ? 10.892  77.433  84.311  1.00 32.56 ? 1143 GLN   B N     1 
ATOM   17541 C  CA    . GLN   B  1  1145 ? 11.728  76.666  85.232  1.00 30.20 ? 1143 GLN   B CA    1 
ATOM   17542 C  C     . GLN   B  1  1145 ? 11.272  75.218  85.348  1.00 27.80 ? 1143 GLN   B C     1 
ATOM   17543 O  O     . GLN   B  1  1145 ? 12.102  74.326  85.541  1.00 27.41 ? 1143 GLN   B O     1 
ATOM   17544 C  CB    . GLN   B  1  1145 ? 11.748  77.318  86.617  1.00 32.96 ? 1143 GLN   B CB    1 
ATOM   17545 N  N     . THR   B  1  1146 ? 9.964   74.961  85.239  1.00 28.45 ? 1144 THR   B N     1 
ATOM   17546 C  CA    . THR   B  1  1146 ? 9.496   73.579  85.256  1.00 33.76 ? 1144 THR   B CA    1 
ATOM   17547 C  C     . THR   B  1  1146 ? 10.146  72.778  84.142  1.00 29.99 ? 1144 THR   B C     1 
ATOM   17548 O  O     . THR   B  1  1146 ? 10.558  71.627  84.343  1.00 31.66 ? 1144 THR   B O     1 
ATOM   17549 C  CB    . THR   B  1  1146 ? 7.982   73.541  85.088  1.00 33.18 ? 1144 THR   B CB    1 
ATOM   17550 O  OG1   . THR   B  1  1146 ? 7.604   74.431  84.031  1.00 35.57 ? 1144 THR   B OG1   1 
ATOM   17551 C  CG2   . THR   B  1  1146 ? 7.292   73.957  86.382  1.00 38.80 ? 1144 THR   B CG2   1 
ATOM   17552 N  N     . VAL   B  1  1147 ? 10.263  73.376  82.962  1.00 25.45 ? 1145 VAL   B N     1 
ATOM   17553 C  CA    . VAL   B  1  1147 ? 10.930  72.681  81.873  1.00 22.27 ? 1145 VAL   B CA    1 
ATOM   17554 C  C     . VAL   B  1  1147 ? 12.439  72.716  82.060  1.00 25.72 ? 1145 VAL   B C     1 
ATOM   17555 O  O     . VAL   B  1  1147 ? 13.129  71.718  81.832  1.00 25.13 ? 1145 VAL   B O     1 
ATOM   17556 C  CB    . VAL   B  1  1147 ? 10.505  73.260  80.517  1.00 21.84 ? 1145 VAL   B CB    1 
ATOM   17557 C  CG1   . VAL   B  1  1147 ? 11.059  72.389  79.392  1.00 24.95 ? 1145 VAL   B CG1   1 
ATOM   17558 C  CG2   . VAL   B  1  1147 ? 8.991   73.379  80.433  1.00 22.49 ? 1145 VAL   B CG2   1 
ATOM   17559 N  N     . GLY   B  1  1148 ? 12.972  73.858  82.491  1.00 26.03 ? 1146 GLY   B N     1 
ATOM   17560 C  CA    . GLY   B  1  1148 ? 14.412  73.988  82.631  1.00 24.93 ? 1146 GLY   B CA    1 
ATOM   17561 C  C     . GLY   B  1  1148 ? 15.010  72.992  83.598  1.00 25.45 ? 1146 GLY   B C     1 
ATOM   17562 O  O     . GLY   B  1  1148 ? 16.142  72.536  83.404  1.00 26.09 ? 1146 GLY   B O     1 
ATOM   17563 N  N     . LEU   B  1  1149 ? 14.266  72.627  84.645  1.00 25.61 ? 1147 LEU   B N     1 
ATOM   17564 C  CA    . LEU   B  1  1149 ? 14.768  71.655  85.606  1.00 27.04 ? 1147 LEU   B CA    1 
ATOM   17565 C  C     . LEU   B  1  1149 ? 15.027  70.301  84.966  1.00 26.33 ? 1147 LEU   B C     1 
ATOM   17566 O  O     . LEU   B  1  1149 ? 15.824  69.524  85.501  1.00 27.91 ? 1147 LEU   B O     1 
ATOM   17567 C  CB    . LEU   B  1  1149 ? 13.793  71.495  86.777  1.00 35.54 ? 1147 LEU   B CB    1 
ATOM   17568 N  N     . ARG   B  1  1150 ? 14.374  70.000  83.842  1.00 22.15 ? 1148 ARG   B N     1 
ATOM   17569 C  CA    . ARG   B  1  1150 ? 14.580  68.744  83.130  1.00 21.50 ? 1148 ARG   B CA    1 
ATOM   17570 C  C     . ARG   B  1  1150 ? 15.629  68.847  82.044  1.00 20.26 ? 1148 ARG   B C     1 
ATOM   17571 O  O     . ARG   B  1  1150 ? 15.880  67.850  81.367  1.00 19.78 ? 1148 ARG   B O     1 
ATOM   17572 C  CB    . ARG   B  1  1150 ? 13.288  68.314  82.447  1.00 21.98 ? 1148 ARG   B CB    1 
ATOM   17573 C  CG    . ARG   B  1  1150 ? 12.213  67.856  83.389  1.00 25.20 ? 1148 ARG   B CG    1 
ATOM   17574 C  CD    . ARG   B  1  1150 ? 11.828  66.436  83.065  1.00 24.08 ? 1148 ARG   B CD    1 
ATOM   17575 N  NE    . ARG   B  1  1150 ? 10.589  66.064  83.721  1.00 23.67 ? 1148 ARG   B NE    1 
ATOM   17576 C  CZ    . ARG   B  1  1150 ? 9.526   65.592  83.091  1.00 22.46 ? 1148 ARG   B CZ    1 
ATOM   17577 N  NH1   . ARG   B  1  1150 ? 9.538   65.354  81.786  1.00 19.31 ? 1148 ARG   B NH1   1 
ATOM   17578 N  NH2   . ARG   B  1  1150 ? 8.428   65.339  83.791  1.00 19.81 ? 1148 ARG   B NH2   1 
ATOM   17579 N  N     . VAL   B  1  1151 ? 16.209  70.021  81.833  1.00 21.71 ? 1149 VAL   B N     1 
ATOM   17580 C  CA    . VAL   B  1  1151 ? 17.063  70.278  80.680  1.00 21.16 ? 1149 VAL   B CA    1 
ATOM   17581 C  C     . VAL   B  1  1151 ? 18.468  70.569  81.167  1.00 22.87 ? 1149 VAL   B C     1 
ATOM   17582 O  O     . VAL   B  1  1151 ? 18.669  71.431  82.027  1.00 24.07 ? 1149 VAL   B O     1 
ATOM   17583 C  CB    . VAL   B  1  1151 ? 16.554  71.463  79.845  1.00 22.97 ? 1149 VAL   B CB    1 
ATOM   17584 C  CG1   . VAL   B  1  1151 ? 17.594  71.852  78.775  1.00 24.61 ? 1149 VAL   B CG1   1 
ATOM   17585 C  CG2   . VAL   B  1  1151 ? 15.222  71.130  79.198  1.00 23.56 ? 1149 VAL   B CG2   1 
ATOM   17586 N  N     . SER   B  1  1152 ? 19.435  69.865  80.610  1.00 20.10 ? 1150 SER   B N     1 
ATOM   17587 C  CA    . SER   B  1  1152 ? 20.823  70.227  80.793  1.00 19.99 ? 1150 SER   B CA    1 
ATOM   17588 C  C     . SER   B  1  1152 ? 21.467  70.242  79.421  1.00 20.92 ? 1150 SER   B C     1 
ATOM   17589 O  O     . SER   B  1  1152 ? 20.928  69.686  78.461  1.00 20.95 ? 1150 SER   B O     1 
ATOM   17590 C  CB    . SER   B  1  1152 ? 21.551  69.274  81.753  1.00 24.42 ? 1150 SER   B CB    1 
ATOM   17591 O  OG    . SER   B  1  1152 ? 21.573  67.962  81.227  1.00 28.64 ? 1150 SER   B OG    1 
ATOM   17592 N  N     . TRP   B  1  1153 ? 22.608  70.909  79.330  1.00 22.07 ? 1151 TRP   B N     1 
ATOM   17593 C  CA    . TRP   B  1  1153 ? 23.379  70.977  78.104  1.00 20.17 ? 1151 TRP   B CA    1 
ATOM   17594 C  C     . TRP   B  1  1153 ? 24.682  70.241  78.342  1.00 22.60 ? 1151 TRP   B C     1 
ATOM   17595 O  O     . TRP   B  1  1153 ? 25.315  70.426  79.384  1.00 24.05 ? 1151 TRP   B O     1 
ATOM   17596 C  CB    . TRP   B  1  1153 ? 23.662  72.429  77.729  1.00 21.41 ? 1151 TRP   B CB    1 
ATOM   17597 C  CG    . TRP   B  1  1153 ? 22.431  73.117  77.267  1.00 21.15 ? 1151 TRP   B CG    1 
ATOM   17598 C  CD1   . TRP   B  1  1153 ? 21.492  73.729  78.044  1.00 25.09 ? 1151 TRP   B CD1   1 
ATOM   17599 C  CD2   . TRP   B  1  1153 ? 21.998  73.254  75.920  1.00 21.18 ? 1151 TRP   B CD2   1 
ATOM   17600 N  NE1   . TRP   B  1  1153 ? 20.497  74.246  77.252  1.00 23.23 ? 1151 TRP   B NE1   1 
ATOM   17601 C  CE2   . TRP   B  1  1153 ? 20.778  73.964  75.941  1.00 21.84 ? 1151 TRP   B CE2   1 
ATOM   17602 C  CE3   . TRP   B  1  1153 ? 22.516  72.841  74.687  1.00 21.61 ? 1151 TRP   B CE3   1 
ATOM   17603 C  CZ2   . TRP   B  1  1153 ? 20.081  74.281  74.777  1.00 23.04 ? 1151 TRP   B CZ2   1 
ATOM   17604 C  CZ3   . TRP   B  1  1153 ? 21.824  73.156  73.539  1.00 21.23 ? 1151 TRP   B CZ3   1 
ATOM   17605 C  CH2   . TRP   B  1  1153 ? 20.614  73.866  73.591  1.00 22.55 ? 1151 TRP   B CH2   1 
ATOM   17606 N  N     . SER   B  1  1154 ? 25.071  69.397  77.395  1.00 18.22 ? 1152 SER   B N     1 
ATOM   17607 C  CA    . SER   B  1  1154 ? 26.257  68.573  77.580  1.00 18.96 ? 1152 SER   B CA    1 
ATOM   17608 C  C     . SER   B  1  1154 ? 27.304  68.931  76.547  1.00 19.51 ? 1152 SER   B C     1 
ATOM   17609 O  O     . SER   B  1  1154 ? 27.039  68.884  75.341  1.00 19.79 ? 1152 SER   B O     1 
ATOM   17610 C  CB    . SER   B  1  1154 ? 25.934  67.087  77.478  1.00 21.53 ? 1152 SER   B CB    1 
ATOM   17611 O  OG    . SER   B  1  1154 ? 27.144  66.358  77.581  1.00 19.86 ? 1152 SER   B OG    1 
ATOM   17612 N  N     . LYS   B  1  1155 ? 28.491  69.291  77.031  1.00 18.39 ? 1153 LYS   B N     1 
ATOM   17613 C  CA    . LYS   B  1  1155 ? 29.682  69.410  76.205  1.00 22.91 ? 1153 LYS   B CA    1 
ATOM   17614 C  C     . LYS   B  1  1155 ? 30.569  68.181  76.327  1.00 20.69 ? 1153 LYS   B C     1 
ATOM   17615 O  O     . LYS   B  1  1155 ? 31.719  68.204  75.867  1.00 21.46 ? 1153 LYS   B O     1 
ATOM   17616 C  CB    . LYS   B  1  1155 ? 30.468  70.663  76.592  1.00 24.45 ? 1153 LYS   B CB    1 
ATOM   17617 N  N     . ASP   B  1  1156 ? 30.076  67.121  76.955  1.00 17.77 ? 1154 ASP   B N     1 
ATOM   17618 C  CA    . ASP   B  1  1156 ? 30.888  65.928  77.184  1.00 16.75 ? 1154 ASP   B CA    1 
ATOM   17619 C  C     . ASP   B  1  1156 ? 29.903  64.783  77.437  1.00 17.43 ? 1154 ASP   B C     1 
ATOM   17620 O  O     . ASP   B  1  1156 ? 29.537  64.515  78.581  1.00 17.73 ? 1154 ASP   B O     1 
ATOM   17621 C  CB    . ASP   B  1  1156 ? 31.801  66.145  78.367  1.00 17.61 ? 1154 ASP   B CB    1 
ATOM   17622 C  CG    . ASP   B  1  1156 ? 32.820  65.039  78.522  1.00 18.15 ? 1154 ASP   B CG    1 
ATOM   17623 O  OD1   . ASP   B  1  1156 ? 32.546  63.892  78.113  1.00 18.19 ? 1154 ASP   B OD1   1 
ATOM   17624 O  OD2   . ASP   B  1  1156 ? 33.902  65.346  79.064  1.00 19.27 ? 1154 ASP   B OD2   1 
ATOM   17625 N  N     . TRP   B  1  1157 ? 29.491  64.122  76.359  1.00 15.75 ? 1155 TRP   B N     1 
ATOM   17626 C  CA    . TRP   B  1  1157 ? 28.419  63.140  76.497  1.00 15.94 ? 1155 TRP   B CA    1 
ATOM   17627 C  C     . TRP   B  1  1157 ? 28.827  62.007  77.415  1.00 17.58 ? 1155 TRP   B C     1 
ATOM   17628 O  O     . TRP   B  1  1157 ? 28.030  61.540  78.233  1.00 19.07 ? 1155 TRP   B O     1 
ATOM   17629 C  CB    . TRP   B  1  1157 ? 28.037  62.553  75.147  1.00 17.29 ? 1155 TRP   B CB    1 
ATOM   17630 C  CG    . TRP   B  1  1157 ? 27.593  63.538  74.133  1.00 16.14 ? 1155 TRP   B CG    1 
ATOM   17631 C  CD1   . TRP   B  1  1157 ? 27.356  64.878  74.308  1.00 17.54 ? 1155 TRP   B CD1   1 
ATOM   17632 C  CD2   . TRP   B  1  1157 ? 27.342  63.262  72.757  1.00 15.74 ? 1155 TRP   B CD2   1 
ATOM   17633 N  NE1   . TRP   B  1  1157 ? 26.980  65.445  73.116  1.00 18.15 ? 1155 TRP   B NE1   1 
ATOM   17634 C  CE2   . TRP   B  1  1157 ? 26.969  64.474  72.144  1.00 16.99 ? 1155 TRP   B CE2   1 
ATOM   17635 C  CE3   . TRP   B  1  1157 ? 27.413  62.101  71.976  1.00 17.74 ? 1155 TRP   B CE3   1 
ATOM   17636 C  CZ2   . TRP   B  1  1157 ? 26.655  64.558  70.790  1.00 18.56 ? 1155 TRP   B CZ2   1 
ATOM   17637 C  CZ3   . TRP   B  1  1157 ? 27.102  62.183  70.645  1.00 18.68 ? 1155 TRP   B CZ3   1 
ATOM   17638 C  CH2   . TRP   B  1  1157 ? 26.733  63.405  70.056  1.00 19.40 ? 1155 TRP   B CH2   1 
ATOM   17639 N  N     . ALA   B  1  1158 ? 30.071  61.550  77.297  1.00 16.60 ? 1156 ALA   B N     1 
ATOM   17640 C  CA    . ALA   B  1  1158 ? 30.492  60.398  78.075  1.00 16.94 ? 1156 ALA   B CA    1 
ATOM   17641 C  C     . ALA   B  1  1158 ? 30.586  60.724  79.555  1.00 19.80 ? 1156 ALA   B C     1 
ATOM   17642 O  O     . ALA   B  1  1158 ? 30.367  59.846  80.391  1.00 24.68 ? 1156 ALA   B O     1 
ATOM   17643 C  CB    . ALA   B  1  1158 ? 31.836  59.882  77.561  1.00 17.79 ? 1156 ALA   B CB    1 
ATOM   17644 N  N     . ALA   B  1  1159 ? 30.914  61.967  79.902  1.00 17.06 ? 1157 ALA   B N     1 
ATOM   17645 C  CA    . ALA   B  1  1159 ? 31.002  62.343  81.305  1.00 19.17 ? 1157 ALA   B CA    1 
ATOM   17646 C  C     . ALA   B  1  1159 ? 29.631  62.598  81.913  1.00 21.23 ? 1157 ALA   B C     1 
ATOM   17647 O  O     . ALA   B  1  1159 ? 29.469  62.463  83.128  1.00 21.95 ? 1157 ALA   B O     1 
ATOM   17648 C  CB    . ALA   B  1  1159 ? 31.886  63.580  81.470  1.00 21.47 ? 1157 ALA   B CB    1 
ATOM   17649 N  N     . ASP   B  1  1160 ? 28.645  62.959  81.094  1.00 20.68 ? 1158 ASP   B N     1 
ATOM   17650 C  CA    . ASP   B  1  1160 ? 27.360  63.440  81.578  1.00 21.81 ? 1158 ASP   B CA    1 
ATOM   17651 C  C     . ASP   B  1  1160 ? 26.290  62.362  81.595  1.00 20.84 ? 1158 ASP   B C     1 
ATOM   17652 O  O     . ASP   B  1  1160 ? 25.151  62.643  81.986  1.00 24.94 ? 1158 ASP   B O     1 
ATOM   17653 C  CB    . ASP   B  1  1160 ? 26.914  64.645  80.743  1.00 20.62 ? 1158 ASP   B CB    1 
ATOM   17654 C  CG    . ASP   B  1  1160 ? 27.821  65.847  80.936  1.00 21.69 ? 1158 ASP   B CG    1 
ATOM   17655 O  OD1   . ASP   B  1  1160 ? 28.601  65.854  81.920  1.00 25.91 ? 1158 ASP   B OD1   1 
ATOM   17656 O  OD2   . ASP   B  1  1160 ? 27.785  66.776  80.112  1.00 22.93 ? 1158 ASP   B OD2   1 
ATOM   17657 N  N     . GLY   B  1  1161 ? 26.622  61.142  81.191  1.00 19.24 ? 1159 GLY   B N     1 
ATOM   17658 C  CA    . GLY   B  1  1161 ? 25.722  60.025  81.296  1.00 22.90 ? 1159 GLY   B CA    1 
ATOM   17659 C  C     . GLY   B  1  1161 ? 25.732  59.412  82.683  1.00 23.67 ? 1159 GLY   B C     1 
ATOM   17660 O  O     . GLY   B  1  1161 ? 26.319  59.957  83.627  1.00 27.49 ? 1159 GLY   B O     1 
ATOM   17661 N  N     . PRO   B  1  1162 ? 25.118  58.239  82.827  1.00 24.91 ? 1160 PRO   B N     1 
ATOM   17662 C  CA    . PRO   B  1  1162 ? 24.507  57.430  81.772  1.00 22.04 ? 1160 PRO   B CA    1 
ATOM   17663 C  C     . PRO   B  1  1162 ? 23.176  57.993  81.319  1.00 21.05 ? 1160 PRO   B C     1 
ATOM   17664 O  O     . PRO   B  1  1162 ? 22.380  58.546  82.078  1.00 22.21 ? 1160 PRO   B O     1 
ATOM   17665 C  CB    . PRO   B  1  1162 ? 24.344  56.056  82.442  1.00 24.46 ? 1160 PRO   B CB    1 
ATOM   17666 C  CG    . PRO   B  1  1162 ? 24.131  56.381  83.884  1.00 27.48 ? 1160 PRO   B CG    1 
ATOM   17667 C  CD    . PRO   B  1  1162 ? 25.053  57.559  84.137  1.00 28.00 ? 1160 PRO   B CD    1 
ATOM   17668 N  N     . PHE   B  1  1163 ? 22.951  57.866  80.023  1.00 16.89 ? 1161 PHE   B N     1 
ATOM   17669 C  CA    . PHE   B  1  1163 ? 21.676  58.178  79.413  1.00 17.49 ? 1161 PHE   B CA    1 
ATOM   17670 C  C     . PHE   B  1  1163 ? 20.874  56.894  79.272  1.00 15.46 ? 1161 PHE   B C     1 
ATOM   17671 O  O     . PHE   B  1  1163 ? 21.354  55.791  79.532  1.00 17.79 ? 1161 PHE   B O     1 
ATOM   17672 C  CB    . PHE   B  1  1163 ? 21.914  58.895  78.082  1.00 16.73 ? 1161 PHE   B CB    1 
ATOM   17673 C  CG    . PHE   B  1  1163 ? 22.741  60.125  78.228  1.00 16.73 ? 1161 PHE   B CG    1 
ATOM   17674 C  CD1   . PHE   B  1  1163 ? 22.291  61.183  78.995  1.00 22.84 ? 1161 PHE   B CD1   1 
ATOM   17675 C  CD2   . PHE   B  1  1163 ? 23.996  60.209  77.646  1.00 19.19 ? 1161 PHE   B CD2   1 
ATOM   17676 C  CE1   . PHE   B  1  1163 ? 23.064  62.316  79.174  1.00 22.71 ? 1161 PHE   B CE1   1 
ATOM   17677 C  CE2   . PHE   B  1  1163 ? 24.765  61.350  77.804  1.00 20.57 ? 1161 PHE   B CE2   1 
ATOM   17678 C  CZ    . PHE   B  1  1163 ? 24.299  62.404  78.565  1.00 20.12 ? 1161 PHE   B CZ    1 
ATOM   17679 N  N     . ALA   B  1  1164 ? 19.615  57.052  78.886  1.00 16.14 ? 1162 ALA   B N     1 
ATOM   17680 C  CA    . ALA   B  1  1164 ? 18.722  55.917  78.699  1.00 16.79 ? 1162 ALA   B CA    1 
ATOM   17681 C  C     . ALA   B  1  1164 ? 18.138  55.883  77.303  1.00 18.29 ? 1162 ALA   B C     1 
ATOM   17682 O  O     . ALA   B  1  1164 ? 17.193  55.127  77.045  1.00 19.71 ? 1162 ALA   B O     1 
ATOM   17683 C  CB    . ALA   B  1  1164 ? 17.594  55.944  79.735  1.00 17.67 ? 1162 ALA   B CB    1 
ATOM   17684 N  N     . GLY   B  1  1165 ? 18.685  56.677  76.400  1.00 15.62 ? 1163 GLY   B N     1 
ATOM   17685 C  CA    . GLY   B  1  1165 ? 18.227  56.756  75.034  1.00 16.44 ? 1163 GLY   B CA    1 
ATOM   17686 C  C     . GLY   B  1  1165 ? 18.824  57.984  74.396  1.00 16.37 ? 1163 GLY   B C     1 
ATOM   17687 O  O     . GLY   B  1  1165 ? 19.437  58.818  75.059  1.00 16.14 ? 1163 GLY   B O     1 
ATOM   17688 N  N     . ALA   B  1  1166 ? 18.631  58.090  73.088  1.00 16.74 ? 1164 ALA   B N     1 
ATOM   17689 C  CA    . ALA   B  1  1166 ? 19.155  59.248  72.389  1.00 14.77 ? 1164 ALA   B CA    1 
ATOM   17690 C  C     . ALA   B  1  1166 ? 18.254  59.554  71.216  1.00 16.11 ? 1164 ALA   B C     1 
ATOM   17691 O  O     . ALA   B  1  1166 ? 17.746  58.645  70.560  1.00 18.27 ? 1164 ALA   B O     1 
ATOM   17692 C  CB    . ALA   B  1  1166 ? 20.575  58.995  71.882  1.00 16.95 ? 1164 ALA   B CB    1 
ATOM   17693 N  N     . LEU   B  1  1167 ? 18.053  60.838  70.964  1.00 14.97 ? 1165 LEU   B N     1 
ATOM   17694 C  CA    . LEU   B  1  1167 ? 17.352  61.295  69.777  1.00 14.97 ? 1165 LEU   B CA    1 
ATOM   17695 C  C     . LEU   B  1  1167 ? 18.329  62.127  68.968  1.00 17.44 ? 1165 LEU   B C     1 
ATOM   17696 O  O     . LEU   B  1  1167 ? 18.979  63.020  69.513  1.00 17.10 ? 1165 LEU   B O     1 
ATOM   17697 C  CB    . LEU   B  1  1167 ? 16.146  62.151  70.154  1.00 16.97 ? 1165 LEU   B CB    1 
ATOM   17698 C  CG    . LEU   B  1  1167 ? 15.157  61.472  71.098  1.00 14.96 ? 1165 LEU   B CG    1 
ATOM   17699 C  CD1   . LEU   B  1  1167 ? 14.042  62.431  71.427  1.00 18.34 ? 1165 LEU   B CD1   1 
ATOM   17700 C  CD2   . LEU   B  1  1167 ? 14.600  60.220  70.418  1.00 19.13 ? 1165 LEU   B CD2   1 
ATOM   17701 N  N     . VAL   B  1  1168 ? 18.428  61.832  67.682  1.00 16.43 ? 1166 VAL   B N     1 
ATOM   17702 C  CA    . VAL   B  1  1168 ? 19.432  62.443  66.828  1.00 16.62 ? 1166 VAL   B CA    1 
ATOM   17703 C  C     . VAL   B  1  1168 ? 18.730  63.040  65.625  1.00 17.23 ? 1166 VAL   B C     1 
ATOM   17704 O  O     . VAL   B  1  1168 ? 17.822  62.429  65.052  1.00 17.33 ? 1166 VAL   B O     1 
ATOM   17705 C  CB    . VAL   B  1  1168 ? 20.465  61.390  66.391  1.00 17.11 ? 1166 VAL   B CB    1 
ATOM   17706 C  CG1   . VAL   B  1  1168 ? 21.516  62.017  65.470  1.00 17.69 ? 1166 VAL   B CG1   1 
ATOM   17707 C  CG2   . VAL   B  1  1168 ? 21.091  60.728  67.623  1.00 17.59 ? 1166 VAL   B CG2   1 
ATOM   17708 N  N     . GLU   B  1  1169 ? 19.133  64.248  65.257  1.00 17.06 ? 1167 GLU   B N     1 
ATOM   17709 C  CA    . GLU   B  1  1169 ? 18.662  64.901  64.047  1.00 17.55 ? 1167 GLU   B CA    1 
ATOM   17710 C  C     . GLU   B  1  1169 ? 19.867  65.178  63.163  1.00 19.84 ? 1167 GLU   B C     1 
ATOM   17711 O  O     . GLU   B  1  1169 ? 20.881  65.689  63.641  1.00 20.40 ? 1167 GLU   B O     1 
ATOM   17712 C  CB    . GLU   B  1  1169 ? 17.984  66.226  64.383  1.00 17.55 ? 1167 GLU   B CB    1 
ATOM   17713 C  CG    . GLU   B  1  1169 ? 17.526  67.014  63.157  1.00 19.55 ? 1167 GLU   B CG    1 
ATOM   17714 C  CD    . GLU   B  1  1169 ? 17.132  68.441  63.501  1.00 20.07 ? 1167 GLU   B CD    1 
ATOM   17715 O  OE1   . GLU   B  1  1169 ? 17.392  68.880  64.636  1.00 19.93 ? 1167 GLU   B OE1   1 
ATOM   17716 O  OE2   . GLU   B  1  1169 ? 16.546  69.124  62.636  1.00 22.95 ? 1167 GLU   B OE2   1 
ATOM   17717 N  N     . GLY   B  1  1170 ? 19.761  64.844  61.890  1.00 20.31 ? 1168 GLY   B N     1 
ATOM   17718 C  CA    . GLY   B  1  1170 ? 20.830  65.179  60.972  1.00 20.28 ? 1168 GLY   B CA    1 
ATOM   17719 C  C     . GLY   B  1  1170 ? 20.686  64.421  59.681  1.00 23.14 ? 1168 GLY   B C     1 
ATOM   17720 O  O     . GLY   B  1  1170 ? 19.803  63.584  59.517  1.00 20.91 ? 1168 GLY   B O     1 
ATOM   17721 N  N     . ASP   B  1  1171 ? 21.574  64.745  58.744  1.00 23.42 ? 1169 ASP   B N     1 
ATOM   17722 C  CA    . ASP   B  1  1171 ? 21.630  63.960  57.520  1.00 21.22 ? 1169 ASP   B CA    1 
ATOM   17723 C  C     . ASP   B  1  1171 ? 22.325  62.626  57.777  1.00 22.52 ? 1169 ASP   B C     1 
ATOM   17724 O  O     . ASP   B  1  1171 ? 22.787  62.334  58.883  1.00 20.89 ? 1169 ASP   B O     1 
ATOM   17725 C  CB    . ASP   B  1  1171 ? 22.237  64.760  56.362  1.00 22.76 ? 1169 ASP   B CB    1 
ATOM   17726 C  CG    . ASP   B  1  1171 ? 23.694  65.124  56.578  1.00 26.81 ? 1169 ASP   B CG    1 
ATOM   17727 O  OD1   . ASP   B  1  1171 ? 24.338  64.656  57.542  1.00 25.24 ? 1169 ASP   B OD1   1 
ATOM   17728 O  OD2   . ASP   B  1  1171 ? 24.214  65.911  55.757  1.00 31.80 ? 1169 ASP   B OD2   1 
ATOM   17729 N  N     . ALA   B  1  1172 ? 22.399  61.801  56.735  1.00 22.81 ? 1170 ALA   B N     1 
ATOM   17730 C  CA    . ALA   B  1  1172 ? 22.892  60.439  56.904  1.00 25.18 ? 1170 ALA   B CA    1 
ATOM   17731 C  C     . ALA   B  1  1172 ? 24.285  60.420  57.515  1.00 23.66 ? 1170 ALA   B C     1 
ATOM   17732 O  O     . ALA   B  1  1172 ? 24.556  59.655  58.446  1.00 23.58 ? 1170 ALA   B O     1 
ATOM   17733 C  CB    . ALA   B  1  1172 ? 22.878  59.697  55.568  1.00 25.66 ? 1170 ALA   B CB    1 
ATOM   17734 N  N     . GLU   B  1  1173 ? 25.198  61.247  57.004  1.00 24.06 ? 1171 GLU   B N     1 
ATOM   17735 C  CA    . GLU   B  1  1173 ? 26.544  61.181  57.554  1.00 23.13 ? 1171 GLU   B CA    1 
ATOM   17736 C  C     . GLU   B  1  1173 ? 26.614  61.722  58.978  1.00 22.90 ? 1171 GLU   B C     1 
ATOM   17737 O  O     . GLU   B  1  1173 ? 27.411  61.227  59.782  1.00 21.83 ? 1171 GLU   B O     1 
ATOM   17738 C  CB    . GLU   B  1  1173 ? 27.558  61.828  56.613  1.00 34.12 ? 1171 GLU   B CB    1 
ATOM   17739 C  CG    . GLU   B  1  1173 ? 27.818  60.986  55.361  1.00 38.10 ? 1171 GLU   B CG    1 
ATOM   17740 C  CD    . GLU   B  1  1173 ? 28.116  59.511  55.666  1.00 36.46 ? 1171 GLU   B CD    1 
ATOM   17741 O  OE1   . GLU   B  1  1173 ? 28.961  59.217  56.543  1.00 35.02 ? 1171 GLU   B OE1   1 
ATOM   17742 O  OE2   . GLU   B  1  1173 ? 27.500  58.636  55.018  1.00 44.43 ? 1171 GLU   B OE2   1 
ATOM   17743 N  N     . ARG   B  1  1174 ? 25.788  62.717  59.311  1.00 21.40 ? 1172 ARG   B N     1 
ATOM   17744 C  CA    . ARG   B  1  1174 ? 25.718  63.180  60.693  1.00 22.85 ? 1172 ARG   B CA    1 
ATOM   17745 C  C     . ARG   B  1  1174 ? 25.195  62.078  61.601  1.00 18.80 ? 1172 ARG   B C     1 
ATOM   17746 O  O     . ARG   B  1  1174 ? 25.754  61.826  62.671  1.00 20.20 ? 1172 ARG   B O     1 
ATOM   17747 C  CB    . ARG   B  1  1174 ? 24.824  64.415  60.779  1.00 22.40 ? 1172 ARG   B CB    1 
ATOM   17748 C  CG    . ARG   B  1  1174 ? 24.579  64.929  62.192  1.00 21.18 ? 1172 ARG   B CG    1 
ATOM   17749 C  CD    . ARG   B  1  1174 ? 25.880  65.318  62.869  1.00 24.80 ? 1172 ARG   B CD    1 
ATOM   17750 N  NE    . ARG   B  1  1174 ? 25.635  65.871  64.193  1.00 23.14 ? 1172 ARG   B NE    1 
ATOM   17751 C  CZ    . ARG   B  1  1174 ? 26.549  65.965  65.148  1.00 21.80 ? 1172 ARG   B CZ    1 
ATOM   17752 N  NH1   . ARG   B  1  1174 ? 27.797  65.567  64.955  1.00 23.05 ? 1172 ARG   B NH1   1 
ATOM   17753 N  NH2   . ARG   B  1  1174 ? 26.198  66.441  66.340  1.00 22.14 ? 1172 ARG   B NH2   1 
ATOM   17754 N  N     . ILE   B  1  1175 ? 24.141  61.396  61.161  1.00 18.91 ? 1173 ILE   B N     1 
ATOM   17755 C  CA    . ILE   B  1  1175 ? 23.588  60.293  61.937  1.00 18.56 ? 1173 ILE   B CA    1 
ATOM   17756 C  C     . ILE   B  1  1175 ? 24.642  59.227  62.180  1.00 19.38 ? 1173 ILE   B C     1 
ATOM   17757 O  O     . ILE   B  1  1175 ? 24.797  58.732  63.301  1.00 19.07 ? 1173 ILE   B O     1 
ATOM   17758 C  CB    . ILE   B  1  1175 ? 22.355  59.721  61.232  1.00 17.61 ? 1173 ILE   B CB    1 
ATOM   17759 C  CG1   . ILE   B  1  1175 ? 21.213  60.733  61.327  1.00 19.33 ? 1173 ILE   B CG1   1 
ATOM   17760 C  CG2   . ILE   B  1  1175 ? 21.988  58.397  61.861  1.00 18.56 ? 1173 ILE   B CG2   1 
ATOM   17761 C  CD1   . ILE   B  1  1175 ? 20.030  60.404  60.449  1.00 20.09 ? 1173 ILE   B CD1   1 
ATOM   17762 N  N     . ARG   B  1  1176 ? 25.383  58.849  61.134  1.00 20.37 ? 1174 ARG   B N     1 
ATOM   17763 C  CA    . ARG   B  1  1176 ? 26.404  57.819  61.308  1.00 18.99 ? 1174 ARG   B CA    1 
ATOM   17764 C  C     . ARG   B  1  1176 ? 27.460  58.251  62.319  1.00 19.23 ? 1174 ARG   B C     1 
ATOM   17765 O  O     . ARG   B  1  1176 ? 27.856  57.474  63.190  1.00 20.15 ? 1174 ARG   B O     1 
ATOM   17766 C  CB    . ARG   B  1  1176 ? 27.064  57.482  59.971  1.00 22.19 ? 1174 ARG   B CB    1 
ATOM   17767 C  CG    . ARG   B  1  1176 ? 27.979  56.271  60.046  1.00 24.16 ? 1174 ARG   B CG    1 
ATOM   17768 C  CD    . ARG   B  1  1176 ? 28.912  56.177  58.821  1.00 28.78 ? 1174 ARG   B CD    1 
ATOM   17769 N  NE    . ARG   B  1  1176 ? 28.212  56.345  57.554  1.00 31.97 ? 1174 ARG   B NE    1 
ATOM   17770 C  CZ    . ARG   B  1  1176 ? 27.702  55.353  56.836  1.00 32.26 ? 1174 ARG   B CZ    1 
ATOM   17771 N  NH1   . ARG   B  1  1176 ? 27.766  54.097  57.248  1.00 31.25 ? 1174 ARG   B NH1   1 
ATOM   17772 N  NH2   . ARG   B  1  1176 ? 27.130  55.625  55.667  1.00 36.79 ? 1174 ARG   B NH2   1 
ATOM   17773 N  N     . ALA   B  1  1177 ? 27.940  59.495  62.202  1.00 20.55 ? 1175 ALA   B N     1 
ATOM   17774 C  CA    . ALA   B  1  1177 ? 28.969  59.978  63.115  1.00 20.22 ? 1175 ALA   B CA    1 
ATOM   17775 C  C     . ALA   B  1  1177 ? 28.461  60.009  64.551  1.00 18.59 ? 1175 ALA   B C     1 
ATOM   17776 O  O     . ALA   B  1  1177 ? 29.169  59.619  65.481  1.00 19.82 ? 1175 ALA   B O     1 
ATOM   17777 C  CB    . ALA   B  1  1177 ? 29.426  61.376  62.695  1.00 21.86 ? 1175 ALA   B CB    1 
ATOM   17778 N  N     . VAL   B  1  1178 ? 27.231  60.466  64.743  1.00 18.83 ? 1176 VAL   B N     1 
ATOM   17779 C  CA    . VAL   B  1  1178 ? 26.676  60.518  66.091  1.00 19.00 ? 1176 VAL   B CA    1 
ATOM   17780 C  C     . VAL   B  1  1178 ? 26.456  59.113  66.624  1.00 17.99 ? 1176 VAL   B C     1 
ATOM   17781 O  O     . VAL   B  1  1178 ? 26.746  58.819  67.786  1.00 18.58 ? 1176 VAL   B O     1 
ATOM   17782 C  CB    . VAL   B  1  1178 ? 25.376  61.335  66.084  1.00 18.08 ? 1176 VAL   B CB    1 
ATOM   17783 C  CG1   . VAL   B  1  1178 ? 24.628  61.176  67.419  1.00 19.99 ? 1176 VAL   B CG1   1 
ATOM   17784 C  CG2   . VAL   B  1  1178 ? 25.691  62.800  65.799  1.00 21.27 ? 1176 VAL   B CG2   1 
ATOM   17785 N  N     . ASN   B  1  1179 ? 25.945  58.224  65.778  1.00 18.04 ? 1177 ASN   B N     1 
ATOM   17786 C  CA    . ASN   B  1  1179 ? 25.720  56.855  66.215  1.00 19.04 ? 1177 ASN   B CA    1 
ATOM   17787 C  C     . ASN   B  1  1179 ? 27.030  56.191  66.616  1.00 18.08 ? 1177 ASN   B C     1 
ATOM   17788 O  O     . ASN   B  1  1179 ? 27.096  55.477  67.623  1.00 18.97 ? 1177 ASN   B O     1 
ATOM   17789 C  CB    . ASN   B  1  1179 ? 25.027  56.096  65.090  1.00 18.85 ? 1177 ASN   B CB    1 
ATOM   17790 C  CG    . ASN   B  1  1179 ? 24.335  54.840  65.566  1.00 20.48 ? 1177 ASN   B CG    1 
ATOM   17791 O  OD1   . ASN   B  1  1179 ? 23.931  54.720  66.727  1.00 22.08 ? 1177 ASN   B OD1   1 
ATOM   17792 N  ND2   . ASN   B  1  1179 ? 24.177  53.893  64.652  1.00 21.61 ? 1177 ASN   B ND2   1 
ATOM   17793 N  N     . LYS   B  1  1180 ? 28.102  56.445  65.860  1.00 18.62 ? 1178 LYS   B N     1 
ATOM   17794 C  CA    . LYS   B  1  1180 ? 29.407  55.935  66.256  1.00 20.55 ? 1178 LYS   B CA    1 
ATOM   17795 C  C     . LYS   B  1  1180 ? 29.834  56.489  67.608  1.00 17.74 ? 1178 LYS   B C     1 
ATOM   17796 O  O     . LYS   B  1  1180 ? 30.333  55.745  68.460  1.00 20.10 ? 1178 LYS   B O     1 
ATOM   17797 C  CB    . LYS   B  1  1180 ? 30.452  56.268  65.190  1.00 22.13 ? 1178 LYS   B CB    1 
ATOM   17798 C  CG    . LYS   B  1  1180 ? 30.393  55.376  63.973  1.00 24.94 ? 1178 LYS   B CG    1 
ATOM   17799 C  CD    . LYS   B  1  1180 ? 31.442  55.802  62.940  1.00 28.11 ? 1178 LYS   B CD    1 
ATOM   17800 C  CE    . LYS   B  1  1180 ? 32.843  55.591  63.470  1.00 40.67 ? 1178 LYS   B CE    1 
ATOM   17801 N  NZ    . LYS   B  1  1180 ? 33.188  54.143  63.548  1.00 51.39 ? 1178 LYS   B NZ    1 
ATOM   17802 N  N     . ALA   B  1  1181 ? 29.659  57.800  67.816  1.00 18.51 ? 1179 ALA   B N     1 
ATOM   17803 C  CA    . ALA   B  1  1181 ? 30.040  58.396  69.095  1.00 18.83 ? 1179 ALA   B CA    1 
ATOM   17804 C  C     . ALA   B  1  1181 ? 29.214  57.814  70.236  1.00 18.32 ? 1179 ALA   B C     1 
ATOM   17805 O  O     . ALA   B  1  1181 ? 29.741  57.545  71.319  1.00 19.73 ? 1179 ALA   B O     1 
ATOM   17806 C  CB    . ALA   B  1  1181 ? 29.864  59.913  69.036  1.00 18.49 ? 1179 ALA   B CB    1 
ATOM   17807 N  N     . ILE   B  1  1182 ? 27.921  57.595  69.998  1.00 17.33 ? 1180 ILE   B N     1 
ATOM   17808 C  CA    . ILE   B  1  1182 ? 27.076  57.028  71.039  1.00 18.60 ? 1180 ILE   B CA    1 
ATOM   17809 C  C     . ILE   B  1  1182 ? 27.503  55.604  71.365  1.00 18.08 ? 1180 ILE   B C     1 
ATOM   17810 O  O     . ILE   B  1  1182 ? 27.534  55.205  72.530  1.00 18.69 ? 1180 ILE   B O     1 
ATOM   17811 C  CB    . ILE   B  1  1182 ? 25.602  57.113  70.620  1.00 18.92 ? 1180 ILE   B CB    1 
ATOM   17812 C  CG1   . ILE   B  1  1182 ? 25.150  58.568  70.662  1.00 18.97 ? 1180 ILE   B CG1   1 
ATOM   17813 C  CG2   . ILE   B  1  1182 ? 24.748  56.236  71.535  1.00 21.58 ? 1180 ILE   B CG2   1 
ATOM   17814 C  CD1   . ILE   B  1  1182 ? 23.773  58.795  70.048  1.00 20.51 ? 1180 ILE   B CD1   1 
ATOM   17815 N  N     . ALA   B  1  1183 ? 27.849  54.812  70.344  1.00 19.94 ? 1181 ALA   B N     1 
ATOM   17816 C  CA    . ALA   B  1  1183 ? 28.256  53.441  70.610  1.00 20.72 ? 1181 ALA   B CA    1 
ATOM   17817 C  C     . ALA   B  1  1183 ? 29.530  53.373  71.424  1.00 22.37 ? 1181 ALA   B C     1 
ATOM   17818 O  O     . ALA   B  1  1183 ? 29.774  52.364  72.097  1.00 25.22 ? 1181 ALA   B O     1 
ATOM   17819 C  CB    . ALA   B  1  1183 ? 28.397  52.652  69.306  1.00 20.16 ? 1181 ALA   B CB    1 
ATOM   17820 N  N     . ALA   B  1  1184 ? 30.333  54.429  71.403  1.00 19.54 ? 1182 ALA   B N     1 
ATOM   17821 C  CA    . ALA   B  1  1184 ? 31.541  54.487  72.208  1.00 20.12 ? 1182 ALA   B CA    1 
ATOM   17822 C  C     . ALA   B  1  1184 ? 31.319  55.048  73.607  1.00 21.12 ? 1182 ALA   B C     1 
ATOM   17823 O  O     . ALA   B  1  1184 ? 32.280  55.154  74.368  1.00 21.30 ? 1182 ALA   B O     1 
ATOM   17824 C  CB    . ALA   B  1  1184 ? 32.628  55.303  71.492  1.00 22.65 ? 1182 ALA   B CB    1 
ATOM   17825 N  N     . LEU   B  1  1185 ? 30.097  55.427  73.968  1.00 19.16 ? 1183 LEU   B N     1 
ATOM   17826 C  CA    . LEU   B  1  1185 ? 29.885  55.914  75.324  1.00 19.58 ? 1183 LEU   B CA    1 
ATOM   17827 C  C     . LEU   B  1  1185 ? 29.997  54.755  76.308  1.00 19.96 ? 1183 LEU   B C     1 
ATOM   17828 O  O     . LEU   B  1  1185 ? 29.585  53.631  76.005  1.00 22.95 ? 1183 LEU   B O     1 
ATOM   17829 C  CB    . LEU   B  1  1185 ? 28.517  56.575  75.469  1.00 18.23 ? 1183 LEU   B CB    1 
ATOM   17830 C  CG    . LEU   B  1  1185 ? 28.337  57.791  74.567  1.00 18.56 ? 1183 LEU   B CG    1 
ATOM   17831 C  CD1   . LEU   B  1  1185 ? 26.900  58.253  74.646  1.00 18.36 ? 1183 LEU   B CD1   1 
ATOM   17832 C  CD2   . LEU   B  1  1185 ? 29.293  58.931  74.933  1.00 19.18 ? 1183 LEU   B CD2   1 
ATOM   17833 N  N     . PRO   B  1  1186 ? 30.568  54.983  77.477  1.00 19.49 ? 1184 PRO   B N     1 
ATOM   17834 C  CA    . PRO   B  1  1186 ? 30.593  53.931  78.490  1.00 21.38 ? 1184 PRO   B CA    1 
ATOM   17835 C  C     . PRO   B  1  1186 ? 29.202  53.727  79.058  1.00 19.29 ? 1184 PRO   B C     1 
ATOM   17836 O  O     . PRO   B  1  1186 ? 28.318  54.571  78.934  1.00 22.43 ? 1184 PRO   B O     1 
ATOM   17837 C  CB    . PRO   B  1  1186 ? 31.535  54.496  79.558  1.00 26.93 ? 1184 PRO   B CB    1 
ATOM   17838 C  CG    . PRO   B  1  1186 ? 31.379  55.981  79.432  1.00 29.12 ? 1184 PRO   B CG    1 
ATOM   17839 C  CD    . PRO   B  1  1186 ? 31.127  56.255  77.968  1.00 23.92 ? 1184 PRO   B CD    1 
ATOM   17840 N  N     . GLY   B  1  1187 ? 29.027  52.584  79.699  1.00 21.71 ? 1185 GLY   B N     1 
ATOM   17841 C  CA    . GLY   B  1  1187 ? 27.793  52.299  80.385  1.00 21.25 ? 1185 GLY   B CA    1 
ATOM   17842 C  C     . GLY   B  1  1187 ? 26.787  51.605  79.501  1.00 19.36 ? 1185 GLY   B C     1 
ATOM   17843 O  O     . GLY   B  1  1187 ? 27.120  50.743  78.692  1.00 23.14 ? 1185 GLY   B O     1 
ATOM   17844 N  N     . PRO   B  1  1188 ? 25.523  51.961  79.659  1.00 17.16 ? 1186 PRO   B N     1 
ATOM   17845 C  CA    . PRO   B  1  1188 ? 24.468  51.232  78.957  1.00 17.33 ? 1186 PRO   B CA    1 
ATOM   17846 C  C     . PRO   B  1  1188 ? 24.520  51.459  77.458  1.00 18.33 ? 1186 PRO   B C     1 
ATOM   17847 O  O     . PRO   B  1  1188 ? 24.972  52.496  76.965  1.00 20.16 ? 1186 PRO   B O     1 
ATOM   17848 C  CB    . PRO   B  1  1188 ? 23.180  51.810  79.548  1.00 20.60 ? 1186 PRO   B CB    1 
ATOM   17849 C  CG    . PRO   B  1  1188 ? 23.572  53.145  80.083  1.00 26.98 ? 1186 PRO   B CG    1 
ATOM   17850 C  CD    . PRO   B  1  1188 ? 24.998  53.020  80.532  1.00 20.13 ? 1186 PRO   B CD    1 
ATOM   17851 N  N     . LEU   B  1  1189 ? 24.041  50.466  76.732  1.00 18.00 ? 1187 LEU   B N     1 
ATOM   17852 C  CA    . LEU   B  1  1189 ? 23.859  50.607  75.296  1.00 16.37 ? 1187 LEU   B CA    1 
ATOM   17853 C  C     . LEU   B  1  1189 ? 22.613  51.439  75.061  1.00 16.84 ? 1187 LEU   B C     1 
ATOM   17854 O  O     . LEU   B  1  1189 ? 21.528  51.061  75.515  1.00 19.91 ? 1187 LEU   B O     1 
ATOM   17855 C  CB    . LEU   B  1  1189 ? 23.657  49.236  74.665  1.00 18.53 ? 1187 LEU   B CB    1 
ATOM   17856 C  CG    . LEU   B  1  1189 ? 24.923  48.439  74.369  1.00 19.42 ? 1187 LEU   B CG    1 
ATOM   17857 C  CD1   . LEU   B  1  1189 ? 25.512  47.859  75.655  1.00 26.72 ? 1187 LEU   B CD1   1 
ATOM   17858 C  CD2   . LEU   B  1  1189 ? 24.588  47.348  73.364  1.00 23.53 ? 1187 LEU   B CD2   1 
ATOM   17859 N  N     . LEU   B  1  1190 ? 22.747  52.568  74.378  1.00 16.41 ? 1188 LEU   B N     1 
ATOM   17860 C  CA    . LEU   B  1  1190 ? 21.613  53.468  74.219  1.00 17.80 ? 1188 LEU   B CA    1 
ATOM   17861 C  C     . LEU   B  1  1190 ? 20.759  53.076  73.028  1.00 18.67 ? 1188 LEU   B C     1 
ATOM   17862 O  O     . LEU   B  1  1190 ? 21.267  52.775  71.940  1.00 18.14 ? 1188 LEU   B O     1 
ATOM   17863 C  CB    . LEU   B  1  1190 ? 22.068  54.915  74.035  1.00 17.87 ? 1188 LEU   B CB    1 
ATOM   17864 C  CG    . LEU   B  1  1190 ? 22.944  55.507  75.126  1.00 16.33 ? 1188 LEU   B CG    1 
ATOM   17865 C  CD1   . LEU   B  1  1190 ? 23.042  57.000  74.883  1.00 18.76 ? 1188 LEU   B CD1   1 
ATOM   17866 C  CD2   . LEU   B  1  1190 ? 22.383  55.215  76.514  1.00 19.40 ? 1188 LEU   B CD2   1 
ATOM   17867 N  N     . LEU   B  1  1191 ? 19.455  53.123  73.238  1.00 17.36 ? 1189 LEU   B N     1 
ATOM   17868 C  CA    . LEU   B  1  1191 ? 18.504  52.989  72.143  1.00 15.46 ? 1189 LEU   B CA    1 
ATOM   17869 C  C     . LEU   B  1  1191 ? 18.431  54.337  71.431  1.00 17.88 ? 1189 LEU   B C     1 
ATOM   17870 O  O     . LEU   B  1  1191 ? 17.916  55.320  71.979  1.00 19.31 ? 1189 LEU   B O     1 
ATOM   17871 C  CB    . LEU   B  1  1191 ? 17.147  52.528  72.672  1.00 16.57 ? 1189 LEU   B CB    1 
ATOM   17872 C  CG    . LEU   B  1  1191 ? 16.186  51.910  71.657  1.00 17.53 ? 1189 LEU   B CG    1 
ATOM   17873 C  CD1   . LEU   B  1  1191 ? 15.036  51.265  72.398  1.00 17.50 ? 1189 LEU   B CD1   1 
ATOM   17874 C  CD2   . LEU   B  1  1191 ? 15.675  52.959  70.676  1.00 17.40 ? 1189 LEU   B CD2   1 
ATOM   17875 N  N     . VAL   B  1  1192 ? 18.981  54.381  70.224  1.00 16.36 ? 1190 VAL   B N     1 
ATOM   17876 C  CA    . VAL   B  1  1192 ? 19.138  55.606  69.453  1.00 17.67 ? 1190 VAL   B CA    1 
ATOM   17877 C  C     . VAL   B  1  1192 ? 18.018  55.687  68.435  1.00 17.83 ? 1190 VAL   B C     1 
ATOM   17878 O  O     . VAL   B  1  1192 ? 17.746  54.712  67.726  1.00 18.98 ? 1190 VAL   B O     1 
ATOM   17879 C  CB    . VAL   B  1  1192 ? 20.491  55.616  68.726  1.00 18.02 ? 1190 VAL   B CB    1 
ATOM   17880 C  CG1   . VAL   B  1  1192 ? 20.640  56.852  67.854  1.00 19.12 ? 1190 VAL   B CG1   1 
ATOM   17881 C  CG2   . VAL   B  1  1192 ? 21.646  55.548  69.724  1.00 18.66 ? 1190 VAL   B CG2   1 
ATOM   17882 N  N     . GLN   B  1  1193 ? 17.405  56.858  68.325  1.00 15.96 ? 1191 GLN   B N     1 
ATOM   17883 C  CA    . GLN   B  1  1193 ? 16.469  57.148  67.252  1.00 14.53 ? 1191 GLN   B CA    1 
ATOM   17884 C  C     . GLN   B  1  1193 ? 16.974  58.348  66.482  1.00 16.77 ? 1191 GLN   B C     1 
ATOM   17885 O  O     . GLN   B  1  1193 ? 17.303  59.379  67.077  1.00 17.28 ? 1191 GLN   B O     1 
ATOM   17886 C  CB    . GLN   B  1  1193 ? 15.094  57.486  67.809  1.00 15.95 ? 1191 GLN   B CB    1 
ATOM   17887 C  CG    . GLN   B  1  1193 ? 14.525  56.415  68.705  1.00 17.43 ? 1191 GLN   B CG    1 
ATOM   17888 C  CD    . GLN   B  1  1193 ? 13.059  56.636  68.941  1.00 19.65 ? 1191 GLN   B CD    1 
ATOM   17889 O  OE1   . GLN   B  1  1193 ? 12.261  56.539  68.024  1.00 18.31 ? 1191 GLN   B OE1   1 
ATOM   17890 N  NE2   . GLN   B  1  1193 ? 12.700  56.959  70.169  1.00 18.76 ? 1191 GLN   B NE2   1 
ATOM   17891 N  N     . ALA   B  1  1194 ? 17.010  58.222  65.162  1.00 16.82 ? 1192 ALA   B N     1 
ATOM   17892 C  CA    . ALA   B  1  1194 ? 17.528  59.278  64.312  1.00 16.82 ? 1192 ALA   B CA    1 
ATOM   17893 C  C     . ALA   B  1  1194 ? 16.508  59.663  63.258  1.00 19.08 ? 1192 ALA   B C     1 
ATOM   17894 O  O     . ALA   B  1  1194 ? 15.693  58.847  62.815  1.00 21.66 ? 1192 ALA   B O     1 
ATOM   17895 C  CB    . ALA   B  1  1194 ? 18.816  58.840  63.624  1.00 19.10 ? 1192 ALA   B CB    1 
ATOM   17896 N  N     . ALA   B  1  1195 ? 16.563  60.926  62.857  1.00 18.07 ? 1193 ALA   B N     1 
ATOM   17897 C  CA    . ALA   B  1  1195 ? 15.689  61.416  61.806  1.00 19.41 ? 1193 ALA   B CA    1 
ATOM   17898 C  C     . ALA   B  1  1195 ? 16.368  62.608  61.172  1.00 20.16 ? 1193 ALA   B C     1 
ATOM   17899 O  O     . ALA   B  1  1195 ? 17.163  63.290  61.813  1.00 20.22 ? 1193 ALA   B O     1 
ATOM   17900 C  CB    . ALA   B  1  1195 ? 14.332  61.853  62.368  1.00 20.78 ? 1193 ALA   B CB    1 
ATOM   17901 N  N     . SER   B  1  1196 ? 16.073  62.837  59.902  1.00 20.44 ? 1194 SER   B N     1 
ATOM   17902 C  CA    . SER   B  1  1196 ? 16.531  64.064  59.283  1.00 22.22 ? 1194 SER   B CA    1 
ATOM   17903 C  C     . SER   B  1  1196 ? 15.595  65.208  59.652  1.00 22.60 ? 1194 SER   B C     1 
ATOM   17904 O  O     . SER   B  1  1196 ? 14.478  65.005  60.132  1.00 21.73 ? 1194 SER   B O     1 
ATOM   17905 C  CB    . SER   B  1  1196 ? 16.515  63.910  57.769  1.00 22.53 ? 1194 SER   B CB    1 
ATOM   17906 O  OG    . SER   B  1  1196 ? 15.184  63.723  57.344  1.00 24.35 ? 1194 SER   B OG    1 
ATOM   17907 N  N     . SER   B  1  1197 ? 16.067  66.433  59.415  1.00 23.14 ? 1195 SER   B N     1 
ATOM   17908 C  CA    . SER   B  1  1197 ? 15.211  67.591  59.637  1.00 22.63 ? 1195 SER   B CA    1 
ATOM   17909 C  C     . SER   B  1  1197 ? 13.943  67.499  58.801  1.00 21.64 ? 1195 SER   B C     1 
ATOM   17910 O  O     . SER   B  1  1197 ? 12.851  67.833  59.273  1.00 23.46 ? 1195 SER   B O     1 
ATOM   17911 C  CB    . SER   B  1  1197 ? 15.974  68.874  59.316  1.00 23.49 ? 1195 SER   B CB    1 
ATOM   17912 O  OG    . SER   B  1  1197 ? 17.135  68.982  60.113  1.00 24.49 ? 1195 SER   B OG    1 
ATOM   17913 N  N     . GLY   B  1  1198 ? 14.069  67.044  57.555  1.00 25.44 ? 1196 GLY   B N     1 
ATOM   17914 C  CA    . GLY   B  1  1198 ? 12.891  66.911  56.717  1.00 26.85 ? 1196 GLY   B CA    1 
ATOM   17915 C  C     . GLY   B  1  1198 ? 11.934  65.863  57.242  1.00 29.41 ? 1196 GLY   B C     1 
ATOM   17916 O  O     . GLY   B  1  1198 ? 10.716  66.037  57.187  1.00 27.98 ? 1196 GLY   B O     1 
ATOM   17917 N  N     . GLU   B  1  1199 ? 12.477  64.767  57.776  1.00 23.89 ? 1197 GLU   B N     1 
ATOM   17918 C  CA    . GLU   B  1  1199 ? 11.635  63.719  58.337  1.00 27.40 ? 1197 GLU   B CA    1 
ATOM   17919 C  C     . GLU   B  1  1199 ? 10.879  64.222  59.562  1.00 27.28 ? 1197 GLU   B C     1 
ATOM   17920 O  O     . GLU   B  1  1199 ? 9.700   63.902  59.750  1.00 26.15 ? 1197 GLU   B O     1 
ATOM   17921 C  CB    . GLU   B  1  1199 ? 12.504  62.508  58.671  1.00 27.60 ? 1197 GLU   B CB    1 
ATOM   17922 C  CG    . GLU   B  1  1199 ? 11.753  61.307  59.193  1.00 36.47 ? 1197 GLU   B CG    1 
ATOM   17923 C  CD    . GLU   B  1  1199 ? 12.682  60.147  59.491  1.00 40.67 ? 1197 GLU   B CD    1 
ATOM   17924 O  OE1   . GLU   B  1  1199 ? 13.882  60.231  59.129  1.00 41.51 ? 1197 GLU   B OE1   1 
ATOM   17925 O  OE2   . GLU   B  1  1199 ? 12.219  59.157  60.095  1.00 50.44 ? 1197 GLU   B OE2   1 
ATOM   17926 N  N     . ILE   B  1  1200 ? 11.534  65.026  60.401  1.00 22.37 ? 1198 ILE   B N     1 
ATOM   17927 C  CA    . ILE   B  1  1200 ? 10.855  65.603  61.558  1.00 23.30 ? 1198 ILE   B CA    1 
ATOM   17928 C  C     . ILE   B  1  1200 ? 9.713   66.506  61.115  1.00 26.92 ? 1198 ILE   B C     1 
ATOM   17929 O  O     . ILE   B  1  1200 ? 8.640   66.533  61.735  1.00 26.61 ? 1198 ILE   B O     1 
ATOM   17930 C  CB    . ILE   B  1  1200 ? 11.871  66.352  62.436  1.00 22.08 ? 1198 ILE   B CB    1 
ATOM   17931 C  CG1   . ILE   B  1  1200 ? 12.869  65.363  63.040  1.00 22.11 ? 1198 ILE   B CG1   1 
ATOM   17932 C  CG2   . ILE   B  1  1200 ? 11.159  67.147  63.522  1.00 22.88 ? 1198 ILE   B CG2   1 
ATOM   17933 C  CD1   . ILE   B  1  1200 ? 14.010  66.034  63.777  1.00 22.61 ? 1198 ILE   B CD1   1 
ATOM   17934 N  N     . ALA   B  1  1201 ? 9.925   67.266  60.042  1.00 27.81 ? 1199 ALA   B N     1 
ATOM   17935 C  CA    . ALA   B  1  1201 ? 8.877   68.148  59.552  1.00 30.35 ? 1199 ALA   B CA    1 
ATOM   17936 C  C     . ALA   B  1  1201 ? 7.732   67.360  58.931  1.00 28.99 ? 1199 ALA   B C     1 
ATOM   17937 O  O     . ALA   B  1  1201 ? 6.568   67.742  59.076  1.00 33.27 ? 1199 ALA   B O     1 
ATOM   17938 C  CB    . ALA   B  1  1201 ? 9.459   69.128  58.534  1.00 28.90 ? 1199 ALA   B CB    1 
ATOM   17939 N  N     . ARG   B  1  1202 ? 8.044   66.252  58.250  1.00 29.74 ? 1200 ARG   B N     1 
ATOM   17940 C  CA    . ARG   B  1  1202 ? 7.047   65.525  57.464  1.00 31.80 ? 1200 ARG   B CA    1 
ATOM   17941 C  C     . ARG   B  1  1202 ? 6.265   64.530  58.306  1.00 32.56 ? 1200 ARG   B C     1 
ATOM   17942 O  O     . ARG   B  1  1202 ? 5.070   64.316  58.067  1.00 34.86 ? 1200 ARG   B O     1 
ATOM   17943 C  CB    . ARG   B  1  1202 ? 7.729   64.744  56.342  1.00 32.83 ? 1200 ARG   B CB    1 
ATOM   17944 C  CG    . ARG   B  1  1202 ? 8.316   65.585  55.229  1.00 42.25 ? 1200 ARG   B CG    1 
ATOM   17945 C  CD    . ARG   B  1  1202 ? 8.827   64.713  54.090  1.00 49.18 ? 1200 ARG   B CD    1 
ATOM   17946 N  NE    . ARG   B  1  1202 ? 9.707   63.643  54.547  1.00 48.64 ? 1200 ARG   B NE    1 
ATOM   17947 C  CZ    . ARG   B  1  1202 ? 11.033  63.704  54.534  1.00 46.41 ? 1200 ARG   B CZ    1 
ATOM   17948 N  NH1   . ARG   B  1  1202 ? 11.672  64.785  54.113  1.00 45.38 ? 1200 ARG   B NH1   1 
ATOM   17949 N  NH2   . ARG   B  1  1202 ? 11.734  62.651  54.943  1.00 43.68 ? 1200 ARG   B NH2   1 
ATOM   17950 N  N     . ASN   B  1  1203 ? 6.919   63.905  59.275  1.00 28.20 ? 1201 ASN   B N     1 
ATOM   17951 C  CA    . ASN   B  1  1203 ? 6.397   62.705  59.925  1.00 27.54 ? 1201 ASN   B CA    1 
ATOM   17952 C  C     . ASN   B  1  1203 ? 6.193   62.976  61.402  1.00 27.33 ? 1201 ASN   B C     1 
ATOM   17953 O  O     . ASN   B  1  1203 ? 7.185   63.097  62.148  1.00 25.76 ? 1201 ASN   B O     1 
ATOM   17954 C  CB    . ASN   B  1  1203 ? 7.382   61.553  59.730  1.00 29.37 ? 1201 ASN   B CB    1 
ATOM   17955 C  CG    . ASN   B  1  1203 ? 6.912   60.257  60.367  1.00 29.87 ? 1201 ASN   B CG    1 
ATOM   17956 O  OD1   . ASN   B  1  1203 ? 5.783   60.156  60.849  1.00 34.95 ? 1201 ASN   B OD1   1 
ATOM   17957 N  ND2   . ASN   B  1  1203 ? 7.777   59.252  60.357  1.00 33.05 ? 1201 ASN   B ND2   1 
ATOM   17958 N  N     . PRO   B  1  1204 ? 4.948   63.051  61.878  1.00 28.94 ? 1202 PRO   B N     1 
ATOM   17959 C  CA    . PRO   B  1  1204 ? 4.727   63.246  63.321  1.00 30.53 ? 1202 PRO   B CA    1 
ATOM   17960 C  C     . PRO   B  1  1204 ? 5.318   62.141  64.175  1.00 27.77 ? 1202 PRO   B C     1 
ATOM   17961 O  O     . PRO   B  1  1204 ? 5.537   62.353  65.372  1.00 28.86 ? 1202 PRO   B O     1 
ATOM   17962 C  CB    . PRO   B  1  1204 ? 3.195   63.293  63.444  1.00 37.11 ? 1202 PRO   B CB    1 
ATOM   17963 C  CG    . PRO   B  1  1204 ? 2.702   63.619  62.063  1.00 37.41 ? 1202 PRO   B CG    1 
ATOM   17964 C  CD    . PRO   B  1  1204 ? 3.683   62.989  61.122  1.00 32.26 ? 1202 PRO   B CD    1 
ATOM   17965 N  N     . ASP   B  1  1205 ? 5.584   60.968  63.600  1.00 27.02 ? 1203 ASP   B N     1 
ATOM   17966 C  CA    . ASP   B  1  1205 ? 6.147   59.839  64.328  1.00 28.91 ? 1203 ASP   B CA    1 
ATOM   17967 C  C     . ASP   B  1  1205 ? 7.614   59.597  63.977  1.00 29.92 ? 1203 ASP   B C     1 
ATOM   17968 O  O     . ASP   B  1  1205 ? 8.110   58.474  64.097  1.00 28.84 ? 1203 ASP   B O     1 
ATOM   17969 C  CB    . ASP   B  1  1205 ? 5.318   58.573  64.107  1.00 33.60 ? 1203 ASP   B CB    1 
ATOM   17970 C  CG    . ASP   B  1  1205 ? 3.908   58.684  64.673  1.00 36.90 ? 1203 ASP   B CG    1 
ATOM   17971 O  OD1   . ASP   B  1  1205 ? 3.687   59.497  65.599  1.00 33.35 ? 1203 ASP   B OD1   1 
ATOM   17972 O  OD2   . ASP   B  1  1205 ? 3.015   57.953  64.191  1.00 40.38 ? 1203 ASP   B OD2   1 
ATOM   17973 N  N     . ALA   B  1  1206 ? 8.318   60.647  63.538  1.00 25.51 ? 1204 ALA   B N     1 
ATOM   17974 C  CA    . ALA   B  1  1206 ? 9.741   60.514  63.238  1.00 25.91 ? 1204 ALA   B CA    1 
ATOM   17975 C  C     . ALA   B  1  1206 ? 10.498  59.938  64.425  1.00 22.63 ? 1204 ALA   B C     1 
ATOM   17976 O  O     . ALA   B  1  1206 ? 11.388  59.094  64.263  1.00 26.15 ? 1204 ALA   B O     1 
ATOM   17977 C  CB    . ALA   B  1  1206 ? 10.311  61.875  62.841  1.00 26.92 ? 1204 ALA   B CB    1 
ATOM   17978 N  N     . TYR   B  1  1207 ? 10.156  60.376  65.628  1.00 20.57 ? 1205 TYR   B N     1 
ATOM   17979 C  CA    . TYR   B  1  1207 ? 10.640  59.744  66.844  1.00 21.48 ? 1205 TYR   B CA    1 
ATOM   17980 C  C     . TYR   B  1  1207 ? 9.487   58.978  67.471  1.00 20.82 ? 1205 TYR   B C     1 
ATOM   17981 O  O     . TYR   B  1  1207 ? 8.383   59.516  67.615  1.00 27.95 ? 1205 TYR   B O     1 
ATOM   17982 C  CB    . TYR   B  1  1207 ? 11.185  60.778  67.825  1.00 20.21 ? 1205 TYR   B CB    1 
ATOM   17983 C  CG    . TYR   B  1  1207 ? 12.346  61.550  67.268  1.00 18.77 ? 1205 TYR   B CG    1 
ATOM   17984 C  CD1   . TYR   B  1  1207 ? 13.518  60.907  66.904  1.00 18.98 ? 1205 TYR   B CD1   1 
ATOM   17985 C  CD2   . TYR   B  1  1207 ? 12.278  62.925  67.121  1.00 18.87 ? 1205 TYR   B CD2   1 
ATOM   17986 C  CE1   . TYR   B  1  1207 ? 14.595  61.611  66.402  1.00 16.98 ? 1205 TYR   B CE1   1 
ATOM   17987 C  CE2   . TYR   B  1  1207 ? 13.348  63.645  66.608  1.00 19.13 ? 1205 TYR   B CE2   1 
ATOM   17988 C  CZ    . TYR   B  1  1207 ? 14.503  62.976  66.258  1.00 18.10 ? 1205 TYR   B CZ    1 
ATOM   17989 O  OH    . TYR   B  1  1207 ? 15.567  63.690  65.754  1.00 18.85 ? 1205 TYR   B OH    1 
ATOM   17990 N  N     . CYS   B  1  1208 ? 9.740   57.730  67.826  1.00 16.66 ? 1206 CYS   B N     1 
ATOM   17991 C  CA    . CYS   B  1  1208 ? 8.709   56.846  68.344  1.00 16.00 ? 1206 CYS   B CA    1 
ATOM   17992 C  C     . CYS   B  1  1208 ? 8.723   56.910  69.864  1.00 16.72 ? 1206 CYS   B C     1 
ATOM   17993 O  O     . CYS   B  1  1208 ? 9.749   56.639  70.490  1.00 16.72 ? 1206 CYS   B O     1 
ATOM   17994 C  CB    . CYS   B  1  1208 ? 8.999   55.423  67.879  1.00 19.74 ? 1206 CYS   B CB    1 
ATOM   17995 S  SG    . CYS   B  1  1208 ? 7.769   54.241  68.421  1.00 22.48 ? 1206 CYS   B SG    1 
ATOM   17996 N  N     . LEU   B  1  1209 ? 7.575   57.245  70.453  1.00 16.12 ? 1207 LEU   B N     1 
ATOM   17997 C  CA    . LEU   B  1  1209 ? 7.491   57.328  71.907  1.00 15.30 ? 1207 LEU   B CA    1 
ATOM   17998 C  C     . LEU   B  1  1209 ? 7.545   55.963  72.576  1.00 15.03 ? 1207 LEU   B C     1 
ATOM   17999 O  O     . LEU   B  1  1209 ? 7.776   55.907  73.782  1.00 15.41 ? 1207 LEU   B O     1 
ATOM   18000 C  CB    . LEU   B  1  1209 ? 6.232   58.084  72.311  1.00 14.69 ? 1207 LEU   B CB    1 
ATOM   18001 C  CG    . LEU   B  1  1209 ? 6.073   59.468  71.702  1.00 18.42 ? 1207 LEU   B CG    1 
ATOM   18002 C  CD1   . LEU   B  1  1209 ? 4.868   60.158  72.332  1.00 19.11 ? 1207 LEU   B CD1   1 
ATOM   18003 C  CD2   . LEU   B  1  1209 ? 7.318   60.304  71.878  1.00 19.45 ? 1207 LEU   B CD2   1 
ATOM   18004 N  N     . ASN   B  1  1210 ? 7.368   54.871  71.822  1.00 15.70 ? 1208 ASN   B N     1 
ATOM   18005 C  CA    . ASN   B  1  1210 ? 7.427   53.547  72.427  1.00 17.52 ? 1208 ASN   B CA    1 
ATOM   18006 C  C     . ASN   B  1  1210 ? 8.788   53.308  73.052  1.00 16.99 ? 1208 ASN   B C     1 
ATOM   18007 O  O     . ASN   B  1  1210 ? 8.893   52.591  74.052  1.00 19.12 ? 1208 ASN   B O     1 
ATOM   18008 C  CB    . ASN   B  1  1210 ? 7.169   52.446  71.384  1.00 21.81 ? 1208 ASN   B CB    1 
ATOM   18009 C  CG    . ASN   B  1  1210 ? 5.765   52.506  70.767  1.00 20.91 ? 1208 ASN   B CG    1 
ATOM   18010 O  OD1   . ASN   B  1  1210 ? 5.015   53.452  70.983  1.00 26.69 ? 1208 ASN   B OD1   1 
ATOM   18011 N  ND2   . ASN   B  1  1210 ? 5.437   51.504  69.951  1.00 28.89 ? 1208 ASN   B ND2   1 
ATOM   18012 N  N     . TRP   B  1  1211 ? 9.840   53.895  72.477  1.00 16.25 ? 1209 TRP   B N     1 
ATOM   18013 C  CA    . TRP   B  1  1211 ? 11.198  53.609  72.922  1.00 16.14 ? 1209 TRP   B CA    1 
ATOM   18014 C  C     . TRP   B  1  1211 ? 11.684  54.582  73.974  1.00 17.75 ? 1209 TRP   B C     1 
ATOM   18015 O  O     . TRP   B  1  1211 ? 12.802  54.427  74.477  1.00 19.03 ? 1209 TRP   B O     1 
ATOM   18016 C  CB    . TRP   B  1  1211 ? 12.167  53.580  71.726  1.00 18.07 ? 1209 TRP   B CB    1 
ATOM   18017 C  CG    . TRP   B  1  1211 ? 11.568  52.914  70.531  1.00 18.06 ? 1209 TRP   B CG    1 
ATOM   18018 C  CD1   . TRP   B  1  1211 ? 11.508  53.415  69.269  1.00 19.81 ? 1209 TRP   B CD1   1 
ATOM   18019 C  CD2   . TRP   B  1  1211 ? 10.903  51.645  70.490  1.00 17.44 ? 1209 TRP   B CD2   1 
ATOM   18020 N  NE1   . TRP   B  1  1211 ? 10.855  52.536  68.438  1.00 20.72 ? 1209 TRP   B NE1   1 
ATOM   18021 C  CE2   . TRP   B  1  1211 ? 10.485  51.436  69.163  1.00 17.77 ? 1209 TRP   B CE2   1 
ATOM   18022 C  CE3   . TRP   B  1  1211 ? 10.638  50.651  71.445  1.00 18.64 ? 1209 TRP   B CE3   1 
ATOM   18023 C  CZ2   . TRP   B  1  1211 ? 9.791   50.296  68.764  1.00 20.27 ? 1209 TRP   B CZ2   1 
ATOM   18024 C  CZ3   . TRP   B  1  1211 ? 9.949   49.515  71.039  1.00 18.37 ? 1209 TRP   B CZ3   1 
ATOM   18025 C  CH2   . TRP   B  1  1211 ? 9.529   49.352  69.715  1.00 19.58 ? 1209 TRP   B CH2   1 
ATOM   18026 N  N     . LEU   B  1  1212 ? 10.869  55.567  74.324  1.00 15.76 ? 1210 LEU   B N     1 
ATOM   18027 C  CA    . LEU   B  1  1212 ? 11.245  56.596  75.267  1.00 14.25 ? 1210 LEU   B CA    1 
ATOM   18028 C  C     . LEU   B  1  1212 ? 10.629  56.374  76.631  1.00 14.73 ? 1210 LEU   B C     1 
ATOM   18029 O  O     . LEU   B  1  1212 ? 10.793  57.210  77.517  1.00 15.07 ? 1210 LEU   B O     1 
ATOM   18030 C  CB    . LEU   B  1  1212 ? 10.860  57.962  74.713  1.00 13.96 ? 1210 LEU   B CB    1 
ATOM   18031 C  CG    . LEU   B  1  1212 ? 11.769  58.403  73.568  1.00 13.39 ? 1210 LEU   B CG    1 
ATOM   18032 C  CD1   . LEU   B  1  1212 ? 11.141  59.543  72.819  1.00 17.78 ? 1210 LEU   B CD1   1 
ATOM   18033 C  CD2   . LEU   B  1  1212 ? 13.137  58.808  74.126  1.00 16.46 ? 1210 LEU   B CD2   1 
ATOM   18034 N  N     . VAL   B  1  1213 ? 9.933   55.259  76.808  1.00 14.65 ? 1211 VAL   B N     1 
ATOM   18035 C  CA    . VAL   B  1  1213 ? 9.468   54.828  78.113  1.00 15.17 ? 1211 VAL   B CA    1 
ATOM   18036 C  C     . VAL   B  1  1213 ? 10.194  53.546  78.468  1.00 13.97 ? 1211 VAL   B C     1 
ATOM   18037 O  O     . VAL   B  1  1213 ? 10.731  52.838  77.606  1.00 15.52 ? 1211 VAL   B O     1 
ATOM   18038 C  CB    . VAL   B  1  1213 ? 7.941   54.635  78.139  1.00 15.20 ? 1211 VAL   B CB    1 
ATOM   18039 C  CG1   . VAL   B  1  1213 ? 7.257   55.993  78.012  1.00 16.96 ? 1211 VAL   B CG1   1 
ATOM   18040 C  CG2   . VAL   B  1  1213 ? 7.510   53.679  77.036  1.00 16.33 ? 1211 VAL   B CG2   1 
ATOM   18041 N  N     . GLU   B  1  1214 ? 10.253  53.271  79.766  1.00 14.38 ? 1212 GLU   B N     1 
ATOM   18042 C  CA    . GLU   B  1  1214 ? 10.818  52.033  80.277  1.00 16.64 ? 1212 GLU   B CA    1 
ATOM   18043 C  C     . GLU   B  1  1214 ? 9.685   51.156  80.793  1.00 14.19 ? 1212 GLU   B C     1 
ATOM   18044 O  O     . GLU   B  1  1214 ? 8.859   51.602  81.582  1.00 14.98 ? 1212 GLU   B O     1 
ATOM   18045 C  CB    . GLU   B  1  1214 ? 11.810  52.303  81.414  1.00 18.72 ? 1212 GLU   B CB    1 
ATOM   18046 C  CG    . GLU   B  1  1214 ? 12.435  51.002  81.943  1.00 21.11 ? 1212 GLU   B CG    1 
ATOM   18047 C  CD    . GLU   B  1  1214 ? 13.306  51.157  83.178  1.00 26.74 ? 1212 GLU   B CD    1 
ATOM   18048 O  OE1   . GLU   B  1  1214 ? 13.814  52.264  83.433  1.00 27.51 ? 1212 GLU   B OE1   1 
ATOM   18049 O  OE2   . GLU   B  1  1214 ? 13.480  50.146  83.901  1.00 30.45 ? 1212 GLU   B OE2   1 
ATOM   18050 N  N     . GLU   B  1  1215 ? 9.668   49.915  80.349  1.00 13.73 ? 1213 GLU   B N     1 
ATOM   18051 C  CA    . GLU   B  1  1215 ? 8.718   48.947  80.857  1.00 14.05 ? 1213 GLU   B CA    1 
ATOM   18052 C  C     . GLU   B  1  1215 ? 9.218   48.359  82.164  1.00 13.48 ? 1213 GLU   B C     1 
ATOM   18053 O  O     . GLU   B  1  1215 ? 10.398  48.005  82.300  1.00 14.27 ? 1213 GLU   B O     1 
ATOM   18054 C  CB    . GLU   B  1  1215 ? 8.618   47.803  79.864  1.00 14.75 ? 1213 GLU   B CB    1 
ATOM   18055 C  CG    . GLU   B  1  1215 ? 8.138   48.188  78.474  1.00 15.49 ? 1213 GLU   B CG    1 
ATOM   18056 C  CD    . GLU   B  1  1215 ? 8.355   47.071  77.508  1.00 14.99 ? 1213 GLU   B CD    1 
ATOM   18057 O  OE1   . GLU   B  1  1215 ? 9.481   46.957  76.988  1.00 15.59 ? 1213 GLU   B OE1   1 
ATOM   18058 O  OE2   . GLU   B  1  1215 ? 7.397   46.322  77.255  1.00 15.85 ? 1213 GLU   B OE2   1 
ATOM   18059 N  N     . VAL   B  1  1216 ? 8.308   48.213  83.114  1.00 13.70 ? 1214 VAL   B N     1 
ATOM   18060 C  CA    . VAL   B  1  1216 ? 8.608   47.526  84.361  1.00 14.32 ? 1214 VAL   B CA    1 
ATOM   18061 C  C     . VAL   B  1  1216 ? 7.530   46.495  84.601  1.00 13.61 ? 1214 VAL   B C     1 
ATOM   18062 O  O     . VAL   B  1  1216 ? 6.330   46.806  84.539  1.00 14.94 ? 1214 VAL   B O     1 
ATOM   18063 C  CB    . VAL   B  1  1216 ? 8.734   48.476  85.563  1.00 14.81 ? 1214 VAL   B CB    1 
ATOM   18064 C  CG1   . VAL   B  1  1216 ? 8.946   47.670  86.850  1.00 17.34 ? 1214 VAL   B CG1   1 
ATOM   18065 C  CG2   . VAL   B  1  1216 ? 9.873   49.456  85.328  1.00 16.10 ? 1214 VAL   B CG2   1 
ATOM   18066 N  N     . SER   B  1  1217 ? 7.955   45.261  84.835  1.00 12.62 ? 1215 SER   B N     1 
ATOM   18067 C  CA    . SER   B  1  1217 ? 7.069   44.168  85.189  1.00 13.25 ? 1215 SER   B CA    1 
ATOM   18068 C  C     . SER   B  1  1217 ? 7.247   43.884  86.665  1.00 13.84 ? 1215 SER   B C     1 
ATOM   18069 O  O     . SER   B  1  1217 ? 8.375   43.864  87.159  1.00 14.40 ? 1215 SER   B O     1 
ATOM   18070 C  CB    . SER   B  1  1217 ? 7.486   42.922  84.408  1.00 15.36 ? 1215 SER   B CB    1 
ATOM   18071 O  OG    . SER   B  1  1217 ? 6.980   41.719  84.980  1.00 16.98 ? 1215 SER   B OG    1 
ATOM   18072 N  N     . ALA   B  1  1218 ? 6.143   43.661  87.366  1.00 13.34 ? 1216 ALA   B N     1 
ATOM   18073 C  CA    . ALA   B  1  1218 ? 6.204   43.286  88.772  1.00 13.71 ? 1216 ALA   B CA    1 
ATOM   18074 C  C     . ALA   B  1  1218 ? 5.278   42.109  88.992  1.00 14.34 ? 1216 ALA   B C     1 
ATOM   18075 O  O     . ALA   B  1  1218 ? 4.106   42.158  88.614  1.00 16.18 ? 1216 ALA   B O     1 
ATOM   18076 C  CB    . ALA   B  1  1218 ? 5.813   44.448  89.685  1.00 16.12 ? 1216 ALA   B CB    1 
ATOM   18077 N  N     . SER   B  1  1219 ? 5.801   41.045  89.582  1.00 13.46 ? 1217 SER   B N     1 
ATOM   18078 C  CA    . SER   B  1  1219 ? 5.027   39.851  89.859  1.00 13.49 ? 1217 SER   B CA    1 
ATOM   18079 C  C     . SER   B  1  1219 ? 4.954   39.683  91.363  1.00 13.30 ? 1217 SER   B C     1 
ATOM   18080 O  O     . SER   B  1  1219 ? 5.985   39.520  92.019  1.00 13.86 ? 1217 SER   B O     1 
ATOM   18081 C  CB    . SER   B  1  1219 ? 5.682   38.635  89.217  1.00 14.96 ? 1217 SER   B CB    1 
ATOM   18082 O  OG    . SER   B  1  1219 ? 4.906   37.479  89.478  1.00 15.57 ? 1217 SER   B OG    1 
ATOM   18083 N  N     . ILE   B  1  1220 ? 3.746   39.738  91.896  1.00 15.01 ? 1218 ILE   B N     1 
ATOM   18084 C  CA    . ILE   B  1  1220 ? 3.519   39.673  93.330  1.00 14.13 ? 1218 ILE   B CA    1 
ATOM   18085 C  C     . ILE   B  1  1220 ? 2.827   38.358  93.632  1.00 15.55 ? 1218 ILE   B C     1 
ATOM   18086 O  O     . ILE   B  1  1220 ? 1.746   38.085  93.106  1.00 15.64 ? 1218 ILE   B O     1 
ATOM   18087 C  CB    . ILE   B  1  1220 ? 2.644   40.845  93.775  1.00 15.94 ? 1218 ILE   B CB    1 
ATOM   18088 C  CG1   . ILE   B  1  1220 ? 3.284   42.160  93.332  1.00 19.71 ? 1218 ILE   B CG1   1 
ATOM   18089 C  CG2   . ILE   B  1  1220 ? 2.386   40.767  95.279  1.00 18.27 ? 1218 ILE   B CG2   1 
ATOM   18090 C  CD1   . ILE   B  1  1220 ? 2.333   43.323  93.351  1.00 29.31 ? 1218 ILE   B CD1   1 
ATOM   18091 N  N     . ASN   B  1  1221 ? 3.433   37.554  94.493  1.00 15.73 ? 1219 ASN   B N     1 
ATOM   18092 C  CA    . ASN   B  1  1221 ? 2.796   36.332  94.968  1.00 15.68 ? 1219 ASN   B CA    1 
ATOM   18093 C  C     . ASN   B  1  1221 ? 1.776   36.712  96.033  1.00 16.29 ? 1219 ASN   B C     1 
ATOM   18094 O  O     . ASN   B  1  1221 ? 2.146   37.064  97.157  1.00 17.65 ? 1219 ASN   B O     1 
ATOM   18095 C  CB    . ASN   B  1  1221 ? 3.869   35.432  95.561  1.00 15.97 ? 1219 ASN   B CB    1 
ATOM   18096 C  CG    . ASN   B  1  1221 ? 3.298   34.193  96.215  1.00 16.48 ? 1219 ASN   B CG    1 
ATOM   18097 O  OD1   . ASN   B  1  1221 ? 2.110   33.910  96.099  1.00 17.10 ? 1219 ASN   B OD1   1 
ATOM   18098 N  ND2   . ASN   B  1  1221 ? 4.153   33.442  96.907  1.00 19.07 ? 1219 ASN   B ND2   1 
ATOM   18099 N  N     . THR   B  1  1222 ? 0.494   36.648  95.704  1.00 14.78 ? 1220 THR   B N     1 
ATOM   18100 C  CA    . THR   B  1  1222 ? -0.551  37.041  96.641  1.00 17.37 ? 1220 THR   B CA    1 
ATOM   18101 C  C     . THR   B  1  1222 ? -1.069  35.868  97.449  1.00 21.09 ? 1220 THR   B C     1 
ATOM   18102 O  O     . THR   B  1  1222 ? -2.019  36.032  98.223  1.00 25.28 ? 1220 THR   B O     1 
ATOM   18103 C  CB    . THR   B  1  1222 ? -1.699  37.720  95.913  1.00 18.41 ? 1220 THR   B CB    1 
ATOM   18104 O  OG1   . THR   B  1  1222 ? -2.209  36.823  94.921  1.00 20.44 ? 1220 THR   B OG1   1 
ATOM   18105 C  CG2   . THR   B  1  1222 ? -1.225  39.005  95.233  1.00 20.09 ? 1220 THR   B CG2   1 
ATOM   18106 N  N     . ALA   B  1  1223 ? -0.465  34.697  97.299  1.00 18.73 ? 1221 ALA   B N     1 
ATOM   18107 C  CA    . ALA   B  1  1223 ? -0.720  33.567  98.172  1.00 22.98 ? 1221 ALA   B CA    1 
ATOM   18108 C  C     . ALA   B  1  1223 ? 0.331   33.433  99.268  1.00 29.52 ? 1221 ALA   B C     1 
ATOM   18109 O  O     . ALA   B  1  1223 ? 0.282   32.468  100.035 1.00 33.67 ? 1221 ALA   B O     1 
ATOM   18110 C  CB    . ALA   B  1  1223 ? -0.766  32.274  97.352  1.00 24.89 ? 1221 ALA   B CB    1 
ATOM   18111 N  N     . ALA   B  1  1224 ? 1.274   34.380  99.364  0.64 21.05 ? 1222 ALA   B N     1 
ATOM   18112 C  CA    . ALA   B  1  1224 ? 2.426   34.208  100.242 0.64 25.58 ? 1222 ALA   B CA    1 
ATOM   18113 C  C     . ALA   B  1  1224 ? 2.044   34.145  101.713 0.64 25.02 ? 1222 ALA   B C     1 
ATOM   18114 O  O     . ALA   B  1  1224 ? 2.812   33.601  102.512 0.64 26.86 ? 1222 ALA   B O     1 
ATOM   18115 C  CB    . ALA   B  1  1224 ? 3.442   35.327  100.016 0.64 24.82 ? 1222 ALA   B CB    1 
ATOM   18116 N  N     . ALA   B  1  1225 ? 0.883   34.686  102.095 0.64 25.76 ? 1223 ALA   B N     1 
ATOM   18117 C  CA    . ALA   B  1  1225 ? 0.473   34.640  103.493 0.64 26.73 ? 1223 ALA   B CA    1 
ATOM   18118 C  C     . ALA   B  1  1225 ? -0.106  33.292  103.896 0.64 29.95 ? 1223 ALA   B C     1 
ATOM   18119 O  O     . ALA   B  1  1225 ? -0.396  33.091  105.079 0.64 30.84 ? 1223 ALA   B O     1 
ATOM   18120 C  CB    . ALA   B  1  1225 ? -0.530  35.756  103.806 0.64 33.16 ? 1223 ALA   B CB    1 
ATOM   18121 N  N     . GLY   B  1  1226 ? -0.279  32.370  102.954 0.64 25.94 ? 1224 GLY   B N     1 
ATOM   18122 C  CA    . GLY   B  1  1226 ? -0.780  31.040  103.257 0.64 27.84 ? 1224 GLY   B CA    1 
ATOM   18123 C  C     . GLY   B  1  1226 ? -2.097  30.695  102.599 0.64 31.28 ? 1224 GLY   B C     1 
ATOM   18124 O  O     . GLY   B  1  1226 ? -2.576  29.566  102.779 0.64 31.35 ? 1224 GLY   B O     1 
ATOM   18125 N  N     . GLY   B  1  1227 ? -2.710  31.612  101.855 0.64 25.35 ? 1225 GLY   B N     1 
ATOM   18126 C  CA    . GLY   B  1  1227 ? -3.921  31.317  101.110 0.64 28.14 ? 1225 GLY   B CA    1 
ATOM   18127 C  C     . GLY   B  1  1227 ? -4.174  32.402  100.086 0.64 30.44 ? 1225 GLY   B C     1 
ATOM   18128 O  O     . GLY   B  1  1227 ? -3.427  33.378  99.985  0.64 27.95 ? 1225 GLY   B O     1 
ATOM   18129 N  N     . ASN   B  1  1228 ? -5.260  32.226  99.335  0.64 26.50 ? 1226 ASN   B N     1 
ATOM   18130 C  CA    . ASN   B  1  1228 ? -5.657  33.145  98.273  0.64 27.74 ? 1226 ASN   B CA    1 
ATOM   18131 C  C     . ASN   B  1  1228 ? -6.953  33.842  98.671  0.64 30.21 ? 1226 ASN   B C     1 
ATOM   18132 O  O     . ASN   B  1  1228 ? -7.997  33.192  98.801  0.64 34.64 ? 1226 ASN   B O     1 
ATOM   18133 C  CB    . ASN   B  1  1228 ? -5.848  32.377  96.965  0.64 27.56 ? 1226 ASN   B CB    1 
ATOM   18134 C  CG    . ASN   B  1  1228 ? -6.037  33.288  95.759  0.64 28.36 ? 1226 ASN   B CG    1 
ATOM   18135 O  OD1   . ASN   B  1  1228 ? -6.617  34.370  95.854  0.64 32.56 ? 1226 ASN   B OD1   1 
ATOM   18136 N  ND2   . ASN   B  1  1228 ? -5.554  32.841  94.611  0.64 23.39 ? 1226 ASN   B ND2   1 
ATOM   18137 N  N     . ALA   B  1  1229 ? -6.887  35.167  98.835  0.64 30.56 ? 1227 ALA   B N     1 
ATOM   18138 C  CA    . ALA   B  1  1229 ? -8.070  35.944  99.202  0.64 32.58 ? 1227 ALA   B CA    1 
ATOM   18139 C  C     . ALA   B  1  1229 ? -9.147  35.860  98.128  0.64 31.14 ? 1227 ALA   B C     1 
ATOM   18140 O  O     . ALA   B  1  1229 ? -10.323 35.622  98.428  0.64 28.51 ? 1227 ALA   B O     1 
ATOM   18141 C  CB    . ALA   B  1  1229 ? -7.677  37.402  99.424  0.64 30.76 ? 1227 ALA   B CB    1 
ATOM   18142 N  N     . SER   B  1  1230 ? -8.764  36.070  96.867  0.64 34.69 ? 1228 SER   B N     1 
ATOM   18143 C  CA    . SER   B  1  1230 ? -9.754  36.165  95.799  0.64 32.04 ? 1228 SER   B CA    1 
ATOM   18144 C  C     . SER   B  1  1230 ? -10.493 34.845  95.610  0.64 36.70 ? 1228 SER   B C     1 
ATOM   18145 O  O     . SER   B  1  1230 ? -11.694 34.834  95.315  0.64 39.11 ? 1228 SER   B O     1 
ATOM   18146 C  CB    . SER   B  1  1230 ? -9.090  36.625  94.503  0.64 36.07 ? 1228 SER   B CB    1 
ATOM   18147 N  N     . LEU   B  1  1231 ? -9.800  33.719  95.784  0.64 31.84 ? 1229 LEU   B N     1 
ATOM   18148 C  CA    . LEU   B  1  1231 ? -10.447 32.422  95.619  0.64 34.36 ? 1229 LEU   B CA    1 
ATOM   18149 C  C     . LEU   B  1  1231 ? -11.300 32.017  96.817  0.64 36.86 ? 1229 LEU   B C     1 
ATOM   18150 O  O     . LEU   B  1  1231 ? -12.053 31.039  96.719  0.64 35.88 ? 1229 LEU   B O     1 
ATOM   18151 C  CB    . LEU   B  1  1231 ? -9.419  31.335  95.300  0.64 35.86 ? 1229 LEU   B CB    1 
ATOM   18152 C  CG    . LEU   B  1  1231 ? -8.828  31.176  93.894  0.64 28.31 ? 1229 LEU   B CG    1 
ATOM   18153 C  CD1   . LEU   B  1  1231 ? -8.078  29.857  93.812  0.64 24.35 ? 1229 LEU   B CD1   1 
ATOM   18154 C  CD2   . LEU   B  1  1231 ? -9.882  31.244  92.808  0.64 32.31 ? 1229 LEU   B CD2   1 
ATOM   18155 N  N     . MET   B  1  1232 ? -11.211 32.738  97.939  0.64 34.68 ? 1230 MET   B N     1 
ATOM   18156 C  CA    . MET   B  1  1232 ? -12.128 32.488  99.048  0.64 32.34 ? 1230 MET   B CA    1 
ATOM   18157 C  C     . MET   B  1  1232 ? -13.576 32.736  98.639  0.64 37.21 ? 1230 MET   B C     1 
ATOM   18158 O  O     . MET   B  1  1232 ? -14.488 32.050  99.121  0.64 32.83 ? 1230 MET   B O     1 
ATOM   18159 C  CB    . MET   B  1  1232 ? -11.751 33.359  100.245 0.64 31.32 ? 1230 MET   B CB    1 
ATOM   18160 N  N     . ALA   B  1  1233 ? -13.806 33.702  97.749  0.64 40.89 ? 1231 ALA   B N     1 
ATOM   18161 C  CA    . ALA   B  1  1233 ? -15.139 33.989  97.231  0.64 43.95 ? 1231 ALA   B CA    1 
ATOM   18162 C  C     . ALA   B  1  1233 ? -15.555 33.049  96.108  0.64 42.19 ? 1231 ALA   B C     1 
ATOM   18163 O  O     . ALA   B  1  1233 ? -16.683 33.160  95.612  0.64 44.64 ? 1231 ALA   B O     1 
ATOM   18164 C  CB    . ALA   B  1  1233 ? -15.214 35.439  96.743  0.64 43.68 ? 1231 ALA   B CB    1 
ATOM   18165 N  N     . ILE   B  1  1234 ? -14.685 32.131  95.700  0.64 37.51 ? 1232 ILE   B N     1 
ATOM   18166 C  CA    . ILE   B  1  1234 ? -14.942 31.246  94.572  0.64 39.84 ? 1232 ILE   B CA    1 
ATOM   18167 C  C     . ILE   B  1  1234 ? -15.308 29.875  95.128  0.64 37.62 ? 1232 ILE   B C     1 
ATOM   18168 O  O     . ILE   B  1  1234 ? -14.445 29.110  95.568  0.64 33.02 ? 1232 ILE   B O     1 
ATOM   18169 C  CB    . ILE   B  1  1234 ? -13.755 31.196  93.607  0.64 36.22 ? 1232 ILE   B CB    1 
ATOM   18170 C  CG1   . ILE   B  1  1234 ? -13.581 32.561  92.938  0.64 38.60 ? 1232 ILE   B CG1   1 
ATOM   18171 C  CG2   . ILE   B  1  1234 ? -13.957 30.112  92.568  0.64 30.68 ? 1232 ILE   B CG2   1 
ATOM   18172 C  CD1   . ILE   B  1  1234 ? -12.943 32.515  91.571  0.64 34.79 ? 1232 ILE   B CD1   1 
ATOM   18173 N  N     . GLY   B  1  1235 ? -16.601 29.576  95.120  0.64 36.67 ? 1233 GLY   B N     1 
ATOM   18174 C  CA    . GLY   B  1  1235 ? -17.100 28.261  95.459  0.64 32.72 ? 1233 GLY   B CA    1 
ATOM   18175 C  C     . GLY   B  1  1235 ? -17.979 27.769  94.328  0.64 29.96 ? 1233 GLY   B C     1 
ATOM   18176 O  O     . GLY   B  1  1235 ? -18.727 28.535  93.721  0.64 41.43 ? 1233 GLY   B O     1 
ATOM   18177 O  OXT   . GLY   B  1  1235 ? -17.974 26.604  93.971  0.64 19.73 ? 1233 GLY   B OXT   1 
HETATM 18178 P  PA    A FAD   C  2  .    ? -37.868 43.274  82.671  0.59 18.33 ? 2001 FAD   A PA    1 
HETATM 18179 P  PA    B FAD   C  2  .    ? -37.886 43.303  82.295  0.41 21.63 ? 2001 FAD   A PA    1 
HETATM 18180 O  O1A   A FAD   C  2  .    ? -36.451 42.697  82.424  0.59 23.34 ? 2001 FAD   A O1A   1 
HETATM 18181 O  O1A   B FAD   C  2  .    ? -36.412 42.843  82.162  0.41 21.06 ? 2001 FAD   A O1A   1 
HETATM 18182 O  O2A   A FAD   C  2  .    ? -38.955 42.355  82.980  0.59 23.35 ? 2001 FAD   A O2A   1 
HETATM 18183 O  O2A   B FAD   C  2  .    ? -38.875 42.344  82.750  0.41 23.16 ? 2001 FAD   A O2A   1 
HETATM 18184 O  O5B   A FAD   C  2  .    ? -37.952 44.297  83.724  0.59 18.28 ? 2001 FAD   A O5B   1 
HETATM 18185 O  O5B   B FAD   C  2  .    ? -38.103 44.388  83.287  0.41 19.62 ? 2001 FAD   A O5B   1 
HETATM 18186 C  C5B   A FAD   C  2  .    ? -36.914 45.258  83.847  0.59 19.70 ? 2001 FAD   A C5B   1 
HETATM 18187 C  C5B   B FAD   C  2  .    ? -37.030 45.232  83.718  0.41 19.85 ? 2001 FAD   A C5B   1 
HETATM 18188 C  C4B   A FAD   C  2  .    ? -37.422 46.348  84.775  0.59 19.59 ? 2001 FAD   A C4B   1 
HETATM 18189 C  C4B   B FAD   C  2  .    ? -37.506 46.289  84.724  0.41 19.57 ? 2001 FAD   A C4B   1 
HETATM 18190 O  O4B   A FAD   C  2  .    ? -37.459 45.900  86.096  0.59 19.32 ? 2001 FAD   A O4B   1 
HETATM 18191 O  O4B   B FAD   C  2  .    ? -37.449 45.849  86.047  0.41 19.39 ? 2001 FAD   A O4B   1 
HETATM 18192 C  C3B   A FAD   C  2  .    ? -36.601 47.595  84.832  0.59 19.41 ? 2001 FAD   A C3B   1 
HETATM 18193 C  C3B   B FAD   C  2  .    ? -36.709 47.555  84.736  0.41 19.78 ? 2001 FAD   A C3B   1 
HETATM 18194 O  O3B   A FAD   C  2  .    ? -36.736 48.420  83.721  0.59 19.58 ? 2001 FAD   A O3B   1 
HETATM 18195 O  O3B   B FAD   C  2  .    ? -36.993 48.400  83.677  0.41 19.72 ? 2001 FAD   A O3B   1 
HETATM 18196 C  C2B   A FAD   C  2  .    ? -37.141 48.208  86.065  0.59 19.63 ? 2001 FAD   A C2B   1 
HETATM 18197 C  C2B   B FAD   C  2  .    ? -37.069 48.168  86.040  0.41 19.56 ? 2001 FAD   A C2B   1 
HETATM 18198 O  O2B   A FAD   C  2  .    ? -38.390 48.772  85.869  0.59 17.54 ? 2001 FAD   A O2B   1 
HETATM 18199 O  O2B   B FAD   C  2  .    ? -38.217 48.937  85.993  0.41 18.56 ? 2001 FAD   A O2B   1 
HETATM 18200 C  C1B   A FAD   C  2  .    ? -37.308 47.010  86.927  0.59 18.13 ? 2001 FAD   A C1B   1 
HETATM 18201 C  C1B   B FAD   C  2  .    ? -37.300 46.965  86.882  0.41 18.15 ? 2001 FAD   A C1B   1 
HETATM 18202 N  N9A   A FAD   C  2  .    ? -36.211 46.739  87.818  0.59 20.12 ? 2001 FAD   A N9A   1 
HETATM 18203 N  N9A   B FAD   C  2  .    ? -36.224 46.696  87.800  0.41 20.14 ? 2001 FAD   A N9A   1 
HETATM 18204 C  C8A   A FAD   C  2  .    ? -34.916 46.375  87.490  0.59 22.15 ? 2001 FAD   A C8A   1 
HETATM 18205 C  C8A   B FAD   C  2  .    ? -34.934 46.313  87.478  0.41 22.13 ? 2001 FAD   A C8A   1 
HETATM 18206 N  N7A   A FAD   C  2  .    ? -34.211 46.197  88.613  0.59 21.03 ? 2001 FAD   A N7A   1 
HETATM 18207 N  N7A   B FAD   C  2  .    ? -34.227 46.147  88.601  0.41 21.05 ? 2001 FAD   A N7A   1 
HETATM 18208 C  C5A   A FAD   C  2  .    ? -35.022 46.431  89.715  0.59 21.10 ? 2001 FAD   A C5A   1 
HETATM 18209 C  C5A   B FAD   C  2  .    ? -35.029 46.414  89.702  0.41 21.12 ? 2001 FAD   A C5A   1 
HETATM 18210 C  C6A   A FAD   C  2  .    ? -34.850 46.395  91.090  0.59 21.77 ? 2001 FAD   A C6A   1 
HETATM 18211 C  C6A   B FAD   C  2  .    ? -34.840 46.401  91.077  0.41 21.75 ? 2001 FAD   A C6A   1 
HETATM 18212 N  N6A   A FAD   C  2  .    ? -33.586 46.048  91.686  0.59 22.52 ? 2001 FAD   A N6A   1 
HETATM 18213 N  N6A   B FAD   C  2  .    ? -33.567 46.047  91.651  0.41 22.53 ? 2001 FAD   A N6A   1 
HETATM 18214 N  N1A   A FAD   C  2  .    ? -35.884 46.686  91.893  0.59 19.84 ? 2001 FAD   A N1A   1 
HETATM 18215 N  N1A   B FAD   C  2  .    ? -35.859 46.720  91.891  0.41 19.86 ? 2001 FAD   A N1A   1 
HETATM 18216 C  C2A   A FAD   C  2  .    ? -37.105 47.010  91.400  0.59 20.62 ? 2001 FAD   A C2A   1 
HETATM 18217 C  C2A   B FAD   C  2  .    ? -37.081 47.053  91.403  0.41 20.61 ? 2001 FAD   A C2A   1 
HETATM 18218 N  N3A   A FAD   C  2  .    ? -37.308 47.050  90.059  0.59 20.74 ? 2001 FAD   A N3A   1 
HETATM 18219 N  N3A   B FAD   C  2  .    ? -37.298 47.072  90.063  0.41 20.73 ? 2001 FAD   A N3A   1 
HETATM 18220 C  C4A   A FAD   C  2  .    ? -36.303 46.775  89.215  0.59 20.44 ? 2001 FAD   A C4A   1 
HETATM 18221 C  C4A   B FAD   C  2  .    ? -36.310 46.767  89.205  0.41 20.44 ? 2001 FAD   A C4A   1 
HETATM 18222 N  N1    A FAD   C  2  .    ? -41.080 53.370  81.532  0.59 14.83 ? 2001 FAD   A N1    1 
HETATM 18223 N  N1    B FAD   C  2  .    ? -40.645 53.512  81.102  0.41 17.56 ? 2001 FAD   A N1    1 
HETATM 18224 C  C2    A FAD   C  2  .    ? -41.320 54.631  82.125  0.59 15.92 ? 2001 FAD   A C2    1 
HETATM 18225 C  C2    B FAD   C  2  .    ? -41.172 54.552  81.925  0.41 15.95 ? 2001 FAD   A C2    1 
HETATM 18226 O  O2    A FAD   C  2  .    ? -40.794 54.935  83.302  0.59 16.48 ? 2001 FAD   A O2    1 
HETATM 18227 O  O2    B FAD   C  2  .    ? -40.620 54.837  83.105  0.41 15.66 ? 2001 FAD   A O2    1 
HETATM 18228 N  N3    A FAD   C  2  .    ? -42.118 55.561  81.506  0.59 16.08 ? 2001 FAD   A N3    1 
HETATM 18229 N  N3    B FAD   C  2  .    ? -42.180 55.367  81.478  0.41 15.85 ? 2001 FAD   A N3    1 
HETATM 18230 C  C4    A FAD   C  2  .    ? -42.689 55.299  80.291  0.59 18.19 ? 2001 FAD   A C4    1 
HETATM 18231 C  C4    B FAD   C  2  .    ? -42.778 55.125  80.277  0.41 17.89 ? 2001 FAD   A C4    1 
HETATM 18232 O  O4    A FAD   C  2  .    ? -43.477 56.253  79.739  0.59 17.25 ? 2001 FAD   A O4    1 
HETATM 18233 O  O4    B FAD   C  2  .    ? -43.779 55.942  79.866  0.41 15.21 ? 2001 FAD   A O4    1 
HETATM 18234 C  C4X   A FAD   C  2  .    ? -42.470 53.996  79.609  0.59 16.32 ? 2001 FAD   A C4X   1 
HETATM 18235 C  C4X   B FAD   C  2  .    ? -42.434 53.906  79.504  0.41 16.35 ? 2001 FAD   A C4X   1 
HETATM 18236 N  N5    A FAD   C  2  .    ? -43.031 53.667  78.380  0.59 16.33 ? 2001 FAD   A N5    1 
HETATM 18237 N  N5    B FAD   C  2  .    ? -43.165 53.507  78.399  0.41 16.84 ? 2001 FAD   A N5    1 
HETATM 18238 C  C5X   A FAD   C  2  .    ? -42.779 52.404  77.837  0.59 16.88 ? 2001 FAD   A C5X   1 
HETATM 18239 C  C5X   B FAD   C  2  .    ? -42.811 52.336  77.735  0.41 16.89 ? 2001 FAD   A C5X   1 
HETATM 18240 C  C6    A FAD   C  2  .    ? -43.326 52.022  76.600  0.59 16.06 ? 2001 FAD   A C6    1 
HETATM 18241 C  C6    B FAD   C  2  .    ? -43.532 51.926  76.611  0.41 16.42 ? 2001 FAD   A C6    1 
HETATM 18242 C  C7    A FAD   C  2  .    ? -43.064 50.754  76.092  0.59 17.83 ? 2001 FAD   A C7    1 
HETATM 18243 C  C7    B FAD   C  2  .    ? -43.187 50.760  75.949  0.41 17.63 ? 2001 FAD   A C7    1 
HETATM 18244 C  C7M   A FAD   C  2  .    ? -43.654 50.340  74.775  0.59 18.83 ? 2001 FAD   A C7M   1 
HETATM 18245 C  C7M   B FAD   C  2  .    ? -44.005 50.362  74.755  0.41 16.92 ? 2001 FAD   A C7M   1 
HETATM 18246 C  C8    A FAD   C  2  .    ? -42.262 49.855  76.776  0.59 16.82 ? 2001 FAD   A C8    1 
HETATM 18247 C  C8    B FAD   C  2  .    ? -42.120 49.986  76.386  0.41 17.47 ? 2001 FAD   A C8    1 
HETATM 18248 C  C8M   A FAD   C  2  .    ? -41.981 48.493  76.220  0.59 16.71 ? 2001 FAD   A C8M   1 
HETATM 18249 C  C8M   B FAD   C  2  .    ? -41.727 48.726  75.681  0.41 20.13 ? 2001 FAD   A C8M   1 
HETATM 18250 C  C9    A FAD   C  2  .    ? -41.712 50.218  78.003  0.59 17.65 ? 2001 FAD   A C9    1 
HETATM 18251 C  C9    B FAD   C  2  .    ? -41.393 50.386  77.505  0.41 16.74 ? 2001 FAD   A C9    1 
HETATM 18252 C  C9A   A FAD   C  2  .    ? -41.972 51.481  78.525  0.59 17.67 ? 2001 FAD   A C9A   1 
HETATM 18253 C  C9A   B FAD   C  2  .    ? -41.738 51.551  78.169  0.41 17.05 ? 2001 FAD   A C9A   1 
HETATM 18254 N  N10   A FAD   C  2  .    ? -41.387 51.818  79.768  0.59 18.32 ? 2001 FAD   A N10   1 
HETATM 18255 N  N10   B FAD   C  2  .    ? -40.987 51.940  79.302  0.41 15.70 ? 2001 FAD   A N10   1 
HETATM 18256 C  C10   A FAD   C  2  .    ? -41.639 53.062  80.327  0.59 15.58 ? 2001 FAD   A C10   1 
HETATM 18257 C  C10   B FAD   C  2  .    ? -41.335 53.111  79.988  0.41 16.97 ? 2001 FAD   A C10   1 
HETATM 18258 C  "C1'" A FAD   C  2  .    ? -40.604 50.814  80.515  0.59 18.81 ? 2001 FAD   A "C1'" 1 
HETATM 18259 C  "C1'" B FAD   C  2  .    ? -39.841 51.119  79.756  0.41 18.51 ? 2001 FAD   A "C1'" 1 
HETATM 18260 C  "C2'" A FAD   C  2  .    ? -39.109 50.937  80.625  0.59 19.82 ? 2001 FAD   A "C2'" 1 
HETATM 18261 C  "C2'" B FAD   C  2  .    ? -40.303 50.086  80.768  0.41 20.90 ? 2001 FAD   A "C2'" 1 
HETATM 18262 O  "O2'" A FAD   C  2  .    ? -38.598 51.775  79.667  0.59 21.85 ? 2001 FAD   A "O2'" 1 
HETATM 18263 O  "O2'" B FAD   C  2  .    ? -40.769 50.738  81.875  0.41 17.49 ? 2001 FAD   A "O2'" 1 
HETATM 18264 C  "C3'" A FAD   C  2  .    ? -38.589 49.507  80.448  0.59 17.40 ? 2001 FAD   A "C3'" 1 
HETATM 18265 C  "C3'" B FAD   C  2  .    ? -39.178 49.104  81.145  0.41 18.81 ? 2001 FAD   A "C3'" 1 
HETATM 18266 O  "O3'" A FAD   C  2  .    ? -38.721 49.144  79.129  0.59 20.66 ? 2001 FAD   A "O3'" 1 
HETATM 18267 O  "O3'" B FAD   C  2  .    ? -38.123 49.766  81.744  0.41 19.47 ? 2001 FAD   A "O3'" 1 
HETATM 18268 C  "C4'" A FAD   C  2  .    ? -39.311 48.473  81.298  0.59 18.59 ? 2001 FAD   A "C4'" 1 
HETATM 18269 C  "C4'" B FAD   C  2  .    ? -38.652 48.312  79.958  0.41 19.35 ? 2001 FAD   A "C4'" 1 
HETATM 18270 O  "O4'" A FAD   C  2  .    ? -39.323 48.863  82.618  0.59 18.09 ? 2001 FAD   A "O4'" 1 
HETATM 18271 O  "O4'" B FAD   C  2  .    ? -39.668 48.098  79.056  0.41 21.34 ? 2001 FAD   A "O4'" 1 
HETATM 18272 C  "C5'" A FAD   C  2  .    ? -38.666 47.100  81.143  0.59 20.23 ? 2001 FAD   A "C5'" 1 
HETATM 18273 C  "C5'" B FAD   C  2  .    ? -38.040 46.973  80.364  0.41 19.44 ? 2001 FAD   A "C5'" 1 
HETATM 18274 O  "O5'" A FAD   C  2  .    ? -39.547 46.143  81.687  0.59 19.34 ? 2001 FAD   A "O5'" 1 
HETATM 18275 O  "O5'" B FAD   C  2  .    ? -38.962 46.269  81.168  0.41 19.78 ? 2001 FAD   A "O5'" 1 
HETATM 18276 P  P     A FAD   C  2  .    ? -39.747 44.693  81.044  0.59 24.70 ? 2001 FAD   A P     1 
HETATM 18277 P  P     B FAD   C  2  .    ? -39.643 44.877  80.755  0.41 15.97 ? 2001 FAD   A P     1 
HETATM 18278 O  O1P   A FAD   C  2  .    ? -41.049 43.867  81.354  0.59 22.56 ? 2001 FAD   A O1P   1 
HETATM 18279 O  O1P   B FAD   C  2  .    ? -41.030 44.600  81.437  0.41 20.23 ? 2001 FAD   A O1P   1 
HETATM 18280 O  O2P   A FAD   C  2  .    ? -39.481 45.048  79.543  0.59 22.14 ? 2001 FAD   A O2P   1 
HETATM 18281 O  O2P   B FAD   C  2  .    ? -39.554 44.917  79.181  0.41 21.38 ? 2001 FAD   A O2P   1 
HETATM 18282 O  O3P   A FAD   C  2  .    ? -38.338 43.996  81.442  0.59 19.22 ? 2001 FAD   A O3P   1 
HETATM 18283 O  O3P   B FAD   C  2  .    ? -38.505 43.751  81.013  0.41 20.62 ? 2001 FAD   A O3P   1 
HETATM 18284 C  C01   . A1BDD D  3  .    ? -37.928 52.952  75.962  0.68 26.90 ? 2002 A1BDD A C01   1 
HETATM 18285 C  C03   . A1BDD D  3  .    ? -39.595 54.110  77.139  0.68 21.42 ? 2002 A1BDD A C03   1 
HETATM 18286 C  C04   . A1BDD D  3  .    ? -38.898 54.533  78.258  0.68 21.43 ? 2002 A1BDD A C04   1 
HETATM 18287 C  C05   . A1BDD D  3  .    ? -39.271 55.700  78.913  0.68 23.13 ? 2002 A1BDD A C05   1 
HETATM 18288 C  C06   . A1BDD D  3  .    ? -40.346 56.440  78.447  0.68 18.31 ? 2002 A1BDD A C06   1 
HETATM 18289 C  C07   . A1BDD D  3  .    ? -40.791 57.720  79.142  0.68 17.00 ? 2002 A1BDD A C07   1 
HETATM 18290 C  C09   . A1BDD D  3  .    ? -41.043 56.017  77.336  0.68 20.66 ? 2002 A1BDD A C09   1 
HETATM 18291 C  C10   . A1BDD D  3  .    ? -40.668 54.857  76.680  0.68 20.89 ? 2002 A1BDD A C10   1 
HETATM 18292 O  O02   . A1BDD D  3  .    ? -39.228 52.931  76.479  0.68 30.47 ? 2002 A1BDD A O02   1 
HETATM 18293 O  O08   . A1BDD D  3  .    ? -40.001 58.008  80.250  0.68 27.35 ? 2002 A1BDD A O08   1 
HETATM 18294 C  C1    . PGE   E  4  .    ? -3.338  61.045  95.746  1.00 41.72 ? 2003 PGE   A C1    1 
HETATM 18295 O  O1    . PGE   E  4  .    ? -2.812  59.766  95.461  1.00 41.99 ? 2003 PGE   A O1    1 
HETATM 18296 C  C2    . PGE   E  4  .    ? -2.508  61.749  96.795  1.00 35.71 ? 2003 PGE   A C2    1 
HETATM 18297 O  O2    . PGE   E  4  .    ? -1.136  61.603  96.505  1.00 35.13 ? 2003 PGE   A O2    1 
HETATM 18298 C  C3    . PGE   E  4  .    ? -0.321  62.688  96.875  1.00 32.35 ? 2003 PGE   A C3    1 
HETATM 18299 C  C4    . PGE   E  4  .    ? 1.159   62.383  96.864  1.00 30.23 ? 2003 PGE   A C4    1 
HETATM 18300 O  O4    . PGE   E  4  .    ? 2.009   58.267  95.576  1.00 49.91 ? 2003 PGE   A O4    1 
HETATM 18301 C  C6    . PGE   E  4  .    ? 2.816   59.424  95.524  1.00 42.11 ? 2003 PGE   A C6    1 
HETATM 18302 C  C5    . PGE   E  4  .    ? 2.328   60.382  96.595  1.00 41.36 ? 2003 PGE   A C5    1 
HETATM 18303 O  O3    . PGE   E  4  .    ? 1.444   61.308  96.010  1.00 43.66 ? 2003 PGE   A O3    1 
HETATM 18304 C  C     . FMT   F  5  .    ? -40.088 61.259  102.850 1.00 21.50 ? 2004 FMT   A C     1 
HETATM 18305 O  O1    . FMT   F  5  .    ? -39.424 60.687  103.737 1.00 36.18 ? 2004 FMT   A O1    1 
HETATM 18306 O  O2    . FMT   F  5  .    ? -41.330 61.247  102.650 1.00 36.76 ? 2004 FMT   A O2    1 
HETATM 18307 C  C1    . PEG   G  6  .    ? -47.144 75.964  72.532  1.00 27.66 ? 2005 PEG   A C1    1 
HETATM 18308 O  O1    . PEG   G  6  .    ? -46.568 77.085  73.167  1.00 42.32 ? 2005 PEG   A O1    1 
HETATM 18309 C  C2    . PEG   G  6  .    ? -48.408 76.358  71.811  1.00 33.15 ? 2005 PEG   A C2    1 
HETATM 18310 O  O2    . PEG   G  6  .    ? -49.450 76.549  72.738  1.00 43.75 ? 2005 PEG   A O2    1 
HETATM 18311 C  C3    . PEG   G  6  .    ? -50.520 75.646  72.564  1.00 37.14 ? 2005 PEG   A C3    1 
HETATM 18312 C  C4    . PEG   G  6  .    ? -51.844 76.276  72.926  1.00 38.08 ? 2005 PEG   A C4    1 
HETATM 18313 O  O4    . PEG   G  6  .    ? -51.797 76.927  74.175  1.00 42.97 ? 2005 PEG   A O4    1 
HETATM 18314 C  C1    . PEG   H  6  .    ? -25.883 52.768  113.339 1.00 44.08 ? 2006 PEG   A C1    1 
HETATM 18315 O  O1    . PEG   H  6  .    ? -27.016 52.221  113.976 1.00 54.06 ? 2006 PEG   A O1    1 
HETATM 18316 C  C2    . PEG   H  6  .    ? -25.823 54.260  113.556 1.00 41.56 ? 2006 PEG   A C2    1 
HETATM 18317 O  O2    . PEG   H  6  .    ? -25.007 54.563  114.663 1.00 46.83 ? 2006 PEG   A O2    1 
HETATM 18318 C  C3    . PEG   H  6  .    ? -25.467 55.672  115.393 1.00 43.67 ? 2006 PEG   A C3    1 
HETATM 18319 C  C4    . PEG   H  6  .    ? -24.457 56.059  116.445 1.00 45.81 ? 2006 PEG   A C4    1 
HETATM 18320 O  O4    . PEG   H  6  .    ? -23.487 56.902  115.864 1.00 43.28 ? 2006 PEG   A O4    1 
HETATM 18321 P  PA    . NAD   I  7  .    ? -18.033 88.088  107.227 1.00 21.37 ? 2007 NAD   A PA    1 
HETATM 18322 O  O1A   . NAD   I  7  .    ? -16.514 88.031  106.993 1.00 21.53 ? 2007 NAD   A O1A   1 
HETATM 18323 O  O2A   . NAD   I  7  .    ? -18.732 89.311  106.840 1.00 22.64 ? 2007 NAD   A O2A   1 
HETATM 18324 O  O5B   . NAD   I  7  .    ? -18.486 87.871  108.639 1.00 21.89 ? 2007 NAD   A O5B   1 
HETATM 18325 C  C5B   . NAD   I  7  .    ? -18.197 86.640  109.259 1.00 21.39 ? 2007 NAD   A C5B   1 
HETATM 18326 C  C4B   . NAD   I  7  .    ? -18.186 86.736  110.785 1.00 18.04 ? 2007 NAD   A C4B   1 
HETATM 18327 O  O4B   . NAD   I  7  .    ? -17.057 87.474  111.215 1.00 20.09 ? 2007 NAD   A O4B   1 
HETATM 18328 C  C3B   . NAD   I  7  .    ? -19.409 87.342  111.421 1.00 19.49 ? 2007 NAD   A C3B   1 
HETATM 18329 O  O3B   . NAD   I  7  .    ? -19.795 86.675  112.568 1.00 22.06 ? 2007 NAD   A O3B   1 
HETATM 18330 C  C2B   . NAD   I  7  .    ? -18.969 88.718  111.691 1.00 22.31 ? 2007 NAD   A C2B   1 
HETATM 18331 O  O2B   . NAD   I  7  .    ? -19.696 89.300  112.715 1.00 22.06 ? 2007 NAD   A O2B   1 
HETATM 18332 C  C1B   . NAD   I  7  .    ? -17.568 88.457  112.089 1.00 21.71 ? 2007 NAD   A C1B   1 
HETATM 18333 N  N9A   . NAD   I  7  .    ? -16.689 89.592  112.005 1.00 20.52 ? 2007 NAD   A N9A   1 
HETATM 18334 C  C8A   . NAD   I  7  .    ? -16.747 90.677  111.163 1.00 22.01 ? 2007 NAD   A C8A   1 
HETATM 18335 N  N7A   . NAD   I  7  .    ? -15.701 91.471  111.395 1.00 23.11 ? 2007 NAD   A N7A   1 
HETATM 18336 C  C5A   . NAD   I  7  .    ? -14.917 90.922  112.394 1.00 20.20 ? 2007 NAD   A C5A   1 
HETATM 18337 C  C6A   . NAD   I  7  .    ? -13.746 91.293  113.027 1.00 24.61 ? 2007 NAD   A C6A   1 
HETATM 18338 N  N6A   . NAD   I  7  .    ? -13.080 92.508  112.660 1.00 28.56 ? 2007 NAD   A N6A   1 
HETATM 18339 N  N1A   . NAD   I  7  .    ? -13.246 90.501  113.974 1.00 24.78 ? 2007 NAD   A N1A   1 
HETATM 18340 C  C2A   . NAD   I  7  .    ? -13.835 89.340  114.355 1.00 25.26 ? 2007 NAD   A C2A   1 
HETATM 18341 N  N3A   . NAD   I  7  .    ? -14.993 88.947  113.761 1.00 22.78 ? 2007 NAD   A N3A   1 
HETATM 18342 C  C4A   . NAD   I  7  .    ? -15.533 89.714  112.798 1.00 21.71 ? 2007 NAD   A C4A   1 
HETATM 18343 O  O3    . NAD   I  7  .    ? -18.762 87.039  106.414 1.00 22.01 ? 2007 NAD   A O3    1 
HETATM 18344 P  PN    . NAD   I  7  .    ? -20.296 86.676  106.115 1.00 21.37 ? 2007 NAD   A PN    1 
HETATM 18345 O  O1N   . NAD   I  7  .    ? -20.804 87.733  105.186 1.00 25.09 ? 2007 NAD   A O1N   1 
HETATM 18346 O  O2N   . NAD   I  7  .    ? -21.106 86.471  107.365 1.00 22.56 ? 2007 NAD   A O2N   1 
HETATM 18347 O  O5D   . NAD   I  7  .    ? -20.205 85.309  105.300 1.00 21.44 ? 2007 NAD   A O5D   1 
HETATM 18348 C  C5D   . NAD   I  7  .    ? -19.844 85.328  103.937 1.00 23.71 ? 2007 NAD   A C5D   1 
HETATM 18349 C  C4D   . NAD   I  7  .    ? -18.393 84.942  103.673 1.00 21.13 ? 2007 NAD   A C4D   1 
HETATM 18350 O  O4D   . NAD   I  7  .    ? -18.063 83.739  104.305 1.00 21.74 ? 2007 NAD   A O4D   1 
HETATM 18351 C  C3D   . NAD   I  7  .    ? -18.095 84.775  102.215 1.00 21.76 ? 2007 NAD   A C3D   1 
HETATM 18352 O  O3D   . NAD   I  7  .    ? -16.905 85.361  101.878 1.00 24.93 ? 2007 NAD   A O3D   1 
HETATM 18353 C  C2D   . NAD   I  7  .    ? -18.041 83.315  102.064 1.00 20.34 ? 2007 NAD   A C2D   1 
HETATM 18354 O  O2D   . NAD   I  7  .    ? -17.338 82.858  100.951 1.00 21.00 ? 2007 NAD   A O2D   1 
HETATM 18355 C  C1D   . NAD   I  7  .    ? -17.433 82.920  103.358 1.00 20.41 ? 2007 NAD   A C1D   1 
HETATM 18356 N  N1N   . NAD   I  7  .    ? -17.754 81.564  103.669 1.00 18.40 ? 2007 NAD   A N1N   1 
HETATM 18357 C  C2N   . NAD   I  7  .    ? -16.753 80.558  103.600 1.00 17.88 ? 2007 NAD   A C2N   1 
HETATM 18358 C  C3N   . NAD   I  7  .    ? -17.117 79.256  103.895 1.00 18.91 ? 2007 NAD   A C3N   1 
HETATM 18359 C  C7N   . NAD   I  7  .    ? -16.139 78.141  103.842 1.00 16.34 ? 2007 NAD   A C7N   1 
HETATM 18360 O  O7N   . NAD   I  7  .    ? -16.471 77.035  104.232 1.00 21.35 ? 2007 NAD   A O7N   1 
HETATM 18361 N  N7N   . NAD   I  7  .    ? -14.844 78.385  103.326 1.00 18.87 ? 2007 NAD   A N7N   1 
HETATM 18362 C  C4N   . NAD   I  7  .    ? -18.452 78.969  104.269 1.00 30.77 ? 2007 NAD   A C4N   1 
HETATM 18363 C  C5N   . NAD   I  7  .    ? -19.452 79.965  104.303 1.00 25.02 ? 2007 NAD   A C5N   1 
HETATM 18364 C  C6N   . NAD   I  7  .    ? -19.089 81.260  103.998 1.00 20.76 ? 2007 NAD   A C6N   1 
HETATM 18365 S  S     . SO4   J  8  .    ? -9.055  52.675  111.029 1.00 18.44 ? 2008 SO4   A S     1 
HETATM 18366 O  O1    . SO4   J  8  .    ? -7.971  52.873  110.039 1.00 20.19 ? 2008 SO4   A O1    1 
HETATM 18367 O  O2    . SO4   J  8  .    ? -10.116 51.830  110.418 1.00 22.24 ? 2008 SO4   A O2    1 
HETATM 18368 O  O3    . SO4   J  8  .    ? -8.510  51.978  112.261 1.00 18.72 ? 2008 SO4   A O3    1 
HETATM 18369 O  O4    . SO4   J  8  .    ? -9.598  54.012  111.398 1.00 22.46 ? 2008 SO4   A O4    1 
HETATM 18370 S  S     . SO4   K  8  .    ? -12.275 74.984  70.199  0.62 29.12 ? 2009 SO4   A S     1 
HETATM 18371 O  O1    . SO4   K  8  .    ? -12.347 76.330  69.552  0.62 38.06 ? 2009 SO4   A O1    1 
HETATM 18372 O  O2    . SO4   K  8  .    ? -12.104 73.927  69.151  0.62 35.22 ? 2009 SO4   A O2    1 
HETATM 18373 O  O3    . SO4   K  8  .    ? -11.088 74.953  71.102  0.62 28.50 ? 2009 SO4   A O3    1 
HETATM 18374 O  O4    . SO4   K  8  .    ? -13.537 74.718  70.958  0.62 22.95 ? 2009 SO4   A O4    1 
HETATM 18375 S  S     . SO4   L  8  .    ? 29.459  70.813  105.700 0.74 38.17 ? 2010 SO4   A S     1 
HETATM 18376 O  O1    . SO4   L  8  .    ? 29.894  69.628  106.504 0.74 44.12 ? 2010 SO4   A O1    1 
HETATM 18377 O  O2    . SO4   L  8  .    ? 29.442  70.445  104.248 0.74 47.57 ? 2010 SO4   A O2    1 
HETATM 18378 O  O3    . SO4   L  8  .    ? 28.098  71.263  106.136 0.74 45.24 ? 2010 SO4   A O3    1 
HETATM 18379 O  O4    . SO4   L  8  .    ? 30.417  71.946  105.908 0.74 42.06 ? 2010 SO4   A O4    1 
HETATM 18380 S  S     . SO4   M  8  .    ? 12.718  75.198  125.970 0.66 35.21 ? 2011 SO4   A S     1 
HETATM 18381 O  O1    . SO4   M  8  .    ? 13.801  74.177  126.135 0.66 38.82 ? 2011 SO4   A O1    1 
HETATM 18382 O  O2    . SO4   M  8  .    ? 11.473  74.543  125.451 0.66 30.65 ? 2011 SO4   A O2    1 
HETATM 18383 O  O3    . SO4   M  8  .    ? 12.414  75.839  127.292 0.66 45.62 ? 2011 SO4   A O3    1 
HETATM 18384 O  O4    . SO4   M  8  .    ? 13.172  76.260  125.022 0.66 45.06 ? 2011 SO4   A O4    1 
HETATM 18385 MG MG    . MG    N  9  .    ? -19.763 91.105  107.066 1.00 26.06 ? 2012 MG    A MG    1 
HETATM 18386 P  PA    A FAD   O  2  .    ? -17.009 22.847  104.166 0.72 19.12 ? 2001 FAD   B PA    1 
HETATM 18387 P  PA    B FAD   O  2  .    ? -16.863 22.746  104.332 0.28 20.63 ? 2001 FAD   B PA    1 
HETATM 18388 O  O1A   A FAD   O  2  .    ? -17.217 24.369  104.291 0.72 23.10 ? 2001 FAD   B O1A   1 
HETATM 18389 O  O1A   B FAD   O  2  .    ? -17.261 24.244  104.240 0.28 23.11 ? 2001 FAD   B O1A   1 
HETATM 18390 O  O2A   A FAD   O  2  .    ? -18.149 21.960  103.935 0.72 20.67 ? 2001 FAD   B O2A   1 
HETATM 18391 O  O2A   B FAD   O  2  .    ? -17.873 21.725  104.176 0.28 23.92 ? 2001 FAD   B O2A   1 
HETATM 18392 O  O5B   A FAD   O  2  .    ? -16.111 22.479  103.000 0.72 18.20 ? 2001 FAD   B O5B   1 
HETATM 18393 O  O5B   B FAD   O  2  .    ? -15.892 22.261  103.317 0.28 20.61 ? 2001 FAD   B O5B   1 
HETATM 18394 C  C5B   A FAD   O  2  .    ? -14.993 23.315  102.695 0.72 20.74 ? 2001 FAD   B C5B   1 
HETATM 18395 C  C5B   B FAD   O  2  .    ? -14.962 23.187  102.781 0.28 20.68 ? 2001 FAD   B C5B   1 
HETATM 18396 C  C4B   A FAD   O  2  .    ? -14.008 22.591  101.780 0.72 17.66 ? 2001 FAD   B C4B   1 
HETATM 18397 C  C4B   B FAD   O  2  .    ? -14.031 22.477  101.808 0.28 17.74 ? 2001 FAD   B C4B   1 
HETATM 18398 O  O4B   A FAD   O  2  .    ? -14.506 22.532  100.476 0.72 17.71 ? 2001 FAD   B O4B   1 
HETATM 18399 O  O4B   B FAD   O  2  .    ? -14.532 22.477  100.507 0.28 17.76 ? 2001 FAD   B O4B   1 
HETATM 18400 C  C3B   A FAD   O  2  .    ? -12.681 23.263  101.616 0.72 16.81 ? 2001 FAD   B C3B   1 
HETATM 18401 C  C3B   B FAD   O  2  .    ? -12.691 23.124  101.730 0.28 17.24 ? 2001 FAD   B C3B   1 
HETATM 18402 O  O3B   A FAD   O  2  .    ? -11.822 23.145  102.699 0.72 16.72 ? 2001 FAD   B O3B   1 
HETATM 18403 O  O3B   B FAD   O  2  .    ? -11.844 22.699  102.731 0.28 17.99 ? 2001 FAD   B O3B   1 
HETATM 18404 C  C2B   A FAD   O  2  .    ? -12.174 22.574  100.398 0.72 17.06 ? 2001 FAD   B C2B   1 
HETATM 18405 C  C2B   B FAD   O  2  .    ? -12.196 22.703  100.400 0.28 17.22 ? 2001 FAD   B C2B   1 
HETATM 18406 O  O2B   A FAD   O  2  .    ? -11.826 21.266  100.607 0.72 16.34 ? 2001 FAD   B O2B   1 
HETATM 18407 O  O2B   B FAD   O  2  .    ? -11.510 21.521  100.452 0.28 18.15 ? 2001 FAD   B O2B   1 
HETATM 18408 C  C1B   A FAD   O  2  .    ? -13.412 22.517  99.589  0.72 17.65 ? 2001 FAD   B C1B   1 
HETATM 18409 C  C1B   B FAD   O  2  .    ? -13.444 22.505  99.621  0.28 17.69 ? 2001 FAD   B C1B   1 
HETATM 18410 N  N9A   A FAD   O  2  .    ? -13.610 23.592  98.656  0.72 17.73 ? 2001 FAD   B N9A   1 
HETATM 18411 N  N9A   B FAD   O  2  .    ? -13.668 23.558  98.670  0.28 17.76 ? 2001 FAD   B N9A   1 
HETATM 18412 C  C8A   A FAD   O  2  .    ? -13.743 24.943  98.897  0.72 19.89 ? 2001 FAD   B C8A   1 
HETATM 18413 C  C8A   B FAD   O  2  .    ? -13.836 24.900  98.947  0.28 19.80 ? 2001 FAD   B C8A   1 
HETATM 18414 N  N7A   A FAD   O  2  .    ? -13.939 25.603  97.755  0.72 19.47 ? 2001 FAD   B N7A   1 
HETATM 18415 N  N7A   B FAD   O  2  .    ? -14.025 25.578  97.813  0.28 19.43 ? 2001 FAD   B N7A   1 
HETATM 18416 C  C5A   A FAD   O  2  .    ? -13.949 24.681  96.715  0.72 15.74 ? 2001 FAD   B C5A   1 
HETATM 18417 C  C5A   B FAD   O  2  .    ? -13.988 24.693  96.745  0.28 15.95 ? 2001 FAD   B C5A   1 
HETATM 18418 C  C6A   A FAD   O  2  .    ? -14.124 24.759  95.349  0.72 17.83 ? 2001 FAD   B C6A   1 
HETATM 18419 C  C6A   B FAD   O  2  .    ? -14.128 24.825  95.374  0.28 17.81 ? 2001 FAD   B C6A   1 
HETATM 18420 N  N6A   A FAD   O  2  .    ? -14.348 26.035  94.726  0.72 18.64 ? 2001 FAD   B N6A   1 
HETATM 18421 N  N6A   B FAD   O  2  .    ? -14.366 26.126  94.799  0.28 18.65 ? 2001 FAD   B N6A   1 
HETATM 18422 N  N1A   A FAD   O  2  .    ? -14.076 23.622  94.634  0.72 16.45 ? 2001 FAD   B N1A   1 
HETATM 18423 N  N1A   B FAD   O  2  .    ? -14.037 23.732  94.596  0.28 16.58 ? 2001 FAD   B N1A   1 
HETATM 18424 C  C2A   A FAD   O  2  .    ? -13.882 22.409  95.206  0.72 15.95 ? 2001 FAD   B C2A   1 
HETATM 18425 C  C2A   B FAD   O  2  .    ? -13.821 22.498  95.120  0.28 16.06 ? 2001 FAD   B C2A   1 
HETATM 18426 N  N3A   A FAD   O  2  .    ? -13.718 22.293  96.546  0.72 16.36 ? 2001 FAD   B N3A   1 
HETATM 18427 N  N3A   B FAD   O  2  .    ? -13.684 22.335  96.461  0.28 16.54 ? 2001 FAD   B N3A   1 
HETATM 18428 C  C4A   A FAD   O  2  .    ? -13.748 23.400  97.280  0.72 17.29 ? 2001 FAD   B C4A   1 
HETATM 18429 C  C4A   B FAD   O  2  .    ? -13.761 23.397  97.273  0.28 17.30 ? 2001 FAD   B C4A   1 
HETATM 18430 N  N1    A FAD   O  2  .    ? -7.446  18.213  105.016 0.72 15.13 ? 2001 FAD   B N1    1 
HETATM 18431 N  N1    B FAD   O  2  .    ? -7.104  18.596  105.223 0.28 16.21 ? 2001 FAD   B N1    1 
HETATM 18432 C  C2    A FAD   O  2  .    ? -6.288  17.713  104.391 0.72 17.03 ? 2001 FAD   B C2    1 
HETATM 18433 C  C2    B FAD   O  2  .    ? -6.110  17.937  104.424 0.28 17.01 ? 2001 FAD   B C2    1 
HETATM 18434 O  O2    A FAD   O  2  .    ? -6.045  18.142  103.163 0.72 14.64 ? 2001 FAD   B O2    1 
HETATM 18435 O  O2    B FAD   O  2  .    ? -5.792  18.451  103.213 0.28 18.00 ? 2001 FAD   B O2    1 
HETATM 18436 N  N3    A FAD   O  2  .    ? -5.444  16.821  104.980 0.72 15.44 ? 2001 FAD   B N3    1 
HETATM 18437 N  N3    B FAD   O  2  .    ? -5.439  16.828  104.896 0.28 15.57 ? 2001 FAD   B N3    1 
HETATM 18438 C  C4    A FAD   O  2  .    ? -5.677  16.376  106.246 0.72 16.16 ? 2001 FAD   B C4    1 
HETATM 18439 C  C4    B FAD   O  2  .    ? -5.739  16.289  106.124 0.28 16.37 ? 2001 FAD   B C4    1 
HETATM 18440 O  O4    A FAD   O  2  .    ? -4.850  15.475  106.807 0.72 17.74 ? 2001 FAD   B O4    1 
HETATM 18441 O  O4    B FAD   O  2  .    ? -5.067  15.185  106.568 0.28 14.32 ? 2001 FAD   B O4    1 
HETATM 18442 C  C4X   A FAD   O  2  .    ? -6.869  16.861  106.956 0.72 16.30 ? 2001 FAD   B C4X   1 
HETATM 18443 C  C4X   B FAD   O  2  .    ? -6.849  16.865  106.930 0.28 16.32 ? 2001 FAD   B C4X   1 
HETATM 18444 N  N5    A FAD   O  2  .    ? -7.194  16.425  108.227 0.72 16.44 ? 2001 FAD   B N5    1 
HETATM 18445 N  N5    B FAD   O  2  .    ? -7.273  16.290  108.122 0.28 16.48 ? 2001 FAD   B N5    1 
HETATM 18446 C  C5X   A FAD   O  2  .    ? -8.354  16.911  108.818 0.72 16.85 ? 2001 FAD   B C5X   1 
HETATM 18447 C  C5X   B FAD   O  2  .    ? -8.329  16.863  108.828 0.28 16.89 ? 2001 FAD   B C5X   1 
HETATM 18448 C  C6    A FAD   O  2  .    ? -8.689  16.484  110.113 0.72 16.48 ? 2001 FAD   B C6    1 
HETATM 18449 C  C6    B FAD   O  2  .    ? -8.748  16.291  110.036 0.28 16.74 ? 2001 FAD   B C6    1 
HETATM 18450 C  C7    A FAD   O  2  .    ? -9.857  16.968  110.692 0.72 17.71 ? 2001 FAD   B C7    1 
HETATM 18451 C  C7    B FAD   O  2  .    ? -9.802  16.853  110.742 0.28 17.82 ? 2001 FAD   B C7    1 
HETATM 18452 C  C7M   A FAD   O  2  .    ? -10.255 16.523  112.074 0.72 20.28 ? 2001 FAD   B C7M   1 
HETATM 18453 C  C7M   B FAD   O  2  .    ? -10.243 16.215  112.033 0.28 19.05 ? 2001 FAD   B C7M   1 
HETATM 18454 C  C8    A FAD   O  2  .    ? -10.676 17.846  110.018 0.72 16.84 ? 2001 FAD   B C8    1 
HETATM 18455 C  C8    B FAD   O  2  .    ? -10.443 17.980  110.269 0.28 17.43 ? 2001 FAD   B C8    1 
HETATM 18456 C  C8M   A FAD   O  2  .    ? -11.933 18.368  110.634 0.72 17.35 ? 2001 FAD   B C8M   1 
HETATM 18457 C  C8M   B FAD   O  2  .    ? -11.576 18.597  111.025 0.28 18.99 ? 2001 FAD   B C8M   1 
HETATM 18458 C  C9    A FAD   O  2  .    ? -10.352 18.273  108.743 0.72 18.82 ? 2001 FAD   B C9    1 
HETATM 18459 C  C9    B FAD   O  2  .    ? -10.031 18.562  109.075 0.28 16.86 ? 2001 FAD   B C9    1 
HETATM 18460 C  C9A   A FAD   O  2  .    ? -9.199  17.808  108.155 0.72 17.47 ? 2001 FAD   B C9A   1 
HETATM 18461 C  C9A   B FAD   O  2  .    ? -8.981  18.002  108.361 0.28 16.41 ? 2001 FAD   B C9A   1 
HETATM 18462 N  N10   A FAD   O  2  .    ? -8.866  18.265  106.852 0.72 17.71 ? 2001 FAD   B N10   1 
HETATM 18463 N  N10   B FAD   O  2  .    ? -8.567  18.601  107.138 0.28 16.00 ? 2001 FAD   B N10   1 
HETATM 18464 C  C10   A FAD   O  2  .    ? -7.724  17.771  106.261 0.72 16.87 ? 2001 FAD   B C10   1 
HETATM 18465 C  C10   B FAD   O  2  .    ? -7.506  18.036  106.416 0.28 16.55 ? 2001 FAD   B C10   1 
HETATM 18466 C  "C1'" A FAD   O  2  .    ? -9.792  19.147  106.091 0.72 19.45 ? 2001 FAD   B "C1'" 1 
HETATM 18467 C  "C1'" B FAD   O  2  .    ? -9.248  19.805  106.635 0.28 19.10 ? 2001 FAD   B "C1'" 1 
HETATM 18468 C  "C2'" A FAD   O  2  .    ? -9.498  20.611  105.885 0.72 21.00 ? 2001 FAD   B "C2'" 1 
HETATM 18469 C  "C2'" B FAD   O  2  .    ? -10.423 19.347  105.788 0.28 17.98 ? 2001 FAD   B "C2'" 1 
HETATM 18470 O  "O2'" A FAD   O  2  .    ? -8.561  21.043  106.795 0.72 20.14 ? 2001 FAD   B "O2'" 1 
HETATM 18471 O  "O2'" B FAD   O  2  .    ? -9.948  18.634  104.717 0.28 18.01 ? 2001 FAD   B "O2'" 1 
HETATM 18472 C  "C3'" A FAD   O  2  .    ? -10.825 21.352  106.071 0.72 20.12 ? 2001 FAD   B "C3'" 1 
HETATM 18473 C  "C3'" B FAD   O  2  .    ? -11.260 20.530  105.298 0.28 20.20 ? 2001 FAD   B "C3'" 1 
HETATM 18474 O  "O3'" A FAD   O  2  .    ? -11.150 21.330  107.406 0.72 19.42 ? 2001 FAD   B "O3'" 1 
HETATM 18475 O  "O3'" B FAD   O  2  .    ? -10.423 21.427  104.670 0.28 19.03 ? 2001 FAD   B "O3'" 1 
HETATM 18476 C  "C4'" A FAD   O  2  .    ? -11.983 20.739  105.310 0.72 20.07 ? 2001 FAD   B "C4'" 1 
HETATM 18477 C  "C4'" B FAD   O  2  .    ? -12.026 21.262  106.384 0.28 21.53 ? 2001 FAD   B "C4'" 1 
HETATM 18478 O  "O4'" A FAD   O  2  .    ? -11.682 20.683  103.957 0.72 17.67 ? 2001 FAD   B "O4'" 1 
HETATM 18479 O  "O4'" B FAD   O  2  .    ? -12.319 20.415  107.428 0.28 18.78 ? 2001 FAD   B "O4'" 1 
HETATM 18480 C  "C5'" A FAD   O  2  .    ? -13.230 21.570  105.580 0.72 20.46 ? 2001 FAD   B "C5'" 1 
HETATM 18481 C  "C5'" B FAD   O  2  .    ? -13.294 21.906  105.829 0.28 20.87 ? 2001 FAD   B "C5'" 1 
HETATM 18482 O  "O5'" A FAD   O  2  .    ? -14.343 20.821  105.165 0.72 18.78 ? 2001 FAD   B "O5'" 1 
HETATM 18483 O  "O5'" B FAD   O  2  .    ? -14.182 20.911  105.373 0.28 20.07 ? 2001 FAD   B "O5'" 1 
HETATM 18484 P  P     A FAD   O  2  .    ? -15.775 20.896  105.882 0.72 20.66 ? 2001 FAD   B P     1 
HETATM 18485 P  P     B FAD   O  2  .    ? -15.674 20.833  105.945 0.28 20.30 ? 2001 FAD   B P     1 
HETATM 18486 O  O1P   A FAD   O  2  .    ? -16.677 19.668  105.522 0.72 23.52 ? 2001 FAD   B O1P   1 
HETATM 18487 O  O1P   B FAD   O  2  .    ? -16.540 19.577  105.556 0.28 23.12 ? 2001 FAD   B O1P   1 
HETATM 18488 O  O2P   A FAD   O  2  .    ? -15.448 21.146  107.408 0.72 21.33 ? 2001 FAD   B O2P   1 
HETATM 18489 O  O2P   B FAD   O  2  .    ? -15.402 21.135  107.468 0.28 21.35 ? 2001 FAD   B O2P   1 
HETATM 18490 O  O3P   A FAD   O  2  .    ? -16.319 22.340  105.409 0.72 21.54 ? 2001 FAD   B O3P   1 
HETATM 18491 O  O3P   B FAD   O  2  .    ? -16.235 22.304  105.600 0.28 21.02 ? 2001 FAD   B O3P   1 
HETATM 18492 C  C01   . A1BDD P  3  .    ? 13.412  33.312  78.763  0.71 19.89 ? 2002 A1BDD B C01   1 
HETATM 18493 C  C03   . A1BDD P  3  .    ? 13.291  31.144  79.749  0.71 19.34 ? 2002 A1BDD B C03   1 
HETATM 18494 C  C04   . A1BDD P  3  .    ? 13.213  29.768  79.640  0.71 20.49 ? 2002 A1BDD B C04   1 
HETATM 18495 C  C05   . A1BDD P  3  .    ? 13.157  28.971  80.768  0.71 21.04 ? 2002 A1BDD B C05   1 
HETATM 18496 C  C06   . A1BDD P  3  .    ? 13.207  29.538  82.032  0.71 21.27 ? 2002 A1BDD B C06   1 
HETATM 18497 C  C07   . A1BDD P  3  .    ? 13.160  28.638  83.270  0.71 25.98 ? 2002 A1BDD B C07   1 
HETATM 18498 C  C09   . A1BDD P  3  .    ? 13.295  30.925  82.156  0.71 23.94 ? 2002 A1BDD B C09   1 
HETATM 18499 C  C10   . A1BDD P  3  .    ? 13.338  31.727  81.013  0.71 21.12 ? 2002 A1BDD B C10   1 
HETATM 18500 O  O02   . A1BDD P  3  .    ? 13.348  31.919  78.585  0.71 19.64 ? 2002 A1BDD B O02   1 
HETATM 18501 O  O08   . A1BDD P  3  .    ? 14.442  28.088  83.475  0.71 24.09 ? 2002 A1BDD B O08   1 
HETATM 18502 C  C1    . PEG   Q  6  .    ? 16.219  65.851  54.636  1.00 44.05 ? 2003 PEG   B C1    1 
HETATM 18503 O  O1    . PEG   Q  6  .    ? 16.164  66.794  55.693  1.00 28.79 ? 2003 PEG   B O1    1 
HETATM 18504 C  C2    . PEG   Q  6  .    ? 14.896  65.621  53.945  1.00 35.01 ? 2003 PEG   B C2    1 
HETATM 18505 O  O2    . PEG   Q  6  .    ? 14.506  64.266  54.018  1.00 43.92 ? 2003 PEG   B O2    1 
HETATM 18506 C  C3    . PEG   Q  6  .    ? 15.551  63.343  53.811  1.00 43.15 ? 2003 PEG   B C3    1 
HETATM 18507 C  C4    . PEG   Q  6  .    ? 15.189  62.002  54.401  1.00 33.25 ? 2003 PEG   B C4    1 
HETATM 18508 O  O4    . PEG   Q  6  .    ? 16.358  61.379  54.882  1.00 44.51 ? 2003 PEG   B O4    1 
HETATM 18509 C  C01   . A1BDD R  3  .    ? -7.258  21.847  110.081 0.76 29.60 ? 2004 A1BDD B C01   1 
HETATM 18510 C  C03   . A1BDD R  3  .    ? -6.214  19.868  109.303 0.76 18.86 ? 2004 A1BDD B C03   1 
HETATM 18511 C  C04   . A1BDD R  3  .    ? -5.625  18.719  109.791 0.76 19.81 ? 2004 A1BDD B C04   1 
HETATM 18512 C  C05   . A1BDD R  3  .    ? -4.580  18.134  109.101 0.76 19.96 ? 2004 A1BDD B C05   1 
HETATM 18513 C  C06   . A1BDD R  3  .    ? -4.109  18.695  107.930 0.76 19.62 ? 2004 A1BDD B C06   1 
HETATM 18514 C  C07   . A1BDD R  3  .    ? -2.955  17.988  107.229 0.76 16.67 ? 2004 A1BDD B C07   1 
HETATM 18515 C  C09   . A1BDD R  3  .    ? -4.693  19.849  107.430 0.76 19.65 ? 2004 A1BDD B C09   1 
HETATM 18516 C  C10   . A1BDD R  3  .    ? -5.744  20.434  108.124 0.76 20.74 ? 2004 A1BDD B C10   1 
HETATM 18517 O  O02   . A1BDD R  3  .    ? -7.282  20.448  110.008 0.76 29.56 ? 2004 A1BDD B O02   1 
HETATM 18518 O  O08   . A1BDD R  3  .    ? -2.536  18.662  106.073 0.76 24.57 ? 2004 A1BDD B O08   1 
HETATM 18519 C  C1    . PGE   S  4  .    ? 1.849   60.137  87.422  1.00 41.52 ? 2005 PGE   B C1    1 
HETATM 18520 O  O1    . PGE   S  4  .    ? 0.685   59.384  87.149  1.00 43.95 ? 2005 PGE   B O1    1 
HETATM 18521 C  C2    . PGE   S  4  .    ? 2.899   59.881  86.370  1.00 36.58 ? 2005 PGE   B C2    1 
HETATM 18522 O  O2    . PGE   S  4  .    ? 3.353   58.551  86.469  1.00 45.03 ? 2005 PGE   B O2    1 
HETATM 18523 C  C3    . PGE   S  4  .    ? 4.182   58.095  85.427  1.00 30.77 ? 2005 PGE   B C3    1 
HETATM 18524 C  C4    . PGE   S  4  .    ? 4.667   56.675  85.630  1.00 31.50 ? 2005 PGE   B C4    1 
HETATM 18525 O  O4    . PGE   S  4  .    ? 2.160   54.262  88.010  1.00 43.49 ? 2005 PGE   B O4    1 
HETATM 18526 C  C6    . PGE   S  4  .    ? 2.602   53.875  86.732  1.00 36.91 ? 2005 PGE   B C6    1 
HETATM 18527 C  C5    . PGE   S  4  .    ? 3.912   54.583  86.432  1.00 36.28 ? 2005 PGE   B C5    1 
HETATM 18528 O  O3    . PGE   S  4  .    ? 3.597   55.916  86.129  1.00 38.34 ? 2005 PGE   B O3    1 
HETATM 18529 C  C     . FMT   T  5  .    ? -3.394  43.184  58.558  0.62 20.14 ? 2006 FMT   B C     1 
HETATM 18530 O  O1    . FMT   T  5  .    ? -4.514  43.183  57.988  0.62 28.77 ? 2006 FMT   B O1    1 
HETATM 18531 O  O2    . FMT   T  5  .    ? -2.339  42.582  58.224  0.62 21.53 ? 2006 FMT   B O2    1 
HETATM 18532 C  C     . FMT   U  5  .    ? 11.265  49.041  77.931  0.51 14.00 ? 2007 FMT   B C     1 
HETATM 18533 O  O1    . FMT   U  5  .    ? 12.146  49.239  78.808  0.51 19.74 ? 2007 FMT   B O1    1 
HETATM 18534 O  O2    . FMT   U  5  .    ? 11.348  48.928  76.679  0.51 18.88 ? 2007 FMT   B O2    1 
HETATM 18535 C  C     . FMT   V  5  .    ? -0.873  16.671  83.144  1.00 14.22 ? 2008 FMT   B C     1 
HETATM 18536 O  O1    . FMT   V  5  .    ? -1.117  15.457  83.327  1.00 35.27 ? 2008 FMT   B O1    1 
HETATM 18537 O  O2    . FMT   V  5  .    ? -1.253  17.432  82.250  1.00 32.33 ? 2008 FMT   B O2    1 
HETATM 18538 C  C1    . PGE   W  4  .    ? -6.903  33.272  65.599  1.00 47.90 ? 2009 PGE   B C1    1 
HETATM 18539 O  O1    . PGE   W  4  .    ? -7.410  33.976  66.712  1.00 45.37 ? 2009 PGE   B O1    1 
HETATM 18540 C  C2    . PGE   W  4  .    ? -5.943  32.203  66.059  1.00 43.55 ? 2009 PGE   B C2    1 
HETATM 18541 O  O2    . PGE   W  4  .    ? -6.351  31.732  67.323  1.00 50.91 ? 2009 PGE   B O2    1 
HETATM 18542 C  C3    . PGE   W  4  .    ? -5.342  31.216  68.154  1.00 44.51 ? 2009 PGE   B C3    1 
HETATM 18543 C  C4    . PGE   W  4  .    ? -5.478  31.652  69.595  1.00 34.51 ? 2009 PGE   B C4    1 
HETATM 18544 O  O4    . PGE   W  4  .    ? -7.824  30.973  72.695  1.00 40.47 ? 2009 PGE   B O4    1 
HETATM 18545 C  C6    . PGE   W  4  .    ? -7.973  30.021  71.666  1.00 43.43 ? 2009 PGE   B C6    1 
HETATM 18546 C  C5    . PGE   W  4  .    ? -6.699  30.068  70.844  1.00 39.00 ? 2009 PGE   B C5    1 
HETATM 18547 O  O3    . PGE   W  4  .    ? -6.729  31.261  70.106  1.00 45.05 ? 2009 PGE   B O3    1 
HETATM 18548 O  OH2   . 1PE   X  10 .    ? 42.494  34.821  84.361  1.00 28.51 ? 2010 1PE   B OH2   1 
HETATM 18549 C  C12   . 1PE   X  10 .    ? 42.304  33.683  83.549  1.00 30.04 ? 2010 1PE   B C12   1 
HETATM 18550 C  C22   . 1PE   X  10 .    ? 41.344  33.952  82.415  1.00 39.66 ? 2010 1PE   B C22   1 
HETATM 18551 O  OH3   . 1PE   X  10 .    ? 40.134  34.519  82.865  1.00 41.54 ? 2010 1PE   B OH3   1 
HETATM 18552 C  C13   . 1PE   X  10 .    ? 38.381  35.947  82.038  1.00 48.02 ? 2010 1PE   B C13   1 
HETATM 18553 C  C23   . 1PE   X  10 .    ? 39.212  34.706  81.816  1.00 45.38 ? 2010 1PE   B C23   1 
HETATM 18554 O  OH4   . 1PE   X  10 .    ? 37.903  36.007  83.358  1.00 47.21 ? 2010 1PE   B OH4   1 
HETATM 18555 C  C14   . 1PE   X  10 .    ? 37.033  38.191  83.891  1.00 39.78 ? 2010 1PE   B C14   1 
HETATM 18556 C  C24   . 1PE   X  10 .    ? 36.727  36.776  83.465  1.00 36.08 ? 2010 1PE   B C24   1 
HETATM 18557 O  OH5   . 1PE   X  10 .    ? 37.841  38.204  85.044  1.00 41.54 ? 2010 1PE   B OH5   1 
HETATM 18558 C  C15   . 1PE   X  10 .    ? 39.276  40.130  85.157  1.00 38.04 ? 2010 1PE   B C15   1 
HETATM 18559 C  C25   . 1PE   X  10 .    ? 37.978  39.497  85.592  1.00 36.24 ? 2010 1PE   B C25   1 
HETATM 18560 O  OH6   . 1PE   X  10 .    ? 40.378  39.328  85.508  1.00 38.02 ? 2010 1PE   B OH6   1 
HETATM 18561 C  C16   . 1PE   X  10 .    ? 42.546  39.182  86.517  1.00 35.07 ? 2010 1PE   B C16   1 
HETATM 18562 C  C26   . 1PE   X  10 .    ? 41.450  40.085  86.017  1.00 32.92 ? 2010 1PE   B C26   1 
HETATM 18563 O  OH7   . 1PE   X  10 .    ? 42.461  37.923  85.883  1.00 31.30 ? 2010 1PE   B OH7   1 
HETATM 18564 P  PA    . NAD   Y  7  .    ? 27.627  35.353  75.328  1.00 15.32 ? 2011 NAD   B PA    1 
HETATM 18565 O  O1A   . NAD   Y  7  .    ? 27.676  36.887  75.304  1.00 15.93 ? 2011 NAD   B O1A   1 
HETATM 18566 O  O2A   . NAD   Y  7  .    ? 28.853  34.600  75.636  1.00 17.09 ? 2011 NAD   B O2A   1 
HETATM 18567 O  O5B   . NAD   Y  7  .    ? 27.219  34.804  73.970  1.00 15.13 ? 2011 NAD   B O5B   1 
HETATM 18568 C  C5B   . NAD   Y  7  .    ? 25.980  35.164  73.388  1.00 15.81 ? 2011 NAD   B C5B   1 
HETATM 18569 C  C4B   . NAD   Y  7  .    ? 25.963  34.943  71.886  1.00 14.96 ? 2011 NAD   B C4B   1 
HETATM 18570 O  O4B   . NAD   Y  7  .    ? 26.744  35.940  71.266  1.00 14.39 ? 2011 NAD   B O4B   1 
HETATM 18571 C  C3B   . NAD   Y  7  .    ? 26.421  33.599  71.399  1.00 14.79 ? 2011 NAD   B C3B   1 
HETATM 18572 O  O3B   . NAD   Y  7  .    ? 25.666  33.194  70.302  1.00 14.44 ? 2011 NAD   B O3B   1 
HETATM 18573 C  C2B   . NAD   Y  7  .    ? 27.807  33.915  70.976  1.00 14.78 ? 2011 NAD   B C2B   1 
HETATM 18574 O  O2B   . NAD   Y  7  .    ? 28.368  33.068  70.021  1.00 15.17 ? 2011 NAD   B O2B   1 
HETATM 18575 C  C1B   . NAD   Y  7  .    ? 27.635  35.257  70.401  1.00 15.08 ? 2011 NAD   B C1B   1 
HETATM 18576 N  N9A   . NAD   Y  7  .    ? 28.856  36.017  70.276  1.00 15.37 ? 2011 NAD   B N9A   1 
HETATM 18577 C  C8A   . NAD   Y  7  .    ? 29.983  35.944  71.085  1.00 17.95 ? 2011 NAD   B C8A   1 
HETATM 18578 N  N7A   . NAD   Y  7  .    ? 30.859  36.870  70.671  1.00 18.54 ? 2011 NAD   B N7A   1 
HETATM 18579 C  C5A   . NAD   Y  7  .    ? 30.334  37.588  69.617  1.00 16.81 ? 2011 NAD   B C5A   1 
HETATM 18580 C  C6A   . NAD   Y  7  .    ? 30.731  38.637  68.813  1.00 17.16 ? 2011 NAD   B C6A   1 
HETATM 18581 N  N6A   . NAD   Y  7  .    ? 32.021  39.248  68.985  1.00 22.10 ? 2011 NAD   B N6A   1 
HETATM 18582 N  N1A   . NAD   Y  7  .    ? 29.926  39.106  67.872  1.00 17.95 ? 2011 NAD   B N1A   1 
HETATM 18583 C  C2A   . NAD   Y  7  .    ? 28.686  38.590  67.628  1.00 17.30 ? 2011 NAD   B C2A   1 
HETATM 18584 N  N3A   . NAD   Y  7  .    ? 28.256  37.558  68.386  1.00 15.46 ? 2011 NAD   B N3A   1 
HETATM 18585 C  C4A   . NAD   Y  7  .    ? 29.037  37.057  69.362  1.00 13.90 ? 2011 NAD   B C4A   1 
HETATM 18586 O  O3    . NAD   Y  7  .    ? 26.530  34.834  76.231  1.00 14.68 ? 2011 NAD   B O3    1 
HETATM 18587 P  PN    . NAD   Y  7  .    ? 26.152  33.406  76.796  1.00 15.07 ? 2011 NAD   B PN    1 
HETATM 18588 O  O1N   . NAD   Y  7  .    ? 27.282  32.902  77.638  1.00 18.54 ? 2011 NAD   B O1N   1 
HETATM 18589 O  O2N   . NAD   Y  7  .    ? 25.772  32.511  75.648  1.00 16.83 ? 2011 NAD   B O2N   1 
HETATM 18590 O  O5D   . NAD   Y  7  .    ? 24.883  33.684  77.672  1.00 16.62 ? 2011 NAD   B O5D   1 
HETATM 18591 C  C5D   . NAD   Y  7  .    ? 24.965  34.163  78.994  1.00 17.49 ? 2011 NAD   B C5D   1 
HETATM 18592 C  C4D   . NAD   Y  7  .    ? 24.786  35.672  79.038  1.00 14.75 ? 2011 NAD   B C4D   1 
HETATM 18593 O  O4D   . NAD   Y  7  .    ? 23.554  36.038  78.444  1.00 15.27 ? 2011 NAD   B O4D   1 
HETATM 18594 C  C3D   . NAD   Y  7  .    ? 24.793  36.225  80.433  1.00 14.86 ? 2011 NAD   B C3D   1 
HETATM 18595 O  O3D   . NAD   Y  7  .    ? 25.479  37.426  80.489  1.00 16.78 ? 2011 NAD   B O3D   1 
HETATM 18596 C  C2D   . NAD   Y  7  .    ? 23.343  36.423  80.665  1.00 15.39 ? 2011 NAD   B C2D   1 
HETATM 18597 O  O2D   . NAD   Y  7  .    ? 22.985  37.261  81.722  1.00 14.56 ? 2011 NAD   B O2D   1 
HETATM 18598 C  C1D   . NAD   Y  7  .    ? 22.862  36.877  79.322  1.00 13.83 ? 2011 NAD   B C1D   1 
HETATM 18599 N  N1N   . NAD   Y  7  .    ? 21.458  36.630  79.173  1.00 14.61 ? 2011 NAD   B N1N   1 
HETATM 18600 C  C2N   . NAD   Y  7  .    ? 20.556  37.711  79.189  1.00 14.12 ? 2011 NAD   B C2N   1 
HETATM 18601 C  C3N   . NAD   Y  7  .    ? 19.218  37.443  79.127  1.00 14.80 ? 2011 NAD   B C3N   1 
HETATM 18602 C  C7N   . NAD   Y  7  .    ? 18.205  38.518  79.126  1.00 14.97 ? 2011 NAD   B C7N   1 
HETATM 18603 O  O7N   . NAD   Y  7  .    ? 17.035  38.216  78.919  1.00 15.73 ? 2011 NAD   B O7N   1 
HETATM 18604 N  N7N   . NAD   Y  7  .    ? 18.583  39.848  79.401  1.00 15.06 ? 2011 NAD   B N7N   1 
HETATM 18605 C  C4N   . NAD   Y  7  .    ? 18.786  36.112  78.962  1.00 29.64 ? 2011 NAD   B C4N   1 
HETATM 18606 C  C5N   . NAD   Y  7  .    ? 19.680  35.020  79.023  1.00 19.48 ? 2011 NAD   B C5N   1 
HETATM 18607 C  C6N   . NAD   Y  7  .    ? 21.033  35.302  79.099  1.00 14.85 ? 2011 NAD   B C6N   1 
HETATM 18608 S  S     . SO4   Z  8  .    ? -7.136  47.204  73.280  1.00 17.61 ? 2012 SO4   B S     1 
HETATM 18609 O  O1    . SO4   Z  8  .    ? -5.932  46.433  72.833  1.00 21.24 ? 2012 SO4   B O1    1 
HETATM 18610 O  O2    . SO4   Z  8  .    ? -7.881  47.705  72.095  1.00 16.72 ? 2012 SO4   B O2    1 
HETATM 18611 O  O3    . SO4   Z  8  .    ? -8.049  46.351  74.054  1.00 20.66 ? 2012 SO4   B O3    1 
HETATM 18612 O  O4    . SO4   Z  8  .    ? -6.635  48.357  74.074  1.00 22.06 ? 2012 SO4   B O4    1 
HETATM 18613 MG MG    . MG    AA 9  .    ? 30.382  33.292  75.409  1.00 23.07 ? 2013 MG    B MG    1 
HETATM 18614 O  O     . HOH   BA 11 .    ? -10.534 91.152  114.295 1.00 32.90 ? 2101 HOH   A O     1 
HETATM 18615 O  O     . HOH   BA 11 .    ? -19.235 72.353  97.610  1.00 25.82 ? 2102 HOH   A O     1 
HETATM 18616 O  O     . HOH   BA 11 .    ? 14.773  76.001  123.640 1.00 30.36 ? 2103 HOH   A O     1 
HETATM 18617 O  O     . HOH   BA 11 .    ? -42.816 79.855  75.322  1.00 42.66 ? 2104 HOH   A O     1 
HETATM 18618 O  O     . HOH   BA 11 .    ? -1.117  88.553  105.622 1.00 18.99 ? 2105 HOH   A O     1 
HETATM 18619 O  O     . HOH   BA 11 .    ? -32.214 55.759  86.030  1.00 26.31 ? 2106 HOH   A O     1 
HETATM 18620 O  O     . HOH   BA 11 .    ? 1.605   93.922  117.130 1.00 35.08 ? 2107 HOH   A O     1 
HETATM 18621 O  O     . HOH   BA 11 .    ? -10.422 62.814  48.710  1.00 43.20 ? 2108 HOH   A O     1 
HETATM 18622 O  O     . HOH   BA 11 .    ? 26.150  71.567  104.993 1.00 34.44 ? 2109 HOH   A O     1 
HETATM 18623 O  O     . HOH   BA 11 .    ? -39.274 37.290  64.444  1.00 41.75 ? 2110 HOH   A O     1 
HETATM 18624 O  O     . HOH   BA 11 .    ? -31.935 79.469  99.228  1.00 26.34 ? 2111 HOH   A O     1 
HETATM 18625 O  O     . HOH   BA 11 .    ? -51.406 73.577  68.191  1.00 34.07 ? 2112 HOH   A O     1 
HETATM 18626 O  O     . HOH   BA 11 .    ? -9.849  80.735  135.738 1.00 49.20 ? 2113 HOH   A O     1 
HETATM 18627 O  O     . HOH   BA 11 .    ? 9.003   90.352  103.129 1.00 40.72 ? 2114 HOH   A O     1 
HETATM 18628 O  O     . HOH   BA 11 .    ? -49.111 49.621  104.796 1.00 45.37 ? 2115 HOH   A O     1 
HETATM 18629 O  O     . HOH   BA 11 .    ? -25.225 60.438  127.882 1.00 36.08 ? 2116 HOH   A O     1 
HETATM 18630 O  O     . HOH   BA 11 .    ? 11.735  74.480  129.063 1.00 33.48 ? 2117 HOH   A O     1 
HETATM 18631 O  O     . HOH   BA 11 .    ? -2.945  81.791  114.911 1.00 31.92 ? 2118 HOH   A O     1 
HETATM 18632 O  O     . HOH   BA 11 .    ? -25.563 96.340  119.224 1.00 44.91 ? 2119 HOH   A O     1 
HETATM 18633 O  O     . HOH   BA 11 .    ? -41.832 80.032  69.854  1.00 39.03 ? 2120 HOH   A O     1 
HETATM 18634 O  O     . HOH   BA 11 .    ? -36.265 64.412  62.685  1.00 38.16 ? 2121 HOH   A O     1 
HETATM 18635 O  O     . HOH   BA 11 .    ? -57.092 49.125  58.059  1.00 41.73 ? 2122 HOH   A O     1 
HETATM 18636 O  O     . HOH   BA 11 .    ? -33.209 71.295  76.765  1.00 37.48 ? 2123 HOH   A O     1 
HETATM 18637 O  O     . HOH   BA 11 .    ? -0.565  91.648  115.437 1.00 36.77 ? 2124 HOH   A O     1 
HETATM 18638 O  O     . HOH   BA 11 .    ? 15.036  54.817  110.863 1.00 37.18 ? 2125 HOH   A O     1 
HETATM 18639 O  O     . HOH   BA 11 .    ? 4.936   74.244  120.253 1.00 40.21 ? 2126 HOH   A O     1 
HETATM 18640 O  O     . HOH   BA 11 .    ? -21.505 55.180  49.951  1.00 43.32 ? 2127 HOH   A O     1 
HETATM 18641 O  O     . HOH   BA 11 .    ? -5.736  70.347  72.944  1.00 42.50 ? 2128 HOH   A O     1 
HETATM 18642 O  O     . HOH   BA 11 .    ? -26.865 63.775  71.178  1.00 44.06 ? 2129 HOH   A O     1 
HETATM 18643 O  O     . HOH   BA 11 .    ? -36.056 85.333  104.165 1.00 34.61 ? 2130 HOH   A O     1 
HETATM 18644 O  O     . HOH   BA 11 .    ? -17.685 58.708  86.375  1.00 32.55 ? 2131 HOH   A O     1 
HETATM 18645 O  O     . HOH   BA 11 .    ? -15.288 92.819  131.187 1.00 42.87 ? 2132 HOH   A O     1 
HETATM 18646 O  O     . HOH   BA 11 .    ? -20.609 54.689  115.781 1.00 42.68 ? 2133 HOH   A O     1 
HETATM 18647 O  O     . HOH   BA 11 .    ? 0.226   82.085  113.562 1.00 37.45 ? 2134 HOH   A O     1 
HETATM 18648 O  O     . HOH   BA 11 .    ? 12.048  55.247  110.852 1.00 39.24 ? 2135 HOH   A O     1 
HETATM 18649 O  O     . HOH   BA 11 .    ? -57.399 67.152  61.656  1.00 28.82 ? 2136 HOH   A O     1 
HETATM 18650 O  O     . HOH   BA 11 .    ? -21.639 95.189  120.963 1.00 38.13 ? 2137 HOH   A O     1 
HETATM 18651 O  O     . HOH   BA 11 .    ? -21.151 56.437  53.614  1.00 35.10 ? 2138 HOH   A O     1 
HETATM 18652 O  O     . HOH   BA 11 .    ? -38.891 66.857  69.302  1.00 38.53 ? 2139 HOH   A O     1 
HETATM 18653 O  O     . HOH   BA 11 .    ? -24.166 92.515  126.862 1.00 32.04 ? 2140 HOH   A O     1 
HETATM 18654 O  O     . HOH   BA 11 .    ? -52.424 61.013  101.867 1.00 28.80 ? 2141 HOH   A O     1 
HETATM 18655 O  O     . HOH   BA 11 .    ? -12.358 87.373  99.150  1.00 37.39 ? 2142 HOH   A O     1 
HETATM 18656 O  O     . HOH   BA 11 .    ? -46.121 25.521  86.102  1.00 45.00 ? 2143 HOH   A O     1 
HETATM 18657 O  O     . HOH   BA 11 .    ? -35.673 55.831  78.215  1.00 41.23 ? 2144 HOH   A O     1 
HETATM 18658 O  O     . HOH   BA 11 .    ? 21.797  67.677  116.545 1.00 31.53 ? 2145 HOH   A O     1 
HETATM 18659 O  O     . HOH   BA 11 .    ? -4.748  69.956  76.491  1.00 38.73 ? 2146 HOH   A O     1 
HETATM 18660 O  O     . HOH   BA 11 .    ? -55.257 75.259  92.224  1.00 43.55 ? 2147 HOH   A O     1 
HETATM 18661 O  O     . HOH   BA 11 .    ? 5.031   80.669  129.545 1.00 38.85 ? 2148 HOH   A O     1 
HETATM 18662 O  O     . HOH   BA 11 .    ? 4.247   86.723  98.504  1.00 37.32 ? 2149 HOH   A O     1 
HETATM 18663 O  O     . HOH   BA 11 .    ? -33.155 70.606  81.395  1.00 38.70 ? 2150 HOH   A O     1 
HETATM 18664 O  O     . HOH   BA 11 .    ? -45.269 72.811  114.522 1.00 41.52 ? 2151 HOH   A O     1 
HETATM 18665 O  O     . HOH   BA 11 .    ? -54.984 33.328  71.491  1.00 34.74 ? 2152 HOH   A O     1 
HETATM 18666 O  O     . HOH   BA 11 .    ? -43.068 80.356  89.783  1.00 31.09 ? 2153 HOH   A O     1 
HETATM 18667 O  O     . HOH   BA 11 .    ? -55.093 75.799  83.680  1.00 35.69 ? 2154 HOH   A O     1 
HETATM 18668 O  O     . HOH   BA 11 .    ? -0.328  63.362  109.895 1.00 22.32 ? 2155 HOH   A O     1 
HETATM 18669 O  O     . HOH   BA 11 .    ? 8.507   92.503  98.935  1.00 43.72 ? 2156 HOH   A O     1 
HETATM 18670 O  O     . HOH   BA 11 .    ? -29.078 57.314  115.513 1.00 39.45 ? 2157 HOH   A O     1 
HETATM 18671 O  O     . HOH   BA 11 .    ? -32.263 95.850  125.537 1.00 42.06 ? 2158 HOH   A O     1 
HETATM 18672 O  O     . HOH   BA 11 .    ? -0.226  79.398  81.912  1.00 39.32 ? 2159 HOH   A O     1 
HETATM 18673 O  O     . HOH   BA 11 .    ? -3.841  78.933  103.992 1.00 23.90 ? 2160 HOH   A O     1 
HETATM 18674 O  O     . HOH   BA 11 .    ? -66.958 72.179  75.330  1.00 30.69 ? 2161 HOH   A O     1 
HETATM 18675 O  O     . HOH   BA 11 .    ? -49.696 33.353  100.108 1.00 44.41 ? 2162 HOH   A O     1 
HETATM 18676 O  O     . HOH   BA 11 .    ? -48.432 54.240  61.394  1.00 24.72 ? 2163 HOH   A O     1 
HETATM 18677 O  O     . HOH   BA 11 .    ? -32.845 25.614  85.360  1.00 43.78 ? 2164 HOH   A O     1 
HETATM 18678 O  O     . HOH   BA 11 .    ? -44.680 29.821  96.337  1.00 44.68 ? 2165 HOH   A O     1 
HETATM 18679 O  O     . HOH   BA 11 .    ? -37.916 48.837  76.739  1.00 31.50 ? 2166 HOH   A O     1 
HETATM 18680 O  O     . HOH   BA 11 .    ? -52.628 24.178  82.639  1.00 41.06 ? 2167 HOH   A O     1 
HETATM 18681 O  O     . HOH   BA 11 .    ? -41.272 62.847  73.673  1.00 28.46 ? 2168 HOH   A O     1 
HETATM 18682 O  O     . HOH   BA 11 .    ? -47.141 75.321  66.930  1.00 34.15 ? 2169 HOH   A O     1 
HETATM 18683 O  O     . HOH   BA 11 .    ? -40.090 96.536  109.463 1.00 41.26 ? 2170 HOH   A O     1 
HETATM 18684 O  O     . HOH   BA 11 .    ? -14.206 75.441  110.050 1.00 22.06 ? 2171 HOH   A O     1 
HETATM 18685 O  O     . HOH   BA 11 .    ? 0.263   58.997  108.805 1.00 30.20 ? 2172 HOH   A O     1 
HETATM 18686 O  O     . HOH   BA 11 .    ? -0.319  59.790  94.903  1.00 37.12 ? 2173 HOH   A O     1 
HETATM 18687 O  O     . HOH   BA 11 .    ? -11.549 62.854  113.304 1.00 19.35 ? 2174 HOH   A O     1 
HETATM 18688 O  O     . HOH   BA 11 .    ? -38.624 65.005  96.551  1.00 30.63 ? 2175 HOH   A O     1 
HETATM 18689 O  O     . HOH   BA 11 .    ? -27.720 60.752  84.490  1.00 36.96 ? 2176 HOH   A O     1 
HETATM 18690 O  O     . HOH   BA 11 .    ? 17.838  78.008  120.039 1.00 35.45 ? 2177 HOH   A O     1 
HETATM 18691 O  O     . HOH   BA 11 .    ? 21.132  57.153  105.216 1.00 32.44 ? 2178 HOH   A O     1 
HETATM 18692 O  O     . HOH   BA 11 .    ? -28.719 74.873  101.990 1.00 33.19 ? 2179 HOH   A O     1 
HETATM 18693 O  O     . HOH   BA 11 .    ? 8.394   89.376  120.379 1.00 27.40 ? 2180 HOH   A O     1 
HETATM 18694 O  O     . HOH   BA 11 .    ? -43.414 33.111  102.557 1.00 38.71 ? 2181 HOH   A O     1 
HETATM 18695 O  O     . HOH   BA 11 .    ? -37.774 62.230  81.621  1.00 28.63 ? 2182 HOH   A O     1 
HETATM 18696 O  O     . HOH   BA 11 .    ? -13.688 74.050  106.155 1.00 20.99 ? 2183 HOH   A O     1 
HETATM 18697 O  O     . HOH   BA 11 .    ? -18.698 53.938  94.754  1.00 40.01 ? 2184 HOH   A O     1 
HETATM 18698 O  O     . HOH   BA 11 .    ? -36.457 64.347  83.112  1.00 33.31 ? 2185 HOH   A O     1 
HETATM 18699 O  O     . HOH   BA 11 .    ? -33.572 93.088  86.212  1.00 39.02 ? 2186 HOH   A O     1 
HETATM 18700 O  O     . HOH   BA 11 .    ? -10.086 80.802  91.342  1.00 23.71 ? 2187 HOH   A O     1 
HETATM 18701 O  O     . HOH   BA 11 .    ? -31.852 73.011  73.608  1.00 43.27 ? 2188 HOH   A O     1 
HETATM 18702 O  O     . HOH   BA 11 .    ? 14.139  86.677  98.697  1.00 40.30 ? 2189 HOH   A O     1 
HETATM 18703 O  O     . HOH   BA 11 .    ? -23.186 63.554  97.941  1.00 21.77 ? 2190 HOH   A O     1 
HETATM 18704 O  O     . HOH   BA 11 .    ? -27.073 99.621  94.684  1.00 44.87 ? 2191 HOH   A O     1 
HETATM 18705 O  O     . HOH   BA 11 .    ? -14.170 61.196  107.647 1.00 25.59 ? 2192 HOH   A O     1 
HETATM 18706 O  O     . HOH   BA 11 .    ? -24.896 66.625  86.563  1.00 31.98 ? 2193 HOH   A O     1 
HETATM 18707 O  O     . HOH   BA 11 .    ? -55.030 56.248  64.825  1.00 19.44 ? 2194 HOH   A O     1 
HETATM 18708 O  O     . HOH   BA 11 .    ? -6.558  58.123  120.069 1.00 21.76 ? 2195 HOH   A O     1 
HETATM 18709 O  O     . HOH   BA 11 .    ? -49.246 66.485  94.060  1.00 21.90 ? 2196 HOH   A O     1 
HETATM 18710 O  O     . HOH   BA 11 .    ? -27.656 78.479  101.164 1.00 30.19 ? 2197 HOH   A O     1 
HETATM 18711 O  O     . HOH   BA 11 .    ? -6.155  68.199  92.580  1.00 29.25 ? 2198 HOH   A O     1 
HETATM 18712 O  O     . HOH   BA 11 .    ? -32.376 79.052  96.426  1.00 31.87 ? 2199 HOH   A O     1 
HETATM 18713 O  O     . HOH   BA 11 .    ? 5.988   75.861  125.888 1.00 41.69 ? 2200 HOH   A O     1 
HETATM 18714 O  O     . HOH   BA 11 .    ? -38.003 62.080  105.384 1.00 35.15 ? 2201 HOH   A O     1 
HETATM 18715 O  O     . HOH   BA 11 .    ? -3.561  69.930  117.693 1.00 25.35 ? 2202 HOH   A O     1 
HETATM 18716 O  O     . HOH   BA 11 .    ? -34.718 67.022  125.281 1.00 32.79 ? 2203 HOH   A O     1 
HETATM 18717 O  O     . HOH   BA 11 .    ? -68.546 56.288  82.804  1.00 30.20 ? 2204 HOH   A O     1 
HETATM 18718 O  O     . HOH   BA 11 .    ? -38.582 37.830  87.880  1.00 37.41 ? 2205 HOH   A O     1 
HETATM 18719 O  O     . HOH   BA 11 .    ? -28.571 56.823  60.174  1.00 35.50 ? 2206 HOH   A O     1 
HETATM 18720 O  O     . HOH   BA 11 .    ? -11.639 68.322  76.562  1.00 27.76 ? 2207 HOH   A O     1 
HETATM 18721 O  O     . HOH   BA 11 .    ? -4.889  71.590  95.733  1.00 40.61 ? 2208 HOH   A O     1 
HETATM 18722 O  O     . HOH   BA 11 .    ? 12.128  81.469  98.162  1.00 38.63 ? 2209 HOH   A O     1 
HETATM 18723 O  O     . HOH   BA 11 .    ? -22.876 80.053  110.319 1.00 26.70 ? 2210 HOH   A O     1 
HETATM 18724 O  O     . HOH   BA 11 .    ? -48.884 33.261  89.532  1.00 38.99 ? 2211 HOH   A O     1 
HETATM 18725 O  O     . HOH   BA 11 .    ? -24.748 64.891  94.675  1.00 35.84 ? 2212 HOH   A O     1 
HETATM 18726 O  O     . HOH   BA 11 .    ? -36.010 51.692  69.366  1.00 33.93 ? 2213 HOH   A O     1 
HETATM 18727 O  O     . HOH   BA 11 .    ? -33.874 97.183  98.193  1.00 41.17 ? 2214 HOH   A O     1 
HETATM 18728 O  O     . HOH   BA 11 .    ? -14.687 48.524  75.977  1.00 29.85 ? 2215 HOH   A O     1 
HETATM 18729 O  O     . HOH   BA 11 .    ? -32.338 82.088  97.785  1.00 30.63 ? 2216 HOH   A O     1 
HETATM 18730 O  O     . HOH   BA 11 .    ? -37.448 77.731  120.273 1.00 39.29 ? 2217 HOH   A O     1 
HETATM 18731 O  O     . HOH   BA 11 .    ? 14.643  60.752  94.735  1.00 27.81 ? 2218 HOH   A O     1 
HETATM 18732 O  O     . HOH   BA 11 .    ? -39.296 60.907  74.536  1.00 35.29 ? 2219 HOH   A O     1 
HETATM 18733 O  O     . HOH   BA 11 .    ? -62.823 43.570  82.277  1.00 30.85 ? 2220 HOH   A O     1 
HETATM 18734 O  O     . HOH   BA 11 .    ? -47.105 34.822  86.992  1.00 31.10 ? 2221 HOH   A O     1 
HETATM 18735 O  O     . HOH   BA 11 .    ? -32.961 91.905  107.160 1.00 33.01 ? 2222 HOH   A O     1 
HETATM 18736 O  O     . HOH   BA 11 .    ? -10.426 49.273  110.059 1.00 21.91 ? 2223 HOH   A O     1 
HETATM 18737 O  O     . HOH   BA 11 .    ? 14.439  86.511  110.311 1.00 29.97 ? 2224 HOH   A O     1 
HETATM 18738 O  O     . HOH   BA 11 .    ? -0.036  92.732  104.826 1.00 24.86 ? 2225 HOH   A O     1 
HETATM 18739 O  O     . HOH   BA 11 .    ? -1.043  49.943  58.087  1.00 26.82 ? 2226 HOH   A O     1 
HETATM 18740 O  O     . HOH   BA 11 .    ? -50.750 38.771  60.860  1.00 44.70 ? 2227 HOH   A O     1 
HETATM 18741 O  O     . HOH   BA 11 .    ? -66.642 67.689  72.067  1.00 33.39 ? 2228 HOH   A O     1 
HETATM 18742 O  O     . HOH   BA 11 .    ? -50.349 32.469  91.808  1.00 37.95 ? 2229 HOH   A O     1 
HETATM 18743 O  O     . HOH   BA 11 .    ? 12.694  73.847  91.715  1.00 36.35 ? 2230 HOH   A O     1 
HETATM 18744 O  O     . HOH   BA 11 .    ? -44.503 41.101  104.141 1.00 32.17 ? 2231 HOH   A O     1 
HETATM 18745 O  O     . HOH   BA 11 .    ? -61.923 57.178  63.736  1.00 31.25 ? 2232 HOH   A O     1 
HETATM 18746 O  O     . HOH   BA 11 .    ? -31.329 58.103  115.534 1.00 43.76 ? 2233 HOH   A O     1 
HETATM 18747 O  O     . HOH   BA 11 .    ? -37.402 63.735  67.139  1.00 32.40 ? 2234 HOH   A O     1 
HETATM 18748 O  O     . HOH   BA 11 .    ? -38.823 77.320  97.224  1.00 24.48 ? 2235 HOH   A O     1 
HETATM 18749 O  O     . HOH   BA 11 .    ? 7.116   53.800  101.531 1.00 18.92 ? 2236 HOH   A O     1 
HETATM 18750 O  O     . HOH   BA 11 .    ? -42.566 38.502  85.043  1.00 28.35 ? 2237 HOH   A O     1 
HETATM 18751 O  O     . HOH   BA 11 .    ? -23.010 60.178  115.877 1.00 21.78 ? 2238 HOH   A O     1 
HETATM 18752 O  O     . HOH   BA 11 .    ? -14.646 63.712  99.473  1.00 26.55 ? 2239 HOH   A O     1 
HETATM 18753 O  O     . HOH   BA 11 .    ? -44.118 62.039  70.108  1.00 25.34 ? 2240 HOH   A O     1 
HETATM 18754 O  O     . HOH   BA 11 .    ? -65.409 47.700  85.576  1.00 36.15 ? 2241 HOH   A O     1 
HETATM 18755 O  O     . HOH   BA 11 .    ? -11.719 72.666  128.626 1.00 27.99 ? 2242 HOH   A O     1 
HETATM 18756 O  O     . HOH   BA 11 .    ? -26.934 53.595  109.657 1.00 28.58 ? 2243 HOH   A O     1 
HETATM 18757 O  O     . HOH   BA 11 .    ? -31.125 89.835  127.947 1.00 43.50 ? 2244 HOH   A O     1 
HETATM 18758 O  O     . HOH   BA 11 .    ? -50.576 69.540  100.342 1.00 22.01 ? 2245 HOH   A O     1 
HETATM 18759 O  O     . HOH   BA 11 .    ? -60.452 59.458  90.525  1.00 20.30 ? 2246 HOH   A O     1 
HETATM 18760 O  O     . HOH   BA 11 .    ? -46.590 68.915  56.497  1.00 27.57 ? 2247 HOH   A O     1 
HETATM 18761 O  O     . HOH   BA 11 .    ? -35.709 39.273  84.502  1.00 38.81 ? 2248 HOH   A O     1 
HETATM 18762 O  O     . HOH   BA 11 .    ? -19.975 58.918  76.389  1.00 22.20 ? 2249 HOH   A O     1 
HETATM 18763 O  O     . HOH   BA 11 .    ? -48.394 80.984  84.865  1.00 37.32 ? 2250 HOH   A O     1 
HETATM 18764 O  O     . HOH   BA 11 .    ? -44.706 63.106  81.447  1.00 16.51 ? 2251 HOH   A O     1 
HETATM 18765 O  O     . HOH   BA 11 .    ? 6.388   90.491  106.731 1.00 31.01 ? 2252 HOH   A O     1 
HETATM 18766 O  O     . HOH   BA 11 .    ? -11.631 71.465  76.935  1.00 35.98 ? 2253 HOH   A O     1 
HETATM 18767 O  O     . HOH   BA 11 .    ? -7.073  50.077  76.738  1.00 26.75 ? 2254 HOH   A O     1 
HETATM 18768 O  O     . HOH   BA 11 .    ? -50.709 51.777  63.992  1.00 22.03 ? 2255 HOH   A O     1 
HETATM 18769 O  O     . HOH   BA 11 .    ? -16.150 75.213  106.103 1.00 22.16 ? 2256 HOH   A O     1 
HETATM 18770 O  O     . HOH   BA 11 .    ? -35.175 76.081  92.152  1.00 33.17 ? 2257 HOH   A O     1 
HETATM 18771 O  O     . HOH   BA 11 .    ? -1.340  76.586  87.947  1.00 30.98 ? 2258 HOH   A O     1 
HETATM 18772 O  O     . HOH   BA 11 .    ? -7.082  80.209  128.266 1.00 33.56 ? 2259 HOH   A O     1 
HETATM 18773 O  O     . HOH   BA 11 .    ? -58.594 37.913  76.251  1.00 31.11 ? 2260 HOH   A O     1 
HETATM 18774 O  O     . HOH   BA 11 .    ? -39.138 27.396  86.597  1.00 42.66 ? 2261 HOH   A O     1 
HETATM 18775 O  O     . HOH   BA 11 .    ? -43.412 75.347  114.064 1.00 29.85 ? 2262 HOH   A O     1 
HETATM 18776 O  O     . HOH   BA 11 .    ? -8.331  80.228  74.760  1.00 32.36 ? 2263 HOH   A O     1 
HETATM 18777 O  O     . HOH   BA 11 .    ? -22.839 66.748  97.551  1.00 21.91 ? 2264 HOH   A O     1 
HETATM 18778 O  O     . HOH   BA 11 .    ? -31.765 86.331  76.592  1.00 37.26 ? 2265 HOH   A O     1 
HETATM 18779 O  O     . HOH   BA 11 .    ? -10.657 68.809  133.680 1.00 32.54 ? 2266 HOH   A O     1 
HETATM 18780 O  O     . HOH   BA 11 .    ? -51.920 47.151  69.077  1.00 30.37 ? 2267 HOH   A O     1 
HETATM 18781 O  O     . HOH   BA 11 .    ? -29.346 37.559  85.374  1.00 42.68 ? 2268 HOH   A O     1 
HETATM 18782 O  O     . HOH   BA 11 .    ? -51.468 54.992  75.941  1.00 18.35 ? 2269 HOH   A O     1 
HETATM 18783 O  O     . HOH   BA 11 .    ? -61.250 55.191  67.566  1.00 20.34 ? 2270 HOH   A O     1 
HETATM 18784 O  O     . HOH   BA 11 .    ? -59.305 75.712  77.200  1.00 34.48 ? 2271 HOH   A O     1 
HETATM 18785 O  O     . HOH   BA 11 .    ? -9.129  44.723  55.952  1.00 33.03 ? 2272 HOH   A O     1 
HETATM 18786 O  O     . HOH   BA 11 .    ? 0.698   84.826  111.811 1.00 27.21 ? 2273 HOH   A O     1 
HETATM 18787 O  O     . HOH   BA 11 .    ? -32.608 91.831  126.158 1.00 38.59 ? 2274 HOH   A O     1 
HETATM 18788 O  O     . HOH   BA 11 .    ? -17.502 72.415  111.341 1.00 19.72 ? 2275 HOH   A O     1 
HETATM 18789 O  O     . HOH   BA 11 .    ? 18.126  58.581  95.810  1.00 29.25 ? 2276 HOH   A O     1 
HETATM 18790 O  O     . HOH   BA 11 .    ? -14.189 64.327  51.411  1.00 36.63 ? 2277 HOH   A O     1 
HETATM 18791 O  O     . HOH   BA 11 .    ? -1.078  77.609  114.640 1.00 26.08 ? 2278 HOH   A O     1 
HETATM 18792 O  O     . HOH   BA 11 .    ? -23.769 65.014  130.061 1.00 41.67 ? 2279 HOH   A O     1 
HETATM 18793 O  O     . HOH   BA 11 .    ? -63.611 73.192  78.476  1.00 33.30 ? 2280 HOH   A O     1 
HETATM 18794 O  O     . HOH   BA 11 .    ? -21.585 46.898  58.105  1.00 31.67 ? 2281 HOH   A O     1 
HETATM 18795 O  O     . HOH   BA 11 .    ? -27.736 55.709  90.522  1.00 31.39 ? 2282 HOH   A O     1 
HETATM 18796 O  O     . HOH   BA 11 .    ? -0.476  69.899  96.274  1.00 33.30 ? 2283 HOH   A O     1 
HETATM 18797 O  O     . HOH   BA 11 .    ? -4.947  54.212  108.301 1.00 19.97 ? 2284 HOH   A O     1 
HETATM 18798 O  O     . HOH   BA 11 .    ? 25.730  79.640  107.413 1.00 32.81 ? 2285 HOH   A O     1 
HETATM 18799 O  O     . HOH   BA 11 .    ? -45.278 89.010  106.215 1.00 36.85 ? 2286 HOH   A O     1 
HETATM 18800 O  O     . HOH   BA 11 .    ? -36.916 84.958  85.740  1.00 35.65 ? 2287 HOH   A O     1 
HETATM 18801 O  O     . HOH   BA 11 .    ? -39.387 35.209  86.021  1.00 33.17 ? 2288 HOH   A O     1 
HETATM 18802 O  O     . HOH   BA 11 .    ? -42.553 60.462  74.251  1.00 34.51 ? 2289 HOH   A O     1 
HETATM 18803 O  O     . HOH   BA 11 .    ? -46.699 59.445  102.105 1.00 23.89 ? 2290 HOH   A O     1 
HETATM 18804 O  O     . HOH   BA 11 .    ? -15.182 55.089  121.705 1.00 36.59 ? 2291 HOH   A O     1 
HETATM 18805 O  O     . HOH   BA 11 .    ? -60.291 50.776  62.218  1.00 35.68 ? 2292 HOH   A O     1 
HETATM 18806 O  O     . HOH   BA 11 .    ? -41.253 85.455  113.795 1.00 29.66 ? 2293 HOH   A O     1 
HETATM 18807 O  O     . HOH   BA 11 .    ? -13.215 55.191  81.501  1.00 32.26 ? 2294 HOH   A O     1 
HETATM 18808 O  O     . HOH   BA 11 .    ? 2.211   85.544  118.245 1.00 23.95 ? 2295 HOH   A O     1 
HETATM 18809 O  O     . HOH   BA 11 .    ? -41.012 71.419  114.312 1.00 32.22 ? 2296 HOH   A O     1 
HETATM 18810 O  O     . HOH   BA 11 .    ? -44.880 63.284  84.317  1.00 18.12 ? 2297 HOH   A O     1 
HETATM 18811 O  O     . HOH   BA 11 .    ? -43.047 48.019  60.176  1.00 28.05 ? 2298 HOH   A O     1 
HETATM 18812 O  O     . HOH   BA 11 .    ? -21.470 90.019  106.355 1.00 29.74 ? 2299 HOH   A O     1 
HETATM 18813 O  O     . HOH   BA 11 .    ? -13.278 58.938  122.586 1.00 26.93 ? 2300 HOH   A O     1 
HETATM 18814 O  O     . HOH   BA 11 .    ? 2.080   91.417  121.277 1.00 40.91 ? 2301 HOH   A O     1 
HETATM 18815 O  O     . HOH   BA 11 .    ? -21.701 88.465  109.013 1.00 26.17 ? 2302 HOH   A O     1 
HETATM 18816 O  O     . HOH   BA 11 .    ? 8.040   91.059  113.607 1.00 33.29 ? 2303 HOH   A O     1 
HETATM 18817 O  O     . HOH   BA 11 .    ? -52.405 48.604  62.777  1.00 35.25 ? 2304 HOH   A O     1 
HETATM 18818 O  O     . HOH   BA 11 .    ? -5.490  53.261  110.903 1.00 17.18 ? 2305 HOH   A O     1 
HETATM 18819 O  O     . HOH   BA 11 .    ? -38.743 49.242  102.472 1.00 32.87 ? 2306 HOH   A O     1 
HETATM 18820 O  O     . HOH   BA 11 .    ? 4.401   73.395  116.469 1.00 28.26 ? 2307 HOH   A O     1 
HETATM 18821 O  O     . HOH   BA 11 .    ? -18.236 79.072  127.398 1.00 24.17 ? 2308 HOH   A O     1 
HETATM 18822 O  O     . HOH   BA 11 .    ? -4.020  69.719  106.916 1.00 31.60 ? 2309 HOH   A O     1 
HETATM 18823 O  O     . HOH   BA 11 .    ? -31.271 46.466  88.238  1.00 34.00 ? 2310 HOH   A O     1 
HETATM 18824 O  O     . HOH   BA 11 .    ? -24.492 99.817  94.384  1.00 38.27 ? 2311 HOH   A O     1 
HETATM 18825 O  O     . HOH   BA 11 .    ? -39.901 57.000  88.071  1.00 17.41 ? 2312 HOH   A O     1 
HETATM 18826 O  O     . HOH   BA 11 .    ? -34.968 64.690  66.328  1.00 31.46 ? 2313 HOH   A O     1 
HETATM 18827 O  O     . HOH   BA 11 .    ? -12.258 76.742  103.248 1.00 19.60 ? 2314 HOH   A O     1 
HETATM 18828 O  O     . HOH   BA 11 .    ? -3.258  57.026  68.222  1.00 34.34 ? 2315 HOH   A O     1 
HETATM 18829 O  O     . HOH   BA 11 .    ? -42.934 84.982  97.395  1.00 27.19 ? 2316 HOH   A O     1 
HETATM 18830 O  O     . HOH   BA 11 .    ? -16.610 55.464  112.368 1.00 33.16 ? 2317 HOH   A O     1 
HETATM 18831 O  O     . HOH   BA 11 .    ? 5.877   73.622  95.804  1.00 44.97 ? 2318 HOH   A O     1 
HETATM 18832 O  O     . HOH   BA 11 .    ? -23.643 82.848  112.001 1.00 21.75 ? 2319 HOH   A O     1 
HETATM 18833 O  O     . HOH   BA 11 .    ? -59.535 53.945  74.743  1.00 19.32 ? 2320 HOH   A O     1 
HETATM 18834 O  O     . HOH   BA 11 .    ? -8.025  59.655  94.252  1.00 37.69 ? 2321 HOH   A O     1 
HETATM 18835 O  O     . HOH   BA 11 .    ? -16.074 91.081  104.545 1.00 34.03 ? 2322 HOH   A O     1 
HETATM 18836 O  O     . HOH   BA 11 .    ? -23.796 63.176  91.769  1.00 22.03 ? 2323 HOH   A O     1 
HETATM 18837 O  O     . HOH   BA 11 .    ? -19.692 76.199  67.440  1.00 38.46 ? 2324 HOH   A O     1 
HETATM 18838 O  O     . HOH   BA 11 .    ? -1.104  83.482  115.328 1.00 29.34 ? 2325 HOH   A O     1 
HETATM 18839 O  O     . HOH   BA 11 .    ? -34.228 76.332  96.243  1.00 35.40 ? 2326 HOH   A O     1 
HETATM 18840 O  O     . HOH   BA 11 .    ? -45.689 75.811  94.409  1.00 26.69 ? 2327 HOH   A O     1 
HETATM 18841 O  O     . HOH   BA 11 .    ? -23.022 56.654  84.051  1.00 35.42 ? 2328 HOH   A O     1 
HETATM 18842 O  O     . HOH   BA 11 .    ? -57.547 64.471  90.917  1.00 28.87 ? 2329 HOH   A O     1 
HETATM 18843 O  O     . HOH   BA 11 .    ? -10.586 62.773  72.821  1.00 29.82 ? 2330 HOH   A O     1 
HETATM 18844 O  O     . HOH   BA 11 .    ? -18.685 58.872  104.358 1.00 25.90 ? 2331 HOH   A O     1 
HETATM 18845 O  O     . HOH   BA 11 .    ? -26.205 82.289  112.565 1.00 23.00 ? 2332 HOH   A O     1 
HETATM 18846 O  O     . HOH   BA 11 .    ? 20.777  58.040  111.126 1.00 31.97 ? 2333 HOH   A O     1 
HETATM 18847 O  O     . HOH   BA 11 .    ? -44.837 79.715  79.358  1.00 39.59 ? 2334 HOH   A O     1 
HETATM 18848 O  O     . HOH   BA 11 .    ? -13.289 77.627  111.194 1.00 21.50 ? 2335 HOH   A O     1 
HETATM 18849 O  O     . HOH   BA 11 .    ? -55.336 29.570  79.998  1.00 36.05 ? 2336 HOH   A O     1 
HETATM 18850 O  O     . HOH   BA 11 .    ? -7.980  87.131  93.570  1.00 41.05 ? 2337 HOH   A O     1 
HETATM 18851 O  O     . HOH   BA 11 .    ? -27.629 87.598  75.236  1.00 43.68 ? 2338 HOH   A O     1 
HETATM 18852 O  O     . HOH   BA 11 .    ? -30.806 66.790  98.759  1.00 37.95 ? 2339 HOH   A O     1 
HETATM 18853 O  O     . HOH   BA 11 .    ? -19.779 93.513  111.740 1.00 32.25 ? 2340 HOH   A O     1 
HETATM 18854 O  O     . HOH   BA 11 .    ? -10.559 67.467  108.200 1.00 17.43 ? 2341 HOH   A O     1 
HETATM 18855 O  O     . HOH   BA 11 .    ? -24.417 92.555  105.158 1.00 38.42 ? 2342 HOH   A O     1 
HETATM 18856 O  O     . HOH   BA 11 .    ? -18.145 73.764  131.976 1.00 37.28 ? 2343 HOH   A O     1 
HETATM 18857 O  O     . HOH   BA 11 .    ? -26.231 56.218  107.969 1.00 21.78 ? 2344 HOH   A O     1 
HETATM 18858 O  O     . HOH   BA 11 .    ? -27.363 82.091  129.709 1.00 32.58 ? 2345 HOH   A O     1 
HETATM 18859 O  O     . HOH   BA 11 .    ? -1.406  57.865  96.726  1.00 31.58 ? 2346 HOH   A O     1 
HETATM 18860 O  O     . HOH   BA 11 .    ? -61.248 52.889  91.260  1.00 27.54 ? 2347 HOH   A O     1 
HETATM 18861 O  O     . HOH   BA 11 .    ? -36.894 80.196  78.993  1.00 20.71 ? 2348 HOH   A O     1 
HETATM 18862 O  O     . HOH   BA 11 .    ? -9.352  64.638  76.488  1.00 22.13 ? 2349 HOH   A O     1 
HETATM 18863 O  O     . HOH   BA 11 .    ? -16.474 76.107  108.689 1.00 19.46 ? 2350 HOH   A O     1 
HETATM 18864 O  O     . HOH   BA 11 .    ? -18.749 61.168  85.468  1.00 22.40 ? 2351 HOH   A O     1 
HETATM 18865 O  O     . HOH   BA 11 .    ? -35.478 72.942  83.628  1.00 24.94 ? 2352 HOH   A O     1 
HETATM 18866 O  O     . HOH   BA 11 .    ? -9.014  77.443  131.886 1.00 37.90 ? 2353 HOH   A O     1 
HETATM 18867 O  O     . HOH   BA 11 .    ? -25.823 69.369  131.284 1.00 37.99 ? 2354 HOH   A O     1 
HETATM 18868 O  O     . HOH   BA 11 .    ? -52.928 63.421  98.353  1.00 21.78 ? 2355 HOH   A O     1 
HETATM 18869 O  O     . HOH   BA 11 .    ? -45.158 63.445  105.337 1.00 37.74 ? 2356 HOH   A O     1 
HETATM 18870 O  O     . HOH   BA 11 .    ? -25.862 50.544  105.231 1.00 36.56 ? 2357 HOH   A O     1 
HETATM 18871 O  O     . HOH   BA 11 .    ? -30.993 91.054  80.708  1.00 35.56 ? 2358 HOH   A O     1 
HETATM 18872 O  O     . HOH   BA 11 .    ? -58.307 72.245  80.110  1.00 35.36 ? 2359 HOH   A O     1 
HETATM 18873 O  O     . HOH   BA 11 .    ? 10.849  54.621  108.883 1.00 40.71 ? 2360 HOH   A O     1 
HETATM 18874 O  O     . HOH   BA 11 .    ? -1.016  83.548  118.091 1.00 24.92 ? 2361 HOH   A O     1 
HETATM 18875 O  O     . HOH   BA 11 .    ? 0.540   85.263  103.126 1.00 22.26 ? 2362 HOH   A O     1 
HETATM 18876 O  O     . HOH   BA 11 .    ? -19.875 78.493  70.353  1.00 25.93 ? 2363 HOH   A O     1 
HETATM 18877 O  O     . HOH   BA 11 .    ? -46.462 30.391  85.508  1.00 30.96 ? 2364 HOH   A O     1 
HETATM 18878 O  O     . HOH   BA 11 .    ? -65.790 58.608  75.927  1.00 20.67 ? 2365 HOH   A O     1 
HETATM 18879 O  O     . HOH   BA 11 .    ? -38.412 62.525  55.788  1.00 38.09 ? 2366 HOH   A O     1 
HETATM 18880 O  O     . HOH   BA 11 .    ? -26.502 85.646  137.288 1.00 42.92 ? 2367 HOH   A O     1 
HETATM 18881 O  O     . HOH   BA 11 .    ? -20.807 73.435  99.823  1.00 31.80 ? 2368 HOH   A O     1 
HETATM 18882 O  O     . HOH   BA 11 .    ? -21.507 65.998  70.336  1.00 46.92 ? 2369 HOH   A O     1 
HETATM 18883 O  O     . HOH   BA 11 .    ? -6.132  54.422  105.241 1.00 33.69 ? 2370 HOH   A O     1 
HETATM 18884 O  O     . HOH   BA 11 .    ? -46.563 67.073  59.698  1.00 24.97 ? 2371 HOH   A O     1 
HETATM 18885 O  O     . HOH   BA 11 .    ? -59.717 60.503  75.901  1.00 17.61 ? 2372 HOH   A O     1 
HETATM 18886 O  O     . HOH   BA 11 .    ? -6.945  41.694  66.454  1.00 25.50 ? 2373 HOH   A O     1 
HETATM 18887 O  O     . HOH   BA 11 .    ? -21.800 42.646  60.961  1.00 35.00 ? 2374 HOH   A O     1 
HETATM 18888 O  O     . HOH   BA 11 .    ? -31.342 59.853  105.515 1.00 26.58 ? 2375 HOH   A O     1 
HETATM 18889 O  O     . HOH   BA 11 .    ? -11.081 91.910  124.305 1.00 35.57 ? 2376 HOH   A O     1 
HETATM 18890 O  O     . HOH   BA 11 .    ? -50.860 50.184  57.450  1.00 34.44 ? 2377 HOH   A O     1 
HETATM 18891 O  O     . HOH   BA 11 .    ? -36.520 58.651  94.239  1.00 18.69 ? 2378 HOH   A O     1 
HETATM 18892 O  O     . HOH   BA 11 .    ? -32.363 59.578  109.641 1.00 31.41 ? 2379 HOH   A O     1 
HETATM 18893 O  O     . HOH   BA 11 .    ? -51.930 46.161  67.028  1.00 34.98 ? 2380 HOH   A O     1 
HETATM 18894 O  O     . HOH   BA 11 .    ? -53.147 56.310  55.264  1.00 36.46 ? 2381 HOH   A O     1 
HETATM 18895 O  O     . HOH   BA 11 .    ? -19.687 54.698  107.118 1.00 31.53 ? 2382 HOH   A O     1 
HETATM 18896 O  O     . HOH   BA 11 .    ? -42.652 60.995  100.191 1.00 26.00 ? 2383 HOH   A O     1 
HETATM 18897 O  O     . HOH   BA 11 .    ? 5.060   66.939  96.109  1.00 27.16 ? 2384 HOH   A O     1 
HETATM 18898 O  O     . HOH   BA 11 .    ? -18.768 69.807  87.812  1.00 26.71 ? 2385 HOH   A O     1 
HETATM 18899 O  O     . HOH   BA 11 .    ? -28.426 76.852  103.252 1.00 35.18 ? 2386 HOH   A O     1 
HETATM 18900 O  O     . HOH   BA 11 .    ? -20.574 47.265  54.922  1.00 31.42 ? 2387 HOH   A O     1 
HETATM 18901 O  O     . HOH   BA 11 .    ? -19.663 88.425  75.222  1.00 36.64 ? 2388 HOH   A O     1 
HETATM 18902 O  O     . HOH   BA 11 .    ? -0.426  74.126  86.247  1.00 41.03 ? 2389 HOH   A O     1 
HETATM 18903 O  O     . HOH   BA 11 .    ? -12.956 93.764  130.755 1.00 45.90 ? 2390 HOH   A O     1 
HETATM 18904 O  O     . HOH   BA 11 .    ? 20.656  83.045  101.251 1.00 36.76 ? 2391 HOH   A O     1 
HETATM 18905 O  O     . HOH   BA 11 .    ? -38.943 88.643  90.691  1.00 36.03 ? 2392 HOH   A O     1 
HETATM 18906 O  O     . HOH   BA 11 .    ? -61.868 57.921  70.204  1.00 20.17 ? 2393 HOH   A O     1 
HETATM 18907 O  O     . HOH   BA 11 .    ? -15.395 43.558  76.900  1.00 43.74 ? 2394 HOH   A O     1 
HETATM 18908 O  O     . HOH   BA 11 .    ? -44.746 58.733  55.238  1.00 30.57 ? 2395 HOH   A O     1 
HETATM 18909 O  O     . HOH   BA 11 .    ? -22.701 58.594  75.952  1.00 29.55 ? 2396 HOH   A O     1 
HETATM 18910 O  O     . HOH   BA 11 .    ? -36.363 94.786  93.979  1.00 34.56 ? 2397 HOH   A O     1 
HETATM 18911 O  O     . HOH   BA 11 .    ? 1.643   72.879  116.008 1.00 29.81 ? 2398 HOH   A O     1 
HETATM 18912 O  O     . HOH   BA 11 .    ? -23.314 63.497  106.216 1.00 19.13 ? 2399 HOH   A O     1 
HETATM 18913 O  O     . HOH   BA 11 .    ? 18.412  57.062  105.276 1.00 29.47 ? 2400 HOH   A O     1 
HETATM 18914 O  O     . HOH   BA 11 .    ? -52.495 53.812  100.251 1.00 27.30 ? 2401 HOH   A O     1 
HETATM 18915 O  O     . HOH   BA 11 .    ? -21.065 54.778  94.979  1.00 36.57 ? 2402 HOH   A O     1 
HETATM 18916 O  O     . HOH   BA 11 .    ? -28.618 41.803  92.567  1.00 44.43 ? 2403 HOH   A O     1 
HETATM 18917 O  O     . HOH   BA 11 .    ? -20.148 90.632  109.191 1.00 28.43 ? 2404 HOH   A O     1 
HETATM 18918 O  O     . HOH   BA 11 .    ? -36.765 61.349  74.917  1.00 36.37 ? 2405 HOH   A O     1 
HETATM 18919 O  O     . HOH   BA 11 .    ? -25.171 95.690  123.801 1.00 37.82 ? 2406 HOH   A O     1 
HETATM 18920 O  O     . HOH   BA 11 .    ? -59.273 51.610  66.081  1.00 22.05 ? 2407 HOH   A O     1 
HETATM 18921 O  O     . HOH   BA 11 .    ? -12.123 78.986  94.641  1.00 18.49 ? 2408 HOH   A O     1 
HETATM 18922 O  O     . HOH   BA 11 .    ? -60.683 67.932  94.344  1.00 39.31 ? 2409 HOH   A O     1 
HETATM 18923 O  O     . HOH   BA 11 .    ? -44.340 30.775  68.996  1.00 36.05 ? 2410 HOH   A O     1 
HETATM 18924 O  O     . HOH   BA 11 .    ? -36.603 63.040  96.030  1.00 28.30 ? 2411 HOH   A O     1 
HETATM 18925 O  O     . HOH   BA 11 .    ? -3.812  78.960  111.196 1.00 29.53 ? 2412 HOH   A O     1 
HETATM 18926 O  O     . HOH   BA 11 .    ? -4.019  72.701  117.091 1.00 26.37 ? 2413 HOH   A O     1 
HETATM 18927 O  O     . HOH   BA 11 .    ? -42.417 47.326  81.187  1.00 22.21 ? 2414 HOH   A O     1 
HETATM 18928 O  O     . HOH   BA 11 .    ? -49.563 53.996  59.279  1.00 32.81 ? 2415 HOH   A O     1 
HETATM 18929 O  O     . HOH   BA 11 .    ? -46.022 33.240  82.752  1.00 36.22 ? 2416 HOH   A O     1 
HETATM 18930 O  O     . HOH   BA 11 .    ? -17.026 79.823  67.892  1.00 40.93 ? 2417 HOH   A O     1 
HETATM 18931 O  O     . HOH   BA 11 .    ? -6.583  71.836  98.170  1.00 37.13 ? 2418 HOH   A O     1 
HETATM 18932 O  O     . HOH   BA 11 .    ? -5.279  77.378  95.115  1.00 25.54 ? 2419 HOH   A O     1 
HETATM 18933 O  O     . HOH   BA 11 .    ? -70.176 60.799  85.275  1.00 36.05 ? 2420 HOH   A O     1 
HETATM 18934 O  O     . HOH   BA 11 .    ? -32.214 92.769  103.798 1.00 26.77 ? 2421 HOH   A O     1 
HETATM 18935 O  O     . HOH   BA 11 .    ? -20.379 54.593  91.266  1.00 38.31 ? 2422 HOH   A O     1 
HETATM 18936 O  O     . HOH   BA 11 .    ? -20.627 70.560  75.761  1.00 23.92 ? 2423 HOH   A O     1 
HETATM 18937 O  O     . HOH   BA 11 .    ? 32.412  71.926  107.750 1.00 45.39 ? 2424 HOH   A O     1 
HETATM 18938 O  O     . HOH   BA 11 .    ? -32.303 48.186  84.098  1.00 35.49 ? 2425 HOH   A O     1 
HETATM 18939 O  O     . HOH   BA 11 .    ? -56.814 45.703  71.205  1.00 21.65 ? 2426 HOH   A O     1 
HETATM 18940 O  O     . HOH   BA 11 .    ? -41.639 79.450  79.965  1.00 29.96 ? 2427 HOH   A O     1 
HETATM 18941 O  O     . HOH   BA 11 .    ? -20.134 43.355  70.473  1.00 41.06 ? 2428 HOH   A O     1 
HETATM 18942 O  O     . HOH   BA 11 .    ? -26.742 88.995  77.736  1.00 31.70 ? 2429 HOH   A O     1 
HETATM 18943 O  O     . HOH   BA 11 .    ? -3.852  77.986  122.725 1.00 23.54 ? 2430 HOH   A O     1 
HETATM 18944 O  O     . HOH   BA 11 .    ? -56.109 55.551  95.031  1.00 21.99 ? 2431 HOH   A O     1 
HETATM 18945 O  O     . HOH   BA 11 .    ? 10.884  57.052  105.858 1.00 27.02 ? 2432 HOH   A O     1 
HETATM 18946 O  O     . HOH   BA 11 .    ? -24.334 59.215  121.613 1.00 39.50 ? 2433 HOH   A O     1 
HETATM 18947 O  O     . HOH   BA 11 .    ? -17.856 82.269  96.740  1.00 20.46 ? 2434 HOH   A O     1 
HETATM 18948 O  O     . HOH   BA 11 .    ? -28.141 61.771  102.190 1.00 18.85 ? 2435 HOH   A O     1 
HETATM 18949 O  O     . HOH   BA 11 .    ? -14.777 66.921  73.219  1.00 23.53 ? 2436 HOH   A O     1 
HETATM 18950 O  O     . HOH   BA 11 .    ? -58.153 65.120  94.386  1.00 27.84 ? 2437 HOH   A O     1 
HETATM 18951 O  O     . HOH   BA 11 .    ? -61.746 65.167  91.572  1.00 41.25 ? 2438 HOH   A O     1 
HETATM 18952 O  O     . HOH   BA 11 .    ? -31.740 82.081  75.459  1.00 22.07 ? 2439 HOH   A O     1 
HETATM 18953 O  O     . HOH   BA 11 .    ? -25.769 63.428  104.729 1.00 22.27 ? 2440 HOH   A O     1 
HETATM 18954 O  O     . HOH   BA 11 .    ? -49.083 29.202  74.088  1.00 39.62 ? 2441 HOH   A O     1 
HETATM 18955 O  O     . HOH   BA 11 .    ? -52.304 78.009  87.574  1.00 29.24 ? 2442 HOH   A O     1 
HETATM 18956 O  O     . HOH   BA 11 .    ? -3.725  57.337  72.952  1.00 23.82 ? 2443 HOH   A O     1 
HETATM 18957 O  O     . HOH   BA 11 .    ? -25.298 62.281  110.097 1.00 21.66 ? 2444 HOH   A O     1 
HETATM 18958 O  O     . HOH   BA 11 .    ? -12.348 76.949  91.115  1.00 17.08 ? 2445 HOH   A O     1 
HETATM 18959 O  O     . HOH   BA 11 .    ? 6.539   78.307  95.134  1.00 45.27 ? 2446 HOH   A O     1 
HETATM 18960 O  O     . HOH   BA 11 .    ? 25.119  76.983  109.595 1.00 32.67 ? 2447 HOH   A O     1 
HETATM 18961 O  O     . HOH   BA 11 .    ? 7.531   66.690  112.382 1.00 37.70 ? 2448 HOH   A O     1 
HETATM 18962 O  O     . HOH   BA 11 .    ? -34.191 69.036  76.244  1.00 31.72 ? 2449 HOH   A O     1 
HETATM 18963 O  O     . HOH   BA 11 .    ? 9.495   80.948  96.720  1.00 42.92 ? 2450 HOH   A O     1 
HETATM 18964 O  O     . HOH   BA 11 .    ? -47.840 54.756  58.317  1.00 35.60 ? 2451 HOH   A O     1 
HETATM 18965 O  O     . HOH   BA 11 .    ? -27.137 64.534  100.185 1.00 27.79 ? 2452 HOH   A O     1 
HETATM 18966 O  O     . HOH   BA 11 .    ? -33.295 48.536  75.279  1.00 30.43 ? 2453 HOH   A O     1 
HETATM 18967 O  O     . HOH   BA 11 .    ? -5.764  79.108  71.109  1.00 44.36 ? 2454 HOH   A O     1 
HETATM 18968 O  O     . HOH   BA 11 .    ? -17.999 57.118  97.321  1.00 21.09 ? 2455 HOH   A O     1 
HETATM 18969 O  O     . HOH   BA 11 .    ? 5.791   62.740  97.359  1.00 20.24 ? 2456 HOH   A O     1 
HETATM 18970 O  O     . HOH   BA 11 .    ? -6.229  82.418  103.411 1.00 20.63 ? 2457 HOH   A O     1 
HETATM 18971 O  O     . HOH   BA 11 .    ? -49.784 68.391  92.001  1.00 22.09 ? 2458 HOH   A O     1 
HETATM 18972 O  O     . HOH   BA 11 .    ? -47.544 48.918  95.908  1.00 22.17 ? 2459 HOH   A O     1 
HETATM 18973 O  O     . HOH   BA 11 .    ? -17.129 86.498  92.270  1.00 25.60 ? 2460 HOH   A O     1 
HETATM 18974 O  O     . HOH   BA 11 .    ? -56.508 34.234  86.454  1.00 26.00 ? 2461 HOH   A O     1 
HETATM 18975 O  O     . HOH   BA 11 .    ? -57.973 27.881  85.723  1.00 38.52 ? 2462 HOH   A O     1 
HETATM 18976 O  O     . HOH   BA 11 .    ? -0.915  58.163  111.069 1.00 29.75 ? 2463 HOH   A O     1 
HETATM 18977 O  O     . HOH   BA 11 .    ? 18.655  61.905  94.587  1.00 30.65 ? 2464 HOH   A O     1 
HETATM 18978 O  O     . HOH   BA 11 .    ? -31.153 34.748  72.655  1.00 44.68 ? 2465 HOH   A O     1 
HETATM 18979 O  O     . HOH   BA 11 .    ? -22.163 67.298  81.406  1.00 26.87 ? 2466 HOH   A O     1 
HETATM 18980 O  O     . HOH   BA 11 .    ? 13.826  86.367  121.013 1.00 36.76 ? 2467 HOH   A O     1 
HETATM 18981 O  O     . HOH   BA 11 .    ? -20.116 65.771  81.193  1.00 27.12 ? 2468 HOH   A O     1 
HETATM 18982 O  O     . HOH   BA 11 .    ? -51.023 69.682  93.939  1.00 22.16 ? 2469 HOH   A O     1 
HETATM 18983 O  O     . HOH   BA 11 .    ? -5.334  67.645  78.056  1.00 32.39 ? 2470 HOH   A O     1 
HETATM 18984 O  O     . HOH   BA 11 .    ? -9.355  55.799  82.679  1.00 32.12 ? 2471 HOH   A O     1 
HETATM 18985 O  O     . HOH   BA 11 .    ? 7.403   57.210  112.358 1.00 33.64 ? 2472 HOH   A O     1 
HETATM 18986 O  O     . HOH   BA 11 .    ? -41.013 48.648  64.048  1.00 24.84 ? 2473 HOH   A O     1 
HETATM 18987 O  O     . HOH   BA 11 .    ? 4.158   57.591  104.981 1.00 21.32 ? 2474 HOH   A O     1 
HETATM 18988 O  O     . HOH   BA 11 .    ? -51.676 72.721  105.571 1.00 31.52 ? 2475 HOH   A O     1 
HETATM 18989 O  O     . HOH   BA 11 .    ? -40.940 90.406  98.670  1.00 27.66 ? 2476 HOH   A O     1 
HETATM 18990 O  O     . HOH   BA 11 .    ? 16.712  57.549  102.861 1.00 21.75 ? 2477 HOH   A O     1 
HETATM 18991 O  O     . HOH   BA 11 .    ? -41.932 67.580  91.120  1.00 19.72 ? 2478 HOH   A O     1 
HETATM 18992 O  O     . HOH   BA 11 .    ? -31.211 83.979  99.240  1.00 23.54 ? 2479 HOH   A O     1 
HETATM 18993 O  O     . HOH   BA 11 .    ? -17.186 67.767  135.079 1.00 42.80 ? 2480 HOH   A O     1 
HETATM 18994 O  O     . HOH   BA 11 .    ? -44.123 55.458  95.059  1.00 17.62 ? 2481 HOH   A O     1 
HETATM 18995 O  O     . HOH   BA 11 .    ? -47.919 57.498  86.290  1.00 16.86 ? 2482 HOH   A O     1 
HETATM 18996 O  O     . HOH   BA 11 .    ? -55.834 36.557  76.277  1.00 30.37 ? 2483 HOH   A O     1 
HETATM 18997 O  O     . HOH   BA 11 .    ? -12.345 63.943  129.784 1.00 33.08 ? 2484 HOH   A O     1 
HETATM 18998 O  O     . HOH   BA 11 .    ? -4.594  82.007  125.157 1.00 38.95 ? 2485 HOH   A O     1 
HETATM 18999 O  O     . HOH   BA 11 .    ? -63.099 53.762  72.187  1.00 26.10 ? 2486 HOH   A O     1 
HETATM 19000 O  O     . HOH   BA 11 .    ? -24.599 88.578  99.910  1.00 22.40 ? 2487 HOH   A O     1 
HETATM 19001 O  O     . HOH   BA 11 .    ? 15.291  82.800  111.295 1.00 24.15 ? 2488 HOH   A O     1 
HETATM 19002 O  O     . HOH   BA 11 .    ? -31.691 88.688  108.636 1.00 29.20 ? 2489 HOH   A O     1 
HETATM 19003 O  O     . HOH   BA 11 .    ? -52.366 29.019  92.708  1.00 43.05 ? 2490 HOH   A O     1 
HETATM 19004 O  O     . HOH   BA 11 .    ? -55.172 47.444  69.938  1.00 22.47 ? 2491 HOH   A O     1 
HETATM 19005 O  O     . HOH   BA 11 .    ? -5.765  75.781  111.285 1.00 19.12 ? 2492 HOH   A O     1 
HETATM 19006 O  O     . HOH   BA 11 .    ? -61.652 70.096  82.975  1.00 21.15 ? 2493 HOH   A O     1 
HETATM 19007 O  O     . HOH   BA 11 .    ? -31.726 38.112  99.662  1.00 50.63 ? 2494 HOH   A O     1 
HETATM 19008 O  O     . HOH   BA 11 .    ? -45.745 64.964  91.797  1.00 18.88 ? 2495 HOH   A O     1 
HETATM 19009 O  O     . HOH   BA 11 .    ? 11.089  67.300  116.729 1.00 26.37 ? 2496 HOH   A O     1 
HETATM 19010 O  O     . HOH   BA 11 .    ? -49.513 77.879  77.536  1.00 30.31 ? 2497 HOH   A O     1 
HETATM 19011 O  O     . HOH   BA 11 .    ? -32.035 61.514  111.636 1.00 24.08 ? 2498 HOH   A O     1 
HETATM 19012 O  O     . HOH   BA 11 .    ? -51.144 64.655  94.836  1.00 20.49 ? 2499 HOH   A O     1 
HETATM 19013 O  O     . HOH   BA 11 .    ? -0.203  77.074  117.194 1.00 25.59 ? 2500 HOH   A O     1 
HETATM 19014 O  O     . HOH   BA 11 .    ? -47.261 60.033  85.178  1.00 16.87 ? 2501 HOH   A O     1 
HETATM 19015 O  O     . HOH   BA 11 .    ? -1.532  77.546  121.414 1.00 26.38 ? 2502 HOH   A O     1 
HETATM 19016 O  O     . HOH   BA 11 .    ? -23.381 54.145  101.384 1.00 26.19 ? 2503 HOH   A O     1 
HETATM 19017 O  O     . HOH   BA 11 .    ? -31.732 58.825  63.203  1.00 31.14 ? 2504 HOH   A O     1 
HETATM 19018 O  O     . HOH   BA 11 .    ? 17.127  68.880  117.958 1.00 27.57 ? 2505 HOH   A O     1 
HETATM 19019 O  O     . HOH   BA 11 .    ? -39.361 78.010  99.928  1.00 22.69 ? 2506 HOH   A O     1 
HETATM 19020 O  O     . HOH   BA 11 .    ? -22.113 95.632  129.586 1.00 42.07 ? 2507 HOH   A O     1 
HETATM 19021 O  O     . HOH   BA 11 .    ? -48.647 56.711  104.651 1.00 40.32 ? 2508 HOH   A O     1 
HETATM 19022 O  O     . HOH   BA 11 .    ? -53.820 55.230  68.477  1.00 18.46 ? 2509 HOH   A O     1 
HETATM 19023 O  O     . HOH   BA 11 .    ? -2.241  74.124  84.467  1.00 31.84 ? 2510 HOH   A O     1 
HETATM 19024 O  O     . HOH   BA 11 .    ? -34.072 82.225  118.541 1.00 24.17 ? 2511 HOH   A O     1 
HETATM 19025 O  O     . HOH   BA 11 .    ? -23.249 62.270  66.432  1.00 37.77 ? 2512 HOH   A O     1 
HETATM 19026 O  O     . HOH   BA 11 .    ? -2.402  53.548  104.586 1.00 27.31 ? 2513 HOH   A O     1 
HETATM 19027 O  O     . HOH   BA 11 .    ? -44.490 73.527  75.003  1.00 27.98 ? 2514 HOH   A O     1 
HETATM 19028 O  O     . HOH   BA 11 .    ? -11.054 58.140  125.601 1.00 35.99 ? 2515 HOH   A O     1 
HETATM 19029 O  O     . HOH   BA 11 .    ? -13.365 54.970  103.580 1.00 34.32 ? 2516 HOH   A O     1 
HETATM 19030 O  O     . HOH   BA 11 .    ? -67.439 59.628  69.908  1.00 29.79 ? 2517 HOH   A O     1 
HETATM 19031 O  O     . HOH   BA 11 .    ? 8.322   67.735  114.665 1.00 33.47 ? 2518 HOH   A O     1 
HETATM 19032 O  O     . HOH   BA 11 .    ? -35.553 51.523  85.380  1.00 19.07 ? 2519 HOH   A O     1 
HETATM 19033 O  O     . HOH   BA 11 .    ? -35.245 40.223  92.068  1.00 25.78 ? 2520 HOH   A O     1 
HETATM 19034 O  O     . HOH   BA 11 .    ? -64.536 44.809  78.120  1.00 38.11 ? 2521 HOH   A O     1 
HETATM 19035 O  O     . HOH   BA 11 .    ? -34.130 75.187  83.123  1.00 25.11 ? 2522 HOH   A O     1 
HETATM 19036 O  O     . HOH   BA 11 .    ? -31.032 60.602  90.540  1.00 23.37 ? 2523 HOH   A O     1 
HETATM 19037 O  O     . HOH   BA 11 .    ? -46.518 54.110  89.717  1.00 18.13 ? 2524 HOH   A O     1 
HETATM 19038 O  O     . HOH   BA 11 .    ? -30.584 90.740  107.130 1.00 26.79 ? 2525 HOH   A O     1 
HETATM 19039 O  O     . HOH   BA 11 .    ? -28.811 76.260  72.949  1.00 27.24 ? 2526 HOH   A O     1 
HETATM 19040 O  O     . HOH   BA 11 .    ? -38.037 40.661  71.636  1.00 30.14 ? 2527 HOH   A O     1 
HETATM 19041 O  O     . HOH   BA 11 .    ? -38.128 65.180  88.210  1.00 33.73 ? 2528 HOH   A O     1 
HETATM 19042 O  O     . HOH   BA 11 .    ? -59.650 39.908  78.801  1.00 40.95 ? 2529 HOH   A O     1 
HETATM 19043 O  O     . HOH   BA 11 .    ? -15.859 67.745  96.791  1.00 17.56 ? 2530 HOH   A O     1 
HETATM 19044 O  O     . HOH   BA 11 .    ? -16.284 60.022  106.543 1.00 23.07 ? 2531 HOH   A O     1 
HETATM 19045 O  O     . HOH   BA 11 .    ? -25.375 87.554  133.025 1.00 41.11 ? 2532 HOH   A O     1 
HETATM 19046 O  O     . HOH   BA 11 .    ? -20.120 68.869  71.152  1.00 40.75 ? 2533 HOH   A O     1 
HETATM 19047 O  O     . HOH   BA 11 .    ? -57.545 57.692  101.215 1.00 26.21 ? 2534 HOH   A O     1 
HETATM 19048 O  O     . HOH   BA 11 .    ? -26.406 50.039  96.582  1.00 27.91 ? 2535 HOH   A O     1 
HETATM 19049 O  O     . HOH   BA 11 .    ? -12.774 62.969  131.885 1.00 43.73 ? 2536 HOH   A O     1 
HETATM 19050 O  O     . HOH   BA 11 .    ? -44.222 40.679  85.759  1.00 38.17 ? 2537 HOH   A O     1 
HETATM 19051 O  O     . HOH   BA 11 .    ? 20.682  61.747  99.052  1.00 24.70 ? 2538 HOH   A O     1 
HETATM 19052 O  O     . HOH   BA 11 .    ? -46.510 31.751  70.358  1.00 34.95 ? 2539 HOH   A O     1 
HETATM 19053 O  O     . HOH   BA 11 .    ? -69.699 64.660  73.964  1.00 27.95 ? 2540 HOH   A O     1 
HETATM 19054 O  O     . HOH   BA 11 .    ? -54.074 79.059  81.438  1.00 32.86 ? 2541 HOH   A O     1 
HETATM 19055 O  O     . HOH   BA 11 .    ? 22.337  85.162  106.183 1.00 44.18 ? 2542 HOH   A O     1 
HETATM 19056 O  O     . HOH   BA 11 .    ? -21.722 52.703  104.218 1.00 36.04 ? 2543 HOH   A O     1 
HETATM 19057 O  O     . HOH   BA 11 .    ? -65.446 71.134  80.510  1.00 26.64 ? 2544 HOH   A O     1 
HETATM 19058 O  O     . HOH   BA 11 .    ? -44.128 24.933  76.273  1.00 40.61 ? 2545 HOH   A O     1 
HETATM 19059 O  O     . HOH   BA 11 .    ? -60.230 46.855  88.758  1.00 25.96 ? 2546 HOH   A O     1 
HETATM 19060 O  O     . HOH   BA 11 .    ? -26.377 50.593  56.403  1.00 37.16 ? 2547 HOH   A O     1 
HETATM 19061 O  O     . HOH   BA 11 .    ? -0.061  86.289  105.912 1.00 24.04 ? 2548 HOH   A O     1 
HETATM 19062 O  O     . HOH   BA 11 .    ? -50.176 66.264  106.331 1.00 28.42 ? 2549 HOH   A O     1 
HETATM 19063 O  O     . HOH   BA 11 .    ? 23.380  65.468  114.998 1.00 26.52 ? 2550 HOH   A O     1 
HETATM 19064 O  O     . HOH   BA 11 .    ? -5.752  64.827  114.276 1.00 22.72 ? 2551 HOH   A O     1 
HETATM 19065 O  O     . HOH   BA 11 .    ? -33.714 52.340  82.071  1.00 36.23 ? 2552 HOH   A O     1 
HETATM 19066 O  O     . HOH   BA 11 .    ? -48.239 65.798  57.862  1.00 25.74 ? 2553 HOH   A O     1 
HETATM 19067 O  O     . HOH   BA 11 .    ? 12.261  75.408  95.042  1.00 33.66 ? 2554 HOH   A O     1 
HETATM 19068 O  O     . HOH   BA 11 .    ? -46.207 64.893  107.072 1.00 36.84 ? 2555 HOH   A O     1 
HETATM 19069 O  O     . HOH   BA 11 .    ? -4.016  75.911  124.733 1.00 28.52 ? 2556 HOH   A O     1 
HETATM 19070 O  O     . HOH   BA 11 .    ? -32.903 39.343  102.264 1.00 46.97 ? 2557 HOH   A O     1 
HETATM 19071 O  O     . HOH   BA 11 .    ? 14.113  81.849  114.263 1.00 23.98 ? 2558 HOH   A O     1 
HETATM 19072 O  O     . HOH   BA 11 .    ? -36.851 51.423  61.101  1.00 31.16 ? 2559 HOH   A O     1 
HETATM 19073 O  O     . HOH   BA 11 .    ? -18.859 59.335  70.084  1.00 22.03 ? 2560 HOH   A O     1 
HETATM 19074 O  O     . HOH   BA 11 .    ? -30.065 62.771  91.993  1.00 35.16 ? 2561 HOH   A O     1 
HETATM 19075 O  O     . HOH   BA 11 .    ? -46.310 29.199  89.347  1.00 35.86 ? 2562 HOH   A O     1 
HETATM 19076 O  O     . HOH   BA 11 .    ? 10.461  62.776  113.157 1.00 29.66 ? 2563 HOH   A O     1 
HETATM 19077 O  O     . HOH   BA 11 .    ? -31.152 71.618  82.748  1.00 32.27 ? 2564 HOH   A O     1 
HETATM 19078 O  O     . HOH   BA 11 .    ? -6.683  70.263  94.215  1.00 24.94 ? 2565 HOH   A O     1 
HETATM 19079 O  O     . HOH   BA 11 .    ? -47.828 64.025  96.774  1.00 22.71 ? 2566 HOH   A O     1 
HETATM 19080 O  O     . HOH   BA 11 .    ? 9.233   55.002  105.026 1.00 27.36 ? 2567 HOH   A O     1 
HETATM 19081 O  O     . HOH   BA 11 .    ? -12.605 43.044  54.785  1.00 41.14 ? 2568 HOH   A O     1 
HETATM 19082 O  O     . HOH   BA 11 .    ? 16.156  61.347  116.194 1.00 33.70 ? 2569 HOH   A O     1 
HETATM 19083 O  O     . HOH   BA 11 .    ? -49.487 75.653  101.548 1.00 23.86 ? 2570 HOH   A O     1 
HETATM 19084 O  O     . HOH   BA 11 .    ? -14.984 55.178  51.115  1.00 39.09 ? 2571 HOH   A O     1 
HETATM 19085 O  O     . HOH   BA 11 .    ? -9.632  74.013  104.265 1.00 20.85 ? 2572 HOH   A O     1 
HETATM 19086 O  O     . HOH   BA 11 .    ? 14.258  87.612  106.320 1.00 38.13 ? 2573 HOH   A O     1 
HETATM 19087 O  O     . HOH   BA 11 .    ? -45.682 78.021  96.068  1.00 21.58 ? 2574 HOH   A O     1 
HETATM 19088 O  O     . HOH   BA 11 .    ? -62.090 61.530  68.202  1.00 24.62 ? 2575 HOH   A O     1 
HETATM 19089 O  O     . HOH   BA 11 .    ? -38.425 50.164  98.338  1.00 25.49 ? 2576 HOH   A O     1 
HETATM 19090 O  O     . HOH   BA 11 .    ? -48.898 82.880  108.974 1.00 34.16 ? 2577 HOH   A O     1 
HETATM 19091 O  O     . HOH   BA 11 .    ? -50.070 56.483  71.748  1.00 25.13 ? 2578 HOH   A O     1 
HETATM 19092 O  O     . HOH   BA 11 .    ? -32.957 69.941  100.332 1.00 35.41 ? 2579 HOH   A O     1 
HETATM 19093 O  O     . HOH   BA 11 .    ? -39.168 52.576  105.494 1.00 37.65 ? 2580 HOH   A O     1 
HETATM 19094 O  O     . HOH   BA 11 .    ? -58.156 57.527  63.089  1.00 19.62 ? 2581 HOH   A O     1 
HETATM 19095 O  O     . HOH   BA 11 .    ? -57.190 59.891  61.066  1.00 19.23 ? 2582 HOH   A O     1 
HETATM 19096 O  O     . HOH   BA 11 .    ? -34.630 80.255  120.309 1.00 25.59 ? 2583 HOH   A O     1 
HETATM 19097 O  O     . HOH   BA 11 .    ? -1.819  85.132  113.265 1.00 26.35 ? 2584 HOH   A O     1 
HETATM 19098 O  O     . HOH   BA 11 .    ? 19.447  81.718  113.327 1.00 31.19 ? 2585 HOH   A O     1 
HETATM 19099 O  O     . HOH   BA 11 .    ? 2.826   83.677  126.810 1.00 37.33 ? 2586 HOH   A O     1 
HETATM 19100 O  O     . HOH   BA 11 .    ? -8.541  64.793  114.052 1.00 20.18 ? 2587 HOH   A O     1 
HETATM 19101 O  O     . HOH   BA 11 .    ? -66.325 61.235  75.760  1.00 18.00 ? 2588 HOH   A O     1 
HETATM 19102 O  O     . HOH   BA 11 .    ? -49.872 48.764  99.839  1.00 27.64 ? 2589 HOH   A O     1 
HETATM 19103 O  O     . HOH   BA 11 .    ? -60.066 50.370  90.840  1.00 35.07 ? 2590 HOH   A O     1 
HETATM 19104 O  O     . HOH   BA 11 .    ? -45.020 86.787  111.884 1.00 46.28 ? 2591 HOH   A O     1 
HETATM 19105 O  O     . HOH   BA 11 .    ? -45.916 72.246  64.247  1.00 18.17 ? 2592 HOH   A O     1 
HETATM 19106 O  O     . HOH   BA 11 .    ? -18.324 60.577  67.054  1.00 26.26 ? 2593 HOH   A O     1 
HETATM 19107 O  O     . HOH   BA 11 .    ? -37.325 45.208  104.147 1.00 32.26 ? 2594 HOH   A O     1 
HETATM 19108 O  O     . HOH   BA 11 .    ? -41.388 63.886  103.587 1.00 22.83 ? 2595 HOH   A O     1 
HETATM 19109 O  O     . HOH   BA 11 .    ? -0.802  72.989  88.948  1.00 35.14 ? 2596 HOH   A O     1 
HETATM 19110 O  O     . HOH   BA 11 .    ? 9.684   67.844  94.064  1.00 36.59 ? 2597 HOH   A O     1 
HETATM 19111 O  O     . HOH   BA 11 .    ? -42.442 77.652  75.806  1.00 25.73 ? 2598 HOH   A O     1 
HETATM 19112 O  O     . HOH   BA 11 .    ? -2.558  55.643  99.928  1.00 30.49 ? 2599 HOH   A O     1 
HETATM 19113 O  O     . HOH   BA 11 .    ? -8.612  59.825  107.172 1.00 20.51 ? 2600 HOH   A O     1 
HETATM 19114 O  O     . HOH   BA 11 .    ? -42.520 65.950  63.819  1.00 35.66 ? 2601 HOH   A O     1 
HETATM 19115 O  O     . HOH   BA 11 .    ? -19.491 84.713  75.576  1.00 32.92 ? 2602 HOH   A O     1 
HETATM 19116 O  O     . HOH   BA 11 .    ? -13.940 84.682  77.164  1.00 32.09 ? 2603 HOH   A O     1 
HETATM 19117 O  O     . HOH   BA 11 .    ? -1.410  79.035  100.126 1.00 28.38 ? 2604 HOH   A O     1 
HETATM 19118 O  O     . HOH   BA 11 .    ? -46.532 66.361  93.882  1.00 19.84 ? 2605 HOH   A O     1 
HETATM 19119 O  O     . HOH   BA 11 .    ? -31.693 88.270  95.165  1.00 22.99 ? 2606 HOH   A O     1 
HETATM 19120 O  O     . HOH   BA 11 .    ? -8.233  92.764  105.971 1.00 24.03 ? 2607 HOH   A O     1 
HETATM 19121 O  O     . HOH   BA 11 .    ? -27.437 58.409  76.265  1.00 39.99 ? 2608 HOH   A O     1 
HETATM 19122 O  O     . HOH   BA 11 .    ? -46.633 82.081  101.469 1.00 25.91 ? 2609 HOH   A O     1 
HETATM 19123 O  O     . HOH   BA 11 .    ? -54.450 47.209  67.406  1.00 30.30 ? 2610 HOH   A O     1 
HETATM 19124 O  O     . HOH   BA 11 .    ? -1.702  77.601  105.421 1.00 21.17 ? 2611 HOH   A O     1 
HETATM 19125 O  O     . HOH   BA 11 .    ? -48.201 74.904  95.559  1.00 23.08 ? 2612 HOH   A O     1 
HETATM 19126 O  O     . HOH   BA 11 .    ? -60.326 61.148  92.679  1.00 23.59 ? 2613 HOH   A O     1 
HETATM 19127 O  O     . HOH   BA 11 .    ? -19.954 59.363  79.106  1.00 34.16 ? 2614 HOH   A O     1 
HETATM 19128 O  O     . HOH   BA 11 .    ? -34.180 96.233  112.478 1.00 44.10 ? 2615 HOH   A O     1 
HETATM 19129 O  O     . HOH   BA 11 .    ? -9.018  86.937  89.063  1.00 46.58 ? 2616 HOH   A O     1 
HETATM 19130 O  O     . HOH   BA 11 .    ? -16.071 46.638  53.958  1.00 31.09 ? 2617 HOH   A O     1 
HETATM 19131 O  O     . HOH   BA 11 .    ? -62.364 54.603  63.328  1.00 34.11 ? 2618 HOH   A O     1 
HETATM 19132 O  O     . HOH   BA 11 .    ? -20.511 81.175  115.876 1.00 20.63 ? 2619 HOH   A O     1 
HETATM 19133 O  O     . HOH   BA 11 .    ? -45.372 62.378  92.599  1.00 17.29 ? 2620 HOH   A O     1 
HETATM 19134 O  O     . HOH   BA 11 .    ? -0.372  83.501  109.738 1.00 29.05 ? 2621 HOH   A O     1 
HETATM 19135 O  O     . HOH   BA 11 .    ? -64.501 59.371  92.935  1.00 35.52 ? 2622 HOH   A O     1 
HETATM 19136 O  O     . HOH   BA 11 .    ? -50.402 37.726  99.839  1.00 37.93 ? 2623 HOH   A O     1 
HETATM 19137 O  O     . HOH   BA 11 .    ? -67.945 36.925  75.656  1.00 36.09 ? 2624 HOH   A O     1 
HETATM 19138 O  O     . HOH   BA 11 .    ? 0.374   76.328  123.223 1.00 35.73 ? 2625 HOH   A O     1 
HETATM 19139 O  O     . HOH   BA 11 .    ? -46.265 24.125  82.671  1.00 38.77 ? 2626 HOH   A O     1 
HETATM 19140 O  O     . HOH   BA 11 .    ? -38.933 31.751  96.828  1.00 37.37 ? 2627 HOH   A O     1 
HETATM 19141 O  O     . HOH   BA 11 .    ? -32.518 92.334  110.278 1.00 34.95 ? 2628 HOH   A O     1 
HETATM 19142 O  O     . HOH   BA 11 .    ? -28.514 61.670  116.802 1.00 23.16 ? 2629 HOH   A O     1 
HETATM 19143 O  O     . HOH   BA 11 .    ? 18.916  72.946  118.223 1.00 24.53 ? 2630 HOH   A O     1 
HETATM 19144 O  O     . HOH   BA 11 .    ? -51.435 58.717  105.028 1.00 40.63 ? 2631 HOH   A O     1 
HETATM 19145 O  O     . HOH   BA 11 .    ? -47.233 70.343  111.193 1.00 34.03 ? 2632 HOH   A O     1 
HETATM 19146 O  O     . HOH   BA 11 .    ? -40.703 79.829  87.589  1.00 21.78 ? 2633 HOH   A O     1 
HETATM 19147 O  O     . HOH   BA 11 .    ? -58.089 73.176  90.815  1.00 43.46 ? 2634 HOH   A O     1 
HETATM 19148 O  O     . HOH   BA 11 .    ? 17.096  71.168  119.294 1.00 27.54 ? 2635 HOH   A O     1 
HETATM 19149 O  O     . HOH   BA 11 .    ? -27.517 70.611  90.096  1.00 28.72 ? 2636 HOH   A O     1 
HETATM 19150 O  O     . HOH   BA 11 .    ? -23.831 60.805  63.737  1.00 32.31 ? 2637 HOH   A O     1 
HETATM 19151 O  O     . HOH   BA 11 .    ? -19.962 51.934  78.294  1.00 27.49 ? 2638 HOH   A O     1 
HETATM 19152 O  O     . HOH   BA 11 .    ? -47.635 84.778  101.852 1.00 40.02 ? 2639 HOH   A O     1 
HETATM 19153 O  O     . HOH   BA 11 .    ? -23.988 66.978  105.286 1.00 23.04 ? 2640 HOH   A O     1 
HETATM 19154 O  O     . HOH   BA 11 .    ? -3.102  87.453  104.996 1.00 26.80 ? 2641 HOH   A O     1 
HETATM 19155 O  O     . HOH   BA 11 .    ? -34.399 49.925  83.430  1.00 32.35 ? 2642 HOH   A O     1 
HETATM 19156 O  O     . HOH   BA 11 .    ? -38.415 36.203  82.558  1.00 34.00 ? 2643 HOH   A O     1 
HETATM 19157 O  O     . HOH   BA 11 .    ? -19.193 91.529  105.201 1.00 30.21 ? 2644 HOH   A O     1 
HETATM 19158 O  O     . HOH   BA 11 .    ? -34.109 56.287  105.400 1.00 24.64 ? 2645 HOH   A O     1 
HETATM 19159 O  O     . HOH   BA 11 .    ? -7.099  62.070  107.204 1.00 19.71 ? 2646 HOH   A O     1 
HETATM 19160 O  O     . HOH   BA 11 .    ? -30.912 81.215  129.181 1.00 41.87 ? 2647 HOH   A O     1 
HETATM 19161 O  O     . HOH   BA 11 .    ? -46.233 55.775  87.420  1.00 16.16 ? 2648 HOH   A O     1 
HETATM 19162 O  O     . HOH   BA 11 .    ? -48.773 61.359  56.854  1.00 23.14 ? 2649 HOH   A O     1 
HETATM 19163 O  O     . HOH   BA 11 .    ? -41.613 70.561  95.270  1.00 24.98 ? 2650 HOH   A O     1 
HETATM 19164 O  O     . HOH   BA 11 .    ? -34.744 94.713  96.275  1.00 30.30 ? 2651 HOH   A O     1 
HETATM 19165 O  O     . HOH   BA 11 .    ? -41.864 55.281  104.836 1.00 39.27 ? 2652 HOH   A O     1 
HETATM 19166 O  O     . HOH   BA 11 .    ? -11.612 59.375  84.782  1.00 28.43 ? 2653 HOH   A O     1 
HETATM 19167 O  O     . HOH   BA 11 .    ? -3.016  77.570  101.545 1.00 26.33 ? 2654 HOH   A O     1 
HETATM 19168 O  O     . HOH   BA 11 .    ? -60.952 68.338  68.613  1.00 22.96 ? 2655 HOH   A O     1 
HETATM 19169 O  O     . HOH   BA 11 .    ? -2.776  62.207  77.738  1.00 23.13 ? 2656 HOH   A O     1 
HETATM 19170 O  O     . HOH   BA 11 .    ? -25.275 88.122  116.247 1.00 23.80 ? 2657 HOH   A O     1 
HETATM 19171 O  O     . HOH   BA 11 .    ? -19.850 86.407  91.678  1.00 24.04 ? 2658 HOH   A O     1 
HETATM 19172 O  O     . HOH   BA 11 .    ? -49.869 48.343  56.089  1.00 39.93 ? 2659 HOH   A O     1 
HETATM 19173 O  O     . HOH   BA 11 .    ? -19.239 90.542  77.039  1.00 33.13 ? 2660 HOH   A O     1 
HETATM 19174 O  O     . HOH   BA 11 .    ? -65.793 68.740  69.166  1.00 34.45 ? 2661 HOH   A O     1 
HETATM 19175 O  O     . HOH   BA 11 .    ? -65.215 54.285  90.925  1.00 34.62 ? 2662 HOH   A O     1 
HETATM 19176 O  O     . HOH   BA 11 .    ? -52.432 72.363  64.333  1.00 27.28 ? 2663 HOH   A O     1 
HETATM 19177 O  O     . HOH   BA 11 .    ? -39.243 76.404  93.200  1.00 24.66 ? 2664 HOH   A O     1 
HETATM 19178 O  O     . HOH   BA 11 .    ? -50.195 27.042  77.449  1.00 34.20 ? 2665 HOH   A O     1 
HETATM 19179 O  O     . HOH   BA 11 .    ? -22.875 53.540  92.687  1.00 31.82 ? 2666 HOH   A O     1 
HETATM 19180 O  O     . HOH   BA 11 .    ? -24.811 87.869  79.294  1.00 27.97 ? 2667 HOH   A O     1 
HETATM 19181 O  O     . HOH   BA 11 .    ? -30.192 80.861  122.981 1.00 30.30 ? 2668 HOH   A O     1 
HETATM 19182 O  O     . HOH   BA 11 .    ? -33.351 60.760  114.192 1.00 44.25 ? 2669 HOH   A O     1 
HETATM 19183 O  O     . HOH   BA 11 .    ? -49.832 72.126  101.125 1.00 23.73 ? 2670 HOH   A O     1 
HETATM 19184 O  O     . HOH   BA 11 .    ? -52.285 61.739  94.696  1.00 20.50 ? 2671 HOH   A O     1 
HETATM 19185 O  O     . HOH   BA 11 .    ? -41.578 71.239  64.228  1.00 27.62 ? 2672 HOH   A O     1 
HETATM 19186 O  O     . HOH   BA 11 .    ? -46.958 34.512  100.987 1.00 38.77 ? 2673 HOH   A O     1 
HETATM 19187 O  O     . HOH   BA 11 .    ? -38.332 61.279  91.808  1.00 20.51 ? 2674 HOH   A O     1 
HETATM 19188 O  O     . HOH   BA 11 .    ? -7.036  84.715  86.753  1.00 38.20 ? 2675 HOH   A O     1 
HETATM 19189 O  O     . HOH   BA 11 .    ? -41.557 88.471  96.814  1.00 30.50 ? 2676 HOH   A O     1 
HETATM 19190 O  O     . HOH   BA 11 .    ? -7.259  37.586  63.809  1.00 37.78 ? 2677 HOH   A O     1 
HETATM 19191 O  O     . HOH   BA 11 .    ? -19.662 90.509  97.724  1.00 39.60 ? 2678 HOH   A O     1 
HETATM 19192 O  O     . HOH   BA 11 .    ? -56.994 31.553  80.306  1.00 36.94 ? 2679 HOH   A O     1 
HETATM 19193 O  O     . HOH   BA 11 .    ? -33.501 45.444  84.798  1.00 27.22 ? 2680 HOH   A O     1 
HETATM 19194 O  O     . HOH   BA 11 .    ? -63.651 70.682  70.830  1.00 26.17 ? 2681 HOH   A O     1 
HETATM 19195 O  O     . HOH   BA 11 .    ? 12.799  66.858  93.397  1.00 30.78 ? 2682 HOH   A O     1 
HETATM 19196 O  O     . HOH   BA 11 .    ? -7.819  72.119  100.741 1.00 27.99 ? 2683 HOH   A O     1 
HETATM 19197 O  O     . HOH   BA 11 .    ? -47.039 48.702  93.206  1.00 20.05 ? 2684 HOH   A O     1 
HETATM 19198 O  O     . HOH   BA 11 .    ? -34.597 66.359  101.666 1.00 23.76 ? 2685 HOH   A O     1 
HETATM 19199 O  O     . HOH   BA 11 .    ? -19.806 78.659  115.007 1.00 20.57 ? 2686 HOH   A O     1 
HETATM 19200 O  O     . HOH   BA 11 .    ? 5.311   54.755  96.963  1.00 27.21 ? 2687 HOH   A O     1 
HETATM 19201 O  O     . HOH   BA 11 .    ? 1.269   74.487  107.500 1.00 25.78 ? 2688 HOH   A O     1 
HETATM 19202 O  O     . HOH   BA 11 .    ? -22.363 98.264  100.434 1.00 39.52 ? 2689 HOH   A O     1 
HETATM 19203 O  O     . HOH   BA 11 .    ? -48.181 82.639  111.294 1.00 33.19 ? 2690 HOH   A O     1 
HETATM 19204 O  O     . HOH   BA 11 .    ? 1.986   64.130  119.302 1.00 42.94 ? 2691 HOH   A O     1 
HETATM 19205 O  O     . HOH   BA 11 .    ? -22.963 64.011  70.652  1.00 43.81 ? 2692 HOH   A O     1 
HETATM 19206 O  O     . HOH   BA 11 .    ? -17.090 52.934  76.370  1.00 32.27 ? 2693 HOH   A O     1 
HETATM 19207 O  O     . HOH   BA 11 .    ? 6.869   60.760  103.316 1.00 18.86 ? 2694 HOH   A O     1 
HETATM 19208 O  O     . HOH   BA 11 .    ? 17.535  80.104  97.002  1.00 32.63 ? 2695 HOH   A O     1 
HETATM 19209 O  O     . HOH   BA 11 .    ? -25.069 78.933  95.087  1.00 23.02 ? 2696 HOH   A O     1 
HETATM 19210 O  O     . HOH   BA 11 .    ? -32.641 60.168  73.477  1.00 38.35 ? 2697 HOH   A O     1 
HETATM 19211 O  O     . HOH   BA 11 .    ? -38.052 76.993  64.788  1.00 36.97 ? 2698 HOH   A O     1 
HETATM 19212 O  O     . HOH   BA 11 .    ? -30.924 73.638  88.151  1.00 35.93 ? 2699 HOH   A O     1 
HETATM 19213 O  O     . HOH   BA 11 .    ? -25.846 61.657  75.908  1.00 38.44 ? 2700 HOH   A O     1 
HETATM 19214 O  O     . HOH   BA 11 .    ? -38.533 86.854  86.975  1.00 39.69 ? 2701 HOH   A O     1 
HETATM 19215 O  O     . HOH   BA 11 .    ? -22.707 94.618  109.548 1.00 46.80 ? 2702 HOH   A O     1 
HETATM 19216 O  O     . HOH   BA 11 .    ? -42.277 56.468  89.472  1.00 17.92 ? 2703 HOH   A O     1 
HETATM 19217 O  O     . HOH   BA 11 .    ? -21.969 54.131  86.179  1.00 36.02 ? 2704 HOH   A O     1 
HETATM 19218 O  O     . HOH   BA 11 .    ? -7.966  76.858  92.117  1.00 23.34 ? 2705 HOH   A O     1 
HETATM 19219 O  O     . HOH   BA 11 .    ? -22.648 83.107  91.578  1.00 20.98 ? 2706 HOH   A O     1 
HETATM 19220 O  O     . HOH   BA 11 .    ? 5.973   80.436  97.123  1.00 34.65 ? 2707 HOH   A O     1 
HETATM 19221 O  O     . HOH   BA 11 .    ? -43.868 59.195  87.592  1.00 16.18 ? 2708 HOH   A O     1 
HETATM 19222 O  O     . HOH   BA 11 .    ? -12.654 89.506  101.732 1.00 33.21 ? 2709 HOH   A O     1 
HETATM 19223 O  O     . HOH   BA 11 .    ? -29.619 83.204  101.368 1.00 26.98 ? 2710 HOH   A O     1 
HETATM 19224 O  O     . HOH   BA 11 .    ? -2.990  89.745  108.914 1.00 24.90 ? 2711 HOH   A O     1 
HETATM 19225 O  O     . HOH   BA 11 .    ? 15.164  75.512  94.178  1.00 37.30 ? 2712 HOH   A O     1 
HETATM 19226 O  O     . HOH   BA 11 .    ? -54.569 37.329  89.264  1.00 30.90 ? 2713 HOH   A O     1 
HETATM 19227 O  O     . HOH   BA 11 .    ? -32.053 74.933  126.392 1.00 28.55 ? 2714 HOH   A O     1 
HETATM 19228 O  O     . HOH   BA 11 .    ? -9.607  39.643  61.451  1.00 40.56 ? 2715 HOH   A O     1 
HETATM 19229 O  O     . HOH   BA 11 .    ? -33.146 77.712  74.041  1.00 24.84 ? 2716 HOH   A O     1 
HETATM 19230 O  O     . HOH   BA 11 .    ? 10.714  66.840  112.058 1.00 34.81 ? 2717 HOH   A O     1 
HETATM 19231 O  O     . HOH   BA 11 .    ? -49.251 47.459  97.473  1.00 24.10 ? 2718 HOH   A O     1 
HETATM 19232 O  O     . HOH   BA 11 .    ? -26.950 51.589  98.683  1.00 23.59 ? 2719 HOH   A O     1 
HETATM 19233 O  O     . HOH   BA 11 .    ? 22.928  72.677  98.521  1.00 34.68 ? 2720 HOH   A O     1 
HETATM 19234 O  O     . HOH   BA 11 .    ? -22.676 74.773  99.706  1.00 27.28 ? 2721 HOH   A O     1 
HETATM 19235 O  O     . HOH   BA 11 .    ? 11.478  89.015  104.698 1.00 39.17 ? 2722 HOH   A O     1 
HETATM 19236 O  O     . HOH   BA 11 .    ? -36.070 71.218  121.323 1.00 33.10 ? 2723 HOH   A O     1 
HETATM 19237 O  O     . HOH   BA 11 .    ? -7.790  74.696  70.527  1.00 32.20 ? 2724 HOH   A O     1 
HETATM 19238 O  O     . HOH   BA 11 .    ? -36.840 60.290  96.337  1.00 20.05 ? 2725 HOH   A O     1 
HETATM 19239 O  O     . HOH   BA 11 .    ? -13.970 41.645  71.334  1.00 30.39 ? 2726 HOH   A O     1 
HETATM 19240 O  O     . HOH   BA 11 .    ? -61.913 67.839  89.391  1.00 38.77 ? 2727 HOH   A O     1 
HETATM 19241 O  O     . HOH   BA 11 .    ? -36.856 49.652  100.747 1.00 28.69 ? 2728 HOH   A O     1 
HETATM 19242 O  O     . HOH   BA 11 .    ? -28.581 83.565  73.256  1.00 42.75 ? 2729 HOH   A O     1 
HETATM 19243 O  O     . HOH   BA 11 .    ? -40.438 64.433  62.261  1.00 29.44 ? 2730 HOH   A O     1 
HETATM 19244 O  O     . HOH   BA 11 .    ? -4.596  58.795  118.445 1.00 22.42 ? 2731 HOH   A O     1 
HETATM 19245 O  O     . HOH   BA 11 .    ? 25.715  64.007  102.658 1.00 29.14 ? 2732 HOH   A O     1 
HETATM 19246 O  O     . HOH   BA 11 .    ? -41.774 29.391  89.503  1.00 39.52 ? 2733 HOH   A O     1 
HETATM 19247 O  O     . HOH   BA 11 .    ? -36.154 37.139  83.424  1.00 34.50 ? 2734 HOH   A O     1 
HETATM 19248 O  O     . HOH   BA 11 .    ? -45.353 65.219  52.916  1.00 36.72 ? 2735 HOH   A O     1 
HETATM 19249 O  O     . HOH   BA 11 .    ? -59.074 58.075  76.908  1.00 17.94 ? 2736 HOH   A O     1 
HETATM 19250 O  O     . HOH   BA 11 .    ? -34.574 77.189  85.029  1.00 24.39 ? 2737 HOH   A O     1 
HETATM 19251 O  O     . HOH   BA 11 .    ? -17.533 85.234  77.572  1.00 31.81 ? 2738 HOH   A O     1 
HETATM 19252 O  O     . HOH   BA 11 .    ? -44.757 85.535  100.004 1.00 42.67 ? 2739 HOH   A O     1 
HETATM 19253 O  O     . HOH   BA 11 .    ? -36.827 68.124  83.244  1.00 29.12 ? 2740 HOH   A O     1 
HETATM 19254 O  O     . HOH   BA 11 .    ? -25.733 45.711  74.674  1.00 45.67 ? 2741 HOH   A O     1 
HETATM 19255 O  O     . HOH   BA 11 .    ? -7.664  42.045  62.225  1.00 27.25 ? 2742 HOH   A O     1 
HETATM 19256 O  O     . HOH   BA 11 .    ? -21.349 58.963  122.516 1.00 29.55 ? 2743 HOH   A O     1 
HETATM 19257 O  O     . HOH   BA 11 .    ? -11.481 88.273  128.866 1.00 32.68 ? 2744 HOH   A O     1 
HETATM 19258 O  O     . HOH   BA 11 .    ? -64.605 42.737  86.166  1.00 31.45 ? 2745 HOH   A O     1 
HETATM 19259 O  O     . HOH   BA 11 .    ? 4.178   60.177  101.117 1.00 25.08 ? 2746 HOH   A O     1 
HETATM 19260 O  O     . HOH   BA 11 .    ? -8.245  81.662  105.148 1.00 21.68 ? 2747 HOH   A O     1 
HETATM 19261 O  O     . HOH   BA 11 .    ? -31.946 98.173  123.749 1.00 43.76 ? 2748 HOH   A O     1 
HETATM 19262 O  O     . HOH   BA 11 .    ? 2.552   83.786  101.813 1.00 24.47 ? 2749 HOH   A O     1 
HETATM 19263 O  O     . HOH   BA 11 .    ? -57.132 53.269  96.203  1.00 25.08 ? 2750 HOH   A O     1 
HETATM 19264 O  O     . HOH   BA 11 .    ? -42.825 28.547  86.502  1.00 40.40 ? 2751 HOH   A O     1 
HETATM 19265 O  O     . HOH   BA 11 .    ? -46.604 81.030  93.385  1.00 41.62 ? 2752 HOH   A O     1 
HETATM 19266 O  O     . HOH   BA 11 .    ? -28.479 94.732  89.097  1.00 36.63 ? 2753 HOH   A O     1 
HETATM 19267 O  O     . HOH   BA 11 .    ? -26.351 96.819  89.114  1.00 39.08 ? 2754 HOH   A O     1 
HETATM 19268 O  O     . HOH   BA 11 .    ? -44.437 31.409  84.125  1.00 28.33 ? 2755 HOH   A O     1 
HETATM 19269 O  O     . HOH   BA 11 .    ? -13.883 95.007  119.571 1.00 34.85 ? 2756 HOH   A O     1 
HETATM 19270 O  O     . HOH   BA 11 .    ? -26.301 83.981  74.217  1.00 36.89 ? 2757 HOH   A O     1 
HETATM 19271 O  O     . HOH   BA 11 .    ? -40.030 39.024  98.677  1.00 37.16 ? 2758 HOH   A O     1 
HETATM 19272 O  O     . HOH   BA 11 .    ? -1.394  79.665  88.243  1.00 37.54 ? 2759 HOH   A O     1 
HETATM 19273 O  O     . HOH   BA 11 .    ? -36.552 69.179  119.253 1.00 30.41 ? 2760 HOH   A O     1 
HETATM 19274 O  O     . HOH   BA 11 .    ? -0.166  73.819  96.266  1.00 35.80 ? 2761 HOH   A O     1 
HETATM 19275 O  O     . HOH   BA 11 .    ? -4.009  72.652  77.250  1.00 29.12 ? 2762 HOH   A O     1 
HETATM 19276 O  O     . HOH   BA 11 .    ? -47.828 58.959  82.800  1.00 15.71 ? 2763 HOH   A O     1 
HETATM 19277 O  O     . HOH   BA 11 .    ? -53.860 42.884  65.577  1.00 39.72 ? 2764 HOH   A O     1 
HETATM 19278 O  O     . HOH   BA 11 .    ? -35.173 62.897  116.049 1.00 34.34 ? 2765 HOH   A O     1 
HETATM 19279 O  O     . HOH   BA 11 .    ? -16.043 53.595  100.722 1.00 35.65 ? 2766 HOH   A O     1 
HETATM 19280 O  O     . HOH   BA 11 .    ? -38.456 73.016  90.335  1.00 32.29 ? 2767 HOH   A O     1 
HETATM 19281 O  O     . HOH   BA 11 .    ? -43.111 77.175  67.858  1.00 27.28 ? 2768 HOH   A O     1 
HETATM 19282 O  O     . HOH   BA 11 .    ? -0.190  52.319  63.241  1.00 26.94 ? 2769 HOH   A O     1 
HETATM 19283 O  O     . HOH   BA 11 .    ? -12.875 68.856  73.956  1.00 33.62 ? 2770 HOH   A O     1 
HETATM 19284 O  O     . HOH   BA 11 .    ? -44.746 60.847  85.525  1.00 17.46 ? 2771 HOH   A O     1 
HETATM 19285 O  O     . HOH   BA 11 .    ? -17.843 79.924  134.630 1.00 39.63 ? 2772 HOH   A O     1 
HETATM 19286 O  O     . HOH   BA 11 .    ? -32.190 52.040  86.142  1.00 28.27 ? 2773 HOH   A O     1 
HETATM 19287 O  O     . HOH   BA 11 .    ? -38.766 70.930  84.278  1.00 26.77 ? 2774 HOH   A O     1 
HETATM 19288 O  O     . HOH   BA 11 .    ? -12.547 65.586  112.846 1.00 18.23 ? 2775 HOH   A O     1 
HETATM 19289 O  O     . HOH   BA 11 .    ? -9.438  63.614  96.246  1.00 22.53 ? 2776 HOH   A O     1 
HETATM 19290 O  O     . HOH   BA 11 .    ? -28.082 64.502  64.292  1.00 46.37 ? 2777 HOH   A O     1 
HETATM 19291 O  O     . HOH   BA 11 .    ? -40.495 81.475  110.741 1.00 32.47 ? 2778 HOH   A O     1 
HETATM 19292 O  O     . HOH   BA 11 .    ? -47.594 53.461  104.284 1.00 45.37 ? 2779 HOH   A O     1 
HETATM 19293 O  O     . HOH   BA 11 .    ? -10.903 83.773  134.194 1.00 44.77 ? 2780 HOH   A O     1 
HETATM 19294 O  O     . HOH   BA 11 .    ? -41.571 27.522  70.340  1.00 40.34 ? 2781 HOH   A O     1 
HETATM 19295 O  O     . HOH   BA 11 .    ? -33.908 90.303  122.180 1.00 33.18 ? 2782 HOH   A O     1 
HETATM 19296 O  O     . HOH   BA 11 .    ? -64.569 70.574  83.259  1.00 38.52 ? 2783 HOH   A O     1 
HETATM 19297 O  O     . HOH   BA 11 .    ? -53.522 68.559  93.434  1.00 23.55 ? 2784 HOH   A O     1 
HETATM 19298 O  O     . HOH   BA 11 .    ? -12.334 39.767  68.486  1.00 44.49 ? 2785 HOH   A O     1 
HETATM 19299 O  O     . HOH   BA 11 .    ? -7.478  50.340  53.185  1.00 27.88 ? 2786 HOH   A O     1 
HETATM 19300 O  O     . HOH   BA 11 .    ? -38.392 70.094  81.788  1.00 21.68 ? 2787 HOH   A O     1 
HETATM 19301 O  O     . HOH   BA 11 .    ? 5.890   58.334  97.441  1.00 32.83 ? 2788 HOH   A O     1 
HETATM 19302 O  O     . HOH   BA 11 .    ? -30.548 86.528  102.143 1.00 31.25 ? 2789 HOH   A O     1 
HETATM 19303 O  O     . HOH   BA 11 .    ? -11.405 43.318  74.277  1.00 29.35 ? 2790 HOH   A O     1 
HETATM 19304 O  O     . HOH   BA 11 .    ? 7.937   88.675  127.265 1.00 35.79 ? 2791 HOH   A O     1 
HETATM 19305 O  O     . HOH   BA 11 .    ? -0.411  66.855  90.235  1.00 41.48 ? 2792 HOH   A O     1 
HETATM 19306 O  O     . HOH   BA 11 .    ? -55.499 48.881  95.210  1.00 41.14 ? 2793 HOH   A O     1 
HETATM 19307 O  O     . HOH   BA 11 .    ? -3.334  56.258  95.530  1.00 39.48 ? 2794 HOH   A O     1 
HETATM 19308 O  O     . HOH   BA 11 .    ? -8.746  51.636  107.568 1.00 29.13 ? 2795 HOH   A O     1 
HETATM 19309 O  O     . HOH   BA 11 .    ? 12.568  65.013  118.702 1.00 31.83 ? 2796 HOH   A O     1 
HETATM 19310 O  O     . HOH   BA 11 .    ? -13.384 53.900  77.389  1.00 26.93 ? 2797 HOH   A O     1 
HETATM 19311 O  O     . HOH   BA 11 .    ? -37.521 30.327  66.246  1.00 44.60 ? 2798 HOH   A O     1 
HETATM 19312 O  O     . HOH   BA 11 .    ? -45.204 57.301  102.145 1.00 29.24 ? 2799 HOH   A O     1 
HETATM 19313 O  O     . HOH   BA 11 .    ? 14.247  78.151  121.112 1.00 30.85 ? 2800 HOH   A O     1 
HETATM 19314 O  O     . HOH   BA 11 .    ? -53.620 76.027  94.227  1.00 38.76 ? 2801 HOH   A O     1 
HETATM 19315 O  O     . HOH   BA 11 .    ? -4.305  54.580  61.652  1.00 33.63 ? 2802 HOH   A O     1 
HETATM 19316 O  O     . HOH   BA 11 .    ? -37.898 67.453  98.212  1.00 25.78 ? 2803 HOH   A O     1 
HETATM 19317 O  O     . HOH   BA 11 .    ? -24.873 82.424  72.660  1.00 32.32 ? 2804 HOH   A O     1 
HETATM 19318 O  O     . HOH   BA 11 .    ? -5.279  90.333  120.006 1.00 33.32 ? 2805 HOH   A O     1 
HETATM 19319 O  O     . HOH   BA 11 .    ? 2.965   64.573  113.246 1.00 31.77 ? 2806 HOH   A O     1 
HETATM 19320 O  O     . HOH   BA 11 .    ? -59.522 62.667  77.594  1.00 21.84 ? 2807 HOH   A O     1 
HETATM 19321 O  O     . HOH   BA 11 .    ? 13.901  78.503  123.376 1.00 39.16 ? 2808 HOH   A O     1 
HETATM 19322 O  O     . HOH   BA 11 .    ? -23.130 88.793  102.275 1.00 27.41 ? 2809 HOH   A O     1 
HETATM 19323 O  O     . HOH   BA 11 .    ? -39.345 88.324  119.250 1.00 34.68 ? 2810 HOH   A O     1 
HETATM 19324 O  O     . HOH   BA 11 .    ? -55.117 26.363  91.933  1.00 35.13 ? 2811 HOH   A O     1 
HETATM 19325 O  O     . HOH   BA 11 .    ? -6.389  53.468  100.310 1.00 42.07 ? 2812 HOH   A O     1 
HETATM 19326 O  O     . HOH   BA 11 .    ? -28.171 60.023  124.943 1.00 38.91 ? 2813 HOH   A O     1 
HETATM 19327 O  O     . HOH   BA 11 .    ? 2.498   76.189  116.988 1.00 25.42 ? 2814 HOH   A O     1 
HETATM 19328 O  O     . HOH   BA 11 .    ? -17.894 70.875  106.000 1.00 30.85 ? 2815 HOH   A O     1 
HETATM 19329 O  O     . HOH   BA 11 .    ? -15.005 58.741  126.726 1.00 30.66 ? 2816 HOH   A O     1 
HETATM 19330 O  O     . HOH   BA 11 .    ? -53.564 72.036  68.177  1.00 26.24 ? 2817 HOH   A O     1 
HETATM 19331 O  O     . HOH   BA 11 .    ? -25.370 67.874  90.734  1.00 28.23 ? 2818 HOH   A O     1 
HETATM 19332 O  O     . HOH   BA 11 .    ? -35.315 97.553  116.242 1.00 38.19 ? 2819 HOH   A O     1 
HETATM 19333 O  O     . HOH   BA 11 .    ? -10.445 86.757  91.605  1.00 36.09 ? 2820 HOH   A O     1 
HETATM 19334 O  O     . HOH   BA 11 .    ? -7.445  88.780  99.812  1.00 41.58 ? 2821 HOH   A O     1 
HETATM 19335 O  O     . HOH   BA 11 .    ? -1.890  77.691  75.879  1.00 27.57 ? 2822 HOH   A O     1 
HETATM 19336 O  O     . HOH   BA 11 .    ? 1.332   66.113  96.733  1.00 22.06 ? 2823 HOH   A O     1 
HETATM 19337 O  O     . HOH   BA 11 .    ? -44.214 76.184  74.569  1.00 31.77 ? 2824 HOH   A O     1 
HETATM 19338 O  O     . HOH   BA 11 .    ? -14.823 52.840  75.760  1.00 29.47 ? 2825 HOH   A O     1 
HETATM 19339 O  O     . HOH   BA 11 .    ? -28.890 54.597  111.487 1.00 38.71 ? 2826 HOH   A O     1 
HETATM 19340 O  O     . HOH   BA 11 .    ? 8.881   64.673  94.447  1.00 27.55 ? 2827 HOH   A O     1 
HETATM 19341 O  O     . HOH   BA 11 .    ? -61.043 41.549  67.181  1.00 41.73 ? 2828 HOH   A O     1 
HETATM 19342 O  O     . HOH   BA 11 .    ? -33.456 83.331  123.301 1.00 29.69 ? 2829 HOH   A O     1 
HETATM 19343 O  O     . HOH   BA 11 .    ? -31.974 98.254  99.516  1.00 42.33 ? 2830 HOH   A O     1 
HETATM 19344 O  O     . HOH   BA 11 .    ? -26.893 79.641  70.211  1.00 39.30 ? 2831 HOH   A O     1 
HETATM 19345 O  O     . HOH   BA 11 .    ? -45.472 79.098  71.407  1.00 38.76 ? 2832 HOH   A O     1 
HETATM 19346 O  O     . HOH   BA 11 .    ? -18.274 39.293  68.577  1.00 42.33 ? 2833 HOH   A O     1 
HETATM 19347 O  O     . HOH   BA 11 .    ? 3.074   73.983  109.530 1.00 25.10 ? 2834 HOH   A O     1 
HETATM 19348 O  O     . HOH   BA 11 .    ? -3.200  82.003  97.633  1.00 24.11 ? 2835 HOH   A O     1 
HETATM 19349 O  O     . HOH   BA 11 .    ? -6.881  93.454  113.411 1.00 30.71 ? 2836 HOH   A O     1 
HETATM 19350 O  O     . HOH   BA 11 .    ? -17.112 54.590  78.515  1.00 32.01 ? 2837 HOH   A O     1 
HETATM 19351 O  O     . HOH   BA 11 .    ? -51.775 86.933  103.449 1.00 45.25 ? 2838 HOH   A O     1 
HETATM 19352 O  O     . HOH   BA 11 .    ? -30.832 83.577  123.360 1.00 25.95 ? 2839 HOH   A O     1 
HETATM 19353 O  O     . HOH   BA 11 .    ? -49.752 35.220  87.967  1.00 29.63 ? 2840 HOH   A O     1 
HETATM 19354 O  O     . HOH   BA 11 .    ? -15.865 94.471  91.565  1.00 41.23 ? 2841 HOH   A O     1 
HETATM 19355 O  O     . HOH   BA 11 .    ? -53.160 37.028  61.317  1.00 44.43 ? 2842 HOH   A O     1 
HETATM 19356 O  O     . HOH   BA 11 .    ? -38.163 72.588  87.503  1.00 32.93 ? 2843 HOH   A O     1 
HETATM 19357 O  O     . HOH   BA 11 .    ? -32.268 64.267  122.029 1.00 28.45 ? 2844 HOH   A O     1 
HETATM 19358 O  O     . HOH   BA 11 .    ? -28.018 69.135  85.919  1.00 32.56 ? 2845 HOH   A O     1 
HETATM 19359 O  O     . HOH   BA 11 .    ? -9.874  82.068  78.273  1.00 41.52 ? 2846 HOH   A O     1 
HETATM 19360 O  O     . HOH   BA 11 .    ? -1.497  54.096  101.978 1.00 22.96 ? 2847 HOH   A O     1 
HETATM 19361 O  O     . HOH   BA 11 .    ? -24.642 69.022  74.594  1.00 28.59 ? 2848 HOH   A O     1 
HETATM 19362 O  O     . HOH   BA 11 .    ? -20.800 57.969  97.342  1.00 23.06 ? 2849 HOH   A O     1 
HETATM 19363 O  O     . HOH   BA 11 .    ? -0.049  66.797  86.462  1.00 36.37 ? 2850 HOH   A O     1 
HETATM 19364 O  O     . HOH   BA 11 .    ? -25.601 93.766  78.203  1.00 34.66 ? 2851 HOH   A O     1 
HETATM 19365 O  O     . HOH   BA 11 .    ? -4.939  55.455  101.361 1.00 31.60 ? 2852 HOH   A O     1 
HETATM 19366 O  O     . HOH   BA 11 .    ? -29.449 62.259  61.900  1.00 38.01 ? 2853 HOH   A O     1 
HETATM 19367 O  O     . HOH   BA 11 .    ? -18.314 68.584  104.679 1.00 22.19 ? 2854 HOH   A O     1 
HETATM 19368 O  O     . HOH   BA 11 .    ? -25.354 59.048  114.470 1.00 26.26 ? 2855 HOH   A O     1 
HETATM 19369 O  O     . HOH   BA 11 .    ? 10.442  80.965  125.396 1.00 29.13 ? 2856 HOH   A O     1 
HETATM 19370 O  O     . HOH   BA 11 .    ? 4.684   85.727  101.098 1.00 27.19 ? 2857 HOH   A O     1 
HETATM 19371 O  O     . HOH   BA 11 .    ? -22.101 76.563  70.388  1.00 24.62 ? 2858 HOH   A O     1 
HETATM 19372 O  O     . HOH   BA 11 .    ? -0.688  77.298  126.798 1.00 37.24 ? 2859 HOH   A O     1 
HETATM 19373 O  O     . HOH   BA 11 .    ? -33.191 52.884  108.920 1.00 39.71 ? 2860 HOH   A O     1 
HETATM 19374 O  O     . HOH   BA 11 .    ? -10.292 63.348  115.684 1.00 21.51 ? 2861 HOH   A O     1 
HETATM 19375 O  O     . HOH   BA 11 .    ? 16.401  64.864  119.908 1.00 30.38 ? 2862 HOH   A O     1 
HETATM 19376 O  O     . HOH   BA 11 .    ? -62.575 67.336  66.453  1.00 29.05 ? 2863 HOH   A O     1 
HETATM 19377 O  O     . HOH   BA 11 .    ? 23.000  75.957  114.785 1.00 26.17 ? 2864 HOH   A O     1 
HETATM 19378 O  O     . HOH   BA 11 .    ? -18.607 97.361  126.767 1.00 44.35 ? 2865 HOH   A O     1 
HETATM 19379 O  O     . HOH   BA 11 .    ? -45.562 54.758  92.212  1.00 17.35 ? 2866 HOH   A O     1 
HETATM 19380 O  O     . HOH   BA 11 .    ? -2.182  62.185  113.257 1.00 33.51 ? 2867 HOH   A O     1 
HETATM 19381 O  O     . HOH   BA 11 .    ? -39.548 84.553  103.766 1.00 31.13 ? 2868 HOH   A O     1 
HETATM 19382 O  O     . HOH   BA 11 .    ? -6.419  70.595  104.386 1.00 29.95 ? 2869 HOH   A O     1 
HETATM 19383 O  O     . HOH   BA 11 .    ? -17.068 88.691  99.601  1.00 39.63 ? 2870 HOH   A O     1 
HETATM 19384 O  O     . HOH   BA 11 .    ? -39.019 66.524  94.466  1.00 27.75 ? 2871 HOH   A O     1 
HETATM 19385 O  O     . HOH   BA 11 .    ? -59.734 38.306  82.738  1.00 32.90 ? 2872 HOH   A O     1 
HETATM 19386 O  O     . HOH   BA 11 .    ? -22.536 47.855  83.302  1.00 36.17 ? 2873 HOH   A O     1 
HETATM 19387 O  O     . HOH   BA 11 .    ? -13.740 86.263  100.942 1.00 25.85 ? 2874 HOH   A O     1 
HETATM 19388 O  O     . HOH   BA 11 .    ? -56.035 36.706  92.677  1.00 37.77 ? 2875 HOH   A O     1 
HETATM 19389 O  O     . HOH   BA 11 .    ? -1.154  69.728  116.483 1.00 24.26 ? 2876 HOH   A O     1 
HETATM 19390 O  O     . HOH   BA 11 .    ? -30.483 95.618  105.076 1.00 32.82 ? 2877 HOH   A O     1 
HETATM 19391 O  O     . HOH   BA 11 .    ? -48.970 65.188  54.178  1.00 26.13 ? 2878 HOH   A O     1 
HETATM 19392 O  O     . HOH   BA 11 .    ? -64.644 54.992  80.859  1.00 23.99 ? 2879 HOH   A O     1 
HETATM 19393 O  O     . HOH   BA 11 .    ? -39.606 61.352  94.478  1.00 21.39 ? 2880 HOH   A O     1 
HETATM 19394 O  O     . HOH   BA 11 .    ? -9.153  60.204  84.407  1.00 23.01 ? 2881 HOH   A O     1 
HETATM 19395 O  O     . HOH   BA 11 .    ? -64.149 47.407  73.970  1.00 40.52 ? 2882 HOH   A O     1 
HETATM 19396 O  O     . HOH   BA 11 .    ? -48.613 78.091  75.072  1.00 32.62 ? 2883 HOH   A O     1 
HETATM 19397 O  O     . HOH   BA 11 .    ? -32.902 40.474  95.184  1.00 42.70 ? 2884 HOH   A O     1 
HETATM 19398 O  O     . HOH   BA 11 .    ? -27.268 61.620  89.029  1.00 21.08 ? 2885 HOH   A O     1 
HETATM 19399 O  O     . HOH   BA 11 .    ? 0.596   63.932  107.352 1.00 19.34 ? 2886 HOH   A O     1 
HETATM 19400 O  O     . HOH   BA 11 .    ? -39.250 86.164  89.345  1.00 28.78 ? 2887 HOH   A O     1 
HETATM 19401 O  O     . HOH   BA 11 .    ? 2.744   77.643  98.267  1.00 26.26 ? 2888 HOH   A O     1 
HETATM 19402 O  O     . HOH   BA 11 .    ? -3.421  81.918  110.168 1.00 32.52 ? 2889 HOH   A O     1 
HETATM 19403 O  O     . HOH   BA 11 .    ? -53.556 49.099  60.335  1.00 28.39 ? 2890 HOH   A O     1 
HETATM 19404 O  O     . HOH   BA 11 .    ? -2.714  75.629  77.502  1.00 21.62 ? 2891 HOH   A O     1 
HETATM 19405 O  O     . HOH   BA 11 .    ? -25.712 69.309  95.872  1.00 32.89 ? 2892 HOH   A O     1 
HETATM 19406 O  O     . HOH   BA 11 .    ? 22.322  64.973  93.303  1.00 40.11 ? 2893 HOH   A O     1 
HETATM 19407 O  O     . HOH   BA 11 .    ? -3.231  74.694  102.131 1.00 32.43 ? 2894 HOH   A O     1 
HETATM 19408 O  O     . HOH   BA 11 .    ? -1.903  90.723  105.766 1.00 27.88 ? 2895 HOH   A O     1 
HETATM 19409 O  O     . HOH   BA 11 .    ? -43.962 88.759  113.340 1.00 47.33 ? 2896 HOH   A O     1 
HETATM 19410 O  O     . HOH   BA 11 .    ? -36.016 44.034  66.504  1.00 37.51 ? 2897 HOH   A O     1 
HETATM 19411 O  O     . HOH   BA 11 .    ? -56.185 68.617  100.083 1.00 36.98 ? 2898 HOH   A O     1 
HETATM 19412 O  O     . HOH   BA 11 .    ? -22.635 94.332  118.289 1.00 33.05 ? 2899 HOH   A O     1 
HETATM 19413 O  O     . HOH   BA 11 .    ? -58.962 42.226  89.543  1.00 37.50 ? 2900 HOH   A O     1 
HETATM 19414 O  O     . HOH   BA 11 .    ? -42.602 77.398  78.429  1.00 23.82 ? 2901 HOH   A O     1 
HETATM 19415 O  O     . HOH   BA 11 .    ? 1.420   62.010  111.400 1.00 29.93 ? 2902 HOH   A O     1 
HETATM 19416 O  O     . HOH   BA 11 .    ? -63.772 52.779  90.044  1.00 34.00 ? 2903 HOH   A O     1 
HETATM 19417 O  O     . HOH   BA 11 .    ? -11.084 53.712  100.589 1.00 26.86 ? 2904 HOH   A O     1 
HETATM 19418 O  O     . HOH   BA 11 .    ? 1.869   85.985  98.849  1.00 39.18 ? 2905 HOH   A O     1 
HETATM 19419 O  O     . HOH   BA 11 .    ? -16.856 54.251  117.160 1.00 34.53 ? 2906 HOH   A O     1 
HETATM 19420 O  O     . HOH   BA 11 .    ? -6.013  70.581  106.384 1.00 34.26 ? 2907 HOH   A O     1 
HETATM 19421 O  O     . HOH   BA 11 .    ? -46.858 76.896  92.078  1.00 25.67 ? 2908 HOH   A O     1 
HETATM 19422 O  O     . HOH   BA 11 .    ? -12.191 81.378  72.764  1.00 39.51 ? 2909 HOH   A O     1 
HETATM 19423 O  O     . HOH   BA 11 .    ? -32.635 77.639  93.074  1.00 37.60 ? 2910 HOH   A O     1 
HETATM 19424 O  O     . HOH   BA 11 .    ? -21.881 66.864  73.973  1.00 38.99 ? 2911 HOH   A O     1 
HETATM 19425 O  O     . HOH   BA 11 .    ? 12.959  88.362  116.356 1.00 33.66 ? 2912 HOH   A O     1 
HETATM 19426 O  O     . HOH   BA 11 .    ? -10.269 63.930  125.163 1.00 38.22 ? 2913 HOH   A O     1 
HETATM 19427 O  O     . HOH   BA 11 .    ? -60.587 40.644  81.162  1.00 40.52 ? 2914 HOH   A O     1 
HETATM 19428 O  O     . HOH   BA 11 .    ? -30.530 49.995  104.798 1.00 30.81 ? 2915 HOH   A O     1 
HETATM 19429 O  O     . HOH   BA 11 .    ? -23.265 85.973  73.771  1.00 37.88 ? 2916 HOH   A O     1 
HETATM 19430 O  O     . HOH   BA 11 .    ? -64.195 57.777  67.175  1.00 35.62 ? 2917 HOH   A O     1 
HETATM 19431 O  O     . HOH   BA 11 .    ? -36.045 80.345  75.564  1.00 25.20 ? 2918 HOH   A O     1 
HETATM 19432 O  O     . HOH   BA 11 .    ? 7.227   54.926  98.941  1.00 20.09 ? 2919 HOH   A O     1 
HETATM 19433 O  O     . HOH   BA 11 .    ? -33.000 57.125  72.552  1.00 33.76 ? 2920 HOH   A O     1 
HETATM 19434 O  O     . HOH   BA 11 .    ? -12.628 53.324  110.785 1.00 35.69 ? 2921 HOH   A O     1 
HETATM 19435 O  O     . HOH   BA 11 .    ? -66.377 68.422  83.937  1.00 27.48 ? 2922 HOH   A O     1 
HETATM 19436 O  O     . HOH   BA 11 .    ? -14.041 57.888  110.045 1.00 38.23 ? 2923 HOH   A O     1 
HETATM 19437 O  O     . HOH   BA 11 .    ? -30.497 91.112  111.434 1.00 33.97 ? 2924 HOH   A O     1 
HETATM 19438 O  O     . HOH   BA 11 .    ? -1.234  80.257  112.046 1.00 31.24 ? 2925 HOH   A O     1 
HETATM 19439 O  O     . HOH   BA 11 .    ? -49.907 72.670  62.809  1.00 21.71 ? 2926 HOH   A O     1 
HETATM 19440 O  O     . HOH   BA 11 .    ? -34.894 36.457  69.050  1.00 45.68 ? 2927 HOH   A O     1 
HETATM 19441 O  O     . HOH   BA 11 .    ? -43.022 49.439  55.839  1.00 31.84 ? 2928 HOH   A O     1 
HETATM 19442 O  O     . HOH   BA 11 .    ? -26.696 62.632  86.601  1.00 23.70 ? 2929 HOH   A O     1 
HETATM 19443 O  O     . HOH   BA 11 .    ? 18.563  74.909  96.673  1.00 34.83 ? 2930 HOH   A O     1 
HETATM 19444 O  O     . HOH   BA 11 .    ? 11.235  60.907  115.287 1.00 31.35 ? 2931 HOH   A O     1 
HETATM 19445 O  O     . HOH   BA 11 .    ? 1.453   56.920  107.727 1.00 20.38 ? 2932 HOH   A O     1 
HETATM 19446 O  O     . HOH   BA 11 .    ? -22.138 54.295  97.292  1.00 31.64 ? 2933 HOH   A O     1 
HETATM 19447 O  O     . HOH   BA 11 .    ? 21.795  72.508  116.081 1.00 26.95 ? 2934 HOH   A O     1 
HETATM 19448 O  O     . HOH   BA 11 .    ? -37.862 39.222  100.130 1.00 42.27 ? 2935 HOH   A O     1 
HETATM 19449 O  O     . HOH   BA 11 .    ? -0.118  67.327  117.757 1.00 33.08 ? 2936 HOH   A O     1 
HETATM 19450 O  O     . HOH   BA 11 .    ? -22.922 54.793  88.667  1.00 37.07 ? 2937 HOH   A O     1 
HETATM 19451 O  O     . HOH   BA 11 .    ? -41.616 64.281  58.513  1.00 26.12 ? 2938 HOH   A O     1 
HETATM 19452 O  O     . HOH   BA 11 .    ? -18.974 69.009  66.114  1.00 49.64 ? 2939 HOH   A O     1 
HETATM 19453 O  O     . HOH   BA 11 .    ? -2.902  85.426  124.785 1.00 34.69 ? 2940 HOH   A O     1 
HETATM 19454 O  O     . HOH   BA 11 .    ? -43.484 90.283  100.000 1.00 33.15 ? 2941 HOH   A O     1 
HETATM 19455 O  O     . HOH   BA 11 .    ? -13.916 55.590  111.541 1.00 32.88 ? 2942 HOH   A O     1 
HETATM 19456 O  O     . HOH   BA 11 .    ? -43.999 69.257  109.110 1.00 37.22 ? 2943 HOH   A O     1 
HETATM 19457 O  O     . HOH   BA 11 .    ? -18.726 59.444  108.234 1.00 32.87 ? 2944 HOH   A O     1 
HETATM 19458 O  O     . HOH   BA 11 .    ? -52.293 29.674  73.118  1.00 41.36 ? 2945 HOH   A O     1 
HETATM 19459 O  O     . HOH   BA 11 .    ? -14.808 89.717  98.765  1.00 40.25 ? 2946 HOH   A O     1 
HETATM 19460 O  O     . HOH   BA 11 .    ? 12.974  63.310  121.010 1.00 34.88 ? 2947 HOH   A O     1 
HETATM 19461 O  O     . HOH   BA 11 .    ? 22.262  78.590  115.381 1.00 40.20 ? 2948 HOH   A O     1 
HETATM 19462 O  O     . HOH   BA 11 .    ? -56.647 39.978  67.687  1.00 36.02 ? 2949 HOH   A O     1 
HETATM 19463 O  O     . HOH   BA 11 .    ? -43.035 56.051  92.055  1.00 17.18 ? 2950 HOH   A O     1 
HETATM 19464 O  O     . HOH   BA 11 .    ? 2.523   86.174  126.302 1.00 38.68 ? 2951 HOH   A O     1 
HETATM 19465 O  O     . HOH   BA 11 .    ? -19.077 75.628  103.939 1.00 33.61 ? 2952 HOH   A O     1 
HETATM 19466 O  O     . HOH   BA 11 .    ? -41.480 88.304  93.929  1.00 36.64 ? 2953 HOH   A O     1 
HETATM 19467 O  O     . HOH   BA 11 .    ? -27.078 90.110  115.740 1.00 26.73 ? 2954 HOH   A O     1 
HETATM 19468 O  O     . HOH   BA 11 .    ? -56.682 73.171  96.223  1.00 35.23 ? 2955 HOH   A O     1 
HETATM 19469 O  O     . HOH   BA 11 .    ? -67.689 64.024  85.380  1.00 33.52 ? 2956 HOH   A O     1 
HETATM 19470 O  O     . HOH   BA 11 .    ? -34.326 55.024  71.380  1.00 37.86 ? 2957 HOH   A O     1 
HETATM 19471 O  O     . HOH   BA 11 .    ? -56.355 24.976  88.488  1.00 39.54 ? 2958 HOH   A O     1 
HETATM 19472 O  O     . HOH   BA 11 .    ? -65.752 72.073  71.852  1.00 39.64 ? 2959 HOH   A O     1 
HETATM 19473 O  O     . HOH   BA 11 .    ? 11.275  84.817  124.748 1.00 25.55 ? 2960 HOH   A O     1 
HETATM 19474 O  O     . HOH   BA 11 .    ? -3.460  78.557  93.567  1.00 33.43 ? 2961 HOH   A O     1 
HETATM 19475 O  O     . HOH   BA 11 .    ? -21.378 52.621  88.864  1.00 37.57 ? 2962 HOH   A O     1 
HETATM 19476 O  O     . HOH   BA 11 .    ? -12.973 40.591  55.743  1.00 43.37 ? 2963 HOH   A O     1 
HETATM 19477 O  O     . HOH   BA 11 .    ? -30.173 54.006  57.904  1.00 42.93 ? 2964 HOH   A O     1 
HETATM 19478 O  O     . HOH   BA 11 .    ? 21.009  75.269  100.402 1.00 35.90 ? 2965 HOH   A O     1 
HETATM 19479 O  O     . HOH   BA 11 .    ? -65.072 57.554  71.448  1.00 36.47 ? 2966 HOH   A O     1 
HETATM 19480 O  O     . HOH   BA 11 .    ? -30.773 65.945  126.810 1.00 37.95 ? 2967 HOH   A O     1 
HETATM 19481 O  O     . HOH   BA 11 .    ? -64.371 47.312  76.383  1.00 37.69 ? 2968 HOH   A O     1 
HETATM 19482 O  O     . HOH   BA 11 .    ? -46.340 51.672  72.152  1.00 27.12 ? 2969 HOH   A O     1 
HETATM 19483 O  O     . HOH   BA 11 .    ? -63.014 62.011  97.815  1.00 33.33 ? 2970 HOH   A O     1 
HETATM 19484 O  O     . HOH   BA 11 .    ? -1.812  79.727  97.478  1.00 28.28 ? 2971 HOH   A O     1 
HETATM 19485 O  O     . HOH   BA 11 .    ? -51.824 77.310  101.509 1.00 39.16 ? 2972 HOH   A O     1 
HETATM 19486 O  O     . HOH   BA 11 .    ? 18.961  71.006  92.253  1.00 43.47 ? 2973 HOH   A O     1 
HETATM 19487 O  O     . HOH   BA 11 .    ? -39.967 47.063  106.585 1.00 39.62 ? 2974 HOH   A O     1 
HETATM 19488 O  O     . HOH   BA 11 .    ? -37.209 65.152  108.709 1.00 36.91 ? 2975 HOH   A O     1 
HETATM 19489 O  O     . HOH   BA 11 .    ? -20.291 54.419  99.053  1.00 29.02 ? 2976 HOH   A O     1 
HETATM 19490 O  O     . HOH   BA 11 .    ? -33.307 60.081  82.815  1.00 42.01 ? 2977 HOH   A O     1 
HETATM 19491 O  O     . HOH   BA 11 .    ? -61.933 59.737  95.876  1.00 26.50 ? 2978 HOH   A O     1 
HETATM 19492 O  O     . HOH   BA 11 .    ? -22.854 67.185  129.758 1.00 39.26 ? 2979 HOH   A O     1 
HETATM 19493 O  O     . HOH   BA 11 .    ? -31.424 40.957  98.202  1.00 38.20 ? 2980 HOH   A O     1 
HETATM 19494 O  O     . HOH   BA 11 .    ? -37.810 40.181  74.404  1.00 34.66 ? 2981 HOH   A O     1 
HETATM 19495 O  O     . HOH   BA 11 .    ? -40.015 37.753  85.250  1.00 30.88 ? 2982 HOH   A O     1 
HETATM 19496 O  O     . HOH   BA 11 .    ? -16.252 42.866  72.073  1.00 38.20 ? 2983 HOH   A O     1 
HETATM 19497 O  O     . HOH   BA 11 .    ? -36.409 82.310  120.798 1.00 30.33 ? 2984 HOH   A O     1 
HETATM 19498 O  O     . HOH   BA 11 .    ? -18.096 92.051  107.909 1.00 35.14 ? 2985 HOH   A O     1 
HETATM 19499 O  O     . HOH   BA 11 .    ? -61.241 61.370  62.645  1.00 32.19 ? 2986 HOH   A O     1 
HETATM 19500 O  O     . HOH   BA 11 .    ? -43.879 37.164  104.930 1.00 38.10 ? 2987 HOH   A O     1 
HETATM 19501 O  O     . HOH   BA 11 .    ? -0.592  52.296  59.167  1.00 35.26 ? 2988 HOH   A O     1 
HETATM 19502 O  O     . HOH   BA 11 .    ? 2.967   66.382  120.417 1.00 40.31 ? 2989 HOH   A O     1 
HETATM 19503 O  O     . HOH   BA 11 .    ? -53.639 39.715  66.650  1.00 38.86 ? 2990 HOH   A O     1 
HETATM 19504 O  O     . HOH   BA 11 .    ? -38.412 57.601  75.398  1.00 39.25 ? 2991 HOH   A O     1 
HETATM 19505 O  O     . HOH   BA 11 .    ? -37.335 85.873  101.921 1.00 27.06 ? 2992 HOH   A O     1 
HETATM 19506 O  O     . HOH   BA 11 .    ? -52.795 66.213  102.039 1.00 37.88 ? 2993 HOH   A O     1 
HETATM 19507 O  O     . HOH   BA 11 .    ? -10.762 66.483  127.577 1.00 36.74 ? 2994 HOH   A O     1 
HETATM 19508 O  O     . HOH   BA 11 .    ? -57.013 32.031  87.901  1.00 26.36 ? 2995 HOH   A O     1 
HETATM 19509 O  O     . HOH   BA 11 .    ? -49.569 54.060  74.048  1.00 20.85 ? 2996 HOH   A O     1 
HETATM 19510 O  O     . HOH   BA 11 .    ? -61.921 66.825  60.579  1.00 36.23 ? 2997 HOH   A O     1 
HETATM 19511 O  O     . HOH   BA 11 .    ? -26.652 39.004  77.366  1.00 43.08 ? 2998 HOH   A O     1 
HETATM 19512 O  O     . HOH   BA 11 .    ? -21.010 50.036  108.611 1.00 38.56 ? 2999 HOH   A O     1 
HETATM 19513 O  O     . HOH   BA 11 .    ? 23.612  57.976  103.588 1.00 33.31 ? 3000 HOH   A O     1 
HETATM 19514 O  O     . HOH   BA 11 .    ? -43.231 28.311  68.882  1.00 40.98 ? 3001 HOH   A O     1 
HETATM 19515 O  O     . HOH   BA 11 .    ? -0.612  74.460  116.808 1.00 29.80 ? 3002 HOH   A O     1 
HETATM 19516 O  O     . HOH   BA 11 .    ? -37.244 75.168  97.616  1.00 28.34 ? 3003 HOH   A O     1 
HETATM 19517 O  O     . HOH   BA 11 .    ? -35.051 70.505  82.570  1.00 36.59 ? 3004 HOH   A O     1 
HETATM 19518 O  O     . HOH   BA 11 .    ? -32.316 44.471  103.259 1.00 41.21 ? 3005 HOH   A O     1 
HETATM 19519 O  O     . HOH   BA 11 .    ? 19.533  64.175  93.319  1.00 30.89 ? 3006 HOH   A O     1 
HETATM 19520 O  O     . HOH   BA 11 .    ? -6.177  61.816  69.325  1.00 43.48 ? 3007 HOH   A O     1 
HETATM 19521 O  O     . HOH   BA 11 .    ? -54.206 44.914  92.106  1.00 30.95 ? 3008 HOH   A O     1 
HETATM 19522 O  O     . HOH   BA 11 .    ? -8.868  83.523  81.197  1.00 42.17 ? 3009 HOH   A O     1 
HETATM 19523 O  O     . HOH   BA 11 .    ? -25.924 74.404  132.666 1.00 30.69 ? 3010 HOH   A O     1 
HETATM 19524 O  O     . HOH   BA 11 .    ? -23.369 75.734  133.440 1.00 33.06 ? 3011 HOH   A O     1 
HETATM 19525 O  O     . HOH   BA 11 .    ? -8.867  40.877  69.426  1.00 34.39 ? 3012 HOH   A O     1 
HETATM 19526 O  O     . HOH   BA 11 .    ? -67.219 57.223  90.075  1.00 42.31 ? 3013 HOH   A O     1 
HETATM 19527 O  O     . HOH   BA 11 .    ? -3.730  57.604  63.627  1.00 42.75 ? 3014 HOH   A O     1 
HETATM 19528 O  O     . HOH   BA 11 .    ? -31.461 94.050  127.196 1.00 37.98 ? 3015 HOH   A O     1 
HETATM 19529 O  O     . HOH   BA 11 .    ? -19.375 70.281  132.791 1.00 37.07 ? 3016 HOH   A O     1 
HETATM 19530 O  O     . HOH   BA 11 .    ? -47.696 79.852  95.739  1.00 36.72 ? 3017 HOH   A O     1 
HETATM 19531 O  O     . HOH   BA 11 .    ? -55.262 41.636  96.816  1.00 41.82 ? 3018 HOH   A O     1 
HETATM 19532 O  O     . HOH   BA 11 .    ? -44.104 91.233  111.369 1.00 35.65 ? 3019 HOH   A O     1 
HETATM 19533 O  O     . HOH   BA 11 .    ? -31.051 77.928  91.016  1.00 34.30 ? 3020 HOH   A O     1 
HETATM 19534 O  O     . HOH   BA 11 .    ? 11.095  64.893  114.341 1.00 36.97 ? 3021 HOH   A O     1 
HETATM 19535 O  O     . HOH   BA 11 .    ? -29.511 58.348  79.134  1.00 33.87 ? 3022 HOH   A O     1 
HETATM 19536 O  O     . HOH   BA 11 .    ? -30.915 59.008  82.063  1.00 46.18 ? 3023 HOH   A O     1 
HETATM 19537 O  O     . HOH   BA 11 .    ? 0.133   87.101  124.485 1.00 33.01 ? 3024 HOH   A O     1 
HETATM 19538 O  O     . HOH   BA 11 .    ? 15.083  82.233  119.461 1.00 29.60 ? 3025 HOH   A O     1 
HETATM 19539 O  O     . HOH   BA 11 .    ? -14.773 47.811  51.631  1.00 37.94 ? 3026 HOH   A O     1 
HETATM 19540 O  O     . HOH   BA 11 .    ? -54.224 61.906  103.616 1.00 40.98 ? 3027 HOH   A O     1 
HETATM 19541 O  O     . HOH   BA 11 .    ? 11.653  78.921  124.709 1.00 43.33 ? 3028 HOH   A O     1 
HETATM 19542 O  O     . HOH   BA 11 .    ? -39.547 46.876  103.981 1.00 35.32 ? 3029 HOH   A O     1 
HETATM 19543 O  O     . HOH   BA 11 .    ? 21.230  70.968  94.998  1.00 38.16 ? 3030 HOH   A O     1 
HETATM 19544 O  O     . HOH   BA 11 .    ? 8.121   79.096  125.763 1.00 41.60 ? 3031 HOH   A O     1 
HETATM 19545 O  O     . HOH   BA 11 .    ? -17.964 53.611  98.741  1.00 31.24 ? 3032 HOH   A O     1 
HETATM 19546 O  O     . HOH   BA 11 .    ? -66.034 64.129  88.069  1.00 31.94 ? 3033 HOH   A O     1 
HETATM 19547 O  O     . HOH   BA 11 .    ? -26.878 60.428  122.709 1.00 31.83 ? 3034 HOH   A O     1 
HETATM 19548 O  O     . HOH   BA 11 .    ? -57.017 63.358  105.079 1.00 45.37 ? 3035 HOH   A O     1 
HETATM 19549 O  O     . HOH   BA 11 .    ? -41.767 24.170  81.629  1.00 46.98 ? 3036 HOH   A O     1 
HETATM 19550 O  O     . HOH   BA 11 .    ? -26.987 68.862  103.534 1.00 34.16 ? 3037 HOH   A O     1 
HETATM 19551 O  O     . HOH   BA 11 .    ? -57.776 72.134  88.384  1.00 39.42 ? 3038 HOH   A O     1 
HETATM 19552 O  O     . HOH   BA 11 .    ? -37.208 74.867  64.269  1.00 38.84 ? 3039 HOH   A O     1 
HETATM 19553 O  O     . HOH   BA 11 .    ? -55.725 36.149  96.674  1.00 44.49 ? 3040 HOH   A O     1 
HETATM 19554 O  O     . HOH   BA 11 .    ? -45.044 92.282  98.726  1.00 40.19 ? 3041 HOH   A O     1 
HETATM 19555 O  O     . HOH   BA 11 .    ? -42.228 85.065  105.273 1.00 35.09 ? 3042 HOH   A O     1 
HETATM 19556 O  O     . HOH   BA 11 .    ? 26.182  73.972  98.195  1.00 42.43 ? 3043 HOH   A O     1 
HETATM 19557 O  O     . HOH   BA 11 .    ? -57.751 33.062  71.975  1.00 44.62 ? 3044 HOH   A O     1 
HETATM 19558 O  O     . HOH   BA 11 .    ? 1.182   69.237  87.635  1.00 33.01 ? 3045 HOH   A O     1 
HETATM 19559 O  O     . HOH   BA 11 .    ? -45.717 78.081  89.955  1.00 23.78 ? 3046 HOH   A O     1 
HETATM 19560 O  O     . HOH   BA 11 .    ? -50.373 54.571  104.848 1.00 39.05 ? 3047 HOH   A O     1 
HETATM 19561 O  O     . HOH   BA 11 .    ? -35.498 59.754  88.676  1.00 31.62 ? 3048 HOH   A O     1 
HETATM 19562 O  O     . HOH   BA 11 .    ? -51.260 79.488  78.634  1.00 38.75 ? 3049 HOH   A O     1 
HETATM 19563 O  O     . HOH   BA 11 .    ? -27.438 51.049  109.765 1.00 40.28 ? 3050 HOH   A O     1 
HETATM 19564 O  O     . HOH   BA 11 .    ? -3.846  59.803  68.670  1.00 44.26 ? 3051 HOH   A O     1 
HETATM 19565 O  O     . HOH   BA 11 .    ? -9.167  72.937  131.824 1.00 38.43 ? 3052 HOH   A O     1 
HETATM 19566 O  O     . HOH   BA 11 .    ? -44.505 92.610  88.878  1.00 45.67 ? 3053 HOH   A O     1 
HETATM 19567 O  O     . HOH   BA 11 .    ? -5.613  74.706  103.302 1.00 28.98 ? 3054 HOH   A O     1 
HETATM 19568 O  O     . HOH   BA 11 .    ? -41.625 89.316  115.615 1.00 44.32 ? 3055 HOH   A O     1 
HETATM 19569 O  O     . HOH   BA 11 .    ? -36.412 76.252  95.294  1.00 37.45 ? 3056 HOH   A O     1 
HETATM 19570 O  O     . HOH   BA 11 .    ? -23.775 100.173 101.125 1.00 40.70 ? 3057 HOH   A O     1 
HETATM 19571 O  O     . HOH   BA 11 .    ? -60.550 59.297  62.189  1.00 31.49 ? 3058 HOH   A O     1 
HETATM 19572 O  O     . HOH   BA 11 .    ? -5.368  47.011  55.835  1.00 36.94 ? 3059 HOH   A O     1 
HETATM 19573 O  O     . HOH   BA 11 .    ? -67.935 70.186  73.608  1.00 32.74 ? 3060 HOH   A O     1 
HETATM 19574 O  O     . HOH   BA 11 .    ? -61.002 72.419  81.692  1.00 37.82 ? 3061 HOH   A O     1 
HETATM 19575 O  O     . HOH   BA 11 .    ? -40.835 68.731  63.209  1.00 40.62 ? 3062 HOH   A O     1 
HETATM 19576 O  O     . HOH   BA 11 .    ? 16.441  64.340  116.980 1.00 41.20 ? 3063 HOH   A O     1 
HETATM 19577 O  O     . HOH   BA 11 .    ? 17.090  86.614  112.069 1.00 42.76 ? 3064 HOH   A O     1 
HETATM 19578 O  O     . HOH   BA 11 .    ? -63.335 64.570  63.164  1.00 41.40 ? 3065 HOH   A O     1 
HETATM 19579 O  O     . HOH   BA 11 .    ? -31.763 67.581  101.415 1.00 34.04 ? 3066 HOH   A O     1 
HETATM 19580 O  O     . HOH   BA 11 .    ? -67.183 65.360  69.795  1.00 43.04 ? 3067 HOH   A O     1 
HETATM 19581 O  O     . HOH   BA 11 .    ? 8.280   69.604  125.130 1.00 44.73 ? 3068 HOH   A O     1 
HETATM 19582 O  O     . HOH   BA 11 .    ? -60.907 68.732  91.947  1.00 39.68 ? 3069 HOH   A O     1 
HETATM 19583 O  O     . HOH   BA 11 .    ? -34.043 58.861  106.311 1.00 29.98 ? 3070 HOH   A O     1 
HETATM 19584 O  O     . HOH   BA 11 .    ? -26.567 47.860  101.926 1.00 41.90 ? 3071 HOH   A O     1 
HETATM 19585 O  O     . HOH   BA 11 .    ? -52.686 56.756  73.867  1.00 26.80 ? 3072 HOH   A O     1 
HETATM 19586 O  O     . HOH   BA 11 .    ? -64.069 50.797  73.311  1.00 37.00 ? 3073 HOH   A O     1 
HETATM 19587 O  O     . HOH   BA 11 .    ? -9.949  66.507  74.592  1.00 32.63 ? 3074 HOH   A O     1 
HETATM 19588 O  O     . HOH   BA 11 .    ? -48.556 30.462  69.296  1.00 42.77 ? 3075 HOH   A O     1 
HETATM 19589 O  O     . HOH   BA 11 .    ? -65.918 54.608  78.433  1.00 34.78 ? 3076 HOH   A O     1 
HETATM 19590 O  O     . HOH   BA 11 .    ? -22.478 73.959  69.849  1.00 32.96 ? 3077 HOH   A O     1 
HETATM 19591 O  O     . HOH   BA 11 .    ? 6.948   91.144  118.622 1.00 34.86 ? 3078 HOH   A O     1 
HETATM 19592 O  O     . HOH   BA 11 .    ? -50.526 23.775  80.954  1.00 40.90 ? 3079 HOH   A O     1 
HETATM 19593 O  O     . HOH   BA 11 .    ? -19.008 52.757  114.812 1.00 48.09 ? 3080 HOH   A O     1 
HETATM 19594 O  O     . HOH   BA 11 .    ? -44.515 69.259  111.265 1.00 37.30 ? 3081 HOH   A O     1 
HETATM 19595 O  O     . HOH   BA 11 .    ? -39.945 67.497  89.076  1.00 31.31 ? 3082 HOH   A O     1 
HETATM 19596 O  O     . HOH   BA 11 .    ? -16.338 98.263  127.676 1.00 51.89 ? 3083 HOH   A O     1 
HETATM 19597 O  O     . HOH   BA 11 .    ? -1.259  91.789  109.383 1.00 29.77 ? 3084 HOH   A O     1 
HETATM 19598 O  O     . HOH   BA 11 .    ? -51.800 54.942  70.545  1.00 26.01 ? 3085 HOH   A O     1 
HETATM 19599 O  O     . HOH   BA 11 .    ? -47.651 32.900  85.650  1.00 40.41 ? 3086 HOH   A O     1 
HETATM 19600 O  O     . HOH   BA 11 .    ? -63.949 65.056  66.640  1.00 35.56 ? 3087 HOH   A O     1 
HETATM 19601 O  O     . HOH   BA 11 .    ? -46.239 62.855  53.761  1.00 38.09 ? 3088 HOH   A O     1 
HETATM 19602 O  O     . HOH   BA 11 .    ? -44.026 81.349  71.412  1.00 42.05 ? 3089 HOH   A O     1 
HETATM 19603 O  O     . HOH   BA 11 .    ? -48.530 26.855  75.007  1.00 42.61 ? 3090 HOH   A O     1 
HETATM 19604 O  O     . HOH   BA 11 .    ? -64.803 56.858  94.359  1.00 41.79 ? 3091 HOH   A O     1 
HETATM 19605 O  O     . HOH   BA 11 .    ? -18.643 59.304  111.081 1.00 25.44 ? 3092 HOH   A O     1 
HETATM 19606 O  O     . HOH   BA 11 .    ? -47.635 63.645  56.175  1.00 29.66 ? 3093 HOH   A O     1 
HETATM 19607 O  O     . HOH   BA 11 .    ? -30.530 48.943  86.428  1.00 38.65 ? 3094 HOH   A O     1 
HETATM 19608 O  O     . HOH   BA 11 .    ? -7.389  72.683  103.637 1.00 31.90 ? 3095 HOH   A O     1 
HETATM 19609 O  O     . HOH   BA 11 .    ? -42.003 75.200  120.430 1.00 41.47 ? 3096 HOH   A O     1 
HETATM 19610 O  O     . HOH   BA 11 .    ? 5.429   70.940  96.204  1.00 37.30 ? 3097 HOH   A O     1 
HETATM 19611 O  O     . HOH   BA 11 .    ? -37.836 70.540  86.592  1.00 37.14 ? 3098 HOH   A O     1 
HETATM 19612 O  O     . HOH   BA 11 .    ? -10.681 60.542  127.942 1.00 35.66 ? 3099 HOH   A O     1 
HETATM 19613 O  O     . HOH   BA 11 .    ? -44.689 87.845  99.606  1.00 42.16 ? 3100 HOH   A O     1 
HETATM 19614 O  O     . HOH   BA 11 .    ? -28.578 57.326  88.803  1.00 30.25 ? 3101 HOH   A O     1 
HETATM 19615 O  O     . HOH   BA 11 .    ? -28.437 67.124  93.064  1.00 45.47 ? 3102 HOH   A O     1 
HETATM 19616 O  O     . HOH   BA 11 .    ? -64.268 62.897  68.546  1.00 34.17 ? 3103 HOH   A O     1 
HETATM 19617 O  O     . HOH   BA 11 .    ? -15.218 57.467  106.278 1.00 34.57 ? 3104 HOH   A O     1 
HETATM 19618 O  O     . HOH   BA 11 .    ? -11.017 40.625  57.722  1.00 42.24 ? 3105 HOH   A O     1 
HETATM 19619 O  O     . HOH   BA 11 .    ? -59.754 63.968  92.305  1.00 30.09 ? 3106 HOH   A O     1 
HETATM 19620 O  O     . HOH   BA 11 .    ? -9.831  90.068  127.921 1.00 38.93 ? 3107 HOH   A O     1 
HETATM 19621 O  O     . HOH   BA 11 .    ? -18.808 54.233  118.667 1.00 38.73 ? 3108 HOH   A O     1 
HETATM 19622 O  O     . HOH   BA 11 .    ? -53.475 50.641  101.311 1.00 41.19 ? 3109 HOH   A O     1 
HETATM 19623 O  O     . HOH   BA 11 .    ? 7.809   62.260  112.556 1.00 33.35 ? 3110 HOH   A O     1 
HETATM 19624 O  O     . HOH   BA 11 .    ? -40.754 46.604  59.789  1.00 37.57 ? 3111 HOH   A O     1 
HETATM 19625 O  O     . HOH   BA 11 .    ? -47.409 85.441  111.885 1.00 44.98 ? 3112 HOH   A O     1 
HETATM 19626 O  O     . HOH   BA 11 .    ? -34.014 61.004  86.483  1.00 37.72 ? 3113 HOH   A O     1 
HETATM 19627 O  O     . HOH   BA 11 .    ? -40.984 66.430  70.789  1.00 33.76 ? 3114 HOH   A O     1 
HETATM 19628 O  O     . HOH   BA 11 .    ? -55.183 57.508  102.366 1.00 30.25 ? 3115 HOH   A O     1 
HETATM 19629 O  O     . HOH   BA 11 .    ? -55.386 27.532  81.926  1.00 40.68 ? 3116 HOH   A O     1 
HETATM 19630 O  O     . HOH   BA 11 .    ? -24.492 93.994  108.276 1.00 48.03 ? 3117 HOH   A O     1 
HETATM 19631 O  O     . HOH   BA 11 .    ? 12.757  63.907  116.738 1.00 36.64 ? 3118 HOH   A O     1 
HETATM 19632 O  O     . HOH   BA 11 .    ? -32.528 95.019  110.997 1.00 43.67 ? 3119 HOH   A O     1 
HETATM 19633 O  O     . HOH   BA 11 .    ? -20.003 52.727  105.872 1.00 40.90 ? 3120 HOH   A O     1 
HETATM 19634 O  O     . HOH   BA 11 .    ? 12.610  88.220  118.996 1.00 38.06 ? 3121 HOH   A O     1 
HETATM 19635 O  O     . HOH   BA 11 .    ? -24.731 100.164 91.595  1.00 41.97 ? 3122 HOH   A O     1 
HETATM 19636 O  O     . HOH   BA 11 .    ? -26.805 65.330  102.849 1.00 31.29 ? 3123 HOH   A O     1 
HETATM 19637 O  O     . HOH   BA 11 .    ? -39.428 77.858  121.591 1.00 45.27 ? 3124 HOH   A O     1 
HETATM 19638 O  O     . HOH   BA 11 .    ? -3.185  67.786  93.003  1.00 40.98 ? 3125 HOH   A O     1 
HETATM 19639 O  O     . HOH   BA 11 .    ? -53.375 40.102  63.344  1.00 41.56 ? 3126 HOH   A O     1 
HETATM 19640 O  O     . HOH   BA 11 .    ? -53.873 42.429  60.898  1.00 47.81 ? 3127 HOH   A O     1 
HETATM 19641 O  O     . HOH   BA 11 .    ? -32.869 83.922  76.997  1.00 29.49 ? 3128 HOH   A O     1 
HETATM 19642 O  O     . HOH   BA 11 .    ? -22.748 70.984  74.045  1.00 35.66 ? 3129 HOH   A O     1 
HETATM 19643 O  O     . HOH   BA 11 .    ? -46.847 30.679  72.948  1.00 37.90 ? 3130 HOH   A O     1 
HETATM 19644 O  O     . HOH   BA 11 .    ? -46.104 56.505  54.561  1.00 36.32 ? 3131 HOH   A O     1 
HETATM 19645 O  O     . HOH   BA 11 .    ? -10.358 63.341  127.794 1.00 39.29 ? 3132 HOH   A O     1 
HETATM 19646 O  O     . HOH   BA 11 .    ? -27.564 63.613  90.854  1.00 35.30 ? 3133 HOH   A O     1 
HETATM 19647 O  O     . HOH   BA 11 .    ? -11.245 63.773  51.363  1.00 42.65 ? 3134 HOH   A O     1 
HETATM 19648 O  O     . HOH   BA 11 .    ? -6.866  65.481  92.805  1.00 37.32 ? 3135 HOH   A O     1 
HETATM 19649 O  O     . HOH   BA 11 .    ? -39.258 35.498  88.872  1.00 35.43 ? 3136 HOH   A O     1 
HETATM 19650 O  O     . HOH   BA 11 .    ? -25.903 67.089  94.221  1.00 37.77 ? 3137 HOH   A O     1 
HETATM 19651 O  O     . HOH   BA 11 .    ? -23.210 54.880  52.207  1.00 42.60 ? 3138 HOH   A O     1 
HETATM 19652 O  O     . HOH   BA 11 .    ? -28.693 65.716  129.019 1.00 41.88 ? 3139 HOH   A O     1 
HETATM 19653 O  O     . HOH   BA 11 .    ? -21.595 54.361  118.219 1.00 45.13 ? 3140 HOH   A O     1 
HETATM 19654 O  O     . HOH   BA 11 .    ? -43.768 24.430  80.461  1.00 45.51 ? 3141 HOH   A O     1 
HETATM 19655 O  O     . HOH   BA 11 .    ? -21.062 98.960  98.317  1.00 41.84 ? 3142 HOH   A O     1 
HETATM 19656 O  O     . HOH   BA 11 .    ? -2.553  56.595  70.889  1.00 31.49 ? 3143 HOH   A O     1 
HETATM 19657 O  O     . HOH   BA 11 .    ? -24.477 65.171  96.891  1.00 37.81 ? 3144 HOH   A O     1 
HETATM 19658 O  O     . HOH   BA 11 .    ? -9.852  66.500  132.339 1.00 36.50 ? 3145 HOH   A O     1 
HETATM 19659 O  O     . HOH   BA 11 .    ? -43.669 87.867  92.956  1.00 45.99 ? 3146 HOH   A O     1 
HETATM 19660 O  O     . HOH   BA 11 .    ? -50.953 67.941  108.151 1.00 37.98 ? 3147 HOH   A O     1 
HETATM 19661 O  O     . HOH   BA 11 .    ? -56.864 44.436  92.434  1.00 38.75 ? 3148 HOH   A O     1 
HETATM 19662 O  O     . HOH   BA 11 .    ? -11.179 49.617  78.540  1.00 45.72 ? 3149 HOH   A O     1 
HETATM 19663 O  O     . HOH   BA 11 .    ? -39.272 75.615  122.332 1.00 40.70 ? 3150 HOH   A O     1 
HETATM 19664 O  O     . HOH   BA 11 .    ? 5.001   60.294  98.432  1.00 25.28 ? 3151 HOH   A O     1 
HETATM 19665 O  O     . HOH   BA 11 .    ? -20.967 92.707  107.159 1.00 33.34 ? 3152 HOH   A O     1 
HETATM 19666 O  O     . HOH   BA 11 .    ? -52.578 51.112  104.106 1.00 45.50 ? 3153 HOH   A O     1 
HETATM 19667 O  O     . HOH   BA 11 .    ? -58.196 46.204  64.185  1.00 45.33 ? 3154 HOH   A O     1 
HETATM 19668 O  O     . HOH   BA 11 .    ? -50.805 80.881  83.700  1.00 41.82 ? 3155 HOH   A O     1 
HETATM 19669 O  O     . HOH   BA 11 .    ? 2.475   83.553  129.524 1.00 44.15 ? 3156 HOH   A O     1 
HETATM 19670 O  O     . HOH   BA 11 .    ? -8.942  66.948  129.624 1.00 34.77 ? 3157 HOH   A O     1 
HETATM 19671 O  O     . HOH   BA 11 .    ? -11.451 59.566  106.762 1.00 33.60 ? 3158 HOH   A O     1 
HETATM 19672 O  O     . HOH   BA 11 .    ? -67.638 62.084  68.879  1.00 43.72 ? 3159 HOH   A O     1 
HETATM 19673 O  O     . HOH   BA 11 .    ? -31.673 74.043  83.754  1.00 26.35 ? 3160 HOH   A O     1 
HETATM 19674 O  O     . HOH   BA 11 .    ? -58.902 30.527  86.646  1.00 33.46 ? 3161 HOH   A O     1 
HETATM 19675 O  O     . HOH   BA 11 .    ? -56.121 31.606  92.480  1.00 42.62 ? 3162 HOH   A O     1 
HETATM 19676 O  O     . HOH   BA 11 .    ? -45.127 84.676  90.346  1.00 45.73 ? 3163 HOH   A O     1 
HETATM 19677 O  O     . HOH   BA 11 .    ? -5.558  90.153  98.927  1.00 44.63 ? 3164 HOH   A O     1 
HETATM 19678 O  O     . HOH   BA 11 .    ? -45.420 28.606  87.192  1.00 38.68 ? 3165 HOH   A O     1 
HETATM 19679 O  O     . HOH   BA 11 .    ? -35.304 73.244  86.623  1.00 33.51 ? 3166 HOH   A O     1 
HETATM 19680 O  O     . HOH   BA 11 .    ? -6.722  54.827  82.788  1.00 27.90 ? 3167 HOH   A O     1 
HETATM 19681 O  O     . HOH   BA 11 .    ? -9.200  92.297  125.646 1.00 45.26 ? 3168 HOH   A O     1 
HETATM 19682 O  O     . HOH   BA 11 .    ? -10.399 78.343  92.475  1.00 20.23 ? 3169 HOH   A O     1 
HETATM 19683 O  O     . HOH   BA 11 .    ? -44.275 61.406  104.864 1.00 47.02 ? 3170 HOH   A O     1 
HETATM 19684 O  O     . HOH   BA 11 .    ? -45.461 55.265  104.220 1.00 43.14 ? 3171 HOH   A O     1 
HETATM 19685 O  O     . HOH   BA 11 .    ? -62.910 61.038  93.559  1.00 34.78 ? 3172 HOH   A O     1 
HETATM 19686 O  O     . HOH   BA 11 .    ? -14.649 51.913  112.438 1.00 42.14 ? 3173 HOH   A O     1 
HETATM 19687 O  O     . HOH   BA 11 .    ? -58.334 74.434  94.930  1.00 41.48 ? 3174 HOH   A O     1 
HETATM 19688 O  O     . HOH   BA 11 .    ? -17.035 96.723  92.170  1.00 37.89 ? 3175 HOH   A O     1 
HETATM 19689 O  O     . HOH   BA 11 .    ? -34.444 75.860  87.350  1.00 29.41 ? 3176 HOH   A O     1 
HETATM 19690 O  O     . HOH   BA 11 .    ? -52.259 73.822  61.947  1.00 22.12 ? 3177 HOH   A O     1 
HETATM 19691 O  O     . HOH   BA 11 .    ? -44.125 23.055  78.611  1.00 46.14 ? 3178 HOH   A O     1 
HETATM 19692 O  O     . HOH   BA 11 .    ? -52.629 66.482  104.884 1.00 39.80 ? 3179 HOH   A O     1 
HETATM 19693 O  O     . HOH   BA 11 .    ? -52.353 63.788  100.792 1.00 31.07 ? 3180 HOH   A O     1 
HETATM 19694 O  O     . HOH   BA 11 .    ? -9.828  93.658  114.078 1.00 39.33 ? 3181 HOH   A O     1 
HETATM 19695 O  O     . HOH   BA 11 .    ? -16.953 49.941  77.004  1.00 41.60 ? 3182 HOH   A O     1 
HETATM 19696 O  O     . HOH   BA 11 .    ? -34.932 54.691  107.481 1.00 33.03 ? 3183 HOH   A O     1 
HETATM 19697 O  O     . HOH   BA 11 .    ? -56.303 74.433  79.296  1.00 31.96 ? 3184 HOH   A O     1 
HETATM 19698 O  O     . HOH   BA 11 .    ? -29.127 60.456  120.983 1.00 38.41 ? 3185 HOH   A O     1 
HETATM 19699 O  O     . HOH   BA 11 .    ? -52.577 48.225  57.952  1.00 36.09 ? 3186 HOH   A O     1 
HETATM 19700 O  O     . HOH   BA 11 .    ? -66.972 54.271  82.276  1.00 29.76 ? 3187 HOH   A O     1 
HETATM 19701 O  O     . HOH   BA 11 .    ? 16.237  82.998  116.567 1.00 38.09 ? 3188 HOH   A O     1 
HETATM 19702 O  O     . HOH   BA 11 .    ? -31.238 76.065  74.477  1.00 31.90 ? 3189 HOH   A O     1 
HETATM 19703 O  O     . HOH   BA 11 .    ? 17.254  83.640  112.997 1.00 36.65 ? 3190 HOH   A O     1 
HETATM 19704 O  O     . HOH   BA 11 .    ? -16.830 57.134  110.376 1.00 39.35 ? 3191 HOH   A O     1 
HETATM 19705 O  O     . HOH   BA 11 .    ? -34.791 38.806  94.688  1.00 36.28 ? 3192 HOH   A O     1 
HETATM 19706 O  O     . HOH   BA 11 .    ? -6.278  86.451  88.726  1.00 44.10 ? 3193 HOH   A O     1 
HETATM 19707 O  O     . HOH   BA 11 .    ? 6.821   66.593  93.868  1.00 35.14 ? 3194 HOH   A O     1 
HETATM 19708 O  O     . HOH   BA 11 .    ? 16.327  66.216  90.362  1.00 39.89 ? 3195 HOH   A O     1 
HETATM 19709 O  O     . HOH   BA 11 .    ? -39.192 69.990  118.256 1.00 36.35 ? 3196 HOH   A O     1 
HETATM 19710 O  O     . HOH   BA 11 .    ? -44.320 83.151  85.981  1.00 44.05 ? 3197 HOH   A O     1 
HETATM 19711 O  O     . HOH   BA 11 .    ? -8.360  61.250  86.943  1.00 38.78 ? 3198 HOH   A O     1 
HETATM 19712 O  O     . HOH   BA 11 .    ? 4.094   76.156  95.393  1.00 43.84 ? 3199 HOH   A O     1 
HETATM 19713 O  O     . HOH   BA 11 .    ? -36.048 90.244  123.639 1.00 39.20 ? 3200 HOH   A O     1 
HETATM 19714 O  O     . HOH   BA 11 .    ? -14.179 95.631  114.571 1.00 45.03 ? 3201 HOH   A O     1 
HETATM 19715 O  O     . HOH   BA 11 .    ? -25.883 82.898  69.928  1.00 43.14 ? 3202 HOH   A O     1 
HETATM 19716 O  O     . HOH   BA 11 .    ? -66.745 72.432  77.712  1.00 42.89 ? 3203 HOH   A O     1 
HETATM 19717 O  O     . HOH   BA 11 .    ? -24.252 96.885  121.201 1.00 45.34 ? 3204 HOH   A O     1 
HETATM 19718 O  O     . HOH   BA 11 .    ? -67.006 65.785  83.322  1.00 24.37 ? 3205 HOH   A O     1 
HETATM 19719 O  O     . HOH   BA 11 .    ? 6.667   81.011  127.339 1.00 35.78 ? 3206 HOH   A O     1 
HETATM 19720 O  O     . HOH   BA 11 .    ? -26.851 93.027  110.279 1.00 41.17 ? 3207 HOH   A O     1 
HETATM 19721 O  O     . HOH   BA 11 .    ? -41.781 63.793  106.292 1.00 39.54 ? 3208 HOH   A O     1 
HETATM 19722 O  O     . HOH   BA 11 .    ? -66.324 66.833  66.568  1.00 47.87 ? 3209 HOH   A O     1 
HETATM 19723 O  O     . HOH   BA 11 .    ? -35.429 38.758  89.908  1.00 42.41 ? 3210 HOH   A O     1 
HETATM 19724 O  O     . HOH   BA 11 .    ? -37.176 62.881  114.166 1.00 34.05 ? 3211 HOH   A O     1 
HETATM 19725 O  O     . HOH   BA 11 .    ? -36.130 37.522  86.726  1.00 43.18 ? 3212 HOH   A O     1 
HETATM 19726 O  O     . HOH   BA 11 .    ? -25.528 47.811  56.015  1.00 46.71 ? 3213 HOH   A O     1 
HETATM 19727 O  O     . HOH   BA 11 .    ? 2.336   74.702  119.480 1.00 39.05 ? 3214 HOH   A O     1 
HETATM 19728 O  O     . HOH   BA 11 .    ? -23.893 77.406  68.375  1.00 39.83 ? 3215 HOH   A O     1 
HETATM 19729 O  O     . HOH   BA 11 .    ? -12.795 52.836  79.521  1.00 40.39 ? 3216 HOH   A O     1 
HETATM 19730 O  O     . HOH   BA 11 .    ? -37.672 49.186  105.279 1.00 46.06 ? 3217 HOH   A O     1 
HETATM 19731 O  O     . HOH   BA 11 .    ? -58.172 32.058  90.344  1.00 28.73 ? 3218 HOH   A O     1 
HETATM 19732 O  O     . HOH   BA 11 .    ? 20.491  61.410  96.429  1.00 32.64 ? 3219 HOH   A O     1 
HETATM 19733 O  O     . HOH   BA 11 .    ? -36.033 62.830  90.440  1.00 36.76 ? 3220 HOH   A O     1 
HETATM 19734 O  O     . HOH   BA 11 .    ? -37.878 74.216  93.491  1.00 37.44 ? 3221 HOH   A O     1 
HETATM 19735 O  O     . HOH   BA 11 .    ? 11.140  90.534  119.717 1.00 41.01 ? 3222 HOH   A O     1 
HETATM 19736 O  O     . HOH   BA 11 .    ? -30.351 79.232  125.745 1.00 41.29 ? 3223 HOH   A O     1 
HETATM 19737 O  O     . HOH   BA 11 .    ? -10.762 68.707  136.394 1.00 44.39 ? 3224 HOH   A O     1 
HETATM 19738 O  O     . HOH   BA 11 .    ? 10.465  68.128  114.397 1.00 33.84 ? 3225 HOH   A O     1 
HETATM 19739 O  O     . HOH   BA 11 .    ? -44.721 82.250  88.837  1.00 41.54 ? 3226 HOH   A O     1 
HETATM 19740 O  O     . HOH   BA 11 .    ? -33.599 80.380  74.639  1.00 30.67 ? 3227 HOH   A O     1 
HETATM 19741 O  O     . HOH   BA 11 .    ? -63.599 48.647  71.992  1.00 40.45 ? 3228 HOH   A O     1 
HETATM 19742 O  O     . HOH   BA 11 .    ? -22.696 91.048  103.776 1.00 36.53 ? 3229 HOH   A O     1 
HETATM 19743 O  O     . HOH   BA 11 .    ? -27.072 58.990  116.345 1.00 37.75 ? 3230 HOH   A O     1 
HETATM 19744 O  O     . HOH   BA 11 .    ? -30.474 70.222  87.792  1.00 45.70 ? 3231 HOH   A O     1 
HETATM 19745 O  O     . HOH   BA 11 .    ? -34.149 42.761  67.776  1.00 44.18 ? 3232 HOH   A O     1 
HETATM 19746 O  O     . HOH   BA 11 .    ? -15.116 53.399  105.198 1.00 43.37 ? 3233 HOH   A O     1 
HETATM 19747 O  O     . HOH   BA 11 .    ? -33.552 80.724  122.731 1.00 30.20 ? 3234 HOH   A O     1 
HETATM 19748 O  O     . HOH   BA 11 .    ? 19.256  80.102  118.670 1.00 43.64 ? 3235 HOH   A O     1 
HETATM 19749 O  O     . HOH   BA 11 .    ? -13.342 60.145  86.924  1.00 41.61 ? 3236 HOH   A O     1 
HETATM 19750 O  O     . HOH   BA 11 .    ? -2.905  58.662  127.590 1.00 46.81 ? 3237 HOH   A O     1 
HETATM 19751 O  O     . HOH   BA 11 .    ? -54.810 24.826  80.802  1.00 44.12 ? 3238 HOH   A O     1 
HETATM 19752 O  O     . HOH   BA 11 .    ? -40.970 68.326  93.510  1.00 30.87 ? 3239 HOH   A O     1 
HETATM 19753 O  O     . HOH   BA 11 .    ? -27.819 48.967  104.359 1.00 40.45 ? 3240 HOH   A O     1 
HETATM 19754 O  O     . HOH   BA 11 .    ? -25.411 64.936  91.707  1.00 38.92 ? 3241 HOH   A O     1 
HETATM 19755 O  O     . HOH   BA 11 .    ? -24.872 97.078  126.261 1.00 44.45 ? 3242 HOH   A O     1 
HETATM 19756 O  O     . HOH   BA 11 .    ? -4.885  81.595  129.168 1.00 45.99 ? 3243 HOH   A O     1 
HETATM 19757 O  O     . HOH   BA 11 .    ? -53.005 68.784  100.834 1.00 29.93 ? 3244 HOH   A O     1 
HETATM 19758 O  O     . HOH   BA 11 .    ? -0.435  79.273  94.990  1.00 43.34 ? 3245 HOH   A O     1 
HETATM 19759 O  O     . HOH   BA 11 .    ? -18.397 74.243  109.335 1.00 22.82 ? 3246 HOH   A O     1 
HETATM 19760 O  O     . HOH   BA 11 .    ? -9.287  73.408  129.312 1.00 34.79 ? 3247 HOH   A O     1 
HETATM 19761 O  O     . HOH   BA 11 .    ? -62.483 53.589  65.878  1.00 33.82 ? 3248 HOH   A O     1 
HETATM 19762 O  O     . HOH   BA 11 .    ? -66.806 47.199  73.706  1.00 35.68 ? 3249 HOH   A O     1 
HETATM 19763 O  O     . HOH   BA 11 .    ? -58.690 55.411  101.034 1.00 41.58 ? 3250 HOH   A O     1 
HETATM 19764 O  O     . HOH   BA 11 .    ? -53.230 45.676  94.681  1.00 37.08 ? 3251 HOH   A O     1 
HETATM 19765 O  O     . HOH   BA 11 .    ? -56.320 49.037  97.716  1.00 41.71 ? 3252 HOH   A O     1 
HETATM 19766 O  O     . HOH   BA 11 .    ? -20.730 91.469  136.775 1.00 47.29 ? 3253 HOH   A O     1 
HETATM 19767 O  O     . HOH   BA 11 .    ? -10.642 65.752  72.586  1.00 41.50 ? 3254 HOH   A O     1 
HETATM 19768 O  O     . HOH   BA 11 .    ? 3.884   64.574  96.465  1.00 27.27 ? 3255 HOH   A O     1 
HETATM 19769 O  O     . HOH   BA 11 .    ? -25.372 61.975  102.290 1.00 31.93 ? 3256 HOH   A O     1 
HETATM 19770 O  O     . HOH   BA 11 .    ? 8.861   89.940  105.478 1.00 42.04 ? 3257 HOH   A O     1 
HETATM 19771 O  O     . HOH   BA 11 .    ? -8.640  52.624  101.188 1.00 37.75 ? 3258 HOH   A O     1 
HETATM 19772 O  O     . HOH   BA 11 .    ? -12.847 52.008  99.386  1.00 43.60 ? 3259 HOH   A O     1 
HETATM 19773 O  O     . HOH   BA 11 .    ? 18.407  64.137  90.588  1.00 39.53 ? 3260 HOH   A O     1 
HETATM 19774 O  O     . HOH   BA 11 .    ? -3.901  79.784  124.989 1.00 33.16 ? 3261 HOH   A O     1 
HETATM 19775 O  O     . HOH   BA 11 .    ? 10.984  79.382  128.903 1.00 33.77 ? 3262 HOH   A O     1 
HETATM 19776 O  O     . HOH   BA 11 .    ? -48.282 56.502  56.015  1.00 32.58 ? 3263 HOH   A O     1 
HETATM 19777 O  O     . HOH   BA 11 .    ? -51.948 72.921  102.716 1.00 30.05 ? 3264 HOH   A O     1 
HETATM 19778 O  O     . HOH   BA 11 .    ? -4.285  95.888  119.525 1.00 50.04 ? 3265 HOH   A O     1 
HETATM 19779 O  O     . HOH   BA 11 .    ? 0.963   71.125  117.563 1.00 35.40 ? 3266 HOH   A O     1 
HETATM 19780 O  O     . HOH   BA 11 .    ? -69.752 61.303  72.732  1.00 26.82 ? 3267 HOH   A O     1 
HETATM 19781 O  O     . HOH   BA 11 .    ? -8.627  57.257  84.479  1.00 37.24 ? 3268 HOH   A O     1 
HETATM 19782 O  O     . HOH   BA 11 .    ? 20.887  70.467  118.910 1.00 37.77 ? 3269 HOH   A O     1 
HETATM 19783 O  O     . HOH   BA 11 .    ? -36.676 82.123  77.302  1.00 36.55 ? 3270 HOH   A O     1 
HETATM 19784 O  O     . HOH   BA 11 .    ? 8.975   65.379  111.565 1.00 41.14 ? 3271 HOH   A O     1 
HETATM 19785 O  O     . HOH   BA 11 .    ? -1.941  73.514  118.885 1.00 35.77 ? 3272 HOH   A O     1 
HETATM 19786 O  O     . HOH   BA 11 .    ? -60.234 44.810  90.435  1.00 37.20 ? 3273 HOH   A O     1 
HETATM 19787 O  O     . HOH   BA 11 .    ? -13.541 95.893  117.157 1.00 39.14 ? 3274 HOH   A O     1 
HETATM 19788 O  O     . HOH   BA 11 .    ? -46.672 80.610  89.963  1.00 36.30 ? 3275 HOH   A O     1 
HETATM 19789 O  O     . HOH   BA 11 .    ? -41.023 82.398  68.758  1.00 33.01 ? 3276 HOH   A O     1 
HETATM 19790 O  O     . HOH   BA 11 .    ? 23.129  69.920  115.914 1.00 27.99 ? 3277 HOH   A O     1 
HETATM 19791 O  O     . HOH   BA 11 .    ? -56.725 72.706  99.057  1.00 39.79 ? 3278 HOH   A O     1 
HETATM 19792 O  O     . HOH   BA 11 .    ? -7.355  64.106  67.686  1.00 51.36 ? 3279 HOH   A O     1 
HETATM 19793 O  O     . HOH   BA 11 .    ? -29.300 92.140  108.909 1.00 35.70 ? 3280 HOH   A O     1 
HETATM 19794 O  O     . HOH   BA 11 .    ? -48.785 77.306  93.832  1.00 36.59 ? 3281 HOH   A O     1 
HETATM 19795 O  O     . HOH   BA 11 .    ? 1.380   58.697  114.432 1.00 44.49 ? 3282 HOH   A O     1 
HETATM 19796 O  O     . HOH   BA 11 .    ? -33.651 76.052  89.823  1.00 42.18 ? 3283 HOH   A O     1 
HETATM 19797 O  O     . HOH   BA 11 .    ? 3.126   68.459  94.911  1.00 40.48 ? 3284 HOH   A O     1 
HETATM 19798 O  O     . HOH   BA 11 .    ? -6.163  61.860  93.586  1.00 46.02 ? 3285 HOH   A O     1 
HETATM 19799 O  O     . HOH   BA 11 .    ? -0.556  60.442  112.562 1.00 34.77 ? 3286 HOH   A O     1 
HETATM 19800 O  O     . HOH   BA 11 .    ? -52.444 38.460  102.150 1.00 46.34 ? 3287 HOH   A O     1 
HETATM 19801 O  O     . HOH   BA 11 .    ? -18.497 70.613  69.286  1.00 42.97 ? 3288 HOH   A O     1 
HETATM 19802 O  O     . HOH   BA 11 .    ? -54.549 54.479  102.245 1.00 37.53 ? 3289 HOH   A O     1 
HETATM 19803 O  O     . HOH   BA 11 .    ? -2.152  91.640  98.477  1.00 29.35 ? 3290 HOH   A O     1 
HETATM 19804 O  O     . HOH   BA 11 .    ? -31.982 75.118  85.518  1.00 35.71 ? 3291 HOH   A O     1 
HETATM 19805 O  O     . HOH   BA 11 .    ? -55.414 45.853  65.294  1.00 38.10 ? 3292 HOH   A O     1 
HETATM 19806 O  O     . HOH   BA 11 .    ? -26.690 66.280  98.149  1.00 34.56 ? 3293 HOH   A O     1 
HETATM 19807 O  O     . HOH   BA 11 .    ? -28.644 77.349  70.383  1.00 32.53 ? 3294 HOH   A O     1 
HETATM 19808 O  O     . HOH   BA 11 .    ? -31.706 54.491  110.878 1.00 40.99 ? 3295 HOH   A O     1 
HETATM 19809 O  O     . HOH   BA 11 .    ? -33.118 58.042  113.631 1.00 39.99 ? 3296 HOH   A O     1 
HETATM 19810 O  O     . HOH   BA 11 .    ? -9.849  48.817  107.264 1.00 37.69 ? 3297 HOH   A O     1 
HETATM 19811 O  O     . HOH   BA 11 .    ? -47.958 37.107  100.482 1.00 35.30 ? 3298 HOH   A O     1 
HETATM 19812 O  O     . HOH   BA 11 .    ? -9.293  62.160  94.163  1.00 32.47 ? 3299 HOH   A O     1 
HETATM 19813 O  O     . HOH   BA 11 .    ? -62.651 55.219  69.933  1.00 25.84 ? 3300 HOH   A O     1 
HETATM 19814 O  O     . HOH   BA 11 .    ? -54.823 41.432  99.845  1.00 44.92 ? 3301 HOH   A O     1 
HETATM 19815 O  O     . HOH   BA 11 .    ? -18.659 46.521  53.270  1.00 34.99 ? 3302 HOH   A O     1 
HETATM 19816 O  O     . HOH   BA 11 .    ? -8.569  76.388  129.548 1.00 37.36 ? 3303 HOH   A O     1 
HETATM 19817 O  O     . HOH   BA 11 .    ? 6.862   62.387  94.868  1.00 26.84 ? 3304 HOH   A O     1 
HETATM 19818 O  O     . HOH   BA 11 .    ? -0.290  85.846  96.928  1.00 38.72 ? 3305 HOH   A O     1 
HETATM 19819 O  O     . HOH   BA 11 .    ? -46.967 34.886  103.568 1.00 42.77 ? 3306 HOH   A O     1 
HETATM 19820 O  O     . HOH   BA 11 .    ? 25.025  62.820  100.470 1.00 39.54 ? 3307 HOH   A O     1 
HETATM 19821 O  O     . HOH   BA 11 .    ? -67.045 38.797  73.985  1.00 38.75 ? 3308 HOH   A O     1 
HETATM 19822 O  O     . HOH   BA 11 .    ? -20.104 74.527  101.901 1.00 31.95 ? 3309 HOH   A O     1 
HETATM 19823 O  O     . HOH   BA 11 .    ? -18.376 73.620  106.307 1.00 25.19 ? 3310 HOH   A O     1 
HETATM 19824 O  O     . HOH   BA 11 .    ? -44.003 28.365  90.596  1.00 44.86 ? 3311 HOH   A O     1 
HETATM 19825 O  O     . HOH   BA 11 .    ? -53.856 79.462  77.168  1.00 45.10 ? 3312 HOH   A O     1 
HETATM 19826 O  O     . HOH   BA 11 .    ? -29.960 59.940  86.006  1.00 34.29 ? 3313 HOH   A O     1 
HETATM 19827 O  O     . HOH   BA 11 .    ? -31.007 83.774  73.523  1.00 35.86 ? 3314 HOH   A O     1 
HETATM 19828 O  O     . HOH   BA 11 .    ? -20.645 52.541  101.386 1.00 38.93 ? 3315 HOH   A O     1 
HETATM 19829 O  O     . HOH   BA 11 .    ? -32.334 65.324  124.651 1.00 32.28 ? 3316 HOH   A O     1 
HETATM 19830 O  O     . HOH   BA 11 .    ? -63.336 57.477  96.443  1.00 37.48 ? 3317 HOH   A O     1 
HETATM 19831 O  O     . HOH   BA 11 .    ? -8.546  70.526  132.647 1.00 45.12 ? 3318 HOH   A O     1 
HETATM 19832 O  O     . HOH   BA 11 .    ? -24.554 51.841  100.119 1.00 33.04 ? 3319 HOH   A O     1 
HETATM 19833 O  O     . HOH   BA 11 .    ? 25.280  76.122  113.410 1.00 33.33 ? 3320 HOH   A O     1 
HETATM 19834 O  O     . HOH   BA 11 .    ? -21.877 68.494  132.140 1.00 40.36 ? 3321 HOH   A O     1 
HETATM 19835 O  O     . HOH   BA 11 .    ? -24.054 50.220  95.582  1.00 35.57 ? 3322 HOH   A O     1 
HETATM 19836 O  O     . HOH   BA 11 .    ? -29.258 59.704  88.674  1.00 23.37 ? 3323 HOH   A O     1 
HETATM 19837 O  O     . HOH   BA 11 .    ? -54.403 80.105  84.225  1.00 44.27 ? 3324 HOH   A O     1 
HETATM 19838 O  O     . HOH   BA 11 .    ? -3.264  83.186  112.445 1.00 29.43 ? 3325 HOH   A O     1 
HETATM 19839 O  O     . HOH   BA 11 .    ? -19.085 57.379  106.802 1.00 28.41 ? 3326 HOH   A O     1 
HETATM 19840 O  O     . HOH   BA 11 .    ? -56.614 75.906  76.960  1.00 27.06 ? 3327 HOH   A O     1 
HETATM 19841 O  O     . HOH   BA 11 .    ? 2.567   70.845  95.478  1.00 42.22 ? 3328 HOH   A O     1 
HETATM 19842 O  O     . HOH   BA 11 .    ? 24.079  57.685  100.779 1.00 35.64 ? 3329 HOH   A O     1 
HETATM 19843 O  O     . HOH   BA 11 .    ? -22.947 51.955  97.518  1.00 37.84 ? 3330 HOH   A O     1 
HETATM 19844 O  O     . HOH   BA 11 .    ? -7.377  68.926  130.140 1.00 42.90 ? 3331 HOH   A O     1 
HETATM 19845 O  O     . HOH   BA 11 .    ? -20.523 89.377  138.219 1.00 43.54 ? 3332 HOH   A O     1 
HETATM 19846 O  O     . HOH   BA 11 .    ? -61.591 50.358  66.533  1.00 41.06 ? 3333 HOH   A O     1 
HETATM 19847 O  O     . HOH   BA 11 .    ? 3.813   68.920  88.465  1.00 35.54 ? 3334 HOH   A O     1 
HETATM 19848 O  O     . HOH   BA 11 .    ? -32.687 58.413  84.886  1.00 39.65 ? 3335 HOH   A O     1 
HETATM 19849 O  O     . HOH   BA 11 .    ? -1.737  74.854  121.076 1.00 34.58 ? 3336 HOH   A O     1 
HETATM 19850 O  O     . HOH   BA 11 .    ? -65.193 56.045  69.623  1.00 36.49 ? 3337 HOH   A O     1 
HETATM 19851 O  O     . HOH   BA 11 .    ? -61.471 70.419  85.747  1.00 31.98 ? 3338 HOH   A O     1 
HETATM 19852 O  O     . HOH   BA 11 .    ? 12.749  62.184  93.306  1.00 32.43 ? 3339 HOH   A O     1 
HETATM 19853 O  O     . HOH   BA 11 .    ? -51.851 47.028  96.553  1.00 31.10 ? 3340 HOH   A O     1 
HETATM 19854 O  O     . HOH   BA 11 .    ? -35.531 39.056  104.621 1.00 48.06 ? 3341 HOH   A O     1 
HETATM 19855 O  O     . HOH   BA 11 .    ? -56.753 52.277  98.775  1.00 33.44 ? 3342 HOH   A O     1 
HETATM 19856 O  O     . HOH   BA 11 .    ? -61.737 52.697  94.000  1.00 37.11 ? 3343 HOH   A O     1 
HETATM 19857 O  O     . HOH   BA 11 .    ? -58.843 73.859  82.312  1.00 42.73 ? 3344 HOH   A O     1 
HETATM 19858 O  O     . HOH   BA 11 .    ? -17.275 55.859  123.012 1.00 44.90 ? 3345 HOH   A O     1 
HETATM 19859 O  O     . HOH   BA 11 .    ? -56.475 76.012  81.010  1.00 37.08 ? 3346 HOH   A O     1 
HETATM 19860 O  O     . HOH   BA 11 .    ? -22.057 64.429  132.322 1.00 40.89 ? 3347 HOH   A O     1 
HETATM 19861 O  O     . HOH   BA 11 .    ? -12.308 61.490  105.215 1.00 32.21 ? 3348 HOH   A O     1 
HETATM 19862 O  O     . HOH   BA 11 .    ? -57.160 27.857  92.498  1.00 36.10 ? 3349 HOH   A O     1 
HETATM 19863 O  O     . HOH   BA 11 .    ? -2.313  84.620  96.697  1.00 34.34 ? 3350 HOH   A O     1 
HETATM 19864 O  O     . HOH   BA 11 .    ? -54.970 52.685  100.528 1.00 35.05 ? 3351 HOH   A O     1 
HETATM 19865 O  O     . HOH   BA 11 .    ? -35.114 84.034  76.837  1.00 44.40 ? 3352 HOH   A O     1 
HETATM 19866 O  O     . HOH   BA 11 .    ? -34.751 63.614  121.621 1.00 40.15 ? 3353 HOH   A O     1 
HETATM 19867 O  O     . HOH   BA 11 .    ? -35.673 39.316  73.449  1.00 41.37 ? 3354 HOH   A O     1 
HETATM 19868 O  O     . HOH   BA 11 .    ? -15.158 39.036  70.791  1.00 44.00 ? 3355 HOH   A O     1 
HETATM 19869 O  O     . HOH   BA 11 .    ? -55.006 42.026  63.035  1.00 46.23 ? 3356 HOH   A O     1 
HETATM 19870 O  O     . HOH   BA 11 .    ? -37.957 69.025  95.695  1.00 35.06 ? 3357 HOH   A O     1 
HETATM 19871 O  O     . HOH   BA 11 .    ? -39.468 83.052  76.398  1.00 42.19 ? 3358 HOH   A O     1 
HETATM 19872 O  O     . HOH   BA 11 .    ? -46.299 38.824  104.569 1.00 33.69 ? 3359 HOH   A O     1 
HETATM 19873 O  O     . HOH   BA 11 .    ? -25.072 62.586  99.835  1.00 30.20 ? 3360 HOH   A O     1 
HETATM 19874 O  O     . HOH   BA 11 .    ? 22.835  62.949  95.231  1.00 42.14 ? 3361 HOH   A O     1 
HETATM 19875 O  O     . HOH   BA 11 .    ? -7.127  61.135  90.808  1.00 45.41 ? 3362 HOH   A O     1 
HETATM 19876 O  O     . HOH   BA 11 .    ? -19.447 55.643  123.309 1.00 42.45 ? 3363 HOH   A O     1 
HETATM 19877 O  O     . HOH   BA 11 .    ? -31.585 61.369  121.978 1.00 35.63 ? 3364 HOH   A O     1 
HETATM 19878 O  O     . HOH   BA 11 .    ? -39.168 71.750  95.734  1.00 34.33 ? 3365 HOH   A O     1 
HETATM 19879 O  O     . HOH   BA 11 .    ? 11.381  64.328  93.267  1.00 32.67 ? 3366 HOH   A O     1 
HETATM 19880 O  O     . HOH   BA 11 .    ? -68.047 62.980  89.658  1.00 44.32 ? 3367 HOH   A O     1 
HETATM 19881 O  O     . HOH   BA 11 .    ? 12.141  91.110  115.909 1.00 46.21 ? 3368 HOH   A O     1 
HETATM 19882 O  O     . HOH   BA 11 .    ? 13.996  65.751  90.655  1.00 36.57 ? 3369 HOH   A O     1 
HETATM 19883 O  O     . HOH   BA 11 .    ? -33.011 57.018  110.971 1.00 38.51 ? 3370 HOH   A O     1 
HETATM 19884 O  O     . HOH   BA 11 .    ? -37.172 34.191  90.011  1.00 38.07 ? 3371 HOH   A O     1 
HETATM 19885 O  O     . HOH   BA 11 .    ? -31.424 60.594  124.386 1.00 42.92 ? 3372 HOH   A O     1 
HETATM 19886 O  O     . HOH   BA 11 .    ? 6.860   59.658  94.325  1.00 37.63 ? 3373 HOH   A O     1 
HETATM 19887 O  O     . HOH   BA 11 .    ? -62.515 55.322  97.864  1.00 49.07 ? 3374 HOH   A O     1 
HETATM 19888 O  O     . HOH   BA 11 .    ? -68.239 69.883  69.317  1.00 36.38 ? 3375 HOH   A O     1 
HETATM 19889 O  O     . HOH   BA 11 .    ? -33.276 78.122  71.226  1.00 41.62 ? 3376 HOH   A O     1 
HETATM 19890 O  O     . HOH   BA 11 .    ? -53.996 71.007  102.500 1.00 37.50 ? 3377 HOH   A O     1 
HETATM 19891 O  O     . HOH   BA 11 .    ? -34.442 37.098  106.245 1.00 52.39 ? 3378 HOH   A O     1 
HETATM 19892 O  O     . HOH   BA 11 .    ? -35.662 80.763  70.267  1.00 47.67 ? 3379 HOH   A O     1 
HETATM 19893 O  O     . HOH   BA 11 .    ? -23.168 88.648  138.926 1.00 37.99 ? 3380 HOH   A O     1 
HETATM 19894 O  O     . HOH   BA 11 .    ? -65.955 68.882  86.816  1.00 43.01 ? 3381 HOH   A O     1 
HETATM 19895 O  O     . HOH   BA 11 .    ? -36.711 31.687  90.858  1.00 35.32 ? 3382 HOH   A O     1 
HETATM 19896 O  O     . HOH   BA 11 .    ? -55.981 78.510  77.438  1.00 34.08 ? 3383 HOH   A O     1 
HETATM 19897 O  O     . HOH   BA 11 .    ? -35.207 56.395  109.736 1.00 37.55 ? 3384 HOH   A O     1 
HETATM 19898 O  O     . HOH   BA 11 .    ? -53.784 47.349  98.552  1.00 41.13 ? 3385 HOH   A O     1 
HETATM 19899 O  O     . HOH   BA 11 .    ? -33.947 81.108  71.701  1.00 38.52 ? 3386 HOH   A O     1 
HETATM 19900 O  O     . HOH   BA 11 .    ? 13.769  62.896  90.773  1.00 36.75 ? 3387 HOH   A O     1 
HETATM 19901 O  O     . HOH   CA 11 .    ? 30.655  41.712  67.091  1.00 28.04 ? 2101 HOH   B O     1 
HETATM 19902 O  O     . HOH   CA 11 .    ? 0.098   55.938  74.026  1.00 34.04 ? 2102 HOH   B O     1 
HETATM 19903 O  O     . HOH   CA 11 .    ? -11.048 27.377  81.266  1.00 26.82 ? 2103 HOH   B O     1 
HETATM 19904 O  O     . HOH   CA 11 .    ? 2.250   23.313  100.114 1.00 41.34 ? 2104 HOH   B O     1 
HETATM 19905 O  O     . HOH   CA 11 .    ? -0.548  47.657  87.448  1.00 36.67 ? 2105 HOH   B O     1 
HETATM 19906 O  O     . HOH   CA 11 .    ? 40.447  41.590  93.430  1.00 45.86 ? 2106 HOH   B O     1 
HETATM 19907 O  O     . HOH   CA 11 .    ? 32.979  68.147  74.052  1.00 28.16 ? 2107 HOH   B O     1 
HETATM 19908 O  O     . HOH   CA 11 .    ? -0.304  76.442  74.163  1.00 35.03 ? 2108 HOH   B O     1 
HETATM 19909 O  O     . HOH   CA 11 .    ? 4.251   54.884  72.602  1.00 26.16 ? 2109 HOH   B O     1 
HETATM 19910 O  O     . HOH   CA 11 .    ? 28.794  50.393  74.828  1.00 42.95 ? 2110 HOH   B O     1 
HETATM 19911 O  O     . HOH   CA 11 .    ? 28.140  39.221  50.534  1.00 40.62 ? 2111 HOH   B O     1 
HETATM 19912 O  O     . HOH   CA 11 .    ? 4.224   71.962  85.619  1.00 38.90 ? 2112 HOH   B O     1 
HETATM 19913 O  O     . HOH   CA 11 .    ? 0.014   18.280  80.502  1.00 26.34 ? 2113 HOH   B O     1 
HETATM 19914 O  O     . HOH   CA 11 .    ? -25.459 6.271   111.912 1.00 35.77 ? 2114 HOH   B O     1 
HETATM 19915 O  O     . HOH   CA 11 .    ? -4.095  23.577  107.952 1.00 44.44 ? 2115 HOH   B O     1 
HETATM 19916 O  O     . HOH   CA 11 .    ? 25.643  58.110  53.687  1.00 45.70 ? 2116 HOH   B O     1 
HETATM 19917 O  O     . HOH   CA 11 .    ? -8.968  40.646  130.367 1.00 39.98 ? 2117 HOH   B O     1 
HETATM 19918 O  O     . HOH   CA 11 .    ? -0.239  73.009  77.688  1.00 31.30 ? 2118 HOH   B O     1 
HETATM 19919 O  O     . HOH   CA 11 .    ? -18.676 49.923  120.655 1.00 39.45 ? 2119 HOH   B O     1 
HETATM 19920 O  O     . HOH   CA 11 .    ? 12.350  6.064   117.861 1.00 39.90 ? 2120 HOH   B O     1 
HETATM 19921 O  O     . HOH   CA 11 .    ? 21.291  39.417  47.868  1.00 42.69 ? 2121 HOH   B O     1 
HETATM 19922 O  O     . HOH   CA 11 .    ? 10.942  -8.158  112.370 1.00 46.43 ? 2122 HOH   B O     1 
HETATM 19923 O  O     . HOH   CA 11 .    ? -36.175 24.423  116.085 1.00 32.37 ? 2123 HOH   B O     1 
HETATM 19924 O  O     . HOH   CA 11 .    ? -20.389 -1.546  106.197 1.00 36.34 ? 2124 HOH   B O     1 
HETATM 19925 O  O     . HOH   CA 11 .    ? -14.392 14.694  78.873  1.00 34.26 ? 2125 HOH   B O     1 
HETATM 19926 O  O     . HOH   CA 11 .    ? 13.189  81.334  73.438  1.00 44.02 ? 2126 HOH   B O     1 
HETATM 19927 O  O     . HOH   CA 11 .    ? -28.595 17.418  84.853  1.00 38.74 ? 2127 HOH   B O     1 
HETATM 19928 O  O     . HOH   CA 11 .    ? 2.381   16.932  112.486 1.00 30.88 ? 2128 HOH   B O     1 
HETATM 19929 O  O     . HOH   CA 11 .    ? 6.980   50.972  57.596  1.00 29.85 ? 2129 HOH   B O     1 
HETATM 19930 O  O     . HOH   CA 11 .    ? -1.748  62.196  69.612  1.00 37.60 ? 2130 HOH   B O     1 
HETATM 19931 O  O     . HOH   CA 11 .    ? 30.198  34.988  50.767  1.00 32.16 ? 2131 HOH   B O     1 
HETATM 19932 O  O     . HOH   CA 11 .    ? 30.834  25.730  52.941  1.00 35.93 ? 2132 HOH   B O     1 
HETATM 19933 O  O     . HOH   CA 11 .    ? -8.622  23.903  77.185  1.00 32.15 ? 2133 HOH   B O     1 
HETATM 19934 O  O     . HOH   CA 11 .    ? 3.744   21.206  102.541 1.00 30.59 ? 2134 HOH   B O     1 
HETATM 19935 O  O     . HOH   CA 11 .    ? -1.066  21.993  71.326  1.00 31.86 ? 2135 HOH   B O     1 
HETATM 19936 O  O     . HOH   CA 11 .    ? 22.913  34.587  115.523 1.00 27.37 ? 2136 HOH   B O     1 
HETATM 19937 O  O     . HOH   CA 11 .    ? 32.624  18.711  58.133  1.00 29.28 ? 2137 HOH   B O     1 
HETATM 19938 O  O     . HOH   CA 11 .    ? -18.123 30.944  93.496  1.00 44.87 ? 2138 HOH   B O     1 
HETATM 19939 O  O     . HOH   CA 11 .    ? 6.606   15.171  124.641 1.00 32.65 ? 2139 HOH   B O     1 
HETATM 19940 O  O     . HOH   CA 11 .    ? 1.837   20.139  104.065 1.00 25.08 ? 2140 HOH   B O     1 
HETATM 19941 O  O     . HOH   CA 11 .    ? 1.806   56.994  87.656  1.00 36.17 ? 2141 HOH   B O     1 
HETATM 19942 O  O     . HOH   CA 11 .    ? -4.705  6.590   82.065  1.00 40.04 ? 2142 HOH   B O     1 
HETATM 19943 O  O     . HOH   CA 11 .    ? 25.637  8.364   75.411  1.00 40.40 ? 2143 HOH   B O     1 
HETATM 19944 O  O     . HOH   CA 11 .    ? 14.218  57.783  60.696  1.00 39.24 ? 2144 HOH   B O     1 
HETATM 19945 O  O     . HOH   CA 11 .    ? 18.825  20.836  55.223  1.00 35.28 ? 2145 HOH   B O     1 
HETATM 19946 O  O     . HOH   CA 11 .    ? 3.811   55.973  62.877  1.00 41.80 ? 2146 HOH   B O     1 
HETATM 19947 O  O     . HOH   CA 11 .    ? 34.418  62.231  78.297  1.00 18.20 ? 2147 HOH   B O     1 
HETATM 19948 O  O     . HOH   CA 11 .    ? -14.180 8.984   118.567 1.00 30.92 ? 2148 HOH   B O     1 
HETATM 19949 O  O     . HOH   CA 11 .    ? 16.840  14.124  109.448 1.00 26.23 ? 2149 HOH   B O     1 
HETATM 19950 O  O     . HOH   CA 11 .    ? 6.296   -6.005  116.695 1.00 36.27 ? 2150 HOH   B O     1 
HETATM 19951 O  O     . HOH   CA 11 .    ? 18.630  38.034  115.649 1.00 31.92 ? 2151 HOH   B O     1 
HETATM 19952 O  O     . HOH   CA 11 .    ? -9.995  -2.880  115.812 1.00 32.35 ? 2152 HOH   B O     1 
HETATM 19953 O  O     . HOH   CA 11 .    ? 34.426  41.122  90.720  1.00 36.93 ? 2153 HOH   B O     1 
HETATM 19954 O  O     . HOH   CA 11 .    ? 37.188  27.903  93.195  1.00 32.01 ? 2154 HOH   B O     1 
HETATM 19955 O  O     . HOH   CA 11 .    ? -5.439  39.311  90.268  1.00 39.80 ? 2155 HOH   B O     1 
HETATM 19956 O  O     . HOH   CA 11 .    ? 20.796  10.167  101.649 1.00 45.64 ? 2156 HOH   B O     1 
HETATM 19957 O  O     . HOH   CA 11 .    ? 6.015   36.770  136.774 1.00 46.67 ? 2157 HOH   B O     1 
HETATM 19958 O  O     . HOH   CA 11 .    ? 15.741  21.504  88.567  1.00 34.24 ? 2158 HOH   B O     1 
HETATM 19959 O  O     . HOH   CA 11 .    ? -2.467  28.932  57.725  1.00 31.82 ? 2159 HOH   B O     1 
HETATM 19960 O  O     . HOH   CA 11 .    ? 4.938   56.602  112.811 1.00 41.02 ? 2160 HOH   B O     1 
HETATM 19961 O  O     . HOH   CA 11 .    ? 11.186  79.487  67.791  1.00 42.52 ? 2161 HOH   B O     1 
HETATM 19962 O  O     . HOH   CA 11 .    ? 29.680  30.689  50.223  1.00 42.57 ? 2162 HOH   B O     1 
HETATM 19963 O  O     . HOH   CA 11 .    ? 31.067  14.452  64.780  1.00 42.34 ? 2163 HOH   B O     1 
HETATM 19964 O  O     . HOH   CA 11 .    ? -0.344  26.681  68.658  1.00 17.37 ? 2164 HOH   B O     1 
HETATM 19965 O  O     . HOH   CA 11 .    ? 19.056  66.899  82.550  1.00 26.23 ? 2165 HOH   B O     1 
HETATM 19966 O  O     . HOH   CA 11 .    ? 9.462   25.566  55.271  1.00 20.97 ? 2166 HOH   B O     1 
HETATM 19967 O  O     . HOH   CA 11 .    ? -2.470  4.570   85.111  1.00 28.29 ? 2167 HOH   B O     1 
HETATM 19968 O  O     . HOH   CA 11 .    ? -35.478 16.567  101.702 1.00 43.65 ? 2168 HOH   B O     1 
HETATM 19969 O  O     . HOH   CA 11 .    ? 10.696  51.039  75.396  1.00 22.00 ? 2169 HOH   B O     1 
HETATM 19970 O  O     . HOH   CA 11 .    ? -12.047 24.415  110.264 1.00 31.83 ? 2170 HOH   B O     1 
HETATM 19971 O  O     . HOH   CA 11 .    ? 21.728  79.368  69.881  1.00 36.26 ? 2171 HOH   B O     1 
HETATM 19972 O  O     . HOH   CA 11 .    ? -13.961 53.853  118.085 1.00 28.43 ? 2172 HOH   B O     1 
HETATM 19973 O  O     . HOH   CA 11 .    ? -21.243 26.659  83.897  1.00 43.45 ? 2173 HOH   B O     1 
HETATM 19974 O  O     . HOH   CA 11 .    ? 14.118  41.172  76.931  1.00 17.37 ? 2174 HOH   B O     1 
HETATM 19975 O  O     . HOH   CA 11 .    ? -4.097  45.104  89.812  1.00 40.12 ? 2175 HOH   B O     1 
HETATM 19976 O  O     . HOH   CA 11 .    ? 17.903  12.471  117.251 1.00 27.98 ? 2176 HOH   B O     1 
HETATM 19977 O  O     . HOH   CA 11 .    ? 19.342  41.103  47.404  1.00 42.10 ? 2177 HOH   B O     1 
HETATM 19978 O  O     . HOH   CA 11 .    ? 1.139   -10.683 110.913 1.00 29.04 ? 2178 HOH   B O     1 
HETATM 19979 O  O     . HOH   CA 11 .    ? 33.156  29.393  61.908  1.00 26.56 ? 2179 HOH   B O     1 
HETATM 19980 O  O     . HOH   CA 11 .    ? 3.723   7.541   92.404  1.00 21.25 ? 2180 HOH   B O     1 
HETATM 19981 O  O     . HOH   CA 11 .    ? -5.386  -1.907  123.611 1.00 35.88 ? 2181 HOH   B O     1 
HETATM 19982 O  O     . HOH   CA 11 .    ? 15.124  40.027  72.969  1.00 18.26 ? 2182 HOH   B O     1 
HETATM 19983 O  O     . HOH   CA 11 .    ? 13.623  10.067  91.459  1.00 23.71 ? 2183 HOH   B O     1 
HETATM 19984 O  O     . HOH   CA 11 .    ? -22.447 18.939  102.250 1.00 29.01 ? 2184 HOH   B O     1 
HETATM 19985 O  O     . HOH   CA 11 .    ? -29.058 22.463  90.226  1.00 36.15 ? 2185 HOH   B O     1 
HETATM 19986 O  O     . HOH   CA 11 .    ? 11.372  24.496  108.182 1.00 27.92 ? 2186 HOH   B O     1 
HETATM 19987 O  O     . HOH   CA 11 .    ? 4.826   35.333  117.825 1.00 44.83 ? 2187 HOH   B O     1 
HETATM 19988 O  O     . HOH   CA 11 .    ? 23.608  64.690  82.297  1.00 38.05 ? 2188 HOH   B O     1 
HETATM 19989 O  O     . HOH   CA 11 .    ? 29.119  68.965  79.797  1.00 24.64 ? 2189 HOH   B O     1 
HETATM 19990 O  O     . HOH   CA 11 .    ? 15.054  55.634  74.856  1.00 26.11 ? 2190 HOH   B O     1 
HETATM 19991 O  O     . HOH   CA 11 .    ? 0.962   19.380  111.689 1.00 32.12 ? 2191 HOH   B O     1 
HETATM 19992 O  O     . HOH   CA 11 .    ? 29.539  41.960  84.232  1.00 26.88 ? 2192 HOH   B O     1 
HETATM 19993 O  O     . HOH   CA 11 .    ? 18.680  7.227   100.723 1.00 37.37 ? 2193 HOH   B O     1 
HETATM 19994 O  O     . HOH   CA 11 .    ? -5.220  39.479  72.285  1.00 26.14 ? 2194 HOH   B O     1 
HETATM 19995 O  O     . HOH   CA 11 .    ? 23.501  18.037  80.489  1.00 27.01 ? 2195 HOH   B O     1 
HETATM 19996 O  O     . HOH   CA 11 .    ? -6.351  12.019  125.352 1.00 27.53 ? 2196 HOH   B O     1 
HETATM 19997 O  O     . HOH   CA 11 .    ? 26.823  41.507  49.759  1.00 42.12 ? 2197 HOH   B O     1 
HETATM 19998 O  O     . HOH   CA 11 .    ? -4.153  63.924  81.030  1.00 17.60 ? 2198 HOH   B O     1 
HETATM 19999 O  O     . HOH   CA 11 .    ? -4.611  26.687  70.268  1.00 30.74 ? 2199 HOH   B O     1 
HETATM 20000 O  O     . HOH   CA 11 .    ? -5.955  39.982  62.939  1.00 33.33 ? 2200 HOH   B O     1 
HETATM 20001 O  O     . HOH   CA 11 .    ? -8.684  45.066  108.911 1.00 30.48 ? 2201 HOH   B O     1 
HETATM 20002 O  O     . HOH   CA 11 .    ? 9.383   61.388  55.781  1.00 48.07 ? 2202 HOH   B O     1 
HETATM 20003 O  O     . HOH   CA 11 .    ? 6.324   19.448  94.073  1.00 36.76 ? 2203 HOH   B O     1 
HETATM 20004 O  O     . HOH   CA 11 .    ? 16.410  10.259  112.412 1.00 41.23 ? 2204 HOH   B O     1 
HETATM 20005 O  O     . HOH   CA 11 .    ? -17.052 14.964  79.838  1.00 36.32 ? 2205 HOH   B O     1 
HETATM 20006 O  O     . HOH   CA 11 .    ? 9.133   23.011  109.068 1.00 30.40 ? 2206 HOH   B O     1 
HETATM 20007 O  O     . HOH   CA 11 .    ? -5.438  4.856   122.236 1.00 23.62 ? 2207 HOH   B O     1 
HETATM 20008 O  O     . HOH   CA 11 .    ? -2.312  45.224  102.724 1.00 31.34 ? 2208 HOH   B O     1 
HETATM 20009 O  O     . HOH   CA 11 .    ? -28.865 12.841  98.813  1.00 42.45 ? 2209 HOH   B O     1 
HETATM 20010 O  O     . HOH   CA 11 .    ? -11.950 3.526   129.596 1.00 44.16 ? 2210 HOH   B O     1 
HETATM 20011 O  O     . HOH   CA 11 .    ? 11.138  46.120  106.714 1.00 30.11 ? 2211 HOH   B O     1 
HETATM 20012 O  O     . HOH   CA 11 .    ? 21.583  6.641   83.455  1.00 34.67 ? 2212 HOH   B O     1 
HETATM 20013 O  O     . HOH   CA 11 .    ? 18.978  61.887  57.462  1.00 34.12 ? 2213 HOH   B O     1 
HETATM 20014 O  O     . HOH   CA 11 .    ? 3.412   18.048  89.043  1.00 26.21 ? 2214 HOH   B O     1 
HETATM 20015 O  O     . HOH   CA 11 .    ? 27.448  12.801  66.700  1.00 33.90 ? 2215 HOH   B O     1 
HETATM 20016 O  O     . HOH   CA 11 .    ? 11.007  38.030  95.759  1.00 25.94 ? 2216 HOH   B O     1 
HETATM 20017 O  O     . HOH   CA 11 .    ? -10.233 25.160  103.127 1.00 31.40 ? 2217 HOH   B O     1 
HETATM 20018 O  O     . HOH   CA 11 .    ? 38.505  33.720  102.688 1.00 28.90 ? 2218 HOH   B O     1 
HETATM 20019 O  O     . HOH   CA 11 .    ? -10.602 46.230  74.547  1.00 19.62 ? 2219 HOH   B O     1 
HETATM 20020 O  O     . HOH   CA 11 .    ? 12.094  44.925  109.138 1.00 37.10 ? 2220 HOH   B O     1 
HETATM 20021 O  O     . HOH   CA 11 .    ? 29.827  26.967  56.191  1.00 22.31 ? 2221 HOH   B O     1 
HETATM 20022 O  O     . HOH   CA 11 .    ? -10.127 10.707  129.848 1.00 37.23 ? 2222 HOH   B O     1 
HETATM 20023 O  O     . HOH   CA 11 .    ? -28.688 4.273   116.032 1.00 44.17 ? 2223 HOH   B O     1 
HETATM 20024 O  O     . HOH   CA 11 .    ? 11.265  5.552   121.775 1.00 29.64 ? 2224 HOH   B O     1 
HETATM 20025 O  O     . HOH   CA 11 .    ? -7.858  19.736  79.705  1.00 33.34 ? 2225 HOH   B O     1 
HETATM 20026 O  O     . HOH   CA 11 .    ? 18.860  12.679  95.491  1.00 27.11 ? 2226 HOH   B O     1 
HETATM 20027 O  O     . HOH   CA 11 .    ? 5.619   43.495  58.675  1.00 30.00 ? 2227 HOH   B O     1 
HETATM 20028 O  O     . HOH   CA 11 .    ? 21.029  5.067   68.283  1.00 44.51 ? 2228 HOH   B O     1 
HETATM 20029 O  O     . HOH   CA 11 .    ? 22.404  45.280  90.605  1.00 17.02 ? 2229 HOH   B O     1 
HETATM 20030 O  O     . HOH   CA 11 .    ? 4.430   41.840  84.437  1.00 22.99 ? 2230 HOH   B O     1 
HETATM 20031 O  O     . HOH   CA 11 .    ? -12.709 8.538   124.539 1.00 31.24 ? 2231 HOH   B O     1 
HETATM 20032 O  O     . HOH   CA 11 .    ? 4.051   13.831  72.981  1.00 32.46 ? 2232 HOH   B O     1 
HETATM 20033 O  O     . HOH   CA 11 .    ? 16.329  2.186   104.595 1.00 38.40 ? 2233 HOH   B O     1 
HETATM 20034 O  O     . HOH   CA 11 .    ? -17.462 -0.113  99.675  1.00 32.07 ? 2234 HOH   B O     1 
HETATM 20035 O  O     . HOH   CA 11 .    ? 3.575   33.465  86.691  1.00 20.01 ? 2235 HOH   B O     1 
HETATM 20036 O  O     . HOH   CA 11 .    ? -6.243  50.742  73.077  1.00 16.00 ? 2236 HOH   B O     1 
HETATM 20037 O  O     . HOH   CA 11 .    ? 21.564  50.191  87.678  1.00 21.90 ? 2237 HOH   B O     1 
HETATM 20038 O  O     . HOH   CA 11 .    ? -12.508 19.712  84.004  1.00 23.41 ? 2238 HOH   B O     1 
HETATM 20039 O  O     . HOH   CA 11 .    ? -2.220  48.500  63.647  1.00 18.60 ? 2239 HOH   B O     1 
HETATM 20040 O  O     . HOH   CA 11 .    ? 1.140   38.642  108.220 1.00 26.53 ? 2240 HOH   B O     1 
HETATM 20041 O  O     . HOH   CA 11 .    ? -9.669  -5.034  107.294 1.00 27.57 ? 2241 HOH   B O     1 
HETATM 20042 O  O     . HOH   CA 11 .    ? 22.625  9.316   69.706  1.00 40.12 ? 2242 HOH   B O     1 
HETATM 20043 O  O     . HOH   CA 11 .    ? 6.016   25.329  86.377  1.00 30.44 ? 2243 HOH   B O     1 
HETATM 20044 O  O     . HOH   CA 11 .    ? 28.380  18.441  58.053  1.00 31.67 ? 2244 HOH   B O     1 
HETATM 20045 O  O     . HOH   CA 11 .    ? -6.437  10.947  127.750 1.00 31.04 ? 2245 HOH   B O     1 
HETATM 20046 O  O     . HOH   CA 11 .    ? -1.291  14.247  85.990  1.00 22.63 ? 2246 HOH   B O     1 
HETATM 20047 O  O     . HOH   CA 11 .    ? 4.120   -9.039  104.286 1.00 32.55 ? 2247 HOH   B O     1 
HETATM 20048 O  O     . HOH   CA 11 .    ? 8.599   -1.322  107.107 1.00 33.69 ? 2248 HOH   B O     1 
HETATM 20049 O  O     . HOH   CA 11 .    ? 8.128   7.708   72.781  1.00 38.10 ? 2249 HOH   B O     1 
HETATM 20050 O  O     . HOH   CA 11 .    ? 9.859   30.202  110.068 1.00 39.91 ? 2250 HOH   B O     1 
HETATM 20051 O  O     . HOH   CA 11 .    ? -37.640 10.520  106.362 1.00 44.14 ? 2251 HOH   B O     1 
HETATM 20052 O  O     . HOH   CA 11 .    ? 24.272  18.754  98.100  1.00 29.58 ? 2252 HOH   B O     1 
HETATM 20053 O  O     . HOH   CA 11 .    ? -32.489 16.052  98.625  1.00 37.22 ? 2253 HOH   B O     1 
HETATM 20054 O  O     . HOH   CA 11 .    ? -4.519  -2.377  97.060  1.00 21.00 ? 2254 HOH   B O     1 
HETATM 20055 O  O     . HOH   CA 11 .    ? 1.716   12.848  101.960 1.00 19.13 ? 2255 HOH   B O     1 
HETATM 20056 O  O     . HOH   CA 11 .    ? 32.575  26.453  68.597  1.00 35.75 ? 2256 HOH   B O     1 
HETATM 20057 O  O     . HOH   CA 11 .    ? 2.719   21.527  130.377 1.00 29.66 ? 2257 HOH   B O     1 
HETATM 20058 O  O     . HOH   CA 11 .    ? 33.673  12.022  74.824  1.00 32.19 ? 2258 HOH   B O     1 
HETATM 20059 O  O     . HOH   CA 11 .    ? -6.922  8.160   111.205 1.00 20.71 ? 2259 HOH   B O     1 
HETATM 20060 O  O     . HOH   CA 11 .    ? -11.354 -4.956  97.883  1.00 37.64 ? 2260 HOH   B O     1 
HETATM 20061 O  O     . HOH   CA 11 .    ? 14.453  33.439  84.041  1.00 18.51 ? 2261 HOH   B O     1 
HETATM 20062 O  O     . HOH   CA 11 .    ? -29.765 11.600  96.420  1.00 38.74 ? 2262 HOH   B O     1 
HETATM 20063 O  O     . HOH   CA 11 .    ? 6.752   5.495   92.417  1.00 20.93 ? 2263 HOH   B O     1 
HETATM 20064 O  O     . HOH   CA 11 .    ? 22.991  54.062  53.662  1.00 36.53 ? 2264 HOH   B O     1 
HETATM 20065 O  O     . HOH   CA 11 .    ? 28.379  13.147  86.026  1.00 28.40 ? 2265 HOH   B O     1 
HETATM 20066 O  O     . HOH   CA 11 .    ? -5.731  39.120  106.819 1.00 28.22 ? 2266 HOH   B O     1 
HETATM 20067 O  O     . HOH   CA 11 .    ? 13.714  57.923  64.659  1.00 27.54 ? 2267 HOH   B O     1 
HETATM 20068 O  O     . HOH   CA 11 .    ? -9.947  39.550  127.334 1.00 37.48 ? 2268 HOH   B O     1 
HETATM 20069 O  O     . HOH   CA 11 .    ? -2.169  39.205  87.240  1.00 18.15 ? 2269 HOH   B O     1 
HETATM 20070 O  O     . HOH   CA 11 .    ? 4.397   21.167  118.898 1.00 31.71 ? 2270 HOH   B O     1 
HETATM 20071 O  O     . HOH   CA 11 .    ? -4.632  43.822  81.170  1.00 30.68 ? 2271 HOH   B O     1 
HETATM 20072 O  O     . HOH   CA 11 .    ? 19.842  19.217  105.712 1.00 18.11 ? 2272 HOH   B O     1 
HETATM 20073 O  O     . HOH   CA 11 .    ? 11.091  18.909  61.467  1.00 27.93 ? 2273 HOH   B O     1 
HETATM 20074 O  O     . HOH   CA 11 .    ? 15.588  53.281  81.712  1.00 22.64 ? 2274 HOH   B O     1 
HETATM 20075 O  O     . HOH   CA 11 .    ? -31.144 15.860  102.459 1.00 32.94 ? 2275 HOH   B O     1 
HETATM 20076 O  O     . HOH   CA 11 .    ? 18.910  24.477  54.554  1.00 22.97 ? 2276 HOH   B O     1 
HETATM 20077 O  O     . HOH   CA 11 .    ? -21.733 31.822  101.018 1.00 43.93 ? 2277 HOH   B O     1 
HETATM 20078 O  O     . HOH   CA 11 .    ? -3.092  67.429  70.632  1.00 40.94 ? 2278 HOH   B O     1 
HETATM 20079 O  O     . HOH   CA 11 .    ? 31.356  28.458  77.567  1.00 27.16 ? 2279 HOH   B O     1 
HETATM 20080 O  O     . HOH   CA 11 .    ? -21.030 15.309  82.841  1.00 26.55 ? 2280 HOH   B O     1 
HETATM 20081 O  O     . HOH   CA 11 .    ? -4.454  59.548  125.545 1.00 31.82 ? 2281 HOH   B O     1 
HETATM 20082 O  O     . HOH   CA 11 .    ? -21.082 5.346   90.741  1.00 38.30 ? 2282 HOH   B O     1 
HETATM 20083 O  O     . HOH   CA 11 .    ? 31.917  38.165  84.173  1.00 28.25 ? 2283 HOH   B O     1 
HETATM 20084 O  O     . HOH   CA 11 .    ? 39.349  26.617  87.603  1.00 34.56 ? 2284 HOH   B O     1 
HETATM 20085 O  O     . HOH   CA 11 .    ? -4.551  1.835   124.104 1.00 24.32 ? 2285 HOH   B O     1 
HETATM 20086 O  O     . HOH   CA 11 .    ? -2.434  14.223  81.393  1.00 41.34 ? 2286 HOH   B O     1 
HETATM 20087 O  O     . HOH   CA 11 .    ? 2.703   30.367  80.167  1.00 17.97 ? 2287 HOH   B O     1 
HETATM 20088 O  O     . HOH   CA 11 .    ? 23.786  39.025  111.234 1.00 34.97 ? 2288 HOH   B O     1 
HETATM 20089 O  O     . HOH   CA 11 .    ? 9.190   3.631   81.019  1.00 25.35 ? 2289 HOH   B O     1 
HETATM 20090 O  O     . HOH   CA 11 .    ? 2.247   29.671  54.902  1.00 37.18 ? 2290 HOH   B O     1 
HETATM 20091 O  O     . HOH   CA 11 .    ? -5.706  37.077  77.779  1.00 27.07 ? 2291 HOH   B O     1 
HETATM 20092 O  O     . HOH   CA 11 .    ? 31.762  37.355  106.623 1.00 34.84 ? 2292 HOH   B O     1 
HETATM 20093 O  O     . HOH   CA 11 .    ? 18.960  31.021  73.263  1.00 18.41 ? 2293 HOH   B O     1 
HETATM 20094 O  O     . HOH   CA 11 .    ? -11.618 17.952  126.744 1.00 25.81 ? 2294 HOH   B O     1 
HETATM 20095 O  O     . HOH   CA 11 .    ? -5.075  51.331  75.548  1.00 20.43 ? 2295 HOH   B O     1 
HETATM 20096 O  O     . HOH   CA 11 .    ? 15.146  38.662  77.114  1.00 15.53 ? 2296 HOH   B O     1 
HETATM 20097 O  O     . HOH   CA 11 .    ? 19.824  50.765  77.524  1.00 19.82 ? 2297 HOH   B O     1 
HETATM 20098 O  O     . HOH   CA 11 .    ? -1.348  -6.625  117.392 1.00 36.83 ? 2298 HOH   B O     1 
HETATM 20099 O  O     . HOH   CA 11 .    ? 8.016   65.020  63.821  1.00 28.74 ? 2299 HOH   B O     1 
HETATM 20100 O  O     . HOH   CA 11 .    ? -4.045  18.437  98.223  1.00 15.61 ? 2300 HOH   B O     1 
HETATM 20101 O  O     . HOH   CA 11 .    ? 17.439  54.707  97.213  1.00 27.65 ? 2301 HOH   B O     1 
HETATM 20102 O  O     . HOH   CA 11 .    ? -6.402  52.284  107.169 1.00 29.27 ? 2302 HOH   B O     1 
HETATM 20103 O  O     . HOH   CA 11 .    ? -1.229  38.022  80.194  1.00 22.21 ? 2303 HOH   B O     1 
HETATM 20104 O  O     . HOH   CA 11 .    ? 7.200   19.066  116.551 1.00 31.11 ? 2304 HOH   B O     1 
HETATM 20105 O  O     . HOH   CA 11 .    ? 1.725   13.238  104.811 1.00 18.13 ? 2305 HOH   B O     1 
HETATM 20106 O  O     . HOH   CA 11 .    ? 10.245  50.453  64.688  1.00 24.06 ? 2306 HOH   B O     1 
HETATM 20107 O  O     . HOH   CA 11 .    ? 10.094  48.724  55.859  1.00 34.47 ? 2307 HOH   B O     1 
HETATM 20108 O  O     . HOH   CA 11 .    ? 1.589   5.905   91.863  1.00 20.16 ? 2308 HOH   B O     1 
HETATM 20109 O  O     . HOH   CA 11 .    ? 31.824  59.764  65.460  1.00 25.82 ? 2309 HOH   B O     1 
HETATM 20110 O  O     . HOH   CA 11 .    ? -7.243  25.414  104.007 1.00 39.12 ? 2310 HOH   B O     1 
HETATM 20111 O  O     . HOH   CA 11 .    ? 7.710   48.901  106.636 1.00 21.53 ? 2311 HOH   B O     1 
HETATM 20112 O  O     . HOH   CA 11 .    ? -2.315  41.518  61.770  1.00 23.88 ? 2312 HOH   B O     1 
HETATM 20113 O  O     . HOH   CA 11 .    ? 5.479   51.042  109.899 1.00 36.09 ? 2313 HOH   B O     1 
HETATM 20114 O  O     . HOH   CA 11 .    ? 1.040   41.913  76.233  1.00 24.23 ? 2314 HOH   B O     1 
HETATM 20115 O  O     . HOH   CA 11 .    ? 27.245  32.547  104.904 1.00 36.70 ? 2315 HOH   B O     1 
HETATM 20116 O  O     . HOH   CA 11 .    ? -24.900 3.714   111.875 1.00 34.97 ? 2316 HOH   B O     1 
HETATM 20117 O  O     . HOH   CA 11 .    ? 6.340   5.450   86.112  1.00 20.42 ? 2317 HOH   B O     1 
HETATM 20118 O  O     . HOH   CA 11 .    ? 16.153  69.428  55.288  1.00 41.13 ? 2318 HOH   B O     1 
HETATM 20119 O  O     . HOH   CA 11 .    ? -4.677  7.903   131.463 1.00 42.75 ? 2319 HOH   B O     1 
HETATM 20120 O  O     . HOH   CA 11 .    ? 12.345  21.068  101.474 1.00 24.24 ? 2320 HOH   B O     1 
HETATM 20121 O  O     . HOH   CA 11 .    ? 2.693   43.690  70.462  1.00 16.47 ? 2321 HOH   B O     1 
HETATM 20122 O  O     . HOH   CA 11 .    ? 19.353  78.909  68.454  1.00 29.79 ? 2322 HOH   B O     1 
HETATM 20123 O  O     . HOH   CA 11 .    ? -31.987 16.938  91.550  1.00 34.36 ? 2323 HOH   B O     1 
HETATM 20124 O  O     . HOH   CA 11 .    ? 15.418  16.608  88.008  1.00 20.59 ? 2324 HOH   B O     1 
HETATM 20125 O  O     . HOH   CA 11 .    ? 17.255  40.686  71.503  1.00 17.63 ? 2325 HOH   B O     1 
HETATM 20126 O  O     . HOH   CA 11 .    ? -4.827  30.460  77.499  1.00 17.68 ? 2326 HOH   B O     1 
HETATM 20127 O  O     . HOH   CA 11 .    ? 5.156   35.623  49.123  1.00 32.54 ? 2327 HOH   B O     1 
HETATM 20128 O  O     . HOH   CA 11 .    ? 6.992   42.236  49.699  1.00 26.42 ? 2328 HOH   B O     1 
HETATM 20129 O  O     . HOH   CA 11 .    ? 6.017   31.612  79.229  1.00 19.60 ? 2329 HOH   B O     1 
HETATM 20130 O  O     . HOH   CA 11 .    ? 33.928  67.627  80.450  1.00 21.47 ? 2330 HOH   B O     1 
HETATM 20131 O  O     . HOH   CA 11 .    ? -13.482 17.789  105.742 1.00 21.31 ? 2331 HOH   B O     1 
HETATM 20132 O  O     . HOH   CA 11 .    ? 5.167   31.954  89.214  1.00 32.85 ? 2332 HOH   B O     1 
HETATM 20133 O  O     . HOH   CA 11 .    ? -3.381  10.404  84.551  1.00 22.26 ? 2333 HOH   B O     1 
HETATM 20134 O  O     . HOH   CA 11 .    ? 23.037  48.180  78.073  1.00 19.63 ? 2334 HOH   B O     1 
HETATM 20135 O  O     . HOH   CA 11 .    ? 8.135   56.431  87.434  1.00 33.02 ? 2335 HOH   B O     1 
HETATM 20136 O  O     . HOH   CA 11 .    ? -15.066 48.833  129.297 1.00 45.97 ? 2336 HOH   B O     1 
HETATM 20137 O  O     . HOH   CA 11 .    ? 1.463   21.870  110.996 1.00 32.02 ? 2337 HOH   B O     1 
HETATM 20138 O  O     . HOH   CA 11 .    ? 19.293  70.233  59.155  1.00 34.70 ? 2338 HOH   B O     1 
HETATM 20139 O  O     . HOH   CA 11 .    ? 18.826  44.694  53.768  1.00 27.01 ? 2339 HOH   B O     1 
HETATM 20140 O  O     . HOH   CA 11 .    ? 17.544  27.132  83.040  1.00 23.78 ? 2340 HOH   B O     1 
HETATM 20141 O  O     . HOH   CA 11 .    ? 18.982  5.597   74.392  1.00 26.57 ? 2341 HOH   B O     1 
HETATM 20142 O  O     . HOH   CA 11 .    ? 2.775   53.225  69.541  1.00 32.16 ? 2342 HOH   B O     1 
HETATM 20143 O  O     . HOH   CA 11 .    ? -7.462  24.119  116.684 1.00 38.73 ? 2343 HOH   B O     1 
HETATM 20144 O  O     . HOH   CA 11 .    ? 11.984  37.721  47.447  1.00 32.67 ? 2344 HOH   B O     1 
HETATM 20145 O  O     . HOH   CA 11 .    ? 4.817   30.305  54.805  1.00 33.87 ? 2345 HOH   B O     1 
HETATM 20146 O  O     . HOH   CA 11 .    ? 14.261  71.908  61.059  1.00 27.94 ? 2346 HOH   B O     1 
HETATM 20147 O  O     . HOH   CA 11 .    ? -18.272 25.677  83.250  1.00 35.70 ? 2347 HOH   B O     1 
HETATM 20148 O  O     . HOH   CA 11 .    ? 13.231  50.983  86.430  1.00 29.85 ? 2348 HOH   B O     1 
HETATM 20149 O  O     . HOH   CA 11 .    ? 15.110  20.647  92.700  1.00 28.24 ? 2349 HOH   B O     1 
HETATM 20150 O  O     . HOH   CA 11 .    ? 16.026  52.504  57.944  1.00 33.71 ? 2350 HOH   B O     1 
HETATM 20151 O  O     . HOH   CA 11 .    ? 23.618  52.245  70.561  1.00 28.10 ? 2351 HOH   B O     1 
HETATM 20152 O  O     . HOH   CA 11 .    ? -5.405  54.778  78.750  1.00 24.75 ? 2352 HOH   B O     1 
HETATM 20153 O  O     . HOH   CA 11 .    ? 12.033  10.729  71.654  1.00 21.65 ? 2353 HOH   B O     1 
HETATM 20154 O  O     . HOH   CA 11 .    ? 25.707  53.061  96.452  1.00 38.14 ? 2354 HOH   B O     1 
HETATM 20155 O  O     . HOH   CA 11 .    ? 12.016  3.003   74.318  1.00 42.59 ? 2355 HOH   B O     1 
HETATM 20156 O  O     . HOH   CA 11 .    ? 32.708  47.236  92.177  1.00 37.53 ? 2356 HOH   B O     1 
HETATM 20157 O  O     . HOH   CA 11 .    ? 26.471  20.196  55.807  1.00 31.73 ? 2357 HOH   B O     1 
HETATM 20158 O  O     . HOH   CA 11 .    ? 37.585  23.599  84.652  1.00 37.57 ? 2358 HOH   B O     1 
HETATM 20159 O  O     . HOH   CA 11 .    ? -0.488  23.705  74.320  1.00 20.07 ? 2359 HOH   B O     1 
HETATM 20160 O  O     . HOH   CA 11 .    ? 10.122  70.834  61.749  1.00 30.76 ? 2360 HOH   B O     1 
HETATM 20161 O  O     . HOH   CA 11 .    ? 26.074  54.885  77.474  1.00 23.73 ? 2361 HOH   B O     1 
HETATM 20162 O  O     . HOH   CA 11 .    ? 12.020  0.487   94.179  1.00 37.96 ? 2362 HOH   B O     1 
HETATM 20163 O  O     . HOH   CA 11 .    ? 21.962  52.964  67.202  1.00 24.19 ? 2363 HOH   B O     1 
HETATM 20164 O  O     . HOH   CA 11 .    ? -7.271  15.377  81.788  1.00 32.80 ? 2364 HOH   B O     1 
HETATM 20165 O  O     . HOH   CA 11 .    ? 25.559  54.494  62.116  1.00 21.75 ? 2365 HOH   B O     1 
HETATM 20166 O  O     . HOH   CA 11 .    ? 28.580  36.898  82.749  1.00 31.39 ? 2366 HOH   B O     1 
HETATM 20167 O  O     . HOH   CA 11 .    ? -7.572  -1.172  119.981 1.00 28.03 ? 2367 HOH   B O     1 
HETATM 20168 O  O     . HOH   CA 11 .    ? 10.140  50.237  90.095  1.00 29.59 ? 2368 HOH   B O     1 
HETATM 20169 O  O     . HOH   CA 11 .    ? -11.525 -4.968  109.428 1.00 31.15 ? 2369 HOH   B O     1 
HETATM 20170 O  O     . HOH   CA 11 .    ? 29.490  31.877  76.508  1.00 23.11 ? 2370 HOH   B O     1 
HETATM 20171 O  O     . HOH   CA 11 .    ? 22.343  11.853  71.604  1.00 23.74 ? 2371 HOH   B O     1 
HETATM 20172 O  O     . HOH   CA 11 .    ? -9.185  9.726   123.044 1.00 23.46 ? 2372 HOH   B O     1 
HETATM 20173 O  O     . HOH   CA 11 .    ? 5.019   60.170  67.830  1.00 37.09 ? 2373 HOH   B O     1 
HETATM 20174 O  O     . HOH   CA 11 .    ? 22.996  67.037  64.599  1.00 22.49 ? 2374 HOH   B O     1 
HETATM 20175 O  O     . HOH   CA 11 .    ? -16.839 15.862  131.353 1.00 38.52 ? 2375 HOH   B O     1 
HETATM 20176 O  O     . HOH   CA 11 .    ? 32.462  8.693   74.845  1.00 40.69 ? 2376 HOH   B O     1 
HETATM 20177 O  O     . HOH   CA 11 .    ? 31.463  53.818  59.267  1.00 45.56 ? 2377 HOH   B O     1 
HETATM 20178 O  O     . HOH   CA 11 .    ? 20.186  43.226  87.791  1.00 14.61 ? 2378 HOH   B O     1 
HETATM 20179 O  O     . HOH   CA 11 .    ? -5.086  9.545   115.082 1.00 24.90 ? 2379 HOH   B O     1 
HETATM 20180 O  O     . HOH   CA 11 .    ? 31.201  21.061  79.970  1.00 19.54 ? 2380 HOH   B O     1 
HETATM 20181 O  O     . HOH   CA 11 .    ? -24.938 10.107  87.718  1.00 29.38 ? 2381 HOH   B O     1 
HETATM 20182 O  O     . HOH   CA 11 .    ? 12.321  70.081  60.649  1.00 37.39 ? 2382 HOH   B O     1 
HETATM 20183 O  O     . HOH   CA 11 .    ? 29.320  68.141  72.543  1.00 37.68 ? 2383 HOH   B O     1 
HETATM 20184 O  O     . HOH   CA 11 .    ? 2.781   45.468  53.925  1.00 36.07 ? 2384 HOH   B O     1 
HETATM 20185 O  O     . HOH   CA 11 .    ? 31.112  37.641  77.541  1.00 34.70 ? 2385 HOH   B O     1 
HETATM 20186 O  O     . HOH   CA 11 .    ? 30.012  19.942  76.941  1.00 28.84 ? 2386 HOH   B O     1 
HETATM 20187 O  O     . HOH   CA 11 .    ? 14.331  25.425  110.994 1.00 34.37 ? 2387 HOH   B O     1 
HETATM 20188 O  O     . HOH   CA 11 .    ? -13.717 -0.674  96.966  1.00 35.04 ? 2388 HOH   B O     1 
HETATM 20189 O  O     . HOH   CA 11 .    ? -0.082  55.707  86.352  1.00 33.05 ? 2389 HOH   B O     1 
HETATM 20190 O  O     . HOH   CA 11 .    ? 1.051   28.506  83.080  1.00 15.06 ? 2390 HOH   B O     1 
HETATM 20191 O  O     . HOH   CA 11 .    ? -1.371  32.360  69.195  1.00 15.21 ? 2391 HOH   B O     1 
HETATM 20192 O  O     . HOH   CA 11 .    ? 6.382   21.263  89.340  1.00 38.23 ? 2392 HOH   B O     1 
HETATM 20193 O  O     . HOH   CA 11 .    ? 30.244  49.690  71.521  1.00 29.80 ? 2393 HOH   B O     1 
HETATM 20194 O  O     . HOH   CA 11 .    ? 17.455  48.636  58.968  1.00 22.60 ? 2394 HOH   B O     1 
HETATM 20195 O  O     . HOH   CA 11 .    ? 4.854   49.022  68.714  1.00 22.22 ? 2395 HOH   B O     1 
HETATM 20196 O  O     . HOH   CA 11 .    ? -10.872 1.482   121.707 1.00 23.83 ? 2396 HOH   B O     1 
HETATM 20197 O  O     . HOH   CA 11 .    ? 15.427  3.622   98.544  1.00 29.72 ? 2397 HOH   B O     1 
HETATM 20198 O  O     . HOH   CA 11 .    ? -26.693 14.728  100.742 1.00 35.44 ? 2398 HOH   B O     1 
HETATM 20199 O  O     . HOH   CA 11 .    ? 19.676  5.075   76.958  1.00 31.39 ? 2399 HOH   B O     1 
HETATM 20200 O  O     . HOH   CA 11 .    ? 3.712   33.384  92.919  1.00 20.57 ? 2400 HOH   B O     1 
HETATM 20201 O  O     . HOH   CA 11 .    ? 35.664  38.491  90.596  1.00 37.57 ? 2401 HOH   B O     1 
HETATM 20202 O  O     . HOH   CA 11 .    ? -25.429 6.968   98.679  1.00 33.61 ? 2402 HOH   B O     1 
HETATM 20203 O  O     . HOH   CA 11 .    ? 28.800  46.309  92.550  1.00 36.86 ? 2403 HOH   B O     1 
HETATM 20204 O  O     . HOH   CA 11 .    ? 31.842  53.569  67.955  1.00 25.44 ? 2404 HOH   B O     1 
HETATM 20205 O  O     . HOH   CA 11 .    ? -22.337 9.084   122.184 1.00 38.73 ? 2405 HOH   B O     1 
HETATM 20206 O  O     . HOH   CA 11 .    ? 19.922  23.999  46.319  1.00 22.06 ? 2406 HOH   B O     1 
HETATM 20207 O  O     . HOH   CA 11 .    ? 5.544   69.146  63.334  1.00 37.26 ? 2407 HOH   B O     1 
HETATM 20208 O  O     . HOH   CA 11 .    ? -9.424  18.865  81.065  1.00 35.56 ? 2408 HOH   B O     1 
HETATM 20209 O  O     . HOH   CA 11 .    ? -7.730  35.454  80.951  1.00 34.95 ? 2409 HOH   B O     1 
HETATM 20210 O  O     . HOH   CA 11 .    ? 5.106   62.571  84.207  1.00 21.26 ? 2410 HOH   B O     1 
HETATM 20211 O  O     . HOH   CA 11 .    ? 34.064  47.197  97.852  1.00 40.68 ? 2411 HOH   B O     1 
HETATM 20212 O  O     . HOH   CA 11 .    ? 8.082   74.075  62.080  1.00 41.00 ? 2412 HOH   B O     1 
HETATM 20213 O  O     . HOH   CA 11 .    ? 0.944   -4.426  95.981  1.00 38.44 ? 2413 HOH   B O     1 
HETATM 20214 O  O     . HOH   CA 11 .    ? 17.166  42.555  79.349  1.00 16.01 ? 2414 HOH   B O     1 
HETATM 20215 O  O     . HOH   CA 11 .    ? 24.376  68.503  67.407  1.00 22.18 ? 2415 HOH   B O     1 
HETATM 20216 O  O     . HOH   CA 11 .    ? 3.947   19.011  60.507  1.00 33.20 ? 2416 HOH   B O     1 
HETATM 20217 O  O     . HOH   CA 11 .    ? -0.026  4.007   88.579  1.00 21.94 ? 2417 HOH   B O     1 
HETATM 20218 O  O     . HOH   CA 11 .    ? 3.668   -4.794  98.072  1.00 41.16 ? 2418 HOH   B O     1 
HETATM 20219 O  O     . HOH   CA 11 .    ? 10.714  70.083  86.553  1.00 43.75 ? 2419 HOH   B O     1 
HETATM 20220 O  O     . HOH   CA 11 .    ? -0.661  55.737  121.716 1.00 31.93 ? 2420 HOH   B O     1 
HETATM 20221 O  O     . HOH   CA 11 .    ? -0.496  -1.614  124.599 1.00 41.28 ? 2421 HOH   B O     1 
HETATM 20222 O  O     . HOH   CA 11 .    ? -0.946  55.089  72.360  1.00 30.79 ? 2422 HOH   B O     1 
HETATM 20223 O  O     . HOH   CA 11 .    ? -4.598  50.283  78.608  1.00 29.20 ? 2423 HOH   B O     1 
HETATM 20224 O  O     . HOH   CA 11 .    ? 32.589  32.697  70.777  1.00 26.29 ? 2424 HOH   B O     1 
HETATM 20225 O  O     . HOH   CA 11 .    ? 13.319  1.391   103.598 1.00 39.57 ? 2425 HOH   B O     1 
HETATM 20226 O  O     . HOH   CA 11 .    ? -7.757  29.658  76.089  1.00 24.11 ? 2426 HOH   B O     1 
HETATM 20227 O  O     . HOH   CA 11 .    ? -35.893 21.039  107.051 1.00 44.22 ? 2427 HOH   B O     1 
HETATM 20228 O  O     . HOH   CA 11 .    ? 1.112   55.348  110.506 1.00 28.62 ? 2428 HOH   B O     1 
HETATM 20229 O  O     . HOH   CA 11 .    ? 21.563  29.846  71.500  1.00 14.21 ? 2429 HOH   B O     1 
HETATM 20230 O  O     . HOH   CA 11 .    ? 33.865  37.404  62.093  1.00 26.02 ? 2430 HOH   B O     1 
HETATM 20231 O  O     . HOH   CA 11 .    ? -30.750 20.838  84.045  1.00 43.51 ? 2431 HOH   B O     1 
HETATM 20232 O  O     . HOH   CA 11 .    ? 16.029  42.764  50.407  1.00 31.07 ? 2432 HOH   B O     1 
HETATM 20233 O  O     . HOH   CA 11 .    ? -8.708  23.700  100.958 1.00 18.67 ? 2433 HOH   B O     1 
HETATM 20234 O  O     . HOH   CA 11 .    ? 34.879  26.721  100.195 1.00 39.37 ? 2434 HOH   B O     1 
HETATM 20235 O  O     . HOH   CA 11 .    ? -11.255 20.161  88.274  1.00 20.83 ? 2435 HOH   B O     1 
HETATM 20236 O  O     . HOH   CA 11 .    ? -19.726 27.649  91.367  1.00 36.16 ? 2436 HOH   B O     1 
HETATM 20237 O  O     . HOH   CA 11 .    ? 9.565   -6.181  109.214 1.00 37.38 ? 2437 HOH   B O     1 
HETATM 20238 O  O     . HOH   CA 11 .    ? 8.748   35.433  102.621 1.00 25.07 ? 2438 HOH   B O     1 
HETATM 20239 O  O     . HOH   CA 11 .    ? 6.581   16.002  121.656 1.00 32.47 ? 2439 HOH   B O     1 
HETATM 20240 O  O     . HOH   CA 11 .    ? 10.848  8.923   69.958  1.00 32.85 ? 2440 HOH   B O     1 
HETATM 20241 O  O     . HOH   CA 11 .    ? -10.883 19.861  122.854 1.00 29.61 ? 2441 HOH   B O     1 
HETATM 20242 O  O     . HOH   CA 11 .    ? -1.823  35.455  100.862 1.00 32.27 ? 2442 HOH   B O     1 
HETATM 20243 O  O     . HOH   CA 11 .    ? 1.454   14.709  116.206 1.00 21.73 ? 2443 HOH   B O     1 
HETATM 20244 O  O     . HOH   CA 11 .    ? 27.197  52.372  75.425  1.00 28.52 ? 2444 HOH   B O     1 
HETATM 20245 O  O     . HOH   CA 11 .    ? 28.107  67.229  68.237  1.00 25.28 ? 2445 HOH   B O     1 
HETATM 20246 O  O     . HOH   CA 11 .    ? 5.651   6.920   94.360  1.00 22.16 ? 2446 HOH   B O     1 
HETATM 20247 O  O     . HOH   CA 11 .    ? 23.511  51.623  62.484  1.00 21.08 ? 2447 HOH   B O     1 
HETATM 20248 O  O     . HOH   CA 11 .    ? 11.057  52.682  104.678 1.00 32.57 ? 2448 HOH   B O     1 
HETATM 20249 O  O     . HOH   CA 11 .    ? -28.597 7.816   116.970 1.00 35.96 ? 2449 HOH   B O     1 
HETATM 20250 O  O     . HOH   CA 11 .    ? 18.254  11.211  106.194 1.00 38.59 ? 2450 HOH   B O     1 
HETATM 20251 O  O     . HOH   CA 11 .    ? -20.079 25.110  102.856 1.00 39.06 ? 2451 HOH   B O     1 
HETATM 20252 O  O     . HOH   CA 11 .    ? -5.490  -6.822  112.184 1.00 29.07 ? 2452 HOH   B O     1 
HETATM 20253 O  O     . HOH   CA 11 .    ? -1.847  10.869  101.442 1.00 17.35 ? 2453 HOH   B O     1 
HETATM 20254 O  O     . HOH   CA 11 .    ? 26.753  21.653  75.367  1.00 21.39 ? 2454 HOH   B O     1 
HETATM 20255 O  O     . HOH   CA 11 .    ? 6.822   7.742   75.176  1.00 24.80 ? 2455 HOH   B O     1 
HETATM 20256 O  O     . HOH   CA 11 .    ? 9.870   43.386  110.212 1.00 28.67 ? 2456 HOH   B O     1 
HETATM 20257 O  O     . HOH   CA 11 .    ? -4.025  -0.696  110.750 1.00 23.48 ? 2457 HOH   B O     1 
HETATM 20258 O  O     . HOH   CA 11 .    ? 22.878  37.023  86.041  1.00 15.85 ? 2458 HOH   B O     1 
HETATM 20259 O  O     . HOH   CA 11 .    ? -2.841  -2.623  94.747  1.00 23.69 ? 2459 HOH   B O     1 
HETATM 20260 O  O     . HOH   CA 11 .    ? 12.565  1.763   111.443 1.00 27.94 ? 2460 HOH   B O     1 
HETATM 20261 O  O     . HOH   CA 11 .    ? 12.666  37.038  107.892 1.00 22.96 ? 2461 HOH   B O     1 
HETATM 20262 O  O     . HOH   CA 11 .    ? 7.694   44.701  75.097  1.00 14.97 ? 2462 HOH   B O     1 
HETATM 20263 O  O     . HOH   CA 11 .    ? 20.849  55.203  85.484  1.00 36.78 ? 2463 HOH   B O     1 
HETATM 20264 O  O     . HOH   CA 11 .    ? -2.511  62.576  85.525  1.00 26.42 ? 2464 HOH   B O     1 
HETATM 20265 O  O     . HOH   CA 11 .    ? 12.901  49.746  65.054  1.00 21.78 ? 2465 HOH   B O     1 
HETATM 20266 O  O     . HOH   CA 11 .    ? 0.208   12.058  93.859  1.00 16.77 ? 2466 HOH   B O     1 
HETATM 20267 O  O     . HOH   CA 11 .    ? 15.625  9.779   89.534  1.00 18.68 ? 2467 HOH   B O     1 
HETATM 20268 O  O     . HOH   CA 11 .    ? -8.174  23.694  106.338 1.00 28.65 ? 2468 HOH   B O     1 
HETATM 20269 O  O     . HOH   CA 11 .    ? 15.882  55.314  92.808  1.00 28.70 ? 2469 HOH   B O     1 
HETATM 20270 O  O     . HOH   CA 11 .    ? 16.724  82.249  79.308  1.00 48.18 ? 2470 HOH   B O     1 
HETATM 20271 O  O     . HOH   CA 11 .    ? 11.790  37.034  72.338  1.00 15.14 ? 2471 HOH   B O     1 
HETATM 20272 O  O     . HOH   CA 11 .    ? 20.728  27.321  71.343  1.00 16.23 ? 2472 HOH   B O     1 
HETATM 20273 O  O     . HOH   CA 11 .    ? -3.201  12.107  130.902 1.00 36.69 ? 2473 HOH   B O     1 
HETATM 20274 O  O     . HOH   CA 11 .    ? 6.809   77.112  64.060  1.00 39.05 ? 2474 HOH   B O     1 
HETATM 20275 O  O     . HOH   CA 11 .    ? -0.059  -7.607  107.054 1.00 25.03 ? 2475 HOH   B O     1 
HETATM 20276 O  O     . HOH   CA 11 .    ? 12.262  53.241  90.793  1.00 35.83 ? 2476 HOH   B O     1 
HETATM 20277 O  O     . HOH   CA 11 .    ? 31.773  29.864  74.505  1.00 36.02 ? 2477 HOH   B O     1 
HETATM 20278 O  O     . HOH   CA 11 .    ? -0.036  39.916  77.798  1.00 21.92 ? 2478 HOH   B O     1 
HETATM 20279 O  O     . HOH   CA 11 .    ? 0.971   30.581  74.841  1.00 15.76 ? 2479 HOH   B O     1 
HETATM 20280 O  O     . HOH   CA 11 .    ? -1.212  66.945  75.355  1.00 27.92 ? 2480 HOH   B O     1 
HETATM 20281 O  O     . HOH   CA 11 .    ? 11.560  34.133  51.954  1.00 30.39 ? 2481 HOH   B O     1 
HETATM 20282 O  O     . HOH   CA 11 .    ? -4.423  37.843  93.707  1.00 37.68 ? 2482 HOH   B O     1 
HETATM 20283 O  O     . HOH   CA 11 .    ? 20.973  37.176  112.502 1.00 21.24 ? 2483 HOH   B O     1 
HETATM 20284 O  O     . HOH   CA 11 .    ? 27.467  37.741  89.929  1.00 19.67 ? 2484 HOH   B O     1 
HETATM 20285 O  O     . HOH   CA 11 .    ? -19.256 -3.096  110.432 1.00 40.09 ? 2485 HOH   B O     1 
HETATM 20286 O  O     . HOH   CA 11 .    ? 10.503  24.312  103.522 1.00 28.88 ? 2486 HOH   B O     1 
HETATM 20287 O  O     . HOH   CA 11 .    ? 18.036  68.252  84.548  1.00 35.09 ? 2487 HOH   B O     1 
HETATM 20288 O  O     . HOH   CA 11 .    ? 33.103  28.259  53.142  1.00 36.36 ? 2488 HOH   B O     1 
HETATM 20289 O  O     . HOH   CA 11 .    ? 0.312   27.788  122.215 1.00 38.34 ? 2489 HOH   B O     1 
HETATM 20290 O  O     . HOH   CA 11 .    ? -23.143 3.001   101.525 1.00 37.68 ? 2490 HOH   B O     1 
HETATM 20291 O  O     . HOH   CA 11 .    ? 20.316  50.274  67.092  1.00 24.91 ? 2491 HOH   B O     1 
HETATM 20292 O  O     . HOH   CA 11 .    ? 9.340   61.600  85.186  1.00 25.79 ? 2492 HOH   B O     1 
HETATM 20293 O  O     . HOH   CA 11 .    ? 23.553  55.728  99.152  1.00 28.49 ? 2493 HOH   B O     1 
HETATM 20294 O  O     . HOH   CA 11 .    ? -14.520 23.636  108.480 1.00 25.34 ? 2494 HOH   B O     1 
HETATM 20295 O  O     . HOH   CA 11 .    ? 11.270  41.053  54.500  1.00 19.10 ? 2495 HOH   B O     1 
HETATM 20296 O  O     . HOH   CA 11 .    ? 27.664  31.555  73.934  1.00 20.90 ? 2496 HOH   B O     1 
HETATM 20297 O  O     . HOH   CA 11 .    ? -9.653  5.802   87.172  1.00 24.28 ? 2497 HOH   B O     1 
HETATM 20298 O  O     . HOH   CA 11 .    ? -3.197  65.885  77.195  1.00 28.29 ? 2498 HOH   B O     1 
HETATM 20299 O  O     . HOH   CA 11 .    ? 26.352  39.388  52.922  1.00 26.36 ? 2499 HOH   B O     1 
HETATM 20300 O  O     . HOH   CA 11 .    ? -2.313  23.864  76.641  1.00 24.00 ? 2500 HOH   B O     1 
HETATM 20301 O  O     . HOH   CA 11 .    ? 7.293   32.115  97.525  1.00 33.96 ? 2501 HOH   B O     1 
HETATM 20302 O  O     . HOH   CA 11 .    ? 14.172  80.893  69.500  1.00 39.34 ? 2502 HOH   B O     1 
HETATM 20303 O  O     . HOH   CA 11 .    ? -22.208 20.186  88.365  1.00 30.13 ? 2503 HOH   B O     1 
HETATM 20304 O  O     . HOH   CA 11 .    ? 31.907  58.969  72.169  1.00 24.72 ? 2504 HOH   B O     1 
HETATM 20305 O  O     . HOH   CA 11 .    ? 15.496  61.745  84.515  1.00 34.51 ? 2505 HOH   B O     1 
HETATM 20306 O  O     . HOH   CA 11 .    ? 23.351  48.212  106.870 1.00 32.47 ? 2506 HOH   B O     1 
HETATM 20307 O  O     . HOH   CA 11 .    ? 15.697  37.950  74.602  1.00 15.73 ? 2507 HOH   B O     1 
HETATM 20308 O  O     . HOH   CA 11 .    ? 18.288  52.247  66.686  1.00 22.99 ? 2508 HOH   B O     1 
HETATM 20309 O  O     . HOH   CA 11 .    ? 1.310   -1.081  92.870  1.00 25.29 ? 2509 HOH   B O     1 
HETATM 20310 O  O     . HOH   CA 11 .    ? 18.423  43.477  91.512  1.00 13.33 ? 2510 HOH   B O     1 
HETATM 20311 O  O     . HOH   CA 11 .    ? 25.348  29.823  108.560 1.00 36.07 ? 2511 HOH   B O     1 
HETATM 20312 O  O     . HOH   CA 11 .    ? 14.750  22.218  101.806 1.00 21.33 ? 2512 HOH   B O     1 
HETATM 20313 O  O     . HOH   CA 11 .    ? 8.640   22.971  84.768  1.00 30.43 ? 2513 HOH   B O     1 
HETATM 20314 O  O     . HOH   CA 11 .    ? -10.000 32.083  89.169  1.00 22.05 ? 2514 HOH   B O     1 
HETATM 20315 O  O     . HOH   CA 11 .    ? 2.781   11.353  94.544  1.00 18.52 ? 2515 HOH   B O     1 
HETATM 20316 O  O     . HOH   CA 11 .    ? -6.345  0.034   86.299  1.00 26.94 ? 2516 HOH   B O     1 
HETATM 20317 O  O     . HOH   CA 11 .    ? 35.581  31.818  61.290  1.00 43.59 ? 2517 HOH   B O     1 
HETATM 20318 O  O     . HOH   CA 11 .    ? 19.723  54.500  93.523  1.00 25.08 ? 2518 HOH   B O     1 
HETATM 20319 O  O     . HOH   CA 11 .    ? 6.081   47.835  110.691 1.00 34.04 ? 2519 HOH   B O     1 
HETATM 20320 O  O     . HOH   CA 11 .    ? 25.770  69.077  81.718  1.00 36.05 ? 2520 HOH   B O     1 
HETATM 20321 O  O     . HOH   CA 11 .    ? 5.284   3.137   93.138  1.00 21.89 ? 2521 HOH   B O     1 
HETATM 20322 O  O     . HOH   CA 11 .    ? 2.697   39.195  98.779  1.00 21.84 ? 2522 HOH   B O     1 
HETATM 20323 O  O     . HOH   CA 11 .    ? -4.526  10.557  100.501 1.00 16.83 ? 2523 HOH   B O     1 
HETATM 20324 O  O     . HOH   CA 11 .    ? 25.264  13.525  65.207  1.00 31.17 ? 2524 HOH   B O     1 
HETATM 20325 O  O     . HOH   CA 11 .    ? 1.273   9.059   89.725  1.00 22.81 ? 2525 HOH   B O     1 
HETATM 20326 O  O     . HOH   CA 11 .    ? -28.134 16.302  104.922 1.00 36.62 ? 2526 HOH   B O     1 
HETATM 20327 O  O     . HOH   CA 11 .    ? 18.862  50.049  70.114  1.00 26.32 ? 2527 HOH   B O     1 
HETATM 20328 O  O     . HOH   CA 11 .    ? 39.775  29.320  87.759  1.00 22.90 ? 2528 HOH   B O     1 
HETATM 20329 O  O     . HOH   CA 11 .    ? 8.203   13.521  71.732  1.00 22.59 ? 2529 HOH   B O     1 
HETATM 20330 O  O     . HOH   CA 11 .    ? 23.533  2.306   82.178  1.00 45.78 ? 2530 HOH   B O     1 
HETATM 20331 O  O     . HOH   CA 11 .    ? -11.511 0.785   125.796 1.00 40.99 ? 2531 HOH   B O     1 
HETATM 20332 O  O     . HOH   CA 11 .    ? -2.479  21.119  91.751  1.00 16.67 ? 2532 HOH   B O     1 
HETATM 20333 O  O     . HOH   CA 11 .    ? 12.130  -2.410  110.106 1.00 40.49 ? 2533 HOH   B O     1 
HETATM 20334 O  O     . HOH   CA 11 .    ? 1.558   49.060  89.413  1.00 34.72 ? 2534 HOH   B O     1 
HETATM 20335 O  O     . HOH   CA 11 .    ? 35.942  35.837  56.217  1.00 43.37 ? 2535 HOH   B O     1 
HETATM 20336 O  O     . HOH   CA 11 .    ? 2.470   61.653  68.740  1.00 38.19 ? 2536 HOH   B O     1 
HETATM 20337 O  O     . HOH   CA 11 .    ? 15.894  6.714   108.232 1.00 32.40 ? 2537 HOH   B O     1 
HETATM 20338 O  O     . HOH   CA 11 .    ? -14.410 39.735  124.829 1.00 37.46 ? 2538 HOH   B O     1 
HETATM 20339 O  O     . HOH   CA 11 .    ? -4.610  34.112  56.927  1.00 43.92 ? 2539 HOH   B O     1 
HETATM 20340 O  O     . HOH   CA 11 .    ? -0.142  75.328  68.095  1.00 34.44 ? 2540 HOH   B O     1 
HETATM 20341 O  O     . HOH   CA 11 .    ? 33.071  45.531  67.334  1.00 30.28 ? 2541 HOH   B O     1 
HETATM 20342 O  O     . HOH   CA 11 .    ? 28.122  29.325  83.161  1.00 17.04 ? 2542 HOH   B O     1 
HETATM 20343 O  O     . HOH   CA 11 .    ? -10.269 31.598  80.352  1.00 29.79 ? 2543 HOH   B O     1 
HETATM 20344 O  O     . HOH   CA 11 .    ? 26.229  47.040  100.110 1.00 30.68 ? 2544 HOH   B O     1 
HETATM 20345 O  O     . HOH   CA 11 .    ? 22.649  53.951  93.089  1.00 25.75 ? 2545 HOH   B O     1 
HETATM 20346 O  O     . HOH   CA 11 .    ? -7.822  26.787  99.955  1.00 26.19 ? 2546 HOH   B O     1 
HETATM 20347 O  O     . HOH   CA 11 .    ? 12.062  11.705  121.471 1.00 28.91 ? 2547 HOH   B O     1 
HETATM 20348 O  O     . HOH   CA 11 .    ? 1.788   9.642   79.173  1.00 27.82 ? 2548 HOH   B O     1 
HETATM 20349 O  O     . HOH   CA 11 .    ? -30.374 16.649  123.997 1.00 39.91 ? 2549 HOH   B O     1 
HETATM 20350 O  O     . HOH   CA 11 .    ? -1.870  2.328   125.898 1.00 23.67 ? 2550 HOH   B O     1 
HETATM 20351 O  O     . HOH   CA 11 .    ? 6.669   33.362  86.862  1.00 18.20 ? 2551 HOH   B O     1 
HETATM 20352 O  O     . HOH   CA 11 .    ? 12.015  20.612  59.013  1.00 18.12 ? 2552 HOH   B O     1 
HETATM 20353 O  O     . HOH   CA 11 .    ? 33.304  26.084  59.150  1.00 23.07 ? 2553 HOH   B O     1 
HETATM 20354 O  O     . HOH   CA 11 .    ? 1.190   10.235  129.600 1.00 26.67 ? 2554 HOH   B O     1 
HETATM 20355 O  O     . HOH   CA 11 .    ? -24.049 23.501  104.623 1.00 34.90 ? 2555 HOH   B O     1 
HETATM 20356 O  O     . HOH   CA 11 .    ? 12.574  54.109  85.040  1.00 35.67 ? 2556 HOH   B O     1 
HETATM 20357 O  O     . HOH   CA 11 .    ? 7.443   37.627  102.900 1.00 27.98 ? 2557 HOH   B O     1 
HETATM 20358 O  O     . HOH   CA 11 .    ? 5.906   14.887  94.774  1.00 17.38 ? 2558 HOH   B O     1 
HETATM 20359 O  O     . HOH   CA 11 .    ? -16.308 -8.914  106.345 1.00 35.71 ? 2559 HOH   B O     1 
HETATM 20360 O  O     . HOH   CA 11 .    ? 3.961   10.250  92.357  1.00 18.08 ? 2560 HOH   B O     1 
HETATM 20361 O  O     . HOH   CA 11 .    ? 35.185  64.438  81.314  1.00 20.77 ? 2561 HOH   B O     1 
HETATM 20362 O  O     . HOH   CA 11 .    ? -13.528 11.559  91.319  1.00 17.98 ? 2562 HOH   B O     1 
HETATM 20363 O  O     . HOH   CA 11 .    ? 5.792   55.526  104.689 1.00 24.15 ? 2563 HOH   B O     1 
HETATM 20364 O  O     . HOH   CA 11 .    ? 33.396  22.683  64.453  1.00 30.70 ? 2564 HOH   B O     1 
HETATM 20365 O  O     . HOH   CA 11 .    ? 18.738  8.890   92.263  1.00 38.36 ? 2565 HOH   B O     1 
HETATM 20366 O  O     . HOH   CA 11 .    ? -0.662  -3.229  86.267  1.00 39.34 ? 2566 HOH   B O     1 
HETATM 20367 O  O     . HOH   CA 11 .    ? 2.266   41.193  54.180  1.00 26.15 ? 2567 HOH   B O     1 
HETATM 20368 O  O     . HOH   CA 11 .    ? 20.600  74.893  62.822  1.00 39.81 ? 2568 HOH   B O     1 
HETATM 20369 O  O     . HOH   CA 11 .    ? 19.530  15.733  63.679  1.00 20.66 ? 2569 HOH   B O     1 
HETATM 20370 O  O     . HOH   CA 11 .    ? 22.307  24.269  108.504 1.00 25.59 ? 2570 HOH   B O     1 
HETATM 20371 O  O     . HOH   CA 11 .    ? 38.929  25.469  80.525  1.00 34.57 ? 2571 HOH   B O     1 
HETATM 20372 O  O     . HOH   CA 11 .    ? -2.689  54.637  83.617  1.00 32.31 ? 2572 HOH   B O     1 
HETATM 20373 O  O     . HOH   CA 11 .    ? 23.870  25.737  50.705  1.00 26.42 ? 2573 HOH   B O     1 
HETATM 20374 O  O     A HOH   CA 11 .    ? 0.600   63.300  84.609  0.57 23.24 ? 2574 HOH   B O     1 
HETATM 20375 O  O     . HOH   CA 11 .    ? 0.381   19.944  70.055  1.00 25.08 ? 2575 HOH   B O     1 
HETATM 20376 O  O     . HOH   CA 11 .    ? -6.602  13.977  91.590  1.00 17.21 ? 2576 HOH   B O     1 
HETATM 20377 O  O     . HOH   CA 11 .    ? 26.519  65.147  54.465  1.00 38.94 ? 2577 HOH   B O     1 
HETATM 20378 O  O     . HOH   CA 11 .    ? 26.601  22.164  50.422  1.00 35.60 ? 2578 HOH   B O     1 
HETATM 20379 O  O     . HOH   CA 11 .    ? -14.382 6.838   120.295 1.00 26.87 ? 2579 HOH   B O     1 
HETATM 20380 O  O     . HOH   CA 11 .    ? 24.250  21.451  97.355  1.00 26.64 ? 2580 HOH   B O     1 
HETATM 20381 O  O     . HOH   CA 11 .    ? 4.052   29.322  84.712  1.00 23.98 ? 2581 HOH   B O     1 
HETATM 20382 O  O     . HOH   CA 11 .    ? -0.470  3.459   130.859 1.00 41.03 ? 2582 HOH   B O     1 
HETATM 20383 O  O     . HOH   CA 11 .    ? 3.723   -3.975  92.959  1.00 34.99 ? 2583 HOH   B O     1 
HETATM 20384 O  O     . HOH   CA 11 .    ? -7.890  12.158  97.203  1.00 17.74 ? 2584 HOH   B O     1 
HETATM 20385 O  O     . HOH   CA 11 .    ? 18.025  23.552  110.521 1.00 22.84 ? 2585 HOH   B O     1 
HETATM 20386 O  O     . HOH   CA 11 .    ? -28.112 5.519   101.774 1.00 39.87 ? 2586 HOH   B O     1 
HETATM 20387 O  O     . HOH   CA 11 .    ? 15.418  26.409  81.228  1.00 24.74 ? 2587 HOH   B O     1 
HETATM 20388 O  O     . HOH   CA 11 .    ? 4.456   18.886  97.544  1.00 34.53 ? 2588 HOH   B O     1 
HETATM 20389 O  O     . HOH   CA 11 .    ? 12.518  5.790   84.618  1.00 22.81 ? 2589 HOH   B O     1 
HETATM 20390 O  O     . HOH   CA 11 .    ? 37.520  30.898  81.587  1.00 28.82 ? 2590 HOH   B O     1 
HETATM 20391 O  O     . HOH   CA 11 .    ? 12.087  49.429  88.499  1.00 20.86 ? 2591 HOH   B O     1 
HETATM 20392 O  O     . HOH   CA 11 .    ? 29.043  22.494  76.545  1.00 20.68 ? 2592 HOH   B O     1 
HETATM 20393 O  O     . HOH   CA 11 .    ? 21.103  30.083  113.088 1.00 35.19 ? 2593 HOH   B O     1 
HETATM 20394 O  O     . HOH   CA 11 .    ? 1.850   20.299  89.738  1.00 21.74 ? 2594 HOH   B O     1 
HETATM 20395 O  O     . HOH   CA 11 .    ? 22.839  23.320  84.833  1.00 19.37 ? 2595 HOH   B O     1 
HETATM 20396 O  O     . HOH   CA 11 .    ? 30.746  39.952  57.360  1.00 24.34 ? 2596 HOH   B O     1 
HETATM 20397 O  O     . HOH   CA 11 .    ? -4.081  30.519  94.857  1.00 26.44 ? 2597 HOH   B O     1 
HETATM 20398 O  O     . HOH   CA 11 .    ? -18.798 23.690  115.235 1.00 28.53 ? 2598 HOH   B O     1 
HETATM 20399 O  O     . HOH   CA 11 .    ? 2.866   5.640   80.322  1.00 27.46 ? 2599 HOH   B O     1 
HETATM 20400 O  O     . HOH   CA 11 .    ? 7.029   -8.691  107.557 1.00 35.78 ? 2600 HOH   B O     1 
HETATM 20401 O  O     . HOH   CA 11 .    ? 3.517   40.793  117.246 1.00 27.50 ? 2601 HOH   B O     1 
HETATM 20402 O  O     . HOH   CA 11 .    ? 25.744  33.142  109.874 1.00 40.72 ? 2602 HOH   B O     1 
HETATM 20403 O  O     . HOH   CA 11 .    ? 4.057   17.259  75.473  1.00 26.10 ? 2603 HOH   B O     1 
HETATM 20404 O  O     . HOH   CA 11 .    ? -16.644 4.584   116.616 1.00 24.72 ? 2604 HOH   B O     1 
HETATM 20405 O  O     . HOH   CA 11 .    ? -11.291 -2.307  96.667  1.00 28.24 ? 2605 HOH   B O     1 
HETATM 20406 O  O     . HOH   CA 11 .    ? 8.547   14.550  90.495  1.00 23.74 ? 2606 HOH   B O     1 
HETATM 20407 O  O     . HOH   CA 11 .    ? -18.135 7.754   122.189 1.00 32.12 ? 2607 HOH   B O     1 
HETATM 20408 O  O     . HOH   CA 11 .    ? -2.976  30.615  63.689  1.00 28.57 ? 2608 HOH   B O     1 
HETATM 20409 O  O     . HOH   CA 11 .    ? 16.114  48.192  70.762  1.00 15.79 ? 2609 HOH   B O     1 
HETATM 20410 O  O     . HOH   CA 11 .    ? -6.794  34.993  69.230  1.00 33.38 ? 2610 HOH   B O     1 
HETATM 20411 O  O     . HOH   CA 11 .    ? 0.486   11.036  81.040  1.00 33.53 ? 2611 HOH   B O     1 
HETATM 20412 O  O     . HOH   CA 11 .    ? 8.461   24.661  105.604 1.00 34.47 ? 2612 HOH   B O     1 
HETATM 20413 O  O     . HOH   CA 11 .    ? 29.804  60.013  59.059  1.00 26.70 ? 2613 HOH   B O     1 
HETATM 20414 O  O     . HOH   CA 11 .    ? -6.493  6.090   118.650 1.00 21.15 ? 2614 HOH   B O     1 
HETATM 20415 O  O     . HOH   CA 11 .    ? 19.818  32.703  67.463  1.00 14.56 ? 2615 HOH   B O     1 
HETATM 20416 O  O     . HOH   CA 11 .    ? 23.688  32.730  91.603  1.00 16.93 ? 2616 HOH   B O     1 
HETATM 20417 O  O     . HOH   CA 11 .    ? 2.593   62.988  78.374  1.00 18.52 ? 2617 HOH   B O     1 
HETATM 20418 O  O     . HOH   CA 11 .    ? -9.565  9.870   82.704  1.00 38.86 ? 2618 HOH   B O     1 
HETATM 20419 O  O     . HOH   CA 11 .    ? -8.056  2.181   92.485  1.00 21.47 ? 2619 HOH   B O     1 
HETATM 20420 O  O     . HOH   CA 11 .    ? 20.045  22.175  74.495  1.00 28.05 ? 2620 HOH   B O     1 
HETATM 20421 O  O     . HOH   CA 11 .    ? -14.511 5.781   117.689 1.00 23.05 ? 2621 HOH   B O     1 
HETATM 20422 O  O     . HOH   CA 11 .    ? -4.572  37.021  98.667  1.00 34.38 ? 2622 HOH   B O     1 
HETATM 20423 O  O     . HOH   CA 11 .    ? -15.116 46.859  113.942 1.00 30.87 ? 2623 HOH   B O     1 
HETATM 20424 O  O     . HOH   CA 11 .    ? -6.084  12.392  99.354  1.00 15.47 ? 2624 HOH   B O     1 
HETATM 20425 O  O     . HOH   CA 11 .    ? -4.705  36.643  89.943  1.00 29.81 ? 2625 HOH   B O     1 
HETATM 20426 O  O     . HOH   CA 11 .    ? 0.456   26.605  94.828  1.00 20.44 ? 2626 HOH   B O     1 
HETATM 20427 O  O     . HOH   CA 11 .    ? 14.246  34.337  111.745 1.00 39.86 ? 2627 HOH   B O     1 
HETATM 20428 O  O     . HOH   CA 11 .    ? 10.826  14.744  124.951 1.00 35.16 ? 2628 HOH   B O     1 
HETATM 20429 O  O     . HOH   CA 11 .    ? -1.027  20.461  89.603  1.00 16.95 ? 2629 HOH   B O     1 
HETATM 20430 O  O     . HOH   CA 11 .    ? 22.827  11.596  87.611  1.00 28.94 ? 2630 HOH   B O     1 
HETATM 20431 O  O     . HOH   CA 11 .    ? 8.564   40.415  86.849  1.00 15.37 ? 2631 HOH   B O     1 
HETATM 20432 O  O     . HOH   CA 11 .    ? -5.902  -4.394  120.573 1.00 41.47 ? 2632 HOH   B O     1 
HETATM 20433 O  O     . HOH   CA 11 .    ? 11.755  25.947  101.762 1.00 25.46 ? 2633 HOH   B O     1 
HETATM 20434 O  O     . HOH   CA 11 .    ? -1.570  25.227  80.166  1.00 20.51 ? 2634 HOH   B O     1 
HETATM 20435 O  O     . HOH   CA 11 .    ? 17.117  33.881  56.051  1.00 16.76 ? 2635 HOH   B O     1 
HETATM 20436 O  O     . HOH   CA 11 .    ? 20.329  53.857  81.240  1.00 20.91 ? 2636 HOH   B O     1 
HETATM 20437 O  O     . HOH   CA 11 .    ? 16.013  15.769  85.394  1.00 19.45 ? 2637 HOH   B O     1 
HETATM 20438 O  O     . HOH   CA 11 .    ? 17.428  28.310  110.841 1.00 25.82 ? 2638 HOH   B O     1 
HETATM 20439 O  O     . HOH   CA 11 .    ? 13.313  55.522  65.662  1.00 29.15 ? 2639 HOH   B O     1 
HETATM 20440 O  O     . HOH   CA 11 .    ? 33.385  57.689  74.091  1.00 29.30 ? 2640 HOH   B O     1 
HETATM 20441 O  O     . HOH   CA 11 .    ? -22.118 12.208  126.840 1.00 39.79 ? 2641 HOH   B O     1 
HETATM 20442 O  O     . HOH   CA 11 .    ? 18.669  66.595  58.450  1.00 29.81 ? 2642 HOH   B O     1 
HETATM 20443 O  O     . HOH   CA 11 .    ? -5.845  -7.717  115.755 1.00 35.24 ? 2643 HOH   B O     1 
HETATM 20444 O  O     . HOH   CA 11 .    ? 3.092   22.805  58.946  1.00 31.92 ? 2644 HOH   B O     1 
HETATM 20445 O  O     . HOH   CA 11 .    ? -3.221  -11.515 100.895 1.00 24.29 ? 2645 HOH   B O     1 
HETATM 20446 O  O     . HOH   CA 11 .    ? -0.756  -9.226  102.202 1.00 25.32 ? 2646 HOH   B O     1 
HETATM 20447 O  O     . HOH   CA 11 .    ? 14.609  45.395  78.341  1.00 17.81 ? 2647 HOH   B O     1 
HETATM 20448 O  O     . HOH   CA 11 .    ? 43.865  36.641  87.912  1.00 27.29 ? 2648 HOH   B O     1 
HETATM 20449 O  O     . HOH   CA 11 .    ? 25.973  8.488   78.989  1.00 35.77 ? 2649 HOH   B O     1 
HETATM 20450 O  O     . HOH   CA 11 .    ? 6.535   -4.456  104.680 1.00 27.78 ? 2650 HOH   B O     1 
HETATM 20451 O  O     . HOH   CA 11 .    ? 25.687  53.423  73.829  1.00 22.65 ? 2651 HOH   B O     1 
HETATM 20452 O  O     . HOH   CA 11 .    ? 2.950   69.660  64.270  1.00 35.82 ? 2652 HOH   B O     1 
HETATM 20453 O  O     . HOH   CA 11 .    ? -33.832 10.137  95.883  1.00 42.90 ? 2653 HOH   B O     1 
HETATM 20454 O  O     . HOH   CA 11 .    ? 19.207  7.994   84.169  1.00 26.89 ? 2654 HOH   B O     1 
HETATM 20455 O  O     . HOH   CA 11 .    ? -7.184  36.714  66.270  1.00 40.09 ? 2655 HOH   B O     1 
HETATM 20456 O  O     . HOH   CA 11 .    ? -1.380  31.245  125.602 1.00 38.85 ? 2656 HOH   B O     1 
HETATM 20457 O  O     . HOH   CA 11 .    ? 33.041  44.861  74.986  1.00 27.48 ? 2657 HOH   B O     1 
HETATM 20458 O  O     . HOH   CA 11 .    ? 4.899   21.629  83.841  1.00 21.25 ? 2658 HOH   B O     1 
HETATM 20459 O  O     . HOH   CA 11 .    ? 27.245  18.027  62.032  1.00 23.36 ? 2659 HOH   B O     1 
HETATM 20460 O  O     . HOH   CA 11 .    ? 27.101  48.663  94.640  1.00 28.74 ? 2660 HOH   B O     1 
HETATM 20461 O  O     . HOH   CA 11 .    ? 23.291  72.421  65.068  1.00 31.77 ? 2661 HOH   B O     1 
HETATM 20462 O  O     . HOH   CA 11 .    ? 6.212   51.423  93.742  1.00 40.03 ? 2662 HOH   B O     1 
HETATM 20463 O  O     . HOH   CA 11 .    ? 17.063  52.606  64.136  1.00 26.61 ? 2663 HOH   B O     1 
HETATM 20464 O  O     . HOH   CA 11 .    ? 19.694  18.872  66.396  1.00 15.56 ? 2664 HOH   B O     1 
HETATM 20465 O  O     . HOH   CA 11 .    ? -1.504  49.102  101.313 1.00 29.63 ? 2665 HOH   B O     1 
HETATM 20466 O  O     . HOH   CA 11 .    ? 2.151   40.111  114.421 1.00 26.56 ? 2666 HOH   B O     1 
HETATM 20467 O  O     . HOH   CA 11 .    ? 14.971  6.674   68.979  1.00 28.09 ? 2667 HOH   B O     1 
HETATM 20468 O  O     . HOH   CA 11 .    ? 2.776   32.639  78.478  1.00 14.37 ? 2668 HOH   B O     1 
HETATM 20469 O  O     . HOH   CA 11 .    ? 0.418   36.142  108.843 1.00 34.19 ? 2669 HOH   B O     1 
HETATM 20470 O  O     . HOH   CA 11 .    ? -23.585 30.387  114.312 1.00 43.38 ? 2670 HOH   B O     1 
HETATM 20471 O  O     . HOH   CA 11 .    ? -10.534 1.422   91.466  1.00 23.34 ? 2671 HOH   B O     1 
HETATM 20472 O  O     . HOH   CA 11 .    ? -5.980  41.460  84.116  1.00 31.86 ? 2672 HOH   B O     1 
HETATM 20473 O  O     . HOH   CA 11 .    ? 0.140   19.189  94.150  1.00 20.47 ? 2673 HOH   B O     1 
HETATM 20474 O  O     . HOH   CA 11 .    ? 23.259  12.159  68.127  1.00 26.52 ? 2674 HOH   B O     1 
HETATM 20475 O  O     . HOH   CA 11 .    ? 9.498   56.742  97.516  1.00 29.37 ? 2675 HOH   B O     1 
HETATM 20476 O  O     . HOH   CA 11 .    ? -17.675 54.323  121.178 1.00 41.16 ? 2676 HOH   B O     1 
HETATM 20477 O  O     . HOH   CA 11 .    ? -6.059  34.127  83.935  1.00 22.45 ? 2677 HOH   B O     1 
HETATM 20478 O  O     . HOH   CA 11 .    ? 10.071  51.801  107.801 1.00 44.41 ? 2678 HOH   B O     1 
HETATM 20479 O  O     . HOH   CA 11 .    ? -13.478 12.253  93.986  1.00 17.77 ? 2679 HOH   B O     1 
HETATM 20480 O  O     . HOH   CA 11 .    ? 29.907  32.812  73.589  1.00 22.59 ? 2680 HOH   B O     1 
HETATM 20481 O  O     . HOH   CA 11 .    ? -5.200  -2.553  117.144 1.00 27.39 ? 2681 HOH   B O     1 
HETATM 20482 O  O     . HOH   CA 11 .    ? 33.187  37.623  104.416 1.00 31.19 ? 2682 HOH   B O     1 
HETATM 20483 O  O     . HOH   CA 11 .    ? -14.185 9.068   87.471  1.00 24.21 ? 2683 HOH   B O     1 
HETATM 20484 O  O     . HOH   CA 11 .    ? 25.201  23.360  81.767  1.00 28.08 ? 2684 HOH   B O     1 
HETATM 20485 O  O     . HOH   CA 11 .    ? -5.430  12.376  84.510  1.00 26.25 ? 2685 HOH   B O     1 
HETATM 20486 O  O     . HOH   CA 11 .    ? 1.892   65.647  65.672  1.00 41.16 ? 2686 HOH   B O     1 
HETATM 20487 O  O     . HOH   CA 11 .    ? 20.460  52.166  69.336  1.00 20.92 ? 2687 HOH   B O     1 
HETATM 20488 O  O     . HOH   CA 11 .    ? -1.011  60.249  77.421  1.00 21.35 ? 2688 HOH   B O     1 
HETATM 20489 O  O     . HOH   CA 11 .    ? 27.366  22.721  88.703  1.00 17.40 ? 2689 HOH   B O     1 
HETATM 20490 O  O     . HOH   CA 11 .    ? 34.618  54.475  75.743  1.00 37.02 ? 2690 HOH   B O     1 
HETATM 20491 O  O     . HOH   CA 11 .    ? -1.137  50.611  64.969  1.00 18.96 ? 2691 HOH   B O     1 
HETATM 20492 O  O     . HOH   CA 11 .    ? -1.391  5.136   92.273  1.00 19.01 ? 2692 HOH   B O     1 
HETATM 20493 O  O     . HOH   CA 11 .    ? 12.258  7.604   90.516  1.00 22.90 ? 2693 HOH   B O     1 
HETATM 20494 O  O     . HOH   CA 11 .    ? -2.500  59.832  120.088 1.00 27.91 ? 2694 HOH   B O     1 
HETATM 20495 O  O     . HOH   CA 11 .    ? 36.604  20.502  78.557  1.00 39.48 ? 2695 HOH   B O     1 
HETATM 20496 O  O     . HOH   CA 11 .    ? 28.739  46.172  87.808  1.00 29.38 ? 2696 HOH   B O     1 
HETATM 20497 O  O     . HOH   CA 11 .    ? 27.303  42.288  104.810 1.00 28.46 ? 2697 HOH   B O     1 
HETATM 20498 O  O     . HOH   CA 11 .    ? -31.705 14.500  114.265 1.00 36.26 ? 2698 HOH   B O     1 
HETATM 20499 O  O     . HOH   CA 11 .    ? 23.718  51.491  83.790  1.00 25.14 ? 2699 HOH   B O     1 
HETATM 20500 O  O     . HOH   CA 11 .    ? 4.877   18.416  124.211 1.00 26.19 ? 2700 HOH   B O     1 
HETATM 20501 O  O     . HOH   CA 11 .    ? 0.336   47.456  76.493  1.00 18.98 ? 2701 HOH   B O     1 
HETATM 20502 O  O     . HOH   CA 11 .    ? 1.578   14.897  82.414  1.00 19.79 ? 2702 HOH   B O     1 
HETATM 20503 O  O     . HOH   CA 11 .    ? 1.709   46.156  98.973  1.00 27.22 ? 2703 HOH   B O     1 
HETATM 20504 O  O     . HOH   CA 11 .    ? 18.666  13.277  74.635  1.00 24.87 ? 2704 HOH   B O     1 
HETATM 20505 O  O     . HOH   CA 11 .    ? 9.450   18.649  103.802 1.00 21.21 ? 2705 HOH   B O     1 
HETATM 20506 O  O     . HOH   CA 11 .    ? 16.992  33.482  48.685  1.00 29.58 ? 2706 HOH   B O     1 
HETATM 20507 O  O     . HOH   CA 11 .    ? 28.141  65.226  84.613  1.00 42.22 ? 2707 HOH   B O     1 
HETATM 20508 O  O     . HOH   CA 11 .    ? 24.930  50.578  67.165  1.00 21.93 ? 2708 HOH   B O     1 
HETATM 20509 O  O     . HOH   CA 11 .    ? -9.254  32.572  69.829  1.00 42.70 ? 2709 HOH   B O     1 
HETATM 20510 O  O     . HOH   CA 11 .    ? 13.391  25.629  96.019  1.00 27.05 ? 2710 HOH   B O     1 
HETATM 20511 O  O     . HOH   CA 11 .    ? 8.040   65.502  68.531  1.00 30.52 ? 2711 HOH   B O     1 
HETATM 20512 O  O     . HOH   CA 11 .    ? -2.898  10.661  103.874 1.00 17.23 ? 2712 HOH   B O     1 
HETATM 20513 O  O     . HOH   CA 11 .    ? 15.386  53.738  66.564  1.00 26.32 ? 2713 HOH   B O     1 
HETATM 20514 O  O     . HOH   CA 11 .    ? 4.770   46.307  69.240  1.00 15.32 ? 2714 HOH   B O     1 
HETATM 20515 O  O     . HOH   CA 11 .    ? -1.050  66.520  83.906  1.00 28.62 ? 2715 HOH   B O     1 
HETATM 20516 O  O     . HOH   CA 11 .    ? 4.971   17.643  91.265  1.00 22.45 ? 2716 HOH   B O     1 
HETATM 20517 O  O     . HOH   CA 11 .    ? 18.379  14.695  97.582  1.00 26.39 ? 2717 HOH   B O     1 
HETATM 20518 O  O     . HOH   CA 11 .    ? 31.549  52.116  65.642  1.00 30.00 ? 2718 HOH   B O     1 
HETATM 20519 O  O     . HOH   CA 11 .    ? 36.690  19.972  64.545  1.00 41.40 ? 2719 HOH   B O     1 
HETATM 20520 O  O     . HOH   CA 11 .    ? 15.308  48.587  57.325  1.00 27.22 ? 2720 HOH   B O     1 
HETATM 20521 O  O     . HOH   CA 11 .    ? -29.692 17.961  103.714 1.00 29.42 ? 2721 HOH   B O     1 
HETATM 20522 O  O     . HOH   CA 11 .    ? -4.956  16.050  97.009  1.00 16.09 ? 2722 HOH   B O     1 
HETATM 20523 O  O     . HOH   CA 11 .    ? 2.116   19.904  92.490  1.00 33.34 ? 2723 HOH   B O     1 
HETATM 20524 O  O     . HOH   CA 11 .    ? 10.082  2.104   117.405 1.00 27.18 ? 2724 HOH   B O     1 
HETATM 20525 O  O     . HOH   CA 11 .    ? 25.181  52.967  68.534  1.00 24.12 ? 2725 HOH   B O     1 
HETATM 20526 O  O     . HOH   CA 11 .    ? 10.825  29.114  94.211  1.00 25.37 ? 2726 HOH   B O     1 
HETATM 20527 O  O     . HOH   CA 11 .    ? 12.593  1.970   92.291  1.00 35.50 ? 2727 HOH   B O     1 
HETATM 20528 O  O     . HOH   CA 11 .    ? -37.200 13.277  94.895  1.00 49.19 ? 2728 HOH   B O     1 
HETATM 20529 O  O     . HOH   CA 11 .    ? -28.955 26.173  120.629 1.00 42.83 ? 2729 HOH   B O     1 
HETATM 20530 O  O     . HOH   CA 11 .    ? 11.781  16.085  67.821  1.00 31.87 ? 2730 HOH   B O     1 
HETATM 20531 O  O     . HOH   CA 11 .    ? 30.621  19.894  73.746  1.00 33.42 ? 2731 HOH   B O     1 
HETATM 20532 O  O     . HOH   CA 11 .    ? 18.123  76.086  63.811  1.00 31.07 ? 2732 HOH   B O     1 
HETATM 20533 O  O     . HOH   CA 11 .    ? 30.907  51.426  74.499  1.00 39.11 ? 2733 HOH   B O     1 
HETATM 20534 O  O     . HOH   CA 11 .    ? 22.931  9.680   85.284  1.00 39.19 ? 2734 HOH   B O     1 
HETATM 20535 O  O     . HOH   CA 11 .    ? -12.637 49.228  130.134 1.00 43.79 ? 2735 HOH   B O     1 
HETATM 20536 O  O     . HOH   CA 11 .    ? 21.231  47.266  56.039  1.00 30.51 ? 2736 HOH   B O     1 
HETATM 20537 O  O     . HOH   CA 11 .    ? 4.746   77.371  80.279  1.00 29.93 ? 2737 HOH   B O     1 
HETATM 20538 O  O     . HOH   CA 11 .    ? 14.134  3.261   84.811  1.00 40.85 ? 2738 HOH   B O     1 
HETATM 20539 O  O     . HOH   CA 11 .    ? -4.843  42.310  72.868  1.00 29.75 ? 2739 HOH   B O     1 
HETATM 20540 O  O     . HOH   CA 11 .    ? 22.140  45.975  76.723  1.00 18.63 ? 2740 HOH   B O     1 
HETATM 20541 O  O     . HOH   CA 11 .    ? 7.540   20.305  102.316 1.00 27.86 ? 2741 HOH   B O     1 
HETATM 20542 O  O     . HOH   CA 11 .    ? 16.474  21.243  99.812  1.00 20.48 ? 2742 HOH   B O     1 
HETATM 20543 O  O     . HOH   CA 11 .    ? 29.129  23.730  51.181  1.00 31.65 ? 2743 HOH   B O     1 
HETATM 20544 O  O     . HOH   CA 11 .    ? 29.931  57.809  82.293  1.00 38.47 ? 2744 HOH   B O     1 
HETATM 20545 O  O     . HOH   CA 11 .    ? 19.184  51.767  79.985  1.00 20.24 ? 2745 HOH   B O     1 
HETATM 20546 O  O     . HOH   CA 11 .    ? -4.220  55.474  81.701  1.00 28.32 ? 2746 HOH   B O     1 
HETATM 20547 O  O     . HOH   CA 11 .    ? 31.158  66.965  82.354  1.00 31.62 ? 2747 HOH   B O     1 
HETATM 20548 O  O     . HOH   CA 11 .    ? 2.865   44.034  58.538  1.00 30.07 ? 2748 HOH   B O     1 
HETATM 20549 O  O     . HOH   CA 11 .    ? 26.330  27.263  67.211  1.00 16.32 ? 2749 HOH   B O     1 
HETATM 20550 O  O     . HOH   CA 11 .    ? -24.791 16.658  82.109  1.00 31.11 ? 2750 HOH   B O     1 
HETATM 20551 O  O     . HOH   CA 11 .    ? -2.936  33.493  62.563  1.00 23.56 ? 2751 HOH   B O     1 
HETATM 20552 O  O     . HOH   CA 11 .    ? -6.561  34.547  129.195 1.00 40.03 ? 2752 HOH   B O     1 
HETATM 20553 O  O     . HOH   CA 11 .    ? 27.199  35.155  90.935  1.00 17.35 ? 2753 HOH   B O     1 
HETATM 20554 O  O     . HOH   CA 11 .    ? 0.954   -8.236  109.496 1.00 29.61 ? 2754 HOH   B O     1 
HETATM 20555 O  O     . HOH   CA 11 .    ? 6.519   11.852  126.616 1.00 20.40 ? 2755 HOH   B O     1 
HETATM 20556 O  O     . HOH   CA 11 .    ? 24.045  31.323  110.361 1.00 27.78 ? 2756 HOH   B O     1 
HETATM 20557 O  O     . HOH   CA 11 .    ? 25.087  57.123  78.324  1.00 21.34 ? 2757 HOH   B O     1 
HETATM 20558 O  O     . HOH   CA 11 .    ? 41.315  34.312  91.242  1.00 24.78 ? 2758 HOH   B O     1 
HETATM 20559 O  O     . HOH   CA 11 .    ? 33.085  25.238  101.997 1.00 28.82 ? 2759 HOH   B O     1 
HETATM 20560 O  O     . HOH   CA 11 .    ? -5.953  37.079  96.330  1.00 41.72 ? 2760 HOH   B O     1 
HETATM 20561 O  O     . HOH   CA 11 .    ? -12.063 7.617   127.152 1.00 27.14 ? 2761 HOH   B O     1 
HETATM 20562 O  O     . HOH   CA 11 .    ? 5.296   42.447  70.804  1.00 14.19 ? 2762 HOH   B O     1 
HETATM 20563 O  O     . HOH   CA 11 .    ? -14.898 18.484  80.217  1.00 31.25 ? 2763 HOH   B O     1 
HETATM 20564 O  O     . HOH   CA 11 .    ? 6.808   81.697  75.475  1.00 33.65 ? 2764 HOH   B O     1 
HETATM 20565 O  O     . HOH   CA 11 .    ? 2.637   -2.916  86.169  1.00 42.77 ? 2765 HOH   B O     1 
HETATM 20566 O  O     . HOH   CA 11 .    ? 22.957  61.223  83.086  1.00 32.63 ? 2766 HOH   B O     1 
HETATM 20567 O  O     . HOH   CA 11 .    ? -16.085 4.245   92.974  1.00 39.27 ? 2767 HOH   B O     1 
HETATM 20568 O  O     . HOH   CA 11 .    ? 3.210   35.185  121.247 1.00 34.03 ? 2768 HOH   B O     1 
HETATM 20569 O  O     . HOH   CA 11 .    ? -16.242 26.336  83.006  1.00 40.68 ? 2769 HOH   B O     1 
HETATM 20570 O  O     . HOH   CA 11 .    ? -3.276  45.718  106.988 1.00 24.20 ? 2770 HOH   B O     1 
HETATM 20571 O  O     . HOH   CA 11 .    ? 18.637  52.933  75.948  1.00 18.87 ? 2771 HOH   B O     1 
HETATM 20572 O  O     . HOH   CA 11 .    ? 27.283  58.825  78.587  1.00 20.54 ? 2772 HOH   B O     1 
HETATM 20573 O  O     . HOH   CA 11 .    ? -9.092  45.413  131.021 1.00 32.56 ? 2773 HOH   B O     1 
HETATM 20574 O  O     . HOH   CA 11 .    ? 14.808  16.423  92.055  1.00 21.43 ? 2774 HOH   B O     1 
HETATM 20575 O  O     . HOH   CA 11 .    ? 18.661  47.710  90.039  1.00 21.19 ? 2775 HOH   B O     1 
HETATM 20576 O  O     . HOH   CA 11 .    ? 5.665   11.629  77.821  1.00 28.94 ? 2776 HOH   B O     1 
HETATM 20577 O  O     . HOH   CA 11 .    ? -1.560  36.497  87.421  1.00 20.06 ? 2777 HOH   B O     1 
HETATM 20578 O  O     . HOH   CA 11 .    ? -3.922  52.477  79.987  1.00 31.03 ? 2778 HOH   B O     1 
HETATM 20579 O  O     . HOH   CA 11 .    ? -4.363  44.453  108.804 1.00 27.66 ? 2779 HOH   B O     1 
HETATM 20580 O  O     . HOH   CA 11 .    ? 38.608  32.319  83.816  1.00 28.99 ? 2780 HOH   B O     1 
HETATM 20581 O  O     . HOH   CA 11 .    ? 30.707  34.064  84.561  1.00 27.80 ? 2781 HOH   B O     1 
HETATM 20582 O  O     . HOH   CA 11 .    ? 18.095  53.590  82.892  1.00 24.39 ? 2782 HOH   B O     1 
HETATM 20583 O  O     . HOH   CA 11 .    ? 10.726  33.137  109.419 1.00 25.77 ? 2783 HOH   B O     1 
HETATM 20584 O  O     . HOH   CA 11 .    ? 28.346  48.663  97.864  1.00 36.83 ? 2784 HOH   B O     1 
HETATM 20585 O  O     . HOH   CA 11 .    ? 26.259  19.879  53.021  1.00 30.08 ? 2785 HOH   B O     1 
HETATM 20586 O  O     . HOH   CA 11 .    ? 18.676  10.569  114.202 1.00 45.07 ? 2786 HOH   B O     1 
HETATM 20587 O  O     . HOH   CA 11 .    ? 17.462  33.812  68.425  1.00 14.28 ? 2787 HOH   B O     1 
HETATM 20588 O  O     . HOH   CA 11 .    ? 36.992  21.359  83.791  1.00 31.82 ? 2788 HOH   B O     1 
HETATM 20589 O  O     . HOH   CA 11 .    ? 8.162   57.781  85.210  1.00 24.44 ? 2789 HOH   B O     1 
HETATM 20590 O  O     . HOH   CA 11 .    ? 18.946  30.245  88.560  1.00 18.05 ? 2790 HOH   B O     1 
HETATM 20591 O  O     . HOH   CA 11 .    ? 2.676   48.691  76.148  1.00 19.26 ? 2791 HOH   B O     1 
HETATM 20592 O  O     . HOH   CA 11 .    ? -16.262 25.060  106.929 1.00 31.29 ? 2792 HOH   B O     1 
HETATM 20593 O  O     . HOH   CA 11 .    ? 33.450  19.067  87.608  1.00 23.23 ? 2793 HOH   B O     1 
HETATM 20594 O  O     . HOH   CA 11 .    ? -2.709  25.957  60.539  1.00 35.90 ? 2794 HOH   B O     1 
HETATM 20595 O  O     . HOH   CA 11 .    ? 1.428   22.197  63.688  1.00 24.08 ? 2795 HOH   B O     1 
HETATM 20596 O  O     . HOH   CA 11 .    ? 5.796   66.358  61.837  1.00 36.69 ? 2796 HOH   B O     1 
HETATM 20597 O  O     . HOH   CA 11 .    ? 27.955  10.530  84.919  1.00 28.55 ? 2797 HOH   B O     1 
HETATM 20598 O  O     . HOH   CA 11 .    ? 32.557  28.850  64.683  1.00 22.14 ? 2798 HOH   B O     1 
HETATM 20599 O  O     . HOH   CA 11 .    ? -1.629  -1.324  109.097 1.00 25.03 ? 2799 HOH   B O     1 
HETATM 20600 O  O     . HOH   CA 11 .    ? 24.985  15.801  95.176  1.00 25.44 ? 2800 HOH   B O     1 
HETATM 20601 O  O     . HOH   CA 11 .    ? 0.802   40.776  51.965  1.00 40.02 ? 2801 HOH   B O     1 
HETATM 20602 O  O     . HOH   CA 11 .    ? 5.015   48.859  54.304  1.00 41.10 ? 2802 HOH   B O     1 
HETATM 20603 O  O     . HOH   CA 11 .    ? 18.437  14.432  105.253 1.00 36.45 ? 2803 HOH   B O     1 
HETATM 20604 O  O     . HOH   CA 11 .    ? 11.158  20.141  120.358 1.00 38.64 ? 2804 HOH   B O     1 
HETATM 20605 O  O     . HOH   CA 11 .    ? 8.053   40.765  122.144 1.00 41.07 ? 2805 HOH   B O     1 
HETATM 20606 O  O     . HOH   CA 11 .    ? 28.855  58.899  84.422  1.00 39.24 ? 2806 HOH   B O     1 
HETATM 20607 O  O     . HOH   CA 11 .    ? -5.532  35.374  87.785  1.00 28.89 ? 2807 HOH   B O     1 
HETATM 20608 O  O     . HOH   CA 11 .    ? 0.804   -0.172  96.297  1.00 24.65 ? 2808 HOH   B O     1 
HETATM 20609 O  O     . HOH   CA 11 .    ? 8.337   62.483  66.292  1.00 33.83 ? 2809 HOH   B O     1 
HETATM 20610 O  O     . HOH   CA 11 .    ? -15.284 10.002  89.901  1.00 19.84 ? 2810 HOH   B O     1 
HETATM 20611 O  O     . HOH   CA 11 .    ? 18.188  23.013  61.472  1.00 20.10 ? 2811 HOH   B O     1 
HETATM 20612 O  O     . HOH   CA 11 .    ? -9.294  0.314   112.648 1.00 23.17 ? 2812 HOH   B O     1 
HETATM 20613 O  O     . HOH   CA 11 .    ? -28.781 16.981  117.533 1.00 33.35 ? 2813 HOH   B O     1 
HETATM 20614 O  O     A HOH   CA 11 .    ? 2.056   60.603  80.957  0.57 19.76 ? 2814 HOH   B O     1 
HETATM 20615 O  O     . HOH   CA 11 .    ? -7.102  27.512  74.417  1.00 26.23 ? 2815 HOH   B O     1 
HETATM 20616 O  O     . HOH   CA 11 .    ? 27.837  50.316  100.428 1.00 41.01 ? 2816 HOH   B O     1 
HETATM 20617 O  O     . HOH   CA 11 .    ? 8.968   5.759   85.169  1.00 20.46 ? 2817 HOH   B O     1 
HETATM 20618 O  O     . HOH   CA 11 .    ? 16.996  51.097  59.980  1.00 26.72 ? 2818 HOH   B O     1 
HETATM 20619 O  O     . HOH   CA 11 .    ? 10.207  21.745  102.758 1.00 30.98 ? 2819 HOH   B O     1 
HETATM 20620 O  O     . HOH   CA 11 .    ? -13.857 -8.300  103.304 1.00 34.88 ? 2820 HOH   B O     1 
HETATM 20621 O  O     . HOH   CA 11 .    ? 11.066  15.993  121.866 1.00 33.28 ? 2821 HOH   B O     1 
HETATM 20622 O  O     . HOH   CA 11 .    ? 2.570   3.456   84.771  1.00 31.78 ? 2822 HOH   B O     1 
HETATM 20623 O  O     . HOH   CA 11 .    ? -1.756  27.861  62.815  1.00 24.76 ? 2823 HOH   B O     1 
HETATM 20624 O  O     . HOH   CA 11 .    ? 1.496   38.522  105.521 1.00 31.35 ? 2824 HOH   B O     1 
HETATM 20625 O  O     . HOH   CA 11 .    ? -4.147  53.721  130.701 1.00 35.55 ? 2825 HOH   B O     1 
HETATM 20626 O  O     . HOH   CA 11 .    ? -10.560 51.965  128.515 1.00 35.73 ? 2826 HOH   B O     1 
HETATM 20627 O  O     . HOH   CA 11 .    ? -2.429  14.221  98.865  1.00 15.99 ? 2827 HOH   B O     1 
HETATM 20628 O  O     . HOH   CA 11 .    ? -31.711 20.597  98.410  1.00 44.49 ? 2828 HOH   B O     1 
HETATM 20629 O  O     . HOH   CA 11 .    ? 21.556  53.459  83.557  1.00 26.12 ? 2829 HOH   B O     1 
HETATM 20630 O  O     . HOH   CA 11 .    ? -5.391  22.796  80.721  1.00 21.59 ? 2830 HOH   B O     1 
HETATM 20631 O  O     . HOH   CA 11 .    ? 13.260  47.817  82.146  1.00 25.45 ? 2831 HOH   B O     1 
HETATM 20632 O  O     . HOH   CA 11 .    ? 10.589  66.268  86.587  1.00 39.07 ? 2832 HOH   B O     1 
HETATM 20633 O  O     . HOH   CA 11 .    ? 27.486  39.112  104.677 1.00 31.00 ? 2833 HOH   B O     1 
HETATM 20634 O  O     . HOH   CA 11 .    ? -4.638  56.168  127.100 1.00 37.48 ? 2834 HOH   B O     1 
HETATM 20635 O  O     . HOH   CA 11 .    ? 9.303   31.711  83.873  1.00 25.71 ? 2835 HOH   B O     1 
HETATM 20636 O  O     . HOH   CA 11 .    ? -0.806  13.231  100.837 1.00 16.36 ? 2836 HOH   B O     1 
HETATM 20637 O  O     . HOH   CA 11 .    ? 8.356   31.478  94.022  1.00 24.85 ? 2837 HOH   B O     1 
HETATM 20638 O  O     . HOH   CA 11 .    ? 28.158  25.285  67.800  1.00 19.12 ? 2838 HOH   B O     1 
HETATM 20639 O  O     . HOH   CA 11 .    ? -13.315 53.703  122.603 1.00 29.08 ? 2839 HOH   B O     1 
HETATM 20640 O  O     . HOH   CA 11 .    ? 16.549  53.472  104.878 1.00 28.34 ? 2840 HOH   B O     1 
HETATM 20641 O  O     . HOH   CA 11 .    ? 28.201  8.740   73.938  1.00 31.90 ? 2841 HOH   B O     1 
HETATM 20642 O  O     . HOH   CA 11 .    ? 31.285  50.805  79.863  1.00 30.62 ? 2842 HOH   B O     1 
HETATM 20643 O  O     . HOH   CA 11 .    ? -5.904  35.336  92.556  1.00 28.66 ? 2843 HOH   B O     1 
HETATM 20644 O  O     . HOH   CA 11 .    ? 8.468   37.133  79.204  1.00 17.27 ? 2844 HOH   B O     1 
HETATM 20645 O  O     . HOH   CA 11 .    ? 5.701   18.287  87.471  1.00 26.09 ? 2845 HOH   B O     1 
HETATM 20646 O  O     . HOH   CA 11 .    ? 35.565  25.222  77.719  1.00 25.81 ? 2846 HOH   B O     1 
HETATM 20647 O  O     . HOH   CA 11 .    ? -20.341 25.027  94.633  1.00 25.62 ? 2847 HOH   B O     1 
HETATM 20648 O  O     . HOH   CA 11 .    ? -7.657  2.616   130.767 1.00 41.40 ? 2848 HOH   B O     1 
HETATM 20649 O  O     . HOH   CA 11 .    ? -0.139  39.200  131.355 1.00 39.11 ? 2849 HOH   B O     1 
HETATM 20650 O  O     . HOH   CA 11 .    ? -10.596 36.092  76.461  1.00 40.34 ? 2850 HOH   B O     1 
HETATM 20651 O  O     . HOH   CA 11 .    ? 2.059   30.333  96.021  1.00 20.42 ? 2851 HOH   B O     1 
HETATM 20652 O  O     . HOH   CA 11 .    ? -34.289 12.897  111.153 1.00 35.10 ? 2852 HOH   B O     1 
HETATM 20653 O  O     . HOH   CA 11 .    ? 10.122  52.905  65.668  1.00 23.98 ? 2853 HOH   B O     1 
HETATM 20654 O  O     . HOH   CA 11 .    ? 19.775  77.742  77.027  1.00 40.86 ? 2854 HOH   B O     1 
HETATM 20655 O  O     . HOH   CA 11 .    ? 31.171  34.162  77.305  1.00 26.07 ? 2855 HOH   B O     1 
HETATM 20656 O  O     . HOH   CA 11 .    ? 35.121  32.091  55.122  1.00 30.80 ? 2856 HOH   B O     1 
HETATM 20657 O  O     . HOH   CA 11 .    ? 29.560  32.145  103.253 1.00 26.08 ? 2857 HOH   B O     1 
HETATM 20658 O  O     . HOH   CA 11 .    ? -11.832 21.654  85.711  1.00 21.62 ? 2858 HOH   B O     1 
HETATM 20659 O  O     . HOH   CA 11 .    ? 28.394  44.121  89.750  1.00 24.11 ? 2859 HOH   B O     1 
HETATM 20660 O  O     . HOH   CA 11 .    ? 4.770   -4.028  95.373  1.00 33.92 ? 2860 HOH   B O     1 
HETATM 20661 O  O     . HOH   CA 11 .    ? 5.128   57.497  68.930  1.00 24.32 ? 2861 HOH   B O     1 
HETATM 20662 O  O     . HOH   CA 11 .    ? -8.501  31.261  86.962  1.00 18.52 ? 2862 HOH   B O     1 
HETATM 20663 O  O     . HOH   CA 11 .    ? 29.590  41.249  80.055  1.00 26.20 ? 2863 HOH   B O     1 
HETATM 20664 O  O     . HOH   CA 11 .    ? 22.118  24.841  82.582  1.00 22.25 ? 2864 HOH   B O     1 
HETATM 20665 O  O     . HOH   CA 11 .    ? -0.339  17.724  91.576  1.00 22.10 ? 2865 HOH   B O     1 
HETATM 20666 O  O     . HOH   CA 11 .    ? -22.907 25.359  103.494 1.00 34.83 ? 2866 HOH   B O     1 
HETATM 20667 O  O     . HOH   CA 11 .    ? 15.306  35.926  79.362  1.00 20.85 ? 2867 HOH   B O     1 
HETATM 20668 O  O     . HOH   CA 11 .    ? 9.592   29.084  98.365  1.00 29.29 ? 2868 HOH   B O     1 
HETATM 20669 O  O     . HOH   CA 11 .    ? 23.180  72.527  81.673  1.00 29.53 ? 2869 HOH   B O     1 
HETATM 20670 O  O     . HOH   CA 11 .    ? 34.166  22.224  78.224  1.00 26.08 ? 2870 HOH   B O     1 
HETATM 20671 O  O     . HOH   CA 11 .    ? -15.845 51.909  123.572 1.00 37.28 ? 2871 HOH   B O     1 
HETATM 20672 O  O     . HOH   CA 11 .    ? -16.226 21.704  82.439  1.00 26.52 ? 2872 HOH   B O     1 
HETATM 20673 O  O     . HOH   CA 11 .    ? -1.924  57.342  75.252  1.00 18.39 ? 2873 HOH   B O     1 
HETATM 20674 O  O     . HOH   CA 11 .    ? -2.517  30.190  70.754  1.00 19.54 ? 2874 HOH   B O     1 
HETATM 20675 O  O     . HOH   CA 11 .    ? -8.279  -2.119  124.368 1.00 41.22 ? 2875 HOH   B O     1 
HETATM 20676 O  O     . HOH   CA 11 .    ? -7.307  12.922  94.607  1.00 16.30 ? 2876 HOH   B O     1 
HETATM 20677 O  O     . HOH   CA 11 .    ? -17.001 27.211  115.846 1.00 42.16 ? 2877 HOH   B O     1 
HETATM 20678 O  O     . HOH   CA 11 .    ? -18.402 43.575  125.023 1.00 45.06 ? 2878 HOH   B O     1 
HETATM 20679 O  O     . HOH   CA 11 .    ? 37.801  29.513  102.457 1.00 39.16 ? 2879 HOH   B O     1 
HETATM 20680 O  O     . HOH   CA 11 .    ? 0.596   25.789  112.260 1.00 44.52 ? 2880 HOH   B O     1 
HETATM 20681 O  O     . HOH   CA 11 .    ? 34.885  16.649  67.730  1.00 28.22 ? 2881 HOH   B O     1 
HETATM 20682 O  O     . HOH   CA 11 .    ? 36.026  31.170  103.829 1.00 33.54 ? 2882 HOH   B O     1 
HETATM 20683 O  O     . HOH   CA 11 .    ? 1.133   80.477  75.438  1.00 41.69 ? 2883 HOH   B O     1 
HETATM 20684 O  O     . HOH   CA 11 .    ? 5.011   47.131  87.115  1.00 20.05 ? 2884 HOH   B O     1 
HETATM 20685 O  O     . HOH   CA 11 .    ? 7.600   66.031  86.497  1.00 31.36 ? 2885 HOH   B O     1 
HETATM 20686 O  O     . HOH   CA 11 .    ? -2.132  -7.871  110.552 1.00 22.94 ? 2886 HOH   B O     1 
HETATM 20687 O  O     . HOH   CA 11 .    ? 2.710   48.674  99.043  1.00 21.96 ? 2887 HOH   B O     1 
HETATM 20688 O  O     . HOH   CA 11 .    ? 20.658  21.626  61.051  1.00 17.23 ? 2888 HOH   B O     1 
HETATM 20689 O  O     . HOH   CA 11 .    ? 30.684  46.516  61.048  1.00 42.46 ? 2889 HOH   B O     1 
HETATM 20690 O  O     . HOH   CA 11 .    ? 16.917  46.631  54.703  1.00 34.77 ? 2890 HOH   B O     1 
HETATM 20691 O  O     . HOH   CA 11 .    ? 3.077   53.929  66.937  1.00 34.82 ? 2891 HOH   B O     1 
HETATM 20692 O  O     . HOH   CA 11 .    ? 2.984   44.670  67.908  1.00 17.63 ? 2892 HOH   B O     1 
HETATM 20693 O  O     . HOH   CA 11 .    ? -23.685 23.045  84.625  1.00 34.42 ? 2893 HOH   B O     1 
HETATM 20694 O  O     . HOH   CA 11 .    ? -18.070 1.603   95.919  1.00 42.58 ? 2894 HOH   B O     1 
HETATM 20695 O  O     . HOH   CA 11 .    ? -0.603  43.556  56.084  1.00 32.52 ? 2895 HOH   B O     1 
HETATM 20696 O  O     . HOH   CA 11 .    ? 14.583  8.775   93.654  1.00 21.57 ? 2896 HOH   B O     1 
HETATM 20697 O  O     . HOH   CA 11 .    ? -6.896  43.671  73.865  1.00 30.15 ? 2897 HOH   B O     1 
HETATM 20698 O  O     . HOH   CA 11 .    ? -0.455  -8.141  99.693  1.00 24.56 ? 2898 HOH   B O     1 
HETATM 20699 O  O     . HOH   CA 11 .    ? 16.509  51.066  54.002  1.00 40.14 ? 2899 HOH   B O     1 
HETATM 20700 O  O     . HOH   CA 11 .    ? -29.498 11.521  87.679  1.00 45.18 ? 2900 HOH   B O     1 
HETATM 20701 O  O     . HOH   CA 11 .    ? 29.911  8.496   86.281  1.00 40.11 ? 2901 HOH   B O     1 
HETATM 20702 O  O     . HOH   CA 11 .    ? 20.176  18.646  60.157  1.00 24.61 ? 2902 HOH   B O     1 
HETATM 20703 O  O     . HOH   CA 11 .    ? 3.294   31.032  98.328  1.00 25.26 ? 2903 HOH   B O     1 
HETATM 20704 O  O     . HOH   CA 11 .    ? -32.651 7.418   108.280 1.00 41.74 ? 2904 HOH   B O     1 
HETATM 20705 O  O     . HOH   CA 11 .    ? 4.939   55.923  75.022  1.00 17.89 ? 2905 HOH   B O     1 
HETATM 20706 O  O     . HOH   CA 11 .    ? -32.539 19.620  101.563 1.00 39.63 ? 2906 HOH   B O     1 
HETATM 20707 O  O     . HOH   CA 11 .    ? 27.488  56.368  81.092  1.00 34.73 ? 2907 HOH   B O     1 
HETATM 20708 O  O     . HOH   CA 11 .    ? 34.519  12.718  80.881  1.00 32.39 ? 2908 HOH   B O     1 
HETATM 20709 O  O     . HOH   CA 11 .    ? 31.873  62.037  75.037  1.00 21.06 ? 2909 HOH   B O     1 
HETATM 20710 O  O     . HOH   CA 11 .    ? 9.454   -0.669  90.395  1.00 34.69 ? 2910 HOH   B O     1 
HETATM 20711 O  O     . HOH   CA 11 .    ? 11.765  17.782  94.922  1.00 32.08 ? 2911 HOH   B O     1 
HETATM 20712 O  O     . HOH   CA 11 .    ? -2.631  64.234  83.372  1.00 17.41 ? 2912 HOH   B O     1 
HETATM 20713 O  O     . HOH   CA 11 .    ? 17.680  43.886  111.988 1.00 33.15 ? 2913 HOH   B O     1 
HETATM 20714 O  O     . HOH   CA 11 .    ? -3.215  52.042  82.466  1.00 26.64 ? 2914 HOH   B O     1 
HETATM 20715 O  O     . HOH   CA 11 .    ? -5.415  46.218  84.081  1.00 25.60 ? 2915 HOH   B O     1 
HETATM 20716 O  O     . HOH   CA 11 .    ? 8.707   -1.117  98.835  1.00 36.71 ? 2916 HOH   B O     1 
HETATM 20717 O  O     . HOH   CA 11 .    ? 5.708   53.217  113.432 1.00 37.39 ? 2917 HOH   B O     1 
HETATM 20718 O  O     . HOH   CA 11 .    ? 18.505  33.963  46.280  1.00 38.42 ? 2918 HOH   B O     1 
HETATM 20719 O  O     . HOH   CA 11 .    ? -4.451  48.920  103.195 1.00 40.50 ? 2919 HOH   B O     1 
HETATM 20720 O  O     . HOH   CA 11 .    ? -22.963 3.970   96.596  1.00 40.01 ? 2920 HOH   B O     1 
HETATM 20721 O  O     . HOH   CA 11 .    ? 18.042  49.570  111.731 1.00 33.18 ? 2921 HOH   B O     1 
HETATM 20722 O  O     . HOH   CA 11 .    ? 22.886  49.772  53.721  1.00 40.28 ? 2922 HOH   B O     1 
HETATM 20723 O  O     . HOH   CA 11 .    ? 5.062   42.613  56.013  1.00 29.64 ? 2923 HOH   B O     1 
HETATM 20724 O  O     . HOH   CA 11 .    ? 29.241  65.009  62.456  1.00 30.78 ? 2924 HOH   B O     1 
HETATM 20725 O  O     . HOH   CA 11 .    ? -21.132 1.148   121.192 1.00 38.47 ? 2925 HOH   B O     1 
HETATM 20726 O  O     . HOH   CA 11 .    ? -13.378 48.784  110.575 1.00 32.69 ? 2926 HOH   B O     1 
HETATM 20727 O  O     . HOH   CA 11 .    ? -4.125  42.336  108.229 1.00 34.65 ? 2927 HOH   B O     1 
HETATM 20728 O  O     . HOH   CA 11 .    ? 7.043   2.024   127.225 1.00 42.03 ? 2928 HOH   B O     1 
HETATM 20729 O  O     . HOH   CA 11 .    ? 19.439  54.253  104.131 1.00 25.49 ? 2929 HOH   B O     1 
HETATM 20730 O  O     . HOH   CA 11 .    ? 7.840   53.997  64.522  1.00 30.18 ? 2930 HOH   B O     1 
HETATM 20731 O  O     . HOH   CA 11 .    ? 12.480  77.296  64.201  1.00 34.53 ? 2931 HOH   B O     1 
HETATM 20732 O  O     . HOH   CA 11 .    ? 15.961  9.982   95.630  1.00 24.65 ? 2932 HOH   B O     1 
HETATM 20733 O  O     . HOH   CA 11 .    ? 25.891  74.924  76.712  1.00 31.03 ? 2933 HOH   B O     1 
HETATM 20734 O  O     . HOH   CA 11 .    ? 26.484  12.715  88.017  1.00 31.65 ? 2934 HOH   B O     1 
HETATM 20735 O  O     . HOH   CA 11 .    ? -12.593 20.616  127.088 1.00 42.14 ? 2935 HOH   B O     1 
HETATM 20736 O  O     . HOH   CA 11 .    ? 18.991  35.218  112.940 1.00 20.10 ? 2936 HOH   B O     1 
HETATM 20737 O  O     . HOH   CA 11 .    ? -34.881 21.841  115.979 1.00 41.78 ? 2937 HOH   B O     1 
HETATM 20738 O  O     . HOH   CA 11 .    ? 42.322  37.588  95.865  1.00 32.41 ? 2938 HOH   B O     1 
HETATM 20739 O  O     . HOH   CA 11 .    ? -2.838  39.624  57.933  1.00 25.63 ? 2939 HOH   B O     1 
HETATM 20740 O  O     . HOH   CA 11 .    ? -14.453 26.605  101.523 1.00 28.12 ? 2940 HOH   B O     1 
HETATM 20741 O  O     . HOH   CA 11 .    ? 8.501   15.626  92.869  1.00 30.66 ? 2941 HOH   B O     1 
HETATM 20742 O  O     . HOH   CA 11 .    ? 28.474  25.308  104.754 1.00 44.01 ? 2942 HOH   B O     1 
HETATM 20743 O  O     . HOH   CA 11 .    ? 28.313  30.514  80.712  1.00 22.98 ? 2943 HOH   B O     1 
HETATM 20744 O  O     . HOH   CA 11 .    ? 11.511  18.208  97.917  1.00 28.39 ? 2944 HOH   B O     1 
HETATM 20745 O  O     . HOH   CA 11 .    ? 16.415  55.594  63.945  1.00 25.16 ? 2945 HOH   B O     1 
HETATM 20746 O  O     . HOH   CA 11 .    ? 36.589  20.380  90.058  1.00 41.39 ? 2946 HOH   B O     1 
HETATM 20747 O  O     . HOH   CA 11 .    ? 18.343  75.544  78.810  1.00 35.97 ? 2947 HOH   B O     1 
HETATM 20748 O  O     . HOH   CA 11 .    ? 2.628   18.619  77.304  1.00 28.06 ? 2948 HOH   B O     1 
HETATM 20749 O  O     . HOH   CA 11 .    ? -11.628 27.226  102.315 1.00 36.16 ? 2949 HOH   B O     1 
HETATM 20750 O  O     . HOH   CA 11 .    ? -7.861  47.785  76.708  1.00 30.35 ? 2950 HOH   B O     1 
HETATM 20751 O  O     . HOH   CA 11 .    ? 23.077  50.995  65.151  1.00 21.27 ? 2951 HOH   B O     1 
HETATM 20752 O  O     . HOH   CA 11 .    ? 9.971   18.103  101.215 1.00 24.33 ? 2952 HOH   B O     1 
HETATM 20753 O  O     . HOH   CA 11 .    ? -27.365 4.894   118.670 1.00 45.93 ? 2953 HOH   B O     1 
HETATM 20754 O  O     . HOH   CA 11 .    ? -26.966 12.213  100.049 1.00 41.46 ? 2954 HOH   B O     1 
HETATM 20755 O  O     . HOH   CA 11 .    ? -36.972 17.491  105.890 1.00 41.97 ? 2955 HOH   B O     1 
HETATM 20756 O  O     . HOH   CA 11 .    ? -19.370 28.586  88.441  1.00 28.14 ? 2956 HOH   B O     1 
HETATM 20757 O  O     . HOH   CA 11 .    ? 19.444  58.090  82.314  1.00 26.89 ? 2957 HOH   B O     1 
HETATM 20758 O  O     . HOH   CA 11 .    ? -6.272  8.720   82.163  1.00 32.53 ? 2958 HOH   B O     1 
HETATM 20759 O  O     . HOH   CA 11 .    ? 35.720  32.819  80.765  1.00 39.10 ? 2959 HOH   B O     1 
HETATM 20760 O  O     . HOH   CA 11 .    ? 22.147  14.700  81.144  1.00 23.30 ? 2960 HOH   B O     1 
HETATM 20761 O  O     . HOH   CA 11 .    ? 4.494   77.010  63.163  1.00 39.09 ? 2961 HOH   B O     1 
HETATM 20762 O  O     . HOH   CA 11 .    ? -0.930  37.543  76.361  1.00 26.47 ? 2962 HOH   B O     1 
HETATM 20763 O  O     . HOH   CA 11 .    ? 25.719  53.357  54.359  1.00 44.07 ? 2963 HOH   B O     1 
HETATM 20764 O  O     . HOH   CA 11 .    ? 10.732  37.303  77.716  1.00 22.16 ? 2964 HOH   B O     1 
HETATM 20765 O  O     . HOH   CA 11 .    ? -7.631  23.694  125.255 1.00 33.41 ? 2965 HOH   B O     1 
HETATM 20766 O  O     . HOH   CA 11 .    ? 14.294  75.448  62.935  1.00 28.19 ? 2966 HOH   B O     1 
HETATM 20767 O  O     . HOH   CA 11 .    ? 20.335  20.139  109.253 1.00 21.80 ? 2967 HOH   B O     1 
HETATM 20768 O  O     . HOH   CA 11 .    ? 16.496  51.833  79.588  1.00 22.13 ? 2968 HOH   B O     1 
HETATM 20769 O  O     . HOH   CA 11 .    ? 32.499  40.091  90.624  1.00 30.75 ? 2969 HOH   B O     1 
HETATM 20770 O  O     . HOH   CA 11 .    ? 36.839  16.248  79.301  1.00 46.72 ? 2970 HOH   B O     1 
HETATM 20771 O  O     . HOH   CA 11 .    ? 27.194  65.406  57.930  1.00 37.27 ? 2971 HOH   B O     1 
HETATM 20772 O  O     . HOH   CA 11 .    ? -19.446 23.633  112.687 1.00 33.02 ? 2972 HOH   B O     1 
HETATM 20773 O  O     . HOH   CA 11 .    ? -12.019 34.605  86.570  1.00 41.69 ? 2973 HOH   B O     1 
HETATM 20774 O  O     . HOH   CA 11 .    ? -5.680  15.219  94.554  1.00 16.16 ? 2974 HOH   B O     1 
HETATM 20775 O  O     . HOH   CA 11 .    ? 23.265  76.373  65.504  1.00 41.07 ? 2975 HOH   B O     1 
HETATM 20776 O  O     . HOH   CA 11 .    ? 37.302  37.268  88.964  1.00 21.71 ? 2976 HOH   B O     1 
HETATM 20777 O  O     . HOH   CA 11 .    ? -22.821 21.492  102.077 1.00 29.99 ? 2977 HOH   B O     1 
HETATM 20778 O  O     . HOH   CA 11 .    ? -7.679  9.417   131.225 1.00 44.45 ? 2978 HOH   B O     1 
HETATM 20779 O  O     . HOH   CA 11 .    ? 25.016  62.785  54.450  1.00 32.30 ? 2979 HOH   B O     1 
HETATM 20780 O  O     . HOH   CA 11 .    ? 30.129  23.630  103.595 1.00 43.45 ? 2980 HOH   B O     1 
HETATM 20781 O  O     . HOH   CA 11 .    ? 13.510  18.536  87.608  1.00 21.65 ? 2981 HOH   B O     1 
HETATM 20782 O  O     . HOH   CA 11 .    ? 18.383  23.168  85.223  1.00 14.01 ? 2982 HOH   B O     1 
HETATM 20783 O  O     . HOH   CA 11 .    ? 12.947  61.409  84.433  1.00 34.49 ? 2983 HOH   B O     1 
HETATM 20784 O  O     . HOH   CA 11 .    ? 18.168  74.372  81.791  1.00 36.18 ? 2984 HOH   B O     1 
HETATM 20785 O  O     . HOH   CA 11 .    ? 4.662   -0.084  86.736  1.00 32.81 ? 2985 HOH   B O     1 
HETATM 20786 O  O     . HOH   CA 11 .    ? -14.891 19.048  82.760  1.00 26.40 ? 2986 HOH   B O     1 
HETATM 20787 O  O     . HOH   CA 11 .    ? 9.246   45.630  131.946 1.00 35.87 ? 2987 HOH   B O     1 
HETATM 20788 O  O     . HOH   CA 11 .    ? 29.000  22.323  72.385  1.00 31.37 ? 2988 HOH   B O     1 
HETATM 20789 O  O     . HOH   CA 11 .    ? -16.633 49.169  116.620 1.00 40.33 ? 2989 HOH   B O     1 
HETATM 20790 O  O     . HOH   CA 11 .    ? 18.979  65.780  55.855  1.00 32.15 ? 2990 HOH   B O     1 
HETATM 20791 O  O     . HOH   CA 11 .    ? -9.153  13.856  114.797 1.00 27.85 ? 2991 HOH   B O     1 
HETATM 20792 O  O     . HOH   CA 11 .    ? 31.950  36.652  51.302  1.00 40.38 ? 2992 HOH   B O     1 
HETATM 20793 O  O     . HOH   CA 11 .    ? 28.390  33.536  80.352  1.00 37.73 ? 2993 HOH   B O     1 
HETATM 20794 O  O     . HOH   CA 11 .    ? -4.701  -4.160  91.861  1.00 27.43 ? 2994 HOH   B O     1 
HETATM 20795 O  O     . HOH   CA 11 .    ? 20.982  62.357  54.144  1.00 34.12 ? 2995 HOH   B O     1 
HETATM 20796 O  O     . HOH   CA 11 .    ? -7.409  10.216  112.897 1.00 20.59 ? 2996 HOH   B O     1 
HETATM 20797 O  O     . HOH   CA 11 .    ? 35.478  31.057  58.475  1.00 31.22 ? 2997 HOH   B O     1 
HETATM 20798 O  O     . HOH   CA 11 .    ? -23.767 9.836   126.843 1.00 39.15 ? 2998 HOH   B O     1 
HETATM 20799 O  O     . HOH   CA 11 .    ? 5.076   35.524  103.860 1.00 39.62 ? 2999 HOH   B O     1 
HETATM 20800 O  O     . HOH   CA 11 .    ? -18.128 5.874   95.724  1.00 33.31 ? 3000 HOH   B O     1 
HETATM 20801 O  O     . HOH   CA 11 .    ? 42.609  31.919  96.479  1.00 40.58 ? 3001 HOH   B O     1 
HETATM 20802 O  O     . HOH   CA 11 .    ? 12.779  29.168  50.483  1.00 27.82 ? 3002 HOH   B O     1 
HETATM 20803 O  O     . HOH   CA 11 .    ? 15.579  49.260  79.013  1.00 25.94 ? 3003 HOH   B O     1 
HETATM 20804 O  O     . HOH   CA 11 .    ? 16.410  13.743  106.942 1.00 25.54 ? 3004 HOH   B O     1 
HETATM 20805 O  O     . HOH   CA 11 .    ? 5.568   23.599  119.737 1.00 42.86 ? 3005 HOH   B O     1 
HETATM 20806 O  O     . HOH   CA 11 .    ? -22.094 5.459   120.487 1.00 38.16 ? 3006 HOH   B O     1 
HETATM 20807 O  O     . HOH   CA 11 .    ? 16.175  7.788   110.865 1.00 35.79 ? 3007 HOH   B O     1 
HETATM 20808 O  O     . HOH   CA 11 .    ? -12.643 31.383  83.834  1.00 36.21 ? 3008 HOH   B O     1 
HETATM 20809 O  O     . HOH   CA 11 .    ? 38.143  22.793  90.252  1.00 45.53 ? 3009 HOH   B O     1 
HETATM 20810 O  O     . HOH   CA 11 .    ? 30.894  19.502  56.269  1.00 28.91 ? 3010 HOH   B O     1 
HETATM 20811 O  O     . HOH   CA 11 .    ? 31.673  34.848  74.544  1.00 30.62 ? 3011 HOH   B O     1 
HETATM 20812 O  O     . HOH   CA 11 .    ? 33.491  37.809  71.862  1.00 40.12 ? 3012 HOH   B O     1 
HETATM 20813 O  O     . HOH   CA 11 .    ? 3.645   20.373  96.170  1.00 38.19 ? 3013 HOH   B O     1 
HETATM 20814 O  O     . HOH   CA 11 .    ? -28.902 8.167   90.799  1.00 40.53 ? 3014 HOH   B O     1 
HETATM 20815 O  O     . HOH   CA 11 .    ? 0.719   20.905  132.133 1.00 34.61 ? 3015 HOH   B O     1 
HETATM 20816 O  O     . HOH   CA 11 .    ? 26.766  40.790  81.237  1.00 25.48 ? 3016 HOH   B O     1 
HETATM 20817 O  O     . HOH   CA 11 .    ? 23.460  24.204  47.725  1.00 34.71 ? 3017 HOH   B O     1 
HETATM 20818 O  O     . HOH   CA 11 .    ? 33.143  25.788  54.597  1.00 39.75 ? 3018 HOH   B O     1 
HETATM 20819 O  O     . HOH   CA 11 .    ? 6.344   49.579  88.652  1.00 38.88 ? 3019 HOH   B O     1 
HETATM 20820 O  O     . HOH   CA 11 .    ? 33.182  46.924  87.592  1.00 45.84 ? 3020 HOH   B O     1 
HETATM 20821 O  O     . HOH   CA 11 .    ? -13.998 44.365  113.330 1.00 41.09 ? 3021 HOH   B O     1 
HETATM 20822 O  O     . HOH   CA 11 .    ? 23.923  16.864  82.679  1.00 24.42 ? 3022 HOH   B O     1 
HETATM 20823 O  O     . HOH   CA 11 .    ? -10.096 18.244  131.112 1.00 34.28 ? 3023 HOH   B O     1 
HETATM 20824 O  O     . HOH   CA 11 .    ? -16.234 7.805   127.467 1.00 42.14 ? 3024 HOH   B O     1 
HETATM 20825 O  O     . HOH   CA 11 .    ? -0.943  22.397  97.046  1.00 29.25 ? 3025 HOH   B O     1 
HETATM 20826 O  O     . HOH   CA 11 .    ? 5.911   69.917  61.138  1.00 37.95 ? 3026 HOH   B O     1 
HETATM 20827 O  O     . HOH   CA 11 .    ? 40.532  22.582  58.181  1.00 46.42 ? 3027 HOH   B O     1 
HETATM 20828 O  O     . HOH   CA 11 .    ? -6.631  38.837  67.478  1.00 31.55 ? 3028 HOH   B O     1 
HETATM 20829 O  O     . HOH   CA 11 .    ? 25.321  79.096  67.416  1.00 45.74 ? 3029 HOH   B O     1 
HETATM 20830 O  O     . HOH   CA 11 .    ? 6.518   24.425  83.755  1.00 25.44 ? 3030 HOH   B O     1 
HETATM 20831 O  O     . HOH   CA 11 .    ? -2.452  41.913  74.364  1.00 32.31 ? 3031 HOH   B O     1 
HETATM 20832 O  O     . HOH   CA 11 .    ? 6.593   35.885  113.825 1.00 39.19 ? 3032 HOH   B O     1 
HETATM 20833 O  O     . HOH   CA 11 .    ? 25.312  17.775  100.318 1.00 34.29 ? 3033 HOH   B O     1 
HETATM 20834 O  O     . HOH   CA 11 .    ? -4.514  38.802  56.357  1.00 40.58 ? 3034 HOH   B O     1 
HETATM 20835 O  O     . HOH   CA 11 .    ? 15.096  56.676  72.102  1.00 25.28 ? 3035 HOH   B O     1 
HETATM 20836 O  O     . HOH   CA 11 .    ? -2.520  -5.783  89.710  1.00 33.72 ? 3036 HOH   B O     1 
HETATM 20837 O  O     . HOH   CA 11 .    ? 26.686  12.951  90.951  1.00 41.48 ? 3037 HOH   B O     1 
HETATM 20838 O  O     . HOH   CA 11 .    ? 18.698  63.397  55.092  1.00 34.89 ? 3038 HOH   B O     1 
HETATM 20839 O  O     . HOH   CA 11 .    ? -4.172  26.370  99.839  1.00 25.30 ? 3039 HOH   B O     1 
HETATM 20840 O  O     . HOH   CA 11 .    ? 24.575  67.383  80.705  1.00 35.30 ? 3040 HOH   B O     1 
HETATM 20841 O  O     . HOH   CA 11 .    ? 28.234  75.614  70.443  1.00 42.85 ? 3041 HOH   B O     1 
HETATM 20842 O  O     . HOH   CA 11 .    ? 9.959   68.174  55.061  1.00 44.21 ? 3042 HOH   B O     1 
HETATM 20843 O  O     . HOH   CA 11 .    ? 17.196  7.509   90.075  1.00 36.89 ? 3043 HOH   B O     1 
HETATM 20844 O  O     . HOH   CA 11 .    ? 5.914   -3.870  99.731  1.00 40.22 ? 3044 HOH   B O     1 
HETATM 20845 O  O     . HOH   CA 11 .    ? 26.597  51.519  55.785  1.00 35.40 ? 3045 HOH   B O     1 
HETATM 20846 O  O     . HOH   CA 11 .    ? 15.157  28.696  49.315  1.00 31.05 ? 3046 HOH   B O     1 
HETATM 20847 O  O     . HOH   CA 11 .    ? -15.537 8.381   85.509  1.00 41.57 ? 3047 HOH   B O     1 
HETATM 20848 O  O     . HOH   CA 11 .    ? 28.382  41.232  53.277  1.00 32.52 ? 3048 HOH   B O     1 
HETATM 20849 O  O     . HOH   CA 11 .    ? -2.697  22.574  79.578  1.00 22.48 ? 3049 HOH   B O     1 
HETATM 20850 O  O     . HOH   CA 11 .    ? 8.886   30.531  88.555  1.00 32.36 ? 3050 HOH   B O     1 
HETATM 20851 O  O     . HOH   CA 11 .    ? 26.782  46.960  102.796 1.00 37.87 ? 3051 HOH   B O     1 
HETATM 20852 O  O     . HOH   CA 11 .    ? -27.650 13.957  86.420  1.00 35.77 ? 3052 HOH   B O     1 
HETATM 20853 O  O     . HOH   CA 11 .    ? -5.362  37.200  86.087  1.00 29.36 ? 3053 HOH   B O     1 
HETATM 20854 O  O     . HOH   CA 11 .    ? 12.374  57.688  94.046  1.00 28.90 ? 3054 HOH   B O     1 
HETATM 20855 O  O     . HOH   CA 11 .    ? 23.135  67.345  59.586  1.00 28.91 ? 3055 HOH   B O     1 
HETATM 20856 O  O     . HOH   CA 11 .    ? -30.554 5.224   100.262 1.00 36.65 ? 3056 HOH   B O     1 
HETATM 20857 O  O     . HOH   CA 11 .    ? -9.183  7.551   82.129  1.00 40.41 ? 3057 HOH   B O     1 
HETATM 20858 O  O     . HOH   CA 11 .    ? 13.209  23.217  89.273  1.00 37.24 ? 3058 HOH   B O     1 
HETATM 20859 O  O     . HOH   CA 11 .    ? -20.750 7.972   120.866 1.00 40.30 ? 3059 HOH   B O     1 
HETATM 20860 O  O     . HOH   CA 11 .    ? 24.094  49.800  102.757 1.00 41.09 ? 3060 HOH   B O     1 
HETATM 20861 O  O     . HOH   CA 11 .    ? 25.319  23.958  49.872  1.00 39.15 ? 3061 HOH   B O     1 
HETATM 20862 O  O     . HOH   CA 11 .    ? 2.992   56.844  70.920  1.00 29.84 ? 3062 HOH   B O     1 
HETATM 20863 O  O     . HOH   CA 11 .    ? 2.178   24.159  95.226  1.00 34.77 ? 3063 HOH   B O     1 
HETATM 20864 O  O     . HOH   CA 11 .    ? 18.160  46.195  111.801 1.00 35.87 ? 3064 HOH   B O     1 
HETATM 20865 O  O     . HOH   CA 11 .    ? 34.882  6.012   81.560  1.00 43.29 ? 3065 HOH   B O     1 
HETATM 20866 O  O     . HOH   CA 11 .    ? 33.001  19.867  72.357  1.00 38.09 ? 3066 HOH   B O     1 
HETATM 20867 O  O     . HOH   CA 11 .    ? -6.780  6.859   113.809 1.00 36.86 ? 3067 HOH   B O     1 
HETATM 20868 O  O     . HOH   CA 11 .    ? -3.194  -2.913  85.168  1.00 39.03 ? 3068 HOH   B O     1 
HETATM 20869 O  O     . HOH   CA 11 .    ? -2.159  59.865  124.165 1.00 41.21 ? 3069 HOH   B O     1 
HETATM 20870 O  O     . HOH   CA 11 .    ? 39.603  29.030  80.959  1.00 34.04 ? 3070 HOH   B O     1 
HETATM 20871 O  O     . HOH   CA 11 .    ? -3.887  -5.066  94.347  1.00 37.13 ? 3071 HOH   B O     1 
HETATM 20872 O  O     . HOH   CA 11 .    ? -6.030  39.522  86.262  1.00 31.83 ? 3072 HOH   B O     1 
HETATM 20873 O  O     . HOH   CA 11 .    ? 5.736   20.609  86.026  1.00 41.49 ? 3073 HOH   B O     1 
HETATM 20874 O  O     . HOH   CA 11 .    ? -5.299  50.734  83.253  1.00 37.27 ? 3074 HOH   B O     1 
HETATM 20875 O  O     . HOH   CA 11 .    ? 28.594  75.482  72.744  1.00 42.03 ? 3075 HOH   B O     1 
HETATM 20876 O  O     . HOH   CA 11 .    ? -3.207  -0.925  124.824 1.00 39.23 ? 3076 HOH   B O     1 
HETATM 20877 O  O     . HOH   CA 11 .    ? 35.683  19.724  85.633  1.00 35.25 ? 3077 HOH   B O     1 
HETATM 20878 O  O     . HOH   CA 11 .    ? -21.907 7.562   86.087  1.00 37.90 ? 3078 HOH   B O     1 
HETATM 20879 O  O     . HOH   CA 11 .    ? 32.167  44.918  61.657  1.00 38.41 ? 3079 HOH   B O     1 
HETATM 20880 O  O     . HOH   CA 11 .    ? 8.011   -9.525  111.349 1.00 38.61 ? 3080 HOH   B O     1 
HETATM 20881 O  O     . HOH   CA 11 .    ? 33.022  25.717  70.930  1.00 43.09 ? 3081 HOH   B O     1 
HETATM 20882 O  O     . HOH   CA 11 .    ? -23.923 -2.249  112.689 1.00 44.35 ? 3082 HOH   B O     1 
HETATM 20883 O  O     . HOH   CA 11 .    ? 10.941  9.856   123.259 1.00 32.35 ? 3083 HOH   B O     1 
HETATM 20884 O  O     . HOH   CA 11 .    ? 11.466  43.367  51.004  1.00 31.44 ? 3084 HOH   B O     1 
HETATM 20885 O  O     . HOH   CA 11 .    ? -14.784 50.806  127.093 1.00 42.44 ? 3085 HOH   B O     1 
HETATM 20886 O  O     . HOH   CA 11 .    ? -21.779 22.360  86.986  1.00 41.29 ? 3086 HOH   B O     1 
HETATM 20887 O  O     . HOH   CA 11 .    ? 16.793  56.145  95.029  1.00 31.92 ? 3087 HOH   B O     1 
HETATM 20888 O  O     . HOH   CA 11 .    ? -2.704  20.548  110.785 1.00 36.64 ? 3088 HOH   B O     1 
HETATM 20889 O  O     . HOH   CA 11 .    ? -1.148  56.802  124.781 1.00 44.05 ? 3089 HOH   B O     1 
HETATM 20890 O  O     . HOH   CA 11 .    ? -33.239 16.398  121.525 1.00 33.37 ? 3090 HOH   B O     1 
HETATM 20891 O  O     . HOH   CA 11 .    ? 7.832   28.479  81.289  1.00 33.45 ? 3091 HOH   B O     1 
HETATM 20892 O  O     . HOH   CA 11 .    ? 23.310  7.830   73.747  1.00 41.13 ? 3092 HOH   B O     1 
HETATM 20893 O  O     . HOH   CA 11 .    ? 17.038  22.935  92.338  1.00 38.78 ? 3093 HOH   B O     1 
HETATM 20894 O  O     . HOH   CA 11 .    ? 35.675  17.092  83.133  1.00 43.73 ? 3094 HOH   B O     1 
HETATM 20895 O  O     . HOH   CA 11 .    ? 6.256   17.080  96.540  1.00 30.65 ? 3095 HOH   B O     1 
HETATM 20896 O  O     . HOH   CA 11 .    ? 9.474   23.464  122.010 1.00 36.18 ? 3096 HOH   B O     1 
HETATM 20897 O  O     . HOH   CA 11 .    ? -32.800 3.660   101.421 1.00 49.12 ? 3097 HOH   B O     1 
HETATM 20898 O  O     . HOH   CA 11 .    ? -7.277  55.795  128.019 1.00 41.61 ? 3098 HOH   B O     1 
HETATM 20899 O  O     . HOH   CA 11 .    ? 7.579   33.459  51.400  1.00 31.72 ? 3099 HOH   B O     1 
HETATM 20900 O  O     . HOH   CA 11 .    ? 13.314  34.817  109.517 1.00 35.13 ? 3100 HOH   B O     1 
HETATM 20901 O  O     . HOH   CA 11 .    ? 34.624  15.874  62.097  1.00 36.47 ? 3101 HOH   B O     1 
HETATM 20902 O  O     . HOH   CA 11 .    ? 12.850  46.384  111.431 1.00 41.53 ? 3102 HOH   B O     1 
HETATM 20903 O  O     . HOH   CA 11 .    ? 27.335  72.853  78.380  1.00 40.83 ? 3103 HOH   B O     1 
HETATM 20904 O  O     . HOH   CA 11 .    ? 12.672  39.433  132.279 1.00 44.18 ? 3104 HOH   B O     1 
HETATM 20905 O  O     . HOH   CA 11 .    ? 17.109  5.012   107.535 1.00 41.06 ? 3105 HOH   B O     1 
HETATM 20906 O  O     . HOH   CA 11 .    ? 17.121  24.408  52.522  1.00 27.95 ? 3106 HOH   B O     1 
HETATM 20907 O  O     . HOH   CA 11 .    ? -1.313  37.415  73.603  1.00 18.22 ? 3107 HOH   B O     1 
HETATM 20908 O  O     . HOH   CA 11 .    ? 1.149   55.622  65.684  1.00 40.71 ? 3108 HOH   B O     1 
HETATM 20909 O  O     . HOH   CA 11 .    ? 30.308  70.762  72.700  1.00 35.27 ? 3109 HOH   B O     1 
HETATM 20910 O  O     . HOH   CA 11 .    ? 22.053  58.524  96.562  1.00 42.31 ? 3110 HOH   B O     1 
HETATM 20911 O  O     . HOH   CA 11 .    ? -2.570  69.158  75.604  1.00 34.14 ? 3111 HOH   B O     1 
HETATM 20912 O  O     . HOH   CA 11 .    ? -3.465  14.060  131.950 1.00 37.42 ? 3112 HOH   B O     1 
HETATM 20913 O  O     . HOH   CA 11 .    ? 16.149  35.131  113.415 1.00 32.64 ? 3113 HOH   B O     1 
HETATM 20914 O  O     . HOH   CA 11 .    ? 6.329   17.036  115.046 1.00 31.30 ? 3114 HOH   B O     1 
HETATM 20915 O  O     . HOH   CA 11 .    ? 9.759   48.382  108.534 1.00 32.57 ? 3115 HOH   B O     1 
HETATM 20916 O  O     . HOH   CA 11 .    ? 9.443   0.397   119.575 1.00 37.39 ? 3116 HOH   B O     1 
HETATM 20917 O  O     . HOH   CA 11 .    ? 33.043  34.857  72.372  1.00 32.78 ? 3117 HOH   B O     1 
HETATM 20918 O  O     . HOH   CA 11 .    ? -0.053  -2.365  94.960  1.00 28.19 ? 3118 HOH   B O     1 
HETATM 20919 O  O     . HOH   CA 11 .    ? 5.402   66.496  64.191  1.00 40.27 ? 3119 HOH   B O     1 
HETATM 20920 O  O     . HOH   CA 11 .    ? 21.394  5.906   73.375  1.00 35.44 ? 3120 HOH   B O     1 
HETATM 20921 O  O     . HOH   CA 11 .    ? 19.392  59.855  54.415  1.00 36.93 ? 3121 HOH   B O     1 
HETATM 20922 O  O     . HOH   CA 11 .    ? -6.593  7.827   116.459 1.00 26.65 ? 3122 HOH   B O     1 
HETATM 20923 O  O     . HOH   CA 11 .    ? 4.583   29.379  82.067  1.00 26.12 ? 3123 HOH   B O     1 
HETATM 20924 O  O     . HOH   CA 11 .    ? 33.028  58.360  67.364  1.00 29.54 ? 3124 HOH   B O     1 
HETATM 20925 O  O     . HOH   CA 11 .    ? 7.687   49.670  90.353  1.00 40.89 ? 3125 HOH   B O     1 
HETATM 20926 O  O     . HOH   CA 11 .    ? 18.650  10.441  120.219 1.00 45.15 ? 3126 HOH   B O     1 
HETATM 20927 O  O     . HOH   CA 11 .    ? -36.103 27.314  115.492 1.00 38.97 ? 3127 HOH   B O     1 
HETATM 20928 O  O     . HOH   CA 11 .    ? 7.456   19.001  97.500  1.00 35.52 ? 3128 HOH   B O     1 
HETATM 20929 O  O     . HOH   CA 11 .    ? 34.460  37.955  66.881  1.00 39.23 ? 3129 HOH   B O     1 
HETATM 20930 O  O     . HOH   CA 11 .    ? -32.796 16.962  101.094 1.00 39.84 ? 3130 HOH   B O     1 
HETATM 20931 O  O     . HOH   CA 11 .    ? 31.971  35.007  80.916  1.00 45.15 ? 3131 HOH   B O     1 
HETATM 20932 O  O     . HOH   CA 11 .    ? -2.433  41.161  78.096  1.00 32.54 ? 3132 HOH   B O     1 
HETATM 20933 O  O     . HOH   CA 11 .    ? 30.823  31.650  83.644  1.00 34.03 ? 3133 HOH   B O     1 
HETATM 20934 O  O     . HOH   CA 11 .    ? 32.690  20.172  76.296  1.00 36.97 ? 3134 HOH   B O     1 
HETATM 20935 O  O     . HOH   CA 11 .    ? 30.806  41.951  55.510  1.00 34.06 ? 3135 HOH   B O     1 
HETATM 20936 O  O     . HOH   CA 11 .    ? 9.677   18.853  98.692  1.00 32.82 ? 3136 HOH   B O     1 
HETATM 20937 O  O     . HOH   CA 11 .    ? 3.690   37.072  103.059 1.00 42.64 ? 3137 HOH   B O     1 
HETATM 20938 O  O     . HOH   CA 11 .    ? -6.683  2.424   85.097  1.00 30.78 ? 3138 HOH   B O     1 
HETATM 20939 O  O     . HOH   CA 11 .    ? -37.879 12.822  108.048 1.00 45.55 ? 3139 HOH   B O     1 
HETATM 20940 O  O     . HOH   CA 11 .    ? 39.977  38.020  88.736  1.00 34.06 ? 3140 HOH   B O     1 
HETATM 20941 O  O     . HOH   CA 11 .    ? 23.968  68.362  62.365  1.00 29.18 ? 3141 HOH   B O     1 
HETATM 20942 O  O     . HOH   CA 11 .    ? -2.414  29.508  96.968  1.00 30.49 ? 3142 HOH   B O     1 
HETATM 20943 O  O     . HOH   CA 11 .    ? 9.041   16.899  123.396 1.00 41.53 ? 3143 HOH   B O     1 
HETATM 20944 O  O     . HOH   CA 11 .    ? 4.815   43.102  51.117  1.00 28.21 ? 3144 HOH   B O     1 
HETATM 20945 O  O     . HOH   CA 11 .    ? 2.304   3.559   82.061  1.00 32.46 ? 3145 HOH   B O     1 
HETATM 20946 O  O     . HOH   CA 11 .    ? 40.773  29.921  90.203  1.00 25.97 ? 3146 HOH   B O     1 
HETATM 20947 O  O     . HOH   CA 11 .    ? 5.350   44.211  53.718  1.00 27.45 ? 3147 HOH   B O     1 
HETATM 20948 O  O     . HOH   CA 11 .    ? -7.711  -9.862  99.673  1.00 33.61 ? 3148 HOH   B O     1 
HETATM 20949 O  O     . HOH   CA 11 .    ? -16.438 51.936  115.879 1.00 45.17 ? 3149 HOH   B O     1 
HETATM 20950 O  O     . HOH   CA 11 .    ? 11.142  50.320  109.235 1.00 42.91 ? 3150 HOH   B O     1 
HETATM 20951 O  O     . HOH   CA 11 .    ? -4.034  63.758  69.841  1.00 42.57 ? 3151 HOH   B O     1 
HETATM 20952 O  O     . HOH   CA 11 .    ? 15.548  52.398  51.594  1.00 44.65 ? 3152 HOH   B O     1 
HETATM 20953 O  O     . HOH   CA 11 .    ? 33.327  40.003  61.612  1.00 33.90 ? 3153 HOH   B O     1 
HETATM 20954 O  O     . HOH   CA 11 .    ? 3.707   49.255  96.711  1.00 34.71 ? 3154 HOH   B O     1 
HETATM 20955 O  O     . HOH   CA 11 .    ? 19.807  45.212  89.792  1.00 16.13 ? 3155 HOH   B O     1 
HETATM 20956 O  O     . HOH   CA 11 .    ? -1.799  25.886  64.755  1.00 29.04 ? 3156 HOH   B O     1 
HETATM 20957 O  O     . HOH   CA 11 .    ? 6.167   30.168  98.263  1.00 38.96 ? 3157 HOH   B O     1 
HETATM 20958 O  O     . HOH   CA 11 .    ? 8.890   -3.671  105.734 1.00 36.02 ? 3158 HOH   B O     1 
HETATM 20959 O  O     . HOH   CA 11 .    ? 39.273  26.360  92.103  1.00 39.28 ? 3159 HOH   B O     1 
HETATM 20960 O  O     . HOH   CA 11 .    ? 1.458   21.746  95.506  1.00 35.14 ? 3160 HOH   B O     1 
HETATM 20961 O  O     . HOH   CA 11 .    ? 33.321  41.108  53.791  1.00 43.79 ? 3161 HOH   B O     1 
HETATM 20962 O  O     . HOH   CA 11 .    ? 42.661  31.935  99.466  1.00 37.79 ? 3162 HOH   B O     1 
HETATM 20963 O  O     . HOH   CA 11 .    ? 30.000  73.169  72.572  1.00 36.42 ? 3163 HOH   B O     1 
HETATM 20964 O  O     . HOH   CA 11 .    ? -1.327  -5.373  86.857  1.00 43.91 ? 3164 HOH   B O     1 
HETATM 20965 O  O     . HOH   CA 11 .    ? 33.086  41.932  66.843  1.00 30.09 ? 3165 HOH   B O     1 
HETATM 20966 O  O     . HOH   CA 11 .    ? 5.073   4.022   78.815  1.00 37.47 ? 3166 HOH   B O     1 
HETATM 20967 O  O     . HOH   CA 11 .    ? 34.352  36.018  68.859  1.00 37.95 ? 3167 HOH   B O     1 
HETATM 20968 O  O     . HOH   CA 11 .    ? -10.300 29.771  76.233  1.00 35.47 ? 3168 HOH   B O     1 
HETATM 20969 O  O     . HOH   CA 11 .    ? 27.823  50.690  95.765  1.00 34.64 ? 3169 HOH   B O     1 
HETATM 20970 O  O     . HOH   CA 11 .    ? 39.310  40.540  89.047  1.00 40.87 ? 3170 HOH   B O     1 
HETATM 20971 O  O     . HOH   CA 11 .    ? 14.244  51.752  63.521  1.00 29.65 ? 3171 HOH   B O     1 
HETATM 20972 O  O     . HOH   CA 11 .    ? -2.284  51.706  101.053 1.00 26.90 ? 3172 HOH   B O     1 
HETATM 20973 O  O     . HOH   CA 11 .    ? 10.710  -2.467  92.140  1.00 42.46 ? 3173 HOH   B O     1 
HETATM 20974 O  O     . HOH   CA 11 .    ? 0.408   4.375   86.094  1.00 29.52 ? 3174 HOH   B O     1 
HETATM 20975 O  O     . HOH   CA 11 .    ? 18.632  7.952   106.969 1.00 41.54 ? 3175 HOH   B O     1 
HETATM 20976 O  O     . HOH   CA 11 .    ? 32.545  51.763  69.850  1.00 39.91 ? 3176 HOH   B O     1 
HETATM 20977 O  O     . HOH   CA 11 .    ? 12.309  -2.050  113.191 1.00 45.17 ? 3177 HOH   B O     1 
HETATM 20978 O  O     . HOH   CA 11 .    ? 28.911  64.523  59.775  1.00 36.56 ? 3178 HOH   B O     1 
HETATM 20979 O  O     . HOH   CA 11 .    ? 15.262  3.969   72.624  1.00 39.76 ? 3179 HOH   B O     1 
HETATM 20980 O  O     . HOH   CA 11 .    ? 42.900  34.516  93.277  1.00 37.25 ? 3180 HOH   B O     1 
HETATM 20981 O  O     . HOH   CA 11 .    ? 18.354  6.665   98.250  1.00 33.30 ? 3181 HOH   B O     1 
HETATM 20982 O  O     . HOH   CA 11 .    ? -25.120 22.300  98.451  1.00 34.11 ? 3182 HOH   B O     1 
HETATM 20983 O  O     . HOH   CA 11 .    ? 3.959   29.708  94.242  1.00 35.12 ? 3183 HOH   B O     1 
HETATM 20984 O  O     A HOH   CA 11 .    ? 2.589   61.795  83.481  0.57 22.48 ? 3184 HOH   B O     1 
HETATM 20985 O  O     . HOH   CA 11 .    ? -7.675  12.175  82.651  1.00 39.39 ? 3185 HOH   B O     1 
HETATM 20986 O  O     . HOH   CA 11 .    ? -5.112  51.627  102.205 1.00 41.92 ? 3186 HOH   B O     1 
HETATM 20987 O  O     . HOH   CA 11 .    ? 14.861  55.401  61.939  1.00 37.50 ? 3187 HOH   B O     1 
HETATM 20988 O  O     . HOH   CA 11 .    ? 21.460  18.205  110.950 1.00 36.87 ? 3188 HOH   B O     1 
HETATM 20989 O  O     . HOH   CA 11 .    ? 0.372   18.096  72.090  1.00 34.05 ? 3189 HOH   B O     1 
HETATM 20990 O  O     . HOH   CA 11 .    ? 31.149  58.540  60.703  1.00 32.34 ? 3190 HOH   B O     1 
HETATM 20991 O  O     . HOH   CA 11 .    ? -22.000 25.720  91.995  1.00 36.74 ? 3191 HOH   B O     1 
HETATM 20992 O  O     . HOH   CA 11 .    ? -15.845 27.265  118.479 1.00 43.75 ? 3192 HOH   B O     1 
HETATM 20993 O  O     . HOH   CA 11 .    ? -30.232 15.165  119.075 1.00 38.07 ? 3193 HOH   B O     1 
HETATM 20994 O  O     . HOH   CA 11 .    ? 35.410  39.889  104.633 1.00 45.14 ? 3194 HOH   B O     1 
HETATM 20995 O  O     . HOH   CA 11 .    ? 2.019   43.329  55.868  1.00 32.39 ? 3195 HOH   B O     1 
HETATM 20996 O  O     . HOH   CA 11 .    ? 9.363   63.660  86.961  1.00 37.51 ? 3196 HOH   B O     1 
HETATM 20997 O  O     . HOH   CA 11 .    ? 21.093  74.244  81.885  1.00 39.99 ? 3197 HOH   B O     1 
HETATM 20998 O  O     . HOH   CA 11 .    ? 19.315  13.467  109.912 1.00 39.03 ? 3198 HOH   B O     1 
HETATM 20999 O  O     . HOH   CA 11 .    ? 32.068  32.179  75.384  1.00 26.22 ? 3199 HOH   B O     1 
HETATM 21000 O  O     . HOH   CA 11 .    ? 31.228  25.669  73.074  1.00 33.44 ? 3200 HOH   B O     1 
HETATM 21001 O  O     . HOH   CA 11 .    ? -32.107 29.338  121.225 1.00 47.51 ? 3201 HOH   B O     1 
HETATM 21002 O  O     . HOH   CA 11 .    ? -7.946  37.211  79.265  1.00 35.79 ? 3202 HOH   B O     1 
HETATM 21003 O  O     . HOH   CA 11 .    ? 36.662  41.867  88.980  1.00 40.17 ? 3203 HOH   B O     1 
HETATM 21004 O  O     . HOH   CA 11 .    ? -27.549 16.281  82.889  1.00 42.81 ? 3204 HOH   B O     1 
HETATM 21005 O  O     . HOH   CA 11 .    ? 16.866  25.841  109.710 1.00 24.32 ? 3205 HOH   B O     1 
HETATM 21006 O  O     . HOH   CA 11 .    ? -3.370  47.738  87.865  1.00 40.91 ? 3206 HOH   B O     1 
HETATM 21007 O  O     . HOH   CA 11 .    ? 0.495   24.017  99.092  1.00 35.77 ? 3207 HOH   B O     1 
HETATM 21008 O  O     . HOH   CA 11 .    ? 22.031  77.598  78.044  1.00 40.47 ? 3208 HOH   B O     1 
HETATM 21009 O  O     . HOH   CA 11 .    ? -0.593  3.402   81.454  1.00 38.94 ? 3209 HOH   B O     1 
HETATM 21010 O  O     . HOH   CA 11 .    ? 12.355  20.866  98.690  1.00 30.15 ? 3210 HOH   B O     1 
HETATM 21011 O  O     . HOH   CA 11 .    ? 6.392   60.229  87.961  1.00 35.85 ? 3211 HOH   B O     1 
HETATM 21012 O  O     . HOH   CA 11 .    ? 20.787  58.058  52.934  1.00 40.08 ? 3212 HOH   B O     1 
HETATM 21013 O  O     . HOH   CA 11 .    ? -7.254  22.182  78.706  1.00 30.27 ? 3213 HOH   B O     1 
HETATM 21014 O  O     . HOH   CA 11 .    ? -28.807 14.156  102.251 1.00 40.64 ? 3214 HOH   B O     1 
HETATM 21015 O  O     . HOH   CA 11 .    ? -11.502 -1.172  91.667  1.00 42.65 ? 3215 HOH   B O     1 
HETATM 21016 O  O     . HOH   CA 11 .    ? -1.262  37.808  132.865 1.00 46.71 ? 3216 HOH   B O     1 
HETATM 21017 O  O     . HOH   CA 11 .    ? 25.696  67.861  59.032  1.00 41.76 ? 3217 HOH   B O     1 
HETATM 21018 O  O     . HOH   CA 11 .    ? -3.449  39.517  74.364  1.00 33.05 ? 3218 HOH   B O     1 
HETATM 21019 O  O     . HOH   CA 11 .    ? 26.718  68.664  61.873  1.00 38.06 ? 3219 HOH   B O     1 
HETATM 21020 O  O     . HOH   CA 11 .    ? 14.279  21.528  95.155  1.00 37.53 ? 3220 HOH   B O     1 
HETATM 21021 O  O     . HOH   CA 11 .    ? -12.701 -8.324  106.078 1.00 37.09 ? 3221 HOH   B O     1 
HETATM 21022 O  O     . HOH   CA 11 .    ? 0.186   18.622  75.943  1.00 38.02 ? 3222 HOH   B O     1 
HETATM 21023 O  O     . HOH   CA 11 .    ? 33.446  15.244  64.834  1.00 39.55 ? 3223 HOH   B O     1 
HETATM 21024 O  O     . HOH   CA 11 .    ? 9.707   74.500  89.002  1.00 39.53 ? 3224 HOH   B O     1 
HETATM 21025 O  O     . HOH   CA 11 .    ? -11.950 29.857  81.670  1.00 39.57 ? 3225 HOH   B O     1 
HETATM 21026 O  O     . HOH   CA 11 .    ? 11.061  38.064  130.622 1.00 42.57 ? 3226 HOH   B O     1 
HETATM 21027 O  O     . HOH   CA 11 .    ? 2.281   23.860  129.762 1.00 37.91 ? 3227 HOH   B O     1 
HETATM 21028 O  O     . HOH   CA 11 .    ? -12.813 5.400   83.819  1.00 46.13 ? 3228 HOH   B O     1 
HETATM 21029 O  O     . HOH   CA 11 .    ? 30.423  30.605  79.040  1.00 30.58 ? 3229 HOH   B O     1 
HETATM 21030 O  O     . HOH   CA 11 .    ? 1.461   14.121  79.690  1.00 27.87 ? 3230 HOH   B O     1 
HETATM 21031 O  O     . HOH   CA 11 .    ? 11.885  17.124  89.462  1.00 32.37 ? 3231 HOH   B O     1 
HETATM 21032 O  O     . HOH   CA 11 .    ? -13.285 4.823   86.105  1.00 39.88 ? 3232 HOH   B O     1 
HETATM 21033 O  O     . HOH   CA 11 .    ? -12.684 8.871   129.622 1.00 37.13 ? 3233 HOH   B O     1 
HETATM 21034 O  O     . HOH   CA 11 .    ? -0.900  9.601   131.657 1.00 44.15 ? 3234 HOH   B O     1 
HETATM 21035 O  O     . HOH   CA 11 .    ? -31.658 17.830  84.814  1.00 46.95 ? 3235 HOH   B O     1 
HETATM 21036 O  O     . HOH   CA 11 .    ? 17.173  76.224  83.693  1.00 44.27 ? 3236 HOH   B O     1 
HETATM 21037 O  O     . HOH   CA 11 .    ? 37.393  44.089  90.490  1.00 37.39 ? 3237 HOH   B O     1 
HETATM 21038 O  O     . HOH   CA 11 .    ? 5.828   10.552  75.244  1.00 31.46 ? 3238 HOH   B O     1 
HETATM 21039 O  O     . HOH   CA 11 .    ? -2.715  28.085  68.995  1.00 26.72 ? 3239 HOH   B O     1 
HETATM 21040 O  O     . HOH   CA 11 .    ? 20.551  31.625  114.516 1.00 37.70 ? 3240 HOH   B O     1 
HETATM 21041 O  O     . HOH   CA 11 .    ? 10.253  52.929  89.319  1.00 38.06 ? 3241 HOH   B O     1 
HETATM 21042 O  O     . HOH   CA 11 .    ? -22.282 3.572   93.064  1.00 45.41 ? 3242 HOH   B O     1 
HETATM 21043 O  O     . HOH   CA 11 .    ? 33.717  46.865  64.965  1.00 44.11 ? 3243 HOH   B O     1 
HETATM 21044 O  O     . HOH   CA 11 .    ? -21.622 25.456  96.813  1.00 39.14 ? 3244 HOH   B O     1 
HETATM 21045 O  O     . HOH   CA 11 .    ? 5.203   31.393  92.816  1.00 36.31 ? 3245 HOH   B O     1 
HETATM 21046 O  O     . HOH   CA 11 .    ? 6.710   23.519  124.982 1.00 34.36 ? 3246 HOH   B O     1 
HETATM 21047 O  O     . HOH   CA 11 .    ? 6.566   41.659  46.934  1.00 40.88 ? 3247 HOH   B O     1 
HETATM 21048 O  O     . HOH   CA 11 .    ? 24.273  32.365  115.520 1.00 34.95 ? 3248 HOH   B O     1 
HETATM 21049 O  O     B HOH   CA 11 .    ? -3.577  59.799  85.140  0.43 23.47 ? 3249 HOH   B O     1 
HETATM 21050 O  O     . HOH   CA 11 .    ? -7.088  43.887  85.399  1.00 45.23 ? 3250 HOH   B O     1 
HETATM 21051 O  O     . HOH   CA 11 .    ? -10.285 -7.246  105.925 1.00 27.79 ? 3251 HOH   B O     1 
HETATM 21052 O  O     . HOH   CA 11 .    ? 25.219  70.148  65.379  1.00 33.77 ? 3252 HOH   B O     1 
HETATM 21053 O  O     . HOH   CA 11 .    ? 17.583  42.078  46.396  1.00 45.04 ? 3253 HOH   B O     1 
HETATM 21054 O  O     . HOH   CA 11 .    ? 7.062   18.517  89.840  1.00 29.30 ? 3254 HOH   B O     1 
HETATM 21055 O  O     . HOH   CA 11 .    ? 30.926  62.558  58.786  1.00 38.39 ? 3255 HOH   B O     1 
HETATM 21056 O  O     . HOH   CA 11 .    ? 7.022   2.148   79.913  1.00 36.92 ? 3256 HOH   B O     1 
HETATM 21057 O  O     . HOH   CA 11 .    ? 12.764  17.859  92.030  1.00 31.37 ? 3257 HOH   B O     1 
HETATM 21058 O  O     . HOH   CA 11 .    ? -33.203 18.142  97.220  1.00 45.92 ? 3258 HOH   B O     1 
HETATM 21059 O  O     . HOH   CA 11 .    ? 21.498  10.932  98.981  1.00 43.31 ? 3259 HOH   B O     1 
HETATM 21060 O  O     . HOH   CA 11 .    ? 23.429  71.224  61.489  1.00 40.86 ? 3260 HOH   B O     1 
HETATM 21061 O  O     . HOH   CA 11 .    ? 20.534  22.704  109.749 1.00 32.34 ? 3261 HOH   B O     1 
HETATM 21062 O  O     . HOH   CA 11 .    ? 20.783  68.536  85.562  1.00 49.81 ? 3262 HOH   B O     1 
HETATM 21063 O  O     . HOH   CA 11 .    ? -3.996  39.920  60.592  1.00 28.84 ? 3263 HOH   B O     1 
HETATM 21064 O  O     . HOH   CA 11 .    ? 32.746  27.420  74.293  1.00 38.13 ? 3264 HOH   B O     1 
HETATM 21065 O  O     . HOH   CA 11 .    ? 1.157   31.194  82.665  1.00 27.50 ? 3265 HOH   B O     1 
HETATM 21066 O  O     . HOH   CA 11 .    ? -7.940  -2.988  117.693 1.00 33.15 ? 3266 HOH   B O     1 
HETATM 21067 O  O     . HOH   CA 11 .    ? 8.463   76.808  88.378  1.00 42.04 ? 3267 HOH   B O     1 
HETATM 21068 O  O     . HOH   CA 11 .    ? 40.930  30.917  84.258  1.00 38.06 ? 3268 HOH   B O     1 
HETATM 21069 O  O     . HOH   CA 11 .    ? -37.620 15.651  96.106  1.00 52.12 ? 3269 HOH   B O     1 
HETATM 21070 O  O     . HOH   CA 11 .    ? 35.679  29.146  53.890  1.00 43.21 ? 3270 HOH   B O     1 
HETATM 21071 O  O     . HOH   CA 11 .    ? 14.115  24.798  100.724 1.00 23.85 ? 3271 HOH   B O     1 
HETATM 21072 O  O     . HOH   CA 11 .    ? 24.956  54.924  94.918  1.00 38.98 ? 3272 HOH   B O     1 
HETATM 21073 O  O     . HOH   CA 11 .    ? -1.969  19.418  78.696  1.00 41.07 ? 3273 HOH   B O     1 
HETATM 21074 O  O     . HOH   CA 11 .    ? -2.094  25.942  101.266 1.00 38.76 ? 3274 HOH   B O     1 
HETATM 21075 O  O     . HOH   CA 11 .    ? -19.400 31.472  88.733  1.00 41.04 ? 3275 HOH   B O     1 
HETATM 21076 O  O     . HOH   CA 11 .    ? 32.997  40.601  59.078  1.00 36.37 ? 3276 HOH   B O     1 
HETATM 21077 O  O     . HOH   CA 11 .    ? 1.692   11.013  76.790  1.00 34.35 ? 3277 HOH   B O     1 
HETATM 21078 O  O     . HOH   CA 11 .    ? 14.943  21.796  97.725  1.00 24.28 ? 3278 HOH   B O     1 
HETATM 21079 O  O     . HOH   CA 11 .    ? 12.931  4.288   93.731  1.00 46.39 ? 3279 HOH   B O     1 
HETATM 21080 O  O     . HOH   CA 11 .    ? 22.947  56.407  53.624  1.00 43.94 ? 3280 HOH   B O     1 
HETATM 21081 O  O     . HOH   CA 11 .    ? 10.635  74.518  60.530  1.00 43.87 ? 3281 HOH   B O     1 
HETATM 21082 O  O     . HOH   CA 11 .    ? 7.856   23.475  89.432  1.00 39.37 ? 3282 HOH   B O     1 
HETATM 21083 O  O     . HOH   CA 11 .    ? 36.032  22.074  65.077  1.00 42.14 ? 3283 HOH   B O     1 
HETATM 21084 O  O     . HOH   CA 11 .    ? 0.998   55.289  70.141  1.00 35.26 ? 3284 HOH   B O     1 
HETATM 21085 O  O     . HOH   CA 11 .    ? -11.084 -5.965  112.081 1.00 37.66 ? 3285 HOH   B O     1 
HETATM 21086 O  O     . HOH   CA 11 .    ? -7.134  -6.429  117.692 1.00 45.70 ? 3286 HOH   B O     1 
HETATM 21087 O  O     . HOH   CA 11 .    ? 6.616   -10.121 104.992 1.00 41.61 ? 3287 HOH   B O     1 
HETATM 21088 O  O     . HOH   CA 11 .    ? -32.815 16.669  88.883  1.00 44.28 ? 3288 HOH   B O     1 
HETATM 21089 O  O     . HOH   CA 11 .    ? 10.766  0.450   107.199 1.00 36.23 ? 3289 HOH   B O     1 
HETATM 21090 O  O     . HOH   CA 11 .    ? 11.767  0.422   113.790 1.00 37.46 ? 3290 HOH   B O     1 
HETATM 21091 O  O     . HOH   CA 11 .    ? -18.598 12.924  79.969  1.00 41.92 ? 3291 HOH   B O     1 
HETATM 21092 O  O     . HOH   CA 11 .    ? -4.915  3.013   83.343  1.00 43.25 ? 3292 HOH   B O     1 
HETATM 21093 O  O     . HOH   CA 11 .    ? 6.286   27.589  87.990  1.00 38.37 ? 3293 HOH   B O     1 
HETATM 21094 O  O     . HOH   CA 11 .    ? -15.947 6.227   122.475 1.00 34.13 ? 3294 HOH   B O     1 
HETATM 21095 O  O     . HOH   CA 11 .    ? -15.161 7.312   124.843 1.00 34.65 ? 3295 HOH   B O     1 
HETATM 21096 O  O     . HOH   CA 11 .    ? 25.785  10.999  68.403  1.00 44.11 ? 3296 HOH   B O     1 
HETATM 21097 O  O     . HOH   CA 11 .    ? 14.957  50.853  56.122  1.00 35.58 ? 3297 HOH   B O     1 
HETATM 21098 O  O     . HOH   CA 11 .    ? 22.808  16.719  108.313 1.00 37.59 ? 3298 HOH   B O     1 
HETATM 21099 O  O     . HOH   CA 11 .    ? -4.675  13.908  82.179  1.00 42.19 ? 3299 HOH   B O     1 
HETATM 21100 O  O     . HOH   CA 11 .    ? 6.481   15.566  92.140  1.00 27.52 ? 3300 HOH   B O     1 
HETATM 21101 O  O     . HOH   CA 11 .    ? -0.871  18.360  68.153  1.00 43.07 ? 3301 HOH   B O     1 
HETATM 21102 O  O     . HOH   CA 11 .    ? 14.970  1.380   100.204 1.00 43.47 ? 3302 HOH   B O     1 
HETATM 21103 O  O     . HOH   CA 11 .    ? 34.646  26.030  56.893  1.00 27.74 ? 3303 HOH   B O     1 
HETATM 21104 O  O     . HOH   CA 11 .    ? 12.040  43.474  53.516  1.00 28.61 ? 3304 HOH   B O     1 
HETATM 21105 O  O     . HOH   CA 11 .    ? 5.200   2.978   85.898  1.00 31.41 ? 3305 HOH   B O     1 
HETATM 21106 O  O     . HOH   CA 11 .    ? 7.361   53.516  90.684  1.00 42.41 ? 3306 HOH   B O     1 
HETATM 21107 O  O     . HOH   CA 11 .    ? -23.859 17.290  79.671  1.00 45.20 ? 3307 HOH   B O     1 
HETATM 21108 O  O     . HOH   CA 11 .    ? 19.006  48.105  56.548  1.00 30.74 ? 3308 HOH   B O     1 
HETATM 21109 O  O     . HOH   CA 11 .    ? -10.784 33.126  84.100  1.00 41.99 ? 3309 HOH   B O     1 
HETATM 21110 O  O     . HOH   CA 11 .    ? 31.690  62.739  66.290  1.00 47.42 ? 3310 HOH   B O     1 
HETATM 21111 O  O     . HOH   CA 11 .    ? -19.485 3.563   95.910  1.00 40.90 ? 3311 HOH   B O     1 
HETATM 21112 O  O     . HOH   CA 11 .    ? 0.917   6.610   78.932  1.00 43.66 ? 3312 HOH   B O     1 
HETATM 21113 O  O     . HOH   CA 11 .    ? 5.091   55.708  66.949  1.00 37.30 ? 3313 HOH   B O     1 
HETATM 21114 O  O     . HOH   CA 11 .    ? 20.093  33.858  115.072 1.00 26.41 ? 3314 HOH   B O     1 
HETATM 21115 O  O     . HOH   CA 11 .    ? 18.089  3.299   73.392  1.00 38.32 ? 3315 HOH   B O     1 
HETATM 21116 O  O     . HOH   CA 11 .    ? 20.781  46.251  51.828  1.00 46.99 ? 3316 HOH   B O     1 
HETATM 21117 O  O     . HOH   CA 11 .    ? 16.503  76.699  62.058  1.00 40.33 ? 3317 HOH   B O     1 
HETATM 21118 O  O     . HOH   CA 11 .    ? -18.856 14.498  132.106 1.00 46.88 ? 3318 HOH   B O     1 
HETATM 21119 O  O     . HOH   CA 11 .    ? 13.640  36.167  74.283  1.00 17.98 ? 3319 HOH   B O     1 
HETATM 21120 O  O     . HOH   CA 11 .    ? -15.341 6.377   87.086  1.00 37.31 ? 3320 HOH   B O     1 
HETATM 21121 O  O     . HOH   CA 11 .    ? 9.436   3.561   83.811  1.00 28.05 ? 3321 HOH   B O     1 
HETATM 21122 O  O     . HOH   CA 11 .    ? 12.542  7.360   68.219  1.00 35.18 ? 3322 HOH   B O     1 
HETATM 21123 O  O     . HOH   CA 11 .    ? 2.223   -8.035  98.714  1.00 38.93 ? 3323 HOH   B O     1 
HETATM 21124 O  O     . HOH   CA 11 .    ? 34.596  27.230  61.285  1.00 29.27 ? 3324 HOH   B O     1 
HETATM 21125 O  O     . HOH   CA 11 .    ? -24.580 8.466   85.486  1.00 47.61 ? 3325 HOH   B O     1 
HETATM 21126 O  O     . HOH   CA 11 .    ? 5.598   81.475  77.611  1.00 42.14 ? 3326 HOH   B O     1 
HETATM 21127 O  O     . HOH   CA 11 .    ? 32.749  44.645  57.227  1.00 44.27 ? 3327 HOH   B O     1 
HETATM 21128 O  O     . HOH   CA 11 .    ? 3.295   13.061  77.598  1.00 31.81 ? 3328 HOH   B O     1 
HETATM 21129 O  O     . HOH   CA 11 .    ? 31.857  32.106  80.915  1.00 37.24 ? 3329 HOH   B O     1 
HETATM 21130 O  O     . HOH   CA 11 .    ? -17.470 6.576   93.166  1.00 34.92 ? 3330 HOH   B O     1 
HETATM 21131 O  O     . HOH   CA 11 .    ? 15.851  59.501  92.703  1.00 39.30 ? 3331 HOH   B O     1 
HETATM 21132 O  O     . HOH   CA 11 .    ? 14.438  35.141  81.877  1.00 19.78 ? 3332 HOH   B O     1 
HETATM 21133 O  O     . HOH   CA 11 .    ? -13.523 16.807  78.671  1.00 35.81 ? 3333 HOH   B O     1 
HETATM 21134 O  O     . HOH   CA 11 .    ? 2.018   64.470  87.193  1.00 43.25 ? 3334 HOH   B O     1 
HETATM 21135 O  O     . HOH   CA 11 .    ? 14.652  6.584   91.938  1.00 38.38 ? 3335 HOH   B O     1 
HETATM 21136 O  O     . HOH   CA 11 .    ? 7.550   27.788  83.920  1.00 44.82 ? 3336 HOH   B O     1 
HETATM 21137 O  O     . HOH   CA 11 .    ? 15.600  72.614  58.570  1.00 37.59 ? 3337 HOH   B O     1 
HETATM 21138 O  O     . HOH   CA 11 .    ? 6.845   60.603  85.220  1.00 25.66 ? 3338 HOH   B O     1 
HETATM 21139 O  O     . HOH   CA 11 .    ? 21.910  19.389  107.220 1.00 25.15 ? 3339 HOH   B O     1 
HETATM 21140 O  O     . HOH   CA 11 .    ? -9.270  -2.249  122.088 1.00 42.11 ? 3340 HOH   B O     1 
HETATM 21141 O  O     . HOH   CA 11 .    ? 11.599  2.144   84.639  1.00 38.07 ? 3341 HOH   B O     1 
HETATM 21142 O  O     . HOH   CA 11 .    ? 30.449  63.846  71.260  1.00 37.91 ? 3342 HOH   B O     1 
HETATM 21143 O  O     . HOH   CA 11 .    ? -15.733 -1.058  98.601  1.00 43.59 ? 3343 HOH   B O     1 
HETATM 21144 O  O     . HOH   CA 11 .    ? -15.166 3.259   90.435  1.00 42.45 ? 3344 HOH   B O     1 
HETATM 21145 O  O     . HOH   CA 11 .    ? 9.176   -5.482  117.033 1.00 42.74 ? 3345 HOH   B O     1 
HETATM 21146 O  O     . HOH   CA 11 .    ? -10.713 46.809  77.341  1.00 34.86 ? 3346 HOH   B O     1 
HETATM 21147 O  O     . HOH   CA 11 .    ? 14.835  43.663  52.932  1.00 32.31 ? 3347 HOH   B O     1 
HETATM 21148 O  O     . HOH   CA 11 .    ? 9.107   64.548  66.204  1.00 32.33 ? 3348 HOH   B O     1 
HETATM 21149 O  O     . HOH   CA 11 .    ? 8.117   30.975  86.214  1.00 36.17 ? 3349 HOH   B O     1 
HETATM 21150 O  O     . HOH   CA 11 .    ? 12.512  0.235   109.140 1.00 33.30 ? 3350 HOH   B O     1 
HETATM 21151 O  O     . HOH   CA 11 .    ? 31.913  66.600  65.618  1.00 45.91 ? 3351 HOH   B O     1 
HETATM 21152 O  O     . HOH   CA 11 .    ? -7.080  24.857  75.040  1.00 31.19 ? 3352 HOH   B O     1 
HETATM 21153 O  O     . HOH   CA 11 .    ? 4.849   63.800  86.605  1.00 35.40 ? 3353 HOH   B O     1 
HETATM 21154 O  O     . HOH   CA 11 .    ? -9.215  -0.682  86.893  1.00 42.22 ? 3354 HOH   B O     1 
HETATM 21155 O  O     . HOH   CA 11 .    ? 9.105   24.258  87.210  1.00 32.04 ? 3355 HOH   B O     1 
HETATM 21156 O  O     . HOH   CA 11 .    ? 42.021  36.745  90.014  1.00 32.36 ? 3356 HOH   B O     1 
HETATM 21157 O  O     . HOH   CA 11 .    ? -0.293  56.695  68.025  1.00 37.86 ? 3357 HOH   B O     1 
HETATM 21158 O  O     . HOH   CA 11 .    ? 22.760  81.787  69.107  1.00 43.84 ? 3358 HOH   B O     1 
HETATM 21159 O  O     . HOH   CA 11 .    ? 12.973  55.401  105.520 1.00 32.24 ? 3359 HOH   B O     1 
HETATM 21160 O  O     . HOH   CA 11 .    ? -0.243  79.983  77.620  1.00 46.85 ? 3360 HOH   B O     1 
HETATM 21161 O  O     . HOH   CA 11 .    ? 10.355  25.337  99.657  1.00 44.06 ? 3361 HOH   B O     1 
HETATM 21162 O  O     . HOH   CA 11 .    ? 19.002  78.378  65.309  1.00 38.53 ? 3362 HOH   B O     1 
HETATM 21163 O  O     . HOH   CA 11 .    ? 30.513  23.537  74.465  1.00 26.28 ? 3363 HOH   B O     1 
HETATM 21164 O  O     . HOH   CA 11 .    ? 14.558  51.598  61.125  1.00 42.01 ? 3364 HOH   B O     1 
HETATM 21165 O  O     . HOH   CA 11 .    ? 18.464  8.984   95.681  1.00 32.71 ? 3365 HOH   B O     1 
HETATM 21166 O  O     . HOH   CA 11 .    ? 13.142  74.516  60.918  1.00 38.44 ? 3366 HOH   B O     1 
HETATM 21167 O  O     . HOH   CA 11 .    ? -7.448  46.812  133.277 1.00 40.71 ? 3367 HOH   B O     1 
HETATM 21168 O  O     . HOH   CA 11 .    ? 20.428  67.131  53.995  1.00 42.20 ? 3368 HOH   B O     1 
HETATM 21169 O  O     . HOH   CA 11 .    ? 26.476  52.053  83.907  1.00 33.10 ? 3369 HOH   B O     1 
HETATM 21170 O  O     . HOH   CA 11 .    ? 18.580  2.712   77.645  1.00 38.33 ? 3370 HOH   B O     1 
HETATM 21171 O  O     . HOH   CA 11 .    ? -8.340  33.353  85.302  1.00 30.99 ? 3371 HOH   B O     1 
HETATM 21172 O  O     . HOH   CA 11 .    ? 2.206   44.338  97.028  1.00 31.37 ? 3372 HOH   B O     1 
HETATM 21173 O  O     . HOH   CA 11 .    ? -22.409 24.214  82.406  1.00 43.56 ? 3373 HOH   B O     1 
HETATM 21174 O  O     . HOH   CA 11 .    ? 2.927   9.880   74.955  1.00 41.22 ? 3374 HOH   B O     1 
HETATM 21175 O  O     . HOH   CA 11 .    ? -4.616  10.921  80.939  1.00 42.64 ? 3375 HOH   B O     1 
HETATM 21176 O  O     . HOH   CA 11 .    ? 13.332  36.525  77.248  1.00 17.98 ? 3376 HOH   B O     1 
HETATM 21177 O  O     . HOH   CA 11 .    ? 15.288  4.202   70.098  1.00 41.51 ? 3377 HOH   B O     1 
HETATM 21178 O  O     . HOH   CA 11 .    ? 10.817  44.973  130.108 1.00 43.17 ? 3378 HOH   B O     1 
HETATM 21179 O  O     . HOH   CA 11 .    ? 13.853  24.310  98.169  1.00 27.53 ? 3379 HOH   B O     1 
HETATM 21180 O  O     . HOH   CA 11 .    ? -19.170 0.366   97.580  1.00 38.86 ? 3380 HOH   B O     1 
HETATM 21181 O  O     . HOH   CA 11 .    ? 6.278   11.830  73.078  1.00 32.31 ? 3381 HOH   B O     1 
HETATM 21182 O  O     . HOH   CA 11 .    ? -5.654  33.615  62.468  1.00 42.44 ? 3382 HOH   B O     1 
HETATM 21183 O  O     . HOH   CA 11 .    ? 31.864  69.286  80.370  1.00 34.22 ? 3383 HOH   B O     1 
HETATM 21184 O  O     . HOH   CA 11 .    ? -8.949  3.381   85.064  1.00 37.87 ? 3384 HOH   B O     1 
HETATM 21185 O  O     . HOH   CA 11 .    ? 5.588   70.166  87.044  1.00 39.74 ? 3385 HOH   B O     1 
HETATM 21186 O  O     . HOH   CA 11 .    ? -11.505 1.603   89.112  1.00 30.77 ? 3386 HOH   B O     1 
HETATM 21187 O  O     . HOH   CA 11 .    ? 15.239  55.607  104.348 1.00 29.57 ? 3387 HOH   B O     1 
HETATM 21188 O  O     . HOH   CA 11 .    ? -5.604  37.965  61.729  1.00 37.11 ? 3388 HOH   B O     1 
HETATM 21189 O  O     . HOH   CA 11 .    ? 32.666  59.644  62.735  1.00 33.02 ? 3389 HOH   B O     1 
HETATM 21190 O  O     . HOH   CA 11 .    ? 12.989  59.115  85.722  1.00 36.58 ? 3390 HOH   B O     1 
HETATM 21191 O  O     . HOH   CA 11 .    ? 22.725  50.006  68.758  1.00 25.68 ? 3391 HOH   B O     1 
HETATM 21192 O  O     . HOH   CA 11 .    ? -9.556  34.536  90.121  1.00 42.05 ? 3392 HOH   B O     1 
HETATM 21193 O  O     . HOH   CA 11 .    ? 5.513   30.241  86.740  1.00 36.72 ? 3393 HOH   B O     1 
HETATM 21194 O  O     . HOH   CA 11 .    ? 8.945   44.176  50.243  1.00 38.62 ? 3394 HOH   B O     1 
HETATM 21195 O  O     . HOH   CA 11 .    ? 27.657  54.618  83.498  1.00 37.73 ? 3395 HOH   B O     1 
HETATM 21196 O  O     . HOH   CA 11 .    ? 12.021  1.279   116.042 1.00 34.10 ? 3396 HOH   B O     1 
HETATM 21197 O  O     . HOH   CA 11 .    ? -25.203 12.743  86.751  1.00 32.00 ? 3397 HOH   B O     1 
HETATM 21198 O  O     . HOH   CA 11 .    ? 12.729  20.346  91.672  1.00 37.56 ? 3398 HOH   B O     1 
HETATM 21199 O  O     . HOH   CA 11 .    ? 24.283  76.150  78.732  1.00 43.05 ? 3399 HOH   B O     1 
HETATM 21200 O  O     . HOH   CA 11 .    ? 3.855   47.582  89.366  1.00 34.80 ? 3400 HOH   B O     1 
HETATM 21201 O  O     . HOH   CA 11 .    ? 20.124  10.579  96.615  1.00 36.13 ? 3401 HOH   B O     1 
HETATM 21202 O  O     . HOH   CA 11 .    ? 0.610   19.697  64.822  1.00 37.15 ? 3402 HOH   B O     1 
HETATM 21203 O  O     . HOH   CA 11 .    ? -7.625  36.642  83.945  1.00 34.34 ? 3403 HOH   B O     1 
HETATM 21204 O  O     . HOH   CA 11 .    ? 21.791  4.345   70.646  1.00 43.27 ? 3404 HOH   B O     1 
HETATM 21205 O  O     . HOH   CA 11 .    ? -6.324  35.827  61.636  1.00 41.15 ? 3405 HOH   B O     1 
HETATM 21206 O  O     . HOH   CA 11 .    ? 35.053  38.314  64.714  1.00 37.41 ? 3406 HOH   B O     1 
HETATM 21207 O  O     . HOH   CA 11 .    ? -4.210  22.925  72.474  1.00 40.46 ? 3407 HOH   B O     1 
HETATM 21208 O  O     . HOH   CA 11 .    ? 10.614  59.558  86.565  1.00 42.66 ? 3408 HOH   B O     1 
HETATM 21209 O  O     . HOH   CA 11 .    ? 23.736  59.238  98.532  1.00 45.70 ? 3409 HOH   B O     1 
HETATM 21210 O  O     . HOH   CA 11 .    ? 9.437   16.804  89.927  1.00 28.59 ? 3410 HOH   B O     1 
HETATM 21211 O  O     . HOH   CA 11 .    ? -8.442  42.587  134.184 1.00 47.49 ? 3411 HOH   B O     1 
HETATM 21212 O  O     . HOH   CA 11 .    ? 11.280  0.274   86.734  1.00 40.20 ? 3412 HOH   B O     1 
HETATM 21213 O  O     . HOH   CA 11 .    ? 0.148   28.497  96.666  1.00 24.15 ? 3413 HOH   B O     1 
HETATM 21214 O  O     . HOH   CA 11 .    ? -16.864 53.642  124.984 1.00 47.31 ? 3414 HOH   B O     1 
HETATM 21215 O  O     . HOH   CA 11 .    ? -16.121 7.446   91.074  1.00 28.64 ? 3415 HOH   B O     1 
HETATM 21216 O  O     . HOH   CA 11 .    ? 6.488   -5.093  101.972 1.00 37.43 ? 3416 HOH   B O     1 
HETATM 21217 O  O     . HOH   CA 11 .    ? -12.540 -0.762  121.535 1.00 39.30 ? 3417 HOH   B O     1 
HETATM 21218 O  O     . HOH   CA 11 .    ? -11.016 3.534   86.968  1.00 31.93 ? 3418 HOH   B O     1 
HETATM 21219 O  O     . HOH   CA 11 .    ? 33.590  19.148  54.196  1.00 35.18 ? 3419 HOH   B O     1 
HETATM 21220 O  O     . HOH   CA 11 .    ? -7.146  -5.386  91.673  1.00 38.94 ? 3420 HOH   B O     1 
HETATM 21221 O  O     . HOH   CA 11 .    ? -16.643 3.740   123.637 1.00 38.57 ? 3421 HOH   B O     1 
HETATM 21222 O  O     . HOH   CA 11 .    ? -2.970  37.629  78.095  1.00 27.34 ? 3422 HOH   B O     1 
HETATM 21223 O  O     . HOH   CA 11 .    ? -4.947  -1.119  84.374  1.00 39.70 ? 3423 HOH   B O     1 
HETATM 21224 O  O     . HOH   CA 11 .    ? -18.284 21.868  80.859  1.00 38.74 ? 3424 HOH   B O     1 
HETATM 21225 O  O     . HOH   CA 11 .    ? -13.917 22.551  81.610  1.00 37.83 ? 3425 HOH   B O     1 
HETATM 21226 O  O     . HOH   CA 11 .    ? 2.209   21.561  61.239  1.00 31.10 ? 3426 HOH   B O     1 
HETATM 21227 O  O     . HOH   CA 11 .    ? -21.075 16.393  80.112  1.00 38.01 ? 3427 HOH   B O     1 
HETATM 21228 O  O     . HOH   CA 11 .    ? 28.572  50.838  83.952  1.00 38.04 ? 3428 HOH   B O     1 
HETATM 21229 O  O     . HOH   CA 11 .    ? -1.196  22.985  63.966  1.00 31.67 ? 3429 HOH   B O     1 
HETATM 21230 O  O     . HOH   CA 11 .    ? -23.390 13.924  82.412  1.00 31.02 ? 3430 HOH   B O     1 
HETATM 21231 O  O     . HOH   CA 11 .    ? 3.217   14.687  75.581  1.00 29.97 ? 3431 HOH   B O     1 
HETATM 21232 O  O     . HOH   CA 11 .    ? 13.944  44.238  49.595  1.00 39.13 ? 3432 HOH   B O     1 
HETATM 21233 O  O     . HOH   CA 11 .    ? -6.459  17.492  77.966  1.00 38.55 ? 3433 HOH   B O     1 
HETATM 21234 O  O     . HOH   CA 11 .    ? 36.331  28.242  56.244  1.00 42.72 ? 3434 HOH   B O     1 
HETATM 21235 O  O     . HOH   CA 11 .    ? -9.151  42.598  57.908  1.00 36.95 ? 3435 HOH   B O     1 
HETATM 21236 O  O     . HOH   CA 11 .    ? 4.900   -6.263  91.754  1.00 41.81 ? 3436 HOH   B O     1 
HETATM 21237 O  O     . HOH   CA 11 .    ? -4.587  29.927  59.956  1.00 43.33 ? 3437 HOH   B O     1 
HETATM 21238 O  O     . HOH   CA 11 .    ? -20.048 7.925   83.736  1.00 42.72 ? 3438 HOH   B O     1 
HETATM 21239 O  O     . HOH   CA 11 .    ? -8.239  35.055  87.531  1.00 40.75 ? 3439 HOH   B O     1 
HETATM 21240 O  O     . HOH   CA 11 .    ? -11.535 -2.745  93.693  1.00 44.15 ? 3440 HOH   B O     1 
HETATM 21241 O  O     . HOH   CA 11 .    ? 31.353  73.274  69.968  1.00 40.26 ? 3441 HOH   B O     1 
HETATM 21242 O  O     . HOH   CA 11 .    ? 9.572   9.852   67.904  1.00 37.70 ? 3442 HOH   B O     1 
HETATM 21243 O  O     . HOH   CA 11 .    ? 2.319   31.539  85.130  1.00 23.64 ? 3443 HOH   B O     1 
HETATM 21244 O  O     . HOH   CA 11 .    ? -19.584 6.955   124.475 1.00 37.30 ? 3444 HOH   B O     1 
HETATM 21245 O  O     . HOH   CA 11 .    ? 11.380  -0.410  104.545 1.00 43.16 ? 3445 HOH   B O     1 
HETATM 21246 O  O     . HOH   CA 11 .    ? -19.316 19.867  78.928  1.00 40.30 ? 3446 HOH   B O     1 
HETATM 21247 O  O     . HOH   CA 11 .    ? 32.502  24.831  50.926  1.00 39.27 ? 3447 HOH   B O     1 
HETATM 21248 O  O     . HOH   CA 11 .    ? 41.420  27.565  91.213  1.00 39.93 ? 3448 HOH   B O     1 
HETATM 21249 O  O     . HOH   CA 11 .    ? -4.770  23.283  75.218  1.00 27.92 ? 3449 HOH   B O     1 
HETATM 21250 O  O     . HOH   CA 11 .    ? 33.608  43.613  59.333  1.00 42.12 ? 3450 HOH   B O     1 
HETATM 21251 O  O     . HOH   CA 11 .    ? -17.491 6.261   85.313  1.00 45.84 ? 3451 HOH   B O     1 
HETATM 21252 O  O     . HOH   CA 11 .    ? 18.462  2.586   69.111  1.00 49.02 ? 3452 HOH   B O     1 
HETATM 21253 O  O     . HOH   CA 11 .    ? 11.364  59.859  92.620  1.00 36.27 ? 3453 HOH   B O     1 
HETATM 21254 O  O     . HOH   CA 11 .    ? -26.123 24.213  97.230  1.00 38.57 ? 3454 HOH   B O     1 
HETATM 21255 O  O     . HOH   CA 11 .    ? -2.368  23.051  61.532  1.00 35.90 ? 3455 HOH   B O     1 
HETATM 21256 O  O     . HOH   CA 11 .    ? 19.520  31.504  45.436  1.00 39.61 ? 3456 HOH   B O     1 
HETATM 21257 O  O     . HOH   CA 11 .    ? 22.271  31.009  45.362  1.00 35.88 ? 3457 HOH   B O     1 
HETATM 21258 O  O     . HOH   CA 11 .    ? 32.951  22.909  74.917  1.00 42.41 ? 3458 HOH   B O     1 
HETATM 21259 O  O     . HOH   CA 11 .    ? 0.974   27.237  98.972  1.00 36.86 ? 3459 HOH   B O     1 
HETATM 21260 O  O     . HOH   CA 11 .    ? -18.559 3.620   89.167  1.00 47.09 ? 3460 HOH   B O     1 
HETATM 21261 O  O     . HOH   CA 11 .    ? -24.804 12.554  84.089  1.00 35.21 ? 3461 HOH   B O     1 
HETATM 21262 O  O     . HOH   CA 11 .    ? 22.762  28.909  44.037  1.00 40.54 ? 3462 HOH   B O     1 
HETATM 21263 O  O     . HOH   CA 11 .    ? -7.617  44.641  135.078 1.00 50.04 ? 3463 HOH   B O     1 
HETATM 21264 O  O     . HOH   CA 11 .    ? 7.221   1.745   84.402  1.00 32.92 ? 3464 HOH   B O     1 
HETATM 21265 O  O     . HOH   CA 11 .    ? 32.758  62.324  61.737  1.00 44.29 ? 3465 HOH   B O     1 
HETATM 21266 O  O     . HOH   CA 11 .    ? 19.585  2.494   71.096  1.00 45.64 ? 3466 HOH   B O     1 
HETATM 21267 O  O     . HOH   CA 11 .    ? -20.410 23.752  80.725  1.00 43.17 ? 3467 HOH   B O     1 
HETATM 21268 O  O     . HOH   CA 11 .    ? -15.915 5.428   89.214  1.00 39.57 ? 3468 HOH   B O     1 
HETATM 21269 O  O     . HOH   CA 11 .    ? -24.641 10.126  83.525  1.00 48.23 ? 3469 HOH   B O     1 
HETATM 21270 O  O     . HOH   CA 11 .    ? 18.177  1.461   75.558  1.00 45.70 ? 3470 HOH   B O     1 
HETATM 21271 O  O     . HOH   CA 11 .    ? 10.636  -2.373  103.628 1.00 41.08 ? 3471 HOH   B O     1 
HETATM 21272 O  O     . HOH   CA 11 .    ? -16.458 23.501  78.768  1.00 44.03 ? 3472 HOH   B O     1 
HETATM 21273 O  O     . HOH   CA 11 .    ? -24.877 25.796  95.421  1.00 44.62 ? 3473 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   ? 0.6146 0.6625 0.6978 0.0936  -0.0256 -0.1274 14   ALA A N   
2     C CA  . ALA A 16   ? 0.6169 0.6638 0.6905 0.0902  -0.0226 -0.1208 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5780 0.6322 0.6427 0.0889  -0.0172 -0.1147 14   ALA A C   
4     O O   . ALA A 16   ? 0.5732 0.6393 0.6360 0.0919  -0.0149 -0.1183 14   ALA A O   
5     C CB  . ALA A 16   ? 0.6086 0.6611 0.6801 0.0922  -0.0234 -0.1267 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5424 0.5898 0.6021 0.0843  -0.0152 -0.1054 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4805 0.5339 0.5325 0.0828  -0.0103 -0.0992 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4597 0.5236 0.5039 0.0838  -0.0073 -0.0999 15   PRO A C   
9     O O   . PRO A 17   ? 0.4642 0.5267 0.5063 0.0834  -0.0083 -0.1012 15   PRO A O   
10    C CB  . PRO A 17   ? 0.5112 0.5535 0.5606 0.0777  -0.0098 -0.0900 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5809 0.6143 0.6332 0.0765  -0.0133 -0.0911 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.5185 0.5528 0.5795 0.0804  -0.0173 -0.1002 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4255 0.5004 0.4658 0.0850  -0.0037 -0.0989 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3789 0.4653 0.4121 0.0860  -0.0008 -0.0992 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3310 0.4121 0.3574 0.0819  0.0009  -0.0915 16   ALA A C   
16    O O   . ALA A 18   ? 0.3422 0.4150 0.3675 0.0782  0.0018  -0.0842 16   ALA A O   
17    C CB  . ALA A 18   ? 0.4285 0.5270 0.4588 0.0873  0.0029  -0.0979 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3146 0.4006 0.3366 0.0824  0.0014  -0.0930 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3085 0.3893 0.3246 0.0786  0.0027  -0.0861 17   PRO A CA  
20    C C   . PRO A 19   ? 0.2940 0.3779 0.3047 0.0761  0.0067  -0.0778 17   PRO A C   
21    O O   . PRO A 19   ? 0.3229 0.4185 0.3313 0.0778  0.0093  -0.0778 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3646 0.4533 0.3774 0.0806  0.0026  -0.0904 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3911 0.4844 0.4098 0.0851  -0.0002 -0.1006 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3466 0.4429 0.3692 0.0866  0.0004  -0.1016 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2825 0.3562 0.2918 0.0721  0.0071  -0.0707 18   PHE A N   
26    C CA  . PHE A 20   ? 0.2939 0.3682 0.2987 0.0691  0.0103  -0.0624 18   PHE A CA  
27    C C   . PHE A 20   ? 0.2954 0.3730 0.3024 0.0695  0.0118  -0.0608 18   PHE A C   
28    O O   . PHE A 20   ? 0.3106 0.3912 0.3143 0.0676  0.0147  -0.0545 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2932 0.3769 0.2915 0.0690  0.0131  -0.0597 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2968 0.3776 0.2926 0.0684  0.0118  -0.0607 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2781 0.3486 0.2724 0.0648  0.0114  -0.0555 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.3032 0.3921 0.2984 0.0715  0.0110  -0.0671 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.2893 0.3572 0.2814 0.0642  0.0103  -0.0563 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.3270 0.4132 0.3199 0.0709  0.0097  -0.0680 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.3309 0.4065 0.3223 0.0673  0.0094  -0.0625 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3087 0.3857 0.3216 0.0720  0.0098  -0.0663 19   ALA A N   
37    C CA  . ALA A 21   ? 0.2930 0.3731 0.3083 0.0724  0.0111  -0.0649 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3539 0.4239 0.3697 0.0686  0.0114  -0.0579 19   ALA A C   
39    O O   . ALA A 21   ? 0.3718 0.4447 0.3881 0.0682  0.0132  -0.0548 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3721 0.4540 0.3942 0.0762  0.0086  -0.0729 19   ALA A CB  
41    N N   . ASP A 22   ? 0.2974 0.3563 0.3130 0.0659  0.0097  -0.0553 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3500 0.3996 0.3658 0.0622  0.0099  -0.0489 20   ASP A CA  
43    C C   . ASP A 22   ? 0.2902 0.3351 0.3009 0.0590  0.0108  -0.0436 20   ASP A C   
44    O O   . ASP A 22   ? 0.3046 0.3397 0.3160 0.0562  0.0096  -0.0404 20   ASP A O   
45    C CB  . ASP A 22   ? 0.4023 0.4420 0.4242 0.0619  0.0064  -0.0509 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.5675 0.6108 0.5952 0.0649  0.0053  -0.0557 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.5690 0.6207 0.5957 0.0662  0.0077  -0.0553 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.7214 0.7590 0.7549 0.0660  0.0019  -0.0597 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2557 0.3083 0.2616 0.0594  0.0129  -0.0427 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2405 0.2890 0.2422 0.0568  0.0133  -0.0389 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2457 0.2875 0.2460 0.0531  0.0144  -0.0317 21   PHE A C   
52    O O   . PHE A 23   ? 0.2326 0.2653 0.2330 0.0507  0.0130  -0.0298 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2491 0.3077 0.2460 0.0580  0.0154  -0.0388 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2344 0.2893 0.2272 0.0553  0.0160  -0.0344 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2514 0.2989 0.2443 0.0546  0.0137  -0.0362 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2620 0.3206 0.2511 0.0535  0.0186  -0.0282 21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2463 0.2905 0.2357 0.0522  0.0142  -0.0323 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2920 0.3470 0.2779 0.0512  0.0189  -0.0243 21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2587 0.3066 0.2446 0.0506  0.0168  -0.0265 21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2421 0.2888 0.2414 0.0525  0.0169  -0.0277 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2605 0.3016 0.2587 0.0490  0.0179  -0.0211 22   ALA A CA  
62    C C   . ALA A 24   ? 0.2302 0.2755 0.2297 0.0488  0.0197  -0.0182 22   ALA A C   
63    O O   . ALA A 24   ? 0.2437 0.2924 0.2411 0.0473  0.0218  -0.0132 22   ALA A O   
64    C CB  . ALA A 24   ? 0.2757 0.3177 0.2693 0.0473  0.0192  -0.0172 22   ALA A CB  
65    N N   . PRO A 25   ? 0.2640 0.3092 0.2676 0.0503  0.0187  -0.0211 23   PRO A N   
66    C CA  . PRO A 25   ? 0.2786 0.3283 0.2837 0.0502  0.0204  -0.0185 23   PRO A CA  
67    C C   . PRO A 25   ? 0.2685 0.3117 0.2733 0.0467  0.0210  -0.0123 23   PRO A C   
68    O O   . PRO A 25   ? 0.2643 0.2980 0.2698 0.0448  0.0192  -0.0116 23   PRO A O   
69    C CB  . PRO A 25   ? 0.3005 0.3489 0.3105 0.0524  0.0186  -0.0233 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.2907 0.3297 0.3023 0.0518  0.0157  -0.0257 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.2872 0.3270 0.2949 0.0517  0.0158  -0.0262 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2426 0.2909 0.2466 0.0457  0.0232  -0.0077 24   PRO A N   
73    C CA  . PRO A 26   ? 0.2515 0.2938 0.2557 0.0424  0.0236  -0.0022 24   PRO A CA  
74    C C   . PRO A 26   ? 0.2362 0.2728 0.2442 0.0420  0.0222  -0.0028 24   PRO A C   
75    O O   . PRO A 26   ? 0.2761 0.3152 0.2870 0.0442  0.0216  -0.0064 24   PRO A O   
76    C CB  . PRO A 26   ? 0.2860 0.3366 0.2895 0.0420  0.0261  0.0022  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.3528 0.4137 0.3569 0.0452  0.0271  -0.0014 24   PRO A CG  
78    C CD  . PRO A 26   ? 0.2706 0.3309 0.2738 0.0475  0.0255  -0.0075 24   PRO A CD  
79    N N   . VAL A 27   ? 0.2368 0.2659 0.2450 0.0391  0.0216  0.0008  25   VAL A N   
80    C CA  . VAL A 27   ? 0.2628 0.2865 0.2742 0.0381  0.0204  0.0013  25   VAL A CA  
81    C C   . VAL A 27   ? 0.2632 0.2932 0.2774 0.0392  0.0216  0.0018  25   VAL A C   
82    O O   . VAL A 27   ? 0.3084 0.3372 0.3259 0.0404  0.0204  -0.0006 25   VAL A O   
83    C CB  . VAL A 27   ? 0.2636 0.2804 0.2743 0.0348  0.0201  0.0055  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2850 0.2980 0.2989 0.0338  0.0191  0.0065  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2630 0.2735 0.2716 0.0338  0.0186  0.0045  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.2833 0.3200 0.2964 0.0389  0.0238  0.0051  26   ARG A N   
87    C CA  . ARG A 28   ? 0.2798 0.3234 0.2955 0.0397  0.0252  0.0062  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3298 0.3836 0.3435 0.0407  0.0276  0.0077  26   ARG A C   
89    O O   . ARG A 28   ? 0.2861 0.3404 0.2966 0.0400  0.0281  0.0091  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3305 0.3701 0.3481 0.0370  0.0254  0.0108  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3186 0.3579 0.3345 0.0344  0.0265  0.0159  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3380 0.3721 0.3561 0.0318  0.0260  0.0196  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.3714 0.3960 0.3892 0.0304  0.0239  0.0184  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.4151 0.4357 0.4351 0.0307  0.0224  0.0165  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.3859 0.4103 0.4087 0.0322  0.0226  0.0153  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.3626 0.3754 0.3819 0.0294  0.0206  0.0158  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.2756 0.3383 0.2912 0.0423  0.0290  0.0075  27   PRO A N   
98    C CA  . PRO A 29   ? 0.2799 0.3533 0.2938 0.0428  0.0314  0.0100  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2888 0.3605 0.3022 0.0395  0.0322  0.0168  27   PRO A C   
100   O O   . PRO A 29   ? 0.3109 0.3771 0.3268 0.0374  0.0317  0.0197  27   PRO A O   
101   C CB  . PRO A 29   ? 0.3319 0.4144 0.3488 0.0448  0.0325  0.0089  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3337 0.4110 0.3532 0.0465  0.0305  0.0034  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3050 0.3694 0.3245 0.0440  0.0285  0.0047  27   PRO A CD  
104   N N   . GLN A 30   ? 0.2992 0.3757 0.3099 0.0392  0.0333  0.0191  28   GLN A N   
105   C CA  . GLN A 30   ? 0.2825 0.3565 0.2932 0.0361  0.0337  0.0253  28   GLN A CA  
106   C C   . GLN A 30   ? 0.2801 0.3618 0.2938 0.0352  0.0354  0.0304  28   GLN A C   
107   O O   . GLN A 30   ? 0.3041 0.3970 0.3172 0.0366  0.0371  0.0312  28   GLN A O   
108   C CB  . GLN A 30   ? 0.3012 0.3772 0.3083 0.0361  0.0341  0.0261  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2702 0.3393 0.2745 0.0370  0.0324  0.0210  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2832 0.3400 0.2882 0.0348  0.0306  0.0215  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2592 0.3121 0.2636 0.0326  0.0305  0.0252  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2569 0.3079 0.2634 0.0353  0.0292  0.0179  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2823 0.3584 0.2992 0.0328  0.0349  0.0339  29   SER A N   
114   C CA  . SER A 31   ? 0.2567 0.3392 0.2771 0.0315  0.0362  0.0391  29   SER A CA  
115   C C   . SER A 31   ? 0.2813 0.3687 0.3013 0.0299  0.0372  0.0447  29   SER A C   
116   O O   . SER A 31   ? 0.2539 0.3383 0.2709 0.0295  0.0367  0.0447  29   SER A O   
117   C CB  . SER A 31   ? 0.2586 0.3329 0.2827 0.0292  0.0350  0.0412  29   SER A CB  
118   O OG  . SER A 31   ? 0.2432 0.3092 0.2667 0.0268  0.0338  0.0432  29   SER A OG  
119   N N   . THR A 32   ? 0.2726 0.3679 0.2958 0.0289  0.0385  0.0499  30   THR A N   
120   C CA  . THR A 32   ? 0.2303 0.3301 0.2543 0.0270  0.0392  0.0563  30   THR A CA  
121   C C   . THR A 32   ? 0.2406 0.3295 0.2655 0.0245  0.0374  0.0585  30   THR A C   
122   O O   . THR A 32   ? 0.2440 0.3330 0.2672 0.0238  0.0372  0.0606  30   THR A O   
123   C CB  . THR A 32   ? 0.2733 0.3814 0.3021 0.0258  0.0404  0.0620  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3518 0.4711 0.3797 0.0284  0.0422  0.0597  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.3153 0.4284 0.3458 0.0237  0.0408  0.0693  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2277 0.3075 0.2553 0.0231  0.0360  0.0577  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2278 0.2977 0.2565 0.0208  0.0342  0.0592  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2415 0.3052 0.2653 0.0218  0.0333  0.0548  31   LEU A C   
129   O O   . LEU A 33   ? 0.2265 0.2865 0.2500 0.0204  0.0326  0.0567  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2318 0.2941 0.2642 0.0194  0.0329  0.0587  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2759 0.3427 0.3142 0.0176  0.0333  0.0644  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2513 0.3124 0.2928 0.0168  0.0322  0.0630  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.3379 0.4036 0.3794 0.0152  0.0325  0.0699  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2147 0.2772 0.2353 0.0240  0.0333  0.0490  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2202 0.2772 0.2366 0.0248  0.0324  0.0451  32   ARG A CA  
136   C C   . ARG A 34   ? 0.2173 0.2808 0.2307 0.0256  0.0333  0.0462  32   ARG A C   
137   O O   . ARG A 34   ? 0.2344 0.2935 0.2456 0.0251  0.0325  0.0458  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2431 0.2976 0.2575 0.0269  0.0318  0.0389  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2315 0.2777 0.2481 0.0259  0.0304  0.0373  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2532 0.2896 0.2686 0.0243  0.0287  0.0367  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2385 0.2720 0.2501 0.0256  0.0280  0.0326  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.2504 0.2792 0.2610 0.0265  0.0269  0.0283  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2631 0.2899 0.2763 0.0265  0.0263  0.0274  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2735 0.2998 0.2810 0.0275  0.0261  0.0249  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2227 0.2974 0.2360 0.0270  0.0350  0.0475  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2215 0.3037 0.2317 0.0280  0.0360  0.0486  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2129 0.2948 0.2249 0.0255  0.0358  0.0548  33   ARG A C   
148   O O   . ARG A 35   ? 0.2420 0.3248 0.2511 0.0257  0.0356  0.0552  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2575 0.3529 0.2674 0.0300  0.0379  0.0486  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2621 0.3584 0.2699 0.0330  0.0379  0.0414  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.3578 0.4679 0.3657 0.0352  0.0398  0.0409  33   ARG A CD  
152   N NE  . ARG A 35   ? 0.4482 0.5585 0.4547 0.0383  0.0395  0.0334  33   ARG A NE  
153   C CZ  . ARG A 35   ? 0.5636 0.6756 0.5665 0.0405  0.0391  0.0283  33   ARG A CZ  
154   N NH1 . ARG A 35   ? 0.6093 0.7235 0.6091 0.0402  0.0392  0.0299  33   ARG A NH1 
155   N NH2 . ARG A 35   ? 0.5458 0.6571 0.5487 0.0432  0.0383  0.0214  33   ARG A NH2 
156   N N   . ALA A 36   ? 0.2193 0.2996 0.2362 0.0232  0.0355  0.0597  34   ALA A N   
157   C CA  . ALA A 36   ? 0.2492 0.3282 0.2689 0.0207  0.0348  0.0657  34   ALA A CA  
158   C C   . ALA A 36   ? 0.2247 0.2928 0.2433 0.0198  0.0330  0.0636  34   ALA A C   
159   O O   . ALA A 36   ? 0.2555 0.3232 0.2743 0.0188  0.0325  0.0666  34   ALA A O   
160   C CB  . ALA A 36   ? 0.2610 0.3402 0.2871 0.0185  0.0346  0.0708  34   ALA A CB  
161   N N   . ILE A 37   ? 0.2101 0.2695 0.2275 0.0202  0.0320  0.0585  35   ILE A N   
162   C CA  . ILE A 37   ? 0.2173 0.2674 0.2331 0.0196  0.0305  0.0559  35   ILE A CA  
163   C C   . ILE A 37   ? 0.2134 0.2657 0.2241 0.0212  0.0308  0.0535  35   ILE A C   
164   O O   . ILE A 37   ? 0.2144 0.2647 0.2247 0.0204  0.0301  0.0552  35   ILE A O   
165   C CB  . ILE A 37   ? 0.2029 0.2448 0.2183 0.0198  0.0294  0.0512  35   ILE A CB  
166   C CG1 . ILE A 37   ? 0.2089 0.2478 0.2295 0.0179  0.0288  0.0537  35   ILE A CG1 
167   C CG2 . ILE A 37   ? 0.2095 0.2431 0.2225 0.0194  0.0280  0.0482  35   ILE A CG2 
168   C CD1 . ILE A 37   ? 0.2084 0.2416 0.2288 0.0183  0.0280  0.0495  35   ILE A CD1 
169   N N   . THR A 38   ? 0.2091 0.2657 0.2163 0.0236  0.0316  0.0493  36   THR A N   
170   C CA  . THR A 38   ? 0.2212 0.2796 0.2238 0.0253  0.0317  0.0463  36   THR A CA  
171   C C   . THR A 38   ? 0.2165 0.2827 0.2187 0.0250  0.0325  0.0509  36   THR A C   
172   O O   . THR A 38   ? 0.2308 0.2955 0.2304 0.0251  0.0320  0.0503  36   THR A O   
173   C CB  . THR A 38   ? 0.2295 0.2922 0.2296 0.0280  0.0324  0.0410  36   THR A CB  
174   O OG1 . THR A 38   ? 0.2308 0.2866 0.2322 0.0281  0.0315  0.0376  36   THR A OG1 
175   C CG2 . THR A 38   ? 0.2387 0.3019 0.2344 0.0297  0.0320  0.0370  36   THR A CG2 
176   N N   . ALA A 39   ? 0.2271 0.3016 0.2320 0.0244  0.0337  0.0558  37   ALA A N   
177   C CA  . ALA A 39   ? 0.2311 0.3142 0.2359 0.0241  0.0345  0.0609  37   ALA A CA  
178   C C   . ALA A 39   ? 0.2617 0.3388 0.2687 0.0218  0.0331  0.0649  37   ALA A C   
179   O O   . ALA A 39   ? 0.2802 0.3621 0.2860 0.0217  0.0332  0.0679  37   ALA A O   
180   C CB  . ALA A 39   ? 0.2449 0.3379 0.2531 0.0236  0.0359  0.0660  37   ALA A CB  
181   N N   . ALA A 40   ? 0.2180 0.2851 0.2283 0.0200  0.0317  0.0650  38   ALA A N   
182   C CA  . ALA A 40   ? 0.2304 0.2918 0.2437 0.0180  0.0302  0.0683  38   ALA A CA  
183   C C   . ALA A 40   ? 0.2329 0.2862 0.2429 0.0184  0.0290  0.0638  38   ALA A C   
184   O O   . ALA A 40   ? 0.2451 0.2935 0.2574 0.0169  0.0277  0.0659  38   ALA A O   
185   C CB  . ALA A 40   ? 0.2355 0.2910 0.2549 0.0159  0.0291  0.0707  38   ALA A CB  
186   N N   . TYR A 41   ? 0.2076 0.2597 0.2127 0.0203  0.0293  0.0578  39   TYR A N   
187   C CA  . TYR A 41   ? 0.2059 0.2495 0.2083 0.0206  0.0281  0.0532  39   TYR A CA  
188   C C   . TYR A 41   ? 0.2335 0.2761 0.2356 0.0198  0.0273  0.0553  39   TYR A C   
189   O O   . TYR A 41   ? 0.2303 0.2651 0.2339 0.0186  0.0259  0.0547  39   TYR A O   
190   C CB  . TYR A 41   ? 0.2305 0.2756 0.2282 0.0229  0.0286  0.0474  39   TYR A CB  
191   C CG  . TYR A 41   ? 0.2151 0.2514 0.2106 0.0232  0.0274  0.0420  39   TYR A CG  
192   C CD1 . TYR A 41   ? 0.2306 0.2596 0.2265 0.0218  0.0261  0.0420  39   TYR A CD1 
193   C CD2 . TYR A 41   ? 0.2280 0.2638 0.2214 0.0249  0.0275  0.0370  39   TYR A CD2 
194   C CE1 . TYR A 41   ? 0.2151 0.2370 0.2090 0.0220  0.0250  0.0374  39   TYR A CE1 
195   C CE2 . TYR A 41   ? 0.2425 0.2709 0.2344 0.0250  0.0262  0.0327  39   TYR A CE2 
196   C CZ  . TYR A 41   ? 0.2217 0.2434 0.2137 0.0235  0.0251  0.0330  39   TYR A CZ  
197   O OH  . TYR A 41   ? 0.2312 0.2463 0.2216 0.0235  0.0239  0.0290  39   TYR A OH  
198   N N   . ARG A 42   ? 0.2383 0.2891 0.2387 0.0206  0.0281  0.0578  40   ARG A N   
199   C CA  . ARG A 42   ? 0.2476 0.2981 0.2476 0.0201  0.0273  0.0599  40   ARG A CA  
200   C C   . ARG A 42   ? 0.2326 0.2911 0.2356 0.0191  0.0278  0.0671  40   ARG A C   
201   O O   . ARG A 42   ? 0.2839 0.3473 0.2852 0.0195  0.0278  0.0692  40   ARG A O   
202   C CB  . ARG A 42   ? 0.2813 0.3328 0.2756 0.0220  0.0275  0.0553  40   ARG A CB  
203   C CG  . ARG A 42   ? 0.2697 0.3121 0.2620 0.0224  0.0265  0.0492  40   ARG A CG  
204   C CD  . ARG A 42   ? 0.2985 0.3424 0.2857 0.0244  0.0266  0.0443  40   ARG A CD  
205   N NE  . ARG A 42   ? 0.2810 0.3180 0.2671 0.0248  0.0260  0.0389  40   ARG A NE  
206   C CZ  . ARG A 42   ? 0.2519 0.2802 0.2382 0.0238  0.0247  0.0369  40   ARG A CZ  
207   N NH1 . ARG A 42   ? 0.2584 0.2836 0.2455 0.0226  0.0239  0.0389  40   ARG A NH1 
208   N NH2 . ARG A 42   ? 0.2507 0.2736 0.2364 0.0241  0.0242  0.0327  40   ARG A NH2 
209   N N   . ARG A 43   ? 0.2436 0.3037 0.2514 0.0178  0.0280  0.0711  41   ARG A N   
210   C CA  . ARG A 43   ? 0.2501 0.3181 0.2618 0.0166  0.0283  0.0786  41   ARG A CA  
211   C C   . ARG A 43   ? 0.2789 0.3436 0.2936 0.0151  0.0266  0.0823  41   ARG A C   
212   O O   . ARG A 43   ? 0.2642 0.3191 0.2812 0.0142  0.0250  0.0806  41   ARG A O   
213   C CB  . ARG A 43   ? 0.2474 0.3150 0.2649 0.0151  0.0283  0.0819  41   ARG A CB  
214   C CG  . ARG A 43   ? 0.2652 0.3406 0.2880 0.0134  0.0283  0.0904  41   ARG A CG  
215   C CD  . ARG A 43   ? 0.2811 0.3578 0.3085 0.0124  0.0288  0.0926  41   ARG A CD  
216   N NE  . ARG A 43   ? 0.2631 0.3464 0.2861 0.0144  0.0308  0.0892  41   ARG A NE  
217   C CZ  . ARG A 43   ? 0.2619 0.3443 0.2866 0.0144  0.0314  0.0877  41   ARG A CZ  
218   N NH1 . ARG A 43   ? 0.2625 0.3379 0.2929 0.0126  0.0301  0.0892  41   ARG A NH1 
219   N NH2 . ARG A 43   ? 0.2888 0.3776 0.3094 0.0165  0.0332  0.0844  41   ARG A NH2 
220   N N   . PRO A 44   ? 0.2848 0.3578 0.2996 0.0150  0.0269  0.0874  42   PRO A N   
221   C CA  . PRO A 44   ? 0.2973 0.3674 0.3157 0.0136  0.0251  0.0915  42   PRO A CA  
222   C C   . PRO A 44   ? 0.2567 0.3196 0.2831 0.0113  0.0233  0.0946  42   PRO A C   
223   O O   . PRO A 44   ? 0.2809 0.3455 0.3115 0.0103  0.0236  0.0974  42   PRO A O   
224   C CB  . PRO A 44   ? 0.2924 0.3748 0.3109 0.0134  0.0258  0.0981  42   PRO A CB  
225   C CG  . PRO A 44   ? 0.3541 0.4450 0.3659 0.0157  0.0281  0.0944  42   PRO A CG  
226   C CD  . PRO A 44   ? 0.3234 0.4094 0.3352 0.0161  0.0287  0.0899  42   PRO A CD  
227   N N   . GLU A 45   ? 0.2646 0.3192 0.2933 0.0106  0.0213  0.0935  43   GLU A N   
228   C CA  . GLU A 45   ? 0.2947 0.3418 0.3312 0.0087  0.0193  0.0952  43   GLU A CA  
229   C C   . GLU A 45   ? 0.2922 0.3444 0.3365 0.0068  0.0185  0.1037  43   GLU A C   
230   O O   . GLU A 45   ? 0.3015 0.3503 0.3523 0.0054  0.0175  0.1053  43   GLU A O   
231   C CB  . GLU A 45   ? 0.3259 0.3647 0.3632 0.0087  0.0174  0.0924  43   GLU A CB  
232   C CG  . GLU A 45   ? 0.3598 0.3888 0.4002 0.0081  0.0161  0.0880  43   GLU A CG  
233   C CD  . GLU A 45   ? 0.2822 0.3037 0.3213 0.0085  0.0147  0.0834  43   GLU A CD  
234   O OE1 . GLU A 45   ? 0.2734 0.2965 0.3067 0.0098  0.0154  0.0813  43   GLU A OE1 
235   O OE2 . GLU A 45   ? 0.2644 0.2790 0.3086 0.0076  0.0130  0.0818  43   GLU A OE2 
236   N N   . THR A 46   ? 0.2989 0.3597 0.3432 0.0066  0.0188  0.1095  44   THR A N   
237   C CA  . THR A 46   ? 0.3434 0.4101 0.3954 0.0046  0.0180  0.1184  44   THR A CA  
238   C C   . THR A 46   ? 0.3457 0.4183 0.3985 0.0043  0.0196  0.1204  44   THR A C   
239   O O   . THR A 46   ? 0.3564 0.4310 0.4172 0.0023  0.0186  0.1267  44   THR A O   
240   C CB  . THR A 46   ? 0.3175 0.3935 0.3685 0.0046  0.0181  0.1243  44   THR A CB  
241   O OG1 . THR A 46   ? 0.3762 0.4602 0.4179 0.0067  0.0207  0.1212  44   THR A OG1 
242   C CG2 . THR A 46   ? 0.3055 0.3754 0.3580 0.0045  0.0160  0.1238  44   THR A CG2 
243   N N   . GLU A 47   ? 0.2825 0.3583 0.3279 0.0062  0.0220  0.1151  45   GLU A N   
244   C CA  . GLU A 47   ? 0.3144 0.3956 0.3604 0.0061  0.0236  0.1162  45   GLU A CA  
245   C C   . GLU A 47   ? 0.3114 0.3830 0.3608 0.0055  0.0228  0.1124  45   GLU A C   
246   O O   . GLU A 47   ? 0.3068 0.3810 0.3608 0.0044  0.0230  0.1155  45   GLU A O   
247   C CB  . GLU A 47   ? 0.3438 0.4328 0.3810 0.0086  0.0263  0.1121  45   GLU A CB  
248   C CG  . GLU A 47   ? 0.4817 0.5812 0.5152 0.0094  0.0272  0.1154  45   GLU A CG  
249   C CD  . GLU A 47   ? 0.4945 0.6026 0.5199 0.0119  0.0297  0.1110  45   GLU A CD  
250   O OE1 . GLU A 47   ? 0.5561 0.6641 0.5802 0.0128  0.0309  0.1072  45   GLU A OE1 
251   O OE2 . GLU A 47   ? 0.6064 0.7215 0.6271 0.0132  0.0303  0.1111  45   GLU A OE2 
252   N N   . CYS A 48   ? 0.2689 0.3301 0.3164 0.0061  0.0217  0.1059  46   CYS A N   
253   C CA  . CYS A 48   ? 0.2822 0.3350 0.3321 0.0057  0.0210  0.1018  46   CYS A CA  
254   C C   . CYS A 48   ? 0.2148 0.2629 0.2747 0.0033  0.0185  0.1061  46   CYS A C   
255   O O   . CYS A 48   ? 0.2664 0.3121 0.3303 0.0025  0.0182  0.1058  46   CYS A O   
256   C CB  . CYS A 48   ? 0.2750 0.3188 0.3199 0.0069  0.0205  0.0940  46   CYS A CB  
257   S SG  . CYS A 48   ? 0.2857 0.3327 0.3199 0.0097  0.0229  0.0876  46   CYS A SG  
258   N N   . LEU A 49   ? 0.2734 0.3198 0.3378 0.0023  0.0166  0.1097  47   LEU A N   
259   C CA  . LEU A 49   ? 0.2794 0.3191 0.3535 0.0004  0.0137  0.1118  47   LEU A CA  
260   C C   . LEU A 49   ? 0.2400 0.2841 0.3229 -0.0017 0.0130  0.1191  47   LEU A C   
261   O O   . LEU A 49   ? 0.2823 0.3205 0.3716 -0.0028 0.0113  0.1183  47   LEU A O   
262   C CB  . LEU A 49   ? 0.2926 0.3282 0.3698 0.0000  0.0115  0.1128  47   LEU A CB  
263   C CG  . LEU A 49   ? 0.2913 0.3168 0.3663 0.0010  0.0104  0.1049  47   LEU A CG  
264   C CD1 . LEU A 49   ? 0.2938 0.3121 0.3746 0.0001  0.0087  0.1021  47   LEU A CD1 
265   C CD2 . LEU A 49   ? 0.2995 0.3251 0.3635 0.0031  0.0127  0.0984  47   LEU A CD2 
266   N N   . PRO A 50   ? 0.3105 0.3649 0.3942 -0.0023 0.0140  0.1263  48   PRO A N   
267   C CA  . PRO A 50   ? 0.2923 0.3508 0.3855 -0.0046 0.0130  0.1341  48   PRO A CA  
268   C C   . PRO A 50   ? 0.3008 0.3576 0.3958 -0.0049 0.0135  0.1318  48   PRO A C   
269   O O   . PRO A 50   ? 0.3120 0.3644 0.4162 -0.0068 0.0112  0.1342  48   PRO A O   
270   C CB  . PRO A 50   ? 0.2997 0.3714 0.3905 -0.0047 0.0149  0.1410  48   PRO A CB  
271   C CG  . PRO A 50   ? 0.3119 0.3839 0.3963 -0.0033 0.0152  0.1389  48   PRO A CG  
272   C CD  . PRO A 50   ? 0.2773 0.3399 0.3548 -0.0013 0.0156  0.1286  48   PRO A CD  
273   N N   . PRO A 51   ? 0.2871 0.3469 0.3739 -0.0032 0.0163  0.1271  49   PRO A N   
274   C CA  . PRO A 51   ? 0.3257 0.3832 0.4148 -0.0036 0.0165  0.1249  49   PRO A CA  
275   C C   . PRO A 51   ? 0.2695 0.3149 0.3613 -0.0037 0.0144  0.1189  49   PRO A C   
276   O O   . PRO A 51   ? 0.3052 0.3478 0.4029 -0.0049 0.0133  0.1192  49   PRO A O   
277   C CB  . PRO A 51   ? 0.3061 0.3694 0.3856 -0.0014 0.0198  0.1208  49   PRO A CB  
278   C CG  . PRO A 51   ? 0.3576 0.4216 0.4292 0.0005  0.0207  0.1176  49   PRO A CG  
279   C CD  . PRO A 51   ? 0.3195 0.3851 0.3956 -0.0009 0.0191  0.1238  49   PRO A CD  
280   N N   . LEU A 52   ? 0.3005 0.3393 0.3882 -0.0026 0.0137  0.1135  50   LEU A N   
281   C CA  . LEU A 52   ? 0.2982 0.3265 0.3885 -0.0027 0.0116  0.1078  50   LEU A CA  
282   C C   . LEU A 52   ? 0.2370 0.2614 0.3388 -0.0048 0.0082  0.1119  50   LEU A C   
283   O O   . LEU A 52   ? 0.2759 0.2948 0.3836 -0.0057 0.0064  0.1100  50   LEU A O   
284   C CB  . LEU A 52   ? 0.2824 0.3056 0.3654 -0.0010 0.0118  0.1013  50   LEU A CB  
285   C CG  . LEU A 52   ? 0.2954 0.3208 0.3675 0.0011  0.0146  0.0963  50   LEU A CG  
286   C CD1 . LEU A 52   ? 0.2702 0.2912 0.3363 0.0025  0.0145  0.0912  50   LEU A CD1 
287   C CD2 . LEU A 52   ? 0.2794 0.3021 0.3500 0.0015  0.0153  0.0918  50   LEU A CD2 
288   N N   . VAL A 53   ? 0.2814 0.3088 0.3870 -0.0056 0.0072  0.1178  51   VAL A N   
289   C CA  . VAL A 53   ? 0.3085 0.3330 0.4262 -0.0077 0.0038  0.1227  51   VAL A CA  
290   C C   . VAL A 53   ? 0.2631 0.2906 0.3885 -0.0095 0.0032  0.1274  51   VAL A C   
291   O O   . VAL A 53   ? 0.2937 0.3152 0.4280 -0.0107 0.0005  0.1268  51   VAL A O   
292   C CB  . VAL A 53   ? 0.2621 0.2910 0.3823 -0.0083 0.0030  0.1292  51   VAL A CB  
293   C CG1 . VAL A 53   ? 0.3181 0.3450 0.4520 -0.0106 -0.0007 0.1355  51   VAL A CG1 
294   C CG2 . VAL A 53   ? 0.2616 0.2862 0.3757 -0.0066 0.0030  0.1241  51   VAL A CG2 
295   N N   . GLU A 54   ? 0.2851 0.3220 0.4073 -0.0096 0.0058  0.1319  52   GLU A N   
296   C CA  . GLU A 54   ? 0.3211 0.3617 0.4502 -0.0114 0.0056  0.1366  52   GLU A CA  
297   C C   . GLU A 54   ? 0.2913 0.3253 0.4208 -0.0110 0.0052  0.1301  52   GLU A C   
298   O O   . GLU A 54   ? 0.3158 0.3463 0.4550 -0.0127 0.0027  0.1317  52   GLU A O   
299   C CB  . GLU A 54   ? 0.3558 0.4085 0.4799 -0.0111 0.0089  0.1414  52   GLU A CB  
300   N N   . ALA A 55   ? 0.2809 0.3128 0.4002 -0.0089 0.0073  0.1225  53   ALA A N   
301   C CA  . ALA A 55   ? 0.3082 0.3349 0.4271 -0.0085 0.0072  0.1166  53   ALA A CA  
302   C C   . ALA A 55   ? 0.2520 0.2686 0.3766 -0.0090 0.0039  0.1121  53   ALA A C   
303   O O   . ALA A 55   ? 0.2928 0.3056 0.4215 -0.0095 0.0027  0.1094  53   ALA A O   
304   C CB  . ALA A 55   ? 0.3095 0.3367 0.4164 -0.0062 0.0101  0.1101  53   ALA A CB  
305   N N   . ALA A 56   ? 0.2549 0.2677 0.3800 -0.0087 0.0024  0.1111  54   ALA A N   
306   C CA  . ALA A 56   ? 0.2937 0.2975 0.4237 -0.0087 -0.0006 0.1061  54   ALA A CA  
307   C C   . ALA A 56   ? 0.3426 0.3445 0.4863 -0.0108 -0.0043 0.1110  54   ALA A C   
308   O O   . ALA A 56   ? 0.2933 0.2881 0.4426 -0.0109 -0.0072 0.1068  54   ALA A O   
309   C CB  . ALA A 56   ? 0.2587 0.2593 0.3822 -0.0072 -0.0004 0.1016  54   ALA A CB  
310   N N   . THR A 57   ? 0.3257 0.3339 0.4751 -0.0124 -0.0044 0.1197  55   THR A N   
311   C CA  . THR A 57   ? 0.3227 0.3292 0.4858 -0.0146 -0.0081 0.1252  55   THR A CA  
312   C C   . THR A 57   ? 0.2966 0.2987 0.4680 -0.0156 -0.0104 0.1229  55   THR A C   
313   O O   . THR A 57   ? 0.3298 0.3344 0.4982 -0.0156 -0.0086 0.1220  55   THR A O   
314   C CB  . THR A 57   ? 0.3367 0.3523 0.5034 -0.0162 -0.0073 0.1357  55   THR A CB  
315   O OG1 . THR A 57   ? 0.3430 0.3628 0.5026 -0.0152 -0.0056 0.1377  55   THR A OG1 
316   C CG2 . THR A 57   ? 0.3948 0.4110 0.5750 -0.0181 -0.0115 0.1393  55   THR A CG2 
317   N N   . GLN A 58   ? 0.3055 0.3010 0.4874 -0.0164 -0.0145 0.1217  56   GLN A N   
318   C CA  . GLN A 58   ? 0.2858 0.2772 0.4772 -0.0175 -0.0173 0.1197  56   GLN A CA  
319   C C   . GLN A 58   ? 0.2798 0.2726 0.4840 -0.0190 -0.0214 0.1230  56   GLN A C   
320   O O   . GLN A 58   ? 0.3290 0.3237 0.5351 -0.0190 -0.0224 0.1259  56   GLN A O   
321   C CB  . GLN A 58   ? 0.3155 0.2993 0.5042 -0.0158 -0.0184 0.1091  56   GLN A CB  
322   C CG  . GLN A 58   ? 0.2998 0.2845 0.4739 -0.0138 -0.0146 0.1029  56   GLN A CG  
323   C CD  . GLN A 58   ? 0.2739 0.2524 0.4463 -0.0126 -0.0158 0.0934  56   GLN A CD  
324   O OE1 . GLN A 58   ? 0.3129 0.2904 0.4886 -0.0132 -0.0166 0.0914  56   GLN A OE1 
325   N NE2 . GLN A 58   ? 0.3090 0.2838 0.4764 -0.0111 -0.0159 0.0876  56   GLN A NE2 
326   N N   . SER A 59   ? 0.3027 0.2946 0.5159 -0.0201 -0.0239 0.1224  57   SER A N   
327   C CA  . SER A 59   ? 0.2926 0.2862 0.5189 -0.0215 -0.0280 0.1256  57   SER A CA  
328   C C   . SER A 59   ? 0.3529 0.3403 0.5846 -0.0208 -0.0315 0.1210  57   SER A C   
329   O O   . SER A 59   ? 0.3050 0.2858 0.5322 -0.0193 -0.0314 0.1139  57   SER A O   
330   C CB  . SER A 59   ? 0.3289 0.3215 0.5636 -0.0226 -0.0302 0.1244  57   SER A CB  
331   O OG  . SER A 59   ? 0.3368 0.3211 0.5728 -0.0216 -0.0321 0.1157  57   SER A OG  
332   N N   . LYS A 60   ? 0.3427 0.3329 0.5847 -0.0219 -0.0347 0.1253  58   LYS A N   
333   C CA  . LYS A 60   ? 0.3345 0.3194 0.5834 -0.0214 -0.0384 0.1212  58   LYS A CA  
334   C C   . LYS A 60   ? 0.3489 0.3265 0.6029 -0.0206 -0.0412 0.1125  58   LYS A C   
335   O O   . LYS A 60   ? 0.3762 0.3480 0.6294 -0.0191 -0.0424 0.1059  58   LYS A O   
336   C CB  . LYS A 60   ? 0.3474 0.3369 0.6083 -0.0229 -0.0418 0.1276  58   LYS A CB  
337   C CG  . LYS A 60   ? 0.3599 0.3447 0.6289 -0.0224 -0.0458 0.1239  58   LYS A CG  
338   C CD  . LYS A 60   ? 0.4358 0.4183 0.6953 -0.0208 -0.0437 0.1215  58   LYS A CD  
339   C CE  . LYS A 60   ? 0.4785 0.4591 0.7464 -0.0207 -0.0474 0.1210  58   LYS A CE  
340   N NZ  . LYS A 60   ? 0.4900 0.4641 0.7670 -0.0199 -0.0516 0.1130  58   LYS A NZ  
341   N N   . GLU A 61   ? 0.3482 0.3263 0.6075 -0.0215 -0.0422 0.1124  59   GLU A N   
342   C CA  . GLU A 61   ? 0.3518 0.3237 0.6160 -0.0208 -0.0449 0.1040  59   GLU A CA  
343   C C   . GLU A 61   ? 0.3411 0.3078 0.5939 -0.0190 -0.0422 0.0968  59   GLU A C   
344   O O   . GLU A 61   ? 0.3861 0.3472 0.6408 -0.0176 -0.0443 0.0888  59   GLU A O   
345   C CB  . GLU A 61   ? 0.3819 0.3559 0.6529 -0.0221 -0.0462 0.1057  59   GLU A CB  
346   N N   . ILE A 62   ? 0.3422 0.3114 0.5835 -0.0188 -0.0376 0.0994  60   ILE A N   
347   C CA  . ILE A 62   ? 0.3158 0.2805 0.5462 -0.0171 -0.0350 0.0933  60   ILE A CA  
348   C C   . ILE A 62   ? 0.3456 0.3071 0.5716 -0.0156 -0.0348 0.0902  60   ILE A C   
349   O O   . ILE A 62   ? 0.3211 0.2771 0.5446 -0.0140 -0.0354 0.0824  60   ILE A O   
350   C CB  . ILE A 62   ? 0.3255 0.2940 0.5454 -0.0174 -0.0302 0.0972  60   ILE A CB  
351   C CG1 . ILE A 62   ? 0.3646 0.3341 0.5879 -0.0184 -0.0305 0.0971  60   ILE A CG1 
352   C CG2 . ILE A 62   ? 0.3311 0.2981 0.5367 -0.0152 -0.0270 0.0908  60   ILE A CG2 
353   C CD1 . ILE A 62   ? 0.4133 0.3874 0.6263 -0.0184 -0.0261 0.0998  60   ILE A CD1 
354   N N   . ARG A 63   ? 0.3030 0.2684 0.5279 -0.0159 -0.0340 0.0962  61   ARG A N   
355   C CA  . ARG A 63   ? 0.3357 0.2984 0.5565 -0.0145 -0.0339 0.0938  61   ARG A CA  
356   C C   . ARG A 63   ? 0.3413 0.2990 0.5713 -0.0137 -0.0383 0.0873  61   ARG A C   
357   O O   . ARG A 63   ? 0.3395 0.2927 0.5655 -0.0120 -0.0383 0.0811  61   ARG A O   
358   C CB  . ARG A 63   ? 0.3506 0.3192 0.5698 -0.0152 -0.0326 0.1018  61   ARG A CB  
359   C CG  . ARG A 63   ? 0.4352 0.4088 0.6431 -0.0153 -0.0278 0.1067  61   ARG A CG  
360   C CD  . ARG A 63   ? 0.4919 0.4717 0.6969 -0.0157 -0.0263 0.1138  61   ARG A CD  
361   N NE  . ARG A 63   ? 0.4826 0.4686 0.6966 -0.0177 -0.0281 0.1209  61   ARG A NE  
362   C CZ  . ARG A 63   ? 0.5100 0.4968 0.7333 -0.0184 -0.0314 0.1233  61   ARG A CZ  
363   N NH1 . ARG A 63   ? 0.5014 0.4834 0.7263 -0.0174 -0.0333 0.1193  61   ARG A NH1 
364   N NH2 . ARG A 63   ? 0.4902 0.4833 0.7217 -0.0203 -0.0329 0.1302  61   ARG A NH2 
365   N N   . ASP A 64   ? 0.3856 0.3444 0.6283 -0.0150 -0.0421 0.0885  62   ASP A N   
366   C CA  . ASP A 64   ? 0.3513 0.3058 0.6035 -0.0142 -0.0465 0.0818  62   ASP A CA  
367   C C   . ASP A 64   ? 0.3547 0.3044 0.6052 -0.0128 -0.0470 0.0724  62   ASP A C   
368   O O   . ASP A 64   ? 0.3488 0.2944 0.6000 -0.0111 -0.0487 0.0649  62   ASP A O   
369   C CB  . ASP A 64   ? 0.3593 0.3165 0.6259 -0.0158 -0.0507 0.0856  62   ASP A CB  
370   C CG  . ASP A 64   ? 0.3663 0.3281 0.6361 -0.0170 -0.0510 0.0940  62   ASP A CG  
371   O OD1 . ASP A 64   ? 0.3972 0.3598 0.6585 -0.0164 -0.0484 0.0960  62   ASP A OD1 
372   O OD2 . ASP A 64   ? 0.4860 0.4511 0.7673 -0.0186 -0.0540 0.0986  62   ASP A OD2 
373   N N   . ALA A 65   ? 0.3052 0.2555 0.5534 -0.0135 -0.0456 0.0727  63   ALA A N   
374   C CA  . ALA A 65   ? 0.3110 0.2573 0.5571 -0.0123 -0.0460 0.0640  63   ALA A CA  
375   C C   . ALA A 65   ? 0.3672 0.3110 0.6006 -0.0105 -0.0427 0.0596  63   ALA A C   
376   O O   . ALA A 65   ? 0.3363 0.2779 0.5676 -0.0088 -0.0435 0.0505  63   ALA A O   
377   C CB  . ALA A 65   ? 0.3444 0.2924 0.5907 -0.0136 -0.0451 0.0659  63   ALA A CB  
378   N N   . ALA A 66   ? 0.3230 0.2705 0.5454 -0.0106 -0.0385 0.0648  64   ALA A N   
379   C CA  . ALA A 66   ? 0.3291 0.2776 0.5368 -0.0087 -0.0349 0.0600  64   ALA A CA  
380   C C   . ALA A 66   ? 0.3382 0.2838 0.5476 -0.0073 -0.0366 0.0557  64   ALA A C   
381   O O   . ALA A 66   ? 0.3092 0.2537 0.5118 -0.0055 -0.0359 0.0477  64   ALA A O   
382   C CB  . ALA A 66   ? 0.3382 0.2914 0.5355 -0.0091 -0.0305 0.0667  64   ALA A CB  
383   N N   . ALA A 67   ? 0.2994 0.2438 0.5179 -0.0080 -0.0390 0.0610  65   ALA A N   
384   C CA  . ALA A 67   ? 0.3367 0.2784 0.5579 -0.0066 -0.0410 0.0572  65   ALA A CA  
385   C C   . ALA A 67   ? 0.3301 0.2679 0.5590 -0.0054 -0.0447 0.0479  65   ALA A C   
386   O O   . ALA A 67   ? 0.3500 0.2867 0.5750 -0.0036 -0.0447 0.0408  65   ALA A O   
387   C CB  . ALA A 67   ? 0.3398 0.2830 0.5693 -0.0078 -0.0429 0.0646  65   ALA A CB  
388   N N   . SER A 68   ? 0.3292 0.2665 0.5681 -0.0065 -0.0476 0.0474  66   SER A N   
389   C CA  . SER A 68   ? 0.3587 0.2937 0.6046 -0.0053 -0.0511 0.0380  66   SER A CA  
390   C C   . SER A 68   ? 0.3755 0.3105 0.6108 -0.0037 -0.0488 0.0299  66   SER A C   
391   O O   . SER A 68   ? 0.3535 0.2876 0.5882 -0.0019 -0.0500 0.0213  66   SER A O   
392   C CB  . SER A 68   ? 0.4012 0.3377 0.6587 -0.0068 -0.0544 0.0393  66   SER A CB  
393   O OG  . SER A 68   ? 0.4722 0.4071 0.7357 -0.0055 -0.0577 0.0298  66   SER A OG  
394   N N   . THR A 69   ? 0.3465 0.2845 0.5721 -0.0045 -0.0452 0.0323  67   THR A N   
395   C CA  . THR A 69   ? 0.2988 0.2387 0.5124 -0.0032 -0.0425 0.0252  67   THR A CA  
396   C C   . THR A 69   ? 0.3034 0.2443 0.5060 -0.0016 -0.0399 0.0222  67   THR A C   
397   O O   . THR A 69   ? 0.3025 0.2438 0.5008 0.0000  -0.0399 0.0139  67   THR A O   
398   C CB  . THR A 69   ? 0.2997 0.2425 0.5053 -0.0043 -0.0391 0.0293  67   THR A CB  
399   O OG1 . THR A 69   ? 0.3149 0.2570 0.5307 -0.0057 -0.0417 0.0307  67   THR A OG1 
400   C CG2 . THR A 69   ? 0.3187 0.2637 0.5114 -0.0031 -0.0362 0.0229  67   THR A CG2 
401   N N   . ALA A 70   ? 0.3059 0.2476 0.5039 -0.0020 -0.0376 0.0288  68   ALA A N   
402   C CA  . ALA A 70   ? 0.3134 0.2559 0.5013 -0.0006 -0.0352 0.0264  68   ALA A CA  
403   C C   . ALA A 70   ? 0.3381 0.2783 0.5327 0.0009  -0.0384 0.0202  68   ALA A C   
404   O O   . ALA A 70   ? 0.3229 0.2640 0.5103 0.0025  -0.0372 0.0135  68   ALA A O   
405   C CB  . ALA A 70   ? 0.3135 0.2575 0.4967 -0.0013 -0.0327 0.0348  68   ALA A CB  
406   N N   . ARG A 71   ? 0.3211 0.2584 0.5298 0.0004  -0.0425 0.0222  69   ARG A N   
407   C CA  . ARG A 71   ? 0.3327 0.2677 0.5492 0.0020  -0.0459 0.0159  69   ARG A CA  
408   C C   . ARG A 71   ? 0.3512 0.2867 0.5680 0.0033  -0.0473 0.0056  69   ARG A C   
409   O O   . ARG A 71   ? 0.3354 0.2717 0.5487 0.0052  -0.0472 -0.0015 69   ARG A O   
410   C CB  . ARG A 71   ? 0.3687 0.3004 0.6018 0.0010  -0.0505 0.0203  69   ARG A CB  
411   C CG  . ARG A 71   ? 0.3936 0.3229 0.6374 0.0027  -0.0549 0.0127  69   ARG A CG  
412   C CD  . ARG A 71   ? 0.3910 0.3216 0.6470 0.0014  -0.0585 0.0173  69   ARG A CD  
413   N NE  . ARG A 71   ? 0.4177 0.3488 0.6713 0.0009  -0.0572 0.0243  69   ARG A NE  
414   C CZ  . ARG A 71   ? 0.4133 0.3437 0.6656 0.0025  -0.0575 0.0212  69   ARG A CZ  
415   N NH1 . ARG A 71   ? 0.4205 0.3499 0.6733 0.0047  -0.0588 0.0112  69   ARG A NH1 
416   N NH2 . ARG A 71   ? 0.4009 0.3320 0.6509 0.0019  -0.0563 0.0282  69   ARG A NH2 
417   N N   . LYS A 72   ? 0.3306 0.2662 0.5513 0.0025  -0.0484 0.0047  70   LYS A N   
418   C CA  . LYS A 72   ? 0.3487 0.2857 0.5693 0.0037  -0.0496 -0.0049 70   LYS A CA  
419   C C   . LYS A 72   ? 0.3911 0.3318 0.5961 0.0048  -0.0456 -0.0094 70   LYS A C   
420   O O   . LYS A 72   ? 0.3490 0.2913 0.5526 0.0066  -0.0464 -0.0179 70   LYS A O   
421   C CB  . LYS A 72   ? 0.3347 0.2716 0.5605 0.0024  -0.0509 -0.0039 70   LYS A CB  
422   C CG  . LYS A 72   ? 0.4080 0.3467 0.6347 0.0035  -0.0525 -0.0135 70   LYS A CG  
423   C CD  . LYS A 72   ? 0.4541 0.3922 0.6879 0.0020  -0.0543 -0.0118 70   LYS A CD  
424   C CE  . LYS A 72   ? 0.5636 0.5026 0.8041 0.0032  -0.0578 -0.0216 70   LYS A CE  
425   N NZ  . LYS A 72   ? 0.6290 0.5726 0.8567 0.0042  -0.0550 -0.0275 70   LYS A NZ  
426   N N   . LEU A 73   ? 0.3463 0.2887 0.5396 0.0039  -0.0413 -0.0038 71   LEU A N   
427   C CA  . LEU A 73   ? 0.3461 0.2918 0.5248 0.0047  -0.0375 -0.0071 71   LEU A CA  
428   C C   . LEU A 73   ? 0.3347 0.2807 0.5101 0.0062  -0.0370 -0.0099 71   LEU A C   
429   O O   . LEU A 73   ? 0.3425 0.2911 0.5117 0.0075  -0.0362 -0.0167 71   LEU A O   
430   C CB  . LEU A 73   ? 0.3292 0.2761 0.4976 0.0035  -0.0334 0.0000  71   LEU A CB  
431   C CG  . LEU A 73   ? 0.3298 0.2774 0.4993 0.0022  -0.0331 0.0027  71   LEU A CG  
432   C CD1 . LEU A 73   ? 0.2851 0.2341 0.4453 0.0012  -0.0291 0.0100  71   LEU A CD1 
433   C CD2 . LEU A 73   ? 0.3684 0.3183 0.5346 0.0028  -0.0333 -0.0047 71   LEU A CD2 
434   N N   . ILE A 74   ? 0.3167 0.2604 0.4960 0.0059  -0.0375 -0.0045 72   ILE A N   
435   C CA  . ILE A 74   ? 0.3299 0.2738 0.5061 0.0072  -0.0369 -0.0066 72   ILE A CA  
436   C C   . ILE A 74   ? 0.3751 0.3185 0.5599 0.0089  -0.0406 -0.0150 72   ILE A C   
437   O O   . ILE A 74   ? 0.3702 0.3157 0.5498 0.0104  -0.0398 -0.0206 72   ILE A O   
438   C CB  . ILE A 74   ? 0.3126 0.2544 0.4910 0.0064  -0.0366 0.0018  72   ILE A CB  
439   C CG1 . ILE A 74   ? 0.3468 0.2905 0.5137 0.0053  -0.0323 0.0085  72   ILE A CG1 
440   C CG2 . ILE A 74   ? 0.3283 0.2697 0.5068 0.0078  -0.0371 -0.0006 72   ILE A CG2 
441   C CD1 . ILE A 74   ? 0.3256 0.2684 0.4955 0.0041  -0.0320 0.0177  72   ILE A CD1 
442   N N   . GLU A 75   ? 0.3600 0.3011 0.5585 0.0087  -0.0448 -0.0163 73   GLU A N   
443   C CA  . GLU A 75   ? 0.3570 0.2979 0.5646 0.0105  -0.0486 -0.0251 73   GLU A CA  
444   C C   . GLU A 75   ? 0.4159 0.3613 0.6165 0.0117  -0.0476 -0.0339 73   GLU A C   
445   O O   . GLU A 75   ? 0.3842 0.3320 0.5840 0.0135  -0.0483 -0.0413 73   GLU A O   
446   C CB  . GLU A 75   ? 0.3878 0.3251 0.6121 0.0100  -0.0536 -0.0245 73   GLU A CB  
447   C CG  . GLU A 75   ? 0.4179 0.3514 0.6515 0.0094  -0.0556 -0.0179 73   GLU A CG  
448   C CD  . GLU A 75   ? 0.4913 0.4213 0.7404 0.0081  -0.0599 -0.0141 73   GLU A CD  
449   O OE1 . GLU A 75   ? 0.5017 0.4322 0.7539 0.0074  -0.0610 -0.0158 73   GLU A OE1 
450   O OE2 . GLU A 75   ? 0.5167 0.4466 0.7723 0.0074  -0.0616 -0.0089 73   GLU A OE2 
451   N N   . ALA A 76   ? 0.3990 0.3461 0.5942 0.0106  -0.0460 -0.0331 74   ALA A N   
452   C CA  . ALA A 76   ? 0.3880 0.3400 0.5753 0.0115  -0.0447 -0.0404 74   ALA A CA  
453   C C   . ALA A 76   ? 0.4106 0.3659 0.5843 0.0122  -0.0408 -0.0412 74   ALA A C   
454   O O   . ALA A 76   ? 0.4209 0.3806 0.5913 0.0136  -0.0408 -0.0487 74   ALA A O   
455   C CB  . ALA A 76   ? 0.4114 0.3643 0.5954 0.0101  -0.0435 -0.0381 74   ALA A CB  
456   N N   . LEU A 77   ? 0.3911 0.3451 0.5573 0.0111  -0.0376 -0.0335 75   LEU A N   
457   C CA  . LEU A 77   ? 0.3665 0.3232 0.5203 0.0116  -0.0340 -0.0338 75   LEU A CA  
458   C C   . LEU A 77   ? 0.4599 0.4172 0.6167 0.0133  -0.0354 -0.0387 75   LEU A C   
459   O O   . LEU A 77   ? 0.4833 0.4451 0.6343 0.0144  -0.0344 -0.0447 75   LEU A O   
460   C CB  . LEU A 77   ? 0.3797 0.3344 0.5267 0.0103  -0.0309 -0.0248 75   LEU A CB  
461   C CG  . LEU A 77   ? 0.3870 0.3429 0.5250 0.0090  -0.0279 -0.0207 75   LEU A CG  
462   C CD1 . LEU A 77   ? 0.3703 0.3246 0.5028 0.0080  -0.0251 -0.0125 75   LEU A CD1 
463   C CD2 . LEU A 77   ? 0.3934 0.3538 0.5214 0.0095  -0.0258 -0.0258 75   LEU A CD2 
464   N N   . ARG A 78   ? 0.3753 0.3287 0.5415 0.0135  -0.0378 -0.0360 76   ARG A N   
465   C CA  . ARG A 78   ? 0.3922 0.3460 0.5622 0.0152  -0.0393 -0.0403 76   ARG A CA  
466   C C   . ARG A 78   ? 0.4268 0.3831 0.6042 0.0169  -0.0425 -0.0503 76   ARG A C   
467   O O   . ARG A 78   ? 0.4819 0.4407 0.6592 0.0186  -0.0429 -0.0559 76   ARG A O   
468   C CB  . ARG A 78   ? 0.3879 0.3367 0.5670 0.0148  -0.0413 -0.0344 76   ARG A CB  
469   C CG  . ARG A 78   ? 0.3919 0.3396 0.5625 0.0135  -0.0378 -0.0256 76   ARG A CG  
470   C CD  . ARG A 78   ? 0.3713 0.3152 0.5503 0.0133  -0.0398 -0.0199 76   ARG A CD  
471   N NE  . ARG A 78   ? 0.3661 0.3104 0.5354 0.0128  -0.0364 -0.0141 76   ARG A NE  
472   C CZ  . ARG A 78   ? 0.3688 0.3109 0.5422 0.0124  -0.0371 -0.0081 76   ARG A CZ  
473   N NH1 . ARG A 78   ? 0.3879 0.3267 0.5750 0.0123  -0.0411 -0.0062 76   ARG A NH1 
474   N NH2 . ARG A 78   ? 0.3916 0.3347 0.5553 0.0122  -0.0339 -0.0038 76   ARG A NH2 
475   N N   . GLY A 79   ? 0.4205 0.3768 0.6045 0.0167  -0.0448 -0.0530 77   GLY A N   
476   C CA  . GLY A 79   ? 0.5112 0.4704 0.7028 0.0185  -0.0482 -0.0630 77   GLY A CA  
477   C C   . GLY A 79   ? 0.5380 0.5044 0.7197 0.0194  -0.0461 -0.0700 77   GLY A C   
478   O O   . GLY A 79   ? 0.5825 0.5528 0.7687 0.0213  -0.0483 -0.0790 77   GLY A O   
479   N N   . LYS A 80   ? 0.5087 0.4773 0.6772 0.0181  -0.0420 -0.0660 78   LYS A N   
480   C CA  . LYS A 80   ? 0.5609 0.5366 0.7197 0.0187  -0.0399 -0.0715 78   LYS A CA  
481   C C   . LYS A 80   ? 0.5520 0.5304 0.6990 0.0186  -0.0362 -0.0696 78   LYS A C   
482   O O   . LYS A 80   ? 0.6101 0.5948 0.7486 0.0189  -0.0343 -0.0734 78   LYS A O   
483   C CB  . LYS A 80   ? 0.5403 0.5174 0.6942 0.0172  -0.0387 -0.0696 78   LYS A CB  
484   C CG  . LYS A 80   ? 0.5557 0.5288 0.7029 0.0152  -0.0357 -0.0597 78   LYS A CG  
485   C CD  . LYS A 80   ? 0.4934 0.4673 0.6381 0.0139  -0.0352 -0.0584 78   LYS A CD  
486   C CE  . LYS A 80   ? 0.4882 0.4584 0.6275 0.0121  -0.0325 -0.0489 78   LYS A CE  
487   N NZ  . LYS A 80   ? 0.3654 0.3365 0.5030 0.0109  -0.0321 -0.0477 78   LYS A NZ  
488   N N   . HIS A 81   ? 0.5485 0.5225 0.6949 0.0183  -0.0352 -0.0638 79   HIS A N   
489   C CA  . HIS A 81   ? 0.6044 0.5804 0.7400 0.0181  -0.0317 -0.0614 79   HIS A CA  
490   C C   . HIS A 81   ? 0.6443 0.6264 0.7783 0.0199  -0.0319 -0.0693 79   HIS A C   
491   O O   . HIS A 81   ? 0.7390 0.7222 0.8824 0.0216  -0.0351 -0.0759 79   HIS A O   
492   C CB  . HIS A 81   ? 0.6104 0.5808 0.7479 0.0177  -0.0314 -0.0545 79   HIS A CB  
493   N N   . SER A 84   ? 0.6416 0.6399 0.7177 0.0169  -0.0146 -0.0582 82   SER A N   
494   C CA  . SER A 84   ? 0.6070 0.6102 0.6889 0.0187  -0.0166 -0.0661 82   SER A CA  
495   C C   . SER A 84   ? 0.5638 0.5760 0.6387 0.0187  -0.0151 -0.0700 82   SER A C   
496   O O   . SER A 84   ? 0.5172 0.5344 0.5945 0.0201  -0.0159 -0.0758 82   SER A O   
497   C CB  . SER A 84   ? 0.5911 0.5940 0.6820 0.0195  -0.0196 -0.0705 82   SER A CB  
498   N N   . GLY A 85   ? 0.5303 0.5448 0.5967 0.0171  -0.0129 -0.0668 83   GLY A N   
499   C CA  . GLY A 85   ? 0.4455 0.4687 0.5048 0.0167  -0.0113 -0.0693 83   GLY A CA  
500   C C   . GLY A 85   ? 0.3457 0.3701 0.4011 0.0168  -0.0097 -0.0679 83   GLY A C   
501   O O   . GLY A 85   ? 0.3835 0.4147 0.4392 0.0178  -0.0099 -0.0730 83   GLY A O   
502   N N   . VAL A 86   ? 0.3872 0.4053 0.4389 0.0157  -0.0082 -0.0611 84   VAL A N   
503   C CA  . VAL A 86   ? 0.3722 0.3905 0.4206 0.0157  -0.0068 -0.0595 84   VAL A CA  
504   C C   . VAL A 86   ? 0.4063 0.4235 0.4625 0.0177  -0.0087 -0.0635 84   VAL A C   
505   O O   . VAL A 86   ? 0.3074 0.3292 0.3630 0.0184  -0.0084 -0.0665 84   VAL A O   
506   C CB  . VAL A 86   ? 0.4090 0.4206 0.4525 0.0143  -0.0051 -0.0518 84   VAL A CB  
507   C CG1 . VAL A 86   ? 0.4251 0.4352 0.4676 0.0147  -0.0044 -0.0503 84   VAL A CG1 
508   C CG2 . VAL A 86   ? 0.4257 0.4400 0.4609 0.0125  -0.0031 -0.0485 84   VAL A CG2 
509   N N   . GLU A 87   ? 0.3811 0.3923 0.4452 0.0185  -0.0108 -0.0635 85   GLU A N   
510   C CA  . GLU A 87   ? 0.3999 0.4096 0.4727 0.0203  -0.0131 -0.0672 85   GLU A CA  
511   C C   . GLU A 87   ? 0.3906 0.4084 0.4669 0.0219  -0.0144 -0.0759 85   GLU A C   
512   O O   . GLU A 87   ? 0.4032 0.4234 0.4823 0.0233  -0.0150 -0.0793 85   GLU A O   
513   C CB  . GLU A 87   ? 0.4943 0.4968 0.5758 0.0207  -0.0154 -0.0656 85   GLU A CB  
514   N N   . GLY A 88   ? 0.3634 0.3861 0.4396 0.0219  -0.0150 -0.0796 86   GLY A N   
515   C CA  . GLY A 88   ? 0.3613 0.3930 0.4405 0.0236  -0.0162 -0.0882 86   GLY A CA  
516   C C   . GLY A 88   ? 0.3346 0.3743 0.4066 0.0234  -0.0140 -0.0895 86   GLY A C   
517   O O   . GLY A 88   ? 0.3617 0.4075 0.4371 0.0251  -0.0149 -0.0957 86   GLY A O   
518   N N   . LEU A 89   ? 0.3389 0.3788 0.4013 0.0213  -0.0112 -0.0834 87   LEU A N   
519   C CA  . LEU A 89   ? 0.3342 0.3815 0.3898 0.0207  -0.0091 -0.0835 87   LEU A CA  
520   C C   . LEU A 89   ? 0.2987 0.3434 0.3562 0.0215  -0.0090 -0.0829 87   LEU A C   
521   O O   . LEU A 89   ? 0.2782 0.3299 0.3362 0.0226  -0.0090 -0.0875 87   LEU A O   
522   C CB  . LEU A 89   ? 0.3705 0.4175 0.4166 0.0182  -0.0066 -0.0766 87   LEU A CB  
523   C CG  . LEU A 89   ? 0.4102 0.4668 0.4486 0.0170  -0.0046 -0.0765 87   LEU A CG  
524   C CD1 . LEU A 89   ? 0.4136 0.4678 0.4445 0.0145  -0.0027 -0.0693 87   LEU A CD1 
525   C CD2 . LEU A 89   ? 0.4472 0.5066 0.4845 0.0174  -0.0037 -0.0769 87   LEU A CD2 
526   N N   . VAL A 90   ? 0.2781 0.3129 0.3367 0.0211  -0.0090 -0.0772 88   VAL A N   
527   C CA  . VAL A 90   ? 0.2914 0.3230 0.3523 0.0219  -0.0091 -0.0763 88   VAL A CA  
528   C C   . VAL A 90   ? 0.3266 0.3610 0.3968 0.0245  -0.0117 -0.0838 88   VAL A C   
529   O O   . VAL A 90   ? 0.2909 0.3290 0.3618 0.0254  -0.0115 -0.0863 88   VAL A O   
530   C CB  . VAL A 90   ? 0.2734 0.2945 0.3352 0.0212  -0.0092 -0.0694 88   VAL A CB  
531   C CG1 . VAL A 90   ? 0.3443 0.3617 0.4106 0.0224  -0.0101 -0.0691 88   VAL A CG1 
532   C CG2 . VAL A 90   ? 0.3189 0.3381 0.3713 0.0190  -0.0065 -0.0625 88   VAL A CG2 
533   N N   . GLN A 91   ? 0.3424 0.3751 0.4203 0.0256  -0.0142 -0.0875 89   GLN A N   
534   C CA  . GLN A 91   ? 0.3231 0.3579 0.4110 0.0281  -0.0171 -0.0951 89   GLN A CA  
535   C C   . GLN A 91   ? 0.3501 0.3969 0.4365 0.0293  -0.0167 -0.1026 89   GLN A C   
536   O O   . GLN A 91   ? 0.3563 0.4067 0.4465 0.0310  -0.0175 -0.1071 89   GLN A O   
537   C CB  . GLN A 91   ? 0.3610 0.3915 0.4576 0.0289  -0.0200 -0.0973 89   GLN A CB  
538   N N   . GLU A 92   ? 0.3286 0.3821 0.4095 0.0284  -0.0156 -0.1040 90   GLU A N   
539   C CA  . GLU A 92   ? 0.3139 0.3800 0.3939 0.0295  -0.0155 -0.1115 90   GLU A CA  
540   C C   . GLU A 92   ? 0.3277 0.3997 0.4023 0.0293  -0.0133 -0.1109 90   GLU A C   
541   O O   . GLU A 92   ? 0.3105 0.3908 0.3883 0.0312  -0.0140 -0.1178 90   GLU A O   
542   C CB  . GLU A 92   ? 0.3205 0.3927 0.3945 0.0281  -0.0144 -0.1115 90   GLU A CB  
543   C CG  . GLU A 92   ? 0.3421 0.4287 0.4132 0.0288  -0.0138 -0.1179 90   GLU A CG  
544   C CD  . GLU A 92   ? 0.4410 0.5337 0.5068 0.0275  -0.0130 -0.1179 90   GLU A CD  
545   O OE1 . GLU A 92   ? 0.4726 0.5579 0.5365 0.0259  -0.0129 -0.1125 90   GLU A OE1 
546   O OE2 . GLU A 92   ? 0.4443 0.5496 0.5078 0.0280  -0.0127 -0.1231 90   GLU A OE2 
547   N N   . TYR A 93   ? 0.2815 0.3495 0.3484 0.0271  -0.0109 -0.1029 91   TYR A N   
548   C CA  . TYR A 93   ? 0.3010 0.3744 0.3625 0.0265  -0.0088 -0.1015 91   TYR A CA  
549   C C   . TYR A 93   ? 0.2601 0.3259 0.3242 0.0270  -0.0090 -0.0985 91   TYR A C   
550   O O   . TYR A 93   ? 0.2723 0.3407 0.3316 0.0262  -0.0072 -0.0961 91   TYR A O   
551   C CB  . TYR A 93   ? 0.2812 0.3571 0.3321 0.0236  -0.0059 -0.0953 91   TYR A CB  
552   C CG  . TYR A 93   ? 0.2758 0.3620 0.3239 0.0232  -0.0056 -0.0988 91   TYR A CG  
553   C CD1 . TYR A 93   ? 0.2602 0.3594 0.3062 0.0237  -0.0049 -0.1035 91   TYR A CD1 
554   C CD2 . TYR A 93   ? 0.2730 0.3564 0.3207 0.0225  -0.0062 -0.0975 91   TYR A CD2 
555   C CE1 . TYR A 93   ? 0.2981 0.4076 0.3415 0.0234  -0.0046 -0.1067 91   TYR A CE1 
556   C CE2 . TYR A 93   ? 0.3446 0.4377 0.3896 0.0222  -0.0061 -0.1008 91   TYR A CE2 
557   C CZ  . TYR A 93   ? 0.2856 0.3919 0.3284 0.0226  -0.0053 -0.1053 91   TYR A CZ  
558   O OH  . TYR A 93   ? 0.3771 0.4941 0.4172 0.0223  -0.0051 -0.1084 91   TYR A OH  
559   N N   . SER A 94   ? 0.2727 0.3296 0.3447 0.0282  -0.0113 -0.0986 92   SER A N   
560   C CA  . SER A 94   ? 0.2663 0.3163 0.3418 0.0288  -0.0119 -0.0959 92   SER A CA  
561   C C   . SER A 94   ? 0.2549 0.3010 0.3218 0.0266  -0.0092 -0.0877 92   SER A C   
562   O O   . SER A 94   ? 0.2818 0.3285 0.3473 0.0267  -0.0084 -0.0865 92   SER A O   
563   C CB  . SER A 94   ? 0.2991 0.3552 0.3800 0.0311  -0.0130 -0.1026 92   SER A CB  
564   O OG  . SER A 94   ? 0.3148 0.3752 0.4037 0.0333  -0.0155 -0.1110 92   SER A OG  
565   N N   . LEU A 95   ? 0.2307 0.2731 0.2921 0.0246  -0.0080 -0.0822 93   LEU A N   
566   C CA  . LEU A 95   ? 0.2585 0.2974 0.3118 0.0225  -0.0056 -0.0748 93   LEU A CA  
567   C C   . LEU A 95   ? 0.2430 0.2719 0.2991 0.0226  -0.0063 -0.0699 93   LEU A C   
568   O O   . LEU A 95   ? 0.2539 0.2767 0.3158 0.0232  -0.0081 -0.0694 93   LEU A O   
569   C CB  . LEU A 95   ? 0.2175 0.2560 0.2646 0.0204  -0.0043 -0.0709 93   LEU A CB  
570   C CG  . LEU A 95   ? 0.2182 0.2667 0.2617 0.0199  -0.0035 -0.0745 93   LEU A CG  
571   C CD1 . LEU A 95   ? 0.2669 0.3134 0.3040 0.0177  -0.0021 -0.0692 93   LEU A CD1 
572   C CD2 . LEU A 95   ? 0.2413 0.2986 0.2811 0.0197  -0.0021 -0.0762 93   LEU A CD2 
573   N N   . SER A 96   ? 0.2209 0.2486 0.2728 0.0219  -0.0049 -0.0661 94   SER A N   
574   C CA  . SER A 96   ? 0.2047 0.2235 0.2566 0.0214  -0.0049 -0.0601 94   SER A CA  
575   C C   . SER A 96   ? 0.2119 0.2266 0.2582 0.0196  -0.0037 -0.0546 94   SER A C   
576   O O   . SER A 96   ? 0.2185 0.2372 0.2604 0.0185  -0.0026 -0.0549 94   SER A O   
577   C CB  . SER A 96   ? 0.2224 0.2418 0.2704 0.0210  -0.0036 -0.0576 94   SER A CB  
578   O OG  . SER A 96   ? 0.2032 0.2262 0.2427 0.0191  -0.0014 -0.0551 94   SER A OG  
579   N N   . SER A 97   ? 0.2234 0.2305 0.2701 0.0192  -0.0038 -0.0493 95   SER A N   
580   C CA  . SER A 97   ? 0.2342 0.2375 0.2760 0.0176  -0.0026 -0.0441 95   SER A CA  
581   C C   . SER A 97   ? 0.2011 0.2075 0.2341 0.0160  -0.0003 -0.0417 95   SER A C   
582   O O   . SER A 97   ? 0.2060 0.2135 0.2348 0.0147  0.0007  -0.0404 95   SER A O   
583   C CB  . SER A 97   ? 0.2881 0.2839 0.3316 0.0176  -0.0030 -0.0389 95   SER A CB  
584   O OG  . SER A 97   ? 0.3876 0.3802 0.4392 0.0187  -0.0052 -0.0401 95   SER A OG  
585   N N   . GLN A 98   ? 0.1983 0.2061 0.2289 0.0159  0.0005  -0.0410 96   GLN A N   
586   C CA  . GLN A 98   ? 0.2057 0.2163 0.2289 0.0142  0.0024  -0.0385 96   GLN A CA  
587   C C   . GLN A 98   ? 0.1720 0.1905 0.1931 0.0136  0.0029  -0.0419 96   GLN A C   
588   O O   . GLN A 98   ? 0.1879 0.2081 0.2036 0.0120  0.0041  -0.0394 96   GLN A O   
589   C CB  . GLN A 98   ? 0.1871 0.1979 0.2088 0.0143  0.0029  -0.0374 96   GLN A CB  
590   C CG  . GLN A 98   ? 0.2135 0.2171 0.2349 0.0144  0.0028  -0.0327 96   GLN A CG  
591   C CD  . GLN A 98   ? 0.2130 0.2133 0.2288 0.0129  0.0040  -0.0280 96   GLN A CD  
592   O OE1 . GLN A 98   ? 0.2437 0.2411 0.2602 0.0127  0.0038  -0.0267 96   GLN A OE1 
593   N NE2 . GLN A 98   ? 0.2401 0.2407 0.2509 0.0119  0.0051  -0.0255 96   GLN A NE2 
594   N N   . GLU A 99   ? 0.1696 0.1933 0.1952 0.0150  0.0019  -0.0477 97   GLU A N   
595   C CA  . GLU A 99   ? 0.1729 0.2052 0.1968 0.0145  0.0023  -0.0512 97   GLU A CA  
596   C C   . GLU A 99   ? 0.1880 0.2194 0.2111 0.0139  0.0022  -0.0506 97   GLU A C   
597   O O   . GLU A 99   ? 0.1916 0.2277 0.2099 0.0124  0.0032  -0.0496 97   GLU A O   
598   C CB  . GLU A 99   ? 0.1760 0.2143 0.2056 0.0165  0.0011  -0.0581 97   GLU A CB  
599   C CG  . GLU A 99   ? 0.1802 0.2221 0.2092 0.0168  0.0016  -0.0589 97   GLU A CG  
600   C CD  . GLU A 99   ? 0.1822 0.2289 0.2179 0.0191  0.0002  -0.0658 97   GLU A CD  
601   O OE1 . GLU A 99   ? 0.2136 0.2601 0.2548 0.0205  -0.0015 -0.0700 97   GLU A OE1 
602   O OE2 . GLU A 99   ? 0.1976 0.2481 0.2334 0.0195  0.0005  -0.0672 97   GLU A OE2 
603   N N   . GLY A 100  ? 0.1796 0.2050 0.2075 0.0148  0.0008  -0.0508 98   GLY A N   
604   C CA  . GLY A 100  ? 0.1911 0.2152 0.2185 0.0141  0.0006  -0.0499 98   GLY A CA  
605   C C   . GLY A 100  ? 0.2157 0.2369 0.2363 0.0121  0.0022  -0.0438 98   GLY A C   
606   O O   . GLY A 100  ? 0.1950 0.2195 0.2123 0.0110  0.0028  -0.0432 98   GLY A O   
607   N N   . VAL A 101  ? 0.1810 0.1963 0.1999 0.0118  0.0028  -0.0393 99   VAL A N   
608   C CA  . VAL A 101  ? 0.1912 0.2036 0.2042 0.0101  0.0042  -0.0339 99   VAL A CA  
609   C C   . VAL A 101  ? 0.1825 0.2013 0.1903 0.0087  0.0054  -0.0334 99   VAL A C   
610   O O   . VAL A 101  ? 0.1999 0.2198 0.2040 0.0072  0.0060  -0.0312 99   VAL A O   
611   C CB  . VAL A 101  ? 0.1916 0.1974 0.2040 0.0103  0.0045  -0.0299 99   VAL A CB  
612   C CG1 . VAL A 101  ? 0.2190 0.2228 0.2256 0.0087  0.0058  -0.0251 99   VAL A CG1 
613   C CG2 . VAL A 101  ? 0.2056 0.2055 0.2231 0.0114  0.0033  -0.0293 99   VAL A CG2 
614   N N   . ALA A 102  ? 0.1736 0.1970 0.1813 0.0089  0.0056  -0.0355 100  ALA A N   
615   C CA  . ALA A 102  ? 0.1783 0.2080 0.1813 0.0073  0.0067  -0.0345 100  ALA A CA  
616   C C   . ALA A 102  ? 0.1791 0.2163 0.1814 0.0067  0.0067  -0.0368 100  ALA A C   
617   O O   . ALA A 102  ? 0.1894 0.2297 0.1874 0.0049  0.0074  -0.0339 100  ALA A O   
618   C CB  . ALA A 102  ? 0.1904 0.2243 0.1942 0.0078  0.0069  -0.0366 100  ALA A CB  
619   N N   . LEU A 103  ? 0.1701 0.2102 0.1768 0.0082  0.0056  -0.0420 101  LEU A N   
620   C CA  . LEU A 103  ? 0.1735 0.2211 0.1797 0.0079  0.0054  -0.0448 101  LEU A CA  
621   C C   . LEU A 103  ? 0.1873 0.2316 0.1910 0.0066  0.0056  -0.0412 101  LEU A C   
622   O O   . LEU A 103  ? 0.2094 0.2595 0.2095 0.0051  0.0061  -0.0401 101  LEU A O   
623   C CB  . LEU A 103  ? 0.1794 0.2294 0.1917 0.0101  0.0039  -0.0515 101  LEU A CB  
624   C CG  . LEU A 103  ? 0.1911 0.2489 0.2034 0.0100  0.0035  -0.0551 101  LEU A CG  
625   C CD1 . LEU A 103  ? 0.2267 0.2957 0.2350 0.0089  0.0045  -0.0560 101  LEU A CD1 
626   C CD2 . LEU A 103  ? 0.2251 0.2835 0.2445 0.0123  0.0016  -0.0617 101  LEU A CD2 
627   N N   . MET A 104  ? 0.1930 0.2283 0.1986 0.0071  0.0051  -0.0392 102  MET A N   
628   C CA  . MET A 104  ? 0.1889 0.2212 0.1924 0.0061  0.0052  -0.0359 102  MET A CA  
629   C C   . MET A 104  ? 0.2031 0.2344 0.2011 0.0041  0.0064  -0.0303 102  MET A C   
630   O O   . MET A 104  ? 0.2172 0.2503 0.2126 0.0028  0.0066  -0.0281 102  MET A O   
631   C CB  . MET A 104  ? 0.2037 0.2272 0.2109 0.0071  0.0044  -0.0349 102  MET A CB  
632   C CG  . MET A 104  ? 0.2211 0.2453 0.2348 0.0089  0.0028  -0.0403 102  MET A CG  
633   S SD  . MET A 104  ? 0.3084 0.3418 0.3231 0.0090  0.0020  -0.0455 102  MET A SD  
634   C CE  . MET A 104  ? 0.3298 0.3595 0.3420 0.0076  0.0022  -0.0413 102  MET A CE  
635   N N   . CYS A 105  ? 0.1925 0.2213 0.1891 0.0039  0.0070  -0.0281 103  CYS A N   
636   C CA  . CYS A 105  ? 0.2000 0.2284 0.1920 0.0020  0.0078  -0.0233 103  CYS A CA  
637   C C   . CYS A 105  ? 0.2306 0.2683 0.2200 0.0005  0.0082  -0.0234 103  CYS A C   
638   O O   . CYS A 105  ? 0.2443 0.2831 0.2308 -0.0012 0.0084  -0.0198 103  CYS A O   
639   C CB  . CYS A 105  ? 0.2145 0.2391 0.2061 0.0022  0.0082  -0.0216 103  CYS A CB  
640   S SG  . CYS A 105  ? 0.2309 0.2452 0.2244 0.0036  0.0080  -0.0198 103  CYS A SG  
641   N N   . LEU A 106  ? 0.1985 0.2434 0.1892 0.0011  0.0082  -0.0275 104  LEU A N   
642   C CA  . LEU A 106  ? 0.2179 0.2732 0.2064 -0.0003 0.0085  -0.0279 104  LEU A CA  
643   C C   . LEU A 106  ? 0.2342 0.2929 0.2221 -0.0008 0.0081  -0.0283 104  LEU A C   
644   O O   . LEU A 106  ? 0.2324 0.2961 0.2173 -0.0027 0.0084  -0.0252 104  LEU A O   
645   C CB  . LEU A 106  ? 0.2189 0.2819 0.2095 0.0009  0.0085  -0.0332 104  LEU A CB  
646   C CG  . LEU A 106  ? 0.2083 0.2837 0.1969 -0.0002 0.0088  -0.0345 104  LEU A CG  
647   C CD1 . LEU A 106  ? 0.2660 0.3442 0.2507 -0.0028 0.0096  -0.0288 104  LEU A CD1 
648   C CD2 . LEU A 106  ? 0.2453 0.3283 0.2368 0.0015  0.0087  -0.0408 104  LEU A CD2 
649   N N   . ALA A 107  ? 0.2037 0.2601 0.1949 0.0009  0.0073  -0.0321 105  ALA A N   
650   C CA  . ALA A 107  ? 0.2262 0.2861 0.2172 0.0005  0.0068  -0.0329 105  ALA A CA  
651   C C   . ALA A 107  ? 0.2663 0.3210 0.2544 -0.0011 0.0070  -0.0270 105  ALA A C   
652   O O   . ALA A 107  ? 0.2538 0.3138 0.2394 -0.0027 0.0070  -0.0251 105  ALA A O   
653   C CB  . ALA A 107  ? 0.2034 0.2605 0.1992 0.0026  0.0056  -0.0378 105  ALA A CB  
654   N N   . GLU A 108  ? 0.2364 0.2812 0.2249 -0.0008 0.0071  -0.0241 106  GLU A N   
655   C CA  . GLU A 108  ? 0.2440 0.2835 0.2302 -0.0022 0.0072  -0.0188 106  GLU A CA  
656   C C   . GLU A 108  ? 0.3225 0.3669 0.3052 -0.0044 0.0076  -0.0148 106  GLU A C   
657   O O   . GLU A 108  ? 0.3187 0.3645 0.2996 -0.0058 0.0074  -0.0117 106  GLU A O   
658   C CB  . GLU A 108  ? 0.2676 0.2972 0.2547 -0.0013 0.0075  -0.0167 106  GLU A CB  
659   C CG  . GLU A 108  ? 0.2880 0.3119 0.2731 -0.0024 0.0076  -0.0117 106  GLU A CG  
660   C CD  . GLU A 108  ? 0.3239 0.3403 0.3089 -0.0018 0.0079  -0.0095 106  GLU A CD  
661   O OE1 . GLU A 108  ? 0.3003 0.3141 0.2875 -0.0003 0.0080  -0.0118 106  GLU A OE1 
662   O OE2 . GLU A 108  ? 0.3415 0.3548 0.3246 -0.0028 0.0080  -0.0057 106  GLU A OE2 
663   N N   . ALA A 109  ? 0.2806 0.3277 0.2625 -0.0048 0.0081  -0.0146 107  ALA A N   
664   C CA  . ALA A 109  ? 0.2901 0.3418 0.2693 -0.0070 0.0084  -0.0105 107  ALA A CA  
665   C C   . ALA A 109  ? 0.3225 0.3851 0.3004 -0.0083 0.0082  -0.0110 107  ALA A C   
666   O O   . ALA A 109  ? 0.3605 0.4258 0.3366 -0.0103 0.0080  -0.0066 107  ALA A O   
667   C CB  . ALA A 109  ? 0.3156 0.3685 0.2948 -0.0070 0.0089  -0.0107 107  ALA A CB  
668   N N   . LEU A 110  ? 0.2764 0.3458 0.2556 -0.0070 0.0083  -0.0164 108  LEU A N   
669   C CA  . LEU A 110  ? 0.2837 0.3646 0.2616 -0.0080 0.0081  -0.0175 108  LEU A CA  
670   C C   . LEU A 110  ? 0.2944 0.3744 0.2716 -0.0086 0.0075  -0.0157 108  LEU A C   
671   O O   . LEU A 110  ? 0.3206 0.4088 0.2958 -0.0104 0.0073  -0.0135 108  LEU A O   
672   C CB  . LEU A 110  ? 0.2539 0.3416 0.2339 -0.0060 0.0081  -0.0246 108  LEU A CB  
673   C CG  . LEU A 110  ? 0.2728 0.3649 0.2531 -0.0057 0.0088  -0.0263 108  LEU A CG  
674   C CD1 . LEU A 110  ? 0.2614 0.3578 0.2449 -0.0033 0.0085  -0.0339 108  LEU A CD1 
675   C CD2 . LEU A 110  ? 0.3349 0.4380 0.3122 -0.0082 0.0093  -0.0229 108  LEU A CD2 
676   N N   . LEU A 111  ? 0.2864 0.3571 0.2655 -0.0073 0.0071  -0.0165 109  LEU A N   
677   C CA  . LEU A 111  ? 0.3167 0.3857 0.2955 -0.0078 0.0064  -0.0148 109  LEU A CA  
678   C C   . LEU A 111  ? 0.3974 0.4622 0.3742 -0.0097 0.0063  -0.0081 109  LEU A C   
679   O O   . LEU A 111  ? 0.4181 0.4831 0.3944 -0.0105 0.0057  -0.0060 109  LEU A O   
680   C CB  . LEU A 111  ? 0.3176 0.3784 0.2995 -0.0057 0.0060  -0.0179 109  LEU A CB  
681   C CG  . LEU A 111  ? 0.3131 0.3785 0.2980 -0.0038 0.0055  -0.0248 109  LEU A CG  
682   C CD1 . LEU A 111  ? 0.3446 0.4011 0.3334 -0.0019 0.0050  -0.0272 109  LEU A CD1 
683   C CD2 . LEU A 111  ? 0.3201 0.3956 0.3041 -0.0043 0.0050  -0.0270 109  LEU A CD2 
684   N N   . ARG A 112  ? 0.3873 0.4486 0.3635 -0.0105 0.0067  -0.0048 110  ARG A N   
685   C CA  . ARG A 112  ? 0.4227 0.4817 0.3975 -0.0125 0.0063  0.0014  110  ARG A CA  
686   C C   . ARG A 112  ? 0.4652 0.5348 0.4383 -0.0149 0.0060  0.0044  110  ARG A C   
687   O O   . ARG A 112  ? 0.4844 0.5532 0.4570 -0.0168 0.0053  0.0098  110  ARG A O   
688   C CB  . ARG A 112  ? 0.4448 0.4966 0.4199 -0.0125 0.0066  0.0037  110  ARG A CB  
689   C CG  . ARG A 112  ? 0.3943 0.4355 0.3709 -0.0105 0.0068  0.0020  110  ARG A CG  
690   C CD  . ARG A 112  ? 0.4254 0.4618 0.4023 -0.0100 0.0072  0.0025  110  ARG A CD  
691   N NE  . ARG A 112  ? 0.5515 0.5848 0.5278 -0.0116 0.0067  0.0074  110  ARG A NE  
692   C CZ  . ARG A 112  ? 0.6376 0.6626 0.6145 -0.0111 0.0063  0.0094  110  ARG A CZ  
693   N NH1 . ARG A 112  ? 0.5833 0.6025 0.5610 -0.0093 0.0066  0.0076  110  ARG A NH1 
694   N NH2 . ARG A 112  ? 0.6476 0.6706 0.6247 -0.0125 0.0056  0.0135  110  ARG A NH2 
695   N N   . ILE A 113  ? 0.4202 0.5001 0.3926 -0.0149 0.0064  0.0011  111  ILE A N   
696   C CA  . ILE A 113  ? 0.4294 0.5213 0.4001 -0.0170 0.0062  0.0035  111  ILE A CA  
697   C C   . ILE A 113  ? 0.4620 0.5573 0.4324 -0.0169 0.0055  0.0025  111  ILE A C   
698   O O   . ILE A 113  ? 0.4862 0.5839 0.4573 -0.0151 0.0056  -0.0033 111  ILE A O   
699   C CB  . ILE A 113  ? 0.3805 0.4830 0.3506 -0.0168 0.0069  -0.0001 111  ILE A CB  
700   C CG1 . ILE A 113  ? 0.4201 0.5195 0.3907 -0.0171 0.0075  0.0015  111  ILE A CG1 
701   C CG2 . ILE A 113  ? 0.4515 0.5678 0.4197 -0.0189 0.0067  0.0021  111  ILE A CG2 
702   C CD1 . ILE A 113  ? 0.4385 0.5463 0.4091 -0.0163 0.0084  -0.0030 111  ILE A CD1 
703   N N   . PRO A 114  ? 0.5556 0.6513 0.5252 -0.0189 0.0046  0.0080  112  PRO A N   
704   C CA  . PRO A 114  ? 0.4923 0.5900 0.4617 -0.0187 0.0039  0.0072  112  PRO A CA  
705   C C   . PRO A 114  ? 0.5196 0.6310 0.4877 -0.0188 0.0039  0.0038  112  PRO A C   
706   O O   . PRO A 114  ? 0.5933 0.7056 0.5620 -0.0172 0.0037  -0.0010 112  PRO A O   
707   C CB  . PRO A 114  ? 0.5443 0.6398 0.5135 -0.0210 0.0028  0.0146  112  PRO A CB  
708   C CG  . PRO A 114  ? 0.6326 0.7202 0.6027 -0.0215 0.0030  0.0180  112  PRO A CG  
709   C CD  . PRO A 114  ? 0.5855 0.6779 0.5551 -0.0211 0.0040  0.0150  112  PRO A CD  
710   N N   . ASP A 115  ? 0.5575 0.6800 0.5239 -0.0207 0.0041  0.0062  113  ASP A N   
711   C CA  . ASP A 115  ? 0.5635 0.7006 0.5283 -0.0209 0.0041  0.0035  113  ASP A CA  
712   C C   . ASP A 115  ? 0.5194 0.6605 0.4850 -0.0184 0.0049  -0.0048 113  ASP A C   
713   O O   . ASP A 115  ? 0.5001 0.6412 0.4661 -0.0181 0.0058  -0.0059 113  ASP A O   
714   C CB  . ASP A 115  ? 0.5209 0.6694 0.4837 -0.0239 0.0040  0.0093  113  ASP A CB  
715   C CG  . ASP A 115  ? 0.5684 0.7334 0.5294 -0.0242 0.0041  0.0066  113  ASP A CG  
716   O OD1 . ASP A 115  ? 0.6663 0.8338 0.6268 -0.0239 0.0033  0.0055  113  ASP A OD1 
717   O OD2 . ASP A 115  ? 0.5906 0.7665 0.5505 -0.0247 0.0049  0.0055  113  ASP A OD2 
718   N N   . THR A 116  ? 0.4925 0.6373 0.4587 -0.0167 0.0045  -0.0106 114  THR A N   
719   C CA  . THR A 116  ? 0.4368 0.5846 0.4049 -0.0141 0.0048  -0.0190 114  THR A CA  
720   C C   . THR A 116  ? 0.4985 0.6601 0.4651 -0.0145 0.0056  -0.0209 114  THR A C   
721   O O   . THR A 116  ? 0.4707 0.6316 0.4388 -0.0129 0.0063  -0.0252 114  THR A O   
722   C CB  . THR A 116  ? 0.5112 0.6613 0.4806 -0.0124 0.0039  -0.0246 114  THR A CB  
723   O OG1 . THR A 116  ? 0.5406 0.6772 0.5119 -0.0117 0.0032  -0.0234 114  THR A OG1 
724   C CG2 . THR A 116  ? 0.5406 0.6952 0.5125 -0.0096 0.0039  -0.0337 114  THR A CG2 
725   N N   . ALA A 117  ? 0.4726 0.6473 0.4364 -0.0166 0.0055  -0.0176 115  ALA A N   
726   C CA  . ALA A 117  ? 0.4462 0.6355 0.4085 -0.0172 0.0064  -0.0190 115  ALA A CA  
727   C C   . ALA A 117  ? 0.3921 0.5778 0.3544 -0.0184 0.0073  -0.0149 115  ALA A C   
728   O O   . ALA A 117  ? 0.4414 0.6334 0.4042 -0.0174 0.0082  -0.0187 115  ALA A O   
729   C CB  . ALA A 117  ? 0.5229 0.7271 0.4822 -0.0196 0.0061  -0.0151 115  ALA A CB  
730   N N   . THR A 118  ? 0.4259 0.6017 0.3880 -0.0203 0.0070  -0.0074 116  THR A N   
731   C CA  . THR A 118  ? 0.4393 0.6107 0.4020 -0.0213 0.0077  -0.0036 116  THR A CA  
732   C C   . THR A 118  ? 0.3716 0.5333 0.3366 -0.0185 0.0083  -0.0094 116  THR A C   
733   O O   . THR A 118  ? 0.4165 0.5809 0.3819 -0.0183 0.0091  -0.0106 116  THR A O   
734   C CB  . THR A 118  ? 0.4215 0.5830 0.3842 -0.0236 0.0069  0.0048  116  THR A CB  
735   O OG1 . THR A 118  ? 0.6118 0.7820 0.5729 -0.0262 0.0062  0.0104  116  THR A OG1 
736   C CG2 . THR A 118  ? 0.4317 0.5897 0.3952 -0.0249 0.0074  0.0088  116  THR A CG2 
737   N N   . ARG A 119  ? 0.4116 0.5623 0.3783 -0.0164 0.0078  -0.0127 117  ARG A N   
738   C CA  A ARG A 119  ? 0.3886 0.5301 0.3580 -0.0138 0.0081  -0.0178 117  ARG A CA  
739   C CA  B ARG A 119  ? 0.3884 0.5299 0.3578 -0.0138 0.0081  -0.0178 117  ARG A CA  
740   C C   . ARG A 119  ? 0.3527 0.5039 0.3233 -0.0118 0.0085  -0.0255 117  ARG A C   
741   O O   . ARG A 119  ? 0.3827 0.5325 0.3546 -0.0109 0.0092  -0.0276 117  ARG A O   
742   C CB  A ARG A 119  ? 0.3663 0.4962 0.3377 -0.0121 0.0073  -0.0198 117  ARG A CB  
743   C CB  B ARG A 119  ? 0.3674 0.4968 0.3388 -0.0121 0.0073  -0.0197 117  ARG A CB  
744   C CG  A ARG A 119  ? 0.3205 0.4393 0.2949 -0.0098 0.0075  -0.0235 117  ARG A CG  
745   C CG  B ARG A 119  ? 0.3350 0.4569 0.3097 -0.0093 0.0074  -0.0257 117  ARG A CG  
746   C CD  A ARG A 119  ? 0.3424 0.4526 0.3191 -0.0081 0.0066  -0.0261 117  ARG A CD  
747   C CD  B ARG A 119  ? 0.3458 0.4554 0.3227 -0.0079 0.0067  -0.0264 117  ARG A CD  
748   N NE  A ARG A 119  ? 0.3508 0.4549 0.3262 -0.0096 0.0062  -0.0205 117  ARG A NE  
749   N NE  B ARG A 119  ? 0.3373 0.4505 0.3144 -0.0076 0.0059  -0.0285 117  ARG A NE  
750   C CZ  A ARG A 119  ? 0.3584 0.4635 0.3338 -0.0095 0.0054  -0.0210 117  ARG A CZ  
751   C CZ  B ARG A 119  ? 0.3668 0.4767 0.3426 -0.0090 0.0054  -0.0240 117  ARG A CZ  
752   N NH1 A ARG A 119  ? 0.3604 0.4719 0.3372 -0.0081 0.0049  -0.0271 117  ARG A NH1 
753   N NH1 B ARG A 119  ? 0.3772 0.4801 0.3516 -0.0106 0.0056  -0.0173 117  ARG A NH1 
754   N NH2 A ARG A 119  ? 0.4364 0.5358 0.4109 -0.0109 0.0050  -0.0155 117  ARG A NH2 
755   N NH2 B ARG A 119  ? 0.3833 0.4970 0.3595 -0.0085 0.0045  -0.0265 117  ARG A NH2 
756   N N   . ASP A 120  ? 0.3744 0.5357 0.3447 -0.0111 0.0081  -0.0299 118  ASP A N   
757   C CA  . ASP A 120  ? 0.3789 0.5498 0.3510 -0.0089 0.0083  -0.0381 118  ASP A CA  
758   C C   . ASP A 120  ? 0.4129 0.5953 0.3833 -0.0100 0.0094  -0.0371 118  ASP A C   
759   O O   . ASP A 120  ? 0.3905 0.5758 0.3630 -0.0081 0.0098  -0.0426 118  ASP A O   
760   C CB  . ASP A 120  ? 0.3865 0.5667 0.3586 -0.0080 0.0074  -0.0429 118  ASP A CB  
761   C CG  . ASP A 120  ? 0.5046 0.6736 0.4790 -0.0066 0.0062  -0.0447 118  ASP A CG  
762   O OD1 . ASP A 120  ? 0.4764 0.6308 0.4525 -0.0062 0.0062  -0.0426 118  ASP A OD1 
763   O OD2 . ASP A 120  ? 0.4693 0.6442 0.4438 -0.0060 0.0054  -0.0480 118  ASP A OD2 
764   N N   . ALA A 121  ? 0.3979 0.5873 0.3650 -0.0132 0.0098  -0.0299 119  ALA A N   
765   C CA  . ALA A 121  ? 0.4161 0.6165 0.3818 -0.0146 0.0108  -0.0279 119  ALA A CA  
766   C C   . ALA A 121  ? 0.4213 0.6117 0.3886 -0.0145 0.0114  -0.0261 119  ALA A C   
767   O O   . ALA A 121  ? 0.4174 0.6141 0.3854 -0.0138 0.0122  -0.0291 119  ALA A O   
768   C CB  . ALA A 121  ? 0.4319 0.6413 0.3944 -0.0183 0.0108  -0.0197 119  ALA A CB  
769   N N   . LEU A 122  ? 0.4061 0.5815 0.3738 -0.0152 0.0109  -0.0213 120  LEU A N   
770   C CA  . LEU A 122  ? 0.4238 0.5894 0.3930 -0.0149 0.0113  -0.0200 120  LEU A CA  
771   C C   . LEU A 122  ? 0.4211 0.5832 0.3934 -0.0115 0.0115  -0.0282 120  LEU A C   
772   O O   . LEU A 122  ? 0.3947 0.5577 0.3680 -0.0109 0.0121  -0.0296 120  LEU A O   
773   C CB  . LEU A 122  ? 0.4433 0.5938 0.4127 -0.0158 0.0107  -0.0144 120  LEU A CB  
774   C CG  . LEU A 122  ? 0.4168 0.5581 0.3871 -0.0161 0.0110  -0.0116 120  LEU A CG  
775   C CD1 . LEU A 122  ? 0.5049 0.6550 0.4740 -0.0188 0.0115  -0.0064 120  LEU A CD1 
776   C CD2 . LEU A 122  ? 0.4088 0.5354 0.3796 -0.0163 0.0103  -0.0075 120  LEU A CD2 
777   N N   . ILE A 123  ? 0.3958 0.5542 0.3698 -0.0092 0.0107  -0.0336 121  ILE A N   
778   C CA  . ILE A 123  ? 0.3784 0.5337 0.3562 -0.0059 0.0105  -0.0413 121  ILE A CA  
779   C C   . ILE A 123  ? 0.3994 0.5692 0.3779 -0.0049 0.0110  -0.0469 121  ILE A C   
780   O O   . ILE A 123  ? 0.3880 0.5570 0.3685 -0.0037 0.0114  -0.0497 121  ILE A O   
781   C CB  . ILE A 123  ? 0.3492 0.4989 0.3294 -0.0040 0.0093  -0.0457 121  ILE A CB  
782   C CG1 . ILE A 123  ? 0.3473 0.4816 0.3274 -0.0045 0.0089  -0.0407 121  ILE A CG1 
783   C CG2 . ILE A 123  ? 0.3040 0.4538 0.2889 -0.0006 0.0087  -0.0545 121  ILE A CG2 
784   C CD1 . ILE A 123  ? 0.3417 0.4718 0.3235 -0.0034 0.0078  -0.0432 121  ILE A CD1 
785   N N   . ARG A 124  ? 0.3763 0.5598 0.3531 -0.0054 0.0110  -0.0488 122  ARG A N   
786   C CA  . ARG A 124  ? 0.4068 0.6052 0.3845 -0.0040 0.0114  -0.0554 122  ARG A CA  
787   C C   . ARG A 124  ? 0.4654 0.6713 0.4415 -0.0057 0.0127  -0.0519 122  ARG A C   
788   O O   . ARG A 124  ? 0.4725 0.6831 0.4508 -0.0039 0.0131  -0.0571 122  ARG A O   
789   C CB  . ARG A 124  ? 0.4166 0.6288 0.3924 -0.0043 0.0111  -0.0577 122  ARG A CB  
790   N N   . ASP A 125  ? 0.4785 0.6854 0.4511 -0.0091 0.0133  -0.0431 123  ASP A N   
791   C CA  . ASP A 125  ? 0.5496 0.7662 0.5207 -0.0111 0.0144  -0.0393 123  ASP A CA  
792   C C   . ASP A 125  ? 0.5470 0.7521 0.5192 -0.0117 0.0147  -0.0356 123  ASP A C   
793   O O   . ASP A 125  ? 0.5795 0.7913 0.5521 -0.0120 0.0156  -0.0356 123  ASP A O   
794   C CB  . ASP A 125  ? 0.6086 0.8345 0.5760 -0.0148 0.0146  -0.0316 123  ASP A CB  
795   C CG  . ASP A 125  ? 0.6298 0.8687 0.5956 -0.0145 0.0143  -0.0349 123  ASP A CG  
796   O OD1 . ASP A 125  ? 0.6747 0.9228 0.6419 -0.0118 0.0144  -0.0434 123  ASP A OD1 
797   O OD2 . ASP A 125  ? 0.6402 0.8805 0.6036 -0.0167 0.0138  -0.0292 123  ASP A OD2 
798   N N   . LYS A 126  ? 0.4719 0.6605 0.4447 -0.0117 0.0140  -0.0324 124  LYS A N   
799   C CA  . LYS A 126  ? 0.4694 0.6473 0.4429 -0.0125 0.0142  -0.0280 124  LYS A CA  
800   C C   . LYS A 126  ? 0.5267 0.6909 0.5033 -0.0097 0.0137  -0.0323 124  LYS A C   
801   O O   . LYS A 126  ? 0.5785 0.7410 0.5568 -0.0088 0.0141  -0.0340 124  LYS A O   
802   C CB  . LYS A 126  ? 0.5562 0.7275 0.5277 -0.0156 0.0137  -0.0190 124  LYS A CB  
803   N N   . ILE A 127  ? 0.4532 0.6078 0.4307 -0.0083 0.0129  -0.0339 125  ILE A N   
804   C CA  . ILE A 127  ? 0.4192 0.5604 0.3997 -0.0059 0.0124  -0.0368 125  ILE A CA  
805   C C   . ILE A 127  ? 0.4376 0.5832 0.4216 -0.0030 0.0123  -0.0450 125  ILE A C   
806   O O   . ILE A 127  ? 0.4938 0.6338 0.4801 -0.0017 0.0123  -0.0464 125  ILE A O   
807   C CB  . ILE A 127  ? 0.3840 0.5154 0.3650 -0.0052 0.0115  -0.0366 125  ILE A CB  
808   C CG1 . ILE A 127  ? 0.4731 0.6014 0.4509 -0.0080 0.0114  -0.0289 125  ILE A CG1 
809   C CG2 . ILE A 127  ? 0.3992 0.5167 0.3832 -0.0032 0.0110  -0.0382 125  ILE A CG2 
810   C CD1 . ILE A 127  ? 0.4064 0.5274 0.3833 -0.0097 0.0116  -0.0228 125  ILE A CD1 
811   N N   . ALA A 128  ? 0.3692 0.5249 0.3541 -0.0017 0.0120  -0.0507 126  ALA A N   
812   C CA  . ALA A 128  ? 0.3578 0.5172 0.3470 0.0014  0.0116  -0.0593 126  ALA A CA  
813   C C   . ALA A 128  ? 0.4831 0.6510 0.4726 0.0014  0.0125  -0.0605 126  ALA A C   
814   O O   . ALA A 128  ? 0.4836 0.6486 0.4770 0.0037  0.0122  -0.0653 126  ALA A O   
815   C CB  . ALA A 128  ? 0.3639 0.5332 0.3540 0.0027  0.0109  -0.0653 126  ALA A CB  
816   N N   . ASP A 129  ? 0.6459 0.8242 0.6316 -0.0012 0.0136  -0.0560 127  ASP A N   
817   C CA  . ASP A 129  ? 0.6898 0.8789 0.6758 -0.0014 0.0146  -0.0574 127  ASP A CA  
818   C C   . ASP A 129  ? 0.6915 0.8714 0.6786 -0.0016 0.0149  -0.0544 127  ASP A C   
819   O O   . ASP A 129  ? 0.7547 0.9410 0.7434 -0.0008 0.0154  -0.0573 127  ASP A O   
820   C CB  . ASP A 129  ? 0.6672 0.8705 0.6490 -0.0044 0.0156  -0.0527 127  ASP A CB  
821   N N   . GLY A 130  ? 0.6677 0.8334 0.6539 -0.0027 0.0145  -0.0489 128  GLY A N   
822   C CA  . GLY A 130  ? 0.6669 0.8240 0.6543 -0.0027 0.0146  -0.0465 128  GLY A CA  
823   C C   . GLY A 130  ? 0.7018 0.8446 0.6877 -0.0041 0.0142  -0.0401 128  GLY A C   
824   O O   . GLY A 130  ? 0.6979 0.8299 0.6851 -0.0027 0.0134  -0.0411 128  GLY A O   
825   N N   . ASN A 131  ? 0.7251 0.8681 0.7088 -0.0068 0.0147  -0.0335 129  ASN A N   
826   C CA  . ASN A 131  ? 0.6707 0.8006 0.6536 -0.0080 0.0142  -0.0278 129  ASN A CA  
827   C C   . ASN A 131  ? 0.5877 0.7118 0.5689 -0.0088 0.0136  -0.0248 129  ASN A C   
828   O O   . ASN A 131  ? 0.6320 0.7609 0.6108 -0.0113 0.0137  -0.0201 129  ASN A O   
829   C CB  . ASN A 131  ? 0.6564 0.7894 0.6379 -0.0108 0.0146  -0.0218 129  ASN A CB  
830   N N   . TRP A 132  ? 0.5452 0.6591 0.5278 -0.0067 0.0130  -0.0274 130  TRP A N   
831   C CA  . TRP A 132  ? 0.4382 0.5451 0.4196 -0.0074 0.0125  -0.0243 130  TRP A CA  
832   C C   . TRP A 132  ? 0.4197 0.5182 0.3996 -0.0093 0.0122  -0.0176 130  TRP A C   
833   O O   . TRP A 132  ? 0.5003 0.5960 0.4785 -0.0108 0.0118  -0.0135 130  TRP A O   
834   C CB  . TRP A 132  ? 0.4343 0.5324 0.4180 -0.0047 0.0118  -0.0286 130  TRP A CB  
835   C CG  . TRP A 132  ? 0.3797 0.4687 0.3656 -0.0031 0.0116  -0.0295 130  TRP A CG  
836   C CD1 . TRP A 132  ? 0.3682 0.4589 0.3571 -0.0010 0.0116  -0.0344 130  TRP A CD1 
837   C CD2 . TRP A 132  ? 0.2959 0.3733 0.2813 -0.0034 0.0114  -0.0254 130  TRP A CD2 
838   N NE1 . TRP A 132  ? 0.3290 0.4097 0.3192 -0.0001 0.0113  -0.0333 130  TRP A NE1 
839   C CE2 . TRP A 132  ? 0.2877 0.3605 0.2756 -0.0016 0.0112  -0.0279 130  TRP A CE2 
840   C CE3 . TRP A 132  ? 0.3204 0.3913 0.3037 -0.0049 0.0112  -0.0201 130  TRP A CE3 
841   C CZ2 . TRP A 132  ? 0.3183 0.3808 0.3063 -0.0013 0.0110  -0.0252 130  TRP A CZ2 
842   C CZ3 . TRP A 132  ? 0.3121 0.3726 0.2955 -0.0045 0.0109  -0.0178 130  TRP A CZ3 
843   C CH2 . TRP A 132  ? 0.3157 0.3724 0.3013 -0.0027 0.0108  -0.0203 130  TRP A CH2 
844   N N   . LYS A 133  ? 0.4683 0.5627 0.4489 -0.0092 0.0123  -0.0166 131  LYS A N   
845   C CA  . LYS A 133  ? 0.5179 0.6042 0.4977 -0.0108 0.0119  -0.0109 131  LYS A CA  
846   C C   . LYS A 133  ? 0.6185 0.7111 0.5966 -0.0140 0.0118  -0.0053 131  LYS A C   
847   O O   . LYS A 133  ? 0.6829 0.7696 0.6604 -0.0155 0.0111  -0.0006 131  LYS A O   
848   C CB  . LYS A 133  ? 0.5010 0.5833 0.4822 -0.0101 0.0120  -0.0115 131  LYS A CB  
849   N N   . SER A 134  ? 0.6686 0.7737 0.6465 -0.0152 0.0124  -0.0057 132  SER A N   
850   C CA  . SER A 134  ? 0.7032 0.8155 0.6800 -0.0185 0.0122  0.0002  132  SER A CA  
851   C C   . SER A 134  ? 0.7144 0.8272 0.6898 -0.0197 0.0116  0.0032  132  SER A C   
852   O O   . SER A 134  ? 0.7643 0.8785 0.7394 -0.0225 0.0110  0.0094  132  SER A O   
853   C CB  . SER A 134  ? 0.6787 0.8057 0.6554 -0.0192 0.0131  -0.0013 132  SER A CB  
854   O OG  . SER A 134  ? 0.7158 0.8428 0.6941 -0.0178 0.0136  -0.0046 132  SER A OG  
855   N N   . HIS A 135  ? 0.7029 0.8144 0.6778 -0.0178 0.0117  -0.0008 133  HIS A N   
856   C CA  . HIS A 135  ? 0.6748 0.7881 0.6485 -0.0189 0.0112  0.0015  133  HIS A CA  
857   C C   . HIS A 135  ? 0.7160 0.8166 0.6899 -0.0178 0.0105  0.0020  133  HIS A C   
858   O O   . HIS A 135  ? 0.7328 0.8330 0.7059 -0.0191 0.0099  0.0054  133  HIS A O   
859   C CB  . HIS A 135  ? 0.6648 0.7894 0.6378 -0.0180 0.0118  -0.0032 133  HIS A CB  
860   C CG  . HIS A 135  ? 0.7245 0.8626 0.6973 -0.0186 0.0126  -0.0048 133  HIS A CG  
861   N ND1 . HIS A 135  ? 0.7191 0.8585 0.6934 -0.0165 0.0133  -0.0101 133  HIS A ND1 
862   C CD2 . HIS A 135  ? 0.6732 0.8245 0.6446 -0.0210 0.0129  -0.0016 133  HIS A CD2 
863   C CE1 . HIS A 135  ? 0.7743 0.9272 0.7482 -0.0175 0.0140  -0.0104 133  HIS A CE1 
864   N NE2 . HIS A 135  ? 0.7868 0.9475 0.7589 -0.0203 0.0138  -0.0052 133  HIS A NE2 
865   N N   . LEU A 136  ? 0.6744 0.7653 0.6495 -0.0155 0.0106  -0.0012 134  LEU A N   
866   C CA  . LEU A 136  ? 0.6742 0.7534 0.6496 -0.0145 0.0100  -0.0006 134  LEU A CA  
867   C C   . LEU A 136  ? 0.7497 0.8187 0.7261 -0.0136 0.0099  0.0000  134  LEU A C   
868   O O   . LEU A 136  ? 0.7806 0.8406 0.7571 -0.0136 0.0093  0.0025  134  LEU A O   
869   C CB  . LEU A 136  ? 0.6330 0.7113 0.6091 -0.0121 0.0102  -0.0060 134  LEU A CB  
870   C CG  . LEU A 136  ? 0.5910 0.6779 0.5662 -0.0126 0.0101  -0.0072 134  LEU A CG  
871   C CD1 . LEU A 136  ? 0.5285 0.6148 0.5053 -0.0099 0.0101  -0.0136 134  LEU A CD1 
872   C CD2 . LEU A 136  ? 0.5273 0.6112 0.5013 -0.0142 0.0094  -0.0022 134  LEU A CD2 
873   N N   . SER A 139  ? 0.5399 0.5771 0.5195 -0.0183 0.0054  0.0189  137  SER A N   
874   C CA  . SER A 139  ? 0.5450 0.5730 0.5256 -0.0179 0.0043  0.0206  137  SER A CA  
875   C C   . SER A 139  ? 0.5418 0.5630 0.5215 -0.0151 0.0050  0.0171  137  SER A C   
876   O O   . SER A 139  ? 0.5213 0.5349 0.5016 -0.0140 0.0044  0.0171  137  SER A O   
877   C CB  . SER A 139  ? 0.5515 0.5806 0.5330 -0.0199 0.0030  0.0250  137  SER A CB  
878   N N   . ARG A 140  ? 0.3935 0.4177 0.3719 -0.0139 0.0061  0.0140  138  ARG A N   
879   C CA  . ARG A 140  ? 0.4101 0.4288 0.3882 -0.0115 0.0067  0.0109  138  ARG A CA  
880   C C   . ARG A 140  ? 0.3883 0.4103 0.3663 -0.0101 0.0077  0.0067  138  ARG A C   
881   O O   . ARG A 140  ? 0.3814 0.4109 0.3590 -0.0106 0.0081  0.0054  138  ARG A O   
882   C CB  . ARG A 140  ? 0.4451 0.4639 0.4229 -0.0117 0.0065  0.0116  138  ARG A CB  
883   C CG  . ARG A 140  ? 0.4634 0.4782 0.4411 -0.0094 0.0071  0.0084  138  ARG A CG  
884   C CD  . ARG A 140  ? 0.5469 0.5638 0.5244 -0.0099 0.0070  0.0089  138  ARG A CD  
885   N NE  . ARG A 140  ? 0.5615 0.5756 0.5395 -0.0080 0.0075  0.0059  138  ARG A NE  
886   C CZ  . ARG A 140  ? 0.6051 0.6234 0.5835 -0.0071 0.0079  0.0023  138  ARG A CZ  
887   N NH1 . ARG A 140  ? 0.5720 0.5978 0.5501 -0.0078 0.0082  0.0009  138  ARG A NH1 
888   N NH2 . ARG A 140  ? 0.5532 0.5684 0.5328 -0.0056 0.0081  0.0001  138  ARG A NH2 
889   N N   . SER A 141  ? 0.3506 0.3672 0.3290 -0.0081 0.0080  0.0045  139  SER A N   
890   C CA  . SER A 141  ? 0.2835 0.3023 0.2625 -0.0066 0.0087  0.0005  139  SER A CA  
891   C C   . SER A 141  ? 0.2875 0.3090 0.2668 -0.0059 0.0090  -0.0019 139  SER A C   
892   O O   . SER A 141  ? 0.2858 0.3039 0.2650 -0.0057 0.0088  -0.0010 139  SER A O   
893   C CB  . SER A 141  ? 0.3001 0.3120 0.2798 -0.0046 0.0088  -0.0008 139  SER A CB  
894   O OG  . SER A 141  ? 0.2847 0.2981 0.2658 -0.0029 0.0092  -0.0045 139  SER A OG  
895   N N   . LEU A 142  ? 0.2809 0.3089 0.2610 -0.0055 0.0094  -0.0051 140  LEU A N   
896   C CA  . LEU A 142  ? 0.2642 0.2945 0.2453 -0.0045 0.0094  -0.0083 140  LEU A CA  
897   C C   . LEU A 142  ? 0.2396 0.2623 0.2224 -0.0025 0.0093  -0.0097 140  LEU A C   
898   O O   . LEU A 142  ? 0.2571 0.2794 0.2409 -0.0018 0.0091  -0.0112 140  LEU A O   
899   C CB  . LEU A 142  ? 0.2814 0.3191 0.2638 -0.0038 0.0097  -0.0124 140  LEU A CB  
900   C CG  . LEU A 142  ? 0.3607 0.4068 0.3430 -0.0042 0.0097  -0.0147 140  LEU A CG  
901   C CD1 . LEU A 142  ? 0.3872 0.4392 0.3670 -0.0067 0.0098  -0.0108 140  LEU A CD1 
902   C CD2 . LEU A 142  ? 0.3438 0.3962 0.3281 -0.0029 0.0099  -0.0196 140  LEU A CD2 
903   N N   . PHE A 143  ? 0.2273 0.2442 0.2105 -0.0016 0.0093  -0.0091 141  PHE A N   
904   C CA  . PHE A 143  ? 0.2184 0.2296 0.2037 0.0004  0.0092  -0.0106 141  PHE A CA  
905   C C   . PHE A 143  ? 0.2380 0.2421 0.2224 0.0005  0.0091  -0.0075 141  PHE A C   
906   O O   . PHE A 143  ? 0.2406 0.2399 0.2264 0.0020  0.0091  -0.0078 141  PHE A O   
907   C CB  . PHE A 143  ? 0.2054 0.2164 0.1921 0.0015  0.0092  -0.0124 141  PHE A CB  
908   C CG  . PHE A 143  ? 0.2145 0.2330 0.2023 0.0014  0.0093  -0.0156 141  PHE A CG  
909   C CD1 . PHE A 143  ? 0.2074 0.2299 0.1973 0.0022  0.0090  -0.0192 141  PHE A CD1 
910   C CD2 . PHE A 143  ? 0.2176 0.2397 0.2043 0.0006  0.0096  -0.0152 141  PHE A CD2 
911   C CE1 . PHE A 143  ? 0.2142 0.2444 0.2051 0.0023  0.0091  -0.0226 141  PHE A CE1 
912   C CE2 . PHE A 143  ? 0.2194 0.2493 0.2071 0.0006  0.0097  -0.0182 141  PHE A CE2 
913   C CZ  . PHE A 143  ? 0.1996 0.2337 0.1893 0.0016  0.0095  -0.0221 141  PHE A CZ  
914   N N   . VAL A 144  ? 0.2406 0.2444 0.2230 -0.0009 0.0091  -0.0046 142  VAL A N   
915   C CA  A VAL A 144  ? 0.2556 0.2532 0.2373 -0.0006 0.0090  -0.0021 142  VAL A CA  
916   C CA  B VAL A 144  ? 0.2554 0.2531 0.2371 -0.0006 0.0090  -0.0021 142  VAL A CA  
917   C C   . VAL A 144  ? 0.2611 0.2553 0.2446 0.0008  0.0090  -0.0031 142  VAL A C   
918   O O   . VAL A 144  ? 0.2900 0.2791 0.2736 0.0018  0.0091  -0.0020 142  VAL A O   
919   C CB  A VAL A 144  ? 0.2723 0.2704 0.2525 -0.0023 0.0086  0.0009  142  VAL A CB  
920   C CB  B VAL A 144  ? 0.2689 0.2674 0.2491 -0.0024 0.0086  0.0008  142  VAL A CB  
921   C CG1 A VAL A 144  ? 0.2969 0.2977 0.2762 -0.0038 0.0083  0.0024  142  VAL A CG1 
922   C CG1 B VAL A 144  ? 0.2677 0.2603 0.2477 -0.0018 0.0084  0.0028  142  VAL A CG1 
923   C CG2 A VAL A 144  ? 0.2823 0.2847 0.2626 -0.0031 0.0085  0.0005  142  VAL A CG2 
924   C CG2 B VAL A 144  ? 0.2948 0.2956 0.2740 -0.0038 0.0083  0.0026  142  VAL A CG2 
925   N N   . ASN A 145  ? 0.2517 0.2488 0.2366 0.0009  0.0089  -0.0051 143  ASN A N   
926   C CA  . ASN A 145  ? 0.2587 0.2526 0.2457 0.0021  0.0088  -0.0059 143  ASN A CA  
927   C C   . ASN A 145  ? 0.2554 0.2495 0.2458 0.0035  0.0085  -0.0089 143  ASN A C   
928   O O   . ASN A 145  ? 0.2546 0.2477 0.2478 0.0043  0.0081  -0.0102 143  ASN A O   
929   C CB  . ASN A 145  ? 0.2958 0.2921 0.2829 0.0014  0.0085  -0.0060 143  ASN A CB  
930   C CG  . ASN A 145  ? 0.2895 0.2841 0.2742 0.0002  0.0086  -0.0026 143  ASN A CG  
931   O OD1 . ASN A 145  ? 0.3472 0.3369 0.3317 0.0008  0.0087  -0.0006 143  ASN A OD1 
932   N ND2 . ASN A 145  ? 0.3341 0.3332 0.3175 -0.0013 0.0083  -0.0019 143  ASN A ND2 
933   N N   . ALA A 146  ? 0.2342 0.2296 0.2248 0.0039  0.0086  -0.0100 144  ALA A N   
934   C CA  . ALA A 146  ? 0.2345 0.2303 0.2288 0.0053  0.0081  -0.0131 144  ALA A CA  
935   C C   . ALA A 146  ? 0.2238 0.2141 0.2208 0.0065  0.0077  -0.0121 144  ALA A C   
936   O O   . ALA A 146  ? 0.2643 0.2545 0.2656 0.0076  0.0070  -0.0143 144  ALA A O   
937   C CB  . ALA A 146  ? 0.2358 0.2340 0.2298 0.0054  0.0082  -0.0142 144  ALA A CB  
938   N N   . ALA A 147  ? 0.2433 0.2294 0.2384 0.0065  0.0082  -0.0087 145  ALA A N   
939   C CA  . ALA A 147  ? 0.2801 0.2621 0.2778 0.0076  0.0079  -0.0074 145  ALA A CA  
940   C C   . ALA A 147  ? 0.2518 0.2334 0.2524 0.0077  0.0074  -0.0080 145  ALA A C   
941   O O   . ALA A 147  ? 0.2780 0.2579 0.2830 0.0086  0.0067  -0.0085 145  ALA A O   
942   C CB  . ALA A 147  ? 0.3316 0.3103 0.3265 0.0076  0.0086  -0.0039 145  ALA A CB  
943   N N   . THR A 148  ? 0.2521 0.2353 0.2506 0.0067  0.0077  -0.0079 146  THR A N   
944   C CA  . THR A 148  ? 0.2475 0.2308 0.2487 0.0067  0.0072  -0.0088 146  THR A CA  
945   C C   . THR A 148  ? 0.2198 0.2063 0.2250 0.0072  0.0062  -0.0130 146  THR A C   
946   O O   . THR A 148  ? 0.2469 0.2319 0.2568 0.0080  0.0052  -0.0141 146  THR A O   
947   C CB  . THR A 148  ? 0.3077 0.2926 0.3057 0.0055  0.0076  -0.0077 146  THR A CB  
948   O OG1 . THR A 148  ? 0.3244 0.3061 0.3194 0.0052  0.0083  -0.0043 146  THR A OG1 
949   C CG2 . THR A 148  ? 0.3633 0.3483 0.3638 0.0055  0.0070  -0.0086 146  THR A CG2 
950   N N   . TRP A 149  ? 0.2409 0.2322 0.2445 0.0068  0.0063  -0.0154 147  TRP A N   
951   C CA  . TRP A 149  ? 0.2354 0.2305 0.2430 0.0076  0.0053  -0.0200 147  TRP A CA  
952   C C   . TRP A 149  ? 0.2234 0.2159 0.2357 0.0090  0.0044  -0.0212 147  TRP A C   
953   O O   . TRP A 149  ? 0.2308 0.2241 0.2483 0.0100  0.0031  -0.0245 147  TRP A O   
954   C CB  . TRP A 149  ? 0.2257 0.2273 0.2305 0.0069  0.0057  -0.0222 147  TRP A CB  
955   C CG  . TRP A 149  ? 0.2320 0.2373 0.2335 0.0055  0.0061  -0.0215 147  TRP A CG  
956   C CD1 . TRP A 149  ? 0.2670 0.2741 0.2637 0.0041  0.0070  -0.0187 147  TRP A CD1 
957   C CD2 . TRP A 149  ? 0.2569 0.2644 0.2598 0.0054  0.0055  -0.0233 147  TRP A CD2 
958   N NE1 . TRP A 149  ? 0.2616 0.2721 0.2567 0.0030  0.0069  -0.0184 147  TRP A NE1 
959   C CE2 . TRP A 149  ? 0.2680 0.2789 0.2665 0.0038  0.0061  -0.0213 147  TRP A CE2 
960   C CE3 . TRP A 149  ? 0.2518 0.2589 0.2596 0.0065  0.0043  -0.0264 147  TRP A CE3 
961   C CZ2 . TRP A 149  ? 0.2730 0.2873 0.2716 0.0033  0.0056  -0.0223 147  TRP A CZ2 
962   C CZ3 . TRP A 149  ? 0.3015 0.3117 0.3094 0.0060  0.0038  -0.0277 147  TRP A CZ3 
963   C CH2 . TRP A 149  ? 0.3296 0.3435 0.3327 0.0045  0.0046  -0.0256 147  TRP A CH2 
964   N N   . GLY A 150  ? 0.2205 0.2100 0.2313 0.0092  0.0050  -0.0185 148  GLY A N   
965   C CA  . GLY A 150  ? 0.2486 0.2353 0.2641 0.0105  0.0040  -0.0188 148  GLY A CA  
966   C C   . GLY A 150  ? 0.2598 0.2427 0.2800 0.0110  0.0031  -0.0176 148  GLY A C   
967   O O   . GLY A 150  ? 0.2610 0.2432 0.2874 0.0120  0.0016  -0.0195 148  GLY A O   
968   N N   . LEU A 151  ? 0.2638 0.2444 0.2817 0.0103  0.0038  -0.0142 149  LEU A N   
969   C CA  . LEU A 151  ? 0.2938 0.2713 0.3161 0.0106  0.0030  -0.0128 149  LEU A CA  
970   C C   . LEU A 151  ? 0.2685 0.2481 0.2956 0.0108  0.0016  -0.0168 149  LEU A C   
971   O O   . LEU A 151  ? 0.3158 0.2935 0.3495 0.0116  0.0000  -0.0176 149  LEU A O   
972   C CB  . LEU A 151  ? 0.3478 0.3233 0.3663 0.0098  0.0041  -0.0089 149  LEU A CB  
973   C CG  . LEU A 151  ? 0.4339 0.4060 0.4555 0.0099  0.0038  -0.0055 149  LEU A CG  
974   C CD1 . LEU A 151  ? 0.3231 0.2931 0.3480 0.0107  0.0032  -0.0035 149  LEU A CD1 
975   C CD2 . LEU A 151  ? 0.4508 0.4219 0.4673 0.0093  0.0053  -0.0021 149  LEU A CD2 
976   N N   . VAL A 152  ? 0.2554 0.2391 0.2795 0.0102  0.0020  -0.0195 150  VAL A N   
977   C CA  . VAL A 152  ? 0.2772 0.2639 0.3054 0.0106  0.0006  -0.0239 150  VAL A CA  
978   C C   . VAL A 152  ? 0.3009 0.2892 0.3348 0.0119  -0.0009 -0.0284 150  VAL A C   
979   O O   . VAL A 152  ? 0.3244 0.3122 0.3650 0.0127  -0.0027 -0.0310 150  VAL A O   
980   C CB  . VAL A 152  ? 0.2862 0.2781 0.3093 0.0096  0.0015  -0.0256 150  VAL A CB  
981   C CG1 . VAL A 152  ? 0.3187 0.3153 0.3457 0.0101  0.0001  -0.0310 150  VAL A CG1 
982   C CG2 . VAL A 152  ? 0.3260 0.3160 0.3451 0.0084  0.0025  -0.0216 150  VAL A CG2 
983   N N   . VAL A 153  ? 0.2745 0.2650 0.3063 0.0122  -0.0004 -0.0294 151  VAL A N   
984   C CA  . VAL A 153  ? 0.2927 0.2856 0.3296 0.0135  -0.0018 -0.0341 151  VAL A CA  
985   C C   . VAL A 153  ? 0.2912 0.2791 0.3344 0.0146  -0.0031 -0.0326 151  VAL A C   
986   O O   . VAL A 153  ? 0.3394 0.3272 0.3902 0.0157  -0.0052 -0.0361 151  VAL A O   
987   C CB  . VAL A 153  ? 0.2765 0.2742 0.3089 0.0134  -0.0006 -0.0357 151  VAL A CB  
988   C CG1 . VAL A 153  ? 0.3043 0.3044 0.3422 0.0150  -0.0020 -0.0404 151  VAL A CG1 
989   C CG2 . VAL A 153  ? 0.2808 0.2846 0.3083 0.0124  0.0004  -0.0373 151  VAL A CG2 
990   N N   . THR A 154  ? 0.3085 0.2924 0.3491 0.0141  -0.0022 -0.0275 152  THR A N   
991   C CA  . THR A 154  ? 0.3151 0.2953 0.3609 0.0150  -0.0034 -0.0257 152  THR A CA  
992   C C   . THR A 154  ? 0.3491 0.3245 0.3976 0.0147  -0.0038 -0.0209 152  THR A C   
993   O O   . THR A 154  ? 0.3519 0.3245 0.4063 0.0153  -0.0053 -0.0193 152  THR A O   
994   C CB  . THR A 154  ? 0.3397 0.3198 0.3809 0.0150  -0.0022 -0.0234 152  THR A CB  
995   O OG1 . THR A 154  ? 0.3510 0.3288 0.3861 0.0139  -0.0004 -0.0183 152  THR A OG1 
996   C CG2 . THR A 154  ? 0.3318 0.3171 0.3692 0.0150  -0.0013 -0.0272 152  THR A CG2 
997   N N   . GLY A 155  ? 0.3334 0.3080 0.3781 0.0136  -0.0027 -0.0184 153  GLY A N   
998   C CA  . GLY A 155  ? 0.3119 0.2827 0.3584 0.0132  -0.0028 -0.0135 153  GLY A CA  
999   C C   . GLY A 155  ? 0.3659 0.3349 0.4082 0.0130  -0.0014 -0.0085 153  GLY A C   
1000  O O   . GLY A 155  ? 0.3467 0.3133 0.3903 0.0127  -0.0014 -0.0041 153  GLY A O   
1001  N N   . LYS A 156  ? 0.3377 0.3082 0.3753 0.0131  -0.0004 -0.0090 154  LYS A N   
1002  C CA  . LYS A 156  ? 0.3542 0.3234 0.3878 0.0131  0.0007  -0.0049 154  LYS A CA  
1003  C C   . LYS A 156  ? 0.3829 0.3535 0.4082 0.0123  0.0027  -0.0045 154  LYS A C   
1004  O O   . LYS A 156  ? 0.3310 0.3042 0.3537 0.0119  0.0031  -0.0077 154  LYS A O   
1005  C CB  . LYS A 156  ? 0.4411 0.4107 0.4769 0.0139  -0.0001 -0.0058 154  LYS A CB  
1006  N N   . LEU A 157  ? 0.3389 0.3082 0.3605 0.0120  0.0038  -0.0005 155  LEU A N   
1007  C CA  . LEU A 157  ? 0.3548 0.3250 0.3694 0.0114  0.0054  0.0002  155  LEU A CA  
1008  C C   . LEU A 157  ? 0.4218 0.3924 0.4335 0.0118  0.0058  0.0007  155  LEU A C   
1009  O O   . LEU A 157  ? 0.4393 0.4089 0.4526 0.0124  0.0055  0.0031  155  LEU A O   
1010  C CB  . LEU A 157  ? 0.3772 0.3460 0.3898 0.0111  0.0063  0.0037  155  LEU A CB  
1011  C CG  . LEU A 157  ? 0.4762 0.4455 0.4823 0.0107  0.0076  0.0044  155  LEU A CG  
1012  C CD1 . LEU A 157  ? 0.4335 0.4044 0.4375 0.0098  0.0078  0.0017  155  LEU A CD1 
1013  C CD2 . LEU A 157  ? 0.4660 0.4343 0.4710 0.0107  0.0084  0.0076  155  LEU A CD2 
1014  N N   . THR A 158  ? 0.4791 0.4516 0.4868 0.0113  0.0064  -0.0013 156  THR A N   
1015  C CA  . THR A 158  ? 0.4889 0.4619 0.4933 0.0114  0.0069  -0.0009 156  THR A CA  
1016  C C   . THR A 158  ? 0.5439 0.5172 0.5428 0.0106  0.0080  0.0000  156  THR A C   
1017  O O   . THR A 158  ? 0.5859 0.5607 0.5833 0.0098  0.0082  -0.0016 156  THR A O   
1018  C CB  . THR A 158  ? 0.5131 0.4884 0.5188 0.0116  0.0063  -0.0042 156  THR A CB  
1019  N N   . SER A 159  ? 0.4051 0.3772 0.4012 0.0109  0.0085  0.0024  157  SER A N   
1020  C CA  . SER A 159  ? 0.3519 0.3237 0.3438 0.0103  0.0093  0.0033  157  SER A CA  
1021  C C   . SER A 159  ? 0.3688 0.3422 0.3581 0.0094  0.0093  0.0016  157  SER A C   
1022  O O   . SER A 159  ? 0.4279 0.4015 0.4150 0.0086  0.0096  0.0018  157  SER A O   
1023  C CB  . SER A 159  ? 0.4610 0.4319 0.4510 0.0111  0.0096  0.0057  157  SER A CB  
1024  O OG  . SER A 159  ? 0.4847 0.4562 0.4748 0.0117  0.0093  0.0055  157  SER A OG  
1025  N N   . THR A 160  ? 0.3300 0.3047 0.3197 0.0096  0.0090  0.0003  158  THR A N   
1026  C CA  . THR A 160  ? 0.2956 0.2725 0.2833 0.0086  0.0091  -0.0010 158  THR A CA  
1027  C C   . THR A 160  ? 0.2838 0.2634 0.2739 0.0084  0.0087  -0.0037 158  THR A C   
1028  O O   . THR A 160  ? 0.3285 0.3080 0.3221 0.0093  0.0082  -0.0047 158  THR A O   
1029  C CB  . THR A 160  ? 0.3300 0.3066 0.3156 0.0088  0.0090  -0.0005 158  THR A CB  
1030  O OG1 . THR A 160  ? 0.3517 0.3285 0.3395 0.0098  0.0086  -0.0010 158  THR A OG1 
1031  C CG2 . THR A 160  ? 0.3999 0.3743 0.3833 0.0091  0.0092  0.0015  158  THR A CG2 
1032  N N   . VAL A 161  ? 0.2336 0.2163 0.2221 0.0073  0.0088  -0.0048 159  VAL A N   
1033  C CA  . VAL A 161  ? 0.2311 0.2178 0.2214 0.0070  0.0086  -0.0075 159  VAL A CA  
1034  C C   . VAL A 161  ? 0.2185 0.2076 0.2088 0.0070  0.0085  -0.0087 159  VAL A C   
1035  O O   . VAL A 161  ? 0.2235 0.2129 0.2112 0.0062  0.0087  -0.0075 159  VAL A O   
1036  C CB  . VAL A 161  ? 0.2544 0.2439 0.2427 0.0054  0.0089  -0.0074 159  VAL A CB  
1037  C CG1 . VAL A 161  ? 0.2655 0.2606 0.2550 0.0050  0.0088  -0.0103 159  VAL A CG1 
1038  C CG2 . VAL A 161  ? 0.2952 0.2824 0.2836 0.0054  0.0090  -0.0063 159  VAL A CG2 
1039  N N   . ASN A 162  ? 0.2024 0.1932 0.1960 0.0080  0.0081  -0.0113 160  ASN A N   
1040  C CA  . ASN A 162  ? 0.2002 0.1941 0.1941 0.0080  0.0080  -0.0128 160  ASN A CA  
1041  C C   . ASN A 162  ? 0.1960 0.1958 0.1892 0.0068  0.0083  -0.0147 160  ASN A C   
1042  O O   . ASN A 162  ? 0.2023 0.2057 0.1981 0.0074  0.0080  -0.0179 160  ASN A O   
1043  C CB  . ASN A 162  ? 0.2108 0.2042 0.2089 0.0096  0.0072  -0.0146 160  ASN A CB  
1044  C CG  . ASN A 162  ? 0.2147 0.2111 0.2131 0.0097  0.0071  -0.0160 160  ASN A CG  
1045  O OD1 . ASN A 162  ? 0.2201 0.2201 0.2161 0.0085  0.0076  -0.0163 160  ASN A OD1 
1046  N ND2 . ASN A 162  ? 0.2827 0.2776 0.2841 0.0111  0.0064  -0.0166 160  ASN A ND2 
1047  N N   . ASP A 163  ? 0.1820 0.1830 0.1718 0.0052  0.0087  -0.0127 161  ASP A N   
1048  C CA  . ASP A 163  ? 0.1964 0.2034 0.1852 0.0038  0.0090  -0.0135 161  ASP A CA  
1049  C C   . ASP A 163  ? 0.1926 0.2054 0.1826 0.0038  0.0091  -0.0160 161  ASP A C   
1050  O O   . ASP A 163  ? 0.2061 0.2251 0.1964 0.0033  0.0093  -0.0180 161  ASP A O   
1051  C CB  . ASP A 163  ? 0.2295 0.2361 0.2151 0.0019  0.0092  -0.0101 161  ASP A CB  
1052  C CG  . ASP A 163  ? 0.2472 0.2508 0.2314 0.0016  0.0090  -0.0079 161  ASP A CG  
1053  O OD1 . ASP A 163  ? 0.2335 0.2328 0.2183 0.0030  0.0088  -0.0079 161  ASP A OD1 
1054  O OD2 . ASP A 163  ? 0.2683 0.2740 0.2511 -0.0001 0.0090  -0.0060 161  ASP A OD2 
1055  N N   . ARG A 164  ? 0.1959 0.2072 0.1866 0.0045  0.0089  -0.0161 162  ARG A N   
1056  C CA  A ARG A 164  ? 0.1881 0.2050 0.1804 0.0047  0.0089  -0.0187 162  ARG A CA  
1057  C CA  B ARG A 164  ? 0.1888 0.2058 0.1811 0.0048  0.0089  -0.0187 162  ARG A CA  
1058  C C   . ARG A 164  ? 0.1710 0.1899 0.1673 0.0065  0.0085  -0.0229 162  ARG A C   
1059  O O   . ARG A 164  ? 0.1855 0.2112 0.1831 0.0066  0.0086  -0.0260 162  ARG A O   
1060  C CB  A ARG A 164  ? 0.2149 0.2298 0.2069 0.0049  0.0087  -0.0175 162  ARG A CB  
1061  C CB  B ARG A 164  ? 0.2147 0.2294 0.2068 0.0050  0.0087  -0.0175 162  ARG A CB  
1062  C CG  A ARG A 164  ? 0.2224 0.2366 0.2112 0.0031  0.0088  -0.0141 162  ARG A CG  
1063  C CG  B ARG A 164  ? 0.2265 0.2396 0.2153 0.0033  0.0088  -0.0139 162  ARG A CG  
1064  C CD  A ARG A 164  ? 0.2692 0.2892 0.2566 0.0011  0.0093  -0.0132 162  ARG A CD  
1065  C CD  B ARG A 164  ? 0.2585 0.2781 0.2465 0.0015  0.0091  -0.0137 162  ARG A CD  
1066  N NE  A ARG A 164  ? 0.3208 0.3487 0.3094 0.0009  0.0096  -0.0159 162  ARG A NE  
1067  N NE  B ARG A 164  ? 0.3127 0.3388 0.3006 0.0006  0.0095  -0.0147 162  ARG A NE  
1068  C CZ  A ARG A 164  ? 0.3222 0.3569 0.3101 -0.0005 0.0100  -0.0160 162  ARG A CZ  
1069  C CZ  B ARG A 164  ? 0.3075 0.3337 0.2938 -0.0007 0.0097  -0.0128 162  ARG A CZ  
1070  N NH1 A ARG A 164  ? 0.3513 0.3854 0.3373 -0.0019 0.0101  -0.0134 162  ARG A NH1 
1071  N NH1 B ARG A 164  ? 0.3281 0.3481 0.3129 -0.0010 0.0094  -0.0100 162  ARG A NH1 
1072  N NH2 A ARG A 164  ? 0.2883 0.3309 0.2775 -0.0004 0.0104  -0.0188 162  ARG A NH2 
1073  N NH2 B ARG A 164  ? 0.3484 0.3816 0.3346 -0.0015 0.0101  -0.0139 162  ARG A NH2 
1074  N N   . SER A 165  ? 0.1648 0.1782 0.1634 0.0080  0.0078  -0.0230 163  SER A N   
1075  C CA  . SER A 165  ? 0.1569 0.1714 0.1602 0.0096  0.0071  -0.0269 163  SER A CA  
1076  C C   . SER A 165  ? 0.1783 0.1971 0.1817 0.0092  0.0072  -0.0290 163  SER A C   
1077  O O   . SER A 165  ? 0.1749 0.1991 0.1814 0.0101  0.0068  -0.0333 163  SER A O   
1078  C CB  . SER A 165  ? 0.1911 0.1987 0.1971 0.0110  0.0063  -0.0256 163  SER A CB  
1079  O OG  . SER A 165  ? 0.2125 0.2206 0.2236 0.0123  0.0052  -0.0290 163  SER A OG  
1080  N N   . LEU A 166  ? 0.1816 0.1984 0.1819 0.0080  0.0077  -0.0262 164  LEU A N   
1081  C CA  . LEU A 166  ? 0.1774 0.1985 0.1775 0.0074  0.0078  -0.0279 164  LEU A CA  
1082  C C   . LEU A 166  ? 0.1722 0.2021 0.1704 0.0063  0.0084  -0.0293 164  LEU A C   
1083  O O   . LEU A 166  ? 0.1782 0.2142 0.1780 0.0066  0.0083  -0.0329 164  LEU A O   
1084  C CB  . LEU A 166  ? 0.1750 0.1920 0.1722 0.0063  0.0081  -0.0241 164  LEU A CB  
1085  C CG  . LEU A 166  ? 0.1770 0.1867 0.1765 0.0075  0.0075  -0.0232 164  LEU A CG  
1086  C CD1 . LEU A 166  ? 0.2088 0.2147 0.2053 0.0065  0.0080  -0.0194 164  LEU A CD1 
1087  C CD2 . LEU A 166  ? 0.2122 0.2230 0.2164 0.0088  0.0066  -0.0270 164  LEU A CD2 
1088  N N   . ALA A 167  ? 0.1728 0.2040 0.1681 0.0048  0.0090  -0.0264 165  ALA A N   
1089  C CA  . ALA A 167  ? 0.1855 0.2258 0.1793 0.0035  0.0096  -0.0272 165  ALA A CA  
1090  C C   . ALA A 167  ? 0.1952 0.2413 0.1923 0.0050  0.0094  -0.0323 165  ALA A C   
1091  O O   . ALA A 167  ? 0.1967 0.2515 0.1941 0.0049  0.0096  -0.0352 165  ALA A O   
1092  C CB  . ALA A 167  ? 0.2118 0.2517 0.2025 0.0017  0.0101  -0.0231 165  ALA A CB  
1093  N N   . ALA A 168  ? 0.1787 0.2208 0.1785 0.0066  0.0089  -0.0334 166  ALA A N   
1094  C CA  . ALA A 168  ? 0.1770 0.2241 0.1808 0.0083  0.0085  -0.0384 166  ALA A CA  
1095  C C   . ALA A 168  ? 0.1742 0.2235 0.1817 0.0098  0.0077  -0.0431 166  ALA A C   
1096  O O   . ALA A 168  ? 0.1780 0.2357 0.1874 0.0105  0.0076  -0.0477 166  ALA A O   
1097  C CB  . ALA A 168  ? 0.1832 0.2243 0.1896 0.0097  0.0078  -0.0382 166  ALA A CB  
1098  N N   . ALA A 169  ? 0.1743 0.2165 0.1830 0.0104  0.0070  -0.0421 167  ALA A N   
1099  C CA  . ALA A 169  ? 0.1598 0.2033 0.1726 0.0118  0.0060  -0.0465 167  ALA A CA  
1100  C C   . ALA A 169  ? 0.1714 0.2229 0.1820 0.0108  0.0065  -0.0482 167  ALA A C   
1101  O O   . ALA A 169  ? 0.1724 0.2298 0.1863 0.0121  0.0059  -0.0536 167  ALA A O   
1102  C CB  . ALA A 169  ? 0.1831 0.2173 0.1972 0.0122  0.0053  -0.0440 167  ALA A CB  
1103  N N   . LEU A 170  ? 0.1662 0.2183 0.1714 0.0086  0.0076  -0.0437 168  LEU A N   
1104  C CA  . LEU A 170  ? 0.1704 0.2307 0.1733 0.0074  0.0081  -0.0446 168  LEU A CA  
1105  C C   . LEU A 170  ? 0.1765 0.2480 0.1792 0.0073  0.0086  -0.0478 168  LEU A C   
1106  O O   . LEU A 170  ? 0.1783 0.2580 0.1823 0.0080  0.0084  -0.0522 168  LEU A O   
1107  C CB  . LEU A 170  ? 0.2017 0.2596 0.1994 0.0050  0.0089  -0.0384 168  LEU A CB  
1108  C CG  . LEU A 170  ? 0.1885 0.2539 0.1838 0.0036  0.0092  -0.0384 168  LEU A CG  
1109  C CD1 . LEU A 170  ? 0.2089 0.2742 0.2074 0.0052  0.0083  -0.0426 168  LEU A CD1 
1110  C CD2 . LEU A 170  ? 0.2061 0.2677 0.1974 0.0014  0.0097  -0.0322 168  LEU A CD2 
1111  N N   . THR A 171  ? 0.1816 0.2541 0.1830 0.0066  0.0093  -0.0457 169  THR A N   
1112  C CA  . THR A 171  ? 0.1888 0.2722 0.1904 0.0066  0.0098  -0.0487 169  THR A CA  
1113  C C   . THR A 171  ? 0.1769 0.2639 0.1841 0.0094  0.0089  -0.0560 169  THR A C   
1114  O O   . THR A 171  ? 0.1932 0.2908 0.2012 0.0099  0.0090  -0.0605 169  THR A O   
1115  C CB  . THR A 171  ? 0.2076 0.2898 0.2080 0.0057  0.0104  -0.0455 169  THR A CB  
1116  O OG1 . THR A 171  ? 0.2454 0.3248 0.2412 0.0031  0.0110  -0.0390 169  THR A OG1 
1117  C CG2 . THR A 171  ? 0.2151 0.3085 0.2162 0.0058  0.0110  -0.0487 169  THR A CG2 
1118  N N   . ARG A 172  ? 0.1784 0.2567 0.1898 0.0113  0.0077  -0.0574 170  ARG A N   
1119  C CA  . ARG A 172  ? 0.1800 0.2606 0.1976 0.0141  0.0065  -0.0642 170  ARG A CA  
1120  C C   . ARG A 172  ? 0.1864 0.2711 0.2063 0.0150  0.0056  -0.0688 170  ARG A C   
1121  O O   . ARG A 172  ? 0.1800 0.2736 0.2030 0.0165  0.0052  -0.0751 170  ARG A O   
1122  C CB  . ARG A 172  ? 0.1680 0.2378 0.1899 0.0156  0.0052  -0.0635 170  ARG A CB  
1123  C CG  . ARG A 172  ? 0.1713 0.2433 0.2004 0.0184  0.0037  -0.0700 170  ARG A CG  
1124  C CD  . ARG A 172  ? 0.1975 0.2586 0.2314 0.0198  0.0021  -0.0689 170  ARG A CD  
1125  N NE  . ARG A 172  ? 0.1702 0.2246 0.2004 0.0185  0.0029  -0.0626 170  ARG A NE  
1126  C CZ  . ARG A 172  ? 0.1802 0.2263 0.2078 0.0174  0.0031  -0.0573 170  ARG A CZ  
1127  N NH1 . ARG A 172  ? 0.1802 0.2231 0.2082 0.0173  0.0027  -0.0569 170  ARG A NH1 
1128  N NH2 . ARG A 172  ? 0.1834 0.2246 0.2078 0.0164  0.0038  -0.0524 170  ARG A NH2 
1129  N N   . LEU A 173  ? 0.1809 0.2595 0.1994 0.0143  0.0054  -0.0660 171  LEU A N   
1130  C CA  . LEU A 173  ? 0.1731 0.2547 0.1945 0.0153  0.0043  -0.0705 171  LEU A CA  
1131  C C   . LEU A 173  ? 0.1762 0.2702 0.1939 0.0143  0.0053  -0.0723 171  LEU A C   
1132  O O   . LEU A 173  ? 0.1937 0.2951 0.2146 0.0158  0.0045  -0.0786 171  LEU A O   
1133  C CB  . LEU A 173  ? 0.1993 0.2711 0.2206 0.0149  0.0037  -0.0671 171  LEU A CB  
1134  C CG  . LEU A 173  ? 0.2054 0.2756 0.2202 0.0123  0.0050  -0.0609 171  LEU A CG  
1135  C CD1 . LEU A 173  ? 0.2189 0.2966 0.2324 0.0118  0.0050  -0.0632 171  LEU A CD1 
1136  C CD2 . LEU A 173  ? 0.2029 0.2609 0.2180 0.0121  0.0046  -0.0564 171  LEU A CD2 
1137  N N   . ILE A 174  ? 0.1831 0.2800 0.1945 0.0117  0.0069  -0.0668 172  ILE A N   
1138  C CA  . ILE A 174  ? 0.1740 0.2835 0.1819 0.0104  0.0078  -0.0676 172  ILE A CA  
1139  C C   . ILE A 174  ? 0.1875 0.3084 0.1974 0.0116  0.0081  -0.0730 172  ILE A C   
1140  O O   . ILE A 174  ? 0.1898 0.3217 0.2004 0.0124  0.0079  -0.0781 172  ILE A O   
1141  C CB  . ILE A 174  ? 0.1897 0.2993 0.1912 0.0072  0.0092  -0.0599 172  ILE A CB  
1142  C CG1 . ILE A 174  ? 0.2157 0.3163 0.2154 0.0061  0.0089  -0.0555 172  ILE A CG1 
1143  C CG2 . ILE A 174  ? 0.2324 0.3567 0.2308 0.0057  0.0101  -0.0604 172  ILE A CG2 
1144  C CD1 . ILE A 174  ? 0.2390 0.3376 0.2336 0.0032  0.0099  -0.0478 172  ILE A CD1 
1145  N N   . SER A 175  ? 0.1950 0.3138 0.2058 0.0119  0.0084  -0.0722 173  SER A N   
1146  C CA  . SER A 175  ? 0.1685 0.2983 0.1815 0.0131  0.0087  -0.0773 173  SER A CA  
1147  C C   . SER A 175  ? 0.2025 0.3342 0.2223 0.0164  0.0070  -0.0860 173  SER A C   
1148  O O   . SER A 175  ? 0.2312 0.3747 0.2528 0.0177  0.0071  -0.0919 173  SER A O   
1149  C CB  . SER A 175  ? 0.2276 0.3540 0.2404 0.0127  0.0093  -0.0744 173  SER A CB  
1150  O OG  . SER A 175  ? 0.2608 0.3873 0.2678 0.0096  0.0107  -0.0670 173  SER A OG  
1151  N N   . ARG A 176  ? 0.1997 0.3203 0.2237 0.0179  0.0054  -0.0869 174  ARG A N   
1152  C CA  . ARG A 176  ? 0.1952 0.3169 0.2269 0.0211  0.0034  -0.0951 174  ARG A CA  
1153  C C   . ARG A 176  ? 0.2384 0.3662 0.2707 0.0216  0.0027  -0.0994 174  ARG A C   
1154  O O   . ARG A 176  ? 0.2455 0.3824 0.2820 0.0238  0.0017  -0.1073 174  ARG A O   
1155  C CB  . ARG A 176  ? 0.2388 0.3462 0.2755 0.0223  0.0018  -0.0938 174  ARG A CB  
1156  C CG  . ARG A 176  ? 0.2139 0.3208 0.2599 0.0256  -0.0007 -0.1016 174  ARG A CG  
1157  C CD  . ARG A 176  ? 0.2310 0.3237 0.2816 0.0264  -0.0022 -0.0987 174  ARG A CD  
1158  N NE  . ARG A 176  ? 0.2263 0.3104 0.2764 0.0255  -0.0028 -0.0950 174  ARG A NE  
1159  C CZ  . ARG A 176  ? 0.2367 0.3113 0.2826 0.0236  -0.0019 -0.0873 174  ARG A CZ  
1160  N NH1 . ARG A 176  ? 0.2153 0.2868 0.2574 0.0224  -0.0006 -0.0823 174  ARG A NH1 
1161  N NH2 . ARG A 176  ? 0.2703 0.3387 0.3161 0.0229  -0.0024 -0.0848 174  ARG A NH2 
1162  N N   . CYS A 177  ? 0.2281 0.3516 0.2563 0.0197  0.0031  -0.0946 175  CYS A N   
1163  C CA  . CYS A 177  ? 0.2394 0.3662 0.2690 0.0204  0.0020  -0.0984 175  CYS A CA  
1164  C C   . CYS A 177  ? 0.2489 0.3850 0.2717 0.0181  0.0035  -0.0958 175  CYS A C   
1165  O O   . CYS A 177  ? 0.2840 0.4258 0.3078 0.0187  0.0027  -0.0999 175  CYS A O   
1166  C CB  . CYS A 177  ? 0.2636 0.3767 0.2958 0.0205  0.0007  -0.0959 175  CYS A CB  
1167  S SG  . CYS A 177  ? 0.2997 0.4011 0.3405 0.0230  -0.0014 -0.0979 175  CYS A SG  
1168  N N   . GLY A 178  ? 0.2461 0.3837 0.2625 0.0154  0.0054  -0.0889 176  GLY A N   
1169  C CA  . GLY A 178  ? 0.2334 0.3819 0.2438 0.0131  0.0067  -0.0864 176  GLY A CA  
1170  C C   . GLY A 178  ? 0.2129 0.3582 0.2209 0.0119  0.0064  -0.0835 176  GLY A C   
1171  O O   . GLY A 178  ? 0.2371 0.3700 0.2463 0.0119  0.0056  -0.0809 176  GLY A O   
1172  N N   . GLU A 179  ? 0.2257 0.3835 0.2302 0.0107  0.0070  -0.0840 177  GLU A N   
1173  C CA  . GLU A 179  ? 0.2326 0.3895 0.2342 0.0093  0.0067  -0.0810 177  GLU A CA  
1174  C C   . GLU A 179  ? 0.2063 0.3555 0.2127 0.0113  0.0048  -0.0853 177  GLU A C   
1175  O O   . GLU A 179  ? 0.2410 0.3814 0.2458 0.0101  0.0046  -0.0806 177  GLU A O   
1176  C CB  . GLU A 179  ? 0.2589 0.4325 0.2566 0.0081  0.0075  -0.0819 177  GLU A CB  
1177  C CG  . GLU A 179  ? 0.3559 0.5297 0.3499 0.0061  0.0073  -0.0776 177  GLU A CG  
1178  C CD  . GLU A 179  ? 0.4761 0.6516 0.4734 0.0081  0.0057  -0.0841 177  GLU A CD  
1179  O OE1 . GLU A 179  ? 0.4789 0.6597 0.4809 0.0109  0.0047  -0.0928 177  GLU A OE1 
1180  O OE2 . GLU A 179  ? 0.5316 0.7030 0.5270 0.0069  0.0053  -0.0808 177  GLU A OE2 
1181  N N   . PRO A 180  ? 0.2181 0.3699 0.2307 0.0143  0.0033  -0.0939 178  PRO A N   
1182  C CA  . PRO A 180  ? 0.2306 0.3750 0.2483 0.0159  0.0013  -0.0974 178  PRO A CA  
1183  C C   . PRO A 180  ? 0.2220 0.3495 0.2411 0.0155  0.0009  -0.0921 178  PRO A C   
1184  O O   . PRO A 180  ? 0.2296 0.3510 0.2493 0.0152  0.0001  -0.0906 178  PRO A O   
1185  C CB  . PRO A 180  ? 0.2559 0.4053 0.2808 0.0193  -0.0004 -0.1074 178  PRO A CB  
1186  C CG  . PRO A 180  ? 0.2524 0.4175 0.2744 0.0192  0.0009  -0.1101 178  PRO A CG  
1187  C CD  . PRO A 180  ? 0.2235 0.3871 0.2389 0.0163  0.0032  -0.1013 178  PRO A CD  
1188  N N   . VAL A 181  ? 0.2199 0.3403 0.2394 0.0155  0.0015  -0.0890 179  VAL A N   
1189  C CA  . VAL A 181  ? 0.2158 0.3214 0.2366 0.0151  0.0012  -0.0840 179  VAL A CA  
1190  C C   . VAL A 181  ? 0.2110 0.3125 0.2251 0.0122  0.0026  -0.0757 179  VAL A C   
1191  O O   . VAL A 181  ? 0.1981 0.2898 0.2128 0.0118  0.0021  -0.0723 179  VAL A O   
1192  C CB  . VAL A 181  ? 0.2051 0.3043 0.2288 0.0161  0.0011  -0.0836 179  VAL A CB  
1193  C CG1 . VAL A 181  ? 0.2139 0.3161 0.2319 0.0142  0.0032  -0.0787 179  VAL A CG1 
1194  C CG2 . VAL A 181  ? 0.2585 0.3434 0.2852 0.0164  0.0002  -0.0800 179  VAL A CG2 
1195  N N   . ILE A 182  ? 0.2139 0.3231 0.2221 0.0102  0.0042  -0.0722 180  ILE A N   
1196  C CA  . ILE A 182  ? 0.2220 0.3279 0.2247 0.0075  0.0052  -0.0645 180  ILE A CA  
1197  C C   . ILE A 182  ? 0.2429 0.3501 0.2450 0.0071  0.0045  -0.0648 180  ILE A C   
1198  O O   . ILE A 182  ? 0.2352 0.3337 0.2361 0.0061  0.0044  -0.0602 180  ILE A O   
1199  C CB  . ILE A 182  ? 0.2233 0.3382 0.2207 0.0053  0.0068  -0.0608 180  ILE A CB  
1200  C CG1 . ILE A 182  ? 0.2315 0.3449 0.2296 0.0057  0.0075  -0.0605 180  ILE A CG1 
1201  C CG2 . ILE A 182  ? 0.2308 0.3420 0.2233 0.0026  0.0075  -0.0528 180  ILE A CG2 
1202  C CD1 . ILE A 182  ? 0.2770 0.4016 0.2713 0.0040  0.0088  -0.0585 180  ILE A CD1 
1203  N N   . ARG A 183  ? 0.2257 0.3443 0.2287 0.0079  0.0040  -0.0706 181  ARG A N   
1204  C CA  A ARG A 183  ? 0.2466 0.3676 0.2494 0.0078  0.0031  -0.0718 181  ARG A CA  
1205  C CA  B ARG A 183  ? 0.2461 0.3671 0.2490 0.0078  0.0031  -0.0719 181  ARG A CA  
1206  C C   . ARG A 183  ? 0.2582 0.3674 0.2659 0.0091  0.0016  -0.0730 181  ARG A C   
1207  O O   . ARG A 183  ? 0.2591 0.3634 0.2654 0.0081  0.0014  -0.0694 181  ARG A O   
1208  C CB  A ARG A 183  ? 0.2492 0.3846 0.2532 0.0090  0.0025  -0.0792 181  ARG A CB  
1209  C CB  B ARG A 183  ? 0.2477 0.3830 0.2522 0.0092  0.0024  -0.0796 181  ARG A CB  
1210  C CG  A ARG A 183  ? 0.3220 0.4607 0.3269 0.0094  0.0012  -0.0821 181  ARG A CG  
1211  C CG  B ARG A 183  ? 0.3227 0.4626 0.3276 0.0094  0.0013  -0.0824 181  ARG A CG  
1212  C CD  A ARG A 183  ? 0.3452 0.4823 0.3447 0.0066  0.0020  -0.0745 181  ARG A CD  
1213  C CD  B ARG A 183  ? 0.3661 0.5126 0.3641 0.0066  0.0024  -0.0764 181  ARG A CD  
1214  N NE  A ARG A 183  ? 0.3126 0.4573 0.3060 0.0042  0.0036  -0.0691 181  ARG A NE  
1215  N NE  B ARG A 183  ? 0.3155 0.4504 0.3116 0.0048  0.0026  -0.0691 181  ARG A NE  
1216  C CZ  A ARG A 183  ? 0.3640 0.5057 0.3530 0.0015  0.0044  -0.0611 181  ARG A CZ  
1217  C CZ  B ARG A 183  ? 0.3612 0.4968 0.3518 0.0021  0.0037  -0.0615 181  ARG A CZ  
1218  N NH1 A ARG A 183  ? 0.3243 0.4556 0.3135 0.0010  0.0039  -0.0577 181  ARG A NH1 
1219  N NH1 B ARG A 183  ? 0.3850 0.5318 0.3716 0.0005  0.0048  -0.0595 181  ARG A NH1 
1220  N NH2 A ARG A 183  ? 0.3759 0.5253 0.3604 -0.0007 0.0056  -0.0564 181  ARG A NH2 
1221  N NH2 B ARG A 183  ? 0.3141 0.4391 0.3038 0.0009  0.0036  -0.0558 181  ARG A NH2 
1222  N N   . ARG A 184  ? 0.2439 0.3486 0.2578 0.0115  0.0004  -0.0778 182  ARG A N   
1223  C CA  . ARG A 184  ? 0.2676 0.3615 0.2868 0.0127  -0.0011 -0.0785 182  ARG A CA  
1224  C C   . ARG A 184  ? 0.2617 0.3436 0.2785 0.0112  -0.0003 -0.0706 182  ARG A C   
1225  O O   . ARG A 184  ? 0.2696 0.3443 0.2877 0.0109  -0.0009 -0.0685 182  ARG A O   
1226  C CB  . ARG A 184  ? 0.2638 0.3556 0.2907 0.0154  -0.0027 -0.0848 182  ARG A CB  
1227  C CG  . ARG A 184  ? 0.3410 0.4427 0.3723 0.0174  -0.0043 -0.0938 182  ARG A CG  
1228  C CD  . ARG A 184  ? 0.3454 0.4423 0.3825 0.0185  -0.0066 -0.0969 182  ARG A CD  
1229  N NE  . ARG A 184  ? 0.3800 0.4682 0.4255 0.0205  -0.0085 -0.0996 182  ARG A NE  
1230  C CZ  . ARG A 184  ? 0.3806 0.4569 0.4293 0.0203  -0.0093 -0.0957 182  ARG A CZ  
1231  N NH1 . ARG A 184  ? 0.3874 0.4586 0.4318 0.0183  -0.0083 -0.0893 182  ARG A NH1 
1232  N NH2 . ARG A 184  ? 0.3554 0.4252 0.4124 0.0221  -0.0112 -0.0982 182  ARG A NH2 
1233  N N   . GLY A 185  ? 0.2404 0.3201 0.2540 0.0102  0.0012  -0.0664 183  GLY A N   
1234  C CA  . GLY A 185  ? 0.2243 0.2935 0.2354 0.0089  0.0020  -0.0592 183  GLY A CA  
1235  C C   . GLY A 185  ? 0.2337 0.3029 0.2398 0.0068  0.0027  -0.0541 183  GLY A C   
1236  O O   . GLY A 185  ? 0.2337 0.2945 0.2399 0.0064  0.0025  -0.0505 183  GLY A O   
1237  N N   . VAL A 186  ? 0.2259 0.3052 0.2277 0.0054  0.0034  -0.0537 184  VAL A N   
1238  C CA  . VAL A 186  ? 0.2529 0.3332 0.2503 0.0033  0.0039  -0.0487 184  VAL A CA  
1239  C C   . VAL A 186  ? 0.2509 0.3292 0.2507 0.0039  0.0027  -0.0507 184  VAL A C   
1240  O O   . VAL A 186  ? 0.2432 0.3150 0.2418 0.0029  0.0027  -0.0462 184  VAL A O   
1241  C CB  . VAL A 186  ? 0.2518 0.3447 0.2450 0.0018  0.0047  -0.0482 184  VAL A CB  
1242  C CG1 . VAL A 186  ? 0.2687 0.3643 0.2584 -0.0001 0.0046  -0.0444 184  VAL A CG1 
1243  C CG2 . VAL A 186  ? 0.2512 0.3443 0.2415 0.0005  0.0059  -0.0442 184  VAL A CG2 
1244  N N   . ASP A 187  ? 0.2380 0.3220 0.2417 0.0056  0.0015  -0.0577 185  ASP A N   
1245  C CA  . ASP A 187  ? 0.2852 0.3681 0.2917 0.0062  0.0001  -0.0600 185  ASP A CA  
1246  C C   . ASP A 187  ? 0.3070 0.3772 0.3176 0.0070  -0.0006 -0.0584 185  ASP A C   
1247  O O   . ASP A 187  ? 0.2984 0.3643 0.3092 0.0064  -0.0011 -0.0561 185  ASP A O   
1248  C CB  . ASP A 187  ? 0.2827 0.3748 0.2931 0.0081  -0.0013 -0.0684 185  ASP A CB  
1249  C CG  . ASP A 187  ? 0.3088 0.4151 0.3147 0.0071  -0.0006 -0.0698 185  ASP A CG  
1250  O OD1 . ASP A 187  ? 0.3950 0.5037 0.3952 0.0048  0.0006  -0.0637 185  ASP A OD1 
1251  O OD2 . ASP A 187  ? 0.3577 0.4733 0.3663 0.0087  -0.0015 -0.0769 185  ASP A OD2 
1252  N N   . MET A 188  ? 0.2800 0.3445 0.2941 0.0082  -0.0008 -0.0593 186  MET A N   
1253  C CA  . MET A 188  ? 0.2744 0.3273 0.2924 0.0089  -0.0014 -0.0571 186  MET A CA  
1254  C C   . MET A 188  ? 0.3027 0.3488 0.3160 0.0071  0.0000  -0.0494 186  MET A C   
1255  O O   . MET A 188  ? 0.2754 0.3153 0.2901 0.0069  -0.0004 -0.0470 186  MET A O   
1256  C CB  . MET A 188  ? 0.3017 0.3509 0.3238 0.0104  -0.0018 -0.0591 186  MET A CB  
1257  C CG  . MET A 188  ? 0.3769 0.4152 0.4036 0.0110  -0.0025 -0.0568 186  MET A CG  
1258  S SD  . MET A 188  ? 0.5049 0.5416 0.5392 0.0123  -0.0050 -0.0612 186  MET A SD  
1259  C CE  . MET A 188  ? 0.4336 0.4794 0.4728 0.0144  -0.0066 -0.0705 186  MET A CE  
1260  N N   . ALA A 189  ? 0.2586 0.3060 0.2668 0.0059  0.0015  -0.0457 187  ALA A N   
1261  C CA  . ALA A 189  ? 0.2664 0.3077 0.2706 0.0043  0.0026  -0.0389 187  ALA A CA  
1262  C C   . ALA A 189  ? 0.2633 0.3062 0.2649 0.0030  0.0025  -0.0366 187  ALA A C   
1263  O O   . ALA A 189  ? 0.2654 0.3016 0.2665 0.0025  0.0027  -0.0325 187  ALA A O   
1264  C CB  . ALA A 189  ? 0.2957 0.3389 0.2956 0.0032  0.0039  -0.0359 187  ALA A CB  
1265  N N   . MET A 190  ? 0.2629 0.3155 0.2632 0.0025  0.0022  -0.0391 188  MET A N   
1266  C CA  . MET A 190  ? 0.2883 0.3433 0.2862 0.0012  0.0020  -0.0369 188  MET A CA  
1267  C C   . MET A 190  ? 0.3037 0.3533 0.3056 0.0021  0.0009  -0.0382 188  MET A C   
1268  O O   . MET A 190  ? 0.3137 0.3589 0.3144 0.0012  0.0010  -0.0342 188  MET A O   
1269  C CB  . MET A 190  ? 0.3025 0.3700 0.2986 0.0008  0.0018  -0.0401 188  MET A CB  
1270  C CG  . MET A 190  ? 0.3680 0.4394 0.3609 -0.0009 0.0016  -0.0370 188  MET A CG  
1271  S SD  . MET A 190  ? 0.4377 0.5252 0.4289 -0.0012 0.0012  -0.0413 188  MET A SD  
1272  C CE  . MET A 190  ? 0.3511 0.4440 0.3403 -0.0015 0.0025  -0.0415 188  MET A CE  
1273  N N   . ARG A 191  ? 0.2600 0.3100 0.2672 0.0039  -0.0003 -0.0440 189  ARG A N   
1274  C CA  . ARG A 191  ? 0.3194 0.3643 0.3316 0.0048  -0.0017 -0.0454 189  ARG A CA  
1275  C C   . ARG A 191  ? 0.3211 0.3550 0.3343 0.0047  -0.0012 -0.0406 189  ARG A C   
1276  O O   . ARG A 191  ? 0.3205 0.3500 0.3344 0.0043  -0.0014 -0.0380 189  ARG A O   
1277  C CB  . ARG A 191  ? 0.3139 0.3610 0.3324 0.0068  -0.0033 -0.0525 189  ARG A CB  
1278  C CG  . ARG A 191  ? 0.3996 0.4428 0.4242 0.0077  -0.0051 -0.0548 189  ARG A CG  
1279  C CD  . ARG A 191  ? 0.5310 0.5783 0.5621 0.0096  -0.0071 -0.0627 189  ARG A CD  
1280  N NE  . ARG A 191  ? 0.6561 0.6988 0.6916 0.0109  -0.0075 -0.0640 189  ARG A NE  
1281  C CZ  . ARG A 191  ? 0.7129 0.7483 0.7556 0.0120  -0.0090 -0.0647 189  ARG A CZ  
1282  N NH1 . ARG A 191  ? 0.7183 0.7502 0.7649 0.0119  -0.0104 -0.0646 189  ARG A NH1 
1283  N NH2 . ARG A 191  ? 0.6698 0.7015 0.7161 0.0131  -0.0093 -0.0654 189  ARG A NH2 
1284  N N   . MET A 192  ? 0.2632 0.2930 0.2767 0.0052  -0.0005 -0.0394 190  MET A N   
1285  C CA  . MET A 192  ? 0.2830 0.3034 0.2978 0.0053  -0.0001 -0.0352 190  MET A CA  
1286  C C   . MET A 192  ? 0.3119 0.3294 0.3215 0.0038  0.0011  -0.0293 190  MET A C   
1287  O O   . MET A 192  ? 0.2887 0.3007 0.2995 0.0037  0.0011  -0.0265 190  MET A O   
1288  C CB  . MET A 192  ? 0.3108 0.3282 0.3265 0.0061  0.0003  -0.0352 190  MET A CB  
1289  C CG  . MET A 192  ? 0.2849 0.3030 0.3071 0.0079  -0.0012 -0.0406 190  MET A CG  
1290  S SD  . MET A 192  ? 0.4397 0.4543 0.4630 0.0087  -0.0008 -0.0400 190  MET A SD  
1291  C CE  . MET A 192  ? 0.4306 0.4351 0.4569 0.0089  -0.0009 -0.0352 190  MET A CE  
1292  N N   . MET A 193  ? 0.2655 0.2870 0.2699 0.0026  0.0022  -0.0273 191  MET A N   
1293  C CA  A MET A 193  ? 0.2964 0.3151 0.2966 0.0013  0.0031  -0.0218 191  MET A CA  
1294  C CA  B MET A 193  ? 0.2968 0.3154 0.2972 0.0013  0.0031  -0.0218 191  MET A CA  
1295  C C   . MET A 193  ? 0.3105 0.3317 0.3096 0.0003  0.0027  -0.0207 191  MET A C   
1296  O O   . MET A 193  ? 0.3570 0.3744 0.3542 -0.0005 0.0031  -0.0164 191  MET A O   
1297  C CB  A MET A 193  ? 0.3115 0.3335 0.3074 0.0002  0.0041  -0.0198 191  MET A CB  
1298  C CB  B MET A 193  ? 0.3125 0.3337 0.3085 0.0003  0.0041  -0.0196 191  MET A CB  
1299  C CG  A MET A 193  ? 0.2924 0.3130 0.2891 0.0011  0.0045  -0.0211 191  MET A CG  
1300  C CG  B MET A 193  ? 0.3013 0.3180 0.2979 0.0011  0.0047  -0.0192 191  MET A CG  
1301  S SD  A MET A 193  ? 0.3245 0.3491 0.3164 -0.0003 0.0055  -0.0186 191  MET A SD  
1302  S SD  B MET A 193  ? 0.3307 0.3488 0.3224 -0.0003 0.0058  -0.0155 191  MET A SD  
1303  C CE  A MET A 193  ? 0.3737 0.3902 0.3634 -0.0010 0.0061  -0.0126 191  MET A CE  
1304  C CE  B MET A 193  ? 0.3349 0.3641 0.3254 -0.0010 0.0056  -0.0188 191  MET A CE  
1305  N N   . GLY A 194  ? 0.3007 0.3285 0.3011 0.0004  0.0017  -0.0246 192  GLY A N   
1306  C CA  . GLY A 194  ? 0.3281 0.3590 0.3272 -0.0005 0.0012  -0.0237 192  GLY A CA  
1307  C C   . GLY A 194  ? 0.3471 0.3754 0.3507 0.0003  0.0000  -0.0257 192  GLY A C   
1308  O O   . GLY A 194  ? 0.3613 0.3896 0.3642 -0.0004 -0.0003 -0.0238 192  GLY A O   
1309  N N   . GLU A 195  ? 0.2884 0.3142 0.2970 0.0018  -0.0007 -0.0295 193  GLU A N   
1310  C CA  . GLU A 195  ? 0.2792 0.3031 0.2930 0.0026  -0.0022 -0.0321 193  GLU A CA  
1311  C C   . GLU A 195  ? 0.2901 0.3058 0.3089 0.0037  -0.0025 -0.0314 193  GLU A C   
1312  O O   . GLU A 195  ? 0.2798 0.2927 0.3028 0.0039  -0.0035 -0.0318 193  GLU A O   
1313  C CB  . GLU A 195  ? 0.3288 0.3601 0.3458 0.0036  -0.0036 -0.0389 193  GLU A CB  
1314  C CG  . GLU A 195  ? 0.4198 0.4610 0.4322 0.0027  -0.0034 -0.0402 193  GLU A CG  
1315  C CD  . GLU A 195  ? 0.5476 0.5965 0.5632 0.0039  -0.0048 -0.0475 193  GLU A CD  
1316  O OE1 . GLU A 195  ? 0.5761 0.6225 0.5979 0.0053  -0.0064 -0.0515 193  GLU A OE1 
1317  O OE2 . GLU A 195  ? 0.6468 0.7044 0.6589 0.0036  -0.0043 -0.0493 193  GLU A OE2 
1318  N N   . GLN A 196  ? 0.3009 0.3131 0.3198 0.0042  -0.0017 -0.0303 194  GLN A N   
1319  C CA  A GLN A 196  ? 0.3082 0.3133 0.3318 0.0050  -0.0020 -0.0292 194  GLN A CA  
1320  C CA  B GLN A 196  ? 0.3082 0.3133 0.3318 0.0050  -0.0020 -0.0292 194  GLN A CA  
1321  C C   . GLN A 196  ? 0.3172 0.3164 0.3380 0.0045  -0.0005 -0.0233 194  GLN A C   
1322  O O   . GLN A 196  ? 0.3373 0.3318 0.3607 0.0045  -0.0007 -0.0208 194  GLN A O   
1323  C CB  A GLN A 196  ? 0.3358 0.3415 0.3627 0.0063  -0.0026 -0.0328 194  GLN A CB  
1324  C CB  B GLN A 196  ? 0.3359 0.3412 0.3628 0.0063  -0.0026 -0.0326 194  GLN A CB  
1325  C CG  A GLN A 196  ? 0.3430 0.3552 0.3733 0.0071  -0.0042 -0.0394 194  GLN A CG  
1326  C CG  B GLN A 196  ? 0.3767 0.3750 0.4087 0.0070  -0.0030 -0.0307 194  GLN A CG  
1327  C CD  A GLN A 196  ? 0.3654 0.3790 0.3987 0.0084  -0.0048 -0.0433 194  GLN A CD  
1328  C CD  B GLN A 196  ? 0.3616 0.3596 0.3966 0.0082  -0.0035 -0.0332 194  GLN A CD  
1329  O OE1 A GLN A 196  ? 0.3784 0.3988 0.4125 0.0090  -0.0056 -0.0486 194  GLN A OE1 
1330  O OE1 B GLN A 196  ? 0.3823 0.3855 0.4182 0.0088  -0.0042 -0.0381 194  GLN A OE1 
1331  N NE2 A GLN A 196  ? 0.3968 0.4044 0.4318 0.0088  -0.0044 -0.0407 194  GLN A NE2 
1332  N NE2 B GLN A 196  ? 0.3749 0.3672 0.4114 0.0084  -0.0032 -0.0297 194  GLN A NE2 
1333  N N   . PHE A 197  ? 0.2913 0.2908 0.3068 0.0040  0.0009  -0.0210 195  PHE A N   
1334  C CA  . PHE A 197  ? 0.3057 0.3002 0.3185 0.0036  0.0021  -0.0160 195  PHE A CA  
1335  C C   . PHE A 197  ? 0.3115 0.3056 0.3217 0.0027  0.0025  -0.0129 195  PHE A C   
1336  O O   . PHE A 197  ? 0.3234 0.3131 0.3327 0.0026  0.0033  -0.0092 195  PHE A O   
1337  C CB  . PHE A 197  ? 0.3197 0.3150 0.3282 0.0034  0.0033  -0.0148 195  PHE A CB  
1338  C CG  . PHE A 197  ? 0.3706 0.3661 0.3814 0.0043  0.0030  -0.0174 195  PHE A CG  
1339  C CD1 . PHE A 197  ? 0.4407 0.4326 0.4569 0.0054  0.0021  -0.0184 195  PHE A CD1 
1340  C CD2 . PHE A 197  ? 0.3392 0.3385 0.3469 0.0041  0.0035  -0.0185 195  PHE A CD2 
1341  C CE1 . PHE A 197  ? 0.4292 0.4213 0.4480 0.0064  0.0017  -0.0207 195  PHE A CE1 
1342  C CE2 . PHE A 197  ? 0.3854 0.3849 0.3954 0.0051  0.0032  -0.0210 195  PHE A CE2 
1343  C CZ  . PHE A 197  ? 0.3759 0.3717 0.3914 0.0063  0.0023  -0.0221 195  PHE A CZ  
1344  N N   . VAL A 198  ? 0.2751 0.2743 0.2840 0.0019  0.0020  -0.0145 196  VAL A N   
1345  C CA  . VAL A 198  ? 0.2650 0.2644 0.2723 0.0011  0.0020  -0.0121 196  VAL A CA  
1346  C C   . VAL A 198  ? 0.2705 0.2738 0.2808 0.0011  0.0006  -0.0156 196  VAL A C   
1347  O O   . VAL A 198  ? 0.3158 0.3235 0.3279 0.0016  -0.0003 -0.0200 196  VAL A O   
1348  C CB  . VAL A 198  ? 0.2600 0.2622 0.2619 -0.0002 0.0026  -0.0094 196  VAL A CB  
1349  C CG1 . VAL A 198  ? 0.2797 0.2778 0.2791 -0.0002 0.0038  -0.0062 196  VAL A CG1 
1350  C CG2 . VAL A 198  ? 0.2807 0.2905 0.2808 -0.0008 0.0022  -0.0123 196  VAL A CG2 
1351  N N   . THR A 199  ? 0.2490 0.2509 0.2602 0.0007  0.0002  -0.0138 197  THR A N   
1352  C CA  . THR A 199  ? 0.2785 0.2846 0.2919 0.0006  -0.0011 -0.0167 197  THR A CA  
1353  C C   . THR A 199  ? 0.2813 0.2945 0.2903 -0.0005 -0.0012 -0.0172 197  THR A C   
1354  O O   . THR A 199  ? 0.3428 0.3620 0.3528 -0.0004 -0.0023 -0.0212 197  THR A O   
1355  C CB  . THR A 199  ? 0.2756 0.2780 0.2911 0.0004  -0.0014 -0.0143 197  THR A CB  
1356  O OG1 . THR A 199  ? 0.2981 0.2944 0.3175 0.0012  -0.0012 -0.0131 197  THR A OG1 
1357  C CG2 . THR A 199  ? 0.3335 0.3398 0.3520 0.0003  -0.0030 -0.0176 197  THR A CG2 
1358  N N   . GLY A 200  ? 0.2630 0.2760 0.2673 -0.0014 -0.0002 -0.0132 198  GLY A N   
1359  C CA  . GLY A 200  ? 0.2765 0.2966 0.2768 -0.0027 -0.0003 -0.0129 198  GLY A CA  
1360  C C   . GLY A 200  ? 0.2521 0.2702 0.2486 -0.0035 0.0008  -0.0083 198  GLY A C   
1361  O O   . GLY A 200  ? 0.2491 0.2604 0.2457 -0.0032 0.0015  -0.0055 198  GLY A O   
1362  N N   . GLU A 201  ? 0.2634 0.2878 0.2565 -0.0047 0.0008  -0.0075 199  GLU A N   
1363  C CA  . GLU A 201  ? 0.2618 0.2848 0.2518 -0.0058 0.0015  -0.0032 199  GLU A CA  
1364  C C   . GLU A 201  ? 0.2821 0.3023 0.2714 -0.0066 0.0012  0.0012  199  GLU A C   
1365  O O   . GLU A 201  ? 0.3111 0.3269 0.2994 -0.0069 0.0016  0.0047  199  GLU A O   
1366  C CB  . GLU A 201  ? 0.3248 0.3561 0.3120 -0.0069 0.0014  -0.0035 199  GLU A CB  
1367  C CG  . GLU A 201  ? 0.4344 0.4650 0.4189 -0.0082 0.0019  0.0010  199  GLU A CG  
1368  C CD  . GLU A 201  ? 0.5947 0.6343 0.5768 -0.0095 0.0018  0.0008  199  GLU A CD  
1369  O OE1 . GLU A 201  ? 0.6130 0.6603 0.5950 -0.0096 0.0014  -0.0022 199  GLU A OE1 
1370  O OE2 . GLU A 201  ? 0.6653 0.7047 0.6459 -0.0104 0.0023  0.0035  199  GLU A OE2 
1371  N N   . THR A 202  ? 0.2583 0.2811 0.2484 -0.0070 0.0003  0.0010  200  THR A N   
1372  C CA  . THR A 202  ? 0.2399 0.2604 0.2298 -0.0077 -0.0002 0.0049  200  THR A CA  
1373  C C   . THR A 202  ? 0.2329 0.2510 0.2259 -0.0068 -0.0007 0.0033  200  THR A C   
1374  O O   . THR A 202  ? 0.2383 0.2581 0.2334 -0.0060 -0.0009 -0.0008 200  THR A O   
1375  C CB  . THR A 202  ? 0.2756 0.3037 0.2634 -0.0094 -0.0012 0.0069  200  THR A CB  
1376  O OG1 . THR A 202  ? 0.3010 0.3356 0.2894 -0.0093 -0.0018 0.0030  200  THR A OG1 
1377  C CG2 . THR A 202  ? 0.3045 0.3366 0.2896 -0.0106 -0.0009 0.0086  200  THR A CG2 
1378  N N   . ILE A 203  ? 0.2347 0.2489 0.2284 -0.0069 -0.0009 0.0065  201  ILE A N   
1379  C CA  . ILE A 203  ? 0.2322 0.2438 0.2289 -0.0062 -0.0012 0.0054  201  ILE A CA  
1380  C C   . ILE A 203  ? 0.2533 0.2717 0.2508 -0.0066 -0.0025 0.0028  201  ILE A C   
1381  O O   . ILE A 203  ? 0.2405 0.2584 0.2410 -0.0058 -0.0029 -0.0005 201  ILE A O   
1382  C CB  . ILE A 203  ? 0.2510 0.2577 0.2485 -0.0061 -0.0012 0.0093  201  ILE A CB  
1383  C CG1 . ILE A 203  ? 0.2236 0.2273 0.2246 -0.0052 -0.0014 0.0082  201  ILE A CG1 
1384  C CG2 . ILE A 203  ? 0.2717 0.2820 0.2674 -0.0076 -0.0022 0.0125  201  ILE A CG2 
1385  C CD1 . ILE A 203  ? 0.2371 0.2371 0.2406 -0.0039 -0.0006 0.0057  201  ILE A CD1 
1386  N N   . ARG A 204  ? 0.2377 0.2628 0.2325 -0.0080 -0.0032 0.0040  202  ARG A N   
1387  C CA  . ARG A 204  ? 0.2431 0.2755 0.2381 -0.0084 -0.0044 0.0012  202  ARG A CA  
1388  C C   . ARG A 204  ? 0.2332 0.2691 0.2295 -0.0074 -0.0044 -0.0045 202  ARG A C   
1389  O O   . ARG A 204  ? 0.2561 0.2941 0.2550 -0.0068 -0.0053 -0.0082 202  ARG A O   
1390  C CB  . ARG A 204  ? 0.3166 0.3565 0.3084 -0.0101 -0.0051 0.0041  202  ARG A CB  
1391  C CG  . ARG A 204  ? 0.4043 0.4424 0.3963 -0.0110 -0.0058 0.0086  202  ARG A CG  
1392  C CD  . ARG A 204  ? 0.4427 0.4861 0.4319 -0.0129 -0.0065 0.0130  202  ARG A CD  
1393  N NE  . ARG A 204  ? 0.4280 0.4694 0.4181 -0.0136 -0.0074 0.0174  202  ARG A NE  
1394  C CZ  . ARG A 204  ? 0.4273 0.4607 0.4189 -0.0131 -0.0071 0.0203  202  ARG A CZ  
1395  N NH1 . ARG A 204  ? 0.3396 0.3665 0.3316 -0.0121 -0.0059 0.0197  202  ARG A NH1 
1396  N NH2 . ARG A 204  ? 0.3713 0.4036 0.3642 -0.0137 -0.0082 0.0239  202  ARG A NH2 
1397  N N   . GLU A 205  ? 0.2555 0.2922 0.2502 -0.0073 -0.0035 -0.0054 203  GLU A N   
1398  C CA  . GLU A 205  ? 0.2773 0.3169 0.2738 -0.0062 -0.0036 -0.0110 203  GLU A CA  
1399  C C   . GLU A 205  ? 0.2584 0.2908 0.2595 -0.0046 -0.0037 -0.0134 203  GLU A C   
1400  O O   . GLU A 205  ? 0.2532 0.2880 0.2577 -0.0037 -0.0047 -0.0182 203  GLU A O   
1401  C CB  . GLU A 205  ? 0.2839 0.3248 0.2780 -0.0063 -0.0026 -0.0109 203  GLU A CB  
1402  C CG  . GLU A 205  ? 0.3352 0.3804 0.3308 -0.0052 -0.0028 -0.0168 203  GLU A CG  
1403  C CD  . GLU A 205  ? 0.4396 0.4875 0.4325 -0.0055 -0.0018 -0.0164 203  GLU A CD  
1404  O OE1 . GLU A 205  ? 0.3779 0.4190 0.3710 -0.0051 -0.0008 -0.0147 203  GLU A OE1 
1405  O OE2 . GLU A 205  ? 0.4774 0.5346 0.4679 -0.0062 -0.0020 -0.0177 203  GLU A OE2 
1406  N N   . ALA A 206  ? 0.2342 0.2584 0.2359 -0.0043 -0.0028 -0.0100 204  ALA A N   
1407  C CA  . ALA A 206  ? 0.2408 0.2587 0.2470 -0.0031 -0.0028 -0.0114 204  ALA A CA  
1408  C C   . ALA A 206  ? 0.2350 0.2532 0.2447 -0.0030 -0.0040 -0.0126 204  ALA A C   
1409  O O   . ALA A 206  ? 0.2644 0.2815 0.2788 -0.0020 -0.0049 -0.0161 204  ALA A O   
1410  C CB  . ALA A 206  ? 0.2381 0.2485 0.2438 -0.0029 -0.0015 -0.0070 204  ALA A CB  
1411  N N   . LEU A 207  ? 0.2351 0.2549 0.2431 -0.0039 -0.0043 -0.0097 205  LEU A N   
1412  C CA  . LEU A 207  ? 0.2345 0.2549 0.2456 -0.0039 -0.0056 -0.0107 205  LEU A CA  
1413  C C   . LEU A 207  ? 0.2721 0.2995 0.2848 -0.0037 -0.0071 -0.0161 205  LEU A C   
1414  O O   . LEU A 207  ? 0.2627 0.2893 0.2802 -0.0030 -0.0083 -0.0191 205  LEU A O   
1415  C CB  . LEU A 207  ? 0.2522 0.2732 0.2609 -0.0050 -0.0057 -0.0065 205  LEU A CB  
1416  C CG  . LEU A 207  ? 0.2384 0.2522 0.2470 -0.0048 -0.0046 -0.0019 205  LEU A CG  
1417  C CD1 . LEU A 207  ? 0.2488 0.2642 0.2547 -0.0060 -0.0048 0.0022  205  LEU A CD1 
1418  C CD2 . LEU A 207  ? 0.2483 0.2572 0.2617 -0.0040 -0.0047 -0.0023 205  LEU A CD2 
1419  N N   . LYS A 208  ? 0.2597 0.2945 0.2688 -0.0042 -0.0072 -0.0176 206  LYS A N   
1420  C CA  . LYS A 208  ? 0.2882 0.3308 0.2988 -0.0038 -0.0086 -0.0233 206  LYS A CA  
1421  C C   . LYS A 208  ? 0.2977 0.3378 0.3133 -0.0023 -0.0091 -0.0284 206  LYS A C   
1422  O O   . LYS A 208  ? 0.3337 0.3760 0.3536 -0.0015 -0.0107 -0.0331 206  LYS A O   
1423  C CB  . LYS A 208  ? 0.3135 0.3649 0.3190 -0.0046 -0.0083 -0.0236 206  LYS A CB  
1424  N N   . ARG A 209  ? 0.2756 0.3108 0.2910 -0.0018 -0.0078 -0.0274 207  ARG A N   
1425  C CA  . ARG A 209  ? 0.2889 0.3215 0.3093 -0.0003 -0.0084 -0.0317 207  ARG A CA  
1426  C C   . ARG A 209  ? 0.3167 0.3417 0.3430 0.0003  -0.0090 -0.0311 207  ARG A C   
1427  O O   . ARG A 209  ? 0.3470 0.3700 0.3788 0.0014  -0.0100 -0.0347 207  ARG A O   
1428  C CB  . ARG A 209  ? 0.2933 0.3238 0.3114 -0.0001 -0.0069 -0.0305 207  ARG A CB  
1429  C CG  . ARG A 209  ? 0.3276 0.3666 0.3413 -0.0005 -0.0066 -0.0323 207  ARG A CG  
1430  C CD  . ARG A 209  ? 0.3350 0.3717 0.3459 -0.0005 -0.0051 -0.0303 207  ARG A CD  
1431  N NE  . ARG A 209  ? 0.3800 0.4252 0.3866 -0.0011 -0.0047 -0.0313 207  ARG A NE  
1432  C CZ  . ARG A 209  ? 0.4339 0.4788 0.4377 -0.0014 -0.0034 -0.0296 207  ARG A CZ  
1433  N NH1 . ARG A 209  ? 0.3450 0.3818 0.3495 -0.0010 -0.0024 -0.0270 207  ARG A NH1 
1434  N NH2 . ARG A 209  ? 0.4863 0.5399 0.4866 -0.0021 -0.0031 -0.0305 207  ARG A NH2 
1435  N N   . SER A 210  ? 0.2972 0.3184 0.3231 -0.0004 -0.0086 -0.0267 208  SER A N   
1436  C CA  . SER A 210  ? 0.2735 0.2880 0.3049 0.0000  -0.0090 -0.0254 208  SER A CA  
1437  C C   . SER A 210  ? 0.3012 0.3178 0.3378 0.0002  -0.0112 -0.0290 208  SER A C   
1438  O O   . SER A 210  ? 0.2904 0.3022 0.3331 0.0006  -0.0120 -0.0290 208  SER A O   
1439  C CB  . SER A 210  ? 0.2881 0.2977 0.3169 -0.0007 -0.0076 -0.0192 208  SER A CB  
1440  O OG  . SER A 210  ? 0.2971 0.3040 0.3221 -0.0007 -0.0058 -0.0163 208  SER A OG  
1441  N N   . LYS A 211  ? 0.3029 0.3269 0.3376 -0.0001 -0.0122 -0.0319 209  LYS A N   
1442  C CA  . LYS A 211  ? 0.2988 0.3251 0.3382 0.0000  -0.0143 -0.0350 209  LYS A CA  
1443  C C   . LYS A 211  ? 0.2978 0.3229 0.3451 0.0012  -0.0162 -0.0405 209  LYS A C   
1444  O O   . LYS A 211  ? 0.3245 0.3467 0.3780 0.0014  -0.0177 -0.0413 209  LYS A O   
1445  C CB  . LYS A 211  ? 0.3638 0.3995 0.3993 -0.0005 -0.0151 -0.0374 209  LYS A CB  
1446  N N   . GLU A 212  ? 0.3145 0.3414 0.3620 0.0021  -0.0162 -0.0441 210  GLU A N   
1447  C CA  . GLU A 212  ? 0.3608 0.3871 0.4162 0.0034  -0.0183 -0.0498 210  GLU A CA  
1448  C C   . GLU A 212  ? 0.3589 0.3763 0.4211 0.0036  -0.0188 -0.0471 210  GLU A C   
1449  O O   . GLU A 212  ? 0.3650 0.3811 0.4348 0.0040  -0.0210 -0.0498 210  GLU A O   
1450  C CB  . GLU A 212  ? 0.4012 0.4305 0.4553 0.0044  -0.0180 -0.0534 210  GLU A CB  
1451  C CG  . GLU A 212  ? 0.5161 0.5452 0.5789 0.0059  -0.0204 -0.0598 210  GLU A CG  
1452  C CD  . GLU A 212  ? 0.6527 0.6840 0.7144 0.0069  -0.0199 -0.0628 210  GLU A CD  
1453  O OE1 . GLU A 212  ? 0.7182 0.7541 0.7722 0.0064  -0.0180 -0.0615 210  GLU A OE1 
1454  O OE2 . GLU A 212  ? 0.7087 0.7372 0.7778 0.0082  -0.0215 -0.0663 210  GLU A OE2 
1455  N N   . LEU A 213  ? 0.3285 0.3401 0.3883 0.0032  -0.0167 -0.0415 211  LEU A N   
1456  C CA  . LEU A 213  ? 0.3057 0.3097 0.3717 0.0033  -0.0170 -0.0385 211  LEU A CA  
1457  C C   . LEU A 213  ? 0.2988 0.3002 0.3658 0.0023  -0.0168 -0.0342 211  LEU A C   
1458  O O   . LEU A 213  ? 0.2945 0.2917 0.3687 0.0023  -0.0180 -0.0331 211  LEU A O   
1459  C CB  . LEU A 213  ? 0.2750 0.2745 0.3387 0.0034  -0.0151 -0.0346 211  LEU A CB  
1460  C CG  . LEU A 213  ? 0.3122 0.3131 0.3777 0.0045  -0.0157 -0.0389 211  LEU A CG  
1461  C CD1 . LEU A 213  ? 0.3288 0.3250 0.3922 0.0046  -0.0139 -0.0348 211  LEU A CD1 
1462  C CD2 . LEU A 213  ? 0.3892 0.3896 0.4647 0.0055  -0.0188 -0.0441 211  LEU A CD2 
1463  N N   . GLU A 214  ? 0.2749 0.2789 0.3352 0.0015  -0.0155 -0.0316 212  GLU A N   
1464  C CA  . GLU A 214  ? 0.2795 0.2817 0.3413 0.0007  -0.0156 -0.0283 212  GLU A CA  
1465  C C   . GLU A 214  ? 0.3223 0.3265 0.3912 0.0009  -0.0185 -0.0326 212  GLU A C   
1466  O O   . GLU A 214  ? 0.3164 0.3170 0.3907 0.0005  -0.0192 -0.0306 212  GLU A O   
1467  C CB  . GLU A 214  ? 0.2768 0.2818 0.3307 -0.0001 -0.0141 -0.0252 212  GLU A CB  
1468  C CG  . GLU A 214  ? 0.2738 0.2753 0.3222 -0.0004 -0.0116 -0.0200 212  GLU A CG  
1469  C CD  . GLU A 214  ? 0.3184 0.3222 0.3603 -0.0012 -0.0104 -0.0167 212  GLU A CD  
1470  O OE1 . GLU A 214  ? 0.3334 0.3426 0.3737 -0.0016 -0.0115 -0.0189 212  GLU A OE1 
1471  O OE2 . GLU A 214  ? 0.3379 0.3381 0.3766 -0.0014 -0.0086 -0.0121 212  GLU A OE2 
1472  N N   . GLU A 215  ? 0.3115 0.3216 0.3807 0.0015  -0.0201 -0.0389 213  GLU A N   
1473  C CA  . GLU A 215  ? 0.3618 0.3745 0.4381 0.0018  -0.0230 -0.0439 213  GLU A CA  
1474  C C   . GLU A 215  ? 0.3829 0.3904 0.4692 0.0024  -0.0249 -0.0455 213  GLU A C   
1475  O O   . GLU A 215  ? 0.4214 0.4286 0.5151 0.0024  -0.0273 -0.0478 213  GLU A O   
1476  C CB  . GLU A 215  ? 0.3935 0.4146 0.4676 0.0025  -0.0243 -0.0507 213  GLU A CB  
1477  N N   . LYS A 216  ? 0.3667 0.3701 0.4538 0.0029  -0.0240 -0.0439 214  LYS A N   
1478  C CA  . LYS A 216  ? 0.3733 0.3716 0.4701 0.0033  -0.0258 -0.0444 214  LYS A CA  
1479  C C   . LYS A 216  ? 0.3874 0.3792 0.4865 0.0023  -0.0247 -0.0371 214  LYS A C   
1480  O O   . LYS A 216  ? 0.4771 0.4647 0.5850 0.0024  -0.0263 -0.0364 214  LYS A O   
1481  C CB  . LYS A 216  ? 0.3555 0.3532 0.4525 0.0043  -0.0256 -0.0466 214  LYS A CB  
1482  N N   . GLY A 217  ? 0.3268 0.3182 0.4189 0.0015  -0.0221 -0.0317 215  GLY A N   
1483  C CA  . GLY A 217  ? 0.3302 0.3167 0.4239 0.0007  -0.0209 -0.0251 215  GLY A CA  
1484  C C   . GLY A 217  ? 0.2971 0.2809 0.3846 0.0006  -0.0179 -0.0199 215  GLY A C   
1485  O O   . GLY A 217  ? 0.3146 0.2950 0.4034 0.0001  -0.0168 -0.0144 215  GLY A O   
1486  N N   . PHE A 218  ? 0.2723 0.2580 0.3536 0.0012  -0.0167 -0.0216 216  PHE A N   
1487  C CA  . PHE A 218  ? 0.2295 0.2131 0.3043 0.0011  -0.0139 -0.0169 216  PHE A CA  
1488  C C   . PHE A 218  ? 0.2556 0.2409 0.3229 0.0005  -0.0121 -0.0140 216  PHE A C   
1489  O O   . PHE A 218  ? 0.2550 0.2439 0.3208 0.0002  -0.0128 -0.0160 216  PHE A O   
1490  C CB  . PHE A 218  ? 0.2520 0.2371 0.3229 0.0018  -0.0134 -0.0197 216  PHE A CB  
1491  C CG  . PHE A 218  ? 0.2544 0.2372 0.3320 0.0026  -0.0149 -0.0218 216  PHE A CG  
1492  C CD1 . PHE A 218  ? 0.2896 0.2744 0.3739 0.0032  -0.0177 -0.0277 216  PHE A CD1 
1493  C CD2 . PHE A 218  ? 0.2580 0.2371 0.3356 0.0027  -0.0136 -0.0180 216  PHE A CD2 
1494  C CE1 . PHE A 218  ? 0.2963 0.2789 0.3875 0.0039  -0.0193 -0.0298 216  PHE A CE1 
1495  C CE2 . PHE A 218  ? 0.2848 0.2618 0.3689 0.0034  -0.0151 -0.0197 216  PHE A CE2 
1496  C CZ  . PHE A 218  ? 0.2577 0.2362 0.3488 0.0040  -0.0180 -0.0255 216  PHE A CZ  
1497  N N   . SER A 219  ? 0.2498 0.2325 0.3127 0.0004  -0.0097 -0.0091 217  SER A N   
1498  C CA  . SER A 219  ? 0.2303 0.2144 0.2859 0.0000  -0.0080 -0.0065 217  SER A CA  
1499  C C   . SER A 219  ? 0.2150 0.1985 0.2647 0.0004  -0.0062 -0.0054 217  SER A C   
1500  O O   . SER A 219  ? 0.2039 0.1861 0.2551 0.0009  -0.0063 -0.0066 217  SER A O   
1501  C CB  . SER A 219  ? 0.2417 0.2236 0.2983 -0.0003 -0.0070 -0.0017 217  SER A CB  
1502  O OG  . SER A 219  ? 0.2571 0.2355 0.3160 -0.0001 -0.0060 0.0016  217  SER A OG  
1503  N N   . TYR A 220  ? 0.2011 0.1854 0.2443 0.0001  -0.0047 -0.0030 218  TYR A N   
1504  C CA  . TYR A 220  ? 0.2027 0.1869 0.2402 0.0003  -0.0032 -0.0021 218  TYR A CA  
1505  C C   . TYR A 220  ? 0.2087 0.1906 0.2424 0.0003  -0.0013 0.0024  218  TYR A C   
1506  O O   . TYR A 220  ? 0.2064 0.1885 0.2402 0.0000  -0.0013 0.0044  218  TYR A O   
1507  C CB  . TYR A 220  ? 0.2195 0.2083 0.2524 -0.0001 -0.0036 -0.0048 218  TYR A CB  
1508  C CG  . TYR A 220  ? 0.2098 0.2012 0.2449 0.0003  -0.0048 -0.0097 218  TYR A CG  
1509  C CD1 . TYR A 220  ? 0.2572 0.2509 0.2972 0.0004  -0.0068 -0.0135 218  TYR A CD1 
1510  C CD2 . TYR A 220  ? 0.2274 0.2189 0.2602 0.0007  -0.0042 -0.0107 218  TYR A CD2 
1511  C CE1 . TYR A 220  ? 0.2406 0.2370 0.2831 0.0009  -0.0082 -0.0185 218  TYR A CE1 
1512  C CE2 . TYR A 220  ? 0.2377 0.2319 0.2728 0.0012  -0.0054 -0.0154 218  TYR A CE2 
1513  C CZ  . TYR A 220  ? 0.2565 0.2532 0.2966 0.0014  -0.0074 -0.0194 218  TYR A CZ  
1514  O OH  . TYR A 220  ? 0.2561 0.2557 0.2989 0.0021  -0.0087 -0.0246 218  TYR A OH  
1515  N N   . SER A 221  ? 0.2109 0.1911 0.2418 0.0007  0.0000  0.0038  219  SER A N   
1516  C CA  . SER A 221  ? 0.2133 0.1921 0.2397 0.0009  0.0016  0.0071  219  SER A CA  
1517  C C   . SER A 221  ? 0.2050 0.1848 0.2266 0.0009  0.0021  0.0062  219  SER A C   
1518  O O   . SER A 221  ? 0.2478 0.2269 0.2696 0.0013  0.0023  0.0051  219  SER A O   
1519  C CB  . SER A 221  ? 0.2305 0.2063 0.2587 0.0016  0.0028  0.0101  219  SER A CB  
1520  O OG  . SER A 221  ? 0.2447 0.2197 0.2688 0.0019  0.0041  0.0126  219  SER A OG  
1521  N N   . TYR A 222  ? 0.1833 0.1647 0.2008 0.0004  0.0022  0.0070  220  TYR A N   
1522  C CA  . TYR A 222  ? 0.1999 0.1829 0.2131 0.0001  0.0025  0.0062  220  TYR A CA  
1523  C C   . TYR A 222  ? 0.2425 0.2227 0.2529 0.0005  0.0038  0.0087  220  TYR A C   
1524  O O   . TYR A 222  ? 0.2287 0.2073 0.2386 0.0008  0.0043  0.0112  220  TYR A O   
1525  C CB  . TYR A 222  ? 0.2226 0.2095 0.2333 -0.0009 0.0016  0.0059  220  TYR A CB  
1526  C CG  . TYR A 222  ? 0.2074 0.1979 0.2207 -0.0013 0.0002  0.0028  220  TYR A CG  
1527  C CD1 . TYR A 222  ? 0.2062 0.1997 0.2198 -0.0012 -0.0003 -0.0008 220  TYR A CD1 
1528  C CD2 . TYR A 222  ? 0.1880 0.1791 0.2038 -0.0015 -0.0006 0.0031  220  TYR A CD2 
1529  C CE1 . TYR A 222  ? 0.2169 0.2139 0.2332 -0.0013 -0.0017 -0.0043 220  TYR A CE1 
1530  C CE2 . TYR A 222  ? 0.2183 0.2127 0.2367 -0.0017 -0.0020 -0.0001 220  TYR A CE2 
1531  C CZ  . TYR A 222  ? 0.2147 0.2122 0.2335 -0.0016 -0.0026 -0.0039 220  TYR A CZ  
1532  O OH  . TYR A 222  ? 0.2389 0.2401 0.2607 -0.0016 -0.0042 -0.0077 220  TYR A OH  
1533  N N   . ASP A 223  ? 0.2449 0.2250 0.2535 0.0007  0.0042  0.0078  221  ASP A N   
1534  C CA  . ASP A 223  ? 0.3003 0.2782 0.3062 0.0012  0.0053  0.0095  221  ASP A CA  
1535  C C   . ASP A 223  ? 0.2901 0.2702 0.2923 0.0004  0.0051  0.0093  221  ASP A C   
1536  O O   . ASP A 223  ? 0.2725 0.2548 0.2740 0.0001  0.0048  0.0072  221  ASP A O   
1537  C CB  . ASP A 223  ? 0.3097 0.2859 0.3171 0.0020  0.0059  0.0088  221  ASP A CB  
1538  C CG  . ASP A 223  ? 0.3512 0.3258 0.3556 0.0025  0.0068  0.0100  221  ASP A CG  
1539  O OD1 . ASP A 223  ? 0.3644 0.3382 0.3664 0.0025  0.0072  0.0117  221  ASP A OD1 
1540  O OD2 . ASP A 223  ? 0.4699 0.4440 0.4746 0.0029  0.0071  0.0090  221  ASP A OD2 
1541  N N   . MET A 224  ? 0.2920 0.2717 0.2921 0.0000  0.0051  0.0115  222  MET A N   
1542  C CA  . MET A 224  ? 0.3027 0.2843 0.2998 -0.0009 0.0047  0.0120  222  MET A CA  
1543  C C   . MET A 224  ? 0.3112 0.2912 0.3065 -0.0005 0.0054  0.0121  222  MET A C   
1544  O O   . MET A 224  ? 0.4012 0.3826 0.3944 -0.0013 0.0051  0.0129  222  MET A O   
1545  C CB  . MET A 224  ? 0.3036 0.2853 0.3002 -0.0015 0.0040  0.0145  222  MET A CB  
1546  C CG  . MET A 224  ? 0.3158 0.2998 0.3141 -0.0021 0.0031  0.0145  222  MET A CG  
1547  S SD  . MET A 224  ? 0.3926 0.3825 0.3905 -0.0031 0.0023  0.0119  222  MET A SD  
1548  C CE  . MET A 224  ? 0.4587 0.4520 0.4532 -0.0045 0.0018  0.0133  222  MET A CE  
1549  N N   . LEU A 225  ? 0.3828 0.3602 0.3792 0.0007  0.0063  0.0115  223  LEU A N   
1550  C CA  . LEU A 225  ? 0.3736 0.3499 0.3686 0.0011  0.0069  0.0111  223  LEU A CA  
1551  C C   . LEU A 225  ? 0.4574 0.4316 0.4504 0.0014  0.0072  0.0129  223  LEU A C   
1552  O O   . LEU A 225  ? 0.4869 0.4605 0.4785 0.0016  0.0075  0.0126  223  LEU A O   
1553  C CB  . LEU A 225  ? 0.4123 0.3917 0.4062 0.0004  0.0066  0.0091  223  LEU A CB  
1554  C CG  . LEU A 225  ? 0.3325 0.3134 0.3289 0.0007  0.0063  0.0063  223  LEU A CG  
1555  C CD1 . LEU A 225  ? 0.4154 0.4005 0.4106 0.0000  0.0059  0.0041  223  LEU A CD1 
1556  C CD2 . LEU A 225  ? 0.4036 0.3814 0.4020 0.0019  0.0070  0.0061  223  LEU A CD2 
1557  N N   . GLY A 226  ? 0.3976 0.3708 0.3910 0.0014  0.0068  0.0145  224  GLY A N   
1558  C CA  . GLY A 226  ? 0.4398 0.4109 0.4323 0.0019  0.0068  0.0158  224  GLY A CA  
1559  C C   . GLY A 226  ? 0.3687 0.3376 0.3616 0.0035  0.0079  0.0156  224  GLY A C   
1560  O O   . GLY A 226  ? 0.3418 0.3105 0.3363 0.0042  0.0085  0.0156  224  GLY A O   
1561  N N   . GLU A 227  ? 0.3489 0.3165 0.3405 0.0041  0.0081  0.0156  225  GLU A N   
1562  C CA  . GLU A 227  ? 0.3242 0.2907 0.3158 0.0057  0.0091  0.0154  225  GLU A CA  
1563  C C   . GLU A 227  ? 0.3078 0.2731 0.2979 0.0062  0.0088  0.0151  225  GLU A C   
1564  O O   . GLU A 227  ? 0.2921 0.2575 0.2812 0.0052  0.0081  0.0150  225  GLU A O   
1565  C CB  . GLU A 227  ? 0.3592 0.3263 0.3509 0.0057  0.0098  0.0146  225  GLU A CB  
1566  C CG  . GLU A 227  ? 0.4514 0.4179 0.4431 0.0071  0.0108  0.0148  225  GLU A CG  
1567  C CD  . GLU A 227  ? 0.5386 0.5056 0.5313 0.0070  0.0110  0.0142  225  GLU A CD  
1568  O OE1 . GLU A 227  ? 0.4211 0.3890 0.4151 0.0060  0.0105  0.0135  225  GLU A OE1 
1569  O OE2 . GLU A 227  ? 0.5519 0.5189 0.5444 0.0078  0.0116  0.0144  225  GLU A OE2 
1570  N N   . ALA A 228  ? 0.2685 0.2331 0.2589 0.0077  0.0093  0.0150  226  ALA A N   
1571  C CA  . ALA A 228  ? 0.2952 0.2590 0.2845 0.0086  0.0091  0.0142  226  ALA A CA  
1572  C C   . ALA A 228  ? 0.2439 0.2067 0.2334 0.0076  0.0075  0.0144  226  ALA A C   
1573  O O   . ALA A 228  ? 0.2967 0.2593 0.2853 0.0069  0.0070  0.0141  226  ALA A O   
1574  C CB  . ALA A 228  ? 0.3405 0.3047 0.3282 0.0087  0.0098  0.0136  226  ALA A CB  
1575  N N   . ALA A 229  ? 0.2419 0.2042 0.2332 0.0075  0.0067  0.0151  227  ALA A N   
1576  C CA  . ALA A 229  ? 0.2251 0.1863 0.2176 0.0068  0.0049  0.0156  227  ALA A CA  
1577  C C   . ALA A 229  ? 0.2446 0.2045 0.2371 0.0079  0.0045  0.0142  227  ALA A C   
1578  O O   . ALA A 229  ? 0.2410 0.2009 0.2335 0.0098  0.0052  0.0128  227  ALA A O   
1579  C CB  . ALA A 229  ? 0.2330 0.1936 0.2280 0.0071  0.0041  0.0164  227  ALA A CB  
1580  N N   . THR A 230  ? 0.2438 0.2030 0.2364 0.0067  0.0032  0.0147  228  THR A N   
1581  C CA  . THR A 230  ? 0.2501 0.2080 0.2432 0.0075  0.0023  0.0133  228  THR A CA  
1582  C C   . THR A 230  ? 0.2361 0.1922 0.2328 0.0076  0.0001  0.0136  228  THR A C   
1583  O O   . THR A 230  ? 0.2396 0.1945 0.2378 0.0090  -0.0007 0.0117  228  THR A O   
1584  C CB  . THR A 230  ? 0.2785 0.2369 0.2701 0.0060  0.0022  0.0137  228  THR A CB  
1585  O OG1 . THR A 230  ? 0.3563 0.3163 0.3453 0.0061  0.0040  0.0133  228  THR A OG1 
1586  C CG2 . THR A 230  ? 0.3155 0.2726 0.3077 0.0069  0.0013  0.0122  228  THR A CG2 
1587  N N   . THR A 231  ? 0.2318 0.1878 0.2303 0.0061  -0.0010 0.0157  229  THR A N   
1588  C CA  . THR A 231  ? 0.2129 0.1671 0.2155 0.0058  -0.0034 0.0166  229  THR A CA  
1589  C C   . THR A 231  ? 0.2315 0.1859 0.2357 0.0058  -0.0036 0.0178  229  THR A C   
1590  O O   . THR A 231  ? 0.2158 0.1720 0.2179 0.0055  -0.0021 0.0184  229  THR A O   
1591  C CB  . THR A 231  ? 0.2312 0.1854 0.2349 0.0033  -0.0051 0.0191  229  THR A CB  
1592  O OG1 . THR A 231  ? 0.2526 0.2092 0.2548 0.0014  -0.0047 0.0216  229  THR A OG1 
1593  C CG2 . THR A 231  ? 0.2435 0.1980 0.2451 0.0029  -0.0047 0.0183  229  THR A CG2 
1594  N N   . ALA A 232  ? 0.2336 0.1862 0.2421 0.0063  -0.0057 0.0179  230  ALA A N   
1595  C CA  . ALA A 232  ? 0.2339 0.1866 0.2446 0.0061  -0.0065 0.0195  230  ALA A CA  
1596  C C   . ALA A 232  ? 0.2596 0.2143 0.2691 0.0034  -0.0066 0.0228  230  ALA A C   
1597  O O   . ALA A 232  ? 0.2494 0.2056 0.2581 0.0032  -0.0058 0.0237  230  ALA A O   
1598  C CB  . ALA A 232  ? 0.2420 0.1923 0.2583 0.0067  -0.0092 0.0194  230  ALA A CB  
1599  N N   . ALA A 233  ? 0.2480 0.2032 0.2574 0.0014  -0.0077 0.0247  231  ALA A N   
1600  C CA  . ALA A 233  ? 0.2912 0.2494 0.2993 -0.0011 -0.0079 0.0279  231  ALA A CA  
1601  C C   . ALA A 233  ? 0.2577 0.2185 0.2613 -0.0012 -0.0053 0.0268  231  ALA A C   
1602  O O   . ALA A 233  ? 0.2956 0.2590 0.2985 -0.0023 -0.0051 0.0283  231  ALA A O   
1603  C CB  . ALA A 233  ? 0.3142 0.2732 0.3231 -0.0033 -0.0094 0.0302  231  ALA A CB  
1604  N N   . ASP A 234  ? 0.2519 0.2125 0.2529 0.0000  -0.0035 0.0243  232  ASP A N   
1605  C CA  . ASP A 234  ? 0.2699 0.2326 0.2676 0.0001  -0.0014 0.0232  232  ASP A CA  
1606  C C   . ASP A 234  ? 0.2675 0.2302 0.2658 0.0012  -0.0006 0.0227  232  ASP A C   
1607  O O   . ASP A 234  ? 0.2681 0.2330 0.2651 0.0005  0.0001  0.0231  232  ASP A O   
1608  C CB  . ASP A 234  ? 0.3214 0.2832 0.3171 0.0016  0.0002  0.0207  232  ASP A CB  
1609  C CG  . ASP A 234  ? 0.4333 0.3957 0.4276 0.0006  0.0000  0.0207  232  ASP A CG  
1610  O OD1 . ASP A 234  ? 0.3961 0.3605 0.3904 -0.0014 -0.0009 0.0226  232  ASP A OD1 
1611  O OD2 . ASP A 234  ? 0.3539 0.3151 0.3470 0.0020  0.0009  0.0187  232  ASP A OD2 
1612  N N   . ALA A 235  ? 0.2489 0.2093 0.2490 0.0031  -0.0007 0.0216  233  ALA A N   
1613  C CA  . ALA A 235  ? 0.2401 0.2008 0.2410 0.0042  0.0001  0.0212  233  ALA A CA  
1614  C C   . ALA A 235  ? 0.2662 0.2279 0.2689 0.0029  -0.0012 0.0234  233  ALA A C   
1615  O O   . ALA A 235  ? 0.2354 0.1986 0.2377 0.0028  -0.0004 0.0236  233  ALA A O   
1616  C CB  . ALA A 235  ? 0.2513 0.2102 0.2541 0.0065  0.0001  0.0195  233  ALA A CB  
1617  N N   . GLU A 236  ? 0.2450 0.2061 0.2499 0.0017  -0.0033 0.0253  234  GLU A N   
1618  C CA  . GLU A 236  ? 0.2299 0.1924 0.2364 0.0002  -0.0048 0.0279  234  GLU A CA  
1619  C C   . GLU A 236  ? 0.2495 0.2158 0.2532 -0.0017 -0.0041 0.0290  234  GLU A C   
1620  O O   . GLU A 236  ? 0.2460 0.2143 0.2498 -0.0023 -0.0041 0.0298  234  GLU A O   
1621  C CB  . GLU A 236  ? 0.3015 0.2628 0.3114 -0.0008 -0.0074 0.0302  234  GLU A CB  
1622  C CG  . GLU A 236  ? 0.3628 0.3208 0.3768 0.0011  -0.0086 0.0290  234  GLU A CG  
1623  C CD  . GLU A 236  ? 0.5119 0.4679 0.5293 0.0003  -0.0112 0.0304  234  GLU A CD  
1624  O OE1 . GLU A 236  ? 0.5807 0.5383 0.5974 -0.0020 -0.0120 0.0330  234  GLU A OE1 
1625  O OE2 . GLU A 236  ? 0.5795 0.5326 0.6004 0.0021  -0.0124 0.0288  234  GLU A OE2 
1626  N N   . ARG A 237  ? 0.2568 0.2243 0.2581 -0.0026 -0.0036 0.0287  235  ARG A N   
1627  C CA  . ARG A 237  ? 0.2575 0.2292 0.2562 -0.0042 -0.0030 0.0290  235  ARG A CA  
1628  C C   . ARG A 237  ? 0.2877 0.2601 0.2850 -0.0031 -0.0012 0.0268  235  ARG A C   
1629  O O   . ARG A 237  ? 0.2512 0.2266 0.2479 -0.0040 -0.0012 0.0271  235  ARG A O   
1630  C CB  . ARG A 237  ? 0.2907 0.2636 0.2874 -0.0050 -0.0026 0.0288  235  ARG A CB  
1631  C CG  . ARG A 237  ? 0.3883 0.3659 0.3823 -0.0063 -0.0018 0.0283  235  ARG A CG  
1632  C CD  . ARG A 237  ? 0.4685 0.4481 0.4610 -0.0074 -0.0018 0.0285  235  ARG A CD  
1633  N NE  . ARG A 237  ? 0.5217 0.4976 0.5139 -0.0060 -0.0010 0.0267  235  ARG A NE  
1634  C CZ  . ARG A 237  ? 0.5719 0.5474 0.5622 -0.0048 0.0007  0.0240  235  ARG A CZ  
1635  N NH1 . ARG A 237  ? 0.5849 0.5634 0.5739 -0.0049 0.0017  0.0225  235  ARG A NH1 
1636  N NH2 . ARG A 237  ? 0.4851 0.4575 0.4752 -0.0035 0.0012  0.0226  235  ARG A NH2 
1637  N N   . TYR A 238  ? 0.2344 0.2042 0.2313 -0.0013 0.0002  0.0246  236  TYR A N   
1638  C CA  . TYR A 238  ? 0.2258 0.1962 0.2220 -0.0005 0.0017  0.0230  236  TYR A CA  
1639  C C   . TYR A 238  ? 0.2273 0.1978 0.2256 -0.0001 0.0014  0.0237  236  TYR A C   
1640  O O   . TYR A 238  ? 0.2274 0.1998 0.2257 -0.0005 0.0018  0.0232  236  TYR A O   
1641  C CB  . TYR A 238  ? 0.2177 0.1859 0.2134 0.0013  0.0032  0.0211  236  TYR A CB  
1642  C CG  . TYR A 238  ? 0.2282 0.1967 0.2218 0.0011  0.0038  0.0201  236  TYR A CG  
1643  C CD1 . TYR A 238  ? 0.3041 0.2755 0.2963 -0.0003 0.0038  0.0198  236  TYR A CD1 
1644  C CD2 . TYR A 238  ? 0.2494 0.2158 0.2426 0.0023  0.0043  0.0192  236  TYR A CD2 
1645  C CE1 . TYR A 238  ? 0.3435 0.3153 0.3340 -0.0005 0.0043  0.0188  236  TYR A CE1 
1646  C CE2 . TYR A 238  ? 0.3172 0.2839 0.3086 0.0021  0.0047  0.0183  236  TYR A CE2 
1647  C CZ  . TYR A 238  ? 0.3325 0.3018 0.3227 0.0007  0.0048  0.0182  236  TYR A CZ  
1648  O OH  . TYR A 238  ? 0.3406 0.3102 0.3292 0.0006  0.0052  0.0172  236  TYR A OH  
1649  N N   . TYR A 239  ? 0.2048 0.1732 0.2053 0.0006  0.0004  0.0246  237  TYR A N   
1650  C CA  . TYR A 239  ? 0.2088 0.1775 0.2116 0.0008  -0.0001 0.0255  237  TYR A CA  
1651  C C   . TYR A 239  ? 0.2212 0.1930 0.2238 -0.0011 -0.0012 0.0271  237  TYR A C   
1652  O O   . TYR A 239  ? 0.2210 0.1944 0.2239 -0.0012 -0.0009 0.0268  237  TYR A O   
1653  C CB  . TYR A 239  ? 0.2290 0.1952 0.2346 0.0018  -0.0014 0.0262  237  TYR A CB  
1654  C CG  . TYR A 239  ? 0.2377 0.2043 0.2458 0.0021  -0.0020 0.0271  237  TYR A CG  
1655  C CD1 . TYR A 239  ? 0.2650 0.2332 0.2743 0.0005  -0.0037 0.0294  237  TYR A CD1 
1656  C CD2 . TYR A 239  ? 0.2493 0.2152 0.2585 0.0039  -0.0007 0.0257  237  TYR A CD2 
1657  C CE1 . TYR A 239  ? 0.2908 0.2594 0.3025 0.0008  -0.0043 0.0301  237  TYR A CE1 
1658  C CE2 . TYR A 239  ? 0.2783 0.2449 0.2900 0.0042  -0.0012 0.0264  237  TYR A CE2 
1659  C CZ  . TYR A 239  ? 0.2752 0.2429 0.2881 0.0027  -0.0030 0.0285  237  TYR A CZ  
1660  O OH  . TYR A 239  ? 0.3389 0.3073 0.3543 0.0030  -0.0036 0.0293  237  TYR A OH  
1661  N N   . ARG A 240  ? 0.2161 0.1892 0.2185 -0.0027 -0.0027 0.0291  238  ARG A N   
1662  C CA  . ARG A 240  ? 0.2109 0.1880 0.2132 -0.0045 -0.0038 0.0309  238  ARG A CA  
1663  C C   . ARG A 240  ? 0.2054 0.1862 0.2051 -0.0052 -0.0027 0.0292  238  ARG A C   
1664  O O   . ARG A 240  ? 0.2167 0.2008 0.2165 -0.0060 -0.0032 0.0295  238  ARG A O   
1665  C CB  . ARG A 240  ? 0.2732 0.2515 0.2763 -0.0062 -0.0058 0.0340  238  ARG A CB  
1666  C CG  . ARG A 240  ? 0.3055 0.2853 0.3063 -0.0072 -0.0055 0.0340  238  ARG A CG  
1667  C CD  . ARG A 240  ? 0.2633 0.2449 0.2655 -0.0092 -0.0076 0.0378  238  ARG A CD  
1668  N NE  . ARG A 240  ? 0.3033 0.2856 0.3040 -0.0099 -0.0073 0.0377  238  ARG A NE  
1669  C CZ  . ARG A 240  ? 0.3428 0.3210 0.3449 -0.0093 -0.0078 0.0377  238  ARG A CZ  
1670  N NH1 . ARG A 240  ? 0.2905 0.2642 0.2960 -0.0080 -0.0088 0.0378  238  ARG A NH1 
1671  N NH2 . ARG A 240  ? 0.3846 0.3638 0.3851 -0.0100 -0.0073 0.0373  238  ARG A NH2 
1672  N N   . ASP A 241  ? 0.2050 0.1853 0.2028 -0.0047 -0.0014 0.0271  239  ASP A N   
1673  C CA  . ASP A 241  ? 0.2088 0.1920 0.2049 -0.0049 -0.0004 0.0248  239  ASP A CA  
1674  C C   . ASP A 241  ? 0.2205 0.2029 0.2183 -0.0038 0.0003  0.0233  239  ASP A C   
1675  O O   . ASP A 241  ? 0.2316 0.2171 0.2294 -0.0044 0.0001  0.0222  239  ASP A O   
1676  C CB  . ASP A 241  ? 0.2744 0.2568 0.2688 -0.0044 0.0008  0.0229  239  ASP A CB  
1677  C CG  . ASP A 241  ? 0.4008 0.3854 0.3937 -0.0058 0.0001  0.0241  239  ASP A CG  
1678  O OD1 . ASP A 241  ? 0.4822 0.4694 0.4753 -0.0073 -0.0012 0.0267  239  ASP A OD1 
1679  O OD2 . ASP A 241  ? 0.5341 0.5177 0.5257 -0.0053 0.0010  0.0228  239  ASP A OD2 
1680  N N   . TYR A 242  ? 0.2154 0.1938 0.2146 -0.0022 0.0010  0.0231  240  TYR A N   
1681  C CA  . TYR A 242  ? 0.2073 0.1851 0.2084 -0.0013 0.0016  0.0222  240  TYR A CA  
1682  C C   . TYR A 242  ? 0.1998 0.1792 0.2024 -0.0020 0.0004  0.0235  240  TYR A C   
1683  O O   . TYR A 242  ? 0.2034 0.1847 0.2071 -0.0022 0.0004  0.0226  240  TYR A O   
1684  C CB  . TYR A 242  ? 0.1947 0.1689 0.1969 0.0004  0.0027  0.0221  240  TYR A CB  
1685  C CG  . TYR A 242  ? 0.2076 0.1804 0.2087 0.0013  0.0040  0.0207  240  TYR A CG  
1686  C CD1 . TYR A 242  ? 0.2335 0.2075 0.2340 0.0010  0.0046  0.0191  240  TYR A CD1 
1687  C CD2 . TYR A 242  ? 0.2184 0.1887 0.2194 0.0027  0.0046  0.0208  240  TYR A CD2 
1688  C CE1 . TYR A 242  ? 0.2352 0.2078 0.2350 0.0019  0.0057  0.0181  240  TYR A CE1 
1689  C CE2 . TYR A 242  ? 0.2059 0.1753 0.2059 0.0035  0.0058  0.0198  240  TYR A CE2 
1690  C CZ  . TYR A 242  ? 0.1908 0.1612 0.1902 0.0031  0.0064  0.0186  240  TYR A CZ  
1691  O OH  . TYR A 242  ? 0.2177 0.1872 0.2164 0.0039  0.0074  0.0179  240  TYR A OH  
1692  N N   . GLU A 243  ? 0.1842 0.1631 0.1875 -0.0023 -0.0008 0.0257  241  GLU A N   
1693  C CA  . GLU A 243  ? 0.1970 0.1774 0.2021 -0.0029 -0.0021 0.0273  241  GLU A CA  
1694  C C   . GLU A 243  ? 0.2031 0.1885 0.2070 -0.0046 -0.0029 0.0273  241  GLU A C   
1695  O O   . GLU A 243  ? 0.2036 0.1909 0.2085 -0.0048 -0.0033 0.0269  241  GLU A O   
1696  C CB  . GLU A 243  ? 0.2163 0.1951 0.2229 -0.0030 -0.0035 0.0299  241  GLU A CB  
1697  C CG  . GLU A 243  ? 0.2600 0.2403 0.2687 -0.0037 -0.0052 0.0320  241  GLU A CG  
1698  C CD  . GLU A 243  ? 0.3056 0.2847 0.3160 -0.0042 -0.0070 0.0348  241  GLU A CD  
1699  O OE1 . GLU A 243  ? 0.3838 0.3626 0.3930 -0.0049 -0.0073 0.0355  241  GLU A OE1 
1700  O OE2 . GLU A 243  ? 0.2748 0.2532 0.2882 -0.0040 -0.0082 0.0363  241  GLU A OE2 
1701  N N   . SER A 244  ? 0.2098 0.1977 0.2113 -0.0058 -0.0032 0.0276  242  SER A N   
1702  C CA  . SER A 244  ? 0.1958 0.1895 0.1959 -0.0073 -0.0039 0.0274  242  SER A CA  
1703  C C   . SER A 244  ? 0.2057 0.2009 0.2057 -0.0067 -0.0030 0.0238  242  SER A C   
1704  O O   . SER A 244  ? 0.2296 0.2289 0.2299 -0.0074 -0.0037 0.0230  242  SER A O   
1705  C CB  . SER A 244  ? 0.2325 0.2292 0.2302 -0.0087 -0.0043 0.0285  242  SER A CB  
1706  O OG  . SER A 244  ? 0.2823 0.2775 0.2786 -0.0080 -0.0029 0.0262  242  SER A OG  
1707  N N   . ALA A 245  ? 0.1986 0.1907 0.1986 -0.0055 -0.0016 0.0217  243  ALA A N   
1708  C CA  . ALA A 245  ? 0.1901 0.1830 0.1911 -0.0050 -0.0010 0.0185  243  ALA A CA  
1709  C C   . ALA A 245  ? 0.1951 0.1868 0.1990 -0.0044 -0.0012 0.0184  243  ALA A C   
1710  O O   . ALA A 245  ? 0.2116 0.2061 0.2168 -0.0046 -0.0017 0.0163  243  ALA A O   
1711  C CB  . ALA A 245  ? 0.2249 0.2146 0.2257 -0.0038 0.0004  0.0168  243  ALA A CB  
1712  N N   . ILE A 246  ? 0.1973 0.1853 0.2026 -0.0036 -0.0010 0.0203  244  ILE A N   
1713  C CA  . ILE A 246  ? 0.1906 0.1779 0.1989 -0.0031 -0.0012 0.0205  244  ILE A CA  
1714  C C   . ILE A 246  ? 0.2131 0.2046 0.2217 -0.0043 -0.0027 0.0209  244  ILE A C   
1715  O O   . ILE A 246  ? 0.2147 0.2077 0.2254 -0.0043 -0.0031 0.0195  244  ILE A O   
1716  C CB  . ILE A 246  ? 0.1914 0.1749 0.2011 -0.0020 -0.0006 0.0224  244  ILE A CB  
1717  C CG1 . ILE A 246  ? 0.1966 0.1769 0.2064 -0.0007 0.0010  0.0216  244  ILE A CG1 
1718  C CG2 . ILE A 246  ? 0.2135 0.1972 0.2262 -0.0017 -0.0011 0.0230  244  ILE A CG2 
1719  C CD1 . ILE A 246  ? 0.2224 0.1998 0.2328 0.0005  0.0016  0.0230  244  ILE A CD1 
1720  N N   . HIS A 247  ? 0.1903 0.1841 0.1971 -0.0054 -0.0038 0.0230  245  HIS A N   
1721  C CA  . HIS A 247  ? 0.1843 0.1829 0.1913 -0.0066 -0.0054 0.0238  245  HIS A CA  
1722  C C   . HIS A 247  ? 0.1994 0.2027 0.2055 -0.0071 -0.0056 0.0206  245  HIS A C   
1723  O O   . HIS A 247  ? 0.2127 0.2188 0.2204 -0.0073 -0.0064 0.0193  245  HIS A O   
1724  C CB  . HIS A 247  ? 0.2139 0.2146 0.2193 -0.0078 -0.0066 0.0270  245  HIS A CB  
1725  C CG  . HIS A 247  ? 0.2427 0.2397 0.2501 -0.0074 -0.0071 0.0300  245  HIS A CG  
1726  N ND1 . HIS A 247  ? 0.2290 0.2254 0.2389 -0.0071 -0.0079 0.0311  245  HIS A ND1 
1727  C CD2 . HIS A 247  ? 0.2450 0.2386 0.2525 -0.0071 -0.0071 0.0320  245  HIS A CD2 
1728  C CE1 . HIS A 247  ? 0.2673 0.2603 0.2790 -0.0066 -0.0084 0.0334  245  HIS A CE1 
1729  N NE2 . HIS A 247  ? 0.2407 0.2318 0.2510 -0.0066 -0.0080 0.0339  245  HIS A NE2 
1730  N N   . ALA A 248  ? 0.1949 0.1996 0.1988 -0.0073 -0.0049 0.0189  246  ALA A N   
1731  C CA  . ALA A 248  ? 0.2039 0.2137 0.2073 -0.0076 -0.0053 0.0154  246  ALA A CA  
1732  C C   . ALA A 248  ? 0.2067 0.2144 0.2134 -0.0065 -0.0050 0.0122  246  ALA A C   
1733  O O   . ALA A 248  ? 0.2138 0.2254 0.2219 -0.0067 -0.0060 0.0098  246  ALA A O   
1734  C CB  . ALA A 248  ? 0.2109 0.2223 0.2116 -0.0078 -0.0046 0.0143  246  ALA A CB  
1735  N N   . ILE A 249  ? 0.2017 0.2035 0.2100 -0.0054 -0.0038 0.0124  247  ILE A N   
1736  C CA  . ILE A 249  ? 0.1955 0.1951 0.2075 -0.0045 -0.0035 0.0101  247  ILE A CA  
1737  C C   . ILE A 249  ? 0.1961 0.1957 0.2110 -0.0045 -0.0044 0.0109  247  ILE A C   
1738  O O   . ILE A 249  ? 0.2167 0.2178 0.2347 -0.0044 -0.0052 0.0084  247  ILE A O   
1739  C CB  . ILE A 249  ? 0.1974 0.1914 0.2101 -0.0034 -0.0020 0.0109  247  ILE A CB  
1740  C CG1 . ILE A 249  ? 0.2043 0.1983 0.2146 -0.0033 -0.0013 0.0096  247  ILE A CG1 
1741  C CG2 . ILE A 249  ? 0.2122 0.2038 0.2294 -0.0026 -0.0019 0.0096  247  ILE A CG2 
1742  C CD1 . ILE A 249  ? 0.2137 0.2029 0.2235 -0.0024 0.0002  0.0113  247  ILE A CD1 
1743  N N   . GLY A 250  ? 0.1875 0.1856 0.2018 -0.0046 -0.0044 0.0143  248  GLY A N   
1744  C CA  . GLY A 250  ? 0.2054 0.2037 0.2226 -0.0046 -0.0052 0.0152  248  GLY A CA  
1745  C C   . GLY A 250  ? 0.2038 0.2078 0.2207 -0.0057 -0.0069 0.0141  248  GLY A C   
1746  O O   . GLY A 250  ? 0.2174 0.2224 0.2374 -0.0057 -0.0077 0.0129  248  GLY A O   
1747  N N   . LYS A 251  ? 0.2020 0.2102 0.2154 -0.0067 -0.0075 0.0146  249  LYS A N   
1748  C CA  . LYS A 251  ? 0.2189 0.2338 0.2317 -0.0077 -0.0091 0.0134  249  LYS A CA  
1749  C C   . LYS A 251  ? 0.2254 0.2428 0.2400 -0.0073 -0.0095 0.0085  249  LYS A C   
1750  O O   . LYS A 251  ? 0.2321 0.2532 0.2487 -0.0075 -0.0108 0.0066  249  LYS A O   
1751  C CB  . LYS A 251  ? 0.2385 0.2583 0.2472 -0.0089 -0.0095 0.0149  249  LYS A CB  
1752  C CG  . LYS A 251  ? 0.2316 0.2503 0.2392 -0.0096 -0.0099 0.0198  249  LYS A CG  
1753  C CD  . LYS A 251  ? 0.2642 0.2872 0.2681 -0.0108 -0.0101 0.0212  249  LYS A CD  
1754  C CE  . LYS A 251  ? 0.2605 0.2825 0.2639 -0.0116 -0.0108 0.0263  249  LYS A CE  
1755  N NZ  . LYS A 251  ? 0.2526 0.2792 0.2529 -0.0130 -0.0110 0.0278  249  LYS A NZ  
1756  N N   . ALA A 252  ? 0.2236 0.2392 0.2381 -0.0067 -0.0085 0.0062  250  ALA A N   
1757  C CA  . ALA A 252  ? 0.2353 0.2530 0.2522 -0.0062 -0.0091 0.0013  250  ALA A CA  
1758  C C   . ALA A 252  ? 0.2407 0.2542 0.2629 -0.0054 -0.0093 0.0003  250  ALA A C   
1759  O O   . ALA A 252  ? 0.2487 0.2647 0.2742 -0.0053 -0.0106 -0.0033 250  ALA A O   
1760  C CB  . ALA A 252  ? 0.2790 0.2957 0.2945 -0.0057 -0.0080 -0.0005 250  ALA A CB  
1761  N N   . SER A 253  ? 0.2396 0.2470 0.2630 -0.0049 -0.0080 0.0034  251  SER A N   
1762  C CA  . SER A 253  ? 0.2252 0.2292 0.2539 -0.0043 -0.0082 0.0031  251  SER A CA  
1763  C C   . SER A 253  ? 0.2456 0.2526 0.2766 -0.0048 -0.0098 0.0026  251  SER A C   
1764  O O   . SER A 253  ? 0.2483 0.2554 0.2841 -0.0046 -0.0108 0.0000  251  SER A O   
1765  C CB  . SER A 253  ? 0.2244 0.2230 0.2533 -0.0038 -0.0065 0.0070  251  SER A CB  
1766  O OG  . SER A 253  ? 0.2257 0.2217 0.2597 -0.0034 -0.0066 0.0072  251  SER A OG  
1767  N N   . ALA A 254  ? 0.2382 0.2478 0.2664 -0.0055 -0.0102 0.0050  252  ALA A N   
1768  C CA  . ALA A 254  ? 0.2605 0.2740 0.2902 -0.0061 -0.0119 0.0045  252  ALA A CA  
1769  C C   . ALA A 254  ? 0.2863 0.2967 0.3215 -0.0056 -0.0122 0.0046  252  ALA A C   
1770  O O   . ALA A 254  ? 0.2858 0.2988 0.3245 -0.0058 -0.0138 0.0018  252  ALA A O   
1771  C CB  . ALA A 254  ? 0.3110 0.3312 0.3399 -0.0065 -0.0134 0.0003  252  ALA A CB  
1772  N N   . GLY A 255  ? 0.2579 0.2632 0.2943 -0.0051 -0.0107 0.0077  253  GLY A N   
1773  C CA  . GLY A 255  ? 0.2592 0.2620 0.3006 -0.0048 -0.0108 0.0086  253  GLY A CA  
1774  C C   . GLY A 255  ? 0.2375 0.2379 0.2839 -0.0044 -0.0108 0.0065  253  GLY A C   
1775  O O   . GLY A 255  ? 0.3013 0.3004 0.3527 -0.0044 -0.0112 0.0072  253  GLY A O   
1776  N N   . ARG A 256  ? 0.2374 0.2373 0.2830 -0.0041 -0.0105 0.0042  254  ARG A N   
1777  C CA  . ARG A 256  ? 0.2435 0.2410 0.2946 -0.0038 -0.0107 0.0026  254  ARG A CA  
1778  C C   . ARG A 256  ? 0.2470 0.2399 0.3001 -0.0033 -0.0090 0.0063  254  ARG A C   
1779  O O   . ARG A 256  ? 0.2613 0.2522 0.3199 -0.0033 -0.0093 0.0062  254  ARG A O   
1780  C CB  . ARG A 256  ? 0.2361 0.2341 0.2860 -0.0035 -0.0109 -0.0007 254  ARG A CB  
1781  C CG  . ARG A 256  ? 0.2831 0.2860 0.3342 -0.0038 -0.0131 -0.0057 254  ARG A CG  
1782  C CD  . ARG A 256  ? 0.3068 0.3107 0.3565 -0.0033 -0.0131 -0.0090 254  ARG A CD  
1783  N NE  . ARG A 256  ? 0.2532 0.2591 0.2958 -0.0035 -0.0118 -0.0078 254  ARG A NE  
1784  C CZ  . ARG A 256  ? 0.2889 0.2958 0.3291 -0.0032 -0.0114 -0.0098 254  ARG A CZ  
1785  N NH1 . ARG A 256  ? 0.2995 0.3051 0.3437 -0.0025 -0.0119 -0.0130 254  ARG A NH1 
1786  N NH2 . ARG A 256  ? 0.2759 0.2853 0.3099 -0.0036 -0.0104 -0.0085 254  ARG A NH2 
1787  N N   . GLY A 257  ? 0.2118 0.2033 0.2607 -0.0030 -0.0073 0.0097  255  GLY A N   
1788  C CA  . GLY A 257  ? 0.2209 0.2092 0.2714 -0.0025 -0.0056 0.0130  255  GLY A CA  
1789  C C   . GLY A 257  ? 0.2087 0.1946 0.2580 -0.0019 -0.0044 0.0132  255  GLY A C   
1790  O O   . GLY A 257  ? 0.2223 0.2087 0.2698 -0.0020 -0.0047 0.0107  255  GLY A O   
1791  N N   . ILE A 258  ? 0.1996 0.1833 0.2503 -0.0014 -0.0028 0.0162  256  ILE A N   
1792  C CA  . ILE A 258  ? 0.1920 0.1738 0.2405 -0.0008 -0.0013 0.0171  256  ILE A CA  
1793  C C   . ILE A 258  ? 0.2303 0.2110 0.2829 -0.0009 -0.0019 0.0159  256  ILE A C   
1794  O O   . ILE A 258  ? 0.2186 0.1980 0.2692 -0.0005 -0.0011 0.0159  256  ILE A O   
1795  C CB  . ILE A 258  ? 0.1900 0.1708 0.2377 -0.0001 0.0006  0.0207  256  ILE A CB  
1796  C CG1 . ILE A 258  ? 0.2331 0.2142 0.2869 -0.0002 0.0006  0.0228  256  ILE A CG1 
1797  C CG2 . ILE A 258  ? 0.2170 0.1986 0.2609 0.0003  0.0010  0.0216  256  ILE A CG2 
1798  C CD1 . ILE A 258  ? 0.2264 0.2077 0.2796 0.0006  0.0026  0.0262  256  ILE A CD1 
1799  N N   . TYR A 259  ? 0.2295 0.2105 0.2882 -0.0015 -0.0035 0.0150  257  TYR A N   
1800  C CA  . TYR A 259  ? 0.2130 0.1926 0.2768 -0.0016 -0.0044 0.0140  257  TYR A CA  
1801  C C   . TYR A 259  ? 0.2659 0.2466 0.3302 -0.0018 -0.0063 0.0091  257  TYR A C   
1802  O O   . TYR A 259  ? 0.2778 0.2576 0.3416 -0.0014 -0.0063 0.0075  257  TYR A O   
1803  C CB  . TYR A 259  ? 0.2603 0.2395 0.3318 -0.0021 -0.0051 0.0160  257  TYR A CB  
1804  C CG  . TYR A 259  ? 0.2381 0.2174 0.3090 -0.0019 -0.0032 0.0207  257  TYR A CG  
1805  C CD1 . TYR A 259  ? 0.2622 0.2407 0.3305 -0.0013 -0.0012 0.0234  257  TYR A CD1 
1806  C CD2 . TYR A 259  ? 0.2419 0.2227 0.3148 -0.0022 -0.0033 0.0222  257  TYR A CD2 
1807  C CE1 . TYR A 259  ? 0.2538 0.2333 0.3214 -0.0009 0.0006  0.0272  257  TYR A CE1 
1808  C CE2 . TYR A 259  ? 0.2657 0.2472 0.3381 -0.0019 -0.0014 0.0261  257  TYR A CE2 
1809  C CZ  . TYR A 259  ? 0.2529 0.2339 0.3225 -0.0012 0.0005  0.0285  257  TYR A CZ  
1810  O OH  . TYR A 259  ? 0.2454 0.2281 0.3145 -0.0006 0.0024  0.0320  257  TYR A OH  
1811  N N   . GLU A 260  ? 0.2290 0.2121 0.2943 -0.0022 -0.0079 0.0065  258  GLU A N   
1812  C CA  . GLU A 260  ? 0.2689 0.2542 0.3344 -0.0022 -0.0097 0.0014  258  GLU A CA  
1813  C C   . GLU A 260  ? 0.2867 0.2739 0.3444 -0.0020 -0.0087 0.0002  258  GLU A C   
1814  O O   . GLU A 260  ? 0.3294 0.3180 0.3863 -0.0017 -0.0094 -0.0033 258  GLU A O   
1815  C CB  . GLU A 260  ? 0.3050 0.2931 0.3737 -0.0027 -0.0118 -0.0011 258  GLU A CB  
1816  C CG  . GLU A 260  ? 0.4058 0.3972 0.4749 -0.0026 -0.0137 -0.0069 258  GLU A CG  
1817  C CD  . GLU A 260  ? 0.4893 0.4845 0.5602 -0.0030 -0.0157 -0.0097 258  GLU A CD  
1818  O OE1 . GLU A 260  ? 0.5067 0.5011 0.5812 -0.0034 -0.0162 -0.0076 258  GLU A OE1 
1819  O OE2 . GLU A 260  ? 0.4484 0.4480 0.5170 -0.0029 -0.0168 -0.0141 258  GLU A OE2 
1820  N N   . GLY A 261  ? 0.2281 0.2157 0.2805 -0.0021 -0.0073 0.0030  259  GLY A N   
1821  C CA  . GLY A 261  ? 0.2163 0.2061 0.2620 -0.0021 -0.0068 0.0023  259  GLY A CA  
1822  C C   . GLY A 261  ? 0.2200 0.2075 0.2619 -0.0016 -0.0050 0.0040  259  GLY A C   
1823  O O   . GLY A 261  ? 0.2111 0.1953 0.2547 -0.0012 -0.0039 0.0063  259  GLY A O   
1824  N N   . PRO A 262  ? 0.2116 0.2012 0.2482 -0.0018 -0.0047 0.0030  260  PRO A N   
1825  C CA  . PRO A 262  ? 0.2104 0.1982 0.2433 -0.0013 -0.0032 0.0040  260  PRO A CA  
1826  C C   . PRO A 262  ? 0.2097 0.1951 0.2399 -0.0011 -0.0016 0.0081  260  PRO A C   
1827  O O   . PRO A 262  ? 0.2422 0.2281 0.2720 -0.0013 -0.0017 0.0099  260  PRO A O   
1828  C CB  . PRO A 262  ? 0.2145 0.2062 0.2430 -0.0018 -0.0037 0.0018  260  PRO A CB  
1829  C CG  . PRO A 262  ? 0.2408 0.2362 0.2690 -0.0025 -0.0049 0.0015  260  PRO A CG  
1830  C CD  . PRO A 262  ? 0.2281 0.2226 0.2623 -0.0024 -0.0059 0.0006  260  PRO A CD  
1831  N N   . GLY A 263  ? 0.2033 0.1862 0.2317 -0.0005 -0.0003 0.0093  261  GLY A N   
1832  C CA  . GLY A 263  ? 0.2026 0.1837 0.2281 -0.0001 0.0011  0.0124  261  GLY A CA  
1833  C C   . GLY A 263  ? 0.1814 0.1619 0.2025 0.0001  0.0020  0.0124  261  GLY A C   
1834  O O   . GLY A 263  ? 0.1994 0.1815 0.2192 -0.0002 0.0015  0.0100  261  GLY A O   
1835  N N   . ILE A 264  ? 0.1943 0.1729 0.2133 0.0007  0.0032  0.0147  262  ILE A N   
1836  C CA  . ILE A 264  ? 0.1998 0.1776 0.2150 0.0009  0.0039  0.0149  262  ILE A CA  
1837  C C   . ILE A 264  ? 0.1956 0.1708 0.2111 0.0020  0.0053  0.0163  262  ILE A C   
1838  O O   . ILE A 264  ? 0.1953 0.1698 0.2132 0.0026  0.0059  0.0178  262  ILE A O   
1839  C CB  . ILE A 264  ? 0.2128 0.1912 0.2248 0.0006  0.0036  0.0162  262  ILE A CB  
1840  C CG1 . ILE A 264  ? 0.2343 0.2126 0.2427 0.0004  0.0038  0.0159  262  ILE A CG1 
1841  C CG2 . ILE A 264  ? 0.2197 0.1964 0.2326 0.0014  0.0042  0.0185  262  ILE A CG2 
1842  C CD1 . ILE A 264  ? 0.2509 0.2300 0.2570 -0.0002 0.0032  0.0175  262  ILE A CD1 
1843  N N   . SER A 265  ? 0.1795 0.1540 0.1927 0.0023  0.0058  0.0157  263  SER A N   
1844  C CA  . SER A 265  ? 0.1922 0.1650 0.2049 0.0033  0.0071  0.0170  263  SER A CA  
1845  C C   . SER A 265  ? 0.2124 0.1845 0.2211 0.0035  0.0075  0.0173  263  SER A C   
1846  O O   . SER A 265  ? 0.2525 0.2255 0.2590 0.0028  0.0069  0.0163  263  SER A O   
1847  C CB  . SER A 265  ? 0.2199 0.1921 0.2339 0.0035  0.0073  0.0160  263  SER A CB  
1848  O OG  . SER A 265  ? 0.2366 0.2089 0.2553 0.0033  0.0069  0.0161  263  SER A OG  
1849  N N   . ILE A 266  ? 0.1962 0.1673 0.2044 0.0046  0.0084  0.0188  264  ILE A N   
1850  C CA  . ILE A 266  ? 0.2042 0.1745 0.2095 0.0050  0.0086  0.0189  264  ILE A CA  
1851  C C   . ILE A 266  ? 0.1931 0.1626 0.1975 0.0062  0.0098  0.0192  264  ILE A C   
1852  O O   . ILE A 266  ? 0.2028 0.1728 0.2092 0.0068  0.0106  0.0200  264  ILE A O   
1853  C CB  . ILE A 266  ? 0.2221 0.1923 0.2276 0.0053  0.0081  0.0199  264  ILE A CB  
1854  C CG1 . ILE A 266  ? 0.2339 0.2043 0.2414 0.0066  0.0091  0.0209  264  ILE A CG1 
1855  C CG2 . ILE A 266  ? 0.2246 0.1959 0.2310 0.0041  0.0069  0.0200  264  ILE A CG2 
1856  C CD1 . ILE A 266  ? 0.2411 0.2114 0.2491 0.0073  0.0087  0.0214  264  ILE A CD1 
1857  N N   . LYS A 267  ? 0.2053 0.1740 0.2071 0.0065  0.0098  0.0187  265  LYS A N   
1858  C CA  . LYS A 267  ? 0.1907 0.1591 0.1914 0.0077  0.0107  0.0188  265  LYS A CA  
1859  C C   . LYS A 267  ? 0.1905 0.1585 0.1905 0.0086  0.0106  0.0188  265  LYS A C   
1860  O O   . LYS A 267  ? 0.2033 0.1703 0.2023 0.0081  0.0095  0.0185  265  LYS A O   
1861  C CB  . LYS A 267  ? 0.2182 0.1861 0.2169 0.0074  0.0107  0.0179  265  LYS A CB  
1862  C CG  . LYS A 267  ? 0.2573 0.2255 0.2573 0.0070  0.0109  0.0176  265  LYS A CG  
1863  C CD  . LYS A 267  ? 0.3051 0.2730 0.3032 0.0068  0.0109  0.0165  265  LYS A CD  
1864  C CE  . LYS A 267  ? 0.4094 0.3776 0.4094 0.0065  0.0109  0.0160  265  LYS A CE  
1865  N NZ  . LYS A 267  ? 0.4188 0.3876 0.4214 0.0056  0.0101  0.0154  265  LYS A NZ  
1866  N N   . LEU A 268  ? 0.1909 0.1598 0.1915 0.0101  0.0115  0.0192  266  LEU A N   
1867  C CA  . LEU A 268  ? 0.2021 0.1709 0.2026 0.0113  0.0112  0.0186  266  LEU A CA  
1868  C C   . LEU A 268  ? 0.1964 0.1638 0.1947 0.0115  0.0106  0.0174  266  LEU A C   
1869  O O   . LEU A 268  ? 0.2138 0.1802 0.2126 0.0117  0.0095  0.0168  266  LEU A O   
1870  C CB  . LEU A 268  ? 0.2087 0.1799 0.2102 0.0130  0.0124  0.0189  266  LEU A CB  
1871  C CG  . LEU A 268  ? 0.2145 0.1873 0.2186 0.0128  0.0129  0.0203  266  LEU A CG  
1872  C CD1 . LEU A 268  ? 0.2367 0.2127 0.2417 0.0145  0.0143  0.0208  266  LEU A CD1 
1873  C CD2 . LEU A 268  ? 0.2592 0.2309 0.2648 0.0122  0.0117  0.0203  266  LEU A CD2 
1874  N N   . SER A 269  ? 0.1992 0.1666 0.1958 0.0113  0.0111  0.0171  267  SER A N   
1875  C CA  . SER A 269  ? 0.2080 0.1742 0.2028 0.0114  0.0105  0.0160  267  SER A CA  
1876  C C   . SER A 269  ? 0.2247 0.1894 0.2193 0.0098  0.0091  0.0161  267  SER A C   
1877  O O   . SER A 269  ? 0.2264 0.1900 0.2203 0.0098  0.0082  0.0154  267  SER A O   
1878  C CB  . SER A 269  ? 0.2233 0.1900 0.2164 0.0114  0.0114  0.0157  267  SER A CB  
1879  O OG  . SER A 269  ? 0.2260 0.1923 0.2190 0.0099  0.0112  0.0161  267  SER A OG  
1880  N N   . ALA A 270  ? 0.1949 0.1600 0.1903 0.0084  0.0087  0.0169  268  ALA A N   
1881  C CA  . ALA A 270  ? 0.2019 0.1666 0.1971 0.0068  0.0073  0.0174  268  ALA A CA  
1882  C C   . ALA A 270  ? 0.1949 0.1587 0.1918 0.0070  0.0061  0.0180  268  ALA A C   
1883  O O   . ALA A 270  ? 0.2105 0.1738 0.2075 0.0058  0.0046  0.0188  268  ALA A O   
1884  C CB  . ALA A 270  ? 0.2252 0.1913 0.2206 0.0054  0.0073  0.0179  268  ALA A CB  
1885  N N   . LEU A 271  ? 0.1965 0.1603 0.1951 0.0084  0.0064  0.0179  269  LEU A N   
1886  C CA  . LEU A 271  ? 0.2118 0.1749 0.2127 0.0086  0.0051  0.0184  269  LEU A CA  
1887  C C   . LEU A 271  ? 0.2180 0.1799 0.2201 0.0102  0.0044  0.0172  269  LEU A C   
1888  O O   . LEU A 271  ? 0.2322 0.1934 0.2370 0.0105  0.0030  0.0174  269  LEU A O   
1889  C CB  . LEU A 271  ? 0.2129 0.1772 0.2155 0.0091  0.0057  0.0190  269  LEU A CB  
1890  C CG  . LEU A 271  ? 0.2356 0.2011 0.2379 0.0074  0.0057  0.0200  269  LEU A CG  
1891  C CD1 . LEU A 271  ? 0.2675 0.2342 0.2718 0.0079  0.0064  0.0204  269  LEU A CD1 
1892  C CD2 . LEU A 271  ? 0.2645 0.2298 0.2672 0.0058  0.0039  0.0212  269  LEU A CD2 
1893  N N   . HIS A 272  ? 0.2154 0.1773 0.2160 0.0112  0.0052  0.0158  270  HIS A N   
1894  C CA  . HIS A 272  ? 0.2044 0.1654 0.2063 0.0127  0.0042  0.0141  270  HIS A CA  
1895  C C   . HIS A 272  ? 0.2070 0.1678 0.2066 0.0129  0.0047  0.0130  270  HIS A C   
1896  O O   . HIS A 272  ? 0.2265 0.1886 0.2238 0.0131  0.0063  0.0129  270  HIS A O   
1897  C CB  . HIS A 272  ? 0.2358 0.1984 0.2391 0.0150  0.0051  0.0127  270  HIS A CB  
1898  C CG  . HIS A 272  ? 0.2466 0.2084 0.2525 0.0166  0.0036  0.0106  270  HIS A CG  
1899  N ND1 . HIS A 272  ? 0.2632 0.2247 0.2684 0.0177  0.0032  0.0085  270  HIS A ND1 
1900  C CD2 . HIS A 272  ? 0.2872 0.2482 0.2967 0.0174  0.0021  0.0101  270  HIS A CD2 
1901  C CE1 . HIS A 272  ? 0.2854 0.2460 0.2940 0.0191  0.0015  0.0066  270  HIS A CE1 
1902  N NE2 . HIS A 272  ? 0.2946 0.2549 0.3061 0.0190  0.0008  0.0076  270  HIS A NE2 
1903  N N   . PRO A 273  ? 0.2379 0.1969 0.2385 0.0128  0.0031  0.0122  271  PRO A N   
1904  C CA  . PRO A 273  ? 0.2253 0.1842 0.2237 0.0130  0.0033  0.0110  271  PRO A CA  
1905  C C   . PRO A 273  ? 0.2301 0.1906 0.2278 0.0154  0.0044  0.0086  271  PRO A C   
1906  O O   . PRO A 273  ? 0.2435 0.2045 0.2391 0.0156  0.0050  0.0078  271  PRO A O   
1907  C CB  . PRO A 273  ? 0.2463 0.2028 0.2469 0.0121  0.0010  0.0111  271  PRO A CB  
1908  C CG  . PRO A 273  ? 0.2656 0.2212 0.2701 0.0128  -0.0005 0.0110  271  PRO A CG  
1909  C CD  . PRO A 273  ? 0.2408 0.1978 0.2448 0.0125  0.0007  0.0125  271  PRO A CD  
1910  N N   . ARG A 274  ? 0.2075 0.1694 0.2068 0.0172  0.0047  0.0075  272  ARG A N   
1911  C CA  . ARG A 274  ? 0.2063 0.1710 0.2047 0.0196  0.0058  0.0052  272  ARG A CA  
1912  C C   . ARG A 274  ? 0.2319 0.1999 0.2298 0.0204  0.0078  0.0061  272  ARG A C   
1913  O O   . ARG A 274  ? 0.2427 0.2133 0.2421 0.0223  0.0081  0.0046  272  ARG A O   
1914  C CB  . ARG A 274  ? 0.2321 0.1967 0.2335 0.0215  0.0042  0.0023  272  ARG A CB  
1915  C CG  . ARG A 274  ? 0.2222 0.1836 0.2248 0.0208  0.0020  0.0013  272  ARG A CG  
1916  C CD  . ARG A 274  ? 0.2411 0.2031 0.2404 0.0205  0.0028  0.0010  272  ARG A CD  
1917  N NE  . ARG A 274  ? 0.2527 0.2185 0.2501 0.0227  0.0043  -0.0012 272  ARG A NE  
1918  C CZ  . ARG A 274  ? 0.2400 0.2072 0.2387 0.0249  0.0034  -0.0047 272  ARG A CZ  
1919  N NH1 . ARG A 274  ? 0.2521 0.2168 0.2548 0.0253  0.0009  -0.0066 272  ARG A NH1 
1920  N NH2 . ARG A 274  ? 0.2493 0.2210 0.2458 0.0268  0.0050  -0.0063 272  ARG A NH2 
1921  N N   . TYR A 275  ? 0.2132 0.1814 0.2095 0.0188  0.0090  0.0085  273  TYR A N   
1922  C CA  . TYR A 275  ? 0.2075 0.1785 0.2038 0.0192  0.0107  0.0098  273  TYR A CA  
1923  C C   . TYR A 275  ? 0.2086 0.1831 0.2029 0.0205  0.0123  0.0094  273  TYR A C   
1924  O O   . TYR A 275  ? 0.2217 0.1962 0.2141 0.0196  0.0130  0.0106  273  TYR A O   
1925  C CB  . TYR A 275  ? 0.2057 0.1754 0.2019 0.0171  0.0110  0.0123  273  TYR A CB  
1926  C CG  . TYR A 275  ? 0.1941 0.1664 0.1908 0.0172  0.0125  0.0139  273  TYR A CG  
1927  C CD1 . TYR A 275  ? 0.2172 0.1918 0.2158 0.0185  0.0130  0.0138  273  TYR A CD1 
1928  C CD2 . TYR A 275  ? 0.1937 0.1662 0.1895 0.0161  0.0134  0.0155  273  TYR A CD2 
1929  C CE1 . TYR A 275  ? 0.2225 0.1999 0.2220 0.0185  0.0144  0.0156  273  TYR A CE1 
1930  C CE2 . TYR A 275  ? 0.2009 0.1758 0.1980 0.0161  0.0146  0.0172  273  TYR A CE2 
1931  C CZ  . TYR A 275  ? 0.2263 0.2037 0.2252 0.0172  0.0151  0.0175  273  TYR A CZ  
1932  O OH  . TYR A 275  ? 0.2287 0.2087 0.2292 0.0171  0.0162  0.0196  273  TYR A OH  
1933  N N   . SER A 276  ? 0.2003 0.1782 0.1952 0.0227  0.0127  0.0077  274  SER A N   
1934  C CA  . SER A 276  ? 0.1874 0.1697 0.1803 0.0240  0.0141  0.0074  274  SER A CA  
1935  C C   . SER A 276  ? 0.2011 0.1883 0.1953 0.0263  0.0148  0.0059  274  SER A C   
1936  O O   . SER A 276  ? 0.2064 0.1929 0.2030 0.0272  0.0137  0.0040  274  SER A O   
1937  C CB  . SER A 276  ? 0.2567 0.2381 0.2478 0.0245  0.0133  0.0053  274  SER A CB  
1938  O OG  . SER A 276  ? 0.2993 0.2803 0.2920 0.0261  0.0118  0.0019  274  SER A OG  
1939  N N   . ARG A 277  ? 0.2021 0.1948 0.1949 0.0273  0.0165  0.0068  275  ARG A N   
1940  C CA  . ARG A 277  ? 0.2007 0.1995 0.1942 0.0296  0.0174  0.0053  275  ARG A CA  
1941  C C   . ARG A 277  ? 0.2064 0.2058 0.2005 0.0318  0.0160  0.0006  275  ARG A C   
1942  O O   . ARG A 277  ? 0.2076 0.2098 0.2039 0.0336  0.0159  -0.0016 275  ARG A O   
1943  C CB  . ARG A 277  ? 0.2009 0.2061 0.1926 0.0301  0.0193  0.0074  275  ARG A CB  
1944  C CG  . ARG A 277  ? 0.2103 0.2236 0.2022 0.0326  0.0204  0.0057  275  ARG A CG  
1945  C CD  . ARG A 277  ? 0.2056 0.2203 0.2006 0.0330  0.0207  0.0060  275  ARG A CD  
1946  N NE  . ARG A 277  ? 0.2007 0.2239 0.1959 0.0356  0.0218  0.0042  275  ARG A NE  
1947  C CZ  . ARG A 277  ? 0.1969 0.2222 0.1931 0.0380  0.0209  -0.0007 275  ARG A CZ  
1948  N NH1 . ARG A 277  ? 0.2237 0.2429 0.2208 0.0382  0.0188  -0.0040 275  ARG A NH1 
1949  N NH2 . ARG A 277  ? 0.2066 0.2406 0.2033 0.0404  0.0221  -0.0023 275  ARG A NH2 
1950  N N   . ALA A 278  ? 0.2105 0.2075 0.2031 0.0317  0.0150  -0.0011 276  ALA A N   
1951  C CA  . ALA A 278  ? 0.2405 0.2380 0.2343 0.0338  0.0134  -0.0058 276  ALA A CA  
1952  C C   . ALA A 278  ? 0.2197 0.2127 0.2173 0.0338  0.0114  -0.0074 276  ALA A C   
1953  O O   . ALA A 278  ? 0.2552 0.2497 0.2552 0.0360  0.0102  -0.0114 276  ALA A O   
1954  C CB  . ALA A 278  ? 0.2457 0.2407 0.2375 0.0334  0.0124  -0.0069 276  ALA A CB  
1955  N N   . GLN A 279  ? 0.2151 0.2030 0.2136 0.0315  0.0110  -0.0045 277  GLN A N   
1956  C CA  . GLN A 279  ? 0.2114 0.1951 0.2136 0.0311  0.0090  -0.0051 277  GLN A CA  
1957  C C   . GLN A 279  ? 0.2247 0.2096 0.2285 0.0308  0.0099  -0.0031 277  GLN A C   
1958  O O   . GLN A 279  ? 0.2188 0.1996 0.2247 0.0294  0.0087  -0.0017 277  GLN A O   
1959  C CB  . GLN A 279  ? 0.2262 0.2036 0.2282 0.0285  0.0075  -0.0033 277  GLN A CB  
1960  C CG  . GLN A 279  ? 0.2443 0.2202 0.2453 0.0287  0.0064  -0.0053 277  GLN A CG  
1961  C CD  . GLN A 279  ? 0.2697 0.2458 0.2739 0.0309  0.0044  -0.0096 277  GLN A CD  
1962  O OE1 . GLN A 279  ? 0.4098 0.3843 0.4180 0.0314  0.0029  -0.0105 277  GLN A OE1 
1963  N NE2 . GLN A 279  ? 0.2606 0.2389 0.2636 0.0323  0.0043  -0.0124 277  GLN A NE2 
1964  N N   . ALA A 280  ? 0.2117 0.2026 0.2146 0.0322  0.0119  -0.0029 278  ALA A N   
1965  C CA  . ALA A 280  ? 0.2171 0.2095 0.2215 0.0316  0.0130  -0.0004 278  ALA A CA  
1966  C C   . ALA A 280  ? 0.2292 0.2196 0.2378 0.0323  0.0113  -0.0020 278  ALA A C   
1967  O O   . ALA A 280  ? 0.2117 0.2000 0.2217 0.0309  0.0112  0.0005  278  ALA A O   
1968  C CB  . ALA A 280  ? 0.2391 0.2391 0.2424 0.0331  0.0153  0.0001  278  ALA A CB  
1969  N N   . ALA A 281  ? 0.2245 0.2157 0.2354 0.0346  0.0098  -0.0062 279  ALA A N   
1970  C CA  . ALA A 281  ? 0.2340 0.2232 0.2496 0.0354  0.0079  -0.0077 279  ALA A CA  
1971  C C   . ALA A 281  ? 0.2299 0.2118 0.2468 0.0328  0.0059  -0.0054 279  ALA A C   
1972  O O   . ALA A 281  ? 0.2429 0.2231 0.2624 0.0321  0.0052  -0.0038 279  ALA A O   
1973  C CB  . ALA A 281  ? 0.2720 0.2632 0.2905 0.0384  0.0064  -0.0130 279  ALA A CB  
1974  N N   . ARG A 282  ? 0.2137 0.1919 0.2289 0.0314  0.0050  -0.0050 280  ARG A N   
1975  C CA  . ARG A 282  ? 0.2258 0.1982 0.2420 0.0288  0.0033  -0.0024 280  ARG A CA  
1976  C C   . ARG A 282  ? 0.2197 0.1919 0.2337 0.0265  0.0048  0.0017  280  ARG A C   
1977  O O   . ARG A 282  ? 0.2222 0.1914 0.2378 0.0248  0.0036  0.0038  280  ARG A O   
1978  C CB  . ARG A 282  ? 0.2551 0.2244 0.2699 0.0278  0.0021  -0.0027 280  ARG A CB  
1979  C CG  . ARG A 282  ? 0.2697 0.2380 0.2878 0.0296  -0.0002 -0.0066 280  ARG A CG  
1980  C CD  . ARG A 282  ? 0.2615 0.2260 0.2788 0.0279  -0.0016 -0.0060 280  ARG A CD  
1981  N NE  . ARG A 282  ? 0.2460 0.2063 0.2647 0.0252  -0.0030 -0.0024 280  ARG A NE  
1982  C CZ  . ARG A 282  ? 0.2554 0.2129 0.2728 0.0229  -0.0038 -0.0004 280  ARG A CZ  
1983  N NH1 . ARG A 282  ? 0.2532 0.2109 0.2681 0.0229  -0.0034 -0.0016 280  ARG A NH1 
1984  N NH2 . ARG A 282  ? 0.2841 0.2390 0.3028 0.0205  -0.0050 0.0030  280  ARG A NH2 
1985  N N   . VAL A 283  ? 0.2096 0.1848 0.2200 0.0263  0.0072  0.0028  281  VAL A N   
1986  C CA  . VAL A 283  ? 0.2107 0.1858 0.2197 0.0243  0.0085  0.0063  281  VAL A CA  
1987  C C   . VAL A 283  ? 0.2126 0.1889 0.2244 0.0246  0.0085  0.0072  281  VAL A C   
1988  O O   . VAL A 283  ? 0.2101 0.1840 0.2228 0.0228  0.0079  0.0094  281  VAL A O   
1989  C CB  . VAL A 283  ? 0.2008 0.1792 0.2065 0.0244  0.0108  0.0073  281  VAL A CB  
1990  C CG1 . VAL A 283  ? 0.2446 0.2233 0.2500 0.0226  0.0119  0.0105  281  VAL A CG1 
1991  C CG2 . VAL A 283  ? 0.2203 0.1968 0.2233 0.0236  0.0105  0.0069  281  VAL A CG2 
1992  N N   . MET A 284  ? 0.2048 0.1852 0.2181 0.0269  0.0093  0.0053  282  MET A N   
1993  C CA  . MET A 284  ? 0.2211 0.2032 0.2374 0.0273  0.0094  0.0060  282  MET A CA  
1994  C C   . MET A 284  ? 0.2275 0.2058 0.2475 0.0271  0.0068  0.0055  282  MET A C   
1995  O O   . MET A 284  ? 0.2627 0.2402 0.2846 0.0262  0.0065  0.0073  282  MET A O   
1996  C CB  . MET A 284  ? 0.2075 0.1958 0.2246 0.0300  0.0109  0.0040  282  MET A CB  
1997  C CG  . MET A 284  ? 0.2438 0.2366 0.2577 0.0300  0.0134  0.0054  282  MET A CG  
1998  S SD  . MET A 284  ? 0.2651 0.2570 0.2777 0.0271  0.0147  0.0102  282  MET A SD  
1999  C CE  . MET A 284  ? 0.2805 0.2748 0.2970 0.0275  0.0149  0.0112  282  MET A CE  
2000  N N   . GLY A 285  ? 0.2215 0.1972 0.2428 0.0279  0.0049  0.0031  283  GLY A N   
2001  C CA  . GLY A 285  ? 0.2349 0.2074 0.2606 0.0279  0.0022  0.0027  283  GLY A CA  
2002  C C   . GLY A 285  ? 0.2366 0.2045 0.2619 0.0249  0.0007  0.0058  283  GLY A C   
2003  O O   . GLY A 285  ? 0.2622 0.2280 0.2906 0.0241  -0.0010 0.0072  283  GLY A O   
2004  N N   . GLU A 286  ? 0.2273 0.1939 0.2487 0.0233  0.0014  0.0070  284  GLU A N   
2005  C CA  . GLU A 286  ? 0.2272 0.1903 0.2481 0.0206  -0.0001 0.0096  284  GLU A CA  
2006  C C   . GLU A 286  ? 0.2261 0.1896 0.2434 0.0185  0.0015  0.0123  284  GLU A C   
2007  O O   . GLU A 286  ? 0.2597 0.2218 0.2774 0.0164  0.0005  0.0147  284  GLU A O   
2008  C CB  . GLU A 286  ? 0.2235 0.1844 0.2436 0.0205  -0.0012 0.0084  284  GLU A CB  
2009  C CG  . GLU A 286  ? 0.2592 0.2192 0.2836 0.0226  -0.0032 0.0053  284  GLU A CG  
2010  C CD  . GLU A 286  ? 0.2843 0.2428 0.3078 0.0227  -0.0040 0.0036  284  GLU A CD  
2011  O OE1 . GLU A 286  ? 0.3011 0.2581 0.3219 0.0206  -0.0039 0.0057  284  GLU A OE1 
2012  O OE2 . GLU A 286  ? 0.3212 0.2805 0.3469 0.0251  -0.0048 -0.0001 284  GLU A OE2 
2013  N N   . LEU A 287  ? 0.2093 0.1751 0.2234 0.0188  0.0039  0.0120  285  LEU A N   
2014  C CA  . LEU A 287  ? 0.2092 0.1754 0.2206 0.0169  0.0051  0.0142  285  LEU A CA  
2015  C C   . LEU A 287  ? 0.2295 0.1975 0.2425 0.0167  0.0058  0.0156  285  LEU A C   
2016  O O   . LEU A 287  ? 0.2254 0.1926 0.2382 0.0149  0.0054  0.0175  285  LEU A O   
2017  C CB  . LEU A 287  ? 0.2257 0.1936 0.2339 0.0174  0.0071  0.0137  285  LEU A CB  
2018  C CG  . LEU A 287  ? 0.2845 0.2518 0.2900 0.0154  0.0078  0.0152  285  LEU A CG  
2019  C CD1 . LEU A 287  ? 0.2967 0.2658 0.2999 0.0162  0.0095  0.0146  285  LEU A CD1 
2020  C CD2 . LEU A 287  ? 0.3149 0.2829 0.3210 0.0142  0.0083  0.0171  285  LEU A CD2 
2021  N N   . LEU A 288  ? 0.2177 0.1884 0.2322 0.0187  0.0068  0.0146  286  LEU A N   
2022  C CA  . LEU A 288  ? 0.2290 0.2017 0.2453 0.0186  0.0075  0.0159  286  LEU A CA  
2023  C C   . LEU A 288  ? 0.2296 0.2003 0.2482 0.0173  0.0057  0.0172  286  LEU A C   
2024  O O   . LEU A 288  ? 0.2247 0.1957 0.2431 0.0158  0.0060  0.0191  286  LEU A O   
2025  C CB  . LEU A 288  ? 0.2671 0.2436 0.2849 0.0211  0.0087  0.0143  286  LEU A CB  
2026  C CG  . LEU A 288  ? 0.3125 0.2913 0.3331 0.0212  0.0091  0.0155  286  LEU A CG  
2027  C CD1 . LEU A 288  ? 0.2877 0.2676 0.3071 0.0196  0.0106  0.0180  286  LEU A CD1 
2028  C CD2 . LEU A 288  ? 0.4114 0.3945 0.4338 0.0239  0.0101  0.0136  286  LEU A CD2 
2029  N N   . PRO A 289  ? 0.2174 0.1862 0.2385 0.0178  0.0036  0.0165  287  PRO A N   
2030  C CA  . PRO A 289  ? 0.2233 0.1906 0.2466 0.0163  0.0018  0.0184  287  PRO A CA  
2031  C C   . PRO A 289  ? 0.2364 0.2025 0.2572 0.0137  0.0013  0.0205  287  PRO A C   
2032  O O   . PRO A 289  ? 0.2112 0.1776 0.2330 0.0124  0.0006  0.0223  287  PRO A O   
2033  C CB  . PRO A 289  ? 0.2519 0.2172 0.2785 0.0173  -0.0006 0.0173  287  PRO A CB  
2034  C CG  . PRO A 289  ? 0.2941 0.2608 0.3211 0.0199  0.0003  0.0142  287  PRO A CG  
2035  C CD  . PRO A 289  ? 0.2480 0.2162 0.2706 0.0197  0.0026  0.0140  287  PRO A CD  
2036  N N   . ARG A 290  ? 0.1984 0.1635 0.2163 0.0130  0.0016  0.0202  288  ARG A N   
2037  C CA  . ARG A 290  ? 0.2107 0.1755 0.2263 0.0106  0.0014  0.0219  288  ARG A CA  
2038  C C   . ARG A 290  ? 0.1985 0.1652 0.2127 0.0099  0.0030  0.0223  288  ARG A C   
2039  O O   . ARG A 290  ? 0.2038 0.1711 0.2179 0.0083  0.0024  0.0236  288  ARG A O   
2040  C CB  . ARG A 290  ? 0.2263 0.1899 0.2393 0.0101  0.0014  0.0213  288  ARG A CB  
2041  C CG  . ARG A 290  ? 0.2527 0.2142 0.2677 0.0104  -0.0006 0.0211  288  ARG A CG  
2042  C CD  . ARG A 290  ? 0.3056 0.2661 0.3184 0.0102  -0.0005 0.0201  288  ARG A CD  
2043  N NE  . ARG A 290  ? 0.3350 0.2934 0.3506 0.0107  -0.0026 0.0198  288  ARG A NE  
2044  C CZ  . ARG A 290  ? 0.3295 0.2867 0.3445 0.0114  -0.0028 0.0182  288  ARG A CZ  
2045  N NH1 . ARG A 290  ? 0.3023 0.2603 0.3138 0.0117  -0.0010 0.0170  288  ARG A NH1 
2046  N NH2 . ARG A 290  ? 0.4116 0.3668 0.4302 0.0118  -0.0051 0.0178  288  ARG A NH2 
2047  N N   . VAL A 291  ? 0.1911 0.1590 0.2046 0.0112  0.0049  0.0213  289  VAL A N   
2048  C CA  . VAL A 291  ? 0.2003 0.1699 0.2136 0.0106  0.0062  0.0220  289  VAL A CA  
2049  C C   . VAL A 291  ? 0.1947 0.1654 0.2109 0.0105  0.0057  0.0229  289  VAL A C   
2050  O O   . VAL A 291  ? 0.2029 0.1743 0.2194 0.0091  0.0056  0.0238  289  VAL A O   
2051  C CB  . VAL A 291  ? 0.1987 0.1698 0.2114 0.0119  0.0082  0.0214  289  VAL A CB  
2052  C CG1 . VAL A 291  ? 0.2224 0.1948 0.2357 0.0110  0.0091  0.0224  289  VAL A CG1 
2053  C CG2 . VAL A 291  ? 0.2359 0.2059 0.2459 0.0121  0.0085  0.0204  289  VAL A CG2 
2054  N N   . LYS A 292  ? 0.1901 0.1611 0.2086 0.0119  0.0053  0.0226  290  LYS A N   
2055  C CA  . LYS A 292  ? 0.1780 0.1502 0.1995 0.0119  0.0048  0.0235  290  LYS A CA  
2056  C C   . LYS A 292  ? 0.2202 0.1914 0.2420 0.0101  0.0029  0.0248  290  LYS A C   
2057  O O   . LYS A 292  ? 0.1858 0.1582 0.2087 0.0091  0.0027  0.0257  290  LYS A O   
2058  C CB  . LYS A 292  ? 0.2008 0.1735 0.2250 0.0140  0.0045  0.0225  290  LYS A CB  
2059  C CG  . LYS A 292  ? 0.2156 0.1894 0.2432 0.0140  0.0038  0.0234  290  LYS A CG  
2060  C CD  . LYS A 292  ? 0.2375 0.2122 0.2684 0.0162  0.0034  0.0222  290  LYS A CD  
2061  C CE  . LYS A 292  ? 0.2316 0.2075 0.2658 0.0160  0.0026  0.0234  290  LYS A CE  
2062  N NZ  . LYS A 292  ? 0.2331 0.2106 0.2708 0.0184  0.0025  0.0218  290  LYS A NZ  
2063  N N   . ALA A 293  ? 0.1833 0.1528 0.2042 0.0094  0.0014  0.0250  291  ALA A N   
2064  C CA  . ALA A 293  ? 0.2000 0.1695 0.2212 0.0075  -0.0004 0.0267  291  ALA A CA  
2065  C C   . ALA A 293  ? 0.1817 0.1526 0.2005 0.0058  0.0001  0.0270  291  ALA A C   
2066  O O   . ALA A 293  ? 0.1982 0.1707 0.2177 0.0046  -0.0008 0.0280  291  ALA A O   
2067  C CB  . ALA A 293  ? 0.1972 0.1649 0.2183 0.0071  -0.0022 0.0273  291  ALA A CB  
2068  N N   . LEU A 294  ? 0.1833 0.1540 0.1995 0.0057  0.0014  0.0259  292  LEU A N   
2069  C CA  . LEU A 294  ? 0.1897 0.1618 0.2042 0.0043  0.0018  0.0256  292  LEU A CA  
2070  C C   . LEU A 294  ? 0.1961 0.1695 0.2126 0.0046  0.0026  0.0254  292  LEU A C   
2071  O O   . LEU A 294  ? 0.1863 0.1613 0.2032 0.0034  0.0020  0.0255  292  LEU A O   
2072  C CB  . LEU A 294  ? 0.2083 0.1797 0.2202 0.0045  0.0030  0.0244  292  LEU A CB  
2073  C CG  . LEU A 294  ? 0.1911 0.1614 0.2010 0.0040  0.0022  0.0246  292  LEU A CG  
2074  C CD1 . LEU A 294  ? 0.2158 0.1854 0.2235 0.0044  0.0035  0.0233  292  LEU A CD1 
2075  C CD2 . LEU A 294  ? 0.2094 0.1815 0.2183 0.0020  0.0008  0.0255  292  LEU A CD2 
2076  N N   . ALA A 295  ? 0.1769 0.1501 0.1950 0.0062  0.0038  0.0253  293  ALA A N   
2077  C CA  . ALA A 295  ? 0.1894 0.1641 0.2100 0.0063  0.0045  0.0255  293  ALA A CA  
2078  C C   . ALA A 295  ? 0.1894 0.1652 0.2125 0.0058  0.0032  0.0264  293  ALA A C   
2079  O O   . ALA A 295  ? 0.1916 0.1687 0.2162 0.0050  0.0030  0.0265  293  ALA A O   
2080  C CB  . ALA A 295  ? 0.1974 0.1726 0.2192 0.0080  0.0062  0.0255  293  ALA A CB  
2081  N N   . LEU A 296  ? 0.1804 0.1555 0.2041 0.0062  0.0021  0.0270  294  LEU A N   
2082  C CA  . LEU A 296  ? 0.1893 0.1655 0.2154 0.0057  0.0006  0.0281  294  LEU A CA  
2083  C C   . LEU A 296  ? 0.1961 0.1736 0.2209 0.0037  -0.0006 0.0284  294  LEU A C   
2084  O O   . LEU A 296  ? 0.1833 0.1625 0.2099 0.0030  -0.0013 0.0288  294  LEU A O   
2085  C CB  . LEU A 296  ? 0.1922 0.1672 0.2196 0.0065  -0.0007 0.0287  294  LEU A CB  
2086  C CG  . LEU A 296  ? 0.2029 0.1777 0.2326 0.0087  0.0002  0.0280  294  LEU A CG  
2087  C CD1 . LEU A 296  ? 0.2166 0.1897 0.2477 0.0095  -0.0014 0.0281  294  LEU A CD1 
2088  C CD2 . LEU A 296  ? 0.2505 0.2273 0.2834 0.0092  0.0005  0.0285  294  LEU A CD2 
2089  N N   . LEU A 297  ? 0.1885 0.1656 0.2103 0.0028  -0.0010 0.0281  295  LEU A N   
2090  C CA  . LEU A 297  ? 0.1962 0.1757 0.2166 0.0010  -0.0021 0.0282  295  LEU A CA  
2091  C C   . LEU A 297  ? 0.1832 0.1640 0.2039 0.0007  -0.0012 0.0265  295  LEU A C   
2092  O O   . LEU A 297  ? 0.1992 0.1823 0.2207 -0.0003 -0.0022 0.0262  295  LEU A O   
2093  C CB  . LEU A 297  ? 0.2312 0.2107 0.2485 0.0001  -0.0026 0.0284  295  LEU A CB  
2094  C CG  . LEU A 297  ? 0.2586 0.2416 0.2744 -0.0018 -0.0040 0.0288  295  LEU A CG  
2095  C CD1 . LEU A 297  ? 0.2880 0.2728 0.3055 -0.0025 -0.0058 0.0309  295  LEU A CD1 
2096  C CD2 . LEU A 297  ? 0.3091 0.2923 0.3219 -0.0026 -0.0041 0.0291  295  LEU A CD2 
2097  N N   . ALA A 298  ? 0.1756 0.1548 0.1959 0.0015  0.0004  0.0254  296  ALA A N   
2098  C CA  . ALA A 298  ? 0.1852 0.1652 0.2069 0.0012  0.0009  0.0240  296  ALA A CA  
2099  C C   . ALA A 298  ? 0.1933 0.1743 0.2188 0.0014  0.0007  0.0246  296  ALA A C   
2100  O O   . ALA A 298  ? 0.1986 0.1811 0.2258 0.0006  0.0000  0.0236  296  ALA A O   
2101  C CB  . ALA A 298  ? 0.2049 0.1832 0.2262 0.0021  0.0026  0.0235  296  ALA A CB  
2102  N N   . LYS A 299  ? 0.1794 0.1596 0.2064 0.0025  0.0012  0.0259  297  LYS A N   
2103  C CA  A LYS A 299  ? 0.1893 0.1707 0.2200 0.0026  0.0009  0.0266  297  LYS A CA  
2104  C CA  B LYS A 299  ? 0.1894 0.1708 0.2202 0.0026  0.0009  0.0266  297  LYS A CA  
2105  C C   . LYS A 299  ? 0.1963 0.1796 0.2276 0.0014  -0.0010 0.0267  297  LYS A C   
2106  O O   . LYS A 299  ? 0.2081 0.1929 0.2420 0.0009  -0.0016 0.0263  297  LYS A O   
2107  C CB  A LYS A 299  ? 0.1841 0.1649 0.2162 0.0042  0.0016  0.0278  297  LYS A CB  
2108  C CB  B LYS A 299  ? 0.1843 0.1651 0.2164 0.0042  0.0017  0.0278  297  LYS A CB  
2109  C CG  A LYS A 299  ? 0.2032 0.1855 0.2388 0.0043  0.0009  0.0288  297  LYS A CG  
2110  C CG  B LYS A 299  ? 0.2036 0.1859 0.2394 0.0044  0.0011  0.0287  297  LYS A CG  
2111  C CD  A LYS A 299  ? 0.2148 0.1971 0.2522 0.0060  0.0017  0.0295  297  LYS A CD  
2112  C CD  B LYS A 299  ? 0.2085 0.1908 0.2459 0.0062  0.0022  0.0294  297  LYS A CD  
2113  C CE  A LYS A 299  ? 0.2016 0.1853 0.2422 0.0061  0.0006  0.0304  297  LYS A CE  
2114  C CE  B LYS A 299  ? 0.2379 0.2218 0.2789 0.0064  0.0014  0.0303  297  LYS A CE  
2115  N NZ  A LYS A 299  ? 0.2264 0.2109 0.2694 0.0080  0.0015  0.0307  297  LYS A NZ  
2116  N NZ  B LYS A 299  ? 0.2676 0.2512 0.3081 0.0057  -0.0007 0.0307  297  LYS A NZ  
2117  N N   . ASN A 300  ? 0.1907 0.1742 0.2197 0.0010  -0.0022 0.0274  298  ASN A N   
2118  C CA  . ASN A 300  ? 0.1846 0.1707 0.2143 -0.0002 -0.0040 0.0279  298  ASN A CA  
2119  C C   . ASN A 300  ? 0.2126 0.2012 0.2415 -0.0014 -0.0047 0.0261  298  ASN A C   
2120  O O   . ASN A 300  ? 0.2348 0.2258 0.2656 -0.0021 -0.0059 0.0257  298  ASN A O   
2121  C CB  . ASN A 300  ? 0.2215 0.2076 0.2493 -0.0006 -0.0053 0.0296  298  ASN A CB  
2122  C CG  . ASN A 300  ? 0.3119 0.3009 0.3409 -0.0017 -0.0073 0.0308  298  ASN A CG  
2123  O OD1 . ASN A 300  ? 0.3756 0.3645 0.4076 -0.0011 -0.0078 0.0319  298  ASN A OD1 
2124  N ND2 . ASN A 300  ? 0.2874 0.2796 0.3142 -0.0031 -0.0084 0.0305  298  ASN A ND2 
2125  N N   . TYR A 301  ? 0.1976 0.1859 0.2241 -0.0017 -0.0040 0.0246  299  TYR A N   
2126  C CA  . TYR A 301  ? 0.1946 0.1854 0.2210 -0.0026 -0.0046 0.0221  299  TYR A CA  
2127  C C   . TYR A 301  ? 0.2007 0.1904 0.2305 -0.0021 -0.0040 0.0206  299  TYR A C   
2128  O O   . TYR A 301  ? 0.2272 0.2189 0.2581 -0.0027 -0.0048 0.0182  299  TYR A O   
2129  C CB  . TYR A 301  ? 0.1961 0.1873 0.2187 -0.0030 -0.0043 0.0211  299  TYR A CB  
2130  C CG  . TYR A 301  ? 0.1975 0.1912 0.2170 -0.0039 -0.0054 0.0224  299  TYR A CG  
2131  C CD1 . TYR A 301  ? 0.2276 0.2260 0.2466 -0.0051 -0.0070 0.0220  299  TYR A CD1 
2132  C CD2 . TYR A 301  ? 0.2022 0.1939 0.2195 -0.0038 -0.0049 0.0241  299  TYR A CD2 
2133  C CE1 . TYR A 301  ? 0.2218 0.2232 0.2380 -0.0062 -0.0080 0.0237  299  TYR A CE1 
2134  C CE2 . TYR A 301  ? 0.2195 0.2135 0.2345 -0.0048 -0.0061 0.0258  299  TYR A CE2 
2135  C CZ  . TYR A 301  ? 0.2250 0.2240 0.2393 -0.0061 -0.0076 0.0258  299  TYR A CZ  
2136  O OH  . TYR A 301  ? 0.2269 0.2290 0.2391 -0.0074 -0.0088 0.0280  299  TYR A OH  
2137  N N   . ASP A 302  ? 0.1982 0.1852 0.2300 -0.0011 -0.0026 0.0219  300  ASP A N   
2138  C CA  . ASP A 302  ? 0.1883 0.1744 0.2238 -0.0008 -0.0019 0.0213  300  ASP A CA  
2139  C C   . ASP A 302  ? 0.1897 0.1752 0.2245 -0.0009 -0.0016 0.0193  300  ASP A C   
2140  O O   . ASP A 302  ? 0.2143 0.2006 0.2521 -0.0014 -0.0025 0.0174  300  ASP A O   
2141  C CB  . ASP A 302  ? 0.1948 0.1826 0.2346 -0.0013 -0.0031 0.0209  300  ASP A CB  
2142  C CG  . ASP A 302  ? 0.2519 0.2385 0.2963 -0.0008 -0.0022 0.0217  300  ASP A CG  
2143  O OD1 . ASP A 302  ? 0.2365 0.2215 0.2806 0.0001  -0.0006 0.0235  300  ASP A OD1 
2144  O OD2 . ASP A 302  ? 0.2599 0.2474 0.3085 -0.0014 -0.0033 0.0206  300  ASP A OD2 
2145  N N   . ILE A 303  ? 0.1780 0.1620 0.2093 -0.0005 -0.0006 0.0196  301  ILE A N   
2146  C CA  . ILE A 303  ? 0.1910 0.1742 0.2216 -0.0005 -0.0001 0.0179  301  ILE A CA  
2147  C C   . ILE A 303  ? 0.1970 0.1777 0.2276 0.0006  0.0016  0.0196  301  ILE A C   
2148  O O   . ILE A 303  ? 0.1863 0.1662 0.2163 0.0013  0.0025  0.0216  301  ILE A O   
2149  C CB  . ILE A 303  ? 0.2023 0.1867 0.2285 -0.0010 -0.0005 0.0166  301  ILE A CB  
2150  C CG1 . ILE A 303  ? 0.1965 0.1795 0.2189 -0.0005 0.0003  0.0185  301  ILE A CG1 
2151  C CG2 . ILE A 303  ? 0.2158 0.2039 0.2416 -0.0020 -0.0023 0.0153  301  ILE A CG2 
2152  C CD1 . ILE A 303  ? 0.2104 0.1945 0.2289 -0.0011 0.0001  0.0175  301  ILE A CD1 
2153  N N   . GLY A 304  ? 0.1959 0.1756 0.2274 0.0007  0.0020  0.0186  302  GLY A N   
2154  C CA  . GLY A 304  ? 0.2046 0.1825 0.2358 0.0015  0.0036  0.0201  302  GLY A CA  
2155  C C   . GLY A 304  ? 0.1905 0.1676 0.2167 0.0020  0.0044  0.0202  302  GLY A C   
2156  O O   . GLY A 304  ? 0.1850 0.1627 0.2084 0.0015  0.0037  0.0187  302  GLY A O   
2157  N N   . LEU A 305  ? 0.1786 0.1548 0.2039 0.0030  0.0058  0.0219  303  LEU A N   
2158  C CA  . LEU A 305  ? 0.1850 0.1601 0.2063 0.0036  0.0065  0.0219  303  LEU A CA  
2159  C C   . LEU A 305  ? 0.1852 0.1597 0.2069 0.0046  0.0079  0.0229  303  LEU A C   
2160  O O   . LEU A 305  ? 0.1914 0.1666 0.2146 0.0054  0.0089  0.0245  303  LEU A O   
2161  C CB  . LEU A 305  ? 0.2048 0.1799 0.2246 0.0041  0.0064  0.0228  303  LEU A CB  
2162  C CG  . LEU A 305  ? 0.2420 0.2158 0.2581 0.0047  0.0067  0.0226  303  LEU A CG  
2163  C CD1 . LEU A 305  ? 0.2775 0.2514 0.2925 0.0044  0.0056  0.0229  303  LEU A CD1 
2164  C CD2 . LEU A 305  ? 0.3264 0.2998 0.3423 0.0062  0.0082  0.0233  303  LEU A CD2 
2165  N N   . ASN A 306  ? 0.1938 0.1675 0.2143 0.0045  0.0081  0.0220  304  ASN A N   
2166  C CA  . ASN A 306  ? 0.1916 0.1651 0.2128 0.0052  0.0093  0.0231  304  ASN A CA  
2167  C C   . ASN A 306  ? 0.1902 0.1631 0.2074 0.0060  0.0101  0.0229  304  ASN A C   
2168  O O   . ASN A 306  ? 0.1998 0.1718 0.2140 0.0056  0.0096  0.0214  304  ASN A O   
2169  C CB  . ASN A 306  ? 0.1906 0.1636 0.2139 0.0045  0.0086  0.0221  304  ASN A CB  
2170  C CG  . ASN A 306  ? 0.2116 0.1843 0.2352 0.0051  0.0096  0.0234  304  ASN A CG  
2171  O OD1 . ASN A 306  ? 0.2477 0.2196 0.2685 0.0054  0.0099  0.0225  304  ASN A OD1 
2172  N ND2 . ASN A 306  ? 0.2003 0.1740 0.2275 0.0053  0.0101  0.0257  304  ASN A ND2 
2173  N N   . ILE A 307  ? 0.1881 0.1617 0.2051 0.0071  0.0114  0.0244  305  ILE A N   
2174  C CA  . ILE A 307  ? 0.2010 0.1744 0.2147 0.0081  0.0122  0.0240  305  ILE A CA  
2175  C C   . ILE A 307  ? 0.1802 0.1534 0.1941 0.0081  0.0126  0.0244  305  ILE A C   
2176  O O   . ILE A 307  ? 0.1828 0.1575 0.1991 0.0083  0.0133  0.0263  305  ILE A O   
2177  C CB  . ILE A 307  ? 0.2016 0.1767 0.2150 0.0095  0.0132  0.0250  305  ILE A CB  
2178  C CG1 . ILE A 307  ? 0.2251 0.2000 0.2387 0.0096  0.0125  0.0245  305  ILE A CG1 
2179  C CG2 . ILE A 307  ? 0.2346 0.2098 0.2449 0.0106  0.0139  0.0243  305  ILE A CG2 
2180  C CD1 . ILE A 307  ? 0.2753 0.2523 0.2895 0.0112  0.0134  0.0250  305  ILE A CD1 
2181  N N   . ASP A 308  ? 0.1988 0.1705 0.2104 0.0077  0.0121  0.0228  306  ASP A N   
2182  C CA  . ASP A 308  ? 0.1832 0.1547 0.1949 0.0077  0.0124  0.0229  306  ASP A CA  
2183  C C   . ASP A 308  ? 0.1908 0.1635 0.2009 0.0089  0.0136  0.0241  306  ASP A C   
2184  O O   . ASP A 308  ? 0.2002 0.1735 0.2080 0.0098  0.0141  0.0238  306  ASP A O   
2185  C CB  . ASP A 308  ? 0.2061 0.1762 0.2154 0.0071  0.0116  0.0207  306  ASP A CB  
2186  C CG  . ASP A 308  ? 0.2629 0.2328 0.2740 0.0059  0.0104  0.0192  306  ASP A CG  
2187  O OD1 . ASP A 308  ? 0.2412 0.2115 0.2558 0.0055  0.0099  0.0196  306  ASP A OD1 
2188  O OD2 . ASP A 308  ? 0.2735 0.2431 0.2824 0.0054  0.0098  0.0173  306  ASP A OD2 
2189  N N   . ALA A 309  ? 0.1854 0.1589 0.1971 0.0091  0.0140  0.0255  307  ALA A N   
2190  C CA  . ALA A 309  ? 0.1933 0.1688 0.2033 0.0102  0.0152  0.0269  307  ALA A CA  
2191  C C   . ALA A 309  ? 0.1848 0.1591 0.1917 0.0104  0.0151  0.0254  307  ALA A C   
2192  O O   . ALA A 309  ? 0.2029 0.1754 0.2105 0.0097  0.0143  0.0245  307  ALA A O   
2193  C CB  . ALA A 309  ? 0.2046 0.1823 0.2183 0.0101  0.0156  0.0299  307  ALA A CB  
2194  N N   . GLU A 310  ? 0.1841 0.1596 0.1879 0.0116  0.0158  0.0250  308  GLU A N   
2195  C CA  . GLU A 310  ? 0.1869 0.1612 0.1876 0.0119  0.0156  0.0234  308  GLU A CA  
2196  C C   . GLU A 310  ? 0.1893 0.1662 0.1891 0.0129  0.0165  0.0248  308  GLU A C   
2197  O O   . GLU A 310  ? 0.2030 0.1817 0.2055 0.0127  0.0169  0.0273  308  GLU A O   
2198  C CB  . GLU A 310  ? 0.2049 0.1779 0.2030 0.0122  0.0152  0.0213  308  GLU A CB  
2199  C CG  . GLU A 310  ? 0.2241 0.1951 0.2231 0.0109  0.0142  0.0204  308  GLU A CG  
2200  C CD  . GLU A 310  ? 0.2347 0.2044 0.2316 0.0109  0.0135  0.0188  308  GLU A CD  
2201  O OE1 . GLU A 310  ? 0.2673 0.2357 0.2622 0.0105  0.0130  0.0177  308  GLU A OE1 
2202  O OE2 . GLU A 310  ? 0.2304 0.2002 0.2279 0.0112  0.0133  0.0189  308  GLU A OE2 
2203  N N   . GLU A 311  ? 0.1982 0.1756 0.1948 0.0139  0.0168  0.0233  309  GLU A N   
2204  C CA  . GLU A 311  ? 0.2108 0.1912 0.2062 0.0149  0.0175  0.0244  309  GLU A CA  
2205  C C   . GLU A 311  ? 0.1941 0.1790 0.1905 0.0159  0.0186  0.0265  309  GLU A C   
2206  O O   . GLU A 311  ? 0.2015 0.1873 0.1987 0.0162  0.0189  0.0263  309  GLU A O   
2207  C CB  . GLU A 311  ? 0.2162 0.1963 0.2081 0.0159  0.0174  0.0219  309  GLU A CB  
2208  C CG  . GLU A 311  ? 0.2360 0.2125 0.2267 0.0150  0.0164  0.0202  309  GLU A CG  
2209  C CD  . GLU A 311  ? 0.2881 0.2616 0.2785 0.0142  0.0155  0.0184  309  GLU A CD  
2210  O OE1 . GLU A 311  ? 0.2239 0.1975 0.2156 0.0141  0.0155  0.0186  309  GLU A OE1 
2211  O OE2 . GLU A 311  ? 0.3637 0.3351 0.3527 0.0136  0.0147  0.0169  309  GLU A OE2 
2212  N N   . ALA A 312  ? 0.1966 0.1850 0.1930 0.0164  0.0193  0.0286  310  ALA A N   
2213  C CA  . ALA A 312  ? 0.1883 0.1822 0.1859 0.0171  0.0205  0.0311  310  ALA A CA  
2214  C C   . ALA A 312  ? 0.1872 0.1842 0.1825 0.0188  0.0211  0.0290  310  ALA A C   
2215  O O   . ALA A 312  ? 0.2008 0.2015 0.1975 0.0194  0.0219  0.0302  310  ALA A O   
2216  C CB  . ALA A 312  ? 0.2014 0.1991 0.1991 0.0173  0.0209  0.0340  310  ALA A CB  
2217  N N   . ASP A 313  ? 0.1999 0.1954 0.1921 0.0198  0.0207  0.0256  311  ASP A N   
2218  C CA  . ASP A 313  ? 0.2088 0.2071 0.1995 0.0216  0.0210  0.0230  311  ASP A CA  
2219  C C   . ASP A 313  ? 0.1878 0.1832 0.1798 0.0214  0.0204  0.0213  311  ASP A C   
2220  O O   . ASP A 313  ? 0.2217 0.2188 0.2132 0.0230  0.0203  0.0188  311  ASP A O   
2221  C CB  . ASP A 313  ? 0.2461 0.2445 0.2336 0.0228  0.0205  0.0200  311  ASP A CB  
2222  C CG  . ASP A 313  ? 0.2803 0.2723 0.2671 0.0218  0.0191  0.0178  311  ASP A CG  
2223  O OD1 . ASP A 313  ? 0.2548 0.2426 0.2431 0.0203  0.0185  0.0184  311  ASP A OD1 
2224  O OD2 . ASP A 313  ? 0.3279 0.3196 0.3126 0.0226  0.0186  0.0155  311  ASP A OD2 
2225  N N   . ARG A 314  ? 0.1882 0.1796 0.1822 0.0197  0.0198  0.0225  312  ARG A N   
2226  C CA  . ARG A 314  ? 0.1948 0.1838 0.1903 0.0194  0.0192  0.0215  312  ARG A CA  
2227  C C   . ARG A 314  ? 0.1975 0.1886 0.1962 0.0189  0.0199  0.0241  312  ARG A C   
2228  O O   . ARG A 314  ? 0.2003 0.1906 0.2004 0.0189  0.0195  0.0235  312  ARG A O   
2229  C CB  . ARG A 314  ? 0.2032 0.1865 0.1987 0.0178  0.0179  0.0205  312  ARG A CB  
2230  C CG  . ARG A 314  ? 0.2201 0.2012 0.2131 0.0184  0.0169  0.0177  312  ARG A CG  
2231  C CD  . ARG A 314  ? 0.2425 0.2193 0.2349 0.0167  0.0159  0.0173  312  ARG A CD  
2232  N NE  . ARG A 314  ? 0.2571 0.2318 0.2484 0.0170  0.0147  0.0150  312  ARG A NE  
2233  C CZ  . ARG A 314  ? 0.2249 0.1965 0.2154 0.0158  0.0137  0.0143  312  ARG A CZ  
2234  N NH1 . ARG A 314  ? 0.2316 0.2022 0.2220 0.0144  0.0138  0.0154  312  ARG A NH1 
2235  N NH2 . ARG A 314  ? 0.2524 0.2222 0.2425 0.0159  0.0125  0.0127  312  ARG A NH2 
2236  N N   . LEU A 315  ? 0.1895 0.1835 0.1895 0.0184  0.0207  0.0272  313  LEU A N   
2237  C CA  . LEU A 315  ? 0.1959 0.1919 0.1995 0.0177  0.0212  0.0301  313  LEU A CA  
2238  C C   . LEU A 315  ? 0.1996 0.1996 0.2038 0.0190  0.0219  0.0296  313  LEU A C   
2239  O O   . LEU A 315  ? 0.1951 0.1937 0.2014 0.0185  0.0216  0.0295  313  LEU A O   
2240  C CB  . LEU A 315  ? 0.2082 0.2076 0.2133 0.0172  0.0219  0.0338  313  LEU A CB  
2241  C CG  . LEU A 315  ? 0.2229 0.2223 0.2327 0.0156  0.0217  0.0372  313  LEU A CG  
2242  C CD1 . LEU A 315  ? 0.2062 0.2085 0.2178 0.0151  0.0220  0.0411  313  LEU A CD1 
2243  C CD2 . LEU A 315  ? 0.2447 0.2474 0.2566 0.0160  0.0224  0.0382  313  LEU A CD2 
2244  N N   . GLU A 316  ? 0.1962 0.2017 0.1987 0.0207  0.0230  0.0293  314  GLU A N   
2245  C CA  . GLU A 316  ? 0.1933 0.2038 0.1968 0.0222  0.0239  0.0289  314  GLU A CA  
2246  C C   . GLU A 316  ? 0.2189 0.2263 0.2223 0.0230  0.0229  0.0252  314  GLU A C   
2247  O O   . GLU A 316  ? 0.2164 0.2249 0.2220 0.0233  0.0231  0.0252  314  GLU A O   
2248  C CB  . GLU A 316  ? 0.2030 0.2214 0.2049 0.0239  0.0253  0.0293  314  GLU A CB  
2249  C CG  . GLU A 316  ? 0.2232 0.2456 0.2267 0.0227  0.0262  0.0343  314  GLU A CG  
2250  C CD  . GLU A 316  ? 0.2248 0.2560 0.2267 0.0242  0.0276  0.0354  314  GLU A CD  
2251  O OE1 . GLU A 316  ? 0.2457 0.2824 0.2470 0.0261  0.0284  0.0334  314  GLU A OE1 
2252  O OE2 . GLU A 316  ? 0.2316 0.2645 0.2330 0.0236  0.0278  0.0381  314  GLU A OE2 
2253  N N   . LEU A 317  ? 0.2102 0.2133 0.2113 0.0233  0.0218  0.0222  315  LEU A N   
2254  C CA  . LEU A 317  ? 0.2240 0.2235 0.2256 0.0238  0.0205  0.0192  315  LEU A CA  
2255  C C   . LEU A 317  ? 0.2118 0.2073 0.2158 0.0220  0.0197  0.0205  315  LEU A C   
2256  O O   . LEU A 317  ? 0.2128 0.2082 0.2187 0.0225  0.0193  0.0196  315  LEU A O   
2257  C CB  . LEU A 317  ? 0.2476 0.2429 0.2468 0.0238  0.0193  0.0166  315  LEU A CB  
2258  C CG  . LEU A 317  ? 0.2523 0.2436 0.2525 0.0240  0.0176  0.0139  315  LEU A CG  
2259  C CD1 . LEU A 317  ? 0.3029 0.2979 0.3048 0.0263  0.0177  0.0117  315  LEU A CD1 
2260  C CD2 . LEU A 317  ? 0.3002 0.2878 0.2984 0.0239  0.0164  0.0120  315  LEU A CD2 
2261  N N   . SER A 318  ? 0.1871 0.1797 0.1913 0.0200  0.0195  0.0226  316  SER A N   
2262  C CA  . SER A 318  ? 0.1984 0.1876 0.2048 0.0184  0.0187  0.0236  316  SER A CA  
2263  C C   . SER A 318  ? 0.2001 0.1927 0.2096 0.0185  0.0194  0.0254  316  SER A C   
2264  O O   . SER A 318  ? 0.1949 0.1856 0.2063 0.0179  0.0186  0.0253  316  SER A O   
2265  C CB  . SER A 318  ? 0.1860 0.1722 0.1924 0.0165  0.0182  0.0250  316  SER A CB  
2266  O OG  . SER A 318  ? 0.1988 0.1879 0.2070 0.0161  0.0192  0.0278  316  SER A OG  
2267  N N   . LEU A 319  ? 0.1987 0.1967 0.2087 0.0193  0.0209  0.0272  317  LEU A N   
2268  C CA  . LEU A 319  ? 0.1988 0.2010 0.2120 0.0195  0.0217  0.0292  317  LEU A CA  
2269  C C   . LEU A 319  ? 0.2071 0.2107 0.2209 0.0211  0.0216  0.0269  317  LEU A C   
2270  O O   . LEU A 319  ? 0.2058 0.2104 0.2225 0.0208  0.0216  0.0278  317  LEU A O   
2271  C CB  . LEU A 319  ? 0.2173 0.2259 0.2309 0.0200  0.0233  0.0320  317  LEU A CB  
2272  C CG  . LEU A 319  ? 0.2069 0.2145 0.2214 0.0183  0.0233  0.0351  317  LEU A CG  
2273  C CD1 . LEU A 319  ? 0.2257 0.2406 0.2406 0.0189  0.0249  0.0382  317  LEU A CD1 
2274  C CD2 . LEU A 319  ? 0.2198 0.2241 0.2380 0.0163  0.0224  0.0371  317  LEU A CD2 
2275  N N   . ASP A 320  ? 0.2138 0.2176 0.2253 0.0228  0.0213  0.0237  318  ASP A N   
2276  C CA  . ASP A 320  ? 0.2316 0.2363 0.2444 0.0244  0.0208  0.0210  318  ASP A CA  
2277  C C   . ASP A 320  ? 0.2284 0.2274 0.2428 0.0232  0.0191  0.0205  318  ASP A C   
2278  O O   . ASP A 320  ? 0.2436 0.2434 0.2605 0.0238  0.0188  0.0201  318  ASP A O   
2279  C CB  . ASP A 320  ? 0.2340 0.2400 0.2447 0.0266  0.0206  0.0175  318  ASP A CB  
2280  C CG  . ASP A 320  ? 0.2718 0.2856 0.2816 0.0283  0.0224  0.0176  318  ASP A CG  
2281  O OD1 . ASP A 320  ? 0.2970 0.3163 0.3089 0.0291  0.0235  0.0184  318  ASP A OD1 
2282  O OD2 . ASP A 320  ? 0.3257 0.3405 0.3327 0.0287  0.0227  0.0170  318  ASP A OD2 
2283  N N   . LEU A 321  ? 0.2144 0.2079 0.2273 0.0215  0.0180  0.0208  319  LEU A N   
2284  C CA  . LEU A 321  ? 0.2076 0.1966 0.2218 0.0202  0.0164  0.0207  319  LEU A CA  
2285  C C   . LEU A 321  ? 0.2145 0.2042 0.2313 0.0188  0.0167  0.0233  319  LEU A C   
2286  O O   . LEU A 321  ? 0.2152 0.2041 0.2342 0.0185  0.0158  0.0233  319  LEU A O   
2287  C CB  . LEU A 321  ? 0.2140 0.1982 0.2260 0.0187  0.0152  0.0203  319  LEU A CB  
2288  C CG  . LEU A 321  ? 0.2601 0.2424 0.2704 0.0198  0.0142  0.0177  319  LEU A CG  
2289  C CD1 . LEU A 321  ? 0.3005 0.2848 0.3084 0.0208  0.0152  0.0169  319  LEU A CD1 
2290  C CD2 . LEU A 321  ? 0.3202 0.2977 0.3298 0.0180  0.0125  0.0176  319  LEU A CD2 
2291  N N   . LEU A 322  ? 0.2054 0.1964 0.2223 0.0178  0.0177  0.0255  320  LEU A N   
2292  C CA  . LEU A 322  ? 0.2148 0.2064 0.2348 0.0164  0.0177  0.0279  320  LEU A CA  
2293  C C   . LEU A 322  ? 0.2097 0.2055 0.2324 0.0175  0.0185  0.0286  320  LEU A C   
2294  O O   . LEU A 322  ? 0.2123 0.2075 0.2377 0.0167  0.0178  0.0292  320  LEU A O   
2295  C CB  . LEU A 322  ? 0.2091 0.2019 0.2295 0.0154  0.0185  0.0303  320  LEU A CB  
2296  C CG  . LEU A 322  ? 0.2174 0.2106 0.2419 0.0139  0.0183  0.0328  320  LEU A CG  
2297  C CD1 . LEU A 322  ? 0.2185 0.2071 0.2436 0.0123  0.0167  0.0319  320  LEU A CD1 
2298  C CD2 . LEU A 322  ? 0.2062 0.2016 0.2320 0.0133  0.0192  0.0356  320  LEU A CD2 
2299  N N   . GLU A 323  ? 0.1934 0.1941 0.2155 0.0194  0.0198  0.0281  321  GLU A N   
2300  C CA  . GLU A 323  ? 0.2216 0.2274 0.2463 0.0207  0.0207  0.0284  321  GLU A CA  
2301  C C   . GLU A 323  ? 0.2264 0.2298 0.2524 0.0213  0.0193  0.0262  321  GLU A C   
2302  O O   . GLU A 323  ? 0.2189 0.2234 0.2480 0.0209  0.0191  0.0273  321  GLU A O   
2303  C CB  . GLU A 323  ? 0.2302 0.2421 0.2535 0.0228  0.0222  0.0275  321  GLU A CB  
2304  C CG  . GLU A 323  ? 0.2939 0.3117 0.3196 0.0247  0.0230  0.0268  321  GLU A CG  
2305  C CD  . GLU A 323  ? 0.3167 0.3418 0.3441 0.0246  0.0250  0.0302  321  GLU A CD  
2306  O OE1 . GLU A 323  ? 0.3300 0.3558 0.3568 0.0233  0.0256  0.0331  321  GLU A OE1 
2307  O OE2 . GLU A 323  ? 0.3404 0.3709 0.3702 0.0258  0.0257  0.0302  321  GLU A OE2 
2308  N N   . VAL A 324  ? 0.2060 0.2064 0.2301 0.0222  0.0182  0.0233  322  VAL A N   
2309  C CA  . VAL A 324  ? 0.2126 0.2109 0.2386 0.0229  0.0166  0.0215  322  VAL A CA  
2310  C C   . VAL A 324  ? 0.2035 0.1978 0.2309 0.0207  0.0153  0.0230  322  VAL A C   
2311  O O   . VAL A 324  ? 0.2058 0.2005 0.2360 0.0209  0.0146  0.0232  322  VAL A O   
2312  C CB  . VAL A 324  ? 0.2294 0.2248 0.2537 0.0240  0.0154  0.0184  322  VAL A CB  
2313  C CG1 . VAL A 324  ? 0.2571 0.2499 0.2841 0.0244  0.0134  0.0171  322  VAL A CG1 
2314  C CG2 . VAL A 324  ? 0.2425 0.2427 0.2659 0.0265  0.0165  0.0162  322  VAL A CG2 
2315  N N   . LEU A 325  ? 0.1921 0.1830 0.2176 0.0188  0.0149  0.0241  323  LEU A N   
2316  C CA  . LEU A 325  ? 0.1940 0.1816 0.2206 0.0168  0.0135  0.0251  323  LEU A CA  
2317  C C   . LEU A 325  ? 0.1894 0.1796 0.2192 0.0161  0.0140  0.0272  323  LEU A C   
2318  O O   . LEU A 325  ? 0.1883 0.1777 0.2204 0.0156  0.0130  0.0275  323  LEU A O   
2319  C CB  . LEU A 325  ? 0.2069 0.1912 0.2309 0.0151  0.0130  0.0254  323  LEU A CB  
2320  C CG  . LEU A 325  ? 0.2193 0.2007 0.2405 0.0154  0.0121  0.0236  323  LEU A CG  
2321  C CD1 . LEU A 325  ? 0.2421 0.2218 0.2607 0.0141  0.0123  0.0239  323  LEU A CD1 
2322  C CD2 . LEU A 325  ? 0.2333 0.2120 0.2552 0.0147  0.0101  0.0232  323  LEU A CD2 
2323  N N   . CYS A 326  ? 0.1950 0.1884 0.2254 0.0161  0.0156  0.0288  324  CYS A N   
2324  C CA  . CYS A 326  ? 0.1878 0.1836 0.2219 0.0153  0.0161  0.0311  324  CYS A CA  
2325  C C   . CYS A 326  ? 0.2093 0.2089 0.2461 0.0167  0.0165  0.0311  324  CYS A C   
2326  O O   . CYS A 326  ? 0.2187 0.2195 0.2589 0.0158  0.0163  0.0326  324  CYS A O   
2327  C CB  . CYS A 326  ? 0.2002 0.1986 0.2349 0.0147  0.0174  0.0334  324  CYS A CB  
2328  S SG  . CYS A 326  ? 0.2360 0.2299 0.2692 0.0128  0.0165  0.0337  324  CYS A SG  
2329  N N   . LEU A 327  ? 0.1969 0.1987 0.2327 0.0188  0.0170  0.0291  325  LEU A N   
2330  C CA  . LEU A 327  ? 0.1919 0.1975 0.2304 0.0205  0.0174  0.0285  325  LEU A CA  
2331  C C   . LEU A 327  ? 0.2096 0.2117 0.2491 0.0209  0.0154  0.0266  325  LEU A C   
2332  O O   . LEU A 327  ? 0.2182 0.2230 0.2605 0.0222  0.0153  0.0258  325  LEU A O   
2333  C CB  . LEU A 327  ? 0.2033 0.2142 0.2409 0.0229  0.0189  0.0271  325  LEU A CB  
2334  C CG  . LEU A 327  ? 0.2597 0.2755 0.2968 0.0226  0.0210  0.0296  325  LEU A CG  
2335  C CD1 . LEU A 327  ? 0.2923 0.3139 0.3278 0.0251  0.0224  0.0277  325  LEU A CD1 
2336  C CD2 . LEU A 327  ? 0.3013 0.3208 0.3423 0.0215  0.0217  0.0328  325  LEU A CD2 
2337  N N   . ASP A 328  ? 0.1935 0.1902 0.2310 0.0196  0.0138  0.0259  326  ASP A N   
2338  C CA  . ASP A 328  ? 0.2042 0.1978 0.2427 0.0199  0.0117  0.0246  326  ASP A CA  
2339  C C   . ASP A 328  ? 0.2166 0.2094 0.2577 0.0184  0.0106  0.0262  326  ASP A C   
2340  O O   . ASP A 328  ? 0.1974 0.1883 0.2378 0.0163  0.0101  0.0276  326  ASP A O   
2341  C CB  . ASP A 328  ? 0.2136 0.2024 0.2489 0.0189  0.0104  0.0238  326  ASP A CB  
2342  C CG  . ASP A 328  ? 0.2534 0.2393 0.2899 0.0193  0.0082  0.0226  326  ASP A CG  
2343  O OD1 . ASP A 328  ? 0.2554 0.2414 0.2948 0.0190  0.0071  0.0233  326  ASP A OD1 
2344  O OD2 . ASP A 328  ? 0.3057 0.2894 0.3407 0.0199  0.0074  0.0212  326  ASP A OD2 
2345  N N   . GLY A 329  ? 0.2030 0.1977 0.2475 0.0195  0.0101  0.0258  327  GLY A N   
2346  C CA  . GLY A 329  ? 0.2034 0.1981 0.2508 0.0183  0.0091  0.0273  327  GLY A CA  
2347  C C   . GLY A 329  ? 0.2320 0.2224 0.2784 0.0164  0.0070  0.0278  327  GLY A C   
2348  O O   . GLY A 329  ? 0.2006 0.1908 0.2482 0.0148  0.0063  0.0292  327  GLY A O   
2349  N N   . ASP A 330  ? 0.2147 0.2019 0.2588 0.0165  0.0058  0.0267  328  ASP A N   
2350  C CA  . ASP A 330  ? 0.2259 0.2099 0.2688 0.0146  0.0038  0.0275  328  ASP A CA  
2351  C C   . ASP A 330  ? 0.1915 0.1749 0.2321 0.0125  0.0042  0.0284  328  ASP A C   
2352  O O   . ASP A 330  ? 0.2130 0.1952 0.2531 0.0108  0.0027  0.0291  328  ASP A O   
2353  C CB  . ASP A 330  ? 0.2278 0.2089 0.2690 0.0150  0.0025  0.0265  328  ASP A CB  
2354  C CG  . ASP A 330  ? 0.3090 0.2898 0.3534 0.0167  0.0012  0.0256  328  ASP A CG  
2355  O OD1 . ASP A 330  ? 0.3346 0.3171 0.3825 0.0173  0.0007  0.0260  328  ASP A OD1 
2356  O OD2 . ASP A 330  ? 0.2678 0.2468 0.3117 0.0176  0.0005  0.0243  328  ASP A OD2 
2357  N N   . LEU A 331  ? 0.1864 0.1709 0.2257 0.0127  0.0061  0.0283  329  LEU A N   
2358  C CA  . LEU A 331  ? 0.1903 0.1741 0.2280 0.0109  0.0064  0.0289  329  LEU A CA  
2359  C C   . LEU A 331  ? 0.1919 0.1779 0.2327 0.0103  0.0069  0.0301  329  LEU A C   
2360  O O   . LEU A 331  ? 0.2115 0.1971 0.2521 0.0089  0.0071  0.0304  329  LEU A O   
2361  C CB  . LEU A 331  ? 0.1936 0.1768 0.2283 0.0113  0.0077  0.0283  329  LEU A CB  
2362  C CG  . LEU A 331  ? 0.1937 0.1742 0.2252 0.0113  0.0069  0.0271  329  LEU A CG  
2363  C CD1 . LEU A 331  ? 0.2077 0.1881 0.2367 0.0121  0.0083  0.0264  329  LEU A CD1 
2364  C CD2 . LEU A 331  ? 0.2269 0.2055 0.2568 0.0093  0.0054  0.0273  329  LEU A CD2 
2365  N N   . SER A 332  ? 0.2025 0.1909 0.2466 0.0111  0.0072  0.0307  330  SER A N   
2366  C CA  . SER A 332  ? 0.2262 0.2171 0.2737 0.0105  0.0079  0.0321  330  SER A CA  
2367  C C   . SER A 332  ? 0.2011 0.1909 0.2499 0.0086  0.0062  0.0323  330  SER A C   
2368  O O   . SER A 332  ? 0.2385 0.2266 0.2859 0.0080  0.0045  0.0317  330  SER A O   
2369  C CB  . SER A 332  ? 0.2280 0.2222 0.2788 0.0120  0.0085  0.0326  330  SER A CB  
2370  O OG  . SER A 332  ? 0.2663 0.2598 0.3186 0.0120  0.0068  0.0323  330  SER A OG  
2371  N N   . GLY A 333  ? 0.1964 0.1874 0.2478 0.0076  0.0065  0.0333  331  GLY A N   
2372  C CA  . GLY A 333  ? 0.2031 0.1935 0.2562 0.0059  0.0049  0.0331  331  GLY A CA  
2373  C C   . GLY A 333  ? 0.2054 0.1937 0.2562 0.0047  0.0043  0.0319  331  GLY A C   
2374  O O   . GLY A 333  ? 0.2518 0.2399 0.3042 0.0034  0.0030  0.0312  331  GLY A O   
2375  N N   . TRP A 334  ? 0.1982 0.1851 0.2455 0.0053  0.0053  0.0314  332  TRP A N   
2376  C CA  . TRP A 334  ? 0.1989 0.1839 0.2438 0.0043  0.0049  0.0301  332  TRP A CA  
2377  C C   . TRP A 334  ? 0.1914 0.1765 0.2368 0.0047  0.0064  0.0309  332  TRP A C   
2378  O O   . TRP A 334  ? 0.2064 0.1922 0.2505 0.0059  0.0079  0.0318  332  TRP A O   
2379  C CB  . TRP A 334  ? 0.2073 0.1907 0.2476 0.0047  0.0045  0.0290  332  TRP A CB  
2380  C CG  . TRP A 334  ? 0.1968 0.1786 0.2340 0.0041  0.0044  0.0277  332  TRP A CG  
2381  C CD1 . TRP A 334  ? 0.1935 0.1753 0.2306 0.0028  0.0032  0.0263  332  TRP A CD1 
2382  C CD2 . TRP A 334  ? 0.1920 0.1726 0.2259 0.0049  0.0055  0.0275  332  TRP A CD2 
2383  N NE1 . TRP A 334  ? 0.2012 0.1817 0.2350 0.0027  0.0036  0.0253  332  TRP A NE1 
2384  C CE2 . TRP A 334  ? 0.1863 0.1659 0.2181 0.0039  0.0049  0.0261  332  TRP A CE2 
2385  C CE3 . TRP A 334  ? 0.2058 0.1863 0.2384 0.0063  0.0068  0.0280  332  TRP A CE3 
2386  C CZ2 . TRP A 334  ? 0.1933 0.1715 0.2217 0.0043  0.0057  0.0255  332  TRP A CZ2 
2387  C CZ3 . TRP A 334  ? 0.2203 0.1995 0.2496 0.0068  0.0074  0.0273  332  TRP A CZ3 
2388  C CH2 . TRP A 334  ? 0.2105 0.1884 0.2378 0.0057  0.0069  0.0262  332  TRP A CH2 
2389  N N   . ASN A 335  ? 0.1822 0.1668 0.2298 0.0036  0.0058  0.0306  333  ASN A N   
2390  C CA  . ASN A 335  ? 0.1888 0.1734 0.2375 0.0037  0.0070  0.0317  333  ASN A CA  
2391  C C   . ASN A 335  ? 0.2003 0.1827 0.2458 0.0034  0.0067  0.0301  333  ASN A C   
2392  O O   . ASN A 335  ? 0.1949 0.1769 0.2420 0.0031  0.0071  0.0307  333  ASN A O   
2393  C CB  . ASN A 335  ? 0.2175 0.2030 0.2722 0.0026  0.0063  0.0330  333  ASN A CB  
2394  C CG  . ASN A 335  ? 0.2337 0.2221 0.2920 0.0030  0.0071  0.0355  333  ASN A CG  
2395  O OD1 . ASN A 335  ? 0.2093 0.1995 0.2659 0.0042  0.0087  0.0367  333  ASN A OD1 
2396  N ND2 . ASN A 335  ? 0.2730 0.2621 0.3367 0.0019  0.0060  0.0362  333  ASN A ND2 
2397  N N   . GLY A 336  ? 0.1902 0.1714 0.2315 0.0034  0.0061  0.0282  334  GLY A N   
2398  C CA  . GLY A 336  ? 0.1743 0.1540 0.2127 0.0031  0.0058  0.0265  334  GLY A CA  
2399  C C   . GLY A 336  ? 0.1881 0.1669 0.2230 0.0041  0.0073  0.0269  334  GLY A C   
2400  O O   . GLY A 336  ? 0.1909 0.1685 0.2238 0.0038  0.0071  0.0256  334  GLY A O   
2401  N N   . MET A 337  ? 0.1782 0.1580 0.2125 0.0053  0.0086  0.0284  335  MET A N   
2402  C CA  A MET A 337  ? 0.1914 0.1709 0.2227 0.0063  0.0099  0.0285  335  MET A CA  
2403  C CA  B MET A 337  ? 0.1918 0.1712 0.2230 0.0063  0.0099  0.0285  335  MET A CA  
2404  C C   . MET A 337  ? 0.1829 0.1625 0.2157 0.0060  0.0105  0.0295  335  MET A C   
2405  O O   . MET A 337  ? 0.2004 0.1816 0.2373 0.0058  0.0108  0.0314  335  MET A O   
2406  C CB  A MET A 337  ? 0.2173 0.1986 0.2481 0.0078  0.0111  0.0295  335  MET A CB  
2407  C CB  B MET A 337  ? 0.2171 0.1984 0.2479 0.0078  0.0111  0.0295  335  MET A CB  
2408  C CG  A MET A 337  ? 0.2379 0.2191 0.2653 0.0090  0.0122  0.0290  335  MET A CG  
2409  C CG  B MET A 337  ? 0.2562 0.2379 0.2843 0.0090  0.0124  0.0296  335  MET A CG  
2410  S SD  A MET A 337  ? 0.3190 0.2972 0.3421 0.0089  0.0110  0.0268  335  MET A SD  
2411  S SD  B MET A 337  ? 0.2597 0.2413 0.2849 0.0106  0.0125  0.0282  335  MET A SD  
2412  C CE  A MET A 337  ? 0.3071 0.2860 0.3310 0.0100  0.0105  0.0266  335  MET A CE  
2413  C CE  B MET A 337  ? 0.2016 0.1798 0.2247 0.0093  0.0106  0.0266  335  MET A CE  
2414  N N   . GLY A 338  ? 0.1895 0.1675 0.2194 0.0060  0.0106  0.0284  336  GLY A N   
2415  C CA  . GLY A 338  ? 0.2048 0.1827 0.2363 0.0058  0.0109  0.0292  336  GLY A CA  
2416  C C   . GLY A 338  ? 0.2018 0.1798 0.2297 0.0068  0.0121  0.0294  336  GLY A C   
2417  O O   . GLY A 338  ? 0.1862 0.1637 0.2102 0.0076  0.0124  0.0282  336  GLY A O   
2418  N N   . PHE A 339  ? 0.1834 0.1623 0.2130 0.0069  0.0127  0.0311  337  PHE A N   
2419  C CA  . PHE A 339  ? 0.1882 0.1680 0.2147 0.0079  0.0140  0.0316  337  PHE A CA  
2420  C C   . PHE A 339  ? 0.1994 0.1790 0.2280 0.0074  0.0138  0.0330  337  PHE A C   
2421  O O   . PHE A 339  ? 0.1956 0.1761 0.2291 0.0067  0.0135  0.0351  337  PHE A O   
2422  C CB  . PHE A 339  ? 0.1835 0.1670 0.2103 0.0091  0.0154  0.0336  337  PHE A CB  
2423  C CG  . PHE A 339  ? 0.1946 0.1798 0.2178 0.0105  0.0167  0.0335  337  PHE A CG  
2424  C CD1 . PHE A 339  ? 0.2094 0.1939 0.2287 0.0115  0.0168  0.0312  337  PHE A CD1 
2425  C CD2 . PHE A 339  ? 0.1860 0.1739 0.2100 0.0107  0.0176  0.0359  337  PHE A CD2 
2426  C CE1 . PHE A 339  ? 0.2127 0.1991 0.2291 0.0129  0.0177  0.0308  337  PHE A CE1 
2427  C CE2 . PHE A 339  ? 0.2292 0.2194 0.2497 0.0121  0.0187  0.0357  337  PHE A CE2 
2428  C CZ  . PHE A 339  ? 0.2198 0.2091 0.2365 0.0132  0.0188  0.0329  337  PHE A CZ  
2429  N N   . VAL A 340  ? 0.1946 0.1729 0.2200 0.0078  0.0140  0.0318  338  VAL A N   
2430  C CA  . VAL A 340  ? 0.1810 0.1589 0.2082 0.0074  0.0137  0.0328  338  VAL A CA  
2431  C C   . VAL A 340  ? 0.1722 0.1533 0.1991 0.0082  0.0151  0.0357  338  VAL A C   
2432  O O   . VAL A 340  ? 0.1946 0.1775 0.2176 0.0094  0.0163  0.0354  338  VAL A O   
2433  C CB  . VAL A 340  ? 0.1882 0.1635 0.2121 0.0074  0.0131  0.0300  338  VAL A CB  
2434  C CG1 . VAL A 340  ? 0.2040 0.1789 0.2300 0.0072  0.0128  0.0310  338  VAL A CG1 
2435  C CG2 . VAL A 340  ? 0.2108 0.1841 0.2350 0.0065  0.0118  0.0273  338  VAL A CG2 
2436  N N   . VAL A 341  ? 0.1821 0.1643 0.2133 0.0076  0.0148  0.0386  339  VAL A N   
2437  C CA  A VAL A 341  ? 0.1896 0.1753 0.2206 0.0082  0.0160  0.0416  339  VAL A CA  
2438  C CA  B VAL A 341  ? 0.1894 0.1751 0.2203 0.0082  0.0160  0.0416  339  VAL A CA  
2439  C C   . VAL A 341  ? 0.1916 0.1755 0.2245 0.0077  0.0150  0.0423  339  VAL A C   
2440  O O   . VAL A 341  ? 0.2077 0.1891 0.2452 0.0066  0.0134  0.0421  339  VAL A O   
2441  C CB  A VAL A 341  ? 0.2076 0.1977 0.2424 0.0080  0.0167  0.0458  339  VAL A CB  
2442  C CB  B VAL A 341  ? 0.2077 0.1977 0.2424 0.0080  0.0167  0.0457  339  VAL A CB  
2443  C CG1 A VAL A 341  ? 0.2069 0.1991 0.2396 0.0088  0.0177  0.0448  339  VAL A CG1 
2444  C CG1 B VAL A 341  ? 0.2229 0.2179 0.2556 0.0090  0.0182  0.0483  339  VAL A CG1 
2445  C CG2 A VAL A 341  ? 0.2012 0.1899 0.2430 0.0064  0.0152  0.0476  339  VAL A CG2 
2446  C CG2 B VAL A 341  ? 0.2029 0.1939 0.2372 0.0083  0.0172  0.0446  339  VAL A CG2 
2447  N N   . GLN A 342  ? 0.1865 0.1719 0.2160 0.0085  0.0158  0.0428  340  GLN A N   
2448  C CA  . GLN A 342  ? 0.1886 0.1723 0.2190 0.0082  0.0150  0.0430  340  GLN A CA  
2449  C C   . GLN A 342  ? 0.1894 0.1767 0.2238 0.0079  0.0151  0.0480  340  GLN A C   
2450  O O   . GLN A 342  ? 0.2097 0.2015 0.2415 0.0087  0.0166  0.0502  340  GLN A O   
2451  C CB  . GLN A 342  ? 0.1821 0.1652 0.2063 0.0093  0.0156  0.0403  340  GLN A CB  
2452  C CG  . GLN A 342  ? 0.1844 0.1643 0.2049 0.0094  0.0153  0.0359  340  GLN A CG  
2453  C CD  . GLN A 342  ? 0.1926 0.1733 0.2073 0.0106  0.0163  0.0341  340  GLN A CD  
2454  O OE1 . GLN A 342  ? 0.1982 0.1824 0.2110 0.0116  0.0175  0.0353  340  GLN A OE1 
2455  N NE2 . GLN A 342  ? 0.1882 0.1660 0.2001 0.0106  0.0157  0.0311  340  GLN A NE2 
2456  N N   . ALA A 343  ? 0.1784 0.1639 0.2193 0.0067  0.0135  0.0497  341  ALA A N   
2457  C CA  . ALA A 343  ? 0.1997 0.1883 0.2456 0.0061  0.0132  0.0551  341  ALA A CA  
2458  C C   . ALA A 343  ? 0.2222 0.2122 0.2661 0.0066  0.0134  0.0565  341  ALA A C   
2459  O O   . ALA A 343  ? 0.2149 0.2091 0.2615 0.0063  0.0137  0.0615  341  ALA A O   
2460  C CB  . ALA A 343  ? 0.2257 0.2114 0.2801 0.0046  0.0110  0.0562  341  ALA A CB  
2461  N N   . TYR A 344  ? 0.2033 0.1905 0.2427 0.0074  0.0134  0.0525  342  TYR A N   
2462  C CA  . TYR A 344  ? 0.1962 0.1853 0.2329 0.0080  0.0138  0.0538  342  TYR A CA  
2463  C C   . TYR A 344  ? 0.2341 0.2288 0.2654 0.0092  0.0159  0.0550  342  TYR A C   
2464  O O   . TYR A 344  ? 0.2339 0.2314 0.2630 0.0098  0.0163  0.0566  342  TYR A O   
2465  C CB  . TYR A 344  ? 0.2028 0.1876 0.2369 0.0084  0.0130  0.0495  342  TYR A CB  
2466  C CG  . TYR A 344  ? 0.1831 0.1664 0.2101 0.0093  0.0139  0.0447  342  TYR A CG  
2467  C CD1 . TYR A 344  ? 0.1954 0.1802 0.2187 0.0099  0.0153  0.0435  342  TYR A CD1 
2468  C CD2 . TYR A 344  ? 0.1988 0.1790 0.2235 0.0096  0.0133  0.0414  342  TYR A CD2 
2469  C CE1 . TYR A 344  ? 0.2049 0.1879 0.2226 0.0106  0.0157  0.0394  342  TYR A CE1 
2470  C CE2 . TYR A 344  ? 0.2080 0.1868 0.2270 0.0102  0.0139  0.0375  342  TYR A CE2 
2471  C CZ  . TYR A 344  ? 0.2035 0.1836 0.2192 0.0107  0.0150  0.0366  342  TYR A CZ  
2472  O OH  . TYR A 344  ? 0.1997 0.1781 0.2105 0.0112  0.0153  0.0329  342  TYR A OH  
2473  N N   . GLY A 345  ? 0.2029 0.1995 0.2321 0.0096  0.0171  0.0542  343  GLY A N   
2474  C CA  . GLY A 345  ? 0.2089 0.2109 0.2331 0.0109  0.0189  0.0545  343  GLY A CA  
2475  C C   . GLY A 345  ? 0.2157 0.2245 0.2431 0.0106  0.0198  0.0599  343  GLY A C   
2476  O O   . GLY A 345  ? 0.2124 0.2213 0.2451 0.0095  0.0193  0.0625  343  GLY A O   
2477  N N   . LYS A 346  ? 0.2081 0.2231 0.2322 0.0117  0.0211  0.0616  344  LYS A N   
2478  C CA  . LYS A 346  ? 0.2024 0.2253 0.2288 0.0115  0.0220  0.0670  344  LYS A CA  
2479  C C   . LYS A 346  ? 0.2241 0.2504 0.2507 0.0118  0.0232  0.0669  344  LYS A C   
2480  O O   . LYS A 346  ? 0.2221 0.2541 0.2525 0.0111  0.0238  0.0718  344  LYS A O   
2481  C CB  . LYS A 346  ? 0.2138 0.2433 0.2359 0.0127  0.0232  0.0682  344  LYS A CB  
2482  C CG  . LYS A 346  ? 0.2269 0.2539 0.2495 0.0123  0.0219  0.0691  344  LYS A CG  
2483  C CD  . LYS A 346  ? 0.2472 0.2806 0.2648 0.0137  0.0230  0.0696  344  LYS A CD  
2484  C CE  . LYS A 346  ? 0.2449 0.2766 0.2642 0.0130  0.0216  0.0718  344  LYS A CE  
2485  N NZ  . LYS A 346  ? 0.2611 0.2985 0.2751 0.0145  0.0225  0.0715  344  LYS A NZ  
2486  N N   . ARG A 347  ? 0.2055 0.2287 0.2285 0.0129  0.0236  0.0617  345  ARG A N   
2487  C CA  . ARG A 347  ? 0.1976 0.2237 0.2208 0.0133  0.0246  0.0611  345  ARG A CA  
2488  C C   . ARG A 347  ? 0.2075 0.2290 0.2359 0.0118  0.0235  0.0617  345  ARG A C   
2489  O O   . ARG A 347  ? 0.2044 0.2287 0.2341 0.0119  0.0243  0.0621  345  ARG A O   
2490  C CB  . ARG A 347  ? 0.2259 0.2510 0.2433 0.0152  0.0253  0.0554  345  ARG A CB  
2491  C CG  . ARG A 347  ? 0.2071 0.2383 0.2199 0.0170  0.0265  0.0546  345  ARG A CG  
2492  C CD  . ARG A 347  ? 0.2012 0.2296 0.2091 0.0187  0.0265  0.0486  345  ARG A CD  
2493  N NE  . ARG A 347  ? 0.2112 0.2319 0.2177 0.0181  0.0252  0.0460  345  ARG A NE  
2494  C CZ  . ARG A 347  ? 0.2058 0.2222 0.2091 0.0190  0.0247  0.0412  345  ARG A CZ  
2495  N NH1 . ARG A 347  ? 0.2079 0.2264 0.2092 0.0206  0.0252  0.0381  345  ARG A NH1 
2496  N NH2 . ARG A 347  ? 0.2064 0.2164 0.2087 0.0182  0.0235  0.0394  345  ARG A NH2 
2497  N N   . CYS A 348  ? 0.1982 0.2134 0.2299 0.0104  0.0218  0.0618  346  CYS A N   
2498  C CA  . CYS A 348  ? 0.2007 0.2110 0.2369 0.0091  0.0205  0.0610  346  CYS A CA  
2499  C C   . CYS A 348  ? 0.1976 0.2119 0.2387 0.0083  0.0208  0.0647  346  CYS A C   
2500  O O   . CYS A 348  ? 0.2103 0.2235 0.2516 0.0084  0.0209  0.0626  346  CYS A O   
2501  C CB  . CYS A 348  ? 0.2229 0.2275 0.2631 0.0078  0.0184  0.0611  346  CYS A CB  
2502  S SG  . CYS A 348  ? 0.2649 0.2628 0.3088 0.0067  0.0166  0.0579  346  CYS A SG  
2503  N N   . PRO A 349  ? 0.1992 0.2185 0.2448 0.0074  0.0209  0.0705  347  PRO A N   
2504  C CA  . PRO A 349  ? 0.2108 0.2340 0.2615 0.0064  0.0212  0.0742  347  PRO A CA  
2505  C C   . PRO A 349  ? 0.2141 0.2431 0.2610 0.0079  0.0233  0.0731  347  PRO A C   
2506  O O   . PRO A 349  ? 0.2200 0.2497 0.2698 0.0074  0.0233  0.0734  347  PRO A O   
2507  C CB  . PRO A 349  ? 0.2307 0.2589 0.2865 0.0052  0.0209  0.0811  347  PRO A CB  
2508  C CG  . PRO A 349  ? 0.2623 0.2921 0.3133 0.0062  0.0214  0.0808  347  PRO A CG  
2509  C CD  . PRO A 349  ? 0.2161 0.2384 0.2625 0.0071  0.0208  0.0743  347  PRO A CD  
2510  N N   . PHE A 350  ? 0.2029 0.2359 0.2436 0.0097  0.0248  0.0713  348  PHE A N   
2511  C CA  . PHE A 350  ? 0.2133 0.2520 0.2506 0.0114  0.0266  0.0695  348  PHE A CA  
2512  C C   . PHE A 350  ? 0.2075 0.2403 0.2421 0.0123  0.0262  0.0637  348  PHE A C   
2513  O O   . PHE A 350  ? 0.2062 0.2414 0.2410 0.0130  0.0270  0.0626  348  PHE A O   
2514  C CB  . PHE A 350  ? 0.2189 0.2641 0.2510 0.0132  0.0281  0.0692  348  PHE A CB  
2515  C CG  . PHE A 350  ? 0.2271 0.2780 0.2616 0.0122  0.0283  0.0753  348  PHE A CG  
2516  C CD1 . PHE A 350  ? 0.2639 0.3233 0.3022 0.0115  0.0293  0.0808  348  PHE A CD1 
2517  C CD2 . PHE A 350  ? 0.2386 0.2863 0.2724 0.0117  0.0273  0.0758  348  PHE A CD2 
2518  C CE1 . PHE A 350  ? 0.2573 0.3223 0.2984 0.0103  0.0292  0.0871  348  PHE A CE1 
2519  C CE2 . PHE A 350  ? 0.2826 0.3354 0.3192 0.0107  0.0272  0.0818  348  PHE A CE2 
2520  C CZ  . PHE A 350  ? 0.2819 0.3434 0.3222 0.0099  0.0281  0.0876  348  PHE A CZ  
2521  N N   . VAL A 351  ? 0.2016 0.2268 0.2340 0.0122  0.0250  0.0601  349  VAL A N   
2522  C CA  . VAL A 351  ? 0.2025 0.2218 0.2330 0.0126  0.0243  0.0552  349  VAL A CA  
2523  C C   . VAL A 351  ? 0.2090 0.2258 0.2447 0.0111  0.0233  0.0563  349  VAL A C   
2524  O O   . VAL A 351  ? 0.2081 0.2247 0.2435 0.0116  0.0235  0.0543  349  VAL A O   
2525  C CB  . VAL A 351  ? 0.1807 0.1931 0.2082 0.0125  0.0231  0.0518  349  VAL A CB  
2526  C CG1 . VAL A 351  ? 0.1985 0.2053 0.2250 0.0125  0.0222  0.0476  349  VAL A CG1 
2527  C CG2 . VAL A 351  ? 0.2131 0.2279 0.2353 0.0141  0.0240  0.0501  349  VAL A CG2 
2528  N N   . LEU A 352  ? 0.2097 0.2249 0.2507 0.0093  0.0221  0.0596  350  LEU A N   
2529  C CA  . LEU A 352  ? 0.1950 0.2083 0.2417 0.0078  0.0210  0.0608  350  LEU A CA  
2530  C C   . LEU A 352  ? 0.2030 0.2227 0.2519 0.0080  0.0223  0.0636  350  LEU A C   
2531  O O   . LEU A 352  ? 0.2103 0.2288 0.2610 0.0078  0.0220  0.0623  350  LEU A O   
2532  C CB  . LEU A 352  ? 0.2134 0.2243 0.2662 0.0059  0.0193  0.0640  350  LEU A CB  
2533  C CG  . LEU A 352  ? 0.2151 0.2190 0.2667 0.0056  0.0177  0.0606  350  LEU A CG  
2534  C CD1 . LEU A 352  ? 0.2477 0.2501 0.3060 0.0041  0.0160  0.0638  350  LEU A CD1 
2535  C CD2 . LEU A 352  ? 0.2509 0.2497 0.3018 0.0055  0.0167  0.0561  350  LEU A CD2 
2536  N N   . ASP A 353  ? 0.2019 0.2292 0.2509 0.0084  0.0238  0.0674  351  ASP A N   
2537  C CA  . ASP A 353  ? 0.2118 0.2464 0.2625 0.0088  0.0253  0.0698  351  ASP A CA  
2538  C C   . ASP A 353  ? 0.1941 0.2288 0.2405 0.0107  0.0262  0.0650  351  ASP A C   
2539  O O   . ASP A 353  ? 0.2064 0.2428 0.2552 0.0107  0.0264  0.0651  351  ASP A O   
2540  C CB  . ASP A 353  ? 0.2149 0.2587 0.2649 0.0093  0.0270  0.0740  351  ASP A CB  
2541  C CG  . ASP A 353  ? 0.2436 0.2890 0.2994 0.0073  0.0261  0.0803  351  ASP A CG  
2542  O OD1 . ASP A 353  ? 0.2597 0.3007 0.3216 0.0054  0.0244  0.0820  351  ASP A OD1 
2543  O OD2 . ASP A 353  ? 0.3006 0.3521 0.3551 0.0075  0.0271  0.0834  351  ASP A OD2 
2544  N N   . PHE A 354  ? 0.2059 0.2388 0.2462 0.0124  0.0265  0.0608  352  PHE A N   
2545  C CA  . PHE A 354  ? 0.1856 0.2181 0.2224 0.0142  0.0270  0.0561  352  PHE A CA  
2546  C C   . PHE A 354  ? 0.1886 0.2140 0.2271 0.0133  0.0254  0.0537  352  PHE A C   
2547  O O   . PHE A 354  ? 0.2005 0.2270 0.2397 0.0140  0.0256  0.0523  352  PHE A O   
2548  C CB  . PHE A 354  ? 0.1977 0.2289 0.2285 0.0159  0.0272  0.0523  352  PHE A CB  
2549  C CG  . PHE A 354  ? 0.2142 0.2427 0.2421 0.0175  0.0270  0.0472  352  PHE A CG  
2550  C CD1 . PHE A 354  ? 0.2245 0.2589 0.2513 0.0195  0.0282  0.0456  352  PHE A CD1 
2551  C CD2 . PHE A 354  ? 0.2310 0.2513 0.2579 0.0169  0.0253  0.0442  352  PHE A CD2 
2552  C CE1 . PHE A 354  ? 0.2421 0.2738 0.2672 0.0210  0.0276  0.0410  352  PHE A CE1 
2553  C CE2 . PHE A 354  ? 0.2326 0.2504 0.2575 0.0181  0.0249  0.0401  352  PHE A CE2 
2554  C CZ  . PHE A 354  ? 0.2310 0.2542 0.2554 0.0201  0.0259  0.0386  352  PHE A CZ  
2555  N N   . ILE A 355  ? 0.1792 0.1977 0.2184 0.0119  0.0238  0.0530  353  ILE A N   
2556  C CA  . ILE A 355  ? 0.1828 0.1952 0.2231 0.0111  0.0222  0.0504  353  ILE A CA  
2557  C C   . ILE A 355  ? 0.2097 0.2234 0.2557 0.0099  0.0218  0.0530  353  ILE A C   
2558  O O   . ILE A 355  ? 0.2003 0.2125 0.2470 0.0100  0.0212  0.0511  353  ILE A O   
2559  C CB  . ILE A 355  ? 0.2013 0.2071 0.2410 0.0100  0.0206  0.0490  353  ILE A CB  
2560  C CG1 . ILE A 355  ? 0.2151 0.2191 0.2489 0.0113  0.0209  0.0458  353  ILE A CG1 
2561  C CG2 . ILE A 355  ? 0.2116 0.2124 0.2533 0.0089  0.0189  0.0469  353  ILE A CG2 
2562  C CD1 . ILE A 355  ? 0.2412 0.2401 0.2744 0.0103  0.0196  0.0449  353  ILE A CD1 
2563  N N   . ILE A 356  ? 0.2041 0.2205 0.2548 0.0085  0.0218  0.0575  354  ILE A N   
2564  C CA  . ILE A 356  ? 0.1950 0.2130 0.2519 0.0072  0.0212  0.0603  354  ILE A CA  
2565  C C   . ILE A 356  ? 0.2018 0.2257 0.2585 0.0084  0.0228  0.0606  354  ILE A C   
2566  O O   . ILE A 356  ? 0.2049 0.2281 0.2643 0.0081  0.0222  0.0600  354  ILE A O   
2567  C CB  . ILE A 356  ? 0.2179 0.2381 0.2803 0.0056  0.0208  0.0655  354  ILE A CB  
2568  C CG1 . ILE A 356  ? 0.2226 0.2359 0.2866 0.0043  0.0187  0.0644  354  ILE A CG1 
2569  C CG2 . ILE A 356  ? 0.2400 0.2639 0.3091 0.0043  0.0207  0.0693  354  ILE A CG2 
2570  C CD1 . ILE A 356  ? 0.2347 0.2497 0.3033 0.0031  0.0182  0.0691  354  ILE A CD1 
2571  N N   . ASP A 357  ? 0.2067 0.2367 0.2601 0.0100  0.0247  0.0612  355  ASP A N   
2572  C CA  . ASP A 357  ? 0.2019 0.2381 0.2550 0.0115  0.0262  0.0607  355  ASP A CA  
2573  C C   . ASP A 357  ? 0.1908 0.2228 0.2408 0.0129  0.0256  0.0555  355  ASP A C   
2574  O O   . ASP A 357  ? 0.2032 0.2371 0.2553 0.0133  0.0257  0.0550  355  ASP A O   
2575  C CB  . ASP A 357  ? 0.2183 0.2626 0.2684 0.0131  0.0283  0.0620  355  ASP A CB  
2576  C CG  . ASP A 357  ? 0.2434 0.2942 0.2927 0.0151  0.0297  0.0603  355  ASP A CG  
2577  O OD1 . ASP A 357  ? 0.2775 0.3343 0.3310 0.0146  0.0305  0.0637  355  ASP A OD1 
2578  O OD2 . ASP A 357  ? 0.2356 0.2855 0.2806 0.0172  0.0300  0.0557  355  ASP A OD2 
2579  N N   . LEU A 358  ? 0.1936 0.2202 0.2390 0.0135  0.0249  0.0518  356  LEU A N   
2580  C CA  . LEU A 358  ? 0.1955 0.2178 0.2386 0.0145  0.0240  0.0474  356  LEU A CA  
2581  C C   . LEU A 358  ? 0.1914 0.2092 0.2379 0.0129  0.0224  0.0474  356  LEU A C   
2582  O O   . LEU A 358  ? 0.1966 0.2141 0.2437 0.0135  0.0220  0.0456  356  LEU A O   
2583  C CB  . LEU A 358  ? 0.1772 0.1944 0.2154 0.0150  0.0234  0.0442  356  LEU A CB  
2584  C CG  . LEU A 358  ? 0.1886 0.2006 0.2247 0.0156  0.0221  0.0402  356  LEU A CG  
2585  C CD1 . LEU A 358  ? 0.2292 0.2449 0.2649 0.0177  0.0227  0.0382  356  LEU A CD1 
2586  C CD2 . LEU A 358  ? 0.1881 0.1956 0.2198 0.0158  0.0214  0.0378  356  LEU A CD2 
2587  N N   . ALA A 359  ? 0.1903 0.2048 0.2395 0.0109  0.0213  0.0492  357  ALA A N   
2588  C CA  . ALA A 359  ? 0.2005 0.2114 0.2535 0.0094  0.0196  0.0491  357  ALA A CA  
2589  C C   . ALA A 359  ? 0.1944 0.2100 0.2520 0.0092  0.0201  0.0515  357  ALA A C   
2590  O O   . ALA A 359  ? 0.2080 0.2220 0.2672 0.0090  0.0192  0.0501  357  ALA A O   
2591  C CB  . ALA A 359  ? 0.2315 0.2388 0.2873 0.0075  0.0182  0.0504  357  ALA A CB  
2592  N N   . ARG A 360  ? 0.1972 0.2191 0.2571 0.0092  0.0216  0.0552  358  ARG A N   
2593  C CA  . ARG A 360  ? 0.2073 0.2347 0.2716 0.0091  0.0223  0.0577  358  ARG A CA  
2594  C C   . ARG A 360  ? 0.2380 0.2680 0.2999 0.0112  0.0232  0.0549  358  ARG A C   
2595  O O   . ARG A 360  ? 0.2502 0.2805 0.3150 0.0111  0.0226  0.0545  358  ARG A O   
2596  C CB  . ARG A 360  ? 0.2224 0.2570 0.2895 0.0087  0.0238  0.0626  358  ARG A CB  
2597  C CG  . ARG A 360  ? 0.2901 0.3227 0.3620 0.0063  0.0226  0.0664  358  ARG A CG  
2598  C CD  . ARG A 360  ? 0.3490 0.3896 0.4250 0.0056  0.0239  0.0723  358  ARG A CD  
2599  N NE  . ARG A 360  ? 0.3740 0.4127 0.4533 0.0038  0.0228  0.0757  358  ARG A NE  
2600  C CZ  . ARG A 360  ? 0.4632 0.4987 0.5493 0.0016  0.0208  0.0779  358  ARG A CZ  
2601  N NH1 . ARG A 360  ? 0.5300 0.5644 0.6202 0.0008  0.0198  0.0776  358  ARG A NH1 
2602  N NH2 . ARG A 360  ? 0.4408 0.4742 0.5298 0.0003  0.0196  0.0805  358  ARG A NH2 
2603  N N   . ARG A 361  ? 0.2233 0.2553 0.2804 0.0132  0.0244  0.0527  359  ARG A N   
2604  C CA  . ARG A 361  ? 0.2288 0.2635 0.2841 0.0155  0.0251  0.0497  359  ARG A CA  
2605  C C   . ARG A 361  ? 0.2269 0.2551 0.2816 0.0155  0.0232  0.0463  359  ARG A C   
2606  O O   . ARG A 361  ? 0.2521 0.2817 0.3086 0.0163  0.0230  0.0452  359  ARG A O   
2607  C CB  . ARG A 361  ? 0.2626 0.2999 0.3130 0.0176  0.0263  0.0475  359  ARG A CB  
2608  C CG  . ARG A 361  ? 0.2836 0.3297 0.3343 0.0182  0.0284  0.0505  359  ARG A CG  
2609  C CD  . ARG A 361  ? 0.2740 0.3228 0.3198 0.0207  0.0293  0.0473  359  ARG A CD  
2610  N NE  . ARG A 361  ? 0.2572 0.3007 0.2993 0.0202  0.0286  0.0463  359  ARG A NE  
2611  C CZ  . ARG A 361  ? 0.2490 0.2879 0.2872 0.0215  0.0278  0.0420  359  ARG A CZ  
2612  N NH1 . ARG A 361  ? 0.2569 0.2947 0.2948 0.0231  0.0273  0.0382  359  ARG A NH1 
2613  N NH2 . ARG A 361  ? 0.2396 0.2752 0.2745 0.0211  0.0275  0.0415  359  ARG A NH2 
2614  N N   . SER A 362  ? 0.2154 0.2366 0.2674 0.0147  0.0218  0.0446  360  SER A N   
2615  C CA  . SER A 362  ? 0.2061 0.2216 0.2569 0.0146  0.0200  0.0416  360  SER A CA  
2616  C C   . SER A 362  ? 0.2118 0.2248 0.2666 0.0127  0.0185  0.0427  360  SER A C   
2617  O O   . SER A 362  ? 0.2205 0.2305 0.2753 0.0127  0.0171  0.0408  360  SER A O   
2618  C CB  . SER A 362  ? 0.2164 0.2265 0.2629 0.0144  0.0192  0.0395  360  SER A CB  
2619  O OG  . SER A 362  ? 0.2036 0.2112 0.2511 0.0124  0.0186  0.0412  360  SER A OG  
2620  N N   . GLY A 363  ? 0.2131 0.2273 0.2715 0.0110  0.0186  0.0458  361  GLY A N   
2621  C CA  . GLY A 363  ? 0.2241 0.2353 0.2863 0.0091  0.0168  0.0464  361  GLY A CA  
2622  C C   . GLY A 363  ? 0.2466 0.2516 0.3067 0.0081  0.0150  0.0441  361  GLY A C   
2623  O O   . GLY A 363  ? 0.2657 0.2682 0.3283 0.0067  0.0134  0.0437  361  GLY A O   
2624  N N   . ARG A 364  ? 0.2145 0.2172 0.2700 0.0086  0.0153  0.0426  362  ARG A N   
2625  C CA  . ARG A 364  ? 0.2344 0.2318 0.2875 0.0077  0.0138  0.0405  362  ARG A CA  
2626  C C   . ARG A 364  ? 0.2096 0.2063 0.2649 0.0064  0.0136  0.0422  362  ARG A C   
2627  O O   . ARG A 364  ? 0.2319 0.2311 0.2869 0.0068  0.0150  0.0441  362  ARG A O   
2628  C CB  . ARG A 364  ? 0.2501 0.2457 0.2976 0.0089  0.0142  0.0382  362  ARG A CB  
2629  C CG  . ARG A 364  ? 0.3004 0.2967 0.3459 0.0105  0.0143  0.0365  362  ARG A CG  
2630  C CD  . ARG A 364  ? 0.2331 0.2260 0.2777 0.0099  0.0125  0.0346  362  ARG A CD  
2631  N NE  . ARG A 364  ? 0.2203 0.2145 0.2650 0.0113  0.0125  0.0339  362  ARG A NE  
2632  C CZ  . ARG A 364  ? 0.2045 0.1976 0.2465 0.0126  0.0123  0.0320  362  ARG A CZ  
2633  N NH1 . ARG A 364  ? 0.2010 0.1913 0.2393 0.0125  0.0120  0.0308  362  ARG A NH1 
2634  N NH2 . ARG A 364  ? 0.2061 0.2009 0.2493 0.0141  0.0122  0.0314  362  ARG A NH2 
2635  N N   . ARG A 365  ? 0.2126 0.2064 0.2704 0.0049  0.0118  0.0414  363  ARG A N   
2636  C CA  . ARG A 365  ? 0.1934 0.1860 0.2540 0.0037  0.0113  0.0425  363  ARG A CA  
2637  C C   . ARG A 365  ? 0.2042 0.1939 0.2600 0.0041  0.0112  0.0403  363  ARG A C   
2638  O O   . ARG A 365  ? 0.2303 0.2168 0.2849 0.0035  0.0097  0.0376  363  ARG A O   
2639  C CB  . ARG A 365  ? 0.2166 0.2075 0.2823 0.0022  0.0092  0.0419  363  ARG A CB  
2640  C CG  . ARG A 365  ? 0.2245 0.2143 0.2945 0.0011  0.0082  0.0431  363  ARG A CG  
2641  C CD  . ARG A 365  ? 0.2756 0.2654 0.3528 -0.0003 0.0064  0.0438  363  ARG A CD  
2642  N NE  . ARG A 365  ? 0.2410 0.2297 0.3233 -0.0013 0.0054  0.0453  363  ARG A NE  
2643  C CZ  . ARG A 365  ? 0.2272 0.2126 0.3115 -0.0020 0.0034  0.0424  363  ARG A CZ  
2644  N NH1 . ARG A 365  ? 0.2725 0.2560 0.3541 -0.0019 0.0022  0.0382  363  ARG A NH1 
2645  N NH2 . ARG A 365  ? 0.2142 0.1986 0.3033 -0.0027 0.0024  0.0439  363  ARG A NH2 
2646  N N   . ILE A 366  ? 0.1959 0.1870 0.2487 0.0051  0.0128  0.0414  364  ILE A N   
2647  C CA  . ILE A 366  ? 0.2073 0.1960 0.2552 0.0056  0.0129  0.0393  364  ILE A CA  
2648  C C   . ILE A 366  ? 0.2053 0.1913 0.2553 0.0044  0.0116  0.0388  364  ILE A C   
2649  O O   . ILE A 366  ? 0.1985 0.1855 0.2533 0.0037  0.0114  0.0414  364  ILE A O   
2650  C CB  . ILE A 366  ? 0.1978 0.1892 0.2426 0.0070  0.0148  0.0406  364  ILE A CB  
2651  C CG1 . ILE A 366  ? 0.2298 0.2239 0.2728 0.0084  0.0159  0.0401  364  ILE A CG1 
2652  C CG2 . ILE A 366  ? 0.2235 0.2124 0.2637 0.0074  0.0148  0.0386  364  ILE A CG2 
2653  C CD1 . ILE A 366  ? 0.2277 0.2259 0.2684 0.0100  0.0178  0.0412  364  ILE A CD1 
2654  N N   . MET A 367  ? 0.1989 0.1818 0.2458 0.0043  0.0106  0.0357  365  MET A N   
2655  C CA  . MET A 367  ? 0.1858 0.1663 0.2343 0.0035  0.0094  0.0345  365  MET A CA  
2656  C C   . MET A 367  ? 0.2098 0.1903 0.2557 0.0041  0.0105  0.0354  365  MET A C   
2657  O O   . MET A 367  ? 0.2487 0.2289 0.2892 0.0050  0.0113  0.0341  365  MET A O   
2658  C CB  . MET A 367  ? 0.1847 0.1630 0.2306 0.0031  0.0080  0.0307  365  MET A CB  
2659  C CG  . MET A 367  ? 0.2006 0.1794 0.2482 0.0026  0.0070  0.0299  365  MET A CG  
2660  S SD  . MET A 367  ? 0.2290 0.2066 0.2736 0.0020  0.0053  0.0258  365  MET A SD  
2661  C CE  . MET A 367  ? 0.2735 0.2504 0.3238 0.0010  0.0033  0.0238  365  MET A CE  
2662  N N   . VAL A 368  ? 0.1704 0.1515 0.2204 0.0036  0.0103  0.0378  366  VAL A N   
2663  C CA  . VAL A 368  ? 0.1814 0.1632 0.2293 0.0043  0.0114  0.0393  366  VAL A CA  
2664  C C   . VAL A 368  ? 0.1831 0.1620 0.2326 0.0036  0.0100  0.0377  366  VAL A C   
2665  O O   . VAL A 368  ? 0.2035 0.1818 0.2592 0.0027  0.0086  0.0388  366  VAL A O   
2666  C CB  . VAL A 368  ? 0.1966 0.1823 0.2478 0.0042  0.0125  0.0439  366  VAL A CB  
2667  C CG1 . VAL A 368  ? 0.2145 0.2013 0.2633 0.0049  0.0135  0.0453  366  VAL A CG1 
2668  C CG2 . VAL A 368  ? 0.2142 0.2034 0.2639 0.0050  0.0139  0.0449  366  VAL A CG2 
2669  N N   . ARG A 369  ? 0.1757 0.1530 0.2202 0.0042  0.0102  0.0352  367  ARG A N   
2670  C CA  . ARG A 369  ? 0.1938 0.1688 0.2396 0.0039  0.0090  0.0336  367  ARG A CA  
2671  C C   . ARG A 369  ? 0.1934 0.1695 0.2393 0.0043  0.0098  0.0364  367  ARG A C   
2672  O O   . ARG A 369  ? 0.2138 0.1910 0.2545 0.0052  0.0113  0.0366  367  ARG A O   
2673  C CB  . ARG A 369  ? 0.2021 0.1753 0.2427 0.0042  0.0087  0.0295  367  ARG A CB  
2674  C CG  . ARG A 369  ? 0.2094 0.1807 0.2518 0.0039  0.0074  0.0275  367  ARG A CG  
2675  C CD  . ARG A 369  ? 0.2200 0.1905 0.2566 0.0043  0.0077  0.0246  367  ARG A CD  
2676  N NE  . ARG A 369  ? 0.2119 0.1824 0.2462 0.0040  0.0072  0.0219  367  ARG A NE  
2677  C CZ  . ARG A 369  ? 0.2340 0.2045 0.2628 0.0042  0.0076  0.0202  367  ARG A CZ  
2678  N NH1 . ARG A 369  ? 0.2241 0.1943 0.2490 0.0049  0.0087  0.0205  367  ARG A NH1 
2679  N NH2 . ARG A 369  ? 0.2155 0.1866 0.2430 0.0037  0.0070  0.0184  367  ARG A NH2 
2680  N N   . LEU A 370  ? 0.1919 0.1677 0.2439 0.0035  0.0087  0.0385  368  LEU A N   
2681  C CA  . LEU A 370  ? 0.1799 0.1569 0.2328 0.0037  0.0092  0.0415  368  LEU A CA  
2682  C C   . LEU A 370  ? 0.2012 0.1753 0.2535 0.0039  0.0081  0.0386  368  LEU A C   
2683  O O   . LEU A 370  ? 0.1925 0.1642 0.2492 0.0033  0.0061  0.0364  368  LEU A O   
2684  C CB  . LEU A 370  ? 0.2115 0.1898 0.2723 0.0027  0.0083  0.0459  368  LEU A CB  
2685  C CG  . LEU A 370  ? 0.2185 0.1989 0.2808 0.0028  0.0087  0.0501  368  LEU A CG  
2686  C CD1 . LEU A 370  ? 0.2340 0.2189 0.2907 0.0037  0.0112  0.0524  368  LEU A CD1 
2687  C CD2 . LEU A 370  ? 0.2245 0.2058 0.2960 0.0014  0.0072  0.0544  368  LEU A CD2 
2688  N N   . VAL A 371  ? 0.1954 0.1699 0.2423 0.0047  0.0092  0.0384  369  VAL A N   
2689  C CA  . VAL A 371  ? 0.1960 0.1683 0.2419 0.0050  0.0084  0.0359  369  VAL A CA  
2690  C C   . VAL A 371  ? 0.1895 0.1634 0.2357 0.0053  0.0090  0.0394  369  VAL A C   
2691  O O   . VAL A 371  ? 0.2163 0.1935 0.2622 0.0055  0.0103  0.0432  369  VAL A O   
2692  C CB  . VAL A 371  ? 0.1959 0.1672 0.2345 0.0056  0.0092  0.0321  369  VAL A CB  
2693  C CG1 . VAL A 371  ? 0.2135 0.1841 0.2513 0.0053  0.0087  0.0293  369  VAL A CG1 
2694  C CG2 . VAL A 371  ? 0.2208 0.1942 0.2537 0.0066  0.0112  0.0335  369  VAL A CG2 
2695  N N   . LYS A 372  ? 0.2009 0.1730 0.2478 0.0054  0.0081  0.0381  370  LYS A N   
2696  C CA  . LYS A 372  ? 0.2140 0.1879 0.2600 0.0059  0.0087  0.0411  370  LYS A CA  
2697  C C   . LYS A 372  ? 0.2141 0.1893 0.2519 0.0069  0.0106  0.0398  370  LYS A C   
2698  O O   . LYS A 372  ? 0.2512 0.2298 0.2863 0.0075  0.0121  0.0425  370  LYS A O   
2699  C CB  . LYS A 372  ? 0.2351 0.2068 0.2864 0.0055  0.0068  0.0411  370  LYS A CB  
2700  C CG  . LYS A 372  ? 0.2168 0.1882 0.2773 0.0045  0.0050  0.0439  370  LYS A CG  
2701  C CD  . LYS A 372  ? 0.2483 0.2173 0.3158 0.0041  0.0026  0.0436  370  LYS A CD  
2702  C CE  . LYS A 372  ? 0.2315 0.1995 0.3083 0.0030  0.0005  0.0453  370  LYS A CE  
2703  N NZ  . LYS A 372  ? 0.2432 0.2086 0.3281 0.0028  -0.0023 0.0447  370  LYS A NZ  
2704  N N   . GLY A 373  ? 0.2018 0.1746 0.2356 0.0073  0.0104  0.0356  371  GLY A N   
2705  C CA  . GLY A 373  ? 0.2051 0.1787 0.2317 0.0082  0.0118  0.0340  371  GLY A CA  
2706  C C   . GLY A 373  ? 0.1989 0.1704 0.2229 0.0084  0.0113  0.0307  371  GLY A C   
2707  O O   . GLY A 373  ? 0.2210 0.1916 0.2481 0.0083  0.0103  0.0308  371  GLY A O   
2708  N N   . ALA A 374  ? 0.1985 0.1695 0.2170 0.0088  0.0120  0.0280  372  ALA A N   
2709  C CA  . ALA A 374  ? 0.1924 0.1617 0.2086 0.0088  0.0114  0.0247  372  ALA A CA  
2710  C C   . ALA A 374  ? 0.2338 0.2037 0.2454 0.0095  0.0122  0.0244  372  ALA A C   
2711  O O   . ALA A 374  ? 0.2337 0.2024 0.2435 0.0095  0.0118  0.0219  372  ALA A O   
2712  C CB  . ALA A 374  ? 0.2232 0.1916 0.2372 0.0083  0.0112  0.0217  372  ALA A CB  
2713  N N   . TYR A 375  ? 0.2098 0.1819 0.2195 0.0103  0.0133  0.0268  373  TYR A N   
2714  C CA  . TYR A 375  ? 0.2008 0.1737 0.2058 0.0112  0.0140  0.0261  373  TYR A CA  
2715  C C   . TYR A 375  ? 0.1960 0.1711 0.2019 0.0117  0.0143  0.0287  373  TYR A C   
2716  O O   . TYR A 375  ? 0.2194 0.1966 0.2217 0.0126  0.0151  0.0290  373  TYR A O   
2717  C CB  . TYR A 375  ? 0.2277 0.2021 0.2292 0.0119  0.0150  0.0257  373  TYR A CB  
2718  C CG  . TYR A 375  ? 0.2079 0.1805 0.2086 0.0114  0.0147  0.0236  373  TYR A CG  
2719  C CD1 . TYR A 375  ? 0.2133 0.1859 0.2170 0.0108  0.0146  0.0245  373  TYR A CD1 
2720  C CD2 . TYR A 375  ? 0.2509 0.2222 0.2482 0.0114  0.0145  0.0211  373  TYR A CD2 
2721  C CE1 . TYR A 375  ? 0.2380 0.2093 0.2410 0.0103  0.0142  0.0228  373  TYR A CE1 
2722  C CE2 . TYR A 375  ? 0.2543 0.2243 0.2511 0.0108  0.0141  0.0197  373  TYR A CE2 
2723  C CZ  . TYR A 375  ? 0.2964 0.2666 0.2960 0.0103  0.0140  0.0206  373  TYR A CZ  
2724  O OH  . TYR A 375  ? 0.3012 0.2704 0.3002 0.0097  0.0135  0.0194  373  TYR A OH  
2725  N N   . TRP A 376  ? 0.1942 0.1690 0.2049 0.0112  0.0134  0.0307  374  TRP A N   
2726  C CA  . TRP A 376  ? 0.2144 0.1919 0.2267 0.0115  0.0135  0.0343  374  TRP A CA  
2727  C C   . TRP A 376  ? 0.2248 0.2031 0.2331 0.0123  0.0138  0.0334  374  TRP A C   
2728  O O   . TRP A 376  ? 0.2212 0.2031 0.2270 0.0131  0.0147  0.0352  374  TRP A O   
2729  C CB  . TRP A 376  ? 0.2170 0.1934 0.2361 0.0107  0.0121  0.0365  374  TRP A CB  
2730  C CG  . TRP A 376  ? 0.2270 0.2067 0.2483 0.0109  0.0121  0.0410  374  TRP A CG  
2731  C CD1 . TRP A 376  ? 0.2232 0.2068 0.2460 0.0108  0.0128  0.0453  374  TRP A CD1 
2732  C CD2 . TRP A 376  ? 0.2296 0.2093 0.2515 0.0111  0.0114  0.0417  374  TRP A CD2 
2733  N NE1 . TRP A 376  ? 0.2310 0.2174 0.2554 0.0109  0.0125  0.0490  374  TRP A NE1 
2734  C CE2 . TRP A 376  ? 0.2375 0.2213 0.2615 0.0111  0.0116  0.0469  374  TRP A CE2 
2735  C CE3 . TRP A 376  ? 0.2600 0.2371 0.2813 0.0113  0.0105  0.0387  374  TRP A CE3 
2736  C CZ2 . TRP A 376  ? 0.2416 0.2268 0.2669 0.0113  0.0108  0.0492  374  TRP A CZ2 
2737  C CZ3 . TRP A 376  ? 0.2710 0.2491 0.2936 0.0116  0.0098  0.0407  374  TRP A CZ3 
2738  C CH2 . TRP A 376  ? 0.2682 0.2501 0.2928 0.0116  0.0100  0.0460  374  TRP A CH2 
2739  N N   . ASP A 377  ? 0.2329 0.2084 0.2408 0.0121  0.0130  0.0306  375  ASP A N   
2740  C CA  A ASP A 377  ? 0.2301 0.2062 0.2347 0.0128  0.0131  0.0297  375  ASP A CA  
2741  C CA  B ASP A 377  ? 0.2292 0.2056 0.2340 0.0128  0.0131  0.0300  375  ASP A CA  
2742  C C   . ASP A 377  ? 0.2197 0.1976 0.2187 0.0137  0.0142  0.0285  375  ASP A C   
2743  O O   . ASP A 377  ? 0.2305 0.2110 0.2271 0.0145  0.0146  0.0293  375  ASP A O   
2744  C CB  A ASP A 377  ? 0.2698 0.2429 0.2743 0.0124  0.0122  0.0262  375  ASP A CB  
2745  C CB  B ASP A 377  ? 0.2616 0.2352 0.2673 0.0125  0.0120  0.0274  375  ASP A CB  
2746  C CG  A ASP A 377  ? 0.2999 0.2715 0.3101 0.0119  0.0107  0.0265  375  ASP A CG  
2747  C CG  B ASP A 377  ? 0.2595 0.2307 0.2639 0.0120  0.0118  0.0236  375  ASP A CG  
2748  O OD1 A ASP A 377  ? 0.3950 0.3678 0.4090 0.0120  0.0103  0.0299  375  ASP A OD1 
2749  O OD1 B ASP A 377  ? 0.3346 0.3059 0.3353 0.0121  0.0126  0.0224  375  ASP A OD1 
2750  O OD2 A ASP A 377  ? 0.3890 0.3585 0.4001 0.0115  0.0100  0.0233  375  ASP A OD2 
2751  O OD2 B ASP A 377  ? 0.3061 0.2755 0.3132 0.0115  0.0107  0.0217  375  ASP A OD2 
2752  N N   . ALA A 378  ? 0.2082 0.1848 0.2054 0.0135  0.0145  0.0263  376  ALA A N   
2753  C CA  . ALA A 378  ? 0.2038 0.1814 0.1965 0.0144  0.0153  0.0247  376  ALA A CA  
2754  C C   . ALA A 378  ? 0.2144 0.1963 0.2064 0.0153  0.0163  0.0269  376  ALA A C   
2755  O O   . ALA A 378  ? 0.2140 0.1982 0.2027 0.0165  0.0168  0.0260  376  ALA A O   
2756  C CB  . ALA A 378  ? 0.2224 0.1976 0.2143 0.0138  0.0151  0.0223  376  ALA A CB  
2757  N N   . GLU A 379  ? 0.2124 0.1958 0.2077 0.0150  0.0166  0.0298  377  GLU A N   
2758  C CA  . GLU A 379  ? 0.1972 0.1856 0.1920 0.0159  0.0176  0.0322  377  GLU A CA  
2759  C C   . GLU A 379  ? 0.2068 0.1990 0.2010 0.0165  0.0178  0.0345  377  GLU A C   
2760  O O   . GLU A 379  ? 0.2222 0.2191 0.2137 0.0177  0.0187  0.0349  377  GLU A O   
2761  C CB  . GLU A 379  ? 0.2034 0.1928 0.2024 0.0151  0.0178  0.0352  377  GLU A CB  
2762  C CG  . GLU A 379  ? 0.2192 0.2056 0.2191 0.0145  0.0176  0.0333  377  GLU A CG  
2763  C CD  . GLU A 379  ? 0.2256 0.2132 0.2221 0.0156  0.0184  0.0311  377  GLU A CD  
2764  O OE1 . GLU A 379  ? 0.2415 0.2327 0.2351 0.0169  0.0191  0.0307  377  GLU A OE1 
2765  O OE2 . GLU A 379  ? 0.2262 0.2113 0.2233 0.0151  0.0181  0.0295  377  GLU A OE2 
2766  N N   . ILE A 380  ? 0.2036 0.1941 0.2004 0.0157  0.0169  0.0359  378  ILE A N   
2767  C CA  . ILE A 380  ? 0.2224 0.2164 0.2187 0.0162  0.0168  0.0382  378  ILE A CA  
2768  C C   . ILE A 380  ? 0.2227 0.2174 0.2139 0.0174  0.0170  0.0350  378  ILE A C   
2769  O O   . ILE A 380  ? 0.2138 0.2135 0.2024 0.0185  0.0177  0.0358  378  ILE A O   
2770  C CB  . ILE A 380  ? 0.2247 0.2162 0.2255 0.0153  0.0155  0.0401  378  ILE A CB  
2771  C CG1 . ILE A 380  ? 0.2186 0.2093 0.2253 0.0141  0.0149  0.0432  378  ILE A CG1 
2772  C CG2 . ILE A 380  ? 0.2352 0.2303 0.2354 0.0158  0.0153  0.0426  378  ILE A CG2 
2773  C CD1 . ILE A 380  ? 0.2341 0.2305 0.2421 0.0142  0.0158  0.0477  378  ILE A CD1 
2774  N N   . LYS A 381  ? 0.1992 0.1891 0.1890 0.0171  0.0164  0.0313  379  LYS A N   
2775  C CA  . LYS A 381  ? 0.2068 0.1969 0.1924 0.0180  0.0164  0.0282  379  LYS A CA  
2776  C C   . LYS A 381  ? 0.2194 0.2127 0.2019 0.0193  0.0172  0.0267  379  LYS A C   
2777  O O   . LYS A 381  ? 0.2102 0.2070 0.1898 0.0205  0.0174  0.0259  379  LYS A O   
2778  C CB  . LYS A 381  ? 0.2191 0.2040 0.2043 0.0172  0.0156  0.0249  379  LYS A CB  
2779  C CG  . LYS A 381  ? 0.2303 0.2150 0.2117 0.0180  0.0153  0.0218  379  LYS A CG  
2780  C CD  . LYS A 381  ? 0.2201 0.2003 0.2015 0.0170  0.0145  0.0192  379  LYS A CD  
2781  C CE  . LYS A 381  ? 0.2432 0.2234 0.2216 0.0175  0.0141  0.0166  379  LYS A CE  
2782  N NZ  . LYS A 381  ? 0.2254 0.2020 0.2039 0.0164  0.0133  0.0145  379  LYS A NZ  
2783  N N   . ARG A 382  ? 0.2117 0.2039 0.1948 0.0191  0.0176  0.0260  380  ARG A N   
2784  C CA  . ARG A 382  ? 0.2167 0.2115 0.1974 0.0204  0.0182  0.0239  380  ARG A CA  
2785  C C   . ARG A 382  ? 0.2106 0.2125 0.1904 0.0217  0.0191  0.0259  380  ARG A C   
2786  O O   . ARG A 382  ? 0.2263 0.2316 0.2033 0.0232  0.0193  0.0237  380  ARG A O   
2787  C CB  . ARG A 382  ? 0.2353 0.2280 0.2176 0.0200  0.0184  0.0233  380  ARG A CB  
2788  C CG  . ARG A 382  ? 0.2765 0.2711 0.2569 0.0213  0.0187  0.0207  380  ARG A CG  
2789  C CD  . ARG A 382  ? 0.4768 0.4671 0.4557 0.0213  0.0176  0.0169  380  ARG A CD  
2790  N NE  . ARG A 382  ? 0.5100 0.5029 0.4863 0.0228  0.0173  0.0147  380  ARG A NE  
2791  C CZ  . ARG A 382  ? 0.5632 0.5533 0.5384 0.0228  0.0163  0.0119  380  ARG A CZ  
2792  N NH1 . ARG A 382  ? 0.6001 0.5849 0.5760 0.0213  0.0154  0.0112  380  ARG A NH1 
2793  N NH2 . ARG A 382  ? 0.4639 0.4568 0.4371 0.0243  0.0160  0.0097  380  ARG A NH2 
2794  N N   . ALA A 383  ? 0.2173 0.2220 0.1997 0.0211  0.0197  0.0302  381  ALA A N   
2795  C CA  . ALA A 383  ? 0.2171 0.2297 0.1989 0.0222  0.0207  0.0328  381  ALA A CA  
2796  C C   . ALA A 383  ? 0.2196 0.2354 0.1989 0.0230  0.0204  0.0328  381  ALA A C   
2797  O O   . ALA A 383  ? 0.2363 0.2586 0.2129 0.0245  0.0211  0.0321  381  ALA A O   
2798  C CB  . ALA A 383  ? 0.2370 0.2517 0.2228 0.0210  0.0210  0.0380  381  ALA A CB  
2799  N N   . GLN A 384  ? 0.2124 0.2241 0.1925 0.0220  0.0194  0.0332  382  GLN A N   
2800  C CA  . GLN A 384  ? 0.2196 0.2342 0.1975 0.0228  0.0190  0.0332  382  GLN A CA  
2801  C C   . GLN A 384  ? 0.2243 0.2387 0.1983 0.0241  0.0188  0.0280  382  GLN A C   
2802  O O   . GLN A 384  ? 0.2386 0.2587 0.2098 0.0256  0.0191  0.0273  382  GLN A O   
2803  C CB  . GLN A 384  ? 0.2032 0.2132 0.1835 0.0215  0.0179  0.0345  382  GLN A CB  
2804  C CG  . GLN A 384  ? 0.2184 0.2293 0.2031 0.0203  0.0177  0.0398  382  GLN A CG  
2805  C CD  . GLN A 384  ? 0.2278 0.2348 0.2152 0.0194  0.0164  0.0407  382  GLN A CD  
2806  O OE1 . GLN A 384  ? 0.2546 0.2571 0.2407 0.0193  0.0158  0.0372  382  GLN A OE1 
2807  N NE2 . GLN A 384  ? 0.2504 0.2594 0.2419 0.0186  0.0159  0.0456  382  GLN A NE2 
2808  N N   . LEU A 385  ? 0.2204 0.2285 0.1942 0.0237  0.0182  0.0244  383  LEU A N   
2809  C CA  . LEU A 385  ? 0.2267 0.2341 0.1977 0.0249  0.0177  0.0197  383  LEU A CA  
2810  C C   . LEU A 385  ? 0.2388 0.2521 0.2082 0.0267  0.0184  0.0181  383  LEU A C   
2811  O O   . LEU A 385  ? 0.2607 0.2771 0.2277 0.0282  0.0181  0.0151  383  LEU A O   
2812  C CB  . LEU A 385  ? 0.2155 0.2159 0.1874 0.0239  0.0170  0.0170  383  LEU A CB  
2813  C CG  . LEU A 385  ? 0.2723 0.2672 0.2451 0.0223  0.0161  0.0170  383  LEU A CG  
2814  C CD1 . LEU A 385  ? 0.2947 0.2841 0.2683 0.0214  0.0155  0.0148  383  LEU A CD1 
2815  C CD2 . LEU A 385  ? 0.3022 0.2978 0.2731 0.0229  0.0154  0.0154  383  LEU A CD2 
2816  N N   . ASP A 386  ? 0.2273 0.2424 0.1982 0.0267  0.0194  0.0196  384  ASP A N   
2817  C CA  . ASP A 386  ? 0.2443 0.2648 0.2141 0.0285  0.0200  0.0176  384  ASP A CA  
2818  C C   . ASP A 386  ? 0.2488 0.2787 0.2173 0.0297  0.0211  0.0201  384  ASP A C   
2819  O O   . ASP A 386  ? 0.2511 0.2871 0.2186 0.0314  0.0217  0.0183  384  ASP A O   
2820  C CB  . ASP A 386  ? 0.2524 0.2707 0.2244 0.0280  0.0205  0.0179  384  ASP A CB  
2821  C CG  . ASP A 386  ? 0.3276 0.3380 0.3004 0.0273  0.0193  0.0147  384  ASP A CG  
2822  O OD1 . ASP A 386  ? 0.3467 0.3538 0.3183 0.0273  0.0182  0.0120  384  ASP A OD1 
2823  O OD2 . ASP A 386  ? 0.3469 0.3546 0.3217 0.0266  0.0195  0.0152  384  ASP A OD2 
2824  N N   . GLY A 387  ? 0.2417 0.2734 0.2105 0.0288  0.0211  0.0241  385  GLY A N   
2825  C CA  . GLY A 387  ? 0.2460 0.2874 0.2136 0.0297  0.0220  0.0271  385  GLY A CA  
2826  C C   . GLY A 387  ? 0.2502 0.2974 0.2193 0.0299  0.0234  0.0300  385  GLY A C   
2827  O O   . GLY A 387  ? 0.2525 0.3089 0.2198 0.0315  0.0243  0.0300  385  GLY A O   
2828  N N   . LEU A 388  ? 0.2467 0.2893 0.2192 0.0283  0.0235  0.0326  386  LEU A N   
2829  C CA  . LEU A 388  ? 0.2547 0.3025 0.2288 0.0284  0.0248  0.0350  386  LEU A CA  
2830  C C   . LEU A 388  ? 0.2555 0.3089 0.2319 0.0272  0.0253  0.0419  386  LEU A C   
2831  O O   . LEU A 388  ? 0.2801 0.3322 0.2573 0.0262  0.0246  0.0448  386  LEU A O   
2832  C CB  . LEU A 388  ? 0.2406 0.2813 0.2172 0.0274  0.0246  0.0338  386  LEU A CB  
2833  C CG  . LEU A 388  ? 0.2661 0.3021 0.2410 0.0285  0.0240  0.0275  386  LEU A CG  
2834  C CD1 . LEU A 388  ? 0.2658 0.2950 0.2431 0.0275  0.0237  0.0268  386  LEU A CD1 
2835  C CD2 . LEU A 388  ? 0.2816 0.3249 0.2539 0.0310  0.0246  0.0240  386  LEU A CD2 
2836  N N   . ALA A 389  ? 0.2799 0.3400 0.2576 0.0274  0.0266  0.0446  387  ALA A N   
2837  C CA  . ALA A 389  ? 0.3032 0.3709 0.2828 0.0266  0.0272  0.0514  387  ALA A CA  
2838  C C   . ALA A 389  ? 0.2883 0.3499 0.2729 0.0241  0.0261  0.0564  387  ALA A C   
2839  O O   . ALA A 389  ? 0.2932 0.3582 0.2796 0.0231  0.0258  0.0615  387  ALA A O   
2840  C CB  . ALA A 389  ? 0.3300 0.4066 0.3102 0.0273  0.0288  0.0532  387  ALA A CB  
2841  N N   . ASP A 390  ? 0.2499 0.3028 0.2372 0.0230  0.0256  0.0548  388  ASP A N   
2842  C CA  . ASP A 390  ? 0.2594 0.3065 0.2520 0.0208  0.0245  0.0589  388  ASP A CA  
2843  C C   . ASP A 390  ? 0.2428 0.2799 0.2362 0.0202  0.0237  0.0546  388  ASP A C   
2844  O O   . ASP A 390  ? 0.2327 0.2677 0.2227 0.0214  0.0240  0.0493  388  ASP A O   
2845  C CB  . ASP A 390  ? 0.2553 0.3083 0.2523 0.0197  0.0251  0.0650  388  ASP A CB  
2846  C CG  . ASP A 390  ? 0.2789 0.3292 0.2818 0.0176  0.0237  0.0708  388  ASP A CG  
2847  O OD1 . ASP A 390  ? 0.2871 0.3286 0.2924 0.0166  0.0223  0.0692  388  ASP A OD1 
2848  O OD2 . ASP A 390  ? 0.3293 0.3869 0.3351 0.0168  0.0240  0.0770  388  ASP A OD2 
2849  N N   . PHE A 391  ? 0.2303 0.2617 0.2284 0.0185  0.0226  0.0568  389  PHE A N   
2850  C CA  . PHE A 391  ? 0.2265 0.2492 0.2258 0.0178  0.0218  0.0531  389  PHE A CA  
2851  C C   . PHE A 391  ? 0.2301 0.2531 0.2318 0.0174  0.0224  0.0538  389  PHE A C   
2852  O O   . PHE A 391  ? 0.2353 0.2640 0.2397 0.0170  0.0231  0.0583  389  PHE A O   
2853  C CB  . PHE A 391  ? 0.2354 0.2522 0.2390 0.0162  0.0202  0.0547  389  PHE A CB  
2854  C CG  . PHE A 391  ? 0.2107 0.2271 0.2123 0.0166  0.0195  0.0543  389  PHE A CG  
2855  C CD1 . PHE A 391  ? 0.2270 0.2396 0.2244 0.0174  0.0193  0.0491  389  PHE A CD1 
2856  C CD2 . PHE A 391  ? 0.2356 0.2561 0.2396 0.0162  0.0191  0.0592  389  PHE A CD2 
2857  C CE1 . PHE A 391  ? 0.2564 0.2689 0.2519 0.0178  0.0187  0.0485  389  PHE A CE1 
2858  C CE2 . PHE A 391  ? 0.2535 0.2740 0.2556 0.0166  0.0184  0.0587  389  PHE A CE2 
2859  C CZ  . PHE A 391  ? 0.2438 0.2603 0.2416 0.0175  0.0183  0.0532  389  PHE A CZ  
2860  N N   . PRO A 392  ? 0.2180 0.2354 0.2188 0.0174  0.0222  0.0495  390  PRO A N   
2861  C CA  . PRO A 392  ? 0.2192 0.2362 0.2227 0.0169  0.0226  0.0500  390  PRO A CA  
2862  C C   . PRO A 392  ? 0.2184 0.2301 0.2274 0.0150  0.0213  0.0519  390  PRO A C   
2863  O O   . PRO A 392  ? 0.2331 0.2434 0.2446 0.0144  0.0213  0.0520  390  PRO A O   
2864  C CB  . PRO A 392  ? 0.2105 0.2239 0.2103 0.0179  0.0227  0.0444  390  PRO A CB  
2865  C CG  . PRO A 392  ? 0.1885 0.1965 0.1861 0.0178  0.0217  0.0415  390  PRO A CG  
2866  C CD  . PRO A 392  ? 0.2065 0.2183 0.2038 0.0180  0.0216  0.0442  390  PRO A CD  
2867  N N   . VAL A 393  ? 0.2088 0.2175 0.2198 0.0142  0.0201  0.0531  391  VAL A N   
2868  C CA  . VAL A 393  ? 0.2137 0.2176 0.2305 0.0126  0.0185  0.0545  391  VAL A CA  
2869  C C   . VAL A 393  ? 0.2229 0.2293 0.2438 0.0119  0.0178  0.0595  391  VAL A C   
2870  O O   . VAL A 393  ? 0.2338 0.2446 0.2521 0.0126  0.0183  0.0611  391  VAL A O   
2871  C CB  . VAL A 393  ? 0.1981 0.1948 0.2140 0.0124  0.0174  0.0498  391  VAL A CB  
2872  C CG1 . VAL A 393  ? 0.2200 0.2142 0.2326 0.0128  0.0179  0.0454  391  VAL A CG1 
2873  C CG2 . VAL A 393  ? 0.2269 0.2232 0.2393 0.0131  0.0172  0.0483  391  VAL A CG2 
2874  N N   . PHE A 394  ? 0.2131 0.2170 0.2409 0.0104  0.0163  0.0621  392  PHE A N   
2875  C CA  . PHE A 394  ? 0.2089 0.2139 0.2419 0.0095  0.0150  0.0669  392  PHE A CA  
2876  C C   . PHE A 394  ? 0.2241 0.2252 0.2558 0.0099  0.0140  0.0642  392  PHE A C   
2877  O O   . PHE A 394  ? 0.2345 0.2312 0.2625 0.0104  0.0139  0.0588  392  PHE A O   
2878  C CB  . PHE A 394  ? 0.2382 0.2407 0.2797 0.0079  0.0134  0.0696  392  PHE A CB  
2879  C CG  . PHE A 394  ? 0.2060 0.2127 0.2491 0.0074  0.0144  0.0726  392  PHE A CG  
2880  C CD1 . PHE A 394  ? 0.2436 0.2583 0.2868 0.0074  0.0155  0.0781  392  PHE A CD1 
2881  C CD2 . PHE A 394  ? 0.2292 0.2328 0.2735 0.0071  0.0144  0.0700  392  PHE A CD2 
2882  C CE1 . PHE A 394  ? 0.2264 0.2459 0.2710 0.0071  0.0167  0.0808  392  PHE A CE1 
2883  C CE2 . PHE A 394  ? 0.2375 0.2455 0.2834 0.0067  0.0154  0.0728  392  PHE A CE2 
2884  C CZ  . PHE A 394  ? 0.2287 0.2446 0.2748 0.0067  0.0165  0.0782  392  PHE A CZ  
2885  N N   . THR A 395  ? 0.2209 0.2243 0.2554 0.0096  0.0131  0.0683  393  THR A N   
2886  C CA  . THR A 395  ? 0.2435 0.2437 0.2774 0.0099  0.0120  0.0663  393  THR A CA  
2887  C C   . THR A 395  ? 0.2388 0.2351 0.2810 0.0088  0.0095  0.0683  393  THR A C   
2888  O O   . THR A 395  ? 0.2530 0.2461 0.2956 0.0091  0.0083  0.0661  393  THR A O   
2889  C CB  . THR A 395  ? 0.2369 0.2427 0.2665 0.0108  0.0128  0.0686  393  THR A CB  
2890  O OG1 . THR A 395  ? 0.2466 0.2583 0.2805 0.0100  0.0126  0.0756  393  THR A OG1 
2891  C CG2 . THR A 395  ? 0.2578 0.2670 0.2792 0.0122  0.0150  0.0653  393  THR A CG2 
2892  N N   . ARG A 396  ? 0.2466 0.2434 0.2961 0.0075  0.0085  0.0723  394  ARG A N   
2893  C CA  . ARG A 396  ? 0.2558 0.2481 0.3143 0.0065  0.0058  0.0733  394  ARG A CA  
2894  C C   . ARG A 396  ? 0.2434 0.2313 0.3048 0.0060  0.0052  0.0699  394  ARG A C   
2895  O O   . ARG A 396  ? 0.2431 0.2332 0.3040 0.0056  0.0063  0.0710  394  ARG A O   
2896  C CB  . ARG A 396  ? 0.2620 0.2581 0.3280 0.0053  0.0045  0.0811  394  ARG A CB  
2897  C CG  . ARG A 396  ? 0.2707 0.2716 0.3344 0.0057  0.0048  0.0850  394  ARG A CG  
2898  C CD  . ARG A 396  ? 0.3365 0.3405 0.4092 0.0042  0.0029  0.0930  394  ARG A CD  
2899  N NE  . ARG A 396  ? 0.3698 0.3804 0.4396 0.0045  0.0036  0.0977  394  ARG A NE  
2900  C CZ  . ARG A 396  ? 0.4464 0.4572 0.5213 0.0041  0.0016  0.1015  394  ARG A CZ  
2901  N NH1 . ARG A 396  ? 0.4637 0.4684 0.5475 0.0033  -0.0014 0.1014  394  ARG A NH1 
2902  N NH2 . ARG A 396  ? 0.3670 0.3845 0.4380 0.0045  0.0024  0.1054  394  ARG A NH2 
2903  N N   . LYS A 397  ? 0.2617 0.2439 0.3262 0.0060  0.0034  0.0654  395  LYS A N   
2904  C CA  . LYS A 397  ? 0.2582 0.2364 0.3250 0.0057  0.0027  0.0614  395  LYS A CA  
2905  C C   . LYS A 397  ? 0.2483 0.2275 0.3231 0.0043  0.0016  0.0658  395  LYS A C   
2906  O O   . LYS A 397  ? 0.2426 0.2213 0.3171 0.0040  0.0022  0.0642  395  LYS A O   
2907  C CB  . LYS A 397  ? 0.2838 0.2570 0.3536 0.0060  0.0007  0.0563  395  LYS A CB  
2908  C CG  . LYS A 397  ? 0.2945 0.2644 0.3639 0.0060  0.0005  0.0507  395  LYS A CG  
2909  C CD  . LYS A 397  ? 0.2690 0.2367 0.3482 0.0050  -0.0019 0.0514  395  LYS A CD  
2910  C CE  . LYS A 397  ? 0.2703 0.2356 0.3486 0.0051  -0.0021 0.0457  395  LYS A CE  
2911  N NZ  . LYS A 397  ? 0.2948 0.2578 0.3831 0.0043  -0.0048 0.0455  395  LYS A NZ  
2912  N N   . ILE A 398  ? 0.2463 0.2269 0.3284 0.0035  0.0000  0.0715  396  ILE A N   
2913  C CA  . ILE A 398  ? 0.2559 0.2373 0.3467 0.0020  -0.0014 0.0760  396  ILE A CA  
2914  C C   . ILE A 398  ? 0.2167 0.2035 0.3035 0.0017  0.0010  0.0794  396  ILE A C   
2915  O O   . ILE A 398  ? 0.2582 0.2451 0.3498 0.0007  0.0005  0.0811  396  ILE A O   
2916  C CB  . ILE A 398  ? 0.2915 0.2734 0.3914 0.0011  -0.0039 0.0819  396  ILE A CB  
2917  C CG1 . ILE A 398  ? 0.3192 0.3000 0.4302 -0.0005 -0.0063 0.0855  396  ILE A CG1 
2918  C CG2 . ILE A 398  ? 0.2803 0.2689 0.3764 0.0011  -0.0023 0.0881  396  ILE A CG2 
2919  C CD1 . ILE A 398  ? 0.3366 0.3160 0.4586 -0.0014 -0.0097 0.0899  396  ILE A CD1 
2920  N N   . HIS A 399  ? 0.2538 0.2453 0.3320 0.0027  0.0036  0.0802  397  HIS A N   
2921  C CA  . HIS A 399  ? 0.2404 0.2375 0.3144 0.0027  0.0060  0.0826  397  HIS A CA  
2922  C C   . HIS A 399  ? 0.2279 0.2222 0.2985 0.0031  0.0069  0.0772  397  HIS A C   
2923  O O   . HIS A 399  ? 0.2372 0.2336 0.3099 0.0024  0.0075  0.0792  397  HIS A O   
2924  C CB  . HIS A 399  ? 0.2444 0.2471 0.3100 0.0039  0.0083  0.0835  397  HIS A CB  
2925  C CG  . HIS A 399  ? 0.2158 0.2229 0.2844 0.0034  0.0076  0.0898  397  HIS A CG  
2926  N ND1 . HIS A 399  ? 0.2598 0.2718 0.3218 0.0045  0.0091  0.0906  397  HIS A ND1 
2927  C CD2 . HIS A 399  ? 0.3050 0.3126 0.3830 0.0019  0.0054  0.0956  397  HIS A CD2 
2928  C CE1 . HIS A 399  ? 0.2714 0.2870 0.3382 0.0037  0.0079  0.0969  397  HIS A CE1 
2929  N NE2 . HIS A 399  ? 0.2926 0.3055 0.3693 0.0021  0.0056  0.1002  397  HIS A NE2 
2930  N N   . THR A 400  ? 0.2348 0.2244 0.3005 0.0041  0.0070  0.0707  398  THR A N   
2931  C CA  . THR A 400  ? 0.2084 0.1951 0.2714 0.0043  0.0075  0.0656  398  THR A CA  
2932  C C   . THR A 400  ? 0.2254 0.2092 0.2969 0.0031  0.0055  0.0658  398  THR A C   
2933  O O   . THR A 400  ? 0.2161 0.2003 0.2875 0.0028  0.0061  0.0651  398  THR A O   
2934  C CB  . THR A 400  ? 0.2134 0.1961 0.2709 0.0053  0.0076  0.0593  398  THR A CB  
2935  O OG1 . THR A 400  ? 0.2235 0.2094 0.2730 0.0065  0.0096  0.0590  398  THR A OG1 
2936  C CG2 . THR A 400  ? 0.1961 0.1757 0.2516 0.0054  0.0077  0.0542  398  THR A CG2 
2937  N N   . ASP A 401  ? 0.2135 0.1943 0.2929 0.0024  0.0029  0.0668  399  ASP A N   
2938  C CA  . ASP A 401  ? 0.2356 0.2135 0.3239 0.0012  0.0006  0.0666  399  ASP A CA  
2939  C C   . ASP A 401  ? 0.2231 0.2050 0.3160 0.0000  0.0008  0.0727  399  ASP A C   
2940  O O   . ASP A 401  ? 0.2331 0.2140 0.3289 -0.0006 0.0004  0.0718  399  ASP A O   
2941  C CB  . ASP A 401  ? 0.2440 0.2182 0.3407 0.0008  -0.0026 0.0665  399  ASP A CB  
2942  C CG  . ASP A 401  ? 0.2793 0.2494 0.3727 0.0020  -0.0031 0.0596  399  ASP A CG  
2943  O OD1 . ASP A 401  ? 0.2994 0.2686 0.3859 0.0027  -0.0017 0.0545  399  ASP A OD1 
2944  O OD2 . ASP A 401  ? 0.3010 0.2692 0.3987 0.0022  -0.0050 0.0594  399  ASP A OD2 
2945  N N   . VAL A 402  ? 0.2292 0.2161 0.3230 -0.0004 0.0015  0.0792  400  VAL A N   
2946  C CA  . VAL A 402  ? 0.2482 0.2400 0.3462 -0.0016 0.0019  0.0855  400  VAL A CA  
2947  C C   . VAL A 402  ? 0.2153 0.2104 0.3059 -0.0009 0.0047  0.0839  400  VAL A C   
2948  O O   . VAL A 402  ? 0.2260 0.2223 0.3203 -0.0018 0.0047  0.0855  400  VAL A O   
2949  C CB  . VAL A 402  ? 0.2284 0.2260 0.3281 -0.0021 0.0022  0.0929  400  VAL A CB  
2950  C CG1 . VAL A 402  ? 0.2209 0.2251 0.3241 -0.0034 0.0031  0.0997  400  VAL A CG1 
2951  C CG2 . VAL A 402  ? 0.2717 0.2659 0.3802 -0.0029 -0.0010 0.0950  400  VAL A CG2 
2952  N N   . SER A 403  ? 0.2316 0.2282 0.3124 0.0006  0.0070  0.0807  401  SER A N   
2953  C CA  . SER A 403  ? 0.2214 0.2204 0.2952 0.0015  0.0095  0.0783  401  SER A CA  
2954  C C   . SER A 403  ? 0.2409 0.2353 0.3165 0.0012  0.0086  0.0739  401  SER A C   
2955  O O   . SER A 403  ? 0.2176 0.2142 0.2937 0.0009  0.0094  0.0748  401  SER A O   
2956  C CB  . SER A 403  ? 0.2362 0.2358 0.3002 0.0033  0.0113  0.0744  401  SER A CB  
2957  O OG  . SER A 403  ? 0.2361 0.2374 0.2942 0.0042  0.0133  0.0716  401  SER A OG  
2958  N N   . TYR A 404  ? 0.2123 0.2005 0.2887 0.0014  0.0069  0.0690  402  TYR A N   
2959  C CA  . TYR A 404  ? 0.2284 0.2126 0.3062 0.0011  0.0060  0.0645  402  TYR A CA  
2960  C C   . TYR A 404  ? 0.2002 0.1848 0.2870 -0.0004 0.0044  0.0678  402  TYR A C   
2961  O O   . TYR A 404  ? 0.2185 0.2037 0.3050 -0.0006 0.0050  0.0668  402  TYR A O   
2962  C CB  . TYR A 404  ? 0.2108 0.1895 0.2890 0.0015  0.0042  0.0592  402  TYR A CB  
2963  C CG  . TYR A 404  ? 0.2254 0.2008 0.3027 0.0016  0.0036  0.0536  402  TYR A CG  
2964  C CD1 . TYR A 404  ? 0.2182 0.1918 0.3031 0.0006  0.0015  0.0532  402  TYR A CD1 
2965  C CD2 . TYR A 404  ? 0.2039 0.1783 0.2729 0.0026  0.0049  0.0488  402  TYR A CD2 
2966  C CE1 . TYR A 404  ? 0.2295 0.2008 0.3135 0.0007  0.0009  0.0480  402  TYR A CE1 
2967  C CE2 . TYR A 404  ? 0.2080 0.1800 0.2762 0.0026  0.0043  0.0440  402  TYR A CE2 
2968  C CZ  . TYR A 404  ? 0.2079 0.1786 0.2834 0.0016  0.0023  0.0436  402  TYR A CZ  
2969  O OH  . TYR A 404  ? 0.2423 0.2113 0.3168 0.0016  0.0016  0.0390  402  TYR A OH  
2970  N N   . ILE A 405  ? 0.2346 0.2190 0.3299 -0.0015 0.0024  0.0720  403  ILE A N   
2971  C CA  . ILE A 405  ? 0.2275 0.2118 0.3326 -0.0030 0.0005  0.0752  403  ILE A CA  
2972  C C   . ILE A 405  ? 0.2127 0.2033 0.3174 -0.0036 0.0024  0.0806  403  ILE A C   
2973  O O   . ILE A 405  ? 0.2385 0.2294 0.3469 -0.0044 0.0020  0.0810  403  ILE A O   
2974  C CB  . ILE A 405  ? 0.2551 0.2375 0.3700 -0.0041 -0.0025 0.0784  403  ILE A CB  
2975  C CG1 . ILE A 405  ? 0.2886 0.2649 0.4042 -0.0033 -0.0045 0.0719  403  ILE A CG1 
2976  C CG2 . ILE A 405  ? 0.2763 0.2588 0.4020 -0.0058 -0.0046 0.0823  403  ILE A CG2 
2977  C CD1 . ILE A 405  ? 0.3196 0.2940 0.4427 -0.0038 -0.0070 0.0742  403  ILE A CD1 
2978  N N   . ALA A 406  ? 0.2247 0.2207 0.3245 -0.0031 0.0046  0.0845  404  ALA A N   
2979  C CA  . ALA A 406  ? 0.2278 0.2310 0.3263 -0.0034 0.0067  0.0891  404  ALA A CA  
2980  C C   . ALA A 406  ? 0.2190 0.2222 0.3112 -0.0024 0.0085  0.0846  404  ALA A C   
2981  O O   . ALA A 406  ? 0.2497 0.2560 0.3444 -0.0030 0.0091  0.0868  404  ALA A O   
2982  C CB  . ALA A 406  ? 0.2219 0.2313 0.3150 -0.0026 0.0088  0.0927  404  ALA A CB  
2983  N N   . CYS A 407  ? 0.2102 0.2102 0.2944 -0.0008 0.0094  0.0785  405  CYS A N   
2984  C CA  . CYS A 407  ? 0.2240 0.2238 0.3025 0.0001  0.0109  0.0742  405  CYS A CA  
2985  C C   . CYS A 407  ? 0.2229 0.2185 0.3064 -0.0008 0.0091  0.0716  405  CYS A C   
2986  O O   . CYS A 407  ? 0.2263 0.2233 0.3087 -0.0007 0.0100  0.0708  405  CYS A O   
2987  C CB  . CYS A 407  ? 0.2505 0.2481 0.3201 0.0018  0.0120  0.0690  405  CYS A CB  
2988  S SG  . CYS A 407  ? 0.2872 0.2915 0.3502 0.0031  0.0146  0.0717  405  CYS A SG  
2989  N N   . ALA A 408  ? 0.2179 0.2084 0.3073 -0.0016 0.0064  0.0702  406  ALA A N   
2990  C CA  . ALA A 408  ? 0.2458 0.2328 0.3409 -0.0025 0.0044  0.0678  406  ALA A CA  
2991  C C   . ALA A 408  ? 0.2081 0.1985 0.3107 -0.0039 0.0040  0.0730  406  ALA A C   
2992  O O   . ALA A 408  ? 0.2348 0.2246 0.3393 -0.0043 0.0035  0.0715  406  ALA A O   
2993  C CB  . ALA A 408  ? 0.2524 0.2341 0.3530 -0.0029 0.0015  0.0650  406  ALA A CB  
2994  N N   . ALA A 409  ? 0.2275 0.2217 0.3347 -0.0048 0.0039  0.0795  407  ALA A N   
2995  C CA  . ALA A 409  ? 0.2188 0.2172 0.3329 -0.0063 0.0037  0.0853  407  ALA A CA  
2996  C C   . ALA A 409  ? 0.2308 0.2343 0.3390 -0.0055 0.0065  0.0856  407  ALA A C   
2997  O O   . ALA A 409  ? 0.2506 0.2554 0.3630 -0.0064 0.0062  0.0868  407  ALA A O   
2998  C CB  . ALA A 409  ? 0.2691 0.2715 0.3884 -0.0073 0.0033  0.0927  407  ALA A CB  
2999  N N   . LYS A 410  ? 0.2208 0.2272 0.3197 -0.0039 0.0092  0.0843  408  LYS A N   
3000  C CA  . LYS A 410  ? 0.2235 0.2346 0.3169 -0.0029 0.0117  0.0838  408  LYS A CA  
3001  C C   . LYS A 410  ? 0.2213 0.2281 0.3130 -0.0025 0.0112  0.0781  408  LYS A C   
3002  O O   . LYS A 410  ? 0.2215 0.2308 0.3147 -0.0027 0.0118  0.0789  408  LYS A O   
3003  C CB  . LYS A 410  ? 0.2337 0.2480 0.3178 -0.0010 0.0142  0.0825  408  LYS A CB  
3004  C CG  . LYS A 410  ? 0.2393 0.2589 0.3179 0.0003  0.0167  0.0815  408  LYS A CG  
3005  C CD  . LYS A 410  ? 0.2715 0.2938 0.3416 0.0023  0.0188  0.0795  408  LYS A CD  
3006  C CE  . LYS A 410  ? 0.2840 0.3120 0.3547 0.0021  0.0194  0.0848  408  LYS A CE  
3007  N NZ  . LYS A 410  ? 0.3025 0.3399 0.3749 0.0019  0.0212  0.0897  408  LYS A NZ  
3008  N N   . LEU A 411  ? 0.2052 0.2058 0.2939 -0.0019 0.0101  0.0725  409  LEU A N   
3009  C CA  . LEU A 411  ? 0.2006 0.1974 0.2874 -0.0016 0.0096  0.0673  409  LEU A CA  
3010  C C   . LEU A 411  ? 0.1928 0.1879 0.2882 -0.0031 0.0073  0.0681  409  LEU A C   
3011  O O   . LEU A 411  ? 0.2062 0.2017 0.3016 -0.0031 0.0075  0.0666  409  LEU A O   
3012  C CB  . LEU A 411  ? 0.2050 0.1963 0.2873 -0.0008 0.0087  0.0617  409  LEU A CB  
3013  C CG  . LEU A 411  ? 0.2118 0.2042 0.2848 0.0009  0.0109  0.0596  409  LEU A CG  
3014  C CD1 . LEU A 411  ? 0.2138 0.2016 0.2835 0.0013  0.0100  0.0555  409  LEU A CD1 
3015  C CD2 . LEU A 411  ? 0.2119 0.2054 0.2800 0.0018  0.0122  0.0571  409  LEU A CD2 
3016  N N   . LEU A 412  ? 0.2093 0.2028 0.3128 -0.0045 0.0051  0.0706  410  LEU A N   
3017  C CA  . LEU A 412  ? 0.2206 0.2122 0.3331 -0.0059 0.0026  0.0708  410  LEU A CA  
3018  C C   . LEU A 412  ? 0.2402 0.2369 0.3570 -0.0069 0.0034  0.0761  410  LEU A C   
3019  O O   . LEU A 412  ? 0.2753 0.2710 0.3981 -0.0079 0.0018  0.0757  410  LEU A O   
3020  C CB  . LEU A 412  ? 0.2417 0.2297 0.3625 -0.0070 -0.0004 0.0718  410  LEU A CB  
3021  C CG  . LEU A 412  ? 0.2263 0.2088 0.3447 -0.0062 -0.0018 0.0652  410  LEU A CG  
3022  C CD1 . LEU A 412  ? 0.2744 0.2541 0.4010 -0.0070 -0.0046 0.0665  410  LEU A CD1 
3023  C CD2 . LEU A 412  ? 0.2662 0.2459 0.3847 -0.0061 -0.0031 0.0597  410  LEU A CD2 
3024  N N   . ALA A 413  ? 0.2195 0.2222 0.3334 -0.0066 0.0058  0.0807  411  ALA A N   
3025  C CA  . ALA A 413  ? 0.2410 0.2499 0.3580 -0.0073 0.0070  0.0854  411  ALA A CA  
3026  C C   . ALA A 413  ? 0.2462 0.2568 0.3569 -0.0060 0.0089  0.0821  411  ALA A C   
3027  O O   . ALA A 413  ? 0.2760 0.2915 0.3889 -0.0064 0.0100  0.0851  411  ALA A O   
3028  C CB  . ALA A 413  ? 0.2571 0.2730 0.3736 -0.0074 0.0089  0.0918  411  ALA A CB  
3029  N N   . ALA A 414  ? 0.2163 0.2228 0.3195 -0.0045 0.0093  0.0760  412  ALA A N   
3030  C CA  . ALA A 414  ? 0.2481 0.2560 0.3448 -0.0031 0.0111  0.0728  412  ALA A CA  
3031  C C   . ALA A 414  ? 0.2217 0.2238 0.3168 -0.0029 0.0096  0.0669  412  ALA A C   
3032  O O   . ALA A 414  ? 0.2219 0.2237 0.3104 -0.0015 0.0107  0.0634  412  ALA A O   
3033  C CB  . ALA A 414  ? 0.2646 0.2750 0.3525 -0.0012 0.0136  0.0718  412  ALA A CB  
3034  N N   . THR A 415  ? 0.2299 0.2278 0.3313 -0.0042 0.0068  0.0658  413  THR A N   
3035  C CA  . THR A 415  ? 0.2272 0.2206 0.3273 -0.0040 0.0053  0.0601  413  THR A CA  
3036  C C   . THR A 415  ? 0.2332 0.2282 0.3326 -0.0038 0.0057  0.0590  413  THR A C   
3037  O O   . THR A 415  ? 0.2681 0.2603 0.3642 -0.0034 0.0050  0.0544  413  THR A O   
3038  C CB  . THR A 415  ? 0.2453 0.2346 0.3529 -0.0053 0.0021  0.0586  413  THR A CB  
3039  O OG1 . THR A 415  ? 0.2870 0.2781 0.4037 -0.0068 0.0008  0.0625  413  THR A OG1 
3040  C CG2 . THR A 415  ? 0.2823 0.2696 0.3906 -0.0053 0.0015  0.0591  413  THR A CG2 
3041  N N   . ASP A 416  ? 0.2488 0.2487 0.3511 -0.0042 0.0069  0.0633  414  ASP A N   
3042  C CA  . ASP A 416  ? 0.2349 0.2366 0.3359 -0.0037 0.0075  0.0621  414  ASP A CA  
3043  C C   . ASP A 416  ? 0.2459 0.2484 0.3378 -0.0018 0.0096  0.0595  414  ASP A C   
3044  O O   . ASP A 416  ? 0.3213 0.3232 0.4109 -0.0012 0.0095  0.0568  414  ASP A O   
3045  C CB  . ASP A 416  ? 0.3022 0.3093 0.4092 -0.0046 0.0081  0.0672  414  ASP A CB  
3046  C CG  . ASP A 416  ? 0.4053 0.4181 0.5108 -0.0041 0.0106  0.0718  414  ASP A CG  
3047  O OD1 . ASP A 416  ? 0.3965 0.4086 0.5007 -0.0041 0.0107  0.0728  414  ASP A OD1 
3048  O OD2 . ASP A 416  ? 0.5080 0.5266 0.6134 -0.0036 0.0123  0.0741  414  ASP A OD2 
3049  N N   . VAL A 417  ? 0.2453 0.2491 0.3323 -0.0007 0.0113  0.0601  415  VAL A N   
3050  C CA  . VAL A 417  ? 0.2610 0.2660 0.3403 0.0011  0.0132  0.0579  415  VAL A CA  
3051  C C   . VAL A 417  ? 0.2208 0.2216 0.2940 0.0020  0.0129  0.0541  415  VAL A C   
3052  O O   . VAL A 417  ? 0.2294 0.2296 0.2968 0.0033  0.0137  0.0512  415  VAL A O   
3053  C CB  . VAL A 417  ? 0.3443 0.3559 0.4223 0.0021  0.0156  0.0613  415  VAL A CB  
3054  C CG1 . VAL A 417  ? 0.3752 0.3918 0.4592 0.0013  0.0160  0.0651  415  VAL A CG1 
3055  C CG2 . VAL A 417  ? 0.2897 0.3026 0.3676 0.0019  0.0162  0.0640  415  VAL A CG2 
3056  N N   . VAL A 418  ? 0.2126 0.2103 0.2872 0.0012  0.0118  0.0539  416  VAL A N   
3057  C CA  . VAL A 418  ? 0.2017 0.1952 0.2711 0.0017  0.0113  0.0502  416  VAL A CA  
3058  C C   . VAL A 418  ? 0.1967 0.1860 0.2701 0.0005  0.0088  0.0481  416  VAL A C   
3059  O O   . VAL A 418  ? 0.2118 0.2012 0.2923 -0.0008 0.0075  0.0501  416  VAL A O   
3060  C CB  . VAL A 418  ? 0.2009 0.1956 0.2667 0.0025  0.0127  0.0515  416  VAL A CB  
3061  C CG1 . VAL A 418  ? 0.2372 0.2363 0.2984 0.0041  0.0150  0.0523  416  VAL A CG1 
3062  C CG2 . VAL A 418  ? 0.2340 0.2299 0.3057 0.0014  0.0122  0.0556  416  VAL A CG2 
3063  N N   . PHE A 419  ? 0.1930 0.1789 0.2619 0.0009  0.0082  0.0441  417  PHE A N   
3064  C CA  . PHE A 419  ? 0.2186 0.2010 0.2905 0.0000  0.0059  0.0413  417  PHE A CA  
3065  C C   . PHE A 419  ? 0.1974 0.1783 0.2676 0.0003  0.0060  0.0409  417  PHE A C   
3066  O O   . PHE A 419  ? 0.2026 0.1824 0.2664 0.0012  0.0068  0.0385  417  PHE A O   
3067  C CB  . PHE A 419  ? 0.2101 0.1909 0.2783 0.0002  0.0051  0.0368  417  PHE A CB  
3068  C CG  . PHE A 419  ? 0.2029 0.1811 0.2732 -0.0004 0.0029  0.0332  417  PHE A CG  
3069  C CD1 . PHE A 419  ? 0.2206 0.1982 0.2986 -0.0014 0.0008  0.0331  417  PHE A CD1 
3070  C CD2 . PHE A 419  ? 0.2108 0.1875 0.2757 0.0001  0.0027  0.0297  417  PHE A CD2 
3071  C CE1 . PHE A 419  ? 0.2252 0.2008 0.3054 -0.0018 -0.0014 0.0291  417  PHE A CE1 
3072  C CE2 . PHE A 419  ? 0.2075 0.1827 0.2742 -0.0003 0.0008  0.0260  417  PHE A CE2 
3073  C CZ  . PHE A 419  ? 0.2092 0.1840 0.2835 -0.0012 -0.0013 0.0254  417  PHE A CZ  
3074  N N   . PRO A 420  ? 0.1822 0.1629 0.2582 -0.0004 0.0051  0.0434  418  PRO A N   
3075  C CA  . PRO A 420  ? 0.1891 0.1684 0.2637 -0.0001 0.0052  0.0433  418  PRO A CA  
3076  C C   . PRO A 420  ? 0.1908 0.1666 0.2650 -0.0001 0.0034  0.0384  418  PRO A C   
3077  O O   . PRO A 420  ? 0.2002 0.1747 0.2790 -0.0008 0.0014  0.0361  418  PRO A O   
3078  C CB  . PRO A 420  ? 0.1887 0.1690 0.2710 -0.0011 0.0044  0.0479  418  PRO A CB  
3079  C CG  . PRO A 420  ? 0.2083 0.1918 0.2946 -0.0017 0.0047  0.0512  418  PRO A CG  
3080  C CD  . PRO A 420  ? 0.1967 0.1788 0.2810 -0.0016 0.0042  0.0471  418  PRO A CD  
3081  N N   . GLN A 421  ? 0.1827 0.1575 0.2514 0.0007  0.0041  0.0367  419  GLN A N   
3082  C CA  . GLN A 421  ? 0.1820 0.1543 0.2494 0.0008  0.0028  0.0321  419  GLN A CA  
3083  C C   . GLN A 421  ? 0.2018 0.1732 0.2696 0.0011  0.0028  0.0330  419  GLN A C   
3084  O O   . GLN A 421  ? 0.2118 0.1840 0.2742 0.0018  0.0046  0.0342  419  GLN A O   
3085  C CB  . GLN A 421  ? 0.1774 0.1497 0.2370 0.0015  0.0038  0.0289  419  GLN A CB  
3086  C CG  . GLN A 421  ? 0.2044 0.1779 0.2635 0.0012  0.0038  0.0287  419  GLN A CG  
3087  C CD  . GLN A 421  ? 0.1869 0.1609 0.2385 0.0019  0.0051  0.0271  419  GLN A CD  
3088  O OE1 . GLN A 421  ? 0.2173 0.1920 0.2647 0.0027  0.0068  0.0287  419  GLN A OE1 
3089  N NE2 . GLN A 421  ? 0.2115 0.1853 0.2616 0.0016  0.0040  0.0239  419  GLN A NE2 
3090  N N   . PHE A 422  ? 0.1836 0.1533 0.2583 0.0006  0.0007  0.0324  420  PHE A N   
3091  C CA  . PHE A 422  ? 0.1709 0.1397 0.2475 0.0007  0.0004  0.0340  420  PHE A CA  
3092  C C   . PHE A 422  ? 0.1785 0.1456 0.2521 0.0014  -0.0003 0.0291  420  PHE A C   
3093  O O   . PHE A 422  ? 0.2080 0.1735 0.2863 0.0012  -0.0025 0.0257  420  PHE A O   
3094  C CB  . PHE A 422  ? 0.2006 0.1688 0.2874 -0.0003 -0.0017 0.0368  420  PHE A CB  
3095  C CG  . PHE A 422  ? 0.2137 0.1845 0.3035 -0.0010 -0.0009 0.0421  420  PHE A CG  
3096  C CD1 . PHE A 422  ? 0.2300 0.2037 0.3163 -0.0007 0.0013  0.0467  420  PHE A CD1 
3097  C CD2 . PHE A 422  ? 0.2057 0.1765 0.3016 -0.0019 -0.0023 0.0423  420  PHE A CD2 
3098  C CE1 . PHE A 422  ? 0.2194 0.1965 0.3084 -0.0013 0.0022  0.0515  420  PHE A CE1 
3099  C CE2 . PHE A 422  ? 0.2311 0.2048 0.3298 -0.0026 -0.0015 0.0473  420  PHE A CE2 
3100  C CZ  . PHE A 422  ? 0.2301 0.2071 0.3253 -0.0023 0.0008  0.0519  420  PHE A CZ  
3101  N N   . ALA A 423  ? 0.1895 0.1571 0.2554 0.0021  0.0016  0.0288  421  ALA A N   
3102  C CA  . ALA A 423  ? 0.1888 0.1552 0.2511 0.0027  0.0012  0.0246  421  ALA A CA  
3103  C C   . ALA A 423  ? 0.2145 0.1799 0.2801 0.0029  0.0005  0.0257  421  ALA A C   
3104  O O   . ALA A 423  ? 0.2367 0.2029 0.2999 0.0033  0.0019  0.0292  421  ALA A O   
3105  C CB  . ALA A 423  ? 0.1975 0.1649 0.2507 0.0034  0.0034  0.0239  421  ALA A CB  
3106  N N   . THR A 424  ? 0.2046 0.1684 0.2758 0.0029  -0.0018 0.0227  422  THR A N   
3107  C CA  . THR A 424  ? 0.2133 0.1760 0.2881 0.0032  -0.0027 0.0234  422  THR A CA  
3108  C C   . THR A 424  ? 0.2220 0.1833 0.3013 0.0034  -0.0051 0.0181  422  THR A C   
3109  O O   . THR A 424  ? 0.2356 0.1968 0.3187 0.0031  -0.0067 0.0151  422  THR A O   
3110  C CB  . THR A 424  ? 0.2411 0.2037 0.3231 0.0025  -0.0035 0.0290  422  THR A CB  
3111  O OG1 . THR A 424  ? 0.2520 0.2135 0.3370 0.0028  -0.0044 0.0299  422  THR A OG1 
3112  C CG2 . THR A 424  ? 0.2725 0.2341 0.3634 0.0017  -0.0058 0.0287  422  THR A CG2 
3113  N N   . HIS A 425  ? 0.2243 0.1849 0.3030 0.0041  -0.0054 0.0167  423  HIS A N   
3114  C CA  . HIS A 425  ? 0.2253 0.1850 0.3095 0.0046  -0.0079 0.0117  423  HIS A CA  
3115  C C   . HIS A 425  ? 0.2512 0.2089 0.3449 0.0045  -0.0101 0.0141  423  HIS A C   
3116  O O   . HIS A 425  ? 0.2801 0.2367 0.3794 0.0050  -0.0124 0.0101  423  HIS A O   
3117  C CB  . HIS A 425  ? 0.2405 0.2010 0.3182 0.0054  -0.0070 0.0081  423  HIS A CB  
3118  C CG  . HIS A 425  ? 0.2293 0.1919 0.2986 0.0054  -0.0052 0.0057  423  HIS A CG  
3119  N ND1 . HIS A 425  ? 0.2610 0.2246 0.3219 0.0057  -0.0031 0.0060  423  HIS A ND1 
3120  C CD2 . HIS A 425  ? 0.2578 0.2218 0.3260 0.0051  -0.0054 0.0032  423  HIS A CD2 
3121  C CE1 . HIS A 425  ? 0.2700 0.2353 0.3253 0.0055  -0.0021 0.0041  423  HIS A CE1 
3122  N NE2 . HIS A 425  ? 0.2439 0.2097 0.3033 0.0051  -0.0035 0.0024  423  HIS A NE2 
3123  N N   . ASN A 426  ? 0.2384 0.1958 0.3343 0.0038  -0.0096 0.0205  424  ASN A N   
3124  C CA  . ASN A 426  ? 0.2663 0.2223 0.3711 0.0035  -0.0116 0.0240  424  ASN A CA  
3125  C C   . ASN A 426  ? 0.2582 0.2130 0.3734 0.0026  -0.0142 0.0246  424  ASN A C   
3126  O O   . ASN A 426  ? 0.2545 0.2103 0.3700 0.0017  -0.0135 0.0283  424  ASN A O   
3127  C CB  . ASN A 426  ? 0.2436 0.2011 0.3449 0.0032  -0.0095 0.0308  424  ASN A CB  
3128  C CG  . ASN A 426  ? 0.2500 0.2066 0.3596 0.0028  -0.0114 0.0352  424  ASN A CG  
3129  O OD1 . ASN A 426  ? 0.2830 0.2379 0.4028 0.0022  -0.0142 0.0359  424  ASN A OD1 
3130  N ND2 . ASN A 426  ? 0.2556 0.2133 0.3610 0.0032  -0.0100 0.0384  424  ASN A ND2 
3131  N N   . ALA A 427  ? 0.2375 0.1902 0.3616 0.0030  -0.0175 0.0209  425  ALA A N   
3132  C CA  . ALA A 427  ? 0.2467 0.1980 0.3815 0.0022  -0.0205 0.0207  425  ALA A CA  
3133  C C   . ALA A 427  ? 0.2387 0.1897 0.3805 0.0008  -0.0211 0.0287  425  ALA A C   
3134  O O   . ALA A 427  ? 0.2446 0.1953 0.3929 -0.0002 -0.0225 0.0303  425  ALA A O   
3135  C CB  . ALA A 427  ? 0.2848 0.2341 0.4283 0.0031  -0.0240 0.0148  425  ALA A CB  
3136  N N   . GLN A 428  ? 0.2493 0.2008 0.3902 0.0007  -0.0203 0.0339  426  GLN A N   
3137  C CA  . GLN A 428  ? 0.2718 0.2241 0.4184 -0.0007 -0.0206 0.0422  426  GLN A CA  
3138  C C   . GLN A 428  ? 0.2575 0.2130 0.3974 -0.0014 -0.0176 0.0460  426  GLN A C   
3139  O O   . GLN A 428  ? 0.2617 0.2180 0.4077 -0.0027 -0.0184 0.0500  426  GLN A O   
3140  C CB  . GLN A 428  ? 0.2427 0.1955 0.3890 -0.0005 -0.0203 0.0468  426  GLN A CB  
3141  C CG  . GLN A 428  ? 0.2746 0.2282 0.4302 -0.0020 -0.0218 0.0553  426  GLN A CG  
3142  C CD  . GLN A 428  ? 0.3357 0.2936 0.4869 -0.0031 -0.0191 0.0617  426  GLN A CD  
3143  O OE1 . GLN A 428  ? 0.3317 0.2924 0.4715 -0.0025 -0.0156 0.0617  426  GLN A OE1 
3144  N NE2 . GLN A 428  ? 0.3110 0.2696 0.4717 -0.0048 -0.0208 0.0673  426  GLN A NE2 
3145  N N   . THR A 429  ? 0.2513 0.2088 0.3790 -0.0006 -0.0142 0.0447  427  THR A N   
3146  C CA  . THR A 429  ? 0.2496 0.2101 0.3706 -0.0010 -0.0113 0.0472  427  THR A CA  
3147  C C   . THR A 429  ? 0.2424 0.2022 0.3664 -0.0015 -0.0123 0.0444  427  THR A C   
3148  O O   . THR A 429  ? 0.2426 0.2043 0.3690 -0.0025 -0.0119 0.0485  427  THR A O   
3149  C CB  . THR A 429  ? 0.2463 0.2081 0.3546 0.0002  -0.0082 0.0444  427  THR A CB  
3150  O OG1 . THR A 429  ? 0.2584 0.2205 0.3642 0.0008  -0.0077 0.0460  427  THR A OG1 
3151  C CG2 . THR A 429  ? 0.2730 0.2383 0.3750 0.0000  -0.0053 0.0478  427  THR A CG2 
3152  N N   . LEU A 430  ? 0.2463 0.2040 0.3706 -0.0008 -0.0137 0.0373  428  LEU A N   
3153  C CA  . LEU A 430  ? 0.2410 0.1984 0.3676 -0.0011 -0.0148 0.0338  428  LEU A CA  
3154  C C   . LEU A 430  ? 0.2494 0.2058 0.3884 -0.0024 -0.0176 0.0371  428  LEU A C   
3155  O O   . LEU A 430  ? 0.2498 0.2075 0.3902 -0.0033 -0.0173 0.0392  428  LEU A O   
3156  C CB  . LEU A 430  ? 0.2321 0.1881 0.3579 0.0000  -0.0162 0.0256  428  LEU A CB  
3157  C CG  . LEU A 430  ? 0.2826 0.2391 0.4076 0.0000  -0.0169 0.0202  428  LEU A CG  
3158  C CD1 . LEU A 430  ? 0.3181 0.2745 0.4400 0.0013  -0.0175 0.0129  428  LEU A CD1 
3159  C CD2 . LEU A 430  ? 0.3013 0.2565 0.4378 -0.0008 -0.0201 0.0200  428  LEU A CD2 
3160  N N   . ALA A 431  ? 0.2697 0.2238 0.4181 -0.0025 -0.0206 0.0374  429  ALA A N   
3161  C CA  . ALA A 431  ? 0.2692 0.2219 0.4307 -0.0038 -0.0239 0.0402  429  ALA A CA  
3162  C C   . ALA A 431  ? 0.2665 0.2218 0.4296 -0.0053 -0.0226 0.0491  429  ALA A C   
3163  O O   . ALA A 431  ? 0.2494 0.2051 0.4194 -0.0066 -0.0238 0.0514  429  ALA A O   
3164  C CB  . ALA A 431  ? 0.2626 0.2123 0.4338 -0.0036 -0.0273 0.0394  429  ALA A CB  
3165  N N   . ALA A 432  ? 0.2505 0.2081 0.4074 -0.0052 -0.0200 0.0540  430  ALA A N   
3166  C CA  . ALA A 432  ? 0.2648 0.2262 0.4225 -0.0066 -0.0184 0.0624  430  ALA A CA  
3167  C C   . ALA A 432  ? 0.2846 0.2487 0.4373 -0.0069 -0.0162 0.0625  430  ALA A C   
3168  O O   . ALA A 432  ? 0.2820 0.2483 0.4402 -0.0083 -0.0165 0.0677  430  ALA A O   
3169  C CB  . ALA A 432  ? 0.2750 0.2392 0.4252 -0.0060 -0.0158 0.0664  430  ALA A CB  
3170  N N   . ILE A 433  ? 0.2604 0.2244 0.4028 -0.0056 -0.0141 0.0569  431  ILE A N   
3171  C CA  . ILE A 433  ? 0.2379 0.2043 0.3751 -0.0057 -0.0120 0.0568  431  ILE A CA  
3172  C C   . ILE A 433  ? 0.2523 0.2169 0.3966 -0.0064 -0.0145 0.0536  431  ILE A C   
3173  O O   . ILE A 433  ? 0.2415 0.2082 0.3878 -0.0073 -0.0141 0.0564  431  ILE A O   
3174  C CB  . ILE A 433  ? 0.2529 0.2199 0.3773 -0.0042 -0.0092 0.0523  431  ILE A CB  
3175  C CG1 . ILE A 433  ? 0.2913 0.2609 0.4092 -0.0037 -0.0066 0.0563  431  ILE A CG1 
3176  C CG2 . ILE A 433  ? 0.2665 0.2351 0.3862 -0.0042 -0.0077 0.0507  431  ILE A CG2 
3177  C CD1 . ILE A 433  ? 0.3153 0.2851 0.4218 -0.0022 -0.0042 0.0523  431  ILE A CD1 
3178  N N   . TYR A 434  ? 0.2493 0.2103 0.3977 -0.0059 -0.0172 0.0475  432  TYR A N   
3179  C CA  . TYR A 434  ? 0.2534 0.2128 0.4092 -0.0064 -0.0200 0.0439  432  TYR A CA  
3180  C C   . TYR A 434  ? 0.2562 0.2159 0.4236 -0.0082 -0.0221 0.0498  432  TYR A C   
3181  O O   . TYR A 434  ? 0.2731 0.2336 0.4437 -0.0090 -0.0227 0.0500  432  TYR A O   
3182  C CB  . TYR A 434  ? 0.2909 0.2470 0.4506 -0.0054 -0.0229 0.0368  432  TYR A CB  
3183  C CG  . TYR A 434  ? 0.2649 0.2193 0.4349 -0.0059 -0.0266 0.0329  432  TYR A CG  
3184  C CD1 . TYR A 434  ? 0.2823 0.2378 0.4495 -0.0058 -0.0264 0.0290  432  TYR A CD1 
3185  C CD2 . TYR A 434  ? 0.3048 0.2565 0.4877 -0.0064 -0.0305 0.0331  432  TYR A CD2 
3186  C CE1 . TYR A 434  ? 0.2950 0.2492 0.4715 -0.0062 -0.0299 0.0251  432  TYR A CE1 
3187  C CE2 . TYR A 434  ? 0.3385 0.2885 0.5312 -0.0067 -0.0342 0.0291  432  TYR A CE2 
3188  C CZ  . TYR A 434  ? 0.3538 0.3052 0.5431 -0.0066 -0.0338 0.0250  432  TYR A CZ  
3189  O OH  . TYR A 434  ? 0.3878 0.3379 0.5870 -0.0068 -0.0376 0.0206  432  TYR A OH  
3190  N N   . HIS A 435  ? 0.2728 0.2321 0.4468 -0.0089 -0.0233 0.0550  433  HIS A N   
3191  C CA  . HIS A 435  ? 0.2924 0.2523 0.4782 -0.0108 -0.0254 0.0615  433  HIS A CA  
3192  C C   . HIS A 435  ? 0.3002 0.2652 0.4820 -0.0117 -0.0223 0.0689  433  HIS A C   
3193  O O   . HIS A 435  ? 0.2928 0.2593 0.4815 -0.0132 -0.0232 0.0727  433  HIS A O   
3194  C CB  . HIS A 435  ? 0.3142 0.2720 0.5097 -0.0113 -0.0283 0.0646  433  HIS A CB  
3195  C CG  . HIS A 435  ? 0.3258 0.2788 0.5294 -0.0106 -0.0323 0.0577  433  HIS A CG  
3196  N ND1 . HIS A 435  ? 0.3403 0.2911 0.5566 -0.0116 -0.0363 0.0566  433  HIS A ND1 
3197  C CD2 . HIS A 435  ? 0.2759 0.2263 0.4764 -0.0089 -0.0330 0.0510  433  HIS A CD2 
3198  C CE1 . HIS A 435  ? 0.3389 0.2860 0.5599 -0.0104 -0.0394 0.0493  433  HIS A CE1 
3199  N NE2 . HIS A 435  ? 0.3079 0.2549 0.5195 -0.0088 -0.0374 0.0458  433  HIS A NE2 
3200  N N   . MET A 436  ? 0.2790 0.2469 0.4498 -0.0109 -0.0187 0.0707  434  MET A N   
3201  C CA  . MET A 436  ? 0.2944 0.2678 0.4602 -0.0114 -0.0154 0.0766  434  MET A CA  
3202  C C   . MET A 436  ? 0.2533 0.2279 0.4165 -0.0114 -0.0144 0.0741  434  MET A C   
3203  O O   . MET A 436  ? 0.2864 0.2648 0.4523 -0.0126 -0.0136 0.0793  434  MET A O   
3204  C CB  . MET A 436  ? 0.2936 0.2696 0.4474 -0.0100 -0.0119 0.0769  434  MET A CB  
3205  C CG  . MET A 436  ? 0.2859 0.2683 0.4349 -0.0103 -0.0087 0.0828  434  MET A CG  
3206  S SD  . MET A 436  ? 0.2946 0.2794 0.4289 -0.0083 -0.0047 0.0809  434  MET A SD  
3207  C CE  . MET A 436  ? 0.3315 0.3163 0.4689 -0.0085 -0.0058 0.0851  434  MET A CE  
3208  N N   . ALA A 437  ? 0.2444 0.2160 0.4023 -0.0102 -0.0146 0.0663  435  ALA A N   
3209  C CA  . ALA A 437  ? 0.2792 0.2520 0.4339 -0.0101 -0.0136 0.0638  435  ALA A CA  
3210  C C   . ALA A 437  ? 0.3171 0.2888 0.4832 -0.0116 -0.0167 0.0642  435  ALA A C   
3211  O O   . ALA A 437  ? 0.3035 0.2773 0.4691 -0.0120 -0.0159 0.0649  435  ALA A O   
3212  C CB  . ALA A 437  ? 0.2953 0.2658 0.4412 -0.0085 -0.0129 0.0558  435  ALA A CB  
3213  N N   . GLY A 438  ? 0.3559 0.3242 0.5325 -0.0123 -0.0204 0.0636  436  GLY A N   
3214  C CA  . GLY A 438  ? 0.3716 0.3388 0.5604 -0.0138 -0.0237 0.0646  436  GLY A CA  
3215  C C   . GLY A 438  ? 0.3467 0.3113 0.5365 -0.0132 -0.0257 0.0565  436  GLY A C   
3216  O O   . GLY A 438  ? 0.3349 0.2986 0.5161 -0.0116 -0.0247 0.0500  436  GLY A O   
3217  N N   . LYS A 439  ? 0.4226 0.3865 0.6235 -0.0145 -0.0287 0.0572  437  LYS A N   
3218  C CA  . LYS A 439  ? 0.4370 0.3984 0.6415 -0.0141 -0.0316 0.0495  437  LYS A CA  
3219  C C   . LYS A 439  ? 0.3789 0.3426 0.5759 -0.0137 -0.0296 0.0468  437  LYS A C   
3220  O O   . LYS A 439  ? 0.5069 0.4695 0.7026 -0.0128 -0.0310 0.0395  437  LYS A O   
3221  C CB  . LYS A 439  ? 0.5179 0.4773 0.7386 -0.0156 -0.0361 0.0510  437  LYS A CB  
3222  N N   . ASP A 440  ? 0.3124 0.2799 0.5045 -0.0143 -0.0265 0.0524  438  ASP A N   
3223  C CA  . ASP A 440  ? 0.4285 0.3983 0.6135 -0.0138 -0.0246 0.0502  438  ASP A CA  
3224  C C   . ASP A 440  ? 0.4289 0.3988 0.6005 -0.0120 -0.0218 0.0457  438  ASP A C   
3225  O O   . ASP A 440  ? 0.4395 0.4110 0.6035 -0.0114 -0.0188 0.0488  438  ASP A O   
3226  C CB  . ASP A 440  ? 0.4547 0.4287 0.6392 -0.0149 -0.0221 0.0576  438  ASP A CB  
3227  C CG  . ASP A 440  ? 0.5321 0.5066 0.7296 -0.0169 -0.0248 0.0615  438  ASP A CG  
3228  O OD1 . ASP A 440  ? 0.4779 0.4490 0.6850 -0.0174 -0.0288 0.0583  438  ASP A OD1 
3229  O OD2 . ASP A 440  ? 0.5203 0.4989 0.7186 -0.0179 -0.0231 0.0677  438  ASP A OD2 
3230  N N   . PHE A 441  ? 0.3365 0.3052 0.5052 -0.0111 -0.0230 0.0384  439  PHE A N   
3231  C CA  . PHE A 441  ? 0.3115 0.2806 0.4680 -0.0095 -0.0207 0.0343  439  PHE A CA  
3232  C C   . PHE A 441  ? 0.3498 0.3202 0.5022 -0.0091 -0.0208 0.0296  439  PHE A C   
3233  O O   . PHE A 441  ? 0.3532 0.3232 0.5125 -0.0096 -0.0236 0.0264  439  PHE A O   
3234  C CB  . PHE A 441  ? 0.2714 0.2379 0.4269 -0.0085 -0.0218 0.0296  439  PHE A CB  
3235  C CG  . PHE A 441  ? 0.2948 0.2621 0.4379 -0.0071 -0.0193 0.0263  439  PHE A CG  
3236  C CD1 . PHE A 441  ? 0.2749 0.2431 0.4104 -0.0066 -0.0161 0.0302  439  PHE A CD1 
3237  C CD2 . PHE A 441  ? 0.2812 0.2490 0.4202 -0.0063 -0.0200 0.0197  439  PHE A CD2 
3238  C CE1 . PHE A 441  ? 0.2557 0.2245 0.3804 -0.0054 -0.0139 0.0274  439  PHE A CE1 
3239  C CE2 . PHE A 441  ? 0.2862 0.2551 0.4142 -0.0052 -0.0177 0.0173  439  PHE A CE2 
3240  C CZ  . PHE A 441  ? 0.2706 0.2397 0.3917 -0.0048 -0.0147 0.0213  439  PHE A CZ  
3241  N N   . HIS A 442  ? 0.2781 0.2501 0.4195 -0.0082 -0.0178 0.0291  440  HIS A N   
3242  C CA  . HIS A 442  ? 0.2977 0.2710 0.4336 -0.0077 -0.0178 0.0245  440  HIS A CA  
3243  C C   . HIS A 442  ? 0.3584 0.3322 0.4829 -0.0064 -0.0152 0.0229  440  HIS A C   
3244  O O   . HIS A 442  ? 0.2738 0.2476 0.3941 -0.0061 -0.0128 0.0266  440  HIS A O   
3245  C CB  . HIS A 442  ? 0.3329 0.3086 0.4691 -0.0083 -0.0169 0.0276  440  HIS A CB  
3246  C CG  . HIS A 442  ? 0.3061 0.2837 0.4369 -0.0081 -0.0134 0.0331  440  HIS A CG  
3247  N ND1 . HIS A 442  ? 0.3085 0.2869 0.4443 -0.0089 -0.0127 0.0393  440  HIS A ND1 
3248  C CD2 . HIS A 442  ? 0.3245 0.3035 0.4456 -0.0072 -0.0107 0.0334  440  HIS A CD2 
3249  C CE1 . HIS A 442  ? 0.2951 0.2759 0.4242 -0.0084 -0.0095 0.0427  440  HIS A CE1 
3250  N NE2 . HIS A 442  ? 0.2866 0.2675 0.4070 -0.0073 -0.0083 0.0391  440  HIS A NE2 
3251  N N   . VAL A 443  ? 0.3609 0.3354 0.4807 -0.0058 -0.0159 0.0173  441  VAL A N   
3252  C CA  . VAL A 443  ? 0.3719 0.3471 0.4812 -0.0048 -0.0136 0.0160  441  VAL A CA  
3253  C C   . VAL A 443  ? 0.3160 0.2925 0.4196 -0.0047 -0.0108 0.0204  441  VAL A C   
3254  O O   . VAL A 443  ? 0.3035 0.2816 0.4085 -0.0052 -0.0109 0.0216  441  VAL A O   
3255  C CB  . VAL A 443  ? 0.3586 0.3352 0.4642 -0.0044 -0.0149 0.0098  441  VAL A CB  
3256  C CG1 . VAL A 443  ? 0.3779 0.3558 0.4729 -0.0037 -0.0125 0.0097  441  VAL A CG1 
3257  C CG2 . VAL A 443  ? 0.4079 0.3835 0.5176 -0.0040 -0.0171 0.0052  441  VAL A CG2 
3258  N N   . GLY A 444  ? 0.2696 0.2458 0.3672 -0.0041 -0.0084 0.0226  442  GLY A N   
3259  C CA  . GLY A 444  ? 0.2376 0.2152 0.3308 -0.0038 -0.0058 0.0267  442  GLY A CA  
3260  C C   . GLY A 444  ? 0.2207 0.1986 0.3173 -0.0040 -0.0046 0.0320  442  GLY A C   
3261  O O   . GLY A 444  ? 0.2423 0.2218 0.3346 -0.0035 -0.0022 0.0351  442  GLY A O   
3262  N N   . LYS A 445  ? 0.2282 0.2049 0.3328 -0.0048 -0.0063 0.0331  443  LYS A N   
3263  C CA  . LYS A 445  ? 0.2258 0.2034 0.3338 -0.0052 -0.0053 0.0387  443  LYS A CA  
3264  C C   . LYS A 445  ? 0.2507 0.2277 0.3532 -0.0043 -0.0036 0.0395  443  LYS A C   
3265  O O   . LYS A 445  ? 0.2241 0.2033 0.3227 -0.0039 -0.0012 0.0431  443  LYS A O   
3266  C CB  . LYS A 445  ? 0.2690 0.2455 0.3881 -0.0064 -0.0079 0.0403  443  LYS A CB  
3267  C CG  . LYS A 445  ? 0.2999 0.2785 0.4229 -0.0072 -0.0068 0.0471  443  LYS A CG  
3268  C CD  . LYS A 445  ? 0.3761 0.3536 0.5110 -0.0086 -0.0096 0.0495  443  LYS A CD  
3269  C CE  . LYS A 445  ? 0.3903 0.3715 0.5294 -0.0096 -0.0084 0.0569  443  LYS A CE  
3270  N NZ  . LYS A 445  ? 0.4825 0.4629 0.6340 -0.0113 -0.0113 0.0601  443  LYS A NZ  
3271  N N   . TYR A 446  ? 0.2281 0.2026 0.3303 -0.0040 -0.0049 0.0358  444  TYR A N   
3272  C CA  . TYR A 446  ? 0.2237 0.1974 0.3201 -0.0031 -0.0036 0.0354  444  TYR A CA  
3273  C C   . TYR A 446  ? 0.2165 0.1880 0.3120 -0.0027 -0.0053 0.0296  444  TYR A C   
3274  O O   . TYR A 446  ? 0.2236 0.1945 0.3235 -0.0031 -0.0076 0.0261  444  TYR A O   
3275  C CB  . TYR A 446  ? 0.2078 0.1816 0.3086 -0.0035 -0.0034 0.0401  444  TYR A CB  
3276  C CG  . TYR A 446  ? 0.2414 0.2128 0.3514 -0.0042 -0.0064 0.0393  444  TYR A CG  
3277  C CD1 . TYR A 446  ? 0.3490 0.3204 0.4688 -0.0055 -0.0085 0.0416  444  TYR A CD1 
3278  C CD2 . TYR A 446  ? 0.2847 0.2539 0.3938 -0.0036 -0.0073 0.0362  444  TYR A CD2 
3279  C CE1 . TYR A 446  ? 0.2794 0.2483 0.4084 -0.0061 -0.0116 0.0407  444  TYR A CE1 
3280  C CE2 . TYR A 446  ? 0.3400 0.3068 0.4579 -0.0041 -0.0102 0.0351  444  TYR A CE2 
3281  C CZ  . TYR A 446  ? 0.3320 0.2986 0.4599 -0.0053 -0.0124 0.0373  444  TYR A CZ  
3282  O OH  . TYR A 446  ? 0.3969 0.3609 0.5342 -0.0056 -0.0156 0.0359  444  TYR A OH  
3283  N N   . GLU A 447  ? 0.1915 0.1622 0.2814 -0.0019 -0.0043 0.0283  445  GLU A N   
3284  C CA  . GLU A 447  ? 0.2067 0.1760 0.2962 -0.0015 -0.0059 0.0230  445  GLU A CA  
3285  C C   . GLU A 447  ? 0.2292 0.1974 0.3171 -0.0010 -0.0052 0.0238  445  GLU A C   
3286  O O   . GLU A 447  ? 0.2197 0.1884 0.3049 -0.0008 -0.0033 0.0280  445  GLU A O   
3287  C CB  . GLU A 447  ? 0.1989 0.1692 0.2809 -0.0010 -0.0052 0.0189  445  GLU A CB  
3288  C CG  . GLU A 447  ? 0.2170 0.1880 0.2901 -0.0003 -0.0025 0.0205  445  GLU A CG  
3289  C CD  . GLU A 447  ? 0.2228 0.1950 0.2892 -0.0001 -0.0021 0.0174  445  GLU A CD  
3290  O OE1 . GLU A 447  ? 0.2448 0.2181 0.3130 -0.0005 -0.0035 0.0147  445  GLU A OE1 
3291  O OE2 . GLU A 447  ? 0.2172 0.1896 0.2768 0.0005  -0.0003 0.0179  445  GLU A OE2 
3292  N N   . PHE A 448  ? 0.2068 0.1737 0.2961 -0.0006 -0.0068 0.0194  446  PHE A N   
3293  C CA  . PHE A 448  ? 0.2066 0.1726 0.2929 0.0001  -0.0062 0.0190  446  PHE A CA  
3294  C C   . PHE A 448  ? 0.1865 0.1535 0.2636 0.0008  -0.0048 0.0155  446  PHE A C   
3295  O O   . PHE A 448  ? 0.2007 0.1690 0.2750 0.0007  -0.0049 0.0129  446  PHE A O   
3296  C CB  . PHE A 448  ? 0.2315 0.1957 0.3254 0.0002  -0.0089 0.0163  446  PHE A CB  
3297  C CG  . PHE A 448  ? 0.2367 0.1997 0.3404 -0.0006 -0.0105 0.0203  446  PHE A CG  
3298  C CD1 . PHE A 448  ? 0.2296 0.1923 0.3341 -0.0008 -0.0096 0.0255  446  PHE A CD1 
3299  C CD2 . PHE A 448  ? 0.2433 0.2057 0.3554 -0.0013 -0.0131 0.0191  446  PHE A CD2 
3300  C CE1 . PHE A 448  ? 0.2858 0.2478 0.3995 -0.0017 -0.0111 0.0300  446  PHE A CE1 
3301  C CE2 . PHE A 448  ? 0.2811 0.2424 0.4029 -0.0023 -0.0147 0.0233  446  PHE A CE2 
3302  C CZ  . PHE A 448  ? 0.2546 0.2158 0.3772 -0.0025 -0.0137 0.0290  446  PHE A CZ  
3303  N N   . GLN A 449  ? 0.1912 0.1577 0.2639 0.0014  -0.0037 0.0157  447  GLN A N   
3304  C CA  . GLN A 449  ? 0.1993 0.1668 0.2642 0.0020  -0.0027 0.0125  447  GLN A CA  
3305  C C   . GLN A 449  ? 0.2257 0.1924 0.2905 0.0026  -0.0031 0.0104  447  GLN A C   
3306  O O   . GLN A 449  ? 0.2132 0.1784 0.2821 0.0027  -0.0035 0.0127  447  GLN A O   
3307  C CB  . GLN A 449  ? 0.1962 0.1645 0.2534 0.0022  -0.0001 0.0151  447  GLN A CB  
3308  C CG  . GLN A 449  ? 0.1871 0.1564 0.2443 0.0018  0.0004  0.0171  447  GLN A CG  
3309  C CD  . GLN A 449  ? 0.2173 0.1875 0.2669 0.0021  0.0024  0.0182  447  GLN A CD  
3310  O OE1 . GLN A 449  ? 0.2297 0.1997 0.2744 0.0027  0.0036  0.0182  447  GLN A OE1 
3311  N NE2 . GLN A 449  ? 0.2067 0.1780 0.2557 0.0019  0.0026  0.0189  447  GLN A NE2 
3312  N N   . CYS A 450  ? 0.2000 0.1680 0.2604 0.0029  -0.0031 0.0062  448  CYS A N   
3313  C CA  . CYS A 450  ? 0.1986 0.1664 0.2583 0.0035  -0.0034 0.0039  448  CYS A CA  
3314  C C   . CYS A 450  ? 0.2209 0.1907 0.2724 0.0037  -0.0021 0.0017  448  CYS A C   
3315  O O   . CYS A 450  ? 0.2184 0.1897 0.2657 0.0033  -0.0014 0.0017  448  CYS A O   
3316  C CB  . CYS A 450  ? 0.2179 0.1856 0.2851 0.0037  -0.0061 -0.0003 448  CYS A CB  
3317  S SG  . CYS A 450  ? 0.2493 0.2205 0.3155 0.0038  -0.0074 -0.0066 448  CYS A SG  
3318  N N   . LEU A 451  ? 0.2097 0.1795 0.2593 0.0042  -0.0020 0.0001  449  LEU A N   
3319  C CA  . LEU A 451  ? 0.2377 0.2096 0.2802 0.0043  -0.0009 -0.0018 449  LEU A CA  
3320  C C   . LEU A 451  ? 0.2369 0.2120 0.2806 0.0044  -0.0024 -0.0073 449  LEU A C   
3321  O O   . LEU A 451  ? 0.2386 0.2136 0.2883 0.0049  -0.0041 -0.0102 449  LEU A O   
3322  C CB  . LEU A 451  ? 0.2419 0.2127 0.2817 0.0048  0.0002  -0.0005 449  LEU A CB  
3323  C CG  . LEU A 451  ? 0.2829 0.2558 0.3160 0.0048  0.0012  -0.0021 449  LEU A CG  
3324  C CD1 . LEU A 451  ? 0.2709 0.2444 0.2979 0.0043  0.0026  0.0001  449  LEU A CD1 
3325  C CD2 . LEU A 451  ? 0.3059 0.2774 0.3379 0.0054  0.0019  -0.0012 449  LEU A CD2 
3326  N N   . HIS A 452  ? 0.2264 0.2047 0.2648 0.0040  -0.0018 -0.0086 450  HIS A N   
3327  C CA  . HIS A 452  ? 0.2148 0.1974 0.2529 0.0041  -0.0029 -0.0137 450  HIS A CA  
3328  C C   . HIS A 452  ? 0.2390 0.2223 0.2778 0.0048  -0.0032 -0.0163 450  HIS A C   
3329  O O   . HIS A 452  ? 0.2703 0.2519 0.3058 0.0050  -0.0019 -0.0140 450  HIS A O   
3330  C CB  . HIS A 452  ? 0.2227 0.2088 0.2539 0.0033  -0.0019 -0.0133 450  HIS A CB  
3331  C CG  . HIS A 452  ? 0.2015 0.1932 0.2311 0.0034  -0.0026 -0.0179 450  HIS A CG  
3332  N ND1 . HIS A 452  ? 0.2471 0.2429 0.2790 0.0033  -0.0041 -0.0216 450  HIS A ND1 
3333  C CD2 . HIS A 452  ? 0.2527 0.2472 0.2791 0.0035  -0.0021 -0.0195 450  HIS A CD2 
3334  C CE1 . HIS A 452  ? 0.2634 0.2647 0.2932 0.0034  -0.0044 -0.0253 450  HIS A CE1 
3335  N NE2 . HIS A 452  ? 0.2543 0.2548 0.2808 0.0035  -0.0031 -0.0241 450  HIS A NE2 
3336  N N   . GLY A 453  ? 0.2623 0.2483 0.3055 0.0054  -0.0050 -0.0215 451  GLY A N   
3337  C CA  . GLY A 453  ? 0.2932 0.2806 0.3371 0.0062  -0.0053 -0.0246 451  GLY A CA  
3338  C C   . GLY A 453  ? 0.3983 0.3810 0.4467 0.0069  -0.0056 -0.0228 451  GLY A C   
3339  O O   . GLY A 453  ? 0.4232 0.4064 0.4710 0.0075  -0.0054 -0.0240 451  GLY A O   
3340  N N   . MET A 454  ? 0.3040 0.2826 0.3571 0.0067  -0.0062 -0.0196 452  MET A N   
3341  C CA  . MET A 454  ? 0.2700 0.2445 0.3279 0.0072  -0.0066 -0.0171 452  MET A CA  
3342  C C   . MET A 454  ? 0.3044 0.2764 0.3708 0.0070  -0.0085 -0.0162 452  MET A C   
3343  O O   . MET A 454  ? 0.3228 0.2932 0.3969 0.0076  -0.0106 -0.0178 452  MET A O   
3344  C CB  . MET A 454  ? 0.3040 0.2762 0.3564 0.0068  -0.0043 -0.0114 452  MET A CB  
3345  C CG  . MET A 454  ? 0.3161 0.2847 0.3731 0.0071  -0.0047 -0.0079 452  MET A CG  
3346  S SD  . MET A 454  ? 0.3852 0.3539 0.4467 0.0082  -0.0063 -0.0116 452  MET A SD  
3347  C CE  . MET A 454  ? 0.4095 0.3805 0.4611 0.0083  -0.0040 -0.0122 452  MET A CE  
3348  N N   . GLY A 455  ? 0.2825 0.2541 0.3480 0.0062  -0.0081 -0.0137 453  GLY A N   
3349  C CA  . GLY A 455  ? 0.2664 0.2356 0.3398 0.0059  -0.0097 -0.0118 453  GLY A CA  
3350  C C   . GLY A 455  ? 0.2740 0.2447 0.3535 0.0060  -0.0121 -0.0166 453  GLY A C   
3351  O O   . GLY A 455  ? 0.2925 0.2610 0.3801 0.0057  -0.0140 -0.0155 453  GLY A O   
3352  N N   . GLU A 456  ? 0.2910 0.2659 0.3672 0.0063  -0.0124 -0.0218 454  GLU A N   
3353  C CA  . GLU A 456  ? 0.3002 0.2774 0.3819 0.0065  -0.0148 -0.0267 454  GLU A CA  
3354  C C   . GLU A 456  ? 0.3336 0.3091 0.4260 0.0073  -0.0179 -0.0301 454  GLU A C   
3355  O O   . GLU A 456  ? 0.3246 0.2994 0.4241 0.0071  -0.0200 -0.0314 454  GLU A O   
3356  C CB  . GLU A 456  ? 0.3327 0.3158 0.4085 0.0067  -0.0144 -0.0316 454  GLU A CB  
3357  C CG  . GLU A 456  ? 0.3768 0.3616 0.4435 0.0057  -0.0120 -0.0284 454  GLU A CG  
3358  C CD  . GLU A 456  ? 0.3686 0.3543 0.4277 0.0057  -0.0098 -0.0267 454  GLU A CD  
3359  O OE1 . GLU A 456  ? 0.3582 0.3414 0.4188 0.0063  -0.0096 -0.0259 454  GLU A OE1 
3360  O OE2 . GLU A 456  ? 0.3841 0.3730 0.4359 0.0052  -0.0084 -0.0262 454  GLU A OE2 
3361  N N   . PRO A 457  ? 0.3187 0.2936 0.4133 0.0082  -0.0185 -0.0320 455  PRO A N   
3362  C CA  . PRO A 457  ? 0.3270 0.3000 0.4332 0.0091  -0.0218 -0.0352 455  PRO A CA  
3363  C C   . PRO A 457  ? 0.3185 0.2866 0.4324 0.0082  -0.0231 -0.0300 455  PRO A C   
3364  O O   . PRO A 457  ? 0.3324 0.2996 0.4560 0.0084  -0.0261 -0.0326 455  PRO A O   
3365  C CB  . PRO A 457  ? 0.3328 0.3055 0.4387 0.0101  -0.0216 -0.0364 455  PRO A CB  
3366  C CG  . PRO A 457  ? 0.3449 0.3218 0.4396 0.0101  -0.0189 -0.0374 455  PRO A CG  
3367  C CD  . PRO A 457  ? 0.3169 0.2934 0.4046 0.0087  -0.0165 -0.0322 455  PRO A CD  
3368  N N   . LEU A 458  ? 0.2998 0.2652 0.4099 0.0073  -0.0208 -0.0228 456  LEU A N   
3369  C CA  . LEU A 458  ? 0.2835 0.2452 0.4005 0.0063  -0.0218 -0.0171 456  LEU A CA  
3370  C C   . LEU A 458  ? 0.2825 0.2451 0.4006 0.0055  -0.0221 -0.0169 456  LEU A C   
3371  O O   . LEU A 458  ? 0.2819 0.2428 0.4097 0.0051  -0.0248 -0.0171 456  LEU A O   
3372  C CB  . LEU A 458  ? 0.2924 0.2523 0.4041 0.0057  -0.0191 -0.0098 456  LEU A CB  
3373  C CG  . LEU A 458  ? 0.3067 0.2642 0.4241 0.0045  -0.0194 -0.0031 456  LEU A CG  
3374  C CD1 . LEU A 458  ? 0.2665 0.2213 0.3970 0.0046  -0.0231 -0.0033 456  LEU A CD1 
3375  C CD2 . LEU A 458  ? 0.2976 0.2546 0.4088 0.0042  -0.0166 0.0034  456  LEU A CD2 
3376  N N   . TYR A 459  ? 0.2691 0.2342 0.3777 0.0051  -0.0197 -0.0166 457  TYR A N   
3377  C CA  . TYR A 459  ? 0.2819 0.2477 0.3911 0.0042  -0.0197 -0.0153 457  TYR A CA  
3378  C C   . TYR A 459  ? 0.2887 0.2569 0.4024 0.0046  -0.0223 -0.0220 457  TYR A C   
3379  O O   . TYR A 459  ? 0.2882 0.2565 0.4055 0.0039  -0.0233 -0.0213 457  TYR A O   
3380  C CB  . TYR A 459  ? 0.2543 0.2214 0.3527 0.0036  -0.0164 -0.0117 457  TYR A CB  
3381  C CG  . TYR A 459  ? 0.2380 0.2026 0.3353 0.0031  -0.0145 -0.0045 457  TYR A CG  
3382  C CD1 . TYR A 459  ? 0.2568 0.2199 0.3592 0.0021  -0.0149 0.0001  457  TYR A CD1 
3383  C CD2 . TYR A 459  ? 0.2527 0.2168 0.3444 0.0035  -0.0126 -0.0024 457  TYR A CD2 
3384  C CE1 . TYR A 459  ? 0.2643 0.2261 0.3658 0.0017  -0.0132 0.0066  457  TYR A CE1 
3385  C CE2 . TYR A 459  ? 0.2322 0.1947 0.3229 0.0031  -0.0110 0.0040  457  TYR A CE2 
3386  C CZ  . TYR A 459  ? 0.2669 0.2286 0.3625 0.0022  -0.0113 0.0084  457  TYR A CZ  
3387  O OH  . TYR A 459  ? 0.2599 0.2211 0.3544 0.0018  -0.0096 0.0146  457  TYR A OH  
3388  N N   . GLU A 460  ? 0.2886 0.2594 0.4028 0.0058  -0.0236 -0.0286 458  GLU A N   
3389  C CA  . GLU A 460  ? 0.3166 0.2897 0.4373 0.0064  -0.0267 -0.0353 458  GLU A CA  
3390  C C   . GLU A 460  ? 0.3552 0.3246 0.4893 0.0063  -0.0301 -0.0354 458  GLU A C   
3391  O O   . GLU A 460  ? 0.3444 0.3152 0.4853 0.0066  -0.0330 -0.0404 458  GLU A O   
3392  C CB  . GLU A 460  ? 0.3942 0.3720 0.5120 0.0077  -0.0271 -0.0426 458  GLU A CB  
3393  C CG  . GLU A 460  ? 0.4887 0.4721 0.5967 0.0075  -0.0252 -0.0446 458  GLU A CG  
3394  C CD  . GLU A 460  ? 0.6209 0.6096 0.7241 0.0086  -0.0248 -0.0502 458  GLU A CD  
3395  O OE1 . GLU A 460  ? 0.6453 0.6331 0.7525 0.0097  -0.0258 -0.0527 458  GLU A OE1 
3396  O OE2 . GLU A 460  ? 0.6387 0.6328 0.7343 0.0084  -0.0235 -0.0519 458  GLU A OE2 
3397  N N   . GLU A 461  ? 0.3147 0.2796 0.4529 0.0059  -0.0301 -0.0299 459  GLU A N   
3398  C CA  . GLU A 461  ? 0.3524 0.3135 0.5035 0.0055  -0.0332 -0.0280 459  GLU A CA  
3399  C C   . GLU A 461  ? 0.3381 0.2973 0.4902 0.0038  -0.0323 -0.0209 459  GLU A C   
3400  O O   . GLU A 461  ? 0.3260 0.2822 0.4886 0.0030  -0.0347 -0.0179 459  GLU A O   
3401  C CB  . GLU A 461  ? 0.3089 0.2668 0.4648 0.0059  -0.0340 -0.0255 459  GLU A CB  
3402  C CG  . GLU A 461  ? 0.3387 0.2984 0.4933 0.0076  -0.0346 -0.0321 459  GLU A CG  
3403  C CD  . GLU A 461  ? 0.4053 0.3669 0.5681 0.0088  -0.0383 -0.0409 459  GLU A CD  
3404  O OE1 . GLU A 461  ? 0.4057 0.3654 0.5789 0.0083  -0.0413 -0.0413 459  GLU A OE1 
3405  O OE2 . GLU A 461  ? 0.4115 0.3770 0.5709 0.0102  -0.0383 -0.0476 459  GLU A OE2 
3406  N N   . VAL A 462  ? 0.3195 0.2808 0.4614 0.0032  -0.0291 -0.0182 460  VAL A N   
3407  C CA  . VAL A 462  ? 0.2716 0.2317 0.4129 0.0017  -0.0277 -0.0113 460  VAL A CA  
3408  C C   . VAL A 462  ? 0.3022 0.2650 0.4409 0.0013  -0.0276 -0.0136 460  VAL A C   
3409  O O   . VAL A 462  ? 0.3097 0.2717 0.4553 0.0004  -0.0292 -0.0119 460  VAL A O   
3410  C CB  . VAL A 462  ? 0.3059 0.2659 0.4378 0.0014  -0.0239 -0.0051 460  VAL A CB  
3411  C CG1 . VAL A 462  ? 0.2782 0.2381 0.4092 0.0001  -0.0223 0.0013  460  VAL A CG1 
3412  C CG2 . VAL A 462  ? 0.2961 0.2536 0.4312 0.0017  -0.0241 -0.0023 460  VAL A CG2 
3413  N N   . VAL A 463  ? 0.2986 0.2649 0.4278 0.0019  -0.0259 -0.0173 461  VAL A N   
3414  C CA  . VAL A 463  ? 0.3044 0.2736 0.4300 0.0015  -0.0256 -0.0190 461  VAL A CA  
3415  C C   . VAL A 463  ? 0.3728 0.3434 0.5068 0.0019  -0.0293 -0.0254 461  VAL A C   
3416  O O   . VAL A 463  ? 0.3882 0.3595 0.5264 0.0030  -0.0315 -0.0312 461  VAL A O   
3417  C CB  . VAL A 463  ? 0.2962 0.2691 0.4098 0.0020  -0.0230 -0.0209 461  VAL A CB  
3418  C CG1 . VAL A 463  ? 0.3280 0.3044 0.4380 0.0016  -0.0230 -0.0229 461  VAL A CG1 
3419  C CG2 . VAL A 463  ? 0.2907 0.2621 0.3965 0.0017  -0.0196 -0.0148 461  VAL A CG2 
3420  N N   . GLY A 464  ? 0.3461 0.3175 0.4827 0.0011  -0.0301 -0.0248 462  GLY A N   
3421  C CA  . GLY A 464  ? 0.4268 0.4002 0.5702 0.0015  -0.0335 -0.0314 462  GLY A CA  
3422  C C   . GLY A 464  ? 0.4085 0.3784 0.5653 0.0008  -0.0367 -0.0300 462  GLY A C   
3423  O O   . GLY A 464  ? 0.3893 0.3552 0.5519 0.0004  -0.0372 -0.0258 462  GLY A O   
3424  N N   . ARG A 465  ? 0.3753 0.3470 0.5373 0.0006  -0.0391 -0.0336 463  ARG A N   
3425  C CA  . ARG A 465  ? 0.4359 0.4044 0.6111 -0.0002 -0.0424 -0.0323 463  ARG A CA  
3426  C C   . ARG A 465  ? 0.4316 0.3973 0.6176 0.0006  -0.0458 -0.0357 463  ARG A C   
3427  O O   . ARG A 465  ? 0.4916 0.4533 0.6884 -0.0003 -0.0479 -0.0319 463  ARG A O   
3428  C CB  . ARG A 465  ? 0.4229 0.3943 0.6012 -0.0004 -0.0446 -0.0367 463  ARG A CB  
3429  N N   . GLY A 466  ? 0.3702 0.3383 0.5541 0.0022  -0.0465 -0.0425 464  GLY A N   
3430  C CA  . GLY A 466  ? 0.4035 0.3691 0.5975 0.0032  -0.0497 -0.0461 464  GLY A CA  
3431  C C   . GLY A 466  ? 0.4453 0.4071 0.6387 0.0031  -0.0481 -0.0404 464  GLY A C   
3432  O O   . GLY A 466  ? 0.4495 0.4090 0.6516 0.0039  -0.0508 -0.0427 464  GLY A O   
3433  N N   . LYS A 467  ? 0.3709 0.3323 0.5545 0.0021  -0.0440 -0.0330 465  LYS A N   
3434  C CA  . LYS A 467  ? 0.3293 0.2877 0.5113 0.0019  -0.0422 -0.0272 465  LYS A CA  
3435  C C   . LYS A 467  ? 0.3543 0.3101 0.5387 0.0001  -0.0411 -0.0178 465  LYS A C   
3436  O O   . LYS A 467  ? 0.4095 0.3634 0.6049 -0.0009 -0.0440 -0.0164 465  LYS A O   
3437  C CB  . LYS A 467  ? 0.3486 0.3095 0.5172 0.0028  -0.0386 -0.0279 465  LYS A CB  
3438  C CG  . LYS A 467  ? 0.3628 0.3270 0.5298 0.0046  -0.0397 -0.0369 465  LYS A CG  
3439  C CD  . LYS A 467  ? 0.3968 0.3584 0.5743 0.0056  -0.0429 -0.0399 465  LYS A CD  
3440  C CE  . LYS A 467  ? 0.4228 0.3884 0.5972 0.0075  -0.0435 -0.0484 465  LYS A CE  
3441  N NZ  . LYS A 467  ? 0.3852 0.3484 0.5699 0.0087  -0.0466 -0.0515 465  LYS A NZ  
3442  N N   . LEU A 468  ? 0.3327 0.2888 0.5073 -0.0005 -0.0371 -0.0116 466  LEU A N   
3443  C CA  . LEU A 468  ? 0.3513 0.3063 0.5266 -0.0021 -0.0355 -0.0029 466  LEU A CA  
3444  C C   . LEU A 468  ? 0.3306 0.2880 0.4996 -0.0028 -0.0336 -0.0018 466  LEU A C   
3445  O O   . LEU A 468  ? 0.3305 0.2877 0.5006 -0.0041 -0.0324 0.0049  466  LEU A O   
3446  C CB  . LEU A 468  ? 0.3463 0.3007 0.5148 -0.0021 -0.0324 0.0030  466  LEU A CB  
3447  C CG  . LEU A 468  ? 0.3282 0.2802 0.5018 -0.0014 -0.0339 0.0025  466  LEU A CG  
3448  C CD1 . LEU A 468  ? 0.3449 0.2966 0.5127 -0.0018 -0.0310 0.0095  466  LEU A CD1 
3449  C CD2 . LEU A 468  ? 0.4052 0.3543 0.5944 -0.0020 -0.0384 0.0028  466  LEU A CD2 
3450  N N   . ASP A 469  ? 0.3458 0.3061 0.5084 -0.0019 -0.0332 -0.0080 467  ASP A N   
3451  C CA  . ASP A 469  ? 0.3253 0.2881 0.4823 -0.0025 -0.0317 -0.0075 467  ASP A CA  
3452  C C   . ASP A 469  ? 0.3085 0.2719 0.4566 -0.0031 -0.0277 -0.0006 467  ASP A C   
3453  O O   . ASP A 469  ? 0.2833 0.2472 0.4318 -0.0041 -0.0268 0.0036  467  ASP A O   
3454  C CB  . ASP A 469  ? 0.3518 0.3142 0.5190 -0.0034 -0.0346 -0.0076 467  ASP A CB  
3455  C CG  . ASP A 469  ? 0.3648 0.3305 0.5271 -0.0035 -0.0341 -0.0103 467  ASP A CG  
3456  O OD1 . ASP A 469  ? 0.3929 0.3615 0.5455 -0.0027 -0.0324 -0.0139 467  ASP A OD1 
3457  O OD2 . ASP A 469  ? 0.4307 0.3963 0.5990 -0.0046 -0.0354 -0.0085 467  ASP A OD2 
3458  N N   . ARG A 470  ? 0.3168 0.2800 0.4572 -0.0024 -0.0253 0.0005  468  ARG A N   
3459  C CA  . ARG A 470  ? 0.2814 0.2454 0.4124 -0.0026 -0.0215 0.0057  468  ARG A CA  
3460  C C   . ARG A 470  ? 0.2714 0.2375 0.3912 -0.0016 -0.0194 0.0022  468  ARG A C   
3461  O O   . ARG A 470  ? 0.2733 0.2396 0.3922 -0.0007 -0.0202 -0.0025 468  ARG A O   
3462  C CB  . ARG A 470  ? 0.2735 0.2357 0.4059 -0.0028 -0.0204 0.0116  468  ARG A CB  
3463  C CG  . ARG A 470  ? 0.2433 0.2039 0.3868 -0.0040 -0.0222 0.0166  468  ARG A CG  
3464  C CD  . ARG A 470  ? 0.2500 0.2123 0.3933 -0.0051 -0.0211 0.0207  468  ARG A CD  
3465  N NE  . ARG A 470  ? 0.2939 0.2553 0.4484 -0.0064 -0.0230 0.0256  468  ARG A NE  
3466  C CZ  . ARG A 470  ? 0.2964 0.2570 0.4609 -0.0072 -0.0262 0.0238  468  ARG A CZ  
3467  N NH1 . ARG A 470  ? 0.3046 0.2655 0.4690 -0.0066 -0.0279 0.0170  468  ARG A NH1 
3468  N NH2 . ARG A 470  ? 0.3298 0.2895 0.5046 -0.0086 -0.0279 0.0291  468  ARG A NH2 
3469  N N   . PRO A 471  ? 0.2467 0.2146 0.3584 -0.0017 -0.0169 0.0042  469  PRO A N   
3470  C CA  . PRO A 471  ? 0.2416 0.2117 0.3432 -0.0010 -0.0152 0.0012  469  PRO A CA  
3471  C C   . PRO A 471  ? 0.2459 0.2151 0.3415 -0.0005 -0.0130 0.0033  469  PRO A C   
3472  O O   . PRO A 471  ? 0.2254 0.1929 0.3223 -0.0007 -0.0119 0.0082  469  PRO A O   
3473  C CB  . PRO A 471  ? 0.2690 0.2407 0.3656 -0.0015 -0.0135 0.0037  469  PRO A CB  
3474  C CG  . PRO A 471  ? 0.2844 0.2547 0.3855 -0.0022 -0.0129 0.0097  469  PRO A CG  
3475  C CD  . PRO A 471  ? 0.2517 0.2201 0.3637 -0.0026 -0.0157 0.0092  469  PRO A CD  
3476  N N   . CYS A 472  ? 0.2240 0.1948 0.3129 0.0002  -0.0123 -0.0004 470  CYS A N   
3477  C CA  . CYS A 472  ? 0.2488 0.2191 0.3314 0.0008  -0.0102 0.0010  470  CYS A CA  
3478  C C   . CYS A 472  ? 0.2261 0.1988 0.2993 0.0009  -0.0085 -0.0003 470  CYS A C   
3479  O O   . CYS A 472  ? 0.2402 0.2156 0.3122 0.0010  -0.0096 -0.0047 470  CYS A O   
3480  C CB  . CYS A 472  ? 0.2398 0.2093 0.3254 0.0015  -0.0116 -0.0025 470  CYS A CB  
3481  S SG  . CYS A 472  ? 0.2562 0.2250 0.3347 0.0021  -0.0093 -0.0006 470  CYS A SG  
3482  N N   . ARG A 473  ? 0.2032 0.1754 0.2701 0.0010  -0.0061 0.0035  471  ARG A N   
3483  C CA  . ARG A 473  ? 0.2081 0.1822 0.2666 0.0011  -0.0046 0.0028  471  ARG A CA  
3484  C C   . ARG A 473  ? 0.2201 0.1941 0.2745 0.0017  -0.0038 0.0015  471  ARG A C   
3485  O O   . ARG A 473  ? 0.2289 0.2008 0.2836 0.0020  -0.0029 0.0041  471  ARG A O   
3486  C CB  . ARG A 473  ? 0.2212 0.1948 0.2758 0.0010  -0.0026 0.0073  471  ARG A CB  
3487  C CG  . ARG A 473  ? 0.2149 0.1903 0.2619 0.0009  -0.0015 0.0068  471  ARG A CG  
3488  C CD  . ARG A 473  ? 0.2174 0.1924 0.2618 0.0010  0.0001  0.0107  471  ARG A CD  
3489  N NE  . ARG A 473  ? 0.2155 0.1906 0.2648 0.0005  -0.0006 0.0121  471  ARG A NE  
3490  C CZ  . ARG A 473  ? 0.2279 0.2047 0.2779 0.0001  -0.0016 0.0107  471  ARG A CZ  
3491  N NH1 . ARG A 473  ? 0.2273 0.2062 0.2729 -0.0001 -0.0019 0.0084  471  ARG A NH1 
3492  N NH2 . ARG A 473  ? 0.2371 0.2138 0.2926 -0.0003 -0.0024 0.0119  471  ARG A NH2 
3493  N N   . ILE A 474  ? 0.1986 0.1753 0.2492 0.0017  -0.0041 -0.0022 472  ILE A N   
3494  C CA  . ILE A 474  ? 0.2050 0.1823 0.2520 0.0022  -0.0035 -0.0038 472  ILE A CA  
3495  C C   . ILE A 474  ? 0.2161 0.1935 0.2554 0.0021  -0.0014 -0.0011 472  ILE A C   
3496  O O   . ILE A 474  ? 0.2211 0.2006 0.2566 0.0016  -0.0011 -0.0011 472  ILE A O   
3497  C CB  . ILE A 474  ? 0.2126 0.1936 0.2597 0.0023  -0.0050 -0.0094 472  ILE A CB  
3498  C CG1 . ILE A 474  ? 0.2416 0.2222 0.2972 0.0027  -0.0074 -0.0126 472  ILE A CG1 
3499  C CG2 . ILE A 474  ? 0.2281 0.2104 0.2710 0.0028  -0.0042 -0.0108 472  ILE A CG2 
3500  C CD1 . ILE A 474  ? 0.2512 0.2365 0.3076 0.0029  -0.0091 -0.0186 472  ILE A CD1 
3501  N N   . TYR A 475  ? 0.2111 0.1864 0.2484 0.0025  -0.0001 0.0010  473  TYR A N   
3502  C CA  . TYR A 475  ? 0.2181 0.1934 0.2487 0.0025  0.0016  0.0031  473  TYR A CA  
3503  C C   . TYR A 475  ? 0.2115 0.1895 0.2384 0.0024  0.0014  0.0000  473  TYR A C   
3504  O O   . TYR A 475  ? 0.2214 0.1995 0.2496 0.0029  0.0010  -0.0022 473  TYR A O   
3505  C CB  . TYR A 475  ? 0.2340 0.2066 0.2643 0.0031  0.0029  0.0062  473  TYR A CB  
3506  C CG  . TYR A 475  ? 0.2422 0.2145 0.2664 0.0033  0.0045  0.0084  473  TYR A CG  
3507  C CD1 . TYR A 475  ? 0.2942 0.2669 0.3143 0.0034  0.0050  0.0073  473  TYR A CD1 
3508  C CD2 . TYR A 475  ? 0.2311 0.2027 0.2541 0.0034  0.0055  0.0114  473  TYR A CD2 
3509  C CE1 . TYR A 475  ? 0.3100 0.2822 0.3253 0.0036  0.0062  0.0091  473  TYR A CE1 
3510  C CE2 . TYR A 475  ? 0.2449 0.2161 0.2631 0.0037  0.0068  0.0130  473  TYR A CE2 
3511  C CZ  . TYR A 475  ? 0.3160 0.2874 0.3305 0.0038  0.0070  0.0118  473  TYR A CZ  
3512  O OH  . TYR A 475  ? 0.3110 0.2818 0.3213 0.0041  0.0080  0.0131  473  TYR A OH  
3513  N N   . ALA A 476  ? 0.2172 0.1976 0.2398 0.0018  0.0016  -0.0002 474  ALA A N   
3514  C CA  . ALA A 476  ? 0.2052 0.1897 0.2251 0.0015  0.0011  -0.0032 474  ALA A CA  
3515  C C   . ALA A 476  ? 0.2119 0.1967 0.2260 0.0011  0.0023  -0.0012 474  ALA A C   
3516  O O   . ALA A 476  ? 0.2198 0.2053 0.2311 0.0005  0.0026  0.0009  474  ALA A O   
3517  C CB  . ALA A 476  ? 0.2460 0.2342 0.2665 0.0008  -0.0001 -0.0050 474  ALA A CB  
3518  N N   . PRO A 477  ? 0.2251 0.2095 0.2376 0.0015  0.0029  -0.0017 475  PRO A N   
3519  C CA  . PRO A 477  ? 0.2402 0.2251 0.2475 0.0010  0.0038  0.0000  475  PRO A CA  
3520  C C   . PRO A 477  ? 0.2122 0.2024 0.2170 0.0000  0.0032  -0.0013 475  PRO A C   
3521  O O   . PRO A 477  ? 0.2258 0.2198 0.2320 -0.0001 0.0023  -0.0047 475  PRO A O   
3522  C CB  . PRO A 477  ? 0.2254 0.2093 0.2325 0.0016  0.0043  -0.0010 475  PRO A CB  
3523  C CG  . PRO A 477  ? 0.2894 0.2710 0.3017 0.0025  0.0038  -0.0020 475  PRO A CG  
3524  C CD  . PRO A 477  ? 0.2416 0.2251 0.2573 0.0022  0.0026  -0.0039 475  PRO A CD  
3525  N N   . VAL A 478  ? 0.2072 0.1978 0.2084 -0.0008 0.0036  0.0014  476  VAL A N   
3526  C CA  . VAL A 478  ? 0.2343 0.2300 0.2330 -0.0020 0.0030  0.0013  476  VAL A CA  
3527  C C   . VAL A 478  ? 0.2644 0.2601 0.2596 -0.0026 0.0035  0.0035  476  VAL A C   
3528  O O   . VAL A 478  ? 0.2940 0.2856 0.2883 -0.0024 0.0041  0.0063  476  VAL A O   
3529  C CB  . VAL A 478  ? 0.2317 0.2279 0.2308 -0.0026 0.0023  0.0031  476  VAL A CB  
3530  C CG1 . VAL A 478  ? 0.2461 0.2481 0.2425 -0.0040 0.0016  0.0037  476  VAL A CG1 
3531  C CG2 . VAL A 478  ? 0.2466 0.2425 0.2496 -0.0020 0.0017  0.0010  476  VAL A CG2 
3532  N N   . GLY A 479  ? 0.2552 0.2556 0.2484 -0.0032 0.0034  0.0021  477  GLY A N   
3533  C CA  . GLY A 479  ? 0.2831 0.2838 0.2735 -0.0040 0.0037  0.0046  477  GLY A CA  
3534  C C   . GLY A 479  ? 0.2711 0.2770 0.2600 -0.0045 0.0038  0.0026  477  GLY A C   
3535  O O   . GLY A 479  ? 0.2726 0.2817 0.2628 -0.0040 0.0036  -0.0011 477  GLY A O   
3536  N N   . THR A 480  ? 0.3329 0.3397 0.3194 -0.0055 0.0040  0.0050  478  THR A N   
3537  C CA  . THR A 480  ? 0.3229 0.3352 0.3078 -0.0062 0.0041  0.0039  478  THR A CA  
3538  C C   . THR A 480  ? 0.3999 0.4094 0.3854 -0.0050 0.0049  0.0017  478  THR A C   
3539  O O   . THR A 480  ? 0.3651 0.3685 0.3521 -0.0037 0.0053  0.0015  478  THR A O   
3540  C CB  . THR A 480  ? 0.3716 0.3854 0.3544 -0.0079 0.0038  0.0079  478  THR A CB  
3541  O OG1 . THR A 480  ? 0.4429 0.4497 0.4258 -0.0073 0.0041  0.0100  478  THR A OG1 
3542  C CG2 . THR A 480  ? 0.3877 0.4043 0.3702 -0.0092 0.0028  0.0106  478  THR A CG2 
3543  N N   . HIS A 481  ? 0.4235 0.4380 0.4079 -0.0054 0.0050  0.0002  479  HIS A N   
3544  C CA  . HIS A 481  ? 0.4724 0.4849 0.4575 -0.0043 0.0057  -0.0019 479  HIS A CA  
3545  C C   . HIS A 481  ? 0.4885 0.4945 0.4728 -0.0041 0.0062  0.0011  479  HIS A C   
3546  O O   . HIS A 481  ? 0.4322 0.4334 0.4180 -0.0027 0.0066  0.0002  479  HIS A O   
3547  C CB  . HIS A 481  ? 0.4190 0.4386 0.4028 -0.0050 0.0058  -0.0036 479  HIS A CB  
3548  C CG  . HIS A 481  ? 0.4366 0.4634 0.4213 -0.0048 0.0053  -0.0074 479  HIS A CG  
3549  N ND1 . HIS A 481  ? 0.4212 0.4558 0.4050 -0.0051 0.0054  -0.0098 479  HIS A ND1 
3550  C CD2 . HIS A 481  ? 0.4455 0.4731 0.4321 -0.0042 0.0047  -0.0096 479  HIS A CD2 
3551  C CE1 . HIS A 481  ? 0.4490 0.4892 0.4341 -0.0047 0.0048  -0.0135 479  HIS A CE1 
3552  N NE2 . HIS A 481  ? 0.4393 0.4752 0.4261 -0.0042 0.0043  -0.0135 479  HIS A NE2 
3553  N N   . GLU A 482  ? 0.5258 0.5321 0.5084 -0.0054 0.0059  0.0046  480  GLU A N   
3554  C CA  . GLU A 482  ? 0.5818 0.5823 0.5639 -0.0052 0.0061  0.0070  480  GLU A CA  
3555  C C   . GLU A 482  ? 0.5302 0.5244 0.5137 -0.0038 0.0064  0.0073  480  GLU A C   
3556  O O   . GLU A 482  ? 0.5242 0.5140 0.5080 -0.0027 0.0069  0.0072  480  GLU A O   
3557  C CB  . GLU A 482  ? 0.5638 0.5654 0.5448 -0.0069 0.0054  0.0107  480  GLU A CB  
3558  N N   . THR A 483  ? 0.4712 0.4655 0.4556 -0.0039 0.0060  0.0077  481  THR A N   
3559  C CA  . THR A 483  ? 0.4658 0.4549 0.4517 -0.0027 0.0062  0.0083  481  THR A CA  
3560  C C   . THR A 483  ? 0.4758 0.4628 0.4635 -0.0012 0.0068  0.0059  481  THR A C   
3561  O O   . THR A 483  ? 0.4447 0.4274 0.4332 -0.0001 0.0073  0.0065  481  THR A O   
3562  C CB  . THR A 483  ? 0.4089 0.3990 0.3954 -0.0033 0.0056  0.0093  481  THR A CB  
3563  O OG1 . THR A 483  ? 0.5217 0.5136 0.5070 -0.0047 0.0048  0.0121  481  THR A OG1 
3564  C CG2 . THR A 483  ? 0.5222 0.5074 0.5103 -0.0021 0.0059  0.0101  481  THR A CG2 
3565  N N   . LEU A 484  ? 0.4203 0.4109 0.4093 -0.0012 0.0066  0.0030  482  LEU A N   
3566  C CA  . LEU A 484  ? 0.4036 0.3921 0.3954 0.0002  0.0067  0.0009  482  LEU A CA  
3567  C C   . LEU A 484  ? 0.4151 0.4016 0.4069 0.0010  0.0073  0.0004  482  LEU A C   
3568  O O   . LEU A 484  ? 0.4172 0.4003 0.4110 0.0021  0.0075  0.0004  482  LEU A O   
3569  C CB  . LEU A 484  ? 0.4067 0.3994 0.4006 0.0002  0.0060  -0.0025 482  LEU A CB  
3570  C CG  . LEU A 484  ? 0.4141 0.4124 0.4071 -0.0003 0.0058  -0.0051 482  LEU A CG  
3571  C CD1 . LEU A 484  ? 0.4230 0.4203 0.4184 0.0010  0.0059  -0.0079 482  LEU A CD1 
3572  C CD2 . LEU A 484  ? 0.4559 0.4601 0.4494 -0.0008 0.0050  -0.0074 482  LEU A CD2 
3573  N N   . LEU A 485  ? 0.4589 0.4479 0.4485 0.0004  0.0074  0.0001  483  LEU A N   
3574  C CA  . LEU A 485  ? 0.3698 0.3573 0.3594 0.0011  0.0078  -0.0005 483  LEU A CA  
3575  C C   . LEU A 485  ? 0.4424 0.4250 0.4311 0.0017  0.0083  0.0021  483  LEU A C   
3576  O O   . LEU A 485  ? 0.4503 0.4309 0.4396 0.0027  0.0087  0.0017  483  LEU A O   
3577  C CB  . LEU A 485  ? 0.4023 0.3940 0.3899 0.0002  0.0078  -0.0012 483  LEU A CB  
3578  C CG  . LEU A 485  ? 0.4314 0.4290 0.4200 0.0000  0.0074  -0.0045 483  LEU A CG  
3579  C CD1 . LEU A 485  ? 0.4305 0.4332 0.4167 -0.0012 0.0075  -0.0043 483  LEU A CD1 
3580  C CD2 . LEU A 485  ? 0.4181 0.4149 0.4099 0.0015  0.0072  -0.0077 483  LEU A CD2 
3581  N N   . ALA A 486  ? 0.4708 0.4518 0.4582 0.0013  0.0083  0.0044  484  ALA A N   
3582  C CA  . ALA A 486  ? 0.4790 0.4563 0.4654 0.0019  0.0087  0.0064  484  ALA A CA  
3583  C C   . ALA A 486  ? 0.5096 0.4840 0.4977 0.0034  0.0092  0.0064  484  ALA A C   
3584  O O   . ALA A 486  ? 0.4758 0.4486 0.4631 0.0041  0.0096  0.0067  484  ALA A O   
3585  C CB  . ALA A 486  ? 0.4782 0.4544 0.4640 0.0014  0.0084  0.0085  484  ALA A CB  
3586  N N   . TYR A 487  ? 0.4837 0.4577 0.4742 0.0037  0.0092  0.0061  485  TYR A N   
3587  C CA  . TYR A 487  ? 0.4756 0.4474 0.4682 0.0049  0.0096  0.0067  485  TYR A CA  
3588  C C   . TYR A 487  ? 0.4644 0.4370 0.4606 0.0051  0.0091  0.0050  485  TYR A C   
3589  O O   . TYR A 487  ? 0.3911 0.3622 0.3902 0.0057  0.0091  0.0059  485  TYR A O   
3590  C CB  . TYR A 487  ? 0.5232 0.4933 0.5161 0.0053  0.0099  0.0088  485  TYR A CB  
3591  C CG  . TYR A 487  ? 0.5803 0.5495 0.5704 0.0054  0.0102  0.0100  485  TYR A CG  
3592  C CD1 . TYR A 487  ? 0.5912 0.5592 0.5800 0.0063  0.0107  0.0106  485  TYR A CD1 
3593  C CD2 . TYR A 487  ? 0.5678 0.5375 0.5568 0.0045  0.0097  0.0105  485  TYR A CD2 
3594  C CE1 . TYR A 487  ? 0.6610 0.6282 0.6479 0.0065  0.0106  0.0112  485  TYR A CE1 
3595  C CE2 . TYR A 487  ? 0.5942 0.5628 0.5816 0.0046  0.0096  0.0115  485  TYR A CE2 
3596  C CZ  . TYR A 487  ? 0.7158 0.6831 0.7023 0.0056  0.0100  0.0116  485  TYR A CZ  
3597  O OH  . TYR A 487  ? 0.7325 0.6988 0.7179 0.0059  0.0096  0.0121  485  TYR A OH  
3598  N N   . LEU A 488  ? 0.4259 0.4010 0.4225 0.0047  0.0086  0.0025  486  LEU A N   
3599  C CA  . LEU A 488  ? 0.3940 0.3699 0.3946 0.0051  0.0078  0.0002  486  LEU A CA  
3600  C C   . LEU A 488  ? 0.3762 0.3501 0.3794 0.0061  0.0078  0.0006  486  LEU A C   
3601  O O   . LEU A 488  ? 0.3655 0.3386 0.3732 0.0066  0.0071  0.0000  486  LEU A O   
3602  C CB  . LEU A 488  ? 0.3716 0.3516 0.3718 0.0045  0.0073  -0.0029 486  LEU A CB  
3603  C CG  . LEU A 488  ? 0.4324 0.4139 0.4373 0.0051  0.0062  -0.0062 486  LEU A CG  
3604  C CD1 . LEU A 488  ? 0.4322 0.4125 0.4400 0.0050  0.0057  -0.0057 486  LEU A CD1 
3605  C CD2 . LEU A 488  ? 0.4039 0.3907 0.4080 0.0046  0.0058  -0.0096 486  LEU A CD2 
3606  N N   . VAL A 489  ? 0.4327 0.4057 0.4333 0.0064  0.0084  0.0018  487  VAL A N   
3607  C CA  . VAL A 489  ? 0.3568 0.3281 0.3596 0.0073  0.0084  0.0026  487  VAL A CA  
3608  C C   . VAL A 489  ? 0.3722 0.3414 0.3776 0.0078  0.0084  0.0052  487  VAL A C   
3609  O O   . VAL A 489  ? 0.3618 0.3303 0.3718 0.0082  0.0077  0.0054  487  VAL A O   
3610  C CB  . VAL A 489  ? 0.3722 0.3432 0.3715 0.0076  0.0090  0.0035  487  VAL A CB  
3611  C CG1 . VAL A 489  ? 0.4242 0.3936 0.4254 0.0085  0.0090  0.0052  487  VAL A CG1 
3612  C CG2 . VAL A 489  ? 0.3602 0.3335 0.3582 0.0072  0.0088  0.0009  487  VAL A CG2 
3613  N N   . ARG A 490  ? 0.4278 0.3964 0.4308 0.0076  0.0092  0.0073  488  ARG A N   
3614  C CA  . ARG A 490  ? 0.4357 0.4032 0.4410 0.0080  0.0095  0.0100  488  ARG A CA  
3615  C C   . ARG A 490  ? 0.4425 0.4100 0.4527 0.0077  0.0085  0.0092  488  ARG A C   
3616  O O   . ARG A 490  ? 0.4071 0.3738 0.4216 0.0080  0.0081  0.0109  488  ARG A O   
3617  C CB  . ARG A 490  ? 0.4456 0.4130 0.4476 0.0080  0.0104  0.0117  488  ARG A CB  
3618  C CG  . ARG A 490  ? 0.4404 0.4076 0.4444 0.0085  0.0109  0.0146  488  ARG A CG  
3619  C CD  . ARG A 490  ? 0.4742 0.4416 0.4755 0.0086  0.0117  0.0157  488  ARG A CD  
3620  N NE  . ARG A 490  ? 0.4855 0.4529 0.4870 0.0078  0.0113  0.0146  488  ARG A NE  
3621  C CZ  . ARG A 490  ? 0.4715 0.4390 0.4700 0.0076  0.0114  0.0140  488  ARG A CZ  
3622  N NH1 . ARG A 490  ? 0.4540 0.4213 0.4493 0.0080  0.0118  0.0141  488  ARG A NH1 
3623  N NH2 . ARG A 490  ? 0.4246 0.3924 0.4237 0.0068  0.0109  0.0133  488  ARG A NH2 
3624  N N   . ARG A 491  ? 0.4172 0.3858 0.4271 0.0070  0.0080  0.0068  489  ARG A N   
3625  C CA  . ARG A 491  ? 0.4938 0.4627 0.5084 0.0068  0.0069  0.0056  489  ARG A CA  
3626  C C   . ARG A 491  ? 0.5656 0.5343 0.5854 0.0072  0.0056  0.0038  489  ARG A C   
3627  O O   . ARG A 491  ? 0.5430 0.5108 0.5683 0.0072  0.0046  0.0043  489  ARG A O   
3628  C CB  . ARG A 491  ? 0.5246 0.4956 0.5372 0.0060  0.0066  0.0033  489  ARG A CB  
3629  N N   . LEU A 492  ? 0.5148 0.4843 0.5335 0.0075  0.0055  0.0018  490  LEU A N   
3630  C CA  . LEU A 492  ? 0.5066 0.4760 0.5308 0.0080  0.0041  -0.0004 490  LEU A CA  
3631  C C   . LEU A 492  ? 0.5309 0.4980 0.5588 0.0086  0.0038  0.0028  490  LEU A C   
3632  O O   . LEU A 492  ? 0.4555 0.4217 0.4901 0.0088  0.0022  0.0024  490  LEU A O   
3633  C CB  . LEU A 492  ? 0.4462 0.4177 0.4681 0.0083  0.0041  -0.0035 490  LEU A CB  
3634  C CG  . LEU A 492  ? 0.4686 0.4436 0.4877 0.0077  0.0041  -0.0068 490  LEU A CG  
3635  C CD1 . LEU A 492  ? 0.4675 0.4448 0.4832 0.0077  0.0045  -0.0086 490  LEU A CD1 
3636  C CD2 . LEU A 492  ? 0.4849 0.4615 0.5093 0.0079  0.0025  -0.0105 490  LEU A CD2 
3637  N N   . LEU A 493  ? 0.4604 0.4268 0.4845 0.0087  0.0051  0.0061  491  LEU A N   
3638  C CA  . LEU A 493  ? 0.3724 0.3376 0.3995 0.0091  0.0049  0.0096  491  LEU A CA  
3639  C C   . LEU A 493  ? 0.4796 0.4439 0.5112 0.0088  0.0044  0.0123  491  LEU A C   
3640  O O   . LEU A 493  ? 0.5213 0.4850 0.5580 0.0089  0.0036  0.0149  491  LEU A O   
3641  C CB  . LEU A 493  ? 0.4848 0.4503 0.5063 0.0094  0.0065  0.0122  491  LEU A CB  
3642  C CG  . LEU A 493  ? 0.5240 0.4902 0.5414 0.0097  0.0069  0.0102  491  LEU A CG  
3643  C CD1 . LEU A 493  ? 0.5041 0.4706 0.5174 0.0101  0.0081  0.0129  491  LEU A CD1 
3644  C CD2 . LEU A 493  ? 0.5485 0.5145 0.5702 0.0101  0.0055  0.0080  491  LEU A CD2 
3645  N N   . ALA A 497  ? 0.5113 0.4730 0.5609 0.0102  -0.0006 0.0120  495  ALA A N   
3646  C CA  . ALA A 497  ? 0.4690 0.4305 0.5198 0.0104  -0.0006 0.0164  495  ALA A CA  
3647  C C   . ALA A 497  ? 0.4246 0.3846 0.4852 0.0104  -0.0031 0.0180  495  ALA A C   
3648  O O   . ALA A 497  ? 0.4202 0.3792 0.4867 0.0101  -0.0045 0.0169  495  ALA A O   
3649  C CB  . ALA A 497  ? 0.4116 0.3743 0.4580 0.0100  0.0013  0.0212  495  ALA A CB  
3650  N N   . ASN A 498  ? 0.4504 0.4103 0.5132 0.0108  -0.0037 0.0207  496  ASN A N   
3651  C CA  . ASN A 498  ? 0.4392 0.3975 0.5123 0.0108  -0.0064 0.0225  496  ASN A CA  
3652  C C   . ASN A 498  ? 0.4097 0.3677 0.4881 0.0098  -0.0071 0.0270  496  ASN A C   
3653  O O   . ASN A 498  ? 0.4432 0.3994 0.5310 0.0096  -0.0097 0.0269  496  ASN A O   
3654  C CB  . ASN A 498  ? 0.5079 0.4666 0.5820 0.0112  -0.0069 0.0257  496  ASN A CB  
3655  C CG  . ASN A 498  ? 0.6515 0.6101 0.7235 0.0122  -0.0071 0.0210  496  ASN A CG  
3656  O OD1 . ASN A 498  ? 0.6606 0.6188 0.7337 0.0126  -0.0078 0.0152  496  ASN A OD1 
3657  N ND2 . ASN A 498  ? 0.6839 0.6435 0.7530 0.0126  -0.0065 0.0233  496  ASN A ND2 
3658  N N   . SER A 499  ? 0.4025 0.3623 0.4754 0.0093  -0.0050 0.0307  497  SER A N   
3659  C CA  . SER A 499  ? 0.4220 0.3822 0.4996 0.0083  -0.0054 0.0353  497  SER A CA  
3660  C C   . SER A 499  ? 0.3299 0.2891 0.4083 0.0079  -0.0055 0.0321  497  SER A C   
3661  O O   . SER A 499  ? 0.3868 0.3461 0.4704 0.0070  -0.0062 0.0352  497  SER A O   
3662  C CB  . SER A 499  ? 0.4605 0.4240 0.5322 0.0080  -0.0030 0.0406  497  SER A CB  
3663  O OG  . SER A 499  ? 0.5093 0.4739 0.5710 0.0085  -0.0005 0.0378  497  SER A OG  
3664  N N   . SER A 500  ? 0.3381 0.2970 0.4119 0.0084  -0.0049 0.0262  498  SER A N   
3665  C CA  . SER A 500  ? 0.2994 0.2580 0.3730 0.0080  -0.0048 0.0232  498  SER A CA  
3666  C C   . SER A 500  ? 0.3776 0.3343 0.4612 0.0078  -0.0078 0.0208  498  SER A C   
3667  O O   . SER A 500  ? 0.3478 0.3034 0.4366 0.0085  -0.0098 0.0181  498  SER A O   
3668  C CB  . SER A 500  ? 0.3719 0.3313 0.4378 0.0085  -0.0034 0.0179  498  SER A CB  
3669  O OG  . SER A 500  ? 0.4123 0.3733 0.4694 0.0085  -0.0008 0.0199  498  SER A OG  
3670  N N   . PHE A 501  ? 0.3075 0.2641 0.3943 0.0071  -0.0083 0.0215  499  PHE A N   
3671  C CA  . PHE A 501  ? 0.3193 0.2741 0.4160 0.0070  -0.0113 0.0190  499  PHE A CA  
3672  C C   . PHE A 501  ? 0.3734 0.3281 0.4702 0.0079  -0.0124 0.0114  499  PHE A C   
3673  O O   . PHE A 501  ? 0.3681 0.3215 0.4734 0.0084  -0.0152 0.0085  499  PHE A O   
3674  C CB  . PHE A 501  ? 0.3088 0.2638 0.4074 0.0060  -0.0113 0.0204  499  PHE A CB  
3675  C CG  . PHE A 501  ? 0.2895 0.2428 0.3983 0.0059  -0.0145 0.0172  499  PHE A CG  
3676  C CD1 . PHE A 501  ? 0.2923 0.2439 0.4119 0.0053  -0.0171 0.0209  499  PHE A CD1 
3677  C CD2 . PHE A 501  ? 0.3527 0.3066 0.4606 0.0064  -0.0151 0.0104  499  PHE A CD2 
3678  C CE1 . PHE A 501  ? 0.3282 0.2781 0.4579 0.0052  -0.0203 0.0176  499  PHE A CE1 
3679  C CE2 . PHE A 501  ? 0.3223 0.2749 0.4397 0.0064  -0.0183 0.0069  499  PHE A CE2 
3680  C CZ  . PHE A 501  ? 0.3534 0.3038 0.4820 0.0059  -0.0209 0.0103  499  PHE A CZ  
3681  N N   . VAL A 502  ? 0.3651 0.3217 0.4531 0.0082  -0.0104 0.0080  500  VAL A N   
3682  C CA  . VAL A 502  ? 0.3954 0.3532 0.4830 0.0089  -0.0112 0.0008  500  VAL A CA  
3683  C C   . VAL A 502  ? 0.4150 0.3728 0.5037 0.0100  -0.0120 -0.0015 500  VAL A C   
3684  O O   . VAL A 502  ? 0.4959 0.4542 0.5894 0.0108  -0.0140 -0.0070 500  VAL A O   
3685  C CB  . VAL A 502  ? 0.4210 0.3813 0.4989 0.0087  -0.0089 -0.0013 500  VAL A CB  
3686  C CG1 . VAL A 502  ? 0.5455 0.5082 0.6221 0.0095  -0.0095 -0.0083 500  VAL A CG1 
3687  C CG2 . VAL A 502  ? 0.4253 0.3857 0.5035 0.0079  -0.0087 0.0001  500  VAL A CG2 
3688  N N   . HIS A 503  ? 0.3603 0.3177 0.4448 0.0100  -0.0105 0.0025  501  HIS A N   
3689  C CA  . HIS A 503  ? 0.3625 0.3196 0.4491 0.0109  -0.0114 0.0010  501  HIS A CA  
3690  C C   . HIS A 503  ? 0.4164 0.3712 0.5149 0.0112  -0.0146 0.0020  501  HIS A C   
3691  O O   . HIS A 503  ? 0.3746 0.3291 0.4787 0.0122  -0.0168 -0.0025 501  HIS A O   
3692  C CB  . HIS A 503  ? 0.3995 0.3570 0.4790 0.0109  -0.0092 0.0053  501  HIS A CB  
3693  C CG  . HIS A 503  ? 0.4772 0.4345 0.5584 0.0118  -0.0100 0.0043  501  HIS A CG  
3694  N ND1 . HIS A 503  ? 0.4592 0.4149 0.5465 0.0118  -0.0115 0.0085  501  HIS A ND1 
3695  C CD2 . HIS A 503  ? 0.4908 0.4497 0.5687 0.0126  -0.0097 -0.0003 501  HIS A CD2 
3696  C CE1 . HIS A 503  ? 0.4708 0.4268 0.5585 0.0128  -0.0120 0.0063  501  HIS A CE1 
3697  N NE2 . HIS A 503  ? 0.4587 0.4166 0.5407 0.0132  -0.0109 0.0009  501  HIS A NE2 
3698  N N   . ARG A 504  ? 0.3601 0.3134 0.4631 0.0102  -0.0152 0.0079  502  ARG A N   
3699  C CA  . ARG A 504  ? 0.3553 0.3062 0.4701 0.0102  -0.0184 0.0100  502  ARG A CA  
3700  C C   . ARG A 504  ? 0.3888 0.3386 0.5127 0.0106  -0.0215 0.0045  502  ARG A C   
3701  O O   . ARG A 504  ? 0.3924 0.3405 0.5258 0.0113  -0.0245 0.0026  502  ARG A O   
3702  C CB  . ARG A 504  ? 0.3709 0.3213 0.4879 0.0089  -0.0181 0.0182  502  ARG A CB  
3703  C CG  . ARG A 504  ? 0.3707 0.3225 0.4805 0.0088  -0.0157 0.0234  502  ARG A CG  
3704  C CD  . ARG A 504  ? 0.3761 0.3293 0.4847 0.0075  -0.0143 0.0307  502  ARG A CD  
3705  N NE  . ARG A 504  ? 0.4200 0.3717 0.5400 0.0066  -0.0171 0.0345  502  ARG A NE  
3706  C CZ  . ARG A 504  ? 0.4589 0.4098 0.5868 0.0063  -0.0192 0.0389  502  ARG A CZ  
3707  N NH1 . ARG A 504  ? 0.4821 0.4334 0.6080 0.0070  -0.0191 0.0397  502  ARG A NH1 
3708  N NH2 . ARG A 504  ? 0.4475 0.3973 0.5860 0.0052  -0.0217 0.0429  502  ARG A NH2 
3709  N N   . ILE A 505  ? 0.4004 0.3512 0.5218 0.0102  -0.0208 0.0017  503  ILE A N   
3710  C CA  . ILE A 505  ? 0.3991 0.3495 0.5288 0.0107  -0.0237 -0.0041 503  ILE A CA  
3711  C C   . ILE A 505  ? 0.4394 0.3911 0.5706 0.0123  -0.0251 -0.0116 503  ILE A C   
3712  O O   . ILE A 505  ? 0.4743 0.4250 0.6158 0.0131  -0.0285 -0.0159 503  ILE A O   
3713  C CB  . ILE A 505  ? 0.4529 0.4049 0.5784 0.0100  -0.0226 -0.0057 503  ILE A CB  
3714  C CG1 . ILE A 505  ? 0.5250 0.4764 0.6603 0.0104  -0.0259 -0.0109 503  ILE A CG1 
3715  C CG2 . ILE A 505  ? 0.4754 0.4306 0.5894 0.0105  -0.0198 -0.0097 503  ILE A CG2 
3716  C CD1 . ILE A 505  ? 0.4077 0.3563 0.5529 0.0093  -0.0281 -0.0061 503  ILE A CD1 
3717  N N   . ASN A 506  ? 0.3973 0.3513 0.5189 0.0129  -0.0226 -0.0133 504  ASN A N   
3718  C CA  . ASN A 506  ? 0.4515 0.4077 0.5735 0.0144  -0.0234 -0.0201 504  ASN A CA  
3719  C C   . ASN A 506  ? 0.4500 0.4044 0.5766 0.0152  -0.0247 -0.0189 504  ASN A C   
3720  O O   . ASN A 506  ? 0.5008 0.4570 0.6286 0.0166  -0.0255 -0.0245 504  ASN A O   
3721  C CB  . ASN A 506  ? 0.4711 0.4311 0.5806 0.0144  -0.0201 -0.0225 504  ASN A CB  
3722  C CG  . ASN A 506  ? 0.4807 0.4433 0.5864 0.0139  -0.0193 -0.0254 504  ASN A CG  
3723  O OD1 . ASN A 506  ? 0.5886 0.5512 0.7014 0.0142  -0.0216 -0.0289 504  ASN A OD1 
3724  N ND2 . ASN A 506  ? 0.5880 0.5527 0.6827 0.0133  -0.0162 -0.0241 504  ASN A ND2 
3725  N N   . ASP A 507  ? 0.4182 0.3698 0.5477 0.0144  -0.0249 -0.0116 505  ASP A N   
3726  C CA  . ASP A 507  ? 0.4281 0.3781 0.5622 0.0150  -0.0263 -0.0097 505  ASP A CA  
3727  C C   . ASP A 507  ? 0.5044 0.4515 0.6534 0.0155  -0.0307 -0.0105 505  ASP A C   
3728  O O   . ASP A 507  ? 0.4214 0.3662 0.5763 0.0143  -0.0319 -0.0053 505  ASP A O   
3729  C CB  . ASP A 507  ? 0.4302 0.3795 0.5594 0.0140  -0.0243 -0.0012 505  ASP A CB  
3730  C CG  . ASP A 507  ? 0.5081 0.4564 0.6407 0.0146  -0.0254 0.0010  505  ASP A CG  
3731  O OD1 . ASP A 507  ? 0.5546 0.5020 0.6956 0.0158  -0.0283 -0.0032 505  ASP A OD1 
3732  O OD2 . ASP A 507  ? 0.5068 0.4556 0.6336 0.0140  -0.0234 0.0068  505  ASP A OD2 
3733  N N   . PRO A 508  ? 0.5475 0.4948 0.7033 0.0171  -0.0332 -0.0167 506  PRO A N   
3734  C CA  . PRO A 508  ? 0.5433 0.4875 0.7143 0.0176  -0.0379 -0.0177 506  PRO A CA  
3735  C C   . PRO A 508  ? 0.5168 0.4577 0.6945 0.0167  -0.0394 -0.0094 506  PRO A C   
3736  O O   . PRO A 508  ? 0.6178 0.5558 0.8083 0.0165  -0.0431 -0.0078 506  PRO A O   
3737  C CB  . PRO A 508  ? 0.5626 0.5085 0.7376 0.0198  -0.0398 -0.0265 506  PRO A CB  
3738  C CG  . PRO A 508  ? 0.6336 0.5842 0.7952 0.0202  -0.0360 -0.0308 506  PRO A CG  
3739  C CD  . PRO A 508  ? 0.5277 0.4783 0.6780 0.0186  -0.0322 -0.0232 506  PRO A CD  
3740  N N   . LYS A 509  ? 0.4634 0.4051 0.6332 0.0163  -0.0368 -0.0041 507  LYS A N   
3741  C CA  . LYS A 509  ? 0.4485 0.3881 0.6234 0.0153  -0.0379 0.0045  507  LYS A CA  
3742  C C   . LYS A 509  ? 0.4816 0.4206 0.6568 0.0133  -0.0373 0.0121  507  LYS A C   
3743  O O   . LYS A 509  ? 0.5084 0.4461 0.6895 0.0123  -0.0386 0.0196  507  LYS A O   
3744  C CB  . LYS A 509  ? 0.5264 0.4676 0.6921 0.0156  -0.0353 0.0074  507  LYS A CB  
3745  N N   . VAL A 510  ? 0.4477 0.3879 0.6168 0.0127  -0.0352 0.0106  508  VAL A N   
3746  C CA  . VAL A 510  ? 0.4151 0.3552 0.5841 0.0108  -0.0344 0.0174  508  VAL A CA  
3747  C C   . VAL A 510  ? 0.3896 0.3275 0.5704 0.0105  -0.0378 0.0152  508  VAL A C   
3748  O O   . VAL A 510  ? 0.4115 0.3498 0.5921 0.0113  -0.0383 0.0077  508  VAL A O   
3749  C CB  . VAL A 510  ? 0.4232 0.3661 0.5781 0.0103  -0.0299 0.0177  508  VAL A CB  
3750  C CG1 . VAL A 510  ? 0.4027 0.3460 0.5580 0.0085  -0.0291 0.0244  508  VAL A CG1 
3751  C CG2 . VAL A 510  ? 0.3804 0.3254 0.5243 0.0107  -0.0268 0.0195  508  VAL A CG2 
3752  N N   . SER A 511  ? 0.3632 0.2991 0.5545 0.0093  -0.0404 0.0218  509  SER A N   
3753  C CA  . SER A 511  ? 0.3566 0.2901 0.5606 0.0088  -0.0441 0.0202  509  SER A CA  
3754  C C   . SER A 511  ? 0.3403 0.2750 0.5397 0.0075  -0.0422 0.0218  509  SER A C   
3755  O O   . SER A 511  ? 0.3895 0.3267 0.5779 0.0066  -0.0383 0.0263  509  SER A O   
3756  C CB  . SER A 511  ? 0.4480 0.3790 0.6658 0.0078  -0.0479 0.0274  509  SER A CB  
3757  O OG  . SER A 511  ? 0.4156 0.3483 0.6297 0.0058  -0.0458 0.0374  509  SER A OG  
3758  N N   . ILE A 512  ? 0.3615 0.2946 0.5700 0.0074  -0.0451 0.0179  510  ILE A N   
3759  C CA  . ILE A 512  ? 0.3657 0.2998 0.5720 0.0061  -0.0438 0.0198  510  ILE A CA  
3760  C C   . ILE A 512  ? 0.4242 0.3585 0.6331 0.0040  -0.0434 0.0306  510  ILE A C   
3761  O O   . ILE A 512  ? 0.3713 0.3079 0.5724 0.0028  -0.0403 0.0345  510  ILE A O   
3762  C CB  . ILE A 512  ? 0.3857 0.3180 0.6022 0.0065  -0.0475 0.0132  510  ILE A CB  
3763  C CG1 . ILE A 512  ? 0.4003 0.3340 0.6116 0.0086  -0.0471 0.0024  510  ILE A CG1 
3764  C CG2 . ILE A 512  ? 0.4116 0.3446 0.6274 0.0049  -0.0466 0.0159  510  ILE A CG2 
3765  C CD1 . ILE A 512  ? 0.4365 0.3694 0.6574 0.0094  -0.0506 -0.0052 510  ILE A CD1 
3766  N N   . ASP A 513  ? 0.3775 0.3099 0.5976 0.0034  -0.0466 0.0359  511  ASP A N   
3767  C CA  . ASP A 513  ? 0.3872 0.3209 0.6098 0.0013  -0.0461 0.0468  511  ASP A CA  
3768  C C   . ASP A 513  ? 0.4024 0.3400 0.6104 0.0011  -0.0412 0.0515  511  ASP A C   
3769  O O   . ASP A 513  ? 0.3942 0.3347 0.5984 -0.0004 -0.0390 0.0581  511  ASP A O   
3770  C CB  . ASP A 513  ? 0.4604 0.3956 0.6938 0.0004  -0.0496 0.0503  511  ASP A CB  
3771  C CG  . ASP A 513  ? 0.4868 0.4216 0.7333 -0.0001 -0.0541 0.0465  511  ASP A CG  
3772  O OD1 . ASP A 513  ? 0.5232 0.4582 0.7715 -0.0010 -0.0542 0.0462  511  ASP A OD1 
3773  O OD2 . ASP A 513  ? 0.6489 0.5832 0.9042 0.0004  -0.0575 0.0438  511  ASP A OD2 
3774  N N   . GLU A 514  ? 0.3501 0.2883 0.5501 0.0026  -0.0395 0.0480  512  GLU A N   
3775  C CA  . GLU A 514  ? 0.3895 0.3314 0.5752 0.0026  -0.0350 0.0513  512  GLU A CA  
3776  C C   . GLU A 514  ? 0.3971 0.3411 0.5718 0.0025  -0.0314 0.0485  512  GLU A C   
3777  O O   . GLU A 514  ? 0.3612 0.3086 0.5276 0.0018  -0.0282 0.0536  512  GLU A O   
3778  C CB  . GLU A 514  ? 0.4050 0.3468 0.5850 0.0043  -0.0342 0.0470  512  GLU A CB  
3779  C CG  . GLU A 514  ? 0.4854 0.4260 0.6738 0.0044  -0.0369 0.0511  512  GLU A CG  
3780  C CD  . GLU A 514  ? 0.5570 0.4971 0.7410 0.0062  -0.0366 0.0454  512  GLU A CD  
3781  O OE1 . GLU A 514  ? 0.5553 0.4930 0.7441 0.0076  -0.0388 0.0376  512  GLU A OE1 
3782  O OE2 . GLU A 514  ? 0.6139 0.5564 0.7895 0.0064  -0.0342 0.0486  512  GLU A OE2 
3783  N N   . LEU A 515  ? 0.3916 0.3341 0.5661 0.0034  -0.0320 0.0404  513  LEU A N   
3784  C CA  . LEU A 515  ? 0.3437 0.2881 0.5078 0.0034  -0.0288 0.0375  513  LEU A CA  
3785  C C   . LEU A 515  ? 0.3349 0.2801 0.5023 0.0018  -0.0288 0.0422  513  LEU A C   
3786  O O   . LEU A 515  ? 0.3446 0.2923 0.5028 0.0014  -0.0255 0.0432  513  LEU A O   
3787  C CB  . LEU A 515  ? 0.3468 0.2900 0.5103 0.0047  -0.0297 0.0276  513  LEU A CB  
3788  C CG  . LEU A 515  ? 0.3476 0.2911 0.5051 0.0064  -0.0289 0.0221  513  LEU A CG  
3789  C CD1 . LEU A 515  ? 0.3771 0.3202 0.5366 0.0077  -0.0305 0.0126  513  LEU A CD1 
3790  C CD2 . LEU A 515  ? 0.3471 0.2934 0.4900 0.0065  -0.0244 0.0235  513  LEU A CD2 
3791  N N   . ILE A 516  ? 0.3198 0.2630 0.5007 0.0008  -0.0324 0.0452  514  ILE A N   
3792  C CA  . ILE A 516  ? 0.3040 0.2483 0.4890 -0.0009 -0.0326 0.0501  514  ILE A CA  
3793  C C   . ILE A 516  ? 0.3414 0.2884 0.5275 -0.0025 -0.0316 0.0605  514  ILE A C   
3794  O O   . ILE A 516  ? 0.3410 0.2894 0.5315 -0.0041 -0.0319 0.0657  514  ILE A O   
3795  C CB  . ILE A 516  ? 0.3277 0.2686 0.5267 -0.0014 -0.0370 0.0472  514  ILE A CB  
3796  C CG1 . ILE A 516  ? 0.4005 0.3388 0.6133 -0.0017 -0.0412 0.0505  514  ILE A CG1 
3797  C CG2 . ILE A 516  ? 0.3516 0.2911 0.5483 0.0003  -0.0376 0.0365  514  ILE A CG2 
3798  C CD1 . ILE A 516  ? 0.4306 0.3656 0.6582 -0.0021 -0.0460 0.0476  514  ILE A CD1 
3799  N N   . ALA A 517  ? 0.3209 0.2694 0.5031 -0.0021 -0.0305 0.0638  515  ALA A N   
3800  C CA  . ALA A 517  ? 0.3761 0.3285 0.5578 -0.0034 -0.0293 0.0735  515  ALA A CA  
3801  C C   . ALA A 517  ? 0.3682 0.3247 0.5407 -0.0041 -0.0255 0.0760  515  ALA A C   
3802  O O   . ALA A 517  ? 0.3548 0.3119 0.5163 -0.0030 -0.0226 0.0707  515  ALA A O   
3803  C CB  . ALA A 517  ? 0.3907 0.3447 0.5661 -0.0025 -0.0278 0.0751  515  ALA A CB  
3804  N N   . ASP A 518  ? 0.3308 0.2904 0.5083 -0.0058 -0.0257 0.0841  516  ASP A N   
3805  C CA  . ASP A 518  ? 0.3083 0.2725 0.4790 -0.0065 -0.0224 0.0870  516  ASP A CA  
3806  C C   . ASP A 518  ? 0.3087 0.2783 0.4684 -0.0061 -0.0188 0.0909  516  ASP A C   
3807  O O   . ASP A 518  ? 0.3507 0.3238 0.5138 -0.0070 -0.0191 0.0985  516  ASP A O   
3808  C CB  . ASP A 518  ? 0.3352 0.3010 0.5169 -0.0087 -0.0244 0.0941  516  ASP A CB  
3809  C CG  . ASP A 518  ? 0.3633 0.3340 0.5388 -0.0094 -0.0212 0.0971  516  ASP A CG  
3810  O OD1 . ASP A 518  ? 0.3396 0.3121 0.5027 -0.0081 -0.0177 0.0933  516  ASP A OD1 
3811  O OD2 . ASP A 518  ? 0.4372 0.4102 0.6210 -0.0112 -0.0224 0.1034  516  ASP A OD2 
3812  N N   . PRO A 519  ? 0.3069 0.2777 0.4539 -0.0047 -0.0153 0.0862  517  PRO A N   
3813  C CA  . PRO A 519  ? 0.2930 0.2689 0.4300 -0.0041 -0.0121 0.0893  517  PRO A CA  
3814  C C   . PRO A 519  ? 0.2811 0.2638 0.4186 -0.0054 -0.0106 0.0977  517  PRO A C   
3815  O O   . PRO A 519  ? 0.2907 0.2784 0.4243 -0.0053 -0.0092 0.1025  517  PRO A O   
3816  C CB  . PRO A 519  ? 0.3087 0.2839 0.4336 -0.0025 -0.0092 0.0821  517  PRO A CB  
3817  C CG  . PRO A 519  ? 0.3784 0.3503 0.5066 -0.0028 -0.0102 0.0776  517  PRO A CG  
3818  C CD  . PRO A 519  ? 0.2895 0.2573 0.4309 -0.0037 -0.0144 0.0781  517  PRO A CD  
3819  N N   . VAL A 520  ? 0.3247 0.3083 0.4668 -0.0066 -0.0109 0.0996  518  VAL A N   
3820  C CA  . VAL A 520  ? 0.2690 0.2598 0.4116 -0.0079 -0.0094 0.1076  518  VAL A CA  
3821  C C   . VAL A 520  ? 0.3595 0.3530 0.5112 -0.0094 -0.0116 0.1161  518  VAL A C   
3822  O O   . VAL A 520  ? 0.3237 0.3242 0.4719 -0.0096 -0.0098 0.1222  518  VAL A O   
3823  C CB  . VAL A 520  ? 0.3030 0.2938 0.4499 -0.0089 -0.0096 0.1077  518  VAL A CB  
3824  C CG1 . VAL A 520  ? 0.3162 0.3153 0.4633 -0.0102 -0.0078 0.1159  518  VAL A CG1 
3825  C CG2 . VAL A 520  ? 0.3161 0.3041 0.4541 -0.0075 -0.0076 0.0994  518  VAL A CG2 
3826  N N   . GLU A 521  ? 0.3133 0.3016 0.4772 -0.0104 -0.0156 0.1166  519  GLU A N   
3827  C CA  . GLU A 521  ? 0.3468 0.3377 0.5203 -0.0119 -0.0182 0.1241  519  GLU A CA  
3828  C C   . GLU A 521  ? 0.3692 0.3605 0.5387 -0.0108 -0.0180 0.1249  519  GLU A C   
3829  O O   . GLU A 521  ? 0.3793 0.3772 0.5504 -0.0117 -0.0182 0.1310  519  GLU A O   
3830  C CB  . GLU A 521  ? 0.3867 0.3732 0.5735 -0.0129 -0.0227 0.1219  519  GLU A CB  
3831  C CG  . GLU A 521  ? 0.4021 0.3897 0.5940 -0.0142 -0.0232 0.1227  519  GLU A CG  
3832  C CD  . GLU A 521  ? 0.4570 0.4542 0.6477 -0.0156 -0.0212 0.1307  519  GLU A CD  
3833  O OE1 . GLU A 521  ? 0.5201 0.5233 0.7132 -0.0164 -0.0217 0.1366  519  GLU A OE1 
3834  O OE2 . GLU A 521  ? 0.4999 0.4993 0.6874 -0.0159 -0.0191 0.1311  519  GLU A OE2 
3835  N N   . VAL A 522  ? 0.3171 0.3033 0.4802 -0.0089 -0.0175 0.1170  520  VAL A N   
3836  C CA  . VAL A 522  ? 0.3014 0.2883 0.4600 -0.0078 -0.0171 0.1171  520  VAL A CA  
3837  C C   . VAL A 522  ? 0.4205 0.4156 0.5681 -0.0074 -0.0133 0.1210  520  VAL A C   
3838  O O   . VAL A 522  ? 0.3827 0.3823 0.5307 -0.0078 -0.0134 0.1270  520  VAL A O   
3839  C CB  . VAL A 522  ? 0.3985 0.3789 0.5524 -0.0058 -0.0173 0.1072  520  VAL A CB  
3840  C CG1 . VAL A 522  ? 0.3791 0.3608 0.5275 -0.0047 -0.0166 0.1074  520  VAL A CG1 
3841  C CG2 . VAL A 522  ? 0.4036 0.3768 0.5693 -0.0061 -0.0215 0.1035  520  VAL A CG2 
3842  N N   . VAL A 523  ? 0.3008 0.2982 0.4388 -0.0066 -0.0099 0.1175  521  VAL A N   
3843  C CA  . VAL A 523  ? 0.3332 0.3387 0.4611 -0.0060 -0.0063 0.1204  521  VAL A CA  
3844  C C   . VAL A 523  ? 0.3205 0.3341 0.4538 -0.0079 -0.0063 0.1306  521  VAL A C   
3845  O O   . VAL A 523  ? 0.3365 0.3573 0.4659 -0.0078 -0.0050 0.1356  521  VAL A O   
3846  C CB  . VAL A 523  ? 0.2714 0.2773 0.3890 -0.0047 -0.0031 0.1142  521  VAL A CB  
3847  C CG1 . VAL A 523  ? 0.3424 0.3575 0.4516 -0.0043 0.0003  0.1177  521  VAL A CG1 
3848  C CG2 . VAL A 523  ? 0.3128 0.3125 0.4235 -0.0029 -0.0027 0.1052  521  VAL A CG2 
3849  N N   . ARG A 524  ? 0.3148 0.3278 0.4572 -0.0096 -0.0079 0.1339  522  ARG A N   
3850  C CA  . ARG A 524  ? 0.3364 0.3579 0.4843 -0.0115 -0.0081 0.1429  522  ARG A CA  
3851  C C   . ARG A 524  ? 0.4164 0.4420 0.5692 -0.0123 -0.0101 0.1476  522  ARG A C   
3852  O O   . ARG A 524  ? 0.4263 0.4619 0.5778 -0.0130 -0.0090 0.1537  522  ARG A O   
3853  C CB  . ARG A 524  ? 0.3835 0.4030 0.5415 -0.0131 -0.0103 0.1431  522  ARG A CB  
3854  C CG  . ARG A 524  ? 0.3888 0.4180 0.5529 -0.0150 -0.0108 0.1506  522  ARG A CG  
3855  C CD  . ARG A 524  ? 0.4906 0.5170 0.6666 -0.0167 -0.0140 0.1508  522  ARG A CD  
3856  N NE  . ARG A 524  ? 0.4669 0.4868 0.6412 -0.0162 -0.0133 0.1452  522  ARG A NE  
3857  C CZ  . ARG A 524  ? 0.3736 0.3973 0.5425 -0.0161 -0.0104 0.1457  522  ARG A CZ  
3858  N NH1 . ARG A 524  ? 0.4520 0.4858 0.6159 -0.0163 -0.0076 0.1511  522  ARG A NH1 
3859  N NH2 . ARG A 524  ? 0.4484 0.4657 0.6171 -0.0157 -0.0103 0.1405  522  ARG A NH2 
3860  N N   . ALA A 525  ? 0.3699 0.3883 0.5283 -0.0121 -0.0132 0.1447  523  ALA A N   
3861  C CA  . ALA A 525  ? 0.4241 0.4454 0.5892 -0.0130 -0.0158 0.1489  523  ALA A CA  
3862  C C   . ALA A 525  ? 0.4165 0.4398 0.5736 -0.0116 -0.0144 0.1492  523  ALA A C   
3863  O O   . ALA A 525  ? 0.4629 0.4894 0.6246 -0.0123 -0.0163 0.1531  523  ALA A O   
3864  C CB  . ALA A 525  ? 0.4128 0.4258 0.5896 -0.0135 -0.0203 0.1455  523  ALA A CB  
3865  N N   . MET A 526  ? 0.3920 0.4136 0.5375 -0.0097 -0.0113 0.1454  524  MET A N   
3866  C CA  A MET A 526  ? 0.4138 0.4374 0.5514 -0.0082 -0.0099 0.1455  524  MET A CA  
3867  C CA  B MET A 526  ? 0.4140 0.4376 0.5517 -0.0083 -0.0100 0.1455  524  MET A CA  
3868  C C   . MET A 526  ? 0.4335 0.4693 0.5682 -0.0089 -0.0084 0.1525  524  MET A C   
3869  O O   . MET A 526  ? 0.4009 0.4440 0.5354 -0.0099 -0.0069 0.1561  524  MET A O   
3870  C CB  A MET A 526  ? 0.4603 0.4817 0.5851 -0.0060 -0.0067 0.1372  524  MET A CB  
3871  C CB  B MET A 526  ? 0.4600 0.4811 0.5850 -0.0060 -0.0068 0.1371  524  MET A CB  
3872  C CG  A MET A 526  ? 0.4468 0.4577 0.5721 -0.0049 -0.0079 0.1279  524  MET A CG  
3873  C CG  B MET A 526  ? 0.4395 0.4510 0.5639 -0.0046 -0.0082 0.1286  524  MET A CG  
3874  S SD  A MET A 526  ? 0.5188 0.5236 0.6496 -0.0044 -0.0113 0.1264  524  MET A SD  
3875  S SD  B MET A 526  ? 0.4284 0.4355 0.5418 -0.0027 -0.0054 0.1176  524  MET A SD  
3876  C CE  A MET A 526  ? 0.4441 0.4548 0.5624 -0.0028 -0.0084 0.1260  524  MET A CE  
3877  C CE  B MET A 526  ? 0.4326 0.4319 0.5445 -0.0011 -0.0069 0.1102  524  MET A CE  
3878  N N   . PRO A 527  ? 0.4593 0.4981 0.5920 -0.0085 -0.0088 0.1544  525  PRO A N   
3879  C CA  . PRO A 527  ? 0.4626 0.5138 0.5928 -0.0091 -0.0076 0.1610  525  PRO A CA  
3880  C C   . PRO A 527  ? 0.4705 0.5295 0.5894 -0.0080 -0.0033 0.1610  525  PRO A C   
3881  O O   . PRO A 527  ? 0.4223 0.4913 0.5416 -0.0090 -0.0022 0.1658  525  PRO A O   
3882  C CB  . PRO A 527  ? 0.4869 0.5379 0.6160 -0.0084 -0.0088 0.1615  525  PRO A CB  
3883  C CG  . PRO A 527  ? 0.5065 0.5464 0.6324 -0.0067 -0.0090 0.1544  525  PRO A CG  
3884  C CD  . PRO A 527  ? 0.4650 0.4965 0.5975 -0.0073 -0.0105 0.1508  525  PRO A CD  
3885  N N   . VAL A 528  ? 0.4630 0.5177 0.5720 -0.0059 -0.0010 0.1556  526  VAL A N   
3886  C CA  . VAL A 528  ? 0.3781 0.4389 0.4765 -0.0046 0.0029  0.1527  526  VAL A CA  
3887  C C   . VAL A 528  ? 0.3733 0.4256 0.4701 -0.0039 0.0035  0.1444  526  VAL A C   
3888  O O   . VAL A 528  ? 0.4241 0.4677 0.5180 -0.0026 0.0030  0.1367  526  VAL A O   
3889  C CB  . VAL A 528  ? 0.3973 0.4622 0.4845 -0.0024 0.0050  0.1490  526  VAL A CB  
3890  C CG1 . VAL A 528  ? 0.4483 0.5190 0.5254 -0.0009 0.0087  0.1447  526  VAL A CG1 
3891  C CG2 . VAL A 528  ? 0.4446 0.5185 0.5334 -0.0032 0.0043  0.1573  526  VAL A CG2 
3892  N N   . VAL A 529  ? 0.3440 0.3991 0.4427 -0.0047 0.0045  0.1461  527  VAL A N   
3893  C CA  . VAL A 529  ? 0.3438 0.3913 0.4414 -0.0042 0.0050  0.1389  527  VAL A CA  
3894  C C   . VAL A 529  ? 0.3803 0.4279 0.4655 -0.0017 0.0080  0.1308  527  VAL A C   
3895  O O   . VAL A 529  ? 0.3692 0.4256 0.4473 -0.0008 0.0107  0.1317  527  VAL A O   
3896  C CB  . VAL A 529  ? 0.3343 0.3854 0.4374 -0.0057 0.0053  0.1432  527  VAL A CB  
3897  C CG1 . VAL A 529  ? 0.3262 0.3709 0.4265 -0.0049 0.0062  0.1354  527  VAL A CG1 
3898  C CG2 . VAL A 529  ? 0.3854 0.4345 0.5022 -0.0082 0.0017  0.1503  527  VAL A CG2 
3899  N N   . GLY A 530  ? 0.3226 0.3607 0.4054 -0.0007 0.0074  0.1228  528  GLY A N   
3900  C CA  . GLY A 530  ? 0.3446 0.3817 0.4167 0.0014  0.0098  0.1150  528  GLY A CA  
3901  C C   . GLY A 530  ? 0.3066 0.3460 0.3710 0.0030  0.0108  0.1128  528  GLY A C   
3902  O O   . GLY A 530  ? 0.3305 0.3717 0.3860 0.0048  0.0131  0.1078  528  GLY A O   
3903  N N   . ALA A 531  ? 0.3205 0.3600 0.3883 0.0026  0.0090  0.1163  529  ALA A N   
3904  C CA  . ALA A 531  ? 0.3004 0.3420 0.3609 0.0041  0.0098  0.1141  529  ALA A CA  
3905  C C   . ALA A 531  ? 0.2836 0.3170 0.3384 0.0056  0.0102  0.1048  529  ALA A C   
3906  O O   . ALA A 531  ? 0.3367 0.3616 0.3956 0.0052  0.0086  0.1012  529  ALA A O   
3907  C CB  . ALA A 531  ? 0.3179 0.3600 0.3842 0.0032  0.0075  0.1195  529  ALA A CB  
3908  N N   . LYS A 532  ? 0.2799 0.3166 0.3255 0.0074  0.0121  0.1011  530  LYS A N   
3909  C CA  . LYS A 532  ? 0.2843 0.3143 0.3242 0.0087  0.0123  0.0931  530  LYS A CA  
3910  C C   . LYS A 532  ? 0.3093 0.3326 0.3537 0.0083  0.0099  0.0922  530  LYS A C   
3911  O O   . LYS A 532  ? 0.2994 0.3246 0.3492 0.0075  0.0083  0.0977  530  LYS A O   
3912  C CB  . LYS A 532  ? 0.3530 0.3889 0.3839 0.0105  0.0142  0.0909  530  LYS A CB  
3913  C CG  . LYS A 532  ? 0.4210 0.4510 0.4459 0.0119  0.0145  0.0831  530  LYS A CG  
3914  C CD  . LYS A 532  ? 0.3297 0.3658 0.3467 0.0136  0.0160  0.0812  530  LYS A CD  
3915  C CE  . LYS A 532  ? 0.3699 0.4114 0.3877 0.0135  0.0152  0.0861  530  LYS A CE  
3916  N NZ  . LYS A 532  ? 0.3260 0.3607 0.3465 0.0132  0.0132  0.0848  530  LYS A NZ  
3917  N N   . HIS A 533  ? 0.2889 0.3046 0.3315 0.0089  0.0096  0.0854  531  HIS A N   
3918  C CA  . HIS A 533  ? 0.2852 0.2950 0.3310 0.0089  0.0075  0.0835  531  HIS A CA  
3919  C C   . HIS A 533  ? 0.3356 0.3493 0.3776 0.0097  0.0076  0.0849  531  HIS A C   
3920  O O   . HIS A 533  ? 0.3116 0.3294 0.3456 0.0109  0.0095  0.0828  531  HIS A O   
3921  C CB  . HIS A 533  ? 0.2920 0.2947 0.3346 0.0096  0.0076  0.0756  531  HIS A CB  
3922  C CG  . HIS A 533  ? 0.3118 0.3081 0.3595 0.0093  0.0053  0.0733  531  HIS A CG  
3923  N ND1 . HIS A 533  ? 0.2959 0.2921 0.3434 0.0098  0.0044  0.0734  531  HIS A ND1 
3924  C CD2 . HIS A 533  ? 0.3442 0.3346 0.3977 0.0087  0.0037  0.0706  531  HIS A CD2 
3925  C CE1 . HIS A 533  ? 0.3985 0.3888 0.4514 0.0096  0.0023  0.0707  531  HIS A CE1 
3926  N NE2 . HIS A 533  ? 0.4237 0.4106 0.4803 0.0090  0.0018  0.0689  531  HIS A NE2 
3927  N N   . ASP A 534  ? 0.3123 0.3248 0.3606 0.0090  0.0053  0.0883  532  ASP A N   
3928  C CA  . ASP A 534  ? 0.3115 0.3280 0.3572 0.0097  0.0051  0.0904  532  ASP A CA  
3929  C C   . ASP A 534  ? 0.3434 0.3568 0.3821 0.0111  0.0058  0.0835  532  ASP A C   
3930  O O   . ASP A 534  ? 0.3821 0.4000 0.4156 0.0120  0.0065  0.0839  532  ASP A O   
3931  C CB  . ASP A 534  ? 0.3431 0.3578 0.3981 0.0086  0.0022  0.0951  532  ASP A CB  
3932  C CG  . ASP A 534  ? 0.5443 0.5625 0.6072 0.0070  0.0011  0.1028  532  ASP A CG  
3933  O OD1 . ASP A 534  ? 0.6432 0.6690 0.7030 0.0068  0.0029  0.1068  532  ASP A OD1 
3934  O OD2 . ASP A 534  ? 0.7167 0.7303 0.7892 0.0059  -0.0016 0.1049  532  ASP A OD2 
3935  N N   . ARG A 535  ? 0.3084 0.3145 0.3469 0.0113  0.0055  0.0774  533  ARG A N   
3936  C CA  . ARG A 535  ? 0.3099 0.3127 0.3431 0.0124  0.0059  0.0713  533  ARG A CA  
3937  C C   . ARG A 535  ? 0.2882 0.2912 0.3132 0.0133  0.0081  0.0661  533  ARG A C   
3938  O O   . ARG A 535  ? 0.3393 0.3391 0.3600 0.0141  0.0084  0.0608  533  ARG A O   
3939  C CB  . ARG A 535  ? 0.3891 0.3845 0.4276 0.0121  0.0039  0.0677  533  ARG A CB  
3940  N N   . ILE A 536  ? 0.2999 0.3069 0.3228 0.0133  0.0096  0.0677  534  ILE A N   
3941  C CA  . ILE A 536  ? 0.3016 0.3092 0.3173 0.0143  0.0116  0.0632  534  ILE A CA  
3942  C C   . ILE A 536  ? 0.2813 0.2972 0.2922 0.0152  0.0131  0.0656  534  ILE A C   
3943  O O   . ILE A 536  ? 0.3013 0.3228 0.3146 0.0147  0.0135  0.0708  534  ILE A O   
3944  C CB  . ILE A 536  ? 0.2857 0.2905 0.3029 0.0137  0.0121  0.0617  534  ILE A CB  
3945  C CG1 . ILE A 536  ? 0.3325 0.3299 0.3545 0.0129  0.0105  0.0590  534  ILE A CG1 
3946  C CG2 . ILE A 536  ? 0.3122 0.3180 0.3226 0.0147  0.0139  0.0574  534  ILE A CG2 
3947  C CD1 . ILE A 536  ? 0.3373 0.3321 0.3612 0.0123  0.0108  0.0576  534  ILE A CD1 
3948  N N   . ALA A 537  ? 0.2715 0.2888 0.2762 0.0165  0.0138  0.0619  535  ALA A N   
3949  C CA  . ALA A 537  ? 0.2600 0.2856 0.2599 0.0176  0.0151  0.0633  535  ALA A CA  
3950  C C   . ALA A 537  ? 0.2758 0.3039 0.2724 0.0183  0.0168  0.0612  535  ALA A C   
3951  O O   . ALA A 537  ? 0.2588 0.2818 0.2535 0.0185  0.0171  0.0562  535  ALA A O   
3952  C CB  . ALA A 537  ? 0.3105 0.3363 0.3052 0.0188  0.0150  0.0595  535  ALA A CB  
3953  N N   . LEU A 538  ? 0.2484 0.2849 0.2447 0.0185  0.0178  0.0652  536  LEU A N   
3954  C CA  . LEU A 538  ? 0.2524 0.2930 0.2445 0.0197  0.0195  0.0625  536  LEU A CA  
3955  C C   . LEU A 538  ? 0.2908 0.3314 0.2767 0.0214  0.0199  0.0565  536  LEU A C   
3956  O O   . LEU A 538  ? 0.2707 0.3118 0.2549 0.0218  0.0191  0.0562  536  LEU A O   
3957  C CB  . LEU A 538  ? 0.2719 0.3232 0.2641 0.0200  0.0206  0.0677  536  LEU A CB  
3958  C CG  . LEU A 538  ? 0.2851 0.3377 0.2835 0.0183  0.0205  0.0738  536  LEU A CG  
3959  C CD1 . LEU A 538  ? 0.3471 0.4117 0.3451 0.0185  0.0216  0.0793  536  LEU A CD1 
3960  C CD2 . LEU A 538  ? 0.3048 0.3529 0.3044 0.0180  0.0211  0.0712  536  LEU A CD2 
3961  N N   . PRO A 539  ? 0.2446 0.2842 0.2275 0.0225  0.0207  0.0517  537  PRO A N   
3962  C CA  . PRO A 539  ? 0.2557 0.2948 0.2335 0.0241  0.0207  0.0460  537  PRO A CA  
3963  C C   . PRO A 539  ? 0.2661 0.3137 0.2405 0.0254  0.0210  0.0466  537  PRO A C   
3964  O O   . PRO A 539  ? 0.2585 0.3046 0.2304 0.0261  0.0202  0.0436  537  PRO A O   
3965  C CB  . PRO A 539  ? 0.2447 0.2830 0.2211 0.0249  0.0216  0.0420  537  PRO A CB  
3966  C CG  . PRO A 539  ? 0.2564 0.2900 0.2373 0.0232  0.0216  0.0445  537  PRO A CG  
3967  C CD  . PRO A 539  ? 0.2339 0.2715 0.2185 0.0221  0.0214  0.0511  537  PRO A CD  
3968  N N   . ALA A 540  ? 0.2589 0.3159 0.2334 0.0258  0.0220  0.0508  538  ALA A N   
3969  C CA  . ALA A 540  ? 0.2770 0.3434 0.2482 0.0271  0.0222  0.0515  538  ALA A CA  
3970  C C   . ALA A 540  ? 0.3118 0.3773 0.2840 0.0263  0.0209  0.0546  538  ALA A C   
3971  O O   . ALA A 540  ? 0.3049 0.3763 0.2737 0.0275  0.0208  0.0539  538  ALA A O   
3972  C CB  . ALA A 540  ? 0.2875 0.3649 0.2589 0.0274  0.0236  0.0561  538  ALA A CB  
3973  N N   . GLU A 541  ? 0.2817 0.3403 0.2587 0.0244  0.0199  0.0578  539  GLU A N   
3974  C CA  . GLU A 541  ? 0.2797 0.3379 0.2588 0.0236  0.0185  0.0616  539  GLU A CA  
3975  C C   . GLU A 541  ? 0.2920 0.3407 0.2713 0.0233  0.0172  0.0576  539  GLU A C   
3976  O O   . GLU A 541  ? 0.2918 0.3381 0.2742 0.0224  0.0159  0.0604  539  GLU A O   
3977  C CB  . GLU A 541  ? 0.3415 0.4005 0.3270 0.0217  0.0180  0.0690  539  GLU A CB  
3978  C CG  . GLU A 541  ? 0.3881 0.4574 0.3736 0.0219  0.0194  0.0735  539  GLU A CG  
3979  C CD  . GLU A 541  ? 0.5146 0.5858 0.5067 0.0199  0.0187  0.0816  539  GLU A CD  
3980  O OE1 . GLU A 541  ? 0.6605 0.7299 0.6560 0.0190  0.0171  0.0852  539  GLU A OE1 
3981  O OE2 . GLU A 541  ? 0.6052 0.6795 0.5995 0.0193  0.0196  0.0845  539  GLU A OE2 
3982  N N   . LEU A 542  ? 0.2781 0.3217 0.2544 0.0241  0.0175  0.0511  540  LEU A N   
3983  C CA  . LEU A 542  ? 0.2902 0.3253 0.2667 0.0237  0.0164  0.0473  540  LEU A CA  
3984  C C   . LEU A 542  ? 0.2852 0.3220 0.2606 0.0240  0.0153  0.0477  540  LEU A C   
3985  O O   . LEU A 542  ? 0.3158 0.3466 0.2933 0.0233  0.0142  0.0471  540  LEU A O   
3986  C CB  . LEU A 542  ? 0.3296 0.3613 0.3026 0.0246  0.0168  0.0407  540  LEU A CB  
3987  C CG  . LEU A 542  ? 0.3941 0.4199 0.3687 0.0239  0.0172  0.0388  540  LEU A CG  
3988  C CD1 . LEU A 542  ? 0.3340 0.3554 0.3057 0.0246  0.0169  0.0327  540  LEU A CD1 
3989  C CD2 . LEU A 542  ? 0.3466 0.3663 0.3263 0.0221  0.0164  0.0414  540  LEU A CD2 
3990  N N   . PHE A 543  ? 0.2786 0.3238 0.2505 0.0253  0.0157  0.0484  541  PHE A N   
3991  C CA  . PHE A 543  ? 0.3000 0.3473 0.2704 0.0258  0.0147  0.0485  541  PHE A CA  
3992  C C   . PHE A 543  ? 0.2880 0.3416 0.2611 0.0252  0.0142  0.0556  541  PHE A C   
3993  O O   . PHE A 543  ? 0.2935 0.3504 0.2652 0.0256  0.0134  0.0564  541  PHE A O   
3994  C CB  . PHE A 543  ? 0.2796 0.3316 0.2443 0.0277  0.0151  0.0436  541  PHE A CB  
3995  C CG  . PHE A 543  ? 0.2707 0.3173 0.2337 0.0283  0.0154  0.0372  541  PHE A CG  
3996  C CD1 . PHE A 543  ? 0.3281 0.3652 0.2925 0.0273  0.0146  0.0343  541  PHE A CD1 
3997  C CD2 . PHE A 543  ? 0.2586 0.3095 0.2189 0.0296  0.0164  0.0344  541  PHE A CD2 
3998  C CE1 . PHE A 543  ? 0.3018 0.3340 0.2650 0.0276  0.0147  0.0292  541  PHE A CE1 
3999  C CE2 . PHE A 543  ? 0.2752 0.3207 0.2347 0.0300  0.0164  0.0289  541  PHE A CE2 
4000  C CZ  . PHE A 543  ? 0.2994 0.3355 0.2603 0.0289  0.0156  0.0265  541  PHE A CZ  
4001  N N   . GLY A 544  ? 0.2752 0.3304 0.2523 0.0241  0.0146  0.0608  542  GLY A N   
4002  C CA  . GLY A 544  ? 0.3443 0.4046 0.3251 0.0231  0.0138  0.0682  542  GLY A CA  
4003  C C   . GLY A 544  ? 0.3268 0.3985 0.3036 0.0243  0.0142  0.0702  542  GLY A C   
4004  O O   . GLY A 544  ? 0.3173 0.3956 0.2896 0.0257  0.0157  0.0680  542  GLY A O   
4005  N N   . ASP A 545  ? 0.3445 0.4188 0.3229 0.0239  0.0129  0.0743  543  ASP A N   
4006  C CA  . ASP A 545  ? 0.3749 0.4609 0.3499 0.0249  0.0131  0.0772  543  ASP A CA  
4007  C C   . ASP A 545  ? 0.3845 0.4732 0.3527 0.0269  0.0134  0.0704  543  ASP A C   
4008  O O   . ASP A 545  ? 0.4051 0.5046 0.3695 0.0281  0.0139  0.0716  543  ASP A O   
4009  C CB  . ASP A 545  ? 0.4190 0.5064 0.3982 0.0238  0.0112  0.0837  543  ASP A CB  
4010  C CG  . ASP A 545  ? 0.5528 0.6396 0.5395 0.0218  0.0106  0.0913  543  ASP A CG  
4011  O OD1 . ASP A 545  ? 0.5507 0.6374 0.5387 0.0213  0.0117  0.0920  543  ASP A OD1 
4012  O OD2 . ASP A 545  ? 0.6673 0.7534 0.6590 0.0207  0.0087  0.0966  543  ASP A OD2 
4013  N N   . ALA A 546  ? 0.3243 0.4040 0.2910 0.0274  0.0131  0.0636  544  ALA A N   
4014  C CA  . ALA A 546  ? 0.3435 0.4252 0.3047 0.0292  0.0131  0.0573  544  ALA A CA  
4015  C C   . ALA A 546  ? 0.3585 0.4477 0.3152 0.0309  0.0146  0.0539  544  ALA A C   
4016  O O   . ALA A 546  ? 0.3593 0.4568 0.3117 0.0326  0.0146  0.0519  544  ALA A O   
4017  C CB  . ALA A 546  ? 0.3290 0.3995 0.2903 0.0291  0.0124  0.0513  544  ALA A CB  
4018  N N   . ARG A 547  ? 0.2942 0.3808 0.2519 0.0307  0.0158  0.0529  545  ARG A N   
4019  C CA  . ARG A 547  ? 0.3233 0.4168 0.2774 0.0324  0.0171  0.0493  545  ARG A CA  
4020  C C   . ARG A 547  ? 0.2555 0.3448 0.2122 0.0316  0.0182  0.0499  545  ARG A C   
4021  O O   . ARG A 547  ? 0.2790 0.3590 0.2396 0.0299  0.0178  0.0513  545  ARG A O   
4022  C CB  . ARG A 547  ? 0.3543 0.4460 0.3044 0.0343  0.0168  0.0409  545  ARG A CB  
4023  C CG  . ARG A 547  ? 0.3416 0.4208 0.2932 0.0336  0.0162  0.0364  545  ARG A CG  
4024  C CD  . ARG A 547  ? 0.3237 0.4015 0.2720 0.0353  0.0155  0.0287  545  ARG A CD  
4025  N NE  . ARG A 547  ? 0.2880 0.3544 0.2380 0.0342  0.0144  0.0261  545  ARG A NE  
4026  C CZ  . ARG A 547  ? 0.2780 0.3365 0.2292 0.0338  0.0145  0.0224  545  ARG A CZ  
4027  N NH1 . ARG A 547  ? 0.2782 0.3383 0.2290 0.0346  0.0154  0.0203  545  ARG A NH1 
4028  N NH2 . ARG A 547  ? 0.2934 0.3426 0.2461 0.0326  0.0135  0.0209  545  ARG A NH2 
4029  N N   . THR A 548  ? 0.2690 0.3657 0.2235 0.0329  0.0196  0.0483  546  THR A N   
4030  C CA  . THR A 548  ? 0.2500 0.3442 0.2065 0.0324  0.0207  0.0484  546  THR A CA  
4031  C C   . THR A 548  ? 0.2407 0.3269 0.1960 0.0333  0.0206  0.0407  546  THR A C   
4032  O O   . THR A 548  ? 0.2516 0.3406 0.2033 0.0353  0.0204  0.0349  546  THR A O   
4033  C CB  . THR A 548  ? 0.2891 0.3961 0.2439 0.0336  0.0223  0.0504  546  THR A CB  
4034  O OG1 . THR A 548  ? 0.3553 0.4706 0.3112 0.0327  0.0223  0.0580  546  THR A OG1 
4035  C CG2 . THR A 548  ? 0.3075 0.4123 0.2647 0.0330  0.0234  0.0509  546  THR A CG2 
4036  N N   . ASN A 549  ? 0.2350 0.3114 0.1935 0.0318  0.0205  0.0408  547  ASN A N   
4037  C CA  . ASN A 549  ? 0.2409 0.3097 0.1987 0.0324  0.0203  0.0343  547  ASN A CA  
4038  C C   . ASN A 549  ? 0.2504 0.3256 0.2064 0.0342  0.0214  0.0312  547  ASN A C   
4039  O O   . ASN A 549  ? 0.2561 0.3389 0.2126 0.0343  0.0226  0.0349  547  ASN A O   
4040  C CB  . ASN A 549  ? 0.2338 0.2927 0.1957 0.0304  0.0200  0.0359  547  ASN A CB  
4041  C CG  . ASN A 549  ? 0.2404 0.2905 0.2019 0.0305  0.0195  0.0300  547  ASN A CG  
4042  O OD1 . ASN A 549  ? 0.2450 0.2951 0.2038 0.0319  0.0189  0.0249  547  ASN A OD1 
4043  N ND2 . ASN A 549  ? 0.2547 0.2976 0.2193 0.0290  0.0195  0.0309  547  ASN A ND2 
4044  N N   . SER A 550  ? 0.2413 0.3138 0.1955 0.0357  0.0209  0.0243  548  SER A N   
4045  C CA  . SER A 550  ? 0.2416 0.3186 0.1949 0.0374  0.0217  0.0207  548  SER A CA  
4046  C C   . SER A 550  ? 0.2297 0.3015 0.1862 0.0361  0.0225  0.0227  548  SER A C   
4047  O O   . SER A 550  ? 0.2565 0.3192 0.2155 0.0341  0.0220  0.0244  548  SER A O   
4048  C CB  . SER A 550  ? 0.2353 0.3089 0.1871 0.0391  0.0206  0.0130  548  SER A CB  
4049  O OG  . SER A 550  ? 0.2475 0.3093 0.2013 0.0376  0.0195  0.0114  548  SER A OG  
4050  N N   . ALA A 551  ? 0.2428 0.3212 0.1992 0.0373  0.0237  0.0222  549  ALA A N   
4051  C CA  . ALA A 551  ? 0.2724 0.3473 0.2318 0.0363  0.0245  0.0239  549  ALA A CA  
4052  C C   . ALA A 551  ? 0.2595 0.3306 0.2189 0.0377  0.0241  0.0174  549  ALA A C   
4053  O O   . ALA A 551  ? 0.2444 0.3209 0.2018 0.0400  0.0239  0.0124  549  ALA A O   
4054  C CB  . ALA A 551  ? 0.2795 0.3649 0.2394 0.0365  0.0261  0.0284  549  ALA A CB  
4055  N N   . GLY A 552  ? 0.2490 0.3112 0.2110 0.0362  0.0238  0.0175  550  GLY A N   
4056  C CA  . GLY A 552  ? 0.2566 0.3149 0.2195 0.0372  0.0234  0.0125  550  GLY A CA  
4057  C C   . GLY A 552  ? 0.2691 0.3317 0.2337 0.0376  0.0247  0.0139  550  GLY A C   
4058  O O   . GLY A 552  ? 0.2828 0.3540 0.2473 0.0377  0.0261  0.0179  550  GLY A O   
4059  N N   . LEU A 553  ? 0.2588 0.3156 0.2253 0.0377  0.0242  0.0108  551  LEU A N   
4060  C CA  . LEU A 553  ? 0.2362 0.2960 0.2046 0.0381  0.0253  0.0114  551  LEU A CA  
4061  C C   . LEU A 553  ? 0.2619 0.3114 0.2330 0.0363  0.0246  0.0118  551  LEU A C   
4062  O O   . LEU A 553  ? 0.2774 0.3189 0.2487 0.0358  0.0231  0.0090  551  LEU A O   
4063  C CB  . LEU A 553  ? 0.2895 0.3545 0.2573 0.0410  0.0251  0.0054  551  LEU A CB  
4064  C CG  . LEU A 553  ? 0.2883 0.3654 0.2534 0.0433  0.0259  0.0041  551  LEU A CG  
4065  C CD1 . LEU A 553  ? 0.3640 0.4451 0.3292 0.0463  0.0253  -0.0029 551  LEU A CD1 
4066  C CD2 . LEU A 553  ? 0.3291 0.4155 0.2942 0.0427  0.0279  0.0101  551  LEU A CD2 
4067  N N   . ASP A 554  ? 0.2582 0.3084 0.2316 0.0352  0.0256  0.0155  552  ASP A N   
4068  C CA  . ASP A 554  ? 0.2746 0.3159 0.2507 0.0333  0.0250  0.0164  552  ASP A CA  
4069  C C   . ASP A 554  ? 0.2517 0.2924 0.2292 0.0347  0.0247  0.0124  552  ASP A C   
4070  O O   . ASP A 554  ? 0.2319 0.2781 0.2107 0.0354  0.0259  0.0134  552  ASP A O   
4071  C CB  . ASP A 554  ? 0.2556 0.2978 0.2341 0.0314  0.0260  0.0225  552  ASP A CB  
4072  C CG  . ASP A 554  ? 0.2569 0.2903 0.2382 0.0295  0.0253  0.0233  552  ASP A CG  
4073  O OD1 . ASP A 554  ? 0.2742 0.3013 0.2553 0.0296  0.0241  0.0194  552  ASP A OD1 
4074  O OD2 . ASP A 554  ? 0.2876 0.3205 0.2713 0.0278  0.0257  0.0278  552  ASP A OD2 
4075  N N   . LEU A 555  ? 0.2454 0.2793 0.2230 0.0350  0.0231  0.0082  553  LEU A N   
4076  C CA  . LEU A 555  ? 0.2394 0.2722 0.2189 0.0363  0.0225  0.0043  553  LEU A CA  
4077  C C   . LEU A 555  ? 0.2356 0.2632 0.2179 0.0346  0.0225  0.0066  553  LEU A C   
4078  O O   . LEU A 555  ? 0.2682 0.2938 0.2525 0.0354  0.0217  0.0038  553  LEU A O   
4079  C CB  . LEU A 555  ? 0.2402 0.2684 0.2195 0.0373  0.0205  -0.0009 553  LEU A CB  
4080  C CG  . LEU A 555  ? 0.2414 0.2753 0.2182 0.0392  0.0203  -0.0039 553  LEU A CG  
4081  C CD1 . LEU A 555  ? 0.3188 0.3479 0.2963 0.0401  0.0181  -0.0091 553  LEU A CD1 
4082  C CD2 . LEU A 555  ? 0.3018 0.3464 0.2781 0.0417  0.0217  -0.0052 553  LEU A CD2 
4083  N N   . SER A 556  ? 0.2295 0.2551 0.2124 0.0324  0.0232  0.0115  554  SER A N   
4084  C CA  . SER A 556  ? 0.2371 0.2596 0.2227 0.0309  0.0234  0.0139  554  SER A CA  
4085  C C   . SER A 556  ? 0.2610 0.2908 0.2479 0.0311  0.0251  0.0173  554  SER A C   
4086  O O   . SER A 556  ? 0.2593 0.2875 0.2489 0.0301  0.0253  0.0193  554  SER A O   
4087  C CB  . SER A 556  ? 0.2514 0.2667 0.2376 0.0283  0.0227  0.0166  554  SER A CB  
4088  O OG  . SER A 556  ? 0.2812 0.2994 0.2675 0.0272  0.0237  0.0209  554  SER A OG  
4089  N N   . ASN A 557  ? 0.2283 0.2667 0.2136 0.0325  0.0263  0.0181  555  ASN A N   
4090  C CA  . ASN A 557  ? 0.2321 0.2785 0.2186 0.0325  0.0280  0.0220  555  ASN A CA  
4091  C C   . ASN A 557  ? 0.2561 0.3092 0.2429 0.0349  0.0286  0.0187  555  ASN A C   
4092  O O   . ASN A 557  ? 0.2292 0.2868 0.2139 0.0372  0.0285  0.0146  555  ASN A O   
4093  C CB  . ASN A 557  ? 0.2359 0.2884 0.2205 0.0324  0.0287  0.0252  555  ASN A CB  
4094  C CG  . ASN A 557  ? 0.2375 0.2993 0.2236 0.0322  0.0304  0.0301  555  ASN A CG  
4095  O OD1 . ASN A 557  ? 0.2615 0.3301 0.2480 0.0337  0.0314  0.0289  555  ASN A OD1 
4096  N ND2 . ASN A 557  ? 0.2740 0.3362 0.2612 0.0302  0.0306  0.0357  555  ASN A ND2 
4097  N N   . GLU A 558  ? 0.2298 0.2839 0.2195 0.0346  0.0292  0.0202  556  GLU A N   
4098  C CA  . GLU A 558  ? 0.2618 0.3219 0.2523 0.0370  0.0298  0.0167  556  GLU A CA  
4099  C C   . GLU A 558  ? 0.2274 0.3000 0.2162 0.0390  0.0313  0.0167  556  GLU A C   
4100  O O   . GLU A 558  ? 0.2517 0.3295 0.2399 0.0418  0.0313  0.0117  556  GLU A O   
4101  C CB  . GLU A 558  ? 0.2527 0.3121 0.2469 0.0362  0.0302  0.0187  556  GLU A CB  
4102  C CG  . GLU A 558  ? 0.2736 0.3222 0.2696 0.0348  0.0286  0.0175  556  GLU A CG  
4103  C CD  . GLU A 558  ? 0.2354 0.2797 0.2312 0.0366  0.0269  0.0114  556  GLU A CD  
4104  O OE1 . GLU A 558  ? 0.2573 0.3068 0.2523 0.0392  0.0269  0.0072  556  GLU A OE1 
4105  O OE2 . GLU A 558  ? 0.2554 0.2908 0.2524 0.0352  0.0254  0.0109  556  GLU A OE2 
4106  N N   . GLU A 559  ? 0.2320 0.3099 0.2201 0.0377  0.0325  0.0223  557  GLU A N   
4107  C CA  . GLU A 559  ? 0.2494 0.3401 0.2356 0.0395  0.0340  0.0227  557  GLU A CA  
4108  C C   . GLU A 559  ? 0.2453 0.3369 0.2278 0.0414  0.0332  0.0178  557  GLU A C   
4109  O O   . GLU A 559  ? 0.2585 0.3589 0.2397 0.0442  0.0337  0.0137  557  GLU A O   
4110  C CB  . GLU A 559  ? 0.2950 0.3904 0.2815 0.0374  0.0351  0.0303  557  GLU A CB  
4111  C CG  . GLU A 559  ? 0.3054 0.4019 0.2960 0.0354  0.0360  0.0359  557  GLU A CG  
4112  C CD  . GLU A 559  ? 0.4289 0.5286 0.4206 0.0331  0.0365  0.0435  557  GLU A CD  
4113  O OE1 . GLU A 559  ? 0.5238 0.6272 0.5128 0.0334  0.0366  0.0445  557  GLU A OE1 
4114  O OE2 . GLU A 559  ? 0.3967 0.4952 0.3924 0.0310  0.0368  0.0486  557  GLU A OE2 
4115  N N   . THR A 560  ? 0.2397 0.3226 0.2210 0.0400  0.0318  0.0178  558  THR A N   
4116  C CA  . THR A 560  ? 0.2546 0.3378 0.2329 0.0417  0.0308  0.0131  558  THR A CA  
4117  C C   . THR A 560  ? 0.2314 0.3124 0.2103 0.0441  0.0296  0.0058  558  THR A C   
4118  O O   . THR A 560  ? 0.2530 0.3404 0.2302 0.0467  0.0294  0.0010  558  THR A O   
4119  C CB  . THR A 560  ? 0.2467 0.3202 0.2242 0.0396  0.0296  0.0147  558  THR A CB  
4120  O OG1 . THR A 560  ? 0.2858 0.3613 0.2636 0.0374  0.0305  0.0215  558  THR A OG1 
4121  C CG2 . THR A 560  ? 0.2755 0.3493 0.2500 0.0411  0.0285  0.0101  558  THR A CG2 
4122  N N   . LEU A 561  ? 0.2243 0.2966 0.2059 0.0433  0.0287  0.0047  559  LEU A N   
4123  C CA  . LEU A 561  ? 0.2146 0.2843 0.1977 0.0454  0.0272  -0.0019 559  LEU A CA  
4124  C C   . LEU A 561  ? 0.2532 0.3337 0.2371 0.0483  0.0282  -0.0051 559  LEU A C   
4125  O O   . LEU A 561  ? 0.2510 0.3340 0.2351 0.0511  0.0271  -0.0114 559  LEU A O   
4126  C CB  . LEU A 561  ? 0.2075 0.2667 0.1937 0.0437  0.0260  -0.0016 559  LEU A CB  
4127  C CG  . LEU A 561  ? 0.2116 0.2602 0.1970 0.0413  0.0246  0.0000  559  LEU A CG  
4128  C CD1 . LEU A 561  ? 0.2369 0.2769 0.2253 0.0397  0.0237  0.0007  559  LEU A CD1 
4129  C CD2 . LEU A 561  ? 0.2413 0.2874 0.2254 0.0425  0.0229  -0.0049 559  LEU A CD2 
4130  N N   . ALA A 562  ? 0.2497 0.3368 0.2345 0.0478  0.0301  -0.0009 560  ALA A N   
4131  C CA  . ALA A 562  ? 0.2440 0.3424 0.2297 0.0506  0.0313  -0.0037 560  ALA A CA  
4132  C C   . ALA A 562  ? 0.2522 0.3619 0.2346 0.0529  0.0320  -0.0059 560  ALA A C   
4133  O O   . ALA A 562  ? 0.2548 0.3711 0.2375 0.0561  0.0317  -0.0122 560  ALA A O   
4134  C CB  . ALA A 562  ? 0.2804 0.3835 0.2680 0.0493  0.0332  0.0018  560  ALA A CB  
4135  N N   . SER A 563  ? 0.2539 0.3665 0.2335 0.0513  0.0329  -0.0010 561  SER A N   
4136  C CA  A SER A 563  ? 0.2623 0.3861 0.2385 0.0532  0.0336  -0.0026 561  SER A CA  
4137  C CA  B SER A 563  ? 0.2621 0.3859 0.2383 0.0533  0.0336  -0.0027 561  SER A CA  
4138  C C   . SER A 563  ? 0.2716 0.3913 0.2465 0.0551  0.0315  -0.0096 561  SER A C   
4139  O O   . SER A 563  ? 0.2921 0.4208 0.2657 0.0582  0.0315  -0.0150 561  SER A O   
4140  C CB  A SER A 563  ? 0.2865 0.4128 0.2605 0.0508  0.0347  0.0050  561  SER A CB  
4141  C CB  B SER A 563  ? 0.2871 0.4149 0.2611 0.0510  0.0349  0.0048  561  SER A CB  
4142  O OG  A SER A 563  ? 0.2782 0.4155 0.2488 0.0525  0.0353  0.0039  561  SER A OG  
4143  O OG  B SER A 563  ? 0.3264 0.4429 0.2997 0.0487  0.0336  0.0069  561  SER A OG  
4144  N N   . LEU A 564  ? 0.2674 0.3740 0.2428 0.0533  0.0297  -0.0098 562  LEU A N   
4145  C CA  . LEU A 564  ? 0.2665 0.3685 0.2413 0.0548  0.0275  -0.0161 562  LEU A CA  
4146  C C   . LEU A 564  ? 0.2731 0.3754 0.2510 0.0577  0.0262  -0.0236 562  LEU A C   
4147  O O   . LEU A 564  ? 0.2726 0.3791 0.2500 0.0605  0.0250  -0.0299 562  LEU A O   
4148  C CB  . LEU A 564  ? 0.2769 0.3648 0.2521 0.0520  0.0260  -0.0141 562  LEU A CB  
4149  C CG  . LEU A 564  ? 0.3337 0.4162 0.3079 0.0526  0.0238  -0.0186 562  LEU A CG  
4150  C CD1 . LEU A 564  ? 0.3148 0.4063 0.2853 0.0537  0.0245  -0.0187 562  LEU A CD1 
4151  C CD2 . LEU A 564  ? 0.2853 0.3552 0.2600 0.0495  0.0228  -0.0153 562  LEU A CD2 
4152  N N   . THR A 565  ? 0.2583 0.3567 0.2397 0.0573  0.0262  -0.0232 563  THR A N   
4153  C CA  . THR A 565  ? 0.2730 0.3719 0.2579 0.0602  0.0248  -0.0301 563  THR A CA  
4154  C C   . THR A 565  ? 0.2640 0.3774 0.2480 0.0638  0.0257  -0.0349 563  THR A C   
4155  O O   . THR A 565  ? 0.2911 0.4059 0.2766 0.0667  0.0238  -0.0424 563  THR A O   
4156  C CB  . THR A 565  ? 0.2675 0.3627 0.2560 0.0592  0.0252  -0.0279 563  THR A CB  
4157  O OG1 . THR A 565  ? 0.2755 0.3574 0.2651 0.0561  0.0240  -0.0245 563  THR A OG1 
4158  C CG2 . THR A 565  ? 0.3092 0.4061 0.3019 0.0624  0.0237  -0.0351 563  THR A CG2 
4159  N N   . GLU A 566  ? 0.2679 0.3925 0.2496 0.0637  0.0284  -0.0306 564  GLU A N   
4160  C CA  . GLU A 566  ? 0.2726 0.4125 0.2532 0.0672  0.0294  -0.0348 564  GLU A CA  
4161  C C   . GLU A 566  ? 0.2805 0.4251 0.2577 0.0687  0.0287  -0.0384 564  GLU A C   
4162  O O   . GLU A 566  ? 0.2667 0.4183 0.2445 0.0723  0.0277  -0.0460 564  GLU A O   
4163  C CB  . GLU A 566  ? 0.3150 0.4661 0.2942 0.0663  0.0325  -0.0284 564  GLU A CB  
4164  C CG  . GLU A 566  ? 0.3734 0.5209 0.3563 0.0651  0.0333  -0.0254 564  GLU A CG  
4165  C CD  . GLU A 566  ? 0.4634 0.6105 0.4506 0.0681  0.0319  -0.0330 564  GLU A CD  
4166  O OE1 . GLU A 566  ? 0.5121 0.6700 0.4992 0.0717  0.0319  -0.0393 564  GLU A OE1 
4167  O OE2 . GLU A 566  ? 0.4931 0.6291 0.4838 0.0669  0.0307  -0.0327 564  GLU A OE2 
4168  N N   . ALA A 567  ? 0.2744 0.4151 0.2483 0.0661  0.0289  -0.0331 565  ALA A N   
4169  C CA  . ALA A 567  ? 0.2868 0.4317 0.2575 0.0673  0.0281  -0.0361 565  ALA A CA  
4170  C C   . ALA A 567  ? 0.2432 0.3795 0.2162 0.0690  0.0249  -0.0440 565  ALA A C   
4171  O O   . ALA A 567  ? 0.2734 0.4163 0.2455 0.0718  0.0239  -0.0504 565  ALA A O   
4172  C CB  . ALA A 567  ? 0.2859 0.4271 0.2533 0.0640  0.0288  -0.0286 565  ALA A CB  
4173  N N   . LEU A 568  ? 0.2530 0.3752 0.2293 0.0672  0.0233  -0.0437 566  LEU A N   
4174  C CA  . LEU A 568  ? 0.2428 0.3566 0.2222 0.0684  0.0201  -0.0505 566  LEU A CA  
4175  C C   . LEU A 568  ? 0.2547 0.3746 0.2378 0.0724  0.0189  -0.0588 566  LEU A C   
4176  O O   . LEU A 568  ? 0.2794 0.4012 0.2636 0.0750  0.0168  -0.0660 566  LEU A O   
4177  C CB  . LEU A 568  ? 0.2495 0.3477 0.2317 0.0654  0.0187  -0.0475 566  LEU A CB  
4178  C CG  . LEU A 568  ? 0.2407 0.3315 0.2198 0.0616  0.0193  -0.0405 566  LEU A CG  
4179  C CD1 . LEU A 568  ? 0.2543 0.3316 0.2364 0.0588  0.0182  -0.0375 566  LEU A CD1 
4180  C CD2 . LEU A 568  ? 0.2887 0.3788 0.2655 0.0619  0.0179  -0.0428 566  LEU A CD2 
4181  N N   . ARG A 569  ? 0.2544 0.3776 0.2399 0.0730  0.0201  -0.0581 567  ARG A N   
4182  C CA  . ARG A 569  ? 0.2849 0.4154 0.2741 0.0770  0.0192  -0.0661 567  ARG A CA  
4183  C C   . ARG A 569  ? 0.2929 0.4386 0.2791 0.0803  0.0200  -0.0707 567  ARG A C   
4184  O O   . ARG A 569  ? 0.3072 0.4563 0.2960 0.0837  0.0178  -0.0794 567  ARG A O   
4185  C CB  . ARG A 569  ? 0.2918 0.4252 0.2833 0.0770  0.0210  -0.0635 567  ARG A CB  
4186  C CG  . ARG A 569  ? 0.3190 0.4381 0.3144 0.0745  0.0196  -0.0607 567  ARG A CG  
4187  C CD  . ARG A 569  ? 0.3906 0.5132 0.3881 0.0744  0.0215  -0.0579 567  ARG A CD  
4188  N NE  . ARG A 569  ? 0.3918 0.5012 0.3927 0.0718  0.0203  -0.0547 567  ARG A NE  
4189  C CZ  . ARG A 569  ? 0.4880 0.5972 0.4904 0.0706  0.0218  -0.0506 567  ARG A CZ  
4190  N NH1 . ARG A 569  ? 0.5538 0.6752 0.5550 0.0716  0.0245  -0.0488 567  ARG A NH1 
4191  N NH2 . ARG A 569  ? 0.5504 0.6475 0.5558 0.0684  0.0204  -0.0481 567  ARG A NH2 
4192  N N   . GLU A 570  ? 0.2556 0.4110 0.2366 0.0792  0.0229  -0.0649 568  GLU A N   
4193  C CA  . GLU A 570  ? 0.2723 0.4436 0.2500 0.0821  0.0239  -0.0685 568  GLU A CA  
4194  C C   . GLU A 570  ? 0.3169 0.4855 0.2934 0.0831  0.0215  -0.0736 568  GLU A C   
4195  O O   . GLU A 570  ? 0.3314 0.5100 0.3078 0.0868  0.0206  -0.0812 568  GLU A O   
4196  C CB  . GLU A 570  ? 0.3259 0.5070 0.2985 0.0801  0.0273  -0.0599 568  GLU A CB  
4197  C CG  . GLU A 570  ? 0.3365 0.5255 0.3103 0.0802  0.0298  -0.0566 568  GLU A CG  
4198  C CD  . GLU A 570  ? 0.5156 0.7114 0.4855 0.0774  0.0329  -0.0465 568  GLU A CD  
4199  O OE1 . GLU A 570  ? 0.5968 0.7886 0.5636 0.0749  0.0329  -0.0415 568  GLU A OE1 
4200  O OE2 . GLU A 570  ? 0.6360 0.8411 0.6066 0.0776  0.0351  -0.0435 568  GLU A OE2 
4201  N N   . SER A 571  ? 0.2901 0.4455 0.2658 0.0800  0.0203  -0.0697 569  SER A N   
4202  C CA  . SER A 571  ? 0.3221 0.4745 0.2970 0.0807  0.0179  -0.0742 569  SER A CA  
4203  C C   . SER A 571  ? 0.3130 0.4611 0.2937 0.0837  0.0144  -0.0840 569  SER A C   
4204  O O   . SER A 571  ? 0.3338 0.4857 0.3145 0.0861  0.0125  -0.0906 569  SER A O   
4205  C CB  . SER A 571  ? 0.2824 0.4213 0.2558 0.0766  0.0174  -0.0678 569  SER A CB  
4206  O OG  . SER A 571  ? 0.2935 0.4179 0.2718 0.0752  0.0152  -0.0685 569  SER A OG  
4207  N N   . ALA A 572  ? 0.3307 0.4710 0.3167 0.0836  0.0134  -0.0851 570  ALA A N   
4208  C CA  . ALA A 572  ? 0.3251 0.4605 0.3176 0.0862  0.0098  -0.0940 570  ALA A CA  
4209  C C   . ALA A 572  ? 0.4148 0.5642 0.4093 0.0911  0.0096  -0.1026 570  ALA A C   
4210  O O   . ALA A 572  ? 0.4268 0.5742 0.4269 0.0939  0.0063  -0.1112 570  ALA A O   
4211  C CB  . ALA A 572  ? 0.3872 0.5096 0.3850 0.0844  0.0085  -0.0919 570  ALA A CB  
4212  N N   . ALA A 573  ? 0.3364 0.5002 0.3268 0.0921  0.0129  -0.1004 571  ALA A N   
4213  C CA  . ALA A 573  ? 0.4188 0.5983 0.4101 0.0968  0.0131  -0.1084 571  ALA A CA  
4214  C C   . ALA A 573  ? 0.4859 0.6757 0.4729 0.0977  0.0127  -0.1106 571  ALA A C   
4215  O O   . ALA A 573  ? 0.4443 0.6450 0.4324 0.0996  0.0115  -0.1152 571  ALA A O   
4216  C CB  . ALA A 573  ? 0.3919 0.5818 0.3818 0.0969  0.0167  -0.1041 571  ALA A CB  
4217  N N   . MET A 574  ? 0.3947 0.5810 0.3772 0.0960  0.0133  -0.1071 572  MET A N   
4218  C CA  . MET A 574  ? 0.3938 0.5888 0.3724 0.0963  0.0125  -0.1083 572  MET A CA  
4219  C C   . MET A 574  ? 0.4193 0.6095 0.4027 0.0981  0.0079  -0.1172 572  MET A C   
4220  O O   . MET A 574  ? 0.3520 0.5292 0.3405 0.0982  0.0054  -0.1206 572  MET A O   
4221  C CB  . MET A 574  ? 0.4316 0.6248 0.4037 0.0937  0.0149  -0.1006 572  MET A CB  
4222  C CG  . MET A 574  ? 0.4432 0.6433 0.4108 0.0913  0.0190  -0.0908 572  MET A CG  
4223  S SD  . MET A 574  ? 0.4415 0.6337 0.4040 0.0862  0.0204  -0.0792 572  MET A SD  
4224  C CE  . MET A 574  ? 0.5730 0.7753 0.5326 0.0843  0.0247  -0.0694 572  MET A CE  
4225  N N   . LYS A 575  ? 0.4190 0.6204 0.4011 0.0994  0.0065  -0.1209 573  LYS A N   
4226  C CA  . LYS A 575  ? 0.4436 0.6426 0.4304 0.1012  0.0020  -0.1295 573  LYS A CA  
4227  C C   . LYS A 575  ? 0.3771 0.5721 0.3604 0.0999  0.0013  -0.1281 573  LYS A C   
4228  O O   . LYS A 575  ? 0.3931 0.5976 0.3734 0.1004  0.0008  -0.1292 573  LYS A O   
4229  C CB  . LYS A 575  ? 0.4503 0.6640 0.4386 0.1038  0.0006  -0.1352 573  LYS A CB  
4230  N N   . TRP A 576  ? 0.3230 0.5036 0.3067 0.0981  0.0013  -0.1255 574  TRP A N   
4231  C CA  . TRP A 576  ? 0.2909 0.4661 0.2712 0.0966  0.0009  -0.1234 574  TRP A CA  
4232  C C   . TRP A 576  ? 0.2813 0.4557 0.2658 0.0981  -0.0036 -0.1313 574  TRP A C   
4233  O O   . TRP A 576  ? 0.3163 0.4843 0.3082 0.0993  -0.0071 -0.1376 574  TRP A O   
4234  C CB  . TRP A 576  ? 0.2893 0.4484 0.2706 0.0943  0.0012  -0.1195 574  TRP A CB  
4235  C CG  . TRP A 576  ? 0.2721 0.4290 0.2502 0.0911  0.0047  -0.1093 574  TRP A CG  
4236  C CD1 . TRP A 576  ? 0.2833 0.4334 0.2651 0.0900  0.0052  -0.1068 574  TRP A CD1 
4237  C CD2 . TRP A 576  ? 0.2675 0.4293 0.2387 0.0885  0.0081  -0.1003 574  TRP A CD2 
4238  N NE1 . TRP A 576  ? 0.3072 0.4575 0.2847 0.0869  0.0086  -0.0971 574  TRP A NE1 
4239  C CE2 . TRP A 576  ? 0.2896 0.4468 0.2609 0.0859  0.0104  -0.0929 574  TRP A CE2 
4240  C CE3 . TRP A 576  ? 0.2784 0.4478 0.2437 0.0880  0.0092  -0.0977 574  TRP A CE3 
4241  C CZ2 . TRP A 576  ? 0.2804 0.4400 0.2465 0.0829  0.0136  -0.0831 574  TRP A CZ2 
4242  C CZ3 . TRP A 576  ? 0.2838 0.4556 0.2440 0.0851  0.0123  -0.0878 574  TRP A CZ3 
4243  C CH2 . TRP A 576  ? 0.3031 0.4700 0.2639 0.0825  0.0145  -0.0807 574  TRP A CH2 
4244  N N   . THR A 577  ? 0.2809 0.4618 0.2610 0.0978  -0.0036 -0.1307 575  THR A N   
4245  C CA  . THR A 577  ? 0.2666 0.4465 0.2504 0.0990  -0.0078 -0.1376 575  THR A CA  
4246  C C   . THR A 577  ? 0.3020 0.4788 0.2810 0.0973  -0.0074 -0.1342 575  THR A C   
4247  O O   . THR A 577  ? 0.3132 0.4927 0.2852 0.0955  -0.0039 -0.1267 575  THR A O   
4248  C CB  . THR A 577  ? 0.3101 0.5054 0.2950 0.1016  -0.0092 -0.1430 575  THR A CB  
4249  O OG1 . THR A 577  ? 0.3426 0.5504 0.3199 0.1010  -0.0061 -0.1376 575  THR A OG1 
4250  C CG2 . THR A 577  ? 0.3397 0.5395 0.3293 0.1035  -0.0096 -0.1467 575  THR A CG2 
4251  N N   . ALA A 578  ? 0.3067 0.4778 0.2899 0.0978  -0.0113 -0.1397 576  ALA A N   
4252  C CA  . ALA A 578  ? 0.2922 0.4615 0.2717 0.0965  -0.0117 -0.1380 576  ALA A CA  
4253  C C   . ALA A 578  ? 0.3335 0.5090 0.3170 0.0986  -0.0156 -0.1457 576  ALA A C   
4254  O O   . ALA A 578  ? 0.3132 0.4838 0.3047 0.0999  -0.0193 -0.1524 576  ALA A O   
4255  C CB  . ALA A 578  ? 0.2825 0.4350 0.2639 0.0945  -0.0129 -0.1366 576  ALA A CB  
4256  N N   . LEU A 579  ? 0.3016 0.4880 0.2800 0.0988  -0.0148 -0.1444 577  LEU A N   
4257  C CA  . LEU A 579  ? 0.3254 0.5201 0.3069 0.1010  -0.0180 -0.1513 577  LEU A CA  
4258  C C   . LEU A 579  ? 0.3468 0.5402 0.3246 0.0998  -0.0185 -0.1495 577  LEU A C   
4259  O O   . LEU A 579  ? 0.3040 0.4950 0.2752 0.0975  -0.0155 -0.1421 577  LEU A O   
4260  C CB  . LEU A 579  ? 0.3105 0.5233 0.2895 0.1029  -0.0166 -0.1519 577  LEU A CB  
4261  C CG  . LEU A 579  ? 0.3653 0.5823 0.3462 0.1040  -0.0152 -0.1522 577  LEU A CG  
4262  C CD1 . LEU A 579  ? 0.3732 0.6090 0.3516 0.1059  -0.0141 -0.1529 577  LEU A CD1 
4263  C CD2 . LEU A 579  ? 0.4135 0.6225 0.4037 0.1055  -0.0190 -0.1599 577  LEU A CD2 
4264  N N   . PRO A 580  ? 0.3187 0.5139 0.3008 0.1012  -0.0223 -0.1562 578  PRO A N   
4265  C CA  . PRO A 580  ? 0.2731 0.4704 0.2514 0.1004  -0.0226 -0.1547 578  PRO A CA  
4266  C C   . PRO A 580  ? 0.3644 0.5777 0.3357 0.1008  -0.0197 -0.1505 578  PRO A C   
4267  O O   . PRO A 580  ? 0.3871 0.6136 0.3600 0.1033  -0.0207 -0.1549 578  PRO A O   
4268  C CB  . PRO A 580  ? 0.3497 0.5468 0.3357 0.1024  -0.0276 -0.1637 578  PRO A CB  
4269  C CG  . PRO A 580  ? 0.3306 0.5219 0.3249 0.1037  -0.0300 -0.1692 578  PRO A CG  
4270  C CD  . PRO A 580  ? 0.3139 0.5110 0.3048 0.1038  -0.0265 -0.1654 578  PRO A CD  
4271  N N   . GLN A 581  ? 0.2924 0.5050 0.2563 0.0985  -0.0160 -0.1417 579  GLN A N   
4272  C CA  . GLN A 581  ? 0.3070 0.5340 0.2643 0.0983  -0.0130 -0.1361 579  GLN A CA  
4273  C C   . GLN A 581  ? 0.3084 0.5385 0.2626 0.0978  -0.0139 -0.1351 579  GLN A C   
4274  O O   . GLN A 581  ? 0.3361 0.5612 0.2854 0.0954  -0.0122 -0.1285 579  GLN A O   
4275  C CB  . GLN A 581  ? 0.3004 0.5250 0.2522 0.0959  -0.0087 -0.1267 579  GLN A CB  
4276  C CG  . GLN A 581  ? 0.2844 0.5062 0.2390 0.0964  -0.0076 -0.1271 579  GLN A CG  
4277  C CD  . GLN A 581  ? 0.3162 0.5533 0.2717 0.0985  -0.0072 -0.1293 579  GLN A CD  
4278  O OE1 . GLN A 581  ? 0.3175 0.5680 0.2712 0.0996  -0.0074 -0.1298 579  GLN A OE1 
4279  N NE2 . GLN A 581  ? 0.3492 0.5850 0.3078 0.0992  -0.0065 -0.1306 579  GLN A NE2 
4280  N N   . LEU A 582  ? 0.3171 0.5560 0.2746 0.1002  -0.0167 -0.1419 580  LEU A N   
4281  C CA  . LEU A 582  ? 0.3248 0.5688 0.2800 0.1001  -0.0178 -0.1418 580  LEU A CA  
4282  C C   . LEU A 582  ? 0.3438 0.6023 0.2923 0.0996  -0.0146 -0.1347 580  LEU A C   
4283  O O   . LEU A 582  ? 0.3849 0.6514 0.3317 0.0998  -0.0121 -0.1313 580  LEU A O   
4284  C CB  . LEU A 582  ? 0.3483 0.5973 0.3099 0.1030  -0.0219 -0.1518 580  LEU A CB  
4285  C CG  . LEU A 582  ? 0.4439 0.6787 0.4117 0.1029  -0.0258 -0.1577 580  LEU A CG  
4286  C CD1 . LEU A 582  ? 0.4300 0.6507 0.4019 0.1020  -0.0261 -0.1583 580  LEU A CD1 
4287  C CD2 . LEU A 582  ? 0.4615 0.7034 0.4360 0.1060  -0.0298 -0.1673 580  LEU A CD2 
4288  N N   . ALA A 583  ? 0.3240 0.5859 0.2691 0.0989  -0.0147 -0.1322 581  ALA A N   
4289  C CA  . ALA A 583  ? 0.3644 0.6403 0.3040 0.0983  -0.0121 -0.1252 581  ALA A CA  
4290  C C   . ALA A 583  ? 0.3698 0.6627 0.3112 0.1010  -0.0124 -0.1290 581  ALA A C   
4291  O O   . ALA A 583  ? 0.4494 0.7540 0.3872 0.1005  -0.0097 -0.1228 581  ALA A O   
4292  C CB  . ALA A 583  ? 0.3703 0.6475 0.3071 0.0975  -0.0130 -0.1234 581  ALA A CB  
4293  N N   . THR A 584  ? 0.3594 0.6542 0.3069 0.1038  -0.0157 -0.1390 582  THR A N   
4294  C CA  . THR A 584  ? 0.3854 0.6965 0.3355 0.1068  -0.0165 -0.1441 582  THR A CA  
4295  C C   . THR A 584  ? 0.4261 0.7381 0.3785 0.1076  -0.0156 -0.1453 582  THR A C   
4296  O O   . THR A 584  ? 0.4338 0.7596 0.3884 0.1101  -0.0161 -0.1493 582  THR A O   
4297  C CB  . THR A 584  ? 0.4122 0.7251 0.3685 0.1096  -0.0209 -0.1547 582  THR A CB  
4298  O OG1 . THR A 584  ? 0.4944 0.7909 0.4561 0.1096  -0.0234 -0.1600 582  THR A OG1 
4299  C CG2 . THR A 584  ? 0.4019 0.7179 0.3557 0.1093  -0.0218 -0.1538 582  THR A CG2 
4300  N N   . GLY A 585  ? 0.3962 0.6941 0.3484 0.1057  -0.0142 -0.1421 583  GLY A N   
4301  C CA  . GLY A 585  ? 0.4082 0.7057 0.3629 0.1064  -0.0134 -0.1432 583  GLY A CA  
4302  C C   . GLY A 585  ? 0.4093 0.6911 0.3700 0.1068  -0.0159 -0.1493 583  GLY A C   
4303  O O   . GLY A 585  ? 0.4153 0.6872 0.3788 0.1066  -0.0185 -0.1530 583  GLY A O   
4304  N N   . PRO A 586  ? 0.3699 0.6493 0.3332 0.1072  -0.0152 -0.1504 584  PRO A N   
4305  C CA  . PRO A 586  ? 0.3793 0.6441 0.3491 0.1076  -0.0177 -0.1559 584  PRO A CA  
4306  C C   . PRO A 586  ? 0.4468 0.7128 0.4239 0.1102  -0.0225 -0.1662 584  PRO A C   
4307  O O   . PRO A 586  ? 0.4216 0.7021 0.4003 0.1128  -0.0238 -0.1710 584  PRO A O   
4308  C CB  . PRO A 586  ? 0.4548 0.7216 0.4259 0.1081  -0.0161 -0.1554 584  PRO A CB  
4309  C CG  . PRO A 586  ? 0.5055 0.7857 0.4699 0.1073  -0.0122 -0.1478 584  PRO A CG  
4310  C CD  . PRO A 586  ? 0.4200 0.7115 0.3814 0.1079  -0.0126 -0.1474 584  PRO A CD  
4311  N N   . ALA A 587  ? 0.3687 0.6196 0.3507 0.1096  -0.0253 -0.1696 585  ALA A N   
4312  C CA  . ALA A 587  ? 0.4049 0.6545 0.3949 0.1117  -0.0301 -0.1791 585  ALA A CA  
4313  C C   . ALA A 587  ? 0.4279 0.6687 0.4260 0.1127  -0.0326 -0.1844 585  ALA A C   
4314  O O   . ALA A 587  ? 0.4144 0.6452 0.4119 0.1110  -0.0308 -0.1803 585  ALA A O   
4315  C CB  . ALA A 587  ? 0.4339 0.6730 0.4242 0.1102  -0.0320 -0.1789 585  ALA A CB  
4316  N N   . ALA A 588  ? 0.4049 0.6500 0.4110 0.1154  -0.0368 -0.1934 586  ALA A N   
4317  C CA  . ALA A 588  ? 0.3533 0.5901 0.3682 0.1163  -0.0397 -0.1988 586  ALA A CA  
4318  C C   . ALA A 588  ? 0.3918 0.6105 0.4117 0.1145  -0.0424 -0.1993 586  ALA A C   
4319  O O   . ALA A 588  ? 0.4491 0.6636 0.4669 0.1131  -0.0429 -0.1976 586  ALA A O   
4320  C CB  . ALA A 588  ? 0.3687 0.6167 0.3910 0.1200  -0.0435 -0.2085 586  ALA A CB  
4321  N N   . GLY A 589  ? 0.3931 0.6014 0.4199 0.1143  -0.0443 -0.2014 587  GLY A N   
4322  C CA  . GLY A 589  ? 0.3800 0.5714 0.4127 0.1125  -0.0472 -0.2018 587  GLY A CA  
4323  C C   . GLY A 589  ? 0.4228 0.6047 0.4629 0.1124  -0.0489 -0.2034 587  GLY A C   
4324  O O   . GLY A 589  ? 0.4584 0.6472 0.4996 0.1141  -0.0482 -0.2053 587  GLY A O   
4325  N N   . GLU A 590  ? 0.4574 0.6235 0.5027 0.1103  -0.0512 -0.2024 588  GLU A N   
4326  C CA  . GLU A 590  ? 0.4085 0.5641 0.4613 0.1098  -0.0529 -0.2030 588  GLU A CA  
4327  C C   . GLU A 590  ? 0.3804 0.5329 0.4264 0.1082  -0.0481 -0.1958 588  GLU A C   
4328  O O   . GLU A 590  ? 0.3750 0.5219 0.4137 0.1057  -0.0449 -0.1888 588  GLU A O   
4329  C CB  . GLU A 590  ? 0.4742 0.6141 0.5343 0.1077  -0.0566 -0.2029 588  GLU A CB  
4330  N N   . THR A 591  ? 0.3666 0.5226 0.4153 0.1096  -0.0478 -0.1975 589  THR A N   
4331  C CA  . THR A 591  ? 0.3924 0.5472 0.4354 0.1085  -0.0434 -0.1914 589  THR A CA  
4332  C C   . THR A 591  ? 0.3878 0.5288 0.4381 0.1073  -0.0451 -0.1907 589  THR A C   
4333  O O   . THR A 591  ? 0.4066 0.5451 0.4668 0.1086  -0.0495 -0.1966 589  THR A O   
4334  C CB  . THR A 591  ? 0.3921 0.5627 0.4320 0.1110  -0.0412 -0.1933 589  THR A CB  
4335  O OG1 . THR A 591  ? 0.4238 0.6076 0.4568 0.1118  -0.0395 -0.1930 589  THR A OG1 
4336  C CG2 . THR A 591  ? 0.3932 0.5627 0.4280 0.1099  -0.0368 -0.1871 589  THR A CG2 
4337  N N   . ARG A 592  ? 0.3236 0.4558 0.3692 0.1048  -0.0418 -0.1834 590  ARG A N   
4338  C CA  . ARG A 592  ? 0.3807 0.5004 0.4325 0.1036  -0.0430 -0.1817 590  ARG A CA  
4339  C C   . ARG A 592  ? 0.3478 0.4666 0.3922 0.1023  -0.0378 -0.1745 590  ARG A C   
4340  O O   . ARG A 592  ? 0.3512 0.4762 0.3860 0.1018  -0.0337 -0.1700 590  ARG A O   
4341  C CB  . ARG A 592  ? 0.3916 0.4962 0.4489 0.1012  -0.0462 -0.1804 590  ARG A CB  
4342  C CG  . ARG A 592  ? 0.4372 0.5362 0.4865 0.0986  -0.0432 -0.1737 590  ARG A CG  
4343  C CD  . ARG A 592  ? 0.4418 0.5246 0.4969 0.0959  -0.0459 -0.1712 590  ARG A CD  
4344  N NE  . ARG A 592  ? 0.4659 0.5443 0.5138 0.0936  -0.0436 -0.1659 590  ARG A NE  
4345  C CZ  . ARG A 592  ? 0.4681 0.5437 0.5087 0.0920  -0.0394 -0.1592 590  ARG A CZ  
4346  N NH1 . ARG A 592  ? 0.4429 0.5189 0.4822 0.0923  -0.0368 -0.1566 590  ARG A NH1 
4347  N NH2 . ARG A 592  ? 0.4800 0.5521 0.5145 0.0901  -0.0377 -0.1550 590  ARG A NH2 
4348  N N   . THR A 593  ? 0.3461 0.4573 0.3954 0.1019  -0.0383 -0.1734 591  THR A N   
4349  C CA  . THR A 593  ? 0.3418 0.4512 0.3851 0.1007  -0.0337 -0.1667 591  THR A CA  
4350  C C   . THR A 593  ? 0.3720 0.4694 0.4122 0.0977  -0.0324 -0.1602 591  THR A C   
4351  O O   . THR A 593  ? 0.3746 0.4621 0.4194 0.0963  -0.0356 -0.1609 591  THR A O   
4352  C CB  . THR A 593  ? 0.3854 0.4909 0.4353 0.1013  -0.0346 -0.1676 591  THR A CB  
4353  O OG1 . THR A 593  ? 0.3899 0.4822 0.4494 0.1001  -0.0392 -0.1692 591  THR A OG1 
4354  C CG2 . THR A 593  ? 0.4224 0.5407 0.4748 0.1043  -0.0355 -0.1737 591  THR A CG2 
4355  N N   . VAL A 594  ? 0.3102 0.4088 0.3427 0.0967  -0.0276 -0.1539 592  VAL A N   
4356  C CA  . VAL A 594  ? 0.3095 0.3972 0.3387 0.0941  -0.0258 -0.1474 592  VAL A CA  
4357  C C   . VAL A 594  ? 0.3463 0.4274 0.3783 0.0928  -0.0248 -0.1432 592  VAL A C   
4358  O O   . VAL A 594  ? 0.3329 0.4219 0.3620 0.0941  -0.0218 -0.1421 592  VAL A O   
4359  C CB  . VAL A 594  ? 0.3068 0.4012 0.3251 0.0925  -0.0213 -0.1410 592  VAL A CB  
4360  C CG1 . VAL A 594  ? 0.3295 0.4120 0.3450 0.0873  -0.0199 -0.1305 592  VAL A CG1 
4361  C CG2 . VAL A 594  ? 0.3439 0.4456 0.3594 0.0939  -0.0224 -0.1453 592  VAL A CG2 
4362  N N   . LEU A 595  ? 0.3179 0.3850 0.3559 0.0901  -0.0275 -0.1402 593  LEU A N   
4363  C CA  . LEU A 595  ? 0.3250 0.3851 0.3669 0.0886  -0.0273 -0.1363 593  LEU A CA  
4364  C C   . LEU A 595  ? 0.3131 0.3650 0.3497 0.0836  -0.0245 -0.1251 593  LEU A C   
4365  O O   . LEU A 595  ? 0.3253 0.3717 0.3594 0.0808  -0.0247 -0.1211 593  LEU A O   
4366  C CB  . LEU A 595  ? 0.3230 0.3735 0.3765 0.0893  -0.0326 -0.1411 593  LEU A CB  
4367  C CG  . LEU A 595  ? 0.3439 0.4001 0.4045 0.0928  -0.0365 -0.1509 593  LEU A CG  
4368  C CD1 . LEU A 595  ? 0.3929 0.4383 0.4653 0.0918  -0.0418 -0.1526 593  LEU A CD1 
4369  C CD2 . LEU A 595  ? 0.3619 0.4308 0.4207 0.0955  -0.0345 -0.1539 593  LEU A CD2 
4370  N N   . ASN A 596  ? 0.2972 0.3486 0.3326 0.0826  -0.0220 -0.1203 594  ASN A N   
4371  C CA  . ASN A 596  ? 0.2868 0.3305 0.3183 0.0780  -0.0197 -0.1102 594  ASN A CA  
4372  C C   . ASN A 596  ? 0.2738 0.3039 0.3115 0.0752  -0.0232 -0.1081 594  ASN A C   
4373  O O   . ASN A 596  ? 0.2870 0.3123 0.3331 0.0762  -0.0264 -0.1113 594  ASN A O   
4374  C CB  . ASN A 596  ? 0.2934 0.3394 0.3246 0.0782  -0.0173 -0.1074 594  ASN A CB  
4375  C CG  . ASN A 596  ? 0.3040 0.3441 0.3303 0.0739  -0.0143 -0.0973 594  ASN A CG  
4376  O OD1 . ASN A 596  ? 0.2967 0.3275 0.3230 0.0705  -0.0152 -0.0926 594  ASN A OD1 
4377  N ND2 . ASN A 596  ? 0.3363 0.3823 0.3587 0.0740  -0.0109 -0.0940 594  ASN A ND2 
4378  N N   . PRO A 597  ? 0.2662 0.2902 0.3005 0.0717  -0.0228 -0.1025 595  PRO A N   
4379  C CA  . PRO A 597  ? 0.2643 0.2763 0.3046 0.0689  -0.0262 -0.1002 595  PRO A CA  
4380  C C   . PRO A 597  ? 0.3047 0.3098 0.3484 0.0668  -0.0263 -0.0953 595  PRO A C   
4381  O O   . PRO A 597  ? 0.2711 0.2676 0.3221 0.0654  -0.0298 -0.0949 595  PRO A O   
4382  C CB  . PRO A 597  ? 0.2766 0.2857 0.3108 0.0656  -0.0246 -0.0945 595  PRO A CB  
4383  C CG  . PRO A 597  ? 0.2921 0.3094 0.3171 0.0657  -0.0199 -0.0912 595  PRO A CG  
4384  C CD  . PRO A 597  ? 0.2458 0.2740 0.2710 0.0701  -0.0194 -0.0979 595  PRO A CD  
4385  N N   . GLY A 598  ? 0.2610 0.2699 0.2999 0.0666  -0.0226 -0.0915 596  GLY A N   
4386  C CA  . GLY A 598  ? 0.2718 0.2749 0.3137 0.0648  -0.0226 -0.0870 596  GLY A CA  
4387  C C   . GLY A 598  ? 0.3100 0.3149 0.3590 0.0678  -0.0245 -0.0924 596  GLY A C   
4388  O O   . GLY A 598  ? 0.3054 0.3050 0.3580 0.0665  -0.0251 -0.0891 596  GLY A O   
4389  N N   . ASP A 599  ? 0.2858 0.2983 0.3370 0.0720  -0.0257 -0.1006 597  ASP A N   
4390  C CA  . ASP A 599  ? 0.3030 0.3182 0.3613 0.0755  -0.0277 -0.1068 597  ASP A CA  
4391  C C   . ASP A 599  ? 0.2757 0.2994 0.3355 0.0798  -0.0291 -0.1163 597  ASP A C   
4392  O O   . ASP A 599  ? 0.3047 0.3394 0.3584 0.0820  -0.0260 -0.1183 597  ASP A O   
4393  C CB  . ASP A 599  ? 0.3169 0.3378 0.3713 0.0760  -0.0239 -0.1040 597  ASP A CB  
4394  C CG  . ASP A 599  ? 0.3363 0.3593 0.3983 0.0793  -0.0259 -0.1097 597  ASP A CG  
4395  O OD1 . ASP A 599  ? 0.3279 0.3511 0.3974 0.0822  -0.0298 -0.1175 597  ASP A OD1 
4396  O OD2 . ASP A 599  ? 0.3855 0.4102 0.4464 0.0789  -0.0237 -0.1064 597  ASP A OD2 
4397  N N   . HIS A 600  ? 0.2795 0.2985 0.3478 0.0810  -0.0340 -0.1220 598  HIS A N   
4398  C CA  . HIS A 600  ? 0.3181 0.3447 0.3885 0.0851  -0.0359 -0.1315 598  HIS A CA  
4399  C C   . HIS A 600  ? 0.3550 0.3924 0.4271 0.0898  -0.0353 -0.1389 598  HIS A C   
4400  O O   . HIS A 600  ? 0.3652 0.4118 0.4366 0.0929  -0.0358 -0.1459 598  HIS A O   
4401  C CB  . HIS A 600  ? 0.3568 0.3751 0.4371 0.0852  -0.0416 -0.1358 598  HIS A CB  
4402  C CG  . HIS A 600  ? 0.3768 0.3875 0.4546 0.0812  -0.0421 -0.1302 598  HIS A CG  
4403  N ND1 . HIS A 600  ? 0.4247 0.4268 0.5109 0.0801  -0.0470 -0.1319 598  HIS A ND1 
4404  C CD2 . HIS A 600  ? 0.3601 0.3708 0.4283 0.0780  -0.0384 -0.1230 598  HIS A CD2 
4405  C CE1 . HIS A 600  ? 0.4540 0.4516 0.5356 0.0765  -0.0461 -0.1259 598  HIS A CE1 
4406  N NE2 . HIS A 600  ? 0.4074 0.4099 0.4781 0.0752  -0.0410 -0.1207 598  HIS A NE2 
4407  N N   . ARG A 601  ? 0.3397 0.3768 0.4137 0.0900  -0.0342 -0.1368 599  ARG A N   
4408  C CA  . ARG A 601  ? 0.3589 0.4071 0.4337 0.0943  -0.0331 -0.1430 599  ARG A CA  
4409  C C   . ARG A 601  ? 0.4050 0.4656 0.4689 0.0950  -0.0277 -0.1411 599  ARG A C   
4410  O O   . ARG A 601  ? 0.3658 0.4382 0.4289 0.0979  -0.0267 -0.1459 599  ARG A O   
4411  C CB  . ARG A 601  ? 0.3590 0.4030 0.4389 0.0940  -0.0333 -0.1405 599  ARG A CB  
4412  C CG  . ARG A 601  ? 0.3619 0.3935 0.4526 0.0926  -0.0385 -0.1407 599  ARG A CG  
4413  C CD  . ARG A 601  ? 0.3822 0.4089 0.4763 0.0916  -0.0382 -0.1363 599  ARG A CD  
4414  N NE  . ARG A 601  ? 0.3609 0.3847 0.4462 0.0872  -0.0340 -0.1258 599  ARG A NE  
4415  C CZ  . ARG A 601  ? 0.4110 0.4311 0.4967 0.0854  -0.0327 -0.1200 599  ARG A CZ  
4416  N NH1 . ARG A 601  ? 0.4075 0.4262 0.5017 0.0873  -0.0352 -0.1233 599  ARG A NH1 
4417  N NH2 . ARG A 601  ? 0.3673 0.3852 0.4450 0.0815  -0.0290 -0.1110 599  ARG A NH2 
4418  N N   . ASP A 602  ? 0.3322 0.3906 0.3876 0.0911  -0.0245 -0.1325 600  ASP A N   
4419  C CA  . ASP A 602  ? 0.3450 0.4143 0.3903 0.0911  -0.0195 -0.1292 600  ASP A CA  
4420  C C   . ASP A 602  ? 0.3579 0.4337 0.3995 0.0925  -0.0198 -0.1334 600  ASP A C   
4421  O O   . ASP A 602  ? 0.3591 0.4289 0.3977 0.0897  -0.0201 -0.1295 600  ASP A O   
4422  C CB  . ASP A 602  ? 0.3459 0.4091 0.3848 0.0862  -0.0162 -0.1179 600  ASP A CB  
4423  C CG  . ASP A 602  ? 0.3608 0.4346 0.3901 0.0859  -0.0113 -0.1138 600  ASP A CG  
4424  O OD1 . ASP A 602  ? 0.3669 0.4536 0.3948 0.0895  -0.0100 -0.1188 600  ASP A OD1 
4425  O OD2 . ASP A 602  ? 0.3554 0.4251 0.3790 0.0821  -0.0089 -0.1054 600  ASP A OD2 
4426  N N   . VAL A 603  ? 0.3352 0.4237 0.3770 0.0970  -0.0199 -0.1416 601  VAL A N   
4427  C CA  . VAL A 603  ? 0.3370 0.4334 0.3748 0.0980  -0.0201 -0.1449 601  VAL A CA  
4428  C C   . VAL A 603  ? 0.3479 0.4530 0.3750 0.0971  -0.0149 -0.1390 601  VAL A C   
4429  O O   . VAL A 603  ? 0.3646 0.4788 0.3881 0.0980  -0.0116 -0.1371 601  VAL A O   
4430  C CB  . VAL A 603  ? 0.3875 0.4939 0.4294 0.1006  -0.0226 -0.1524 601  VAL A CB  
4431  C CG1 . VAL A 603  ? 0.3733 0.4887 0.4107 0.1013  -0.0228 -0.1551 601  VAL A CG1 
4432  C CG2 . VAL A 603  ? 0.3739 0.4713 0.4270 0.1009  -0.0281 -0.1574 601  VAL A CG2 
4433  N N   . VAL A 604  ? 0.2988 0.4004 0.3209 0.0944  -0.0144 -0.1347 602  VAL A N   
4434  C CA  . VAL A 604  ? 0.3187 0.4266 0.3312 0.0924  -0.0100 -0.1272 602  VAL A CA  
4435  C C   . VAL A 604  ? 0.3016 0.4249 0.3094 0.0955  -0.0089 -0.1321 602  VAL A C   
4436  O O   . VAL A 604  ? 0.3200 0.4541 0.3212 0.0956  -0.0051 -0.1283 602  VAL A O   
4437  C CB  . VAL A 604  ? 0.2921 0.3884 0.3017 0.0877  -0.0099 -0.1194 602  VAL A CB  
4438  C CG1 . VAL A 604  ? 0.2728 0.3748 0.2733 0.0855  -0.0056 -0.1114 602  VAL A CG1 
4439  C CG2 . VAL A 604  ? 0.3049 0.3870 0.3193 0.0847  -0.0111 -0.1148 602  VAL A CG2 
4440  N N   . GLY A 605  ? 0.2891 0.4133 0.3006 0.0973  -0.0126 -0.1395 603  GLY A N   
4441  C CA  . GLY A 605  ? 0.2939 0.4316 0.3017 0.0987  -0.0124 -0.1421 603  GLY A CA  
4442  C C   . GLY A 605  ? 0.3001 0.4361 0.3138 0.0998  -0.0173 -0.1494 603  GLY A C   
4443  O O   . GLY A 605  ? 0.3282 0.4543 0.3502 0.0999  -0.0211 -0.1532 603  GLY A O   
4444  N N   . SER A 606  ? 0.2904 0.4364 0.3001 0.1005  -0.0173 -0.1510 604  SER A N   
4445  C CA  A SER A 606  ? 0.2981 0.4447 0.3131 0.1018  -0.0218 -0.1581 604  SER A CA  
4446  C CA  B SER A 606  ? 0.2987 0.4457 0.3136 0.1018  -0.0218 -0.1582 604  SER A CA  
4447  C C   . SER A 606  ? 0.3253 0.4741 0.3346 0.1008  -0.0213 -0.1563 604  SER A C   
4448  O O   . SER A 606  ? 0.3312 0.4886 0.3322 0.1003  -0.0176 -0.1514 604  SER A O   
4449  C CB  A SER A 606  ? 0.3122 0.4722 0.3301 0.1047  -0.0232 -0.1645 604  SER A CB  
4450  C CB  B SER A 606  ? 0.3110 0.4724 0.3279 0.1048  -0.0228 -0.1640 604  SER A CB  
4451  O OG  A SER A 606  ? 0.3282 0.4853 0.3526 0.1058  -0.0245 -0.1671 604  SER A OG  
4452  O OG  B SER A 606  ? 0.3056 0.4698 0.3270 0.1062  -0.0269 -0.1709 604  SER A OG  
4453  N N   . VAL A 607  ? 0.3004 0.4411 0.3146 0.1004  -0.0252 -0.1599 605  VAL A N   
4454  C CA  . VAL A 607  ? 0.2941 0.4360 0.3039 0.0996  -0.0253 -0.1589 605  VAL A CA  
4455  C C   . VAL A 607  ? 0.3188 0.4667 0.3341 0.1017  -0.0296 -0.1668 605  VAL A C   
4456  O O   . VAL A 607  ? 0.3106 0.4529 0.3351 0.1026  -0.0337 -0.1724 605  VAL A O   
4457  C CB  . VAL A 607  ? 0.3044 0.4312 0.3142 0.0968  -0.0258 -0.1551 605  VAL A CB  
4458  C CG1 . VAL A 607  ? 0.3297 0.4438 0.3499 0.0965  -0.0303 -0.1590 605  VAL A CG1 
4459  C CG2 . VAL A 607  ? 0.3007 0.4295 0.3063 0.0961  -0.0262 -0.1546 605  VAL A CG2 
4460  N N   . THR A 608  ? 0.3230 0.4824 0.3329 0.1024  -0.0287 -0.1671 606  THR A N   
4461  C CA  . THR A 608  ? 0.3546 0.5195 0.3688 0.1042  -0.0325 -0.1739 606  THR A CA  
4462  C C   . THR A 608  ? 0.3253 0.4835 0.3370 0.1023  -0.0331 -0.1717 606  THR A C   
4463  O O   . THR A 608  ? 0.3126 0.4740 0.3157 0.1009  -0.0297 -0.1658 606  THR A O   
4464  C CB  . THR A 608  ? 0.3256 0.5089 0.3356 0.1065  -0.0310 -0.1756 606  THR A CB  
4465  O OG1 . THR A 608  ? 0.3380 0.5273 0.3503 0.1081  -0.0304 -0.1775 606  THR A OG1 
4466  C CG2 . THR A 608  ? 0.3824 0.5722 0.3969 0.1085  -0.0350 -0.1830 606  THR A CG2 
4467  N N   . GLU A 609  ? 0.3242 0.4731 0.3437 0.1021  -0.0375 -0.1761 607  GLU A N   
4468  C CA  . GLU A 609  ? 0.3723 0.5133 0.3902 0.1001  -0.0384 -0.1739 607  GLU A CA  
4469  C C   . GLU A 609  ? 0.3327 0.4835 0.3498 0.1015  -0.0401 -0.1779 607  GLU A C   
4470  O O   . GLU A 609  ? 0.3139 0.4754 0.3344 0.1042  -0.0420 -0.1840 607  GLU A O   
4471  C CB  . GLU A 609  ? 0.4044 0.5291 0.4308 0.0985  -0.0420 -0.1750 607  GLU A CB  
4472  C CG  . GLU A 609  ? 0.4075 0.5225 0.4326 0.0966  -0.0394 -0.1692 607  GLU A CG  
4473  C CD  . GLU A 609  ? 0.5033 0.6023 0.5368 0.0947  -0.0428 -0.1692 607  GLU A CD  
4474  O OE1 . GLU A 609  ? 0.5630 0.6595 0.6060 0.0956  -0.0475 -0.1750 607  GLU A OE1 
4475  O OE2 . GLU A 609  ? 0.4672 0.5565 0.4980 0.0923  -0.0408 -0.1633 607  GLU A OE2 
4476  N N   . THR A 610  ? 0.3340 0.4815 0.3463 0.0997  -0.0393 -0.1743 608  THR A N   
4477  C CA  . THR A 610  ? 0.3275 0.4845 0.3370 0.1007  -0.0400 -0.1763 608  THR A CA  
4478  C C   . THR A 610  ? 0.4026 0.5542 0.4211 0.1012  -0.0453 -0.1828 608  THR A C   
4479  O O   . THR A 610  ? 0.3947 0.5324 0.4177 0.0992  -0.0474 -0.1820 608  THR A O   
4480  C CB  . THR A 610  ? 0.3224 0.4777 0.3228 0.0982  -0.0368 -0.1691 608  THR A CB  
4481  O OG1 . THR A 610  ? 0.3262 0.4842 0.3192 0.0973  -0.0321 -0.1623 608  THR A OG1 
4482  C CG2 . THR A 610  ? 0.3521 0.5187 0.3487 0.0993  -0.0371 -0.1704 608  THR A CG2 
4483  N N   . SER A 611  ? 0.3470 0.5100 0.3685 0.1039  -0.0476 -0.1891 609  SER A N   
4484  C CA  . SER A 611  ? 0.3987 0.5580 0.4283 0.1045  -0.0525 -0.1950 609  SER A CA  
4485  C C   . SER A 611  ? 0.4150 0.5706 0.4396 0.1025  -0.0520 -0.1914 609  SER A C   
4486  O O   . SER A 611  ? 0.3588 0.5198 0.3737 0.1016  -0.0481 -0.1859 609  SER A O   
4487  C CB  . SER A 611  ? 0.4049 0.5786 0.4384 0.1081  -0.0549 -0.2027 609  SER A CB  
4488  O OG  . SER A 611  ? 0.4270 0.6131 0.4525 0.1088  -0.0525 -0.2011 609  SER A OG  
4489  N N   . GLU A 612  ? 0.4060 0.5524 0.4378 0.1016  -0.0560 -0.1943 610  GLU A N   
4490  C CA  . GLU A 612  ? 0.4163 0.5591 0.4441 0.0997  -0.0559 -0.1914 610  GLU A CA  
4491  C C   . GLU A 612  ? 0.4035 0.5609 0.4266 0.1017  -0.0553 -0.1934 610  GLU A C   
4492  O O   . GLU A 612  ? 0.4055 0.5639 0.4212 0.1002  -0.0532 -0.1889 610  GLU A O   
4493  C CB  . GLU A 612  ? 0.5311 0.6610 0.5682 0.0983  -0.0605 -0.1939 610  GLU A CB  
4494  C CG  . GLU A 612  ? 0.5165 0.6309 0.5552 0.0953  -0.0600 -0.1888 610  GLU A CG  
4495  C CD  . GLU A 612  ? 0.5758 0.6786 0.6265 0.0943  -0.0651 -0.1920 610  GLU A CD  
4496  O OE1 . GLU A 612  ? 0.6362 0.7335 0.6896 0.0929  -0.0675 -0.1921 610  GLU A OE1 
4497  O OE2 . GLU A 612  ? 0.6495 0.7488 0.7073 0.0950  -0.0668 -0.1941 610  GLU A OE2 
4498  N N   . GLU A 613  ? 0.3947 0.5640 0.4218 0.1050  -0.0570 -0.1999 611  GLU A N   
4499  C CA  . GLU A 613  ? 0.4563 0.6410 0.4788 0.1070  -0.0561 -0.2016 611  GLU A CA  
4500  C C   . GLU A 613  ? 0.3726 0.5660 0.3837 0.1064  -0.0508 -0.1947 611  GLU A C   
4501  O O   . GLU A 613  ? 0.3619 0.5618 0.3662 0.1059  -0.0489 -0.1914 611  GLU A O   
4502  C CB  . GLU A 613  ? 0.4639 0.6597 0.4938 0.1107  -0.0593 -0.2104 611  GLU A CB  
4503  N N   . ASP A 614  ? 0.3754 0.5694 0.3848 0.1064  -0.0483 -0.1922 612  ASP A N   
4504  C CA  . ASP A 614  ? 0.2949 0.4972 0.2942 0.1057  -0.0433 -0.1852 612  ASP A CA  
4505  C C   . ASP A 614  ? 0.3151 0.5080 0.3072 0.1023  -0.0404 -0.1768 612  ASP A C   
4506  O O   . ASP A 614  ? 0.3293 0.5297 0.3129 0.1015  -0.0369 -0.1708 612  ASP A O   
4507  C CB  . ASP A 614  ? 0.3595 0.5643 0.3593 0.1065  -0.0415 -0.1848 612  ASP A CB  
4508  C CG  . ASP A 614  ? 0.3584 0.5766 0.3632 0.1101  -0.0435 -0.1922 612  ASP A CG  
4509  O OD1 . ASP A 614  ? 0.3987 0.6290 0.4028 0.1119  -0.0444 -0.1953 612  ASP A OD1 
4510  O OD2 . ASP A 614  ? 0.4227 0.6396 0.4323 0.1112  -0.0442 -0.1951 612  ASP A OD2 
4511  N N   . ALA A 615  ? 0.3169 0.4938 0.3127 0.1002  -0.0419 -0.1761 613  ALA A N   
4512  C CA  . ALA A 615  ? 0.3342 0.5023 0.3238 0.0971  -0.0396 -0.1688 613  ALA A CA  
4513  C C   . ALA A 615  ? 0.3096 0.4826 0.2954 0.0968  -0.0400 -0.1680 613  ALA A C   
4514  O O   . ALA A 615  ? 0.3064 0.4826 0.2837 0.0953  -0.0368 -0.1614 613  ALA A O   
4515  C CB  . ALA A 615  ? 0.3185 0.4691 0.3138 0.0950  -0.0418 -0.1689 613  ALA A CB  
4516  N N   . ARG A 616  ? 0.3593 0.5331 0.3515 0.0981  -0.0441 -0.1747 614  ARG A N   
4517  C CA  . ARG A 616  ? 0.3825 0.5621 0.3715 0.0982  -0.0447 -0.1746 614  ARG A CA  
4518  C C   . ARG A 616  ? 0.3102 0.5070 0.2925 0.0998  -0.0419 -0.1727 614  ARG A C   
4519  O O   . ARG A 616  ? 0.3351 0.5360 0.3104 0.0986  -0.0399 -0.1676 614  ARG A O   
4520  C CB  . ARG A 616  ? 0.3972 0.5754 0.3952 0.0997  -0.0497 -0.1828 614  ARG A CB  
4521  C CG  . ARG A 616  ? 0.4826 0.6443 0.4861 0.0973  -0.0525 -0.1830 614  ARG A CG  
4522  C CD  . ARG A 616  ? 0.5602 0.7207 0.5739 0.0989  -0.0577 -0.1910 614  ARG A CD  
4523  N NE  . ARG A 616  ? 0.6130 0.7656 0.6363 0.0993  -0.0605 -0.1950 614  ARG A NE  
4524  C CZ  . ARG A 616  ? 0.5297 0.6888 0.5600 0.1023  -0.0630 -0.2019 614  ARG A CZ  
4525  N NH1 . ARG A 616  ? 0.5909 0.7651 0.6202 0.1052  -0.0632 -0.2061 614  ARG A NH1 
4526  N NH2 . ARG A 616  ? 0.5684 0.7191 0.6074 0.1023  -0.0656 -0.2046 614  ARG A NH2 
4527  N N   . ARG A 617  ? 0.2884 0.4955 0.2729 0.1023  -0.0418 -0.1763 615  ARG A N   
4528  C CA  . ARG A 617  ? 0.3209 0.5449 0.2994 0.1037  -0.0391 -0.1740 615  ARG A CA  
4529  C C   . ARG A 617  ? 0.3299 0.5541 0.2993 0.1013  -0.0343 -0.1641 615  ARG A C   
4530  O O   . ARG A 617  ? 0.3228 0.5568 0.2858 0.1010  -0.0322 -0.1594 615  ARG A O   
4531  C CB  . ARG A 617  ? 0.3492 0.5835 0.3322 0.1067  -0.0399 -0.1797 615  ARG A CB  
4532  C CG  . ARG A 617  ? 0.4423 0.6953 0.4202 0.1084  -0.0376 -0.1781 615  ARG A CG  
4533  C CD  . ARG A 617  ? 0.4646 0.7290 0.4489 0.1120  -0.0401 -0.1867 615  ARG A CD  
4534  N NE  . ARG A 617  ? 0.5270 0.7871 0.5156 0.1127  -0.0403 -0.1889 615  ARG A NE  
4535  C CZ  . ARG A 617  ? 0.5617 0.8298 0.5470 0.1131  -0.0374 -0.1859 615  ARG A CZ  
4536  N NH1 . ARG A 617  ? 0.5742 0.8549 0.5521 0.1128  -0.0340 -0.1801 615  ARG A NH1 
4537  N NH2 . ARG A 617  ? 0.5034 0.7671 0.4934 0.1138  -0.0380 -0.1887 615  ARG A NH2 
4538  N N   . ALA A 618  ? 0.3184 0.5319 0.2873 0.0996  -0.0327 -0.1606 616  ALA A N   
4539  C CA  . ALA A 618  ? 0.3227 0.5360 0.2836 0.0974  -0.0283 -0.1511 616  ALA A CA  
4540  C C   . ALA A 618  ? 0.2842 0.4937 0.2397 0.0950  -0.0275 -0.1455 616  ALA A C   
4541  O O   . ALA A 618  ? 0.2962 0.5129 0.2447 0.0940  -0.0244 -0.1384 616  ALA A O   
4542  C CB  . ALA A 618  ? 0.3281 0.5296 0.2904 0.0960  -0.0271 -0.1491 616  ALA A CB  
4543  N N   . VAL A 619  ? 0.2856 0.4839 0.2446 0.0941  -0.0303 -0.1485 617  VAL A N   
4544  C CA  . VAL A 619  ? 0.2985 0.4931 0.2527 0.0920  -0.0298 -0.1436 617  VAL A CA  
4545  C C   . VAL A 619  ? 0.3023 0.5109 0.2531 0.0931  -0.0297 -0.1433 617  VAL A C   
4546  O O   . VAL A 619  ? 0.3128 0.5250 0.2570 0.0916  -0.0274 -0.1362 617  VAL A O   
4547  C CB  . VAL A 619  ? 0.2983 0.4783 0.2575 0.0908  -0.0332 -0.1471 617  VAL A CB  
4548  C CG1 . VAL A 619  ? 0.3324 0.5093 0.2865 0.0886  -0.0327 -0.1422 617  VAL A CG1 
4549  C CG2 . VAL A 619  ? 0.3029 0.4693 0.2652 0.0894  -0.0330 -0.1465 617  VAL A CG2 
4550  N N   . ARG A 620  ? 0.2894 0.5068 0.2451 0.0959  -0.0323 -0.1507 618  ARG A N   
4551  C CA  . ARG A 620  ? 0.3447 0.5765 0.2976 0.0972  -0.0322 -0.1507 618  ARG A CA  
4552  C C   . ARG A 620  ? 0.3122 0.5567 0.2588 0.0972  -0.0283 -0.1440 618  ARG A C   
4553  O O   . ARG A 620  ? 0.3315 0.5837 0.2728 0.0964  -0.0268 -0.1386 618  ARG A O   
4554  C CB  . ARG A 620  ? 0.3590 0.5980 0.3189 0.1004  -0.0358 -0.1604 618  ARG A CB  
4555  C CG  . ARG A 620  ? 0.4125 0.6409 0.3785 0.1003  -0.0399 -0.1662 618  ARG A CG  
4556  C CD  . ARG A 620  ? 0.4989 0.7353 0.4720 0.1035  -0.0435 -0.1756 618  ARG A CD  
4557  N NE  . ARG A 620  ? 0.6091 0.8368 0.5911 0.1045  -0.0466 -0.1822 618  ARG A NE  
4558  C CZ  . ARG A 620  ? 0.5277 0.7618 0.5141 0.1069  -0.0473 -0.1872 618  ARG A CZ  
4559  N NH1 . ARG A 620  ? 0.5767 0.8267 0.5599 0.1089  -0.0453 -0.1869 618  ARG A NH1 
4560  N NH2 . ARG A 620  ? 0.5204 0.7450 0.5152 0.1074  -0.0502 -0.1924 618  ARG A NH2 
4561  N N   . LEU A 621  ? 0.2873 0.5340 0.2348 0.0978  -0.0268 -0.1438 619  LEU A N   
4562  C CA  . LEU A 621  ? 0.3200 0.5783 0.2619 0.0975  -0.0231 -0.1369 619  LEU A CA  
4563  C C   . LEU A 621  ? 0.2998 0.5521 0.2352 0.0943  -0.0200 -0.1267 619  LEU A C   
4564  O O   . LEU A 621  ? 0.3308 0.5930 0.2611 0.0935  -0.0177 -0.1199 619  LEU A O   
4565  C CB  . LEU A 621  ? 0.3272 0.5878 0.2719 0.0988  -0.0222 -0.1390 619  LEU A CB  
4566  C CG  . LEU A 621  ? 0.3223 0.5914 0.2734 0.1023  -0.0249 -0.1486 619  LEU A CG  
4567  C CD1 . LEU A 621  ? 0.3363 0.6028 0.2908 0.1031  -0.0245 -0.1509 619  LEU A CD1 
4568  C CD2 . LEU A 621  ? 0.3592 0.6477 0.3080 0.1041  -0.0242 -0.1483 619  LEU A CD2 
4569  N N   . ALA A 622  ? 0.3091 0.5455 0.2450 0.0923  -0.0201 -0.1254 620  ALA A N   
4570  C CA  . ALA A 622  ? 0.3143 0.5441 0.2444 0.0893  -0.0176 -0.1163 620  ALA A CA  
4571  C C   . ALA A 622  ? 0.2853 0.5182 0.2120 0.0884  -0.0182 -0.1133 620  ALA A C   
4572  O O   . ALA A 622  ? 0.3003 0.5374 0.2217 0.0867  -0.0157 -0.1048 620  ALA A O   
4573  C CB  . ALA A 622  ? 0.2983 0.5106 0.2302 0.0877  -0.0181 -0.1168 620  ALA A CB  
4574  N N   . ALA A 623  ? 0.3054 0.5361 0.2358 0.0894  -0.0215 -0.1201 621  ALA A N   
4575  C CA  . ALA A 623  ? 0.3084 0.5419 0.2359 0.0887  -0.0223 -0.1178 621  ALA A CA  
4576  C C   . ALA A 623  ? 0.3069 0.5578 0.2312 0.0897  -0.0209 -0.1145 621  ALA A C   
4577  O O   . ALA A 623  ? 0.3219 0.5764 0.2415 0.0881  -0.0195 -0.1074 621  ALA A O   
4578  C CB  . ALA A 623  ? 0.3699 0.5983 0.3027 0.0898  -0.0264 -0.1263 621  ALA A CB  
4579  N N   . ASP A 624  ? 0.3121 0.5743 0.2393 0.0923  -0.0212 -0.1194 622  ASP A N   
4580  C CA  . ASP A 624  ? 0.3663 0.6461 0.2908 0.0933  -0.0198 -0.1164 622  ASP A CA  
4581  C C   . ASP A 624  ? 0.3887 0.6723 0.3081 0.0912  -0.0160 -0.1058 622  ASP A C   
4582  O O   . ASP A 624  ? 0.4410 0.7350 0.3570 0.0905  -0.0147 -0.0996 622  ASP A O   
4583  C CB  . ASP A 624  ? 0.4369 0.7278 0.3660 0.0966  -0.0210 -0.1242 622  ASP A CB  
4584  C CG  . ASP A 624  ? 0.5324 0.8217 0.4672 0.0989  -0.0250 -0.1346 622  ASP A CG  
4585  O OD1 . ASP A 624  ? 0.5746 0.8585 0.5092 0.0981  -0.0267 -0.1352 622  ASP A OD1 
4586  O OD2 . ASP A 624  ? 0.5607 0.8544 0.5006 0.1015  -0.0266 -0.1421 622  ASP A OD2 
4587  N N   . ALA A 625  ? 0.3895 0.6647 0.3089 0.0901  -0.0144 -0.1035 623  ALA A N   
4588  C CA  . ALA A 625  ? 0.4300 0.7079 0.3456 0.0882  -0.0109 -0.0938 623  ALA A CA  
4589  C C   . ALA A 625  ? 0.4218 0.6900 0.3334 0.0850  -0.0096 -0.0855 623  ALA A C   
4590  O O   . ALA A 625  ? 0.4568 0.7275 0.3653 0.0831  -0.0069 -0.0765 623  ALA A O   
4591  C CB  . ALA A 625  ? 0.4416 0.7140 0.3592 0.0885  -0.0097 -0.0954 623  ALA A CB  
4592  N N   . ALA A 626  ? 0.3592 0.6165 0.2711 0.0844  -0.0117 -0.0882 624  ALA A N   
4593  C CA  . ALA A 626  ? 0.3193 0.5664 0.2278 0.0815  -0.0108 -0.0808 624  ALA A CA  
4594  C C   . ALA A 626  ? 0.3832 0.6391 0.2877 0.0798  -0.0090 -0.0711 624  ALA A C   
4595  O O   . ALA A 626  ? 0.3756 0.6273 0.2776 0.0775  -0.0069 -0.0626 624  ALA A O   
4596  C CB  . ALA A 626  ? 0.3564 0.5915 0.2665 0.0813  -0.0136 -0.0862 624  ALA A CB  
4597  N N   . PRO A 627  ? 0.3702 0.6382 0.2743 0.0808  -0.0099 -0.0715 625  PRO A N   
4598  C CA  . PRO A 627  ? 0.3512 0.6269 0.2520 0.0790  -0.0084 -0.0615 625  PRO A CA  
4599  C C   . PRO A 627  ? 0.3433 0.6262 0.2432 0.0780  -0.0054 -0.0538 625  PRO A C   
4600  O O   . PRO A 627  ? 0.3907 0.6723 0.2885 0.0755  -0.0038 -0.0440 625  PRO A O   
4601  C CB  . PRO A 627  ? 0.3609 0.6492 0.2622 0.0808  -0.0100 -0.0652 625  PRO A CB  
4602  C CG  . PRO A 627  ? 0.3981 0.6802 0.3026 0.0829  -0.0130 -0.0764 625  PRO A CG  
4603  C CD  . PRO A 627  ? 0.3889 0.6634 0.2958 0.0835  -0.0126 -0.0807 625  PRO A CD  
4604  N N   . ASP A 628  ? 0.3698 0.6602 0.2717 0.0799  -0.0047 -0.0580 626  ASP A N   
4605  C CA  . ASP A 628  ? 0.3714 0.6699 0.2728 0.0791  -0.0020 -0.0509 626  ASP A CA  
4606  C C   . ASP A 628  ? 0.3884 0.6747 0.2890 0.0768  -0.0001 -0.0453 626  ASP A C   
4607  O O   . ASP A 628  ? 0.3895 0.6794 0.2892 0.0749  0.0021  -0.0361 626  ASP A O   
4608  C CB  . ASP A 628  ? 0.3562 0.6647 0.2601 0.0818  -0.0019 -0.0575 626  ASP A CB  
4609  C CG  . ASP A 628  ? 0.4185 0.7412 0.3235 0.0842  -0.0036 -0.0627 626  ASP A CG  
4610  O OD1 . ASP A 628  ? 0.4716 0.7968 0.3751 0.0835  -0.0045 -0.0603 626  ASP A OD1 
4611  O OD2 . ASP A 628  ? 0.5478 0.8790 0.4553 0.0867  -0.0041 -0.0692 626  ASP A OD2 
4612  N N   . TRP A 629  ? 0.3293 0.6013 0.2306 0.0769  -0.0011 -0.0506 627  TRP A N   
4613  C CA  . TRP A 629  ? 0.3402 0.6007 0.2408 0.0749  0.0007  -0.0457 627  TRP A CA  
4614  C C   . TRP A 629  ? 0.3549 0.6075 0.2530 0.0723  0.0007  -0.0381 627  TRP A C   
4615  O O   . TRP A 629  ? 0.3217 0.5712 0.2189 0.0700  0.0027  -0.0295 627  TRP A O   
4616  C CB  . TRP A 629  ? 0.3103 0.5593 0.2131 0.0762  -0.0003 -0.0542 627  TRP A CB  
4617  C CG  . TRP A 629  ? 0.2913 0.5285 0.1932 0.0742  0.0015  -0.0495 627  TRP A CG  
4618  C CD1 . TRP A 629  ? 0.2753 0.4966 0.1785 0.0728  0.0006  -0.0504 627  TRP A CD1 
4619  C CD2 . TRP A 629  ? 0.2617 0.5013 0.1632 0.0729  0.0044  -0.0423 627  TRP A CD2 
4620  N NE1 . TRP A 629  ? 0.2877 0.5000 0.1930 0.0704  0.0026  -0.0440 627  TRP A NE1 
4621  C CE2 . TRP A 629  ? 0.2724 0.4966 0.1754 0.0708  0.0050  -0.0394 627  TRP A CE2 
4622  C CE3 . TRP A 629  ? 0.2976 0.5498 0.1994 0.0729  0.0062  -0.0376 627  TRP A CE3 
4623  C CZ2 . TRP A 629  ? 0.2814 0.5027 0.1855 0.0688  0.0074  -0.0323 627  TRP A CZ2 
4624  C CZ3 . TRP A 629  ? 0.3070 0.5573 0.2089 0.0712  0.0087  -0.0307 627  TRP A CZ3 
4625  C CH2 . TRP A 629  ? 0.2993 0.5354 0.2009 0.0696  0.0095  -0.0285 627  TRP A CH2 
4626  N N   . ALA A 630  ? 0.3110 0.5606 0.2086 0.0725  -0.0015 -0.0412 628  ALA A N   
4627  C CA  . ALA A 630  ? 0.3487 0.5919 0.2441 0.0702  -0.0018 -0.0342 628  ALA A CA  
4628  C C   . ALA A 630  ? 0.3685 0.6215 0.2630 0.0684  -0.0003 -0.0236 628  ALA A C   
4629  O O   . ALA A 630  ? 0.3613 0.6088 0.2550 0.0661  0.0002  -0.0153 628  ALA A O   
4630  C CB  . ALA A 630  ? 0.3550 0.5954 0.2504 0.0710  -0.0047 -0.0398 628  ALA A CB  
4631  N N   . ALA A 631  ? 0.3431 0.6108 0.2384 0.0696  0.0002  -0.0236 629  ALA A N   
4632  C CA  . ALA A 631  ? 0.3390 0.6171 0.2341 0.0680  0.0014  -0.0137 629  ALA A CA  
4633  C C   . ALA A 631  ? 0.3508 0.6293 0.2468 0.0663  0.0039  -0.0059 629  ALA A C   
4634  O O   . ALA A 631  ? 0.3623 0.6471 0.2590 0.0644  0.0049  0.0036  629  ALA A O   
4635  C CB  . ALA A 631  ? 0.3433 0.6379 0.2390 0.0699  0.0009  -0.0167 629  ALA A CB  
4636  N N   . VAL A 632  ? 0.3284 0.6007 0.2250 0.0669  0.0050  -0.0096 630  VAL A N   
4637  C CA  . VAL A 632  ? 0.3130 0.5839 0.2107 0.0650  0.0073  -0.0020 630  VAL A CA  
4638  C C   . VAL A 632  ? 0.2949 0.5537 0.1921 0.0623  0.0073  0.0052  630  VAL A C   
4639  O O   . VAL A 632  ? 0.3304 0.5771 0.2265 0.0626  0.0063  0.0008  630  VAL A O   
4640  C CB  . VAL A 632  ? 0.3164 0.5835 0.2149 0.0664  0.0083  -0.0082 630  VAL A CB  
4641  C CG1 . VAL A 632  ? 0.3514 0.6166 0.2511 0.0644  0.0107  -0.0001 630  VAL A CG1 
4642  C CG2 . VAL A 632  ? 0.3310 0.6108 0.2306 0.0692  0.0079  -0.0154 630  VAL A CG2 
4643  N N   . PRO A 633  ? 0.3032 0.5648 0.2017 0.0598  0.0082  0.0160  631  PRO A N   
4644  C CA  . PRO A 633  ? 0.2965 0.5471 0.1952 0.0575  0.0078  0.0228  631  PRO A CA  
4645  C C   . PRO A 633  ? 0.2914 0.5256 0.1930 0.0564  0.0084  0.0209  631  PRO A C   
4646  O O   . PRO A 633  ? 0.2899 0.5246 0.1920 0.0570  0.0099  0.0187  631  PRO A O   
4647  C CB  . PRO A 633  ? 0.3446 0.6019 0.2463 0.0550  0.0087  0.0345  631  PRO A CB  
4648  C CG  . PRO A 633  ? 0.3582 0.6318 0.2603 0.0562  0.0091  0.0333  631  PRO A CG  
4649  C CD  . PRO A 633  ? 0.3392 0.6147 0.2396 0.0591  0.0094  0.0226  631  PRO A CD  
4650  N N   . PRO A 634  ? 0.2525 0.4715 0.1573 0.0546  0.0071  0.0214  632  PRO A N   
4651  C CA  . PRO A 634  ? 0.2856 0.4884 0.1943 0.0533  0.0076  0.0195  632  PRO A CA  
4652  C C   . PRO A 634  ? 0.2529 0.4553 0.1638 0.0517  0.0097  0.0258  632  PRO A C   
4653  O O   . PRO A 634  ? 0.2594 0.4550 0.1718 0.0519  0.0106  0.0220  632  PRO A O   
4654  C CB  . PRO A 634  ? 0.2919 0.4819 0.2035 0.0512  0.0061  0.0219  632  PRO A CB  
4655  C CG  . PRO A 634  ? 0.3192 0.5170 0.2280 0.0524  0.0043  0.0205  632  PRO A CG  
4656  C CD  . PRO A 634  ? 0.2952 0.5117 0.2001 0.0539  0.0051  0.0230  632  PRO A CD  
4657  N N   . SER A 635  ? 0.2822 0.4915 0.1938 0.0501  0.0103  0.0356  633  SER A N   
4658  C CA  . SER A 635  ? 0.3077 0.5166 0.2221 0.0485  0.0121  0.0419  633  SER A CA  
4659  C C   . SER A 635  ? 0.2798 0.4986 0.1917 0.0506  0.0139  0.0380  633  SER A C   
4660  O O   . SER A 635  ? 0.2901 0.5035 0.2042 0.0499  0.0152  0.0382  633  SER A O   
4661  C CB  . SER A 635  ? 0.4034 0.6202 0.3193 0.0466  0.0122  0.0532  633  SER A CB  
4662  O OG  . SER A 635  ? 0.5240 0.7589 0.4355 0.0483  0.0124  0.0543  633  SER A OG  
4663  N N   . GLU A 636  ? 0.2761 0.5096 0.1834 0.0531  0.0138  0.0340  634  GLU A N   
4664  C CA  . GLU A 636  ? 0.2816 0.5254 0.1866 0.0554  0.0154  0.0294  634  GLU A CA  
4665  C C   . GLU A 636  ? 0.2769 0.5111 0.1823 0.0572  0.0150  0.0186  634  GLU A C   
4666  O O   . GLU A 636  ? 0.2920 0.5264 0.1981 0.0579  0.0164  0.0161  634  GLU A O   
4667  C CB  . GLU A 636  ? 0.3137 0.5736 0.2180 0.0569  0.0149  0.0280  634  GLU A CB  
4668  C CG  . GLU A 636  ? 0.4151 0.6843 0.3198 0.0590  0.0159  0.0223  634  GLU A CG  
4669  C CD  . GLU A 636  ? 0.4889 0.7578 0.3960 0.0576  0.0180  0.0276  634  GLU A CD  
4670  O OE1 . GLU A 636  ? 0.4747 0.7451 0.3843 0.0550  0.0187  0.0378  634  GLU A OE1 
4671  O OE2 . GLU A 636  ? 0.4639 0.7310 0.3709 0.0592  0.0189  0.0216  634  GLU A OE2 
4672  N N   . ARG A 637  ? 0.2693 0.4948 0.1746 0.0578  0.0129  0.0123  635  ARG A N   
4673  C CA  . ARG A 637  ? 0.2562 0.4709 0.1631 0.0590  0.0123  0.0031  635  ARG A CA  
4674  C C   . ARG A 637  ? 0.2418 0.4425 0.1528 0.0567  0.0133  0.0062  635  ARG A C   
4675  O O   . ARG A 637  ? 0.2513 0.4487 0.1635 0.0576  0.0140  0.0016  635  ARG A O   
4676  C CB  . ARG A 637  ? 0.2498 0.4567 0.1567 0.0595  0.0098  -0.0029 635  ARG A CB  
4677  C CG  . ARG A 637  ? 0.2549 0.4759 0.1577 0.0619  0.0087  -0.0063 635  ARG A CG  
4678  C CD  . ARG A 637  ? 0.2807 0.4947 0.1838 0.0629  0.0061  -0.0142 635  ARG A CD  
4679  N NE  . ARG A 637  ? 0.2898 0.4901 0.1954 0.0602  0.0051  -0.0104 635  ARG A NE  
4680  C CZ  . ARG A 637  ? 0.2943 0.4961 0.1990 0.0597  0.0037  -0.0081 635  ARG A CZ  
4681  N NH1 . ARG A 637  ? 0.3238 0.5401 0.2247 0.0614  0.0031  -0.0086 635  ARG A NH1 
4682  N NH2 . ARG A 637  ? 0.2852 0.4737 0.1927 0.0574  0.0028  -0.0055 635  ARG A NH2 
4683  N N   . ALA A 638  ? 0.2439 0.4366 0.1575 0.0537  0.0132  0.0140  636  ALA A N   
4684  C CA  . ALA A 638  ? 0.2583 0.4382 0.1759 0.0515  0.0141  0.0173  636  ALA A CA  
4685  C C   . ALA A 638  ? 0.2430 0.4299 0.1611 0.0514  0.0162  0.0210  636  ALA A C   
4686  O O   . ALA A 638  ? 0.2407 0.4195 0.1613 0.0508  0.0170  0.0198  636  ALA A O   
4687  C CB  . ALA A 638  ? 0.2651 0.4371 0.1855 0.0486  0.0134  0.0249  636  ALA A CB  
4688  N N   . ALA A 639  ? 0.2430 0.4454 0.1588 0.0519  0.0172  0.0259  637  ALA A N   
4689  C CA  . ALA A 639  ? 0.2659 0.4764 0.1821 0.0519  0.0193  0.0294  637  ALA A CA  
4690  C C   . ALA A 639  ? 0.2700 0.4834 0.1849 0.0546  0.0199  0.0204  637  ALA A C   
4691  O O   . ALA A 639  ? 0.2696 0.4818 0.1863 0.0543  0.0214  0.0213  637  ALA A O   
4692  C CB  . ALA A 639  ? 0.2587 0.4865 0.1727 0.0519  0.0201  0.0366  637  ALA A CB  
4693  N N   . CYS A 640  ? 0.2518 0.4686 0.1639 0.0573  0.0187  0.0117  638  CYS A N   
4694  C CA  . CYS A 640  ? 0.2662 0.4840 0.1780 0.0600  0.0188  0.0023  638  CYS A CA  
4695  C C   . CYS A 640  ? 0.2529 0.4534 0.1686 0.0589  0.0185  -0.0003 638  CYS A C   
4696  O O   . CYS A 640  ? 0.2503 0.4502 0.1674 0.0596  0.0195  -0.0029 638  CYS A O   
4697  C CB  . CYS A 640  ? 0.2588 0.4813 0.1679 0.0630  0.0169  -0.0068 638  CYS A CB  
4698  S SG  . CYS A 640  ? 0.2933 0.5382 0.1977 0.0652  0.0172  -0.0063 638  CYS A SG  
4699  N N   . LEU A 641  ? 0.2426 0.4293 0.1601 0.0570  0.0170  0.0003  639  LEU A N   
4700  C CA  . LEU A 641  ? 0.2492 0.4199 0.1705 0.0556  0.0167  -0.0016 639  LEU A CA  
4701  C C   . LEU A 641  ? 0.2356 0.4035 0.1593 0.0536  0.0185  0.0052  639  LEU A C   
4702  O O   . LEU A 641  ? 0.2344 0.3962 0.1603 0.0536  0.0190  0.0025  639  LEU A O   
4703  C CB  . LEU A 641  ? 0.2445 0.4027 0.1672 0.0538  0.0149  -0.0012 639  LEU A CB  
4704  C CG  . LEU A 641  ? 0.2534 0.4072 0.1756 0.0555  0.0127  -0.0099 639  LEU A CG  
4705  C CD1 . LEU A 641  ? 0.2796 0.4469 0.1983 0.0581  0.0120  -0.0139 639  LEU A CD1 
4706  C CD2 . LEU A 641  ? 0.2298 0.3709 0.1539 0.0532  0.0114  -0.0082 639  LEU A CD2 
4707  N N   . ASP A 642  ? 0.2415 0.4136 0.1654 0.0516  0.0194  0.0143  640  ASP A N   
4708  C CA  . ASP A 642  ? 0.2400 0.4094 0.1669 0.0495  0.0209  0.0210  640  ASP A CA  
4709  C C   . ASP A 642  ? 0.2460 0.4257 0.1721 0.0512  0.0227  0.0197  640  ASP A C   
4710  O O   . ASP A 642  ? 0.2416 0.4157 0.1704 0.0503  0.0237  0.0204  640  ASP A O   
4711  C CB  . ASP A 642  ? 0.2495 0.4219 0.1775 0.0471  0.0212  0.0310  640  ASP A CB  
4712  C CG  . ASP A 642  ? 0.2739 0.4327 0.2046 0.0449  0.0197  0.0333  640  ASP A CG  
4713  O OD1 . ASP A 642  ? 0.2833 0.4293 0.2156 0.0446  0.0190  0.0287  640  ASP A OD1 
4714  O OD2 . ASP A 642  ? 0.3111 0.4725 0.2424 0.0435  0.0192  0.0399  640  ASP A OD2 
4715  N N   . ARG A 643  ? 0.2411 0.4362 0.1637 0.0536  0.0231  0.0174  641  ARG A N   
4716  C CA  . ARG A 643  ? 0.2485 0.4540 0.1703 0.0554  0.0248  0.0152  641  ARG A CA  
4717  C C   . ARG A 643  ? 0.2654 0.4635 0.1885 0.0573  0.0242  0.0059  641  ARG A C   
4718  O O   . ARG A 643  ? 0.2636 0.4621 0.1884 0.0576  0.0255  0.0054  641  ARG A O   
4719  C CB  . ARG A 643  ? 0.2572 0.4819 0.1748 0.0578  0.0253  0.0142  641  ARG A CB  
4720  C CG  . ARG A 643  ? 0.2556 0.4913 0.1725 0.0560  0.0264  0.0247  641  ARG A CG  
4721  C CD  . ARG A 643  ? 0.3045 0.5588 0.2187 0.0582  0.0266  0.0233  641  ARG A CD  
4722  N NE  . ARG A 643  ? 0.2830 0.5392 0.1947 0.0600  0.0246  0.0169  641  ARG A NE  
4723  C CZ  . ARG A 643  ? 0.2720 0.5312 0.1830 0.0590  0.0234  0.0211  641  ARG A CZ  
4724  N NH1 . ARG A 643  ? 0.3218 0.5813 0.2345 0.0560  0.0239  0.0317  641  ARG A NH1 
4725  N NH2 . ARG A 643  ? 0.3139 0.5755 0.2227 0.0609  0.0216  0.0144  641  ARG A NH2 
4726  N N   . ALA A 644  ? 0.2292 0.4203 0.1518 0.0585  0.0222  -0.0014 642  ALA A N   
4727  C CA  . ALA A 644  ? 0.2427 0.4257 0.1674 0.0600  0.0213  -0.0098 642  ALA A CA  
4728  C C   . ALA A 644  ? 0.2365 0.4050 0.1650 0.0575  0.0217  -0.0067 642  ALA A C   
4729  O O   . ALA A 644  ? 0.2446 0.4102 0.1752 0.0583  0.0221  -0.0103 642  ALA A O   
4730  C CB  . ALA A 644  ? 0.2568 0.4346 0.1809 0.0614  0.0189  -0.0174 642  ALA A CB  
4731  N N   . ALA A 645  ? 0.2236 0.3834 0.1533 0.0544  0.0215  -0.0001 643  ALA A N   
4732  C CA  . ALA A 645  ? 0.2330 0.3796 0.1664 0.0520  0.0218  0.0028  643  ALA A CA  
4733  C C   . ALA A 645  ? 0.2350 0.3866 0.1698 0.0515  0.0239  0.0074  643  ALA A C   
4734  O O   . ALA A 645  ? 0.2483 0.3924 0.1857 0.0510  0.0242  0.0060  643  ALA A O   
4735  C CB  . ALA A 645  ? 0.2498 0.3875 0.1843 0.0492  0.0211  0.0086  643  ALA A CB  
4736  N N   . GLU A 646  ? 0.2375 0.4014 0.1708 0.0513  0.0252  0.0134  644  GLU A N   
4737  C CA  . GLU A 646  ? 0.2542 0.4247 0.1888 0.0509  0.0272  0.0178  644  GLU A CA  
4738  C C   . GLU A 646  ? 0.2623 0.4381 0.1966 0.0537  0.0278  0.0105  644  GLU A C   
4739  O O   . GLU A 646  ? 0.2651 0.4378 0.2019 0.0532  0.0288  0.0111  644  GLU A O   
4740  C CB  . GLU A 646  ? 0.3025 0.4877 0.2354 0.0505  0.0284  0.0250  644  GLU A CB  
4741  C CG  . GLU A 646  ? 0.3644 0.5453 0.2989 0.0475  0.0279  0.0335  644  GLU A CG  
4742  C CD  . GLU A 646  ? 0.4934 0.6632 0.4326 0.0446  0.0282  0.0388  644  GLU A CD  
4743  O OE1 . GLU A 646  ? 0.5701 0.7412 0.5110 0.0446  0.0295  0.0394  644  GLU A OE1 
4744  O OE2 . GLU A 646  ? 0.4513 0.6110 0.3926 0.0425  0.0270  0.0421  644  GLU A OE2 
4745  N N   . LEU A 647  ? 0.2673 0.4512 0.1986 0.0567  0.0271  0.0034  645  LEU A N   
4746  C CA  . LEU A 647  ? 0.2515 0.4408 0.1829 0.0598  0.0274  -0.0043 645  LEU A CA  
4747  C C   . LEU A 647  ? 0.2810 0.4554 0.2159 0.0596  0.0261  -0.0095 645  LEU A C   
4748  O O   . LEU A 647  ? 0.2981 0.4728 0.2351 0.0605  0.0269  -0.0118 645  LEU A O   
4749  C CB  . LEU A 647  ? 0.2769 0.4773 0.2051 0.0631  0.0264  -0.0114 645  LEU A CB  
4750  C CG  . LEU A 647  ? 0.2746 0.4928 0.1991 0.0638  0.0278  -0.0071 645  LEU A CG  
4751  C CD1 . LEU A 647  ? 0.2873 0.5150 0.2084 0.0669  0.0265  -0.0145 645  LEU A CD1 
4752  C CD2 . LEU A 647  ? 0.3541 0.5847 0.2788 0.0644  0.0302  -0.0043 645  LEU A CD2 
4753  N N   . MET A 648  ? 0.2594 0.4210 0.1951 0.0585  0.0242  -0.0112 646  MET A N   
4754  C CA  . MET A 648  ? 0.2534 0.4011 0.1925 0.0581  0.0230  -0.0154 646  MET A CA  
4755  C C   . MET A 648  ? 0.2547 0.3950 0.1966 0.0555  0.0242  -0.0095 646  MET A C   
4756  O O   . MET A 648  ? 0.2766 0.4115 0.2212 0.0559  0.0241  -0.0126 646  MET A O   
4757  C CB  . MET A 648  ? 0.2426 0.3789 0.1820 0.0571  0.0208  -0.0177 646  MET A CB  
4758  C CG  . MET A 648  ? 0.2532 0.3945 0.1911 0.0600  0.0191  -0.0257 646  MET A CG  
4759  S SD  . MET A 648  ? 0.3057 0.4319 0.2455 0.0588  0.0163  -0.0293 646  MET A SD  
4760  C CE  . MET A 648  ? 0.3219 0.4570 0.2600 0.0625  0.0143  -0.0384 646  MET A CE  
4761  N N   . GLN A 649  ? 0.2589 0.3987 0.2006 0.0529  0.0252  -0.0011 647  GLN A N   
4762  C CA  . GLN A 649  ? 0.2601 0.3935 0.2048 0.0504  0.0263  0.0045  647  GLN A CA  
4763  C C   . GLN A 649  ? 0.2641 0.4063 0.2096 0.0516  0.0280  0.0047  647  GLN A C   
4764  O O   . GLN A 649  ? 0.2811 0.4167 0.2295 0.0511  0.0283  0.0041  647  GLN A O   
4765  C CB  . GLN A 649  ? 0.2554 0.3882 0.2004 0.0476  0.0268  0.0134  647  GLN A CB  
4766  C CG  . GLN A 649  ? 0.2580 0.3832 0.2066 0.0450  0.0275  0.0189  647  GLN A CG  
4767  C CD  . GLN A 649  ? 0.2659 0.3755 0.2167 0.0435  0.0261  0.0169  647  GLN A CD  
4768  O OE1 . GLN A 649  ? 0.2474 0.3506 0.1982 0.0420  0.0251  0.0187  647  GLN A OE1 
4769  N NE2 . GLN A 649  ? 0.2933 0.3972 0.2459 0.0438  0.0261  0.0133  647  GLN A NE2 
4770  N N   . ALA A 650  ? 0.2644 0.4218 0.2075 0.0533  0.0292  0.0055  648  ALA A N   
4771  C CA  . ALA A 650  ? 0.2770 0.4441 0.2208 0.0545  0.0310  0.0057  648  ALA A CA  
4772  C C   . ALA A 650  ? 0.3394 0.5051 0.2843 0.0573  0.0303  -0.0033 648  ALA A C   
4773  O O   . ALA A 650  ? 0.3330 0.4996 0.2802 0.0576  0.0313  -0.0035 648  ALA A O   
4774  C CB  . ALA A 650  ? 0.3076 0.4927 0.2483 0.0558  0.0324  0.0083  648  ALA A CB  
4775  N N   . ARG A 651  ? 0.2642 0.4276 0.2080 0.0593  0.0285  -0.0108 649  ARG A N   
4776  C CA  . ARG A 651  ? 0.2631 0.4258 0.2086 0.0622  0.0273  -0.0199 649  ARG A CA  
4777  C C   . ARG A 651  ? 0.2622 0.4082 0.2112 0.0609  0.0256  -0.0224 649  ARG A C   
4778  O O   . ARG A 651  ? 0.2967 0.4399 0.2478 0.0631  0.0242  -0.0299 649  ARG A O   
4779  C CB  . ARG A 651  ? 0.3178 0.4883 0.2608 0.0652  0.0260  -0.0272 649  ARG A CB  
4780  C CG  . ARG A 651  ? 0.3690 0.5437 0.3137 0.0690  0.0250  -0.0369 649  ARG A CG  
4781  C CD  . ARG A 651  ? 0.3672 0.5571 0.3089 0.0723  0.0248  -0.0424 649  ARG A CD  
4782  N NE  . ARG A 651  ? 0.3921 0.5856 0.3362 0.0761  0.0234  -0.0525 649  ARG A NE  
4783  C CZ  . ARG A 651  ? 0.4013 0.6027 0.3470 0.0780  0.0247  -0.0547 649  ARG A CZ  
4784  N NH1 . ARG A 651  ? 0.4369 0.6426 0.3822 0.0764  0.0273  -0.0474 649  ARG A NH1 
4785  N NH2 . ARG A 651  ? 0.4234 0.6283 0.3716 0.0817  0.0231  -0.0646 649  ARG A NH2 
4786  N N   . MET A 652  ? 0.2691 0.4042 0.2189 0.0575  0.0256  -0.0163 650  MET A N   
4787  C CA  . MET A 652  ? 0.2684 0.3881 0.2211 0.0562  0.0239  -0.0182 650  MET A CA  
4788  C C   . MET A 652  ? 0.2706 0.3873 0.2268 0.0574  0.0236  -0.0226 650  MET A C   
4789  O O   . MET A 652  ? 0.2836 0.3931 0.2419 0.0584  0.0215  -0.0286 650  MET A O   
4790  C CB  . MET A 652  ? 0.2731 0.3834 0.2265 0.0524  0.0243  -0.0107 650  MET A CB  
4791  C CG  . MET A 652  ? 0.2706 0.3663 0.2270 0.0509  0.0229  -0.0122 650  MET A CG  
4792  S SD  . MET A 652  ? 0.3104 0.3957 0.2678 0.0468  0.0232  -0.0043 650  MET A SD  
4793  C CE  . MET A 652  ? 0.2881 0.3724 0.2428 0.0464  0.0220  -0.0042 650  MET A CE  
4794  N N   . PRO A 653  ? 0.2760 0.3981 0.2333 0.0575  0.0254  -0.0200 651  PRO A N   
4795  C CA  . PRO A 653  ? 0.3142 0.4325 0.2752 0.0587  0.0248  -0.0242 651  PRO A CA  
4796  C C   . PRO A 653  ? 0.2997 0.4219 0.2616 0.0623  0.0232  -0.0335 651  PRO A C   
4797  O O   . PRO A 653  ? 0.2860 0.3994 0.2514 0.0628  0.0212  -0.0382 651  PRO A O   
4798  C CB  . PRO A 653  ? 0.2797 0.4063 0.2410 0.0584  0.0273  -0.0196 651  PRO A CB  
4799  C CG  . PRO A 653  ? 0.3168 0.4441 0.2762 0.0555  0.0287  -0.0110 651  PRO A CG  
4800  C CD  . PRO A 653  ? 0.2885 0.4188 0.2446 0.0562  0.0278  -0.0124 651  PRO A CD  
4801  N N   . THR A 654  ? 0.2639 0.3993 0.2232 0.0648  0.0238  -0.0363 652  THR A N   
4802  C CA  . THR A 654  ? 0.2695 0.4095 0.2300 0.0685  0.0220  -0.0458 652  THR A CA  
4803  C C   . THR A 654  ? 0.2759 0.4060 0.2371 0.0683  0.0191  -0.0499 652  THR A C   
4804  O O   . THR A 654  ? 0.2801 0.4051 0.2451 0.0700  0.0168  -0.0568 652  THR A O   
4805  C CB  . THR A 654  ? 0.2906 0.4480 0.2475 0.0711  0.0234  -0.0474 652  THR A CB  
4806  O OG1 . THR A 654  ? 0.3042 0.4709 0.2609 0.0712  0.0260  -0.0433 652  THR A OG1 
4807  C CG2 . THR A 654  ? 0.3304 0.4934 0.2889 0.0753  0.0214  -0.0579 652  THR A CG2 
4808  N N   . LEU A 655  ? 0.2630 0.3902 0.2213 0.0662  0.0192  -0.0456 653  LEU A N   
4809  C CA  . LEU A 655  ? 0.2714 0.3890 0.2305 0.0657  0.0166  -0.0487 653  LEU A CA  
4810  C C   . LEU A 655  ? 0.2845 0.3873 0.2479 0.0638  0.0150  -0.0488 653  LEU A C   
4811  O O   . LEU A 655  ? 0.2806 0.3768 0.2469 0.0647  0.0123  -0.0544 653  LEU A O   
4812  C CB  . LEU A 655  ? 0.2821 0.3990 0.2373 0.0634  0.0172  -0.0431 653  LEU A CB  
4813  C CG  . LEU A 655  ? 0.2747 0.4065 0.2257 0.0650  0.0185  -0.0425 653  LEU A CG  
4814  C CD1 . LEU A 655  ? 0.2726 0.4025 0.2205 0.0626  0.0188  -0.0366 653  LEU A CD1 
4815  C CD2 . LEU A 655  ? 0.3332 0.4720 0.2843 0.0688  0.0166  -0.0518 653  LEU A CD2 
4816  N N   . LEU A 656  ? 0.2966 0.3941 0.2606 0.0613  0.0165  -0.0426 654  LEU A N   
4817  C CA  . LEU A 656  ? 0.2897 0.3742 0.2577 0.0596  0.0151  -0.0424 654  LEU A CA  
4818  C C   . LEU A 656  ? 0.2887 0.3725 0.2611 0.0622  0.0132  -0.0497 654  LEU A C   
4819  O O   . LEU A 656  ? 0.2929 0.3674 0.2689 0.0619  0.0106  -0.0529 654  LEU A O   
4820  C CB  . LEU A 656  ? 0.3044 0.3859 0.2727 0.0571  0.0171  -0.0355 654  LEU A CB  
4821  C CG  . LEU A 656  ? 0.3160 0.3966 0.2813 0.0542  0.0189  -0.0277 654  LEU A CG  
4822  C CD1 . LEU A 656  ? 0.3412 0.4172 0.3082 0.0519  0.0202  -0.0223 654  LEU A CD1 
4823  C CD2 . LEU A 656  ? 0.2967 0.3692 0.2611 0.0524  0.0174  -0.0271 654  LEU A CD2 
4824  N N   . GLY A 657  ? 0.2851 0.3790 0.2579 0.0647  0.0144  -0.0522 655  GLY A N   
4825  C CA  . GLY A 657  ? 0.3028 0.3965 0.2805 0.0674  0.0126  -0.0591 655  GLY A CA  
4826  C C   . GLY A 657  ? 0.2679 0.3609 0.2477 0.0697  0.0095  -0.0670 655  GLY A C   
4827  O O   . GLY A 657  ? 0.2991 0.3847 0.2841 0.0703  0.0068  -0.0715 655  GLY A O   
4828  N N   . LEU A 658  ? 0.2715 0.3722 0.2475 0.0708  0.0097  -0.0686 656  LEU A N   
4829  C CA  . LEU A 658  ? 0.2870 0.3875 0.2651 0.0730  0.0067  -0.0762 656  LEU A CA  
4830  C C   . LEU A 658  ? 0.2508 0.3371 0.2311 0.0704  0.0043  -0.0750 656  LEU A C   
4831  O O   . LEU A 658  ? 0.2870 0.3672 0.2726 0.0714  0.0011  -0.0806 656  LEU A O   
4832  C CB  . LEU A 658  ? 0.2708 0.3834 0.2440 0.0747  0.0076  -0.0778 656  LEU A CB  
4833  C CG  . LEU A 658  ? 0.3058 0.4197 0.2807 0.0772  0.0045  -0.0860 656  LEU A CG  
4834  C CD1 . LEU A 658  ? 0.3135 0.4289 0.2945 0.0807  0.0021  -0.0949 656  LEU A CD1 
4835  C CD2 . LEU A 658  ? 0.2974 0.4248 0.2669 0.0789  0.0058  -0.0868 656  LEU A CD2 
4836  N N   . ILE A 659  ? 0.2608 0.3418 0.2376 0.0669  0.0057  -0.0676 657  ILE A N   
4837  C CA  . ILE A 659  ? 0.2591 0.3277 0.2378 0.0643  0.0037  -0.0659 657  ILE A CA  
4838  C C   . ILE A 659  ? 0.2772 0.3355 0.2612 0.0631  0.0022  -0.0659 657  ILE A C   
4839  O O   . ILE A 659  ? 0.2612 0.3113 0.2494 0.0627  -0.0008 -0.0687 657  ILE A O   
4840  C CB  . ILE A 659  ? 0.2459 0.3119 0.2198 0.0610  0.0058  -0.0580 657  ILE A CB  
4841  C CG1 . ILE A 659  ? 0.2653 0.3409 0.2345 0.0621  0.0067  -0.0584 657  ILE A CG1 
4842  C CG2 . ILE A 659  ? 0.2794 0.3327 0.2553 0.0581  0.0041  -0.0558 657  ILE A CG2 
4843  C CD1 . ILE A 659  ? 0.2968 0.3725 0.2615 0.0594  0.0090  -0.0505 657  ILE A CD1 
4844  N N   . ILE A 660  ? 0.2440 0.3029 0.2282 0.0625  0.0041  -0.0625 658  ILE A N   
4845  C CA  . ILE A 660  ? 0.2886 0.3387 0.2779 0.0615  0.0028  -0.0622 658  ILE A CA  
4846  C C   . ILE A 660  ? 0.2964 0.3457 0.2918 0.0644  -0.0005 -0.0702 658  ILE A C   
4847  O O   . ILE A 660  ? 0.2990 0.3387 0.2993 0.0632  -0.0033 -0.0712 658  ILE A O   
4848  C CB  . ILE A 660  ? 0.2558 0.3088 0.2443 0.0611  0.0054  -0.0581 658  ILE A CB  
4849  C CG1 . ILE A 660  ? 0.2550 0.3049 0.2394 0.0576  0.0078  -0.0497 658  ILE A CG1 
4850  C CG2 . ILE A 660  ? 0.2983 0.3450 0.2926 0.0612  0.0038  -0.0597 658  ILE A CG2 
4851  C CD1 . ILE A 660  ? 0.3028 0.3573 0.2860 0.0572  0.0106  -0.0455 658  ILE A CD1 
4852  N N   . ARG A 661  ? 0.2621 0.3219 0.2578 0.0681  -0.0004 -0.0761 659  ARG A N   
4853  C CA  . ARG A 661  ? 0.2792 0.3390 0.2815 0.0711  -0.0036 -0.0843 659  ARG A CA  
4854  C C   . ARG A 661  ? 0.3233 0.3811 0.3277 0.0722  -0.0068 -0.0898 659  ARG A C   
4855  O O   . ARG A 661  ? 0.3026 0.3545 0.3140 0.0731  -0.0104 -0.0946 659  ARG A O   
4856  C CB  . ARG A 661  ? 0.2927 0.3649 0.2948 0.0749  -0.0023 -0.0889 659  ARG A CB  
4857  C CG  . ARG A 661  ? 0.2819 0.3543 0.2847 0.0742  -0.0003 -0.0850 659  ARG A CG  
4858  C CD  . ARG A 661  ? 0.2966 0.3825 0.2985 0.0777  0.0016  -0.0886 659  ARG A CD  
4859  N NE  . ARG A 661  ? 0.3128 0.4028 0.3202 0.0818  -0.0013 -0.0984 659  ARG A NE  
4860  C CZ  . ARG A 661  ? 0.3093 0.4115 0.3152 0.0853  -0.0011 -0.1046 659  ARG A CZ  
4861  N NH1 . ARG A 661  ? 0.3442 0.4560 0.3431 0.0851  0.0016  -0.1018 659  ARG A NH1 
4862  N NH2 . ARG A 661  ? 0.3049 0.4103 0.3168 0.0891  -0.0040 -0.1139 659  ARG A NH2 
4863  N N   . GLU A 662  ? 0.2939 0.3566 0.2930 0.0720  -0.0058 -0.0891 660  GLU A N   
4864  C CA  . GLU A 662  ? 0.2827 0.3445 0.2839 0.0733  -0.0089 -0.0948 660  GLU A CA  
4865  C C   . GLU A 662  ? 0.2730 0.3222 0.2762 0.0698  -0.0108 -0.0913 660  GLU A C   
4866  O O   . GLU A 662  ? 0.3045 0.3486 0.3133 0.0704  -0.0145 -0.0961 660  GLU A O   
4867  C CB  . GLU A 662  ? 0.2941 0.3671 0.2892 0.0747  -0.0072 -0.0960 660  GLU A CB  
4868  C CG  . GLU A 662  ? 0.2936 0.3669 0.2910 0.0765  -0.0106 -0.1028 660  GLU A CG  
4869  C CD  . GLU A 662  ? 0.2954 0.3801 0.2866 0.0780  -0.0091 -0.1041 660  GLU A CD  
4870  O OE1 . GLU A 662  ? 0.3195 0.4084 0.3042 0.0763  -0.0058 -0.0974 660  GLU A OE1 
4871  O OE2 . GLU A 662  ? 0.3044 0.3941 0.2979 0.0809  -0.0116 -0.1120 660  GLU A OE2 
4872  N N   . ALA A 663  ? 0.2803 0.3245 0.2794 0.0662  -0.0085 -0.0830 661  ALA A N   
4873  C CA  . ALA A 663  ? 0.2700 0.3045 0.2696 0.0629  -0.0098 -0.0794 661  ALA A CA  
4874  C C   . ALA A 663  ? 0.2969 0.3210 0.2993 0.0598  -0.0101 -0.0742 661  ALA A C   
4875  O O   . ALA A 663  ? 0.3538 0.3704 0.3560 0.0568  -0.0107 -0.0702 661  ALA A O   
4876  C CB  . ALA A 663  ? 0.2955 0.3331 0.2880 0.0613  -0.0074 -0.0747 661  ALA A CB  
4877  N N   . GLY A 664  ? 0.3170 0.3411 0.3220 0.0605  -0.0096 -0.0741 662  GLY A N   
4878  C CA  . GLY A 664  ? 0.3301 0.3449 0.3379 0.0576  -0.0100 -0.0693 662  GLY A CA  
4879  C C   . GLY A 664  ? 0.3134 0.3257 0.3158 0.0543  -0.0070 -0.0612 662  GLY A C   
4880  O O   . GLY A 664  ? 0.3531 0.3572 0.3572 0.0513  -0.0076 -0.0570 662  GLY A O   
4881  N N   . LYS A 665  ? 0.2782 0.2979 0.2746 0.0546  -0.0038 -0.0589 663  LYS A N   
4882  C CA  . LYS A 665  ? 0.2792 0.2967 0.2710 0.0516  -0.0012 -0.0516 663  LYS A CA  
4883  C C   . LYS A 665  ? 0.2444 0.2628 0.2361 0.0511  0.0009  -0.0481 663  LYS A C   
4884  O O   . LYS A 665  ? 0.2497 0.2743 0.2422 0.0535  0.0016  -0.0508 663  LYS A O   
4885  C CB  . LYS A 665  ? 0.2737 0.2985 0.2597 0.0519  0.0010  -0.0501 663  LYS A CB  
4886  C CG  . LYS A 665  ? 0.2882 0.3131 0.2737 0.0525  -0.0008 -0.0533 663  LYS A CG  
4887  C CD  . LYS A 665  ? 0.3682 0.3832 0.3555 0.0496  -0.0025 -0.0510 663  LYS A CD  
4888  C CE  . LYS A 665  ? 0.3534 0.3693 0.3398 0.0500  -0.0040 -0.0537 663  LYS A CE  
4889  N NZ  . LYS A 665  ? 0.3760 0.3826 0.3654 0.0475  -0.0063 -0.0526 663  LYS A NZ  
4890  N N   . SER A 666  ? 0.2844 0.2967 0.2749 0.0479  0.0019  -0.0421 664  SER A N   
4891  C CA  . SER A 666  ? 0.2901 0.3037 0.2796 0.0471  0.0042  -0.0381 664  SER A CA  
4892  C C   . SER A 666  ? 0.2918 0.3138 0.2764 0.0476  0.0072  -0.0355 664  SER A C   
4893  O O   . SER A 666  ? 0.2850 0.3105 0.2665 0.0480  0.0076  -0.0358 664  SER A O   
4894  C CB  . SER A 666  ? 0.3061 0.3116 0.2958 0.0436  0.0044  -0.0327 664  SER A CB  
4895  O OG  . SER A 666  ? 0.3141 0.3194 0.2997 0.0419  0.0057  -0.0292 664  SER A OG  
4896  N N   . ALA A 667  ? 0.2816 0.3070 0.2656 0.0476  0.0093  -0.0327 665  ALA A N   
4897  C CA  . ALA A 667  ? 0.2624 0.2958 0.2424 0.0478  0.0120  -0.0294 665  ALA A CA  
4898  C C   . ALA A 667  ? 0.2813 0.3116 0.2581 0.0451  0.0129  -0.0244 665  ALA A C   
4899  O O   . ALA A 667  ? 0.2631 0.2993 0.2366 0.0456  0.0139  -0.0234 665  ALA A O   
4900  C CB  . ALA A 667  ? 0.3186 0.3551 0.2993 0.0477  0.0139  -0.0266 665  ALA A CB  
4901  N N   . LEU A 668  ? 0.2763 0.2978 0.2542 0.0424  0.0124  -0.0211 666  LEU A N   
4902  C CA  . LEU A 668  ? 0.2729 0.2913 0.2483 0.0400  0.0130  -0.0169 666  LEU A CA  
4903  C C   . LEU A 668  ? 0.3087 0.3277 0.2826 0.0406  0.0119  -0.0193 666  LEU A C   
4904  O O   . LEU A 668  ? 0.2935 0.3154 0.2643 0.0401  0.0129  -0.0169 666  LEU A O   
4905  C CB  . LEU A 668  ? 0.3238 0.3330 0.3010 0.0373  0.0123  -0.0143 666  LEU A CB  
4906  C CG  . LEU A 668  ? 0.4118 0.4197 0.3896 0.0357  0.0138  -0.0100 666  LEU A CG  
4907  C CD1 . LEU A 668  ? 0.3599 0.3593 0.3394 0.0332  0.0127  -0.0083 666  LEU A CD1 
4908  C CD2 . LEU A 668  ? 0.4320 0.4443 0.4073 0.0350  0.0158  -0.0057 666  LEU A CD2 
4909  N N   . ASN A 669  ? 0.2525 0.2683 0.2286 0.0416  0.0096  -0.0241 667  ASN A N   
4910  C CA  . ASN A 669  ? 0.2769 0.2929 0.2519 0.0420  0.0082  -0.0266 667  ASN A CA  
4911  C C   . ASN A 669  ? 0.2729 0.2986 0.2455 0.0447  0.0089  -0.0295 667  ASN A C   
4912  O O   . ASN A 669  ? 0.2784 0.3064 0.2485 0.0447  0.0088  -0.0294 667  ASN A O   
4913  C CB  . ASN A 669  ? 0.3068 0.3165 0.2857 0.0421  0.0053  -0.0306 667  ASN A CB  
4914  C CG  . ASN A 669  ? 0.3912 0.3919 0.3717 0.0390  0.0047  -0.0272 667  ASN A CG  
4915  O OD1 . ASN A 669  ? 0.4528 0.4517 0.4311 0.0369  0.0059  -0.0228 667  ASN A OD1 
4916  N ND2 . ASN A 669  ? 0.4295 0.4253 0.4144 0.0388  0.0026  -0.0292 667  ASN A ND2 
4917  N N   . ALA A 670  ? 0.2581 0.2903 0.2314 0.0470  0.0095  -0.0319 668  ALA A N   
4918  C CA  . ALA A 670  ? 0.2676 0.3106 0.2383 0.0496  0.0104  -0.0342 668  ALA A CA  
4919  C C   . ALA A 670  ? 0.2581 0.3065 0.2248 0.0485  0.0129  -0.0284 668  ALA A C   
4920  O O   . ALA A 670  ? 0.2470 0.3022 0.2108 0.0495  0.0133  -0.0287 668  ALA A O   
4921  C CB  . ALA A 670  ? 0.2468 0.2959 0.2196 0.0523  0.0105  -0.0383 668  ALA A CB  
4922  N N   . ILE A 671  ? 0.2405 0.2862 0.2074 0.0464  0.0145  -0.0229 669  ILE A N   
4923  C CA  . ILE A 671  ? 0.2404 0.2900 0.2045 0.0451  0.0165  -0.0169 669  ILE A CA  
4924  C C   . ILE A 671  ? 0.2544 0.3004 0.2167 0.0436  0.0158  -0.0153 669  ILE A C   
4925  O O   . ILE A 671  ? 0.2733 0.3257 0.2330 0.0439  0.0166  -0.0133 669  ILE A O   
4926  C CB  . ILE A 671  ? 0.2694 0.3151 0.2350 0.0429  0.0178  -0.0116 669  ILE A CB  
4927  C CG1 . ILE A 671  ? 0.2576 0.3087 0.2246 0.0444  0.0189  -0.0125 669  ILE A CG1 
4928  C CG2 . ILE A 671  ? 0.2888 0.3359 0.2526 0.0410  0.0192  -0.0053 669  ILE A CG2 
4929  C CD1 . ILE A 671  ? 0.2908 0.3366 0.2600 0.0423  0.0196  -0.0085 669  ILE A CD1 
4930  N N   . ALA A 672  ? 0.2265 0.2628 0.1906 0.0420  0.0143  -0.0159 670  ALA A N   
4931  C CA  . ALA A 672  ? 0.2435 0.2763 0.2062 0.0406  0.0135  -0.0147 670  ALA A CA  
4932  C C   . ALA A 672  ? 0.2487 0.2868 0.2097 0.0427  0.0125  -0.0189 670  ALA A C   
4933  O O   . ALA A 672  ? 0.2619 0.3024 0.2206 0.0423  0.0127  -0.0170 670  ALA A O   
4934  C CB  . ALA A 672  ? 0.2620 0.2843 0.2271 0.0387  0.0120  -0.0153 670  ALA A CB  
4935  N N   . GLU A 673  ? 0.2393 0.2797 0.2017 0.0450  0.0112  -0.0247 671  GLU A N   
4936  C CA  . GLU A 673  ? 0.2434 0.2890 0.2046 0.0472  0.0099  -0.0296 671  GLU A CA  
4937  C C   . GLU A 673  ? 0.2557 0.3127 0.2132 0.0486  0.0117  -0.0280 671  GLU A C   
4938  O O   . GLU A 673  ? 0.2429 0.3034 0.1980 0.0489  0.0113  -0.0281 671  GLU A O   
4939  C CB  . GLU A 673  ? 0.2500 0.2961 0.2142 0.0495  0.0082  -0.0363 671  GLU A CB  
4940  C CG  . GLU A 673  ? 0.3062 0.3583 0.2700 0.0522  0.0066  -0.0424 671  GLU A CG  
4941  C CD  . GLU A 673  ? 0.3377 0.3824 0.3032 0.0513  0.0041  -0.0447 671  GLU A CD  
4942  O OE1 . GLU A 673  ? 0.3616 0.3967 0.3293 0.0488  0.0035  -0.0422 671  GLU A OE1 
4943  O OE2 . GLU A 673  ? 0.3083 0.3574 0.2730 0.0530  0.0028  -0.0490 671  GLU A OE2 
4944  N N   . VAL A 674  ? 0.2182 0.2816 0.1753 0.0493  0.0135  -0.0261 672  VAL A N   
4945  C CA  . VAL A 674  ? 0.2264 0.3016 0.1802 0.0505  0.0152  -0.0239 672  VAL A CA  
4946  C C   . VAL A 674  ? 0.2381 0.3125 0.1900 0.0481  0.0163  -0.0168 672  VAL A C   
4947  O O   . VAL A 674  ? 0.2204 0.3019 0.1696 0.0486  0.0166  -0.0155 672  VAL A O   
4948  C CB  . VAL A 674  ? 0.2244 0.3069 0.1788 0.0518  0.0169  -0.0236 672  VAL A CB  
4949  C CG1 . VAL A 674  ? 0.2505 0.3461 0.2014 0.0528  0.0187  -0.0207 672  VAL A CG1 
4950  C CG2 . VAL A 674  ? 0.2524 0.3361 0.2091 0.0546  0.0155  -0.0313 672  VAL A CG2 
4951  N N   . ARG A 675  ? 0.2253 0.2912 0.1790 0.0454  0.0168  -0.0123 673  ARG A N   
4952  C CA  . ARG A 675  ? 0.2221 0.2862 0.1749 0.0432  0.0174  -0.0061 673  ARG A CA  
4953  C C   . ARG A 675  ? 0.2205 0.2827 0.1719 0.0430  0.0160  -0.0076 673  ARG A C   
4954  O O   . ARG A 675  ? 0.2294 0.2962 0.1788 0.0427  0.0165  -0.0041 673  ARG A O   
4955  C CB  . ARG A 675  ? 0.2280 0.2823 0.1833 0.0406  0.0177  -0.0025 673  ARG A CB  
4956  C CG  . ARG A 675  ? 0.2338 0.2907 0.1906 0.0402  0.0193  0.0006  673  ARG A CG  
4957  C CD  . ARG A 675  ? 0.2461 0.2940 0.2052 0.0375  0.0194  0.0047  673  ARG A CD  
4958  N NE  . ARG A 675  ? 0.2409 0.2889 0.1997 0.0359  0.0197  0.0099  673  ARG A NE  
4959  C CZ  . ARG A 675  ? 0.2540 0.2943 0.2148 0.0336  0.0194  0.0128  673  ARG A CZ  
4960  N NH1 . ARG A 675  ? 0.2572 0.2895 0.2199 0.0326  0.0189  0.0114  673  ARG A NH1 
4961  N NH2 . ARG A 675  ? 0.2423 0.2834 0.2033 0.0324  0.0195  0.0173  673  ARG A NH2 
4962  N N   . GLU A 676  ? 0.2097 0.2650 0.1623 0.0432  0.0142  -0.0124 674  GLU A N   
4963  C CA  . GLU A 676  ? 0.2249 0.2780 0.1765 0.0430  0.0127  -0.0139 674  GLU A CA  
4964  C C   . GLU A 676  ? 0.2279 0.2915 0.1766 0.0452  0.0125  -0.0162 674  GLU A C   
4965  O O   . GLU A 676  ? 0.2265 0.2921 0.1734 0.0448  0.0123  -0.0142 674  GLU A O   
4966  C CB  . GLU A 676  ? 0.2424 0.2872 0.1963 0.0428  0.0106  -0.0189 674  GLU A CB  
4967  N N   . ALA A 677  ? 0.2185 0.2893 0.1669 0.0478  0.0126  -0.0205 675  ALA A N   
4968  C CA  . ALA A 677  ? 0.2077 0.2897 0.1532 0.0501  0.0125  -0.0230 675  ALA A CA  
4969  C C   . ALA A 677  ? 0.2371 0.3272 0.1799 0.0495  0.0143  -0.0164 675  ALA A C   
4970  O O   . ALA A 677  ? 0.2211 0.3166 0.1614 0.0499  0.0140  -0.0156 675  ALA A O   
4971  C CB  . ALA A 677  ? 0.2260 0.3146 0.1721 0.0531  0.0124  -0.0289 675  ALA A CB  
4972  N N   . ILE A 678  ? 0.2245 0.3159 0.1680 0.0485  0.0162  -0.0115 676  ILE A N   
4973  C CA  . ILE A 678  ? 0.2291 0.3275 0.1712 0.0474  0.0178  -0.0043 676  ILE A CA  
4974  C C   . ILE A 678  ? 0.2307 0.3233 0.1728 0.0452  0.0172  0.0000  676  ILE A C   
4975  O O   . ILE A 678  ? 0.2304 0.3298 0.1705 0.0452  0.0173  0.0035  676  ILE A O   
4976  C CB  . ILE A 678  ? 0.2296 0.3275 0.1736 0.0463  0.0195  0.0002  676  ILE A CB  
4977  C CG1 . ILE A 678  ? 0.2309 0.3368 0.1746 0.0487  0.0203  -0.0038 676  ILE A CG1 
4978  C CG2 . ILE A 678  ? 0.2405 0.3430 0.1843 0.0446  0.0208  0.0085  676  ILE A CG2 
4979  C CD1 . ILE A 678  ? 0.2419 0.3456 0.1882 0.0477  0.0217  -0.0008 676  ILE A CD1 
4980  N N   . ASP A 679  ? 0.2118 0.2921 0.1563 0.0434  0.0163  -0.0001 677  ASP A N   
4981  C CA  . ASP A 679  ? 0.2014 0.2759 0.1464 0.0413  0.0157  0.0037  677  ASP A CA  
4982  C C   . ASP A 679  ? 0.2252 0.3016 0.1681 0.0423  0.0142  0.0005  677  ASP A C   
4983  O O   . ASP A 679  ? 0.2168 0.2952 0.1591 0.0415  0.0141  0.0045  677  ASP A O   
4984  C CB  . ASP A 679  ? 0.2154 0.2772 0.1633 0.0394  0.0152  0.0035  677  ASP A CB  
4985  C CG  . ASP A 679  ? 0.2493 0.3086 0.1995 0.0380  0.0165  0.0074  677  ASP A CG  
4986  O OD1 . ASP A 679  ? 0.2690 0.3346 0.2192 0.0377  0.0178  0.0124  677  ASP A OD1 
4987  O OD2 . ASP A 679  ? 0.2874 0.3386 0.2397 0.0371  0.0162  0.0058  677  ASP A OD2 
4988  N N   . PHE A 680  ? 0.2154 0.2915 0.1579 0.0441  0.0129  -0.0064 678  PHE A N   
4989  C CA  . PHE A 680  ? 0.2190 0.2981 0.1597 0.0452  0.0114  -0.0098 678  PHE A CA  
4990  C C   . PHE A 680  ? 0.2197 0.3116 0.1572 0.0465  0.0122  -0.0074 678  PHE A C   
4991  O O   . PHE A 680  ? 0.2250 0.3191 0.1612 0.0461  0.0116  -0.0052 678  PHE A O   
4992  C CB  . PHE A 680  ? 0.2283 0.3067 0.1694 0.0472  0.0098  -0.0179 678  PHE A CB  
4993  C CG  . PHE A 680  ? 0.2238 0.2904 0.1678 0.0459  0.0082  -0.0207 678  PHE A CG  
4994  C CD1 . PHE A 680  ? 0.2325 0.2928 0.1769 0.0441  0.0074  -0.0187 678  PHE A CD1 
4995  C CD2 . PHE A 680  ? 0.2317 0.2940 0.1782 0.0466  0.0075  -0.0252 678  PHE A CD2 
4996  C CE1 . PHE A 680  ? 0.2357 0.2861 0.1828 0.0429  0.0059  -0.0211 678  PHE A CE1 
4997  C CE2 . PHE A 680  ? 0.2250 0.2772 0.1743 0.0454  0.0059  -0.0274 678  PHE A CE2 
4998  C CZ  . PHE A 680  ? 0.2389 0.2853 0.1885 0.0434  0.0052  -0.0252 678  PHE A CZ  
4999  N N   . LEU A 681  ? 0.2075 0.3085 0.1438 0.0482  0.0134  -0.0079 679  LEU A N   
5000  C CA  . LEU A 681  ? 0.2014 0.3161 0.1347 0.0495  0.0142  -0.0055 679  LEU A CA  
5001  C C   . LEU A 681  ? 0.2358 0.3512 0.1691 0.0472  0.0150  0.0032  679  LEU A C   
5002  O O   . LEU A 681  ? 0.2221 0.3435 0.1535 0.0474  0.0144  0.0052  679  LEU A O   
5003  C CB  . LEU A 681  ? 0.2382 0.3623 0.1708 0.0512  0.0157  -0.0067 679  LEU A CB  
5004  C CG  . LEU A 681  ? 0.2445 0.3708 0.1770 0.0541  0.0147  -0.0158 679  LEU A CG  
5005  C CD1 . LEU A 681  ? 0.2436 0.3749 0.1769 0.0553  0.0162  -0.0169 679  LEU A CD1 
5006  C CD2 . LEU A 681  ? 0.2518 0.3888 0.1812 0.0566  0.0137  -0.0201 679  LEU A CD2 
5007  N N   . ARG A 682  ? 0.2103 0.3196 0.1464 0.0451  0.0160  0.0083  680  ARG A N   
5008  C CA  . ARG A 682  ? 0.2310 0.3412 0.1682 0.0430  0.0165  0.0166  680  ARG A CA  
5009  C C   . ARG A 682  ? 0.2298 0.3318 0.1680 0.0415  0.0150  0.0176  680  ARG A C   
5010  O O   . ARG A 682  ? 0.2280 0.3335 0.1662 0.0407  0.0148  0.0229  680  ARG A O   
5011  C CB  . ARG A 682  ? 0.2241 0.3303 0.1644 0.0413  0.0178  0.0214  680  ARG A CB  
5012  C CG  . ARG A 682  ? 0.2273 0.3433 0.1666 0.0425  0.0195  0.0219  680  ARG A CG  
5013  C CD  . ARG A 682  ? 0.2381 0.3492 0.1809 0.0407  0.0206  0.0262  680  ARG A CD  
5014  N NE  . ARG A 682  ? 0.2428 0.3644 0.1850 0.0418  0.0222  0.0277  680  ARG A NE  
5015  C CZ  . ARG A 682  ? 0.2479 0.3670 0.1926 0.0410  0.0233  0.0295  680  ARG A CZ  
5016  N NH1 . ARG A 682  ? 0.2705 0.3774 0.2184 0.0391  0.0229  0.0300  680  ARG A NH1 
5017  N NH2 . ARG A 682  ? 0.2850 0.4149 0.2291 0.0420  0.0248  0.0307  680  ARG A NH2 
5018  N N   . TYR A 683  ? 0.2198 0.3113 0.1592 0.0412  0.0140  0.0128  681  TYR A N   
5019  C CA  . TYR A 683  ? 0.1997 0.2836 0.1402 0.0398  0.0126  0.0134  681  TYR A CA  
5020  C C   . TYR A 683  ? 0.2465 0.3366 0.1842 0.0412  0.0114  0.0112  681  TYR A C   
5021  O O   . TYR A 683  ? 0.2337 0.3243 0.1716 0.0403  0.0108  0.0152  681  TYR A O   
5022  C CB  . TYR A 683  ? 0.2230 0.2953 0.1654 0.0391  0.0119  0.0089  681  TYR A CB  
5023  C CG  . TYR A 683  ? 0.2236 0.2887 0.1671 0.0379  0.0105  0.0089  681  TYR A CG  
5024  C CD1 . TYR A 683  ? 0.2162 0.2761 0.1623 0.0358  0.0106  0.0141  681  TYR A CD1 
5025  C CD2 . TYR A 683  ? 0.2196 0.2834 0.1619 0.0388  0.0090  0.0035  681  TYR A CD2 
5026  C CE1 . TYR A 683  ? 0.2276 0.2815 0.1749 0.0347  0.0094  0.0139  681  TYR A CE1 
5027  C CE2 . TYR A 683  ? 0.2203 0.2782 0.1637 0.0376  0.0078  0.0036  681  TYR A CE2 
5028  C CZ  . TYR A 683  ? 0.2228 0.2759 0.1685 0.0356  0.0081  0.0088  681  TYR A CZ  
5029  O OH  . TYR A 683  ? 0.2404 0.2881 0.1874 0.0346  0.0069  0.0086  681  TYR A OH  
5030  N N   . TYR A 684  ? 0.2135 0.3084 0.1488 0.0435  0.0109  0.0048  682  TYR A N   
5031  C CA  . TYR A 684  ? 0.2082 0.3095 0.1410 0.0449  0.0096  0.0024  682  TYR A CA  
5032  C C   . TYR A 684  ? 0.2426 0.3564 0.1731 0.0453  0.0104  0.0077  682  TYR A C   
5033  O O   . TYR A 684  ? 0.2304 0.3479 0.1596 0.0454  0.0094  0.0092  682  TYR A O   
5034  C CB  . TYR A 684  ? 0.2185 0.3223 0.1499 0.0473  0.0086  -0.0061 682  TYR A CB  
5035  C CG  . TYR A 684  ? 0.2111 0.3029 0.1452 0.0467  0.0073  -0.0110 682  TYR A CG  
5036  C CD1 . TYR A 684  ? 0.2212 0.3033 0.1571 0.0446  0.0064  -0.0094 682  TYR A CD1 
5037  C CD2 . TYR A 684  ? 0.2286 0.3188 0.1636 0.0480  0.0070  -0.0169 682  TYR A CD2 
5038  C CE1 . TYR A 684  ? 0.2452 0.3171 0.1835 0.0439  0.0053  -0.0134 682  TYR A CE1 
5039  C CE2 . TYR A 684  ? 0.2197 0.2993 0.1575 0.0473  0.0057  -0.0208 682  TYR A CE2 
5040  C CZ  . TYR A 684  ? 0.2204 0.2910 0.1599 0.0451  0.0049  -0.0188 682  TYR A CZ  
5041  O OH  . TYR A 684  ? 0.2364 0.2973 0.1787 0.0442  0.0037  -0.0221 682  TYR A OH  
5042  N N   . ALA A 685  ? 0.2122 0.3328 0.1424 0.0456  0.0121  0.0110  683  ALA A N   
5043  C CA  . ALA A 685  ? 0.2244 0.3567 0.1531 0.0455  0.0129  0.0174  683  ALA A CA  
5044  C C   . ALA A 685  ? 0.2373 0.3648 0.1685 0.0431  0.0124  0.0249  683  ALA A C   
5045  O O   . ALA A 685  ? 0.2357 0.3698 0.1658 0.0431  0.0117  0.0283  683  ALA A O   
5046  C CB  . ALA A 685  ? 0.2389 0.3784 0.1676 0.0459  0.0148  0.0202  683  ALA A CB  
5047  N N   . GLU A 686  ? 0.2283 0.3447 0.1633 0.0410  0.0127  0.0273  684  GLU A N   
5048  C CA  . GLU A 686  ? 0.2425 0.3541 0.1808 0.0388  0.0121  0.0340  684  GLU A CA  
5049  C C   . GLU A 686  ? 0.2242 0.3312 0.1622 0.0387  0.0103  0.0318  684  GLU A C   
5050  O O   . GLU A 686  ? 0.2381 0.3479 0.1770 0.0380  0.0095  0.0367  684  GLU A O   
5051  C CB  . GLU A 686  ? 0.2841 0.3853 0.2267 0.0369  0.0127  0.0363  684  GLU A CB  
5052  C CG  . GLU A 686  ? 0.3190 0.4141 0.2657 0.0347  0.0117  0.0420  684  GLU A CG  
5053  C CD  . GLU A 686  ? 0.3743 0.4782 0.3222 0.0340  0.0117  0.0502  684  GLU A CD  
5054  O OE1 . GLU A 686  ? 0.3554 0.4702 0.3014 0.0348  0.0128  0.0527  684  GLU A OE1 
5055  O OE2 . GLU A 686  ? 0.4037 0.5038 0.3550 0.0327  0.0105  0.0545  684  GLU A OE2 
5056  N N   . GLN A 687  ? 0.2073 0.3074 0.1445 0.0394  0.0096  0.0246  685  GLN A N   
5057  C CA  . GLN A 687  ? 0.2241 0.3202 0.1613 0.0393  0.0079  0.0223  685  GLN A CA  
5058  C C   . GLN A 687  ? 0.2368 0.3440 0.1706 0.0408  0.0071  0.0223  685  GLN A C   
5059  O O   . GLN A 687  ? 0.2493 0.3563 0.1835 0.0403  0.0059  0.0243  685  GLN A O   
5060  C CB  . GLN A 687  ? 0.2248 0.3129 0.1617 0.0398  0.0072  0.0146  685  GLN A CB  
5061  C CG  . GLN A 687  ? 0.2319 0.3084 0.1723 0.0381  0.0076  0.0149  685  GLN A CG  
5062  C CD  . GLN A 687  ? 0.2786 0.3489 0.2222 0.0360  0.0072  0.0196  685  GLN A CD  
5063  O OE1 . GLN A 687  ? 0.2630 0.3316 0.2067 0.0359  0.0059  0.0189  685  GLN A OE1 
5064  N NE2 . GLN A 687  ? 0.3159 0.3829 0.2624 0.0346  0.0081  0.0243  685  GLN A NE2 
5065  N N   . THR A 688  ? 0.2164 0.3340 0.1470 0.0428  0.0078  0.0200  686  THR A N   
5066  C CA  . THR A 688  ? 0.2072 0.3370 0.1343 0.0443  0.0072  0.0201  686  THR A CA  
5067  C C   . THR A 688  ? 0.2422 0.3779 0.1702 0.0430  0.0073  0.0293  686  THR A C   
5068  O O   . THR A 688  ? 0.2468 0.3861 0.1741 0.0430  0.0061  0.0312  686  THR A O   
5069  C CB  . THR A 688  ? 0.2301 0.3707 0.1539 0.0467  0.0081  0.0160  686  THR A CB  
5070  O OG1 . THR A 688  ? 0.2386 0.3742 0.1619 0.0482  0.0072  0.0070  686  THR A OG1 
5071  C CG2 . THR A 688  ? 0.2386 0.3939 0.1587 0.0482  0.0077  0.0173  686  THR A CG2 
5072  N N   . ARG A 689  ? 0.2430 0.3797 0.1731 0.0418  0.0088  0.0352  687  ARG A N   
5073  C CA  . ARG A 689  ? 0.2559 0.3983 0.1880 0.0404  0.0087  0.0444  687  ARG A CA  
5074  C C   . ARG A 689  ? 0.2476 0.3806 0.1835 0.0386  0.0073  0.0477  687  ARG A C   
5075  O O   . ARG A 689  ? 0.2784 0.4162 0.2156 0.0378  0.0064  0.0542  687  ARG A O   
5076  C CB  . ARG A 689  ? 0.2358 0.3796 0.1702 0.0392  0.0104  0.0499  687  ARG A CB  
5077  C CG  . ARG A 689  ? 0.2666 0.4227 0.1974 0.0410  0.0119  0.0483  687  ARG A CG  
5078  C CD  . ARG A 689  ? 0.3034 0.4619 0.2371 0.0396  0.0134  0.0550  687  ARG A CD  
5079  N NE  . ARG A 689  ? 0.3179 0.4638 0.2548 0.0386  0.0140  0.0529  687  ARG A NE  
5080  C CZ  . ARG A 689  ? 0.3321 0.4776 0.2679 0.0396  0.0153  0.0482  687  ARG A CZ  
5081  N NH1 . ARG A 689  ? 0.3167 0.4735 0.2485 0.0418  0.0162  0.0447  687  ARG A NH1 
5082  N NH2 . ARG A 689  ? 0.3285 0.4623 0.2675 0.0385  0.0156  0.0469  687  ARG A NH2 
5083  N N   . ARG A 690  ? 0.2312 0.3511 0.1691 0.0379  0.0068  0.0434  688  ARG A N   
5084  C CA  . ARG A 690  ? 0.2569 0.3681 0.1984 0.0364  0.0054  0.0456  688  ARG A CA  
5085  C C   . ARG A 690  ? 0.2514 0.3640 0.1907 0.0374  0.0038  0.0422  688  ARG A C   
5086  O O   . ARG A 690  ? 0.2626 0.3715 0.2048 0.0363  0.0025  0.0453  688  ARG A O   
5087  C CB  . ARG A 690  ? 0.2581 0.3558 0.2026 0.0353  0.0056  0.0423  688  ARG A CB  
5088  C CG  . ARG A 690  ? 0.2733 0.3679 0.2210 0.0341  0.0069  0.0460  688  ARG A CG  
5089  C CD  . ARG A 690  ? 0.3036 0.3970 0.2564 0.0323  0.0062  0.0541  688  ARG A CD  
5090  N NE  . ARG A 690  ? 0.2944 0.3787 0.2506 0.0313  0.0048  0.0535  688  ARG A NE  
5091  C CZ  . ARG A 690  ? 0.3408 0.4270 0.2983 0.0311  0.0032  0.0567  688  ARG A CZ  
5092  N NH1 . ARG A 690  ? 0.3122 0.4092 0.2681 0.0316  0.0029  0.0611  688  ARG A NH1 
5093  N NH2 . ARG A 690  ? 0.3021 0.3798 0.2629 0.0304  0.0020  0.0555  688  ARG A NH2 
5094  N N   . THR A 691  ? 0.2341 0.3520 0.1690 0.0394  0.0036  0.0358  689  THR A N   
5095  C CA  . THR A 691  ? 0.2461 0.3623 0.1796 0.0401  0.0020  0.0313  689  THR A CA  
5096  C C   . THR A 691  ? 0.2684 0.3968 0.1974 0.0421  0.0012  0.0291  689  THR A C   
5097  O O   . THR A 691  ? 0.3068 0.4372 0.2356 0.0421  -0.0003 0.0301  689  THR A O   
5098  C CB  . THR A 691  ? 0.2445 0.3509 0.1781 0.0403  0.0017  0.0234  689  THR A CB  
5099  O OG1 . THR A 691  ? 0.2514 0.3615 0.1826 0.0418  0.0027  0.0187  689  THR A OG1 
5100  C CG2 . THR A 691  ? 0.2640 0.3579 0.2020 0.0383  0.0020  0.0250  689  THR A CG2 
5101  N N   . LEU A 692  ? 0.2383 0.3753 0.1639 0.0439  0.0022  0.0259  690  LEU A N   
5102  C CA  . LEU A 692  ? 0.2699 0.4167 0.1913 0.0461  0.0012  0.0209  690  LEU A CA  
5103  C C   . LEU A 692  ? 0.2817 0.4418 0.2010 0.0465  0.0009  0.0269  690  LEU A C   
5104  O O   . LEU A 692  ? 0.2953 0.4628 0.2146 0.0460  0.0021  0.0332  690  LEU A O   
5105  C CB  . LEU A 692  ? 0.2662 0.4175 0.1850 0.0482  0.0020  0.0141  690  LEU A CB  
5106  C CG  . LEU A 692  ? 0.2819 0.4209 0.2026 0.0482  0.0018  0.0072  690  LEU A CG  
5107  C CD1 . LEU A 692  ? 0.3227 0.4674 0.2411 0.0506  0.0020  -0.0002 690  LEU A CD1 
5108  C CD2 . LEU A 692  ? 0.3050 0.4358 0.2270 0.0477  -0.0002 0.0036  690  LEU A CD2 
5109  N N   . GLY A 693  ? 0.2871 0.4503 0.2049 0.0472  -0.0009 0.0250  691  GLY A N   
5110  C CA  . GLY A 693  ? 0.3273 0.5034 0.2429 0.0476  -0.0016 0.0300  691  GLY A CA  
5111  C C   . GLY A 693  ? 0.3140 0.4989 0.2253 0.0501  -0.0028 0.0231  691  GLY A C   
5112  O O   . GLY A 693  ? 0.3261 0.5071 0.2364 0.0515  -0.0033 0.0143  691  GLY A O   
5113  N N   . PRO A 694  ? 0.3347 0.5317 0.2436 0.0506  -0.0037 0.0270  692  PRO A N   
5114  C CA  . PRO A 694  ? 0.3313 0.5391 0.2358 0.0532  -0.0049 0.0205  692  PRO A CA  
5115  C C   . PRO A 694  ? 0.3659 0.5648 0.2710 0.0538  -0.0069 0.0126  692  PRO A C   
5116  O O   . PRO A 694  ? 0.4134 0.6174 0.3158 0.0561  -0.0077 0.0043  692  PRO A O   
5117  C CB  . PRO A 694  ? 0.4013 0.6216 0.3041 0.0529  -0.0056 0.0281  692  PRO A CB  
5118  C CG  . PRO A 694  ? 0.3616 0.5817 0.2674 0.0507  -0.0042 0.0383  692  PRO A CG  
5119  C CD  . PRO A 694  ? 0.3454 0.5482 0.2559 0.0490  -0.0035 0.0378  692  PRO A CD  
5120  N N   . GLY A 695  ? 0.3287 0.5148 0.2377 0.0518  -0.0077 0.0148  693  GLY A N   
5121  C CA  . GLY A 695  ? 0.3759 0.5538 0.2859 0.0521  -0.0096 0.0081  693  GLY A CA  
5122  C C   . GLY A 695  ? 0.3612 0.5281 0.2729 0.0523  -0.0093 0.0007  693  GLY A C   
5123  O O   . GLY A 695  ? 0.3595 0.5202 0.2723 0.0526  -0.0110 -0.0052 693  GLY A O   
5124  N N   . HIS A 696  ? 0.3411 0.5055 0.2534 0.0521  -0.0074 0.0010  694  HIS A N   
5125  C CA  . HIS A 696  ? 0.3112 0.4655 0.2254 0.0522  -0.0073 -0.0057 694  HIS A CA  
5126  C C   . HIS A 696  ? 0.3358 0.4994 0.2470 0.0550  -0.0073 -0.0127 694  HIS A C   
5127  O O   . HIS A 696  ? 0.3850 0.5521 0.2954 0.0555  -0.0056 -0.0125 694  HIS A O   
5128  C CB  . HIS A 696  ? 0.3321 0.4770 0.2493 0.0502  -0.0054 -0.0013 694  HIS A CB  
5129  C CG  . HIS A 696  ? 0.2817 0.4206 0.2018 0.0478  -0.0053 0.0064  694  HIS A CG  
5130  N ND1 . HIS A 696  ? 0.3021 0.4445 0.2229 0.0467  -0.0040 0.0147  694  HIS A ND1 
5131  C CD2 . HIS A 696  ? 0.3125 0.4428 0.2353 0.0464  -0.0066 0.0070  694  HIS A CD2 
5132  C CE1 . HIS A 696  ? 0.2901 0.4257 0.2143 0.0448  -0.0046 0.0198  694  HIS A CE1 
5133  N NE2 . HIS A 696  ? 0.3218 0.4503 0.2471 0.0446  -0.0061 0.0151  694  HIS A NE2 
5134  N N   . GLY A 697  ? 0.3400 0.5081 0.2497 0.0568  -0.0093 -0.0192 695  GLY A N   
5135  C CA  . GLY A 697  ? 0.3163 0.4947 0.2234 0.0597  -0.0097 -0.0264 695  GLY A CA  
5136  C C   . GLY A 697  ? 0.2783 0.4482 0.1879 0.0603  -0.0098 -0.0335 695  GLY A C   
5137  O O   . GLY A 697  ? 0.2965 0.4532 0.2097 0.0588  -0.0106 -0.0353 695  GLY A O   
5138  N N   . PRO A 698  ? 0.3101 0.4879 0.2181 0.0625  -0.0091 -0.0376 696  PRO A N   
5139  C CA  . PRO A 698  ? 0.3139 0.4843 0.2248 0.0633  -0.0094 -0.0446 696  PRO A CA  
5140  C C   . PRO A 698  ? 0.2778 0.4440 0.1909 0.0644  -0.0124 -0.0533 696  PRO A C   
5141  O O   . PRO A 698  ? 0.3026 0.4756 0.2139 0.0656  -0.0142 -0.0558 696  PRO A O   
5142  C CB  . PRO A 698  ? 0.3379 0.5209 0.2462 0.0658  -0.0082 -0.0473 696  PRO A CB  
5143  C CG  . PRO A 698  ? 0.4243 0.6228 0.3281 0.0672  -0.0083 -0.0453 696  PRO A CG  
5144  C CD  . PRO A 698  ? 0.4036 0.5984 0.3073 0.0644  -0.0080 -0.0363 696  PRO A CD  
5145  N N   . LEU A 699  ? 0.2803 0.4349 0.1976 0.0639  -0.0132 -0.0577 697  LEU A N   
5146  C CA  . LEU A 699  ? 0.2899 0.4406 0.2101 0.0651  -0.0162 -0.0664 697  LEU A CA  
5147  C C   . LEU A 699  ? 0.2904 0.4534 0.2092 0.0688  -0.0175 -0.0747 697  LEU A C   
5148  O O   . LEU A 699  ? 0.3152 0.4817 0.2344 0.0703  -0.0202 -0.0807 697  LEU A O   
5149  C CB  . LEU A 699  ? 0.2582 0.3947 0.1836 0.0638  -0.0167 -0.0687 697  LEU A CB  
5150  C CG  . LEU A 699  ? 0.3031 0.4266 0.2307 0.0602  -0.0158 -0.0621 697  LEU A CG  
5151  C CD1 . LEU A 699  ? 0.2812 0.3930 0.2136 0.0593  -0.0163 -0.0651 697  LEU A CD1 
5152  C CD2 . LEU A 699  ? 0.3215 0.4423 0.2496 0.0591  -0.0176 -0.0613 697  LEU A CD2 
5153  N N   . GLY A 700  ? 0.2782 0.4481 0.1955 0.0704  -0.0158 -0.0755 698  GLY A N   
5154  C CA  . GLY A 700  ? 0.2703 0.4507 0.1873 0.0741  -0.0171 -0.0844 698  GLY A CA  
5155  C C   . GLY A 700  ? 0.2644 0.4392 0.1849 0.0747  -0.0166 -0.0880 698  GLY A C   
5156  O O   . GLY A 700  ? 0.2940 0.4602 0.2156 0.0724  -0.0146 -0.0822 698  GLY A O   
5157  N N   . PRO A 701  ? 0.2761 0.4557 0.1987 0.0779  -0.0186 -0.0978 699  PRO A N   
5158  C CA  . PRO A 701  ? 0.2923 0.4670 0.2186 0.0787  -0.0184 -0.1016 699  PRO A CA  
5159  C C   . PRO A 701  ? 0.2727 0.4294 0.2043 0.0757  -0.0190 -0.0994 699  PRO A C   
5160  O O   . PRO A 701  ? 0.2724 0.4206 0.2074 0.0746  -0.0215 -0.1016 699  PRO A O   
5161  C CB  . PRO A 701  ? 0.3001 0.4814 0.2296 0.0823  -0.0214 -0.1129 699  PRO A CB  
5162  C CG  . PRO A 701  ? 0.2941 0.4885 0.2211 0.0832  -0.0217 -0.1120 699  PRO A CG  
5163  C CD  . PRO A 701  ? 0.2608 0.4513 0.1831 0.0808  -0.0211 -0.1055 699  PRO A CD  
5164  N N   . ILE A 702  ? 0.2616 0.4128 0.1938 0.0742  -0.0166 -0.0947 700  ILE A N   
5165  C CA  A ILE A 702  ? 0.2571 0.3923 0.1940 0.0714  -0.0169 -0.0922 700  ILE A CA  
5166  C CA  B ILE A 702  ? 0.2572 0.3924 0.1940 0.0714  -0.0168 -0.0920 700  ILE A CA  
5167  C C   . ILE A 702  ? 0.2460 0.3780 0.1873 0.0729  -0.0176 -0.0977 700  ILE A C   
5168  O O   . ILE A 702  ? 0.2598 0.3996 0.1993 0.0746  -0.0158 -0.0982 700  ILE A O   
5169  C CB  A ILE A 702  ? 0.2537 0.3836 0.1881 0.0681  -0.0138 -0.0815 700  ILE A CB  
5170  C CB  B ILE A 702  ? 0.2512 0.3818 0.1855 0.0682  -0.0136 -0.0814 700  ILE A CB  
5171  C CG1 A ILE A 702  ? 0.2501 0.3797 0.1822 0.0663  -0.0141 -0.0769 700  ILE A CG1 
5172  C CG1 B ILE A 702  ? 0.2686 0.4023 0.1990 0.0668  -0.0131 -0.0758 700  ILE A CG1 
5173  C CG2 A ILE A 702  ? 0.2700 0.3852 0.2090 0.0656  -0.0137 -0.0795 700  ILE A CG2 
5174  C CG2 B ILE A 702  ? 0.2703 0.3852 0.2092 0.0653  -0.0138 -0.0790 700  ILE A CG2 
5175  C CD1 A ILE A 702  ? 0.2421 0.3662 0.1725 0.0631  -0.0115 -0.0670 700  ILE A CD1 
5176  C CD1 B ILE A 702  ? 0.2648 0.3902 0.1979 0.0654  -0.0156 -0.0774 700  ILE A CD1 
5177  N N   . VAL A 703  ? 0.2602 0.3810 0.2075 0.0722  -0.0203 -0.1018 701  VAL A N   
5178  C CA  . VAL A 703  ? 0.2531 0.3689 0.2059 0.0732  -0.0214 -0.1067 701  VAL A CA  
5179  C C   . VAL A 703  ? 0.2441 0.3485 0.1980 0.0699  -0.0194 -0.0992 701  VAL A C   
5180  O O   . VAL A 703  ? 0.2496 0.3441 0.2047 0.0668  -0.0197 -0.0949 701  VAL A O   
5181  C CB  . VAL A 703  ? 0.2642 0.3741 0.2236 0.0741  -0.0258 -0.1147 701  VAL A CB  
5182  C CG1 . VAL A 703  ? 0.2706 0.3730 0.2366 0.0744  -0.0272 -0.1184 701  VAL A CG1 
5183  C CG2 . VAL A 703  ? 0.2870 0.4095 0.2454 0.0778  -0.0278 -0.1230 701  VAL A CG2 
5184  N N   . CYS A 704  ? 0.2200 0.3266 0.1732 0.0704  -0.0172 -0.0977 702  CYS A N   
5185  C CA  . CYS A 704  ? 0.2447 0.3415 0.1991 0.0675  -0.0153 -0.0911 702  CYS A CA  
5186  C C   . CYS A 704  ? 0.2509 0.3415 0.2115 0.0684  -0.0171 -0.0962 702  CYS A C   
5187  O O   . CYS A 704  ? 0.2444 0.3420 0.2056 0.0712  -0.0170 -0.1009 702  CYS A O   
5188  C CB  . CYS A 704  ? 0.2577 0.3612 0.2069 0.0672  -0.0115 -0.0846 702  CYS A CB  
5189  S SG  . CYS A 704  ? 0.2569 0.3676 0.1995 0.0661  -0.0095 -0.0778 702  CYS A SG  
5190  N N   . ILE A 705  ? 0.2515 0.3295 0.2169 0.0660  -0.0188 -0.0952 703  ILE A N   
5191  C CA  . ILE A 705  ? 0.2603 0.3309 0.2325 0.0663  -0.0210 -0.0992 703  ILE A CA  
5192  C C   . ILE A 705  ? 0.2476 0.3090 0.2203 0.0631  -0.0189 -0.0919 703  ILE A C   
5193  O O   . ILE A 705  ? 0.2424 0.2973 0.2138 0.0599  -0.0181 -0.0858 703  ILE A O   
5194  C CB  . ILE A 705  ? 0.2582 0.3223 0.2364 0.0660  -0.0251 -0.1043 703  ILE A CB  
5195  C CG1 . ILE A 705  ? 0.2611 0.3349 0.2395 0.0696  -0.0274 -0.1126 703  ILE A CG1 
5196  C CG2 . ILE A 705  ? 0.2737 0.3287 0.2597 0.0656  -0.0274 -0.1067 703  ILE A CG2 
5197  C CD1 . ILE A 705  ? 0.2858 0.3540 0.2695 0.0691  -0.0314 -0.1167 703  ILE A CD1 
5198  N N   . SER A 706  ? 0.2558 0.3172 0.2302 0.0639  -0.0181 -0.0925 704  SER A N   
5199  C CA  . SER A 706  ? 0.2380 0.2929 0.2117 0.0613  -0.0157 -0.0854 704  SER A CA  
5200  C C   . SER A 706  ? 0.2380 0.2846 0.2184 0.0609  -0.0176 -0.0876 704  SER A C   
5201  O O   . SER A 706  ? 0.2623 0.3104 0.2474 0.0635  -0.0202 -0.0948 704  SER A O   
5202  C CB  . SER A 706  ? 0.2462 0.3099 0.2145 0.0622  -0.0121 -0.0821 704  SER A CB  
5203  O OG  . SER A 706  ? 0.2545 0.3267 0.2239 0.0658  -0.0126 -0.0885 704  SER A OG  
5204  N N   . PRO A 707  ? 0.2454 0.2837 0.2265 0.0579  -0.0164 -0.0815 705  PRO A N   
5205  C CA  . PRO A 707  ? 0.2550 0.2850 0.2425 0.0571  -0.0182 -0.0824 705  PRO A CA  
5206  C C   . PRO A 707  ? 0.2416 0.2749 0.2291 0.0586  -0.0165 -0.0827 705  PRO A C   
5207  O O   . PRO A 707  ? 0.2671 0.3081 0.2493 0.0596  -0.0135 -0.0806 705  PRO A O   
5208  C CB  . PRO A 707  ? 0.2532 0.2741 0.2401 0.0530  -0.0171 -0.0750 705  PRO A CB  
5209  C CG  . PRO A 707  ? 0.2437 0.2696 0.2235 0.0522  -0.0134 -0.0694 705  PRO A CG  
5210  C CD  . PRO A 707  ? 0.2478 0.2836 0.2242 0.0549  -0.0135 -0.0732 705  PRO A CD  
5211  N N   . TRP A 708  ? 0.2417 0.2692 0.2355 0.0587  -0.0186 -0.0850 706  TRP A N   
5212  C CA  . TRP A 708  ? 0.2464 0.2769 0.2408 0.0603  -0.0173 -0.0857 706  TRP A CA  
5213  C C   . TRP A 708  ? 0.2684 0.2954 0.2596 0.0575  -0.0141 -0.0777 706  TRP A C   
5214  O O   . TRP A 708  ? 0.2828 0.3147 0.2721 0.0587  -0.0119 -0.0768 706  TRP A O   
5215  C CB  . TRP A 708  ? 0.2409 0.2666 0.2438 0.0616  -0.0208 -0.0911 706  TRP A CB  
5216  C CG  . TRP A 708  ? 0.2576 0.2719 0.2646 0.0582  -0.0219 -0.0863 706  TRP A CG  
5217  C CD1 . TRP A 708  ? 0.2925 0.2990 0.3039 0.0561  -0.0248 -0.0860 706  TRP A CD1 
5218  C CD2 . TRP A 708  ? 0.2689 0.2789 0.2757 0.0562  -0.0200 -0.0808 706  TRP A CD2 
5219  N NE1 . TRP A 708  ? 0.2737 0.2717 0.2874 0.0530  -0.0247 -0.0805 706  TRP A NE1 
5220  C CE2 . TRP A 708  ? 0.2623 0.2623 0.2733 0.0531  -0.0219 -0.0774 706  TRP A CE2 
5221  C CE3 . TRP A 708  ? 0.2553 0.2694 0.2590 0.0569  -0.0170 -0.0785 706  TRP A CE3 
5222  C CZ2 . TRP A 708  ? 0.2712 0.2654 0.2830 0.0506  -0.0208 -0.0719 706  TRP A CZ2 
5223  C CZ3 . TRP A 708  ? 0.2675 0.2753 0.2721 0.0544  -0.0160 -0.0731 706  TRP A CZ3 
5224  C CH2 . TRP A 708  ? 0.2620 0.2601 0.2706 0.0513  -0.0180 -0.0700 706  TRP A CH2 
5225  N N   . ASN A 709  ? 0.2450 0.2642 0.2358 0.0540  -0.0138 -0.0720 707  ASN A N   
5226  C CA  . ASN A 709  ? 0.2588 0.2728 0.2490 0.0515  -0.0118 -0.0657 707  ASN A CA  
5227  C C   . ASN A 709  ? 0.2970 0.3159 0.2805 0.0508  -0.0079 -0.0603 707  ASN A C   
5228  O O   . ASN A 709  ? 0.2706 0.2877 0.2536 0.0496  -0.0061 -0.0563 707  ASN A O   
5229  C CB  . ASN A 709  ? 0.2782 0.2823 0.2709 0.0481  -0.0132 -0.0620 707  ASN A CB  
5230  C CG  . ASN A 709  ? 0.2864 0.2904 0.2748 0.0462  -0.0121 -0.0586 707  ASN A CG  
5231  O OD1 . ASN A 709  ? 0.2968 0.3041 0.2845 0.0474  -0.0133 -0.0618 707  ASN A OD1 
5232  N ND2 . ASN A 709  ? 0.2855 0.2860 0.2712 0.0435  -0.0100 -0.0521 707  ASN A ND2 
5233  N N   . PHE A 710  ? 0.2724 0.2973 0.2513 0.0514  -0.0068 -0.0599 708  PHE A N   
5234  C CA  . PHE A 710  ? 0.2681 0.2994 0.2413 0.0512  -0.0035 -0.0553 708  PHE A CA  
5235  C C   . PHE A 710  ? 0.2732 0.3158 0.2443 0.0547  -0.0033 -0.0601 708  PHE A C   
5236  O O   . PHE A 710  ? 0.2769 0.3245 0.2445 0.0551  -0.0030 -0.0599 708  PHE A O   
5237  C CB  . PHE A 710  ? 0.2653 0.2940 0.2352 0.0486  -0.0023 -0.0499 708  PHE A CB  
5238  C CG  . PHE A 710  ? 0.3178 0.3365 0.2896 0.0453  -0.0024 -0.0454 708  PHE A CG  
5239  C CD1 . PHE A 710  ? 0.3221 0.3369 0.2957 0.0444  -0.0016 -0.0432 708  PHE A CD1 
5240  C CD2 . PHE A 710  ? 0.3080 0.3217 0.2796 0.0432  -0.0032 -0.0435 708  PHE A CD2 
5241  C CE1 . PHE A 710  ? 0.3347 0.3412 0.3098 0.0414  -0.0017 -0.0392 708  PHE A CE1 
5242  C CE2 . PHE A 710  ? 0.3377 0.3434 0.3109 0.0403  -0.0032 -0.0395 708  PHE A CE2 
5243  C CZ  . PHE A 710  ? 0.3809 0.3832 0.3558 0.0394  -0.0024 -0.0374 708  PHE A CZ  
5244  N N   . PRO A 711  ? 0.2632 0.3104 0.2364 0.0572  -0.0036 -0.0645 709  PRO A N   
5245  C CA  . PRO A 711  ? 0.2700 0.3273 0.2426 0.0609  -0.0045 -0.0711 709  PRO A CA  
5246  C C   . PRO A 711  ? 0.2628 0.3318 0.2295 0.0620  -0.0017 -0.0687 709  PRO A C   
5247  O O   . PRO A 711  ? 0.2780 0.3565 0.2433 0.0648  -0.0023 -0.0737 709  PRO A O   
5248  C CB  . PRO A 711  ? 0.2778 0.3357 0.2551 0.0631  -0.0055 -0.0760 709  PRO A CB  
5249  C CG  . PRO A 711  ? 0.2658 0.3186 0.2430 0.0608  -0.0035 -0.0698 709  PRO A CG  
5250  C CD  . PRO A 711  ? 0.2608 0.3040 0.2374 0.0570  -0.0034 -0.0640 709  PRO A CD  
5251  N N   . LEU A 712  ? 0.2629 0.3320 0.2263 0.0599  0.0012  -0.0613 710  LEU A N   
5252  C CA  . LEU A 712  ? 0.2505 0.3300 0.2086 0.0603  0.0037  -0.0577 710  LEU A CA  
5253  C C   . LEU A 712  ? 0.2448 0.3211 0.1999 0.0577  0.0045  -0.0517 710  LEU A C   
5254  O O   . LEU A 712  ? 0.2378 0.3216 0.1894 0.0584  0.0048  -0.0513 710  LEU A O   
5255  C CB  . LEU A 712  ? 0.2493 0.3332 0.2063 0.0603  0.0064  -0.0537 710  LEU A CB  
5256  C CG  . LEU A 712  ? 0.2747 0.3703 0.2268 0.0606  0.0089  -0.0495 710  LEU A CG  
5257  C CD1 . LEU A 712  ? 0.2617 0.3701 0.2120 0.0642  0.0083  -0.0556 710  LEU A CD1 
5258  C CD2 . LEU A 712  ? 0.2679 0.3662 0.2196 0.0598  0.0116  -0.0442 710  LEU A CD2 
5259  N N   . ALA A 713  ? 0.2354 0.3008 0.1920 0.0546  0.0045  -0.0473 711  ALA A N   
5260  C CA  . ALA A 713  ? 0.2247 0.2877 0.1787 0.0521  0.0055  -0.0411 711  ALA A CA  
5261  C C   . ALA A 713  ? 0.2380 0.3002 0.1913 0.0522  0.0036  -0.0436 711  ALA A C   
5262  O O   . ALA A 713  ? 0.2513 0.3193 0.2011 0.0523  0.0043  -0.0412 711  ALA A O   
5263  C CB  . ALA A 713  ? 0.2518 0.3041 0.2077 0.0490  0.0060  -0.0363 711  ALA A CB  
5264  N N   . ILE A 714  ? 0.2293 0.2844 0.1862 0.0521  0.0011  -0.0480 712  ILE A N   
5265  C CA  . ILE A 714  ? 0.2462 0.3002 0.2029 0.0521  -0.0008 -0.0503 712  ILE A CA  
5266  C C   . ILE A 714  ? 0.2450 0.3098 0.1998 0.0553  -0.0016 -0.0556 712  ILE A C   
5267  O O   . ILE A 714  ? 0.2587 0.3279 0.2107 0.0555  -0.0018 -0.0552 712  ILE A O   
5268  C CB  . ILE A 714  ? 0.2510 0.2948 0.2126 0.0510  -0.0035 -0.0533 712  ILE A CB  
5269  C CG1 . ILE A 714  ? 0.2815 0.3159 0.2439 0.0476  -0.0025 -0.0473 712  ILE A CG1 
5270  C CG2 . ILE A 714  ? 0.2753 0.3193 0.2373 0.0514  -0.0059 -0.0570 712  ILE A CG2 
5271  C CD1 . ILE A 714  ? 0.3995 0.4251 0.3652 0.0457  -0.0047 -0.0479 712  ILE A CD1 
5272  N N   . PHE A 715  ? 0.2338 0.3036 0.1902 0.0579  -0.0020 -0.0608 713  PHE A N   
5273  C CA  . PHE A 715  ? 0.2419 0.3236 0.1963 0.0612  -0.0025 -0.0661 713  PHE A CA  
5274  C C   . PHE A 715  ? 0.2671 0.3586 0.2158 0.0612  -0.0001 -0.0611 713  PHE A C   
5275  O O   . PHE A 715  ? 0.2456 0.3435 0.1918 0.0622  -0.0007 -0.0626 713  PHE A O   
5276  C CB  . PHE A 715  ? 0.2602 0.3463 0.2170 0.0638  -0.0025 -0.0708 713  PHE A CB  
5277  C CG  . PHE A 715  ? 0.2327 0.3321 0.1877 0.0675  -0.0028 -0.0767 713  PHE A CG  
5278  C CD1 . PHE A 715  ? 0.2532 0.3538 0.2109 0.0697  -0.0060 -0.0848 713  PHE A CD1 
5279  C CD2 . PHE A 715  ? 0.2415 0.3529 0.1923 0.0687  -0.0001 -0.0742 713  PHE A CD2 
5280  C CE1 . PHE A 715  ? 0.2740 0.3877 0.2300 0.0733  -0.0064 -0.0909 713  PHE A CE1 
5281  C CE2 . PHE A 715  ? 0.2579 0.3827 0.2067 0.0721  -0.0004 -0.0798 713  PHE A CE2 
5282  C CZ  . PHE A 715  ? 0.2859 0.4121 0.2373 0.0746  -0.0035 -0.0884 713  PHE A CZ  
5283  N N   . THR A 716  ? 0.2336 0.3265 0.1806 0.0599  0.0027  -0.0548 714  THR A N   
5284  C CA  . THR A 716  ? 0.2462 0.3486 0.1885 0.0597  0.0049  -0.0493 714  THR A CA  
5285  C C   . THR A 716  ? 0.2500 0.3483 0.1906 0.0574  0.0048  -0.0445 714  THR A C   
5286  O O   . THR A 716  ? 0.2300 0.3369 0.1673 0.0581  0.0051  -0.0430 714  THR A O   
5287  C CB  . THR A 716  ? 0.2455 0.3487 0.1874 0.0586  0.0076  -0.0433 714  THR A CB  
5288  O OG1 . THR A 716  ? 0.2618 0.3702 0.2052 0.0610  0.0078  -0.0479 714  THR A OG1 
5289  C CG2 . THR A 716  ? 0.2623 0.3749 0.2002 0.0580  0.0098  -0.0367 714  THR A CG2 
5290  N N   . GLY A 717  ? 0.2171 0.3030 0.1602 0.0548  0.0042  -0.0421 715  GLY A N   
5291  C CA  . GLY A 717  ? 0.2324 0.3142 0.1743 0.0526  0.0041  -0.0374 715  GLY A CA  
5292  C C   . GLY A 717  ? 0.2237 0.3090 0.1645 0.0538  0.0021  -0.0414 715  GLY A C   
5293  O O   . GLY A 717  ? 0.2395 0.3302 0.1773 0.0535  0.0026  -0.0381 715  GLY A O   
5294  N N   . GLN A 718  ? 0.2305 0.3129 0.1740 0.0551  -0.0003 -0.0486 716  GLN A N   
5295  C CA  . GLN A 718  ? 0.2346 0.3198 0.1775 0.0562  -0.0024 -0.0528 716  GLN A CA  
5296  C C   . GLN A 718  ? 0.2535 0.3530 0.1924 0.0588  -0.0018 -0.0542 716  GLN A C   
5297  O O   . GLN A 718  ? 0.2427 0.3469 0.1790 0.0588  -0.0022 -0.0528 716  GLN A O   
5298  C CB  . GLN A 718  ? 0.2230 0.3031 0.1704 0.0574  -0.0053 -0.0605 716  GLN A CB  
5299  C CG  . GLN A 718  ? 0.2249 0.2915 0.1763 0.0547  -0.0062 -0.0589 716  GLN A CG  
5300  C CD  . GLN A 718  ? 0.2621 0.3235 0.2185 0.0555  -0.0095 -0.0658 716  GLN A CD  
5301  O OE1 . GLN A 718  ? 0.2699 0.3230 0.2289 0.0535  -0.0110 -0.0651 716  GLN A OE1 
5302  N NE2 . GLN A 718  ? 0.2577 0.3241 0.2160 0.0584  -0.0107 -0.0723 716  GLN A NE2 
5303  N N   . ILE A 719  ? 0.2377 0.3449 0.1763 0.0611  -0.0011 -0.0573 717  ILE A N   
5304  C CA  . ILE A 719  ? 0.2328 0.3550 0.1676 0.0638  -0.0006 -0.0593 717  ILE A CA  
5305  C C   . ILE A 719  ? 0.2354 0.3641 0.1660 0.0624  0.0019  -0.0508 717  ILE A C   
5306  O O   . ILE A 719  ? 0.2455 0.3840 0.1727 0.0635  0.0017  -0.0504 717  ILE A O   
5307  C CB  . ILE A 719  ? 0.2708 0.3997 0.2065 0.0665  -0.0001 -0.0642 717  ILE A CB  
5308  C CG1 . ILE A 719  ? 0.2586 0.3830 0.1989 0.0684  -0.0031 -0.0735 717  ILE A CG1 
5309  C CG2 . ILE A 719  ? 0.3306 0.4762 0.2618 0.0689  0.0013  -0.0645 717  ILE A CG2 
5310  C CD1 . ILE A 719  ? 0.3309 0.4568 0.2737 0.0702  -0.0026 -0.0771 717  ILE A CD1 
5311  N N   . ALA A 720  ? 0.2420 0.3658 0.1730 0.0601  0.0040  -0.0439 718  ALA A N   
5312  C CA  . ALA A 720  ? 0.2453 0.3750 0.1733 0.0587  0.0060  -0.0355 718  ALA A CA  
5313  C C   . ALA A 720  ? 0.2310 0.3578 0.1581 0.0572  0.0051  -0.0323 718  ALA A C   
5314  O O   . ALA A 720  ? 0.2379 0.3740 0.1619 0.0574  0.0056  -0.0286 718  ALA A O   
5315  C CB  . ALA A 720  ? 0.2443 0.3672 0.1740 0.0564  0.0080  -0.0292 718  ALA A CB  
5316  N N   . ALA A 721  ? 0.2253 0.3394 0.1551 0.0555  0.0037  -0.0333 719  ALA A N   
5317  C CA  . ALA A 721  ? 0.2066 0.3174 0.1360 0.0540  0.0027  -0.0306 719  ALA A CA  
5318  C C   . ALA A 721  ? 0.2324 0.3522 0.1593 0.0562  0.0010  -0.0352 719  ALA A C   
5319  O O   . ALA A 721  ? 0.2335 0.3594 0.1580 0.0559  0.0012  -0.0312 719  ALA A O   
5320  C CB  . ALA A 721  ? 0.2329 0.3295 0.1658 0.0521  0.0013  -0.0322 719  ALA A CB  
5321  N N   . ALA A 722  ? 0.2284 0.3496 0.1565 0.0585  -0.0007 -0.0436 720  ALA A N   
5322  C CA  . ALA A 722  ? 0.2287 0.3584 0.1548 0.0607  -0.0025 -0.0488 720  ALA A CA  
5323  C C   . ALA A 722  ? 0.2485 0.3940 0.1702 0.0624  -0.0011 -0.0466 720  ALA A C   
5324  O O   . ALA A 722  ? 0.2468 0.3994 0.1657 0.0628  -0.0017 -0.0452 720  ALA A O   
5325  C CB  . ALA A 722  ? 0.2415 0.3697 0.1705 0.0630  -0.0048 -0.0586 720  ALA A CB  
5326  N N   . LEU A 723  ? 0.2347 0.3864 0.1556 0.0635  0.0007  -0.0461 721  LEU A N   
5327  C CA  . LEU A 723  ? 0.2281 0.3958 0.1448 0.0650  0.0022  -0.0436 721  LEU A CA  
5328  C C   . LEU A 723  ? 0.2442 0.4141 0.1589 0.0627  0.0036  -0.0337 721  LEU A C   
5329  O O   . LEU A 723  ? 0.2411 0.4228 0.1525 0.0635  0.0036  -0.0318 721  LEU A O   
5330  C CB  . LEU A 723  ? 0.2488 0.4212 0.1658 0.0661  0.0042  -0.0439 721  LEU A CB  
5331  C CG  . LEU A 723  ? 0.2259 0.4009 0.1446 0.0692  0.0030  -0.0538 721  LEU A CG  
5332  C CD1 . LEU A 723  ? 0.2566 0.4336 0.1761 0.0694  0.0052  -0.0521 721  LEU A CD1 
5333  C CD2 . LEU A 723  ? 0.2532 0.4433 0.1688 0.0724  0.0019  -0.0596 721  LEU A CD2 
5334  N N   . VAL A 724  ? 0.2544 0.4138 0.1713 0.0598  0.0047  -0.0272 722  VAL A N   
5335  C CA  . VAL A 724  ? 0.2408 0.4029 0.1566 0.0577  0.0059  -0.0176 722  VAL A CA  
5336  C C   . VAL A 724  ? 0.2355 0.3956 0.1507 0.0569  0.0042  -0.0166 722  VAL A C   
5337  O O   . VAL A 724  ? 0.2523 0.4193 0.1657 0.0562  0.0046  -0.0103 722  VAL A O   
5338  C CB  . VAL A 724  ? 0.2288 0.3809 0.1475 0.0550  0.0075  -0.0113 722  VAL A CB  
5339  C CG1 . VAL A 724  ? 0.2354 0.3720 0.1574 0.0528  0.0063  -0.0114 722  VAL A CG1 
5340  C CG2 . VAL A 724  ? 0.2422 0.4015 0.1600 0.0535  0.0091  -0.0018 722  VAL A CG2 
5341  N N   . ALA A 725  ? 0.2382 0.3895 0.1552 0.0571  0.0022  -0.0227 723  ALA A N   
5342  C CA  . ALA A 725  ? 0.2542 0.4045 0.1705 0.0567  0.0004  -0.0229 723  ALA A CA  
5343  C C   . ALA A 725  ? 0.2660 0.4304 0.1787 0.0594  -0.0007 -0.0269 723  ALA A C   
5344  O O   . ALA A 725  ? 0.2770 0.4421 0.1890 0.0594  -0.0024 -0.0275 723  ALA A O   
5345  C CB  . ALA A 725  ? 0.2453 0.3823 0.1650 0.0560  -0.0015 -0.0281 723  ALA A CB  
5346  N N   . GLY A 726  ? 0.2474 0.4235 0.1579 0.0617  0.0002  -0.0297 724  GLY A N   
5347  C CA  . GLY A 726  ? 0.2468 0.4380 0.1537 0.0644  -0.0007 -0.0334 724  GLY A CA  
5348  C C   . GLY A 726  ? 0.2707 0.4631 0.1781 0.0673  -0.0028 -0.0447 724  GLY A C   
5349  O O   . GLY A 726  ? 0.2832 0.4877 0.1878 0.0696  -0.0040 -0.0487 724  GLY A O   
5350  N N   . ASN A 727  ? 0.2633 0.4444 0.1746 0.0672  -0.0036 -0.0499 725  ASN A N   
5351  C CA  . ASN A 727  ? 0.2611 0.4416 0.1743 0.0697  -0.0060 -0.0605 725  ASN A CA  
5352  C C   . ASN A 727  ? 0.2715 0.4588 0.1850 0.0723  -0.0053 -0.0659 725  ASN A C   
5353  O O   . ASN A 727  ? 0.2778 0.4605 0.1926 0.0713  -0.0034 -0.0627 725  ASN A O   
5354  C CB  . ASN A 727  ? 0.2571 0.4204 0.1753 0.0679  -0.0076 -0.0628 725  ASN A CB  
5355  C CG  . ASN A 727  ? 0.2564 0.4117 0.1749 0.0652  -0.0081 -0.0574 725  ASN A CG  
5356  O OD1 . ASN A 727  ? 0.2816 0.4391 0.1995 0.0657  -0.0101 -0.0600 725  ASN A OD1 
5357  N ND2 . ASN A 727  ? 0.2539 0.4000 0.1737 0.0623  -0.0064 -0.0502 725  ASN A ND2 
5358  N N   . PRO A 728  ? 0.2553 0.4529 0.1680 0.0757  -0.0069 -0.0744 726  PRO A N   
5359  C CA  . PRO A 728  ? 0.2613 0.4631 0.1755 0.0783  -0.0067 -0.0811 726  PRO A CA  
5360  C C   . PRO A 728  ? 0.2467 0.4332 0.1671 0.0779  -0.0086 -0.0863 726  PRO A C   
5361  O O   . PRO A 728  ? 0.2884 0.4647 0.2115 0.0766  -0.0108 -0.0879 726  PRO A O   
5362  C CB  . PRO A 728  ? 0.2499 0.4645 0.1651 0.0811  -0.0086 -0.0876 726  PRO A CB  
5363  C CG  . PRO A 728  ? 0.2730 0.4848 0.1874 0.0806  -0.0108 -0.0886 726  PRO A CG  
5364  C CD  . PRO A 728  ? 0.2563 0.4610 0.1673 0.0774  -0.0093 -0.0793 726  PRO A CD  
5365  N N   . VAL A 729  ? 0.2850 0.4700 0.2076 0.0787  -0.0077 -0.0886 727  VAL A N   
5366  C CA  . VAL A 729  ? 0.2612 0.4310 0.1897 0.0776  -0.0090 -0.0911 727  VAL A CA  
5367  C C   . VAL A 729  ? 0.2546 0.4275 0.1869 0.0811  -0.0110 -0.1016 727  VAL A C   
5368  O O   . VAL A 729  ? 0.2791 0.4642 0.2097 0.0837  -0.0098 -0.1043 727  VAL A O   
5369  C CB  . VAL A 729  ? 0.2517 0.4141 0.1805 0.0748  -0.0062 -0.0829 727  VAL A CB  
5370  C CG1 . VAL A 729  ? 0.2572 0.4062 0.1918 0.0742  -0.0074 -0.0861 727  VAL A CG1 
5371  C CG2 . VAL A 729  ? 0.2866 0.4424 0.2135 0.0713  -0.0051 -0.0737 727  VAL A CG2 
5372  N N   . LEU A 730  ? 0.2480 0.4096 0.1860 0.0809  -0.0140 -0.1071 728  LEU A N   
5373  C CA  . LEU A 730  ? 0.2647 0.4244 0.2083 0.0834  -0.0162 -0.1160 728  LEU A CA  
5374  C C   . LEU A 730  ? 0.2392 0.3843 0.1870 0.0807  -0.0156 -0.1119 728  LEU A C   
5375  O O   . LEU A 730  ? 0.2508 0.3831 0.2012 0.0778  -0.0167 -0.1089 728  LEU A O   
5376  C CB  . LEU A 730  ? 0.2888 0.4460 0.2369 0.0850  -0.0205 -0.1248 728  LEU A CB  
5377  C CG  . LEU A 730  ? 0.2529 0.4223 0.1998 0.0865  -0.0218 -0.1274 728  LEU A CG  
5378  C CD1 . LEU A 730  ? 0.2787 0.4634 0.2238 0.0884  -0.0200 -0.1269 728  LEU A CD1 
5379  C CD2 . LEU A 730  ? 0.2737 0.4436 0.2148 0.0847  -0.0210 -0.1220 728  LEU A CD2 
5380  N N   . ALA A 731  ? 0.2549 0.4024 0.2031 0.0816  -0.0138 -0.1115 729  ALA A N   
5381  C CA  . ALA A 731  ? 0.2652 0.4005 0.2165 0.0790  -0.0128 -0.1068 729  ALA A CA  
5382  C C   . ALA A 731  ? 0.2652 0.3945 0.2239 0.0808  -0.0157 -0.1149 729  ALA A C   
5383  O O   . ALA A 731  ? 0.2762 0.4139 0.2362 0.0841  -0.0160 -0.1211 729  ALA A O   
5384  C CB  . ALA A 731  ? 0.2600 0.4015 0.2075 0.0786  -0.0089 -0.1006 729  ALA A CB  
5385  N N   . LYS A 732  ? 0.2478 0.3630 0.2117 0.0785  -0.0180 -0.1146 730  LYS A N   
5386  C CA  . LYS A 732  ? 0.2498 0.3579 0.2216 0.0797  -0.0212 -0.1215 730  LYS A CA  
5387  C C   . LYS A 732  ? 0.2658 0.3621 0.2402 0.0768  -0.0201 -0.1156 730  LYS A C   
5388  O O   . LYS A 732  ? 0.2626 0.3474 0.2390 0.0735  -0.0208 -0.1112 730  LYS A O   
5389  C CB  . LYS A 732  ? 0.2783 0.3802 0.2548 0.0795  -0.0253 -0.1263 730  LYS A CB  
5390  C CG  . LYS A 732  ? 0.2987 0.4010 0.2827 0.0827  -0.0294 -0.1369 730  LYS A CG  
5391  C CD  . LYS A 732  ? 0.2625 0.3563 0.2529 0.0824  -0.0301 -0.1373 730  LYS A CD  
5392  C CE  . LYS A 732  ? 0.2780 0.3562 0.2729 0.0783  -0.0315 -0.1323 730  LYS A CE  
5393  N NZ  . LYS A 732  ? 0.2821 0.3524 0.2828 0.0778  -0.0321 -0.1319 730  LYS A NZ  
5394  N N   . PRO A 733  ? 0.2484 0.3476 0.2232 0.0779  -0.0184 -0.1154 731  PRO A N   
5395  C CA  . PRO A 733  ? 0.2509 0.3393 0.2280 0.0751  -0.0173 -0.1098 731  PRO A CA  
5396  C C   . PRO A 733  ? 0.2435 0.3218 0.2294 0.0752  -0.0211 -0.1148 731  PRO A C   
5397  O O   . PRO A 733  ? 0.2686 0.3496 0.2592 0.0781  -0.0244 -0.1234 731  PRO A O   
5398  C CB  . PRO A 733  ? 0.2607 0.3577 0.2355 0.0769  -0.0145 -0.1091 731  PRO A CB  
5399  C CG  . PRO A 733  ? 0.2728 0.3821 0.2483 0.0814  -0.0160 -0.1186 731  PRO A CG  
5400  C CD  . PRO A 733  ? 0.2618 0.3748 0.2348 0.0818  -0.0174 -0.1206 731  PRO A CD  
5401  N N   . ALA A 734  ? 0.2420 0.3088 0.2303 0.0720  -0.0208 -0.1091 732  ALA A N   
5402  C CA  . ALA A 734  ? 0.2495 0.3063 0.2463 0.0716  -0.0243 -0.1123 732  ALA A CA  
5403  C C   . ALA A 734  ? 0.2718 0.3335 0.2734 0.0753  -0.0258 -0.1199 732  ALA A C   
5404  O O   . ALA A 734  ? 0.2817 0.3516 0.2800 0.0771  -0.0232 -0.1198 732  ALA A O   
5405  C CB  . ALA A 734  ? 0.2619 0.3081 0.2594 0.0678  -0.0229 -0.1044 732  ALA A CB  
5406  N N   . GLU A 735  ? 0.2824 0.3392 0.2923 0.0765  -0.0302 -0.1265 733  GLU A N   
5407  C CA  . GLU A 735  ? 0.3095 0.3708 0.3250 0.0804  -0.0322 -0.1346 733  GLU A CA  
5408  C C   . GLU A 735  ? 0.3164 0.3746 0.3333 0.0798  -0.0305 -0.1312 733  GLU A C   
5409  O O   . GLU A 735  ? 0.3067 0.3720 0.3254 0.0831  -0.0304 -0.1365 733  GLU A O   
5410  C CB  . GLU A 735  ? 0.3555 0.4109 0.3810 0.0815  -0.0377 -0.1421 733  GLU A CB  
5411  C CG  . GLU A 735  ? 0.3493 0.3901 0.3808 0.0777  -0.0400 -0.1373 733  GLU A CG  
5412  C CD  . GLU A 735  ? 0.3900 0.4262 0.4193 0.0748  -0.0405 -0.1336 733  GLU A CD  
5413  O OE1 . GLU A 735  ? 0.3370 0.3798 0.3582 0.0746  -0.0377 -0.1313 733  GLU A OE1 
5414  O OE2 . GLU A 735  ? 0.3530 0.3792 0.3892 0.0726  -0.0438 -0.1328 733  GLU A OE2 
5415  N N   . GLU A 736  ? 0.3004 0.3490 0.3165 0.0758  -0.0290 -0.1227 734  GLU A N   
5416  C CA  . GLU A 736  ? 0.2677 0.3129 0.2856 0.0751  -0.0277 -0.1195 734  GLU A CA  
5417  C C   . GLU A 736  ? 0.3044 0.3589 0.3147 0.0759  -0.0230 -0.1161 734  GLU A C   
5418  O O   . GLU A 736  ? 0.3118 0.3680 0.3238 0.0770  -0.0222 -0.1166 734  GLU A O   
5419  C CB  . GLU A 736  ? 0.2898 0.3224 0.3091 0.0705  -0.0277 -0.1115 734  GLU A CB  
5420  C CG  . GLU A 736  ? 0.3397 0.3623 0.3673 0.0692  -0.0323 -0.1135 734  GLU A CG  
5421  C CD  . GLU A 736  ? 0.3759 0.3961 0.4012 0.0672  -0.0329 -0.1117 734  GLU A CD  
5422  O OE1 . GLU A 736  ? 0.3203 0.3481 0.3384 0.0679  -0.0306 -0.1113 734  GLU A OE1 
5423  O OE2 . GLU A 736  ? 0.3387 0.3497 0.3696 0.0649  -0.0358 -0.1103 734  GLU A OE2 
5424  N N   . THR A 737  ? 0.2817 0.3424 0.2841 0.0751  -0.0202 -0.1123 735  THR A N   
5425  C CA  . THR A 737  ? 0.2833 0.3513 0.2786 0.0748  -0.0157 -0.1068 735  THR A CA  
5426  C C   . THR A 737  ? 0.2689 0.3509 0.2582 0.0773  -0.0140 -0.1093 735  THR A C   
5427  O O   . THR A 737  ? 0.2797 0.3652 0.2623 0.0756  -0.0111 -0.1031 735  THR A O   
5428  C CB  . THR A 737  ? 0.2506 0.3108 0.2422 0.0703  -0.0133 -0.0969 735  THR A CB  
5429  O OG1 . THR A 737  ? 0.2717 0.3286 0.2614 0.0686  -0.0142 -0.0954 735  THR A OG1 
5430  C CG2 . THR A 737  ? 0.2646 0.3130 0.2615 0.0681  -0.0145 -0.0942 735  THR A CG2 
5431  N N   . PRO A 738  ? 0.2614 0.3521 0.2531 0.0814  -0.0158 -0.1183 736  PRO A N   
5432  C CA  . PRO A 738  ? 0.2608 0.3660 0.2467 0.0839  -0.0143 -0.1208 736  PRO A CA  
5433  C C   . PRO A 738  ? 0.2797 0.3959 0.2601 0.0846  -0.0102 -0.1170 736  PRO A C   
5434  O O   . PRO A 738  ? 0.2853 0.4123 0.2594 0.0853  -0.0082 -0.1154 736  PRO A O   
5435  C CB  . PRO A 738  ? 0.3124 0.4230 0.3038 0.0882  -0.0179 -0.1324 736  PRO A CB  
5436  C CG  . PRO A 738  ? 0.2764 0.3800 0.2752 0.0888  -0.0196 -0.1350 736  PRO A CG  
5437  C CD  . PRO A 738  ? 0.2965 0.3851 0.2965 0.0841  -0.0194 -0.1267 736  PRO A CD  
5438  N N   . LEU A 739  ? 0.2560 0.3703 0.2387 0.0846  -0.0090 -0.1155 737  LEU A N   
5439  C CA  . LEU A 739  ? 0.2654 0.3916 0.2438 0.0858  -0.0055 -0.1132 737  LEU A CA  
5440  C C   . LEU A 739  ? 0.2277 0.3548 0.1992 0.0825  -0.0018 -0.1028 737  LEU A C   
5441  O O   . LEU A 739  ? 0.2681 0.4078 0.2341 0.0835  0.0006  -0.1008 737  LEU A O   
5442  C CB  . LEU A 739  ? 0.2600 0.3833 0.2429 0.0865  -0.0053 -0.1141 737  LEU A CB  
5443  C CG  . LEU A 739  ? 0.2683 0.3908 0.2590 0.0900  -0.0091 -0.1244 737  LEU A CG  
5444  C CD1 . LEU A 739  ? 0.2581 0.3766 0.2533 0.0901  -0.0087 -0.1239 737  LEU A CD1 
5445  C CD2 . LEU A 739  ? 0.3013 0.4397 0.2908 0.0944  -0.0095 -0.1326 737  LEU A CD2 
5446  N N   . ILE A 740  ? 0.2397 0.3538 0.2117 0.0786  -0.0015 -0.0959 738  ILE A N   
5447  C CA  . ILE A 740  ? 0.2544 0.3687 0.2207 0.0755  0.0017  -0.0862 738  ILE A CA  
5448  C C   . ILE A 740  ? 0.2410 0.3603 0.2028 0.0753  0.0016  -0.0854 738  ILE A C   
5449  O O   . ILE A 740  ? 0.2637 0.3905 0.2202 0.0744  0.0043  -0.0796 738  ILE A O   
5450  C CB  . ILE A 740  ? 0.2584 0.3581 0.2266 0.0716  0.0019  -0.0797 738  ILE A CB  
5451  C CG1 . ILE A 740  ? 0.2629 0.3633 0.2261 0.0686  0.0051  -0.0701 738  ILE A CG1 
5452  C CG2 . ILE A 740  ? 0.2726 0.3613 0.2437 0.0701  -0.0011 -0.0813 738  ILE A CG2 
5453  C CD1 . ILE A 740  ? 0.2874 0.3985 0.2480 0.0695  0.0081  -0.0672 738  ILE A CD1 
5454  N N   . ALA A 741  ? 0.2481 0.3641 0.2122 0.0763  -0.0015 -0.0913 739  ALA A N   
5455  C CA  . ALA A 741  ? 0.2623 0.3838 0.2224 0.0765  -0.0018 -0.0914 739  ALA A CA  
5456  C C   . ALA A 741  ? 0.2748 0.4136 0.2310 0.0798  -0.0005 -0.0946 739  ALA A C   
5457  O O   . ALA A 741  ? 0.2908 0.4374 0.2415 0.0791  0.0013  -0.0900 739  ALA A O   
5458  C CB  . ALA A 741  ? 0.3108 0.4252 0.2752 0.0770  -0.0057 -0.0977 739  ALA A CB  
5459  N N   . ALA A 742  ? 0.2659 0.4116 0.2250 0.0833  -0.0015 -0.1024 740  ALA A N   
5460  C CA  . ALA A 742  ? 0.2441 0.4076 0.1995 0.0866  -0.0001 -0.1058 740  ALA A CA  
5461  C C   . ALA A 742  ? 0.2693 0.4405 0.2198 0.0852  0.0040  -0.0972 740  ALA A C   
5462  O O   . ALA A 742  ? 0.2831 0.4675 0.2283 0.0860  0.0057  -0.0951 740  ALA A O   
5463  C CB  . ALA A 742  ? 0.2600 0.4290 0.2203 0.0907  -0.0020 -0.1158 740  ALA A CB  
5464  N N   . GLU A 743  ? 0.2547 0.4177 0.2069 0.0830  0.0054  -0.0918 741  GLU A N   
5465  C CA  . GLU A 743  ? 0.2890 0.4582 0.2373 0.0813  0.0091  -0.0832 741  GLU A CA  
5466  C C   . GLU A 743  ? 0.2610 0.4285 0.2048 0.0781  0.0104  -0.0747 741  GLU A C   
5467  O O   . GLU A 743  ? 0.2731 0.4519 0.2125 0.0779  0.0128  -0.0695 741  GLU A O   
5468  C CB  . GLU A 743  ? 0.2842 0.4444 0.2360 0.0797  0.0100  -0.0800 741  GLU A CB  
5469  C CG  . GLU A 743  ? 0.3041 0.4683 0.2530 0.0775  0.0136  -0.0707 741  GLU A CG  
5470  C CD  . GLU A 743  ? 0.2758 0.4582 0.2218 0.0800  0.0158  -0.0712 741  GLU A CD  
5471  O OE1 . GLU A 743  ? 0.2840 0.4765 0.2304 0.0838  0.0148  -0.0796 741  GLU A OE1 
5472  O OE2 . GLU A 743  ? 0.3186 0.5053 0.2621 0.0780  0.0186  -0.0630 741  GLU A OE2 
5473  N N   . GLY A 744  ? 0.2672 0.4211 0.2125 0.0757  0.0087  -0.0731 742  GLY A N   
5474  C CA  . GLY A 744  ? 0.2540 0.4063 0.1956 0.0730  0.0095  -0.0659 742  GLY A CA  
5475  C C   . GLY A 744  ? 0.2508 0.4162 0.1883 0.0749  0.0093  -0.0680 742  GLY A C   
5476  O O   . GLY A 744  ? 0.2791 0.4512 0.2124 0.0736  0.0112  -0.0611 742  GLY A O   
5477  N N   . VAL A 745  ? 0.2587 0.4280 0.1974 0.0780  0.0069  -0.0774 743  VAL A N   
5478  C CA  . VAL A 745  ? 0.2519 0.4351 0.1867 0.0803  0.0065  -0.0803 743  VAL A CA  
5479  C C   . VAL A 745  ? 0.2911 0.4915 0.2222 0.0820  0.0093  -0.0783 743  VAL A C   
5480  O O   . VAL A 745  ? 0.2860 0.4973 0.2124 0.0818  0.0106  -0.0740 743  VAL A O   
5481  C CB  . VAL A 745  ? 0.2794 0.4631 0.2173 0.0835  0.0031  -0.0916 743  VAL A CB  
5482  C CG1 . VAL A 745  ? 0.3366 0.5365 0.2716 0.0859  0.0026  -0.0950 743  VAL A CG1 
5483  C CG2 . VAL A 745  ? 0.3112 0.4802 0.2516 0.0814  0.0005  -0.0920 743  VAL A CG2 
5484  N N   . ARG A 746  ? 0.2668 0.4703 0.2003 0.0836  0.0102  -0.0810 744  ARG A N   
5485  C CA  . ARG A 746  ? 0.2762 0.4945 0.2079 0.0842  0.0124  -0.0778 744  ARG A CA  
5486  C C   . ARG A 746  ? 0.2635 0.4844 0.1907 0.0813  0.0157  -0.0664 744  ARG A C   
5487  O O   . ARG A 746  ? 0.2813 0.5145 0.2062 0.0808  0.0167  -0.0615 744  ARG A O   
5488  C CB  . ARG A 746  ? 0.2998 0.5184 0.2357 0.0857  0.0126  -0.0816 744  ARG A CB  
5489  C CG  . ARG A 746  ? 0.3030 0.5372 0.2384 0.0865  0.0141  -0.0795 744  ARG A CG  
5490  C CD  . ARG A 746  ? 0.2973 0.5306 0.2358 0.0871  0.0153  -0.0803 744  ARG A CD  
5491  N NE  . ARG A 746  ? 0.3143 0.5392 0.2512 0.0847  0.0181  -0.0729 744  ARG A NE  
5492  C CZ  . ARG A 746  ? 0.3597 0.5898 0.2933 0.0824  0.0210  -0.0632 744  ARG A CZ  
5493  N NH1 . ARG A 746  ? 0.3926 0.6365 0.3240 0.0821  0.0216  -0.0592 744  ARG A NH1 
5494  N NH2 . ARG A 746  ? 0.3571 0.5768 0.2913 0.0796  0.0226  -0.0563 744  ARG A NH2 
5495  N N   . ILE A 747  ? 0.2490 0.4550 0.1781 0.0780  0.0161  -0.0604 745  ILE A N   
5496  C CA  . ILE A 747  ? 0.2739 0.4794 0.2008 0.0745  0.0184  -0.0491 745  ILE A CA  
5497  C C   . ILE A 747  ? 0.2521 0.4609 0.1754 0.0734  0.0180  -0.0450 745  ILE A C   
5498  O O   . ILE A 747  ? 0.2566 0.4754 0.1768 0.0724  0.0199  -0.0377 745  ILE A O   
5499  C CB  . ILE A 747  ? 0.2727 0.4609 0.2033 0.0713  0.0185  -0.0447 745  ILE A CB  
5500  C CG1 . ILE A 747  ? 0.2669 0.4555 0.2003 0.0722  0.0196  -0.0463 745  ILE A CG1 
5501  C CG2 . ILE A 747  ? 0.2950 0.4798 0.2241 0.0676  0.0200  -0.0338 745  ILE A CG2 
5502  C CD1 . ILE A 747  ? 0.2968 0.4684 0.2343 0.0698  0.0192  -0.0444 745  ILE A CD1 
5503  N N   . LEU A 748  ? 0.2540 0.4544 0.1780 0.0734  0.0155  -0.0492 746  LEU A N   
5504  C CA  . LEU A 748  ? 0.2690 0.4723 0.1898 0.0724  0.0150  -0.0458 746  LEU A CA  
5505  C C   . LEU A 748  ? 0.2732 0.4959 0.1898 0.0751  0.0155  -0.0478 746  LEU A C   
5506  O O   . LEU A 748  ? 0.2702 0.5008 0.1834 0.0739  0.0165  -0.0408 746  LEU A O   
5507  C CB  . LEU A 748  ? 0.2573 0.4487 0.1800 0.0723  0.0120  -0.0511 746  LEU A CB  
5508  C CG  . LEU A 748  ? 0.2897 0.4636 0.2150 0.0686  0.0117  -0.0458 746  LEU A CG  
5509  C CD1 . LEU A 748  ? 0.3290 0.4914 0.2572 0.0687  0.0088  -0.0523 746  LEU A CD1 
5510  C CD2 . LEU A 748  ? 0.2851 0.4599 0.2079 0.0659  0.0128  -0.0367 746  LEU A CD2 
5511  N N   . ARG A 749  ? 0.2344 0.4642 0.1526 0.0783  0.0143  -0.0566 747  ARG A N   
5512  C CA  . ARG A 749  ? 0.2503 0.4958 0.1684 0.0796  0.0137  -0.0574 747  ARG A CA  
5513  C C   . ARG A 749  ? 0.2565 0.5126 0.1736 0.0784  0.0164  -0.0490 747  ARG A C   
5514  O O   . ARG A 749  ? 0.2893 0.5564 0.2047 0.0776  0.0168  -0.0438 747  ARG A O   
5515  C CB  . ARG A 749  ? 0.2927 0.5414 0.2146 0.0829  0.0113  -0.0684 747  ARG A CB  
5516  C CG  . ARG A 749  ? 0.3636 0.6061 0.2868 0.0841  0.0081  -0.0760 747  ARG A CG  
5517  C CD  . ARG A 749  ? 0.4090 0.6544 0.3370 0.0873  0.0053  -0.0868 747  ARG A CD  
5518  N NE  . ARG A 749  ? 0.3484 0.5903 0.2782 0.0885  0.0020  -0.0938 747  ARG A NE  
5519  C CZ  . ARG A 749  ? 0.3818 0.6294 0.3156 0.0912  -0.0008 -0.1025 747  ARG A CZ  
5520  N NH1 . ARG A 749  ? 0.3878 0.6448 0.3242 0.0932  -0.0007 -0.1058 747  ARG A NH1 
5521  N NH2 . ARG A 749  ? 0.3553 0.5995 0.2908 0.0920  -0.0038 -0.1082 747  ARG A NH2 
5522  N N   . GLU A 750  ? 0.2561 0.5090 0.1746 0.0780  0.0182  -0.0473 748  GLU A N   
5523  C CA  . GLU A 750  ? 0.2859 0.5480 0.2041 0.0764  0.0207  -0.0387 748  GLU A CA  
5524  C C   . GLU A 750  ? 0.2858 0.5468 0.2013 0.0732  0.0220  -0.0278 748  GLU A C   
5525  O O   . GLU A 750  ? 0.2929 0.5651 0.2081 0.0720  0.0230  -0.0208 748  GLU A O   
5526  C CB  . GLU A 750  ? 0.3004 0.5573 0.2207 0.0763  0.0224  -0.0385 748  GLU A CB  
5527  C CG  . GLU A 750  ? 0.3172 0.5833 0.2377 0.0746  0.0248  -0.0299 748  GLU A CG  
5528  C CD  . GLU A 750  ? 0.3462 0.6068 0.2689 0.0744  0.0266  -0.0294 748  GLU A CD  
5529  O OE1 . GLU A 750  ? 0.4487 0.7016 0.3733 0.0763  0.0256  -0.0374 748  GLU A OE1 
5530  O OE2 . GLU A 750  ? 0.3447 0.6084 0.2676 0.0722  0.0287  -0.0208 748  GLU A OE2 
5531  N N   . ALA A 751  ? 0.2755 0.5234 0.1897 0.0717  0.0218  -0.0264 749  ALA A N   
5532  C CA  . ALA A 751  ? 0.2662 0.5115 0.1785 0.0687  0.0228  -0.0163 749  ALA A CA  
5533  C C   . ALA A 751  ? 0.2870 0.5401 0.1976 0.0685  0.0214  -0.0146 749  ALA A C   
5534  O O   . ALA A 751  ? 0.3144 0.5670 0.2240 0.0661  0.0218  -0.0059 749  ALA A O   
5535  C CB  . ALA A 751  ? 0.2496 0.4748 0.1645 0.0664  0.0216  -0.0156 749  ALA A CB  
5536  N N   . GLY A 752  ? 0.2694 0.5293 0.1801 0.0712  0.0195  -0.0227 750  GLY A N   
5537  C CA  . GLY A 752  ? 0.2964 0.5657 0.2059 0.0713  0.0182  -0.0214 750  GLY A CA  
5538  C C   . GLY A 752  ? 0.2880 0.5521 0.1965 0.0727  0.0157  -0.0289 750  GLY A C   
5539  O O   . GLY A 752  ? 0.3019 0.5736 0.2094 0.0730  0.0145  -0.0283 750  GLY A O   
5540  N N   . ILE A 753  ? 0.3020 0.5535 0.2111 0.0737  0.0147  -0.0358 751  ILE A N   
5541  C CA  . ILE A 753  ? 0.2919 0.5386 0.2009 0.0751  0.0119  -0.0434 751  ILE A CA  
5542  C C   . ILE A 753  ? 0.2676 0.5255 0.1788 0.0781  0.0102  -0.0516 751  ILE A C   
5543  O O   . ILE A 753  ? 0.2858 0.5449 0.1996 0.0799  0.0102  -0.0571 751  ILE A O   
5544  C CB  . ILE A 753  ? 0.2719 0.5025 0.1819 0.0752  0.0111  -0.0486 751  ILE A CB  
5545  C CG1 . ILE A 753  ? 0.2709 0.4881 0.1822 0.0713  0.0122  -0.0395 751  ILE A CG1 
5546  C CG2 . ILE A 753  ? 0.2925 0.5190 0.2033 0.0766  0.0080  -0.0565 751  ILE A CG2 
5547  C CD1 . ILE A 753  ? 0.2575 0.4713 0.1674 0.0692  0.0113  -0.0342 751  ILE A CD1 
5548  N N   . PRO A 754  ? 0.2943 0.5604 0.2046 0.0788  0.0087  -0.0529 752  PRO A N   
5549  C CA  . PRO A 754  ? 0.2903 0.5675 0.2029 0.0818  0.0069  -0.0610 752  PRO A CA  
5550  C C   . PRO A 754  ? 0.2742 0.5425 0.1902 0.0840  0.0044  -0.0720 752  PRO A C   
5551  O O   . PRO A 754  ? 0.2767 0.5313 0.1929 0.0833  0.0034  -0.0741 752  PRO A O   
5552  C CB  . PRO A 754  ? 0.3200 0.6050 0.2308 0.0818  0.0056  -0.0596 752  PRO A CB  
5553  C CG  . PRO A 754  ? 0.3156 0.5965 0.2232 0.0786  0.0073  -0.0490 752  PRO A CG  
5554  C CD  . PRO A 754  ? 0.2977 0.5634 0.2052 0.0770  0.0084  -0.0471 752  PRO A CD  
5555  N N   . ALA A 755  ? 0.2994 0.5762 0.2187 0.0868  0.0033  -0.0791 753  ALA A N   
5556  C CA  . ALA A 755  ? 0.2790 0.5486 0.2027 0.0890  0.0006  -0.0898 753  ALA A CA  
5557  C C   . ALA A 755  ? 0.2865 0.5508 0.2109 0.0894  -0.0023 -0.0947 753  ALA A C   
5558  O O   . ALA A 755  ? 0.3214 0.5735 0.2489 0.0899  -0.0044 -0.1008 753  ALA A O   
5559  C CB  . ALA A 755  ? 0.3622 0.6443 0.2894 0.0920  -0.0004 -0.0964 753  ALA A CB  
5560  N N   . SER A 756  ? 0.2961 0.5694 0.2179 0.0892  -0.0026 -0.0919 754  SER A N   
5561  C CA  . SER A 756  ? 0.3010 0.5698 0.2233 0.0896  -0.0053 -0.0964 754  SER A CA  
5562  C C   . SER A 756  ? 0.3110 0.5642 0.2314 0.0870  -0.0051 -0.0926 754  SER A C   
5563  O O   . SER A 756  ? 0.3230 0.5677 0.2452 0.0873  -0.0077 -0.0978 754  SER A O   
5564  C CB  . SER A 756  ? 0.3144 0.5972 0.2344 0.0899  -0.0054 -0.0938 754  SER A CB  
5565  O OG  . SER A 756  ? 0.3545 0.6402 0.2700 0.0873  -0.0027 -0.0829 754  SER A OG  
5566  N N   . ALA A 757  ? 0.3074 0.5568 0.2243 0.0846  -0.0022 -0.0836 755  ALA A N   
5567  C CA  . ALA A 757  ? 0.2694 0.5049 0.1842 0.0822  -0.0018 -0.0795 755  ALA A CA  
5568  C C   . ALA A 757  ? 0.2916 0.5131 0.2089 0.0820  -0.0020 -0.0829 755  ALA A C   
5569  O O   . ALA A 757  ? 0.2841 0.4932 0.2007 0.0805  -0.0025 -0.0819 755  ALA A O   
5570  C CB  . ALA A 757  ? 0.2982 0.5363 0.2086 0.0795  0.0011  -0.0679 755  ALA A CB  
5571  N N   . LEU A 758  ? 0.2708 0.4941 0.1913 0.0835  -0.0017 -0.0868 756  LEU A N   
5572  C CA  . LEU A 758  ? 0.2791 0.4895 0.2024 0.0833  -0.0017 -0.0895 756  LEU A CA  
5573  C C   . LEU A 758  ? 0.2865 0.4991 0.2156 0.0860  -0.0038 -0.0987 756  LEU A C   
5574  O O   . LEU A 758  ? 0.3304 0.5521 0.2602 0.0872  -0.0025 -0.0987 756  LEU A O   
5575  C CB  . LEU A 758  ? 0.2699 0.4784 0.1907 0.0815  0.0018  -0.0815 756  LEU A CB  
5576  C CG  . LEU A 758  ? 0.2897 0.4841 0.2152 0.0806  0.0016  -0.0829 756  LEU A CG  
5577  C CD1 . LEU A 758  ? 0.2909 0.4688 0.2203 0.0788  -0.0011 -0.0847 756  LEU A CD1 
5578  C CD2 . LEU A 758  ? 0.2942 0.4856 0.2188 0.0778  0.0047  -0.0732 756  LEU A CD2 
5579  N N   . GLN A 759  ? 0.2588 0.4630 0.1922 0.0870  -0.0071 -0.1063 757  GLN A N   
5580  C CA  . GLN A 759  ? 0.2909 0.4956 0.2309 0.0895  -0.0097 -0.1153 757  GLN A CA  
5581  C C   . GLN A 759  ? 0.2875 0.4768 0.2316 0.0889  -0.0106 -0.1179 757  GLN A C   
5582  O O   . GLN A 759  ? 0.3249 0.5023 0.2689 0.0873  -0.0114 -0.1169 757  GLN A O   
5583  C CB  . GLN A 759  ? 0.2822 0.4905 0.2253 0.0911  -0.0134 -0.1224 757  GLN A CB  
5584  C CG  . GLN A 759  ? 0.2990 0.5236 0.2389 0.0921  -0.0127 -0.1208 757  GLN A CG  
5585  C CD  . GLN A 759  ? 0.2919 0.5195 0.2349 0.0937  -0.0163 -0.1277 757  GLN A CD  
5586  O OE1 . GLN A 759  ? 0.2964 0.5306 0.2442 0.0963  -0.0185 -0.1351 757  GLN A OE1 
5587  N NE2 . GLN A 759  ? 0.2950 0.5174 0.2355 0.0922  -0.0169 -0.1254 757  GLN A NE2 
5588  N N   . LEU A 760  ? 0.2878 0.4778 0.2358 0.0902  -0.0105 -0.1209 758  LEU A N   
5589  C CA  . LEU A 760  ? 0.3027 0.4791 0.2554 0.0899  -0.0115 -0.1233 758  LEU A CA  
5590  C C   . LEU A 760  ? 0.2702 0.4436 0.2310 0.0918  -0.0160 -0.1328 758  LEU A C   
5591  O O   . LEU A 760  ? 0.2723 0.4559 0.2359 0.0942  -0.0173 -0.1378 758  LEU A O   
5592  C CB  . LEU A 760  ? 0.2772 0.4562 0.2297 0.0902  -0.0088 -0.1207 758  LEU A CB  
5593  C CG  . LEU A 760  ? 0.2929 0.4587 0.2510 0.0900  -0.0099 -0.1234 758  LEU A CG  
5594  C CD1 . LEU A 760  ? 0.3067 0.4584 0.2637 0.0861  -0.0087 -0.1155 758  LEU A CD1 
5595  C CD2 . LEU A 760  ? 0.3102 0.4813 0.2699 0.0912  -0.0083 -0.1235 758  LEU A CD2 
5596  N N   . LEU A 761  ? 0.2920 0.4515 0.2569 0.0908  -0.0185 -0.1352 759  LEU A N   
5597  C CA  A LEU A 761  ? 0.3017 0.4568 0.2752 0.0922  -0.0231 -0.1436 759  LEU A CA  
5598  C CA  B LEU A 761  ? 0.3017 0.4567 0.2752 0.0922  -0.0231 -0.1436 759  LEU A CA  
5599  C C   . LEU A 761  ? 0.2962 0.4371 0.2757 0.0914  -0.0245 -0.1448 759  LEU A C   
5600  O O   . LEU A 761  ? 0.2999 0.4284 0.2815 0.0896  -0.0261 -0.1442 759  LEU A O   
5601  C CB  A LEU A 761  ? 0.2829 0.4360 0.2567 0.0917  -0.0257 -0.1456 759  LEU A CB  
5602  C CB  B LEU A 761  ? 0.2832 0.4356 0.2572 0.0917  -0.0258 -0.1456 759  LEU A CB  
5603  C CG  A LEU A 761  ? 0.2974 0.4648 0.2651 0.0924  -0.0242 -0.1437 759  LEU A CG  
5604  C CG  B LEU A 761  ? 0.2935 0.4590 0.2626 0.0925  -0.0252 -0.1450 759  LEU A CG  
5605  C CD1 A LEU A 761  ? 0.2914 0.4556 0.2574 0.0913  -0.0257 -0.1432 759  LEU A CD1 
5606  C CD1 B LEU A 761  ? 0.2974 0.4782 0.2670 0.0951  -0.0249 -0.1481 759  LEU A CD1 
5607  C CD2 A LEU A 761  ? 0.3027 0.4830 0.2740 0.0955  -0.0259 -0.1500 759  LEU A CD2 
5608  C CD2 B LEU A 761  ? 0.2800 0.4466 0.2400 0.0903  -0.0215 -0.1362 759  LEU A CD2 
5609  N N   . PRO A 762  ? 0.2689 0.4115 0.2516 0.0926  -0.0240 -0.1463 760  PRO A N   
5610  C CA  . PRO A 762  ? 0.2895 0.4190 0.2786 0.0919  -0.0255 -0.1475 760  PRO A CA  
5611  C C   . PRO A 762  ? 0.3408 0.4629 0.3392 0.0924  -0.0308 -0.1542 760  PRO A C   
5612  O O   . PRO A 762  ? 0.3318 0.4612 0.3332 0.0942  -0.0334 -0.1597 760  PRO A O   
5613  C CB  . PRO A 762  ? 0.2849 0.4211 0.2755 0.0937  -0.0242 -0.1486 760  PRO A CB  
5614  C CG  . PRO A 762  ? 0.2990 0.4504 0.2819 0.0945  -0.0208 -0.1455 760  PRO A CG  
5615  C CD  . PRO A 762  ? 0.2783 0.4351 0.2589 0.0946  -0.0221 -0.1468 760  PRO A CD  
5616  N N   . GLY A 763  ? 0.2891 0.3971 0.2927 0.0907  -0.0325 -0.1534 761  GLY A N   
5617  C CA  . GLY A 763  ? 0.3392 0.4391 0.3526 0.0907  -0.0376 -0.1589 761  GLY A CA  
5618  C C   . GLY A 763  ? 0.3241 0.4089 0.3395 0.0878  -0.0386 -0.1553 761  GLY A C   
5619  O O   . GLY A 763  ? 0.3063 0.3865 0.3162 0.0851  -0.0354 -0.1474 761  GLY A O   
5620  N N   . ASP A 764  ? 0.3525 0.4298 0.3770 0.0873  -0.0434 -0.1593 762  ASP A N   
5621  C CA  . ASP A 764  ? 0.3498 0.4123 0.3783 0.0844  -0.0451 -0.1562 762  ASP A CA  
5622  C C   . ASP A 764  ? 0.3628 0.4235 0.3881 0.0824  -0.0455 -0.1537 762  ASP A C   
5623  O O   . ASP A 764  ? 0.3110 0.3813 0.3290 0.0835  -0.0436 -0.1541 762  ASP A O   
5624  C CB  . ASP A 764  ? 0.4210 0.4757 0.4619 0.0843  -0.0499 -0.1599 762  ASP A CB  
5625  C CG  . ASP A 764  ? 0.4536 0.5129 0.5014 0.0860  -0.0543 -0.1668 762  ASP A CG  
5626  O OD1 . ASP A 764  ? 0.4338 0.4991 0.4776 0.0864  -0.0542 -0.1681 762  ASP A OD1 
5627  O OD2 . ASP A 764  ? 0.5685 0.6257 0.6262 0.0869  -0.0580 -0.1709 762  ASP A OD2 
5628  N N   . GLY A 765  ? 0.3263 0.3749 0.3572 0.0792  -0.0481 -0.1508 763  GLY A N   
5629  C CA  . GLY A 765  ? 0.3199 0.3659 0.3483 0.0767  -0.0485 -0.1476 763  GLY A CA  
5630  C C   . GLY A 765  ? 0.3516 0.4052 0.3810 0.0797  -0.0512 -0.1560 763  GLY A C   
5631  O O   . GLY A 765  ? 0.3676 0.4231 0.3921 0.0785  -0.0505 -0.1536 763  GLY A O   
5632  N N   . ARG A 766  ? 0.3468 0.4053 0.3830 0.0825  -0.0542 -0.1631 764  ARG A N   
5633  C CA  . ARG A 766  ? 0.3401 0.4073 0.3781 0.0844  -0.0566 -0.1686 764  ARG A CA  
5634  C C   . ARG A 766  ? 0.3595 0.4400 0.3869 0.0860  -0.0528 -0.1679 764  ARG A C   
5635  O O   . ARG A 766  ? 0.3601 0.4462 0.3854 0.0865  -0.0535 -0.1696 764  ARG A O   
5636  C CB  . ARG A 766  ? 0.4181 0.4893 0.4655 0.0869  -0.0600 -0.1753 764  ARG A CB  
5637  C CG  . ARG A 766  ? 0.5155 0.5755 0.5751 0.0857  -0.0649 -0.1771 764  ARG A CG  
5638  C CD  . ARG A 766  ? 0.4512 0.5173 0.5189 0.0886  -0.0677 -0.1837 764  ARG A CD  
5639  N NE  . ARG A 766  ? 0.5018 0.5719 0.5663 0.0899  -0.0647 -0.1827 764  ARG A NE  
5640  C CZ  . ARG A 766  ? 0.5149 0.5961 0.5802 0.0931  -0.0647 -0.1877 764  ARG A CZ  
5641  N NH1 . ARG A 766  ? 0.6079 0.6981 0.6766 0.0956  -0.0674 -0.1941 764  ARG A NH1 
5642  N NH2 . ARG A 766  ? 0.5580 0.6416 0.6206 0.0939  -0.0620 -0.1862 764  ARG A NH2 
5643  N N   . VAL A 767  ? 0.3006 0.3870 0.3219 0.0870  -0.0488 -0.1653 765  VAL A N   
5644  C CA  . VAL A 767  ? 0.3241 0.4234 0.3354 0.0882  -0.0450 -0.1634 765  VAL A CA  
5645  C C   . VAL A 767  ? 0.2975 0.3935 0.3008 0.0858  -0.0426 -0.1574 765  VAL A C   
5646  O O   . VAL A 767  ? 0.3172 0.4213 0.3151 0.0862  -0.0417 -0.1569 765  VAL A O   
5647  C CB  . VAL A 767  ? 0.2927 0.3990 0.3003 0.0896  -0.0416 -0.1617 765  VAL A CB  
5648  C CG1 . VAL A 767  ? 0.3342 0.4547 0.3322 0.0906  -0.0379 -0.1592 765  VAL A CG1 
5649  C CG2 . VAL A 767  ? 0.3346 0.4437 0.3508 0.0919  -0.0444 -0.1681 765  VAL A CG2 
5650  N N   . GLY A 768  ? 0.2993 0.3835 0.3025 0.0828  -0.0415 -0.1514 766  GLY A N   
5651  C CA  . GLY A 768  ? 0.2778 0.3576 0.2758 0.0790  -0.0394 -0.1428 766  GLY A CA  
5652  C C   . GLY A 768  ? 0.2982 0.3764 0.2985 0.0787  -0.0426 -0.1459 766  GLY A C   
5653  O O   . GLY A 768  ? 0.2980 0.3812 0.2922 0.0781  -0.0412 -0.1431 766  GLY A O   
5654  N N   . ALA A 769  ? 0.2903 0.3617 0.3001 0.0791  -0.0473 -0.1519 767  ALA A N   
5655  C CA  . ALA A 769  ? 0.3075 0.3763 0.3204 0.0785  -0.0507 -0.1548 767  ALA A CA  
5656  C C   . ALA A 769  ? 0.3160 0.3980 0.3260 0.0817  -0.0513 -0.1607 767  ALA A C   
5657  O O   . ALA A 769  ? 0.3327 0.4168 0.3395 0.0810  -0.0517 -0.1601 767  ALA A O   
5658  C CB  . ALA A 769  ? 0.3348 0.3937 0.3595 0.0782  -0.0557 -0.1597 767  ALA A CB  
5659  N N   . ALA A 770  ? 0.3208 0.4124 0.3326 0.0845  -0.0513 -0.1647 768  ALA A N   
5660  C CA  . ALA A 770  ? 0.3373 0.4425 0.3473 0.0871  -0.0517 -0.1687 768  ALA A CA  
5661  C C   . ALA A 770  ? 0.3192 0.4327 0.3176 0.0867  -0.0475 -0.1635 768  ALA A C   
5662  O O   . ALA A 770  ? 0.3318 0.4527 0.3277 0.0874  -0.0481 -0.1646 768  ALA A O   
5663  C CB  . ALA A 770  ? 0.3276 0.4417 0.3412 0.0901  -0.0522 -0.1736 768  ALA A CB  
5664  N N   . LEU A 771  ? 0.3090 0.4214 0.3007 0.0857  -0.0435 -0.1575 769  LEU A N   
5665  C CA  . LEU A 771  ? 0.3053 0.4251 0.2865 0.0851  -0.0395 -0.1515 769  LEU A CA  
5666  C C   . LEU A 771  ? 0.3131 0.4261 0.2918 0.0824  -0.0399 -0.1476 769  LEU A C   
5667  O O   . LEU A 771  ? 0.3284 0.4490 0.3015 0.0827  -0.0391 -0.1463 769  LEU A O   
5668  C CB  . LEU A 771  ? 0.2849 0.4042 0.2609 0.0844  -0.0353 -0.1457 769  LEU A CB  
5669  C CG  . LEU A 771  ? 0.3029 0.4312 0.2799 0.0868  -0.0341 -0.1479 769  LEU A CG  
5670  C CD1 . LEU A 771  ? 0.2964 0.4220 0.2691 0.0858  -0.0302 -0.1420 769  LEU A CD1 
5671  C CD2 . LEU A 771  ? 0.3165 0.4612 0.2896 0.0889  -0.0332 -0.1490 769  LEU A CD2 
5672  N N   . VAL A 772  ? 0.2870 0.3855 0.2709 0.0791  -0.0410 -0.1440 770  VAL A N   
5673  C CA  . VAL A 772  ? 0.2911 0.3822 0.2745 0.0757  -0.0414 -0.1385 770  VAL A CA  
5674  C C   . VAL A 772  ? 0.3187 0.4139 0.3040 0.0773  -0.0449 -0.1452 770  VAL A C   
5675  O O   . VAL A 772  ? 0.3473 0.4447 0.3284 0.0761  -0.0442 -0.1417 770  VAL A O   
5676  C CB  . VAL A 772  ? 0.3069 0.3828 0.2966 0.0723  -0.0424 -0.1345 770  VAL A CB  
5677  C CG1 . VAL A 772  ? 0.3164 0.3853 0.3070 0.0691  -0.0435 -0.1306 770  VAL A CG1 
5678  C CG2 . VAL A 772  ? 0.2813 0.3537 0.2676 0.0703  -0.0384 -0.1266 770  VAL A CG2 
5679  N N   . ALA A 773  ? 0.3256 0.4220 0.3179 0.0801  -0.0489 -0.1550 771  ALA A N   
5680  C CA  . ALA A 773  ? 0.3058 0.4049 0.3023 0.0810  -0.0526 -0.1602 771  ALA A CA  
5681  C C   . ALA A 773  ? 0.3907 0.5053 0.3822 0.0835  -0.0514 -0.1618 771  ALA A C   
5682  O O   . ALA A 773  ? 0.3996 0.5175 0.3933 0.0840  -0.0539 -0.1650 771  ALA A O   
5683  C CB  . ALA A 773  ? 0.3569 0.4512 0.3653 0.0819  -0.0570 -0.1667 771  ALA A CB  
5684  N N   . ALA A 774  ? 0.3545 0.4786 0.3398 0.0848  -0.0479 -0.1595 772  ALA A N   
5685  C CA  . ALA A 774  ? 0.3847 0.5244 0.3662 0.0872  -0.0469 -0.1609 772  ALA A CA  
5686  C C   . ALA A 774  ? 0.3364 0.4797 0.3113 0.0861  -0.0459 -0.1569 772  ALA A C   
5687  O O   . ALA A 774  ? 0.3628 0.5001 0.3322 0.0836  -0.0439 -0.1507 772  ALA A O   
5688  C CB  . ALA A 774  ? 0.3772 0.5258 0.3535 0.0885  -0.0431 -0.1580 772  ALA A CB  
5689  N N   . ALA A 775  ? 0.4426 0.5958 0.4181 0.0879  -0.0475 -0.1607 773  ALA A N   
5690  C CA  . ALA A 775  ? 0.3875 0.5428 0.3585 0.0868  -0.0475 -0.1579 773  ALA A CA  
5691  C C   . ALA A 775  ? 0.3148 0.4758 0.2755 0.0856  -0.0432 -0.1496 773  ALA A C   
5692  O O   . ALA A 775  ? 0.3787 0.5363 0.3353 0.0836  -0.0427 -0.1451 773  ALA A O   
5693  C CB  . ALA A 775  ? 0.4051 0.5707 0.3792 0.0892  -0.0500 -0.1638 773  ALA A CB  
5694  N N   . GLU A 776  ? 0.3139 0.4840 0.2710 0.0868  -0.0402 -0.1473 774  GLU A N   
5695  C CA  . GLU A 776  ? 0.3156 0.4923 0.2636 0.0858  -0.0363 -0.1390 774  GLU A CA  
5696  C C   . GLU A 776  ? 0.3197 0.4869 0.2642 0.0834  -0.0336 -0.1325 774  GLU A C   
5697  O O   . GLU A 776  ? 0.3362 0.5077 0.2737 0.0823  -0.0304 -0.1250 774  GLU A O   
5698  C CB  . GLU A 776  ? 0.3458 0.5381 0.2915 0.0880  -0.0343 -0.1387 774  GLU A CB  
5699  C CG  . GLU A 776  ? 0.3913 0.5948 0.3402 0.0906  -0.0367 -0.1450 774  GLU A CG  
5700  C CD  . GLU A 776  ? 0.4464 0.6502 0.4036 0.0931  -0.0394 -0.1539 774  GLU A CD  
5701  O OE1 . GLU A 776  ? 0.3694 0.5623 0.3311 0.0926  -0.0402 -0.1559 774  GLU A OE1 
5702  O OE2 . GLU A 776  ? 0.5215 0.7369 0.4811 0.0957  -0.0408 -0.1590 774  GLU A OE2 
5703  N N   . THR A 777  ? 0.2870 0.4414 0.2364 0.0826  -0.0350 -0.1351 775  THR A N   
5704  C CA  . THR A 777  ? 0.2877 0.4316 0.2362 0.0795  -0.0323 -0.1271 775  THR A CA  
5705  C C   . THR A 777  ? 0.3086 0.4460 0.2551 0.0760  -0.0315 -0.1192 775  THR A C   
5706  O O   . THR A 777  ? 0.3293 0.4604 0.2793 0.0750  -0.0343 -0.1214 775  THR A O   
5707  C CB  . THR A 777  ? 0.3140 0.4454 0.2704 0.0789  -0.0343 -0.1306 775  THR A CB  
5708  O OG1 . THR A 777  ? 0.2931 0.4308 0.2508 0.0820  -0.0344 -0.1367 775  THR A OG1 
5709  C CG2 . THR A 777  ? 0.2971 0.4161 0.2537 0.0749  -0.0318 -0.1213 775  THR A CG2 
5710  N N   . ALA A 778  ? 0.2752 0.4147 0.2163 0.0743  -0.0279 -0.1102 776  ALA A N   
5711  C CA  . ALA A 778  ? 0.2623 0.3980 0.2010 0.0714  -0.0270 -0.1027 776  ALA A CA  
5712  C C   . ALA A 778  ? 0.2756 0.3975 0.2164 0.0678  -0.0254 -0.0955 776  ALA A C   
5713  O O   . ALA A 778  ? 0.2809 0.3978 0.2209 0.0652  -0.0249 -0.0898 776  ALA A O   
5714  C CB  . ALA A 778  ? 0.2809 0.4293 0.2124 0.0720  -0.0244 -0.0972 776  ALA A CB  
5715  N N   . GLY A 779  ? 0.2551 0.3712 0.1988 0.0675  -0.0246 -0.0959 777  GLY A N   
5716  C CA  . GLY A 779  ? 0.2551 0.3587 0.2009 0.0642  -0.0232 -0.0897 777  GLY A CA  
5717  C C   . GLY A 779  ? 0.2411 0.3402 0.1906 0.0647  -0.0231 -0.0924 777  GLY A C   
5718  O O   . GLY A 779  ? 0.2511 0.3582 0.2001 0.0675  -0.0231 -0.0971 777  GLY A O   
5719  N N   . VAL A 780  ? 0.2433 0.3298 0.1967 0.0620  -0.0232 -0.0895 778  VAL A N   
5720  C CA  . VAL A 780  ? 0.2555 0.3362 0.2131 0.0621  -0.0235 -0.0916 778  VAL A CA  
5721  C C   . VAL A 780  ? 0.2429 0.3157 0.1999 0.0590  -0.0207 -0.0834 778  VAL A C   
5722  O O   . VAL A 780  ? 0.2492 0.3149 0.2065 0.0562  -0.0205 -0.0786 778  VAL A O   
5723  C CB  . VAL A 780  ? 0.2532 0.3262 0.2182 0.0621  -0.0273 -0.0978 778  VAL A CB  
5724  C CG1 . VAL A 780  ? 0.2602 0.3275 0.2300 0.0622  -0.0278 -0.0996 778  VAL A CG1 
5725  C CG2 . VAL A 780  ? 0.2605 0.3418 0.2265 0.0653  -0.0303 -0.1064 778  VAL A CG2 
5726  N N   . MET A 781  ? 0.2301 0.3047 0.1862 0.0596  -0.0187 -0.0821 779  MET A N   
5727  C CA  . MET A 781  ? 0.2207 0.2876 0.1769 0.0569  -0.0164 -0.0754 779  MET A CA  
5728  C C   . MET A 781  ? 0.2342 0.2950 0.1957 0.0573  -0.0177 -0.0791 779  MET A C   
5729  O O   . MET A 781  ? 0.2428 0.3093 0.2048 0.0598  -0.0177 -0.0834 779  MET A O   
5730  C CB  . MET A 781  ? 0.2447 0.3190 0.1957 0.0573  -0.0129 -0.0702 779  MET A CB  
5731  C CG  . MET A 781  ? 0.2481 0.3292 0.1942 0.0571  -0.0119 -0.0665 779  MET A CG  
5732  S SD  . MET A 781  ? 0.2580 0.3491 0.1988 0.0577  -0.0083 -0.0606 779  MET A SD  
5733  C CE  . MET A 781  ? 0.2582 0.3382 0.2001 0.0540  -0.0062 -0.0523 779  MET A CE  
5734  N N   . PHE A 782  ? 0.2502 0.3001 0.2161 0.0547  -0.0189 -0.0776 780  PHE A N   
5735  C CA  . PHE A 782  ? 0.2491 0.2921 0.2209 0.0546  -0.0206 -0.0805 780  PHE A CA  
5736  C C   . PHE A 782  ? 0.2467 0.2817 0.2189 0.0516  -0.0186 -0.0738 780  PHE A C   
5737  O O   . PHE A 782  ? 0.2429 0.2727 0.2141 0.0488  -0.0179 -0.0687 780  PHE A O   
5738  C CB  . PHE A 782  ? 0.2485 0.2856 0.2263 0.0540  -0.0245 -0.0847 780  PHE A CB  
5739  C CG  . PHE A 782  ? 0.2554 0.2848 0.2401 0.0535  -0.0265 -0.0869 780  PHE A CG  
5740  C CD1 . PHE A 782  ? 0.2403 0.2729 0.2284 0.0565  -0.0283 -0.0935 780  PHE A CD1 
5741  C CD2 . PHE A 782  ? 0.2397 0.2592 0.2274 0.0501  -0.0267 -0.0821 780  PHE A CD2 
5742  C CE1 . PHE A 782  ? 0.2470 0.2726 0.2419 0.0561  -0.0303 -0.0953 780  PHE A CE1 
5743  C CE2 . PHE A 782  ? 0.2464 0.2593 0.2405 0.0496  -0.0286 -0.0836 780  PHE A CE2 
5744  C CZ  . PHE A 782  ? 0.2331 0.2488 0.2310 0.0525  -0.0305 -0.0901 780  PHE A CZ  
5745  N N   . THR A 783  ? 0.2265 0.2605 0.2002 0.0522  -0.0179 -0.0742 781  THR A N   
5746  C CA  . THR A 783  ? 0.2446 0.2701 0.2202 0.0495  -0.0169 -0.0693 781  THR A CA  
5747  C C   . THR A 783  ? 0.2394 0.2606 0.2216 0.0503  -0.0195 -0.0738 781  THR A C   
5748  O O   . THR A 783  ? 0.2503 0.2768 0.2334 0.0532  -0.0200 -0.0788 781  THR A O   
5749  C CB  . THR A 783  ? 0.2509 0.2795 0.2219 0.0492  -0.0133 -0.0640 781  THR A CB  
5750  O OG1 . THR A 783  ? 0.2466 0.2795 0.2125 0.0485  -0.0113 -0.0599 781  THR A OG1 
5751  C CG2 . THR A 783  ? 0.2692 0.2891 0.2422 0.0463  -0.0123 -0.0590 781  THR A CG2 
5752  N N   . GLY A 784  ? 0.2488 0.2608 0.2357 0.0478  -0.0211 -0.0722 782  GLY A N   
5753  C CA  . GLY A 784  ? 0.2504 0.2578 0.2445 0.0483  -0.0242 -0.0763 782  GLY A CA  
5754  C C   . GLY A 784  ? 0.2258 0.2240 0.2246 0.0451  -0.0262 -0.0736 782  GLY A C   
5755  O O   . GLY A 784  ? 0.2636 0.2588 0.2596 0.0423  -0.0245 -0.0678 782  GLY A O   
5756  N N   . SER A 785  ? 0.2515 0.2457 0.2579 0.0455  -0.0299 -0.0778 783  SER A N   
5757  C CA  . SER A 785  ? 0.2613 0.2471 0.2729 0.0422  -0.0320 -0.0748 783  SER A CA  
5758  C C   . SER A 785  ? 0.2881 0.2737 0.2996 0.0411  -0.0333 -0.0750 783  SER A C   
5759  O O   . SER A 785  ? 0.2797 0.2708 0.2898 0.0434  -0.0341 -0.0796 783  SER A O   
5760  C CB  . SER A 785  ? 0.2868 0.2682 0.3074 0.0429  -0.0359 -0.0788 783  SER A CB  
5761  O OG  . SER A 785  ? 0.3047 0.2897 0.3288 0.0458  -0.0389 -0.0866 783  SER A OG  
5762  N N   . THR A 786  ? 0.2783 0.2579 0.2913 0.0376  -0.0334 -0.0697 784  THR A N   
5763  C CA  . THR A 786  ? 0.2959 0.2749 0.3095 0.0362  -0.0347 -0.0694 784  THR A CA  
5764  C C   . THR A 786  ? 0.2683 0.2470 0.2888 0.0377  -0.0392 -0.0760 784  THR A C   
5765  O O   . THR A 786  ? 0.2859 0.2678 0.3053 0.0385  -0.0401 -0.0788 784  THR A O   
5766  C CB  . THR A 786  ? 0.3029 0.2758 0.3179 0.0321  -0.0342 -0.0629 784  THR A CB  
5767  O OG1 . THR A 786  ? 0.3106 0.2842 0.3194 0.0311  -0.0302 -0.0575 784  THR A OG1 
5768  C CG2 . THR A 786  ? 0.3213 0.2940 0.3365 0.0306  -0.0352 -0.0622 784  THR A CG2 
5769  N N   . GLU A 787  ? 0.2987 0.2735 0.3266 0.0381  -0.0421 -0.0787 785  GLU A N   
5770  C CA  . GLU A 787  ? 0.2839 0.2577 0.3197 0.0395  -0.0468 -0.0851 785  GLU A CA  
5771  C C   . GLU A 787  ? 0.2738 0.2554 0.3072 0.0437  -0.0473 -0.0927 785  GLU A C   
5772  O O   . GLU A 787  ? 0.2900 0.2733 0.3262 0.0447  -0.0501 -0.0973 785  GLU A O   
5773  C CB  . GLU A 787  ? 0.3670 0.3352 0.4118 0.0391  -0.0500 -0.0862 785  GLU A CB  
5774  N N   . VAL A 788  ? 0.2838 0.2708 0.3120 0.0461  -0.0446 -0.0939 786  VAL A N   
5775  C CA  . VAL A 788  ? 0.2701 0.2661 0.2953 0.0501  -0.0447 -0.1006 786  VAL A CA  
5776  C C   . VAL A 788  ? 0.2863 0.2875 0.3042 0.0499  -0.0425 -0.0989 786  VAL A C   
5777  O O   . VAL A 788  ? 0.2798 0.2862 0.2975 0.0520  -0.0443 -0.1044 786  VAL A O   
5778  C CB  . VAL A 788  ? 0.2749 0.2758 0.2968 0.0527  -0.0423 -0.1021 786  VAL A CB  
5779  C CG1 . VAL A 788  ? 0.2888 0.3006 0.3057 0.0564  -0.0415 -0.1077 786  VAL A CG1 
5780  C CG2 . VAL A 788  ? 0.2894 0.2863 0.3199 0.0538  -0.0454 -0.1062 786  VAL A CG2 
5781  N N   . ALA A 789  ? 0.2542 0.2540 0.2660 0.0473  -0.0389 -0.0913 787  ALA A N   
5782  C CA  . ALA A 789  ? 0.2672 0.2713 0.2728 0.0469  -0.0371 -0.0891 787  ALA A CA  
5783  C C   . ALA A 789  ? 0.2466 0.2484 0.2566 0.0460  -0.0404 -0.0914 787  ALA A C   
5784  O O   . ALA A 789  ? 0.2529 0.2604 0.2598 0.0474  -0.0407 -0.0941 787  ALA A O   
5785  C CB  . ALA A 789  ? 0.2398 0.2410 0.2403 0.0439  -0.0334 -0.0805 787  ALA A CB  
5786  N N   . ARG A 790  ? 0.2689 0.2627 0.2863 0.0436  -0.0431 -0.0905 788  ARG A N   
5787  C CA  . ARG A 790  ? 0.2704 0.2616 0.2928 0.0425  -0.0465 -0.0923 788  ARG A CA  
5788  C C   . ARG A 790  ? 0.2807 0.2762 0.3071 0.0459  -0.0502 -0.1013 788  ARG A C   
5789  O O   . ARG A 790  ? 0.2883 0.2861 0.3151 0.0462  -0.0519 -0.1039 788  ARG A O   
5790  C CB  . ARG A 790  ? 0.3144 0.2966 0.3443 0.0391  -0.0486 -0.0887 788  ARG A CB  
5791  C CG  . ARG A 790  ? 0.3034 0.2823 0.3392 0.0373  -0.0521 -0.0895 788  ARG A CG  
5792  C CD  . ARG A 790  ? 0.2740 0.2449 0.3164 0.0334  -0.0535 -0.0842 788  ARG A CD  
5793  N NE  . ARG A 790  ? 0.2899 0.2593 0.3265 0.0306  -0.0495 -0.0762 788  ARG A NE  
5794  C CZ  . ARG A 790  ? 0.2797 0.2457 0.3163 0.0290  -0.0479 -0.0717 788  ARG A CZ  
5795  N NH1 . ARG A 790  ? 0.3385 0.3016 0.3808 0.0297  -0.0498 -0.0736 788  ARG A NH1 
5796  N NH2 . ARG A 790  ? 0.3382 0.3039 0.3693 0.0267  -0.0443 -0.0651 788  ARG A NH2 
5797  N N   . LEU A 791  ? 0.2890 0.2860 0.3186 0.0485  -0.0514 -0.1065 789  LEU A N   
5798  C CA  . LEU A 791  ? 0.2905 0.2928 0.3236 0.0523  -0.0547 -0.1158 789  LEU A CA  
5799  C C   . LEU A 791  ? 0.2959 0.3086 0.3204 0.0548  -0.0524 -0.1181 789  LEU A C   
5800  O O   . LEU A 791  ? 0.2910 0.3082 0.3167 0.0566  -0.0549 -0.1238 789  LEU A O   
5801  C CB  . LEU A 791  ? 0.2895 0.2920 0.3272 0.0547  -0.0561 -0.1206 789  LEU A CB  
5802  C CG  . LEU A 791  ? 0.3564 0.3492 0.4042 0.0527  -0.0593 -0.1196 789  LEU A CG  
5803  C CD1 . LEU A 791  ? 0.3562 0.3499 0.4073 0.0554  -0.0599 -0.1237 789  LEU A CD1 
5804  C CD2 . LEU A 791  ? 0.3715 0.3605 0.4285 0.0523  -0.0645 -0.1238 789  LEU A CD2 
5805  N N   . ILE A 792  ? 0.2576 0.2746 0.2737 0.0549  -0.0479 -0.1135 790  ILE A N   
5806  C CA  . ILE A 792  ? 0.2760 0.3030 0.2837 0.0570  -0.0455 -0.1142 790  ILE A CA  
5807  C C   . ILE A 792  ? 0.2970 0.3237 0.3022 0.0550  -0.0454 -0.1111 790  ILE A C   
5808  O O   . ILE A 792  ? 0.2866 0.3205 0.2893 0.0570  -0.0463 -0.1151 790  ILE A O   
5809  C CB  . ILE A 792  ? 0.2682 0.2991 0.2686 0.0571  -0.0408 -0.1091 790  ILE A CB  
5810  C CG1 . ILE A 792  ? 0.2779 0.3115 0.2806 0.0599  -0.0411 -0.1137 790  ILE A CG1 
5811  C CG2 . ILE A 792  ? 0.2798 0.3204 0.2716 0.0584  -0.0381 -0.1077 790  ILE A CG2 
5812  C CD1 . ILE A 792  ? 0.2743 0.3100 0.2713 0.0596  -0.0368 -0.1084 790  ILE A CD1 
5813  N N   . GLN A 793  ? 0.2593 0.2783 0.2651 0.0512  -0.0444 -0.1041 791  GLN A N   
5814  C CA  . GLN A 793  ? 0.2755 0.2935 0.2799 0.0492  -0.0446 -0.1013 791  GLN A CA  
5815  C C   . GLN A 793  ? 0.2714 0.2896 0.2819 0.0502  -0.0492 -0.1079 791  GLN A C   
5816  O O   . GLN A 793  ? 0.2845 0.3075 0.2922 0.0508  -0.0496 -0.1093 791  GLN A O   
5817  C CB  . GLN A 793  ? 0.2995 0.3086 0.3055 0.0450  -0.0434 -0.0937 791  GLN A CB  
5818  C CG  . GLN A 793  ? 0.2912 0.2985 0.2967 0.0426  -0.0437 -0.0905 791  GLN A CG  
5819  C CD  . GLN A 793  ? 0.3040 0.3026 0.3132 0.0387  -0.0435 -0.0845 791  GLN A CD  
5820  O OE1 . GLN A 793  ? 0.3425 0.3355 0.3581 0.0377  -0.0454 -0.0849 791  GLN A OE1 
5821  N NE2 . GLN A 793  ? 0.3344 0.3323 0.3397 0.0364  -0.0413 -0.0788 791  GLN A NE2 
5822  N N   . ALA A 794  ? 0.2953 0.3084 0.3145 0.0504  -0.0528 -0.1122 792  ALA A N   
5823  C CA  . ALA A 794  ? 0.3336 0.3467 0.3597 0.0514  -0.0576 -0.1190 792  ALA A CA  
5824  C C   . ALA A 794  ? 0.3132 0.3366 0.3364 0.0558  -0.0585 -0.1269 792  ALA A C   
5825  O O   . ALA A 794  ? 0.3544 0.3813 0.3781 0.0565  -0.0605 -0.1303 792  ALA A O   
5826  C CB  . ALA A 794  ? 0.3238 0.3293 0.3606 0.0508  -0.0614 -0.1216 792  ALA A CB  
5827  N N   . GLN A 795  ? 0.2998 0.3289 0.3201 0.0586  -0.0569 -0.1297 793  GLN A N   
5828  C CA  . GLN A 795  ? 0.2974 0.3379 0.3143 0.0628  -0.0574 -0.1370 793  GLN A CA  
5829  C C   . GLN A 795  ? 0.3326 0.3804 0.3409 0.0628  -0.0549 -0.1340 793  GLN A C   
5830  O O   . GLN A 795  ? 0.3348 0.3895 0.3426 0.0650  -0.0569 -0.1396 793  GLN A O   
5831  C CB  . GLN A 795  ? 0.3740 0.4199 0.3876 0.0654  -0.0550 -0.1385 793  GLN A CB  
5832  C CG  . GLN A 795  ? 0.4160 0.4592 0.4377 0.0673  -0.0580 -0.1447 793  GLN A CG  
5833  C CD  . GLN A 795  ? 0.4332 0.4842 0.4503 0.0702  -0.0552 -0.1464 793  GLN A CD  
5834  O OE1 . GLN A 795  ? 0.4544 0.5028 0.4679 0.0687  -0.0517 -0.1399 793  GLN A OE1 
5835  N NE2 . GLN A 795  ? 0.3541 0.4151 0.3712 0.0744  -0.0567 -0.1551 793  GLN A NE2 
5836  N N   . LEU A 796  ? 0.2965 0.3430 0.2981 0.0605  -0.0506 -0.1253 794  LEU A N   
5837  C CA  . LEU A 796  ? 0.3171 0.3707 0.3107 0.0605  -0.0482 -0.1219 794  LEU A CA  
5838  C C   . LEU A 796  ? 0.3000 0.3505 0.2954 0.0586  -0.0501 -0.1208 794  LEU A C   
5839  O O   . LEU A 796  ? 0.3529 0.4106 0.3432 0.0594  -0.0494 -0.1207 794  LEU A O   
5840  C CB  . LEU A 796  ? 0.2855 0.3384 0.2726 0.0587  -0.0434 -0.1130 794  LEU A CB  
5841  C CG  . LEU A 796  ? 0.2918 0.3507 0.2751 0.0609  -0.0408 -0.1134 794  LEU A CG  
5842  C CD1 . LEU A 796  ? 0.3108 0.3682 0.2883 0.0587  -0.0364 -0.1043 794  LEU A CD1 
5843  C CD2 . LEU A 796  ? 0.3312 0.4033 0.3103 0.0647  -0.0411 -0.1191 794  LEU A CD2 
5844  N N   . ALA A 797  ? 0.3192 0.3597 0.3218 0.0559  -0.0524 -0.1199 795  ALA A N   
5845  C CA  . ALA A 797  ? 0.3593 0.3971 0.3639 0.0540  -0.0542 -0.1188 795  ALA A CA  
5846  C C   . ALA A 797  ? 0.3673 0.4117 0.3741 0.0567  -0.0579 -0.1271 795  ALA A C   
5847  O O   . ALA A 797  ? 0.4472 0.4931 0.4529 0.0559  -0.0587 -0.1265 795  ALA A O   
5848  C CB  . ALA A 797  ? 0.3323 0.3588 0.3447 0.0505  -0.0561 -0.1159 795  ALA A CB  
5849  N N   . ASP A 798  ? 0.3508 0.3996 0.3604 0.0601  -0.0600 -0.1351 796  ASP A N   
5850  C CA  . ASP A 798  ? 0.4058 0.4623 0.4170 0.0632  -0.0634 -0.1438 796  ASP A CA  
5851  C C   . ASP A 798  ? 0.4761 0.5446 0.4778 0.0653  -0.0609 -0.1435 796  ASP A C   
5852  O O   . ASP A 798  ? 0.4218 0.4970 0.4234 0.0673  -0.0633 -0.1492 796  ASP A O   
5853  C CB  . ASP A 798  ? 0.3527 0.4115 0.3693 0.0666  -0.0662 -0.1526 796  ASP A CB  
5854  C CG  . ASP A 798  ? 0.5693 0.6172 0.5971 0.0650  -0.0699 -0.1544 796  ASP A CG  
5855  O OD1 . ASP A 798  ? 0.5583 0.5988 0.5908 0.0619  -0.0718 -0.1516 796  ASP A OD1 
5856  O OD2 . ASP A 798  ? 0.5975 0.6443 0.6295 0.0667  -0.0710 -0.1585 796  ASP A OD2 
5857  N N   . ARG A 799  ? 0.3657 0.4369 0.3596 0.0648  -0.0562 -0.1368 797  ARG A N   
5858  C CA  . ARG A 799  ? 0.3425 0.4264 0.3279 0.0673  -0.0538 -0.1370 797  ARG A CA  
5859  C C   . ARG A 799  ? 0.3120 0.3976 0.2907 0.0652  -0.0509 -0.1290 797  ARG A C   
5860  O O   . ARG A 799  ? 0.3260 0.4032 0.3046 0.0619  -0.0491 -0.1215 797  ARG A O   
5861  C CB  . ARG A 799  ? 0.3964 0.4831 0.3786 0.0685  -0.0508 -0.1355 797  ARG A CB  
5862  C CG  . ARG A 799  ? 0.4551 0.5381 0.4447 0.0701  -0.0533 -0.1422 797  ARG A CG  
5863  C CD  . ARG A 799  ? 0.5171 0.6117 0.5066 0.0746  -0.0554 -0.1518 797  ARG A CD  
5864  N NE  . ARG A 799  ? 0.5470 0.6536 0.5272 0.0764  -0.0516 -0.1494 797  ARG A NE  
5865  C CZ  . ARG A 799  ? 0.4864 0.5949 0.4631 0.0766  -0.0483 -0.1458 797  ARG A CZ  
5866  N NH1 . ARG A 799  ? 0.5512 0.6507 0.5327 0.0755  -0.0481 -0.1448 797  ARG A NH1 
5867  N NH2 . ARG A 799  ? 0.5796 0.6995 0.5481 0.0780  -0.0450 -0.1429 797  ARG A NH2 
5868  N N   . LEU A 800  ? 0.3112 0.4082 0.2844 0.0674  -0.0507 -0.1308 798  LEU A N   
5869  C CA  . LEU A 800  ? 0.3578 0.4588 0.3238 0.0661  -0.0478 -0.1233 798  LEU A CA  
5870  C C   . LEU A 800  ? 0.3065 0.4212 0.2654 0.0690  -0.0456 -0.1236 798  LEU A C   
5871  O O   . LEU A 800  ? 0.3689 0.4920 0.3281 0.0723  -0.0471 -0.1313 798  LEU A O   
5872  C CB  . LEU A 800  ? 0.3269 0.4292 0.2936 0.0656  -0.0501 -0.1244 798  LEU A CB  
5873  C CG  . LEU A 800  ? 0.3534 0.4436 0.3268 0.0625  -0.0522 -0.1231 798  LEU A CG  
5874  C CD1 . LEU A 800  ? 0.3766 0.4702 0.3504 0.0626  -0.0548 -0.1255 798  LEU A CD1 
5875  C CD2 . LEU A 800  ? 0.3734 0.4551 0.3453 0.0589  -0.0489 -0.1135 798  LEU A CD2 
5876  N N   . SER A 801  ? 0.3380 0.4551 0.2907 0.0676  -0.0420 -0.1152 799  SER A N   
5877  C CA  . SER A 801  ? 0.3627 0.4934 0.3084 0.0698  -0.0398 -0.1138 799  SER A CA  
5878  C C   . SER A 801  ? 0.4293 0.5707 0.3727 0.0719  -0.0421 -0.1183 799  SER A C   
5879  O O   . SER A 801  ? 0.3801 0.5173 0.3271 0.0712  -0.0449 -0.1210 799  SER A O   
5880  C CB  . SER A 801  ? 0.3882 0.5177 0.3290 0.0673  -0.0360 -0.1031 799  SER A CB  
5881  O OG  . SER A 801  ? 0.3618 0.4899 0.3018 0.0656  -0.0366 -0.0994 799  SER A OG  
5882  N N   . PRO A 802  ? 0.3572 0.5130 0.2949 0.0745  -0.0409 -0.1192 800  PRO A N   
5883  C CA  . PRO A 802  ? 0.3679 0.5350 0.3026 0.0763  -0.0428 -0.1224 800  PRO A CA  
5884  C C   . PRO A 802  ? 0.4065 0.5704 0.3396 0.0737  -0.0426 -0.1156 800  PRO A C   
5885  O O   . PRO A 802  ? 0.4663 0.6352 0.3994 0.0747  -0.0451 -0.1192 800  PRO A O   
5886  C CB  . PRO A 802  ? 0.4273 0.6094 0.3564 0.0785  -0.0403 -0.1208 800  PRO A CB  
5887  C CG  . PRO A 802  ? 0.4322 0.6119 0.3635 0.0794  -0.0390 -0.1229 800  PRO A CG  
5888  C CD  . PRO A 802  ? 0.3895 0.5530 0.3238 0.0763  -0.0384 -0.1188 800  PRO A CD  
5889  N N   . ALA A 803  ? 0.4417 0.5976 0.3739 0.0707  -0.0398 -0.1063 801  ALA A N   
5890  C CA  . ALA A 803  ? 0.4080 0.5589 0.3399 0.0680  -0.0397 -0.1001 801  ALA A CA  
5891  C C   . ALA A 803  ? 0.4969 0.6345 0.4355 0.0659  -0.0420 -0.1022 801  ALA A C   
5892  O O   . ALA A 803  ? 0.4595 0.5922 0.3986 0.0637  -0.0420 -0.0975 801  ALA A O   
5893  C CB  . ALA A 803  ? 0.4932 0.6414 0.4220 0.0657  -0.0360 -0.0896 801  ALA A CB  
5894  N N   . GLY A 804  ? 0.4563 0.5882 0.4003 0.0666  -0.0439 -0.1089 802  GLY A N   
5895  C CA  . GLY A 804  ? 0.3740 0.4936 0.3248 0.0644  -0.0462 -0.1106 802  GLY A CA  
5896  C C   . GLY A 804  ? 0.3695 0.4766 0.3224 0.0609  -0.0441 -0.1035 802  GLY A C   
5897  O O   . GLY A 804  ? 0.4020 0.5008 0.3587 0.0585  -0.0452 -0.1018 802  GLY A O   
5898  N N   . ARG A 805  ? 0.3693 0.4752 0.3200 0.0606  -0.0411 -0.0995 803  ARG A N   
5899  C CA  . ARG A 805  ? 0.3888 0.4837 0.3412 0.0575  -0.0389 -0.0928 803  ARG A CA  
5900  C C   . ARG A 805  ? 0.2886 0.3785 0.2440 0.0577  -0.0385 -0.0951 803  ARG A C   
5901  O O   . ARG A 805  ? 0.3122 0.4084 0.2670 0.0604  -0.0390 -0.1005 803  ARG A O   
5902  C CB  . ARG A 805  ? 0.4072 0.5050 0.3540 0.0564  -0.0353 -0.0841 803  ARG A CB  
5903  C CG  . ARG A 805  ? 0.3838 0.4862 0.3279 0.0560  -0.0357 -0.0811 803  ARG A CG  
5904  C CD  . ARG A 805  ? 0.4465 0.5402 0.3953 0.0538  -0.0377 -0.0812 803  ARG A CD  
5905  N NE  . ARG A 805  ? 0.4046 0.5029 0.3512 0.0536  -0.0382 -0.0787 803  ARG A NE  
5906  C CZ  . ARG A 805  ? 0.4521 0.5559 0.3992 0.0550  -0.0411 -0.0837 803  ARG A CZ  
5907  N NH1 . ARG A 805  ? 0.4427 0.5476 0.3929 0.0567  -0.0439 -0.0919 803  ARG A NH1 
5908  N NH2 . ARG A 805  ? 0.5186 0.6267 0.4633 0.0547  -0.0413 -0.0805 803  ARG A NH2 
5909  N N   . PRO A 806  ? 0.3287 0.4073 0.2877 0.0549  -0.0377 -0.0913 804  PRO A N   
5910  C CA  . PRO A 806  ? 0.3092 0.3825 0.2716 0.0549  -0.0376 -0.0934 804  PRO A CA  
5911  C C   . PRO A 806  ? 0.2888 0.3682 0.2465 0.0565  -0.0347 -0.0916 804  PRO A C   
5912  O O   . PRO A 806  ? 0.3006 0.3841 0.2530 0.0561  -0.0319 -0.0856 804  PRO A O   
5913  C CB  . PRO A 806  ? 0.3121 0.3737 0.2777 0.0513  -0.0367 -0.0878 804  PRO A CB  
5914  C CG  . PRO A 806  ? 0.3419 0.4017 0.3083 0.0497  -0.0378 -0.0860 804  PRO A CG  
5915  C CD  . PRO A 806  ? 0.3489 0.4193 0.3095 0.0516  -0.0372 -0.0857 804  PRO A CD  
5916  N N   . ILE A 807  ? 0.2735 0.3534 0.2337 0.0583  -0.0356 -0.0970 805  ILE A N   
5917  C CA  . ILE A 807  ? 0.2739 0.3589 0.2307 0.0598  -0.0330 -0.0958 805  ILE A CA  
5918  C C   . ILE A 807  ? 0.2768 0.3529 0.2340 0.0570  -0.0303 -0.0888 805  ILE A C   
5919  O O   . ILE A 807  ? 0.2845 0.3508 0.2470 0.0553  -0.0315 -0.0894 805  ILE A O   
5920  C CB  . ILE A 807  ? 0.2835 0.3710 0.2439 0.0626  -0.0351 -0.1042 805  ILE A CB  
5921  C CG1 . ILE A 807  ? 0.3136 0.4099 0.2744 0.0655  -0.0381 -0.1121 805  ILE A CG1 
5922  C CG2 . ILE A 807  ? 0.3009 0.3939 0.2580 0.0641  -0.0323 -0.1029 805  ILE A CG2 
5923  C CD1 . ILE A 807  ? 0.3487 0.4582 0.3022 0.0673  -0.0365 -0.1107 805  ILE A CD1 
5924  N N   . PRO A 808  ? 0.2589 0.3381 0.2110 0.0563  -0.0270 -0.0821 806  PRO A N   
5925  C CA  . PRO A 808  ? 0.2598 0.3306 0.2124 0.0536  -0.0246 -0.0755 806  PRO A CA  
5926  C C   . PRO A 808  ? 0.2549 0.3217 0.2107 0.0540  -0.0245 -0.0780 806  PRO A C   
5927  O O   . PRO A 808  ? 0.2592 0.3327 0.2141 0.0567  -0.0245 -0.0822 806  PRO A O   
5928  C CB  . PRO A 808  ? 0.2878 0.3653 0.2345 0.0536  -0.0214 -0.0691 806  PRO A CB  
5929  C CG  . PRO A 808  ? 0.3125 0.3989 0.2561 0.0550  -0.0224 -0.0704 806  PRO A CG  
5930  C CD  . PRO A 808  ? 0.2709 0.3613 0.2169 0.0577  -0.0254 -0.0796 806  PRO A CD  
5931  N N   . LEU A 809  ? 0.2548 0.3108 0.2143 0.0514  -0.0244 -0.0753 807  LEU A N   
5932  C CA  . LEU A 809  ? 0.2532 0.3041 0.2161 0.0513  -0.0244 -0.0765 807  LEU A CA  
5933  C C   . LEU A 809  ? 0.2644 0.3091 0.2262 0.0486  -0.0215 -0.0690 807  LEU A C   
5934  O O   . LEU A 809  ? 0.2707 0.3092 0.2335 0.0459  -0.0214 -0.0651 807  LEU A O   
5935  C CB  . LEU A 809  ? 0.2645 0.3080 0.2345 0.0507  -0.0278 -0.0812 807  LEU A CB  
5936  C CG  . LEU A 809  ? 0.2527 0.2892 0.2271 0.0499  -0.0280 -0.0815 807  LEU A CG  
5937  C CD1 . LEU A 809  ? 0.2752 0.3178 0.2488 0.0529  -0.0276 -0.0856 807  LEU A CD1 
5938  C CD2 . LEU A 809  ? 0.3094 0.3386 0.2913 0.0489  -0.0317 -0.0851 807  LEU A CD2 
5939  N N   . ILE A 810  ? 0.2346 0.2815 0.1944 0.0492  -0.0193 -0.0672 808  ILE A N   
5940  C CA  . ILE A 810  ? 0.2438 0.2840 0.2039 0.0469  -0.0171 -0.0614 808  ILE A CA  
5941  C C   . ILE A 810  ? 0.2368 0.2716 0.2018 0.0470  -0.0185 -0.0649 808  ILE A C   
5942  O O   . ILE A 810  ? 0.2636 0.3030 0.2290 0.0495  -0.0190 -0.0693 808  ILE A O   
5943  C CB  . ILE A 810  ? 0.2279 0.2737 0.1831 0.0473  -0.0139 -0.0568 808  ILE A CB  
5944  C CG1 . ILE A 810  ? 0.2703 0.3225 0.2211 0.0475  -0.0128 -0.0535 808  ILE A CG1 
5945  C CG2 . ILE A 810  ? 0.2662 0.3045 0.2222 0.0448  -0.0119 -0.0512 808  ILE A CG2 
5946  C CD1 . ILE A 810  ? 0.3024 0.3596 0.2493 0.0475  -0.0098 -0.0479 808  ILE A CD1 
5947  N N   . ALA A 811  ? 0.2355 0.2610 0.2044 0.0444  -0.0193 -0.0629 809  ALA A N   
5948  C CA  . ALA A 811  ? 0.2329 0.2527 0.2072 0.0442  -0.0210 -0.0657 809  ALA A CA  
5949  C C   . ALA A 811  ? 0.2356 0.2486 0.2104 0.0414  -0.0190 -0.0597 809  ALA A C   
5950  O O   . ALA A 811  ? 0.2493 0.2567 0.2251 0.0387  -0.0191 -0.0562 809  ALA A O   
5951  C CB  . ALA A 811  ? 0.2589 0.2745 0.2389 0.0438  -0.0247 -0.0699 809  ALA A CB  
5952  N N   . GLU A 812  ? 0.2150 0.2289 0.1887 0.0421  -0.0173 -0.0587 810  GLU A N   
5953  C CA  . GLU A 812  ? 0.2214 0.2299 0.1950 0.0398  -0.0153 -0.0533 810  GLU A CA  
5954  C C   . GLU A 812  ? 0.2233 0.2267 0.2023 0.0396  -0.0171 -0.0557 810  GLU A C   
5955  O O   . GLU A 812  ? 0.2416 0.2480 0.2217 0.0420  -0.0177 -0.0597 810  GLU A O   
5956  C CB  . GLU A 812  ? 0.2578 0.2716 0.2265 0.0406  -0.0121 -0.0500 810  GLU A CB  
5957  C CG  . GLU A 812  ? 0.2818 0.3007 0.2458 0.0407  -0.0107 -0.0473 810  GLU A CG  
5958  C CD  . GLU A 812  ? 0.3171 0.3306 0.2814 0.0379  -0.0106 -0.0433 810  GLU A CD  
5959  O OE1 . GLU A 812  ? 0.2777 0.2877 0.2413 0.0360  -0.0087 -0.0384 810  GLU A OE1 
5960  O OE2 . GLU A 812  ? 0.3016 0.3146 0.2671 0.0377  -0.0125 -0.0452 810  GLU A OE2 
5961  N N   . THR A 813  ? 0.2295 0.2254 0.2122 0.0369  -0.0181 -0.0533 811  THR A N   
5962  C CA  . THR A 813  ? 0.2511 0.2419 0.2403 0.0366  -0.0209 -0.0560 811  THR A CA  
5963  C C   . THR A 813  ? 0.2459 0.2309 0.2365 0.0341  -0.0198 -0.0512 811  THR A C   
5964  O O   . THR A 813  ? 0.2620 0.2479 0.2487 0.0335  -0.0168 -0.0472 811  THR A O   
5965  C CB  . THR A 813  ? 0.2498 0.2384 0.2434 0.0360  -0.0242 -0.0589 811  THR A CB  
5966  O OG1 . THR A 813  ? 0.2660 0.2526 0.2579 0.0335  -0.0233 -0.0546 811  THR A OG1 
5967  C CG2 . THR A 813  ? 0.2508 0.2460 0.2433 0.0392  -0.0255 -0.0649 811  THR A CG2 
5968  N N   . GLY A 814  ? 0.2651 0.2443 0.2618 0.0326  -0.0223 -0.0516 812  GLY A N   
5969  C CA  . GLY A 814  ? 0.2641 0.2387 0.2629 0.0308  -0.0218 -0.0481 812  GLY A CA  
5970  C C   . GLY A 814  ? 0.2611 0.2326 0.2580 0.0276  -0.0200 -0.0419 812  GLY A C   
5971  O O   . GLY A 814  ? 0.2668 0.2394 0.2611 0.0266  -0.0192 -0.0402 812  GLY A O   
5972  N N   . GLY A 815  ? 0.2430 0.2109 0.2415 0.0259  -0.0195 -0.0387 813  GLY A N   
5973  C CA  . GLY A 815  ? 0.2646 0.2301 0.2616 0.0229  -0.0178 -0.0332 813  GLY A CA  
5974  C C   . GLY A 815  ? 0.2749 0.2355 0.2773 0.0206  -0.0196 -0.0311 813  GLY A C   
5975  O O   . GLY A 815  ? 0.2937 0.2525 0.3008 0.0214  -0.0218 -0.0334 813  GLY A O   
5976  N N   . GLN A 816  ? 0.2478 0.2067 0.2498 0.0177  -0.0189 -0.0267 814  GLN A N   
5977  C CA  . GLN A 816  ? 0.2500 0.2052 0.2560 0.0152  -0.0199 -0.0233 814  GLN A CA  
5978  C C   . GLN A 816  ? 0.2596 0.2157 0.2611 0.0136  -0.0168 -0.0189 814  GLN A C   
5979  O O   . GLN A 816  ? 0.2798 0.2358 0.2810 0.0112  -0.0163 -0.0158 814  GLN A O   
5980  C CB  . GLN A 816  ? 0.2714 0.2244 0.2825 0.0130  -0.0227 -0.0225 814  GLN A CB  
5981  C CG  . GLN A 816  ? 0.3031 0.2528 0.3194 0.0104  -0.0244 -0.0191 814  GLN A CG  
5982  C CD  . GLN A 816  ? 0.3475 0.2949 0.3687 0.0119  -0.0267 -0.0217 814  GLN A CD  
5983  O OE1 . GLN A 816  ? 0.3079 0.2558 0.3271 0.0133  -0.0252 -0.0220 814  GLN A OE1 
5984  N NE2 . GLN A 816  ? 0.3568 0.3019 0.3850 0.0117  -0.0304 -0.0236 814  GLN A NE2 
5985  N N   . ASN A 817  ? 0.2349 0.1923 0.2330 0.0150  -0.0146 -0.0188 815  ASN A N   
5986  C CA  . ASN A 817  ? 0.2311 0.1903 0.2242 0.0144  -0.0115 -0.0159 815  ASN A CA  
5987  C C   . ASN A 817  ? 0.2253 0.1827 0.2196 0.0119  -0.0110 -0.0119 815  ASN A C   
5988  O O   . ASN A 817  ? 0.2345 0.1900 0.2315 0.0117  -0.0120 -0.0114 815  ASN A O   
5989  C CB  . ASN A 817  ? 0.2169 0.1786 0.2065 0.0169  -0.0096 -0.0172 815  ASN A CB  
5990  C CG  . ASN A 817  ? 0.2146 0.1790 0.2034 0.0195  -0.0103 -0.0214 815  ASN A CG  
5991  O OD1 . ASN A 817  ? 0.2218 0.1877 0.2093 0.0196  -0.0104 -0.0221 815  ASN A OD1 
5992  N ND2 . ASN A 817  ? 0.2204 0.1858 0.2102 0.0217  -0.0108 -0.0243 815  ASN A ND2 
5993  N N   . ALA A 818  ? 0.2087 0.1671 0.2008 0.0101  -0.0096 -0.0091 816  ALA A N   
5994  C CA  . ALA A 818  ? 0.2238 0.1816 0.2164 0.0077  -0.0090 -0.0055 816  ALA A CA  
5995  C C   . ALA A 818  ? 0.1957 0.1552 0.1841 0.0080  -0.0061 -0.0041 816  ALA A C   
5996  O O   . ALA A 818  ? 0.2136 0.1749 0.1987 0.0095  -0.0046 -0.0051 816  ALA A O   
5997  C CB  . ALA A 818  ? 0.2249 0.1833 0.2188 0.0053  -0.0096 -0.0036 816  ALA A CB  
5998  N N   . MET A 819  ? 0.2196 0.1787 0.2086 0.0065  -0.0057 -0.0015 817  MET A N   
5999  C CA  . MET A 819  ? 0.2085 0.1691 0.1944 0.0061  -0.0033 0.0001  817  MET A CA  
6000  C C   . MET A 819  ? 0.2197 0.1812 0.2066 0.0034  -0.0034 0.0030  817  MET A C   
6001  O O   . MET A 819  ? 0.2275 0.1879 0.2174 0.0020  -0.0050 0.0045  817  MET A O   
6002  C CB  . MET A 819  ? 0.2273 0.1872 0.2126 0.0073  -0.0025 0.0002  817  MET A CB  
6003  C CG  . MET A 819  ? 0.2343 0.1956 0.2172 0.0068  -0.0004 0.0019  817  MET A CG  
6004  S SD  . MET A 819  ? 0.2570 0.2176 0.2398 0.0077  0.0004  0.0023  817  MET A SD  
6005  C CE  . MET A 819  ? 0.2982 0.2595 0.2795 0.0107  0.0011  -0.0003 817  MET A CE  
6006  N N   . ILE A 820  ? 0.2106 0.1745 0.1953 0.0028  -0.0019 0.0036  818  ILE A N   
6007  C CA  . ILE A 820  ? 0.2271 0.1931 0.2123 0.0004  -0.0017 0.0060  818  ILE A CA  
6008  C C   . ILE A 820  ? 0.1988 0.1661 0.1822 0.0004  0.0000  0.0068  818  ILE A C   
6009  O O   . ILE A 820  ? 0.2231 0.1906 0.2042 0.0020  0.0015  0.0055  818  ILE A O   
6010  C CB  . ILE A 820  ? 0.2108 0.1793 0.1955 -0.0004 -0.0015 0.0058  818  ILE A CB  
6011  C CG1 . ILE A 820  ? 0.2530 0.2203 0.2402 -0.0006 -0.0034 0.0052  818  ILE A CG1 
6012  C CG2 . ILE A 820  ? 0.2423 0.2142 0.2271 -0.0026 -0.0009 0.0080  818  ILE A CG2 
6013  C CD1 . ILE A 820  ? 0.2329 0.2026 0.2197 -0.0014 -0.0033 0.0050  818  ILE A CD1 
6014  N N   . VAL A 821  ? 0.2192 0.1873 0.2037 -0.0013 -0.0004 0.0089  819  VAL A N   
6015  C CA  . VAL A 821  ? 0.2290 0.1983 0.2121 -0.0014 0.0010  0.0096  819  VAL A CA  
6016  C C   . VAL A 821  ? 0.2393 0.2127 0.2227 -0.0036 0.0011  0.0113  819  VAL A C   
6017  O O   . VAL A 821  ? 0.2600 0.2344 0.2454 -0.0055 -0.0002 0.0134  819  VAL A O   
6018  C CB  . VAL A 821  ? 0.2359 0.2031 0.2204 -0.0012 0.0003  0.0105  819  VAL A CB  
6019  C CG1 . VAL A 821  ? 0.2662 0.2349 0.2494 -0.0014 0.0016  0.0112  819  VAL A CG1 
6020  C CG2 . VAL A 821  ? 0.2241 0.1882 0.2087 0.0011  0.0001  0.0085  819  VAL A CG2 
6021  N N   . ASP A 822  ? 0.2369 0.2130 0.2184 -0.0034 0.0027  0.0105  820  ASP A N   
6022  C CA  . ASP A 822  ? 0.2491 0.2300 0.2306 -0.0053 0.0030  0.0117  820  ASP A CA  
6023  C C   . ASP A 822  ? 0.2482 0.2306 0.2292 -0.0057 0.0036  0.0124  820  ASP A C   
6024  O O   . ASP A 822  ? 0.2485 0.2279 0.2293 -0.0045 0.0037  0.0121  820  ASP A O   
6025  C CB  . ASP A 822  ? 0.2625 0.2464 0.2430 -0.0050 0.0039  0.0100  820  ASP A CB  
6026  C CG  . ASP A 822  ? 0.2383 0.2223 0.2175 -0.0033 0.0054  0.0078  820  ASP A CG  
6027  O OD1 . ASP A 822  ? 0.2527 0.2352 0.2315 -0.0026 0.0058  0.0076  820  ASP A OD1 
6028  O OD2 . ASP A 822  ? 0.2668 0.2524 0.2458 -0.0027 0.0059  0.0062  820  ASP A OD2 
6029  N N   . SER A 823  ? 0.2475 0.2352 0.2284 -0.0073 0.0038  0.0132  821  SER A N   
6030  C CA  . SER A 823  ? 0.2590 0.2488 0.2394 -0.0078 0.0042  0.0139  821  SER A CA  
6031  C C   . SER A 823  ? 0.2845 0.2739 0.2638 -0.0060 0.0055  0.0113  821  SER A C   
6032  O O   . SER A 823  ? 0.3089 0.2997 0.2880 -0.0063 0.0058  0.0114  821  SER A O   
6033  C CB  . SER A 823  ? 0.2775 0.2741 0.2580 -0.0101 0.0040  0.0156  821  SER A CB  
6034  O OG  . SER A 823  ? 0.3164 0.3170 0.2962 -0.0099 0.0049  0.0135  821  SER A OG  
6035  N N   . SER A 824  ? 0.2476 0.2352 0.2265 -0.0043 0.0063  0.0090  822  SER A N   
6036  C CA  . SER A 824  ? 0.2578 0.2446 0.2364 -0.0027 0.0072  0.0069  822  SER A CA  
6037  C C   . SER A 824  ? 0.2635 0.2452 0.2422 -0.0012 0.0073  0.0070  822  SER A C   
6038  O O   . SER A 824  ? 0.2859 0.2668 0.2649 -0.0001 0.0080  0.0059  822  SER A O   
6039  C CB  . SER A 824  ? 0.2551 0.2430 0.2339 -0.0017 0.0078  0.0046  822  SER A CB  
6040  O OG  . SER A 824  ? 0.2480 0.2322 0.2266 -0.0006 0.0077  0.0045  822  SER A OG  
6041  N N   . ALA A 825  ? 0.2718 0.2503 0.2506 -0.0011 0.0066  0.0082  823  ALA A N   
6042  C CA  . ALA A 825  ? 0.2714 0.2460 0.2502 0.0004  0.0067  0.0082  823  ALA A CA  
6043  C C   . ALA A 825  ? 0.2766 0.2507 0.2559 0.0001  0.0066  0.0092  823  ALA A C   
6044  O O   . ALA A 825  ? 0.2898 0.2661 0.2695 -0.0015 0.0061  0.0105  823  ALA A O   
6045  C CB  . ALA A 825  ? 0.2694 0.2414 0.2485 0.0007  0.0057  0.0087  823  ALA A CB  
6046  N N   . LEU A 826  ? 0.2894 0.2612 0.2687 0.0016  0.0072  0.0088  824  LEU A N   
6047  C CA  . LEU A 826  ? 0.2910 0.2621 0.2709 0.0016  0.0072  0.0097  824  LEU A CA  
6048  C C   . LEU A 826  ? 0.3131 0.2818 0.2938 0.0017  0.0062  0.0107  824  LEU A C   
6049  O O   . LEU A 826  ? 0.3007 0.2673 0.2813 0.0031  0.0062  0.0101  824  LEU A O   
6050  C CB  . LEU A 826  ? 0.3452 0.3153 0.3254 0.0031  0.0082  0.0089  824  LEU A CB  
6051  N N   . ALA A 827  ? 0.2938 0.2632 0.2754 0.0003  0.0052  0.0123  825  ALA A N   
6052  C CA  . ALA A 827  ? 0.2667 0.2339 0.2499 0.0001  0.0039  0.0134  825  ALA A CA  
6053  C C   . ALA A 827  ? 0.2837 0.2481 0.2673 0.0021  0.0041  0.0125  825  ALA A C   
6054  O O   . ALA A 827  ? 0.2615 0.2239 0.2459 0.0031  0.0034  0.0118  825  ALA A O   
6055  C CB  . ALA A 827  ? 0.3021 0.2708 0.2866 -0.0018 0.0027  0.0157  825  ALA A CB  
6056  N N   . GLU A 828  ? 0.2805 0.2451 0.2637 0.0028  0.0051  0.0124  826  GLU A N   
6057  C CA  . GLU A 828  ? 0.2876 0.2505 0.2714 0.0046  0.0055  0.0118  826  GLU A CA  
6058  C C   . GLU A 828  ? 0.2799 0.2422 0.2626 0.0063  0.0062  0.0102  826  GLU A C   
6059  O O   . GLU A 828  ? 0.2924 0.2536 0.2757 0.0078  0.0059  0.0094  826  GLU A O   
6060  C CB  . GLU A 828  ? 0.3184 0.2821 0.3022 0.0048  0.0065  0.0121  826  GLU A CB  
6061  C CG  . GLU A 828  ? 0.3672 0.3314 0.3522 0.0035  0.0058  0.0136  826  GLU A CG  
6062  C CD  . GLU A 828  ? 0.4684 0.4351 0.4528 0.0016  0.0055  0.0143  826  GLU A CD  
6063  O OE1 . GLU A 828  ? 0.4455 0.4136 0.4288 0.0012  0.0059  0.0136  826  GLU A OE1 
6064  O OE2 . GLU A 828  ? 0.5281 0.4960 0.5133 0.0004  0.0048  0.0157  826  GLU A OE2 
6065  N N   . GLN A 829  ? 0.2893 0.2527 0.2706 0.0063  0.0070  0.0097  827  GLN A N   
6066  C CA  . GLN A 829  ? 0.2964 0.2598 0.2768 0.0078  0.0076  0.0085  827  GLN A CA  
6067  C C   . GLN A 829  ? 0.2646 0.2271 0.2451 0.0079  0.0064  0.0077  827  GLN A C   
6068  O O   . GLN A 829  ? 0.2754 0.2376 0.2558 0.0095  0.0063  0.0065  827  GLN A O   
6069  C CB  . GLN A 829  ? 0.3166 0.2813 0.2961 0.0074  0.0084  0.0084  827  GLN A CB  
6070  C CG  . GLN A 829  ? 0.4568 0.4220 0.4356 0.0090  0.0093  0.0080  827  GLN A CG  
6071  C CD  . GLN A 829  ? 0.4747 0.4410 0.4537 0.0085  0.0099  0.0079  827  GLN A CD  
6072  O OE1 . GLN A 829  ? 0.4178 0.3848 0.3967 0.0075  0.0095  0.0074  827  GLN A OE1 
6073  N NE2 . GLN A 829  ? 0.5185 0.4852 0.4983 0.0093  0.0107  0.0085  827  GLN A NE2 
6074  N N   . VAL A 830  ? 0.2573 0.2200 0.2384 0.0062  0.0054  0.0082  828  VAL A N   
6075  C CA  . VAL A 830  ? 0.2680 0.2296 0.2500 0.0060  0.0039  0.0077  828  VAL A CA  
6076  C C   . VAL A 830  ? 0.2532 0.2130 0.2371 0.0070  0.0028  0.0071  828  VAL A C   
6077  O O   . VAL A 830  ? 0.2461 0.2052 0.2305 0.0084  0.0021  0.0054  828  VAL A O   
6078  C CB  . VAL A 830  ? 0.2448 0.2074 0.2277 0.0037  0.0030  0.0091  828  VAL A CB  
6079  C CG1 . VAL A 830  ? 0.2559 0.2170 0.2409 0.0033  0.0010  0.0090  828  VAL A CG1 
6080  C CG2 . VAL A 830  ? 0.2611 0.2259 0.2422 0.0031  0.0040  0.0089  828  VAL A CG2 
6081  N N   . VAL A 831  ? 0.2326 0.1918 0.2179 0.0064  0.0024  0.0084  829  VAL A N   
6082  C CA  . VAL A 831  ? 0.2375 0.1949 0.2254 0.0072  0.0010  0.0079  829  VAL A CA  
6083  C C   . VAL A 831  ? 0.2254 0.1830 0.2125 0.0098  0.0018  0.0057  829  VAL A C   
6084  O O   . VAL A 831  ? 0.2272 0.1840 0.2159 0.0111  0.0007  0.0038  829  VAL A O   
6085  C CB  . VAL A 831  ? 0.2511 0.2082 0.2407 0.0060  0.0004  0.0099  829  VAL A CB  
6086  C CG1 . VAL A 831  ? 0.2417 0.1971 0.2342 0.0073  -0.0009 0.0090  829  VAL A CG1 
6087  C CG2 . VAL A 831  ? 0.2750 0.2326 0.2657 0.0034  -0.0008 0.0122  829  VAL A CG2 
6088  N N   . GLY A 832  ? 0.2416 0.2008 0.2267 0.0105  0.0038  0.0059  830  GLY A N   
6089  C CA  . GLY A 832  ? 0.2429 0.2033 0.2272 0.0128  0.0047  0.0043  830  GLY A CA  
6090  C C   . GLY A 832  ? 0.2372 0.1984 0.2204 0.0140  0.0045  0.0024  830  GLY A C   
6091  O O   . GLY A 832  ? 0.2421 0.2040 0.2260 0.0158  0.0040  0.0003  830  GLY A O   
6092  N N   . ASP A 833  ? 0.2355 0.1969 0.2173 0.0130  0.0047  0.0029  831  ASP A N   
6093  C CA  . ASP A 833  ? 0.2321 0.1945 0.2129 0.0141  0.0045  0.0011  831  ASP A CA  
6094  C C   . ASP A 833  ? 0.2439 0.2046 0.2269 0.0141  0.0023  -0.0006 831  ASP A C   
6095  O O   . ASP A 833  ? 0.2371 0.1988 0.2200 0.0157  0.0018  -0.0029 831  ASP A O   
6096  C CB  . ASP A 833  ? 0.2431 0.2061 0.2222 0.0130  0.0052  0.0021  831  ASP A CB  
6097  C CG  . ASP A 833  ? 0.2401 0.2047 0.2176 0.0134  0.0070  0.0033  831  ASP A CG  
6098  O OD1 . ASP A 833  ? 0.2986 0.2644 0.2760 0.0147  0.0078  0.0033  831  ASP A OD1 
6099  O OD2 . ASP A 833  ? 0.2612 0.2262 0.2380 0.0124  0.0076  0.0042  831  ASP A OD2 
6100  N N   . VAL A 834  ? 0.2214 0.1801 0.2068 0.0123  0.0009  0.0006  832  VAL A N   
6101  C CA  . VAL A 834  ? 0.2220 0.1788 0.2106 0.0122  -0.0015 -0.0006 832  VAL A CA  
6102  C C   . VAL A 834  ? 0.2517 0.2080 0.2426 0.0141  -0.0025 -0.0028 832  VAL A C   
6103  O O   . VAL A 834  ? 0.2453 0.2014 0.2379 0.0156  -0.0039 -0.0056 832  VAL A O   
6104  C CB  . VAL A 834  ? 0.2277 0.1829 0.2185 0.0095  -0.0028 0.0021  832  VAL A CB  
6105  C CG1 . VAL A 834  ? 0.2461 0.1991 0.2414 0.0092  -0.0056 0.0014  832  VAL A CG1 
6106  C CG2 . VAL A 834  ? 0.2498 0.2063 0.2387 0.0078  -0.0020 0.0035  832  VAL A CG2 
6107  N N   . ILE A 835  ? 0.2335 0.1897 0.2248 0.0143  -0.0018 -0.0018 833  ILE A N   
6108  C CA  . ILE A 835  ? 0.2493 0.2054 0.2430 0.0163  -0.0027 -0.0040 833  ILE A CA  
6109  C C   . ILE A 835  ? 0.2496 0.2087 0.2414 0.0190  -0.0017 -0.0071 833  ILE A C   
6110  O O   . ILE A 835  ? 0.2872 0.2466 0.2813 0.0208  -0.0032 -0.0104 833  ILE A O   
6111  C CB  . ILE A 835  ? 0.2645 0.2207 0.2585 0.0161  -0.0018 -0.0022 833  ILE A CB  
6112  C CG1 . ILE A 835  ? 0.2922 0.2459 0.2889 0.0137  -0.0032 0.0006  833  ILE A CG1 
6113  C CG2 . ILE A 835  ? 0.2936 0.2509 0.2894 0.0186  -0.0020 -0.0048 833  ILE A CG2 
6114  C CD1 . ILE A 835  ? 0.3197 0.2709 0.3216 0.0138  -0.0061 -0.0004 833  ILE A CD1 
6115  N N   . THR A 836  ? 0.2547 0.2164 0.2425 0.0193  0.0006  -0.0061 834  THR A N   
6116  C CA  . THR A 836  ? 0.2696 0.2350 0.2554 0.0216  0.0015  -0.0084 834  THR A CA  
6117  C C   . THR A 836  ? 0.2587 0.2241 0.2447 0.0221  0.0001  -0.0108 834  THR A C   
6118  O O   . THR A 836  ? 0.2861 0.2533 0.2730 0.0242  -0.0008 -0.0143 834  THR A O   
6119  C CB  . THR A 836  ? 0.3205 0.2884 0.3027 0.0213  0.0040  -0.0061 834  THR A CB  
6120  O OG1 . THR A 836  ? 0.3881 0.3563 0.3705 0.0212  0.0052  -0.0043 834  THR A OG1 
6121  C CG2 . THR A 836  ? 0.3798 0.3520 0.3596 0.0234  0.0050  -0.0077 834  THR A CG2 
6122  N N   . SER A 837  ? 0.2570 0.2207 0.2424 0.0201  -0.0002 -0.0093 835  SER A N   
6123  C CA  . SER A 837  ? 0.2366 0.2007 0.2219 0.0206  -0.0013 -0.0114 835  SER A CA  
6124  C C   . SER A 837  ? 0.2321 0.1940 0.2218 0.0210  -0.0042 -0.0141 835  SER A C   
6125  O O   . SER A 837  ? 0.2426 0.2059 0.2328 0.0225  -0.0053 -0.0173 835  SER A O   
6126  C CB  . SER A 837  ? 0.2499 0.2128 0.2339 0.0183  -0.0010 -0.0090 835  SER A CB  
6127  O OG  . SER A 837  ? 0.2402 0.2050 0.2208 0.0181  0.0013  -0.0069 835  SER A OG  
6128  N N   . ALA A 838  ? 0.2263 0.1850 0.2195 0.0196  -0.0056 -0.0128 836  ALA A N   
6129  C CA  . ALA A 838  ? 0.2268 0.1830 0.2252 0.0197  -0.0087 -0.0149 836  ALA A CA  
6130  C C   . ALA A 838  ? 0.2510 0.2079 0.2521 0.0223  -0.0098 -0.0184 836  ALA A C   
6131  O O   . ALA A 838  ? 0.2522 0.2085 0.2571 0.0235  -0.0122 -0.0220 836  ALA A O   
6132  C CB  . ALA A 838  ? 0.2559 0.2085 0.2576 0.0169  -0.0101 -0.0115 836  ALA A CB  
6133  N N   . PHE A 839  ? 0.2371 0.1954 0.2370 0.0231  -0.0082 -0.0178 837  PHE A N   
6134  C CA  . PHE A 839  ? 0.2627 0.2213 0.2661 0.0252  -0.0094 -0.0207 837  PHE A CA  
6135  C C   . PHE A 839  ? 0.2619 0.2257 0.2624 0.0281  -0.0074 -0.0233 837  PHE A C   
6136  O O   . PHE A 839  ? 0.2730 0.2381 0.2766 0.0304  -0.0086 -0.0269 837  PHE A O   
6137  C CB  . PHE A 839  ? 0.2676 0.2232 0.2738 0.0238  -0.0099 -0.0178 837  PHE A CB  
6138  C CG  . PHE A 839  ? 0.2497 0.2012 0.2592 0.0209  -0.0120 -0.0150 837  PHE A CG  
6139  C CD1 . PHE A 839  ? 0.2829 0.2321 0.2973 0.0209  -0.0151 -0.0170 837  PHE A CD1 
6140  C CD2 . PHE A 839  ? 0.2863 0.2367 0.2941 0.0182  -0.0108 -0.0103 837  PHE A CD2 
6141  C CE1 . PHE A 839  ? 0.2716 0.2175 0.2893 0.0181  -0.0171 -0.0139 837  PHE A CE1 
6142  C CE2 . PHE A 839  ? 0.3406 0.2882 0.3512 0.0156  -0.0127 -0.0075 837  PHE A CE2 
6143  C CZ  . PHE A 839  ? 0.3059 0.2513 0.3216 0.0154  -0.0158 -0.0090 837  PHE A CZ  
6144  N N   . ASP A 840  ? 0.2799 0.2470 0.2752 0.0280  -0.0046 -0.0214 838  ASP A N   
6145  C CA  . ASP A 840  ? 0.3000 0.2729 0.2924 0.0307  -0.0029 -0.0236 838  ASP A CA  
6146  C C   . ASP A 840  ? 0.2815 0.2569 0.2756 0.0331  -0.0047 -0.0289 838  ASP A C   
6147  O O   . ASP A 840  ? 0.2805 0.2541 0.2755 0.0325  -0.0063 -0.0300 838  ASP A O   
6148  C CB  . ASP A 840  ? 0.3475 0.3230 0.3347 0.0299  -0.0003 -0.0206 838  ASP A CB  
6149  C CG  . ASP A 840  ? 0.4186 0.4008 0.4029 0.0322  0.0017  -0.0217 838  ASP A CG  
6150  O OD1 . ASP A 840  ? 0.4338 0.4198 0.4169 0.0340  0.0013  -0.0248 838  ASP A OD1 
6151  O OD2 . ASP A 840  ? 0.5034 0.4874 0.4866 0.0322  0.0035  -0.0194 838  ASP A OD2 
6152  N N   . SER A 841  ? 0.2739 0.2536 0.2687 0.0359  -0.0046 -0.0324 839  SER A N   
6153  C CA  . SER A 841  ? 0.2633 0.2464 0.2599 0.0386  -0.0064 -0.0382 839  SER A CA  
6154  C C   . SER A 841  ? 0.2535 0.2311 0.2563 0.0382  -0.0101 -0.0408 839  SER A C   
6155  O O   . SER A 841  ? 0.2471 0.2256 0.2516 0.0395  -0.0120 -0.0449 839  SER A O   
6156  C CB  . SER A 841  ? 0.3062 0.2937 0.2983 0.0392  -0.0053 -0.0388 839  SER A CB  
6157  O OG  . SER A 841  ? 0.3684 0.3608 0.3555 0.0393  -0.0021 -0.0357 839  SER A OG  
6158  N N   . ALA A 842  ? 0.2611 0.2332 0.2675 0.0363  -0.0111 -0.0381 840  ALA A N   
6159  C CA  . ALA A 842  ? 0.2246 0.1910 0.2374 0.0353  -0.0148 -0.0392 840  ALA A CA  
6160  C C   . ALA A 842  ? 0.2390 0.2033 0.2515 0.0338  -0.0160 -0.0387 840  ALA A C   
6161  O O   . ALA A 842  ? 0.2634 0.2255 0.2810 0.0341  -0.0191 -0.0418 840  ALA A O   
6162  C CB  . ALA A 842  ? 0.2703 0.2377 0.2890 0.0383  -0.0175 -0.0452 840  ALA A CB  
6163  N N   . GLY A 843  ? 0.2315 0.1963 0.2385 0.0319  -0.0135 -0.0348 841  GLY A N   
6164  C CA  . GLY A 843  ? 0.2316 0.1949 0.2381 0.0303  -0.0144 -0.0340 841  GLY A CA  
6165  C C   . GLY A 843  ? 0.2346 0.2015 0.2403 0.0326  -0.0151 -0.0388 841  GLY A C   
6166  O O   . GLY A 843  ? 0.2454 0.2109 0.2518 0.0316  -0.0165 -0.0390 841  GLY A O   
6167  N N   . GLN A 844  ? 0.2327 0.2051 0.2370 0.0357  -0.0143 -0.0426 842  GLN A N   
6168  C CA  . GLN A 844  ? 0.2098 0.1868 0.2134 0.0382  -0.0152 -0.0477 842  GLN A CA  
6169  C C   . GLN A 844  ? 0.2626 0.2448 0.2590 0.0384  -0.0121 -0.0458 842  GLN A C   
6170  O O   . GLN A 844  ? 0.2644 0.2534 0.2579 0.0409  -0.0109 -0.0484 842  GLN A O   
6171  C CB  . GLN A 844  ? 0.2382 0.2189 0.2449 0.0416  -0.0164 -0.0534 842  GLN A CB  
6172  C CG  . GLN A 844  ? 0.2535 0.2285 0.2684 0.0414  -0.0201 -0.0556 842  GLN A CG  
6173  C CD  . GLN A 844  ? 0.2519 0.2300 0.2705 0.0447  -0.0212 -0.0608 842  GLN A CD  
6174  O OE1 . GLN A 844  ? 0.2535 0.2314 0.2777 0.0466  -0.0245 -0.0665 842  GLN A OE1 
6175  N NE2 . GLN A 844  ? 0.2694 0.2503 0.2853 0.0453  -0.0186 -0.0590 842  GLN A NE2 
6176  N N   . ARG A 845  ? 0.2435 0.2228 0.2374 0.0356  -0.0109 -0.0409 843  ARG A N   
6177  C CA  . ARG A 845  ? 0.2550 0.2379 0.2433 0.0353  -0.0087 -0.0389 843  ARG A CA  
6178  C C   . ARG A 845  ? 0.2484 0.2280 0.2378 0.0336  -0.0103 -0.0385 843  ARG A C   
6179  O O   . ARG A 845  ? 0.2668 0.2407 0.2597 0.0314  -0.0118 -0.0368 843  ARG A O   
6180  C CB  . ARG A 845  ? 0.2875 0.2699 0.2722 0.0335  -0.0058 -0.0332 843  ARG A CB  
6181  C CG  . ARG A 845  ? 0.2747 0.2605 0.2580 0.0348  -0.0038 -0.0326 843  ARG A CG  
6182  C CD  . ARG A 845  ? 0.3672 0.3518 0.3477 0.0327  -0.0013 -0.0270 843  ARG A CD  
6183  N NE  . ARG A 845  ? 0.3960 0.3840 0.3753 0.0338  0.0006  -0.0260 843  ARG A NE  
6184  C CZ  . ARG A 845  ? 0.4360 0.4301 0.4118 0.0350  0.0027  -0.0249 843  ARG A CZ  
6185  N NH1 . ARG A 845  ? 0.4404 0.4378 0.4132 0.0353  0.0032  -0.0247 843  ARG A NH1 
6186  N NH2 . ARG A 845  ? 0.4802 0.4773 0.4555 0.0358  0.0043  -0.0238 843  ARG A NH2 
6187  N N   . CYS A 846  ? 0.2456 0.2291 0.2321 0.0346  -0.0101 -0.0401 844  CYS A N   
6188  C CA  . CYS A 846  ? 0.2598 0.2405 0.2473 0.0329  -0.0115 -0.0396 844  CYS A CA  
6189  C C   . CYS A 846  ? 0.2263 0.2033 0.2121 0.0298  -0.0100 -0.0339 844  CYS A C   
6190  O O   . CYS A 846  ? 0.2206 0.1937 0.2087 0.0277  -0.0114 -0.0327 844  CYS A O   
6191  C CB  . CYS A 846  ? 0.2404 0.2266 0.2246 0.0346  -0.0113 -0.0419 844  CYS A CB  
6192  S SG  . CYS A 846  ? 0.3014 0.2940 0.2787 0.0354  -0.0076 -0.0387 844  CYS A SG  
6193  N N   . SER A 847  ? 0.2296 0.2081 0.2118 0.0295  -0.0072 -0.0305 845  SER A N   
6194  C CA  . SER A 847  ? 0.2048 0.1807 0.1854 0.0269  -0.0056 -0.0255 845  SER A CA  
6195  C C   . SER A 847  ? 0.2359 0.2071 0.2195 0.0250  -0.0060 -0.0233 845  SER A C   
6196  O O   . SER A 847  ? 0.2347 0.2039 0.2172 0.0228  -0.0048 -0.0194 845  SER A O   
6197  C CB  . SER A 847  ? 0.2290 0.2088 0.2053 0.0276  -0.0027 -0.0230 845  SER A CB  
6198  O OG  . SER A 847  ? 0.2592 0.2411 0.2359 0.0293  -0.0022 -0.0243 845  SER A OG  
6199  N N   . ALA A 848  ? 0.2341 0.2037 0.2215 0.0258  -0.0078 -0.0257 846  ALA A N   
6200  C CA  . ALA A 848  ? 0.2051 0.1710 0.1952 0.0243  -0.0080 -0.0233 846  ALA A CA  
6201  C C   . ALA A 848  ? 0.2178 0.1797 0.2097 0.0212  -0.0090 -0.0203 846  ALA A C   
6202  O O   . ALA A 848  ? 0.2234 0.1843 0.2170 0.0204  -0.0106 -0.0211 846  ALA A O   
6203  C CB  . ALA A 848  ? 0.2327 0.1975 0.2276 0.0258  -0.0103 -0.0268 846  ALA A CB  
6204  N N   . LEU A 849  ? 0.2268 0.1869 0.2187 0.0194  -0.0080 -0.0167 847  LEU A N   
6205  C CA  . LEU A 849  ? 0.2291 0.1864 0.2226 0.0164  -0.0087 -0.0135 847  LEU A CA  
6206  C C   . LEU A 849  ? 0.2191 0.1733 0.2186 0.0157  -0.0119 -0.0143 847  LEU A C   
6207  O O   . LEU A 849  ? 0.2401 0.1930 0.2426 0.0164  -0.0129 -0.0151 847  LEU A O   
6208  C CB  . LEU A 849  ? 0.2398 0.1967 0.2317 0.0150  -0.0069 -0.0099 847  LEU A CB  
6209  C CG  . LEU A 849  ? 0.2302 0.1853 0.2238 0.0119  -0.0075 -0.0065 847  LEU A CG  
6210  C CD1 . LEU A 849  ? 0.2325 0.1888 0.2243 0.0108  -0.0071 -0.0058 847  LEU A CD1 
6211  C CD2 . LEU A 849  ? 0.2317 0.1870 0.2238 0.0109  -0.0058 -0.0036 847  LEU A CD2 
6212  N N   . ARG A 850  ? 0.2249 0.1779 0.2265 0.0143  -0.0136 -0.0141 848  ARG A N   
6213  C CA  . ARG A 850  ? 0.2399 0.1899 0.2480 0.0133  -0.0170 -0.0145 848  ARG A CA  
6214  C C   . ARG A 850  ? 0.2539 0.2023 0.2641 0.0099  -0.0176 -0.0098 848  ARG A C   
6215  O O   . ARG A 850  ? 0.2484 0.1942 0.2641 0.0087  -0.0201 -0.0087 848  ARG A O   
6216  C CB  . ARG A 850  ? 0.2529 0.2031 0.2631 0.0141  -0.0191 -0.0178 848  ARG A CB  
6217  C CG  . ARG A 850  ? 0.2567 0.2095 0.2646 0.0175  -0.0186 -0.0227 848  ARG A CG  
6218  C CD  . ARG A 850  ? 0.2544 0.2073 0.2643 0.0197  -0.0191 -0.0253 848  ARG A CD  
6219  N NE  . ARG A 850  ? 0.2604 0.2169 0.2684 0.0230  -0.0188 -0.0302 848  ARG A NE  
6220  C CZ  . ARG A 850  ? 0.2570 0.2152 0.2656 0.0255  -0.0188 -0.0333 848  ARG A CZ  
6221  N NH1 . ARG A 850  ? 0.2534 0.2095 0.2645 0.0253  -0.0191 -0.0321 848  ARG A NH1 
6222  N NH2 . ARG A 850  ? 0.2692 0.2318 0.2757 0.0285  -0.0185 -0.0377 848  ARG A NH2 
6223  N N   . VAL A 851  ? 0.2356 0.1857 0.2419 0.0082  -0.0156 -0.0071 849  VAL A N   
6224  C CA  . VAL A 851  ? 0.2656 0.2155 0.2735 0.0050  -0.0160 -0.0028 849  VAL A CA  
6225  C C   . VAL A 851  ? 0.2440 0.1962 0.2469 0.0041  -0.0129 -0.0002 849  VAL A C   
6226  O O   . VAL A 851  ? 0.2570 0.2113 0.2557 0.0046  -0.0109 -0.0007 849  VAL A O   
6227  C CB  . VAL A 851  ? 0.3133 0.2637 0.3226 0.0036  -0.0172 -0.0025 849  VAL A CB  
6228  C CG1 . VAL A 851  ? 0.3299 0.2808 0.3414 0.0001  -0.0178 0.0022  849  VAL A CG1 
6229  C CG2 . VAL A 851  ? 0.3621 0.3105 0.3764 0.0047  -0.0203 -0.0059 849  VAL A CG2 
6230  N N   . LEU A 852  ? 0.2303 0.1821 0.2340 0.0029  -0.0128 0.0025  850  LEU A N   
6231  C CA  . LEU A 852  ? 0.2330 0.1871 0.2329 0.0019  -0.0103 0.0049  850  LEU A CA  
6232  C C   . LEU A 852  ? 0.2253 0.1811 0.2265 -0.0012 -0.0108 0.0085  850  LEU A C   
6233  O O   . LEU A 852  ? 0.2341 0.1889 0.2397 -0.0030 -0.0130 0.0108  850  LEU A O   
6234  C CB  . LEU A 852  ? 0.2382 0.1914 0.2385 0.0023  -0.0099 0.0058  850  LEU A CB  
6235  C CG  . LEU A 852  ? 0.2373 0.1927 0.2343 0.0012  -0.0077 0.0082  850  LEU A CG  
6236  C CD1 . LEU A 852  ? 0.2460 0.2032 0.2383 0.0027  -0.0051 0.0065  850  LEU A CD1 
6237  C CD2 . LEU A 852  ? 0.2559 0.2101 0.2542 0.0015  -0.0079 0.0090  850  LEU A CD2 
6238  N N   . CYS A 853  ? 0.2263 0.1850 0.2239 -0.0019 -0.0088 0.0091  851  CYS A N   
6239  C CA  . CYS A 853  ? 0.2366 0.1982 0.2350 -0.0046 -0.0090 0.0121  851  CYS A CA  
6240  C C   . CYS A 853  ? 0.2194 0.1839 0.2147 -0.0055 -0.0069 0.0138  851  CYS A C   
6241  O O   . CYS A 853  ? 0.2315 0.1972 0.2231 -0.0041 -0.0048 0.0122  851  CYS A O   
6242  C CB  . CYS A 853  ? 0.2531 0.2162 0.2503 -0.0046 -0.0087 0.0108  851  CYS A CB  
6243  S SG  . CYS A 853  ? 0.2720 0.2320 0.2719 -0.0030 -0.0108 0.0077  851  CYS A SG  
6244  N N   . LEU A 854  ? 0.2285 0.1944 0.2258 -0.0076 -0.0078 0.0171  852  LEU A N   
6245  C CA  . LEU A 854  ? 0.2356 0.2044 0.2305 -0.0083 -0.0062 0.0186  852  LEU A CA  
6246  C C   . LEU A 854  ? 0.2339 0.2079 0.2286 -0.0109 -0.0059 0.0212  852  LEU A C   
6247  O O   . LEU A 854  ? 0.2409 0.2160 0.2390 -0.0131 -0.0078 0.0241  852  LEU A O   
6248  C CB  . LEU A 854  ? 0.2349 0.2020 0.2321 -0.0087 -0.0073 0.0204  852  LEU A CB  
6249  C CG  . LEU A 854  ? 0.2471 0.2097 0.2447 -0.0061 -0.0075 0.0178  852  LEU A CG  
6250  C CD1 . LEU A 854  ? 0.2373 0.1985 0.2377 -0.0067 -0.0089 0.0198  852  LEU A CD1 
6251  C CD2 . LEU A 854  ? 0.2583 0.2213 0.2516 -0.0040 -0.0050 0.0151  852  LEU A CD2 
6252  N N   . GLN A 855  ? 0.2309 0.2084 0.2221 -0.0106 -0.0037 0.0202  853  GLN A N   
6253  C CA  . GLN A 855  ? 0.2288 0.2124 0.2197 -0.0129 -0.0033 0.0224  853  GLN A CA  
6254  C C   . GLN A 855  ? 0.2529 0.2387 0.2457 -0.0151 -0.0044 0.0261  853  GLN A C   
6255  O O   . GLN A 855  ? 0.2477 0.2318 0.2402 -0.0144 -0.0043 0.0263  853  GLN A O   
6256  C CB  . GLN A 855  ? 0.2370 0.2239 0.2243 -0.0119 -0.0010 0.0201  853  GLN A CB  
6257  C CG  . GLN A 855  ? 0.2570 0.2508 0.2440 -0.0139 -0.0005 0.0214  853  GLN A CG  
6258  C CD  . GLN A 855  ? 0.2782 0.2756 0.2623 -0.0129 0.0015  0.0189  853  GLN A CD  
6259  O OE1 . GLN A 855  ? 0.3054 0.3001 0.2880 -0.0107 0.0026  0.0158  853  GLN A OE1 
6260  N NE2 . GLN A 855  ? 0.3317 0.3358 0.3153 -0.0145 0.0020  0.0201  853  GLN A NE2 
6261  N N   . GLU A 856  ? 0.2569 0.2470 0.2518 -0.0177 -0.0055 0.0295  854  GLU A N   
6262  C CA  . GLU A 856  ? 0.2863 0.2783 0.2840 -0.0200 -0.0072 0.0339  854  GLU A CA  
6263  C C   . GLU A 856  ? 0.2865 0.2814 0.2820 -0.0201 -0.0060 0.0344  854  GLU A C   
6264  O O   . GLU A 856  ? 0.3055 0.2984 0.3028 -0.0205 -0.0073 0.0365  854  GLU A O   
6265  C CB  . GLU A 856  ? 0.3039 0.3017 0.3037 -0.0230 -0.0081 0.0376  854  GLU A CB  
6266  C CG  . GLU A 856  ? 0.3498 0.3511 0.3526 -0.0258 -0.0098 0.0430  854  GLU A CG  
6267  C CD  . GLU A 856  ? 0.4637 0.4585 0.4713 -0.0259 -0.0125 0.0447  854  GLU A CD  
6268  O OE1 . GLU A 856  ? 0.4068 0.3961 0.4169 -0.0248 -0.0138 0.0430  854  GLU A OE1 
6269  O OE2 . GLU A 856  ? 0.4705 0.4660 0.4795 -0.0269 -0.0135 0.0477  854  GLU A OE2 
6270  N N   . ASP A 857  ? 0.2858 0.2850 0.2774 -0.0194 -0.0038 0.0322  855  ASP A N   
6271  C CA  . ASP A 857  ? 0.3102 0.3132 0.2998 -0.0196 -0.0028 0.0324  855  ASP A CA  
6272  C C   . ASP A 857  ? 0.3195 0.3168 0.3086 -0.0176 -0.0027 0.0307  855  ASP A C   
6273  O O   . ASP A 857  ? 0.3692 0.3685 0.3579 -0.0181 -0.0026 0.0320  855  ASP A O   
6274  C CB  . ASP A 857  ? 0.3910 0.3994 0.3772 -0.0190 -0.0007 0.0295  855  ASP A CB  
6275  N N   . VAL A 858  ? 0.2735 0.2643 0.2627 -0.0154 -0.0025 0.0280  856  VAL A N   
6276  C CA  . VAL A 858  ? 0.2767 0.2627 0.2655 -0.0134 -0.0022 0.0264  856  VAL A CA  
6277  C C   . VAL A 858  ? 0.2530 0.2334 0.2451 -0.0129 -0.0041 0.0272  856  VAL A C   
6278  O O   . VAL A 858  ? 0.2702 0.2468 0.2623 -0.0112 -0.0040 0.0260  856  VAL A O   
6279  C CB  . VAL A 858  ? 0.2868 0.2710 0.2728 -0.0109 -0.0003 0.0223  856  VAL A CB  
6280  C CG1 . VAL A 858  ? 0.3076 0.2972 0.2912 -0.0111 0.0013  0.0211  856  VAL A CG1 
6281  C CG2 . VAL A 858  ? 0.2744 0.2561 0.2605 -0.0099 -0.0003 0.0205  856  VAL A CG2 
6282  N N   . ALA A 859  ? 0.2570 0.2369 0.2522 -0.0143 -0.0060 0.0292  857  ALA A N   
6283  C CA  . ALA A 859  ? 0.2458 0.2200 0.2446 -0.0135 -0.0080 0.0290  857  ALA A CA  
6284  C C   . ALA A 859  ? 0.2698 0.2421 0.2712 -0.0136 -0.0094 0.0309  857  ALA A C   
6285  O O   . ALA A 859  ? 0.2661 0.2336 0.2686 -0.0116 -0.0099 0.0289  857  ALA A O   
6286  C CB  . ALA A 859  ? 0.2654 0.2398 0.2678 -0.0152 -0.0100 0.0310  857  ALA A CB  
6287  N N   . ASP A 860  ? 0.2798 0.2560 0.2820 -0.0160 -0.0100 0.0348  858  ASP A N   
6288  C CA  . ASP A 860  ? 0.2686 0.2430 0.2737 -0.0163 -0.0116 0.0369  858  ASP A CA  
6289  C C   . ASP A 860  ? 0.2722 0.2448 0.2747 -0.0140 -0.0099 0.0342  858  ASP A C   
6290  O O   . ASP A 860  ? 0.2891 0.2574 0.2938 -0.0127 -0.0109 0.0335  858  ASP A O   
6291  C CB  . ASP A 860  ? 0.2923 0.2724 0.2987 -0.0194 -0.0125 0.0419  858  ASP A CB  
6292  C CG  . ASP A 860  ? 0.3894 0.3705 0.4002 -0.0218 -0.0150 0.0457  858  ASP A CG  
6293  O OD1 . ASP A 860  ? 0.4562 0.4320 0.4712 -0.0211 -0.0169 0.0451  858  ASP A OD1 
6294  O OD2 . ASP A 860  ? 0.5929 0.5804 0.6034 -0.0244 -0.0150 0.0493  858  ASP A OD2 
6295  N N   . ARG A 861  ? 0.2680 0.2439 0.2659 -0.0136 -0.0075 0.0325  859  ARG A N   
6296  C CA  . ARG A 861  ? 0.2842 0.2586 0.2800 -0.0116 -0.0060 0.0302  859  ARG A CA  
6297  C C   . ARG A 861  ? 0.2422 0.2113 0.2379 -0.0088 -0.0055 0.0266  859  ARG A C   
6298  O O   . ARG A 861  ? 0.2773 0.2436 0.2739 -0.0074 -0.0056 0.0257  859  ARG A O   
6299  C CB  . ARG A 861  ? 0.3725 0.3514 0.3642 -0.0116 -0.0037 0.0288  859  ARG A CB  
6300  C CG  . ARG A 861  ? 0.4576 0.4347 0.4475 -0.0096 -0.0022 0.0262  859  ARG A CG  
6301  C CD  . ARG A 861  ? 0.5830 0.5647 0.5701 -0.0098 -0.0006 0.0252  859  ARG A CD  
6302  N NE  . ARG A 861  ? 0.7199 0.6997 0.7062 -0.0081 0.0005  0.0233  859  ARG A NE  
6303  C CZ  . ARG A 861  ? 0.6423 0.6202 0.6271 -0.0062 0.0020  0.0204  859  ARG A CZ  
6304  N NH1 . ARG A 861  ? 0.6743 0.6522 0.6581 -0.0057 0.0027  0.0188  859  ARG A NH1 
6305  N NH2 . ARG A 861  ? 0.5712 0.5475 0.5560 -0.0049 0.0027  0.0193  859  ARG A NH2 
6306  N N   . ILE A 862  ? 0.2401 0.2085 0.2349 -0.0081 -0.0050 0.0247  860  ILE A N   
6307  C CA  . ILE A 862  ? 0.2566 0.2210 0.2510 -0.0055 -0.0045 0.0214  860  ILE A CA  
6308  C C   . ILE A 862  ? 0.2551 0.2156 0.2537 -0.0049 -0.0068 0.0215  860  ILE A C   
6309  O O   . ILE A 862  ? 0.2365 0.1944 0.2355 -0.0028 -0.0066 0.0193  860  ILE A O   
6310  C CB  . ILE A 862  ? 0.2330 0.1980 0.2254 -0.0050 -0.0036 0.0194  860  ILE A CB  
6311  C CG1 . ILE A 862  ? 0.2650 0.2332 0.2538 -0.0049 -0.0013 0.0185  860  ILE A CG1 
6312  C CG2 . ILE A 862  ? 0.2819 0.2432 0.2745 -0.0025 -0.0037 0.0164  860  ILE A CG2 
6313  C CD1 . ILE A 862  ? 0.2918 0.2611 0.2789 -0.0045 -0.0004 0.0168  860  ILE A CD1 
6314  N N   . LEU A 863  ? 0.2415 0.2019 0.2437 -0.0068 -0.0091 0.0239  861  LEU A N   
6315  C CA  A LEU A 863  ? 0.2448 0.2015 0.2521 -0.0063 -0.0117 0.0239  861  LEU A CA  
6316  C CA  B LEU A 863  ? 0.2448 0.2014 0.2521 -0.0063 -0.0117 0.0239  861  LEU A CA  
6317  C C   . LEU A 863  ? 0.2340 0.1894 0.2431 -0.0058 -0.0123 0.0248  861  LEU A C   
6318  O O   . LEU A 863  ? 0.2342 0.1862 0.2457 -0.0038 -0.0133 0.0226  861  LEU A O   
6319  C CB  A LEU A 863  ? 0.2666 0.2237 0.2782 -0.0088 -0.0143 0.0271  861  LEU A CB  
6320  C CB  B LEU A 863  ? 0.2668 0.2241 0.2782 -0.0089 -0.0142 0.0272  861  LEU A CB  
6321  C CG  A LEU A 863  ? 0.2963 0.2526 0.3087 -0.0087 -0.0149 0.0256  861  LEU A CG  
6322  C CG  B LEU A 863  ? 0.2966 0.2498 0.3143 -0.0086 -0.0174 0.0271  861  LEU A CG  
6323  C CD1 A LEU A 863  ? 0.2828 0.2403 0.2997 -0.0117 -0.0174 0.0297  861  LEU A CD1 
6324  C CD1 B LEU A 863  ? 0.2837 0.2339 0.3009 -0.0056 -0.0171 0.0220  861  LEU A CD1 
6325  C CD2 A LEU A 863  ? 0.3168 0.2687 0.3314 -0.0060 -0.0160 0.0217  861  LEU A CD2 
6326  C CD2 B LEU A 863  ? 0.3239 0.2785 0.3454 -0.0114 -0.0196 0.0307  861  LEU A CD2 
6327  N N   . THR A 864  ? 0.2457 0.2041 0.2538 -0.0075 -0.0119 0.0278  862  THR A N   
6328  C CA  . THR A 864  ? 0.2583 0.2158 0.2679 -0.0071 -0.0124 0.0286  862  THR A CA  
6329  C C   . THR A 864  ? 0.2297 0.1856 0.2366 -0.0042 -0.0103 0.0249  862  THR A C   
6330  O O   . THR A 864  ? 0.2232 0.1764 0.2326 -0.0026 -0.0112 0.0237  862  THR A O   
6331  C CB  . THR A 864  ? 0.2603 0.2221 0.2683 -0.0093 -0.0119 0.0321  862  THR A CB  
6332  O OG1 . THR A 864  ? 0.2913 0.2549 0.3026 -0.0121 -0.0140 0.0362  862  THR A OG1 
6333  C CG2 . THR A 864  ? 0.2784 0.2395 0.2875 -0.0087 -0.0121 0.0327  862  THR A CG2 
6334  N N   . MET A 865  ? 0.2201 0.1779 0.2222 -0.0036 -0.0077 0.0231  863  MET A N   
6335  C CA  . MET A 865  ? 0.2402 0.1970 0.2401 -0.0011 -0.0059 0.0202  863  MET A CA  
6336  C C   . MET A 865  ? 0.2199 0.1738 0.2212 0.0012  -0.0064 0.0171  863  MET A C   
6337  O O   . MET A 865  ? 0.2146 0.1673 0.2165 0.0032  -0.0061 0.0154  863  MET A O   
6338  C CB  . MET A 865  ? 0.2413 0.2007 0.2366 -0.0010 -0.0034 0.0192  863  MET A CB  
6339  C CG  . MET A 865  ? 0.2738 0.2327 0.2671 0.0012  -0.0014 0.0170  863  MET A CG  
6340  S SD  . MET A 865  ? 0.3164 0.2780 0.3056 0.0011  0.0010  0.0161  863  MET A SD  
6341  C CE  . MET A 865  ? 0.3522 0.3173 0.3414 -0.0017 0.0004  0.0188  863  MET A CE  
6342  N N   . LEU A 866  ? 0.2224 0.1757 0.2244 0.0010  -0.0073 0.0164  864  LEU A N   
6343  C CA  . LEU A 866  ? 0.2173 0.1684 0.2206 0.0032  -0.0080 0.0132  864  LEU A CA  
6344  C C   . LEU A 866  ? 0.2078 0.1563 0.2162 0.0040  -0.0104 0.0127  864  LEU A C   
6345  O O   . LEU A 866  ? 0.2294 0.1769 0.2385 0.0066  -0.0102 0.0096  864  LEU A O   
6346  C CB  . LEU A 866  ? 0.2369 0.1879 0.2406 0.0024  -0.0088 0.0128  864  LEU A CB  
6347  C CG  . LEU A 866  ? 0.2501 0.1993 0.2555 0.0046  -0.0099 0.0093  864  LEU A CG  
6348  C CD1 . LEU A 866  ? 0.2737 0.2240 0.2752 0.0071  -0.0075 0.0063  864  LEU A CD1 
6349  C CD2 . LEU A 866  ? 0.2910 0.2402 0.2969 0.0035  -0.0108 0.0093  864  LEU A CD2 
6350  N N   . LYS A 867  ? 0.2266 0.1743 0.2391 0.0020  -0.0127 0.0158  865  LYS A N   
6351  C CA  . LYS A 867  ? 0.2405 0.1855 0.2587 0.0027  -0.0153 0.0155  865  LYS A CA  
6352  C C   . LYS A 867  ? 0.2316 0.1769 0.2492 0.0041  -0.0142 0.0150  865  LYS A C   
6353  O O   . LYS A 867  ? 0.2330 0.1765 0.2536 0.0063  -0.0152 0.0124  865  LYS A O   
6354  C CB  . LYS A 867  ? 0.2729 0.2174 0.2958 -0.0002 -0.0181 0.0198  865  LYS A CB  
6355  C CG  . LYS A 867  ? 0.2799 0.2236 0.3050 -0.0014 -0.0198 0.0202  865  LYS A CG  
6356  C CD  . LYS A 867  ? 0.2896 0.2341 0.3187 -0.0047 -0.0221 0.0254  865  LYS A CD  
6357  C CE  . LYS A 867  ? 0.3575 0.3017 0.3889 -0.0061 -0.0237 0.0259  865  LYS A CE  
6358  N NZ  . LYS A 867  ? 0.4219 0.3679 0.4567 -0.0096 -0.0257 0.0317  865  LYS A NZ  
6359  N N   . GLY A 868  ? 0.2348 0.1824 0.2486 0.0030  -0.0122 0.0171  866  GLY A N   
6360  C CA  . GLY A 868  ? 0.2356 0.1836 0.2488 0.0043  -0.0111 0.0166  866  GLY A CA  
6361  C C   . GLY A 868  ? 0.2225 0.1707 0.2335 0.0073  -0.0092 0.0126  866  GLY A C   
6362  O O   . GLY A 868  ? 0.2424 0.1901 0.2552 0.0092  -0.0094 0.0109  866  GLY A O   
6363  N N   . ALA A 869  ? 0.2139 0.1633 0.2209 0.0077  -0.0075 0.0112  867  ALA A N   
6364  C CA  . ALA A 869  ? 0.2093 0.1597 0.2141 0.0103  -0.0057 0.0079  867  ALA A CA  
6365  C C   . ALA A 869  ? 0.2377 0.1867 0.2458 0.0125  -0.0075 0.0045  867  ALA A C   
6366  O O   . ALA A 869  ? 0.2376 0.1878 0.2458 0.0149  -0.0067 0.0019  867  ALA A O   
6367  C CB  . ALA A 869  ? 0.2199 0.1720 0.2203 0.0101  -0.0038 0.0075  867  ALA A CB  
6368  N N   . LEU A 870  ? 0.2240 0.1711 0.2354 0.0116  -0.0099 0.0045  868  LEU A N   
6369  C CA  . LEU A 870  ? 0.2334 0.1791 0.2490 0.0136  -0.0121 0.0010  868  LEU A CA  
6370  C C   . LEU A 870  ? 0.2696 0.2145 0.2891 0.0151  -0.0132 -0.0001 868  LEU A C   
6371  O O   . LEU A 870  ? 0.2737 0.2194 0.2945 0.0179  -0.0134 -0.0041 868  LEU A O   
6372  C CB  . LEU A 870  ? 0.2581 0.2013 0.2778 0.0118  -0.0150 0.0021  868  LEU A CB  
6373  C CG  . LEU A 870  ? 0.2886 0.2299 0.3134 0.0135  -0.0178 -0.0016 868  LEU A CG  
6374  C CD1 . LEU A 870  ? 0.3437 0.2865 0.3653 0.0147  -0.0168 -0.0045 868  LEU A CD1 
6375  C CD2 . LEU A 870  ? 0.3538 0.2920 0.3851 0.0114  -0.0214 0.0009  868  LEU A CD2 
6376  N N   . HIS A 871  ? 0.2356 0.1795 0.2571 0.0134  -0.0140 0.0033  869  HIS A N   
6377  C CA  . HIS A 871  ? 0.2530 0.1958 0.2790 0.0147  -0.0155 0.0025  869  HIS A CA  
6378  C C   . HIS A 871  ? 0.2867 0.2321 0.3099 0.0168  -0.0130 0.0008  869  HIS A C   
6379  O O   . HIS A 871  ? 0.2855 0.2306 0.3124 0.0183  -0.0140 -0.0006 869  HIS A O   
6380  C CB  . HIS A 871  ? 0.3163 0.2573 0.3461 0.0121  -0.0175 0.0069  869  HIS A CB  
6381  C CG  . HIS A 871  ? 0.3292 0.2675 0.3640 0.0106  -0.0208 0.0081  869  HIS A CG  
6382  N ND1 . HIS A 871  ? 0.3954 0.3312 0.4370 0.0121  -0.0240 0.0054  869  HIS A ND1 
6383  C CD2 . HIS A 871  ? 0.3223 0.2605 0.3569 0.0077  -0.0216 0.0117  869  HIS A CD2 
6384  C CE1 . HIS A 871  ? 0.3891 0.3229 0.4346 0.0101  -0.0266 0.0075  869  HIS A CE1 
6385  N NE2 . HIS A 871  ? 0.3803 0.3156 0.4215 0.0073  -0.0252 0.0115  869  HIS A NE2 
6386  N N   . GLU A 872  ? 0.2352 0.1833 0.2525 0.0169  -0.0099 0.0009  870  GLU A N   
6387  C CA  . GLU A 872  ? 0.2541 0.2050 0.2688 0.0188  -0.0074 -0.0005 870  GLU A CA  
6388  C C   . GLU A 872  ? 0.2460 0.1994 0.2598 0.0217  -0.0067 -0.0048 870  GLU A C   
6389  O O   . GLU A 872  ? 0.2563 0.2130 0.2681 0.0234  -0.0046 -0.0059 870  GLU A O   
6390  C CB  . GLU A 872  ? 0.2466 0.1993 0.2562 0.0173  -0.0047 0.0023  870  GLU A CB  
6391  C CG  . GLU A 872  ? 0.2581 0.2096 0.2683 0.0146  -0.0052 0.0063  870  GLU A CG  
6392  C CD  . GLU A 872  ? 0.3041 0.2551 0.3175 0.0150  -0.0061 0.0069  870  GLU A CD  
6393  O OE1 . GLU A 872  ? 0.2981 0.2507 0.3121 0.0173  -0.0052 0.0046  870  GLU A OE1 
6394  O OE2 . GLU A 872  ? 0.2927 0.2423 0.3083 0.0130  -0.0076 0.0098  870  GLU A OE2 
6395  N N   . LEU A 873  ? 0.2394 0.1919 0.2548 0.0224  -0.0083 -0.0073 871  LEU A N   
6396  C CA  . LEU A 873  ? 0.2391 0.1946 0.2535 0.0252  -0.0077 -0.0116 871  LEU A CA  
6397  C C   . LEU A 873  ? 0.2500 0.2062 0.2692 0.0279  -0.0094 -0.0155 871  LEU A C   
6398  O O   . LEU A 873  ? 0.2836 0.2365 0.3085 0.0276  -0.0122 -0.0156 871  LEU A O   
6399  C CB  . LEU A 873  ? 0.2454 0.1997 0.2598 0.0249  -0.0090 -0.0131 871  LEU A CB  
6400  C CG  . LEU A 873  ? 0.2503 0.2044 0.2601 0.0225  -0.0074 -0.0099 871  LEU A CG  
6401  C CD1 . LEU A 873  ? 0.2609 0.2139 0.2715 0.0223  -0.0090 -0.0115 871  LEU A CD1 
6402  C CD2 . LEU A 873  ? 0.3048 0.2629 0.3091 0.0234  -0.0041 -0.0096 871  LEU A CD2 
6403  N N   . HIS A 874  ? 0.2539 0.2149 0.2711 0.0306  -0.0076 -0.0186 872  HIS A N   
6404  C CA  . HIS A 874  ? 0.2435 0.2066 0.2649 0.0336  -0.0089 -0.0230 872  HIS A CA  
6405  C C   . HIS A 874  ? 0.2229 0.1881 0.2450 0.0358  -0.0100 -0.0280 872  HIS A C   
6406  O O   . HIS A 874  ? 0.2473 0.2166 0.2644 0.0366  -0.0079 -0.0289 872  HIS A O   
6407  C CB  . HIS A 874  ? 0.2530 0.2213 0.2718 0.0351  -0.0060 -0.0230 872  HIS A CB  
6408  C CG  . HIS A 874  ? 0.2950 0.2665 0.3177 0.0384  -0.0069 -0.0276 872  HIS A CG  
6409  N ND1 . HIS A 874  ? 0.3738 0.3503 0.3952 0.0398  -0.0047 -0.0277 872  HIS A ND1 
6410  C CD2 . HIS A 874  ? 0.3786 0.3494 0.4069 0.0405  -0.0099 -0.0324 872  HIS A CD2 
6411  C CE1 . HIS A 874  ? 0.3324 0.3114 0.3580 0.0428  -0.0061 -0.0325 872  HIS A CE1 
6412  N NE2 . HIS A 874  ? 0.3101 0.2857 0.3402 0.0434  -0.0093 -0.0357 872  HIS A NE2 
6413  N N   . ILE A 875  ? 0.2433 0.2056 0.2717 0.0368  -0.0135 -0.0313 873  ILE A N   
6414  C CA  . ILE A 875  ? 0.2488 0.2127 0.2792 0.0390  -0.0152 -0.0367 873  ILE A CA  
6415  C C   . ILE A 875  ? 0.2992 0.2672 0.3333 0.0428  -0.0160 -0.0423 873  ILE A C   
6416  O O   . ILE A 875  ? 0.2886 0.2544 0.3282 0.0432  -0.0178 -0.0427 873  ILE A O   
6417  C CB  . ILE A 875  ? 0.3008 0.2586 0.3368 0.0375  -0.0190 -0.0366 873  ILE A CB  
6418  C CG1 . ILE A 875  ? 0.3767 0.3319 0.4087 0.0341  -0.0181 -0.0318 873  ILE A CG1 
6419  C CG2 . ILE A 875  ? 0.3205 0.2797 0.3602 0.0402  -0.0214 -0.0430 873  ILE A CG2 
6420  C CD1 . ILE A 875  ? 0.4469 0.3993 0.4771 0.0309  -0.0169 -0.0255 873  ILE A CD1 
6421  N N   . GLY A 876  ? 0.2701 0.2444 0.3015 0.0455  -0.0148 -0.0467 874  GLY A N   
6422  C CA  . GLY A 876  ? 0.2605 0.2397 0.2954 0.0493  -0.0155 -0.0526 874  GLY A CA  
6423  C C   . GLY A 876  ? 0.2619 0.2493 0.2925 0.0520  -0.0137 -0.0568 874  GLY A C   
6424  O O   . GLY A 876  ? 0.2596 0.2483 0.2850 0.0510  -0.0123 -0.0553 874  GLY A O   
6425  N N   . ARG A 877  ? 0.2799 0.2733 0.3130 0.0556  -0.0139 -0.0622 875  ARG A N   
6426  C CA  . ARG A 877  ? 0.2627 0.2656 0.2916 0.0584  -0.0120 -0.0662 875  ARG A CA  
6427  C C   . ARG A 877  ? 0.2492 0.2565 0.2701 0.0569  -0.0076 -0.0607 875  ARG A C   
6428  O O   . ARG A 877  ? 0.2735 0.2798 0.2934 0.0555  -0.0058 -0.0563 875  ARG A O   
6429  C CB  . ARG A 877  ? 0.3598 0.3689 0.3930 0.0624  -0.0128 -0.0726 875  ARG A CB  
6430  C CG  . ARG A 877  ? 0.3202 0.3393 0.3511 0.0659  -0.0121 -0.0787 875  ARG A CG  
6431  C CD  . ARG A 877  ? 0.3660 0.3911 0.4019 0.0699  -0.0133 -0.0856 875  ARG A CD  
6432  N NE  . ARG A 877  ? 0.3467 0.3792 0.3792 0.0708  -0.0098 -0.0836 875  ARG A NE  
6433  C CZ  . ARG A 877  ? 0.4596 0.4995 0.4954 0.0743  -0.0099 -0.0890 875  ARG A CZ  
6434  N NH1 . ARG A 877  ? 0.4433 0.4836 0.4860 0.0775  -0.0134 -0.0970 875  ARG A NH1 
6435  N NH2 . ARG A 877  ? 0.4050 0.4522 0.4372 0.0748  -0.0065 -0.0865 875  ARG A NH2 
6436  N N   . THR A 878  ? 0.2598 0.2718 0.2753 0.0571  -0.0060 -0.0608 876  THR A N   
6437  C CA  . THR A 878  ? 0.2392 0.2529 0.2479 0.0548  -0.0026 -0.0545 876  THR A CA  
6438  C C   . THR A 878  ? 0.2587 0.2819 0.2638 0.0563  0.0007  -0.0537 876  THR A C   
6439  O O   . THR A 878  ? 0.2673 0.2929 0.2671 0.0547  0.0034  -0.0488 876  THR A O   
6440  C CB  . THR A 878  ? 0.2666 0.2805 0.2715 0.0540  -0.0025 -0.0543 876  THR A CB  
6441  O OG1 . THR A 878  ? 0.2951 0.3159 0.3005 0.0574  -0.0036 -0.0609 876  THR A OG1 
6442  C CG2 . THR A 878  ? 0.3267 0.3309 0.3342 0.0514  -0.0050 -0.0527 876  THR A CG2 
6443  N N   . ASP A 879  ? 0.2503 0.2791 0.2585 0.0594  0.0004  -0.0583 877  ASP A N   
6444  C CA  . ASP A 879  ? 0.2866 0.3248 0.2917 0.0606  0.0035  -0.0571 877  ASP A CA  
6445  C C   . ASP A 879  ? 0.2685 0.3035 0.2743 0.0587  0.0049  -0.0519 877  ASP A C   
6446  O O   . ASP A 879  ? 0.2723 0.3142 0.2781 0.0602  0.0067  -0.0520 877  ASP A O   
6447  C CB  . ASP A 879  ? 0.2580 0.3055 0.2656 0.0650  0.0029  -0.0645 877  ASP A CB  
6448  C CG  . ASP A 879  ? 0.3475 0.3908 0.3626 0.0666  -0.0001 -0.0691 877  ASP A CG  
6449  O OD1 . ASP A 879  ? 0.3727 0.4056 0.3918 0.0648  -0.0027 -0.0684 877  ASP A OD1 
6450  O OD2 . ASP A 879  ? 0.3479 0.3987 0.3653 0.0697  0.0002  -0.0734 877  ASP A OD2 
6451  N N   . ARG A 880  ? 0.2681 0.2932 0.2747 0.0555  0.0041  -0.0474 878  ARG A N   
6452  C CA  . ARG A 880  ? 0.2596 0.2814 0.2661 0.0532  0.0055  -0.0419 878  ARG A CA  
6453  C C   . ARG A 880  ? 0.2389 0.2559 0.2413 0.0497  0.0067  -0.0359 878  ARG A C   
6454  O O   . ARG A 880  ? 0.2499 0.2610 0.2523 0.0483  0.0051  -0.0358 878  ARG A O   
6455  C CB  . ARG A 880  ? 0.3087 0.3229 0.3212 0.0526  0.0029  -0.0427 878  ARG A CB  
6456  C CG  . ARG A 880  ? 0.3409 0.3589 0.3585 0.0560  0.0015  -0.0483 878  ARG A CG  
6457  C CD  . ARG A 880  ? 0.4034 0.4130 0.4271 0.0550  -0.0013 -0.0481 878  ARG A CD  
6458  N NE  . ARG A 880  ? 0.6291 0.6418 0.6588 0.0583  -0.0031 -0.0538 878  ARG A NE  
6459  C CZ  . ARG A 880  ? 0.6492 0.6628 0.6816 0.0588  -0.0027 -0.0531 878  ARG A CZ  
6460  N NH1 . ARG A 880  ? 0.6887 0.7003 0.7186 0.0562  -0.0007 -0.0470 878  ARG A NH1 
6461  N NH2 . ARG A 880  ? 0.6853 0.7021 0.7234 0.0621  -0.0044 -0.0589 878  ARG A NH2 
6462  N N   . LEU A 881  ? 0.2254 0.2452 0.2247 0.0483  0.0095  -0.0309 879  LEU A N   
6463  C CA  . LEU A 881  ? 0.2132 0.2289 0.2091 0.0451  0.0106  -0.0253 879  LEU A CA  
6464  C C   . LEU A 881  ? 0.2368 0.2424 0.2349 0.0425  0.0087  -0.0234 879  LEU A C   
6465  O O   . LEU A 881  ? 0.2346 0.2359 0.2305 0.0403  0.0087  -0.0208 879  LEU A O   
6466  C CB  . LEU A 881  ? 0.2510 0.2709 0.2447 0.0442  0.0134  -0.0205 879  LEU A CB  
6467  C CG  . LEU A 881  ? 0.2542 0.2710 0.2449 0.0412  0.0147  -0.0149 879  LEU A CG  
6468  C CD1 . LEU A 881  ? 0.2670 0.2873 0.2540 0.0414  0.0154  -0.0148 879  LEU A CD1 
6469  C CD2 . LEU A 881  ? 0.2746 0.2945 0.2651 0.0402  0.0169  -0.0105 879  LEU A CD2 
6470  N N   . SER A 882  ? 0.2374 0.2396 0.2398 0.0428  0.0072  -0.0246 880  SER A N   
6471  C CA  . SER A 882  ? 0.2345 0.2282 0.2391 0.0402  0.0054  -0.0223 880  SER A CA  
6472  C C   . SER A 882  ? 0.2696 0.2585 0.2759 0.0399  0.0027  -0.0246 880  SER A C   
6473  O O   . SER A 882  ? 0.2746 0.2569 0.2824 0.0376  0.0013  -0.0223 880  SER A O   
6474  C CB  . SER A 882  ? 0.2435 0.2354 0.2528 0.0406  0.0043  -0.0227 880  SER A CB  
6475  O OG  . SER A 882  ? 0.2946 0.2885 0.3079 0.0436  0.0024  -0.0282 880  SER A OG  
6476  N N   . VAL A 883  ? 0.2488 0.2411 0.2551 0.0422  0.0020  -0.0291 881  VAL A N   
6477  C CA  . VAL A 883  ? 0.2563 0.2441 0.2649 0.0419  -0.0008 -0.0314 881  VAL A CA  
6478  C C   . VAL A 883  ? 0.2500 0.2359 0.2541 0.0397  0.0001  -0.0285 881  VAL A C   
6479  O O   . VAL A 883  ? 0.2869 0.2778 0.2866 0.0402  0.0023  -0.0280 881  VAL A O   
6480  C CB  . VAL A 883  ? 0.2720 0.2638 0.2831 0.0453  -0.0024 -0.0381 881  VAL A CB  
6481  C CG1 . VAL A 883  ? 0.2589 0.2464 0.2720 0.0449  -0.0051 -0.0402 881  VAL A CG1 
6482  C CG2 . VAL A 883  ? 0.2583 0.2504 0.2750 0.0473  -0.0040 -0.0412 881  VAL A CG2 
6483  N N   . ASP A 884  ? 0.2296 0.2088 0.2353 0.0373  -0.0016 -0.0265 882  ASP A N   
6484  C CA  . ASP A 884  ? 0.2640 0.2412 0.2662 0.0352  -0.0010 -0.0239 882  ASP A CA  
6485  C C   . ASP A 884  ? 0.2913 0.2679 0.2946 0.0360  -0.0030 -0.0274 882  ASP A C   
6486  O O   . ASP A 884  ? 0.3285 0.3070 0.3280 0.0357  -0.0020 -0.0270 882  ASP A O   
6487  C CB  . ASP A 884  ? 0.2462 0.2173 0.2494 0.0319  -0.0017 -0.0195 882  ASP A CB  
6488  C CG  . ASP A 884  ? 0.2361 0.2075 0.2384 0.0310  0.0001  -0.0161 882  ASP A CG  
6489  O OD1 . ASP A 884  ? 0.2687 0.2438 0.2672 0.0310  0.0026  -0.0144 882  ASP A OD1 
6490  O OD2 . ASP A 884  ? 0.2547 0.2228 0.2605 0.0302  -0.0013 -0.0152 882  ASP A OD2 
6491  N N   . VAL A 885  ? 0.2504 0.2243 0.2592 0.0370  -0.0061 -0.0308 883  VAL A N   
6492  C CA  . VAL A 885  ? 0.2781 0.2504 0.2892 0.0374  -0.0086 -0.0341 883  VAL A CA  
6493  C C   . VAL A 885  ? 0.2601 0.2356 0.2753 0.0409  -0.0104 -0.0404 883  VAL A C   
6494  O O   . VAL A 885  ? 0.2493 0.2233 0.2695 0.0418  -0.0119 -0.0417 883  VAL A O   
6495  C CB  . VAL A 885  ? 0.2750 0.2401 0.2901 0.0347  -0.0112 -0.0316 883  VAL A CB  
6496  C CG1 . VAL A 885  ? 0.2902 0.2536 0.3084 0.0351  -0.0140 -0.0350 883  VAL A CG1 
6497  C CG2 . VAL A 885  ? 0.3050 0.2678 0.3161 0.0314  -0.0093 -0.0258 883  VAL A CG2 
6498  N N   . GLY A 886  ? 0.2539 0.2341 0.2674 0.0430  -0.0103 -0.0444 884  GLY A N   
6499  C CA  . GLY A 886  ? 0.2358 0.2197 0.2531 0.0466  -0.0122 -0.0512 884  GLY A CA  
6500  C C   . GLY A 886  ? 0.2311 0.2105 0.2545 0.0468  -0.0162 -0.0549 884  GLY A C   
6501  O O   . GLY A 886  ? 0.2526 0.2252 0.2785 0.0440  -0.0180 -0.0517 884  GLY A O   
6502  N N   . PRO A 887  ? 0.2417 0.2254 0.2681 0.0502  -0.0179 -0.0617 885  PRO A N   
6503  C CA  . PRO A 887  ? 0.2432 0.2228 0.2768 0.0508  -0.0223 -0.0661 885  PRO A CA  
6504  C C   . PRO A 887  ? 0.2395 0.2185 0.2706 0.0498  -0.0228 -0.0662 885  PRO A C   
6505  O O   . PRO A 887  ? 0.2539 0.2369 0.2778 0.0493  -0.0198 -0.0641 885  PRO A O   
6506  C CB  . PRO A 887  ? 0.2377 0.2237 0.2744 0.0553  -0.0234 -0.0740 885  PRO A CB  
6507  C CG  . PRO A 887  ? 0.2667 0.2619 0.2953 0.0568  -0.0193 -0.0739 885  PRO A CG  
6508  C CD  . PRO A 887  ? 0.2674 0.2604 0.2911 0.0537  -0.0160 -0.0660 885  PRO A CD  
6509  N N   . VAL A 888  ? 0.2372 0.2111 0.2749 0.0493  -0.0267 -0.0684 886  VAL A N   
6510  C CA  . VAL A 888  ? 0.2482 0.2228 0.2851 0.0495  -0.0279 -0.0709 886  VAL A CA  
6511  C C   . VAL A 888  ? 0.2491 0.2307 0.2874 0.0538  -0.0291 -0.0793 886  VAL A C   
6512  O O   . VAL A 888  ? 0.2608 0.2449 0.3031 0.0566  -0.0301 -0.0838 886  VAL A O   
6513  C CB  . VAL A 888  ? 0.2738 0.2404 0.3172 0.0469  -0.0317 -0.0694 886  VAL A CB  
6514  C CG1 . VAL A 888  ? 0.2805 0.2417 0.3216 0.0427  -0.0302 -0.0610 886  VAL A CG1 
6515  C CG2 . VAL A 888  ? 0.3164 0.2796 0.3699 0.0484  -0.0361 -0.0737 886  VAL A CG2 
6516  N N   . ILE A 889  ? 0.2605 0.2458 0.2953 0.0545  -0.0288 -0.0816 887  ILE A N   
6517  C CA  . ILE A 889  ? 0.2661 0.2608 0.2992 0.0586  -0.0285 -0.0886 887  ILE A CA  
6518  C C   . ILE A 889  ? 0.2520 0.2466 0.2940 0.0617  -0.0328 -0.0968 887  ILE A C   
6519  O O   . ILE A 889  ? 0.2685 0.2707 0.3109 0.0654  -0.0326 -0.1028 887  ILE A O   
6520  C CB  . ILE A 889  ? 0.2831 0.2822 0.3098 0.0584  -0.0270 -0.0885 887  ILE A CB  
6521  C CG1 . ILE A 889  ? 0.2800 0.2903 0.3037 0.0626  -0.0260 -0.0949 887  ILE A CG1 
6522  C CG2 . ILE A 889  ? 0.2820 0.2752 0.3131 0.0570  -0.0305 -0.0897 887  ILE A CG2 
6523  C CD1 . ILE A 889  ? 0.2889 0.3061 0.3078 0.0639  -0.0224 -0.0933 887  ILE A CD1 
6524  N N   . THR A 890  ? 0.2664 0.2531 0.3162 0.0603  -0.0370 -0.0975 888  THR A N   
6525  C CA  . THR A 890  ? 0.2693 0.2556 0.3286 0.0633  -0.0416 -0.1057 888  THR A CA  
6526  C C   . THR A 890  ? 0.2712 0.2473 0.3399 0.0609  -0.0456 -0.1032 888  THR A C   
6527  O O   . THR A 890  ? 0.2753 0.2450 0.3429 0.0568  -0.0449 -0.0957 888  THR A O   
6528  C CB  . THR A 890  ? 0.3106 0.2997 0.3710 0.0648  -0.0439 -0.1115 888  THR A CB  
6529  O OG1 . THR A 890  ? 0.3188 0.3010 0.3792 0.0610  -0.0449 -0.1063 888  THR A OG1 
6530  C CG2 . THR A 890  ? 0.3112 0.3113 0.3627 0.0673  -0.0406 -0.1143 888  THR A CG2 
6531  N N   . SER A 891  ? 0.3054 0.2803 0.3840 0.0635  -0.0499 -0.1100 889  SER A N   
6532  C CA  A SER A 891  ? 0.3271 0.2925 0.4163 0.0615  -0.0544 -0.1082 889  SER A CA  
6533  C CA  B SER A 891  ? 0.3271 0.2924 0.4161 0.0614  -0.0543 -0.1080 889  SER A CA  
6534  C C   . SER A 891  ? 0.3228 0.2827 0.4140 0.0585  -0.0566 -0.1056 889  SER A C   
6535  O O   . SER A 891  ? 0.3233 0.2754 0.4188 0.0548  -0.0584 -0.0995 889  SER A O   
6536  C CB  A SER A 891  ? 0.3214 0.2872 0.4215 0.0653  -0.0591 -0.1170 889  SER A CB  
6537  C CB  B SER A 891  ? 0.3213 0.2868 0.4212 0.0652  -0.0589 -0.1165 889  SER A CB  
6538  O OG  A SER A 891  ? 0.3292 0.2992 0.4286 0.0678  -0.0574 -0.1190 889  SER A OG  
6539  O OG  B SER A 891  ? 0.3719 0.3419 0.4740 0.0682  -0.0612 -0.1249 889  SER A OG  
6540  N N   . GLU A 892  ? 0.3001 0.2645 0.3883 0.0599  -0.0567 -0.1100 890  GLU A N   
6541  C CA  . GLU A 892  ? 0.3264 0.2861 0.4165 0.0571  -0.0587 -0.1077 890  GLU A CA  
6542  C C   . GLU A 892  ? 0.3559 0.3129 0.4381 0.0527  -0.0550 -0.0979 890  GLU A C   
6543  O O   . GLU A 892  ? 0.3384 0.2887 0.4245 0.0491  -0.0569 -0.0928 890  GLU A O   
6544  C CB  . GLU A 892  ? 0.3319 0.2979 0.4198 0.0598  -0.0593 -0.1146 890  GLU A CB  
6545  C CG  . GLU A 892  ? 0.4601 0.4303 0.5551 0.0646  -0.0628 -0.1253 890  GLU A CG  
6546  C CD  . GLU A 892  ? 0.4936 0.4743 0.5812 0.0685  -0.0591 -0.1297 890  GLU A CD  
6547  O OE1 . GLU A 892  ? 0.4142 0.3958 0.5020 0.0694  -0.0577 -0.1290 890  GLU A OE1 
6548  O OE2 . GLU A 892  ? 0.6614 0.6499 0.7431 0.0705  -0.0576 -0.1337 890  GLU A OE2 
6549  N N   . ALA A 893  ? 0.3103 0.2728 0.3819 0.0529  -0.0499 -0.0952 891  ALA A N   
6550  C CA  . ALA A 893  ? 0.3122 0.2724 0.3767 0.0490  -0.0463 -0.0863 891  ALA A CA  
6551  C C   . ALA A 893  ? 0.3306 0.2840 0.3995 0.0461  -0.0471 -0.0802 891  ALA A C   
6552  O O   . ALA A 893  ? 0.3098 0.2580 0.3790 0.0423  -0.0473 -0.0739 891  ALA A O   
6553  C CB  . ALA A 893  ? 0.3064 0.2738 0.3600 0.0501  -0.0410 -0.0849 891  ALA A CB  
6554  N N   . LYS A 894  ? 0.2877 0.2412 0.3601 0.0479  -0.0476 -0.0820 892  LYS A N   
6555  C CA  . LYS A 894  ? 0.3021 0.2495 0.3794 0.0454  -0.0488 -0.0767 892  LYS A CA  
6556  C C   . LYS A 894  ? 0.3346 0.2748 0.4217 0.0431  -0.0537 -0.0752 892  LYS A C   
6557  O O   . LYS A 894  ? 0.3599 0.2952 0.4478 0.0392  -0.0538 -0.0679 892  LYS A O   
6558  C CB  . LYS A 894  ? 0.3140 0.2632 0.3950 0.0484  -0.0493 -0.0805 892  LYS A CB  
6559  C CG  . LYS A 894  ? 0.3215 0.2646 0.4085 0.0463  -0.0510 -0.0757 892  LYS A CG  
6560  C CD  . LYS A 894  ? 0.3452 0.2909 0.4353 0.0496  -0.0512 -0.0798 892  LYS A CD  
6561  C CE  . LYS A 894  ? 0.4029 0.3426 0.4995 0.0475  -0.0532 -0.0751 892  LYS A CE  
6562  N NZ  . LYS A 894  ? 0.5372 0.4789 0.6391 0.0511  -0.0545 -0.0803 892  LYS A NZ  
6563  N N   . ASP A 895  ? 0.3194 0.2591 0.4145 0.0454  -0.0580 -0.0822 893  ASP A N   
6564  C CA  . ASP A 895  ? 0.3830 0.3158 0.4884 0.0431  -0.0631 -0.0809 893  ASP A CA  
6565  C C   . ASP A 895  ? 0.3485 0.2794 0.4502 0.0393  -0.0621 -0.0751 893  ASP A C   
6566  O O   . ASP A 895  ? 0.3594 0.2847 0.4663 0.0356  -0.0643 -0.0691 893  ASP A O   
6567  C CB  . ASP A 895  ? 0.3720 0.3054 0.4863 0.0466  -0.0678 -0.0902 893  ASP A CB  
6568  C CG  . ASP A 895  ? 0.4492 0.3834 0.5701 0.0502  -0.0699 -0.0960 893  ASP A CG  
6569  O OD1 . ASP A 895  ? 0.5224 0.4549 0.6435 0.0493  -0.0687 -0.0918 893  ASP A OD1 
6570  O OD2 . ASP A 895  ? 0.4980 0.4349 0.6243 0.0539  -0.0728 -0.1049 893  ASP A OD2 
6571  N N   . ASN A 896  ? 0.3136 0.2495 0.4067 0.0400  -0.0591 -0.0767 894  ASN A N   
6572  C CA  . ASN A 896  ? 0.3198 0.2543 0.4091 0.0367  -0.0581 -0.0717 894  ASN A CA  
6573  C C   . ASN A 896  ? 0.3686 0.3012 0.4526 0.0329  -0.0549 -0.0626 894  ASN A C   
6574  O O   . ASN A 896  ? 0.3362 0.2650 0.4225 0.0292  -0.0560 -0.0569 894  ASN A O   
6575  C CB  . ASN A 896  ? 0.3456 0.2863 0.4263 0.0386  -0.0553 -0.0753 894  ASN A CB  
6576  C CG  . ASN A 896  ? 0.4977 0.4374 0.5742 0.0353  -0.0540 -0.0704 894  ASN A CG  
6577  O OD1 . ASN A 896  ? 0.5442 0.4858 0.6120 0.0336  -0.0497 -0.0652 894  ASN A OD1 
6578  N ND2 . ASN A 896  ? 0.5135 0.4504 0.5968 0.0344  -0.0579 -0.0719 894  ASN A ND2 
6579  N N   . ILE A 897  ? 0.3373 0.2730 0.4143 0.0337  -0.0509 -0.0611 895  ILE A N   
6580  C CA  . ILE A 897  ? 0.3170 0.2514 0.3889 0.0304  -0.0478 -0.0530 895  ILE A CA  
6581  C C   . ILE A 897  ? 0.3608 0.2895 0.4410 0.0279  -0.0509 -0.0487 895  ILE A C   
6582  O O   . ILE A 897  ? 0.3497 0.2758 0.4296 0.0241  -0.0507 -0.0419 895  ILE A O   
6583  C CB  . ILE A 897  ? 0.2757 0.2146 0.3393 0.0322  -0.0433 -0.0530 895  ILE A CB  
6584  C CG1 . ILE A 897  ? 0.3016 0.2465 0.3569 0.0342  -0.0402 -0.0562 895  ILE A CG1 
6585  C CG2 . ILE A 897  ? 0.3013 0.2387 0.3604 0.0288  -0.0405 -0.0451 895  ILE A CG2 
6586  C CD1 . ILE A 897  ? 0.2968 0.2472 0.3467 0.0372  -0.0370 -0.0587 895  ILE A CD1 
6587  N N   . GLU A 898  ? 0.3391 0.2661 0.4269 0.0301  -0.0539 -0.0524 896  GLU A N   
6588  C CA  . GLU A 898  ? 0.3518 0.2736 0.4478 0.0278  -0.0570 -0.0480 896  GLU A CA  
6589  C C   . GLU A 898  ? 0.3791 0.2964 0.4833 0.0249  -0.0612 -0.0454 896  GLU A C   
6590  O O   . GLU A 898  ? 0.3838 0.2978 0.4915 0.0213  -0.0624 -0.0384 896  GLU A O   
6591  C CB  . GLU A 898  ? 0.3496 0.2708 0.4524 0.0310  -0.0594 -0.0530 896  GLU A CB  
6592  C CG  . GLU A 898  ? 0.4032 0.3286 0.4987 0.0330  -0.0552 -0.0535 896  GLU A CG  
6593  C CD  . GLU A 898  ? 0.4863 0.4116 0.5885 0.0363  -0.0575 -0.0587 896  GLU A CD  
6594  O OE1 . GLU A 898  ? 0.5048 0.4284 0.6163 0.0383  -0.0620 -0.0644 896  GLU A OE1 
6595  O OE2 . GLU A 898  ? 0.5916 0.5187 0.6903 0.0370  -0.0550 -0.0574 896  GLU A OE2 
6596  N N   . LYS A 899  ? 0.3609 0.2784 0.4684 0.0263  -0.0636 -0.0506 897  LYS A N   
6597  C CA  . LYS A 899  ? 0.3790 0.2925 0.4942 0.0234  -0.0675 -0.0479 897  LYS A CA  
6598  C C   . LYS A 899  ? 0.4277 0.3418 0.5364 0.0192  -0.0647 -0.0401 897  LYS A C   
6599  O O   . LYS A 899  ? 0.3920 0.3027 0.5063 0.0155  -0.0670 -0.0341 897  LYS A O   
6600  C CB  . LYS A 899  ? 0.3969 0.3112 0.5155 0.0258  -0.0702 -0.0554 897  LYS A CB  
6601  N N   . HIS A 900  ? 0.3538 0.2723 0.4508 0.0197  -0.0596 -0.0400 898  HIS A N   
6602  C CA  . HIS A 900  ? 0.3644 0.2839 0.4549 0.0161  -0.0566 -0.0330 898  HIS A CA  
6603  C C   . HIS A 900  ? 0.3780 0.2963 0.4681 0.0133  -0.0555 -0.0259 898  HIS A C   
6604  O O   . HIS A 900  ? 0.4097 0.3268 0.5015 0.0095  -0.0561 -0.0194 898  HIS A O   
6605  C CB  . HIS A 900  ? 0.3353 0.2598 0.4142 0.0176  -0.0517 -0.0348 898  HIS A CB  
6606  C CG  . HIS A 900  ? 0.3552 0.2812 0.4269 0.0143  -0.0482 -0.0281 898  HIS A CG  
6607  N ND1 . HIS A 900  ? 0.3747 0.3005 0.4468 0.0116  -0.0488 -0.0251 898  HIS A ND1 
6608  C CD2 . HIS A 900  ? 0.3614 0.2893 0.4260 0.0133  -0.0443 -0.0240 898  HIS A CD2 
6609  C CE1 . HIS A 900  ? 0.3583 0.2860 0.4235 0.0092  -0.0453 -0.0197 898  HIS A CE1 
6610  N NE2 . HIS A 900  ? 0.3528 0.2817 0.4135 0.0103  -0.0426 -0.0191 898  HIS A NE2 
6611  N N   . ILE A 901  ? 0.3279 0.2470 0.4156 0.0153  -0.0538 -0.0270 899  ILE A N   
6612  C CA  . ILE A 901  ? 0.3596 0.2778 0.4469 0.0129  -0.0529 -0.0206 899  ILE A CA  
6613  C C   . ILE A 901  ? 0.4085 0.3224 0.5068 0.0102  -0.0577 -0.0165 899  ILE A C   
6614  O O   . ILE A 901  ? 0.4284 0.3420 0.5267 0.0066  -0.0574 -0.0093 899  ILE A O   
6615  C CB  . ILE A 901  ? 0.3204 0.2401 0.4047 0.0157  -0.0508 -0.0232 899  ILE A CB  
6616  C CG1 . ILE A 901  ? 0.3534 0.2779 0.4266 0.0176  -0.0458 -0.0256 899  ILE A CG1 
6617  C CG2 . ILE A 901  ? 0.3509 0.2693 0.4363 0.0133  -0.0506 -0.0168 899  ILE A CG2 
6618  C CD1 . ILE A 901  ? 0.3346 0.2612 0.4053 0.0209  -0.0440 -0.0291 899  ILE A CD1 
6619  N N   . GLU A 902  ? 0.4104 0.3212 0.5186 0.0120  -0.0623 -0.0211 900  GLU A N   
6620  C CA  . GLU A 902  ? 0.4768 0.3832 0.5967 0.0095  -0.0674 -0.0172 900  GLU A CA  
6621  C C   . GLU A 902  ? 0.4478 0.3533 0.5709 0.0058  -0.0692 -0.0125 900  GLU A C   
6622  O O   . GLU A 902  ? 0.5137 0.4173 0.6423 0.0022  -0.0714 -0.0055 900  GLU A O   
6623  C CB  . GLU A 902  ? 0.5246 0.4278 0.6550 0.0128  -0.0721 -0.0239 900  GLU A CB  
6624  C CG  . GLU A 902  ? 0.5925 0.4961 0.7222 0.0157  -0.0711 -0.0267 900  GLU A CG  
6625  C CD  . GLU A 902  ? 0.5834 0.4866 0.7119 0.0128  -0.0699 -0.0190 900  GLU A CD  
6626  O OE1 . GLU A 902  ? 0.6328 0.5328 0.7695 0.0097  -0.0734 -0.0132 900  GLU A OE1 
6627  O OE2 . GLU A 902  ? 0.5889 0.4952 0.7082 0.0137  -0.0654 -0.0185 900  GLU A OE2 
6628  N N   . ARG A 903  ? 0.4333 0.3403 0.5531 0.0065  -0.0684 -0.0160 901  ARG A N   
6629  C CA  . ARG A 903  ? 0.4914 0.3984 0.6129 0.0029  -0.0695 -0.0112 901  ARG A CA  
6630  C C   . ARG A 903  ? 0.5605 0.4704 0.6749 -0.0008 -0.0658 -0.0031 901  ARG A C   
6631  O O   . ARG A 903  ? 0.5478 0.4572 0.6670 -0.0047 -0.0678 0.0037  901  ARG A O   
6632  C CB  . ARG A 903  ? 0.4902 0.3991 0.6077 0.0045  -0.0685 -0.0166 901  ARG A CB  
6633  N N   . MET A 904  ? 0.5044 0.4179 0.6076 0.0005  -0.0607 -0.0038 902  MET A N   
6634  C CA  . MET A 904  ? 0.4766 0.3932 0.5728 -0.0025 -0.0572 0.0031  902  MET A CA  
6635  C C   . MET A 904  ? 0.4851 0.4003 0.5865 -0.0048 -0.0589 0.0089  902  MET A C   
6636  O O   . MET A 904  ? 0.5031 0.4199 0.6052 -0.0086 -0.0590 0.0160  902  MET A O   
6637  C CB  . MET A 904  ? 0.4044 0.3244 0.4889 -0.0003 -0.0518 0.0005  902  MET A CB  
6638  C CG  . MET A 904  ? 0.4340 0.3562 0.5126 0.0016  -0.0497 -0.0042 902  MET A CG  
6639  S SD  . MET A 904  ? 0.5823 0.5068 0.6590 -0.0021 -0.0490 0.0004  902  MET A SD  
6640  C CE  . MET A 904  ? 0.5312 0.4524 0.6175 -0.0016 -0.0541 -0.0035 902  MET A CE  
6641  N N   . ARG A 905  ? 0.4355 0.3483 0.5406 -0.0023 -0.0603 0.0060  903  ARG A N   
6642  C CA  . ARG A 905  ? 0.4752 0.3865 0.5857 -0.0043 -0.0623 0.0114  903  ARG A CA  
6643  C C   . ARG A 905  ? 0.5335 0.4422 0.6554 -0.0075 -0.0674 0.0162  903  ARG A C   
6644  O O   . ARG A 905  ? 0.4630 0.3725 0.5873 -0.0109 -0.0683 0.0237  903  ARG A O   
6645  C CB  . ARG A 905  ? 0.4685 0.3775 0.5819 -0.0007 -0.0633 0.0066  903  ARG A CB  
6646  C CG  . ARG A 905  ? 0.4928 0.4014 0.6087 -0.0023 -0.0639 0.0119  903  ARG A CG  
6647  C CD  . ARG A 905  ? 0.5632 0.4689 0.6844 0.0012  -0.0659 0.0069  903  ARG A CD  
6648  N NE  . ARG A 905  ? 0.4971 0.4048 0.6107 0.0053  -0.0624 -0.0003 903  ARG A NE  
6649  C CZ  . ARG A 905  ? 0.5089 0.4194 0.6142 0.0064  -0.0582 -0.0002 903  ARG A CZ  
6650  N NH1 . ARG A 905  ? 0.4716 0.3835 0.5741 0.0037  -0.0567 0.0063  903  ARG A NH1 
6651  N NH2 . ARG A 905  ? 0.5454 0.4579 0.6452 0.0102  -0.0556 -0.0068 903  ARG A NH2 
6652  N N   . GLY A 906  ? 0.5010 0.4067 0.6301 -0.0064 -0.0710 0.0120  904  GLY A N   
6653  C CA  . GLY A 906  ? 0.5882 0.4911 0.7291 -0.0095 -0.0762 0.0165  904  GLY A CA  
6654  C C   . GLY A 906  ? 0.6350 0.5413 0.7733 -0.0139 -0.0751 0.0237  904  GLY A C   
6655  O O   . GLY A 906  ? 0.7147 0.6203 0.8613 -0.0176 -0.0786 0.0305  904  GLY A O   
6656  N N   . LEU A 907  ? 0.5987 0.5091 0.7260 -0.0137 -0.0704 0.0226  905  LEU A N   
6657  C CA  . LEU A 907  ? 0.5568 0.4713 0.6808 -0.0176 -0.0688 0.0289  905  LEU A CA  
6658  C C   . LEU A 907  ? 0.5736 0.4924 0.6924 -0.0203 -0.0661 0.0360  905  LEU A C   
6659  O O   . LEU A 907  ? 0.6032 0.5265 0.7182 -0.0234 -0.0642 0.0411  905  LEU A O   
6660  C CB  . LEU A 907  ? 0.5362 0.4535 0.6510 -0.0162 -0.0651 0.0246  905  LEU A CB  
6661  C CG  . LEU A 907  ? 0.5625 0.4769 0.6821 -0.0140 -0.0677 0.0182  905  LEU A CG  
6662  C CD1 . LEU A 907  ? 0.6308 0.5485 0.7412 -0.0132 -0.0640 0.0151  905  LEU A CD1 
6663  C CD2 . LEU A 907  ? 0.6265 0.5382 0.7585 -0.0170 -0.0732 0.0219  905  LEU A CD2 
6664  N N   . GLY A 908  ? 0.5233 0.4411 0.6417 -0.0191 -0.0657 0.0362  906  GLY A N   
6665  C CA  . GLY A 908  ? 0.5015 0.4233 0.6151 -0.0215 -0.0633 0.0426  906  GLY A CA  
6666  C C   . GLY A 908  ? 0.4500 0.3756 0.5507 -0.0198 -0.0575 0.0402  906  GLY A C   
6667  O O   . GLY A 908  ? 0.4377 0.3671 0.5340 -0.0216 -0.0554 0.0449  906  GLY A O   
6668  N N   . ARG A 909  ? 0.4438 0.3687 0.5388 -0.0165 -0.0551 0.0331  907  ARG A N   
6669  C CA  . ARG A 909  ? 0.3841 0.3126 0.4676 -0.0150 -0.0498 0.0311  907  ARG A CA  
6670  C C   . ARG A 909  ? 0.4318 0.3595 0.5132 -0.0131 -0.0486 0.0301  907  ARG A C   
6671  O O   . ARG A 909  ? 0.4546 0.3783 0.5417 -0.0110 -0.0512 0.0271  907  ARG A O   
6672  C CB  . ARG A 909  ? 0.3897 0.3177 0.4685 -0.0119 -0.0480 0.0241  907  ARG A CB  
6673  C CG  . ARG A 909  ? 0.4164 0.3444 0.4981 -0.0133 -0.0497 0.0241  907  ARG A CG  
6674  C CD  . ARG A 909  ? 0.4454 0.3785 0.5225 -0.0166 -0.0474 0.0294  907  ARG A CD  
6675  N NE  . ARG A 909  ? 0.4945 0.4282 0.5726 -0.0173 -0.0481 0.0283  907  ARG A NE  
6676  C CZ  . ARG A 909  ? 0.6258 0.5592 0.7115 -0.0202 -0.0514 0.0322  907  ARG A CZ  
6677  N NH1 . ARG A 909  ? 0.5872 0.5198 0.6804 -0.0229 -0.0546 0.0378  907  ARG A NH1 
6678  N NH2 . ARG A 909  ? 0.5337 0.4678 0.6195 -0.0206 -0.0517 0.0307  907  ARG A NH2 
6679  N N   . LYS A 910  ? 0.3343 0.2660 0.4077 -0.0138 -0.0448 0.0324  908  LYS A N   
6680  C CA  . LYS A 910  ? 0.3581 0.2896 0.4287 -0.0122 -0.0433 0.0317  908  LYS A CA  
6681  C C   . LYS A 910  ? 0.3415 0.2714 0.4082 -0.0079 -0.0414 0.0243  908  LYS A C   
6682  O O   . LYS A 910  ? 0.3449 0.2765 0.4050 -0.0067 -0.0385 0.0211  908  LYS A O   
6683  C CB  . LYS A 910  ? 0.4041 0.3408 0.4671 -0.0142 -0.0397 0.0357  908  LYS A CB  
6684  C CG  . LYS A 910  ? 0.5124 0.4496 0.5751 -0.0142 -0.0394 0.0380  908  LYS A CG  
6685  C CD  . LYS A 910  ? 0.4700 0.4130 0.5263 -0.0166 -0.0365 0.0424  908  LYS A CD  
6686  C CE  . LYS A 910  ? 0.5861 0.5299 0.6427 -0.0170 -0.0365 0.0452  908  LYS A CE  
6687  N NZ  . LYS A 910  ? 0.6056 0.5555 0.6558 -0.0190 -0.0337 0.0487  908  LYS A NZ  
6688  N N   . VAL A 911  ? 0.3221 0.2489 0.3930 -0.0057 -0.0431 0.0216  909  VAL A N   
6689  C CA  . VAL A 911  ? 0.3116 0.2372 0.3802 -0.0015 -0.0419 0.0145  909  VAL A CA  
6690  C C   . VAL A 911  ? 0.3248 0.2509 0.3907 -0.0001 -0.0401 0.0143  909  VAL A C   
6691  O O   . VAL A 911  ? 0.3882 0.3125 0.4602 -0.0007 -0.0426 0.0167  909  VAL A O   
6692  C CB  . VAL A 911  ? 0.3342 0.2557 0.4115 0.0004  -0.0460 0.0101  909  VAL A CB  
6693  C CG1 . VAL A 911  ? 0.3969 0.3184 0.4718 0.0049  -0.0447 0.0028  909  VAL A CG1 
6694  C CG2 . VAL A 911  ? 0.3460 0.2671 0.4261 -0.0009 -0.0478 0.0101  909  VAL A CG2 
6695  N N   . GLU A 912  ? 0.3343 0.2631 0.3918 0.0016  -0.0360 0.0119  910  GLU A N   
6696  C CA  . GLU A 912  ? 0.3418 0.2714 0.3963 0.0032  -0.0340 0.0112  910  GLU A CA  
6697  C C   . GLU A 912  ? 0.3396 0.2687 0.3936 0.0073  -0.0335 0.0044  910  GLU A C   
6698  O O   . GLU A 912  ? 0.3209 0.2515 0.3707 0.0087  -0.0318 0.0009  910  GLU A O   
6699  C CB  . GLU A 912  ? 0.3439 0.2773 0.3895 0.0021  -0.0298 0.0134  910  GLU A CB  
6700  C CG  . GLU A 912  ? 0.3346 0.2691 0.3774 0.0032  -0.0278 0.0136  910  GLU A CG  
6701  C CD  . GLU A 912  ? 0.4031 0.3372 0.4499 0.0008  -0.0296 0.0187  910  GLU A CD  
6702  O OE1 . GLU A 912  ? 0.4028 0.3368 0.4529 -0.0021 -0.0317 0.0230  910  GLU A OE1 
6703  O OE2 . GLU A 912  ? 0.3956 0.3297 0.4423 0.0018  -0.0291 0.0187  910  GLU A OE2 
6704  N N   . GLN A 913  ? 0.3326 0.2602 0.3909 0.0091  -0.0349 0.0026  911  GLN A N   
6705  C CA  . GLN A 913  ? 0.3356 0.2637 0.3940 0.0131  -0.0345 -0.0040 911  GLN A CA  
6706  C C   . GLN A 913  ? 0.4206 0.3498 0.4777 0.0147  -0.0330 -0.0045 911  GLN A C   
6707  O O   . GLN A 913  ? 0.4168 0.3445 0.4775 0.0133  -0.0344 -0.0010 911  GLN A O   
6708  C CB  . GLN A 913  ? 0.3771 0.3020 0.4447 0.0146  -0.0390 -0.0078 911  GLN A CB  
6709  C CG  . GLN A 913  ? 0.3750 0.2990 0.4441 0.0138  -0.0405 -0.0088 911  GLN A CG  
6710  C CD  . GLN A 913  ? 0.3744 0.2960 0.4519 0.0162  -0.0446 -0.0144 911  GLN A CD  
6711  O OE1 . GLN A 913  ? 0.4160 0.3342 0.5024 0.0160  -0.0484 -0.0138 911  GLN A OE1 
6712  N NE2 . GLN A 913  ? 0.3380 0.2614 0.4131 0.0186  -0.0439 -0.0198 911  GLN A NE2 
6713  N N   . ILE A 914  ? 0.4158 0.3480 0.4677 0.0176  -0.0301 -0.0087 912  ILE A N   
6714  C CA  . ILE A 914  ? 0.3709 0.3045 0.4221 0.0197  -0.0288 -0.0102 912  ILE A CA  
6715  C C   . ILE A 914  ? 0.3981 0.3296 0.4581 0.0219  -0.0325 -0.0139 912  ILE A C   
6716  O O   . ILE A 914  ? 0.3841 0.3142 0.4487 0.0232  -0.0351 -0.0178 912  ILE A O   
6717  C CB  . ILE A 914  ? 0.4593 0.3972 0.5035 0.0221  -0.0252 -0.0139 912  ILE A CB  
6718  C CG1 . ILE A 914  ? 0.4545 0.3945 0.4907 0.0201  -0.0216 -0.0100 912  ILE A CG1 
6719  C CG2 . ILE A 914  ? 0.6013 0.5414 0.6462 0.0252  -0.0244 -0.0172 912  ILE A CG2 
6720  C CD1 . ILE A 914  ? 0.4145 0.3584 0.4445 0.0221  -0.0184 -0.0130 912  ILE A CD1 
6721  N N   . GLY A 915  ? 0.4722 0.4032 0.5347 0.0223  -0.0329 -0.0128 913  GLY A N   
6722  C CA  . GLY A 915  ? 0.4529 0.3825 0.5235 0.0249  -0.0361 -0.0169 913  GLY A CA  
6723  C C   . GLY A 915  ? 0.4936 0.4273 0.5614 0.0290  -0.0340 -0.0233 913  GLY A C   
6724  O O   . GLY A 915  ? 0.5649 0.5024 0.6258 0.0295  -0.0302 -0.0229 913  GLY A O   
6725  N N   . LEU A 916  ? 0.4336 0.3672 0.5071 0.0318  -0.0367 -0.0293 914  LEU A N   
6726  C CA  . LEU A 916  ? 0.5011 0.4397 0.5723 0.0358  -0.0350 -0.0359 914  LEU A CA  
6727  C C   . LEU A 916  ? 0.5077 0.4472 0.5839 0.0383  -0.0360 -0.0388 914  LEU A C   
6728  O O   . LEU A 916  ? 0.5143 0.4497 0.5992 0.0382  -0.0399 -0.0387 914  LEU A O   
6729  C CB  . LEU A 916  ? 0.4820 0.4206 0.5566 0.0377  -0.0374 -0.0417 914  LEU A CB  
6730  C CG  . LEU A 916  ? 0.4945 0.4330 0.5641 0.0358  -0.0363 -0.0400 914  LEU A CG  
6731  C CD1 . LEU A 916  ? 0.4668 0.4059 0.5402 0.0382  -0.0388 -0.0465 914  LEU A CD1 
6732  C CD2 . LEU A 916  ? 0.5190 0.4622 0.5779 0.0355  -0.0312 -0.0382 914  LEU A CD2 
6733  N N   . ALA A 917  ? 0.4230 0.3681 0.4939 0.0407  -0.0326 -0.0412 915  ALA A N   
6734  C CA  . ALA A 917  ? 0.4521 0.3992 0.5273 0.0434  -0.0332 -0.0444 915  ALA A CA  
6735  C C   . ALA A 917  ? 0.4468 0.3944 0.5299 0.0470  -0.0368 -0.0520 915  ALA A C   
6736  O O   . ALA A 917  ? 0.4466 0.3950 0.5298 0.0480  -0.0377 -0.0559 915  ALA A O   
6737  C CB  . ALA A 917  ? 0.4826 0.4364 0.5501 0.0450  -0.0285 -0.0451 915  ALA A CB  
6738  N N   . SER A 918  ? 0.4458 0.3930 0.5361 0.0490  -0.0390 -0.0545 916  SER A N   
6739  C CA  . SER A 918  ? 0.4866 0.4345 0.5854 0.0527  -0.0426 -0.0624 916  SER A CA  
6740  C C   . SER A 918  ? 0.4192 0.3750 0.5133 0.0564  -0.0403 -0.0693 916  SER A C   
6741  O O   . SER A 918  ? 0.3876 0.3444 0.4867 0.0590  -0.0431 -0.0759 916  SER A O   
6742  C CB  . SER A 918  ? 0.4530 0.3999 0.5596 0.0544  -0.0449 -0.0637 916  SER A CB  
6743  O OG  . SER A 918  ? 0.5507 0.5028 0.6514 0.0552  -0.0408 -0.0626 916  SER A OG  
6744  N N   . GLU A 919  ? 0.4444 0.4063 0.5293 0.0566  -0.0354 -0.0677 917  GLU A N   
6745  C CA  . GLU A 919  ? 0.4311 0.4017 0.5111 0.0600  -0.0328 -0.0734 917  GLU A CA  
6746  C C   . GLU A 919  ? 0.4557 0.4268 0.5328 0.0598  -0.0331 -0.0755 917  GLU A C   
6747  O O   . GLU A 919  ? 0.4060 0.3840 0.4813 0.0630  -0.0324 -0.0817 917  GLU A O   
6748  C CB  . GLU A 919  ? 0.4603 0.4366 0.5309 0.0594  -0.0276 -0.0696 917  GLU A CB  
6749  C CG  . GLU A 919  ? 0.5252 0.5045 0.5979 0.0610  -0.0266 -0.0699 917  GLU A CG  
6750  C CD  . GLU A 919  ? 0.6293 0.6014 0.7053 0.0579  -0.0278 -0.0638 917  GLU A CD  
6751  O OE1 . GLU A 919  ? 0.6061 0.5716 0.6818 0.0544  -0.0290 -0.0587 917  GLU A OE1 
6752  O OE2 . GLU A 919  ? 0.7054 0.6791 0.7842 0.0591  -0.0276 -0.0640 917  GLU A OE2 
6753  N N   . THR A 920  ? 0.4281 0.3927 0.5047 0.0562  -0.0342 -0.0705 918  THR A N   
6754  C CA  . THR A 920  ? 0.3894 0.3544 0.4633 0.0559  -0.0344 -0.0721 918  THR A CA  
6755  C C   . THR A 920  ? 0.3593 0.3232 0.4419 0.0585  -0.0391 -0.0795 918  THR A C   
6756  O O   . THR A 920  ? 0.3524 0.3188 0.4329 0.0595  -0.0393 -0.0830 918  THR A O   
6757  C CB  . THR A 920  ? 0.3312 0.2900 0.4020 0.0512  -0.0341 -0.0646 918  THR A CB  
6758  O OG1 . THR A 920  ? 0.3782 0.3294 0.4572 0.0492  -0.0380 -0.0618 918  THR A OG1 
6759  C CG2 . THR A 920  ? 0.3470 0.3077 0.4090 0.0490  -0.0294 -0.0582 918  THR A CG2 
6760  N N   . GLY A 921  ? 0.3734 0.3337 0.4660 0.0597  -0.0430 -0.0820 919  GLY A N   
6761  C CA  . GLY A 921  ? 0.3859 0.3442 0.4881 0.0620  -0.0480 -0.0889 919  GLY A CA  
6762  C C   . GLY A 921  ? 0.3419 0.3085 0.4430 0.0665  -0.0477 -0.0980 919  GLY A C   
6763  O O   . GLY A 921  ? 0.3936 0.3593 0.5005 0.0680  -0.0512 -0.1036 919  GLY A O   
6764  N N   . VAL A 922  ? 0.3642 0.3395 0.4584 0.0687  -0.0435 -0.0997 920  VAL A N   
6765  C CA  . VAL A 922  ? 0.3377 0.3223 0.4300 0.0730  -0.0428 -0.1081 920  VAL A CA  
6766  C C   . VAL A 922  ? 0.3490 0.3368 0.4331 0.0721  -0.0406 -0.1074 920  VAL A C   
6767  O O   . VAL A 922  ? 0.3447 0.3401 0.4275 0.0754  -0.0405 -0.1143 920  VAL A O   
6768  C CB  . VAL A 922  ? 0.3145 0.3082 0.4029 0.0758  -0.0394 -0.1102 920  VAL A CB  
6769  C CG1 . VAL A 922  ? 0.3497 0.3414 0.4478 0.0779  -0.0423 -0.1134 920  VAL A CG1 
6770  C CG2 . VAL A 922  ? 0.3264 0.3210 0.4051 0.0727  -0.0343 -0.1015 920  VAL A CG2 
6771  N N   . GLY A 923  ? 0.3279 0.3106 0.4065 0.0678  -0.0388 -0.0993 921  GLY A N   
6772  C CA  . GLY A 923  ? 0.3064 0.2912 0.3779 0.0666  -0.0370 -0.0981 921  GLY A CA  
6773  C C   . GLY A 923  ? 0.3011 0.2770 0.3761 0.0633  -0.0399 -0.0947 921  GLY A C   
6774  O O   . GLY A 923  ? 0.3316 0.3004 0.4157 0.0624  -0.0440 -0.0947 921  GLY A O   
6775  N N   . THR A 924  ? 0.2833 0.2598 0.3515 0.0613  -0.0380 -0.0917 922  THR A N   
6776  C CA  . THR A 924  ? 0.2794 0.2484 0.3503 0.0580  -0.0404 -0.0883 922  THR A CA  
6777  C C   . THR A 924  ? 0.2824 0.2486 0.3457 0.0538  -0.0369 -0.0791 922  THR A C   
6778  O O   . THR A 924  ? 0.2995 0.2697 0.3544 0.0533  -0.0336 -0.0773 922  THR A O   
6779  C CB  . THR A 924  ? 0.2630 0.2346 0.3336 0.0595  -0.0419 -0.0935 922  THR A CB  
6780  O OG1 . THR A 924  ? 0.2865 0.2666 0.3474 0.0609  -0.0377 -0.0944 922  THR A OG1 
6781  C CG2 . THR A 924  ? 0.3213 0.2941 0.4013 0.0633  -0.0463 -0.1027 922  THR A CG2 
6782  N N   . PHE A 925  ? 0.2803 0.2400 0.3471 0.0510  -0.0379 -0.0736 923  PHE A N   
6783  C CA  . PHE A 925  ? 0.2487 0.2060 0.3090 0.0472  -0.0347 -0.0652 923  PHE A CA  
6784  C C   . PHE A 925  ? 0.2731 0.2228 0.3376 0.0434  -0.0374 -0.0604 923  PHE A C   
6785  O O   . PHE A 925  ? 0.3047 0.2497 0.3785 0.0433  -0.0417 -0.0616 923  PHE A O   
6786  C CB  . PHE A 925  ? 0.2497 0.2071 0.3094 0.0470  -0.0330 -0.0621 923  PHE A CB  
6787  C CG  . PHE A 925  ? 0.2804 0.2456 0.3348 0.0499  -0.0296 -0.0649 923  PHE A CG  
6788  C CD1 . PHE A 925  ? 0.2682 0.2377 0.3271 0.0539  -0.0310 -0.0718 923  PHE A CD1 
6789  C CD2 . PHE A 925  ? 0.2591 0.2279 0.3045 0.0486  -0.0250 -0.0605 923  PHE A CD2 
6790  C CE1 . PHE A 925  ? 0.2824 0.2600 0.3365 0.0564  -0.0277 -0.0741 923  PHE A CE1 
6791  C CE2 . PHE A 925  ? 0.2694 0.2457 0.3102 0.0511  -0.0220 -0.0624 923  PHE A CE2 
6792  C CZ  . PHE A 925  ? 0.2503 0.2312 0.2952 0.0549  -0.0232 -0.0691 923  PHE A CZ  
6793  N N   . VAL A 926  ? 0.2829 0.2320 0.3408 0.0404  -0.0349 -0.0549 924  VAL A N   
6794  C CA  . VAL A 926  ? 0.2776 0.2208 0.3377 0.0364  -0.0363 -0.0490 924  VAL A CA  
6795  C C   . VAL A 926  ? 0.2789 0.2220 0.3329 0.0338  -0.0328 -0.0422 924  VAL A C   
6796  O O   . VAL A 926  ? 0.2937 0.2410 0.3395 0.0341  -0.0289 -0.0413 924  VAL A O   
6797  C CB  . VAL A 926  ? 0.2751 0.2180 0.3331 0.0351  -0.0367 -0.0490 924  VAL A CB  
6798  C CG1 . VAL A 926  ? 0.2925 0.2303 0.3522 0.0308  -0.0377 -0.0423 924  VAL A CG1 
6799  C CG2 . VAL A 926  ? 0.3129 0.2559 0.3775 0.0377  -0.0404 -0.0560 924  VAL A CG2 
6800  N N   . PRO A 927  ? 0.2761 0.2149 0.3338 0.0313  -0.0342 -0.0374 925  PRO A N   
6801  C CA  . PRO A 927  ? 0.3028 0.2421 0.3548 0.0290  -0.0309 -0.0314 925  PRO A CA  
6802  C C   . PRO A 927  ? 0.2866 0.2261 0.3326 0.0263  -0.0289 -0.0274 925  PRO A C   
6803  O O   . PRO A 927  ? 0.3020 0.2392 0.3507 0.0248  -0.0310 -0.0270 925  PRO A O   
6804  C CB  . PRO A 927  ? 0.3510 0.2857 0.4097 0.0269  -0.0337 -0.0275 925  PRO A CB  
6805  C CG  . PRO A 927  ? 0.3746 0.3056 0.4418 0.0267  -0.0383 -0.0293 925  PRO A CG  
6806  C CD  . PRO A 927  ? 0.3199 0.2535 0.3878 0.0304  -0.0389 -0.0369 925  PRO A CD  
6807  N N   . PRO A 928  ? 0.3054 0.2477 0.3437 0.0256  -0.0249 -0.0248 926  PRO A N   
6808  C CA  . PRO A 928  ? 0.3097 0.2519 0.3429 0.0228  -0.0231 -0.0205 926  PRO A CA  
6809  C C   . PRO A 928  ? 0.2626 0.2008 0.3003 0.0194  -0.0255 -0.0159 926  PRO A C   
6810  O O   . PRO A 928  ? 0.2950 0.2311 0.3368 0.0185  -0.0270 -0.0135 926  PRO A O   
6811  C CB  . PRO A 928  ? 0.2869 0.2319 0.3137 0.0226  -0.0192 -0.0179 926  PRO A CB  
6812  C CG  . PRO A 928  ? 0.3237 0.2720 0.3498 0.0261  -0.0183 -0.0224 926  PRO A CG  
6813  C CD  . PRO A 928  ? 0.3259 0.2719 0.3601 0.0276  -0.0220 -0.0258 926  PRO A CD  
6814  N N   . THR A 929  ? 0.2895 0.2270 0.3268 0.0177  -0.0261 -0.0147 927  THR A N   
6815  C CA  . THR A 929  ? 0.2813 0.2155 0.3238 0.0146  -0.0290 -0.0108 927  THR A CA  
6816  C C   . THR A 929  ? 0.2816 0.2173 0.3188 0.0119  -0.0269 -0.0068 927  THR A C   
6817  O O   . THR A 929  ? 0.2840 0.2219 0.3161 0.0127  -0.0248 -0.0087 927  THR A O   
6818  C CB  . THR A 929  ? 0.3238 0.2558 0.3732 0.0156  -0.0328 -0.0145 927  THR A CB  
6819  O OG1 . THR A 929  ? 0.3186 0.2497 0.3731 0.0185  -0.0348 -0.0189 927  THR A OG1 
6820  C CG2 . THR A 929  ? 0.3456 0.2744 0.4013 0.0122  -0.0361 -0.0100 927  THR A CG2 
6821  N N   . ILE A 930  ? 0.2775 0.2123 0.3160 0.0087  -0.0274 -0.0014 928  ILE A N   
6822  C CA  . ILE A 930  ? 0.3074 0.2439 0.3422 0.0059  -0.0260 0.0025  928  ILE A CA  
6823  C C   . ILE A 930  ? 0.2969 0.2313 0.3384 0.0032  -0.0295 0.0055  928  ILE A C   
6824  O O   . ILE A 930  ? 0.3293 0.2617 0.3766 0.0021  -0.0320 0.0081  928  ILE A O   
6825  C CB  . ILE A 930  ? 0.2735 0.2121 0.3036 0.0043  -0.0233 0.0065  928  ILE A CB  
6826  C CG1 . ILE A 930  ? 0.3227 0.2634 0.3465 0.0067  -0.0199 0.0039  928  ILE A CG1 
6827  C CG2 . ILE A 930  ? 0.3391 0.2797 0.3665 0.0012  -0.0224 0.0104  928  ILE A CG2 
6828  C CD1 . ILE A 930  ? 0.3393 0.2815 0.3600 0.0056  -0.0178 0.0071  928  ILE A CD1 
6829  N N   . ILE A 931  ? 0.2876 0.2225 0.3286 0.0022  -0.0298 0.0054  929  ILE A N   
6830  C CA  . ILE A 931  ? 0.3135 0.2469 0.3609 -0.0004 -0.0331 0.0083  929  ILE A CA  
6831  C C   . ILE A 931  ? 0.3597 0.2964 0.4029 -0.0033 -0.0312 0.0125  929  ILE A C   
6832  O O   . ILE A 931  ? 0.3330 0.2717 0.3705 -0.0026 -0.0288 0.0106  929  ILE A O   
6833  C CB  . ILE A 931  ? 0.3653 0.2966 0.4172 0.0013  -0.0357 0.0038  929  ILE A CB  
6834  C CG1 . ILE A 931  ? 0.3629 0.2916 0.4194 0.0045  -0.0377 -0.0011 929  ILE A CG1 
6835  C CG2 . ILE A 931  ? 0.3529 0.2827 0.4117 -0.0017 -0.0392 0.0072  929  ILE A CG2 
6836  C CD1 . ILE A 931  ? 0.3624 0.2892 0.4243 0.0062  -0.0408 -0.0061 929  ILE A CD1 
6837  N N   . GLU A 932  ? 0.3292 0.2667 0.3752 -0.0065 -0.0324 0.0182  930  GLU A N   
6838  C CA  . GLU A 932  ? 0.3354 0.2769 0.3777 -0.0093 -0.0306 0.0223  930  GLU A CA  
6839  C C   . GLU A 932  ? 0.2805 0.2216 0.3277 -0.0112 -0.0332 0.0235  930  GLU A C   
6840  O O   . GLU A 932  ? 0.3487 0.2876 0.4038 -0.0128 -0.0369 0.0261  930  GLU A O   
6841  C CB  . GLU A 932  ? 0.3073 0.2512 0.3496 -0.0119 -0.0304 0.0278  930  GLU A CB  
6842  C CG  . GLU A 932  ? 0.3228 0.2675 0.3596 -0.0101 -0.0275 0.0265  930  GLU A CG  
6843  C CD  . GLU A 932  ? 0.4060 0.3526 0.4440 -0.0123 -0.0279 0.0314  930  GLU A CD  
6844  O OE1 . GLU A 932  ? 0.3799 0.3303 0.4176 -0.0153 -0.0279 0.0361  930  GLU A OE1 
6845  O OE2 . GLU A 932  ? 0.3876 0.3323 0.4268 -0.0109 -0.0283 0.0307  930  GLU A OE2 
6846  N N   . LEU A 933  ? 0.3395 0.2826 0.3826 -0.0110 -0.0314 0.0218  931  LEU A N   
6847  C CA  . LEU A 933  ? 0.3454 0.2884 0.3925 -0.0125 -0.0336 0.0225  931  LEU A CA  
6848  C C   . LEU A 933  ? 0.4318 0.3797 0.4773 -0.0160 -0.0325 0.0279  931  LEU A C   
6849  O O   . LEU A 933  ? 0.3861 0.3378 0.4255 -0.0166 -0.0294 0.0295  931  LEU A O   
6850  C CB  . LEU A 933  ? 0.3866 0.3290 0.4306 -0.0100 -0.0326 0.0170  931  LEU A CB  
6851  C CG  . LEU A 933  ? 0.3917 0.3305 0.4373 -0.0064 -0.0337 0.0110  931  LEU A CG  
6852  C CD1 . LEU A 933  ? 0.4647 0.4040 0.5075 -0.0045 -0.0329 0.0065  931  LEU A CD1 
6853  C CD2 . LEU A 933  ? 0.4605 0.3953 0.5159 -0.0068 -0.0383 0.0113  931  LEU A CD2 
6854  N N   . GLU A 934  ? 0.4203 0.3683 0.4714 -0.0183 -0.0352 0.0304  932  GLU A N   
6855  C CA  . GLU A 934  ? 0.5321 0.4853 0.5822 -0.0216 -0.0344 0.0351  932  GLU A CA  
6856  C C   . GLU A 934  ? 0.5176 0.4732 0.5623 -0.0207 -0.0319 0.0320  932  GLU A C   
6857  O O   . GLU A 934  ? 0.6039 0.5645 0.6429 -0.0216 -0.0289 0.0334  932  GLU A O   
6858  C CB  . GLU A 934  ? 0.5582 0.5108 0.6176 -0.0247 -0.0386 0.0396  932  GLU A CB  
6859  N N   . LYS A 935  ? 0.5374 0.4896 0.5841 -0.0189 -0.0333 0.0277  933  LYS A N   
6860  C CA  . LYS A 935  ? 0.5431 0.4972 0.5852 -0.0178 -0.0313 0.0246  933  LYS A CA  
6861  C C   . LYS A 935  ? 0.6066 0.5570 0.6466 -0.0139 -0.0310 0.0181  933  LYS A C   
6862  O O   . LYS A 935  ? 0.5535 0.4999 0.5977 -0.0123 -0.0333 0.0157  933  LYS A O   
6863  C CB  . LYS A 935  ? 0.5777 0.5328 0.6249 -0.0202 -0.0336 0.0266  933  LYS A CB  
6864  N N   . LEU A 936  ? 0.5759 0.5284 0.6098 -0.0123 -0.0283 0.0151  934  LEU A N   
6865  C CA  . LEU A 936  ? 0.5958 0.5459 0.6272 -0.0087 -0.0278 0.0093  934  LEU A CA  
6866  C C   . LEU A 936  ? 0.6218 0.5691 0.6593 -0.0081 -0.0314 0.0065  934  LEU A C   
6867  O O   . LEU A 936  ? 0.6127 0.5576 0.6507 -0.0052 -0.0322 0.0016  934  LEU A O   
6868  C CB  . LEU A 936  ? 0.5411 0.4944 0.5651 -0.0074 -0.0244 0.0074  934  LEU A CB  
6869  C CG  . LEU A 936  ? 0.6013 0.5540 0.6198 -0.0042 -0.0220 0.0037  934  LEU A CG  
6870  C CD1 . LEU A 936  ? 0.5062 0.4623 0.5180 -0.0037 -0.0186 0.0036  934  LEU A CD1 
6871  C CD2 . LEU A 936  ? 0.5640 0.5144 0.5841 -0.0013 -0.0236 -0.0013 934  LEU A CD2 
6872  N N   . SER A 937  ? 0.6488 0.5967 0.6914 -0.0109 -0.0335 0.0095  935  SER A N   
6873  C CA  . SER A 937  ? 0.6488 0.5938 0.6984 -0.0107 -0.0374 0.0071  935  SER A CA  
6874  C C   . SER A 937  ? 0.6082 0.5488 0.6651 -0.0101 -0.0409 0.0064  935  SER A C   
6875  O O   . SER A 937  ? 0.6700 0.6078 0.7332 -0.0093 -0.0443 0.0033  935  SER A O   
6876  C CB  . SER A 937  ? 0.6596 0.6066 0.7132 -0.0141 -0.0389 0.0112  935  SER A CB  
6877  O OG  . SER A 937  ? 0.7156 0.6653 0.7699 -0.0174 -0.0383 0.0176  935  SER A OG  
6878  N N   . ASP A 938  ? 0.6362 0.5762 0.6928 -0.0105 -0.0403 0.0089  936  ASP A N   
6879  C CA  . ASP A 938  ? 0.6128 0.5487 0.6763 -0.0096 -0.0435 0.0077  936  ASP A CA  
6880  C C   . ASP A 938  ? 0.6645 0.5984 0.7267 -0.0053 -0.0436 0.0004  936  ASP A C   
6881  O O   . ASP A 938  ? 0.6377 0.5681 0.7064 -0.0040 -0.0468 -0.0020 936  ASP A O   
6882  C CB  . ASP A 938  ? 0.6784 0.6147 0.7410 -0.0107 -0.0425 0.0119  936  ASP A CB  
6883  C CG  . ASP A 938  ? 0.6959 0.6349 0.7608 -0.0150 -0.0429 0.0193  936  ASP A CG  
6884  O OD1 . ASP A 938  ? 0.7507 0.6910 0.8182 -0.0172 -0.0441 0.0213  936  ASP A OD1 
6885  O OD2 . ASP A 938  ? 0.6612 0.6012 0.7251 -0.0162 -0.0420 0.0231  936  ASP A OD2 
6886  N N   . LEU A 939  ? 0.5919 0.5282 0.6461 -0.0031 -0.0403 -0.0030 937  LEU A N   
6887  C CA  . LEU A 939  ? 0.5559 0.4916 0.6081 0.0009  -0.0401 -0.0096 937  LEU A CA  
6888  C C   . LEU A 939  ? 0.6268 0.5626 0.6809 0.0020  -0.0418 -0.0137 937  LEU A C   
6889  O O   . LEU A 939  ? 0.6359 0.5738 0.6878 0.0004  -0.0409 -0.0120 937  LEU A O   
6890  C CB  . LEU A 939  ? 0.5073 0.4460 0.5498 0.0028  -0.0355 -0.0106 937  LEU A CB  
6891  C CG  . LEU A 939  ? 0.4971 0.4358 0.5372 0.0026  -0.0335 -0.0080 937  LEU A CG  
6892  C CD1 . LEU A 939  ? 0.4990 0.4404 0.5310 0.0052  -0.0297 -0.0104 937  LEU A CD1 
6893  C CD2 . LEU A 939  ? 0.5331 0.4684 0.5802 0.0033  -0.0366 -0.0090 937  LEU A CD2 
6894  N N   . GLN A 940  ? 0.5314 0.4654 0.5897 0.0048  -0.0444 -0.0194 938  GLN A N   
6895  C CA  . GLN A 940  ? 0.5666 0.5010 0.6269 0.0061  -0.0464 -0.0241 938  GLN A CA  
6896  C C   . GLN A 940  ? 0.6010 0.5387 0.6537 0.0098  -0.0436 -0.0294 938  GLN A C   
6897  O O   . GLN A 940  ? 0.6908 0.6315 0.7375 0.0097  -0.0412 -0.0291 938  GLN A O   
6898  C CB  . GLN A 940  ? 0.5519 0.4825 0.6229 0.0067  -0.0516 -0.0273 938  GLN A CB  
6899  N N   . ARG A 941  ? 0.5777 0.5155 0.6309 0.0129  -0.0440 -0.0340 939  ARG A N   
6900  C CA  . ARG A 941  ? 0.4788 0.4205 0.5254 0.0165  -0.0417 -0.0390 939  ARG A CA  
6901  C C   . ARG A 941  ? 0.3879 0.3311 0.4291 0.0177  -0.0385 -0.0380 939  ARG A C   
6902  O O   . ARG A 941  ? 0.4461 0.3869 0.4895 0.0163  -0.0385 -0.0345 939  ARG A O   
6903  C CB  . ARG A 941  ? 0.5348 0.4767 0.5864 0.0196  -0.0451 -0.0464 939  ARG A CB  
6904  N N   . GLU A 942  ? 0.3708 0.3183 0.4050 0.0204  -0.0357 -0.0409 940  GLU A N   
6905  C CA  . GLU A 942  ? 0.3266 0.2762 0.3559 0.0219  -0.0327 -0.0405 940  GLU A CA  
6906  C C   . GLU A 942  ? 0.3050 0.2526 0.3400 0.0235  -0.0350 -0.0433 940  GLU A C   
6907  O O   . GLU A 942  ? 0.3336 0.2809 0.3739 0.0256  -0.0381 -0.0487 940  GLU A O   
6908  C CB  . GLU A 942  ? 0.3587 0.3137 0.3813 0.0248  -0.0303 -0.0441 940  GLU A CB  
6909  C CG  . GLU A 942  ? 0.3315 0.2896 0.3491 0.0267  -0.0273 -0.0442 940  GLU A CG  
6910  C CD  . GLU A 942  ? 0.3287 0.2929 0.3413 0.0298  -0.0258 -0.0482 940  GLU A CD  
6911  O OE1 . GLU A 942  ? 0.3587 0.3245 0.3742 0.0320  -0.0283 -0.0538 940  GLU A OE1 
6912  O OE2 . GLU A 942  ? 0.2848 0.2523 0.2907 0.0300  -0.0224 -0.0458 940  GLU A OE2 
6913  N N   . VAL A 943  ? 0.3150 0.2613 0.3493 0.0227  -0.0335 -0.0399 941  VAL A N   
6914  C CA  . VAL A 943  ? 0.3005 0.2453 0.3397 0.0243  -0.0352 -0.0421 941  VAL A CA  
6915  C C   . VAL A 943  ? 0.3300 0.2789 0.3626 0.0266  -0.0316 -0.0431 941  VAL A C   
6916  O O   . VAL A 943  ? 0.2974 0.2466 0.3252 0.0251  -0.0286 -0.0385 941  VAL A O   
6917  C CB  . VAL A 943  ? 0.3444 0.2845 0.3888 0.0213  -0.0368 -0.0370 941  VAL A CB  
6918  C CG1 . VAL A 943  ? 0.3742 0.3127 0.4240 0.0231  -0.0386 -0.0394 941  VAL A CG1 
6919  C CG2 . VAL A 943  ? 0.3738 0.3104 0.4247 0.0187  -0.0402 -0.0353 941  VAL A CG2 
6920  N N   . PHE A 944  ? 0.3002 0.2527 0.3327 0.0302  -0.0320 -0.0492 942  PHE A N   
6921  C CA  . PHE A 944  ? 0.2780 0.2360 0.3036 0.0324  -0.0285 -0.0503 942  PHE A CA  
6922  C C   . PHE A 944  ? 0.2762 0.2337 0.3040 0.0336  -0.0284 -0.0507 942  PHE A C   
6923  O O   . PHE A 944  ? 0.3004 0.2605 0.3307 0.0367  -0.0295 -0.0560 942  PHE A O   
6924  C CB  . PHE A 944  ? 0.2743 0.2377 0.2982 0.0357  -0.0288 -0.0565 942  PHE A CB  
6925  C CG  . PHE A 944  ? 0.2519 0.2217 0.2675 0.0373  -0.0249 -0.0562 942  PHE A CG  
6926  C CD1 . PHE A 944  ? 0.2452 0.2160 0.2546 0.0355  -0.0221 -0.0518 942  PHE A CD1 
6927  C CD2 . PHE A 944  ? 0.2562 0.2315 0.2707 0.0406  -0.0242 -0.0605 942  PHE A CD2 
6928  C CE1 . PHE A 944  ? 0.2333 0.2101 0.2359 0.0368  -0.0188 -0.0512 942  PHE A CE1 
6929  C CE2 . PHE A 944  ? 0.2562 0.2380 0.2634 0.0419  -0.0206 -0.0597 942  PHE A CE2 
6930  C CZ  . PHE A 944  ? 0.2481 0.2304 0.2496 0.0399  -0.0180 -0.0548 942  PHE A CZ  
6931  N N   . GLY A 945  ? 0.2717 0.2261 0.2988 0.0310  -0.0271 -0.0450 943  GLY A N   
6932  C CA  . GLY A 945  ? 0.2892 0.2426 0.3187 0.0316  -0.0271 -0.0445 943  GLY A CA  
6933  C C   . GLY A 945  ? 0.2830 0.2344 0.3094 0.0287  -0.0247 -0.0378 943  GLY A C   
6934  O O   . GLY A 945  ? 0.2783 0.2298 0.3003 0.0265  -0.0229 -0.0340 943  GLY A O   
6935  N N   . PRO A 946  ? 0.2643 0.2143 0.2931 0.0287  -0.0249 -0.0366 944  PRO A N   
6936  C CA  . PRO A 946  ? 0.2842 0.2332 0.3095 0.0263  -0.0224 -0.0307 944  PRO A CA  
6937  C C   . PRO A 946  ? 0.2732 0.2176 0.3023 0.0228  -0.0242 -0.0260 944  PRO A C   
6938  O O   . PRO A 946  ? 0.2864 0.2283 0.3189 0.0216  -0.0252 -0.0233 944  PRO A O   
6939  C CB  . PRO A 946  ? 0.2646 0.2146 0.2913 0.0282  -0.0220 -0.0321 944  PRO A CB  
6940  C CG  . PRO A 946  ? 0.2923 0.2406 0.3270 0.0301  -0.0260 -0.0370 944  PRO A CG  
6941  C CD  . PRO A 946  ? 0.2633 0.2132 0.2979 0.0313  -0.0271 -0.0410 944  PRO A CD  
6942  N N   . VAL A 947  ? 0.2914 0.2350 0.3201 0.0210  -0.0248 -0.0247 945  VAL A N   
6943  C CA  . VAL A 947  ? 0.2942 0.2341 0.3271 0.0176  -0.0270 -0.0205 945  VAL A CA  
6944  C C   . VAL A 947  ? 0.2919 0.2333 0.3191 0.0152  -0.0244 -0.0164 945  VAL A C   
6945  O O   . VAL A 947  ? 0.2744 0.2171 0.2993 0.0154  -0.0241 -0.0178 945  VAL A O   
6946  C CB  . VAL A 947  ? 0.3276 0.2649 0.3678 0.0177  -0.0311 -0.0231 945  VAL A CB  
6947  C CG1 . VAL A 947  ? 0.3329 0.2670 0.3778 0.0140  -0.0333 -0.0179 945  VAL A CG1 
6948  C CG2 . VAL A 947  ? 0.2976 0.2339 0.3440 0.0205  -0.0338 -0.0279 945  VAL A CG2 
6949  N N   . LEU A 948  ? 0.2691 0.2103 0.2942 0.0130  -0.0229 -0.0117 946  LEU A N   
6950  C CA  . LEU A 948  ? 0.2555 0.1983 0.2757 0.0107  -0.0206 -0.0079 946  LEU A CA  
6951  C C   . LEU A 948  ? 0.2833 0.2242 0.3078 0.0074  -0.0228 -0.0039 946  LEU A C   
6952  O O   . LEU A 948  ? 0.3141 0.2531 0.3433 0.0061  -0.0247 -0.0014 946  LEU A O   
6953  C CB  . LEU A 948  ? 0.2777 0.2221 0.2932 0.0104  -0.0176 -0.0054 946  LEU A CB  
6954  C CG  . LEU A 948  ? 0.2508 0.1970 0.2619 0.0081  -0.0154 -0.0018 946  LEU A CG  
6955  C CD1 . LEU A 948  ? 0.2606 0.2089 0.2674 0.0092  -0.0138 -0.0040 946  LEU A CD1 
6956  C CD2 . LEU A 948  ? 0.2923 0.2397 0.3002 0.0077  -0.0131 0.0005  946  LEU A CD2 
6957  N N   . HIS A 949  ? 0.2802 0.2223 0.3033 0.0060  -0.0225 -0.0030 947  HIS A N   
6958  C CA  . HIS A 949  ? 0.2786 0.2201 0.3051 0.0026  -0.0242 0.0013  947  HIS A CA  
6959  C C   . HIS A 949  ? 0.2809 0.2255 0.3019 0.0006  -0.0212 0.0051  947  HIS A C   
6960  O O   . HIS A 949  ? 0.2825 0.2293 0.2976 0.0018  -0.0183 0.0036  947  HIS A O   
6961  C CB  . HIS A 949  ? 0.3079 0.2488 0.3374 0.0023  -0.0263 -0.0003 947  HIS A CB  
6962  C CG  . HIS A 949  ? 0.2963 0.2346 0.3310 0.0047  -0.0292 -0.0049 947  HIS A CG  
6963  N ND1 . HIS A 949  ? 0.2910 0.2304 0.3228 0.0080  -0.0282 -0.0103 947  HIS A ND1 
6964  C CD2 . HIS A 949  ? 0.3517 0.2868 0.3947 0.0043  -0.0331 -0.0052 947  HIS A CD2 
6965  C CE1 . HIS A 949  ? 0.3259 0.2630 0.3637 0.0097  -0.0314 -0.0141 947  HIS A CE1 
6966  N NE2 . HIS A 949  ? 0.3378 0.2720 0.3828 0.0075  -0.0345 -0.0112 947  HIS A NE2 
6967  N N   . VAL A 950  ? 0.2711 0.2162 0.2944 -0.0023 -0.0220 0.0098  948  VAL A N   
6968  C CA  . VAL A 950  ? 0.2875 0.2361 0.3062 -0.0041 -0.0195 0.0132  948  VAL A CA  
6969  C C   . VAL A 950  ? 0.3237 0.2741 0.3447 -0.0073 -0.0207 0.0169  948  VAL A C   
6970  O O   . VAL A 950  ? 0.3433 0.2924 0.3703 -0.0091 -0.0236 0.0196  948  VAL A O   
6971  C CB  . VAL A 950  ? 0.2936 0.2425 0.3119 -0.0047 -0.0188 0.0156  948  VAL A CB  
6972  C CG1 . VAL A 950  ? 0.2989 0.2520 0.3127 -0.0066 -0.0164 0.0187  948  VAL A CG1 
6973  C CG2 . VAL A 950  ? 0.2991 0.2465 0.3153 -0.0016 -0.0176 0.0121  948  VAL A CG2 
6974  N N   . ILE A 951  ? 0.2828 0.2364 0.2994 -0.0079 -0.0185 0.0171  949  ILE A N   
6975  C CA  . ILE A 951  ? 0.3019 0.2587 0.3199 -0.0110 -0.0191 0.0208  949  ILE A CA  
6976  C C   . ILE A 951  ? 0.3184 0.2799 0.3312 -0.0120 -0.0162 0.0227  949  ILE A C   
6977  O O   . ILE A 951  ? 0.2864 0.2483 0.2943 -0.0102 -0.0136 0.0204  949  ILE A O   
6978  C CB  . ILE A 951  ? 0.3445 0.3012 0.3634 -0.0109 -0.0199 0.0190  949  ILE A CB  
6979  C CG1 . ILE A 951  ? 0.3428 0.3008 0.3556 -0.0088 -0.0170 0.0155  949  ILE A CG1 
6980  C CG2 . ILE A 951  ? 0.4098 0.3620 0.4344 -0.0098 -0.0231 0.0167  949  ILE A CG2 
6981  C CD1 . ILE A 951  ? 0.5097 0.4682 0.5232 -0.0088 -0.0177 0.0139  949  ILE A CD1 
6982  N N   . ARG A 952  ? 0.2965 0.2618 0.3107 -0.0150 -0.0167 0.0269  950  ARG A N   
6983  C CA  . ARG A 952  ? 0.2695 0.2402 0.2795 -0.0162 -0.0142 0.0287  950  ARG A CA  
6984  C C   . ARG A 952  ? 0.2682 0.2431 0.2771 -0.0175 -0.0135 0.0291  950  ARG A C   
6985  O O   . ARG A 952  ? 0.3002 0.2747 0.3130 -0.0188 -0.0155 0.0303  950  ARG A O   
6986  C CB  . ARG A 952  ? 0.3045 0.2779 0.3170 -0.0188 -0.0154 0.0336  950  ARG A CB  
6987  C CG  . ARG A 952  ? 0.3161 0.2852 0.3310 -0.0178 -0.0167 0.0337  950  ARG A CG  
6988  C CD  . ARG A 952  ? 0.3642 0.3353 0.3836 -0.0208 -0.0189 0.0391  950  ARG A CD  
6989  N NE  . ARG A 952  ? 0.3928 0.3695 0.4087 -0.0221 -0.0171 0.0416  950  ARG A NE  
6990  C CZ  . ARG A 952  ? 0.4044 0.3808 0.4196 -0.0217 -0.0168 0.0423  950  ARG A CZ  
6991  N NH1 . ARG A 952  ? 0.3967 0.3674 0.4145 -0.0200 -0.0182 0.0409  950  ARG A NH1 
6992  N NH2 . ARG A 952  ? 0.3702 0.3524 0.3822 -0.0229 -0.0152 0.0443  950  ARG A NH2 
6993  N N   . TYR A 953  ? 0.2655 0.2445 0.2695 -0.0172 -0.0108 0.0281  951  TYR A N   
6994  C CA  . TYR A 953  ? 0.2717 0.2550 0.2746 -0.0182 -0.0100 0.0282  951  TYR A CA  
6995  C C   . TYR A 953  ? 0.2489 0.2389 0.2485 -0.0193 -0.0078 0.0293  951  TYR A C   
6996  O O   . TYR A 953  ? 0.2712 0.2614 0.2679 -0.0181 -0.0063 0.0281  951  TYR A O   
6997  C CB  . TYR A 953  ? 0.2526 0.2335 0.2534 -0.0158 -0.0090 0.0238  951  TYR A CB  
6998  C CG  . TYR A 953  ? 0.2455 0.2263 0.2414 -0.0134 -0.0064 0.0207  951  TYR A CG  
6999  C CD1 . TYR A 953  ? 0.2438 0.2202 0.2386 -0.0112 -0.0061 0.0187  951  TYR A CD1 
7000  C CD2 . TYR A 953  ? 0.2580 0.2435 0.2509 -0.0134 -0.0043 0.0198  951  TYR A CD2 
7001  C CE1 . TYR A 953  ? 0.2447 0.2213 0.2357 -0.0093 -0.0039 0.0164  951  TYR A CE1 
7002  C CE2 . TYR A 953  ? 0.2337 0.2189 0.2230 -0.0114 -0.0023 0.0171  951  TYR A CE2 
7003  C CZ  . TYR A 953  ? 0.2397 0.2204 0.2282 -0.0094 -0.0021 0.0156  951  TYR A CZ  
7004  O OH  . TYR A 953  ? 0.2578 0.2384 0.2433 -0.0076 -0.0002 0.0134  951  TYR A OH  
7005  N N   . ARG A 954  ? 0.2914 0.2872 0.2917 -0.0214 -0.0078 0.0314  952  ARG A N   
7006  C CA  . ARG A 954  ? 0.3054 0.3085 0.3026 -0.0221 -0.0057 0.0316  952  ARG A CA  
7007  C C   . ARG A 954  ? 0.2490 0.2523 0.2428 -0.0199 -0.0037 0.0271  952  ARG A C   
7008  O O   . ARG A 954  ? 0.2680 0.2684 0.2625 -0.0190 -0.0041 0.0253  952  ARG A O   
7009  C CB  . ARG A 954  ? 0.3494 0.3596 0.3490 -0.0254 -0.0065 0.0358  952  ARG A CB  
7010  C CG  . ARG A 954  ? 0.4058 0.4157 0.4099 -0.0279 -0.0090 0.0409  952  ARG A CG  
7011  C CD  . ARG A 954  ? 0.5921 0.6110 0.5960 -0.0306 -0.0087 0.0451  952  ARG A CD  
7012  N NE  . ARG A 954  ? 0.6146 0.6349 0.6154 -0.0298 -0.0074 0.0444  952  ARG A NE  
7013  C CZ  . ARG A 954  ? 0.6438 0.6653 0.6461 -0.0314 -0.0086 0.0482  952  ARG A CZ  
7014  N NH1 . ARG A 954  ? 0.6734 0.6950 0.6807 -0.0339 -0.0112 0.0534  952  ARG A NH1 
7015  N NH2 . ARG A 954  ? 0.5981 0.6208 0.5973 -0.0303 -0.0073 0.0469  952  ARG A NH2 
7016  N N   . ARG A 955  ? 0.2973 0.3039 0.2877 -0.0189 -0.0016 0.0252  953  ARG A N   
7017  C CA  . ARG A 955  ? 0.3146 0.3207 0.3024 -0.0166 0.0001  0.0209  953  ARG A CA  
7018  C C   . ARG A 955  ? 0.2598 0.2687 0.2482 -0.0170 0.0002  0.0202  953  ARG A C   
7019  O O   . ARG A 955  ? 0.3117 0.3173 0.2994 -0.0151 0.0006  0.0174  953  ARG A O   
7020  C CB  . ARG A 955  ? 0.3840 0.3945 0.3693 -0.0160 0.0019  0.0193  953  ARG A CB  
7021  C CG  . ARG A 955  ? 0.4735 0.4841 0.4568 -0.0137 0.0035  0.0150  953  ARG A CG  
7022  C CD  . ARG A 955  ? 0.5191 0.5221 0.5022 -0.0114 0.0033  0.0130  953  ARG A CD  
7023  N NE  . ARG A 955  ? 0.6027 0.6052 0.5845 -0.0092 0.0045  0.0095  953  ARG A NE  
7024  C CZ  . ARG A 955  ? 0.5299 0.5327 0.5120 -0.0087 0.0046  0.0082  953  ARG A CZ  
7025  N NH1 . ARG A 955  ? 0.4289 0.4332 0.4124 -0.0102 0.0036  0.0098  953  ARG A NH1 
7026  N NH2 . ARG A 955  ? 0.5188 0.5205 0.5000 -0.0066 0.0055  0.0053  953  ARG A NH2 
7027  N N   . ASP A 956  ? 0.2900 0.3054 0.2799 -0.0195 -0.0002 0.0231  954  ASP A N   
7028  C CA  . ASP A 956  ? 0.2888 0.3075 0.2795 -0.0200 0.0000  0.0224  954  ASP A CA  
7029  C C   . ASP A 956  ? 0.3103 0.3232 0.3034 -0.0199 -0.0018 0.0227  954  ASP A C   
7030  O O   . ASP A 956  ? 0.3207 0.3347 0.3142 -0.0196 -0.0016 0.0213  954  ASP A O   
7031  C CB  . ASP A 956  ? 0.2930 0.3207 0.2849 -0.0229 -0.0001 0.0258  954  ASP A CB  
7032  C CG  . ASP A 956  ? 0.3448 0.3800 0.3341 -0.0228 0.0018  0.0245  954  ASP A CG  
7033  O OD1 . ASP A 956  ? 0.3864 0.4197 0.3734 -0.0203 0.0031  0.0204  954  ASP A OD1 
7034  O OD2 . ASP A 956  ? 0.4572 0.5004 0.4472 -0.0252 0.0017  0.0276  954  ASP A OD2 
7035  N N   . ASP A 957  ? 0.2735 0.2807 0.2686 -0.0200 -0.0035 0.0242  955  ASP A N   
7036  C CA  . ASP A 957  ? 0.2932 0.2949 0.2910 -0.0197 -0.0054 0.0240  955  ASP A CA  
7037  C C   . ASP A 957  ? 0.2857 0.2808 0.2815 -0.0165 -0.0050 0.0200  955  ASP A C   
7038  O O   . ASP A 957  ? 0.2964 0.2866 0.2944 -0.0159 -0.0067 0.0193  955  ASP A O   
7039  C CB  . ASP A 957  ? 0.3210 0.3206 0.3231 -0.0217 -0.0079 0.0278  955  ASP A CB  
7040  C CG  . ASP A 957  ? 0.4173 0.4237 0.4220 -0.0252 -0.0087 0.0325  955  ASP A CG  
7041  O OD1 . ASP A 957  ? 0.4069 0.4187 0.4114 -0.0261 -0.0079 0.0326  955  ASP A OD1 
7042  O OD2 . ASP A 957  ? 0.4313 0.4382 0.4386 -0.0270 -0.0100 0.0363  955  ASP A OD2 
7043  N N   . LEU A 958  ? 0.2634 0.2589 0.2556 -0.0146 -0.0029 0.0173  956  LEU A N   
7044  C CA  . LEU A 958  ? 0.2532 0.2432 0.2436 -0.0117 -0.0025 0.0141  956  LEU A CA  
7045  C C   . LEU A 958  ? 0.2728 0.2609 0.2637 -0.0106 -0.0031 0.0121  956  LEU A C   
7046  O O   . LEU A 958  ? 0.2580 0.2414 0.2493 -0.0091 -0.0041 0.0106  956  LEU A O   
7047  C CB  . LEU A 958  ? 0.2803 0.2716 0.2674 -0.0100 -0.0003 0.0120  956  LEU A CB  
7048  C CG  . LEU A 958  ? 0.2665 0.2532 0.2517 -0.0072 0.0003  0.0091  956  LEU A CG  
7049  C CD1 . LEU A 958  ? 0.2699 0.2516 0.2557 -0.0064 -0.0007 0.0094  956  LEU A CD1 
7050  C CD2 . LEU A 958  ? 0.3132 0.3015 0.2961 -0.0059 0.0022  0.0075  956  LEU A CD2 
7051  N N   . ASP A 959  ? 0.2309 0.2232 0.2219 -0.0114 -0.0027 0.0120  957  ASP A N   
7052  C CA  . ASP A 959  ? 0.2555 0.2464 0.2470 -0.0104 -0.0033 0.0101  957  ASP A CA  
7053  C C   . ASP A 959  ? 0.2559 0.2439 0.2510 -0.0115 -0.0058 0.0113  957  ASP A C   
7054  O O   . ASP A 959  ? 0.2638 0.2481 0.2592 -0.0099 -0.0068 0.0091  957  ASP A O   
7055  C CB  . ASP A 959  ? 0.2650 0.2613 0.2563 -0.0111 -0.0024 0.0098  957  ASP A CB  
7056  C CG  . ASP A 959  ? 0.3161 0.3108 0.3071 -0.0095 -0.0026 0.0073  957  ASP A CG  
7057  O OD1 . ASP A 959  ? 0.3057 0.2972 0.2946 -0.0071 -0.0019 0.0050  957  ASP A OD1 
7058  O OD2 . ASP A 959  ? 0.3849 0.3818 0.3780 -0.0107 -0.0035 0.0079  957  ASP A OD2 
7059  N N   . ARG A 960  ? 0.2538 0.2438 0.2520 -0.0141 -0.0070 0.0147  958  ARG A N   
7060  C CA  . ARG A 960  ? 0.2927 0.2797 0.2954 -0.0153 -0.0098 0.0161  958  ARG A CA  
7061  C C   . ARG A 960  ? 0.2709 0.2518 0.2739 -0.0134 -0.0109 0.0144  958  ARG A C   
7062  O O   . ARG A 960  ? 0.3002 0.2774 0.3057 -0.0126 -0.0128 0.0128  958  ARG A O   
7063  C CB  . ARG A 960  ? 0.2946 0.2852 0.3008 -0.0187 -0.0109 0.0208  958  ARG A CB  
7064  C CG  . ARG A 960  ? 0.3404 0.3284 0.3525 -0.0204 -0.0142 0.0229  958  ARG A CG  
7065  C CD  . ARG A 960  ? 0.5050 0.4882 0.5195 -0.0202 -0.0159 0.0237  958  ARG A CD  
7066  N NE  . ARG A 960  ? 0.5107 0.4958 0.5225 -0.0204 -0.0142 0.0253  958  ARG A NE  
7067  C CZ  . ARG A 960  ? 0.5324 0.5135 0.5441 -0.0192 -0.0146 0.0248  958  ARG A CZ  
7068  N NH1 . ARG A 960  ? 0.5523 0.5277 0.5666 -0.0177 -0.0166 0.0228  958  ARG A NH1 
7069  N NH2 . ARG A 960  ? 0.5651 0.5485 0.5742 -0.0195 -0.0130 0.0262  958  ARG A NH2 
7070  N N   . LEU A 961  ? 0.2542 0.2344 0.2549 -0.0127 -0.0096 0.0145  959  LEU A N   
7071  C CA  . LEU A 961  ? 0.2645 0.2396 0.2653 -0.0108 -0.0103 0.0129  959  LEU A CA  
7072  C C   . LEU A 961  ? 0.2707 0.2432 0.2692 -0.0079 -0.0099 0.0089  959  LEU A C   
7073  O O   . LEU A 961  ? 0.2667 0.2355 0.2670 -0.0066 -0.0115 0.0070  959  LEU A O   
7074  C CB  . LEU A 961  ? 0.2560 0.2316 0.2544 -0.0106 -0.0088 0.0138  959  LEU A CB  
7075  C CG  . LEU A 961  ? 0.2560 0.2270 0.2538 -0.0083 -0.0090 0.0118  959  LEU A CG  
7076  C CD1 . LEU A 961  ? 0.3474 0.3151 0.3503 -0.0091 -0.0119 0.0128  959  LEU A CD1 
7077  C CD2 . LEU A 961  ? 0.3074 0.2794 0.3025 -0.0080 -0.0071 0.0125  959  LEU A CD2 
7078  N N   . VAL A 962  ? 0.2455 0.2202 0.2403 -0.0067 -0.0077 0.0074  960  VAL A N   
7079  C CA  . VAL A 962  ? 0.2586 0.2316 0.2513 -0.0041 -0.0073 0.0041  960  VAL A CA  
7080  C C   . VAL A 962  ? 0.2929 0.2648 0.2883 -0.0042 -0.0095 0.0029  960  VAL A C   
7081  O O   . VAL A 962  ? 0.2625 0.2319 0.2580 -0.0022 -0.0104 0.0003  960  VAL A O   
7082  C CB  . VAL A 962  ? 0.2627 0.2383 0.2517 -0.0031 -0.0050 0.0031  960  VAL A CB  
7083  C CG1 . VAL A 962  ? 0.2994 0.2738 0.2867 -0.0006 -0.0048 0.0003  960  VAL A CG1 
7084  C CG2 . VAL A 962  ? 0.2976 0.2735 0.2843 -0.0026 -0.0032 0.0037  960  VAL A CG2 
7085  N N   . ASP A 963  ? 0.2862 0.2606 0.2841 -0.0065 -0.0103 0.0047  961  ASP A N   
7086  C CA  . ASP A 963  ? 0.2798 0.2532 0.2813 -0.0069 -0.0127 0.0039  961  ASP A CA  
7087  C C   . ASP A 963  ? 0.2986 0.2680 0.3040 -0.0067 -0.0152 0.0035  961  ASP A C   
7088  O O   . ASP A 963  ? 0.3236 0.2907 0.3305 -0.0053 -0.0169 0.0006  961  ASP A O   
7089  C CB  . ASP A 963  ? 0.3063 0.2832 0.3106 -0.0098 -0.0133 0.0068  961  ASP A CB  
7090  C CG  . ASP A 963  ? 0.3734 0.3545 0.3749 -0.0097 -0.0113 0.0064  961  ASP A CG  
7091  O OD1 . ASP A 963  ? 0.5233 0.5039 0.5216 -0.0074 -0.0102 0.0036  961  ASP A OD1 
7092  O OD2 . ASP A 963  ? 0.5235 0.5089 0.5261 -0.0121 -0.0109 0.0091  961  ASP A OD2 
7093  N N   . ASP A 964  ? 0.2939 0.2625 0.3012 -0.0082 -0.0157 0.0061  962  ASP A N   
7094  C CA  . ASP A 964  ? 0.3337 0.2983 0.3454 -0.0080 -0.0184 0.0057  962  ASP A CA  
7095  C C   . ASP A 964  ? 0.3500 0.3117 0.3595 -0.0047 -0.0181 0.0016  962  ASP A C   
7096  O O   . ASP A 964  ? 0.3492 0.3082 0.3622 -0.0036 -0.0205 -0.0009 962  ASP A O   
7097  C CB  . ASP A 964  ? 0.3627 0.3274 0.3765 -0.0101 -0.0187 0.0096  962  ASP A CB  
7098  C CG  . ASP A 964  ? 0.4041 0.3720 0.4215 -0.0136 -0.0197 0.0140  962  ASP A CG  
7099  O OD1 . ASP A 964  ? 0.4388 0.4079 0.4581 -0.0145 -0.0207 0.0140  962  ASP A OD1 
7100  O OD2 . ASP A 964  ? 0.4888 0.4584 0.5069 -0.0155 -0.0195 0.0176  962  ASP A OD2 
7101  N N   . VAL A 965  ? 0.2979 0.2606 0.3021 -0.0031 -0.0153 0.0009  963  VAL A N   
7102  C CA  . VAL A 965  ? 0.2983 0.2593 0.3002 0.0000  -0.0149 -0.0026 963  VAL A CA  
7103  C C   . VAL A 965  ? 0.3372 0.2986 0.3386 0.0017  -0.0156 -0.0060 963  VAL A C   
7104  O O   . VAL A 965  ? 0.3292 0.2890 0.3320 0.0036  -0.0171 -0.0092 963  VAL A O   
7105  C CB  . VAL A 965  ? 0.2598 0.2222 0.2566 0.0011  -0.0118 -0.0023 963  VAL A CB  
7106  C CG1 . VAL A 965  ? 0.2889 0.2506 0.2831 0.0042  -0.0112 -0.0055 963  VAL A CG1 
7107  C CG2 . VAL A 965  ? 0.2935 0.2555 0.2910 -0.0004 -0.0114 0.0006  963  VAL A CG2 
7108  N N   . ASN A 966  ? 0.2720 0.2360 0.2715 0.0011  -0.0145 -0.0055 964  ASN A N   
7109  C CA  . ASN A 966  ? 0.2857 0.2504 0.2846 0.0026  -0.0152 -0.0085 964  ASN A CA  
7110  C C   . ASN A 966  ? 0.3188 0.2817 0.3232 0.0020  -0.0186 -0.0098 964  ASN A C   
7111  O O   . ASN A 966  ? 0.3224 0.2851 0.3271 0.0039  -0.0199 -0.0134 964  ASN A O   
7112  C CB  . ASN A 966  ? 0.2794 0.2472 0.2760 0.0018  -0.0137 -0.0073 964  ASN A CB  
7113  C CG  . ASN A 966  ? 0.2765 0.2459 0.2680 0.0031  -0.0107 -0.0070 964  ASN A CG  
7114  O OD1 . ASN A 966  ? 0.2891 0.2578 0.2784 0.0050  -0.0098 -0.0081 964  ASN A OD1 
7115  N ND2 . ASN A 966  ? 0.2869 0.2590 0.2772 0.0020  -0.0093 -0.0054 964  ASN A ND2 
7116  N N   . ALA A 967  ? 0.3177 0.2797 0.3267 -0.0007 -0.0202 -0.0069 965  ALA A N   
7117  C CA  . ALA A 967  ? 0.3603 0.3206 0.3755 -0.0018 -0.0236 -0.0075 965  ALA A CA  
7118  C C   . ALA A 967  ? 0.3388 0.2959 0.3574 0.0001  -0.0261 -0.0110 965  ALA A C   
7119  O O   . ALA A 967  ? 0.3960 0.3517 0.4197 0.0000  -0.0292 -0.0129 965  ALA A O   
7120  C CB  . ALA A 967  ? 0.4101 0.3708 0.4298 -0.0054 -0.0247 -0.0028 965  ALA A CB  
7121  N N   . THR A 968  ? 0.3093 0.2654 0.3256 0.0020  -0.0250 -0.0122 966  THR A N   
7122  C CA  . THR A 968  ? 0.3079 0.2616 0.3274 0.0042  -0.0273 -0.0162 966  THR A CA  
7123  C C   . THR A 968  ? 0.3183 0.2735 0.3362 0.0068  -0.0279 -0.0212 966  THR A C   
7124  O O   . THR A 968  ? 0.3392 0.2930 0.3612 0.0084  -0.0306 -0.0251 966  THR A O   
7125  C CB  . THR A 968  ? 0.3301 0.2833 0.3468 0.0059  -0.0257 -0.0167 966  THR A CB  
7126  O OG1 . THR A 968  ? 0.3103 0.2663 0.3201 0.0080  -0.0227 -0.0182 966  THR A OG1 
7127  C CG2 . THR A 968  ? 0.2961 0.2485 0.3134 0.0035  -0.0248 -0.0119 966  THR A CG2 
7128  N N   . GLY A 969  ? 0.3030 0.2613 0.3155 0.0074  -0.0256 -0.0212 967  GLY A N   
7129  C CA  . GLY A 969  ? 0.2921 0.2525 0.3023 0.0100  -0.0258 -0.0255 967  GLY A CA  
7130  C C   . GLY A 969  ? 0.2663 0.2287 0.2714 0.0130  -0.0237 -0.0277 967  GLY A C   
7131  O O   . GLY A 969  ? 0.2640 0.2295 0.2658 0.0150  -0.0232 -0.0304 967  GLY A O   
7132  N N   . TYR A 970  ? 0.2632 0.2244 0.2677 0.0132  -0.0227 -0.0265 968  TYR A N   
7133  C CA  . TYR A 970  ? 0.2664 0.2299 0.2661 0.0157  -0.0204 -0.0278 968  TYR A CA  
7134  C C   . TYR A 970  ? 0.2316 0.1972 0.2257 0.0151  -0.0171 -0.0245 968  TYR A C   
7135  O O   . TYR A 970  ? 0.2921 0.2573 0.2862 0.0129  -0.0164 -0.0214 968  TYR A O   
7136  C CB  . TYR A 970  ? 0.2661 0.2275 0.2677 0.0161  -0.0206 -0.0278 968  TYR A CB  
7137  C CG  . TYR A 970  ? 0.2743 0.2338 0.2816 0.0173  -0.0240 -0.0317 968  TYR A CG  
7138  C CD1 . TYR A 970  ? 0.2951 0.2572 0.3017 0.0205  -0.0246 -0.0367 968  TYR A CD1 
7139  C CD2 . TYR A 970  ? 0.3050 0.2607 0.3189 0.0151  -0.0267 -0.0304 968  TYR A CD2 
7140  C CE1 . TYR A 970  ? 0.3175 0.2780 0.3299 0.0218  -0.0279 -0.0410 968  TYR A CE1 
7141  C CE2 . TYR A 970  ? 0.3394 0.2930 0.3595 0.0162  -0.0302 -0.0342 968  TYR A CE2 
7142  C CZ  . TYR A 970  ? 0.3533 0.3093 0.3728 0.0197  -0.0308 -0.0397 968  TYR A CZ  
7143  O OH  . TYR A 970  ? 0.4441 0.3983 0.4703 0.0210  -0.0344 -0.0440 968  TYR A OH  
7144  N N   . GLY A 971  ? 0.2246 0.1927 0.2144 0.0172  -0.0150 -0.0252 969  GLY A N   
7145  C CA  . GLY A 971  ? 0.2185 0.1886 0.2037 0.0169  -0.0122 -0.0223 969  GLY A CA  
7146  C C   . GLY A 971  ? 0.2167 0.1895 0.1981 0.0192  -0.0103 -0.0229 969  GLY A C   
7147  O O   . GLY A 971  ? 0.2234 0.1995 0.2013 0.0203  -0.0090 -0.0228 969  GLY A O   
7148  N N   . LEU A 972  ? 0.2101 0.1818 0.1923 0.0198  -0.0102 -0.0232 970  LEU A N   
7149  C CA  . LEU A 972  ? 0.2137 0.1886 0.1928 0.0220  -0.0085 -0.0239 970  LEU A CA  
7150  C C   . LEU A 972  ? 0.2198 0.1942 0.1965 0.0210  -0.0060 -0.0200 970  LEU A C   
7151  O O   . LEU A 972  ? 0.2309 0.2071 0.2049 0.0208  -0.0044 -0.0179 970  LEU A O   
7152  C CB  . LEU A 972  ? 0.2200 0.1949 0.2013 0.0238  -0.0100 -0.0274 970  LEU A CB  
7153  C CG  . LEU A 972  ? 0.2200 0.1995 0.1982 0.0264  -0.0085 -0.0287 970  LEU A CG  
7154  C CD1 . LEU A 972  ? 0.2315 0.2161 0.2059 0.0278  -0.0077 -0.0294 970  LEU A CD1 
7155  C CD2 . LEU A 972  ? 0.2546 0.2345 0.2358 0.0283  -0.0103 -0.0331 970  LEU A CD2 
7156  N N   . THR A 973  ? 0.2209 0.1930 0.1992 0.0204  -0.0058 -0.0190 971  THR A N   
7157  C CA  . THR A 973  ? 0.2171 0.1886 0.1936 0.0194  -0.0036 -0.0155 971  THR A CA  
7158  C C   . THR A 973  ? 0.2123 0.1805 0.1910 0.0166  -0.0039 -0.0131 971  THR A C   
7159  O O   . THR A 973  ? 0.2123 0.1783 0.1944 0.0155  -0.0059 -0.0137 971  THR A O   
7160  C CB  . THR A 973  ? 0.2074 0.1795 0.1836 0.0206  -0.0027 -0.0157 971  THR A CB  
7161  O OG1 . THR A 973  ? 0.2226 0.1921 0.2025 0.0204  -0.0046 -0.0172 971  THR A OG1 
7162  C CG2 . THR A 973  ? 0.2107 0.1875 0.1845 0.0233  -0.0021 -0.0176 971  THR A CG2 
7163  N N   . PHE A 974  ? 0.2080 0.1764 0.1850 0.0156  -0.0021 -0.0102 972  PHE A N   
7164  C CA  . PHE A 974  ? 0.2124 0.1789 0.1908 0.0131  -0.0021 -0.0079 972  PHE A CA  
7165  C C   . PHE A 974  ? 0.1982 0.1651 0.1750 0.0127  0.0000  -0.0056 972  PHE A C   
7166  O O   . PHE A 974  ? 0.2217 0.1903 0.1962 0.0137  0.0014  -0.0051 972  PHE A O   
7167  C CB  . PHE A 974  ? 0.2195 0.1868 0.1979 0.0119  -0.0023 -0.0074 972  PHE A CB  
7168  C CG  . PHE A 974  ? 0.2233 0.1900 0.2027 0.0095  -0.0020 -0.0050 972  PHE A CG  
7169  C CD1 . PHE A 974  ? 0.2064 0.1715 0.1889 0.0077  -0.0036 -0.0043 972  PHE A CD1 
7170  C CD2 . PHE A 974  ? 0.2094 0.1774 0.1870 0.0090  -0.0002 -0.0034 972  PHE A CD2 
7171  C CE1 . PHE A 974  ? 0.2314 0.1971 0.2147 0.0054  -0.0032 -0.0018 972  PHE A CE1 
7172  C CE2 . PHE A 974  ? 0.2090 0.1774 0.1876 0.0069  0.0002  -0.0016 972  PHE A CE2 
7173  C CZ  . PHE A 974  ? 0.2167 0.1842 0.1978 0.0051  -0.0013 -0.0007 972  PHE A CZ  
7174  N N   . GLY A 975  ? 0.2092 0.1744 0.1874 0.0112  -0.0001 -0.0041 973  GLY A N   
7175  C CA  . GLY A 975  ? 0.2093 0.1748 0.1864 0.0108  0.0016  -0.0021 973  GLY A CA  
7176  C C   . GLY A 975  ? 0.2011 0.1667 0.1790 0.0085  0.0017  -0.0003 973  GLY A C   
7177  O O   . GLY A 975  ? 0.1983 0.1634 0.1782 0.0069  0.0004  0.0002  973  GLY A O   
7178  N N   . LEU A 976  ? 0.2128 0.1796 0.1894 0.0083  0.0033  0.0007  974  LEU A N   
7179  C CA  . LEU A 976  ? 0.2122 0.1799 0.1893 0.0064  0.0036  0.0021  974  LEU A CA  
7180  C C   . LEU A 976  ? 0.1971 0.1650 0.1737 0.0065  0.0049  0.0030  974  LEU A C   
7181  O O   . LEU A 976  ? 0.2113 0.1795 0.1870 0.0078  0.0059  0.0028  974  LEU A O   
7182  C CB  . LEU A 976  ? 0.2062 0.1758 0.1828 0.0062  0.0041  0.0017  974  LEU A CB  
7183  C CG  . LEU A 976  ? 0.2090 0.1808 0.1860 0.0046  0.0046  0.0025  974  LEU A CG  
7184  C CD1 . LEU A 976  ? 0.2441 0.2166 0.2226 0.0025  0.0035  0.0036  974  LEU A CD1 
7185  C CD2 . LEU A 976  ? 0.2525 0.2261 0.2292 0.0050  0.0051  0.0016  974  LEU A CD2 
7186  N N   . HIS A 977  ? 0.2080 0.1760 0.1856 0.0050  0.0046  0.0042  975  HIS A N   
7187  C CA  . HIS A 977  ? 0.2118 0.1803 0.1892 0.0048  0.0056  0.0049  975  HIS A CA  
7188  C C   . HIS A 977  ? 0.1916 0.1628 0.1693 0.0031  0.0059  0.0054  975  HIS A C   
7189  O O   . HIS A 977  ? 0.2105 0.1828 0.1890 0.0014  0.0051  0.0064  975  HIS A O   
7190  C CB  . HIS A 977  ? 0.2200 0.1870 0.1984 0.0045  0.0051  0.0058  975  HIS A CB  
7191  C CG  . HIS A 977  ? 0.2451 0.2106 0.2230 0.0064  0.0055  0.0052  975  HIS A CG  
7192  N ND1 . HIS A 977  ? 0.3226 0.2881 0.3003 0.0069  0.0065  0.0058  975  HIS A ND1 
7193  C CD2 . HIS A 977  ? 0.3241 0.2886 0.3018 0.0080  0.0051  0.0041  975  HIS A CD2 
7194  C CE1 . HIS A 977  ? 0.2877 0.2525 0.2651 0.0086  0.0068  0.0053  975  HIS A CE1 
7195  N NE2 . HIS A 977  ? 0.3270 0.2913 0.3042 0.0093  0.0060  0.0041  975  HIS A NE2 
7196  N N   . THR A 978  ? 0.1926 0.1651 0.1699 0.0037  0.0069  0.0046  976  THR A N   
7197  C CA  . THR A 978  ? 0.2133 0.1890 0.1910 0.0026  0.0072  0.0043  976  THR A CA  
7198  C C   . THR A 978  ? 0.2187 0.1948 0.1969 0.0038  0.0081  0.0033  976  THR A C   
7199  O O   . THR A 978  ? 0.2407 0.2150 0.2188 0.0053  0.0084  0.0030  976  THR A O   
7200  C CB  . THR A 978  ? 0.2218 0.1995 0.1996 0.0019  0.0069  0.0038  976  THR A CB  
7201  O OG1 . THR A 978  ? 0.2233 0.2050 0.2016 0.0010  0.0073  0.0032  976  THR A OG1 
7202  C CG2 . THR A 978  ? 0.2353 0.2120 0.2128 0.0034  0.0070  0.0027  976  THR A CG2 
7203  N N   . ARG A 979  ? 0.2233 0.2019 0.2021 0.0031  0.0085  0.0027  977  ARG A N   
7204  C CA  . ARG A 979  ? 0.2461 0.2253 0.2263 0.0041  0.0090  0.0013  977  ARG A CA  
7205  C C   . ARG A 979  ? 0.2237 0.2055 0.2047 0.0042  0.0089  -0.0004 977  ARG A C   
7206  O O   . ARG A 979  ? 0.2642 0.2465 0.2470 0.0051  0.0091  -0.0018 977  ARG A O   
7207  C CB  . ARG A 979  ? 0.2424 0.2230 0.2234 0.0036  0.0091  0.0010  977  ARG A CB  
7208  C CG  . ARG A 979  ? 0.2953 0.2732 0.2758 0.0037  0.0092  0.0025  977  ARG A CG  
7209  C CD  . ARG A 979  ? 0.4091 0.3888 0.3904 0.0030  0.0092  0.0023  977  ARG A CD  
7210  N NE  . ARG A 979  ? 0.4495 0.4266 0.4308 0.0033  0.0093  0.0037  977  ARG A NE  
7211  C CZ  . ARG A 979  ? 0.5222 0.5000 0.5043 0.0030  0.0093  0.0036  977  ARG A CZ  
7212  N NH1 . ARG A 979  ? 0.4215 0.4027 0.4045 0.0024  0.0092  0.0021  977  ARG A NH1 
7213  N NH2 . ARG A 979  ? 0.4642 0.4396 0.4464 0.0034  0.0094  0.0049  977  ARG A NH2 
7214  N N   . LEU A 980  ? 0.2053 0.1889 0.1856 0.0032  0.0086  -0.0003 978  LEU A N   
7215  C CA  . LEU A 980  ? 0.2042 0.1916 0.1853 0.0029  0.0087  -0.0019 978  LEU A CA  
7216  C C   . LEU A 980  ? 0.2182 0.2043 0.1995 0.0039  0.0085  -0.0024 978  LEU A C   
7217  O O   . LEU A 980  ? 0.2263 0.2111 0.2065 0.0036  0.0081  -0.0013 978  LEU A O   
7218  C CB  . LEU A 980  ? 0.2131 0.2044 0.1935 0.0010  0.0085  -0.0013 978  LEU A CB  
7219  C CG  . LEU A 980  ? 0.2082 0.2013 0.1883 -0.0002 0.0085  -0.0003 978  LEU A CG  
7220  C CD1 . LEU A 980  ? 0.2452 0.2426 0.2247 -0.0023 0.0081  0.0010  978  LEU A CD1 
7221  C CD2 . LEU A 980  ? 0.2477 0.2432 0.2290 0.0004  0.0089  -0.0026 978  LEU A CD2 
7222  N N   . ASP A 981  ? 0.2140 0.2009 0.1972 0.0051  0.0086  -0.0041 979  ASP A N   
7223  C CA  . ASP A 981  ? 0.2298 0.2157 0.2134 0.0061  0.0083  -0.0043 979  ASP A CA  
7224  C C   . ASP A 981  ? 0.2277 0.2159 0.2105 0.0051  0.0080  -0.0045 979  ASP A C   
7225  O O   . ASP A 981  ? 0.2184 0.2050 0.2005 0.0056  0.0076  -0.0039 979  ASP A O   
7226  C CB  . ASP A 981  ? 0.2365 0.2233 0.2231 0.0073  0.0082  -0.0062 979  ASP A CB  
7227  C CG  . ASP A 981  ? 0.2516 0.2355 0.2397 0.0085  0.0081  -0.0056 979  ASP A CG  
7228  O OD1 . ASP A 981  ? 0.2826 0.2637 0.2691 0.0086  0.0083  -0.0036 979  ASP A OD1 
7229  O OD2 . ASP A 981  ? 0.2873 0.2719 0.2787 0.0093  0.0078  -0.0071 979  ASP A OD2 
7230  N N   . GLU A 982  ? 0.2184 0.2109 0.2015 0.0038  0.0081  -0.0052 980  GLU A N   
7231  C CA  . GLU A 982  ? 0.2166 0.2117 0.1993 0.0027  0.0079  -0.0051 980  GLU A CA  
7232  C C   . GLU A 982  ? 0.2140 0.2064 0.1951 0.0018  0.0073  -0.0028 980  GLU A C   
7233  O O   . GLU A 982  ? 0.2229 0.2148 0.2039 0.0018  0.0067  -0.0026 980  GLU A O   
7234  C CB  . GLU A 982  ? 0.2305 0.2317 0.2137 0.0013  0.0082  -0.0058 980  GLU A CB  
7235  C CG  . GLU A 982  ? 0.2510 0.2554 0.2340 -0.0001 0.0078  -0.0051 980  GLU A CG  
7236  C CD  . GLU A 982  ? 0.3241 0.3350 0.3072 -0.0020 0.0081  -0.0047 980  GLU A CD  
7237  O OE1 . GLU A 982  ? 0.3554 0.3666 0.3376 -0.0031 0.0082  -0.0032 980  GLU A OE1 
7238  O OE2 . GLU A 982  ? 0.2837 0.2998 0.2677 -0.0025 0.0083  -0.0058 980  GLU A OE2 
7239  N N   . THR A 983  ? 0.2027 0.1932 0.1829 0.0013  0.0073  -0.0014 981  THR A N   
7240  C CA  . THR A 983  ? 0.2146 0.2026 0.1941 0.0005  0.0065  0.0004  981  THR A CA  
7241  C C   . THR A 983  ? 0.2029 0.1867 0.1817 0.0022  0.0062  0.0002  981  THR A C   
7242  O O   . THR A 983  ? 0.2201 0.2027 0.1989 0.0021  0.0053  0.0005  981  THR A O   
7243  C CB  . THR A 983  ? 0.2074 0.1948 0.1866 -0.0004 0.0065  0.0019  981  THR A CB  
7244  O OG1 . THR A 983  ? 0.2463 0.2386 0.2259 -0.0021 0.0066  0.0024  981  THR A OG1 
7245  C CG2 . THR A 983  ? 0.2438 0.2280 0.2229 -0.0009 0.0054  0.0035  981  THR A CG2 
7246  N N   . ILE A 984  ? 0.2052 0.1874 0.1839 0.0039  0.0068  -0.0004 982  ILE A N   
7247  C CA  . ILE A 984  ? 0.2192 0.1986 0.1972 0.0055  0.0066  -0.0004 982  ILE A CA  
7248  C C   . ILE A 984  ? 0.2184 0.1988 0.1967 0.0059  0.0062  -0.0012 982  ILE A C   
7249  O O   . ILE A 984  ? 0.2125 0.1915 0.1900 0.0064  0.0055  -0.0012 982  ILE A O   
7250  C CB  . ILE A 984  ? 0.2189 0.1971 0.1973 0.0069  0.0073  -0.0004 982  ILE A CB  
7251  C CG1 . ILE A 984  ? 0.2397 0.2166 0.2177 0.0066  0.0077  0.0005  982  ILE A CG1 
7252  C CG2 . ILE A 984  ? 0.2528 0.2295 0.2306 0.0086  0.0072  -0.0002 982  ILE A CG2 
7253  C CD1 . ILE A 984  ? 0.2817 0.2578 0.2608 0.0077  0.0083  0.0006  982  ILE A CD1 
7254  N N   . ALA A 985  ? 0.2000 0.1830 0.1796 0.0058  0.0065  -0.0023 983  ALA A N   
7255  C CA  . ALA A 985  ? 0.2280 0.2121 0.2081 0.0063  0.0060  -0.0031 983  ALA A CA  
7256  C C   . ALA A 985  ? 0.2107 0.1957 0.1905 0.0050  0.0053  -0.0028 983  ALA A C   
7257  O O   . ALA A 985  ? 0.2346 0.2187 0.2140 0.0056  0.0046  -0.0030 983  ALA A O   
7258  C CB  . ALA A 985  ? 0.2350 0.2221 0.2170 0.0065  0.0064  -0.0045 983  ALA A CB  
7259  N N   . HIS A 986  ? 0.2208 0.2077 0.2009 0.0032  0.0053  -0.0022 984  HIS A N   
7260  C CA  . HIS A 986  ? 0.2322 0.2201 0.2128 0.0016  0.0043  -0.0014 984  HIS A CA  
7261  C C   . HIS A 986  ? 0.2291 0.2132 0.2091 0.0019  0.0033  -0.0008 984  HIS A C   
7262  O O   . HIS A 986  ? 0.2350 0.2184 0.2153 0.0022  0.0024  -0.0013 984  HIS A O   
7263  C CB  . HIS A 986  ? 0.2376 0.2285 0.2188 -0.0005 0.0045  -0.0002 984  HIS A CB  
7264  C CG  . HIS A 986  ? 0.2702 0.2621 0.2525 -0.0025 0.0034  0.0014  984  HIS A CG  
7265  N ND1 . HIS A 986  ? 0.3334 0.3280 0.3163 -0.0046 0.0032  0.0033  984  HIS A ND1 
7266  C CD2 . HIS A 986  ? 0.2638 0.2544 0.2469 -0.0027 0.0021  0.0016  984  HIS A CD2 
7267  C CE1 . HIS A 986  ? 0.3577 0.3525 0.3422 -0.0062 0.0019  0.0049  984  HIS A CE1 
7268  N NE2 . HIS A 986  ? 0.2624 0.2546 0.2472 -0.0051 0.0012  0.0037  984  HIS A NE2 
7269  N N   . VAL A 987  ? 0.2291 0.2109 0.2085 0.0021  0.0034  -0.0001 985  VAL A N   
7270  C CA  . VAL A 987  ? 0.2207 0.1994 0.2000 0.0024  0.0023  0.0002  985  VAL A CA  
7271  C C   . VAL A 987  ? 0.2355 0.2126 0.2138 0.0045  0.0021  -0.0012 985  VAL A C   
7272  O O   . VAL A 987  ? 0.2356 0.2117 0.2144 0.0047  0.0009  -0.0018 985  VAL A O   
7273  C CB  . VAL A 987  ? 0.2127 0.1896 0.1918 0.0022  0.0025  0.0011  985  VAL A CB  
7274  C CG1 . VAL A 987  ? 0.2302 0.2040 0.2096 0.0031  0.0014  0.0007  985  VAL A CG1 
7275  C CG2 . VAL A 987  ? 0.2582 0.2371 0.2386 -0.0001 0.0023  0.0028  985  VAL A CG2 
7276  N N   . THR A 988  ? 0.2212 0.1984 0.1984 0.0060  0.0032  -0.0015 986  THR A N   
7277  C CA  . THR A 988  ? 0.2495 0.2259 0.2256 0.0079  0.0030  -0.0023 986  THR A CA  
7278  C C   . THR A 988  ? 0.3063 0.2842 0.2827 0.0081  0.0023  -0.0032 986  THR A C   
7279  O O   . THR A 988  ? 0.3120 0.2896 0.2876 0.0093  0.0017  -0.0040 986  THR A O   
7280  C CB  . THR A 988  ? 0.2694 0.2457 0.2446 0.0094  0.0041  -0.0019 986  THR A CB  
7281  O OG1 . THR A 988  ? 0.2768 0.2547 0.2530 0.0092  0.0048  -0.0018 986  THR A OG1 
7282  C CG2 . THR A 988  ? 0.2727 0.2476 0.2476 0.0093  0.0047  -0.0011 986  THR A CG2 
7283  N N   . SER A 989  ? 0.2391 0.2190 0.2167 0.0069  0.0025  -0.0032 987  SER A N   
7284  C CA  . SER A 989  ? 0.2867 0.2681 0.2648 0.0070  0.0018  -0.0040 987  SER A CA  
7285  C C   . SER A 989  ? 0.3110 0.2921 0.2901 0.0059  0.0004  -0.0042 987  SER A C   
7286  O O   . SER A 989  ? 0.3994 0.3811 0.3787 0.0064  -0.0005 -0.0052 987  SER A O   
7287  C CB  . SER A 989  ? 0.2926 0.2769 0.2720 0.0063  0.0025  -0.0041 987  SER A CB  
7288  O OG  . SER A 989  ? 0.3770 0.3630 0.3575 0.0043  0.0025  -0.0036 987  SER A OG  
7289  N N   . ARG A 990  ? 0.2497 0.2299 0.2297 0.0044  -0.0001 -0.0034 988  ARG A N   
7290  C CA  . ARG A 990  ? 0.2832 0.2631 0.2652 0.0030  -0.0017 -0.0032 988  ARG A CA  
7291  C C   . ARG A 990  ? 0.2586 0.2354 0.2408 0.0038  -0.0030 -0.0040 988  ARG A C   
7292  O O   . ARG A 990  ? 0.2762 0.2524 0.2602 0.0034  -0.0048 -0.0047 988  ARG A O   
7293  C CB  . ARG A 990  ? 0.2882 0.2697 0.2718 0.0005  -0.0017 -0.0014 988  ARG A CB  
7294  C CG  . ARG A 990  ? 0.4066 0.3920 0.3902 -0.0002 -0.0005 -0.0011 988  ARG A CG  
7295  C CD  . ARG A 990  ? 0.4123 0.4002 0.3974 -0.0010 -0.0012 -0.0014 988  ARG A CD  
7296  N NE  . ARG A 990  ? 0.3750 0.3652 0.3624 -0.0036 -0.0020 0.0005  988  ARG A NE  
7297  C CZ  . ARG A 990  ? 0.3670 0.3598 0.3564 -0.0048 -0.0028 0.0008  988  ARG A CZ  
7298  N NH1 . ARG A 990  ? 0.4112 0.4042 0.4004 -0.0036 -0.0030 -0.0009 988  ARG A NH1 
7299  N NH2 . ARG A 990  ? 0.3890 0.3844 0.3807 -0.0074 -0.0034 0.0031  988  ARG A NH2 
7300  N N   . ILE A 991  ? 0.2397 0.2149 0.2205 0.0050  -0.0024 -0.0040 989  ILE A N   
7301  C CA  . ILE A 991  ? 0.2292 0.2021 0.2105 0.0060  -0.0036 -0.0052 989  ILE A CA  
7302  C C   . ILE A 991  ? 0.2600 0.2334 0.2400 0.0080  -0.0041 -0.0074 989  ILE A C   
7303  O O   . ILE A 991  ? 0.2646 0.2397 0.2427 0.0090  -0.0030 -0.0075 989  ILE A O   
7304  C CB  . ILE A 991  ? 0.2427 0.2143 0.2226 0.0068  -0.0025 -0.0047 989  ILE A CB  
7305  C CG1 . ILE A 991  ? 0.2592 0.2286 0.2403 0.0076  -0.0039 -0.0060 989  ILE A CG1 
7306  C CG2 . ILE A 991  ? 0.2488 0.2215 0.2260 0.0086  -0.0009 -0.0049 989  ILE A CG2 
7307  C CD1 . ILE A 991  ? 0.3010 0.2689 0.2856 0.0055  -0.0056 -0.0049 989  ILE A CD1 
7308  N N   . LYS A 992  ? 0.2367 0.2089 0.2183 0.0085  -0.0060 -0.0092 990  LYS A N   
7309  C CA  . LYS A 992  ? 0.2534 0.2267 0.2339 0.0105  -0.0068 -0.0117 990  LYS A CA  
7310  C C   . LYS A 992  ? 0.2361 0.2085 0.2161 0.0124  -0.0072 -0.0134 990  LYS A C   
7311  O O   . LYS A 992  ? 0.2755 0.2466 0.2581 0.0125  -0.0091 -0.0153 990  LYS A O   
7312  C CB  . LYS A 992  ? 0.2674 0.2406 0.2506 0.0097  -0.0089 -0.0129 990  LYS A CB  
7313  C CG  . LYS A 992  ? 0.3049 0.2796 0.2888 0.0079  -0.0085 -0.0113 990  LYS A CG  
7314  C CD  . LYS A 992  ? 0.4513 0.4257 0.4388 0.0068  -0.0109 -0.0122 990  LYS A CD  
7315  C CE  . LYS A 992  ? 0.5554 0.5318 0.5440 0.0048  -0.0106 -0.0105 990  LYS A CE  
7316  N NZ  . LYS A 992  ? 0.6449 0.6208 0.6378 0.0031  -0.0131 -0.0107 990  LYS A NZ  
7317  N N   . ALA A 993  ? 0.2454 0.2190 0.2225 0.0138  -0.0054 -0.0129 991  ALA A N   
7318  C CA  . ALA A 993  ? 0.2264 0.2001 0.2027 0.0157  -0.0055 -0.0145 991  ALA A CA  
7319  C C   . ALA A 993  ? 0.2416 0.2185 0.2145 0.0175  -0.0038 -0.0141 991  ALA A C   
7320  O O   . ALA A 993  ? 0.2583 0.2361 0.2298 0.0171  -0.0024 -0.0120 991  ALA A O   
7321  C CB  . ALA A 993  ? 0.2357 0.2071 0.2131 0.0149  -0.0050 -0.0132 991  ALA A CB  
7322  N N   . GLY A 994  ? 0.2108 0.1897 0.1826 0.0196  -0.0041 -0.0162 992  GLY A N   
7323  C CA  . GLY A 994  ? 0.2272 0.2100 0.1958 0.0214  -0.0028 -0.0157 992  GLY A CA  
7324  C C   . GLY A 994  ? 0.1951 0.1782 0.1623 0.0216  -0.0008 -0.0131 992  GLY A C   
7325  O O   . GLY A 994  ? 0.2086 0.1945 0.1739 0.0223  0.0004  -0.0112 992  GLY A O   
7326  N N   . ASN A 995  ? 0.1988 0.1793 0.1673 0.0209  -0.0006 -0.0128 993  ASN A N   
7327  C CA  . ASN A 995  ? 0.2172 0.1980 0.1848 0.0210  0.0012  -0.0105 993  ASN A CA  
7328  C C   . ASN A 995  ? 0.2158 0.1928 0.1851 0.0190  0.0015  -0.0088 993  ASN A C   
7329  O O   . ASN A 995  ? 0.2143 0.1889 0.1856 0.0183  0.0004  -0.0098 993  ASN A O   
7330  C CB  . ASN A 995  ? 0.2076 0.1904 0.1746 0.0229  0.0012  -0.0122 993  ASN A CB  
7331  C CG  . ASN A 995  ? 0.2066 0.1947 0.1711 0.0249  0.0016  -0.0128 993  ASN A CG  
7332  O OD1 . ASN A 995  ? 0.2272 0.2174 0.1915 0.0260  0.0003  -0.0155 993  ASN A OD1 
7333  N ND2 . ASN A 995  ? 0.2211 0.2118 0.1841 0.0254  0.0033  -0.0101 993  ASN A ND2 
7334  N N   . LEU A 996  ? 0.1979 0.1747 0.1668 0.0180  0.0027  -0.0063 994  LEU A N   
7335  C CA  . LEU A 996  ? 0.2094 0.1836 0.1797 0.0161  0.0031  -0.0048 994  LEU A CA  
7336  C C   . LEU A 996  ? 0.1906 0.1648 0.1605 0.0164  0.0046  -0.0030 994  LEU A C   
7337  O O   . LEU A 996  ? 0.1981 0.1745 0.1668 0.0176  0.0055  -0.0020 994  LEU A O   
7338  C CB  . LEU A 996  ? 0.2228 0.1970 0.1935 0.0149  0.0034  -0.0037 994  LEU A CB  
7339  C CG  . LEU A 996  ? 0.2274 0.2024 0.1983 0.0149  0.0022  -0.0051 994  LEU A CG  
7340  C CD1 . LEU A 996  ? 0.2857 0.2611 0.2573 0.0137  0.0026  -0.0041 994  LEU A CD1 
7341  C CD2 . LEU A 996  ? 0.2505 0.2239 0.2231 0.0141  0.0006  -0.0067 994  LEU A CD2 
7342  N N   . TYR A 997  ? 0.2026 0.1746 0.1737 0.0152  0.0047  -0.0024 995  TYR A N   
7343  C CA  . TYR A 997  ? 0.1999 0.1718 0.1709 0.0153  0.0059  -0.0009 995  TYR A CA  
7344  C C   . TYR A 997  ? 0.2065 0.1767 0.1788 0.0134  0.0061  0.0003  995  TYR A C   
7345  O O   . TYR A 997  ? 0.2264 0.1953 0.1999 0.0121  0.0052  -0.0001 995  TYR A O   
7346  C CB  . TYR A 997  ? 0.2071 0.1786 0.1784 0.0162  0.0056  -0.0019 995  TYR A CB  
7347  C CG  . TYR A 997  ? 0.2062 0.1802 0.1764 0.0182  0.0052  -0.0037 995  TYR A CG  
7348  C CD1 . TYR A 997  ? 0.2270 0.2006 0.1978 0.0185  0.0036  -0.0062 995  TYR A CD1 
7349  C CD2 . TYR A 997  ? 0.2302 0.2073 0.1989 0.0197  0.0063  -0.0029 995  TYR A CD2 
7350  C CE1 . TYR A 997  ? 0.2531 0.2295 0.2229 0.0205  0.0031  -0.0084 995  TYR A CE1 
7351  C CE2 . TYR A 997  ? 0.2181 0.1985 0.1855 0.0217  0.0060  -0.0048 995  TYR A CE2 
7352  C CZ  . TYR A 997  ? 0.2507 0.2307 0.2186 0.0221  0.0043  -0.0077 995  TYR A CZ  
7353  O OH  . TYR A 997  ? 0.2819 0.2657 0.2487 0.0242  0.0039  -0.0101 995  TYR A OH  
7354  N N   . ILE A 998  ? 0.1965 0.1672 0.1689 0.0132  0.0072  0.0017  996  ILE A N   
7355  C CA  A ILE A 998  ? 0.1986 0.1686 0.1722 0.0116  0.0075  0.0024  996  ILE A CA  
7356  C CA  B ILE A 998  ? 0.1986 0.1686 0.1722 0.0116  0.0075  0.0024  996  ILE A CA  
7357  C C   . ILE A 998  ? 0.1971 0.1665 0.1712 0.0117  0.0083  0.0035  996  ILE A C   
7358  O O   . ILE A 998  ? 0.1982 0.1683 0.1723 0.0126  0.0090  0.0044  996  ILE A O   
7359  C CB  A ILE A 998  ? 0.2047 0.1758 0.1789 0.0114  0.0079  0.0027  996  ILE A CB  
7360  C CB  B ILE A 998  ? 0.2047 0.1758 0.1789 0.0114  0.0078  0.0027  996  ILE A CB  
7361  C CG1 A ILE A 998  ? 0.2297 0.2017 0.2033 0.0117  0.0072  0.0017  996  ILE A CG1 
7362  C CG1 B ILE A 998  ? 0.2223 0.1941 0.1962 0.0112  0.0070  0.0016  996  ILE A CG1 
7363  C CG2 A ILE A 998  ? 0.2127 0.1839 0.1880 0.0098  0.0079  0.0027  996  ILE A CG2 
7364  C CG2 B ILE A 998  ? 0.2197 0.1908 0.1952 0.0101  0.0082  0.0030  996  ILE A CG2 
7365  C CD1 A ILE A 998  ? 0.2234 0.1949 0.1973 0.0104  0.0062  0.0008  996  ILE A CD1 
7366  C CD1 B ILE A 998  ? 0.2387 0.2117 0.2132 0.0113  0.0072  0.0016  996  ILE A CD1 
7367  N N   . ASN A 999  ? 0.2054 0.1738 0.1802 0.0105  0.0079  0.0036  997  ASN A N   
7368  C CA  . ASN A 999  ? 0.2076 0.1754 0.1830 0.0102  0.0085  0.0046  997  ASN A CA  
7369  C C   . ASN A 999  ? 0.1938 0.1615 0.1688 0.0117  0.0089  0.0048  997  ASN A C   
7370  O O   . ASN A 999  ? 0.2209 0.1889 0.1964 0.0121  0.0097  0.0059  997  ASN A O   
7371  C CB  . ASN A 999  ? 0.2056 0.1741 0.1819 0.0098  0.0092  0.0051  997  ASN A CB  
7372  C CG  . ASN A 999  ? 0.1927 0.1622 0.1695 0.0083  0.0088  0.0046  997  ASN A CG  
7373  O OD1 . ASN A 999  ? 0.2260 0.1954 0.2027 0.0071  0.0082  0.0046  997  ASN A OD1 
7374  N ND2 . ASN A 999  ? 0.2172 0.1878 0.1949 0.0083  0.0092  0.0042  997  ASN A ND2 
7375  N N   . ARG A 1000 ? 0.2026 0.1703 0.1770 0.0126  0.0082  0.0037  998  ARG A N   
7376  C CA  . ARG A 1000 ? 0.2153 0.1838 0.1893 0.0143  0.0086  0.0035  998  ARG A CA  
7377  C C   . ARG A 1000 ? 0.2116 0.1794 0.1858 0.0148  0.0073  0.0015  998  ARG A C   
7378  O O   . ARG A 1000 ? 0.2320 0.1986 0.2069 0.0138  0.0061  0.0009  998  ARG A O   
7379  C CB  . ARG A 1000 ? 0.2066 0.1776 0.1795 0.0156  0.0095  0.0041  998  ARG A CB  
7380  C CG  . ARG A 1000 ? 0.2155 0.1874 0.1875 0.0159  0.0090  0.0033  998  ARG A CG  
7381  C CD  . ARG A 1000 ? 0.2260 0.2011 0.1966 0.0177  0.0094  0.0034  998  ARG A CD  
7382  N NE  . ARG A 1000 ? 0.2107 0.1870 0.1806 0.0191  0.0091  0.0017  998  ARG A NE  
7383  C CZ  . ARG A 1000 ? 0.2289 0.2089 0.1976 0.0208  0.0095  0.0015  998  ARG A CZ  
7384  N NH1 . ARG A 1000 ? 0.2427 0.2254 0.2106 0.0212  0.0103  0.0034  998  ARG A NH1 
7385  N NH2 . ARG A 1000 ? 0.2350 0.2164 0.2034 0.0221  0.0091  -0.0007 998  ARG A NH2 
7386  N N   . ASN A 1001 ? 0.2112 0.1801 0.1853 0.0164  0.0073  0.0006  999  ASN A N   
7387  C CA  . ASN A 1001 ? 0.2120 0.1805 0.1870 0.0172  0.0058  -0.0018 999  ASN A CA  
7388  C C   . ASN A 1001 ? 0.2280 0.1981 0.2018 0.0180  0.0053  -0.0033 999  ASN A C   
7389  O O   . ASN A 1001 ? 0.2283 0.2000 0.2004 0.0181  0.0063  -0.0023 999  ASN A O   
7390  C CB  . ASN A 1001 ? 0.2497 0.2193 0.2251 0.0189  0.0059  -0.0029 999  ASN A CB  
7391  C CG  . ASN A 1001 ? 0.2624 0.2363 0.2359 0.0208  0.0072  -0.0031 999  ASN A CG  
7392  O OD1 . ASN A 1001 ? 0.2565 0.2324 0.2286 0.0216  0.0072  -0.0038 999  ASN A OD1 
7393  N ND2 . ASN A 1001 ? 0.3595 0.3350 0.3331 0.0216  0.0083  -0.0022 999  ASN A ND2 
7394  N N   A ILE A 1002 ? 0.2069 0.1763 0.1820 0.0186  0.0036  -0.0058 1000 ILE A N   
7395  N N   B ILE A 1002 ? 0.2067 0.1762 0.1817 0.0186  0.0037  -0.0058 1000 ILE A N   
7396  C CA  A ILE A 1002 ? 0.2095 0.1800 0.1839 0.0191  0.0028  -0.0075 1000 ILE A CA  
7397  C CA  B ILE A 1002 ? 0.2089 0.1798 0.1830 0.0194  0.0029  -0.0076 1000 ILE A CA  
7398  C C   A ILE A 1002 ? 0.2247 0.1983 0.1985 0.0216  0.0024  -0.0103 1000 ILE A C   
7399  C C   B ILE A 1002 ? 0.2185 0.1927 0.1919 0.0219  0.0027  -0.0103 1000 ILE A C   
7400  O O   A ILE A 1002 ? 0.2217 0.1958 0.1958 0.0222  0.0010  -0.0127 1000 ILE A O   
7401  O O   B ILE A 1002 ? 0.2480 0.2234 0.2213 0.0228  0.0016  -0.0126 1000 ILE A O   
7402  C CB  A ILE A 1002 ? 0.2118 0.1794 0.1884 0.0175  0.0009  -0.0080 1000 ILE A CB  
7403  C CB  B ILE A 1002 ? 0.2026 0.1708 0.1789 0.0179  0.0010  -0.0084 1000 ILE A CB  
7404  C CG1 A ILE A 1002 ? 0.2273 0.1930 0.2071 0.0178  -0.0010 -0.0100 1000 ILE A CG1 
7405  C CG1 B ILE A 1002 ? 0.2276 0.1937 0.2071 0.0182  -0.0009 -0.0102 1000 ILE A CG1 
7406  C CG2 A ILE A 1002 ? 0.2123 0.1781 0.1892 0.0151  0.0015  -0.0052 1000 ILE A CG2 
7407  C CG2 B ILE A 1002 ? 0.2069 0.1732 0.1835 0.0155  0.0015  -0.0057 1000 ILE A CG2 
7408  C CD1 A ILE A 1002 ? 0.2368 0.2003 0.2194 0.0165  -0.0032 -0.0108 1000 ILE A CD1 
7409  C CD1 B ILE A 1002 ? 0.2353 0.1990 0.2177 0.0167  -0.0031 -0.0108 1000 ILE A CD1 
7410  N N   A ILE A 1003 ? 0.2231 0.1992 0.1960 0.0230  0.0035  -0.0103 1001 ILE A N   
7411  N N   B ILE A 1003 ? 0.2235 0.1998 0.1964 0.0232  0.0038  -0.0101 1001 ILE A N   
7412  C CA  A ILE A 1003 ? 0.2482 0.2282 0.2205 0.0255  0.0032  -0.0133 1001 ILE A CA  
7413  C CA  B ILE A 1003 ? 0.2412 0.2214 0.2137 0.0257  0.0035  -0.0131 1001 ILE A CA  
7414  C C   A ILE A 1003 ? 0.2877 0.2730 0.2569 0.0268  0.0049  -0.0121 1001 ILE A C   
7415  C C   B ILE A 1003 ? 0.2349 0.2200 0.2047 0.0269  0.0056  -0.0113 1001 ILE A C   
7416  O O   A ILE A 1003 ? 0.2755 0.2655 0.2438 0.0290  0.0050  -0.0142 1001 ILE A O   
7417  O O   B ILE A 1003 ? 0.2604 0.2451 0.2293 0.0257  0.0070  -0.0079 1001 ILE A O   
7418  C CB  A ILE A 1003 ? 0.2449 0.2247 0.2194 0.0266  0.0027  -0.0150 1001 ILE A CB  
7419  C CB  B ILE A 1003 ? 0.2503 0.2291 0.2256 0.0265  0.0023  -0.0154 1001 ILE A CB  
7420  C CG1 A ILE A 1003 ? 0.2534 0.2333 0.2273 0.0261  0.0045  -0.0120 1001 ILE A CG1 
7421  C CG1 B ILE A 1003 ? 0.2470 0.2248 0.2227 0.0258  0.0036  -0.0128 1001 ILE A CG1 
7422  C CG2 A ILE A 1003 ? 0.2332 0.2081 0.2114 0.0256  0.0004  -0.0165 1001 ILE A CG2 
7423  C CG2 B ILE A 1003 ? 0.2367 0.2109 0.2155 0.0252  -0.0001 -0.0167 1001 ILE A CG2 
7424  C CD1 A ILE A 1003 ? 0.3215 0.3018 0.2974 0.0273  0.0042  -0.0136 1001 ILE A CD1 
7425  C CD1 B ILE A 1003 ? 0.3007 0.2787 0.2788 0.0272  0.0029  -0.0151 1001 ILE A CD1 
7426  N N   A GLY A 1004 ? 0.2501 0.2351 0.2180 0.0255  0.0060  -0.0089 1002 GLY A N   
7427  N N   B GLY A 1004 ? 0.2491 0.2392 0.2179 0.0292  0.0055  -0.0138 1002 GLY A N   
7428  C CA  A GLY A 1004 ? 0.2427 0.2324 0.2083 0.0264  0.0075  -0.0069 1002 GLY A CA  
7429  C CA  B GLY A 1004 ? 0.2716 0.2676 0.2380 0.0304  0.0074  -0.0120 1002 GLY A CA  
7430  C C   A GLY A 1004 ? 0.2386 0.2322 0.2025 0.0278  0.0068  -0.0088 1002 GLY A C   
7431  C C   B GLY A 1004 ? 0.2471 0.2452 0.2113 0.0298  0.0082  -0.0093 1002 GLY A C   
7432  O O   A GLY A 1004 ? 0.2508 0.2425 0.2149 0.0271  0.0057  -0.0096 1002 GLY A O   
7433  O O   B GLY A 1004 ? 0.2745 0.2745 0.2379 0.0294  0.0097  -0.0056 1002 GLY A O   
7434  N N   A ALA A 1005 ? 0.2271 0.2268 0.1893 0.0297  0.0074  -0.0094 1003 ALA A N   
7435  N N   B ALA A 1005 ? 0.2599 0.2577 0.2236 0.0299  0.0070  -0.0110 1003 ALA A N   
7436  C CA  A ALA A 1005 ? 0.2278 0.2324 0.1881 0.0312  0.0069  -0.0109 1003 ALA A CA  
7437  C CA  B ALA A 1005 ? 0.2524 0.2524 0.2141 0.0295  0.0075  -0.0087 1003 ALA A CA  
7438  C C   A ALA A 1005 ? 0.2679 0.2793 0.2260 0.0321  0.0085  -0.0080 1003 ALA A C   
7439  C C   B ALA A 1005 ? 0.2504 0.2579 0.2101 0.0311  0.0088  -0.0072 1003 ALA A C   
7440  O O   A ALA A 1005 ? 0.2391 0.2571 0.1954 0.0340  0.0084  -0.0097 1003 ALA A O   
7441  O O   B ALA A 1005 ? 0.2779 0.2902 0.2368 0.0331  0.0087  -0.0098 1003 ALA A O   
7442  C CB  A ALA A 1005 ? 0.2535 0.2598 0.2143 0.0330  0.0053  -0.0162 1003 ALA A CB  
7443  C CB  B ALA A 1005 ? 0.2510 0.2507 0.2126 0.0298  0.0059  -0.0114 1003 ALA A CB  
7444  N N   A VAL A 1006 ? 0.2483 0.2585 0.2070 0.0308  0.0099  -0.0035 1004 VAL A N   
7445  N N   B VAL A 1006 ? 0.2481 0.2569 0.2071 0.0303  0.0099  -0.0029 1004 VAL A N   
7446  C CA  A VAL A 1006 ? 0.2280 0.2443 0.1855 0.0313  0.0113  0.0002  1004 VAL A CA  
7447  C CA  B VAL A 1006 ? 0.2282 0.2440 0.1857 0.0313  0.0112  -0.0001 1004 VAL A CA  
7448  C C   A VAL A 1006 ? 0.2291 0.2499 0.1847 0.0319  0.0109  0.0010  1004 VAL A C   
7449  C C   B VAL A 1006 ? 0.2312 0.2517 0.1868 0.0320  0.0107  0.0002  1004 VAL A C   
7450  O O   A VAL A 1006 ? 0.2160 0.2337 0.1722 0.0307  0.0104  0.0025  1004 VAL A O   
7451  O O   B VAL A 1006 ? 0.2348 0.2519 0.1908 0.0310  0.0100  0.0007  1004 VAL A O   
7452  C CB  A VAL A 1006 ? 0.2332 0.2463 0.1925 0.0295  0.0124  0.0048  1004 VAL A CB  
7453  C CB  B VAL A 1006 ? 0.2309 0.2452 0.1899 0.0298  0.0124  0.0049  1004 VAL A CB  
7454  C CG1 A VAL A 1006 ? 0.2509 0.2705 0.2097 0.0299  0.0135  0.0091  1004 VAL A CG1 
7455  C CG1 B VAL A 1006 ? 0.2472 0.2690 0.2053 0.0305  0.0136  0.0086  1004 VAL A CG1 
7456  C CG2 A VAL A 1006 ? 0.2631 0.2724 0.2240 0.0290  0.0127  0.0040  1004 VAL A CG2 
7457  C CG2 B VAL A 1006 ? 0.2638 0.2743 0.2245 0.0292  0.0129  0.0045  1004 VAL A CG2 
7458  N N   . VAL A 1007 ? 0.2257 0.2544 0.1792 0.0339  0.0111  -0.0003 1005 VAL A N   
7459  C CA  . VAL A 1007 ? 0.2263 0.2604 0.1778 0.0348  0.0106  0.0000  1005 VAL A CA  
7460  C C   . VAL A 1007 ? 0.2180 0.2517 0.1702 0.0333  0.0111  0.0056  1005 VAL A C   
7461  O O   . VAL A 1007 ? 0.2370 0.2717 0.1904 0.0325  0.0123  0.0099  1005 VAL A O   
7462  C CB  . VAL A 1007 ? 0.2229 0.2670 0.1720 0.0370  0.0112  -0.0012 1005 VAL A CB  
7463  C CG1 . VAL A 1007 ? 0.2240 0.2747 0.1709 0.0378  0.0108  -0.0002 1005 VAL A CG1 
7464  C CG2 . VAL A 1007 ? 0.2431 0.2872 0.1923 0.0387  0.0103  -0.0076 1005 VAL A CG2 
7465  N N   . GLY A 1008 ? 0.2178 0.2502 0.1697 0.0329  0.0101  0.0055  1006 GLY A N   
7466  C CA  . GLY A 1008 ? 0.2268 0.2589 0.1798 0.0316  0.0102  0.0104  1006 GLY A CA  
7467  C C   . GLY A 1008 ? 0.2307 0.2550 0.1869 0.0296  0.0104  0.0126  1006 GLY A C   
7468  O O   . GLY A 1008 ? 0.2525 0.2760 0.2105 0.0286  0.0103  0.0165  1006 GLY A O   
7469  N N   . VAL A 1009 ? 0.2259 0.2448 0.1831 0.0291  0.0105  0.0101  1007 VAL A N   
7470  C CA  . VAL A 1009 ? 0.2399 0.2520 0.1999 0.0272  0.0107  0.0116  1007 VAL A CA  
7471  C C   . VAL A 1009 ? 0.2169 0.2229 0.1773 0.0265  0.0097  0.0079  1007 VAL A C   
7472  O O   . VAL A 1009 ? 0.2371 0.2390 0.1990 0.0252  0.0093  0.0085  1007 VAL A O   
7473  C CB  . VAL A 1009 ? 0.2172 0.2290 0.1783 0.0270  0.0118  0.0132  1007 VAL A CB  
7474  C CG1 . VAL A 1009 ? 0.2419 0.2471 0.2059 0.0251  0.0119  0.0145  1007 VAL A CG1 
7475  C CG2 . VAL A 1009 ? 0.2367 0.2548 0.1978 0.0275  0.0127  0.0175  1007 VAL A CG2 
7476  N N   . GLN A 1010 ? 0.2158 0.2215 0.1751 0.0273  0.0093  0.0040  1008 GLN A N   
7477  C CA  . GLN A 1010 ? 0.2202 0.2217 0.1799 0.0268  0.0080  0.0004  1008 GLN A CA  
7478  C C   . GLN A 1010 ? 0.2177 0.2235 0.1755 0.0286  0.0070  -0.0029 1008 GLN A C   
7479  O O   . GLN A 1010 ? 0.2560 0.2625 0.2137 0.0296  0.0065  -0.0063 1008 GLN A O   
7480  C CB  . GLN A 1010 ? 0.2516 0.2485 0.2128 0.0260  0.0079  -0.0014 1008 GLN A CB  
7481  C CG  . GLN A 1010 ? 0.2414 0.2345 0.2043 0.0244  0.0088  0.0015  1008 GLN A CG  
7482  C CD  . GLN A 1010 ? 0.2473 0.2422 0.2104 0.0249  0.0100  0.0030  1008 GLN A CD  
7483  O OE1 . GLN A 1010 ? 0.2468 0.2440 0.2091 0.0262  0.0099  0.0009  1008 GLN A OE1 
7484  N NE2 . GLN A 1010 ? 0.2458 0.2399 0.2103 0.0240  0.0109  0.0064  1008 GLN A NE2 
7485  N N   . PRO A 1011 ? 0.2207 0.2298 0.1772 0.0290  0.0066  -0.0023 1009 PRO A N   
7486  C CA  . PRO A 1011 ? 0.2394 0.2521 0.1944 0.0306  0.0053  -0.0060 1009 PRO A CA  
7487  C C   . PRO A 1011 ? 0.2234 0.2311 0.1800 0.0301  0.0039  -0.0101 1009 PRO A C   
7488  O O   . PRO A 1011 ? 0.2158 0.2177 0.1743 0.0283  0.0036  -0.0095 1009 PRO A O   
7489  C CB  . PRO A 1011 ? 0.2444 0.2586 0.1989 0.0303  0.0049  -0.0042 1009 PRO A CB  
7490  C CG  . PRO A 1011 ? 0.2601 0.2748 0.2153 0.0294  0.0062  0.0010  1009 PRO A CG  
7491  C CD  . PRO A 1011 ? 0.2208 0.2302 0.1779 0.0282  0.0070  0.0017  1009 PRO A CD  
7492  N N   . PHE A 1012 ? 0.2241 0.2342 0.1805 0.0317  0.0030  -0.0141 1010 PHE A N   
7493  C CA  . PHE A 1012 ? 0.2107 0.2159 0.1695 0.0313  0.0017  -0.0175 1010 PHE A CA  
7494  C C   . PHE A 1012 ? 0.2234 0.2290 0.1829 0.0321  -0.0005 -0.0217 1010 PHE A C   
7495  O O   . PHE A 1012 ? 0.2358 0.2473 0.1936 0.0341  -0.0010 -0.0241 1010 PHE A O   
7496  C CB  . PHE A 1012 ? 0.2256 0.2322 0.1849 0.0326  0.0020  -0.0194 1010 PHE A CB  
7497  C CG  . PHE A 1012 ? 0.2140 0.2151 0.1766 0.0320  0.0005  -0.0221 1010 PHE A CG  
7498  C CD1 . PHE A 1012 ? 0.2377 0.2329 0.2020 0.0299  0.0010  -0.0195 1010 PHE A CD1 
7499  C CD2 . PHE A 1012 ? 0.2480 0.2496 0.2122 0.0334  -0.0016 -0.0271 1010 PHE A CD2 
7500  C CE1 . PHE A 1012 ? 0.2344 0.2247 0.2020 0.0291  -0.0005 -0.0214 1010 PHE A CE1 
7501  C CE2 . PHE A 1012 ? 0.2679 0.2641 0.2360 0.0326  -0.0033 -0.0291 1010 PHE A CE2 
7502  C CZ  . PHE A 1012 ? 0.2461 0.2368 0.2158 0.0304  -0.0027 -0.0260 1010 PHE A CZ  
7503  N N   . GLY A 1013 ? 0.2150 0.2148 0.1771 0.0304  -0.0018 -0.0225 1011 GLY A N   
7504  C CA  . GLY A 1013 ? 0.2489 0.2484 0.2126 0.0309  -0.0041 -0.0266 1011 GLY A CA  
7505  C C   . GLY A 1013 ? 0.2222 0.2161 0.1881 0.0286  -0.0050 -0.0254 1011 GLY A C   
7506  O O   . GLY A 1013 ? 0.2372 0.2298 0.2023 0.0271  -0.0038 -0.0218 1011 GLY A O   
7507  N N   . GLY A 1014 ? 0.2266 0.2178 0.1957 0.0282  -0.0073 -0.0286 1012 GLY A N   
7508  C CA  . GLY A 1014 ? 0.2573 0.2438 0.2290 0.0258  -0.0082 -0.0272 1012 GLY A CA  
7509  C C   . GLY A 1014 ? 0.2537 0.2408 0.2266 0.0258  -0.0102 -0.0295 1012 GLY A C   
7510  O O   . GLY A 1014 ? 0.2564 0.2481 0.2275 0.0277  -0.0107 -0.0318 1012 GLY A O   
7511  N N   . ARG A 1015 ? 0.2235 0.2065 0.1996 0.0236  -0.0114 -0.0288 1013 ARG A N   
7512  C CA  . ARG A 1015 ? 0.2430 0.2260 0.2207 0.0230  -0.0132 -0.0301 1013 ARG A CA  
7513  C C   . ARG A 1015 ? 0.2286 0.2078 0.2116 0.0219  -0.0159 -0.0321 1013 ARG A C   
7514  O O   . ARG A 1015 ? 0.2378 0.2144 0.2232 0.0216  -0.0163 -0.0322 1013 ARG A O   
7515  C CB  . ARG A 1015 ? 0.2558 0.2381 0.2325 0.0210  -0.0119 -0.0264 1013 ARG A CB  
7516  C CG  . ARG A 1015 ? 0.2464 0.2246 0.2251 0.0186  -0.0112 -0.0234 1013 ARG A CG  
7517  C CD  . ARG A 1015 ? 0.2930 0.2707 0.2719 0.0165  -0.0105 -0.0206 1013 ARG A CD  
7518  N NE  . ARG A 1015 ? 0.3429 0.3222 0.3224 0.0166  -0.0119 -0.0221 1013 ARG A NE  
7519  C CZ  . ARG A 1015 ? 0.3764 0.3543 0.3596 0.0157  -0.0143 -0.0238 1013 ARG A CZ  
7520  N NH1 . ARG A 1015 ? 0.3459 0.3207 0.3328 0.0144  -0.0156 -0.0238 1013 ARG A NH1 
7521  N NH2 . ARG A 1015 ? 0.3258 0.3056 0.3093 0.0160  -0.0155 -0.0253 1013 ARG A NH2 
7522  N N   . GLY A 1016 ? 0.2476 0.2266 0.2329 0.0212  -0.0178 -0.0335 1014 GLY A N   
7523  C CA  . GLY A 1016 ? 0.2476 0.2231 0.2388 0.0200  -0.0207 -0.0350 1014 GLY A CA  
7524  C C   . GLY A 1016 ? 0.2434 0.2191 0.2369 0.0222  -0.0226 -0.0395 1014 GLY A C   
7525  O O   . GLY A 1016 ? 0.2552 0.2350 0.2463 0.0249  -0.0227 -0.0430 1014 GLY A O   
7526  N N   . LEU A 1017 ? 0.2428 0.2146 0.2411 0.0212  -0.0242 -0.0395 1015 LEU A N   
7527  C CA  . LEU A 1017 ? 0.2462 0.2177 0.2477 0.0232  -0.0262 -0.0439 1015 LEU A CA  
7528  C C   . LEU A 1017 ? 0.2421 0.2166 0.2392 0.0255  -0.0240 -0.0446 1015 LEU A C   
7529  O O   . LEU A 1017 ? 0.2535 0.2289 0.2527 0.0277  -0.0254 -0.0487 1015 LEU A O   
7530  C CB  . LEU A 1017 ? 0.2562 0.2224 0.2641 0.0213  -0.0284 -0.0428 1015 LEU A CB  
7531  C CG  . LEU A 1017 ? 0.2606 0.2238 0.2742 0.0188  -0.0312 -0.0419 1015 LEU A CG  
7532  C CD1 . LEU A 1017 ? 0.2762 0.2347 0.2959 0.0167  -0.0329 -0.0396 1015 LEU A CD1 
7533  C CD2 . LEU A 1017 ? 0.2779 0.2425 0.2947 0.0206  -0.0343 -0.0475 1015 LEU A CD2 
7534  N N   . SER A 1018 ? 0.2194 0.1956 0.2111 0.0251  -0.0206 -0.0408 1016 SER A N   
7535  C CA  . SER A 1018 ? 0.2497 0.2287 0.2376 0.0269  -0.0183 -0.0406 1016 SER A CA  
7536  C C   . SER A 1018 ? 0.2212 0.2066 0.2042 0.0294  -0.0171 -0.0424 1016 SER A C   
7537  O O   . SER A 1018 ? 0.2370 0.2259 0.2172 0.0312  -0.0155 -0.0427 1016 SER A O   
7538  C CB  . SER A 1018 ? 0.2400 0.2172 0.2254 0.0250  -0.0156 -0.0352 1016 SER A CB  
7539  O OG  . SER A 1018 ? 0.2328 0.2049 0.2224 0.0228  -0.0166 -0.0334 1016 SER A OG  
7540  N N   . GLY A 1019 ? 0.2272 0.2148 0.2093 0.0295  -0.0178 -0.0434 1017 GLY A N   
7541  C CA  . GLY A 1019 ? 0.2436 0.2378 0.2210 0.0318  -0.0167 -0.0446 1017 GLY A CA  
7542  C C   . GLY A 1019 ? 0.2312 0.2276 0.2073 0.0316  -0.0173 -0.0447 1017 GLY A C   
7543  O O   . GLY A 1019 ? 0.2537 0.2465 0.2314 0.0293  -0.0177 -0.0424 1017 GLY A O   
7544  N N   . THR A 1020 ? 0.2451 0.2480 0.2184 0.0340  -0.0174 -0.0474 1018 THR A N   
7545  C CA  . THR A 1020 ? 0.2445 0.2506 0.2154 0.0341  -0.0175 -0.0468 1018 THR A CA  
7546  C C   . THR A 1020 ? 0.2394 0.2486 0.2056 0.0339  -0.0145 -0.0419 1018 THR A C   
7547  O O   . THR A 1020 ? 0.2464 0.2567 0.2111 0.0332  -0.0143 -0.0399 1018 THR A O   
7548  C CB  . THR A 1020 ? 0.2465 0.2591 0.2167 0.0369  -0.0192 -0.0522 1018 THR A CB  
7549  O OG1 . THR A 1020 ? 0.2468 0.2652 0.2137 0.0393  -0.0177 -0.0531 1018 THR A OG1 
7550  C CG2 . THR A 1020 ? 0.2884 0.2981 0.2640 0.0373  -0.0226 -0.0576 1018 THR A CG2 
7551  N N   . GLY A 1021 ? 0.2549 0.2657 0.2189 0.0346  -0.0125 -0.0402 1019 GLY A N   
7552  C CA  . GLY A 1021 ? 0.2593 0.2745 0.2192 0.0350  -0.0102 -0.0361 1019 GLY A CA  
7553  C C   . GLY A 1021 ? 0.2596 0.2831 0.2165 0.0374  -0.0106 -0.0383 1019 GLY A C   
7554  O O   . GLY A 1021 ? 0.2564 0.2823 0.2144 0.0389  -0.0128 -0.0435 1019 GLY A O   
7555  N N   . PRO A 1022 ? 0.2457 0.2741 0.1990 0.0378  -0.0087 -0.0345 1020 PRO A N   
7556  C CA  . PRO A 1022 ? 0.2494 0.2757 0.2018 0.0363  -0.0064 -0.0286 1020 PRO A CA  
7557  C C   . PRO A 1022 ? 0.2485 0.2739 0.2012 0.0366  -0.0051 -0.0283 1020 PRO A C   
7558  O O   . PRO A 1022 ? 0.2753 0.3031 0.2283 0.0383  -0.0057 -0.0323 1020 PRO A O   
7559  C CB  . PRO A 1022 ? 0.2583 0.2922 0.2073 0.0374  -0.0054 -0.0257 1020 PRO A CB  
7560  C CG  . PRO A 1022 ? 0.2893 0.3309 0.2366 0.0400  -0.0065 -0.0303 1020 PRO A CG  
7561  C CD  . PRO A 1022 ? 0.2412 0.2787 0.1914 0.0400  -0.0090 -0.0358 1020 PRO A CD  
7562  N N   . LYS A 1023 ? 0.2381 0.2601 0.1909 0.0350  -0.0033 -0.0236 1021 LYS A N   
7563  C CA  . LYS A 1023 ? 0.2224 0.2429 0.1757 0.0350  -0.0020 -0.0228 1021 LYS A CA  
7564  C C   . LYS A 1023 ? 0.2372 0.2657 0.1879 0.0370  -0.0008 -0.0226 1021 LYS A C   
7565  O O   . LYS A 1023 ? 0.2418 0.2756 0.1902 0.0374  0.0001  -0.0192 1021 LYS A O   
7566  C CB  . LYS A 1023 ? 0.2206 0.2365 0.1747 0.0329  -0.0004 -0.0178 1021 LYS A CB  
7567  C CG  . LYS A 1023 ? 0.2245 0.2328 0.1814 0.0307  -0.0011 -0.0177 1021 LYS A CG  
7568  C CD  . LYS A 1023 ? 0.2269 0.2324 0.1842 0.0290  0.0006  -0.0130 1021 LYS A CD  
7569  C CE  . LYS A 1023 ? 0.2389 0.2375 0.1988 0.0269  0.0003  -0.0127 1021 LYS A CE  
7570  N NZ  . LYS A 1023 ? 0.2342 0.2296 0.1955 0.0265  0.0003  -0.0139 1021 LYS A NZ  
7571  N N   . ALA A 1024 ? 0.2475 0.2768 0.1989 0.0383  -0.0010 -0.0258 1022 ALA A N   
7572  C CA  . ALA A 1024 ? 0.2611 0.2972 0.2105 0.0398  0.0006  -0.0249 1022 ALA A CA  
7573  C C   . ALA A 1024 ? 0.2351 0.2695 0.1843 0.0382  0.0027  -0.0188 1022 ALA A C   
7574  O O   . ALA A 1024 ? 0.2392 0.2661 0.1905 0.0362  0.0030  -0.0168 1022 ALA A O   
7575  C CB  . ALA A 1024 ? 0.2509 0.2867 0.2019 0.0412  -0.0001 -0.0296 1022 ALA A CB  
7576  N N   . GLY A 1025 ? 0.2430 0.2848 0.1898 0.0391  0.0041  -0.0157 1023 GLY A N   
7577  C CA  . GLY A 1025 ? 0.2513 0.2920 0.1985 0.0377  0.0060  -0.0099 1023 GLY A CA  
7578  C C   . GLY A 1025 ? 0.2453 0.2822 0.1932 0.0358  0.0060  -0.0057 1023 GLY A C   
7579  O O   . GLY A 1025 ? 0.2319 0.2654 0.1814 0.0343  0.0070  -0.0015 1023 GLY A O   
7580  N N   . GLY A 1026 ? 0.2169 0.2545 0.1642 0.0360  0.0047  -0.0070 1024 GLY A N   
7581  C CA  . GLY A 1026 ? 0.2168 0.2513 0.1650 0.0344  0.0044  -0.0036 1024 GLY A CA  
7582  C C   . GLY A 1026 ? 0.2235 0.2653 0.1697 0.0355  0.0039  -0.0024 1024 GLY A C   
7583  O O   . GLY A 1026 ? 0.2280 0.2771 0.1718 0.0374  0.0036  -0.0047 1024 GLY A O   
7584  N N   . PRO A 1027 ? 0.2141 0.2541 0.1614 0.0343  0.0037  0.0012  1025 PRO A N   
7585  C CA  . PRO A 1027 ? 0.2306 0.2778 0.1763 0.0350  0.0033  0.0041  1025 PRO A CA  
7586  C C   . PRO A 1027 ? 0.1882 0.2380 0.1324 0.0360  0.0017  0.0003  1025 PRO A C   
7587  O O   . PRO A 1027 ? 0.2229 0.2796 0.1653 0.0368  0.0013  0.0022  1025 PRO A O   
7588  C CB  . PRO A 1027 ? 0.2491 0.2921 0.1976 0.0332  0.0035  0.0093  1025 PRO A CB  
7589  C CG  . PRO A 1027 ? 0.2457 0.2792 0.1966 0.0318  0.0033  0.0070  1025 PRO A CG  
7590  C CD  . PRO A 1027 ? 0.2124 0.2444 0.1627 0.0322  0.0039  0.0036  1025 PRO A CD  
7591  N N   . LEU A 1028 ? 0.2134 0.2579 0.1584 0.0359  0.0006  -0.0047 1026 LEU A N   
7592  C CA  . LEU A 1028 ? 0.2211 0.2678 0.1651 0.0368  -0.0012 -0.0086 1026 LEU A CA  
7593  C C   . LEU A 1028 ? 0.2204 0.2728 0.1624 0.0390  -0.0018 -0.0138 1026 LEU A C   
7594  O O   . LEU A 1028 ? 0.2417 0.2975 0.1828 0.0401  -0.0034 -0.0174 1026 LEU A O   
7595  C CB  . LEU A 1028 ? 0.2268 0.2652 0.1734 0.0354  -0.0024 -0.0111 1026 LEU A CB  
7596  C CG  . LEU A 1028 ? 0.2705 0.3046 0.2191 0.0336  -0.0022 -0.0071 1026 LEU A CG  
7597  C CD1 . LEU A 1028 ? 0.2830 0.3094 0.2342 0.0321  -0.0030 -0.0096 1026 LEU A CD1 
7598  C CD2 . LEU A 1028 ? 0.3652 0.4048 0.3125 0.0343  -0.0030 -0.0054 1026 LEU A CD2 
7599  N N   . TYR A 1029 ? 0.2191 0.2732 0.1606 0.0397  -0.0007 -0.0143 1027 TYR A N   
7600  C CA  . TYR A 1029 ? 0.2275 0.2857 0.1682 0.0418  -0.0015 -0.0202 1027 TYR A CA  
7601  C C   . TYR A 1029 ? 0.2190 0.2885 0.1564 0.0440  -0.0019 -0.0214 1027 TYR A C   
7602  O O   . TYR A 1029 ? 0.2369 0.3091 0.1739 0.0455  -0.0037 -0.0270 1027 TYR A O   
7603  C CB  . TYR A 1029 ? 0.2376 0.2955 0.1786 0.0420  0.0001  -0.0197 1027 TYR A CB  
7604  C CG  . TYR A 1029 ? 0.2270 0.2854 0.1687 0.0437  -0.0008 -0.0259 1027 TYR A CG  
7605  C CD1 . TYR A 1029 ? 0.2298 0.2803 0.1746 0.0431  -0.0024 -0.0301 1027 TYR A CD1 
7606  C CD2 . TYR A 1029 ? 0.2321 0.2990 0.1719 0.0458  0.0000  -0.0274 1027 TYR A CD2 
7607  C CE1 . TYR A 1029 ? 0.2341 0.2847 0.1805 0.0446  -0.0034 -0.0356 1027 TYR A CE1 
7608  C CE2 . TYR A 1029 ? 0.2455 0.3128 0.1866 0.0475  -0.0008 -0.0334 1027 TYR A CE2 
7609  C CZ  . TYR A 1029 ? 0.2412 0.2999 0.1858 0.0469  -0.0027 -0.0375 1027 TYR A CZ  
7610  O OH  . TYR A 1029 ? 0.2633 0.3221 0.2100 0.0485  -0.0038 -0.0433 1027 TYR A OH  
7611  N N   . LEU A 1030 ? 0.2216 0.2981 0.1568 0.0442  -0.0004 -0.0163 1028 LEU A N   
7612  C CA  . LEU A 1030 ? 0.2215 0.3101 0.1534 0.0463  -0.0007 -0.0172 1028 LEU A CA  
7613  C C   . LEU A 1030 ? 0.2447 0.3347 0.1759 0.0465  -0.0026 -0.0186 1028 LEU A C   
7614  O O   . LEU A 1030 ? 0.2447 0.3429 0.1737 0.0486  -0.0037 -0.0227 1028 LEU A O   
7615  C CB  . LEU A 1030 ? 0.2409 0.3369 0.1711 0.0461  0.0011  -0.0103 1028 LEU A CB  
7616  C CG  . LEU A 1030 ? 0.2423 0.3390 0.1729 0.0460  0.0030  -0.0085 1028 LEU A CG  
7617  C CD1 . LEU A 1030 ? 0.2974 0.4022 0.2266 0.0457  0.0045  -0.0011 1028 LEU A CD1 
7618  C CD2 . LEU A 1030 ? 0.2795 0.3811 0.2088 0.0485  0.0028  -0.0152 1028 LEU A CD2 
7619  N N   . GLY A 1031 ? 0.2305 0.3131 0.1638 0.0445  -0.0030 -0.0156 1029 GLY A N   
7620  C CA  . GLY A 1031 ? 0.2512 0.3350 0.1840 0.0446  -0.0047 -0.0165 1029 GLY A CA  
7621  C C   . GLY A 1031 ? 0.2483 0.3309 0.1816 0.0458  -0.0068 -0.0242 1029 GLY A C   
7622  O O   . GLY A 1031 ? 0.2628 0.3495 0.1951 0.0466  -0.0084 -0.0261 1029 GLY A O   
7623  N N   . ARG A 1032 ? 0.2334 0.3104 0.1688 0.0459  -0.0071 -0.0286 1030 ARG A N   
7624  C CA  . ARG A 1032 ? 0.2245 0.3001 0.1614 0.0470  -0.0094 -0.0359 1030 ARG A CA  
7625  C C   . ARG A 1032 ? 0.2378 0.3241 0.1723 0.0500  -0.0101 -0.0409 1030 ARG A C   
7626  O O   . ARG A 1032 ? 0.2792 0.3665 0.2148 0.0513  -0.0124 -0.0473 1030 ARG A O   
7627  C CB  . ARG A 1032 ? 0.2663 0.3323 0.2069 0.0459  -0.0095 -0.0382 1030 ARG A CB  
7628  C CG  . ARG A 1032 ? 0.2531 0.3150 0.1968 0.0463  -0.0122 -0.0448 1030 ARG A CG  
7629  C CD  . ARG A 1032 ? 0.2651 0.3219 0.2105 0.0446  -0.0135 -0.0438 1030 ARG A CD  
7630  N NE  . ARG A 1032 ? 0.2663 0.3180 0.2157 0.0445  -0.0160 -0.0494 1030 ARG A NE  
7631  C CZ  . ARG A 1032 ? 0.2992 0.3525 0.2496 0.0451  -0.0184 -0.0532 1030 ARG A CZ  
7632  N NH1 . ARG A 1032 ? 0.3086 0.3689 0.2559 0.0460  -0.0186 -0.0524 1030 ARG A NH1 
7633  N NH2 . ARG A 1032 ? 0.3139 0.3617 0.2688 0.0447  -0.0207 -0.0577 1030 ARG A NH2 
7634  N N   . LEU A 1033 ? 0.2262 0.3208 0.1578 0.0511  -0.0083 -0.0382 1031 LEU A N   
7635  C CA  . LEU A 1033 ? 0.2397 0.3453 0.1689 0.0540  -0.0086 -0.0430 1031 LEU A CA  
7636  C C   . LEU A 1033 ? 0.2415 0.3590 0.1667 0.0553  -0.0087 -0.0413 1031 LEU A C   
7637  O O   . LEU A 1033 ? 0.2563 0.3852 0.1788 0.0577  -0.0085 -0.0440 1031 LEU A O   
7638  C CB  . LEU A 1033 ? 0.2358 0.3435 0.1645 0.0545  -0.0064 -0.0414 1031 LEU A CB  
7639  C CG  . LEU A 1033 ? 0.2558 0.3517 0.1884 0.0530  -0.0062 -0.0422 1031 LEU A CG  
7640  C CD1 . LEU A 1033 ? 0.2506 0.3489 0.1827 0.0534  -0.0040 -0.0404 1031 LEU A CD1 
7641  C CD2 . LEU A 1033 ? 0.2687 0.3597 0.2046 0.0539  -0.0088 -0.0501 1031 LEU A CD2 
7642  N N   . VAL A 1034 ? 0.2375 0.3532 0.1625 0.0538  -0.0091 -0.0369 1032 VAL A N   
7643  C CA  . VAL A 1034 ? 0.2502 0.3763 0.1719 0.0547  -0.0096 -0.0350 1032 VAL A CA  
7644  C C   . VAL A 1034 ? 0.2772 0.3988 0.2004 0.0541  -0.0119 -0.0374 1032 VAL A C   
7645  O O   . VAL A 1034 ? 0.2742 0.3844 0.2009 0.0525  -0.0126 -0.0384 1032 VAL A O   
7646  C CB  . VAL A 1034 ? 0.2663 0.3957 0.1864 0.0532  -0.0076 -0.0256 1032 VAL A CB  
7647  C CG1 . VAL A 1034 ? 0.2658 0.4022 0.1842 0.0540  -0.0054 -0.0233 1032 VAL A CG1 
7648  C CG2 . VAL A 1034 ? 0.2492 0.3659 0.1728 0.0503  -0.0071 -0.0205 1032 VAL A CG2 
7649  N N   . THR A 1035 ? 0.2794 0.4108 0.1999 0.0555  -0.0131 -0.0382 1033 THR A N   
7650  C CA  . THR A 1035 ? 0.2890 0.4171 0.2109 0.0552  -0.0155 -0.0411 1033 THR A CA  
7651  C C   . THR A 1035 ? 0.3578 0.4788 0.2812 0.0526  -0.0151 -0.0344 1033 THR A C   
7652  O O   . THR A 1035 ? 0.4038 0.5169 0.3300 0.0515  -0.0167 -0.0363 1033 THR A O   
7653  C CB  . THR A 1035 ? 0.3409 0.4818 0.2595 0.0577  -0.0171 -0.0446 1033 THR A CB  
7654  O OG1 . THR A 1035 ? 0.4721 0.6235 0.3869 0.0579  -0.0155 -0.0380 1033 THR A OG1 
7655  C CG2 . THR A 1035 ? 0.3363 0.4830 0.2544 0.0604  -0.0179 -0.0529 1033 THR A CG2 
7656  N N   . THR A 1036 ? 0.2945 0.4183 0.2165 0.0516  -0.0133 -0.0265 1034 THR A N   
7657  C CA  . THR A 1036 ? 0.3022 0.4194 0.2263 0.0492  -0.0129 -0.0200 1034 THR A CA  
7658  C C   . THR A 1036 ? 0.3197 0.4311 0.2453 0.0476  -0.0106 -0.0149 1034 THR A C   
7659  O O   . THR A 1036 ? 0.3265 0.4448 0.2503 0.0481  -0.0091 -0.0111 1034 THR A O   
7660  C CB  . THR A 1036 ? 0.3690 0.4956 0.2908 0.0495  -0.0133 -0.0147 1034 THR A CB  
7661  O OG1 . THR A 1036 ? 0.4026 0.5354 0.3228 0.0511  -0.0155 -0.0197 1034 THR A OG1 
7662  C CG2 . THR A 1036 ? 0.3878 0.5072 0.3126 0.0472  -0.0131 -0.0082 1034 THR A CG2 
7663  N N   . ALA A 1037 ? 0.3153 0.4148 0.2445 0.0458  -0.0105 -0.0148 1035 ALA A N   
7664  C CA  . ALA A 1037 ? 0.3119 0.4055 0.2428 0.0444  -0.0085 -0.0112 1035 ALA A CA  
7665  C C   . ALA A 1037 ? 0.2908 0.3859 0.2222 0.0431  -0.0074 -0.0029 1035 ALA A C   
7666  O O   . ALA A 1037 ? 0.3071 0.4011 0.2397 0.0423  -0.0084 -0.0001 1035 ALA A O   
7667  C CB  . ALA A 1037 ? 0.3241 0.4052 0.2585 0.0427  -0.0087 -0.0134 1035 ALA A CB  
7668  N N   . PRO A 1038 ? 0.2697 0.3674 0.2008 0.0429  -0.0056 0.0012  1036 PRO A N   
7669  C CA  . PRO A 1038 ? 0.2500 0.3475 0.1828 0.0415  -0.0048 0.0093  1036 PRO A CA  
7670  C C   . PRO A 1038 ? 0.2664 0.3518 0.2034 0.0394  -0.0046 0.0106  1036 PRO A C   
7671  O O   . PRO A 1038 ? 0.2545 0.3321 0.1927 0.0390  -0.0047 0.0060  1036 PRO A O   
7672  C CB  . PRO A 1038 ? 0.3038 0.4071 0.2352 0.0419  -0.0030 0.0121  1036 PRO A CB  
7673  C CG  . PRO A 1038 ? 0.3121 0.4116 0.2430 0.0427  -0.0025 0.0056  1036 PRO A CG  
7674  C CD  . PRO A 1038 ? 0.2690 0.3690 0.1986 0.0440  -0.0044 -0.0014 1036 PRO A CD  
7675  N N   . VAL A 1039 ? 0.2690 0.3532 0.2086 0.0381  -0.0043 0.0173  1037 VAL A N   
7676  C CA  . VAL A 1039 ? 0.2475 0.3213 0.1914 0.0363  -0.0039 0.0191  1037 VAL A CA  
7677  C C   . VAL A 1039 ? 0.2421 0.3141 0.1867 0.0357  -0.0022 0.0208  1037 VAL A C   
7678  O O   . VAL A 1039 ? 0.2474 0.3250 0.1921 0.0357  -0.0014 0.0261  1037 VAL A O   
7679  C CB  . VAL A 1039 ? 0.2590 0.3326 0.2062 0.0353  -0.0048 0.0251  1037 VAL A CB  
7680  C CG1 . VAL A 1039 ? 0.2908 0.3542 0.2427 0.0336  -0.0045 0.0262  1037 VAL A CG1 
7681  C CG2 . VAL A 1039 ? 0.3071 0.3836 0.2534 0.0359  -0.0066 0.0236  1037 VAL A CG2 
7682  N N   . PRO A 1040 ? 0.2439 0.3085 0.1892 0.0353  -0.0015 0.0169  1038 PRO A N   
7683  C CA  . PRO A 1040 ? 0.2525 0.3155 0.1985 0.0348  0.0001  0.0184  1038 PRO A CA  
7684  C C   . PRO A 1040 ? 0.2368 0.2967 0.1868 0.0333  0.0006  0.0247  1038 PRO A C   
7685  O O   . PRO A 1040 ? 0.2312 0.2872 0.1842 0.0324  -0.0004 0.0265  1038 PRO A O   
7686  C CB  . PRO A 1040 ? 0.2588 0.3135 0.2054 0.0344  0.0003  0.0129  1038 PRO A CB  
7687  C CG  . PRO A 1040 ? 0.2818 0.3365 0.2271 0.0351  -0.0012 0.0079  1038 PRO A CG  
7688  C CD  . PRO A 1040 ? 0.2603 0.3183 0.2059 0.0351  -0.0023 0.0110  1038 PRO A CD  
7689  N N   . PRO A 1041 ? 0.2311 0.2923 0.1817 0.0330  0.0019  0.0278  1039 PRO A N   
7690  C CA  . PRO A 1041 ? 0.2305 0.2877 0.1857 0.0314  0.0021  0.0332  1039 PRO A CA  
7691  C C   . PRO A 1041 ? 0.2265 0.2733 0.1847 0.0303  0.0019  0.0306  1039 PRO A C   
7692  O O   . PRO A 1041 ? 0.2442 0.2866 0.2011 0.0303  0.0022  0.0254  1039 PRO A O   
7693  C CB  . PRO A 1041 ? 0.2600 0.3196 0.2149 0.0314  0.0037  0.0350  1039 PRO A CB  
7694  C CG  . PRO A 1041 ? 0.3030 0.3712 0.2529 0.0332  0.0042  0.0324  1039 PRO A CG  
7695  C CD  . PRO A 1041 ? 0.2744 0.3408 0.2220 0.0341  0.0032  0.0262  1039 PRO A CD  
7696  N N   . GLN A 1042 ? 0.2069 0.2503 0.1696 0.0292  0.0011  0.0342  1040 GLN A N   
7697  C CA  . GLN A 1042 ? 0.2213 0.2558 0.1876 0.0281  0.0008  0.0324  1040 GLN A CA  
7698  C C   . GLN A 1042 ? 0.2250 0.2561 0.1899 0.0282  0.0001  0.0271  1040 GLN A C   
7699  O O   . GLN A 1042 ? 0.2443 0.2687 0.2115 0.0273  0.0001  0.0250  1040 GLN A O   
7700  C CB  . GLN A 1042 ? 0.2639 0.2937 0.2313 0.0273  0.0021  0.0316  1040 GLN A CB  
7701  C CG  . GLN A 1042 ? 0.3446 0.3773 0.3140 0.0270  0.0028  0.0368  1040 GLN A CG  
7702  C CD  . GLN A 1042 ? 0.4122 0.4398 0.3829 0.0262  0.0040  0.0358  1040 GLN A CD  
7703  O OE1 . GLN A 1042 ? 0.4988 0.5276 0.4663 0.0267  0.0051  0.0335  1040 GLN A OE1 
7704  N NE2 . GLN A 1042 ? 0.4954 0.5173 0.4709 0.0251  0.0036  0.0371  1040 GLN A NE2 
7705  N N   . HIS A 1043 ? 0.2166 0.2525 0.1781 0.0293  -0.0005 0.0251  1041 HIS A N   
7706  C CA  . HIS A 1043 ? 0.2156 0.2486 0.1756 0.0294  -0.0012 0.0198  1041 HIS A CA  
7707  C C   . HIS A 1043 ? 0.2265 0.2588 0.1889 0.0292  -0.0027 0.0208  1041 HIS A C   
7708  O O   . HIS A 1043 ? 0.2184 0.2563 0.1795 0.0300  -0.0036 0.0220  1041 HIS A O   
7709  C CB  . HIS A 1043 ? 0.2279 0.2665 0.1834 0.0308  -0.0014 0.0164  1041 HIS A CB  
7710  C CG  . HIS A 1043 ? 0.2190 0.2549 0.1736 0.0310  -0.0024 0.0110  1041 HIS A CG  
7711  N ND1 . HIS A 1043 ? 0.2220 0.2530 0.1764 0.0306  -0.0020 0.0067  1041 HIS A ND1 
7712  C CD2 . HIS A 1043 ? 0.2290 0.2668 0.1830 0.0314  -0.0038 0.0094  1041 HIS A CD2 
7713  C CE1 . HIS A 1043 ? 0.2415 0.2713 0.1955 0.0306  -0.0033 0.0029  1041 HIS A CE1 
7714  N NE2 . HIS A 1043 ? 0.2399 0.2737 0.1935 0.0312  -0.0043 0.0042  1041 HIS A NE2 
7715  N N   . SER A 1044 ? 0.2198 0.2456 0.1858 0.0280  -0.0028 0.0203  1042 SER A N   
7716  C CA  . SER A 1044 ? 0.1963 0.2208 0.1651 0.0278  -0.0041 0.0205  1042 SER A CA  
7717  C C   . SER A 1044 ? 0.2051 0.2226 0.1769 0.0266  -0.0038 0.0182  1042 SER A C   
7718  O O   . SER A 1044 ? 0.2300 0.2441 0.2021 0.0260  -0.0027 0.0176  1042 SER A O   
7719  C CB  . SER A 1044 ? 0.2255 0.2528 0.1975 0.0279  -0.0050 0.0260  1042 SER A CB  
7720  O OG  . SER A 1044 ? 0.2329 0.2570 0.2087 0.0271  -0.0044 0.0289  1042 SER A OG  
7721  N N   . SER A 1045 ? 0.2103 0.2261 0.1845 0.0264  -0.0048 0.0171  1043 SER A N   
7722  C CA  . SER A 1045 ? 0.2103 0.2205 0.1876 0.0253  -0.0046 0.0152  1043 SER A CA  
7723  C C   . SER A 1045 ? 0.2052 0.2154 0.1867 0.0254  -0.0059 0.0163  1043 SER A C   
7724  O O   . SER A 1045 ? 0.2067 0.2198 0.1873 0.0260  -0.0070 0.0161  1043 SER A O   
7725  C CB  . SER A 1045 ? 0.2344 0.2424 0.2096 0.0248  -0.0042 0.0105  1043 SER A CB  
7726  O OG  . SER A 1045 ? 0.2273 0.2312 0.2056 0.0237  -0.0040 0.0090  1043 SER A OG  
7727  N N   . VAL A 1046 ? 0.2137 0.2205 0.1998 0.0249  -0.0059 0.0170  1044 VAL A N   
7728  C CA  . VAL A 1046 ? 0.2334 0.2398 0.2241 0.0250  -0.0072 0.0173  1044 VAL A CA  
7729  C C   . VAL A 1046 ? 0.2190 0.2235 0.2098 0.0245  -0.0072 0.0130  1044 VAL A C   
7730  O O   . VAL A 1046 ? 0.2367 0.2413 0.2312 0.0247  -0.0083 0.0126  1044 VAL A O   
7731  C CB  . VAL A 1046 ? 0.2383 0.2423 0.2350 0.0249  -0.0076 0.0196  1044 VAL A CB  
7732  C CG1 . VAL A 1046 ? 0.2659 0.2723 0.2635 0.0253  -0.0079 0.0248  1044 VAL A CG1 
7733  C CG2 . VAL A 1046 ? 0.2585 0.2586 0.2562 0.0241  -0.0064 0.0170  1044 VAL A CG2 
7734  N N   . HIS A 1047 ? 0.2098 0.2130 0.1971 0.0238  -0.0061 0.0099  1045 HIS A N   
7735  C CA  . HIS A 1047 ? 0.2321 0.2338 0.2199 0.0231  -0.0060 0.0062  1045 HIS A CA  
7736  C C   . HIS A 1047 ? 0.2298 0.2339 0.2150 0.0233  -0.0069 0.0047  1045 HIS A C   
7737  O O   . HIS A 1047 ? 0.2272 0.2334 0.2087 0.0238  -0.0070 0.0050  1045 HIS A O   
7738  C CB  . HIS A 1047 ? 0.2625 0.2616 0.2487 0.0220  -0.0046 0.0042  1045 HIS A CB  
7739  C CG  . HIS A 1047 ? 0.2891 0.2861 0.2777 0.0218  -0.0039 0.0056  1045 HIS A CG  
7740  N ND1 . HIS A 1047 ? 0.3171 0.3129 0.3105 0.0217  -0.0041 0.0052  1045 HIS A ND1 
7741  C CD2 . HIS A 1047 ? 0.3309 0.3271 0.3184 0.0219  -0.0031 0.0074  1045 HIS A CD2 
7742  C CE1 . HIS A 1047 ? 0.3424 0.3364 0.3374 0.0217  -0.0036 0.0065  1045 HIS A CE1 
7743  N NE2 . HIS A 1047 ? 0.3430 0.3372 0.3345 0.0217  -0.0029 0.0080  1045 HIS A NE2 
7744  N N   . THR A 1048 ? 0.2173 0.2214 0.2045 0.0229  -0.0075 0.0028  1046 THR A N   
7745  C CA  . THR A 1048 ? 0.2205 0.2268 0.2060 0.0230  -0.0085 0.0011  1046 THR A CA  
7746  C C   . THR A 1048 ? 0.2272 0.2320 0.2127 0.0217  -0.0080 -0.0022 1046 THR A C   
7747  O O   . THR A 1048 ? 0.2496 0.2532 0.2380 0.0210  -0.0075 -0.0031 1046 THR A O   
7748  C CB  . THR A 1048 ? 0.2137 0.2221 0.2022 0.0238  -0.0099 0.0021  1046 THR A CB  
7749  O OG1 . THR A 1048 ? 0.2508 0.2606 0.2402 0.0248  -0.0104 0.0058  1046 THR A OG1 
7750  C CG2 . THR A 1048 ? 0.2464 0.2574 0.2327 0.0240  -0.0110 0.0006  1046 THR A CG2 
7751  N N   . ASP A 1049 ? 0.2225 0.2277 0.2049 0.0213  -0.0083 -0.0039 1047 ASP A N   
7752  C CA  . ASP A 1049 ? 0.2068 0.2107 0.1896 0.0198  -0.0081 -0.0064 1047 ASP A CA  
7753  C C   . ASP A 1049 ? 0.2152 0.2205 0.2010 0.0194  -0.0088 -0.0074 1047 ASP A C   
7754  O O   . ASP A 1049 ? 0.2152 0.2228 0.2013 0.0203  -0.0101 -0.0072 1047 ASP A O   
7755  C CB  . ASP A 1049 ? 0.2070 0.2112 0.1869 0.0197  -0.0088 -0.0080 1047 ASP A CB  
7756  C CG  . ASP A 1049 ? 0.2302 0.2330 0.2110 0.0180  -0.0089 -0.0101 1047 ASP A CG  
7757  O OD1 . ASP A 1049 ? 0.2310 0.2351 0.2135 0.0175  -0.0098 -0.0112 1047 ASP A OD1 
7758  O OD2 . ASP A 1049 ? 0.2416 0.2422 0.2217 0.0171  -0.0081 -0.0104 1047 ASP A OD2 
7759  N N   . PRO A 1050 ? 0.1938 0.1984 0.1819 0.0182  -0.0081 -0.0084 1048 PRO A N   
7760  C CA  . PRO A 1050 ? 0.2080 0.2146 0.1994 0.0180  -0.0086 -0.0094 1048 PRO A CA  
7761  C C   . PRO A 1050 ? 0.2056 0.2136 0.1966 0.0172  -0.0097 -0.0109 1048 PRO A C   
7762  O O   . PRO A 1050 ? 0.2205 0.2308 0.2137 0.0175  -0.0106 -0.0114 1048 PRO A O   
7763  C CB  . PRO A 1050 ? 0.2403 0.2464 0.2338 0.0169  -0.0073 -0.0102 1048 PRO A CB  
7764  C CG  . PRO A 1050 ? 0.2284 0.2322 0.2192 0.0160  -0.0064 -0.0101 1048 PRO A CG  
7765  C CD  . PRO A 1050 ? 0.2181 0.2206 0.2061 0.0171  -0.0067 -0.0087 1048 PRO A CD  
7766  N N   . VAL A 1051 ? 0.1972 0.2041 0.1860 0.0163  -0.0098 -0.0117 1049 VAL A N   
7767  C CA  . VAL A 1051 ? 0.2183 0.2264 0.2074 0.0155  -0.0111 -0.0132 1049 VAL A CA  
7768  C C   . VAL A 1051 ? 0.2064 0.2159 0.1939 0.0171  -0.0126 -0.0133 1049 VAL A C   
7769  O O   . VAL A 1051 ? 0.2224 0.2340 0.2112 0.0170  -0.0139 -0.0142 1049 VAL A O   
7770  C CB  . VAL A 1051 ? 0.2086 0.2147 0.1966 0.0141  -0.0111 -0.0141 1049 VAL A CB  
7771  C CG1 . VAL A 1051 ? 0.2623 0.2695 0.2515 0.0132  -0.0128 -0.0156 1049 VAL A CG1 
7772  C CG2 . VAL A 1051 ? 0.2143 0.2196 0.2037 0.0125  -0.0097 -0.0136 1049 VAL A CG2 
7773  N N   . LEU A 1052 ? 0.1993 0.2085 0.1842 0.0185  -0.0124 -0.0122 1050 LEU A N   
7774  C CA  . LEU A 1052 ? 0.1993 0.2110 0.1827 0.0201  -0.0137 -0.0117 1050 LEU A CA  
7775  C C   . LEU A 1052 ? 0.2227 0.2365 0.2088 0.0207  -0.0142 -0.0107 1050 LEU A C   
7776  O O   . LEU A 1052 ? 0.1967 0.2129 0.1832 0.0212  -0.0157 -0.0113 1050 LEU A O   
7777  C CB  . LEU A 1052 ? 0.2121 0.2238 0.1927 0.0214  -0.0131 -0.0100 1050 LEU A CB  
7778  C CG  . LEU A 1052 ? 0.2110 0.2262 0.1896 0.0231  -0.0141 -0.0088 1050 LEU A CG  
7779  C CD1 . LEU A 1052 ? 0.2129 0.2298 0.1940 0.0239  -0.0144 -0.0062 1050 LEU A CD1 
7780  C CD2 . LEU A 1052 ? 0.2175 0.2351 0.1949 0.0234  -0.0158 -0.0114 1050 LEU A CD2 
7781  N N   . LEU A 1053 ? 0.2107 0.2235 0.1990 0.0207  -0.0132 -0.0092 1051 LEU A N   
7782  C CA  . LEU A 1053 ? 0.2087 0.2233 0.2005 0.0214  -0.0138 -0.0084 1051 LEU A CA  
7783  C C   . LEU A 1053 ? 0.1915 0.2075 0.1855 0.0205  -0.0145 -0.0104 1051 LEU A C   
7784  O O   . LEU A 1053 ? 0.2083 0.2267 0.2036 0.0213  -0.0159 -0.0103 1051 LEU A O   
7785  C CB  . LEU A 1053 ? 0.2275 0.2405 0.2221 0.0216  -0.0127 -0.0072 1051 LEU A CB  
7786  C CG  . LEU A 1053 ? 0.2377 0.2498 0.2312 0.0227  -0.0124 -0.0044 1051 LEU A CG  
7787  C CD1 . LEU A 1053 ? 0.2439 0.2540 0.2408 0.0226  -0.0114 -0.0038 1051 LEU A CD1 
7788  C CD2 . LEU A 1053 ? 0.2659 0.2806 0.2596 0.0241  -0.0139 -0.0021 1051 LEU A CD2 
7789  N N   . ASP A 1054 ? 0.2047 0.2197 0.1992 0.0189  -0.0138 -0.0121 1052 ASP A N   
7790  C CA  . ASP A 1054 ? 0.2112 0.2282 0.2081 0.0178  -0.0144 -0.0137 1052 ASP A CA  
7791  C C   . ASP A 1054 ? 0.2078 0.2261 0.2033 0.0179  -0.0162 -0.0147 1052 ASP A C   
7792  O O   . ASP A 1054 ? 0.2247 0.2453 0.2222 0.0179  -0.0173 -0.0154 1052 ASP A O   
7793  C CB  . ASP A 1054 ? 0.2188 0.2349 0.2163 0.0158  -0.0133 -0.0148 1052 ASP A CB  
7794  C CG  . ASP A 1054 ? 0.2702 0.2863 0.2698 0.0156  -0.0117 -0.0145 1052 ASP A CG  
7795  O OD1 . ASP A 1054 ? 0.2441 0.2608 0.2456 0.0170  -0.0118 -0.0139 1052 ASP A OD1 
7796  O OD2 . ASP A 1054 ? 0.3074 0.3232 0.3071 0.0140  -0.0107 -0.0149 1052 ASP A OD2 
7797  N N   . PHE A 1055 ? 0.1989 0.2158 0.1910 0.0181  -0.0165 -0.0149 1053 PHE A N   
7798  C CA  . PHE A 1055 ? 0.2039 0.2224 0.1949 0.0184  -0.0183 -0.0163 1053 PHE A CA  
7799  C C   . PHE A 1055 ? 0.1998 0.2212 0.1904 0.0202  -0.0195 -0.0154 1053 PHE A C   
7800  O O   . PHE A 1055 ? 0.2147 0.2383 0.2062 0.0203  -0.0211 -0.0165 1053 PHE A O   
7801  C CB  . PHE A 1055 ? 0.2029 0.2197 0.1906 0.0186  -0.0184 -0.0171 1053 PHE A CB  
7802  C CG  . PHE A 1055 ? 0.2039 0.2224 0.1906 0.0191  -0.0204 -0.0192 1053 PHE A CG  
7803  C CD1 . PHE A 1055 ? 0.2463 0.2654 0.2355 0.0179  -0.0219 -0.0211 1053 PHE A CD1 
7804  C CD2 . PHE A 1055 ? 0.2203 0.2402 0.2036 0.0208  -0.0210 -0.0194 1053 PHE A CD2 
7805  C CE1 . PHE A 1055 ? 0.2636 0.2842 0.2522 0.0184  -0.0240 -0.0235 1053 PHE A CE1 
7806  C CE2 . PHE A 1055 ? 0.2330 0.2550 0.2153 0.0215  -0.0230 -0.0219 1053 PHE A CE2 
7807  C CZ  . PHE A 1055 ? 0.2526 0.2747 0.2377 0.0203  -0.0246 -0.0241 1053 PHE A CZ  
7808  N N   . ALA A 1056 ? 0.2082 0.2297 0.1977 0.0216  -0.0188 -0.0131 1054 ALA A N   
7809  C CA  . ALA A 1056 ? 0.2202 0.2447 0.2097 0.0232  -0.0200 -0.0115 1054 ALA A CA  
7810  C C   . ALA A 1056 ? 0.2310 0.2569 0.2245 0.0230  -0.0207 -0.0116 1054 ALA A C   
7811  O O   . ALA A 1056 ? 0.2250 0.2539 0.2189 0.0238  -0.0224 -0.0116 1054 ALA A O   
7812  C CB  . ALA A 1056 ? 0.2269 0.2511 0.2155 0.0243  -0.0192 -0.0084 1054 ALA A CB  
7813  N N   . LYS A 1057 ? 0.2279 0.2523 0.2246 0.0222  -0.0196 -0.0118 1055 LYS A N   
7814  C CA  . LYS A 1057 ? 0.2575 0.2838 0.2583 0.0221  -0.0202 -0.0123 1055 LYS A CA  
7815  C C   . LYS A 1057 ? 0.2311 0.2590 0.2325 0.0210  -0.0213 -0.0146 1055 LYS A C   
7816  O O   . LYS A 1057 ? 0.2546 0.2852 0.2581 0.0215  -0.0226 -0.0148 1055 LYS A O   
7817  C CB  . LYS A 1057 ? 0.2801 0.3051 0.2842 0.0215  -0.0187 -0.0126 1055 LYS A CB  
7818  C CG  . LYS A 1057 ? 0.2736 0.2975 0.2790 0.0228  -0.0182 -0.0104 1055 LYS A CG  
7819  C CD  . LYS A 1057 ? 0.2703 0.2938 0.2798 0.0224  -0.0171 -0.0114 1055 LYS A CD  
7820  C CE  . LYS A 1057 ? 0.2786 0.3006 0.2865 0.0208  -0.0154 -0.0129 1055 LYS A CE  
7821  N NZ  . LYS A 1057 ? 0.3161 0.3379 0.3274 0.0208  -0.0142 -0.0136 1055 LYS A NZ  
7822  N N   . TRP A 1058 ? 0.2211 0.2475 0.2210 0.0196  -0.0208 -0.0161 1056 TRP A N   
7823  C CA  . TRP A 1058 ? 0.2493 0.2770 0.2501 0.0184  -0.0221 -0.0180 1056 TRP A CA  
7824  C C   . TRP A 1058 ? 0.2318 0.2616 0.2309 0.0196  -0.0242 -0.0186 1056 TRP A C   
7825  O O   . TRP A 1058 ? 0.2544 0.2865 0.2554 0.0194  -0.0257 -0.0196 1056 TRP A O   
7826  C CB  . TRP A 1058 ? 0.2630 0.2884 0.2630 0.0166  -0.0215 -0.0191 1056 TRP A CB  
7827  C CG  . TRP A 1058 ? 0.2573 0.2836 0.2588 0.0152  -0.0231 -0.0209 1056 TRP A CG  
7828  C CD1 . TRP A 1058 ? 0.2968 0.3244 0.3019 0.0134  -0.0232 -0.0215 1056 TRP A CD1 
7829  C CD2 . TRP A 1058 ? 0.2762 0.3022 0.2760 0.0155  -0.0249 -0.0226 1056 TRP A CD2 
7830  N NE1 . TRP A 1058 ? 0.3257 0.3537 0.3318 0.0124  -0.0251 -0.0230 1056 TRP A NE1 
7831  C CE2 . TRP A 1058 ? 0.3297 0.3566 0.3327 0.0137  -0.0263 -0.0240 1056 TRP A CE2 
7832  C CE3 . TRP A 1058 ? 0.2741 0.2999 0.2703 0.0171  -0.0257 -0.0231 1056 TRP A CE3 
7833  C CZ2 . TRP A 1058 ? 0.3112 0.3380 0.3142 0.0136  -0.0285 -0.0261 1056 TRP A CZ2 
7834  C CZ3 . TRP A 1058 ? 0.3019 0.3282 0.2978 0.0171  -0.0277 -0.0256 1056 TRP A CZ3 
7835  C CH2 . TRP A 1058 ? 0.3160 0.3425 0.3155 0.0154  -0.0292 -0.0271 1056 TRP A CH2 
7836  N N   . LEU A 1059 ? 0.2270 0.2564 0.2223 0.0208  -0.0243 -0.0179 1057 LEU A N   
7837  C CA  . LEU A 1059 ? 0.2485 0.2808 0.2417 0.0222  -0.0262 -0.0185 1057 LEU A CA  
7838  C C   . LEU A 1059 ? 0.2536 0.2890 0.2487 0.0233  -0.0272 -0.0170 1057 LEU A C   
7839  O O   . LEU A 1059 ? 0.2657 0.3040 0.2613 0.0236  -0.0291 -0.0183 1057 LEU A O   
7840  C CB  . LEU A 1059 ? 0.2242 0.2565 0.2132 0.0235  -0.0258 -0.0176 1057 LEU A CB  
7841  C CG  . LEU A 1059 ? 0.2400 0.2702 0.2270 0.0228  -0.0256 -0.0198 1057 LEU A CG  
7842  C CD1 . LEU A 1059 ? 0.2337 0.2640 0.2168 0.0241  -0.0248 -0.0186 1057 LEU A CD1 
7843  C CD2 . LEU A 1059 ? 0.2723 0.3044 0.2593 0.0228  -0.0279 -0.0229 1057 LEU A CD2 
7844  N N   . ASP A 1060 ? 0.2378 0.2728 0.2344 0.0240  -0.0262 -0.0145 1058 ASP A N   
7845  C CA  . ASP A 1060 ? 0.3128 0.3505 0.3120 0.0250  -0.0273 -0.0129 1058 ASP A CA  
7846  C C   . ASP A 1060 ? 0.2871 0.3258 0.2902 0.0241  -0.0280 -0.0148 1058 ASP A C   
7847  O O   . ASP A 1060 ? 0.3365 0.3783 0.3409 0.0248  -0.0298 -0.0149 1058 ASP A O   
7848  C CB  . ASP A 1060 ? 0.2925 0.3289 0.2936 0.0258  -0.0263 -0.0101 1058 ASP A CB  
7849  C CG  . ASP A 1060 ? 0.2841 0.3220 0.2827 0.0273  -0.0267 -0.0070 1058 ASP A CG  
7850  O OD1 . ASP A 1060 ? 0.3606 0.4020 0.3569 0.0281  -0.0283 -0.0067 1058 ASP A OD1 
7851  O OD2 . ASP A 1060 ? 0.3791 0.4151 0.3781 0.0276  -0.0256 -0.0048 1058 ASP A OD2 
7852  N N   . GLY A 1061 ? 0.2892 0.3260 0.2943 0.0225  -0.0267 -0.0162 1059 GLY A N   
7853  C CA  . GLY A 1061 ? 0.2949 0.3335 0.3038 0.0214  -0.0272 -0.0178 1059 GLY A CA  
7854  C C   . GLY A 1061 ? 0.3223 0.3625 0.3305 0.0208  -0.0290 -0.0197 1059 GLY A C   
7855  O O   . GLY A 1061 ? 0.3354 0.3782 0.3466 0.0205  -0.0302 -0.0206 1059 GLY A O   
7856  N N   . LYS A 1062 ? 0.3058 0.3447 0.3105 0.0206  -0.0294 -0.0206 1060 LYS A N   
7857  C CA  . LYS A 1062 ? 0.3225 0.3628 0.3268 0.0202  -0.0314 -0.0229 1060 LYS A CA  
7858  C C   . LYS A 1062 ? 0.3264 0.3701 0.3290 0.0221  -0.0334 -0.0227 1060 LYS A C   
7859  O O   . LYS A 1062 ? 0.4025 0.4481 0.4051 0.0220  -0.0354 -0.0248 1060 LYS A O   
7860  C CB  . LYS A 1062 ? 0.3372 0.3749 0.3389 0.0195  -0.0313 -0.0244 1060 LYS A CB  
7861  C CG  . LYS A 1062 ? 0.3503 0.3852 0.3543 0.0172  -0.0301 -0.0248 1060 LYS A CG  
7862  C CD  . LYS A 1062 ? 0.4635 0.5001 0.4718 0.0155  -0.0312 -0.0260 1060 LYS A CD  
7863  C CE  . LYS A 1062 ? 0.4777 0.5125 0.4885 0.0130  -0.0300 -0.0257 1060 LYS A CE  
7864  N NZ  . LYS A 1062 ? 0.5195 0.5567 0.5348 0.0112  -0.0310 -0.0264 1060 LYS A NZ  
7865  N N   . GLY A 1063 ? 0.2819 0.3266 0.2833 0.0237  -0.0330 -0.0201 1061 GLY A N   
7866  C CA  . GLY A 1063 ? 0.3345 0.3831 0.3339 0.0255  -0.0347 -0.0192 1061 GLY A CA  
7867  C C   . GLY A 1063 ? 0.3720 0.4215 0.3664 0.0266  -0.0349 -0.0194 1061 GLY A C   
7868  O O   . GLY A 1063 ? 0.3584 0.4120 0.3508 0.0280  -0.0365 -0.0189 1061 GLY A O   
7869  N N   . ALA A 1064 ? 0.3007 0.3468 0.2931 0.0259  -0.0334 -0.0201 1062 ALA A N   
7870  C CA  . ALA A 1064 ? 0.3007 0.3480 0.2886 0.0270  -0.0335 -0.0205 1062 ALA A CA  
7871  C C   . ALA A 1064 ? 0.3182 0.3661 0.3043 0.0282  -0.0322 -0.0165 1062 ALA A C   
7872  O O   . ALA A 1064 ? 0.2641 0.3092 0.2489 0.0279  -0.0304 -0.0155 1062 ALA A O   
7873  C CB  . ALA A 1064 ? 0.3213 0.3649 0.3084 0.0258  -0.0328 -0.0231 1062 ALA A CB  
7874  N N   . ARG A 1065 ? 0.2768 0.3285 0.2634 0.0294  -0.0332 -0.0140 1063 ARG A N   
7875  C CA  . ARG A 1065 ? 0.2491 0.3011 0.2357 0.0302  -0.0323 -0.0095 1063 ARG A CA  
7876  C C   . ARG A 1065 ? 0.2925 0.3461 0.2746 0.0311  -0.0316 -0.0083 1063 ARG A C   
7877  O O   . ARG A 1065 ? 0.2897 0.3408 0.2718 0.0310  -0.0299 -0.0058 1063 ARG A O   
7878  C CB  . ARG A 1065 ? 0.2992 0.3552 0.2879 0.0312  -0.0340 -0.0069 1063 ARG A CB  
7879  N N   . ALA A 1066 ? 0.2678 0.3258 0.2462 0.0320  -0.0328 -0.0101 1064 ALA A N   
7880  C CA  . ALA A 1066 ? 0.2509 0.3113 0.2249 0.0329  -0.0321 -0.0092 1064 ALA A CA  
7881  C C   . ALA A 1066 ? 0.2496 0.3049 0.2227 0.0320  -0.0302 -0.0112 1064 ALA A C   
7882  O O   . ALA A 1066 ? 0.2598 0.3147 0.2312 0.0323  -0.0287 -0.0089 1064 ALA A O   
7883  C CB  . ALA A 1066 ? 0.2959 0.3629 0.2662 0.0343  -0.0339 -0.0115 1064 ALA A CB  
7884  N N   . GLU A 1067 ? 0.2551 0.3068 0.2299 0.0308  -0.0304 -0.0152 1065 GLU A N   
7885  C CA  . GLU A 1067 ? 0.2370 0.2838 0.2114 0.0298  -0.0289 -0.0168 1065 GLU A CA  
7886  C C   . GLU A 1067 ? 0.2567 0.2990 0.2334 0.0288  -0.0268 -0.0138 1065 GLU A C   
7887  O O   . GLU A 1067 ? 0.2442 0.2840 0.2195 0.0286  -0.0252 -0.0133 1065 GLU A O   
7888  C CB  . GLU A 1067 ? 0.2585 0.3028 0.2347 0.0286  -0.0299 -0.0212 1065 GLU A CB  
7889  C CG  . GLU A 1067 ? 0.2504 0.2986 0.2244 0.0297  -0.0319 -0.0251 1065 GLU A CG  
7890  C CD  . GLU A 1067 ? 0.3484 0.4015 0.3228 0.0305  -0.0341 -0.0256 1065 GLU A CD  
7891  O OE1 . GLU A 1067 ? 0.2774 0.3304 0.2544 0.0301  -0.0341 -0.0232 1065 GLU A OE1 
7892  O OE2 . GLU A 1067 ? 0.3799 0.4373 0.3523 0.0317  -0.0358 -0.0286 1065 GLU A OE2 
7893  N N   . ALA A 1068 ? 0.2442 0.2857 0.2245 0.0284  -0.0269 -0.0122 1066 ALA A N   
7894  C CA  . ALA A 1068 ? 0.2322 0.2700 0.2151 0.0277  -0.0252 -0.0097 1066 ALA A CA  
7895  C C   . ALA A 1068 ? 0.2550 0.2940 0.2364 0.0287  -0.0244 -0.0059 1066 ALA A C   
7896  O O   . ALA A 1068 ? 0.2378 0.2734 0.2195 0.0283  -0.0227 -0.0047 1066 ALA A O   
7897  C CB  . ALA A 1068 ? 0.2599 0.2976 0.2473 0.0273  -0.0258 -0.0090 1066 ALA A CB  
7898  N N   . GLU A 1069 ? 0.2544 0.2983 0.2343 0.0301  -0.0257 -0.0037 1067 GLU A N   
7899  C CA  . GLU A 1069 ? 0.2424 0.2883 0.2209 0.0310  -0.0251 0.0005  1067 GLU A CA  
7900  C C   . GLU A 1069 ? 0.2530 0.2989 0.2274 0.0311  -0.0238 -0.0006 1067 GLU A C   
7901  O O   . GLU A 1069 ? 0.2622 0.3063 0.2365 0.0310  -0.0224 0.0020  1067 GLU A O   
7902  C CB  . GLU A 1069 ? 0.2873 0.3395 0.2650 0.0323  -0.0268 0.0031  1067 GLU A CB  
7903  C CG  . GLU A 1069 ? 0.3366 0.3923 0.3124 0.0331  -0.0264 0.0077  1067 GLU A CG  
7904  C CD  . GLU A 1069 ? 0.4504 0.5033 0.4306 0.0328  -0.0259 0.0122  1067 GLU A CD  
7905  O OE1 . GLU A 1069 ? 0.5143 0.5627 0.4990 0.0321  -0.0258 0.0113  1067 GLU A OE1 
7906  O OE2 . GLU A 1069 ? 0.5739 0.6296 0.5535 0.0333  -0.0257 0.0166  1067 GLU A OE2 
7907  N N   . ALA A 1070 ? 0.2555 0.3033 0.2269 0.0314  -0.0245 -0.0044 1068 ALA A N   
7908  C CA  . ALA A 1070 ? 0.2414 0.2890 0.2092 0.0316  -0.0235 -0.0061 1068 ALA A CA  
7909  C C   . ALA A 1070 ? 0.2304 0.2714 0.1999 0.0302  -0.0217 -0.0069 1068 ALA A C   
7910  O O   . ALA A 1070 ? 0.2322 0.2722 0.1999 0.0303  -0.0203 -0.0060 1068 ALA A O   
7911  C CB  . ALA A 1070 ? 0.2834 0.3338 0.2489 0.0322  -0.0249 -0.0108 1068 ALA A CB  
7912  N N   . ALA A 1071 ? 0.2283 0.2653 0.2011 0.0289  -0.0218 -0.0085 1069 ALA A N   
7913  C CA  . ALA A 1071 ? 0.2095 0.2409 0.1839 0.0275  -0.0202 -0.0091 1069 ALA A CA  
7914  C C   . ALA A 1071 ? 0.2218 0.2515 0.1976 0.0275  -0.0187 -0.0053 1069 ALA A C   
7915  O O   . ALA A 1071 ? 0.2124 0.2394 0.1872 0.0271  -0.0172 -0.0049 1069 ALA A O   
7916  C CB  . ALA A 1071 ? 0.2210 0.2497 0.1987 0.0261  -0.0206 -0.0113 1069 ALA A CB  
7917  N N   . ARG A 1072 ? 0.2192 0.2503 0.1976 0.0279  -0.0193 -0.0025 1070 ARG A N   
7918  C CA  . ARG A 1072 ? 0.2215 0.2510 0.2019 0.0280  -0.0183 0.0012  1070 ARG A CA  
7919  C C   . ARG A 1072 ? 0.2259 0.2576 0.2032 0.0288  -0.0177 0.0037  1070 ARG A C   
7920  O O   . ARG A 1072 ? 0.2334 0.2624 0.2113 0.0285  -0.0163 0.0053  1070 ARG A O   
7921  C CB  . ARG A 1072 ? 0.2513 0.2823 0.2356 0.0286  -0.0195 0.0038  1070 ARG A CB  
7922  C CG  . ARG A 1072 ? 0.2746 0.3032 0.2629 0.0278  -0.0197 0.0016  1070 ARG A CG  
7923  C CD  . ARG A 1072 ? 0.3054 0.3353 0.2982 0.0285  -0.0209 0.0042  1070 ARG A CD  
7924  N NE  . ARG A 1072 ? 0.3212 0.3558 0.3130 0.0294  -0.0228 0.0052  1070 ARG A NE  
7925  C CZ  . ARG A 1072 ? 0.3361 0.3722 0.3285 0.0293  -0.0239 0.0028  1070 ARG A CZ  
7926  N NH1 . ARG A 1072 ? 0.3484 0.3820 0.3427 0.0282  -0.0234 -0.0005 1070 ARG A NH1 
7927  N NH2 . ARG A 1072 ? 0.3303 0.3710 0.3216 0.0302  -0.0257 0.0039  1070 ARG A NH2 
7928  N N   . ASN A 1073 ? 0.2303 0.2673 0.2043 0.0299  -0.0187 0.0040  1071 ASN A N   
7929  C CA  . ASN A 1073 ? 0.2298 0.2701 0.2006 0.0307  -0.0180 0.0063  1071 ASN A CA  
7930  C C   . ASN A 1073 ? 0.2303 0.2677 0.1987 0.0303  -0.0165 0.0037  1071 ASN A C   
7931  O O   . ASN A 1073 ? 0.2500 0.2869 0.2177 0.0303  -0.0152 0.0059  1071 ASN A O   
7932  C CB  . ASN A 1073 ? 0.2327 0.2802 0.2001 0.0321  -0.0194 0.0066  1071 ASN A CB  
7933  C CG  . ASN A 1073 ? 0.3199 0.3710 0.2896 0.0326  -0.0208 0.0106  1071 ASN A CG  
7934  O OD1 . ASN A 1073 ? 0.3634 0.4117 0.3373 0.0321  -0.0207 0.0139  1071 ASN A OD1 
7935  N ND2 . ASN A 1073 ? 0.3448 0.4021 0.3121 0.0336  -0.0223 0.0103  1071 ASN A ND2 
7936  N N   . ALA A 1074 ? 0.2234 0.2588 0.1911 0.0298  -0.0168 -0.0010 1072 ALA A N   
7937  C CA  . ALA A 1074 ? 0.2343 0.2664 0.2004 0.0292  -0.0156 -0.0035 1072 ALA A CA  
7938  C C   . ALA A 1074 ? 0.2223 0.2489 0.1910 0.0280  -0.0140 -0.0020 1072 ALA A C   
7939  O O   . ALA A 1074 ? 0.2097 0.2349 0.1772 0.0279  -0.0127 -0.0015 1072 ALA A O   
7940  C CB  . ALA A 1074 ? 0.2671 0.2977 0.2332 0.0287  -0.0166 -0.0083 1072 ALA A CB  
7941  N N   . GLY A 1075 ? 0.2133 0.2375 0.1858 0.0272  -0.0142 -0.0014 1073 GLY A N   
7942  C CA  . GLY A 1075 ? 0.2217 0.2414 0.1968 0.0262  -0.0128 -0.0004 1073 GLY A CA  
7943  C C   . GLY A 1075 ? 0.2126 0.2327 0.1879 0.0267  -0.0120 0.0035  1073 GLY A C   
7944  O O   . GLY A 1075 ? 0.2228 0.2398 0.1984 0.0261  -0.0106 0.0039  1073 GLY A O   
7945  N N   . SER A 1076 ? 0.2356 0.2597 0.2111 0.0277  -0.0129 0.0067  1074 SER A N   
7946  C CA  . SER A 1076 ? 0.2249 0.2500 0.2013 0.0281  -0.0123 0.0111  1074 SER A CA  
7947  C C   . SER A 1076 ? 0.2349 0.2624 0.2070 0.0286  -0.0114 0.0114  1074 SER A C   
7948  O O   . SER A 1076 ? 0.2645 0.2905 0.2370 0.0284  -0.0102 0.0135  1074 SER A O   
7949  C CB  . SER A 1076 ? 0.2741 0.3034 0.2522 0.0290  -0.0138 0.0149  1074 SER A CB  
7950  O OG  . SER A 1076 ? 0.3728 0.3996 0.3558 0.0286  -0.0146 0.0153  1074 SER A OG  
7951  N N   . SER A 1077 ? 0.2385 0.2700 0.2067 0.0294  -0.0120 0.0092  1075 SER A N   
7952  C CA  A SER A 1077 ? 0.2491 0.2840 0.2134 0.0302  -0.0113 0.0091  1075 SER A CA  
7953  C CA  B SER A 1077 ? 0.2492 0.2842 0.2134 0.0302  -0.0113 0.0090  1075 SER A CA  
7954  C C   . SER A 1077 ? 0.2296 0.2601 0.1929 0.0295  -0.0099 0.0061  1075 SER A C   
7955  O O   . SER A 1077 ? 0.2607 0.2929 0.2219 0.0299  -0.0089 0.0069  1075 SER A O   
7956  C CB  A SER A 1077 ? 0.2491 0.2899 0.2099 0.0314  -0.0125 0.0067  1075 SER A CB  
7957  C CB  B SER A 1077 ? 0.2487 0.2894 0.2095 0.0313  -0.0126 0.0065  1075 SER A CB  
7958  O OG  A SER A 1077 ? 0.3017 0.3479 0.2627 0.0321  -0.0136 0.0103  1075 SER A OG  
7959  O OG  B SER A 1077 ? 0.3025 0.3472 0.2595 0.0323  -0.0120 0.0055  1075 SER A OG  
7960  N N   . SER A 1078 ? 0.2141 0.2396 0.1790 0.0284  -0.0100 0.0030  1076 SER A N   
7961  C CA  . SER A 1078 ? 0.2224 0.2437 0.1869 0.0276  -0.0089 0.0005  1076 SER A CA  
7962  C C   . SER A 1078 ? 0.2220 0.2410 0.1876 0.0272  -0.0073 0.0034  1076 SER A C   
7963  O O   . SER A 1078 ? 0.2291 0.2469 0.1977 0.0268  -0.0072 0.0064  1076 SER A O   
7964  C CB  . SER A 1078 ? 0.2186 0.2354 0.1855 0.0263  -0.0092 -0.0021 1076 SER A CB  
7965  O OG  . SER A 1078 ? 0.2099 0.2227 0.1768 0.0253  -0.0082 -0.0038 1076 SER A OG  
7966  N N   . ALA A 1079 ? 0.2076 0.2260 0.1712 0.0273  -0.0064 0.0024  1077 ALA A N   
7967  C CA  . ALA A 1079 ? 0.2102 0.2260 0.1749 0.0267  -0.0049 0.0048  1077 ALA A CA  
7968  C C   . ALA A 1079 ? 0.2066 0.2167 0.1729 0.0254  -0.0042 0.0025  1077 ALA A C   
7969  O O   . ALA A 1079 ? 0.2126 0.2203 0.1794 0.0249  -0.0031 0.0037  1077 ALA A O   
7970  C CB  . ALA A 1079 ? 0.2185 0.2380 0.1803 0.0277  -0.0042 0.0058  1077 ALA A CB  
7971  N N   . LEU A 1080 ? 0.1992 0.2073 0.1662 0.0246  -0.0050 -0.0004 1078 LEU A N   
7972  C CA  . LEU A 1080 ? 0.2125 0.2160 0.1813 0.0231  -0.0044 -0.0019 1078 LEU A CA  
7973  C C   . LEU A 1080 ? 0.1951 0.1964 0.1666 0.0225  -0.0035 0.0005  1078 LEU A C   
7974  O O   . LEU A 1080 ? 0.2018 0.2041 0.1755 0.0228  -0.0040 0.0023  1078 LEU A O   
7975  C CB  . LEU A 1080 ? 0.2030 0.2059 0.1731 0.0224  -0.0055 -0.0043 1078 LEU A CB  
7976  C CG  . LEU A 1080 ? 0.2174 0.2166 0.1896 0.0207  -0.0050 -0.0054 1078 LEU A CG  
7977  C CD1 . LEU A 1080 ? 0.2393 0.2364 0.2102 0.0201  -0.0047 -0.0071 1078 LEU A CD1 
7978  C CD2 . LEU A 1080 ? 0.2174 0.2170 0.1914 0.0200  -0.0061 -0.0070 1078 LEU A CD2 
7979  N N   . GLY A 1081 ? 0.1913 0.1897 0.1631 0.0217  -0.0024 0.0004  1079 GLY A N   
7980  C CA  . GLY A 1081 ? 0.2098 0.2063 0.1846 0.0212  -0.0016 0.0022  1079 GLY A CA  
7981  C C   . GLY A 1081 ? 0.2250 0.2222 0.1997 0.0219  -0.0010 0.0052  1079 GLY A C   
7982  O O   . GLY A 1081 ? 0.2319 0.2272 0.2093 0.0214  -0.0005 0.0066  1079 GLY A O   
7983  N N   . LEU A 1082 ? 0.1977 0.1981 0.1697 0.0229  -0.0010 0.0063  1080 LEU A N   
7984  C CA  A LEU A 1082 ? 0.1979 0.1995 0.1697 0.0234  -0.0003 0.0092  1080 LEU A CA  
7985  C CA  B LEU A 1082 ? 0.1979 0.1994 0.1696 0.0234  -0.0003 0.0092  1080 LEU A CA  
7986  C C   . LEU A 1082 ? 0.2206 0.2185 0.1928 0.0225  0.0009  0.0085  1080 LEU A C   
7987  O O   . LEU A 1082 ? 0.2147 0.2107 0.1855 0.0219  0.0011  0.0056  1080 LEU A O   
7988  C CB  A LEU A 1082 ? 0.2094 0.2153 0.1774 0.0246  -0.0003 0.0093  1080 LEU A CB  
7989  C CB  B LEU A 1082 ? 0.2092 0.2152 0.1772 0.0246  -0.0003 0.0092  1080 LEU A CB  
7990  C CG  A LEU A 1082 ? 0.2124 0.2208 0.1797 0.0251  0.0006  0.0124  1080 LEU A CG  
7991  C CG  B LEU A 1082 ? 0.2122 0.2208 0.1792 0.0252  0.0006  0.0122  1080 LEU A CG  
7992  C CD1 A LEU A 1082 ? 0.2244 0.2340 0.1950 0.0251  0.0003  0.0169  1080 LEU A CD1 
7993  C CD1 B LEU A 1082 ? 0.2129 0.2281 0.1772 0.0266  0.0001  0.0132  1080 LEU A CD1 
7994  C CD2 A LEU A 1082 ? 0.2207 0.2345 0.1842 0.0264  0.0006  0.0117  1080 LEU A CD2 
7995  C CD2 B LEU A 1082 ? 0.2202 0.2266 0.1859 0.0249  0.0017  0.0104  1080 LEU A CD2 
7996  N N   . ASP A 1083 ? 0.2106 0.2076 0.1852 0.0223  0.0014  0.0112  1081 ASP A N   
7997  C CA  . ASP A 1083 ? 0.2249 0.2186 0.2004 0.0214  0.0024  0.0105  1081 ASP A CA  
7998  C C   . ASP A 1083 ? 0.2590 0.2536 0.2359 0.0217  0.0029  0.0141  1081 ASP A C   
7999  O O   . ASP A 1083 ? 0.2887 0.2829 0.2694 0.0216  0.0025  0.0164  1081 ASP A O   
8000  C CB  . ASP A 1083 ? 0.2755 0.2662 0.2542 0.0205  0.0022  0.0091  1081 ASP A CB  
8001  C CG  . ASP A 1083 ? 0.3918 0.3795 0.3712 0.0195  0.0031  0.0082  1081 ASP A CG  
8002  O OD1 . ASP A 1083 ? 0.3998 0.3872 0.3770 0.0195  0.0039  0.0082  1081 ASP A OD1 
8003  O OD2 . ASP A 1083 ? 0.4503 0.4363 0.4327 0.0188  0.0030  0.0072  1081 ASP A OD2 
8004  N N   . LEU A 1084 ? 0.2352 0.2312 0.2095 0.0221  0.0037  0.0145  1082 LEU A N   
8005  C CA  . LEU A 1084 ? 0.2446 0.2427 0.2198 0.0224  0.0043  0.0182  1082 LEU A CA  
8006  C C   . LEU A 1084 ? 0.2458 0.2414 0.2210 0.0218  0.0053  0.0176  1082 LEU A C   
8007  O O   . LEU A 1084 ? 0.2554 0.2491 0.2284 0.0216  0.0057  0.0145  1082 LEU A O   
8008  C CB  . LEU A 1084 ? 0.2527 0.2563 0.2246 0.0236  0.0043  0.0194  1082 LEU A CB  
8009  C CG  . LEU A 1084 ? 0.2899 0.2973 0.2612 0.0243  0.0033  0.0204  1082 LEU A CG  
8010  C CD1 . LEU A 1084 ? 0.3022 0.3156 0.2695 0.0256  0.0035  0.0207  1082 LEU A CD1 
8011  C CD2 . LEU A 1084 ? 0.3072 0.3151 0.2828 0.0241  0.0025  0.0248  1082 LEU A CD2 
8012  N N   . GLU A 1085 ? 0.2368 0.2325 0.2146 0.0216  0.0057  0.0209  1083 GLU A N   
8013  C CA  . GLU A 1085 ? 0.2422 0.2368 0.2197 0.0213  0.0067  0.0210  1083 GLU A CA  
8014  C C   . GLU A 1085 ? 0.2481 0.2478 0.2238 0.0222  0.0073  0.0238  1083 GLU A C   
8015  O O   . GLU A 1085 ? 0.2669 0.2698 0.2444 0.0224  0.0069  0.0277  1083 GLU A O   
8016  C CB  . GLU A 1085 ? 0.2676 0.2590 0.2498 0.0204  0.0067  0.0224  1083 GLU A CB  
8017  C CG  . GLU A 1085 ? 0.2852 0.2757 0.2668 0.0200  0.0077  0.0226  1083 GLU A CG  
8018  C CD  . GLU A 1085 ? 0.3982 0.3851 0.3841 0.0191  0.0076  0.0230  1083 GLU A CD  
8019  O OE1 . GLU A 1085 ? 0.4092 0.3939 0.3982 0.0187  0.0068  0.0220  1083 GLU A OE1 
8020  O OE2 . GLU A 1085 ? 0.3617 0.3485 0.3479 0.0189  0.0084  0.0241  1083 GLU A OE2 
8021  N N   . LEU A 1086 ? 0.2418 0.2425 0.2143 0.0226  0.0082  0.0220  1084 LEU A N   
8022  C CA  . LEU A 1086 ? 0.2264 0.2328 0.1968 0.0236  0.0088  0.0239  1084 LEU A CA  
8023  C C   . LEU A 1086 ? 0.2686 0.2748 0.2410 0.0231  0.0097  0.0265  1084 LEU A C   
8024  O O   . LEU A 1086 ? 0.2683 0.2700 0.2417 0.0223  0.0101  0.0248  1084 LEU A O   
8025  C CB  . LEU A 1086 ? 0.2429 0.2511 0.2092 0.0246  0.0091  0.0199  1084 LEU A CB  
8026  C CG  . LEU A 1086 ? 0.2636 0.2719 0.2281 0.0251  0.0080  0.0170  1084 LEU A CG  
8027  C CD1 . LEU A 1086 ? 0.2964 0.3063 0.2576 0.0261  0.0080  0.0129  1084 LEU A CD1 
8028  C CD2 . LEU A 1086 ? 0.3041 0.3171 0.2685 0.0257  0.0074  0.0198  1084 LEU A CD2 
8029  N N   . PRO A 1087 ? 0.2556 0.2670 0.2288 0.0234  0.0100  0.0308  1085 PRO A N   
8030  C CA  . PRO A 1087 ? 0.2915 0.3034 0.2668 0.0229  0.0109  0.0336  1085 PRO A CA  
8031  C C   . PRO A 1087 ? 0.2791 0.2906 0.2516 0.0234  0.0119  0.0304  1085 PRO A C   
8032  O O   . PRO A 1087 ? 0.3085 0.3231 0.2771 0.0246  0.0122  0.0276  1085 PRO A O   
8033  C CB  . PRO A 1087 ? 0.3327 0.3521 0.3081 0.0235  0.0110  0.0385  1085 PRO A CB  
8034  C CG  . PRO A 1087 ? 0.3226 0.3438 0.2977 0.0238  0.0099  0.0392  1085 PRO A CG  
8035  C CD  . PRO A 1087 ? 0.2416 0.2590 0.2139 0.0242  0.0095  0.0336  1085 PRO A CD  
8036  N N   . GLY A 1088 ? 0.2795 0.2874 0.2544 0.0225  0.0124  0.0308  1086 GLY A N   
8037  C CA  . GLY A 1088 ? 0.2953 0.3026 0.2684 0.0228  0.0133  0.0282  1086 GLY A CA  
8038  C C   . GLY A 1088 ? 0.2484 0.2531 0.2247 0.0218  0.0138  0.0301  1086 GLY A C   
8039  O O   . GLY A 1088 ? 0.2444 0.2492 0.2245 0.0210  0.0135  0.0340  1086 GLY A O   
8040  N N   . PRO A 1089 ? 0.2722 0.2744 0.2475 0.0217  0.0143  0.0274  1087 PRO A N   
8041  C CA  . PRO A 1089 ? 0.2526 0.2526 0.2308 0.0208  0.0147  0.0289  1087 PRO A CA  
8042  C C   . PRO A 1089 ? 0.2818 0.2761 0.2635 0.0195  0.0139  0.0288  1087 PRO A C   
8043  O O   . PRO A 1089 ? 0.2655 0.2570 0.2468 0.0192  0.0131  0.0265  1087 PRO A O   
8044  C CB  . PRO A 1089 ? 0.2905 0.2893 0.2663 0.0213  0.0153  0.0254  1087 PRO A CB  
8045  C CG  . PRO A 1089 ? 0.3139 0.3109 0.2871 0.0217  0.0146  0.0214  1087 PRO A CG  
8046  C CD  . PRO A 1089 ? 0.2800 0.2811 0.2520 0.0225  0.0142  0.0227  1087 PRO A CD  
8047  N N   . VAL A 1090 ? 0.2457 0.2388 0.2311 0.0186  0.0139  0.0311  1088 VAL A N   
8048  C CA  . VAL A 1090 ? 0.2345 0.2225 0.2234 0.0175  0.0131  0.0302  1088 VAL A CA  
8049  C C   . VAL A 1090 ? 0.2284 0.2127 0.2150 0.0172  0.0132  0.0259  1088 VAL A C   
8050  O O   . VAL A 1090 ? 0.2321 0.2173 0.2156 0.0177  0.0139  0.0241  1088 VAL A O   
8051  C CB  . VAL A 1090 ? 0.2446 0.2321 0.2383 0.0166  0.0130  0.0332  1088 VAL A CB  
8052  C CG1 . VAL A 1090 ? 0.2652 0.2564 0.2619 0.0167  0.0127  0.0381  1088 VAL A CG1 
8053  C CG2 . VAL A 1090 ? 0.2705 0.2586 0.2629 0.0167  0.0141  0.0328  1088 VAL A CG2 
8054  N N   . GLY A 1091 ? 0.2273 0.2080 0.2160 0.0163  0.0124  0.0242  1089 GLY A N   
8055  C CA  . GLY A 1091 ? 0.2417 0.2195 0.2287 0.0158  0.0125  0.0207  1089 GLY A CA  
8056  C C   . GLY A 1091 ? 0.2146 0.1924 0.1977 0.0162  0.0124  0.0181  1089 GLY A C   
8057  O O   . GLY A 1091 ? 0.2242 0.2002 0.2057 0.0158  0.0124  0.0157  1089 GLY A O   
8058  N N   . GLU A 1092 ? 0.2201 0.2000 0.2022 0.0169  0.0121  0.0187  1090 GLU A N   
8059  C CA  . GLU A 1092 ? 0.2348 0.2149 0.2138 0.0173  0.0119  0.0163  1090 GLU A CA  
8060  C C   . GLU A 1092 ? 0.2249 0.2060 0.2045 0.0176  0.0112  0.0171  1090 GLU A C   
8061  O O   . GLU A 1092 ? 0.2462 0.2294 0.2278 0.0179  0.0111  0.0200  1090 GLU A O   
8062  C CB  . GLU A 1092 ? 0.2908 0.2737 0.2667 0.0185  0.0124  0.0159  1090 GLU A CB  
8063  C CG  . GLU A 1092 ? 0.3257 0.3079 0.2989 0.0188  0.0119  0.0127  1090 GLU A CG  
8064  C CD  . GLU A 1092 ? 0.3591 0.3440 0.3303 0.0200  0.0123  0.0119  1090 GLU A CD  
8065  O OE1 . GLU A 1092 ? 0.2929 0.2819 0.2626 0.0212  0.0125  0.0126  1090 GLU A OE1 
8066  O OE2 . GLU A 1092 ? 0.3540 0.3374 0.3251 0.0199  0.0125  0.0106  1090 GLU A OE2 
8067  N N   . ARG A 1093 ? 0.2050 0.1849 0.1834 0.0174  0.0106  0.0147  1091 ARG A N   
8068  C CA  . ARG A 1093 ? 0.2203 0.2015 0.1989 0.0178  0.0100  0.0150  1091 ARG A CA  
8069  C C   . ARG A 1093 ? 0.2101 0.1928 0.1851 0.0185  0.0098  0.0130  1091 ARG A C   
8070  O O   . ARG A 1093 ? 0.2307 0.2116 0.2044 0.0181  0.0096  0.0104  1091 ARG A O   
8071  C CB  . ARG A 1093 ? 0.2628 0.2418 0.2439 0.0170  0.0093  0.0137  1091 ARG A CB  
8072  C CG  . ARG A 1093 ? 0.4063 0.3848 0.3918 0.0168  0.0089  0.0158  1091 ARG A CG  
8073  C CD  . ARG A 1093 ? 0.5057 0.4833 0.4935 0.0166  0.0080  0.0145  1091 ARG A CD  
8074  N NE  . ARG A 1093 ? 0.6574 0.6336 0.6439 0.0159  0.0080  0.0112  1091 ARG A NE  
8075  C CZ  . ARG A 1093 ? 0.6740 0.6488 0.6622 0.0150  0.0081  0.0097  1091 ARG A CZ  
8076  N NH1 . ARG A 1093 ? 0.6202 0.5941 0.6116 0.0149  0.0080  0.0108  1091 ARG A NH1 
8077  N NH2 . ARG A 1093 ? 0.6212 0.5956 0.6079 0.0143  0.0082  0.0071  1091 ARG A NH2 
8078  N N   . ASN A 1094 ? 0.2131 0.1993 0.1869 0.0196  0.0097  0.0143  1092 ASN A N   
8079  C CA  . ASN A 1094 ? 0.2060 0.1943 0.1766 0.0205  0.0094  0.0123  1092 ASN A CA  
8080  C C   . ASN A 1094 ? 0.2248 0.2144 0.1953 0.0208  0.0086  0.0124  1092 ASN A C   
8081  O O   . ASN A 1094 ? 0.2389 0.2312 0.2104 0.0212  0.0085  0.0152  1092 ASN A O   
8082  C CB  . ASN A 1094 ? 0.2095 0.2020 0.1783 0.0217  0.0101  0.0134  1092 ASN A CB  
8083  C CG  . ASN A 1094 ? 0.1978 0.1888 0.1664 0.0216  0.0107  0.0124  1092 ASN A CG  
8084  O OD1 . ASN A 1094 ? 0.2286 0.2175 0.1961 0.0214  0.0104  0.0094  1092 ASN A OD1 
8085  N ND2 . ASN A 1094 ? 0.2460 0.2379 0.2160 0.0215  0.0116  0.0150  1092 ASN A ND2 
8086  N N   . LEU A 1095 ? 0.2158 0.2036 0.1856 0.0204  0.0079  0.0096  1093 LEU A N   
8087  C CA  . LEU A 1095 ? 0.2080 0.1964 0.1783 0.0204  0.0071  0.0094  1093 LEU A CA  
8088  C C   . LEU A 1095 ? 0.2309 0.2215 0.1984 0.0213  0.0064  0.0072  1093 LEU A C   
8089  O O   . LEU A 1095 ? 0.2314 0.2216 0.1974 0.0215  0.0063  0.0049  1093 LEU A O   
8090  C CB  . LEU A 1095 ? 0.2412 0.2261 0.2133 0.0191  0.0067  0.0078  1093 LEU A CB  
8091  C CG  . LEU A 1095 ? 0.2625 0.2452 0.2375 0.0183  0.0072  0.0091  1093 LEU A CG  
8092  C CD1 . LEU A 1095 ? 0.3215 0.3019 0.2980 0.0171  0.0069  0.0071  1093 LEU A CD1 
8093  C CD2 . LEU A 1095 ? 0.3136 0.2977 0.2912 0.0188  0.0071  0.0122  1093 LEU A CD2 
8094  N N   . TYR A 1096 ? 0.2203 0.2133 0.1877 0.0219  0.0057  0.0079  1094 TYR A N   
8095  C CA  . TYR A 1096 ? 0.2031 0.1989 0.1681 0.0229  0.0049  0.0059  1094 TYR A CA  
8096  C C   . TYR A 1096 ? 0.2111 0.2066 0.1772 0.0225  0.0040  0.0056  1094 TYR A C   
8097  O O   . TYR A 1096 ? 0.2207 0.2170 0.1885 0.0225  0.0039  0.0082  1094 TYR A O   
8098  C CB  . TYR A 1096 ? 0.2115 0.2128 0.1746 0.0244  0.0052  0.0078  1094 TYR A CB  
8099  C CG  . TYR A 1096 ? 0.2158 0.2212 0.1765 0.0256  0.0043  0.0058  1094 TYR A CG  
8100  C CD1 . TYR A 1096 ? 0.2280 0.2347 0.1867 0.0265  0.0040  0.0023  1094 TYR A CD1 
8101  C CD2 . TYR A 1096 ? 0.2435 0.2517 0.2043 0.0260  0.0036  0.0073  1094 TYR A CD2 
8102  C CE1 . TYR A 1096 ? 0.2133 0.2240 0.1700 0.0278  0.0030  0.0001  1094 TYR A CE1 
8103  C CE2 . TYR A 1096 ? 0.2395 0.2520 0.1980 0.0272  0.0027  0.0054  1094 TYR A CE2 
8104  C CZ  . TYR A 1096 ? 0.2165 0.2303 0.1729 0.0281  0.0024  0.0017  1094 TYR A CZ  
8105  O OH  . TYR A 1096 ? 0.2300 0.2482 0.1843 0.0294  0.0013  -0.0006 1094 TYR A OH  
8106  N N   . THR A 1097 ? 0.2073 0.2014 0.1727 0.0222  0.0032  0.0026  1095 THR A N   
8107  C CA  . THR A 1097 ? 0.2188 0.2124 0.1856 0.0217  0.0023  0.0020  1095 THR A CA  
8108  C C   . THR A 1097 ? 0.2361 0.2314 0.2012 0.0223  0.0011  -0.0007 1095 THR A C   
8109  O O   . THR A 1097 ? 0.2374 0.2328 0.2011 0.0226  0.0008  -0.0030 1095 THR A O   
8110  C CB  . THR A 1097 ? 0.2805 0.2701 0.2494 0.0200  0.0025  0.0011  1095 THR A CB  
8111  O OG1 . THR A 1097 ? 0.3115 0.2992 0.2797 0.0194  0.0024  -0.0011 1095 THR A OG1 
8112  C CG2 . THR A 1097 ? 0.2800 0.2681 0.2509 0.0195  0.0034  0.0032  1095 THR A CG2 
8113  N N   . LEU A 1098 ? 0.2171 0.2138 0.1827 0.0224  0.0003  -0.0006 1096 LEU A N   
8114  C CA  . LEU A 1098 ? 0.2243 0.2226 0.1889 0.0229  -0.0011 -0.0033 1096 LEU A CA  
8115  C C   . LEU A 1098 ? 0.1909 0.1865 0.1575 0.0215  -0.0017 -0.0047 1096 LEU A C   
8116  O O   . LEU A 1098 ? 0.2056 0.2008 0.1742 0.0209  -0.0016 -0.0033 1096 LEU A O   
8117  C CB  . LEU A 1098 ? 0.2081 0.2111 0.1715 0.0242  -0.0017 -0.0021 1096 LEU A CB  
8118  C CG  . LEU A 1098 ? 0.1992 0.2063 0.1603 0.0256  -0.0011 -0.0006 1096 LEU A CG  
8119  C CD1 . LEU A 1098 ? 0.2192 0.2315 0.1792 0.0268  -0.0019 0.0008  1096 LEU A CD1 
8120  C CD2 . LEU A 1098 ? 0.2190 0.2269 0.1782 0.0264  -0.0012 -0.0037 1096 LEU A CD2 
8121  N N   . HIS A 1099 ? 0.2011 0.1953 0.1679 0.0209  -0.0025 -0.0074 1097 HIS A N   
8122  C CA  . HIS A 1099 ? 0.2092 0.2012 0.1780 0.0193  -0.0032 -0.0086 1097 HIS A CA  
8123  C C   . HIS A 1099 ? 0.2126 0.2061 0.1812 0.0198  -0.0049 -0.0111 1097 HIS A C   
8124  O O   . HIS A 1099 ? 0.2228 0.2189 0.1897 0.0213  -0.0056 -0.0123 1097 HIS A O   
8125  C CB  . HIS A 1099 ? 0.2430 0.2317 0.2128 0.0179  -0.0029 -0.0092 1097 HIS A CB  
8126  C CG  . HIS A 1099 ? 0.2544 0.2416 0.2245 0.0175  -0.0014 -0.0072 1097 HIS A CG  
8127  N ND1 . HIS A 1099 ? 0.3392 0.3249 0.3111 0.0160  -0.0007 -0.0064 1097 HIS A ND1 
8128  C CD2 . HIS A 1099 ? 0.2811 0.2685 0.2499 0.0183  -0.0003 -0.0059 1097 HIS A CD2 
8129  C CE1 . HIS A 1099 ? 0.3109 0.2956 0.2828 0.0160  0.0005  -0.0049 1097 HIS A CE1 
8130  N NE2 . HIS A 1099 ? 0.2969 0.2825 0.2670 0.0173  0.0007  -0.0044 1097 HIS A NE2 
8131  N N   . ALA A 1100 ? 0.2167 0.2091 0.1874 0.0184  -0.0057 -0.0119 1098 ALA A N   
8132  C CA  . ALA A 1100 ? 0.2317 0.2249 0.2031 0.0184  -0.0076 -0.0144 1098 ALA A CA  
8133  C C   . ALA A 1100 ? 0.2487 0.2402 0.2203 0.0184  -0.0084 -0.0165 1098 ALA A C   
8134  O O   . ALA A 1100 ? 0.2504 0.2394 0.2225 0.0176  -0.0076 -0.0159 1098 ALA A O   
8135  C CB  . ALA A 1100 ? 0.2437 0.2359 0.2177 0.0166  -0.0081 -0.0145 1098 ALA A CB  
8136  N N   . ARG A 1101 ? 0.2459 0.2390 0.2175 0.0194  -0.0102 -0.0193 1099 ARG A N   
8137  C CA  A ARG A 1101 ? 0.2488 0.2403 0.2216 0.0196  -0.0115 -0.0219 1099 ARG A CA  
8138  C CA  B ARG A 1101 ? 0.2491 0.2406 0.2219 0.0196  -0.0115 -0.0219 1099 ARG A CA  
8139  C C   . ARG A 1101 ? 0.2377 0.2259 0.2143 0.0173  -0.0127 -0.0222 1099 ARG A C   
8140  O O   . ARG A 1101 ? 0.2520 0.2375 0.2304 0.0165  -0.0131 -0.0225 1099 ARG A O   
8141  C CB  A ARG A 1101 ? 0.2775 0.2722 0.2494 0.0216  -0.0132 -0.0253 1099 ARG A CB  
8142  C CB  B ARG A 1101 ? 0.2773 0.2720 0.2492 0.0215  -0.0132 -0.0253 1099 ARG A CB  
8143  C CG  A ARG A 1101 ? 0.2694 0.2684 0.2375 0.0238  -0.0122 -0.0250 1099 ARG A CG  
8144  C CG  B ARG A 1101 ? 0.2755 0.2741 0.2437 0.0238  -0.0122 -0.0253 1099 ARG A CG  
8145  C CD  A ARG A 1101 ? 0.2476 0.2506 0.2149 0.0259  -0.0139 -0.0288 1099 ARG A CD  
8146  C CD  B ARG A 1101 ? 0.2926 0.2921 0.2610 0.0253  -0.0134 -0.0290 1099 ARG A CD  
8147  N NE  A ARG A 1101 ? 0.2377 0.2398 0.2062 0.0267  -0.0151 -0.0323 1099 ARG A NE  
8148  N NE  B ARG A 1101 ? 0.2633 0.2670 0.2283 0.0274  -0.0122 -0.0288 1099 ARG A NE  
8149  C CZ  A ARG A 1101 ? 0.2827 0.2866 0.2492 0.0282  -0.0141 -0.0328 1099 ARG A CZ  
8150  C CZ  B ARG A 1101 ? 0.2876 0.2941 0.2520 0.0293  -0.0131 -0.0323 1099 ARG A CZ  
8151  N NH1 A ARG A 1101 ? 0.2959 0.3027 0.2592 0.0289  -0.0120 -0.0297 1099 ARG A NH1 
8152  N NH1 B ARG A 1101 ? 0.2648 0.2699 0.2322 0.0295  -0.0154 -0.0365 1099 ARG A NH1 
8153  N NH2 A ARG A 1101 ? 0.2731 0.2762 0.2416 0.0290  -0.0155 -0.0363 1099 ARG A NH2 
8154  N NH2 B ARG A 1101 ? 0.2695 0.2806 0.2306 0.0311  -0.0117 -0.0315 1099 ARG A NH2 
8155  N N   . GLY A 1102 ? 0.2390 0.2277 0.2173 0.0162  -0.0134 -0.0219 1100 GLY A N   
8156  C CA  . GLY A 1102 ? 0.2713 0.2577 0.2535 0.0139  -0.0146 -0.0218 1100 GLY A CA  
8157  C C   . GLY A 1102 ? 0.2317 0.2195 0.2157 0.0136  -0.0165 -0.0233 1100 GLY A C   
8158  O O   . GLY A 1102 ? 0.2500 0.2403 0.2328 0.0140  -0.0159 -0.0226 1100 GLY A O   
8159  N N   . ARG A 1103 ? 0.2317 0.2182 0.2192 0.0130  -0.0189 -0.0255 1101 ARG A N   
8160  C CA  . ARG A 1103 ? 0.2320 0.2198 0.2218 0.0127  -0.0210 -0.0272 1101 ARG A CA  
8161  C C   . ARG A 1103 ? 0.2140 0.2036 0.2029 0.0152  -0.0227 -0.0311 1101 ARG A C   
8162  O O   . ARG A 1103 ? 0.2362 0.2245 0.2264 0.0160  -0.0240 -0.0335 1101 ARG A O   
8163  C CB  . ARG A 1103 ? 0.2536 0.2392 0.2489 0.0101  -0.0228 -0.0267 1101 ARG A CB  
8164  C CG  . ARG A 1103 ? 0.2764 0.2637 0.2743 0.0095  -0.0247 -0.0279 1101 ARG A CG  
8165  C CD  . ARG A 1103 ? 0.3083 0.2940 0.3116 0.0065  -0.0262 -0.0262 1101 ARG A CD  
8166  N NE  . ARG A 1103 ? 0.3601 0.3462 0.3631 0.0045  -0.0239 -0.0223 1101 ARG A NE  
8167  C CZ  . ARG A 1103 ? 0.4357 0.4244 0.4386 0.0033  -0.0229 -0.0204 1101 ARG A CZ  
8168  N NH1 . ARG A 1103 ? 0.3356 0.3265 0.3387 0.0039  -0.0237 -0.0218 1101 ARG A NH1 
8169  N NH2 . ARG A 1103 ? 0.4274 0.4167 0.4301 0.0017  -0.0209 -0.0173 1101 ARG A NH2 
8170  N N   . ILE A 1104 ? 0.2148 0.2079 0.2015 0.0165  -0.0228 -0.0319 1102 ILE A N   
8171  C CA  . ILE A 1104 ? 0.2072 0.2034 0.1924 0.0190  -0.0243 -0.0356 1102 ILE A CA  
8172  C C   . ILE A 1104 ? 0.2172 0.2135 0.2065 0.0184  -0.0273 -0.0384 1102 ILE A C   
8173  O O   . ILE A 1104 ? 0.2243 0.2209 0.2151 0.0169  -0.0275 -0.0369 1102 ILE A O   
8174  C CB  . ILE A 1104 ? 0.2348 0.2352 0.2152 0.0207  -0.0227 -0.0345 1102 ILE A CB  
8175  C CG1 . ILE A 1104 ? 0.2280 0.2281 0.2054 0.0210  -0.0198 -0.0312 1102 ILE A CG1 
8176  C CG2 . ILE A 1104 ? 0.2202 0.2249 0.1987 0.0234  -0.0242 -0.0383 1102 ILE A CG2 
8177  C CD1 . ILE A 1104 ? 0.2487 0.2482 0.2249 0.0221  -0.0194 -0.0324 1102 ILE A CD1 
8178  N N   . LEU A 1105 ? 0.2178 0.2140 0.2091 0.0196  -0.0297 -0.0426 1103 LEU A N   
8179  C CA  . LEU A 1105 ? 0.2230 0.2199 0.2182 0.0195  -0.0329 -0.0459 1103 LEU A CA  
8180  C C   . LEU A 1105 ? 0.2143 0.2164 0.2059 0.0215  -0.0331 -0.0476 1103 LEU A C   
8181  O O   . LEU A 1105 ? 0.2321 0.2379 0.2198 0.0240  -0.0325 -0.0494 1103 LEU A O   
8182  C CB  . LEU A 1105 ? 0.2540 0.2493 0.2528 0.0204  -0.0356 -0.0503 1103 LEU A CB  
8183  C CG  . LEU A 1105 ? 0.2599 0.2557 0.2635 0.0206  -0.0393 -0.0546 1103 LEU A CG  
8184  C CD1 . LEU A 1105 ? 0.2867 0.2795 0.2956 0.0174  -0.0405 -0.0521 1103 LEU A CD1 
8185  C CD2 . LEU A 1105 ? 0.2786 0.2731 0.2859 0.0220  -0.0419 -0.0594 1103 LEU A CD2 
8186  N N   . LEU A 1106 ? 0.2033 0.2064 0.1965 0.0204  -0.0339 -0.0469 1104 LEU A N   
8187  C CA  . LEU A 1106 ? 0.2207 0.2288 0.2113 0.0222  -0.0345 -0.0485 1104 LEU A CA  
8188  C C   . LEU A 1106 ? 0.2601 0.2689 0.2549 0.0225  -0.0382 -0.0532 1104 LEU A C   
8189  O O   . LEU A 1106 ? 0.2384 0.2442 0.2386 0.0203  -0.0399 -0.0530 1104 LEU A O   
8190  C CB  . LEU A 1106 ? 0.2293 0.2384 0.2189 0.0209  -0.0330 -0.0447 1104 LEU A CB  
8191  C CG  . LEU A 1106 ? 0.2997 0.3080 0.2861 0.0205  -0.0297 -0.0400 1104 LEU A CG  
8192  C CD1 . LEU A 1106 ? 0.2581 0.2690 0.2433 0.0203  -0.0287 -0.0375 1104 LEU A CD1 
8193  C CD2 . LEU A 1106 ? 0.2752 0.2851 0.2572 0.0225  -0.0280 -0.0398 1104 LEU A CD2 
8194  N N   . VAL A 1107 ? 0.2336 0.2469 0.2263 0.0252  -0.0395 -0.0573 1105 VAL A N   
8195  C CA  . VAL A 1107 ? 0.2430 0.2577 0.2396 0.0259  -0.0432 -0.0625 1105 VAL A CA  
8196  C C   . VAL A 1107 ? 0.2412 0.2622 0.2340 0.0276  -0.0434 -0.0633 1105 VAL A C   
8197  O O   . VAL A 1107 ? 0.2409 0.2672 0.2300 0.0303  -0.0437 -0.0663 1105 VAL A O   
8198  C CB  . VAL A 1107 ? 0.2321 0.2468 0.2303 0.0278  -0.0452 -0.0677 1105 VAL A CB  
8199  C CG1 . VAL A 1107 ? 0.2689 0.2841 0.2725 0.0282  -0.0494 -0.0733 1105 VAL A CG1 
8200  C CG2 . VAL A 1107 ? 0.2607 0.2694 0.2618 0.0262  -0.0444 -0.0659 1105 VAL A CG2 
8201  N N   . PRO A 1108 ? 0.2177 0.2387 0.2111 0.0261  -0.0432 -0.0605 1106 PRO A N   
8202  C CA  . PRO A 1108 ? 0.2326 0.2596 0.2225 0.0276  -0.0434 -0.0608 1106 PRO A CA  
8203  C C   . PRO A 1108 ? 0.2595 0.2889 0.2528 0.0284  -0.0471 -0.0660 1106 PRO A C   
8204  O O   . PRO A 1108 ? 0.2824 0.3082 0.2816 0.0272  -0.0496 -0.0688 1106 PRO A O   
8205  C CB  . PRO A 1108 ? 0.2606 0.2858 0.2510 0.0254  -0.0416 -0.0556 1106 PRO A CB  
8206  C CG  . PRO A 1108 ? 0.2605 0.2798 0.2568 0.0226  -0.0425 -0.0550 1106 PRO A CG  
8207  C CD  . PRO A 1108 ? 0.2655 0.2817 0.2625 0.0229  -0.0424 -0.0565 1106 PRO A CD  
8208  N N   . ALA A 1109 ? 0.2339 0.2697 0.2236 0.0303  -0.0476 -0.0672 1107 ALA A N   
8209  C CA  . ALA A 1109 ? 0.2514 0.2905 0.2437 0.0311  -0.0510 -0.0717 1107 ALA A CA  
8210  C C   . ALA A 1109 ? 0.2908 0.3322 0.2827 0.0303  -0.0510 -0.0690 1107 ALA A C   
8211  O O   . ALA A 1109 ? 0.3236 0.3650 0.3196 0.0296  -0.0537 -0.0715 1107 ALA A O   
8212  C CB  . ALA A 1109 ? 0.2679 0.3141 0.2566 0.0345  -0.0523 -0.0767 1107 ALA A CB  
8213  N N   . THR A 1110 ? 0.2525 0.2957 0.2398 0.0304  -0.0481 -0.0641 1108 THR A N   
8214  C CA  . THR A 1110 ? 0.2505 0.2963 0.2372 0.0300  -0.0480 -0.0614 1108 THR A CA  
8215  C C   . THR A 1110 ? 0.2496 0.2915 0.2363 0.0280  -0.0450 -0.0554 1108 THR A C   
8216  O O   . THR A 1110 ? 0.2424 0.2813 0.2276 0.0276  -0.0426 -0.0530 1108 THR A O   
8217  C CB  . THR A 1110 ? 0.2731 0.3267 0.2543 0.0326  -0.0479 -0.0613 1108 THR A CB  
8218  O OG1 . THR A 1110 ? 0.2614 0.3160 0.2379 0.0334  -0.0449 -0.0576 1108 THR A OG1 
8219  C CG2 . THR A 1110 ? 0.2625 0.3212 0.2432 0.0349  -0.0507 -0.0676 1108 THR A CG2 
8220  N N   . GLU A 1111 ? 0.2570 0.2993 0.2454 0.0269  -0.0452 -0.0532 1109 GLU A N   
8221  C CA  . GLU A 1111 ? 0.2598 0.2994 0.2485 0.0253  -0.0425 -0.0481 1109 GLU A CA  
8222  C C   . GLU A 1111 ? 0.2539 0.2952 0.2375 0.0267  -0.0399 -0.0446 1109 GLU A C   
8223  O O   . GLU A 1111 ? 0.2436 0.2812 0.2268 0.0258  -0.0375 -0.0416 1109 GLU A O   
8224  C CB  . GLU A 1111 ? 0.2841 0.3252 0.2752 0.0245  -0.0434 -0.0469 1109 GLU A CB  
8225  C CG  . GLU A 1111 ? 0.2889 0.3284 0.2801 0.0234  -0.0407 -0.0420 1109 GLU A CG  
8226  C CD  . GLU A 1111 ? 0.3351 0.3760 0.3296 0.0224  -0.0416 -0.0411 1109 GLU A CD  
8227  O OE1 . GLU A 1111 ? 0.3421 0.3808 0.3411 0.0204  -0.0428 -0.0424 1109 GLU A OE1 
8228  O OE2 . GLU A 1111 ? 0.3745 0.4187 0.3673 0.0235  -0.0413 -0.0390 1109 GLU A OE2 
8229  N N   . SER A 1112 ? 0.2533 0.3005 0.2331 0.0289  -0.0404 -0.0447 1110 SER A N   
8230  C CA  . SER A 1112 ? 0.2440 0.2934 0.2195 0.0301  -0.0381 -0.0409 1110 SER A CA  
8231  C C   . SER A 1112 ? 0.2606 0.3080 0.2341 0.0305  -0.0367 -0.0415 1110 SER A C   
8232  O O   . SER A 1112 ? 0.2505 0.2958 0.2226 0.0302  -0.0342 -0.0379 1110 SER A O   
8233  C CB  . SER A 1112 ? 0.2882 0.3452 0.2602 0.0323  -0.0391 -0.0408 1110 SER A CB  
8234  O OG  . SER A 1112 ? 0.2889 0.3478 0.2575 0.0332  -0.0370 -0.0363 1110 SER A OG  
8235  N N   . GLY A 1113 ? 0.2397 0.2876 0.2134 0.0313  -0.0384 -0.0463 1111 GLY A N   
8236  C CA  . GLY A 1113 ? 0.2137 0.2595 0.1862 0.0316  -0.0372 -0.0473 1111 GLY A CA  
8237  C C   . GLY A 1113 ? 0.2183 0.2568 0.1936 0.0293  -0.0356 -0.0451 1111 GLY A C   
8238  O O   . GLY A 1113 ? 0.2232 0.2599 0.1966 0.0293  -0.0333 -0.0427 1111 GLY A O   
8239  N N   . LEU A 1114 ? 0.2386 0.2733 0.2186 0.0273  -0.0367 -0.0456 1112 LEU A N   
8240  C CA  . LEU A 1114 ? 0.2318 0.2605 0.2145 0.0249  -0.0351 -0.0432 1112 LEU A CA  
8241  C C   . LEU A 1114 ? 0.2184 0.2465 0.1991 0.0245  -0.0323 -0.0382 1112 LEU A C   
8242  O O   . LEU A 1114 ? 0.2139 0.2387 0.1942 0.0238  -0.0302 -0.0362 1112 LEU A O   
8243  C CB  . LEU A 1114 ? 0.2523 0.2785 0.2404 0.0227  -0.0368 -0.0441 1112 LEU A CB  
8244  C CG  . LEU A 1114 ? 0.2567 0.2779 0.2476 0.0201  -0.0351 -0.0411 1112 LEU A CG  
8245  C CD1 . LEU A 1114 ? 0.2753 0.2929 0.2660 0.0199  -0.0343 -0.0414 1112 LEU A CD1 
8246  C CD2 . LEU A 1114 ? 0.2706 0.2904 0.2670 0.0179  -0.0370 -0.0418 1112 LEU A CD2 
8247  N N   . TYR A 1115 ? 0.2263 0.2577 0.2062 0.0251  -0.0322 -0.0363 1113 TYR A N   
8248  C CA  . TYR A 1115 ? 0.2320 0.2629 0.2110 0.0248  -0.0299 -0.0318 1113 TYR A CA  
8249  C C   . TYR A 1115 ? 0.2190 0.2510 0.1941 0.0262  -0.0281 -0.0299 1113 TYR A C   
8250  O O   . TYR A 1115 ? 0.2249 0.2540 0.1999 0.0255  -0.0260 -0.0270 1113 TYR A O   
8251  C CB  . TYR A 1115 ? 0.2252 0.2597 0.2047 0.0253  -0.0306 -0.0303 1113 TYR A CB  
8252  C CG  . TYR A 1115 ? 0.2282 0.2617 0.2119 0.0238  -0.0319 -0.0314 1113 TYR A CG  
8253  C CD1 . TYR A 1115 ? 0.2218 0.2513 0.2090 0.0216  -0.0319 -0.0324 1113 TYR A CD1 
8254  C CD2 . TYR A 1115 ? 0.2576 0.2948 0.2420 0.0244  -0.0332 -0.0311 1113 TYR A CD2 
8255  C CE1 . TYR A 1115 ? 0.2662 0.2955 0.2574 0.0201  -0.0331 -0.0330 1113 TYR A CE1 
8256  C CE2 . TYR A 1115 ? 0.2543 0.2910 0.2428 0.0229  -0.0344 -0.0320 1113 TYR A CE2 
8257  C CZ  . TYR A 1115 ? 0.2952 0.3281 0.2871 0.0207  -0.0342 -0.0329 1113 TYR A CZ  
8258  O OH  . TYR A 1115 ? 0.2902 0.3232 0.2862 0.0192  -0.0354 -0.0336 1113 TYR A OH  
8259  N N   . HIS A 1116 ? 0.2270 0.2633 0.1989 0.0282  -0.0291 -0.0317 1114 HIS A N   
8260  C CA  . HIS A 1116 ? 0.2261 0.2642 0.1943 0.0295  -0.0274 -0.0299 1114 HIS A CA  
8261  C C   . HIS A 1116 ? 0.2197 0.2533 0.1882 0.0288  -0.0263 -0.0309 1114 HIS A C   
8262  O O   . HIS A 1116 ? 0.2197 0.2520 0.1868 0.0288  -0.0242 -0.0281 1114 HIS A O   
8263  C CB  . HIS A 1116 ? 0.2464 0.2914 0.2112 0.0318  -0.0288 -0.0319 1114 HIS A CB  
8264  C CG  . HIS A 1116 ? 0.2383 0.2887 0.2015 0.0328  -0.0291 -0.0290 1114 HIS A CG  
8265  N ND1 . HIS A 1116 ? 0.2837 0.3365 0.2483 0.0329  -0.0311 -0.0301 1114 HIS A ND1 
8266  C CD2 . HIS A 1116 ? 0.2666 0.3205 0.2273 0.0337  -0.0279 -0.0246 1114 HIS A CD2 
8267  C CE1 . HIS A 1116 ? 0.2760 0.3337 0.2389 0.0338  -0.0310 -0.0267 1114 HIS A CE1 
8268  N NE2 . HIS A 1116 ? 0.3149 0.3734 0.2757 0.0343  -0.0292 -0.0232 1114 HIS A NE2 
8269  N N   . GLN A 1117 ? 0.2150 0.2464 0.1857 0.0282  -0.0279 -0.0349 1115 GLN A N   
8270  C CA  . GLN A 1117 ? 0.2211 0.2481 0.1926 0.0275  -0.0271 -0.0358 1115 GLN A CA  
8271  C C   . GLN A 1117 ? 0.1974 0.2194 0.1710 0.0253  -0.0252 -0.0324 1115 GLN A C   
8272  O O   . GLN A 1117 ? 0.2036 0.2232 0.1762 0.0251  -0.0233 -0.0307 1115 GLN A O   
8273  C CB  . GLN A 1117 ? 0.2142 0.2393 0.1889 0.0270  -0.0295 -0.0404 1115 GLN A CB  
8274  C CG  . GLN A 1117 ? 0.2301 0.2601 0.2033 0.0293  -0.0315 -0.0449 1115 GLN A CG  
8275  C CD  . GLN A 1117 ? 0.2797 0.3073 0.2572 0.0288  -0.0342 -0.0496 1115 GLN A CD  
8276  O OE1 . GLN A 1117 ? 0.2493 0.2721 0.2311 0.0265  -0.0348 -0.0491 1115 GLN A OE1 
8277  N NE2 . GLN A 1117 ? 0.2313 0.2626 0.2079 0.0309  -0.0360 -0.0543 1115 GLN A NE2 
8278  N N   . LEU A 1118 ? 0.2037 0.2243 0.1802 0.0238  -0.0256 -0.0315 1116 LEU A N   
8279  C CA  A LEU A 1118 ? 0.2160 0.2328 0.1945 0.0218  -0.0239 -0.0287 1116 LEU A CA  
8280  C CA  B LEU A 1118 ? 0.2162 0.2330 0.1947 0.0218  -0.0239 -0.0286 1116 LEU A CA  
8281  C C   . LEU A 1118 ? 0.2103 0.2278 0.1866 0.0225  -0.0216 -0.0250 1116 LEU A C   
8282  O O   . LEU A 1118 ? 0.2128 0.2272 0.1893 0.0216  -0.0198 -0.0231 1116 LEU A O   
8283  C CB  A LEU A 1118 ? 0.2289 0.2454 0.2112 0.0202  -0.0249 -0.0287 1116 LEU A CB  
8284  C CB  B LEU A 1118 ? 0.2301 0.2470 0.2121 0.0204  -0.0248 -0.0285 1116 LEU A CB  
8285  C CG  A LEU A 1118 ? 0.2275 0.2409 0.2125 0.0180  -0.0235 -0.0266 1116 LEU A CG  
8286  C CG  B LEU A 1118 ? 0.2351 0.2499 0.2209 0.0187  -0.0266 -0.0310 1116 LEU A CG  
8287  C CD1 A LEU A 1118 ? 0.2358 0.2454 0.2216 0.0168  -0.0229 -0.0268 1116 LEU A CD1 
8288  C CD1 B LEU A 1118 ? 0.2169 0.2331 0.2057 0.0177  -0.0276 -0.0307 1116 LEU A CD1 
8289  C CD2 A LEU A 1118 ? 0.2520 0.2661 0.2409 0.0165  -0.0250 -0.0275 1116 LEU A CD2 
8290  C CD2 B LEU A 1118 ? 0.2436 0.2542 0.2312 0.0168  -0.0254 -0.0298 1116 LEU A CD2 
8291  N N   . ALA A 1119 ? 0.2174 0.2389 0.1918 0.0240  -0.0219 -0.0238 1117 ALA A N   
8292  C CA  . ALA A 1119 ? 0.2340 0.2562 0.2071 0.0246  -0.0201 -0.0200 1117 ALA A CA  
8293  C C   . ALA A 1119 ? 0.2312 0.2526 0.2017 0.0253  -0.0187 -0.0193 1117 ALA A C   
8294  O O   . ALA A 1119 ? 0.2263 0.2453 0.1972 0.0247  -0.0170 -0.0167 1117 ALA A O   
8295  C CB  . ALA A 1119 ? 0.2541 0.2813 0.2259 0.0262  -0.0210 -0.0186 1117 ALA A CB  
8296  N N   . ALA A 1120 ? 0.2143 0.2380 0.1825 0.0265  -0.0196 -0.0217 1118 ALA A N   
8297  C CA  . ALA A 1120 ? 0.2074 0.2311 0.1732 0.0272  -0.0183 -0.0213 1118 ALA A CA  
8298  C C   . ALA A 1120 ? 0.2107 0.2287 0.1782 0.0256  -0.0172 -0.0215 1118 ALA A C   
8299  O O   . ALA A 1120 ? 0.2139 0.2303 0.1807 0.0255  -0.0154 -0.0190 1118 ALA A O   
8300  C CB  . ALA A 1120 ? 0.2098 0.2374 0.1733 0.0289  -0.0197 -0.0248 1118 ALA A CB  
8301  N N   . ALA A 1121 ? 0.2051 0.2203 0.1753 0.0244  -0.0184 -0.0240 1119 ALA A N   
8302  C CA  . ALA A 1121 ? 0.2152 0.2256 0.1873 0.0227  -0.0176 -0.0241 1119 ALA A CA  
8303  C C   . ALA A 1121 ? 0.1978 0.2058 0.1713 0.0212  -0.0159 -0.0209 1119 ALA A C   
8304  O O   . ALA A 1121 ? 0.2071 0.2124 0.1806 0.0205  -0.0143 -0.0195 1119 ALA A O   
8305  C CB  . ALA A 1121 ? 0.2342 0.2426 0.2094 0.0215  -0.0196 -0.0272 1119 ALA A CB  
8306  N N   . LEU A 1122 ? 0.2020 0.2111 0.1772 0.0207  -0.0162 -0.0199 1120 LEU A N   
8307  C CA  . LEU A 1122 ? 0.1943 0.2016 0.1712 0.0195  -0.0147 -0.0175 1120 LEU A CA  
8308  C C   . LEU A 1122 ? 0.1996 0.2074 0.1749 0.0205  -0.0131 -0.0147 1120 LEU A C   
8309  O O   . LEU A 1122 ? 0.1961 0.2016 0.1723 0.0197  -0.0116 -0.0132 1120 LEU A O   
8310  C CB  . LEU A 1122 ? 0.2205 0.2294 0.1999 0.0189  -0.0155 -0.0175 1120 LEU A CB  
8311  C CG  . LEU A 1122 ? 0.2132 0.2216 0.1951 0.0175  -0.0170 -0.0197 1120 LEU A CG  
8312  C CD1 . LEU A 1122 ? 0.2265 0.2371 0.2105 0.0173  -0.0177 -0.0195 1120 LEU A CD1 
8313  C CD2 . LEU A 1122 ? 0.2292 0.2344 0.2130 0.0154  -0.0163 -0.0196 1120 LEU A CD2 
8314  N N   . ALA A 1123 ? 0.2016 0.2127 0.1748 0.0223  -0.0135 -0.0139 1121 ALA A N   
8315  C CA  . ALA A 1123 ? 0.2038 0.2157 0.1760 0.0232  -0.0123 -0.0108 1121 ALA A CA  
8316  C C   . ALA A 1123 ? 0.2092 0.2190 0.1801 0.0231  -0.0109 -0.0102 1121 ALA A C   
8317  O O   . ALA A 1123 ? 0.2103 0.2193 0.1814 0.0232  -0.0096 -0.0076 1121 ALA A O   
8318  C CB  . ALA A 1123 ? 0.2012 0.2179 0.1712 0.0250  -0.0131 -0.0097 1121 ALA A CB  
8319  N N   . THR A 1124 ? 0.1863 0.1951 0.1560 0.0229  -0.0112 -0.0128 1122 THR A N   
8320  C CA  . THR A 1124 ? 0.1907 0.1974 0.1592 0.0228  -0.0100 -0.0126 1122 THR A CA  
8321  C C   . THR A 1124 ? 0.1905 0.1930 0.1613 0.0209  -0.0095 -0.0133 1122 THR A C   
8322  O O   . THR A 1124 ? 0.2136 0.2140 0.1838 0.0206  -0.0089 -0.0137 1122 THR A O   
8323  C CB  . THR A 1124 ? 0.1991 0.2082 0.1651 0.0242  -0.0108 -0.0149 1122 THR A CB  
8324  O OG1 . THR A 1124 ? 0.2021 0.2117 0.1691 0.0241  -0.0128 -0.0182 1122 THR A OG1 
8325  C CG2 . THR A 1124 ? 0.2228 0.2370 0.1863 0.0261  -0.0107 -0.0131 1122 THR A CG2 
8326  N N   . GLY A 1125 ? 0.1882 0.1896 0.1614 0.0196  -0.0097 -0.0132 1123 GLY A N   
8327  C CA  . GLY A 1125 ? 0.2182 0.2166 0.1935 0.0177  -0.0090 -0.0131 1123 GLY A CA  
8328  C C   . GLY A 1125 ? 0.2083 0.2052 0.1850 0.0164  -0.0102 -0.0152 1123 GLY A C   
8329  O O   . GLY A 1125 ? 0.2193 0.2141 0.1976 0.0147  -0.0096 -0.0147 1123 GLY A O   
8330  N N   . ASN A 1126 ? 0.2022 0.2002 0.1785 0.0172  -0.0119 -0.0174 1124 ASN A N   
8331  C CA  . ASN A 1126 ? 0.2066 0.2028 0.1848 0.0161  -0.0133 -0.0194 1124 ASN A CA  
8332  C C   . ASN A 1126 ? 0.2012 0.1977 0.1826 0.0144  -0.0145 -0.0199 1124 ASN A C   
8333  O O   . ASN A 1126 ? 0.2225 0.2211 0.2041 0.0147  -0.0146 -0.0194 1124 ASN A O   
8334  C CB  . ASN A 1126 ? 0.2106 0.2083 0.1876 0.0178  -0.0149 -0.0222 1124 ASN A CB  
8335  C CG  . ASN A 1126 ? 0.2188 0.2170 0.1927 0.0194  -0.0139 -0.0220 1124 ASN A CG  
8336  O OD1 . ASN A 1126 ? 0.2245 0.2202 0.1987 0.0189  -0.0132 -0.0218 1124 ASN A OD1 
8337  N ND2 . ASN A 1126 ? 0.2074 0.2092 0.1785 0.0213  -0.0136 -0.0218 1124 ASN A ND2 
8338  N N   . SER A 1127 ? 0.2226 0.2170 0.2067 0.0128  -0.0155 -0.0206 1125 SER A N   
8339  C CA  . SER A 1127 ? 0.2320 0.2269 0.2195 0.0113  -0.0173 -0.0215 1125 SER A CA  
8340  C C   . SER A 1127 ? 0.2210 0.2162 0.2090 0.0125  -0.0198 -0.0247 1125 SER A C   
8341  O O   . SER A 1127 ? 0.2253 0.2205 0.2111 0.0143  -0.0199 -0.0262 1125 SER A O   
8342  C CB  . SER A 1127 ? 0.2417 0.2346 0.2326 0.0087  -0.0174 -0.0201 1125 SER A CB  
8343  O OG  . SER A 1127 ? 0.3013 0.2915 0.2928 0.0086  -0.0181 -0.0208 1125 SER A OG  
8344  N N   . VAL A 1128 ? 0.2359 0.2317 0.2271 0.0115  -0.0217 -0.0259 1126 VAL A N   
8345  C CA  . VAL A 1128 ? 0.2425 0.2390 0.2347 0.0127  -0.0243 -0.0294 1126 VAL A CA  
8346  C C   . VAL A 1128 ? 0.2340 0.2287 0.2316 0.0106  -0.0267 -0.0303 1126 VAL A C   
8347  O O   . VAL A 1128 ? 0.2592 0.2538 0.2596 0.0083  -0.0265 -0.0280 1126 VAL A O   
8348  C CB  . VAL A 1128 ? 0.2384 0.2387 0.2285 0.0145  -0.0249 -0.0306 1126 VAL A CB  
8349  C CG1 . VAL A 1128 ? 0.2447 0.2470 0.2300 0.0164  -0.0228 -0.0293 1126 VAL A CG1 
8350  C CG2 . VAL A 1128 ? 0.2541 0.2556 0.2467 0.0128  -0.0250 -0.0292 1126 VAL A CG2 
8351  N N   . ALA A 1129 ? 0.2178 0.2116 0.2175 0.0115  -0.0292 -0.0336 1127 ALA A N   
8352  C CA  . ALA A 1129 ? 0.2513 0.2440 0.2568 0.0099  -0.0323 -0.0352 1127 ALA A CA  
8353  C C   . ALA A 1129 ? 0.2214 0.2168 0.2265 0.0120  -0.0344 -0.0393 1127 ALA A C   
8354  O O   . ALA A 1129 ? 0.2592 0.2554 0.2620 0.0145  -0.0350 -0.0424 1127 ALA A O   
8355  C CB  . ALA A 1129 ? 0.3085 0.2974 0.3179 0.0091  -0.0339 -0.0360 1127 ALA A CB  
8356  N N   . ILE A 1130 ? 0.2220 0.2191 0.2292 0.0111  -0.0356 -0.0393 1128 ILE A N   
8357  C CA  . ILE A 1130 ? 0.2296 0.2298 0.2362 0.0130  -0.0376 -0.0429 1128 ILE A CA  
8358  C C   . ILE A 1130 ? 0.3015 0.3001 0.3144 0.0123  -0.0414 -0.0463 1128 ILE A C   
8359  O O   . ILE A 1130 ? 0.2735 0.2699 0.2918 0.0095  -0.0426 -0.0445 1128 ILE A O   
8360  C CB  . ILE A 1130 ? 0.2224 0.2258 0.2279 0.0127  -0.0368 -0.0412 1128 ILE A CB  
8361  C CG1 . ILE A 1130 ? 0.2615 0.2659 0.2621 0.0131  -0.0332 -0.0376 1128 ILE A CG1 
8362  C CG2 . ILE A 1130 ? 0.2589 0.2661 0.2630 0.0150  -0.0387 -0.0449 1128 ILE A CG2 
8363  C CD1 . ILE A 1130 ? 0.2590 0.2660 0.2597 0.0124  -0.0324 -0.0356 1128 ILE A CD1 
8364  N N   . ASP A 1131 ? 0.2658 0.2658 0.2783 0.0147  -0.0435 -0.0511 1129 ASP A N   
8365  C CA  . ASP A 1131 ? 0.2719 0.2706 0.2908 0.0145  -0.0475 -0.0551 1129 ASP A CA  
8366  C C   . ASP A 1131 ? 0.2786 0.2782 0.3015 0.0126  -0.0493 -0.0545 1129 ASP A C   
8367  O O   . ASP A 1131 ? 0.2672 0.2708 0.2875 0.0138  -0.0492 -0.0555 1129 ASP A O   
8368  C CB  . ASP A 1131 ? 0.2479 0.2498 0.2646 0.0179  -0.0492 -0.0609 1129 ASP A CB  
8369  C CG  . ASP A 1131 ? 0.3390 0.3397 0.3626 0.0180  -0.0537 -0.0658 1129 ASP A CG  
8370  O OD1 . ASP A 1131 ? 0.2819 0.2781 0.3122 0.0155  -0.0554 -0.0647 1129 ASP A OD1 
8371  O OD2 . ASP A 1131 ? 0.3013 0.3060 0.3240 0.0204  -0.0556 -0.0708 1129 ASP A OD2 
8372  N N   . ALA A 1132 ? 0.2875 0.2839 0.3173 0.0096  -0.0509 -0.0528 1130 ALA A N   
8373  C CA  . ALA A 1132 ? 0.3178 0.3152 0.3520 0.0077  -0.0526 -0.0520 1130 ALA A CA  
8374  C C   . ALA A 1132 ? 0.3474 0.3465 0.3848 0.0092  -0.0565 -0.0575 1130 ALA A C   
8375  O O   . ALA A 1132 ? 0.3541 0.3555 0.3930 0.0085  -0.0575 -0.0576 1130 ALA A O   
8376  C CB  . ALA A 1132 ? 0.3456 0.3397 0.3867 0.0039  -0.0535 -0.0483 1130 ALA A CB  
8377  N N   . ALA A 1133 ? 0.2917 0.2898 0.3301 0.0113  -0.0586 -0.0624 1131 ALA A N   
8378  C CA  . ALA A 1133 ? 0.3124 0.3125 0.3539 0.0131  -0.0625 -0.0684 1131 ALA A CA  
8379  C C   . ALA A 1133 ? 0.3219 0.3279 0.3567 0.0157  -0.0614 -0.0704 1131 ALA A C   
8380  O O   . ALA A 1133 ? 0.3696 0.3782 0.4063 0.0171  -0.0644 -0.0752 1131 ALA A O   
8381  C CB  . ALA A 1133 ? 0.3386 0.3368 0.3832 0.0149  -0.0651 -0.0735 1131 ALA A CB  
8382  N N   . SER A 1134 ? 0.3349 0.3430 0.3622 0.0165  -0.0574 -0.0669 1132 SER A N   
8383  C CA  . SER A 1134 ? 0.3032 0.3170 0.3245 0.0187  -0.0564 -0.0678 1132 SER A CA  
8384  C C   . SER A 1134 ? 0.2974 0.3130 0.3210 0.0173  -0.0574 -0.0666 1132 SER A C   
8385  O O   . SER A 1134 ? 0.3130 0.3335 0.3335 0.0192  -0.0579 -0.0685 1132 SER A O   
8386  C CB  . SER A 1134 ? 0.2949 0.3098 0.3090 0.0194  -0.0520 -0.0634 1132 SER A CB  
8387  O OG  . SER A 1134 ? 0.2947 0.3073 0.3097 0.0166  -0.0499 -0.0580 1132 SER A OG  
8388  N N   . GLY A 1135 ? 0.3259 0.3382 0.3549 0.0140  -0.0577 -0.0633 1133 GLY A N   
8389  C CA  . GLY A 1135 ? 0.3051 0.3193 0.3365 0.0125  -0.0584 -0.0618 1133 GLY A CA  
8390  C C   . GLY A 1135 ? 0.3474 0.3647 0.3730 0.0129  -0.0550 -0.0581 1133 GLY A C   
8391  O O   . GLY A 1135 ? 0.3545 0.3747 0.3811 0.0125  -0.0557 -0.0578 1133 GLY A O   
8392  N N   . LEU A 1136 ? 0.2910 0.3080 0.3112 0.0137  -0.0516 -0.0553 1134 LEU A N   
8393  C CA  . LEU A 1136 ? 0.3156 0.3356 0.3306 0.0144  -0.0487 -0.0522 1134 LEU A CA  
8394  C C   . LEU A 1136 ? 0.2896 0.3078 0.3059 0.0119  -0.0462 -0.0472 1134 LEU A C   
8395  O O   . LEU A 1136 ? 0.2976 0.3175 0.3100 0.0124  -0.0435 -0.0443 1134 LEU A O   
8396  C CB  . LEU A 1136 ? 0.3149 0.3364 0.3232 0.0171  -0.0467 -0.0523 1134 LEU A CB  
8397  C CG  . LEU A 1136 ? 0.2905 0.3159 0.2963 0.0200  -0.0487 -0.0571 1134 LEU A CG  
8398  C CD1 . LEU A 1136 ? 0.2931 0.3200 0.2928 0.0223  -0.0465 -0.0567 1134 LEU A CD1 
8399  C CD2 . LEU A 1136 ? 0.3067 0.3369 0.3115 0.0209  -0.0498 -0.0576 1134 LEU A CD2 
8400  N N   . GLN A 1137 ? 0.3048 0.3202 0.3269 0.0090  -0.0472 -0.0460 1135 GLN A N   
8401  C CA  . GLN A 1137 ? 0.3406 0.3552 0.3640 0.0065  -0.0449 -0.0414 1135 GLN A CA  
8402  C C   . GLN A 1137 ? 0.3044 0.3228 0.3265 0.0066  -0.0435 -0.0396 1135 GLN A C   
8403  O O   . GLN A 1137 ? 0.3138 0.3327 0.3336 0.0063  -0.0405 -0.0364 1135 GLN A O   
8404  C CB  . GLN A 1137 ? 0.3458 0.3583 0.3765 0.0033  -0.0468 -0.0405 1135 GLN A CB  
8405  C CG  . GLN A 1137 ? 0.3209 0.3291 0.3535 0.0026  -0.0473 -0.0406 1135 GLN A CG  
8406  C CD  . GLN A 1137 ? 0.3269 0.3336 0.3617 0.0041  -0.0508 -0.0455 1135 GLN A CD  
8407  O OE1 . GLN A 1137 ? 0.3601 0.3693 0.3936 0.0061  -0.0524 -0.0490 1135 GLN A OE1 
8408  N NE2 . GLN A 1137 ? 0.3865 0.3893 0.4247 0.0032  -0.0521 -0.0459 1135 GLN A NE2 
8409  N N   . ALA A 1138 ? 0.3187 0.3399 0.3424 0.0072  -0.0457 -0.0418 1136 ALA A N   
8410  C CA  . ALA A 1138 ? 0.3221 0.3469 0.3451 0.0073  -0.0447 -0.0401 1136 ALA A CA  
8411  C C   . ALA A 1138 ? 0.3732 0.3998 0.3900 0.0099  -0.0425 -0.0392 1136 ALA A C   
8412  O O   . ALA A 1138 ? 0.3954 0.4246 0.4117 0.0100  -0.0413 -0.0374 1136 ALA A O   
8413  C CB  . ALA A 1138 ? 0.3460 0.3733 0.3723 0.0074  -0.0478 -0.0427 1136 ALA A CB  
8414  N N   . SER A 1139 ? 0.3328 0.3585 0.3453 0.0119  -0.0419 -0.0404 1137 SER A N   
8415  C CA  . SER A 1139 ? 0.3145 0.3421 0.3216 0.0141  -0.0399 -0.0389 1137 SER A CA  
8416  C C   . SER A 1139 ? 0.3007 0.3264 0.3065 0.0134  -0.0366 -0.0353 1137 SER A C   
8417  O O   . SER A 1139 ? 0.3424 0.3695 0.3447 0.0149  -0.0349 -0.0336 1137 SER A O   
8418  C CB  . SER A 1139 ? 0.3073 0.3354 0.3103 0.0165  -0.0405 -0.0414 1137 SER A CB  
8419  O OG  . SER A 1139 ? 0.3610 0.3921 0.3645 0.0178  -0.0434 -0.0449 1137 SER A OG  
8420  N N   . LEU A 1140 ? 0.3049 0.3278 0.3135 0.0111  -0.0359 -0.0341 1138 LEU A N   
8421  C CA  . LEU A 1140 ? 0.3133 0.3346 0.3206 0.0103  -0.0329 -0.0312 1138 LEU A CA  
8422  C C   . LEU A 1140 ? 0.3234 0.3456 0.3347 0.0079  -0.0321 -0.0291 1138 LEU A C   
8423  O O   . LEU A 1140 ? 0.3960 0.4165 0.4083 0.0062  -0.0307 -0.0273 1138 LEU A O   
8424  C CB  . LEU A 1140 ? 0.3726 0.3902 0.3788 0.0100  -0.0324 -0.0313 1138 LEU A CB  
8425  C CG  . LEU A 1140 ? 0.4099 0.4269 0.4113 0.0124  -0.0318 -0.0322 1138 LEU A CG  
8426  C CD1 . LEU A 1140 ? 0.3705 0.3840 0.3715 0.0116  -0.0306 -0.0313 1138 LEU A CD1 
8427  C CD2 . LEU A 1140 ? 0.3202 0.3396 0.3179 0.0143  -0.0301 -0.0305 1138 LEU A CD2 
8428  N N   . LYS A 1141 ? 0.3365 0.3617 0.3500 0.0077  -0.0330 -0.0293 1139 LYS A N   
8429  C CA  . LYS A 1141 ? 0.4282 0.4554 0.4457 0.0055  -0.0323 -0.0276 1139 LYS A CA  
8430  C C   . LYS A 1141 ? 0.3582 0.3867 0.3740 0.0061  -0.0295 -0.0255 1139 LYS A C   
8431  O O   . LYS A 1141 ? 0.3652 0.3943 0.3780 0.0083  -0.0288 -0.0255 1139 LYS A O   
8432  C CB  . LYS A 1141 ? 0.4033 0.4335 0.4240 0.0051  -0.0344 -0.0287 1139 LYS A CB  
8433  N N   . ASN A 1142 ? 0.3518 0.3811 0.3698 0.0040  -0.0279 -0.0238 1140 ASN A N   
8434  C CA  . ASN A 1142 ? 0.3559 0.3873 0.3736 0.0044  -0.0255 -0.0224 1140 ASN A CA  
8435  C C   . ASN A 1142 ? 0.3401 0.3691 0.3537 0.0062  -0.0237 -0.0218 1140 ASN A C   
8436  O O   . ASN A 1142 ? 0.3299 0.3601 0.3426 0.0077  -0.0225 -0.0214 1140 ASN A O   
8437  C CB  . ASN A 1142 ? 0.4288 0.4640 0.4480 0.0055  -0.0259 -0.0229 1140 ASN A CB  
8438  C CG  . ASN A 1142 ? 0.4835 0.5212 0.5068 0.0039  -0.0279 -0.0235 1140 ASN A CG  
8439  O OD1 . ASN A 1142 ? 0.5298 0.5682 0.5533 0.0050  -0.0298 -0.0249 1140 ASN A OD1 
8440  N ND2 . ASN A 1142 ? 0.4716 0.5111 0.4984 0.0012  -0.0275 -0.0224 1140 ASN A ND2 
8441  N N   . LEU A 1143 ? 0.3488 0.3742 0.3602 0.0060  -0.0236 -0.0218 1141 LEU A N   
8442  C CA  . LEU A 1143 ? 0.3195 0.3426 0.3272 0.0075  -0.0219 -0.0211 1141 LEU A CA  
8443  C C   . LEU A 1143 ? 0.3596 0.3841 0.3683 0.0068  -0.0196 -0.0197 1141 LEU A C   
8444  O O   . LEU A 1143 ? 0.3442 0.3706 0.3556 0.0046  -0.0191 -0.0190 1141 LEU A O   
8445  C CB  . LEU A 1143 ? 0.3091 0.3286 0.3150 0.0071  -0.0221 -0.0213 1141 LEU A CB  
8446  C CG  . LEU A 1143 ? 0.3332 0.3512 0.3371 0.0086  -0.0240 -0.0231 1141 LEU A CG  
8447  C CD1 . LEU A 1143 ? 0.3223 0.3368 0.3253 0.0080  -0.0242 -0.0235 1141 LEU A CD1 
8448  C CD2 . LEU A 1143 ? 0.3083 0.3270 0.3086 0.0113  -0.0235 -0.0231 1141 LEU A CD2 
8449  N N   . PRO A 1144 ? 0.3004 0.3245 0.3071 0.0085  -0.0182 -0.0192 1142 PRO A N   
8450  C CA  . PRO A 1144 ? 0.3071 0.3320 0.3144 0.0080  -0.0160 -0.0183 1142 PRO A CA  
8451  C C   . PRO A 1144 ? 0.3017 0.3245 0.3082 0.0062  -0.0153 -0.0176 1142 PRO A C   
8452  O O   . PRO A 1144 ? 0.2887 0.3083 0.2933 0.0062  -0.0160 -0.0176 1142 PRO A O   
8453  C CB  . PRO A 1144 ? 0.3682 0.3914 0.3732 0.0104  -0.0152 -0.0180 1142 PRO A CB  
8454  C CG  . PRO A 1144 ? 0.3805 0.4036 0.3844 0.0121  -0.0169 -0.0184 1142 PRO A CG  
8455  C CD  . PRO A 1144 ? 0.3443 0.3669 0.3480 0.0110  -0.0186 -0.0193 1142 PRO A CD  
8456  N N   . GLN A 1145 ? 0.3281 0.3534 0.3364 0.0046  -0.0138 -0.0169 1143 GLN A N   
8457  C CA  . GLN A 1145 ? 0.3290 0.3529 0.3369 0.0027  -0.0132 -0.0157 1143 GLN A CA  
8458  C C   . GLN A 1145 ? 0.2872 0.3068 0.2917 0.0039  -0.0125 -0.0154 1143 GLN A C   
8459  O O   . GLN A 1145 ? 0.2912 0.3082 0.2950 0.0028  -0.0130 -0.0148 1143 GLN A O   
8460  C CB  . GLN A 1145 ? 0.3724 0.4007 0.3824 0.0012  -0.0115 -0.0150 1143 GLN A CB  
8461  N N   . THR A 1146 ? 0.3064 0.3252 0.3091 0.0060  -0.0116 -0.0157 1144 THR A N   
8462  C CA  . THR A 1146 ? 0.2983 0.3133 0.2979 0.0071  -0.0110 -0.0153 1144 THR A CA  
8463  C C   . THR A 1146 ? 0.2705 0.2826 0.2682 0.0076  -0.0125 -0.0157 1144 THR A C   
8464  O O   . THR A 1146 ? 0.2921 0.3013 0.2880 0.0075  -0.0123 -0.0154 1144 THR A O   
8465  C CB  . THR A 1146 ? 0.2995 0.3143 0.2983 0.0093  -0.0101 -0.0153 1144 THR A CB  
8466  O OG1 . THR A 1146 ? 0.3103 0.3264 0.3097 0.0107  -0.0114 -0.0158 1144 THR A OG1 
8467  C CG2 . THR A 1146 ? 0.2787 0.2959 0.2794 0.0090  -0.0086 -0.0154 1144 THR A CG2 
8468  N N   . VAL A 1147 ? 0.2777 0.2908 0.2758 0.0085  -0.0141 -0.0167 1145 VAL A N   
8469  C CA  . VAL A 1147 ? 0.2690 0.2802 0.2654 0.0092  -0.0157 -0.0177 1145 VAL A CA  
8470  C C   . VAL A 1147 ? 0.2662 0.2766 0.2647 0.0072  -0.0171 -0.0182 1145 VAL A C   
8471  O O   . VAL A 1147 ? 0.2570 0.2647 0.2545 0.0072  -0.0179 -0.0188 1145 VAL A O   
8472  C CB  . VAL A 1147 ? 0.2531 0.2661 0.2491 0.0109  -0.0171 -0.0186 1145 VAL A CB  
8473  C CG1 . VAL A 1147 ? 0.2382 0.2500 0.2321 0.0120  -0.0187 -0.0200 1145 VAL A CG1 
8474  C CG2 . VAL A 1147 ? 0.2745 0.2886 0.2695 0.0128  -0.0160 -0.0175 1145 VAL A CG2 
8475  N N   . GLY A 1148 ? 0.2590 0.2718 0.2610 0.0053  -0.0175 -0.0179 1146 GLY A N   
8476  C CA  . GLY A 1148 ? 0.2624 0.2745 0.2673 0.0030  -0.0189 -0.0178 1146 GLY A CA  
8477  C C   . GLY A 1148 ? 0.2859 0.2954 0.2903 0.0018  -0.0182 -0.0166 1146 GLY A C   
8478  O O   . GLY A 1148 ? 0.2912 0.2984 0.2971 0.0009  -0.0198 -0.0169 1146 GLY A O   
8479  N N   . LEU A 1149 ? 0.2541 0.2639 0.2569 0.0019  -0.0159 -0.0153 1147 LEU A N   
8480  C CA  . LEU A 1149 ? 0.2942 0.3017 0.2964 0.0009  -0.0151 -0.0140 1147 LEU A CA  
8481  C C   . LEU A 1149 ? 0.2771 0.2806 0.2770 0.0023  -0.0159 -0.0151 1147 LEU A C   
8482  O O   . LEU A 1149 ? 0.3174 0.3186 0.3180 0.0013  -0.0163 -0.0145 1147 LEU A O   
8483  C CB  . LEU A 1149 ? 0.3072 0.3160 0.3079 0.0011  -0.0126 -0.0129 1147 LEU A CB  
8484  C CG  . LEU A 1149 ? 0.3949 0.4083 0.3980 -0.0007 -0.0116 -0.0117 1147 LEU A CG  
8485  C CD1 . LEU A 1149 ? 0.4433 0.4580 0.4448 0.0001  -0.0093 -0.0115 1147 LEU A CD1 
8486  C CD2 . LEU A 1149 ? 0.4055 0.4197 0.4113 -0.0036 -0.0123 -0.0099 1147 LEU A CD2 
8487  N N   . ARG A 1150 ? 0.2671 0.2703 0.2645 0.0048  -0.0162 -0.0167 1148 ARG A N   
8488  C CA  . ARG A 1150 ? 0.2615 0.2619 0.2564 0.0064  -0.0168 -0.0180 1148 ARG A CA  
8489  C C   . ARG A 1150 ? 0.2668 0.2667 0.2633 0.0066  -0.0195 -0.0202 1148 ARG A C   
8490  O O   . ARG A 1150 ? 0.2681 0.2662 0.2631 0.0080  -0.0203 -0.0218 1148 ARG A O   
8491  C CB  . ARG A 1150 ? 0.2794 0.2807 0.2708 0.0089  -0.0158 -0.0182 1148 ARG A CB  
8492  C CG  . ARG A 1150 ? 0.3174 0.3185 0.3074 0.0091  -0.0134 -0.0163 1148 ARG A CG  
8493  C CD  . ARG A 1150 ? 0.3114 0.3106 0.2981 0.0108  -0.0127 -0.0163 1148 ARG A CD  
8494  N NE  . ARG A 1150 ? 0.2778 0.2771 0.2634 0.0114  -0.0107 -0.0147 1148 ARG A NE  
8495  C CZ  . ARG A 1150 ? 0.2726 0.2723 0.2561 0.0133  -0.0102 -0.0141 1148 ARG A CZ  
8496  N NH1 . ARG A 1150 ? 0.2347 0.2352 0.2163 0.0149  -0.0112 -0.0149 1148 ARG A NH1 
8497  N NH2 . ARG A 1150 ? 0.2406 0.2401 0.2240 0.0136  -0.0086 -0.0127 1148 ARG A NH2 
8498  N N   . VAL A 1151 ? 0.2494 0.2510 0.2491 0.0054  -0.0210 -0.0206 1149 VAL A N   
8499  C CA  . VAL A 1151 ? 0.2516 0.2532 0.2531 0.0059  -0.0237 -0.0232 1149 VAL A CA  
8500  C C   . VAL A 1151 ? 0.3069 0.3071 0.3134 0.0033  -0.0256 -0.0229 1149 VAL A C   
8501  O O   . VAL A 1151 ? 0.3282 0.3298 0.3376 0.0010  -0.0252 -0.0207 1149 VAL A O   
8502  C CB  . VAL A 1151 ? 0.2836 0.2885 0.2852 0.0067  -0.0244 -0.0240 1149 VAL A CB  
8503  C CG1 . VAL A 1151 ? 0.2920 0.2971 0.2962 0.0068  -0.0275 -0.0268 1149 VAL A CG1 
8504  C CG2 . VAL A 1151 ? 0.2601 0.2663 0.2572 0.0093  -0.0230 -0.0241 1149 VAL A CG2 
8505  N N   . SER A 1152 ? 0.2782 0.2759 0.2862 0.0037  -0.0277 -0.0250 1150 SER A N   
8506  C CA  . SER A 1152 ? 0.3033 0.2996 0.3171 0.0015  -0.0303 -0.0251 1150 SER A CA  
8507  C C   . SER A 1152 ? 0.2872 0.2832 0.3025 0.0031  -0.0333 -0.0291 1150 SER A C   
8508  O O   . SER A 1152 ? 0.2880 0.2847 0.2994 0.0058  -0.0332 -0.0317 1150 SER A O   
8509  C CB  . SER A 1152 ? 0.3007 0.2938 0.3164 0.0001  -0.0304 -0.0236 1150 SER A CB  
8510  O OG  . SER A 1152 ? 0.3687 0.3595 0.3818 0.0023  -0.0305 -0.0259 1150 SER A OG  
8511  N N   . TRP A 1153 ? 0.2890 0.2845 0.3102 0.0012  -0.0361 -0.0296 1151 TRP A N   
8512  C CA  . TRP A 1153 ? 0.2820 0.2771 0.3058 0.0025  -0.0394 -0.0338 1151 TRP A CA  
8513  C C   . TRP A 1153 ? 0.3132 0.3044 0.3421 0.0014  -0.0419 -0.0347 1151 TRP A C   
8514  O O   . TRP A 1153 ? 0.3525 0.3421 0.3855 -0.0014 -0.0421 -0.0313 1151 TRP A O   
8515  C CB  . TRP A 1153 ? 0.2922 0.2897 0.3195 0.0013  -0.0411 -0.0340 1151 TRP A CB  
8516  C CG  . TRP A 1153 ? 0.3195 0.3207 0.3423 0.0028  -0.0393 -0.0340 1151 TRP A CG  
8517  C CD1 . TRP A 1153 ? 0.3192 0.3226 0.3398 0.0020  -0.0366 -0.0307 1151 TRP A CD1 
8518  C CD2 . TRP A 1153 ? 0.2915 0.2949 0.3115 0.0055  -0.0403 -0.0375 1151 TRP A CD2 
8519  N NE1 . TRP A 1153 ? 0.3466 0.3530 0.3637 0.0039  -0.0359 -0.0318 1151 TRP A NE1 
8520  C CE2 . TRP A 1153 ? 0.3280 0.3346 0.3445 0.0060  -0.0381 -0.0357 1151 TRP A CE2 
8521  C CE3 . TRP A 1153 ? 0.2797 0.2832 0.3000 0.0075  -0.0430 -0.0420 1151 TRP A CE3 
8522  C CZ2 . TRP A 1153 ? 0.2915 0.3012 0.3048 0.0084  -0.0385 -0.0378 1151 TRP A CZ2 
8523  C CZ3 . TRP A 1153 ? 0.3202 0.3273 0.3370 0.0099  -0.0432 -0.0443 1151 TRP A CZ3 
8524  C CH2 . TRP A 1153 ? 0.3414 0.3515 0.3547 0.0103  -0.0411 -0.0420 1151 TRP A CH2 
8525  N N   . SER A 1154 ? 0.2974 0.2875 0.3264 0.0037  -0.0440 -0.0392 1152 SER A N   
8526  C CA  . SER A 1154 ? 0.3139 0.3001 0.3476 0.0033  -0.0463 -0.0405 1152 SER A CA  
8527  C C   . SER A 1154 ? 0.3250 0.3107 0.3642 0.0040  -0.0506 -0.0453 1152 SER A C   
8528  O O   . SER A 1154 ? 0.3173 0.3053 0.3535 0.0070  -0.0513 -0.0498 1152 SER A O   
8529  C CB  . SER A 1154 ? 0.2921 0.2771 0.3212 0.0056  -0.0446 -0.0418 1152 SER A CB  
8530  O OG  . SER A 1154 ? 0.3245 0.3059 0.3587 0.0054  -0.0472 -0.0435 1152 SER A OG  
8531  N N   . LYS A 1155 ? 0.3220 0.3053 0.3694 0.0014  -0.0536 -0.0443 1153 LYS A N   
8532  C CA  . LYS A 1155 ? 0.3858 0.3677 0.4398 0.0020  -0.0582 -0.0491 1153 LYS A CA  
8533  C C   . LYS A 1155 ? 0.3937 0.3720 0.4508 0.0032  -0.0602 -0.0520 1153 LYS A C   
8534  O O   . LYS A 1155 ? 0.5374 0.5156 0.5969 0.0055  -0.0632 -0.0579 1153 LYS A O   
8535  C CB  . LYS A 1155 ? 0.3964 0.3776 0.4588 -0.0015 -0.0608 -0.0465 1153 LYS A CB  
8536  N N   . ASP A 1156 ? 0.3512 0.3269 0.4083 0.0019  -0.0586 -0.0484 1154 ASP A N   
8537  C CA  . ASP A 1156 ? 0.3521 0.3241 0.4124 0.0029  -0.0604 -0.0506 1154 ASP A CA  
8538  C C   . ASP A 1156 ? 0.3536 0.3264 0.4056 0.0047  -0.0562 -0.0495 1154 ASP A C   
8539  O O   . ASP A 1156 ? 0.3566 0.3283 0.4072 0.0027  -0.0538 -0.0444 1154 ASP A O   
8540  C CB  . ASP A 1156 ? 0.3799 0.3480 0.4489 -0.0007 -0.0625 -0.0464 1154 ASP A CB  
8541  C CG  . ASP A 1156 ? 0.5313 0.4953 0.6047 0.0002  -0.0647 -0.0486 1154 ASP A CG  
8542  O OD1 . ASP A 1156 ? 0.5241 0.4886 0.5939 0.0037  -0.0645 -0.0537 1154 ASP A OD1 
8543  O OD2 . ASP A 1156 ? 0.5228 0.4835 0.6036 -0.0027 -0.0667 -0.0450 1154 ASP A OD2 
8544  N N   . TRP A 1157 ? 0.3246 0.2997 0.3712 0.0083  -0.0555 -0.0543 1155 TRP A N   
8545  C CA  . TRP A 1157 ? 0.2909 0.2673 0.3294 0.0100  -0.0515 -0.0530 1155 TRP A CA  
8546  C C   . TRP A 1157 ? 0.3451 0.3177 0.3857 0.0092  -0.0512 -0.0511 1155 TRP A C   
8547  O O   . TRP A 1157 ? 0.3386 0.3113 0.3742 0.0088  -0.0477 -0.0474 1155 TRP A O   
8548  C CB  . TRP A 1157 ? 0.3316 0.3118 0.3651 0.0140  -0.0514 -0.0585 1155 TRP A CB  
8549  C CG  . TRP A 1157 ? 0.2887 0.2731 0.3198 0.0152  -0.0518 -0.0608 1155 TRP A CG  
8550  C CD1 . TRP A 1157 ? 0.2790 0.2645 0.3107 0.0133  -0.0517 -0.0582 1155 TRP A CD1 
8551  C CD2 . TRP A 1157 ? 0.2728 0.2615 0.3006 0.0187  -0.0527 -0.0664 1155 TRP A CD2 
8552  N NE1 . TRP A 1157 ? 0.3144 0.3043 0.3435 0.0154  -0.0524 -0.0617 1155 TRP A NE1 
8553  C CE2 . TRP A 1157 ? 0.2980 0.2901 0.3246 0.0187  -0.0531 -0.0667 1155 TRP A CE2 
8554  C CE3 . TRP A 1157 ? 0.2787 0.2694 0.3047 0.0219  -0.0532 -0.0713 1155 TRP A CE3 
8555  C CZ2 . TRP A 1157 ? 0.2918 0.2891 0.3151 0.0217  -0.0539 -0.0715 1155 TRP A CZ2 
8556  C CZ3 . TRP A 1157 ? 0.2883 0.2846 0.3109 0.0249  -0.0539 -0.0761 1155 TRP A CZ3 
8557  C CH2 . TRP A 1157 ? 0.3369 0.3365 0.3582 0.0248  -0.0544 -0.0761 1155 TRP A CH2 
8558  N N   . ALA A 1158 ? 0.3436 0.3129 0.3918 0.0091  -0.0550 -0.0537 1156 ALA A N   
8559  C CA  . ALA A 1158 ? 0.3552 0.3210 0.4058 0.0086  -0.0550 -0.0522 1156 ALA A CA  
8560  C C   . ALA A 1158 ? 0.4264 0.3901 0.4788 0.0047  -0.0536 -0.0450 1156 ALA A C   
8561  O O   . ALA A 1158 ? 0.4916 0.4534 0.5428 0.0042  -0.0520 -0.0422 1156 ALA A O   
8562  C CB  . ALA A 1158 ? 0.3922 0.3547 0.4515 0.0094  -0.0598 -0.0568 1156 ALA A CB  
8563  N N   . ALA A 1159 ? 0.3673 0.3318 0.4225 0.0020  -0.0542 -0.0419 1157 ALA A N   
8564  C CA  . ALA A 1159 ? 0.4333 0.3971 0.4900 -0.0018 -0.0529 -0.0351 1157 ALA A CA  
8565  C C   . ALA A 1159 ? 0.4233 0.3903 0.4715 -0.0018 -0.0480 -0.0316 1157 ALA A C   
8566  O O   . ALA A 1159 ? 0.4461 0.4128 0.4939 -0.0041 -0.0462 -0.0266 1157 ALA A O   
8567  C CB  . ALA A 1159 ? 0.3962 0.3605 0.4596 -0.0047 -0.0554 -0.0330 1157 ALA A CB  
8568  N N   . ASP A 1160 ? 0.4000 0.3700 0.4414 0.0007  -0.0459 -0.0342 1158 ASP A N   
8569  C CA  . ASP A 1160 ? 0.3998 0.3729 0.4341 0.0005  -0.0418 -0.0311 1158 ASP A CA  
8570  C C   . ASP A 1160 ? 0.3304 0.3039 0.3577 0.0030  -0.0388 -0.0319 1158 ASP A C   
8571  O O   . ASP A 1160 ? 0.3533 0.3293 0.3747 0.0034  -0.0355 -0.0299 1158 ASP A O   
8572  C CB  . ASP A 1160 ? 0.3604 0.3369 0.3929 0.0010  -0.0417 -0.0324 1158 ASP A CB  
8573  C CG  . ASP A 1160 ? 0.4259 0.4024 0.4654 -0.0017 -0.0444 -0.0311 1158 ASP A CG  
8574  O OD1 . ASP A 1160 ? 0.5019 0.4768 0.5464 -0.0047 -0.0452 -0.0273 1158 ASP A OD1 
8575  O OD2 . ASP A 1160 ? 0.4083 0.3867 0.4485 -0.0010 -0.0458 -0.0337 1158 ASP A OD2 
8576  N N   . GLY A 1161 ? 0.3186 0.2899 0.3466 0.0048  -0.0399 -0.0346 1159 GLY A N   
8577  C CA  . GLY A 1161 ? 0.3472 0.3191 0.3692 0.0069  -0.0371 -0.0350 1159 GLY A CA  
8578  C C   . GLY A 1161 ? 0.3698 0.3396 0.3917 0.0050  -0.0353 -0.0306 1159 GLY A C   
8579  O O   . GLY A 1161 ? 0.4075 0.3764 0.4331 0.0020  -0.0357 -0.0268 1159 GLY A O   
8580  N N   . PRO A 1162 ? 0.3311 0.3006 0.3489 0.0068  -0.0333 -0.0309 1160 PRO A N   
8581  C CA  . PRO A 1162 ? 0.3290 0.3002 0.3424 0.0103  -0.0327 -0.0350 1160 PRO A CA  
8582  C C   . PRO A 1162 ? 0.3508 0.3260 0.3581 0.0115  -0.0303 -0.0348 1160 PRO A C   
8583  O O   . PRO A 1162 ? 0.3316 0.3078 0.3363 0.0101  -0.0279 -0.0311 1160 PRO A O   
8584  C CB  . PRO A 1162 ? 0.3485 0.3181 0.3600 0.0108  -0.0310 -0.0337 1160 PRO A CB  
8585  C CG  . PRO A 1162 ? 0.3857 0.3543 0.3972 0.0078  -0.0292 -0.0283 1160 PRO A CG  
8586  C CD  . PRO A 1162 ? 0.3454 0.3132 0.3628 0.0051  -0.0316 -0.0269 1160 PRO A CD  
8587  N N   . PHE A 1163 ? 0.2851 0.2629 0.2902 0.0143  -0.0309 -0.0388 1161 PHE A N   
8588  C CA  . PHE A 1163 ? 0.2471 0.2289 0.2462 0.0157  -0.0287 -0.0385 1161 PHE A CA  
8589  C C   . PHE A 1163 ? 0.2652 0.2485 0.2594 0.0178  -0.0264 -0.0384 1161 PHE A C   
8590  O O   . PHE A 1163 ? 0.3109 0.2925 0.3061 0.0184  -0.0266 -0.0395 1161 PHE A O   
8591  C CB  . PHE A 1163 ? 0.2369 0.2217 0.2365 0.0173  -0.0309 -0.0425 1161 PHE A CB  
8592  C CG  . PHE A 1163 ? 0.2504 0.2337 0.2555 0.0152  -0.0334 -0.0426 1161 PHE A CG  
8593  C CD1 . PHE A 1163 ? 0.2890 0.2723 0.2942 0.0129  -0.0322 -0.0387 1161 PHE A CD1 
8594  C CD2 . PHE A 1163 ? 0.2647 0.2468 0.2753 0.0156  -0.0371 -0.0467 1161 PHE A CD2 
8595  C CE1 . PHE A 1163 ? 0.3183 0.3009 0.3288 0.0108  -0.0345 -0.0385 1161 PHE A CE1 
8596  C CE2 . PHE A 1163 ? 0.2966 0.2774 0.3127 0.0134  -0.0396 -0.0464 1161 PHE A CE2 
8597  C CZ  . PHE A 1163 ? 0.2899 0.2710 0.3059 0.0110  -0.0382 -0.0422 1161 PHE A CZ  
8598  N N   . ALA A 1164 ? 0.2433 0.2298 0.2324 0.0187  -0.0240 -0.0368 1162 ALA A N   
8599  C CA  . ALA A 1164 ? 0.2438 0.2322 0.2283 0.0205  -0.0217 -0.0361 1162 ALA A CA  
8600  C C   . ALA A 1164 ? 0.2346 0.2283 0.2154 0.0233  -0.0217 -0.0386 1162 ALA A C   
8601  O O   . ALA A 1164 ? 0.2777 0.2740 0.2545 0.0247  -0.0198 -0.0376 1162 ALA A O   
8602  C CB  . ALA A 1164 ? 0.2826 0.2703 0.2646 0.0192  -0.0188 -0.0313 1162 ALA A CB  
8603  N N   . GLY A 1165 ? 0.2430 0.2386 0.2252 0.0238  -0.0240 -0.0415 1163 GLY A N   
8604  C CA  . GLY A 1165 ? 0.2409 0.2422 0.2199 0.0264  -0.0244 -0.0442 1163 GLY A CA  
8605  C C   . GLY A 1165 ? 0.2249 0.2271 0.2064 0.0261  -0.0268 -0.0465 1163 GLY A C   
8606  O O   . GLY A 1165 ? 0.2281 0.2266 0.2137 0.0239  -0.0280 -0.0457 1163 GLY A O   
8607  N N   . ALA A 1166 ? 0.2266 0.2344 0.2057 0.0284  -0.0277 -0.0494 1164 ALA A N   
8608  C CA  . ALA A 1166 ? 0.2268 0.2360 0.2081 0.0283  -0.0302 -0.0519 1164 ALA A CA  
8609  C C   . ALA A 1166 ? 0.2217 0.2376 0.1984 0.0302  -0.0296 -0.0520 1164 ALA A C   
8610  O O   . ALA A 1166 ? 0.2594 0.2797 0.2319 0.0323  -0.0284 -0.0522 1164 ALA A O   
8611  C CB  . ALA A 1166 ? 0.2508 0.2593 0.2367 0.0291  -0.0336 -0.0576 1164 ALA A CB  
8612  N N   . LEU A 1167 ? 0.2095 0.2262 0.1871 0.0295  -0.0307 -0.0516 1165 LEU A N   
8613  C CA  . LEU A 1167 ? 0.1964 0.2196 0.1706 0.0312  -0.0309 -0.0521 1165 LEU A CA  
8614  C C   . LEU A 1167 ? 0.2396 0.2642 0.2170 0.0316  -0.0343 -0.0568 1165 LEU A C   
8615  O O   . LEU A 1167 ? 0.2376 0.2579 0.2196 0.0295  -0.0357 -0.0568 1165 LEU A O   
8616  C CB  . LEU A 1167 ? 0.2218 0.2451 0.1942 0.0300  -0.0290 -0.0469 1165 LEU A CB  
8617  C CG  . LEU A 1167 ? 0.2170 0.2388 0.1868 0.0295  -0.0258 -0.0421 1165 LEU A CG  
8618  C CD1 . LEU A 1167 ? 0.2682 0.2895 0.2375 0.0282  -0.0245 -0.0376 1165 LEU A CD1 
8619  C CD2 . LEU A 1167 ? 0.2434 0.2703 0.2088 0.0318  -0.0247 -0.0422 1165 LEU A CD2 
8620  N N   . VAL A 1168 ? 0.2269 0.2578 0.2021 0.0342  -0.0356 -0.0609 1166 VAL A N   
8621  C CA  . VAL A 1168 ? 0.2327 0.2655 0.2111 0.0351  -0.0391 -0.0664 1166 VAL A CA  
8622  C C   . VAL A 1168 ? 0.2351 0.2754 0.2096 0.0367  -0.0395 -0.0669 1166 VAL A C   
8623  O O   . VAL A 1168 ? 0.2307 0.2769 0.1999 0.0385  -0.0378 -0.0655 1166 VAL A O   
8624  C CB  . VAL A 1168 ? 0.2315 0.2651 0.2120 0.0369  -0.0410 -0.0724 1166 VAL A CB  
8625  C CG1 . VAL A 1168 ? 0.2467 0.2818 0.2313 0.0378  -0.0451 -0.0786 1166 VAL A CG1 
8626  C CG2 . VAL A 1168 ? 0.2368 0.2629 0.2209 0.0353  -0.0406 -0.0714 1166 VAL A CG2 
8627  N N   . GLU A 1169 ? 0.2208 0.2613 0.1982 0.0361  -0.0418 -0.0686 1167 GLU A N   
8628  C CA  . GLU A 1169 ? 0.2125 0.2602 0.1870 0.0377  -0.0428 -0.0698 1167 GLU A CA  
8629  C C   . GLU A 1169 ? 0.2643 0.3144 0.2423 0.0391  -0.0467 -0.0770 1167 GLU A C   
8630  O O   . GLU A 1169 ? 0.2584 0.3030 0.2425 0.0375  -0.0489 -0.0791 1167 GLU A O   
8631  C CB  . GLU A 1169 ? 0.2135 0.2598 0.1886 0.0358  -0.0423 -0.0654 1167 GLU A CB  
8632  C CG  . GLU A 1169 ? 0.2277 0.2813 0.2002 0.0373  -0.0435 -0.0663 1167 GLU A CG  
8633  C CD  . GLU A 1169 ? 0.2415 0.2931 0.2160 0.0354  -0.0436 -0.0628 1167 GLU A CD  
8634  O OE1 . GLU A 1169 ? 0.2442 0.2890 0.2224 0.0329  -0.0430 -0.0605 1167 GLU A OE1 
8635  O OE2 . GLU A 1169 ? 0.2608 0.3181 0.2331 0.0364  -0.0442 -0.0623 1167 GLU A OE2 
8636  N N   . GLY A 1170 ? 0.2336 0.2921 0.2081 0.0419  -0.0476 -0.0807 1168 GLY A N   
8637  C CA  . GLY A 1170 ? 0.2576 0.3191 0.2354 0.0434  -0.0515 -0.0878 1168 GLY A CA  
8638  C C   . GLY A 1170 ? 0.2384 0.3101 0.2116 0.0469  -0.0520 -0.0921 1168 GLY A C   
8639  O O   . GLY A 1170 ? 0.2891 0.3652 0.2569 0.0481  -0.0493 -0.0894 1168 GLY A O   
8640  N N   . ASP A 1171 ? 0.2538 0.3294 0.2295 0.0485  -0.0556 -0.0990 1169 ASP A N   
8641  C CA  . ASP A 1171 ? 0.2626 0.3483 0.2349 0.0521  -0.0565 -0.1046 1169 ASP A CA  
8642  C C   . ASP A 1171 ? 0.2715 0.3554 0.2455 0.0533  -0.0565 -0.1084 1169 ASP A C   
8643  O O   . ASP A 1171 ? 0.2632 0.3379 0.2414 0.0513  -0.0560 -0.1068 1169 ASP A O   
8644  C CB  . ASP A 1171 ? 0.2798 0.3712 0.2539 0.0536  -0.0603 -0.1109 1169 ASP A CB  
8645  C CG  . ASP A 1171 ? 0.3701 0.4549 0.3530 0.0528  -0.0643 -0.1169 1169 ASP A CG  
8646  O OD1 . ASP A 1171 ? 0.3187 0.3960 0.3062 0.0518  -0.0644 -0.1175 1169 ASP A OD1 
8647  O OD2 . ASP A 1171 ? 0.3925 0.4798 0.3780 0.0533  -0.0675 -0.1209 1169 ASP A OD2 
8648  N N   . ALA A 1172 ? 0.2786 0.3720 0.2495 0.0566  -0.0570 -0.1136 1170 ALA A N   
8649  C CA  . ALA A 1172 ? 0.3216 0.4147 0.2932 0.0581  -0.0565 -0.1169 1170 ALA A CA  
8650  C C   . ALA A 1172 ? 0.2679 0.3521 0.2484 0.0573  -0.0596 -0.1218 1170 ALA A C   
8651  O O   . ALA A 1172 ? 0.2804 0.3580 0.2631 0.0563  -0.0584 -0.1203 1170 ALA A O   
8652  C CB  . ALA A 1172 ? 0.3068 0.4128 0.2742 0.0621  -0.0570 -0.1226 1170 ALA A CB  
8653  N N   . GLU A 1173 ? 0.2869 0.3706 0.2728 0.0576  -0.0637 -0.1275 1171 GLU A N   
8654  C CA  . GLU A 1173 ? 0.3312 0.4068 0.3263 0.0568  -0.0670 -0.1322 1171 GLU A CA  
8655  C C   . GLU A 1173 ? 0.3035 0.3672 0.3029 0.0527  -0.0662 -0.1256 1171 GLU A C   
8656  O O   . GLU A 1173 ? 0.3011 0.3573 0.3063 0.0516  -0.0671 -0.1263 1171 GLU A O   
8657  C CB  . GLU A 1173 ? 0.3586 0.4375 0.3591 0.0585  -0.0720 -0.1408 1171 GLU A CB  
8658  C CG  . GLU A 1173 ? 0.3902 0.4806 0.3877 0.0630  -0.0732 -0.1489 1171 GLU A CG  
8659  C CD  . GLU A 1173 ? 0.4191 0.5096 0.4170 0.0647  -0.0721 -0.1514 1171 GLU A CD  
8660  O OE1 . GLU A 1173 ? 0.4295 0.5102 0.4341 0.0631  -0.0731 -0.1513 1171 GLU A OE1 
8661  O OE2 . GLU A 1173 ? 0.4258 0.5265 0.4174 0.0677  -0.0704 -0.1534 1171 GLU A OE2 
8662  N N   . ARG A 1174 ? 0.2674 0.3297 0.2640 0.0503  -0.0644 -0.1191 1172 ARG A N   
8663  C CA  . ARG A 1174 ? 0.2933 0.3459 0.2928 0.0465  -0.0629 -0.1123 1172 ARG A CA  
8664  C C   . ARG A 1174 ? 0.2762 0.3256 0.2727 0.0459  -0.0592 -0.1076 1172 ARG A C   
8665  O O   . ARG A 1174 ? 0.2707 0.3119 0.2720 0.0438  -0.0593 -0.1057 1172 ARG A O   
8666  C CB  . ARG A 1174 ? 0.2786 0.3318 0.2749 0.0447  -0.0613 -0.1065 1172 ARG A CB  
8667  C CG  . ARG A 1174 ? 0.2763 0.3208 0.2747 0.0409  -0.0593 -0.0992 1172 ARG A CG  
8668  C CD  . ARG A 1174 ? 0.3132 0.3499 0.3208 0.0387  -0.0624 -0.1011 1172 ARG A CD  
8669  N NE  . ARG A 1174 ? 0.2966 0.3262 0.3060 0.0351  -0.0605 -0.0941 1172 ARG A NE  
8670  C CZ  . ARG A 1174 ? 0.3257 0.3480 0.3423 0.0326  -0.0621 -0.0934 1172 ARG A CZ  
8671  N NH1 . ARG A 1174 ? 0.3370 0.3572 0.3605 0.0332  -0.0658 -0.0991 1172 ARG A NH1 
8672  N NH2 . ARG A 1174 ? 0.3024 0.3198 0.3198 0.0294  -0.0599 -0.0869 1172 ARG A NH2 
8673  N N   . ILE A 1175 ? 0.2475 0.3036 0.2363 0.0478  -0.0562 -0.1057 1173 ILE A N   
8674  C CA  . ILE A 1175 ? 0.2663 0.3200 0.2522 0.0474  -0.0528 -0.1015 1173 ILE A CA  
8675  C C   . ILE A 1175 ? 0.2541 0.3048 0.2447 0.0485  -0.0544 -0.1066 1173 ILE A C   
8676  O O   . ILE A 1175 ? 0.2641 0.3077 0.2572 0.0467  -0.0533 -0.1034 1173 ILE A O   
8677  C CB  . ILE A 1175 ? 0.2875 0.3501 0.2648 0.0494  -0.0497 -0.0989 1173 ILE A CB  
8678  C CG1 . ILE A 1175 ? 0.2690 0.3329 0.2425 0.0478  -0.0478 -0.0926 1173 ILE A CG1 
8679  C CG2 . ILE A 1175 ? 0.2802 0.3413 0.2551 0.0495  -0.0467 -0.0961 1173 ILE A CG2 
8680  C CD1 . ILE A 1175 ? 0.3007 0.3743 0.2665 0.0497  -0.0455 -0.0901 1173 ILE A CD1 
8681  N N   . ARG A 1176 ? 0.2844 0.3408 0.2769 0.0515  -0.0574 -0.1147 1174 ARG A N   
8682  C CA  . ARG A 1176 ? 0.2927 0.3467 0.2903 0.0528  -0.0593 -0.1202 1174 ARG A CA  
8683  C C   . ARG A 1176 ? 0.2571 0.3002 0.2638 0.0500  -0.0618 -0.1198 1174 ARG A C   
8684  O O   . ARG A 1176 ? 0.2765 0.3137 0.2864 0.0491  -0.0614 -0.1186 1174 ARG A O   
8685  C CB  . ARG A 1176 ? 0.2572 0.3198 0.2558 0.0567  -0.0625 -0.1297 1174 ARG A CB  
8686  C CG  . ARG A 1176 ? 0.3345 0.3972 0.3363 0.0589  -0.0635 -0.1352 1174 ARG A CG  
8687  C CD  . ARG A 1176 ? 0.3373 0.4065 0.3430 0.0624  -0.0677 -0.1457 1174 ARG A CD  
8688  N NE  . ARG A 1176 ? 0.3330 0.4144 0.3317 0.0650  -0.0671 -0.1480 1174 ARG A NE  
8689  C CZ  . ARG A 1176 ? 0.3651 0.4568 0.3572 0.0680  -0.0650 -0.1497 1174 ARG A CZ  
8690  N NH1 . ARG A 1176 ? 0.3450 0.4362 0.3362 0.0688  -0.0629 -0.1491 1174 ARG A NH1 
8691  N NH2 . ARG A 1176 ? 0.3667 0.4699 0.3532 0.0702  -0.0649 -0.1520 1174 ARG A NH2 
8692  N N   . ALA A 1177 ? 0.2784 0.3191 0.2894 0.0485  -0.0645 -0.1204 1175 ALA A N   
8693  C CA  . ALA A 1177 ? 0.2953 0.3264 0.3154 0.0455  -0.0671 -0.1196 1175 ALA A CA  
8694  C C   . ALA A 1177 ? 0.2642 0.2882 0.2833 0.0421  -0.0639 -0.1109 1175 ALA A C   
8695  O O   . ALA A 1177 ? 0.2832 0.3002 0.3080 0.0405  -0.0647 -0.1099 1175 ALA A O   
8696  C CB  . ALA A 1177 ? 0.3033 0.3341 0.3274 0.0444  -0.0702 -0.1212 1175 ALA A CB  
8697  N N   . VAL A 1178 ? 0.2663 0.2922 0.2785 0.0410  -0.0602 -0.1047 1176 VAL A N   
8698  C CA  . VAL A 1178 ? 0.2480 0.2679 0.2590 0.0379  -0.0570 -0.0968 1176 VAL A CA  
8699  C C   . VAL A 1178 ? 0.2643 0.2829 0.2735 0.0386  -0.0549 -0.0957 1176 VAL A C   
8700  O O   . VAL A 1178 ? 0.2754 0.2872 0.2878 0.0363  -0.0542 -0.0921 1176 VAL A O   
8701  C CB  . VAL A 1178 ? 0.2445 0.2673 0.2488 0.0369  -0.0538 -0.0910 1176 VAL A CB  
8702  C CG1 . VAL A 1178 ? 0.2599 0.2776 0.2624 0.0343  -0.0503 -0.0836 1176 VAL A CG1 
8703  C CG2 . VAL A 1178 ? 0.2501 0.2727 0.2576 0.0355  -0.0560 -0.0913 1176 VAL A CG2 
8704  N N   . ASN A 1179 ? 0.2624 0.2878 0.2664 0.0419  -0.0537 -0.0989 1177 ASN A N   
8705  C CA  . ASN A 1179 ? 0.2561 0.2809 0.2581 0.0428  -0.0516 -0.0980 1177 ASN A CA  
8706  C C   . ASN A 1179 ? 0.2725 0.2915 0.2826 0.0426  -0.0545 -0.1018 1177 ASN A C   
8707  O O   . ASN A 1179 ? 0.2748 0.2888 0.2860 0.0413  -0.0531 -0.0985 1177 ASN A O   
8708  C CB  . ASN A 1179 ? 0.3370 0.3716 0.3328 0.0465  -0.0504 -0.1015 1177 ASN A CB  
8709  C CG  . ASN A 1179 ? 0.3936 0.4296 0.3834 0.0467  -0.0463 -0.0970 1177 ASN A CG  
8710  O OD1 . ASN A 1179 ? 0.4164 0.4465 0.4058 0.0442  -0.0439 -0.0907 1177 ASN A OD1 
8711  N ND2 . ASN A 1179 ? 0.4423 0.4867 0.4278 0.0499  -0.0454 -0.1002 1177 ASN A ND2 
8712  N N   . LYS A 1180 ? 0.2754 0.2948 0.2919 0.0438  -0.0589 -0.1086 1178 LYS A N   
8713  C CA  . LYS A 1180 ? 0.2943 0.3077 0.3200 0.0434  -0.0624 -0.1121 1178 LYS A CA  
8714  C C   . LYS A 1180 ? 0.2744 0.2786 0.3053 0.0391  -0.0626 -0.1059 1178 LYS A C   
8715  O O   . LYS A 1180 ? 0.2847 0.2832 0.3199 0.0380  -0.0629 -0.1043 1178 LYS A O   
8716  C CB  . LYS A 1180 ? 0.3176 0.3334 0.3494 0.0455  -0.0673 -0.1207 1178 LYS A CB  
8717  C CG  . LYS A 1180 ? 0.3335 0.3589 0.3611 0.0500  -0.0675 -0.1278 1178 LYS A CG  
8718  C CD  . LYS A 1180 ? 0.3245 0.3539 0.3570 0.0521  -0.0721 -0.1362 1178 LYS A CD  
8719  C CE  . LYS A 1180 ? 0.4445 0.4667 0.4892 0.0515  -0.0772 -0.1408 1178 LYS A CE  
8720  N NZ  . LYS A 1180 ? 0.4945 0.5203 0.5446 0.0536  -0.0821 -0.1494 1178 LYS A NZ  
8721  N N   . ALA A 1181 ? 0.2671 0.2702 0.2978 0.0368  -0.0625 -0.1023 1179 ALA A N   
8722  C CA  . ALA A 1181 ? 0.2867 0.2824 0.3220 0.0326  -0.0626 -0.0962 1179 ALA A CA  
8723  C C   . ALA A 1181 ? 0.2851 0.2785 0.3155 0.0310  -0.0582 -0.0893 1179 ALA A C   
8724  O O   . ALA A 1181 ? 0.2830 0.2702 0.3179 0.0285  -0.0585 -0.0857 1179 ALA A O   
8725  C CB  . ALA A 1181 ? 0.2852 0.2815 0.3206 0.0307  -0.0630 -0.0939 1179 ALA A CB  
8726  N N   . ILE A 1182 ? 0.2494 0.2478 0.2708 0.0325  -0.0544 -0.0873 1180 ILE A N   
8727  C CA  . ILE A 1182 ? 0.2713 0.2677 0.2881 0.0311  -0.0503 -0.0810 1180 ILE A CA  
8728  C C   . ILE A 1182 ? 0.2827 0.2768 0.3014 0.0321  -0.0504 -0.0825 1180 ILE A C   
8729  O O   . ILE A 1182 ? 0.2653 0.2544 0.2854 0.0299  -0.0491 -0.0779 1180 ILE A O   
8730  C CB  . ILE A 1182 ? 0.2771 0.2793 0.2846 0.0324  -0.0466 -0.0785 1180 ILE A CB  
8731  C CG1 . ILE A 1182 ? 0.2792 0.2821 0.2855 0.0306  -0.0462 -0.0754 1180 ILE A CG1 
8732  C CG2 . ILE A 1182 ? 0.2880 0.2888 0.2911 0.0317  -0.0427 -0.0735 1180 ILE A CG2 
8733  C CD1 . ILE A 1182 ? 0.3051 0.3140 0.3033 0.0319  -0.0431 -0.0730 1180 ILE A CD1 
8734  N N   . ALA A 1183 ? 0.2821 0.2802 0.3010 0.0355  -0.0519 -0.0890 1181 ALA A N   
8735  C CA  . ALA A 1183 ? 0.2756 0.2720 0.2967 0.0367  -0.0521 -0.0910 1181 ALA A CA  
8736  C C   . ALA A 1183 ? 0.2658 0.2544 0.2964 0.0345  -0.0553 -0.0907 1181 ALA A C   
8737  O O   . ALA A 1183 ? 0.2756 0.2605 0.3080 0.0339  -0.0547 -0.0889 1181 ALA A O   
8738  C CB  . ALA A 1183 ? 0.2626 0.2657 0.2827 0.0409  -0.0535 -0.0988 1181 ALA A CB  
8739  N N   . ALA A 1184 ? 0.2701 0.2562 0.3070 0.0329  -0.0587 -0.0919 1182 ALA A N   
8740  C CA  . ALA A 1184 ? 0.2755 0.2546 0.3224 0.0306  -0.0621 -0.0912 1182 ALA A CA  
8741  C C   . ALA A 1184 ? 0.2948 0.2688 0.3418 0.0265  -0.0600 -0.0827 1182 ALA A C   
8742  O O   . ALA A 1184 ? 0.2879 0.2562 0.3426 0.0243  -0.0624 -0.0809 1182 ALA A O   
8743  C CB  . ALA A 1184 ? 0.3006 0.2790 0.3550 0.0304  -0.0668 -0.0955 1182 ALA A CB  
8744  N N   . LEU A 1185 ? 0.2660 0.2422 0.3051 0.0255  -0.0559 -0.0777 1183 LEU A N   
8745  C CA  . LEU A 1185 ? 0.2853 0.2577 0.3244 0.0218  -0.0539 -0.0701 1183 LEU A CA  
8746  C C   . LEU A 1185 ? 0.2686 0.2376 0.3085 0.0214  -0.0528 -0.0678 1183 LEU A C   
8747  O O   . LEU A 1185 ? 0.2893 0.2606 0.3252 0.0240  -0.0512 -0.0702 1183 LEU A O   
8748  C CB  . LEU A 1185 ? 0.2709 0.2467 0.3014 0.0213  -0.0497 -0.0658 1183 LEU A CB  
8749  C CG  . LEU A 1185 ? 0.2787 0.2579 0.3080 0.0215  -0.0505 -0.0673 1183 LEU A CG  
8750  C CD1 . LEU A 1185 ? 0.2794 0.2619 0.3006 0.0212  -0.0463 -0.0631 1183 LEU A CD1 
8751  C CD2 . LEU A 1185 ? 0.3105 0.2863 0.3477 0.0186  -0.0536 -0.0662 1183 LEU A CD2 
8752  N N   . PRO A 1186 ? 0.2892 0.2533 0.3341 0.0181  -0.0535 -0.0630 1184 PRO A N   
8753  C CA  . PRO A 1186 ? 0.2901 0.2512 0.3358 0.0176  -0.0525 -0.0605 1184 PRO A CA  
8754  C C   . PRO A 1186 ? 0.2503 0.2138 0.2868 0.0178  -0.0474 -0.0567 1184 PRO A C   
8755  O O   . PRO A 1186 ? 0.3017 0.2678 0.3325 0.0172  -0.0448 -0.0540 1184 PRO A O   
8756  C CB  . PRO A 1186 ? 0.3308 0.2872 0.3836 0.0135  -0.0543 -0.0553 1184 PRO A CB  
8757  C CG  . PRO A 1186 ? 0.3670 0.3251 0.4188 0.0116  -0.0539 -0.0530 1184 PRO A CG  
8758  C CD  . PRO A 1186 ? 0.3134 0.2753 0.3634 0.0146  -0.0550 -0.0592 1184 PRO A CD  
8759  N N   . GLY A 1187 ? 0.2577 0.2203 0.2931 0.0189  -0.0463 -0.0567 1185 GLY A N   
8760  C CA  . GLY A 1187 ? 0.2983 0.2620 0.3265 0.0186  -0.0420 -0.0524 1185 GLY A CA  
8761  C C   . GLY A 1187 ? 0.2572 0.2261 0.2779 0.0219  -0.0394 -0.0551 1185 GLY A C   
8762  O O   . GLY A 1187 ? 0.2972 0.2681 0.3184 0.0248  -0.0406 -0.0604 1185 GLY A O   
8763  N N   . PRO A 1188 ? 0.2581 0.2295 0.2720 0.0214  -0.0359 -0.0515 1186 PRO A N   
8764  C CA  . PRO A 1188 ? 0.2451 0.2211 0.2519 0.0240  -0.0330 -0.0525 1186 PRO A CA  
8765  C C   . PRO A 1188 ? 0.2397 0.2207 0.2446 0.0268  -0.0341 -0.0576 1186 PRO A C   
8766  O O   . PRO A 1188 ? 0.2549 0.2364 0.2621 0.0263  -0.0361 -0.0591 1186 PRO A O   
8767  C CB  . PRO A 1188 ? 0.2723 0.2489 0.2739 0.0222  -0.0295 -0.0468 1186 PRO A CB  
8768  C CG  . PRO A 1188 ? 0.2780 0.2525 0.2829 0.0196  -0.0309 -0.0449 1186 PRO A CG  
8769  C CD  . PRO A 1188 ? 0.2689 0.2392 0.2818 0.0184  -0.0344 -0.0462 1186 PRO A CD  
8770  N N   . LEU A 1189 ? 0.2533 0.2387 0.2542 0.0296  -0.0328 -0.0601 1187 LEU A N   
8771  C CA  . LEU A 1189 ? 0.2481 0.2400 0.2456 0.0323  -0.0331 -0.0640 1187 LEU A CA  
8772  C C   . LEU A 1189 ? 0.2533 0.2475 0.2455 0.0313  -0.0306 -0.0598 1187 LEU A C   
8773  O O   . LEU A 1189 ? 0.3021 0.2951 0.2909 0.0299  -0.0277 -0.0546 1187 LEU A O   
8774  C CB  . LEU A 1189 ? 0.2628 0.2597 0.2567 0.0354  -0.0318 -0.0668 1187 LEU A CB  
8775  C CG  . LEU A 1189 ? 0.2719 0.2689 0.2708 0.0376  -0.0347 -0.0732 1187 LEU A CG  
8776  C CD1 . LEU A 1189 ? 0.2849 0.2751 0.2892 0.0359  -0.0355 -0.0715 1187 LEU A CD1 
8777  C CD2 . LEU A 1189 ? 0.3465 0.3510 0.3408 0.0410  -0.0333 -0.0764 1187 LEU A CD2 
8778  N N   . LEU A 1190 ? 0.2586 0.2558 0.2505 0.0319  -0.0320 -0.0620 1188 LEU A N   
8779  C CA  . LEU A 1190 ? 0.2705 0.2700 0.2581 0.0310  -0.0301 -0.0583 1188 LEU A CA  
8780  C C   . LEU A 1190 ? 0.2335 0.2407 0.2153 0.0338  -0.0288 -0.0597 1188 LEU A C   
8781  O O   . LEU A 1190 ? 0.2713 0.2829 0.2535 0.0363  -0.0307 -0.0651 1188 LEU A O   
8782  C CB  . LEU A 1190 ? 0.2858 0.2839 0.2768 0.0296  -0.0324 -0.0590 1188 LEU A CB  
8783  C CG  . LEU A 1190 ? 0.2767 0.2682 0.2739 0.0265  -0.0339 -0.0571 1188 LEU A CG  
8784  C CD1 . LEU A 1190 ? 0.3621 0.3535 0.3614 0.0250  -0.0354 -0.0567 1188 LEU A CD1 
8785  C CD2 . LEU A 1190 ? 0.3028 0.2910 0.2984 0.0244  -0.0310 -0.0512 1188 LEU A CD2 
8786  N N   . LEU A 1191 ? 0.2471 0.2562 0.2239 0.0334  -0.0257 -0.0550 1189 LEU A N   
8787  C CA  . LEU A 1191 ? 0.2337 0.2503 0.2052 0.0356  -0.0246 -0.0551 1189 LEU A CA  
8788  C C   . LEU A 1191 ? 0.2448 0.2634 0.2164 0.0353  -0.0260 -0.0557 1189 LEU A C   
8789  O O   . LEU A 1191 ? 0.2523 0.2683 0.2239 0.0333  -0.0251 -0.0516 1189 LEU A O   
8790  C CB  . LEU A 1191 ? 0.2421 0.2595 0.2094 0.0350  -0.0211 -0.0494 1189 LEU A CB  
8791  C CG  . LEU A 1191 ? 0.2435 0.2689 0.2055 0.0373  -0.0196 -0.0488 1189 LEU A CG  
8792  C CD1 . LEU A 1191 ? 0.2554 0.2799 0.2150 0.0364  -0.0165 -0.0432 1189 LEU A CD1 
8793  C CD2 . LEU A 1191 ? 0.2497 0.2799 0.2096 0.0378  -0.0202 -0.0483 1189 LEU A CD2 
8794  N N   . VAL A 1192 ? 0.2487 0.2721 0.2206 0.0374  -0.0283 -0.0609 1190 VAL A N   
8795  C CA  . VAL A 1192 ? 0.2318 0.2574 0.2042 0.0374  -0.0302 -0.0625 1190 VAL A CA  
8796  C C   . VAL A 1192 ? 0.2337 0.2677 0.2004 0.0393  -0.0289 -0.0615 1190 VAL A C   
8797  O O   . VAL A 1192 ? 0.2668 0.3069 0.2304 0.0417  -0.0283 -0.0634 1190 VAL A O   
8798  C CB  . VAL A 1192 ? 0.2777 0.3037 0.2547 0.0387  -0.0339 -0.0695 1190 VAL A CB  
8799  C CG1 . VAL A 1192 ? 0.2846 0.3132 0.2624 0.0387  -0.0360 -0.0714 1190 VAL A CG1 
8800  C CG2 . VAL A 1192 ? 0.2816 0.2997 0.2651 0.0369  -0.0355 -0.0703 1190 VAL A CG2 
8801  N N   . GLN A 1193 ? 0.2288 0.2636 0.1944 0.0383  -0.0286 -0.0585 1191 GLN A N   
8802  C CA  . GLN A 1193 ? 0.2113 0.2542 0.1723 0.0400  -0.0282 -0.0577 1191 GLN A CA  
8803  C C   . GLN A 1193 ? 0.2209 0.2654 0.1837 0.0401  -0.0309 -0.0608 1191 GLN A C   
8804  O O   . GLN A 1193 ? 0.2336 0.2727 0.2000 0.0380  -0.0317 -0.0597 1191 GLN A O   
8805  C CB  . GLN A 1193 ? 0.2153 0.2579 0.1735 0.0387  -0.0254 -0.0507 1191 GLN A CB  
8806  C CG  . GLN A 1193 ? 0.2544 0.2953 0.2109 0.0384  -0.0227 -0.0472 1191 GLN A CG  
8807  C CD  . GLN A 1193 ? 0.2682 0.3105 0.2220 0.0377  -0.0204 -0.0408 1191 GLN A CD  
8808  O OE1 . GLN A 1193 ? 0.2742 0.3237 0.2245 0.0391  -0.0199 -0.0394 1191 GLN A OE1 
8809  N NE2 . GLN A 1193 ? 0.2516 0.2872 0.2073 0.0354  -0.0191 -0.0370 1191 GLN A NE2 
8810  N N   . ALA A 1194 ? 0.2128 0.2655 0.1733 0.0426  -0.0322 -0.0646 1192 ALA A N   
8811  C CA  . ALA A 1194 ? 0.2050 0.2600 0.1672 0.0430  -0.0350 -0.0682 1192 ALA A CA  
8812  C C   . ALA A 1194 ? 0.2270 0.2907 0.1842 0.0444  -0.0344 -0.0662 1192 ALA A C   
8813  O O   . ALA A 1194 ? 0.2519 0.3219 0.2046 0.0459  -0.0326 -0.0642 1192 ALA A O   
8814  C CB  . ALA A 1194 ? 0.2410 0.2982 0.2060 0.0450  -0.0380 -0.0761 1192 ALA A CB  
8815  N N   . ALA A 1195 ? 0.2206 0.2850 0.1791 0.0439  -0.0362 -0.0668 1193 ALA A N   
8816  C CA  . ALA A 1195 ? 0.2323 0.3051 0.1867 0.0452  -0.0362 -0.0651 1193 ALA A CA  
8817  C C   . ALA A 1195 ? 0.2412 0.3151 0.1982 0.0453  -0.0394 -0.0692 1193 ALA A C   
8818  O O   . ALA A 1195 ? 0.2532 0.3201 0.2153 0.0435  -0.0408 -0.0706 1193 ALA A O   
8819  C CB  . ALA A 1195 ? 0.2475 0.3185 0.2000 0.0435  -0.0337 -0.0573 1193 ALA A CB  
8820  N N   . SER A 1196 ? 0.2464 0.3298 0.2001 0.0473  -0.0404 -0.0709 1194 SER A N   
8821  C CA  . SER A 1196 ? 0.2599 0.3449 0.2158 0.0474  -0.0433 -0.0740 1194 SER A CA  
8822  C C   . SER A 1196 ? 0.2424 0.3250 0.1983 0.0454  -0.0424 -0.0678 1194 SER A C   
8823  O O   . SER A 1196 ? 0.2480 0.3296 0.2016 0.0445  -0.0397 -0.0615 1194 SER A O   
8824  C CB  . SER A 1196 ? 0.2855 0.3822 0.2377 0.0504  -0.0449 -0.0780 1194 SER A CB  
8825  O OG  . SER A 1196 ? 0.2780 0.3815 0.2248 0.0509  -0.0427 -0.0722 1194 SER A OG  
8826  N N   . SER A 1197 ? 0.2619 0.3434 0.2209 0.0447  -0.0448 -0.0699 1195 SER A N   
8827  C CA  . SER A 1197 ? 0.2684 0.3486 0.2275 0.0431  -0.0441 -0.0646 1195 SER A CA  
8828  C C   . SER A 1197 ? 0.2481 0.3369 0.2019 0.0446  -0.0429 -0.0605 1195 SER A C   
8829  O O   . SER A 1197 ? 0.2852 0.3724 0.2381 0.0434  -0.0410 -0.0541 1195 SER A O   
8830  C CB  . SER A 1197 ? 0.2751 0.3544 0.2383 0.0425  -0.0472 -0.0680 1195 SER A CB  
8831  O OG  . SER A 1197 ? 0.2857 0.3573 0.2546 0.0409  -0.0485 -0.0711 1195 SER A OG  
8832  N N   . GLY A 1198 ? 0.2610 0.3593 0.2114 0.0471  -0.0442 -0.0640 1196 GLY A N   
8833  C CA  . GLY A 1198 ? 0.2853 0.3928 0.2306 0.0484  -0.0432 -0.0598 1196 GLY A CA  
8834  C C   . GLY A 1198 ? 0.3069 0.4143 0.2493 0.0482  -0.0399 -0.0542 1196 GLY A C   
8835  O O   . GLY A 1198 ? 0.3034 0.4135 0.2438 0.0478  -0.0385 -0.0478 1196 GLY A O   
8836  N N   . GLU A 1199 ? 0.2541 0.3584 0.1968 0.0484  -0.0389 -0.0565 1197 GLU A N   
8837  C CA  . GLU A 1199 ? 0.2809 0.3842 0.2214 0.0481  -0.0358 -0.0513 1197 GLU A CA  
8838  C C   . GLU A 1199 ? 0.2884 0.3830 0.2314 0.0455  -0.0341 -0.0451 1197 GLU A C   
8839  O O   . GLU A 1199 ? 0.2821 0.3780 0.2232 0.0451  -0.0321 -0.0389 1197 GLU A O   
8840  C CB  . GLU A 1199 ? 0.2603 0.3612 0.2013 0.0487  -0.0353 -0.0556 1197 GLU A CB  
8841  C CG  . GLU A 1199 ? 0.3748 0.4758 0.3134 0.0487  -0.0324 -0.0513 1197 GLU A CG  
8842  C CD  . GLU A 1199 ? 0.5012 0.6007 0.4405 0.0496  -0.0323 -0.0564 1197 GLU A CD  
8843  O OE1 . GLU A 1199 ? 0.4087 0.5080 0.3504 0.0506  -0.0348 -0.0635 1197 GLU A OE1 
8844  O OE2 . GLU A 1199 ? 0.5393 0.6378 0.4773 0.0495  -0.0300 -0.0535 1197 GLU A OE2 
8845  N N   . ILE A 1200 ? 0.2540 0.3400 0.2015 0.0437  -0.0349 -0.0469 1198 ILE A N   
8846  C CA  . ILE A 1200 ? 0.2668 0.3453 0.2168 0.0414  -0.0334 -0.0416 1198 ILE A CA  
8847  C C   . ILE A 1200 ? 0.2973 0.3799 0.2463 0.0413  -0.0335 -0.0368 1198 ILE A C   
8848  O O   . ILE A 1200 ? 0.2876 0.3680 0.2368 0.0404  -0.0317 -0.0310 1198 ILE A O   
8849  C CB  . ILE A 1200 ? 0.2572 0.3273 0.2122 0.0395  -0.0345 -0.0445 1198 ILE A CB  
8850  C CG1 . ILE A 1200 ? 0.2532 0.3185 0.2097 0.0392  -0.0342 -0.0480 1198 ILE A CG1 
8851  C CG2 . ILE A 1200 ? 0.2713 0.3353 0.2289 0.0373  -0.0332 -0.0395 1198 ILE A CG2 
8852  C CD1 . ILE A 1200 ? 0.2751 0.3333 0.2367 0.0375  -0.0358 -0.0511 1198 ILE A CD1 
8853  N N   . ALA A 1201 ? 0.2672 0.3559 0.2154 0.0425  -0.0357 -0.0392 1199 ALA A N   
8854  C CA  . ALA A 1201 ? 0.2901 0.3832 0.2377 0.0425  -0.0361 -0.0346 1199 ALA A CA  
8855  C C   . ALA A 1201 ? 0.3070 0.4075 0.2505 0.0437  -0.0347 -0.0296 1199 ALA A C   
8856  O O   . ALA A 1201 ? 0.3093 0.4102 0.2533 0.0431  -0.0341 -0.0235 1199 ALA A O   
8857  C CB  . ALA A 1201 ? 0.2939 0.3921 0.2417 0.0435  -0.0391 -0.0387 1199 ALA A CB  
8858  N N   . ARG A 1202 ? 0.2643 0.3710 0.2042 0.0454  -0.0345 -0.0320 1200 ARG A N   
8859  C CA  . ARG A 1202 ? 0.2724 0.3879 0.2084 0.0465  -0.0334 -0.0273 1200 ARG A CA  
8860  C C   . ARG A 1202 ? 0.2958 0.4075 0.2318 0.0456  -0.0306 -0.0224 1200 ARG A C   
8861  O O   . ARG A 1202 ? 0.3323 0.4483 0.2670 0.0456  -0.0296 -0.0160 1200 ARG A O   
8862  C CB  . ARG A 1202 ? 0.2879 0.4136 0.2198 0.0490  -0.0344 -0.0322 1200 ARG A CB  
8863  C CG  . ARG A 1202 ? 0.2823 0.4147 0.2135 0.0503  -0.0372 -0.0363 1200 ARG A CG  
8864  C CD  . ARG A 1202 ? 0.3228 0.4668 0.2497 0.0529  -0.0380 -0.0409 1200 ARG A CD  
8865  N NE  . ARG A 1202 ? 0.3425 0.4830 0.2702 0.0535  -0.0379 -0.0473 1200 ARG A NE  
8866  C CZ  . ARG A 1202 ? 0.3691 0.5078 0.2989 0.0543  -0.0402 -0.0553 1200 ARG A CZ  
8867  N NH1 . ARG A 1202 ? 0.3139 0.4552 0.2448 0.0547  -0.0428 -0.0584 1200 ARG A NH1 
8868  N NH2 . ARG A 1202 ? 0.3563 0.4904 0.2878 0.0546  -0.0400 -0.0602 1200 ARG A NH2 
8869  N N   . ASN A 1203 ? 0.2827 0.3866 0.2203 0.0449  -0.0295 -0.0251 1201 ASN A N   
8870  C CA  . ASN A 1203 ? 0.2875 0.3890 0.2245 0.0444  -0.0270 -0.0215 1201 ASN A CA  
8871  C C   . ASN A 1203 ? 0.3412 0.4313 0.2822 0.0421  -0.0258 -0.0197 1201 ASN A C   
8872  O O   . ASN A 1203 ? 0.2984 0.3818 0.2416 0.0414  -0.0261 -0.0241 1201 ASN A O   
8873  C CB  . ASN A 1203 ? 0.3151 0.4192 0.2499 0.0457  -0.0266 -0.0265 1201 ASN A CB  
8874  C CG  . ASN A 1203 ? 0.3603 0.4625 0.2943 0.0453  -0.0241 -0.0230 1201 ASN A CG  
8875  O OD1 . ASN A 1203 ? 0.3457 0.4452 0.2809 0.0440  -0.0226 -0.0166 1201 ASN A OD1 
8876  N ND2 . ASN A 1203 ? 0.3681 0.4718 0.3008 0.0464  -0.0236 -0.0272 1201 ASN A ND2 
8877  N N   . PRO A 1204 ? 0.3319 0.4198 0.2744 0.0410  -0.0246 -0.0132 1202 PRO A N   
8878  C CA  . PRO A 1204 ? 0.3587 0.4364 0.3050 0.0390  -0.0234 -0.0118 1202 PRO A CA  
8879  C C   . PRO A 1204 ? 0.3372 0.4099 0.2836 0.0386  -0.0218 -0.0137 1202 PRO A C   
8880  O O   . PRO A 1204 ? 0.3323 0.3968 0.2816 0.0371  -0.0213 -0.0147 1202 PRO A O   
8881  C CB  . PRO A 1204 ? 0.4270 0.5052 0.3747 0.0385  -0.0226 -0.0046 1202 PRO A CB  
8882  C CG  . PRO A 1204 ? 0.4563 0.5441 0.4017 0.0398  -0.0240 -0.0024 1202 PRO A CG  
8883  C CD  . PRO A 1204 ? 0.3912 0.4860 0.3323 0.0415  -0.0244 -0.0070 1202 PRO A CD  
8884  N N   . ASP A 1205 ? 0.3300 0.4079 0.2731 0.0399  -0.0211 -0.0145 1203 ASP A N   
8885  C CA  . ASP A 1205 ? 0.3053 0.3791 0.2482 0.0397  -0.0197 -0.0165 1203 ASP A CA  
8886  C C   . ASP A 1205 ? 0.3292 0.4039 0.2714 0.0408  -0.0210 -0.0236 1203 ASP A C   
8887  O O   . ASP A 1205 ? 0.3771 0.4519 0.3183 0.0414  -0.0201 -0.0257 1203 ASP A O   
8888  C CB  . ASP A 1205 ? 0.4111 0.4898 0.3516 0.0404  -0.0179 -0.0124 1203 ASP A CB  
8889  C CG  . ASP A 1205 ? 0.4832 0.5607 0.4253 0.0393  -0.0169 -0.0052 1203 ASP A CG  
8890  O OD1 . ASP A 1205 ? 0.4182 0.4887 0.3638 0.0378  -0.0170 -0.0039 1203 ASP A OD1 
8891  O OD2 . ASP A 1205 ? 0.5531 0.6368 0.4934 0.0399  -0.0160 -0.0008 1203 ASP A OD2 
8892  N N   . ALA A 1206 ? 0.2848 0.3605 0.2279 0.0411  -0.0232 -0.0275 1204 ALA A N   
8893  C CA  . ALA A 1206 ? 0.2889 0.3648 0.2324 0.0421  -0.0249 -0.0346 1204 ALA A CA  
8894  C C   . ALA A 1206 ? 0.2946 0.3624 0.2407 0.0410  -0.0241 -0.0366 1204 ALA A C   
8895  O O   . ALA A 1206 ? 0.3323 0.4014 0.2778 0.0422  -0.0245 -0.0410 1204 ALA A O   
8896  C CB  . ALA A 1206 ? 0.2930 0.3680 0.2389 0.0418  -0.0274 -0.0377 1204 ALA A CB  
8897  N N   . TYR A 1207 ? 0.2707 0.3304 0.2197 0.0388  -0.0231 -0.0336 1205 TYR A N   
8898  C CA  . TYR A 1207 ? 0.2878 0.3401 0.2388 0.0376  -0.0220 -0.0341 1205 TYR A CA  
8899  C C   . TYR A 1207 ? 0.2885 0.3398 0.2384 0.0370  -0.0194 -0.0285 1205 TYR A C   
8900  O O   . TYR A 1207 ? 0.3715 0.4214 0.3220 0.0359  -0.0186 -0.0239 1205 TYR A O   
8901  C CB  . TYR A 1207 ? 0.2747 0.3193 0.2300 0.0354  -0.0228 -0.0348 1205 TYR A CB  
8902  C CG  . TYR A 1207 ? 0.2285 0.2736 0.1859 0.0357  -0.0256 -0.0399 1205 TYR A CG  
8903  C CD1 . TYR A 1207 ? 0.2660 0.3120 0.2241 0.0369  -0.0271 -0.0454 1205 TYR A CD1 
8904  C CD2 . TYR A 1207 ? 0.2576 0.3023 0.2168 0.0348  -0.0268 -0.0395 1205 TYR A CD2 
8905  C CE1 . TYR A 1207 ? 0.2388 0.2850 0.1996 0.0371  -0.0299 -0.0503 1205 TYR A CE1 
8906  C CE2 . TYR A 1207 ? 0.2606 0.3058 0.2221 0.0350  -0.0295 -0.0442 1205 TYR A CE2 
8907  C CZ  . TYR A 1207 ? 0.2412 0.2869 0.2036 0.0361  -0.0311 -0.0496 1205 TYR A CZ  
8908  O OH  . TYR A 1207 ? 0.2714 0.3174 0.2368 0.0362  -0.0340 -0.0543 1205 TYR A OH  
8909  N N   . CYS A 1208 ? 0.2632 0.3150 0.2116 0.0377  -0.0182 -0.0290 1206 CYS A N   
8910  C CA  . CYS A 1208 ? 0.2830 0.3347 0.2302 0.0373  -0.0158 -0.0239 1206 CYS A CA  
8911  C C   . CYS A 1208 ? 0.2665 0.3092 0.2168 0.0351  -0.0147 -0.0223 1206 CYS A C   
8912  O O   . CYS A 1208 ? 0.2472 0.2852 0.1993 0.0346  -0.0150 -0.0255 1206 CYS A O   
8913  C CB  . CYS A 1208 ? 0.3032 0.3602 0.2477 0.0390  -0.0151 -0.0253 1206 CYS A CB  
8914  S SG  . CYS A 1208 ? 0.3520 0.4093 0.2954 0.0385  -0.0123 -0.0192 1206 CYS A SG  
8915  N N   . LEU A 1209 ? 0.2340 0.2747 0.1851 0.0340  -0.0135 -0.0172 1207 LEU A N   
8916  C CA  . LEU A 1209 ? 0.2263 0.2593 0.1803 0.0320  -0.0124 -0.0157 1207 LEU A CA  
8917  C C   . LEU A 1209 ? 0.2329 0.2638 0.1865 0.0319  -0.0108 -0.0152 1207 LEU A C   
8918  O O   . LEU A 1209 ? 0.2495 0.2742 0.2053 0.0304  -0.0101 -0.0152 1207 LEU A O   
8919  C CB  . LEU A 1209 ? 0.2340 0.2660 0.1896 0.0311  -0.0118 -0.0111 1207 LEU A CB  
8920  C CG  . LEU A 1209 ? 0.2437 0.2776 0.2002 0.0312  -0.0134 -0.0113 1207 LEU A CG  
8921  C CD1 . LEU A 1209 ? 0.2615 0.2935 0.2204 0.0303  -0.0128 -0.0070 1207 LEU A CD1 
8922  C CD2 . LEU A 1209 ? 0.2712 0.3015 0.2296 0.0303  -0.0147 -0.0156 1207 LEU A CD2 
8923  N N   . ASN A 1210 ? 0.2465 0.2827 0.1972 0.0335  -0.0101 -0.0148 1208 ASN A N   
8924  C CA  . ASN A 1210 ? 0.2596 0.2943 0.2099 0.0335  -0.0087 -0.0146 1208 ASN A CA  
8925  C C   . ASN A 1210 ? 0.2456 0.2753 0.1976 0.0330  -0.0094 -0.0191 1208 ASN A C   
8926  O O   . ASN A 1210 ? 0.2738 0.2989 0.2269 0.0321  -0.0083 -0.0185 1208 ASN A O   
8927  C CB  . ASN A 1210 ? 0.2962 0.3388 0.2433 0.0355  -0.0083 -0.0147 1208 ASN A CB  
8928  C CG  . ASN A 1210 ? 0.3166 0.3647 0.2622 0.0358  -0.0073 -0.0092 1208 ASN A CG  
8929  O OD1 . ASN A 1210 ? 0.4235 0.4699 0.3707 0.0348  -0.0074 -0.0057 1208 ASN A OD1 
8930  N ND2 . ASN A 1210 ? 0.4221 0.4771 0.3650 0.0373  -0.0066 -0.0084 1208 ASN A ND2 
8931  N N   . TRP A 1211 ? 0.2340 0.2647 0.1865 0.0337  -0.0114 -0.0237 1209 TRP A N   
8932  C CA  . TRP A 1211 ? 0.2523 0.2789 0.2069 0.0334  -0.0125 -0.0280 1209 TRP A CA  
8933  C C   . TRP A 1211 ? 0.2485 0.2684 0.2067 0.0312  -0.0133 -0.0283 1209 TRP A C   
8934  O O   . TRP A 1211 ? 0.2863 0.3027 0.2470 0.0307  -0.0146 -0.0315 1209 TRP A O   
8935  C CB  . TRP A 1211 ? 0.2502 0.2820 0.2040 0.0355  -0.0144 -0.0334 1209 TRP A CB  
8936  C CG  . TRP A 1211 ? 0.2597 0.3001 0.2096 0.0377  -0.0137 -0.0328 1209 TRP A CG  
8937  C CD1 . TRP A 1211 ? 0.2683 0.3160 0.2160 0.0393  -0.0149 -0.0343 1209 TRP A CD1 
8938  C CD2 . TRP A 1211 ? 0.2557 0.2991 0.2033 0.0384  -0.0117 -0.0301 1209 TRP A CD2 
8939  N NE1 . TRP A 1211 ? 0.2941 0.3495 0.2383 0.0409  -0.0137 -0.0326 1209 TRP A NE1 
8940  C CE2 . TRP A 1211 ? 0.2551 0.3080 0.1993 0.0404  -0.0117 -0.0300 1209 TRP A CE2 
8941  C CE3 . TRP A 1211 ? 0.2699 0.3093 0.2182 0.0375  -0.0099 -0.0278 1209 TRP A CE3 
8942  C CZ2 . TRP A 1211 ? 0.2860 0.3445 0.2276 0.0414  -0.0099 -0.0273 1209 TRP A CZ2 
8943  C CZ3 . TRP A 1211 ? 0.2674 0.3119 0.2131 0.0386  -0.0082 -0.0254 1209 TRP A CZ3 
8944  C CH2 . TRP A 1211 ? 0.2799 0.3339 0.2224 0.0404  -0.0082 -0.0251 1209 TRP A CH2 
8945  N N   . LEU A 1212 ? 0.2211 0.2396 0.1799 0.0299  -0.0127 -0.0248 1210 LEU A N   
8946  C CA  . LEU A 1212 ? 0.2339 0.2471 0.1959 0.0278  -0.0132 -0.0246 1210 LEU A CA  
8947  C C   . LEU A 1212 ? 0.2026 0.2113 0.1657 0.0261  -0.0113 -0.0212 1210 LEU A C   
8948  O O   . LEU A 1212 ? 0.2173 0.2223 0.1829 0.0243  -0.0114 -0.0206 1210 LEU A O   
8949  C CB  . LEU A 1212 ? 0.2121 0.2275 0.1745 0.0277  -0.0141 -0.0240 1210 LEU A CB  
8950  C CG  . LEU A 1212 ? 0.2292 0.2475 0.1917 0.0288  -0.0165 -0.0283 1210 LEU A CG  
8951  C CD1 . LEU A 1212 ? 0.2385 0.2606 0.2003 0.0292  -0.0173 -0.0273 1210 LEU A CD1 
8952  C CD2 . LEU A 1212 ? 0.2668 0.2805 0.2332 0.0274  -0.0181 -0.0313 1210 LEU A CD2 
8953  N N   . VAL A 1213 ? 0.2227 0.2323 0.1840 0.0267  -0.0096 -0.0189 1211 VAL A N   
8954  C CA  . VAL A 1213 ? 0.2335 0.2391 0.1959 0.0254  -0.0079 -0.0162 1211 VAL A CA  
8955  C C   . VAL A 1213 ? 0.2230 0.2269 0.1851 0.0256  -0.0075 -0.0176 1211 VAL A C   
8956  O O   . VAL A 1213 ? 0.2367 0.2434 0.1975 0.0271  -0.0083 -0.0203 1211 VAL A O   
8957  C CB  . VAL A 1213 ? 0.2252 0.2324 0.1866 0.0256  -0.0064 -0.0120 1211 VAL A CB  
8958  C CG1 . VAL A 1213 ? 0.2527 0.2605 0.2154 0.0251  -0.0068 -0.0104 1211 VAL A CG1 
8959  C CG2 . VAL A 1213 ? 0.2431 0.2556 0.2017 0.0275  -0.0059 -0.0112 1211 VAL A CG2 
8960  N N   . GLU A 1214 ? 0.2226 0.2223 0.1862 0.0241  -0.0065 -0.0161 1212 GLU A N   
8961  C CA  . GLU A 1214 ? 0.2556 0.2531 0.2194 0.0240  -0.0061 -0.0170 1212 GLU A CA  
8962  C C   . GLU A 1214 ? 0.2298 0.2272 0.1927 0.0240  -0.0040 -0.0136 1212 GLU A C   
8963  O O   . GLU A 1214 ? 0.2188 0.2145 0.1826 0.0228  -0.0031 -0.0110 1212 GLU A O   
8964  C CB  . GLU A 1214 ? 0.3082 0.3010 0.2751 0.0220  -0.0068 -0.0177 1212 GLU A CB  
8965  C CG  . GLU A 1214 ? 0.4043 0.3944 0.3723 0.0217  -0.0068 -0.0187 1212 GLU A CG  
8966  C CD  . GLU A 1214 ? 0.4324 0.4187 0.4038 0.0196  -0.0080 -0.0193 1212 GLU A CD  
8967  O OE1 . GLU A 1214 ? 0.4446 0.4309 0.4177 0.0197  -0.0101 -0.0219 1212 GLU A OE1 
8968  O OE2 . GLU A 1214 ? 0.4643 0.4480 0.4367 0.0179  -0.0070 -0.0170 1212 GLU A OE2 
8969  N N   . GLU A 1215 ? 0.2324 0.2318 0.1936 0.0253  -0.0034 -0.0139 1213 GLU A N   
8970  C CA  . GLU A 1215 ? 0.2037 0.2029 0.1644 0.0252  -0.0016 -0.0108 1213 GLU A CA  
8971  C C   . GLU A 1215 ? 0.2021 0.1964 0.1645 0.0237  -0.0011 -0.0108 1213 GLU A C   
8972  O O   . GLU A 1215 ? 0.2233 0.2159 0.1867 0.0236  -0.0020 -0.0134 1213 GLU A O   
8973  C CB  . GLU A 1215 ? 0.2121 0.2160 0.1704 0.0271  -0.0011 -0.0110 1213 GLU A CB  
8974  C CG  . GLU A 1215 ? 0.2283 0.2383 0.1846 0.0286  -0.0014 -0.0106 1213 GLU A CG  
8975  C CD  . GLU A 1215 ? 0.2295 0.2451 0.1835 0.0306  -0.0013 -0.0121 1213 GLU A CD  
8976  O OE1 . GLU A 1215 ? 0.2511 0.2677 0.2050 0.0316  -0.0025 -0.0165 1213 GLU A OE1 
8977  O OE2 . GLU A 1215 ? 0.2491 0.2683 0.2017 0.0312  0.0001  -0.0090 1213 GLU A OE2 
8978  N N   . VAL A 1216 ? 0.2098 0.2022 0.1730 0.0227  0.0002  -0.0078 1214 VAL A N   
8979  C CA  . VAL A 1216 ? 0.2263 0.2149 0.1908 0.0214  0.0009  -0.0074 1214 VAL A CA  
8980  C C   . VAL A 1216 ? 0.2281 0.2175 0.1921 0.0218  0.0025  -0.0047 1214 VAL A C   
8981  O O   . VAL A 1216 ? 0.2346 0.2252 0.1987 0.0218  0.0031  -0.0022 1214 VAL A O   
8982  C CB  . VAL A 1216 ? 0.2130 0.1983 0.1796 0.0194  0.0007  -0.0069 1214 VAL A CB  
8983  C CG1 . VAL A 1216 ? 0.2322 0.2145 0.2000 0.0182  0.0014  -0.0062 1214 VAL A CG1 
8984  C CG2 . VAL A 1216 ? 0.2523 0.2371 0.2200 0.0189  -0.0009 -0.0093 1214 VAL A CG2 
8985  N N   . SER A 1217 ? 0.2090 0.1976 0.1728 0.0220  0.0029  -0.0051 1215 SER A N   
8986  C CA  . SER A 1217 ? 0.2179 0.2068 0.1816 0.0221  0.0044  -0.0026 1215 SER A CA  
8987  C C   . SER A 1217 ? 0.2136 0.1981 0.1790 0.0204  0.0047  -0.0022 1215 SER A C   
8988  O O   . SER A 1217 ? 0.2153 0.1975 0.1815 0.0197  0.0039  -0.0041 1215 SER A O   
8989  C CB  . SER A 1217 ? 0.2375 0.2292 0.1998 0.0237  0.0046  -0.0036 1215 SER A CB  
8990  O OG  . SER A 1217 ? 0.2620 0.2530 0.2247 0.0234  0.0059  -0.0017 1215 SER A OG  
8991  N N   . ALA A 1218 ? 0.2008 0.1846 0.1672 0.0198  0.0058  0.0003  1216 ALA A N   
8992  C CA  . ALA A 1218 ? 0.2079 0.1884 0.1759 0.0183  0.0062  0.0007  1216 ALA A CA  
8993  C C   . ALA A 1218 ? 0.2171 0.1981 0.1855 0.0186  0.0074  0.0029  1216 ALA A C   
8994  O O   . ALA A 1218 ? 0.2430 0.2257 0.2118 0.0191  0.0078  0.0051  1216 ALA A O   
8995  C CB  . ALA A 1218 ? 0.2183 0.1974 0.1879 0.0170  0.0060  0.0010  1216 ALA A CB  
8996  N N   . SER A 1219 ? 0.2041 0.1836 0.1726 0.0183  0.0077  0.0026  1217 SER A N   
8997  C CA  . SER A 1219 ? 0.2225 0.2022 0.1916 0.0185  0.0087  0.0045  1217 SER A CA  
8998  C C   . SER A 1219 ? 0.2033 0.1799 0.1740 0.0169  0.0089  0.0048  1217 SER A C   
8999  O O   . SER A 1219 ? 0.2143 0.1890 0.1851 0.0162  0.0085  0.0034  1217 SER A O   
9000  C CB  . SER A 1219 ? 0.2432 0.2246 0.2111 0.0197  0.0090  0.0038  1217 SER A CB  
9001  O OG  . SER A 1219 ? 0.2263 0.2082 0.1950 0.0197  0.0100  0.0059  1217 SER A OG  
9002  N N   . ILE A 1220 ? 0.2132 0.1897 0.1857 0.0165  0.0095  0.0065  1218 ILE A N   
9003  C CA  . ILE A 1220 ? 0.2099 0.1842 0.1841 0.0151  0.0096  0.0065  1218 ILE A CA  
9004  C C   . ILE A 1220 ? 0.2098 0.1839 0.1851 0.0153  0.0103  0.0082  1218 ILE A C   
9005  O O   . ILE A 1220 ? 0.2230 0.1985 0.1994 0.0159  0.0107  0.0101  1218 ILE A O   
9006  C CB  . ILE A 1220 ? 0.2456 0.2199 0.2217 0.0146  0.0093  0.0066  1218 ILE A CB  
9007  C CG1 . ILE A 1220 ? 0.2772 0.2519 0.2522 0.0146  0.0086  0.0052  1218 ILE A CG1 
9008  C CG2 . ILE A 1220 ? 0.2638 0.2366 0.2416 0.0134  0.0094  0.0061  1218 ILE A CG2 
9009  C CD1 . ILE A 1220 ? 0.4108 0.3862 0.3876 0.0145  0.0083  0.0052  1218 ILE A CD1 
9010  N N   . ASN A 1221 ? 0.2132 0.1859 0.1886 0.0146  0.0105  0.0076  1219 ASN A N   
9011  C CA  . ASN A 1221 ? 0.2230 0.1954 0.1997 0.0145  0.0111  0.0090  1219 ASN A CA  
9012  C C   . ASN A 1221 ? 0.2069 0.1784 0.1861 0.0135  0.0110  0.0093  1219 ASN A C   
9013  O O   . ASN A 1221 ? 0.2737 0.2442 0.2533 0.0125  0.0108  0.0081  1219 ASN A O   
9014  C CB  . ASN A 1221 ? 0.2353 0.2065 0.2113 0.0141  0.0111  0.0082  1219 ASN A CB  
9015  C CG  . ASN A 1221 ? 0.2393 0.2101 0.2168 0.0138  0.0116  0.0094  1219 ASN A CG  
9016  O OD1 . ASN A 1221 ? 0.2285 0.2001 0.2076 0.0141  0.0121  0.0111  1219 ASN A OD1 
9017  N ND2 . ASN A 1221 ? 0.2738 0.2434 0.2511 0.0132  0.0115  0.0088  1219 ASN A ND2 
9018  N N   . THR A 1222 ? 0.2144 0.1867 0.1958 0.0140  0.0112  0.0110  1220 THR A N   
9019  C CA  . THR A 1222 ? 0.2493 0.2208 0.2339 0.0134  0.0108  0.0109  1220 THR A CA  
9020  C C   . THR A 1222 ? 0.2810 0.2517 0.2677 0.0129  0.0110  0.0116  1220 THR A C   
9021  O O   . THR A 1222 ? 0.3507 0.3209 0.3406 0.0125  0.0106  0.0112  1220 THR A O   
9022  C CB  . THR A 1222 ? 0.2708 0.2431 0.2577 0.0140  0.0104  0.0124  1220 THR A CB  
9023  O OG1 . THR A 1222 ? 0.2711 0.2448 0.2585 0.0147  0.0108  0.0152  1220 THR A OG1 
9024  C CG2 . THR A 1222 ? 0.2585 0.2317 0.2436 0.0144  0.0100  0.0114  1220 THR A CG2 
9025  N N   . ALA A 1223 ? 0.2397 0.2105 0.2249 0.0131  0.0116  0.0124  1221 ALA A N   
9026  C CA  . ALA A 1223 ? 0.2803 0.2503 0.2671 0.0126  0.0118  0.0129  1221 ALA A CA  
9027  C C   . ALA A 1223 ? 0.3263 0.2954 0.3117 0.0117  0.0117  0.0110  1221 ALA A C   
9028  O O   . ALA A 1223 ? 0.3768 0.3454 0.3631 0.0112  0.0119  0.0112  1221 ALA A O   
9029  C CB  . ALA A 1223 ? 0.3081 0.2794 0.2946 0.0133  0.0125  0.0150  1221 ALA A CB  
9030  N N   . ALA A 1224 ? 0.2661 0.2351 0.2493 0.0113  0.0114  0.0094  1222 ALA A N   
9031  C CA  . ALA A 1224 ? 0.3074 0.2758 0.2892 0.0104  0.0112  0.0084  1222 ALA A CA  
9032  C C   . ALA A 1224 ? 0.3246 0.2933 0.3081 0.0092  0.0110  0.0076  1222 ALA A C   
9033  O O   . ALA A 1224 ? 0.3660 0.3345 0.3490 0.0084  0.0108  0.0076  1222 ALA A O   
9034  C CB  . ALA A 1224 ? 0.3023 0.2710 0.2823 0.0100  0.0107  0.0073  1222 ALA A CB  
9035  N N   . ALA A 1225 ? 0.3009 0.2702 0.2867 0.0092  0.0108  0.0070  1223 ALA A N   
9036  C CA  . ALA A 1225 ? 0.3169 0.2871 0.3044 0.0083  0.0105  0.0057  1223 ALA A CA  
9037  C C   . ALA A 1225 ? 0.3656 0.3350 0.3549 0.0083  0.0106  0.0066  1223 ALA A C   
9038  O O   . ALA A 1225 ? 0.3626 0.3330 0.3531 0.0076  0.0103  0.0054  1223 ALA A O   
9039  C CB  . ALA A 1225 ? 0.3690 0.3402 0.3589 0.0085  0.0100  0.0041  1223 ALA A CB  
9040  N N   . GLY A 1226 ? 0.3232 0.2917 0.3128 0.0091  0.0110  0.0085  1224 GLY A N   
9041  C CA  . GLY A 1226 ? 0.3102 0.2782 0.3015 0.0091  0.0111  0.0096  1224 GLY A CA  
9042  C C   . GLY A 1226 ? 0.3680 0.3358 0.3627 0.0098  0.0111  0.0113  1224 GLY A C   
9043  O O   . GLY A 1226 ? 0.3620 0.3296 0.3586 0.0098  0.0112  0.0126  1224 GLY A O   
9044  N N   . GLY A 1227 ? 0.3053 0.2733 0.3012 0.0103  0.0109  0.0116  1225 GLY A N   
9045  C CA  . GLY A 1227 ? 0.3639 0.3319 0.3634 0.0108  0.0107  0.0138  1225 GLY A CA  
9046  C C   . GLY A 1227 ? 0.3185 0.2870 0.3178 0.0115  0.0105  0.0145  1225 GLY A C   
9047  O O   . GLY A 1227 ? 0.3261 0.2948 0.3227 0.0116  0.0106  0.0130  1225 GLY A O   
9048  N N   . ASN A 1228 ? 0.2878 0.2566 0.2904 0.0119  0.0102  0.0171  1226 ASN A N   
9049  C CA  . ASN A 1228 ? 0.2982 0.2680 0.3011 0.0126  0.0100  0.0186  1226 ASN A CA  
9050  C C   . ASN A 1228 ? 0.3206 0.2895 0.3293 0.0125  0.0086  0.0186  1226 ASN A C   
9051  O O   . ASN A 1228 ? 0.3278 0.2964 0.3412 0.0123  0.0080  0.0207  1226 ASN A O   
9052  C CB  . ASN A 1228 ? 0.3250 0.2968 0.3271 0.0131  0.0107  0.0223  1226 ASN A CB  
9053  C CG  . ASN A 1228 ? 0.3471 0.3206 0.3487 0.0138  0.0106  0.0241  1226 ASN A CG  
9054  O OD1 . ASN A 1228 ? 0.3661 0.3391 0.3707 0.0138  0.0096  0.0240  1226 ASN A OD1 
9055  N ND2 . ASN A 1228 ? 0.3579 0.3341 0.3560 0.0145  0.0115  0.0257  1226 ASN A ND2 
9056  N N   . ALA A 1229 ? 0.3177 0.2862 0.3263 0.0126  0.0080  0.0162  1227 ALA A N   
9057  C CA  . ALA A 1229 ? 0.3134 0.2812 0.3280 0.0127  0.0065  0.0153  1227 ALA A CA  
9058  C C   . ALA A 1229 ? 0.3415 0.3095 0.3603 0.0131  0.0057  0.0193  1227 ALA A C   
9059  O O   . ALA A 1229 ? 0.3277 0.2948 0.3529 0.0129  0.0044  0.0202  1227 ALA A O   
9060  C CB  . ALA A 1229 ? 0.3400 0.3081 0.3534 0.0129  0.0061  0.0121  1227 ALA A CB  
9061  N N   . SER A 1230 ? 0.3419 0.3116 0.3576 0.0136  0.0063  0.0217  1228 SER A N   
9062  C CA  . SER A 1230 ? 0.3594 0.3302 0.3789 0.0138  0.0055  0.0260  1228 SER A CA  
9063  C C   . SER A 1230 ? 0.3736 0.3449 0.3963 0.0134  0.0056  0.0296  1228 SER A C   
9064  O O   . SER A 1230 ? 0.3677 0.3388 0.3968 0.0132  0.0042  0.0325  1228 SER A O   
9065  C CB  . SER A 1230 ? 0.4146 0.3879 0.4293 0.0144  0.0064  0.0278  1228 SER A CB  
9066  O OG  . SER A 1230 ? 0.4717 0.4445 0.4847 0.0148  0.0060  0.0249  1228 SER A OG  
9067  N N   . LEU A 1231 ? 0.3544 0.3264 0.3732 0.0132  0.0070  0.0296  1229 LEU A N   
9068  C CA  . LEU A 1231 ? 0.3513 0.3241 0.3729 0.0127  0.0071  0.0329  1229 LEU A CA  
9069  C C   . LEU A 1231 ? 0.3766 0.3468 0.4042 0.0120  0.0059  0.0317  1229 LEU A C   
9070  O O   . LEU A 1231 ? 0.4014 0.3721 0.4332 0.0115  0.0055  0.0348  1229 LEU A O   
9071  C CB  . LEU A 1231 ? 0.3250 0.2998 0.3410 0.0129  0.0090  0.0332  1229 LEU A CB  
9072  C CG  . LEU A 1231 ? 0.3861 0.3648 0.3977 0.0136  0.0101  0.0356  1229 LEU A CG  
9073  C CD1 . LEU A 1231 ? 0.3319 0.3126 0.3395 0.0138  0.0117  0.0357  1229 LEU A CD1 
9074  C CD2 . LEU A 1231 ? 0.4549 0.4363 0.4706 0.0136  0.0094  0.0407  1229 LEU A CD2 
9075  N N   . MET A 1232 ? 0.3945 0.3625 0.4229 0.0120  0.0051  0.0271  1230 MET A N   
9076  C CA  . MET A 1232 ? 0.3622 0.3281 0.3971 0.0116  0.0036  0.0255  1230 MET A CA  
9077  C C   . MET A 1232 ? 0.3975 0.3629 0.4406 0.0115  0.0016  0.0284  1230 MET A C   
9078  O O   . MET A 1232 ? 0.4270 0.3910 0.4766 0.0111  0.0001  0.0286  1230 MET A O   
9079  C CB  . MET A 1232 ? 0.3878 0.3526 0.4218 0.0117  0.0031  0.0198  1230 MET A CB  
9080  N N   . ALA A 1233 ? 0.4229 0.3893 0.4660 0.0120  0.0013  0.0308  1231 ALA A N   
9081  C CA  . ALA A 1233 ? 0.4601 0.4262 0.5112 0.0119  -0.0007 0.0344  1231 ALA A CA  
9082  C C   . ALA A 1233 ? 0.4860 0.4546 0.5383 0.0114  -0.0004 0.0410  1231 ALA A C   
9083  O O   . ALA A 1233 ? 0.4849 0.4537 0.5442 0.0111  -0.0021 0.0450  1231 ALA A O   
9084  C CB  . ALA A 1233 ? 0.4488 0.4150 0.5000 0.0126  -0.0015 0.0337  1231 ALA A CB  
9085  N N   . ILE A 1234 ? 0.4643 0.4353 0.5104 0.0112  0.0018  0.0423  1232 ILE A N   
9086  C CA  . ILE A 1234 ? 0.4848 0.4594 0.5313 0.0108  0.0025  0.0483  1232 ILE A CA  
9087  C C   . ILE A 1234 ? 0.4390 0.4132 0.4887 0.0100  0.0025  0.0493  1232 ILE A C   
9088  O O   . ILE A 1234 ? 0.4205 0.3946 0.4653 0.0100  0.0040  0.0468  1232 ILE A O   
9089  C CB  . ILE A 1234 ? 0.4276 0.4061 0.4655 0.0115  0.0047  0.0491  1232 ILE A CB  
9090  C CG1 . ILE A 1234 ? 0.4756 0.4548 0.5113 0.0122  0.0044  0.0487  1232 ILE A CG1 
9091  C CG2 . ILE A 1234 ? 0.3996 0.3828 0.4379 0.0111  0.0055  0.0550  1232 ILE A CG2 
9092  C CD1 . ILE A 1234 ? 0.4616 0.4459 0.4917 0.0128  0.0059  0.0517  1232 ILE A CD1 
9093  N N   . GLY A 1235 ? 0.4573 0.4312 0.5157 0.0092  0.0006  0.0532  1233 GLY A N   
9094  C CA  . GLY A 1235 ? 0.3798 0.3536 0.4422 0.0083  0.0004  0.0550  1233 GLY A CA  
9095  C C   . GLY A 1235 ? 0.3432 0.3203 0.4111 0.0074  -0.0003 0.0625  1233 GLY A C   
9096  O O   . GLY A 1235 ? 0.3790 0.3566 0.4514 0.0073  -0.0018 0.0656  1233 GLY A O   
9097  O OXT . GLY A 1235 ? 0.2659 0.2458 0.3344 0.0067  0.0006  0.0660  1233 GLY A OXT 
9098  N N   . ALA B 16   ? 0.5801 0.5093 0.5804 0.0533  -0.0079 -0.0219 14   ALA B N   
9099  C CA  . ALA B 16   ? 0.5685 0.5016 0.5688 0.0489  -0.0081 -0.0215 14   ALA B CA  
9100  C C   . ALA B 16   ? 0.5577 0.4843 0.5518 0.0454  -0.0088 -0.0221 14   ALA B C   
9101  O O   . ALA B 16   ? 0.5928 0.5141 0.5829 0.0459  -0.0079 -0.0238 14   ALA B O   
9102  C CB  . ALA B 16   ? 0.5202 0.4598 0.5232 0.0488  -0.0057 -0.0227 14   ALA B CB  
9103  N N   . PRO B 17   ? 0.5314 0.4587 0.5247 0.0420  -0.0104 -0.0208 15   PRO B N   
9104  C CA  . PRO B 17   ? 0.5297 0.4517 0.5177 0.0383  -0.0112 -0.0211 15   PRO B CA  
9105  C C   . PRO B 17   ? 0.4521 0.3752 0.4384 0.0367  -0.0094 -0.0229 15   PRO B C   
9106  O O   . PRO B 17   ? 0.4650 0.3947 0.4546 0.0366  -0.0081 -0.0233 15   PRO B O   
9107  C CB  . PRO B 17   ? 0.5507 0.4756 0.5395 0.0353  -0.0128 -0.0192 15   PRO B CB  
9108  C CG  . PRO B 17   ? 0.5578 0.4908 0.5524 0.0366  -0.0124 -0.0185 15   PRO B CG  
9109  C CD  . PRO B 17   ? 0.5115 0.4447 0.5089 0.0410  -0.0116 -0.0189 15   PRO B CD  
9110  N N   . ALA B 18   ? 0.4457 0.3622 0.4267 0.0353  -0.0096 -0.0241 16   ALA B N   
9111  C CA  . ALA B 18   ? 0.4143 0.3311 0.3931 0.0335  -0.0082 -0.0258 16   ALA B CA  
9112  C C   . ALA B 18   ? 0.3728 0.2955 0.3531 0.0298  -0.0084 -0.0250 16   ALA B C   
9113  O O   . ALA B 18   ? 0.3933 0.3161 0.3734 0.0275  -0.0099 -0.0235 16   ALA B O   
9114  C CB  . ALA B 18   ? 0.3977 0.3060 0.3703 0.0320  -0.0089 -0.0269 16   ALA B CB  
9115  N N   . PRO B 19   ? 0.3163 0.2437 0.2979 0.0294  -0.0068 -0.0260 17   PRO B N   
9116  C CA  . PRO B 19   ? 0.3219 0.2549 0.3050 0.0262  -0.0069 -0.0253 17   PRO B CA  
9117  C C   . PRO B 19   ? 0.3040 0.2336 0.2833 0.0224  -0.0082 -0.0249 17   PRO B C   
9118  O O   . PRO B 19   ? 0.3261 0.2505 0.3011 0.0213  -0.0083 -0.0261 17   PRO B O   
9119  C CB  . PRO B 19   ? 0.3306 0.2674 0.3146 0.0267  -0.0049 -0.0267 17   PRO B CB  
9120  C CG  . PRO B 19   ? 0.3467 0.2828 0.3320 0.0307  -0.0036 -0.0276 17   PRO B CG  
9121  C CD  . PRO B 19   ? 0.3471 0.2756 0.3292 0.0320  -0.0047 -0.0278 17   PRO B CD  
9122  N N   . PHE B 20   ? 0.2942 0.2268 0.2749 0.0202  -0.0092 -0.0233 18   PHE B N   
9123  C CA  . PHE B 20   ? 0.2728 0.2040 0.2507 0.0164  -0.0103 -0.0227 18   PHE B CA  
9124  C C   . PHE B 20   ? 0.3308 0.2543 0.3045 0.0155  -0.0117 -0.0223 18   PHE B C   
9125  O O   . PHE B 20   ? 0.3557 0.2774 0.3266 0.0121  -0.0125 -0.0219 18   PHE B O   
9126  C CB  . PHE B 20   ? 0.2824 0.2155 0.2590 0.0141  -0.0095 -0.0238 18   PHE B CB  
9127  C CG  . PHE B 20   ? 0.2469 0.1871 0.2272 0.0146  -0.0082 -0.0240 18   PHE B CG  
9128  C CD1 . PHE B 20   ? 0.2560 0.2015 0.2390 0.0132  -0.0084 -0.0227 18   PHE B CD1 
9129  C CD2 . PHE B 20   ? 0.2769 0.2185 0.2578 0.0165  -0.0066 -0.0255 18   PHE B CD2 
9130  C CE1 . PHE B 20   ? 0.2813 0.2329 0.2675 0.0137  -0.0073 -0.0229 18   PHE B CE1 
9131  C CE2 . PHE B 20   ? 0.2579 0.2059 0.2421 0.0168  -0.0055 -0.0255 18   PHE B CE2 
9132  C CZ  . PHE B 20   ? 0.2676 0.2204 0.2544 0.0154  -0.0059 -0.0241 18   PHE B CZ  
9133  N N   . ALA B 21   ? 0.3748 0.2939 0.3481 0.0184  -0.0121 -0.0223 19   ALA B N   
9134  C CA  . ALA B 21   ? 0.3806 0.2918 0.3497 0.0177  -0.0135 -0.0220 19   ALA B CA  
9135  C C   . ALA B 21   ? 0.4365 0.3475 0.4052 0.0152  -0.0151 -0.0198 19   ALA B C   
9136  O O   . ALA B 21   ? 0.4882 0.3931 0.4530 0.0133  -0.0163 -0.0192 19   ALA B O   
9137  C CB  . ALA B 21   ? 0.4582 0.3649 0.4273 0.0218  -0.0135 -0.0224 19   ALA B CB  
9138  N N   . ASP B 22   ? 0.3347 0.2521 0.3071 0.0151  -0.0151 -0.0185 20   ASP B N   
9139  C CA  . ASP B 22   ? 0.3546 0.2724 0.3265 0.0129  -0.0164 -0.0165 20   ASP B CA  
9140  C C   . ASP B 22   ? 0.3056 0.2304 0.2796 0.0106  -0.0158 -0.0162 20   ASP B C   
9141  O O   . ASP B 22   ? 0.3227 0.2510 0.2985 0.0102  -0.0163 -0.0148 20   ASP B O   
9142  C CB  . ASP B 22   ? 0.4279 0.3451 0.4015 0.0154  -0.0174 -0.0151 20   ASP B CB  
9143  N N   . PHE B 23   ? 0.2765 0.2034 0.2502 0.0091  -0.0147 -0.0175 21   PHE B N   
9144  C CA  . PHE B 23   ? 0.2636 0.1976 0.2399 0.0076  -0.0140 -0.0173 21   PHE B CA  
9145  C C   . PHE B 23   ? 0.2567 0.1920 0.2321 0.0046  -0.0148 -0.0157 21   PHE B C   
9146  O O   . PHE B 23   ? 0.2540 0.1938 0.2318 0.0047  -0.0148 -0.0148 21   PHE B O   
9147  C CB  . PHE B 23   ? 0.2616 0.1973 0.2375 0.0065  -0.0128 -0.0189 21   PHE B CB  
9148  C CG  . PHE B 23   ? 0.2396 0.1820 0.2178 0.0050  -0.0121 -0.0186 21   PHE B CG  
9149  C CD1 . PHE B 23   ? 0.2454 0.1932 0.2275 0.0069  -0.0114 -0.0186 21   PHE B CD1 
9150  C CD2 . PHE B 23   ? 0.2683 0.2119 0.2450 0.0017  -0.0123 -0.0184 21   PHE B CD2 
9151  C CE1 . PHE B 23   ? 0.2474 0.2010 0.2315 0.0056  -0.0108 -0.0184 21   PHE B CE1 
9152  C CE2 . PHE B 23   ? 0.2527 0.2025 0.2317 0.0006  -0.0116 -0.0181 21   PHE B CE2 
9153  C CZ  . PHE B 23   ? 0.2591 0.2136 0.2416 0.0027  -0.0109 -0.0182 21   PHE B CZ  
9154  N N   . ALA B 24   ? 0.2591 0.1904 0.2309 0.0018  -0.0155 -0.0153 22   ALA B N   
9155  C CA  . ALA B 24   ? 0.2665 0.1995 0.2374 -0.0012 -0.0161 -0.0136 22   ALA B CA  
9156  C C   . ALA B 24   ? 0.2531 0.1799 0.2199 -0.0038 -0.0172 -0.0129 22   ALA B C   
9157  O O   . ALA B 24   ? 0.2761 0.2037 0.2414 -0.0070 -0.0171 -0.0126 22   ALA B O   
9158  C CB  . ALA B 24   ? 0.2959 0.2351 0.2684 -0.0032 -0.0151 -0.0140 22   ALA B CB  
9159  N N   . PRO B 25   ? 0.2773 0.1977 0.2419 -0.0024 -0.0182 -0.0124 23   PRO B N   
9160  C CA  . PRO B 25   ? 0.3190 0.2328 0.2795 -0.0049 -0.0194 -0.0116 23   PRO B CA  
9161  C C   . PRO B 25   ? 0.3137 0.2295 0.2732 -0.0083 -0.0198 -0.0095 23   PRO B C   
9162  O O   . PRO B 25   ? 0.2997 0.2191 0.2609 -0.0076 -0.0199 -0.0084 23   PRO B O   
9163  C CB  . PRO B 25   ? 0.3550 0.2625 0.3142 -0.0021 -0.0204 -0.0112 23   PRO B CB  
9164  C CG  . PRO B 25   ? 0.3441 0.2563 0.3070 0.0009  -0.0201 -0.0108 23   PRO B CG  
9165  C CD  . PRO B 25   ? 0.3102 0.2295 0.2765 0.0013  -0.0186 -0.0122 23   PRO B CD  
9166  N N   . PRO B 26   ? 0.2883 0.2020 0.2451 -0.0120 -0.0202 -0.0091 24   PRO B N   
9167  C CA  . PRO B 26   ? 0.2944 0.2103 0.2504 -0.0153 -0.0205 -0.0071 24   PRO B CA  
9168  C C   . PRO B 26   ? 0.3198 0.2308 0.2735 -0.0151 -0.0217 -0.0051 24   PRO B C   
9169  O O   . PRO B 26   ? 0.3212 0.2256 0.2730 -0.0132 -0.0227 -0.0052 24   PRO B O   
9170  C CB  . PRO B 26   ? 0.3368 0.2509 0.2905 -0.0192 -0.0207 -0.0072 24   PRO B CB  
9171  C CG  . PRO B 26   ? 0.3418 0.2492 0.2933 -0.0180 -0.0212 -0.0088 24   PRO B CG  
9172  C CD  . PRO B 26   ? 0.3302 0.2395 0.2846 -0.0135 -0.0204 -0.0104 24   PRO B CD  
9173  N N   . VAL B 27   ? 0.3200 0.2344 0.2737 -0.0169 -0.0217 -0.0032 25   VAL B N   
9174  C CA  . VAL B 27   ? 0.3124 0.2225 0.2635 -0.0171 -0.0230 -0.0011 25   VAL B CA  
9175  C C   . VAL B 27   ? 0.3082 0.2100 0.2551 -0.0192 -0.0242 -0.0003 25   VAL B C   
9176  O O   . VAL B 27   ? 0.3502 0.2456 0.2948 -0.0179 -0.0255 0.0006  25   VAL B O   
9177  C CB  . VAL B 27   ? 0.3077 0.2232 0.2590 -0.0193 -0.0225 0.0007  25   VAL B CB  
9178  C CG1 . VAL B 27   ? 0.3551 0.2656 0.3030 -0.0203 -0.0239 0.0032  25   VAL B CG1 
9179  C CG2 . VAL B 27   ? 0.3215 0.2438 0.2765 -0.0168 -0.0216 0.0000  25   VAL B CG2 
9180  N N   . ARG B 28   ? 0.3117 0.2132 0.2574 -0.0226 -0.0240 -0.0007 26   ARG B N   
9181  C CA  . ARG B 28   ? 0.3339 0.2273 0.2754 -0.0251 -0.0252 0.0000  26   ARG B CA  
9182  C C   . ARG B 28   ? 0.3597 0.2533 0.3011 -0.0272 -0.0248 -0.0018 26   ARG B C   
9183  O O   . ARG B 28   ? 0.3331 0.2339 0.2775 -0.0275 -0.0236 -0.0029 26   ARG B O   
9184  C CB  . ARG B 28   ? 0.3521 0.2449 0.2912 -0.0290 -0.0257 0.0028  26   ARG B CB  
9185  C CG  . ARG B 28   ? 0.3627 0.2630 0.3033 -0.0327 -0.0246 0.0032  26   ARG B CG  
9186  C CD  . ARG B 28   ? 0.3869 0.2875 0.3254 -0.0361 -0.0248 0.0062  26   ARG B CD  
9187  N NE  . ARG B 28   ? 0.3849 0.2884 0.3242 -0.0340 -0.0246 0.0074  26   ARG B NE  
9188  C CZ  . ARG B 28   ? 0.4553 0.3535 0.3921 -0.0328 -0.0258 0.0089  26   ARG B CZ  
9189  N NH1 . ARG B 28   ? 0.4687 0.3578 0.4019 -0.0334 -0.0273 0.0096  26   ARG B NH1 
9190  N NH2 . ARG B 28   ? 0.4205 0.3222 0.3581 -0.0310 -0.0256 0.0099  26   ARG B NH2 
9191  N N   . PRO B 29   ? 0.3529 0.2383 0.2906 -0.0285 -0.0259 -0.0022 27   PRO B N   
9192  C CA  . PRO B 29   ? 0.3428 0.2282 0.2799 -0.0311 -0.0258 -0.0037 27   PRO B CA  
9193  C C   . PRO B 29   ? 0.3318 0.2235 0.2699 -0.0356 -0.0254 -0.0023 27   PRO B C   
9194  O O   . PRO B 29   ? 0.3632 0.2549 0.3001 -0.0381 -0.0257 0.0001  27   PRO B O   
9195  C CB  . PRO B 29   ? 0.3888 0.2633 0.3211 -0.0321 -0.0274 -0.0038 27   PRO B CB  
9196  C CG  . PRO B 29   ? 0.4253 0.2946 0.3567 -0.0280 -0.0280 -0.0034 27   PRO B CG  
9197  C CD  . PRO B 29   ? 0.3915 0.2672 0.3255 -0.0275 -0.0275 -0.0014 27   PRO B CD  
9198  N N   . GLN B 30   ? 0.3421 0.2396 0.2825 -0.0364 -0.0245 -0.0038 28   GLN B N   
9199  C CA  . GLN B 30   ? 0.3504 0.2553 0.2927 -0.0401 -0.0238 -0.0026 28   GLN B CA  
9200  C C   . GLN B 30   ? 0.3217 0.2227 0.2609 -0.0451 -0.0250 -0.0018 28   GLN B C   
9201  O O   . GLN B 30   ? 0.3630 0.2603 0.3006 -0.0460 -0.0257 -0.0035 28   GLN B O   
9202  C CB  . GLN B 30   ? 0.3175 0.2303 0.2637 -0.0388 -0.0226 -0.0045 28   GLN B CB  
9203  C CG  . GLN B 30   ? 0.3116 0.2282 0.2608 -0.0340 -0.0214 -0.0054 28   GLN B CG  
9204  C CD  . GLN B 30   ? 0.3075 0.2292 0.2585 -0.0338 -0.0207 -0.0035 28   GLN B CD  
9205  O OE1 . GLN B 30   ? 0.3208 0.2498 0.2740 -0.0355 -0.0198 -0.0028 28   GLN B OE1 
9206  N NE2 . GLN B 30   ? 0.3017 0.2195 0.2515 -0.0316 -0.0212 -0.0026 28   GLN B NE2 
9207  N N   . SER B 31   ? 0.3280 0.2297 0.2662 -0.0485 -0.0252 0.0008  29   SER B N   
9208  C CA  . SER B 31   ? 0.3263 0.2249 0.2620 -0.0537 -0.0263 0.0020  29   SER B CA  
9209  C C   . SER B 31   ? 0.3221 0.2281 0.2605 -0.0564 -0.0258 0.0013  29   SER B C   
9210  O O   . SER B 31   ? 0.3146 0.2285 0.2568 -0.0544 -0.0244 0.0003  29   SER B O   
9211  C CB  . SER B 31   ? 0.3420 0.2410 0.2765 -0.0565 -0.0264 0.0052  29   SER B CB  
9212  O OG  . SER B 31   ? 0.3358 0.2453 0.2742 -0.0569 -0.0247 0.0061  29   SER B OG  
9213  N N   . THR B 32   ? 0.3324 0.2356 0.2686 -0.0612 -0.0270 0.0020  30   THR B N   
9214  C CA  . THR B 32   ? 0.3255 0.2360 0.2643 -0.0644 -0.0267 0.0018  30   THR B CA  
9215  C C   . THR B 32   ? 0.3055 0.2270 0.2486 -0.0647 -0.0249 0.0034  30   THR B C   
9216  O O   . THR B 32   ? 0.3217 0.2511 0.2685 -0.0638 -0.0239 0.0023  30   THR B O   
9217  C CB  . THR B 32   ? 0.3608 0.2666 0.2964 -0.0700 -0.0284 0.0030  30   THR B CB  
9218  O OG1 . THR B 32   ? 0.4412 0.3367 0.3727 -0.0695 -0.0300 0.0011  30   THR B OG1 
9219  C CG2 . THR B 32   ? 0.3791 0.2931 0.3177 -0.0737 -0.0282 0.0031  30   THR B CG2 
9220  N N   . LEU B 33   ? 0.3222 0.2440 0.2646 -0.0658 -0.0245 0.0059  31   LEU B N   
9221  C CA  . LEU B 33   ? 0.2981 0.2300 0.2442 -0.0659 -0.0227 0.0073  31   LEU B CA  
9222  C C   . LEU B 33   ? 0.2984 0.2350 0.2475 -0.0607 -0.0212 0.0058  31   LEU B C   
9223  O O   . LEU B 33   ? 0.2767 0.2224 0.2296 -0.0602 -0.0198 0.0056  31   LEU B O   
9224  C CB  . LEU B 33   ? 0.3042 0.2348 0.2483 -0.0683 -0.0226 0.0103  31   LEU B CB  
9225  C CG  . LEU B 33   ? 0.3288 0.2570 0.2708 -0.0742 -0.0237 0.0122  31   LEU B CG  
9226  C CD1 . LEU B 33   ? 0.3446 0.2698 0.2838 -0.0763 -0.0237 0.0152  31   LEU B CD1 
9227  C CD2 . LEU B 33   ? 0.3899 0.3280 0.3358 -0.0771 -0.0228 0.0125  31   LEU B CD2 
9228  N N   . ARG B 34   ? 0.2799 0.2106 0.2274 -0.0568 -0.0216 0.0047  32   ARG B N   
9229  C CA  . ARG B 34   ? 0.2696 0.2048 0.2200 -0.0520 -0.0204 0.0032  32   ARG B CA  
9230  C C   . ARG B 34   ? 0.2690 0.2079 0.2220 -0.0507 -0.0200 0.0009  32   ARG B C   
9231  O O   . ARG B 34   ? 0.2669 0.2132 0.2235 -0.0485 -0.0186 0.0002  32   ARG B O   
9232  C CB  . ARG B 34   ? 0.2656 0.1940 0.2141 -0.0482 -0.0209 0.0027  32   ARG B CB  
9233  C CG  . ARG B 34   ? 0.2938 0.2196 0.2401 -0.0485 -0.0211 0.0050  32   ARG B CG  
9234  C CD  . ARG B 34   ? 0.2967 0.2305 0.2457 -0.0471 -0.0195 0.0058  32   ARG B CD  
9235  N NE  . ARG B 34   ? 0.2877 0.2236 0.2391 -0.0424 -0.0189 0.0040  32   ARG B NE  
9236  C CZ  . ARG B 34   ? 0.3030 0.2355 0.2535 -0.0391 -0.0193 0.0039  32   ARG B CZ  
9237  N NH1 . ARG B 34   ? 0.3169 0.2435 0.2641 -0.0397 -0.0204 0.0057  32   ARG B NH1 
9238  N NH2 . ARG B 34   ? 0.3040 0.2391 0.2572 -0.0352 -0.0187 0.0022  32   ARG B NH2 
9239  N N   . ARG B 35   ? 0.2740 0.2078 0.2251 -0.0520 -0.0213 -0.0004 33   ARG B N   
9240  C CA  . ARG B 35   ? 0.2911 0.2281 0.2442 -0.0509 -0.0211 -0.0026 33   ARG B CA  
9241  C C   . ARG B 35   ? 0.2692 0.2153 0.2255 -0.0535 -0.0203 -0.0019 33   ARG B C   
9242  O O   . ARG B 35   ? 0.2647 0.2167 0.2242 -0.0515 -0.0195 -0.0032 33   ARG B O   
9243  C CB  . ARG B 35   ? 0.2972 0.2262 0.2468 -0.0521 -0.0227 -0.0040 33   ARG B CB  
9244  C CG  . ARG B 35   ? 0.3201 0.2412 0.2673 -0.0483 -0.0231 -0.0054 33   ARG B CG  
9245  C CD  . ARG B 35   ? 0.3992 0.3120 0.3426 -0.0493 -0.0246 -0.0070 33   ARG B CD  
9246  N NE  . ARG B 35   ? 0.5075 0.4126 0.4486 -0.0456 -0.0249 -0.0081 33   ARG B NE  
9247  C CZ  . ARG B 35   ? 0.5965 0.5023 0.5390 -0.0410 -0.0240 -0.0100 33   ARG B CZ  
9248  N NH1 . ARG B 35   ? 0.6019 0.5153 0.5479 -0.0398 -0.0229 -0.0111 33   ARG B NH1 
9249  N NH2 . ARG B 35   ? 0.5691 0.4681 0.5096 -0.0377 -0.0243 -0.0107 33   ARG B NH2 
9250  N N   . ALA B 36   ? 0.2632 0.2108 0.2191 -0.0579 -0.0206 0.0002  34   ALA B N   
9251  C CA  . ALA B 36   ? 0.2737 0.2308 0.2331 -0.0603 -0.0198 0.0011  34   ALA B CA  
9252  C C   . ALA B 36   ? 0.2700 0.2352 0.2331 -0.0575 -0.0178 0.0015  34   ALA B C   
9253  O O   . ALA B 36   ? 0.2857 0.2588 0.2523 -0.0573 -0.0169 0.0011  34   ALA B O   
9254  C CB  . ALA B 36   ? 0.2817 0.2385 0.2398 -0.0658 -0.0206 0.0034  34   ALA B CB  
9255  N N   . ILE B 37   ? 0.2512 0.2143 0.2132 -0.0554 -0.0172 0.0022  35   ILE B N   
9256  C CA  . ILE B 37   ? 0.2530 0.2226 0.2179 -0.0523 -0.0154 0.0022  35   ILE B CA  
9257  C C   . ILE B 37   ? 0.2651 0.2365 0.2322 -0.0483 -0.0150 -0.0002 35   ILE B C   
9258  O O   . ILE B 37   ? 0.2270 0.2059 0.1976 -0.0473 -0.0139 -0.0006 35   ILE B O   
9259  C CB  . ILE B 37   ? 0.2405 0.2064 0.2032 -0.0507 -0.0152 0.0034  35   ILE B CB  
9260  C CG1 . ILE B 37   ? 0.2439 0.2094 0.2047 -0.0548 -0.0153 0.0060  35   ILE B CG1 
9261  C CG2 . ILE B 37   ? 0.2397 0.2112 0.2051 -0.0469 -0.0136 0.0028  35   ILE B CG2 
9262  C CD1 . ILE B 37   ? 0.2579 0.2171 0.2153 -0.0538 -0.0158 0.0072  35   ILE B CD1 
9263  N N   . THR B 38   ? 0.2282 0.1928 0.1934 -0.0460 -0.0159 -0.0017 36   THR B N   
9264  C CA  . THR B 38   ? 0.2423 0.2084 0.2095 -0.0421 -0.0154 -0.0038 36   THR B CA  
9265  C C   . THR B 38   ? 0.2494 0.2201 0.2187 -0.0432 -0.0154 -0.0048 36   THR B C   
9266  O O   . THR B 38   ? 0.2461 0.2221 0.2183 -0.0408 -0.0144 -0.0058 36   THR B O   
9267  C CB  . THR B 38   ? 0.2404 0.1982 0.2050 -0.0399 -0.0164 -0.0052 36   THR B CB  
9268  O OG1 . THR B 38   ? 0.2475 0.2008 0.2100 -0.0392 -0.0166 -0.0040 36   THR B OG1 
9269  C CG2 . THR B 38   ? 0.2978 0.2574 0.2645 -0.0357 -0.0156 -0.0072 36   THR B CG2 
9270  N N   . ALA B 39   ? 0.2357 0.2044 0.2033 -0.0469 -0.0166 -0.0045 37   ALA B N   
9271  C CA  . ALA B 39   ? 0.2356 0.2085 0.2050 -0.0482 -0.0169 -0.0054 37   ALA B CA  
9272  C C   . ALA B 39   ? 0.2612 0.2441 0.2348 -0.0485 -0.0156 -0.0045 37   ALA B C   
9273  O O   . ALA B 39   ? 0.2708 0.2583 0.2466 -0.0478 -0.0154 -0.0054 37   ALA B O   
9274  C CB  . ALA B 39   ? 0.2765 0.2453 0.2432 -0.0527 -0.0186 -0.0050 37   ALA B CB  
9275  N N   . ALA B 40   ? 0.2368 0.2230 0.2112 -0.0493 -0.0146 -0.0027 38   ALA B N   
9276  C CA  . ALA B 40   ? 0.2423 0.2380 0.2206 -0.0496 -0.0132 -0.0017 38   ALA B CA  
9277  C C   . ALA B 40   ? 0.2212 0.2207 0.2018 -0.0452 -0.0117 -0.0024 38   ALA B C   
9278  O O   . ALA B 40   ? 0.2267 0.2338 0.2104 -0.0448 -0.0104 -0.0019 38   ALA B O   
9279  C CB  . ALA B 40   ? 0.2634 0.2612 0.2413 -0.0529 -0.0128 0.0007  38   ALA B CB  
9280  N N   . TYR B 41   ? 0.2309 0.2251 0.2099 -0.0420 -0.0117 -0.0037 39   TYR B N   
9281  C CA  . TYR B 41   ? 0.2252 0.2219 0.2059 -0.0382 -0.0104 -0.0041 39   TYR B CA  
9282  C C   . TYR B 41   ? 0.2089 0.2134 0.1933 -0.0367 -0.0093 -0.0047 39   TYR B C   
9283  O O   . TYR B 41   ? 0.2150 0.2247 0.2013 -0.0357 -0.0079 -0.0040 39   TYR B O   
9284  C CB  . TYR B 41   ? 0.2177 0.2080 0.1967 -0.0352 -0.0109 -0.0056 39   TYR B CB  
9285  C CG  . TYR B 41   ? 0.2222 0.2123 0.2016 -0.0319 -0.0101 -0.0058 39   TYR B CG  
9286  C CD1 . TYR B 41   ? 0.2268 0.2231 0.2085 -0.0307 -0.0087 -0.0054 39   TYR B CD1 
9287  C CD2 . TYR B 41   ? 0.2394 0.2231 0.2167 -0.0301 -0.0108 -0.0064 39   TYR B CD2 
9288  C CE1 . TYR B 41   ? 0.2193 0.2149 0.2010 -0.0278 -0.0081 -0.0057 39   TYR B CE1 
9289  C CE2 . TYR B 41   ? 0.2295 0.2130 0.2072 -0.0272 -0.0103 -0.0065 39   TYR B CE2 
9290  C CZ  . TYR B 41   ? 0.2227 0.2120 0.2025 -0.0262 -0.0090 -0.0062 39   TYR B CZ  
9291  O OH  . TYR B 41   ? 0.2272 0.2161 0.2071 -0.0236 -0.0087 -0.0064 39   TYR B OH  
9292  N N   . ARG B 42   ? 0.2221 0.2274 0.2076 -0.0365 -0.0099 -0.0058 40   ARG B N   
9293  C CA  . ARG B 42   ? 0.2122 0.2244 0.2011 -0.0348 -0.0090 -0.0064 40   ARG B CA  
9294  C C   . ARG B 42   ? 0.2325 0.2484 0.2227 -0.0376 -0.0097 -0.0060 40   ARG B C   
9295  O O   . ARG B 42   ? 0.2506 0.2696 0.2426 -0.0363 -0.0098 -0.0069 40   ARG B O   
9296  C CB  . ARG B 42   ? 0.2359 0.2462 0.2253 -0.0310 -0.0088 -0.0081 40   ARG B CB  
9297  C CG  . ARG B 42   ? 0.2388 0.2467 0.2275 -0.0284 -0.0080 -0.0083 40   ARG B CG  
9298  C CD  . ARG B 42   ? 0.2304 0.2359 0.2194 -0.0250 -0.0079 -0.0098 40   ARG B CD  
9299  N NE  . ARG B 42   ? 0.2328 0.2346 0.2205 -0.0233 -0.0077 -0.0098 40   ARG B NE  
9300  C CZ  . ARG B 42   ? 0.2387 0.2430 0.2275 -0.0216 -0.0068 -0.0095 40   ARG B CZ  
9301  N NH1 . ARG B 42   ? 0.2289 0.2393 0.2201 -0.0209 -0.0057 -0.0093 40   ARG B NH1 
9302  N NH2 . ARG B 42   ? 0.2194 0.2199 0.2066 -0.0205 -0.0069 -0.0094 40   ARG B NH2 
9303  N N   . ARG B 43   ? 0.2139 0.2298 0.2032 -0.0414 -0.0104 -0.0046 41   ARG B N   
9304  C CA  . ARG B 43   ? 0.2322 0.2514 0.2225 -0.0446 -0.0114 -0.0042 41   ARG B CA  
9305  C C   . ARG B 43   ? 0.2379 0.2666 0.2326 -0.0436 -0.0103 -0.0038 41   ARG B C   
9306  O O   . ARG B 43   ? 0.2246 0.2576 0.2211 -0.0421 -0.0087 -0.0030 41   ARG B O   
9307  C CB  . ARG B 43   ? 0.2159 0.2342 0.2048 -0.0490 -0.0120 -0.0024 41   ARG B CB  
9308  C CG  . ARG B 43   ? 0.2318 0.2539 0.2219 -0.0529 -0.0132 -0.0017 41   ARG B CG  
9309  C CD  . ARG B 43   ? 0.2679 0.2863 0.2555 -0.0574 -0.0142 -0.0002 41   ARG B CD  
9310  N NE  . ARG B 43   ? 0.2700 0.2783 0.2532 -0.0576 -0.0156 -0.0014 41   ARG B NE  
9311  C CZ  . ARG B 43   ? 0.3157 0.3178 0.2956 -0.0598 -0.0162 -0.0004 41   ARG B CZ  
9312  N NH1 . ARG B 43   ? 0.2878 0.2928 0.2683 -0.0623 -0.0155 0.0018  41   ARG B NH1 
9313  N NH2 . ARG B 43   ? 0.2784 0.2712 0.2543 -0.0595 -0.0174 -0.0017 41   ARG B NH2 
9314  N N   . PRO B 44   ? 0.2256 0.2574 0.2219 -0.0442 -0.0111 -0.0043 42   PRO B N   
9315  C CA  . PRO B 44   ? 0.2282 0.2689 0.2287 -0.0430 -0.0102 -0.0037 42   PRO B CA  
9316  C C   . PRO B 44   ? 0.2189 0.2659 0.2216 -0.0452 -0.0092 -0.0017 42   PRO B C   
9317  O O   . PRO B 44   ? 0.2158 0.2618 0.2173 -0.0491 -0.0099 -0.0005 42   PRO B O   
9318  C CB  . PRO B 44   ? 0.2401 0.2822 0.2411 -0.0446 -0.0118 -0.0042 42   PRO B CB  
9319  C CG  . PRO B 44   ? 0.3007 0.3340 0.2978 -0.0439 -0.0130 -0.0060 42   PRO B CG  
9320  C CD  . PRO B 44   ? 0.2523 0.2793 0.2463 -0.0452 -0.0129 -0.0055 42   PRO B CD  
9321  N N   . GLU B 45   ? 0.2329 0.2863 0.2387 -0.0426 -0.0075 -0.0013 43   GLU B N   
9322  C CA  . GLU B 45   ? 0.2186 0.2785 0.2267 -0.0440 -0.0061 0.0005  43   GLU B CA  
9323  C C   . GLU B 45   ? 0.2284 0.2936 0.2386 -0.0481 -0.0071 0.0019  43   GLU B C   
9324  O O   . GLU B 45   ? 0.2449 0.3123 0.2553 -0.0513 -0.0068 0.0036  43   GLU B O   
9325  C CB  . GLU B 45   ? 0.2791 0.3448 0.2902 -0.0401 -0.0042 0.0003  43   GLU B CB  
9326  C CG  . GLU B 45   ? 0.2970 0.3663 0.3087 -0.0401 -0.0023 0.0015  43   GLU B CG  
9327  C CD  . GLU B 45   ? 0.2092 0.2794 0.2214 -0.0356 -0.0005 0.0007  43   GLU B CD  
9328  O OE1 . GLU B 45   ? 0.2089 0.2762 0.2207 -0.0324 -0.0007 -0.0009 43   GLU B OE1 
9329  O OE2 . GLU B 45   ? 0.2129 0.2870 0.2257 -0.0353 0.0013  0.0016  43   GLU B OE2 
9330  N N   . THR B 46   ? 0.2288 0.2960 0.2404 -0.0483 -0.0085 0.0013  44   THR B N   
9331  C CA  . THR B 46   ? 0.2322 0.3044 0.2459 -0.0523 -0.0098 0.0025  44   THR B CA  
9332  C C   . THR B 46   ? 0.2322 0.2984 0.2425 -0.0570 -0.0116 0.0030  44   THR B C   
9333  O O   . THR B 46   ? 0.2738 0.3442 0.2856 -0.0611 -0.0124 0.0045  44   THR B O   
9334  C CB  . THR B 46   ? 0.2410 0.3159 0.2564 -0.0514 -0.0111 0.0016  44   THR B CB  
9335  O OG1 . THR B 46   ? 0.2509 0.3174 0.2626 -0.0499 -0.0123 -0.0003 44   THR B OG1 
9336  C CG2 . THR B 46   ? 0.2595 0.3417 0.2790 -0.0474 -0.0096 0.0017  44   THR B CG2 
9337  N N   . GLU B 47   ? 0.2443 0.3008 0.2500 -0.0565 -0.0122 0.0017  45   GLU B N   
9338  C CA  . GLU B 47   ? 0.2468 0.2968 0.2489 -0.0606 -0.0137 0.0022  45   GLU B CA  
9339  C C   . GLU B 47   ? 0.2595 0.3086 0.2606 -0.0620 -0.0124 0.0038  45   GLU B C   
9340  O O   . GLU B 47   ? 0.2911 0.3385 0.2908 -0.0664 -0.0134 0.0052  45   GLU B O   
9341  C CB  . GLU B 47   ? 0.2547 0.2945 0.2523 -0.0594 -0.0150 0.0001  45   GLU B CB  
9342  C CG  . GLU B 47   ? 0.3415 0.3811 0.3392 -0.0588 -0.0164 -0.0014 45   GLU B CG  
9343  C CD  . GLU B 47   ? 0.3751 0.4050 0.3684 -0.0570 -0.0173 -0.0035 45   GLU B CD  
9344  O OE1 . GLU B 47   ? 0.4123 0.4349 0.4021 -0.0579 -0.0175 -0.0035 45   GLU B OE1 
9345  O OE2 . GLU B 47   ? 0.4495 0.4793 0.4429 -0.0545 -0.0176 -0.0050 45   GLU B OE2 
9346  N N   . CYS B 48   ? 0.2249 0.2751 0.2266 -0.0584 -0.0104 0.0037  46   CYS B N   
9347  C CA  . CYS B 48   ? 0.2486 0.2975 0.2488 -0.0595 -0.0092 0.0052  46   CYS B CA  
9348  C C   . CYS B 48   ? 0.2286 0.2862 0.2320 -0.0624 -0.0082 0.0075  46   CYS B C   
9349  O O   . CYS B 48   ? 0.2395 0.2958 0.2413 -0.0657 -0.0081 0.0092  46   CYS B O   
9350  C CB  . CYS B 48   ? 0.2196 0.2679 0.2195 -0.0549 -0.0074 0.0044  46   CYS B CB  
9351  S SG  . CYS B 48   ? 0.2425 0.2805 0.2386 -0.0515 -0.0083 0.0021  46   CYS B SG  
9352  N N   . LEU B 49   ? 0.2157 0.2823 0.2236 -0.0610 -0.0073 0.0077  47   LEU B N   
9353  C CA  . LEU B 49   ? 0.2357 0.3115 0.2471 -0.0626 -0.0057 0.0098  47   LEU B CA  
9354  C C   . LEU B 49   ? 0.2263 0.3050 0.2387 -0.0684 -0.0069 0.0118  47   LEU B C   
9355  O O   . LEU B 49   ? 0.2371 0.3190 0.2499 -0.0708 -0.0057 0.0138  47   LEU B O   
9356  C CB  . LEU B 49   ? 0.2351 0.3198 0.2511 -0.0590 -0.0041 0.0095  47   LEU B CB  
9357  C CG  . LEU B 49   ? 0.2150 0.3007 0.2309 -0.0549 -0.0016 0.0092  47   LEU B CG  
9358  C CD1 . LEU B 49   ? 0.2442 0.3325 0.2596 -0.0571 0.0001  0.0112  47   LEU B CD1 
9359  C CD2 . LEU B 49   ? 0.2360 0.3123 0.2478 -0.0519 -0.0020 0.0072  47   LEU B CD2 
9360  N N   . PRO B 50   ? 0.2417 0.3198 0.2545 -0.0708 -0.0092 0.0114  48   PRO B N   
9361  C CA  . PRO B 50   ? 0.2559 0.3377 0.2701 -0.0765 -0.0104 0.0134  48   PRO B CA  
9362  C C   . PRO B 50   ? 0.2707 0.3467 0.2812 -0.0805 -0.0106 0.0149  48   PRO B C   
9363  O O   . PRO B 50   ? 0.2666 0.3484 0.2791 -0.0839 -0.0098 0.0172  48   PRO B O   
9364  C CB  . PRO B 50   ? 0.2505 0.3298 0.2643 -0.0780 -0.0132 0.0121  48   PRO B CB  
9365  C CG  . PRO B 50   ? 0.2375 0.3185 0.2528 -0.0727 -0.0126 0.0101  48   PRO B CG  
9366  C CD  . PRO B 50   ? 0.2259 0.3022 0.2389 -0.0684 -0.0106 0.0092  48   PRO B CD  
9367  N N   . PRO B 51   ? 0.2634 0.3282 0.2686 -0.0801 -0.0116 0.0137  49   PRO B N   
9368  C CA  . PRO B 51   ? 0.2675 0.3271 0.2693 -0.0838 -0.0118 0.0154  49   PRO B CA  
9369  C C   . PRO B 51   ? 0.2444 0.3079 0.2468 -0.0827 -0.0091 0.0170  49   PRO B C   
9370  O O   . PRO B 51   ? 0.2686 0.3328 0.2702 -0.0867 -0.0087 0.0193  49   PRO B O   
9371  C CB  . PRO B 51   ? 0.3064 0.3534 0.3026 -0.0827 -0.0133 0.0136  49   PRO B CB  
9372  C CG  . PRO B 51   ? 0.3339 0.3802 0.3307 -0.0774 -0.0131 0.0111  49   PRO B CG  
9373  C CD  . PRO B 51   ? 0.2687 0.3250 0.2707 -0.0771 -0.0129 0.0110  49   PRO B CD  
9374  N N   . LEU B 52   ? 0.2660 0.3322 0.2696 -0.0775 -0.0071 0.0159  50   LEU B N   
9375  C CA  . LEU B 52   ? 0.2394 0.3096 0.2434 -0.0762 -0.0044 0.0173  50   LEU B CA  
9376  C C   . LEU B 52   ? 0.2750 0.3570 0.2839 -0.0783 -0.0029 0.0194  50   LEU B C   
9377  O O   . LEU B 52   ? 0.2463 0.3310 0.2549 -0.0805 -0.0014 0.0215  50   LEU B O   
9378  C CB  . LEU B 52   ? 0.2427 0.3126 0.2468 -0.0701 -0.0029 0.0153  50   LEU B CB  
9379  C CG  . LEU B 52   ? 0.2189 0.2780 0.2185 -0.0675 -0.0041 0.0133  50   LEU B CG  
9380  C CD1 . LEU B 52   ? 0.2418 0.3021 0.2425 -0.0618 -0.0028 0.0114  50   LEU B CD1 
9381  C CD2 . LEU B 52   ? 0.2591 0.3114 0.2543 -0.0693 -0.0041 0.0145  50   LEU B CD2 
9382  N N   . VAL B 53   ? 0.2495 0.3388 0.2631 -0.0776 -0.0032 0.0189  51   VAL B N   
9383  C CA  . VAL B 53   ? 0.2389 0.3399 0.2576 -0.0797 -0.0019 0.0209  51   VAL B CA  
9384  C C   . VAL B 53   ? 0.2696 0.3706 0.2877 -0.0862 -0.0030 0.0234  51   VAL B C   
9385  O O   . VAL B 53   ? 0.2604 0.3679 0.2803 -0.0884 -0.0012 0.0258  51   VAL B O   
9386  C CB  . VAL B 53   ? 0.2496 0.3574 0.2730 -0.0782 -0.0027 0.0200  51   VAL B CB  
9387  C CG1 . VAL B 53   ? 0.2476 0.3672 0.2766 -0.0814 -0.0021 0.0224  51   VAL B CG1 
9388  C CG2 . VAL B 53   ? 0.2375 0.3472 0.2623 -0.0718 -0.0011 0.0181  51   VAL B CG2 
9389  N N   . GLU B 54   ? 0.2630 0.3564 0.2783 -0.0894 -0.0060 0.0229  52   GLU B N   
9390  C CA  . GLU B 54   ? 0.3019 0.3939 0.3161 -0.0959 -0.0073 0.0251  52   GLU B CA  
9391  C C   . GLU B 54   ? 0.2977 0.3855 0.3082 -0.0973 -0.0059 0.0268  52   GLU B C   
9392  O O   . GLU B 54   ? 0.3069 0.4001 0.3189 -0.1013 -0.0050 0.0295  52   GLU B O   
9393  C CB  . GLU B 54   ? 0.3531 0.4361 0.3640 -0.0985 -0.0107 0.0238  52   GLU B CB  
9394  N N   . ALA B 55   ? 0.2763 0.3550 0.2821 -0.0940 -0.0058 0.0253  53   ALA B N   
9395  C CA  . ALA B 55   ? 0.3076 0.3815 0.3094 -0.0952 -0.0047 0.0269  53   ALA B CA  
9396  C C   . ALA B 55   ? 0.2862 0.3693 0.2906 -0.0938 -0.0013 0.0285  53   ALA B C   
9397  O O   . ALA B 55   ? 0.3198 0.4027 0.3222 -0.0966 -0.0003 0.0309  53   ALA B O   
9398  C CB  . ALA B 55   ? 0.3290 0.3916 0.3256 -0.0916 -0.0054 0.0249  53   ALA B CB  
9399  N N   . ALA B 56   ? 0.2760 0.3668 0.2843 -0.0893 0.0004  0.0273  54   ALA B N   
9400  C CA  . ALA B 56   ? 0.2741 0.3733 0.2846 -0.0872 0.0037  0.0284  54   ALA B CA  
9401  C C   . ALA B 56   ? 0.2836 0.3948 0.2995 -0.0904 0.0049  0.0308  54   ALA B C   
9402  O O   . ALA B 56   ? 0.3086 0.4277 0.3266 -0.0890 0.0079  0.0319  54   ALA B O   
9403  C CB  . ALA B 56   ? 0.2991 0.4005 0.3111 -0.0807 0.0051  0.0259  54   ALA B CB  
9404  N N   . THR B 57   ? 0.2849 0.3980 0.3032 -0.0947 0.0028  0.0315  55   THR B N   
9405  C CA  . THR B 57   ? 0.3258 0.4511 0.3499 -0.0978 0.0037  0.0338  55   THR B CA  
9406  C C   . THR B 57   ? 0.3394 0.4673 0.3626 -0.1020 0.0054  0.0369  55   THR B C   
9407  O O   . THR B 57   ? 0.3556 0.4749 0.3739 -0.1055 0.0042  0.0379  55   THR B O   
9408  C CB  . THR B 57   ? 0.3441 0.4694 0.3702 -0.1018 0.0005  0.0338  55   THR B CB  
9409  O OG1 . THR B 57   ? 0.3454 0.4699 0.3728 -0.0977 -0.0007 0.0310  55   THR B OG1 
9410  C CG2 . THR B 57   ? 0.3219 0.4598 0.3540 -0.1058 0.0012  0.0364  55   THR B CG2 
9411  N N   . GLN B 58   ? 0.3521 0.4920 0.3799 -0.1014 0.0083  0.0386  56   GLN B N   
9412  C CA  . GLN B 58   ? 0.3177 0.4623 0.3455 -0.1055 0.0103  0.0418  56   GLN B CA  
9413  C C   . GLN B 58   ? 0.3593 0.5175 0.3943 -0.1084 0.0111  0.0439  56   GLN B C   
9414  O O   . GLN B 58   ? 0.3324 0.4979 0.3725 -0.1056 0.0111  0.0427  56   GLN B O   
9415  C CB  . GLN B 58   ? 0.3616 0.5073 0.3872 -0.1015 0.0138  0.0419  56   GLN B CB  
9416  C CG  . GLN B 58   ? 0.3310 0.4647 0.3503 -0.0976 0.0132  0.0395  56   GLN B CG  
9417  C CD  . GLN B 58   ? 0.3882 0.5203 0.4034 -0.0965 0.0158  0.0406  56   GLN B CD  
9418  O OE1 . GLN B 58   ? 0.4451 0.5744 0.4572 -0.1009 0.0158  0.0430  56   GLN B OE1 
9419  N NE2 . GLN B 58   ? 0.3745 0.5083 0.3894 -0.0906 0.0180  0.0388  56   GLN B NE2 
9420  N N   . SER B 59   ? 0.4210 0.5828 0.4564 -0.1141 0.0117  0.0472  57   SER B N   
9421  C CA  . SER B 59   ? 0.3746 0.5496 0.4169 -0.1177 0.0124  0.0497  57   SER B CA  
9422  C C   . SER B 59   ? 0.3919 0.5794 0.4394 -0.1128 0.0162  0.0496  57   SER B C   
9423  O O   . SER B 59   ? 0.3628 0.5488 0.4078 -0.1077 0.0187  0.0484  57   SER B O   
9424  C CB  . SER B 59   ? 0.3843 0.5604 0.4255 -0.1244 0.0130  0.0533  57   SER B CB  
9425  O OG  . SER B 59   ? 0.4215 0.5982 0.4598 -0.1225 0.0165  0.0544  57   SER B OG  
9426  N N   . LYS B 60   ? 0.3598 0.5599 0.4146 -0.1145 0.0165  0.0511  58   LYS B N   
9427  C CA  . LYS B 60   ? 0.4044 0.6173 0.4646 -0.1101 0.0201  0.0513  58   LYS B CA  
9428  C C   . LYS B 60   ? 0.3639 0.5797 0.4221 -0.1099 0.0240  0.0532  58   LYS B C   
9429  O O   . LYS B 60   ? 0.3640 0.5835 0.4225 -0.1042 0.0272  0.0520  58   LYS B O   
9430  C CB  . LYS B 60   ? 0.3620 0.5883 0.4305 -0.1129 0.0197  0.0532  58   LYS B CB  
9431  N N   . GLU B 61   ? 0.3537 0.5677 0.4096 -0.1161 0.0239  0.0561  59   GLU B N   
9432  C CA  . GLU B 61   ? 0.3599 0.5771 0.4137 -0.1165 0.0277  0.0582  59   GLU B CA  
9433  C C   . GLU B 61   ? 0.3735 0.5808 0.4203 -0.1114 0.0288  0.0559  59   GLU B C   
9434  O O   . GLU B 61   ? 0.3828 0.5950 0.4295 -0.1071 0.0325  0.0556  59   GLU B O   
9435  C CB  . GLU B 61   ? 0.4328 0.6479 0.4846 -0.1245 0.0267  0.0616  59   GLU B CB  
9436  N N   . ILE B 62   ? 0.3690 0.5622 0.4099 -0.1117 0.0258  0.0541  60   ILE B N   
9437  C CA  . ILE B 62   ? 0.3632 0.5466 0.3975 -0.1071 0.0265  0.0520  60   ILE B CA  
9438  C C   . ILE B 62   ? 0.3309 0.5170 0.3671 -0.0995 0.0278  0.0488  60   ILE B C   
9439  O O   . ILE B 62   ? 0.3836 0.5685 0.4167 -0.0951 0.0303  0.0478  60   ILE B O   
9440  C CB  . ILE B 62   ? 0.4374 0.6057 0.4656 -0.1092 0.0227  0.0510  60   ILE B CB  
9441  C CG1 . ILE B 62   ? 0.4891 0.6537 0.5140 -0.1162 0.0220  0.0543  60   ILE B CG1 
9442  C CG2 . ILE B 62   ? 0.4616 0.6201 0.4840 -0.1037 0.0229  0.0483  60   ILE B CG2 
9443  C CD1 . ILE B 62   ? 0.4682 0.6184 0.4875 -0.1187 0.0182  0.0536  60   ILE B CD1 
9444  N N   . ARG B 63   ? 0.3235 0.5130 0.3646 -0.0980 0.0261  0.0473  61   ARG B N   
9445  C CA  . ARG B 63   ? 0.3155 0.5074 0.3585 -0.0909 0.0272  0.0444  61   ARG B CA  
9446  C C   . ARG B 63   ? 0.3408 0.5448 0.3875 -0.0878 0.0315  0.0452  61   ARG B C   
9447  O O   . ARG B 63   ? 0.3757 0.5787 0.4205 -0.0820 0.0336  0.0432  61   ARG B O   
9448  C CB  . ARG B 63   ? 0.3534 0.5469 0.4008 -0.0903 0.0244  0.0429  61   ARG B CB  
9449  C CG  . ARG B 63   ? 0.3849 0.5653 0.4278 -0.0915 0.0205  0.0411  61   ARG B CG  
9450  C CD  . ARG B 63   ? 0.4558 0.6372 0.5025 -0.0900 0.0179  0.0393  61   ARG B CD  
9451  N NE  . ARG B 63   ? 0.3955 0.5849 0.4476 -0.0949 0.0164  0.0413  61   ARG B NE  
9452  C CZ  . ARG B 63   ? 0.4658 0.6669 0.5249 -0.0934 0.0172  0.0417  61   ARG B CZ  
9453  N NH1 . ARG B 63   ? 0.4812 0.6874 0.5426 -0.0871 0.0195  0.0402  61   ARG B NH1 
9454  N NH2 . ARG B 63   ? 0.4970 0.7045 0.5606 -0.0983 0.0154  0.0436  61   ARG B NH2 
9455  N N   . ASP B 64   ? 0.3076 0.5231 0.3597 -0.0915 0.0329  0.0481  62   ASP B N   
9456  C CA  . ASP B 64   ? 0.3286 0.5559 0.3841 -0.0886 0.0373  0.0491  62   ASP B CA  
9457  C C   . ASP B 64   ? 0.2593 0.4827 0.3086 -0.0878 0.0401  0.0496  62   ASP B C   
9458  O O   . ASP B 64   ? 0.4019 0.6284 0.4505 -0.0825 0.0433  0.0484  62   ASP B O   
9459  C CB  . ASP B 64   ? 0.3237 0.5642 0.3862 -0.0932 0.0382  0.0524  62   ASP B CB  
9460  C CG  . ASP B 64   ? 0.3990 0.6451 0.4681 -0.0936 0.0356  0.0520  62   ASP B CG  
9461  O OD1 . ASP B 64   ? 0.4272 0.6693 0.4964 -0.0890 0.0341  0.0490  62   ASP B OD1 
9462  O OD2 . ASP B 64   ? 0.4207 0.6755 0.4951 -0.0987 0.0352  0.0548  62   ASP B OD2 
9463  N N   . ALA B 65   ? 0.3039 0.5202 0.3483 -0.0931 0.0390  0.0515  63   ALA B N   
9464  C CA  . ALA B 65   ? 0.3100 0.5222 0.3481 -0.0928 0.0414  0.0523  63   ALA B CA  
9465  C C   . ALA B 65   ? 0.3790 0.5812 0.4114 -0.0869 0.0412  0.0488  63   ALA B C   
9466  O O   . ALA B 65   ? 0.4052 0.6084 0.4347 -0.0833 0.0443  0.0483  63   ALA B O   
9467  C CB  . ALA B 65   ? 0.3422 0.5478 0.3761 -0.0997 0.0397  0.0550  63   ALA B CB  
9468  N N   . ALA B 66   ? 0.3566 0.5492 0.3874 -0.0859 0.0376  0.0465  64   ALA B N   
9469  C CA  . ALA B 66   ? 0.3356 0.5189 0.3615 -0.0804 0.0371  0.0432  64   ALA B CA  
9470  C C   . ALA B 66   ? 0.3421 0.5321 0.3712 -0.0738 0.0395  0.0410  64   ALA B C   
9471  O O   . ALA B 66   ? 0.3776 0.5643 0.4028 -0.0693 0.0412  0.0392  64   ALA B O   
9472  C CB  . ALA B 66   ? 0.3267 0.4991 0.3507 -0.0810 0.0328  0.0414  64   ALA B CB  
9473  N N   . ALA B 67   ? 0.3446 0.5442 0.3810 -0.0732 0.0396  0.0410  65   ALA B N   
9474  C CA  . ALA B 67   ? 0.3248 0.5309 0.3645 -0.0669 0.0419  0.0390  65   ALA B CA  
9475  C C   . ALA B 67   ? 0.3881 0.6014 0.4271 -0.0649 0.0464  0.0400  65   ALA B C   
9476  O O   . ALA B 67   ? 0.3707 0.5840 0.4083 -0.0591 0.0484  0.0377  65   ALA B O   
9477  C CB  . ALA B 67   ? 0.3551 0.5707 0.4029 -0.0671 0.0410  0.0394  65   ALA B CB  
9478  N N   . SER B 68   ? 0.3859 0.6054 0.4257 -0.0697 0.0481  0.0433  66   SER B N   
9479  C CA  A SER B 68   ? 0.3732 0.5995 0.4119 -0.0681 0.0526  0.0444  66   SER B CA  
9480  C CA  B SER B 68   ? 0.3725 0.5988 0.4112 -0.0681 0.0526  0.0444  66   SER B CA  
9481  C C   . SER B 68   ? 0.3955 0.6117 0.4255 -0.0667 0.0532  0.0434  66   SER B C   
9482  O O   . SER B 68   ? 0.3642 0.5824 0.3919 -0.0623 0.0564  0.0422  66   SER B O   
9483  C CB  A SER B 68   ? 0.4421 0.6781 0.4844 -0.0739 0.0542  0.0484  66   SER B CB  
9484  C CB  B SER B 68   ? 0.4431 0.6790 0.4853 -0.0740 0.0541  0.0484  66   SER B CB  
9485  O OG  A SER B 68   ? 0.4296 0.6580 0.4679 -0.0802 0.0518  0.0504  66   SER B OG  
9486  O OG  B SER B 68   ? 0.4647 0.7110 0.5153 -0.0751 0.0537  0.0494  66   SER B OG  
9487  N N   . THR B 69   ? 0.3842 0.5894 0.4091 -0.0705 0.0503  0.0439  67   THR B N   
9488  C CA  . THR B 69   ? 0.3569 0.5521 0.3736 -0.0691 0.0504  0.0430  67   THR B CA  
9489  C C   . THR B 69   ? 0.3596 0.5490 0.3741 -0.0625 0.0500  0.0390  67   THR B C   
9490  O O   . THR B 69   ? 0.3333 0.5205 0.3431 -0.0590 0.0521  0.0378  67   THR B O   
9491  C CB  . THR B 69   ? 0.3570 0.5414 0.3693 -0.0742 0.0469  0.0442  67   THR B CB  
9492  O OG1 . THR B 69   ? 0.3818 0.5706 0.3944 -0.0803 0.0478  0.0480  67   THR B OG1 
9493  C CG2 . THR B 69   ? 0.3536 0.5266 0.3576 -0.0720 0.0464  0.0427  67   THR B CG2 
9494  N N   . ALA B 70   ? 0.3374 0.5243 0.3552 -0.0609 0.0472  0.0370  68   ALA B N   
9495  C CA  . ALA B 70   ? 0.3725 0.5545 0.3889 -0.0547 0.0468  0.0334  68   ALA B CA  
9496  C C   . ALA B 70   ? 0.3560 0.5469 0.3748 -0.0496 0.0506  0.0323  68   ALA B C   
9497  O O   . ALA B 70   ? 0.3548 0.5414 0.3695 -0.0450 0.0517  0.0299  68   ALA B O   
9498  C CB  . ALA B 70   ? 0.3503 0.5292 0.3703 -0.0543 0.0433  0.0318  68   ALA B CB  
9499  N N   . ARG B 71   ? 0.3749 0.5779 0.4001 -0.0504 0.0526  0.0340  69   ARG B N   
9500  C CA  A ARG B 71   ? 0.3935 0.6055 0.4211 -0.0455 0.0565  0.0331  69   ARG B CA  
9501  C CA  B ARG B 71   ? 0.3936 0.6054 0.4212 -0.0454 0.0565  0.0331  69   ARG B CA  
9502  C C   . ARG B 71   ? 0.2895 0.5008 0.3112 -0.0444 0.0598  0.0334  69   ARG B C   
9503  O O   . ARG B 71   ? 0.3770 0.5872 0.3960 -0.0390 0.0617  0.0310  69   ARG B O   
9504  C CB  A ARG B 71   ? 0.3842 0.6100 0.4200 -0.0473 0.0581  0.0355  69   ARG B CB  
9505  C CB  B ARG B 71   ? 0.3844 0.6100 0.4203 -0.0468 0.0580  0.0352  69   ARG B CB  
9506  C CG  A ARG B 71   ? 0.3857 0.6221 0.4238 -0.0432 0.0628  0.0355  69   ARG B CG  
9507  C CG  B ARG B 71   ? 0.3856 0.6214 0.4238 -0.0422 0.0626  0.0349  69   ARG B CG  
9508  C CD  A ARG B 71   ? 0.3799 0.6219 0.4238 -0.0379 0.0631  0.0335  69   ARG B CD  
9509  C CD  B ARG B 71   ? 0.3668 0.6163 0.4141 -0.0426 0.0638  0.0366  69   ARG B CD  
9510  N NE  A ARG B 71   ? 0.3684 0.6169 0.4199 -0.0408 0.0609  0.0350  69   ARG B NE  
9511  N NE  B ARG B 71   ? 0.3687 0.6183 0.4207 -0.0397 0.0614  0.0347  69   ARG B NE  
9512  C CZ  A ARG B 71   ? 0.3875 0.6397 0.4444 -0.0372 0.0600  0.0336  69   ARG B CZ  
9513  C CZ  B ARG B 71   ? 0.4046 0.6546 0.4575 -0.0331 0.0624  0.0320  69   ARG B CZ  
9514  N NH1 A ARG B 71   ? 0.4169 0.6671 0.4728 -0.0306 0.0611  0.0307  69   ARG B NH1 
9515  N NH1 B ARG B 71   ? 0.3328 0.5829 0.3819 -0.0286 0.0658  0.0305  69   ARG B NH1 
9516  N NH2 A ARG B 71   ? 0.3711 0.6290 0.4344 -0.0405 0.0578  0.0352  69   ARG B NH2 
9517  N NH2 B ARG B 71   ? 0.4197 0.6697 0.4769 -0.0310 0.0600  0.0307  69   ARG B NH2 
9518  N N   . LYS B 72   ? 0.3359 0.5474 0.3550 -0.0496 0.0603  0.0363  70   LYS B N   
9519  C CA  . LYS B 72   ? 0.3355 0.5463 0.3485 -0.0492 0.0633  0.0369  70   LYS B CA  
9520  C C   . LYS B 72   ? 0.3866 0.5852 0.3919 -0.0460 0.0620  0.0341  70   LYS B C   
9521  O O   . LYS B 72   ? 0.3891 0.5877 0.3904 -0.0420 0.0647  0.0327  70   LYS B O   
9522  C CB  . LYS B 72   ? 0.3512 0.5629 0.3626 -0.0560 0.0634  0.0408  70   LYS B CB  
9523  C CG  . LYS B 72   ? 0.3898 0.6009 0.3945 -0.0564 0.0664  0.0420  70   LYS B CG  
9524  C CD  . LYS B 72   ? 0.3247 0.5382 0.3291 -0.0635 0.0666  0.0462  70   LYS B CD  
9525  C CE  . LYS B 72   ? 0.4331 0.6451 0.4303 -0.0643 0.0694  0.0476  70   LYS B CE  
9526  N NZ  . LYS B 72   ? 0.4096 0.6319 0.4077 -0.0607 0.0744  0.0475  70   LYS B NZ  
9527  N N   . LEU B 73   ? 0.3695 0.5577 0.3728 -0.0474 0.0579  0.0333  71   LEU B N   
9528  C CA  . LEU B 73   ? 0.3490 0.5258 0.3454 -0.0445 0.0564  0.0307  71   LEU B CA  
9529  C C   . LEU B 73   ? 0.3051 0.4820 0.3024 -0.0379 0.0573  0.0271  71   LEU B C   
9530  O O   . LEU B 73   ? 0.3604 0.5331 0.3522 -0.0344 0.0585  0.0253  71   LEU B O   
9531  C CB  . LEU B 73   ? 0.3217 0.4882 0.3167 -0.0474 0.0519  0.0306  71   LEU B CB  
9532  C CG  . LEU B 73   ? 0.3495 0.5135 0.3425 -0.0538 0.0506  0.0339  71   LEU B CG  
9533  C CD1 . LEU B 73   ? 0.3239 0.4787 0.3167 -0.0561 0.0461  0.0334  71   LEU B CD1 
9534  C CD2 . LEU B 73   ? 0.3664 0.5260 0.3518 -0.0545 0.0520  0.0348  71   LEU B CD2 
9535  N N   . ILE B 74   ? 0.3387 0.5206 0.3427 -0.0361 0.0566  0.0262  72   ILE B N   
9536  C CA  . ILE B 74   ? 0.3455 0.5264 0.3504 -0.0300 0.0569  0.0229  72   ILE B CA  
9537  C C   . ILE B 74   ? 0.4643 0.6527 0.4691 -0.0258 0.0613  0.0222  72   ILE B C   
9538  O O   . ILE B 74   ? 0.4081 0.5922 0.4089 -0.0211 0.0621  0.0195  72   ILE B O   
9539  C CB  . ILE B 74   ? 0.3670 0.5508 0.3790 -0.0295 0.0547  0.0224  72   ILE B CB  
9540  C CG1 . ILE B 74   ? 0.4041 0.5782 0.4148 -0.0324 0.0503  0.0221  72   ILE B CG1 
9541  C CG2 . ILE B 74   ? 0.3657 0.5505 0.3794 -0.0231 0.0556  0.0193  72   ILE B CG2 
9542  C CD1 . ILE B 74   ? 0.3672 0.5442 0.3844 -0.0334 0.0480  0.0223  72   ILE B CD1 
9543  N N   . GLU B 75   ? 0.4443 0.6439 0.4533 -0.0275 0.0641  0.0246  73   GLU B N   
9544  C CA  . GLU B 75   ? 0.4613 0.6684 0.4698 -0.0238 0.0687  0.0242  73   GLU B CA  
9545  C C   . GLU B 75   ? 0.4325 0.6335 0.4323 -0.0233 0.0701  0.0237  73   GLU B C   
9546  O O   . GLU B 75   ? 0.4953 0.6955 0.4918 -0.0183 0.0724  0.0213  73   GLU B O   
9547  C CB  . GLU B 75   ? 0.4634 0.6838 0.4781 -0.0265 0.0714  0.0274  73   GLU B CB  
9548  C CG  . GLU B 75   ? 0.4958 0.7235 0.5195 -0.0262 0.0702  0.0277  73   GLU B CG  
9549  C CD  . GLU B 75   ? 0.5027 0.7440 0.5328 -0.0292 0.0726  0.0310  73   GLU B CD  
9550  O OE1 . GLU B 75   ? 0.5697 0.8133 0.5974 -0.0333 0.0743  0.0336  73   GLU B OE1 
9551  O OE2 . GLU B 75   ? 0.4813 0.7310 0.5189 -0.0274 0.0729  0.0311  73   GLU B OE2 
9552  N N   . ALA B 76   ? 0.3809 0.5768 0.3765 -0.0284 0.0687  0.0258  74   ALA B N   
9553  C CA  . ALA B 76   ? 0.3856 0.5744 0.3724 -0.0282 0.0694  0.0253  74   ALA B CA  
9554  C C   . ALA B 76   ? 0.4130 0.5913 0.3951 -0.0239 0.0674  0.0216  74   ALA B C   
9555  O O   . ALA B 76   ? 0.4511 0.6266 0.4274 -0.0207 0.0692  0.0199  74   ALA B O   
9556  C CB  . ALA B 76   ? 0.4289 0.6132 0.4124 -0.0345 0.0676  0.0283  74   ALA B CB  
9557  N N   . LEU B 77   ? 0.3720 0.5443 0.3565 -0.0239 0.0635  0.0204  75   LEU B N   
9558  C CA  . LEU B 77   ? 0.4366 0.5994 0.4174 -0.0201 0.0614  0.0170  75   LEU B CA  
9559  C C   . LEU B 77   ? 0.4063 0.5725 0.3883 -0.0139 0.0638  0.0142  75   LEU B C   
9560  O O   . LEU B 77   ? 0.4823 0.6433 0.4588 -0.0104 0.0644  0.0118  75   LEU B O   
9561  C CB  . LEU B 77   ? 0.3692 0.5260 0.3530 -0.0216 0.0571  0.0165  75   LEU B CB  
9562  C CG  . LEU B 77   ? 0.4295 0.5785 0.4100 -0.0265 0.0540  0.0183  75   LEU B CG  
9563  C CD1 . LEU B 77   ? 0.3712 0.5158 0.3555 -0.0275 0.0502  0.0177  75   LEU B CD1 
9564  C CD2 . LEU B 77   ? 0.4319 0.5718 0.4043 -0.0254 0.0533  0.0170  75   LEU B CD2 
9565  N N   . ARG B 78   ? 0.4153 0.5901 0.4047 -0.0124 0.0649  0.0144  76   ARG B N   
9566  C CA  . ARG B 78   ? 0.4008 0.5786 0.3918 -0.0064 0.0669  0.0117  76   ARG B CA  
9567  C C   . ARG B 78   ? 0.4069 0.5907 0.3951 -0.0038 0.0715  0.0115  76   ARG B C   
9568  O O   . ARG B 78   ? 0.4598 0.6441 0.4473 0.0016  0.0733  0.0089  76   ARG B O   
9569  C CB  . ARG B 78   ? 0.4426 0.6282 0.4425 -0.0055 0.0666  0.0121  76   ARG B CB  
9570  C CG  . ARG B 78   ? 0.4150 0.5946 0.4174 -0.0073 0.0622  0.0118  76   ARG B CG  
9571  C CD  . ARG B 78   ? 0.4837 0.6705 0.4943 -0.0061 0.0619  0.0121  76   ARG B CD  
9572  N NE  . ARG B 78   ? 0.4303 0.6101 0.4416 -0.0038 0.0587  0.0098  76   ARG B NE  
9573  C CZ  . ARG B 78   ? 0.4892 0.6726 0.5068 -0.0028 0.0574  0.0097  76   ARG B CZ  
9574  N NH1 . ARG B 78   ? 0.4841 0.6783 0.5082 -0.0039 0.0587  0.0117  76   ARG B NH1 
9575  N NH2 . ARG B 78   ? 0.4768 0.6531 0.4941 -0.0006 0.0547  0.0075  76   ARG B NH2 
9576  N N   . GLY B 79   ? 0.4362 0.6243 0.4226 -0.0075 0.0735  0.0143  77   GLY B N   
9577  C CA  . GLY B 79   ? 0.4528 0.6468 0.4363 -0.0052 0.0781  0.0143  77   GLY B CA  
9578  C C   . GLY B 79   ? 0.5325 0.7180 0.5064 -0.0035 0.0786  0.0124  77   GLY B C   
9579  O O   . GLY B 79   ? 0.4553 0.6449 0.4260 -0.0008 0.0824  0.0118  77   GLY B O   
9580  N N   . LYS B 80   ? 0.5289 0.7032 0.4983 -0.0047 0.0748  0.0113  78   LYS B N   
9581  C CA  . LYS B 80   ? 0.5079 0.6740 0.4680 -0.0039 0.0748  0.0099  78   LYS B CA  
9582  C C   . LYS B 80   ? 0.4739 0.6296 0.4308 -0.0005 0.0719  0.0063  78   LYS B C   
9583  O O   . LYS B 80   ? 0.5253 0.6787 0.4869 0.0003  0.0692  0.0053  78   LYS B O   
9584  C CB  . LYS B 80   ? 0.5540 0.7166 0.5101 -0.0096 0.0734  0.0128  78   LYS B CB  
9585  C CG  . LYS B 80   ? 0.4725 0.6290 0.4310 -0.0134 0.0688  0.0139  78   LYS B CG  
9586  C CD  . LYS B 80   ? 0.4584 0.6140 0.4145 -0.0194 0.0681  0.0175  78   LYS B CD  
9587  C CE  . LYS B 80   ? 0.3916 0.5391 0.3486 -0.0227 0.0633  0.0181  78   LYS B CE  
9588  N NZ  . LYS B 80   ? 0.4266 0.5733 0.3817 -0.0286 0.0625  0.0218  78   LYS B NZ  
9589  N N   . GLY B 85   ? 0.5581 0.6397 0.4807 0.0161  0.0522  -0.0157 83   GLY B N   
9590  C CA  . GLY B 85   ? 0.5105 0.5857 0.4254 0.0184  0.0519  -0.0184 83   GLY B CA  
9591  C C   . GLY B 85   ? 0.4940 0.5642 0.4099 0.0220  0.0505  -0.0216 83   GLY B C   
9592  O O   . GLY B 85   ? 0.4846 0.5530 0.3964 0.0255  0.0520  -0.0243 83   GLY B O   
9593  N N   . VAL B 86   ? 0.5124 0.5803 0.4336 0.0210  0.0475  -0.0214 84   VAL B N   
9594  C CA  . VAL B 86   ? 0.5217 0.5851 0.4444 0.0241  0.0460  -0.0241 84   VAL B CA  
9595  C C   . VAL B 86   ? 0.4685 0.5373 0.3946 0.0281  0.0491  -0.0253 84   VAL B C   
9596  O O   . VAL B 86   ? 0.4431 0.5084 0.3669 0.0317  0.0495  -0.0282 84   VAL B O   
9597  C CB  . VAL B 86   ? 0.5047 0.5650 0.4325 0.0220  0.0423  -0.0232 84   VAL B CB  
9598  C CG1 . VAL B 86   ? 0.5233 0.5810 0.4542 0.0252  0.0414  -0.0255 84   VAL B CG1 
9599  C CG2 . VAL B 86   ? 0.5755 0.6288 0.4990 0.0194  0.0390  -0.0230 84   VAL B CG2 
9600  N N   . GLU B 87   ? 0.4926 0.5701 0.4243 0.0274  0.0513  -0.0232 85   GLU B N   
9601  C CA  . GLU B 87   ? 0.5034 0.5869 0.4388 0.0313  0.0543  -0.0241 85   GLU B CA  
9602  C C   . GLU B 87   ? 0.4475 0.5312 0.3768 0.0346  0.0575  -0.0261 85   GLU B C   
9603  O O   . GLU B 87   ? 0.4645 0.5478 0.3939 0.0390  0.0589  -0.0285 85   GLU B O   
9604  C CB  . GLU B 87   ? 0.5810 0.6744 0.5231 0.0294  0.0561  -0.0211 85   GLU B CB  
9605  N N   . GLY B 88   ? 0.4410 0.5252 0.3646 0.0327  0.0588  -0.0252 86   GLY B N   
9606  C CA  . GLY B 88   ? 0.4622 0.5463 0.3793 0.0358  0.0619  -0.0272 86   GLY B CA  
9607  C C   . GLY B 88   ? 0.4075 0.4819 0.3184 0.0383  0.0601  -0.0307 86   GLY B C   
9608  O O   . GLY B 88   ? 0.4389 0.5125 0.3464 0.0425  0.0623  -0.0334 86   GLY B O   
9609  N N   . LEU B 89   ? 0.4234 0.4902 0.3329 0.0359  0.0559  -0.0309 87   LEU B N   
9610  C CA  . LEU B 89   ? 0.4274 0.4849 0.3317 0.0378  0.0537  -0.0341 87   LEU B CA  
9611  C C   . LEU B 89   ? 0.3753 0.4316 0.2838 0.0416  0.0536  -0.0362 87   LEU B C   
9612  O O   . LEU B 89   ? 0.3658 0.4180 0.2700 0.0452  0.0544  -0.0392 87   LEU B O   
9613  C CB  . LEU B 89   ? 0.4549 0.5058 0.3578 0.0341  0.0493  -0.0334 87   LEU B CB  
9614  C CG  . LEU B 89   ? 0.4786 0.5199 0.3777 0.0352  0.0462  -0.0362 87   LEU B CG  
9615  C CD1 . LEU B 89   ? 0.5442 0.5815 0.4342 0.0373  0.0475  -0.0388 87   LEU B CD1 
9616  C CD2 . LEU B 89   ? 0.5351 0.5716 0.4345 0.0313  0.0419  -0.0348 87   LEU B CD2 
9617  N N   . VAL B 90   ? 0.3971 0.4569 0.3137 0.0408  0.0526  -0.0346 88   VAL B N   
9618  C CA  . VAL B 90   ? 0.4111 0.4704 0.3322 0.0442  0.0525  -0.0361 88   VAL B CA  
9619  C C   . VAL B 90   ? 0.4431 0.5074 0.3640 0.0487  0.0567  -0.0374 88   VAL B C   
9620  O O   . VAL B 90   ? 0.4163 0.4768 0.3359 0.0527  0.0570  -0.0401 88   VAL B O   
9621  C CB  . VAL B 90   ? 0.4342 0.4974 0.3639 0.0421  0.0508  -0.0337 88   VAL B CB  
9622  C CG1 . VAL B 90   ? 0.4495 0.5136 0.3842 0.0458  0.0512  -0.0349 88   VAL B CG1 
9623  C CG2 . VAL B 90   ? 0.3930 0.4501 0.3226 0.0384  0.0466  -0.0330 88   VAL B CG2 
9624  N N   . GLN B 91   ? 0.4270 0.4999 0.3491 0.0482  0.0599  -0.0355 89   GLN B N   
9625  C CA  . GLN B 91   ? 0.4769 0.5555 0.3992 0.0526  0.0642  -0.0366 89   GLN B CA  
9626  C C   . GLN B 91   ? 0.4435 0.5165 0.3568 0.0556  0.0657  -0.0398 89   GLN B C   
9627  O O   . GLN B 91   ? 0.4699 0.5419 0.3822 0.0603  0.0675  -0.0423 89   GLN B O   
9628  C CB  . GLN B 91   ? 0.5446 0.6341 0.4705 0.0509  0.0673  -0.0336 89   GLN B CB  
9629  N N   . GLU B 92   ? 0.4331 0.5020 0.3394 0.0529  0.0648  -0.0398 90   GLU B N   
9630  C CA  . GLU B 92   ? 0.4442 0.5083 0.3413 0.0554  0.0664  -0.0426 90   GLU B CA  
9631  C C   . GLU B 92   ? 0.4085 0.4628 0.3022 0.0582  0.0642  -0.0462 90   GLU B C   
9632  O O   . GLU B 92   ? 0.4352 0.4870 0.3240 0.0624  0.0663  -0.0491 90   GLU B O   
9633  C CB  . GLU B 92   ? 0.4820 0.5435 0.3723 0.0516  0.0655  -0.0417 90   GLU B CB  
9634  C CG  . GLU B 92   ? 0.4850 0.5410 0.3651 0.0540  0.0668  -0.0447 90   GLU B CG  
9635  C CD  . GLU B 92   ? 0.5282 0.5818 0.4013 0.0503  0.0659  -0.0437 90   GLU B CD  
9636  O OE1 . GLU B 92   ? 0.5975 0.6524 0.4733 0.0458  0.0638  -0.0407 90   GLU B OE1 
9637  O OE2 . GLU B 92   ? 0.5138 0.5637 0.3783 0.0520  0.0673  -0.0460 90   GLU B OE2 
9638  N N   . TYR B 93   ? 0.3937 0.4423 0.2898 0.0560  0.0599  -0.0461 91   TYR B N   
9639  C CA  . TYR B 93   ? 0.4302 0.4692 0.3231 0.0581  0.0575  -0.0492 91   TYR B CA  
9640  C C   . TYR B 93   ? 0.3984 0.4378 0.2984 0.0605  0.0568  -0.0496 91   TYR B C   
9641  O O   . TYR B 93   ? 0.3982 0.4297 0.2968 0.0617  0.0544  -0.0517 91   TYR B O   
9642  C CB  . TYR B 93   ? 0.3931 0.4243 0.2824 0.0542  0.0531  -0.0492 91   TYR B CB  
9643  C CG  . TYR B 93   ? 0.3844 0.4134 0.2650 0.0528  0.0536  -0.0498 91   TYR B CG  
9644  C CD1 . TYR B 93   ? 0.3728 0.3953 0.2451 0.0554  0.0541  -0.0532 91   TYR B CD1 
9645  C CD2 . TYR B 93   ? 0.4083 0.4418 0.2889 0.0490  0.0538  -0.0468 91   TYR B CD2 
9646  C CE1 . TYR B 93   ? 0.3775 0.3980 0.2414 0.0542  0.0546  -0.0537 91   TYR B CE1 
9647  C CE2 . TYR B 93   ? 0.4329 0.4644 0.3052 0.0478  0.0543  -0.0471 91   TYR B CE2 
9648  C CZ  . TYR B 93   ? 0.4132 0.4384 0.2772 0.0504  0.0547  -0.0506 91   TYR B CZ  
9649  O OH  . TYR B 93   ? 0.4678 0.4909 0.3232 0.0492  0.0552  -0.0509 91   TYR B OH  
9650  N N   . SER B 94   ? 0.3484 0.3969 0.2559 0.0613  0.0590  -0.0474 92   SER B N   
9651  C CA  . SER B 94   ? 0.3577 0.4075 0.2720 0.0638  0.0587  -0.0475 92   SER B CA  
9652  C C   . SER B 94   ? 0.3512 0.3945 0.2679 0.0614  0.0542  -0.0473 92   SER B C   
9653  O O   . SER B 94   ? 0.3555 0.3934 0.2728 0.0638  0.0528  -0.0492 92   SER B O   
9654  C CB  . SER B 94   ? 0.3604 0.4078 0.2720 0.0696  0.0610  -0.0506 92   SER B CB  
9655  O OG  . SER B 94   ? 0.4153 0.4692 0.3249 0.0720  0.0654  -0.0508 92   SER B OG  
9656  N N   . LEU B 95   ? 0.3079 0.3517 0.2260 0.0566  0.0519  -0.0450 93   LEU B N   
9657  C CA  . LEU B 95   ? 0.2988 0.3370 0.2191 0.0540  0.0477  -0.0447 93   LEU B CA  
9658  C C   . LEU B 95   ? 0.3259 0.3686 0.2549 0.0541  0.0471  -0.0429 93   LEU B C   
9659  O O   . LEU B 95   ? 0.3380 0.3893 0.2722 0.0536  0.0490  -0.0407 93   LEU B O   
9660  C CB  . LEU B 95   ? 0.3264 0.3635 0.2449 0.0491  0.0455  -0.0429 93   LEU B CB  
9661  C CG  . LEU B 95   ? 0.3325 0.3652 0.2421 0.0483  0.0456  -0.0442 93   LEU B CG  
9662  C CD1 . LEU B 95   ? 0.3407 0.3717 0.2495 0.0435  0.0427  -0.0422 93   LEU B CD1 
9663  C CD2 . LEU B 95   ? 0.3388 0.3627 0.2428 0.0509  0.0444  -0.0477 93   LEU B CD2 
9664  N N   . SER B 96   ? 0.2835 0.3204 0.2143 0.0546  0.0444  -0.0439 94   SER B N   
9665  C CA  . SER B 96   ? 0.2887 0.3287 0.2272 0.0535  0.0430  -0.0419 94   SER B CA  
9666  C C   . SER B 96   ? 0.3026 0.3432 0.2428 0.0484  0.0406  -0.0396 94   SER B C   
9667  O O   . SER B 96   ? 0.2783 0.3157 0.2136 0.0460  0.0396  -0.0397 94   SER B O   
9668  C CB  . SER B 96   ? 0.2852 0.3181 0.2243 0.0552  0.0407  -0.0436 94   SER B CB  
9669  O OG  . SER B 96   ? 0.2647 0.2899 0.1999 0.0525  0.0375  -0.0444 94   SER B OG  
9670  N N   . SER B 97   ? 0.2734 0.3180 0.2204 0.0469  0.0396  -0.0374 95   SER B N   
9671  C CA  . SER B 97   ? 0.2823 0.3271 0.2311 0.0423  0.0373  -0.0353 95   SER B CA  
9672  C C   . SER B 97   ? 0.2749 0.3109 0.2201 0.0406  0.0340  -0.0365 95   SER B C   
9673  O O   . SER B 97   ? 0.2656 0.2999 0.2078 0.0376  0.0327  -0.0357 95   SER B O   
9674  C CB  . SER B 97   ? 0.3159 0.3653 0.2723 0.0413  0.0365  -0.0332 95   SER B CB  
9675  O OG  . SER B 97   ? 0.3812 0.4394 0.3412 0.0423  0.0394  -0.0319 95   SER B OG  
9676  N N   . GLN B 98   ? 0.2631 0.2937 0.2085 0.0425  0.0325  -0.0382 96   GLN B N   
9677  C CA  . GLN B 98   ? 0.2488 0.2714 0.1911 0.0409  0.0293  -0.0392 96   GLN B CA  
9678  C C   . GLN B 98   ? 0.2413 0.2595 0.1759 0.0408  0.0294  -0.0409 96   GLN B C   
9679  O O   . GLN B 98   ? 0.2583 0.2723 0.1903 0.0380  0.0269  -0.0408 96   GLN B O   
9680  C CB  . GLN B 98   ? 0.2564 0.2740 0.2001 0.0431  0.0280  -0.0408 96   GLN B CB  
9681  C CG  . GLN B 98   ? 0.2451 0.2652 0.1958 0.0423  0.0268  -0.0391 96   GLN B CG  
9682  C CD  . GLN B 98   ? 0.2624 0.2817 0.2150 0.0383  0.0242  -0.0374 96   GLN B CD  
9683  O OE1 . GLN B 98   ? 0.3116 0.3355 0.2657 0.0359  0.0246  -0.0354 96   GLN B OE1 
9684  N NE2 . GLN B 98   ? 0.2713 0.2845 0.2237 0.0375  0.0215  -0.0381 96   GLN B NE2 
9685  N N   . GLU B 99   ? 0.2498 0.2689 0.1807 0.0438  0.0321  -0.0425 97   GLU B N   
9686  C CA  . GLU B 99   ? 0.2653 0.2807 0.1885 0.0437  0.0324  -0.0441 97   GLU B CA  
9687  C C   . GLU B 99   ? 0.2996 0.3186 0.2214 0.0404  0.0327  -0.0419 97   GLU B C   
9688  O O   . GLU B 99   ? 0.2845 0.2992 0.2013 0.0384  0.0309  -0.0423 97   GLU B O   
9689  C CB  . GLU B 99   ? 0.2772 0.2932 0.1968 0.0479  0.0356  -0.0462 97   GLU B CB  
9690  C CG  . GLU B 99   ? 0.2767 0.2864 0.1951 0.0511  0.0349  -0.0488 97   GLU B CG  
9691  C CD  . GLU B 99   ? 0.2824 0.2937 0.1987 0.0557  0.0384  -0.0507 97   GLU B CD  
9692  O OE1 . GLU B 99   ? 0.3158 0.3336 0.2317 0.0566  0.0416  -0.0499 97   GLU B OE1 
9693  O OE2 . GLU B 99   ? 0.2983 0.3040 0.2130 0.0586  0.0380  -0.0530 97   GLU B OE2 
9694  N N   . GLY B 100  ? 0.2632 0.2902 0.1895 0.0398  0.0347  -0.0396 98   GLY B N   
9695  C CA  . GLY B 100  ? 0.2771 0.3075 0.2026 0.0364  0.0348  -0.0373 98   GLY B CA  
9696  C C   . GLY B 100  ? 0.2815 0.3082 0.2080 0.0327  0.0312  -0.0361 98   GLY B C   
9697  O O   . GLY B 100  ? 0.2718 0.2964 0.1942 0.0303  0.0300  -0.0355 98   GLY B O   
9698  N N   . VAL B 101  ? 0.2582 0.2840 0.1902 0.0323  0.0293  -0.0356 99   VAL B N   
9699  C CA  . VAL B 101  ? 0.2464 0.2689 0.1799 0.0291  0.0259  -0.0345 99   VAL B CA  
9700  C C   . VAL B 101  ? 0.2629 0.2776 0.1908 0.0288  0.0235  -0.0363 99   VAL B C   
9701  O O   . VAL B 101  ? 0.2728 0.2852 0.1983 0.0262  0.0215  -0.0355 99   VAL B O   
9702  C CB  . VAL B 101  ? 0.2577 0.2809 0.1980 0.0291  0.0246  -0.0338 99   VAL B CB  
9703  C CG1 . VAL B 101  ? 0.2838 0.3030 0.2252 0.0262  0.0212  -0.0329 99   VAL B CG1 
9704  C CG2 . VAL B 101  ? 0.2638 0.2947 0.2094 0.0288  0.0266  -0.0317 99   VAL B CG2 
9705  N N   . ALA B 102  ? 0.2503 0.2609 0.1762 0.0316  0.0235  -0.0389 100  ALA B N   
9706  C CA  . ALA B 102  ? 0.2646 0.2677 0.1855 0.0313  0.0210  -0.0408 100  ALA B CA  
9707  C C   . ALA B 102  ? 0.2718 0.2738 0.1857 0.0304  0.0214  -0.0411 100  ALA B C   
9708  O O   . ALA B 102  ? 0.2757 0.2733 0.1863 0.0282  0.0187  -0.0411 100  ALA B O   
9709  C CB  . ALA B 102  ? 0.2663 0.2652 0.1856 0.0346  0.0213  -0.0435 100  ALA B CB  
9710  N N   . LEU B 103  ? 0.2627 0.2687 0.1741 0.0320  0.0247  -0.0413 101  LEU B N   
9711  C CA  . LEU B 103  ? 0.2639 0.2691 0.1683 0.0312  0.0254  -0.0415 101  LEU B CA  
9712  C C   . LEU B 103  ? 0.2971 0.3040 0.2020 0.0274  0.0239  -0.0387 101  LEU B C   
9713  O O   . LEU B 103  ? 0.2952 0.2984 0.1946 0.0258  0.0222  -0.0389 101  LEU B O   
9714  C CB  . LEU B 103  ? 0.2751 0.2856 0.1778 0.0337  0.0297  -0.0418 101  LEU B CB  
9715  C CG  . LEU B 103  ? 0.2751 0.2860 0.1707 0.0329  0.0310  -0.0418 101  LEU B CG  
9716  C CD1 . LEU B 103  ? 0.3456 0.3487 0.2335 0.0337  0.0294  -0.0446 101  LEU B CD1 
9717  C CD2 . LEU B 103  ? 0.3060 0.3234 0.2013 0.0353  0.0355  -0.0417 101  LEU B CD2 
9718  N N   . MET B 104  ? 0.2760 0.2883 0.1870 0.0260  0.0245  -0.0362 102  MET B N   
9719  C CA  . MET B 104  ? 0.3063 0.3198 0.2178 0.0224  0.0231  -0.0336 102  MET B CA  
9720  C C   . MET B 104  ? 0.2888 0.2968 0.2006 0.0205  0.0191  -0.0335 102  MET B C   
9721  O O   . MET B 104  ? 0.3046 0.3107 0.2134 0.0181  0.0173  -0.0323 102  MET B O   
9722  C CB  . MET B 104  ? 0.3161 0.3365 0.2341 0.0213  0.0246  -0.0310 102  MET B CB  
9723  C CG  . MET B 104  ? 0.3234 0.3501 0.2411 0.0228  0.0286  -0.0307 102  MET B CG  
9724  S SD  . MET B 104  ? 0.4345 0.4614 0.3437 0.0223  0.0304  -0.0306 102  MET B SD  
9725  C CE  . MET B 104  ? 0.5426 0.5713 0.4532 0.0177  0.0289  -0.0269 102  MET B CE  
9726  N N   . CYS B 105  ? 0.2608 0.2661 0.1763 0.0215  0.0175  -0.0347 103  CYS B N   
9727  C CA  . CYS B 105  ? 0.2828 0.2830 0.1986 0.0199  0.0138  -0.0349 103  CYS B CA  
9728  C C   . CYS B 105  ? 0.2858 0.2805 0.1944 0.0199  0.0122  -0.0366 103  CYS B C   
9729  O O   . CYS B 105  ? 0.3106 0.3024 0.2174 0.0177  0.0095  -0.0358 103  CYS B O   
9730  C CB  . CYS B 105  ? 0.2609 0.2592 0.1814 0.0213  0.0128  -0.0360 103  CYS B CB  
9731  S SG  . CYS B 105  ? 0.2781 0.2818 0.2072 0.0208  0.0135  -0.0338 103  CYS B SG  
9732  N N   . LEU B 106  ? 0.2794 0.2723 0.1837 0.0224  0.0138  -0.0391 104  LEU B N   
9733  C CA  . LEU B 106  ? 0.2807 0.2684 0.1774 0.0224  0.0125  -0.0409 104  LEU B CA  
9734  C C   . LEU B 106  ? 0.2875 0.2768 0.1797 0.0205  0.0129  -0.0393 104  LEU B C   
9735  O O   . LEU B 106  ? 0.3249 0.3102 0.2129 0.0188  0.0102  -0.0393 104  LEU B O   
9736  C CB  . LEU B 106  ? 0.2982 0.2840 0.1908 0.0257  0.0147  -0.0438 104  LEU B CB  
9737  C CG  . LEU B 106  ? 0.3020 0.2827 0.1856 0.0258  0.0139  -0.0458 104  LEU B CG  
9738  C CD1 . LEU B 106  ? 0.3584 0.3327 0.2411 0.0243  0.0096  -0.0469 104  LEU B CD1 
9739  C CD2 . LEU B 106  ? 0.3475 0.3272 0.2267 0.0293  0.0167  -0.0486 104  LEU B CD2 
9740  N N   . ALA B 107  ? 0.2912 0.2862 0.1839 0.0207  0.0160  -0.0378 105  ALA B N   
9741  C CA  . ALA B 107  ? 0.3141 0.3108 0.2025 0.0188  0.0166  -0.0360 105  ALA B CA  
9742  C C   . ALA B 107  ? 0.3281 0.3239 0.2188 0.0156  0.0135  -0.0335 105  ALA B C   
9743  O O   . ALA B 107  ? 0.3434 0.3366 0.2291 0.0139  0.0117  -0.0330 105  ALA B O   
9744  C CB  . ALA B 107  ? 0.3206 0.3242 0.2106 0.0194  0.0205  -0.0346 105  ALA B CB  
9745  N N   . GLU B 108  ? 0.3279 0.3258 0.2260 0.0148  0.0127  -0.0321 106  GLU B N   
9746  C CA  . GLU B 108  ? 0.3321 0.3290 0.2328 0.0120  0.0098  -0.0299 106  GLU B CA  
9747  C C   . GLU B 108  ? 0.3839 0.3748 0.2815 0.0114  0.0061  -0.0310 106  GLU B C   
9748  O O   . GLU B 108  ? 0.3865 0.3757 0.2816 0.0093  0.0040  -0.0295 106  GLU B O   
9749  C CB  . GLU B 108  ? 0.3509 0.3503 0.2598 0.0118  0.0096  -0.0289 106  GLU B CB  
9750  C CG  . GLU B 108  ? 0.3991 0.3966 0.3113 0.0095  0.0064  -0.0271 106  GLU B CG  
9751  C CD  . GLU B 108  ? 0.4351 0.4338 0.3548 0.0098  0.0059  -0.0269 106  GLU B CD  
9752  O OE1 . GLU B 108  ? 0.3835 0.3854 0.3063 0.0114  0.0082  -0.0275 106  GLU B OE1 
9753  O OE2 . GLU B 108  ? 0.4418 0.4383 0.3642 0.0086  0.0032  -0.0261 106  GLU B OE2 
9754  N N   . ALA B 109  ? 0.3330 0.3205 0.2308 0.0130  0.0052  -0.0335 107  ALA B N   
9755  C CA  . ALA B 109  ? 0.3511 0.3332 0.2463 0.0123  0.0016  -0.0346 107  ALA B CA  
9756  C C   . ALA B 109  ? 0.3693 0.3487 0.2560 0.0118  0.0012  -0.0353 107  ALA B C   
9757  O O   . ALA B 109  ? 0.3823 0.3590 0.2668 0.0100  -0.0019 -0.0345 107  ALA B O   
9758  C CB  . ALA B 109  ? 0.3552 0.3342 0.2521 0.0140  0.0010  -0.0371 107  ALA B CB  
9759  N N   . LEU B 110  ? 0.3502 0.3306 0.2322 0.0136  0.0041  -0.0367 108  LEU B N   
9760  C CA  . LEU B 110  ? 0.3472 0.3251 0.2206 0.0133  0.0039  -0.0375 108  LEU B CA  
9761  C C   . LEU B 110  ? 0.3531 0.3329 0.2246 0.0109  0.0035  -0.0345 108  LEU B C   
9762  O O   . LEU B 110  ? 0.4135 0.3902 0.2789 0.0097  0.0015  -0.0344 108  LEU B O   
9763  C CB  . LEU B 110  ? 0.3416 0.3206 0.2105 0.0159  0.0076  -0.0395 108  LEU B CB  
9764  C CG  . LEU B 110  ? 0.3413 0.3164 0.2095 0.0183  0.0076  -0.0429 108  LEU B CG  
9765  C CD1 . LEU B 110  ? 0.3450 0.3225 0.2109 0.0213  0.0118  -0.0444 108  LEU B CD1 
9766  C CD2 . LEU B 110  ? 0.3890 0.3574 0.2506 0.0177  0.0044  -0.0449 108  LEU B CD2 
9767  N N   . LEU B 111  ? 0.3687 0.3534 0.2453 0.0101  0.0051  -0.0320 109  LEU B N   
9768  C CA  . LEU B 111  ? 0.4293 0.4156 0.3045 0.0077  0.0047  -0.0290 109  LEU B CA  
9769  C C   . LEU B 111  ? 0.4663 0.4498 0.3437 0.0056  0.0006  -0.0274 109  LEU B C   
9770  O O   . LEU B 111  ? 0.5010 0.4845 0.3760 0.0037  -0.0005 -0.0251 109  LEU B O   
9771  C CB  . LEU B 111  ? 0.4300 0.4223 0.3097 0.0073  0.0078  -0.0268 109  LEU B CB  
9772  C CG  . LEU B 111  ? 0.4067 0.4026 0.2833 0.0090  0.0120  -0.0277 109  LEU B CG  
9773  C CD1 . LEU B 111  ? 0.4316 0.4337 0.3141 0.0087  0.0147  -0.0257 109  LEU B CD1 
9774  C CD2 . LEU B 111  ? 0.4446 0.4396 0.3127 0.0082  0.0126  -0.0272 109  LEU B CD2 
9775  N N   . ARG B 112  ? 0.4147 0.3960 0.2965 0.0060  -0.0017 -0.0285 110  ARG B N   
9776  C CA  . ARG B 112  ? 0.4558 0.4342 0.3392 0.0043  -0.0058 -0.0275 110  ARG B CA  
9777  C C   . ARG B 112  ? 0.4645 0.4385 0.3407 0.0038  -0.0084 -0.0285 110  ARG B C   
9778  O O   . ARG B 112  ? 0.5180 0.4901 0.3944 0.0023  -0.0117 -0.0272 110  ARG B O   
9779  C CB  . ARG B 112  ? 0.4639 0.4417 0.3544 0.0048  -0.0073 -0.0283 110  ARG B CB  
9780  C CG  . ARG B 112  ? 0.4637 0.4456 0.3613 0.0050  -0.0052 -0.0269 110  ARG B CG  
9781  C CD  . ARG B 112  ? 0.5738 0.5549 0.4781 0.0051  -0.0071 -0.0272 110  ARG B CD  
9782  N NE  . ARG B 112  ? 0.5435 0.5236 0.4491 0.0070  -0.0064 -0.0298 110  ARG B NE  
9783  C CZ  . ARG B 112  ? 0.5510 0.5338 0.4608 0.0084  -0.0040 -0.0302 110  ARG B CZ  
9784  N NH1 . ARG B 112  ? 0.6038 0.5908 0.5171 0.0080  -0.0020 -0.0284 110  ARG B NH1 
9785  N NH2 . ARG B 112  ? 0.5914 0.5725 0.5019 0.0101  -0.0037 -0.0325 110  ARG B NH2 
9786  N N   . ILE B 113  ? 0.4310 0.4036 0.3011 0.0052  -0.0070 -0.0308 111  ILE B N   
9787  C CA  . ILE B 113  ? 0.4633 0.4318 0.3255 0.0045  -0.0092 -0.0318 111  ILE B CA  
9788  C C   . ILE B 113  ? 0.4974 0.4677 0.3547 0.0033  -0.0081 -0.0295 111  ILE B C   
9789  O O   . ILE B 113  ? 0.5214 0.4942 0.3758 0.0042  -0.0044 -0.0296 111  ILE B O   
9790  C CB  . ILE B 113  ? 0.4527 0.4185 0.3097 0.0065  -0.0080 -0.0353 111  ILE B CB  
9791  C CG1 . ILE B 113  ? 0.4656 0.4294 0.3276 0.0076  -0.0091 -0.0374 111  ILE B CG1 
9792  C CG2 . ILE B 113  ? 0.4810 0.4426 0.3291 0.0057  -0.0103 -0.0363 111  ILE B CG2 
9793  C CD1 . ILE B 113  ? 0.4613 0.4224 0.3190 0.0098  -0.0075 -0.0409 111  ILE B CD1 
9794  N N   . PRO B 114  ? 0.5778 0.5468 0.4340 0.0013  -0.0111 -0.0272 112  PRO B N   
9795  C CA  . PRO B 114  ? 0.5491 0.5197 0.4011 0.0000  -0.0100 -0.0246 112  PRO B CA  
9796  C C   . PRO B 114  ? 0.5384 0.5073 0.3806 0.0002  -0.0090 -0.0258 112  PRO B C   
9797  O O   . PRO B 114  ? 0.5842 0.5557 0.4230 -0.0001 -0.0063 -0.0243 112  PRO B O   
9798  C CB  . PRO B 114  ? 0.5129 0.4819 0.3668 -0.0020 -0.0139 -0.0221 112  PRO B CB  
9799  C CG  . PRO B 114  ? 0.5733 0.5390 0.4289 -0.0017 -0.0175 -0.0240 112  PRO B CG  
9800  C CD  . PRO B 114  ? 0.5380 0.5043 0.3973 0.0002  -0.0155 -0.0267 112  PRO B CD  
9801  N N   . ASP B 115  ? 0.5408 0.5055 0.3783 0.0008  -0.0112 -0.0284 113  ASP B N   
9802  C CA  . ASP B 115  ? 0.6239 0.5865 0.4514 0.0011  -0.0106 -0.0297 113  ASP B CA  
9803  C C   . ASP B 115  ? 0.6251 0.5892 0.4504 0.0034  -0.0062 -0.0322 113  ASP B C   
9804  O O   . ASP B 115  ? 0.5612 0.5240 0.3888 0.0051  -0.0059 -0.0350 113  ASP B O   
9805  C CB  . ASP B 115  ? 0.5876 0.5450 0.4110 0.0006  -0.0149 -0.0315 113  ASP B CB  
9806  C CG  . ASP B 115  ? 0.6533 0.6078 0.4657 0.0008  -0.0145 -0.0331 113  ASP B CG  
9807  O OD1 . ASP B 115  ? 0.7230 0.6788 0.5305 -0.0002 -0.0136 -0.0310 113  ASP B OD1 
9808  O OD2 . ASP B 115  ? 0.6331 0.5840 0.4418 0.0019  -0.0153 -0.0364 113  ASP B OD2 
9809  N N   . THR B 116  ? 0.5861 0.5531 0.4068 0.0035  -0.0028 -0.0312 114  THR B N   
9810  C CA  . THR B 116  ? 0.6310 0.6001 0.4495 0.0059  0.0017  -0.0333 114  THR B CA  
9811  C C   . THR B 116  ? 0.5908 0.5550 0.4031 0.0077  0.0010  -0.0374 114  THR B C   
9812  O O   . THR B 116  ? 0.5605 0.5249 0.3745 0.0102  0.0033  -0.0400 114  THR B O   
9813  C CB  . THR B 116  ? 0.6787 0.6514 0.4922 0.0054  0.0051  -0.0314 114  THR B CB  
9814  O OG1 . THR B 116  ? 0.7467 0.7239 0.5665 0.0037  0.0059  -0.0278 114  THR B OG1 
9815  C CG2 . THR B 116  ? 0.6711 0.6464 0.4820 0.0081  0.0099  -0.0337 114  THR B CG2 
9816  N N   . ALA B 117  ? 0.5851 0.5448 0.3900 0.0066  -0.0021 -0.0379 115  ALA B N   
9817  C CA  . ALA B 117  ? 0.5805 0.5351 0.3786 0.0081  -0.0027 -0.0418 115  ALA B CA  
9818  C C   . ALA B 117  ? 0.5281 0.4795 0.3315 0.0088  -0.0052 -0.0441 115  ALA B C   
9819  O O   . ALA B 117  ? 0.5932 0.5422 0.3945 0.0110  -0.0038 -0.0475 115  ALA B O   
9820  C CB  . ALA B 117  ? 0.5383 0.4888 0.3271 0.0064  -0.0058 -0.0418 115  ALA B CB  
9821  N N   . THR B 118  ? 0.5219 0.4733 0.3320 0.0070  -0.0087 -0.0423 116  THR B N   
9822  C CA  . THR B 118  ? 0.5121 0.4610 0.3279 0.0075  -0.0108 -0.0440 116  THR B CA  
9823  C C   . THR B 118  ? 0.4978 0.4498 0.3200 0.0098  -0.0072 -0.0449 116  THR B C   
9824  O O   . THR B 118  ? 0.5446 0.4939 0.3675 0.0114  -0.0071 -0.0477 116  THR B O   
9825  C CB  . THR B 118  ? 0.5318 0.4809 0.3539 0.0052  -0.0149 -0.0415 116  THR B CB  
9826  O OG1 . THR B 118  ? 0.5692 0.5154 0.3854 0.0033  -0.0186 -0.0408 116  THR B OG1 
9827  C CG2 . THR B 118  ? 0.5507 0.4978 0.3791 0.0055  -0.0169 -0.0431 116  THR B CG2 
9828  N N   . ARG B 119  ? 0.5303 0.4879 0.3569 0.0098  -0.0042 -0.0424 117  ARG B N   
9829  C CA  . ARG B 119  ? 0.4752 0.4365 0.3082 0.0118  -0.0007 -0.0428 117  ARG B CA  
9830  C C   . ARG B 119  ? 0.5215 0.4823 0.3492 0.0147  0.0029  -0.0458 117  ARG B C   
9831  O O   . ARG B 119  ? 0.4850 0.4449 0.3156 0.0169  0.0040  -0.0480 117  ARG B O   
9832  C CB  . ARG B 119  ? 0.4860 0.4534 0.3240 0.0109  0.0014  -0.0394 117  ARG B CB  
9833  C CG  . ARG B 119  ? 0.4307 0.4024 0.2763 0.0126  0.0045  -0.0394 117  ARG B CG  
9834  C CD  . ARG B 119  ? 0.4255 0.4033 0.2739 0.0117  0.0073  -0.0363 117  ARG B CD  
9835  N NE  . ARG B 119  ? 0.4679 0.4463 0.3190 0.0089  0.0047  -0.0331 117  ARG B NE  
9836  C CZ  . ARG B 119  ? 0.5689 0.5495 0.4172 0.0071  0.0055  -0.0305 117  ARG B CZ  
9837  N NH1 . ARG B 119  ? 0.5106 0.4937 0.3537 0.0078  0.0089  -0.0305 117  ARG B NH1 
9838  N NH2 . ARG B 119  ? 0.6029 0.5832 0.4537 0.0047  0.0028  -0.0277 117  ARG B NH2 
9839  N N   . ASP B 120  ? 0.4764 0.4377 0.2963 0.0149  0.0048  -0.0458 118  ASP B N   
9840  C CA  . ASP B 120  ? 0.5005 0.4615 0.3149 0.0178  0.0085  -0.0486 118  ASP B CA  
9841  C C   . ASP B 120  ? 0.5825 0.5364 0.3920 0.0191  0.0064  -0.0525 118  ASP B C   
9842  O O   . ASP B 120  ? 0.5330 0.4859 0.3417 0.0220  0.0089  -0.0552 118  ASP B O   
9843  C CB  . ASP B 120  ? 0.5446 0.5076 0.3512 0.0174  0.0108  -0.0476 118  ASP B CB  
9844  C CG  . ASP B 120  ? 0.6244 0.5947 0.4357 0.0165  0.0137  -0.0440 118  ASP B CG  
9845  O OD1 . ASP B 120  ? 0.6227 0.5965 0.4431 0.0165  0.0141  -0.0426 118  ASP B OD1 
9846  O OD2 . ASP B 120  ? 0.7032 0.6757 0.5090 0.0157  0.0155  -0.0425 118  ASP B OD2 
9847  N N   . ALA B 121  ? 0.5082 0.4572 0.3145 0.0169  0.0018  -0.0528 119  ALA B N   
9848  C CA  . ALA B 121  ? 0.6023 0.5443 0.4043 0.0178  -0.0005 -0.0564 119  ALA B CA  
9849  C C   . ALA B 121  ? 0.5614 0.5024 0.3712 0.0188  -0.0011 -0.0575 119  ALA B C   
9850  O O   . ALA B 121  ? 0.5856 0.5227 0.3930 0.0211  -0.0003 -0.0608 119  ALA B O   
9851  C CB  . ALA B 121  ? 0.5849 0.5224 0.3821 0.0149  -0.0055 -0.0562 119  ALA B CB  
9852  N N   . LEU B 122  ? 0.5129 0.4573 0.3319 0.0173  -0.0024 -0.0549 120  LEU B N   
9853  C CA  . LEU B 122  ? 0.5039 0.4477 0.3305 0.0182  -0.0030 -0.0556 120  LEU B CA  
9854  C C   . LEU B 122  ? 0.5261 0.4724 0.3547 0.0215  0.0016  -0.0569 120  LEU B C   
9855  O O   . LEU B 122  ? 0.5118 0.4550 0.3419 0.0233  0.0017  -0.0593 120  LEU B O   
9856  C CB  . LEU B 122  ? 0.5000 0.4475 0.3357 0.0160  -0.0048 -0.0523 120  LEU B CB  
9857  C CG  . LEU B 122  ? 0.5565 0.5032 0.4001 0.0165  -0.0059 -0.0528 120  LEU B CG  
9858  C CD1 . LEU B 122  ? 0.5805 0.5206 0.4215 0.0155  -0.0100 -0.0550 120  LEU B CD1 
9859  C CD2 . LEU B 122  ? 0.5356 0.4869 0.3880 0.0148  -0.0066 -0.0495 120  LEU B CD2 
9860  N N   . ILE B 123  ? 0.4721 0.4243 0.3010 0.0223  0.0054  -0.0553 121  ILE B N   
9861  C CA  . ILE B 123  ? 0.5180 0.4735 0.3490 0.0256  0.0099  -0.0562 121  ILE B CA  
9862  C C   . ILE B 123  ? 0.5379 0.4886 0.3611 0.0284  0.0114  -0.0601 121  ILE B C   
9863  O O   . ILE B 123  ? 0.5366 0.4856 0.3619 0.0311  0.0126  -0.0622 121  ILE B O   
9864  C CB  . ILE B 123  ? 0.4626 0.4256 0.2948 0.0255  0.0135  -0.0535 121  ILE B CB  
9865  C CG1 . ILE B 123  ? 0.4076 0.3752 0.2486 0.0231  0.0123  -0.0499 121  ILE B CG1 
9866  C CG2 . ILE B 123  ? 0.4930 0.4596 0.3258 0.0290  0.0183  -0.0548 121  ILE B CG2 
9867  C CD1 . ILE B 123  ? 0.3846 0.3584 0.2258 0.0220  0.0149  -0.0469 121  ILE B CD1 
9868  N N   . ARG B 124  ? 0.5158 0.4640 0.3297 0.0281  0.0113  -0.0611 122  ARG B N   
9869  C CA  . ARG B 124  ? 0.5919 0.5355 0.3974 0.0309  0.0130  -0.0649 122  ARG B CA  
9870  C C   . ARG B 124  ? 0.6523 0.5877 0.4559 0.0310  0.0095  -0.0680 122  ARG B C   
9871  O O   . ARG B 124  ? 0.7160 0.6479 0.5171 0.0341  0.0112  -0.0711 122  ARG B O   
9872  C CB  . ARG B 124  ? 0.6527 0.5958 0.4485 0.0302  0.0137  -0.0651 122  ARG B CB  
9873  N N   . ASP B 125  ? 0.6065 0.5388 0.4113 0.0278  0.0047  -0.0671 123  ASP B N   
9874  C CA  . ASP B 125  ? 0.7107 0.6351 0.5127 0.0273  0.0011  -0.0699 123  ASP B CA  
9875  C C   . ASP B 125  ? 0.7238 0.6474 0.5346 0.0272  -0.0005 -0.0697 123  ASP B C   
9876  O O   . ASP B 125  ? 0.7902 0.7073 0.5991 0.0278  -0.0023 -0.0724 123  ASP B O   
9877  C CB  . ASP B 125  ? 0.7069 0.6279 0.5044 0.0237  -0.0036 -0.0693 123  ASP B CB  
9878  C CG  . ASP B 125  ? 0.7839 0.7047 0.5716 0.0236  -0.0026 -0.0696 123  ASP B CG  
9879  O OD1 . ASP B 125  ? 0.7687 0.6898 0.5512 0.0265  0.0014  -0.0715 123  ASP B OD1 
9880  O OD2 . ASP B 125  ? 0.8237 0.7441 0.6089 0.0206  -0.0057 -0.0680 123  ASP B OD2 
9881  N N   . LYS B 126  ? 0.5834 0.5131 0.4036 0.0265  0.0001  -0.0666 124  LYS B N   
9882  C CA  . LYS B 126  ? 0.6555 0.5843 0.4837 0.0261  -0.0017 -0.0663 124  LYS B CA  
9883  C C   . LYS B 126  ? 0.6152 0.5495 0.4512 0.0283  0.0018  -0.0651 124  LYS B C   
9884  O O   . LYS B 126  ? 0.6770 0.6091 0.5167 0.0298  0.0018  -0.0663 124  LYS B O   
9885  C CB  . LYS B 126  ? 0.6714 0.6010 0.5043 0.0223  -0.0059 -0.0637 124  LYS B CB  
9886  N N   . ILE B 127  ? 0.5711 0.5124 0.4095 0.0285  0.0047  -0.0626 125  ILE B N   
9887  C CA  . ILE B 127  ? 0.5318 0.4789 0.3784 0.0301  0.0075  -0.0611 125  ILE B CA  
9888  C C   . ILE B 127  ? 0.5790 0.5267 0.4232 0.0342  0.0117  -0.0633 125  ILE B C   
9889  O O   . ILE B 127  ? 0.5219 0.4703 0.3713 0.0363  0.0130  -0.0637 125  ILE B O   
9890  C CB  . ILE B 127  ? 0.4751 0.4295 0.3264 0.0283  0.0085  -0.0574 125  ILE B CB  
9891  C CG1 . ILE B 127  ? 0.5408 0.4942 0.3936 0.0245  0.0043  -0.0553 125  ILE B CG1 
9892  C CG2 . ILE B 127  ? 0.4314 0.3913 0.2916 0.0295  0.0107  -0.0558 125  ILE B CG2 
9893  C CD1 . ILE B 127  ? 0.6188 0.5696 0.4776 0.0234  0.0012  -0.0553 125  ILE B CD1 
9894  N N   . ALA B 128  ? 0.4819 0.4296 0.3184 0.0355  0.0140  -0.0645 126  ALA B N   
9895  C CA  . ALA B 128  ? 0.4934 0.4421 0.3275 0.0396  0.0183  -0.0665 126  ALA B CA  
9896  C C   . ALA B 128  ? 0.6386 0.5801 0.4704 0.0421  0.0175  -0.0701 126  ALA B C   
9897  O O   . ALA B 128  ? 0.5957 0.5381 0.4282 0.0458  0.0208  -0.0715 126  ALA B O   
9898  C CB  . ALA B 128  ? 0.5422 0.4920 0.3678 0.0403  0.0207  -0.0672 126  ALA B CB  
9899  N N   . ASP B 129  ? 0.6372 0.5716 0.4665 0.0400  0.0133  -0.0714 127  ASP B N   
9900  C CA  . ASP B 129  ? 0.7523 0.6791 0.5798 0.0417  0.0120  -0.0745 127  ASP B CA  
9901  C C   . ASP B 129  ? 0.7674 0.6944 0.6040 0.0412  0.0104  -0.0732 127  ASP B C   
9902  O O   . ASP B 129  ? 0.8701 0.7903 0.7060 0.0409  0.0078  -0.0751 127  ASP B O   
9903  C CB  . ASP B 129  ? 0.8205 0.7392 0.6398 0.0398  0.0084  -0.0768 127  ASP B CB  
9904  C CG  . ASP B 129  ? 0.9181 0.8363 0.7277 0.0403  0.0099  -0.0780 127  ASP B CG  
9905  O OD1 . ASP B 129  ? 0.9290 0.8501 0.7363 0.0437  0.0143  -0.0789 127  ASP B OD1 
9906  O OD2 . ASP B 129  ? 0.9580 0.8732 0.7625 0.0374  0.0068  -0.0781 127  ASP B OD2 
9907  N N   . GLY B 130  ? 0.7153 0.6500 0.5603 0.0408  0.0117  -0.0701 128  GLY B N   
9908  C CA  . GLY B 130  ? 0.7444 0.6800 0.5978 0.0408  0.0110  -0.0690 128  GLY B CA  
9909  C C   . GLY B 130  ? 0.7746 0.7081 0.6322 0.0371  0.0066  -0.0675 128  GLY B C   
9910  O O   . GLY B 130  ? 0.7908 0.7276 0.6564 0.0364  0.0062  -0.0655 128  GLY B O   
9911  N N   . ASN B 131  ? 0.8551 0.7833 0.7072 0.0347  0.0033  -0.0686 129  ASN B N   
9912  C CA  . ASN B 131  ? 0.8441 0.7702 0.7000 0.0312  -0.0010 -0.0674 129  ASN B CA  
9913  C C   . ASN B 131  ? 0.8098 0.7424 0.6715 0.0286  -0.0017 -0.0637 129  ASN B C   
9914  O O   . ASN B 131  ? 0.8500 0.7815 0.7115 0.0255  -0.0051 -0.0627 129  ASN B O   
9915  C CB  . ASN B 131  ? 0.8380 0.7568 0.6863 0.0294  -0.0045 -0.0695 129  ASN B CB  
9916  N N   . TRP B 132  ? 0.6584 0.5979 0.5255 0.0298  0.0013  -0.0617 130  TRP B N   
9917  C CA  . TRP B 132  ? 0.6042 0.5498 0.4763 0.0275  0.0010  -0.0584 130  TRP B CA  
9918  C C   . TRP B 132  ? 0.5797 0.5253 0.4588 0.0252  -0.0020 -0.0567 130  TRP B C   
9919  O O   . TRP B 132  ? 0.6187 0.5670 0.5003 0.0226  -0.0038 -0.0543 130  TRP B O   
9920  C CB  . TRP B 132  ? 0.5728 0.5256 0.4485 0.0293  0.0051  -0.0568 130  TRP B CB  
9921  C CG  . TRP B 132  ? 0.4567 0.4112 0.3390 0.0314  0.0066  -0.0567 130  TRP B CG  
9922  C CD1 . TRP B 132  ? 0.4751 0.4286 0.3563 0.0349  0.0091  -0.0587 130  TRP B CD1 
9923  C CD2 . TRP B 132  ? 0.4224 0.3799 0.3130 0.0301  0.0056  -0.0545 130  TRP B CD2 
9924  N NE1 . TRP B 132  ? 0.4175 0.3733 0.3061 0.0358  0.0097  -0.0577 130  TRP B NE1 
9925  C CE2 . TRP B 132  ? 0.3703 0.3286 0.2646 0.0329  0.0076  -0.0552 130  TRP B CE2 
9926  C CE3 . TRP B 132  ? 0.3825 0.3421 0.2778 0.0271  0.0033  -0.0520 130  TRP B CE3 
9927  C CZ2 . TRP B 132  ? 0.3684 0.3293 0.2704 0.0325  0.0072  -0.0534 130  TRP B CZ2 
9928  C CZ3 . TRP B 132  ? 0.3674 0.3297 0.2705 0.0268  0.0031  -0.0504 130  TRP B CZ3 
9929  C CH2 . TRP B 132  ? 0.3637 0.3266 0.2699 0.0294  0.0050  -0.0511 130  TRP B CH2 
9930  N N   . LYS B 133  ? 0.6080 0.5507 0.4903 0.0261  -0.0026 -0.0577 131  LYS B N   
9931  C CA  . LYS B 133  ? 0.6094 0.5527 0.4989 0.0242  -0.0050 -0.0560 131  LYS B CA  
9932  C C   . LYS B 133  ? 0.7755 0.7155 0.6636 0.0210  -0.0091 -0.0558 131  LYS B C   
9933  O O   . LYS B 133  ? 0.7893 0.7312 0.6832 0.0189  -0.0111 -0.0538 131  LYS B O   
9934  C CB  . LYS B 133  ? 0.6379 0.5783 0.5304 0.0259  -0.0047 -0.0573 131  LYS B CB  
9935  N N   . SER B 134  ? 0.8355 0.7708 0.7159 0.0206  -0.0105 -0.0578 132  SER B N   
9936  C CA  . SER B 134  ? 0.8174 0.7491 0.6959 0.0176  -0.0147 -0.0579 132  SER B CA  
9937  C C   . SER B 134  ? 0.8404 0.7740 0.7146 0.0162  -0.0154 -0.0568 132  SER B C   
9938  O O   . SER B 134  ? 0.9267 0.8562 0.7949 0.0148  -0.0179 -0.0581 132  SER B O   
9939  C CB  . SER B 134  ? 0.7771 0.7012 0.6501 0.0179  -0.0164 -0.0610 132  SER B CB  
9940  O OG  . SER B 134  ? 0.8772 0.7990 0.7431 0.0205  -0.0139 -0.0635 132  SER B OG  
9941  N N   . HIS B 135  ? 0.8456 0.7852 0.7225 0.0163  -0.0133 -0.0544 133  HIS B N   
9942  C CA  . HIS B 135  ? 0.8762 0.8176 0.7487 0.0150  -0.0137 -0.0533 133  HIS B CA  
9943  C C   . HIS B 135  ? 0.8830 0.8305 0.7612 0.0138  -0.0132 -0.0498 133  HIS B C   
9944  O O   . HIS B 135  ? 0.9626 0.9108 0.8394 0.0118  -0.0152 -0.0482 133  HIS B O   
9945  C CB  . HIS B 135  ? 0.8316 0.7725 0.6966 0.0171  -0.0106 -0.0549 133  HIS B CB  
9946  C CG  . HIS B 135  ? 0.8880 0.8222 0.7453 0.0178  -0.0118 -0.0583 133  HIS B CG  
9947  N ND1 . HIS B 135  ? 0.9571 0.8881 0.8123 0.0205  -0.0098 -0.0610 133  HIS B ND1 
9948  C CD2 . HIS B 135  ? 0.9268 0.8566 0.7777 0.0160  -0.0149 -0.0593 133  HIS B CD2 
9949  C CE1 . HIS B 135  ? 0.9866 0.9112 0.8342 0.0204  -0.0116 -0.0637 133  HIS B CE1 
9950  N NE2 . HIS B 135  ? 0.9825 0.9064 0.8274 0.0176  -0.0147 -0.0628 133  HIS B NE2 
9951  N N   . LEU B 136  ? 0.7728 0.7245 0.6571 0.0151  -0.0106 -0.0487 134  LEU B N   
9952  C CA  . LEU B 136  ? 0.7714 0.7286 0.6607 0.0140  -0.0098 -0.0456 134  LEU B CA  
9953  C C   . LEU B 136  ? 0.7081 0.6673 0.6060 0.0137  -0.0103 -0.0443 134  LEU B C   
9954  O O   . LEU B 136  ? 0.7403 0.7037 0.6429 0.0128  -0.0099 -0.0419 134  LEU B O   
9955  C CB  . LEU B 136  ? 0.6758 0.6372 0.5636 0.0156  -0.0058 -0.0451 134  LEU B CB  
9956  C CG  . LEU B 136  ? 0.5984 0.5586 0.4776 0.0160  -0.0047 -0.0461 134  LEU B CG  
9957  C CD1 . LEU B 136  ? 0.5532 0.5179 0.4320 0.0180  -0.0003 -0.0459 134  LEU B CD1 
9958  C CD2 . LEU B 136  ? 0.6506 0.6109 0.5271 0.0135  -0.0070 -0.0442 134  LEU B CD2 
9959  N N   . ARG B 140  ? 0.5161 0.4825 0.4441 0.0087  -0.0167 -0.0371 138  ARG B N   
9960  C CA  . ARG B 140  ? 0.6165 0.5872 0.5476 0.0095  -0.0139 -0.0357 138  ARG B CA  
9961  C C   . ARG B 140  ? 0.5735 0.5447 0.5019 0.0116  -0.0108 -0.0371 138  ARG B C   
9962  O O   . ARG B 140  ? 0.4518 0.4213 0.3741 0.0121  -0.0102 -0.0384 138  ARG B O   
9963  C CB  . ARG B 140  ? 0.5925 0.5657 0.5231 0.0082  -0.0141 -0.0335 138  ARG B CB  
9964  N N   . SER B 141  ? 0.4472 0.4211 0.3801 0.0128  -0.0087 -0.0368 139  SER B N   
9965  C CA  . SER B 141  ? 0.3841 0.3588 0.3153 0.0150  -0.0058 -0.0381 139  SER B CA  
9966  C C   . SER B 141  ? 0.3760 0.3533 0.3031 0.0152  -0.0038 -0.0376 139  SER B C   
9967  O O   . SER B 141  ? 0.3986 0.3787 0.3268 0.0138  -0.0038 -0.0355 139  SER B O   
9968  C CB  . SER B 141  ? 0.4036 0.3816 0.3409 0.0160  -0.0041 -0.0372 139  SER B CB  
9969  O OG  . SER B 141  ? 0.4138 0.3934 0.3502 0.0183  -0.0012 -0.0382 139  SER B OG  
9970  N N   . LEU B 142  ? 0.3577 0.3338 0.2801 0.0171  -0.0020 -0.0394 140  LEU B N   
9971  C CA  . LEU B 142  ? 0.3464 0.3257 0.2656 0.0176  0.0006  -0.0389 140  LEU B CA  
9972  C C   . LEU B 142  ? 0.3132 0.2983 0.2375 0.0179  0.0029  -0.0371 140  LEU B C   
9973  O O   . LEU B 142  ? 0.3030 0.2916 0.2260 0.0173  0.0046  -0.0357 140  LEU B O   
9974  C CB  . LEU B 142  ? 0.3334 0.3107 0.2476 0.0202  0.0026  -0.0415 140  LEU B CB  
9975  C CG  . LEU B 142  ? 0.3957 0.3735 0.3033 0.0204  0.0040  -0.0419 140  LEU B CG  
9976  C CD1 . LEU B 142  ? 0.4004 0.3742 0.3033 0.0184  0.0010  -0.0421 140  LEU B CD1 
9977  C CD2 . LEU B 142  ? 0.4230 0.3992 0.3266 0.0234  0.0063  -0.0444 140  LEU B CD2 
9978  N N   . PHE B 143  ? 0.2934 0.2796 0.2234 0.0186  0.0031  -0.0369 141  PHE B N   
9979  C CA  . PHE B 143  ? 0.2715 0.2630 0.2061 0.0193  0.0055  -0.0356 141  PHE B CA  
9980  C C   . PHE B 143  ? 0.2757 0.2696 0.2154 0.0172  0.0044  -0.0333 141  PHE B C   
9981  O O   . PHE B 143  ? 0.2794 0.2773 0.2237 0.0176  0.0058  -0.0323 141  PHE B O   
9982  C CB  . PHE B 143  ? 0.2941 0.2853 0.2307 0.0219  0.0068  -0.0371 141  PHE B CB  
9983  C CG  . PHE B 143  ? 0.2670 0.2550 0.1981 0.0241  0.0078  -0.0396 141  PHE B CG  
9984  C CD1 . PHE B 143  ? 0.2677 0.2579 0.1946 0.0251  0.0102  -0.0399 141  PHE B CD1 
9985  C CD2 . PHE B 143  ? 0.2596 0.2423 0.1894 0.0252  0.0065  -0.0416 141  PHE B CD2 
9986  C CE1 . PHE B 143  ? 0.2823 0.2695 0.2038 0.0273  0.0112  -0.0423 141  PHE B CE1 
9987  C CE2 . PHE B 143  ? 0.2887 0.2681 0.2132 0.0273  0.0073  -0.0440 141  PHE B CE2 
9988  C CZ  . PHE B 143  ? 0.2806 0.2621 0.2008 0.0284  0.0098  -0.0445 141  PHE B CZ  
9989  N N   . VAL B 144  ? 0.2950 0.2868 0.2341 0.0151  0.0018  -0.0324 142  VAL B N   
9990  C CA  . VAL B 144  ? 0.3101 0.3036 0.2538 0.0132  0.0007  -0.0303 142  VAL B CA  
9991  C C   . VAL B 144  ? 0.3238 0.3223 0.2693 0.0127  0.0028  -0.0285 142  VAL B C   
9992  O O   . VAL B 144  ? 0.3279 0.3288 0.2784 0.0122  0.0029  -0.0273 142  VAL B O   
9993  C CB  . VAL B 144  ? 0.3386 0.3292 0.2805 0.0113  -0.0022 -0.0296 142  VAL B CB  
9994  C CG1 . VAL B 144  ? 0.3862 0.3787 0.3324 0.0096  -0.0031 -0.0274 142  VAL B CG1 
9995  C CG2 . VAL B 144  ? 0.3591 0.3454 0.3005 0.0115  -0.0045 -0.0311 142  VAL B CG2 
9996  N N   . ASN B 145  ? 0.2975 0.2978 0.2391 0.0127  0.0045  -0.0283 143  ASN B N   
9997  C CA  . ASN B 145  ? 0.3177 0.3228 0.2608 0.0119  0.0064  -0.0264 143  ASN B CA  
9998  C C   . ASN B 145  ? 0.3009 0.3100 0.2448 0.0138  0.0095  -0.0271 143  ASN B C   
9999  O O   . ASN B 145  ? 0.3011 0.3144 0.2449 0.0133  0.0115  -0.0258 143  ASN B O   
10000 C CB  . ASN B 145  ? 0.3384 0.3435 0.2772 0.0101  0.0063  -0.0251 143  ASN B CB  
10001 C CG  . ASN B 145  ? 0.4253 0.4276 0.3646 0.0080  0.0034  -0.0238 143  ASN B CG  
10002 O OD1 . ASN B 145  ? 0.4564 0.4595 0.4005 0.0072  0.0025  -0.0227 143  ASN B OD1 
10003 N ND2 . ASN B 145  ? 0.4144 0.4136 0.3489 0.0073  0.0019  -0.0239 143  ASN B ND2 
10004 N N   . ALA B 146  ? 0.2625 0.2704 0.2075 0.0161  0.0099  -0.0289 144  ALA B N   
10005 C CA  . ALA B 146  ? 0.3132 0.3247 0.2588 0.0184  0.0128  -0.0296 144  ALA B CA  
10006 C C   . ALA B 146  ? 0.2801 0.2973 0.2312 0.0180  0.0142  -0.0279 144  ALA B C   
10007 O O   . ALA B 146  ? 0.2917 0.3135 0.2433 0.0192  0.0168  -0.0277 144  ALA B O   
10008 C CB  . ALA B 146  ? 0.2914 0.2997 0.2368 0.0210  0.0127  -0.0319 144  ALA B CB  
10009 N N   . ALA B 147  ? 0.2886 0.3058 0.2439 0.0163  0.0125  -0.0266 145  ALA B N   
10010 C CA  . ALA B 147  ? 0.2909 0.3133 0.2509 0.0157  0.0137  -0.0250 145  ALA B CA  
10011 C C   . ALA B 147  ? 0.2972 0.3234 0.2558 0.0139  0.0151  -0.0233 145  ALA B C   
10012 O O   . ALA B 147  ? 0.3098 0.3415 0.2707 0.0142  0.0172  -0.0224 145  ALA B O   
10013 C CB  . ALA B 147  ? 0.3047 0.3259 0.2688 0.0142  0.0116  -0.0240 145  ALA B CB  
10014 N N   . THR B 148  ? 0.2985 0.3220 0.2532 0.0122  0.0139  -0.0227 146  THR B N   
10015 C CA  . THR B 148  ? 0.2919 0.3185 0.2447 0.0104  0.0152  -0.0210 146  THR B CA  
10016 C C   . THR B 148  ? 0.3129 0.3425 0.2626 0.0121  0.0181  -0.0218 146  THR B C   
10017 O O   . THR B 148  ? 0.3149 0.3499 0.2658 0.0117  0.0203  -0.0205 146  THR B O   
10018 C CB  . THR B 148  ? 0.3958 0.4182 0.3449 0.0082  0.0131  -0.0202 146  THR B CB  
10019 O OG1 . THR B 148  ? 0.4380 0.4583 0.3905 0.0068  0.0108  -0.0193 146  THR B OG1 
10020 C CG2 . THR B 148  ? 0.4726 0.4978 0.4192 0.0063  0.0144  -0.0183 146  THR B CG2 
10021 N N   . TRP B 149  ? 0.2920 0.3182 0.2377 0.0142  0.0181  -0.0239 147  TRP B N   
10022 C CA  . TRP B 149  ? 0.2930 0.3218 0.2356 0.0162  0.0209  -0.0249 147  TRP B CA  
10023 C C   . TRP B 149  ? 0.2712 0.3049 0.2183 0.0185  0.0232  -0.0253 147  TRP B C   
10024 O O   . TRP B 149  ? 0.2853 0.3239 0.2318 0.0195  0.0260  -0.0250 147  TRP B O   
10025 C CB  . TRP B 149  ? 0.2971 0.3206 0.2340 0.0180  0.0204  -0.0273 147  TRP B CB  
10026 C CG  . TRP B 149  ? 0.2949 0.3146 0.2268 0.0158  0.0186  -0.0268 147  TRP B CG  
10027 C CD1 . TRP B 149  ? 0.3287 0.3426 0.2590 0.0150  0.0155  -0.0275 147  TRP B CD1 
10028 C CD2 . TRP B 149  ? 0.3302 0.3518 0.2582 0.0142  0.0197  -0.0253 147  TRP B CD2 
10029 N NE1 . TRP B 149  ? 0.3195 0.3316 0.2451 0.0131  0.0145  -0.0265 147  TRP B NE1 
10030 C CE2 . TRP B 149  ? 0.3518 0.3683 0.2757 0.0125  0.0170  -0.0252 147  TRP B CE2 
10031 C CE3 . TRP B 149  ? 0.3706 0.3979 0.2982 0.0139  0.0227  -0.0240 147  TRP B CE3 
10032 C CZ2 . TRP B 149  ? 0.3981 0.4147 0.3173 0.0107  0.0172  -0.0238 147  TRP B CZ2 
10033 C CZ3 . TRP B 149  ? 0.4082 0.4356 0.3310 0.0119  0.0230  -0.0226 147  TRP B CZ3 
10034 C CH2 . TRP B 149  ? 0.4247 0.4466 0.3433 0.0104  0.0202  -0.0225 147  TRP B CH2 
10035 N N   . GLY B 150  ? 0.2743 0.3070 0.2258 0.0193  0.0219  -0.0258 148  GLY B N   
10036 C CA  . GLY B 150  ? 0.3042 0.3417 0.2603 0.0213  0.0237  -0.0258 148  GLY B CA  
10037 C C   . GLY B 150  ? 0.2864 0.3308 0.2459 0.0195  0.0252  -0.0234 148  GLY B C   
10038 O O   . GLY B 150  ? 0.2957 0.3458 0.2570 0.0210  0.0278  -0.0232 148  GLY B O   
10039 N N   . LEU B 151  ? 0.2911 0.3350 0.2515 0.0161  0.0236  -0.0215 149  LEU B N   
10040 C CA  A LEU B 151  ? 0.3527 0.4026 0.3158 0.0139  0.0248  -0.0192 149  LEU B CA  
10041 C CA  B LEU B 151  ? 0.3526 0.4025 0.3157 0.0139  0.0248  -0.0192 149  LEU B CA  
10042 C C   . LEU B 151  ? 0.3502 0.4038 0.3099 0.0138  0.0274  -0.0187 149  LEU B C   
10043 O O   . LEU B 151  ? 0.3730 0.4332 0.3352 0.0139  0.0297  -0.0175 149  LEU B O   
10044 C CB  A LEU B 151  ? 0.3497 0.3972 0.3135 0.0104  0.0224  -0.0175 149  LEU B CB  
10045 C CB  B LEU B 151  ? 0.3497 0.3972 0.3136 0.0104  0.0224  -0.0175 149  LEU B CB  
10046 C CG  A LEU B 151  ? 0.3467 0.3954 0.3160 0.0094  0.0211  -0.0166 149  LEU B CG  
10047 C CG  B LEU B 151  ? 0.3528 0.4055 0.3200 0.0077  0.0230  -0.0151 149  LEU B CG  
10048 C CD1 A LEU B 151  ? 0.3892 0.4348 0.3583 0.0062  0.0189  -0.0152 149  LEU B CD1 
10049 C CD1 B LEU B 151  ? 0.3641 0.4219 0.3370 0.0090  0.0239  -0.0150 149  LEU B CD1 
10050 C CD2 A LEU B 151  ? 0.3704 0.4268 0.3439 0.0093  0.0232  -0.0154 149  LEU B CD2 
10051 C CD2 B LEU B 151  ? 0.4087 0.4577 0.3761 0.0047  0.0204  -0.0138 149  LEU B CD2 
10052 N N   . VAL B 152  ? 0.3188 0.3682 0.2726 0.0137  0.0270  -0.0194 150  VAL B N   
10053 C CA  . VAL B 152  ? 0.3339 0.3863 0.2836 0.0136  0.0296  -0.0189 150  VAL B CA  
10054 C C   . VAL B 152  ? 0.3524 0.4090 0.3025 0.0172  0.0326  -0.0204 150  VAL B C   
10055 O O   . VAL B 152  ? 0.3861 0.4491 0.3369 0.0172  0.0353  -0.0192 150  VAL B O   
10056 C CB  . VAL B 152  ? 0.3120 0.3585 0.2549 0.0130  0.0283  -0.0197 150  VAL B CB  
10057 C CG1 . VAL B 152  ? 0.4167 0.4661 0.3548 0.0136  0.0312  -0.0196 150  VAL B CG1 
10058 C CG2 . VAL B 152  ? 0.3597 0.4029 0.3023 0.0095  0.0257  -0.0179 150  VAL B CG2 
10059 N N   . VAL B 153  ? 0.3112 0.3643 0.2609 0.0203  0.0321  -0.0228 151  VAL B N   
10060 C CA  . VAL B 153  ? 0.3248 0.3805 0.2739 0.0241  0.0349  -0.0245 151  VAL B CA  
10061 C C   . VAL B 153  ? 0.3195 0.3817 0.2752 0.0254  0.0363  -0.0237 151  VAL B C   
10062 O O   . VAL B 153  ? 0.3460 0.4143 0.3025 0.0272  0.0394  -0.0236 151  VAL B O   
10063 C CB  . VAL B 153  ? 0.3375 0.3861 0.2831 0.0268  0.0336  -0.0274 151  VAL B CB  
10064 C CG1 . VAL B 153  ? 0.3406 0.3913 0.2859 0.0311  0.0363  -0.0293 151  VAL B CG1 
10065 C CG2 . VAL B 153  ? 0.3097 0.3525 0.2483 0.0255  0.0324  -0.0282 151  VAL B CG2 
10066 N N   . THR B 154  ? 0.3145 0.3759 0.2751 0.0247  0.0342  -0.0232 152  THR B N   
10067 C CA  . THR B 154  ? 0.3447 0.4115 0.3114 0.0263  0.0352  -0.0228 152  THR B CA  
10068 C C   . THR B 154  ? 0.3839 0.4559 0.3556 0.0231  0.0347  -0.0201 152  THR B C   
10069 O O   . THR B 154  ? 0.3979 0.4759 0.3747 0.0241  0.0358  -0.0194 152  THR B O   
10070 C CB  . THR B 154  ? 0.3480 0.4101 0.3166 0.0283  0.0332  -0.0244 152  THR B CB  
10071 O OG1 . THR B 154  ? 0.3473 0.4061 0.3178 0.0254  0.0302  -0.0234 152  THR B OG1 
10072 C CG2 . THR B 154  ? 0.3984 0.4537 0.3617 0.0308  0.0329  -0.0270 152  THR B CG2 
10073 N N   . GLY B 155  ? 0.3228 0.3925 0.2933 0.0193  0.0329  -0.0187 153  GLY B N   
10074 C CA  . GLY B 155  ? 0.3680 0.4415 0.3430 0.0162  0.0321  -0.0163 153  GLY B CA  
10075 C C   . GLY B 155  ? 0.3650 0.4362 0.3440 0.0160  0.0297  -0.0165 153  GLY B C   
10076 O O   . GLY B 155  ? 0.4122 0.4865 0.3951 0.0136  0.0289  -0.0147 153  GLY B O   
10077 N N   . LYS B 156  ? 0.3424 0.4082 0.3204 0.0183  0.0284  -0.0185 154  LYS B N   
10078 C CA  . LYS B 156  ? 0.3660 0.4294 0.3476 0.0184  0.0263  -0.0187 154  LYS B CA  
10079 C C   . LYS B 156  ? 0.3588 0.4142 0.3373 0.0174  0.0237  -0.0196 154  LYS B C   
10080 O O   . LYS B 156  ? 0.3663 0.4176 0.3401 0.0182  0.0237  -0.0209 154  LYS B O   
10081 C CB  . LYS B 156  ? 0.4564 0.5207 0.4401 0.0222  0.0271  -0.0201 154  LYS B CB  
10082 N N   . LEU B 157  ? 0.3348 0.3884 0.3159 0.0155  0.0215  -0.0188 155  LEU B N   
10083 C CA  . LEU B 157  ? 0.3569 0.4036 0.3360 0.0145  0.0190  -0.0194 155  LEU B CA  
10084 C C   . LEU B 157  ? 0.4299 0.4738 0.4111 0.0165  0.0178  -0.0207 155  LEU B C   
10085 O O   . LEU B 157  ? 0.4605 0.5073 0.4459 0.0169  0.0179  -0.0202 155  LEU B O   
10086 C CB  . LEU B 157  ? 0.4026 0.4488 0.3828 0.0111  0.0174  -0.0177 155  LEU B CB  
10087 N N   . THR B 158  ? 0.4499 0.4880 0.4281 0.0176  0.0167  -0.0223 156  THR B N   
10088 C CA  . THR B 158  ? 0.4813 0.5156 0.4612 0.0187  0.0151  -0.0233 156  THR B CA  
10089 C C   . THR B 158  ? 0.4642 0.4938 0.4431 0.0165  0.0127  -0.0230 156  THR B C   
10090 O O   . THR B 158  ? 0.4949 0.5228 0.4706 0.0150  0.0122  -0.0227 156  THR B O   
10091 C CB  . THR B 158  ? 0.5615 0.5928 0.5391 0.0217  0.0156  -0.0253 156  THR B CB  
10092 O OG1 . THR B 158  ? 0.5881 0.6150 0.5608 0.0212  0.0149  -0.0263 156  THR B OG1 
10093 C CG2 . THR B 158  ? 0.4983 0.5343 0.4762 0.0241  0.0183  -0.0257 156  THR B CG2 
10094 N N   . SER B 159  ? 0.4003 0.4279 0.3820 0.0164  0.0112  -0.0231 157  SER B N   
10095 C CA  . SER B 159  ? 0.3753 0.3988 0.3564 0.0146  0.0090  -0.0228 157  SER B CA  
10096 C C   . SER B 159  ? 0.4275 0.4459 0.4055 0.0154  0.0078  -0.0243 157  SER B C   
10097 O O   . SER B 159  ? 0.4049 0.4203 0.3809 0.0140  0.0064  -0.0241 157  SER B O   
10098 C CB  . SER B 159  ? 0.4575 0.4809 0.4426 0.0141  0.0079  -0.0222 157  SER B CB  
10099 O OG  . SER B 159  ? 0.5342 0.5590 0.5215 0.0163  0.0087  -0.0229 157  SER B OG  
10100 N N   . THR B 160  ? 0.3681 0.3852 0.3456 0.0178  0.0084  -0.0258 158  THR B N   
10101 C CA  . THR B 160  ? 0.2937 0.3057 0.2680 0.0185  0.0073  -0.0273 158  THR B CA  
10102 C C   . THR B 160  ? 0.2957 0.3079 0.2669 0.0208  0.0090  -0.0288 158  THR B C   
10103 O O   . THR B 160  ? 0.3529 0.3693 0.3250 0.0220  0.0111  -0.0285 158  THR B O   
10104 C CB  . THR B 160  ? 0.3375 0.3465 0.3142 0.0192  0.0059  -0.0279 158  THR B CB  
10105 O OG1 . THR B 160  ? 0.3824 0.3936 0.3615 0.0212  0.0073  -0.0281 158  THR B OG1 
10106 C CG2 . THR B 160  ? 0.3762 0.3851 0.3559 0.0171  0.0043  -0.0266 158  THR B CG2 
10107 N N   . VAL B 161  ? 0.2393 0.2468 0.2068 0.0213  0.0081  -0.0303 159  VAL B N   
10108 C CA  . VAL B 161  ? 0.2888 0.2952 0.2517 0.0230  0.0094  -0.0318 159  VAL B CA  
10109 C C   . VAL B 161  ? 0.2574 0.2601 0.2197 0.0253  0.0092  -0.0337 159  VAL B C   
10110 O O   . VAL B 161  ? 0.2487 0.2472 0.2114 0.0247  0.0072  -0.0341 159  VAL B O   
10111 C CB  . VAL B 161  ? 0.3208 0.3240 0.2790 0.0214  0.0081  -0.0321 159  VAL B CB  
10112 C CG1 . VAL B 161  ? 0.3610 0.3612 0.3139 0.0231  0.0087  -0.0342 159  VAL B CG1 
10113 C CG2 . VAL B 161  ? 0.4390 0.4461 0.3971 0.0195  0.0087  -0.0303 159  VAL B CG2 
10114 N N   . ASN B 162  ? 0.2385 0.2427 0.1999 0.0280  0.0114  -0.0346 160  ASN B N   
10115 C CA  . ASN B 162  ? 0.2388 0.2385 0.1987 0.0303  0.0112  -0.0365 160  ASN B CA  
10116 C C   . ASN B 162  ? 0.2428 0.2378 0.1965 0.0305  0.0107  -0.0384 160  ASN B C   
10117 O O   . ASN B 162  ? 0.2509 0.2466 0.2011 0.0323  0.0126  -0.0395 160  ASN B O   
10118 C CB  . ASN B 162  ? 0.2497 0.2524 0.2114 0.0334  0.0135  -0.0369 160  ASN B CB  
10119 C CG  . ASN B 162  ? 0.2356 0.2330 0.1958 0.0358  0.0131  -0.0388 160  ASN B CG  
10120 O OD1 . ASN B 162  ? 0.2497 0.2412 0.2062 0.0353  0.0115  -0.0402 160  ASN B OD1 
10121 N ND2 . ASN B 162  ? 0.2750 0.2744 0.2379 0.0384  0.0145  -0.0387 160  ASN B ND2 
10122 N N   . ASP B 163  ? 0.2329 0.2234 0.1853 0.0286  0.0081  -0.0387 161  ASP B N   
10123 C CA  . ASP B 163  ? 0.2475 0.2335 0.1939 0.0282  0.0072  -0.0403 161  ASP B CA  
10124 C C   . ASP B 163  ? 0.2489 0.2303 0.1917 0.0308  0.0077  -0.0428 161  ASP B C   
10125 O O   . ASP B 163  ? 0.2463 0.2250 0.1835 0.0312  0.0078  -0.0443 161  ASP B O   
10126 C CB  . ASP B 163  ? 0.2445 0.2274 0.1909 0.0253  0.0041  -0.0398 161  ASP B CB  
10127 C CG  . ASP B 163  ? 0.2813 0.2619 0.2318 0.0248  0.0023  -0.0396 161  ASP B CG  
10128 O OD1 . ASP B 163  ? 0.2665 0.2501 0.2218 0.0254  0.0031  -0.0385 161  ASP B OD1 
10129 O OD2 . ASP B 163  ? 0.3040 0.2799 0.2528 0.0237  0.0000  -0.0404 161  ASP B OD2 
10130 N N   . ARG B 164  ? 0.2314 0.2115 0.1770 0.0324  0.0078  -0.0432 162  ARG B N   
10131 C CA  . ARG B 164  ? 0.2355 0.2109 0.1774 0.0351  0.0084  -0.0455 162  ARG B CA  
10132 C C   . ARG B 164  ? 0.2266 0.2054 0.1667 0.0381  0.0116  -0.0462 162  ARG B C   
10133 O O   . ARG B 164  ? 0.2307 0.2060 0.1653 0.0399  0.0124  -0.0484 162  ARG B O   
10134 C CB  . ARG B 164  ? 0.2474 0.2200 0.1926 0.0361  0.0076  -0.0457 162  ARG B CB  
10135 C CG  . ARG B 164  ? 0.2506 0.2195 0.1973 0.0333  0.0045  -0.0452 162  ARG B CG  
10136 C CD  . ARG B 164  ? 0.3271 0.2911 0.2686 0.0317  0.0025  -0.0466 162  ARG B CD  
10137 N NE  . ARG B 164  ? 0.4398 0.3988 0.3756 0.0339  0.0031  -0.0492 162  ARG B NE  
10138 C CZ  . ARG B 164  ? 0.5175 0.4729 0.4474 0.0332  0.0022  -0.0508 162  ARG B CZ  
10139 N NH1 . ARG B 164  ? 0.5270 0.4833 0.4560 0.0304  0.0006  -0.0500 162  ARG B NH1 
10140 N NH2 . ARG B 164  ? 0.4433 0.3938 0.3679 0.0355  0.0029  -0.0533 162  ARG B NH2 
10141 N N   . SER B 165  ? 0.2377 0.2233 0.1822 0.0386  0.0135  -0.0444 163  SER B N   
10142 C CA  . SER B 165  ? 0.2110 0.2010 0.1544 0.0412  0.0167  -0.0447 163  SER B CA  
10143 C C   . SER B 165  ? 0.2345 0.2253 0.1729 0.0402  0.0175  -0.0451 163  SER B C   
10144 O O   . SER B 165  ? 0.2297 0.2203 0.1640 0.0426  0.0195  -0.0467 163  SER B O   
10145 C CB  . SER B 165  ? 0.2221 0.2197 0.1718 0.0411  0.0180  -0.0424 163  SER B CB  
10146 O OG  . SER B 165  ? 0.2531 0.2561 0.2022 0.0431  0.0211  -0.0423 163  SER B OG  
10147 N N   . LEU B 166  ? 0.2353 0.2271 0.1740 0.0368  0.0159  -0.0437 164  LEU B N   
10148 C CA  . LEU B 166  ? 0.2301 0.2225 0.1639 0.0357  0.0164  -0.0437 164  LEU B CA  
10149 C C   . LEU B 166  ? 0.2512 0.2367 0.1782 0.0362  0.0153  -0.0463 164  LEU B C   
10150 O O   . LEU B 166  ? 0.2516 0.2372 0.1734 0.0372  0.0169  -0.0474 164  LEU B O   
10151 C CB  . LEU B 166  ? 0.2317 0.2261 0.1676 0.0320  0.0147  -0.0415 164  LEU B CB  
10152 C CG  . LEU B 166  ? 0.2298 0.2315 0.1712 0.0314  0.0162  -0.0391 164  LEU B CG  
10153 C CD1 . LEU B 166  ? 0.2921 0.2948 0.2359 0.0280  0.0143  -0.0370 164  LEU B CD1 
10154 C CD2 . LEU B 166  ? 0.2449 0.2515 0.1843 0.0326  0.0194  -0.0389 164  LEU B CD2 
10155 N N   . ALA B 167  ? 0.2354 0.2150 0.1621 0.0354  0.0125  -0.0472 165  ALA B N   
10156 C CA  . ALA B 167  ? 0.2407 0.2134 0.1609 0.0357  0.0112  -0.0497 165  ALA B CA  
10157 C C   . ALA B 167  ? 0.2629 0.2337 0.1796 0.0396  0.0136  -0.0521 165  ALA B C   
10158 O O   . ALA B 167  ? 0.2764 0.2445 0.1866 0.0405  0.0143  -0.0539 165  ALA B O   
10159 C CB  . ALA B 167  ? 0.2675 0.2347 0.1891 0.0341  0.0079  -0.0501 165  ALA B CB  
10160 N N   . ALA B 168  ? 0.2525 0.2247 0.1733 0.0420  0.0149  -0.0520 166  ALA B N   
10161 C CA  . ALA B 168  ? 0.2492 0.2201 0.1673 0.0460  0.0174  -0.0541 166  ALA B CA  
10162 C C   . ALA B 168  ? 0.2324 0.2087 0.1481 0.0475  0.0207  -0.0540 166  ALA B C   
10163 O O   . ALA B 168  ? 0.2652 0.2390 0.1751 0.0499  0.0222  -0.0562 166  ALA B O   
10164 C CB  . ALA B 168  ? 0.2624 0.2352 0.1864 0.0482  0.0182  -0.0534 166  ALA B CB  
10165 N N   . ALA B 169  ? 0.2310 0.2149 0.1511 0.0460  0.0217  -0.0514 167  ALA B N   
10166 C CA  . ALA B 169  ? 0.2491 0.2389 0.1676 0.0471  0.0249  -0.0509 167  ALA B CA  
10167 C C   . ALA B 169  ? 0.2641 0.2514 0.1754 0.0457  0.0247  -0.0519 167  ALA B C   
10168 O O   . ALA B 169  ? 0.2610 0.2497 0.1679 0.0478  0.0273  -0.0531 167  ALA B O   
10169 C CB  . ALA B 169  ? 0.2507 0.2485 0.1755 0.0451  0.0257  -0.0478 167  ALA B CB  
10170 N N   . LEU B 170  ? 0.2503 0.2341 0.1602 0.0423  0.0215  -0.0514 168  LEU B N   
10171 C CA  . LEU B 170  ? 0.2523 0.2334 0.1552 0.0408  0.0209  -0.0522 168  LEU B CA  
10172 C C   . LEU B 170  ? 0.2729 0.2471 0.1688 0.0431  0.0209  -0.0556 168  LEU B C   
10173 O O   . LEU B 170  ? 0.2840 0.2579 0.1736 0.0442  0.0226  -0.0569 168  LEU B O   
10174 C CB  . LEU B 170  ? 0.2709 0.2499 0.1745 0.0368  0.0173  -0.0508 168  LEU B CB  
10175 C CG  . LEU B 170  ? 0.2779 0.2551 0.1748 0.0350  0.0165  -0.0510 168  LEU B CG  
10176 C CD1 . LEU B 170  ? 0.3091 0.2927 0.2048 0.0352  0.0196  -0.0497 168  LEU B CD1 
10177 C CD2 . LEU B 170  ? 0.3138 0.2893 0.2124 0.0313  0.0129  -0.0494 168  LEU B CD2 
10178 N N   . THR B 171  ? 0.2842 0.2524 0.1806 0.0438  0.0189  -0.0571 169  THR B N   
10179 C CA  . THR B 171  ? 0.3009 0.2620 0.1908 0.0462  0.0189  -0.0605 169  THR B CA  
10180 C C   . THR B 171  ? 0.2974 0.2611 0.1853 0.0505  0.0230  -0.0618 169  THR B C   
10181 O O   . THR B 171  ? 0.3068 0.2674 0.1874 0.0521  0.0242  -0.0641 169  THR B O   
10182 C CB  . THR B 171  ? 0.3160 0.2712 0.2082 0.0464  0.0164  -0.0614 169  THR B CB  
10183 O OG1 . THR B 171  ? 0.3571 0.3100 0.2508 0.0424  0.0127  -0.0603 169  THR B OG1 
10184 C CG2 . THR B 171  ? 0.3411 0.2885 0.2265 0.0489  0.0164  -0.0649 169  THR B CG2 
10185 N N   . ARG B 172  ? 0.2768 0.2463 0.1711 0.0523  0.0251  -0.0604 170  ARG B N   
10186 C CA  . ARG B 172  ? 0.2780 0.2505 0.1713 0.0567  0.0290  -0.0615 170  ARG B CA  
10187 C C   . ARG B 172  ? 0.2751 0.2525 0.1644 0.0567  0.0317  -0.0612 170  ARG B C   
10188 O O   . ARG B 172  ? 0.2893 0.2651 0.1728 0.0596  0.0340  -0.0635 170  ARG B O   
10189 C CB  . ARG B 172  ? 0.2812 0.2599 0.1828 0.0583  0.0305  -0.0596 170  ARG B CB  
10190 C CG  . ARG B 172  ? 0.2671 0.2481 0.1682 0.0633  0.0342  -0.0610 170  ARG B CG  
10191 C CD  . ARG B 172  ? 0.2603 0.2486 0.1701 0.0646  0.0356  -0.0588 170  ARG B CD  
10192 N NE  . ARG B 172  ? 0.2570 0.2429 0.1720 0.0628  0.0326  -0.0576 170  ARG B NE  
10193 C CZ  . ARG B 172  ? 0.2560 0.2463 0.1766 0.0594  0.0311  -0.0548 170  ARG B CZ  
10194 N NH1 . ARG B 172  ? 0.2661 0.2630 0.1880 0.0572  0.0321  -0.0528 170  ARG B NH1 
10195 N NH2 . ARG B 172  ? 0.2495 0.2372 0.1743 0.0581  0.0286  -0.0540 170  ARG B NH2 
10196 N N   . LEU B 173  ? 0.2947 0.2780 0.1871 0.0534  0.0315  -0.0583 171  LEU B N   
10197 C CA  . LEU B 173  ? 0.2751 0.2636 0.1641 0.0534  0.0343  -0.0577 171  LEU B CA  
10198 C C   . LEU B 173  ? 0.3096 0.2923 0.1893 0.0526  0.0334  -0.0597 171  LEU B C   
10199 O O   . LEU B 173  ? 0.3039 0.2882 0.1784 0.0545  0.0363  -0.0608 171  LEU B O   
10200 C CB  . LEU B 173  ? 0.2991 0.2950 0.1935 0.0500  0.0342  -0.0541 171  LEU B CB  
10201 C CG  . LEU B 173  ? 0.2932 0.2870 0.1874 0.0454  0.0307  -0.0524 171  LEU B CG  
10202 C CD1 . LEU B 173  ? 0.3270 0.3211 0.2145 0.0438  0.0313  -0.0523 171  LEU B CD1 
10203 C CD2 . LEU B 173  ? 0.2944 0.2944 0.1967 0.0431  0.0303  -0.0492 171  LEU B CD2 
10204 N N   . ILE B 174  ? 0.3073 0.2835 0.1848 0.0498  0.0294  -0.0602 172  ILE B N   
10205 C CA  . ILE B 174  ? 0.3069 0.2773 0.1753 0.0490  0.0283  -0.0622 172  ILE B CA  
10206 C C   . ILE B 174  ? 0.3398 0.3042 0.2019 0.0528  0.0295  -0.0659 172  ILE B C   
10207 O O   . ILE B 174  ? 0.3575 0.3203 0.2120 0.0540  0.0311  -0.0677 172  ILE B O   
10208 C CB  . ILE B 174  ? 0.3165 0.2818 0.1845 0.0450  0.0236  -0.0616 172  ILE B CB  
10209 C CG1 . ILE B 174  ? 0.3295 0.3005 0.2023 0.0414  0.0226  -0.0580 172  ILE B CG1 
10210 C CG2 . ILE B 174  ? 0.3485 0.3072 0.2068 0.0444  0.0221  -0.0640 172  ILE B CG2 
10211 C CD1 . ILE B 174  ? 0.3442 0.3112 0.2183 0.0378  0.0181  -0.0572 172  ILE B CD1 
10212 N N   . SER B 175  ? 0.3407 0.3012 0.2057 0.0547  0.0287  -0.0673 173  SER B N   
10213 C CA  . SER B 175  ? 0.3410 0.2951 0.2001 0.0585  0.0298  -0.0709 173  SER B CA  
10214 C C   . SER B 175  ? 0.3147 0.2739 0.1727 0.0628  0.0347  -0.0716 173  SER B C   
10215 O O   . SER B 175  ? 0.3788 0.3336 0.2297 0.0658  0.0363  -0.0747 173  SER B O   
10216 C CB  . SER B 175  ? 0.3646 0.3134 0.2274 0.0596  0.0279  -0.0719 173  SER B CB  
10217 O OG  . SER B 175  ? 0.4324 0.3761 0.2955 0.0558  0.0234  -0.0715 173  SER B OG  
10218 N N   . ARG B 176  ? 0.3267 0.2954 0.1916 0.0630  0.0371  -0.0688 174  ARG B N   
10219 C CA  . ARG B 176  ? 0.3220 0.2967 0.1869 0.0670  0.0419  -0.0692 174  ARG B CA  
10220 C C   . ARG B 176  ? 0.3499 0.3286 0.2093 0.0660  0.0441  -0.0687 174  ARG B C   
10221 O O   . ARG B 176  ? 0.3745 0.3536 0.2287 0.0694  0.0474  -0.0707 174  ARG B O   
10222 C CB  . ARG B 176  ? 0.3333 0.3167 0.2083 0.0676  0.0434  -0.0663 174  ARG B CB  
10223 C CG  . ARG B 176  ? 0.3464 0.3365 0.2226 0.0721  0.0482  -0.0666 174  ARG B CG  
10224 C CD  . ARG B 176  ? 0.3195 0.3175 0.2061 0.0726  0.0490  -0.0638 174  ARG B CD  
10225 N NE  . ARG B 176  ? 0.3222 0.3279 0.2135 0.0686  0.0489  -0.0602 174  ARG B NE  
10226 C CZ  . ARG B 176  ? 0.3294 0.3363 0.2268 0.0651  0.0460  -0.0578 174  ARG B CZ  
10227 N NH1 . ARG B 176  ? 0.3133 0.3148 0.2134 0.0649  0.0431  -0.0583 174  ARG B NH1 
10228 N NH2 . ARG B 176  ? 0.3662 0.3796 0.2668 0.0616  0.0461  -0.0548 174  ARG B NH2 
10229 N N   . CYS B 177  ? 0.3453 0.3269 0.2060 0.0615  0.0423  -0.0660 175  CYS B N   
10230 C CA  . CYS B 177  ? 0.3629 0.3499 0.2201 0.0603  0.0447  -0.0648 175  CYS B CA  
10231 C C   . CYS B 177  ? 0.3976 0.3794 0.2473 0.0570  0.0420  -0.0652 175  CYS B C   
10232 O O   . CYS B 177  ? 0.4152 0.3998 0.2598 0.0565  0.0441  -0.0648 175  CYS B O   
10233 C CB  . CYS B 177  ? 0.3611 0.3578 0.2262 0.0581  0.0457  -0.0607 175  CYS B CB  
10234 S SG  . CYS B 177  ? 0.4395 0.4438 0.3144 0.0615  0.0486  -0.0596 175  CYS B SG  
10235 N N   . GLY B 178  ? 0.3876 0.3622 0.2366 0.0546  0.0376  -0.0658 176  GLY B N   
10236 C CA  . GLY B 178  ? 0.3970 0.3658 0.2377 0.0522  0.0351  -0.0669 176  GLY B CA  
10237 C C   . GLY B 178  ? 0.3911 0.3643 0.2320 0.0482  0.0343  -0.0637 176  GLY B C   
10238 O O   . GLY B 178  ? 0.3765 0.3562 0.2247 0.0463  0.0345  -0.0605 176  GLY B O   
10239 N N   . GLU B 179  ? 0.3909 0.3602 0.2232 0.0468  0.0332  -0.0647 177  GLU B N   
10240 C CA  . GLU B 179  ? 0.4197 0.3922 0.2510 0.0430  0.0322  -0.0618 177  GLU B CA  
10241 C C   . GLU B 179  ? 0.3500 0.3319 0.1848 0.0429  0.0360  -0.0589 177  GLU B C   
10242 O O   . GLU B 179  ? 0.3643 0.3501 0.2036 0.0396  0.0347  -0.0556 177  GLU B O   
10243 C CB  . GLU B 179  ? 0.4581 0.4247 0.2787 0.0419  0.0306  -0.0635 177  GLU B CB  
10244 C CG  . GLU B 179  ? 0.4778 0.4475 0.2968 0.0381  0.0297  -0.0604 177  GLU B CG  
10245 C CD  . GLU B 179  ? 0.6905 0.6541 0.4996 0.0366  0.0272  -0.0618 177  GLU B CD  
10246 O OE1 . GLU B 179  ? 0.7194 0.6756 0.5235 0.0378  0.0254  -0.0652 177  GLU B OE1 
10247 O OE2 . GLU B 179  ? 0.7806 0.7466 0.5868 0.0341  0.0269  -0.0595 177  GLU B OE2 
10248 N N   . PRO B 180  ? 0.3737 0.3599 0.2072 0.0463  0.0406  -0.0598 178  PRO B N   
10249 C CA  . PRO B 180  ? 0.3855 0.3812 0.2226 0.0457  0.0441  -0.0568 178  PRO B CA  
10250 C C   . PRO B 180  ? 0.3986 0.3999 0.2464 0.0439  0.0433  -0.0536 178  PRO B C   
10251 O O   . PRO B 180  ? 0.4006 0.4075 0.2509 0.0410  0.0438  -0.0503 178  PRO B O   
10252 C CB  . PRO B 180  ? 0.4062 0.4051 0.2413 0.0504  0.0489  -0.0588 178  PRO B CB  
10253 C CG  . PRO B 180  ? 0.4506 0.4408 0.2763 0.0525  0.0481  -0.0628 178  PRO B CG  
10254 C CD  . PRO B 180  ? 0.4190 0.4014 0.2462 0.0506  0.0430  -0.0637 178  PRO B CD  
10255 N N   . VAL B 181  ? 0.3397 0.3395 0.1936 0.0453  0.0421  -0.0544 179  VAL B N   
10256 C CA  . VAL B 181  ? 0.3276 0.3328 0.1912 0.0434  0.0414  -0.0514 179  VAL B CA  
10257 C C   . VAL B 181  ? 0.3161 0.3185 0.1812 0.0390  0.0371  -0.0494 179  VAL B C   
10258 O O   . VAL B 181  ? 0.3272 0.3346 0.1979 0.0365  0.0368  -0.0462 179  VAL B O   
10259 C CB  . VAL B 181  ? 0.3269 0.3323 0.1971 0.0463  0.0417  -0.0524 179  VAL B CB  
10260 C CG1 . VAL B 181  ? 0.3440 0.3406 0.2134 0.0461  0.0377  -0.0544 179  VAL B CG1 
10261 C CG2 . VAL B 181  ? 0.3756 0.3884 0.2553 0.0448  0.0421  -0.0492 179  VAL B CG2 
10262 N N   . ILE B 182  ? 0.3238 0.3182 0.1840 0.0382  0.0337  -0.0512 180  ILE B N   
10263 C CA  . ILE B 182  ? 0.3474 0.3391 0.2085 0.0342  0.0296  -0.0494 180  ILE B CA  
10264 C C   . ILE B 182  ? 0.3558 0.3510 0.2138 0.0315  0.0302  -0.0468 180  ILE B C   
10265 O O   . ILE B 182  ? 0.3530 0.3509 0.2155 0.0285  0.0288  -0.0438 180  ILE B O   
10266 C CB  . ILE B 182  ? 0.3537 0.3365 0.2098 0.0338  0.0259  -0.0519 180  ILE B CB  
10267 C CG1 . ILE B 182  ? 0.3454 0.3246 0.2050 0.0362  0.0252  -0.0541 180  ILE B CG1 
10268 C CG2 . ILE B 182  ? 0.3695 0.3501 0.2266 0.0298  0.0217  -0.0499 180  ILE B CG2 
10269 C CD1 . ILE B 182  ? 0.3879 0.3583 0.2416 0.0365  0.0223  -0.0571 180  ILE B CD1 
10270 N N   . ARG B 183  ? 0.3873 0.3823 0.2375 0.0326  0.0325  -0.0480 181  ARG B N   
10271 C CA  . ARG B 183  ? 0.3924 0.3907 0.2390 0.0301  0.0334  -0.0455 181  ARG B CA  
10272 C C   . ARG B 183  ? 0.4001 0.4070 0.2535 0.0292  0.0360  -0.0423 181  ARG B C   
10273 O O   . ARG B 183  ? 0.4101 0.4190 0.2651 0.0258  0.0348  -0.0392 181  ARG B O   
10274 C CB  . ARG B 183  ? 0.4089 0.4059 0.2459 0.0320  0.0359  -0.0476 181  ARG B CB  
10275 C CG  . ARG B 183  ? 0.5438 0.5454 0.3768 0.0301  0.0380  -0.0451 181  ARG B CG  
10276 C CD  . ARG B 183  ? 0.5609 0.5611 0.3943 0.0258  0.0344  -0.0421 181  ARG B CD  
10277 N NE  . ARG B 183  ? 0.6175 0.6096 0.4462 0.0248  0.0300  -0.0438 181  ARG B NE  
10278 C CZ  . ARG B 183  ? 0.5600 0.5495 0.3905 0.0217  0.0259  -0.0420 181  ARG B CZ  
10279 N NH1 . ARG B 183  ? 0.5572 0.5509 0.3942 0.0193  0.0255  -0.0385 181  ARG B NH1 
10280 N NH2 . ARG B 183  ? 0.5733 0.5558 0.3993 0.0210  0.0221  -0.0437 181  ARG B NH2 
10281 N N   . ARG B 184  ? 0.4020 0.4139 0.2594 0.0321  0.0396  -0.0428 182  ARG B N   
10282 C CA  . ARG B 184  ? 0.3969 0.4174 0.2613 0.0311  0.0419  -0.0398 182  ARG B CA  
10283 C C   . ARG B 184  ? 0.3900 0.4107 0.2621 0.0284  0.0389  -0.0376 182  ARG B C   
10284 O O   . ARG B 184  ? 0.3953 0.4206 0.2708 0.0256  0.0390  -0.0344 182  ARG B O   
10285 C CB  . ARG B 184  ? 0.4071 0.4327 0.2748 0.0350  0.0459  -0.0410 182  ARG B CB  
10286 C CG  . ARG B 184  ? 0.4751 0.5034 0.3364 0.0374  0.0501  -0.0422 182  ARG B CG  
10287 C CD  . ARG B 184  ? 0.5310 0.5679 0.3940 0.0354  0.0531  -0.0389 182  ARG B CD  
10288 N NE  . ARG B 184  ? 0.4489 0.4939 0.3198 0.0372  0.0561  -0.0379 182  ARG B NE  
10289 C CZ  . ARG B 184  ? 0.4525 0.5035 0.3310 0.0346  0.0560  -0.0347 182  ARG B CZ  
10290 N NH1 . ARG B 184  ? 0.4954 0.5451 0.3748 0.0303  0.0532  -0.0321 182  ARG B NH1 
10291 N NH2 . ARG B 184  ? 0.4922 0.5504 0.3774 0.0365  0.0587  -0.0340 182  ARG B NH2 
10292 N N   . GLY B 185  ? 0.3831 0.3991 0.2582 0.0293  0.0361  -0.0392 183  GLY B N   
10293 C CA  . GLY B 185  ? 0.3549 0.3710 0.2371 0.0269  0.0333  -0.0373 183  GLY B CA  
10294 C C   . GLY B 185  ? 0.3832 0.3966 0.2633 0.0230  0.0302  -0.0352 183  GLY B C   
10295 O O   . GLY B 185  ? 0.3560 0.3725 0.2410 0.0205  0.0294  -0.0324 183  GLY B O   
10296 N N   . VAL B 186  ? 0.3659 0.3734 0.2386 0.0227  0.0283  -0.0366 184  VAL B N   
10297 C CA  . VAL B 186  ? 0.4014 0.4061 0.2717 0.0193  0.0252  -0.0348 184  VAL B CA  
10298 C C   . VAL B 186  ? 0.3901 0.4000 0.2595 0.0171  0.0272  -0.0317 184  VAL B C   
10299 O O   . VAL B 186  ? 0.3909 0.4018 0.2635 0.0142  0.0255  -0.0289 184  VAL B O   
10300 C CB  . VAL B 186  ? 0.3775 0.3753 0.2396 0.0195  0.0230  -0.0370 184  VAL B CB  
10301 C CG1 . VAL B 186  ? 0.4183 0.4143 0.2765 0.0162  0.0205  -0.0348 184  VAL B CG1 
10302 C CG2 . VAL B 186  ? 0.3830 0.3753 0.2471 0.0204  0.0199  -0.0393 184  VAL B CG2 
10303 N N   . ASP B 187  ? 0.3808 0.3940 0.2457 0.0185  0.0308  -0.0321 185  ASP B N   
10304 C CA  . ASP B 187  ? 0.4452 0.4636 0.3091 0.0164  0.0330  -0.0291 185  ASP B CA  
10305 C C   . ASP B 187  ? 0.4548 0.4794 0.3274 0.0151  0.0341  -0.0265 185  ASP B C   
10306 O O   . ASP B 187  ? 0.4125 0.4391 0.2863 0.0120  0.0336  -0.0234 185  ASP B O   
10307 C CB  . ASP B 187  ? 0.4205 0.4419 0.2786 0.0185  0.0372  -0.0303 185  ASP B CB  
10308 C CG  . ASP B 187  ? 0.4607 0.4760 0.3090 0.0192  0.0361  -0.0325 185  ASP B CG  
10309 O OD1 . ASP B 187  ? 0.5167 0.5262 0.3626 0.0174  0.0321  -0.0324 185  ASP B OD1 
10310 O OD2 . ASP B 187  ? 0.4922 0.5087 0.3352 0.0216  0.0393  -0.0342 185  ASP B OD2 
10311 N N   . MET B 188  ? 0.4195 0.4467 0.2981 0.0175  0.0354  -0.0278 186  MET B N   
10312 C CA  . MET B 188  ? 0.4116 0.4446 0.2985 0.0164  0.0362  -0.0255 186  MET B CA  
10313 C C   . MET B 188  ? 0.3892 0.4193 0.2803 0.0135  0.0323  -0.0238 186  MET B C   
10314 O O   . MET B 188  ? 0.4156 0.4489 0.3099 0.0107  0.0323  -0.0209 186  MET B O   
10315 C CB  . MET B 188  ? 0.4042 0.4400 0.2962 0.0198  0.0380  -0.0274 186  MET B CB  
10316 C CG  . MET B 188  ? 0.4792 0.5213 0.3796 0.0189  0.0390  -0.0253 186  MET B CG  
10317 S SD  . MET B 188  ? 0.6654 0.7158 0.5660 0.0166  0.0425  -0.0220 186  MET B SD  
10318 C CE  . MET B 188  ? 0.6009 0.6538 0.4954 0.0203  0.0468  -0.0242 186  MET B CE  
10319 N N   . ALA B 189  ? 0.3920 0.4159 0.2830 0.0142  0.0291  -0.0256 187  ALA B N   
10320 C CA  . ALA B 189  ? 0.3904 0.4116 0.2855 0.0117  0.0255  -0.0241 187  ALA B CA  
10321 C C   . ALA B 189  ? 0.3983 0.4177 0.2895 0.0086  0.0238  -0.0218 187  ALA B C   
10322 O O   . ALA B 189  ? 0.3989 0.4189 0.2938 0.0061  0.0223  -0.0194 187  ALA B O   
10323 C CB  . ALA B 189  ? 0.4172 0.4324 0.3128 0.0131  0.0226  -0.0265 187  ALA B CB  
10324 N N   . MET B 190  ? 0.3791 0.3958 0.2625 0.0087  0.0240  -0.0225 188  MET B N   
10325 C CA  . MET B 190  ? 0.4197 0.4347 0.2987 0.0058  0.0224  -0.0202 188  MET B CA  
10326 C C   . MET B 190  ? 0.4407 0.4613 0.3219 0.0036  0.0247  -0.0169 188  MET B C   
10327 O O   . MET B 190  ? 0.4286 0.4484 0.3113 0.0008  0.0227  -0.0143 188  MET B O   
10328 C CB  . MET B 190  ? 0.4458 0.4578 0.3156 0.0066  0.0228  -0.0216 188  MET B CB  
10329 C CG  . MET B 190  ? 0.5085 0.5173 0.3732 0.0038  0.0204  -0.0195 188  MET B CG  
10330 S SD  . MET B 190  ? 0.6231 0.6291 0.4765 0.0047  0.0212  -0.0210 188  MET B SD  
10331 C CE  . MET B 190  ? 0.4868 0.4887 0.3393 0.0082  0.0205  -0.0256 188  MET B CE  
10332 N N   . ARG B 191  ? 0.3950 0.4215 0.2767 0.0048  0.0287  -0.0170 189  ARG B N   
10333 C CA  . ARG B 191  ? 0.4280 0.4604 0.3121 0.0025  0.0309  -0.0139 189  ARG B CA  
10334 C C   . ARG B 191  ? 0.4707 0.5050 0.3632 0.0011  0.0297  -0.0124 189  ARG B C   
10335 O O   . ARG B 191  ? 0.4158 0.4508 0.3098 -0.0020 0.0289  -0.0095 189  ARG B O   
10336 C CB  . ARG B 191  ? 0.4401 0.4790 0.3236 0.0045  0.0356  -0.0145 189  ARG B CB  
10337 C CG  . ARG B 191  ? 0.5589 0.6044 0.4442 0.0019  0.0381  -0.0112 189  ARG B CG  
10338 C CD  . ARG B 191  ? 0.6368 0.6893 0.5222 0.0041  0.0429  -0.0118 189  ARG B CD  
10339 N NE  . ARG B 191  ? 0.7039 0.7603 0.5965 0.0065  0.0440  -0.0132 189  ARG B NE  
10340 C CZ  . ARG B 191  ? 0.7082 0.7708 0.6023 0.0090  0.0479  -0.0141 189  ARG B CZ  
10341 N NH1 . ARG B 191  ? 0.7574 0.8234 0.6464 0.0096  0.0512  -0.0139 189  ARG B NH1 
10342 N NH2 . ARG B 191  ? 0.7505 0.8160 0.6513 0.0112  0.0484  -0.0152 189  ARG B NH2 
10343 N N   . MET B 192  ? 0.3993 0.4341 0.2971 0.0033  0.0296  -0.0143 190  MET B N   
10344 C CA  . MET B 192  ? 0.3822 0.4189 0.2878 0.0022  0.0285  -0.0131 190  MET B CA  
10345 C C   . MET B 192  ? 0.4290 0.4604 0.3351 -0.0002 0.0246  -0.0118 190  MET B C   
10346 O O   . MET B 192  ? 0.3923 0.4250 0.3015 -0.0029 0.0240  -0.0093 190  MET B O   
10347 C CB  . MET B 192  ? 0.4013 0.4387 0.3117 0.0052  0.0288  -0.0155 190  MET B CB  
10348 C CG  . MET B 192  ? 0.4735 0.5164 0.3842 0.0078  0.0327  -0.0167 190  MET B CG  
10349 S SD  . MET B 192  ? 0.5725 0.6166 0.4900 0.0109  0.0328  -0.0189 190  MET B SD  
10350 C CE  . MET B 192  ? 0.4648 0.5141 0.3902 0.0081  0.0326  -0.0159 190  MET B CE  
10351 N N   . MET B 193  ? 0.3820 0.4073 0.2851 0.0007  0.0219  -0.0135 191  MET B N   
10352 C CA  A MET B 193  ? 0.4227 0.4431 0.3268 -0.0011 0.0181  -0.0125 191  MET B CA  
10353 C CA  B MET B 193  ? 0.4224 0.4430 0.3267 -0.0011 0.0181  -0.0124 191  MET B CA  
10354 C C   . MET B 193  ? 0.4226 0.4410 0.3220 -0.0038 0.0170  -0.0100 191  MET B C   
10355 O O   . MET B 193  ? 0.4232 0.4387 0.3242 -0.0057 0.0143  -0.0084 191  MET B O   
10356 C CB  A MET B 193  ? 0.4302 0.4452 0.3331 0.0008  0.0155  -0.0151 191  MET B CB  
10357 C CB  B MET B 193  ? 0.4303 0.4455 0.3339 0.0007  0.0155  -0.0150 191  MET B CB  
10358 C CG  A MET B 193  ? 0.4045 0.4205 0.3116 0.0035  0.0163  -0.0176 191  MET B CG  
10359 C CG  B MET B 193  ? 0.4274 0.4438 0.3371 0.0027  0.0157  -0.0168 191  MET B CG  
10360 S SD  A MET B 193  ? 0.4218 0.4313 0.3269 0.0053  0.0133  -0.0205 191  MET B SD  
10361 S SD  B MET B 193  ? 0.4463 0.4564 0.3564 0.0040  0.0121  -0.0191 191  MET B SD  
10362 C CE  A MET B 193  ? 0.5022 0.5093 0.4135 0.0037  0.0099  -0.0193 191  MET B CE  
10363 C CE  B MET B 193  ? 0.4385 0.4458 0.3407 0.0060  0.0128  -0.0216 191  MET B CE  
10364 N N   . GLY B 194  ? 0.4091 0.4289 0.3025 -0.0040 0.0190  -0.0096 192  GLY B N   
10365 C CA  . GLY B 194  ? 0.4350 0.4525 0.3231 -0.0064 0.0179  -0.0073 192  GLY B CA  
10366 C C   . GLY B 194  ? 0.4045 0.4266 0.2931 -0.0089 0.0202  -0.0042 192  GLY B C   
10367 O O   . GLY B 194  ? 0.4160 0.4360 0.3021 -0.0116 0.0188  -0.0016 192  GLY B O   
10368 N N   . GLU B 195  ? 0.3870 0.4153 0.2789 -0.0083 0.0236  -0.0043 193  GLU B N   
10369 C CA  . GLU B 195  ? 0.4412 0.4746 0.3333 -0.0107 0.0262  -0.0015 193  GLU B CA  
10370 C C   . GLU B 195  ? 0.4014 0.4403 0.3012 -0.0113 0.0276  -0.0007 193  GLU B C   
10371 O O   . GLU B 195  ? 0.3717 0.4139 0.2726 -0.0141 0.0288  0.0022  193  GLU B O   
10372 C CB  . GLU B 195  ? 0.4551 0.4923 0.3419 -0.0095 0.0298  -0.0020 193  GLU B CB  
10373 C CG  . GLU B 195  ? 0.5841 0.6164 0.4626 -0.0086 0.0288  -0.0032 193  GLU B CG  
10374 C CD  . GLU B 195  ? 0.6224 0.6585 0.4962 -0.0067 0.0326  -0.0045 193  GLU B CD  
10375 O OE1 . GLU B 195  ? 0.6696 0.7121 0.5446 -0.0076 0.0360  -0.0029 193  GLU B OE1 
10376 O OE2 . GLU B 195  ? 0.6953 0.7280 0.5641 -0.0043 0.0322  -0.0072 193  GLU B OE2 
10377 N N   . GLN B 196  ? 0.4036 0.4434 0.3086 -0.0090 0.0275  -0.0029 194  GLN B N   
10378 C CA  . GLN B 196  ? 0.4111 0.4563 0.3234 -0.0094 0.0289  -0.0022 194  GLN B CA  
10379 C C   . GLN B 196  ? 0.4370 0.4790 0.3544 -0.0104 0.0257  -0.0019 194  GLN B C   
10380 O O   . GLN B 196  ? 0.4652 0.5090 0.3861 -0.0130 0.0255  0.0003  194  GLN B O   
10381 C CB  . GLN B 196  ? 0.4628 0.5123 0.3774 -0.0059 0.0314  -0.0047 194  GLN B CB  
10382 C CG  . GLN B 196  ? 0.5705 0.6262 0.4925 -0.0059 0.0329  -0.0042 194  GLN B CG  
10383 C CD  . GLN B 196  ? 0.6207 0.6800 0.5446 -0.0020 0.0352  -0.0067 194  GLN B CD  
10384 O OE1 . GLN B 196  ? 0.6663 0.7250 0.5854 0.0003  0.0368  -0.0085 194  GLN B OE1 
10385 N NE2 . GLN B 196  ? 0.6700 0.7327 0.6006 -0.0012 0.0354  -0.0070 194  GLN B NE2 
10386 N N   . PHE B 197  ? 0.3975 0.4346 0.3152 -0.0084 0.0233  -0.0041 195  PHE B N   
10387 C CA  . PHE B 197  ? 0.4084 0.4423 0.3307 -0.0092 0.0204  -0.0039 195  PHE B CA  
10388 C C   . PHE B 197  ? 0.4119 0.4412 0.3318 -0.0121 0.0179  -0.0016 195  PHE B C   
10389 O O   . PHE B 197  ? 0.4365 0.4644 0.3603 -0.0135 0.0161  -0.0006 195  PHE B O   
10390 C CB  . PHE B 197  ? 0.4433 0.4732 0.3663 -0.0064 0.0186  -0.0068 195  PHE B CB  
10391 C CG  . PHE B 197  ? 0.4018 0.4353 0.3275 -0.0034 0.0207  -0.0091 195  PHE B CG  
10392 C CD1 . PHE B 197  ? 0.4849 0.5249 0.4148 -0.0035 0.0233  -0.0084 195  PHE B CD1 
10393 C CD2 . PHE B 197  ? 0.4485 0.4788 0.3723 -0.0006 0.0200  -0.0118 195  PHE B CD2 
10394 C CE1 . PHE B 197  ? 0.5266 0.5699 0.4591 -0.0005 0.0252  -0.0104 195  PHE B CE1 
10395 C CE2 . PHE B 197  ? 0.4685 0.5016 0.3946 0.0022  0.0219  -0.0139 195  PHE B CE2 
10396 C CZ  . PHE B 197  ? 0.4802 0.5198 0.4106 0.0024  0.0245  -0.0131 195  PHE B CZ  
10397 N N   . VAL B 198  ? 0.4094 0.4364 0.3229 -0.0127 0.0177  -0.0009 196  VAL B N   
10398 C CA  . VAL B 198  ? 0.3812 0.4041 0.2920 -0.0154 0.0155  0.0016  196  VAL B CA  
10399 C C   . VAL B 198  ? 0.3764 0.4015 0.2819 -0.0172 0.0176  0.0036  196  VAL B C   
10400 O O   . VAL B 198  ? 0.3967 0.4251 0.2993 -0.0158 0.0202  0.0026  196  VAL B O   
10401 C CB  . VAL B 198  ? 0.3550 0.3711 0.2626 -0.0145 0.0121  0.0006  196  VAL B CB  
10402 C CG1 . VAL B 198  ? 0.3988 0.4128 0.3116 -0.0129 0.0101  -0.0012 196  VAL B CG1 
10403 C CG2 . VAL B 198  ? 0.4124 0.4278 0.3141 -0.0126 0.0128  -0.0011 196  VAL B CG2 
10404 N N   . THR B 199  ? 0.3569 0.3804 0.2612 -0.0203 0.0166  0.0066  197  THR B N   
10405 C CA  A THR B 199  ? 0.3694 0.3940 0.2681 -0.0223 0.0182  0.0088  197  THR B CA  
10406 C CA  B THR B 199  ? 0.3696 0.3942 0.2682 -0.0222 0.0182  0.0088  197  THR B CA  
10407 C C   . THR B 199  ? 0.3982 0.4180 0.2897 -0.0215 0.0166  0.0084  197  THR B C   
10408 O O   . THR B 199  ? 0.4194 0.4407 0.3053 -0.0221 0.0184  0.0093  197  THR B O   
10409 C CB  A THR B 199  ? 0.3717 0.3957 0.2714 -0.0260 0.0175  0.0123  197  THR B CB  
10410 C CB  B THR B 199  ? 0.3715 0.3957 0.2711 -0.0260 0.0177  0.0123  197  THR B CB  
10411 O OG1 A THR B 199  ? 0.3630 0.3911 0.2696 -0.0267 0.0185  0.0124  197  THR B OG1 
10412 O OG1 B THR B 199  ? 0.4195 0.4448 0.3133 -0.0280 0.0192  0.0146  197  THR B OG1 
10413 C CG2 A THR B 199  ? 0.4179 0.4443 0.3126 -0.0284 0.0197  0.0149  197  THR B CG2 
10414 C CG2 B THR B 199  ? 0.3324 0.3496 0.2322 -0.0267 0.0137  0.0129  197  THR B CG2 
10415 N N   . GLY B 200  ? 0.3576 0.3720 0.2492 -0.0202 0.0133  0.0071  198  GLY B N   
10416 C CA  . GLY B 200  ? 0.3588 0.3687 0.2440 -0.0193 0.0115  0.0065  198  GLY B CA  
10417 C C   . GLY B 200  ? 0.3686 0.3737 0.2563 -0.0177 0.0079  0.0048  198  GLY B C   
10418 O O   . GLY B 200  ? 0.3506 0.3552 0.2442 -0.0178 0.0067  0.0047  198  GLY B O   
10419 N N   . GLU B 201  ? 0.4038 0.4055 0.2867 -0.0163 0.0062  0.0033  199  GLU B N   
10420 C CA  . GLU B 201  ? 0.4222 0.4194 0.3070 -0.0150 0.0027  0.0019  199  GLU B CA  
10421 C C   . GLU B 201  ? 0.4028 0.3956 0.2873 -0.0167 -0.0005 0.0044  199  GLU B C   
10422 O O   . GLU B 201  ? 0.4939 0.4841 0.3826 -0.0161 -0.0031 0.0038  199  GLU B O   
10423 C CB  . GLU B 201  ? 0.4778 0.4728 0.3576 -0.0130 0.0019  -0.0006 199  GLU B CB  
10424 N N   . THR B 202  ? 0.3557 0.3475 0.2353 -0.0188 -0.0005 0.0071  200  THR B N   
10425 C CA  . THR B 202  ? 0.3639 0.3514 0.2428 -0.0205 -0.0034 0.0098  200  THR B CA  
10426 C C   . THR B 202  ? 0.3793 0.3684 0.2583 -0.0233 -0.0016 0.0128  200  THR B C   
10427 O O   . THR B 202  ? 0.3503 0.3440 0.2284 -0.0241 0.0017  0.0131  200  THR B O   
10428 C CB  . THR B 202  ? 0.4071 0.3909 0.2787 -0.0206 -0.0055 0.0106  200  THR B CB  
10429 O OG1 . THR B 202  ? 0.4142 0.4002 0.2798 -0.0219 -0.0029 0.0118  200  THR B OG1 
10430 C CG2 . THR B 202  ? 0.4890 0.4713 0.3595 -0.0182 -0.0071 0.0076  200  THR B CG2 
10431 N N   . ILE B 203  ? 0.3344 0.3198 0.2146 -0.0248 -0.0040 0.0152  201  ILE B N   
10432 C CA  . ILE B 203  ? 0.3243 0.3103 0.2044 -0.0277 -0.0027 0.0182  201  ILE B CA  
10433 C C   . ILE B 203  ? 0.3770 0.3637 0.2498 -0.0294 -0.0012 0.0203  201  ILE B C   
10434 O O   . ILE B 203  ? 0.3505 0.3408 0.2230 -0.0315 0.0016  0.0219  201  ILE B O   
10435 C CB  . ILE B 203  ? 0.3314 0.3125 0.2140 -0.0288 -0.0057 0.0201  201  ILE B CB  
10436 C CG1 . ILE B 203  ? 0.3364 0.3183 0.2198 -0.0319 -0.0042 0.0229  201  ILE B CG1 
10437 C CG2 . ILE B 203  ? 0.3645 0.3400 0.2420 -0.0287 -0.0090 0.0217  201  ILE B CG2 
10438 C CD1 . ILE B 203  ? 0.3324 0.3199 0.2214 -0.0322 -0.0013 0.0217  201  ILE B CD1 
10439 N N   . ARG B 204  ? 0.3709 0.3546 0.2378 -0.0286 -0.0030 0.0202  202  ARG B N   
10440 C CA  . ARG B 204  ? 0.4042 0.3885 0.2636 -0.0299 -0.0016 0.0219  202  ARG B CA  
10441 C C   . ARG B 204  ? 0.3381 0.3287 0.1969 -0.0296 0.0027  0.0206  202  ARG B C   
10442 O O   . ARG B 204  ? 0.3973 0.3906 0.2533 -0.0318 0.0053  0.0228  202  ARG B O   
10443 C CB  . ARG B 204  ? 0.4754 0.4559 0.3292 -0.0283 -0.0043 0.0210  202  ARG B CB  
10444 C CG  . ARG B 204  ? 0.6423 0.6195 0.4887 -0.0301 -0.0056 0.0241  202  ARG B CG  
10445 C CD  . ARG B 204  ? 0.4896 0.4625 0.3319 -0.0285 -0.0092 0.0231  202  ARG B CD  
10446 N NE  . ARG B 204  ? 0.4641 0.4391 0.3047 -0.0262 -0.0082 0.0196  202  ARG B NE  
10447 C CZ  . ARG B 204  ? 0.5218 0.4992 0.3562 -0.0263 -0.0057 0.0190  202  ARG B CZ  
10448 N NH1 . ARG B 204  ? 0.5152 0.4940 0.3451 -0.0285 -0.0035 0.0217  202  ARG B NH1 
10449 N NH2 . ARG B 204  ? 0.4992 0.4775 0.3319 -0.0240 -0.0054 0.0156  202  ARG B NH2 
10450 N N   . GLU B 205  ? 0.3772 0.3701 0.2384 -0.0269 0.0036  0.0171  203  GLU B N   
10451 C CA  . GLU B 205  ? 0.3785 0.3773 0.2392 -0.0261 0.0076  0.0155  203  GLU B CA  
10452 C C   . GLU B 205  ? 0.3678 0.3715 0.2343 -0.0276 0.0104  0.0165  203  GLU B C   
10453 O O   . GLU B 205  ? 0.3770 0.3856 0.2418 -0.0286 0.0138  0.0175  203  GLU B O   
10454 C CB  . GLU B 205  ? 0.4224 0.4217 0.2850 -0.0227 0.0075  0.0114  203  GLU B CB  
10455 C CG  . GLU B 205  ? 0.4130 0.4178 0.2750 -0.0212 0.0116  0.0094  203  GLU B CG  
10456 C CD  . GLU B 205  ? 0.5616 0.5659 0.4245 -0.0179 0.0112  0.0055  203  GLU B CD  
10457 O OE1 . GLU B 205  ? 0.5396 0.5429 0.4085 -0.0168 0.0095  0.0040  203  GLU B OE1 
10458 O OE2 . GLU B 205  ? 0.7747 0.7795 0.6321 -0.0165 0.0126  0.0038  203  GLU B OE2 
10459 N N   . ALA B 206  ? 0.3346 0.3374 0.2078 -0.0277 0.0088  0.0164  204  ALA B N   
10460 C CA  . ALA B 206  ? 0.3030 0.3102 0.1819 -0.0292 0.0110  0.0174  204  ALA B CA  
10461 C C   . ALA B 206  ? 0.3442 0.3520 0.2204 -0.0329 0.0121  0.0212  204  ALA B C   
10462 O O   . ALA B 206  ? 0.3312 0.3448 0.2087 -0.0343 0.0153  0.0221  204  ALA B O   
10463 C CB  . ALA B 206  ? 0.3237 0.3284 0.2092 -0.0288 0.0086  0.0167  204  ALA B CB  
10464 N N   . LEU B 207  ? 0.3124 0.3144 0.1849 -0.0345 0.0093  0.0235  205  LEU B N   
10465 C CA  . LEU B 207  ? 0.3519 0.3537 0.2213 -0.0381 0.0100  0.0274  205  LEU B CA  
10466 C C   . LEU B 207  ? 0.3900 0.3959 0.2535 -0.0388 0.0132  0.0282  205  LEU B C   
10467 O O   . LEU B 207  ? 0.3679 0.3778 0.2314 -0.0415 0.0158  0.0306  205  LEU B O   
10468 C CB  . LEU B 207  ? 0.3842 0.3783 0.2501 -0.0392 0.0062  0.0296  205  LEU B CB  
10469 C CG  . LEU B 207  ? 0.4037 0.3939 0.2753 -0.0393 0.0034  0.0297  205  LEU B CG  
10470 C CD1 . LEU B 207  ? 0.4292 0.4120 0.2976 -0.0391 -0.0006 0.0310  205  LEU B CD1 
10471 C CD2 . LEU B 207  ? 0.3582 0.3501 0.2331 -0.0426 0.0047  0.0320  205  LEU B CD2 
10472 N N   . LYS B 208  ? 0.3293 0.3344 0.1878 -0.0364 0.0131  0.0264  206  LYS B N   
10473 C CA  . LYS B 208  ? 0.3640 0.3729 0.2165 -0.0368 0.0164  0.0269  206  LYS B CA  
10474 C C   . LYS B 208  ? 0.3711 0.3881 0.2278 -0.0362 0.0207  0.0256  206  LYS B C   
10475 O O   . LYS B 208  ? 0.3892 0.4109 0.2437 -0.0381 0.0239  0.0275  206  LYS B O   
10476 C CB  . LYS B 208  ? 0.4021 0.4082 0.2485 -0.0341 0.0152  0.0247  206  LYS B CB  
10477 N N   . ARG B 209  ? 0.3818 0.4007 0.2445 -0.0336 0.0207  0.0225  207  ARG B N   
10478 C CA  . ARG B 209  ? 0.3679 0.3945 0.2349 -0.0327 0.0246  0.0211  207  ARG B CA  
10479 C C   . ARG B 209  ? 0.4229 0.4535 0.2954 -0.0357 0.0260  0.0236  207  ARG B C   
10480 O O   . ARG B 209  ? 0.4107 0.4486 0.2863 -0.0355 0.0295  0.0233  207  ARG B O   
10481 C CB  . ARG B 209  ? 0.3922 0.4190 0.2638 -0.0290 0.0240  0.0172  207  ARG B CB  
10482 C CG  . ARG B 209  ? 0.3916 0.4157 0.2577 -0.0259 0.0235  0.0144  207  ARG B CG  
10483 C CD  . ARG B 209  ? 0.4248 0.4489 0.2956 -0.0226 0.0229  0.0107  207  ARG B CD  
10484 N NE  . ARG B 209  ? 0.5658 0.5874 0.4317 -0.0197 0.0224  0.0078  207  ARG B NE  
10485 C CZ  . ARG B 209  ? 0.6043 0.6247 0.4730 -0.0168 0.0215  0.0045  207  ARG B CZ  
10486 N NH1 . ARG B 209  ? 0.4588 0.4805 0.3351 -0.0162 0.0210  0.0036  207  ARG B NH1 
10487 N NH2 . ARG B 209  ? 0.6690 0.6868 0.5325 -0.0145 0.0211  0.0020  207  ARG B NH2 
10488 N N   . SER B 210  ? 0.3421 0.3683 0.2159 -0.0383 0.0233  0.0260  208  SER B N   
10489 C CA  . SER B 210  ? 0.3446 0.3740 0.2237 -0.0414 0.0241  0.0282  208  SER B CA  
10490 C C   . SER B 210  ? 0.3451 0.3779 0.2207 -0.0449 0.0267  0.0317  208  SER B C   
10491 O O   . SER B 210  ? 0.3694 0.4068 0.2494 -0.0475 0.0283  0.0334  208  SER B O   
10492 C CB  . SER B 210  ? 0.3053 0.3280 0.1869 -0.0427 0.0202  0.0291  208  SER B CB  
10493 O OG  . SER B 210  ? 0.3965 0.4171 0.2822 -0.0395 0.0183  0.0259  208  SER B OG  
10494 N N   . LYS B 211  ? 0.3511 0.3819 0.2190 -0.0453 0.0270  0.0330  209  LYS B N   
10495 C CA  . LYS B 211  ? 0.3453 0.3786 0.2094 -0.0490 0.0291  0.0367  209  LYS B CA  
10496 C C   . LYS B 211  ? 0.3590 0.4021 0.2262 -0.0495 0.0338  0.0368  209  LYS B C   
10497 O O   . LYS B 211  ? 0.4052 0.4518 0.2737 -0.0532 0.0354  0.0400  209  LYS B O   
10498 C CB  . LYS B 211  ? 0.3962 0.4258 0.2510 -0.0489 0.0288  0.0377  209  LYS B CB  
10499 C CG  . LYS B 211  ? 0.4677 0.4883 0.3195 -0.0477 0.0242  0.0372  209  LYS B CG  
10500 C CD  . LYS B 211  ? 0.4868 0.5019 0.3414 -0.0503 0.0209  0.0396  209  LYS B CD  
10501 C CE  . LYS B 211  ? 0.6126 0.6190 0.4633 -0.0492 0.0166  0.0395  209  LYS B CE  
10502 N NZ  . LYS B 211  ? 0.5925 0.5930 0.4463 -0.0510 0.0132  0.0413  209  LYS B NZ  
10503 N N   . GLU B 212  ? 0.3724 0.4200 0.2410 -0.0457 0.0359  0.0334  210  GLU B N   
10504 C CA  . GLU B 212  ? 0.4359 0.4932 0.3070 -0.0456 0.0405  0.0334  210  GLU B CA  
10505 C C   . GLU B 212  ? 0.3661 0.4283 0.2453 -0.0480 0.0412  0.0348  210  GLU B C   
10506 O O   . GLU B 212  ? 0.3628 0.4310 0.2429 -0.0510 0.0440  0.0376  210  GLU B O   
10507 C CB  . GLU B 212  ? 0.4922 0.5523 0.3639 -0.0407 0.0422  0.0292  210  GLU B CB  
10508 C CG  . GLU B 212  ? 0.5959 0.6661 0.4706 -0.0398 0.0470  0.0289  210  GLU B CG  
10509 C CD  . GLU B 212  ? 0.6977 0.7705 0.5753 -0.0349 0.0482  0.0246  210  GLU B CD  
10510 O OE1 . GLU B 212  ? 0.8034 0.8701 0.6780 -0.0320 0.0459  0.0219  210  GLU B OE1 
10511 O OE2 . GLU B 212  ? 0.7430 0.8238 0.6259 -0.0340 0.0512  0.0241  210  GLU B OE2 
10512 N N   . LEU B 213  ? 0.3466 0.4064 0.2319 -0.0469 0.0387  0.0330  211  LEU B N   
10513 C CA  . LEU B 213  ? 0.3421 0.4062 0.2350 -0.0492 0.0390  0.0341  211  LEU B CA  
10514 C C   . LEU B 213  ? 0.3386 0.3984 0.2312 -0.0540 0.0368  0.0378  211  LEU B C   
10515 O O   . LEU B 213  ? 0.3391 0.4036 0.2360 -0.0572 0.0380  0.0399  211  LEU B O   
10516 C CB  . LEU B 213  ? 0.3342 0.3981 0.2336 -0.0461 0.0375  0.0308  211  LEU B CB  
10517 C CG  . LEU B 213  ? 0.3637 0.4334 0.2649 -0.0418 0.0403  0.0275  211  LEU B CG  
10518 C CD1 . LEU B 213  ? 0.3682 0.4380 0.2761 -0.0391 0.0389  0.0247  211  LEU B CD1 
10519 C CD2 . LEU B 213  ? 0.4108 0.4905 0.3134 -0.0428 0.0448  0.0290  211  LEU B CD2 
10520 N N   . GLU B 214  ? 0.3271 0.3780 0.2145 -0.0546 0.0336  0.0386  212  GLU B N   
10521 C CA  . GLU B 214  ? 0.3082 0.3545 0.1944 -0.0592 0.0317  0.0423  212  GLU B CA  
10522 C C   . GLU B 214  ? 0.3551 0.4065 0.2385 -0.0630 0.0347  0.0459  212  GLU B C   
10523 O O   . GLU B 214  ? 0.3765 0.4292 0.2626 -0.0671 0.0348  0.0487  212  GLU B O   
10524 C CB  . GLU B 214  ? 0.3367 0.3728 0.2176 -0.0587 0.0278  0.0426  212  GLU B CB  
10525 C CG  . GLU B 214  ? 0.3205 0.3515 0.2054 -0.0562 0.0245  0.0399  212  GLU B CG  
10526 C CD  . GLU B 214  ? 0.3676 0.3889 0.2482 -0.0559 0.0205  0.0404  212  GLU B CD  
10527 O OE1 . GLU B 214  ? 0.3990 0.4176 0.2727 -0.0565 0.0204  0.0421  212  GLU B OE1 
10528 O OE2 . GLU B 214  ? 0.3618 0.3785 0.2460 -0.0549 0.0176  0.0392  212  GLU B OE2 
10529 N N   . GLU B 215  ? 0.3613 0.4157 0.2392 -0.0617 0.0373  0.0459  213  GLU B N   
10530 C CA  . GLU B 215  ? 0.3525 0.4125 0.2277 -0.0650 0.0407  0.0492  213  GLU B CA  
10531 C C   . GLU B 215  ? 0.3881 0.4581 0.2705 -0.0665 0.0439  0.0497  213  GLU B C   
10532 O O   . GLU B 215  ? 0.4253 0.4997 0.3073 -0.0706 0.0460  0.0532  213  GLU B O   
10533 C CB  . GLU B 215  ? 0.3921 0.4539 0.2602 -0.0627 0.0432  0.0485  213  GLU B CB  
10534 C CG  . GLU B 215  ? 0.4737 0.5263 0.3337 -0.0624 0.0403  0.0491  213  GLU B CG  
10535 C CD  . GLU B 215  ? 0.5931 0.6475 0.4457 -0.0603 0.0427  0.0484  213  GLU B CD  
10536 O OE1 . GLU B 215  ? 0.7315 0.7930 0.5825 -0.0618 0.0467  0.0501  213  GLU B OE1 
10537 O OE2 . GLU B 215  ? 0.6928 0.7414 0.5409 -0.0573 0.0405  0.0462  213  GLU B OE2 
10538 N N   . LYS B 216  ? 0.3542 0.4282 0.2431 -0.0634 0.0443  0.0465  214  LYS B N   
10539 C CA  . LYS B 216  ? 0.3524 0.4359 0.2486 -0.0646 0.0469  0.0469  214  LYS B CA  
10540 C C   . LYS B 216  ? 0.4088 0.4904 0.3108 -0.0680 0.0443  0.0483  214  LYS B C   
10541 O O   . LYS B 216  ? 0.3944 0.4837 0.3023 -0.0702 0.0462  0.0494  214  LYS B O   
10542 C CB  . LYS B 216  ? 0.3685 0.4575 0.2688 -0.0596 0.0487  0.0429  214  LYS B CB  
10543 N N   . GLY B 217  ? 0.3354 0.4072 0.2358 -0.0686 0.0402  0.0482  215  GLY B N   
10544 C CA  . GLY B 217  ? 0.3208 0.3896 0.2258 -0.0717 0.0375  0.0494  215  GLY B CA  
10545 C C   . GLY B 217  ? 0.3486 0.4133 0.2579 -0.0686 0.0347  0.0460  215  GLY B C   
10546 O O   . GLY B 217  ? 0.3419 0.4044 0.2554 -0.0708 0.0326  0.0465  215  GLY B O   
10547 N N   . PHE B 218  ? 0.3096 0.3732 0.2179 -0.0636 0.0346  0.0426  216  PHE B N   
10548 C CA  . PHE B 218  ? 0.2822 0.3407 0.1936 -0.0608 0.0315  0.0396  216  PHE B CA  
10549 C C   . PHE B 218  ? 0.2894 0.3371 0.1963 -0.0613 0.0277  0.0403  216  PHE B C   
10550 O O   . PHE B 218  ? 0.3069 0.3509 0.2074 -0.0627 0.0275  0.0423  216  PHE B O   
10551 C CB  . PHE B 218  ? 0.2915 0.3522 0.2033 -0.0554 0.0326  0.0358  216  PHE B CB  
10552 C CG  . PHE B 218  ? 0.2955 0.3662 0.2128 -0.0539 0.0359  0.0344  216  PHE B CG  
10553 C CD1 . PHE B 218  ? 0.3129 0.3912 0.2286 -0.0542 0.0398  0.0356  216  PHE B CD1 
10554 C CD2 . PHE B 218  ? 0.3106 0.3830 0.2344 -0.0520 0.0351  0.0321  216  PHE B CD2 
10555 C CE1 . PHE B 218  ? 0.3431 0.4307 0.2641 -0.0525 0.0428  0.0343  216  PHE B CE1 
10556 C CE2 . PHE B 218  ? 0.3355 0.4170 0.2643 -0.0504 0.0379  0.0310  216  PHE B CE2 
10557 C CZ  . PHE B 218  ? 0.3200 0.4091 0.2475 -0.0505 0.0418  0.0321  216  PHE B CZ  
10558 N N   . SER B 219  ? 0.2870 0.3296 0.1972 -0.0602 0.0247  0.0385  217  SER B N   
10559 C CA  . SER B 219  ? 0.3029 0.3356 0.2096 -0.0594 0.0211  0.0383  217  SER B CA  
10560 C C   . SER B 219  ? 0.2934 0.3244 0.2025 -0.0547 0.0197  0.0344  217  SER B C   
10561 O O   . SER B 219  ? 0.2577 0.2947 0.1709 -0.0523 0.0216  0.0320  217  SER B O   
10562 C CB  . SER B 219  ? 0.2928 0.3201 0.2009 -0.0629 0.0185  0.0404  217  SER B CB  
10563 O OG  . SER B 219  ? 0.3411 0.3711 0.2559 -0.0629 0.0182  0.0389  217  SER B OG  
10564 N N   . TYR B 220  ? 0.2861 0.3089 0.1929 -0.0533 0.0164  0.0338  218  TYR B N   
10565 C CA  . TYR B 220  ? 0.2616 0.2824 0.1701 -0.0490 0.0150  0.0303  218  TYR B CA  
10566 C C   . TYR B 220  ? 0.2553 0.2689 0.1658 -0.0487 0.0115  0.0298  218  TYR B C   
10567 O O   . TYR B 220  ? 0.2856 0.2935 0.1938 -0.0512 0.0095  0.0321  218  TYR B O   
10568 C CB  . TYR B 220  ? 0.2688 0.2874 0.1714 -0.0465 0.0149  0.0294  218  TYR B CB  
10569 C CG  . TYR B 220  ? 0.2660 0.2917 0.1677 -0.0449 0.0184  0.0283  218  TYR B CG  
10570 C CD1 . TYR B 220  ? 0.2927 0.3227 0.1910 -0.0473 0.0211  0.0307  218  TYR B CD1 
10571 C CD2 . TYR B 220  ? 0.2642 0.2925 0.1684 -0.0411 0.0191  0.0248  218  TYR B CD2 
10572 C CE1 . TYR B 220  ? 0.2911 0.3279 0.1887 -0.0456 0.0246  0.0295  218  TYR B CE1 
10573 C CE2 . TYR B 220  ? 0.2966 0.3310 0.1999 -0.0393 0.0223  0.0236  218  TYR B CE2 
10574 C CZ  . TYR B 220  ? 0.2670 0.3058 0.1670 -0.0415 0.0251  0.0259  218  TYR B CZ  
10575 O OH  . TYR B 220  ? 0.3344 0.3794 0.2334 -0.0396 0.0285  0.0246  218  TYR B OH  
10576 N N   . SER B 221  ? 0.2442 0.2581 0.1588 -0.0455 0.0107  0.0267  219  SER B N   
10577 C CA  . SER B 221  ? 0.2482 0.2554 0.1643 -0.0442 0.0074  0.0255  219  SER B CA  
10578 C C   . SER B 221  ? 0.2602 0.2670 0.1764 -0.0399 0.0069  0.0225  219  SER B C   
10579 O O   . SER B 221  ? 0.2783 0.2902 0.1978 -0.0379 0.0086  0.0202  219  SER B O   
10580 C CB  . SER B 221  ? 0.2549 0.2632 0.1770 -0.0451 0.0071  0.0249  219  SER B CB  
10581 O OG  . SER B 221  ? 0.2711 0.2732 0.1946 -0.0436 0.0041  0.0237  219  SER B OG  
10582 N N   . TYR B 222  ? 0.2559 0.2568 0.1685 -0.0387 0.0045  0.0225  220  TYR B N   
10583 C CA  . TYR B 222  ? 0.2576 0.2579 0.1694 -0.0350 0.0038  0.0198  220  TYR B CA  
10584 C C   . TYR B 222  ? 0.2746 0.2722 0.1910 -0.0328 0.0017  0.0176  220  TYR B C   
10585 O O   . TYR B 222  ? 0.2844 0.2773 0.2020 -0.0335 -0.0005 0.0184  220  TYR B O   
10586 C CB  . TYR B 222  ? 0.2568 0.2527 0.1623 -0.0348 0.0023  0.0209  220  TYR B CB  
10587 C CG  . TYR B 222  ? 0.2372 0.2363 0.1380 -0.0367 0.0047  0.0228  220  TYR B CG  
10588 C CD1 . TYR B 222  ? 0.2721 0.2766 0.1718 -0.0351 0.0074  0.0212  220  TYR B CD1 
10589 C CD2 . TYR B 222  ? 0.2732 0.2701 0.1706 -0.0400 0.0045  0.0262  220  TYR B CD2 
10590 C CE1 . TYR B 222  ? 0.2667 0.2746 0.1621 -0.0367 0.0099  0.0229  220  TYR B CE1 
10591 C CE2 . TYR B 222  ? 0.2649 0.2651 0.1579 -0.0418 0.0069  0.0281  220  TYR B CE2 
10592 C CZ  . TYR B 222  ? 0.2628 0.2687 0.1549 -0.0401 0.0097  0.0263  220  TYR B CZ  
10593 O OH  . TYR B 222  ? 0.2886 0.2981 0.1764 -0.0419 0.0123  0.0281  220  TYR B OH  
10594 N N   . ASP B 223  ? 0.2704 0.2709 0.1890 -0.0299 0.0025  0.0148  221  ASP B N   
10595 C CA  . ASP B 223  ? 0.2963 0.2951 0.2193 -0.0275 0.0008  0.0125  221  ASP B CA  
10596 C C   . ASP B 223  ? 0.2899 0.2864 0.2105 -0.0248 -0.0005 0.0108  221  ASP B C   
10597 O O   . ASP B 223  ? 0.3198 0.3195 0.2392 -0.0232 0.0010  0.0092  221  ASP B O   
10598 C CB  . ASP B 223  ? 0.3015 0.3061 0.2296 -0.0267 0.0030  0.0107  221  ASP B CB  
10599 C CG  . ASP B 223  ? 0.3655 0.3692 0.2975 -0.0238 0.0018  0.0080  221  ASP B CG  
10600 O OD1 . ASP B 223  ? 0.3473 0.3461 0.2797 -0.0231 -0.0008 0.0078  221  ASP B OD1 
10601 O OD2 . ASP B 223  ? 0.3898 0.3979 0.3245 -0.0222 0.0036  0.0061  221  ASP B OD2 
10602 N N   . MET B 224  ? 0.2780 0.2690 0.1980 -0.0242 -0.0035 0.0111  222  MET B N   
10603 C CA  . MET B 224  ? 0.3341 0.3227 0.2519 -0.0219 -0.0053 0.0097  222  MET B CA  
10604 C C   . MET B 224  ? 0.3490 0.3386 0.2713 -0.0193 -0.0056 0.0067  222  MET B C   
10605 O O   . MET B 224  ? 0.3768 0.3642 0.2982 -0.0175 -0.0074 0.0055  222  MET B O   
10606 C CB  . MET B 224  ? 0.3451 0.3277 0.2605 -0.0223 -0.0084 0.0114  222  MET B CB  
10607 C CG  . MET B 224  ? 0.3065 0.2873 0.2168 -0.0249 -0.0083 0.0144  222  MET B CG  
10608 S SD  . MET B 224  ? 0.3736 0.3581 0.2780 -0.0255 -0.0058 0.0147  222  MET B SD  
10609 C CE  . MET B 224  ? 0.3882 0.3706 0.2901 -0.0226 -0.0079 0.0126  222  MET B CE  
10610 N N   . LEU B 225  ? 0.3824 0.3754 0.3095 -0.0192 -0.0041 0.0058  223  LEU B N   
10611 C CA  . LEU B 225  ? 0.3625 0.3575 0.2937 -0.0169 -0.0037 0.0031  223  LEU B CA  
10612 C C   . LEU B 225  ? 0.4266 0.4182 0.3614 -0.0156 -0.0061 0.0023  223  LEU B C   
10613 O O   . LEU B 225  ? 0.4403 0.4334 0.3788 -0.0138 -0.0059 0.0002  223  LEU B O   
10614 C CB  . LEU B 225  ? 0.4204 0.4170 0.3493 -0.0149 -0.0029 0.0011  223  LEU B CB  
10615 C CG  . LEU B 225  ? 0.4794 0.4799 0.4049 -0.0156 -0.0001 0.0015  223  LEU B CG  
10616 C CD1 . LEU B 225  ? 0.5298 0.5308 0.4524 -0.0134 0.0003  -0.0006 223  LEU B CD1 
10617 C CD2 . LEU B 225  ? 0.4198 0.4254 0.3490 -0.0162 0.0025  0.0015  223  LEU B CD2 
10618 N N   . GLY B 226  ? 0.3857 0.3729 0.3198 -0.0165 -0.0083 0.0039  224  GLY B N   
10619 C CA  . GLY B 226  ? 0.3752 0.3597 0.3130 -0.0151 -0.0104 0.0031  224  GLY B CA  
10620 C C   . GLY B 226  ? 0.3223 0.3085 0.2649 -0.0153 -0.0094 0.0024  224  GLY B C   
10621 O O   . GLY B 226  ? 0.3384 0.3260 0.2814 -0.0172 -0.0081 0.0035  224  GLY B O   
10622 N N   . GLU B 227  ? 0.3208 0.3071 0.2673 -0.0133 -0.0100 0.0005  225  GLU B N   
10623 C CA  . GLU B 227  ? 0.2981 0.2860 0.2491 -0.0133 -0.0092 -0.0003 225  GLU B CA  
10624 C C   . GLU B 227  ? 0.2735 0.2603 0.2280 -0.0111 -0.0105 -0.0020 225  GLU B C   
10625 O O   . GLU B 227  ? 0.2952 0.2821 0.2492 -0.0095 -0.0111 -0.0031 225  GLU B O   
10626 C CB  . GLU B 227  ? 0.3167 0.3099 0.2688 -0.0135 -0.0066 -0.0011 225  GLU B CB  
10627 C CG  . GLU B 227  ? 0.3522 0.3477 0.3087 -0.0136 -0.0056 -0.0018 225  GLU B CG  
10628 C CD  . GLU B 227  ? 0.3799 0.3807 0.3372 -0.0139 -0.0031 -0.0023 225  GLU B CD  
10629 O OE1 . GLU B 227  ? 0.3660 0.3688 0.3203 -0.0142 -0.0019 -0.0019 225  GLU B OE1 
10630 O OE2 . GLU B 227  ? 0.4100 0.4132 0.3710 -0.0136 -0.0023 -0.0030 225  GLU B OE2 
10631 N N   . ALA B 228  ? 0.2525 0.2383 0.2103 -0.0111 -0.0109 -0.0021 226  ALA B N   
10632 C CA  . ALA B 228  ? 0.2716 0.2574 0.2333 -0.0091 -0.0115 -0.0038 226  ALA B CA  
10633 C C   . ALA B 228  ? 0.2581 0.2416 0.2192 -0.0075 -0.0135 -0.0041 226  ALA B C   
10634 O O   . ALA B 228  ? 0.2797 0.2646 0.2421 -0.0060 -0.0136 -0.0056 226  ALA B O   
10635 C CB  . ALA B 228  ? 0.2825 0.2725 0.2465 -0.0082 -0.0097 -0.0055 226  ALA B CB  
10636 N N   . ALA B 229  ? 0.2335 0.2132 0.1927 -0.0079 -0.0152 -0.0026 227  ALA B N   
10637 C CA  . ALA B 229  ? 0.2350 0.2126 0.1943 -0.0064 -0.0174 -0.0027 227  ALA B CA  
10638 C C   . ALA B 229  ? 0.2157 0.1941 0.1797 -0.0046 -0.0177 -0.0043 227  ALA B C   
10639 O O   . ALA B 229  ? 0.2409 0.2192 0.2076 -0.0046 -0.0171 -0.0045 227  ALA B O   
10640 C CB  . ALA B 229  ? 0.2424 0.2158 0.1999 -0.0069 -0.0192 -0.0008 227  ALA B CB  
10641 N N   . THR B 230  ? 0.2330 0.2122 0.1978 -0.0033 -0.0186 -0.0053 228  THR B N   
10642 C CA  . THR B 230  ? 0.2202 0.2003 0.1893 -0.0017 -0.0191 -0.0066 228  THR B CA  
10643 C C   . THR B 230  ? 0.2198 0.1975 0.1901 -0.0006 -0.0214 -0.0059 228  THR B C   
10644 O O   . THR B 230  ? 0.2354 0.2132 0.2096 0.0006  -0.0216 -0.0064 228  THR B O   
10645 C CB  . THR B 230  ? 0.2421 0.2245 0.2115 -0.0010 -0.0187 -0.0082 228  THR B CB  
10646 O OG1 . THR B 230  ? 0.2880 0.2726 0.2560 -0.0018 -0.0166 -0.0087 228  THR B OG1 
10647 C CG2 . THR B 230  ? 0.2345 0.2181 0.2086 0.0004  -0.0188 -0.0095 228  THR B CG2 
10648 N N   . THR B 231  ? 0.2174 0.1932 0.1846 -0.0009 -0.0230 -0.0047 229  THR B N   
10649 C CA  . THR B 231  ? 0.2209 0.1948 0.1891 0.0003  -0.0254 -0.0038 229  THR B CA  
10650 C C   . THR B 231  ? 0.2171 0.1875 0.1820 -0.0005 -0.0264 -0.0018 229  THR B C   
10651 O O   . THR B 231  ? 0.2269 0.1966 0.1880 -0.0021 -0.0255 -0.0009 229  THR B O   
10652 C CB  . THR B 231  ? 0.2303 0.2051 0.1978 0.0008  -0.0270 -0.0043 229  THR B CB  
10653 O OG1 . THR B 231  ? 0.2384 0.2122 0.2007 -0.0004 -0.0274 -0.0035 229  THR B OG1 
10654 C CG2 . THR B 231  ? 0.2428 0.2206 0.2127 0.0012  -0.0259 -0.0063 229  THR B CG2 
10655 N N   . ALA B 232  ? 0.2291 0.1974 0.1953 0.0007  -0.0284 -0.0008 230  ALA B N   
10656 C CA  . ALA B 232  ? 0.2390 0.2036 0.2019 0.0003  -0.0298 0.0013  230  ALA B CA  
10657 C C   . ALA B 232  ? 0.2347 0.1991 0.1927 -0.0009 -0.0306 0.0022  230  ALA B C   
10658 O O   . ALA B 232  ? 0.2590 0.2210 0.2129 -0.0023 -0.0305 0.0038  230  ALA B O   
10659 C CB  . ALA B 232  ? 0.2606 0.2234 0.2260 0.0022  -0.0320 0.0021  230  ALA B CB  
10660 N N   . ALA B 233  ? 0.2477 0.2143 0.2057 -0.0004 -0.0314 0.0013  231  ALA B N   
10661 C CA  . ALA B 233  ? 0.2571 0.2234 0.2100 -0.0015 -0.0322 0.0019  231  ALA B CA  
10662 C C   . ALA B 233  ? 0.2571 0.2243 0.2065 -0.0033 -0.0297 0.0017  231  ALA B C   
10663 O O   . ALA B 233  ? 0.2625 0.2284 0.2070 -0.0045 -0.0298 0.0031  231  ALA B O   
10664 C CB  . ALA B 233  ? 0.2877 0.2559 0.2413 -0.0007 -0.0336 0.0007  231  ALA B CB  
10665 N N   . ASP B 234  ? 0.2380 0.2077 0.1901 -0.0033 -0.0274 0.0001  232  ASP B N   
10666 C CA  . ASP B 234  ? 0.2538 0.2250 0.2033 -0.0049 -0.0249 0.0000  232  ASP B CA  
10667 C C   . ASP B 234  ? 0.2385 0.2073 0.1858 -0.0064 -0.0245 0.0020  232  ASP B C   
10668 O O   . ASP B 234  ? 0.2394 0.2080 0.1823 -0.0079 -0.0238 0.0032  232  ASP B O   
10669 C CB  . ASP B 234  ? 0.2650 0.2391 0.2182 -0.0046 -0.0227 -0.0018 232  ASP B CB  
10670 C CG  . ASP B 234  ? 0.3136 0.2900 0.2685 -0.0035 -0.0225 -0.0039 232  ASP B CG  
10671 O OD1 . ASP B 234  ? 0.3176 0.2940 0.2697 -0.0034 -0.0235 -0.0042 232  ASP B OD1 
10672 O OD2 . ASP B 234  ? 0.3019 0.2802 0.2609 -0.0028 -0.0214 -0.0052 232  ASP B OD2 
10673 N N   . ALA B 235  ? 0.2320 0.1989 0.1822 -0.0060 -0.0249 0.0025  233  ALA B N   
10674 C CA  . ALA B 235  ? 0.2383 0.2025 0.1867 -0.0075 -0.0245 0.0043  233  ALA B CA  
10675 C C   . ALA B 235  ? 0.2352 0.1960 0.1790 -0.0081 -0.0264 0.0065  233  ALA B C   
10676 O O   . ALA B 235  ? 0.2557 0.2152 0.1959 -0.0101 -0.0257 0.0082  233  ALA B O   
10677 C CB  . ALA B 235  ? 0.2390 0.2014 0.1912 -0.0067 -0.0248 0.0041  233  ALA B CB  
10678 N N   . GLU B 236  ? 0.2399 0.1995 0.1840 -0.0066 -0.0288 0.0068  234  GLU B N   
10679 C CA  . GLU B 236  ? 0.2665 0.2229 0.2062 -0.0070 -0.0308 0.0090  234  GLU B CA  
10680 C C   . GLU B 236  ? 0.2723 0.2300 0.2068 -0.0086 -0.0300 0.0094  234  GLU B C   
10681 O O   . GLU B 236  ? 0.2737 0.2292 0.2037 -0.0101 -0.0302 0.0115  234  GLU B O   
10682 C CB  . GLU B 236  ? 0.2773 0.2326 0.2187 -0.0049 -0.0336 0.0091  234  GLU B CB  
10683 C CG  . GLU B 236  ? 0.3417 0.2934 0.2793 -0.0050 -0.0360 0.0116  234  GLU B CG  
10684 C CD  . GLU B 236  ? 0.4405 0.3915 0.3805 -0.0027 -0.0389 0.0118  234  GLU B CD  
10685 O OE1 . GLU B 236  ? 0.5105 0.4642 0.4552 -0.0012 -0.0389 0.0099  234  GLU B OE1 
10686 O OE2 . GLU B 236  ? 0.4757 0.4236 0.4130 -0.0025 -0.0411 0.0139  234  GLU B OE2 
10687 N N   . ARG B 237  ? 0.2521 0.2135 0.1871 -0.0082 -0.0290 0.0074  235  ARG B N   
10688 C CA  . ARG B 237  ? 0.2895 0.2524 0.2196 -0.0094 -0.0280 0.0075  235  ARG B CA  
10689 C C   . ARG B 237  ? 0.2824 0.2463 0.2107 -0.0114 -0.0253 0.0082  235  ARG B C   
10690 O O   . ARG B 237  ? 0.2777 0.2408 0.2010 -0.0130 -0.0250 0.0099  235  ARG B O   
10691 C CB  . ARG B 237  ? 0.3117 0.2779 0.2431 -0.0083 -0.0274 0.0049  235  ARG B CB  
10692 C CG  . ARG B 237  ? 0.3291 0.2966 0.2550 -0.0093 -0.0264 0.0048  235  ARG B CG  
10693 C CD  . ARG B 237  ? 0.3760 0.3465 0.3029 -0.0084 -0.0253 0.0021  235  ARG B CD  
10694 N NE  . ARG B 237  ? 0.4316 0.4029 0.3527 -0.0092 -0.0243 0.0020  235  ARG B NE  
10695 C CZ  . ARG B 237  ? 0.4813 0.4541 0.4010 -0.0084 -0.0240 0.0000  235  ARG B CZ  
10696 N NH1 . ARG B 237  ? 0.5299 0.5034 0.4535 -0.0070 -0.0246 -0.0021 235  ARG B NH1 
10697 N NH2 . ARG B 237  ? 0.4636 0.4367 0.3775 -0.0091 -0.0230 0.0000  235  ARG B NH2 
10698 N N   . TYR B 238  ? 0.2594 0.2251 0.1916 -0.0116 -0.0234 0.0071  236  TYR B N   
10699 C CA  . TYR B 238  ? 0.2492 0.2164 0.1802 -0.0136 -0.0209 0.0079  236  TYR B CA  
10700 C C   . TYR B 238  ? 0.2437 0.2071 0.1719 -0.0154 -0.0217 0.0106  236  TYR B C   
10701 O O   . TYR B 238  ? 0.2532 0.2171 0.1777 -0.0175 -0.0204 0.0121  236  TYR B O   
10702 C CB  . TYR B 238  ? 0.2414 0.2112 0.1775 -0.0134 -0.0191 0.0063  236  TYR B CB  
10703 C CG  . TYR B 238  ? 0.2845 0.2583 0.2229 -0.0120 -0.0179 0.0038  236  TYR B CG  
10704 C CD1 . TYR B 238  ? 0.3194 0.2953 0.2547 -0.0118 -0.0172 0.0030  236  TYR B CD1 
10705 C CD2 . TYR B 238  ? 0.2709 0.2461 0.2145 -0.0108 -0.0175 0.0021  236  TYR B CD2 
10706 C CE1 . TYR B 238  ? 0.3768 0.3558 0.3142 -0.0105 -0.0161 0.0006  236  TYR B CE1 
10707 C CE2 . TYR B 238  ? 0.2872 0.2657 0.2329 -0.0096 -0.0164 -0.0001 236  TYR B CE2 
10708 C CZ  . TYR B 238  ? 0.3884 0.3686 0.3310 -0.0094 -0.0157 -0.0008 236  TYR B CZ  
10709 O OH  . TYR B 238  ? 0.4058 0.3887 0.3505 -0.0080 -0.0147 -0.0031 236  TYR B OH  
10710 N N   . TYR B 239  ? 0.2457 0.2052 0.1756 -0.0146 -0.0238 0.0114  237  TYR B N   
10711 C CA  . TYR B 239  ? 0.2747 0.2297 0.2017 -0.0160 -0.0249 0.0141  237  TYR B CA  
10712 C C   . TYR B 239  ? 0.2934 0.2471 0.2145 -0.0169 -0.0258 0.0160  237  TYR B C   
10713 O O   . TYR B 239  ? 0.2832 0.2356 0.2005 -0.0192 -0.0251 0.0181  237  TYR B O   
10714 C CB  . TYR B 239  ? 0.2680 0.2188 0.1974 -0.0143 -0.0272 0.0145  237  TYR B CB  
10715 C CG  . TYR B 239  ? 0.3110 0.2564 0.2369 -0.0155 -0.0287 0.0173  237  TYR B CG  
10716 C CD1 . TYR B 239  ? 0.3017 0.2448 0.2276 -0.0173 -0.0278 0.0184  237  TYR B CD1 
10717 C CD2 . TYR B 239  ? 0.4075 0.3500 0.3299 -0.0149 -0.0311 0.0191  237  TYR B CD2 
10718 C CE1 . TYR B 239  ? 0.3101 0.2477 0.2326 -0.0185 -0.0292 0.0210  237  TYR B CE1 
10719 C CE2 . TYR B 239  ? 0.4054 0.3428 0.3245 -0.0159 -0.0325 0.0218  237  TYR B CE2 
10720 C CZ  . TYR B 239  ? 0.3851 0.3199 0.3042 -0.0178 -0.0315 0.0227  237  TYR B CZ  
10721 O OH  . TYR B 239  ? 0.4803 0.4093 0.3959 -0.0189 -0.0328 0.0255  237  TYR B OH  
10722 N N   . ARG B 240  ? 0.2742 0.2280 0.1943 -0.0152 -0.0276 0.0154  238  ARG B N   
10723 C CA  . ARG B 240  ? 0.2923 0.2447 0.2065 -0.0160 -0.0287 0.0172  238  ARG B CA  
10724 C C   . ARG B 240  ? 0.2977 0.2534 0.2082 -0.0178 -0.0261 0.0171  238  ARG B C   
10725 O O   . ARG B 240  ? 0.3057 0.2600 0.2109 -0.0195 -0.0261 0.0193  238  ARG B O   
10726 C CB  . ARG B 240  ? 0.3148 0.2672 0.2291 -0.0138 -0.0312 0.0162  238  ARG B CB  
10727 C CG  . ARG B 240  ? 0.3241 0.2732 0.2413 -0.0121 -0.0340 0.0169  238  ARG B CG  
10728 C CD  . ARG B 240  ? 0.3748 0.3189 0.2886 -0.0130 -0.0355 0.0200  238  ARG B CD  
10729 N NE  . ARG B 240  ? 0.4203 0.3614 0.3375 -0.0109 -0.0379 0.0205  238  ARG B NE  
10730 C CZ  . ARG B 240  ? 0.5571 0.4933 0.4730 -0.0111 -0.0394 0.0228  238  ARG B CZ  
10731 N NH1 . ARG B 240  ? 0.4801 0.4136 0.3913 -0.0135 -0.0387 0.0251  238  ARG B NH1 
10732 N NH2 . ARG B 240  ? 0.5529 0.4868 0.4723 -0.0088 -0.0415 0.0229  238  ARG B NH2 
10733 N N   . ASP B 241  ? 0.2983 0.2585 0.2116 -0.0174 -0.0238 0.0147  239  ASP B N   
10734 C CA  . ASP B 241  ? 0.3173 0.2811 0.2275 -0.0188 -0.0211 0.0144  239  ASP B CA  
10735 C C   . ASP B 241  ? 0.2743 0.2381 0.1834 -0.0214 -0.0193 0.0165  239  ASP B C   
10736 O O   . ASP B 241  ? 0.2971 0.2618 0.2015 -0.0232 -0.0180 0.0180  239  ASP B O   
10737 C CB  . ASP B 241  ? 0.3430 0.3114 0.2567 -0.0174 -0.0192 0.0114  239  ASP B CB  
10738 C CG  . ASP B 241  ? 0.4206 0.3891 0.3339 -0.0153 -0.0208 0.0095  239  ASP B CG  
10739 O OD1 . ASP B 241  ? 0.4378 0.4036 0.3478 -0.0149 -0.0233 0.0105  239  ASP B OD1 
10740 O OD2 . ASP B 241  ? 0.5370 0.5085 0.4535 -0.0140 -0.0197 0.0070  239  ASP B OD2 
10741 N N   . TYR B 242  ? 0.2645 0.2273 0.1778 -0.0218 -0.0191 0.0166  240  TYR B N   
10742 C CA  . TYR B 242  ? 0.2611 0.2234 0.1734 -0.0246 -0.0178 0.0187  240  TYR B CA  
10743 C C   . TYR B 242  ? 0.2647 0.2221 0.1720 -0.0261 -0.0195 0.0218  240  TYR B C   
10744 O O   . TYR B 242  ? 0.2601 0.2177 0.1637 -0.0287 -0.0182 0.0239  240  TYR B O   
10745 C CB  . TYR B 242  ? 0.2644 0.2255 0.1818 -0.0246 -0.0179 0.0182  240  TYR B CB  
10746 C CG  . TYR B 242  ? 0.2442 0.2101 0.1665 -0.0240 -0.0159 0.0157  240  TYR B CG  
10747 C CD1 . TYR B 242  ? 0.2646 0.2359 0.1865 -0.0247 -0.0131 0.0149  240  TYR B CD1 
10748 C CD2 . TYR B 242  ? 0.2610 0.2258 0.1881 -0.0225 -0.0166 0.0142  240  TYR B CD2 
10749 C CE1 . TYR B 242  ? 0.2662 0.2418 0.1928 -0.0239 -0.0114 0.0127  240  TYR B CE1 
10750 C CE2 . TYR B 242  ? 0.2531 0.2221 0.1846 -0.0219 -0.0149 0.0121  240  TYR B CE2 
10751 C CZ  . TYR B 242  ? 0.2637 0.2379 0.1949 -0.0226 -0.0124 0.0114  240  TYR B CZ  
10752 O OH  . TYR B 242  ? 0.2694 0.2475 0.2051 -0.0218 -0.0109 0.0094  240  TYR B OH  
10753 N N   . GLU B 243  ? 0.2688 0.2216 0.1758 -0.0245 -0.0225 0.0223  241  GLU B N   
10754 C CA  . GLU B 243  ? 0.2929 0.2406 0.1953 -0.0256 -0.0244 0.0254  241  GLU B CA  
10755 C C   . GLU B 243  ? 0.2793 0.2283 0.1755 -0.0268 -0.0239 0.0266  241  GLU B C   
10756 O O   . GLU B 243  ? 0.2764 0.2236 0.1682 -0.0292 -0.0234 0.0293  241  GLU B O   
10757 C CB  . GLU B 243  ? 0.2905 0.2341 0.1942 -0.0231 -0.0277 0.0253  241  GLU B CB  
10758 C CG  . GLU B 243  ? 0.3560 0.2940 0.2550 -0.0238 -0.0301 0.0285  241  GLU B CG  
10759 C CD  . GLU B 243  ? 0.3970 0.3320 0.2976 -0.0209 -0.0334 0.0283  241  GLU B CD  
10760 O OE1 . GLU B 243  ? 0.4369 0.3748 0.3404 -0.0187 -0.0339 0.0260  241  GLU B OE1 
10761 O OE2 . GLU B 243  ? 0.4522 0.3818 0.3513 -0.0208 -0.0355 0.0305  241  GLU B OE2 
10762 N N   . SER B 244  ? 0.2700 0.2219 0.1656 -0.0250 -0.0239 0.0247  242  SER B N   
10763 C CA  A SER B 244  ? 0.2886 0.2418 0.1780 -0.0258 -0.0233 0.0255  242  SER B CA  
10764 C CA  B SER B 244  ? 0.2889 0.2421 0.1783 -0.0258 -0.0233 0.0256  242  SER B CA  
10765 C C   . SER B 244  ? 0.2678 0.2249 0.1555 -0.0282 -0.0198 0.0260  242  SER B C   
10766 O O   . SER B 244  ? 0.2846 0.2413 0.1668 -0.0302 -0.0191 0.0283  242  SER B O   
10767 C CB  A SER B 244  ? 0.3230 0.2788 0.2129 -0.0234 -0.0239 0.0228  242  SER B CB  
10768 C CB  B SER B 244  ? 0.3231 0.2787 0.2125 -0.0235 -0.0240 0.0229  242  SER B CB  
10769 O OG  A SER B 244  ? 0.3378 0.2946 0.2215 -0.0239 -0.0234 0.0232  242  SER B OG  
10770 O OG  B SER B 244  ? 0.3126 0.2649 0.2034 -0.0215 -0.0274 0.0228  242  SER B OG  
10771 N N   . ALA B 245  ? 0.2743 0.2357 0.1670 -0.0281 -0.0174 0.0240  243  ALA B N   
10772 C CA  . ALA B 245  ? 0.2801 0.2459 0.1719 -0.0302 -0.0140 0.0245  243  ALA B CA  
10773 C C   . ALA B 245  ? 0.2908 0.2541 0.1810 -0.0334 -0.0138 0.0277  243  ALA B C   
10774 O O   . ALA B 245  ? 0.2954 0.2606 0.1818 -0.0357 -0.0118 0.0295  243  ALA B O   
10775 C CB  . ALA B 245  ? 0.2851 0.2556 0.1830 -0.0293 -0.0119 0.0218  243  ALA B CB  
10776 N N   . ILE B 246  ? 0.2758 0.2347 0.1687 -0.0336 -0.0157 0.0285  244  ILE B N   
10777 C CA  . ILE B 246  ? 0.2894 0.2451 0.1805 -0.0367 -0.0156 0.0316  244  ILE B CA  
10778 C C   . ILE B 246  ? 0.3118 0.2643 0.1960 -0.0381 -0.0166 0.0346  244  ILE B C   
10779 O O   . ILE B 246  ? 0.3141 0.2671 0.1951 -0.0412 -0.0151 0.0371  244  ILE B O   
10780 C CB  . ILE B 246  ? 0.2917 0.2424 0.1865 -0.0364 -0.0177 0.0317  244  ILE B CB  
10781 C CG1 . ILE B 246  ? 0.2962 0.2506 0.1973 -0.0358 -0.0162 0.0292  244  ILE B CG1 
10782 C CG2 . ILE B 246  ? 0.2939 0.2400 0.1857 -0.0396 -0.0183 0.0352  244  ILE B CG2 
10783 C CD1 . ILE B 246  ? 0.3259 0.2756 0.2307 -0.0349 -0.0183 0.0288  244  ILE B CD1 
10784 N N   . HIS B 247  ? 0.3010 0.2505 0.1826 -0.0360 -0.0192 0.0346  245  HIS B N   
10785 C CA  . HIS B 247  ? 0.3025 0.2490 0.1771 -0.0373 -0.0202 0.0374  245  HIS B CA  
10786 C C   . HIS B 247  ? 0.3065 0.2582 0.1771 -0.0388 -0.0172 0.0377  245  HIS B C   
10787 O O   . HIS B 247  ? 0.3205 0.2712 0.1862 -0.0416 -0.0164 0.0406  245  HIS B O   
10788 C CB  . HIS B 247  ? 0.3201 0.2632 0.1928 -0.0346 -0.0236 0.0371  245  HIS B CB  
10789 C CG  . HIS B 247  ? 0.3390 0.2761 0.2141 -0.0335 -0.0267 0.0380  245  HIS B CG  
10790 N ND1 . HIS B 247  ? 0.3361 0.2676 0.2083 -0.0354 -0.0280 0.0413  245  HIS B ND1 
10791 C CD2 . HIS B 247  ? 0.3468 0.2826 0.2268 -0.0307 -0.0286 0.0360  245  HIS B CD2 
10792 C CE1 . HIS B 247  ? 0.3585 0.2855 0.2338 -0.0336 -0.0306 0.0413  245  HIS B CE1 
10793 N NE2 . HIS B 247  ? 0.3767 0.3064 0.2568 -0.0307 -0.0310 0.0381  245  HIS B NE2 
10794 N N   . ALA B 248  ? 0.2883 0.2453 0.1607 -0.0370 -0.0155 0.0346  246  ALA B N   
10795 C CA  . ALA B 248  ? 0.3038 0.2656 0.1721 -0.0380 -0.0125 0.0346  246  ALA B CA  
10796 C C   . ALA B 248  ? 0.2846 0.2502 0.1544 -0.0410 -0.0093 0.0359  246  ALA B C   
10797 O O   . ALA B 248  ? 0.3102 0.2772 0.1751 -0.0433 -0.0075 0.0382  246  ALA B O   
10798 C CB  . ALA B 248  ? 0.3146 0.2809 0.1850 -0.0352 -0.0115 0.0308  246  ALA B CB  
10799 N N   . ILE B 249  ? 0.2953 0.2627 0.1716 -0.0410 -0.0085 0.0346  247  ILE B N   
10800 C CA  . ILE B 249  ? 0.3002 0.2716 0.1784 -0.0438 -0.0056 0.0357  247  ILE B CA  
10801 C C   . ILE B 249  ? 0.2999 0.2669 0.1750 -0.0473 -0.0064 0.0396  247  ILE B C   
10802 O O   . ILE B 249  ? 0.3099 0.2798 0.1829 -0.0504 -0.0041 0.0417  247  ILE B O   
10803 C CB  . ILE B 249  ? 0.2763 0.2500 0.1621 -0.0430 -0.0051 0.0334  247  ILE B CB  
10804 C CG1 . ILE B 249  ? 0.2763 0.2547 0.1649 -0.0398 -0.0040 0.0297  247  ILE B CG1 
10805 C CG2 . ILE B 249  ? 0.3160 0.2932 0.2040 -0.0464 -0.0027 0.0349  247  ILE B CG2 
10806 C CD1 . ILE B 249  ? 0.2887 0.2673 0.1841 -0.0381 -0.0047 0.0273  247  ILE B CD1 
10807 N N   . GLY B 250  ? 0.3141 0.2741 0.1891 -0.0470 -0.0098 0.0406  248  GLY B N   
10808 C CA  . GLY B 250  ? 0.3229 0.2777 0.1948 -0.0501 -0.0109 0.0443  248  GLY B CA  
10809 C C   . GLY B 250  ? 0.3668 0.3206 0.2313 -0.0518 -0.0106 0.0472  248  GLY B C   
10810 O O   . GLY B 250  ? 0.3514 0.3048 0.2131 -0.0554 -0.0094 0.0503  248  GLY B O   
10811 N N   . LYS B 251  ? 0.3359 0.2892 0.1967 -0.0494 -0.0117 0.0464  249  LYS B N   
10812 C CA  . LYS B 251  ? 0.3902 0.3429 0.2434 -0.0508 -0.0113 0.0490  249  LYS B CA  
10813 C C   . LYS B 251  ? 0.3304 0.2903 0.1823 -0.0528 -0.0071 0.0492  249  LYS B C   
10814 O O   . LYS B 251  ? 0.3733 0.3332 0.2205 -0.0559 -0.0059 0.0524  249  LYS B O   
10815 C CB  . LYS B 251  ? 0.3729 0.3237 0.2226 -0.0478 -0.0136 0.0477  249  LYS B CB  
10816 N N   . ALA B 252  ? 0.3546 0.3209 0.2108 -0.0510 -0.0048 0.0458  250  ALA B N   
10817 C CA  . ALA B 252  ? 0.3540 0.3277 0.2095 -0.0524 -0.0007 0.0457  250  ALA B CA  
10818 C C   . ALA B 252  ? 0.3563 0.3320 0.2144 -0.0562 0.0012  0.0481  250  ALA B C   
10819 O O   . ALA B 252  ? 0.3809 0.3608 0.2363 -0.0588 0.0041  0.0500  250  ALA B O   
10820 C CB  . ALA B 252  ? 0.3384 0.3179 0.1983 -0.0493 0.0011  0.0416  250  ALA B CB  
10821 N N   . SER B 253  ? 0.3528 0.3258 0.2163 -0.0567 -0.0004 0.0479  251  SER B N   
10822 C CA  . SER B 253  ? 0.3432 0.3173 0.2090 -0.0606 0.0010  0.0501  251  SER B CA  
10823 C C   . SER B 253  ? 0.3443 0.3149 0.2039 -0.0643 0.0008  0.0545  251  SER B C   
10824 O O   . SER B 253  ? 0.3743 0.3490 0.2334 -0.0678 0.0034  0.0567  251  SER B O   
10825 C CB  . SER B 253  ? 0.3302 0.2999 0.2013 -0.0605 -0.0014 0.0493  251  SER B CB  
10826 O OG  . SER B 253  ? 0.3528 0.3232 0.2257 -0.0645 -0.0004 0.0516  251  SER B OG  
10827 N N   . ALA B 254  ? 0.3529 0.3160 0.2077 -0.0636 -0.0024 0.0560  252  ALA B N   
10828 C CA  . ALA B 254  ? 0.3985 0.3577 0.2464 -0.0666 -0.0028 0.0602  252  ALA B CA  
10829 C C   . ALA B 254  ? 0.4191 0.3768 0.2680 -0.0712 -0.0023 0.0633  252  ALA B C   
10830 O O   . ALA B 254  ? 0.4422 0.4017 0.2872 -0.0748 -0.0004 0.0665  252  ALA B O   
10831 C CB  . ALA B 254  ? 0.4161 0.3802 0.2583 -0.0668 -0.0002 0.0608  252  ALA B CB  
10832 N N   . GLY B 255  ? 0.4276 0.3821 0.2818 -0.0713 -0.0040 0.0624  253  GLY B N   
10833 C CA  . GLY B 255  ? 0.4368 0.3889 0.2919 -0.0757 -0.0039 0.0652  253  GLY B CA  
10834 C C   . GLY B 255  ? 0.3976 0.3579 0.2569 -0.0785 -0.0004 0.0650  253  GLY B C   
10835 O O   . GLY B 255  ? 0.4247 0.3838 0.2841 -0.0828 0.0000  0.0678  253  GLY B O   
10836 N N   . ARG B 256  ? 0.3598 0.3284 0.2227 -0.0762 0.0021  0.0620  254  ARG B N   
10837 C CA  . ARG B 256  ? 0.3793 0.3563 0.2468 -0.0786 0.0054  0.0619  254  ARG B CA  
10838 C C   . ARG B 256  ? 0.3676 0.3432 0.2413 -0.0797 0.0043  0.0609  254  ARG B C   
10839 O O   . ARG B 256  ? 0.3915 0.3730 0.2689 -0.0827 0.0065  0.0615  254  ARG B O   
10840 C CB  . ARG B 256  ? 0.3538 0.3397 0.2235 -0.0756 0.0084  0.0588  254  ARG B CB  
10841 C CG  . ARG B 256  ? 0.3697 0.3598 0.2336 -0.0761 0.0110  0.0604  254  ARG B CG  
10842 C CD  . ARG B 256  ? 0.3799 0.3781 0.2459 -0.0726 0.0138  0.0570  254  ARG B CD  
10843 N NE  . ARG B 256  ? 0.3437 0.3384 0.2089 -0.0680 0.0116  0.0539  254  ARG B NE  
10844 C CZ  . ARG B 256  ? 0.3686 0.3682 0.2361 -0.0643 0.0131  0.0503  254  ARG B CZ  
10845 N NH1 . ARG B 256  ? 0.3831 0.3913 0.2544 -0.0643 0.0165  0.0492  254  ARG B NH1 
10846 N NH2 . ARG B 256  ? 0.3784 0.3741 0.2443 -0.0605 0.0109  0.0479  254  ARG B NH2 
10847 N N   . GLY B 257  ? 0.3605 0.3290 0.2356 -0.0775 0.0010  0.0593  255  GLY B N   
10848 C CA  . GLY B 257  ? 0.3516 0.3181 0.2321 -0.0784 -0.0002 0.0582  255  GLY B CA  
10849 C C   . GLY B 257  ? 0.3410 0.3138 0.2279 -0.0753 0.0009  0.0542  255  GLY B C   
10850 O O   . GLY B 257  ? 0.3274 0.3064 0.2151 -0.0726 0.0028  0.0522  255  GLY B O   
10851 N N   . ILE B 258  ? 0.3341 0.3052 0.2257 -0.0760 -0.0003 0.0531  256  ILE B N   
10852 C CA  . ILE B 258  ? 0.3103 0.2856 0.2079 -0.0728 0.0002  0.0492  256  ILE B CA  
10853 C C   . ILE B 258  ? 0.3165 0.3024 0.2183 -0.0737 0.0036  0.0484  256  ILE B C   
10854 O O   . ILE B 258  ? 0.3339 0.3244 0.2400 -0.0706 0.0044  0.0452  256  ILE B O   
10855 C CB  . ILE B 258  ? 0.3420 0.3115 0.2429 -0.0727 -0.0024 0.0480  256  ILE B CB  
10856 C CG1 . ILE B 258  ? 0.3507 0.3202 0.2528 -0.0779 -0.0021 0.0503  256  ILE B CG1 
10857 C CG2 . ILE B 258  ? 0.3555 0.3149 0.2528 -0.0710 -0.0057 0.0485  256  ILE B CG2 
10858 C CD1 . ILE B 258  ? 0.3761 0.3398 0.2810 -0.0781 -0.0045 0.0491  256  ILE B CD1 
10859 N N   . TYR B 259  ? 0.3232 0.3132 0.2240 -0.0780 0.0056  0.0513  257  TYR B N   
10860 C CA  . TYR B 259  ? 0.3355 0.3360 0.2406 -0.0790 0.0089  0.0508  257  TYR B CA  
10861 C C   . TYR B 259  ? 0.3495 0.3567 0.2523 -0.0773 0.0119  0.0507  257  TYR B C   
10862 O O   . TYR B 259  ? 0.3322 0.3459 0.2383 -0.0741 0.0136  0.0479  257  TYR B O   
10863 C CB  . TYR B 259  ? 0.3310 0.3330 0.2372 -0.0847 0.0095  0.0539  257  TYR B CB  
10864 C CG  . TYR B 259  ? 0.3627 0.3572 0.2705 -0.0864 0.0064  0.0538  257  TYR B CG  
10865 C CD1 . TYR B 259  ? 0.3508 0.3462 0.2640 -0.0844 0.0055  0.0508  257  TYR B CD1 
10866 C CD2 . TYR B 259  ? 0.3910 0.3771 0.2945 -0.0897 0.0043  0.0568  257  TYR B CD2 
10867 C CE1 . TYR B 259  ? 0.3361 0.3245 0.2504 -0.0857 0.0028  0.0505  257  TYR B CE1 
10868 C CE2 . TYR B 259  ? 0.3511 0.3298 0.2558 -0.0910 0.0015  0.0565  257  TYR B CE2 
10869 C CZ  . TYR B 259  ? 0.3559 0.3360 0.2660 -0.0889 0.0008  0.0533  257  TYR B CZ  
10870 O OH  . TYR B 259  ? 0.3753 0.3480 0.2862 -0.0900 -0.0019 0.0528  257  TYR B OH  
10871 N N   . GLU B 260  ? 0.3406 0.3461 0.2374 -0.0794 0.0125  0.0537  258  GLU B N   
10872 C CA  . GLU B 260  ? 0.3499 0.3613 0.2437 -0.0777 0.0153  0.0536  258  GLU B CA  
10873 C C   . GLU B 260  ? 0.4050 0.4130 0.2964 -0.0726 0.0140  0.0508  258  GLU B C   
10874 O O   . GLU B 260  ? 0.3783 0.3921 0.2702 -0.0696 0.0161  0.0486  258  GLU B O   
10875 C CB  . GLU B 260  ? 0.3844 0.3949 0.2722 -0.0814 0.0163  0.0577  258  GLU B CB  
10876 C CG  . GLU B 260  ? 0.4742 0.4902 0.3580 -0.0797 0.0193  0.0576  258  GLU B CG  
10877 C CD  . GLU B 260  ? 0.5056 0.5192 0.3823 -0.0830 0.0198  0.0616  258  GLU B CD  
10878 O OE1 . GLU B 260  ? 0.5468 0.5562 0.4226 -0.0873 0.0185  0.0648  258  GLU B OE1 
10879 O OE2 . GLU B 260  ? 0.5112 0.5269 0.3831 -0.0812 0.0214  0.0616  258  GLU B OE2 
10880 N N   . GLY B 261  ? 0.3392 0.3380 0.2284 -0.0716 0.0105  0.0507  259  GLY B N   
10881 C CA  . GLY B 261  ? 0.3230 0.3181 0.2093 -0.0674 0.0089  0.0487  259  GLY B CA  
10882 C C   . GLY B 261  ? 0.3218 0.3177 0.2133 -0.0634 0.0080  0.0446  259  GLY B C   
10883 O O   . GLY B 261  ? 0.3174 0.3149 0.2146 -0.0638 0.0079  0.0434  259  GLY B O   
10884 N N   . PRO B 262  ? 0.2980 0.2927 0.1876 -0.0595 0.0073  0.0424  260  PRO B N   
10885 C CA  . PRO B 262  ? 0.2798 0.2757 0.1740 -0.0555 0.0067  0.0386  260  PRO B CA  
10886 C C   . PRO B 262  ? 0.3079 0.2968 0.2047 -0.0547 0.0033  0.0378  260  PRO B C   
10887 O O   . PRO B 262  ? 0.3348 0.3168 0.2288 -0.0562 0.0009  0.0399  260  PRO B O   
10888 C CB  . PRO B 262  ? 0.3131 0.3088 0.2032 -0.0522 0.0067  0.0370  260  PRO B CB  
10889 C CG  . PRO B 262  ? 0.3370 0.3277 0.2202 -0.0541 0.0055  0.0402  260  PRO B CG  
10890 C CD  . PRO B 262  ? 0.3188 0.3118 0.2015 -0.0587 0.0073  0.0435  260  PRO B CD  
10891 N N   . GLY B 263  ? 0.2684 0.2594 0.1706 -0.0521 0.0031  0.0347  261  GLY B N   
10892 C CA  . GLY B 263  ? 0.2960 0.2809 0.2006 -0.0506 0.0001  0.0335  261  GLY B CA  
10893 C C   . GLY B 263  ? 0.2667 0.2524 0.1738 -0.0463 -0.0005 0.0300  261  GLY B C   
10894 O O   . GLY B 263  ? 0.2764 0.2665 0.1825 -0.0444 0.0011  0.0286  261  GLY B O   
10895 N N   . ILE B 264  ? 0.2766 0.2583 0.1869 -0.0447 -0.0028 0.0286  262  ILE B N   
10896 C CA  . ILE B 264  ? 0.2574 0.2394 0.1704 -0.0408 -0.0036 0.0254  262  ILE B CA  
10897 C C   . ILE B 264  ? 0.2577 0.2409 0.1768 -0.0403 -0.0036 0.0236  262  ILE B C   
10898 O O   . ILE B 264  ? 0.2787 0.2595 0.1991 -0.0426 -0.0042 0.0249  262  ILE B O   
10899 C CB  . ILE B 264  ? 0.2798 0.2552 0.1901 -0.0388 -0.0066 0.0255  262  ILE B CB  
10900 C CG1 . ILE B 264  ? 0.2813 0.2581 0.1938 -0.0350 -0.0071 0.0223  262  ILE B CG1 
10901 C CG2 . ILE B 264  ? 0.2884 0.2574 0.2000 -0.0396 -0.0091 0.0264  262  ILE B CG2 
10902 C CD1 . ILE B 264  ? 0.2974 0.2687 0.2075 -0.0329 -0.0101 0.0223  262  ILE B CD1 
10903 N N   . SER B 265  ? 0.2285 0.2152 0.1511 -0.0374 -0.0029 0.0207  263  SER B N   
10904 C CA  . SER B 265  ? 0.2462 0.2338 0.1743 -0.0364 -0.0032 0.0188  263  SER B CA  
10905 C C   . SER B 265  ? 0.2675 0.2519 0.1969 -0.0330 -0.0052 0.0166  263  SER B C   
10906 O O   . SER B 265  ? 0.2898 0.2747 0.2173 -0.0308 -0.0053 0.0156  263  SER B O   
10907 C CB  . SER B 265  ? 0.2696 0.2648 0.2010 -0.0360 -0.0005 0.0173  263  SER B CB  
10908 O OG  . SER B 265  ? 0.2760 0.2748 0.2077 -0.0393 0.0013  0.0192  263  SER B OG  
10909 N N   . ILE B 266  ? 0.2348 0.2157 0.1672 -0.0325 -0.0068 0.0160  264  ILE B N   
10910 C CA  . ILE B 266  ? 0.2357 0.2138 0.1699 -0.0294 -0.0087 0.0141  264  ILE B CA  
10911 C C   . ILE B 266  ? 0.2324 0.2126 0.1719 -0.0283 -0.0083 0.0120  264  ILE B C   
10912 O O   . ILE B 266  ? 0.2399 0.2221 0.1814 -0.0302 -0.0072 0.0123  264  ILE B O   
10913 C CB  . ILE B 266  ? 0.2600 0.2309 0.1921 -0.0293 -0.0114 0.0154  264  ILE B CB  
10914 C CG1 . ILE B 266  ? 0.2945 0.2620 0.2279 -0.0313 -0.0120 0.0164  264  ILE B CG1 
10915 C CG2 . ILE B 266  ? 0.2749 0.2436 0.2014 -0.0305 -0.0120 0.0178  264  ILE B CG2 
10916 C CD1 . ILE B 266  ? 0.3244 0.2848 0.2570 -0.0304 -0.0147 0.0171  264  ILE B CD1 
10917 N N   . LYS B 267  ? 0.2296 0.2092 0.1713 -0.0253 -0.0092 0.0099  265  LYS B N   
10918 C CA  . LYS B 267  ? 0.2349 0.2157 0.1813 -0.0240 -0.0091 0.0080  265  LYS B CA  
10919 C C   . LYS B 267  ? 0.2214 0.1967 0.1686 -0.0224 -0.0115 0.0076  265  LYS B C   
10920 O O   . LYS B 267  ? 0.2431 0.2163 0.1890 -0.0206 -0.0129 0.0075  265  LYS B O   
10921 C CB  . LYS B 267  ? 0.2333 0.2189 0.1821 -0.0217 -0.0079 0.0057  265  LYS B CB  
10922 C CG  . LYS B 267  ? 0.2936 0.2851 0.2427 -0.0229 -0.0053 0.0057  265  LYS B CG  
10923 C CD  . LYS B 267  ? 0.3466 0.3419 0.2973 -0.0203 -0.0042 0.0035  265  LYS B CD  
10924 C CE  . LYS B 267  ? 0.3893 0.3907 0.3404 -0.0210 -0.0015 0.0035  265  LYS B CE  
10925 N NZ  . LYS B 267  ? 0.4099 0.4121 0.3571 -0.0233 -0.0006 0.0056  265  LYS B NZ  
10926 N N   . LEU B 268  ? 0.2167 0.1898 0.1660 -0.0232 -0.0120 0.0076  266  LEU B N   
10927 C CA  . LEU B 268  ? 0.2227 0.1908 0.1729 -0.0214 -0.0140 0.0072  266  LEU B CA  
10928 C C   . LEU B 268  ? 0.2438 0.2135 0.1969 -0.0182 -0.0144 0.0050  266  LEU B C   
10929 O O   . LEU B 268  ? 0.2340 0.2003 0.1869 -0.0164 -0.0162 0.0050  266  LEU B O   
10930 C CB  . LEU B 268  ? 0.2241 0.1896 0.1758 -0.0226 -0.0143 0.0071  266  LEU B CB  
10931 C CG  . LEU B 268  ? 0.2354 0.1987 0.1843 -0.0260 -0.0142 0.0094  266  LEU B CG  
10932 C CD1 . LEU B 268  ? 0.2701 0.2303 0.2204 -0.0270 -0.0147 0.0090  266  LEU B CD1 
10933 C CD2 . LEU B 268  ? 0.2795 0.2379 0.2241 -0.0265 -0.0157 0.0115  266  LEU B CD2 
10934 N N   . SER B 269  ? 0.2197 0.1944 0.1753 -0.0175 -0.0128 0.0034  267  SER B N   
10935 C CA  . SER B 269  ? 0.2121 0.1882 0.1704 -0.0147 -0.0132 0.0014  267  SER B CA  
10936 C C   . SER B 269  ? 0.2332 0.2086 0.1890 -0.0135 -0.0142 0.0017  267  SER B C   
10937 O O   . SER B 269  ? 0.2238 0.1990 0.1814 -0.0113 -0.0152 0.0005  267  SER B O   
10938 C CB  . SER B 269  ? 0.2253 0.2066 0.1864 -0.0142 -0.0113 -0.0002 267  SER B CB  
10939 O OG  . SER B 269  ? 0.2348 0.2196 0.1939 -0.0149 -0.0099 0.0000  267  SER B OG  
10940 N N   . ALA B 270  ? 0.2121 0.1875 0.1639 -0.0150 -0.0139 0.0032  268  ALA B N   
10941 C CA  . ALA B 270  ? 0.2206 0.1950 0.1697 -0.0140 -0.0151 0.0035  268  ALA B CA  
10942 C C   . ALA B 270  ? 0.2463 0.2157 0.1946 -0.0132 -0.0176 0.0045  268  ALA B C   
10943 O O   . ALA B 270  ? 0.2380 0.2065 0.1852 -0.0119 -0.0191 0.0044  268  ALA B O   
10944 C CB  . ALA B 270  ? 0.2395 0.2149 0.1840 -0.0159 -0.0141 0.0050  268  ALA B CB  
10945 N N   . LEU B 271  ? 0.2277 0.1936 0.1763 -0.0141 -0.0183 0.0056  269  LEU B N   
10946 C CA  . LEU B 271  ? 0.2533 0.2140 0.2003 -0.0135 -0.0206 0.0071  269  LEU B CA  
10947 C C   . LEU B 271  ? 0.2317 0.1906 0.1825 -0.0112 -0.0218 0.0059  269  LEU B C   
10948 O O   . LEU B 271  ? 0.2513 0.2061 0.2013 -0.0103 -0.0238 0.0070  269  LEU B O   
10949 C CB  . LEU B 271  ? 0.2409 0.1980 0.1851 -0.0160 -0.0206 0.0092  269  LEU B CB  
10950 C CG  . LEU B 271  ? 0.2596 0.2183 0.1996 -0.0183 -0.0195 0.0108  269  LEU B CG  
10951 C CD1 . LEU B 271  ? 0.3142 0.2695 0.2518 -0.0211 -0.0195 0.0129  269  LEU B CD1 
10952 C CD2 . LEU B 271  ? 0.2686 0.2262 0.2052 -0.0175 -0.0210 0.0117  269  LEU B CD2 
10953 N N   . HIS B 272  ? 0.2352 0.1971 0.1901 -0.0101 -0.0207 0.0039  270  HIS B N   
10954 C CA  . HIS B 272  ? 0.2418 0.2026 0.2003 -0.0078 -0.0218 0.0028  270  HIS B CA  
10955 C C   . HIS B 272  ? 0.2177 0.1828 0.1798 -0.0066 -0.0205 0.0006  270  HIS B C   
10956 O O   . HIS B 272  ? 0.2343 0.2024 0.1970 -0.0078 -0.0187 -0.0001 270  HIS B O   
10957 C CB  . HIS B 272  ? 0.2566 0.2138 0.2158 -0.0082 -0.0218 0.0032  270  HIS B CB  
10958 C CG  . HIS B 272  ? 0.2503 0.2050 0.2121 -0.0057 -0.0232 0.0026  270  HIS B CG  
10959 N ND1 . HIS B 272  ? 0.2839 0.2411 0.2499 -0.0040 -0.0226 0.0007  270  HIS B ND1 
10960 C CD2 . HIS B 272  ? 0.3165 0.2669 0.2775 -0.0046 -0.0251 0.0038  270  HIS B CD2 
10961 C CE1 . HIS B 272  ? 0.3002 0.2550 0.2680 -0.0018 -0.0239 0.0007  270  HIS B CE1 
10962 N NE2 . HIS B 272  ? 0.3199 0.2704 0.2847 -0.0020 -0.0255 0.0025  270  HIS B NE2 
10963 N N   . PRO B 273  ? 0.2285 0.1944 0.1935 -0.0044 -0.0215 -0.0004 271  PRO B N   
10964 C CA  . PRO B 273  ? 0.2237 0.1936 0.1921 -0.0034 -0.0204 -0.0024 271  PRO B CA  
10965 C C   . PRO B 273  ? 0.2099 0.1802 0.1814 -0.0031 -0.0193 -0.0035 271  PRO B C   
10966 O O   . PRO B 273  ? 0.2385 0.2121 0.2126 -0.0025 -0.0181 -0.0050 271  PRO B O   
10967 C CB  . PRO B 273  ? 0.2502 0.2203 0.2203 -0.0014 -0.0221 -0.0028 271  PRO B CB  
10968 C CG  . PRO B 273  ? 0.2598 0.2258 0.2289 -0.0008 -0.0239 -0.0013 271  PRO B CG  
10969 C CD  . PRO B 273  ? 0.2417 0.2052 0.2066 -0.0029 -0.0238 0.0004  271  PRO B CD  
10970 N N   . ARG B 274  ? 0.2236 0.1904 0.1948 -0.0034 -0.0196 -0.0028 272  ARG B N   
10971 C CA  . ARG B 274  ? 0.2173 0.1841 0.1911 -0.0031 -0.0187 -0.0038 272  ARG B CA  
10972 C C   . ARG B 274  ? 0.2284 0.1930 0.1998 -0.0054 -0.0181 -0.0029 272  ARG B C   
10973 O O   . ARG B 274  ? 0.2479 0.2089 0.2193 -0.0053 -0.0185 -0.0028 272  ARG B O   
10974 C CB  . ARG B 274  ? 0.2197 0.1841 0.1958 -0.0009 -0.0198 -0.0041 272  ARG B CB  
10975 C CG  . ARG B 274  ? 0.2466 0.2135 0.2257 0.0013  -0.0204 -0.0050 272  ARG B CG  
10976 C CD  . ARG B 274  ? 0.2327 0.2041 0.2142 0.0013  -0.0189 -0.0066 272  ARG B CD  
10977 N NE  . ARG B 274  ? 0.2337 0.2056 0.2169 0.0012  -0.0175 -0.0076 272  ARG B NE  
10978 C CZ  . ARG B 274  ? 0.2306 0.2020 0.2166 0.0029  -0.0175 -0.0084 272  ARG B CZ  
10979 N NH1 . ARG B 274  ? 0.2244 0.1951 0.2122 0.0048  -0.0186 -0.0082 272  ARG B NH1 
10980 N NH2 . ARG B 274  ? 0.2429 0.2150 0.2300 0.0026  -0.0162 -0.0093 272  ARG B NH2 
10981 N N   . TYR B 275  ? 0.2247 0.1915 0.1942 -0.0074 -0.0171 -0.0024 273  TYR B N   
10982 C CA  . TYR B 275  ? 0.2413 0.2068 0.2088 -0.0099 -0.0164 -0.0015 273  TYR B CA  
10983 C C   . TYR B 275  ? 0.2340 0.2020 0.2041 -0.0103 -0.0151 -0.0029 273  TYR B C   
10984 O O   . TYR B 275  ? 0.2317 0.2042 0.2029 -0.0109 -0.0137 -0.0035 273  TYR B O   
10985 C CB  . TYR B 275  ? 0.2261 0.1935 0.1907 -0.0120 -0.0158 -0.0002 273  TYR B CB  
10986 C CG  . TYR B 275  ? 0.2118 0.1788 0.1747 -0.0149 -0.0150 0.0008  273  TYR B CG  
10987 C CD1 . TYR B 275  ? 0.2426 0.2047 0.2042 -0.0159 -0.0159 0.0017  273  TYR B CD1 
10988 C CD2 . TYR B 275  ? 0.2320 0.2037 0.1949 -0.0165 -0.0133 0.0009  273  TYR B CD2 
10989 C CE1 . TYR B 275  ? 0.2492 0.2107 0.2093 -0.0189 -0.0153 0.0027  273  TYR B CE1 
10990 C CE2 . TYR B 275  ? 0.2233 0.1951 0.1850 -0.0193 -0.0126 0.0020  273  TYR B CE2 
10991 C CZ  . TYR B 275  ? 0.2272 0.1940 0.1876 -0.0207 -0.0137 0.0029  273  TYR B CZ  
10992 O OH  . TYR B 275  ? 0.2539 0.2207 0.2132 -0.0238 -0.0131 0.0040  273  TYR B OH  
10993 N N   . SER B 276  ? 0.2138 0.1788 0.1849 -0.0097 -0.0155 -0.0034 274  SER B N   
10994 C CA  . SER B 276  ? 0.2249 0.1918 0.1982 -0.0100 -0.0144 -0.0047 274  SER B CA  
10995 C C   . SER B 276  ? 0.2164 0.1785 0.1890 -0.0101 -0.0151 -0.0048 274  SER B C   
10996 O O   . SER B 276  ? 0.2204 0.1779 0.1919 -0.0090 -0.0164 -0.0043 274  SER B O   
10997 C CB  . SER B 276  ? 0.2741 0.2445 0.2509 -0.0076 -0.0139 -0.0064 274  SER B CB  
10998 O OG  . SER B 276  ? 0.3274 0.2950 0.3053 -0.0053 -0.0149 -0.0068 274  SER B OG  
10999 N N   . ARG B 277  ? 0.2103 0.1733 0.1836 -0.0114 -0.0143 -0.0056 275  ARG B N   
11000 C CA  . ARG B 277  ? 0.2075 0.1657 0.1799 -0.0116 -0.0149 -0.0059 275  ARG B CA  
11001 C C   . ARG B 277  ? 0.2135 0.1698 0.1876 -0.0084 -0.0154 -0.0071 275  ARG B C   
11002 O O   . ARG B 277  ? 0.2312 0.1822 0.2040 -0.0077 -0.0163 -0.0071 275  ARG B O   
11003 C CB  . ARG B 277  ? 0.2272 0.1874 0.2001 -0.0135 -0.0141 -0.0067 275  ARG B CB  
11004 C CG  . ARG B 277  ? 0.2374 0.1928 0.2093 -0.0135 -0.0146 -0.0076 275  ARG B CG  
11005 C CD  . ARG B 277  ? 0.2376 0.1865 0.2060 -0.0150 -0.0159 -0.0063 275  ARG B CD  
11006 N NE  . ARG B 277  ? 0.2408 0.1847 0.2079 -0.0149 -0.0164 -0.0073 275  ARG B NE  
11007 C CZ  . ARG B 277  ? 0.2474 0.1874 0.2146 -0.0121 -0.0168 -0.0082 275  ARG B CZ  
11008 N NH1 . ARG B 277  ? 0.2732 0.2144 0.2423 -0.0092 -0.0169 -0.0083 275  ARG B NH1 
11009 N NH2 . ARG B 277  ? 0.2561 0.1909 0.2214 -0.0124 -0.0173 -0.0091 275  ARG B NH2 
11010 N N   . ALA B 278  ? 0.2119 0.1723 0.1890 -0.0064 -0.0147 -0.0081 276  ALA B N   
11011 C CA  . ALA B 278  ? 0.2345 0.1937 0.2136 -0.0035 -0.0150 -0.0091 276  ALA B CA  
11012 C C   . ALA B 278  ? 0.2354 0.1910 0.2136 -0.0020 -0.0164 -0.0081 276  ALA B C   
11013 O O   . ALA B 278  ? 0.2512 0.2043 0.2304 0.0002  -0.0168 -0.0087 276  ALA B O   
11014 C CB  . ALA B 278  ? 0.2403 0.2049 0.2228 -0.0020 -0.0141 -0.0102 276  ALA B CB  
11015 N N   . GLN B 279  ? 0.2263 0.1819 0.2028 -0.0031 -0.0171 -0.0067 277  GLN B N   
11016 C CA  . GLN B 279  ? 0.2236 0.1758 0.1989 -0.0019 -0.0186 -0.0055 277  GLN B CA  
11017 C C   . GLN B 279  ? 0.2207 0.1679 0.1919 -0.0039 -0.0195 -0.0039 277  GLN B C   
11018 O O   . GLN B 279  ? 0.2380 0.1836 0.2073 -0.0041 -0.0206 -0.0023 277  GLN B O   
11019 C CB  . GLN B 279  ? 0.2485 0.2042 0.2246 -0.0013 -0.0190 -0.0050 277  GLN B CB  
11020 C CG  . GLN B 279  ? 0.2543 0.2144 0.2342 0.0006  -0.0183 -0.0065 277  GLN B CG  
11021 C CD  . GLN B 279  ? 0.2866 0.2452 0.2689 0.0033  -0.0188 -0.0071 277  GLN B CD  
11022 O OE1 . GLN B 279  ? 0.3150 0.2695 0.2963 0.0043  -0.0200 -0.0063 277  GLN B OE1 
11023 N NE2 . GLN B 279  ? 0.2458 0.2075 0.2313 0.0046  -0.0178 -0.0085 277  GLN B NE2 
11024 N N   . ALA B 280  ? 0.2405 0.1852 0.2104 -0.0056 -0.0191 -0.0041 278  ALA B N   
11025 C CA  . ALA B 280  ? 0.2444 0.1845 0.2104 -0.0081 -0.0198 -0.0025 278  ALA B CA  
11026 C C   . ALA B 280  ? 0.2627 0.1972 0.2268 -0.0067 -0.0215 -0.0013 278  ALA B C   
11027 O O   . ALA B 280  ? 0.2548 0.1867 0.2159 -0.0083 -0.0224 0.0006  278  ALA B O   
11028 C CB  . ALA B 280  ? 0.2781 0.2157 0.2430 -0.0099 -0.0194 -0.0033 278  ALA B CB  
11029 N N   . ALA B 281  ? 0.2487 0.1811 0.2145 -0.0035 -0.0220 -0.0022 279  ALA B N   
11030 C CA  . ALA B 281  ? 0.2678 0.1949 0.2321 -0.0018 -0.0237 -0.0010 279  ALA B CA  
11031 C C   . ALA B 281  ? 0.2551 0.1843 0.2191 -0.0015 -0.0246 0.0006  279  ALA B C   
11032 O O   . ALA B 281  ? 0.2827 0.2078 0.2437 -0.0021 -0.0260 0.0025  279  ALA B O   
11033 C CB  . ALA B 281  ? 0.2842 0.2098 0.2510 0.0018  -0.0238 -0.0023 279  ALA B CB  
11034 N N   . ARG B 282  ? 0.2370 0.1722 0.2039 -0.0007 -0.0240 -0.0001 280  ARG B N   
11035 C CA  . ARG B 282  ? 0.2395 0.1767 0.2058 -0.0006 -0.0250 0.0012  280  ARG B CA  
11036 C C   . ARG B 282  ? 0.2510 0.1885 0.2137 -0.0038 -0.0247 0.0026  280  ARG B C   
11037 O O   . ARG B 282  ? 0.2614 0.1974 0.2216 -0.0042 -0.0259 0.0043  280  ARG B O   
11038 C CB  . ARG B 282  ? 0.2695 0.2129 0.2395 0.0009  -0.0244 -0.0001 280  ARG B CB  
11039 C CG  . ARG B 282  ? 0.2862 0.2298 0.2598 0.0042  -0.0248 -0.0011 280  ARG B CG  
11040 C CD  . ARG B 282  ? 0.2839 0.2333 0.2607 0.0053  -0.0247 -0.0019 280  ARG B CD  
11041 N NE  . ARG B 282  ? 0.2733 0.2231 0.2485 0.0050  -0.0261 -0.0005 280  ARG B NE  
11042 C CZ  . ARG B 282  ? 0.2676 0.2217 0.2438 0.0050  -0.0262 -0.0008 280  ARG B CZ  
11043 N NH1 . ARG B 282  ? 0.2754 0.2338 0.2545 0.0052  -0.0248 -0.0025 280  ARG B NH1 
11044 N NH2 . ARG B 282  ? 0.2711 0.2250 0.2453 0.0048  -0.0277 0.0005  280  ARG B NH2 
11045 N N   . VAL B 283  ? 0.2467 0.1863 0.2092 -0.0062 -0.0231 0.0019  281  VAL B N   
11046 C CA  . VAL B 283  ? 0.2533 0.1935 0.2127 -0.0094 -0.0227 0.0033  281  VAL B CA  
11047 C C   . VAL B 283  ? 0.2614 0.1952 0.2168 -0.0108 -0.0239 0.0053  281  VAL B C   
11048 O O   . VAL B 283  ? 0.2673 0.2003 0.2198 -0.0120 -0.0246 0.0072  281  VAL B O   
11049 C CB  . VAL B 283  ? 0.2436 0.1874 0.2041 -0.0114 -0.0208 0.0023  281  VAL B CB  
11050 C CG1 . VAL B 283  ? 0.2688 0.2129 0.2261 -0.0149 -0.0203 0.0039  281  VAL B CG1 
11051 C CG2 . VAL B 283  ? 0.2474 0.1976 0.2112 -0.0101 -0.0197 0.0007  281  VAL B CG2 
11052 N N   . MET B 284  ? 0.2528 0.1816 0.2079 -0.0106 -0.0244 0.0050  282  MET B N   
11053 C CA  . MET B 284  ? 0.2812 0.2033 0.2323 -0.0120 -0.0256 0.0069  282  MET B CA  
11054 C C   . MET B 284  ? 0.2878 0.2064 0.2378 -0.0097 -0.0275 0.0083  282  MET B C   
11055 O O   . MET B 284  ? 0.3052 0.2200 0.2515 -0.0112 -0.0286 0.0105  282  MET B O   
11056 C CB  . MET B 284  ? 0.2804 0.1976 0.2312 -0.0123 -0.0257 0.0060  282  MET B CB  
11057 C CG  . MET B 284  ? 0.2955 0.2158 0.2471 -0.0148 -0.0241 0.0048  282  MET B CG  
11058 S SD  . MET B 284  ? 0.3220 0.2446 0.2709 -0.0195 -0.0233 0.0067  282  MET B SD  
11059 C CE  . MET B 284  ? 0.3610 0.2742 0.3050 -0.0215 -0.0250 0.0088  282  MET B CE  
11060 N N   . GLY B 285  ? 0.2737 0.1940 0.2269 -0.0062 -0.0280 0.0072  283  GLY B N   
11061 C CA  . GLY B 285  ? 0.3021 0.2193 0.2546 -0.0038 -0.0299 0.0085  283  GLY B CA  
11062 C C   . GLY B 285  ? 0.2989 0.2195 0.2505 -0.0041 -0.0306 0.0098  283  GLY B C   
11063 O O   . GLY B 285  ? 0.3210 0.2382 0.2703 -0.0035 -0.0324 0.0117  283  GLY B O   
11064 N N   . GLU B 286  ? 0.2740 0.2010 0.2272 -0.0049 -0.0292 0.0087  284  GLU B N   
11065 C CA  . GLU B 286  ? 0.2494 0.1801 0.2022 -0.0047 -0.0298 0.0094  284  GLU B CA  
11066 C C   . GLU B 286  ? 0.3064 0.2399 0.2564 -0.0079 -0.0285 0.0101  284  GLU B C   
11067 O O   . GLU B 286  ? 0.3375 0.2709 0.2845 -0.0086 -0.0293 0.0117  284  GLU B O   
11068 C CB  . GLU B 286  ? 0.2745 0.2104 0.2317 -0.0024 -0.0294 0.0074  284  GLU B CB  
11069 C CG  . GLU B 286  ? 0.2791 0.2134 0.2397 0.0009  -0.0304 0.0066  284  GLU B CG  
11070 C CD  . GLU B 286  ? 0.3394 0.2791 0.3048 0.0027  -0.0296 0.0046  284  GLU B CD  
11071 O OE1 . GLU B 286  ? 0.3281 0.2723 0.2940 0.0021  -0.0292 0.0042  284  GLU B OE1 
11072 O OE2 . GLU B 286  ? 0.3544 0.2936 0.3228 0.0048  -0.0294 0.0034  284  GLU B OE2 
11073 N N   . LEU B 287  ? 0.2782 0.2145 0.2292 -0.0097 -0.0265 0.0089  285  LEU B N   
11074 C CA  . LEU B 287  ? 0.2685 0.2080 0.2173 -0.0125 -0.0251 0.0096  285  LEU B CA  
11075 C C   . LEU B 287  ? 0.3060 0.2411 0.2505 -0.0153 -0.0254 0.0119  285  LEU B C   
11076 O O   . LEU B 287  ? 0.2730 0.2087 0.2142 -0.0170 -0.0255 0.0135  285  LEU B O   
11077 C CB  . LEU B 287  ? 0.2554 0.1998 0.2072 -0.0133 -0.0230 0.0076  285  LEU B CB  
11078 C CG  . LEU B 287  ? 0.2828 0.2328 0.2340 -0.0149 -0.0212 0.0074  285  LEU B CG  
11079 C CD1 . LEU B 287  ? 0.2661 0.2205 0.2209 -0.0149 -0.0195 0.0054  285  LEU B CD1 
11080 C CD2 . LEU B 287  ? 0.2963 0.2453 0.2436 -0.0182 -0.0207 0.0095  285  LEU B CD2 
11081 N N   . LEU B 288  ? 0.2772 0.2079 0.2216 -0.0161 -0.0257 0.0120  286  LEU B N   
11082 C CA  . LEU B 288  ? 0.2796 0.2058 0.2200 -0.0191 -0.0260 0.0142  286  LEU B CA  
11083 C C   . LEU B 288  ? 0.2933 0.2156 0.2297 -0.0191 -0.0277 0.0167  286  LEU B C   
11084 O O   . LEU B 288  ? 0.2921 0.2144 0.2250 -0.0220 -0.0273 0.0186  286  LEU B O   
11085 C CB  . LEU B 288  ? 0.3157 0.2368 0.2564 -0.0194 -0.0263 0.0136  286  LEU B CB  
11086 C CG  . LEU B 288  ? 0.3378 0.2528 0.2742 -0.0224 -0.0271 0.0159  286  LEU B CG  
11087 C CD1 . LEU B 288  ? 0.3240 0.2426 0.2587 -0.0264 -0.0255 0.0171  286  LEU B CD1 
11088 C CD2 . LEU B 288  ? 0.4232 0.3327 0.3600 -0.0223 -0.0275 0.0150  286  LEU B CD2 
11089 N N   . PRO B 289  ? 0.2913 0.2106 0.2280 -0.0161 -0.0296 0.0169  287  PRO B N   
11090 C CA  . PRO B 289  ? 0.2990 0.2148 0.2316 -0.0163 -0.0314 0.0195  287  PRO B CA  
11091 C C   . PRO B 289  ? 0.2810 0.2016 0.2116 -0.0175 -0.0307 0.0203  287  PRO B C   
11092 O O   . PRO B 289  ? 0.3008 0.2189 0.2269 -0.0193 -0.0314 0.0227  287  PRO B O   
11093 C CB  . PRO B 289  ? 0.3387 0.2521 0.2733 -0.0123 -0.0334 0.0191  287  PRO B CB  
11094 C CG  . PRO B 289  ? 0.3563 0.2688 0.2947 -0.0108 -0.0328 0.0169  287  PRO B CG  
11095 C CD  . PRO B 289  ? 0.3104 0.2285 0.2508 -0.0126 -0.0304 0.0151  287  PRO B CD  
11096 N N   . ARG B 290  ? 0.2714 0.1984 0.2049 -0.0166 -0.0294 0.0182  288  ARG B N   
11097 C CA  A ARG B 290  ? 0.2832 0.2147 0.2146 -0.0177 -0.0286 0.0187  288  ARG B CA  
11098 C CA  B ARG B 290  ? 0.2830 0.2146 0.2145 -0.0177 -0.0286 0.0187  288  ARG B CA  
11099 C C   . ARG B 290  ? 0.2622 0.1952 0.1911 -0.0214 -0.0267 0.0198  288  ARG B C   
11100 O O   . ARG B 290  ? 0.2787 0.2117 0.2034 -0.0231 -0.0267 0.0217  288  ARG B O   
11101 C CB  A ARG B 290  ? 0.2955 0.2331 0.2307 -0.0158 -0.0277 0.0161  288  ARG B CB  
11102 C CB  B ARG B 290  ? 0.2950 0.2327 0.2303 -0.0159 -0.0276 0.0160  288  ARG B CB  
11103 C CG  A ARG B 290  ? 0.3297 0.2666 0.2670 -0.0125 -0.0297 0.0154  288  ARG B CG  
11104 C CG  B ARG B 290  ? 0.3299 0.2671 0.2675 -0.0125 -0.0295 0.0152  288  ARG B CG  
11105 C CD  A ARG B 290  ? 0.3508 0.2923 0.2931 -0.0105 -0.0288 0.0127  288  ARG B CD  
11106 C CD  B ARG B 290  ? 0.3339 0.2769 0.2753 -0.0110 -0.0285 0.0127  288  ARG B CD  
11107 N NE  A ARG B 290  ? 0.3269 0.2675 0.2718 -0.0075 -0.0307 0.0121  288  ARG B NE  
11108 N NE  B ARG B 290  ? 0.3033 0.2469 0.2453 -0.0087 -0.0304 0.0125  288  ARG B NE  
11109 C CZ  A ARG B 290  ? 0.3281 0.2717 0.2777 -0.0055 -0.0303 0.0100  288  ARG B CZ  
11110 C CZ  B ARG B 290  ? 0.3730 0.3204 0.3186 -0.0069 -0.0303 0.0105  288  ARG B CZ  
11111 N NH1 A ARG B 290  ? 0.2734 0.2209 0.2254 -0.0061 -0.0282 0.0081  288  ARG B NH1 
11112 N NH1 B ARG B 290  ? 0.3420 0.2927 0.2910 -0.0068 -0.0283 0.0085  288  ARG B NH1 
11113 N NH2 A ARG B 290  ? 0.3361 0.2789 0.2880 -0.0028 -0.0321 0.0098  288  ARG B NH2 
11114 N NH2 B ARG B 290  ? 0.3954 0.3432 0.3411 -0.0052 -0.0322 0.0106  288  ARG B NH2 
11115 N N   . VAL B 291  ? 0.2794 0.2136 0.2106 -0.0228 -0.0252 0.0187  289  VAL B N   
11116 C CA  . VAL B 291  ? 0.2711 0.2071 0.2003 -0.0264 -0.0234 0.0199  289  VAL B CA  
11117 C C   . VAL B 291  ? 0.2831 0.2129 0.2077 -0.0287 -0.0246 0.0229  289  VAL B C   
11118 O O   . VAL B 291  ? 0.2878 0.2187 0.2090 -0.0314 -0.0238 0.0249  289  VAL B O   
11119 C CB  . VAL B 291  ? 0.2734 0.2117 0.2061 -0.0275 -0.0218 0.0183  289  VAL B CB  
11120 C CG1 . VAL B 291  ? 0.3101 0.2513 0.2411 -0.0313 -0.0200 0.0196  289  VAL B CG1 
11121 C CG2 . VAL B 291  ? 0.3165 0.2602 0.2536 -0.0251 -0.0208 0.0155  289  VAL B CG2 
11122 N N   . LYS B 292  ? 0.2727 0.1959 0.1971 -0.0276 -0.0265 0.0233  290  LYS B N   
11123 C CA  A LYS B 292  ? 0.3060 0.2227 0.2260 -0.0297 -0.0278 0.0262  290  LYS B CA  
11124 C CA  B LYS B 292  ? 0.3062 0.2228 0.2262 -0.0297 -0.0279 0.0262  290  LYS B CA  
11125 C C   . LYS B 292  ? 0.2958 0.2120 0.2116 -0.0297 -0.0288 0.0284  290  LYS B C   
11126 O O   . LYS B 292  ? 0.3187 0.2332 0.2304 -0.0328 -0.0285 0.0310  290  LYS B O   
11127 C CB  A LYS B 292  ? 0.3220 0.2313 0.2425 -0.0279 -0.0298 0.0261  290  LYS B CB  
11128 C CB  B LYS B 292  ? 0.3223 0.2317 0.2429 -0.0276 -0.0299 0.0260  290  LYS B CB  
11129 C CG  A LYS B 292  ? 0.3077 0.2093 0.2235 -0.0301 -0.0312 0.0291  290  LYS B CG  
11130 C CG  B LYS B 292  ? 0.3476 0.2494 0.2636 -0.0282 -0.0320 0.0290  290  LYS B CG  
11131 C CD  A LYS B 292  ? 0.3759 0.2736 0.2886 -0.0282 -0.0335 0.0311  290  LYS B CD  
11132 C CD  B LYS B 292  ? 0.3392 0.2383 0.2515 -0.0327 -0.0314 0.0313  290  LYS B CD  
11133 C CE  A LYS B 292  ? 0.4120 0.3017 0.3197 -0.0305 -0.0349 0.0343  290  LYS B CE  
11134 C CE  B LYS B 292  ? 0.4386 0.3298 0.3459 -0.0332 -0.0335 0.0344  290  LYS B CE  
11135 N NZ  A LYS B 292  ? 0.4202 0.3032 0.3287 -0.0301 -0.0358 0.0337  290  LYS B NZ  
11136 N NZ  B LYS B 292  ? 0.4191 0.3029 0.3271 -0.0306 -0.0356 0.0340  290  LYS B NZ  
11137 N N   . ALA B 293  ? 0.2824 0.2002 0.1993 -0.0265 -0.0298 0.0275  291  ALA B N   
11138 C CA  . ALA B 293  ? 0.2999 0.2172 0.2125 -0.0265 -0.0309 0.0295  291  ALA B CA  
11139 C C   . ALA B 293  ? 0.3203 0.2429 0.2305 -0.0291 -0.0287 0.0301  291  ALA B C   
11140 O O   . ALA B 293  ? 0.3145 0.2355 0.2198 -0.0311 -0.0290 0.0327  291  ALA B O   
11141 C CB  . ALA B 293  ? 0.3225 0.2413 0.2372 -0.0227 -0.0325 0.0282  291  ALA B CB  
11142 N N   . LEU B 294  ? 0.2784 0.2075 0.1919 -0.0291 -0.0265 0.0278  292  LEU B N   
11143 C CA  . LEU B 294  ? 0.3012 0.2358 0.2129 -0.0313 -0.0242 0.0281  292  LEU B CA  
11144 C C   . LEU B 294  ? 0.2929 0.2262 0.2022 -0.0353 -0.0230 0.0303  292  LEU B C   
11145 O O   . LEU B 294  ? 0.2957 0.2302 0.2010 -0.0376 -0.0221 0.0324  292  LEU B O   
11146 C CB  . LEU B 294  ? 0.2715 0.2130 0.1875 -0.0302 -0.0222 0.0251  292  LEU B CB  
11147 C CG  . LEU B 294  ? 0.2757 0.2191 0.1940 -0.0266 -0.0231 0.0229  292  LEU B CG  
11148 C CD1 . LEU B 294  ? 0.2904 0.2398 0.2130 -0.0258 -0.0210 0.0201  292  LEU B CD1 
11149 C CD2 . LEU B 294  ? 0.2855 0.2294 0.1995 -0.0261 -0.0238 0.0239  292  LEU B CD2 
11150 N N   . ALA B 295  ? 0.2906 0.2215 0.2024 -0.0363 -0.0230 0.0300  293  ALA B N   
11151 C CA  . ALA B 295  ? 0.2896 0.2190 0.1995 -0.0404 -0.0221 0.0321  293  ALA B CA  
11152 C C   . ALA B 295  ? 0.3040 0.2270 0.2083 -0.0420 -0.0238 0.0355  293  ALA B C   
11153 O O   . ALA B 295  ? 0.3080 0.2316 0.2090 -0.0455 -0.0227 0.0379  293  ALA B O   
11154 C CB  . ALA B 295  ? 0.3008 0.2278 0.2141 -0.0409 -0.0223 0.0308  293  ALA B CB  
11155 N N   . LEU B 296  ? 0.3053 0.2223 0.2085 -0.0395 -0.0264 0.0359  294  LEU B N   
11156 C CA  . LEU B 296  ? 0.3248 0.2353 0.2226 -0.0407 -0.0282 0.0392  294  LEU B CA  
11157 C C   . LEU B 296  ? 0.3203 0.2341 0.2139 -0.0417 -0.0275 0.0409  294  LEU B C   
11158 O O   . LEU B 296  ? 0.3321 0.2436 0.2211 -0.0447 -0.0274 0.0439  294  LEU B O   
11159 C CB  . LEU B 296  ? 0.3636 0.2680 0.2618 -0.0372 -0.0311 0.0391  294  LEU B CB  
11160 C CG  . LEU B 296  ? 0.4293 0.3259 0.3223 -0.0379 -0.0335 0.0425  294  LEU B CG  
11161 C CD1 . LEU B 296  ? 0.4415 0.3333 0.3319 -0.0419 -0.0331 0.0447  294  LEU B CD1 
11162 C CD2 . LEU B 296  ? 0.4701 0.3615 0.3645 -0.0338 -0.0362 0.0419  294  LEU B CD2 
11163 N N   . LEU B 297  ? 0.3171 0.2363 0.2122 -0.0392 -0.0270 0.0389  295  LEU B N   
11164 C CA  . LEU B 297  ? 0.3455 0.2683 0.2364 -0.0400 -0.0261 0.0401  295  LEU B CA  
11165 C C   . LEU B 297  ? 0.3211 0.2487 0.2110 -0.0438 -0.0230 0.0410  295  LEU B C   
11166 O O   . LEU B 297  ? 0.3251 0.2524 0.2100 -0.0462 -0.0225 0.0437  295  LEU B O   
11167 C CB  . LEU B 297  ? 0.3298 0.2576 0.2228 -0.0367 -0.0259 0.0374  295  LEU B CB  
11168 C CG  . LEU B 297  ? 0.4140 0.3384 0.3071 -0.0332 -0.0290 0.0369  295  LEU B CG  
11169 C CD1 . LEU B 297  ? 0.3814 0.3114 0.2769 -0.0306 -0.0284 0.0340  295  LEU B CD1 
11170 C CD2 . LEU B 297  ? 0.4549 0.3746 0.3418 -0.0338 -0.0309 0.0402  295  LEU B CD2 
11171 N N   . ALA B 298  ? 0.3224 0.2546 0.2170 -0.0442 -0.0210 0.0388  296  ALA B N   
11172 C CA  . ALA B 298  ? 0.3022 0.2397 0.1966 -0.0476 -0.0181 0.0396  296  ALA B CA  
11173 C C   . ALA B 298  ? 0.3488 0.2816 0.2401 -0.0516 -0.0184 0.0430  296  ALA B C   
11174 O O   . ALA B 298  ? 0.3537 0.2889 0.2417 -0.0547 -0.0167 0.0452  296  ALA B O   
11175 C CB  . ALA B 298  ? 0.3097 0.2525 0.2101 -0.0472 -0.0163 0.0368  296  ALA B CB  
11176 N N   . LYS B 299  ? 0.3315 0.2574 0.2236 -0.0516 -0.0205 0.0433  297  LYS B N   
11177 C CA  A LYS B 299  ? 0.3314 0.2516 0.2202 -0.0554 -0.0212 0.0465  297  LYS B CA  
11178 C CA  B LYS B 299  ? 0.3313 0.2516 0.2202 -0.0554 -0.0212 0.0465  297  LYS B CA  
11179 C C   . LYS B 299  ? 0.3784 0.2953 0.2608 -0.0564 -0.0221 0.0499  297  LYS B C   
11180 O O   . LYS B 299  ? 0.3851 0.3017 0.2641 -0.0604 -0.0211 0.0528  297  LYS B O   
11181 C CB  A LYS B 299  ? 0.3872 0.2998 0.2777 -0.0544 -0.0236 0.0460  297  LYS B CB  
11182 C CB  B LYS B 299  ? 0.3874 0.2998 0.2777 -0.0544 -0.0236 0.0461  297  LYS B CB  
11183 C CG  A LYS B 299  ? 0.4125 0.3179 0.2995 -0.0581 -0.0247 0.0492  297  LYS B CG  
11184 C CG  B LYS B 299  ? 0.4100 0.3148 0.2961 -0.0579 -0.0249 0.0496  297  LYS B CG  
11185 C CD  A LYS B 299  ? 0.3943 0.2911 0.2768 -0.0566 -0.0276 0.0513  297  LYS B CD  
11186 C CD  B LYS B 299  ? 0.4450 0.3409 0.3313 -0.0558 -0.0278 0.0493  297  LYS B CD  
11187 C CE  A LYS B 299  ? 0.4459 0.3349 0.3246 -0.0603 -0.0287 0.0545  297  LYS B CE  
11188 C CE  B LYS B 299  ? 0.4685 0.3562 0.3506 -0.0594 -0.0290 0.0525  297  LYS B CE  
11189 N NZ  A LYS B 299  ? 0.5046 0.3898 0.3864 -0.0611 -0.0292 0.0531  297  LYS B NZ  
11190 N NZ  B LYS B 299  ? 0.4741 0.3592 0.3502 -0.0608 -0.0297 0.0562  297  LYS B NZ  
11191 N N   . ASN B 300  ? 0.3504 0.2648 0.2311 -0.0530 -0.0241 0.0496  298  ASN B N   
11192 C CA  . ASN B 300  ? 0.3959 0.3064 0.2702 -0.0539 -0.0254 0.0528  298  ASN B CA  
11193 C C   . ASN B 300  ? 0.3996 0.3164 0.2706 -0.0561 -0.0227 0.0540  298  ASN B C   
11194 O O   . ASN B 300  ? 0.4142 0.3285 0.2798 -0.0588 -0.0228 0.0575  298  ASN B O   
11195 C CB  . ASN B 300  ? 0.4065 0.3137 0.2800 -0.0496 -0.0281 0.0521  298  ASN B CB  
11196 C CG  . ASN B 300  ? 0.4530 0.3524 0.3283 -0.0478 -0.0309 0.0520  298  ASN B CG  
11197 O OD1 . ASN B 300  ? 0.5285 0.4228 0.4032 -0.0502 -0.0313 0.0536  298  ASN B OD1 
11198 N ND2 . ASN B 300  ? 0.5824 0.4810 0.4598 -0.0436 -0.0329 0.0502  298  ASN B ND2 
11199 N N   . TYR B 301  ? 0.3557 0.2807 0.2299 -0.0550 -0.0203 0.0513  299  TYR B N   
11200 C CA  . TYR B 301  ? 0.3758 0.3074 0.2473 -0.0570 -0.0175 0.0522  299  TYR B CA  
11201 C C   . TYR B 301  ? 0.3247 0.2606 0.1983 -0.0608 -0.0147 0.0529  299  TYR B C   
11202 O O   . TYR B 301  ? 0.3553 0.2970 0.2270 -0.0627 -0.0120 0.0538  299  TYR B O   
11203 C CB  . TYR B 301  ? 0.3402 0.2785 0.2139 -0.0537 -0.0162 0.0488  299  TYR B CB  
11204 C CG  . TYR B 301  ? 0.3482 0.2839 0.2190 -0.0504 -0.0185 0.0484  299  TYR B CG  
11205 C CD1 . TYR B 301  ? 0.3477 0.2822 0.2118 -0.0513 -0.0188 0.0508  299  TYR B CD1 
11206 C CD2 . TYR B 301  ? 0.3468 0.2815 0.2214 -0.0466 -0.0203 0.0455  299  TYR B CD2 
11207 C CE1 . TYR B 301  ? 0.3490 0.2813 0.2103 -0.0484 -0.0211 0.0504  299  TYR B CE1 
11208 C CE2 . TYR B 301  ? 0.3348 0.2676 0.2070 -0.0438 -0.0225 0.0451  299  TYR B CE2 
11209 C CZ  . TYR B 301  ? 0.3363 0.2679 0.2019 -0.0447 -0.0230 0.0475  299  TYR B CZ  
11210 O OH  . TYR B 301  ? 0.3646 0.2944 0.2278 -0.0420 -0.0254 0.0472  299  TYR B OH  
11211 N N   . ASP B 302  ? 0.3309 0.2643 0.2084 -0.0619 -0.0153 0.0524  300  ASP B N   
11212 C CA  . ASP B 302  ? 0.3554 0.2931 0.2359 -0.0655 -0.0130 0.0527  300  ASP B CA  
11213 C C   . ASP B 302  ? 0.3170 0.2648 0.2009 -0.0647 -0.0098 0.0504  300  ASP B C   
11214 O O   . ASP B 302  ? 0.3403 0.2939 0.2234 -0.0675 -0.0071 0.0517  300  ASP B O   
11215 C CB  . ASP B 302  ? 0.3489 0.2843 0.2250 -0.0704 -0.0124 0.0569  300  ASP B CB  
11216 C CG  . ASP B 302  ? 0.3987 0.3359 0.2784 -0.0742 -0.0113 0.0573  300  ASP B CG  
11217 O OD1 . ASP B 302  ? 0.4109 0.3469 0.2953 -0.0729 -0.0122 0.0549  300  ASP B OD1 
11218 O OD2 . ASP B 302  ? 0.4701 0.4102 0.3479 -0.0783 -0.0094 0.0600  300  ASP B OD2 
11219 N N   . ILE B 303  ? 0.3092 0.2592 0.1972 -0.0607 -0.0101 0.0468  301  ILE B N   
11220 C CA  . ILE B 303  ? 0.2958 0.2547 0.1878 -0.0595 -0.0074 0.0442  301  ILE B CA  
11221 C C   . ILE B 303  ? 0.3135 0.2730 0.2118 -0.0587 -0.0077 0.0417  301  ILE B C   
11222 O O   . ILE B 303  ? 0.3136 0.2666 0.2129 -0.0581 -0.0101 0.0414  301  ILE B O   
11223 C CB  . ILE B 303  ? 0.2885 0.2502 0.1796 -0.0555 -0.0071 0.0419  301  ILE B CB  
11224 C CG1 . ILE B 303  ? 0.3159 0.2732 0.2093 -0.0517 -0.0098 0.0396  301  ILE B CG1 
11225 C CG2 . ILE B 303  ? 0.3173 0.2776 0.2017 -0.0561 -0.0072 0.0443  301  ILE B CG2 
11226 C CD1 . ILE B 303  ? 0.3467 0.3073 0.2403 -0.0479 -0.0096 0.0369  301  ILE B CD1 
11227 N N   . GLY B 304  ? 0.2689 0.2364 0.1714 -0.0585 -0.0052 0.0398  302  GLY B N   
11228 C CA  . GLY B 304  ? 0.2863 0.2552 0.1947 -0.0573 -0.0054 0.0372  302  GLY B CA  
11229 C C   . GLY B 304  ? 0.2973 0.2654 0.2078 -0.0526 -0.0066 0.0341  302  GLY B C   
11230 O O   . GLY B 304  ? 0.2983 0.2687 0.2073 -0.0502 -0.0060 0.0331  302  GLY B O   
11231 N N   . LEU B 305  ? 0.2551 0.2197 0.1691 -0.0514 -0.0082 0.0325  303  LEU B N   
11232 C CA  . LEU B 305  ? 0.2721 0.2368 0.1891 -0.0472 -0.0091 0.0294  303  LEU B CA  
11233 C C   . LEU B 305  ? 0.2689 0.2365 0.1914 -0.0472 -0.0084 0.0273  303  LEU B C   
11234 O O   . LEU B 305  ? 0.2747 0.2383 0.1982 -0.0488 -0.0096 0.0278  303  LEU B O   
11235 C CB  . LEU B 305  ? 0.2895 0.2462 0.2048 -0.0452 -0.0122 0.0295  303  LEU B CB  
11236 C CG  . LEU B 305  ? 0.2866 0.2436 0.2052 -0.0410 -0.0131 0.0265  303  LEU B CG  
11237 C CD1 . LEU B 305  ? 0.3338 0.2860 0.2495 -0.0387 -0.0154 0.0269  303  LEU B CD1 
11238 C CD2 . LEU B 305  ? 0.3306 0.2853 0.2534 -0.0403 -0.0140 0.0249  303  LEU B CD2 
11239 N N   . ASN B 306  ? 0.2510 0.2252 0.1767 -0.0452 -0.0067 0.0251  304  ASN B N   
11240 C CA  . ASN B 306  ? 0.2424 0.2207 0.1733 -0.0453 -0.0057 0.0233  304  ASN B CA  
11241 C C   . ASN B 306  ? 0.2432 0.2209 0.1774 -0.0414 -0.0066 0.0203  304  ASN B C   
11242 O O   . ASN B 306  ? 0.2454 0.2240 0.1789 -0.0385 -0.0067 0.0191  304  ASN B O   
11243 C CB  . ASN B 306  ? 0.2557 0.2427 0.1882 -0.0460 -0.0027 0.0231  304  ASN B CB  
11244 C CG  . ASN B 306  ? 0.2511 0.2428 0.1890 -0.0455 -0.0018 0.0211  304  ASN B CG  
11245 O OD1 . ASN B 306  ? 0.2897 0.2818 0.2294 -0.0483 -0.0017 0.0220  304  ASN B OD1 
11246 N ND2 . ASN B 306  ? 0.2614 0.2563 0.2018 -0.0421 -0.0012 0.0185  304  ASN B ND2 
11247 N N   . ILE B 307  ? 0.2478 0.2239 0.1853 -0.0414 -0.0074 0.0192  305  ILE B N   
11248 C CA  . ILE B 307  ? 0.2331 0.2094 0.1742 -0.0381 -0.0080 0.0164  305  ILE B CA  
11249 C C   . ILE B 307  ? 0.2533 0.2371 0.1985 -0.0377 -0.0059 0.0148  305  ILE B C   
11250 O O   . ILE B 307  ? 0.2298 0.2156 0.1771 -0.0399 -0.0053 0.0150  305  ILE B O   
11251 C CB  . ILE B 307  ? 0.2434 0.2136 0.1855 -0.0380 -0.0100 0.0160  305  ILE B CB  
11252 C CG1 . ILE B 307  ? 0.2827 0.2455 0.2209 -0.0379 -0.0122 0.0176  305  ILE B CG1 
11253 C CG2 . ILE B 307  ? 0.2749 0.2461 0.2210 -0.0347 -0.0103 0.0131  305  ILE B CG2 
11254 C CD1 . ILE B 307  ? 0.2969 0.2533 0.2358 -0.0378 -0.0140 0.0173  305  ILE B CD1 
11255 N N   . ASP B 308  ? 0.2304 0.2180 0.1765 -0.0350 -0.0050 0.0131  306  ASP B N   
11256 C CA  . ASP B 308  ? 0.2348 0.2292 0.1848 -0.0341 -0.0031 0.0115  306  ASP B CA  
11257 C C   . ASP B 308  ? 0.2279 0.2213 0.1818 -0.0330 -0.0039 0.0097  306  ASP B C   
11258 O O   . ASP B 308  ? 0.2442 0.2323 0.1980 -0.0316 -0.0058 0.0091  306  ASP B O   
11259 C CB  . ASP B 308  ? 0.2354 0.2327 0.1851 -0.0310 -0.0022 0.0100  306  ASP B CB  
11260 C CG  . ASP B 308  ? 0.2551 0.2545 0.2009 -0.0319 -0.0008 0.0114  306  ASP B CG  
11261 O OD1 . ASP B 308  ? 0.2564 0.2566 0.2004 -0.0350 -0.0001 0.0136  306  ASP B OD1 
11262 O OD2 . ASP B 308  ? 0.2692 0.2696 0.2137 -0.0296 -0.0005 0.0102  306  ASP B OD2 
11263 N N   . ALA B 309  ? 0.2052 0.2041 0.1626 -0.0335 -0.0025 0.0090  307  ALA B N   
11264 C CA  . ALA B 309  ? 0.2109 0.2094 0.1719 -0.0327 -0.0032 0.0074  307  ALA B CA  
11265 C C   . ALA B 309  ? 0.2017 0.2033 0.1653 -0.0292 -0.0026 0.0051  307  ALA B C   
11266 O O   . ALA B 309  ? 0.2233 0.2299 0.1873 -0.0282 -0.0009 0.0047  307  ALA B O   
11267 C CB  . ALA B 309  ? 0.2163 0.2188 0.1795 -0.0355 -0.0023 0.0080  307  ALA B CB  
11268 N N   . GLU B 310  ? 0.1995 0.1977 0.1646 -0.0272 -0.0039 0.0035  308  GLU B N   
11269 C CA  . GLU B 310  ? 0.1991 0.1993 0.1664 -0.0239 -0.0036 0.0014  308  GLU B CA  
11270 C C   . GLU B 310  ? 0.1898 0.1921 0.1610 -0.0233 -0.0034 0.0000  308  GLU B C   
11271 O O   . GLU B 310  ? 0.1929 0.1989 0.1656 -0.0252 -0.0025 0.0005  308  GLU B O   
11272 C CB  . GLU B 310  ? 0.2099 0.2050 0.1756 -0.0218 -0.0052 0.0009  308  GLU B CB  
11273 C CG  . GLU B 310  ? 0.2320 0.2256 0.1937 -0.0224 -0.0054 0.0024  308  GLU B CG  
11274 C CD  . GLU B 310  ? 0.2458 0.2351 0.2061 -0.0203 -0.0070 0.0019  308  GLU B CD  
11275 O OE1 . GLU B 310  ? 0.2578 0.2489 0.2191 -0.0180 -0.0068 0.0005  308  GLU B OE1 
11276 O OE2 . GLU B 310  ? 0.2440 0.2282 0.2021 -0.0210 -0.0086 0.0031  308  GLU B OE2 
11277 N N   . GLU B 311  ? 0.2012 0.2015 0.1740 -0.0209 -0.0042 -0.0016 309  GLU B N   
11278 C CA  . GLU B 311  ? 0.1864 0.1890 0.1627 -0.0202 -0.0040 -0.0029 309  GLU B CA  
11279 C C   . GLU B 311  ? 0.1953 0.1954 0.1716 -0.0224 -0.0048 -0.0024 309  GLU B C   
11280 O O   . GLU B 311  ? 0.2067 0.2019 0.1806 -0.0238 -0.0060 -0.0013 309  GLU B O   
11281 C CB  . GLU B 311  ? 0.1940 0.1948 0.1717 -0.0171 -0.0046 -0.0046 309  GLU B CB  
11282 C CG  . GLU B 311  ? 0.2301 0.2333 0.2079 -0.0149 -0.0039 -0.0054 309  GLU B CG  
11283 C CD  . GLU B 311  ? 0.2735 0.2732 0.2484 -0.0143 -0.0048 -0.0050 309  GLU B CD  
11284 O OE1 . GLU B 311  ? 0.2342 0.2304 0.2066 -0.0158 -0.0057 -0.0036 309  GLU B OE1 
11285 O OE2 . GLU B 311  ? 0.3374 0.3377 0.3125 -0.0122 -0.0047 -0.0060 309  GLU B OE2 
11286 N N   . ALA B 312  ? 0.1893 0.1927 0.1684 -0.0227 -0.0043 -0.0031 310  ALA B N   
11287 C CA  . ALA B 312  ? 0.2070 0.2085 0.1861 -0.0250 -0.0052 -0.0027 310  ALA B CA  
11288 C C   . ALA B 312  ? 0.1881 0.1828 0.1659 -0.0243 -0.0068 -0.0033 310  ALA B C   
11289 O O   . ALA B 312  ? 0.2052 0.1960 0.1812 -0.0265 -0.0078 -0.0025 310  ALA B O   
11290 C CB  . ALA B 312  ? 0.2028 0.2089 0.1850 -0.0250 -0.0045 -0.0036 310  ALA B CB  
11291 N N   . ASP B 313  ? 0.1993 0.1924 0.1779 -0.0213 -0.0071 -0.0046 311  ASP B N   
11292 C CA  . ASP B 313  ? 0.1941 0.1812 0.1718 -0.0203 -0.0084 -0.0052 311  ASP B CA  
11293 C C   . ASP B 313  ? 0.2220 0.2041 0.1967 -0.0205 -0.0095 -0.0040 311  ASP B C   
11294 O O   . ASP B 313  ? 0.2209 0.1980 0.1948 -0.0194 -0.0106 -0.0044 311  ASP B O   
11295 C CB  . ASP B 313  ? 0.2239 0.2114 0.2039 -0.0171 -0.0084 -0.0069 311  ASP B CB  
11296 C CG  . ASP B 313  ? 0.2497 0.2387 0.2302 -0.0149 -0.0081 -0.0072 311  ASP B CG  
11297 O OD1 . ASP B 313  ? 0.2536 0.2429 0.2323 -0.0155 -0.0080 -0.0062 311  ASP B OD1 
11298 O OD2 . ASP B 313  ? 0.2827 0.2724 0.2652 -0.0125 -0.0080 -0.0085 311  ASP B OD2 
11299 N N   . ARG B 314  ? 0.2054 0.1888 0.1783 -0.0219 -0.0091 -0.0026 312  ARG B N   
11300 C CA  . ARG B 314  ? 0.2143 0.1929 0.1840 -0.0225 -0.0102 -0.0011 312  ARG B CA  
11301 C C   . ARG B 314  ? 0.2116 0.1885 0.1789 -0.0261 -0.0104 0.0006  312  ARG B C   
11302 O O   . ARG B 314  ? 0.2286 0.2007 0.1930 -0.0269 -0.0114 0.0020  312  ARG B O   
11303 C CB  . ARG B 314  ? 0.2140 0.1946 0.1828 -0.0213 -0.0097 -0.0007 312  ARG B CB  
11304 C CG  . ARG B 314  ? 0.2127 0.1928 0.1830 -0.0180 -0.0102 -0.0021 312  ARG B CG  
11305 C CD  . ARG B 314  ? 0.2240 0.2074 0.1940 -0.0168 -0.0095 -0.0022 312  ARG B CD  
11306 N NE  . ARG B 314  ? 0.2344 0.2160 0.2051 -0.0141 -0.0105 -0.0031 312  ARG B NE  
11307 C CZ  . ARG B 314  ? 0.2241 0.2078 0.1947 -0.0127 -0.0103 -0.0036 312  ARG B CZ  
11308 N NH1 . ARG B 314  ? 0.2355 0.2232 0.2055 -0.0132 -0.0089 -0.0036 312  ARG B NH1 
11309 N NH2 . ARG B 314  ? 0.2505 0.2320 0.2214 -0.0106 -0.0115 -0.0041 312  ARG B NH2 
11310 N N   . LEU B 315  ? 0.2120 0.1927 0.1807 -0.0283 -0.0095 0.0007  313  LEU B N   
11311 C CA  . LEU B 315  ? 0.2257 0.2056 0.1924 -0.0320 -0.0096 0.0026  313  LEU B CA  
11312 C C   . LEU B 315  ? 0.2370 0.2091 0.2012 -0.0332 -0.0114 0.0030  313  LEU B C   
11313 O O   . LEU B 315  ? 0.2287 0.1968 0.1897 -0.0347 -0.0121 0.0048  313  LEU B O   
11314 C CB  . LEU B 315  ? 0.2131 0.1986 0.1823 -0.0340 -0.0086 0.0024  313  LEU B CB  
11315 C CG  . LEU B 315  ? 0.2266 0.2142 0.1947 -0.0380 -0.0082 0.0044  313  LEU B CG  
11316 C CD1 . LEU B 315  ? 0.2393 0.2334 0.2108 -0.0392 -0.0073 0.0039  313  LEU B CD1 
11317 C CD2 . LEU B 315  ? 0.2833 0.2641 0.2483 -0.0409 -0.0097 0.0057  313  LEU B CD2 
11318 N N   . GLU B 316  ? 0.2236 0.1931 0.1888 -0.0323 -0.0121 0.0015  314  GLU B N   
11319 C CA  . GLU B 316  ? 0.2314 0.1935 0.1940 -0.0335 -0.0137 0.0018  314  GLU B CA  
11320 C C   . GLU B 316  ? 0.2476 0.2038 0.2081 -0.0313 -0.0148 0.0022  314  GLU B C   
11321 O O   . GLU B 316  ? 0.2551 0.2053 0.2124 -0.0329 -0.0159 0.0035  314  GLU B O   
11322 C CB  . GLU B 316  ? 0.2308 0.1917 0.1948 -0.0332 -0.0140 0.0000  314  GLU B CB  
11323 C CG  . GLU B 316  ? 0.2257 0.1916 0.1911 -0.0362 -0.0134 0.0002  314  GLU B CG  
11324 C CD  . GLU B 316  ? 0.2756 0.2406 0.2420 -0.0362 -0.0138 -0.0016 314  GLU B CD  
11325 O OE1 . GLU B 316  ? 0.2698 0.2279 0.2340 -0.0359 -0.0151 -0.0022 314  GLU B OE1 
11326 O OE2 . GLU B 316  ? 0.2545 0.2255 0.2236 -0.0365 -0.0130 -0.0022 314  GLU B OE2 
11327 N N   . LEU B 317  ? 0.2420 0.1998 0.2042 -0.0279 -0.0145 0.0011  315  LEU B N   
11328 C CA  . LEU B 317  ? 0.2645 0.2177 0.2250 -0.0258 -0.0156 0.0016  315  LEU B CA  
11329 C C   . LEU B 317  ? 0.2522 0.2042 0.2095 -0.0277 -0.0159 0.0040  315  LEU B C   
11330 O O   . LEU B 317  ? 0.2751 0.2209 0.2296 -0.0278 -0.0172 0.0052  315  LEU B O   
11331 C CB  . LEU B 317  ? 0.2840 0.2405 0.2471 -0.0222 -0.0152 0.0003  315  LEU B CB  
11332 C CG  . LEU B 317  ? 0.2913 0.2440 0.2532 -0.0198 -0.0164 0.0008  315  LEU B CG  
11333 C CD1 . LEU B 317  ? 0.3322 0.2778 0.2927 -0.0190 -0.0178 0.0007  315  LEU B CD1 
11334 C CD2 . LEU B 317  ? 0.3065 0.2630 0.2714 -0.0167 -0.0159 -0.0007 315  LEU B CD2 
11335 N N   . SER B 318  ? 0.2352 0.1930 0.1929 -0.0293 -0.0145 0.0048  316  SER B N   
11336 C CA  . SER B 318  ? 0.2373 0.1943 0.1918 -0.0312 -0.0146 0.0071  316  SER B CA  
11337 C C   . SER B 318  ? 0.2451 0.1971 0.1967 -0.0346 -0.0155 0.0089  316  SER B C   
11338 O O   . SER B 318  ? 0.2559 0.2041 0.2042 -0.0357 -0.0163 0.0108  316  SER B O   
11339 C CB  . SER B 318  ? 0.2510 0.2154 0.2064 -0.0321 -0.0128 0.0075  316  SER B CB  
11340 O OG  . SER B 318  ? 0.2468 0.2148 0.2035 -0.0350 -0.0118 0.0077  316  SER B OG  
11341 N N   . LEU B 319  ? 0.2394 0.1911 0.1920 -0.0365 -0.0155 0.0082  317  LEU B N   
11342 C CA  . LEU B 319  ? 0.2466 0.1931 0.1963 -0.0400 -0.0164 0.0098  317  LEU B CA  
11343 C C   . LEU B 319  ? 0.2629 0.2003 0.2098 -0.0387 -0.0183 0.0101  317  LEU B C   
11344 O O   . LEU B 319  ? 0.2731 0.2052 0.2166 -0.0411 -0.0193 0.0120  317  LEU B O   
11345 C CB  . LEU B 319  ? 0.2460 0.1938 0.1974 -0.0421 -0.0162 0.0088  317  LEU B CB  
11346 C CG  . LEU B 319  ? 0.2377 0.1944 0.1920 -0.0437 -0.0145 0.0087  317  LEU B CG  
11347 C CD1 . LEU B 319  ? 0.2567 0.2139 0.2127 -0.0453 -0.0148 0.0075  317  LEU B CD1 
11348 C CD2 . LEU B 319  ? 0.2980 0.2575 0.2508 -0.0471 -0.0137 0.0113  317  LEU B CD2 
11349 N N   . ASP B 320  ? 0.2776 0.2133 0.2260 -0.0348 -0.0189 0.0082  318  ASP B N   
11350 C CA  . ASP B 320  ? 0.3003 0.2278 0.2463 -0.0331 -0.0206 0.0085  318  ASP B CA  
11351 C C   . ASP B 320  ? 0.2822 0.2077 0.2256 -0.0328 -0.0213 0.0106  318  ASP B C   
11352 O O   . ASP B 320  ? 0.3270 0.2453 0.2673 -0.0331 -0.0228 0.0120  318  ASP B O   
11353 C CB  . ASP B 320  ? 0.2982 0.2253 0.2468 -0.0290 -0.0208 0.0061  318  ASP B CB  
11354 C CG  . ASP B 320  ? 0.2856 0.2117 0.2353 -0.0295 -0.0206 0.0042  318  ASP B CG  
11355 O OD1 . ASP B 320  ? 0.3233 0.2435 0.2704 -0.0316 -0.0216 0.0047  318  ASP B OD1 
11356 O OD2 . ASP B 320  ? 0.3206 0.2518 0.2737 -0.0280 -0.0196 0.0024  318  ASP B OD2 
11357 N N   . LEU B 321  ? 0.2540 0.1854 0.1984 -0.0321 -0.0203 0.0110  319  LEU B N   
11358 C CA  . LEU B 321  ? 0.2929 0.2227 0.2344 -0.0321 -0.0209 0.0131  319  LEU B CA  
11359 C C   . LEU B 321  ? 0.2854 0.2142 0.2236 -0.0364 -0.0207 0.0156  319  LEU B C   
11360 O O   . LEU B 321  ? 0.3123 0.2354 0.2468 -0.0373 -0.0220 0.0177  319  LEU B O   
11361 C CB  . LEU B 321  ? 0.2919 0.2282 0.2351 -0.0301 -0.0200 0.0126  319  LEU B CB  
11362 C CG  . LEU B 321  ? 0.2891 0.2253 0.2347 -0.0258 -0.0206 0.0107  319  LEU B CG  
11363 C CD1 . LEU B 321  ? 0.3209 0.2611 0.2707 -0.0245 -0.0195 0.0081  319  LEU B CD1 
11364 C CD2 . LEU B 321  ? 0.3137 0.2530 0.2588 -0.0243 -0.0206 0.0112  319  LEU B CD2 
11365 N N   . LEU B 322  ? 0.2787 0.2130 0.2183 -0.0392 -0.0192 0.0156  320  LEU B N   
11366 C CA  . LEU B 322  ? 0.2900 0.2240 0.2268 -0.0436 -0.0188 0.0181  320  LEU B CA  
11367 C C   . LEU B 322  ? 0.2915 0.2167 0.2253 -0.0456 -0.0206 0.0193  320  LEU B C   
11368 O O   . LEU B 322  ? 0.3054 0.2269 0.2354 -0.0480 -0.0212 0.0219  320  LEU B O   
11369 C CB  . LEU B 322  ? 0.2738 0.2150 0.2133 -0.0460 -0.0170 0.0176  320  LEU B CB  
11370 C CG  . LEU B 322  ? 0.2812 0.2235 0.2186 -0.0508 -0.0164 0.0202  320  LEU B CG  
11371 C CD1 . LEU B 322  ? 0.3059 0.2505 0.2409 -0.0510 -0.0156 0.0222  320  LEU B CD1 
11372 C CD2 . LEU B 322  ? 0.2770 0.2266 0.2178 -0.0530 -0.0148 0.0195  320  LEU B CD2 
11373 N N   . GLU B 323  ? 0.3025 0.2242 0.2376 -0.0446 -0.0213 0.0174  321  GLU B N   
11374 C CA  . GLU B 323  ? 0.3086 0.2215 0.2407 -0.0462 -0.0230 0.0181  321  GLU B CA  
11375 C C   . GLU B 323  ? 0.3012 0.2067 0.2298 -0.0446 -0.0247 0.0197  321  GLU B C   
11376 O O   . GLU B 323  ? 0.3474 0.2471 0.2721 -0.0473 -0.0257 0.0220  321  GLU B O   
11377 C CB  . GLU B 323  ? 0.3506 0.2613 0.2848 -0.0445 -0.0235 0.0153  321  GLU B CB  
11378 C CG  . GLU B 323  ? 0.4131 0.3136 0.3439 -0.0452 -0.0253 0.0155  321  GLU B CG  
11379 C CD  . GLU B 323  ? 0.4287 0.3278 0.3584 -0.0498 -0.0254 0.0159  321  GLU B CD  
11380 O OE1 . GLU B 323  ? 0.4045 0.3112 0.3369 -0.0520 -0.0241 0.0156  321  GLU B OE1 
11381 O OE2 . GLU B 323  ? 0.4057 0.2961 0.3320 -0.0513 -0.0270 0.0165  321  GLU B OE2 
11382 N N   . VAL B 324  ? 0.2907 0.1965 0.2206 -0.0401 -0.0251 0.0185  322  VAL B N   
11383 C CA  . VAL B 324  ? 0.3267 0.2260 0.2537 -0.0382 -0.0268 0.0200  322  VAL B CA  
11384 C C   . VAL B 324  ? 0.2922 0.1921 0.2158 -0.0406 -0.0268 0.0231  322  VAL B C   
11385 O O   . VAL B 324  ? 0.3382 0.2312 0.2579 -0.0419 -0.0282 0.0254  322  VAL B O   
11386 C CB  . VAL B 324  ? 0.3212 0.2220 0.2508 -0.0331 -0.0272 0.0183  322  VAL B CB  
11387 C CG1 . VAL B 324  ? 0.3480 0.2431 0.2747 -0.0312 -0.0290 0.0201  322  VAL B CG1 
11388 C CG2 . VAL B 324  ? 0.3471 0.2463 0.2794 -0.0308 -0.0273 0.0155  322  VAL B CG2 
11389 N N   . LEU B 325  ? 0.3060 0.2141 0.2311 -0.0412 -0.0251 0.0232  323  LEU B N   
11390 C CA  . LEU B 325  ? 0.3292 0.2384 0.2510 -0.0432 -0.0249 0.0259  323  LEU B CA  
11391 C C   . LEU B 325  ? 0.3050 0.2109 0.2236 -0.0481 -0.0249 0.0284  323  LEU B C   
11392 O O   . LEU B 325  ? 0.3204 0.2219 0.2348 -0.0496 -0.0259 0.0312  323  LEU B O   
11393 C CB  . LEU B 325  ? 0.3113 0.2300 0.2353 -0.0429 -0.0228 0.0253  323  LEU B CB  
11394 C CG  . LEU B 325  ? 0.3295 0.2511 0.2563 -0.0383 -0.0230 0.0231  323  LEU B CG  
11395 C CD1 . LEU B 325  ? 0.3527 0.2834 0.2821 -0.0381 -0.0208 0.0218  323  LEU B CD1 
11396 C CD2 . LEU B 325  ? 0.3260 0.2434 0.2497 -0.0364 -0.0247 0.0247  323  LEU B CD2 
11397 N N   . CYS B 326  ? 0.3239 0.2318 0.2443 -0.0508 -0.0240 0.0276  324  CYS B N   
11398 C CA  . CYS B 326  ? 0.3108 0.2160 0.2284 -0.0559 -0.0241 0.0300  324  CYS B CA  
11399 C C   . CYS B 326  ? 0.3343 0.2285 0.2483 -0.0566 -0.0264 0.0311  324  CYS B C   
11400 O O   . CYS B 326  ? 0.3343 0.2247 0.2447 -0.0605 -0.0269 0.0338  324  CYS B O   
11401 C CB  . CYS B 326  ? 0.3222 0.2328 0.2430 -0.0586 -0.0227 0.0287  324  CYS B CB  
11402 S SG  . CYS B 326  ? 0.3420 0.2655 0.2663 -0.0590 -0.0198 0.0284  324  CYS B SG  
11403 N N   . LEU B 327  ? 0.3440 0.2330 0.2586 -0.0528 -0.0278 0.0292  325  LEU B N   
11404 C CA  . LEU B 327  ? 0.3736 0.2517 0.2847 -0.0527 -0.0300 0.0300  325  LEU B CA  
11405 C C   . LEU B 327  ? 0.3975 0.2707 0.3059 -0.0498 -0.0315 0.0316  325  LEU B C   
11406 O O   . LEU B 327  ? 0.4187 0.2825 0.3240 -0.0492 -0.0334 0.0325  325  LEU B O   
11407 C CB  . LEU B 327  ? 0.3636 0.2384 0.2769 -0.0503 -0.0306 0.0269  325  LEU B CB  
11408 C CG  . LEU B 327  ? 0.4371 0.3155 0.3527 -0.0532 -0.0295 0.0254  325  LEU B CG  
11409 C CD1 . LEU B 327  ? 0.4991 0.3739 0.4163 -0.0505 -0.0301 0.0223  325  LEU B CD1 
11410 C CD2 . LEU B 327  ? 0.4801 0.3549 0.3925 -0.0588 -0.0299 0.0277  325  LEU B CD2 
11411 N N   . ASP B 328  ? 0.3498 0.2288 0.2591 -0.0479 -0.0308 0.0320  326  ASP B N   
11412 C CA  . ASP B 328  ? 0.3493 0.2245 0.2564 -0.0449 -0.0324 0.0333  326  ASP B CA  
11413 C C   . ASP B 328  ? 0.3661 0.2375 0.2679 -0.0482 -0.0330 0.0372  326  ASP B C   
11414 O O   . ASP B 328  ? 0.3723 0.2495 0.2733 -0.0508 -0.0316 0.0386  326  ASP B O   
11415 C CB  . ASP B 328  ? 0.3589 0.2422 0.2689 -0.0418 -0.0314 0.0320  326  ASP B CB  
11416 C CG  . ASP B 328  ? 0.4497 0.3299 0.3582 -0.0382 -0.0332 0.0330  326  ASP B CG  
11417 O OD1 . ASP B 328  ? 0.4213 0.2943 0.3254 -0.0390 -0.0348 0.0357  326  ASP B OD1 
11418 O OD2 . ASP B 328  ? 0.4800 0.3647 0.3915 -0.0346 -0.0330 0.0312  326  ASP B OD2 
11419 N N   . GLY B 329  ? 0.4043 0.2658 0.3025 -0.0481 -0.0352 0.0389  327  GLY B N   
11420 C CA  . GLY B 329  ? 0.4181 0.2749 0.3110 -0.0514 -0.0360 0.0427  327  GLY B CA  
11421 C C   . GLY B 329  ? 0.4158 0.2763 0.3068 -0.0505 -0.0360 0.0447  327  GLY B C   
11422 O O   . GLY B 329  ? 0.3957 0.2552 0.2826 -0.0540 -0.0359 0.0478  327  GLY B O   
11423 N N   . ASP B 330  ? 0.4032 0.2679 0.2969 -0.0461 -0.0360 0.0429  328  ASP B N   
11424 C CA  . ASP B 330  ? 0.3770 0.2460 0.2689 -0.0454 -0.0359 0.0445  328  ASP B CA  
11425 C C   . ASP B 330  ? 0.4269 0.3040 0.3187 -0.0490 -0.0333 0.0450  328  ASP B C   
11426 O O   . ASP B 330  ? 0.4515 0.3307 0.3401 -0.0499 -0.0331 0.0472  328  ASP B O   
11427 C CB  . ASP B 330  ? 0.3981 0.2708 0.2934 -0.0403 -0.0364 0.0421  328  ASP B CB  
11428 C CG  . ASP B 330  ? 0.4783 0.3435 0.3732 -0.0364 -0.0391 0.0422  328  ASP B CG  
11429 O OD1 . ASP B 330  ? 0.5235 0.3803 0.4144 -0.0375 -0.0408 0.0447  328  ASP B OD1 
11430 O OD2 . ASP B 330  ? 0.4739 0.3417 0.3726 -0.0323 -0.0395 0.0399  328  ASP B OD2 
11431 N N   . LEU B 331  ? 0.3691 0.2510 0.2643 -0.0509 -0.0314 0.0432  329  LEU B N   
11432 C CA  . LEU B 331  ? 0.3776 0.2676 0.2733 -0.0542 -0.0288 0.0436  329  LEU B CA  
11433 C C   . LEU B 331  ? 0.3670 0.2547 0.2602 -0.0596 -0.0283 0.0460  329  LEU B C   
11434 O O   . LEU B 331  ? 0.3805 0.2751 0.2752 -0.0626 -0.0260 0.0460  329  LEU B O   
11435 C CB  . LEU B 331  ? 0.3649 0.2629 0.2663 -0.0527 -0.0270 0.0401  329  LEU B CB  
11436 C CG  . LEU B 331  ? 0.3445 0.2453 0.2487 -0.0476 -0.0274 0.0376  329  LEU B CG  
11437 C CD1 . LEU B 331  ? 0.3227 0.2303 0.2324 -0.0462 -0.0257 0.0342  329  LEU B CD1 
11438 C CD2 . LEU B 331  ? 0.3265 0.2308 0.2281 -0.0469 -0.0271 0.0390  329  LEU B CD2 
11439 N N   . SER B 332  ? 0.4067 0.2847 0.2962 -0.0609 -0.0303 0.0482  330  SER B N   
11440 C CA  . SER B 332  ? 0.4067 0.2809 0.2936 -0.0662 -0.0303 0.0505  330  SER B CA  
11441 C C   . SER B 332  ? 0.4063 0.2871 0.2916 -0.0703 -0.0281 0.0529  330  SER B C   
11442 O O   . SER B 332  ? 0.4455 0.3281 0.3279 -0.0700 -0.0278 0.0548  330  SER B O   
11443 C CB  . SER B 332  ? 0.4809 0.3436 0.3629 -0.0664 -0.0330 0.0530  330  SER B CB  
11444 O OG  . SER B 332  ? 0.5402 0.3986 0.4194 -0.0717 -0.0330 0.0554  330  SER B OG  
11445 N N   . GLY B 333  ? 0.3892 0.2738 0.2765 -0.0744 -0.0266 0.0529  331  GLY B N   
11446 C CA  . GLY B 333  ? 0.3946 0.2852 0.2806 -0.0789 -0.0244 0.0553  331  GLY B CA  
11447 C C   . GLY B 333  ? 0.4107 0.3126 0.2994 -0.0775 -0.0218 0.0541  331  GLY B C   
11448 O O   . GLY B 333  ? 0.4253 0.3330 0.3131 -0.0809 -0.0197 0.0561  331  GLY B O   
11449 N N   . TRP B 334  ? 0.3968 0.3018 0.2885 -0.0726 -0.0217 0.0510  332  TRP B N   
11450 C CA  . TRP B 334  ? 0.3696 0.2847 0.2637 -0.0709 -0.0193 0.0496  332  TRP B CA  
11451 C C   . TRP B 334  ? 0.3397 0.2624 0.2391 -0.0721 -0.0173 0.0475  332  TRP B C   
11452 O O   . TRP B 334  ? 0.3598 0.2813 0.2628 -0.0705 -0.0180 0.0448  332  TRP B O   
11453 C CB  . TRP B 334  ? 0.3969 0.3117 0.2919 -0.0654 -0.0203 0.0473  332  TRP B CB  
11454 C CG  . TRP B 334  ? 0.3595 0.2835 0.2569 -0.0631 -0.0182 0.0453  332  TRP B CG  
11455 C CD1 . TRP B 334  ? 0.3846 0.3145 0.2799 -0.0642 -0.0162 0.0466  332  TRP B CD1 
11456 C CD2 . TRP B 334  ? 0.3333 0.2612 0.2354 -0.0591 -0.0179 0.0416  332  TRP B CD2 
11457 N NE1 . TRP B 334  ? 0.3350 0.2720 0.2334 -0.0610 -0.0147 0.0438  332  TRP B NE1 
11458 C CE2 . TRP B 334  ? 0.3312 0.2671 0.2339 -0.0580 -0.0158 0.0408  332  TRP B CE2 
11459 C CE3 . TRP B 334  ? 0.3427 0.2682 0.2487 -0.0565 -0.0192 0.0389  332  TRP B CE3 
11460 C CZ2 . TRP B 334  ? 0.3084 0.2494 0.2152 -0.0544 -0.0151 0.0375  332  TRP B CZ2 
11461 C CZ3 . TRP B 334  ? 0.3735 0.3043 0.2835 -0.0530 -0.0183 0.0358  332  TRP B CZ3 
11462 C CH2 . TRP B 334  ? 0.3500 0.2885 0.2605 -0.0520 -0.0164 0.0351  332  TRP B CH2 
11463 N N   . ASN B 335  ? 0.3455 0.2761 0.2454 -0.0749 -0.0147 0.0486  333  ASN B N   
11464 C CA  . ASN B 335  ? 0.3414 0.2799 0.2465 -0.0762 -0.0127 0.0469  333  ASN B CA  
11465 C C   . ASN B 335  ? 0.3256 0.2728 0.2339 -0.0726 -0.0107 0.0443  333  ASN B C   
11466 O O   . ASN B 335  ? 0.3355 0.2907 0.2478 -0.0735 -0.0086 0.0432  333  ASN B O   
11467 C CB  . ASN B 335  ? 0.3737 0.3155 0.2780 -0.0818 -0.0112 0.0498  333  ASN B CB  
11468 C CG  . ASN B 335  ? 0.3909 0.3243 0.2930 -0.0856 -0.0133 0.0518  333  ASN B CG  
11469 O OD1 . ASN B 335  ? 0.3684 0.2953 0.2714 -0.0842 -0.0154 0.0501  333  ASN B OD1 
11470 N ND2 . ASN B 335  ? 0.4198 0.3529 0.3189 -0.0905 -0.0126 0.0553  333  ASN B ND2 
11471 N N   . GLY B 336  ? 0.3149 0.2606 0.2216 -0.0686 -0.0114 0.0433  334  GLY B N   
11472 C CA  . GLY B 336  ? 0.3209 0.2741 0.2300 -0.0653 -0.0097 0.0410  334  GLY B CA  
11473 C C   . GLY B 336  ? 0.3038 0.2579 0.2175 -0.0614 -0.0102 0.0373  334  GLY B C   
11474 O O   . GLY B 336  ? 0.2918 0.2516 0.2074 -0.0585 -0.0089 0.0353  334  GLY B O   
11475 N N   . MET B 337  ? 0.3108 0.2595 0.2263 -0.0611 -0.0121 0.0363  335  MET B N   
11476 C CA  . MET B 337  ? 0.2853 0.2356 0.2053 -0.0575 -0.0124 0.0328  335  MET B CA  
11477 C C   . MET B 337  ? 0.2923 0.2513 0.2168 -0.0585 -0.0101 0.0315  335  MET B C   
11478 O O   . MET B 337  ? 0.2908 0.2512 0.2163 -0.0621 -0.0095 0.0325  335  MET B O   
11479 C CB  . MET B 337  ? 0.3468 0.2894 0.2674 -0.0573 -0.0147 0.0322  335  MET B CB  
11480 C CG  . MET B 337  ? 0.3388 0.2826 0.2638 -0.0536 -0.0150 0.0287  335  MET B CG  
11481 S SD  . MET B 337  ? 0.4648 0.4065 0.3891 -0.0484 -0.0162 0.0274  335  MET B SD  
11482 C CE  . MET B 337  ? 0.3959 0.3473 0.3246 -0.0460 -0.0140 0.0246  335  MET B CE  
11483 N N   . GLY B 338  ? 0.2623 0.2269 0.1895 -0.0552 -0.0088 0.0291  336  GLY B N   
11484 C CA  . GLY B 338  ? 0.2795 0.2526 0.2110 -0.0554 -0.0066 0.0277  336  GLY B CA  
11485 C C   . GLY B 338  ? 0.2577 0.2316 0.1935 -0.0522 -0.0071 0.0245  336  GLY B C   
11486 O O   . GLY B 338  ? 0.2623 0.2324 0.1979 -0.0488 -0.0085 0.0230  336  GLY B O   
11487 N N   . PHE B 339  ? 0.2457 0.2248 0.1855 -0.0533 -0.0060 0.0235  337  PHE B N   
11488 C CA  . PHE B 339  ? 0.2436 0.2233 0.1874 -0.0507 -0.0064 0.0207  337  PHE B CA  
11489 C C   . PHE B 339  ? 0.2246 0.2132 0.1725 -0.0510 -0.0043 0.0197  337  PHE B C   
11490 O O   . PHE B 339  ? 0.2499 0.2419 0.1985 -0.0546 -0.0034 0.0213  337  PHE B O   
11491 C CB  . PHE B 339  ? 0.2566 0.2297 0.2004 -0.0521 -0.0085 0.0206  337  PHE B CB  
11492 C CG  . PHE B 339  ? 0.2550 0.2271 0.2019 -0.0490 -0.0093 0.0178  337  PHE B CG  
11493 C CD1 . PHE B 339  ? 0.2830 0.2499 0.2290 -0.0456 -0.0107 0.0166  337  PHE B CD1 
11494 C CD2 . PHE B 339  ? 0.2446 0.2209 0.1953 -0.0496 -0.0087 0.0164  337  PHE B CD2 
11495 C CE1 . PHE B 339  ? 0.2915 0.2577 0.2405 -0.0428 -0.0114 0.0141  337  PHE B CE1 
11496 C CE2 . PHE B 339  ? 0.2779 0.2531 0.2312 -0.0468 -0.0094 0.0139  337  PHE B CE2 
11497 C CZ  . PHE B 339  ? 0.2896 0.2598 0.2421 -0.0435 -0.0106 0.0127  337  PHE B CZ  
11498 N N   . VAL B 340  ? 0.2278 0.2200 0.1784 -0.0475 -0.0036 0.0174  338  VAL B N   
11499 C CA  . VAL B 340  ? 0.2161 0.2167 0.1708 -0.0471 -0.0016 0.0163  338  VAL B CA  
11500 C C   . VAL B 340  ? 0.2327 0.2332 0.1909 -0.0474 -0.0024 0.0149  338  VAL B C   
11501 O O   . VAL B 340  ? 0.2175 0.2127 0.1758 -0.0455 -0.0041 0.0134  338  VAL B O   
11502 C CB  . VAL B 340  ? 0.2190 0.2232 0.1746 -0.0431 -0.0005 0.0144  338  VAL B CB  
11503 C CG1 . VAL B 340  ? 0.2427 0.2551 0.2025 -0.0424 0.0015  0.0133  338  VAL B CG1 
11504 C CG2 . VAL B 340  ? 0.2293 0.2333 0.1809 -0.0428 0.0003  0.0157  338  VAL B CG2 
11505 N N   . VAL B 341  ? 0.2142 0.2208 0.1753 -0.0495 -0.0013 0.0153  339  VAL B N   
11506 C CA  A VAL B 341  ? 0.2226 0.2307 0.1874 -0.0494 -0.0018 0.0138  339  VAL B CA  
11507 C CA  B VAL B 341  ? 0.2226 0.2306 0.1874 -0.0494 -0.0018 0.0138  339  VAL B CA  
11508 C C   . VAL B 341  ? 0.2029 0.2200 0.1717 -0.0480 0.0002  0.0128  339  VAL B C   
11509 O O   . VAL B 341  ? 0.2170 0.2402 0.1862 -0.0493 0.0021  0.0142  339  VAL B O   
11510 C CB  A VAL B 341  ? 0.2317 0.2375 0.1962 -0.0538 -0.0030 0.0152  339  VAL B CB  
11511 C CB  B VAL B 341  ? 0.2318 0.2377 0.1964 -0.0538 -0.0029 0.0152  339  VAL B CB  
11512 C CG1 A VAL B 341  ? 0.2559 0.2519 0.2165 -0.0545 -0.0051 0.0158  339  VAL B CG1 
11513 C CG1 B VAL B 341  ? 0.2201 0.2247 0.1872 -0.0532 -0.0042 0.0133  339  VAL B CG1 
11514 C CG2 A VAL B 341  ? 0.2742 0.2855 0.2388 -0.0575 -0.0015 0.0177  339  VAL B CG2 
11515 C CG2 B VAL B 341  ? 0.2624 0.2601 0.2223 -0.0557 -0.0045 0.0169  339  VAL B CG2 
11516 N N   . GLN B 342  ? 0.1979 0.2160 0.1695 -0.0452 -0.0001 0.0106  340  GLN B N   
11517 C CA  . GLN B 342  ? 0.2135 0.2393 0.1888 -0.0431 0.0017  0.0094  340  GLN B CA  
11518 C C   . GLN B 342  ? 0.2045 0.2350 0.1835 -0.0451 0.0017  0.0095  340  GLN B C   
11519 O O   . GLN B 342  ? 0.2017 0.2294 0.1818 -0.0450 0.0002  0.0083  340  GLN B O   
11520 C CB  . GLN B 342  ? 0.1804 0.2043 0.1565 -0.0387 0.0013  0.0070  340  GLN B CB  
11521 C CG  . GLN B 342  ? 0.1873 0.2073 0.1601 -0.0366 0.0012  0.0068  340  GLN B CG  
11522 C CD  . GLN B 342  ? 0.1855 0.2003 0.1583 -0.0335 -0.0002 0.0048  340  GLN B CD  
11523 O OE1 . GLN B 342  ? 0.1997 0.2102 0.1728 -0.0340 -0.0018 0.0043  340  GLN B OE1 
11524 N NE2 . GLN B 342  ? 0.1893 0.2046 0.1617 -0.0304 0.0003  0.0037  340  GLN B NE2 
11525 N N   . ALA B 343  ? 0.1979 0.2360 0.1789 -0.0468 0.0034  0.0108  341  ALA B N   
11526 C CA  . ALA B 343  ? 0.1820 0.2254 0.1666 -0.0491 0.0034  0.0112  341  ALA B CA  
11527 C C   . ALA B 343  ? 0.1934 0.2405 0.1818 -0.0459 0.0036  0.0092  341  ALA B C   
11528 O O   . ALA B 343  ? 0.2034 0.2536 0.1947 -0.0475 0.0030  0.0092  341  ALA B O   
11529 C CB  . ALA B 343  ? 0.2029 0.2537 0.1887 -0.0517 0.0053  0.0134  341  ALA B CB  
11530 N N   . TYR B 344  ? 0.1980 0.2449 0.1864 -0.0417 0.0043  0.0075  342  TYR B N   
11531 C CA  . TYR B 344  ? 0.1850 0.2341 0.1766 -0.0389 0.0042  0.0056  342  TYR B CA  
11532 C C   . TYR B 344  ? 0.1992 0.2419 0.1902 -0.0388 0.0019  0.0043  342  TYR B C   
11533 O O   . TYR B 344  ? 0.1977 0.2417 0.1911 -0.0369 0.0016  0.0029  342  TYR B O   
11534 C CB  . TYR B 344  ? 0.1944 0.2456 0.1865 -0.0346 0.0056  0.0041  342  TYR B CB  
11535 C CG  . TYR B 344  ? 0.1919 0.2364 0.1810 -0.0319 0.0050  0.0028  342  TYR B CG  
11536 C CD1 . TYR B 344  ? 0.1850 0.2218 0.1709 -0.0330 0.0032  0.0030  342  TYR B CD1 
11537 C CD2 . TYR B 344  ? 0.1886 0.2347 0.1782 -0.0282 0.0061  0.0014  342  TYR B CD2 
11538 C CE1 . TYR B 344  ? 0.1832 0.2147 0.1670 -0.0304 0.0026  0.0019  342  TYR B CE1 
11539 C CE2 . TYR B 344  ? 0.1926 0.2332 0.1798 -0.0259 0.0054  0.0003  342  TYR B CE2 
11540 C CZ  . TYR B 344  ? 0.1914 0.2250 0.1758 -0.0270 0.0037  0.0006  342  TYR B CZ  
11541 O OH  . TYR B 344  ? 0.1841 0.2130 0.1665 -0.0246 0.0030  -0.0005 342  TYR B OH  
11542 N N   . GLY B 345  ? 0.1968 0.2324 0.1844 -0.0408 0.0005  0.0049  343  GLY B N   
11543 C CA  . GLY B 345  ? 0.1950 0.2240 0.1816 -0.0404 -0.0015 0.0036  343  GLY B CA  
11544 C C   . GLY B 345  ? 0.2005 0.2292 0.1876 -0.0441 -0.0028 0.0043  343  GLY B C   
11545 O O   . GLY B 345  ? 0.2068 0.2367 0.1933 -0.0477 -0.0027 0.0062  343  GLY B O   
11546 N N   . LYS B 346  ? 0.1944 0.2211 0.1825 -0.0432 -0.0040 0.0028  344  LYS B N   
11547 C CA  . LYS B 346  ? 0.2014 0.2275 0.1899 -0.0466 -0.0054 0.0031  344  LYS B CA  
11548 C C   . LYS B 346  ? 0.1995 0.2180 0.1841 -0.0495 -0.0069 0.0039  344  LYS B C   
11549 O O   . LYS B 346  ? 0.2143 0.2324 0.1986 -0.0532 -0.0080 0.0047  344  LYS B O   
11550 C CB  . LYS B 346  ? 0.2084 0.2336 0.1981 -0.0445 -0.0063 0.0011  344  LYS B CB  
11551 C CG  . LYS B 346  ? 0.2131 0.2458 0.2067 -0.0420 -0.0050 0.0004  344  LYS B CG  
11552 C CD  . LYS B 346  ? 0.2139 0.2454 0.2084 -0.0399 -0.0059 -0.0014 344  LYS B CD  
11553 C CE  . LYS B 346  ? 0.2093 0.2485 0.2077 -0.0377 -0.0047 -0.0018 344  LYS B CE  
11554 N NZ  . LYS B 346  ? 0.2018 0.2394 0.2008 -0.0352 -0.0054 -0.0035 344  LYS B NZ  
11555 N N   . ARG B 347  ? 0.2033 0.2154 0.1848 -0.0480 -0.0072 0.0038  345  ARG B N   
11556 C CA  . ARG B 347  ? 0.2258 0.2301 0.2035 -0.0504 -0.0087 0.0046  345  ARG B CA  
11557 C C   . ARG B 347  ? 0.2158 0.2209 0.1919 -0.0535 -0.0082 0.0070  345  ARG B C   
11558 O O   . ARG B 347  ? 0.2319 0.2307 0.2048 -0.0562 -0.0094 0.0081  345  ARG B O   
11559 C CB  . ARG B 347  ? 0.2191 0.2160 0.1943 -0.0472 -0.0094 0.0033  345  ARG B CB  
11560 C CG  . ARG B 347  ? 0.2043 0.1993 0.1806 -0.0447 -0.0101 0.0010  345  ARG B CG  
11561 C CD  . ARG B 347  ? 0.2263 0.2165 0.2013 -0.0409 -0.0102 -0.0002 345  ARG B CD  
11562 N NE  . ARG B 347  ? 0.1975 0.1926 0.1745 -0.0380 -0.0087 -0.0004 345  ARG B NE  
11563 C CZ  . ARG B 347  ? 0.2182 0.2103 0.1943 -0.0349 -0.0087 -0.0011 345  ARG B CZ  
11564 N NH1 . ARG B 347  ? 0.2117 0.1965 0.1855 -0.0341 -0.0100 -0.0015 345  ARG B NH1 
11565 N NH2 . ARG B 347  ? 0.2027 0.1992 0.1804 -0.0326 -0.0074 -0.0013 345  ARG B NH2 
11566 N N   . CYS B 348  ? 0.2184 0.2309 0.1965 -0.0533 -0.0063 0.0080  346  CYS B N   
11567 C CA  . CYS B 348  ? 0.2248 0.2385 0.2013 -0.0557 -0.0054 0.0104  346  CYS B CA  
11568 C C   . CYS B 348  ? 0.2322 0.2429 0.2067 -0.0607 -0.0066 0.0123  346  CYS B C   
11569 O O   . CYS B 348  ? 0.2537 0.2584 0.2245 -0.0621 -0.0072 0.0136  346  CYS B O   
11570 C CB  . CYS B 348  ? 0.2056 0.2287 0.1850 -0.0549 -0.0030 0.0110  346  CYS B CB  
11571 S SG  . CYS B 348  ? 0.2817 0.3060 0.2584 -0.0567 -0.0016 0.0136  346  CYS B SG  
11572 N N   . PRO B 349  ? 0.2312 0.2457 0.2081 -0.0638 -0.0070 0.0126  347  PRO B N   
11573 C CA  . PRO B 349  ? 0.2497 0.2612 0.2247 -0.0690 -0.0082 0.0146  347  PRO B CA  
11574 C C   . PRO B 349  ? 0.2328 0.2331 0.2035 -0.0696 -0.0105 0.0140  347  PRO B C   
11575 O O   . PRO B 349  ? 0.2445 0.2398 0.2120 -0.0728 -0.0113 0.0158  347  PRO B O   
11576 C CB  . PRO B 349  ? 0.2878 0.3060 0.2665 -0.0715 -0.0085 0.0146  347  PRO B CB  
11577 C CG  . PRO B 349  ? 0.2602 0.2817 0.2419 -0.0675 -0.0081 0.0123  347  PRO B CG  
11578 C CD  . PRO B 349  ? 0.2376 0.2591 0.2189 -0.0628 -0.0067 0.0114  347  PRO B CD  
11579 N N   . PHE B 350  ? 0.2395 0.2357 0.2101 -0.0663 -0.0114 0.0115  348  PHE B N   
11580 C CA  . PHE B 350  ? 0.2504 0.2360 0.2170 -0.0662 -0.0134 0.0107  348  PHE B CA  
11581 C C   . PHE B 350  ? 0.2444 0.2243 0.2078 -0.0642 -0.0133 0.0113  348  PHE B C   
11582 O O   . PHE B 350  ? 0.2657 0.2374 0.2252 -0.0659 -0.0147 0.0121  348  PHE B O   
11583 C CB  . PHE B 350  ? 0.2382 0.2221 0.2059 -0.0633 -0.0142 0.0079  348  PHE B CB  
11584 C CG  . PHE B 350  ? 0.2499 0.2402 0.2209 -0.0651 -0.0142 0.0074  348  PHE B CG  
11585 C CD1 . PHE B 350  ? 0.2878 0.2758 0.2576 -0.0695 -0.0158 0.0080  348  PHE B CD1 
11586 C CD2 . PHE B 350  ? 0.2467 0.2455 0.2218 -0.0626 -0.0128 0.0066  348  PHE B CD2 
11587 C CE1 . PHE B 350  ? 0.3032 0.2977 0.2762 -0.0713 -0.0161 0.0077  348  PHE B CE1 
11588 C CE2 . PHE B 350  ? 0.2693 0.2743 0.2476 -0.0642 -0.0129 0.0064  348  PHE B CE2 
11589 C CZ  . PHE B 350  ? 0.2801 0.2832 0.2574 -0.0686 -0.0146 0.0069  348  PHE B CZ  
11590 N N   . VAL B 351  ? 0.2398 0.2240 0.2046 -0.0608 -0.0117 0.0111  349  VAL B N   
11591 C CA  . VAL B 351  ? 0.2445 0.2243 0.2063 -0.0592 -0.0116 0.0119  349  VAL B CA  
11592 C C   . VAL B 351  ? 0.2476 0.2268 0.2069 -0.0632 -0.0114 0.0149  349  VAL B C   
11593 O O   . VAL B 351  ? 0.2545 0.2264 0.2100 -0.0638 -0.0125 0.0160  349  VAL B O   
11594 C CB  . VAL B 351  ? 0.2242 0.2093 0.1880 -0.0551 -0.0099 0.0110  349  VAL B CB  
11595 C CG1 . VAL B 351  ? 0.2587 0.2397 0.2192 -0.0538 -0.0099 0.0121  349  VAL B CG1 
11596 C CG2 . VAL B 351  ? 0.2410 0.2256 0.2068 -0.0512 -0.0102 0.0083  349  VAL B CG2 
11597 N N   . LEU B 352  ? 0.2366 0.2237 0.1983 -0.0660 -0.0101 0.0162  350  LEU B N   
11598 C CA  . LEU B 352  ? 0.2496 0.2369 0.2092 -0.0702 -0.0098 0.0192  350  LEU B CA  
11599 C C   . LEU B 352  ? 0.2565 0.2357 0.2130 -0.0740 -0.0120 0.0202  350  LEU B C   
11600 O O   . LEU B 352  ? 0.2739 0.2476 0.2267 -0.0760 -0.0125 0.0222  350  LEU B O   
11601 C CB  . LEU B 352  ? 0.2507 0.2486 0.2140 -0.0724 -0.0079 0.0204  350  LEU B CB  
11602 C CG  . LEU B 352  ? 0.2609 0.2664 0.2263 -0.0691 -0.0055 0.0200  350  LEU B CG  
11603 C CD1 . LEU B 352  ? 0.2679 0.2838 0.2373 -0.0712 -0.0037 0.0211  350  LEU B CD1 
11604 C CD2 . LEU B 352  ? 0.2912 0.2939 0.2529 -0.0686 -0.0048 0.0216  350  LEU B CD2 
11605 N N   . ASP B 353  ? 0.2612 0.2392 0.2191 -0.0751 -0.0132 0.0187  351  ASP B N   
11606 C CA  . ASP B 353  ? 0.2791 0.2486 0.2337 -0.0786 -0.0155 0.0193  351  ASP B CA  
11607 C C   . ASP B 353  ? 0.2606 0.2195 0.2108 -0.0762 -0.0168 0.0189  351  ASP B C   
11608 O O   . ASP B 353  ? 0.2950 0.2467 0.2413 -0.0790 -0.0180 0.0206  351  ASP B O   
11609 C CB  . ASP B 353  ? 0.2758 0.2449 0.2320 -0.0791 -0.0167 0.0171  351  ASP B CB  
11610 C CG  . ASP B 353  ? 0.3330 0.3115 0.2933 -0.0823 -0.0160 0.0178  351  ASP B CG  
11611 O OD1 . ASP B 353  ? 0.3389 0.3225 0.3000 -0.0856 -0.0150 0.0203  351  ASP B OD1 
11612 O OD2 . ASP B 353  ? 0.3449 0.3258 0.3076 -0.0814 -0.0165 0.0158  351  ASP B OD2 
11613 N N   . PHE B 354  ? 0.2732 0.2312 0.2242 -0.0711 -0.0166 0.0167  352  PHE B N   
11614 C CA  . PHE B 354  ? 0.2759 0.2247 0.2233 -0.0683 -0.0177 0.0162  352  PHE B CA  
11615 C C   . PHE B 354  ? 0.2807 0.2280 0.2253 -0.0689 -0.0173 0.0188  352  PHE B C   
11616 O O   . PHE B 354  ? 0.2861 0.2247 0.2267 -0.0697 -0.0188 0.0199  352  PHE B O   
11617 C CB  . PHE B 354  ? 0.2806 0.2304 0.2300 -0.0628 -0.0173 0.0136  352  PHE B CB  
11618 C CG  . PHE B 354  ? 0.2743 0.2168 0.2208 -0.0596 -0.0182 0.0134  352  PHE B CG  
11619 C CD1 . PHE B 354  ? 0.2939 0.2271 0.2378 -0.0589 -0.0200 0.0125  352  PHE B CD1 
11620 C CD2 . PHE B 354  ? 0.2829 0.2276 0.2291 -0.0574 -0.0172 0.0144  352  PHE B CD2 
11621 C CE1 . PHE B 354  ? 0.2947 0.2215 0.2362 -0.0558 -0.0208 0.0125  352  PHE B CE1 
11622 C CE2 . PHE B 354  ? 0.3124 0.2506 0.2562 -0.0546 -0.0182 0.0144  352  PHE B CE2 
11623 C CZ  . PHE B 354  ? 0.2937 0.2231 0.2352 -0.0537 -0.0200 0.0136  352  PHE B CZ  
11624 N N   . ILE B 355  ? 0.2683 0.2237 0.2149 -0.0684 -0.0153 0.0197  353  ILE B N   
11625 C CA  . ILE B 355  ? 0.2744 0.2288 0.2181 -0.0688 -0.0148 0.0221  353  ILE B CA  
11626 C C   . ILE B 355  ? 0.2722 0.2241 0.2132 -0.0742 -0.0153 0.0251  353  ILE B C   
11627 O O   . ILE B 355  ? 0.2840 0.2294 0.2208 -0.0750 -0.0162 0.0270  353  ILE B O   
11628 C CB  . ILE B 355  ? 0.2808 0.2447 0.2271 -0.0669 -0.0124 0.0221  353  ILE B CB  
11629 C CG1 . ILE B 355  ? 0.2949 0.2599 0.2432 -0.0615 -0.0122 0.0194  353  ILE B CG1 
11630 C CG2 . ILE B 355  ? 0.2910 0.2549 0.2341 -0.0681 -0.0117 0.0248  353  ILE B CG2 
11631 C CD1 . ILE B 355  ? 0.3099 0.2841 0.2609 -0.0596 -0.0099 0.0190  353  ILE B CD1 
11632 N N   . ILE B 356  ? 0.2804 0.2375 0.2236 -0.0780 -0.0148 0.0257  354  ILE B N   
11633 C CA  . ILE B 356  ? 0.3111 0.2662 0.2520 -0.0836 -0.0153 0.0286  354  ILE B CA  
11634 C C   . ILE B 356  ? 0.3015 0.2446 0.2381 -0.0850 -0.0179 0.0288  354  ILE B C   
11635 O O   . ILE B 356  ? 0.3110 0.2485 0.2437 -0.0877 -0.0186 0.0314  354  ILE B O   
11636 C CB  . ILE B 356  ? 0.3029 0.2663 0.2476 -0.0873 -0.0144 0.0290  354  ILE B CB  
11637 C CG1 . ILE B 356  ? 0.3167 0.2916 0.2648 -0.0865 -0.0116 0.0297  354  ILE B CG1 
11638 C CG2 . ILE B 356  ? 0.3154 0.2750 0.2577 -0.0934 -0.0156 0.0316  354  ILE B CG2 
11639 C CD1 . ILE B 356  ? 0.2918 0.2762 0.2450 -0.0883 -0.0107 0.0291  354  ILE B CD1 
11640 N N   . ASP B 357  ? 0.3055 0.2445 0.2428 -0.0831 -0.0192 0.0261  355  ASP B N   
11641 C CA  . ASP B 357  ? 0.3139 0.2411 0.2470 -0.0838 -0.0216 0.0259  355  ASP B CA  
11642 C C   . ASP B 357  ? 0.2966 0.2167 0.2262 -0.0805 -0.0223 0.0264  355  ASP B C   
11643 O O   . ASP B 357  ? 0.3090 0.2203 0.2343 -0.0825 -0.0238 0.0282  355  ASP B O   
11644 C CB  . ASP B 357  ? 0.3254 0.2503 0.2600 -0.0821 -0.0227 0.0227  355  ASP B CB  
11645 C CG  . ASP B 357  ? 0.3333 0.2456 0.2634 -0.0817 -0.0250 0.0221  355  ASP B CG  
11646 O OD1 . ASP B 357  ? 0.3755 0.2822 0.3028 -0.0862 -0.0265 0.0233  355  ASP B OD1 
11647 O OD2 . ASP B 357  ? 0.3278 0.2358 0.2572 -0.0769 -0.0254 0.0204  355  ASP B OD2 
11648 N N   . LEU B 358  ? 0.3035 0.2269 0.2349 -0.0755 -0.0213 0.0250  356  LEU B N   
11649 C CA  . LEU B 358  ? 0.2992 0.2168 0.2276 -0.0723 -0.0219 0.0256  356  LEU B CA  
11650 C C   . LEU B 358  ? 0.2856 0.2024 0.2108 -0.0752 -0.0217 0.0291  356  LEU B C   
11651 O O   . LEU B 358  ? 0.3105 0.2187 0.2314 -0.0753 -0.0232 0.0306  356  LEU B O   
11652 C CB  . LEU B 358  ? 0.2741 0.1972 0.2054 -0.0671 -0.0207 0.0237  356  LEU B CB  
11653 C CG  . LEU B 358  ? 0.2730 0.1919 0.2020 -0.0634 -0.0213 0.0242  356  LEU B CG  
11654 C CD1 . LEU B 358  ? 0.3176 0.2257 0.2437 -0.0619 -0.0235 0.0237  356  LEU B CD1 
11655 C CD2 . LEU B 358  ? 0.3013 0.2266 0.2338 -0.0588 -0.0200 0.0220  356  LEU B CD2 
11656 N N   . ALA B 359  ? 0.2954 0.2212 0.2225 -0.0777 -0.0197 0.0306  357  ALA B N   
11657 C CA  . ALA B 359  ? 0.2886 0.2143 0.2125 -0.0807 -0.0192 0.0340  357  ALA B CA  
11658 C C   . ALA B 359  ? 0.3295 0.2471 0.2497 -0.0855 -0.0210 0.0362  357  ALA B C   
11659 O O   . ALA B 359  ? 0.3338 0.2446 0.2495 -0.0863 -0.0220 0.0385  357  ALA B O   
11660 C CB  . ALA B 359  ? 0.3248 0.2622 0.2519 -0.0827 -0.0166 0.0350  357  ALA B CB  
11661 N N   . ARG B 360  ? 0.3238 0.2416 0.2457 -0.0887 -0.0215 0.0355  358  ARG B N   
11662 C CA  A ARG B 360  ? 0.3537 0.2638 0.2720 -0.0936 -0.0232 0.0375  358  ARG B CA  
11663 C CA  B ARG B 360  ? 0.3536 0.2638 0.2720 -0.0937 -0.0232 0.0375  358  ARG B CA  
11664 C C   . ARG B 360  ? 0.3375 0.2347 0.2514 -0.0917 -0.0257 0.0371  358  ARG B C   
11665 O O   . ARG B 360  ? 0.3640 0.2537 0.2734 -0.0944 -0.0269 0.0397  358  ARG B O   
11666 C CB  A ARG B 360  ? 0.3590 0.2720 0.2802 -0.0969 -0.0236 0.0362  358  ARG B CB  
11667 C CB  B ARG B 360  ? 0.3590 0.2719 0.2801 -0.0970 -0.0236 0.0363  358  ARG B CB  
11668 C CG  A ARG B 360  ? 0.4115 0.3350 0.3358 -0.1012 -0.0217 0.0381  358  ARG B CG  
11669 C CG  B ARG B 360  ? 0.4382 0.3593 0.3612 -0.1024 -0.0222 0.0387  358  ARG B CG  
11670 C CD  A ARG B 360  ? 0.4060 0.3339 0.3339 -0.1035 -0.0220 0.0364  358  ARG B CD  
11671 C CD  B ARG B 360  ? 0.4020 0.3234 0.3268 -0.1064 -0.0233 0.0379  358  ARG B CD  
11672 N NE  A ARG B 360  ? 0.4037 0.3413 0.3345 -0.1081 -0.0204 0.0387  358  ARG B NE  
11673 N NE  B ARG B 360  ? 0.4265 0.3585 0.3570 -0.1050 -0.0219 0.0358  358  ARG B NE  
11674 C CZ  A ARG B 360  ? 0.4290 0.3754 0.3646 -0.1094 -0.0197 0.0376  358  ARG B CZ  
11675 C CZ  B ARG B 360  ? 0.4196 0.3625 0.3539 -0.1079 -0.0201 0.0371  358  ARG B CZ  
11676 N NH1 A ARG B 360  ? 0.4893 0.4359 0.4272 -0.1066 -0.0204 0.0343  358  ARG B NH1 
11677 N NH1 B ARG B 360  ? 0.5056 0.4509 0.4388 -0.1123 -0.0193 0.0406  358  ARG B NH1 
11678 N NH2 A ARG B 360  ? 0.4808 0.4360 0.4190 -0.1135 -0.0182 0.0400  358  ARG B NH2 
11679 N NH2 B ARG B 360  ? 0.4946 0.4463 0.4340 -0.1062 -0.0190 0.0350  358  ARG B NH2 
11680 N N   . ARG B 361  ? 0.3513 0.2457 0.2664 -0.0869 -0.0264 0.0339  359  ARG B N   
11681 C CA  . ARG B 361  ? 0.3785 0.2607 0.2895 -0.0850 -0.0286 0.0334  359  ARG B CA  
11682 C C   . ARG B 361  ? 0.3255 0.2040 0.2340 -0.0815 -0.0289 0.0347  359  ARG B C   
11683 O O   . ARG B 361  ? 0.3760 0.2440 0.2804 -0.0808 -0.0308 0.0354  359  ARG B O   
11684 C CB  . ARG B 361  ? 0.4262 0.3061 0.3391 -0.0816 -0.0294 0.0296  359  ARG B CB  
11685 C CG  . ARG B 361  ? 0.3781 0.2644 0.2948 -0.0761 -0.0280 0.0272  359  ARG B CG  
11686 C CD  . ARG B 361  ? 0.3506 0.2353 0.2692 -0.0737 -0.0286 0.0236  359  ARG B CD  
11687 N NE  . ARG B 361  ? 0.3218 0.2156 0.2451 -0.0701 -0.0269 0.0214  359  ARG B NE  
11688 C CZ  . ARG B 361  ? 0.3039 0.1978 0.2284 -0.0648 -0.0267 0.0198  359  ARG B CZ  
11689 N NH1 . ARG B 361  ? 0.3559 0.2419 0.2774 -0.0622 -0.0279 0.0203  359  ARG B NH1 
11690 N NH2 . ARG B 361  ? 0.3246 0.2269 0.2534 -0.0621 -0.0251 0.0179  359  ARG B NH2 
11691 N N   . SER B 362  ? 0.3344 0.2211 0.2450 -0.0793 -0.0272 0.0350  360  SER B N   
11692 C CA  . SER B 362  ? 0.3408 0.2247 0.2490 -0.0759 -0.0275 0.0361  360  SER B CA  
11693 C C   . SER B 362  ? 0.3355 0.2196 0.2403 -0.0793 -0.0271 0.0400  360  SER B C   
11694 O O   . SER B 362  ? 0.3621 0.2427 0.2641 -0.0771 -0.0278 0.0414  360  SER B O   
11695 C CB  . SER B 362  ? 0.3558 0.2475 0.2678 -0.0710 -0.0261 0.0339  360  SER B CB  
11696 O OG  . SER B 362  ? 0.3457 0.2481 0.2603 -0.0728 -0.0238 0.0346  360  SER B OG  
11697 N N   . GLY B 363  ? 0.3373 0.2256 0.2423 -0.0846 -0.0261 0.0419  361  GLY B N   
11698 C CA  . GLY B 363  ? 0.3704 0.2596 0.2722 -0.0879 -0.0254 0.0457  361  GLY B CA  
11699 C C   . GLY B 363  ? 0.3721 0.2698 0.2752 -0.0854 -0.0234 0.0460  361  GLY B C   
11700 O O   . GLY B 363  ? 0.4050 0.3008 0.3044 -0.0855 -0.0235 0.0485  361  GLY B O   
11701 N N   . ARG B 364  ? 0.3452 0.2520 0.2532 -0.0829 -0.0217 0.0433  362  ARG B N   
11702 C CA  . ARG B 364  ? 0.3654 0.2804 0.2747 -0.0803 -0.0197 0.0431  362  ARG B CA  
11703 C C   . ARG B 364  ? 0.3513 0.2771 0.2647 -0.0827 -0.0172 0.0427  362  ARG B C   
11704 O O   . ARG B 364  ? 0.3602 0.2888 0.2775 -0.0828 -0.0171 0.0405  362  ARG B O   
11705 C CB  . ARG B 364  ? 0.3624 0.2781 0.2743 -0.0743 -0.0200 0.0397  362  ARG B CB  
11706 C CG  . ARG B 364  ? 0.3408 0.2469 0.2497 -0.0710 -0.0224 0.0395  362  ARG B CG  
11707 C CD  . ARG B 364  ? 0.3360 0.2407 0.2410 -0.0702 -0.0226 0.0420  362  ARG B CD  
11708 N NE  . ARG B 364  ? 0.3625 0.2576 0.2646 -0.0672 -0.0251 0.0421  362  ARG B NE  
11709 C CZ  . ARG B 364  ? 0.3430 0.2376 0.2468 -0.0621 -0.0259 0.0399  362  ARG B CZ  
11710 N NH1 . ARG B 364  ? 0.3338 0.2364 0.2417 -0.0594 -0.0244 0.0374  362  ARG B NH1 
11711 N NH2 . ARG B 364  ? 0.3768 0.2627 0.2782 -0.0597 -0.0282 0.0403  362  ARG B NH2 
11712 N N   . ARG B 365  ? 0.3500 0.2823 0.2627 -0.0844 -0.0152 0.0448  363  ARG B N   
11713 C CA  . ARG B 365  ? 0.3231 0.2669 0.2404 -0.0850 -0.0126 0.0439  363  ARG B CA  
11714 C C   . ARG B 365  ? 0.3304 0.2786 0.2502 -0.0794 -0.0118 0.0410  363  ARG B C   
11715 O O   . ARG B 365  ? 0.3423 0.2885 0.2594 -0.0766 -0.0120 0.0412  363  ARG B O   
11716 C CB  . ARG B 365  ? 0.3349 0.2844 0.2505 -0.0886 -0.0105 0.0471  363  ARG B CB  
11717 C CG  . ARG B 365  ? 0.3365 0.2973 0.2570 -0.0904 -0.0080 0.0466  363  ARG B CG  
11718 C CD  . ARG B 365  ? 0.3787 0.3446 0.2975 -0.0946 -0.0060 0.0502  363  ARG B CD  
11719 N NE  . ARG B 365  ? 0.3805 0.3572 0.3043 -0.0968 -0.0037 0.0500  363  ARG B NE  
11720 C CZ  . ARG B 365  ? 0.3608 0.3469 0.2857 -0.0971 -0.0007 0.0511  363  ARG B CZ  
11721 N NH1 . ARG B 365  ? 0.3473 0.3335 0.2683 -0.0956 0.0004  0.0523  363  ARG B NH1 
11722 N NH2 . ARG B 365  ? 0.3233 0.3189 0.2531 -0.0989 0.0011  0.0509  363  ARG B NH2 
11723 N N   . ILE B 366  ? 0.2998 0.2531 0.2244 -0.0779 -0.0111 0.0382  364  ILE B N   
11724 C CA  . ILE B 366  ? 0.3065 0.2639 0.2338 -0.0728 -0.0104 0.0353  364  ILE B CA  
11725 C C   . ILE B 366  ? 0.2950 0.2636 0.2253 -0.0731 -0.0075 0.0352  364  ILE B C   
11726 O O   . ILE B 366  ? 0.2897 0.2637 0.2227 -0.0763 -0.0063 0.0359  364  ILE B O   
11727 C CB  . ILE B 366  ? 0.2907 0.2459 0.2213 -0.0705 -0.0117 0.0322  364  ILE B CB  
11728 C CG1 . ILE B 366  ? 0.3066 0.2506 0.2340 -0.0698 -0.0144 0.0323  364  ILE B CG1 
11729 C CG2 . ILE B 366  ? 0.2673 0.2276 0.2011 -0.0656 -0.0107 0.0293  364  ILE B CG2 
11730 C CD1 . ILE B 366  ? 0.3281 0.2690 0.2580 -0.0682 -0.0157 0.0295  364  ILE B CD1 
11731 N N   . MET B 367  ? 0.2866 0.2585 0.2162 -0.0698 -0.0062 0.0346  365  MET B N   
11732 C CA  . MET B 367  ? 0.2940 0.2762 0.2263 -0.0693 -0.0034 0.0342  365  MET B CA  
11733 C C   . MET B 367  ? 0.3001 0.2863 0.2375 -0.0662 -0.0031 0.0309  365  MET B C   
11734 O O   . MET B 367  ? 0.2971 0.2796 0.2348 -0.0624 -0.0044 0.0287  365  MET B O   
11735 C CB  . MET B 367  ? 0.2857 0.2690 0.2148 -0.0670 -0.0024 0.0347  365  MET B CB  
11736 C CG  . MET B 367  ? 0.2840 0.2614 0.2074 -0.0694 -0.0033 0.0378  365  MET B CG  
11737 S SD  . MET B 367  ? 0.3200 0.2993 0.2391 -0.0670 -0.0021 0.0384  365  MET B SD  
11738 C CE  . MET B 367  ? 0.4069 0.3958 0.3259 -0.0702 0.0015  0.0406  365  MET B CE  
11739 N N   . VAL B 368  ? 0.2485 0.2421 0.1900 -0.0679 -0.0016 0.0306  366  VAL B N   
11740 C CA  . VAL B 368  ? 0.2476 0.2447 0.1939 -0.0653 -0.0015 0.0276  366  VAL B CA  
11741 C C   . VAL B 368  ? 0.2709 0.2779 0.2201 -0.0637 0.0012  0.0269  366  VAL B C   
11742 O O   . VAL B 368  ? 0.2582 0.2719 0.2090 -0.0664 0.0030  0.0284  366  VAL B O   
11743 C CB  . VAL B 368  ? 0.2723 0.2691 0.2212 -0.0684 -0.0025 0.0276  366  VAL B CB  
11744 C CG1 . VAL B 368  ? 0.2581 0.2589 0.2117 -0.0655 -0.0023 0.0247  366  VAL B CG1 
11745 C CG2 . VAL B 368  ? 0.2982 0.2843 0.2439 -0.0698 -0.0053 0.0281  366  VAL B CG2 
11746 N N   . ARG B 369  ? 0.2441 0.2520 0.1939 -0.0591 0.0016  0.0246  367  ARG B N   
11747 C CA  . ARG B 369  ? 0.2343 0.2509 0.1868 -0.0570 0.0041  0.0235  367  ARG B CA  
11748 C C   . ARG B 369  ? 0.2274 0.2481 0.1852 -0.0560 0.0042  0.0215  367  ARG B C   
11749 O O   . ARG B 369  ? 0.2381 0.2551 0.1970 -0.0533 0.0027  0.0193  367  ARG B O   
11750 C CB  . ARG B 369  ? 0.2367 0.2523 0.1872 -0.0528 0.0045  0.0220  367  ARG B CB  
11751 C CG  . ARG B 369  ? 0.2657 0.2899 0.2184 -0.0507 0.0072  0.0210  367  ARG B CG  
11752 C CD  . ARG B 369  ? 0.2496 0.2725 0.2013 -0.0463 0.0072  0.0187  367  ARG B CD  
11753 N NE  . ARG B 369  ? 0.2447 0.2630 0.1910 -0.0461 0.0067  0.0198  367  ARG B NE  
11754 C CZ  . ARG B 369  ? 0.2558 0.2696 0.2000 -0.0430 0.0054  0.0184  367  ARG B CZ  
11755 N NH1 . ARG B 369  ? 0.2443 0.2573 0.1914 -0.0399 0.0045  0.0158  367  ARG B NH1 
11756 N NH2 . ARG B 369  ? 0.2605 0.2705 0.1998 -0.0433 0.0048  0.0198  367  ARG B NH2 
11757 N N   . LEU B 370  ? 0.2285 0.2568 0.1896 -0.0581 0.0058  0.0223  368  LEU B N   
11758 C CA  . LEU B 370  ? 0.2213 0.2546 0.1875 -0.0570 0.0060  0.0205  368  LEU B CA  
11759 C C   . LEU B 370  ? 0.2152 0.2548 0.1833 -0.0531 0.0082  0.0189  368  LEU B C   
11760 O O   . LEU B 370  ? 0.2354 0.2808 0.2031 -0.0533 0.0105  0.0200  368  LEU B O   
11761 C CB  . LEU B 370  ? 0.2244 0.2630 0.1933 -0.0614 0.0066  0.0223  368  LEU B CB  
11762 C CG  . LEU B 370  ? 0.2305 0.2739 0.2046 -0.0606 0.0064  0.0207  368  LEU B CG  
11763 C CD1 . LEU B 370  ? 0.2573 0.2932 0.2311 -0.0599 0.0037  0.0191  368  LEU B CD1 
11764 C CD2 . LEU B 370  ? 0.2412 0.2910 0.2181 -0.0650 0.0071  0.0228  368  LEU B CD2 
11765 N N   . VAL B 371  ? 0.1982 0.2365 0.1680 -0.0494 0.0075  0.0163  369  VAL B N   
11766 C CA  . VAL B 371  ? 0.2171 0.2606 0.1889 -0.0455 0.0092  0.0145  369  VAL B CA  
11767 C C   . VAL B 371  ? 0.2161 0.2632 0.1928 -0.0445 0.0089  0.0130  369  VAL B C   
11768 O O   . VAL B 371  ? 0.2183 0.2626 0.1962 -0.0464 0.0071  0.0130  369  VAL B O   
11769 C CB  . VAL B 371  ? 0.2002 0.2384 0.1693 -0.0418 0.0085  0.0127  369  VAL B CB  
11770 C CG1 . VAL B 371  ? 0.2306 0.2646 0.1946 -0.0429 0.0083  0.0144  369  VAL B CG1 
11771 C CG2 . VAL B 371  ? 0.2234 0.2555 0.1933 -0.0404 0.0061  0.0111  369  VAL B CG2 
11772 N N   . LYS B 372  ? 0.1963 0.2492 0.1757 -0.0414 0.0106  0.0116  370  LYS B N   
11773 C CA  . LYS B 372  ? 0.2018 0.2569 0.1853 -0.0397 0.0101  0.0099  370  LYS B CA  
11774 C C   . LYS B 372  ? 0.2006 0.2491 0.1832 -0.0367 0.0083  0.0077  370  LYS B C   
11775 O O   . LYS B 372  ? 0.2232 0.2675 0.2063 -0.0375 0.0064  0.0072  370  LYS B O   
11776 C CB  . LYS B 372  ? 0.2166 0.2808 0.2037 -0.0378 0.0125  0.0095  370  LYS B CB  
11777 C CG  . LYS B 372  ? 0.2157 0.2866 0.2047 -0.0414 0.0137  0.0118  370  LYS B CG  
11778 C CD  . LYS B 372  ? 0.2296 0.3101 0.2223 -0.0397 0.0163  0.0117  370  LYS B CD  
11779 C CE  . LYS B 372  ? 0.2418 0.3288 0.2358 -0.0437 0.0176  0.0144  370  LYS B CE  
11780 N NZ  . LYS B 372  ? 0.2372 0.3340 0.2349 -0.0418 0.0203  0.0145  370  LYS B NZ  
11781 N N   . GLY B 373  ? 0.1984 0.2455 0.1792 -0.0334 0.0090  0.0064  371  GLY B N   
11782 C CA  . GLY B 373  ? 0.1937 0.2342 0.1733 -0.0310 0.0073  0.0047  371  GLY B CA  
11783 C C   . GLY B 373  ? 0.2073 0.2492 0.1872 -0.0269 0.0083  0.0028  371  GLY B C   
11784 O O   . GLY B 373  ? 0.2170 0.2650 0.1996 -0.0255 0.0099  0.0022  371  GLY B O   
11785 N N   . ALA B 374  ? 0.1838 0.2201 0.1611 -0.0251 0.0072  0.0018  372  ALA B N   
11786 C CA  . ALA B 374  ? 0.1995 0.2364 0.1760 -0.0217 0.0081  0.0003  372  ALA B CA  
11787 C C   . ALA B 374  ? 0.2056 0.2405 0.1843 -0.0188 0.0071  -0.0018 372  ALA B C   
11788 O O   . ALA B 374  ? 0.2412 0.2761 0.2193 -0.0161 0.0076  -0.0032 372  ALA B O   
11789 C CB  . ALA B 374  ? 0.2308 0.2632 0.2027 -0.0215 0.0076  0.0007  372  ALA B CB  
11790 N N   . TYR B 375  ? 0.1973 0.2302 0.1781 -0.0195 0.0056  -0.0021 373  TYR B N   
11791 C CA  . TYR B 375  ? 0.1867 0.2170 0.1690 -0.0170 0.0046  -0.0039 373  TYR B CA  
11792 C C   . TYR B 375  ? 0.1743 0.2085 0.1607 -0.0164 0.0050  -0.0046 373  TYR B C   
11793 O O   . TYR B 375  ? 0.1877 0.2194 0.1755 -0.0153 0.0038  -0.0057 373  TYR B O   
11794 C CB  . TYR B 375  ? 0.2170 0.2408 0.1980 -0.0175 0.0025  -0.0039 373  TYR B CB  
11795 C CG  . TYR B 375  ? 0.2165 0.2360 0.1937 -0.0181 0.0018  -0.0031 373  TYR B CG  
11796 C CD1 . TYR B 375  ? 0.2211 0.2401 0.1958 -0.0209 0.0019  -0.0012 373  TYR B CD1 
11797 C CD2 . TYR B 375  ? 0.2432 0.2588 0.2191 -0.0159 0.0008  -0.0042 373  TYR B CD2 
11798 C CE1 . TYR B 375  ? 0.2363 0.2511 0.2072 -0.0213 0.0011  -0.0003 373  TYR B CE1 
11799 C CE2 . TYR B 375  ? 0.2580 0.2697 0.2303 -0.0163 -0.0001 -0.0034 373  TYR B CE2 
11800 C CZ  . TYR B 375  ? 0.2442 0.2554 0.2140 -0.0189 0.0000  -0.0015 373  TYR B CZ  
11801 O OH  . TYR B 375  ? 0.2874 0.2946 0.2536 -0.0192 -0.0010 -0.0006 373  TYR B OH  
11802 N N   . TRP B 376  ? 0.1832 0.2236 0.1714 -0.0170 0.0065  -0.0040 374  TRP B N   
11803 C CA  . TRP B 376  ? 0.1730 0.2172 0.1650 -0.0171 0.0066  -0.0042 374  TRP B CA  
11804 C C   . TRP B 376  ? 0.1748 0.2183 0.1687 -0.0140 0.0062  -0.0060 374  TRP B C   
11805 O O   . TRP B 376  ? 0.1885 0.2303 0.1839 -0.0142 0.0050  -0.0065 374  TRP B O   
11806 C CB  . TRP B 376  ? 0.1796 0.2313 0.1736 -0.0180 0.0084  -0.0031 374  TRP B CB  
11807 C CG  . TRP B 376  ? 0.1929 0.2485 0.1907 -0.0183 0.0081  -0.0032 374  TRP B CG  
11808 C CD1 . TRP B 376  ? 0.1745 0.2300 0.1734 -0.0212 0.0069  -0.0023 374  TRP B CD1 
11809 C CD2 . TRP B 376  ? 0.1864 0.2462 0.1873 -0.0156 0.0089  -0.0042 374  TRP B CD2 
11810 N NE1 . TRP B 376  ? 0.1826 0.2424 0.1851 -0.0205 0.0069  -0.0027 374  TRP B NE1 
11811 C CE2 . TRP B 376  ? 0.1864 0.2489 0.1902 -0.0171 0.0081  -0.0037 374  TRP B CE2 
11812 C CE3 . TRP B 376  ? 0.2251 0.2865 0.2264 -0.0121 0.0102  -0.0054 374  TRP B CE3 
11813 C CZ2 . TRP B 376  ? 0.1835 0.2502 0.1906 -0.0150 0.0085  -0.0044 374  TRP B CZ2 
11814 C CZ3 . TRP B 376  ? 0.2238 0.2891 0.2283 -0.0101 0.0106  -0.0060 374  TRP B CZ3 
11815 C CH2 . TRP B 376  ? 0.2203 0.2885 0.2279 -0.0115 0.0098  -0.0054 374  TRP B CH2 
11816 N N   . ASP B 377  ? 0.1978 0.2426 0.1915 -0.0112 0.0074  -0.0070 375  ASP B N   
11817 C CA  . ASP B 377  ? 0.2107 0.2549 0.2061 -0.0084 0.0071  -0.0086 375  ASP B CA  
11818 C C   . ASP B 377  ? 0.1803 0.2184 0.1749 -0.0081 0.0053  -0.0094 375  ASP B C   
11819 O O   . ASP B 377  ? 0.1952 0.2327 0.1918 -0.0070 0.0046  -0.0102 375  ASP B O   
11820 C CB  . ASP B 377  ? 0.2577 0.3026 0.2521 -0.0056 0.0084  -0.0097 375  ASP B CB  
11821 C CG  . ASP B 377  ? 0.3857 0.4369 0.3811 -0.0050 0.0105  -0.0092 375  ASP B CG  
11822 O OD1 . ASP B 377  ? 0.5347 0.5905 0.5334 -0.0051 0.0109  -0.0088 375  ASP B OD1 
11823 O OD2 . ASP B 377  ? 0.5735 0.6251 0.5665 -0.0044 0.0116  -0.0093 375  ASP B OD2 
11824 N N   . ALA B 378  ? 0.1834 0.2170 0.1751 -0.0089 0.0045  -0.0091 376  ALA B N   
11825 C CA  . ALA B 378  ? 0.1839 0.2120 0.1749 -0.0084 0.0028  -0.0098 376  ALA B CA  
11826 C C   . ALA B 378  ? 0.1969 0.2236 0.1890 -0.0102 0.0017  -0.0094 376  ALA B C   
11827 O O   . ALA B 378  ? 0.1911 0.2149 0.1840 -0.0092 0.0007  -0.0102 376  ALA B O   
11828 C CB  . ALA B 378  ? 0.2053 0.2292 0.1930 -0.0088 0.0022  -0.0094 376  ALA B CB  
11829 N N   . GLU B 379  ? 0.1817 0.2101 0.1736 -0.0128 0.0019  -0.0080 377  GLU B N   
11830 C CA  . GLU B 379  ? 0.1773 0.2040 0.1698 -0.0147 0.0007  -0.0077 377  GLU B CA  
11831 C C   . GLU B 379  ? 0.1907 0.2206 0.1863 -0.0138 0.0009  -0.0085 377  GLU B C   
11832 O O   . GLU B 379  ? 0.1851 0.2124 0.1811 -0.0139 -0.0002 -0.0090 377  GLU B O   
11833 C CB  . GLU B 379  ? 0.1894 0.2172 0.1809 -0.0180 0.0007  -0.0061 377  GLU B CB  
11834 C CG  . GLU B 379  ? 0.2082 0.2325 0.1964 -0.0193 0.0005  -0.0050 377  GLU B CG  
11835 C CD  . GLU B 379  ? 0.2142 0.2316 0.2004 -0.0192 -0.0012 -0.0053 377  GLU B CD  
11836 O OE1 . GLU B 379  ? 0.2326 0.2475 0.2198 -0.0183 -0.0021 -0.0063 377  GLU B OE1 
11837 O OE2 . GLU B 379  ? 0.2193 0.2337 0.2027 -0.0200 -0.0016 -0.0044 377  GLU B OE2 
11838 N N   . ILE B 380  ? 0.1778 0.2132 0.1753 -0.0128 0.0022  -0.0085 378  ILE B N   
11839 C CA  . ILE B 380  ? 0.1811 0.2195 0.1815 -0.0117 0.0022  -0.0091 378  ILE B CA  
11840 C C   . ILE B 380  ? 0.1721 0.2071 0.1728 -0.0092 0.0017  -0.0105 378  ILE B C   
11841 O O   . ILE B 380  ? 0.1766 0.2102 0.1781 -0.0091 0.0008  -0.0110 378  ILE B O   
11842 C CB  . ILE B 380  ? 0.1706 0.2155 0.1731 -0.0106 0.0038  -0.0088 378  ILE B CB  
11843 C CG1 . ILE B 380  ? 0.1766 0.2256 0.1793 -0.0133 0.0045  -0.0073 378  ILE B CG1 
11844 C CG2 . ILE B 380  ? 0.1874 0.2352 0.1928 -0.0093 0.0037  -0.0093 378  ILE B CG2 
11845 C CD1 . ILE B 380  ? 0.2043 0.2535 0.2077 -0.0164 0.0033  -0.0064 378  ILE B CD1 
11846 N N   . LYS B 381  ? 0.1804 0.2138 0.1800 -0.0072 0.0021  -0.0111 379  LYS B N   
11847 C CA  . LYS B 381  ? 0.1665 0.1969 0.1664 -0.0049 0.0016  -0.0124 379  LYS B CA  
11848 C C   . LYS B 381  ? 0.1734 0.1989 0.1724 -0.0057 0.0002  -0.0126 379  LYS B C   
11849 O O   . LYS B 381  ? 0.1809 0.2052 0.1811 -0.0047 -0.0003 -0.0133 379  LYS B O   
11850 C CB  . LYS B 381  ? 0.1732 0.2022 0.1717 -0.0031 0.0021  -0.0130 379  LYS B CB  
11851 C CG  . LYS B 381  ? 0.1991 0.2251 0.1981 -0.0011 0.0015  -0.0141 379  LYS B CG  
11852 C CD  . LYS B 381  ? 0.1773 0.2023 0.1749 0.0005  0.0019  -0.0148 379  LYS B CD  
11853 C CE  . LYS B 381  ? 0.2057 0.2280 0.2040 0.0023  0.0012  -0.0158 379  LYS B CE  
11854 N NZ  . LYS B 381  ? 0.1888 0.2098 0.1856 0.0038  0.0015  -0.0166 379  LYS B NZ  
11855 N N   . ARG B 382  ? 0.1737 0.1963 0.1705 -0.0073 -0.0004 -0.0119 380  ARG B N   
11856 C CA  . ARG B 382  ? 0.1788 0.1964 0.1747 -0.0076 -0.0017 -0.0122 380  ARG B CA  
11857 C C   . ARG B 382  ? 0.1758 0.1932 0.1726 -0.0087 -0.0022 -0.0122 380  ARG B C   
11858 O O   . ARG B 382  ? 0.1909 0.2056 0.1880 -0.0078 -0.0028 -0.0130 380  ARG B O   
11859 C CB  . ARG B 382  ? 0.1941 0.2086 0.1873 -0.0092 -0.0022 -0.0113 380  ARG B CB  
11860 C CG  . ARG B 382  ? 0.2355 0.2446 0.2275 -0.0093 -0.0035 -0.0115 380  ARG B CG  
11861 C CD  . ARG B 382  ? 0.3008 0.3080 0.2937 -0.0068 -0.0039 -0.0125 380  ARG B CD  
11862 N NE  . ARG B 382  ? 0.3408 0.3432 0.3328 -0.0067 -0.0050 -0.0126 380  ARG B NE  
11863 C CZ  . ARG B 382  ? 0.4961 0.4954 0.4863 -0.0068 -0.0058 -0.0121 380  ARG B CZ  
11864 N NH1 . ARG B 382  ? 0.4411 0.4413 0.4299 -0.0070 -0.0055 -0.0115 380  ARG B NH1 
11865 N NH2 . ARG B 382  ? 0.4961 0.4912 0.4856 -0.0065 -0.0068 -0.0121 380  ARG B NH2 
11866 N N   . ALA B 383  ? 0.1751 0.1954 0.1722 -0.0108 -0.0020 -0.0114 381  ALA B N   
11867 C CA  . ALA B 383  ? 0.1810 0.2011 0.1786 -0.0120 -0.0027 -0.0116 381  ALA B CA  
11868 C C   . ALA B 383  ? 0.1818 0.2039 0.1815 -0.0101 -0.0025 -0.0125 381  ALA B C   
11869 O O   . ALA B 383  ? 0.1879 0.2078 0.1875 -0.0101 -0.0032 -0.0131 381  ALA B O   
11870 C CB  . ALA B 383  ? 0.1894 0.2129 0.1872 -0.0148 -0.0026 -0.0104 381  ALA B CB  
11871 N N   . GLN B 384  ? 0.1663 0.1924 0.1677 -0.0085 -0.0015 -0.0125 382  GLN B N   
11872 C CA  . GLN B 384  ? 0.1827 0.2104 0.1859 -0.0066 -0.0013 -0.0132 382  GLN B CA  
11873 C C   . GLN B 384  ? 0.1798 0.2033 0.1826 -0.0048 -0.0016 -0.0142 382  GLN B C   
11874 O O   . GLN B 384  ? 0.1841 0.2068 0.1875 -0.0042 -0.0020 -0.0147 382  GLN B O   
11875 C CB  . GLN B 384  ? 0.1680 0.2003 0.1730 -0.0051 -0.0001 -0.0131 382  GLN B CB  
11876 C CG  . GLN B 384  ? 0.1750 0.2124 0.1812 -0.0066 0.0003  -0.0121 382  GLN B CG  
11877 C CD  . GLN B 384  ? 0.1767 0.2188 0.1848 -0.0046 0.0015  -0.0121 382  GLN B CD  
11878 O OE1 . GLN B 384  ? 0.2084 0.2492 0.2161 -0.0025 0.0021  -0.0128 382  GLN B OE1 
11879 N NE2 . GLN B 384  ? 0.1816 0.2290 0.1917 -0.0053 0.0018  -0.0113 382  GLN B NE2 
11880 N N   . LEU B 385  ? 0.1751 0.1963 0.1770 -0.0039 -0.0015 -0.0144 383  LEU B N   
11881 C CA  . LEU B 385  ? 0.1705 0.1882 0.1723 -0.0023 -0.0019 -0.0152 383  LEU B CA  
11882 C C   . LEU B 385  ? 0.1938 0.2081 0.1948 -0.0031 -0.0028 -0.0154 383  LEU B C   
11883 O O   . LEU B 385  ? 0.1886 0.2013 0.1902 -0.0019 -0.0029 -0.0160 383  LEU B O   
11884 C CB  . LEU B 385  ? 0.1936 0.2092 0.1942 -0.0017 -0.0020 -0.0152 383  LEU B CB  
11885 C CG  . LEU B 385  ? 0.2291 0.2470 0.2301 -0.0004 -0.0012 -0.0153 383  LEU B CG  
11886 C CD1 . LEU B 385  ? 0.2501 0.2654 0.2494 -0.0002 -0.0016 -0.0154 383  LEU B CD1 
11887 C CD2 . LEU B 385  ? 0.2547 0.2734 0.2575 0.0015  -0.0009 -0.0161 383  LEU B CD2 
11888 N N   . ASP B 386  ? 0.1821 0.1948 0.1814 -0.0051 -0.0033 -0.0148 384  ASP B N   
11889 C CA  . ASP B 386  ? 0.1804 0.1890 0.1784 -0.0058 -0.0041 -0.0151 384  ASP B CA  
11890 C C   . ASP B 386  ? 0.2050 0.2144 0.2032 -0.0067 -0.0043 -0.0154 384  ASP B C   
11891 O O   . ASP B 386  ? 0.2108 0.2166 0.2076 -0.0071 -0.0050 -0.0158 384  ASP B O   
11892 C CB  . ASP B 386  ? 0.2135 0.2191 0.2094 -0.0074 -0.0047 -0.0144 384  ASP B CB  
11893 C CG  . ASP B 386  ? 0.2634 0.2673 0.2588 -0.0062 -0.0048 -0.0143 384  ASP B CG  
11894 O OD1 . ASP B 386  ? 0.2835 0.2881 0.2802 -0.0042 -0.0045 -0.0148 384  ASP B OD1 
11895 O OD2 . ASP B 386  ? 0.2900 0.2918 0.2835 -0.0074 -0.0053 -0.0135 384  ASP B OD2 
11896 N N   . GLY B 387  ? 0.1796 0.1934 0.1792 -0.0070 -0.0039 -0.0151 385  GLY B N   
11897 C CA  . GLY B 387  ? 0.1792 0.1939 0.1788 -0.0079 -0.0043 -0.0153 385  GLY B CA  
11898 C C   . GLY B 387  ? 0.2085 0.2212 0.2062 -0.0106 -0.0052 -0.0150 385  GLY B C   
11899 O O   . GLY B 387  ? 0.2152 0.2259 0.2119 -0.0112 -0.0058 -0.0156 385  GLY B O   
11900 N N   . LEU B 388  ? 0.2052 0.2182 0.2022 -0.0122 -0.0052 -0.0142 386  LEU B N   
11901 C CA  . LEU B 388  ? 0.2202 0.2305 0.2151 -0.0149 -0.0061 -0.0138 386  LEU B CA  
11902 C C   . LEU B 388  ? 0.2185 0.2328 0.2142 -0.0172 -0.0065 -0.0132 386  LEU B C   
11903 O O   . LEU B 388  ? 0.2036 0.2232 0.2016 -0.0166 -0.0059 -0.0130 386  LEU B O   
11904 C CB  . LEU B 388  ? 0.2201 0.2282 0.2136 -0.0159 -0.0062 -0.0129 386  LEU B CB  
11905 C CG  . LEU B 388  ? 0.2133 0.2174 0.2062 -0.0136 -0.0062 -0.0135 386  LEU B CG  
11906 C CD1 . LEU B 388  ? 0.2558 0.2575 0.2470 -0.0144 -0.0064 -0.0126 386  LEU B CD1 
11907 C CD2 . LEU B 388  ? 0.2449 0.2442 0.2364 -0.0129 -0.0068 -0.0146 386  LEU B CD2 
11908 N N   . ALA B 389  ? 0.2188 0.2304 0.2124 -0.0199 -0.0075 -0.0130 387  ALA B N   
11909 C CA  . ALA B 389  ? 0.2246 0.2395 0.2188 -0.0222 -0.0081 -0.0127 387  ALA B CA  
11910 C C   . ALA B 389  ? 0.2044 0.2258 0.2010 -0.0233 -0.0075 -0.0113 387  ALA B C   
11911 O O   . ALA B 389  ? 0.2427 0.2690 0.2412 -0.0239 -0.0076 -0.0111 387  ALA B O   
11912 C CB  . ALA B 389  ? 0.2674 0.2776 0.2587 -0.0251 -0.0095 -0.0127 387  ALA B CB  
11913 N N   . ASP B 390  ? 0.2074 0.2290 0.2038 -0.0237 -0.0069 -0.0104 388  ASP B N   
11914 C CA  . ASP B 390  ? 0.1926 0.2203 0.1911 -0.0248 -0.0061 -0.0091 388  ASP B CA  
11915 C C   . ASP B 390  ? 0.1796 0.2062 0.1773 -0.0240 -0.0052 -0.0086 388  ASP B C   
11916 O O   . ASP B 390  ? 0.1992 0.2204 0.1949 -0.0227 -0.0054 -0.0092 388  ASP B O   
11917 C CB  . ASP B 390  ? 0.2092 0.2383 0.2073 -0.0288 -0.0070 -0.0081 388  ASP B CB  
11918 C CG  . ASP B 390  ? 0.2212 0.2584 0.2225 -0.0298 -0.0063 -0.0069 388  ASP B CG  
11919 O OD1 . ASP B 390  ? 0.2148 0.2559 0.2177 -0.0284 -0.0049 -0.0063 388  ASP B OD1 
11920 O OD2 . ASP B 390  ? 0.2666 0.3064 0.2688 -0.0320 -0.0073 -0.0065 388  ASP B OD2 
11921 N N   . PHE B 391  ? 0.1988 0.2305 0.1979 -0.0247 -0.0041 -0.0075 389  PHE B N   
11922 C CA  . PHE B 391  ? 0.1846 0.2155 0.1826 -0.0242 -0.0032 -0.0069 389  PHE B CA  
11923 C C   . PHE B 391  ? 0.1880 0.2153 0.1833 -0.0274 -0.0040 -0.0057 389  PHE B C   
11924 O O   . PHE B 391  ? 0.1991 0.2268 0.1943 -0.0304 -0.0048 -0.0051 389  PHE B O   
11925 C CB  . PHE B 391  ? 0.1956 0.2336 0.1960 -0.0236 -0.0017 -0.0061 389  PHE B CB  
11926 C CG  . PHE B 391  ? 0.1711 0.2123 0.1739 -0.0204 -0.0010 -0.0071 389  PHE B CG  
11927 C CD1 . PHE B 391  ? 0.1717 0.2103 0.1740 -0.0174 -0.0006 -0.0082 389  PHE B CD1 
11928 C CD2 . PHE B 391  ? 0.1818 0.2281 0.1873 -0.0206 -0.0011 -0.0070 389  PHE B CD2 
11929 C CE1 . PHE B 391  ? 0.1795 0.2202 0.1837 -0.0146 -0.0001 -0.0091 389  PHE B CE1 
11930 C CE2 . PHE B 391  ? 0.1730 0.2217 0.1805 -0.0177 -0.0006 -0.0078 389  PHE B CE2 
11931 C CZ  . PHE B 391  ? 0.1768 0.2225 0.1836 -0.0147 -0.0001 -0.0089 389  PHE B CZ  
11932 N N   . PRO B 392  ? 0.1741 0.1980 0.1673 -0.0269 -0.0037 -0.0054 390  PRO B N   
11933 C CA  . PRO B 392  ? 0.1745 0.1951 0.1651 -0.0298 -0.0043 -0.0041 390  PRO B CA  
11934 C C   . PRO B 392  ? 0.1952 0.2210 0.1863 -0.0315 -0.0031 -0.0025 390  PRO B C   
11935 O O   . PRO B 392  ? 0.1971 0.2206 0.1860 -0.0340 -0.0033 -0.0011 390  PRO B O   
11936 C CB  . PRO B 392  ? 0.2013 0.2158 0.1894 -0.0279 -0.0047 -0.0046 390  PRO B CB  
11937 C CG  . PRO B 392  ? 0.2110 0.2286 0.2008 -0.0245 -0.0035 -0.0055 390  PRO B CG  
11938 C CD  . PRO B 392  ? 0.1744 0.1965 0.1672 -0.0236 -0.0031 -0.0063 390  PRO B CD  
11939 N N   . VAL B 393  ? 0.2031 0.2355 0.1971 -0.0300 -0.0017 -0.0026 391  VAL B N   
11940 C CA  . VAL B 393  ? 0.1892 0.2277 0.1842 -0.0312 -0.0002 -0.0011 391  VAL B CA  
11941 C C   . VAL B 393  ? 0.1899 0.2355 0.1886 -0.0315 0.0003  -0.0010 391  VAL B C   
11942 O O   . VAL B 393  ? 0.1887 0.2346 0.1891 -0.0301 -0.0003 -0.0022 391  VAL B O   
11943 C CB  . VAL B 393  ? 0.1867 0.2265 0.1812 -0.0283 0.0014  -0.0015 391  VAL B CB  
11944 C CG1 . VAL B 393  ? 0.1849 0.2181 0.1757 -0.0281 0.0007  -0.0014 391  VAL B CG1 
11945 C CG2 . VAL B 393  ? 0.1766 0.2178 0.1731 -0.0246 0.0018  -0.0032 391  VAL B CG2 
11946 N N   . PHE B 394  ? 0.1837 0.2353 0.1838 -0.0334 0.0014  0.0005  392  PHE B N   
11947 C CA  . PHE B 394  ? 0.1634 0.2228 0.1675 -0.0334 0.0021  0.0008  392  PHE B CA  
11948 C C   . PHE B 394  ? 0.1828 0.2457 0.1889 -0.0292 0.0035  -0.0003 392  PHE B C   
11949 O O   . PHE B 394  ? 0.1879 0.2482 0.1923 -0.0267 0.0042  -0.0011 392  PHE B O   
11950 C CB  . PHE B 394  ? 0.1768 0.2421 0.1821 -0.0366 0.0030  0.0029  392  PHE B CB  
11951 C CG  . PHE B 394  ? 0.1791 0.2407 0.1824 -0.0410 0.0015  0.0041  392  PHE B CG  
11952 C CD1 . PHE B 394  ? 0.1950 0.2556 0.1991 -0.0431 -0.0003 0.0039  392  PHE B CD1 
11953 C CD2 . PHE B 394  ? 0.2013 0.2597 0.2015 -0.0430 0.0018  0.0054  392  PHE B CD2 
11954 C CE1 . PHE B 394  ? 0.1984 0.2548 0.2004 -0.0471 -0.0018 0.0049  392  PHE B CE1 
11955 C CE2 . PHE B 394  ? 0.1938 0.2479 0.1919 -0.0470 0.0003  0.0065  392  PHE B CE2 
11956 C CZ  . PHE B 394  ? 0.1984 0.2513 0.1973 -0.0491 -0.0015 0.0061  392  PHE B CZ  
11957 N N   . THR B 395  ? 0.1907 0.2593 0.2004 -0.0284 0.0036  -0.0005 393  THR B N   
11958 C CA  . THR B 395  ? 0.1757 0.2476 0.1875 -0.0243 0.0048  -0.0015 393  THR B CA  
11959 C C   . THR B 395  ? 0.1601 0.2408 0.1751 -0.0239 0.0066  -0.0005 393  THR B C   
11960 O O   . THR B 395  ? 0.2006 0.2838 0.2169 -0.0204 0.0079  -0.0013 393  THR B O   
11961 C CB  . THR B 395  ? 0.1804 0.2513 0.1936 -0.0227 0.0035  -0.0027 393  THR B CB  
11962 O OG1 . THR B 395  ? 0.1807 0.2559 0.1964 -0.0252 0.0026  -0.0018 393  THR B OG1 
11963 C CG2 . THR B 395  ? 0.2013 0.2638 0.2115 -0.0225 0.0021  -0.0039 393  THR B CG2 
11964 N N   . ARG B 396  ? 0.1712 0.2566 0.1876 -0.0272 0.0068  0.0013  394  ARG B N   
11965 C CA  . ARG B 396  ? 0.1846 0.2786 0.2039 -0.0269 0.0088  0.0025  394  ARG B CA  
11966 C C   . ARG B 396  ? 0.1956 0.2892 0.2125 -0.0289 0.0100  0.0037  394  ARG B C   
11967 O O   . ARG B 396  ? 0.2011 0.2910 0.2157 -0.0325 0.0089  0.0046  394  ARG B O   
11968 C CB  . ARG B 396  ? 0.1923 0.2934 0.2157 -0.0293 0.0082  0.0038  394  ARG B CB  
11969 C CG  . ARG B 396  ? 0.2119 0.3141 0.2377 -0.0275 0.0069  0.0028  394  ARG B CG  
11970 C CD  . ARG B 396  ? 0.2250 0.3355 0.2552 -0.0296 0.0065  0.0043  394  ARG B CD  
11971 N NE  . ARG B 396  ? 0.2539 0.3642 0.2856 -0.0284 0.0049  0.0034  394  ARG B NE  
11972 C CZ  . ARG B 396  ? 0.2736 0.3910 0.3095 -0.0266 0.0051  0.0037  394  ARG B CZ  
11973 N NH1 . ARG B 396  ? 0.2775 0.4034 0.3169 -0.0259 0.0069  0.0050  394  ARG B NH1 
11974 N NH2 . ARG B 396  ? 0.2862 0.4024 0.3229 -0.0254 0.0034  0.0029  394  ARG B NH2 
11975 N N   . LYS B 397  ? 0.1989 0.2963 0.2160 -0.0265 0.0124  0.0037  395  LYS B N   
11976 C CA  . LYS B 397  ? 0.1991 0.2959 0.2133 -0.0280 0.0137  0.0048  395  LYS B CA  
11977 C C   . LYS B 397  ? 0.1874 0.2887 0.2029 -0.0326 0.0138  0.0071  395  LYS B C   
11978 O O   . LYS B 397  ? 0.2141 0.3120 0.2265 -0.0356 0.0136  0.0083  395  LYS B O   
11979 C CB  . LYS B 397  ? 0.2415 0.3422 0.2559 -0.0244 0.0163  0.0042  395  LYS B CB  
11980 C CG  . LYS B 397  ? 0.2494 0.3477 0.2597 -0.0249 0.0176  0.0047  395  LYS B CG  
11981 C CD  . LYS B 397  ? 0.2624 0.3682 0.2742 -0.0274 0.0195  0.0069  395  LYS B CD  
11982 C CE  . LYS B 397  ? 0.2461 0.3493 0.2534 -0.0280 0.0208  0.0075  395  LYS B CE  
11983 N NZ  . LYS B 397  ? 0.2467 0.3572 0.2553 -0.0307 0.0227  0.0098  395  LYS B NZ  
11984 N N   . ILE B 398  ? 0.2020 0.3110 0.2222 -0.0335 0.0139  0.0080  396  ILE B N   
11985 C CA  . ILE B 398  ? 0.2485 0.3625 0.2705 -0.0381 0.0138  0.0103  396  ILE B CA  
11986 C C   . ILE B 398  ? 0.1876 0.2947 0.2071 -0.0422 0.0112  0.0107  396  ILE B C   
11987 O O   . ILE B 398  ? 0.2113 0.3190 0.2300 -0.0465 0.0110  0.0126  396  ILE B O   
11988 C CB  . ILE B 398  ? 0.2670 0.3908 0.2949 -0.0377 0.0142  0.0109  396  ILE B CB  
11989 C CG1 . ILE B 398  ? 0.3329 0.4637 0.3631 -0.0422 0.0148  0.0135  396  ILE B CG1 
11990 C CG2 . ILE B 398  ? 0.2404 0.3622 0.2698 -0.0376 0.0117  0.0099  396  ILE B CG2 
11991 C CD1 . ILE B 398  ? 0.3281 0.4700 0.3642 -0.0411 0.0160  0.0144  396  ILE B CD1 
11992 N N   . HIS B 399  ? 0.2046 0.3047 0.2225 -0.0410 0.0091  0.0090  397  HIS B N   
11993 C CA  . HIS B 399  ? 0.1951 0.2879 0.2102 -0.0445 0.0067  0.0091  397  HIS B CA  
11994 C C   . HIS B 399  ? 0.1874 0.2735 0.1977 -0.0456 0.0069  0.0096  397  HIS B C   
11995 O O   . HIS B 399  ? 0.2119 0.2949 0.2203 -0.0497 0.0059  0.0110  397  HIS B O   
11996 C CB  . HIS B 399  ? 0.1958 0.2831 0.2104 -0.0424 0.0048  0.0071  397  HIS B CB  
11997 C CG  . HIS B 399  ? 0.1998 0.2927 0.2184 -0.0421 0.0041  0.0068  397  HIS B CG  
11998 N ND1 . HIS B 399  ? 0.2096 0.2994 0.2284 -0.0396 0.0028  0.0050  397  HIS B ND1 
11999 C CD2 . HIS B 399  ? 0.2392 0.3407 0.2620 -0.0439 0.0044  0.0083  397  HIS B CD2 
12000 C CE1 . HIS B 399  ? 0.2229 0.3190 0.2456 -0.0399 0.0023  0.0054  397  HIS B CE1 
12001 N NE2 . HIS B 399  ? 0.2327 0.3361 0.2580 -0.0425 0.0032  0.0073  397  HIS B NE2 
12002 N N   . THR B 400  ? 0.1967 0.2802 0.2049 -0.0420 0.0081  0.0085  398  THR B N   
12003 C CA  . THR B 400  ? 0.2029 0.2807 0.2066 -0.0428 0.0084  0.0091  398  THR B CA  
12004 C C   . THR B 400  ? 0.1820 0.2649 0.1858 -0.0461 0.0099  0.0115  398  THR B C   
12005 O O   . THR B 400  ? 0.2206 0.2990 0.2211 -0.0492 0.0093  0.0128  398  THR B O   
12006 C CB  . THR B 400  ? 0.1973 0.2728 0.1992 -0.0384 0.0096  0.0075  398  THR B CB  
12007 O OG1 . THR B 400  ? 0.1878 0.2574 0.1891 -0.0361 0.0079  0.0055  398  THR B OG1 
12008 C CG2 . THR B 400  ? 0.2250 0.2962 0.2224 -0.0392 0.0101  0.0083  398  THR B CG2 
12009 N N   . ASP B 401  ? 0.2079 0.3002 0.2154 -0.0454 0.0120  0.0122  399  ASP B N   
12010 C CA  . ASP B 401  ? 0.2354 0.3334 0.2434 -0.0485 0.0137  0.0147  399  ASP B CA  
12011 C C   . ASP B 401  ? 0.2166 0.3146 0.2253 -0.0539 0.0120  0.0165  399  ASP B C   
12012 O O   . ASP B 401  ? 0.2311 0.3277 0.2374 -0.0575 0.0122  0.0185  399  ASP B O   
12013 C CB  . ASP B 401  ? 0.2398 0.3485 0.2522 -0.0464 0.0162  0.0149  399  ASP B CB  
12014 C CG  . ASP B 401  ? 0.2898 0.3988 0.3008 -0.0416 0.0183  0.0135  399  ASP B CG  
12015 O OD1 . ASP B 401  ? 0.2553 0.3575 0.2615 -0.0408 0.0183  0.0129  399  ASP B OD1 
12016 O OD2 . ASP B 401  ? 0.2808 0.3966 0.2953 -0.0386 0.0199  0.0128  399  ASP B OD2 
12017 N N   . VAL B 402  ? 0.2120 0.3111 0.2237 -0.0547 0.0102  0.0160  400  VAL B N   
12018 C CA  . VAL B 402  ? 0.2390 0.3375 0.2511 -0.0600 0.0083  0.0175  400  VAL B CA  
12019 C C   . VAL B 402  ? 0.1949 0.2823 0.2017 -0.0620 0.0063  0.0174  400  VAL B C   
12020 O O   . VAL B 402  ? 0.2313 0.3169 0.2363 -0.0665 0.0057  0.0194  400  VAL B O   
12021 C CB  . VAL B 402  ? 0.2135 0.3152 0.2295 -0.0601 0.0067  0.0167  400  VAL B CB  
12022 C CG1 . VAL B 402  ? 0.2567 0.3556 0.2721 -0.0656 0.0042  0.0179  400  VAL B CG1 
12023 C CG2 . VAL B 402  ? 0.2291 0.3425 0.2506 -0.0586 0.0086  0.0173  400  VAL B CG2 
12024 N N   . SER B 403  ? 0.1979 0.2779 0.2021 -0.0587 0.0054  0.0152  401  SER B N   
12025 C CA  . SER B 403  ? 0.2237 0.2931 0.2230 -0.0598 0.0036  0.0149  401  SER B CA  
12026 C C   . SER B 403  ? 0.1921 0.2594 0.1879 -0.0613 0.0047  0.0167  401  SER B C   
12027 O O   . SER B 403  ? 0.2128 0.2746 0.2055 -0.0650 0.0034  0.0181  401  SER B O   
12028 C CB  . SER B 403  ? 0.2061 0.2695 0.2038 -0.0553 0.0029  0.0123  401  SER B CB  
12029 O OG  . SER B 403  ? 0.2199 0.2735 0.2131 -0.0559 0.0014  0.0121  401  SER B OG  
12030 N N   . TYR B 404  ? 0.2105 0.2822 0.2065 -0.0587 0.0071  0.0168  402  TYR B N   
12031 C CA  . TYR B 404  ? 0.2231 0.2933 0.2155 -0.0599 0.0084  0.0185  402  TYR B CA  
12032 C C   . TYR B 404  ? 0.2146 0.2886 0.2076 -0.0652 0.0087  0.0214  402  TYR B C   
12033 O O   . TYR B 404  ? 0.2426 0.3111 0.2317 -0.0683 0.0080  0.0230  402  TYR B O   
12034 C CB  . TYR B 404  ? 0.2337 0.3092 0.2266 -0.0560 0.0111  0.0179  402  TYR B CB  
12035 C CG  . TYR B 404  ? 0.2120 0.2849 0.2005 -0.0563 0.0123  0.0191  402  TYR B CG  
12036 C CD1 . TYR B 404  ? 0.2321 0.3094 0.2201 -0.0597 0.0138  0.0217  402  TYR B CD1 
12037 C CD2 . TYR B 404  ? 0.2129 0.2790 0.1976 -0.0531 0.0118  0.0177  402  TYR B CD2 
12038 C CE1 . TYR B 404  ? 0.2463 0.3212 0.2298 -0.0599 0.0149  0.0229  402  TYR B CE1 
12039 C CE2 . TYR B 404  ? 0.2208 0.2844 0.2011 -0.0533 0.0127  0.0187  402  TYR B CE2 
12040 C CZ  . TYR B 404  ? 0.2406 0.3085 0.2202 -0.0567 0.0143  0.0214  402  TYR B CZ  
12041 O OH  . TYR B 404  ? 0.2694 0.3349 0.2444 -0.0569 0.0153  0.0226  402  TYR B OH  
12042 N N   . ILE B 405  ? 0.2318 0.3152 0.2296 -0.0664 0.0097  0.0221  403  ILE B N   
12043 C CA  . ILE B 405  ? 0.2466 0.3348 0.2457 -0.0717 0.0101  0.0250  403  ILE B CA  
12044 C C   . ILE B 405  ? 0.2324 0.3139 0.2299 -0.0762 0.0072  0.0257  403  ILE B C   
12045 O O   . ILE B 405  ? 0.2699 0.3491 0.2650 -0.0805 0.0069  0.0280  403  ILE B O   
12046 C CB  . ILE B 405  ? 0.2653 0.3657 0.2705 -0.0716 0.0119  0.0256  403  ILE B CB  
12047 C CG1 . ILE B 405  ? 0.3099 0.4163 0.3159 -0.0673 0.0150  0.0251  403  ILE B CG1 
12048 C CG2 . ILE B 405  ? 0.2754 0.3811 0.2824 -0.0774 0.0120  0.0286  403  ILE B CG2 
12049 C CD1 . ILE B 405  ? 0.4048 0.5225 0.4168 -0.0655 0.0168  0.0250  403  ILE B CD1 
12050 N N   . ALA B 406  ? 0.2448 0.3225 0.2431 -0.0751 0.0050  0.0237  404  ALA B N   
12051 C CA  . ALA B 406  ? 0.2699 0.3403 0.2662 -0.0790 0.0021  0.0240  404  ALA B CA  
12052 C C   . ALA B 406  ? 0.2519 0.3115 0.2422 -0.0795 0.0011  0.0242  404  ALA B C   
12053 O O   . ALA B 406  ? 0.2847 0.3394 0.2724 -0.0840 -0.0003 0.0259  404  ALA B O   
12054 C CB  . ALA B 406  ? 0.2556 0.3238 0.2534 -0.0771 0.0001  0.0215  404  ALA B CB  
12055 N N   . CYS B 407  ? 0.2390 0.2946 0.2270 -0.0749 0.0017  0.0227  405  CYS B N   
12056 C CA  . CYS B 407  ? 0.2591 0.3047 0.2415 -0.0749 0.0007  0.0229  405  CYS B CA  
12057 C C   . CYS B 407  ? 0.2230 0.2698 0.2030 -0.0777 0.0022  0.0257  405  CYS B C   
12058 O O   . CYS B 407  ? 0.2861 0.3253 0.2619 -0.0802 0.0009  0.0271  405  CYS B O   
12059 C CB  . CYS B 407  ? 0.2488 0.2904 0.2299 -0.0694 0.0008  0.0204  405  CYS B CB  
12060 S SG  . CYS B 407  ? 0.3013 0.3386 0.2838 -0.0671 -0.0014 0.0174  405  CYS B SG  
12061 N N   . ALA B 408  ? 0.2331 0.2894 0.2157 -0.0772 0.0048  0.0267  406  ALA B N   
12062 C CA  . ALA B 408  ? 0.2472 0.3059 0.2279 -0.0802 0.0064  0.0296  406  ALA B CA  
12063 C C   . ALA B 408  ? 0.2547 0.3132 0.2356 -0.0864 0.0053  0.0321  406  ALA B C   
12064 O O   . ALA B 408  ? 0.2999 0.3541 0.2770 -0.0897 0.0050  0.0344  406  ALA B O   
12065 C CB  . ALA B 408  ? 0.2816 0.3512 0.2655 -0.0783 0.0097  0.0300  406  ALA B CB  
12066 N N   . ALA B 409  ? 0.2808 0.3439 0.2661 -0.0882 0.0044  0.0317  407  ALA B N   
12067 C CA  . ALA B 409  ? 0.2991 0.3617 0.2846 -0.0944 0.0029  0.0340  407  ALA B CA  
12068 C C   . ALA B 409  ? 0.2735 0.3233 0.2537 -0.0963 0.0002  0.0339  407  ALA B C   
12069 O O   . ALA B 409  ? 0.3433 0.3897 0.3208 -0.1010 -0.0005 0.0365  407  ALA B O   
12070 C CB  . ALA B 409  ? 0.2720 0.3412 0.2629 -0.0956 0.0021  0.0332  407  ALA B CB  
12071 N N   . LYS B 410  ? 0.2814 0.3238 0.2599 -0.0926 -0.0015 0.0312  408  LYS B N   
12072 C CA  . LYS B 410  ? 0.2567 0.2867 0.2301 -0.0937 -0.0040 0.0309  408  LYS B CA  
12073 C C   . LYS B 410  ? 0.3142 0.3390 0.2828 -0.0937 -0.0034 0.0326  408  LYS B C   
12074 O O   . LYS B 410  ? 0.3454 0.3628 0.3102 -0.0973 -0.0048 0.0344  408  LYS B O   
12075 C CB  . LYS B 410  ? 0.3110 0.3355 0.2841 -0.0891 -0.0054 0.0275  408  LYS B CB  
12076 C CG  . LYS B 410  ? 0.3225 0.3342 0.2906 -0.0897 -0.0080 0.0270  408  LYS B CG  
12077 C CD  . LYS B 410  ? 0.3261 0.3330 0.2939 -0.0847 -0.0090 0.0237  408  LYS B CD  
12078 C CE  . LYS B 410  ? 0.3395 0.3501 0.3111 -0.0843 -0.0097 0.0217  408  LYS B CE  
12079 N NZ  . LYS B 410  ? 0.3717 0.3767 0.3418 -0.0884 -0.0122 0.0218  408  LYS B NZ  
12080 N N   . LEU B 411  ? 0.3107 0.3389 0.2793 -0.0897 -0.0012 0.0322  409  LEU B N   
12081 C CA  . LEU B 411  ? 0.3068 0.3305 0.2706 -0.0894 -0.0006 0.0338  409  LEU B CA  
12082 C C   . LEU B 411  ? 0.3028 0.3301 0.2657 -0.0945 0.0005  0.0374  409  LEU B C   
12083 O O   . LEU B 411  ? 0.3137 0.3339 0.2720 -0.0970 -0.0004 0.0394  409  LEU B O   
12084 C CB  . LEU B 411  ? 0.2779 0.3050 0.2419 -0.0841 0.0013  0.0323  409  LEU B CB  
12085 C CG  . LEU B 411  ? 0.2950 0.3156 0.2579 -0.0792 -0.0001 0.0293  409  LEU B CG  
12086 C CD1 . LEU B 411  ? 0.2986 0.3244 0.2630 -0.0743 0.0019  0.0276  409  LEU B CD1 
12087 C CD2 . LEU B 411  ? 0.3228 0.3321 0.2803 -0.0793 -0.0020 0.0299  409  LEU B CD2 
12088 N N   . LEU B 412  ? 0.3145 0.3528 0.2820 -0.0962 0.0026  0.0384  410  LEU B N   
12089 C CA  . LEU B 412  ? 0.3057 0.3486 0.2729 -0.1011 0.0040  0.0419  410  LEU B CA  
12090 C C   . LEU B 412  ? 0.3222 0.3593 0.2877 -0.1070 0.0016  0.0438  410  LEU B C   
12091 O O   . LEU B 412  ? 0.3904 0.4268 0.3535 -0.1113 0.0020  0.0470  410  LEU B O   
12092 C CB  . LEU B 412  ? 0.3422 0.3988 0.3150 -0.1012 0.0068  0.0424  410  LEU B CB  
12093 C CG  . LEU B 412  ? 0.3062 0.3683 0.2792 -0.0962 0.0097  0.0414  410  LEU B CG  
12094 C CD1 . LEU B 412  ? 0.4271 0.5023 0.4063 -0.0952 0.0122  0.0413  410  LEU B CD1 
12095 C CD2 . LEU B 412  ? 0.3744 0.4344 0.3425 -0.0972 0.0111  0.0438  410  LEU B CD2 
12096 N N   . ALA B 413  ? 0.3391 0.3719 0.3058 -0.1075 -0.0009 0.0420  411  ALA B N   
12097 C CA  . ALA B 413  ? 0.3987 0.4243 0.3631 -0.1128 -0.0035 0.0434  411  ALA B CA  
12098 C C   . ALA B 413  ? 0.4085 0.4207 0.3664 -0.1123 -0.0055 0.0435  411  ALA B C   
12099 O O   . ALA B 413  ? 0.4180 0.4228 0.3731 -0.1167 -0.0076 0.0449  411  ALA B O   
12100 C CB  . ALA B 413  ? 0.3608 0.3867 0.3285 -0.1136 -0.0056 0.0414  411  ALA B CB  
12101 N N   . ALA B 414  ? 0.3579 0.3668 0.3135 -0.1072 -0.0049 0.0421  412  ALA B N   
12102 C CA  . ALA B 414  ? 0.3102 0.3067 0.2601 -0.1060 -0.0068 0.0420  412  ALA B CA  
12103 C C   . ALA B 414  ? 0.3687 0.3643 0.3148 -0.1048 -0.0053 0.0439  412  ALA B C   
12104 O O   . ALA B 414  ? 0.3586 0.3457 0.3007 -0.1019 -0.0065 0.0432  412  ALA B O   
12105 C CB  . ALA B 414  ? 0.3592 0.3505 0.3092 -0.1008 -0.0082 0.0383  412  ALA B CB  
12106 N N   . THR B 415  ? 0.3448 0.3490 0.2921 -0.1070 -0.0028 0.0463  413  THR B N   
12107 C CA  . THR B 415  ? 0.3523 0.3561 0.2958 -0.1056 -0.0012 0.0480  413  THR B CA  
12108 C C   . THR B 415  ? 0.3690 0.3622 0.3064 -0.1084 -0.0030 0.0504  413  THR B C   
12109 O O   . THR B 415  ? 0.3807 0.3708 0.3140 -0.1065 -0.0025 0.0514  413  THR B O   
12110 C CB  . THR B 415  ? 0.3566 0.3721 0.3025 -0.1075 0.0021  0.0501  413  THR B CB  
12111 O OG1 . THR B 415  ? 0.4183 0.4356 0.3649 -0.1140 0.0019  0.0531  413  THR B OG1 
12112 C CG2 . THR B 415  ? 0.3957 0.4217 0.3475 -0.1042 0.0040  0.0477  413  THR B CG2 
12113 N N   . ASP B 416  ? 0.3864 0.3736 0.3228 -0.1128 -0.0052 0.0515  414  ASP B N   
12114 C CA  . ASP B 416  ? 0.4270 0.4024 0.3575 -0.1150 -0.0074 0.0534  414  ASP B CA  
12115 C C   . ASP B 416  ? 0.3757 0.3411 0.3034 -0.1102 -0.0095 0.0510  414  ASP B C   
12116 O O   . ASP B 416  ? 0.4412 0.3968 0.3636 -0.1107 -0.0111 0.0525  414  ASP B O   
12117 C CB  . ASP B 416  ? 0.3886 0.3603 0.3189 -0.1212 -0.0092 0.0551  414  ASP B CB  
12118 C CG  . ASP B 416  ? 0.6030 0.5751 0.5373 -0.1208 -0.0107 0.0521  414  ASP B CG  
12119 O OD1 . ASP B 416  ? 0.5028 0.4842 0.4422 -0.1183 -0.0092 0.0500  414  ASP B OD1 
12120 O OD2 . ASP B 416  ? 0.6398 0.6026 0.5718 -0.1231 -0.0134 0.0518  414  ASP B OD2 
12121 N N   . VAL B 417  ? 0.3624 0.3299 0.2934 -0.1055 -0.0096 0.0473  415  VAL B N   
12122 C CA  . VAL B 417  ? 0.3470 0.3054 0.2760 -0.1012 -0.0117 0.0448  415  VAL B CA  
12123 C C   . VAL B 417  ? 0.3472 0.3088 0.2771 -0.0951 -0.0105 0.0427  415  VAL B C   
12124 O O   . VAL B 417  ? 0.3604 0.3147 0.2876 -0.0915 -0.0119 0.0417  415  VAL B O   
12125 C CB  . VAL B 417  ? 0.4260 0.3823 0.3577 -0.1014 -0.0134 0.0423  415  VAL B CB  
12126 C CG1 . VAL B 417  ? 0.3794 0.3271 0.3095 -0.0968 -0.0153 0.0395  415  VAL B CG1 
12127 C CG2 . VAL B 417  ? 0.4349 0.3869 0.3651 -0.1077 -0.0149 0.0444  415  VAL B CG2 
12128 N N   . VAL B 418  ? 0.3174 0.2899 0.2514 -0.0937 -0.0080 0.0419  416  VAL B N   
12129 C CA  . VAL B 418  ? 0.3008 0.2770 0.2359 -0.0883 -0.0067 0.0398  416  VAL B CA  
12130 C C   . VAL B 418  ? 0.3272 0.3129 0.2630 -0.0891 -0.0037 0.0415  416  VAL B C   
12131 O O   . VAL B 418  ? 0.3183 0.3092 0.2552 -0.0935 -0.0025 0.0438  416  VAL B O   
12132 C CB  . VAL B 418  ? 0.3068 0.2863 0.2465 -0.0846 -0.0068 0.0362  416  VAL B CB  
12133 C CG1 . VAL B 418  ? 0.3125 0.2824 0.2510 -0.0832 -0.0095 0.0344  416  VAL B CG1 
12134 C CG2 . VAL B 418  ? 0.3240 0.3126 0.2687 -0.0873 -0.0055 0.0361  416  VAL B CG2 
12135 N N   . PHE B 419  ? 0.2811 0.2690 0.2162 -0.0848 -0.0025 0.0404  417  PHE B N   
12136 C CA  . PHE B 419  ? 0.2787 0.2753 0.2141 -0.0847 0.0004  0.0416  417  PHE B CA  
12137 C C   . PHE B 419  ? 0.2699 0.2748 0.2103 -0.0809 0.0021  0.0386  417  PHE B C   
12138 O O   . PHE B 419  ? 0.2768 0.2803 0.2171 -0.0762 0.0018  0.0363  417  PHE B O   
12139 C CB  . PHE B 419  ? 0.2919 0.2846 0.2221 -0.0827 0.0005  0.0426  417  PHE B CB  
12140 C CG  . PHE B 419  ? 0.3031 0.3042 0.2330 -0.0821 0.0036  0.0434  417  PHE B CG  
12141 C CD1 . PHE B 419  ? 0.3100 0.3175 0.2404 -0.0863 0.0057  0.0461  417  PHE B CD1 
12142 C CD2 . PHE B 419  ? 0.3047 0.3073 0.2337 -0.0774 0.0045  0.0415  417  PHE B CD2 
12143 C CE1 . PHE B 419  ? 0.3220 0.3374 0.2520 -0.0856 0.0088  0.0468  417  PHE B CE1 
12144 C CE2 . PHE B 419  ? 0.2992 0.3092 0.2275 -0.0768 0.0073  0.0421  417  PHE B CE2 
12145 C CZ  . PHE B 419  ? 0.2925 0.3090 0.2213 -0.0807 0.0096  0.0447  417  PHE B CZ  
12146 N N   . PRO B 420  ? 0.2662 0.2796 0.2112 -0.0828 0.0036  0.0387  418  PRO B N   
12147 C CA  . PRO B 420  ? 0.2559 0.2766 0.2058 -0.0792 0.0050  0.0359  418  PRO B CA  
12148 C C   . PRO B 420  ? 0.2478 0.2747 0.1972 -0.0762 0.0077  0.0356  418  PRO B C   
12149 O O   . PRO B 420  ? 0.2529 0.2836 0.2004 -0.0783 0.0096  0.0380  418  PRO B O   
12150 C CB  . PRO B 420  ? 0.2867 0.3148 0.2413 -0.0828 0.0057  0.0367  418  PRO B CB  
12151 C CG  . PRO B 420  ? 0.2884 0.3103 0.2406 -0.0880 0.0038  0.0392  418  PRO B CG  
12152 C CD  . PRO B 420  ? 0.2864 0.3024 0.2327 -0.0885 0.0038  0.0412  418  PRO B CD  
12153 N N   . GLN B 421  ? 0.2594 0.2869 0.2101 -0.0712 0.0078  0.0327  419  GLN B N   
12154 C CA  . GLN B 421  ? 0.2639 0.2965 0.2140 -0.0679 0.0102  0.0319  419  GLN B CA  
12155 C C   . GLN B 421  ? 0.2440 0.2837 0.1995 -0.0649 0.0114  0.0293  419  GLN B C   
12156 O O   . GLN B 421  ? 0.2348 0.2714 0.1919 -0.0619 0.0099  0.0268  419  GLN B O   
12157 C CB  . GLN B 421  ? 0.2665 0.2917 0.2121 -0.0646 0.0088  0.0309  419  GLN B CB  
12158 C CG  . GLN B 421  ? 0.2693 0.2865 0.2096 -0.0674 0.0072  0.0334  419  GLN B CG  
12159 C CD  . GLN B 421  ? 0.2622 0.2711 0.1991 -0.0642 0.0050  0.0322  419  GLN B CD  
12160 O OE1 . GLN B 421  ? 0.2844 0.2893 0.2231 -0.0621 0.0031  0.0301  419  GLN B OE1 
12161 N NE2 . GLN B 421  ? 0.2585 0.2652 0.1905 -0.0638 0.0053  0.0335  419  GLN B NE2 
12162 N N   . PHE B 422  ? 0.2472 0.2964 0.2055 -0.0657 0.0141  0.0301  420  PHE B N   
12163 C CA  . PHE B 422  ? 0.2334 0.2898 0.1973 -0.0633 0.0152  0.0280  420  PHE B CA  
12164 C C   . PHE B 422  ? 0.2190 0.2785 0.1824 -0.0585 0.0171  0.0260  420  PHE B C   
12165 O O   . PHE B 422  ? 0.2389 0.3049 0.2020 -0.0583 0.0198  0.0269  420  PHE B O   
12166 C CB  . PHE B 422  ? 0.2383 0.3034 0.2062 -0.0668 0.0168  0.0299  420  PHE B CB  
12167 C CG  . PHE B 422  ? 0.2693 0.3311 0.2376 -0.0717 0.0147  0.0317  420  PHE B CG  
12168 C CD1 . PHE B 422  ? 0.2663 0.3239 0.2367 -0.0716 0.0122  0.0301  420  PHE B CD1 
12169 C CD2 . PHE B 422  ? 0.2521 0.3144 0.2185 -0.0766 0.0152  0.0350  420  PHE B CD2 
12170 C CE1 . PHE B 422  ? 0.2790 0.3329 0.2493 -0.0761 0.0101  0.0315  420  PHE B CE1 
12171 C CE2 . PHE B 422  ? 0.3077 0.3662 0.2742 -0.0812 0.0131  0.0365  420  PHE B CE2 
12172 C CZ  . PHE B 422  ? 0.2986 0.3529 0.2671 -0.0809 0.0105  0.0347  420  PHE B CZ  
12173 N N   . ALA B 423  ? 0.2270 0.2816 0.1901 -0.0547 0.0156  0.0234  421  ALA B N   
12174 C CA  . ALA B 423  ? 0.2431 0.2997 0.2058 -0.0501 0.0170  0.0212  421  ALA B CA  
12175 C C   . ALA B 423  ? 0.2407 0.3050 0.2090 -0.0479 0.0184  0.0196  421  ALA B C   
12176 O O   . ALA B 423  ? 0.2782 0.3414 0.2498 -0.0471 0.0169  0.0181  421  ALA B O   
12177 C CB  . ALA B 423  ? 0.2379 0.2862 0.1983 -0.0472 0.0146  0.0192  421  ALA B CB  
12178 N N   . THR B 424  ? 0.2578 0.3298 0.2270 -0.0468 0.0214  0.0198  422  THR B N   
12179 C CA  . THR B 424  ? 0.2403 0.3197 0.2146 -0.0443 0.0229  0.0183  422  THR B CA  
12180 C C   . THR B 424  ? 0.2276 0.3134 0.2010 -0.0422 0.0262  0.0183  422  THR B C   
12181 O O   . THR B 424  ? 0.2556 0.3430 0.2259 -0.0442 0.0278  0.0203  422  THR B O   
12182 C CB  . THR B 424  ? 0.2855 0.3706 0.2649 -0.0474 0.0228  0.0197  422  THR B CB  
12183 O OG1 . THR B 424  ? 0.2788 0.3710 0.2631 -0.0445 0.0242  0.0182  422  THR B OG1 
12184 C CG2 . THR B 424  ? 0.2566 0.3466 0.2356 -0.0517 0.0245  0.0228  422  THR B CG2 
12185 N N   . HIS B 425  ? 0.2461 0.3352 0.2219 -0.0380 0.0273  0.0159  423  HIS B N   
12186 C CA  . HIS B 425  ? 0.2403 0.3364 0.2161 -0.0355 0.0306  0.0156  423  HIS B CA  
12187 C C   . HIS B 425  ? 0.2767 0.3827 0.2587 -0.0356 0.0325  0.0161  423  HIS B C   
12188 O O   . HIS B 425  ? 0.2764 0.3890 0.2592 -0.0332 0.0354  0.0157  423  HIS B O   
12189 C CB  . HIS B 425  ? 0.2537 0.3465 0.2275 -0.0306 0.0308  0.0126  423  HIS B CB  
12190 C CG  . HIS B 425  ? 0.2689 0.3530 0.2366 -0.0303 0.0292  0.0121  423  HIS B CG  
12191 N ND1 . HIS B 425  ? 0.2903 0.3677 0.2568 -0.0276 0.0271  0.0098  423  HIS B ND1 
12192 C CD2 . HIS B 425  ? 0.2807 0.3619 0.2432 -0.0325 0.0294  0.0139  423  HIS B CD2 
12193 C CE1 . HIS B 425  ? 0.2620 0.3329 0.2231 -0.0281 0.0260  0.0101  423  HIS B CE1 
12194 N NE2 . HIS B 425  ? 0.2591 0.3320 0.2175 -0.0309 0.0273  0.0125  423  HIS B NE2 
12195 N N   . ASN B 426  ? 0.2625 0.3697 0.2487 -0.0381 0.0308  0.0169  424  ASN B N   
12196 C CA  . ASN B 426  ? 0.2600 0.3764 0.2525 -0.0382 0.0320  0.0174  424  ASN B CA  
12197 C C   . ASN B 426  ? 0.2766 0.3997 0.2704 -0.0426 0.0336  0.0205  424  ASN B C   
12198 O O   . ASN B 426  ? 0.2446 0.3647 0.2375 -0.0471 0.0319  0.0224  424  ASN B O   
12199 C CB  . ASN B 426  ? 0.2582 0.3717 0.2541 -0.0390 0.0290  0.0166  424  ASN B CB  
12200 C CG  . ASN B 426  ? 0.2666 0.3889 0.2690 -0.0385 0.0297  0.0167  424  ASN B CG  
12201 O OD1 . ASN B 426  ? 0.2843 0.4150 0.2897 -0.0405 0.0316  0.0187  424  ASN B OD1 
12202 N ND2 . ASN B 426  ? 0.2542 0.3747 0.2590 -0.0357 0.0282  0.0146  424  ASN B ND2 
12203 N N   . ALA B 427  ? 0.2807 0.4128 0.2764 -0.0411 0.0370  0.0210  425  ALA B N   
12204 C CA  . ALA B 427  ? 0.3068 0.4463 0.3038 -0.0451 0.0389  0.0241  425  ALA B CA  
12205 C C   . ALA B 427  ? 0.2366 0.3806 0.2392 -0.0490 0.0375  0.0258  425  ALA B C   
12206 O O   . ALA B 427  ? 0.2798 0.4263 0.2826 -0.0539 0.0377  0.0287  425  ALA B O   
12207 C CB  . ALA B 427  ? 0.3292 0.4779 0.3275 -0.0421 0.0430  0.0241  425  ALA B CB  
12208 N N   . GLN B 428  ? 0.2629 0.4080 0.2699 -0.0471 0.0360  0.0242  426  GLN B N   
12209 C CA  . GLN B 428  ? 0.2792 0.4279 0.2911 -0.0509 0.0343  0.0257  426  GLN B CA  
12210 C C   . GLN B 428  ? 0.2652 0.4046 0.2740 -0.0551 0.0310  0.0264  426  GLN B C   
12211 O O   . GLN B 428  ? 0.2836 0.4248 0.2935 -0.0603 0.0302  0.0289  426  GLN B O   
12212 C CB  . GLN B 428  ? 0.2729 0.4250 0.2901 -0.0476 0.0334  0.0238  426  GLN B CB  
12213 C CG  . GLN B 428  ? 0.2933 0.4522 0.3164 -0.0511 0.0323  0.0254  426  GLN B CG  
12214 C CD  . GLN B 428  ? 0.2910 0.4425 0.3129 -0.0553 0.0286  0.0258  426  GLN B CD  
12215 O OE1 . GLN B 428  ? 0.3180 0.4596 0.3362 -0.0540 0.0265  0.0240  426  GLN B OE1 
12216 N NE2 . GLN B 428  ? 0.3440 0.5000 0.3689 -0.0604 0.0279  0.0283  426  GLN B NE2 
12217 N N   . THR B 429  ? 0.2808 0.4099 0.2854 -0.0530 0.0290  0.0244  427  THR B N   
12218 C CA  . THR B 429  ? 0.2815 0.4012 0.2827 -0.0565 0.0260  0.0250  427  THR B CA  
12219 C C   . THR B 429  ? 0.2497 0.3679 0.2469 -0.0605 0.0267  0.0277  427  THR B C   
12220 O O   . THR B 429  ? 0.2884 0.4044 0.2853 -0.0654 0.0251  0.0296  427  THR B O   
12221 C CB  . THR B 429  ? 0.2507 0.3606 0.2480 -0.0530 0.0242  0.0224  427  THR B CB  
12222 O OG1 . THR B 429  ? 0.2646 0.3762 0.2653 -0.0488 0.0240  0.0199  427  THR B OG1 
12223 C CG2 . THR B 429  ? 0.3085 0.4091 0.3032 -0.0561 0.0210  0.0227  427  THR B CG2 
12224 N N   . LEU B 430  ? 0.2833 0.4023 0.2771 -0.0585 0.0292  0.0278  428  LEU B N   
12225 C CA  . LEU B 430  ? 0.2804 0.3983 0.2700 -0.0620 0.0302  0.0304  428  LEU B CA  
12226 C C   . LEU B 430  ? 0.3072 0.4334 0.3005 -0.0669 0.0313  0.0335  428  LEU B C   
12227 O O   . LEU B 430  ? 0.2911 0.4140 0.2824 -0.0718 0.0301  0.0359  428  LEU B O   
12228 C CB  . LEU B 430  ? 0.3167 0.4361 0.3027 -0.0586 0.0330  0.0298  428  LEU B CB  
12229 C CG  . LEU B 430  ? 0.3134 0.4301 0.2934 -0.0608 0.0342  0.0319  428  LEU B CG  
12230 C CD1 . LEU B 430  ? 0.3424 0.4595 0.3190 -0.0562 0.0365  0.0302  428  LEU B CD1 
12231 C CD2 . LEU B 430  ? 0.3592 0.4834 0.3408 -0.0655 0.0362  0.0354  428  LEU B CD2 
12232 N N   . ALA B 431  ? 0.3182 0.4553 0.3169 -0.0655 0.0337  0.0335  429  ALA B N   
12233 C CA  . ALA B 431  ? 0.3334 0.4799 0.3363 -0.0699 0.0350  0.0365  429  ALA B CA  
12234 C C   . ALA B 431  ? 0.3032 0.4473 0.3085 -0.0747 0.0318  0.0376  429  ALA B C   
12235 O O   . ALA B 431  ? 0.3167 0.4621 0.3218 -0.0801 0.0316  0.0406  429  ALA B O   
12236 C CB  . ALA B 431  ? 0.3090 0.4675 0.3179 -0.0668 0.0378  0.0360  429  ALA B CB  
12237 N N   . ALA B 432  ? 0.3148 0.4547 0.3217 -0.0728 0.0292  0.0353  430  ALA B N   
12238 C CA  . ALA B 432  ? 0.2914 0.4283 0.3001 -0.0771 0.0260  0.0360  430  ALA B CA  
12239 C C   . ALA B 432  ? 0.3115 0.4383 0.3146 -0.0812 0.0240  0.0374  430  ALA B C   
12240 O O   . ALA B 432  ? 0.3339 0.4607 0.3376 -0.0867 0.0227  0.0397  430  ALA B O   
12241 C CB  . ALA B 432  ? 0.3167 0.4500 0.3274 -0.0737 0.0237  0.0330  430  ALA B CB  
12242 N N   . ILE B 433  ? 0.2980 0.4158 0.2953 -0.0786 0.0236  0.0361  431  ILE B N   
12243 C CA  . ILE B 433  ? 0.3508 0.4585 0.3425 -0.0820 0.0216  0.0374  431  ILE B CA  
12244 C C   . ILE B 433  ? 0.3017 0.4126 0.2913 -0.0859 0.0236  0.0408  431  ILE B C   
12245 O O   . ILE B 433  ? 0.3068 0.4133 0.2943 -0.0910 0.0221  0.0431  431  ILE B O   
12246 C CB  . ILE B 433  ? 0.3255 0.4233 0.3122 -0.0778 0.0205  0.0351  431  ILE B CB  
12247 C CG1 . ILE B 433  ? 0.3909 0.4844 0.3795 -0.0753 0.0180  0.0323  431  ILE B CG1 
12248 C CG2 . ILE B 433  ? 0.3878 0.4762 0.3683 -0.0807 0.0192  0.0368  431  ILE B CG2 
12249 C CD1 . ILE B 433  ? 0.3902 0.4762 0.3752 -0.0708 0.0173  0.0298  431  ILE B CD1 
12250 N N   . TYR B 434  ? 0.3028 0.4208 0.2925 -0.0836 0.0270  0.0412  432  TYR B N   
12251 C CA  . TYR B 434  ? 0.3168 0.4388 0.3045 -0.0872 0.0293  0.0445  432  TYR B CA  
12252 C C   . TYR B 434  ? 0.3223 0.4502 0.3142 -0.0932 0.0290  0.0474  432  TYR B C   
12253 O O   . TYR B 434  ? 0.3225 0.4473 0.3114 -0.0982 0.0285  0.0503  432  TYR B O   
12254 C CB  . TYR B 434  ? 0.3381 0.4687 0.3266 -0.0833 0.0333  0.0441  432  TYR B CB  
12255 C CG  . TYR B 434  ? 0.3327 0.4701 0.3204 -0.0866 0.0363  0.0474  432  TYR B CG  
12256 C CD1 . TYR B 434  ? 0.3261 0.4574 0.3072 -0.0887 0.0366  0.0493  432  TYR B CD1 
12257 C CD2 . TYR B 434  ? 0.3600 0.5103 0.3536 -0.0875 0.0391  0.0487  432  TYR B CD2 
12258 C CE1 . TYR B 434  ? 0.3760 0.5137 0.3561 -0.0918 0.0395  0.0525  432  TYR B CE1 
12259 C CE2 . TYR B 434  ? 0.3302 0.4872 0.3232 -0.0905 0.0421  0.0519  432  TYR B CE2 
12260 C CZ  . TYR B 434  ? 0.3799 0.5306 0.3661 -0.0927 0.0423  0.0537  432  TYR B CZ  
12261 O OH  . TYR B 434  ? 0.3882 0.5457 0.3736 -0.0958 0.0454  0.0570  432  TYR B OH  
12262 N N   . HIS B 435  ? 0.3595 0.4953 0.3581 -0.0930 0.0289  0.0467  433  HIS B N   
12263 C CA  . HIS B 435  ? 0.3500 0.4917 0.3527 -0.0989 0.0284  0.0495  433  HIS B CA  
12264 C C   . HIS B 435  ? 0.3438 0.4765 0.3454 -0.1028 0.0243  0.0495  433  HIS B C   
12265 O O   . HIS B 435  ? 0.3502 0.4827 0.3517 -0.1088 0.0233  0.0523  433  HIS B O   
12266 C CB  . HIS B 435  ? 0.3961 0.5508 0.4066 -0.0973 0.0301  0.0491  433  HIS B CB  
12267 C CG  . HIS B 435  ? 0.3314 0.4963 0.3433 -0.0953 0.0345  0.0501  433  HIS B CG  
12268 N ND1 . HIS B 435  ? 0.3479 0.5203 0.3610 -0.0998 0.0367  0.0537  433  HIS B ND1 
12269 C CD2 . HIS B 435  ? 0.3567 0.5253 0.3687 -0.0892 0.0372  0.0481  433  HIS B CD2 
12270 C CE1 . HIS B 435  ? 0.4070 0.5876 0.4209 -0.0964 0.0407  0.0538  433  HIS B CE1 
12271 N NE2 . HIS B 435  ? 0.2903 0.4687 0.3035 -0.0900 0.0410  0.0503  433  HIS B NE2 
12272 N N   . MET B 436  ? 0.3247 0.4497 0.3252 -0.0994 0.0218  0.0464  434  MET B N   
12273 C CA  . MET B 436  ? 0.3180 0.4335 0.3166 -0.1026 0.0180  0.0461  434  MET B CA  
12274 C C   . MET B 436  ? 0.3605 0.4666 0.3528 -0.1064 0.0169  0.0482  434  MET B C   
12275 O O   . MET B 436  ? 0.3767 0.4777 0.3680 -0.1113 0.0144  0.0495  434  MET B O   
12276 C CB  . MET B 436  ? 0.3419 0.4503 0.3396 -0.0976 0.0160  0.0424  434  MET B CB  
12277 C CG  . MET B 436  ? 0.3538 0.4511 0.3486 -0.1000 0.0122  0.0417  434  MET B CG  
12278 S SD  . MET B 436  ? 0.4151 0.5048 0.4086 -0.0936 0.0106  0.0374  434  MET B SD  
12279 C CE  . MET B 436  ? 0.3671 0.4675 0.3682 -0.0916 0.0109  0.0358  434  MET B CE  
12280 N N   . ALA B 437  ? 0.3180 0.4216 0.3058 -0.1042 0.0188  0.0486  435  ALA B N   
12281 C CA  . ALA B 437  ? 0.3455 0.4395 0.3267 -0.1072 0.0177  0.0506  435  ALA B CA  
12282 C C   . ALA B 437  ? 0.4032 0.5017 0.3847 -0.1137 0.0187  0.0547  435  ALA B C   
12283 O O   . ALA B 437  ? 0.4415 0.5318 0.4182 -0.1175 0.0172  0.0567  435  ALA B O   
12284 C CB  . ALA B 437  ? 0.3725 0.4629 0.3488 -0.1029 0.0193  0.0498  435  ALA B CB  
12285 N N   . GLY B 438  ? 0.4012 0.5125 0.3884 -0.1150 0.0211  0.0560  436  GLY B N   
12286 C CA  . GLY B 438  ? 0.4257 0.5424 0.4140 -0.1214 0.0222  0.0600  436  GLY B CA  
12287 C C   . GLY B 438  ? 0.5045 0.6240 0.4892 -0.1215 0.0254  0.0623  436  GLY B C   
12288 O O   . GLY B 438  ? 0.4501 0.5672 0.4313 -0.1167 0.0269  0.0608  436  GLY B O   
12289 N N   . LYS B 439  ? 0.4780 0.6024 0.4635 -0.1274 0.0265  0.0661  437  LYS B N   
12290 C CA  . LYS B 439  ? 0.4718 0.6006 0.4544 -0.1283 0.0299  0.0688  437  LYS B CA  
12291 C C   . LYS B 439  ? 0.4627 0.5792 0.4368 -0.1292 0.0288  0.0700  437  LYS B C   
12292 O O   . LYS B 439  ? 0.5583 0.6766 0.5287 -0.1280 0.0316  0.0712  437  LYS B O   
12293 C CB  . LYS B 439  ? 0.4421 0.5810 0.4289 -0.1346 0.0316  0.0727  437  LYS B CB  
12294 N N   . ASP B 440  ? 0.4485 0.5529 0.4193 -0.1313 0.0249  0.0697  438  ASP B N   
12295 C CA  . ASP B 440  ? 0.5032 0.5958 0.4661 -0.1327 0.0236  0.0713  438  ASP B CA  
12296 C C   . ASP B 440  ? 0.4374 0.5228 0.3962 -0.1261 0.0231  0.0681  438  ASP B C   
12297 O O   . ASP B 440  ? 0.5228 0.6039 0.4830 -0.1226 0.0209  0.0647  438  ASP B O   
12298 C CB  . ASP B 440  ? 0.5196 0.6020 0.4807 -0.1377 0.0196  0.0723  438  ASP B CB  
12299 N N   . PHE B 441  ? 0.4566 0.5408 0.4102 -0.1245 0.0250  0.0691  439  PHE B N   
12300 C CA  . PHE B 441  ? 0.4121 0.4896 0.3616 -0.1185 0.0245  0.0663  439  PHE B CA  
12301 C C   . PHE B 441  ? 0.4336 0.5040 0.3753 -0.1193 0.0247  0.0686  439  PHE B C   
12302 O O   . PHE B 441  ? 0.4317 0.5069 0.3716 -0.1226 0.0271  0.0719  439  PHE B O   
12303 C CB  . PHE B 441  ? 0.3929 0.4792 0.3454 -0.1127 0.0274  0.0635  439  PHE B CB  
12304 C CG  . PHE B 441  ? 0.3781 0.4571 0.3266 -0.1068 0.0264  0.0605  439  PHE B CG  
12305 C CD1 . PHE B 441  ? 0.3608 0.4339 0.3108 -0.1036 0.0237  0.0572  439  PHE B CD1 
12306 C CD2 . PHE B 441  ? 0.3506 0.4282 0.2935 -0.1047 0.0282  0.0612  439  PHE B CD2 
12307 C CE1 . PHE B 441  ? 0.3496 0.4161 0.2960 -0.0984 0.0227  0.0546  439  PHE B CE1 
12308 C CE2 . PHE B 441  ? 0.3672 0.4380 0.3063 -0.0996 0.0270  0.0585  439  PHE B CE2 
12309 C CZ  . PHE B 441  ? 0.3591 0.4244 0.3002 -0.0965 0.0243  0.0552  439  PHE B CZ  
12310 N N   . HIS B 442  ? 0.4329 0.4923 0.3700 -0.1162 0.0221  0.0668  440  HIS B N   
12311 C CA  . HIS B 442  ? 0.4058 0.4585 0.3355 -0.1154 0.0221  0.0683  440  HIS B CA  
12312 C C   . HIS B 442  ? 0.3785 0.4251 0.3063 -0.1091 0.0207  0.0646  440  HIS B C   
12313 O O   . HIS B 442  ? 0.3956 0.4395 0.3266 -0.1067 0.0186  0.0616  440  HIS B O   
12314 C CB  . HIS B 442  ? 0.4311 0.4735 0.3562 -0.1204 0.0194  0.0713  440  HIS B CB  
12315 C CG  . HIS B 442  ? 0.4994 0.5332 0.4259 -0.1207 0.0155  0.0696  440  HIS B CG  
12316 N ND1 . HIS B 442  ? 0.5502 0.5735 0.4734 -0.1168 0.0128  0.0674  440  HIS B ND1 
12317 C CD2 . HIS B 442  ? 0.4903 0.5243 0.4209 -0.1243 0.0140  0.0697  440  HIS B CD2 
12318 C CE1 . HIS B 442  ? 0.5443 0.5619 0.4694 -0.1179 0.0099  0.0661  440  HIS B CE1 
12319 N NE2 . HIS B 442  ? 0.5506 0.5742 0.4800 -0.1225 0.0105  0.0675  440  HIS B NE2 
12320 N N   . VAL B 443  ? 0.3909 0.4356 0.3133 -0.1065 0.0217  0.0648  441  VAL B N   
12321 C CA  . VAL B 443  ? 0.3892 0.4274 0.3093 -0.1009 0.0200  0.0616  441  VAL B CA  
12322 C C   . VAL B 443  ? 0.3696 0.3958 0.2878 -0.1017 0.0158  0.0614  441  VAL B C   
12323 O O   . VAL B 443  ? 0.4240 0.4438 0.3385 -0.1059 0.0144  0.0645  441  VAL B O   
12324 C CB  . VAL B 443  ? 0.4320 0.4694 0.3458 -0.0987 0.0215  0.0623  441  VAL B CB  
12325 C CG1 . VAL B 443  ? 0.4124 0.4412 0.3233 -0.0939 0.0189  0.0596  441  VAL B CG1 
12326 C CG2 . VAL B 443  ? 0.4405 0.4896 0.3566 -0.0965 0.0256  0.0614  441  VAL B CG2 
12327 N N   . GLY B 444  ? 0.3710 0.3939 0.2916 -0.0976 0.0140  0.0578  442  GLY B N   
12328 C CA  . GLY B 444  ? 0.3757 0.3882 0.2955 -0.0978 0.0103  0.0571  442  GLY B CA  
12329 C C   . GLY B 444  ? 0.3662 0.3802 0.2915 -0.0997 0.0092  0.0560  442  GLY B C   
12330 O O   . GLY B 444  ? 0.3587 0.3646 0.2840 -0.0989 0.0062  0.0546  442  GLY B O   
12331 N N   . LYS B 445  ? 0.3507 0.3747 0.2807 -0.1022 0.0114  0.0567  443  LYS B N   
12332 C CA  . LYS B 445  ? 0.3342 0.3602 0.2697 -0.1038 0.0103  0.0555  443  LYS B CA  
12333 C C   . LYS B 445  ? 0.3401 0.3681 0.2796 -0.0983 0.0100  0.0513  443  LYS B C   
12334 O O   . LYS B 445  ? 0.3384 0.3606 0.2791 -0.0975 0.0074  0.0493  443  LYS B O   
12335 C CB  . LYS B 445  ? 0.3464 0.3831 0.2861 -0.1080 0.0127  0.0576  443  LYS B CB  
12336 C CG  . LYS B 445  ? 0.3931 0.4317 0.3381 -0.1104 0.0112  0.0567  443  LYS B CG  
12337 C CD  . LYS B 445  ? 0.4532 0.5028 0.4025 -0.1149 0.0134  0.0591  443  LYS B CD  
12338 C CE  . LYS B 445  ? 0.5209 0.5727 0.4756 -0.1173 0.0118  0.0582  443  LYS B CE  
12339 N NZ  . LYS B 445  ? 0.5145 0.5767 0.4734 -0.1223 0.0137  0.0609  443  LYS B NZ  
12340 N N   . TYR B 446  ? 0.3000 0.3360 0.2412 -0.0947 0.0127  0.0499  444  TYR B N   
12341 C CA  . TYR B 446  ? 0.2901 0.3279 0.2344 -0.0892 0.0127  0.0460  444  TYR B CA  
12342 C C   . TYR B 446  ? 0.3137 0.3578 0.2571 -0.0858 0.0157  0.0455  444  TYR B C   
12343 O O   . TYR B 446  ? 0.2998 0.3479 0.2410 -0.0879 0.0179  0.0480  444  TYR B O   
12344 C CB  . TYR B 446  ? 0.2936 0.3379 0.2446 -0.0898 0.0128  0.0446  444  TYR B CB  
12345 C CG  . TYR B 446  ? 0.3513 0.4080 0.3065 -0.0914 0.0160  0.0459  444  TYR B CG  
12346 C CD1 . TYR B 446  ? 0.3036 0.3684 0.2615 -0.0872 0.0185  0.0440  444  TYR B CD1 
12347 C CD2 . TYR B 446  ? 0.3419 0.4023 0.2985 -0.0972 0.0163  0.0490  444  TYR B CD2 
12348 C CE1 . TYR B 446  ? 0.4013 0.4776 0.3631 -0.0883 0.0216  0.0452  444  TYR B CE1 
12349 C CE2 . TYR B 446  ? 0.3846 0.4568 0.3453 -0.0986 0.0193  0.0503  444  TYR B CE2 
12350 C CZ  . TYR B 446  ? 0.3441 0.4244 0.3076 -0.0940 0.0220  0.0483  444  TYR B CZ  
12351 O OH  . TYR B 446  ? 0.4995 0.5918 0.4673 -0.0952 0.0250  0.0496  444  TYR B OH  
12352 N N   . GLU B 447  ? 0.2791 0.3238 0.2239 -0.0806 0.0157  0.0422  445  GLU B N   
12353 C CA  . GLU B 447  ? 0.2758 0.3265 0.2199 -0.0771 0.0186  0.0412  445  GLU B CA  
12354 C C   . GLU B 447  ? 0.2412 0.2969 0.1904 -0.0729 0.0192  0.0378  445  GLU B C   
12355 O O   . GLU B 447  ? 0.2615 0.3147 0.2139 -0.0722 0.0172  0.0361  445  GLU B O   
12356 C CB  . GLU B 447  ? 0.2718 0.3156 0.2096 -0.0746 0.0179  0.0410  445  GLU B CB  
12357 C CG  . GLU B 447  ? 0.2631 0.2994 0.2009 -0.0710 0.0151  0.0381  445  GLU B CG  
12358 C CD  . GLU B 447  ? 0.2709 0.2999 0.2026 -0.0689 0.0139  0.0381  445  GLU B CD  
12359 O OE1 . GLU B 447  ? 0.2981 0.3269 0.2253 -0.0708 0.0149  0.0406  445  GLU B OE1 
12360 O OE2 . GLU B 447  ? 0.2727 0.2965 0.2043 -0.0655 0.0119  0.0357  445  GLU B OE2 
12361 N N   . PHE B 448  ? 0.2622 0.3249 0.2120 -0.0700 0.0220  0.0369  446  PHE B N   
12362 C CA  . PHE B 448  ? 0.2461 0.3119 0.1993 -0.0651 0.0226  0.0335  446  PHE B CA  
12363 C C   . PHE B 448  ? 0.2224 0.2819 0.1712 -0.0611 0.0217  0.0316  446  PHE B C   
12364 O O   . PHE B 448  ? 0.2562 0.3106 0.1994 -0.0619 0.0212  0.0330  446  PHE B O   
12365 C CB  . PHE B 448  ? 0.2933 0.3703 0.2497 -0.0640 0.0262  0.0335  446  PHE B CB  
12366 C CG  . PHE B 448  ? 0.2560 0.3403 0.2178 -0.0677 0.0269  0.0352  446  PHE B CG  
12367 C CD1 . PHE B 448  ? 0.2908 0.3774 0.2582 -0.0669 0.0258  0.0336  446  PHE B CD1 
12368 C CD2 . PHE B 448  ? 0.2914 0.3799 0.2523 -0.0721 0.0286  0.0385  446  PHE B CD2 
12369 C CE1 . PHE B 448  ? 0.2759 0.3693 0.2482 -0.0704 0.0263  0.0352  446  PHE B CE1 
12370 C CE2 . PHE B 448  ? 0.3476 0.4430 0.3136 -0.0757 0.0291  0.0402  446  PHE B CE2 
12371 C CZ  . PHE B 448  ? 0.3046 0.4024 0.2763 -0.0749 0.0279  0.0385  446  PHE B CZ  
12372 N N   . GLN B 449  ? 0.2428 0.3023 0.1941 -0.0568 0.0212  0.0284  447  GLN B N   
12373 C CA  . GLN B 449  ? 0.2319 0.2867 0.1796 -0.0528 0.0206  0.0263  447  GLN B CA  
12374 C C   . GLN B 449  ? 0.2397 0.3002 0.1906 -0.0485 0.0224  0.0235  447  GLN B C   
12375 O O   . GLN B 449  ? 0.2355 0.3015 0.1917 -0.0481 0.0231  0.0227  447  GLN B O   
12376 C CB  . GLN B 449  ? 0.2304 0.2758 0.1771 -0.0519 0.0171  0.0251  447  GLN B CB  
12377 C CG  . GLN B 449  ? 0.2625 0.3014 0.2063 -0.0558 0.0151  0.0277  447  GLN B CG  
12378 C CD  . GLN B 449  ? 0.2408 0.2703 0.1820 -0.0541 0.0120  0.0266  447  GLN B CD  
12379 O OE1 . GLN B 449  ? 0.2886 0.3169 0.2315 -0.0504 0.0113  0.0239  447  GLN B OE1 
12380 N NE2 . GLN B 449  ? 0.2648 0.2877 0.2021 -0.0567 0.0103  0.0288  447  GLN B NE2 
12381 N N   . CYS B 450  ? 0.2353 0.2942 0.1825 -0.0452 0.0231  0.0221  448  CYS B N   
12382 C CA  . CYS B 450  ? 0.2380 0.3010 0.1873 -0.0409 0.0246  0.0193  448  CYS B CA  
12383 C C   . CYS B 450  ? 0.2350 0.2915 0.1801 -0.0377 0.0232  0.0173  448  CYS B C   
12384 O O   . CYS B 450  ? 0.2587 0.3088 0.1993 -0.0388 0.0215  0.0183  448  CYS B O   
12385 C CB  . CYS B 450  ? 0.2381 0.3099 0.1876 -0.0405 0.0284  0.0199  448  CYS B CB  
12386 S SG  . CYS B 450  ? 0.2837 0.3540 0.2253 -0.0406 0.0300  0.0211  448  CYS B SG  
12387 N N   . LEU B 451  ? 0.2489 0.3075 0.1956 -0.0337 0.0240  0.0146  449  LEU B N   
12388 C CA  . LEU B 451  ? 0.2644 0.3176 0.2075 -0.0305 0.0228  0.0124  449  LEU B CA  
12389 C C   . LEU B 451  ? 0.3003 0.3559 0.2388 -0.0291 0.0253  0.0123  449  LEU B C   
12390 O O   . LEU B 451  ? 0.3073 0.3700 0.2472 -0.0284 0.0283  0.0122  449  LEU B O   
12391 C CB  . LEU B 451  ? 0.2776 0.3311 0.2249 -0.0270 0.0223  0.0095  449  LEU B CB  
12392 C CG  . LEU B 451  ? 0.3233 0.3716 0.2680 -0.0236 0.0209  0.0070  449  LEU B CG  
12393 C CD1 . LEU B 451  ? 0.3255 0.3656 0.2673 -0.0247 0.0176  0.0076  449  LEU B CD1 
12394 C CD2 . LEU B 451  ? 0.3688 0.4186 0.3183 -0.0207 0.0207  0.0045  449  LEU B CD2 
12395 N N   . HIS B 452  ? 0.2551 0.3047 0.1878 -0.0287 0.0239  0.0122  450  HIS B N   
12396 C CA  . HIS B 452  ? 0.2920 0.3429 0.2197 -0.0270 0.0258  0.0116  450  HIS B CA  
12397 C C   . HIS B 452  ? 0.2952 0.3499 0.2249 -0.0231 0.0276  0.0086  450  HIS B C   
12398 O O   . HIS B 452  ? 0.3215 0.3741 0.2544 -0.0208 0.0261  0.0065  450  HIS B O   
12399 C CB  . HIS B 452  ? 0.2701 0.3131 0.1922 -0.0264 0.0232  0.0111  450  HIS B CB  
12400 C CG  . HIS B 452  ? 0.2962 0.3395 0.2129 -0.0241 0.0247  0.0099  450  HIS B CG  
12401 N ND1 . HIS B 452  ? 0.3421 0.3873 0.2536 -0.0257 0.0267  0.0117  450  HIS B ND1 
12402 C CD2 . HIS B 452  ? 0.3319 0.3739 0.2473 -0.0205 0.0247  0.0069  450  HIS B CD2 
12403 C CE1 . HIS B 452  ? 0.3560 0.4008 0.2630 -0.0231 0.0277  0.0098  450  HIS B CE1 
12404 N NE2 . HIS B 452  ? 0.3142 0.3570 0.2234 -0.0199 0.0265  0.0068  450  HIS B NE2 
12405 N N   . GLY B 453  ? 0.3666 0.4266 0.2942 -0.0221 0.0309  0.0086  451  GLY B N   
12406 C CA  . GLY B 453  ? 0.4635 0.5264 0.3921 -0.0180 0.0327  0.0056  451  GLY B CA  
12407 C C   . GLY B 453  ? 0.5103 0.5784 0.4462 -0.0168 0.0335  0.0047  451  GLY B C   
12408 O O   . GLY B 453  ? 0.5032 0.5721 0.4404 -0.0132 0.0342  0.0021  451  GLY B O   
12409 N N   . MET B 454  ? 0.3550 0.4261 0.2953 -0.0197 0.0333  0.0069  452  MET B N   
12410 C CA  . MET B 454  ? 0.3613 0.4383 0.3086 -0.0190 0.0342  0.0064  452  MET B CA  
12411 C C   . MET B 454  ? 0.3512 0.4349 0.3011 -0.0225 0.0360  0.0094  452  MET B C   
12412 O O   . MET B 454  ? 0.3650 0.4567 0.3186 -0.0217 0.0386  0.0095  452  MET B O   
12413 C CB  . MET B 454  ? 0.3001 0.3726 0.2512 -0.0191 0.0310  0.0056  452  MET B CB  
12414 C CG  . MET B 454  ? 0.3588 0.4370 0.3169 -0.0189 0.0315  0.0055  452  MET B CG  
12415 S SD  . MET B 454  ? 0.4677 0.5529 0.4282 -0.0144 0.0347  0.0033  452  MET B SD  
12416 C CE  . MET B 454  ? 0.4870 0.5643 0.4445 -0.0104 0.0328  0.0000  452  MET B CE  
12417 N N   . GLY B 455  ? 0.2953 0.3758 0.2432 -0.0266 0.0345  0.0119  453  GLY B N   
12418 C CA  . GLY B 455  ? 0.3166 0.4025 0.2675 -0.0305 0.0355  0.0148  453  GLY B CA  
12419 C C   . GLY B 455  ? 0.3569 0.4475 0.3046 -0.0324 0.0384  0.0170  453  GLY B C   
12420 O O   . GLY B 455  ? 0.3420 0.4385 0.2927 -0.0356 0.0397  0.0194  453  GLY B O   
12421 N N   . GLU B 456  ? 0.3644 0.4527 0.3059 -0.0307 0.0395  0.0163  454  GLU B N   
12422 C CA  . GLU B 456  ? 0.3807 0.4733 0.3185 -0.0326 0.0424  0.0186  454  GLU B CA  
12423 C C   . GLU B 456  ? 0.3855 0.4889 0.3276 -0.0321 0.0462  0.0191  454  GLU B C   
12424 O O   . GLU B 456  ? 0.3898 0.4982 0.3324 -0.0357 0.0478  0.0221  454  GLU B O   
12425 C CB  . GLU B 456  ? 0.4446 0.5328 0.3748 -0.0305 0.0428  0.0175  454  GLU B CB  
12426 C CG  . GLU B 456  ? 0.5123 0.5908 0.4377 -0.0320 0.0393  0.0180  454  GLU B CG  
12427 C CD  . GLU B 456  ? 0.5076 0.5797 0.4332 -0.0287 0.0365  0.0149  454  GLU B CD  
12428 O OE1 . GLU B 456  ? 0.4790 0.5537 0.4099 -0.0263 0.0367  0.0129  454  GLU B OE1 
12429 O OE2 . GLU B 456  ? 0.4083 0.4731 0.3289 -0.0285 0.0342  0.0146  454  GLU B OE2 
12430 N N   . PRO B 457  ? 0.3777 0.4854 0.3231 -0.0279 0.0477  0.0165  455  PRO B N   
12431 C CA  . PRO B 457  ? 0.3873 0.5058 0.3371 -0.0274 0.0514  0.0173  455  PRO B CA  
12432 C C   . PRO B 457  ? 0.4041 0.5281 0.3600 -0.0315 0.0512  0.0200  455  PRO B C   
12433 O O   . PRO B 457  ? 0.3721 0.5043 0.3296 -0.0335 0.0540  0.0223  455  PRO B O   
12434 C CB  . PRO B 457  ? 0.3809 0.5009 0.3337 -0.0221 0.0519  0.0139  455  PRO B CB  
12435 C CG  . PRO B 457  ? 0.4218 0.5324 0.3688 -0.0196 0.0500  0.0114  455  PRO B CG  
12436 C CD  . PRO B 457  ? 0.4163 0.5192 0.3610 -0.0233 0.0465  0.0129  455  PRO B CD  
12437 N N   . LEU B 458  ? 0.3703 0.4900 0.3295 -0.0329 0.0478  0.0199  456  LEU B N   
12438 C CA  . LEU B 458  ? 0.3108 0.4349 0.2753 -0.0372 0.0472  0.0224  456  LEU B CA  
12439 C C   . LEU B 458  ? 0.3341 0.4563 0.2950 -0.0423 0.0469  0.0258  456  LEU B C   
12440 O O   . LEU B 458  ? 0.3265 0.4558 0.2897 -0.0456 0.0487  0.0285  456  LEU B O   
12441 C CB  . LEU B 458  ? 0.3140 0.4333 0.2822 -0.0373 0.0435  0.0212  456  LEU B CB  
12442 C CG  . LEU B 458  ? 0.3049 0.4274 0.2781 -0.0418 0.0423  0.0236  456  LEU B CG  
12443 C CD1 . LEU B 458  ? 0.3608 0.4954 0.3399 -0.0419 0.0453  0.0247  456  LEU B CD1 
12444 C CD2 . LEU B 458  ? 0.3368 0.4539 0.3130 -0.0415 0.0388  0.0221  456  LEU B CD2 
12445 N N   . TYR B 459  ? 0.2849 0.3975 0.2399 -0.0431 0.0445  0.0257  457  TYR B N   
12446 C CA  . TYR B 459  ? 0.2806 0.3900 0.2324 -0.0481 0.0436  0.0290  457  TYR B CA  
12447 C C   . TYR B 459  ? 0.2896 0.4025 0.2366 -0.0493 0.0467  0.0310  457  TYR B C   
12448 O O   . TYR B 459  ? 0.3088 0.4215 0.2540 -0.0539 0.0466  0.0342  457  TYR B O   
12449 C CB  . TYR B 459  ? 0.2907 0.3885 0.2388 -0.0487 0.0396  0.0285  457  TYR B CB  
12450 C CG  . TYR B 459  ? 0.2857 0.3816 0.2391 -0.0498 0.0368  0.0280  457  TYR B CG  
12451 C CD1 . TYR B 459  ? 0.2719 0.3686 0.2276 -0.0547 0.0358  0.0307  457  TYR B CD1 
12452 C CD2 . TYR B 459  ? 0.2758 0.3692 0.2319 -0.0460 0.0352  0.0248  457  TYR B CD2 
12453 C CE1 . TYR B 459  ? 0.2705 0.3653 0.2307 -0.0558 0.0333  0.0301  457  TYR B CE1 
12454 C CE2 . TYR B 459  ? 0.2793 0.3711 0.2400 -0.0471 0.0328  0.0244  457  TYR B CE2 
12455 C CZ  . TYR B 459  ? 0.2390 0.3315 0.2017 -0.0519 0.0318  0.0270  457  TYR B CZ  
12456 O OH  . TYR B 459  ? 0.2699 0.3605 0.2367 -0.0531 0.0294  0.0265  457  TYR B OH  
12457 N N   . GLU B 460  ? 0.3255 0.4416 0.2702 -0.0452 0.0494  0.0291  458  GLU B N   
12458 C CA  . GLU B 460  ? 0.3354 0.4573 0.2767 -0.0461 0.0531  0.0310  458  GLU B CA  
12459 C C   . GLU B 460  ? 0.3964 0.5291 0.3436 -0.0490 0.0557  0.0335  458  GLU B C   
12460 O O   . GLU B 460  ? 0.3738 0.5110 0.3186 -0.0517 0.0583  0.0362  458  GLU B O   
12461 C CB  . GLU B 460  ? 0.3949 0.5183 0.3330 -0.0408 0.0556  0.0281  458  GLU B CB  
12462 N N   . GLU B 461  ? 0.3648 0.5018 0.3195 -0.0487 0.0550  0.0328  459  GLU B N   
12463 C CA  . GLU B 461  ? 0.3797 0.5269 0.3408 -0.0518 0.0568  0.0353  459  GLU B CA  
12464 C C   . GLU B 461  ? 0.4014 0.5456 0.3641 -0.0577 0.0541  0.0381  459  GLU B C   
12465 O O   . GLU B 461  ? 0.3408 0.4926 0.3093 -0.0607 0.0548  0.0401  459  GLU B O   
12466 C CB  . GLU B 461  ? 0.3395 0.4934 0.3079 -0.0483 0.0575  0.0331  459  GLU B CB  
12467 C CG  . GLU B 461  ? 0.3667 0.5221 0.3337 -0.0421 0.0598  0.0299  459  GLU B CG  
12468 C CD  . GLU B 461  ? 0.4851 0.6478 0.4495 -0.0412 0.0643  0.0309  459  GLU B CD  
12469 O OE1 . GLU B 461  ? 0.4580 0.6276 0.4241 -0.0453 0.0662  0.0342  459  GLU B OE1 
12470 O OE2 . GLU B 461  ? 0.5172 0.6786 0.4776 -0.0366 0.0660  0.0284  459  GLU B OE2 
12471 N N   . VAL B 462  ? 0.3654 0.4987 0.3232 -0.0593 0.0508  0.0383  460  VAL B N   
12472 C CA  . VAL B 462  ? 0.3317 0.4603 0.2905 -0.0644 0.0477  0.0405  460  VAL B CA  
12473 C C   . VAL B 462  ? 0.3298 0.4523 0.2818 -0.0681 0.0471  0.0433  460  VAL B C   
12474 O O   . VAL B 462  ? 0.3634 0.4880 0.3160 -0.0733 0.0473  0.0467  460  VAL B O   
12475 C CB  . VAL B 462  ? 0.3034 0.4238 0.2637 -0.0627 0.0436  0.0380  460  VAL B CB  
12476 C CG1 . VAL B 462  ? 0.3216 0.4359 0.2819 -0.0678 0.0404  0.0401  460  VAL B CG1 
12477 C CG2 . VAL B 462  ? 0.3400 0.4666 0.3073 -0.0596 0.0441  0.0356  460  VAL B CG2 
12478 N N   . VAL B 463  ? 0.3154 0.4303 0.2607 -0.0656 0.0464  0.0420  461  VAL B N   
12479 C CA  . VAL B 463  ? 0.3194 0.4278 0.2577 -0.0687 0.0456  0.0445  461  VAL B CA  
12480 C C   . VAL B 463  ? 0.3425 0.4585 0.2784 -0.0704 0.0496  0.0471  461  VAL B C   
12481 O O   . VAL B 463  ? 0.3777 0.5010 0.3143 -0.0671 0.0530  0.0457  461  VAL B O   
12482 C CB  . VAL B 463  ? 0.3197 0.4184 0.2519 -0.0651 0.0435  0.0422  461  VAL B CB  
12483 C CG1 . VAL B 463  ? 0.4015 0.4937 0.3263 -0.0680 0.0427  0.0449  461  VAL B CG1 
12484 C CG2 . VAL B 463  ? 0.3208 0.4123 0.2556 -0.0636 0.0396  0.0399  461  VAL B CG2 
12485 N N   . GLY B 464  ? 0.3835 0.4976 0.3165 -0.0756 0.0493  0.0508  462  GLY B N   
12486 C CA  . GLY B 464  ? 0.3913 0.5115 0.3210 -0.0775 0.0530  0.0536  462  GLY B CA  
12487 C C   . GLY B 464  ? 0.4372 0.5660 0.3721 -0.0825 0.0547  0.0569  462  GLY B C   
12488 O O   . GLY B 464  ? 0.3988 0.5332 0.3411 -0.0828 0.0545  0.0562  462  GLY B O   
12489 N N   . ARG B 465  ? 0.4317 0.5618 0.3625 -0.0867 0.0564  0.0607  463  ARG B N   
12490 C CA  . ARG B 465  ? 0.4868 0.6252 0.4222 -0.0921 0.0581  0.0643  463  ARG B CA  
12491 C C   . ARG B 465  ? 0.4859 0.6380 0.4279 -0.0900 0.0620  0.0634  463  ARG B C   
12492 O O   . ARG B 465  ? 0.5645 0.7241 0.5133 -0.0933 0.0625  0.0652  463  ARG B O   
12493 C CB  . ARG B 465  ? 0.5569 0.6943 0.4859 -0.0965 0.0596  0.0684  463  ARG B CB  
12494 N N   . GLY B 466  ? 0.4532 0.6086 0.3936 -0.0844 0.0647  0.0607  464  GLY B N   
12495 C CA  . GLY B 466  ? 0.5228 0.6907 0.4693 -0.0814 0.0684  0.0595  464  GLY B CA  
12496 C C   . GLY B 466  ? 0.5349 0.7041 0.4882 -0.0777 0.0668  0.0560  464  GLY B C   
12497 O O   . GLY B 466  ? 0.4985 0.6775 0.4569 -0.0745 0.0696  0.0547  464  GLY B O   
12498 N N   . LYS B 467  ? 0.4458 0.6053 0.3991 -0.0778 0.0623  0.0546  465  LYS B N   
12499 C CA  . LYS B 467  ? 0.4253 0.5854 0.3849 -0.0749 0.0604  0.0516  465  LYS B CA  
12500 C C   . LYS B 467  ? 0.4517 0.6094 0.4155 -0.0798 0.0570  0.0533  465  LYS B C   
12501 O O   . LYS B 467  ? 0.4472 0.6113 0.4143 -0.0847 0.0580  0.0565  465  LYS B O   
12502 C CB  . LYS B 467  ? 0.3698 0.5205 0.3255 -0.0696 0.0582  0.0477  465  LYS B CB  
12503 C CG  . LYS B 467  ? 0.4584 0.6107 0.4095 -0.0647 0.0614  0.0457  465  LYS B CG  
12504 C CD  . LYS B 467  ? 0.4744 0.6383 0.4313 -0.0611 0.0649  0.0443  465  LYS B CD  
12505 C CE  . LYS B 467  ? 0.4583 0.6239 0.4104 -0.0561 0.0683  0.0422  465  LYS B CE  
12506 N NZ  . LYS B 467  ? 0.5043 0.6790 0.4621 -0.0515 0.0710  0.0399  465  LYS B NZ  
12507 N N   . LEU B 468  ? 0.3857 0.5344 0.3496 -0.0786 0.0531  0.0511  466  LEU B N   
12508 C CA  . LEU B 468  ? 0.3752 0.5206 0.3423 -0.0832 0.0497  0.0525  466  LEU B CA  
12509 C C   . LEU B 468  ? 0.3647 0.4998 0.3256 -0.0875 0.0472  0.0548  466  LEU B C   
12510 O O   . LEU B 468  ? 0.3632 0.4948 0.3259 -0.0919 0.0445  0.0563  466  LEU B O   
12511 C CB  . LEU B 468  ? 0.3788 0.5205 0.3497 -0.0802 0.0468  0.0492  466  LEU B CB  
12512 C CG  . LEU B 468  ? 0.3902 0.5413 0.3674 -0.0757 0.0488  0.0468  466  LEU B CG  
12513 C CD1 . LEU B 468  ? 0.4085 0.5552 0.3890 -0.0733 0.0456  0.0439  466  LEU B CD1 
12514 C CD2 . LEU B 468  ? 0.3994 0.5633 0.3828 -0.0789 0.0514  0.0494  466  LEU B CD2 
12515 N N   . ASP B 469  ? 0.3343 0.4642 0.2879 -0.0863 0.0480  0.0551  467  ASP B N   
12516 C CA  . ASP B 469  ? 0.4105 0.5305 0.3577 -0.0900 0.0457  0.0574  467  ASP B CA  
12517 C C   . ASP B 469  ? 0.3357 0.4448 0.2827 -0.0901 0.0410  0.0559  467  ASP B C   
12518 O O   . ASP B 469  ? 0.3544 0.4577 0.3002 -0.0947 0.0386  0.0582  467  ASP B O   
12519 C CB  . ASP B 469  ? 0.4082 0.5323 0.3555 -0.0965 0.0469  0.0620  467  ASP B CB  
12520 C CG  . ASP B 469  ? 0.5168 0.6325 0.4562 -0.0995 0.0460  0.0647  467  ASP B CG  
12521 O OD1 . ASP B 469  ? 0.5094 0.6174 0.4428 -0.0961 0.0450  0.0631  467  ASP B OD1 
12522 O OD2 . ASP B 469  ? 0.5292 0.6456 0.4681 -0.1053 0.0460  0.0685  467  ASP B OD2 
12523 N N   . ARG B 470  ? 0.3819 0.4883 0.3301 -0.0849 0.0398  0.0521  468  ARG B N   
12524 C CA  . ARG B 470  ? 0.3604 0.4568 0.3083 -0.0840 0.0357  0.0503  468  ARG B CA  
12525 C C   . ARG B 470  ? 0.3416 0.4306 0.2843 -0.0792 0.0348  0.0477  468  ARG B C   
12526 O O   . ARG B 470  ? 0.3274 0.4207 0.2699 -0.0749 0.0370  0.0456  468  ARG B O   
12527 C CB  . ARG B 470  ? 0.3244 0.4245 0.2795 -0.0824 0.0348  0.0479  468  ARG B CB  
12528 C CG  . ARG B 470  ? 0.3335 0.4404 0.2942 -0.0873 0.0350  0.0501  468  ARG B CG  
12529 C CD  . ARG B 470  ? 0.2990 0.3983 0.2571 -0.0929 0.0323  0.0529  468  ARG B CD  
12530 N NE  . ARG B 470  ? 0.3525 0.4581 0.3158 -0.0980 0.0323  0.0551  468  ARG B NE  
12531 C CZ  . ARG B 470  ? 0.4162 0.5276 0.3795 -0.1025 0.0344  0.0587  468  ARG B CZ  
12532 N NH1 . ARG B 470  ? 0.4051 0.5174 0.3635 -0.1026 0.0368  0.0605  468  ARG B NH1 
12533 N NH2 . ARG B 470  ? 0.4123 0.5290 0.3806 -0.1072 0.0340  0.0606  468  ARG B NH2 
12534 N N   . PRO B 471  ? 0.3168 0.3949 0.2553 -0.0799 0.0315  0.0479  469  PRO B N   
12535 C CA  . PRO B 471  ? 0.3147 0.3859 0.2482 -0.0757 0.0304  0.0458  469  PRO B CA  
12536 C C   . PRO B 471  ? 0.2834 0.3534 0.2204 -0.0710 0.0291  0.0418  469  PRO B C   
12537 O O   . PRO B 471  ? 0.2734 0.3448 0.2158 -0.0713 0.0279  0.0408  469  PRO B O   
12538 C CB  . PRO B 471  ? 0.3185 0.3789 0.2472 -0.0785 0.0271  0.0477  469  PRO B CB  
12539 C CG  . PRO B 471  ? 0.3516 0.4114 0.2846 -0.0823 0.0254  0.0487  469  PRO B CG  
12540 C CD  . PRO B 471  ? 0.3429 0.4143 0.2809 -0.0845 0.0285  0.0500  469  PRO B CD  
12541 N N   . CYS B 472  ? 0.2791 0.3462 0.2126 -0.0666 0.0291  0.0396  470  CYS B N   
12542 C CA  . CYS B 472  ? 0.2735 0.3386 0.2096 -0.0621 0.0278  0.0359  470  CYS B CA  
12543 C C   . CYS B 472  ? 0.2673 0.3235 0.1977 -0.0596 0.0257  0.0347  470  CYS B C   
12544 O O   . CYS B 472  ? 0.2902 0.3457 0.2152 -0.0590 0.0268  0.0355  470  CYS B O   
12545 C CB  . CYS B 472  ? 0.3073 0.3812 0.2466 -0.0585 0.0308  0.0337  470  CYS B CB  
12546 S SG  . CYS B 472  ? 0.3142 0.3855 0.2566 -0.0531 0.0292  0.0293  470  CYS B SG  
12547 N N   . ARG B 473  ? 0.2662 0.3157 0.1979 -0.0582 0.0225  0.0330  471  ARG B N   
12548 C CA  . ARG B 473  ? 0.2623 0.3038 0.1898 -0.0555 0.0203  0.0316  471  ARG B CA  
12549 C C   . ARG B 473  ? 0.2571 0.3004 0.1867 -0.0506 0.0206  0.0280  471  ARG B C   
12550 O O   . ARG B 473  ? 0.2917 0.3372 0.2267 -0.0493 0.0204  0.0261  471  ARG B O   
12551 C CB  . ARG B 473  ? 0.2534 0.2864 0.1809 -0.0569 0.0166  0.0321  471  ARG B CB  
12552 C CG  . ARG B 473  ? 0.2721 0.2970 0.1952 -0.0544 0.0142  0.0311  471  ARG B CG  
12553 C CD  . ARG B 473  ? 0.2478 0.2642 0.1704 -0.0559 0.0108  0.0319  471  ARG B CD  
12554 N NE  . ARG B 473  ? 0.2736 0.2889 0.1950 -0.0607 0.0108  0.0353  471  ARG B NE  
12555 C CZ  . ARG B 473  ? 0.3047 0.3166 0.2206 -0.0630 0.0106  0.0381  471  ARG B CZ  
12556 N NH1 . ARG B 473  ? 0.2997 0.3083 0.2106 -0.0609 0.0100  0.0380  471  ARG B NH1 
12557 N NH2 . ARG B 473  ? 0.3260 0.3379 0.2412 -0.0676 0.0109  0.0412  471  ARG B NH2 
12558 N N   . ILE B 474  ? 0.2650 0.3070 0.1901 -0.0480 0.0212  0.0270  472  ILE B N   
12559 C CA  . ILE B 474  ? 0.2553 0.2985 0.1815 -0.0434 0.0216  0.0236  472  ILE B CA  
12560 C C   . ILE B 474  ? 0.2676 0.3028 0.1931 -0.0414 0.0182  0.0219  472  ILE B C   
12561 O O   . ILE B 474  ? 0.2730 0.3019 0.1936 -0.0419 0.0163  0.0229  472  ILE B O   
12562 C CB  . ILE B 474  ? 0.2616 0.3075 0.1829 -0.0417 0.0240  0.0233  472  ILE B CB  
12563 C CG1 . ILE B 474  ? 0.2636 0.3184 0.1863 -0.0435 0.0277  0.0248  472  ILE B CG1 
12564 C CG2 . ILE B 474  ? 0.2681 0.3138 0.1898 -0.0371 0.0240  0.0197  472  ILE B CG2 
12565 C CD1 . ILE B 474  ? 0.3087 0.3661 0.2259 -0.0423 0.0304  0.0250  472  ILE B CD1 
12566 N N   . TYR B 475  ? 0.2407 0.2762 0.1710 -0.0391 0.0173  0.0195  473  TYR B N   
12567 C CA  . TYR B 475  ? 0.2500 0.2790 0.1803 -0.0367 0.0144  0.0175  473  TYR B CA  
12568 C C   . TYR B 475  ? 0.2580 0.2869 0.1851 -0.0333 0.0150  0.0155  473  TYR B C   
12569 O O   . TYR B 475  ? 0.2654 0.2995 0.1944 -0.0310 0.0172  0.0136  473  TYR B O   
12570 C CB  . TYR B 475  ? 0.2587 0.2888 0.1952 -0.0356 0.0137  0.0158  473  TYR B CB  
12571 C CG  . TYR B 475  ? 0.2551 0.2788 0.1924 -0.0337 0.0108  0.0141  473  TYR B CG  
12572 C CD1 . TYR B 475  ? 0.2720 0.2950 0.2095 -0.0300 0.0104  0.0114  473  TYR B CD1 
12573 C CD2 . TYR B 475  ? 0.2578 0.2763 0.1957 -0.0355 0.0083  0.0152  473  TYR B CD2 
12574 C CE1 . TYR B 475  ? 0.2636 0.2813 0.2022 -0.0283 0.0078  0.0100  473  TYR B CE1 
12575 C CE2 . TYR B 475  ? 0.2397 0.2527 0.1786 -0.0336 0.0058  0.0137  473  TYR B CE2 
12576 C CZ  . TYR B 475  ? 0.2833 0.2963 0.2227 -0.0300 0.0056  0.0112  473  TYR B CZ  
12577 O OH  . TYR B 475  ? 0.2936 0.3017 0.2341 -0.0282 0.0032  0.0098  473  TYR B OH  
12578 N N   . ALA B 476  ? 0.2509 0.2739 0.1732 -0.0329 0.0131  0.0158  474  ALA B N   
12579 C CA  . ALA B 476  ? 0.2881 0.3107 0.2059 -0.0305 0.0137  0.0144  474  ALA B CA  
12580 C C   . ALA B 476  ? 0.2755 0.2925 0.1931 -0.0279 0.0108  0.0123  474  ALA B C   
12581 O O   . ALA B 476  ? 0.2689 0.2799 0.1838 -0.0286 0.0081  0.0134  474  ALA B O   
12582 C CB  . ALA B 476  ? 0.3093 0.3304 0.2206 -0.0326 0.0141  0.0170  474  ALA B CB  
12583 N N   . PRO B 477  ? 0.2834 0.3021 0.2040 -0.0248 0.0112  0.0094  475  PRO B N   
12584 C CA  . PRO B 477  ? 0.2900 0.3039 0.2102 -0.0224 0.0086  0.0074  475  PRO B CA  
12585 C C   . PRO B 477  ? 0.2875 0.2986 0.2012 -0.0217 0.0080  0.0074  475  PRO B C   
12586 O O   . PRO B 477  ? 0.2929 0.3069 0.2029 -0.0217 0.0102  0.0075  475  PRO B O   
12587 C CB  . PRO B 477  ? 0.3081 0.3255 0.2323 -0.0196 0.0099  0.0046  475  PRO B CB  
12588 C CG  . PRO B 477  ? 0.3110 0.3344 0.2391 -0.0208 0.0124  0.0053  475  PRO B CG  
12589 C CD  . PRO B 477  ? 0.2830 0.3082 0.2075 -0.0236 0.0139  0.0080  475  PRO B CD  
12590 N N   . VAL B 478  ? 0.2753 0.2806 0.1875 -0.0212 0.0048  0.0073  476  VAL B N   
12591 C CA  . VAL B 478  ? 0.2828 0.2848 0.1889 -0.0206 0.0035  0.0074  476  VAL B CA  
12592 C C   . VAL B 478  ? 0.3244 0.3230 0.2320 -0.0182 0.0010  0.0051  476  VAL B C   
12593 O O   . VAL B 478  ? 0.3445 0.3402 0.2556 -0.0181 -0.0013 0.0052  476  VAL B O   
12594 C CB  . VAL B 478  ? 0.3004 0.2984 0.2028 -0.0231 0.0018  0.0105  476  VAL B CB  
12595 C CG1 . VAL B 478  ? 0.3392 0.3338 0.2352 -0.0225 0.0003  0.0106  476  VAL B CG1 
12596 C CG2 . VAL B 478  ? 0.3039 0.3053 0.2054 -0.0260 0.0043  0.0130  476  VAL B CG2 
12597 N N   . GLY B 479  ? 0.3771 0.3760 0.2819 -0.0162 0.0013  0.0029  477  GLY B N   
12598 C CA  . GLY B 479  ? 0.4271 0.4227 0.3329 -0.0142 -0.0012 0.0009  477  GLY B CA  
12599 C C   . GLY B 479  ? 0.4028 0.3997 0.3066 -0.0119 -0.0001 -0.0019 477  GLY B C   
12600 O O   . GLY B 479  ? 0.3767 0.3772 0.2785 -0.0116 0.0028  -0.0024 477  GLY B O   
12601 N N   . THR B 480  ? 0.4854 0.4793 0.3900 -0.0103 -0.0026 -0.0037 478  THR B N   
12602 C CA  . THR B 480  ? 0.5403 0.5340 0.4426 -0.0083 -0.0023 -0.0064 478  THR B CA  
12603 C C   . THR B 480  ? 0.5668 0.5637 0.4738 -0.0066 -0.0002 -0.0085 478  THR B C   
12604 O O   . THR B 480  ? 0.5889 0.5882 0.5012 -0.0069 0.0007  -0.0079 478  THR B O   
12605 C CB  . THR B 480  ? 0.4966 0.4859 0.3984 -0.0076 -0.0060 -0.0073 478  THR B CB  
12606 O OG1 . THR B 480  ? 0.7017 0.6905 0.6102 -0.0072 -0.0074 -0.0075 478  THR B OG1 
12607 C CG2 . THR B 480  ? 0.5400 0.5261 0.4375 -0.0092 -0.0083 -0.0050 478  THR B CG2 
12608 N N   . HIS B 481  ? 0.6662 0.6628 0.5710 -0.0046 0.0003  -0.0111 479  HIS B N   
12609 C CA  . HIS B 481  ? 0.6543 0.6535 0.5630 -0.0027 0.0022  -0.0132 479  HIS B CA  
12610 C C   . HIS B 481  ? 0.7029 0.7011 0.6181 -0.0023 0.0005  -0.0137 479  HIS B C   
12611 O O   . HIS B 481  ? 0.6647 0.6660 0.5849 -0.0019 0.0020  -0.0138 479  HIS B O   
12612 C CB  . HIS B 481  ? 0.5932 0.5909 0.4976 -0.0007 0.0026  -0.0160 479  HIS B CB  
12613 C CG  . HIS B 481  ? 0.6171 0.6164 0.5153 -0.0006 0.0050  -0.0159 479  HIS B CG  
12614 N ND1 . HIS B 481  ? 0.6761 0.6746 0.5699 0.0013  0.0061  -0.0184 479  HIS B ND1 
12615 C CD2 . HIS B 481  ? 0.5670 0.5687 0.4625 -0.0023 0.0066  -0.0136 479  HIS B CD2 
12616 C CE1 . HIS B 481  ? 0.6901 0.6905 0.5787 0.0010  0.0084  -0.0177 479  HIS B CE1 
12617 N NE2 . HIS B 481  ? 0.7022 0.7047 0.5917 -0.0013 0.0087  -0.0148 479  HIS B NE2 
12618 N N   . GLU B 482  ? 0.6882 0.6824 0.6034 -0.0023 -0.0028 -0.0140 480  GLU B N   
12619 C CA  . GLU B 482  ? 0.6610 0.6544 0.5823 -0.0018 -0.0044 -0.0145 480  GLU B CA  
12620 C C   . GLU B 482  ? 0.5971 0.5922 0.5230 -0.0031 -0.0040 -0.0125 480  GLU B C   
12621 O O   . GLU B 482  ? 0.7011 0.6975 0.6323 -0.0025 -0.0037 -0.0130 480  GLU B O   
12622 C CB  . GLU B 482  ? 0.7158 0.7051 0.6361 -0.0019 -0.0079 -0.0148 480  GLU B CB  
12623 N N   . THR B 483  ? 0.6629 0.6578 0.5865 -0.0050 -0.0041 -0.0101 481  THR B N   
12624 C CA  . THR B 483  ? 0.6803 0.6761 0.6077 -0.0064 -0.0041 -0.0082 481  THR B CA  
12625 C C   . THR B 483  ? 0.6801 0.6805 0.6098 -0.0067 -0.0010 -0.0080 481  THR B C   
12626 O O   . THR B 483  ? 0.7171 0.7189 0.6518 -0.0070 -0.0007 -0.0077 481  THR B O   
12627 C CB  . THR B 483  ? 0.7388 0.7322 0.6628 -0.0083 -0.0055 -0.0057 481  THR B CB  
12628 O OG1 . THR B 483  ? 0.7811 0.7707 0.7025 -0.0079 -0.0083 -0.0060 481  THR B OG1 
12629 C CG2 . THR B 483  ? 0.7299 0.7228 0.6578 -0.0096 -0.0062 -0.0040 481  THR B CG2 
12630 N N   . LEU B 484  ? 0.6443 0.6474 0.5705 -0.0067 0.0014  -0.0081 482  LEU B N   
12631 C CA  . LEU B 484  ? 0.6199 0.6282 0.5487 -0.0070 0.0044  -0.0077 482  LEU B CA  
12632 C C   . LEU B 484  ? 0.5915 0.6019 0.5248 -0.0049 0.0053  -0.0098 482  LEU B C   
12633 O O   . LEU B 484  ? 0.5652 0.5790 0.5029 -0.0052 0.0067  -0.0094 482  LEU B O   
12634 C CB  . LEU B 484  ? 0.5884 0.5994 0.5124 -0.0073 0.0069  -0.0073 482  LEU B CB  
12635 C CG  . LEU B 484  ? 0.5854 0.5970 0.5060 -0.0050 0.0083  -0.0096 482  LEU B CG  
12636 C CD1 . LEU B 484  ? 0.5622 0.5786 0.4865 -0.0033 0.0111  -0.0110 482  LEU B CD1 
12637 C CD2 . LEU B 484  ? 0.5623 0.5740 0.4763 -0.0057 0.0093  -0.0088 482  LEU B CD2 
12638 N N   . LEU B 485  ? 0.5610 0.5694 0.4934 -0.0028 0.0046  -0.0121 483  LEU B N   
12639 C CA  . LEU B 485  ? 0.6459 0.6558 0.5824 -0.0008 0.0054  -0.0140 483  LEU B CA  
12640 C C   . LEU B 485  ? 0.5843 0.5937 0.5265 -0.0011 0.0040  -0.0137 483  LEU B C   
12641 O O   . LEU B 485  ? 0.5743 0.5861 0.5206 0.0000  0.0050  -0.0145 483  LEU B O   
12642 C CB  . LEU B 485  ? 0.5853 0.5922 0.5191 0.0012  0.0045  -0.0164 483  LEU B CB  
12643 C CG  . LEU B 485  ? 0.5305 0.5384 0.4592 0.0024  0.0065  -0.0176 483  LEU B CG  
12644 C CD1 . LEU B 485  ? 0.5471 0.5508 0.4728 0.0040  0.0049  -0.0199 483  LEU B CD1 
12645 C CD2 . LEU B 485  ? 0.5654 0.5783 0.4965 0.0038  0.0097  -0.0182 483  LEU B CD2 
12646 N N   . ALA B 486  ? 0.5771 0.5834 0.5194 -0.0026 0.0016  -0.0123 484  ALA B N   
12647 C CA  . ALA B 486  ? 0.5135 0.5185 0.4607 -0.0026 0.0000  -0.0123 484  ALA B CA  
12648 C C   . ALA B 486  ? 0.6350 0.6435 0.5864 -0.0034 0.0015  -0.0115 484  ALA B C   
12649 O O   . ALA B 486  ? 0.6554 0.6639 0.6111 -0.0028 0.0009  -0.0121 484  ALA B O   
12650 C CB  . ALA B 486  ? 0.5930 0.5940 0.5392 -0.0038 -0.0026 -0.0110 484  ALA B CB  
12651 N N   . TYR B 487  ? 0.6188 0.6304 0.5691 -0.0048 0.0033  -0.0101 485  TYR B N   
12652 C CA  . TYR B 487  ? 0.5909 0.6060 0.5452 -0.0057 0.0046  -0.0092 485  TYR B CA  
12653 C C   . TYR B 487  ? 0.5818 0.6023 0.5356 -0.0059 0.0075  -0.0089 485  TYR B C   
12654 O O   . TYR B 487  ? 0.4352 0.4589 0.3914 -0.0075 0.0085  -0.0075 485  TYR B O   
12655 C CB  . TYR B 487  ? 0.5891 0.6024 0.5442 -0.0082 0.0032  -0.0072 485  TYR B CB  
12656 C CG  . TYR B 487  ? 0.6572 0.6662 0.6142 -0.0078 0.0007  -0.0076 485  TYR B CG  
12657 C CD1 . TYR B 487  ? 0.7043 0.7141 0.6659 -0.0070 0.0005  -0.0084 485  TYR B CD1 
12658 C CD2 . TYR B 487  ? 0.6501 0.6547 0.6044 -0.0080 -0.0014 -0.0071 485  TYR B CD2 
12659 C CE1 . TYR B 487  ? 0.6976 0.7038 0.6611 -0.0066 -0.0015 -0.0088 485  TYR B CE1 
12660 C CE2 . TYR B 487  ? 0.6579 0.6591 0.6143 -0.0075 -0.0035 -0.0074 485  TYR B CE2 
12661 C CZ  . TYR B 487  ? 0.7050 0.7071 0.6660 -0.0068 -0.0035 -0.0082 485  TYR B CZ  
12662 O OH  . TYR B 487  ? 0.7748 0.7739 0.7379 -0.0062 -0.0055 -0.0085 485  TYR B OH  
12663 N N   . LEU B 488  ? 0.5987 0.6201 0.5494 -0.0043 0.0088  -0.0101 486  LEU B N   
12664 C CA  . LEU B 488  ? 0.5402 0.5670 0.4907 -0.0040 0.0118  -0.0099 486  LEU B CA  
12665 C C   . LEU B 488  ? 0.5386 0.5696 0.4944 -0.0029 0.0130  -0.0105 486  LEU B C   
12666 O O   . LEU B 488  ? 0.3989 0.4351 0.3562 -0.0036 0.0151  -0.0096 486  LEU B O   
12667 C CB  . LEU B 488  ? 0.5413 0.5678 0.4873 -0.0021 0.0129  -0.0114 486  LEU B CB  
12668 C CG  . LEU B 488  ? 0.5246 0.5562 0.4688 -0.0017 0.0161  -0.0111 486  LEU B CG  
12669 C CD1 . LEU B 488  ? 0.4668 0.4959 0.4047 -0.0008 0.0163  -0.0120 486  LEU B CD1 
12670 C CD2 . LEU B 488  ? 0.5066 0.5426 0.4545 0.0008  0.0181  -0.0126 486  LEU B CD2 
12671 N N   . VAL B 489  ? 0.5183 0.5473 0.4768 -0.0012 0.0118  -0.0121 487  VAL B N   
12672 C CA  . VAL B 489  ? 0.4207 0.4533 0.3841 -0.0001 0.0127  -0.0126 487  VAL B CA  
12673 C C   . VAL B 489  ? 0.4532 0.4891 0.4197 -0.0026 0.0130  -0.0106 487  VAL B C   
12674 O O   . VAL B 489  ? 0.5926 0.6341 0.5612 -0.0026 0.0150  -0.0101 487  VAL B O   
12675 C CB  . VAL B 489  ? 0.4690 0.4981 0.4347 0.0014  0.0109  -0.0141 487  VAL B CB  
12676 C CG1 . VAL B 489  ? 0.4716 0.5043 0.4425 0.0021  0.0115  -0.0143 487  VAL B CG1 
12677 C CG2 . VAL B 489  ? 0.4801 0.5065 0.4431 0.0038  0.0108  -0.0162 487  VAL B CG2 
12678 N N   . ARG B 490  ? 0.5493 0.5819 0.5160 -0.0047 0.0110  -0.0095 488  ARG B N   
12679 C CA  . ARG B 490  ? 0.5706 0.6053 0.5398 -0.0072 0.0110  -0.0078 488  ARG B CA  
12680 C C   . ARG B 490  ? 0.5311 0.5696 0.4985 -0.0093 0.0127  -0.0059 488  ARG B C   
12681 O O   . ARG B 490  ? 0.5449 0.5873 0.5150 -0.0110 0.0135  -0.0047 488  ARG B O   
12682 C CB  . ARG B 490  ? 0.5310 0.5603 0.4999 -0.0088 0.0084  -0.0071 488  ARG B CB  
12683 C CG  . ARG B 490  ? 0.5184 0.5486 0.4895 -0.0115 0.0080  -0.0054 488  ARG B CG  
12684 C CD  . ARG B 490  ? 0.4987 0.5229 0.4683 -0.0129 0.0056  -0.0047 488  ARG B CD  
12685 N NE  . ARG B 490  ? 0.5165 0.5383 0.4816 -0.0141 0.0053  -0.0035 488  ARG B NE  
12686 C CZ  . ARG B 490  ? 0.4482 0.4645 0.4110 -0.0143 0.0033  -0.0032 488  ARG B CZ  
12687 N NH1 . ARG B 490  ? 0.4439 0.4568 0.4086 -0.0133 0.0015  -0.0040 488  ARG B NH1 
12688 N NH2 . ARG B 490  ? 0.3855 0.4000 0.3441 -0.0154 0.0031  -0.0019 488  ARG B NH2 
12689 N N   . ARG B 491  ? 0.4404 0.4779 0.4033 -0.0091 0.0134  -0.0058 489  ARG B N   
12690 C CA  . ARG B 491  ? 0.5637 0.6028 0.5240 -0.0118 0.0143  -0.0036 489  ARG B CA  
12691 C C   . ARG B 491  ? 0.4762 0.5222 0.4370 -0.0118 0.0174  -0.0031 489  ARG B C   
12692 O O   . ARG B 491  ? 0.4726 0.5235 0.4375 -0.0124 0.0184  -0.0025 489  ARG B O   
12693 C CB  . ARG B 491  ? 0.5987 0.6330 0.5533 -0.0119 0.0134  -0.0034 489  ARG B CB  
12694 N N   . LEU B 492  ? 0.4962 0.5428 0.4526 -0.0110 0.0188  -0.0032 490  LEU B N   
12695 C CA  . LEU B 492  ? 0.4712 0.5240 0.4271 -0.0117 0.0218  -0.0020 490  LEU B CA  
12696 C C   . LEU B 492  ? 0.5323 0.5916 0.4930 -0.0099 0.0238  -0.0029 490  LEU B C   
12697 O O   . LEU B 492  ? 0.4784 0.5439 0.4414 -0.0114 0.0256  -0.0013 490  LEU B O   
12698 C CB  . LEU B 492  ? 0.5352 0.5870 0.4853 -0.0105 0.0230  -0.0026 490  LEU B CB  
12699 N N   . LEU B 493  ? 0.4817 0.5398 0.4442 -0.0068 0.0233  -0.0052 491  LEU B N   
12700 C CA  . LEU B 493  ? 0.5101 0.5739 0.4767 -0.0044 0.0252  -0.0061 491  LEU B CA  
12701 C C   . LEU B 493  ? 0.4460 0.5115 0.4183 -0.0052 0.0240  -0.0057 491  LEU B C   
12702 O O   . LEU B 493  ? 0.5481 0.6181 0.5242 -0.0032 0.0252  -0.0065 491  LEU B O   
12703 C CB  . LEU B 493  ? 0.4913 0.5529 0.4562 -0.0005 0.0256  -0.0088 491  LEU B CB  
12704 C CG  . LEU B 493  ? 0.4906 0.5504 0.4494 0.0003  0.0267  -0.0094 491  LEU B CG  
12705 C CD1 . LEU B 493  ? 0.5099 0.5663 0.4666 0.0040  0.0267  -0.0122 491  LEU B CD1 
12706 C CD2 . LEU B 493  ? 0.5353 0.6019 0.4934 -0.0002 0.0299  -0.0081 491  LEU B CD2 
12707 N N   . GLU B 494  ? 0.5099 0.5720 0.4828 -0.0080 0.0217  -0.0046 492  GLU B N   
12708 C CA  . GLU B 494  ? 0.4445 0.5078 0.4222 -0.0091 0.0205  -0.0041 492  GLU B CA  
12709 C C   . GLU B 494  ? 0.4764 0.5392 0.4570 -0.0059 0.0200  -0.0061 492  GLU B C   
12710 O O   . GLU B 494  ? 0.5313 0.5985 0.5163 -0.0055 0.0204  -0.0061 492  GLU B O   
12711 C CB  . GLU B 494  ? 0.4586 0.5293 0.4395 -0.0113 0.0221  -0.0022 492  GLU B CB  
12712 C CG  . GLU B 494  ? 0.3681 0.4400 0.3461 -0.0144 0.0231  0.0000  492  GLU B CG  
12713 C CD  . GLU B 494  ? 0.4486 0.5147 0.4246 -0.0176 0.0207  0.0013  492  GLU B CD  
12714 O OE1 . GLU B 494  ? 0.4192 0.4804 0.3962 -0.0174 0.0184  0.0005  492  GLU B OE1 
12715 O OE2 . GLU B 494  ? 0.4187 0.4850 0.3920 -0.0204 0.0212  0.0032  492  GLU B OE2 
12716 N N   . ASN B 495  ? 0.4556 0.5131 0.4336 -0.0037 0.0191  -0.0079 493  ASN B N   
12717 C CA  . ASN B 495  ? 0.5362 0.5922 0.5162 -0.0008 0.0185  -0.0099 493  ASN B CA  
12718 C C   . ASN B 495  ? 0.5320 0.5938 0.5146 0.0018  0.0207  -0.0106 493  ASN B C   
12719 O O   . ASN B 495  ? 0.5531 0.6152 0.5388 0.0037  0.0202  -0.0116 493  ASN B O   
12720 C CB  . ASN B 495  ? 0.5423 0.5959 0.5254 -0.0018 0.0163  -0.0097 493  ASN B CB  
12721 C CG  . ASN B 495  ? 0.6587 0.7065 0.6395 -0.0040 0.0141  -0.0091 493  ASN B CG  
12722 O OD1 . ASN B 495  ? 0.6600 0.7026 0.6388 -0.0029 0.0127  -0.0103 493  ASN B OD1 
12723 N ND2 . ASN B 495  ? 0.6457 0.6944 0.6269 -0.0071 0.0137  -0.0073 493  ASN B ND2 
12724 N N   . GLY B 496  ? 0.5113 0.5777 0.4927 0.0019  0.0231  -0.0100 494  GLY B N   
12725 C CA  . GLY B 496  ? 0.5684 0.6411 0.5525 0.0044  0.0254  -0.0104 494  GLY B CA  
12726 C C   . GLY B 496  ? 0.6538 0.7311 0.6436 0.0039  0.0251  -0.0096 494  GLY B C   
12727 O O   . GLY B 496  ? 0.6471 0.7264 0.6396 0.0068  0.0256  -0.0106 494  GLY B O   
12728 N N   . ALA B 497  ? 0.5217 0.6005 0.5132 0.0003  0.0242  -0.0077 495  ALA B N   
12729 C CA  . ALA B 497  ? 0.5297 0.6131 0.5264 -0.0006 0.0237  -0.0067 495  ALA B CA  
12730 C C   . ALA B 497  ? 0.4160 0.5083 0.4155 -0.0002 0.0263  -0.0057 495  ALA B C   
12731 O O   . ALA B 497  ? 0.4385 0.5340 0.4366 -0.0019 0.0278  -0.0044 495  ALA B O   
12732 C CB  . ALA B 497  ? 0.4200 0.5013 0.4170 -0.0047 0.0218  -0.0052 495  ALA B CB  
12733 N N   . ASN B 498  ? 0.4654 0.5620 0.4692 0.0021  0.0267  -0.0061 496  ASN B N   
12734 C CA  . ASN B 498  ? 0.4723 0.5781 0.4797 0.0027  0.0290  -0.0050 496  ASN B CA  
12735 C C   . ASN B 498  ? 0.4501 0.5608 0.4601 -0.0016 0.0287  -0.0026 496  ASN B C   
12736 O O   . ASN B 498  ? 0.4508 0.5690 0.4626 -0.0022 0.0309  -0.0012 496  ASN B O   
12737 C CB  . ASN B 498  ? 0.5100 0.6188 0.5214 0.0061  0.0291  -0.0060 496  ASN B CB  
12738 C CG  . ASN B 498  ? 0.6014 0.7063 0.6104 0.0106  0.0299  -0.0083 496  ASN B CG  
12739 O OD1 . ASN B 498  ? 0.6392 0.7422 0.6442 0.0116  0.0313  -0.0091 496  ASN B OD1 
12740 N ND2 . ASN B 498  ? 0.7127 0.8163 0.7239 0.0131  0.0289  -0.0093 496  ASN B ND2 
12741 N N   . SER B 499  ? 0.4017 0.5083 0.4117 -0.0047 0.0262  -0.0020 497  SER B N   
12742 C CA  . SER B 499  ? 0.3618 0.4720 0.3739 -0.0091 0.0256  0.0003  497  SER B CA  
12743 C C   . SER B 499  ? 0.3094 0.4186 0.3179 -0.0121 0.0263  0.0016  497  SER B C   
12744 O O   . SER B 499  ? 0.3505 0.4631 0.3604 -0.0160 0.0262  0.0037  497  SER B O   
12745 C CB  . SER B 499  ? 0.3961 0.5013 0.4088 -0.0112 0.0226  0.0002  497  SER B CB  
12746 O OG  . SER B 499  ? 0.4330 0.5293 0.4413 -0.0111 0.0211  -0.0009 497  SER B OG  
12747 N N   . SER B 500  ? 0.3430 0.4474 0.3467 -0.0107 0.0270  0.0006  498  SER B N   
12748 C CA  . SER B 500  ? 0.3205 0.4227 0.3201 -0.0136 0.0273  0.0020  498  SER B CA  
12749 C C   . SER B 500  ? 0.3805 0.4905 0.3805 -0.0139 0.0304  0.0033  498  SER B C   
12750 O O   . SER B 500  ? 0.4117 0.5266 0.4132 -0.0105 0.0326  0.0024  498  SER B O   
12751 C CB  . SER B 500  ? 0.4068 0.5007 0.4010 -0.0120 0.0266  0.0004  498  SER B CB  
12752 O OG  . SER B 500  ? 0.4827 0.5775 0.4758 -0.0078 0.0283  -0.0014 498  SER B OG  
12753 N N   . PHE B 501  ? 0.3255 0.4365 0.3242 -0.0180 0.0306  0.0056  499  PHE B N   
12754 C CA  . PHE B 501  ? 0.3582 0.4762 0.3567 -0.0186 0.0337  0.0071  499  PHE B CA  
12755 C C   . PHE B 501  ? 0.4374 0.5536 0.4313 -0.0153 0.0357  0.0056  499  PHE B C   
12756 O O   . PHE B 501  ? 0.5174 0.6404 0.5122 -0.0134 0.0386  0.0057  499  PHE B O   
12757 C CB  . PHE B 501  ? 0.3643 0.4823 0.3614 -0.0239 0.0332  0.0098  499  PHE B CB  
12758 C CG  . PHE B 501  ? 0.3729 0.4993 0.3708 -0.0253 0.0363  0.0118  499  PHE B CG  
12759 C CD1 . PHE B 501  ? 0.4230 0.5488 0.4160 -0.0246 0.0384  0.0120  499  PHE B CD1 
12760 C CD2 . PHE B 501  ? 0.3663 0.5015 0.3697 -0.0274 0.0371  0.0136  499  PHE B CD2 
12761 C CE1 . PHE B 501  ? 0.4272 0.5610 0.4208 -0.0259 0.0415  0.0139  499  PHE B CE1 
12762 C CE2 . PHE B 501  ? 0.4374 0.5809 0.4419 -0.0287 0.0401  0.0156  499  PHE B CE2 
12763 C CZ  . PHE B 501  ? 0.4133 0.5561 0.4128 -0.0280 0.0424  0.0158  499  PHE B CZ  
12764 N N   . VAL B 502  ? 0.4671 0.5744 0.4561 -0.0143 0.0341  0.0041  500  VAL B N   
12765 C CA  . VAL B 502  ? 0.5538 0.6589 0.5380 -0.0114 0.0357  0.0026  500  VAL B CA  
12766 C C   . VAL B 502  ? 0.5561 0.6643 0.5422 -0.0065 0.0373  0.0005  500  VAL B C   
12767 O O   . VAL B 502  ? 0.5588 0.6690 0.5423 -0.0040 0.0398  -0.0003 500  VAL B O   
12768 C CB  . VAL B 502  ? 0.5582 0.6532 0.5371 -0.0115 0.0333  0.0016  500  VAL B CB  
12769 C CG1 . VAL B 502  ? 0.5869 0.6789 0.5633 -0.0160 0.0320  0.0039  500  VAL B CG1 
12770 C CG2 . VAL B 502  ? 0.4976 0.5876 0.4786 -0.0099 0.0306  -0.0002 500  VAL B CG2 
12771 N N   . HIS B 503  ? 0.4697 0.5781 0.4602 -0.0049 0.0360  -0.0005 501  HIS B N   
12772 C CA  . HIS B 503  ? 0.4665 0.5781 0.4593 -0.0004 0.0374  -0.0024 501  HIS B CA  
12773 C C   . HIS B 503  ? 0.5092 0.6313 0.5070 -0.0001 0.0399  -0.0010 501  HIS B C   
12774 O O   . HIS B 503  ? 0.4342 0.5607 0.4321 0.0033  0.0426  -0.0018 501  HIS B O   
12775 C CB  . HIS B 503  ? 0.4740 0.5812 0.4691 0.0012  0.0349  -0.0039 501  HIS B CB  
12776 C CG  . HIS B 503  ? 0.4340 0.5445 0.4321 0.0056  0.0361  -0.0054 501  HIS B CG  
12777 N ND1 . HIS B 503  ? 0.5009 0.6187 0.5050 0.0059  0.0366  -0.0045 501  HIS B ND1 
12778 C CD2 . HIS B 503  ? 0.5036 0.6110 0.4996 0.0098  0.0367  -0.0078 501  HIS B CD2 
12779 C CE1 . HIS B 503  ? 0.4941 0.6131 0.4996 0.0103  0.0375  -0.0062 501  HIS B CE1 
12780 N NE2 . HIS B 503  ? 0.5027 0.6152 0.5033 0.0127  0.0377  -0.0082 501  HIS B NE2 
12781 N N   . ARG B 504  ? 0.4168 0.5432 0.4186 -0.0038 0.0391  0.0012  502  ARG B N   
12782 C CA  . ARG B 504  ? 0.3659 0.5027 0.3735 -0.0037 0.0409  0.0026  502  ARG B CA  
12783 C C   . ARG B 504  ? 0.4504 0.5938 0.4568 -0.0040 0.0444  0.0039  502  ARG B C   
12784 O O   . ARG B 504  ? 0.4237 0.5754 0.4338 -0.0016 0.0469  0.0041  502  ARG B O   
12785 C CB  . ARG B 504  ? 0.4362 0.5753 0.4481 -0.0078 0.0388  0.0046  502  ARG B CB  
12786 C CG  . ARG B 504  ? 0.4318 0.5665 0.4458 -0.0068 0.0359  0.0033  502  ARG B CG  
12787 C CD  . ARG B 504  ? 0.3462 0.4799 0.3623 -0.0114 0.0333  0.0049  502  ARG B CD  
12788 N NE  . ARG B 504  ? 0.3557 0.4988 0.3766 -0.0141 0.0342  0.0072  502  ARG B NE  
12789 C CZ  . ARG B 504  ? 0.4081 0.5588 0.4346 -0.0124 0.0348  0.0074  502  ARG B CZ  
12790 N NH1 . ARG B 504  ? 0.3980 0.5480 0.4258 -0.0079 0.0347  0.0055  502  ARG B NH1 
12791 N NH2 . ARG B 504  ? 0.4022 0.5612 0.4330 -0.0154 0.0353  0.0097  502  ARG B NH2 
12792 N N   . ILE B 505  ? 0.4484 0.5885 0.4500 -0.0069 0.0446  0.0049  503  ILE B N   
12793 C CA  . ILE B 505  ? 0.4461 0.5923 0.4461 -0.0074 0.0480  0.0063  503  ILE B CA  
12794 C C   . ILE B 505  ? 0.5001 0.6479 0.4982 -0.0021 0.0508  0.0041  503  ILE B C   
12795 O O   . ILE B 505  ? 0.4341 0.5899 0.4334 -0.0010 0.0542  0.0049  503  ILE B O   
12796 C CB  . ILE B 505  ? 0.4123 0.5534 0.4067 -0.0113 0.0474  0.0077  503  ILE B CB  
12797 N N   . ASN B 506  ? 0.4449 0.5850 0.4399 0.0013  0.0495  0.0013  504  ASN B N   
12798 C CA  . ASN B 506  ? 0.5272 0.6671 0.5196 0.0064  0.0518  -0.0010 504  ASN B CA  
12799 C C   . ASN B 506  ? 0.5436 0.6868 0.5410 0.0106  0.0521  -0.0025 504  ASN B C   
12800 O O   . ASN B 506  ? 0.5611 0.7033 0.5565 0.0152  0.0538  -0.0047 504  ASN B O   
12801 C CB  . ASN B 506  ? 0.5365 0.6659 0.5219 0.0075  0.0504  -0.0032 504  ASN B CB  
12802 C CG  . ASN B 506  ? 0.5571 0.6840 0.5368 0.0044  0.0508  -0.0019 504  ASN B CG  
12803 O OD1 . ASN B 506  ? 0.6066 0.7395 0.5853 0.0038  0.0538  -0.0006 504  ASN B OD1 
12804 N ND2 . ASN B 506  ? 0.6494 0.7676 0.6253 0.0023  0.0478  -0.0021 504  ASN B ND2 
12805 N N   . ASP B 507  ? 0.4840 0.6309 0.4876 0.0092  0.0506  -0.0013 505  ASP B N   
12806 C CA  . ASP B 507  ? 0.5218 0.6721 0.5303 0.0131  0.0507  -0.0024 505  ASP B CA  
12807 C C   . ASP B 507  ? 0.5811 0.7435 0.5949 0.0137  0.0537  -0.0007 505  ASP B C   
12808 O O   . ASP B 507  ? 0.5258 0.6940 0.5436 0.0097  0.0532  0.0019  505  ASP B O   
12809 C CB  . ASP B 507  ? 0.5063 0.6536 0.5183 0.0114  0.0472  -0.0022 505  ASP B CB  
12810 C CG  . ASP B 507  ? 0.5869 0.7345 0.6022 0.0159  0.0467  -0.0038 505  ASP B CG  
12811 O OD1 . ASP B 507  ? 0.6668 0.8208 0.6845 0.0195  0.0493  -0.0042 505  ASP B OD1 
12812 O OD2 . ASP B 507  ? 0.7037 0.8449 0.7190 0.0158  0.0439  -0.0047 505  ASP B OD2 
12813 N N   . PRO B 508  ? 0.6382 0.8047 0.6522 0.0184  0.0567  -0.0019 506  PRO B N   
12814 C CA  . PRO B 508  ? 0.6202 0.7989 0.6395 0.0191  0.0597  -0.0002 506  PRO B CA  
12815 C C   . PRO B 508  ? 0.5980 0.7830 0.6252 0.0192  0.0584  0.0010  506  PRO B C   
12816 O O   . PRO B 508  ? 0.6711 0.8667 0.7036 0.0184  0.0602  0.0030  506  PRO B O   
12817 C CB  . PRO B 508  ? 0.6980 0.8778 0.7149 0.0250  0.0630  -0.0024 506  PRO B CB  
12818 C CG  . PRO B 508  ? 0.6749 0.8428 0.6841 0.0261  0.0618  -0.0050 506  PRO B CG  
12819 C CD  . PRO B 508  ? 0.5994 0.7596 0.6086 0.0233  0.0575  -0.0050 506  PRO B CD  
12820 N N   . LYS B 509  ? 0.6025 0.7815 0.6307 0.0200  0.0552  -0.0002 507  LYS B N   
12821 C CA  . LYS B 509  ? 0.5910 0.7753 0.6261 0.0196  0.0535  0.0010  507  LYS B CA  
12822 C C   . LYS B 509  ? 0.6516 0.8385 0.6893 0.0134  0.0516  0.0036  507  LYS B C   
12823 O O   . LYS B 509  ? 0.7078 0.9005 0.7515 0.0124  0.0503  0.0050  507  LYS B O   
12824 C CB  . LYS B 509  ? 0.5623 0.7387 0.5969 0.0222  0.0508  -0.0011 507  LYS B CB  
12825 N N   . VAL B 510  ? 0.6508 0.8335 0.6841 0.0093  0.0512  0.0044  508  VAL B N   
12826 C CA  . VAL B 510  ? 0.5713 0.7551 0.6063 0.0033  0.0492  0.0068  508  VAL B CA  
12827 C C   . VAL B 510  ? 0.5708 0.7635 0.6072 0.0006  0.0520  0.0092  508  VAL B C   
12828 O O   . VAL B 510  ? 0.6014 0.7926 0.6329 0.0006  0.0541  0.0091  508  VAL B O   
12829 C CB  . VAL B 510  ? 0.5222 0.6947 0.5513 0.0004  0.0466  0.0061  508  VAL B CB  
12830 C CG1 . VAL B 510  ? 0.5346 0.7076 0.5654 -0.0057 0.0443  0.0085  508  VAL B CG1 
12831 C CG2 . VAL B 510  ? 0.5034 0.6673 0.5309 0.0034  0.0442  0.0036  508  VAL B CG2 
12832 N N   . SER B 511  ? 0.5358 0.7380 0.5787 -0.0017 0.0520  0.0115  509  SER B N   
12833 C CA  . SER B 511  ? 0.5475 0.7591 0.5924 -0.0045 0.0546  0.0141  509  SER B CA  
12834 C C   . SER B 511  ? 0.5389 0.7461 0.5802 -0.0107 0.0532  0.0159  509  SER B C   
12835 O O   . SER B 511  ? 0.5129 0.7112 0.5516 -0.0131 0.0500  0.0154  509  SER B O   
12836 C CB  . SER B 511  ? 0.5186 0.7419 0.5720 -0.0052 0.0548  0.0161  509  SER B CB  
12837 O OG  . SER B 511  ? 0.5387 0.7606 0.5944 -0.0101 0.0512  0.0175  509  SER B OG  
12838 N N   . ILE B 512  ? 0.5128 0.7266 0.5542 -0.0132 0.0559  0.0181  510  ILE B N   
12839 C CA  . ILE B 512  ? 0.4823 0.6934 0.5212 -0.0195 0.0547  0.0203  510  ILE B CA  
12840 C C   . ILE B 512  ? 0.5561 0.7696 0.6000 -0.0241 0.0517  0.0221  510  ILE B C   
12841 O O   . ILE B 512  ? 0.4906 0.6973 0.5319 -0.0286 0.0490  0.0229  510  ILE B O   
12842 C CB  . ILE B 512  ? 0.4632 0.6811 0.5008 -0.0211 0.0585  0.0223  510  ILE B CB  
12843 C CG1 . ILE B 512  ? 0.5072 0.7195 0.5379 -0.0173 0.0607  0.0202  510  ILE B CG1 
12844 C CG2 . ILE B 512  ? 0.4533 0.6702 0.4897 -0.0280 0.0572  0.0252  510  ILE B CG2 
12845 C CD1 . ILE B 512  ? 0.5164 0.7379 0.5483 -0.0134 0.0653  0.0202  510  ILE B CD1 
12846 N N   . ASP B 513  ? 0.4805 0.7034 0.5317 -0.0228 0.0519  0.0227  511  ASP B N   
12847 C CA  . ASP B 513  ? 0.4854 0.7105 0.5413 -0.0269 0.0488  0.0242  511  ASP B CA  
12848 C C   . ASP B 513  ? 0.4211 0.6348 0.4741 -0.0271 0.0448  0.0223  511  ASP B C   
12849 O O   . ASP B 513  ? 0.4372 0.6467 0.4895 -0.0320 0.0420  0.0234  511  ASP B O   
12850 C CB  . ASP B 513  ? 0.5195 0.7564 0.5835 -0.0247 0.0496  0.0249  511  ASP B CB  
12851 C CG  . ASP B 513  ? 0.5823 0.8320 0.6508 -0.0268 0.0526  0.0278  511  ASP B CG  
12852 O OD1 . ASP B 513  ? 0.5636 0.8134 0.6300 -0.0319 0.0531  0.0299  511  ASP B OD1 
12853 O OD2 . ASP B 513  ? 0.6563 0.9162 0.7306 -0.0234 0.0546  0.0281  511  ASP B OD2 
12854 N N   . GLU B 514  ? 0.4296 0.6380 0.4808 -0.0218 0.0446  0.0195  512  GLU B N   
12855 C CA  . GLU B 514  ? 0.4651 0.6627 0.5134 -0.0216 0.0411  0.0177  512  GLU B CA  
12856 C C   . GLU B 514  ? 0.4603 0.6478 0.5020 -0.0249 0.0398  0.0176  512  GLU B C   
12857 O O   . GLU B 514  ? 0.4144 0.5952 0.4547 -0.0279 0.0366  0.0176  512  GLU B O   
12858 C CB  . GLU B 514  ? 0.4420 0.6359 0.4893 -0.0153 0.0414  0.0148  512  GLU B CB  
12859 C CG  . GLU B 514  ? 0.5765 0.7787 0.6301 -0.0117 0.0421  0.0146  512  GLU B CG  
12860 C CD  . GLU B 514  ? 0.6279 0.8262 0.6799 -0.0053 0.0428  0.0118  512  GLU B CD  
12861 O OE1 . GLU B 514  ? 0.6027 0.8043 0.6539 -0.0017 0.0460  0.0112  512  GLU B OE1 
12862 O OE2 . GLU B 514  ? 0.7328 0.9243 0.7840 -0.0041 0.0402  0.0103  512  GLU B OE2 
12863 N N   . LEU B 515  ? 0.3992 0.5854 0.4365 -0.0243 0.0423  0.0176  513  LEU B N   
12864 C CA  . LEU B 515  ? 0.4061 0.5825 0.4367 -0.0269 0.0411  0.0176  513  LEU B CA  
12865 C C   . LEU B 515  ? 0.3644 0.5415 0.3954 -0.0334 0.0399  0.0203  513  LEU B C   
12866 O O   . LEU B 515  ? 0.3881 0.5561 0.4147 -0.0362 0.0376  0.0203  513  LEU B O   
12867 C CB  . LEU B 515  ? 0.3610 0.5364 0.3867 -0.0246 0.0442  0.0170  513  LEU B CB  
12868 C CG  . LEU B 515  ? 0.3881 0.5600 0.4117 -0.0184 0.0451  0.0139  513  LEU B CG  
12869 C CD1 . LEU B 515  ? 0.4396 0.6123 0.4587 -0.0166 0.0484  0.0137  513  LEU B CD1 
12870 C CD2 . LEU B 515  ? 0.3927 0.5529 0.4124 -0.0176 0.0420  0.0119  513  LEU B CD2 
12871 N N   . ILE B 516  ? 0.3599 0.5474 0.3959 -0.0360 0.0412  0.0228  514  ILE B N   
12872 C CA  . ILE B 516  ? 0.3128 0.5013 0.3493 -0.0425 0.0400  0.0255  514  ILE B CA  
12873 C C   . ILE B 516  ? 0.3107 0.4999 0.3515 -0.0453 0.0367  0.0260  514  ILE B C   
12874 O O   . ILE B 516  ? 0.3033 0.4935 0.3449 -0.0509 0.0354  0.0283  514  ILE B O   
12875 C CB  . ILE B 516  ? 0.3466 0.5456 0.3854 -0.0447 0.0433  0.0283  514  ILE B CB  
12876 C CG1 . ILE B 516  ? 0.3767 0.5883 0.4234 -0.0432 0.0446  0.0290  514  ILE B CG1 
12877 C CG2 . ILE B 516  ? 0.3670 0.5648 0.4008 -0.0419 0.0465  0.0277  514  ILE B CG2 
12878 C CD1 . ILE B 516  ? 0.4106 0.6337 0.4602 -0.0450 0.0482  0.0317  514  ILE B CD1 
12879 N N   . ALA B 517  ? 0.3516 0.5400 0.3948 -0.0416 0.0354  0.0239  515  ALA B N   
12880 C CA  . ALA B 517  ? 0.3614 0.5492 0.4078 -0.0440 0.0320  0.0241  515  ALA B CA  
12881 C C   . ALA B 517  ? 0.3333 0.5108 0.3751 -0.0484 0.0291  0.0243  515  ALA B C   
12882 O O   . ALA B 517  ? 0.3204 0.4885 0.3564 -0.0474 0.0288  0.0230  515  ALA B O   
12883 C CB  . ALA B 517  ? 0.3249 0.5106 0.3728 -0.0390 0.0309  0.0215  515  ALA B CB  
12884 N N   . ASP B 518  ? 0.3214 0.5009 0.3657 -0.0535 0.0270  0.0261  516  ASP B N   
12885 C CA  . ASP B 518  ? 0.3164 0.4868 0.3568 -0.0581 0.0243  0.0266  516  ASP B CA  
12886 C C   . ASP B 518  ? 0.2693 0.4318 0.3085 -0.0565 0.0212  0.0242  516  ASP B C   
12887 O O   . ASP B 518  ? 0.2980 0.4644 0.3414 -0.0568 0.0195  0.0241  516  ASP B O   
12888 C CB  . ASP B 518  ? 0.2967 0.4730 0.3402 -0.0643 0.0234  0.0295  516  ASP B CB  
12889 C CG  . ASP B 518  ? 0.3538 0.5205 0.3931 -0.0694 0.0205  0.0301  516  ASP B CG  
12890 O OD1 . ASP B 518  ? 0.2861 0.4419 0.3203 -0.0680 0.0190  0.0282  516  ASP B OD1 
12891 O OD2 . ASP B 518  ? 0.3907 0.5609 0.4318 -0.0749 0.0197  0.0324  516  ASP B OD2 
12892 N N   . PRO B 519  ? 0.2476 0.3995 0.2814 -0.0547 0.0203  0.0224  517  PRO B N   
12893 C CA  . PRO B 519  ? 0.2738 0.4183 0.3065 -0.0531 0.0175  0.0202  517  PRO B CA  
12894 C C   . PRO B 519  ? 0.2464 0.3891 0.2801 -0.0577 0.0145  0.0210  517  PRO B C   
12895 O O   . PRO B 519  ? 0.2532 0.3952 0.2887 -0.0565 0.0126  0.0196  517  PRO B O   
12896 C CB  . PRO B 519  ? 0.2770 0.4106 0.3034 -0.0514 0.0173  0.0187  517  PRO B CB  
12897 C CG  . PRO B 519  ? 0.3213 0.4552 0.3449 -0.0539 0.0190  0.0206  517  PRO B CG  
12898 C CD  . PRO B 519  ? 0.2556 0.4016 0.2838 -0.0544 0.0216  0.0224  517  PRO B CD  
12899 N N   . VAL B 520  ? 0.2550 0.3968 0.2873 -0.0631 0.0139  0.0231  518  VAL B N   
12900 C CA  . VAL B 520  ? 0.2601 0.3992 0.2927 -0.0679 0.0109  0.0238  518  VAL B CA  
12901 C C   . VAL B 520  ? 0.2785 0.4272 0.3173 -0.0686 0.0102  0.0243  518  VAL B C   
12902 O O   . VAL B 520  ? 0.2740 0.4202 0.3135 -0.0690 0.0076  0.0232  518  VAL B O   
12903 C CB  . VAL B 520  ? 0.2741 0.4111 0.3042 -0.0735 0.0107  0.0262  518  VAL B CB  
12904 C CG1 . VAL B 520  ? 0.3346 0.4671 0.3641 -0.0785 0.0073  0.0266  518  VAL B CG1 
12905 C CG2 . VAL B 520  ? 0.2961 0.4244 0.3201 -0.0725 0.0115  0.0258  518  VAL B CG2 
12906 N N   . GLU B 521  ? 0.2785 0.4385 0.3220 -0.0686 0.0126  0.0261  519  GLU B N   
12907 C CA  . GLU B 521  ? 0.2554 0.4253 0.3053 -0.0693 0.0119  0.0269  519  GLU B CA  
12908 C C   . GLU B 521  ? 0.2829 0.4542 0.3350 -0.0636 0.0118  0.0247  519  GLU B C   
12909 O O   . GLU B 521  ? 0.3109 0.4858 0.3666 -0.0641 0.0099  0.0245  519  GLU B O   
12910 C CB  . GLU B 521  ? 0.2989 0.4809 0.3534 -0.0710 0.0145  0.0295  519  GLU B CB  
12911 C CG  . GLU B 521  ? 0.3428 0.5240 0.3957 -0.0774 0.0142  0.0321  519  GLU B CG  
12912 C CD  . GLU B 521  ? 0.4091 0.5859 0.4615 -0.0827 0.0104  0.0325  519  GLU B CD  
12913 O OE1 . GLU B 521  ? 0.4100 0.5903 0.4660 -0.0824 0.0085  0.0319  519  GLU B OE1 
12914 O OE2 . GLU B 521  ? 0.5001 0.6697 0.5482 -0.0870 0.0093  0.0334  519  GLU B OE2 
12915 N N   . VAL B 522  ? 0.2808 0.4491 0.3307 -0.0583 0.0137  0.0229  520  VAL B N   
12916 C CA  . VAL B 522  ? 0.2605 0.4291 0.3121 -0.0531 0.0135  0.0208  520  VAL B CA  
12917 C C   . VAL B 522  ? 0.3031 0.4627 0.3520 -0.0535 0.0102  0.0191  520  VAL B C   
12918 O O   . VAL B 522  ? 0.3202 0.4823 0.3720 -0.0523 0.0087  0.0185  520  VAL B O   
12919 C CB  . VAL B 522  ? 0.3153 0.4821 0.3648 -0.0476 0.0162  0.0193  520  VAL B CB  
12920 C CG1 . VAL B 522  ? 0.3182 0.4840 0.3688 -0.0423 0.0157  0.0171  520  VAL B CG1 
12921 C CG2 . VAL B 522  ? 0.4004 0.5768 0.4526 -0.0468 0.0196  0.0209  520  VAL B CG2 
12922 N N   . VAL B 523  ? 0.2447 0.3937 0.2879 -0.0553 0.0091  0.0184  521  VAL B N   
12923 C CA  . VAL B 523  ? 0.2682 0.4085 0.3086 -0.0558 0.0061  0.0168  521  VAL B CA  
12924 C C   . VAL B 523  ? 0.2662 0.4091 0.3089 -0.0604 0.0035  0.0178  521  VAL B C   
12925 O O   . VAL B 523  ? 0.2818 0.4227 0.3249 -0.0597 0.0014  0.0166  521  VAL B O   
12926 C CB  . VAL B 523  ? 0.2847 0.4136 0.3188 -0.0567 0.0056  0.0160  521  VAL B CB  
12927 C CG1 . VAL B 523  ? 0.2689 0.3893 0.3002 -0.0579 0.0025  0.0146  521  VAL B CG1 
12928 C CG2 . VAL B 523  ? 0.2932 0.4188 0.3249 -0.0516 0.0076  0.0145  521  VAL B CG2 
12929 N N   . ARG B 524  ? 0.2791 0.4263 0.3231 -0.0653 0.0036  0.0202  522  ARG B N   
12930 C CA  . ARG B 524  ? 0.2902 0.4396 0.3361 -0.0702 0.0009  0.0213  522  ARG B CA  
12931 C C   . ARG B 524  ? 0.3080 0.4663 0.3596 -0.0685 0.0003  0.0212  522  ARG B C   
12932 O O   . ARG B 524  ? 0.3630 0.5202 0.4150 -0.0706 -0.0025 0.0209  522  ARG B O   
12933 C CB  . ARG B 524  ? 0.3156 0.4696 0.3627 -0.0756 0.0015  0.0241  522  ARG B CB  
12934 C CG  . ARG B 524  ? 0.3552 0.5106 0.4037 -0.0814 -0.0014 0.0253  522  ARG B CG  
12935 C CD  . ARG B 524  ? 0.3952 0.5586 0.4468 -0.0863 -0.0004 0.0284  522  ARG B CD  
12936 N NE  . ARG B 524  ? 0.3594 0.5186 0.4072 -0.0875 0.0015  0.0294  522  ARG B NE  
12937 C CZ  . ARG B 524  ? 0.3590 0.5079 0.4012 -0.0909 0.0000  0.0294  522  ARG B CZ  
12938 N NH1 . ARG B 524  ? 0.3659 0.5071 0.4054 -0.0934 -0.0033 0.0284  522  ARG B NH1 
12939 N NH2 . ARG B 524  ? 0.3756 0.5217 0.4147 -0.0918 0.0019  0.0306  522  ARG B NH2 
12940 N N   . ALA B 525  ? 0.3248 0.4914 0.3804 -0.0644 0.0028  0.0215  523  ALA B N   
12941 C CA  . ALA B 525  ? 0.3342 0.5105 0.3956 -0.0627 0.0025  0.0219  523  ALA B CA  
12942 C C   . ALA B 525  ? 0.3994 0.5723 0.4603 -0.0576 0.0017  0.0195  523  ALA B C   
12943 O O   . ALA B 525  ? 0.3705 0.5504 0.4359 -0.0559 0.0011  0.0198  523  ALA B O   
12944 C CB  . ALA B 525  ? 0.3620 0.5499 0.4285 -0.0609 0.0057  0.0236  523  ALA B CB  
12945 N N   . MET B 526  ? 0.3426 0.5049 0.3982 -0.0552 0.0017  0.0175  524  MET B N   
12946 C CA  A MET B 526  ? 0.3307 0.4892 0.3855 -0.0505 0.0010  0.0153  524  MET B CA  
12947 C CA  B MET B 526  ? 0.3310 0.4897 0.3859 -0.0505 0.0010  0.0153  524  MET B CA  
12948 C C   . MET B 526  ? 0.3272 0.4841 0.3822 -0.0527 -0.0023 0.0149  524  MET B C   
12949 O O   . MET B 526  ? 0.3290 0.4827 0.3821 -0.0577 -0.0044 0.0155  524  MET B O   
12950 C CB  A MET B 526  ? 0.3576 0.5051 0.4066 -0.0482 0.0016  0.0133  524  MET B CB  
12951 C CB  B MET B 526  ? 0.3575 0.5054 0.4067 -0.0480 0.0017  0.0134  524  MET B CB  
12952 C CG  A MET B 526  ? 0.3760 0.5247 0.4245 -0.0452 0.0048  0.0134  524  MET B CG  
12953 C CG  B MET B 526  ? 0.3824 0.5321 0.4319 -0.0431 0.0047  0.0128  524  MET B CG  
12954 S SD  A MET B 526  ? 0.4304 0.5891 0.4843 -0.0398 0.0070  0.0134  524  MET B SD  
12955 S SD  B MET B 526  ? 0.4063 0.5451 0.4494 -0.0422 0.0058  0.0115  524  MET B SD  
12956 C CE  A MET B 526  ? 0.3866 0.5386 0.4387 -0.0353 0.0056  0.0109  524  MET B CE  
12957 C CE  B MET B 526  ? 0.4223 0.5606 0.4654 -0.0353 0.0078  0.0096  524  MET B CE  
12958 N N   . PRO B 527  ? 0.3659 0.5248 0.4228 -0.0491 -0.0030 0.0139  525  PRO B N   
12959 C CA  . PRO B 527  ? 0.4148 0.5726 0.4717 -0.0512 -0.0062 0.0136  525  PRO B CA  
12960 C C   . PRO B 527  ? 0.3809 0.5268 0.4317 -0.0531 -0.0081 0.0120  525  PRO B C   
12961 O O   . PRO B 527  ? 0.3491 0.4932 0.3988 -0.0572 -0.0108 0.0122  525  PRO B O   
12962 C CB  . PRO B 527  ? 0.4579 0.6192 0.5174 -0.0460 -0.0061 0.0128  525  PRO B CB  
12963 C CG  . PRO B 527  ? 0.4183 0.5771 0.4766 -0.0412 -0.0032 0.0118  525  PRO B CG  
12964 C CD  . PRO B 527  ? 0.4099 0.5712 0.4685 -0.0431 -0.0010 0.0130  525  PRO B CD  
12965 N N   . VAL B 528  ? 0.3373 0.4750 0.3840 -0.0501 -0.0070 0.0103  526  VAL B N   
12966 C CA  . VAL B 528  ? 0.3017 0.4281 0.3426 -0.0515 -0.0084 0.0088  526  VAL B CA  
12967 C C   . VAL B 528  ? 0.2729 0.3949 0.3110 -0.0520 -0.0066 0.0090  526  VAL B C   
12968 O O   . VAL B 528  ? 0.3490 0.4691 0.3862 -0.0481 -0.0046 0.0082  526  VAL B O   
12969 C CB  . VAL B 528  ? 0.3139 0.4345 0.3525 -0.0474 -0.0089 0.0066  526  VAL B CB  
12970 C CG1 . VAL B 528  ? 0.3038 0.4129 0.3366 -0.0486 -0.0100 0.0051  526  VAL B CG1 
12971 C CG2 . VAL B 528  ? 0.3363 0.4611 0.3774 -0.0471 -0.0108 0.0066  526  VAL B CG2 
12972 N N   . VAL B 529  ? 0.2680 0.3881 0.3045 -0.0569 -0.0074 0.0101  527  VAL B N   
12973 C CA  . VAL B 529  ? 0.2463 0.3625 0.2800 -0.0577 -0.0058 0.0106  527  VAL B CA  
12974 C C   . VAL B 529  ? 0.2555 0.3611 0.2842 -0.0550 -0.0058 0.0086  527  VAL B C   
12975 O O   . VAL B 529  ? 0.2680 0.3662 0.2935 -0.0558 -0.0078 0.0072  527  VAL B O   
12976 C CB  . VAL B 529  ? 0.2525 0.3678 0.2852 -0.0638 -0.0070 0.0123  527  VAL B CB  
12977 C CG1 . VAL B 529  ? 0.2551 0.3646 0.2840 -0.0646 -0.0056 0.0127  527  VAL B CG1 
12978 C CG2 . VAL B 529  ? 0.2957 0.4225 0.3338 -0.0665 -0.0066 0.0146  527  VAL B CG2 
12979 N N   . GLY B 530  ? 0.2438 0.3487 0.2718 -0.0517 -0.0035 0.0082  528  GLY B N   
12980 C CA  . GLY B 530  ? 0.2467 0.3420 0.2702 -0.0493 -0.0034 0.0065  528  GLY B CA  
12981 C C   . GLY B 530  ? 0.2281 0.3211 0.2516 -0.0449 -0.0036 0.0045  528  GLY B C   
12982 O O   . GLY B 530  ? 0.2218 0.3067 0.2417 -0.0434 -0.0040 0.0030  528  GLY B O   
12983 N N   . ALA B 531  ? 0.2186 0.3187 0.2461 -0.0427 -0.0033 0.0046  529  ALA B N   
12984 C CA  . ALA B 531  ? 0.2118 0.3096 0.2391 -0.0385 -0.0034 0.0028  529  ALA B CA  
12985 C C   . ALA B 531  ? 0.2258 0.3201 0.2514 -0.0347 -0.0015 0.0019  529  ALA B C   
12986 O O   . ALA B 531  ? 0.2346 0.3322 0.2610 -0.0341 0.0004  0.0026  529  ALA B O   
12987 C CB  . ALA B 531  ? 0.2609 0.3673 0.2929 -0.0367 -0.0032 0.0033  529  ALA B CB  
12988 N N   . LYS B 532  ? 0.2108 0.2985 0.2340 -0.0323 -0.0021 0.0001  530  LYS B N   
12989 C CA  . LYS B 532  ? 0.2107 0.2947 0.2322 -0.0286 -0.0006 -0.0010 530  LYS B CA  
12990 C C   . LYS B 532  ? 0.2074 0.2983 0.2323 -0.0253 0.0013  -0.0007 530  LYS B C   
12991 O O   . LYS B 532  ? 0.2165 0.3139 0.2449 -0.0248 0.0011  -0.0001 530  LYS B O   
12992 C CB  . LYS B 532  ? 0.2635 0.3409 0.2829 -0.0266 -0.0017 -0.0027 530  LYS B CB  
12993 C CG  . LYS B 532  ? 0.2557 0.3295 0.2739 -0.0226 -0.0005 -0.0040 530  LYS B CG  
12994 C CD  . LYS B 532  ? 0.2724 0.3407 0.2890 -0.0209 -0.0017 -0.0055 530  LYS B CD  
12995 C CE  . LYS B 532  ? 0.2561 0.3286 0.2754 -0.0196 -0.0023 -0.0056 530  LYS B CE  
12996 N NZ  . LYS B 532  ? 0.2428 0.3206 0.2649 -0.0163 -0.0008 -0.0054 530  LYS B NZ  
12997 N N   . HIS B 533  ? 0.1937 0.2831 0.2174 -0.0229 0.0030  -0.0012 531  HIS B N   
12998 C CA  . HIS B 533  ? 0.2029 0.2970 0.2288 -0.0192 0.0048  -0.0014 531  HIS B CA  
12999 C C   . HIS B 533  ? 0.2069 0.3012 0.2344 -0.0164 0.0040  -0.0024 531  HIS B C   
13000 O O   . HIS B 533  ? 0.2143 0.3023 0.2396 -0.0158 0.0028  -0.0035 531  HIS B O   
13001 C CB  . HIS B 533  ? 0.2088 0.2987 0.2320 -0.0169 0.0062  -0.0023 531  HIS B CB  
13002 C CG  . HIS B 533  ? 0.2416 0.3365 0.2666 -0.0138 0.0084  -0.0023 531  HIS B CG  
13003 N ND1 . HIS B 533  ? 0.2323 0.3296 0.2595 -0.0102 0.0087  -0.0030 531  HIS B ND1 
13004 C CD2 . HIS B 533  ? 0.2890 0.3871 0.3138 -0.0136 0.0103  -0.0017 531  HIS B CD2 
13005 C CE1 . HIS B 533  ? 0.3053 0.4068 0.3336 -0.0078 0.0108  -0.0030 531  HIS B CE1 
13006 N NE2 . HIS B 533  ? 0.3890 0.4912 0.4158 -0.0098 0.0119  -0.0022 531  HIS B NE2 
13007 N N   . ASP B 534  ? 0.2152 0.3168 0.2465 -0.0146 0.0047  -0.0018 532  ASP B N   
13008 C CA  . ASP B 534  ? 0.2483 0.3507 0.2813 -0.0119 0.0040  -0.0024 532  ASP B CA  
13009 C C   . ASP B 534  ? 0.2540 0.3509 0.2851 -0.0082 0.0046  -0.0039 532  ASP B C   
13010 O O   . ASP B 534  ? 0.2992 0.3938 0.3302 -0.0066 0.0036  -0.0046 532  ASP B O   
13011 C CB  . ASP B 534  ? 0.3260 0.4376 0.3636 -0.0103 0.0049  -0.0013 532  ASP B CB  
13012 C CG  . ASP B 534  ? 0.4524 0.5702 0.4927 -0.0139 0.0038  0.0003  532  ASP B CG  
13013 O OD1 . ASP B 534  ? 0.5291 0.6438 0.5681 -0.0168 0.0018  0.0003  532  ASP B OD1 
13014 O OD2 . ASP B 534  ? 0.5224 0.6484 0.5664 -0.0136 0.0050  0.0016  532  ASP B OD2 
13015 N N   . ARG B 535  ? 0.2280 0.3227 0.2572 -0.0069 0.0061  -0.0045 533  ARG B N   
13016 C CA  . ARG B 535  ? 0.2288 0.3191 0.2565 -0.0033 0.0068  -0.0059 533  ARG B CA  
13017 C C   . ARG B 535  ? 0.2334 0.3155 0.2571 -0.0040 0.0063  -0.0069 533  ARG B C   
13018 O O   . ARG B 535  ? 0.2723 0.3508 0.2945 -0.0014 0.0069  -0.0080 533  ARG B O   
13019 C CB  . ARG B 535  ? 0.2886 0.3827 0.3173 -0.0005 0.0090  -0.0059 533  ARG B CB  
13020 N N   . ILE B 536  ? 0.2017 0.2810 0.2238 -0.0073 0.0050  -0.0066 534  ILE B N   
13021 C CA  . ILE B 536  ? 0.1901 0.2618 0.2088 -0.0080 0.0043  -0.0075 534  ILE B CA  
13022 C C   . ILE B 536  ? 0.1958 0.2644 0.2140 -0.0093 0.0025  -0.0078 534  ILE B C   
13023 O O   . ILE B 536  ? 0.2185 0.2889 0.2373 -0.0121 0.0015  -0.0070 534  ILE B O   
13024 C CB  . ILE B 536  ? 0.2005 0.2708 0.2171 -0.0107 0.0046  -0.0068 534  ILE B CB  
13025 C CG1 . ILE B 536  ? 0.2044 0.2778 0.2210 -0.0092 0.0066  -0.0065 534  ILE B CG1 
13026 C CG2 . ILE B 536  ? 0.2152 0.2776 0.2284 -0.0111 0.0036  -0.0076 534  ILE B CG2 
13027 C CD1 . ILE B 536  ? 0.2751 0.3478 0.2897 -0.0119 0.0070  -0.0056 534  ILE B CD1 
13028 N N   . ALA B 537  ? 0.1869 0.2508 0.2039 -0.0073 0.0020  -0.0089 535  ALA B N   
13029 C CA  . ALA B 537  ? 0.1989 0.2597 0.2153 -0.0081 0.0005  -0.0094 535  ALA B CA  
13030 C C   . ALA B 537  ? 0.1797 0.2350 0.1932 -0.0106 -0.0004 -0.0096 535  ALA B C   
13031 O O   . ALA B 537  ? 0.1864 0.2377 0.1979 -0.0102 0.0000  -0.0100 535  ALA B O   
13032 C CB  . ALA B 537  ? 0.2108 0.2688 0.2270 -0.0051 0.0005  -0.0104 535  ALA B CB  
13033 N N   . LEU B 538  ? 0.1805 0.2352 0.1936 -0.0130 -0.0018 -0.0094 536  LEU B N   
13034 C CA  . LEU B 538  ? 0.1845 0.2329 0.1946 -0.0146 -0.0028 -0.0099 536  LEU B CA  
13035 C C   . LEU B 538  ? 0.1911 0.2347 0.2000 -0.0120 -0.0027 -0.0112 536  LEU B C   
13036 O O   . LEU B 538  ? 0.2098 0.2549 0.2201 -0.0097 -0.0024 -0.0116 536  LEU B O   
13037 C CB  . LEU B 538  ? 0.2174 0.2654 0.2269 -0.0171 -0.0043 -0.0098 536  LEU B CB  
13038 C CG  . LEU B 538  ? 0.2390 0.2903 0.2490 -0.0206 -0.0048 -0.0086 536  LEU B CG  
13039 C CD1 . LEU B 538  ? 0.2829 0.3340 0.2924 -0.0228 -0.0065 -0.0087 536  LEU B CD1 
13040 C CD2 . LEU B 538  ? 0.2494 0.2970 0.2572 -0.0225 -0.0047 -0.0082 536  LEU B CD2 
13041 N N   . PRO B 539  ? 0.1795 0.2174 0.1860 -0.0123 -0.0030 -0.0117 537  PRO B N   
13042 C CA  . PRO B 539  ? 0.1821 0.2158 0.1878 -0.0100 -0.0030 -0.0128 537  PRO B CA  
13043 C C   . PRO B 539  ? 0.1902 0.2238 0.1963 -0.0092 -0.0035 -0.0134 537  PRO B C   
13044 O O   . PRO B 539  ? 0.1916 0.2251 0.1986 -0.0068 -0.0030 -0.0139 537  PRO B O   
13045 C CB  . PRO B 539  ? 0.1927 0.2208 0.1958 -0.0111 -0.0035 -0.0131 537  PRO B CB  
13046 C CG  . PRO B 539  ? 0.1890 0.2186 0.1916 -0.0131 -0.0033 -0.0120 537  PRO B CG  
13047 C CD  . PRO B 539  ? 0.2073 0.2425 0.2118 -0.0147 -0.0033 -0.0112 537  PRO B CD  
13048 N N   . ALA B 540  ? 0.1803 0.2142 0.1858 -0.0113 -0.0045 -0.0132 538  ALA B N   
13049 C CA  . ALA B 540  ? 0.1936 0.2273 0.1990 -0.0107 -0.0051 -0.0138 538  ALA B CA  
13050 C C   . ALA B 540  ? 0.2099 0.2487 0.2179 -0.0090 -0.0046 -0.0133 538  ALA B C   
13051 O O   . ALA B 540  ? 0.2027 0.2412 0.2108 -0.0076 -0.0048 -0.0137 538  ALA B O   
13052 C CB  . ALA B 540  ? 0.2226 0.2558 0.2266 -0.0135 -0.0064 -0.0137 538  ALA B CB  
13053 N N   . GLU B 541  ? 0.2072 0.2507 0.2173 -0.0088 -0.0040 -0.0125 539  GLU B N   
13054 C CA  . GLU B 541  ? 0.1960 0.2449 0.2087 -0.0074 -0.0037 -0.0119 539  GLU B CA  
13055 C C   . GLU B 541  ? 0.1821 0.2318 0.1961 -0.0045 -0.0024 -0.0120 539  GLU B C   
13056 O O   . GLU B 541  ? 0.2045 0.2587 0.2207 -0.0030 -0.0019 -0.0115 539  GLU B O   
13057 C CB  . GLU B 541  ? 0.2430 0.2975 0.2574 -0.0096 -0.0040 -0.0108 539  GLU B CB  
13058 C CG  . GLU B 541  ? 0.2732 0.3262 0.2859 -0.0127 -0.0056 -0.0108 539  GLU B CG  
13059 C CD  . GLU B 541  ? 0.4272 0.4854 0.4414 -0.0155 -0.0063 -0.0096 539  GLU B CD  
13060 O OE1 . GLU B 541  ? 0.3828 0.4462 0.3996 -0.0152 -0.0054 -0.0087 539  GLU B OE1 
13061 O OE2 . GLU B 541  ? 0.4294 0.4863 0.4422 -0.0181 -0.0077 -0.0097 539  GLU B OE2 
13062 N N   . LEU B 542  ? 0.1763 0.2215 0.1889 -0.0034 -0.0019 -0.0128 540  LEU B N   
13063 C CA  . LEU B 542  ? 0.1899 0.2352 0.2033 -0.0008 -0.0008 -0.0130 540  LEU B CA  
13064 C C   . LEU B 542  ? 0.1869 0.2340 0.2019 0.0015  -0.0007 -0.0130 540  LEU B C   
13065 O O   . LEU B 542  ? 0.2181 0.2671 0.2343 0.0035  0.0002  -0.0130 540  LEU B O   
13066 C CB  . LEU B 542  ? 0.2201 0.2600 0.2317 -0.0001 -0.0007 -0.0139 540  LEU B CB  
13067 C CG  . LEU B 542  ? 0.2505 0.2881 0.2606 -0.0015 -0.0006 -0.0139 540  LEU B CG  
13068 C CD1 . LEU B 542  ? 0.2196 0.2527 0.2285 -0.0001 -0.0005 -0.0147 540  LEU B CD1 
13069 C CD2 . LEU B 542  ? 0.2275 0.2690 0.2383 -0.0018 0.0002  -0.0133 540  LEU B CD2 
13070 N N   . PHE B 543  ? 0.1884 0.2345 0.2030 0.0014  -0.0015 -0.0131 541  PHE B N   
13071 C CA  . PHE B 543  ? 0.1997 0.2468 0.2154 0.0035  -0.0014 -0.0130 541  PHE B CA  
13072 C C   . PHE B 543  ? 0.2008 0.2529 0.2181 0.0032  -0.0020 -0.0121 541  PHE B C   
13073 O O   . PHE B 543  ? 0.2179 0.2708 0.2358 0.0047  -0.0023 -0.0118 541  PHE B O   
13074 C CB  . PHE B 543  ? 0.1846 0.2271 0.1987 0.0039  -0.0018 -0.0136 541  PHE B CB  
13075 C CG  . PHE B 543  ? 0.1820 0.2201 0.1948 0.0040  -0.0014 -0.0144 541  PHE B CG  
13076 C CD1 . PHE B 543  ? 0.2289 0.2664 0.2422 0.0056  -0.0006 -0.0146 541  PHE B CD1 
13077 C CD2 . PHE B 543  ? 0.1889 0.2233 0.1999 0.0026  -0.0018 -0.0149 541  PHE B CD2 
13078 C CE1 . PHE B 543  ? 0.2177 0.2514 0.2300 0.0056  -0.0004 -0.0153 541  PHE B CE1 
13079 C CE2 . PHE B 543  ? 0.1949 0.2257 0.2050 0.0029  -0.0015 -0.0155 541  PHE B CE2 
13080 C CZ  . PHE B 543  ? 0.2135 0.2440 0.2243 0.0043  -0.0009 -0.0156 541  PHE B CZ  
13081 N N   . GLY B 544  ? 0.1978 0.2532 0.2157 0.0011  -0.0023 -0.0115 542  GLY B N   
13082 C CA  . GLY B 544  ? 0.1944 0.2553 0.2143 0.0007  -0.0030 -0.0105 542  GLY B CA  
13083 C C   . GLY B 544  ? 0.2313 0.2912 0.2501 0.0001  -0.0043 -0.0105 542  GLY B C   
13084 O O   . GLY B 544  ? 0.2529 0.3087 0.2693 -0.0014 -0.0049 -0.0112 542  GLY B O   
13085 N N   . ASP B 545  ? 0.2518 0.3155 0.2724 0.0015  -0.0046 -0.0098 543  ASP B N   
13086 C CA  . ASP B 545  ? 0.2895 0.3531 0.3091 0.0010  -0.0060 -0.0096 543  ASP B CA  
13087 C C   . ASP B 545  ? 0.2819 0.3402 0.2994 0.0024  -0.0058 -0.0103 543  ASP B C   
13088 O O   . ASP B 545  ? 0.2719 0.3292 0.2878 0.0017  -0.0067 -0.0103 543  ASP B O   
13089 C CB  . ASP B 545  ? 0.2949 0.3643 0.3172 0.0023  -0.0065 -0.0083 543  ASP B CB  
13090 C CG  . ASP B 545  ? 0.4680 0.5436 0.4929 0.0009  -0.0067 -0.0074 543  ASP B CG  
13091 O OD1 . ASP B 545  ? 0.4879 0.5634 0.5120 -0.0020 -0.0071 -0.0076 543  ASP B OD1 
13092 O OD2 . ASP B 545  ? 0.6607 0.7413 0.6886 0.0029  -0.0063 -0.0065 543  ASP B OD2 
13093 N N   . ALA B 546  ? 0.2432 0.2984 0.2606 0.0042  -0.0046 -0.0108 544  ALA B N   
13094 C CA  . ALA B 546  ? 0.2246 0.2754 0.2404 0.0055  -0.0043 -0.0113 544  ALA B CA  
13095 C C   . ALA B 546  ? 0.2214 0.2680 0.2345 0.0037  -0.0047 -0.0122 544  ALA B C   
13096 O O   . ALA B 546  ? 0.2200 0.2647 0.2316 0.0039  -0.0050 -0.0123 544  ALA B O   
13097 C CB  . ALA B 546  ? 0.2592 0.3076 0.2756 0.0075  -0.0031 -0.0117 544  ALA B CB  
13098 N N   . ARG B 547  ? 0.2147 0.2598 0.2270 0.0020  -0.0046 -0.0128 545  ARG B N   
13099 C CA  . ARG B 547  ? 0.2075 0.2482 0.2171 0.0006  -0.0049 -0.0137 545  ARG B CA  
13100 C C   . ARG B 547  ? 0.1922 0.2321 0.2015 -0.0013 -0.0049 -0.0140 545  ARG B C   
13101 O O   . ARG B 547  ? 0.1972 0.2393 0.2080 -0.0012 -0.0044 -0.0136 545  ARG B O   
13102 C CB  . ARG B 547  ? 0.2332 0.2696 0.2419 0.0021  -0.0041 -0.0143 545  ARG B CB  
13103 C CG  . ARG B 547  ? 0.2153 0.2506 0.2252 0.0033  -0.0031 -0.0145 545  ARG B CG  
13104 C CD  . ARG B 547  ? 0.2168 0.2483 0.2261 0.0047  -0.0025 -0.0150 545  ARG B CD  
13105 N NE  . ARG B 547  ? 0.1918 0.2231 0.2025 0.0062  -0.0018 -0.0150 545  ARG B NE  
13106 C CZ  . ARG B 547  ? 0.2057 0.2346 0.2162 0.0061  -0.0014 -0.0155 545  ARG B CZ  
13107 N NH1 . ARG B 547  ? 0.1987 0.2251 0.2079 0.0048  -0.0016 -0.0161 545  ARG B NH1 
13108 N NH2 . ARG B 547  ? 0.2107 0.2396 0.2223 0.0074  -0.0009 -0.0155 545  ARG B NH2 
13109 N N   . THR B 548  ? 0.1919 0.2283 0.1987 -0.0030 -0.0055 -0.0147 546  THR B N   
13110 C CA  . THR B 548  ? 0.1899 0.2246 0.1958 -0.0049 -0.0056 -0.0150 546  THR B CA  
13111 C C   . THR B 548  ? 0.1768 0.2073 0.1821 -0.0037 -0.0048 -0.0157 546  THR B C   
13112 O O   . THR B 548  ? 0.1840 0.2114 0.1883 -0.0026 -0.0045 -0.0163 546  THR B O   
13113 C CB  . THR B 548  ? 0.1806 0.2129 0.1839 -0.0071 -0.0067 -0.0155 546  THR B CB  
13114 O OG1 . THR B 548  ? 0.2488 0.2852 0.2526 -0.0083 -0.0077 -0.0149 546  THR B OG1 
13115 C CG2 . THR B 548  ? 0.2158 0.2456 0.2178 -0.0091 -0.0070 -0.0158 546  THR B CG2 
13116 N N   . ASN B 549  ? 0.1711 0.2019 0.1771 -0.0040 -0.0043 -0.0154 547  ASN B N   
13117 C CA  . ASN B 549  ? 0.1608 0.1879 0.1663 -0.0030 -0.0037 -0.0159 547  ASN B CA  
13118 C C   . ASN B 549  ? 0.1655 0.1879 0.1685 -0.0042 -0.0043 -0.0167 547  ASN B C   
13119 O O   . ASN B 549  ? 0.1932 0.2151 0.1947 -0.0063 -0.0051 -0.0167 547  ASN B O   
13120 C CB  . ASN B 549  ? 0.1832 0.2118 0.1895 -0.0034 -0.0033 -0.0154 547  ASN B CB  
13121 C CG  . ASN B 549  ? 0.1777 0.2033 0.1837 -0.0023 -0.0028 -0.0158 547  ASN B CG  
13122 O OD1 . ASN B 549  ? 0.1794 0.2026 0.1854 -0.0007 -0.0026 -0.0164 547  ASN B OD1 
13123 N ND2 . ASN B 549  ? 0.1785 0.2043 0.1843 -0.0030 -0.0026 -0.0155 547  ASN B ND2 
13124 N N   . SER B 550  ? 0.1622 0.1812 0.1647 -0.0028 -0.0038 -0.0173 548  SER B N   
13125 C CA  . SER B 550  ? 0.1762 0.1906 0.1765 -0.0035 -0.0042 -0.0180 548  SER B CA  
13126 C C   . SER B 550  ? 0.1822 0.1955 0.1818 -0.0052 -0.0046 -0.0176 548  SER B C   
13127 O O   . SER B 550  ? 0.1930 0.2084 0.1938 -0.0052 -0.0043 -0.0170 548  SER B O   
13128 C CB  . SER B 550  ? 0.1837 0.1954 0.1843 -0.0016 -0.0036 -0.0185 548  SER B CB  
13129 O OG  . SER B 550  ? 0.1782 0.1903 0.1802 -0.0007 -0.0032 -0.0182 548  SER B OG  
13130 N N   . ALA B 551  ? 0.1953 0.2050 0.1925 -0.0066 -0.0053 -0.0181 549  ALA B N   
13131 C CA  . ALA B 551  ? 0.2084 0.2162 0.2045 -0.0083 -0.0058 -0.0177 549  ALA B CA  
13132 C C   . ALA B 551  ? 0.2001 0.2031 0.1950 -0.0073 -0.0057 -0.0182 549  ALA B C   
13133 O O   . ALA B 551  ? 0.2094 0.2096 0.2035 -0.0061 -0.0056 -0.0190 549  ALA B O   
13134 C CB  . ALA B 551  ? 0.2125 0.2194 0.2066 -0.0110 -0.0068 -0.0177 549  ALA B CB  
13135 N N   . GLY B 552  ? 0.2064 0.2085 0.2011 -0.0078 -0.0058 -0.0176 550  GLY B N   
13136 C CA  . GLY B 552  ? 0.2108 0.2084 0.2044 -0.0071 -0.0060 -0.0178 550  GLY B CA  
13137 C C   . GLY B 552  ? 0.2166 0.2102 0.2075 -0.0091 -0.0069 -0.0177 550  GLY B C   
13138 O O   . GLY B 552  ? 0.2391 0.2326 0.2287 -0.0110 -0.0075 -0.0178 550  GLY B O   
13139 N N   . LEU B 553  ? 0.2218 0.2118 0.2117 -0.0087 -0.0072 -0.0175 551  LEU B N   
13140 C CA  . LEU B 553  ? 0.2379 0.2233 0.2251 -0.0105 -0.0082 -0.0172 551  LEU B CA  
13141 C C   . LEU B 553  ? 0.2228 0.2078 0.2098 -0.0109 -0.0083 -0.0161 551  LEU B C   
13142 O O   . LEU B 553  ? 0.2452 0.2312 0.2336 -0.0091 -0.0079 -0.0159 551  LEU B O   
13143 C CB  . LEU B 553  ? 0.2301 0.2102 0.2156 -0.0090 -0.0084 -0.0183 551  LEU B CB  
13144 C CG  . LEU B 553  ? 0.2658 0.2455 0.2508 -0.0086 -0.0082 -0.0195 551  LEU B CG  
13145 C CD1 . LEU B 553  ? 0.2954 0.2707 0.2793 -0.0064 -0.0081 -0.0205 551  LEU B CD1 
13146 C CD2 . LEU B 553  ? 0.2999 0.2784 0.2825 -0.0115 -0.0091 -0.0196 551  LEU B CD2 
13147 N N   . ASP B 554  ? 0.2298 0.2134 0.2150 -0.0135 -0.0090 -0.0152 552  ASP B N   
13148 C CA  . ASP B 554  ? 0.2308 0.2144 0.2155 -0.0143 -0.0091 -0.0139 552  ASP B CA  
13149 C C   . ASP B 554  ? 0.2204 0.1977 0.2029 -0.0137 -0.0099 -0.0138 552  ASP B C   
13150 O O   . ASP B 554  ? 0.2403 0.2133 0.2203 -0.0155 -0.0108 -0.0137 552  ASP B O   
13151 C CB  . ASP B 554  ? 0.2549 0.2404 0.2389 -0.0176 -0.0093 -0.0128 552  ASP B CB  
13152 C CG  . ASP B 554  ? 0.2507 0.2365 0.2339 -0.0185 -0.0093 -0.0114 552  ASP B CG  
13153 O OD1 . ASP B 554  ? 0.2496 0.2339 0.2328 -0.0167 -0.0092 -0.0113 552  ASP B OD1 
13154 O OD2 . ASP B 554  ? 0.2666 0.2544 0.2494 -0.0212 -0.0093 -0.0103 552  ASP B OD2 
13155 N N   . LEU B 555  ? 0.2206 0.1974 0.2041 -0.0113 -0.0098 -0.0139 553  LEU B N   
13156 C CA  . LEU B 555  ? 0.2417 0.2130 0.2235 -0.0103 -0.0106 -0.0137 553  LEU B CA  
13157 C C   . LEU B 555  ? 0.2545 0.2238 0.2343 -0.0120 -0.0113 -0.0122 553  LEU B C   
13158 O O   . LEU B 555  ? 0.2525 0.2174 0.2309 -0.0111 -0.0121 -0.0118 553  LEU B O   
13159 C CB  . LEU B 555  ? 0.2333 0.2050 0.2171 -0.0072 -0.0103 -0.0143 553  LEU B CB  
13160 C CG  . LEU B 555  ? 0.2389 0.2125 0.2247 -0.0055 -0.0096 -0.0157 553  LEU B CG  
13161 C CD1 . LEU B 555  ? 0.2828 0.2564 0.2705 -0.0026 -0.0094 -0.0160 553  LEU B CD1 
13162 C CD2 . LEU B 555  ? 0.2924 0.2622 0.2762 -0.0060 -0.0098 -0.0166 553  LEU B CD2 
13163 N N   . SER B 556  ? 0.2267 0.1992 0.2063 -0.0145 -0.0110 -0.0112 554  SER B N   
13164 C CA  . SER B 556  ? 0.2466 0.2170 0.2238 -0.0166 -0.0116 -0.0096 554  SER B CA  
13165 C C   . SER B 556  ? 0.2573 0.2253 0.2324 -0.0198 -0.0122 -0.0092 554  SER B C   
13166 O O   . SER B 556  ? 0.2689 0.2346 0.2418 -0.0220 -0.0127 -0.0078 554  SER B O   
13167 C CB  . SER B 556  ? 0.2359 0.2115 0.2140 -0.0173 -0.0108 -0.0086 554  SER B CB  
13168 O OG  . SER B 556  ? 0.2507 0.2311 0.2301 -0.0190 -0.0100 -0.0086 554  SER B OG  
13169 N N   . ASN B 557  ? 0.2383 0.2065 0.2139 -0.0201 -0.0121 -0.0104 555  ASN B N   
13170 C CA  . ASN B 557  ? 0.2304 0.1965 0.2040 -0.0232 -0.0128 -0.0102 555  ASN B CA  
13171 C C   . ASN B 557  ? 0.2559 0.2142 0.2267 -0.0227 -0.0139 -0.0109 555  ASN B C   
13172 O O   . ASN B 557  ? 0.2502 0.2069 0.2214 -0.0203 -0.0138 -0.0124 555  ASN B O   
13173 C CB  . ASN B 557  ? 0.2371 0.2079 0.2126 -0.0238 -0.0123 -0.0111 555  ASN B CB  
13174 C CG  . ASN B 557  ? 0.2399 0.2092 0.2136 -0.0272 -0.0132 -0.0110 555  ASN B CG  
13175 O OD1 . ASN B 557  ? 0.2600 0.2229 0.2309 -0.0279 -0.0142 -0.0114 555  ASN B OD1 
13176 N ND2 . ASN B 557  ? 0.2630 0.2381 0.2384 -0.0293 -0.0128 -0.0103 555  ASN B ND2 
13177 N N   . GLU B 558  ? 0.2683 0.2216 0.2361 -0.0250 -0.0149 -0.0097 556  GLU B N   
13178 C CA  . GLU B 558  ? 0.2775 0.2228 0.2423 -0.0243 -0.0160 -0.0104 556  GLU B CA  
13179 C C   . GLU B 558  ? 0.2918 0.2349 0.2556 -0.0247 -0.0163 -0.0121 556  GLU B C   
13180 O O   . GLU B 558  ? 0.2827 0.2206 0.2451 -0.0226 -0.0166 -0.0134 556  GLU B O   
13181 C CB  . GLU B 558  ? 0.3016 0.2415 0.2631 -0.0269 -0.0172 -0.0088 556  GLU B CB  
13182 C CG  . GLU B 558  ? 0.2978 0.2377 0.2592 -0.0263 -0.0172 -0.0071 556  GLU B CG  
13183 C CD  . GLU B 558  ? 0.3060 0.2434 0.2679 -0.0222 -0.0173 -0.0076 556  GLU B CD  
13184 O OE1 . GLU B 558  ? 0.3048 0.2390 0.2667 -0.0197 -0.0174 -0.0092 556  GLU B OE1 
13185 O OE2 . GLU B 558  ? 0.2992 0.2381 0.2616 -0.0215 -0.0172 -0.0063 556  GLU B OE2 
13186 N N   . GLU B 559  ? 0.2703 0.2172 0.2347 -0.0274 -0.0162 -0.0122 557  GLU B N   
13187 C CA  . GLU B 559  ? 0.2728 0.2180 0.2361 -0.0277 -0.0166 -0.0139 557  GLU B CA  
13188 C C   . GLU B 559  ? 0.2720 0.2195 0.2375 -0.0239 -0.0155 -0.0155 557  GLU B C   
13189 O O   . GLU B 559  ? 0.2736 0.2168 0.2374 -0.0223 -0.0157 -0.0171 557  GLU B O   
13190 C CB  . GLU B 559  ? 0.3210 0.2712 0.2852 -0.0311 -0.0167 -0.0136 557  GLU B CB  
13191 C CG  . GLU B 559  ? 0.3650 0.3136 0.3273 -0.0354 -0.0177 -0.0120 557  GLU B CG  
13192 C CD  . GLU B 559  ? 0.4687 0.4230 0.4324 -0.0385 -0.0179 -0.0118 557  GLU B CD  
13193 O OE1 . GLU B 559  ? 0.5174 0.4745 0.4823 -0.0375 -0.0177 -0.0132 557  GLU B OE1 
13194 O OE2 . GLU B 559  ? 0.4155 0.3719 0.3793 -0.0419 -0.0182 -0.0100 557  GLU B OE2 
13195 N N   . THR B 560  ? 0.2589 0.2130 0.2279 -0.0225 -0.0144 -0.0151 558  THR B N   
13196 C CA  . THR B 560  ? 0.2502 0.2068 0.2214 -0.0191 -0.0134 -0.0165 558  THR B CA  
13197 C C   . THR B 560  ? 0.2454 0.1972 0.2159 -0.0160 -0.0134 -0.0170 558  THR B C   
13198 O O   . THR B 560  ? 0.2595 0.2098 0.2300 -0.0137 -0.0130 -0.0185 558  THR B O   
13199 C CB  . THR B 560  ? 0.2337 0.1976 0.2085 -0.0182 -0.0124 -0.0158 558  THR B CB  
13200 O OG1 . THR B 560  ? 0.2647 0.2334 0.2404 -0.0210 -0.0124 -0.0152 558  THR B OG1 
13201 C CG2 . THR B 560  ? 0.2611 0.2276 0.2382 -0.0151 -0.0114 -0.0170 558  THR B CG2 
13202 N N   . LEU B 561  ? 0.2340 0.1838 0.2041 -0.0157 -0.0138 -0.0158 559  LEU B N   
13203 C CA  . LEU B 561  ? 0.2161 0.1617 0.1859 -0.0126 -0.0139 -0.0162 559  LEU B CA  
13204 C C   . LEU B 561  ? 0.2576 0.1960 0.2241 -0.0123 -0.0146 -0.0173 559  LEU B C   
13205 O O   . LEU B 561  ? 0.2587 0.1950 0.2256 -0.0092 -0.0142 -0.0185 559  LEU B O   
13206 C CB  . LEU B 561  ? 0.2474 0.1919 0.2170 -0.0127 -0.0144 -0.0144 559  LEU B CB  
13207 C CG  . LEU B 561  ? 0.2277 0.1788 0.2004 -0.0121 -0.0137 -0.0136 559  LEU B CG  
13208 C CD1 . LEU B 561  ? 0.2660 0.2156 0.2377 -0.0127 -0.0144 -0.0118 559  LEU B CD1 
13209 C CD2 . LEU B 561  ? 0.2552 0.2091 0.2309 -0.0087 -0.0128 -0.0147 559  LEU B CD2 
13210 N N   . ALA B 562  ? 0.2491 0.1836 0.2125 -0.0154 -0.0156 -0.0170 560  ALA B N   
13211 C CA  . ALA B 562  ? 0.2680 0.1950 0.2278 -0.0152 -0.0163 -0.0182 560  ALA B CA  
13212 C C   . ALA B 562  ? 0.3013 0.2292 0.2611 -0.0141 -0.0156 -0.0203 560  ALA B C   
13213 O O   . ALA B 562  ? 0.2960 0.2195 0.2544 -0.0116 -0.0154 -0.0217 560  ALA B O   
13214 C CB  . ALA B 562  ? 0.2834 0.2060 0.2397 -0.0193 -0.0177 -0.0173 560  ALA B CB  
13215 N N   . SER B 563  ? 0.2630 0.1964 0.2241 -0.0159 -0.0153 -0.0204 561  SER B N   
13216 C CA  . SER B 563  ? 0.2498 0.1842 0.2107 -0.0150 -0.0147 -0.0223 561  SER B CA  
13217 C C   . SER B 563  ? 0.2641 0.2016 0.2279 -0.0110 -0.0133 -0.0230 561  SER B C   
13218 O O   . SER B 563  ? 0.2900 0.2253 0.2528 -0.0089 -0.0127 -0.0247 561  SER B O   
13219 C CB  . SER B 563  ? 0.2898 0.2295 0.2515 -0.0179 -0.0148 -0.0221 561  SER B CB  
13220 O OG  . SER B 563  ? 0.3400 0.2872 0.3057 -0.0176 -0.0140 -0.0210 561  SER B OG  
13221 N N   . LEU B 564  ? 0.2548 0.1973 0.2221 -0.0099 -0.0127 -0.0218 562  LEU B N   
13222 C CA  . LEU B 564  ? 0.2622 0.2078 0.2326 -0.0064 -0.0114 -0.0223 562  LEU B CA  
13223 C C   . LEU B 564  ? 0.2684 0.2087 0.2378 -0.0035 -0.0114 -0.0229 562  LEU B C   
13224 O O   . LEU B 564  ? 0.2647 0.2051 0.2348 -0.0009 -0.0104 -0.0242 562  LEU B O   
13225 C CB  . LEU B 564  ? 0.2575 0.2089 0.2315 -0.0062 -0.0110 -0.0209 562  LEU B CB  
13226 C CG  . LEU B 564  ? 0.2700 0.2250 0.2473 -0.0031 -0.0099 -0.0212 562  LEU B CG  
13227 C CD1 . LEU B 564  ? 0.2879 0.2458 0.2660 -0.0024 -0.0090 -0.0224 562  LEU B CD1 
13228 C CD2 . LEU B 564  ? 0.2964 0.2563 0.2765 -0.0033 -0.0098 -0.0198 562  LEU B CD2 
13229 N N   . THR B 565  ? 0.2625 0.1981 0.2302 -0.0040 -0.0124 -0.0220 563  THR B N   
13230 C CA  . THR B 565  ? 0.2583 0.1885 0.2250 -0.0011 -0.0125 -0.0225 563  THR B CA  
13231 C C   . THR B 565  ? 0.2858 0.2119 0.2498 0.0000  -0.0121 -0.0245 563  THR B C   
13232 O O   . THR B 565  ? 0.2849 0.2105 0.2499 0.0034  -0.0112 -0.0255 563  THR B O   
13233 C CB  . THR B 565  ? 0.2793 0.2040 0.2434 -0.0024 -0.0140 -0.0212 563  THR B CB  
13234 O OG1 . THR B 565  ? 0.2919 0.2203 0.2583 -0.0030 -0.0142 -0.0194 563  THR B OG1 
13235 C CG2 . THR B 565  ? 0.2981 0.2166 0.2608 0.0007  -0.0142 -0.0218 563  THR B CG2 
13236 N N   . GLU B 566  ? 0.2716 0.1950 0.2323 -0.0028 -0.0128 -0.0252 564  GLU B N   
13237 C CA  . GLU B 566  ? 0.2744 0.1932 0.2318 -0.0020 -0.0125 -0.0273 564  GLU B CA  
13238 C C   . GLU B 566  ? 0.2674 0.1914 0.2270 0.0000  -0.0109 -0.0284 564  GLU B C   
13239 O O   . GLU B 566  ? 0.2760 0.1976 0.2347 0.0028  -0.0100 -0.0299 564  GLU B O   
13240 C CB  . GLU B 566  ? 0.3035 0.2185 0.2568 -0.0058 -0.0138 -0.0276 564  GLU B CB  
13241 C CG  . GLU B 566  ? 0.4140 0.3224 0.3645 -0.0075 -0.0153 -0.0266 564  GLU B CG  
13242 C CD  . GLU B 566  ? 0.5336 0.4367 0.4836 -0.0039 -0.0152 -0.0268 564  GLU B CD  
13243 O OE1 . GLU B 566  ? 0.5851 0.4845 0.5333 -0.0012 -0.0146 -0.0286 564  GLU B OE1 
13244 O OE2 . GLU B 566  ? 0.5154 0.4182 0.4666 -0.0037 -0.0158 -0.0251 564  GLU B OE2 
13245 N N   . ALA B 567  ? 0.2560 0.1868 0.2182 -0.0016 -0.0106 -0.0278 565  ALA B N   
13246 C CA  . ALA B 567  ? 0.2812 0.2168 0.2453 0.0000  -0.0092 -0.0287 565  ALA B CA  
13247 C C   . ALA B 567  ? 0.2534 0.1912 0.2208 0.0038  -0.0079 -0.0286 565  ALA B C   
13248 O O   . ALA B 567  ? 0.2549 0.1936 0.2226 0.0061  -0.0066 -0.0298 565  ALA B O   
13249 C CB  . ALA B 567  ? 0.2740 0.2163 0.2404 -0.0023 -0.0092 -0.0277 565  ALA B CB  
13250 N N   . LEU B 568  ? 0.2403 0.1792 0.2103 0.0044  -0.0083 -0.0271 566  LEU B N   
13251 C CA  . LEU B 568  ? 0.2380 0.1792 0.2114 0.0078  -0.0073 -0.0269 566  LEU B CA  
13252 C C   . LEU B 568  ? 0.2499 0.1857 0.2215 0.0107  -0.0069 -0.0280 566  LEU B C   
13253 O O   . LEU B 568  ? 0.2497 0.1873 0.2231 0.0135  -0.0055 -0.0288 566  LEU B O   
13254 C CB  . LEU B 568  ? 0.2508 0.1939 0.2267 0.0076  -0.0080 -0.0251 566  LEU B CB  
13255 C CG  . LEU B 568  ? 0.2313 0.1802 0.2093 0.0053  -0.0082 -0.0240 566  LEU B CG  
13256 C CD1 . LEU B 568  ? 0.2652 0.2149 0.2448 0.0050  -0.0090 -0.0223 566  LEU B CD1 
13257 C CD2 . LEU B 568  ? 0.2754 0.2301 0.2566 0.0066  -0.0068 -0.0243 566  LEU B CD2 
13258 N N   . ARG B 569  ? 0.2579 0.1870 0.2261 0.0100  -0.0081 -0.0281 567  ARG B N   
13259 C CA  . ARG B 569  ? 0.2685 0.1917 0.2344 0.0128  -0.0078 -0.0294 567  ARG B CA  
13260 C C   . ARG B 569  ? 0.2683 0.1909 0.2323 0.0138  -0.0065 -0.0314 567  ARG B C   
13261 O O   . ARG B 569  ? 0.3156 0.2380 0.2804 0.0172  -0.0052 -0.0324 567  ARG B O   
13262 C CB  . ARG B 569  ? 0.2923 0.2079 0.2542 0.0113  -0.0094 -0.0292 567  ARG B CB  
13263 C CG  . ARG B 569  ? 0.3781 0.2932 0.3416 0.0114  -0.0105 -0.0272 567  ARG B CG  
13264 C CD  . ARG B 569  ? 0.4294 0.3366 0.3887 0.0098  -0.0122 -0.0268 567  ARG B CD  
13265 N NE  . ARG B 569  ? 0.4732 0.3806 0.4339 0.0094  -0.0133 -0.0247 567  ARG B NE  
13266 C CZ  . ARG B 569  ? 0.4752 0.3774 0.4329 0.0071  -0.0148 -0.0236 567  ARG B CZ  
13267 N NH1 . ARG B 569  ? 0.5531 0.4494 0.5063 0.0048  -0.0156 -0.0244 567  ARG B NH1 
13268 N NH2 . ARG B 569  ? 0.5375 0.4406 0.4967 0.0070  -0.0157 -0.0215 567  ARG B NH2 
13269 N N   . GLU B 570  ? 0.2649 0.1875 0.2263 0.0108  -0.0069 -0.0320 568  GLU B N   
13270 C CA  . GLU B 570  ? 0.2935 0.2153 0.2523 0.0114  -0.0058 -0.0340 568  GLU B CA  
13271 C C   . GLU B 570  ? 0.3043 0.2328 0.2669 0.0136  -0.0040 -0.0341 568  GLU B C   
13272 O O   . GLU B 570  ? 0.3212 0.2489 0.2826 0.0158  -0.0026 -0.0356 568  GLU B O   
13273 C CB  . GLU B 570  ? 0.3281 0.2493 0.2837 0.0075  -0.0069 -0.0344 568  GLU B CB  
13274 C CG  . GLU B 570  ? 0.3648 0.2782 0.3157 0.0053  -0.0086 -0.0348 568  GLU B CG  
13275 C CD  . GLU B 570  ? 0.5099 0.4246 0.4594 0.0007  -0.0100 -0.0342 568  GLU B CD  
13276 O OE1 . GLU B 570  ? 0.4781 0.3991 0.4296 -0.0005 -0.0096 -0.0339 568  GLU B OE1 
13277 O OE2 . GLU B 570  ? 0.5306 0.4399 0.4771 -0.0018 -0.0116 -0.0339 568  GLU B OE2 
13278 N N   . SER B 571  ? 0.2860 0.2211 0.2530 0.0129  -0.0039 -0.0324 569  SER B N   
13279 C CA  . SER B 571  ? 0.2818 0.2231 0.2524 0.0147  -0.0023 -0.0323 569  SER B CA  
13280 C C   . SER B 571  ? 0.3271 0.2681 0.2998 0.0185  -0.0010 -0.0326 569  SER B C   
13281 O O   . SER B 571  ? 0.3381 0.2820 0.3120 0.0205  0.0007  -0.0333 569  SER B O   
13282 C CB  . SER B 571  ? 0.2908 0.2384 0.2656 0.0132  -0.0026 -0.0306 569  SER B CB  
13283 O OG  . SER B 571  ? 0.2945 0.2429 0.2724 0.0144  -0.0030 -0.0293 569  SER B OG  
13284 N N   . ALA B 572  ? 0.2897 0.2274 0.2628 0.0197  -0.0018 -0.0321 570  ALA B N   
13285 C CA  . ALA B 572  ? 0.2847 0.2225 0.2602 0.0236  -0.0008 -0.0322 570  ALA B CA  
13286 C C   . ALA B 572  ? 0.3544 0.2870 0.3262 0.0259  0.0003  -0.0342 570  ALA B C   
13287 O O   . ALA B 572  ? 0.4206 0.3545 0.3946 0.0293  0.0018  -0.0346 570  ALA B O   
13288 C CB  . ALA B 572  ? 0.3161 0.2522 0.2933 0.0242  -0.0021 -0.0308 570  ALA B CB  
13289 N N   . ALA B 573  ? 0.3069 0.2341 0.2734 0.0241  -0.0003 -0.0355 571  ALA B N   
13290 C CA  . ALA B 573  ? 0.3788 0.3008 0.3412 0.0262  0.0007  -0.0377 571  ALA B CA  
13291 C C   . ALA B 573  ? 0.3794 0.3046 0.3409 0.0264  0.0024  -0.0390 571  ALA B C   
13292 O O   . ALA B 573  ? 0.3767 0.2984 0.3351 0.0286  0.0037  -0.0408 571  ALA B O   
13293 C CB  . ALA B 573  ? 0.3932 0.3069 0.3499 0.0241  -0.0010 -0.0386 571  ALA B CB  
13294 N N   . MET B 574  ? 0.3386 0.2701 0.3026 0.0244  0.0026  -0.0380 572  MET B N   
13295 C CA  . MET B 574  ? 0.3211 0.2558 0.2841 0.0244  0.0041  -0.0389 572  MET B CA  
13296 C C   . MET B 574  ? 0.3128 0.2521 0.2796 0.0279  0.0064  -0.0388 572  MET B C   
13297 O O   . MET B 574  ? 0.3172 0.2597 0.2888 0.0294  0.0065  -0.0374 572  MET B O   
13298 C CB  . MET B 574  ? 0.3121 0.2521 0.2768 0.0212  0.0033  -0.0377 572  MET B CB  
13299 C CG  . MET B 574  ? 0.3520 0.2886 0.3130 0.0175  0.0013  -0.0378 572  MET B CG  
13300 S SD  . MET B 574  ? 0.3465 0.2897 0.3107 0.0141  0.0003  -0.0359 572  MET B SD  
13301 C CE  . MET B 574  ? 0.3460 0.2842 0.3055 0.0102  -0.0020 -0.0363 572  MET B CE  
13302 N N   . LYS B 575  ? 0.2940 0.2337 0.2585 0.0291  0.0081  -0.0402 573  LYS B N   
13303 C CA  . LYS B 575  ? 0.2825 0.2272 0.2505 0.0320  0.0105  -0.0400 573  LYS B CA  
13304 C C   . LYS B 575  ? 0.2824 0.2342 0.2538 0.0302  0.0108  -0.0385 573  LYS B C   
13305 O O   . LYS B 575  ? 0.2964 0.2491 0.2651 0.0285  0.0110  -0.0390 573  LYS B O   
13306 C CB  . LYS B 575  ? 0.3043 0.2460 0.2679 0.0341  0.0124  -0.0422 573  LYS B CB  
13307 C CG  . LYS B 575  ? 0.3700 0.3170 0.3368 0.0371  0.0151  -0.0421 573  LYS B CG  
13308 C CD  . LYS B 575  ? 0.4225 0.3657 0.3842 0.0394  0.0170  -0.0444 573  LYS B CD  
13309 C CE  . LYS B 575  ? 0.5445 0.4927 0.5094 0.0427  0.0200  -0.0443 573  LYS B CE  
13310 N NZ  . LYS B 575  ? 0.5426 0.4968 0.5085 0.0412  0.0211  -0.0435 573  LYS B NZ  
13311 N N   . TRP B 576  ? 0.2748 0.2314 0.2519 0.0305  0.0106  -0.0367 574  TRP B N   
13312 C CA  . TRP B 576  ? 0.2401 0.2032 0.2208 0.0289  0.0107  -0.0352 574  TRP B CA  
13313 C C   . TRP B 576  ? 0.2389 0.2068 0.2226 0.0313  0.0131  -0.0349 574  TRP B C   
13314 O O   . TRP B 576  ? 0.2561 0.2252 0.2431 0.0339  0.0140  -0.0346 574  TRP B O   
13315 C CB  . TRP B 576  ? 0.2214 0.1868 0.2064 0.0278  0.0092  -0.0334 574  TRP B CB  
13316 C CG  . TRP B 576  ? 0.2325 0.1942 0.2150 0.0251  0.0069  -0.0332 574  TRP B CG  
13317 C CD1 . TRP B 576  ? 0.2806 0.2383 0.2626 0.0252  0.0055  -0.0331 574  TRP B CD1 
13318 C CD2 . TRP B 576  ? 0.2273 0.1895 0.2077 0.0220  0.0059  -0.0331 574  TRP B CD2 
13319 N NE1 . TRP B 576  ? 0.2715 0.2271 0.2512 0.0221  0.0037  -0.0328 574  TRP B NE1 
13320 C CE2 . TRP B 576  ? 0.2661 0.2246 0.2450 0.0202  0.0039  -0.0328 574  TRP B CE2 
13321 C CE3 . TRP B 576  ? 0.2260 0.1916 0.2060 0.0205  0.0063  -0.0330 574  TRP B CE3 
13322 C CZ2 . TRP B 576  ? 0.2770 0.2355 0.2541 0.0169  0.0025  -0.0325 574  TRP B CZ2 
13323 C CZ3 . TRP B 576  ? 0.2372 0.2026 0.2153 0.0175  0.0048  -0.0327 574  TRP B CZ3 
13324 C CH2 . TRP B 576  ? 0.2664 0.2285 0.2433 0.0157  0.0030  -0.0325 574  TRP B CH2 
13325 N N   . THR B 577  ? 0.2552 0.2261 0.2381 0.0302  0.0141  -0.0349 575  THR B N   
13326 C CA  . THR B 577  ? 0.2315 0.2070 0.2168 0.0321  0.0165  -0.0345 575  THR B CA  
13327 C C   . THR B 577  ? 0.2270 0.2076 0.2147 0.0299  0.0163  -0.0329 575  THR B C   
13328 O O   . THR B 577  ? 0.2232 0.2034 0.2094 0.0273  0.0147  -0.0326 575  THR B O   
13329 C CB  . THR B 577  ? 0.2565 0.2297 0.2371 0.0335  0.0183  -0.0363 575  THR B CB  
13330 O OG1 . THR B 577  ? 0.3046 0.2764 0.2808 0.0309  0.0174  -0.0368 575  THR B OG1 
13331 C CG2 . THR B 577  ? 0.2706 0.2379 0.2481 0.0356  0.0184  -0.0381 575  THR B CG2 
13332 N N   . ALA B 578  ? 0.2203 0.2060 0.2119 0.0311  0.0180  -0.0319 576  ALA B N   
13333 C CA  . ALA B 578  ? 0.2177 0.2080 0.2112 0.0294  0.0182  -0.0305 576  ALA B CA  
13334 C C   . ALA B 578  ? 0.1981 0.1915 0.1921 0.0312  0.0209  -0.0305 576  ALA B C   
13335 O O   . ALA B 578  ? 0.2219 0.2171 0.2190 0.0335  0.0223  -0.0303 576  ALA B O   
13336 C CB  . ALA B 578  ? 0.1973 0.1911 0.1963 0.0286  0.0171  -0.0287 576  ALA B CB  
13337 N N   . LEU B 579  ? 0.2079 0.2019 0.1987 0.0301  0.0217  -0.0306 577  LEU B N   
13338 C CA  . LEU B 579  ? 0.2056 0.2022 0.1958 0.0316  0.0243  -0.0307 577  LEU B CA  
13339 C C   . LEU B 579  ? 0.2023 0.2031 0.1940 0.0298  0.0246  -0.0289 577  LEU B C   
13340 O O   . LEU B 579  ? 0.1988 0.1995 0.1903 0.0275  0.0227  -0.0282 577  LEU B O   
13341 C CB  . LEU B 579  ? 0.2600 0.2523 0.2434 0.0321  0.0251  -0.0327 577  LEU B CB  
13342 C CG  . LEU B 579  ? 0.3148 0.3012 0.2949 0.0331  0.0242  -0.0347 577  LEU B CG  
13343 C CD1 . LEU B 579  ? 0.3224 0.3042 0.2952 0.0332  0.0246  -0.0368 577  LEU B CD1 
13344 C CD2 . LEU B 579  ? 0.2886 0.2757 0.2721 0.0362  0.0257  -0.0349 577  LEU B CD2 
13345 N N   . PRO B 580  ? 0.2093 0.2139 0.2025 0.0309  0.0270  -0.0282 578  PRO B N   
13346 C CA  . PRO B 580  ? 0.1968 0.2045 0.1900 0.0292  0.0273  -0.0267 578  PRO B CA  
13347 C C   . PRO B 580  ? 0.1919 0.1965 0.1786 0.0281  0.0270  -0.0278 578  PRO B C   
13348 O O   . PRO B 580  ? 0.2356 0.2390 0.2184 0.0294  0.0287  -0.0290 578  PRO B O   
13349 C CB  . PRO B 580  ? 0.2210 0.2330 0.2169 0.0307  0.0302  -0.0258 578  PRO B CB  
13350 C CG  . PRO B 580  ? 0.2347 0.2468 0.2336 0.0332  0.0310  -0.0265 578  PRO B CG  
13351 C CD  . PRO B 580  ? 0.2069 0.2131 0.2016 0.0337  0.0295  -0.0286 578  PRO B CD  
13352 N N   . GLN B 581  ? 0.2003 0.2037 0.1859 0.0259  0.0247  -0.0274 579  GLN B N   
13353 C CA  . GLN B 581  ? 0.2116 0.2122 0.1914 0.0246  0.0238  -0.0283 579  GLN B CA  
13354 C C   . GLN B 581  ? 0.2382 0.2420 0.2177 0.0234  0.0242  -0.0267 579  GLN B C   
13355 O O   . GLN B 581  ? 0.2310 0.2362 0.2124 0.0217  0.0227  -0.0253 579  GLN B O   
13356 C CB  . GLN B 581  ? 0.2198 0.2176 0.1988 0.0229  0.0210  -0.0288 579  GLN B CB  
13357 C CG  . GLN B 581  ? 0.2314 0.2256 0.2102 0.0239  0.0204  -0.0303 579  GLN B CG  
13358 C CD  . GLN B 581  ? 0.2717 0.2616 0.2448 0.0249  0.0211  -0.0325 579  GLN B CD  
13359 O OE1 . GLN B 581  ? 0.2877 0.2773 0.2565 0.0248  0.0220  -0.0330 579  GLN B OE1 
13360 N NE2 . GLN B 581  ? 0.3674 0.3535 0.3399 0.0259  0.0206  -0.0339 579  GLN B NE2 
13361 N N   . LEU B 582  ? 0.2218 0.2266 0.1989 0.0244  0.0265  -0.0268 580  LEU B N   
13362 C CA  . LEU B 582  ? 0.2237 0.2311 0.1998 0.0233  0.0271  -0.0252 580  LEU B CA  
13363 C C   . LEU B 582  ? 0.2313 0.2361 0.2013 0.0220  0.0257  -0.0260 580  LEU B C   
13364 O O   . LEU B 582  ? 0.2616 0.2625 0.2279 0.0220  0.0247  -0.0280 580  LEU B O   
13365 C CB  . LEU B 582  ? 0.2532 0.2635 0.2297 0.0249  0.0302  -0.0246 580  LEU B CB  
13366 C CG  . LEU B 582  ? 0.2881 0.3027 0.2715 0.0252  0.0312  -0.0227 580  LEU B CG  
13367 C CD1 . LEU B 582  ? 0.2771 0.2914 0.2647 0.0265  0.0309  -0.0234 580  LEU B CD1 
13368 C CD2 . LEU B 582  ? 0.3481 0.3661 0.3316 0.0262  0.0342  -0.0218 580  LEU B CD2 
13369 N N   . ALA B 583  ? 0.2447 0.2515 0.2136 0.0208  0.0256  -0.0245 581  ALA B N   
13370 C CA  . ALA B 583  ? 0.2876 0.2925 0.2511 0.0195  0.0241  -0.0250 581  ALA B CA  
13371 C C   . ALA B 583  ? 0.3246 0.3264 0.2819 0.0204  0.0253  -0.0272 581  ALA B C   
13372 O O   . ALA B 583  ? 0.3451 0.3438 0.2979 0.0194  0.0235  -0.0285 581  ALA B O   
13373 C CB  . ALA B 583  ? 0.3026 0.3103 0.2659 0.0184  0.0242  -0.0227 581  ALA B CB  
13374 N N   . THR B 584  ? 0.2743 0.2770 0.2315 0.0224  0.0281  -0.0276 582  THR B N   
13375 C CA  . THR B 584  ? 0.3022 0.3022 0.2534 0.0237  0.0297  -0.0296 582  THR B CA  
13376 C C   . THR B 584  ? 0.2735 0.2698 0.2241 0.0252  0.0298  -0.0320 582  THR B C   
13377 O O   . THR B 584  ? 0.2850 0.2784 0.2306 0.0266  0.0311  -0.0340 582  THR B O   
13378 C CB  . THR B 584  ? 0.3242 0.3274 0.2755 0.0252  0.0330  -0.0287 582  THR B CB  
13379 O OG1 . THR B 584  ? 0.3412 0.3478 0.2995 0.0262  0.0343  -0.0275 582  THR B OG1 
13380 C CG2 . THR B 584  ? 0.4160 0.4217 0.3658 0.0236  0.0329  -0.0266 582  THR B CG2 
13381 N N   . GLY B 585  ? 0.2869 0.2828 0.2422 0.0251  0.0284  -0.0319 583  GLY B N   
13382 C CA  . GLY B 585  ? 0.2524 0.2446 0.2074 0.0264  0.0282  -0.0339 583  GLY B CA  
13383 C C   . GLY B 585  ? 0.2670 0.2618 0.2286 0.0280  0.0293  -0.0331 583  GLY B C   
13384 O O   . GLY B 585  ? 0.2739 0.2734 0.2402 0.0280  0.0302  -0.0310 583  GLY B O   
13385 N N   . PRO B 586  ? 0.2505 0.2421 0.2126 0.0294  0.0290  -0.0346 584  PRO B N   
13386 C CA  . PRO B 586  ? 0.2331 0.2272 0.2015 0.0310  0.0299  -0.0338 584  PRO B CA  
13387 C C   . PRO B 586  ? 0.2801 0.2776 0.2501 0.0335  0.0332  -0.0335 584  PRO B C   
13388 O O   . PRO B 586  ? 0.2762 0.2719 0.2415 0.0350  0.0351  -0.0351 584  PRO B O   
13389 C CB  . PRO B 586  ? 0.2923 0.2814 0.2595 0.0320  0.0286  -0.0356 584  PRO B CB  
13390 C CG  . PRO B 586  ? 0.3205 0.3047 0.2802 0.0320  0.0287  -0.0379 584  PRO B CG  
13391 C CD  . PRO B 586  ? 0.2919 0.2775 0.2490 0.0294  0.0277  -0.0370 584  PRO B CD  
13392 N N   . ALA B 587  ? 0.2414 0.2437 0.2179 0.0338  0.0339  -0.0316 585  ALA B N   
13393 C CA  . ALA B 587  ? 0.2426 0.2490 0.2217 0.0360  0.0370  -0.0309 585  ALA B CA  
13394 C C   . ALA B 587  ? 0.2509 0.2573 0.2338 0.0385  0.0377  -0.0316 585  ALA B C   
13395 O O   . ALA B 587  ? 0.2540 0.2585 0.2392 0.0382  0.0356  -0.0318 585  ALA B O   
13396 C CB  . ALA B 587  ? 0.2658 0.2780 0.2500 0.0344  0.0374  -0.0282 585  ALA B CB  
13397 N N   . ALA B 588  ? 0.2668 0.2755 0.2502 0.0412  0.0408  -0.0320 586  ALA B N   
13398 C CA  . ALA B 588  ? 0.2435 0.2532 0.2312 0.0439  0.0417  -0.0323 586  ALA B CA  
13399 C C   . ALA B 588  ? 0.2549 0.2703 0.2507 0.0432  0.0412  -0.0299 586  ALA B C   
13400 O O   . ALA B 588  ? 0.2797 0.2991 0.2777 0.0411  0.0413  -0.0279 586  ALA B O   
13401 C CB  . ALA B 588  ? 0.2482 0.2596 0.2345 0.0471  0.0453  -0.0333 586  ALA B CB  
13402 N N   . GLY B 589  ? 0.2427 0.2582 0.2427 0.0449  0.0406  -0.0300 587  GLY B N   
13403 C CA  . GLY B 589  ? 0.2550 0.2759 0.2626 0.0443  0.0402  -0.0277 587  GLY B CA  
13404 C C   . GLY B 589  ? 0.2703 0.2909 0.2817 0.0468  0.0397  -0.0282 587  GLY B C   
13405 O O   . GLY B 589  ? 0.2932 0.3095 0.3013 0.0491  0.0401  -0.0302 587  GLY B O   
13406 N N   . GLU B 590  ? 0.2550 0.2799 0.2731 0.0461  0.0387  -0.0263 588  GLU B N   
13407 C CA  . GLU B 590  ? 0.2754 0.3006 0.2977 0.0483  0.0380  -0.0264 588  GLU B CA  
13408 C C   . GLU B 590  ? 0.2483 0.2676 0.2682 0.0472  0.0348  -0.0272 588  GLU B C   
13409 O O   . GLU B 590  ? 0.2435 0.2620 0.2633 0.0442  0.0325  -0.0264 588  GLU B O   
13410 C CB  . GLU B 590  ? 0.2949 0.3268 0.3250 0.0476  0.0377  -0.0240 588  GLU B CB  
13411 C CG  . GLU B 590  ? 0.4134 0.4519 0.4469 0.0486  0.0409  -0.0228 588  GLU B CG  
13412 C CD  . GLU B 590  ? 0.5088 0.5479 0.5422 0.0527  0.0436  -0.0241 588  GLU B CD  
13413 O OE1 . GLU B 590  ? 0.5528 0.5900 0.5876 0.0550  0.0426  -0.0249 588  GLU B OE1 
13414 O OE2 . GLU B 590  ? 0.6348 0.6760 0.6663 0.0538  0.0467  -0.0244 588  GLU B OE2 
13415 N N   . THR B 591  ? 0.2526 0.2678 0.2708 0.0498  0.0346  -0.0288 589  THR B N   
13416 C CA  . THR B 591  ? 0.2618 0.2707 0.2769 0.0489  0.0318  -0.0298 589  THR B CA  
13417 C C   . THR B 591  ? 0.2454 0.2548 0.2653 0.0503  0.0302  -0.0291 589  THR B C   
13418 O O   . THR B 591  ? 0.2800 0.2922 0.3035 0.0533  0.0317  -0.0289 589  THR B O   
13419 C CB  . THR B 591  ? 0.2862 0.2886 0.2944 0.0505  0.0325  -0.0323 589  THR B CB  
13420 O OG1 . THR B 591  ? 0.2939 0.2960 0.2976 0.0491  0.0338  -0.0329 589  THR B OG1 
13421 C CG2 . THR B 591  ? 0.2952 0.2909 0.3000 0.0493  0.0296  -0.0332 589  THR B CG2 
13422 N N   . ARG B 592  ? 0.2489 0.2559 0.2689 0.0481  0.0273  -0.0286 590  ARG B N   
13423 C CA  . ARG B 592  ? 0.2896 0.2963 0.3132 0.0492  0.0255  -0.0279 590  ARG B CA  
13424 C C   . ARG B 592  ? 0.2637 0.2639 0.2833 0.0474  0.0228  -0.0286 590  ARG B C   
13425 O O   . ARG B 592  ? 0.2494 0.2469 0.2647 0.0449  0.0220  -0.0292 590  ARG B O   
13426 C CB  . ARG B 592  ? 0.2849 0.2980 0.3153 0.0480  0.0247  -0.0257 590  ARG B CB  
13427 C CG  . ARG B 592  ? 0.2899 0.3035 0.3199 0.0442  0.0230  -0.0247 590  ARG B CG  
13428 C CD  . ARG B 592  ? 0.3884 0.4065 0.4244 0.0431  0.0215  -0.0228 590  ARG B CD  
13429 N NE  . ARG B 592  ? 0.3505 0.3694 0.3862 0.0396  0.0203  -0.0219 590  ARG B NE  
13430 C CZ  . ARG B 592  ? 0.3436 0.3590 0.3771 0.0376  0.0179  -0.0220 590  ARG B CZ  
13431 N NH1 . ARG B 592  ? 0.3359 0.3467 0.3672 0.0383  0.0164  -0.0228 590  ARG B NH1 
13432 N NH2 . ARG B 592  ? 0.3479 0.3644 0.3814 0.0348  0.0170  -0.0212 590  ARG B NH2 
13433 N N   . THR B 593  ? 0.2894 0.2876 0.3106 0.0488  0.0212  -0.0284 591  THR B N   
13434 C CA  . THR B 593  ? 0.2654 0.2578 0.2832 0.0471  0.0186  -0.0288 591  THR B CA  
13435 C C   . THR B 593  ? 0.2518 0.2467 0.2721 0.0440  0.0165  -0.0272 591  THR B C   
13436 O O   . THR B 593  ? 0.2665 0.2672 0.2919 0.0436  0.0166  -0.0257 591  THR B O   
13437 C CB  . THR B 593  ? 0.2859 0.2749 0.3041 0.0497  0.0176  -0.0291 591  THR B CB  
13438 O OG1 . THR B 593  ? 0.3453 0.3398 0.3702 0.0510  0.0174  -0.0274 591  THR B OG1 
13439 C CG2 . THR B 593  ? 0.3983 0.3838 0.4134 0.0530  0.0197  -0.0309 591  THR B CG2 
13440 N N   . VAL B 594  ? 0.2360 0.2265 0.2524 0.0416  0.0146  -0.0276 592  VAL B N   
13441 C CA  . VAL B 594  ? 0.2185 0.2101 0.2364 0.0388  0.0125  -0.0263 592  VAL B CA  
13442 C C   . VAL B 594  ? 0.2565 0.2439 0.2736 0.0392  0.0104  -0.0262 592  VAL B C   
13443 O O   . VAL B 594  ? 0.2623 0.2438 0.2748 0.0394  0.0100  -0.0274 592  VAL B O   
13444 C CB  . VAL B 594  ? 0.2349 0.2251 0.2489 0.0358  0.0121  -0.0267 592  VAL B CB  
13445 C CG1 . VAL B 594  ? 0.2459 0.2371 0.2612 0.0331  0.0100  -0.0255 592  VAL B CG1 
13446 C CG2 . VAL B 594  ? 0.2683 0.2622 0.2827 0.0357  0.0142  -0.0268 592  VAL B CG2 
13447 N N   . LEU B 595  ? 0.2417 0.2319 0.2631 0.0393  0.0090  -0.0247 593  LEU B N   
13448 C CA  . LEU B 595  ? 0.2448 0.2315 0.2660 0.0399  0.0070  -0.0243 593  LEU B CA  
13449 C C   . LEU B 595  ? 0.2358 0.2220 0.2565 0.0369  0.0048  -0.0234 593  LEU B C   
13450 O O   . LEU B 595  ? 0.2679 0.2581 0.2906 0.0350  0.0047  -0.0226 593  LEU B O   
13451 C CB  . LEU B 595  ? 0.2418 0.2320 0.2682 0.0426  0.0070  -0.0233 593  LEU B CB  
13452 C CG  . LEU B 595  ? 0.2499 0.2416 0.2777 0.0459  0.0094  -0.0241 593  LEU B CG  
13453 C CD1 . LEU B 595  ? 0.2759 0.2719 0.3096 0.0483  0.0091  -0.0228 593  LEU B CD1 
13454 C CD2 . LEU B 595  ? 0.2769 0.2619 0.2995 0.0477  0.0101  -0.0258 593  LEU B CD2 
13455 N N   . ASN B 596  ? 0.2206 0.2018 0.2384 0.0365  0.0032  -0.0234 594  ASN B N   
13456 C CA  . ASN B 596  ? 0.2097 0.1902 0.2267 0.0338  0.0011  -0.0225 594  ASN B CA  
13457 C C   . ASN B 596  ? 0.2094 0.1943 0.2313 0.0341  0.0001  -0.0210 594  ASN B C   
13458 O O   . ASN B 596  ? 0.2065 0.1917 0.2308 0.0364  -0.0004 -0.0205 594  ASN B O   
13459 C CB  . ASN B 596  ? 0.2058 0.1799 0.2189 0.0338  -0.0003 -0.0228 594  ASN B CB  
13460 C CG  . ASN B 596  ? 0.2198 0.1926 0.2312 0.0309  -0.0022 -0.0220 594  ASN B CG  
13461 O OD1 . ASN B 596  ? 0.2296 0.2062 0.2436 0.0297  -0.0030 -0.0209 594  ASN B OD1 
13462 N ND2 . ASN B 596  ? 0.2657 0.2330 0.2726 0.0298  -0.0030 -0.0224 594  ASN B ND2 
13463 N N   . PRO B 597  ? 0.1886 0.1772 0.2122 0.0319  -0.0004 -0.0203 595  PRO B N   
13464 C CA  . PRO B 597  ? 0.2041 0.1967 0.2321 0.0319  -0.0016 -0.0189 595  PRO B CA  
13465 C C   . PRO B 597  ? 0.2075 0.1975 0.2349 0.0321  -0.0038 -0.0181 595  PRO B C   
13466 O O   . PRO B 597  ? 0.2038 0.1965 0.2348 0.0330  -0.0048 -0.0170 595  PRO B O   
13467 C CB  . PRO B 597  ? 0.2070 0.2025 0.2355 0.0292  -0.0017 -0.0186 595  PRO B CB  
13468 C CG  . PRO B 597  ? 0.2007 0.1926 0.2242 0.0275  -0.0014 -0.0195 595  PRO B CG  
13469 C CD  . PRO B 597  ? 0.1965 0.1857 0.2180 0.0293  0.0000  -0.0207 595  PRO B CD  
13470 N N   . GLY B 598  ? 0.2098 0.1945 0.2327 0.0311  -0.0046 -0.0184 596  GLY B N   
13471 C CA  . GLY B 598  ? 0.2096 0.1915 0.2316 0.0313  -0.0067 -0.0175 596  GLY B CA  
13472 C C   . GLY B 598  ? 0.2124 0.1911 0.2342 0.0342  -0.0068 -0.0176 596  GLY B C   
13473 O O   . GLY B 598  ? 0.2492 0.2257 0.2707 0.0347  -0.0086 -0.0166 596  GLY B O   
13474 N N   . ASP B 599  ? 0.2209 0.1991 0.2427 0.0362  -0.0049 -0.0187 597  ASP B N   
13475 C CA  . ASP B 599  ? 0.2306 0.2056 0.2522 0.0394  -0.0048 -0.0190 597  ASP B CA  
13476 C C   . ASP B 599  ? 0.2335 0.2102 0.2561 0.0414  -0.0023 -0.0202 597  ASP B C   
13477 O O   . ASP B 599  ? 0.2404 0.2138 0.2592 0.0410  -0.0011 -0.0217 597  ASP B O   
13478 C CB  . ASP B 599  ? 0.2370 0.2046 0.2532 0.0388  -0.0057 -0.0194 597  ASP B CB  
13479 C CG  . ASP B 599  ? 0.2676 0.2311 0.2834 0.0421  -0.0060 -0.0195 597  ASP B CG  
13480 O OD1 . ASP B 599  ? 0.2708 0.2372 0.2901 0.0452  -0.0048 -0.0197 597  ASP B OD1 
13481 O OD2 . ASP B 599  ? 0.3003 0.2576 0.3120 0.0416  -0.0073 -0.0194 597  ASP B OD2 
13482 N N   . HIS B 600  ? 0.2230 0.2048 0.2507 0.0437  -0.0015 -0.0197 598  HIS B N   
13483 C CA  . HIS B 600  ? 0.2285 0.2127 0.2575 0.0456  0.0011  -0.0207 598  HIS B CA  
13484 C C   . HIS B 600  ? 0.2385 0.2172 0.2641 0.0483  0.0022  -0.0222 598  HIS B C   
13485 O O   . HIS B 600  ? 0.2927 0.2723 0.3180 0.0496  0.0045  -0.0234 598  HIS B O   
13486 C CB  . HIS B 600  ? 0.2696 0.2610 0.3052 0.0473  0.0018  -0.0197 598  HIS B CB  
13487 C CG  . HIS B 600  ? 0.2549 0.2516 0.2933 0.0445  0.0013  -0.0187 598  HIS B CG  
13488 N ND1 . HIS B 600  ? 0.3173 0.3207 0.3617 0.0452  0.0015  -0.0175 598  HIS B ND1 
13489 C CD2 . HIS B 600  ? 0.2365 0.2328 0.2728 0.0411  0.0007  -0.0187 598  HIS B CD2 
13490 C CE1 . HIS B 600  ? 0.3425 0.3488 0.3879 0.0422  0.0009  -0.0169 598  HIS B CE1 
13491 N NE2 . HIS B 600  ? 0.2783 0.2805 0.3189 0.0399  0.0005  -0.0176 598  HIS B NE2 
13492 N N   . ARG B 601  ? 0.2460 0.2189 0.2689 0.0491  0.0006  -0.0221 599  ARG B N   
13493 C CA  . ARG B 601  ? 0.2679 0.2346 0.2868 0.0514  0.0015  -0.0236 599  ARG B CA  
13494 C C   . ARG B 601  ? 0.2565 0.2187 0.2696 0.0490  0.0021  -0.0251 599  ARG B C   
13495 O O   . ARG B 601  ? 0.3066 0.2643 0.3163 0.0507  0.0034  -0.0268 599  ARG B O   
13496 C CB  . ARG B 601  ? 0.3120 0.2732 0.3294 0.0527  -0.0006 -0.0229 599  ARG B CB  
13497 C CG  . ARG B 601  ? 0.3222 0.2876 0.3452 0.0553  -0.0015 -0.0212 599  ARG B CG  
13498 C CD  . ARG B 601  ? 0.3355 0.2956 0.3567 0.0558  -0.0040 -0.0202 599  ARG B CD  
13499 N NE  . ARG B 601  ? 0.3420 0.3004 0.3606 0.0517  -0.0060 -0.0193 599  ARG B NE  
13500 C CZ  . ARG B 601  ? 0.3696 0.3232 0.3858 0.0512  -0.0083 -0.0183 599  ARG B CZ  
13501 N NH1 . ARG B 601  ? 0.4059 0.3557 0.4219 0.0543  -0.0091 -0.0179 599  ARG B NH1 
13502 N NH2 . ARG B 601  ? 0.3617 0.3142 0.3754 0.0474  -0.0097 -0.0176 599  ARG B NH2 
13503 N N   . ASP B 602  ? 0.2449 0.2083 0.2569 0.0452  0.0013  -0.0247 600  ASP B N   
13504 C CA  . ASP B 602  ? 0.2652 0.2247 0.2720 0.0426  0.0015  -0.0259 600  ASP B CA  
13505 C C   . ASP B 602  ? 0.2715 0.2355 0.2792 0.0422  0.0037  -0.0268 600  ASP B C   
13506 O O   . ASP B 602  ? 0.2630 0.2325 0.2736 0.0404  0.0038  -0.0259 600  ASP B O   
13507 C CB  . ASP B 602  ? 0.2673 0.2260 0.2727 0.0389  -0.0005 -0.0249 600  ASP B CB  
13508 C CG  . ASP B 602  ? 0.3082 0.2638 0.3087 0.0360  -0.0004 -0.0260 600  ASP B CG  
13509 O OD1 . ASP B 602  ? 0.3148 0.2666 0.3119 0.0369  0.0006  -0.0276 600  ASP B OD1 
13510 O OD2 . ASP B 602  ? 0.3061 0.2633 0.3064 0.0329  -0.0014 -0.0252 600  ASP B OD2 
13511 N N   . VAL B 603  ? 0.2679 0.2296 0.2731 0.0440  0.0055  -0.0284 601  VAL B N   
13512 C CA  . VAL B 603  ? 0.2455 0.2109 0.2509 0.0439  0.0077  -0.0293 601  VAL B CA  
13513 C C   . VAL B 603  ? 0.2633 0.2264 0.2642 0.0403  0.0072  -0.0299 601  VAL B C   
13514 O O   . VAL B 603  ? 0.3102 0.2670 0.3060 0.0396  0.0066  -0.0311 601  VAL B O   
13515 C CB  . VAL B 603  ? 0.2749 0.2384 0.2789 0.0474  0.0099  -0.0308 601  VAL B CB  
13516 C CG1 . VAL B 603  ? 0.2955 0.2627 0.2991 0.0470  0.0122  -0.0317 601  VAL B CG1 
13517 C CG2 . VAL B 603  ? 0.3055 0.2717 0.3144 0.0511  0.0103  -0.0301 601  VAL B CG2 
13518 N N   . VAL B 604  ? 0.2304 0.1986 0.2334 0.0381  0.0074  -0.0291 602  VAL B N   
13519 C CA  . VAL B 604  ? 0.2139 0.1808 0.2133 0.0348  0.0068  -0.0295 602  VAL B CA  
13520 C C   . VAL B 604  ? 0.2295 0.1962 0.2259 0.0350  0.0087  -0.0310 602  VAL B C   
13521 O O   . VAL B 604  ? 0.2518 0.2144 0.2434 0.0334  0.0082  -0.0321 602  VAL B O   
13522 C CB  . VAL B 604  ? 0.2186 0.1906 0.2213 0.0324  0.0060  -0.0280 602  VAL B CB  
13523 C CG1 . VAL B 604  ? 0.2360 0.2066 0.2352 0.0292  0.0052  -0.0283 602  VAL B CG1 
13524 C CG2 . VAL B 604  ? 0.2436 0.2159 0.2491 0.0324  0.0042  -0.0266 602  VAL B CG2 
13525 N N   . GLY B 605  ? 0.2274 0.1982 0.2264 0.0371  0.0108  -0.0311 603  GLY B N   
13526 C CA  . GLY B 605  ? 0.2401 0.2111 0.2362 0.0372  0.0126  -0.0324 603  GLY B CA  
13527 C C   . GLY B 605  ? 0.2327 0.2091 0.2327 0.0395  0.0149  -0.0320 603  GLY B C   
13528 O O   . GLY B 605  ? 0.2378 0.2168 0.2422 0.0415  0.0151  -0.0311 603  GLY B O   
13529 N N   . SER B 606  ? 0.2307 0.2090 0.2290 0.0391  0.0166  -0.0325 604  SER B N   
13530 C CA  A SER B 606  ? 0.2481 0.2316 0.2496 0.0411  0.0190  -0.0322 604  SER B CA  
13531 C CA  B SER B 606  ? 0.2477 0.2311 0.2491 0.0411  0.0191  -0.0322 604  SER B CA  
13532 C C   . SER B 606  ? 0.2411 0.2287 0.2429 0.0388  0.0197  -0.0314 604  SER B C   
13533 O O   . SER B 606  ? 0.2570 0.2423 0.2547 0.0366  0.0190  -0.0320 604  SER B O   
13534 C CB  A SER B 606  ? 0.3283 0.3090 0.3265 0.0440  0.0212  -0.0340 604  SER B CB  
13535 C CB  B SER B 606  ? 0.3286 0.3091 0.3264 0.0439  0.0212  -0.0341 604  SER B CB  
13536 O OG  A SER B 606  ? 0.3183 0.2953 0.3104 0.0426  0.0214  -0.0355 604  SER B OG  
13537 O OG  B SER B 606  ? 0.4272 0.4039 0.4250 0.0465  0.0209  -0.0348 604  SER B OG  
13538 N N   . VAL B 607  ? 0.2154 0.2091 0.2222 0.0393  0.0209  -0.0300 605  VAL B N   
13539 C CA  . VAL B 607  ? 0.1934 0.1912 0.2009 0.0374  0.0216  -0.0290 605  VAL B CA  
13540 C C   . VAL B 607  ? 0.2231 0.2246 0.2318 0.0394  0.0246  -0.0290 605  VAL B C   
13541 O O   . VAL B 607  ? 0.2179 0.2221 0.2305 0.0418  0.0258  -0.0287 605  VAL B O   
13542 C CB  . VAL B 607  ? 0.2015 0.2031 0.2139 0.0355  0.0201  -0.0271 605  VAL B CB  
13543 C CG1 . VAL B 607  ? 0.2241 0.2295 0.2424 0.0372  0.0203  -0.0260 605  VAL B CG1 
13544 C CG2 . VAL B 607  ? 0.2100 0.2152 0.2227 0.0336  0.0208  -0.0261 605  VAL B CG2 
13545 N N   . THR B 608  ? 0.2034 0.2051 0.2086 0.0384  0.0257  -0.0294 606  THR B N   
13546 C CA  . THR B 608  ? 0.2154 0.2212 0.2215 0.0397  0.0286  -0.0291 606  THR B CA  
13547 C C   . THR B 608  ? 0.1986 0.2091 0.2078 0.0373  0.0284  -0.0271 606  THR B C   
13548 O O   . THR B 608  ? 0.2220 0.2313 0.2287 0.0348  0.0272  -0.0269 606  THR B O   
13549 C CB  . THR B 608  ? 0.2342 0.2364 0.2337 0.0403  0.0300  -0.0309 606  THR B CB  
13550 O OG1 . THR B 608  ? 0.2489 0.2461 0.2456 0.0425  0.0300  -0.0329 606  THR B OG1 
13551 C CG2 . THR B 608  ? 0.2341 0.2406 0.2341 0.0415  0.0331  -0.0305 606  THR B CG2 
13552 N N   . GLU B 609  ? 0.2078 0.2238 0.2226 0.0380  0.0296  -0.0256 607  GLU B N   
13553 C CA  . GLU B 609  ? 0.2244 0.2444 0.2424 0.0356  0.0292  -0.0236 607  GLU B CA  
13554 C C   . GLU B 609  ? 0.2048 0.2277 0.2215 0.0354  0.0316  -0.0230 607  GLU B C   
13555 O O   . GLU B 609  ? 0.2272 0.2504 0.2419 0.0374  0.0340  -0.0239 607  GLU B O   
13556 C CB  . GLU B 609  ? 0.2487 0.2727 0.2736 0.0358  0.0285  -0.0220 607  GLU B CB  
13557 C CG  . GLU B 609  ? 0.2863 0.3071 0.3116 0.0354  0.0257  -0.0224 607  GLU B CG  
13558 C CD  . GLU B 609  ? 0.3248 0.3491 0.3563 0.0354  0.0246  -0.0210 607  GLU B CD  
13559 O OE1 . GLU B 609  ? 0.4136 0.4426 0.4494 0.0367  0.0262  -0.0201 607  GLU B OE1 
13560 O OE2 . GLU B 609  ? 0.3031 0.3257 0.3353 0.0340  0.0221  -0.0207 607  GLU B OE2 
13561 N N   . THR B 610  ? 0.2034 0.2282 0.2209 0.0329  0.0309  -0.0215 608  THR B N   
13562 C CA  . THR B 610  ? 0.1873 0.2136 0.2024 0.0320  0.0325  -0.0208 608  THR B CA  
13563 C C   . THR B 610  ? 0.2084 0.2406 0.2283 0.0324  0.0347  -0.0191 608  THR B C   
13564 O O   . THR B 610  ? 0.2263 0.2615 0.2517 0.0315  0.0337  -0.0176 608  THR B O   
13565 C CB  . THR B 610  ? 0.2138 0.2391 0.2277 0.0291  0.0305  -0.0199 608  THR B CB  
13566 O OG1 . THR B 610  ? 0.2084 0.2289 0.2187 0.0285  0.0283  -0.0213 608  THR B OG1 
13567 C CG2 . THR B 610  ? 0.2224 0.2485 0.2329 0.0282  0.0320  -0.0193 608  THR B CG2 
13568 N N   . SER B 611  ? 0.2049 0.2388 0.2228 0.0335  0.0375  -0.0192 609  SER B N   
13569 C CA  . SER B 611  ? 0.2172 0.2570 0.2395 0.0334  0.0396  -0.0172 609  SER B CA  
13570 C C   . SER B 611  ? 0.2624 0.3035 0.2852 0.0303  0.0387  -0.0152 609  SER B C   
13571 O O   . SER B 611  ? 0.2193 0.2570 0.2378 0.0289  0.0373  -0.0155 609  SER B O   
13572 C CB  . SER B 611  ? 0.2384 0.2797 0.2579 0.0353  0.0430  -0.0178 609  SER B CB  
13573 O OG  . SER B 611  ? 0.2477 0.2867 0.2612 0.0341  0.0433  -0.0180 609  SER B OG  
13574 N N   . GLU B 612  ? 0.2505 0.2965 0.2787 0.0294  0.0394  -0.0131 610  GLU B N   
13575 C CA  . GLU B 612  ? 0.2599 0.3067 0.2884 0.0266  0.0387  -0.0111 610  GLU B CA  
13576 C C   . GLU B 612  ? 0.2707 0.3168 0.2939 0.0262  0.0404  -0.0109 610  GLU B C   
13577 O O   . GLU B 612  ? 0.2757 0.3198 0.2963 0.0243  0.0391  -0.0102 610  GLU B O   
13578 C CB  . GLU B 612  ? 0.3038 0.3559 0.3391 0.0255  0.0391  -0.0089 610  GLU B CB  
13579 C CG  . GLU B 612  ? 0.3168 0.3691 0.3569 0.0256  0.0369  -0.0091 610  GLU B CG  
13580 C CD  . GLU B 612  ? 0.4556 0.5132 0.5026 0.0245  0.0371  -0.0069 610  GLU B CD  
13581 O OE1 . GLU B 612  ? 0.5429 0.6026 0.5908 0.0225  0.0377  -0.0050 610  GLU B OE1 
13582 O OE2 . GLU B 612  ? 0.4831 0.5426 0.5344 0.0255  0.0364  -0.0071 610  GLU B OE2 
13583 N N   . GLU B 613  ? 0.2515 0.2990 0.2726 0.0282  0.0433  -0.0117 611  GLU B N   
13584 C CA  . GLU B 613  ? 0.2569 0.3033 0.2721 0.0280  0.0448  -0.0117 611  GLU B CA  
13585 C C   . GLU B 613  ? 0.2584 0.2991 0.2675 0.0276  0.0427  -0.0134 611  GLU B C   
13586 O O   . GLU B 613  ? 0.2655 0.3047 0.2708 0.0260  0.0422  -0.0127 611  GLU B O   
13587 C CB  . GLU B 613  ? 0.3300 0.3787 0.3438 0.0305  0.0483  -0.0125 611  GLU B CB  
13588 N N   . ASP B 614  ? 0.2190 0.2563 0.2269 0.0290  0.0415  -0.0156 612  ASP B N   
13589 C CA  . ASP B 614  ? 0.2208 0.2529 0.2231 0.0284  0.0394  -0.0172 612  ASP B CA  
13590 C C   . ASP B 614  ? 0.2301 0.2610 0.2338 0.0260  0.0365  -0.0161 612  ASP B C   
13591 O O   . ASP B 614  ? 0.2241 0.2521 0.2235 0.0248  0.0351  -0.0165 612  ASP B O   
13592 C CB  . ASP B 614  ? 0.2514 0.2799 0.2519 0.0303  0.0389  -0.0197 612  ASP B CB  
13593 C CG  . ASP B 614  ? 0.2968 0.3246 0.2931 0.0326  0.0416  -0.0213 612  ASP B CG  
13594 O OD1 . ASP B 614  ? 0.3577 0.3865 0.3505 0.0323  0.0433  -0.0208 612  ASP B OD1 
13595 O OD2 . ASP B 614  ? 0.3095 0.3358 0.3059 0.0349  0.0421  -0.0231 612  ASP B OD2 
13596 N N   . ALA B 615  ? 0.2198 0.2529 0.2295 0.0253  0.0355  -0.0148 613  ALA B N   
13597 C CA  . ALA B 615  ? 0.2051 0.2372 0.2160 0.0231  0.0330  -0.0137 613  ALA B CA  
13598 C C   . ALA B 615  ? 0.2156 0.2486 0.2245 0.0214  0.0334  -0.0120 613  ALA B C   
13599 O O   . ALA B 615  ? 0.2057 0.2362 0.2117 0.0202  0.0316  -0.0119 613  ALA B O   
13600 C CB  . ALA B 615  ? 0.2406 0.2750 0.2579 0.0226  0.0320  -0.0127 613  ALA B CB  
13601 N N   . ARG B 616  ? 0.2337 0.2703 0.2441 0.0215  0.0358  -0.0105 614  ARG B N   
13602 C CA  . ARG B 616  ? 0.2301 0.2673 0.2383 0.0200  0.0363  -0.0087 614  ARG B CA  
13603 C C   . ARG B 616  ? 0.2159 0.2504 0.2172 0.0203  0.0366  -0.0098 614  ARG B C   
13604 O O   . ARG B 616  ? 0.2306 0.2637 0.2290 0.0190  0.0355  -0.0088 614  ARG B O   
13605 C CB  . ARG B 616  ? 0.2825 0.3243 0.2938 0.0198  0.0389  -0.0068 614  ARG B CB  
13606 C CG  . ARG B 616  ? 0.2875 0.3317 0.3053 0.0185  0.0380  -0.0051 614  ARG B CG  
13607 C CD  . ARG B 616  ? 0.3580 0.4068 0.3787 0.0178  0.0405  -0.0029 614  ARG B CD  
13608 N NE  . ARG B 616  ? 0.3795 0.4316 0.4022 0.0199  0.0430  -0.0037 614  ARG B NE  
13609 C CZ  . ARG B 616  ? 0.3778 0.4322 0.4059 0.0207  0.0427  -0.0040 614  ARG B CZ  
13610 N NH1 . ARG B 616  ? 0.3496 0.4031 0.3814 0.0194  0.0401  -0.0036 614  ARG B NH1 
13611 N NH2 . ARG B 616  ? 0.3654 0.4228 0.3950 0.0228  0.0451  -0.0046 614  ARG B NH2 
13612 N N   . ARG B 617  ? 0.2176 0.2512 0.2159 0.0222  0.0381  -0.0117 615  ARG B N   
13613 C CA  . ARG B 617  ? 0.2387 0.2694 0.2301 0.0225  0.0381  -0.0130 615  ARG B CA  
13614 C C   . ARG B 617  ? 0.2310 0.2580 0.2202 0.0214  0.0349  -0.0139 615  ARG B C   
13615 O O   . ARG B 617  ? 0.2323 0.2578 0.2173 0.0204  0.0340  -0.0135 615  ARG B O   
13616 C CB  . ARG B 617  ? 0.2737 0.3035 0.2624 0.0248  0.0399  -0.0154 615  ARG B CB  
13617 C CG  . ARG B 617  ? 0.2835 0.3100 0.2645 0.0251  0.0400  -0.0169 615  ARG B CG  
13618 C CD  . ARG B 617  ? 0.3673 0.3937 0.3452 0.0274  0.0428  -0.0186 615  ARG B CD  
13619 N NE  . ARG B 617  ? 0.4094 0.4337 0.3884 0.0292  0.0425  -0.0208 615  ARG B NE  
13620 C CZ  . ARG B 617  ? 0.4946 0.5142 0.4692 0.0296  0.0410  -0.0232 615  ARG B CZ  
13621 N NH1 . ARG B 617  ? 0.4224 0.4390 0.3913 0.0282  0.0395  -0.0236 615  ARG B NH1 
13622 N NH2 . ARG B 617  ? 0.4949 0.5125 0.4707 0.0313  0.0408  -0.0250 615  ARG B NH2 
13623 N N   . ALA B 618  ? 0.2147 0.2404 0.2069 0.0216  0.0331  -0.0148 616  ALA B N   
13624 C CA  . ALA B 618  ? 0.1895 0.2121 0.1801 0.0205  0.0302  -0.0155 616  ALA B CA  
13625 C C   . ALA B 618  ? 0.1973 0.2206 0.1885 0.0187  0.0288  -0.0135 616  ALA B C   
13626 O O   . ALA B 618  ? 0.2133 0.2347 0.2011 0.0178  0.0272  -0.0137 616  ALA B O   
13627 C CB  . ALA B 618  ? 0.2051 0.2268 0.1994 0.0209  0.0288  -0.0165 616  ALA B CB  
13628 N N   . VAL B 619  ? 0.2104 0.2364 0.2062 0.0181  0.0294  -0.0115 617  VAL B N   
13629 C CA  . VAL B 619  ? 0.2039 0.2299 0.2001 0.0165  0.0280  -0.0096 617  VAL B CA  
13630 C C   . VAL B 619  ? 0.2250 0.2509 0.2165 0.0160  0.0288  -0.0087 617  VAL B C   
13631 O O   . VAL B 619  ? 0.2326 0.2572 0.2220 0.0151  0.0271  -0.0080 617  VAL B O   
13632 C CB  . VAL B 619  ? 0.2069 0.2354 0.2088 0.0157  0.0283  -0.0077 617  VAL B CB  
13633 C CG1 . VAL B 619  ? 0.2368 0.2647 0.2388 0.0142  0.0269  -0.0058 617  VAL B CG1 
13634 C CG2 . VAL B 619  ? 0.2225 0.2507 0.2285 0.0161  0.0271  -0.0087 617  VAL B CG2 
13635 N N   . ARG B 620  ? 0.2297 0.2571 0.2193 0.0168  0.0314  -0.0086 618  ARG B N   
13636 C CA  . ARG B 620  ? 0.2651 0.2924 0.2496 0.0165  0.0322  -0.0079 618  ARG B CA  
13637 C C   . ARG B 620  ? 0.2174 0.2416 0.1964 0.0166  0.0306  -0.0096 618  ARG B C   
13638 O O   . ARG B 620  ? 0.2401 0.2634 0.2159 0.0157  0.0294  -0.0087 618  ARG B O   
13639 C CB  . ARG B 620  ? 0.2929 0.3224 0.2763 0.0175  0.0355  -0.0077 618  ARG B CB  
13640 C CG  . ARG B 620  ? 0.4769 0.5094 0.4629 0.0165  0.0370  -0.0049 618  ARG B CG  
13641 C CD  . ARG B 620  ? 0.4875 0.5227 0.4723 0.0175  0.0405  -0.0047 618  ARG B CD  
13642 N NE  . ARG B 620  ? 0.5635 0.6012 0.5533 0.0186  0.0419  -0.0054 618  ARG B NE  
13643 C CZ  . ARG B 620  ? 0.5107 0.5482 0.4994 0.0206  0.0433  -0.0076 618  ARG B CZ  
13644 N NH1 . ARG B 620  ? 0.5217 0.5565 0.5041 0.0216  0.0435  -0.0095 618  ARG B NH1 
13645 N NH2 . ARG B 620  ? 0.4489 0.4888 0.4427 0.0217  0.0443  -0.0080 618  ARG B NH2 
13646 N N   . LEU B 621  ? 0.2302 0.2527 0.2084 0.0176  0.0304  -0.0121 619  LEU B N   
13647 C CA  . LEU B 621  ? 0.2270 0.2465 0.2003 0.0175  0.0286  -0.0138 619  LEU B CA  
13648 C C   . LEU B 621  ? 0.2636 0.2821 0.2380 0.0161  0.0256  -0.0132 619  LEU B C   
13649 O O   . LEU B 621  ? 0.2605 0.2777 0.2309 0.0154  0.0241  -0.0133 619  LEU B O   
13650 C CB  . LEU B 621  ? 0.2452 0.2626 0.2177 0.0187  0.0288  -0.0165 619  LEU B CB  
13651 C CG  . LEU B 621  ? 0.2534 0.2712 0.2235 0.0204  0.0318  -0.0175 619  LEU B CG  
13652 C CD1 . LEU B 621  ? 0.2762 0.2920 0.2469 0.0219  0.0320  -0.0199 619  LEU B CD1 
13653 C CD2 . LEU B 621  ? 0.3248 0.3413 0.2879 0.0202  0.0323  -0.0181 619  LEU B CD2 
13654 N N   . ALA B 622  ? 0.2203 0.2396 0.2001 0.0158  0.0247  -0.0126 620  ALA B N   
13655 C CA  . ALA B 622  ? 0.2266 0.2452 0.2077 0.0148  0.0221  -0.0119 620  ALA B CA  
13656 C C   . ALA B 622  ? 0.2179 0.2375 0.1980 0.0139  0.0217  -0.0097 620  ALA B C   
13657 O O   . ALA B 622  ? 0.2232 0.2419 0.2013 0.0133  0.0198  -0.0094 620  ALA B O   
13658 C CB  . ALA B 622  ? 0.2190 0.2382 0.2058 0.0148  0.0214  -0.0118 620  ALA B CB  
13659 N N   . ALA B 623  ? 0.2173 0.2386 0.1987 0.0139  0.0236  -0.0079 621  ALA B N   
13660 C CA  . ALA B 623  ? 0.2188 0.2406 0.1990 0.0131  0.0232  -0.0056 621  ALA B CA  
13661 C C   . ALA B 623  ? 0.2445 0.2655 0.2186 0.0130  0.0230  -0.0058 621  ALA B C   
13662 O O   . ALA B 623  ? 0.2403 0.2608 0.2127 0.0124  0.0213  -0.0047 621  ALA B O   
13663 C CB  . ALA B 623  ? 0.2275 0.2513 0.2101 0.0129  0.0254  -0.0037 621  ALA B CB  
13664 N N   . ASP B 624  ? 0.2510 0.2717 0.2216 0.0137  0.0246  -0.0073 622  ASP B N   
13665 C CA  . ASP B 624  ? 0.2553 0.2750 0.2195 0.0136  0.0243  -0.0078 622  ASP B CA  
13666 C C   . ASP B 624  ? 0.2885 0.3066 0.2511 0.0130  0.0214  -0.0089 622  ASP B C   
13667 O O   . ASP B 624  ? 0.3603 0.3780 0.3191 0.0124  0.0201  -0.0081 622  ASP B O   
13668 C CB  . ASP B 624  ? 0.2942 0.3134 0.2550 0.0146  0.0265  -0.0097 622  ASP B CB  
13669 C CG  . ASP B 624  ? 0.3969 0.4183 0.3587 0.0152  0.0296  -0.0085 622  ASP B CG  
13670 O OD1 . ASP B 624  ? 0.4445 0.4675 0.4081 0.0145  0.0301  -0.0059 622  ASP B OD1 
13671 O OD2 . ASP B 624  ? 0.4526 0.4740 0.4134 0.0164  0.0317  -0.0101 622  ASP B OD2 
13672 N N   . ALA B 625  ? 0.3055 0.3226 0.2707 0.0132  0.0203  -0.0105 623  ALA B N   
13673 C CA  . ALA B 625  ? 0.3643 0.3801 0.3284 0.0126  0.0177  -0.0117 623  ALA B CA  
13674 C C   . ALA B 625  ? 0.3231 0.3399 0.2905 0.0119  0.0156  -0.0101 623  ALA B C   
13675 O O   . ALA B 625  ? 0.3035 0.3198 0.2701 0.0113  0.0134  -0.0107 623  ALA B O   
13676 C CB  . ALA B 625  ? 0.4209 0.4353 0.3864 0.0130  0.0176  -0.0140 623  ALA B CB  
13677 N N   . ALA B 626  ? 0.2584 0.2763 0.2296 0.0120  0.0163  -0.0082 624  ALA B N   
13678 C CA  . ALA B 626  ? 0.2426 0.2609 0.2172 0.0117  0.0145  -0.0071 624  ALA B CA  
13679 C C   . ALA B 626  ? 0.2444 0.2630 0.2164 0.0113  0.0125  -0.0061 624  ALA B C   
13680 O O   . ALA B 626  ? 0.2527 0.2714 0.2263 0.0111  0.0105  -0.0064 624  ALA B O   
13681 C CB  . ALA B 626  ? 0.2331 0.2523 0.2118 0.0118  0.0155  -0.0053 624  ALA B CB  
13682 N N   . PRO B 627  ? 0.2497 0.2685 0.2178 0.0111  0.0128  -0.0048 625  PRO B N   
13683 C CA  . PRO B 627  ? 0.2467 0.2660 0.2126 0.0108  0.0106  -0.0039 625  PRO B CA  
13684 C C   . PRO B 627  ? 0.2711 0.2901 0.2348 0.0103  0.0088  -0.0058 625  PRO B C   
13685 O O   . PRO B 627  ? 0.2605 0.2804 0.2252 0.0100  0.0066  -0.0053 625  PRO B O   
13686 C CB  . PRO B 627  ? 0.3198 0.3392 0.2812 0.0107  0.0116  -0.0024 625  PRO B CB  
13687 C CG  . PRO B 627  ? 0.3458 0.3652 0.3087 0.0110  0.0143  -0.0018 625  PRO B CG  
13688 C CD  . PRO B 627  ? 0.2787 0.2978 0.2446 0.0113  0.0151  -0.0040 625  PRO B CD  
13689 N N   . ASP B 628  ? 0.2573 0.2751 0.2182 0.0101  0.0096  -0.0079 626  ASP B N   
13690 C CA  . ASP B 628  ? 0.2827 0.3000 0.2412 0.0093  0.0078  -0.0097 626  ASP B CA  
13691 C C   . ASP B 628  ? 0.2795 0.2970 0.2424 0.0091  0.0065  -0.0105 626  ASP B C   
13692 O O   . ASP B 628  ? 0.2849 0.3031 0.2475 0.0083  0.0043  -0.0108 626  ASP B O   
13693 C CB  . ASP B 628  ? 0.3064 0.3217 0.2607 0.0093  0.0090  -0.0119 626  ASP B CB  
13694 C CG  . ASP B 628  ? 0.3917 0.4066 0.3407 0.0094  0.0101  -0.0113 626  ASP B CG  
13695 O OD1 . ASP B 628  ? 0.4196 0.4358 0.3669 0.0091  0.0090  -0.0095 626  ASP B OD1 
13696 O OD2 . ASP B 628  ? 0.4691 0.4826 0.4155 0.0099  0.0121  -0.0127 626  ASP B OD2 
13697 N N   . TRP B 629  ? 0.2268 0.2440 0.1938 0.0097  0.0078  -0.0108 627  TRP B N   
13698 C CA  . TRP B 629  ? 0.2287 0.2460 0.1994 0.0095  0.0066  -0.0115 627  TRP B CA  
13699 C C   . TRP B 629  ? 0.2161 0.2353 0.1899 0.0096  0.0052  -0.0096 627  TRP B C   
13700 O O   . TRP B 629  ? 0.2205 0.2405 0.1956 0.0092  0.0034  -0.0100 627  TRP B O   
13701 C CB  . TRP B 629  ? 0.2212 0.2376 0.1951 0.0101  0.0082  -0.0123 627  TRP B CB  
13702 C CG  . TRP B 629  ? 0.1865 0.2030 0.1640 0.0099  0.0070  -0.0130 627  TRP B CG  
13703 C CD1 . TRP B 629  ? 0.2281 0.2452 0.2102 0.0104  0.0072  -0.0123 627  TRP B CD1 
13704 C CD2 . TRP B 629  ? 0.2172 0.2331 0.1939 0.0090  0.0055  -0.0144 627  TRP B CD2 
13705 N NE1 . TRP B 629  ? 0.2023 0.2193 0.1863 0.0100  0.0060  -0.0132 627  TRP B NE1 
13706 C CE2 . TRP B 629  ? 0.1990 0.2154 0.1799 0.0091  0.0050  -0.0144 627  TRP B CE2 
13707 C CE3 . TRP B 629  ? 0.2230 0.2380 0.1957 0.0081  0.0044  -0.0156 627  TRP B CE3 
13708 C CZ2 . TRP B 629  ? 0.2199 0.2360 0.2012 0.0082  0.0035  -0.0155 627  TRP B CZ2 
13709 C CZ3 . TRP B 629  ? 0.2256 0.2402 0.1989 0.0071  0.0029  -0.0167 627  TRP B CZ3 
13710 C CH2 . TRP B 629  ? 0.2379 0.2533 0.2155 0.0072  0.0025  -0.0165 627  TRP B CH2 
13711 N N   . ALA B 630  ? 0.2169 0.2367 0.1917 0.0102  0.0059  -0.0077 628  ALA B N   
13712 C CA  . ALA B 630  ? 0.2300 0.2510 0.2072 0.0106  0.0046  -0.0060 628  ALA B CA  
13713 C C   . ALA B 630  ? 0.2400 0.2625 0.2150 0.0102  0.0025  -0.0055 628  ALA B C   
13714 O O   . ALA B 630  ? 0.2635 0.2874 0.2409 0.0104  0.0010  -0.0048 628  ALA B O   
13715 C CB  . ALA B 630  ? 0.2534 0.2742 0.2313 0.0112  0.0057  -0.0039 628  ALA B CB  
13716 N N   . ALA B 631  ? 0.2342 0.2564 0.2046 0.0096  0.0024  -0.0059 629  ALA B N   
13717 C CA  . ALA B 631  ? 0.2445 0.2682 0.2124 0.0090  0.0002  -0.0055 629  ALA B CA  
13718 C C   . ALA B 631  ? 0.2646 0.2890 0.2330 0.0080  -0.0014 -0.0071 629  ALA B C   
13719 O O   . ALA B 631  ? 0.2751 0.3014 0.2425 0.0074  -0.0035 -0.0067 629  ALA B O   
13720 C CB  . ALA B 631  ? 0.2570 0.2799 0.2192 0.0086  0.0006  -0.0054 629  ALA B CB  
13721 N N   . VAL B 632  ? 0.2392 0.2623 0.2091 0.0077  -0.0006 -0.0089 630  VAL B N   
13722 C CA  . VAL B 632  ? 0.2331 0.2568 0.2038 0.0066  -0.0022 -0.0102 630  VAL B CA  
13723 C C   . VAL B 632  ? 0.2406 0.2667 0.2159 0.0071  -0.0032 -0.0091 630  VAL B C   
13724 O O   . VAL B 632  ? 0.2403 0.2660 0.2190 0.0082  -0.0021 -0.0086 630  VAL B O   
13725 C CB  . VAL B 632  ? 0.2386 0.2598 0.2095 0.0063  -0.0011 -0.0123 630  VAL B CB  
13726 C CG1 . VAL B 632  ? 0.2409 0.2627 0.2129 0.0051  -0.0027 -0.0134 630  VAL B CG1 
13727 C CG2 . VAL B 632  ? 0.2473 0.2661 0.2135 0.0061  0.0001  -0.0136 630  VAL B CG2 
13728 N N   . PRO B 633  ? 0.2245 0.2531 0.2001 0.0065  -0.0053 -0.0086 631  PRO B N   
13729 C CA  . PRO B 633  ? 0.2285 0.2598 0.2084 0.0073  -0.0061 -0.0074 631  PRO B CA  
13730 C C   . PRO B 633  ? 0.2255 0.2562 0.2090 0.0075  -0.0053 -0.0084 631  PRO B C   
13731 O O   . PRO B 633  ? 0.2130 0.2421 0.1958 0.0064  -0.0051 -0.0101 631  PRO B O   
13732 C CB  . PRO B 633  ? 0.2187 0.2530 0.1980 0.0062  -0.0084 -0.0072 631  PRO B CB  
13733 C CG  . PRO B 633  ? 0.2829 0.3163 0.2570 0.0052  -0.0090 -0.0074 631  PRO B CG  
13734 C CD  . PRO B 633  ? 0.2241 0.2535 0.1959 0.0050  -0.0070 -0.0091 631  PRO B CD  
13735 N N   . PRO B 634  ? 0.2198 0.2512 0.2069 0.0088  -0.0050 -0.0073 632  PRO B N   
13736 C CA  . PRO B 634  ? 0.2282 0.2591 0.2186 0.0090  -0.0042 -0.0082 632  PRO B CA  
13737 C C   . PRO B 634  ? 0.2096 0.2416 0.2005 0.0076  -0.0052 -0.0094 632  PRO B C   
13738 O O   . PRO B 634  ? 0.2090 0.2393 0.2005 0.0071  -0.0045 -0.0107 632  PRO B O   
13739 C CB  . PRO B 634  ? 0.2394 0.2714 0.2330 0.0106  -0.0042 -0.0068 632  PRO B CB  
13740 C CG  . PRO B 634  ? 0.2734 0.3052 0.2653 0.0115  -0.0042 -0.0052 632  PRO B CG  
13741 C CD  . PRO B 634  ? 0.2268 0.2590 0.2148 0.0103  -0.0050 -0.0053 632  PRO B CD  
13742 N N   . SER B 635  ? 0.2239 0.2590 0.2147 0.0069  -0.0069 -0.0089 633  SER B N   
13743 C CA  . SER B 635  ? 0.2390 0.2754 0.2305 0.0053  -0.0079 -0.0099 633  SER B CA  
13744 C C   . SER B 635  ? 0.2093 0.2428 0.1973 0.0036  -0.0078 -0.0116 633  SER B C   
13745 O O   . SER B 635  ? 0.2104 0.2431 0.1990 0.0025  -0.0078 -0.0128 633  SER B O   
13746 C CB  . SER B 635  ? 0.2829 0.3235 0.2749 0.0047  -0.0099 -0.0089 633  SER B CB  
13747 O OG  . SER B 635  ? 0.3997 0.4403 0.3881 0.0040  -0.0108 -0.0086 633  SER B OG  
13748 N N   . GLU B 636  ? 0.2235 0.2551 0.2078 0.0035  -0.0076 -0.0118 634  GLU B N   
13749 C CA  . GLU B 636  ? 0.2142 0.2426 0.1949 0.0022  -0.0073 -0.0136 634  GLU B CA  
13750 C C   . GLU B 636  ? 0.2051 0.2302 0.1864 0.0031  -0.0053 -0.0146 634  GLU B C   
13751 O O   . GLU B 636  ? 0.2074 0.2301 0.1876 0.0022  -0.0051 -0.0161 634  GLU B O   
13752 C CB  . GLU B 636  ? 0.2367 0.2642 0.2128 0.0018  -0.0077 -0.0136 634  GLU B CB  
13753 C CG  . GLU B 636  ? 0.3484 0.3721 0.3204 0.0008  -0.0073 -0.0156 634  GLU B CG  
13754 C CD  . GLU B 636  ? 0.4650 0.4881 0.4370 -0.0011 -0.0084 -0.0169 634  GLU B CD  
13755 O OE1 . GLU B 636  ? 0.4027 0.4287 0.3756 -0.0025 -0.0103 -0.0164 634  GLU B OE1 
13756 O OE2 . GLU B 636  ? 0.4086 0.4282 0.3798 -0.0013 -0.0074 -0.0184 634  GLU B OE2 
13757 N N   . ARG B 637  ? 0.1797 0.2046 0.1628 0.0048  -0.0039 -0.0136 635  ARG B N   
13758 C CA  . ARG B 637  ? 0.1864 0.2089 0.1708 0.0056  -0.0022 -0.0144 635  ARG B CA  
13759 C C   . ARG B 637  ? 0.1901 0.2128 0.1775 0.0052  -0.0026 -0.0149 635  ARG B C   
13760 O O   . ARG B 637  ? 0.1999 0.2202 0.1870 0.0049  -0.0019 -0.0162 635  ARG B O   
13761 C CB  . ARG B 637  ? 0.1841 0.2067 0.1702 0.0071  -0.0010 -0.0131 635  ARG B CB  
13762 C CG  . ARG B 637  ? 0.1977 0.2201 0.1808 0.0075  -0.0006 -0.0123 635  ARG B CG  
13763 C CD  . ARG B 637  ? 0.2073 0.2292 0.1918 0.0088  0.0010  -0.0112 635  ARG B CD  
13764 N NE  . ARG B 637  ? 0.2093 0.2326 0.1974 0.0096  0.0006  -0.0098 635  ARG B NE  
13765 C CZ  . ARG B 637  ? 0.2119 0.2361 0.2002 0.0104  0.0004  -0.0081 635  ARG B CZ  
13766 N NH1 . ARG B 637  ? 0.2731 0.2975 0.2583 0.0103  0.0003  -0.0072 635  ARG B NH1 
13767 N NH2 . ARG B 637  ? 0.2103 0.2349 0.2019 0.0113  0.0003  -0.0071 635  ARG B NH2 
13768 N N   . ALA B 638  ? 0.1727 0.1983 0.1627 0.0052  -0.0035 -0.0140 636  ALA B N   
13769 C CA  . ALA B 638  ? 0.1685 0.1947 0.1611 0.0048  -0.0038 -0.0144 636  ALA B CA  
13770 C C   . ALA B 638  ? 0.1870 0.2124 0.1778 0.0028  -0.0047 -0.0156 636  ALA B C   
13771 O O   . ALA B 638  ? 0.1874 0.2113 0.1790 0.0023  -0.0045 -0.0164 636  ALA B O   
13772 C CB  . ALA B 638  ? 0.1739 0.2038 0.1694 0.0054  -0.0046 -0.0130 636  ALA B CB  
13773 N N   . ALA B 639  ? 0.1873 0.2133 0.1753 0.0016  -0.0059 -0.0157 637  ALA B N   
13774 C CA  . ALA B 639  ? 0.1859 0.2106 0.1717 -0.0005 -0.0069 -0.0169 637  ALA B CA  
13775 C C   . ALA B 639  ? 0.1850 0.2051 0.1686 -0.0005 -0.0059 -0.0185 637  ALA B C   
13776 O O   . ALA B 639  ? 0.1955 0.2136 0.1784 -0.0017 -0.0063 -0.0195 637  ALA B O   
13777 C CB  . ALA B 639  ? 0.1955 0.2216 0.1786 -0.0018 -0.0085 -0.0167 637  ALA B CB  
13778 N N   . CYS B 640  ? 0.1825 0.2008 0.1648 0.0010  -0.0045 -0.0186 638  CYS B N   
13779 C CA  . CYS B 640  ? 0.1929 0.2072 0.1736 0.0014  -0.0032 -0.0200 638  CYS B CA  
13780 C C   . CYS B 640  ? 0.1761 0.1896 0.1600 0.0020  -0.0026 -0.0201 638  CYS B C   
13781 O O   . CYS B 640  ? 0.1877 0.1984 0.1706 0.0014  -0.0025 -0.0213 638  CYS B O   
13782 C CB  . CYS B 640  ? 0.1834 0.1967 0.1629 0.0031  -0.0016 -0.0199 638  CYS B CB  
13783 S SG  . CYS B 640  ? 0.2218 0.2349 0.1964 0.0026  -0.0021 -0.0200 638  CYS B SG  
13784 N N   . LEU B 641  ? 0.1677 0.1835 0.1551 0.0030  -0.0021 -0.0189 639  LEU B N   
13785 C CA  . LEU B 641  ? 0.1670 0.1822 0.1573 0.0035  -0.0017 -0.0190 639  LEU B CA  
13786 C C   . LEU B 641  ? 0.1755 0.1908 0.1660 0.0018  -0.0028 -0.0194 639  LEU B C   
13787 O O   . LEU B 641  ? 0.1674 0.1804 0.1580 0.0016  -0.0026 -0.0201 639  LEU B O   
13788 C CB  . LEU B 641  ? 0.1826 0.2003 0.1763 0.0047  -0.0013 -0.0177 639  LEU B CB  
13789 C CG  . LEU B 641  ? 0.1956 0.2125 0.1903 0.0063  0.0002  -0.0173 639  LEU B CG  
13790 C CD1 . LEU B 641  ? 0.2396 0.2560 0.2318 0.0067  0.0008  -0.0172 639  LEU B CD1 
13791 C CD2 . LEU B 641  ? 0.1788 0.1977 0.1766 0.0072  0.0002  -0.0162 639  LEU B CD2 
13792 N N   . ASP B 642  ? 0.1639 0.1821 0.1545 0.0007  -0.0041 -0.0188 640  ASP B N   
13793 C CA  . ASP B 642  ? 0.1882 0.2070 0.1791 -0.0011 -0.0052 -0.0190 640  ASP B CA  
13794 C C   . ASP B 642  ? 0.1734 0.1884 0.1609 -0.0027 -0.0057 -0.0203 640  ASP B C   
13795 O O   . ASP B 642  ? 0.1890 0.2023 0.1766 -0.0037 -0.0060 -0.0208 640  ASP B O   
13796 C CB  . ASP B 642  ? 0.1745 0.1976 0.1663 -0.0021 -0.0065 -0.0180 640  ASP B CB  
13797 C CG  . ASP B 642  ? 0.2073 0.2340 0.2029 -0.0009 -0.0062 -0.0167 640  ASP B CG  
13798 O OD1 . ASP B 642  ? 0.2130 0.2388 0.2104 0.0002  -0.0052 -0.0167 640  ASP B OD1 
13799 O OD2 . ASP B 642  ? 0.2169 0.2473 0.2135 -0.0009 -0.0069 -0.0157 640  ASP B OD2 
13800 N N   . ARG B 643  ? 0.1809 0.1941 0.1651 -0.0028 -0.0058 -0.0210 641  ARG B N   
13801 C CA  . ARG B 643  ? 0.2014 0.2104 0.1820 -0.0040 -0.0062 -0.0225 641  ARG B CA  
13802 C C   . ARG B 643  ? 0.1858 0.1910 0.1665 -0.0027 -0.0049 -0.0234 641  ARG B C   
13803 O O   . ARG B 643  ? 0.1961 0.1981 0.1754 -0.0037 -0.0053 -0.0242 641  ARG B O   
13804 C CB  . ARG B 643  ? 0.1966 0.2043 0.1731 -0.0041 -0.0064 -0.0232 641  ARG B CB  
13805 C CG  . ARG B 643  ? 0.2211 0.2312 0.1963 -0.0062 -0.0083 -0.0229 641  ARG B CG  
13806 C CD  . ARG B 643  ? 0.2589 0.2668 0.2293 -0.0066 -0.0087 -0.0239 641  ARG B CD  
13807 N NE  . ARG B 643  ? 0.2451 0.2541 0.2154 -0.0046 -0.0074 -0.0233 641  ARG B NE  
13808 C CZ  . ARG B 643  ? 0.2477 0.2605 0.2187 -0.0043 -0.0079 -0.0220 641  ARG B CZ  
13809 N NH1 . ARG B 643  ? 0.2564 0.2727 0.2285 -0.0059 -0.0097 -0.0211 641  ARG B NH1 
13810 N NH2 . ARG B 643  ? 0.2808 0.2939 0.2514 -0.0025 -0.0066 -0.0215 641  ARG B NH2 
13811 N N   . ALA B 644  ? 0.1662 0.1718 0.1486 -0.0005 -0.0034 -0.0230 642  ALA B N   
13812 C CA  . ALA B 644  ? 0.1817 0.1845 0.1649 0.0008  -0.0022 -0.0236 642  ALA B CA  
13813 C C   . ALA B 644  ? 0.1878 0.1906 0.1734 0.0002  -0.0027 -0.0233 642  ALA B C   
13814 O O   . ALA B 644  ? 0.1921 0.1916 0.1770 0.0002  -0.0026 -0.0240 642  ALA B O   
13815 C CB  . ALA B 644  ? 0.1809 0.1849 0.1659 0.0029  -0.0007 -0.0231 642  ALA B CB  
13816 N N   . ALA B 645  ? 0.1781 0.1846 0.1663 -0.0002 -0.0032 -0.0221 643  ALA B N   
13817 C CA  . ALA B 645  ? 0.1806 0.1875 0.1709 -0.0008 -0.0035 -0.0217 643  ALA B CA  
13818 C C   . ALA B 645  ? 0.1713 0.1760 0.1594 -0.0030 -0.0047 -0.0222 643  ALA B C   
13819 O O   . ALA B 645  ? 0.1961 0.1985 0.1845 -0.0033 -0.0047 -0.0224 643  ALA B O   
13820 C CB  . ALA B 645  ? 0.1945 0.2058 0.1878 -0.0007 -0.0037 -0.0204 643  ALA B CB  
13821 N N   . GLU B 646  ? 0.1934 0.1987 0.1794 -0.0047 -0.0058 -0.0224 644  GLU B N   
13822 C CA  . GLU B 646  ? 0.2066 0.2097 0.1904 -0.0071 -0.0070 -0.0230 644  GLU B CA  
13823 C C   . GLU B 646  ? 0.1949 0.1922 0.1758 -0.0067 -0.0067 -0.0243 644  GLU B C   
13824 O O   . GLU B 646  ? 0.2074 0.2017 0.1874 -0.0079 -0.0073 -0.0246 644  GLU B O   
13825 C CB  . GLU B 646  ? 0.2347 0.2392 0.2164 -0.0089 -0.0083 -0.0230 644  GLU B CB  
13826 C CG  . GLU B 646  ? 0.2695 0.2799 0.2540 -0.0095 -0.0089 -0.0216 644  GLU B CG  
13827 C CD  . GLU B 646  ? 0.3854 0.3978 0.3723 -0.0108 -0.0093 -0.0208 644  GLU B CD  
13828 O OE1 . GLU B 646  ? 0.4984 0.5085 0.4837 -0.0130 -0.0102 -0.0211 644  GLU B OE1 
13829 O OE2 . GLU B 646  ? 0.4164 0.4327 0.4067 -0.0097 -0.0087 -0.0197 644  GLU B OE2 
13830 N N   . LEU B 647  ? 0.2061 0.2015 0.1854 -0.0049 -0.0057 -0.0252 645  LEU B N   
13831 C CA  . LEU B 647  ? 0.2286 0.2186 0.2053 -0.0041 -0.0052 -0.0265 645  LEU B CA  
13832 C C   . LEU B 647  ? 0.2145 0.2032 0.1935 -0.0028 -0.0045 -0.0263 645  LEU B C   
13833 O O   . LEU B 647  ? 0.2228 0.2073 0.2003 -0.0031 -0.0048 -0.0269 645  LEU B O   
13834 C CB  . LEU B 647  ? 0.2125 0.2015 0.1872 -0.0024 -0.0041 -0.0274 645  LEU B CB  
13835 C CG  . LEU B 647  ? 0.2155 0.2048 0.1869 -0.0036 -0.0049 -0.0279 645  LEU B CG  
13836 C CD1 . LEU B 647  ? 0.2426 0.2308 0.2121 -0.0016 -0.0035 -0.0287 645  LEU B CD1 
13837 C CD2 . LEU B 647  ? 0.2692 0.2545 0.2368 -0.0060 -0.0064 -0.0290 645  LEU B CD2 
13838 N N   . MET B 648  ? 0.1917 0.1838 0.1744 -0.0012 -0.0036 -0.0253 646  MET B N   
13839 C CA  . MET B 648  ? 0.1995 0.1906 0.1844 0.0000  -0.0031 -0.0250 646  MET B CA  
13840 C C   . MET B 648  ? 0.2029 0.1936 0.1881 -0.0018 -0.0042 -0.0244 646  MET B C   
13841 O O   . MET B 648  ? 0.2158 0.2034 0.2008 -0.0016 -0.0042 -0.0246 646  MET B O   
13842 C CB  . MET B 648  ? 0.2148 0.2096 0.2033 0.0016  -0.0021 -0.0240 646  MET B CB  
13843 C CG  . MET B 648  ? 0.2160 0.2109 0.2046 0.0036  -0.0008 -0.0244 646  MET B CG  
13844 S SD  . MET B 648  ? 0.2280 0.2261 0.2209 0.0052  0.0001  -0.0233 646  MET B SD  
13845 C CE  . MET B 648  ? 0.2490 0.2472 0.2414 0.0070  0.0016  -0.0237 646  MET B CE  
13846 N N   . GLN B 649  ? 0.1816 0.1754 0.1673 -0.0037 -0.0050 -0.0237 647  GLN B N   
13847 C CA  . GLN B 649  ? 0.2012 0.1950 0.1872 -0.0056 -0.0059 -0.0230 647  GLN B CA  
13848 C C   . GLN B 649  ? 0.2034 0.1922 0.1860 -0.0072 -0.0068 -0.0238 647  GLN B C   
13849 O O   . GLN B 649  ? 0.2340 0.2202 0.2164 -0.0077 -0.0071 -0.0236 647  GLN B O   
13850 C CB  . GLN B 649  ? 0.1984 0.1970 0.1858 -0.0072 -0.0065 -0.0221 647  GLN B CB  
13851 C CG  . GLN B 649  ? 0.2148 0.2145 0.2030 -0.0092 -0.0072 -0.0212 647  GLN B CG  
13852 C CD  . GLN B 649  ? 0.2139 0.2151 0.2048 -0.0078 -0.0065 -0.0204 647  GLN B CD  
13853 O OE1 . GLN B 649  ? 0.2089 0.2142 0.2023 -0.0069 -0.0059 -0.0198 647  GLN B OE1 
13854 N NE2 . GLN B 649  ? 0.2211 0.2186 0.2112 -0.0076 -0.0064 -0.0206 647  GLN B NE2 
13855 N N   . ALA B 650  ? 0.2094 0.1964 0.1891 -0.0081 -0.0073 -0.0248 648  ALA B N   
13856 C CA  . ALA B 650  ? 0.2277 0.2094 0.2036 -0.0097 -0.0083 -0.0257 648  ALA B CA  
13857 C C   . ALA B 650  ? 0.2507 0.2271 0.2253 -0.0078 -0.0076 -0.0266 648  ALA B C   
13858 O O   . ALA B 650  ? 0.2728 0.2446 0.2453 -0.0088 -0.0084 -0.0269 648  ALA B O   
13859 C CB  . ALA B 650  ? 0.2572 0.2382 0.2300 -0.0111 -0.0091 -0.0266 648  ALA B CB  
13860 N N   . ARG B 651  ? 0.2184 0.1955 0.1943 -0.0049 -0.0063 -0.0270 649  ARG B N   
13861 C CA  . ARG B 651  ? 0.2125 0.1852 0.1874 -0.0027 -0.0055 -0.0278 649  ARG B CA  
13862 C C   . ARG B 651  ? 0.2140 0.1878 0.1923 -0.0012 -0.0050 -0.0269 649  ARG B C   
13863 O O   . ARG B 651  ? 0.2311 0.2024 0.2096 0.0009  -0.0043 -0.0273 649  ARG B O   
13864 C CB  . ARG B 651  ? 0.2354 0.2083 0.2096 -0.0006 -0.0042 -0.0288 649  ARG B CB  
13865 C CG  . ARG B 651  ? 0.2496 0.2204 0.2196 -0.0021 -0.0049 -0.0300 649  ARG B CG  
13866 C CD  . ARG B 651  ? 0.2480 0.2198 0.2171 -0.0003 -0.0036 -0.0308 649  ARG B CD  
13867 N NE  . ARG B 651  ? 0.2723 0.2429 0.2374 -0.0022 -0.0045 -0.0317 649  ARG B NE  
13868 C CZ  . ARG B 651  ? 0.2597 0.2311 0.2229 -0.0014 -0.0038 -0.0324 649  ARG B CZ  
13869 N NH1 . ARG B 651  ? 0.2637 0.2368 0.2285 0.0012  -0.0020 -0.0323 649  ARG B NH1 
13870 N NH2 . ARG B 651  ? 0.2698 0.2404 0.2295 -0.0034 -0.0050 -0.0330 649  ARG B NH2 
13871 N N   . MET B 652  ? 0.2046 0.1821 0.1855 -0.0023 -0.0054 -0.0255 650  MET B N   
13872 C CA  . MET B 652  ? 0.2086 0.1872 0.1924 -0.0010 -0.0050 -0.0246 650  MET B CA  
13873 C C   . MET B 652  ? 0.2117 0.1853 0.1942 -0.0003 -0.0053 -0.0249 650  MET B C   
13874 O O   . MET B 652  ? 0.2321 0.2057 0.2166 0.0019  -0.0047 -0.0248 650  MET B O   
13875 C CB  . MET B 652  ? 0.2089 0.1914 0.1947 -0.0027 -0.0055 -0.0233 650  MET B CB  
13876 C CG  . MET B 652  ? 0.2008 0.1842 0.1890 -0.0016 -0.0053 -0.0225 650  MET B CG  
13877 S SD  . MET B 652  ? 0.2436 0.2314 0.2337 -0.0033 -0.0057 -0.0211 650  MET B SD  
13878 C CE  . MET B 652  ? 0.2327 0.2257 0.2252 -0.0022 -0.0048 -0.0210 650  MET B CE  
13879 N N   . PRO B 653  ? 0.2159 0.1852 0.1955 -0.0020 -0.0064 -0.0252 651  PRO B N   
13880 C CA  . PRO B 653  ? 0.2544 0.2186 0.2327 -0.0011 -0.0067 -0.0253 651  PRO B CA  
13881 C C   . PRO B 653  ? 0.2442 0.2060 0.2223 0.0019  -0.0057 -0.0264 651  PRO B C   
13882 O O   . PRO B 653  ? 0.2465 0.2074 0.2262 0.0039  -0.0055 -0.0261 651  PRO B O   
13883 C CB  . PRO B 653  ? 0.2587 0.2185 0.2333 -0.0037 -0.0080 -0.0255 651  PRO B CB  
13884 C CG  . PRO B 653  ? 0.2356 0.1998 0.2110 -0.0065 -0.0085 -0.0247 651  PRO B CG  
13885 C CD  . PRO B 653  ? 0.2430 0.2119 0.2203 -0.0052 -0.0075 -0.0251 651  PRO B CD  
13886 N N   . THR B 654  ? 0.2335 0.1947 0.2098 0.0024  -0.0051 -0.0277 652  THR B N   
13887 C CA  . THR B 654  ? 0.2462 0.2056 0.2222 0.0054  -0.0039 -0.0288 652  THR B CA  
13888 C C   . THR B 654  ? 0.2635 0.2279 0.2439 0.0075  -0.0027 -0.0281 652  THR B C   
13889 O O   . THR B 654  ? 0.2433 0.2071 0.2253 0.0099  -0.0020 -0.0281 652  THR B O   
13890 C CB  . THR B 654  ? 0.2575 0.2153 0.2302 0.0051  -0.0035 -0.0303 652  THR B CB  
13891 O OG1 . THR B 654  ? 0.2825 0.2352 0.2510 0.0030  -0.0048 -0.0310 652  THR B OG1 
13892 C CG2 . THR B 654  ? 0.2765 0.2327 0.2488 0.0083  -0.0020 -0.0314 652  THR B CG2 
13893 N N   . LEU B 655  ? 0.2261 0.1956 0.2085 0.0065  -0.0024 -0.0274 653  LEU B N   
13894 C CA  . LEU B 655  ? 0.2111 0.1851 0.1974 0.0082  -0.0014 -0.0267 653  LEU B CA  
13895 C C   . LEU B 655  ? 0.2269 0.2013 0.2159 0.0089  -0.0018 -0.0257 653  LEU B C   
13896 O O   . LEU B 655  ? 0.2288 0.2048 0.2205 0.0110  -0.0010 -0.0254 653  LEU B O   
13897 C CB  . LEU B 655  ? 0.2147 0.1935 0.2023 0.0069  -0.0013 -0.0260 653  LEU B CB  
13898 C CG  . LEU B 655  ? 0.2305 0.2096 0.2156 0.0062  -0.0010 -0.0268 653  LEU B CG  
13899 C CD1 . LEU B 655  ? 0.2438 0.2277 0.2307 0.0050  -0.0012 -0.0259 653  LEU B CD1 
13900 C CD2 . LEU B 655  ? 0.2967 0.2753 0.2815 0.0084  0.0004  -0.0277 653  LEU B CD2 
13901 N N   . LEU B 656  ? 0.2374 0.2107 0.2258 0.0071  -0.0031 -0.0250 654  LEU B N   
13902 C CA  . LEU B 656  ? 0.2505 0.2238 0.2408 0.0077  -0.0036 -0.0240 654  LEU B CA  
13903 C C   . LEU B 656  ? 0.2367 0.2067 0.2270 0.0099  -0.0035 -0.0244 654  LEU B C   
13904 O O   . LEU B 656  ? 0.2549 0.2264 0.2480 0.0115  -0.0033 -0.0238 654  LEU B O   
13905 C CB  . LEU B 656  ? 0.2924 0.2638 0.2809 0.0053  -0.0049 -0.0233 654  LEU B CB  
13906 C CG  . LEU B 656  ? 0.3520 0.3267 0.3406 0.0030  -0.0053 -0.0227 654  LEU B CG  
13907 C CD1 . LEU B 656  ? 0.2846 0.2577 0.2720 0.0010  -0.0064 -0.0218 654  LEU B CD1 
13908 C CD2 . LEU B 656  ? 0.3055 0.2853 0.2975 0.0038  -0.0046 -0.0222 654  LEU B CD2 
13909 N N   . GLY B 657  ? 0.2517 0.2169 0.2388 0.0100  -0.0036 -0.0254 655  GLY B N   
13910 C CA  . GLY B 657  ? 0.3019 0.2635 0.2887 0.0124  -0.0035 -0.0258 655  GLY B CA  
13911 C C   . GLY B 657  ? 0.2704 0.2349 0.2601 0.0151  -0.0020 -0.0261 655  GLY B C   
13912 O O   . GLY B 657  ? 0.2666 0.2312 0.2585 0.0172  -0.0019 -0.0257 655  GLY B O   
13913 N N   . LEU B 658  ? 0.2431 0.2103 0.2328 0.0151  -0.0008 -0.0268 656  LEU B N   
13914 C CA  . LEU B 658  ? 0.2096 0.1798 0.2021 0.0175  0.0007  -0.0269 656  LEU B CA  
13915 C C   . LEU B 658  ? 0.2288 0.2038 0.2258 0.0177  0.0006  -0.0256 656  LEU B C   
13916 O O   . LEU B 658  ? 0.2201 0.1965 0.2200 0.0198  0.0011  -0.0252 656  LEU B O   
13917 C CB  . LEU B 658  ? 0.2245 0.1963 0.2156 0.0171  0.0019  -0.0277 656  LEU B CB  
13918 C CG  . LEU B 658  ? 0.2143 0.1893 0.2078 0.0195  0.0037  -0.0279 656  LEU B CG  
13919 C CD1 . LEU B 658  ? 0.2324 0.2047 0.2260 0.0223  0.0044  -0.0286 656  LEU B CD1 
13920 C CD2 . LEU B 658  ? 0.2263 0.2022 0.2176 0.0189  0.0047  -0.0287 656  LEU B CD2 
13921 N N   . ILE B 659  ? 0.2010 0.1784 0.1986 0.0156  -0.0001 -0.0248 657  ILE B N   
13922 C CA  . ILE B 659  ? 0.1938 0.1753 0.1951 0.0157  -0.0003 -0.0236 657  ILE B CA  
13923 C C   . ILE B 659  ? 0.1993 0.1795 0.2020 0.0165  -0.0013 -0.0229 657  ILE B C   
13924 O O   . ILE B 659  ? 0.2011 0.1839 0.2072 0.0178  -0.0012 -0.0223 657  ILE B O   
13925 C CB  . ILE B 659  ? 0.1918 0.1755 0.1929 0.0134  -0.0008 -0.0231 657  ILE B CB  
13926 C CG1 . ILE B 659  ? 0.1952 0.1808 0.1956 0.0130  0.0002  -0.0236 657  ILE B CG1 
13927 C CG2 . ILE B 659  ? 0.2093 0.1961 0.2135 0.0134  -0.0013 -0.0220 657  ILE B CG2 
13928 C CD1 . ILE B 659  ? 0.2011 0.1882 0.2004 0.0108  -0.0004 -0.0232 657  ILE B CD1 
13929 N N   . ILE B 660  ? 0.2055 0.1817 0.2056 0.0157  -0.0024 -0.0229 658  ILE B N   
13930 C CA  . ILE B 660  ? 0.2038 0.1784 0.2047 0.0164  -0.0036 -0.0221 658  ILE B CA  
13931 C C   . ILE B 660  ? 0.2171 0.1915 0.2201 0.0192  -0.0030 -0.0223 658  ILE B C   
13932 O O   . ILE B 660  ? 0.2246 0.2008 0.2305 0.0203  -0.0035 -0.0214 658  ILE B O   
13933 C CB  . ILE B 660  ? 0.2028 0.1725 0.2000 0.0150  -0.0047 -0.0221 658  ILE B CB  
13934 C CG1 . ILE B 660  ? 0.2174 0.1884 0.2136 0.0122  -0.0055 -0.0214 658  ILE B CG1 
13935 C CG2 . ILE B 660  ? 0.2300 0.1968 0.2275 0.0163  -0.0058 -0.0214 658  ILE B CG2 
13936 C CD1 . ILE B 660  ? 0.2358 0.2024 0.2283 0.0104  -0.0065 -0.0214 658  ILE B CD1 
13937 N N   . ARG B 661  ? 0.2087 0.1808 0.2100 0.0206  -0.0020 -0.0235 659  ARG B N   
13938 C CA  . ARG B 661  ? 0.1985 0.1700 0.2015 0.0235  -0.0013 -0.0237 659  ARG B CA  
13939 C C   . ARG B 661  ? 0.2157 0.1923 0.2226 0.0250  0.0001  -0.0236 659  ARG B C   
13940 O O   . ARG B 661  ? 0.2276 0.2059 0.2377 0.0271  0.0003  -0.0232 659  ARG B O   
13941 C CB  . ARG B 661  ? 0.2308 0.1970 0.2300 0.0245  -0.0008 -0.0251 659  ARG B CB  
13942 C CG  . ARG B 661  ? 0.2502 0.2108 0.2463 0.0237  -0.0025 -0.0249 659  ARG B CG  
13943 C CD  . ARG B 661  ? 0.2824 0.2371 0.2742 0.0244  -0.0021 -0.0263 659  ARG B CD  
13944 N NE  . ARG B 661  ? 0.2797 0.2338 0.2726 0.0279  -0.0008 -0.0271 659  ARG B NE  
13945 C CZ  . ARG B 661  ? 0.2902 0.2437 0.2815 0.0290  0.0008  -0.0286 659  ARG B CZ  
13946 N NH1 . ARG B 661  ? 0.3135 0.2672 0.3021 0.0269  0.0012  -0.0294 659  ARG B NH1 
13947 N NH2 . ARG B 661  ? 0.2999 0.2528 0.2921 0.0324  0.0020  -0.0293 659  ARG B NH2 
13948 N N   . GLU B 662  ? 0.2073 0.1866 0.2141 0.0238  0.0011  -0.0239 660  GLU B N   
13949 C CA  . GLU B 662  ? 0.2195 0.2035 0.2297 0.0250  0.0026  -0.0237 660  GLU B CA  
13950 C C   . GLU B 662  ? 0.2207 0.2090 0.2348 0.0242  0.0019  -0.0224 660  GLU B C   
13951 O O   . GLU B 662  ? 0.2148 0.2066 0.2328 0.0256  0.0025  -0.0219 660  GLU B O   
13952 C CB  . GLU B 662  ? 0.2367 0.2217 0.2450 0.0241  0.0040  -0.0245 660  GLU B CB  
13953 C CG  . GLU B 662  ? 0.2343 0.2239 0.2458 0.0252  0.0056  -0.0242 660  GLU B CG  
13954 C CD  . GLU B 662  ? 0.2288 0.2193 0.2383 0.0245  0.0070  -0.0248 660  GLU B CD  
13955 O OE1 . GLU B 662  ? 0.2469 0.2364 0.2537 0.0225  0.0063  -0.0250 660  GLU B OE1 
13956 O OE2 . GLU B 662  ? 0.2373 0.2299 0.2480 0.0261  0.0087  -0.0250 660  GLU B OE2 
13957 N N   . ALA B 663  ? 0.2011 0.1894 0.2144 0.0220  0.0007  -0.0219 661  ALA B N   
13958 C CA  . ALA B 663  ? 0.2031 0.1952 0.2194 0.0211  0.0002  -0.0209 661  ALA B CA  
13959 C C   . ALA B 663  ? 0.2238 0.2151 0.2406 0.0206  -0.0017 -0.0201 661  ALA B C   
13960 O O   . ALA B 663  ? 0.2722 0.2661 0.2909 0.0196  -0.0023 -0.0194 661  ALA B O   
13961 C CB  . ALA B 663  ? 0.2193 0.2129 0.2344 0.0191  0.0005  -0.0210 661  ALA B CB  
13962 N N   . GLY B 664  ? 0.2365 0.2241 0.2515 0.0212  -0.0025 -0.0202 662  GLY B N   
13963 C CA  . GLY B 664  ? 0.2480 0.2349 0.2635 0.0208  -0.0043 -0.0192 662  GLY B CA  
13964 C C   . GLY B 664  ? 0.2430 0.2292 0.2563 0.0184  -0.0052 -0.0189 662  GLY B C   
13965 O O   . GLY B 664  ? 0.2544 0.2414 0.2685 0.0179  -0.0065 -0.0181 662  GLY B O   
13966 N N   . LYS B 665  ? 0.2081 0.1933 0.2187 0.0170  -0.0047 -0.0195 663  LYS B N   
13967 C CA  . LYS B 665  ? 0.2137 0.1990 0.2225 0.0148  -0.0054 -0.0192 663  LYS B CA  
13968 C C   . LYS B 665  ? 0.1960 0.1772 0.2016 0.0139  -0.0064 -0.0190 663  LYS B C   
13969 O O   . LYS B 665  ? 0.2136 0.1914 0.2173 0.0145  -0.0063 -0.0195 663  LYS B O   
13970 C CB  . LYS B 665  ? 0.2184 0.2050 0.2261 0.0136  -0.0043 -0.0198 663  LYS B CB  
13971 C CG  . LYS B 665  ? 0.2646 0.2548 0.2749 0.0143  -0.0032 -0.0199 663  LYS B CG  
13972 C CD  . LYS B 665  ? 0.2616 0.2547 0.2747 0.0142  -0.0037 -0.0192 663  LYS B CD  
13973 C CE  . LYS B 665  ? 0.2933 0.2896 0.3086 0.0145  -0.0027 -0.0192 663  LYS B CE  
13974 N NZ  . LYS B 665  ? 0.2793 0.2779 0.2972 0.0144  -0.0033 -0.0186 663  LYS B NZ  
13975 N N   . SER B 666  ? 0.2221 0.2036 0.2269 0.0124  -0.0073 -0.0182 664  SER B N   
13976 C CA  . SER B 666  ? 0.2227 0.2008 0.2242 0.0109  -0.0081 -0.0179 664  SER B CA  
13977 C C   . SER B 666  ? 0.2308 0.2086 0.2301 0.0092  -0.0075 -0.0185 664  SER B C   
13978 O O   . SER B 666  ? 0.2360 0.2167 0.2364 0.0090  -0.0065 -0.0190 664  SER B O   
13979 C CB  . SER B 666  ? 0.2540 0.2331 0.2552 0.0097  -0.0091 -0.0169 664  SER B CB  
13980 O OG  . SER B 666  ? 0.2726 0.2552 0.2743 0.0085  -0.0085 -0.0171 664  SER B OG  
13981 N N   . ALA B 667  ? 0.2263 0.2008 0.2226 0.0078  -0.0081 -0.0183 665  ALA B N   
13982 C CA  . ALA B 667  ? 0.2301 0.2042 0.2243 0.0059  -0.0077 -0.0187 665  ALA B CA  
13983 C C   . ALA B 667  ? 0.2319 0.2104 0.2271 0.0045  -0.0073 -0.0184 665  ALA B C   
13984 O O   . ALA B 667  ? 0.2164 0.1968 0.2117 0.0040  -0.0066 -0.0190 665  ALA B O   
13985 C CB  . ALA B 667  ? 0.2569 0.2267 0.2478 0.0042  -0.0087 -0.0183 665  ALA B CB  
13986 N N   . LEU B 668  ? 0.2276 0.2078 0.2234 0.0040  -0.0078 -0.0176 666  LEU B N   
13987 C CA  . LEU B 668  ? 0.2416 0.2258 0.2382 0.0030  -0.0073 -0.0174 666  LEU B CA  
13988 C C   . LEU B 668  ? 0.2175 0.2048 0.2166 0.0043  -0.0064 -0.0180 666  LEU B C   
13989 O O   . LEU B 668  ? 0.2080 0.1981 0.2075 0.0036  -0.0058 -0.0182 666  LEU B O   
13990 C CB  . LEU B 668  ? 0.2576 0.2428 0.2541 0.0024  -0.0078 -0.0165 666  LEU B CB  
13991 C CG  . LEU B 668  ? 0.3195 0.3029 0.3132 0.0004  -0.0084 -0.0157 666  LEU B CG  
13992 C CD1 . LEU B 668  ? 0.3763 0.3606 0.3697 0.0001  -0.0089 -0.0148 666  LEU B CD1 
13993 C CD2 . LEU B 668  ? 0.3497 0.3350 0.3427 -0.0015 -0.0078 -0.0158 666  LEU B CD2 
13994 N N   . ASN B 669  ? 0.2108 0.1981 0.2118 0.0061  -0.0064 -0.0181 667  ASN B N   
13995 C CA  . ASN B 669  ? 0.2117 0.2020 0.2151 0.0071  -0.0056 -0.0185 667  ASN B CA  
13996 C C   . ASN B 669  ? 0.2049 0.1949 0.2082 0.0076  -0.0047 -0.0193 667  ASN B C   
13997 O O   . ASN B 669  ? 0.2147 0.2074 0.2192 0.0078  -0.0039 -0.0195 667  ASN B O   
13998 C CB  . ASN B 669  ? 0.2699 0.2609 0.2757 0.0086  -0.0059 -0.0183 667  ASN B CB  
13999 C CG  . ASN B 669  ? 0.2715 0.2633 0.2773 0.0080  -0.0067 -0.0177 667  ASN B CG  
14000 O OD1 . ASN B 669  ? 0.3025 0.2959 0.3075 0.0069  -0.0065 -0.0176 667  ASN B OD1 
14001 N ND2 . ASN B 669  ? 0.3140 0.3048 0.3204 0.0087  -0.0076 -0.0172 667  ASN B ND2 
14002 N N   . ALA B 670  ? 0.1980 0.1847 0.1994 0.0077  -0.0048 -0.0197 668  ALA B N   
14003 C CA  . ALA B 670  ? 0.2075 0.1937 0.2080 0.0079  -0.0040 -0.0205 668  ALA B CA  
14004 C C   . ALA B 670  ? 0.1932 0.1806 0.1921 0.0060  -0.0040 -0.0206 668  ALA B C   
14005 O O   . ALA B 670  ? 0.1909 0.1800 0.1900 0.0060  -0.0033 -0.0210 668  ALA B O   
14006 C CB  . ALA B 670  ? 0.2157 0.1976 0.2143 0.0086  -0.0042 -0.0211 668  ALA B CB  
14007 N N   . ILE B 671  ? 0.1890 0.1757 0.1864 0.0042  -0.0048 -0.0201 669  ILE B N   
14008 C CA  . ILE B 671  ? 0.1891 0.1778 0.1857 0.0024  -0.0048 -0.0199 669  ILE B CA  
14009 C C   . ILE B 671  ? 0.1873 0.1804 0.1862 0.0028  -0.0041 -0.0197 669  ILE B C   
14010 O O   . ILE B 671  ? 0.1932 0.1883 0.1920 0.0025  -0.0037 -0.0199 669  ILE B O   
14011 C CB  . ILE B 671  ? 0.1891 0.1770 0.1842 0.0005  -0.0056 -0.0192 669  ILE B CB  
14012 C CG1 . ILE B 671  ? 0.2184 0.2015 0.2108 -0.0004 -0.0063 -0.0194 669  ILE B CG1 
14013 C CG2 . ILE B 671  ? 0.2134 0.2047 0.2085 -0.0012 -0.0054 -0.0188 669  ILE B CG2 
14014 C CD1 . ILE B 671  ? 0.2448 0.2263 0.2357 -0.0021 -0.0071 -0.0184 669  ILE B CD1 
14015 N N   . ALA B 672  ? 0.1818 0.1762 0.1824 0.0037  -0.0041 -0.0193 670  ALA B N   
14016 C CA  . ALA B 672  ? 0.1944 0.1924 0.1970 0.0042  -0.0036 -0.0191 670  ALA B CA  
14017 C C   . ALA B 672  ? 0.1942 0.1930 0.1979 0.0054  -0.0028 -0.0196 670  ALA B C   
14018 O O   . ALA B 672  ? 0.1896 0.1910 0.1940 0.0053  -0.0024 -0.0195 670  ALA B O   
14019 C CB  . ALA B 672  ? 0.2126 0.2111 0.2166 0.0049  -0.0039 -0.0187 670  ALA B CB  
14020 N N   . GLU B 673  ? 0.1857 0.1825 0.1896 0.0065  -0.0026 -0.0199 671  GLU B N   
14021 C CA  . GLU B 673  ? 0.1782 0.1760 0.1831 0.0076  -0.0017 -0.0203 671  GLU B CA  
14022 C C   . GLU B 673  ? 0.1883 0.1862 0.1913 0.0069  -0.0014 -0.0207 671  GLU B C   
14023 O O   . GLU B 673  ? 0.1892 0.1894 0.1930 0.0071  -0.0008 -0.0206 671  GLU B O   
14024 C CB  . GLU B 673  ? 0.1988 0.1942 0.2039 0.0090  -0.0015 -0.0207 671  GLU B CB  
14025 C CG  . GLU B 673  ? 0.2172 0.2138 0.2236 0.0103  -0.0004 -0.0210 671  GLU B CG  
14026 C CD  . GLU B 673  ? 0.2301 0.2292 0.2395 0.0111  -0.0002 -0.0204 671  GLU B CD  
14027 O OE1 . GLU B 673  ? 0.2352 0.2346 0.2460 0.0110  -0.0009 -0.0199 671  GLU B OE1 
14028 O OE2 . GLU B 673  ? 0.2072 0.2078 0.2176 0.0117  0.0008  -0.0204 671  GLU B OE2 
14029 N N   . VAL B 674  ? 0.1702 0.1657 0.1708 0.0058  -0.0019 -0.0211 672  VAL B N   
14030 C CA  . VAL B 674  ? 0.1713 0.1669 0.1699 0.0049  -0.0018 -0.0216 672  VAL B CA  
14031 C C   . VAL B 674  ? 0.1781 0.1770 0.1771 0.0036  -0.0021 -0.0210 672  VAL B C   
14032 O O   . VAL B 674  ? 0.1737 0.1745 0.1726 0.0036  -0.0018 -0.0210 672  VAL B O   
14033 C CB  . VAL B 674  ? 0.1696 0.1614 0.1653 0.0039  -0.0025 -0.0222 672  VAL B CB  
14034 C CG1 . VAL B 674  ? 0.1875 0.1794 0.1809 0.0027  -0.0026 -0.0227 672  VAL B CG1 
14035 C CG2 . VAL B 674  ? 0.1978 0.1864 0.1931 0.0055  -0.0021 -0.0228 672  VAL B CG2 
14036 N N   . ARG B 675  ? 0.1727 0.1725 0.1724 0.0028  -0.0026 -0.0204 673  ARG B N   
14037 C CA  . ARG B 675  ? 0.1649 0.1682 0.1653 0.0019  -0.0027 -0.0198 673  ARG B CA  
14038 C C   . ARG B 675  ? 0.1498 0.1557 0.1522 0.0033  -0.0021 -0.0195 673  ARG B C   
14039 O O   . ARG B 675  ? 0.1620 0.1704 0.1646 0.0030  -0.0020 -0.0193 673  ARG B O   
14040 C CB  . ARG B 675  ? 0.1672 0.1711 0.1680 0.0012  -0.0031 -0.0192 673  ARG B CB  
14041 C CG  . ARG B 675  ? 0.1869 0.1887 0.1856 -0.0007 -0.0039 -0.0191 673  ARG B CG  
14042 C CD  . ARG B 675  ? 0.1831 0.1865 0.1823 -0.0015 -0.0041 -0.0183 673  ARG B CD  
14043 N NE  . ARG B 675  ? 0.1833 0.1910 0.1837 -0.0019 -0.0038 -0.0179 673  ARG B NE  
14044 C CZ  . ARG B 675  ? 0.1755 0.1857 0.1769 -0.0020 -0.0035 -0.0173 673  ARG B CZ  
14045 N NH1 . ARG B 675  ? 0.2086 0.2173 0.2096 -0.0019 -0.0036 -0.0170 673  ARG B NH1 
14046 N NH2 . ARG B 675  ? 0.1805 0.1947 0.1830 -0.0022 -0.0032 -0.0169 673  ARG B NH2 
14047 N N   . GLU B 676  ? 0.1591 0.1646 0.1631 0.0047  -0.0017 -0.0195 674  GLU B N   
14048 C CA  . GLU B 676  ? 0.1486 0.1562 0.1544 0.0058  -0.0011 -0.0192 674  GLU B CA  
14049 C C   . GLU B 676  ? 0.1592 0.1672 0.1645 0.0062  -0.0006 -0.0194 674  GLU B C   
14050 O O   . GLU B 676  ? 0.1616 0.1717 0.1675 0.0065  -0.0003 -0.0190 674  GLU B O   
14051 C CB  . GLU B 676  ? 0.1764 0.1831 0.1839 0.0070  -0.0009 -0.0192 674  GLU B CB  
14052 C CG  . GLU B 676  ? 0.1712 0.1796 0.1805 0.0079  -0.0004 -0.0188 674  GLU B CG  
14053 C CD  . GLU B 676  ? 0.2325 0.2422 0.2425 0.0079  -0.0007 -0.0185 674  GLU B CD  
14054 O OE1 . GLU B 676  ? 0.2674 0.2774 0.2765 0.0070  -0.0011 -0.0184 674  GLU B OE1 
14055 O OE2 . GLU B 676  ? 0.2293 0.2396 0.2407 0.0087  -0.0005 -0.0182 674  GLU B OE2 
14056 N N   . ALA B 677  ? 0.1561 0.1619 0.1600 0.0064  -0.0004 -0.0200 675  ALA B N   
14057 C CA  . ALA B 677  ? 0.1577 0.1636 0.1605 0.0066  0.0002  -0.0203 675  ALA B CA  
14058 C C   . ALA B 677  ? 0.1522 0.1597 0.1536 0.0054  -0.0004 -0.0201 675  ALA B C   
14059 O O   . ALA B 677  ? 0.1678 0.1772 0.1693 0.0057  -0.0001 -0.0198 675  ALA B O   
14060 C CB  . ALA B 677  ? 0.1695 0.1725 0.1707 0.0070  0.0005  -0.0211 675  ALA B CB  
14061 N N   . ILE B 678  ? 0.1561 0.1629 0.1562 0.0039  -0.0012 -0.0203 676  ILE B N   
14062 C CA  . ILE B 678  ? 0.1588 0.1675 0.1579 0.0025  -0.0019 -0.0201 676  ILE B CA  
14063 C C   . ILE B 678  ? 0.1570 0.1694 0.1581 0.0029  -0.0018 -0.0192 676  ILE B C   
14064 O O   . ILE B 678  ? 0.1635 0.1781 0.1645 0.0028  -0.0020 -0.0188 676  ILE B O   
14065 C CB  . ILE B 678  ? 0.1584 0.1658 0.1562 0.0007  -0.0028 -0.0202 676  ILE B CB  
14066 C CG1 . ILE B 678  ? 0.1679 0.1712 0.1630 0.0003  -0.0030 -0.0212 676  ILE B CG1 
14067 C CG2 . ILE B 678  ? 0.1751 0.1856 0.1727 -0.0009 -0.0036 -0.0197 676  ILE B CG2 
14068 C CD1 . ILE B 678  ? 0.1849 0.1858 0.1789 -0.0011 -0.0037 -0.0213 676  ILE B CD1 
14069 N N   . ASP B 679  ? 0.1547 0.1678 0.1577 0.0035  -0.0016 -0.0188 677  ASP B N   
14070 C CA  . ASP B 679  ? 0.1540 0.1702 0.1589 0.0041  -0.0015 -0.0180 677  ASP B CA  
14071 C C   . ASP B 679  ? 0.1534 0.1703 0.1592 0.0055  -0.0009 -0.0177 677  ASP B C   
14072 O O   . ASP B 679  ? 0.1578 0.1772 0.1642 0.0059  -0.0010 -0.0171 677  ASP B O   
14073 C CB  . ASP B 679  ? 0.1569 0.1732 0.1631 0.0044  -0.0014 -0.0179 677  ASP B CB  
14074 C CG  . ASP B 679  ? 0.1863 0.2026 0.1917 0.0029  -0.0019 -0.0179 677  ASP B CG  
14075 O OD1 . ASP B 679  ? 0.1945 0.2125 0.1992 0.0016  -0.0024 -0.0176 677  ASP B OD1 
14076 O OD2 . ASP B 679  ? 0.1965 0.2113 0.2020 0.0029  -0.0019 -0.0179 677  ASP B OD2 
14077 N N   . PHE B 680  ? 0.1582 0.1730 0.1640 0.0064  -0.0003 -0.0180 678  PHE B N   
14078 C CA  . PHE B 680  ? 0.1522 0.1676 0.1586 0.0075  0.0002  -0.0176 678  PHE B CA  
14079 C C   . PHE B 680  ? 0.1614 0.1779 0.1662 0.0070  0.0001  -0.0175 678  PHE B C   
14080 O O   . PHE B 680  ? 0.1573 0.1756 0.1625 0.0076  0.0001  -0.0167 678  PHE B O   
14081 C CB  . PHE B 680  ? 0.1524 0.1658 0.1591 0.0082  0.0010  -0.0179 678  PHE B CB  
14082 C CG  . PHE B 680  ? 0.1457 0.1586 0.1545 0.0090  0.0012  -0.0177 678  PHE B CG  
14083 C CD1 . PHE B 680  ? 0.1535 0.1676 0.1638 0.0095  0.0011  -0.0171 678  PHE B CD1 
14084 C CD2 . PHE B 680  ? 0.1572 0.1683 0.1664 0.0091  0.0013  -0.0182 678  PHE B CD2 
14085 C CE1 . PHE B 680  ? 0.1622 0.1756 0.1741 0.0100  0.0012  -0.0171 678  PHE B CE1 
14086 C CE2 . PHE B 680  ? 0.1591 0.1699 0.1703 0.0096  0.0012  -0.0180 678  PHE B CE2 
14087 C CZ  . PHE B 680  ? 0.1692 0.1811 0.1816 0.0100  0.0012  -0.0175 678  PHE B CZ  
14088 N N   . LEU B 681  ? 0.1467 0.1617 0.1493 0.0061  -0.0002 -0.0182 679  LEU B N   
14089 C CA  . LEU B 681  ? 0.1414 0.1571 0.1419 0.0055  -0.0005 -0.0182 679  LEU B CA  
14090 C C   . LEU B 681  ? 0.1507 0.1695 0.1517 0.0050  -0.0013 -0.0174 679  LEU B C   
14091 O O   . LEU B 681  ? 0.1641 0.1847 0.1650 0.0054  -0.0015 -0.0168 679  LEU B O   
14092 C CB  . LEU B 681  ? 0.1609 0.1741 0.1588 0.0044  -0.0008 -0.0192 679  LEU B CB  
14093 C CG  . LEU B 681  ? 0.1532 0.1635 0.1502 0.0053  0.0002  -0.0200 679  LEU B CG  
14094 C CD1 . LEU B 681  ? 0.1794 0.1867 0.1741 0.0044  -0.0003 -0.0211 679  LEU B CD1 
14095 C CD2 . LEU B 681  ? 0.1663 0.1769 0.1620 0.0061  0.0009  -0.0199 679  LEU B CD2 
14096 N N   . ARG B 682  ? 0.1581 0.1779 0.1599 0.0040  -0.0020 -0.0174 680  ARG B N   
14097 C CA  . ARG B 682  ? 0.1488 0.1721 0.1514 0.0034  -0.0027 -0.0167 680  ARG B CA  
14098 C C   . ARG B 682  ? 0.1498 0.1754 0.1547 0.0050  -0.0024 -0.0158 680  ARG B C   
14099 O O   . ARG B 682  ? 0.1556 0.1841 0.1610 0.0052  -0.0028 -0.0150 680  ARG B O   
14100 C CB  . ARG B 682  ? 0.1584 0.1823 0.1611 0.0018  -0.0033 -0.0169 680  ARG B CB  
14101 C CG  . ARG B 682  ? 0.1713 0.1929 0.1713 0.0000  -0.0040 -0.0177 680  ARG B CG  
14102 C CD  . ARG B 682  ? 0.1820 0.2039 0.1823 -0.0016 -0.0045 -0.0177 680  ARG B CD  
14103 N NE  . ARG B 682  ? 0.1784 0.1980 0.1760 -0.0036 -0.0054 -0.0183 680  ARG B NE  
14104 C CZ  . ARG B 682  ? 0.1925 0.2105 0.1894 -0.0052 -0.0058 -0.0185 680  ARG B CZ  
14105 N NH1 . ARG B 682  ? 0.1990 0.2177 0.1975 -0.0051 -0.0055 -0.0181 680  ARG B NH1 
14106 N NH2 . ARG B 682  ? 0.2244 0.2398 0.2186 -0.0070 -0.0067 -0.0192 680  ARG B NH2 
14107 N N   . TYR B 683  ? 0.1480 0.1723 0.1542 0.0061  -0.0016 -0.0159 681  TYR B N   
14108 C CA  . TYR B 683  ? 0.1562 0.1820 0.1644 0.0076  -0.0013 -0.0152 681  TYR B CA  
14109 C C   . TYR B 683  ? 0.1506 0.1763 0.1585 0.0086  -0.0011 -0.0145 681  TYR B C   
14110 O O   . TYR B 683  ? 0.1574 0.1853 0.1660 0.0094  -0.0013 -0.0137 681  TYR B O   
14111 C CB  . TYR B 683  ? 0.1528 0.1767 0.1621 0.0083  -0.0007 -0.0155 681  TYR B CB  
14112 C CG  . TYR B 683  ? 0.1455 0.1700 0.1563 0.0099  -0.0004 -0.0150 681  TYR B CG  
14113 C CD1 . TYR B 683  ? 0.1657 0.1925 0.1776 0.0104  -0.0005 -0.0146 681  TYR B CD1 
14114 C CD2 . TYR B 683  ? 0.1531 0.1758 0.1643 0.0108  0.0001  -0.0148 681  TYR B CD2 
14115 C CE1 . TYR B 683  ? 0.1623 0.1892 0.1753 0.0120  -0.0002 -0.0143 681  TYR B CE1 
14116 C CE2 . TYR B 683  ? 0.1574 0.1800 0.1697 0.0121  0.0003  -0.0143 681  TYR B CE2 
14117 C CZ  . TYR B 683  ? 0.1495 0.1741 0.1627 0.0128  0.0001  -0.0141 681  TYR B CZ  
14118 O OH  . TYR B 683  ? 0.1934 0.2174 0.2073 0.0143  0.0003  -0.0138 681  TYR B OH  
14119 N N   . TYR B 684  ? 0.1446 0.1679 0.1514 0.0087  -0.0005 -0.0149 682  TYR B N   
14120 C CA  . TYR B 684  ? 0.1511 0.1744 0.1574 0.0095  -0.0002 -0.0141 682  TYR B CA  
14121 C C   . TYR B 684  ? 0.1631 0.1883 0.1678 0.0089  -0.0010 -0.0137 682  TYR B C   
14122 O O   . TYR B 684  ? 0.1627 0.1891 0.1674 0.0097  -0.0011 -0.0127 682  TYR B O   
14123 C CB  . TYR B 684  ? 0.1515 0.1723 0.1571 0.0096  0.0007  -0.0145 682  TYR B CB  
14124 C CG  . TYR B 684  ? 0.1450 0.1643 0.1525 0.0102  0.0012  -0.0147 682  TYR B CG  
14125 C CD1 . TYR B 684  ? 0.1609 0.1807 0.1701 0.0111  0.0012  -0.0141 682  TYR B CD1 
14126 C CD2 . TYR B 684  ? 0.1414 0.1588 0.1487 0.0100  0.0017  -0.0155 682  TYR B CD2 
14127 C CE1 . TYR B 684  ? 0.1625 0.1807 0.1732 0.0114  0.0015  -0.0144 682  TYR B CE1 
14128 C CE2 . TYR B 684  ? 0.1551 0.1713 0.1642 0.0104  0.0021  -0.0156 682  TYR B CE2 
14129 C CZ  . TYR B 684  ? 0.1533 0.1699 0.1640 0.0110  0.0019  -0.0150 682  TYR B CZ  
14130 O OH  . TYR B 684  ? 0.1578 0.1732 0.1701 0.0113  0.0020  -0.0152 682  TYR B OH  
14131 N N   . ALA B 685  ? 0.1519 0.1775 0.1552 0.0075  -0.0016 -0.0144 683  ALA B N   
14132 C CA  . ALA B 685  ? 0.1500 0.1776 0.1518 0.0067  -0.0027 -0.0140 683  ALA B CA  
14133 C C   . ALA B 685  ? 0.1705 0.2017 0.1744 0.0073  -0.0033 -0.0129 683  ALA B C   
14134 O O   . ALA B 685  ? 0.1677 0.2008 0.1714 0.0078  -0.0038 -0.0120 683  ALA B O   
14135 C CB  . ALA B 685  ? 0.1666 0.1937 0.1666 0.0048  -0.0034 -0.0150 683  ALA B CB  
14136 N N   . GLU B 686  ? 0.1554 0.1878 0.1612 0.0072  -0.0033 -0.0131 684  GLU B N   
14137 C CA  . GLU B 686  ? 0.1754 0.2115 0.1834 0.0081  -0.0037 -0.0121 684  GLU B CA  
14138 C C   . GLU B 686  ? 0.1961 0.2319 0.2052 0.0102  -0.0032 -0.0113 684  GLU B C   
14139 O O   . GLU B 686  ? 0.1750 0.2133 0.1848 0.0111  -0.0037 -0.0102 684  GLU B O   
14140 C CB  . GLU B 686  ? 0.1992 0.2365 0.2088 0.0076  -0.0036 -0.0125 684  GLU B CB  
14141 C CG  . GLU B 686  ? 0.2239 0.2652 0.2360 0.0089  -0.0037 -0.0116 684  GLU B CG  
14142 C CD  . GLU B 686  ? 0.2559 0.3013 0.2683 0.0083  -0.0049 -0.0107 684  GLU B CD  
14143 O OE1 . GLU B 686  ? 0.2446 0.2901 0.2552 0.0066  -0.0058 -0.0108 684  GLU B OE1 
14144 O OE2 . GLU B 686  ? 0.2849 0.3338 0.2995 0.0097  -0.0049 -0.0098 684  GLU B OE2 
14145 N N   . GLN B 687  ? 0.1561 0.1888 0.1654 0.0110  -0.0022 -0.0116 685  GLN B N   
14146 C CA  . GLN B 687  ? 0.1704 0.2023 0.1806 0.0128  -0.0018 -0.0108 685  GLN B CA  
14147 C C   . GLN B 687  ? 0.1768 0.2089 0.1856 0.0131  -0.0022 -0.0099 685  GLN B C   
14148 O O   . GLN B 687  ? 0.1810 0.2140 0.1904 0.0144  -0.0024 -0.0088 685  GLN B O   
14149 C CB  . GLN B 687  ? 0.1699 0.1985 0.1804 0.0132  -0.0009 -0.0114 685  GLN B CB  
14150 C CG  . GLN B 687  ? 0.1783 0.2066 0.1901 0.0132  -0.0007 -0.0121 685  GLN B CG  
14151 C CD  . GLN B 687  ? 0.1951 0.2256 0.2085 0.0146  -0.0008 -0.0117 685  GLN B CD  
14152 O OE1 . GLN B 687  ? 0.1994 0.2292 0.2133 0.0161  -0.0007 -0.0110 685  GLN B OE1 
14153 N NE2 . GLN B 687  ? 0.2408 0.2738 0.2548 0.0141  -0.0011 -0.0119 685  GLN B NE2 
14154 N N   . THR B 688  ? 0.1545 0.1855 0.1611 0.0118  -0.0022 -0.0103 686  THR B N   
14155 C CA  . THR B 688  ? 0.1740 0.2053 0.1788 0.0119  -0.0025 -0.0094 686  THR B CA  
14156 C C   . THR B 688  ? 0.1687 0.2036 0.1736 0.0120  -0.0038 -0.0085 686  THR B C   
14157 O O   . THR B 688  ? 0.1808 0.2165 0.1857 0.0131  -0.0042 -0.0072 686  THR B O   
14158 C CB  . THR B 688  ? 0.1577 0.1873 0.1597 0.0105  -0.0023 -0.0103 686  THR B CB  
14159 O OG1 . THR B 688  ? 0.1792 0.2059 0.1814 0.0108  -0.0010 -0.0108 686  THR B OG1 
14160 C CG2 . THR B 688  ? 0.1866 0.2168 0.1863 0.0105  -0.0027 -0.0094 686  THR B CG2 
14161 N N   . ARG B 689  ? 0.1629 0.2000 0.1681 0.0107  -0.0046 -0.0091 687  ARG B N   
14162 C CA  . ARG B 689  ? 0.1661 0.2073 0.1720 0.0107  -0.0059 -0.0082 687  ARG B CA  
14163 C C   . ARG B 689  ? 0.1748 0.2182 0.1834 0.0127  -0.0059 -0.0071 687  ARG B C   
14164 O O   . ARG B 689  ? 0.2025 0.2490 0.2117 0.0134  -0.0069 -0.0059 687  ARG B O   
14165 C CB  . ARG B 689  ? 0.1854 0.2287 0.1915 0.0087  -0.0066 -0.0090 687  ARG B CB  
14166 C CG  . ARG B 689  ? 0.2159 0.2572 0.2188 0.0067  -0.0070 -0.0100 687  ARG B CG  
14167 C CD  . ARG B 689  ? 0.2120 0.2554 0.2151 0.0046  -0.0080 -0.0105 687  ARG B CD  
14168 N NE  . ARG B 689  ? 0.2224 0.2651 0.2272 0.0044  -0.0073 -0.0112 687  ARG B NE  
14169 C CZ  . ARG B 689  ? 0.2361 0.2755 0.2395 0.0032  -0.0068 -0.0124 687  ARG B CZ  
14170 N NH1 . ARG B 689  ? 0.2265 0.2628 0.2268 0.0023  -0.0069 -0.0133 687  ARG B NH1 
14171 N NH2 . ARG B 689  ? 0.2268 0.2659 0.2317 0.0030  -0.0062 -0.0128 687  ARG B NH2 
14172 N N   . ARG B 690  ? 0.1757 0.2176 0.1860 0.0138  -0.0049 -0.0075 688  ARG B N   
14173 C CA  . ARG B 690  ? 0.1662 0.2094 0.1787 0.0160  -0.0048 -0.0066 688  ARG B CA  
14174 C C   . ARG B 690  ? 0.1820 0.2229 0.1939 0.0177  -0.0045 -0.0056 688  ARG B C   
14175 O O   . ARG B 690  ? 0.1888 0.2309 0.2022 0.0196  -0.0047 -0.0046 688  ARG B O   
14176 C CB  . ARG B 690  ? 0.1913 0.2332 0.2053 0.0165  -0.0038 -0.0076 688  ARG B CB  
14177 C CG  . ARG B 690  ? 0.1971 0.2414 0.2119 0.0151  -0.0039 -0.0084 688  ARG B CG  
14178 C CD  . ARG B 690  ? 0.2450 0.2945 0.2620 0.0158  -0.0045 -0.0076 688  ARG B CD  
14179 N NE  . ARG B 690  ? 0.2817 0.3315 0.3006 0.0184  -0.0039 -0.0072 688  ARG B NE  
14180 C CZ  . ARG B 690  ? 0.2797 0.3310 0.2994 0.0204  -0.0043 -0.0060 688  ARG B CZ  
14181 N NH1 . ARG B 690  ? 0.2749 0.3284 0.2942 0.0201  -0.0054 -0.0049 688  ARG B NH1 
14182 N NH2 . ARG B 690  ? 0.2533 0.3039 0.2743 0.0228  -0.0036 -0.0058 688  ARG B NH2 
14183 N N   . THR B 691  ? 0.1810 0.2186 0.1909 0.0170  -0.0041 -0.0057 689  THR B N   
14184 C CA  . THR B 691  ? 0.1888 0.2237 0.1984 0.0185  -0.0036 -0.0047 689  THR B CA  
14185 C C   . THR B 691  ? 0.1930 0.2270 0.2002 0.0181  -0.0039 -0.0037 689  THR B C   
14186 O O   . THR B 691  ? 0.2375 0.2710 0.2445 0.0195  -0.0042 -0.0022 689  THR B O   
14187 C CB  . THR B 691  ? 0.1803 0.2115 0.1903 0.0185  -0.0024 -0.0055 689  THR B CB  
14188 O OG1 . THR B 691  ? 0.2029 0.2328 0.2116 0.0167  -0.0019 -0.0066 689  THR B OG1 
14189 C CG2 . THR B 691  ? 0.2216 0.2532 0.2337 0.0193  -0.0022 -0.0063 689  THR B CG2 
14190 N N   . LEU B 692  ? 0.1776 0.2108 0.1827 0.0164  -0.0036 -0.0044 690  LEU B N   
14191 C CA  . LEU B 692  ? 0.1902 0.2215 0.1928 0.0162  -0.0033 -0.0036 690  LEU B CA  
14192 C C   . LEU B 692  ? 0.2009 0.2344 0.2018 0.0163  -0.0045 -0.0023 690  LEU B C   
14193 O O   . LEU B 692  ? 0.2275 0.2637 0.2278 0.0153  -0.0056 -0.0027 690  LEU B O   
14194 C CB  . LEU B 692  ? 0.1993 0.2288 0.2002 0.0146  -0.0024 -0.0049 690  LEU B CB  
14195 C CG  . LEU B 692  ? 0.2232 0.2503 0.2257 0.0146  -0.0012 -0.0059 690  LEU B CG  
14196 C CD1 . LEU B 692  ? 0.2572 0.2826 0.2579 0.0134  -0.0002 -0.0068 690  LEU B CD1 
14197 C CD2 . LEU B 692  ? 0.2417 0.2669 0.2456 0.0159  -0.0007 -0.0049 690  LEU B CD2 
14198 N N   . GLY B 693  ? 0.2031 0.2354 0.2031 0.0173  -0.0045 -0.0007 691  GLY B N   
14199 C CA  . GLY B 693  ? 0.2183 0.2524 0.2165 0.0176  -0.0057 0.0008  691  GLY B CA  
14200 C C   . GLY B 693  ? 0.2458 0.2772 0.2411 0.0173  -0.0050 0.0017  691  GLY B C   
14201 O O   . GLY B 693  ? 0.2491 0.2778 0.2441 0.0168  -0.0035 0.0012  691  GLY B O   
14202 N N   . PRO B 694  ? 0.2434 0.2759 0.2366 0.0177  -0.0060 0.0033  692  PRO B N   
14203 C CA  . PRO B 694  ? 0.2626 0.2930 0.2523 0.0171  -0.0053 0.0042  692  PRO B CA  
14204 C C   . PRO B 694  ? 0.2719 0.2991 0.2623 0.0178  -0.0039 0.0052  692  PRO B C   
14205 O O   . PRO B 694  ? 0.3360 0.3612 0.3243 0.0170  -0.0026 0.0053  692  PRO B O   
14206 C CB  . PRO B 694  ? 0.3171 0.3497 0.3047 0.0176  -0.0070 0.0059  692  PRO B CB  
14207 C CG  . PRO B 694  ? 0.3470 0.3827 0.3377 0.0187  -0.0085 0.0062  692  PRO B CG  
14208 C CD  . PRO B 694  ? 0.2605 0.2967 0.2542 0.0183  -0.0079 0.0042  692  PRO B CD  
14209 N N   . GLY B 695  ? 0.2749 0.3013 0.2681 0.0193  -0.0041 0.0059  693  GLY B N   
14210 C CA  . GLY B 695  ? 0.2725 0.2954 0.2663 0.0198  -0.0031 0.0069  693  GLY B CA  
14211 C C   . GLY B 695  ? 0.2713 0.2923 0.2669 0.0191  -0.0016 0.0053  693  GLY B C   
14212 O O   . GLY B 695  ? 0.3235 0.3416 0.3198 0.0192  -0.0008 0.0060  693  GLY B O   
14213 N N   . HIS B 696  ? 0.2673 0.2897 0.2637 0.0182  -0.0014 0.0033  694  HIS B N   
14214 C CA  . HIS B 696  ? 0.2376 0.2585 0.2357 0.0174  -0.0001 0.0018  694  HIS B CA  
14215 C C   . HIS B 696  ? 0.2325 0.2531 0.2285 0.0160  0.0010  0.0012  694  HIS B C   
14216 O O   . HIS B 696  ? 0.3100 0.3317 0.3055 0.0152  0.0011  -0.0004 694  HIS B O   
14217 C CB  . HIS B 696  ? 0.2382 0.2604 0.2385 0.0176  -0.0006 0.0001  694  HIS B CB  
14218 C CG  . HIS B 696  ? 0.2304 0.2536 0.2325 0.0191  -0.0016 0.0007  694  HIS B CG  
14219 N ND1 . HIS B 696  ? 0.2293 0.2557 0.2318 0.0195  -0.0028 0.0004  694  HIS B ND1 
14220 C CD2 . HIS B 696  ? 0.2332 0.2544 0.2367 0.0205  -0.0017 0.0015  694  HIS B CD2 
14221 C CE1 . HIS B 696  ? 0.2233 0.2501 0.2276 0.0212  -0.0034 0.0011  694  HIS B CE1 
14222 N NE2 . HIS B 696  ? 0.2489 0.2723 0.2536 0.0220  -0.0027 0.0017  694  HIS B NE2 
14223 N N   . GLY B 697  ? 0.2645 0.2835 0.2590 0.0158  0.0019  0.0025  695  GLY B N   
14224 C CA  . GLY B 697  ? 0.2463 0.2652 0.2386 0.0147  0.0032  0.0022  695  GLY B CA  
14225 C C   . GLY B 697  ? 0.2228 0.2411 0.2170 0.0140  0.0045  0.0007  695  GLY B C   
14226 O O   . GLY B 697  ? 0.2441 0.2611 0.2411 0.0142  0.0047  0.0006  695  GLY B O   
14227 N N   . PRO B 698  ? 0.2493 0.2681 0.2418 0.0133  0.0054  -0.0006 696  PRO B N   
14228 C CA  . PRO B 698  ? 0.2188 0.2370 0.2132 0.0128  0.0066  -0.0019 696  PRO B CA  
14229 C C   . PRO B 698  ? 0.2201 0.2374 0.2155 0.0126  0.0081  -0.0007 696  PRO B C   
14230 O O   . PRO B 698  ? 0.2370 0.2539 0.2309 0.0125  0.0085  0.0011  696  PRO B O   
14231 C CB  . PRO B 698  ? 0.2818 0.3008 0.2736 0.0123  0.0071  -0.0034 696  PRO B CB  
14232 C CG  . PRO B 698  ? 0.3643 0.3838 0.3523 0.0123  0.0068  -0.0022 696  PRO B CG  
14233 C CD  . PRO B 698  ? 0.3011 0.3210 0.2899 0.0129  0.0052  -0.0009 696  PRO B CD  
14234 N N   . LEU B 699  ? 0.2012 0.2181 0.1993 0.0123  0.0089  -0.0016 697  LEU B N   
14235 C CA  . LEU B 699  ? 0.2045 0.2209 0.2039 0.0118  0.0104  -0.0006 697  LEU B CA  
14236 C C   . LEU B 699  ? 0.2004 0.2179 0.1975 0.0115  0.0120  -0.0006 697  LEU B C   
14237 O O   . LEU B 699  ? 0.2305 0.2480 0.2271 0.0111  0.0132  0.0011  697  LEU B O   
14238 C CB  . LEU B 699  ? 0.2097 0.2259 0.2128 0.0116  0.0106  -0.0016 697  LEU B CB  
14239 C CG  . LEU B 699  ? 0.2205 0.2355 0.2258 0.0119  0.0091  -0.0018 697  LEU B CG  
14240 C CD1 . LEU B 699  ? 0.2314 0.2462 0.2397 0.0116  0.0093  -0.0030 697  LEU B CD1 
14241 C CD2 . LEU B 699  ? 0.2799 0.2933 0.2854 0.0119  0.0088  0.0001  697  LEU B CD2 
14242 N N   . GLY B 700  ? 0.1969 0.2150 0.1924 0.0117  0.0123  -0.0023 698  GLY B N   
14243 C CA  . GLY B 700  ? 0.2024 0.2213 0.1961 0.0116  0.0141  -0.0028 698  GLY B CA  
14244 C C   . GLY B 700  ? 0.1941 0.2133 0.1898 0.0118  0.0146  -0.0047 698  GLY B C   
14245 O O   . GLY B 700  ? 0.1996 0.2183 0.1971 0.0119  0.0134  -0.0059 698  GLY B O   
14246 N N   . PRO B 701  ? 0.1915 0.2114 0.1869 0.0120  0.0166  -0.0051 699  PRO B N   
14247 C CA  . PRO B 701  ? 0.1898 0.2098 0.1869 0.0125  0.0171  -0.0069 699  PRO B CA  
14248 C C   . PRO B 701  ? 0.1812 0.2012 0.1828 0.0123  0.0164  -0.0069 699  PRO B C   
14249 O O   . PRO B 701  ? 0.1977 0.2183 0.2020 0.0118  0.0168  -0.0054 699  PRO B O   
14250 C CB  . PRO B 701  ? 0.2026 0.2240 0.1992 0.0128  0.0195  -0.0067 699  PRO B CB  
14251 C CG  . PRO B 701  ? 0.2301 0.2515 0.2226 0.0125  0.0201  -0.0054 699  PRO B CG  
14252 C CD  . PRO B 701  ? 0.2075 0.2283 0.2009 0.0119  0.0184  -0.0038 699  PRO B CD  
14253 N N   . ILE B 702  ? 0.1687 0.1879 0.1711 0.0125  0.0152  -0.0085 700  ILE B N   
14254 C CA  A ILE B 702  ? 0.1746 0.1936 0.1809 0.0124  0.0144  -0.0086 700  ILE B CA  
14255 C CA  B ILE B 702  ? 0.1745 0.1935 0.1808 0.0124  0.0144  -0.0087 700  ILE B CA  
14256 C C   . ILE B 702  ? 0.1787 0.1980 0.1865 0.0130  0.0152  -0.0100 700  ILE B C   
14257 O O   . ILE B 702  ? 0.1766 0.1952 0.1821 0.0135  0.0153  -0.0115 700  ILE B O   
14258 C CB  A ILE B 702  ? 0.1559 0.1738 0.1622 0.0122  0.0124  -0.0091 700  ILE B CB  
14259 C CB  B ILE B 702  ? 0.1570 0.1749 0.1631 0.0123  0.0124  -0.0093 700  ILE B CB  
14260 C CG1 A ILE B 702  ? 0.1861 0.2037 0.1920 0.0119  0.0117  -0.0075 700  ILE B CG1 
14261 C CG1 B ILE B 702  ? 0.1623 0.1799 0.1670 0.0120  0.0116  -0.0079 700  ILE B CG1 
14262 C CG2 A ILE B 702  ? 0.1676 0.1852 0.1772 0.0122  0.0117  -0.0098 700  ILE B CG2 
14263 C CG2 B ILE B 702  ? 0.1725 0.1901 0.1822 0.0121  0.0116  -0.0095 700  ILE B CG2 
14264 C CD1 A ILE B 702  ? 0.1624 0.1794 0.1683 0.0120  0.0099  -0.0079 700  ILE B CD1 
14265 C CD1 B ILE B 702  ? 0.2042 0.2218 0.2108 0.0117  0.0120  -0.0061 700  ILE B CD1 
14266 N N   . VAL B 703  ? 0.1634 0.1837 0.1749 0.0129  0.0157  -0.0095 701  VAL B N   
14267 C CA  . VAL B 703  ? 0.1789 0.1997 0.1924 0.0135  0.0162  -0.0105 701  VAL B CA  
14268 C C   . VAL B 703  ? 0.1579 0.1776 0.1732 0.0133  0.0144  -0.0113 701  VAL B C   
14269 O O   . VAL B 703  ? 0.1623 0.1818 0.1795 0.0127  0.0134  -0.0105 701  VAL B O   
14270 C CB  . VAL B 703  ? 0.1700 0.1931 0.1869 0.0134  0.0176  -0.0093 701  VAL B CB  
14271 C CG1 . VAL B 703  ? 0.1797 0.2037 0.1996 0.0141  0.0178  -0.0102 701  VAL B CG1 
14272 C CG2 . VAL B 703  ? 0.1787 0.2031 0.1935 0.0137  0.0197  -0.0087 701  VAL B CG2 
14273 N N   . CYS B 704  ? 0.1568 0.1754 0.1710 0.0139  0.0140  -0.0129 702  CYS B N   
14274 C CA  . CYS B 704  ? 0.1548 0.1722 0.1701 0.0138  0.0123  -0.0136 702  CYS B CA  
14275 C C   . CYS B 704  ? 0.1596 0.1775 0.1774 0.0145  0.0127  -0.0142 702  CYS B C   
14276 O O   . CYS B 704  ? 0.1628 0.1802 0.1792 0.0154  0.0135  -0.0152 702  CYS B O   
14277 C CB  . CYS B 704  ? 0.1591 0.1748 0.1712 0.0137  0.0113  -0.0147 702  CYS B CB  
14278 S SG  . CYS B 704  ? 0.1708 0.1865 0.1804 0.0130  0.0107  -0.0140 702  CYS B SG  
14279 N N   . ILE B 705  ? 0.1558 0.1743 0.1769 0.0141  0.0120  -0.0137 703  ILE B N   
14280 C CA  . ILE B 705  ? 0.1548 0.1742 0.1789 0.0147  0.0121  -0.0140 703  ILE B CA  
14281 C C   . ILE B 705  ? 0.1527 0.1706 0.1773 0.0144  0.0103  -0.0146 703  ILE B C   
14282 O O   . ILE B 705  ? 0.1596 0.1770 0.1847 0.0136  0.0091  -0.0141 703  ILE B O   
14283 C CB  . ILE B 705  ? 0.1611 0.1829 0.1888 0.0144  0.0129  -0.0126 703  ILE B CB  
14284 C CG1 . ILE B 705  ? 0.1706 0.1942 0.1977 0.0148  0.0150  -0.0120 703  ILE B CG1 
14285 C CG2 . ILE B 705  ? 0.1623 0.1852 0.1934 0.0148  0.0124  -0.0128 703  ILE B CG2 
14286 C CD1 . ILE B 705  ? 0.1808 0.2069 0.2111 0.0140  0.0157  -0.0104 703  ILE B CD1 
14287 N N   . SER B 706  ? 0.1620 0.1788 0.1861 0.0152  0.0100  -0.0156 704  SER B N   
14288 C CA  . SER B 706  ? 0.1824 0.1974 0.2061 0.0149  0.0083  -0.0162 704  SER B CA  
14289 C C   . SER B 706  ? 0.1528 0.1681 0.1790 0.0156  0.0078  -0.0164 704  SER B C   
14290 O O   . SER B 706  ? 0.1682 0.1848 0.1961 0.0166  0.0089  -0.0164 704  SER B O   
14291 C CB  . SER B 706  ? 0.1589 0.1718 0.1788 0.0150  0.0081  -0.0173 704  SER B CB  
14292 O OG  . SER B 706  ? 0.1634 0.1758 0.1820 0.0160  0.0092  -0.0180 704  SER B OG  
14293 N N   . PRO B 707  ? 0.1549 0.1691 0.1815 0.0151  0.0063  -0.0166 705  PRO B N   
14294 C CA  . PRO B 707  ? 0.1627 0.1771 0.1916 0.0156  0.0055  -0.0166 705  PRO B CA  
14295 C C   . PRO B 707  ? 0.1677 0.1799 0.1946 0.0165  0.0052  -0.0175 705  PRO B C   
14296 O O   . PRO B 707  ? 0.1777 0.1880 0.2013 0.0163  0.0054  -0.0182 705  PRO B O   
14297 C CB  . PRO B 707  ? 0.1810 0.1948 0.2103 0.0145  0.0038  -0.0163 705  PRO B CB  
14298 C CG  . PRO B 707  ? 0.1778 0.1900 0.2038 0.0138  0.0036  -0.0168 705  PRO B CG  
14299 C CD  . PRO B 707  ? 0.1814 0.1944 0.2064 0.0140  0.0051  -0.0166 705  PRO B CD  
14300 N N   . TRP B 708  ? 0.1554 0.1678 0.1843 0.0174  0.0047  -0.0175 706  TRP B N   
14301 C CA  . TRP B 708  ? 0.1718 0.1818 0.1988 0.0183  0.0045  -0.0183 706  TRP B CA  
14302 C C   . TRP B 708  ? 0.1777 0.1851 0.2025 0.0173  0.0029  -0.0186 706  TRP B C   
14303 O O   . TRP B 708  ? 0.1887 0.1935 0.2109 0.0176  0.0027  -0.0193 706  TRP B O   
14304 C CB  . TRP B 708  ? 0.1595 0.1704 0.1893 0.0199  0.0045  -0.0181 706  TRP B CB  
14305 C CG  . TRP B 708  ? 0.1589 0.1703 0.1909 0.0194  0.0027  -0.0175 706  TRP B CG  
14306 C CD1 . TRP B 708  ? 0.2165 0.2308 0.2521 0.0189  0.0023  -0.0166 706  TRP B CD1 
14307 C CD2 . TRP B 708  ? 0.1838 0.1926 0.2143 0.0192  0.0011  -0.0177 706  TRP B CD2 
14308 N NE1 . TRP B 708  ? 0.1942 0.2077 0.2303 0.0184  0.0004  -0.0163 706  TRP B NE1 
14309 C CE2 . TRP B 708  ? 0.1756 0.1859 0.2087 0.0187  -0.0003 -0.0169 706  TRP B CE2 
14310 C CE3 . TRP B 708  ? 0.1978 0.2031 0.2249 0.0194  0.0007  -0.0184 706  TRP B CE3 
14311 C CZ2 . TRP B 708  ? 0.1926 0.2011 0.2247 0.0184  -0.0020 -0.0168 706  TRP B CZ2 
14312 C CZ3 . TRP B 708  ? 0.1880 0.1916 0.2144 0.0190  -0.0010 -0.0182 706  TRP B CZ3 
14313 C CH2 . TRP B 708  ? 0.1946 0.1998 0.2234 0.0186  -0.0023 -0.0174 706  TRP B CH2 
14314 N N   . ASN B 709  ? 0.1628 0.1709 0.1884 0.0162  0.0017  -0.0181 707  ASN B N   
14315 C CA  . ASN B 709  ? 0.1675 0.1737 0.1918 0.0156  0.0002  -0.0182 707  ASN B CA  
14316 C C   . ASN B 709  ? 0.1913 0.1957 0.2122 0.0146  0.0000  -0.0187 707  ASN B C   
14317 O O   . ASN B 709  ? 0.2039 0.2063 0.2231 0.0142  -0.0009 -0.0189 707  ASN B O   
14318 C CB  . ASN B 709  ? 0.1734 0.1808 0.1998 0.0149  -0.0010 -0.0176 707  ASN B CB  
14319 C CG  . ASN B 709  ? 0.1662 0.1744 0.1921 0.0138  -0.0008 -0.0174 707  ASN B CG  
14320 O OD1 . ASN B 709  ? 0.2146 0.2244 0.2417 0.0138  0.0001  -0.0171 707  ASN B OD1 
14321 N ND2 . ASN B 709  ? 0.1997 0.2068 0.2239 0.0129  -0.0018 -0.0176 707  ASN B ND2 
14322 N N   . PHE B 710  ? 0.1825 0.1877 0.2024 0.0141  0.0009  -0.0188 708  PHE B N   
14323 C CA  . PHE B 710  ? 0.1904 0.1945 0.2074 0.0132  0.0008  -0.0192 708  PHE B CA  
14324 C C   . PHE B 710  ? 0.1889 0.1928 0.2046 0.0137  0.0021  -0.0197 708  PHE B C   
14325 O O   . PHE B 710  ? 0.1913 0.1966 0.2068 0.0134  0.0028  -0.0195 708  PHE B O   
14326 C CB  . PHE B 710  ? 0.1916 0.1969 0.2084 0.0122  0.0006  -0.0189 708  PHE B CB  
14327 C CG  . PHE B 710  ? 0.1968 0.2020 0.2143 0.0117  -0.0006 -0.0186 708  PHE B CG  
14328 C CD1 . PHE B 710  ? 0.2319 0.2355 0.2484 0.0115  -0.0015 -0.0187 708  PHE B CD1 
14329 C CD2 . PHE B 710  ? 0.2125 0.2190 0.2313 0.0115  -0.0007 -0.0182 708  PHE B CD2 
14330 C CE1 . PHE B 710  ? 0.2252 0.2287 0.2420 0.0111  -0.0025 -0.0184 708  PHE B CE1 
14331 C CE2 . PHE B 710  ? 0.2240 0.2302 0.2430 0.0111  -0.0017 -0.0181 708  PHE B CE2 
14332 C CZ  . PHE B 710  ? 0.2197 0.2246 0.2377 0.0109  -0.0026 -0.0182 708  PHE B CZ  
14333 N N   . PRO B 711  ? 0.1797 0.1818 0.1945 0.0146  0.0024  -0.0202 709  PRO B N   
14334 C CA  . PRO B 711  ? 0.1888 0.1910 0.2030 0.0156  0.0038  -0.0207 709  PRO B CA  
14335 C C   . PRO B 711  ? 0.1849 0.1861 0.1957 0.0148  0.0042  -0.0213 709  PRO B C   
14336 O O   . PRO B 711  ? 0.1884 0.1899 0.1983 0.0154  0.0054  -0.0216 709  PRO B O   
14337 C CB  . PRO B 711  ? 0.2061 0.2061 0.2201 0.0169  0.0038  -0.0212 709  PRO B CB  
14338 C CG  . PRO B 711  ? 0.2223 0.2200 0.2349 0.0160  0.0023  -0.0213 709  PRO B CG  
14339 C CD  . PRO B 711  ? 0.1904 0.1902 0.2048 0.0149  0.0015  -0.0204 709  PRO B CD  
14340 N N   . LEU B 712  ? 0.1718 0.1719 0.1806 0.0134  0.0031  -0.0214 710  LEU B N   
14341 C CA  . LEU B 712  ? 0.1824 0.1822 0.1885 0.0125  0.0032  -0.0218 710  LEU B CA  
14342 C C   . LEU B 712  ? 0.1715 0.1737 0.1783 0.0115  0.0029  -0.0210 710  LEU B C   
14343 O O   . LEU B 712  ? 0.1825 0.1859 0.1884 0.0112  0.0033  -0.0209 710  LEU B O   
14344 C CB  . LEU B 712  ? 0.1846 0.1814 0.1877 0.0115  0.0023  -0.0225 710  LEU B CB  
14345 C CG  . LEU B 712  ? 0.1699 0.1665 0.1701 0.0103  0.0022  -0.0229 710  LEU B CG  
14346 C CD1 . LEU B 712  ? 0.1966 0.1929 0.1953 0.0112  0.0034  -0.0235 710  LEU B CD1 
14347 C CD2 . LEU B 712  ? 0.2239 0.2177 0.2215 0.0090  0.0011  -0.0234 710  LEU B CD2 
14348 N N   . ALA B 713  ? 0.1692 0.1721 0.1776 0.0110  0.0020  -0.0205 711  ALA B N   
14349 C CA  . ALA B 713  ? 0.1699 0.1747 0.1785 0.0102  0.0017  -0.0199 711  ALA B CA  
14350 C C   . ALA B 713  ? 0.1655 0.1724 0.1759 0.0108  0.0024  -0.0193 711  ALA B C   
14351 O O   . ALA B 713  ? 0.1662 0.1743 0.1758 0.0105  0.0026  -0.0191 711  ALA B O   
14352 C CB  . ALA B 713  ? 0.1867 0.1915 0.1962 0.0097  0.0007  -0.0197 711  ALA B CB  
14353 N N   . ILE B 714  ? 0.1786 0.1860 0.1915 0.0115  0.0027  -0.0190 712  ILE B N   
14354 C CA  . ILE B 714  ? 0.1832 0.1923 0.1975 0.0118  0.0033  -0.0182 712  ILE B CA  
14355 C C   . ILE B 714  ? 0.1781 0.1875 0.1914 0.0122  0.0045  -0.0183 712  ILE B C   
14356 O O   . ILE B 714  ? 0.1717 0.1823 0.1847 0.0121  0.0049  -0.0177 712  ILE B O   
14357 C CB  . ILE B 714  ? 0.1719 0.1815 0.1892 0.0122  0.0032  -0.0178 712  ILE B CB  
14358 C CG1 . ILE B 714  ? 0.1988 0.2081 0.2165 0.0117  0.0021  -0.0178 712  ILE B CG1 
14359 C CG2 . ILE B 714  ? 0.1857 0.1968 0.2045 0.0124  0.0041  -0.0170 712  ILE B CG2 
14360 C CD1 . ILE B 714  ? 0.3053 0.3150 0.3255 0.0118  0.0016  -0.0174 712  ILE B CD1 
14361 N N   . PHE B 715  ? 0.1715 0.1799 0.1842 0.0128  0.0051  -0.0189 713  PHE B N   
14362 C CA  . PHE B 715  ? 0.1710 0.1794 0.1820 0.0133  0.0063  -0.0192 713  PHE B CA  
14363 C C   . PHE B 715  ? 0.1683 0.1768 0.1766 0.0125  0.0060  -0.0193 713  PHE B C   
14364 O O   . PHE B 715  ? 0.1673 0.1769 0.1750 0.0126  0.0067  -0.0188 713  PHE B O   
14365 C CB  . PHE B 715  ? 0.1686 0.1751 0.1785 0.0141  0.0066  -0.0202 713  PHE B CB  
14366 C CG  . PHE B 715  ? 0.1655 0.1716 0.1732 0.0147  0.0079  -0.0208 713  PHE B CG  
14367 C CD1 . PHE B 715  ? 0.1653 0.1731 0.1746 0.0157  0.0094  -0.0203 713  PHE B CD1 
14368 C CD2 . PHE B 715  ? 0.1718 0.1759 0.1757 0.0142  0.0076  -0.0217 713  PHE B CD2 
14369 C CE1 . PHE B 715  ? 0.1783 0.1858 0.1852 0.0164  0.0107  -0.0209 713  PHE B CE1 
14370 C CE2 . PHE B 715  ? 0.1976 0.2012 0.1990 0.0148  0.0088  -0.0223 713  PHE B CE2 
14371 C CZ  . PHE B 715  ? 0.1823 0.1875 0.1851 0.0160  0.0104  -0.0219 713  PHE B CZ  
14372 N N   . THR B 716  ? 0.1547 0.1619 0.1612 0.0117  0.0049  -0.0198 714  THR B N   
14373 C CA  . THR B 716  ? 0.1669 0.1744 0.1709 0.0108  0.0045  -0.0199 714  THR B CA  
14374 C C   . THR B 716  ? 0.1719 0.1816 0.1771 0.0105  0.0042  -0.0189 714  THR B C   
14375 O O   . THR B 716  ? 0.1675 0.1782 0.1714 0.0103  0.0043  -0.0185 714  THR B O   
14376 C CB  . THR B 716  ? 0.1604 0.1663 0.1627 0.0097  0.0034  -0.0206 714  THR B CB  
14377 O OG1 . THR B 716  ? 0.1946 0.1979 0.1953 0.0101  0.0036  -0.0216 714  THR B OG1 
14378 C CG2 . THR B 716  ? 0.1898 0.1966 0.1899 0.0086  0.0027  -0.0205 714  THR B CG2 
14379 N N   . GLY B 717  ? 0.1700 0.1803 0.1775 0.0105  0.0037  -0.0184 715  GLY B N   
14380 C CA  . GLY B 717  ? 0.1710 0.1830 0.1795 0.0104  0.0034  -0.0175 715  GLY B CA  
14381 C C   . GLY B 717  ? 0.1649 0.1778 0.1739 0.0109  0.0042  -0.0167 715  GLY B C   
14382 O O   . GLY B 717  ? 0.1633 0.1772 0.1715 0.0109  0.0041  -0.0161 715  GLY B O   
14383 N N   . GLN B 718  ? 0.1571 0.1697 0.1675 0.0115  0.0051  -0.0165 716  GLN B N   
14384 C CA  . GLN B 718  ? 0.1537 0.1672 0.1647 0.0118  0.0059  -0.0156 716  GLN B CA  
14385 C C   . GLN B 718  ? 0.1650 0.1788 0.1734 0.0118  0.0065  -0.0155 716  GLN B C   
14386 O O   . GLN B 718  ? 0.1585 0.1731 0.1662 0.0118  0.0066  -0.0146 716  GLN B O   
14387 C CB  . GLN B 718  ? 0.1618 0.1755 0.1751 0.0122  0.0068  -0.0153 716  GLN B CB  
14388 C CG  . GLN B 718  ? 0.1577 0.1711 0.1737 0.0121  0.0060  -0.0152 716  GLN B CG  
14389 C CD  . GLN B 718  ? 0.1617 0.1758 0.1803 0.0124  0.0067  -0.0148 716  GLN B CD  
14390 O OE1 . GLN B 718  ? 0.1846 0.1989 0.2052 0.0121  0.0063  -0.0141 716  GLN B OE1 
14391 N NE2 . GLN B 718  ? 0.1688 0.1833 0.1874 0.0129  0.0077  -0.0151 716  GLN B NE2 
14392 N N   . ILE B 719  ? 0.1642 0.1771 0.1708 0.0119  0.0069  -0.0166 717  ILE B N   
14393 C CA  . ILE B 719  ? 0.1627 0.1754 0.1662 0.0119  0.0075  -0.0168 717  ILE B CA  
14394 C C   . ILE B 719  ? 0.1689 0.1821 0.1705 0.0111  0.0064  -0.0166 717  ILE B C   
14395 O O   . ILE B 719  ? 0.1670 0.1810 0.1668 0.0111  0.0066  -0.0160 717  ILE B O   
14396 C CB  . ILE B 719  ? 0.1793 0.1903 0.1811 0.0122  0.0080  -0.0182 717  ILE B CB  
14397 C CG1 . ILE B 719  ? 0.1844 0.1956 0.1883 0.0132  0.0093  -0.0181 717  ILE B CG1 
14398 C CG2 . ILE B 719  ? 0.2299 0.2403 0.2278 0.0119  0.0082  -0.0187 717  ILE B CG2 
14399 C CD1 . ILE B 719  ? 0.2755 0.2848 0.2783 0.0137  0.0095  -0.0195 717  ILE B CD1 
14400 N N   . ALA B 720  ? 0.1638 0.1767 0.1655 0.0105  0.0052  -0.0171 718  ALA B N   
14401 C CA  . ALA B 720  ? 0.1529 0.1669 0.1531 0.0097  0.0040  -0.0169 718  ALA B CA  
14402 C C   . ALA B 720  ? 0.1601 0.1758 0.1614 0.0101  0.0039  -0.0156 718  ALA B C   
14403 O O   . ALA B 720  ? 0.1723 0.1891 0.1720 0.0099  0.0034  -0.0150 718  ALA B O   
14404 C CB  . ALA B 720  ? 0.1781 0.1918 0.1788 0.0090  0.0029  -0.0175 718  ALA B CB  
14405 N N   . ALA B 721  ? 0.1584 0.1743 0.1624 0.0106  0.0040  -0.0150 719  ALA B N   
14406 C CA  . ALA B 721  ? 0.1621 0.1791 0.1672 0.0111  0.0038  -0.0137 719  ALA B CA  
14407 C C   . ALA B 721  ? 0.1510 0.1681 0.1549 0.0114  0.0047  -0.0128 719  ALA B C   
14408 O O   . ALA B 721  ? 0.1594 0.1774 0.1623 0.0115  0.0042  -0.0119 719  ALA B O   
14409 C CB  . ALA B 721  ? 0.1633 0.1799 0.1712 0.0115  0.0039  -0.0135 719  ALA B CB  
14410 N N   . ALA B 722  ? 0.1497 0.1660 0.1538 0.0115  0.0059  -0.0130 720  ALA B N   
14411 C CA  . ALA B 722  ? 0.1456 0.1622 0.1484 0.0117  0.0068  -0.0120 720  ALA B CA  
14412 C C   . ALA B 722  ? 0.1538 0.1707 0.1531 0.0114  0.0066  -0.0122 720  ALA B C   
14413 O O   . ALA B 722  ? 0.1652 0.1828 0.1632 0.0115  0.0065  -0.0110 720  ALA B O   
14414 C CB  . ALA B 722  ? 0.1526 0.1688 0.1563 0.0120  0.0083  -0.0123 720  ALA B CB  
14415 N N   . LEU B 723  ? 0.1548 0.1711 0.1524 0.0110  0.0063  -0.0136 721  LEU B N   
14416 C CA  . LEU B 723  ? 0.1639 0.1802 0.1577 0.0106  0.0060  -0.0140 721  LEU B CA  
14417 C C   . LEU B 723  ? 0.1752 0.1931 0.1687 0.0102  0.0044  -0.0132 721  LEU B C   
14418 O O   . LEU B 723  ? 0.1729 0.1915 0.1640 0.0101  0.0042  -0.0125 721  LEU B O   
14419 C CB  . LEU B 723  ? 0.1722 0.1870 0.1644 0.0100  0.0057  -0.0158 721  LEU B CB  
14420 C CG  . LEU B 723  ? 0.1792 0.1925 0.1707 0.0106  0.0072  -0.0167 721  LEU B CG  
14421 C CD1 . LEU B 723  ? 0.1902 0.2016 0.1805 0.0101  0.0066  -0.0184 721  LEU B CD1 
14422 C CD2 . LEU B 723  ? 0.1891 0.2023 0.1776 0.0109  0.0084  -0.0166 721  LEU B CD2 
14423 N N   . VAL B 724  ? 0.1549 0.1734 0.1505 0.0100  0.0034  -0.0133 722  VAL B N   
14424 C CA  . VAL B 724  ? 0.1572 0.1776 0.1526 0.0097  0.0020  -0.0127 722  VAL B CA  
14425 C C   . VAL B 724  ? 0.1628 0.1842 0.1591 0.0106  0.0020  -0.0109 722  VAL B C   
14426 O O   . VAL B 724  ? 0.1732 0.1962 0.1685 0.0106  0.0010  -0.0101 722  VAL B O   
14427 C CB  . VAL B 724  ? 0.1500 0.1712 0.1474 0.0093  0.0010  -0.0132 722  VAL B CB  
14428 C CG1 . VAL B 724  ? 0.1762 0.1976 0.1768 0.0102  0.0013  -0.0126 722  VAL B CG1 
14429 C CG2 . VAL B 724  ? 0.1723 0.1957 0.1687 0.0086  -0.0004 -0.0130 722  VAL B CG2 
14430 N N   . ALA B 725  ? 0.1750 0.1955 0.1731 0.0113  0.0030  -0.0103 723  ALA B N   
14431 C CA  . ALA B 725  ? 0.1688 0.1894 0.1673 0.0120  0.0032  -0.0087 723  ALA B CA  
14432 C C   . ALA B 725  ? 0.1955 0.2161 0.1912 0.0119  0.0038  -0.0079 723  ALA B C   
14433 O O   . ALA B 725  ? 0.2159 0.2364 0.2115 0.0124  0.0039  -0.0063 723  ALA B O   
14434 C CB  . ALA B 725  ? 0.1825 0.2019 0.1838 0.0125  0.0039  -0.0083 723  ALA B CB  
14435 N N   . GLY B 726  ? 0.1729 0.1931 0.1660 0.0113  0.0042  -0.0089 724  GLY B N   
14436 C CA  . GLY B 726  ? 0.1822 0.2023 0.1719 0.0112  0.0047  -0.0083 724  GLY B CA  
14437 C C   . GLY B 726  ? 0.1940 0.2131 0.1834 0.0114  0.0067  -0.0083 724  GLY B C   
14438 O O   . GLY B 726  ? 0.2089 0.2280 0.1956 0.0114  0.0074  -0.0075 724  GLY B O   
14439 N N   . ASN B 727  ? 0.1722 0.1905 0.1641 0.0115  0.0076  -0.0091 725  ASN B N   
14440 C CA  . ASN B 727  ? 0.1766 0.1945 0.1690 0.0118  0.0094  -0.0089 725  ASN B CA  
14441 C C   . ASN B 727  ? 0.1738 0.1910 0.1647 0.0118  0.0103  -0.0108 725  ASN B C   
14442 O O   . ASN B 727  ? 0.2022 0.2188 0.1939 0.0116  0.0095  -0.0121 725  ASN B O   
14443 C CB  . ASN B 727  ? 0.1755 0.1933 0.1722 0.0120  0.0097  -0.0085 725  ASN B CB  
14444 C CG  . ASN B 727  ? 0.1969 0.2148 0.1951 0.0121  0.0088  -0.0070 725  ASN B CG  
14445 O OD1 . ASN B 727  ? 0.1920 0.2098 0.1899 0.0121  0.0094  -0.0054 725  ASN B OD1 
14446 N ND2 . ASN B 727  ? 0.1765 0.1943 0.1764 0.0122  0.0075  -0.0075 725  ASN B ND2 
14447 N N   . PRO B 728  ? 0.1723 0.1894 0.1610 0.0120  0.0119  -0.0108 726  PRO B N   
14448 C CA  . PRO B 728  ? 0.1820 0.1982 0.1698 0.0124  0.0129  -0.0126 726  PRO B CA  
14449 C C   . PRO B 728  ? 0.2007 0.2171 0.1928 0.0128  0.0137  -0.0126 726  PRO B C   
14450 O O   . PRO B 728  ? 0.1949 0.2123 0.1899 0.0128  0.0141  -0.0112 726  PRO B O   
14451 C CB  . PRO B 728  ? 0.2071 0.2236 0.1917 0.0127  0.0147  -0.0122 726  PRO B CB  
14452 C CG  . PRO B 728  ? 0.2199 0.2377 0.2057 0.0125  0.0151  -0.0100 726  PRO B CG  
14453 C CD  . PRO B 728  ? 0.1868 0.2046 0.1741 0.0121  0.0130  -0.0091 726  PRO B CD  
14454 N N   . VAL B 729  ? 0.1691 0.1845 0.1614 0.0132  0.0139  -0.0143 727  VAL B N   
14455 C CA  . VAL B 729  ? 0.1740 0.1896 0.1704 0.0136  0.0141  -0.0145 727  VAL B CA  
14456 C C   . VAL B 729  ? 0.1820 0.1976 0.1785 0.0146  0.0160  -0.0154 727  VAL B C   
14457 O O   . VAL B 729  ? 0.1843 0.1985 0.1775 0.0151  0.0165  -0.0168 727  VAL B O   
14458 C CB  . VAL B 729  ? 0.1777 0.1921 0.1749 0.0132  0.0124  -0.0156 727  VAL B CB  
14459 C CG1 . VAL B 729  ? 0.1827 0.1969 0.1833 0.0137  0.0126  -0.0160 727  VAL B CG1 
14460 C CG2 . VAL B 729  ? 0.1812 0.1962 0.1795 0.0125  0.0109  -0.0145 727  VAL B CG2 
14461 N N   . LEU B 730  ? 0.1596 0.1766 0.1600 0.0150  0.0169  -0.0146 728  LEU B N   
14462 C CA  . LEU B 730  ? 0.1643 0.1817 0.1662 0.0161  0.0184  -0.0154 728  LEU B CA  
14463 C C   . LEU B 730  ? 0.1602 0.1771 0.1654 0.0162  0.0171  -0.0159 728  LEU B C   
14464 O O   . LEU B 730  ? 0.1778 0.1958 0.1864 0.0156  0.0165  -0.0148 728  LEU B O   
14465 C CB  . LEU B 730  ? 0.1786 0.1987 0.1829 0.0163  0.0202  -0.0139 728  LEU B CB  
14466 C CG  . LEU B 730  ? 0.1981 0.2191 0.1994 0.0162  0.0217  -0.0129 728  LEU B CG  
14467 C CD1 . LEU B 730  ? 0.1977 0.2170 0.1940 0.0169  0.0223  -0.0146 728  LEU B CD1 
14468 C CD2 . LEU B 730  ? 0.1915 0.2126 0.1922 0.0149  0.0206  -0.0113 728  LEU B CD2 
14469 N N   . ALA B 731  ? 0.1655 0.1804 0.1694 0.0168  0.0167  -0.0175 729  ALA B N   
14470 C CA  . ALA B 731  ? 0.1557 0.1697 0.1620 0.0167  0.0153  -0.0180 729  ALA B CA  
14471 C C   . ALA B 731  ? 0.1820 0.1968 0.1911 0.0180  0.0164  -0.0183 729  ALA B C   
14472 O O   . ALA B 731  ? 0.1702 0.1841 0.1776 0.0193  0.0175  -0.0194 729  ALA B O   
14473 C CB  . ALA B 731  ? 0.1875 0.1988 0.1907 0.0164  0.0140  -0.0194 729  ALA B CB  
14474 N N   . LYS B 732  ? 0.1685 0.1851 0.1820 0.0178  0.0160  -0.0173 730  LYS B N   
14475 C CA  . LYS B 732  ? 0.1660 0.1841 0.1829 0.0190  0.0169  -0.0172 730  LYS B CA  
14476 C C   . LYS B 732  ? 0.1673 0.1842 0.1861 0.0189  0.0151  -0.0176 730  LYS B C   
14477 O O   . LYS B 732  ? 0.1625 0.1803 0.1840 0.0179  0.0139  -0.0167 730  LYS B O   
14478 C CB  . LYS B 732  ? 0.1617 0.1831 0.1821 0.0187  0.0179  -0.0156 730  LYS B CB  
14479 C CG  . LYS B 732  ? 0.1679 0.1919 0.1910 0.0201  0.0197  -0.0155 730  LYS B CG  
14480 C CD  . LYS B 732  ? 0.1694 0.1930 0.1949 0.0212  0.0189  -0.0162 730  LYS B CD  
14481 C CE  . LYS B 732  ? 0.1633 0.1883 0.1931 0.0201  0.0174  -0.0151 730  LYS B CE  
14482 N NZ  . LYS B 732  ? 0.1812 0.2058 0.2131 0.0212  0.0165  -0.0157 730  LYS B NZ  
14483 N N   . PRO B 733  ? 0.1552 0.1697 0.1723 0.0198  0.0147  -0.0190 731  PRO B N   
14484 C CA  . PRO B 733  ? 0.1711 0.1842 0.1896 0.0196  0.0129  -0.0192 731  PRO B CA  
14485 C C   . PRO B 733  ? 0.1499 0.1650 0.1727 0.0206  0.0132  -0.0187 731  PRO B C   
14486 O O   . PRO B 733  ? 0.1615 0.1788 0.1860 0.0218  0.0148  -0.0184 731  PRO B O   
14487 C CB  . PRO B 733  ? 0.1821 0.1917 0.1970 0.0202  0.0126  -0.0207 731  PRO B CB  
14488 C CG  . PRO B 733  ? 0.1759 0.1857 0.1891 0.0216  0.0147  -0.0214 731  PRO B CG  
14489 C CD  . PRO B 733  ? 0.1782 0.1907 0.1917 0.0209  0.0158  -0.0203 731  PRO B CD  
14490 N N   . ALA B 734  ? 0.1564 0.1710 0.1810 0.0201  0.0115  -0.0185 732  ALA B N   
14491 C CA  . ALA B 734  ? 0.1638 0.1803 0.1925 0.0210  0.0112  -0.0179 732  ALA B CA  
14492 C C   . ALA B 734  ? 0.1709 0.1869 0.1995 0.0231  0.0123  -0.0187 732  ALA B C   
14493 O O   . ALA B 734  ? 0.1856 0.1984 0.2107 0.0238  0.0124  -0.0200 732  ALA B O   
14494 C CB  . ALA B 734  ? 0.1736 0.1887 0.2029 0.0202  0.0090  -0.0179 732  ALA B CB  
14495 N N   . GLU B 735  ? 0.1661 0.1853 0.1987 0.0242  0.0131  -0.0180 733  GLU B N   
14496 C CA  . GLU B 735  ? 0.1766 0.1957 0.2095 0.0266  0.0144  -0.0187 733  GLU B CA  
14497 C C   . GLU B 735  ? 0.1924 0.2081 0.2242 0.0275  0.0129  -0.0196 733  GLU B C   
14498 O O   . GLU B 735  ? 0.2027 0.2162 0.2326 0.0294  0.0137  -0.0206 733  GLU B O   
14499 C CB  . GLU B 735  ? 0.2000 0.2239 0.2381 0.0277  0.0155  -0.0177 733  GLU B CB  
14500 C CG  . GLU B 735  ? 0.2454 0.2716 0.2879 0.0268  0.0138  -0.0165 733  GLU B CG  
14501 C CD  . GLU B 735  ? 0.2384 0.2669 0.2826 0.0245  0.0134  -0.0152 733  GLU B CD  
14502 O OE1 . GLU B 735  ? 0.2543 0.2814 0.2955 0.0232  0.0137  -0.0154 733  GLU B OE1 
14503 O OE2 . GLU B 735  ? 0.2634 0.2952 0.3121 0.0239  0.0128  -0.0141 733  GLU B OE2 
14504 N N   . GLU B 736  ? 0.1732 0.1879 0.2056 0.0262  0.0107  -0.0191 734  GLU B N   
14505 C CA  . GLU B 736  ? 0.1982 0.2097 0.2296 0.0269  0.0092  -0.0197 734  GLU B CA  
14506 C C   . GLU B 736  ? 0.1907 0.1974 0.2168 0.0265  0.0089  -0.0209 734  GLU B C   
14507 O O   . GLU B 736  ? 0.2195 0.2230 0.2440 0.0275  0.0083  -0.0216 734  GLU B O   
14508 C CB  . GLU B 736  ? 0.1890 0.2010 0.2223 0.0255  0.0070  -0.0188 734  GLU B CB  
14509 C CG  . GLU B 736  ? 0.2103 0.2266 0.2488 0.0258  0.0068  -0.0175 734  GLU B CG  
14510 C CD  . GLU B 736  ? 0.2376 0.2570 0.2780 0.0240  0.0071  -0.0167 734  GLU B CD  
14511 O OE1 . GLU B 736  ? 0.2081 0.2270 0.2461 0.0231  0.0081  -0.0169 734  GLU B OE1 
14512 O OE2 . GLU B 736  ? 0.2800 0.3021 0.3242 0.0234  0.0062  -0.0156 734  GLU B OE2 
14513 N N   . THR B 737  ? 0.1825 0.1887 0.2059 0.0248  0.0091  -0.0211 735  THR B N   
14514 C CA  . THR B 737  ? 0.1889 0.1911 0.2077 0.0238  0.0084  -0.0221 735  THR B CA  
14515 C C   . THR B 737  ? 0.1836 0.1852 0.1991 0.0235  0.0097  -0.0228 735  THR B C   
14516 O O   . THR B 737  ? 0.1927 0.1937 0.2059 0.0218  0.0092  -0.0229 735  THR B O   
14517 C CB  . THR B 737  ? 0.1870 0.1889 0.2056 0.0217  0.0066  -0.0215 735  THR B CB  
14518 O OG1 . THR B 737  ? 0.1905 0.1958 0.2111 0.0207  0.0069  -0.0206 735  THR B OG1 
14519 C CG2 . THR B 737  ? 0.1945 0.1960 0.2152 0.0219  0.0050  -0.0210 735  THR B CG2 
14520 N N   . PRO B 738  ? 0.1727 0.1744 0.1876 0.0253  0.0115  -0.0235 736  PRO B N   
14521 C CA  . PRO B 738  ? 0.1728 0.1740 0.1843 0.0251  0.0128  -0.0242 736  PRO B CA  
14522 C C   . PRO B 738  ? 0.1836 0.1800 0.1899 0.0245  0.0120  -0.0256 736  PRO B C   
14523 O O   . PRO B 738  ? 0.1900 0.1860 0.1932 0.0235  0.0124  -0.0261 736  PRO B O   
14524 C CB  . PRO B 738  ? 0.1807 0.1835 0.1933 0.0274  0.0150  -0.0246 736  PRO B CB  
14525 C CG  . PRO B 738  ? 0.1901 0.1916 0.2047 0.0292  0.0144  -0.0247 736  PRO B CG  
14526 C CD  . PRO B 738  ? 0.1762 0.1788 0.1936 0.0278  0.0124  -0.0236 736  PRO B CD  
14527 N N   . LEU B 739  ? 0.1729 0.1658 0.1782 0.0250  0.0110  -0.0262 737  LEU B N   
14528 C CA  . LEU B 739  ? 0.1846 0.1726 0.1848 0.0245  0.0104  -0.0276 737  LEU B CA  
14529 C C   . LEU B 739  ? 0.1843 0.1718 0.1825 0.0217  0.0089  -0.0274 737  LEU B C   
14530 O O   . LEU B 739  ? 0.1920 0.1779 0.1864 0.0208  0.0090  -0.0282 737  LEU B O   
14531 C CB  . LEU B 739  ? 0.1949 0.1790 0.1945 0.0257  0.0096  -0.0283 737  LEU B CB  
14532 C CG  . LEU B 739  ? 0.1959 0.1805 0.1976 0.0288  0.0111  -0.0285 737  LEU B CG  
14533 C CD1 . LEU B 739  ? 0.2244 0.2048 0.2255 0.0298  0.0099  -0.0289 737  LEU B CD1 
14534 C CD2 . LEU B 739  ? 0.2138 0.1977 0.2127 0.0302  0.0132  -0.0298 737  LEU B CD2 
14535 N N   . ILE B 740  ? 0.1928 0.1816 0.1934 0.0205  0.0076  -0.0263 738  ILE B N   
14536 C CA  . ILE B 740  ? 0.1827 0.1714 0.1816 0.0181  0.0063  -0.0261 738  ILE B CA  
14537 C C   . ILE B 740  ? 0.1684 0.1603 0.1673 0.0173  0.0071  -0.0256 738  ILE B C   
14538 O O   . ILE B 740  ? 0.1900 0.1814 0.1864 0.0157  0.0065  -0.0258 738  ILE B O   
14539 C CB  . ILE B 740  ? 0.2052 0.1945 0.2063 0.0170  0.0048  -0.0251 738  ILE B CB  
14540 C CG1 . ILE B 740  ? 0.2135 0.2026 0.2126 0.0146  0.0036  -0.0249 738  ILE B CG1 
14541 C CG2 . ILE B 740  ? 0.2181 0.2116 0.2235 0.0174  0.0051  -0.0239 738  ILE B CG2 
14542 C CD1 . ILE B 740  ? 0.2331 0.2179 0.2281 0.0137  0.0028  -0.0259 738  ILE B CD1 
14543 N N   . ALA B 741  ? 0.1777 0.1729 0.1796 0.0184  0.0083  -0.0249 739  ALA B N   
14544 C CA  . ALA B 741  ? 0.1784 0.1763 0.1801 0.0178  0.0092  -0.0244 739  ALA B CA  
14545 C C   . ALA B 741  ? 0.1828 0.1790 0.1804 0.0180  0.0100  -0.0255 739  ALA B C   
14546 O O   . ALA B 741  ? 0.1873 0.1839 0.1827 0.0167  0.0097  -0.0255 739  ALA B O   
14547 C CB  . ALA B 741  ? 0.1955 0.1970 0.2011 0.0189  0.0104  -0.0234 739  ALA B CB  
14548 N N   . ALA B 742  ? 0.1818 0.1758 0.1780 0.0197  0.0111  -0.0266 740  ALA B N   
14549 C CA  . ALA B 742  ? 0.1869 0.1787 0.1786 0.0200  0.0119  -0.0279 740  ALA B CA  
14550 C C   . ALA B 742  ? 0.1899 0.1786 0.1778 0.0181  0.0102  -0.0287 740  ALA B C   
14551 O O   . ALA B 742  ? 0.1956 0.1839 0.1800 0.0171  0.0102  -0.0291 740  ALA B O   
14552 C CB  . ALA B 742  ? 0.1951 0.1847 0.1860 0.0224  0.0132  -0.0291 740  ALA B CB  
14553 N N   . GLU B 743  ? 0.1923 0.1789 0.1806 0.0173  0.0087  -0.0287 741  GLU B N   
14554 C CA  . GLU B 743  ? 0.1995 0.1835 0.1845 0.0152  0.0070  -0.0292 741  GLU B CA  
14555 C C   . GLU B 743  ? 0.1841 0.1713 0.1698 0.0133  0.0062  -0.0282 741  GLU B C   
14556 O O   . GLU B 743  ? 0.2007 0.1872 0.1832 0.0118  0.0054  -0.0286 741  GLU B O   
14557 C CB  . GLU B 743  ? 0.2160 0.1972 0.2015 0.0149  0.0057  -0.0292 741  GLU B CB  
14558 C CG  . GLU B 743  ? 0.2281 0.2068 0.2106 0.0125  0.0040  -0.0296 741  GLU B CG  
14559 C CD  . GLU B 743  ? 0.2479 0.2223 0.2254 0.0122  0.0039  -0.0312 741  GLU B CD  
14560 O OE1 . GLU B 743  ? 0.2480 0.2208 0.2239 0.0142  0.0054  -0.0323 741  GLU B OE1 
14561 O OE2 . GLU B 743  ? 0.3008 0.2733 0.2757 0.0099  0.0024  -0.0315 741  GLU B OE2 
14562 N N   . GLY B 744  ? 0.1913 0.1822 0.1810 0.0134  0.0063  -0.0268 742  GLY B N   
14563 C CA  . GLY B 744  ? 0.2002 0.1942 0.1906 0.0120  0.0057  -0.0257 742  GLY B CA  
14564 C C   . GLY B 744  ? 0.1785 0.1736 0.1666 0.0120  0.0065  -0.0259 742  GLY B C   
14565 O O   . GLY B 744  ? 0.1827 0.1785 0.1690 0.0105  0.0056  -0.0257 742  GLY B O   
14566 N N   . VAL B 745  ? 0.1873 0.1827 0.1754 0.0136  0.0083  -0.0261 743  VAL B N   
14567 C CA  . VAL B 745  ? 0.1779 0.1741 0.1633 0.0137  0.0092  -0.0262 743  VAL B CA  
14568 C C   . VAL B 745  ? 0.2020 0.1949 0.1824 0.0129  0.0086  -0.0277 743  VAL B C   
14569 O O   . VAL B 745  ? 0.1961 0.1897 0.1739 0.0118  0.0081  -0.0276 743  VAL B O   
14570 C CB  . VAL B 745  ? 0.1972 0.1948 0.1840 0.0156  0.0113  -0.0260 743  VAL B CB  
14571 C CG1 . VAL B 745  ? 0.2000 0.1978 0.1831 0.0158  0.0124  -0.0264 743  VAL B CG1 
14572 C CG2 . VAL B 745  ? 0.2048 0.2060 0.1963 0.0157  0.0116  -0.0243 743  VAL B CG2 
14573 N N   . ARG B 746  ? 0.1889 0.1780 0.1675 0.0134  0.0084  -0.0291 744  ARG B N   
14574 C CA  . ARG B 746  ? 0.2004 0.1857 0.1739 0.0124  0.0076  -0.0306 744  ARG B CA  
14575 C C   . ARG B 746  ? 0.1986 0.1846 0.1713 0.0098  0.0055  -0.0301 744  ARG B C   
14576 O O   . ARG B 746  ? 0.2039 0.1893 0.1729 0.0086  0.0048  -0.0306 744  ARG B O   
14577 C CB  . ARG B 746  ? 0.2042 0.1847 0.1762 0.0130  0.0073  -0.0320 744  ARG B CB  
14578 C CG  . ARG B 746  ? 0.2239 0.2030 0.1959 0.0157  0.0093  -0.0328 744  ARG B CG  
14579 C CD  . ARG B 746  ? 0.2279 0.2017 0.1979 0.0163  0.0087  -0.0342 744  ARG B CD  
14580 N NE  . ARG B 746  ? 0.2446 0.2176 0.2156 0.0192  0.0106  -0.0348 744  ARG B NE  
14581 C CZ  . ARG B 746  ? 0.2212 0.1956 0.1965 0.0207  0.0110  -0.0340 744  ARG B CZ  
14582 N NH1 . ARG B 746  ? 0.2366 0.2120 0.2151 0.0196  0.0096  -0.0328 744  ARG B NH1 
14583 N NH2 . ARG B 746  ? 0.2417 0.2169 0.2184 0.0234  0.0130  -0.0343 744  ARG B NH2 
14584 N N   . ILE B 747  ? 0.1846 0.1721 0.1607 0.0090  0.0045  -0.0290 745  ILE B N   
14585 C CA  . ILE B 747  ? 0.1872 0.1758 0.1631 0.0067  0.0026  -0.0285 745  ILE B CA  
14586 C C   . ILE B 747  ? 0.1879 0.1806 0.1644 0.0061  0.0025  -0.0274 745  ILE B C   
14587 O O   . ILE B 747  ? 0.1893 0.1824 0.1635 0.0045  0.0013  -0.0274 745  ILE B O   
14588 C CB  . ILE B 747  ? 0.1919 0.1811 0.1711 0.0061  0.0018  -0.0277 745  ILE B CB  
14589 C CG1 . ILE B 747  ? 0.2110 0.1955 0.1884 0.0059  0.0013  -0.0288 745  ILE B CG1 
14590 C CG2 . ILE B 747  ? 0.2055 0.1975 0.1857 0.0041  0.0003  -0.0267 745  ILE B CG2 
14591 C CD1 . ILE B 747  ? 0.2334 0.2179 0.2137 0.0058  0.0007  -0.0281 745  ILE B CD1 
14592 N N   . LEU B 748  ? 0.1777 0.1733 0.1572 0.0075  0.0038  -0.0263 746  LEU B N   
14593 C CA  . LEU B 748  ? 0.1778 0.1768 0.1576 0.0072  0.0037  -0.0251 746  LEU B CA  
14594 C C   . LEU B 748  ? 0.1770 0.1751 0.1525 0.0071  0.0040  -0.0258 746  LEU B C   
14595 O O   . LEU B 748  ? 0.1905 0.1904 0.1647 0.0060  0.0030  -0.0253 746  LEU B O   
14596 C CB  . LEU B 748  ? 0.1892 0.1909 0.1728 0.0086  0.0049  -0.0238 746  LEU B CB  
14597 C CG  . LEU B 748  ? 0.2243 0.2279 0.2119 0.0083  0.0042  -0.0228 746  LEU B CG  
14598 C CD1 . LEU B 748  ? 0.2484 0.2533 0.2395 0.0097  0.0054  -0.0220 746  LEU B CD1 
14599 C CD2 . LEU B 748  ? 0.2496 0.2559 0.2375 0.0072  0.0030  -0.0218 746  LEU B CD2 
14600 N N   . ARG B 749  ? 0.1781 0.1737 0.1513 0.0084  0.0054  -0.0270 747  ARG B N   
14601 C CA  . ARG B 749  ? 0.1921 0.1864 0.1605 0.0083  0.0057  -0.0279 747  ARG B CA  
14602 C C   . ARG B 749  ? 0.1847 0.1766 0.1493 0.0063  0.0038  -0.0290 747  ARG B C   
14603 O O   . ARG B 749  ? 0.2040 0.1967 0.1657 0.0052  0.0030  -0.0289 747  ARG B O   
14604 C CB  . ARG B 749  ? 0.1983 0.1904 0.1651 0.0102  0.0078  -0.0290 747  ARG B CB  
14605 C CG  . ARG B 749  ? 0.2074 0.2026 0.1774 0.0119  0.0098  -0.0278 747  ARG B CG  
14606 C CD  . ARG B 749  ? 0.2417 0.2351 0.2097 0.0138  0.0119  -0.0290 747  ARG B CD  
14607 N NE  . ARG B 749  ? 0.2409 0.2374 0.2114 0.0152  0.0139  -0.0277 747  ARG B NE  
14608 C CZ  . ARG B 749  ? 0.2934 0.2896 0.2625 0.0169  0.0161  -0.0284 747  ARG B CZ  
14609 N NH1 . ARG B 749  ? 0.3108 0.3033 0.2756 0.0176  0.0166  -0.0304 747  ARG B NH1 
14610 N NH2 . ARG B 749  ? 0.2990 0.2985 0.2710 0.0179  0.0179  -0.0270 747  ARG B NH2 
14611 N N   . GLU B 750  ? 0.1867 0.1757 0.1513 0.0056  0.0030  -0.0299 748  GLU B N   
14612 C CA  . GLU B 750  ? 0.2066 0.1931 0.1677 0.0034  0.0010  -0.0308 748  GLU B CA  
14613 C C   . GLU B 750  ? 0.1783 0.1687 0.1409 0.0014  -0.0007 -0.0295 748  GLU B C   
14614 O O   . GLU B 750  ? 0.2206 0.2106 0.1799 -0.0004 -0.0022 -0.0299 748  GLU B O   
14615 C CB  . GLU B 750  ? 0.2122 0.1951 0.1737 0.0030  0.0004  -0.0317 748  GLU B CB  
14616 C CG  . GLU B 750  ? 0.2377 0.2177 0.1956 0.0005  -0.0016 -0.0326 748  GLU B CG  
14617 C CD  . GLU B 750  ? 0.2738 0.2494 0.2313 0.0001  -0.0021 -0.0335 748  GLU B CD  
14618 O OE1 . GLU B 750  ? 0.2753 0.2498 0.2349 0.0022  -0.0007 -0.0335 748  GLU B OE1 
14619 O OE2 . GLU B 750  ? 0.3218 0.2953 0.2771 -0.0023 -0.0039 -0.0339 748  GLU B OE2 
14620 N N   . ALA B 751  ? 0.2060 0.2002 0.1734 0.0018  -0.0006 -0.0278 749  ALA B N   
14621 C CA  . ALA B 751  ? 0.2118 0.2100 0.1812 0.0004  -0.0020 -0.0264 749  ALA B CA  
14622 C C   . ALA B 751  ? 0.2035 0.2045 0.1719 0.0007  -0.0020 -0.0255 749  ALA B C   
14623 O O   . ALA B 751  ? 0.2278 0.2322 0.1976 -0.0003 -0.0033 -0.0243 749  ALA B O   
14624 C CB  . ALA B 751  ? 0.2073 0.2081 0.1819 0.0011  -0.0017 -0.0251 749  ALA B CB  
14625 N N   . GLY B 752  ? 0.1892 0.1891 0.1553 0.0021  -0.0005 -0.0260 750  GLY B N   
14626 C CA  . GLY B 752  ? 0.2144 0.2166 0.1788 0.0022  -0.0006 -0.0251 750  GLY B CA  
14627 C C   . GLY B 752  ? 0.2099 0.2138 0.1763 0.0041  0.0013  -0.0240 750  GLY B C   
14628 O O   . GLY B 752  ? 0.2373 0.2428 0.2020 0.0043  0.0014  -0.0231 750  GLY B O   
14629 N N   . ILE B 753  ? 0.1906 0.1944 0.1604 0.0055  0.0028  -0.0238 751  ILE B N   
14630 C CA  . ILE B 753  ? 0.2018 0.2072 0.1734 0.0071  0.0045  -0.0226 751  ILE B CA  
14631 C C   . ILE B 753  ? 0.2172 0.2206 0.1850 0.0081  0.0062  -0.0236 751  ILE B C   
14632 O O   . ILE B 753  ? 0.2191 0.2196 0.1856 0.0086  0.0069  -0.0252 751  ILE B O   
14633 C CB  . ILE B 753  ? 0.1757 0.1816 0.1521 0.0082  0.0055  -0.0222 751  ILE B CB  
14634 C CG1 . ILE B 753  ? 0.1999 0.2075 0.1796 0.0073  0.0039  -0.0214 751  ILE B CG1 
14635 C CG2 . ILE B 753  ? 0.2075 0.2151 0.1857 0.0095  0.0072  -0.0209 751  ILE B CG2 
14636 C CD1 . ILE B 753  ? 0.1976 0.2084 0.1786 0.0070  0.0032  -0.0197 751  ILE B CD1 
14637 N N   . PRO B 754  ? 0.2078 0.2126 0.1735 0.0083  0.0068  -0.0228 752  PRO B N   
14638 C CA  . PRO B 754  ? 0.2198 0.2228 0.1815 0.0092  0.0085  -0.0238 752  PRO B CA  
14639 C C   . PRO B 754  ? 0.2394 0.2421 0.2035 0.0110  0.0108  -0.0240 752  PRO B C   
14640 O O   . PRO B 754  ? 0.2199 0.2246 0.1889 0.0116  0.0113  -0.0228 752  PRO B O   
14641 C CB  . PRO B 754  ? 0.2422 0.2475 0.2023 0.0092  0.0087  -0.0222 752  PRO B CB  
14642 C CG  . PRO B 754  ? 0.3016 0.3092 0.2636 0.0079  0.0064  -0.0208 752  PRO B CG  
14643 C CD  . PRO B 754  ? 0.2302 0.2380 0.1969 0.0078  0.0058  -0.0209 752  PRO B CD  
14644 N N   . ALA B 755  ? 0.2797 0.2799 0.2404 0.0120  0.0123  -0.0256 753  ALA B N   
14645 C CA  . ALA B 755  ? 0.2602 0.2604 0.2233 0.0138  0.0146  -0.0259 753  ALA B CA  
14646 C C   . ALA B 755  ? 0.2315 0.2352 0.1975 0.0145  0.0162  -0.0238 753  ALA B C   
14647 O O   . ALA B 755  ? 0.2633 0.2685 0.2339 0.0155  0.0173  -0.0232 753  ALA B O   
14648 C CB  . ALA B 755  ? 0.3244 0.3216 0.2829 0.0150  0.0160  -0.0279 753  ALA B CB  
14649 N N   . SER B 756  ? 0.2266 0.2319 0.1904 0.0140  0.0161  -0.0227 754  SER B N   
14650 C CA  . SER B 756  ? 0.2328 0.2410 0.1991 0.0144  0.0176  -0.0206 754  SER B CA  
14651 C C   . SER B 756  ? 0.2124 0.2227 0.1839 0.0138  0.0164  -0.0189 754  SER B C   
14652 O O   . SER B 756  ? 0.2287 0.2411 0.2035 0.0142  0.0176  -0.0173 754  SER B O   
14653 C CB  . SER B 756  ? 0.2631 0.2721 0.2251 0.0139  0.0178  -0.0197 754  SER B CB  
14654 O OG  . SER B 756  ? 0.3047 0.3135 0.2652 0.0125  0.0152  -0.0194 754  SER B OG  
14655 N N   . ALA B 757  ? 0.1873 0.1970 0.1596 0.0128  0.0141  -0.0191 755  ALA B N   
14656 C CA  . ALA B 757  ? 0.1727 0.1840 0.1496 0.0124  0.0130  -0.0178 755  ALA B CA  
14657 C C   . ALA B 757  ? 0.1885 0.1994 0.1695 0.0129  0.0132  -0.0184 755  ALA B C   
14658 O O   . ALA B 757  ? 0.1978 0.2100 0.1827 0.0127  0.0126  -0.0173 755  ALA B O   
14659 C CB  . ALA B 757  ? 0.2003 0.2118 0.1763 0.0111  0.0106  -0.0176 755  ALA B CB  
14660 N N   . LEU B 758  ? 0.1891 0.1980 0.1690 0.0135  0.0138  -0.0201 756  LEU B N   
14661 C CA  . LEU B 758  ? 0.1827 0.1911 0.1664 0.0140  0.0137  -0.0206 756  LEU B CA  
14662 C C   . LEU B 758  ? 0.1875 0.1947 0.1705 0.0154  0.0155  -0.0218 756  LEU B C   
14663 O O   . LEU B 758  ? 0.2178 0.2223 0.1973 0.0157  0.0154  -0.0235 756  LEU B O   
14664 C CB  . LEU B 758  ? 0.1889 0.1958 0.1724 0.0130  0.0117  -0.0214 756  LEU B CB  
14665 C CG  . LEU B 758  ? 0.1827 0.1887 0.1695 0.0135  0.0115  -0.0219 756  LEU B CG  
14666 C CD1 . LEU B 758  ? 0.2011 0.2095 0.1927 0.0138  0.0118  -0.0204 756  LEU B CD1 
14667 C CD2 . LEU B 758  ? 0.2107 0.2151 0.1969 0.0122  0.0095  -0.0226 756  LEU B CD2 
14668 N N   . GLN B 759  ? 0.1746 0.1838 0.1610 0.0164  0.0171  -0.0209 757  GLN B N   
14669 C CA  . GLN B 759  ? 0.1816 0.1904 0.1683 0.0181  0.0191  -0.0218 757  GLN B CA  
14670 C C   . GLN B 759  ? 0.1797 0.1890 0.1713 0.0186  0.0188  -0.0217 757  GLN B C   
14671 O O   . GLN B 759  ? 0.1936 0.2048 0.1889 0.0179  0.0180  -0.0203 757  GLN B O   
14672 C CB  . GLN B 759  ? 0.1799 0.1913 0.1667 0.0187  0.0213  -0.0207 757  GLN B CB  
14673 C CG  . GLN B 759  ? 0.2013 0.2120 0.1826 0.0183  0.0217  -0.0209 757  GLN B CG  
14674 C CD  . GLN B 759  ? 0.1873 0.2006 0.1687 0.0187  0.0239  -0.0195 757  GLN B CD  
14675 O OE1 . GLN B 759  ? 0.2286 0.2420 0.2083 0.0201  0.0260  -0.0202 757  GLN B OE1 
14676 N NE2 . GLN B 759  ? 0.2017 0.2171 0.1850 0.0177  0.0234  -0.0175 757  GLN B NE2 
14677 N N   . LEU B 760  ? 0.1831 0.1907 0.1745 0.0200  0.0193  -0.0231 758  LEU B N   
14678 C CA  . LEU B 760  ? 0.1685 0.1764 0.1641 0.0207  0.0190  -0.0230 758  LEU B CA  
14679 C C   . LEU B 760  ? 0.1887 0.1989 0.1869 0.0224  0.0212  -0.0227 758  LEU B C   
14680 O O   . LEU B 760  ? 0.1962 0.2055 0.1918 0.0238  0.0229  -0.0238 758  LEU B O   
14681 C CB  . LEU B 760  ? 0.1968 0.2008 0.1904 0.0210  0.0179  -0.0248 758  LEU B CB  
14682 C CG  . LEU B 760  ? 0.1769 0.1810 0.1746 0.0218  0.0173  -0.0247 758  LEU B CG  
14683 C CD1 . LEU B 760  ? 0.2162 0.2210 0.2163 0.0201  0.0153  -0.0236 758  LEU B CD1 
14684 C CD2 . LEU B 760  ? 0.2238 0.2238 0.2191 0.0229  0.0170  -0.0264 758  LEU B CD2 
14685 N N   . LEU B 761  ? 0.1910 0.2042 0.1944 0.0224  0.0213  -0.0213 759  LEU B N   
14686 C CA  . LEU B 761  ? 0.1827 0.1989 0.1895 0.0238  0.0233  -0.0207 759  LEU B CA  
14687 C C   . LEU B 761  ? 0.1696 0.1862 0.1807 0.0245  0.0224  -0.0206 759  LEU B C   
14688 O O   . LEU B 761  ? 0.1855 0.2044 0.2008 0.0236  0.0216  -0.0193 759  LEU B O   
14689 C CB  . LEU B 761  ? 0.1943 0.2142 0.2033 0.0229  0.0242  -0.0187 759  LEU B CB  
14690 C CG  . LEU B 761  ? 0.2015 0.2215 0.2066 0.0222  0.0252  -0.0183 759  LEU B CG  
14691 C CD1 . LEU B 761  ? 0.2285 0.2468 0.2289 0.0236  0.0268  -0.0199 759  LEU B CD1 
14692 C CD2 . LEU B 761  ? 0.2438 0.2622 0.2469 0.0204  0.0231  -0.0180 759  LEU B CD2 
14693 N N   . PRO B 762  ? 0.1715 0.1858 0.1818 0.0260  0.0223  -0.0221 760  PRO B N   
14694 C CA  . PRO B 762  ? 0.1758 0.1905 0.1902 0.0268  0.0215  -0.0219 760  PRO B CA  
14695 C C   . PRO B 762  ? 0.1798 0.1992 0.1992 0.0279  0.0231  -0.0207 760  PRO B C   
14696 O O   . PRO B 762  ? 0.1837 0.2053 0.2027 0.0287  0.0253  -0.0205 760  PRO B O   
14697 C CB  . PRO B 762  ? 0.1808 0.1917 0.1924 0.0286  0.0215  -0.0237 760  PRO B CB  
14698 C CG  . PRO B 762  ? 0.1854 0.1930 0.1910 0.0280  0.0216  -0.0250 760  PRO B CG  
14699 C CD  . PRO B 762  ? 0.1727 0.1833 0.1779 0.0272  0.0230  -0.0240 760  PRO B CD  
14700 N N   . GLY B 763  ? 0.1699 0.1909 0.1938 0.0277  0.0219  -0.0198 761  GLY B N   
14701 C CA  . GLY B 763  ? 0.1764 0.2019 0.2055 0.0287  0.0230  -0.0187 761  GLY B CA  
14702 C C   . GLY B 763  ? 0.1593 0.1868 0.1926 0.0270  0.0212  -0.0173 761  GLY B C   
14703 O O   . GLY B 763  ? 0.1828 0.2079 0.2150 0.0255  0.0191  -0.0174 761  GLY B O   
14704 N N   . ASP B 764  ? 0.1943 0.2264 0.2326 0.0273  0.0221  -0.0160 762  ASP B N   
14705 C CA  . ASP B 764  ? 0.2020 0.2359 0.2445 0.0259  0.0203  -0.0147 762  ASP B CA  
14706 C C   . ASP B 764  ? 0.2221 0.2576 0.2652 0.0236  0.0203  -0.0133 762  ASP B C   
14707 O O   . ASP B 764  ? 0.1924 0.2267 0.2320 0.0229  0.0212  -0.0134 762  ASP B O   
14708 C CB  . ASP B 764  ? 0.2373 0.2749 0.2851 0.0274  0.0206  -0.0141 762  ASP B CB  
14709 C CG  . ASP B 764  ? 0.2886 0.3312 0.3394 0.0281  0.0232  -0.0131 762  ASP B CG  
14710 O OD1 . ASP B 764  ? 0.2344 0.2780 0.2839 0.0269  0.0245  -0.0125 762  ASP B OD1 
14711 O OD2 . ASP B 764  ? 0.3805 0.4265 0.4355 0.0298  0.0239  -0.0128 762  ASP B OD2 
14712 N N   . GLY B 765  ? 0.2015 0.2395 0.2490 0.0222  0.0192  -0.0120 763  GLY B N   
14713 C CA  . GLY B 765  ? 0.1932 0.2320 0.2412 0.0199  0.0189  -0.0107 763  GLY B CA  
14714 C C   . GLY B 765  ? 0.1905 0.2322 0.2388 0.0198  0.0214  -0.0097 763  GLY B C   
14715 O O   . GLY B 765  ? 0.2092 0.2504 0.2562 0.0181  0.0214  -0.0088 763  GLY B O   
14716 N N   . ARG B 766  ? 0.2003 0.2451 0.2503 0.0216  0.0235  -0.0097 764  ARG B N   
14717 C CA  . ARG B 766  ? 0.2191 0.2667 0.2689 0.0215  0.0261  -0.0087 764  ARG B CA  
14718 C C   . ARG B 766  ? 0.1858 0.2302 0.2296 0.0215  0.0270  -0.0095 764  ARG B C   
14719 O O   . ARG B 766  ? 0.2037 0.2491 0.2463 0.0204  0.0282  -0.0084 764  ARG B O   
14720 C CB  . ARG B 766  ? 0.2302 0.2818 0.2829 0.0237  0.0284  -0.0087 764  ARG B CB  
14721 C CG  . ARG B 766  ? 0.2565 0.3123 0.3157 0.0237  0.0277  -0.0077 764  ARG B CG  
14722 C CD  . ARG B 766  ? 0.3762 0.4353 0.4378 0.0267  0.0298  -0.0081 764  ARG B CD  
14723 N NE  . ARG B 766  ? 0.4330 0.4880 0.4910 0.0290  0.0295  -0.0102 764  ARG B NE  
14724 C CZ  . ARG B 766  ? 0.5175 0.5736 0.5759 0.0320  0.0311  -0.0111 764  ARG B CZ  
14725 N NH1 . ARG B 766  ? 0.4792 0.5410 0.5418 0.0332  0.0335  -0.0101 764  ARG B NH1 
14726 N NH2 . ARG B 766  ? 0.4843 0.5358 0.5389 0.0338  0.0305  -0.0131 764  ARG B NH2 
14727 N N   . VAL B 767  ? 0.1754 0.2157 0.2152 0.0227  0.0262  -0.0114 765  VAL B N   
14728 C CA  . VAL B 767  ? 0.1917 0.2288 0.2257 0.0226  0.0266  -0.0122 765  VAL B CA  
14729 C C   . VAL B 767  ? 0.1771 0.2124 0.2098 0.0203  0.0248  -0.0115 765  VAL B C   
14730 O O   . VAL B 767  ? 0.1903 0.2252 0.2203 0.0194  0.0255  -0.0108 765  VAL B O   
14731 C CB  . VAL B 767  ? 0.1861 0.2195 0.2165 0.0242  0.0261  -0.0144 765  VAL B CB  
14732 C CG1 . VAL B 767  ? 0.1845 0.2147 0.2090 0.0238  0.0262  -0.0153 765  VAL B CG1 
14733 C CG2 . VAL B 767  ? 0.1965 0.2314 0.2281 0.0267  0.0279  -0.0152 765  VAL B CG2 
14734 N N   . GLY B 768  ? 0.1769 0.2110 0.2116 0.0194  0.0224  -0.0114 766  GLY B N   
14735 C CA  . GLY B 768  ? 0.1797 0.2122 0.2135 0.0174  0.0209  -0.0107 766  GLY B CA  
14736 C C   . GLY B 768  ? 0.1718 0.2069 0.2076 0.0160  0.0218  -0.0087 766  GLY B C   
14737 O O   . GLY B 768  ? 0.1797 0.2135 0.2129 0.0150  0.0217  -0.0080 766  GLY B O   
14738 N N   . ALA B 769  ? 0.1858 0.2245 0.2261 0.0160  0.0226  -0.0077 767  ALA B N   
14739 C CA  . ALA B 769  ? 0.1818 0.2229 0.2243 0.0143  0.0234  -0.0056 767  ALA B CA  
14740 C C   . ALA B 769  ? 0.1882 0.2302 0.2278 0.0146  0.0258  -0.0051 767  ALA B C   
14741 O O   . ALA B 769  ? 0.1972 0.2389 0.2357 0.0131  0.0259  -0.0036 767  ALA B O   
14742 C CB  . ALA B 769  ? 0.1941 0.2394 0.2424 0.0141  0.0238  -0.0046 767  ALA B CB  
14743 N N   . ALA B 770  ? 0.1844 0.2271 0.2221 0.0165  0.0276  -0.0062 768  ALA B N   
14744 C CA  . ALA B 770  ? 0.1869 0.2302 0.2213 0.0169  0.0299  -0.0058 768  ALA B CA  
14745 C C   . ALA B 770  ? 0.1915 0.2310 0.2206 0.0162  0.0289  -0.0061 768  ALA B C   
14746 O O   . ALA B 770  ? 0.2166 0.2564 0.2435 0.0153  0.0299  -0.0049 768  ALA B O   
14747 C CB  . ALA B 770  ? 0.2102 0.2545 0.2432 0.0193  0.0319  -0.0072 768  ALA B CB  
14748 N N   . LEU B 771  ? 0.1825 0.2185 0.2095 0.0165  0.0268  -0.0077 769  LEU B N   
14749 C CA  . LEU B 771  ? 0.1816 0.2145 0.2042 0.0158  0.0257  -0.0079 769  LEU B CA  
14750 C C   . LEU B 771  ? 0.1777 0.2103 0.2015 0.0139  0.0245  -0.0061 769  LEU B C   
14751 O O   . LEU B 771  ? 0.2048 0.2365 0.2257 0.0132  0.0247  -0.0052 769  LEU B O   
14752 C CB  . LEU B 771  ? 0.1650 0.1948 0.1859 0.0163  0.0237  -0.0098 769  LEU B CB  
14753 C CG  . LEU B 771  ? 0.1650 0.1938 0.1834 0.0181  0.0247  -0.0117 769  LEU B CG  
14754 C CD1 . LEU B 771  ? 0.1959 0.2218 0.2134 0.0184  0.0226  -0.0132 769  LEU B CD1 
14755 C CD2 . LEU B 771  ? 0.2014 0.2294 0.2146 0.0184  0.0260  -0.0120 769  LEU B CD2 
14756 N N   . VAL B 772  ? 0.1816 0.2147 0.2095 0.0131  0.0232  -0.0056 770  VAL B N   
14757 C CA  . VAL B 772  ? 0.1807 0.2129 0.2097 0.0114  0.0219  -0.0041 770  VAL B CA  
14758 C C   . VAL B 772  ? 0.2139 0.2480 0.2433 0.0103  0.0235  -0.0020 770  VAL B C   
14759 O O   . VAL B 772  ? 0.2401 0.2725 0.2677 0.0093  0.0230  -0.0008 770  VAL B O   
14760 C CB  . VAL B 772  ? 0.1881 0.2206 0.2214 0.0107  0.0203  -0.0041 770  VAL B CB  
14761 C CG1 . VAL B 772  ? 0.2186 0.2503 0.2534 0.0088  0.0193  -0.0025 770  VAL B CG1 
14762 C CG2 . VAL B 772  ? 0.1892 0.2192 0.2215 0.0114  0.0184  -0.0059 770  VAL B CG2 
14763 N N   . ALA B 773  ? 0.2099 0.2475 0.2415 0.0107  0.0256  -0.0015 771  ALA B N   
14764 C CA  . ALA B 773  ? 0.2127 0.2525 0.2452 0.0095  0.0273  0.0007  771  ALA B CA  
14765 C C   . ALA B 773  ? 0.2562 0.2957 0.2839 0.0100  0.0290  0.0010  771  ALA B C   
14766 O O   . ALA B 773  ? 0.2679 0.3087 0.2953 0.0089  0.0303  0.0030  771  ALA B O   
14767 C CB  . ALA B 773  ? 0.2478 0.2922 0.2850 0.0097  0.0290  0.0013  771  ALA B CB  
14768 N N   . ALA B 774  ? 0.2259 0.2636 0.2496 0.0115  0.0289  -0.0008 772  ALA B N   
14769 C CA  . ALA B 774  ? 0.2244 0.2619 0.2432 0.0121  0.0305  -0.0008 772  ALA B CA  
14770 C C   . ALA B 774  ? 0.2625 0.2982 0.2787 0.0107  0.0297  0.0009  772  ALA B C   
14771 O O   . ALA B 774  ? 0.2660 0.2992 0.2824 0.0099  0.0275  0.0011  772  ALA B O   
14772 C CB  . ALA B 774  ? 0.2460 0.2813 0.2609 0.0137  0.0301  -0.0032 772  ALA B CB  
14773 N N   . ALA B 775  ? 0.2784 0.3152 0.2918 0.0105  0.0317  0.0022  773  ALA B N   
14774 C CA  . ALA B 775  ? 0.3116 0.3470 0.3230 0.0091  0.0312  0.0043  773  ALA B CA  
14775 C C   . ALA B 775  ? 0.2769 0.3087 0.2847 0.0093  0.0288  0.0036  773  ALA B C   
14776 O O   . ALA B 775  ? 0.2917 0.3216 0.2996 0.0082  0.0273  0.0050  773  ALA B O   
14777 C CB  . ALA B 775  ? 0.3229 0.3601 0.3311 0.0091  0.0338  0.0056  773  ALA B CB  
14778 N N   . GLU B 776  ? 0.2471 0.2778 0.2517 0.0106  0.0284  0.0015  774  GLU B N   
14779 C CA  . GLU B 776  ? 0.2320 0.2600 0.2331 0.0107  0.0264  0.0009  774  GLU B CA  
14780 C C   . GLU B 776  ? 0.2135 0.2397 0.2167 0.0109  0.0240  -0.0004 774  GLU B C   
14781 O O   . GLU B 776  ? 0.2237 0.2480 0.2245 0.0110  0.0223  -0.0009 774  GLU B O   
14782 C CB  . GLU B 776  ? 0.2338 0.2614 0.2298 0.0117  0.0271  -0.0006 774  GLU B CB  
14783 C CG  . GLU B 776  ? 0.3275 0.3566 0.3204 0.0117  0.0296  0.0006  774  GLU B CG  
14784 C CD  . GLU B 776  ? 0.4032 0.4351 0.3980 0.0125  0.0323  0.0000  774  GLU B CD  
14785 O OE1 . GLU B 776  ? 0.3132 0.3457 0.3118 0.0131  0.0321  -0.0013 774  GLU B OE1 
14786 O OE2 . GLU B 776  ? 0.4403 0.4738 0.4327 0.0126  0.0346  0.0009  774  GLU B OE2 
14787 N N   . THR B 777  ? 0.1964 0.2234 0.2040 0.0108  0.0239  -0.0009 775  THR B N   
14788 C CA  . THR B 777  ? 0.1947 0.2200 0.2041 0.0109  0.0217  -0.0021 775  THR B CA  
14789 C C   . THR B 777  ? 0.2095 0.2331 0.2193 0.0100  0.0201  -0.0007 775  THR B C   
14790 O O   . THR B 777  ? 0.2204 0.2443 0.2320 0.0090  0.0204  0.0011  775  THR B O   
14791 C CB  . THR B 777  ? 0.1937 0.2205 0.2078 0.0110  0.0220  -0.0026 775  THR B CB  
14792 O OG1 . THR B 777  ? 0.2232 0.2512 0.2366 0.0122  0.0234  -0.0042 775  THR B OG1 
14793 C CG2 . THR B 777  ? 0.2020 0.2270 0.2180 0.0108  0.0198  -0.0036 775  THR B CG2 
14794 N N   . ALA B 778  ? 0.1760 0.1978 0.1839 0.0104  0.0183  -0.0015 776  ALA B N   
14795 C CA  . ALA B 778  ? 0.1891 0.2091 0.1966 0.0100  0.0167  -0.0004 776  ALA B CA  
14796 C C   . ALA B 778  ? 0.1811 0.1998 0.1912 0.0100  0.0150  -0.0012 776  ALA B C   
14797 O O   . ALA B 778  ? 0.2034 0.2205 0.2137 0.0098  0.0137  -0.0004 776  ALA B O   
14798 C CB  . ALA B 778  ? 0.1966 0.2159 0.1999 0.0104  0.0160  -0.0004 776  ALA B CB  
14799 N N   . GLY B 779  ? 0.1699 0.1891 0.1818 0.0103  0.0149  -0.0029 777  GLY B N   
14800 C CA  . GLY B 779  ? 0.1753 0.1934 0.1895 0.0103  0.0133  -0.0037 777  GLY B CA  
14801 C C   . GLY B 779  ? 0.1780 0.1970 0.1939 0.0107  0.0136  -0.0053 777  GLY B C   
14802 O O   . GLY B 779  ? 0.1705 0.1906 0.1852 0.0112  0.0147  -0.0061 777  GLY B O   
14803 N N   . VAL B 780  ? 0.1702 0.1887 0.1890 0.0104  0.0126  -0.0057 778  VAL B N   
14804 C CA  . VAL B 780  ? 0.1612 0.1804 0.1818 0.0108  0.0126  -0.0070 778  VAL B CA  
14805 C C   . VAL B 780  ? 0.1635 0.1812 0.1844 0.0109  0.0108  -0.0081 778  VAL B C   
14806 O O   . VAL B 780  ? 0.1735 0.1900 0.1952 0.0104  0.0098  -0.0076 778  VAL B O   
14807 C CB  . VAL B 780  ? 0.1679 0.1887 0.1921 0.0102  0.0133  -0.0063 778  VAL B CB  
14808 C CG1 . VAL B 780  ? 0.1727 0.1942 0.1989 0.0107  0.0131  -0.0076 778  VAL B CG1 
14809 C CG2 . VAL B 780  ? 0.1850 0.2077 0.2090 0.0101  0.0153  -0.0052 778  VAL B CG2 
14810 N N   . MET B 781  ? 0.1522 0.1698 0.1723 0.0115  0.0106  -0.0096 779  MET B N   
14811 C CA  . MET B 781  ? 0.1490 0.1654 0.1694 0.0115  0.0091  -0.0106 779  MET B CA  
14812 C C   . MET B 781  ? 0.1503 0.1673 0.1729 0.0117  0.0092  -0.0113 779  MET B C   
14813 O O   . MET B 781  ? 0.1634 0.1811 0.1855 0.0124  0.0100  -0.0120 779  MET B O   
14814 C CB  . MET B 781  ? 0.1488 0.1646 0.1663 0.0119  0.0086  -0.0116 779  MET B CB  
14815 C CG  . MET B 781  ? 0.1710 0.1866 0.1864 0.0118  0.0084  -0.0108 779  MET B CG  
14816 S SD  . MET B 781  ? 0.1760 0.1915 0.1882 0.0120  0.0078  -0.0117 779  MET B SD  
14817 C CE  . MET B 781  ? 0.1762 0.1911 0.1895 0.0120  0.0062  -0.0124 779  MET B CE  
14818 N N   . PHE B 782  ? 0.1529 0.1697 0.1780 0.0113  0.0083  -0.0111 780  PHE B N   
14819 C CA  . PHE B 782  ? 0.1560 0.1736 0.1837 0.0114  0.0082  -0.0115 780  PHE B CA  
14820 C C   . PHE B 782  ? 0.1540 0.1703 0.1819 0.0113  0.0066  -0.0124 780  PHE B C   
14821 O O   . PHE B 782  ? 0.1628 0.1779 0.1905 0.0108  0.0056  -0.0122 780  PHE B O   
14822 C CB  . PHE B 782  ? 0.1606 0.1797 0.1916 0.0107  0.0085  -0.0104 780  PHE B CB  
14823 C CG  . PHE B 782  ? 0.1516 0.1718 0.1855 0.0108  0.0080  -0.0107 780  PHE B CG  
14824 C CD1 . PHE B 782  ? 0.1509 0.1729 0.1858 0.0117  0.0092  -0.0109 780  PHE B CD1 
14825 C CD2 . PHE B 782  ? 0.1626 0.1819 0.1980 0.0100  0.0064  -0.0107 780  PHE B CD2 
14826 C CE1 . PHE B 782  ? 0.1573 0.1805 0.1950 0.0120  0.0087  -0.0111 780  PHE B CE1 
14827 C CE2 . PHE B 782  ? 0.1719 0.1925 0.2101 0.0101  0.0058  -0.0109 780  PHE B CE2 
14828 C CZ  . PHE B 782  ? 0.1635 0.1861 0.2030 0.0111  0.0070  -0.0110 780  PHE B CZ  
14829 N N   . THR B 783  ? 0.1493 0.1655 0.1773 0.0119  0.0063  -0.0133 781  THR B N   
14830 C CA  . THR B 783  ? 0.1647 0.1799 0.1932 0.0117  0.0048  -0.0139 781  THR B CA  
14831 C C   . THR B 783  ? 0.1674 0.1837 0.1984 0.0121  0.0048  -0.0140 781  THR B C   
14832 O O   . THR B 783  ? 0.1688 0.1858 0.1997 0.0130  0.0058  -0.0143 781  THR B O   
14833 C CB  . THR B 783  ? 0.1682 0.1818 0.1938 0.0119  0.0043  -0.0149 781  THR B CB  
14834 O OG1 . THR B 783  ? 0.1679 0.1811 0.1916 0.0117  0.0043  -0.0147 781  THR B OG1 
14835 C CG2 . THR B 783  ? 0.1744 0.1870 0.2004 0.0117  0.0028  -0.0154 781  THR B CG2 
14836 N N   . GLY B 784  ? 0.1570 0.1735 0.1903 0.0116  0.0037  -0.0137 782  GLY B N   
14837 C CA  . GLY B 784  ? 0.1580 0.1761 0.1942 0.0119  0.0036  -0.0135 782  GLY B CA  
14838 C C   . GLY B 784  ? 0.1665 0.1850 0.2051 0.0108  0.0023  -0.0129 782  GLY B C   
14839 O O   . GLY B 784  ? 0.1771 0.1939 0.2145 0.0100  0.0013  -0.0130 782  GLY B O   
14840 N N   . SER B 785  ? 0.1734 0.1943 0.2155 0.0108  0.0024  -0.0123 783  SER B N   
14841 C CA  . SER B 785  ? 0.1871 0.2084 0.2316 0.0096  0.0009  -0.0118 783  SER B CA  
14842 C C   . SER B 785  ? 0.2075 0.2289 0.2527 0.0083  0.0012  -0.0109 783  SER B C   
14843 O O   . SER B 785  ? 0.1885 0.2109 0.2337 0.0083  0.0028  -0.0102 783  SER B O   
14844 C CB  . SER B 785  ? 0.2020 0.2263 0.2504 0.0100  0.0007  -0.0113 783  SER B CB  
14845 O OG  . SER B 785  ? 0.1966 0.2238 0.2472 0.0103  0.0025  -0.0104 783  SER B OG  
14846 N N   . THR B 786  ? 0.2026 0.2226 0.2481 0.0070  -0.0005 -0.0108 784  THR B N   
14847 C CA  . THR B 786  ? 0.2148 0.2342 0.2608 0.0056  -0.0005 -0.0100 784  THR B CA  
14848 C C   . THR B 786  ? 0.1963 0.2191 0.2461 0.0049  0.0006  -0.0086 784  THR B C   
14849 O O   . THR B 786  ? 0.2266 0.2496 0.2764 0.0043  0.0017  -0.0076 784  THR B O   
14850 C CB  . THR B 786  ? 0.2190 0.2361 0.2647 0.0044  -0.0026 -0.0103 784  THR B CB  
14851 O OG1 . THR B 786  ? 0.2400 0.2544 0.2822 0.0052  -0.0033 -0.0116 784  THR B OG1 
14852 C CG2 . THR B 786  ? 0.2802 0.2956 0.3257 0.0030  -0.0027 -0.0096 784  THR B CG2 
14853 N N   . GLU B 787  ? 0.2309 0.2566 0.2839 0.0052  0.0003  -0.0084 785  GLU B N   
14854 C CA  . GLU B 787  ? 0.2184 0.2481 0.2755 0.0046  0.0013  -0.0070 785  GLU B CA  
14855 C C   . GLU B 787  ? 0.2165 0.2477 0.2730 0.0056  0.0039  -0.0066 785  GLU B C   
14856 O O   . GLU B 787  ? 0.2116 0.2445 0.2696 0.0046  0.0050  -0.0053 785  GLU B O   
14857 C CB  . GLU B 787  ? 0.2468 0.2796 0.3073 0.0053  0.0007  -0.0070 785  GLU B CB  
14858 N N   . VAL B 788  ? 0.1943 0.2246 0.2481 0.0074  0.0047  -0.0076 786  VAL B N   
14859 C CA  . VAL B 788  ? 0.2015 0.2329 0.2541 0.0084  0.0071  -0.0074 786  VAL B CA  
14860 C C   . VAL B 788  ? 0.1739 0.2031 0.2236 0.0076  0.0075  -0.0070 786  VAL B C   
14861 O O   . VAL B 788  ? 0.1858 0.2164 0.2356 0.0073  0.0092  -0.0060 786  VAL B O   
14862 C CB  . VAL B 788  ? 0.1979 0.2286 0.2483 0.0105  0.0076  -0.0087 786  VAL B CB  
14863 C CG1 . VAL B 788  ? 0.1867 0.2176 0.2347 0.0113  0.0098  -0.0088 786  VAL B CG1 
14864 C CG2 . VAL B 788  ? 0.2101 0.2436 0.2639 0.0116  0.0076  -0.0088 786  VAL B CG2 
14865 N N   . ALA B 789  ? 0.1767 0.2024 0.2238 0.0072  0.0060  -0.0077 787  ALA B N   
14866 C CA  . ALA B 789  ? 0.1718 0.1952 0.2161 0.0067  0.0063  -0.0073 787  ALA B CA  
14867 C C   . ALA B 789  ? 0.1665 0.1907 0.2129 0.0050  0.0066  -0.0057 787  ALA B C   
14868 O O   . ALA B 789  ? 0.1811 0.2049 0.2260 0.0048  0.0077  -0.0048 787  ALA B O   
14869 C CB  . ALA B 789  ? 0.1716 0.1915 0.2134 0.0066  0.0046  -0.0083 787  ALA B CB  
14870 N N   . ARG B 790  ? 0.1836 0.2088 0.2333 0.0037  0.0055  -0.0052 788  ARG B N   
14871 C CA  . ARG B 790  ? 0.2099 0.2358 0.2617 0.0018  0.0056  -0.0036 788  ARG B CA  
14872 C C   . ARG B 790  ? 0.1967 0.2262 0.2502 0.0019  0.0079  -0.0023 788  ARG B C   
14873 O O   . ARG B 790  ? 0.2231 0.2525 0.2765 0.0007  0.0087  -0.0008 788  ARG B O   
14874 C CB  . ARG B 790  ? 0.2432 0.2700 0.2985 0.0003  0.0039  -0.0033 788  ARG B CB  
14875 C CG  . ARG B 790  ? 0.2695 0.2926 0.3231 -0.0002 0.0016  -0.0043 788  ARG B CG  
14876 C CD  . ARG B 790  ? 0.3329 0.3570 0.3900 -0.0021 -0.0001 -0.0038 788  ARG B CD  
14877 N NE  . ARG B 790  ? 0.4594 0.4800 0.5145 -0.0024 -0.0023 -0.0051 788  ARG B NE  
14878 C CZ  . ARG B 790  ? 0.4429 0.4591 0.4952 -0.0031 -0.0033 -0.0054 788  ARG B CZ  
14879 N NH1 . ARG B 790  ? 0.3892 0.4039 0.4405 -0.0038 -0.0024 -0.0044 788  ARG B NH1 
14880 N NH2 . ARG B 790  ? 0.5036 0.5169 0.5540 -0.0031 -0.0051 -0.0067 788  ARG B NH2 
14881 N N   . LEU B 791  ? 0.1968 0.2296 0.2518 0.0033  0.0090  -0.0027 789  LEU B N   
14882 C CA  . LEU B 791  ? 0.1911 0.2275 0.2476 0.0036  0.0114  -0.0016 789  LEU B CA  
14883 C C   . LEU B 791  ? 0.2168 0.2516 0.2692 0.0043  0.0129  -0.0015 789  LEU B C   
14884 O O   . LEU B 791  ? 0.2297 0.2659 0.2823 0.0036  0.0145  -0.0001 789  LEU B O   
14885 C CB  . LEU B 791  ? 0.2185 0.2582 0.2770 0.0054  0.0123  -0.0023 789  LEU B CB  
14886 C CG  . LEU B 791  ? 0.2321 0.2742 0.2951 0.0049  0.0108  -0.0022 789  LEU B CG  
14887 C CD1 . LEU B 791  ? 0.2430 0.2879 0.3074 0.0072  0.0118  -0.0030 789  LEU B CD1 
14888 C CD2 . LEU B 791  ? 0.2685 0.3136 0.3357 0.0027  0.0109  -0.0003 789  LEU B CD2 
14889 N N   . ILE B 792  ? 0.2127 0.2446 0.2614 0.0056  0.0123  -0.0030 790  ILE B N   
14890 C CA  . ILE B 792  ? 0.2007 0.2310 0.2453 0.0063  0.0134  -0.0030 790  ILE B CA  
14891 C C   . ILE B 792  ? 0.1919 0.2199 0.2353 0.0048  0.0130  -0.0018 790  ILE B C   
14892 O O   . ILE B 792  ? 0.2090 0.2373 0.2508 0.0046  0.0144  -0.0006 790  ILE B O   
14893 C CB  . ILE B 792  ? 0.1805 0.2083 0.2218 0.0077  0.0126  -0.0049 790  ILE B CB  
14894 C CG1 . ILE B 792  ? 0.1724 0.2021 0.2144 0.0093  0.0134  -0.0060 790  ILE B CG1 
14895 C CG2 . ILE B 792  ? 0.1835 0.2093 0.2206 0.0080  0.0131  -0.0048 790  ILE B CG2 
14896 C CD1 . ILE B 792  ? 0.1882 0.2155 0.2275 0.0104  0.0124  -0.0077 790  ILE B CD1 
14897 N N   . GLN B 793  ? 0.1980 0.2235 0.2418 0.0038  0.0110  -0.0019 791  GLN B N   
14898 C CA  . GLN B 793  ? 0.2021 0.2248 0.2447 0.0025  0.0103  -0.0008 791  GLN B CA  
14899 C C   . GLN B 793  ? 0.1938 0.2185 0.2387 0.0009  0.0115  0.0013  791  GLN B C   
14900 O O   . GLN B 793  ? 0.2173 0.2407 0.2603 0.0003  0.0121  0.0026  791  GLN B O   
14901 C CB  . GLN B 793  ? 0.2076 0.2275 0.2508 0.0018  0.0080  -0.0015 791  GLN B CB  
14902 C CG  . GLN B 793  ? 0.2284 0.2449 0.2704 0.0005  0.0072  -0.0005 791  GLN B CG  
14903 C CD  . GLN B 793  ? 0.2661 0.2805 0.3094 -0.0006 0.0051  -0.0010 791  GLN B CD  
14904 O OE1 . GLN B 793  ? 0.2871 0.3037 0.3337 -0.0015 0.0046  -0.0011 791  GLN B OE1 
14905 N NE2 . GLN B 793  ? 0.3255 0.3357 0.3664 -0.0006 0.0039  -0.0014 791  GLN B NE2 
14906 N N   . ALA B 794  ? 0.2108 0.2389 0.2598 0.0001  0.0118  0.0018  792  ALA B N   
14907 C CA  . ALA B 794  ? 0.2180 0.2488 0.2696 -0.0016 0.0130  0.0039  792  ALA B CA  
14908 C C   . ALA B 794  ? 0.2261 0.2591 0.2762 -0.0008 0.0156  0.0047  792  ALA B C   
14909 O O   . ALA B 794  ? 0.2531 0.2860 0.3026 -0.0021 0.0165  0.0065  792  ALA B O   
14910 C CB  . ALA B 794  ? 0.2588 0.2934 0.3155 -0.0025 0.0127  0.0041  792  ALA B CB  
14911 N N   . GLN B 795  ? 0.2233 0.2580 0.2723 0.0013  0.0167  0.0034  793  GLN B N   
14912 C CA  . GLN B 795  ? 0.2381 0.2744 0.2848 0.0023  0.0191  0.0039  793  GLN B CA  
14913 C C   . GLN B 795  ? 0.2357 0.2685 0.2780 0.0021  0.0190  0.0045  793  GLN B C   
14914 O O   . GLN B 795  ? 0.2488 0.2825 0.2899 0.0015  0.0206  0.0061  793  GLN B O   
14915 C CB  . GLN B 795  ? 0.2629 0.3003 0.3082 0.0046  0.0199  0.0019  793  GLN B CB  
14916 C CG  . GLN B 795  ? 0.2977 0.3390 0.3469 0.0055  0.0207  0.0014  793  GLN B CG  
14917 C CD  . GLN B 795  ? 0.3237 0.3648 0.3705 0.0080  0.0214  -0.0006 793  GLN B CD  
14918 O OE1 . GLN B 795  ? 0.3377 0.3765 0.3835 0.0088  0.0197  -0.0022 793  GLN B OE1 
14919 N NE2 . GLN B 795  ? 0.2870 0.3303 0.3326 0.0091  0.0238  -0.0005 793  GLN B NE2 
14920 N N   . LEU B 796  ? 0.2051 0.2342 0.2449 0.0027  0.0171  0.0032  794  LEU B N   
14921 C CA  . LEU B 796  ? 0.2045 0.2306 0.2401 0.0029  0.0170  0.0036  794  LEU B CA  
14922 C C   . LEU B 796  ? 0.2398 0.2640 0.2756 0.0011  0.0165  0.0057  794  LEU B C   
14923 O O   . LEU B 796  ? 0.2622 0.2850 0.2950 0.0011  0.0171  0.0068  794  LEU B O   
14924 C CB  . LEU B 796  ? 0.2106 0.2337 0.2440 0.0041  0.0151  0.0018  794  LEU B CB  
14925 C CG  . LEU B 796  ? 0.2146 0.2386 0.2464 0.0059  0.0155  -0.0001 794  LEU B CG  
14926 C CD1 . LEU B 796  ? 0.2314 0.2526 0.2614 0.0066  0.0137  -0.0015 794  LEU B CD1 
14927 C CD2 . LEU B 796  ? 0.2054 0.2305 0.2341 0.0066  0.0173  0.0003  794  LEU B CD2 
14928 N N   . ALA B 797  ? 0.2323 0.2558 0.2712 -0.0004 0.0153  0.0061  795  ALA B N   
14929 C CA  . ALA B 797  ? 0.3001 0.3211 0.3390 -0.0023 0.0146  0.0080  795  ALA B CA  
14930 C C   . ALA B 797  ? 0.3094 0.3328 0.3490 -0.0036 0.0166  0.0103  795  ALA B C   
14931 O O   . ALA B 797  ? 0.3354 0.3563 0.3739 -0.0050 0.0163  0.0121  795  ALA B O   
14932 C CB  . ALA B 797  ? 0.2931 0.3129 0.3352 -0.0038 0.0128  0.0077  795  ALA B CB  
14933 N N   . ASP B 798  ? 0.2787 0.3067 0.3199 -0.0032 0.0186  0.0104  796  ASP B N   
14934 C CA  . ASP B 798  ? 0.3388 0.3695 0.3802 -0.0042 0.0208  0.0126  796  ASP B CA  
14935 C C   . ASP B 798  ? 0.3510 0.3802 0.3875 -0.0032 0.0219  0.0131  796  ASP B C   
14936 O O   . ASP B 798  ? 0.3608 0.3910 0.3965 -0.0043 0.0234  0.0153  796  ASP B O   
14937 C CB  . ASP B 798  ? 0.3087 0.3451 0.3532 -0.0037 0.0229  0.0123  796  ASP B CB  
14938 C CG  . ASP B 798  ? 0.4840 0.5229 0.5340 -0.0050 0.0221  0.0124  796  ASP B CG  
14939 O OD1 . ASP B 798  ? 0.5858 0.6227 0.6375 -0.0072 0.0206  0.0136  796  ASP B OD1 
14940 O OD2 . ASP B 798  ? 0.5436 0.5864 0.5963 -0.0039 0.0230  0.0114  796  ASP B OD2 
14941 N N   . ARG B 799  ? 0.2939 0.3207 0.3270 -0.0013 0.0209  0.0114  797  ARG B N   
14942 C CA  A ARG B 799  ? 0.3512 0.3773 0.3797 -0.0001 0.0218  0.0115  797  ARG B CA  
14943 C CA  B ARG B 799  ? 0.3514 0.3775 0.3799 -0.0002 0.0219  0.0116  797  ARG B CA  
14944 C C   . ARG B 799  ? 0.3060 0.3274 0.3313 0.0001  0.0199  0.0117  797  ARG B C   
14945 O O   . ARG B 799  ? 0.2839 0.3026 0.3104 -0.0001 0.0179  0.0111  797  ARG B O   
14946 C CB  A ARG B 799  ? 0.3607 0.3883 0.3878 0.0020  0.0223  0.0091  797  ARG B CB  
14947 C CB  B ARG B 799  ? 0.3731 0.4013 0.4001 0.0019  0.0228  0.0095  797  ARG B CB  
14948 C CG  A ARG B 799  ? 0.3787 0.4105 0.4092 0.0024  0.0237  0.0083  797  ARG B CG  
14949 C CG  B ARG B 799  ? 0.3781 0.4106 0.4088 0.0021  0.0243  0.0089  797  ARG B CG  
14950 C CD  A ARG B 799  ? 0.3619 0.3943 0.3902 0.0046  0.0241  0.0059  797  ARG B CD  
14951 C CD  B ARG B 799  ? 0.3503 0.3852 0.3786 0.0037  0.0264  0.0081  797  ARG B CD  
14952 N NE  A ARG B 799  ? 0.3965 0.4270 0.4197 0.0054  0.0243  0.0058  797  ARG B NE  
14953 N NE  B ARG B 799  ? 0.3910 0.4231 0.4145 0.0051  0.0256  0.0067  797  ARG B NE  
14954 C CZ  A ARG B 799  ? 0.3418 0.3703 0.3623 0.0067  0.0230  0.0040  797  ARG B CZ  
14955 C CZ  B ARG B 799  ? 0.3558 0.3870 0.3787 0.0065  0.0245  0.0044  797  ARG B CZ  
14956 N NH1 A ARG B 799  ? 0.2910 0.3189 0.3131 0.0074  0.0218  0.0021  797  ARG B NH1 
14957 N NH1 B ARG B 799  ? 0.3413 0.3738 0.3676 0.0069  0.0242  0.0031  797  ARG B NH1 
14958 N NH2 A ARG B 799  ? 0.3135 0.3405 0.3296 0.0072  0.0230  0.0042  797  ARG B NH2 
14959 N NH2 B ARG B 799  ? 0.3688 0.3977 0.3875 0.0074  0.0237  0.0034  797  ARG B NH2 
14960 N N   . LEU B 800  ? 0.2832 0.3039 0.3046 0.0007  0.0206  0.0127  798  LEU B N   
14961 C CA  . LEU B 800  ? 0.2886 0.3055 0.3067 0.0014  0.0189  0.0128  798  LEU B CA  
14962 C C   . LEU B 800  ? 0.3359 0.3538 0.3500 0.0030  0.0196  0.0120  798  LEU B C   
14963 O O   . LEU B 800  ? 0.3407 0.3614 0.3539 0.0031  0.0215  0.0121  798  LEU B O   
14964 C CB  . LEU B 800  ? 0.3020 0.3165 0.3190 0.0000  0.0188  0.0156  798  LEU B CB  
14965 C CG  . LEU B 800  ? 0.3345 0.3466 0.3545 -0.0018 0.0177  0.0166  798  LEU B CG  
14966 C CD1 . LEU B 800  ? 0.3933 0.4026 0.4113 -0.0030 0.0177  0.0194  798  LEU B CD1 
14967 C CD2 . LEU B 800  ? 0.2973 0.3065 0.3181 -0.0009 0.0154  0.0147  798  LEU B CD2 
14968 N N   . SER B 801  ? 0.3055 0.3210 0.3173 0.0041  0.0179  0.0112  799  SER B N   
14969 C CA  . SER B 801  ? 0.3262 0.3422 0.3339 0.0054  0.0181  0.0108  799  SER B CA  
14970 C C   . SER B 801  ? 0.3818 0.3976 0.3866 0.0047  0.0192  0.0133  799  SER B C   
14971 O O   . SER B 801  ? 0.3677 0.3823 0.3736 0.0034  0.0194  0.0154  799  SER B O   
14972 C CB  . SER B 801  ? 0.3711 0.3848 0.3774 0.0066  0.0159  0.0099  799  SER B CB  
14973 O OG  . SER B 801  ? 0.3538 0.3646 0.3594 0.0062  0.0149  0.0118  799  SER B OG  
14974 N N   . PRO B 802  ? 0.4036 0.4205 0.4045 0.0055  0.0199  0.0131  800  PRO B N   
14975 C CA  . PRO B 802  ? 0.4315 0.4479 0.4290 0.0050  0.0206  0.0156  800  PRO B CA  
14976 C C   . PRO B 802  ? 0.4246 0.4375 0.4213 0.0049  0.0188  0.0174  800  PRO B C   
14977 O O   . PRO B 802  ? 0.4299 0.4419 0.4250 0.0040  0.0193  0.0200  800  PRO B O   
14978 C CB  . PRO B 802  ? 0.3848 0.4026 0.3781 0.0061  0.0210  0.0145  800  PRO B CB  
14979 C CG  . PRO B 802  ? 0.4163 0.4362 0.4113 0.0068  0.0217  0.0118  800  PRO B CG  
14980 C CD  . PRO B 802  ? 0.3838 0.4025 0.3831 0.0067  0.0202  0.0108  800  PRO B CD  
14981 N N   . ALA B 803  ? 0.3917 0.4027 0.3894 0.0058  0.0167  0.0162  801  ALA B N   
14982 C CA  . ALA B 803  ? 0.4194 0.4269 0.4168 0.0060  0.0149  0.0176  801  ALA B CA  
14983 C C   . ALA B 803  ? 0.4628 0.4681 0.4635 0.0047  0.0148  0.0186  801  ALA B C   
14984 O O   . ALA B 803  ? 0.4650 0.4668 0.4655 0.0048  0.0134  0.0198  801  ALA B O   
14985 C CB  . ALA B 803  ? 0.3862 0.3928 0.3835 0.0077  0.0129  0.0159  801  ALA B CB  
14986 N N   . GLY B 804  ? 0.3767 0.3841 0.3805 0.0034  0.0161  0.0181  802  GLY B N   
14987 C CA  . GLY B 804  ? 0.3604 0.3660 0.3674 0.0018  0.0159  0.0190  802  GLY B CA  
14988 C C   . GLY B 804  ? 0.3489 0.3524 0.3584 0.0023  0.0141  0.0172  802  GLY B C   
14989 O O   . GLY B 804  ? 0.3598 0.3601 0.3707 0.0014  0.0131  0.0181  802  GLY B O   
14990 N N   . ARG B 805  ? 0.3543 0.3595 0.3644 0.0037  0.0137  0.0146  803  ARG B N   
14991 C CA  . ARG B 805  ? 0.3135 0.3169 0.3256 0.0043  0.0120  0.0128  803  ARG B CA  
14992 C C   . ARG B 805  ? 0.2661 0.2725 0.2810 0.0041  0.0126  0.0108  803  ARG B C   
14993 O O   . ARG B 805  ? 0.2842 0.2938 0.2989 0.0042  0.0141  0.0104  803  ARG B O   
14994 C CB  . ARG B 805  ? 0.3305 0.3328 0.3403 0.0063  0.0106  0.0118  803  ARG B CB  
14995 C CG  . ARG B 805  ? 0.3890 0.3883 0.3963 0.0068  0.0098  0.0138  803  ARG B CG  
14996 C CD  . ARG B 805  ? 0.4185 0.4137 0.4271 0.0059  0.0090  0.0149  803  ARG B CD  
14997 N NE  . ARG B 805  ? 0.4875 0.4794 0.4936 0.0065  0.0081  0.0169  803  ARG B NE  
14998 C CZ  . ARG B 805  ? 0.4053 0.3959 0.4099 0.0054  0.0088  0.0195  803  ARG B CZ  
14999 N NH1 . ARG B 805  ? 0.4192 0.4116 0.4249 0.0033  0.0104  0.0205  803  ARG B NH1 
15000 N NH2 . ARG B 805  ? 0.5013 0.4888 0.5034 0.0063  0.0079  0.0212  803  ARG B NH2 
15001 N N   . PRO B 806  ? 0.2547 0.2597 0.2720 0.0039  0.0114  0.0095  804  PRO B N   
15002 C CA  . PRO B 806  ? 0.2444 0.2520 0.2644 0.0038  0.0117  0.0077  804  PRO B CA  
15003 C C   . PRO B 806  ? 0.2272 0.2370 0.2457 0.0054  0.0120  0.0059  804  PRO B C   
15004 O O   . PRO B 806  ? 0.2356 0.2443 0.2518 0.0067  0.0111  0.0054  804  PRO B O   
15005 C CB  . PRO B 806  ? 0.2703 0.2753 0.2921 0.0036  0.0100  0.0067  804  PRO B CB  
15006 C CG  . PRO B 806  ? 0.3247 0.3258 0.3456 0.0028  0.0092  0.0085  804  PRO B CG  
15007 C CD  . PRO B 806  ? 0.2917 0.2925 0.3092 0.0039  0.0097  0.0097  804  PRO B CD  
15008 N N   . ILE B 807  ? 0.2333 0.2462 0.2534 0.0052  0.0131  0.0050  805  ILE B N   
15009 C CA  . ILE B 807  ? 0.2090 0.2236 0.2280 0.0066  0.0133  0.0031  805  ILE B CA  
15010 C C   . ILE B 807  ? 0.1966 0.2100 0.2169 0.0071  0.0117  0.0013  805  ILE B C   
15011 O O   . ILE B 807  ? 0.2112 0.2245 0.2344 0.0064  0.0113  0.0010  805  ILE B O   
15012 C CB  . ILE B 807  ? 0.2009 0.2188 0.2214 0.0064  0.0151  0.0027  805  ILE B CB  
15013 C CG1 . ILE B 807  ? 0.2575 0.2769 0.2769 0.0057  0.0170  0.0046  805  ILE B CG1 
15014 C CG2 . ILE B 807  ? 0.2280 0.2469 0.2471 0.0077  0.0152  0.0007  805  ILE B CG2 
15015 C CD1 . ILE B 807  ? 0.3151 0.3342 0.3302 0.0066  0.0173  0.0049  805  ILE B CD1 
15016 N N   . PRO B 808  ? 0.1909 0.2034 0.2091 0.0083  0.0108  0.0002  806  PRO B N   
15017 C CA  . PRO B 808  ? 0.2097 0.2211 0.2289 0.0088  0.0093  -0.0014 806  PRO B CA  
15018 C C   . PRO B 808  ? 0.2103 0.2236 0.2314 0.0088  0.0097  -0.0028 806  PRO B C   
15019 O O   . PRO B 808  ? 0.1892 0.2044 0.2096 0.0091  0.0107  -0.0034 806  PRO B O   
15020 C CB  . PRO B 808  ? 0.2175 0.2286 0.2340 0.0100  0.0086  -0.0020 806  PRO B CB  
15021 C CG  . PRO B 808  ? 0.2547 0.2656 0.2690 0.0100  0.0091  -0.0003 806  PRO B CG  
15022 C CD  . PRO B 808  ? 0.1939 0.2065 0.2088 0.0091  0.0108  0.0006  806  PRO B CD  
15023 N N   . LEU B 809  ? 0.1829 0.1952 0.2061 0.0084  0.0086  -0.0036 807  LEU B N   
15024 C CA  . LEU B 809  ? 0.1694 0.1831 0.1944 0.0085  0.0086  -0.0049 807  LEU B CA  
15025 C C   . LEU B 809  ? 0.1690 0.1810 0.1935 0.0091  0.0070  -0.0063 807  LEU B C   
15026 O O   . LEU B 809  ? 0.2062 0.2162 0.2312 0.0088  0.0060  -0.0061 807  LEU B O   
15027 C CB  . LEU B 809  ? 0.1886 0.2031 0.2169 0.0074  0.0087  -0.0043 807  LEU B CB  
15028 C CG  . LEU B 809  ? 0.1816 0.1971 0.2120 0.0074  0.0083  -0.0055 807  LEU B CG  
15029 C CD1 . LEU B 809  ? 0.1912 0.2089 0.2213 0.0084  0.0094  -0.0064 807  LEU B CD1 
15030 C CD2 . LEU B 809  ? 0.2015 0.2180 0.2354 0.0061  0.0082  -0.0046 807  LEU B CD2 
15031 N N   . ILE B 810  ? 0.1624 0.1753 0.1861 0.0098  0.0069  -0.0076 808  ILE B N   
15032 C CA  . ILE B 810  ? 0.1554 0.1673 0.1791 0.0101  0.0057  -0.0089 808  ILE B CA  
15033 C C   . ILE B 810  ? 0.1729 0.1858 0.1988 0.0098  0.0057  -0.0095 808  ILE B C   
15034 O O   . ILE B 810  ? 0.1908 0.2053 0.2169 0.0101  0.0066  -0.0098 808  ILE B O   
15035 C CB  . ILE B 810  ? 0.1773 0.1894 0.1986 0.0109  0.0055  -0.0098 808  ILE B CB  
15036 C CG1 . ILE B 810  ? 0.1810 0.1928 0.2004 0.0113  0.0055  -0.0090 808  ILE B CG1 
15037 C CG2 . ILE B 810  ? 0.2228 0.2340 0.2442 0.0111  0.0043  -0.0110 808  ILE B CG2 
15038 C CD1 . ILE B 810  ? 0.2178 0.2302 0.2352 0.0120  0.0051  -0.0098 808  ILE B CD1 
15039 N N   . ALA B 811  ? 0.1717 0.1836 0.1992 0.0093  0.0047  -0.0097 809  ALA B N   
15040 C CA  . ALA B 811  ? 0.1704 0.1834 0.2003 0.0089  0.0045  -0.0101 809  ALA B CA  
15041 C C   . ALA B 811  ? 0.1917 0.2034 0.2213 0.0090  0.0030  -0.0113 809  ALA B C   
15042 O O   . ALA B 811  ? 0.1895 0.1994 0.2193 0.0085  0.0020  -0.0112 809  ALA B O   
15043 C CB  . ALA B 811  ? 0.1944 0.2081 0.2271 0.0078  0.0046  -0.0090 809  ALA B CB  
15044 N N   . GLU B 812  ? 0.1519 0.1640 0.1807 0.0097  0.0029  -0.0122 810  GLU B N   
15045 C CA  . GLU B 812  ? 0.1652 0.1762 0.1933 0.0098  0.0017  -0.0132 810  GLU B CA  
15046 C C   . GLU B 812  ? 0.1718 0.1837 0.2019 0.0096  0.0013  -0.0135 810  GLU B C   
15047 O O   . GLU B 812  ? 0.1864 0.1996 0.2170 0.0101  0.0020  -0.0136 810  GLU B O   
15048 C CB  . GLU B 812  ? 0.1887 0.1995 0.2142 0.0105  0.0019  -0.0140 810  GLU B CB  
15049 C CG  . GLU B 812  ? 0.1970 0.2074 0.2209 0.0107  0.0023  -0.0135 810  GLU B CG  
15050 C CD  . GLU B 812  ? 0.2192 0.2279 0.2429 0.0106  0.0014  -0.0134 810  GLU B CD  
15051 O OE1 . GLU B 812  ? 0.2106 0.2185 0.2333 0.0109  0.0007  -0.0142 810  GLU B OE1 
15052 O OE2 . GLU B 812  ? 0.2244 0.2324 0.2489 0.0103  0.0016  -0.0126 810  GLU B OE2 
15053 N N   . THR B 813  ? 0.1698 0.1808 0.2010 0.0090  0.0001  -0.0136 811  THR B N   
15054 C CA  . THR B 813  ? 0.1689 0.1812 0.2028 0.0086  -0.0004 -0.0134 811  THR B CA  
15055 C C   . THR B 813  ? 0.1800 0.1913 0.2134 0.0086  -0.0020 -0.0142 811  THR B C   
15056 O O   . THR B 813  ? 0.1805 0.1906 0.2115 0.0091  -0.0022 -0.0149 811  THR B O   
15057 C CB  . THR B 813  ? 0.1829 0.1959 0.2193 0.0076  -0.0004 -0.0123 811  THR B CB  
15058 O OG1 . THR B 813  ? 0.1872 0.1977 0.2223 0.0069  -0.0012 -0.0123 811  THR B OG1 
15059 C CG2 . THR B 813  ? 0.2085 0.2231 0.2454 0.0077  0.0013  -0.0114 811  THR B CG2 
15060 N N   . GLY B 814  ? 0.1842 0.1960 0.2199 0.0079  -0.0030 -0.0139 812  GLY B N   
15061 C CA  . GLY B 814  ? 0.1874 0.1987 0.2227 0.0080  -0.0044 -0.0146 812  GLY B CA  
15062 C C   . GLY B 814  ? 0.1839 0.1926 0.2169 0.0075  -0.0057 -0.0153 812  GLY B C   
15063 O O   . GLY B 814  ? 0.2117 0.2190 0.2434 0.0073  -0.0055 -0.0154 812  GLY B O   
15064 N N   . GLY B 815  ? 0.1897 0.1980 0.2221 0.0075  -0.0070 -0.0158 813  GLY B N   
15065 C CA  . GLY B 815  ? 0.1948 0.2007 0.2248 0.0071  -0.0082 -0.0165 813  GLY B CA  
15066 C C   . GLY B 815  ? 0.1747 0.1806 0.2056 0.0065  -0.0100 -0.0165 813  GLY B C   
15067 O O   . GLY B 815  ? 0.2140 0.2219 0.2474 0.0066  -0.0103 -0.0160 813  GLY B O   
15068 N N   . GLN B 816  ? 0.1792 0.1829 0.2081 0.0059  -0.0112 -0.0172 814  GLN B N   
15069 C CA  . GLN B 816  ? 0.1857 0.1890 0.2145 0.0052  -0.0131 -0.0174 814  GLN B CA  
15070 C C   . GLN B 816  ? 0.1761 0.1769 0.2007 0.0055  -0.0135 -0.0184 814  GLN B C   
15071 O O   . GLN B 816  ? 0.1915 0.1902 0.2143 0.0049  -0.0144 -0.0191 814  GLN B O   
15072 C CB  . GLN B 816  ? 0.1886 0.1919 0.2195 0.0038  -0.0145 -0.0171 814  GLN B CB  
15073 C CG  . GLN B 816  ? 0.1921 0.1956 0.2234 0.0031  -0.0167 -0.0171 814  GLN B CG  
15074 C CD  . GLN B 816  ? 0.1829 0.1895 0.2173 0.0037  -0.0167 -0.0162 814  GLN B CD  
15075 O OE1 . GLN B 816  ? 0.2075 0.2143 0.2406 0.0048  -0.0163 -0.0163 814  GLN B OE1 
15076 N NE2 . GLN B 816  ? 0.1944 0.2036 0.2330 0.0030  -0.0172 -0.0152 814  GLN B NE2 
15077 N N   . ASN B 817  ? 0.1541 0.1552 0.1771 0.0064  -0.0128 -0.0185 815  ASN B N   
15078 C CA  . ASN B 817  ? 0.1566 0.1561 0.1760 0.0068  -0.0123 -0.0193 815  ASN B CA  
15079 C C   . ASN B 817  ? 0.1630 0.1611 0.1798 0.0065  -0.0137 -0.0199 815  ASN B C   
15080 O O   . ASN B 817  ? 0.1783 0.1771 0.1956 0.0064  -0.0146 -0.0194 815  ASN B O   
15081 C CB  . ASN B 817  ? 0.1833 0.1839 0.2021 0.0077  -0.0108 -0.0192 815  ASN B CB  
15082 C CG  . ASN B 817  ? 0.1705 0.1725 0.1916 0.0080  -0.0095 -0.0186 815  ASN B CG  
15083 O OD1 . ASN B 817  ? 0.1638 0.1656 0.1854 0.0079  -0.0089 -0.0186 815  ASN B OD1 
15084 N ND2 . ASN B 817  ? 0.1676 0.1711 0.1901 0.0084  -0.0090 -0.0181 815  ASN B ND2 
15085 N N   . ALA B 818  ? 0.1610 0.1570 0.1748 0.0065  -0.0138 -0.0208 816  ALA B N   
15086 C CA  . ALA B 818  ? 0.1656 0.1600 0.1763 0.0062  -0.0151 -0.0214 816  ALA B CA  
15087 C C   . ALA B 818  ? 0.1664 0.1605 0.1739 0.0069  -0.0140 -0.0219 816  ALA B C   
15088 O O   . ALA B 818  ? 0.1716 0.1662 0.1788 0.0076  -0.0124 -0.0220 816  ALA B O   
15089 C CB  . ALA B 818  ? 0.1922 0.1842 0.2018 0.0055  -0.0162 -0.0222 816  ALA B CB  
15090 N N   . MET B 819  ? 0.1776 0.1709 0.1825 0.0066  -0.0149 -0.0221 817  MET B N   
15091 C CA  . MET B 819  ? 0.1794 0.1721 0.1805 0.0071  -0.0141 -0.0226 817  MET B CA  
15092 C C   . MET B 819  ? 0.1691 0.1596 0.1670 0.0067  -0.0154 -0.0235 817  MET B C   
15093 O O   . MET B 819  ? 0.1929 0.1829 0.1907 0.0059  -0.0173 -0.0232 817  MET B O   
15094 C CB  . MET B 819  ? 0.1974 0.1915 0.1981 0.0071  -0.0137 -0.0218 817  MET B CB  
15095 C CG  . MET B 819  ? 0.2076 0.2014 0.2046 0.0073  -0.0129 -0.0222 817  MET B CG  
15096 S SD  . MET B 819  ? 0.2294 0.2241 0.2254 0.0069  -0.0128 -0.0211 817  MET B SD  
15097 C CE  . MET B 819  ? 0.2554 0.2521 0.2543 0.0073  -0.0111 -0.0205 817  MET B CE  
15098 N N   . ILE B 820  ? 0.1830 0.1722 0.1781 0.0073  -0.0146 -0.0246 818  ILE B N   
15099 C CA  . ILE B 820  ? 0.1759 0.1626 0.1670 0.0071  -0.0156 -0.0257 818  ILE B CA  
15100 C C   . ILE B 820  ? 0.1874 0.1746 0.1750 0.0075  -0.0147 -0.0258 818  ILE B C   
15101 O O   . ILE B 820  ? 0.2005 0.1892 0.1880 0.0083  -0.0128 -0.0257 818  ILE B O   
15102 C CB  . ILE B 820  ? 0.1890 0.1734 0.1790 0.0076  -0.0153 -0.0269 818  ILE B CB  
15103 C CG1 . ILE B 820  ? 0.1987 0.1824 0.1921 0.0068  -0.0164 -0.0267 818  ILE B CG1 
15104 C CG2 . ILE B 820  ? 0.2133 0.1947 0.1985 0.0075  -0.0163 -0.0283 818  ILE B CG2 
15105 C CD1 . ILE B 820  ? 0.2363 0.2172 0.2286 0.0072  -0.0163 -0.0278 818  ILE B CD1 
15106 N N   . VAL B 821  ? 0.1952 0.1814 0.1801 0.0068  -0.0161 -0.0258 819  VAL B N   
15107 C CA  . VAL B 821  ? 0.2119 0.1985 0.1932 0.0069  -0.0154 -0.0256 819  VAL B CA  
15108 C C   . VAL B 821  ? 0.2114 0.1954 0.1880 0.0069  -0.0162 -0.0270 819  VAL B C   
15109 O O   . VAL B 821  ? 0.2228 0.2050 0.1987 0.0060  -0.0184 -0.0272 819  VAL B O   
15110 C CB  . VAL B 821  ? 0.2076 0.1952 0.1896 0.0061  -0.0165 -0.0242 819  VAL B CB  
15111 C CG1 . VAL B 821  ? 0.2354 0.2232 0.2134 0.0060  -0.0158 -0.0239 819  VAL B CG1 
15112 C CG2 . VAL B 821  ? 0.2036 0.1933 0.1901 0.0062  -0.0158 -0.0231 819  VAL B CG2 
15113 N N   . ASP B 822  ? 0.2157 0.1995 0.1890 0.0078  -0.0145 -0.0278 820  ASP B N   
15114 C CA  . ASP B 822  ? 0.2312 0.2123 0.1993 0.0079  -0.0152 -0.0292 820  ASP B CA  
15115 C C   . ASP B 822  ? 0.2418 0.2236 0.2063 0.0075  -0.0150 -0.0285 820  ASP B C   
15116 O O   . ASP B 822  ? 0.2448 0.2289 0.2107 0.0070  -0.0145 -0.0270 820  ASP B O   
15117 C CB  . ASP B 822  ? 0.2385 0.2182 0.2049 0.0093  -0.0137 -0.0309 820  ASP B CB  
15118 C CG  . ASP B 822  ? 0.2477 0.2297 0.2131 0.0106  -0.0109 -0.0308 820  ASP B CG  
15119 O OD1 . ASP B 822  ? 0.2398 0.2244 0.2050 0.0102  -0.0102 -0.0297 820  ASP B OD1 
15120 O OD2 . ASP B 822  ? 0.2716 0.2530 0.2365 0.0121  -0.0095 -0.0320 820  ASP B OD2 
15121 N N   . SER B 823  ? 0.2539 0.2335 0.2133 0.0075  -0.0155 -0.0297 821  SER B N   
15122 C CA  . SER B 823  ? 0.2735 0.2534 0.2289 0.0070  -0.0155 -0.0291 821  SER B CA  
15123 C C   . SER B 823  ? 0.2742 0.2567 0.2283 0.0078  -0.0127 -0.0287 821  SER B C   
15124 O O   . SER B 823  ? 0.3217 0.3049 0.2728 0.0072  -0.0125 -0.0279 821  SER B O   
15125 C CB  . SER B 823  ? 0.2916 0.2682 0.2415 0.0067  -0.0170 -0.0305 821  SER B CB  
15126 O OG  . SER B 823  ? 0.3158 0.2908 0.2630 0.0081  -0.0155 -0.0324 821  SER B OG  
15127 N N   . SER B 824  ? 0.2377 0.2219 0.1942 0.0090  -0.0106 -0.0291 822  SER B N   
15128 C CA  . SER B 824  ? 0.2419 0.2292 0.1979 0.0096  -0.0080 -0.0286 822  SER B CA  
15129 C C   . SER B 824  ? 0.2543 0.2447 0.2146 0.0088  -0.0075 -0.0267 822  SER B C   
15130 O O   . SER B 824  ? 0.2838 0.2769 0.2437 0.0088  -0.0057 -0.0258 822  SER B O   
15131 C CB  . SER B 824  ? 0.2623 0.2502 0.2187 0.0115  -0.0059 -0.0300 822  SER B CB  
15132 O OG  . SER B 824  ? 0.2404 0.2292 0.2018 0.0120  -0.0057 -0.0297 822  SER B OG  
15133 N N   . ALA B 825  ? 0.2387 0.2285 0.2027 0.0081  -0.0091 -0.0260 823  ALA B N   
15134 C CA  . ALA B 825  ? 0.2363 0.2285 0.2042 0.0075  -0.0087 -0.0244 823  ALA B CA  
15135 C C   . ALA B 825  ? 0.2424 0.2349 0.2083 0.0062  -0.0092 -0.0229 823  ALA B C   
15136 O O   . ALA B 825  ? 0.2722 0.2627 0.2347 0.0056  -0.0106 -0.0229 823  ALA B O   
15137 C CB  . ALA B 825  ? 0.2487 0.2400 0.2207 0.0073  -0.0103 -0.0242 823  ALA B CB  
15138 N N   . LEU B 826  ? 0.2758 0.2705 0.2437 0.0057  -0.0082 -0.0216 824  LEU B N   
15139 C CA  . LEU B 826  ? 0.2592 0.2541 0.2256 0.0043  -0.0086 -0.0200 824  LEU B CA  
15140 C C   . LEU B 826  ? 0.2604 0.2538 0.2293 0.0037  -0.0107 -0.0191 824  LEU B C   
15141 O O   . LEU B 826  ? 0.2513 0.2455 0.2242 0.0039  -0.0105 -0.0189 824  LEU B O   
15142 C CB  . LEU B 826  ? 0.3134 0.3112 0.2808 0.0039  -0.0066 -0.0190 824  LEU B CB  
15143 C CG  . LEU B 826  ? 0.3684 0.3661 0.3339 0.0023  -0.0069 -0.0173 824  LEU B CG  
15144 C CD1 . LEU B 826  ? 0.4205 0.4172 0.3808 0.0019  -0.0070 -0.0172 824  LEU B CD1 
15145 C CD2 . LEU B 826  ? 0.4492 0.4499 0.4162 0.0016  -0.0050 -0.0164 824  LEU B CD2 
15146 N N   . ALA B 827  ? 0.2752 0.2664 0.2416 0.0031  -0.0126 -0.0186 825  ALA B N   
15147 C CA  . ALA B 827  ? 0.2448 0.2347 0.2138 0.0029  -0.0147 -0.0179 825  ALA B CA  
15148 C C   . ALA B 827  ? 0.2502 0.2409 0.2221 0.0025  -0.0143 -0.0165 825  ALA B C   
15149 O O   . ALA B 827  ? 0.2369 0.2275 0.2127 0.0028  -0.0150 -0.0165 825  ALA B O   
15150 C CB  . ALA B 827  ? 0.2552 0.2430 0.2207 0.0022  -0.0168 -0.0172 825  ALA B CB  
15151 N N   . GLU B 828  ? 0.2562 0.2475 0.2263 0.0016  -0.0132 -0.0155 826  GLU B N   
15152 C CA  . GLU B 828  ? 0.2698 0.2613 0.2422 0.0011  -0.0130 -0.0143 826  GLU B CA  
15153 C C   . GLU B 828  ? 0.2710 0.2643 0.2474 0.0017  -0.0117 -0.0150 826  GLU B C   
15154 O O   . GLU B 828  ? 0.2359 0.2288 0.2152 0.0017  -0.0122 -0.0146 826  GLU B O   
15155 C CB  . GLU B 828  ? 0.2894 0.2814 0.2590 -0.0002 -0.0118 -0.0131 826  GLU B CB  
15156 C CG  . GLU B 828  ? 0.3360 0.3258 0.3018 -0.0011 -0.0132 -0.0118 826  GLU B CG  
15157 C CD  . GLU B 828  ? 0.3499 0.3397 0.3116 -0.0010 -0.0133 -0.0124 826  GLU B CD  
15158 O OE1 . GLU B 828  ? 0.3484 0.3396 0.3100 -0.0001 -0.0122 -0.0139 826  GLU B OE1 
15159 O OE2 . GLU B 828  ? 0.3829 0.3708 0.3410 -0.0017 -0.0144 -0.0112 826  GLU B OE2 
15160 N N   . GLN B 829  ? 0.2384 0.2337 0.2149 0.0022  -0.0101 -0.0161 827  GLN B N   
15161 C CA  A GLN B 829  ? 0.2466 0.2436 0.2267 0.0029  -0.0090 -0.0167 827  GLN B CA  
15162 C CA  B GLN B 829  ? 0.2466 0.2437 0.2267 0.0029  -0.0090 -0.0167 827  GLN B CA  
15163 C C   . GLN B 829  ? 0.2414 0.2375 0.2244 0.0038  -0.0102 -0.0174 827  GLN B C   
15164 O O   . GLN B 829  ? 0.2361 0.2325 0.2223 0.0040  -0.0101 -0.0173 827  GLN B O   
15165 C CB  A GLN B 829  ? 0.2909 0.2902 0.2703 0.0035  -0.0072 -0.0176 827  GLN B CB  
15166 C CB  B GLN B 829  ? 0.2909 0.2902 0.2703 0.0035  -0.0072 -0.0176 827  GLN B CB  
15167 C CG  A GLN B 829  ? 0.2725 0.2740 0.2504 0.0026  -0.0056 -0.0168 827  GLN B CG  
15168 C CG  B GLN B 829  ? 0.2284 0.2297 0.2113 0.0042  -0.0060 -0.0181 827  GLN B CG  
15169 C CD  A GLN B 829  ? 0.3412 0.3454 0.3193 0.0036  -0.0037 -0.0177 827  GLN B CD  
15170 C CD  B GLN B 829  ? 0.3155 0.3191 0.2976 0.0050  -0.0043 -0.0189 827  GLN B CD  
15171 O OE1 A GLN B 829  ? 0.3374 0.3411 0.3153 0.0049  -0.0037 -0.0190 827  GLN B OE1 
15172 O OE1 B GLN B 829  ? 0.3508 0.3540 0.3299 0.0055  -0.0040 -0.0195 827  GLN B OE1 
15173 N NE2 A GLN B 829  ? 0.3751 0.3823 0.3537 0.0030  -0.0022 -0.0171 827  GLN B NE2 
15174 N NE2 B GLN B 829  ? 0.2937 0.2996 0.2784 0.0054  -0.0031 -0.0190 827  GLN B NE2 
15175 N N   . VAL B 830  ? 0.2244 0.2191 0.2061 0.0042  -0.0113 -0.0182 828  VAL B N   
15176 C CA  . VAL B 830  ? 0.2068 0.2006 0.1912 0.0047  -0.0126 -0.0187 828  VAL B CA  
15177 C C   . VAL B 830  ? 0.2326 0.2258 0.2193 0.0045  -0.0139 -0.0176 828  VAL B C   
15178 O O   . VAL B 830  ? 0.2178 0.2115 0.2080 0.0050  -0.0139 -0.0177 828  VAL B O   
15179 C CB  . VAL B 830  ? 0.2175 0.2098 0.1996 0.0048  -0.0140 -0.0195 828  VAL B CB  
15180 C CG1 . VAL B 830  ? 0.2241 0.2157 0.2092 0.0051  -0.0156 -0.0197 828  VAL B CG1 
15181 C CG2 . VAL B 830  ? 0.2427 0.2352 0.2227 0.0054  -0.0127 -0.0208 828  VAL B CG2 
15182 N N   . VAL B 831  ? 0.2145 0.2064 0.1989 0.0039  -0.0149 -0.0166 829  VAL B N   
15183 C CA  . VAL B 831  ? 0.2069 0.1979 0.1933 0.0039  -0.0163 -0.0156 829  VAL B CA  
15184 C C   . VAL B 831  ? 0.2099 0.2015 0.1987 0.0040  -0.0151 -0.0152 829  VAL B C   
15185 O O   . VAL B 831  ? 0.2113 0.2030 0.2033 0.0046  -0.0155 -0.0151 829  VAL B O   
15186 C CB  . VAL B 831  ? 0.2232 0.2123 0.2063 0.0033  -0.0176 -0.0144 829  VAL B CB  
15187 C CG1 . VAL B 831  ? 0.2240 0.2120 0.2089 0.0035  -0.0186 -0.0133 829  VAL B CG1 
15188 C CG2 . VAL B 831  ? 0.2403 0.2287 0.2217 0.0033  -0.0193 -0.0149 829  VAL B CG2 
15189 N N   . GLY B 832  ? 0.2104 0.2027 0.1977 0.0033  -0.0136 -0.0150 830  GLY B N   
15190 C CA  . GLY B 832  ? 0.2064 0.1993 0.1958 0.0033  -0.0126 -0.0147 830  GLY B CA  
15191 C C   . GLY B 832  ? 0.2080 0.2023 0.2008 0.0041  -0.0118 -0.0157 830  GLY B C   
15192 O O   . GLY B 832  ? 0.2214 0.2156 0.2166 0.0045  -0.0118 -0.0156 830  GLY B O   
15193 N N   . ASP B 833  ? 0.1941 0.1897 0.1869 0.0045  -0.0112 -0.0166 831  ASP B N   
15194 C CA  . ASP B 833  ? 0.2060 0.2029 0.2017 0.0053  -0.0105 -0.0174 831  ASP B CA  
15195 C C   . ASP B 833  ? 0.2136 0.2098 0.2118 0.0059  -0.0118 -0.0175 831  ASP B C   
15196 O O   . ASP B 833  ? 0.2004 0.1974 0.2014 0.0064  -0.0113 -0.0177 831  ASP B O   
15197 C CB  . ASP B 833  ? 0.2036 0.2017 0.1983 0.0056  -0.0095 -0.0183 831  ASP B CB  
15198 C CG  . ASP B 833  ? 0.2164 0.2161 0.2097 0.0052  -0.0080 -0.0181 831  ASP B CG  
15199 O OD1 . ASP B 833  ? 0.2415 0.2415 0.2351 0.0045  -0.0077 -0.0174 831  ASP B OD1 
15200 O OD2 . ASP B 833  ? 0.2363 0.2369 0.2282 0.0055  -0.0072 -0.0187 831  ASP B OD2 
15201 N N   . VAL B 834  ? 0.1919 0.1869 0.1890 0.0058  -0.0133 -0.0173 832  VAL B N   
15202 C CA  . VAL B 834  ? 0.1857 0.1806 0.1856 0.0063  -0.0147 -0.0173 832  VAL B CA  
15203 C C   . VAL B 834  ? 0.1968 0.1914 0.1987 0.0066  -0.0149 -0.0165 832  VAL B C   
15204 O O   . VAL B 834  ? 0.1958 0.1913 0.2009 0.0073  -0.0148 -0.0165 832  VAL B O   
15205 C CB  . VAL B 834  ? 0.1948 0.1885 0.1929 0.0060  -0.0165 -0.0172 832  VAL B CB  
15206 C CG1 . VAL B 834  ? 0.2063 0.2002 0.2074 0.0063  -0.0181 -0.0167 832  VAL B CG1 
15207 C CG2 . VAL B 834  ? 0.2214 0.2151 0.2180 0.0058  -0.0163 -0.0183 832  VAL B CG2 
15208 N N   . ILE B 835  ? 0.1972 0.1906 0.1971 0.0063  -0.0151 -0.0157 833  ILE B N   
15209 C CA  . ILE B 835  ? 0.2325 0.2251 0.2339 0.0068  -0.0153 -0.0150 833  ILE B CA  
15210 C C   . ILE B 835  ? 0.2291 0.2227 0.2324 0.0071  -0.0137 -0.0155 833  ILE B C   
15211 O O   . ILE B 835  ? 0.2363 0.2302 0.2423 0.0079  -0.0136 -0.0155 833  ILE B O   
15212 C CB  . ILE B 835  ? 0.2427 0.2332 0.2411 0.0062  -0.0159 -0.0141 833  ILE B CB  
15213 C CG1 . ILE B 835  ? 0.2922 0.2817 0.2891 0.0061  -0.0177 -0.0135 833  ILE B CG1 
15214 C CG2 . ILE B 835  ? 0.2868 0.2760 0.2865 0.0068  -0.0158 -0.0135 833  ILE B CG2 
15215 C CD1 . ILE B 835  ? 0.3119 0.2993 0.3059 0.0056  -0.0185 -0.0124 833  ILE B CD1 
15216 N N   . THR B 836  ? 0.2003 0.1945 0.2022 0.0064  -0.0124 -0.0158 834  THR B N   
15217 C CA  . THR B 836  ? 0.2019 0.1972 0.2053 0.0066  -0.0110 -0.0162 834  THR B CA  
15218 C C   . THR B 836  ? 0.2241 0.2208 0.2305 0.0074  -0.0107 -0.0168 834  THR B C   
15219 O O   . THR B 836  ? 0.2805 0.2776 0.2890 0.0080  -0.0102 -0.0168 834  THR B O   
15220 C CB  . THR B 836  ? 0.2292 0.2255 0.2308 0.0058  -0.0098 -0.0165 834  THR B CB  
15221 O OG1 . THR B 836  ? 0.2881 0.2833 0.2871 0.0048  -0.0099 -0.0158 834  THR B OG1 
15222 C CG2 . THR B 836  ? 0.2740 0.2718 0.2772 0.0060  -0.0085 -0.0169 834  THR B CG2 
15223 N N   . SER B 837  ? 0.1952 0.1926 0.2016 0.0074  -0.0110 -0.0172 835  SER B N   
15224 C CA  . SER B 837  ? 0.1993 0.1980 0.2083 0.0079  -0.0106 -0.0176 835  SER B CA  
15225 C C   . SER B 837  ? 0.1877 0.1866 0.1995 0.0084  -0.0116 -0.0173 835  SER B C   
15226 O O   . SER B 837  ? 0.1939 0.1939 0.2083 0.0089  -0.0110 -0.0174 835  SER B O   
15227 C CB  . SER B 837  ? 0.1901 0.1890 0.1980 0.0077  -0.0107 -0.0182 835  SER B CB  
15228 O OG  . SER B 837  ? 0.1934 0.1927 0.1991 0.0074  -0.0096 -0.0185 835  SER B OG  
15229 N N   . ALA B 838  ? 0.1888 0.1868 0.2001 0.0084  -0.0132 -0.0169 836  ALA B N   
15230 C CA  . ALA B 838  ? 0.1919 0.1907 0.2062 0.0089  -0.0143 -0.0165 836  ALA B CA  
15231 C C   . ALA B 838  ? 0.1974 0.1960 0.2132 0.0097  -0.0143 -0.0159 836  ALA B C   
15232 O O   . ALA B 838  ? 0.2256 0.2256 0.2447 0.0104  -0.0144 -0.0157 836  ALA B O   
15233 C CB  . ALA B 838  ? 0.1884 0.1865 0.2015 0.0084  -0.0162 -0.0163 836  ALA B CB  
15234 N N   . PHE B 839  ? 0.2074 0.2042 0.2208 0.0097  -0.0144 -0.0156 837  PHE B N   
15235 C CA  . PHE B 839  ? 0.2233 0.2193 0.2377 0.0107  -0.0149 -0.0149 837  PHE B CA  
15236 C C   . PHE B 839  ? 0.2570 0.2517 0.2706 0.0110  -0.0136 -0.0151 837  PHE B C   
15237 O O   . PHE B 839  ? 0.2454 0.2396 0.2604 0.0121  -0.0135 -0.0149 837  PHE B O   
15238 C CB  . PHE B 839  ? 0.2213 0.2155 0.2336 0.0105  -0.0166 -0.0142 837  PHE B CB  
15239 C CG  . PHE B 839  ? 0.2146 0.2097 0.2274 0.0102  -0.0182 -0.0140 837  PHE B CG  
15240 C CD1 . PHE B 839  ? 0.2148 0.2120 0.2315 0.0108  -0.0190 -0.0139 837  PHE B CD1 
15241 C CD2 . PHE B 839  ? 0.2357 0.2298 0.2453 0.0091  -0.0190 -0.0141 837  PHE B CD2 
15242 C CE1 . PHE B 839  ? 0.2120 0.2100 0.2292 0.0103  -0.0206 -0.0138 837  PHE B CE1 
15243 C CE2 . PHE B 839  ? 0.2308 0.2256 0.2406 0.0087  -0.0206 -0.0141 837  PHE B CE2 
15244 C CZ  . PHE B 839  ? 0.2146 0.2112 0.2282 0.0092  -0.0215 -0.0139 837  PHE B CZ  
15245 N N   . ASP B 840  ? 0.2250 0.2193 0.2363 0.0100  -0.0125 -0.0155 838  ASP B N   
15246 C CA  . ASP B 840  ? 0.2434 0.2369 0.2541 0.0101  -0.0113 -0.0158 838  ASP B CA  
15247 C C   . ASP B 840  ? 0.2669 0.2619 0.2805 0.0112  -0.0103 -0.0162 838  ASP B C   
15248 O O   . ASP B 840  ? 0.2395 0.2367 0.2553 0.0113  -0.0101 -0.0164 838  ASP B O   
15249 C CB  . ASP B 840  ? 0.3278 0.3215 0.3362 0.0089  -0.0104 -0.0161 838  ASP B CB  
15250 C CG  . ASP B 840  ? 0.4173 0.4094 0.4240 0.0084  -0.0097 -0.0162 838  ASP B CG  
15251 O OD1 . ASP B 840  ? 0.4629 0.4527 0.4692 0.0090  -0.0102 -0.0159 838  ASP B OD1 
15252 O OD2 . ASP B 840  ? 0.4550 0.4480 0.4608 0.0076  -0.0088 -0.0165 838  ASP B OD2 
15253 N N   . SER B 841  ? 0.2321 0.2259 0.2458 0.0119  -0.0097 -0.0163 839  SER B N   
15254 C CA  . SER B 841  ? 0.2279 0.2231 0.2442 0.0131  -0.0087 -0.0167 839  SER B CA  
15255 C C   . SER B 841  ? 0.2121 0.2092 0.2318 0.0142  -0.0093 -0.0163 839  SER B C   
15256 O O   . SER B 841  ? 0.1992 0.1985 0.2216 0.0148  -0.0084 -0.0164 839  SER B O   
15257 C CB  . SER B 841  ? 0.2787 0.2757 0.2952 0.0126  -0.0073 -0.0172 839  SER B CB  
15258 O OG  . SER B 841  ? 0.2756 0.2714 0.2893 0.0116  -0.0068 -0.0176 839  SER B OG  
15259 N N   . ALA B 842  ? 0.1987 0.1950 0.2183 0.0143  -0.0109 -0.0156 840  ALA B N   
15260 C CA  . ALA B 842  ? 0.2014 0.1997 0.2242 0.0150  -0.0119 -0.0151 840  ALA B CA  
15261 C C   . ALA B 842  ? 0.1841 0.1852 0.2090 0.0143  -0.0116 -0.0153 840  ALA B C   
15262 O O   . ALA B 842  ? 0.1883 0.1918 0.2167 0.0149  -0.0116 -0.0150 840  ALA B O   
15263 C CB  . ALA B 842  ? 0.2068 0.2055 0.2322 0.0169  -0.0117 -0.0148 840  ALA B CB  
15264 N N   . GLY B 843  ? 0.1774 0.1781 0.2001 0.0130  -0.0114 -0.0157 841  GLY B N   
15265 C CA  . GLY B 843  ? 0.1703 0.1730 0.1945 0.0123  -0.0112 -0.0159 841  GLY B CA  
15266 C C   . GLY B 843  ? 0.1810 0.1854 0.2073 0.0126  -0.0096 -0.0161 841  GLY B C   
15267 O O   . GLY B 843  ? 0.1835 0.1895 0.2115 0.0122  -0.0095 -0.0161 841  GLY B O   
15268 N N   . GLN B 844  ? 0.1715 0.1754 0.1973 0.0134  -0.0084 -0.0163 842  GLN B N   
15269 C CA  . GLN B 844  ? 0.1656 0.1711 0.1931 0.0139  -0.0068 -0.0165 842  GLN B CA  
15270 C C   . GLN B 844  ? 0.1796 0.1847 0.2050 0.0131  -0.0057 -0.0170 842  GLN B C   
15271 O O   . GLN B 844  ? 0.1922 0.1969 0.2165 0.0134  -0.0045 -0.0173 842  GLN B O   
15272 C CB  . GLN B 844  ? 0.1731 0.1783 0.2014 0.0154  -0.0060 -0.0165 842  GLN B CB  
15273 C CG  . GLN B 844  ? 0.1697 0.1762 0.2010 0.0164  -0.0071 -0.0159 842  GLN B CG  
15274 C CD  . GLN B 844  ? 0.1780 0.1836 0.2097 0.0181  -0.0065 -0.0159 842  GLN B CD  
15275 O OE1 . GLN B 844  ? 0.1764 0.1842 0.2112 0.0194  -0.0059 -0.0157 842  GLN B OE1 
15276 N NE2 . GLN B 844  ? 0.2020 0.2043 0.2305 0.0183  -0.0069 -0.0162 842  GLN B NE2 
15277 N N   . ARG B 845  ? 0.1781 0.1833 0.2027 0.0121  -0.0062 -0.0170 843  ARG B N   
15278 C CA  . ARG B 845  ? 0.1579 0.1633 0.1811 0.0115  -0.0053 -0.0173 843  ARG B CA  
15279 C C   . ARG B 845  ? 0.1577 0.1643 0.1826 0.0111  -0.0055 -0.0171 843  ARG B C   
15280 O O   . ARG B 845  ? 0.1666 0.1731 0.1923 0.0107  -0.0068 -0.0170 843  ARG B O   
15281 C CB  . ARG B 845  ? 0.1842 0.1881 0.2044 0.0108  -0.0058 -0.0176 843  ARG B CB  
15282 C CG  . ARG B 845  ? 0.2106 0.2129 0.2287 0.0108  -0.0058 -0.0177 843  ARG B CG  
15283 C CD  . ARG B 845  ? 0.2859 0.2876 0.3013 0.0099  -0.0058 -0.0179 843  ARG B CD  
15284 N NE  . ARG B 845  ? 0.2794 0.2797 0.2926 0.0095  -0.0057 -0.0180 843  ARG B NE  
15285 C CZ  . ARG B 845  ? 0.3008 0.2995 0.3123 0.0091  -0.0066 -0.0177 843  ARG B CZ  
15286 N NH1 . ARG B 845  ? 0.3318 0.3303 0.3435 0.0091  -0.0077 -0.0174 843  ARG B NH1 
15287 N NH2 . ARG B 845  ? 0.3538 0.3512 0.3633 0.0084  -0.0064 -0.0177 843  ARG B NH2 
15288 N N   . CYS B 846  ? 0.1740 0.1813 0.1992 0.0110  -0.0044 -0.0171 844  CYS B N   
15289 C CA  . CYS B 846  ? 0.1801 0.1881 0.2067 0.0104  -0.0047 -0.0169 844  CYS B CA  
15290 C C   . CYS B 846  ? 0.1424 0.1490 0.1670 0.0099  -0.0056 -0.0173 844  CYS B C   
15291 O O   . CYS B 846  ? 0.1766 0.1829 0.2020 0.0094  -0.0065 -0.0173 844  CYS B O   
15292 C CB  . CYS B 846  ? 0.1854 0.1940 0.2120 0.0105  -0.0033 -0.0167 844  CYS B CB  
15293 S SG  . CYS B 846  ? 0.1802 0.1882 0.2037 0.0106  -0.0025 -0.0172 844  CYS B SG  
15294 N N   . SER B 847  ? 0.1535 0.1592 0.1754 0.0099  -0.0055 -0.0177 845  SER B N   
15295 C CA  . SER B 847  ? 0.1480 0.1526 0.1678 0.0095  -0.0061 -0.0181 845  SER B CA  
15296 C C   . SER B 847  ? 0.1632 0.1668 0.1822 0.0093  -0.0075 -0.0182 845  SER B C   
15297 O O   . SER B 847  ? 0.1663 0.1690 0.1832 0.0090  -0.0080 -0.0186 845  SER B O   
15298 C CB  . SER B 847  ? 0.1698 0.1744 0.1873 0.0096  -0.0053 -0.0184 845  SER B CB  
15299 O OG  . SER B 847  ? 0.1762 0.1807 0.1935 0.0097  -0.0052 -0.0182 845  SER B OG  
15300 N N   . ALA B 848  ? 0.1563 0.1602 0.1768 0.0094  -0.0081 -0.0178 846  ALA B N   
15301 C CA  . ALA B 848  ? 0.1604 0.1633 0.1798 0.0093  -0.0094 -0.0177 846  ALA B CA  
15302 C C   . ALA B 848  ? 0.1684 0.1707 0.1875 0.0087  -0.0107 -0.0179 846  ALA B C   
15303 O O   . ALA B 848  ? 0.1762 0.1790 0.1970 0.0084  -0.0109 -0.0180 846  ALA B O   
15304 C CB  . ALA B 848  ? 0.1714 0.1750 0.1932 0.0098  -0.0099 -0.0172 846  ALA B CB  
15305 N N   . LEU B 849  ? 0.1646 0.1657 0.1812 0.0084  -0.0117 -0.0181 847  LEU B N   
15306 C CA  . LEU B 849  ? 0.1688 0.1690 0.1844 0.0078  -0.0131 -0.0184 847  LEU B CA  
15307 C C   . LEU B 849  ? 0.1651 0.1660 0.1833 0.0077  -0.0146 -0.0178 847  LEU B C   
15308 O O   . LEU B 849  ? 0.1865 0.1877 0.2055 0.0080  -0.0153 -0.0172 847  LEU B O   
15309 C CB  . LEU B 849  ? 0.1856 0.1844 0.1976 0.0076  -0.0136 -0.0185 847  LEU B CB  
15310 C CG  . LEU B 849  ? 0.1875 0.1851 0.1977 0.0070  -0.0152 -0.0189 847  LEU B CG  
15311 C CD1 . LEU B 849  ? 0.2037 0.2007 0.2135 0.0068  -0.0149 -0.0197 847  LEU B CD1 
15312 C CD2 . LEU B 849  ? 0.2063 0.2028 0.2127 0.0068  -0.0154 -0.0189 847  LEU B CD2 
15313 N N   . ARG B 850  ? 0.1677 0.1688 0.1874 0.0071  -0.0152 -0.0180 848  ARG B N   
15314 C CA  . ARG B 850  ? 0.1795 0.1818 0.2022 0.0068  -0.0167 -0.0175 848  ARG B CA  
15315 C C   . ARG B 850  ? 0.1817 0.1826 0.2026 0.0058  -0.0188 -0.0178 848  ARG B C   
15316 O O   . ARG B 850  ? 0.1785 0.1803 0.2010 0.0056  -0.0205 -0.0173 848  ARG B O   
15317 C CB  . ARG B 850  ? 0.1752 0.1790 0.2012 0.0065  -0.0161 -0.0172 848  ARG B CB  
15318 C CG  . ARG B 850  ? 0.1687 0.1737 0.1961 0.0073  -0.0140 -0.0170 848  ARG B CG  
15319 C CD  . ARG B 850  ? 0.1663 0.1725 0.1949 0.0082  -0.0138 -0.0164 848  ARG B CD  
15320 N NE  . ARG B 850  ? 0.1748 0.1820 0.2046 0.0090  -0.0119 -0.0163 848  ARG B NE  
15321 C CZ  . ARG B 850  ? 0.1740 0.1817 0.2042 0.0100  -0.0112 -0.0160 848  ARG B CZ  
15322 N NH1 . ARG B 850  ? 0.1825 0.1894 0.2120 0.0104  -0.0123 -0.0158 848  ARG B NH1 
15323 N NH2 . ARG B 850  ? 0.1797 0.1882 0.2107 0.0106  -0.0095 -0.0160 848  ARG B NH2 
15324 N N   . VAL B 851  ? 0.1876 0.1864 0.2052 0.0054  -0.0187 -0.0188 849  VAL B N   
15325 C CA  . VAL B 851  ? 0.1906 0.1878 0.2061 0.0045  -0.0205 -0.0193 849  VAL B CA  
15326 C C   . VAL B 851  ? 0.1882 0.1834 0.1989 0.0048  -0.0201 -0.0201 849  VAL B C   
15327 O O   . VAL B 851  ? 0.1937 0.1879 0.2027 0.0051  -0.0187 -0.0209 849  VAL B O   
15328 C CB  . VAL B 851  ? 0.2082 0.2046 0.2247 0.0037  -0.0210 -0.0198 849  VAL B CB  
15329 C CG1 . VAL B 851  ? 0.2281 0.2224 0.2420 0.0026  -0.0232 -0.0205 849  VAL B CG1 
15330 C CG2 . VAL B 851  ? 0.2332 0.2321 0.2547 0.0033  -0.0210 -0.0189 849  VAL B CG2 
15331 N N   . LEU B 852  ? 0.1840 0.1786 0.1925 0.0047  -0.0214 -0.0199 850  LEU B N   
15332 C CA  . LEU B 852  ? 0.1948 0.1876 0.1985 0.0048  -0.0211 -0.0206 850  LEU B CA  
15333 C C   . LEU B 852  ? 0.1885 0.1793 0.1895 0.0040  -0.0227 -0.0215 850  LEU B C   
15334 O O   . LEU B 852  ? 0.1923 0.1830 0.1938 0.0033  -0.0249 -0.0211 850  LEU B O   
15335 C CB  . LEU B 852  ? 0.1949 0.1881 0.1976 0.0050  -0.0215 -0.0196 850  LEU B CB  
15336 C CG  . LEU B 852  ? 0.1935 0.1851 0.1911 0.0049  -0.0212 -0.0200 850  LEU B CG  
15337 C CD1 . LEU B 852  ? 0.2134 0.2052 0.2097 0.0054  -0.0189 -0.0207 850  LEU B CD1 
15338 C CD2 . LEU B 852  ? 0.2211 0.2128 0.2179 0.0049  -0.0218 -0.0189 850  LEU B CD2 
15339 N N   . CYS B 853  ? 0.1894 0.1785 0.1875 0.0042  -0.0218 -0.0227 851  CYS B N   
15340 C CA  . CYS B 853  ? 0.1971 0.1836 0.1921 0.0035  -0.0231 -0.0238 851  CYS B CA  
15341 C C   . CYS B 853  ? 0.1912 0.1763 0.1810 0.0039  -0.0228 -0.0244 851  CYS B C   
15342 O O   . CYS B 853  ? 0.2032 0.1883 0.1912 0.0047  -0.0207 -0.0249 851  CYS B O   
15343 C CB  . CYS B 853  ? 0.2077 0.1927 0.2029 0.0037  -0.0223 -0.0249 851  CYS B CB  
15344 S SG  . CYS B 853  ? 0.2338 0.2207 0.2350 0.0033  -0.0222 -0.0239 851  CYS B SG  
15345 N N   . LEU B 854  ? 0.1991 0.1833 0.1865 0.0031  -0.0248 -0.0244 852  LEU B N   
15346 C CA  . LEU B 854  ? 0.2219 0.2051 0.2043 0.0033  -0.0245 -0.0246 852  LEU B CA  
15347 C C   . LEU B 854  ? 0.2141 0.1943 0.1920 0.0029  -0.0257 -0.0261 852  LEU B C   
15348 O O   . LEU B 854  ? 0.2156 0.1947 0.1939 0.0018  -0.0281 -0.0263 852  LEU B O   
15349 C CB  . LEU B 854  ? 0.2311 0.2152 0.2135 0.0029  -0.0260 -0.0232 852  LEU B CB  
15350 C CG  . LEU B 854  ? 0.2098 0.1963 0.1962 0.0034  -0.0250 -0.0218 852  LEU B CG  
15351 C CD1 . LEU B 854  ? 0.2406 0.2275 0.2269 0.0031  -0.0267 -0.0204 852  LEU B CD1 
15352 C CD2 . LEU B 854  ? 0.2433 0.2304 0.2283 0.0041  -0.0223 -0.0218 852  LEU B CD2 
15353 N N   . GLN B 855  ? 0.2230 0.2020 0.1967 0.0036  -0.0241 -0.0272 853  GLN B N   
15354 C CA  . GLN B 855  ? 0.2213 0.1971 0.1900 0.0033  -0.0252 -0.0288 853  GLN B CA  
15355 C C   . GLN B 855  ? 0.2569 0.2321 0.2231 0.0022  -0.0277 -0.0282 853  GLN B C   
15356 O O   . GLN B 855  ? 0.2447 0.2216 0.2109 0.0022  -0.0276 -0.0268 853  GLN B O   
15357 C CB  . GLN B 855  ? 0.2373 0.2123 0.2016 0.0045  -0.0228 -0.0299 853  GLN B CB  
15358 C CG  . GLN B 855  ? 0.2700 0.2412 0.2293 0.0046  -0.0235 -0.0319 853  GLN B CG  
15359 C CD  . GLN B 855  ? 0.3421 0.3129 0.2973 0.0061  -0.0210 -0.0331 853  GLN B CD  
15360 O OE1 . GLN B 855  ? 0.3453 0.3180 0.3026 0.0073  -0.0186 -0.0329 853  GLN B OE1 
15361 N NE2 . GLN B 855  ? 0.3697 0.3381 0.3190 0.0061  -0.0215 -0.0343 853  GLN B NE2 
15362 N N   . GLU B 856  ? 0.2516 0.2244 0.2159 0.0012  -0.0300 -0.0292 854  GLU B N   
15363 C CA  . GLU B 856  ? 0.2751 0.2477 0.2382 0.0000  -0.0329 -0.0284 854  GLU B CA  
15364 C C   . GLU B 856  ? 0.2680 0.2406 0.2263 0.0003  -0.0326 -0.0279 854  GLU B C   
15365 O O   . GLU B 856  ? 0.2995 0.2733 0.2584 -0.0002 -0.0341 -0.0263 854  GLU B O   
15366 C CB  . GLU B 856  ? 0.3498 0.3193 0.3104 -0.0011 -0.0354 -0.0299 854  GLU B CB  
15367 N N   . ASP B 857  ? 0.2775 0.2488 0.2312 0.0011  -0.0305 -0.0291 855  ASP B N   
15368 C CA  . ASP B 857  ? 0.3187 0.2897 0.2671 0.0012  -0.0302 -0.0287 855  ASP B CA  
15369 C C   . ASP B 857  ? 0.3046 0.2784 0.2551 0.0015  -0.0288 -0.0267 855  ASP B C   
15370 O O   . ASP B 857  ? 0.3381 0.3119 0.2851 0.0011  -0.0292 -0.0257 855  ASP B O   
15371 C CB  . ASP B 857  ? 0.4073 0.3764 0.3502 0.0021  -0.0281 -0.0306 855  ASP B CB  
15372 N N   . VAL B 858  ? 0.2463 0.2223 0.2020 0.0021  -0.0272 -0.0260 856  VAL B N   
15373 C CA  . VAL B 858  ? 0.2548 0.2332 0.2125 0.0023  -0.0259 -0.0242 856  VAL B CA  
15374 C C   . VAL B 858  ? 0.2128 0.1927 0.1760 0.0020  -0.0274 -0.0227 856  VAL B C   
15375 O O   . VAL B 858  ? 0.2411 0.2225 0.2060 0.0021  -0.0266 -0.0212 856  VAL B O   
15376 C CB  . VAL B 858  ? 0.2524 0.2324 0.2111 0.0033  -0.0226 -0.0245 856  VAL B CB  
15377 C CG1 . VAL B 858  ? 0.3065 0.2856 0.2596 0.0038  -0.0210 -0.0257 856  VAL B CG1 
15378 C CG2 . VAL B 858  ? 0.2605 0.2410 0.2236 0.0039  -0.0220 -0.0253 856  VAL B CG2 
15379 N N   . ALA B 859  ? 0.2299 0.2095 0.1959 0.0015  -0.0293 -0.0231 857  ALA B N   
15380 C CA  . ALA B 859  ? 0.2413 0.2227 0.2131 0.0015  -0.0303 -0.0218 857  ALA B CA  
15381 C C   . ALA B 859  ? 0.2402 0.2222 0.2120 0.0013  -0.0317 -0.0200 857  ALA B C   
15382 O O   . ALA B 859  ? 0.2445 0.2281 0.2197 0.0018  -0.0309 -0.0187 857  ALA B O   
15383 C CB  . ALA B 859  ? 0.2409 0.2221 0.2154 0.0009  -0.0323 -0.0224 857  ALA B CB  
15384 N N   . ASP B 860  ? 0.2538 0.2344 0.2217 0.0006  -0.0338 -0.0198 858  ASP B N   
15385 C CA  . ASP B 860  ? 0.2533 0.2342 0.2211 0.0005  -0.0355 -0.0179 858  ASP B CA  
15386 C C   . ASP B 860  ? 0.2556 0.2367 0.2221 0.0009  -0.0335 -0.0168 858  ASP B C   
15387 O O   . ASP B 860  ? 0.2529 0.2348 0.2221 0.0013  -0.0338 -0.0152 858  ASP B O   
15388 C CB  . ASP B 860  ? 0.2523 0.2315 0.2154 -0.0003 -0.0381 -0.0179 858  ASP B CB  
15389 C CG  . ASP B 860  ? 0.3497 0.3289 0.3147 -0.0010 -0.0408 -0.0185 858  ASP B CG  
15390 O OD1 . ASP B 860  ? 0.3858 0.3670 0.3567 -0.0008 -0.0413 -0.0181 858  ASP B OD1 
15391 O OD2 . ASP B 860  ? 0.4087 0.3860 0.3691 -0.0019 -0.0425 -0.0194 858  ASP B OD2 
15392 N N   . ARG B 861  ? 0.2350 0.2153 0.1972 0.0009  -0.0314 -0.0175 859  ARG B N   
15393 C CA  . ARG B 861  ? 0.2645 0.2453 0.2254 0.0010  -0.0295 -0.0164 859  ARG B CA  
15394 C C   . ARG B 861  ? 0.2321 0.2145 0.1980 0.0016  -0.0277 -0.0161 859  ARG B C   
15395 O O   . ARG B 861  ? 0.2474 0.2301 0.2144 0.0016  -0.0274 -0.0146 859  ARG B O   
15396 C CB  . ARG B 861  ? 0.3026 0.2827 0.2581 0.0008  -0.0276 -0.0172 859  ARG B CB  
15397 C CG  . ARG B 861  ? 0.4137 0.3945 0.3679 0.0006  -0.0257 -0.0159 859  ARG B CG  
15398 C CD  . ARG B 861  ? 0.4795 0.4600 0.4281 0.0003  -0.0241 -0.0164 859  ARG B CD  
15399 N NE  . ARG B 861  ? 0.6060 0.5877 0.5544 -0.0001 -0.0220 -0.0151 859  ARG B NE  
15400 C CZ  . ARG B 861  ? 0.5508 0.5344 0.5009 0.0003  -0.0193 -0.0157 859  ARG B CZ  
15401 N NH1 . ARG B 861  ? 0.5085 0.4929 0.4604 0.0012  -0.0183 -0.0175 859  ARG B NH1 
15402 N NH2 . ARG B 861  ? 0.5543 0.5391 0.5045 -0.0003 -0.0177 -0.0144 859  ARG B NH2 
15403 N N   . ILE B 862  ? 0.2171 0.2004 0.1859 0.0021  -0.0266 -0.0174 860  ILE B N   
15404 C CA  . ILE B 862  ? 0.2210 0.2060 0.1944 0.0026  -0.0249 -0.0171 860  ILE B CA  
15405 C C   . ILE B 862  ? 0.2065 0.1920 0.1842 0.0029  -0.0265 -0.0160 860  ILE B C   
15406 O O   . ILE B 862  ? 0.2237 0.2097 0.2034 0.0032  -0.0256 -0.0150 860  ILE B O   
15407 C CB  . ILE B 862  ? 0.2231 0.2089 0.1984 0.0031  -0.0235 -0.0187 860  ILE B CB  
15408 C CG1 . ILE B 862  ? 0.2664 0.2521 0.2377 0.0032  -0.0214 -0.0196 860  ILE B CG1 
15409 C CG2 . ILE B 862  ? 0.2108 0.1983 0.1912 0.0036  -0.0223 -0.0184 860  ILE B CG2 
15410 C CD1 . ILE B 862  ? 0.2960 0.2818 0.2681 0.0038  -0.0202 -0.0213 860  ILE B CD1 
15411 N N   . LEU B 863  ? 0.2214 0.2069 0.2005 0.0028  -0.0288 -0.0160 861  LEU B N   
15412 C CA  . LEU B 863  ? 0.2287 0.2152 0.2122 0.0033  -0.0302 -0.0149 861  LEU B CA  
15413 C C   . LEU B 863  ? 0.2540 0.2395 0.2361 0.0034  -0.0311 -0.0132 861  LEU B C   
15414 O O   . LEU B 863  ? 0.2297 0.2157 0.2149 0.0041  -0.0310 -0.0122 861  LEU B O   
15415 C CB  . LEU B 863  ? 0.2352 0.2221 0.2206 0.0029  -0.0326 -0.0152 861  LEU B CB  
15416 C CG  . LEU B 863  ? 0.2506 0.2385 0.2387 0.0029  -0.0317 -0.0166 861  LEU B CG  
15417 C CD1 . LEU B 863  ? 0.2853 0.2732 0.2741 0.0021  -0.0343 -0.0170 861  LEU B CD1 
15418 C CD2 . LEU B 863  ? 0.2710 0.2608 0.2643 0.0037  -0.0302 -0.0162 861  LEU B CD2 
15419 N N   . THR B 864  ? 0.2280 0.2119 0.2050 0.0027  -0.0320 -0.0128 862  THR B N   
15420 C CA  . THR B 864  ? 0.2563 0.2389 0.2315 0.0028  -0.0329 -0.0110 862  THR B CA  
15421 C C   . THR B 864  ? 0.2451 0.2275 0.2205 0.0029  -0.0305 -0.0105 862  THR B C   
15422 O O   . THR B 864  ? 0.2520 0.2338 0.2291 0.0034  -0.0309 -0.0092 862  THR B O   
15423 C CB  . THR B 864  ? 0.2836 0.2646 0.2529 0.0019  -0.0340 -0.0107 862  THR B CB  
15424 O OG1 . THR B 864  ? 0.3194 0.3003 0.2884 0.0017  -0.0366 -0.0111 862  THR B OG1 
15425 C CG2 . THR B 864  ? 0.3229 0.3021 0.2896 0.0018  -0.0346 -0.0087 862  THR B CG2 
15426 N N   . MET B 865  ? 0.2212 0.2041 0.1951 0.0025  -0.0282 -0.0115 863  MET B N   
15427 C CA  . MET B 865  ? 0.2353 0.2182 0.2093 0.0024  -0.0260 -0.0111 863  MET B CA  
15428 C C   . MET B 865  ? 0.2267 0.2107 0.2060 0.0032  -0.0254 -0.0112 863  MET B C   
15429 O O   . MET B 865  ? 0.2245 0.2077 0.2046 0.0034  -0.0248 -0.0103 863  MET B O   
15430 C CB  . MET B 865  ? 0.2380 0.2218 0.2097 0.0019  -0.0237 -0.0122 863  MET B CB  
15431 C CG  . MET B 865  ? 0.2560 0.2402 0.2275 0.0014  -0.0217 -0.0116 863  MET B CG  
15432 S SD  . MET B 865  ? 0.2776 0.2635 0.2467 0.0010  -0.0190 -0.0128 863  MET B SD  
15433 C CE  . MET B 865  ? 0.3266 0.3113 0.2896 0.0003  -0.0199 -0.0125 863  MET B CE  
15434 N N   . LEU B 866  ? 0.2196 0.2051 0.2022 0.0038  -0.0254 -0.0124 864  LEU B N   
15435 C CA  . LEU B 866  ? 0.2124 0.1991 0.1999 0.0046  -0.0247 -0.0125 864  LEU B CA  
15436 C C   . LEU B 866  ? 0.2131 0.1992 0.2027 0.0054  -0.0262 -0.0112 864  LEU B C   
15437 O O   . LEU B 866  ? 0.2098 0.1955 0.2012 0.0059  -0.0254 -0.0107 864  LEU B O   
15438 C CB  . LEU B 866  ? 0.2266 0.2150 0.2170 0.0049  -0.0247 -0.0137 864  LEU B CB  
15439 C CG  . LEU B 866  ? 0.1941 0.1839 0.1895 0.0058  -0.0241 -0.0138 864  LEU B CG  
15440 C CD1 . LEU B 866  ? 0.2293 0.2194 0.2251 0.0059  -0.0218 -0.0140 864  LEU B CD1 
15441 C CD2 . LEU B 866  ? 0.2449 0.2362 0.2427 0.0057  -0.0243 -0.0149 864  LEU B CD2 
15442 N N   . LYS B 867  ? 0.2162 0.2020 0.2054 0.0055  -0.0286 -0.0106 865  LYS B N   
15443 C CA  . LYS B 867  ? 0.2223 0.2077 0.2138 0.0065  -0.0302 -0.0093 865  LYS B CA  
15444 C C   . LYS B 867  ? 0.2231 0.2060 0.2119 0.0064  -0.0301 -0.0080 865  LYS B C   
15445 O O   . LYS B 867  ? 0.2265 0.2087 0.2175 0.0075  -0.0300 -0.0073 865  LYS B O   
15446 C CB  . LYS B 867  ? 0.2521 0.2380 0.2439 0.0065  -0.0329 -0.0089 865  LYS B CB  
15447 C CG  . LYS B 867  ? 0.2631 0.2515 0.2586 0.0065  -0.0332 -0.0100 865  LYS B CG  
15448 C CD  . LYS B 867  ? 0.2939 0.2828 0.2888 0.0059  -0.0359 -0.0099 865  LYS B CD  
15449 C CE  . LYS B 867  ? 0.3932 0.3842 0.3914 0.0055  -0.0359 -0.0112 865  LYS B CE  
15450 N NZ  . LYS B 867  ? 0.4262 0.4174 0.4232 0.0046  -0.0386 -0.0113 865  LYS B NZ  
15451 N N   . GLY B 868  ? 0.2344 0.2157 0.2183 0.0052  -0.0298 -0.0077 866  GLY B N   
15452 C CA  . GLY B 868  ? 0.2423 0.2211 0.2235 0.0049  -0.0295 -0.0064 866  GLY B CA  
15453 C C   . GLY B 868  ? 0.2281 0.2067 0.2107 0.0049  -0.0273 -0.0067 866  GLY B C   
15454 O O   . GLY B 868  ? 0.2521 0.2286 0.2348 0.0053  -0.0274 -0.0057 866  GLY B O   
15455 N N   . ALA B 869  ? 0.2328 0.2134 0.2164 0.0045  -0.0254 -0.0081 867  ALA B N   
15456 C CA  . ALA B 869  ? 0.2214 0.2022 0.2065 0.0045  -0.0234 -0.0085 867  ALA B CA  
15457 C C   . ALA B 869  ? 0.2010 0.1819 0.1904 0.0060  -0.0236 -0.0086 867  ALA B C   
15458 O O   . ALA B 869  ? 0.2208 0.2003 0.2107 0.0062  -0.0229 -0.0083 867  ALA B O   
15459 C CB  . ALA B 869  ? 0.2281 0.2112 0.2134 0.0039  -0.0215 -0.0099 867  ALA B CB  
15460 N N   . LEU B 870  ? 0.1992 0.1819 0.1918 0.0070  -0.0246 -0.0091 868  LEU B N   
15461 C CA  . LEU B 870  ? 0.2132 0.1966 0.2101 0.0085  -0.0247 -0.0091 868  LEU B CA  
15462 C C   . LEU B 870  ? 0.2226 0.2035 0.2192 0.0095  -0.0260 -0.0078 868  LEU B C   
15463 O O   . LEU B 870  ? 0.2335 0.2138 0.2324 0.0107  -0.0254 -0.0078 868  LEU B O   
15464 C CB  . LEU B 870  ? 0.2313 0.2174 0.2317 0.0092  -0.0257 -0.0096 868  LEU B CB  
15465 C CG  . LEU B 870  ? 0.2405 0.2288 0.2421 0.0086  -0.0242 -0.0110 868  LEU B CG  
15466 C CD1 . LEU B 870  ? 0.2597 0.2502 0.2643 0.0089  -0.0255 -0.0113 868  LEU B CD1 
15467 C CD2 . LEU B 870  ? 0.2564 0.2453 0.2603 0.0092  -0.0221 -0.0116 868  LEU B CD2 
15468 N N   . HIS B 871  ? 0.2172 0.1964 0.2110 0.0091  -0.0277 -0.0066 869  HIS B N   
15469 C CA  A HIS B 871  ? 0.2312 0.2076 0.2244 0.0101  -0.0290 -0.0052 869  HIS B CA  
15470 C CA  B HIS B 871  ? 0.2314 0.2077 0.2244 0.0101  -0.0291 -0.0052 869  HIS B CA  
15471 C C   . HIS B 871  ? 0.2569 0.2302 0.2481 0.0097  -0.0278 -0.0049 869  HIS B C   
15472 O O   . HIS B 871  ? 0.2642 0.2348 0.2555 0.0109  -0.0285 -0.0040 869  HIS B O   
15473 C CB  A HIS B 871  ? 0.2494 0.2246 0.2396 0.0097  -0.0313 -0.0039 869  HIS B CB  
15474 C CB  B HIS B 871  ? 0.2461 0.2211 0.2357 0.0094  -0.0311 -0.0039 869  HIS B CB  
15475 C CG  A HIS B 871  ? 0.2827 0.2602 0.2759 0.0108  -0.0334 -0.0037 869  HIS B CG  
15476 C CG  B HIS B 871  ? 0.2803 0.2524 0.2692 0.0105  -0.0329 -0.0022 869  HIS B CG  
15477 N ND1 A HIS B 871  ? 0.3213 0.3013 0.3147 0.0100  -0.0339 -0.0045 869  HIS B ND1 
15478 N ND1 B HIS B 871  ? 0.3339 0.3069 0.3264 0.0125  -0.0345 -0.0017 869  HIS B ND1 
15479 C CD2 A HIS B 871  ? 0.3321 0.3097 0.3282 0.0126  -0.0350 -0.0027 869  HIS B CD2 
15480 C CD2 B HIS B 871  ? 0.3141 0.2824 0.2992 0.0100  -0.0333 -0.0008 869  HIS B CD2 
15481 C CE1 A HIS B 871  ? 0.3294 0.3111 0.3258 0.0110  -0.0360 -0.0040 869  HIS B CE1 
15482 C CE1 B HIS B 871  ? 0.3150 0.2847 0.3059 0.0134  -0.0358 -0.0001 869  HIS B CE1 
15483 N NE2 A HIS B 871  ? 0.2876 0.2683 0.2859 0.0127  -0.0366 -0.0029 869  HIS B NE2 
15484 N NE2 B HIS B 871  ? 0.3398 0.3063 0.3260 0.0118  -0.0352 0.0005  869  HIS B NE2 
15485 N N   . GLU B 872  ? 0.2092 0.1827 0.1985 0.0082  -0.0259 -0.0056 870  GLU B N   
15486 C CA  . GLU B 872  ? 0.2310 0.2018 0.2183 0.0074  -0.0248 -0.0053 870  GLU B CA  
15487 C C   . GLU B 872  ? 0.2168 0.1880 0.2069 0.0081  -0.0232 -0.0065 870  GLU B C   
15488 O O   . GLU B 872  ? 0.2468 0.2157 0.2353 0.0074  -0.0223 -0.0064 870  GLU B O   
15489 C CB  . GLU B 872  ? 0.2400 0.2109 0.2236 0.0051  -0.0238 -0.0052 870  GLU B CB  
15490 C CG  . GLU B 872  ? 0.2346 0.2048 0.2147 0.0043  -0.0252 -0.0041 870  GLU B CG  
15491 C CD  . GLU B 872  ? 0.2765 0.2427 0.2544 0.0045  -0.0268 -0.0023 870  GLU B CD  
15492 O OE1 . GLU B 872  ? 0.2987 0.2621 0.2765 0.0047  -0.0264 -0.0019 870  GLU B OE1 
15493 O OE2 . GLU B 872  ? 0.2987 0.2643 0.2747 0.0046  -0.0286 -0.0013 870  GLU B OE2 
15494 N N   . LEU B 873  ? 0.2194 0.1936 0.2135 0.0094  -0.0229 -0.0075 871  LEU B N   
15495 C CA  . LEU B 873  ? 0.2214 0.1962 0.2178 0.0101  -0.0213 -0.0086 871  LEU B CA  
15496 C C   . LEU B 873  ? 0.2268 0.1994 0.2248 0.0121  -0.0218 -0.0082 871  LEU B C   
15497 O O   . LEU B 873  ? 0.2654 0.2376 0.2645 0.0135  -0.0234 -0.0074 871  LEU B O   
15498 C CB  . LEU B 873  ? 0.2321 0.2111 0.2321 0.0107  -0.0206 -0.0097 871  LEU B CB  
15499 C CG  . LEU B 873  ? 0.2450 0.2262 0.2438 0.0091  -0.0199 -0.0103 871  LEU B CG  
15500 C CD1 . LEU B 873  ? 0.2824 0.2670 0.2847 0.0097  -0.0191 -0.0114 871  LEU B CD1 
15501 C CD2 . LEU B 873  ? 0.2481 0.2283 0.2441 0.0075  -0.0185 -0.0105 871  LEU B CD2 
15502 N N   . HIS B 874  ? 0.2228 0.1939 0.2207 0.0122  -0.0204 -0.0089 872  HIS B N   
15503 C CA  . HIS B 874  ? 0.2510 0.2197 0.2501 0.0142  -0.0205 -0.0089 872  HIS B CA  
15504 C C   . HIS B 874  ? 0.2234 0.1953 0.2265 0.0156  -0.0192 -0.0102 872  HIS B C   
15505 O O   . HIS B 874  ? 0.2179 0.1912 0.2209 0.0146  -0.0176 -0.0112 872  HIS B O   
15506 C CB  . HIS B 874  ? 0.2600 0.2243 0.2557 0.0132  -0.0200 -0.0089 872  HIS B CB  
15507 C CG  . HIS B 874  ? 0.2712 0.2320 0.2672 0.0152  -0.0200 -0.0091 872  HIS B CG  
15508 N ND1 . HIS B 874  ? 0.3428 0.2989 0.3357 0.0145  -0.0197 -0.0092 872  HIS B ND1 
15509 C CD2 . HIS B 874  ? 0.3466 0.3080 0.3458 0.0180  -0.0202 -0.0093 872  HIS B CD2 
15510 C CE1 . HIS B 874  ? 0.3585 0.3120 0.3523 0.0168  -0.0197 -0.0095 872  HIS B CE1 
15511 N NE2 . HIS B 874  ? 0.3531 0.3099 0.3508 0.0190  -0.0199 -0.0096 872  HIS B NE2 
15512 N N   . ILE B 875  ? 0.2288 0.2021 0.2352 0.0178  -0.0198 -0.0100 873  ILE B N   
15513 C CA  . ILE B 875  ? 0.2229 0.1995 0.2333 0.0193  -0.0185 -0.0109 873  ILE B CA  
15514 C C   . ILE B 875  ? 0.2313 0.2052 0.2421 0.0214  -0.0180 -0.0112 873  ILE B C   
15515 O O   . ILE B 875  ? 0.2524 0.2239 0.2630 0.0229  -0.0193 -0.0103 873  ILE B O   
15516 C CB  . ILE B 875  ? 0.2480 0.2286 0.2623 0.0202  -0.0196 -0.0104 873  ILE B CB  
15517 C CG1 . ILE B 875  ? 0.2745 0.2572 0.2880 0.0182  -0.0204 -0.0102 873  ILE B CG1 
15518 C CG2 . ILE B 875  ? 0.2628 0.2470 0.2813 0.0216  -0.0181 -0.0113 873  ILE B CG2 
15519 C CD1 . ILE B 875  ? 0.3407 0.3258 0.3566 0.0188  -0.0223 -0.0093 873  ILE B CD1 
15520 N N   . GLY B 876  ? 0.2142 0.1882 0.2252 0.0216  -0.0161 -0.0125 874  GLY B N   
15521 C CA  . GLY B 876  ? 0.2275 0.1987 0.2385 0.0238  -0.0155 -0.0129 874  GLY B CA  
15522 C C   . GLY B 876  ? 0.2203 0.1917 0.2309 0.0236  -0.0134 -0.0144 874  GLY B C   
15523 O O   . GLY B 876  ? 0.2185 0.1927 0.2295 0.0221  -0.0125 -0.0149 874  GLY B O   
15524 N N   . ARG B 877  ? 0.2471 0.2152 0.2568 0.0254  -0.0128 -0.0150 875  ARG B N   
15525 C CA  . ARG B 877  ? 0.2374 0.2048 0.2459 0.0253  -0.0110 -0.0165 875  ARG B CA  
15526 C C   . ARG B 877  ? 0.2315 0.1968 0.2361 0.0223  -0.0110 -0.0167 875  ARG B C   
15527 O O   . ARG B 877  ? 0.2532 0.2148 0.2548 0.0210  -0.0122 -0.0161 875  ARG B O   
15528 C CB  . ARG B 877  ? 0.2713 0.2344 0.2786 0.0278  -0.0105 -0.0171 875  ARG B CB  
15529 C CG  . ARG B 877  ? 0.2958 0.2591 0.3028 0.0284  -0.0085 -0.0187 875  ARG B CG  
15530 C CD  . ARG B 877  ? 0.3450 0.3041 0.3510 0.0313  -0.0081 -0.0194 875  ARG B CD  
15531 N NE  . ARG B 877  ? 0.3281 0.2804 0.3289 0.0302  -0.0087 -0.0198 875  ARG B NE  
15532 C CZ  . ARG B 877  ? 0.3942 0.3416 0.3930 0.0323  -0.0083 -0.0207 875  ARG B CZ  
15533 N NH1 . ARG B 877  ? 0.3552 0.3037 0.3566 0.0358  -0.0073 -0.0212 875  ARG B NH1 
15534 N NH2 . ARG B 877  ? 0.4173 0.3583 0.4111 0.0308  -0.0089 -0.0212 875  ARG B NH2 
15535 N N   . THR B 878  ? 0.2210 0.1889 0.2258 0.0211  -0.0096 -0.0176 876  THR B N   
15536 C CA  . THR B 878  ? 0.2458 0.2137 0.2481 0.0181  -0.0097 -0.0176 876  THR B CA  
15537 C C   . THR B 878  ? 0.2190 0.1824 0.2172 0.0169  -0.0095 -0.0183 876  THR B C   
15538 O O   . THR B 878  ? 0.2391 0.2029 0.2354 0.0144  -0.0094 -0.0184 876  THR B O   
15539 C CB  . THR B 878  ? 0.2322 0.2050 0.2366 0.0174  -0.0085 -0.0181 876  THR B CB  
15540 O OG1 . THR B 878  ? 0.2768 0.2505 0.2824 0.0190  -0.0070 -0.0191 876  THR B OG1 
15541 C CG2 . THR B 878  ? 0.2642 0.2411 0.2719 0.0177  -0.0091 -0.0173 876  THR B CG2 
15542 N N   . ASP B 879  ? 0.2209 0.1799 0.2175 0.0184  -0.0095 -0.0189 877  ASP B N   
15543 C CA  . ASP B 879  ? 0.2278 0.1819 0.2202 0.0171  -0.0095 -0.0196 877  ASP B CA  
15544 C C   . ASP B 879  ? 0.2487 0.1984 0.2381 0.0155  -0.0111 -0.0185 877  ASP B C   
15545 O O   . ASP B 879  ? 0.2656 0.2099 0.2516 0.0150  -0.0115 -0.0189 877  ASP B O   
15546 C CB  . ASP B 879  ? 0.2573 0.2081 0.2489 0.0195  -0.0086 -0.0209 877  ASP B CB  
15547 C CG  . ASP B 879  ? 0.2962 0.2442 0.2885 0.0223  -0.0093 -0.0204 877  ASP B CG  
15548 O OD1 . ASP B 879  ? 0.3269 0.2776 0.3222 0.0231  -0.0100 -0.0192 877  ASP B OD1 
15549 O OD2 . ASP B 879  ? 0.3095 0.2524 0.2994 0.0237  -0.0091 -0.0213 877  ASP B OD2 
15550 N N   . ARG B 880  ? 0.2596 0.2116 0.2501 0.0146  -0.0120 -0.0171 878  ARG B N   
15551 C CA  . ARG B 880  ? 0.2622 0.2110 0.2498 0.0125  -0.0134 -0.0159 878  ARG B CA  
15552 C C   . ARG B 880  ? 0.2406 0.1939 0.2287 0.0100  -0.0133 -0.0153 878  ARG B C   
15553 O O   . ARG B 880  ? 0.2439 0.2019 0.2350 0.0107  -0.0130 -0.0152 878  ARG B O   
15554 C CB  . ARG B 880  ? 0.2936 0.2407 0.2818 0.0142  -0.0148 -0.0146 878  ARG B CB  
15555 C CG  . ARG B 880  ? 0.3774 0.3191 0.3646 0.0166  -0.0151 -0.0148 878  ARG B CG  
15556 C CD  . ARG B 880  ? 0.4248 0.3654 0.4128 0.0182  -0.0167 -0.0133 878  ARG B CD  
15557 N NE  . ARG B 880  ? 0.6378 0.5741 0.6257 0.0213  -0.0169 -0.0136 878  ARG B NE  
15558 C CZ  . ARG B 880  ? 0.6941 0.6238 0.6786 0.0214  -0.0180 -0.0130 878  ARG B CZ  
15559 N NH1 . ARG B 880  ? 0.6978 0.6243 0.6787 0.0184  -0.0190 -0.0120 878  ARG B NH1 
15560 N NH2 . ARG B 880  ? 0.6494 0.5755 0.6341 0.0246  -0.0181 -0.0135 878  ARG B NH2 
15561 N N   . LEU B 881  ? 0.2373 0.1889 0.2225 0.0072  -0.0136 -0.0149 879  LEU B N   
15562 C CA  . LEU B 881  ? 0.2347 0.1905 0.2202 0.0050  -0.0134 -0.0143 879  LEU B CA  
15563 C C   . LEU B 881  ? 0.2330 0.1907 0.2195 0.0054  -0.0142 -0.0130 879  LEU B C   
15564 O O   . LEU B 881  ? 0.2318 0.1940 0.2198 0.0047  -0.0138 -0.0129 879  LEU B O   
15565 C CB  . LEU B 881  ? 0.2363 0.1897 0.2185 0.0019  -0.0136 -0.0138 879  LEU B CB  
15566 C CG  . LEU B 881  ? 0.2555 0.2132 0.2377 -0.0005 -0.0133 -0.0132 879  LEU B CG  
15567 C CD1 . LEU B 881  ? 0.2940 0.2564 0.2784 -0.0005 -0.0120 -0.0143 879  LEU B CD1 
15568 C CD2 . LEU B 881  ? 0.2704 0.2252 0.2493 -0.0035 -0.0138 -0.0124 879  LEU B CD2 
15569 N N   . SER B 882  ? 0.2231 0.1772 0.2088 0.0065  -0.0154 -0.0121 880  SER B N   
15570 C CA  . SER B 882  ? 0.2262 0.1817 0.2124 0.0068  -0.0164 -0.0109 880  SER B CA  
15571 C C   . SER B 882  ? 0.2286 0.1884 0.2188 0.0090  -0.0163 -0.0113 880  SER B C   
15572 O O   . SER B 882  ? 0.2397 0.2010 0.2305 0.0092  -0.0172 -0.0104 880  SER B O   
15573 C CB  . SER B 882  ? 0.2361 0.1865 0.2202 0.0074  -0.0179 -0.0097 880  SER B CB  
15574 O OG  . SER B 882  ? 0.2855 0.2342 0.2714 0.0104  -0.0181 -0.0102 880  SER B OG  
15575 N N   . VAL B 883  ? 0.2226 0.1843 0.2154 0.0105  -0.0152 -0.0126 881  VAL B N   
15576 C CA  . VAL B 883  ? 0.2248 0.1905 0.2214 0.0123  -0.0151 -0.0128 881  VAL B CA  
15577 C C   . VAL B 883  ? 0.2368 0.2071 0.2346 0.0110  -0.0143 -0.0132 881  VAL B C   
15578 O O   . VAL B 883  ? 0.2597 0.2311 0.2569 0.0098  -0.0131 -0.0139 881  VAL B O   
15579 C CB  . VAL B 883  ? 0.2484 0.2141 0.2473 0.0146  -0.0142 -0.0138 881  VAL B CB  
15580 C CG1 . VAL B 883  ? 0.2453 0.2159 0.2484 0.0160  -0.0138 -0.0141 881  VAL B CG1 
15581 C CG2 . VAL B 883  ? 0.2746 0.2359 0.2727 0.0165  -0.0151 -0.0134 881  VAL B CG2 
15582 N N   . ASP B 884  ? 0.2157 0.1887 0.2151 0.0112  -0.0150 -0.0126 882  ASP B N   
15583 C CA  . ASP B 884  ? 0.2196 0.1965 0.2199 0.0102  -0.0145 -0.0130 882  ASP B CA  
15584 C C   . ASP B 884  ? 0.2508 0.2311 0.2549 0.0116  -0.0138 -0.0137 882  ASP B C   
15585 O O   . ASP B 884  ? 0.3046 0.2876 0.3096 0.0109  -0.0127 -0.0144 882  ASP B O   
15586 C CB  . ASP B 884  ? 0.2376 0.2149 0.2368 0.0095  -0.0158 -0.0120 882  ASP B CB  
15587 C CG  . ASP B 884  ? 0.2295 0.2036 0.2247 0.0079  -0.0163 -0.0111 882  ASP B CG  
15588 O OD1 . ASP B 884  ? 0.2421 0.2160 0.2356 0.0063  -0.0154 -0.0113 882  ASP B OD1 
15589 O OD2 . ASP B 884  ? 0.2313 0.2032 0.2254 0.0083  -0.0178 -0.0100 882  ASP B OD2 
15590 N N   . VAL B 885  ? 0.2193 0.1999 0.2259 0.0135  -0.0145 -0.0134 883  VAL B N   
15591 C CA  . VAL B 885  ? 0.2143 0.1985 0.2249 0.0146  -0.0141 -0.0139 883  VAL B CA  
15592 C C   . VAL B 885  ? 0.1977 0.1812 0.2101 0.0167  -0.0135 -0.0142 883  VAL B C   
15593 O O   . VAL B 885  ? 0.2150 0.1963 0.2274 0.0180  -0.0144 -0.0136 883  VAL B O   
15594 C CB  . VAL B 885  ? 0.2214 0.2074 0.2336 0.0149  -0.0156 -0.0131 883  VAL B CB  
15595 C CG1 . VAL B 885  ? 0.2456 0.2354 0.2621 0.0159  -0.0152 -0.0134 883  VAL B CG1 
15596 C CG2 . VAL B 885  ? 0.2859 0.2724 0.2958 0.0130  -0.0161 -0.0130 883  VAL B CG2 
15597 N N   . GLY B 886  ? 0.2041 0.1893 0.2180 0.0171  -0.0119 -0.0151 884  GLY B N   
15598 C CA  . GLY B 886  ? 0.1977 0.1827 0.2133 0.0191  -0.0109 -0.0155 884  GLY B CA  
15599 C C   . GLY B 886  ? 0.1908 0.1796 0.2109 0.0206  -0.0109 -0.0152 884  GLY B C   
15600 O O   . GLY B 886  ? 0.1941 0.1853 0.2160 0.0201  -0.0120 -0.0146 884  GLY B O   
15601 N N   . PRO B 887  ? 0.1967 0.1862 0.2187 0.0224  -0.0097 -0.0157 885  PRO B N   
15602 C CA  . PRO B 887  ? 0.1882 0.1816 0.2148 0.0240  -0.0095 -0.0153 885  PRO B CA  
15603 C C   . PRO B 887  ? 0.1674 0.1648 0.1963 0.0229  -0.0085 -0.0155 885  PRO B C   
15604 O O   . PRO B 887  ? 0.1878 0.1850 0.2147 0.0214  -0.0076 -0.0161 885  PRO B O   
15605 C CB  . PRO B 887  ? 0.1895 0.1816 0.2164 0.0262  -0.0080 -0.0160 885  PRO B CB  
15606 C CG  . PRO B 887  ? 0.2002 0.1894 0.2231 0.0251  -0.0069 -0.0170 885  PRO B CG  
15607 C CD  . PRO B 887  ? 0.2001 0.1866 0.2197 0.0230  -0.0083 -0.0167 885  PRO B CD  
15608 N N   . VAL B 888  ? 0.1789 0.1801 0.2120 0.0237  -0.0088 -0.0149 886  VAL B N   
15609 C CA  . VAL B 888  ? 0.1859 0.1908 0.2216 0.0231  -0.0075 -0.0150 886  VAL B CA  
15610 C C   . VAL B 888  ? 0.1744 0.1800 0.2110 0.0248  -0.0054 -0.0156 886  VAL B C   
15611 O O   . VAL B 888  ? 0.1840 0.1881 0.2204 0.0268  -0.0050 -0.0158 886  VAL B O   
15612 C CB  . VAL B 888  ? 0.2121 0.2210 0.2520 0.0229  -0.0087 -0.0141 886  VAL B CB  
15613 C CG1 . VAL B 888  ? 0.2190 0.2267 0.2573 0.0212  -0.0108 -0.0137 886  VAL B CG1 
15614 C CG2 . VAL B 888  ? 0.2974 0.3081 0.3408 0.0251  -0.0090 -0.0134 886  VAL B CG2 
15615 N N   . ILE B 889  ? 0.1729 0.1806 0.2100 0.0239  -0.0039 -0.0160 887  ILE B N   
15616 C CA  . ILE B 889  ? 0.1793 0.1866 0.2155 0.0250  -0.0018 -0.0168 887  ILE B CA  
15617 C C   . ILE B 889  ? 0.1991 0.2088 0.2387 0.0275  -0.0007 -0.0165 887  ILE B C   
15618 O O   . ILE B 889  ? 0.1894 0.1974 0.2276 0.0292  0.0006  -0.0173 887  ILE B O   
15619 C CB  . ILE B 889  ? 0.1797 0.1885 0.2152 0.0235  -0.0005 -0.0170 887  ILE B CB  
15620 C CG1 . ILE B 889  ? 0.1928 0.2006 0.2264 0.0245  0.0016  -0.0179 887  ILE B CG1 
15621 C CG2 . ILE B 889  ? 0.2097 0.2230 0.2495 0.0230  -0.0004 -0.0161 887  ILE B CG2 
15622 C CD1 . ILE B 889  ? 0.2024 0.2055 0.2315 0.0246  0.0014  -0.0189 887  ILE B CD1 
15623 N N   . THR B 890  ? 0.1673 0.1811 0.2115 0.0278  -0.0012 -0.0155 888  THR B N   
15624 C CA  . THR B 890  ? 0.1907 0.2077 0.2388 0.0301  -0.0001 -0.0152 888  THR B CA  
15625 C C   . THR B 890  ? 0.1836 0.2035 0.2360 0.0306  -0.0019 -0.0140 888  THR B C   
15626 O O   . THR B 890  ? 0.1873 0.2074 0.2399 0.0288  -0.0038 -0.0134 888  THR B O   
15627 C CB  . THR B 890  ? 0.1947 0.2159 0.2453 0.0298  0.0020  -0.0150 888  THR B CB  
15628 O OG1 . THR B 890  ? 0.2110 0.2347 0.2636 0.0275  0.0010  -0.0141 888  THR B OG1 
15629 C CG2 . THR B 890  ? 0.2183 0.2371 0.2649 0.0296  0.0039  -0.0161 888  THR B CG2 
15630 N N   . SER B 891  ? 0.1878 0.2103 0.2437 0.0331  -0.0011 -0.0136 889  SER B N   
15631 C CA  A SER B 891  ? 0.1883 0.2147 0.2491 0.0336  -0.0027 -0.0123 889  SER B CA  
15632 C CA  B SER B 891  ? 0.1880 0.2143 0.2488 0.0336  -0.0027 -0.0123 889  SER B CA  
15633 C CA  C SER B 891  ? 0.1882 0.2146 0.2491 0.0337  -0.0027 -0.0123 889  SER B CA  
15634 C C   . SER B 891  ? 0.1908 0.2219 0.2552 0.0314  -0.0030 -0.0114 889  SER B C   
15635 O O   . SER B 891  ? 0.2009 0.2337 0.2675 0.0303  -0.0052 -0.0105 889  SER B O   
15636 C CB  A SER B 891  ? 0.2144 0.2433 0.2787 0.0370  -0.0015 -0.0121 889  SER B CB  
15637 C CB  B SER B 891  ? 0.2148 0.2434 0.2789 0.0370  -0.0016 -0.0121 889  SER B CB  
15638 C CB  C SER B 891  ? 0.2144 0.2432 0.2786 0.0370  -0.0014 -0.0121 889  SER B CB  
15639 O OG  A SER B 891  ? 0.2248 0.2489 0.2858 0.0391  -0.0016 -0.0128 889  SER B OG  
15640 O OG  B SER B 891  ? 0.2261 0.2586 0.2927 0.0376  0.0010  -0.0121 889  SER B OG  
15641 O OG  C SER B 891  ? 0.2253 0.2581 0.2945 0.0378  -0.0031 -0.0107 889  SER B OG  
15642 N N   . GLU B 892  ? 0.1814 0.2144 0.2461 0.0307  -0.0009 -0.0116 890  GLU B N   
15643 C CA  . GLU B 892  ? 0.2040 0.2408 0.2717 0.0284  -0.0011 -0.0107 890  GLU B CA  
15644 C C   . GLU B 892  ? 0.1933 0.2274 0.2582 0.0257  -0.0032 -0.0109 890  GLU B C   
15645 O O   . GLU B 892  ? 0.2163 0.2527 0.2839 0.0241  -0.0049 -0.0100 890  GLU B O   
15646 C CB  . GLU B 892  ? 0.2348 0.2734 0.3025 0.0280  0.0016  -0.0110 890  GLU B CB  
15647 N N   . ALA B 893  ? 0.1884 0.2177 0.2481 0.0251  -0.0030 -0.0119 891  ALA B N   
15648 C CA  . ALA B 893  ? 0.1863 0.2129 0.2430 0.0229  -0.0048 -0.0121 891  ALA B CA  
15649 C C   . ALA B 893  ? 0.1901 0.2161 0.2474 0.0229  -0.0074 -0.0116 891  ALA B C   
15650 O O   . ALA B 893  ? 0.2000 0.2267 0.2579 0.0211  -0.0092 -0.0111 891  ALA B O   
15651 C CB  . ALA B 893  ? 0.2135 0.2355 0.2648 0.0225  -0.0041 -0.0132 891  ALA B CB  
15652 N N   . LYS B 894  ? 0.1833 0.2079 0.2402 0.0250  -0.0078 -0.0116 892  LYS B N   
15653 C CA  . LYS B 894  ? 0.2095 0.2335 0.2670 0.0252  -0.0103 -0.0109 892  LYS B CA  
15654 C C   . LYS B 894  ? 0.1986 0.2276 0.2613 0.0247  -0.0116 -0.0097 892  LYS B C   
15655 O O   . LYS B 894  ? 0.1936 0.2225 0.2562 0.0232  -0.0139 -0.0093 892  LYS B O   
15656 C CB  . LYS B 894  ? 0.1847 0.2067 0.2415 0.0279  -0.0102 -0.0110 892  LYS B CB  
15657 C CG  . LYS B 894  ? 0.1974 0.2189 0.2549 0.0285  -0.0128 -0.0101 892  LYS B CG  
15658 C CD  . LYS B 894  ? 0.2458 0.2643 0.3019 0.0312  -0.0126 -0.0102 892  LYS B CD  
15659 C CE  . LYS B 894  ? 0.3333 0.3524 0.3914 0.0325  -0.0150 -0.0090 892  LYS B CE  
15660 N NZ  . LYS B 894  ? 0.4721 0.4879 0.5265 0.0308  -0.0174 -0.0087 892  LYS B NZ  
15661 N N   . ASP B 895  ? 0.1902 0.2236 0.2575 0.0259  -0.0102 -0.0092 893  ASP B N   
15662 C CA  . ASP B 895  ? 0.1896 0.2284 0.2624 0.0252  -0.0114 -0.0080 893  ASP B CA  
15663 C C   . ASP B 895  ? 0.1812 0.2205 0.2538 0.0220  -0.0123 -0.0079 893  ASP B C   
15664 O O   . ASP B 895  ? 0.2080 0.2493 0.2829 0.0207  -0.0145 -0.0071 893  ASP B O   
15665 C CB  . ASP B 895  ? 0.2049 0.2485 0.2825 0.0269  -0.0092 -0.0074 893  ASP B CB  
15666 C CG  . ASP B 895  ? 0.2450 0.2890 0.3240 0.0303  -0.0087 -0.0074 893  ASP B CG  
15667 O OD1 . ASP B 895  ? 0.2847 0.3259 0.3620 0.0312  -0.0107 -0.0073 893  ASP B OD1 
15668 O OD2 . ASP B 895  ? 0.2798 0.3267 0.3613 0.0321  -0.0064 -0.0073 893  ASP B OD2 
15669 N N   . ASN B 896  ? 0.1829 0.2203 0.2527 0.0209  -0.0106 -0.0087 894  ASN B N   
15670 C CA  . ASN B 896  ? 0.1969 0.2344 0.2663 0.0181  -0.0112 -0.0086 894  ASN B CA  
15671 C C   . ASN B 896  ? 0.2196 0.2534 0.2854 0.0167  -0.0137 -0.0090 894  ASN B C   
15672 O O   . ASN B 896  ? 0.2048 0.2395 0.2716 0.0148  -0.0156 -0.0086 894  ASN B O   
15673 C CB  . ASN B 896  ? 0.2261 0.2619 0.2928 0.0176  -0.0088 -0.0094 894  ASN B CB  
15674 C CG  . ASN B 896  ? 0.3239 0.3591 0.3897 0.0150  -0.0091 -0.0094 894  ASN B CG  
15675 O OD1 . ASN B 896  ? 0.3258 0.3580 0.3886 0.0137  -0.0108 -0.0099 894  ASN B OD1 
15676 N ND2 . ASN B 896  ? 0.4208 0.4585 0.4888 0.0144  -0.0074 -0.0090 894  ASN B ND2 
15677 N N   . ILE B 897  ? 0.1927 0.2224 0.2541 0.0176  -0.0137 -0.0098 895  ILE B N   
15678 C CA  . ILE B 897  ? 0.1850 0.2113 0.2426 0.0164  -0.0158 -0.0102 895  ILE B CA  
15679 C C   . ILE B 897  ? 0.1914 0.2194 0.2514 0.0166  -0.0184 -0.0092 895  ILE B C   
15680 O O   . ILE B 897  ? 0.1969 0.2245 0.2562 0.0148  -0.0205 -0.0091 895  ILE B O   
15681 C CB  . ILE B 897  ? 0.1894 0.2114 0.2423 0.0174  -0.0152 -0.0110 895  ILE B CB  
15682 C CG1 . ILE B 897  ? 0.1807 0.2011 0.2311 0.0170  -0.0129 -0.0119 895  ILE B CG1 
15683 C CG2 . ILE B 897  ? 0.2128 0.2316 0.2620 0.0164  -0.0173 -0.0111 895  ILE B CG2 
15684 C CD1 . ILE B 897  ? 0.1964 0.2136 0.2434 0.0184  -0.0117 -0.0125 895  ILE B CD1 
15685 N N   . GLU B 898  ? 0.1924 0.2223 0.2552 0.0187  -0.0184 -0.0086 896  GLU B N   
15686 C CA  . GLU B 898  ? 0.1798 0.2116 0.2451 0.0192  -0.0210 -0.0075 896  GLU B CA  
15687 C C   . GLU B 898  ? 0.1932 0.2296 0.2631 0.0175  -0.0222 -0.0067 896  GLU B C   
15688 O O   . GLU B 898  ? 0.1897 0.2267 0.2601 0.0165  -0.0250 -0.0061 896  GLU B O   
15689 C CB  . GLU B 898  ? 0.2293 0.2621 0.2967 0.0222  -0.0205 -0.0070 896  GLU B CB  
15690 C CG  . GLU B 898  ? 0.2418 0.2693 0.3041 0.0233  -0.0203 -0.0076 896  GLU B CG  
15691 C CD  . GLU B 898  ? 0.3528 0.3802 0.4164 0.0264  -0.0199 -0.0072 896  GLU B CD  
15692 O OE1 . GLU B 898  ? 0.3682 0.4001 0.4370 0.0279  -0.0191 -0.0066 896  GLU B OE1 
15693 O OE2 . GLU B 898  ? 0.4451 0.4681 0.5048 0.0273  -0.0202 -0.0075 896  GLU B OE2 
15694 N N   . LYS B 899  ? 0.1935 0.2331 0.2667 0.0170  -0.0204 -0.0066 897  LYS B N   
15695 C CA  . LYS B 899  ? 0.2018 0.2455 0.2792 0.0151  -0.0216 -0.0057 897  LYS B CA  
15696 C C   . LYS B 899  ? 0.1772 0.2178 0.2511 0.0123  -0.0234 -0.0063 897  LYS B C   
15697 O O   . LYS B 899  ? 0.1900 0.2324 0.2658 0.0107  -0.0260 -0.0057 897  LYS B O   
15698 C CB  . LYS B 899  ? 0.2193 0.2663 0.3000 0.0149  -0.0190 -0.0054 897  LYS B CB  
15699 C CG  . LYS B 899  ? 0.2487 0.3000 0.3340 0.0126  -0.0202 -0.0044 897  LYS B CG  
15700 C CD  . LYS B 899  ? 0.3488 0.4042 0.4381 0.0126  -0.0175 -0.0038 897  LYS B CD  
15701 C CE  . LYS B 899  ? 0.3356 0.3881 0.4217 0.0108  -0.0160 -0.0045 897  LYS B CE  
15702 N NZ  . LYS B 899  ? 0.3417 0.3986 0.4321 0.0100  -0.0141 -0.0036 897  LYS B NZ  
15703 N N   . HIS B 900  ? 0.1880 0.2241 0.2568 0.0117  -0.0223 -0.0075 898  HIS B N   
15704 C CA  . HIS B 900  ? 0.1934 0.2264 0.2585 0.0094  -0.0239 -0.0082 898  HIS B CA  
15705 C C   . HIS B 900  ? 0.1968 0.2278 0.2595 0.0094  -0.0266 -0.0082 898  HIS B C   
15706 O O   . HIS B 900  ? 0.1931 0.2239 0.2554 0.0076  -0.0289 -0.0082 898  HIS B O   
15707 C CB  . HIS B 900  ? 0.1698 0.1987 0.2302 0.0092  -0.0219 -0.0094 898  HIS B CB  
15708 C CG  . HIS B 900  ? 0.1898 0.2149 0.2456 0.0075  -0.0234 -0.0103 898  HIS B CG  
15709 N ND1 . HIS B 900  ? 0.2411 0.2662 0.2974 0.0053  -0.0244 -0.0104 898  HIS B ND1 
15710 C CD2 . HIS B 900  ? 0.2005 0.2217 0.2513 0.0077  -0.0239 -0.0111 898  HIS B CD2 
15711 C CE1 . HIS B 900  ? 0.2270 0.2482 0.2785 0.0044  -0.0254 -0.0114 898  HIS B CE1 
15712 N NE2 . HIS B 900  ? 0.2130 0.2320 0.2612 0.0058  -0.0251 -0.0118 898  HIS B NE2 
15713 N N   . ILE B 901  ? 0.1886 0.2178 0.2492 0.0114  -0.0263 -0.0082 899  ILE B N   
15714 C CA  . ILE B 901  ? 0.1978 0.2249 0.2557 0.0115  -0.0288 -0.0081 899  ILE B CA  
15715 C C   . ILE B 901  ? 0.2099 0.2408 0.2720 0.0111  -0.0314 -0.0069 899  ILE B C   
15716 O O   . ILE B 901  ? 0.2192 0.2491 0.2795 0.0096  -0.0340 -0.0069 899  ILE B O   
15717 C CB  . ILE B 901  ? 0.1883 0.2131 0.2438 0.0137  -0.0280 -0.0081 899  ILE B CB  
15718 C CG1 . ILE B 901  ? 0.1890 0.2099 0.2399 0.0136  -0.0257 -0.0093 899  ILE B CG1 
15719 C CG2 . ILE B 901  ? 0.2200 0.2430 0.2732 0.0139  -0.0306 -0.0076 899  ILE B CG2 
15720 C CD1 . ILE B 901  ? 0.2237 0.2422 0.2725 0.0156  -0.0246 -0.0093 899  ILE B CD1 
15721 N N   . GLU B 902  ? 0.2143 0.2499 0.2822 0.0125  -0.0308 -0.0059 900  GLU B N   
15722 C CA  . GLU B 902  ? 0.2182 0.2581 0.2907 0.0123  -0.0334 -0.0045 900  GLU B CA  
15723 C C   . GLU B 902  ? 0.2142 0.2562 0.2887 0.0093  -0.0347 -0.0045 900  GLU B C   
15724 O O   . GLU B 902  ? 0.2280 0.2718 0.3041 0.0082  -0.0377 -0.0038 900  GLU B O   
15725 C CB  . GLU B 902  ? 0.2237 0.2683 0.3019 0.0148  -0.0321 -0.0035 900  GLU B CB  
15726 C CG  . GLU B 902  ? 0.3274 0.3696 0.4037 0.0178  -0.0314 -0.0035 900  GLU B CG  
15727 C CD  . GLU B 902  ? 0.3529 0.3919 0.4254 0.0179  -0.0341 -0.0032 900  GLU B CD  
15728 O OE1 . GLU B 902  ? 0.3671 0.4086 0.4419 0.0172  -0.0370 -0.0022 900  GLU B OE1 
15729 O OE2 . GLU B 902  ? 0.3851 0.4190 0.4522 0.0184  -0.0335 -0.0040 900  GLU B OE2 
15730 N N   . ARG B 903  ? 0.2307 0.2721 0.3049 0.0080  -0.0327 -0.0052 901  ARG B N   
15731 C CA  . ARG B 903  ? 0.2375 0.2798 0.3127 0.0050  -0.0341 -0.0052 901  ARG B CA  
15732 C C   . ARG B 903  ? 0.2312 0.2689 0.3009 0.0033  -0.0365 -0.0061 901  ARG B C   
15733 O O   . ARG B 903  ? 0.2506 0.2893 0.3212 0.0013  -0.0392 -0.0058 901  ARG B O   
15734 C CB  . ARG B 903  ? 0.2573 0.2993 0.3329 0.0041  -0.0315 -0.0057 901  ARG B CB  
15735 C CG  . ARG B 903  ? 0.3504 0.3930 0.4272 0.0009  -0.0328 -0.0056 901  ARG B CG  
15736 C CD  . ARG B 903  ? 0.4410 0.4834 0.5182 0.0001  -0.0302 -0.0058 901  ARG B CD  
15737 N NE  . ARG B 903  ? 0.5100 0.5465 0.5811 -0.0004 -0.0293 -0.0073 901  ARG B NE  
15738 C CZ  . ARG B 903  ? 0.4867 0.5200 0.5550 -0.0027 -0.0306 -0.0081 901  ARG B CZ  
15739 N NH1 . ARG B 903  ? 0.5425 0.5774 0.6132 -0.0050 -0.0330 -0.0076 901  ARG B NH1 
15740 N NH2 . ARG B 903  ? 0.5171 0.5456 0.5801 -0.0026 -0.0294 -0.0094 901  ARG B NH2 
15741 N N   . MET B 904  ? 0.2329 0.2656 0.2967 0.0041  -0.0354 -0.0073 902  MET B N   
15742 C CA  . MET B 904  ? 0.2164 0.2448 0.2746 0.0027  -0.0374 -0.0083 902  MET B CA  
15743 C C   . MET B 904  ? 0.2687 0.2979 0.3269 0.0030  -0.0404 -0.0075 902  MET B C   
15744 O O   . MET B 904  ? 0.2684 0.2965 0.3247 0.0012  -0.0431 -0.0077 902  MET B O   
15745 C CB  . MET B 904  ? 0.2376 0.2614 0.2902 0.0037  -0.0354 -0.0094 902  MET B CB  
15746 C CG  . MET B 904  ? 0.2399 0.2626 0.2919 0.0035  -0.0326 -0.0102 902  MET B CG  
15747 S SD  . MET B 904  ? 0.3588 0.3795 0.4091 0.0006  -0.0336 -0.0112 902  MET B SD  
15748 C CE  . MET B 904  ? 0.3598 0.3854 0.4171 -0.0003 -0.0330 -0.0100 902  MET B CE  
15749 N N   . ARG B 905  ? 0.2318 0.2627 0.2919 0.0054  -0.0401 -0.0065 903  ARG B N   
15750 C CA  . ARG B 905  ? 0.2855 0.3174 0.3458 0.0059  -0.0431 -0.0055 903  ARG B CA  
15751 C C   . ARG B 905  ? 0.2760 0.3124 0.3413 0.0044  -0.0457 -0.0045 903  ARG B C   
15752 O O   . ARG B 905  ? 0.2849 0.3208 0.3485 0.0031  -0.0489 -0.0043 903  ARG B O   
15753 C CB  . ARG B 905  ? 0.2808 0.3136 0.3427 0.0090  -0.0421 -0.0046 903  ARG B CB  
15754 C CG  . ARG B 905  ? 0.3577 0.3893 0.4175 0.0099  -0.0448 -0.0038 903  ARG B CG  
15755 C CD  . ARG B 905  ? 0.3931 0.4262 0.4557 0.0130  -0.0440 -0.0027 903  ARG B CD  
15756 N NE  . ARG B 905  ? 0.3615 0.3923 0.4225 0.0146  -0.0406 -0.0034 903  ARG B NE  
15757 C CZ  . ARG B 905  ? 0.3286 0.3545 0.3842 0.0153  -0.0397 -0.0040 903  ARG B CZ  
15758 N NH1 . ARG B 905  ? 0.3886 0.4112 0.4393 0.0144  -0.0418 -0.0040 903  ARG B NH1 
15759 N NH2 . ARG B 905  ? 0.3543 0.3786 0.4092 0.0167  -0.0369 -0.0046 903  ARG B NH2 
15760 N N   . GLY B 906  ? 0.2534 0.2945 0.3248 0.0043  -0.0445 -0.0039 904  GLY B N   
15761 C CA  . GLY B 906  ? 0.2683 0.3143 0.3450 0.0027  -0.0469 -0.0027 904  GLY B CA  
15762 C C   . GLY B 906  ? 0.2840 0.3282 0.3586 -0.0007 -0.0488 -0.0035 904  GLY B C   
15763 O O   . GLY B 906  ? 0.3540 0.4012 0.4314 -0.0025 -0.0518 -0.0027 904  GLY B O   
15764 N N   . LEU B 907  ? 0.2973 0.3366 0.3668 -0.0018 -0.0472 -0.0051 905  LEU B N   
15765 C CA  . LEU B 907  ? 0.3407 0.3769 0.4069 -0.0047 -0.0488 -0.0062 905  LEU B CA  
15766 C C   . LEU B 907  ? 0.3100 0.3419 0.3699 -0.0052 -0.0513 -0.0070 905  LEU B C   
15767 O O   . LEU B 907  ? 0.3418 0.3706 0.3982 -0.0075 -0.0529 -0.0081 905  LEU B O   
15768 C CB  . LEU B 907  ? 0.3633 0.3960 0.4268 -0.0053 -0.0460 -0.0075 905  LEU B CB  
15769 C CG  . LEU B 907  ? 0.4301 0.4664 0.4989 -0.0056 -0.0437 -0.0068 905  LEU B CG  
15770 C CD1 . LEU B 907  ? 0.4530 0.4851 0.5182 -0.0062 -0.0413 -0.0081 905  LEU B CD1 
15771 C CD2 . LEU B 907  ? 0.4382 0.4789 0.5125 -0.0080 -0.0459 -0.0057 905  LEU B CD2 
15772 N N   . GLY B 908  ? 0.3046 0.3361 0.3629 -0.0030 -0.0516 -0.0065 906  GLY B N   
15773 C CA  . GLY B 908  ? 0.3326 0.3603 0.3850 -0.0034 -0.0540 -0.0070 906  GLY B CA  
15774 C C   . GLY B 908  ? 0.3520 0.3740 0.3973 -0.0027 -0.0521 -0.0085 906  GLY B C   
15775 O O   . GLY B 908  ? 0.3368 0.3556 0.3767 -0.0032 -0.0538 -0.0091 906  GLY B O   
15776 N N   . ARG B 909  ? 0.2694 0.2904 0.3147 -0.0017 -0.0486 -0.0092 907  ARG B N   
15777 C CA  . ARG B 909  ? 0.2717 0.2879 0.3107 -0.0011 -0.0467 -0.0104 907  ARG B CA  
15778 C C   . ARG B 909  ? 0.2668 0.2820 0.3036 0.0009  -0.0467 -0.0097 907  ARG B C   
15779 O O   . ARG B 909  ? 0.3170 0.3353 0.3579 0.0026  -0.0467 -0.0084 907  ARG B O   
15780 C CB  . ARG B 909  ? 0.2755 0.2913 0.3155 -0.0005 -0.0432 -0.0111 907  ARG B CB  
15781 C CG  . ARG B 909  ? 0.3602 0.3773 0.4032 -0.0022 -0.0429 -0.0114 907  ARG B CG  
15782 C CD  . ARG B 909  ? 0.4699 0.4831 0.5083 -0.0043 -0.0442 -0.0128 907  ARG B CD  
15783 N NE  . ARG B 909  ? 0.5664 0.5810 0.6082 -0.0064 -0.0447 -0.0128 907  ARG B NE  
15784 C CZ  . ARG B 909  ? 0.6422 0.6532 0.6808 -0.0081 -0.0450 -0.0141 907  ARG B CZ  
15785 N NH1 . ARG B 909  ? 0.6098 0.6160 0.6419 -0.0079 -0.0446 -0.0156 907  ARG B NH1 
15786 N NH2 . ARG B 909  ? 0.6522 0.6646 0.6942 -0.0101 -0.0457 -0.0138 907  ARG B NH2 
15787 N N   . LYS B 910  ? 0.2500 0.2610 0.2805 0.0008  -0.0465 -0.0107 908  LYS B N   
15788 C CA  . LYS B 910  ? 0.2695 0.2790 0.2973 0.0025  -0.0463 -0.0100 908  LYS B CA  
15789 C C   . LYS B 910  ? 0.2624 0.2720 0.2916 0.0043  -0.0429 -0.0100 908  LYS B C   
15790 O O   . LYS B 910  ? 0.2443 0.2522 0.2717 0.0040  -0.0406 -0.0111 908  LYS B O   
15791 C CB  . LYS B 910  ? 0.3012 0.3065 0.3217 0.0018  -0.0468 -0.0109 908  LYS B CB  
15792 C CG  . LYS B 910  ? 0.3318 0.3354 0.3492 0.0032  -0.0469 -0.0100 908  LYS B CG  
15793 C CD  . LYS B 910  ? 0.4331 0.4327 0.4432 0.0024  -0.0471 -0.0108 908  LYS B CD  
15794 C CE  . LYS B 910  ? 0.5523 0.5504 0.5595 0.0035  -0.0475 -0.0096 908  LYS B CE  
15795 N NZ  . LYS B 910  ? 0.5962 0.5905 0.5963 0.0029  -0.0466 -0.0104 908  LYS B NZ  
15796 N N   . VAL B 911  ? 0.2315 0.2430 0.2639 0.0061  -0.0428 -0.0087 909  VAL B N   
15797 C CA  . VAL B 911  ? 0.2239 0.2355 0.2576 0.0079  -0.0399 -0.0086 909  VAL B CA  
15798 C C   . VAL B 911  ? 0.2453 0.2545 0.2761 0.0093  -0.0402 -0.0078 909  VAL B C   
15799 O O   . VAL B 911  ? 0.2638 0.2740 0.2957 0.0101  -0.0425 -0.0066 909  VAL B O   
15800 C CB  . VAL B 911  ? 0.2209 0.2369 0.2616 0.0090  -0.0393 -0.0078 909  VAL B CB  
15801 C CG1 . VAL B 911  ? 0.2350 0.2506 0.2765 0.0110  -0.0366 -0.0077 909  VAL B CG1 
15802 C CG2 . VAL B 911  ? 0.2331 0.2513 0.2766 0.0073  -0.0390 -0.0084 909  VAL B CG2 
15803 N N   . GLU B 912  ? 0.2117 0.2179 0.2388 0.0097  -0.0381 -0.0085 910  GLU B N   
15804 C CA  . GLU B 912  ? 0.2310 0.2346 0.2552 0.0109  -0.0381 -0.0077 910  GLU B CA  
15805 C C   . GLU B 912  ? 0.2354 0.2383 0.2605 0.0122  -0.0353 -0.0080 910  GLU B C   
15806 O O   . GLU B 912  ? 0.2387 0.2415 0.2635 0.0116  -0.0331 -0.0091 910  GLU B O   
15807 C CB  . GLU B 912  ? 0.2981 0.2981 0.3157 0.0096  -0.0385 -0.0082 910  GLU B CB  
15808 C CG  . GLU B 912  ? 0.3143 0.3144 0.3300 0.0083  -0.0414 -0.0080 910  GLU B CG  
15809 C CD  . GLU B 912  ? 0.4846 0.4813 0.4937 0.0071  -0.0414 -0.0086 910  GLU B CD  
15810 O OE1 . GLU B 912  ? 0.5424 0.5369 0.5480 0.0075  -0.0419 -0.0077 910  GLU B OE1 
15811 O OE2 . GLU B 912  ? 0.5706 0.5668 0.5779 0.0058  -0.0409 -0.0100 910  GLU B OE2 
15812 N N   . GLN B 913  ? 0.2198 0.2221 0.2457 0.0140  -0.0354 -0.0069 911  GLN B N   
15813 C CA  . GLN B 913  ? 0.2402 0.2414 0.2665 0.0153  -0.0329 -0.0072 911  GLN B CA  
15814 C C   . GLN B 913  ? 0.2743 0.2715 0.2965 0.0158  -0.0333 -0.0065 911  GLN B C   
15815 O O   . GLN B 913  ? 0.3096 0.3061 0.3312 0.0164  -0.0355 -0.0053 911  GLN B O   
15816 C CB  . GLN B 913  ? 0.2739 0.2780 0.3058 0.0172  -0.0323 -0.0068 911  GLN B CB  
15817 C CG  . GLN B 913  ? 0.2622 0.2704 0.2984 0.0164  -0.0319 -0.0073 911  GLN B CG  
15818 C CD  . GLN B 913  ? 0.3151 0.3266 0.3568 0.0183  -0.0308 -0.0069 911  GLN B CD  
15819 O OE1 . GLN B 913  ? 0.4098 0.4232 0.4545 0.0198  -0.0323 -0.0058 911  GLN B OE1 
15820 N NE2 . GLN B 913  ? 0.2698 0.2822 0.3128 0.0183  -0.0283 -0.0078 911  GLN B NE2 
15821 N N   . ILE B 914  ? 0.2735 0.2681 0.2928 0.0155  -0.0312 -0.0072 912  ILE B N   
15822 C CA  . ILE B 914  ? 0.3728 0.3634 0.3876 0.0155  -0.0313 -0.0066 912  ILE B CA  
15823 C C   . ILE B 914  ? 0.3465 0.3354 0.3618 0.0166  -0.0293 -0.0068 912  ILE B C   
15824 O O   . ILE B 914  ? 0.3261 0.3155 0.3415 0.0161  -0.0272 -0.0080 912  ILE B O   
15825 C CB  . ILE B 914  ? 0.3632 0.3522 0.3731 0.0133  -0.0309 -0.0071 912  ILE B CB  
15826 C CG1 . ILE B 914  ? 0.4118 0.4018 0.4206 0.0123  -0.0330 -0.0070 912  ILE B CG1 
15827 C CG2 . ILE B 914  ? 0.3542 0.3392 0.3597 0.0131  -0.0306 -0.0065 912  ILE B CG2 
15828 C CD1 . ILE B 914  ? 0.3668 0.3558 0.3713 0.0104  -0.0323 -0.0079 912  ILE B CD1 
15829 N N   . GLY B 915  ? 0.4169 0.4037 0.4321 0.0183  -0.0301 -0.0058 913  GLY B N   
15830 C CA  . GLY B 915  ? 0.5111 0.4953 0.5262 0.0196  -0.0287 -0.0059 913  GLY B CA  
15831 C C   . GLY B 915  ? 0.5147 0.5012 0.5348 0.0221  -0.0285 -0.0058 913  GLY B C   
15832 O O   . GLY B 915  ? 0.5436 0.5344 0.5679 0.0224  -0.0284 -0.0062 913  GLY B O   
15833 N N   . LEU B 916  ? 0.6806 0.6640 0.7003 0.0240  -0.0283 -0.0054 914  LEU B N   
15834 C CA  . LEU B 916  ? 0.6327 0.6180 0.6570 0.0268  -0.0280 -0.0053 914  LEU B CA  
15835 C C   . LEU B 916  ? 0.7149 0.6959 0.7380 0.0291  -0.0280 -0.0048 914  LEU B C   
15836 O O   . LEU B 916  ? 0.6984 0.6792 0.7230 0.0310  -0.0297 -0.0036 914  LEU B O   
15837 C CB  . LEU B 916  ? 0.6619 0.6512 0.6901 0.0277  -0.0302 -0.0042 914  LEU B CB  
15838 C CG  . LEU B 916  ? 0.7544 0.7493 0.7886 0.0287  -0.0294 -0.0046 914  LEU B CG  
15839 C CD1 . LEU B 916  ? 0.7581 0.7572 0.7948 0.0276  -0.0315 -0.0039 914  LEU B CD1 
15840 C CD2 . LEU B 916  ? 0.7946 0.7901 0.8324 0.0320  -0.0289 -0.0042 914  LEU B CD2 
15841 N N   . ALA B 917  ? 0.6520 0.6295 0.6725 0.0289  -0.0261 -0.0058 915  ALA B N   
15842 C CA  . ALA B 917  ? 0.6420 0.6145 0.6606 0.0309  -0.0262 -0.0055 915  ALA B CA  
15843 C C   . ALA B 917  ? 0.6436 0.6179 0.6666 0.0343  -0.0254 -0.0058 915  ALA B C   
15844 O O   . ALA B 917  ? 0.5795 0.5583 0.6062 0.0347  -0.0238 -0.0067 915  ALA B O   
15845 C CB  . ALA B 917  ? 0.6525 0.6205 0.6667 0.0294  -0.0246 -0.0065 915  ALA B CB  
15846 N N   . SER B 918  ? 0.6311 0.6020 0.6537 0.0367  -0.0263 -0.0050 916  SER B N   
15847 C CA  . SER B 918  ? 0.6186 0.5909 0.6452 0.0403  -0.0255 -0.0052 916  SER B CA  
15848 C C   . SER B 918  ? 0.5993 0.5704 0.6253 0.0409  -0.0227 -0.0071 916  SER B C   
15849 O O   . SER B 918  ? 0.5091 0.4839 0.5393 0.0430  -0.0212 -0.0077 916  SER B O   
15850 C CB  . SER B 918  ? 0.6311 0.5993 0.6569 0.0430  -0.0272 -0.0039 916  SER B CB  
15851 O OG  . SER B 918  ? 0.7284 0.6891 0.7486 0.0425  -0.0269 -0.0042 916  SER B OG  
15852 N N   . GLU B 919  ? 0.5381 0.5041 0.5589 0.0389  -0.0219 -0.0079 917  GLU B N   
15853 C CA  . GLU B 919  ? 0.5287 0.4933 0.5483 0.0391  -0.0194 -0.0097 917  GLU B CA  
15854 C C   . GLU B 919  ? 0.5228 0.4934 0.5456 0.0381  -0.0177 -0.0107 917  GLU B C   
15855 O O   . GLU B 919  ? 0.4521 0.4226 0.4747 0.0387  -0.0155 -0.0121 917  GLU B O   
15856 C CB  . GLU B 919  ? 0.5426 0.5015 0.5563 0.0365  -0.0193 -0.0102 917  GLU B CB  
15857 C CG  . GLU B 919  ? 0.6759 0.6275 0.6858 0.0375  -0.0204 -0.0096 917  GLU B CG  
15858 C CD  . GLU B 919  ? 0.7181 0.6686 0.7272 0.0371  -0.0230 -0.0076 917  GLU B CD  
15859 O OE1 . GLU B 919  ? 0.6671 0.6217 0.6774 0.0353  -0.0239 -0.0068 917  GLU B OE1 
15860 O OE2 . GLU B 919  ? 0.7065 0.6517 0.7135 0.0387  -0.0242 -0.0068 917  GLU B OE2 
15861 N N   . THR B 920  ? 0.4564 0.4320 0.4818 0.0366  -0.0186 -0.0100 918  THR B N   
15862 C CA  . THR B 920  ? 0.4157 0.3967 0.4441 0.0356  -0.0170 -0.0108 918  THR B CA  
15863 C C   . THR B 920  ? 0.4334 0.4187 0.4670 0.0385  -0.0158 -0.0109 918  THR B C   
15864 O O   . THR B 920  ? 0.3866 0.3753 0.4221 0.0381  -0.0139 -0.0118 918  THR B O   
15865 C CB  . THR B 920  ? 0.4566 0.4410 0.4859 0.0331  -0.0183 -0.0100 918  THR B CB  
15866 O OG1 . THR B 920  ? 0.4316 0.4180 0.4636 0.0342  -0.0205 -0.0086 918  THR B OG1 
15867 C CG2 . THR B 920  ? 0.3419 0.3227 0.3660 0.0302  -0.0189 -0.0101 918  THR B CG2 
15868 N N   . GLY B 921  ? 0.3893 0.3745 0.4252 0.0414  -0.0168 -0.0100 919  GLY B N   
15869 C CA  . GLY B 921  ? 0.4078 0.3981 0.4494 0.0442  -0.0159 -0.0099 919  GLY B CA  
15870 C C   . GLY B 921  ? 0.3993 0.3896 0.4410 0.0457  -0.0129 -0.0115 919  GLY B C   
15871 O O   . GLY B 921  ? 0.4342 0.4298 0.4806 0.0472  -0.0116 -0.0115 919  GLY B O   
15872 N N   . VAL B 922  ? 0.3011 0.2855 0.3376 0.0452  -0.0119 -0.0127 920  VAL B N   
15873 C CA  . VAL B 922  ? 0.2818 0.2655 0.3175 0.0465  -0.0092 -0.0143 920  VAL B CA  
15874 C C   . VAL B 922  ? 0.2672 0.2540 0.3027 0.0439  -0.0077 -0.0151 920  VAL B C   
15875 O O   . VAL B 922  ? 0.2646 0.2520 0.3000 0.0448  -0.0053 -0.0164 920  VAL B O   
15876 C CB  . VAL B 922  ? 0.3210 0.2967 0.3509 0.0471  -0.0090 -0.0154 920  VAL B CB  
15877 C CG1 . VAL B 922  ? 0.3315 0.3042 0.3620 0.0505  -0.0101 -0.0147 920  VAL B CG1 
15878 C CG2 . VAL B 922  ? 0.2923 0.2639 0.3174 0.0436  -0.0103 -0.0153 920  VAL B CG2 
15879 N N   . GLY B 923  ? 0.2422 0.2307 0.2775 0.0408  -0.0088 -0.0145 921  GLY B N   
15880 C CA  . GLY B 923  ? 0.2329 0.2243 0.2683 0.0384  -0.0076 -0.0151 921  GLY B CA  
15881 C C   . GLY B 923  ? 0.2373 0.2346 0.2770 0.0371  -0.0085 -0.0140 921  GLY B C   
15882 O O   . GLY B 923  ? 0.2576 0.2572 0.3008 0.0384  -0.0100 -0.0129 921  GLY B O   
15883 N N   . THR B 924  ? 0.1998 0.1992 0.2393 0.0346  -0.0079 -0.0143 922  THR B N   
15884 C CA  . THR B 924  ? 0.1988 0.2031 0.2419 0.0332  -0.0088 -0.0134 922  THR B CA  
15885 C C   . THR B 924  ? 0.1951 0.1975 0.2351 0.0303  -0.0103 -0.0133 922  THR B C   
15886 O O   . THR B 924  ? 0.2206 0.2220 0.2580 0.0285  -0.0094 -0.0140 922  THR B O   
15887 C CB  . THR B 924  ? 0.1788 0.1874 0.2246 0.0328  -0.0067 -0.0138 922  THR B CB  
15888 O OG1 . THR B 924  ? 0.2106 0.2165 0.2524 0.0317  -0.0051 -0.0150 922  THR B OG1 
15889 C CG2 . THR B 924  ? 0.2335 0.2451 0.2831 0.0357  -0.0052 -0.0138 922  THR B CG2 
15890 N N   . PHE B 925  ? 0.1991 0.2012 0.2394 0.0301  -0.0126 -0.0123 923  PHE B N   
15891 C CA  . PHE B 925  ? 0.2056 0.2059 0.2428 0.0276  -0.0141 -0.0121 923  PHE B CA  
15892 C C   . PHE B 925  ? 0.2042 0.2082 0.2443 0.0265  -0.0158 -0.0112 923  PHE B C   
15893 O O   . PHE B 925  ? 0.2111 0.2179 0.2551 0.0280  -0.0168 -0.0103 923  PHE B O   
15894 C CB  . PHE B 925  ? 0.2043 0.1997 0.2377 0.0279  -0.0156 -0.0116 923  PHE B CB  
15895 C CG  . PHE B 925  ? 0.2030 0.1938 0.2326 0.0282  -0.0143 -0.0126 923  PHE B CG  
15896 C CD1 . PHE B 925  ? 0.2042 0.1935 0.2344 0.0307  -0.0133 -0.0129 923  PHE B CD1 
15897 C CD2 . PHE B 925  ? 0.2080 0.1961 0.2333 0.0259  -0.0140 -0.0131 923  PHE B CD2 
15898 C CE1 . PHE B 925  ? 0.2261 0.2109 0.2525 0.0309  -0.0122 -0.0139 923  PHE B CE1 
15899 C CE2 . PHE B 925  ? 0.2092 0.1932 0.2310 0.0259  -0.0130 -0.0139 923  PHE B CE2 
15900 C CZ  . PHE B 925  ? 0.2216 0.2037 0.2438 0.0283  -0.0122 -0.0143 923  PHE B CZ  
15901 N N   . VAL B 926  ? 0.1982 0.2021 0.2363 0.0241  -0.0162 -0.0114 924  VAL B N   
15902 C CA  . VAL B 926  ? 0.1911 0.1971 0.2304 0.0227  -0.0182 -0.0107 924  VAL B CA  
15903 C C   . VAL B 926  ? 0.1923 0.1945 0.2266 0.0211  -0.0193 -0.0108 924  VAL B C   
15904 O O   . VAL B 926  ? 0.2014 0.2015 0.2325 0.0200  -0.0181 -0.0116 924  VAL B O   
15905 C CB  . VAL B 926  ? 0.2004 0.2098 0.2420 0.0212  -0.0174 -0.0111 924  VAL B CB  
15906 C CG1 . VAL B 926  ? 0.2008 0.2115 0.2428 0.0196  -0.0196 -0.0106 924  VAL B CG1 
15907 C CG2 . VAL B 926  ? 0.2196 0.2330 0.2661 0.0227  -0.0161 -0.0109 924  VAL B CG2 
15908 N N   . PRO B 927  ? 0.2167 0.2182 0.2502 0.0209  -0.0216 -0.0099 925  PRO B N   
15909 C CA  . PRO B 927  ? 0.2240 0.2221 0.2526 0.0194  -0.0225 -0.0099 925  PRO B CA  
15910 C C   . PRO B 927  ? 0.2134 0.2127 0.2409 0.0172  -0.0226 -0.0105 925  PRO B C   
15911 O O   . PRO B 927  ? 0.2147 0.2172 0.2454 0.0168  -0.0228 -0.0105 925  PRO B O   
15912 C CB  . PRO B 927  ? 0.2705 0.2678 0.2989 0.0201  -0.0250 -0.0086 925  PRO B CB  
15913 C CG  . PRO B 927  ? 0.2492 0.2509 0.2829 0.0210  -0.0258 -0.0081 925  PRO B CG  
15914 C CD  . PRO B 927  ? 0.2244 0.2284 0.2615 0.0221  -0.0235 -0.0088 925  PRO B CD  
15915 N N   . PRO B 928  ? 0.2245 0.2212 0.2476 0.0158  -0.0223 -0.0108 926  PRO B N   
15916 C CA  . PRO B 928  ? 0.2120 0.2094 0.2335 0.0140  -0.0226 -0.0114 926  PRO B CA  
15917 C C   . PRO B 928  ? 0.2076 0.2067 0.2307 0.0137  -0.0249 -0.0108 926  PRO B C   
15918 O O   . PRO B 928  ? 0.2202 0.2186 0.2428 0.0142  -0.0268 -0.0098 926  PRO B O   
15919 C CB  . PRO B 928  ? 0.2264 0.2205 0.2427 0.0130  -0.0226 -0.0114 926  PRO B CB  
15920 C CG  . PRO B 928  ? 0.2670 0.2591 0.2826 0.0138  -0.0213 -0.0114 926  PRO B CG  
15921 C CD  . PRO B 928  ? 0.2272 0.2202 0.2464 0.0157  -0.0218 -0.0108 926  PRO B CD  
15922 N N   . THR B 929  ? 0.2043 0.2057 0.2292 0.0127  -0.0248 -0.0114 927  THR B N   
15923 C CA  . THR B 929  ? 0.1981 0.2015 0.2252 0.0122  -0.0268 -0.0110 927  THR B CA  
15924 C C   . THR B 929  ? 0.2023 0.2051 0.2268 0.0104  -0.0271 -0.0119 927  THR B C   
15925 O O   . THR B 929  ? 0.2113 0.2138 0.2350 0.0099  -0.0253 -0.0128 927  THR B O   
15926 C CB  . THR B 929  ? 0.1937 0.2009 0.2265 0.0129  -0.0264 -0.0107 927  THR B CB  
15927 O OG1 . THR B 929  ? 0.2090 0.2167 0.2440 0.0149  -0.0259 -0.0100 927  THR B OG1 
15928 C CG2 . THR B 929  ? 0.2131 0.2228 0.2485 0.0121  -0.0286 -0.0103 927  THR B CG2 
15929 N N   . ILE B 930  ? 0.1981 0.2004 0.2209 0.0096  -0.0294 -0.0116 928  ILE B N   
15930 C CA  . ILE B 930  ? 0.2154 0.2168 0.2355 0.0079  -0.0299 -0.0125 928  ILE B CA  
15931 C C   . ILE B 930  ? 0.2035 0.2069 0.2264 0.0072  -0.0321 -0.0123 928  ILE B C   
15932 O O   . ILE B 930  ? 0.2149 0.2193 0.2390 0.0075  -0.0343 -0.0113 928  ILE B O   
15933 C CB  . ILE B 930  ? 0.2099 0.2082 0.2243 0.0074  -0.0306 -0.0126 928  ILE B CB  
15934 C CG1 . ILE B 930  ? 0.2222 0.2188 0.2341 0.0079  -0.0285 -0.0127 928  ILE B CG1 
15935 C CG2 . ILE B 930  ? 0.2254 0.2227 0.2369 0.0059  -0.0312 -0.0137 928  ILE B CG2 
15936 C CD1 . ILE B 930  ? 0.2854 0.2793 0.2921 0.0074  -0.0291 -0.0125 928  ILE B CD1 
15937 N N   . ILE B 931  ? 0.2117 0.2158 0.2356 0.0061  -0.0317 -0.0131 929  ILE B N   
15938 C CA  . ILE B 931  ? 0.1889 0.1950 0.2157 0.0050  -0.0337 -0.0129 929  ILE B CA  
15939 C C   . ILE B 931  ? 0.2159 0.2195 0.2388 0.0034  -0.0344 -0.0142 929  ILE B C   
15940 O O   . ILE B 931  ? 0.2279 0.2301 0.2491 0.0031  -0.0325 -0.0152 929  ILE B O   
15941 C CB  . ILE B 931  ? 0.1942 0.2034 0.2265 0.0051  -0.0325 -0.0127 929  ILE B CB  
15942 C CG1 . ILE B 931  ? 0.2229 0.2343 0.2587 0.0070  -0.0315 -0.0116 929  ILE B CG1 
15943 C CG2 . ILE B 931  ? 0.2202 0.2316 0.2556 0.0036  -0.0347 -0.0124 929  ILE B CG2 
15944 C CD1 . ILE B 931  ? 0.2224 0.2374 0.2637 0.0073  -0.0303 -0.0112 929  ILE B CD1 
15945 N N   . GLU B 932  ? 0.2131 0.2162 0.2345 0.0023  -0.0371 -0.0141 930  GLU B N   
15946 C CA  . GLU B 932  ? 0.2265 0.2270 0.2439 0.0008  -0.0378 -0.0154 930  GLU B CA  
15947 C C   . GLU B 932  ? 0.2253 0.2272 0.2461 -0.0006 -0.0386 -0.0157 930  GLU B C   
15948 O O   . GLU B 932  ? 0.2403 0.2451 0.2654 -0.0011 -0.0404 -0.0147 930  GLU B O   
15949 C CB  . GLU B 932  ? 0.2992 0.2980 0.3125 0.0002  -0.0405 -0.0154 930  GLU B CB  
15950 C CG  . GLU B 932  ? 0.3353 0.3325 0.3448 0.0013  -0.0397 -0.0150 930  GLU B CG  
15951 C CD  . GLU B 932  ? 0.5134 0.5079 0.5170 0.0005  -0.0415 -0.0155 930  GLU B CD  
15952 O OE1 . GLU B 932  ? 0.5219 0.5160 0.5247 -0.0009 -0.0438 -0.0160 930  GLU B OE1 
15953 O OE2 . GLU B 932  ? 0.4463 0.4390 0.4458 0.0011  -0.0405 -0.0154 930  GLU B OE2 
15954 N N   . LEU B 933  ? 0.2395 0.2394 0.2587 -0.0012 -0.0371 -0.0170 931  LEU B N   
15955 C CA  . LEU B 933  ? 0.2377 0.2380 0.2594 -0.0027 -0.0378 -0.0173 931  LEU B CA  
15956 C C   . LEU B 933  ? 0.2951 0.2918 0.3122 -0.0042 -0.0397 -0.0186 931  LEU B C   
15957 O O   . LEU B 933  ? 0.3464 0.3400 0.3580 -0.0038 -0.0393 -0.0197 931  LEU B O   
15958 C CB  . LEU B 933  ? 0.2645 0.2646 0.2875 -0.0023 -0.0350 -0.0177 931  LEU B CB  
15959 C CG  . LEU B 933  ? 0.2862 0.2893 0.3131 -0.0007 -0.0328 -0.0166 931  LEU B CG  
15960 C CD1 . LEU B 933  ? 0.3377 0.3401 0.3651 -0.0006 -0.0303 -0.0172 931  LEU B CD1 
15961 C CD2 . LEU B 933  ? 0.3958 0.4031 0.4285 -0.0009 -0.0339 -0.0152 931  LEU B CD2 
15962 N N   . GLU B 934  ? 0.3459 0.3432 0.3653 -0.0061 -0.0416 -0.0186 932  GLU B N   
15963 C CA  . GLU B 934  ? 0.3693 0.3627 0.3843 -0.0077 -0.0432 -0.0201 932  GLU B CA  
15964 C C   . GLU B 934  ? 0.3880 0.3785 0.4015 -0.0077 -0.0410 -0.0213 932  GLU B C   
15965 O O   . GLU B 934  ? 0.4294 0.4157 0.4375 -0.0078 -0.0409 -0.0229 932  GLU B O   
15966 C CB  . GLU B 934  ? 0.4369 0.4318 0.4547 -0.0099 -0.0464 -0.0196 932  GLU B CB  
15967 N N   . LYS B 935  ? 0.3216 0.3143 0.3397 -0.0074 -0.0392 -0.0205 933  LYS B N   
15968 C CA  . LYS B 935  ? 0.3541 0.3444 0.3713 -0.0074 -0.0373 -0.0214 933  LYS B CA  
15969 C C   . LYS B 935  ? 0.3154 0.3085 0.3362 -0.0059 -0.0345 -0.0204 933  LYS B C   
15970 O O   . LYS B 935  ? 0.3351 0.3323 0.3605 -0.0056 -0.0344 -0.0190 933  LYS B O   
15971 C CB  . LYS B 935  ? 0.4198 0.4091 0.4388 -0.0097 -0.0389 -0.0215 933  LYS B CB  
15972 N N   . LEU B 936  ? 0.2921 0.2831 0.3109 -0.0050 -0.0322 -0.0212 934  LEU B N   
15973 C CA  . LEU B 936  ? 0.2942 0.2876 0.3159 -0.0037 -0.0296 -0.0203 934  LEU B CA  
15974 C C   . LEU B 936  ? 0.3103 0.3066 0.3376 -0.0047 -0.0296 -0.0190 934  LEU B C   
15975 O O   . LEU B 936  ? 0.3137 0.3134 0.3446 -0.0038 -0.0281 -0.0179 934  LEU B O   
15976 C CB  . LEU B 936  ? 0.3336 0.3241 0.3521 -0.0026 -0.0274 -0.0213 934  LEU B CB  
15977 C CG  . LEU B 936  ? 0.3484 0.3407 0.3671 -0.0007 -0.0249 -0.0209 934  LEU B CG  
15978 C CD1 . LEU B 936  ? 0.3757 0.3650 0.3899 0.0004  -0.0235 -0.0222 934  LEU B CD1 
15979 C CD2 . LEU B 936  ? 0.3756 0.3703 0.3986 -0.0005 -0.0233 -0.0198 934  LEU B CD2 
15980 N N   . SER B 937  ? 0.2900 0.2851 0.3181 -0.0067 -0.0313 -0.0191 935  SER B N   
15981 C CA  . SER B 937  ? 0.3241 0.3222 0.3575 -0.0080 -0.0313 -0.0178 935  SER B CA  
15982 C C   . SER B 937  ? 0.3422 0.3453 0.3804 -0.0082 -0.0324 -0.0164 935  SER B C   
15983 O O   . SER B 937  ? 0.3158 0.3224 0.3590 -0.0089 -0.0320 -0.0151 935  SER B O   
15984 C CB  . SER B 937  ? 0.3396 0.3349 0.3725 -0.0104 -0.0331 -0.0182 935  SER B CB  
15985 O OG  . SER B 937  ? 0.3990 0.3927 0.4296 -0.0117 -0.0359 -0.0190 935  SER B OG  
15986 N N   . ASP B 938  ? 0.3114 0.3152 0.3483 -0.0074 -0.0336 -0.0165 936  ASP B N   
15987 C CA  . ASP B 938  ? 0.3246 0.3333 0.3660 -0.0068 -0.0342 -0.0150 936  ASP B CA  
15988 C C   . ASP B 938  ? 0.2960 0.3075 0.3404 -0.0049 -0.0314 -0.0142 936  ASP B C   
15989 O O   . ASP B 938  ? 0.3248 0.3407 0.3740 -0.0045 -0.0314 -0.0129 936  ASP B O   
15990 C CB  . ASP B 938  ? 0.3770 0.3852 0.4157 -0.0059 -0.0358 -0.0153 936  ASP B CB  
15991 C CG  . ASP B 938  ? 0.4883 0.4938 0.5238 -0.0077 -0.0388 -0.0161 936  ASP B CG  
15992 O OD1 . ASP B 938  ? 0.4339 0.4391 0.4708 -0.0098 -0.0402 -0.0162 936  ASP B OD1 
15993 O OD2 . ASP B 938  ? 0.5284 0.5321 0.5599 -0.0070 -0.0397 -0.0167 936  ASP B OD2 
15994 N N   . LEU B 939  ? 0.2615 0.2707 0.3030 -0.0037 -0.0291 -0.0149 937  LEU B N   
15995 C CA  . LEU B 939  ? 0.3326 0.3438 0.3758 -0.0019 -0.0264 -0.0144 937  LEU B CA  
15996 C C   . LEU B 939  ? 0.3103 0.3220 0.3556 -0.0026 -0.0248 -0.0140 937  LEU B C   
15997 O O   . LEU B 939  ? 0.4051 0.4135 0.4475 -0.0032 -0.0243 -0.0148 937  LEU B O   
15998 C CB  . LEU B 939  ? 0.3014 0.3098 0.3398 -0.0004 -0.0251 -0.0154 937  LEU B CB  
15999 C CG  . LEU B 939  ? 0.3711 0.3806 0.4099 0.0015  -0.0228 -0.0151 937  LEU B CG  
16000 C CD1 . LEU B 939  ? 0.3955 0.4084 0.4376 0.0025  -0.0231 -0.0141 937  LEU B CD1 
16001 C CD2 . LEU B 939  ? 0.2974 0.3038 0.3311 0.0024  -0.0222 -0.0162 937  LEU B CD2 
16002 N N   . GLN B 940  ? 0.2608 0.2767 0.3110 -0.0024 -0.0238 -0.0127 938  GLN B N   
16003 C CA  . GLN B 940  ? 0.3407 0.3577 0.3934 -0.0033 -0.0224 -0.0120 938  GLN B CA  
16004 C C   . GLN B 940  ? 0.3037 0.3221 0.3572 -0.0016 -0.0195 -0.0117 938  GLN B C   
16005 O O   . GLN B 940  ? 0.2908 0.3099 0.3459 -0.0023 -0.0181 -0.0110 938  GLN B O   
16006 C CB  . GLN B 940  ? 0.4374 0.4584 0.4955 -0.0049 -0.0237 -0.0107 938  GLN B CB  
16007 N N   . ARG B 941  ? 0.2306 0.2494 0.2829 0.0004  -0.0185 -0.0120 939  ARG B N   
16008 C CA  . ARG B 941  ? 0.2408 0.2608 0.2936 0.0019  -0.0159 -0.0117 939  ARG B CA  
16009 C C   . ARG B 941  ? 0.2034 0.2214 0.2525 0.0036  -0.0153 -0.0126 939  ARG B C   
16010 O O   . ARG B 941  ? 0.2043 0.2212 0.2518 0.0039  -0.0168 -0.0130 939  ARG B O   
16011 C CB  . ARG B 941  ? 0.2683 0.2933 0.3263 0.0025  -0.0151 -0.0105 939  ARG B CB  
16012 C CG  . ARG B 941  ? 0.2900 0.3168 0.3494 0.0038  -0.0162 -0.0103 939  ARG B CG  
16013 C CD  . ARG B 941  ? 0.2655 0.2976 0.3306 0.0043  -0.0155 -0.0090 939  ARG B CD  
16014 N NE  . ARG B 941  ? 0.2884 0.3224 0.3552 0.0058  -0.0165 -0.0087 939  ARG B NE  
16015 C CZ  . ARG B 941  ? 0.2875 0.3215 0.3537 0.0082  -0.0152 -0.0089 939  ARG B CZ  
16016 N NH1 . ARG B 941  ? 0.2695 0.3016 0.3330 0.0091  -0.0129 -0.0095 939  ARG B NH1 
16017 N NH2 . ARG B 941  ? 0.2694 0.3052 0.3375 0.0096  -0.0162 -0.0084 939  ARG B NH2 
16018 N N   . GLU B 942  ? 0.2210 0.2386 0.2689 0.0047  -0.0131 -0.0128 940  GLU B N   
16019 C CA  . GLU B 942  ? 0.1973 0.2133 0.2421 0.0062  -0.0123 -0.0135 940  GLU B CA  
16020 C C   . GLU B 942  ? 0.1949 0.2132 0.2419 0.0075  -0.0123 -0.0131 940  GLU B C   
16021 O O   . GLU B 942  ? 0.2409 0.2620 0.2911 0.0081  -0.0112 -0.0123 940  GLU B O   
16022 C CB  . GLU B 942  ? 0.2169 0.2322 0.2601 0.0068  -0.0101 -0.0137 940  GLU B CB  
16023 C CG  . GLU B 942  ? 0.2018 0.2157 0.2420 0.0081  -0.0093 -0.0144 940  GLU B CG  
16024 C CD  . GLU B 942  ? 0.2117 0.2257 0.2511 0.0088  -0.0072 -0.0145 940  GLU B CD  
16025 O OE1 . GLU B 942  ? 0.2460 0.2622 0.2879 0.0089  -0.0060 -0.0138 940  GLU B OE1 
16026 O OE2 . GLU B 942  ? 0.1870 0.1990 0.2230 0.0091  -0.0067 -0.0151 940  GLU B OE2 
16027 N N   . VAL B 943  ? 0.1753 0.1922 0.2204 0.0080  -0.0136 -0.0134 941  VAL B N   
16028 C CA  . VAL B 943  ? 0.1822 0.2006 0.2289 0.0095  -0.0138 -0.0130 941  VAL B CA  
16029 C C   . VAL B 943  ? 0.1915 0.2075 0.2347 0.0107  -0.0127 -0.0136 941  VAL B C   
16030 O O   . VAL B 943  ? 0.1838 0.1971 0.2233 0.0104  -0.0134 -0.0142 941  VAL B O   
16031 C CB  . VAL B 943  ? 0.2037 0.2222 0.2509 0.0091  -0.0164 -0.0127 941  VAL B CB  
16032 C CG1 . VAL B 943  ? 0.2168 0.2365 0.2655 0.0108  -0.0166 -0.0121 941  VAL B CG1 
16033 C CG2 . VAL B 943  ? 0.2392 0.2600 0.2898 0.0076  -0.0177 -0.0120 941  VAL B CG2 
16034 N N   . PHE B 944  ? 0.1812 0.1982 0.2253 0.0119  -0.0108 -0.0135 942  PHE B N   
16035 C CA  . PHE B 944  ? 0.1740 0.1888 0.2149 0.0127  -0.0095 -0.0142 942  PHE B CA  
16036 C C   . PHE B 944  ? 0.1760 0.1898 0.2161 0.0140  -0.0100 -0.0142 942  PHE B C   
16037 O O   . PHE B 944  ? 0.1981 0.2124 0.2391 0.0154  -0.0090 -0.0142 942  PHE B O   
16038 C CB  . PHE B 944  ? 0.1783 0.1945 0.2202 0.0132  -0.0073 -0.0142 942  PHE B CB  
16039 C CG  . PHE B 944  ? 0.1809 0.1949 0.2192 0.0133  -0.0060 -0.0149 942  PHE B CG  
16040 C CD1 . PHE B 944  ? 0.1846 0.1972 0.2206 0.0121  -0.0061 -0.0153 942  PHE B CD1 
16041 C CD2 . PHE B 944  ? 0.1837 0.1970 0.2209 0.0145  -0.0048 -0.0153 942  PHE B CD2 
16042 C CE1 . PHE B 944  ? 0.1978 0.2089 0.2309 0.0122  -0.0050 -0.0159 942  PHE B CE1 
16043 C CE2 . PHE B 944  ? 0.1852 0.1967 0.2192 0.0144  -0.0039 -0.0159 942  PHE B CE2 
16044 C CZ  . PHE B 944  ? 0.1956 0.2062 0.2276 0.0132  -0.0040 -0.0162 942  PHE B CZ  
16045 N N   . GLY B 945  ? 0.1791 0.1910 0.2172 0.0135  -0.0118 -0.0142 943  GLY B N   
16046 C CA  . GLY B 945  ? 0.1873 0.1978 0.2243 0.0145  -0.0126 -0.0140 943  GLY B CA  
16047 C C   . GLY B 945  ? 0.1963 0.2044 0.2299 0.0135  -0.0142 -0.0142 943  GLY B C   
16048 O O   . GLY B 945  ? 0.1907 0.1981 0.2225 0.0122  -0.0143 -0.0146 943  GLY B O   
16049 N N   . PRO B 946  ? 0.1830 0.1896 0.2155 0.0142  -0.0153 -0.0138 944  PRO B N   
16050 C CA  . PRO B 946  ? 0.1890 0.1931 0.2176 0.0133  -0.0165 -0.0139 944  PRO B CA  
16051 C C   . PRO B 946  ? 0.1774 0.1822 0.2065 0.0125  -0.0187 -0.0135 944  PRO B C   
16052 O O   . PRO B 946  ? 0.2081 0.2120 0.2364 0.0128  -0.0204 -0.0129 944  PRO B O   
16053 C CB  . PRO B 946  ? 0.1939 0.1958 0.2210 0.0145  -0.0168 -0.0135 944  PRO B CB  
16054 C CG  . PRO B 946  ? 0.2109 0.2149 0.2422 0.0161  -0.0168 -0.0129 944  PRO B CG  
16055 C CD  . PRO B 946  ? 0.1933 0.2002 0.2277 0.0160  -0.0153 -0.0133 944  PRO B CD  
16056 N N   . VAL B 947  ? 0.1883 0.1946 0.2188 0.0115  -0.0188 -0.0138 945  VAL B N   
16057 C CA  . VAL B 947  ? 0.1847 0.1919 0.2161 0.0106  -0.0209 -0.0135 945  VAL B CA  
16058 C C   . VAL B 947  ? 0.2145 0.2201 0.2428 0.0091  -0.0209 -0.0144 945  VAL B C   
16059 O O   . VAL B 947  ? 0.2162 0.2223 0.2451 0.0086  -0.0198 -0.0149 945  VAL B O   
16060 C CB  . VAL B 947  ? 0.2046 0.2153 0.2412 0.0106  -0.0211 -0.0130 945  VAL B CB  
16061 C CG1 . VAL B 947  ? 0.1948 0.2062 0.2321 0.0095  -0.0236 -0.0126 945  VAL B CG1 
16062 C CG2 . VAL B 947  ? 0.2093 0.2218 0.2490 0.0124  -0.0206 -0.0122 945  VAL B CG2 
16063 N N   . LEU B 948  ? 0.1881 0.1916 0.2128 0.0086  -0.0222 -0.0145 946  LEU B N   
16064 C CA  . LEU B 948  ? 0.1927 0.1944 0.2138 0.0075  -0.0223 -0.0154 946  LEU B CA  
16065 C C   . LEU B 948  ? 0.1851 0.1871 0.2066 0.0065  -0.0245 -0.0154 946  LEU B C   
16066 O O   . LEU B 948  ? 0.1998 0.2021 0.2216 0.0065  -0.0265 -0.0147 946  LEU B O   
16067 C CB  . LEU B 948  ? 0.1835 0.1829 0.2001 0.0075  -0.0223 -0.0155 946  LEU B CB  
16068 C CG  . LEU B 948  ? 0.1864 0.1841 0.1991 0.0066  -0.0221 -0.0165 946  LEU B CG  
16069 C CD1 . LEU B 948  ? 0.1904 0.1884 0.2034 0.0066  -0.0201 -0.0173 946  LEU B CD1 
16070 C CD2 . LEU B 948  ? 0.2621 0.2579 0.2705 0.0065  -0.0222 -0.0163 946  LEU B CD2 
16071 N N   . HIS B 949  ? 0.1798 0.1815 0.2012 0.0055  -0.0244 -0.0162 947  HIS B N   
16072 C CA  . HIS B 949  ? 0.1759 0.1773 0.1972 0.0043  -0.0265 -0.0164 947  HIS B CA  
16073 C C   . HIS B 949  ? 0.1932 0.1916 0.2091 0.0037  -0.0268 -0.0175 947  HIS B C   
16074 O O   . HIS B 949  ? 0.2348 0.2319 0.2483 0.0040  -0.0250 -0.0182 947  HIS B O   
16075 C CB  . HIS B 949  ? 0.1960 0.1986 0.2205 0.0035  -0.0263 -0.0166 947  HIS B CB  
16076 C CG  . HIS B 949  ? 0.1873 0.1932 0.2170 0.0042  -0.0255 -0.0155 947  HIS B CG  
16077 N ND1 . HIS B 949  ? 0.1981 0.2048 0.2289 0.0052  -0.0231 -0.0154 947  HIS B ND1 
16078 C CD2 . HIS B 949  ? 0.1861 0.1950 0.2200 0.0041  -0.0268 -0.0145 947  HIS B CD2 
16079 C CE1 . HIS B 949  ? 0.1933 0.2030 0.2286 0.0058  -0.0228 -0.0145 947  HIS B CE1 
16080 N NE2 . HIS B 949  ? 0.1976 0.2089 0.2351 0.0052  -0.0250 -0.0139 947  HIS B NE2 
16081 N N   . VAL B 950  ? 0.2116 0.2090 0.2255 0.0029  -0.0291 -0.0176 948  VAL B N   
16082 C CA  . VAL B 950  ? 0.2130 0.2075 0.2214 0.0025  -0.0294 -0.0186 948  VAL B CA  
16083 C C   . VAL B 950  ? 0.2166 0.2097 0.2240 0.0011  -0.0311 -0.0195 948  VAL B C   
16084 O O   . VAL B 950  ? 0.2339 0.2281 0.2435 0.0002  -0.0333 -0.0190 948  VAL B O   
16085 C CB  . VAL B 950  ? 0.2189 0.2127 0.2244 0.0027  -0.0306 -0.0179 948  VAL B CB  
16086 C CG1 . VAL B 950  ? 0.2500 0.2410 0.2496 0.0021  -0.0311 -0.0190 948  VAL B CG1 
16087 C CG2 . VAL B 950  ? 0.2462 0.2406 0.2520 0.0039  -0.0289 -0.0172 948  VAL B CG2 
16088 N N   . ILE B 951  ? 0.2199 0.2106 0.2238 0.0010  -0.0300 -0.0209 949  ILE B N   
16089 C CA  . ILE B 951  ? 0.2229 0.2112 0.2246 -0.0001 -0.0315 -0.0221 949  ILE B CA  
16090 C C   . ILE B 951  ? 0.2245 0.2100 0.2199 0.0001  -0.0314 -0.0232 949  ILE B C   
16091 O O   . ILE B 951  ? 0.2378 0.2230 0.2311 0.0012  -0.0292 -0.0234 949  ILE B O   
16092 C CB  . ILE B 951  ? 0.2660 0.2536 0.2693 -0.0002 -0.0300 -0.0228 949  ILE B CB  
16093 C CG1 . ILE B 951  ? 0.3158 0.3063 0.3251 -0.0007 -0.0302 -0.0216 949  ILE B CG1 
16094 C CG2 . ILE B 951  ? 0.3794 0.3635 0.3792 -0.0012 -0.0312 -0.0243 949  ILE B CG2 
16095 C CD1 . ILE B 951  ? 0.4185 0.4084 0.4294 -0.0009 -0.0289 -0.0220 949  ILE B CD1 
16096 N N   . ARG B 952  ? 0.2266 0.2102 0.2190 -0.0010 -0.0337 -0.0238 950  ARG B N   
16097 C CA  A ARG B 952  ? 0.2312 0.2117 0.2172 -0.0009 -0.0336 -0.0251 950  ARG B CA  
16098 C CA  B ARG B 952  ? 0.2323 0.2128 0.2183 -0.0009 -0.0337 -0.0251 950  ARG B CA  
16099 C C   . ARG B 952  ? 0.2490 0.2264 0.2329 -0.0013 -0.0336 -0.0269 950  ARG B C   
16100 O O   . ARG B 952  ? 0.3034 0.2804 0.2896 -0.0025 -0.0352 -0.0270 950  ARG B O   
16101 C CB  A ARG B 952  ? 0.2511 0.2312 0.2345 -0.0017 -0.0363 -0.0247 950  ARG B CB  
16102 C CB  B ARG B 952  ? 0.2515 0.2314 0.2348 -0.0018 -0.0364 -0.0248 950  ARG B CB  
16103 C CG  A ARG B 952  ? 0.2667 0.2494 0.2523 -0.0012 -0.0366 -0.0229 950  ARG B CG  
16104 C CG  B ARG B 952  ? 0.2819 0.2639 0.2657 -0.0012 -0.0365 -0.0232 950  ARG B CG  
16105 C CD  A ARG B 952  ? 0.3332 0.3162 0.3181 -0.0021 -0.0398 -0.0221 950  ARG B CD  
16106 C CD  B ARG B 952  ? 0.3256 0.3072 0.3075 -0.0022 -0.0397 -0.0227 950  ARG B CD  
16107 N NE  A ARG B 952  ? 0.3621 0.3476 0.3497 -0.0015 -0.0402 -0.0202 950  ARG B NE  
16108 N NE  B ARG B 952  ? 0.3618 0.3444 0.3426 -0.0015 -0.0399 -0.0212 950  ARG B NE  
16109 C CZ  A ARG B 952  ? 0.3584 0.3433 0.3426 -0.0010 -0.0404 -0.0195 950  ARG B CZ  
16110 C CZ  B ARG B 952  ? 0.3633 0.3485 0.3485 -0.0009 -0.0398 -0.0195 950  ARG B CZ  
16111 N NH1 A ARG B 952  ? 0.2941 0.2764 0.2720 -0.0013 -0.0403 -0.0204 950  ARG B NH1 
16112 N NH1 B ARG B 952  ? 0.3586 0.3462 0.3498 -0.0007 -0.0394 -0.0191 950  ARG B NH1 
16113 N NH2 A ARG B 952  ? 0.3807 0.3675 0.3677 -0.0004 -0.0409 -0.0177 950  ARG B NH2 
16114 N NH2 B ARG B 952  ? 0.3723 0.3576 0.3557 -0.0004 -0.0402 -0.0183 950  ARG B NH2 
16115 N N   . TYR B 953  ? 0.2381 0.2133 0.2175 -0.0004 -0.0318 -0.0282 951  TYR B N   
16116 C CA  . TYR B 953  ? 0.2462 0.2179 0.2233 -0.0005 -0.0317 -0.0300 951  TYR B CA  
16117 C C   . TYR B 953  ? 0.2509 0.2195 0.2211 0.0001  -0.0314 -0.0316 951  TYR B C   
16118 O O   . TYR B 953  ? 0.2605 0.2301 0.2282 0.0010  -0.0302 -0.0313 951  TYR B O   
16119 C CB  . TYR B 953  ? 0.2468 0.2189 0.2266 0.0005  -0.0293 -0.0301 951  TYR B CB  
16120 C CG  . TYR B 953  ? 0.2235 0.1964 0.2015 0.0023  -0.0264 -0.0302 951  TYR B CG  
16121 C CD1 . TYR B 953  ? 0.1987 0.1751 0.1791 0.0030  -0.0251 -0.0288 951  TYR B CD1 
16122 C CD2 . TYR B 953  ? 0.2200 0.1903 0.1938 0.0034  -0.0251 -0.0319 951  TYR B CD2 
16123 C CE1 . TYR B 953  ? 0.2186 0.1959 0.1975 0.0043  -0.0226 -0.0289 951  TYR B CE1 
16124 C CE2 . TYR B 953  ? 0.2517 0.2232 0.2241 0.0050  -0.0225 -0.0319 951  TYR B CE2 
16125 C CZ  . TYR B 953  ? 0.2440 0.2192 0.2191 0.0053  -0.0213 -0.0304 951  TYR B CZ  
16126 O OH  . TYR B 953  ? 0.2521 0.2288 0.2260 0.0067  -0.0189 -0.0304 951  TYR B OH  
16127 N N   . ARG B 954  ? 0.2924 0.2571 0.2595 -0.0005 -0.0325 -0.0333 952  ARG B N   
16128 C CA  . ARG B 954  ? 0.3535 0.3147 0.3138 0.0003  -0.0319 -0.0352 952  ARG B CA  
16129 C C   . ARG B 954  ? 0.3311 0.2915 0.2911 0.0022  -0.0289 -0.0361 952  ARG B C   
16130 O O   . ARG B 954  ? 0.2960 0.2562 0.2596 0.0022  -0.0285 -0.0360 952  ARG B O   
16131 C CB  . ARG B 954  ? 0.3626 0.3195 0.3193 -0.0012 -0.0346 -0.0368 952  ARG B CB  
16132 N N   . ARG B 955  ? 0.3143 0.2744 0.2701 0.0037  -0.0269 -0.0369 953  ARG B N   
16133 C CA  . ARG B 955  ? 0.3418 0.3020 0.2977 0.0057  -0.0239 -0.0375 953  ARG B CA  
16134 C C   . ARG B 955  ? 0.3244 0.2803 0.2795 0.0060  -0.0242 -0.0391 953  ARG B C   
16135 O O   . ARG B 955  ? 0.3241 0.2804 0.2819 0.0071  -0.0225 -0.0390 953  ARG B O   
16136 C CB  . ARG B 955  ? 0.4008 0.3613 0.3518 0.0073  -0.0218 -0.0382 953  ARG B CB  
16137 C CG  . ARG B 955  ? 0.4009 0.3622 0.3524 0.0096  -0.0187 -0.0387 953  ARG B CG  
16138 C CD  . ARG B 955  ? 0.3853 0.3504 0.3432 0.0098  -0.0175 -0.0370 953  ARG B CD  
16139 N NE  . ARG B 955  ? 0.4136 0.3797 0.3718 0.0120  -0.0147 -0.0374 953  ARG B NE  
16140 C CZ  . ARG B 955  ? 0.4596 0.4228 0.4172 0.0132  -0.0140 -0.0387 953  ARG B CZ  
16141 N NH1 . ARG B 955  ? 0.4537 0.4126 0.4103 0.0124  -0.0160 -0.0398 953  ARG B NH1 
16142 N NH2 . ARG B 955  ? 0.3966 0.3614 0.3547 0.0153  -0.0115 -0.0389 953  ARG B NH2 
16143 N N   . ASP B 956  ? 0.3336 0.2852 0.2847 0.0049  -0.0264 -0.0406 954  ASP B N   
16144 C CA  A ASP B 956  ? 0.3478 0.2947 0.2978 0.0050  -0.0269 -0.0422 954  ASP B CA  
16145 C CA  B ASP B 956  ? 0.3474 0.2943 0.2974 0.0050  -0.0268 -0.0422 954  ASP B CA  
16146 C C   . ASP B 956  ? 0.3509 0.2985 0.3069 0.0036  -0.0279 -0.0410 954  ASP B C   
16147 O O   . ASP B 956  ? 0.4116 0.3557 0.3676 0.0038  -0.0279 -0.0419 954  ASP B O   
16148 C CB  A ASP B 956  ? 0.3741 0.3160 0.3183 0.0038  -0.0293 -0.0441 954  ASP B CB  
16149 C CB  B ASP B 956  ? 0.3739 0.3154 0.3175 0.0043  -0.0289 -0.0444 954  ASP B CB  
16150 C CG  A ASP B 956  ? 0.4332 0.3735 0.3706 0.0054  -0.0280 -0.0457 954  ASP B CG  
16151 C CG  B ASP B 956  ? 0.3556 0.2973 0.2991 0.0016  -0.0323 -0.0438 954  ASP B CG  
16152 O OD1 A ASP B 956  ? 0.4818 0.4240 0.4189 0.0077  -0.0250 -0.0458 954  ASP B OD1 
16153 O OD1 B ASP B 956  ? 0.3988 0.3443 0.3479 0.0002  -0.0334 -0.0418 954  ASP B OD1 
16154 O OD2 A ASP B 956  ? 0.4532 0.3908 0.3856 0.0043  -0.0301 -0.0468 954  ASP B OD2 
16155 O OD2 B ASP B 956  ? 0.4260 0.3641 0.3637 0.0010  -0.0339 -0.0454 954  ASP B OD2 
16156 N N   . ASP B 957  ? 0.3105 0.2625 0.2715 0.0024  -0.0287 -0.0389 955  ASP B N   
16157 C CA  . ASP B 957  ? 0.3235 0.2770 0.2905 0.0012  -0.0294 -0.0375 955  ASP B CA  
16158 C C   . ASP B 957  ? 0.2787 0.2361 0.2502 0.0026  -0.0267 -0.0361 955  ASP B C   
16159 O O   . ASP B 957  ? 0.2877 0.2474 0.2644 0.0017  -0.0270 -0.0346 955  ASP B O   
16160 C CB  . ASP B 957  ? 0.3310 0.2869 0.3008 -0.0011 -0.0320 -0.0362 955  ASP B CB  
16161 C CG  . ASP B 957  ? 0.4738 0.4260 0.4404 -0.0030 -0.0351 -0.0374 955  ASP B CG  
16162 O OD1 . ASP B 957  ? 0.4419 0.3891 0.4050 -0.0030 -0.0354 -0.0392 955  ASP B OD1 
16163 O OD2 . ASP B 957  ? 0.5302 0.4842 0.4974 -0.0045 -0.0374 -0.0366 955  ASP B OD2 
16164 N N   . LEU B 958  ? 0.2680 0.2264 0.2375 0.0047  -0.0242 -0.0364 956  LEU B N   
16165 C CA  . LEU B 958  ? 0.2504 0.2127 0.2239 0.0059  -0.0219 -0.0351 956  LEU B CA  
16166 C C   . LEU B 958  ? 0.2586 0.2201 0.2355 0.0061  -0.0214 -0.0347 956  LEU B C   
16167 O O   . LEU B 958  ? 0.2427 0.2075 0.2245 0.0057  -0.0209 -0.0331 956  LEU B O   
16168 C CB  . LEU B 958  ? 0.2569 0.2200 0.2274 0.0081  -0.0194 -0.0357 956  LEU B CB  
16169 C CG  . LEU B 958  ? 0.2447 0.2118 0.2189 0.0094  -0.0171 -0.0344 956  LEU B CG  
16170 C CD1 . LEU B 958  ? 0.2642 0.2354 0.2424 0.0083  -0.0175 -0.0325 956  LEU B CD1 
16171 C CD2 . LEU B 958  ? 0.3025 0.2707 0.2737 0.0113  -0.0148 -0.0350 956  LEU B CD2 
16172 N N   . ASP B 959  ? 0.2466 0.2035 0.2208 0.0065  -0.0215 -0.0362 957  ASP B N   
16173 C CA  . ASP B 959  ? 0.2361 0.1918 0.2132 0.0067  -0.0210 -0.0357 957  ASP B CA  
16174 C C   . ASP B 959  ? 0.2452 0.2020 0.2267 0.0043  -0.0228 -0.0344 957  ASP B C   
16175 O O   . ASP B 959  ? 0.2431 0.2020 0.2289 0.0042  -0.0220 -0.0330 957  ASP B O   
16176 C CB  . ASP B 959  ? 0.2648 0.2147 0.2378 0.0076  -0.0210 -0.0376 957  ASP B CB  
16177 C CG  . ASP B 959  ? 0.2749 0.2240 0.2502 0.0088  -0.0196 -0.0371 957  ASP B CG  
16178 O OD1 . ASP B 959  ? 0.2678 0.2208 0.2457 0.0102  -0.0175 -0.0360 957  ASP B OD1 
16179 O OD2 . ASP B 959  ? 0.2936 0.2380 0.2679 0.0082  -0.0206 -0.0377 957  ASP B OD2 
16180 N N   . ARG B 960  ? 0.2483 0.2037 0.2289 0.0023  -0.0253 -0.0347 958  ARG B N   
16181 C CA  . ARG B 960  ? 0.2438 0.2009 0.2288 -0.0001 -0.0272 -0.0333 958  ARG B CA  
16182 C C   . ARG B 960  ? 0.2344 0.1973 0.2240 -0.0001 -0.0264 -0.0314 958  ARG B C   
16183 O O   . ARG B 960  ? 0.2370 0.2024 0.2315 -0.0010 -0.0265 -0.0300 958  ARG B O   
16184 C CB  . ARG B 960  ? 0.2899 0.2446 0.2726 -0.0022 -0.0301 -0.0342 958  ARG B CB  
16185 N N   . LEU B 961  ? 0.2247 0.1899 0.2127 0.0010  -0.0257 -0.0314 959  LEU B N   
16186 C CA  . LEU B 961  ? 0.2125 0.1828 0.2045 0.0013  -0.0249 -0.0297 959  LEU B CA  
16187 C C   . LEU B 961  ? 0.2136 0.1859 0.2087 0.0024  -0.0225 -0.0288 959  LEU B C   
16188 O O   . LEU B 961  ? 0.2160 0.1915 0.2156 0.0019  -0.0223 -0.0274 959  LEU B O   
16189 C CB  . LEU B 961  ? 0.2346 0.2062 0.2237 0.0022  -0.0244 -0.0300 959  LEU B CB  
16190 C CG  . LEU B 961  ? 0.2281 0.2042 0.2206 0.0026  -0.0235 -0.0283 959  LEU B CG  
16191 C CD1 . LEU B 961  ? 0.2794 0.2576 0.2757 0.0010  -0.0254 -0.0271 959  LEU B CD1 
16192 C CD2 . LEU B 961  ? 0.2533 0.2302 0.2425 0.0035  -0.0227 -0.0285 959  LEU B CD2 
16193 N N   . VAL B 962  ? 0.2055 0.1759 0.1982 0.0041  -0.0208 -0.0297 960  VAL B N   
16194 C CA  . VAL B 962  ? 0.2183 0.1904 0.2138 0.0051  -0.0188 -0.0289 960  VAL B CA  
16195 C C   . VAL B 962  ? 0.2226 0.1942 0.2215 0.0038  -0.0195 -0.0280 960  VAL B C   
16196 O O   . VAL B 962  ? 0.2135 0.1881 0.2163 0.0038  -0.0186 -0.0266 960  VAL B O   
16197 C CB  . VAL B 962  ? 0.2299 0.2000 0.2222 0.0072  -0.0170 -0.0300 960  VAL B CB  
16198 C CG1 . VAL B 962  ? 0.2590 0.2304 0.2541 0.0081  -0.0154 -0.0290 960  VAL B CG1 
16199 C CG2 . VAL B 962  ? 0.2341 0.2061 0.2239 0.0084  -0.0160 -0.0304 960  VAL B CG2 
16200 N N   . ASP B 963  ? 0.2111 0.1787 0.2085 0.0026  -0.0212 -0.0288 961  ASP B N   
16201 C CA  . ASP B 963  ? 0.2295 0.1967 0.2304 0.0009  -0.0220 -0.0278 961  ASP B CA  
16202 C C   . ASP B 963  ? 0.2421 0.2138 0.2476 -0.0005 -0.0228 -0.0262 961  ASP B C   
16203 O O   . ASP B 963  ? 0.2372 0.2111 0.2466 -0.0010 -0.0221 -0.0248 961  ASP B O   
16204 C CB  . ASP B 963  ? 0.2420 0.2043 0.2404 -0.0007 -0.0242 -0.0289 961  ASP B CB  
16205 C CG  . ASP B 963  ? 0.2904 0.2478 0.2848 0.0007  -0.0235 -0.0304 961  ASP B CG  
16206 O OD1 . ASP B 963  ? 0.3061 0.2639 0.3007 0.0026  -0.0214 -0.0301 961  ASP B OD1 
16207 O OD2 . ASP B 963  ? 0.3137 0.2664 0.3045 -0.0002 -0.0252 -0.0318 961  ASP B OD2 
16208 N N   . ASP B 964  ? 0.2185 0.1915 0.2233 -0.0011 -0.0242 -0.0264 962  ASP B N   
16209 C CA  . ASP B 964  ? 0.2292 0.2065 0.2384 -0.0022 -0.0250 -0.0250 962  ASP B CA  
16210 C C   . ASP B 964  ? 0.2244 0.2058 0.2365 -0.0008 -0.0228 -0.0238 962  ASP B C   
16211 O O   . ASP B 964  ? 0.2238 0.2082 0.2403 -0.0014 -0.0226 -0.0224 962  ASP B O   
16212 C CB  . ASP B 964  ? 0.2382 0.2160 0.2457 -0.0026 -0.0268 -0.0254 962  ASP B CB  
16213 C CG  . ASP B 964  ? 0.3043 0.2787 0.3094 -0.0044 -0.0294 -0.0264 962  ASP B CG  
16214 O OD1 . ASP B 964  ? 0.3058 0.2777 0.3113 -0.0056 -0.0300 -0.0266 962  ASP B OD1 
16215 O OD2 . ASP B 964  ? 0.3606 0.3347 0.3632 -0.0047 -0.0309 -0.0269 962  ASP B OD2 
16216 N N   . VAL B 965  ? 0.1967 0.1780 0.2063 0.0010  -0.0211 -0.0243 963  VAL B N   
16217 C CA  . VAL B 965  ? 0.1824 0.1671 0.1944 0.0022  -0.0191 -0.0233 963  VAL B CA  
16218 C C   . VAL B 965  ? 0.2032 0.1881 0.2175 0.0022  -0.0179 -0.0226 963  VAL B C   
16219 O O   . VAL B 965  ? 0.2155 0.2034 0.2335 0.0021  -0.0172 -0.0213 963  VAL B O   
16220 C CB  . VAL B 965  ? 0.1914 0.1760 0.2001 0.0039  -0.0177 -0.0240 963  VAL B CB  
16221 C CG1 . VAL B 965  ? 0.1967 0.1843 0.2076 0.0050  -0.0157 -0.0231 963  VAL B CG1 
16222 C CG2 . VAL B 965  ? 0.2272 0.2120 0.2337 0.0037  -0.0189 -0.0244 963  VAL B CG2 
16223 N N   . ASN B 966  ? 0.2065 0.1879 0.2188 0.0024  -0.0177 -0.0233 964  ASN B N   
16224 C CA  . ASN B 966  ? 0.2081 0.1894 0.2223 0.0025  -0.0166 -0.0225 964  ASN B CA  
16225 C C   . ASN B 966  ? 0.2142 0.1963 0.2321 0.0005  -0.0176 -0.0213 964  ASN B C   
16226 O O   . ASN B 966  ? 0.2315 0.2152 0.2521 0.0004  -0.0165 -0.0201 964  ASN B O   
16227 C CB  . ASN B 966  ? 0.2135 0.1903 0.2244 0.0032  -0.0163 -0.0235 964  ASN B CB  
16228 C CG  . ASN B 966  ? 0.1995 0.1762 0.2076 0.0054  -0.0148 -0.0243 964  ASN B CG  
16229 O OD1 . ASN B 966  ? 0.2184 0.1984 0.2275 0.0064  -0.0135 -0.0238 964  ASN B OD1 
16230 N ND2 . ASN B 966  ? 0.2226 0.1954 0.2271 0.0063  -0.0149 -0.0257 964  ASN B ND2 
16231 N N   . ALA B 967  ? 0.2059 0.1874 0.2240 -0.0011 -0.0197 -0.0216 965  ALA B N   
16232 C CA  . ALA B 967  ? 0.2102 0.1923 0.2316 -0.0032 -0.0209 -0.0206 965  ALA B CA  
16233 C C   . ALA B 967  ? 0.2155 0.2028 0.2418 -0.0035 -0.0203 -0.0190 965  ALA B C   
16234 O O   . ALA B 967  ? 0.2376 0.2263 0.2673 -0.0052 -0.0208 -0.0178 965  ALA B O   
16235 C CB  . ALA B 967  ? 0.2353 0.2155 0.2555 -0.0050 -0.0236 -0.0214 965  ALA B CB  
16236 N N   . THR B 968  ? 0.1981 0.1883 0.2247 -0.0020 -0.0192 -0.0188 966  THR B N   
16237 C CA  . THR B 968  ? 0.2050 0.1999 0.2359 -0.0019 -0.0184 -0.0174 966  THR B CA  
16238 C C   . THR B 968  ? 0.2097 0.2055 0.2424 -0.0017 -0.0164 -0.0164 966  THR B C   
16239 O O   . THR B 968  ? 0.2208 0.2201 0.2574 -0.0021 -0.0158 -0.0152 966  THR B O   
16240 C CB  . THR B 968  ? 0.2083 0.2053 0.2386 -0.0003 -0.0175 -0.0176 966  THR B CB  
16241 O OG1 . THR B 968  ? 0.2075 0.2036 0.2356 0.0013  -0.0156 -0.0180 966  THR B OG1 
16242 C CG2 . THR B 968  ? 0.2226 0.2183 0.2504 -0.0003 -0.0192 -0.0186 966  THR B CG2 
16243 N N   . GLY B 969  ? 0.2036 0.1963 0.2336 -0.0010 -0.0155 -0.0169 967  GLY B N   
16244 C CA  . GLY B 969  ? 0.2086 0.2019 0.2396 -0.0006 -0.0137 -0.0160 967  GLY B CA  
16245 C C   . GLY B 969  ? 0.1999 0.1953 0.2304 0.0013  -0.0118 -0.0159 967  GLY B C   
16246 O O   . GLY B 969  ? 0.1994 0.1947 0.2297 0.0019  -0.0104 -0.0154 967  GLY B O   
16247 N N   . TYR B 970  ? 0.1908 0.1877 0.2207 0.0022  -0.0119 -0.0165 968  TYR B N   
16248 C CA  . TYR B 970  ? 0.1708 0.1691 0.1997 0.0038  -0.0104 -0.0166 968  TYR B CA  
16249 C C   . TYR B 970  ? 0.1736 0.1694 0.1988 0.0049  -0.0101 -0.0177 968  TYR B C   
16250 O O   . TYR B 970  ? 0.2135 0.2063 0.2365 0.0046  -0.0111 -0.0186 968  TYR B O   
16251 C CB  . TYR B 970  ? 0.1854 0.1861 0.2153 0.0041  -0.0107 -0.0167 968  TYR B CB  
16252 C CG  . TYR B 970  ? 0.2036 0.2077 0.2375 0.0037  -0.0104 -0.0155 968  TYR B CG  
16253 C CD1 . TYR B 970  ? 0.2265 0.2325 0.2614 0.0045  -0.0086 -0.0149 968  TYR B CD1 
16254 C CD2 . TYR B 970  ? 0.2355 0.2408 0.2719 0.0026  -0.0119 -0.0151 968  TYR B CD2 
16255 C CE1 . TYR B 970  ? 0.2812 0.2903 0.3196 0.0044  -0.0080 -0.0139 968  TYR B CE1 
16256 C CE2 . TYR B 970  ? 0.2534 0.2624 0.2939 0.0025  -0.0113 -0.0140 968  TYR B CE2 
16257 C CZ  . TYR B 970  ? 0.2856 0.2963 0.3268 0.0035  -0.0093 -0.0135 968  TYR B CZ  
16258 O OH  . TYR B 970  ? 0.3490 0.3633 0.3939 0.0036  -0.0084 -0.0125 968  TYR B OH  
16259 N N   . GLY B 971  ? 0.1725 0.1695 0.1967 0.0062  -0.0087 -0.0177 969  GLY B N   
16260 C CA  . GLY B 971  ? 0.1787 0.1740 0.1998 0.0073  -0.0082 -0.0186 969  GLY B CA  
16261 C C   . GLY B 971  ? 0.1633 0.1608 0.1840 0.0084  -0.0069 -0.0184 969  GLY B C   
16262 O O   . GLY B 971  ? 0.1715 0.1690 0.1914 0.0092  -0.0059 -0.0183 969  GLY B O   
16263 N N   . LEU B 972  ? 0.1552 0.1545 0.1764 0.0083  -0.0070 -0.0184 970  LEU B N   
16264 C CA  . LEU B 972  ? 0.1627 0.1638 0.1835 0.0091  -0.0059 -0.0183 970  LEU B CA  
16265 C C   . LEU B 972  ? 0.1529 0.1536 0.1710 0.0096  -0.0059 -0.0191 970  LEU B C   
16266 O O   . LEU B 972  ? 0.1708 0.1711 0.1874 0.0103  -0.0053 -0.0194 970  LEU B O   
16267 C CB  . LEU B 972  ? 0.1745 0.1776 0.1974 0.0088  -0.0057 -0.0177 970  LEU B CB  
16268 C CG  . LEU B 972  ? 0.1613 0.1659 0.1839 0.0094  -0.0046 -0.0176 970  LEU B CG  
16269 C CD1 . LEU B 972  ? 0.2024 0.2074 0.2248 0.0098  -0.0034 -0.0172 970  LEU B CD1 
16270 C CD2 . LEU B 972  ? 0.1977 0.2038 0.2223 0.0093  -0.0045 -0.0171 970  LEU B CD2 
16271 N N   . THR B 973  ? 0.1537 0.1546 0.1714 0.0093  -0.0067 -0.0193 971  THR B N   
16272 C CA  . THR B 973  ? 0.1561 0.1567 0.1712 0.0096  -0.0067 -0.0199 971  THR B CA  
16273 C C   . THR B 973  ? 0.1477 0.1463 0.1611 0.0092  -0.0079 -0.0206 971  THR B C   
16274 O O   . THR B 973  ? 0.1701 0.1681 0.1848 0.0085  -0.0091 -0.0205 971  THR B O   
16275 C CB  . THR B 973  ? 0.1478 0.1496 0.1627 0.0095  -0.0065 -0.0196 971  THR B CB  
16276 O OG1 . THR B 973  ? 0.1619 0.1637 0.1782 0.0090  -0.0075 -0.0193 971  THR B OG1 
16277 C CG2 . THR B 973  ? 0.1726 0.1760 0.1885 0.0098  -0.0053 -0.0192 971  THR B CG2 
16278 N N   . PHE B 974  ? 0.1540 0.1521 0.1647 0.0097  -0.0077 -0.0212 972  PHE B N   
16279 C CA  . PHE B 974  ? 0.1468 0.1429 0.1552 0.0094  -0.0087 -0.0220 972  PHE B CA  
16280 C C   . PHE B 974  ? 0.1633 0.1599 0.1690 0.0099  -0.0081 -0.0224 972  PHE B C   
16281 O O   . PHE B 974  ? 0.1588 0.1566 0.1640 0.0106  -0.0068 -0.0224 972  PHE B O   
16282 C CB  . PHE B 974  ? 0.1673 0.1612 0.1750 0.0098  -0.0089 -0.0227 972  PHE B CB  
16283 C CG  . PHE B 974  ? 0.1646 0.1563 0.1692 0.0097  -0.0097 -0.0238 972  PHE B CG  
16284 C CD1 . PHE B 974  ? 0.1816 0.1718 0.1861 0.0087  -0.0115 -0.0239 972  PHE B CD1 
16285 C CD2 . PHE B 974  ? 0.1804 0.1716 0.1821 0.0108  -0.0088 -0.0245 972  PHE B CD2 
16286 C CE1 . PHE B 974  ? 0.1926 0.1805 0.1937 0.0085  -0.0124 -0.0250 972  PHE B CE1 
16287 C CE2 . PHE B 974  ? 0.1892 0.1783 0.1877 0.0108  -0.0095 -0.0256 972  PHE B CE2 
16288 C CZ  . PHE B 974  ? 0.1970 0.1842 0.1949 0.0097  -0.0113 -0.0259 972  PHE B CZ  
16289 N N   . GLY B 975  ? 0.1656 0.1615 0.1695 0.0093  -0.0091 -0.0226 973  GLY B N   
16290 C CA  . GLY B 975  ? 0.1694 0.1656 0.1704 0.0095  -0.0086 -0.0229 973  GLY B CA  
16291 C C   . GLY B 975  ? 0.1669 0.1610 0.1647 0.0096  -0.0093 -0.0239 973  GLY B C   
16292 O O   . GLY B 975  ? 0.1818 0.1740 0.1793 0.0091  -0.0107 -0.0242 973  GLY B O   
16293 N N   . LEU B 976  ? 0.1709 0.1656 0.1662 0.0102  -0.0082 -0.0243 974  LEU B N   
16294 C CA  . LEU B 976  ? 0.1752 0.1680 0.1667 0.0105  -0.0085 -0.0253 974  LEU B CA  
16295 C C   . LEU B 976  ? 0.1873 0.1816 0.1765 0.0104  -0.0077 -0.0250 974  LEU B C   
16296 O O   . LEU B 976  ? 0.1948 0.1915 0.1846 0.0108  -0.0061 -0.0246 974  LEU B O   
16297 C CB  . LEU B 976  ? 0.2004 0.1920 0.1909 0.0118  -0.0076 -0.0264 974  LEU B CB  
16298 C CG  . LEU B 976  ? 0.2114 0.2009 0.1976 0.0124  -0.0076 -0.0277 974  LEU B CG  
16299 C CD1 . LEU B 976  ? 0.2429 0.2294 0.2276 0.0113  -0.0097 -0.0283 974  LEU B CD1 
16300 C CD2 . LEU B 976  ? 0.2312 0.2197 0.2167 0.0141  -0.0064 -0.0287 974  LEU B CD2 
16301 N N   . HIS B 977  ? 0.1936 0.1867 0.1802 0.0096  -0.0088 -0.0251 975  HIS B N   
16302 C CA  . HIS B 977  ? 0.1994 0.1936 0.1832 0.0094  -0.0081 -0.0247 975  HIS B CA  
16303 C C   . HIS B 977  ? 0.1977 0.1900 0.1772 0.0100  -0.0080 -0.0260 975  HIS B C   
16304 O O   . HIS B 977  ? 0.2031 0.1929 0.1807 0.0095  -0.0097 -0.0266 975  HIS B O   
16305 C CB  . HIS B 977  ? 0.2236 0.2177 0.2072 0.0081  -0.0094 -0.0236 975  HIS B CB  
16306 C CG  . HIS B 977  ? 0.2117 0.2079 0.1979 0.0077  -0.0087 -0.0224 975  HIS B CG  
16307 N ND1 . HIS B 977  ? 0.3000 0.2975 0.2848 0.0071  -0.0079 -0.0215 975  HIS B ND1 
16308 C CD2 . HIS B 977  ? 0.3090 0.3060 0.2990 0.0077  -0.0088 -0.0219 975  HIS B CD2 
16309 C CE1 . HIS B 977  ? 0.2639 0.2627 0.2514 0.0067  -0.0077 -0.0206 975  HIS B CE1 
16310 N NE2 . HIS B 977  ? 0.2845 0.2829 0.2750 0.0071  -0.0081 -0.0208 975  HIS B NE2 
16311 N N   . THR B 978  ? 0.1945 0.1882 0.1726 0.0111  -0.0061 -0.0265 976  THR B N   
16312 C CA  . THR B 978  ? 0.2024 0.1947 0.1762 0.0119  -0.0056 -0.0278 976  THR B CA  
16313 C C   . THR B 978  ? 0.1997 0.1951 0.1729 0.0129  -0.0032 -0.0277 976  THR B C   
16314 O O   . THR B 978  ? 0.2281 0.2263 0.2045 0.0132  -0.0020 -0.0270 976  THR B O   
16315 C CB  . THR B 978  ? 0.2240 0.2133 0.1974 0.0130  -0.0061 -0.0294 976  THR B CB  
16316 O OG1 . THR B 978  ? 0.2274 0.2150 0.1963 0.0140  -0.0054 -0.0308 976  THR B OG1 
16317 C CG2 . THR B 978  ? 0.2699 0.2605 0.2465 0.0142  -0.0047 -0.0294 976  THR B CG2 
16318 N N   . ARG B 979  ? 0.2304 0.2256 0.1995 0.0133  -0.0024 -0.0284 977  ARG B N   
16319 C CA  . ARG B 979  ? 0.2419 0.2403 0.2102 0.0145  0.0001  -0.0284 977  ARG B CA  
16320 C C   . ARG B 979  ? 0.2501 0.2473 0.2171 0.0167  0.0012  -0.0301 977  ARG B C   
16321 O O   . ARG B 979  ? 0.2601 0.2600 0.2266 0.0181  0.0033  -0.0303 977  ARG B O   
16322 C CB  . ARG B 979  ? 0.2859 0.2853 0.2504 0.0137  0.0007  -0.0279 977  ARG B CB  
16323 C CG  . ARG B 979  ? 0.3449 0.3459 0.3110 0.0117  -0.0001 -0.0260 977  ARG B CG  
16324 C CD  . ARG B 979  ? 0.4377 0.4387 0.3995 0.0106  0.0000  -0.0255 977  ARG B CD  
16325 N NE  . ARG B 979  ? 0.4908 0.4934 0.4540 0.0088  -0.0003 -0.0235 977  ARG B NE  
16326 C CZ  . ARG B 979  ? 0.5590 0.5621 0.5191 0.0076  0.0000  -0.0225 977  ARG B CZ  
16327 N NH1 . ARG B 979  ? 0.4584 0.4609 0.4138 0.0080  0.0006  -0.0232 977  ARG B NH1 
16328 N NH2 . ARG B 979  ? 0.5410 0.5451 0.5026 0.0059  -0.0005 -0.0207 977  ARG B NH2 
16329 N N   . LEU B 980  ? 0.2254 0.2184 0.1917 0.0172  -0.0003 -0.0314 978  LEU B N   
16330 C CA  . LEU B 980  ? 0.2169 0.2075 0.1806 0.0192  0.0005  -0.0333 978  LEU B CA  
16331 C C   . LEU B 980  ? 0.2269 0.2172 0.1940 0.0206  0.0009  -0.0335 978  LEU B C   
16332 O O   . LEU B 980  ? 0.2255 0.2139 0.1951 0.0198  -0.0007 -0.0332 978  LEU B O   
16333 C CB  . LEU B 980  ? 0.2219 0.2074 0.1819 0.0185  -0.0016 -0.0346 978  LEU B CB  
16334 C CG  . LEU B 980  ? 0.2570 0.2423 0.2133 0.0170  -0.0024 -0.0342 978  LEU B CG  
16335 C CD1 . LEU B 980  ? 0.2680 0.2482 0.2206 0.0164  -0.0047 -0.0356 978  LEU B CD1 
16336 C CD2 . LEU B 980  ? 0.2560 0.2438 0.2091 0.0181  0.0000  -0.0344 978  LEU B CD2 
16337 N N   . ASP B 981  ? 0.2279 0.2202 0.1950 0.0228  0.0030  -0.0339 979  ASP B N   
16338 C CA  . ASP B 981  ? 0.2316 0.2241 0.2019 0.0243  0.0035  -0.0340 979  ASP B CA  
16339 C C   . ASP B 981  ? 0.2424 0.2293 0.2117 0.0247  0.0020  -0.0353 979  ASP B C   
16340 O O   . ASP B 981  ? 0.2232 0.2093 0.1957 0.0247  0.0014  -0.0348 979  ASP B O   
16341 C CB  . ASP B 981  ? 0.2518 0.2472 0.2220 0.0269  0.0060  -0.0344 979  ASP B CB  
16342 C CG  . ASP B 981  ? 0.2735 0.2752 0.2462 0.0264  0.0075  -0.0327 979  ASP B CG  
16343 O OD1 . ASP B 981  ? 0.2892 0.2927 0.2645 0.0243  0.0067  -0.0312 979  ASP B OD1 
16344 O OD2 . ASP B 981  ? 0.3083 0.3130 0.2803 0.0283  0.0097  -0.0330 979  ASP B OD2 
16345 N N   . GLU B 982  ? 0.2295 0.2122 0.1941 0.0250  0.0013  -0.0369 980  GLU B N   
16346 C CA  . GLU B 982  ? 0.2396 0.2166 0.2031 0.0251  -0.0003 -0.0382 980  GLU B CA  
16347 C C   . GLU B 982  ? 0.2359 0.2118 0.2021 0.0225  -0.0026 -0.0372 980  GLU B C   
16348 O O   . GLU B 982  ? 0.2372 0.2106 0.2053 0.0224  -0.0036 -0.0372 980  GLU B O   
16349 C CB  . GLU B 982  ? 0.2557 0.2283 0.2133 0.0256  -0.0007 -0.0403 980  GLU B CB  
16350 C CG  . GLU B 982  ? 0.3053 0.2717 0.2615 0.0253  -0.0026 -0.0416 980  GLU B CG  
16351 C CD  . GLU B 982  ? 0.3536 0.3152 0.3038 0.0249  -0.0038 -0.0435 980  GLU B CD  
16352 O OE1 . GLU B 982  ? 0.4228 0.3856 0.3710 0.0234  -0.0045 -0.0433 980  GLU B OE1 
16353 O OE2 . GLU B 982  ? 0.3609 0.3173 0.3082 0.0261  -0.0042 -0.0453 980  GLU B OE2 
16354 N N   . THR B 983  ? 0.2172 0.1951 0.1837 0.0205  -0.0035 -0.0362 981  THR B N   
16355 C CA  . THR B 983  ? 0.2171 0.1944 0.1864 0.0183  -0.0056 -0.0351 981  THR B CA  
16356 C C   . THR B 983  ? 0.2048 0.1851 0.1793 0.0183  -0.0050 -0.0336 981  THR B C   
16357 O O   . THR B 983  ? 0.2204 0.1993 0.1976 0.0174  -0.0063 -0.0332 981  THR B O   
16358 C CB  . THR B 983  ? 0.2458 0.2244 0.2139 0.0165  -0.0066 -0.0344 981  THR B CB  
16359 O OG1 . THR B 983  ? 0.2539 0.2293 0.2169 0.0165  -0.0074 -0.0359 981  THR B OG1 
16360 C CG2 . THR B 983  ? 0.2370 0.2155 0.2084 0.0145  -0.0086 -0.0333 981  THR B CG2 
16361 N N   . ILE B 984  ? 0.2062 0.1908 0.1823 0.0191  -0.0031 -0.0328 982  ILE B N   
16362 C CA  . ILE B 984  ? 0.2038 0.1912 0.1844 0.0192  -0.0026 -0.0314 982  ILE B CA  
16363 C C   . ILE B 984  ? 0.2001 0.1852 0.1818 0.0206  -0.0024 -0.0319 982  ILE B C   
16364 O O   . ILE B 984  ? 0.2141 0.1989 0.1988 0.0198  -0.0032 -0.0311 982  ILE B O   
16365 C CB  . ILE B 984  ? 0.2023 0.1946 0.1838 0.0199  -0.0006 -0.0305 982  ILE B CB  
16366 C CG1 . ILE B 984  ? 0.2451 0.2395 0.2261 0.0181  -0.0010 -0.0297 982  ILE B CG1 
16367 C CG2 . ILE B 984  ? 0.2326 0.2275 0.2183 0.0201  -0.0001 -0.0293 982  ILE B CG2 
16368 C CD1 . ILE B 984  ? 0.2447 0.2434 0.2257 0.0185  0.0009  -0.0290 982  ILE B CD1 
16369 N N   . ALA B 985  ? 0.2122 0.1955 0.1911 0.0226  -0.0014 -0.0332 983  ALA B N   
16370 C CA  . ALA B 985  ? 0.2255 0.2062 0.2052 0.0241  -0.0013 -0.0337 983  ALA B CA  
16371 C C   . ALA B 985  ? 0.2092 0.1851 0.1887 0.0227  -0.0034 -0.0341 983  ALA B C   
16372 O O   . ALA B 985  ? 0.2288 0.2039 0.2111 0.0225  -0.0038 -0.0333 983  ALA B O   
16373 C CB  . ALA B 985  ? 0.2259 0.2052 0.2024 0.0268  0.0002  -0.0352 983  ALA B CB  
16374 N N   . HIS B 986  ? 0.2198 0.1928 0.1961 0.0216  -0.0047 -0.0351 984  HIS B N   
16375 C CA  . HIS B 986  ? 0.2300 0.1986 0.2061 0.0200  -0.0069 -0.0355 984  HIS B CA  
16376 C C   . HIS B 986  ? 0.2165 0.1875 0.1972 0.0180  -0.0079 -0.0337 984  HIS B C   
16377 O O   . HIS B 986  ? 0.2353 0.2047 0.2183 0.0175  -0.0085 -0.0332 984  HIS B O   
16378 C CB  . HIS B 986  ? 0.2517 0.2176 0.2237 0.0189  -0.0083 -0.0368 984  HIS B CB  
16379 C CG  . HIS B 986  ? 0.2590 0.2209 0.2308 0.0169  -0.0107 -0.0371 984  HIS B CG  
16380 N ND1 . HIS B 986  ? 0.3404 0.2992 0.3083 0.0159  -0.0123 -0.0384 984  HIS B ND1 
16381 C CD2 . HIS B 986  ? 0.2703 0.2312 0.2454 0.0156  -0.0119 -0.0363 984  HIS B CD2 
16382 C CE1 . HIS B 986  ? 0.3220 0.2780 0.2909 0.0140  -0.0145 -0.0384 984  HIS B CE1 
16383 N NE2 . HIS B 986  ? 0.2832 0.2404 0.2565 0.0137  -0.0143 -0.0370 984  HIS B NE2 
16384 N N   . VAL B 987  ? 0.2117 0.1862 0.1936 0.0168  -0.0080 -0.0328 985  VAL B N   
16385 C CA  . VAL B 987  ? 0.2137 0.1900 0.1994 0.0150  -0.0090 -0.0313 985  VAL B CA  
16386 C C   . VAL B 987  ? 0.2203 0.1990 0.2098 0.0156  -0.0079 -0.0301 985  VAL B C   
16387 O O   . VAL B 987  ? 0.2283 0.2064 0.2205 0.0146  -0.0087 -0.0293 985  VAL B O   
16388 C CB  . VAL B 987  ? 0.2187 0.1979 0.2045 0.0138  -0.0094 -0.0306 985  VAL B CB  
16389 C CG1 . VAL B 987  ? 0.2291 0.2106 0.2192 0.0124  -0.0100 -0.0291 985  VAL B CG1 
16390 C CG2 . VAL B 987  ? 0.2155 0.1921 0.1979 0.0129  -0.0110 -0.0316 985  VAL B CG2 
16391 N N   . THR B 988  ? 0.2041 0.1856 0.1938 0.0171  -0.0061 -0.0298 986  THR B N   
16392 C CA  . THR B 988  ? 0.2206 0.2044 0.2137 0.0176  -0.0052 -0.0286 986  THR B CA  
16393 C C   . THR B 988  ? 0.2376 0.2181 0.2309 0.0185  -0.0052 -0.0289 986  THR B C   
16394 O O   . THR B 988  ? 0.3182 0.2996 0.3143 0.0183  -0.0052 -0.0277 986  THR B O   
16395 C CB  . THR B 988  ? 0.2507 0.2387 0.2443 0.0188  -0.0034 -0.0281 986  THR B CB  
16396 O OG1 . THR B 988  ? 0.2740 0.2612 0.2650 0.0208  -0.0023 -0.0292 986  THR B OG1 
16397 C CG2 . THR B 988  ? 0.2714 0.2621 0.2649 0.0176  -0.0034 -0.0276 986  THR B CG2 
16398 N N   . SER B 989  ? 0.2533 0.2300 0.2434 0.0196  -0.0054 -0.0303 987  SER B N   
16399 C CA  . SER B 989  ? 0.2766 0.2494 0.2666 0.0204  -0.0057 -0.0306 987  SER B CA  
16400 C C   . SER B 989  ? 0.2840 0.2541 0.2753 0.0182  -0.0075 -0.0302 987  SER B C   
16401 O O   . SER B 989  ? 0.3728 0.3406 0.3651 0.0183  -0.0077 -0.0297 987  SER B O   
16402 C CB  . SER B 989  ? 0.3238 0.2929 0.3098 0.0223  -0.0053 -0.0324 987  SER B CB  
16403 O OG  . SER B 989  ? 0.4069 0.3723 0.3896 0.0212  -0.0067 -0.0338 987  SER B OG  
16404 N N   . ARG B 990  ? 0.2410 0.2113 0.2322 0.0162  -0.0088 -0.0302 988  ARG B N   
16405 C CA  . ARG B 990  ? 0.2452 0.2130 0.2375 0.0141  -0.0107 -0.0300 988  ARG B CA  
16406 C C   . ARG B 990  ? 0.2206 0.1920 0.2169 0.0123  -0.0111 -0.0284 988  ARG B C   
16407 O O   . ARG B 990  ? 0.2230 0.1933 0.2214 0.0108  -0.0122 -0.0277 988  ARG B O   
16408 C CB  . ARG B 990  ? 0.2738 0.2385 0.2627 0.0131  -0.0123 -0.0315 988  ARG B CB  
16409 C CG  . ARG B 990  ? 0.3966 0.3575 0.3809 0.0149  -0.0118 -0.0333 988  ARG B CG  
16410 C CD  . ARG B 990  ? 0.3538 0.3093 0.3368 0.0151  -0.0125 -0.0340 988  ARG B CD  
16411 N NE  . ARG B 990  ? 0.2717 0.2232 0.2530 0.0130  -0.0148 -0.0349 988  ARG B NE  
16412 C CZ  . ARG B 990  ? 0.3043 0.2504 0.2842 0.0126  -0.0158 -0.0355 988  ARG B CZ  
16413 N NH1 . ARG B 990  ? 0.3302 0.2743 0.3105 0.0141  -0.0148 -0.0352 988  ARG B NH1 
16414 N NH2 . ARG B 990  ? 0.3034 0.2461 0.2816 0.0105  -0.0181 -0.0363 988  ARG B NH2 
16415 N N   . ILE B 991  ? 0.2004 0.1760 0.1978 0.0125  -0.0103 -0.0277 989  ILE B N   
16416 C CA  . ILE B 991  ? 0.2149 0.1939 0.2161 0.0112  -0.0105 -0.0263 989  ILE B CA  
16417 C C   . ILE B 991  ? 0.2117 0.1917 0.2155 0.0116  -0.0095 -0.0251 989  ILE B C   
16418 O O   . ILE B 991  ? 0.2300 0.2098 0.2331 0.0132  -0.0083 -0.0252 989  ILE B O   
16419 C CB  . ILE B 991  ? 0.2178 0.2003 0.2189 0.0114  -0.0098 -0.0260 989  ILE B CB  
16420 C CG1 . ILE B 991  ? 0.2458 0.2310 0.2501 0.0101  -0.0104 -0.0248 989  ILE B CG1 
16421 C CG2 . ILE B 991  ? 0.2554 0.2402 0.2565 0.0131  -0.0080 -0.0258 989  ILE B CG2 
16422 C CD1 . ILE B 991  ? 0.2829 0.2668 0.2876 0.0084  -0.0123 -0.0249 989  ILE B CD1 
16423 N N   . LYS B 992  ? 0.1927 0.1741 0.1997 0.0102  -0.0100 -0.0240 990  LYS B N   
16424 C CA  . LYS B 992  ? 0.2014 0.1838 0.2108 0.0104  -0.0091 -0.0227 990  LYS B CA  
16425 C C   . LYS B 992  ? 0.2046 0.1912 0.2166 0.0099  -0.0085 -0.0217 990  LYS B C   
16426 O O   . LYS B 992  ? 0.2651 0.2528 0.2796 0.0086  -0.0090 -0.0209 990  LYS B O   
16427 C CB  . LYS B 992  ? 0.2271 0.2068 0.2375 0.0090  -0.0101 -0.0223 990  LYS B CB  
16428 C CG  . LYS B 992  ? 0.2523 0.2271 0.2597 0.0095  -0.0107 -0.0235 990  LYS B CG  
16429 C CD  . LYS B 992  ? 0.3555 0.3273 0.3640 0.0078  -0.0119 -0.0229 990  LYS B CD  
16430 C CE  . LYS B 992  ? 0.4666 0.4402 0.4781 0.0074  -0.0110 -0.0212 990  LYS B CE  
16431 N NZ  . LYS B 992  ? 0.5151 0.4871 0.5285 0.0052  -0.0122 -0.0203 990  LYS B NZ  
16432 N N   . ALA B 993  ? 0.2018 0.1908 0.2133 0.0110  -0.0074 -0.0217 991  ALA B N   
16433 C CA  . ALA B 993  ? 0.1855 0.1779 0.1989 0.0107  -0.0068 -0.0208 991  ALA B CA  
16434 C C   . ALA B 993  ? 0.1907 0.1850 0.2039 0.0119  -0.0054 -0.0205 991  ALA B C   
16435 O O   . ALA B 993  ? 0.2052 0.1989 0.2166 0.0131  -0.0049 -0.0211 991  ALA B O   
16436 C CB  . ALA B 993  ? 0.2134 0.2070 0.2262 0.0102  -0.0074 -0.0212 991  ALA B CB  
16437 N N   . GLY B 994  ? 0.1703 0.1670 0.1854 0.0116  -0.0047 -0.0196 992  GLY B N   
16438 C CA  . GLY B 994  ? 0.1651 0.1637 0.1801 0.0126  -0.0036 -0.0192 992  GLY B CA  
16439 C C   . GLY B 994  ? 0.1601 0.1606 0.1739 0.0130  -0.0031 -0.0196 992  GLY B C   
16440 O O   . GLY B 994  ? 0.1560 0.1579 0.1694 0.0139  -0.0023 -0.0194 992  GLY B O   
16441 N N   . ASN B 995  ? 0.1630 0.1638 0.1764 0.0123  -0.0037 -0.0199 993  ASN B N   
16442 C CA  . ASN B 995  ? 0.1542 0.1567 0.1665 0.0124  -0.0033 -0.0201 993  ASN B CA  
16443 C C   . ASN B 995  ? 0.1487 0.1499 0.1591 0.0122  -0.0040 -0.0209 993  ASN B C   
16444 O O   . ASN B 995  ? 0.1622 0.1625 0.1730 0.0114  -0.0050 -0.0210 993  ASN B O   
16445 C CB  . ASN B 995  ? 0.1601 0.1642 0.1735 0.0117  -0.0031 -0.0196 993  ASN B CB  
16446 C CG  . ASN B 995  ? 0.1591 0.1649 0.1733 0.0120  -0.0023 -0.0190 993  ASN B CG  
16447 O OD1 . ASN B 995  ? 0.1588 0.1644 0.1744 0.0120  -0.0021 -0.0185 993  ASN B OD1 
16448 N ND2 . ASN B 995  ? 0.1699 0.1775 0.1833 0.0122  -0.0017 -0.0189 993  ASN B ND2 
16449 N N   . LEU B 996  ? 0.1589 0.1603 0.1675 0.0130  -0.0035 -0.0215 994  LEU B N   
16450 C CA  . LEU B 996  ? 0.1557 0.1559 0.1620 0.0130  -0.0040 -0.0223 994  LEU B CA  
16451 C C   . LEU B 996  ? 0.1645 0.1668 0.1697 0.0127  -0.0034 -0.0221 994  LEU B C   
16452 O O   . LEU B 996  ? 0.1624 0.1672 0.1683 0.0130  -0.0024 -0.0216 994  LEU B O   
16453 C CB  . LEU B 996  ? 0.1708 0.1694 0.1753 0.0142  -0.0036 -0.0231 994  LEU B CB  
16454 C CG  . LEU B 996  ? 0.1866 0.1829 0.1920 0.0146  -0.0040 -0.0232 994  LEU B CG  
16455 C CD1 . LEU B 996  ? 0.2297 0.2239 0.2330 0.0160  -0.0036 -0.0241 994  LEU B CD1 
16456 C CD2 . LEU B 996  ? 0.2053 0.1996 0.2115 0.0132  -0.0054 -0.0231 994  LEU B CD2 
16457 N N   . TYR B 997  ? 0.1613 0.1628 0.1648 0.0121  -0.0041 -0.0224 995  TYR B N   
16458 C CA  . TYR B 997  ? 0.1646 0.1678 0.1669 0.0115  -0.0037 -0.0220 995  TYR B CA  
16459 C C   . TYR B 997  ? 0.1630 0.1650 0.1623 0.0116  -0.0039 -0.0227 995  TYR B C   
16460 O O   . TYR B 997  ? 0.1878 0.1876 0.1863 0.0113  -0.0051 -0.0232 995  TYR B O   
16461 C CB  . TYR B 997  ? 0.1688 0.1721 0.1722 0.0104  -0.0044 -0.0213 995  TYR B CB  
16462 C CG  . TYR B 997  ? 0.1663 0.1704 0.1724 0.0103  -0.0042 -0.0208 995  TYR B CG  
16463 C CD1 . TYR B 997  ? 0.1704 0.1733 0.1781 0.0104  -0.0048 -0.0208 995  TYR B CD1 
16464 C CD2 . TYR B 997  ? 0.1846 0.1907 0.1912 0.0101  -0.0034 -0.0202 995  TYR B CD2 
16465 C CE1 . TYR B 997  ? 0.1803 0.1840 0.1902 0.0104  -0.0045 -0.0202 995  TYR B CE1 
16466 C CE2 . TYR B 997  ? 0.1577 0.1643 0.1663 0.0101  -0.0032 -0.0198 995  TYR B CE2 
16467 C CZ  . TYR B 997  ? 0.1668 0.1722 0.1770 0.0103  -0.0037 -0.0198 995  TYR B CZ  
16468 O OH  . TYR B 997  ? 0.1949 0.2010 0.2068 0.0104  -0.0033 -0.0194 995  TYR B OH  
16469 N N   . ILE B 998  ? 0.1684 0.1722 0.1662 0.0121  -0.0028 -0.0228 996  ILE B N   
16470 C CA  . ILE B 998  ? 0.1700 0.1729 0.1646 0.0123  -0.0027 -0.0235 996  ILE B CA  
16471 C C   . ILE B 998  ? 0.1748 0.1793 0.1682 0.0112  -0.0025 -0.0228 996  ILE B C   
16472 O O   . ILE B 998  ? 0.1812 0.1885 0.1753 0.0111  -0.0014 -0.0222 996  ILE B O   
16473 C CB  . ILE B 998  ? 0.1977 0.2014 0.1913 0.0140  -0.0014 -0.0243 996  ILE B CB  
16474 C CG1 . ILE B 998  ? 0.2330 0.2347 0.2277 0.0150  -0.0016 -0.0249 996  ILE B CG1 
16475 C CG2 . ILE B 998  ? 0.2268 0.2294 0.2166 0.0143  -0.0012 -0.0252 996  ILE B CG2 
16476 C CD1 . ILE B 998  ? 0.3001 0.2981 0.2941 0.0145  -0.0032 -0.0255 996  ILE B CD1 
16477 N N   . ASN B 999  ? 0.1668 0.1694 0.1582 0.0104  -0.0036 -0.0228 997  ASN B N   
16478 C CA  . ASN B 999  ? 0.1870 0.1904 0.1765 0.0093  -0.0036 -0.0221 997  ASN B CA  
16479 C C   . ASN B 999  ? 0.1786 0.1833 0.1701 0.0082  -0.0036 -0.0209 997  ASN B C   
16480 O O   . ASN B 999  ? 0.1948 0.2012 0.1855 0.0074  -0.0029 -0.0202 997  ASN B O   
16481 C CB  . ASN B 999  ? 0.1828 0.1881 0.1700 0.0098  -0.0020 -0.0224 997  ASN B CB  
16482 C CG  . ASN B 999  ? 0.1870 0.1902 0.1711 0.0108  -0.0022 -0.0236 997  ASN B CG  
16483 O OD1 . ASN B 999  ? 0.2055 0.2059 0.1884 0.0103  -0.0037 -0.0240 997  ASN B OD1 
16484 N ND2 . ASN B 999  ? 0.1982 0.2028 0.1812 0.0121  -0.0006 -0.0243 997  ASN B ND2 
16485 N N   . ARG B 1000 ? 0.1788 0.1827 0.1729 0.0082  -0.0044 -0.0207 998  ARG B N   
16486 C CA  . ARG B 1000 ? 0.1624 0.1669 0.1582 0.0073  -0.0046 -0.0198 998  ARG B CA  
16487 C C   . ARG B 1000 ? 0.1856 0.1883 0.1833 0.0073  -0.0058 -0.0198 998  ARG B C   
16488 O O   . ARG B 1000 ? 0.2032 0.2045 0.2011 0.0078  -0.0066 -0.0204 998  ARG B O   
16489 C CB  . ARG B 1000 ? 0.1708 0.1778 0.1683 0.0075  -0.0033 -0.0196 998  ARG B CB  
16490 C CG  . ARG B 1000 ? 0.1823 0.1896 0.1815 0.0088  -0.0029 -0.0203 998  ARG B CG  
16491 C CD  . ARG B 1000 ? 0.1856 0.1948 0.1870 0.0089  -0.0022 -0.0199 998  ARG B CD  
16492 N NE  . ARG B 1000 ? 0.1724 0.1806 0.1752 0.0082  -0.0029 -0.0194 998  ARG B NE  
16493 C CZ  . ARG B 1000 ? 0.1676 0.1770 0.1718 0.0079  -0.0026 -0.0190 998  ARG B CZ  
16494 N NH1 . ARG B 1000 ? 0.1913 0.2031 0.1960 0.0082  -0.0017 -0.0189 998  ARG B NH1 
16495 N NH2 . ARG B 1000 ? 0.1853 0.1934 0.1903 0.0074  -0.0032 -0.0188 998  ARG B NH2 
16496 N N   . ASN B 1001 ? 0.1729 0.1757 0.1721 0.0068  -0.0060 -0.0191 999  ASN B N   
16497 C CA  . ASN B 1001 ? 0.1871 0.1888 0.1885 0.0071  -0.0069 -0.0191 999  ASN B CA  
16498 C C   . ASN B 1001 ? 0.1728 0.1753 0.1764 0.0079  -0.0063 -0.0195 999  ASN B C   
16499 O O   . ASN B 1001 ? 0.1776 0.1814 0.1812 0.0083  -0.0053 -0.0198 999  ASN B O   
16500 C CB  . ASN B 1001 ? 0.1907 0.1921 0.1928 0.0065  -0.0071 -0.0183 999  ASN B CB  
16501 C CG  . ASN B 1001 ? 0.2088 0.2117 0.2119 0.0064  -0.0060 -0.0182 999  ASN B CG  
16502 O OD1 . ASN B 1001 ? 0.1941 0.1980 0.1987 0.0070  -0.0053 -0.0186 999  ASN B OD1 
16503 N ND2 . ASN B 1001 ? 0.3175 0.3202 0.3194 0.0055  -0.0058 -0.0177 999  ASN B ND2 
16504 N N   . ILE B 1002 ? 0.1716 0.1733 0.1772 0.0081  -0.0070 -0.0195 1000 ILE B N   
16505 C CA  . ILE B 1002 ? 0.1655 0.1676 0.1731 0.0087  -0.0066 -0.0198 1000 ILE B CA  
16506 C C   . ILE B 1002 ? 0.1846 0.1876 0.1944 0.0088  -0.0061 -0.0193 1000 ILE B C   
16507 O O   . ILE B 1002 ? 0.1824 0.1856 0.1942 0.0091  -0.0060 -0.0193 1000 ILE B O   
16508 C CB  . ILE B 1002 ? 0.1718 0.1726 0.1800 0.0087  -0.0077 -0.0201 1000 ILE B CB  
16509 C CG1 . ILE B 1002 ? 0.1748 0.1752 0.1848 0.0084  -0.0088 -0.0196 1000 ILE B CG1 
16510 C CG2 . ILE B 1002 ? 0.1765 0.1762 0.1820 0.0087  -0.0082 -0.0207 1000 ILE B CG2 
16511 C CD1 . ILE B 1002 ? 0.1711 0.1708 0.1823 0.0083  -0.0099 -0.0198 1000 ILE B CD1 
16512 N N   . ILE B 1003 ? 0.1902 0.1936 0.1996 0.0084  -0.0057 -0.0190 1001 ILE B N   
16513 C CA  . ILE B 1003 ? 0.1853 0.1892 0.1963 0.0086  -0.0053 -0.0187 1001 ILE B CA  
16514 C C   . ILE B 1003 ? 0.2163 0.2215 0.2269 0.0085  -0.0042 -0.0187 1001 ILE B C   
16515 O O   . ILE B 1003 ? 0.2343 0.2397 0.2456 0.0085  -0.0038 -0.0186 1001 ILE B O   
16516 C CB  . ILE B 1003 ? 0.2158 0.2185 0.2268 0.0084  -0.0059 -0.0184 1001 ILE B CB  
16517 C CG1 . ILE B 1003 ? 0.2714 0.2735 0.2800 0.0076  -0.0061 -0.0182 1001 ILE B CG1 
16518 C CG2 . ILE B 1003 ? 0.2227 0.2246 0.2348 0.0086  -0.0071 -0.0183 1001 ILE B CG2 
16519 C CD1 . ILE B 1003 ? 0.3556 0.3563 0.3639 0.0074  -0.0064 -0.0179 1001 ILE B CD1 
16520 N N   . GLY B 1004 ? 0.1894 0.1957 0.1990 0.0085  -0.0037 -0.0189 1002 GLY B N   
16521 C CA  . GLY B 1004 ? 0.2172 0.2252 0.2266 0.0084  -0.0029 -0.0187 1002 GLY B CA  
16522 C C   . GLY B 1004 ? 0.2060 0.2147 0.2169 0.0091  -0.0024 -0.0187 1002 GLY B C   
16523 O O   . GLY B 1004 ? 0.2134 0.2219 0.2251 0.0097  -0.0023 -0.0188 1002 GLY B O   
16524 N N   . ALA B 1005 ? 0.1989 0.2083 0.2100 0.0088  -0.0020 -0.0185 1003 ALA B N   
16525 C CA  . ALA B 1005 ? 0.1983 0.2085 0.2104 0.0093  -0.0015 -0.0183 1003 ALA B CA  
16526 C C   . ALA B 1005 ? 0.2122 0.2241 0.2237 0.0088  -0.0011 -0.0181 1003 ALA B C   
16527 O O   . ALA B 1005 ? 0.1983 0.2105 0.2100 0.0089  -0.0008 -0.0180 1003 ALA B O   
16528 C CB  . ALA B 1005 ? 0.1868 0.1959 0.2001 0.0095  -0.0015 -0.0183 1003 ALA B CB  
16529 N N   . VAL B 1006 ? 0.1679 0.1811 0.1785 0.0084  -0.0011 -0.0181 1004 VAL B N   
16530 C CA  . VAL B 1006 ? 0.1749 0.1900 0.1850 0.0077  -0.0009 -0.0178 1004 VAL B CA  
16531 C C   . VAL B 1006 ? 0.1725 0.1891 0.1834 0.0085  -0.0005 -0.0176 1004 VAL B C   
16532 O O   . VAL B 1006 ? 0.1737 0.1911 0.1853 0.0095  -0.0003 -0.0175 1004 VAL B O   
16533 C CB  . VAL B 1006 ? 0.1843 0.2009 0.1935 0.0070  -0.0009 -0.0177 1004 VAL B CB  
16534 C CG1 . VAL B 1006 ? 0.1982 0.2173 0.2074 0.0061  -0.0008 -0.0173 1004 VAL B CG1 
16535 C CG2 . VAL B 1006 ? 0.2084 0.2232 0.2165 0.0060  -0.0013 -0.0178 1004 VAL B CG2 
16536 N N   . VAL B 1007 ? 0.1761 0.1929 0.1867 0.0081  -0.0005 -0.0175 1005 VAL B N   
16537 C CA  . VAL B 1007 ? 0.1724 0.1904 0.1836 0.0088  -0.0002 -0.0171 1005 VAL B CA  
16538 C C   . VAL B 1007 ? 0.1728 0.1936 0.1844 0.0092  -0.0002 -0.0167 1005 VAL B C   
16539 O O   . VAL B 1007 ? 0.1756 0.1983 0.1869 0.0083  -0.0003 -0.0166 1005 VAL B O   
16540 C CB  . VAL B 1007 ? 0.1762 0.1939 0.1864 0.0081  -0.0003 -0.0171 1005 VAL B CB  
16541 C CG1 . VAL B 1007 ? 0.1855 0.2045 0.1960 0.0088  -0.0001 -0.0166 1005 VAL B CG1 
16542 C CG2 . VAL B 1007 ? 0.1817 0.1968 0.1918 0.0081  -0.0002 -0.0176 1005 VAL B CG2 
16543 N N   . GLY B 1008 ? 0.1654 0.1866 0.1780 0.0105  0.0001  -0.0164 1006 GLY B N   
16544 C CA  . GLY B 1008 ? 0.1758 0.1996 0.1890 0.0114  0.0002  -0.0160 1006 GLY B CA  
16545 C C   . GLY B 1008 ? 0.1765 0.2012 0.1898 0.0116  0.0004  -0.0163 1006 GLY B C   
16546 O O   . GLY B 1008 ? 0.1985 0.2258 0.2124 0.0124  0.0007  -0.0159 1006 GLY B O   
16547 N N   . VAL B 1009 ? 0.1652 0.1879 0.1778 0.0111  0.0004  -0.0168 1007 VAL B N   
16548 C CA  . VAL B 1009 ? 0.1800 0.2031 0.1922 0.0112  0.0006  -0.0171 1007 VAL B CA  
16549 C C   . VAL B 1009 ? 0.1827 0.2028 0.1946 0.0120  0.0005  -0.0177 1007 VAL B C   
16550 O O   . VAL B 1009 ? 0.1878 0.2079 0.1996 0.0132  0.0008  -0.0179 1007 VAL B O   
16551 C CB  . VAL B 1009 ? 0.1845 0.2081 0.1958 0.0096  0.0004  -0.0171 1007 VAL B CB  
16552 C CG1 . VAL B 1009 ? 0.1836 0.2080 0.1943 0.0098  0.0008  -0.0173 1007 VAL B CG1 
16553 C CG2 . VAL B 1009 ? 0.1815 0.2081 0.1931 0.0085  0.0003  -0.0165 1007 VAL B CG2 
16554 N N   . GLN B 1010 ? 0.1725 0.1901 0.1843 0.0114  0.0001  -0.0178 1008 GLN B N   
16555 C CA  . GLN B 1010 ? 0.1723 0.1873 0.1843 0.0120  -0.0002 -0.0182 1008 GLN B CA  
16556 C C   . GLN B 1010 ? 0.1725 0.1867 0.1855 0.0121  -0.0002 -0.0178 1008 GLN B C   
16557 O O   . GLN B 1010 ? 0.1920 0.2050 0.2053 0.0114  -0.0005 -0.0179 1008 GLN B O   
16558 C CB  . GLN B 1010 ? 0.1771 0.1902 0.1884 0.0112  -0.0007 -0.0186 1008 GLN B CB  
16559 C CG  . GLN B 1010 ? 0.2038 0.2176 0.2138 0.0110  -0.0006 -0.0189 1008 GLN B CG  
16560 C CD  . GLN B 1010 ? 0.1917 0.2063 0.2009 0.0096  -0.0007 -0.0186 1008 GLN B CD  
16561 O OE1 . GLN B 1010 ? 0.1925 0.2060 0.2018 0.0089  -0.0011 -0.0184 1008 GLN B OE1 
16562 N NE2 . GLN B 1010 ? 0.1849 0.2016 0.1934 0.0094  -0.0003 -0.0184 1008 GLN B NE2 
16563 N N   . PRO B 1011 ? 0.1585 0.1734 0.1720 0.0129  0.0001  -0.0174 1009 PRO B N   
16564 C CA  . PRO B 1011 ? 0.1843 0.1982 0.1986 0.0131  0.0002  -0.0170 1009 PRO B CA  
16565 C C   . PRO B 1011 ? 0.1620 0.1735 0.1768 0.0128  -0.0002 -0.0173 1009 PRO B C   
16566 O O   . PRO B 1011 ? 0.1514 0.1617 0.1660 0.0132  -0.0005 -0.0177 1009 PRO B O   
16567 C CB  . PRO B 1011 ? 0.1781 0.1924 0.1926 0.0143  0.0004  -0.0166 1009 PRO B CB  
16568 C CG  . PRO B 1011 ? 0.1955 0.2123 0.2096 0.0147  0.0006  -0.0166 1009 PRO B CG  
16569 C CD  . PRO B 1011 ? 0.1960 0.2127 0.2095 0.0140  0.0004  -0.0173 1009 PRO B CD  
16570 N N   . PHE B 1012 ? 0.1571 0.1681 0.1726 0.0123  -0.0002 -0.0171 1010 PHE B N   
16571 C CA  . PHE B 1012 ? 0.1520 0.1615 0.1682 0.0118  -0.0006 -0.0174 1010 PHE B CA  
16572 C C   . PHE B 1012 ? 0.1629 0.1715 0.1805 0.0119  -0.0005 -0.0169 1010 PHE B C   
16573 O O   . PHE B 1012 ? 0.1698 0.1791 0.1878 0.0119  0.0001  -0.0163 1010 PHE B O   
16574 C CB  . PHE B 1012 ? 0.1660 0.1757 0.1821 0.0111  -0.0007 -0.0176 1010 PHE B CB  
16575 C CG  . PHE B 1012 ? 0.1499 0.1583 0.1668 0.0108  -0.0013 -0.0178 1010 PHE B CG  
16576 C CD1 . PHE B 1012 ? 0.1725 0.1801 0.1885 0.0107  -0.0020 -0.0182 1010 PHE B CD1 
16577 C CD2 . PHE B 1012 ? 0.1709 0.1791 0.1894 0.0108  -0.0012 -0.0174 1010 PHE B CD2 
16578 C CE1 . PHE B 1012 ? 0.1742 0.1808 0.1909 0.0104  -0.0028 -0.0183 1010 PHE B CE1 
16579 C CE2 . PHE B 1012 ? 0.1776 0.1850 0.1972 0.0105  -0.0019 -0.0175 1010 PHE B CE2 
16580 C CZ  . PHE B 1012 ? 0.1697 0.1762 0.1883 0.0103  -0.0028 -0.0180 1010 PHE B CZ  
16581 N N   . GLY B 1013 ? 0.1539 0.1609 0.1720 0.0118  -0.0010 -0.0170 1011 GLY B N   
16582 C CA  . GLY B 1013 ? 0.1652 0.1715 0.1849 0.0115  -0.0010 -0.0164 1011 GLY B CA  
16583 C C   . GLY B 1013 ? 0.1600 0.1643 0.1797 0.0114  -0.0018 -0.0167 1011 GLY B C   
16584 O O   . GLY B 1013 ? 0.1771 0.1804 0.1953 0.0121  -0.0020 -0.0172 1011 GLY B O   
16585 N N   . GLY B 1014 ? 0.1747 0.1782 0.1959 0.0107  -0.0022 -0.0164 1012 GLY B N   
16586 C CA  . GLY B 1014 ? 0.2010 0.2023 0.2221 0.0104  -0.0031 -0.0167 1012 GLY B CA  
16587 C C   . GLY B 1014 ? 0.1823 0.1823 0.2045 0.0099  -0.0031 -0.0159 1012 GLY B C   
16588 O O   . GLY B 1014 ? 0.2157 0.2165 0.2383 0.0101  -0.0022 -0.0150 1012 GLY B O   
16589 N N   . ARG B 1015 ? 0.1931 0.1909 0.2154 0.0092  -0.0041 -0.0162 1013 ARG B N   
16590 C CA  . ARG B 1015 ? 0.1978 0.1935 0.2206 0.0086  -0.0044 -0.0155 1013 ARG B CA  
16591 C C   . ARG B 1015 ? 0.1790 0.1747 0.2039 0.0070  -0.0054 -0.0152 1013 ARG B C   
16592 O O   . ARG B 1015 ? 0.1819 0.1792 0.2078 0.0066  -0.0058 -0.0156 1013 ARG B O   
16593 C CB  . ARG B 1015 ? 0.2113 0.2036 0.2317 0.0093  -0.0049 -0.0163 1013 ARG B CB  
16594 C CG  . ARG B 1015 ? 0.2155 0.2064 0.2345 0.0092  -0.0061 -0.0176 1013 ARG B CG  
16595 C CD  . ARG B 1015 ? 0.2695 0.2562 0.2866 0.0092  -0.0070 -0.0183 1013 ARG B CD  
16596 N NE  . ARG B 1015 ? 0.2855 0.2707 0.3043 0.0073  -0.0080 -0.0178 1013 ARG B NE  
16597 C CZ  . ARG B 1015 ? 0.2893 0.2749 0.3090 0.0060  -0.0092 -0.0181 1013 ARG B CZ  
16598 N NH1 . ARG B 1015 ? 0.2750 0.2619 0.2939 0.0063  -0.0096 -0.0189 1013 ARG B NH1 
16599 N NH2 . ARG B 1015 ? 0.3132 0.2980 0.3348 0.0042  -0.0101 -0.0174 1013 ARG B NH2 
16600 N N   . GLY B 1016 ? 0.1951 0.1889 0.2207 0.0060  -0.0058 -0.0145 1014 GLY B N   
16601 C CA  . GLY B 1016 ? 0.1954 0.1896 0.2235 0.0043  -0.0067 -0.0141 1014 GLY B CA  
16602 C C   . GLY B 1016 ? 0.1832 0.1814 0.2142 0.0039  -0.0059 -0.0132 1014 GLY B C   
16603 O O   . GLY B 1016 ? 0.2054 0.2053 0.2368 0.0045  -0.0045 -0.0124 1014 GLY B O   
16604 N N   . LEU B 1017 ? 0.1852 0.1849 0.2179 0.0032  -0.0068 -0.0134 1015 LEU B N   
16605 C CA  . LEU B 1017 ? 0.1905 0.1941 0.2261 0.0031  -0.0061 -0.0126 1015 LEU B CA  
16606 C C   . LEU B 1017 ? 0.1853 0.1905 0.2198 0.0047  -0.0050 -0.0131 1015 LEU B C   
16607 O O   . LEU B 1017 ? 0.1802 0.1883 0.2167 0.0050  -0.0042 -0.0127 1015 LEU B O   
16608 C CB  . LEU B 1017 ? 0.1769 0.1818 0.2148 0.0021  -0.0076 -0.0127 1015 LEU B CB  
16609 C CG  . LEU B 1017 ? 0.2055 0.2093 0.2450 0.0001  -0.0089 -0.0121 1015 LEU B CG  
16610 C CD1 . LEU B 1017 ? 0.2286 0.2340 0.2702 -0.0007 -0.0105 -0.0123 1015 LEU B CD1 
16611 C CD2 . LEU B 1017 ? 0.2351 0.2408 0.2773 -0.0007 -0.0077 -0.0106 1015 LEU B CD2 
16612 N N   . SER B 1018 ? 0.1615 0.1650 0.1930 0.0057  -0.0050 -0.0141 1016 SER B N   
16613 C CA  . SER B 1018 ? 0.1665 0.1712 0.1967 0.0069  -0.0041 -0.0145 1016 SER B CA  
16614 C C   . SER B 1018 ? 0.1542 0.1595 0.1835 0.0077  -0.0026 -0.0141 1016 SER B C   
16615 O O   . SER B 1018 ? 0.1752 0.1818 0.2037 0.0085  -0.0019 -0.0144 1016 SER B O   
16616 C CB  . SER B 1018 ? 0.1659 0.1690 0.1935 0.0075  -0.0049 -0.0157 1016 SER B CB  
16617 O OG  . SER B 1018 ? 0.1725 0.1752 0.2006 0.0069  -0.0063 -0.0161 1016 SER B OG  
16618 N N   . GLY B 1019 ? 0.1694 0.1737 0.1985 0.0075  -0.0023 -0.0134 1017 GLY B N   
16619 C CA  . GLY B 1019 ? 0.1776 0.1826 0.2057 0.0083  -0.0010 -0.0129 1017 GLY B CA  
16620 C C   . GLY B 1019 ? 0.1949 0.1982 0.2225 0.0080  -0.0007 -0.0120 1017 GLY B C   
16621 O O   . GLY B 1019 ? 0.2014 0.2022 0.2286 0.0076  -0.0016 -0.0121 1017 GLY B O   
16622 N N   . THR B 1020 ? 0.1833 0.1878 0.2106 0.0084  0.0004  -0.0111 1018 THR B N   
16623 C CA  . THR B 1020 ? 0.1859 0.1889 0.2121 0.0086  0.0007  -0.0102 1018 THR B CA  
16624 C C   . THR B 1020 ? 0.1801 0.1824 0.2039 0.0100  0.0007  -0.0108 1018 THR B C   
16625 O O   . THR B 1020 ? 0.2012 0.2015 0.2239 0.0104  0.0005  -0.0103 1018 THR B O   
16626 C CB  . THR B 1020 ? 0.1798 0.1846 0.2065 0.0084  0.0020  -0.0089 1018 THR B CB  
16627 O OG1 . THR B 1020 ? 0.1705 0.1776 0.1965 0.0091  0.0028  -0.0094 1018 THR B OG1 
16628 C CG2 . THR B 1020 ? 0.1888 0.1948 0.2182 0.0070  0.0023  -0.0081 1018 THR B CG2 
16629 N N   . GLY B 1021 ? 0.1808 0.1847 0.2039 0.0106  0.0008  -0.0117 1019 GLY B N   
16630 C CA  . GLY B 1021 ? 0.1794 0.1837 0.2006 0.0118  0.0010  -0.0119 1019 GLY B CA  
16631 C C   . GLY B 1021 ? 0.1763 0.1819 0.1970 0.0119  0.0019  -0.0108 1019 GLY B C   
16632 O O   . GLY B 1021 ? 0.1768 0.1828 0.1985 0.0112  0.0025  -0.0099 1019 GLY B O   
16633 N N   . PRO B 1022 ? 0.1712 0.1776 0.1904 0.0129  0.0020  -0.0108 1020 PRO B N   
16634 C CA  . PRO B 1022 ? 0.1848 0.1915 0.2031 0.0137  0.0015  -0.0117 1020 PRO B CA  
16635 C C   . PRO B 1022 ? 0.1914 0.1996 0.2097 0.0133  0.0015  -0.0128 1020 PRO B C   
16636 O O   . PRO B 1022 ? 0.2018 0.2108 0.2207 0.0126  0.0019  -0.0128 1020 PRO B O   
16637 C CB  . PRO B 1022 ? 0.2035 0.2114 0.2206 0.0146  0.0017  -0.0110 1020 PRO B CB  
16638 C CG  . PRO B 1022 ? 0.1945 0.2036 0.2115 0.0139  0.0024  -0.0103 1020 PRO B CG  
16639 C CD  . PRO B 1022 ? 0.1854 0.1930 0.2037 0.0131  0.0027  -0.0098 1020 PRO B CD  
16640 N N   . LYS B 1023 ? 0.1680 0.1764 0.1857 0.0137  0.0010  -0.0136 1021 LYS B N   
16641 C CA  . LYS B 1023 ? 0.1751 0.1845 0.1927 0.0133  0.0009  -0.0145 1021 LYS B CA  
16642 C C   . LYS B 1023 ? 0.1589 0.1703 0.1758 0.0131  0.0013  -0.0145 1021 LYS B C   
16643 O O   . LYS B 1023 ? 0.1695 0.1821 0.1855 0.0135  0.0014  -0.0141 1021 LYS B O   
16644 C CB  . LYS B 1023 ? 0.1568 0.1662 0.1736 0.0138  0.0005  -0.0153 1021 LYS B CB  
16645 C CG  . LYS B 1023 ? 0.1643 0.1716 0.1813 0.0139  -0.0001 -0.0158 1021 LYS B CG  
16646 C CD  . LYS B 1023 ? 0.1528 0.1605 0.1687 0.0146  -0.0002 -0.0165 1021 LYS B CD  
16647 C CE  . LYS B 1023 ? 0.1888 0.1943 0.2042 0.0147  -0.0007 -0.0173 1021 LYS B CE  
16648 N NZ  . LYS B 1023 ? 0.1726 0.1782 0.1881 0.0137  -0.0012 -0.0178 1021 LYS B NZ  
16649 N N   . ALA B 1024 ? 0.1705 0.1821 0.1876 0.0124  0.0015  -0.0148 1022 ALA B N   
16650 C CA  . ALA B 1024 ? 0.1585 0.1713 0.1744 0.0121  0.0016  -0.0151 1022 ALA B CA  
16651 C C   . ALA B 1024 ? 0.1778 0.1915 0.1930 0.0121  0.0012  -0.0156 1022 ALA B C   
16652 O O   . ALA B 1024 ? 0.1827 0.1958 0.1980 0.0122  0.0008  -0.0160 1022 ALA B O   
16653 C CB  . ALA B 1024 ? 0.1830 0.1953 0.1993 0.0116  0.0018  -0.0156 1022 ALA B CB  
16654 N N   . GLY B 1025 ? 0.1547 0.1698 0.1687 0.0118  0.0012  -0.0155 1023 GLY B N   
16655 C CA  . GLY B 1025 ? 0.1723 0.1887 0.1857 0.0116  0.0008  -0.0158 1023 GLY B CA  
16656 C C   . GLY B 1025 ? 0.1695 0.1869 0.1834 0.0125  0.0007  -0.0155 1023 GLY B C   
16657 O O   . GLY B 1025 ? 0.1727 0.1912 0.1864 0.0125  0.0005  -0.0158 1023 GLY B O   
16658 N N   . GLY B 1026 ? 0.1684 0.1853 0.1828 0.0134  0.0009  -0.0149 1024 GLY B N   
16659 C CA  . GLY B 1026 ? 0.1690 0.1864 0.1837 0.0145  0.0008  -0.0146 1024 GLY B CA  
16660 C C   . GLY B 1026 ? 0.1667 0.1851 0.1812 0.0152  0.0008  -0.0136 1024 GLY B C   
16661 O O   . GLY B 1026 ? 0.1601 0.1785 0.1741 0.0146  0.0010  -0.0132 1024 GLY B O   
16662 N N   . PRO B 1027 ? 0.1658 0.1848 0.1806 0.0164  0.0007  -0.0132 1025 PRO B N   
16663 C CA  . PRO B 1027 ? 0.1418 0.1624 0.1564 0.0172  0.0006  -0.0121 1025 PRO B CA  
16664 C C   . PRO B 1027 ? 0.1538 0.1722 0.1682 0.0176  0.0007  -0.0112 1025 PRO B C   
16665 O O   . PRO B 1027 ? 0.1657 0.1852 0.1797 0.0181  0.0005  -0.0102 1025 PRO B O   
16666 C CB  . PRO B 1027 ? 0.1707 0.1929 0.1859 0.0186  0.0005  -0.0121 1025 PRO B CB  
16667 C CG  . PRO B 1027 ? 0.1949 0.2149 0.2104 0.0190  0.0007  -0.0130 1025 PRO B CG  
16668 C CD  . PRO B 1027 ? 0.1813 0.2001 0.1964 0.0174  0.0007  -0.0137 1025 PRO B CD  
16669 N N   . LEU B 1028 ? 0.1574 0.1730 0.1722 0.0174  0.0009  -0.0115 1026 LEU B N   
16670 C CA  . LEU B 1028 ? 0.1672 0.1807 0.1818 0.0175  0.0011  -0.0104 1026 LEU B CA  
16671 C C   . LEU B 1028 ? 0.1735 0.1871 0.1878 0.0163  0.0015  -0.0102 1026 LEU B C   
16672 O O   . LEU B 1028 ? 0.1868 0.1993 0.2009 0.0162  0.0018  -0.0092 1026 LEU B O   
16673 C CB  . LEU B 1028 ? 0.1724 0.1828 0.1876 0.0178  0.0010  -0.0107 1026 LEU B CB  
16674 C CG  . LEU B 1028 ? 0.2147 0.2243 0.2299 0.0192  0.0007  -0.0111 1026 LEU B CG  
16675 C CD1 . LEU B 1028 ? 0.2310 0.2368 0.2463 0.0193  0.0006  -0.0113 1026 LEU B CD1 
16676 C CD2 . LEU B 1028 ? 0.2622 0.2727 0.2770 0.0207  0.0006  -0.0101 1026 LEU B CD2 
16677 N N   . TYR B 1029 ? 0.1585 0.1733 0.1727 0.0153  0.0017  -0.0110 1027 TYR B N   
16678 C CA  . TYR B 1029 ? 0.1663 0.1807 0.1803 0.0143  0.0022  -0.0111 1027 TYR B CA  
16679 C C   . TYR B 1029 ? 0.1542 0.1695 0.1669 0.0143  0.0025  -0.0102 1027 TYR B C   
16680 O O   . TYR B 1029 ? 0.1662 0.1806 0.1789 0.0140  0.0032  -0.0095 1027 TYR B O   
16681 C CB  . TYR B 1029 ? 0.1711 0.1863 0.1849 0.0136  0.0022  -0.0122 1027 TYR B CB  
16682 C CG  . TYR B 1029 ? 0.1610 0.1756 0.1751 0.0129  0.0027  -0.0127 1027 TYR B CG  
16683 C CD1 . TYR B 1029 ? 0.1714 0.1846 0.1870 0.0127  0.0028  -0.0128 1027 TYR B CD1 
16684 C CD2 . TYR B 1029 ? 0.1647 0.1800 0.1775 0.0124  0.0030  -0.0131 1027 TYR B CD2 
16685 C CE1 . TYR B 1029 ? 0.1718 0.1848 0.1880 0.0122  0.0033  -0.0131 1027 TYR B CE1 
16686 C CE2 . TYR B 1029 ? 0.1555 0.1702 0.1686 0.0120  0.0035  -0.0135 1027 TYR B CE2 
16687 C CZ  . TYR B 1029 ? 0.1649 0.1787 0.1799 0.0120  0.0037  -0.0135 1027 TYR B CZ  
16688 O OH  . TYR B 1029 ? 0.1793 0.1929 0.1948 0.0118  0.0043  -0.0140 1027 TYR B OH  
16689 N N   . LEU B 1030 ? 0.1518 0.1690 0.1633 0.0144  0.0021  -0.0101 1028 LEU B N   
16690 C CA  . LEU B 1030 ? 0.1596 0.1777 0.1695 0.0142  0.0023  -0.0093 1028 LEU B CA  
16691 C C   . LEU B 1030 ? 0.1726 0.1897 0.1823 0.0149  0.0025  -0.0078 1028 LEU B C   
16692 O O   . LEU B 1030 ? 0.1706 0.1875 0.1791 0.0145  0.0030  -0.0071 1028 LEU B O   
16693 C CB  . LEU B 1030 ? 0.1688 0.1892 0.1775 0.0142  0.0015  -0.0094 1028 LEU B CB  
16694 C CG  . LEU B 1030 ? 0.1814 0.2026 0.1897 0.0132  0.0013  -0.0107 1028 LEU B CG  
16695 C CD1 . LEU B 1030 ? 0.2144 0.2380 0.2216 0.0128  0.0004  -0.0107 1028 LEU B CD1 
16696 C CD2 . LEU B 1030 ? 0.2215 0.2413 0.2287 0.0124  0.0021  -0.0114 1028 LEU B CD2 
16697 N N   . GLY B 1031 ? 0.1771 0.1932 0.1878 0.0158  0.0020  -0.0074 1029 GLY B N   
16698 C CA  . GLY B 1031 ? 0.1916 0.2064 0.2021 0.0165  0.0020  -0.0059 1029 GLY B CA  
16699 C C   . GLY B 1031 ? 0.1753 0.1880 0.1861 0.0157  0.0028  -0.0053 1029 GLY B C   
16700 O O   . GLY B 1031 ? 0.1995 0.2111 0.2096 0.0159  0.0030  -0.0038 1029 GLY B O   
16701 N N   . ARG B 1032 ? 0.1689 0.1812 0.1808 0.0149  0.0033  -0.0063 1030 ARG B N   
16702 C CA  . ARG B 1032 ? 0.1660 0.1771 0.1786 0.0141  0.0041  -0.0057 1030 ARG B CA  
16703 C C   . ARG B 1032 ? 0.1741 0.1865 0.1854 0.0135  0.0051  -0.0052 1030 ARG B C   
16704 O O   . ARG B 1032 ? 0.1990 0.2109 0.2107 0.0128  0.0060  -0.0044 1030 ARG B O   
16705 C CB  . ARG B 1032 ? 0.1793 0.1898 0.1938 0.0135  0.0042  -0.0069 1030 ARG B CB  
16706 C CG  . ARG B 1032 ? 0.1947 0.2041 0.2107 0.0126  0.0048  -0.0062 1030 ARG B CG  
16707 C CD  . ARG B 1032 ? 0.1997 0.2067 0.2161 0.0127  0.0043  -0.0052 1030 ARG B CD  
16708 N NE  . ARG B 1032 ? 0.2174 0.2235 0.2356 0.0115  0.0047  -0.0047 1030 ARG B NE  
16709 C CZ  . ARG B 1032 ? 0.2532 0.2581 0.2716 0.0108  0.0051  -0.0032 1030 ARG B CZ  
16710 N NH1 . ARG B 1032 ? 0.2550 0.2593 0.2716 0.0113  0.0052  -0.0018 1030 ARG B NH1 
16711 N NH2 . ARG B 1032 ? 0.2543 0.2587 0.2747 0.0096  0.0053  -0.0028 1030 ARG B NH2 
16712 N N   . LEU B 1033 ? 0.1642 0.1784 0.1739 0.0136  0.0049  -0.0058 1031 LEU B N   
16713 C CA  . LEU B 1033 ? 0.1736 0.1888 0.1815 0.0131  0.0058  -0.0059 1031 LEU B CA  
16714 C C   . LEU B 1033 ? 0.1761 0.1919 0.1815 0.0133  0.0057  -0.0047 1031 LEU B C   
16715 O O   . LEU B 1033 ? 0.1848 0.2015 0.1881 0.0130  0.0062  -0.0049 1031 LEU B O   
16716 C CB  . LEU B 1033 ? 0.1871 0.2032 0.1945 0.0128  0.0057  -0.0076 1031 LEU B CB  
16717 C CG  . LEU B 1033 ? 0.1749 0.1904 0.1846 0.0127  0.0056  -0.0087 1031 LEU B CG  
16718 C CD1 . LEU B 1033 ? 0.1818 0.1980 0.1908 0.0124  0.0053  -0.0102 1031 LEU B CD1 
16719 C CD2 . LEU B 1033 ? 0.1986 0.2135 0.2100 0.0123  0.0066  -0.0084 1031 LEU B CD2 
16720 N N   . VAL B 1034 ? 0.1825 0.1976 0.1879 0.0140  0.0050  -0.0034 1032 VAL B N   
16721 C CA  . VAL B 1034 ? 0.1993 0.2148 0.2025 0.0143  0.0047  -0.0019 1032 VAL B CA  
16722 C C   . VAL B 1034 ? 0.2129 0.2264 0.2168 0.0145  0.0049  -0.0002 1032 VAL B C   
16723 O O   . VAL B 1034 ? 0.2273 0.2391 0.2334 0.0145  0.0048  -0.0004 1032 VAL B O   
16724 C CB  . VAL B 1034 ? 0.1994 0.2164 0.2020 0.0151  0.0033  -0.0020 1032 VAL B CB  
16725 C CG1 . VAL B 1034 ? 0.2284 0.2473 0.2298 0.0145  0.0031  -0.0035 1032 VAL B CG1 
16726 C CG2 . VAL B 1034 ? 0.1999 0.2163 0.2048 0.0160  0.0026  -0.0024 1032 VAL B CG2 
16727 N N   . THR B 1035 ? 0.2383 0.2516 0.2401 0.0146  0.0050  0.0015  1033 THR B N   
16728 C CA  . THR B 1035 ? 0.2591 0.2700 0.2613 0.0146  0.0052  0.0033  1033 THR B CA  
16729 C C   . THR B 1035 ? 0.2723 0.2817 0.2752 0.0159  0.0039  0.0040  1033 THR B C   
16730 O O   . THR B 1035 ? 0.3352 0.3419 0.3389 0.0159  0.0039  0.0051  1033 THR B O   
16731 C CB  . THR B 1035 ? 0.3288 0.3398 0.3284 0.0141  0.0059  0.0051  1033 THR B CB  
16732 O OG1 . THR B 1035 ? 0.3653 0.3780 0.3624 0.0147  0.0051  0.0053  1033 THR B OG1 
16733 C CG2 . THR B 1035 ? 0.3564 0.3685 0.3560 0.0129  0.0076  0.0046  1033 THR B CG2 
16734 N N   . THR B 1036 ? 0.2346 0.2456 0.2372 0.0170  0.0028  0.0034  1034 THR B N   
16735 C CA  . THR B 1036 ? 0.2549 0.2650 0.2585 0.0185  0.0016  0.0037  1034 THR B CA  
16736 C C   . THR B 1036 ? 0.2541 0.2661 0.2593 0.0189  0.0012  0.0018  1034 THR B C   
16737 O O   . THR B 1036 ? 0.2389 0.2536 0.2433 0.0187  0.0009  0.0010  1034 THR B O   
16738 C CB  . THR B 1036 ? 0.3230 0.3340 0.3247 0.0196  0.0007  0.0054  1034 THR B CB  
16739 O OG1 . THR B 1036 ? 0.3951 0.4046 0.3948 0.0190  0.0012  0.0073  1034 THR B OG1 
16740 C CG2 . THR B 1036 ? 0.3869 0.3967 0.3897 0.0216  -0.0004 0.0059  1034 THR B CG2 
16741 N N   . ALA B 1037 ? 0.2480 0.2583 0.2550 0.0194  0.0011  0.0009  1035 ALA B N   
16742 C CA  . ALA B 1037 ? 0.2352 0.2472 0.2436 0.0196  0.0008  -0.0009 1035 ALA B CA  
16743 C C   . ALA B 1037 ? 0.2201 0.2342 0.2286 0.0212  -0.0001 -0.0007 1035 ALA B C   
16744 O O   . ALA B 1037 ? 0.2455 0.2584 0.2539 0.0227  -0.0007 0.0004  1035 ALA B O   
16745 C CB  . ALA B 1037 ? 0.2696 0.2790 0.2796 0.0196  0.0010  -0.0019 1035 ALA B CB  
16746 N N   . PRO B 1038 ? 0.1950 0.2123 0.2037 0.0209  -0.0004 -0.0018 1036 PRO B N   
16747 C CA  . PRO B 1038 ? 0.2003 0.2202 0.2097 0.0223  -0.0013 -0.0017 1036 PRO B CA  
16748 C C   . PRO B 1038 ? 0.1969 0.2159 0.2080 0.0235  -0.0012 -0.0027 1036 PRO B C   
16749 O O   . PRO B 1038 ? 0.2047 0.2212 0.2164 0.0230  -0.0007 -0.0035 1036 PRO B O   
16750 C CB  . PRO B 1038 ? 0.2219 0.2452 0.2310 0.0210  -0.0015 -0.0027 1036 PRO B CB  
16751 C CG  . PRO B 1038 ? 0.2428 0.2646 0.2519 0.0195  -0.0006 -0.0040 1036 PRO B CG  
16752 C CD  . PRO B 1038 ? 0.2068 0.2253 0.2152 0.0192  0.0001  -0.0032 1036 PRO B CD  
16753 N N   . VAL B 1039 ? 0.1941 0.2155 0.2062 0.0251  -0.0018 -0.0024 1037 VAL B N   
16754 C CA  . VAL B 1039 ? 0.2011 0.2225 0.2147 0.0263  -0.0017 -0.0035 1037 VAL B CA  
16755 C C   . VAL B 1039 ? 0.1902 0.2146 0.2045 0.0251  -0.0015 -0.0049 1037 VAL B C   
16756 O O   . VAL B 1039 ? 0.2016 0.2299 0.2161 0.0248  -0.0020 -0.0047 1037 VAL B O   
16757 C CB  . VAL B 1039 ? 0.2040 0.2269 0.2184 0.0288  -0.0023 -0.0025 1037 VAL B CB  
16758 C CG1 . VAL B 1039 ? 0.2500 0.2729 0.2657 0.0303  -0.0019 -0.0037 1037 VAL B CG1 
16759 C CG2 . VAL B 1039 ? 0.2538 0.2732 0.2671 0.0300  -0.0025 -0.0009 1037 VAL B CG2 
16760 N N   . PRO B 1040 ? 0.1942 0.2169 0.2088 0.0242  -0.0009 -0.0063 1038 PRO B N   
16761 C CA  . PRO B 1040 ? 0.1959 0.2211 0.2110 0.0229  -0.0008 -0.0074 1038 PRO B CA  
16762 C C   . PRO B 1040 ? 0.1925 0.2211 0.2088 0.0241  -0.0010 -0.0077 1038 PRO B C   
16763 O O   . PRO B 1040 ? 0.1919 0.2202 0.2089 0.0262  -0.0009 -0.0073 1038 PRO B O   
16764 C CB  . PRO B 1040 ? 0.2252 0.2473 0.2402 0.0221  -0.0002 -0.0086 1038 PRO B CB  
16765 C CG  . PRO B 1040 ? 0.2522 0.2705 0.2666 0.0222  0.0000  -0.0080 1038 PRO B CG  
16766 C CD  . PRO B 1040 ? 0.2172 0.2355 0.2316 0.0241  -0.0004 -0.0066 1038 PRO B CD  
16767 N N   . PRO B 1041 ? 0.2048 0.2368 0.2215 0.0228  -0.0011 -0.0082 1039 PRO B N   
16768 C CA  . PRO B 1041 ? 0.2061 0.2416 0.2243 0.0236  -0.0010 -0.0085 1039 PRO B CA  
16769 C C   . PRO B 1041 ? 0.1794 0.2129 0.1980 0.0250  -0.0003 -0.0094 1039 PRO B C   
16770 O O   . PRO B 1041 ? 0.2083 0.2383 0.2261 0.0242  0.0001  -0.0102 1039 PRO B O   
16771 C CB  . PRO B 1041 ? 0.2156 0.2534 0.2336 0.0213  -0.0012 -0.0091 1039 PRO B CB  
16772 C CG  . PRO B 1041 ? 0.2588 0.2950 0.2752 0.0197  -0.0015 -0.0090 1039 PRO B CG  
16773 C CD  . PRO B 1041 ? 0.2299 0.2619 0.2456 0.0205  -0.0012 -0.0087 1039 PRO B CD  
16774 N N   . GLN B 1042 ? 0.1876 0.2232 0.2074 0.0271  -0.0001 -0.0091 1040 GLN B N   
16775 C CA  . GLN B 1042 ? 0.1996 0.2338 0.2196 0.0286  0.0006  -0.0100 1040 GLN B CA  
16776 C C   . GLN B 1042 ? 0.1986 0.2271 0.2173 0.0295  0.0008  -0.0103 1040 GLN B C   
16777 O O   . GLN B 1042 ? 0.2074 0.2337 0.2258 0.0304  0.0013  -0.0114 1040 GLN B O   
16778 C CB  . GLN B 1042 ? 0.2287 0.2637 0.2485 0.0271  0.0012  -0.0113 1040 GLN B CB  
16779 C CG  . GLN B 1042 ? 0.2744 0.3148 0.2954 0.0259  0.0010  -0.0110 1040 GLN B CG  
16780 C CD  . GLN B 1042 ? 0.3556 0.3964 0.3763 0.0244  0.0016  -0.0120 1040 GLN B CD  
16781 O OE1 . GLN B 1042 ? 0.5485 0.5869 0.5680 0.0225  0.0014  -0.0126 1040 GLN B OE1 
16782 N NE2 . GLN B 1042 ? 0.4914 0.5352 0.5130 0.0256  0.0023  -0.0123 1040 GLN B NE2 
16783 N N   . HIS B 1043 ? 0.1851 0.2111 0.2032 0.0292  0.0003  -0.0095 1041 HIS B N   
16784 C CA  . HIS B 1043 ? 0.1835 0.2040 0.2005 0.0295  0.0004  -0.0097 1041 HIS B CA  
16785 C C   . HIS B 1043 ? 0.2043 0.2230 0.2212 0.0322  0.0002  -0.0090 1041 HIS B C   
16786 O O   . HIS B 1043 ? 0.2285 0.2466 0.2452 0.0328  -0.0003 -0.0076 1041 HIS B O   
16787 C CB  . HIS B 1043 ? 0.1878 0.2066 0.2040 0.0276  0.0000  -0.0089 1041 HIS B CB  
16788 C CG  . HIS B 1043 ? 0.1940 0.2077 0.2093 0.0274  0.0001  -0.0089 1041 HIS B CG  
16789 N ND1 . HIS B 1043 ? 0.2009 0.2121 0.2159 0.0260  0.0003  -0.0100 1041 HIS B ND1 
16790 C CD2 . HIS B 1043 ? 0.2270 0.2375 0.2417 0.0283  -0.0002 -0.0078 1041 HIS B CD2 
16791 C CE1 . HIS B 1043 ? 0.1922 0.1993 0.2067 0.0259  0.0001  -0.0097 1041 HIS B CE1 
16792 N NE2 . HIS B 1043 ? 0.1958 0.2023 0.2100 0.0272  -0.0001 -0.0083 1041 HIS B NE2 
16793 N N   . SER B 1044 ? 0.1704 0.1880 0.1873 0.0339  0.0007  -0.0100 1042 SER B N   
16794 C CA  . SER B 1044 ? 0.1764 0.1913 0.1929 0.0367  0.0007  -0.0096 1042 SER B CA  
16795 C C   . SER B 1044 ? 0.1872 0.1995 0.2028 0.0377  0.0013  -0.0113 1042 SER B C   
16796 O O   . SER B 1044 ? 0.2010 0.2146 0.2165 0.0365  0.0018  -0.0125 1042 SER B O   
16797 C CB  . SER B 1044 ? 0.1879 0.2072 0.2059 0.0389  0.0006  -0.0086 1042 SER B CB  
16798 O OG  . SER B 1044 ? 0.2020 0.2258 0.2212 0.0394  0.0012  -0.0094 1042 SER B OG  
16799 N N   . SER B 1045 ? 0.1781 0.1866 0.1929 0.0401  0.0013  -0.0114 1043 SER B N   
16800 C CA  . SER B 1045 ? 0.1710 0.1768 0.1846 0.0416  0.0019  -0.0131 1043 SER B CA  
16801 C C   . SER B 1045 ? 0.1950 0.1992 0.2084 0.0452  0.0021  -0.0128 1043 SER B C   
16802 O O   . SER B 1045 ? 0.2046 0.2064 0.2178 0.0460  0.0014  -0.0114 1043 SER B O   
16803 C CB  . SER B 1045 ? 0.1931 0.1928 0.2048 0.0398  0.0015  -0.0139 1043 SER B CB  
16804 O OG  . SER B 1045 ? 0.2054 0.2019 0.2154 0.0412  0.0020  -0.0156 1043 SER B OG  
16805 N N   . VAL B 1046 ? 0.1897 0.1951 0.2028 0.0473  0.0030  -0.0140 1044 VAL B N   
16806 C CA  . VAL B 1046 ? 0.2128 0.2162 0.2256 0.0511  0.0033  -0.0140 1044 VAL B CA  
16807 C C   . VAL B 1046 ? 0.2253 0.2205 0.2351 0.0518  0.0031  -0.0152 1044 VAL B C   
16808 O O   . VAL B 1046 ? 0.2273 0.2192 0.2363 0.0549  0.0031  -0.0152 1044 VAL B O   
16809 C CB  . VAL B 1046 ? 0.2488 0.2572 0.2627 0.0536  0.0046  -0.0148 1044 VAL B CB  
16810 C CG1 . VAL B 1046 ? 0.2722 0.2886 0.2891 0.0528  0.0046  -0.0135 1044 VAL B CG1 
16811 C CG2 . VAL B 1046 ? 0.2339 0.2411 0.2461 0.0528  0.0054  -0.0169 1044 VAL B CG2 
16812 N N   . HIS B 1047 ? 0.2116 0.2032 0.2199 0.0489  0.0027  -0.0161 1045 HIS B N   
16813 C CA  A HIS B 1047 ? 0.2274 0.2114 0.2329 0.0492  0.0023  -0.0173 1045 HIS B CA  
16814 C CA  B HIS B 1047 ? 0.2273 0.2113 0.2328 0.0489  0.0023  -0.0174 1045 HIS B CA  
16815 C C   . HIS B 1047 ? 0.2158 0.1948 0.2207 0.0482  0.0012  -0.0159 1045 HIS B C   
16816 O O   . HIS B 1047 ? 0.2308 0.2119 0.2372 0.0460  0.0006  -0.0144 1045 HIS B O   
16817 C CB  A HIS B 1047 ? 0.2361 0.2192 0.2404 0.0465  0.0023  -0.0189 1045 HIS B CB  
16818 C CB  B HIS B 1047 ? 0.2239 0.2071 0.2284 0.0458  0.0022  -0.0187 1045 HIS B CB  
16819 C CG  A HIS B 1047 ? 0.2094 0.1976 0.2141 0.0472  0.0035  -0.0201 1045 HIS B CG  
16820 C CG  B HIS B 1047 ? 0.2676 0.2432 0.2695 0.0447  0.0013  -0.0196 1045 HIS B CG  
16821 N ND1 A HIS B 1047 ? 0.2501 0.2378 0.2535 0.0502  0.0045  -0.0214 1045 HIS B ND1 
16822 N ND1 B HIS B 1047 ? 0.2790 0.2495 0.2782 0.0466  0.0015  -0.0213 1045 HIS B ND1 
16823 C CD2 A HIS B 1047 ? 0.2426 0.2366 0.2489 0.0453  0.0039  -0.0199 1045 HIS B CD2 
16824 C CD2 B HIS B 1047 ? 0.2697 0.2422 0.2715 0.0417  0.0003  -0.0191 1045 HIS B CD2 
16825 C CE1 A HIS B 1047 ? 0.3056 0.2988 0.3099 0.0501  0.0055  -0.0220 1045 HIS B CE1 
16826 C CE1 B HIS B 1047 ? 0.2689 0.2332 0.2663 0.0447  0.0004  -0.0218 1045 HIS B CE1 
16827 N NE2 A HIS B 1047 ? 0.2696 0.2665 0.2756 0.0470  0.0051  -0.0211 1045 HIS B NE2 
16828 N NE2 B HIS B 1047 ? 0.2948 0.2605 0.2939 0.0417  -0.0003 -0.0204 1045 HIS B NE2 
16829 N N   . THR B 1048 ? 0.2250 0.1975 0.2278 0.0500  0.0008  -0.0164 1046 THR B N   
16830 C CA  . THR B 1048 ? 0.2268 0.1936 0.2286 0.0490  -0.0003 -0.0151 1046 THR B CA  
16831 C C   . THR B 1048 ? 0.2410 0.2009 0.2403 0.0474  -0.0009 -0.0166 1046 THR B C   
16832 O O   . THR B 1048 ? 0.2557 0.2121 0.2528 0.0491  -0.0006 -0.0185 1046 THR B O   
16833 C CB  . THR B 1048 ? 0.2436 0.2078 0.2450 0.0525  -0.0004 -0.0140 1046 THR B CB  
16834 O OG1 . THR B 1048 ? 0.2648 0.2360 0.2688 0.0544  0.0001  -0.0128 1046 THR B OG1 
16835 C CG2 . THR B 1048 ? 0.2850 0.2442 0.2858 0.0511  -0.0015 -0.0122 1046 THR B CG2 
16836 N N   . ASP B 1049 ? 0.2299 0.1879 0.2294 0.0440  -0.0017 -0.0158 1047 ASP B N   
16837 C CA  . ASP B 1049 ? 0.2234 0.1753 0.2207 0.0420  -0.0025 -0.0171 1047 ASP B CA  
16838 C C   . ASP B 1049 ? 0.2304 0.1745 0.2249 0.0442  -0.0030 -0.0175 1047 ASP B C   
16839 O O   . ASP B 1049 ? 0.2484 0.1905 0.2431 0.0454  -0.0033 -0.0157 1047 ASP B O   
16840 C CB  . ASP B 1049 ? 0.2170 0.1686 0.2154 0.0382  -0.0033 -0.0157 1047 ASP B CB  
16841 C CG  . ASP B 1049 ? 0.2468 0.1928 0.2435 0.0359  -0.0042 -0.0168 1047 ASP B CG  
16842 O OD1 . ASP B 1049 ? 0.2568 0.1962 0.2517 0.0360  -0.0050 -0.0166 1047 ASP B OD1 
16843 O OD2 . ASP B 1049 ? 0.2474 0.1955 0.2444 0.0340  -0.0042 -0.0180 1047 ASP B OD2 
16844 N N   . PRO B 1050 ? 0.2549 0.1944 0.2467 0.0449  -0.0031 -0.0197 1048 PRO B N   
16845 C CA  . PRO B 1050 ? 0.2718 0.2035 0.2606 0.0474  -0.0035 -0.0204 1048 PRO B CA  
16846 C C   . PRO B 1050 ? 0.2689 0.1939 0.2566 0.0451  -0.0049 -0.0192 1048 PRO B C   
16847 O O   . PRO B 1050 ? 0.2968 0.2160 0.2829 0.0471  -0.0054 -0.0186 1048 PRO B O   
16848 C CB  . PRO B 1050 ? 0.3056 0.2346 0.2916 0.0482  -0.0033 -0.0233 1048 PRO B CB  
16849 C CG  . PRO B 1050 ? 0.3107 0.2435 0.2978 0.0446  -0.0034 -0.0239 1048 PRO B CG  
16850 C CD  . PRO B 1050 ? 0.2881 0.2291 0.2790 0.0437  -0.0028 -0.0219 1048 PRO B CD  
16851 N N   . VAL B 1051 ? 0.2762 0.2015 0.2648 0.0409  -0.0057 -0.0188 1049 VAL B N   
16852 C CA  . VAL B 1051 ? 0.2619 0.1815 0.2499 0.0384  -0.0070 -0.0174 1049 VAL B CA  
16853 C C   . VAL B 1051 ? 0.2521 0.1737 0.2420 0.0386  -0.0069 -0.0145 1049 VAL B C   
16854 O O   . VAL B 1051 ? 0.2804 0.1962 0.2691 0.0387  -0.0076 -0.0132 1049 VAL B O   
16855 C CB  . VAL B 1051 ? 0.3011 0.2214 0.2899 0.0340  -0.0078 -0.0178 1049 VAL B CB  
16856 C CG1 . VAL B 1051 ? 0.3125 0.2274 0.3011 0.0311  -0.0090 -0.0161 1049 VAL B CG1 
16857 C CG2 . VAL B 1051 ? 0.2920 0.2097 0.2784 0.0339  -0.0081 -0.0207 1049 VAL B CG2 
16858 N N   . LEU B 1052 ? 0.2442 0.1738 0.2370 0.0386  -0.0060 -0.0135 1050 LEU B N   
16859 C CA  . LEU B 1052 ? 0.2553 0.1872 0.2495 0.0395  -0.0058 -0.0109 1050 LEU B CA  
16860 C C   . LEU B 1052 ? 0.2735 0.2013 0.2661 0.0434  -0.0058 -0.0105 1050 LEU B C   
16861 O O   . LEU B 1052 ? 0.2665 0.1907 0.2585 0.0436  -0.0064 -0.0085 1050 LEU B O   
16862 C CB  . LEU B 1052 ? 0.2378 0.1788 0.2349 0.0395  -0.0048 -0.0103 1050 LEU B CB  
16863 C CG  . LEU B 1052 ? 0.2201 0.1648 0.2188 0.0402  -0.0046 -0.0077 1050 LEU B CG  
16864 C CD1 . LEU B 1052 ? 0.2509 0.1957 0.2492 0.0444  -0.0044 -0.0072 1050 LEU B CD1 
16865 C CD2 . LEU B 1052 ? 0.2422 0.1834 0.2406 0.0376  -0.0053 -0.0056 1050 LEU B CD2 
16866 N N   . LEU B 1053 ? 0.2593 0.1877 0.2510 0.0468  -0.0051 -0.0124 1051 LEU B N   
16867 C CA  . LEU B 1053 ? 0.2922 0.2171 0.2825 0.0510  -0.0051 -0.0122 1051 LEU B CA  
16868 C C   . LEU B 1053 ? 0.2935 0.2082 0.2806 0.0509  -0.0062 -0.0121 1051 LEU B C   
16869 O O   . LEU B 1053 ? 0.3176 0.2287 0.3040 0.0527  -0.0067 -0.0103 1051 LEU B O   
16870 C CB  . LEU B 1053 ? 0.3228 0.2500 0.3126 0.0544  -0.0040 -0.0145 1051 LEU B CB  
16871 C CG  . LEU B 1053 ? 0.3641 0.3012 0.3571 0.0554  -0.0029 -0.0141 1051 LEU B CG  
16872 C CD1 . LEU B 1053 ? 0.3214 0.2606 0.3138 0.0581  -0.0017 -0.0166 1051 LEU B CD1 
16873 C CD2 . LEU B 1053 ? 0.3769 0.3170 0.3717 0.0577  -0.0029 -0.0117 1051 LEU B CD2 
16874 N N   . ASP B 1054 ? 0.3141 0.2238 0.2991 0.0487  -0.0068 -0.0140 1052 ASP B N   
16875 C CA  . ASP B 1054 ? 0.3510 0.2507 0.3329 0.0480  -0.0081 -0.0140 1052 ASP B CA  
16876 C C   . ASP B 1054 ? 0.2974 0.1955 0.2803 0.0451  -0.0089 -0.0111 1052 ASP B C   
16877 O O   . ASP B 1054 ? 0.3310 0.2219 0.3118 0.0458  -0.0098 -0.0099 1052 ASP B O   
16878 C CB  . ASP B 1054 ? 0.3499 0.2457 0.3297 0.0456  -0.0087 -0.0166 1052 ASP B CB  
16879 C CG  . ASP B 1054 ? 0.4205 0.3161 0.3983 0.0488  -0.0079 -0.0196 1052 ASP B CG  
16880 O OD1 . ASP B 1054 ? 0.4107 0.3069 0.3881 0.0532  -0.0070 -0.0197 1052 ASP B OD1 
16881 O OD2 . ASP B 1054 ? 0.4571 0.3518 0.4336 0.0470  -0.0081 -0.0217 1052 ASP B OD2 
16882 N N   . PHE B 1055 ? 0.2800 0.1845 0.2657 0.0418  -0.0087 -0.0098 1053 PHE B N   
16883 C CA  . PHE B 1055 ? 0.2758 0.1794 0.2624 0.0390  -0.0093 -0.0070 1053 PHE B CA  
16884 C C   . PHE B 1055 ? 0.3107 0.2150 0.2976 0.0417  -0.0091 -0.0046 1053 PHE B C   
16885 O O   . PHE B 1055 ? 0.3083 0.2072 0.2940 0.0410  -0.0099 -0.0025 1053 PHE B O   
16886 C CB  . PHE B 1055 ? 0.2956 0.2067 0.2854 0.0355  -0.0088 -0.0064 1053 PHE B CB  
16887 C CG  . PHE B 1055 ? 0.2713 0.1821 0.2621 0.0323  -0.0092 -0.0036 1053 PHE B CG  
16888 C CD1 . PHE B 1055 ? 0.3030 0.2065 0.2921 0.0297  -0.0103 -0.0029 1053 PHE B CD1 
16889 C CD2 . PHE B 1055 ? 0.2692 0.1870 0.2624 0.0316  -0.0084 -0.0017 1053 PHE B CD2 
16890 C CE1 . PHE B 1055 ? 0.3096 0.2132 0.2997 0.0267  -0.0105 -0.0002 1053 PHE B CE1 
16891 C CE2 . PHE B 1055 ? 0.2866 0.2043 0.2805 0.0288  -0.0086 0.0009  1053 PHE B CE2 
16892 C CZ  . PHE B 1055 ? 0.2889 0.1997 0.2814 0.0263  -0.0096 0.0017  1053 PHE B CZ  
16893 N N   . ALA B 1056 ? 0.2915 0.2022 0.2800 0.0448  -0.0082 -0.0047 1054 ALA B N   
16894 C CA  . ALA B 1056 ? 0.2874 0.1993 0.2764 0.0475  -0.0081 -0.0024 1054 ALA B CA  
16895 C C   . ALA B 1056 ? 0.3090 0.2124 0.2950 0.0508  -0.0088 -0.0023 1054 ALA B C   
16896 O O   . ALA B 1056 ? 0.3321 0.2324 0.3174 0.0514  -0.0094 0.0002  1054 ALA B O   
16897 C CB  . ALA B 1056 ? 0.2922 0.2129 0.2835 0.0501  -0.0071 -0.0028 1054 ALA B CB  
16898 N N   . LYS B 1057 ? 0.3305 0.2299 0.3146 0.0529  -0.0087 -0.0050 1055 LYS B N   
16899 C CA  . LYS B 1057 ? 0.3654 0.2559 0.3464 0.0560  -0.0093 -0.0052 1055 LYS B CA  
16900 C C   . LYS B 1057 ? 0.3937 0.2754 0.3723 0.0529  -0.0107 -0.0039 1055 LYS B C   
16901 O O   . LYS B 1057 ? 0.3930 0.2685 0.3698 0.0546  -0.0115 -0.0022 1055 LYS B O   
16902 C CB  . LYS B 1057 ? 0.4005 0.2882 0.3795 0.0585  -0.0089 -0.0087 1055 LYS B CB  
16903 C CG  . LYS B 1057 ? 0.4402 0.3348 0.4208 0.0628  -0.0075 -0.0097 1055 LYS B CG  
16904 C CD  . LYS B 1057 ? 0.3862 0.2773 0.3643 0.0653  -0.0069 -0.0131 1055 LYS B CD  
16905 C CE  . LYS B 1057 ? 0.4093 0.2997 0.3865 0.0614  -0.0071 -0.0152 1055 LYS B CE  
16906 N NZ  . LYS B 1057 ? 0.4841 0.3738 0.4593 0.0639  -0.0062 -0.0186 1055 LYS B NZ  
16907 N N   . TRP B 1058 ? 0.3541 0.2353 0.3329 0.0483  -0.0111 -0.0046 1056 TRP B N   
16908 C CA  . TRP B 1058 ? 0.4030 0.2765 0.3799 0.0448  -0.0124 -0.0032 1056 TRP B CA  
16909 C C   . TRP B 1058 ? 0.3699 0.2450 0.3481 0.0436  -0.0126 0.0005  1056 TRP B C   
16910 O O   . TRP B 1058 ? 0.4117 0.2792 0.3877 0.0434  -0.0136 0.0023  1056 TRP B O   
16911 C CB  . TRP B 1058 ? 0.3618 0.2361 0.3393 0.0401  -0.0127 -0.0046 1056 TRP B CB  
16912 C CG  . TRP B 1058 ? 0.3973 0.2652 0.3738 0.0359  -0.0140 -0.0030 1056 TRP B CG  
16913 C CD1 . TRP B 1058 ? 0.4676 0.3251 0.4405 0.0352  -0.0154 -0.0037 1056 TRP B CD1 
16914 C CD2 . TRP B 1058 ? 0.3732 0.2446 0.3520 0.0316  -0.0141 -0.0005 1056 TRP B CD2 
16915 N NE1 . TRP B 1058 ? 0.4601 0.3147 0.4333 0.0306  -0.0163 -0.0017 1056 TRP B NE1 
16916 C CE2 . TRP B 1058 ? 0.4503 0.3135 0.4272 0.0284  -0.0154 0.0004  1056 TRP B CE2 
16917 C CE3 . TRP B 1058 ? 0.3870 0.2676 0.3692 0.0302  -0.0130 0.0011  1056 TRP B CE3 
16918 C CZ2 . TRP B 1058 ? 0.4207 0.2852 0.3992 0.0238  -0.0157 0.0028  1056 TRP B CZ2 
16919 C CZ3 . TRP B 1058 ? 0.4348 0.3164 0.4185 0.0259  -0.0132 0.0034  1056 TRP B CZ3 
16920 C CH2 . TRP B 1058 ? 0.3872 0.2611 0.3692 0.0228  -0.0145 0.0043  1056 TRP B CH2 
16921 N N   . LEU B 1059 ? 0.3343 0.2188 0.3157 0.0428  -0.0117 0.0018  1057 LEU B N   
16922 C CA  . LEU B 1059 ? 0.3714 0.2580 0.3538 0.0418  -0.0117 0.0052  1057 LEU B CA  
16923 C C   . LEU B 1059 ? 0.4453 0.3283 0.4261 0.0460  -0.0121 0.0069  1057 LEU B C   
16924 O O   . LEU B 1059 ? 0.4443 0.3227 0.4237 0.0453  -0.0129 0.0096  1057 LEU B O   
16925 C CB  . LEU B 1059 ? 0.3364 0.2337 0.3221 0.0408  -0.0107 0.0058  1057 LEU B CB  
16926 C CG  . LEU B 1059 ? 0.3111 0.2122 0.2987 0.0363  -0.0103 0.0050  1057 LEU B CG  
16927 C CD1 . LEU B 1059 ? 0.3151 0.2263 0.3056 0.0361  -0.0092 0.0052  1057 LEU B CD1 
16928 C CD2 . LEU B 1059 ? 0.3724 0.2695 0.3594 0.0323  -0.0109 0.0073  1057 LEU B CD2 
16929 N N   . ASP B 1060 ? 0.3916 0.2770 0.3726 0.0506  -0.0116 0.0054  1058 ASP B N   
16930 C CA  . ASP B 1060 ? 0.4212 0.3035 0.4011 0.0550  -0.0121 0.0070  1058 ASP B CA  
16931 C C   . ASP B 1060 ? 0.5003 0.3708 0.4764 0.0558  -0.0132 0.0069  1058 ASP B C   
16932 O O   . ASP B 1060 ? 0.5191 0.3848 0.4936 0.0572  -0.0140 0.0095  1058 ASP B O   
16933 C CB  . ASP B 1060 ? 0.4764 0.3642 0.4577 0.0597  -0.0112 0.0053  1058 ASP B CB  
16934 C CG  . ASP B 1060 ? 0.4966 0.3944 0.4810 0.0603  -0.0106 0.0070  1058 ASP B CG  
16935 O OD1 . ASP B 1060 ? 0.5700 0.4680 0.5544 0.0599  -0.0112 0.0101  1058 ASP B OD1 
16936 O OD2 . ASP B 1060 ? 0.4748 0.3802 0.4616 0.0611  -0.0096 0.0053  1058 ASP B OD2 
16937 N N   . GLY B 1061 ? 0.4722 0.3374 0.4465 0.0548  -0.0134 0.0041  1059 GLY B N   
16938 C CA  . GLY B 1061 ? 0.4801 0.3334 0.4505 0.0551  -0.0146 0.0038  1059 GLY B CA  
16939 C C   . GLY B 1061 ? 0.5288 0.3769 0.4980 0.0513  -0.0157 0.0070  1059 GLY B C   
16940 O O   . GLY B 1061 ? 0.5492 0.3884 0.5155 0.0526  -0.0167 0.0083  1059 GLY B O   
16941 N N   . LYS B 1062 ? 0.4971 0.3508 0.4687 0.0466  -0.0154 0.0083  1060 LYS B N   
16942 C CA  . LYS B 1062 ? 0.4891 0.3388 0.4599 0.0427  -0.0162 0.0114  1060 LYS B CA  
16943 C C   . LYS B 1062 ? 0.5708 0.4253 0.5429 0.0433  -0.0159 0.0149  1060 LYS B C   
16944 O O   . LYS B 1062 ? 0.5820 0.4348 0.5538 0.0399  -0.0163 0.0178  1060 LYS B O   
16945 C CB  . LYS B 1062 ? 0.5313 0.3832 0.5036 0.0370  -0.0162 0.0108  1060 LYS B CB  
16946 C CG  . LYS B 1062 ? 0.5668 0.4302 0.5430 0.0355  -0.0149 0.0107  1060 LYS B CG  
16947 C CD  . LYS B 1062 ? 0.5078 0.3724 0.4853 0.0302  -0.0149 0.0099  1060 LYS B CD  
16948 C CE  . LYS B 1062 ? 0.5058 0.3654 0.4825 0.0261  -0.0157 0.0128  1060 LYS B CE  
16949 N NZ  . LYS B 1062 ? 0.5596 0.4183 0.5371 0.0213  -0.0162 0.0118  1060 LYS B NZ  
16950 N N   . GLY B 1063 ? 0.5500 0.4104 0.5235 0.0476  -0.0153 0.0150  1061 GLY B N   
16951 C CA  . GLY B 1063 ? 0.5365 0.4008 0.5107 0.0486  -0.0152 0.0183  1061 GLY B CA  
16952 C C   . GLY B 1063 ? 0.5914 0.4656 0.5686 0.0456  -0.0143 0.0194  1061 GLY B C   
16953 O O   . GLY B 1063 ? 0.5689 0.4462 0.5464 0.0460  -0.0143 0.0223  1061 GLY B O   
16954 N N   . ALA B 1064 ? 0.4967 0.3757 0.4759 0.0427  -0.0135 0.0173  1062 ALA B N   
16955 C CA  . ALA B 1064 ? 0.4892 0.3774 0.4711 0.0400  -0.0125 0.0181  1062 ALA B CA  
16956 C C   . ALA B 1064 ? 0.4762 0.3729 0.4602 0.0434  -0.0118 0.0172  1062 ALA B C   
16957 O O   . ALA B 1064 ? 0.4114 0.3139 0.3974 0.0433  -0.0110 0.0147  1062 ALA B O   
16958 C CB  . ALA B 1064 ? 0.4537 0.3436 0.4370 0.0358  -0.0121 0.0162  1062 ALA B CB  
16959 N N   . ARG B 1065 ? 0.4644 0.3618 0.4478 0.0464  -0.0122 0.0194  1063 ARG B N   
16960 C CA  . ARG B 1065 ? 0.4324 0.3368 0.4176 0.0501  -0.0119 0.0187  1063 ARG B CA  
16961 C C   . ARG B 1065 ? 0.4158 0.3301 0.4036 0.0480  -0.0109 0.0184  1063 ARG B C   
16962 O O   . ARG B 1065 ? 0.4227 0.3429 0.4126 0.0494  -0.0102 0.0162  1063 ARG B O   
16963 C CB  . ARG B 1065 ? 0.5143 0.4171 0.4983 0.0535  -0.0127 0.0215  1063 ARG B CB  
16964 N N   . ALA B 1066 ? 0.3830 0.2992 0.3708 0.0447  -0.0108 0.0207  1064 ALA B N   
16965 C CA  . ALA B 1066 ? 0.3716 0.2967 0.3616 0.0427  -0.0098 0.0203  1064 ALA B CA  
16966 C C   . ALA B 1066 ? 0.3700 0.2973 0.3616 0.0407  -0.0090 0.0172  1064 ALA B C   
16967 O O   . ALA B 1066 ? 0.3670 0.3014 0.3607 0.0410  -0.0083 0.0156  1064 ALA B O   
16968 C CB  . ALA B 1066 ? 0.4090 0.3349 0.3982 0.0394  -0.0097 0.0231  1064 ALA B CB  
16969 N N   . GLU B 1067 ? 0.3385 0.2598 0.3293 0.0385  -0.0092 0.0164  1065 GLU B N   
16970 C CA  . GLU B 1067 ? 0.3610 0.2843 0.3532 0.0364  -0.0086 0.0137  1065 GLU B CA  
16971 C C   . GLU B 1067 ? 0.3154 0.2396 0.3082 0.0395  -0.0084 0.0108  1065 GLU B C   
16972 O O   . GLU B 1067 ? 0.3101 0.2396 0.3046 0.0388  -0.0077 0.0088  1065 GLU B O   
16973 C CB  . GLU B 1067 ? 0.3642 0.2810 0.3554 0.0331  -0.0090 0.0138  1065 GLU B CB  
16974 C CG  . GLU B 1067 ? 0.3600 0.2777 0.3514 0.0292  -0.0086 0.0163  1065 GLU B CG  
16975 C CD  . GLU B 1067 ? 0.4137 0.3270 0.4029 0.0298  -0.0093 0.0195  1065 GLU B CD  
16976 O OE1 . GLU B 1067 ? 0.4215 0.3301 0.4090 0.0331  -0.0101 0.0198  1065 GLU B OE1 
16977 O OE2 . GLU B 1067 ? 0.4426 0.3572 0.4318 0.0270  -0.0089 0.0219  1065 GLU B OE2 
16978 N N   . ALA B 1068 ? 0.3232 0.2421 0.3143 0.0429  -0.0091 0.0106  1066 ALA B N   
16979 C CA  . ALA B 1068 ? 0.3458 0.2657 0.3373 0.0462  -0.0088 0.0080  1066 ALA B CA  
16980 C C   . ALA B 1068 ? 0.3066 0.2356 0.3005 0.0481  -0.0081 0.0078  1066 ALA B C   
16981 O O   . ALA B 1068 ? 0.2944 0.2276 0.2896 0.0487  -0.0074 0.0054  1066 ALA B O   
16982 C CB  . ALA B 1068 ? 0.3298 0.2422 0.3190 0.0499  -0.0095 0.0081  1066 ALA B CB  
16983 N N   . GLU B 1069 ? 0.2962 0.2283 0.2904 0.0489  -0.0084 0.0103  1067 GLU B N   
16984 C CA  . GLU B 1069 ? 0.3454 0.2864 0.3419 0.0501  -0.0079 0.0104  1067 GLU B CA  
16985 C C   . GLU B 1069 ? 0.3421 0.2891 0.3404 0.0466  -0.0071 0.0092  1067 GLU B C   
16986 O O   . GLU B 1069 ? 0.3172 0.2702 0.3172 0.0474  -0.0065 0.0076  1067 GLU B O   
16987 C CB  . GLU B 1069 ? 0.3988 0.3415 0.3950 0.0511  -0.0086 0.0135  1067 GLU B CB  
16988 C CG  . GLU B 1069 ? 0.4031 0.3549 0.4014 0.0518  -0.0084 0.0138  1067 GLU B CG  
16989 C CD  . GLU B 1069 ? 0.5125 0.4679 0.5125 0.0558  -0.0082 0.0124  1067 GLU B CD  
16990 O OE1 . GLU B 1069 ? 0.5017 0.4521 0.5009 0.0586  -0.0083 0.0115  1067 GLU B OE1 
16991 O OE2 . GLU B 1069 ? 0.6099 0.5731 0.6119 0.0561  -0.0080 0.0122  1067 GLU B OE2 
16992 N N   . ALA B 1070 ? 0.3124 0.2579 0.3101 0.0429  -0.0070 0.0102  1068 ALA B N   
16993 C CA  . ALA B 1070 ? 0.3345 0.2851 0.3338 0.0398  -0.0062 0.0090  1068 ALA B CA  
16994 C C   . ALA B 1070 ? 0.2524 0.2025 0.2523 0.0396  -0.0058 0.0060  1068 ALA B C   
16995 O O   . ALA B 1070 ? 0.2913 0.2470 0.2929 0.0389  -0.0052 0.0045  1068 ALA B O   
16996 C CB  . ALA B 1070 ? 0.3560 0.3046 0.3547 0.0360  -0.0061 0.0106  1068 ALA B CB  
16997 N N   . ALA B 1071 ? 0.2718 0.2150 0.2702 0.0403  -0.0063 0.0051  1069 ALA B N   
16998 C CA  . ALA B 1071 ? 0.2553 0.1977 0.2539 0.0402  -0.0060 0.0022  1069 ALA B CA  
16999 C C   . ALA B 1071 ? 0.2616 0.2087 0.2612 0.0434  -0.0054 0.0006  1069 ALA B C   
17000 O O   . ALA B 1071 ? 0.2655 0.2170 0.2664 0.0426  -0.0048 -0.0013 1069 ALA B O   
17001 C CB  . ALA B 1071 ? 0.2476 0.1812 0.2439 0.0404  -0.0067 0.0015  1069 ALA B CB  
17002 N N   . ARG B 1072 ? 0.2612 0.2077 0.2604 0.0471  -0.0057 0.0014  1070 ARG B N   
17003 C CA  A ARG B 1072 ? 0.2697 0.2214 0.2702 0.0502  -0.0051 0.0001  1070 ARG B CA  
17004 C CA  B ARG B 1072 ? 0.2699 0.2216 0.2705 0.0501  -0.0051 0.0001  1070 ARG B CA  
17005 C C   . ARG B 1072 ? 0.2783 0.2387 0.2812 0.0489  -0.0046 0.0004  1070 ARG B C   
17006 O O   . ARG B 1072 ? 0.2542 0.2194 0.2586 0.0493  -0.0039 -0.0013 1070 ARG B O   
17007 C CB  A ARG B 1072 ? 0.2938 0.2440 0.2939 0.0544  -0.0055 0.0014  1070 ARG B CB  
17008 C CB  B ARG B 1072 ? 0.2943 0.2441 0.2943 0.0544  -0.0054 0.0012  1070 ARG B CB  
17009 C CG  A ARG B 1072 ? 0.3394 0.2813 0.3371 0.0567  -0.0058 0.0004  1070 ARG B CG  
17010 C CG  B ARG B 1072 ? 0.3326 0.2731 0.3299 0.0559  -0.0059 0.0006  1070 ARG B CG  
17011 C CD  A ARG B 1072 ? 0.3093 0.2504 0.3069 0.0613  -0.0061 0.0016  1070 ARG B CD  
17012 C CD  B ARG B 1072 ? 0.3137 0.2526 0.3105 0.0609  -0.0061 0.0009  1070 ARG B CD  
17013 N NE  A ARG B 1072 ? 0.3378 0.2779 0.3351 0.0609  -0.0070 0.0048  1070 ARG B NE  
17014 N NE  B ARG B 1072 ? 0.3467 0.2759 0.3405 0.0622  -0.0066 0.0004  1070 ARG B NE  
17015 C CZ  A ARG B 1072 ? 0.3763 0.3083 0.3711 0.0609  -0.0079 0.0062  1070 ARG B CZ  
17016 C CZ  B ARG B 1072 ? 0.3381 0.2632 0.3304 0.0627  -0.0062 -0.0023 1070 ARG B CZ  
17017 N NH1 A ARG B 1072 ? 0.3541 0.2781 0.3465 0.0613  -0.0081 0.0046  1070 ARG B NH1 
17018 N NH1 B ARG B 1072 ? 0.3765 0.3066 0.3700 0.0624  -0.0052 -0.0046 1070 ARG B NH1 
17019 N NH2 A ARG B 1072 ? 0.3268 0.2585 0.3212 0.0604  -0.0087 0.0091  1070 ARG B NH2 
17020 N NH2 B ARG B 1072 ? 0.3562 0.2717 0.3453 0.0634  -0.0069 -0.0027 1070 ARG B NH2 
17021 N N   . ASN B 1073 ? 0.2497 0.2123 0.2531 0.0472  -0.0049 0.0027  1071 ASN B N   
17022 C CA  . ASN B 1073 ? 0.2616 0.2320 0.2668 0.0459  -0.0045 0.0029  1071 ASN B CA  
17023 C C   . ASN B 1073 ? 0.2673 0.2396 0.2732 0.0428  -0.0039 0.0011  1071 ASN B C   
17024 O O   . ASN B 1073 ? 0.2797 0.2579 0.2872 0.0426  -0.0034 0.0001  1071 ASN B O   
17025 C CB  . ASN B 1073 ? 0.2846 0.2560 0.2894 0.0446  -0.0050 0.0056  1071 ASN B CB  
17026 C CG  . ASN B 1073 ? 0.3818 0.3533 0.3863 0.0479  -0.0058 0.0075  1071 ASN B CG  
17027 O OD1 . ASN B 1073 ? 0.3924 0.3657 0.3978 0.0510  -0.0058 0.0067  1071 ASN B OD1 
17028 N ND2 . ASN B 1073 ? 0.4242 0.3939 0.4275 0.0471  -0.0064 0.0100  1071 ASN B ND2 
17029 N N   . ALA B 1074 ? 0.2442 0.2117 0.2491 0.0404  -0.0040 0.0008  1072 ALA B N   
17030 C CA  . ALA B 1074 ? 0.2640 0.2331 0.2696 0.0377  -0.0035 -0.0009 1072 ALA B CA  
17031 C C   . ALA B 1074 ? 0.2096 0.1792 0.2154 0.0391  -0.0031 -0.0034 1072 ALA B C   
17032 O O   . ALA B 1074 ? 0.2389 0.2130 0.2459 0.0380  -0.0026 -0.0047 1072 ALA B O   
17033 C CB  . ALA B 1074 ? 0.2522 0.2160 0.2568 0.0350  -0.0037 -0.0006 1072 ALA B CB  
17034 N N   . GLY B 1075 ? 0.2230 0.1880 0.2275 0.0417  -0.0033 -0.0041 1073 GLY B N   
17035 C CA  . GLY B 1075 ? 0.2556 0.2210 0.2599 0.0433  -0.0028 -0.0064 1073 GLY B CA  
17036 C C   . GLY B 1075 ? 0.2668 0.2397 0.2730 0.0447  -0.0021 -0.0067 1073 GLY B C   
17037 O O   . GLY B 1075 ? 0.2611 0.2368 0.2678 0.0443  -0.0015 -0.0085 1073 GLY B O   
17038 N N   . SER B 1076 ? 0.2658 0.2421 0.2731 0.0462  -0.0023 -0.0049 1074 SER B N   
17039 C CA  . SER B 1076 ? 0.2457 0.2292 0.2549 0.0475  -0.0018 -0.0051 1074 SER B CA  
17040 C C   . SER B 1076 ? 0.2480 0.2369 0.2586 0.0445  -0.0016 -0.0049 1074 SER B C   
17041 O O   . SER B 1076 ? 0.2795 0.2731 0.2913 0.0443  -0.0011 -0.0061 1074 SER B O   
17042 C CB  . SER B 1076 ? 0.2834 0.2686 0.2933 0.0504  -0.0023 -0.0031 1074 SER B CB  
17043 O OG  . SER B 1076 ? 0.3204 0.3016 0.3294 0.0538  -0.0022 -0.0036 1074 SER B OG  
17044 N N   . SER B 1077 ? 0.2359 0.2240 0.2462 0.0421  -0.0021 -0.0036 1075 SER B N   
17045 C CA  A SER B 1077 ? 0.2853 0.2780 0.2965 0.0394  -0.0019 -0.0034 1075 SER B CA  
17046 C CA  B SER B 1077 ? 0.2854 0.2784 0.2967 0.0395  -0.0019 -0.0035 1075 SER B CA  
17047 C C   . SER B 1077 ? 0.2538 0.2462 0.2651 0.0370  -0.0014 -0.0052 1075 SER B C   
17048 O O   . SER B 1077 ? 0.3090 0.3057 0.3212 0.0353  -0.0011 -0.0056 1075 SER B O   
17049 C CB  A SER B 1077 ? 0.3177 0.3095 0.3282 0.0378  -0.0023 -0.0014 1075 SER B CB  
17050 C CB  B SER B 1077 ? 0.3228 0.3158 0.3337 0.0380  -0.0023 -0.0014 1075 SER B CB  
17051 O OG  A SER B 1077 ? 0.3144 0.3069 0.3248 0.0399  -0.0029 0.0004  1075 SER B OG  
17052 O OG  B SER B 1077 ? 0.3088 0.2967 0.3184 0.0361  -0.0024 -0.0011 1075 SER B OG  
17053 N N   . SER B 1078 ? 0.2229 0.2099 0.2330 0.0368  -0.0015 -0.0062 1076 SER B N   
17054 C CA  . SER B 1078 ? 0.2162 0.2027 0.2263 0.0346  -0.0012 -0.0078 1076 SER B CA  
17055 C C   . SER B 1078 ? 0.2097 0.2008 0.2207 0.0353  -0.0006 -0.0093 1076 SER B C   
17056 O O   . SER B 1078 ? 0.2176 0.2099 0.2287 0.0379  -0.0004 -0.0097 1076 SER B O   
17057 C CB  . SER B 1078 ? 0.2199 0.2001 0.2284 0.0350  -0.0015 -0.0088 1076 SER B CB  
17058 O OG  . SER B 1078 ? 0.2020 0.1820 0.2104 0.0332  -0.0014 -0.0106 1076 SER B OG  
17059 N N   . ALA B 1079 ? 0.1846 0.1783 0.1963 0.0330  -0.0004 -0.0100 1077 ALA B N   
17060 C CA  . ALA B 1079 ? 0.1876 0.1852 0.1999 0.0331  0.0001  -0.0113 1077 ALA B CA  
17061 C C   . ALA B 1079 ? 0.1918 0.1865 0.2030 0.0325  0.0002  -0.0131 1077 ALA B C   
17062 O O   . ALA B 1079 ? 0.1855 0.1830 0.1970 0.0320  0.0006  -0.0142 1077 ALA B O   
17063 C CB  . ALA B 1079 ? 0.1941 0.1965 0.2075 0.0312  0.0002  -0.0109 1077 ALA B CB  
17064 N N   . LEU B 1080 ? 0.1777 0.1668 0.1876 0.0324  -0.0003 -0.0134 1078 LEU B N   
17065 C CA  . LEU B 1080 ? 0.1826 0.1685 0.1912 0.0319  -0.0004 -0.0152 1078 LEU B CA  
17066 C C   . LEU B 1080 ? 0.1825 0.1700 0.1904 0.0342  0.0003  -0.0165 1078 LEU B C   
17067 O O   . LEU B 1080 ? 0.2014 0.1890 0.2092 0.0369  0.0006  -0.0162 1078 LEU B O   
17068 C CB  . LEU B 1080 ? 0.1939 0.1733 0.2010 0.0321  -0.0010 -0.0151 1078 LEU B CB  
17069 C CG  . LEU B 1080 ? 0.2012 0.1765 0.2063 0.0320  -0.0013 -0.0170 1078 LEU B CG  
17070 C CD1 . LEU B 1080 ? 0.2226 0.1986 0.2282 0.0290  -0.0017 -0.0176 1078 LEU B CD1 
17071 C CD2 . LEU B 1080 ? 0.2205 0.1890 0.2238 0.0326  -0.0020 -0.0170 1078 LEU B CD2 
17072 N N   . GLY B 1081 ? 0.1734 0.1625 0.1810 0.0332  0.0006  -0.0178 1079 GLY B N   
17073 C CA  . GLY B 1081 ? 0.1879 0.1788 0.1948 0.0351  0.0014  -0.0190 1079 GLY B CA  
17074 C C   . GLY B 1081 ? 0.2062 0.2039 0.2149 0.0351  0.0021  -0.0185 1079 GLY B C   
17075 O O   . GLY B 1081 ? 0.2241 0.2242 0.2325 0.0364  0.0029  -0.0194 1079 GLY B O   
17076 N N   . LEU B 1082 ? 0.1919 0.1926 0.2023 0.0336  0.0018  -0.0172 1080 LEU B N   
17077 C CA  A LEU B 1082 ? 0.2031 0.2097 0.2150 0.0330  0.0023  -0.0168 1080 LEU B CA  
17078 C CA  B LEU B 1082 ? 0.2030 0.2097 0.2150 0.0330  0.0023  -0.0168 1080 LEU B CA  
17079 C C   . LEU B 1082 ? 0.1966 0.2040 0.2078 0.0316  0.0026  -0.0181 1080 LEU B C   
17080 O O   . LEU B 1082 ? 0.2052 0.2094 0.2154 0.0300  0.0021  -0.0187 1080 LEU B O   
17081 C CB  A LEU B 1082 ? 0.1979 0.2063 0.2111 0.0311  0.0018  -0.0155 1080 LEU B CB  
17082 C CB  B LEU B 1082 ? 0.1979 0.2063 0.2111 0.0311  0.0018  -0.0155 1080 LEU B CB  
17083 C CG  A LEU B 1082 ? 0.1970 0.2109 0.2115 0.0299  0.0020  -0.0151 1080 LEU B CG  
17084 C CG  B LEU B 1082 ? 0.1969 0.2107 0.2113 0.0298  0.0020  -0.0151 1080 LEU B CG  
17085 C CD1 A LEU B 1082 ? 0.2319 0.2500 0.2474 0.0318  0.0024  -0.0147 1080 LEU B CD1 
17086 C CD1 B LEU B 1082 ? 0.1984 0.2136 0.2138 0.0290  0.0015  -0.0136 1080 LEU B CD1 
17087 C CD2 A LEU B 1082 ? 0.2109 0.2256 0.2261 0.0282  0.0015  -0.0139 1080 LEU B CD2 
17088 C CD2 B LEU B 1082 ? 0.1737 0.1875 0.1877 0.0274  0.0019  -0.0159 1080 LEU B CD2 
17089 N N   . ASP B 1083 ? 0.2100 0.2219 0.2218 0.0323  0.0033  -0.0183 1081 ASP B N   
17090 C CA  . ASP B 1083 ? 0.2553 0.2679 0.2660 0.0312  0.0037  -0.0194 1081 ASP B CA  
17091 C C   . ASP B 1083 ? 0.2351 0.2537 0.2473 0.0308  0.0043  -0.0189 1081 ASP B C   
17092 O O   . ASP B 1083 ? 0.2824 0.3042 0.2953 0.0328  0.0052  -0.0188 1081 ASP B O   
17093 C CB  . ASP B 1083 ? 0.2624 0.2721 0.2711 0.0332  0.0043  -0.0208 1081 ASP B CB  
17094 C CG  . ASP B 1083 ? 0.4070 0.4171 0.4141 0.0323  0.0047  -0.0220 1081 ASP B CG  
17095 O OD1 . ASP B 1083 ? 0.4317 0.4429 0.4391 0.0298  0.0042  -0.0218 1081 ASP B OD1 
17096 O OD2 . ASP B 1083 ? 0.4629 0.4721 0.4683 0.0340  0.0054  -0.0231 1081 ASP B OD2 
17097 N N   . LEU B 1084 ? 0.2069 0.2272 0.2198 0.0284  0.0039  -0.0184 1082 LEU B N   
17098 C CA  . LEU B 1084 ? 0.2280 0.2537 0.2424 0.0275  0.0041  -0.0176 1082 LEU B CA  
17099 C C   . LEU B 1084 ? 0.2090 0.2355 0.2226 0.0255  0.0043  -0.0182 1082 LEU B C   
17100 O O   . LEU B 1084 ? 0.2112 0.2342 0.2235 0.0242  0.0038  -0.0188 1082 LEU B O   
17101 C CB  . LEU B 1084 ? 0.2603 0.2869 0.2759 0.0261  0.0034  -0.0165 1082 LEU B CB  
17102 C CG  . LEU B 1084 ? 0.3051 0.3317 0.3216 0.0277  0.0031  -0.0155 1082 LEU B CG  
17103 C CD1 . LEU B 1084 ? 0.3080 0.3353 0.3251 0.0260  0.0023  -0.0145 1082 LEU B CD1 
17104 C CD2 . LEU B 1084 ? 0.3325 0.3633 0.3504 0.0299  0.0036  -0.0150 1082 LEU B CD2 
17105 N N   . GLU B 1085 ? 0.1961 0.2272 0.2105 0.0251  0.0049  -0.0178 1083 GLU B N   
17106 C CA  . GLU B 1085 ? 0.1890 0.2213 0.2029 0.0228  0.0048  -0.0179 1083 GLU B CA  
17107 C C   . GLU B 1085 ? 0.1983 0.2331 0.2135 0.0210  0.0042  -0.0169 1083 GLU B C   
17108 O O   . GLU B 1085 ? 0.2299 0.2685 0.2468 0.0216  0.0043  -0.0160 1083 GLU B O   
17109 C CB  . GLU B 1085 ? 0.2130 0.2486 0.2266 0.0232  0.0059  -0.0181 1083 GLU B CB  
17110 C CG  . GLU B 1085 ? 0.2265 0.2627 0.2393 0.0205  0.0057  -0.0180 1083 GLU B CG  
17111 C CD  . GLU B 1085 ? 0.3037 0.3425 0.3157 0.0205  0.0068  -0.0182 1083 GLU B CD  
17112 O OE1 . GLU B 1085 ? 0.3476 0.3873 0.3593 0.0227  0.0078  -0.0187 1083 GLU B OE1 
17113 O OE2 . GLU B 1085 ? 0.2849 0.3249 0.2965 0.0183  0.0066  -0.0178 1083 GLU B OE2 
17114 N N   . LEU B 1086 ? 0.1858 0.2184 0.2003 0.0190  0.0035  -0.0170 1084 LEU B N   
17115 C CA  . LEU B 1086 ? 0.1781 0.2121 0.1933 0.0172  0.0029  -0.0162 1084 LEU B CA  
17116 C C   . LEU B 1086 ? 0.2266 0.2635 0.2418 0.0154  0.0030  -0.0160 1084 LEU B C   
17117 O O   . LEU B 1086 ? 0.2406 0.2766 0.2546 0.0148  0.0033  -0.0165 1084 LEU B O   
17118 C CB  . LEU B 1086 ? 0.2015 0.2314 0.2159 0.0162  0.0022  -0.0165 1084 LEU B CB  
17119 C CG  . LEU B 1086 ? 0.1905 0.2175 0.2050 0.0176  0.0020  -0.0166 1084 LEU B CG  
17120 C CD1 . LEU B 1086 ? 0.2347 0.2585 0.2488 0.0164  0.0015  -0.0167 1084 LEU B CD1 
17121 C CD2 . LEU B 1086 ? 0.2572 0.2863 0.2729 0.0187  0.0020  -0.0157 1084 LEU B CD2 
17122 N N   . PRO B 1087 ? 0.1951 0.2353 0.2114 0.0143  0.0026  -0.0152 1085 PRO B N   
17123 C CA  . PRO B 1087 ? 0.2267 0.2693 0.2428 0.0121  0.0026  -0.0149 1085 PRO B CA  
17124 C C   . PRO B 1087 ? 0.2263 0.2652 0.2407 0.0103  0.0021  -0.0153 1085 PRO B C   
17125 O O   . PRO B 1087 ? 0.2334 0.2690 0.2472 0.0101  0.0015  -0.0156 1085 PRO B O   
17126 C CB  . PRO B 1087 ? 0.2395 0.2853 0.2569 0.0113  0.0019  -0.0140 1085 PRO B CB  
17127 C CG  . PRO B 1087 ? 0.2606 0.3075 0.2793 0.0136  0.0020  -0.0137 1085 PRO B CG  
17128 C CD  . PRO B 1087 ? 0.2329 0.2750 0.2504 0.0150  0.0022  -0.0145 1085 PRO B CD  
17129 N N   . GLY B 1088 ? 0.2240 0.2633 0.2375 0.0091  0.0024  -0.0153 1086 GLY B N   
17130 C CA  . GLY B 1088 ? 0.2130 0.2489 0.2249 0.0074  0.0018  -0.0156 1086 GLY B CA  
17131 C C   . GLY B 1088 ? 0.1832 0.2207 0.1943 0.0058  0.0021  -0.0152 1086 GLY B C   
17132 O O   . GLY B 1088 ? 0.2024 0.2443 0.2145 0.0055  0.0027  -0.0146 1086 GLY B O   
17133 N N   . PRO B 1089 ? 0.1950 0.2293 0.2044 0.0048  0.0018  -0.0155 1087 PRO B N   
17134 C CA  . PRO B 1089 ? 0.1857 0.2209 0.1939 0.0030  0.0020  -0.0149 1087 PRO B CA  
17135 C C   . PRO B 1089 ? 0.1941 0.2317 0.2021 0.0041  0.0032  -0.0150 1087 PRO B C   
17136 O O   . PRO B 1089 ? 0.2094 0.2462 0.2174 0.0063  0.0037  -0.0157 1087 PRO B O   
17137 C CB  . PRO B 1089 ? 0.2367 0.2672 0.2430 0.0022  0.0013  -0.0152 1087 PRO B CB  
17138 C CG  . PRO B 1089 ? 0.2606 0.2883 0.2671 0.0042  0.0011  -0.0161 1087 PRO B CG  
17139 C CD  . PRO B 1089 ? 0.2085 0.2380 0.2168 0.0053  0.0012  -0.0161 1087 PRO B CD  
17140 N N   . VAL B 1090 ? 0.1800 0.2204 0.1877 0.0026  0.0037  -0.0142 1088 VAL B N   
17141 C CA  . VAL B 1090 ? 0.1976 0.2399 0.2046 0.0034  0.0049  -0.0142 1088 VAL B CA  
17142 C C   . VAL B 1090 ? 0.1969 0.2347 0.2013 0.0038  0.0047  -0.0149 1088 VAL B C   
17143 O O   . VAL B 1090 ? 0.1996 0.2333 0.2029 0.0029  0.0036  -0.0150 1088 VAL B O   
17144 C CB  . VAL B 1090 ? 0.1904 0.2367 0.1974 0.0013  0.0056  -0.0130 1088 VAL B CB  
17145 C CG1 . VAL B 1090 ? 0.1998 0.2511 0.2096 0.0008  0.0056  -0.0123 1088 VAL B CG1 
17146 C CG2 . VAL B 1090 ? 0.2185 0.2616 0.2234 -0.0013 0.0047  -0.0125 1088 VAL B CG2 
17147 N N   . GLY B 1091 ? 0.1894 0.2279 0.1927 0.0053  0.0057  -0.0153 1089 GLY B N   
17148 C CA  . GLY B 1091 ? 0.1933 0.2278 0.1939 0.0057  0.0054  -0.0160 1089 GLY B CA  
17149 C C   . GLY B 1091 ? 0.1977 0.2282 0.1983 0.0071  0.0045  -0.0170 1089 GLY B C   
17150 O O   . GLY B 1091 ? 0.1887 0.2154 0.1873 0.0070  0.0038  -0.0175 1089 GLY B O   
17151 N N   . GLU B 1092 ? 0.2028 0.2340 0.2055 0.0084  0.0045  -0.0173 1090 GLU B N   
17152 C CA  . GLU B 1092 ? 0.1888 0.2165 0.1917 0.0097  0.0038  -0.0182 1090 GLU B CA  
17153 C C   . GLU B 1092 ? 0.1977 0.2275 0.2024 0.0117  0.0045  -0.0184 1090 GLU B C   
17154 O O   . GLU B 1092 ? 0.2225 0.2562 0.2289 0.0117  0.0050  -0.0178 1090 GLU B O   
17155 C CB  . GLU B 1092 ? 0.2418 0.2675 0.2457 0.0085  0.0026  -0.0179 1090 GLU B CB  
17156 C CG  . GLU B 1092 ? 0.3270 0.3484 0.3299 0.0085  0.0016  -0.0184 1090 GLU B CG  
17157 C CD  . GLU B 1092 ? 0.2975 0.3174 0.3013 0.0074  0.0006  -0.0180 1090 GLU B CD  
17158 O OE1 . GLU B 1092 ? 0.2514 0.2723 0.2569 0.0077  0.0007  -0.0179 1090 GLU B OE1 
17159 O OE2 . GLU B 1092 ? 0.3061 0.3238 0.3088 0.0063  -0.0001 -0.0178 1090 GLU B OE2 
17160 N N   . ARG B 1093 ? 0.1966 0.2237 0.2007 0.0135  0.0043  -0.0194 1091 ARG B N   
17161 C CA  . ARG B 1093 ? 0.1776 0.2054 0.1832 0.0154  0.0047  -0.0196 1091 ARG B CA  
17162 C C   . ARG B 1093 ? 0.1893 0.2136 0.1955 0.0155  0.0036  -0.0198 1091 ARG B C   
17163 O O   . ARG B 1093 ? 0.1984 0.2190 0.2033 0.0153  0.0029  -0.0204 1091 ARG B O   
17164 C CB  . ARG B 1093 ? 0.2170 0.2445 0.2213 0.0176  0.0057  -0.0205 1091 ARG B CB  
17165 C CG  . ARG B 1093 ? 0.3353 0.3677 0.3401 0.0183  0.0071  -0.0201 1091 ARG B CG  
17166 C CD  . ARG B 1093 ? 0.4233 0.4555 0.4275 0.0211  0.0081  -0.0210 1091 ARG B CD  
17167 N NE  . ARG B 1093 ? 0.4733 0.5011 0.4743 0.0216  0.0080  -0.0223 1091 ARG B NE  
17168 C CZ  . ARG B 1093 ? 0.6113 0.6396 0.6099 0.0215  0.0087  -0.0227 1091 ARG B CZ  
17169 N NH1 . ARG B 1093 ? 0.5678 0.6007 0.5668 0.0208  0.0099  -0.0219 1091 ARG B NH1 
17170 N NH2 . ARG B 1093 ? 0.5798 0.6038 0.5754 0.0218  0.0083  -0.0239 1091 ARG B NH2 
17171 N N   . ASN B 1094 ? 0.1600 0.1856 0.1682 0.0156  0.0034  -0.0192 1092 ASN B N   
17172 C CA  . ASN B 1094 ? 0.1561 0.1788 0.1649 0.0154  0.0026  -0.0192 1092 ASN B CA  
17173 C C   . ASN B 1094 ? 0.1732 0.1959 0.1831 0.0174  0.0028  -0.0192 1092 ASN B C   
17174 O O   . ASN B 1094 ? 0.1934 0.2193 0.2046 0.0180  0.0032  -0.0186 1092 ASN B O   
17175 C CB  . ASN B 1094 ? 0.1711 0.1949 0.1809 0.0138  0.0021  -0.0185 1092 ASN B CB  
17176 C CG  . ASN B 1094 ? 0.1788 0.2013 0.1874 0.0120  0.0016  -0.0185 1092 ASN B CG  
17177 O OD1 . ASN B 1094 ? 0.1840 0.2033 0.1920 0.0118  0.0010  -0.0189 1092 ASN B OD1 
17178 N ND2 . ASN B 1094 ? 0.1948 0.2197 0.2031 0.0108  0.0019  -0.0181 1092 ASN B ND2 
17179 N N   . LEU B 1095 ? 0.1704 0.1895 0.1795 0.0183  0.0025  -0.0199 1093 LEU B N   
17180 C CA  . LEU B 1095 ? 0.1822 0.2004 0.1917 0.0203  0.0028  -0.0200 1093 LEU B CA  
17181 C C   . LEU B 1095 ? 0.1593 0.1748 0.1695 0.0200  0.0020  -0.0197 1093 LEU B C   
17182 O O   . LEU B 1095 ? 0.1822 0.1958 0.1924 0.0185  0.0013  -0.0198 1093 LEU B O   
17183 C CB  . LEU B 1095 ? 0.1981 0.2137 0.2057 0.0215  0.0030  -0.0212 1093 LEU B CB  
17184 C CG  . LEU B 1095 ? 0.2219 0.2397 0.2282 0.0217  0.0039  -0.0216 1093 LEU B CG  
17185 C CD1 . LEU B 1095 ? 0.2927 0.3072 0.2964 0.0228  0.0040  -0.0229 1093 LEU B CD1 
17186 C CD2 . LEU B 1095 ? 0.2485 0.2711 0.2562 0.0228  0.0049  -0.0210 1093 LEU B CD2 
17187 N N   . TYR B 1096 ? 0.1678 0.1836 0.1790 0.0214  0.0022  -0.0192 1094 TYR B N   
17188 C CA  . TYR B 1096 ? 0.1616 0.1753 0.1735 0.0211  0.0016  -0.0186 1094 TYR B CA  
17189 C C   . TYR B 1096 ? 0.1584 0.1699 0.1700 0.0231  0.0017  -0.0187 1094 TYR B C   
17190 O O   . TYR B 1096 ? 0.1785 0.1921 0.1905 0.0248  0.0023  -0.0185 1094 TYR B O   
17191 C CB  . TYR B 1096 ? 0.1740 0.1907 0.1873 0.0204  0.0016  -0.0176 1094 TYR B CB  
17192 C CG  . TYR B 1096 ? 0.1655 0.1806 0.1794 0.0203  0.0012  -0.0168 1094 TYR B CG  
17193 C CD1 . TYR B 1096 ? 0.1731 0.1866 0.1872 0.0188  0.0009  -0.0167 1094 TYR B CD1 
17194 C CD2 . TYR B 1096 ? 0.1895 0.2051 0.2039 0.0218  0.0014  -0.0161 1094 TYR B CD2 
17195 C CE1 . TYR B 1096 ? 0.1742 0.1866 0.1888 0.0187  0.0007  -0.0159 1094 TYR B CE1 
17196 C CE2 . TYR B 1096 ? 0.1987 0.2130 0.2135 0.0217  0.0011  -0.0152 1094 TYR B CE2 
17197 C CZ  . TYR B 1096 ? 0.1874 0.2002 0.2022 0.0201  0.0008  -0.0151 1094 TYR B CZ  
17198 O OH  . TYR B 1096 ? 0.1993 0.2110 0.2144 0.0199  0.0007  -0.0142 1094 TYR B OH  
17199 N N   . THR B 1097 ? 0.1759 0.1833 0.1869 0.0229  0.0012  -0.0190 1095 THR B N   
17200 C CA  A THR B 1097 ? 0.1748 0.1791 0.1850 0.0246  0.0012  -0.0193 1095 THR B CA  
17201 C CA  B THR B 1097 ? 0.1756 0.1800 0.1859 0.0246  0.0012  -0.0192 1095 THR B CA  
17202 C C   . THR B 1097 ? 0.1750 0.1763 0.1858 0.0239  0.0005  -0.0185 1095 THR B C   
17203 O O   . THR B 1097 ? 0.2017 0.2025 0.2131 0.0220  0.0000  -0.0183 1095 THR B O   
17204 C CB  A THR B 1097 ? 0.2084 0.2098 0.2167 0.0251  0.0011  -0.0207 1095 THR B CB  
17205 C CB  B THR B 1097 ? 0.2095 0.2112 0.2178 0.0252  0.0011  -0.0207 1095 THR B CB  
17206 O OG1 A THR B 1097 ? 0.2581 0.2572 0.2660 0.0231  0.0002  -0.0211 1095 THR B OG1 
17207 O OG1 B THR B 1097 ? 0.2157 0.2135 0.2229 0.0268  0.0010  -0.0210 1095 THR B OG1 
17208 C CG2 A THR B 1097 ? 0.2023 0.2067 0.2099 0.0256  0.0019  -0.0213 1095 THR B CG2 
17209 C CG2 B THR B 1097 ? 0.2473 0.2470 0.2552 0.0231  0.0004  -0.0211 1095 THR B CG2 
17210 N N   . LEU B 1098 ? 0.1691 0.1684 0.1797 0.0255  0.0005  -0.0181 1096 LEU B N   
17211 C CA  . LEU B 1098 ? 0.1709 0.1671 0.1818 0.0248  0.0000  -0.0173 1096 LEU B CA  
17212 C C   . LEU B 1098 ? 0.1738 0.1649 0.1831 0.0255  -0.0005 -0.0181 1096 LEU B C   
17213 O O   . LEU B 1098 ? 0.1918 0.1815 0.2000 0.0277  -0.0002 -0.0186 1096 LEU B O   
17214 C CB  . LEU B 1098 ? 0.1712 0.1689 0.1830 0.0259  0.0002  -0.0158 1096 LEU B CB  
17215 C CG  . LEU B 1098 ? 0.1673 0.1696 0.1803 0.0250  0.0004  -0.0150 1096 LEU B CG  
17216 C CD1 . LEU B 1098 ? 0.1724 0.1759 0.1860 0.0260  0.0005  -0.0135 1096 LEU B CD1 
17217 C CD2 . LEU B 1098 ? 0.1866 0.1891 0.2002 0.0226  0.0002  -0.0149 1096 LEU B CD2 
17218 N N   . HIS B 1099 ? 0.1769 0.1651 0.1862 0.0237  -0.0012 -0.0182 1097 HIS B N   
17219 C CA  . HIS B 1099 ? 0.1827 0.1656 0.1903 0.0237  -0.0020 -0.0190 1097 HIS B CA  
17220 C C   . HIS B 1099 ? 0.1855 0.1659 0.1940 0.0226  -0.0025 -0.0177 1097 HIS B C   
17221 O O   . HIS B 1099 ? 0.1862 0.1690 0.1963 0.0217  -0.0022 -0.0163 1097 HIS B O   
17222 C CB  . HIS B 1099 ? 0.2074 0.1896 0.2145 0.0219  -0.0026 -0.0201 1097 HIS B CB  
17223 C CG  . HIS B 1099 ? 0.2158 0.2005 0.2220 0.0226  -0.0021 -0.0213 1097 HIS B CG  
17224 N ND1 . HIS B 1099 ? 0.2757 0.2580 0.2795 0.0237  -0.0022 -0.0228 1097 HIS B ND1 
17225 C CD2 . HIS B 1099 ? 0.2727 0.2619 0.2798 0.0223  -0.0015 -0.0211 1097 HIS B CD2 
17226 C CE1 . HIS B 1099 ? 0.2920 0.2775 0.2953 0.0240  -0.0016 -0.0234 1097 HIS B CE1 
17227 N NE2 . HIS B 1099 ? 0.2741 0.2638 0.2796 0.0231  -0.0012 -0.0223 1097 HIS B NE2 
17228 N N   . ALA B 1100 ? 0.2040 0.1791 0.2110 0.0225  -0.0033 -0.0182 1098 ALA B N   
17229 C CA  . ALA B 1100 ? 0.2122 0.1847 0.2200 0.0209  -0.0039 -0.0169 1098 ALA B CA  
17230 C C   . ALA B 1100 ? 0.2161 0.1907 0.2258 0.0183  -0.0042 -0.0165 1098 ALA B C   
17231 O O   . ALA B 1100 ? 0.2339 0.2099 0.2436 0.0175  -0.0044 -0.0176 1098 ALA B O   
17232 C CB  . ALA B 1100 ? 0.2289 0.1951 0.2346 0.0210  -0.0048 -0.0177 1098 ALA B CB  
17233 N N   . ARG B 1101 ? 0.2109 0.1860 0.2222 0.0170  -0.0041 -0.0149 1099 ARG B N   
17234 C CA  . ARG B 1101 ? 0.2290 0.2058 0.2423 0.0145  -0.0044 -0.0144 1099 ARG B CA  
17235 C C   . ARG B 1101 ? 0.2032 0.1763 0.2161 0.0129  -0.0057 -0.0151 1099 ARG B C   
17236 O O   . ARG B 1101 ? 0.2329 0.2077 0.2470 0.0114  -0.0061 -0.0156 1099 ARG B O   
17237 C CB  . ARG B 1101 ? 0.2403 0.2183 0.2552 0.0136  -0.0039 -0.0124 1099 ARG B CB  
17238 C CG  . ARG B 1101 ? 0.2627 0.2455 0.2784 0.0143  -0.0028 -0.0117 1099 ARG B CG  
17239 C CD  . ARG B 1101 ? 0.2721 0.2585 0.2895 0.0129  -0.0025 -0.0119 1099 ARG B CD  
17240 N NE  . ARG B 1101 ? 0.2640 0.2544 0.2819 0.0135  -0.0015 -0.0114 1099 ARG B NE  
17241 C CZ  . ARG B 1101 ? 0.2335 0.2267 0.2529 0.0124  -0.0010 -0.0108 1099 ARG B CZ  
17242 N NH1 . ARG B 1101 ? 0.2313 0.2245 0.2524 0.0107  -0.0012 -0.0106 1099 ARG B NH1 
17243 N NH2 . ARG B 1101 ? 0.2788 0.2750 0.2980 0.0130  -0.0002 -0.0105 1099 ARG B NH2 
17244 N N   . GLY B 1102 ? 0.2096 0.1777 0.2209 0.0130  -0.0063 -0.0152 1100 GLY B N   
17245 C CA  . GLY B 1102 ? 0.2411 0.2054 0.2520 0.0111  -0.0077 -0.0158 1100 GLY B CA  
17246 C C   . GLY B 1102 ? 0.2358 0.1959 0.2466 0.0102  -0.0082 -0.0145 1100 GLY B C   
17247 O O   . GLY B 1102 ? 0.2505 0.2074 0.2594 0.0119  -0.0080 -0.0143 1100 GLY B O   
17248 N N   . ARG B 1103 ? 0.2164 0.1766 0.2291 0.0074  -0.0089 -0.0135 1101 ARG B N   
17249 C CA  . ARG B 1103 ? 0.2386 0.1951 0.2514 0.0061  -0.0093 -0.0120 1101 ARG B CA  
17250 C C   . ARG B 1103 ? 0.2262 0.1865 0.2415 0.0054  -0.0081 -0.0098 1101 ARG B C   
17251 O O   . ARG B 1103 ? 0.2391 0.2041 0.2570 0.0040  -0.0077 -0.0093 1101 ARG B O   
17252 C CB  . ARG B 1103 ? 0.2400 0.1933 0.2532 0.0033  -0.0109 -0.0123 1101 ARG B CB  
17253 C CG  . ARG B 1103 ? 0.2573 0.2060 0.2702 0.0018  -0.0114 -0.0107 1101 ARG B CG  
17254 C CD  . ARG B 1103 ? 0.3141 0.2585 0.3266 -0.0009 -0.0134 -0.0112 1101 ARG B CD  
17255 N NE  . ARG B 1103 ? 0.3910 0.3295 0.3995 0.0005  -0.0144 -0.0134 1101 ARG B NE  
17256 C CZ  . ARG B 1103 ? 0.4891 0.4269 0.4964 0.0002  -0.0155 -0.0154 1101 ARG B CZ  
17257 N NH1 . ARG B 1103 ? 0.5640 0.5066 0.5739 -0.0014 -0.0159 -0.0155 1101 ARG B NH1 
17258 N NH2 . ARG B 1103 ? 0.5171 0.4492 0.5204 0.0017  -0.0163 -0.0173 1101 ARG B NH2 
17259 N N   . ILE B 1104 ? 0.2068 0.1651 0.2211 0.0063  -0.0076 -0.0084 1102 ILE B N   
17260 C CA  . ILE B 1104 ? 0.2035 0.1653 0.2194 0.0059  -0.0063 -0.0063 1102 ILE B CA  
17261 C C   . ILE B 1104 ? 0.2168 0.1758 0.2336 0.0034  -0.0068 -0.0045 1102 ILE B C   
17262 O O   . ILE B 1104 ? 0.2205 0.1736 0.2353 0.0032  -0.0078 -0.0044 1102 ILE B O   
17263 C CB  . ILE B 1104 ? 0.2034 0.1653 0.2177 0.0086  -0.0055 -0.0058 1102 ILE B CB  
17264 C CG1 . ILE B 1104 ? 0.2076 0.1720 0.2210 0.0110  -0.0051 -0.0076 1102 ILE B CG1 
17265 C CG2 . ILE B 1104 ? 0.2136 0.1791 0.2292 0.0082  -0.0043 -0.0037 1102 ILE B CG2 
17266 C CD1 . ILE B 1104 ? 0.2251 0.1954 0.2406 0.0105  -0.0044 -0.0081 1102 ILE B CD1 
17267 N N   . LEU B 1105 ? 0.2056 0.1687 0.2251 0.0015  -0.0061 -0.0031 1103 LEU B N   
17268 C CA  . LEU B 1105 ? 0.2151 0.1765 0.2356 -0.0010 -0.0062 -0.0010 1103 LEU B CA  
17269 C C   . LEU B 1105 ? 0.2121 0.1723 0.2311 0.0001  -0.0053 0.0009  1103 LEU B C   
17270 O O   . LEU B 1105 ? 0.2027 0.1670 0.2219 0.0015  -0.0039 0.0014  1103 LEU B O   
17271 C CB  . LEU B 1105 ? 0.2188 0.1857 0.2429 -0.0032 -0.0055 -0.0001 1103 LEU B CB  
17272 C CG  . LEU B 1105 ? 0.2177 0.1843 0.2435 -0.0060 -0.0052 0.0024  1103 LEU B CG  
17273 C CD1 . LEU B 1105 ? 0.2184 0.1795 0.2438 -0.0083 -0.0071 0.0024  1103 LEU B CD1 
17274 C CD2 . LEU B 1105 ? 0.2345 0.2077 0.2640 -0.0074 -0.0041 0.0031  1103 LEU B CD2 
17275 N N   . LEU B 1106 ? 0.2087 0.1632 0.2260 -0.0005 -0.0060 0.0019  1104 LEU B N   
17276 C CA  . LEU B 1106 ? 0.2185 0.1711 0.2341 0.0005  -0.0054 0.0040  1104 LEU B CA  
17277 C C   . LEU B 1106 ? 0.2152 0.1675 0.2322 -0.0026 -0.0051 0.0065  1104 LEU B C   
17278 O O   . LEU B 1106 ? 0.2292 0.1781 0.2468 -0.0051 -0.0063 0.0067  1104 LEU B O   
17279 C CB  . LEU B 1106 ? 0.2241 0.1697 0.2364 0.0024  -0.0065 0.0034  1104 LEU B CB  
17280 C CG  . LEU B 1106 ? 0.2932 0.2396 0.3037 0.0062  -0.0061 0.0021  1104 LEU B CG  
17281 C CD1 . LEU B 1106 ? 0.3036 0.2551 0.3154 0.0071  -0.0057 0.0000  1104 LEU B CD1 
17282 C CD2 . LEU B 1106 ? 0.2415 0.1808 0.2491 0.0080  -0.0073 0.0013  1104 LEU B CD2 
17283 N N   . VAL B 1107 ? 0.2205 0.1766 0.2380 -0.0026 -0.0036 0.0084  1105 VAL B N   
17284 C CA  . VAL B 1107 ? 0.2197 0.1761 0.2385 -0.0054 -0.0030 0.0110  1105 VAL B CA  
17285 C C   . VAL B 1107 ? 0.2216 0.1755 0.2377 -0.0041 -0.0026 0.0131  1105 VAL B C   
17286 O O   . VAL B 1107 ? 0.2375 0.1956 0.2536 -0.0034 -0.0011 0.0143  1105 VAL B O   
17287 C CB  . VAL B 1107 ? 0.2124 0.1761 0.2344 -0.0067 -0.0015 0.0115  1105 VAL B CB  
17288 C CG1 . VAL B 1107 ? 0.2332 0.1974 0.2568 -0.0099 -0.0009 0.0142  1105 VAL B CG1 
17289 C CG2 . VAL B 1107 ? 0.2201 0.1866 0.2445 -0.0072 -0.0021 0.0092  1105 VAL B CG2 
17290 N N   . PRO B 1108 ? 0.2256 0.1725 0.2392 -0.0037 -0.0038 0.0136  1106 PRO B N   
17291 C CA  . PRO B 1108 ? 0.2463 0.1905 0.2573 -0.0023 -0.0035 0.0157  1106 PRO B CA  
17292 C C   . PRO B 1108 ? 0.2366 0.1801 0.2480 -0.0053 -0.0029 0.0188  1106 PRO B C   
17293 O O   . PRO B 1108 ? 0.2892 0.2330 0.3028 -0.0086 -0.0031 0.0193  1106 PRO B O   
17294 C CB  . PRO B 1108 ? 0.2461 0.1825 0.2544 -0.0008 -0.0052 0.0147  1106 PRO B CB  
17295 C CG  . PRO B 1108 ? 0.2472 0.1810 0.2569 -0.0034 -0.0064 0.0135  1106 PRO B CG  
17296 C CD  . PRO B 1108 ? 0.2472 0.1881 0.2599 -0.0041 -0.0056 0.0120  1106 PRO B CD  
17297 N N   . ALA B 1109 ? 0.2530 0.1957 0.2623 -0.0042 -0.0024 0.0209  1107 ALA B N   
17298 C CA  . ALA B 1109 ? 0.2808 0.2214 0.2894 -0.0067 -0.0019 0.0242  1107 ALA B CA  
17299 C C   . ALA B 1109 ? 0.3201 0.2527 0.3254 -0.0058 -0.0032 0.0256  1107 ALA B C   
17300 O O   . ALA B 1109 ? 0.3248 0.2528 0.3296 -0.0085 -0.0038 0.0276  1107 ALA B O   
17301 C CB  . ALA B 1109 ? 0.2746 0.2211 0.2832 -0.0064 -0.0001 0.0260  1107 ALA B CB  
17302 N N   . THR B 1110 ? 0.2766 0.2072 0.2796 -0.0021 -0.0038 0.0246  1108 THR B N   
17303 C CA  . THR B 1110 ? 0.2769 0.2001 0.2766 -0.0005 -0.0050 0.0259  1108 THR B CA  
17304 C C   . THR B 1110 ? 0.2907 0.2096 0.2893 0.0023  -0.0064 0.0231  1108 THR B C   
17305 O O   . THR B 1110 ? 0.2737 0.1964 0.2737 0.0037  -0.0062 0.0204  1108 THR B O   
17306 C CB  . THR B 1110 ? 0.3160 0.2409 0.3137 0.0019  -0.0043 0.0279  1108 THR B CB  
17307 O OG1 . THR B 1110 ? 0.3046 0.2345 0.3027 0.0051  -0.0040 0.0257  1108 THR B OG1 
17308 C CG2 . THR B 1110 ? 0.3472 0.2766 0.3455 -0.0007 -0.0028 0.0306  1108 THR B CG2 
17309 N N   . GLU B 1111 ? 0.3129 0.2237 0.3088 0.0032  -0.0077 0.0239  1109 GLU B N   
17310 C CA  . GLU B 1111 ? 0.3116 0.2176 0.3059 0.0062  -0.0089 0.0214  1109 GLU B CA  
17311 C C   . GLU B 1111 ? 0.3274 0.2382 0.3217 0.0103  -0.0083 0.0200  1109 GLU B C   
17312 O O   . GLU B 1111 ? 0.2942 0.2066 0.2893 0.0119  -0.0085 0.0170  1109 GLU B O   
17313 C CB  . GLU B 1111 ? 0.3248 0.2213 0.3158 0.0069  -0.0102 0.0229  1109 GLU B CB  
17314 C CG  . GLU B 1111 ? 0.3522 0.2438 0.3412 0.0107  -0.0112 0.0205  1109 GLU B CG  
17315 C CD  . GLU B 1111 ? 0.3721 0.2535 0.3577 0.0113  -0.0126 0.0218  1109 GLU B CD  
17316 O OE1 . GLU B 1111 ? 0.4031 0.2785 0.3880 0.0086  -0.0137 0.0214  1109 GLU B OE1 
17317 O OE2 . GLU B 1111 ? 0.4237 0.3030 0.4074 0.0144  -0.0128 0.0232  1109 GLU B OE2 
17318 N N   . SER B 1112 ? 0.3205 0.2337 0.3139 0.0119  -0.0078 0.0221  1110 SER B N   
17319 C CA  . SER B 1112 ? 0.2950 0.2131 0.2885 0.0156  -0.0074 0.0209  1110 SER B CA  
17320 C C   . SER B 1112 ? 0.2988 0.2248 0.2951 0.0149  -0.0063 0.0188  1110 SER B C   
17321 O O   . SER B 1112 ? 0.2928 0.2215 0.2897 0.0173  -0.0063 0.0164  1110 SER B O   
17322 C CB  . SER B 1112 ? 0.3399 0.2598 0.3321 0.0169  -0.0070 0.0237  1110 SER B CB  
17323 O OG  . SER B 1112 ? 0.3347 0.2595 0.3272 0.0203  -0.0068 0.0225  1110 SER B OG  
17324 N N   . GLY B 1113 ? 0.2868 0.2167 0.2848 0.0116  -0.0054 0.0197  1111 GLY B N   
17325 C CA  . GLY B 1113 ? 0.2563 0.1932 0.2569 0.0108  -0.0044 0.0178  1111 GLY B CA  
17326 C C   . GLY B 1113 ? 0.2675 0.2031 0.2692 0.0109  -0.0051 0.0148  1111 GLY B C   
17327 O O   . GLY B 1113 ? 0.2550 0.1949 0.2578 0.0124  -0.0047 0.0126  1111 GLY B O   
17328 N N   . LEU B 1114 ? 0.2519 0.1815 0.2531 0.0091  -0.0060 0.0147  1112 LEU B N   
17329 C CA  . LEU B 1114 ? 0.2411 0.1688 0.2428 0.0091  -0.0069 0.0118  1112 LEU B CA  
17330 C C   . LEU B 1114 ? 0.2511 0.1772 0.2511 0.0131  -0.0073 0.0099  1112 LEU B C   
17331 O O   . LEU B 1114 ? 0.2386 0.1674 0.2395 0.0141  -0.0072 0.0073  1112 LEU B O   
17332 C CB  . LEU B 1114 ? 0.2770 0.1977 0.2779 0.0065  -0.0081 0.0123  1112 LEU B CB  
17333 C CG  . LEU B 1114 ? 0.2839 0.2008 0.2843 0.0067  -0.0092 0.0094  1112 LEU B CG  
17334 C CD1 . LEU B 1114 ? 0.2658 0.1889 0.2689 0.0055  -0.0088 0.0074  1112 LEU B CD1 
17335 C CD2 . LEU B 1114 ? 0.3155 0.2248 0.3147 0.0039  -0.0106 0.0100  1112 LEU B CD2 
17336 N N   . TYR B 1115 ? 0.2712 0.1931 0.2689 0.0156  -0.0077 0.0111  1113 TYR B N   
17337 C CA  . TYR B 1115 ? 0.2693 0.1902 0.2658 0.0196  -0.0080 0.0093  1113 TYR B CA  
17338 C C   . TYR B 1115 ? 0.2639 0.1929 0.2620 0.0214  -0.0070 0.0084  1113 TYR B C   
17339 O O   . TYR B 1115 ? 0.2642 0.1948 0.2626 0.0234  -0.0070 0.0060  1113 TYR B O   
17340 C CB  . TYR B 1115 ? 0.2728 0.1883 0.2668 0.0221  -0.0087 0.0111  1113 TYR B CB  
17341 C CG  . TYR B 1115 ? 0.2740 0.1801 0.2657 0.0211  -0.0099 0.0117  1113 TYR B CG  
17342 C CD1 . TYR B 1115 ? 0.2904 0.1930 0.2821 0.0185  -0.0105 0.0100  1113 TYR B CD1 
17343 C CD2 . TYR B 1115 ? 0.3445 0.2452 0.3339 0.0226  -0.0105 0.0139  1113 TYR B CD2 
17344 C CE1 . TYR B 1115 ? 0.3374 0.2310 0.3268 0.0174  -0.0118 0.0106  1113 TYR B CE1 
17345 C CE2 . TYR B 1115 ? 0.3492 0.2408 0.3363 0.0216  -0.0116 0.0144  1113 TYR B CE2 
17346 C CZ  . TYR B 1115 ? 0.3809 0.2689 0.3679 0.0189  -0.0123 0.0127  1113 TYR B CZ  
17347 O OH  . TYR B 1115 ? 0.4352 0.3138 0.4197 0.0176  -0.0136 0.0133  1113 TYR B OH  
17348 N N   . HIS B 1116 ? 0.2412 0.1754 0.2404 0.0205  -0.0062 0.0102  1114 HIS B N   
17349 C CA  . HIS B 1116 ? 0.2467 0.1884 0.2473 0.0218  -0.0053 0.0093  1114 HIS B CA  
17350 C C   . HIS B 1116 ? 0.2523 0.1980 0.2550 0.0201  -0.0049 0.0071  1114 HIS B C   
17351 O O   . HIS B 1116 ? 0.2479 0.1974 0.2514 0.0218  -0.0046 0.0052  1114 HIS B O   
17352 C CB  . HIS B 1116 ? 0.2316 0.1775 0.2324 0.0211  -0.0046 0.0117  1114 HIS B CB  
17353 C CG  . HIS B 1116 ? 0.2899 0.2343 0.2889 0.0237  -0.0050 0.0136  1114 HIS B CG  
17354 N ND1 . HIS B 1116 ? 0.3212 0.2597 0.3183 0.0234  -0.0057 0.0159  1114 HIS B ND1 
17355 C CD2 . HIS B 1116 ? 0.2884 0.2366 0.2873 0.0265  -0.0050 0.0137  1114 HIS B CD2 
17356 C CE1 . HIS B 1116 ? 0.3378 0.2764 0.3335 0.0262  -0.0060 0.0173  1114 HIS B CE1 
17357 N NE2 . HIS B 1116 ? 0.3355 0.2801 0.3324 0.0281  -0.0057 0.0160  1114 HIS B NE2 
17358 N N   . GLN B 1117 ? 0.2258 0.1708 0.2296 0.0168  -0.0048 0.0073  1115 GLN B N   
17359 C CA  . GLN B 1117 ? 0.2225 0.1709 0.2282 0.0153  -0.0045 0.0053  1115 GLN B CA  
17360 C C   . GLN B 1117 ? 0.2249 0.1702 0.2299 0.0167  -0.0053 0.0027  1115 GLN B C   
17361 O O   . GLN B 1117 ? 0.2203 0.1693 0.2262 0.0173  -0.0050 0.0007  1115 GLN B O   
17362 C CB  . GLN B 1117 ? 0.2262 0.1741 0.2333 0.0115  -0.0045 0.0062  1115 GLN B CB  
17363 C CG  . GLN B 1117 ? 0.2161 0.1680 0.2242 0.0100  -0.0034 0.0085  1115 GLN B CG  
17364 C CD  . GLN B 1117 ? 0.2221 0.1737 0.2319 0.0063  -0.0032 0.0095  1115 GLN B CD  
17365 O OE1 . GLN B 1117 ? 0.2510 0.1984 0.2609 0.0048  -0.0043 0.0089  1115 GLN B OE1 
17366 N NE2 . GLN B 1117 ? 0.2447 0.2009 0.2558 0.0048  -0.0020 0.0110  1115 GLN B NE2 
17367 N N   . LEU B 1118 ? 0.2308 0.1691 0.2338 0.0171  -0.0063 0.0027  1116 LEU B N   
17368 C CA  . LEU B 1118 ? 0.2460 0.1809 0.2477 0.0187  -0.0070 0.0002  1116 LEU B CA  
17369 C C   . LEU B 1118 ? 0.2382 0.1760 0.2395 0.0224  -0.0065 -0.0010 1116 LEU B C   
17370 O O   . LEU B 1118 ? 0.2476 0.1872 0.2491 0.0232  -0.0064 -0.0033 1116 LEU B O   
17371 C CB  . LEU B 1118 ? 0.2717 0.1979 0.2709 0.0189  -0.0082 0.0005  1116 LEU B CB  
17372 C CG  . LEU B 1118 ? 0.3271 0.2497 0.3266 0.0150  -0.0090 0.0009  1116 LEU B CG  
17373 C CD1 . LEU B 1118 ? 0.3189 0.2328 0.3157 0.0152  -0.0101 0.0018  1116 LEU B CD1 
17374 C CD2 . LEU B 1118 ? 0.3056 0.2286 0.3055 0.0140  -0.0095 -0.0018 1116 LEU B CD2 
17375 N N   . ALA B 1119 ? 0.2534 0.1920 0.2542 0.0245  -0.0062 0.0007  1117 ALA B N   
17376 C CA  . ALA B 1119 ? 0.2518 0.1937 0.2525 0.0280  -0.0058 -0.0003 1117 ALA B CA  
17377 C C   . ALA B 1119 ? 0.2405 0.1898 0.2433 0.0274  -0.0050 -0.0015 1117 ALA B C   
17378 O O   . ALA B 1119 ? 0.2403 0.1914 0.2432 0.0291  -0.0047 -0.0035 1117 ALA B O   
17379 C CB  . ALA B 1119 ? 0.2616 0.2041 0.2618 0.0300  -0.0057 0.0021  1117 ALA B CB  
17380 N N   . ALA B 1120 ? 0.2078 0.1612 0.2122 0.0250  -0.0045 -0.0003 1118 ALA B N   
17381 C CA  . ALA B 1120 ? 0.1967 0.1567 0.2028 0.0245  -0.0037 -0.0013 1118 ALA B CA  
17382 C C   . ALA B 1120 ? 0.2266 0.1865 0.2333 0.0234  -0.0039 -0.0036 1118 ALA B C   
17383 O O   . ALA B 1120 ? 0.2214 0.1847 0.2286 0.0245  -0.0035 -0.0052 1118 ALA B O   
17384 C CB  . ALA B 1120 ? 0.2208 0.1844 0.2281 0.0221  -0.0031 0.0004  1118 ALA B CB  
17385 N N   . ALA B 1121 ? 0.1956 0.1514 0.2021 0.0211  -0.0045 -0.0037 1119 ALA B N   
17386 C CA  . ALA B 1121 ? 0.2091 0.1647 0.2160 0.0199  -0.0048 -0.0058 1119 ALA B CA  
17387 C C   . ALA B 1121 ? 0.1947 0.1472 0.1997 0.0222  -0.0052 -0.0078 1119 ALA B C   
17388 O O   . ALA B 1121 ? 0.2055 0.1605 0.2108 0.0225  -0.0050 -0.0097 1119 ALA B O   
17389 C CB  . ALA B 1121 ? 0.2263 0.1785 0.2336 0.0168  -0.0055 -0.0052 1119 ALA B CB  
17390 N N   . LEU B 1122 ? 0.2159 0.1629 0.2189 0.0239  -0.0057 -0.0075 1120 LEU B N   
17391 C CA  . LEU B 1122 ? 0.2155 0.1593 0.2164 0.0265  -0.0059 -0.0096 1120 LEU B CA  
17392 C C   . LEU B 1122 ? 0.2171 0.1661 0.2186 0.0293  -0.0050 -0.0103 1120 LEU B C   
17393 O O   . LEU B 1122 ? 0.2179 0.1675 0.2186 0.0305  -0.0048 -0.0123 1120 LEU B O   
17394 C CB  . LEU B 1122 ? 0.2209 0.1574 0.2194 0.0279  -0.0066 -0.0091 1120 LEU B CB  
17395 C CG  . LEU B 1122 ? 0.2664 0.1969 0.2640 0.0250  -0.0078 -0.0086 1120 LEU B CG  
17396 C CD1 . LEU B 1122 ? 0.2771 0.2004 0.2723 0.0265  -0.0084 -0.0077 1120 LEU B CD1 
17397 C CD2 . LEU B 1122 ? 0.2792 0.2076 0.2760 0.0234  -0.0085 -0.0109 1120 LEU B CD2 
17398 N N   . ALA B 1123 ? 0.2018 0.1546 0.2044 0.0303  -0.0044 -0.0086 1121 ALA B N   
17399 C CA  . ALA B 1123 ? 0.2239 0.1818 0.2272 0.0329  -0.0037 -0.0090 1121 ALA B CA  
17400 C C   . ALA B 1123 ? 0.2215 0.1848 0.2262 0.0317  -0.0031 -0.0103 1121 ALA B C   
17401 O O   . ALA B 1123 ? 0.2085 0.1753 0.2135 0.0336  -0.0025 -0.0114 1121 ALA B O   
17402 C CB  . ALA B 1123 ? 0.2174 0.1787 0.2218 0.0336  -0.0034 -0.0067 1121 ALA B CB  
17403 N N   . THR B 1124 ? 0.2001 0.1644 0.2058 0.0286  -0.0033 -0.0102 1122 THR B N   
17404 C CA  . THR B 1124 ? 0.1735 0.1424 0.1804 0.0273  -0.0029 -0.0114 1122 THR B CA  
17405 C C   . THR B 1124 ? 0.1812 0.1470 0.1871 0.0263  -0.0034 -0.0133 1122 THR B C   
17406 O O   . THR B 1124 ? 0.2022 0.1709 0.2090 0.0247  -0.0033 -0.0141 1122 THR B O   
17407 C CB  . THR B 1124 ? 0.1880 0.1604 0.1967 0.0249  -0.0027 -0.0101 1122 THR B CB  
17408 O OG1 . THR B 1124 ? 0.2033 0.1721 0.2120 0.0230  -0.0032 -0.0088 1122 THR B OG1 
17409 C CG2 . THR B 1124 ? 0.1848 0.1615 0.1943 0.0261  -0.0021 -0.0087 1122 THR B CG2 
17410 N N   . GLY B 1125 ? 0.1965 0.1564 0.2003 0.0272  -0.0040 -0.0141 1123 GLY B N   
17411 C CA  . GLY B 1125 ? 0.1943 0.1511 0.1965 0.0268  -0.0046 -0.0161 1123 GLY B CA  
17412 C C   . GLY B 1125 ? 0.2026 0.1567 0.2050 0.0235  -0.0056 -0.0161 1123 GLY B C   
17413 O O   . GLY B 1125 ? 0.2090 0.1610 0.2102 0.0227  -0.0062 -0.0178 1123 GLY B O   
17414 N N   . ASN B 1126 ? 0.2073 0.1615 0.2113 0.0216  -0.0058 -0.0142 1124 ASN B N   
17415 C CA  . ASN B 1126 ? 0.1967 0.1498 0.2017 0.0184  -0.0066 -0.0139 1124 ASN B CA  
17416 C C   . ASN B 1126 ? 0.2136 0.1596 0.2168 0.0175  -0.0078 -0.0139 1124 ASN B C   
17417 O O   . ASN B 1126 ? 0.2344 0.1762 0.2358 0.0193  -0.0079 -0.0135 1124 ASN B O   
17418 C CB  . ASN B 1126 ? 0.1952 0.1522 0.2028 0.0167  -0.0061 -0.0118 1124 ASN B CB  
17419 C CG  . ASN B 1126 ? 0.1940 0.1575 0.2031 0.0173  -0.0050 -0.0119 1124 ASN B CG  
17420 O OD1 . ASN B 1126 ? 0.2052 0.1714 0.2152 0.0164  -0.0051 -0.0130 1124 ASN B OD1 
17421 N ND2 . ASN B 1126 ? 0.2023 0.1684 0.2118 0.0187  -0.0042 -0.0107 1124 ASN B ND2 
17422 N N   . SER B 1127 ? 0.2113 0.1559 0.2150 0.0147  -0.0088 -0.0143 1125 SER B N   
17423 C CA  . SER B 1127 ? 0.2271 0.1658 0.2299 0.0128  -0.0100 -0.0137 1125 SER B CA  
17424 C C   . SER B 1127 ? 0.2205 0.1619 0.2263 0.0103  -0.0097 -0.0112 1125 SER B C   
17425 O O   . SER B 1127 ? 0.2205 0.1680 0.2286 0.0102  -0.0087 -0.0104 1125 SER B O   
17426 C CB  . SER B 1127 ? 0.2461 0.1821 0.2481 0.0108  -0.0115 -0.0154 1125 SER B CB  
17427 O OG  . SER B 1127 ? 0.2923 0.2337 0.2970 0.0088  -0.0115 -0.0154 1125 SER B OG  
17428 N N   . VAL B 1128 ? 0.2367 0.1733 0.2420 0.0084  -0.0106 -0.0100 1126 VAL B N   
17429 C CA  . VAL B 1128 ? 0.2341 0.1729 0.2419 0.0062  -0.0102 -0.0075 1126 VAL B CA  
17430 C C   . VAL B 1128 ? 0.2417 0.1776 0.2504 0.0026  -0.0115 -0.0070 1126 VAL B C   
17431 O O   . VAL B 1128 ? 0.2680 0.1979 0.2745 0.0020  -0.0129 -0.0082 1126 VAL B O   
17432 C CB  . VAL B 1128 ? 0.2378 0.1747 0.2446 0.0076  -0.0095 -0.0055 1126 VAL B CB  
17433 C CG1 . VAL B 1128 ? 0.2315 0.1722 0.2379 0.0110  -0.0083 -0.0058 1126 VAL B CG1 
17434 C CG2 . VAL B 1128 ? 0.2589 0.1874 0.2627 0.0080  -0.0107 -0.0056 1126 VAL B CG2 
17435 N N   . ALA B 1129 ? 0.2272 0.1673 0.2390 0.0001  -0.0110 -0.0052 1127 ALA B N   
17436 C CA  . ALA B 1129 ? 0.2417 0.1796 0.2549 -0.0035 -0.0120 -0.0038 1127 ALA B CA  
17437 C C   . ALA B 1129 ? 0.2203 0.1590 0.2344 -0.0041 -0.0109 -0.0010 1127 ALA B C   
17438 O O   . ALA B 1129 ? 0.2318 0.1766 0.2479 -0.0037 -0.0094 0.0001  1127 ALA B O   
17439 C CB  . ALA B 1129 ? 0.2540 0.1970 0.2705 -0.0060 -0.0123 -0.0041 1127 ALA B CB  
17440 N N   . ILE B 1130 ? 0.2226 0.1551 0.2349 -0.0051 -0.0117 0.0002  1128 ILE B N   
17441 C CA  . ILE B 1130 ? 0.2315 0.1639 0.2441 -0.0057 -0.0107 0.0031  1128 ILE B CA  
17442 C C   . ILE B 1130 ? 0.2392 0.1729 0.2546 -0.0098 -0.0109 0.0050  1128 ILE B C   
17443 O O   . ILE B 1130 ? 0.2422 0.1720 0.2576 -0.0124 -0.0126 0.0046  1128 ILE B O   
17444 C CB  . ILE B 1130 ? 0.2387 0.1634 0.2476 -0.0041 -0.0113 0.0037  1128 ILE B CB  
17445 C CG1 . ILE B 1130 ? 0.2662 0.1896 0.2725 0.0001  -0.0113 0.0015  1128 ILE B CG1 
17446 C CG2 . ILE B 1130 ? 0.2456 0.1712 0.2546 -0.0043 -0.0102 0.0067  1128 ILE B CG2 
17447 C CD1 . ILE B 1130 ? 0.2579 0.1729 0.2605 0.0018  -0.0122 0.0015  1128 ILE B CD1 
17448 N N   . ASP B 1131 ? 0.2309 0.1700 0.2486 -0.0106 -0.0093 0.0072  1129 ASP B N   
17449 C CA  . ASP B 1131 ? 0.2392 0.1804 0.2598 -0.0144 -0.0092 0.0093  1129 ASP B CA  
17450 C C   . ASP B 1131 ? 0.2485 0.1822 0.2673 -0.0167 -0.0104 0.0109  1129 ASP B C   
17451 O O   . ASP B 1131 ? 0.2558 0.1859 0.2722 -0.0156 -0.0100 0.0125  1129 ASP B O   
17452 C CB  . ASP B 1131 ? 0.2331 0.1804 0.2554 -0.0142 -0.0070 0.0114  1129 ASP B CB  
17453 C CG  . ASP B 1131 ? 0.2557 0.2057 0.2810 -0.0179 -0.0064 0.0138  1129 ASP B CG  
17454 O OD1 . ASP B 1131 ? 0.2633 0.2134 0.2909 -0.0206 -0.0076 0.0134  1129 ASP B OD1 
17455 O OD2 . ASP B 1131 ? 0.2675 0.2196 0.2930 -0.0182 -0.0049 0.0162  1129 ASP B OD2 
17456 N N   . ALA B 1132 ? 0.2586 0.1900 0.2786 -0.0198 -0.0120 0.0105  1130 ALA B N   
17457 C CA  . ALA B 1132 ? 0.2606 0.1846 0.2789 -0.0224 -0.0134 0.0120  1130 ALA B CA  
17458 C C   . ALA B 1132 ? 0.2874 0.2130 0.3072 -0.0247 -0.0122 0.0155  1130 ALA B C   
17459 O O   . ALA B 1132 ? 0.2959 0.2150 0.3132 -0.0256 -0.0128 0.0172  1130 ALA B O   
17460 C CB  . ALA B 1132 ? 0.2712 0.1930 0.2907 -0.0256 -0.0155 0.0108  1130 ALA B CB  
17461 N N   . ALA B 1133 ? 0.2614 0.1955 0.2849 -0.0255 -0.0104 0.0168  1131 ALA B N   
17462 C CA  . ALA B 1133 ? 0.3149 0.2510 0.3397 -0.0277 -0.0090 0.0202  1131 ALA B CA  
17463 C C   . ALA B 1133 ? 0.3152 0.2488 0.3366 -0.0251 -0.0079 0.0217  1131 ALA B C   
17464 O O   . ALA B 1133 ? 0.3171 0.2508 0.3385 -0.0269 -0.0069 0.0247  1131 ALA B O   
17465 C CB  . ALA B 1133 ? 0.2976 0.2434 0.3270 -0.0288 -0.0072 0.0210  1131 ALA B CB  
17466 N N   . SER B 1134 ? 0.2771 0.2087 0.2956 -0.0211 -0.0080 0.0197  1132 SER B N   
17467 C CA  . SER B 1134 ? 0.2811 0.2099 0.2963 -0.0185 -0.0073 0.0211  1132 SER B CA  
17468 C C   . SER B 1134 ? 0.2852 0.2049 0.2973 -0.0198 -0.0087 0.0227  1132 SER B C   
17469 O O   . SER B 1134 ? 0.3069 0.2245 0.3169 -0.0188 -0.0081 0.0250  1132 SER B O   
17470 C CB  . SER B 1134 ? 0.2707 0.1993 0.2837 -0.0140 -0.0074 0.0185  1132 SER B CB  
17471 O OG  . SER B 1134 ? 0.2880 0.2100 0.2989 -0.0132 -0.0093 0.0163  1132 SER B OG  
17472 N N   . GLY B 1135 ? 0.2847 0.1987 0.2965 -0.0218 -0.0107 0.0217  1133 GLY B N   
17473 C CA  . GLY B 1135 ? 0.3048 0.2094 0.3135 -0.0230 -0.0121 0.0231  1133 GLY B CA  
17474 C C   . GLY B 1135 ? 0.3374 0.2354 0.3416 -0.0189 -0.0128 0.0220  1133 GLY B C   
17475 O O   . GLY B 1135 ? 0.3671 0.2574 0.3684 -0.0192 -0.0137 0.0236  1133 GLY B O   
17476 N N   . LEU B 1136 ? 0.3160 0.2167 0.3197 -0.0150 -0.0124 0.0194  1134 LEU B N   
17477 C CA  . LEU B 1136 ? 0.3216 0.2177 0.3217 -0.0106 -0.0127 0.0185  1134 LEU B CA  
17478 C C   . LEU B 1136 ? 0.3613 0.2505 0.3589 -0.0092 -0.0145 0.0156  1134 LEU B C   
17479 O O   . LEU B 1136 ? 0.3415 0.2285 0.3367 -0.0050 -0.0145 0.0141  1134 LEU B O   
17480 C CB  . LEU B 1136 ? 0.2908 0.1944 0.2918 -0.0071 -0.0111 0.0178  1134 LEU B CB  
17481 C CG  . LEU B 1136 ? 0.3071 0.2167 0.3095 -0.0078 -0.0093 0.0206  1134 LEU B CG  
17482 C CD1 . LEU B 1136 ? 0.3286 0.2456 0.3320 -0.0047 -0.0080 0.0193  1134 LEU B CD1 
17483 C CD2 . LEU B 1136 ? 0.3360 0.2401 0.3355 -0.0073 -0.0095 0.0235  1134 LEU B CD2 
17484 N N   . GLN B 1137 ? 0.3265 0.2125 0.3247 -0.0125 -0.0159 0.0147  1135 GLN B N   
17485 C CA  . GLN B 1137 ? 0.3400 0.2197 0.3356 -0.0113 -0.0176 0.0115  1135 GLN B CA  
17486 C C   . GLN B 1137 ? 0.3999 0.2702 0.3909 -0.0084 -0.0184 0.0115  1135 GLN B C   
17487 O O   . GLN B 1137 ? 0.3985 0.2658 0.3870 -0.0050 -0.0189 0.0087  1135 GLN B O   
17488 C CB  . GLN B 1137 ? 0.3679 0.2449 0.3645 -0.0160 -0.0193 0.0111  1135 GLN B CB  
17489 C CG  . GLN B 1137 ? 0.3613 0.2471 0.3623 -0.0181 -0.0188 0.0102  1135 GLN B CG  
17490 C CD  . GLN B 1137 ? 0.3363 0.2291 0.3414 -0.0213 -0.0175 0.0133  1135 GLN B CD  
17491 O OE1 . GLN B 1137 ? 0.3573 0.2495 0.3619 -0.0213 -0.0165 0.0161  1135 GLN B OE1 
17492 N NE2 . GLN B 1137 ? 0.3656 0.2649 0.3746 -0.0237 -0.0174 0.0128  1135 GLN B NE2 
17493 N N   . ALA B 1138 ? 0.3540 0.2196 0.3436 -0.0096 -0.0186 0.0145  1136 ALA B N   
17494 C CA  . ALA B 1138 ? 0.4117 0.2678 0.3968 -0.0068 -0.0195 0.0147  1136 ALA B CA  
17495 C C   . ALA B 1138 ? 0.4275 0.2862 0.4116 -0.0013 -0.0184 0.0140  1136 ALA B C   
17496 O O   . ALA B 1138 ? 0.4515 0.3032 0.4321 0.0021  -0.0191 0.0131  1136 ALA B O   
17497 C CB  . ALA B 1138 ? 0.4034 0.2544 0.3875 -0.0094 -0.0199 0.0184  1136 ALA B CB  
17498 N N   . SER B 1139 ? 0.3869 0.2554 0.3739 -0.0003 -0.0166 0.0144  1137 SER B N   
17499 C CA  . SER B 1139 ? 0.3861 0.2579 0.3725 0.0046  -0.0156 0.0139  1137 SER B CA  
17500 C C   . SER B 1139 ? 0.4095 0.2808 0.3949 0.0080  -0.0159 0.0102  1137 SER B C   
17501 O O   . SER B 1139 ? 0.3829 0.2547 0.3671 0.0124  -0.0154 0.0096  1137 SER B O   
17502 C CB  . SER B 1139 ? 0.3626 0.2449 0.3524 0.0042  -0.0138 0.0151  1137 SER B CB  
17503 O OG  . SER B 1139 ? 0.4059 0.2886 0.3960 0.0020  -0.0133 0.0188  1137 SER B OG  
17504 N N   . LEU B 1140 ? 0.3831 0.2537 0.3689 0.0061  -0.0166 0.0077  1138 LEU B N   
17505 C CA  . LEU B 1140 ? 0.4053 0.2751 0.3898 0.0090  -0.0169 0.0041  1138 LEU B CA  
17506 C C   . LEU B 1140 ? 0.4669 0.3260 0.4474 0.0092  -0.0186 0.0025  1138 LEU B C   
17507 O O   . LEU B 1140 ? 0.4730 0.3308 0.4523 0.0101  -0.0191 -0.0007 1138 LEU B O   
17508 C CB  . LEU B 1140 ? 0.3934 0.2708 0.3808 0.0074  -0.0164 0.0022  1138 LEU B CB  
17509 C CG  . LEU B 1140 ? 0.3805 0.2682 0.3713 0.0079  -0.0147 0.0033  1138 LEU B CG  
17510 C CD1 . LEU B 1140 ? 0.3662 0.2605 0.3594 0.0071  -0.0143 0.0010  1138 LEU B CD1 
17511 C CD2 . LEU B 1140 ? 0.4340 0.3234 0.4239 0.0125  -0.0137 0.0036  1138 LEU B CD2 
17512 N N   . LYS B 1141 ? 0.4958 0.3470 0.4740 0.0083  -0.0196 0.0045  1139 LYS B N   
17513 C CA  . LYS B 1141 ? 0.5204 0.3606 0.4943 0.0088  -0.0212 0.0029  1139 LYS B CA  
17514 C C   . LYS B 1141 ? 0.5593 0.3971 0.5305 0.0145  -0.0208 0.0005  1139 LYS B C   
17515 O O   . LYS B 1141 ? 0.5100 0.3515 0.4818 0.0182  -0.0196 0.0015  1139 LYS B O   
17516 C CB  . LYS B 1141 ? 0.5179 0.3499 0.4898 0.0070  -0.0222 0.0058  1139 LYS B CB  
17517 N N   . ASN B 1142 ? 0.5377 0.3697 0.5060 0.0153  -0.0218 -0.0027 1140 ASN B N   
17518 C CA  . ASN B 1142 ? 0.5200 0.3490 0.4853 0.0206  -0.0214 -0.0053 1140 ASN B CA  
17519 C C   . ASN B 1142 ? 0.5310 0.3701 0.4990 0.0237  -0.0196 -0.0067 1140 ASN B C   
17520 O O   . ASN B 1142 ? 0.5034 0.3424 0.4700 0.0286  -0.0188 -0.0078 1140 ASN B O   
17521 C CB  . ASN B 1142 ? 0.5837 0.4054 0.5462 0.0241  -0.0216 -0.0038 1140 ASN B CB  
17522 C CG  . ASN B 1142 ? 0.7067 0.5178 0.6664 0.0210  -0.0234 -0.0023 1140 ASN B CG  
17523 O OD1 . ASN B 1142 ? 0.6801 0.4852 0.6378 0.0182  -0.0249 -0.0040 1140 ASN B OD1 
17524 N ND2 . ASN B 1142 ? 0.7416 0.5502 0.7011 0.0214  -0.0234 0.0011  1140 ASN B ND2 
17525 N N   . LEU B 1143 ? 0.4904 0.3384 0.4621 0.0209  -0.0190 -0.0065 1141 LEU B N   
17526 C CA  . LEU B 1143 ? 0.4360 0.2932 0.4100 0.0234  -0.0174 -0.0078 1141 LEU B CA  
17527 C C   . LEU B 1143 ? 0.4547 0.3092 0.4260 0.0261  -0.0175 -0.0116 1141 LEU B C   
17528 O O   . LEU B 1143 ? 0.5605 0.4094 0.5294 0.0240  -0.0189 -0.0135 1141 LEU B O   
17529 C CB  . LEU B 1143 ? 0.4159 0.2815 0.3939 0.0195  -0.0171 -0.0073 1141 LEU B CB  
17530 C CG  . LEU B 1143 ? 0.4223 0.2986 0.4036 0.0210  -0.0154 -0.0075 1141 LEU B CG  
17531 C CD1 . LEU B 1143 ? 0.4158 0.2957 0.3984 0.0231  -0.0143 -0.0048 1141 LEU B CD1 
17532 C CD2 . LEU B 1143 ? 0.3870 0.2693 0.3716 0.0167  -0.0154 -0.0072 1141 LEU B CD2 
17533 N N   . PRO B 1144 ? 0.4567 0.3153 0.4280 0.0306  -0.0161 -0.0127 1142 PRO B N   
17534 C CA  . PRO B 1144 ? 0.5029 0.3603 0.4719 0.0330  -0.0159 -0.0163 1142 PRO B CA  
17535 C C   . PRO B 1144 ? 0.4592 0.3206 0.4294 0.0295  -0.0163 -0.0179 1142 PRO B C   
17536 O O   . PRO B 1144 ? 0.3880 0.2570 0.3619 0.0269  -0.0158 -0.0166 1142 PRO B O   
17537 C CB  . PRO B 1144 ? 0.4944 0.3590 0.4651 0.0376  -0.0140 -0.0164 1142 PRO B CB  
17538 C CG  . PRO B 1144 ? 0.5049 0.3710 0.4773 0.0384  -0.0137 -0.0131 1142 PRO B CG  
17539 C CD  . PRO B 1144 ? 0.4433 0.3087 0.4172 0.0334  -0.0147 -0.0108 1142 PRO B CD  
17540 N N   . GLN B 1145 ? 0.4714 0.3274 0.4381 0.0296  -0.0171 -0.0209 1143 GLN B N   
17541 C CA  . GLN B 1145 ? 0.4404 0.2994 0.4076 0.0265  -0.0177 -0.0226 1143 GLN B CA  
17542 C C   . GLN B 1145 ? 0.4054 0.2751 0.3759 0.0275  -0.0160 -0.0230 1143 GLN B C   
17543 O O   . GLN B 1145 ? 0.3979 0.2727 0.3708 0.0243  -0.0163 -0.0229 1143 GLN B O   
17544 C CB  . GLN B 1145 ? 0.4796 0.3309 0.4419 0.0271  -0.0187 -0.0260 1143 GLN B CB  
17545 N N   . THR B 1146 ? 0.4124 0.2854 0.3830 0.0320  -0.0144 -0.0233 1144 THR B N   
17546 C CA  . THR B 1146 ? 0.4752 0.3584 0.4490 0.0328  -0.0129 -0.0233 1144 THR B CA  
17547 C C   . THR B 1146 ? 0.4238 0.3136 0.4020 0.0298  -0.0127 -0.0206 1144 THR B C   
17548 O O   . THR B 1146 ? 0.4419 0.3384 0.4226 0.0279  -0.0124 -0.0208 1144 THR B O   
17549 C CB  . THR B 1146 ? 0.4670 0.3528 0.4407 0.0378  -0.0112 -0.0235 1144 THR B CB  
17550 O OG1 . THR B 1146 ? 0.4985 0.3807 0.4721 0.0394  -0.0114 -0.0214 1144 THR B OG1 
17551 C CG2 . THR B 1146 ? 0.5409 0.4225 0.5106 0.0410  -0.0109 -0.0266 1144 THR B CG2 
17552 N N   . VAL B 1147 ? 0.3666 0.2545 0.3457 0.0293  -0.0129 -0.0180 1145 VAL B N   
17553 C CA  . VAL B 1147 ? 0.3232 0.2169 0.3062 0.0265  -0.0127 -0.0154 1145 VAL B CA  
17554 C C   . VAL B 1147 ? 0.3672 0.2592 0.3509 0.0216  -0.0140 -0.0152 1145 VAL B C   
17555 O O   . VAL B 1147 ? 0.3565 0.2550 0.3434 0.0191  -0.0138 -0.0145 1145 VAL B O   
17556 C CB  . VAL B 1147 ? 0.3178 0.2106 0.3014 0.0277  -0.0124 -0.0126 1145 VAL B CB  
17557 C CG1 . VAL B 1147 ? 0.3535 0.2534 0.3409 0.0251  -0.0118 -0.0102 1145 VAL B CG1 
17558 C CG2 . VAL B 1147 ? 0.3260 0.2198 0.3087 0.0327  -0.0113 -0.0130 1145 VAL B CG2 
17559 N N   . GLY B 1148 ? 0.3749 0.2583 0.3557 0.0203  -0.0156 -0.0157 1146 GLY B N   
17560 C CA  . GLY B 1148 ? 0.3613 0.2429 0.3429 0.0155  -0.0170 -0.0153 1146 GLY B CA  
17561 C C   . GLY B 1148 ? 0.3659 0.2522 0.3488 0.0136  -0.0173 -0.0171 1146 GLY B C   
17562 O O   . GLY B 1148 ? 0.3720 0.2615 0.3577 0.0098  -0.0179 -0.0160 1146 GLY B O   
17563 N N   . LEU B 1149 ? 0.3684 0.2553 0.3493 0.0163  -0.0169 -0.0197 1147 LEU B N   
17564 C CA  . LEU B 1149 ? 0.3848 0.2759 0.3665 0.0147  -0.0171 -0.0214 1147 LEU B CA  
17565 C C   . LEU B 1149 ? 0.3710 0.2719 0.3574 0.0136  -0.0160 -0.0199 1147 LEU B C   
17566 O O   . LEU B 1149 ? 0.3894 0.2939 0.3774 0.0112  -0.0166 -0.0205 1147 LEU B O   
17567 C CB  . LEU B 1149 ? 0.4939 0.3842 0.4724 0.0181  -0.0166 -0.0243 1147 LEU B CB  
17568 N N   . ARG B 1150 ? 0.3161 0.2211 0.3045 0.0153  -0.0146 -0.0180 1148 ARG B N   
17569 C CA  . ARG B 1150 ? 0.3036 0.2173 0.2961 0.0144  -0.0135 -0.0165 1148 ARG B CA  
17570 C C   . ARG B 1150 ? 0.2865 0.2013 0.2818 0.0111  -0.0137 -0.0139 1148 ARG B C   
17571 O O   . ARG B 1150 ? 0.2772 0.1989 0.2757 0.0103  -0.0128 -0.0126 1148 ARG B O   
17572 C CB  . ARG B 1150 ? 0.3081 0.2259 0.3012 0.0179  -0.0118 -0.0159 1148 ARG B CB  
17573 C CG  . ARG B 1150 ? 0.3488 0.2683 0.3403 0.0210  -0.0110 -0.0181 1148 ARG B CG  
17574 C CD  . ARG B 1150 ? 0.3308 0.2590 0.3252 0.0215  -0.0097 -0.0177 1148 ARG B CD  
17575 N NE  . ARG B 1150 ? 0.3253 0.2555 0.3185 0.0248  -0.0087 -0.0193 1148 ARG B NE  
17576 C CZ  . ARG B 1150 ? 0.3081 0.2430 0.3025 0.0272  -0.0074 -0.0186 1148 ARG B CZ  
17577 N NH1 . ARG B 1150 ? 0.2663 0.2044 0.2630 0.0267  -0.0070 -0.0163 1148 ARG B NH1 
17578 N NH2 . ARG B 1150 ? 0.2743 0.2109 0.2676 0.0301  -0.0066 -0.0201 1148 ARG B NH2 
17579 N N   . VAL B 1151 ? 0.3076 0.2159 0.3015 0.0094  -0.0149 -0.0130 1149 VAL B N   
17580 C CA  . VAL B 1151 ? 0.2996 0.2086 0.2959 0.0066  -0.0150 -0.0102 1149 VAL B CA  
17581 C C   . VAL B 1151 ? 0.3216 0.2285 0.3188 0.0023  -0.0166 -0.0102 1149 VAL B C   
17582 O O   . VAL B 1151 ? 0.3401 0.2400 0.3343 0.0016  -0.0181 -0.0117 1149 VAL B O   
17583 C CB  . VAL B 1151 ? 0.3251 0.2283 0.3194 0.0078  -0.0150 -0.0086 1149 VAL B CB  
17584 C CG1 . VAL B 1151 ? 0.3453 0.2483 0.3416 0.0043  -0.0152 -0.0056 1149 VAL B CG1 
17585 C CG2 . VAL B 1151 ? 0.3316 0.2379 0.3258 0.0118  -0.0134 -0.0081 1149 VAL B CG2 
17586 N N   . SER B 1152 ? 0.2833 0.1960 0.2843 -0.0005 -0.0162 -0.0086 1150 SER B N   
17587 C CA  . SER B 1152 ? 0.2820 0.1933 0.2845 -0.0047 -0.0177 -0.0079 1150 SER B CA  
17588 C C   . SER B 1152 ? 0.2916 0.2060 0.2971 -0.0068 -0.0168 -0.0047 1150 SER B C   
17589 O O   . SER B 1152 ? 0.2901 0.2091 0.2969 -0.0051 -0.0151 -0.0035 1150 SER B O   
17590 C CB  . SER B 1152 ? 0.3359 0.2517 0.3404 -0.0063 -0.0184 -0.0095 1150 SER B CB  
17591 O OG  . SER B 1152 ? 0.3853 0.3097 0.3932 -0.0057 -0.0168 -0.0087 1150 SER B OG  
17592 N N   . TRP B 1153 ? 0.3066 0.2186 0.3133 -0.0107 -0.0180 -0.0035 1151 TRP B N   
17593 C CA  . TRP B 1153 ? 0.2806 0.1956 0.2902 -0.0132 -0.0172 -0.0003 1151 TRP B CA  
17594 C C   . TRP B 1153 ? 0.3080 0.2290 0.3218 -0.0165 -0.0175 0.0000  1151 TRP B C   
17595 O O   . TRP B 1153 ? 0.3270 0.2459 0.3408 -0.0185 -0.0193 -0.0014 1151 TRP B O   
17596 C CB  . TRP B 1153 ? 0.2996 0.2067 0.3072 -0.0152 -0.0183 0.0013  1151 TRP B CB  
17597 C CG  . TRP B 1153 ? 0.2993 0.2012 0.3033 -0.0118 -0.0178 0.0015  1151 TRP B CG  
17598 C CD1 . TRP B 1153 ? 0.3526 0.2480 0.3525 -0.0090 -0.0186 -0.0006 1151 TRP B CD1 
17599 C CD2 . TRP B 1153 ? 0.2991 0.2023 0.3033 -0.0107 -0.0163 0.0041  1151 TRP B CD2 
17600 N NE1 . TRP B 1153 ? 0.3308 0.2232 0.3285 -0.0061 -0.0178 0.0005  1151 TRP B NE1 
17601 C CE2 . TRP B 1153 ? 0.3108 0.2079 0.3110 -0.0071 -0.0164 0.0035  1151 TRP B CE2 
17602 C CE3 . TRP B 1153 ? 0.3017 0.2106 0.3088 -0.0122 -0.0148 0.0069  1151 TRP B CE3 
17603 C CZ2 . TRP B 1153 ? 0.3265 0.2231 0.3257 -0.0052 -0.0154 0.0057  1151 TRP B CZ2 
17604 C CZ3 . TRP B 1153 ? 0.2976 0.2058 0.3034 -0.0105 -0.0137 0.0090  1151 TRP B CZ3 
17605 C CH2 . TRP B 1153 ? 0.3175 0.2197 0.3195 -0.0070 -0.0141 0.0084  1151 TRP B CH2 
17606 N N   . SER B 1154 ? 0.2488 0.1772 0.2663 -0.0169 -0.0158 0.0018  1152 SER B N   
17607 C CA  . SER B 1154 ? 0.2545 0.1895 0.2764 -0.0195 -0.0159 0.0021  1152 SER B CA  
17608 C C   . SER B 1154 ? 0.2597 0.1969 0.2846 -0.0229 -0.0153 0.0052  1152 SER B C   
17609 O O   . SER B 1154 ? 0.2625 0.2016 0.2877 -0.0221 -0.0135 0.0072  1152 SER B O   
17610 C CB  . SER B 1154 ? 0.2839 0.2266 0.3076 -0.0172 -0.0142 0.0013  1152 SER B CB  
17611 O OG  . SER B 1154 ? 0.2592 0.2081 0.2874 -0.0196 -0.0143 0.0018  1152 SER B OG  
17612 N N   . LYS B 1155 ? 0.2448 0.1818 0.2720 -0.0266 -0.0168 0.0056  1153 LYS B N   
17613 C CA  . LYS B 1155 ? 0.2994 0.2403 0.3306 -0.0302 -0.0162 0.0084  1153 LYS B CA  
17614 C C   . LYS B 1155 ? 0.2667 0.2167 0.3028 -0.0310 -0.0156 0.0084  1153 LYS B C   
17615 O O   . LYS B 1155 ? 0.2737 0.2278 0.3138 -0.0341 -0.0153 0.0104  1153 LYS B O   
17616 C CB  . LYS B 1155 ? 0.3210 0.2560 0.3518 -0.0342 -0.0184 0.0092  1153 LYS B CB  
17617 N N   . ASP B 1156 ? 0.2287 0.1818 0.2646 -0.0282 -0.0153 0.0061  1154 ASP B N   
17618 C CA  . ASP B 1156 ? 0.2117 0.1729 0.2520 -0.0287 -0.0149 0.0059  1154 ASP B CA  
17619 C C   . ASP B 1156 ? 0.2200 0.1836 0.2588 -0.0247 -0.0138 0.0039  1154 ASP B C   
17620 O O   . ASP B 1156 ? 0.2249 0.1868 0.2621 -0.0235 -0.0152 0.0015  1154 ASP B O   
17621 C CB  . ASP B 1156 ? 0.2222 0.1826 0.2641 -0.0315 -0.0174 0.0049  1154 ASP B CB  
17622 C CG  . ASP B 1156 ? 0.2245 0.1934 0.2716 -0.0324 -0.0171 0.0052  1154 ASP B CG  
17623 O OD1 . ASP B 1156 ? 0.2228 0.1972 0.2711 -0.0299 -0.0152 0.0050  1154 ASP B OD1 
17624 O OD2 . ASP B 1156 ? 0.2375 0.2073 0.2873 -0.0357 -0.0189 0.0056  1154 ASP B OD2 
17625 N N   . TRP B 1157 ? 0.1971 0.1649 0.2365 -0.0227 -0.0115 0.0049  1155 TRP B N   
17626 C CA  . TRP B 1157 ? 0.1996 0.1690 0.2372 -0.0190 -0.0105 0.0031  1155 TRP B CA  
17627 C C   . TRP B 1157 ? 0.2182 0.1920 0.2579 -0.0186 -0.0110 0.0014  1155 TRP B C   
17628 O O   . TRP B 1157 ? 0.2382 0.2108 0.2756 -0.0164 -0.0116 -0.0008 1155 TRP B O   
17629 C CB  . TRP B 1157 ? 0.2151 0.1886 0.2531 -0.0173 -0.0079 0.0045  1155 TRP B CB  
17630 C CG  . TRP B 1157 ? 0.2026 0.1723 0.2384 -0.0174 -0.0072 0.0063  1155 TRP B CG  
17631 C CD1 . TRP B 1157 ? 0.2236 0.1862 0.2568 -0.0184 -0.0086 0.0067  1155 TRP B CD1 
17632 C CD2 . TRP B 1157 ? 0.1965 0.1692 0.2324 -0.0165 -0.0051 0.0081  1155 TRP B CD2 
17633 N NE1 . TRP B 1157 ? 0.2323 0.1934 0.2641 -0.0181 -0.0074 0.0088  1155 TRP B NE1 
17634 C CE2 . TRP B 1157 ? 0.2149 0.1822 0.2482 -0.0170 -0.0052 0.0097  1155 TRP B CE2 
17635 C CE3 . TRP B 1157 ? 0.2191 0.1983 0.2567 -0.0153 -0.0030 0.0085  1155 TRP B CE3 
17636 C CZ2 . TRP B 1157 ? 0.2348 0.2033 0.2672 -0.0164 -0.0034 0.0118  1155 TRP B CZ2 
17637 C CZ3 . TRP B 1157 ? 0.2310 0.2112 0.2675 -0.0147 -0.0013 0.0103  1155 TRP B CZ3 
17638 C CH2 . TRP B 1157 ? 0.2427 0.2177 0.2767 -0.0153 -0.0015 0.0120  1155 TRP B CH2 
17639 N N   . ALA B 1158 ? 0.2025 0.1817 0.2467 -0.0207 -0.0109 0.0025  1156 ALA B N   
17640 C CA  . ALA B 1158 ? 0.2044 0.1883 0.2509 -0.0201 -0.0114 0.0012  1156 ALA B CA  
17641 C C   . ALA B 1158 ? 0.2423 0.2225 0.2874 -0.0210 -0.0140 -0.0007 1156 ALA B C   
17642 O O   . ALA B 1158 ? 0.3037 0.2855 0.3485 -0.0195 -0.0145 -0.0024 1156 ALA B O   
17643 C CB  . ALA B 1158 ? 0.2110 0.2018 0.2629 -0.0221 -0.0106 0.0030  1156 ALA B CB  
17644 N N   . ALA B 1159 ? 0.2097 0.1848 0.2538 -0.0235 -0.0158 -0.0004 1157 ALA B N   
17645 C CA  . ALA B 1159 ? 0.2383 0.2093 0.2806 -0.0244 -0.0184 -0.0023 1157 ALA B CA  
17646 C C   . ALA B 1159 ? 0.2683 0.2334 0.3051 -0.0217 -0.0187 -0.0045 1157 ALA B C   
17647 O O   . ALA B 1159 ? 0.2787 0.2417 0.3135 -0.0213 -0.0203 -0.0065 1157 ALA B O   
17648 C CB  . ALA B 1159 ? 0.2685 0.2359 0.3115 -0.0283 -0.0203 -0.0012 1157 ALA B CB  
17649 N N   . ASP B 1160 ? 0.2630 0.2255 0.2973 -0.0197 -0.0172 -0.0040 1158 ASP B N   
17650 C CA  . ASP B 1160 ? 0.2810 0.2375 0.3102 -0.0173 -0.0174 -0.0058 1158 ASP B CA  
17651 C C   . ASP B 1160 ? 0.2682 0.2275 0.2962 -0.0137 -0.0159 -0.0071 1158 ASP B C   
17652 O O   . ASP B 1160 ? 0.3228 0.2781 0.3469 -0.0113 -0.0159 -0.0085 1158 ASP B O   
17653 C CB  . ASP B 1160 ? 0.2684 0.2196 0.2954 -0.0174 -0.0170 -0.0045 1158 ASP B CB  
17654 C CG  . ASP B 1160 ? 0.2834 0.2300 0.3106 -0.0210 -0.0189 -0.0036 1158 ASP B CG  
17655 O OD1 . ASP B 1160 ? 0.3367 0.2831 0.3648 -0.0231 -0.0208 -0.0046 1158 ASP B OD1 
17656 O OD2 . ASP B 1160 ? 0.3005 0.2437 0.3270 -0.0219 -0.0185 -0.0019 1158 ASP B OD2 
17657 N N   . GLY B 1161 ? 0.2445 0.2107 0.2757 -0.0132 -0.0147 -0.0065 1159 GLY B N   
17658 C CA  . GLY B 1161 ? 0.2903 0.2594 0.3205 -0.0102 -0.0135 -0.0077 1159 GLY B CA  
17659 C C   . GLY B 1161 ? 0.3002 0.2695 0.3296 -0.0098 -0.0149 -0.0098 1159 GLY B C   
17660 O O   . GLY B 1161 ? 0.3497 0.3162 0.3786 -0.0116 -0.0169 -0.0105 1159 GLY B O   
17661 N N   . PRO B 1162 ? 0.3149 0.2876 0.3441 -0.0076 -0.0139 -0.0107 1160 PRO B N   
17662 C CA  . PRO B 1162 ? 0.2771 0.2535 0.3069 -0.0057 -0.0117 -0.0099 1160 PRO B CA  
17663 C C   . PRO B 1162 ? 0.2667 0.2398 0.2932 -0.0035 -0.0108 -0.0101 1160 PRO B C   
17664 O O   . PRO B 1162 ? 0.2839 0.2527 0.3072 -0.0024 -0.0115 -0.0116 1160 PRO B O   
17665 C CB  . PRO B 1162 ? 0.3064 0.2865 0.3366 -0.0044 -0.0116 -0.0112 1160 PRO B CB  
17666 C CG  . PRO B 1162 ? 0.3467 0.3231 0.3743 -0.0044 -0.0134 -0.0130 1160 PRO B CG  
17667 C CD  . PRO B 1162 ? 0.3543 0.3274 0.3824 -0.0071 -0.0151 -0.0125 1160 PRO B CD  
17668 N N   . PHE B 1163 ? 0.2130 0.1883 0.2405 -0.0029 -0.0091 -0.0086 1161 PHE B N   
17669 C CA  . PHE B 1163 ? 0.2220 0.1955 0.2469 -0.0007 -0.0081 -0.0085 1161 PHE B CA  
17670 C C   . PHE B 1163 ? 0.1950 0.1725 0.2198 0.0014  -0.0069 -0.0092 1161 PHE B C   
17671 O O   . PHE B 1163 ? 0.2227 0.2041 0.2492 0.0012  -0.0068 -0.0096 1161 PHE B O   
17672 C CB  . PHE B 1163 ? 0.2124 0.1854 0.2380 -0.0015 -0.0073 -0.0063 1161 PHE B CB  
17673 C CG  . PHE B 1163 ? 0.2136 0.1826 0.2395 -0.0040 -0.0085 -0.0055 1161 PHE B CG  
17674 C CD1 . PHE B 1163 ? 0.2940 0.2568 0.3169 -0.0037 -0.0098 -0.0065 1161 PHE B CD1 
17675 C CD2 . PHE B 1163 ? 0.2429 0.2143 0.2720 -0.0066 -0.0083 -0.0037 1161 PHE B CD2 
17676 C CE1 . PHE B 1163 ? 0.2939 0.2523 0.3167 -0.0062 -0.0112 -0.0058 1161 PHE B CE1 
17677 C CE2 . PHE B 1163 ? 0.2616 0.2292 0.2909 -0.0091 -0.0096 -0.0029 1161 PHE B CE2 
17678 C CZ  . PHE B 1163 ? 0.2592 0.2201 0.2853 -0.0090 -0.0111 -0.0039 1161 PHE B CZ  
17679 N N   . ALA B 1164 ? 0.2047 0.1812 0.2272 0.0036  -0.0062 -0.0094 1162 ALA B N   
17680 C CA  . ALA B 1164 ? 0.2120 0.1920 0.2341 0.0055  -0.0051 -0.0100 1162 ALA B CA  
17681 C C   . ALA B 1164 ? 0.2305 0.2121 0.2524 0.0065  -0.0038 -0.0086 1162 ALA B C   
17682 O O   . ALA B 1164 ? 0.2479 0.2318 0.2690 0.0081  -0.0030 -0.0090 1162 ALA B O   
17683 C CB  . ALA B 1164 ? 0.2246 0.2026 0.2441 0.0074  -0.0056 -0.0118 1162 ALA B CB  
17684 N N   . GLY B 1165 ? 0.1968 0.1772 0.2193 0.0053  -0.0035 -0.0069 1163 GLY B N   
17685 C CA  . GLY B 1165 ? 0.2070 0.1886 0.2291 0.0060  -0.0024 -0.0053 1163 GLY B CA  
17686 C C   . GLY B 1165 ? 0.2071 0.1857 0.2293 0.0046  -0.0025 -0.0035 1163 GLY B C   
17687 O O   . GLY B 1165 ? 0.2052 0.1804 0.2276 0.0032  -0.0037 -0.0037 1163 GLY B O   
17688 N N   . ALA B 1166 ? 0.2114 0.1912 0.2334 0.0048  -0.0015 -0.0018 1164 ALA B N   
17689 C CA  . ALA B 1166 ? 0.1875 0.1644 0.2093 0.0034  -0.0015 0.0001  1164 ALA B CA  
17690 C C   . ALA B 1166 ? 0.2052 0.1817 0.2250 0.0048  -0.0008 0.0015  1164 ALA B C   
17691 O O   . ALA B 1166 ? 0.2314 0.2118 0.2511 0.0060  0.0002  0.0015  1164 ALA B O   
17692 C CB  . ALA B 1166 ? 0.2132 0.1930 0.2378 0.0008  -0.0009 0.0014  1164 ALA B CB  
17693 N N   . LEU B 1167 ? 0.1929 0.1647 0.2112 0.0048  -0.0013 0.0027  1165 LEU B N   
17694 C CA  . LEU B 1167 ? 0.1937 0.1648 0.2102 0.0059  -0.0008 0.0045  1165 LEU B CA  
17695 C C   . LEU B 1167 ? 0.2255 0.1949 0.2424 0.0035  -0.0005 0.0069  1165 LEU B C   
17696 O O   . LEU B 1167 ? 0.2224 0.1878 0.2396 0.0019  -0.0015 0.0072  1165 LEU B O   
17697 C CB  . LEU B 1167 ? 0.2214 0.1881 0.2354 0.0082  -0.0017 0.0040  1165 LEU B CB  
17698 C CG  . LEU B 1167 ? 0.1956 0.1636 0.2092 0.0105  -0.0020 0.0017  1165 LEU B CG  
17699 C CD1 . LEU B 1167 ? 0.2407 0.2043 0.2520 0.0129  -0.0028 0.0014  1165 LEU B CD1 
17700 C CD2 . LEU B 1167 ? 0.2464 0.2202 0.2604 0.0115  -0.0010 0.0016  1165 LEU B CD2 
17701 N N   . VAL B 1168 ? 0.2117 0.1841 0.2285 0.0033  0.0008  0.0087  1166 VAL B N   
17702 C CA  . VAL B 1168 ? 0.2140 0.1860 0.2315 0.0009  0.0014  0.0111  1166 VAL B CA  
17703 C C   . VAL B 1168 ? 0.2232 0.1936 0.2380 0.0019  0.0017  0.0133  1166 VAL B C   
17704 O O   . VAL B 1168 ? 0.2240 0.1969 0.2375 0.0039  0.0023  0.0131  1166 VAL B O   
17705 C CB  . VAL B 1168 ? 0.2174 0.1952 0.2374 -0.0007 0.0028  0.0114  1166 VAL B CB  
17706 C CG1 . VAL B 1168 ? 0.2245 0.2024 0.2453 -0.0033 0.0037  0.0140  1166 VAL B CG1 
17707 C CG2 . VAL B 1168 ? 0.2221 0.2016 0.2447 -0.0014 0.0023  0.0093  1166 VAL B CG2 
17708 N N   . GLU B 1169 ? 0.2227 0.1888 0.2367 0.0004  0.0014  0.0153  1167 GLU B N   
17709 C CA  . GLU B 1169 ? 0.2303 0.1947 0.2418 0.0009  0.0017  0.0178  1167 GLU B CA  
17710 C C   . GLU B 1169 ? 0.2587 0.2242 0.2711 -0.0021 0.0028  0.0203  1167 GLU B C   
17711 O O   . GLU B 1169 ? 0.2657 0.2296 0.2800 -0.0046 0.0025  0.0207  1167 GLU B O   
17712 C CB  . GLU B 1169 ? 0.2335 0.1908 0.2427 0.0020  0.0002  0.0183  1167 GLU B CB  
17713 C CG  . GLU B 1169 ? 0.2605 0.2153 0.2670 0.0025  0.0003  0.0211  1167 GLU B CG  
17714 C CD  . GLU B 1169 ? 0.2704 0.2174 0.2748 0.0030  -0.0012 0.0219  1167 GLU B CD  
17715 O OE1 . GLU B 1169 ? 0.2696 0.2129 0.2747 0.0025  -0.0023 0.0204  1167 GLU B OE1 
17716 O OE2 . GLU B 1169 ? 0.3086 0.2530 0.3106 0.0041  -0.0014 0.0240  1167 GLU B OE2 
17717 N N   . GLY B 1170 ? 0.2640 0.2325 0.2752 -0.0019 0.0042  0.0220  1168 GLY B N   
17718 C CA  . GLY B 1170 ? 0.2630 0.2327 0.2748 -0.0046 0.0054  0.0246  1168 GLY B CA  
17719 C C   . GLY B 1170 ? 0.2981 0.2725 0.3086 -0.0040 0.0072  0.0257  1168 GLY B C   
17720 O O   . GLY B 1170 ? 0.2695 0.2464 0.2787 -0.0016 0.0073  0.0243  1168 GLY B O   
17721 N N   . ASP B 1171 ? 0.3014 0.2769 0.3118 -0.0062 0.0085  0.0283  1169 ASP B N   
17722 C CA  . ASP B 1171 ? 0.2722 0.2526 0.2814 -0.0059 0.0104  0.0292  1169 ASP B CA  
17723 C C   . ASP B 1171 ? 0.2858 0.2723 0.2978 -0.0061 0.0118  0.0273  1169 ASP B C   
17724 O O   . ASP B 1171 ? 0.2639 0.2510 0.2790 -0.0066 0.0112  0.0254  1169 ASP B O   
17725 C CB  . ASP B 1171 ? 0.2926 0.2721 0.3003 -0.0080 0.0115  0.0327  1169 ASP B CB  
17726 C CG  . ASP B 1171 ? 0.3423 0.3228 0.3533 -0.0114 0.0124  0.0339  1169 ASP B CG  
17727 O OD1 . ASP B 1171 ? 0.3206 0.3031 0.3352 -0.0121 0.0122  0.0321  1169 ASP B OD1 
17728 O OD2 . ASP B 1171 ? 0.4063 0.3855 0.4163 -0.0134 0.0131  0.0370  1169 ASP B OD2 
17729 N N   . ALA B 1172 ? 0.2883 0.2792 0.2991 -0.0057 0.0136  0.0277  1170 ALA B N   
17730 C CA  . ALA B 1172 ? 0.3157 0.3121 0.3287 -0.0053 0.0149  0.0256  1170 ALA B CA  
17731 C C   . ALA B 1172 ? 0.2944 0.2929 0.3118 -0.0076 0.0156  0.0256  1170 ALA B C   
17732 O O   . ALA B 1172 ? 0.2917 0.2923 0.3118 -0.0072 0.0152  0.0234  1170 ALA B O   
17733 C CB  . ALA B 1172 ? 0.3214 0.3217 0.3319 -0.0047 0.0169  0.0264  1170 ALA B CB  
17734 N N   . GLU B 1173 ? 0.2992 0.2974 0.3174 -0.0101 0.0164  0.0283  1171 GLU B N   
17735 C CA  . GLU B 1173 ? 0.2851 0.2861 0.3078 -0.0124 0.0170  0.0284  1171 GLU B CA  
17736 C C   . GLU B 1173 ? 0.2825 0.2799 0.3076 -0.0132 0.0147  0.0271  1171 GLU B C   
17737 O O   . GLU B 1173 ? 0.2668 0.2670 0.2957 -0.0140 0.0147  0.0258  1171 GLU B O   
17738 C CB  . GLU B 1173 ? 0.4236 0.4261 0.4469 -0.0151 0.0187  0.0316  1171 GLU B CB  
17739 C CG  . GLU B 1173 ? 0.4727 0.4804 0.4947 -0.0144 0.0215  0.0323  1171 GLU B CG  
17740 C CD  . GLU B 1173 ? 0.4493 0.4624 0.4735 -0.0129 0.0226  0.0296  1171 GLU B CD  
17741 O OE1 . GLU B 1173 ? 0.4288 0.4442 0.4574 -0.0138 0.0224  0.0286  1171 GLU B OE1 
17742 O OE2 . GLU B 1173 ? 0.5507 0.5655 0.5720 -0.0107 0.0235  0.0286  1171 GLU B OE2 
17743 N N   . ARG B 1174 ? 0.2663 0.2576 0.2891 -0.0128 0.0128  0.0274  1172 ARG B N   
17744 C CA  . ARG B 1174 ? 0.2856 0.2730 0.3098 -0.0131 0.0106  0.0258  1172 ARG B CA  
17745 C C   . ARG B 1174 ? 0.2334 0.2227 0.2584 -0.0108 0.0100  0.0226  1172 ARG B C   
17746 O O   . ARG B 1174 ? 0.2498 0.2399 0.2777 -0.0115 0.0092  0.0210  1172 ARG B O   
17747 C CB  . ARG B 1174 ? 0.2833 0.2635 0.3042 -0.0126 0.0089  0.0267  1172 ARG B CB  
17748 C CG  . ARG B 1174 ? 0.2692 0.2447 0.2908 -0.0125 0.0066  0.0248  1172 ARG B CG  
17749 C CD  . ARG B 1174 ? 0.3139 0.2895 0.3391 -0.0157 0.0061  0.0252  1172 ARG B CD  
17750 N NE  . ARG B 1174 ? 0.2945 0.2650 0.3197 -0.0157 0.0038  0.0234  1172 ARG B NE  
17751 C CZ  . ARG B 1174 ? 0.2764 0.2471 0.3046 -0.0179 0.0028  0.0226  1172 ARG B CZ  
17752 N NH1 . ARG B 1174 ? 0.2893 0.2652 0.3212 -0.0203 0.0039  0.0236  1172 ARG B NH1 
17753 N NH2 . ARG B 1174 ? 0.2827 0.2485 0.3101 -0.0175 0.0007  0.0208  1172 ARG B NH2 
17754 N N   . ILE B 1175 ? 0.2353 0.2256 0.2577 -0.0081 0.0104  0.0216  1173 ILE B N   
17755 C CA  . ILE B 1175 ? 0.2300 0.2223 0.2529 -0.0060 0.0099  0.0186  1173 ILE B CA  
17756 C C   . ILE B 1175 ? 0.2375 0.2352 0.2638 -0.0068 0.0111  0.0176  1173 ILE B C   
17757 O O   . ILE B 1175 ? 0.2326 0.2309 0.2610 -0.0065 0.0101  0.0156  1173 ILE B O   
17758 C CB  . ILE B 1175 ? 0.2188 0.2118 0.2383 -0.0034 0.0102  0.0181  1173 ILE B CB  
17759 C CG1 . ILE B 1175 ? 0.2434 0.2310 0.2601 -0.0022 0.0086  0.0186  1173 ILE B CG1 
17760 C CG2 . ILE B 1175 ? 0.2296 0.2256 0.2500 -0.0017 0.0102  0.0153  1173 ILE B CG2 
17761 C CD1 . ILE B 1175 ? 0.2540 0.2421 0.2673 0.0001  0.0088  0.0188  1173 ILE B CD1 
17762 N N   . ARG B 1176 ? 0.2484 0.2502 0.2753 -0.0076 0.0132  0.0191  1174 ARG B N   
17763 C CA  . ARG B 1176 ? 0.2279 0.2352 0.2584 -0.0080 0.0144  0.0182  1174 ARG B CA  
17764 C C   . ARG B 1176 ? 0.2297 0.2369 0.2642 -0.0102 0.0135  0.0183  1174 ARG B C   
17765 O O   . ARG B 1176 ? 0.2396 0.2492 0.2768 -0.0099 0.0131  0.0164  1174 ARG B O   
17766 C CB  . ARG B 1176 ? 0.2672 0.2786 0.2974 -0.0086 0.0170  0.0200  1174 ARG B CB  
17767 C CG  . ARG B 1176 ? 0.2891 0.3063 0.3225 -0.0083 0.0186  0.0188  1174 ARG B CG  
17768 C CD  . ARG B 1176 ? 0.3460 0.3675 0.3799 -0.0093 0.0213  0.0209  1174 ARG B CD  
17769 N NE  . ARG B 1176 ? 0.3883 0.4088 0.4177 -0.0086 0.0223  0.0222  1174 ARG B NE  
17770 C CZ  . ARG B 1176 ? 0.3922 0.4146 0.4188 -0.0065 0.0235  0.0211  1174 ARG B CZ  
17771 N NH1 . ARG B 1176 ? 0.3782 0.4032 0.4059 -0.0049 0.0239  0.0187  1174 ARG B NH1 
17772 N NH2 . ARG B 1176 ? 0.4514 0.4727 0.4737 -0.0061 0.0244  0.0225  1174 ARG B NH2 
17773 N N   . ALA B 1177 ? 0.2471 0.2517 0.2821 -0.0127 0.0130  0.0204  1175 ALA B N   
17774 C CA  . ALA B 1177 ? 0.2417 0.2462 0.2806 -0.0151 0.0119  0.0206  1175 ALA B CA  
17775 C C   . ALA B 1177 ? 0.2221 0.2231 0.2610 -0.0143 0.0095  0.0182  1175 ALA B C   
17776 O O   . ALA B 1177 ? 0.2360 0.2390 0.2782 -0.0151 0.0088  0.0171  1175 ALA B O   
17777 C CB  . ALA B 1177 ? 0.2636 0.2649 0.3023 -0.0180 0.0117  0.0234  1175 ALA B CB  
17778 N N   . VAL B 1178 ? 0.2281 0.2240 0.2633 -0.0127 0.0083  0.0175  1176 VAL B N   
17779 C CA  . VAL B 1178 ? 0.2315 0.2241 0.2664 -0.0118 0.0061  0.0151  1176 VAL B CA  
17780 C C   . VAL B 1178 ? 0.2171 0.2134 0.2529 -0.0098 0.0064  0.0127  1176 VAL B C   
17781 O O   . VAL B 1178 ? 0.2240 0.2205 0.2616 -0.0100 0.0051  0.0111  1176 VAL B O   
17782 C CB  . VAL B 1178 ? 0.2232 0.2098 0.2540 -0.0102 0.0050  0.0150  1176 VAL B CB  
17783 C CG1 . VAL B 1178 ? 0.2487 0.2325 0.2786 -0.0086 0.0032  0.0123  1176 VAL B CG1 
17784 C CG2 . VAL B 1178 ? 0.2655 0.2473 0.2954 -0.0124 0.0044  0.0173  1176 VAL B CG2 
17785 N N   . ASN B 1179 ? 0.2173 0.2166 0.2516 -0.0079 0.0079  0.0125  1177 ASN B N   
17786 C CA  . ASN B 1179 ? 0.2286 0.2313 0.2636 -0.0060 0.0082  0.0103  1177 ASN B CA  
17787 C C   . ASN B 1179 ? 0.2136 0.2207 0.2528 -0.0073 0.0087  0.0100  1177 ASN B C   
17788 O O   . ASN B 1179 ? 0.2240 0.2321 0.2647 -0.0066 0.0078  0.0082  1177 ASN B O   
17789 C CB  . ASN B 1179 ? 0.2263 0.2311 0.2588 -0.0042 0.0098  0.0104  1177 ASN B CB  
17790 C CG  . ASN B 1179 ? 0.2466 0.2530 0.2784 -0.0020 0.0096  0.0080  1177 ASN B CG  
17791 O OD1 . ASN B 1179 ? 0.2674 0.2720 0.2994 -0.0014 0.0081  0.0062  1177 ASN B OD1 
17792 N ND2 . ASN B 1179 ? 0.2603 0.2698 0.2910 -0.0008 0.0112  0.0078  1177 ASN B ND2 
17793 N N   . LYS B 1180 ? 0.2187 0.2287 0.2602 -0.0091 0.0101  0.0121  1178 LYS B N   
17794 C CA  . LYS B 1180 ? 0.2402 0.2547 0.2861 -0.0104 0.0105  0.0121  1178 LYS B CA  
17795 C C   . LYS B 1180 ? 0.2046 0.2169 0.2527 -0.0120 0.0082  0.0114  1178 LYS B C   
17796 O O   . LYS B 1180 ? 0.2327 0.2475 0.2834 -0.0118 0.0075  0.0101  1178 LYS B O   
17797 C CB  . LYS B 1180 ? 0.2583 0.2763 0.3063 -0.0123 0.0124  0.0146  1178 LYS B CB  
17798 C CG  . LYS B 1180 ? 0.2929 0.3149 0.3398 -0.0107 0.0150  0.0149  1178 LYS B CG  
17799 C CD  . LYS B 1180 ? 0.3313 0.3567 0.3801 -0.0126 0.0170  0.0176  1178 LYS B CD  
17800 C CE  . LYS B 1180 ? 0.4870 0.5170 0.5413 -0.0143 0.0172  0.0180  1178 LYS B CE  
17801 N NZ  . LYS B 1180 ? 0.6205 0.6555 0.6767 -0.0122 0.0184  0.0164  1178 LYS B NZ  
17802 N N   . ALA B 1181 ? 0.2164 0.2237 0.2632 -0.0136 0.0068  0.0124  1179 ALA B N   
17803 C CA  . ALA B 1181 ? 0.2208 0.2254 0.2691 -0.0152 0.0045  0.0116  1179 ALA B CA  
17804 C C   . ALA B 1181 ? 0.2156 0.2183 0.2623 -0.0132 0.0030  0.0089  1179 ALA B C   
17805 O O   . ALA B 1181 ? 0.2325 0.2359 0.2813 -0.0138 0.0016  0.0077  1179 ALA B O   
17806 C CB  . ALA B 1181 ? 0.2191 0.2179 0.2656 -0.0171 0.0033  0.0130  1179 ALA B CB  
17807 N N   . ILE B 1182 ? 0.2050 0.2054 0.2480 -0.0107 0.0032  0.0079  1180 ILE B N   
17808 C CA  . ILE B 1182 ? 0.2222 0.2210 0.2635 -0.0087 0.0020  0.0054  1180 ILE B CA  
17809 C C   . ILE B 1182 ? 0.2132 0.2170 0.2568 -0.0078 0.0026  0.0042  1180 ILE B C   
17810 O O   . ILE B 1182 ? 0.2208 0.2243 0.2651 -0.0075 0.0012  0.0025  1180 ILE B O   
17811 C CB  . ILE B 1182 ? 0.2286 0.2245 0.2658 -0.0064 0.0023  0.0049  1180 ILE B CB  
17812 C CG1 . ILE B 1182 ? 0.2319 0.2219 0.2669 -0.0070 0.0012  0.0057  1180 ILE B CG1 
17813 C CG2 . ILE B 1182 ? 0.2627 0.2585 0.2987 -0.0042 0.0016  0.0025  1180 ILE B CG2 
17814 C CD1 . ILE B 1182 ? 0.2536 0.2410 0.2848 -0.0048 0.0016  0.0058  1180 ILE B CD1 
17815 N N   . ALA B 1183 ? 0.2349 0.2432 0.2797 -0.0072 0.0046  0.0050  1181 ALA B N   
17816 C CA  . ALA B 1183 ? 0.2426 0.2553 0.2894 -0.0061 0.0052  0.0038  1181 ALA B CA  
17817 C C   . ALA B 1183 ? 0.2613 0.2765 0.3123 -0.0078 0.0043  0.0039  1181 ALA B C   
17818 O O   . ALA B 1183 ? 0.2961 0.3135 0.3485 -0.0068 0.0039  0.0026  1181 ALA B O   
17819 C CB  . ALA B 1183 ? 0.2341 0.2508 0.2809 -0.0050 0.0076  0.0045  1181 ALA B CB  
17820 N N   . ALA B 1184 ? 0.2249 0.2395 0.2779 -0.0103 0.0037  0.0055  1182 ALA B N   
17821 C CA  . ALA B 1184 ? 0.2301 0.2470 0.2872 -0.0123 0.0025  0.0057  1182 ALA B CA  
17822 C C   . ALA B 1184 ? 0.2446 0.2572 0.3008 -0.0131 -0.0002 0.0044  1182 ALA B C   
17823 O O   . ALA B 1184 ? 0.2453 0.2594 0.3046 -0.0149 -0.0016 0.0045  1182 ALA B O   
17824 C CB  . ALA B 1184 ? 0.2605 0.2795 0.3206 -0.0150 0.0033  0.0082  1182 ALA B CB  
17825 N N   . LEU B 1185 ? 0.2229 0.2302 0.2748 -0.0119 -0.0010 0.0031  1183 LEU B N   
17826 C CA  . LEU B 1185 ? 0.2300 0.2332 0.2807 -0.0124 -0.0035 0.0017  1183 LEU B CA  
17827 C C   . LEU B 1185 ? 0.2337 0.2394 0.2854 -0.0112 -0.0043 -0.0001 1183 LEU B C   
17828 O O   . LEU B 1185 ? 0.2708 0.2790 0.3220 -0.0091 -0.0030 -0.0008 1183 LEU B O   
17829 C CB  . LEU B 1185 ? 0.2164 0.2137 0.2623 -0.0111 -0.0040 0.0007  1183 LEU B CB  
17830 C CG  . LEU B 1185 ? 0.2222 0.2162 0.2666 -0.0121 -0.0035 0.0025  1183 LEU B CG  
17831 C CD1 . LEU B 1185 ? 0.2229 0.2118 0.2628 -0.0101 -0.0038 0.0015  1183 LEU B CD1 
17832 C CD2 . LEU B 1185 ? 0.2303 0.2221 0.2764 -0.0154 -0.0050 0.0036  1183 LEU B CD2 
17833 N N   . PRO B 1186 ? 0.2276 0.2324 0.2805 -0.0127 -0.0064 -0.0008 1184 PRO B N   
17834 C CA  . PRO B 1186 ? 0.2509 0.2573 0.3041 -0.0115 -0.0073 -0.0024 1184 PRO B CA  
17835 C C   . PRO B 1186 ? 0.2273 0.2298 0.2760 -0.0093 -0.0077 -0.0043 1184 PRO B C   
17836 O O   . PRO B 1186 ? 0.2695 0.2676 0.3150 -0.0089 -0.0078 -0.0045 1184 PRO B O   
17837 C CB  . PRO B 1186 ? 0.3207 0.3265 0.3759 -0.0140 -0.0098 -0.0025 1184 PRO B CB  
17838 C CG  . PRO B 1186 ? 0.3508 0.3516 0.4042 -0.0158 -0.0106 -0.0018 1184 PRO B CG  
17839 C CD  . PRO B 1186 ? 0.2847 0.2862 0.3380 -0.0155 -0.0082 -0.0002 1184 PRO B CD  
17840 N N   . GLY B 1187 ? 0.2573 0.2618 0.3060 -0.0078 -0.0079 -0.0056 1185 GLY B N   
17841 C CA  . GLY B 1187 ? 0.2538 0.2552 0.2985 -0.0059 -0.0083 -0.0074 1185 GLY B CA  
17842 C C   . GLY B 1187 ? 0.2301 0.2324 0.2731 -0.0036 -0.0064 -0.0075 1185 GLY B C   
17843 O O   . GLY B 1187 ? 0.2761 0.2823 0.3209 -0.0030 -0.0049 -0.0069 1185 GLY B O   
17844 N N   . PRO B 1188 ? 0.2047 0.2034 0.2439 -0.0023 -0.0064 -0.0084 1186 PRO B N   
17845 C CA  . PRO B 1188 ? 0.2071 0.2068 0.2445 -0.0003 -0.0048 -0.0087 1186 PRO B CA  
17846 C C   . PRO B 1188 ? 0.2191 0.2202 0.2571 -0.0003 -0.0031 -0.0071 1186 PRO B C   
17847 O O   . PRO B 1188 ? 0.2424 0.2423 0.2812 -0.0017 -0.0031 -0.0059 1186 PRO B O   
17848 C CB  . PRO B 1188 ? 0.2512 0.2467 0.2848 0.0009  -0.0054 -0.0099 1186 PRO B CB  
17849 C CG  . PRO B 1188 ? 0.3334 0.3251 0.3667 -0.0007 -0.0068 -0.0098 1186 PRO B CG  
17850 C CD  . PRO B 1188 ? 0.2449 0.2385 0.2814 -0.0027 -0.0079 -0.0093 1186 PRO B CD  
17851 N N   . LEU B 1189 ? 0.2142 0.2178 0.2518 0.0012  -0.0016 -0.0072 1187 LEU B N   
17852 C CA  . LEU B 1189 ? 0.1933 0.1980 0.2306 0.0015  0.0000  -0.0059 1187 LEU B CA  
17853 C C   . LEU B 1189 ? 0.2016 0.2028 0.2356 0.0023  -0.0001 -0.0060 1187 LEU B C   
17854 O O   . LEU B 1189 ? 0.2415 0.2417 0.2733 0.0038  -0.0004 -0.0072 1187 LEU B O   
17855 C CB  . LEU B 1189 ? 0.2197 0.2276 0.2568 0.0029  0.0014  -0.0063 1187 LEU B CB  
17856 C CG  . LEU B 1189 ? 0.2285 0.2405 0.2690 0.0024  0.0022  -0.0058 1187 LEU B CG  
17857 C CD1 . LEU B 1189 ? 0.3201 0.3328 0.3623 0.0022  0.0008  -0.0068 1187 LEU B CD1 
17858 C CD2 . LEU B 1189 ? 0.2801 0.2944 0.3197 0.0039  0.0039  -0.0059 1187 LEU B CD2 
17859 N N   . LEU B 1190 ? 0.1968 0.1962 0.2306 0.0015  0.0002  -0.0046 1188 LEU B N   
17860 C CA  . LEU B 1190 ? 0.2166 0.2123 0.2474 0.0024  -0.0001 -0.0045 1188 LEU B CA  
17861 C C   . LEU B 1190 ? 0.2277 0.2248 0.2569 0.0038  0.0012  -0.0039 1188 LEU B C   
17862 O O   . LEU B 1190 ? 0.2198 0.2195 0.2499 0.0034  0.0026  -0.0027 1188 LEU B O   
17863 C CB  . LEU B 1190 ? 0.2185 0.2109 0.2494 0.0008  -0.0007 -0.0031 1188 LEU B CB  
17864 C CG  . LEU B 1190 ? 0.1993 0.1896 0.2316 -0.0010 -0.0023 -0.0035 1188 LEU B CG  
17865 C CD1 . LEU B 1190 ? 0.2318 0.2178 0.2632 -0.0022 -0.0029 -0.0023 1188 LEU B CD1 
17866 C CD2 . LEU B 1190 ? 0.2391 0.2278 0.2700 0.0000  -0.0036 -0.0057 1188 LEU B CD2 
17867 N N   . LEU B 1191 ? 0.2125 0.2080 0.2392 0.0055  0.0009  -0.0047 1189 LEU B N   
17868 C CA  . LEU B 1191 ? 0.1887 0.1850 0.2136 0.0068  0.0018  -0.0041 1189 LEU B CA  
17869 C C   . LEU B 1191 ? 0.2206 0.2141 0.2445 0.0064  0.0018  -0.0024 1189 LEU B C   
17870 O O   . LEU B 1191 ? 0.2405 0.2301 0.2631 0.0068  0.0008  -0.0026 1189 LEU B O   
17871 C CB  . LEU B 1191 ? 0.2035 0.1996 0.2265 0.0086  0.0014  -0.0055 1189 LEU B CB  
17872 C CG  . LEU B 1191 ? 0.2153 0.2137 0.2369 0.0099  0.0023  -0.0052 1189 LEU B CG  
17873 C CD1 . LEU B 1191 ? 0.2152 0.2141 0.2356 0.0113  0.0018  -0.0067 1189 LEU B CD1 
17874 C CD2 . LEU B 1191 ? 0.2148 0.2114 0.2348 0.0103  0.0024  -0.0036 1189 LEU B CD2 
17875 N N   . VAL B 1192 ? 0.2008 0.1958 0.2251 0.0056  0.0030  -0.0007 1190 VAL B N   
17876 C CA  . VAL B 1192 ? 0.2184 0.2110 0.2421 0.0048  0.0031  0.0012  1190 VAL B CA  
17877 C C   . VAL B 1192 ? 0.2213 0.2139 0.2424 0.0064  0.0036  0.0020  1190 VAL B C   
17878 O O   . VAL B 1192 ? 0.2349 0.2308 0.2555 0.0070  0.0045  0.0019  1190 VAL B O   
17879 C CB  . VAL B 1192 ? 0.2214 0.2161 0.2471 0.0028  0.0041  0.0028  1190 VAL B CB  
17880 C CG1 . VAL B 1192 ? 0.2365 0.2287 0.2613 0.0018  0.0043  0.0050  1190 VAL B CG1 
17881 C CG2 . VAL B 1192 ? 0.2284 0.2236 0.2571 0.0011  0.0035  0.0022  1190 VAL B CG2 
17882 N N   . GLN B 1193 ? 0.1994 0.1881 0.2188 0.0069  0.0028  0.0029  1191 GLN B N   
17883 C CA  . GLN B 1193 ? 0.1822 0.1707 0.1993 0.0082  0.0032  0.0041  1191 GLN B CA  
17884 C C   . GLN B 1193 ? 0.2117 0.1974 0.2282 0.0070  0.0033  0.0065  1191 GLN B C   
17885 O O   . GLN B 1193 ? 0.2194 0.2011 0.2362 0.0062  0.0024  0.0068  1191 GLN B O   
17886 C CB  . GLN B 1193 ? 0.2014 0.1878 0.2168 0.0104  0.0021  0.0032  1191 GLN B CB  
17887 C CG  . GLN B 1193 ? 0.2192 0.2080 0.2352 0.0115  0.0019  0.0010  1191 GLN B CG  
17888 C CD  . GLN B 1193 ? 0.2480 0.2360 0.2624 0.0138  0.0013  0.0004  1191 GLN B CD  
17889 O OE1 . GLN B 1193 ? 0.2311 0.2205 0.2442 0.0149  0.0015  0.0013  1191 GLN B OE1 
17890 N NE2 . GLN B 1193 ? 0.2375 0.2233 0.2520 0.0146  0.0004  -0.0010 1191 GLN B NE2 
17891 N N   . ALA B 1194 ? 0.2120 0.1996 0.2275 0.0068  0.0043  0.0082  1192 ALA B N   
17892 C CA  . ALA B 1194 ? 0.2130 0.1983 0.2277 0.0055  0.0047  0.0107  1192 ALA B CA  
17893 C C   . ALA B 1194 ? 0.2429 0.2274 0.2547 0.0069  0.0046  0.0121  1192 ALA B C   
17894 O O   . ALA B 1194 ? 0.2750 0.2623 0.2856 0.0084  0.0049  0.0115  1192 ALA B O   
17895 C CB  . ALA B 1194 ? 0.2402 0.2288 0.2565 0.0034  0.0062  0.0117  1192 ALA B CB  
17896 N N   . ALA B 1195 ? 0.2319 0.2123 0.2424 0.0064  0.0042  0.0142  1193 ALA B N   
17897 C CA  . ALA B 1195 ? 0.2501 0.2294 0.2578 0.0077  0.0041  0.0160  1193 ALA B CA  
17898 C C   . ALA B 1195 ? 0.2611 0.2369 0.2680 0.0060  0.0042  0.0187  1193 ALA B C   
17899 O O   . ALA B 1195 ? 0.2624 0.2352 0.2707 0.0043  0.0038  0.0189  1193 ALA B O   
17900 C CB  . ALA B 1195 ? 0.2689 0.2455 0.2753 0.0104  0.0026  0.0151  1193 ALA B CB  
17901 N N   . SER B 1196 ? 0.2653 0.2414 0.2698 0.0062  0.0047  0.0209  1194 SER B N   
17902 C CA  . SER B 1196 ? 0.2897 0.2618 0.2929 0.0048  0.0046  0.0237  1194 SER B CA  
17903 C C   . SER B 1196 ? 0.2969 0.2632 0.2984 0.0066  0.0029  0.0242  1194 SER B C   
17904 O O   . SER B 1196 ? 0.2860 0.2523 0.2871 0.0092  0.0020  0.0226  1194 SER B O   
17905 C CB  . SER B 1196 ? 0.2935 0.2680 0.2944 0.0045  0.0058  0.0260  1194 SER B CB  
17906 O OG  . SER B 1196 ? 0.3172 0.2922 0.3158 0.0072  0.0050  0.0259  1194 SER B OG  
17907 N N   . SER B 1197 ? 0.3057 0.2671 0.3064 0.0051  0.0025  0.0264  1195 SER B N   
17908 C CA  . SER B 1197 ? 0.3019 0.2572 0.3006 0.0069  0.0009  0.0271  1195 SER B CA  
17909 C C   . SER B 1197 ? 0.2899 0.2463 0.2861 0.0097  0.0006  0.0280  1195 SER B C   
17910 O O   . SER B 1197 ? 0.3140 0.2681 0.3094 0.0125  -0.0007 0.0272  1195 SER B O   
17911 C CB  . SER B 1197 ? 0.3150 0.2648 0.3127 0.0047  0.0007  0.0298  1195 SER B CB  
17912 O OG  . SER B 1197 ? 0.3271 0.2760 0.3274 0.0020  0.0008  0.0290  1195 SER B OG  
17913 N N   . GLY B 1198 ? 0.3372 0.2973 0.3321 0.0091  0.0016  0.0297  1196 GLY B N   
17914 C CA  . GLY B 1198 ? 0.3555 0.3169 0.3479 0.0115  0.0011  0.0306  1196 GLY B CA  
17915 C C   . GLY B 1198 ? 0.3862 0.3518 0.3796 0.0138  0.0008  0.0279  1196 GLY B C   
17916 O O   . GLY B 1198 ? 0.3685 0.3337 0.3608 0.0165  -0.0003 0.0279  1196 GLY B O   
17917 N N   . GLU B 1199 ? 0.3141 0.2838 0.3098 0.0127  0.0018  0.0256  1197 GLU B N   
17918 C CA  . GLU B 1199 ? 0.3569 0.3305 0.3536 0.0146  0.0015  0.0230  1197 GLU B CA  
17919 C C   . GLU B 1199 ? 0.3560 0.3266 0.3538 0.0166  0.0001  0.0214  1197 GLU B C   
17920 O O   . GLU B 1199 ? 0.3412 0.3135 0.3388 0.0191  -0.0006 0.0204  1197 GLU B O   
17921 C CB  . GLU B 1199 ? 0.3573 0.3352 0.3562 0.0129  0.0028  0.0211  1197 GLU B CB  
17922 C CG  . GLU B 1199 ? 0.4679 0.4499 0.4678 0.0143  0.0026  0.0185  1197 GLU B CG  
17923 C CD  . GLU B 1199 ? 0.5193 0.5050 0.5210 0.0127  0.0039  0.0168  1197 GLU B CD  
17924 O OE1 . GLU B 1199 ? 0.5297 0.5155 0.5320 0.0105  0.0050  0.0178  1197 GLU B OE1 
17925 O OE2 . GLU B 1199 ? 0.6418 0.6303 0.6445 0.0136  0.0037  0.0146  1197 GLU B OE2 
17926 N N   . ILE B 1200 ? 0.2951 0.2611 0.2938 0.0156  -0.0002 0.0212  1198 ILE B N   
17927 C CA  . ILE B 1200 ? 0.3079 0.2704 0.3071 0.0176  -0.0014 0.0197  1198 ILE B CA  
17928 C C   . ILE B 1200 ? 0.3554 0.3149 0.3525 0.0203  -0.0025 0.0212  1198 ILE B C   
17929 O O   . ILE B 1200 ? 0.3515 0.3109 0.3488 0.0231  -0.0033 0.0199  1198 ILE B O   
17930 C CB  . ILE B 1200 ? 0.2937 0.2513 0.2938 0.0158  -0.0016 0.0193  1198 ILE B CB  
17931 C CG1 . ILE B 1200 ? 0.2921 0.2534 0.2947 0.0136  -0.0007 0.0174  1198 ILE B CG1 
17932 C CG2 . ILE B 1200 ? 0.3057 0.2584 0.3054 0.0180  -0.0029 0.0179  1198 ILE B CG2 
17933 C CD1 . ILE B 1200 ? 0.2993 0.2565 0.3030 0.0112  -0.0010 0.0173  1198 ILE B CD1 
17934 N N   . ALA B 1201 ? 0.3682 0.3251 0.3632 0.0197  -0.0026 0.0241  1199 ALA B N   
17935 C CA  . ALA B 1201 ? 0.4021 0.3560 0.3950 0.0223  -0.0037 0.0259  1199 ALA B CA  
17936 C C   . ALA B 1201 ? 0.3832 0.3426 0.3757 0.0245  -0.0039 0.0258  1199 ALA B C   
17937 O O   . ALA B 1201 ? 0.4377 0.3964 0.4298 0.0275  -0.0050 0.0258  1199 ALA B O   
17938 C CB  . ALA B 1201 ? 0.3858 0.3356 0.3765 0.0208  -0.0038 0.0292  1199 ALA B CB  
17939 N N   . ARG B 1202 ? 0.3908 0.3558 0.3835 0.0229  -0.0029 0.0257  1200 ARG B N   
17940 C CA  . ARG B 1202 ? 0.4156 0.3854 0.4073 0.0245  -0.0032 0.0260  1200 ARG B CA  
17941 C C   . ARG B 1202 ? 0.4230 0.3972 0.4168 0.0259  -0.0034 0.0231  1200 ARG B C   
17942 O O   . ARG B 1202 ? 0.4514 0.4283 0.4450 0.0282  -0.0043 0.0232  1200 ARG B O   
17943 C CB  . ARG B 1202 ? 0.4278 0.4014 0.4183 0.0221  -0.0021 0.0270  1200 ARG B CB  
17944 C CG  . ARG B 1202 ? 0.5489 0.5195 0.5368 0.0208  -0.0018 0.0302  1200 ARG B CG  
17945 C CD  . ARG B 1202 ? 0.6358 0.6106 0.6220 0.0190  -0.0006 0.0310  1200 ARG B CD  
17946 N NE  . ARG B 1202 ? 0.6272 0.6053 0.6155 0.0171  0.0009  0.0287  1200 ARG B NE  
17947 C CZ  . ARG B 1202 ? 0.5990 0.5764 0.5880 0.0145  0.0023  0.0291  1200 ARG B CZ  
17948 N NH1 . ARG B 1202 ? 0.5876 0.5610 0.5755 0.0132  0.0025  0.0317  1200 ARG B NH1 
17949 N NH2 . ARG B 1202 ? 0.5625 0.5434 0.5535 0.0132  0.0035  0.0270  1200 ARG B NH2 
17950 N N   . ASN B 1203 ? 0.3668 0.3420 0.3627 0.0246  -0.0026 0.0208  1201 ASN B N   
17951 C CA  . ASN B 1203 ? 0.3562 0.3362 0.3539 0.0252  -0.0025 0.0182  1201 ASN B CA  
17952 C C   . ASN B 1203 ? 0.3537 0.3315 0.3532 0.0264  -0.0028 0.0161  1201 ASN B C   
17953 O O   . ASN B 1203 ? 0.3343 0.3097 0.3348 0.0247  -0.0023 0.0151  1201 ASN B O   
17954 C CB  . ASN B 1203 ? 0.3781 0.3615 0.3764 0.0226  -0.0012 0.0172  1201 ASN B CB  
17955 C CG  . ASN B 1203 ? 0.3824 0.3704 0.3823 0.0230  -0.0010 0.0147  1201 ASN B CG  
17956 O OD1 . ASN B 1203 ? 0.4460 0.4355 0.4466 0.0250  -0.0018 0.0138  1201 ASN B OD1 
17957 N ND2 . ASN B 1203 ? 0.4215 0.4121 0.4221 0.0210  0.0001  0.0136  1201 ASN B ND2 
17958 N N   . PRO B 1204 ? 0.3735 0.3524 0.3736 0.0291  -0.0036 0.0153  1202 PRO B N   
17959 C CA  . PRO B 1204 ? 0.3937 0.3708 0.3953 0.0303  -0.0038 0.0132  1202 PRO B CA  
17960 C C   . PRO B 1204 ? 0.3574 0.3372 0.3607 0.0286  -0.0030 0.0107  1202 PRO B C   
17961 O O   . PRO B 1204 ? 0.3716 0.3491 0.3758 0.0288  -0.0029 0.0090  1202 PRO B O   
17962 C CB  . PRO B 1204 ? 0.4762 0.4557 0.4782 0.0336  -0.0046 0.0130  1202 PRO B CB  
17963 C CG  . PRO B 1204 ? 0.4803 0.4606 0.4806 0.0343  -0.0052 0.0156  1202 PRO B CG  
17964 C CD  . PRO B 1204 ? 0.4149 0.3968 0.4142 0.0313  -0.0045 0.0165  1202 PRO B CD  
17965 N N   . ASP B 1205 ? 0.3462 0.3307 0.3498 0.0270  -0.0023 0.0105  1203 ASP B N   
17966 C CA  . ASP B 1205 ? 0.3688 0.3559 0.3739 0.0254  -0.0016 0.0084  1203 ASP B CA  
17967 C C   . ASP B 1205 ? 0.3817 0.3682 0.3869 0.0226  -0.0007 0.0087  1203 ASP B C   
17968 O O   . ASP B 1205 ? 0.3666 0.3563 0.3727 0.0212  0.0000  0.0075  1203 ASP B O   
17969 C CB  . ASP B 1205 ? 0.4261 0.4190 0.4316 0.0258  -0.0015 0.0074  1203 ASP B CB  
17970 C CG  . ASP B 1205 ? 0.4672 0.4616 0.4734 0.0285  -0.0023 0.0068  1203 ASP B CG  
17971 O OD1 . ASP B 1205 ? 0.4231 0.4143 0.4298 0.0299  -0.0026 0.0062  1203 ASP B OD1 
17972 O OD2 . ASP B 1205 ? 0.5098 0.5086 0.5161 0.0291  -0.0026 0.0068  1203 ASP B OD2 
17973 N N   . ALA B 1206 ? 0.3275 0.3099 0.3317 0.0217  -0.0007 0.0105  1204 ALA B N   
17974 C CA  . ALA B 1206 ? 0.3326 0.3146 0.3373 0.0190  0.0003  0.0111  1204 ALA B CA  
17975 C C   . ALA B 1206 ? 0.2902 0.2726 0.2969 0.0178  0.0006  0.0089  1204 ALA B C   
17976 O O   . ALA B 1206 ? 0.3336 0.3187 0.3413 0.0160  0.0015  0.0085  1204 ALA B O   
17977 C CB  . ALA B 1206 ? 0.3474 0.3244 0.3510 0.0182  0.0000  0.0132  1204 ALA B CB  
17978 N N   . TYR B 1207 ? 0.2647 0.2446 0.2721 0.0189  -0.0002 0.0075  1205 TYR B N   
17979 C CA  . TYR B 1207 ? 0.2755 0.2562 0.2845 0.0181  0.0000  0.0052  1205 TYR B CA  
17980 C C   . TYR B 1207 ? 0.2661 0.2496 0.2754 0.0200  -0.0003 0.0035  1205 TYR B C   
17981 O O   . TYR B 1207 ? 0.3569 0.3395 0.3654 0.0223  -0.0009 0.0035  1205 TYR B O   
17982 C CB  . TYR B 1207 ? 0.2611 0.2365 0.2703 0.0176  -0.0007 0.0048  1205 TYR B CB  
17983 C CG  . TYR B 1207 ? 0.2437 0.2163 0.2529 0.0154  -0.0006 0.0066  1205 TYR B CG  
17984 C CD1 . TYR B 1207 ? 0.2450 0.2203 0.2557 0.0129  0.0003  0.0070  1205 TYR B CD1 
17985 C CD2 . TYR B 1207 ? 0.2474 0.2146 0.2552 0.0157  -0.0013 0.0080  1205 TYR B CD2 
17986 C CE1 . TYR B 1207 ? 0.2204 0.1935 0.2313 0.0107  0.0006  0.0087  1205 TYR B CE1 
17987 C CE2 . TYR B 1207 ? 0.2516 0.2160 0.2593 0.0134  -0.0011 0.0098  1205 TYR B CE2 
17988 C CZ  . TYR B 1207 ? 0.2369 0.2046 0.2463 0.0108  -0.0002 0.0102  1205 TYR B CZ  
17989 O OH  . TYR B 1207 ? 0.2470 0.2125 0.2566 0.0084  0.0001  0.0122  1205 TYR B OH  
17990 N N   . CYS B 1208 ? 0.2117 0.1990 0.2222 0.0192  0.0002  0.0020  1206 CYS B N   
17991 C CA  . CYS B 1208 ? 0.2021 0.1927 0.2130 0.0205  0.0001  0.0005  1206 CYS B CA  
17992 C C   . CYS B 1208 ? 0.2116 0.2005 0.2232 0.0209  -0.0002 -0.0015 1206 CYS B C   
17993 O O   . CYS B 1208 ? 0.2115 0.1997 0.2241 0.0193  -0.0001 -0.0023 1206 CYS B O   
17994 C CB  . CYS B 1208 ? 0.2479 0.2429 0.2593 0.0193  0.0008  0.0000  1206 CYS B CB  
17995 S SG  . CYS B 1208 ? 0.2811 0.2802 0.2928 0.0205  0.0006  -0.0017 1206 CYS B SG  
17996 N N   . LEU B 1209 ? 0.2042 0.1928 0.2154 0.0231  -0.0007 -0.0021 1207 LEU B N   
17997 C CA  . LEU B 1209 ? 0.1942 0.1813 0.2058 0.0237  -0.0009 -0.0040 1207 LEU B CA  
17998 C C   . LEU B 1209 ? 0.1892 0.1800 0.2018 0.0229  -0.0006 -0.0056 1207 LEU B C   
17999 O O   . LEU B 1209 ? 0.1945 0.1840 0.2072 0.0227  -0.0007 -0.0071 1207 LEU B O   
18000 C CB  . LEU B 1209 ? 0.1872 0.1731 0.1980 0.0265  -0.0013 -0.0042 1207 LEU B CB  
18001 C CG  . LEU B 1209 ? 0.2361 0.2178 0.2457 0.0277  -0.0018 -0.0026 1207 LEU B CG  
18002 C CD1 . LEU B 1209 ? 0.2456 0.2260 0.2546 0.0307  -0.0021 -0.0032 1207 LEU B CD1 
18003 C CD2 . LEU B 1209 ? 0.2511 0.2276 0.2601 0.0259  -0.0021 -0.0023 1207 LEU B CD2 
18004 N N   . ASN B 1210 ? 0.1962 0.1912 0.2091 0.0222  -0.0002 -0.0053 1208 ASN B N   
18005 C CA  . ASN B 1210 ? 0.2180 0.2160 0.2317 0.0214  0.0001  -0.0067 1208 ASN B CA  
18006 C C   . ASN B 1210 ? 0.2115 0.2080 0.2260 0.0196  0.0002  -0.0075 1208 ASN B C   
18007 O O   . ASN B 1210 ? 0.2381 0.2354 0.2530 0.0192  0.0002  -0.0089 1208 ASN B O   
18008 C CB  . ASN B 1210 ? 0.2710 0.2731 0.2848 0.0208  0.0005  -0.0062 1208 ASN B CB  
18009 C CG  . ASN B 1210 ? 0.2589 0.2634 0.2721 0.0224  0.0002  -0.0055 1208 ASN B CG  
18010 O OD1 . ASN B 1210 ? 0.3326 0.3358 0.3456 0.0242  -0.0002 -0.0052 1208 ASN B OD1 
18011 N ND2 . ASN B 1210 ? 0.3590 0.3668 0.3719 0.0218  0.0003  -0.0053 1208 ASN B ND2 
18012 N N   . TRP B 1211 ? 0.2027 0.1971 0.2174 0.0183  0.0003  -0.0064 1209 TRP B N   
18013 C CA  . TRP B 1211 ? 0.2012 0.1950 0.2170 0.0164  0.0003  -0.0068 1209 TRP B CA  
18014 C C   . TRP B 1211 ? 0.2230 0.2127 0.2388 0.0162  -0.0004 -0.0074 1209 TRP B C   
18015 O O   . TRP B 1211 ? 0.2391 0.2282 0.2559 0.0146  -0.0006 -0.0078 1209 TRP B O   
18016 C CB  . TRP B 1211 ? 0.2252 0.2196 0.2416 0.0150  0.0009  -0.0053 1209 TRP B CB  
18017 C CG  . TRP B 1211 ? 0.2244 0.2219 0.2400 0.0154  0.0016  -0.0045 1209 TRP B CG  
18018 C CD1 . TRP B 1211 ? 0.2469 0.2443 0.2616 0.0155  0.0019  -0.0028 1209 TRP B CD1 
18019 C CD2 . TRP B 1211 ? 0.2154 0.2163 0.2308 0.0158  0.0018  -0.0055 1209 TRP B CD2 
18020 N NE1 . TRP B 1211 ? 0.2577 0.2583 0.2715 0.0159  0.0023  -0.0027 1209 TRP B NE1 
18021 C CE2 . TRP B 1211 ? 0.2193 0.2221 0.2336 0.0160  0.0022  -0.0043 1209 TRP B CE2 
18022 C CE3 . TRP B 1211 ? 0.2299 0.2325 0.2458 0.0159  0.0016  -0.0071 1209 TRP B CE3 
18023 C CZ2 . TRP B 1211 ? 0.2502 0.2561 0.2639 0.0163  0.0023  -0.0049 1209 TRP B CZ2 
18024 C CZ3 . TRP B 1211 ? 0.2257 0.2313 0.2411 0.0161  0.0019  -0.0075 1209 TRP B CZ3 
18025 C CH2 . TRP B 1211 ? 0.2408 0.2480 0.2551 0.0163  0.0022  -0.0065 1209 TRP B CH2 
18026 N N   . LEU B 1212 ? 0.1992 0.1861 0.2137 0.0178  -0.0009 -0.0075 1210 LEU B N   
18027 C CA  . LEU B 1212 ? 0.1818 0.1641 0.1957 0.0177  -0.0016 -0.0081 1210 LEU B CA  
18028 C C   . LEU B 1212 ? 0.1882 0.1702 0.2013 0.0189  -0.0019 -0.0101 1210 LEU B C   
18029 O O   . LEU B 1212 ? 0.1941 0.1721 0.2063 0.0191  -0.0026 -0.0109 1210 LEU B O   
18030 C CB  . LEU B 1212 ? 0.1798 0.1582 0.1923 0.0188  -0.0019 -0.0069 1210 LEU B CB  
18031 C CG  . LEU B 1212 ? 0.1727 0.1503 0.1857 0.0171  -0.0017 -0.0049 1210 LEU B CG  
18032 C CD1 . LEU B 1212 ? 0.2298 0.2044 0.2414 0.0185  -0.0019 -0.0034 1210 LEU B CD1 
18033 C CD2 . LEU B 1212 ? 0.2123 0.1871 0.2261 0.0148  -0.0023 -0.0051 1210 LEU B CD2 
18034 N N   . VAL B 1213 ? 0.1857 0.1717 0.1992 0.0195  -0.0015 -0.0108 1211 VAL B N   
18035 C CA  . VAL B 1213 ? 0.1923 0.1788 0.2052 0.0202  -0.0016 -0.0126 1211 VAL B CA  
18036 C C   . VAL B 1213 ? 0.1758 0.1650 0.1899 0.0185  -0.0015 -0.0132 1211 VAL B C   
18037 O O   . VAL B 1213 ? 0.1942 0.1858 0.2095 0.0174  -0.0011 -0.0124 1211 VAL B O   
18038 C CB  . VAL B 1213 ? 0.1920 0.1809 0.2044 0.0225  -0.0011 -0.0129 1211 VAL B CB  
18039 C CG1 . VAL B 1213 ? 0.2158 0.2015 0.2270 0.0245  -0.0013 -0.0124 1211 VAL B CG1 
18040 C CG2 . VAL B 1213 ? 0.2045 0.1979 0.2179 0.0223  -0.0006 -0.0119 1211 VAL B CG2 
18041 N N   . GLU B 1214 ? 0.1814 0.1700 0.1949 0.0185  -0.0019 -0.0147 1212 GLU B N   
18042 C CA  . GLU B 1214 ? 0.2090 0.1999 0.2233 0.0172  -0.0019 -0.0154 1212 GLU B CA  
18043 C C   . GLU B 1214 ? 0.1772 0.1710 0.1908 0.0183  -0.0014 -0.0162 1212 GLU B C   
18044 O O   . GLU B 1214 ? 0.1879 0.1808 0.2002 0.0197  -0.0014 -0.0170 1212 GLU B O   
18045 C CB  . GLU B 1214 ? 0.2364 0.2246 0.2504 0.0160  -0.0028 -0.0163 1212 GLU B CB  
18046 C CG  . GLU B 1214 ? 0.2655 0.2562 0.2804 0.0148  -0.0030 -0.0168 1212 GLU B CG  
18047 C CD  . GLU B 1214 ? 0.3377 0.3261 0.3522 0.0137  -0.0041 -0.0178 1212 GLU B CD  
18048 O OE1 . GLU B 1214 ? 0.3488 0.3336 0.3627 0.0133  -0.0048 -0.0179 1212 GLU B OE1 
18049 O OE2 . GLU B 1214 ? 0.3841 0.3742 0.3986 0.0133  -0.0043 -0.0185 1212 GLU B OE2 
18050 N N   . GLU B 1215 ? 0.1700 0.1673 0.1846 0.0176  -0.0011 -0.0159 1213 GLU B N   
18051 C CA  . GLU B 1215 ? 0.1731 0.1732 0.1873 0.0181  -0.0007 -0.0166 1213 GLU B CA  
18052 C C   . GLU B 1215 ? 0.1663 0.1659 0.1799 0.0173  -0.0011 -0.0177 1213 GLU B C   
18053 O O   . GLU B 1215 ? 0.1763 0.1751 0.1907 0.0159  -0.0016 -0.0177 1213 GLU B O   
18054 C CB  . GLU B 1215 ? 0.1807 0.1841 0.1958 0.0174  -0.0003 -0.0159 1213 GLU B CB  
18055 C CG  . GLU B 1215 ? 0.1896 0.1940 0.2049 0.0179  0.0001  -0.0147 1213 GLU B CG  
18056 C CD  . GLU B 1215 ? 0.1823 0.1892 0.1982 0.0169  0.0004  -0.0142 1213 GLU B CD  
18057 O OE1 . GLU B 1215 ? 0.1899 0.1961 0.2065 0.0159  0.0004  -0.0138 1213 GLU B OE1 
18058 O OE2 . GLU B 1215 ? 0.1923 0.2019 0.2079 0.0172  0.0006  -0.0142 1213 GLU B OE2 
18059 N N   . VAL B 1216 ? 0.1694 0.1695 0.1818 0.0182  -0.0009 -0.0186 1214 VAL B N   
18060 C CA  . VAL B 1216 ? 0.1775 0.1775 0.1890 0.0175  -0.0013 -0.0195 1214 VAL B CA  
18061 C C   . VAL B 1216 ? 0.1675 0.1708 0.1787 0.0178  -0.0007 -0.0197 1214 VAL B C   
18062 O O   . VAL B 1216 ? 0.1839 0.1888 0.1948 0.0191  0.0000  -0.0196 1214 VAL B O   
18063 C CB  . VAL B 1216 ? 0.1854 0.1821 0.1952 0.0181  -0.0018 -0.0206 1214 VAL B CB  
18064 C CG1 . VAL B 1216 ? 0.2179 0.2147 0.2264 0.0173  -0.0021 -0.0215 1214 VAL B CG1 
18065 C CG2 . VAL B 1216 ? 0.2028 0.1960 0.2129 0.0174  -0.0026 -0.0204 1214 VAL B CG2 
18066 N N   . SER B 1217 ? 0.1545 0.1591 0.1660 0.0164  -0.0009 -0.0197 1215 SER B N   
18067 C CA  . SER B 1217 ? 0.1618 0.1691 0.1727 0.0162  -0.0004 -0.0198 1215 SER B CA  
18068 C C   . SER B 1217 ? 0.1700 0.1763 0.1794 0.0159  -0.0008 -0.0206 1215 SER B C   
18069 O O   . SER B 1217 ? 0.1780 0.1821 0.1872 0.0151  -0.0016 -0.0209 1215 SER B O   
18070 C CB  . SER B 1217 ? 0.1875 0.1964 0.1995 0.0149  -0.0005 -0.0192 1215 SER B CB  
18071 O OG  . SER B 1217 ? 0.2077 0.2183 0.2190 0.0142  -0.0004 -0.0193 1215 SER B OG  
18072 N N   . ALA B 1218 ? 0.1635 0.1715 0.1717 0.0165  -0.0002 -0.0210 1216 ALA B N   
18073 C CA  . ALA B 1218 ? 0.1691 0.1764 0.1755 0.0162  -0.0003 -0.0217 1216 ALA B CA  
18074 C C   . ALA B 1218 ? 0.1761 0.1866 0.1822 0.0156  0.0003  -0.0213 1216 ALA B C   
18075 O O   . ALA B 1218 ? 0.1983 0.2116 0.2049 0.0163  0.0011  -0.0210 1216 ALA B O   
18076 C CB  . ALA B 1218 ? 0.2008 0.2064 0.2053 0.0176  -0.0001 -0.0226 1216 ALA B CB  
18077 N N   . SER B 1219 ? 0.1654 0.1755 0.1707 0.0142  -0.0003 -0.0212 1217 SER B N   
18078 C CA  . SER B 1219 ? 0.1650 0.1777 0.1699 0.0133  0.0002  -0.0208 1217 SER B CA  
18079 C C   . SER B 1219 ? 0.1637 0.1755 0.1661 0.0131  0.0002  -0.0213 1217 SER B C   
18080 O O   . SER B 1219 ? 0.1720 0.1813 0.1734 0.0125  -0.0008 -0.0216 1217 SER B O   
18081 C CB  . SER B 1219 ? 0.1834 0.1959 0.1891 0.0118  -0.0005 -0.0202 1217 SER B CB  
18082 O OG  . SER B 1219 ? 0.1907 0.2052 0.1958 0.0108  -0.0002 -0.0197 1217 SER B OG  
18083 N N   . ILE B 1220 ? 0.1848 0.1991 0.1864 0.0137  0.0012  -0.0213 1218 ILE B N   
18084 C CA  . ILE B 1220 ? 0.1747 0.1886 0.1736 0.0137  0.0015  -0.0218 1218 ILE B CA  
18085 C C   . ILE B 1220 ? 0.1919 0.2084 0.1904 0.0123  0.0019  -0.0210 1218 ILE B C   
18086 O O   . ILE B 1220 ? 0.1915 0.2114 0.1913 0.0122  0.0028  -0.0204 1218 ILE B O   
18087 C CB  . ILE B 1220 ? 0.1976 0.2123 0.1957 0.0157  0.0026  -0.0226 1218 ILE B CB  
18088 C CG1 . ILE B 1220 ? 0.2462 0.2579 0.2447 0.0170  0.0021  -0.0233 1218 ILE B CG1 
18089 C CG2 . ILE B 1220 ? 0.2283 0.2426 0.2232 0.0158  0.0031  -0.0232 1218 ILE B CG2 
18090 C CD1 . ILE B 1220 ? 0.3675 0.3801 0.3659 0.0192  0.0033  -0.0239 1218 ILE B CD1 
18091 N N   . ASN B 1221 ? 0.1954 0.2102 0.1920 0.0111  0.0012  -0.0208 1219 ASN B N   
18092 C CA  . ASN B 1221 ? 0.1945 0.2112 0.1902 0.0096  0.0016  -0.0200 1219 ASN B CA  
18093 C C   . ASN B 1221 ? 0.2022 0.2209 0.1960 0.0103  0.0029  -0.0202 1219 ASN B C   
18094 O O   . ASN B 1221 ? 0.2209 0.2376 0.2120 0.0107  0.0028  -0.0209 1219 ASN B O   
18095 C CB  . ASN B 1221 ? 0.1996 0.2134 0.1938 0.0082  0.0003  -0.0197 1219 ASN B CB  
18096 C CG  . ASN B 1221 ? 0.2062 0.2211 0.1988 0.0066  0.0005  -0.0187 1219 ASN B CG  
18097 O OD1 . ASN B 1221 ? 0.2129 0.2311 0.2059 0.0062  0.0017  -0.0182 1219 ASN B OD1 
18098 N ND2 . ASN B 1221 ? 0.2405 0.2528 0.2314 0.0056  -0.0006 -0.0184 1219 ASN B ND2 
18099 N N   . THR B 1222 ? 0.1812 0.2040 0.1763 0.0104  0.0042  -0.0197 1220 THR B N   
18100 C CA  . THR B 1222 ? 0.2137 0.2391 0.2072 0.0113  0.0058  -0.0199 1220 THR B CA  
18101 C C   . THR B 1222 ? 0.2607 0.2879 0.2526 0.0095  0.0063  -0.0189 1220 THR B C   
18102 O O   . THR B 1222 ? 0.3132 0.3433 0.3040 0.0100  0.0077  -0.0189 1220 THR B O   
18103 C CB  . THR B 1222 ? 0.2247 0.2541 0.2207 0.0128  0.0070  -0.0199 1220 THR B CB  
18104 O OG1 . THR B 1222 ? 0.2486 0.2808 0.2471 0.0113  0.0069  -0.0187 1220 THR B OG1 
18105 C CG2 . THR B 1222 ? 0.2464 0.2736 0.2435 0.0148  0.0067  -0.0208 1220 THR B CG2 
18106 N N   . ALA B 1223 ? 0.2315 0.2570 0.2232 0.0074  0.0051  -0.0181 1221 ALA B N   
18107 C CA  . ALA B 1223 ? 0.2858 0.3117 0.2755 0.0055  0.0052  -0.0171 1221 ALA B CA  
18108 C C   . ALA B 1223 ? 0.3711 0.3930 0.3575 0.0053  0.0042  -0.0174 1221 ALA B C   
18109 O O   . ALA B 1223 ? 0.4246 0.4460 0.4088 0.0037  0.0040  -0.0165 1221 ALA B O   
18110 C CB  . ALA B 1223 ? 0.3095 0.3357 0.3007 0.0033  0.0044  -0.0159 1221 ALA B CB  
18111 N N   . ALA B 1224 ? 0.2650 0.2838 0.2509 0.0068  0.0034  -0.0187 1222 ALA B N   
18112 C CA  . ALA B 1224 ? 0.3246 0.3395 0.3078 0.0064  0.0020  -0.0190 1222 ALA B CA  
18113 C C   . ALA B 1224 ? 0.3187 0.3337 0.2980 0.0062  0.0027  -0.0189 1222 ALA B C   
18114 O O   . ALA B 1224 ? 0.3439 0.3561 0.3206 0.0053  0.0015  -0.0186 1222 ALA B O   
18115 C CB  . ALA B 1224 ? 0.3159 0.3278 0.2995 0.0078  0.0010  -0.0203 1222 ALA B CB  
18116 N N   . ALA B 1225 ? 0.3274 0.3456 0.3060 0.0071  0.0046  -0.0192 1223 ALA B N   
18117 C CA  . ALA B 1225 ? 0.3407 0.3593 0.3154 0.0070  0.0055  -0.0193 1223 ALA B CA  
18118 C C   . ALA B 1225 ? 0.3813 0.4018 0.3550 0.0048  0.0060  -0.0175 1223 ALA B C   
18119 O O   . ALA B 1225 ? 0.3936 0.4144 0.3638 0.0044  0.0067  -0.0172 1223 ALA B O   
18120 C CB  . ALA B 1225 ? 0.4215 0.4428 0.3956 0.0091  0.0076  -0.0203 1223 ALA B CB  
18121 N N   . GLY B 1226 ? 0.3291 0.3508 0.3057 0.0033  0.0056  -0.0163 1224 GLY B N   
18122 C CA  . GLY B 1226 ? 0.3531 0.3760 0.3288 0.0009  0.0058  -0.0145 1224 GLY B CA  
18123 C C   . GLY B 1226 ? 0.3940 0.4220 0.3724 0.0001  0.0072  -0.0135 1224 GLY B C   
18124 O O   . GLY B 1226 ? 0.3948 0.4239 0.3727 -0.0022 0.0074  -0.0120 1224 GLY B O   
18125 N N   . GLY B 1227 ? 0.3169 0.3479 0.2982 0.0017  0.0083  -0.0143 1225 GLY B N   
18126 C CA  . GLY B 1227 ? 0.3496 0.3856 0.3340 0.0009  0.0094  -0.0134 1225 GLY B CA  
18127 C C   . GLY B 1227 ? 0.3770 0.4148 0.3647 0.0031  0.0097  -0.0145 1225 GLY B C   
18128 O O   . GLY B 1227 ? 0.3466 0.3815 0.3339 0.0051  0.0092  -0.0159 1225 GLY B O   
18129 N N   . ASN B 1228 ? 0.3245 0.3671 0.3152 0.0026  0.0106  -0.0137 1226 ASN B N   
18130 C CA  . ASN B 1228 ? 0.3384 0.3832 0.3324 0.0044  0.0109  -0.0143 1226 ASN B CA  
18131 C C   . ASN B 1228 ? 0.3674 0.4179 0.3624 0.0060  0.0130  -0.0143 1226 ASN B C   
18132 O O   . ASN B 1228 ? 0.4216 0.4769 0.4177 0.0044  0.0140  -0.0130 1226 ASN B O   
18133 C CB  . ASN B 1228 ? 0.3348 0.3807 0.3317 0.0027  0.0098  -0.0134 1226 ASN B CB  
18134 C CG  . ASN B 1228 ? 0.3434 0.3908 0.3435 0.0045  0.0097  -0.0140 1226 ASN B CG  
18135 O OD1 . ASN B 1228 ? 0.3954 0.4454 0.3964 0.0069  0.0109  -0.0146 1226 ASN B OD1 
18136 N ND2 . ASN B 1228 ? 0.2805 0.3261 0.2820 0.0036  0.0083  -0.0138 1226 ASN B ND2 
18137 N N   . ALA B 1229 ? 0.3722 0.4222 0.3670 0.0090  0.0137  -0.0157 1227 ALA B N   
18138 C CA  . ALA B 1229 ? 0.3957 0.4507 0.3914 0.0110  0.0159  -0.0159 1227 ALA B CA  
18139 C C   . ALA B 1229 ? 0.3741 0.4348 0.3742 0.0109  0.0163  -0.0148 1227 ALA B C   
18140 O O   . ALA B 1229 ? 0.3383 0.4050 0.3399 0.0105  0.0179  -0.0138 1227 ALA B O   
18141 C CB  . ALA B 1229 ? 0.3740 0.4262 0.3685 0.0144  0.0162  -0.0177 1227 ALA B CB  
18142 N N   . SER B 1230 ? 0.4188 0.4781 0.4213 0.0111  0.0149  -0.0150 1228 SER B N   
18143 C CA  . SER B 1230 ? 0.3821 0.4466 0.3887 0.0114  0.0151  -0.0142 1228 SER B CA  
18144 C C   . SER B 1230 ? 0.4392 0.5078 0.4473 0.0081  0.0150  -0.0124 1228 SER B C   
18145 O O   . SER B 1230 ? 0.4667 0.5417 0.4777 0.0080  0.0159  -0.0114 1228 SER B O   
18146 C CB  . SER B 1230 ? 0.4336 0.4952 0.4418 0.0121  0.0135  -0.0147 1228 SER B CB  
18147 N N   . LEU B 1231 ? 0.3795 0.4446 0.3856 0.0052  0.0138  -0.0119 1229 LEU B N   
18148 C CA  . LEU B 1231 ? 0.4102 0.4782 0.4172 0.0019  0.0136  -0.0103 1229 LEU B CA  
18149 C C   . LEU B 1231 ? 0.4408 0.5129 0.4469 0.0008  0.0153  -0.0093 1229 LEU B C   
18150 O O   . LEU B 1231 ? 0.4268 0.5025 0.4341 -0.0020 0.0154  -0.0077 1229 LEU B O   
18151 C CB  . LEU B 1231 ? 0.4317 0.4941 0.4369 -0.0007 0.0116  -0.0101 1229 LEU B CB  
18152 C CG  . LEU B 1231 ? 0.3365 0.3961 0.3432 -0.0011 0.0098  -0.0104 1229 LEU B CG  
18153 C CD1 . LEU B 1231 ? 0.2884 0.3436 0.2932 -0.0039 0.0083  -0.0099 1229 LEU B CD1 
18154 C CD2 . LEU B 1231 ? 0.3841 0.4490 0.3944 -0.0014 0.0098  -0.0097 1229 LEU B CD2 
18155 N N   . MET B 1232 ? 0.4141 0.4857 0.4178 0.0029  0.0168  -0.0101 1230 MET B N   
18156 C CA  . MET B 1232 ? 0.3833 0.4595 0.3861 0.0023  0.0189  -0.0092 1230 MET B CA  
18157 C C   . MET B 1232 ? 0.4407 0.5253 0.4478 0.0028  0.0203  -0.0083 1230 MET B C   
18158 O O   . MET B 1232 ? 0.3833 0.4730 0.3911 0.0008  0.0215  -0.0067 1230 MET B O   
18159 C CB  . MET B 1232 ? 0.3722 0.4462 0.3715 0.0049  0.0202  -0.0106 1230 MET B CB  
18160 N N   . ALA B 1233 ? 0.4859 0.5720 0.4959 0.0054  0.0202  -0.0090 1231 ALA B N   
18161 C CA  . ALA B 1233 ? 0.5204 0.6146 0.5349 0.0061  0.0213  -0.0081 1231 ALA B CA  
18162 C C   . ALA B 1233 ? 0.4963 0.5930 0.5139 0.0029  0.0197  -0.0066 1231 ALA B C   
18163 O O   . ALA B 1233 ? 0.5236 0.6273 0.5452 0.0030  0.0203  -0.0056 1231 ALA B O   
18164 C CB  . ALA B 1233 ? 0.5163 0.6109 0.5325 0.0103  0.0217  -0.0094 1231 ALA B CB  
18165 N N   . ILE B 1234 ? 0.4393 0.5306 0.4552 0.0002  0.0177  -0.0065 1232 ILE B N   
18166 C CA  . ILE B 1234 ? 0.4678 0.5602 0.4859 -0.0027 0.0159  -0.0054 1232 ILE B CA  
18167 C C   . ILE B 1234 ? 0.4396 0.5331 0.4567 -0.0068 0.0160  -0.0038 1232 ILE B C   
18168 O O   . ILE B 1234 ? 0.3844 0.4721 0.3980 -0.0086 0.0151  -0.0038 1232 ILE B O   
18169 C CB  . ILE B 1234 ? 0.4246 0.5101 0.4416 -0.0027 0.0137  -0.0064 1232 ILE B CB  
18170 C CG1 . ILE B 1234 ? 0.4542 0.5395 0.4728 0.0011  0.0137  -0.0077 1232 ILE B CG1 
18171 C CG2 . ILE B 1234 ? 0.3538 0.4396 0.3722 -0.0060 0.0119  -0.0054 1232 ILE B CG2 
18172 C CD1 . ILE B 1234 ? 0.4070 0.4888 0.4262 0.0008  0.0117  -0.0081 1232 ILE B CD1 
18173 N N   . GLY B 1235 ? 0.4240 0.5252 0.4442 -0.0083 0.0169  -0.0022 1233 GLY B N   
18174 C CA  . GLY B 1235 ? 0.3734 0.4764 0.3933 -0.0126 0.0168  -0.0004 1233 GLY B CA  
18175 C C   . GLY B 1235 ? 0.3355 0.4434 0.3594 -0.0149 0.0156  0.0008  1233 GLY B C   
18176 O O   . GLY B 1235 ? 0.4777 0.5913 0.5053 -0.0130 0.0159  0.0008  1233 GLY B O   
18177 O OXT . GLY B 1235 ? 0.2067 0.3128 0.2300 -0.0188 0.0141  0.0018  1233 GLY B OXT 
# 
