data_8QYC
# 
_entry.id   8QYC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8QYC         pdb_00008qyc 10.2210/pdb8qyc/pdb 
WWPDB D_1292134307 ?            ?                   
EMDB  EMD-18750    ?            ?                   
# 
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 2024-11-06 
2 'Structure model' 1 1 2025-02-12 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' em_admin        
# 
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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QYC 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Zorya anti-bacteriophage defense system ZorD in complex with ATP-gamma-S' 
_pdbx_database_related.db_id          EMD-18750 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              nicholas.taylor@cpr.ku.dk 
_pdbx_contact_author.name_first         Nicholas 
_pdbx_contact_author.name_last          Taylor 
_pdbx_contact_author.name_mi            'M. I.' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0761-4921 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Hu, H.'         1 ? 
'Taylor, N.M.I.' 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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure and mechanism of the Zorya anti-phage defense system.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-024-08493-8 
_citation.pdbx_database_id_PubMed   39662505 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hu, H.'          1  0000-0001-7774-9157 
primary 'Popp, P.F.'      2  0000-0002-7825-1550 
primary 'Hughes, T.C.D.'  3  0009-0005-6057-4852 
primary 'Roa-Eguiara, A.' 4  0000-0003-3962-7583 
primary 'Rutbeek, N.R.'   5  0000-0002-6851-8223 
primary 'Martin, F.J.O.'  6  0000-0001-6456-2860 
primary 'Hendriks, I.A.'  7  0000-0002-1439-3701 
primary 'Payne, L.J.'     8  0000-0003-2305-6827 
primary 'Yan, Y.'         9  ?                   
primary 'Humolli, D.'     10 0009-0002-1819-6155 
primary 'Klein-Sousa, V.' 11 0000-0002-0430-4330 
primary 'Songailiene, I.' 12 ?                   
primary 'Wang, Y.'        13 0000-0001-9156-0377 
primary 'Nielsen, M.L.'   14 0000-0002-0067-9039 
primary 'Berry, R.M.'     15 0000-0002-0331-473X 
primary 'Harms, A.'       16 0000-0003-2106-1286 
primary 'Erhardt, M.'     17 0000-0001-6292-619X 
primary 'Jackson, S.A.'   18 0000-0002-4512-3093 
primary 'Taylor, N.M.I.'  19 0000-0003-0761-4921 
# 
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 'DEAD/DEAH box helicase'                     122880.039 1 ? ? ? ? 
2 non-polymer syn 'PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER' 523.247    1 ? ? ? ? 
# 
_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       
;MLKRLLSKLTGNRQQIEHHLKNQYQVEENGLSFPLSLVDDSQLWALASWLEQLAEEDYLISLTDRWLLSWEALYRLLEDE
EHASSLPLIGVPDILPLRASLSSRGALSDSDFRVWIAEWATFPARKPIRFSRTGAILTHDNQQYLLSRENWALLQATEQL
SAQQIQTPGETTNQLGWAAIRKCAKLAAAKFDDYLEKTHVIKPTSLSLRLRKATVADTAVIEIEPHFEDQPANWLGSFDK
NLQVHDSYRIPGENGELSHVIIPPEVKEVLNSIHSIPGRRVAGSEALSFVRNPYTFLGEDAASVIAPEEHEQALFDARIF
FHHFRLIPQLNTENKITEVTLILEPVSPVPQPEITFVFSAPWELDKFIQQLGISVAAQMPAGSWQGYELELSQFTEQQWH
DCQALLTRWQQEIEGKEFSDVLDIAKYGDRVIGIGEFEKISSPWLTKAQSENWLPDGIDFSAFSIETLSGWQPENPLHFD
ELQEIITQAEAAGETYITTPWNDSQLPLDAAKTFSKNWEKQQITANEYQGNVADKTARAVLKIEQNIEETAYIKQRRNSL
LNARHAEPEIPLSLKEHIRLKDHQREGVAWLQQLFLRSPEETAGCLLADDMGLGKTLQILSFLVWFIEKFPQEPPNLIVA
PVSLLDNWERELNNFFYTAGIPVLKLYGETIKAVKYPKQAIPAHLQSKGIKNLLKPGWQGEAKIILTTYETLRDQEFSLA
RQPWSIMVCDEAQKIKNPAALITHAANAVQARFKVACTGTPVENTLVDLWSLFDFAQPGLLGALNEFGKQYVRPIENEDG
RDTERLESLRALIEPQTLRRTKEEVARDLPQKIEVESCKQLTLSGVQKQLYLSSVANWQQQQALREGMQQAGTGMLGLLH
RLKLICAHPAIVNPEPRFRDNSPKLNWLLKILAEIKHTSKDKVIIFTELRDLQRELQHAIHQNFGFRPVIINGDSSTKSQ
SQNSRQRLIDDFQAQPGFGVIILSTVAVGFGVNVQKANHVIHFTRCWNPAKEDQATDRAYRIGQTKNVYVYYPTVRDTEI
TTFEETLDDLLQRRRALARDMLCATPDLNCADFETILKGA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLKRLLSKLTGNRQQIEHHLKNQYQVEENGLSFPLSLVDDSQLWALASWLEQLAEEDYLISLTDRWLLSWEALYRLLEDE
EHASSLPLIGVPDILPLRASLSSRGALSDSDFRVWIAEWATFPARKPIRFSRTGAILTHDNQQYLLSRENWALLQATEQL
SAQQIQTPGETTNQLGWAAIRKCAKLAAAKFDDYLEKTHVIKPTSLSLRLRKATVADTAVIEIEPHFEDQPANWLGSFDK
NLQVHDSYRIPGENGELSHVIIPPEVKEVLNSIHSIPGRRVAGSEALSFVRNPYTFLGEDAASVIAPEEHEQALFDARIF
FHHFRLIPQLNTENKITEVTLILEPVSPVPQPEITFVFSAPWELDKFIQQLGISVAAQMPAGSWQGYELELSQFTEQQWH
DCQALLTRWQQEIEGKEFSDVLDIAKYGDRVIGIGEFEKISSPWLTKAQSENWLPDGIDFSAFSIETLSGWQPENPLHFD
ELQEIITQAEAAGETYITTPWNDSQLPLDAAKTFSKNWEKQQITANEYQGNVADKTARAVLKIEQNIEETAYIKQRRNSL
LNARHAEPEIPLSLKEHIRLKDHQREGVAWLQQLFLRSPEETAGCLLADDMGLGKTLQILSFLVWFIEKFPQEPPNLIVA
PVSLLDNWERELNNFFYTAGIPVLKLYGETIKAVKYPKQAIPAHLQSKGIKNLLKPGWQGEAKIILTTYETLRDQEFSLA
RQPWSIMVCDEAQKIKNPAALITHAANAVQARFKVACTGTPVENTLVDLWSLFDFAQPGLLGALNEFGKQYVRPIENEDG
RDTERLESLRALIEPQTLRRTKEEVARDLPQKIEVESCKQLTLSGVQKQLYLSSVANWQQQQALREGMQQAGTGMLGLLH
RLKLICAHPAIVNPEPRFRDNSPKLNWLLKILAEIKHTSKDKVIIFTELRDLQRELQHAIHQNFGFRPVIINGDSSTKSQ
SQNSRQRLIDDFQAQPGFGVIILSTVAVGFGVNVQKANHVIHFTRCWNPAKEDQATDRAYRIGQTKNVYVYYPTVRDTEI
TTFEETLDDLLQRRRALARDMLCATPDLNCADFETILKGA
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER' 
_pdbx_entity_nonpoly.comp_id     AGS 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    LEU n 
1 3    LYS n 
1 4    ARG n 
1 5    LEU n 
1 6    LEU n 
1 7    SER n 
1 8    LYS n 
1 9    LEU n 
1 10   THR n 
1 11   GLY n 
1 12   ASN n 
1 13   ARG n 
1 14   GLN n 
1 15   GLN n 
1 16   ILE n 
1 17   GLU n 
1 18   HIS n 
1 19   HIS n 
1 20   LEU n 
1 21   LYS n 
1 22   ASN n 
1 23   GLN n 
1 24   TYR n 
1 25   GLN n 
1 26   VAL n 
1 27   GLU n 
1 28   GLU n 
1 29   ASN n 
1 30   GLY n 
1 31   LEU n 
1 32   SER n 
1 33   PHE n 
1 34   PRO n 
1 35   LEU n 
1 36   SER n 
1 37   LEU n 
1 38   VAL n 
1 39   ASP n 
1 40   ASP n 
1 41   SER n 
1 42   GLN n 
1 43   LEU n 
1 44   TRP n 
1 45   ALA n 
1 46   LEU n 
1 47   ALA n 
1 48   SER n 
1 49   TRP n 
1 50   LEU n 
1 51   GLU n 
1 52   GLN n 
1 53   LEU n 
1 54   ALA n 
1 55   GLU n 
1 56   GLU n 
1 57   ASP n 
1 58   TYR n 
1 59   LEU n 
1 60   ILE n 
1 61   SER n 
1 62   LEU n 
1 63   THR n 
1 64   ASP n 
1 65   ARG n 
1 66   TRP n 
1 67   LEU n 
1 68   LEU n 
1 69   SER n 
1 70   TRP n 
1 71   GLU n 
1 72   ALA n 
1 73   LEU n 
1 74   TYR n 
1 75   ARG n 
1 76   LEU n 
1 77   LEU n 
1 78   GLU n 
1 79   ASP n 
1 80   GLU n 
1 81   GLU n 
1 82   HIS n 
1 83   ALA n 
1 84   SER n 
1 85   SER n 
1 86   LEU n 
1 87   PRO n 
1 88   LEU n 
1 89   ILE n 
1 90   GLY n 
1 91   VAL n 
1 92   PRO n 
1 93   ASP n 
1 94   ILE n 
1 95   LEU n 
1 96   PRO n 
1 97   LEU n 
1 98   ARG n 
1 99   ALA n 
1 100  SER n 
1 101  LEU n 
1 102  SER n 
1 103  SER n 
1 104  ARG n 
1 105  GLY n 
1 106  ALA n 
1 107  LEU n 
1 108  SER n 
1 109  ASP n 
1 110  SER n 
1 111  ASP n 
1 112  PHE n 
1 113  ARG n 
1 114  VAL n 
1 115  TRP n 
1 116  ILE n 
1 117  ALA n 
1 118  GLU n 
1 119  TRP n 
1 120  ALA n 
1 121  THR n 
1 122  PHE n 
1 123  PRO n 
1 124  ALA n 
1 125  ARG n 
1 126  LYS n 
1 127  PRO n 
1 128  ILE n 
1 129  ARG n 
1 130  PHE n 
1 131  SER n 
1 132  ARG n 
1 133  THR n 
1 134  GLY n 
1 135  ALA n 
1 136  ILE n 
1 137  LEU n 
1 138  THR n 
1 139  HIS n 
1 140  ASP n 
1 141  ASN n 
1 142  GLN n 
1 143  GLN n 
1 144  TYR n 
1 145  LEU n 
1 146  LEU n 
1 147  SER n 
1 148  ARG n 
1 149  GLU n 
1 150  ASN n 
1 151  TRP n 
1 152  ALA n 
1 153  LEU n 
1 154  LEU n 
1 155  GLN n 
1 156  ALA n 
1 157  THR n 
1 158  GLU n 
1 159  GLN n 
1 160  LEU n 
1 161  SER n 
1 162  ALA n 
1 163  GLN n 
1 164  GLN n 
1 165  ILE n 
1 166  GLN n 
1 167  THR n 
1 168  PRO n 
1 169  GLY n 
1 170  GLU n 
1 171  THR n 
1 172  THR n 
1 173  ASN n 
1 174  GLN n 
1 175  LEU n 
1 176  GLY n 
1 177  TRP n 
1 178  ALA n 
1 179  ALA n 
1 180  ILE n 
1 181  ARG n 
1 182  LYS n 
1 183  CYS n 
1 184  ALA n 
1 185  LYS n 
1 186  LEU n 
1 187  ALA n 
1 188  ALA n 
1 189  ALA n 
1 190  LYS n 
1 191  PHE n 
1 192  ASP n 
1 193  ASP n 
1 194  TYR n 
1 195  LEU n 
1 196  GLU n 
1 197  LYS n 
1 198  THR n 
1 199  HIS n 
1 200  VAL n 
1 201  ILE n 
1 202  LYS n 
1 203  PRO n 
1 204  THR n 
1 205  SER n 
1 206  LEU n 
1 207  SER n 
1 208  LEU n 
1 209  ARG n 
1 210  LEU n 
1 211  ARG n 
1 212  LYS n 
1 213  ALA n 
1 214  THR n 
1 215  VAL n 
1 216  ALA n 
1 217  ASP n 
1 218  THR n 
1 219  ALA n 
1 220  VAL n 
1 221  ILE n 
1 222  GLU n 
1 223  ILE n 
1 224  GLU n 
1 225  PRO n 
1 226  HIS n 
1 227  PHE n 
1 228  GLU n 
1 229  ASP n 
1 230  GLN n 
1 231  PRO n 
1 232  ALA n 
1 233  ASN n 
1 234  TRP n 
1 235  LEU n 
1 236  GLY n 
1 237  SER n 
1 238  PHE n 
1 239  ASP n 
1 240  LYS n 
1 241  ASN n 
1 242  LEU n 
1 243  GLN n 
1 244  VAL n 
1 245  HIS n 
1 246  ASP n 
1 247  SER n 
1 248  TYR n 
1 249  ARG n 
1 250  ILE n 
1 251  PRO n 
1 252  GLY n 
1 253  GLU n 
1 254  ASN n 
1 255  GLY n 
1 256  GLU n 
1 257  LEU n 
1 258  SER n 
1 259  HIS n 
1 260  VAL n 
1 261  ILE n 
1 262  ILE n 
1 263  PRO n 
1 264  PRO n 
1 265  GLU n 
1 266  VAL n 
1 267  LYS n 
1 268  GLU n 
1 269  VAL n 
1 270  LEU n 
1 271  ASN n 
1 272  SER n 
1 273  ILE n 
1 274  HIS n 
1 275  SER n 
1 276  ILE n 
1 277  PRO n 
1 278  GLY n 
1 279  ARG n 
1 280  ARG n 
1 281  VAL n 
1 282  ALA n 
1 283  GLY n 
1 284  SER n 
1 285  GLU n 
1 286  ALA n 
1 287  LEU n 
1 288  SER n 
1 289  PHE n 
1 290  VAL n 
1 291  ARG n 
1 292  ASN n 
1 293  PRO n 
1 294  TYR n 
1 295  THR n 
1 296  PHE n 
1 297  LEU n 
1 298  GLY n 
1 299  GLU n 
1 300  ASP n 
1 301  ALA n 
1 302  ALA n 
1 303  SER n 
1 304  VAL n 
1 305  ILE n 
1 306  ALA n 
1 307  PRO n 
1 308  GLU n 
1 309  GLU n 
1 310  HIS n 
1 311  GLU n 
1 312  GLN n 
1 313  ALA n 
1 314  LEU n 
1 315  PHE n 
1 316  ASP n 
1 317  ALA n 
1 318  ARG n 
1 319  ILE n 
1 320  PHE n 
1 321  PHE n 
1 322  HIS n 
1 323  HIS n 
1 324  PHE n 
1 325  ARG n 
1 326  LEU n 
1 327  ILE n 
1 328  PRO n 
1 329  GLN n 
1 330  LEU n 
1 331  ASN n 
1 332  THR n 
1 333  GLU n 
1 334  ASN n 
1 335  LYS n 
1 336  ILE n 
1 337  THR n 
1 338  GLU n 
1 339  VAL n 
1 340  THR n 
1 341  LEU n 
1 342  ILE n 
1 343  LEU n 
1 344  GLU n 
1 345  PRO n 
1 346  VAL n 
1 347  SER n 
1 348  PRO n 
1 349  VAL n 
1 350  PRO n 
1 351  GLN n 
1 352  PRO n 
1 353  GLU n 
1 354  ILE n 
1 355  THR n 
1 356  PHE n 
1 357  VAL n 
1 358  PHE n 
1 359  SER n 
1 360  ALA n 
1 361  PRO n 
1 362  TRP n 
1 363  GLU n 
1 364  LEU n 
1 365  ASP n 
1 366  LYS n 
1 367  PHE n 
1 368  ILE n 
1 369  GLN n 
1 370  GLN n 
1 371  LEU n 
1 372  GLY n 
1 373  ILE n 
1 374  SER n 
1 375  VAL n 
1 376  ALA n 
1 377  ALA n 
1 378  GLN n 
1 379  MET n 
1 380  PRO n 
1 381  ALA n 
1 382  GLY n 
1 383  SER n 
1 384  TRP n 
1 385  GLN n 
1 386  GLY n 
1 387  TYR n 
1 388  GLU n 
1 389  LEU n 
1 390  GLU n 
1 391  LEU n 
1 392  SER n 
1 393  GLN n 
1 394  PHE n 
1 395  THR n 
1 396  GLU n 
1 397  GLN n 
1 398  GLN n 
1 399  TRP n 
1 400  HIS n 
1 401  ASP n 
1 402  CYS n 
1 403  GLN n 
1 404  ALA n 
1 405  LEU n 
1 406  LEU n 
1 407  THR n 
1 408  ARG n 
1 409  TRP n 
1 410  GLN n 
1 411  GLN n 
1 412  GLU n 
1 413  ILE n 
1 414  GLU n 
1 415  GLY n 
1 416  LYS n 
1 417  GLU n 
1 418  PHE n 
1 419  SER n 
1 420  ASP n 
1 421  VAL n 
1 422  LEU n 
1 423  ASP n 
1 424  ILE n 
1 425  ALA n 
1 426  LYS n 
1 427  TYR n 
1 428  GLY n 
1 429  ASP n 
1 430  ARG n 
1 431  VAL n 
1 432  ILE n 
1 433  GLY n 
1 434  ILE n 
1 435  GLY n 
1 436  GLU n 
1 437  PHE n 
1 438  GLU n 
1 439  LYS n 
1 440  ILE n 
1 441  SER n 
1 442  SER n 
1 443  PRO n 
1 444  TRP n 
1 445  LEU n 
1 446  THR n 
1 447  LYS n 
1 448  ALA n 
1 449  GLN n 
1 450  SER n 
1 451  GLU n 
1 452  ASN n 
1 453  TRP n 
1 454  LEU n 
1 455  PRO n 
1 456  ASP n 
1 457  GLY n 
1 458  ILE n 
1 459  ASP n 
1 460  PHE n 
1 461  SER n 
1 462  ALA n 
1 463  PHE n 
1 464  SER n 
1 465  ILE n 
1 466  GLU n 
1 467  THR n 
1 468  LEU n 
1 469  SER n 
1 470  GLY n 
1 471  TRP n 
1 472  GLN n 
1 473  PRO n 
1 474  GLU n 
1 475  ASN n 
1 476  PRO n 
1 477  LEU n 
1 478  HIS n 
1 479  PHE n 
1 480  ASP n 
1 481  GLU n 
1 482  LEU n 
1 483  GLN n 
1 484  GLU n 
1 485  ILE n 
1 486  ILE n 
1 487  THR n 
1 488  GLN n 
1 489  ALA n 
1 490  GLU n 
1 491  ALA n 
1 492  ALA n 
1 493  GLY n 
1 494  GLU n 
1 495  THR n 
1 496  TYR n 
1 497  ILE n 
1 498  THR n 
1 499  THR n 
1 500  PRO n 
1 501  TRP n 
1 502  ASN n 
1 503  ASP n 
1 504  SER n 
1 505  GLN n 
1 506  LEU n 
1 507  PRO n 
1 508  LEU n 
1 509  ASP n 
1 510  ALA n 
1 511  ALA n 
1 512  LYS n 
1 513  THR n 
1 514  PHE n 
1 515  SER n 
1 516  LYS n 
1 517  ASN n 
1 518  TRP n 
1 519  GLU n 
1 520  LYS n 
1 521  GLN n 
1 522  GLN n 
1 523  ILE n 
1 524  THR n 
1 525  ALA n 
1 526  ASN n 
1 527  GLU n 
1 528  TYR n 
1 529  GLN n 
1 530  GLY n 
1 531  ASN n 
1 532  VAL n 
1 533  ALA n 
1 534  ASP n 
1 535  LYS n 
1 536  THR n 
1 537  ALA n 
1 538  ARG n 
1 539  ALA n 
1 540  VAL n 
1 541  LEU n 
1 542  LYS n 
1 543  ILE n 
1 544  GLU n 
1 545  GLN n 
1 546  ASN n 
1 547  ILE n 
1 548  GLU n 
1 549  GLU n 
1 550  THR n 
1 551  ALA n 
1 552  TYR n 
1 553  ILE n 
1 554  LYS n 
1 555  GLN n 
1 556  ARG n 
1 557  ARG n 
1 558  ASN n 
1 559  SER n 
1 560  LEU n 
1 561  LEU n 
1 562  ASN n 
1 563  ALA n 
1 564  ARG n 
1 565  HIS n 
1 566  ALA n 
1 567  GLU n 
1 568  PRO n 
1 569  GLU n 
1 570  ILE n 
1 571  PRO n 
1 572  LEU n 
1 573  SER n 
1 574  LEU n 
1 575  LYS n 
1 576  GLU n 
1 577  HIS n 
1 578  ILE n 
1 579  ARG n 
1 580  LEU n 
1 581  LYS n 
1 582  ASP n 
1 583  HIS n 
1 584  GLN n 
1 585  ARG n 
1 586  GLU n 
1 587  GLY n 
1 588  VAL n 
1 589  ALA n 
1 590  TRP n 
1 591  LEU n 
1 592  GLN n 
1 593  GLN n 
1 594  LEU n 
1 595  PHE n 
1 596  LEU n 
1 597  ARG n 
1 598  SER n 
1 599  PRO n 
1 600  GLU n 
1 601  GLU n 
1 602  THR n 
1 603  ALA n 
1 604  GLY n 
1 605  CYS n 
1 606  LEU n 
1 607  LEU n 
1 608  ALA n 
1 609  ASP n 
1 610  ASP n 
1 611  MET n 
1 612  GLY n 
1 613  LEU n 
1 614  GLY n 
1 615  LYS n 
1 616  THR n 
1 617  LEU n 
1 618  GLN n 
1 619  ILE n 
1 620  LEU n 
1 621  SER n 
1 622  PHE n 
1 623  LEU n 
1 624  VAL n 
1 625  TRP n 
1 626  PHE n 
1 627  ILE n 
1 628  GLU n 
1 629  LYS n 
1 630  PHE n 
1 631  PRO n 
1 632  GLN n 
1 633  GLU n 
1 634  PRO n 
1 635  PRO n 
1 636  ASN n 
1 637  LEU n 
1 638  ILE n 
1 639  VAL n 
1 640  ALA n 
1 641  PRO n 
1 642  VAL n 
1 643  SER n 
1 644  LEU n 
1 645  LEU n 
1 646  ASP n 
1 647  ASN n 
1 648  TRP n 
1 649  GLU n 
1 650  ARG n 
1 651  GLU n 
1 652  LEU n 
1 653  ASN n 
1 654  ASN n 
1 655  PHE n 
1 656  PHE n 
1 657  TYR n 
1 658  THR n 
1 659  ALA n 
1 660  GLY n 
1 661  ILE n 
1 662  PRO n 
1 663  VAL n 
1 664  LEU n 
1 665  LYS n 
1 666  LEU n 
1 667  TYR n 
1 668  GLY n 
1 669  GLU n 
1 670  THR n 
1 671  ILE n 
1 672  LYS n 
1 673  ALA n 
1 674  VAL n 
1 675  LYS n 
1 676  TYR n 
1 677  PRO n 
1 678  LYS n 
1 679  GLN n 
1 680  ALA n 
1 681  ILE n 
1 682  PRO n 
1 683  ALA n 
1 684  HIS n 
1 685  LEU n 
1 686  GLN n 
1 687  SER n 
1 688  LYS n 
1 689  GLY n 
1 690  ILE n 
1 691  LYS n 
1 692  ASN n 
1 693  LEU n 
1 694  LEU n 
1 695  LYS n 
1 696  PRO n 
1 697  GLY n 
1 698  TRP n 
1 699  GLN n 
1 700  GLY n 
1 701  GLU n 
1 702  ALA n 
1 703  LYS n 
1 704  ILE n 
1 705  ILE n 
1 706  LEU n 
1 707  THR n 
1 708  THR n 
1 709  TYR n 
1 710  GLU n 
1 711  THR n 
1 712  LEU n 
1 713  ARG n 
1 714  ASP n 
1 715  GLN n 
1 716  GLU n 
1 717  PHE n 
1 718  SER n 
1 719  LEU n 
1 720  ALA n 
1 721  ARG n 
1 722  GLN n 
1 723  PRO n 
1 724  TRP n 
1 725  SER n 
1 726  ILE n 
1 727  MET n 
1 728  VAL n 
1 729  CYS n 
1 730  ASP n 
1 731  GLU n 
1 732  ALA n 
1 733  GLN n 
1 734  LYS n 
1 735  ILE n 
1 736  LYS n 
1 737  ASN n 
1 738  PRO n 
1 739  ALA n 
1 740  ALA n 
1 741  LEU n 
1 742  ILE n 
1 743  THR n 
1 744  HIS n 
1 745  ALA n 
1 746  ALA n 
1 747  ASN n 
1 748  ALA n 
1 749  VAL n 
1 750  GLN n 
1 751  ALA n 
1 752  ARG n 
1 753  PHE n 
1 754  LYS n 
1 755  VAL n 
1 756  ALA n 
1 757  CYS n 
1 758  THR n 
1 759  GLY n 
1 760  THR n 
1 761  PRO n 
1 762  VAL n 
1 763  GLU n 
1 764  ASN n 
1 765  THR n 
1 766  LEU n 
1 767  VAL n 
1 768  ASP n 
1 769  LEU n 
1 770  TRP n 
1 771  SER n 
1 772  LEU n 
1 773  PHE n 
1 774  ASP n 
1 775  PHE n 
1 776  ALA n 
1 777  GLN n 
1 778  PRO n 
1 779  GLY n 
1 780  LEU n 
1 781  LEU n 
1 782  GLY n 
1 783  ALA n 
1 784  LEU n 
1 785  ASN n 
1 786  GLU n 
1 787  PHE n 
1 788  GLY n 
1 789  LYS n 
1 790  GLN n 
1 791  TYR n 
1 792  VAL n 
1 793  ARG n 
1 794  PRO n 
1 795  ILE n 
1 796  GLU n 
1 797  ASN n 
1 798  GLU n 
1 799  ASP n 
1 800  GLY n 
1 801  ARG n 
1 802  ASP n 
1 803  THR n 
1 804  GLU n 
1 805  ARG n 
1 806  LEU n 
1 807  GLU n 
1 808  SER n 
1 809  LEU n 
1 810  ARG n 
1 811  ALA n 
1 812  LEU n 
1 813  ILE n 
1 814  GLU n 
1 815  PRO n 
1 816  GLN n 
1 817  THR n 
1 818  LEU n 
1 819  ARG n 
1 820  ARG n 
1 821  THR n 
1 822  LYS n 
1 823  GLU n 
1 824  GLU n 
1 825  VAL n 
1 826  ALA n 
1 827  ARG n 
1 828  ASP n 
1 829  LEU n 
1 830  PRO n 
1 831  GLN n 
1 832  LYS n 
1 833  ILE n 
1 834  GLU n 
1 835  VAL n 
1 836  GLU n 
1 837  SER n 
1 838  CYS n 
1 839  LYS n 
1 840  GLN n 
1 841  LEU n 
1 842  THR n 
1 843  LEU n 
1 844  SER n 
1 845  GLY n 
1 846  VAL n 
1 847  GLN n 
1 848  LYS n 
1 849  GLN n 
1 850  LEU n 
1 851  TYR n 
1 852  LEU n 
1 853  SER n 
1 854  SER n 
1 855  VAL n 
1 856  ALA n 
1 857  ASN n 
1 858  TRP n 
1 859  GLN n 
1 860  GLN n 
1 861  GLN n 
1 862  GLN n 
1 863  ALA n 
1 864  LEU n 
1 865  ARG n 
1 866  GLU n 
1 867  GLY n 
1 868  MET n 
1 869  GLN n 
1 870  GLN n 
1 871  ALA n 
1 872  GLY n 
1 873  THR n 
1 874  GLY n 
1 875  MET n 
1 876  LEU n 
1 877  GLY n 
1 878  LEU n 
1 879  LEU n 
1 880  HIS n 
1 881  ARG n 
1 882  LEU n 
1 883  LYS n 
1 884  LEU n 
1 885  ILE n 
1 886  CYS n 
1 887  ALA n 
1 888  HIS n 
1 889  PRO n 
1 890  ALA n 
1 891  ILE n 
1 892  VAL n 
1 893  ASN n 
1 894  PRO n 
1 895  GLU n 
1 896  PRO n 
1 897  ARG n 
1 898  PHE n 
1 899  ARG n 
1 900  ASP n 
1 901  ASN n 
1 902  SER n 
1 903  PRO n 
1 904  LYS n 
1 905  LEU n 
1 906  ASN n 
1 907  TRP n 
1 908  LEU n 
1 909  LEU n 
1 910  LYS n 
1 911  ILE n 
1 912  LEU n 
1 913  ALA n 
1 914  GLU n 
1 915  ILE n 
1 916  LYS n 
1 917  HIS n 
1 918  THR n 
1 919  SER n 
1 920  LYS n 
1 921  ASP n 
1 922  LYS n 
1 923  VAL n 
1 924  ILE n 
1 925  ILE n 
1 926  PHE n 
1 927  THR n 
1 928  GLU n 
1 929  LEU n 
1 930  ARG n 
1 931  ASP n 
1 932  LEU n 
1 933  GLN n 
1 934  ARG n 
1 935  GLU n 
1 936  LEU n 
1 937  GLN n 
1 938  HIS n 
1 939  ALA n 
1 940  ILE n 
1 941  HIS n 
1 942  GLN n 
1 943  ASN n 
1 944  PHE n 
1 945  GLY n 
1 946  PHE n 
1 947  ARG n 
1 948  PRO n 
1 949  VAL n 
1 950  ILE n 
1 951  ILE n 
1 952  ASN n 
1 953  GLY n 
1 954  ASP n 
1 955  SER n 
1 956  SER n 
1 957  THR n 
1 958  LYS n 
1 959  SER n 
1 960  GLN n 
1 961  SER n 
1 962  GLN n 
1 963  ASN n 
1 964  SER n 
1 965  ARG n 
1 966  GLN n 
1 967  ARG n 
1 968  LEU n 
1 969  ILE n 
1 970  ASP n 
1 971  ASP n 
1 972  PHE n 
1 973  GLN n 
1 974  ALA n 
1 975  GLN n 
1 976  PRO n 
1 977  GLY n 
1 978  PHE n 
1 979  GLY n 
1 980  VAL n 
1 981  ILE n 
1 982  ILE n 
1 983  LEU n 
1 984  SER n 
1 985  THR n 
1 986  VAL n 
1 987  ALA n 
1 988  VAL n 
1 989  GLY n 
1 990  PHE n 
1 991  GLY n 
1 992  VAL n 
1 993  ASN n 
1 994  VAL n 
1 995  GLN n 
1 996  LYS n 
1 997  ALA n 
1 998  ASN n 
1 999  HIS n 
1 1000 VAL n 
1 1001 ILE n 
1 1002 HIS n 
1 1003 PHE n 
1 1004 THR n 
1 1005 ARG n 
1 1006 CYS n 
1 1007 TRP n 
1 1008 ASN n 
1 1009 PRO n 
1 1010 ALA n 
1 1011 LYS n 
1 1012 GLU n 
1 1013 ASP n 
1 1014 GLN n 
1 1015 ALA n 
1 1016 THR n 
1 1017 ASP n 
1 1018 ARG n 
1 1019 ALA n 
1 1020 TYR n 
1 1021 ARG n 
1 1022 ILE n 
1 1023 GLY n 
1 1024 GLN n 
1 1025 THR n 
1 1026 LYS n 
1 1027 ASN n 
1 1028 VAL n 
1 1029 TYR n 
1 1030 VAL n 
1 1031 TYR n 
1 1032 TYR n 
1 1033 PRO n 
1 1034 THR n 
1 1035 VAL n 
1 1036 ARG n 
1 1037 ASP n 
1 1038 THR n 
1 1039 GLU n 
1 1040 ILE n 
1 1041 THR n 
1 1042 THR n 
1 1043 PHE n 
1 1044 GLU n 
1 1045 GLU n 
1 1046 THR n 
1 1047 LEU n 
1 1048 ASP n 
1 1049 ASP n 
1 1050 LEU n 
1 1051 LEU n 
1 1052 GLN n 
1 1053 ARG n 
1 1054 ARG n 
1 1055 ARG n 
1 1056 ALA n 
1 1057 LEU n 
1 1058 ALA n 
1 1059 ARG n 
1 1060 ASP n 
1 1061 MET n 
1 1062 LEU n 
1 1063 CYS n 
1 1064 ALA n 
1 1065 THR n 
1 1066 PRO n 
1 1067 ASP n 
1 1068 LEU n 
1 1069 ASN n 
1 1070 CYS n 
1 1071 ALA n 
1 1072 ASP n 
1 1073 PHE n 
1 1074 GLU n 
1 1075 THR n 
1 1076 ILE n 
1 1077 LEU n 
1 1078 LYS n 
1 1079 GLY n 
1 1080 ALA 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                   1080 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BF481_003650 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_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 
AGS non-polymer         . 'PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER' 
;ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE); ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE
;
'C10 H16 N5 O12 P3 S' 523.247 
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 
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 
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 
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 
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    MET 1    1    ?    ?   ?   A . n 
A 1 2    LEU 2    2    ?    ?   ?   A . n 
A 1 3    LYS 3    3    ?    ?   ?   A . n 
A 1 4    ARG 4    4    ?    ?   ?   A . n 
A 1 5    LEU 5    5    ?    ?   ?   A . n 
A 1 6    LEU 6    6    ?    ?   ?   A . n 
A 1 7    SER 7    7    ?    ?   ?   A . n 
A 1 8    LYS 8    8    ?    ?   ?   A . n 
A 1 9    LEU 9    9    ?    ?   ?   A . n 
A 1 10   THR 10   10   ?    ?   ?   A . n 
A 1 11   GLY 11   11   ?    ?   ?   A . n 
A 1 12   ASN 12   12   ?    ?   ?   A . n 
A 1 13   ARG 13   13   ?    ?   ?   A . n 
A 1 14   GLN 14   14   ?    ?   ?   A . n 
A 1 15   GLN 15   15   ?    ?   ?   A . n 
A 1 16   ILE 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   HIS 18   18   ?    ?   ?   A . n 
A 1 19   HIS 19   19   ?    ?   ?   A . n 
A 1 20   LEU 20   20   ?    ?   ?   A . n 
A 1 21   LYS 21   21   21   LYS LYS A . n 
A 1 22   ASN 22   22   22   ASN ASN A . n 
A 1 23   GLN 23   23   23   GLN GLN A . n 
A 1 24   TYR 24   24   24   TYR TYR A . n 
A 1 25   GLN 25   25   25   GLN GLN A . n 
A 1 26   VAL 26   26   26   VAL VAL A . n 
A 1 27   GLU 27   27   27   GLU GLU A . n 
A 1 28   GLU 28   28   28   GLU GLU A . n 
A 1 29   ASN 29   29   29   ASN ASN A . n 
A 1 30   GLY 30   30   30   GLY GLY A . n 
A 1 31   LEU 31   31   31   LEU LEU A . n 
A 1 32   SER 32   32   32   SER SER A . n 
A 1 33   PHE 33   33   33   PHE PHE A . n 
A 1 34   PRO 34   34   34   PRO PRO A . n 
A 1 35   LEU 35   35   35   LEU LEU A . n 
A 1 36   SER 36   36   36   SER SER A . n 
A 1 37   LEU 37   37   37   LEU LEU A . n 
A 1 38   VAL 38   38   38   VAL VAL A . n 
A 1 39   ASP 39   39   39   ASP ASP A . n 
A 1 40   ASP 40   40   40   ASP ASP A . n 
A 1 41   SER 41   41   41   SER SER A . n 
A 1 42   GLN 42   42   42   GLN GLN A . n 
A 1 43   LEU 43   43   43   LEU LEU A . n 
A 1 44   TRP 44   44   44   TRP TRP A . n 
A 1 45   ALA 45   45   45   ALA ALA A . n 
A 1 46   LEU 46   46   46   LEU LEU A . n 
A 1 47   ALA 47   47   47   ALA ALA A . n 
A 1 48   SER 48   48   48   SER SER A . n 
A 1 49   TRP 49   49   49   TRP TRP A . n 
A 1 50   LEU 50   50   50   LEU LEU A . n 
A 1 51   GLU 51   51   51   GLU GLU A . n 
A 1 52   GLN 52   52   52   GLN GLN A . n 
A 1 53   LEU 53   53   53   LEU LEU A . n 
A 1 54   ALA 54   54   54   ALA ALA A . n 
A 1 55   GLU 55   55   55   GLU GLU A . n 
A 1 56   GLU 56   56   56   GLU GLU A . n 
A 1 57   ASP 57   57   57   ASP ASP A . n 
A 1 58   TYR 58   58   58   TYR TYR A . n 
A 1 59   LEU 59   59   59   LEU LEU A . n 
A 1 60   ILE 60   60   60   ILE ILE A . n 
A 1 61   SER 61   61   61   SER SER A . n 
A 1 62   LEU 62   62   62   LEU LEU A . n 
A 1 63   THR 63   63   63   THR THR A . n 
A 1 64   ASP 64   64   64   ASP ASP A . n 
A 1 65   ARG 65   65   65   ARG ARG A . n 
A 1 66   TRP 66   66   66   TRP TRP A . n 
A 1 67   LEU 67   67   67   LEU LEU A . n 
A 1 68   LEU 68   68   68   LEU LEU A . n 
A 1 69   SER 69   69   69   SER SER A . n 
A 1 70   TRP 70   70   70   TRP TRP A . n 
A 1 71   GLU 71   71   71   GLU GLU A . n 
A 1 72   ALA 72   72   72   ALA ALA A . n 
A 1 73   LEU 73   73   73   LEU LEU A . n 
A 1 74   TYR 74   74   74   TYR TYR A . n 
A 1 75   ARG 75   75   75   ARG ARG A . n 
A 1 76   LEU 76   76   76   LEU LEU A . n 
A 1 77   LEU 77   77   77   LEU LEU A . n 
A 1 78   GLU 78   78   78   GLU GLU A . n 
A 1 79   ASP 79   79   79   ASP ASP A . n 
A 1 80   GLU 80   80   80   GLU GLU A . n 
A 1 81   GLU 81   81   81   GLU GLU A . n 
A 1 82   HIS 82   82   82   HIS HIS A . n 
A 1 83   ALA 83   83   83   ALA ALA A . n 
A 1 84   SER 84   84   84   SER SER A . n 
A 1 85   SER 85   85   85   SER SER A . n 
A 1 86   LEU 86   86   86   LEU LEU A . n 
A 1 87   PRO 87   87   87   PRO PRO A . n 
A 1 88   LEU 88   88   88   LEU LEU A . n 
A 1 89   ILE 89   89   89   ILE ILE A . n 
A 1 90   GLY 90   90   90   GLY GLY A . n 
A 1 91   VAL 91   91   91   VAL VAL A . n 
A 1 92   PRO 92   92   92   PRO PRO A . n 
A 1 93   ASP 93   93   93   ASP ASP A . n 
A 1 94   ILE 94   94   94   ILE ILE A . n 
A 1 95   LEU 95   95   95   LEU LEU A . n 
A 1 96   PRO 96   96   96   PRO PRO A . n 
A 1 97   LEU 97   97   97   LEU LEU A . n 
A 1 98   ARG 98   98   98   ARG ARG A . n 
A 1 99   ALA 99   99   99   ALA ALA A . n 
A 1 100  SER 100  100  100  SER SER A . n 
A 1 101  LEU 101  101  101  LEU LEU A . n 
A 1 102  SER 102  102  102  SER SER A . n 
A 1 103  SER 103  103  103  SER SER A . n 
A 1 104  ARG 104  104  104  ARG ARG A . n 
A 1 105  GLY 105  105  105  GLY GLY A . n 
A 1 106  ALA 106  106  106  ALA ALA A . n 
A 1 107  LEU 107  107  107  LEU LEU A . n 
A 1 108  SER 108  108  108  SER SER A . n 
A 1 109  ASP 109  109  109  ASP ASP A . n 
A 1 110  SER 110  110  110  SER SER A . n 
A 1 111  ASP 111  111  111  ASP ASP A . n 
A 1 112  PHE 112  112  112  PHE PHE A . n 
A 1 113  ARG 113  113  113  ARG ARG A . n 
A 1 114  VAL 114  114  114  VAL VAL A . n 
A 1 115  TRP 115  115  115  TRP TRP A . n 
A 1 116  ILE 116  116  116  ILE ILE A . n 
A 1 117  ALA 117  117  117  ALA ALA A . n 
A 1 118  GLU 118  118  118  GLU GLU A . n 
A 1 119  TRP 119  119  119  TRP TRP A . n 
A 1 120  ALA 120  120  120  ALA ALA A . n 
A 1 121  THR 121  121  121  THR THR A . n 
A 1 122  PHE 122  122  122  PHE PHE A . n 
A 1 123  PRO 123  123  123  PRO PRO A . n 
A 1 124  ALA 124  124  124  ALA ALA A . n 
A 1 125  ARG 125  125  125  ARG ARG A . n 
A 1 126  LYS 126  126  126  LYS LYS A . n 
A 1 127  PRO 127  127  127  PRO PRO A . n 
A 1 128  ILE 128  128  128  ILE ILE A . n 
A 1 129  ARG 129  129  129  ARG ARG A . n 
A 1 130  PHE 130  130  130  PHE PHE A . n 
A 1 131  SER 131  131  131  SER SER A . n 
A 1 132  ARG 132  132  132  ARG ARG A . n 
A 1 133  THR 133  133  133  THR THR A . n 
A 1 134  GLY 134  134  134  GLY GLY A . n 
A 1 135  ALA 135  135  135  ALA ALA A . n 
A 1 136  ILE 136  136  136  ILE ILE A . n 
A 1 137  LEU 137  137  137  LEU LEU A . n 
A 1 138  THR 138  138  138  THR THR A . n 
A 1 139  HIS 139  139  139  HIS HIS A . n 
A 1 140  ASP 140  140  140  ASP ASP A . n 
A 1 141  ASN 141  141  141  ASN ASN A . n 
A 1 142  GLN 142  142  142  GLN GLN A . n 
A 1 143  GLN 143  143  143  GLN GLN A . n 
A 1 144  TYR 144  144  144  TYR TYR A . n 
A 1 145  LEU 145  145  145  LEU LEU A . n 
A 1 146  LEU 146  146  146  LEU LEU A . n 
A 1 147  SER 147  147  147  SER SER A . n 
A 1 148  ARG 148  148  148  ARG ARG A . n 
A 1 149  GLU 149  149  149  GLU GLU A . n 
A 1 150  ASN 150  150  150  ASN ASN A . n 
A 1 151  TRP 151  151  151  TRP TRP A . n 
A 1 152  ALA 152  152  152  ALA ALA A . n 
A 1 153  LEU 153  153  153  LEU LEU A . n 
A 1 154  LEU 154  154  154  LEU LEU A . n 
A 1 155  GLN 155  155  155  GLN GLN A . n 
A 1 156  ALA 156  156  156  ALA ALA A . n 
A 1 157  THR 157  157  157  THR THR A . n 
A 1 158  GLU 158  158  158  GLU GLU A . n 
A 1 159  GLN 159  159  159  GLN GLN A . n 
A 1 160  LEU 160  160  160  LEU LEU A . n 
A 1 161  SER 161  161  161  SER SER A . n 
A 1 162  ALA 162  162  162  ALA ALA A . n 
A 1 163  GLN 163  163  163  GLN GLN A . n 
A 1 164  GLN 164  164  164  GLN GLN A . n 
A 1 165  ILE 165  165  165  ILE ILE A . n 
A 1 166  GLN 166  166  166  GLN GLN A . n 
A 1 167  THR 167  167  167  THR THR A . n 
A 1 168  PRO 168  168  168  PRO PRO A . n 
A 1 169  GLY 169  169  169  GLY GLY A . n 
A 1 170  GLU 170  170  170  GLU GLU A . n 
A 1 171  THR 171  171  171  THR THR A . n 
A 1 172  THR 172  172  172  THR THR A . n 
A 1 173  ASN 173  173  173  ASN ASN A . n 
A 1 174  GLN 174  174  174  GLN GLN A . n 
A 1 175  LEU 175  175  175  LEU LEU A . n 
A 1 176  GLY 176  176  176  GLY GLY A . n 
A 1 177  TRP 177  177  177  TRP TRP A . n 
A 1 178  ALA 178  178  178  ALA ALA A . n 
A 1 179  ALA 179  179  179  ALA ALA A . n 
A 1 180  ILE 180  180  180  ILE ILE A . n 
A 1 181  ARG 181  181  181  ARG ARG A . n 
A 1 182  LYS 182  182  182  LYS LYS A . n 
A 1 183  CYS 183  183  183  CYS CYS A . n 
A 1 184  ALA 184  184  184  ALA ALA A . n 
A 1 185  LYS 185  185  185  LYS LYS A . n 
A 1 186  LEU 186  186  186  LEU LEU A . n 
A 1 187  ALA 187  187  187  ALA ALA A . n 
A 1 188  ALA 188  188  188  ALA ALA A . n 
A 1 189  ALA 189  189  189  ALA ALA A . n 
A 1 190  LYS 190  190  190  LYS LYS A . n 
A 1 191  PHE 191  191  191  PHE PHE A . n 
A 1 192  ASP 192  192  192  ASP ASP A . n 
A 1 193  ASP 193  193  193  ASP ASP A . n 
A 1 194  TYR 194  194  194  TYR TYR A . n 
A 1 195  LEU 195  195  195  LEU LEU A . n 
A 1 196  GLU 196  196  196  GLU GLU A . n 
A 1 197  LYS 197  197  197  LYS LYS A . n 
A 1 198  THR 198  198  198  THR THR A . n 
A 1 199  HIS 199  199  199  HIS HIS A . n 
A 1 200  VAL 200  200  200  VAL VAL A . n 
A 1 201  ILE 201  201  201  ILE ILE A . n 
A 1 202  LYS 202  202  202  LYS LYS A . n 
A 1 203  PRO 203  203  203  PRO PRO A . n 
A 1 204  THR 204  204  204  THR THR A . n 
A 1 205  SER 205  205  205  SER SER A . n 
A 1 206  LEU 206  206  206  LEU LEU A . n 
A 1 207  SER 207  207  207  SER SER A . n 
A 1 208  LEU 208  208  208  LEU LEU A . n 
A 1 209  ARG 209  209  209  ARG ARG A . n 
A 1 210  LEU 210  210  210  LEU LEU A . n 
A 1 211  ARG 211  211  211  ARG ARG A . n 
A 1 212  LYS 212  212  212  LYS LYS A . n 
A 1 213  ALA 213  213  213  ALA ALA A . n 
A 1 214  THR 214  214  214  THR THR A . n 
A 1 215  VAL 215  215  215  VAL VAL A . n 
A 1 216  ALA 216  216  216  ALA ALA A . n 
A 1 217  ASP 217  217  217  ASP ASP A . n 
A 1 218  THR 218  218  218  THR THR A . n 
A 1 219  ALA 219  219  219  ALA ALA A . n 
A 1 220  VAL 220  220  220  VAL VAL A . n 
A 1 221  ILE 221  221  221  ILE ILE A . n 
A 1 222  GLU 222  222  222  GLU GLU A . n 
A 1 223  ILE 223  223  223  ILE ILE A . n 
A 1 224  GLU 224  224  224  GLU GLU A . n 
A 1 225  PRO 225  225  225  PRO PRO A . n 
A 1 226  HIS 226  226  226  HIS HIS A . n 
A 1 227  PHE 227  227  227  PHE PHE A . n 
A 1 228  GLU 228  228  228  GLU GLU A . n 
A 1 229  ASP 229  229  229  ASP ASP A . n 
A 1 230  GLN 230  230  230  GLN GLN A . n 
A 1 231  PRO 231  231  231  PRO PRO A . n 
A 1 232  ALA 232  232  232  ALA ALA A . n 
A 1 233  ASN 233  233  233  ASN ASN A . n 
A 1 234  TRP 234  234  234  TRP TRP A . n 
A 1 235  LEU 235  235  235  LEU LEU A . n 
A 1 236  GLY 236  236  236  GLY GLY A . n 
A 1 237  SER 237  237  237  SER SER A . n 
A 1 238  PHE 238  238  238  PHE PHE A . n 
A 1 239  ASP 239  239  239  ASP ASP A . n 
A 1 240  LYS 240  240  240  LYS LYS A . n 
A 1 241  ASN 241  241  241  ASN ASN A . n 
A 1 242  LEU 242  242  242  LEU LEU A . n 
A 1 243  GLN 243  243  243  GLN GLN A . n 
A 1 244  VAL 244  244  244  VAL VAL A . n 
A 1 245  HIS 245  245  245  HIS HIS A . n 
A 1 246  ASP 246  246  246  ASP ASP A . n 
A 1 247  SER 247  247  247  SER SER A . n 
A 1 248  TYR 248  248  248  TYR TYR A . n 
A 1 249  ARG 249  249  249  ARG ARG A . n 
A 1 250  ILE 250  250  250  ILE ILE A . n 
A 1 251  PRO 251  251  251  PRO PRO A . n 
A 1 252  GLY 252  252  252  GLY GLY A . n 
A 1 253  GLU 253  253  253  GLU GLU A . n 
A 1 254  ASN 254  254  254  ASN ASN A . n 
A 1 255  GLY 255  255  255  GLY GLY A . n 
A 1 256  GLU 256  256  256  GLU GLU A . n 
A 1 257  LEU 257  257  257  LEU LEU A . n 
A 1 258  SER 258  258  258  SER SER A . n 
A 1 259  HIS 259  259  259  HIS HIS A . n 
A 1 260  VAL 260  260  260  VAL VAL A . n 
A 1 261  ILE 261  261  261  ILE ILE A . n 
A 1 262  ILE 262  262  262  ILE ILE A . n 
A 1 263  PRO 263  263  263  PRO PRO A . n 
A 1 264  PRO 264  264  264  PRO PRO A . n 
A 1 265  GLU 265  265  265  GLU GLU A . n 
A 1 266  VAL 266  266  266  VAL VAL A . n 
A 1 267  LYS 267  267  267  LYS LYS A . n 
A 1 268  GLU 268  268  268  GLU GLU A . n 
A 1 269  VAL 269  269  269  VAL VAL A . n 
A 1 270  LEU 270  270  270  LEU LEU A . n 
A 1 271  ASN 271  271  271  ASN ASN A . n 
A 1 272  SER 272  272  272  SER SER A . n 
A 1 273  ILE 273  273  273  ILE ILE A . n 
A 1 274  HIS 274  274  274  HIS HIS A . n 
A 1 275  SER 275  275  275  SER SER A . n 
A 1 276  ILE 276  276  276  ILE ILE A . n 
A 1 277  PRO 277  277  277  PRO PRO A . n 
A 1 278  GLY 278  278  278  GLY GLY A . n 
A 1 279  ARG 279  279  279  ARG ARG A . n 
A 1 280  ARG 280  280  280  ARG ARG A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  ALA 282  282  282  ALA ALA A . n 
A 1 283  GLY 283  283  283  GLY GLY A . n 
A 1 284  SER 284  284  284  SER SER A . n 
A 1 285  GLU 285  285  285  GLU GLU A . n 
A 1 286  ALA 286  286  286  ALA ALA A . n 
A 1 287  LEU 287  287  287  LEU LEU A . n 
A 1 288  SER 288  288  288  SER SER A . n 
A 1 289  PHE 289  289  289  PHE PHE A . n 
A 1 290  VAL 290  290  290  VAL VAL A . n 
A 1 291  ARG 291  291  291  ARG ARG A . n 
A 1 292  ASN 292  292  292  ASN ASN A . n 
A 1 293  PRO 293  293  293  PRO PRO A . n 
A 1 294  TYR 294  294  294  TYR TYR A . n 
A 1 295  THR 295  295  295  THR THR A . n 
A 1 296  PHE 296  296  296  PHE PHE A . n 
A 1 297  LEU 297  297  297  LEU LEU A . n 
A 1 298  GLY 298  298  298  GLY GLY A . n 
A 1 299  GLU 299  299  299  GLU GLU A . n 
A 1 300  ASP 300  300  300  ASP ASP A . n 
A 1 301  ALA 301  301  301  ALA ALA A . n 
A 1 302  ALA 302  302  302  ALA ALA A . n 
A 1 303  SER 303  303  303  SER SER A . n 
A 1 304  VAL 304  304  304  VAL VAL A . n 
A 1 305  ILE 305  305  305  ILE ILE A . n 
A 1 306  ALA 306  306  306  ALA ALA A . n 
A 1 307  PRO 307  307  307  PRO PRO A . n 
A 1 308  GLU 308  308  308  GLU GLU A . n 
A 1 309  GLU 309  309  309  GLU GLU A . n 
A 1 310  HIS 310  310  310  HIS HIS A . n 
A 1 311  GLU 311  311  311  GLU GLU A . n 
A 1 312  GLN 312  312  312  GLN GLN A . n 
A 1 313  ALA 313  313  313  ALA ALA A . n 
A 1 314  LEU 314  314  314  LEU LEU A . n 
A 1 315  PHE 315  315  315  PHE PHE A . n 
A 1 316  ASP 316  316  316  ASP ASP A . n 
A 1 317  ALA 317  317  317  ALA ALA A . n 
A 1 318  ARG 318  318  318  ARG ARG A . n 
A 1 319  ILE 319  319  319  ILE ILE A . n 
A 1 320  PHE 320  320  320  PHE PHE A . n 
A 1 321  PHE 321  321  321  PHE PHE A . n 
A 1 322  HIS 322  322  322  HIS HIS A . n 
A 1 323  HIS 323  323  323  HIS HIS A . n 
A 1 324  PHE 324  324  324  PHE PHE A . n 
A 1 325  ARG 325  325  325  ARG ARG A . n 
A 1 326  LEU 326  326  326  LEU LEU A . n 
A 1 327  ILE 327  327  327  ILE ILE A . n 
A 1 328  PRO 328  328  328  PRO PRO A . n 
A 1 329  GLN 329  329  329  GLN GLN A . n 
A 1 330  LEU 330  330  330  LEU LEU A . n 
A 1 331  ASN 331  331  331  ASN ASN A . n 
A 1 332  THR 332  332  332  THR THR A . n 
A 1 333  GLU 333  333  333  GLU GLU A . n 
A 1 334  ASN 334  334  334  ASN ASN A . n 
A 1 335  LYS 335  335  335  LYS LYS A . n 
A 1 336  ILE 336  336  336  ILE ILE A . n 
A 1 337  THR 337  337  337  THR THR A . n 
A 1 338  GLU 338  338  338  GLU GLU A . n 
A 1 339  VAL 339  339  339  VAL VAL A . n 
A 1 340  THR 340  340  340  THR THR A . n 
A 1 341  LEU 341  341  341  LEU LEU A . n 
A 1 342  ILE 342  342  342  ILE ILE A . n 
A 1 343  LEU 343  343  343  LEU LEU A . n 
A 1 344  GLU 344  344  344  GLU GLU A . n 
A 1 345  PRO 345  345  345  PRO PRO A . n 
A 1 346  VAL 346  346  346  VAL VAL A . n 
A 1 347  SER 347  347  347  SER SER A . n 
A 1 348  PRO 348  348  348  PRO PRO A . n 
A 1 349  VAL 349  349  349  VAL VAL A . n 
A 1 350  PRO 350  350  350  PRO PRO A . n 
A 1 351  GLN 351  351  351  GLN GLN A . n 
A 1 352  PRO 352  352  352  PRO PRO A . n 
A 1 353  GLU 353  353  353  GLU GLU A . n 
A 1 354  ILE 354  354  354  ILE ILE A . n 
A 1 355  THR 355  355  355  THR THR A . n 
A 1 356  PHE 356  356  356  PHE PHE A . n 
A 1 357  VAL 357  357  357  VAL VAL A . n 
A 1 358  PHE 358  358  358  PHE PHE A . n 
A 1 359  SER 359  359  359  SER SER A . n 
A 1 360  ALA 360  360  360  ALA ALA A . n 
A 1 361  PRO 361  361  361  PRO PRO A . n 
A 1 362  TRP 362  362  362  TRP TRP A . n 
A 1 363  GLU 363  363  363  GLU GLU A . n 
A 1 364  LEU 364  364  364  LEU LEU A . n 
A 1 365  ASP 365  365  365  ASP ASP A . n 
A 1 366  LYS 366  366  366  LYS LYS A . n 
A 1 367  PHE 367  367  367  PHE PHE A . n 
A 1 368  ILE 368  368  368  ILE ILE A . n 
A 1 369  GLN 369  369  369  GLN GLN A . n 
A 1 370  GLN 370  370  370  GLN GLN A . n 
A 1 371  LEU 371  371  371  LEU LEU A . n 
A 1 372  GLY 372  372  372  GLY GLY A . n 
A 1 373  ILE 373  373  373  ILE ILE A . n 
A 1 374  SER 374  374  374  SER SER A . n 
A 1 375  VAL 375  375  375  VAL VAL A . n 
A 1 376  ALA 376  376  376  ALA ALA A . n 
A 1 377  ALA 377  377  377  ALA ALA A . n 
A 1 378  GLN 378  378  378  GLN GLN A . n 
A 1 379  MET 379  379  379  MET MET A . n 
A 1 380  PRO 380  380  380  PRO PRO A . n 
A 1 381  ALA 381  381  381  ALA ALA A . n 
A 1 382  GLY 382  382  382  GLY GLY A . n 
A 1 383  SER 383  383  383  SER SER A . n 
A 1 384  TRP 384  384  384  TRP TRP A . n 
A 1 385  GLN 385  385  385  GLN GLN A . n 
A 1 386  GLY 386  386  386  GLY GLY A . n 
A 1 387  TYR 387  387  387  TYR TYR A . n 
A 1 388  GLU 388  388  388  GLU GLU A . n 
A 1 389  LEU 389  389  389  LEU LEU A . n 
A 1 390  GLU 390  390  390  GLU GLU A . n 
A 1 391  LEU 391  391  391  LEU LEU A . n 
A 1 392  SER 392  392  392  SER SER A . n 
A 1 393  GLN 393  393  393  GLN GLN A . n 
A 1 394  PHE 394  394  394  PHE PHE A . n 
A 1 395  THR 395  395  395  THR THR A . n 
A 1 396  GLU 396  396  396  GLU GLU A . n 
A 1 397  GLN 397  397  397  GLN GLN A . n 
A 1 398  GLN 398  398  398  GLN GLN A . n 
A 1 399  TRP 399  399  399  TRP TRP A . n 
A 1 400  HIS 400  400  400  HIS HIS A . n 
A 1 401  ASP 401  401  401  ASP ASP A . n 
A 1 402  CYS 402  402  402  CYS CYS A . n 
A 1 403  GLN 403  403  403  GLN GLN A . n 
A 1 404  ALA 404  404  404  ALA ALA A . n 
A 1 405  LEU 405  405  405  LEU LEU A . n 
A 1 406  LEU 406  406  406  LEU LEU A . n 
A 1 407  THR 407  407  407  THR THR A . n 
A 1 408  ARG 408  408  408  ARG ARG A . n 
A 1 409  TRP 409  409  409  TRP TRP A . n 
A 1 410  GLN 410  410  410  GLN GLN A . n 
A 1 411  GLN 411  411  411  GLN GLN A . n 
A 1 412  GLU 412  412  412  GLU GLU A . n 
A 1 413  ILE 413  413  413  ILE ILE A . n 
A 1 414  GLU 414  414  414  GLU GLU A . n 
A 1 415  GLY 415  415  ?    ?   ?   A . n 
A 1 416  LYS 416  416  ?    ?   ?   A . n 
A 1 417  GLU 417  417  ?    ?   ?   A . n 
A 1 418  PHE 418  418  ?    ?   ?   A . n 
A 1 419  SER 419  419  ?    ?   ?   A . n 
A 1 420  ASP 420  420  ?    ?   ?   A . n 
A 1 421  VAL 421  421  ?    ?   ?   A . n 
A 1 422  LEU 422  422  ?    ?   ?   A . n 
A 1 423  ASP 423  423  ?    ?   ?   A . n 
A 1 424  ILE 424  424  ?    ?   ?   A . n 
A 1 425  ALA 425  425  ?    ?   ?   A . n 
A 1 426  LYS 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLY 428  428  ?    ?   ?   A . n 
A 1 429  ASP 429  429  ?    ?   ?   A . n 
A 1 430  ARG 430  430  ?    ?   ?   A . n 
A 1 431  VAL 431  431  ?    ?   ?   A . n 
A 1 432  ILE 432  432  ?    ?   ?   A . n 
A 1 433  GLY 433  433  ?    ?   ?   A . n 
A 1 434  ILE 434  434  ?    ?   ?   A . n 
A 1 435  GLY 435  435  ?    ?   ?   A . n 
A 1 436  GLU 436  436  ?    ?   ?   A . n 
A 1 437  PHE 437  437  ?    ?   ?   A . n 
A 1 438  GLU 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ILE 440  440  ?    ?   ?   A . n 
A 1 441  SER 441  441  ?    ?   ?   A . n 
A 1 442  SER 442  442  ?    ?   ?   A . n 
A 1 443  PRO 443  443  ?    ?   ?   A . n 
A 1 444  TRP 444  444  ?    ?   ?   A . n 
A 1 445  LEU 445  445  ?    ?   ?   A . n 
A 1 446  THR 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  ALA 448  448  ?    ?   ?   A . n 
A 1 449  GLN 449  449  ?    ?   ?   A . n 
A 1 450  SER 450  450  ?    ?   ?   A . n 
A 1 451  GLU 451  451  ?    ?   ?   A . n 
A 1 452  ASN 452  452  ?    ?   ?   A . n 
A 1 453  TRP 453  453  ?    ?   ?   A . n 
A 1 454  LEU 454  454  ?    ?   ?   A . n 
A 1 455  PRO 455  455  ?    ?   ?   A . n 
A 1 456  ASP 456  456  ?    ?   ?   A . n 
A 1 457  GLY 457  457  ?    ?   ?   A . n 
A 1 458  ILE 458  458  ?    ?   ?   A . n 
A 1 459  ASP 459  459  ?    ?   ?   A . n 
A 1 460  PHE 460  460  ?    ?   ?   A . n 
A 1 461  SER 461  461  ?    ?   ?   A . n 
A 1 462  ALA 462  462  ?    ?   ?   A . n 
A 1 463  PHE 463  463  ?    ?   ?   A . n 
A 1 464  SER 464  464  ?    ?   ?   A . n 
A 1 465  ILE 465  465  ?    ?   ?   A . n 
A 1 466  GLU 466  466  ?    ?   ?   A . n 
A 1 467  THR 467  467  ?    ?   ?   A . n 
A 1 468  LEU 468  468  ?    ?   ?   A . n 
A 1 469  SER 469  469  ?    ?   ?   A . n 
A 1 470  GLY 470  470  ?    ?   ?   A . n 
A 1 471  TRP 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  PRO 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  ASN 475  475  ?    ?   ?   A . n 
A 1 476  PRO 476  476  ?    ?   ?   A . n 
A 1 477  LEU 477  477  ?    ?   ?   A . n 
A 1 478  HIS 478  478  ?    ?   ?   A . n 
A 1 479  PHE 479  479  ?    ?   ?   A . n 
A 1 480  ASP 480  480  ?    ?   ?   A . n 
A 1 481  GLU 481  481  ?    ?   ?   A . n 
A 1 482  LEU 482  482  ?    ?   ?   A . n 
A 1 483  GLN 483  483  ?    ?   ?   A . n 
A 1 484  GLU 484  484  ?    ?   ?   A . n 
A 1 485  ILE 485  485  ?    ?   ?   A . n 
A 1 486  ILE 486  486  ?    ?   ?   A . n 
A 1 487  THR 487  487  ?    ?   ?   A . n 
A 1 488  GLN 488  488  ?    ?   ?   A . n 
A 1 489  ALA 489  489  ?    ?   ?   A . n 
A 1 490  GLU 490  490  ?    ?   ?   A . n 
A 1 491  ALA 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLY 493  493  ?    ?   ?   A . n 
A 1 494  GLU 494  494  ?    ?   ?   A . n 
A 1 495  THR 495  495  ?    ?   ?   A . n 
A 1 496  TYR 496  496  ?    ?   ?   A . n 
A 1 497  ILE 497  497  ?    ?   ?   A . n 
A 1 498  THR 498  498  ?    ?   ?   A . n 
A 1 499  THR 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  TRP 501  501  ?    ?   ?   A . n 
A 1 502  ASN 502  502  ?    ?   ?   A . n 
A 1 503  ASP 503  503  ?    ?   ?   A . n 
A 1 504  SER 504  504  ?    ?   ?   A . n 
A 1 505  GLN 505  505  ?    ?   ?   A . n 
A 1 506  LEU 506  506  ?    ?   ?   A . n 
A 1 507  PRO 507  507  ?    ?   ?   A . n 
A 1 508  LEU 508  508  ?    ?   ?   A . n 
A 1 509  ASP 509  509  ?    ?   ?   A . n 
A 1 510  ALA 510  510  ?    ?   ?   A . n 
A 1 511  ALA 511  511  ?    ?   ?   A . n 
A 1 512  LYS 512  512  ?    ?   ?   A . n 
A 1 513  THR 513  513  ?    ?   ?   A . n 
A 1 514  PHE 514  514  ?    ?   ?   A . n 
A 1 515  SER 515  515  ?    ?   ?   A . n 
A 1 516  LYS 516  516  ?    ?   ?   A . n 
A 1 517  ASN 517  517  ?    ?   ?   A . n 
A 1 518  TRP 518  518  ?    ?   ?   A . n 
A 1 519  GLU 519  519  ?    ?   ?   A . n 
A 1 520  LYS 520  520  ?    ?   ?   A . n 
A 1 521  GLN 521  521  ?    ?   ?   A . n 
A 1 522  GLN 522  522  ?    ?   ?   A . n 
A 1 523  ILE 523  523  ?    ?   ?   A . n 
A 1 524  THR 524  524  ?    ?   ?   A . n 
A 1 525  ALA 525  525  ?    ?   ?   A . n 
A 1 526  ASN 526  526  ?    ?   ?   A . n 
A 1 527  GLU 527  527  ?    ?   ?   A . n 
A 1 528  TYR 528  528  ?    ?   ?   A . n 
A 1 529  GLN 529  529  ?    ?   ?   A . n 
A 1 530  GLY 530  530  ?    ?   ?   A . n 
A 1 531  ASN 531  531  ?    ?   ?   A . n 
A 1 532  VAL 532  532  ?    ?   ?   A . n 
A 1 533  ALA 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  LYS 535  535  ?    ?   ?   A . n 
A 1 536  THR 536  536  ?    ?   ?   A . n 
A 1 537  ALA 537  537  ?    ?   ?   A . n 
A 1 538  ARG 538  538  ?    ?   ?   A . n 
A 1 539  ALA 539  539  ?    ?   ?   A . n 
A 1 540  VAL 540  540  ?    ?   ?   A . n 
A 1 541  LEU 541  541  ?    ?   ?   A . n 
A 1 542  LYS 542  542  ?    ?   ?   A . n 
A 1 543  ILE 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  GLN 545  545  ?    ?   ?   A . n 
A 1 546  ASN 546  546  ?    ?   ?   A . n 
A 1 547  ILE 547  547  ?    ?   ?   A . n 
A 1 548  GLU 548  548  ?    ?   ?   A . n 
A 1 549  GLU 549  549  ?    ?   ?   A . n 
A 1 550  THR 550  550  ?    ?   ?   A . n 
A 1 551  ALA 551  551  ?    ?   ?   A . n 
A 1 552  TYR 552  552  ?    ?   ?   A . n 
A 1 553  ILE 553  553  ?    ?   ?   A . n 
A 1 554  LYS 554  554  ?    ?   ?   A . n 
A 1 555  GLN 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ARG 557  557  ?    ?   ?   A . n 
A 1 558  ASN 558  558  ?    ?   ?   A . n 
A 1 559  SER 559  559  ?    ?   ?   A . n 
A 1 560  LEU 560  560  ?    ?   ?   A . n 
A 1 561  LEU 561  561  ?    ?   ?   A . n 
A 1 562  ASN 562  562  ?    ?   ?   A . n 
A 1 563  ALA 563  563  ?    ?   ?   A . n 
A 1 564  ARG 564  564  ?    ?   ?   A . n 
A 1 565  HIS 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  566  ALA ALA A . n 
A 1 567  GLU 567  567  567  GLU GLU A . n 
A 1 568  PRO 568  568  568  PRO PRO A . n 
A 1 569  GLU 569  569  569  GLU GLU A . n 
A 1 570  ILE 570  570  570  ILE ILE A . n 
A 1 571  PRO 571  571  571  PRO PRO A . n 
A 1 572  LEU 572  572  572  LEU LEU A . n 
A 1 573  SER 573  573  573  SER SER A . n 
A 1 574  LEU 574  574  574  LEU LEU A . n 
A 1 575  LYS 575  575  575  LYS LYS A . n 
A 1 576  GLU 576  576  576  GLU GLU A . n 
A 1 577  HIS 577  577  577  HIS HIS A . n 
A 1 578  ILE 578  578  578  ILE ILE A . n 
A 1 579  ARG 579  579  579  ARG ARG A . n 
A 1 580  LEU 580  580  580  LEU LEU A . n 
A 1 581  LYS 581  581  581  LYS LYS A . n 
A 1 582  ASP 582  582  582  ASP ASP A . n 
A 1 583  HIS 583  583  583  HIS HIS A . n 
A 1 584  GLN 584  584  584  GLN GLN A . n 
A 1 585  ARG 585  585  585  ARG ARG A . n 
A 1 586  GLU 586  586  586  GLU GLU A . n 
A 1 587  GLY 587  587  587  GLY GLY A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  ALA 589  589  589  ALA ALA A . n 
A 1 590  TRP 590  590  590  TRP TRP A . n 
A 1 591  LEU 591  591  591  LEU LEU A . n 
A 1 592  GLN 592  592  592  GLN GLN A . n 
A 1 593  GLN 593  593  593  GLN GLN A . n 
A 1 594  LEU 594  594  594  LEU LEU A . n 
A 1 595  PHE 595  595  595  PHE PHE A . n 
A 1 596  LEU 596  596  596  LEU LEU A . n 
A 1 597  ARG 597  597  597  ARG ARG A . n 
A 1 598  SER 598  598  598  SER SER A . n 
A 1 599  PRO 599  599  599  PRO PRO A . n 
A 1 600  GLU 600  600  600  GLU GLU A . n 
A 1 601  GLU 601  601  601  GLU GLU A . n 
A 1 602  THR 602  602  602  THR THR A . n 
A 1 603  ALA 603  603  603  ALA ALA A . n 
A 1 604  GLY 604  604  604  GLY GLY A . n 
A 1 605  CYS 605  605  605  CYS CYS A . n 
A 1 606  LEU 606  606  606  LEU LEU A . n 
A 1 607  LEU 607  607  607  LEU LEU A . n 
A 1 608  ALA 608  608  608  ALA ALA A . n 
A 1 609  ASP 609  609  609  ASP ASP A . n 
A 1 610  ASP 610  610  610  ASP ASP A . n 
A 1 611  MET 611  611  611  MET MET A . n 
A 1 612  GLY 612  612  612  GLY GLY A . n 
A 1 613  LEU 613  613  613  LEU LEU A . n 
A 1 614  GLY 614  614  614  GLY GLY A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  THR 616  616  616  THR THR A . n 
A 1 617  LEU 617  617  617  LEU LEU A . n 
A 1 618  GLN 618  618  618  GLN GLN A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  LEU 620  620  620  LEU LEU A . n 
A 1 621  SER 621  621  621  SER SER A . n 
A 1 622  PHE 622  622  622  PHE PHE A . n 
A 1 623  LEU 623  623  623  LEU LEU A . n 
A 1 624  VAL 624  624  624  VAL VAL A . n 
A 1 625  TRP 625  625  625  TRP TRP A . n 
A 1 626  PHE 626  626  626  PHE PHE A . n 
A 1 627  ILE 627  627  627  ILE ILE A . n 
A 1 628  GLU 628  628  628  GLU GLU A . n 
A 1 629  LYS 629  629  629  LYS LYS A . n 
A 1 630  PHE 630  630  630  PHE PHE A . n 
A 1 631  PRO 631  631  631  PRO PRO A . n 
A 1 632  GLN 632  632  632  GLN GLN A . n 
A 1 633  GLU 633  633  633  GLU GLU A . n 
A 1 634  PRO 634  634  634  PRO PRO A . n 
A 1 635  PRO 635  635  635  PRO PRO A . n 
A 1 636  ASN 636  636  636  ASN ASN A . n 
A 1 637  LEU 637  637  637  LEU LEU A . n 
A 1 638  ILE 638  638  638  ILE ILE A . n 
A 1 639  VAL 639  639  639  VAL VAL A . n 
A 1 640  ALA 640  640  640  ALA ALA A . n 
A 1 641  PRO 641  641  641  PRO PRO A . n 
A 1 642  VAL 642  642  642  VAL VAL A . n 
A 1 643  SER 643  643  643  SER SER A . n 
A 1 644  LEU 644  644  644  LEU LEU A . n 
A 1 645  LEU 645  645  645  LEU LEU A . n 
A 1 646  ASP 646  646  646  ASP ASP A . n 
A 1 647  ASN 647  647  647  ASN ASN A . n 
A 1 648  TRP 648  648  648  TRP TRP A . n 
A 1 649  GLU 649  649  649  GLU GLU A . n 
A 1 650  ARG 650  650  650  ARG ARG A . n 
A 1 651  GLU 651  651  651  GLU GLU A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ASN 653  653  653  ASN ASN A . n 
A 1 654  ASN 654  654  654  ASN ASN A . n 
A 1 655  PHE 655  655  655  PHE PHE A . n 
A 1 656  PHE 656  656  656  PHE PHE A . n 
A 1 657  TYR 657  657  657  TYR TYR A . n 
A 1 658  THR 658  658  658  THR THR A . n 
A 1 659  ALA 659  659  659  ALA ALA A . n 
A 1 660  GLY 660  660  660  GLY GLY A . n 
A 1 661  ILE 661  661  661  ILE ILE A . n 
A 1 662  PRO 662  662  662  PRO PRO A . n 
A 1 663  VAL 663  663  663  VAL VAL A . n 
A 1 664  LEU 664  664  664  LEU LEU A . n 
A 1 665  LYS 665  665  665  LYS LYS A . n 
A 1 666  LEU 666  666  666  LEU LEU A . n 
A 1 667  TYR 667  667  667  TYR TYR A . n 
A 1 668  GLY 668  668  668  GLY GLY A . n 
A 1 669  GLU 669  669  669  GLU GLU A . n 
A 1 670  THR 670  670  670  THR THR A . n 
A 1 671  ILE 671  671  671  ILE ILE A . n 
A 1 672  LYS 672  672  672  LYS LYS A . n 
A 1 673  ALA 673  673  673  ALA ALA A . n 
A 1 674  VAL 674  674  674  VAL VAL A . n 
A 1 675  LYS 675  675  675  LYS LYS A . n 
A 1 676  TYR 676  676  676  TYR TYR A . n 
A 1 677  PRO 677  677  677  PRO PRO A . n 
A 1 678  LYS 678  678  678  LYS LYS A . n 
A 1 679  GLN 679  679  679  GLN GLN A . n 
A 1 680  ALA 680  680  680  ALA ALA A . n 
A 1 681  ILE 681  681  681  ILE ILE A . n 
A 1 682  PRO 682  682  682  PRO PRO A . n 
A 1 683  ALA 683  683  683  ALA ALA A . n 
A 1 684  HIS 684  684  684  HIS HIS A . n 
A 1 685  LEU 685  685  685  LEU LEU A . n 
A 1 686  GLN 686  686  686  GLN GLN A . n 
A 1 687  SER 687  687  687  SER SER A . n 
A 1 688  LYS 688  688  688  LYS LYS A . n 
A 1 689  GLY 689  689  689  GLY GLY A . n 
A 1 690  ILE 690  690  690  ILE ILE A . n 
A 1 691  LYS 691  691  691  LYS LYS A . n 
A 1 692  ASN 692  692  692  ASN ASN A . n 
A 1 693  LEU 693  693  693  LEU LEU A . n 
A 1 694  LEU 694  694  694  LEU LEU A . n 
A 1 695  LYS 695  695  695  LYS LYS A . n 
A 1 696  PRO 696  696  696  PRO PRO A . n 
A 1 697  GLY 697  697  697  GLY GLY A . n 
A 1 698  TRP 698  698  698  TRP TRP A . n 
A 1 699  GLN 699  699  699  GLN GLN A . n 
A 1 700  GLY 700  700  700  GLY GLY A . n 
A 1 701  GLU 701  701  701  GLU GLU A . n 
A 1 702  ALA 702  702  702  ALA ALA A . n 
A 1 703  LYS 703  703  703  LYS LYS A . n 
A 1 704  ILE 704  704  704  ILE ILE A . n 
A 1 705  ILE 705  705  705  ILE ILE A . n 
A 1 706  LEU 706  706  706  LEU LEU A . n 
A 1 707  THR 707  707  707  THR THR A . n 
A 1 708  THR 708  708  708  THR THR A . n 
A 1 709  TYR 709  709  709  TYR TYR A . n 
A 1 710  GLU 710  710  710  GLU GLU A . n 
A 1 711  THR 711  711  711  THR THR A . n 
A 1 712  LEU 712  712  712  LEU LEU A . n 
A 1 713  ARG 713  713  713  ARG ARG A . n 
A 1 714  ASP 714  714  714  ASP ASP A . n 
A 1 715  GLN 715  715  715  GLN GLN A . n 
A 1 716  GLU 716  716  716  GLU GLU A . n 
A 1 717  PHE 717  717  717  PHE PHE A . n 
A 1 718  SER 718  718  718  SER SER A . n 
A 1 719  LEU 719  719  719  LEU LEU A . n 
A 1 720  ALA 720  720  720  ALA ALA A . n 
A 1 721  ARG 721  721  721  ARG ARG A . n 
A 1 722  GLN 722  722  722  GLN GLN A . n 
A 1 723  PRO 723  723  723  PRO PRO A . n 
A 1 724  TRP 724  724  724  TRP TRP A . n 
A 1 725  SER 725  725  725  SER SER A . n 
A 1 726  ILE 726  726  726  ILE ILE A . n 
A 1 727  MET 727  727  727  MET MET A . n 
A 1 728  VAL 728  728  728  VAL VAL A . n 
A 1 729  CYS 729  729  729  CYS CYS A . n 
A 1 730  ASP 730  730  730  ASP ASP A . n 
A 1 731  GLU 731  731  731  GLU GLU A . n 
A 1 732  ALA 732  732  732  ALA ALA A . n 
A 1 733  GLN 733  733  733  GLN GLN A . n 
A 1 734  LYS 734  734  734  LYS LYS A . n 
A 1 735  ILE 735  735  735  ILE ILE A . n 
A 1 736  LYS 736  736  736  LYS LYS A . n 
A 1 737  ASN 737  737  737  ASN ASN A . n 
A 1 738  PRO 738  738  738  PRO PRO A . n 
A 1 739  ALA 739  739  739  ALA ALA A . n 
A 1 740  ALA 740  740  740  ALA ALA A . n 
A 1 741  LEU 741  741  741  LEU LEU A . n 
A 1 742  ILE 742  742  742  ILE ILE A . n 
A 1 743  THR 743  743  743  THR THR A . n 
A 1 744  HIS 744  744  744  HIS HIS A . n 
A 1 745  ALA 745  745  745  ALA ALA A . n 
A 1 746  ALA 746  746  746  ALA ALA A . n 
A 1 747  ASN 747  747  747  ASN ASN A . n 
A 1 748  ALA 748  748  748  ALA ALA A . n 
A 1 749  VAL 749  749  749  VAL VAL A . n 
A 1 750  GLN 750  750  750  GLN GLN A . n 
A 1 751  ALA 751  751  751  ALA ALA A . n 
A 1 752  ARG 752  752  752  ARG ARG A . n 
A 1 753  PHE 753  753  753  PHE PHE A . n 
A 1 754  LYS 754  754  754  LYS LYS A . n 
A 1 755  VAL 755  755  755  VAL VAL A . n 
A 1 756  ALA 756  756  756  ALA ALA A . n 
A 1 757  CYS 757  757  757  CYS CYS A . n 
A 1 758  THR 758  758  758  THR THR A . n 
A 1 759  GLY 759  759  759  GLY GLY A . n 
A 1 760  THR 760  760  760  THR THR A . n 
A 1 761  PRO 761  761  761  PRO PRO A . n 
A 1 762  VAL 762  762  762  VAL VAL A . n 
A 1 763  GLU 763  763  763  GLU GLU A . n 
A 1 764  ASN 764  764  764  ASN ASN A . n 
A 1 765  THR 765  765  765  THR THR A . n 
A 1 766  LEU 766  766  766  LEU LEU A . n 
A 1 767  VAL 767  767  767  VAL VAL A . n 
A 1 768  ASP 768  768  768  ASP ASP A . n 
A 1 769  LEU 769  769  769  LEU LEU A . n 
A 1 770  TRP 770  770  770  TRP TRP A . n 
A 1 771  SER 771  771  771  SER SER A . n 
A 1 772  LEU 772  772  772  LEU LEU A . n 
A 1 773  PHE 773  773  773  PHE PHE A . n 
A 1 774  ASP 774  774  774  ASP ASP A . n 
A 1 775  PHE 775  775  775  PHE PHE A . n 
A 1 776  ALA 776  776  776  ALA ALA A . n 
A 1 777  GLN 777  777  777  GLN GLN A . n 
A 1 778  PRO 778  778  778  PRO PRO A . n 
A 1 779  GLY 779  779  779  GLY GLY A . n 
A 1 780  LEU 780  780  780  LEU LEU A . n 
A 1 781  LEU 781  781  781  LEU LEU A . n 
A 1 782  GLY 782  782  782  GLY GLY A . n 
A 1 783  ALA 783  783  783  ALA ALA A . n 
A 1 784  LEU 784  784  784  LEU LEU A . n 
A 1 785  ASN 785  785  785  ASN ASN A . n 
A 1 786  GLU 786  786  786  GLU GLU A . n 
A 1 787  PHE 787  787  787  PHE PHE A . n 
A 1 788  GLY 788  788  788  GLY GLY A . n 
A 1 789  LYS 789  789  789  LYS LYS A . n 
A 1 790  GLN 790  790  790  GLN GLN A . n 
A 1 791  TYR 791  791  791  TYR TYR A . n 
A 1 792  VAL 792  792  792  VAL VAL A . n 
A 1 793  ARG 793  793  793  ARG ARG A . n 
A 1 794  PRO 794  794  794  PRO PRO A . n 
A 1 795  ILE 795  795  795  ILE ILE A . n 
A 1 796  GLU 796  796  796  GLU GLU A . n 
A 1 797  ASN 797  797  ?    ?   ?   A . n 
A 1 798  GLU 798  798  ?    ?   ?   A . n 
A 1 799  ASP 799  799  ?    ?   ?   A . n 
A 1 800  GLY 800  800  ?    ?   ?   A . n 
A 1 801  ARG 801  801  ?    ?   ?   A . n 
A 1 802  ASP 802  802  ?    ?   ?   A . n 
A 1 803  THR 803  803  803  THR THR A . n 
A 1 804  GLU 804  804  804  GLU GLU A . n 
A 1 805  ARG 805  805  805  ARG ARG A . n 
A 1 806  LEU 806  806  806  LEU LEU A . n 
A 1 807  GLU 807  807  807  GLU GLU A . n 
A 1 808  SER 808  808  808  SER SER A . n 
A 1 809  LEU 809  809  809  LEU LEU A . n 
A 1 810  ARG 810  810  810  ARG ARG A . n 
A 1 811  ALA 811  811  811  ALA ALA A . n 
A 1 812  LEU 812  812  812  LEU LEU A . n 
A 1 813  ILE 813  813  813  ILE ILE A . n 
A 1 814  GLU 814  814  814  GLU GLU A . n 
A 1 815  PRO 815  815  815  PRO PRO A . n 
A 1 816  GLN 816  816  816  GLN GLN A . n 
A 1 817  THR 817  817  817  THR THR A . n 
A 1 818  LEU 818  818  818  LEU LEU A . n 
A 1 819  ARG 819  819  819  ARG ARG A . n 
A 1 820  ARG 820  820  820  ARG ARG A . n 
A 1 821  THR 821  821  821  THR THR A . n 
A 1 822  LYS 822  822  822  LYS LYS A . n 
A 1 823  GLU 823  823  823  GLU GLU A . n 
A 1 824  GLU 824  824  824  GLU GLU A . n 
A 1 825  VAL 825  825  825  VAL VAL A . n 
A 1 826  ALA 826  826  826  ALA ALA A . n 
A 1 827  ARG 827  827  827  ARG ARG A . n 
A 1 828  ASP 828  828  828  ASP ASP A . n 
A 1 829  LEU 829  829  829  LEU LEU A . n 
A 1 830  PRO 830  830  830  PRO PRO A . n 
A 1 831  GLN 831  831  831  GLN GLN A . n 
A 1 832  LYS 832  832  832  LYS LYS A . n 
A 1 833  ILE 833  833  833  ILE ILE A . n 
A 1 834  GLU 834  834  834  GLU GLU A . n 
A 1 835  VAL 835  835  835  VAL VAL A . n 
A 1 836  GLU 836  836  836  GLU GLU A . n 
A 1 837  SER 837  837  837  SER SER A . n 
A 1 838  CYS 838  838  838  CYS CYS A . n 
A 1 839  LYS 839  839  839  LYS LYS A . n 
A 1 840  GLN 840  840  840  GLN GLN A . n 
A 1 841  LEU 841  841  841  LEU LEU A . n 
A 1 842  THR 842  842  842  THR THR A . n 
A 1 843  LEU 843  843  843  LEU LEU A . n 
A 1 844  SER 844  844  844  SER SER A . n 
A 1 845  GLY 845  845  845  GLY GLY A . n 
A 1 846  VAL 846  846  846  VAL VAL A . n 
A 1 847  GLN 847  847  847  GLN GLN A . n 
A 1 848  LYS 848  848  848  LYS LYS A . n 
A 1 849  GLN 849  849  849  GLN GLN A . n 
A 1 850  LEU 850  850  850  LEU LEU A . n 
A 1 851  TYR 851  851  851  TYR GLY A . n 
A 1 852  LEU 852  852  852  LEU LEU A . n 
A 1 853  SER 853  853  853  SER SER A . n 
A 1 854  SER 854  854  854  SER SER A . n 
A 1 855  VAL 855  855  855  VAL VAL A . n 
A 1 856  ALA 856  856  856  ALA ALA A . n 
A 1 857  ASN 857  857  857  ASN ASN A . n 
A 1 858  TRP 858  858  858  TRP TRP A . n 
A 1 859  GLN 859  859  859  GLN GLN A . n 
A 1 860  GLN 860  860  860  GLN GLN A . n 
A 1 861  GLN 861  861  861  GLN GLN A . n 
A 1 862  GLN 862  862  862  GLN GLN A . n 
A 1 863  ALA 863  863  863  ALA ALA A . n 
A 1 864  LEU 864  864  864  LEU LEU A . n 
A 1 865  ARG 865  865  ?    ?   ?   A . n 
A 1 866  GLU 866  866  ?    ?   ?   A . n 
A 1 867  GLY 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  GLN 869  869  ?    ?   ?   A . n 
A 1 870  GLN 870  870  ?    ?   ?   A . n 
A 1 871  ALA 871  871  ?    ?   ?   A . n 
A 1 872  GLY 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  GLY 874  874  874  GLY GLY A . n 
A 1 875  MET 875  875  875  MET MET A . n 
A 1 876  LEU 876  876  876  LEU LEU A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  LEU 878  878  878  LEU LEU A . n 
A 1 879  LEU 879  879  879  LEU LEU A . n 
A 1 880  HIS 880  880  880  HIS HIS A . n 
A 1 881  ARG 881  881  881  ARG ARG A . n 
A 1 882  LEU 882  882  882  LEU LEU A . n 
A 1 883  LYS 883  883  883  LYS LYS A . n 
A 1 884  LEU 884  884  884  LEU LEU A . n 
A 1 885  ILE 885  885  885  ILE ILE A . n 
A 1 886  CYS 886  886  886  CYS CYS A . n 
A 1 887  ALA 887  887  887  ALA ALA A . n 
A 1 888  HIS 888  888  888  HIS HIS A . n 
A 1 889  PRO 889  889  889  PRO PRO A . n 
A 1 890  ALA 890  890  890  ALA ALA A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  VAL 892  892  892  VAL VAL A . n 
A 1 893  ASN 893  893  893  ASN ASN A . n 
A 1 894  PRO 894  894  894  PRO PRO A . n 
A 1 895  GLU 895  895  895  GLU GLU A . n 
A 1 896  PRO 896  896  896  PRO PRO A . n 
A 1 897  ARG 897  897  897  ARG ARG A . n 
A 1 898  PHE 898  898  898  PHE PHE A . n 
A 1 899  ARG 899  899  899  ARG ARG A . n 
A 1 900  ASP 900  900  900  ASP ASP A . n 
A 1 901  ASN 901  901  901  ASN ASN A . n 
A 1 902  SER 902  902  902  SER SER A . n 
A 1 903  PRO 903  903  903  PRO PRO A . n 
A 1 904  LYS 904  904  904  LYS LYS A . n 
A 1 905  LEU 905  905  905  LEU LEU A . n 
A 1 906  ASN 906  906  906  ASN ASN A . n 
A 1 907  TRP 907  907  907  TRP TRP A . n 
A 1 908  LEU 908  908  908  LEU LEU A . n 
A 1 909  LEU 909  909  909  LEU LEU A . n 
A 1 910  LYS 910  910  910  LYS LYS A . n 
A 1 911  ILE 911  911  911  ILE ILE A . n 
A 1 912  LEU 912  912  912  LEU LEU A . n 
A 1 913  ALA 913  913  913  ALA ALA A . n 
A 1 914  GLU 914  914  914  GLU GLU A . n 
A 1 915  ILE 915  915  915  ILE ILE A . n 
A 1 916  LYS 916  916  916  LYS LYS A . n 
A 1 917  HIS 917  917  917  HIS HIS A . n 
A 1 918  THR 918  918  918  THR THR A . n 
A 1 919  SER 919  919  919  SER SER A . n 
A 1 920  LYS 920  920  920  LYS LYS A . n 
A 1 921  ASP 921  921  921  ASP ASP A . n 
A 1 922  LYS 922  922  922  LYS LYS A . n 
A 1 923  VAL 923  923  923  VAL VAL A . n 
A 1 924  ILE 924  924  924  ILE ILE A . n 
A 1 925  ILE 925  925  925  ILE ILE A . n 
A 1 926  PHE 926  926  926  PHE PHE A . n 
A 1 927  THR 927  927  927  THR THR A . n 
A 1 928  GLU 928  928  928  GLU GLU A . n 
A 1 929  LEU 929  929  929  LEU LEU A . n 
A 1 930  ARG 930  930  930  ARG ARG A . n 
A 1 931  ASP 931  931  931  ASP ASP A . n 
A 1 932  LEU 932  932  932  LEU LEU A . n 
A 1 933  GLN 933  933  933  GLN GLN A . n 
A 1 934  ARG 934  934  934  ARG ARG A . n 
A 1 935  GLU 935  935  935  GLU GLU A . n 
A 1 936  LEU 936  936  936  LEU LEU A . n 
A 1 937  GLN 937  937  937  GLN GLN A . n 
A 1 938  HIS 938  938  938  HIS HIS A . n 
A 1 939  ALA 939  939  939  ALA ALA A . n 
A 1 940  ILE 940  940  940  ILE ILE A . n 
A 1 941  HIS 941  941  941  HIS HIS A . n 
A 1 942  GLN 942  942  942  GLN GLN A . n 
A 1 943  ASN 943  943  943  ASN ASN A . n 
A 1 944  PHE 944  944  944  PHE PHE A . n 
A 1 945  GLY 945  945  945  GLY GLY A . n 
A 1 946  PHE 946  946  946  PHE PHE A . n 
A 1 947  ARG 947  947  947  ARG ARG A . n 
A 1 948  PRO 948  948  948  PRO PRO A . n 
A 1 949  VAL 949  949  949  VAL VAL A . n 
A 1 950  ILE 950  950  950  ILE ILE A . n 
A 1 951  ILE 951  951  951  ILE ILE A . n 
A 1 952  ASN 952  952  952  ASN ASN A . n 
A 1 953  GLY 953  953  953  GLY GLY A . n 
A 1 954  ASP 954  954  954  ASP ASP A . n 
A 1 955  SER 955  955  955  SER SER A . n 
A 1 956  SER 956  956  956  SER SER A . n 
A 1 957  THR 957  957  957  THR THR A . n 
A 1 958  LYS 958  958  958  LYS LYS A . n 
A 1 959  SER 959  959  959  SER SER A . n 
A 1 960  GLN 960  960  960  GLN GLN A . n 
A 1 961  SER 961  961  961  SER SER A . n 
A 1 962  GLN 962  962  962  GLN GLN A . n 
A 1 963  ASN 963  963  963  ASN ASN A . n 
A 1 964  SER 964  964  964  SER SER A . n 
A 1 965  ARG 965  965  965  ARG ARG A . n 
A 1 966  GLN 966  966  966  GLN GLN A . n 
A 1 967  ARG 967  967  967  ARG ARG A . n 
A 1 968  LEU 968  968  968  LEU LEU A . n 
A 1 969  ILE 969  969  969  ILE ILE A . n 
A 1 970  ASP 970  970  970  ASP ASP A . n 
A 1 971  ASP 971  971  971  ASP ASP A . n 
A 1 972  PHE 972  972  972  PHE PHE A . n 
A 1 973  GLN 973  973  973  GLN GLN A . n 
A 1 974  ALA 974  974  974  ALA ALA A . n 
A 1 975  GLN 975  975  975  GLN GLN A . n 
A 1 976  PRO 976  976  976  PRO PRO A . n 
A 1 977  GLY 977  977  977  GLY GLY A . n 
A 1 978  PHE 978  978  978  PHE PHE A . n 
A 1 979  GLY 979  979  979  GLY GLY A . n 
A 1 980  VAL 980  980  980  VAL VAL A . n 
A 1 981  ILE 981  981  981  ILE ILE A . n 
A 1 982  ILE 982  982  982  ILE ILE A . n 
A 1 983  LEU 983  983  983  LEU LEU A . n 
A 1 984  SER 984  984  984  SER SER A . n 
A 1 985  THR 985  985  985  THR THR A . n 
A 1 986  VAL 986  986  986  VAL VAL A . n 
A 1 987  ALA 987  987  987  ALA ALA A . n 
A 1 988  VAL 988  988  988  VAL VAL A . n 
A 1 989  GLY 989  989  989  GLY GLY A . n 
A 1 990  PHE 990  990  990  PHE PHE A . n 
A 1 991  GLY 991  991  991  GLY GLY A . n 
A 1 992  VAL 992  992  992  VAL VAL A . n 
A 1 993  ASN 993  993  993  ASN ASN A . n 
A 1 994  VAL 994  994  994  VAL VAL A . n 
A 1 995  GLN 995  995  995  GLN GLN A . n 
A 1 996  LYS 996  996  996  LYS LYS A . n 
A 1 997  ALA 997  997  997  ALA ALA A . n 
A 1 998  ASN 998  998  998  ASN ASN A . n 
A 1 999  HIS 999  999  999  HIS HIS A . n 
A 1 1000 VAL 1000 1000 1000 VAL VAL A . n 
A 1 1001 ILE 1001 1001 1001 ILE ILE A . n 
A 1 1002 HIS 1002 1002 1002 HIS HIS A . n 
A 1 1003 PHE 1003 1003 1003 PHE PHE A . n 
A 1 1004 THR 1004 1004 1004 THR THR A . n 
A 1 1005 ARG 1005 1005 1005 ARG ARG A . n 
A 1 1006 CYS 1006 1006 1006 CYS CYS A . n 
A 1 1007 TRP 1007 1007 1007 TRP TRP A . n 
A 1 1008 ASN 1008 1008 1008 ASN ASN A . n 
A 1 1009 PRO 1009 1009 1009 PRO PRO A . n 
A 1 1010 ALA 1010 1010 1010 ALA ALA A . n 
A 1 1011 LYS 1011 1011 1011 LYS LYS A . n 
A 1 1012 GLU 1012 1012 1012 GLU GLU A . n 
A 1 1013 ASP 1013 1013 1013 ASP ASP A . n 
A 1 1014 GLN 1014 1014 1014 GLN GLN A . n 
A 1 1015 ALA 1015 1015 1015 ALA ALA A . n 
A 1 1016 THR 1016 1016 1016 THR THR A . n 
A 1 1017 ASP 1017 1017 1017 ASP ASP A . n 
A 1 1018 ARG 1018 1018 1018 ARG ARG A . n 
A 1 1019 ALA 1019 1019 1019 ALA ALA A . n 
A 1 1020 TYR 1020 1020 1020 TYR TYR A . n 
A 1 1021 ARG 1021 1021 1021 ARG ARG A . n 
A 1 1022 ILE 1022 1022 1022 ILE ILE A . n 
A 1 1023 GLY 1023 1023 1023 GLY GLY A . n 
A 1 1024 GLN 1024 1024 1024 GLN GLN A . n 
A 1 1025 THR 1025 1025 1025 THR THR A . n 
A 1 1026 LYS 1026 1026 1026 LYS LYS A . n 
A 1 1027 ASN 1027 1027 1027 ASN ASN A . n 
A 1 1028 VAL 1028 1028 1028 VAL VAL A . n 
A 1 1029 TYR 1029 1029 1029 TYR TYR A . n 
A 1 1030 VAL 1030 1030 1030 VAL VAL A . n 
A 1 1031 TYR 1031 1031 1031 TYR TYR A . n 
A 1 1032 TYR 1032 1032 1032 TYR TYR A . n 
A 1 1033 PRO 1033 1033 1033 PRO PRO A . n 
A 1 1034 THR 1034 1034 1034 THR THR A . n 
A 1 1035 VAL 1035 1035 1035 VAL VAL A . n 
A 1 1036 ARG 1036 1036 1036 ARG ARG A . n 
A 1 1037 ASP 1037 1037 1037 ASP ASP A . n 
A 1 1038 THR 1038 1038 1038 THR THR A . n 
A 1 1039 GLU 1039 1039 1039 GLU GLU A . n 
A 1 1040 ILE 1040 1040 1040 ILE ILE A . n 
A 1 1041 THR 1041 1041 1041 THR THR A . n 
A 1 1042 THR 1042 1042 1042 THR THR A . n 
A 1 1043 PHE 1043 1043 1043 PHE PHE A . n 
A 1 1044 GLU 1044 1044 1044 GLU GLU A . n 
A 1 1045 GLU 1045 1045 1045 GLU GLU A . n 
A 1 1046 THR 1046 1046 1046 THR THR A . n 
A 1 1047 LEU 1047 1047 1047 LEU LEU A . n 
A 1 1048 ASP 1048 1048 1048 ASP ASP A . n 
A 1 1049 ASP 1049 1049 1049 ASP ASP A . n 
A 1 1050 LEU 1050 1050 1050 LEU LEU A . n 
A 1 1051 LEU 1051 1051 1051 LEU LEU A . n 
A 1 1052 GLN 1052 1052 1052 GLN GLN A . n 
A 1 1053 ARG 1053 1053 1053 ARG ARG A . n 
A 1 1054 ARG 1054 1054 1054 ARG ARG A . n 
A 1 1055 ARG 1055 1055 1055 ARG ARG A . n 
A 1 1056 ALA 1056 1056 1056 ALA ALA A . n 
A 1 1057 LEU 1057 1057 1057 LEU LEU A . n 
A 1 1058 ALA 1058 1058 1058 ALA ALA A . n 
A 1 1059 ARG 1059 1059 1059 ARG ARG A . n 
A 1 1060 ASP 1060 1060 1060 ASP ASP A . n 
A 1 1061 MET 1061 1061 1061 MET MET A . n 
A 1 1062 LEU 1062 1062 1062 LEU LEU A . n 
A 1 1063 CYS 1063 1063 1063 CYS CYS A . n 
A 1 1064 ALA 1064 1064 1064 ALA ALA A . n 
A 1 1065 THR 1065 1065 1065 THR THR A . n 
A 1 1066 PRO 1066 1066 1066 PRO PRO A . n 
A 1 1067 ASP 1067 1067 1067 ASP ASP A . n 
A 1 1068 LEU 1068 1068 1068 LEU LEU A . n 
A 1 1069 ASN 1069 1069 1069 ASN ASN A . n 
A 1 1070 CYS 1070 1070 1070 CYS CYS A . n 
A 1 1071 ALA 1071 1071 1071 ALA ALA A . n 
A 1 1072 ASP 1072 1072 1072 ASP ASP A . n 
A 1 1073 PHE 1073 1073 1073 PHE PHE A . n 
A 1 1074 GLU 1074 1074 1074 GLU GLU A . n 
A 1 1075 THR 1075 1075 1075 THR THR A . n 
A 1 1076 ILE 1076 1076 1076 ILE ILE A . n 
A 1 1077 LEU 1077 1077 1077 LEU LEU A . n 
A 1 1078 LYS 1078 1078 1078 LYS LYS A . n 
A 1 1079 GLY 1079 1079 1079 GLY GLY A . n 
A 1 1080 ALA 1080 1080 ?    ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        AGS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   AGS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          AGS 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     1101 
_pdbx_nonpoly_scheme.auth_seq_num    1101 
_pdbx_nonpoly_scheme.pdb_mon_id      AGS 
_pdbx_nonpoly_scheme.auth_mon_id     AGS 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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 TYR 851 ? CB  ? A TYR 851 CB  
2 1 Y 1 A TYR 851 ? CG  ? A TYR 851 CG  
3 1 Y 1 A TYR 851 ? CD1 ? A TYR 851 CD1 
4 1 Y 1 A TYR 851 ? CD2 ? A TYR 851 CD2 
5 1 Y 1 A TYR 851 ? CE1 ? A TYR 851 CE1 
6 1 Y 1 A TYR 851 ? CE2 ? A TYR 851 CE2 
7 1 Y 1 A TYR 851 ? CZ  ? A TYR 851 CZ  
8 1 Y 1 A TYR 851 ? OH  ? A TYR 851 OH  
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QYC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         8QYC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   8QYC 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8QYC 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.002  ? 7368  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.422  ? 10026 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 11.077 ? 2743  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040  ? 1123  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 1295  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8QYC 
_struct.title                        'Zorya anti-bacteriophage defense system ZorD in complex with ATP-gamma-S' 
_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        8QYC 
_struct_keywords.text            'Nuclease, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0V7WZM1_ECOLX 
_struct_ref.pdbx_db_accession          A0A0V7WZM1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLKRLLSKLTGNRQQIEHHLKNQYQVEENGLSFPLSLVDDSQLWALASWLEQLAEEDYLISLTDRWLLSWEALYRLLEDE
EHASSLPLIGVPDILPLRASLSSRGALSDSDFRVWIAEWATFPARKPIRFSRTGAILTHDNQQYLLSRENWALLQATEQL
SAQQIQTPGETTNQLGWAAIRKCAKLAAAKFDDYLEKTHVIKPTSLSLRLRKATVADTAVIEIEPHFEDQPANWLGSFDK
NLQVHDSYRIPGENGELSHVIIPPEVKEVLNSIHSIPGRRVAGSEALSFVRNPYTFLGEDAASVIAPEEHEQALFDARIF
FHHFRLIPQLNTENKITEVTLILEPVSPVPQPEITFVFSAPWELDKFIQQLGISVAAQMPAGSWQGYELELSQFTEQQWH
DCQALLTRWQQEIEGKEFSDVLDIAKYGDRVIGIGEFEKISSPWLTKAQSENWLPDGIDFSAFSIETLSGWQPENPLHFD
ELQEIITQAEAAGETYITTPWNDSQLPLDAAKTFSKNWEKQQITANEYQGNVADKTARAVLKIEQNIEETAYIKQRRNSL
LNARHAEPEIPLSLKEHIRLKDHQREGVAWLQQLFLRSPEETAGCLLADDMGLGKTLQILSFLVWFIEKFPQEPPNLIVA
PVSLLDNWERELNNFFYTAGIPVLKLYGETIKAVKYPKQAIPAHLQSKGIKNLLKPGWQGEAKIILTTYETLRDQEFSLA
RQPWSIMVCDEAQKIKNPAALITHAANAVQARFKVACTGTPVENTLVDLWSLFDFAQPGLLGALNEFGKQYVRPIENEDG
RDTERLESLRALIEPQTLRRTKEEVARDLPQKIEVESCKQLTLSGVQKQLYLSSVANWQQQQALREGMQQAGTGMLGLLH
RLKLICAHPAIVNPEPRFRDNSPKLNWLLKILAEIKHTSKDKVIIFTELRDLQRELQHAIHQNFGFRPVIINGDSSTKSQ
SQNSRQRLIDDFQAQPGFGVIILSTVAVGFGVNVQKANHVIHFTRCWNPAKEDQATDRAYRIGQTKNVYVYYPTVRDTEI
TTFEETLDDLLQRRRALARDMLCATPDLNCADFETILKGA
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QYC 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1080 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0V7WZM1 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1080 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       1080 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 36   ? ASP A 40   ? SER A 36   ASP A 40   5 ? 5  
HELX_P HELX_P2  AA2 LEU A 43   ? GLU A 56   ? LEU A 43   GLU A 56   1 ? 14 
HELX_P HELX_P3  AA3 TRP A 70   ? ASP A 79   ? TRP A 70   ASP A 79   1 ? 10 
HELX_P HELX_P4  AA4 SER A 85   ? ILE A 89   ? SER A 85   ILE A 89   5 ? 5  
HELX_P HELX_P5  AA5 SER A 147  ? ILE A 165  ? SER A 147  ILE A 165  1 ? 19 
HELX_P HELX_P6  AA6 GLY A 169  ? ALA A 188  ? GLY A 169  ALA A 188  1 ? 20 
HELX_P HELX_P7  AA7 ASP A 192  ? LYS A 197  ? ASP A 192  LYS A 197  1 ? 6  
HELX_P HELX_P8  AA8 ASN A 233  ? ASN A 241  ? ASN A 233  ASN A 241  1 ? 9  
HELX_P HELX_P9  AA9 PRO A 263  ? SER A 275  ? PRO A 263  SER A 275  1 ? 13 
HELX_P HELX_P10 AB1 ILE A 276  ? GLY A 278  ? ILE A 276  GLY A 278  5 ? 3  
HELX_P HELX_P11 AB2 GLY A 283  ? ASN A 292  ? GLY A 283  ASN A 292  1 ? 10 
HELX_P HELX_P12 AB3 ASN A 292  ? GLY A 298  ? ASN A 292  GLY A 298  1 ? 7  
HELX_P HELX_P13 AB4 GLU A 299  ? ILE A 305  ? GLU A 299  ILE A 305  1 ? 7  
HELX_P HELX_P14 AB5 ALA A 306  ? ALA A 317  ? ALA A 306  ALA A 317  1 ? 12 
HELX_P HELX_P15 AB6 ALA A 360  ? ALA A 377  ? ALA A 360  ALA A 377  1 ? 18 
HELX_P HELX_P16 AB7 THR A 395  ? GLU A 414  ? THR A 395  GLU A 414  1 ? 20 
HELX_P HELX_P17 AB8 LYS A 581  ? LEU A 596  ? LYS A 581  LEU A 596  1 ? 16 
HELX_P HELX_P18 AB9 GLY A 614  ? PHE A 630  ? GLY A 614  PHE A 630  1 ? 17 
HELX_P HELX_P19 AC1 PRO A 641  ? PHE A 656  ? PRO A 641  PHE A 656  1 ? 16 
HELX_P HELX_P20 AC2 GLU A 669  ? LYS A 675  ? GLU A 669  LYS A 675  1 ? 7  
HELX_P HELX_P21 AC3 PRO A 682  ? SER A 687  ? PRO A 682  SER A 687  1 ? 6  
HELX_P HELX_P22 AC4 THR A 708  ? GLN A 715  ? THR A 708  GLN A 715  1 ? 8  
HELX_P HELX_P23 AC5 GLN A 715  ? ALA A 720  ? GLN A 715  ALA A 720  1 ? 6  
HELX_P HELX_P24 AC6 ALA A 732  ? LYS A 736  ? ALA A 732  LYS A 736  5 ? 5  
HELX_P HELX_P25 AC7 ALA A 740  ? VAL A 749  ? ALA A 740  VAL A 749  1 ? 10 
HELX_P HELX_P26 AC8 THR A 765  ? GLN A 777  ? THR A 765  GLN A 777  1 ? 13 
HELX_P HELX_P27 AC9 ALA A 783  ? VAL A 792  ? ALA A 783  VAL A 792  1 ? 10 
HELX_P HELX_P28 AD1 GLU A 804  ? ILE A 813  ? GLU A 804  ILE A 813  1 ? 10 
HELX_P HELX_P29 AD2 GLU A 836  ? GLN A 840  ? GLU A 836  GLN A 840  5 ? 5  
HELX_P HELX_P30 AD3 SER A 844  ? LEU A 864  ? SER A 844  LEU A 864  1 ? 21 
HELX_P HELX_P31 AD4 MET A 875  ? HIS A 888  ? MET A 875  HIS A 888  1 ? 14 
HELX_P HELX_P32 AD5 HIS A 888  ? ASN A 893  ? HIS A 888  ASN A 893  1 ? 6  
HELX_P HELX_P33 AD6 GLU A 895  ? ASP A 900  ? GLU A 895  ASP A 900  1 ? 6  
HELX_P HELX_P34 AD7 SER A 902  ? SER A 919  ? SER A 902  SER A 919  1 ? 18 
HELX_P HELX_P35 AD8 LEU A 929  ? GLY A 945  ? LEU A 929  GLY A 945  1 ? 17 
HELX_P HELX_P36 AD9 LYS A 958  ? GLN A 975  ? LYS A 958  GLN A 975  1 ? 18 
HELX_P HELX_P37 AE1 ASN A 1008 ? ASP A 1017 ? ASN A 1008 ASP A 1017 1 ? 10 
HELX_P HELX_P38 AE2 THR A 1042 ? ARG A 1059 ? THR A 1042 ARG A 1059 1 ? 18 
HELX_P HELX_P39 AE3 ASN A 1069 ? GLU A 1074 ? ASN A 1069 GLU A 1074 5 ? 6  
HELX_P HELX_P40 AE4 THR A 1075 ? GLY A 1079 ? THR A 1075 GLY A 1079 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 7 ? 
AA8 ? 6 ? 
AA9 ? 2 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? 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      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? parallel      
AA9 1 2 ? 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 GLN A 25   ? GLU A 27   ? GLN A 25   GLU A 27   
AA1 2 GLY A 30   ? PRO A 34   ? GLY A 30   PRO A 34   
AA1 3 ARG A 65   ? SER A 69   ? ARG A 65   SER A 69   
AA1 4 ILE A 60   ? LEU A 62   ? ILE A 60   LEU A 62   
AA2 1 LEU A 97   ? ARG A 104  ? LEU A 97   ARG A 104  
AA2 2 ARG A 113  ? THR A 121  ? ARG A 113  THR A 121  
AA2 3 PRO A 127  ? ILE A 128  ? PRO A 127  ILE A 128  
AA3 1 ILE A 136  ? THR A 138  ? ILE A 136  THR A 138  
AA3 2 GLN A 143  ? LEU A 145  ? GLN A 143  LEU A 145  
AA4 1 THR A 198  ? ILE A 201  ? THR A 198  ILE A 201  
AA4 2 LEU A 257  ? ILE A 261  ? LEU A 257  ILE A 261  
AA4 3 SER A 247  ? PRO A 251  ? SER A 247  PRO A 251  
AA5 1 SER A 207  ? ALA A 213  ? SER A 207  ALA A 213  
AA5 2 VAL A 220  ? HIS A 226  ? VAL A 220  HIS A 226  
AA5 3 ARG A 280  ? VAL A 281  ? ARG A 280  VAL A 281  
AA6 1 ILE A 354  ? PHE A 358  ? ILE A 354  PHE A 358  
AA6 2 ILE A 336  ? GLU A 344  ? ILE A 336  GLU A 344  
AA6 3 PHE A 321  ? LEU A 330  ? PHE A 321  LEU A 330  
AA6 4 GLU A 388  ? LEU A 389  ? GLU A 388  LEU A 389  
AA7 1 VAL A 663  ? LYS A 665  ? VAL A 663  LYS A 665  
AA7 2 ILE A 704  ? THR A 707  ? ILE A 704  THR A 707  
AA7 3 ASN A 636  ? VAL A 639  ? ASN A 636  VAL A 639  
AA7 4 TRP A 724  ? ASP A 730  ? TRP A 724  ASP A 730  
AA7 5 ALA A 751  ? CYS A 757  ? ALA A 751  CYS A 757  
AA7 6 GLY A 604  ? LEU A 607  ? GLY A 604  LEU A 607  
AA7 7 THR A 817  ? LEU A 818  ? THR A 817  LEU A 818  
AA8 1 LYS A 832  ? GLU A 834  ? LYS A 832  GLU A 834  
AA8 2 VAL A 1028 ? TYR A 1031 ? VAL A 1028 TYR A 1031 
AA8 3 ALA A 997  ? HIS A 1002 ? ALA A 997  HIS A 1002 
AA8 4 LYS A 922  ? PHE A 926  ? LYS A 922  PHE A 926  
AA8 5 GLY A 979  ? LEU A 983  ? GLY A 979  LEU A 983  
AA8 6 VAL A 949  ? ILE A 950  ? VAL A 949  ILE A 950  
AA9 1 LEU A 841  ? THR A 842  ? LEU A 841  THR A 842  
AA9 2 VAL A 1035 ? ARG A 1036 ? VAL A 1035 ARG A 1036 
# 
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 GLN A 25   ? N GLN A 25   O SER A 32   ? O SER A 32   
AA1 2 3 N PHE A 33   ? N PHE A 33   O TRP A 66   ? O TRP A 66   
AA1 3 4 O ARG A 65   ? O ARG A 65   N LEU A 62   ? N LEU A 62   
AA2 1 2 N ARG A 98   ? N ARG A 98   O ALA A 120  ? O ALA A 120  
AA2 2 3 N TRP A 119  ? N TRP A 119  O ILE A 128  ? O ILE A 128  
AA3 1 2 N LEU A 137  ? N LEU A 137  O TYR A 144  ? O TYR A 144  
AA4 1 2 N ILE A 201  ? N ILE A 201  O HIS A 259  ? O HIS A 259  
AA4 2 3 O SER A 258  ? O SER A 258  N ILE A 250  ? N ILE A 250  
AA5 1 2 N ALA A 213  ? N ALA A 213  O VAL A 220  ? O VAL A 220  
AA5 2 3 N ILE A 221  ? N ILE A 221  O VAL A 281  ? O VAL A 281  
AA6 1 2 O ILE A 354  ? O ILE A 354  N LEU A 343  ? N LEU A 343  
AA6 2 3 O GLU A 344  ? O GLU A 344  N HIS A 323  ? N HIS A 323  
AA6 3 4 N HIS A 322  ? N HIS A 322  O GLU A 388  ? O GLU A 388  
AA7 1 2 N LEU A 664  ? N LEU A 664  O LEU A 706  ? O LEU A 706  
AA7 2 3 O ILE A 705  ? O ILE A 705  N ILE A 638  ? N ILE A 638  
AA7 3 4 N VAL A 639  ? N VAL A 639  O VAL A 728  ? O VAL A 728  
AA7 4 5 N MET A 727  ? N MET A 727  O PHE A 753  ? O PHE A 753  
AA7 5 6 O ALA A 756  ? O ALA A 756  N CYS A 605  ? N CYS A 605  
AA7 6 7 N LEU A 606  ? N LEU A 606  O LEU A 818  ? O LEU A 818  
AA8 1 2 N ILE A 833  ? N ILE A 833  O VAL A 1028 ? O VAL A 1028 
AA8 2 3 O TYR A 1031 ? O TYR A 1031 N VAL A 1000 ? N VAL A 1000 
AA8 3 4 O ILE A 1001 ? O ILE A 1001 N PHE A 926  ? N PHE A 926  
AA8 4 5 N ILE A 925  ? N ILE A 925  O ILE A 981  ? O ILE A 981  
AA8 5 6 O ILE A 982  ? O ILE A 982  N VAL A 949  ? N VAL A 949  
AA9 1 2 N LEU A 841  ? N LEU A 841  O ARG A 1036 ? O ARG A 1036 
# 
_pdbx_entry_details.entry_id                   8QYC 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 LEU A 62  ? ? -100.98 -169.58 
2 1 PRO A 87  ? ? -59.45  -8.40   
3 1 ASP A 828 ? ? -91.64  50.37   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8QYC 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8QYC 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.75 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               211477 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 'ORGANELLE OR CELLULAR COMPONENT' 
_em_entity_assembly.name                 'Zorya anti-bacteriophage defense system ZorD in complex with ATP-gamma-S' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8QYC 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'SPOT SCAN' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             500 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8QYC 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8QYC 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 MET 1    ? A MET 1    
2   1 Y 1 A LEU 2    ? A LEU 2    
3   1 Y 1 A LYS 3    ? A LYS 3    
4   1 Y 1 A ARG 4    ? A ARG 4    
5   1 Y 1 A LEU 5    ? A LEU 5    
6   1 Y 1 A LEU 6    ? A LEU 6    
7   1 Y 1 A SER 7    ? A SER 7    
8   1 Y 1 A LYS 8    ? A LYS 8    
9   1 Y 1 A LEU 9    ? A LEU 9    
10  1 Y 1 A THR 10   ? A THR 10   
11  1 Y 1 A GLY 11   ? A GLY 11   
12  1 Y 1 A ASN 12   ? A ASN 12   
13  1 Y 1 A ARG 13   ? A ARG 13   
14  1 Y 1 A GLN 14   ? A GLN 14   
15  1 Y 1 A GLN 15   ? A GLN 15   
16  1 Y 1 A ILE 16   ? A ILE 16   
17  1 Y 1 A GLU 17   ? A GLU 17   
18  1 Y 1 A HIS 18   ? A HIS 18   
19  1 Y 1 A HIS 19   ? A HIS 19   
20  1 Y 1 A LEU 20   ? A LEU 20   
21  1 Y 1 A GLY 415  ? A GLY 415  
22  1 Y 1 A LYS 416  ? A LYS 416  
23  1 Y 1 A GLU 417  ? A GLU 417  
24  1 Y 1 A PHE 418  ? A PHE 418  
25  1 Y 1 A SER 419  ? A SER 419  
26  1 Y 1 A ASP 420  ? A ASP 420  
27  1 Y 1 A VAL 421  ? A VAL 421  
28  1 Y 1 A LEU 422  ? A LEU 422  
29  1 Y 1 A ASP 423  ? A ASP 423  
30  1 Y 1 A ILE 424  ? A ILE 424  
31  1 Y 1 A ALA 425  ? A ALA 425  
32  1 Y 1 A LYS 426  ? A LYS 426  
33  1 Y 1 A TYR 427  ? A TYR 427  
34  1 Y 1 A GLY 428  ? A GLY 428  
35  1 Y 1 A ASP 429  ? A ASP 429  
36  1 Y 1 A ARG 430  ? A ARG 430  
37  1 Y 1 A VAL 431  ? A VAL 431  
38  1 Y 1 A ILE 432  ? A ILE 432  
39  1 Y 1 A GLY 433  ? A GLY 433  
40  1 Y 1 A ILE 434  ? A ILE 434  
41  1 Y 1 A GLY 435  ? A GLY 435  
42  1 Y 1 A GLU 436  ? A GLU 436  
43  1 Y 1 A PHE 437  ? A PHE 437  
44  1 Y 1 A GLU 438  ? A GLU 438  
45  1 Y 1 A LYS 439  ? A LYS 439  
46  1 Y 1 A ILE 440  ? A ILE 440  
47  1 Y 1 A SER 441  ? A SER 441  
48  1 Y 1 A SER 442  ? A SER 442  
49  1 Y 1 A PRO 443  ? A PRO 443  
50  1 Y 1 A TRP 444  ? A TRP 444  
51  1 Y 1 A LEU 445  ? A LEU 445  
52  1 Y 1 A THR 446  ? A THR 446  
53  1 Y 1 A LYS 447  ? A LYS 447  
54  1 Y 1 A ALA 448  ? A ALA 448  
55  1 Y 1 A GLN 449  ? A GLN 449  
56  1 Y 1 A SER 450  ? A SER 450  
57  1 Y 1 A GLU 451  ? A GLU 451  
58  1 Y 1 A ASN 452  ? A ASN 452  
59  1 Y 1 A TRP 453  ? A TRP 453  
60  1 Y 1 A LEU 454  ? A LEU 454  
61  1 Y 1 A PRO 455  ? A PRO 455  
62  1 Y 1 A ASP 456  ? A ASP 456  
63  1 Y 1 A GLY 457  ? A GLY 457  
64  1 Y 1 A ILE 458  ? A ILE 458  
65  1 Y 1 A ASP 459  ? A ASP 459  
66  1 Y 1 A PHE 460  ? A PHE 460  
67  1 Y 1 A SER 461  ? A SER 461  
68  1 Y 1 A ALA 462  ? A ALA 462  
69  1 Y 1 A PHE 463  ? A PHE 463  
70  1 Y 1 A SER 464  ? A SER 464  
71  1 Y 1 A ILE 465  ? A ILE 465  
72  1 Y 1 A GLU 466  ? A GLU 466  
73  1 Y 1 A THR 467  ? A THR 467  
74  1 Y 1 A LEU 468  ? A LEU 468  
75  1 Y 1 A SER 469  ? A SER 469  
76  1 Y 1 A GLY 470  ? A GLY 470  
77  1 Y 1 A TRP 471  ? A TRP 471  
78  1 Y 1 A GLN 472  ? A GLN 472  
79  1 Y 1 A PRO 473  ? A PRO 473  
80  1 Y 1 A GLU 474  ? A GLU 474  
81  1 Y 1 A ASN 475  ? A ASN 475  
82  1 Y 1 A PRO 476  ? A PRO 476  
83  1 Y 1 A LEU 477  ? A LEU 477  
84  1 Y 1 A HIS 478  ? A HIS 478  
85  1 Y 1 A PHE 479  ? A PHE 479  
86  1 Y 1 A ASP 480  ? A ASP 480  
87  1 Y 1 A GLU 481  ? A GLU 481  
88  1 Y 1 A LEU 482  ? A LEU 482  
89  1 Y 1 A GLN 483  ? A GLN 483  
90  1 Y 1 A GLU 484  ? A GLU 484  
91  1 Y 1 A ILE 485  ? A ILE 485  
92  1 Y 1 A ILE 486  ? A ILE 486  
93  1 Y 1 A THR 487  ? A THR 487  
94  1 Y 1 A GLN 488  ? A GLN 488  
95  1 Y 1 A ALA 489  ? A ALA 489  
96  1 Y 1 A GLU 490  ? A GLU 490  
97  1 Y 1 A ALA 491  ? A ALA 491  
98  1 Y 1 A ALA 492  ? A ALA 492  
99  1 Y 1 A GLY 493  ? A GLY 493  
100 1 Y 1 A GLU 494  ? A GLU 494  
101 1 Y 1 A THR 495  ? A THR 495  
102 1 Y 1 A TYR 496  ? A TYR 496  
103 1 Y 1 A ILE 497  ? A ILE 497  
104 1 Y 1 A THR 498  ? A THR 498  
105 1 Y 1 A THR 499  ? A THR 499  
106 1 Y 1 A PRO 500  ? A PRO 500  
107 1 Y 1 A TRP 501  ? A TRP 501  
108 1 Y 1 A ASN 502  ? A ASN 502  
109 1 Y 1 A ASP 503  ? A ASP 503  
110 1 Y 1 A SER 504  ? A SER 504  
111 1 Y 1 A GLN 505  ? A GLN 505  
112 1 Y 1 A LEU 506  ? A LEU 506  
113 1 Y 1 A PRO 507  ? A PRO 507  
114 1 Y 1 A LEU 508  ? A LEU 508  
115 1 Y 1 A ASP 509  ? A ASP 509  
116 1 Y 1 A ALA 510  ? A ALA 510  
117 1 Y 1 A ALA 511  ? A ALA 511  
118 1 Y 1 A LYS 512  ? A LYS 512  
119 1 Y 1 A THR 513  ? A THR 513  
120 1 Y 1 A PHE 514  ? A PHE 514  
121 1 Y 1 A SER 515  ? A SER 515  
122 1 Y 1 A LYS 516  ? A LYS 516  
123 1 Y 1 A ASN 517  ? A ASN 517  
124 1 Y 1 A TRP 518  ? A TRP 518  
125 1 Y 1 A GLU 519  ? A GLU 519  
126 1 Y 1 A LYS 520  ? A LYS 520  
127 1 Y 1 A GLN 521  ? A GLN 521  
128 1 Y 1 A GLN 522  ? A GLN 522  
129 1 Y 1 A ILE 523  ? A ILE 523  
130 1 Y 1 A THR 524  ? A THR 524  
131 1 Y 1 A ALA 525  ? A ALA 525  
132 1 Y 1 A ASN 526  ? A ASN 526  
133 1 Y 1 A GLU 527  ? A GLU 527  
134 1 Y 1 A TYR 528  ? A TYR 528  
135 1 Y 1 A GLN 529  ? A GLN 529  
136 1 Y 1 A GLY 530  ? A GLY 530  
137 1 Y 1 A ASN 531  ? A ASN 531  
138 1 Y 1 A VAL 532  ? A VAL 532  
139 1 Y 1 A ALA 533  ? A ALA 533  
140 1 Y 1 A ASP 534  ? A ASP 534  
141 1 Y 1 A LYS 535  ? A LYS 535  
142 1 Y 1 A THR 536  ? A THR 536  
143 1 Y 1 A ALA 537  ? A ALA 537  
144 1 Y 1 A ARG 538  ? A ARG 538  
145 1 Y 1 A ALA 539  ? A ALA 539  
146 1 Y 1 A VAL 540  ? A VAL 540  
147 1 Y 1 A LEU 541  ? A LEU 541  
148 1 Y 1 A LYS 542  ? A LYS 542  
149 1 Y 1 A ILE 543  ? A ILE 543  
150 1 Y 1 A GLU 544  ? A GLU 544  
151 1 Y 1 A GLN 545  ? A GLN 545  
152 1 Y 1 A ASN 546  ? A ASN 546  
153 1 Y 1 A ILE 547  ? A ILE 547  
154 1 Y 1 A GLU 548  ? A GLU 548  
155 1 Y 1 A GLU 549  ? A GLU 549  
156 1 Y 1 A THR 550  ? A THR 550  
157 1 Y 1 A ALA 551  ? A ALA 551  
158 1 Y 1 A TYR 552  ? A TYR 552  
159 1 Y 1 A ILE 553  ? A ILE 553  
160 1 Y 1 A LYS 554  ? A LYS 554  
161 1 Y 1 A GLN 555  ? A GLN 555  
162 1 Y 1 A ARG 556  ? A ARG 556  
163 1 Y 1 A ARG 557  ? A ARG 557  
164 1 Y 1 A ASN 558  ? A ASN 558  
165 1 Y 1 A SER 559  ? A SER 559  
166 1 Y 1 A LEU 560  ? A LEU 560  
167 1 Y 1 A LEU 561  ? A LEU 561  
168 1 Y 1 A ASN 562  ? A ASN 562  
169 1 Y 1 A ALA 563  ? A ALA 563  
170 1 Y 1 A ARG 564  ? A ARG 564  
171 1 Y 1 A HIS 565  ? A HIS 565  
172 1 Y 1 A ASN 797  ? A ASN 797  
173 1 Y 1 A GLU 798  ? A GLU 798  
174 1 Y 1 A ASP 799  ? A ASP 799  
175 1 Y 1 A GLY 800  ? A GLY 800  
176 1 Y 1 A ARG 801  ? A ARG 801  
177 1 Y 1 A ASP 802  ? A ASP 802  
178 1 Y 1 A ARG 865  ? A ARG 865  
179 1 Y 1 A GLU 866  ? A GLU 866  
180 1 Y 1 A GLY 867  ? A GLY 867  
181 1 Y 1 A MET 868  ? A MET 868  
182 1 Y 1 A GLN 869  ? A GLN 869  
183 1 Y 1 A GLN 870  ? A GLN 870  
184 1 Y 1 A ALA 871  ? A ALA 871  
185 1 Y 1 A GLY 872  ? A GLY 872  
186 1 Y 1 A THR 873  ? A THR 873  
187 1 Y 1 A ALA 1080 ? A ALA 1080 
# 
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 
AGS PG     P N N 1   
AGS S1G    S N N 2   
AGS O2G    O N N 3   
AGS O3G    O N N 4   
AGS PB     P N N 5   
AGS O1B    O N N 6   
AGS O2B    O N N 7   
AGS O3B    O N N 8   
AGS PA     P N N 9   
AGS O1A    O N N 10  
AGS O2A    O N N 11  
AGS O3A    O N N 12  
AGS "O5'"  O N N 13  
AGS "C5'"  C N N 14  
AGS "C4'"  C N R 15  
AGS "O4'"  O N N 16  
AGS "C3'"  C N S 17  
AGS "O3'"  O N N 18  
AGS "C2'"  C N R 19  
AGS "O2'"  O N N 20  
AGS "C1'"  C N R 21  
AGS N9     N Y N 22  
AGS C8     C Y N 23  
AGS N7     N Y N 24  
AGS C5     C Y N 25  
AGS C6     C Y N 26  
AGS N6     N N N 27  
AGS N1     N Y N 28  
AGS C2     C Y N 29  
AGS N3     N Y N 30  
AGS C4     C Y N 31  
AGS HOG2   H N N 32  
AGS H21    H N N 33  
AGS HOB2   H N N 34  
AGS HOA2   H N N 35  
AGS "H5'1" H N N 36  
AGS "H5'2" H N N 37  
AGS "H4'"  H N N 38  
AGS "H3'"  H N N 39  
AGS "HO3'" H N N 40  
AGS "H2'"  H N N 41  
AGS "HO2'" H N N 42  
AGS "H1'"  H N N 43  
AGS H8     H N N 44  
AGS HN61   H N N 45  
AGS HN62   H N N 46  
AGS H2     H N N 47  
ALA N      N N N 48  
ALA CA     C N S 49  
ALA C      C N N 50  
ALA O      O N N 51  
ALA CB     C N N 52  
ALA OXT    O N N 53  
ALA H      H N N 54  
ALA H2     H N N 55  
ALA HA     H N N 56  
ALA HB1    H N N 57  
ALA HB2    H N N 58  
ALA HB3    H N N 59  
ALA HXT    H N N 60  
ARG N      N N N 61  
ARG CA     C N S 62  
ARG C      C N N 63  
ARG O      O N N 64  
ARG CB     C N N 65  
ARG CG     C N N 66  
ARG CD     C N N 67  
ARG NE     N N N 68  
ARG CZ     C N N 69  
ARG NH1    N N N 70  
ARG NH2    N N N 71  
ARG OXT    O N N 72  
ARG H      H N N 73  
ARG H2     H N N 74  
ARG HA     H N N 75  
ARG HB2    H N N 76  
ARG HB3    H N N 77  
ARG HG2    H N N 78  
ARG HG3    H N N 79  
ARG HD2    H N N 80  
ARG HD3    H N N 81  
ARG HE     H N N 82  
ARG HH11   H N N 83  
ARG HH12   H N N 84  
ARG HH21   H N N 85  
ARG HH22   H N N 86  
ARG HXT    H N N 87  
ASN N      N N N 88  
ASN CA     C N S 89  
ASN C      C N N 90  
ASN O      O N N 91  
ASN CB     C N N 92  
ASN CG     C N N 93  
ASN OD1    O N N 94  
ASN ND2    N N N 95  
ASN OXT    O N N 96  
ASN H      H N N 97  
ASN H2     H N N 98  
ASN HA     H N N 99  
ASN HB2    H N N 100 
ASN HB3    H N N 101 
ASN HD21   H N N 102 
ASN HD22   H N N 103 
ASN HXT    H N N 104 
ASP N      N N N 105 
ASP CA     C N S 106 
ASP C      C N N 107 
ASP O      O N N 108 
ASP CB     C N N 109 
ASP CG     C N N 110 
ASP OD1    O N N 111 
ASP OD2    O N N 112 
ASP OXT    O N N 113 
ASP H      H N N 114 
ASP H2     H N N 115 
ASP HA     H N N 116 
ASP HB2    H N N 117 
ASP HB3    H N N 118 
ASP HD2    H N N 119 
ASP HXT    H N N 120 
CYS N      N N N 121 
CYS CA     C N R 122 
CYS C      C N N 123 
CYS O      O N N 124 
CYS CB     C N N 125 
CYS SG     S N N 126 
CYS OXT    O N N 127 
CYS H      H N N 128 
CYS H2     H N N 129 
CYS HA     H N N 130 
CYS HB2    H N N 131 
CYS HB3    H N N 132 
CYS HG     H N N 133 
CYS HXT    H N N 134 
GLN N      N N N 135 
GLN CA     C N S 136 
GLN C      C N N 137 
GLN O      O N N 138 
GLN CB     C N N 139 
GLN CG     C N N 140 
GLN CD     C N N 141 
GLN OE1    O N N 142 
GLN NE2    N N N 143 
GLN OXT    O N N 144 
GLN H      H N N 145 
GLN H2     H N N 146 
GLN HA     H N N 147 
GLN HB2    H N N 148 
GLN HB3    H N N 149 
GLN HG2    H N N 150 
GLN HG3    H N N 151 
GLN HE21   H N N 152 
GLN HE22   H N N 153 
GLN HXT    H N N 154 
GLU N      N N N 155 
GLU CA     C N S 156 
GLU C      C N N 157 
GLU O      O N N 158 
GLU CB     C N N 159 
GLU CG     C N N 160 
GLU CD     C N N 161 
GLU OE1    O N N 162 
GLU OE2    O N N 163 
GLU OXT    O N N 164 
GLU H      H N N 165 
GLU H2     H N N 166 
GLU HA     H N N 167 
GLU HB2    H N N 168 
GLU HB3    H N N 169 
GLU HG2    H N N 170 
GLU HG3    H N N 171 
GLU HE2    H N N 172 
GLU HXT    H N N 173 
GLY N      N N N 174 
GLY CA     C N N 175 
GLY C      C N N 176 
GLY O      O N N 177 
GLY OXT    O N N 178 
GLY H      H N N 179 
GLY H2     H N N 180 
GLY HA2    H N N 181 
GLY HA3    H N N 182 
GLY HXT    H N N 183 
HIS N      N N N 184 
HIS CA     C N S 185 
HIS C      C N N 186 
HIS O      O N N 187 
HIS CB     C N N 188 
HIS CG     C Y N 189 
HIS ND1    N Y N 190 
HIS CD2    C Y N 191 
HIS CE1    C Y N 192 
HIS NE2    N Y N 193 
HIS OXT    O N N 194 
HIS H      H N N 195 
HIS H2     H N N 196 
HIS HA     H N N 197 
HIS HB2    H N N 198 
HIS HB3    H N N 199 
HIS HD1    H N N 200 
HIS HD2    H N N 201 
HIS HE1    H N N 202 
HIS HE2    H N N 203 
HIS HXT    H N N 204 
ILE N      N N N 205 
ILE CA     C N S 206 
ILE C      C N N 207 
ILE O      O N N 208 
ILE CB     C N S 209 
ILE CG1    C N N 210 
ILE CG2    C N N 211 
ILE CD1    C N N 212 
ILE OXT    O N N 213 
ILE H      H N N 214 
ILE H2     H N N 215 
ILE HA     H N N 216 
ILE HB     H N N 217 
ILE HG12   H N N 218 
ILE HG13   H N N 219 
ILE HG21   H N N 220 
ILE HG22   H N N 221 
ILE HG23   H N N 222 
ILE HD11   H N N 223 
ILE HD12   H N N 224 
ILE HD13   H N N 225 
ILE HXT    H N N 226 
LEU N      N N N 227 
LEU CA     C N S 228 
LEU C      C N N 229 
LEU O      O N N 230 
LEU CB     C N N 231 
LEU CG     C N N 232 
LEU CD1    C N N 233 
LEU CD2    C N N 234 
LEU OXT    O N N 235 
LEU H      H N N 236 
LEU H2     H N N 237 
LEU HA     H N N 238 
LEU HB2    H N N 239 
LEU HB3    H N N 240 
LEU HG     H N N 241 
LEU HD11   H N N 242 
LEU HD12   H N N 243 
LEU HD13   H N N 244 
LEU HD21   H N N 245 
LEU HD22   H N N 246 
LEU HD23   H N N 247 
LEU HXT    H N N 248 
LYS N      N N N 249 
LYS CA     C N S 250 
LYS C      C N N 251 
LYS O      O N N 252 
LYS CB     C N N 253 
LYS CG     C N N 254 
LYS CD     C N N 255 
LYS CE     C N N 256 
LYS NZ     N N N 257 
LYS OXT    O N N 258 
LYS H      H N N 259 
LYS H2     H N N 260 
LYS HA     H N N 261 
LYS HB2    H N N 262 
LYS HB3    H N N 263 
LYS HG2    H N N 264 
LYS HG3    H N N 265 
LYS HD2    H N N 266 
LYS HD3    H N N 267 
LYS HE2    H N N 268 
LYS HE3    H N N 269 
LYS HZ1    H N N 270 
LYS HZ2    H N N 271 
LYS HZ3    H N N 272 
LYS HXT    H N N 273 
MET N      N N N 274 
MET CA     C N S 275 
MET C      C N N 276 
MET O      O N N 277 
MET CB     C N N 278 
MET CG     C N N 279 
MET SD     S N N 280 
MET CE     C N N 281 
MET OXT    O N N 282 
MET H      H N N 283 
MET H2     H N N 284 
MET HA     H N N 285 
MET HB2    H N N 286 
MET HB3    H N N 287 
MET HG2    H N N 288 
MET HG3    H N N 289 
MET HE1    H N N 290 
MET HE2    H N N 291 
MET HE3    H N N 292 
MET HXT    H N N 293 
PHE N      N N N 294 
PHE CA     C N S 295 
PHE C      C N N 296 
PHE O      O N N 297 
PHE CB     C N N 298 
PHE CG     C Y N 299 
PHE CD1    C Y N 300 
PHE CD2    C Y N 301 
PHE CE1    C Y N 302 
PHE CE2    C Y N 303 
PHE CZ     C Y N 304 
PHE OXT    O N N 305 
PHE H      H N N 306 
PHE H2     H N N 307 
PHE HA     H N N 308 
PHE HB2    H N N 309 
PHE HB3    H N N 310 
PHE HD1    H N N 311 
PHE HD2    H N N 312 
PHE HE1    H N N 313 
PHE HE2    H N N 314 
PHE HZ     H N N 315 
PHE HXT    H N N 316 
PRO N      N N N 317 
PRO CA     C N S 318 
PRO C      C N N 319 
PRO O      O N N 320 
PRO CB     C N N 321 
PRO CG     C N N 322 
PRO CD     C N N 323 
PRO OXT    O N N 324 
PRO H      H N N 325 
PRO HA     H N N 326 
PRO HB2    H N N 327 
PRO HB3    H N N 328 
PRO HG2    H N N 329 
PRO HG3    H N N 330 
PRO HD2    H N N 331 
PRO HD3    H N N 332 
PRO HXT    H N N 333 
SER N      N N N 334 
SER CA     C N S 335 
SER C      C N N 336 
SER O      O N N 337 
SER CB     C N N 338 
SER OG     O N N 339 
SER OXT    O N N 340 
SER H      H N N 341 
SER H2     H N N 342 
SER HA     H N N 343 
SER HB2    H N N 344 
SER HB3    H N N 345 
SER HG     H N N 346 
SER HXT    H N N 347 
THR N      N N N 348 
THR CA     C N S 349 
THR C      C N N 350 
THR O      O N N 351 
THR CB     C N R 352 
THR OG1    O N N 353 
THR CG2    C N N 354 
THR OXT    O N N 355 
THR H      H N N 356 
THR H2     H N N 357 
THR HA     H N N 358 
THR HB     H N N 359 
THR HG1    H N N 360 
THR HG21   H N N 361 
THR HG22   H N N 362 
THR HG23   H N N 363 
THR HXT    H N N 364 
TRP N      N N N 365 
TRP CA     C N S 366 
TRP C      C N N 367 
TRP O      O N N 368 
TRP CB     C N N 369 
TRP CG     C Y N 370 
TRP CD1    C Y N 371 
TRP CD2    C Y N 372 
TRP NE1    N Y N 373 
TRP CE2    C Y N 374 
TRP CE3    C Y N 375 
TRP CZ2    C Y N 376 
TRP CZ3    C Y N 377 
TRP CH2    C Y N 378 
TRP OXT    O N N 379 
TRP H      H N N 380 
TRP H2     H N N 381 
TRP HA     H N N 382 
TRP HB2    H N N 383 
TRP HB3    H N N 384 
TRP HD1    H N N 385 
TRP HE1    H N N 386 
TRP HE3    H N N 387 
TRP HZ2    H N N 388 
TRP HZ3    H N N 389 
TRP HH2    H N N 390 
TRP HXT    H N N 391 
TYR N      N N N 392 
TYR CA     C N S 393 
TYR C      C N N 394 
TYR O      O N N 395 
TYR CB     C N N 396 
TYR CG     C Y N 397 
TYR CD1    C Y N 398 
TYR CD2    C Y N 399 
TYR CE1    C Y N 400 
TYR CE2    C Y N 401 
TYR CZ     C Y N 402 
TYR OH     O N N 403 
TYR OXT    O N N 404 
TYR H      H N N 405 
TYR H2     H N N 406 
TYR HA     H N N 407 
TYR HB2    H N N 408 
TYR HB3    H N N 409 
TYR HD1    H N N 410 
TYR HD2    H N N 411 
TYR HE1    H N N 412 
TYR HE2    H N N 413 
TYR HH     H N N 414 
TYR HXT    H N N 415 
VAL N      N N N 416 
VAL CA     C N S 417 
VAL C      C N N 418 
VAL O      O N N 419 
VAL CB     C N N 420 
VAL CG1    C N N 421 
VAL CG2    C N N 422 
VAL OXT    O N N 423 
VAL H      H N N 424 
VAL H2     H N N 425 
VAL HA     H N N 426 
VAL HB     H N N 427 
VAL HG11   H N N 428 
VAL HG12   H N N 429 
VAL HG13   H N N 430 
VAL HG21   H N N 431 
VAL HG22   H N N 432 
VAL HG23   H N N 433 
VAL HXT    H N N 434 
# 
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 
AGS PG    S1G    doub N N 1   
AGS PG    O2G    sing N N 2   
AGS PG    O3G    sing N N 3   
AGS PG    O3B    sing N N 4   
AGS PB    O1B    doub N N 5   
AGS PB    O2B    sing N N 6   
AGS PB    O3B    sing N N 7   
AGS PB    O3A    sing N N 8   
AGS PA    O1A    doub N N 9   
AGS PA    O2A    sing N N 10  
AGS PA    O3A    sing N N 11  
AGS PA    "O5'"  sing N N 12  
AGS "O5'" "C5'"  sing N N 13  
AGS "C5'" "C4'"  sing N N 14  
AGS "C4'" "O4'"  sing N N 15  
AGS "C4'" "C3'"  sing N N 16  
AGS "O4'" "C1'"  sing N N 17  
AGS "C3'" "O3'"  sing N N 18  
AGS "C3'" "C2'"  sing N N 19  
AGS "C2'" "O2'"  sing N N 20  
AGS "C2'" "C1'"  sing N N 21  
AGS "C1'" N9     sing N N 22  
AGS N9    C8     sing Y N 23  
AGS N9    C4     sing Y N 24  
AGS C8    N7     doub Y N 25  
AGS N7    C5     sing Y N 26  
AGS C5    C6     sing Y N 27  
AGS C5    C4     doub Y N 28  
AGS C6    N6     sing N N 29  
AGS C6    N1     doub Y N 30  
AGS N1    C2     sing Y N 31  
AGS C2    N3     doub Y N 32  
AGS N3    C4     sing Y N 33  
AGS O2G   HOG2   sing N N 34  
AGS O3G   H21    sing N N 35  
AGS O2B   HOB2   sing N N 36  
AGS O2A   HOA2   sing N N 37  
AGS "C5'" "H5'1" sing N N 38  
AGS "C5'" "H5'2" sing N N 39  
AGS "C4'" "H4'"  sing N N 40  
AGS "C3'" "H3'"  sing N N 41  
AGS "O3'" "HO3'" sing N N 42  
AGS "C2'" "H2'"  sing N N 43  
AGS "O2'" "HO2'" sing N N 44  
AGS "C1'" "H1'"  sing N N 45  
AGS C8    H8     sing N N 46  
AGS N6    HN61   sing N N 47  
AGS N6    HN62   sing N N 48  
AGS C2    H2     sing N N 49  
ALA N     CA     sing N N 50  
ALA N     H      sing N N 51  
ALA N     H2     sing N N 52  
ALA CA    C      sing N N 53  
ALA CA    CB     sing N N 54  
ALA CA    HA     sing N N 55  
ALA C     O      doub N N 56  
ALA C     OXT    sing N N 57  
ALA CB    HB1    sing N N 58  
ALA CB    HB2    sing N N 59  
ALA CB    HB3    sing N N 60  
ALA OXT   HXT    sing N N 61  
ARG N     CA     sing N N 62  
ARG N     H      sing N N 63  
ARG N     H2     sing N N 64  
ARG CA    C      sing N N 65  
ARG CA    CB     sing N N 66  
ARG CA    HA     sing N N 67  
ARG C     O      doub N N 68  
ARG C     OXT    sing N N 69  
ARG CB    CG     sing N N 70  
ARG CB    HB2    sing N N 71  
ARG CB    HB3    sing N N 72  
ARG CG    CD     sing N N 73  
ARG CG    HG2    sing N N 74  
ARG CG    HG3    sing N N 75  
ARG CD    NE     sing N N 76  
ARG CD    HD2    sing N N 77  
ARG CD    HD3    sing N N 78  
ARG NE    CZ     sing N N 79  
ARG NE    HE     sing N N 80  
ARG CZ    NH1    sing N N 81  
ARG CZ    NH2    doub N N 82  
ARG NH1   HH11   sing N N 83  
ARG NH1   HH12   sing N N 84  
ARG NH2   HH21   sing N N 85  
ARG NH2   HH22   sing N N 86  
ARG OXT   HXT    sing N N 87  
ASN N     CA     sing N N 88  
ASN N     H      sing N N 89  
ASN N     H2     sing N N 90  
ASN CA    C      sing N N 91  
ASN CA    CB     sing N N 92  
ASN CA    HA     sing N N 93  
ASN C     O      doub N N 94  
ASN C     OXT    sing N N 95  
ASN CB    CG     sing N N 96  
ASN CB    HB2    sing N N 97  
ASN CB    HB3    sing N N 98  
ASN CG    OD1    doub N N 99  
ASN CG    ND2    sing N N 100 
ASN ND2   HD21   sing N N 101 
ASN ND2   HD22   sing N N 102 
ASN OXT   HXT    sing N N 103 
ASP N     CA     sing N N 104 
ASP N     H      sing N N 105 
ASP N     H2     sing N N 106 
ASP CA    C      sing N N 107 
ASP CA    CB     sing N N 108 
ASP CA    HA     sing N N 109 
ASP C     O      doub N N 110 
ASP C     OXT    sing N N 111 
ASP CB    CG     sing N N 112 
ASP CB    HB2    sing N N 113 
ASP CB    HB3    sing N N 114 
ASP CG    OD1    doub N N 115 
ASP CG    OD2    sing N N 116 
ASP OD2   HD2    sing N N 117 
ASP OXT   HXT    sing N N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GLN N     CA     sing N N 132 
GLN N     H      sing N N 133 
GLN N     H2     sing N N 134 
GLN CA    C      sing N N 135 
GLN CA    CB     sing N N 136 
GLN CA    HA     sing N N 137 
GLN C     O      doub N N 138 
GLN C     OXT    sing N N 139 
GLN CB    CG     sing N N 140 
GLN CB    HB2    sing N N 141 
GLN CB    HB3    sing N N 142 
GLN CG    CD     sing N N 143 
GLN CG    HG2    sing N N 144 
GLN CG    HG3    sing N N 145 
GLN CD    OE1    doub N N 146 
GLN CD    NE2    sing N N 147 
GLN NE2   HE21   sing N N 148 
GLN NE2   HE22   sing N N 149 
GLN OXT   HXT    sing N N 150 
GLU N     CA     sing N N 151 
GLU N     H      sing N N 152 
GLU N     H2     sing N N 153 
GLU CA    C      sing N N 154 
GLU CA    CB     sing N N 155 
GLU CA    HA     sing N N 156 
GLU C     O      doub N N 157 
GLU C     OXT    sing N N 158 
GLU CB    CG     sing N N 159 
GLU CB    HB2    sing N N 160 
GLU CB    HB3    sing N N 161 
GLU CG    CD     sing N N 162 
GLU CG    HG2    sing N N 163 
GLU CG    HG3    sing N N 164 
GLU CD    OE1    doub N N 165 
GLU CD    OE2    sing N N 166 
GLU OE2   HE2    sing N N 167 
GLU OXT   HXT    sing N N 168 
GLY N     CA     sing N N 169 
GLY N     H      sing N N 170 
GLY N     H2     sing N N 171 
GLY CA    C      sing N N 172 
GLY CA    HA2    sing N N 173 
GLY CA    HA3    sing N N 174 
GLY C     O      doub N N 175 
GLY C     OXT    sing N N 176 
GLY OXT   HXT    sing N N 177 
HIS N     CA     sing N N 178 
HIS N     H      sing N N 179 
HIS N     H2     sing N N 180 
HIS CA    C      sing N N 181 
HIS CA    CB     sing N N 182 
HIS CA    HA     sing N N 183 
HIS C     O      doub N N 184 
HIS C     OXT    sing N N 185 
HIS CB    CG     sing N N 186 
HIS CB    HB2    sing N N 187 
HIS CB    HB3    sing N N 188 
HIS CG    ND1    sing Y N 189 
HIS CG    CD2    doub Y N 190 
HIS ND1   CE1    doub Y N 191 
HIS ND1   HD1    sing N N 192 
HIS CD2   NE2    sing Y N 193 
HIS CD2   HD2    sing N N 194 
HIS CE1   NE2    sing Y N 195 
HIS CE1   HE1    sing N N 196 
HIS NE2   HE2    sing N N 197 
HIS OXT   HXT    sing N N 198 
ILE N     CA     sing N N 199 
ILE N     H      sing N N 200 
ILE N     H2     sing N N 201 
ILE CA    C      sing N N 202 
ILE CA    CB     sing N N 203 
ILE CA    HA     sing N N 204 
ILE C     O      doub N N 205 
ILE C     OXT    sing N N 206 
ILE CB    CG1    sing N N 207 
ILE CB    CG2    sing N N 208 
ILE CB    HB     sing N N 209 
ILE CG1   CD1    sing N N 210 
ILE CG1   HG12   sing N N 211 
ILE CG1   HG13   sing N N 212 
ILE CG2   HG21   sing N N 213 
ILE CG2   HG22   sing N N 214 
ILE CG2   HG23   sing N N 215 
ILE CD1   HD11   sing N N 216 
ILE CD1   HD12   sing N N 217 
ILE CD1   HD13   sing N N 218 
ILE OXT   HXT    sing N N 219 
LEU N     CA     sing N N 220 
LEU N     H      sing N N 221 
LEU N     H2     sing N N 222 
LEU CA    C      sing N N 223 
LEU CA    CB     sing N N 224 
LEU CA    HA     sing N N 225 
LEU C     O      doub N N 226 
LEU C     OXT    sing N N 227 
LEU CB    CG     sing N N 228 
LEU CB    HB2    sing N N 229 
LEU CB    HB3    sing N N 230 
LEU CG    CD1    sing N N 231 
LEU CG    CD2    sing N N 232 
LEU CG    HG     sing N N 233 
LEU CD1   HD11   sing N N 234 
LEU CD1   HD12   sing N N 235 
LEU CD1   HD13   sing N N 236 
LEU CD2   HD21   sing N N 237 
LEU CD2   HD22   sing N N 238 
LEU CD2   HD23   sing N N 239 
LEU OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
THR N     CA     sing N N 337 
THR N     H      sing N N 338 
THR N     H2     sing N N 339 
THR CA    C      sing N N 340 
THR CA    CB     sing N N 341 
THR CA    HA     sing N N 342 
THR C     O      doub N N 343 
THR C     OXT    sing N N 344 
THR CB    OG1    sing N N 345 
THR CB    CG2    sing N N 346 
THR CB    HB     sing N N 347 
THR OG1   HG1    sing N N 348 
THR CG2   HG21   sing N N 349 
THR CG2   HG22   sing N N 350 
THR CG2   HG23   sing N N 351 
THR OXT   HXT    sing N N 352 
TRP N     CA     sing N N 353 
TRP N     H      sing N N 354 
TRP N     H2     sing N N 355 
TRP CA    C      sing N N 356 
TRP CA    CB     sing N N 357 
TRP CA    HA     sing N N 358 
TRP C     O      doub N N 359 
TRP C     OXT    sing N N 360 
TRP CB    CG     sing N N 361 
TRP CB    HB2    sing N N 362 
TRP CB    HB3    sing N N 363 
TRP CG    CD1    doub Y N 364 
TRP CG    CD2    sing Y N 365 
TRP CD1   NE1    sing Y N 366 
TRP CD1   HD1    sing N N 367 
TRP CD2   CE2    doub Y N 368 
TRP CD2   CE3    sing Y N 369 
TRP NE1   CE2    sing Y N 370 
TRP NE1   HE1    sing N N 371 
TRP CE2   CZ2    sing Y N 372 
TRP CE3   CZ3    doub Y N 373 
TRP CE3   HE3    sing N N 374 
TRP CZ2   CH2    doub Y N 375 
TRP CZ2   HZ2    sing N N 376 
TRP CZ3   CH2    sing Y N 377 
TRP CZ3   HZ3    sing N N 378 
TRP CH2   HH2    sing N N 379 
TRP OXT   HXT    sing N N 380 
TYR N     CA     sing N N 381 
TYR N     H      sing N N 382 
TYR N     H2     sing N N 383 
TYR CA    C      sing N N 384 
TYR CA    CB     sing N N 385 
TYR CA    HA     sing N N 386 
TYR C     O      doub N N 387 
TYR C     OXT    sing N N 388 
TYR CB    CG     sing N N 389 
TYR CB    HB2    sing N N 390 
TYR CB    HB3    sing N N 391 
TYR CG    CD1    doub Y N 392 
TYR CG    CD2    sing Y N 393 
TYR CD1   CE1    sing Y N 394 
TYR CD1   HD1    sing N N 395 
TYR CD2   CE2    doub Y N 396 
TYR CD2   HD2    sing N N 397 
TYR CE1   CZ     doub Y N 398 
TYR CE1   HE1    sing N N 399 
TYR CE2   CZ     sing Y N 400 
TYR CE2   HE2    sing N N 401 
TYR CZ    OH     sing N N 402 
TYR OH    HH     sing N N 403 
TYR OXT   HXT    sing N N 404 
VAL N     CA     sing N N 405 
VAL N     H      sing N N 406 
VAL N     H2     sing N N 407 
VAL CA    C      sing N N 408 
VAL CA    CB     sing N N 409 
VAL CA    HA     sing N N 410 
VAL C     O      doub N N 411 
VAL C     OXT    sing N N 412 
VAL CB    CG1    sing N N 413 
VAL CB    CG2    sing N N 414 
VAL CB    HB     sing N N 415 
VAL CG1   HG11   sing N N 416 
VAL CG1   HG12   sing N N 417 
VAL CG1   HG13   sing N N 418 
VAL CG2   HG21   sing N N 419 
VAL CG2   HG22   sing N N 420 
VAL CG2   HG23   sing N N 421 
VAL OXT   HXT    sing N N 422 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-10-25 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           8QYC 
_em_admin.last_update        2025-02-12 
_em_admin.map_release_date   2024-11-06 
_em_admin.title              'Zorya anti-bacteriophage defense system ZorD in complex with ATP-gamma-S' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          562 
_em_entity_assembly_naturalsource.organism             'Escherichia coli' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON II (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Novo Nordisk Foundation' Denmark NNF17OC0031006 1 
'Novo Nordisk Foundation' Denmark NNF21OC0071948 2 
Lundbeckfonden            Denmark R347-2020-2429 3 
# 
_atom_sites.entry_id                    8QYC 
_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]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_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 
H 
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     . LYS A 1 21   ? 171.903 205.918 167.981 1.00 86.00  ? 21   LYS A N     1 
ATOM   2    C CA    . LYS A 1 21   ? 170.465 205.679 168.043 1.00 86.40  ? 21   LYS A CA    1 
ATOM   3    C C     . LYS A 1 21   ? 170.148 204.191 167.959 1.00 79.23  ? 21   LYS A C     1 
ATOM   4    O O     . LYS A 1 21   ? 170.644 203.489 167.079 1.00 71.91  ? 21   LYS A O     1 
ATOM   5    C CB    . LYS A 1 21   ? 169.749 206.430 166.919 1.00 86.80  ? 21   LYS A CB    1 
ATOM   6    C CG    . LYS A 1 21   ? 168.255 206.158 166.847 1.00 87.36  ? 21   LYS A CG    1 
ATOM   7    C CD    . LYS A 1 21   ? 167.623 206.843 165.648 1.00 87.09  ? 21   LYS A CD    1 
ATOM   8    C CE    . LYS A 1 21   ? 166.139 206.532 165.556 1.00 85.83  ? 21   LYS A CE    1 
ATOM   9    N NZ    . LYS A 1 21   ? 165.507 207.192 164.381 1.00 86.15  ? 21   LYS A NZ    1 
ATOM   10   N N     . ASN A 1 22   ? 169.319 203.715 168.883 1.00 76.64  ? 22   ASN A N     1 
ATOM   11   C CA    . ASN A 1 22   ? 168.891 202.325 168.894 1.00 70.14  ? 22   ASN A CA    1 
ATOM   12   C C     . ASN A 1 22   ? 167.614 202.164 168.082 1.00 67.83  ? 22   ASN A C     1 
ATOM   13   O O     . ASN A 1 22   ? 166.717 203.009 168.136 1.00 70.52  ? 22   ASN A O     1 
ATOM   14   C CB    . ASN A 1 22   ? 168.669 201.840 170.327 1.00 64.74  ? 22   ASN A CB    1 
ATOM   15   C CG    . ASN A 1 22   ? 169.946 201.833 171.142 1.00 73.63  ? 22   ASN A CG    1 
ATOM   16   O OD1   . ASN A 1 22   ? 171.021 201.526 170.627 1.00 74.21  ? 22   ASN A OD1   1 
ATOM   17   N ND2   . ASN A 1 22   ? 169.835 202.176 172.419 1.00 70.85  ? 22   ASN A ND2   1 
ATOM   18   N N     . GLN A 1 23   ? 167.540 201.070 167.326 1.00 65.18  ? 23   GLN A N     1 
ATOM   19   C CA    . GLN A 1 23   ? 166.382 200.802 166.485 1.00 67.82  ? 23   GLN A CA    1 
ATOM   20   C C     . GLN A 1 23   ? 165.217 200.194 167.254 1.00 64.83  ? 23   GLN A C     1 
ATOM   21   O O     . GLN A 1 23   ? 164.134 200.036 166.682 1.00 61.09  ? 23   GLN A O     1 
ATOM   22   C CB    . GLN A 1 23   ? 166.776 199.872 165.336 1.00 68.72  ? 23   GLN A CB    1 
ATOM   23   C CG    . GLN A 1 23   ? 168.014 200.315 164.567 1.00 71.04  ? 23   GLN A CG    1 
ATOM   24   C CD    . GLN A 1 23   ? 167.776 201.558 163.731 1.00 74.61  ? 23   GLN A CD    1 
ATOM   25   O OE1   . GLN A 1 23   ? 166.634 201.941 163.472 1.00 67.06  ? 23   GLN A OE1   1 
ATOM   26   N NE2   . GLN A 1 23   ? 168.859 202.195 163.302 1.00 71.33  ? 23   GLN A NE2   1 
ATOM   27   N N     . TYR A 1 24   ? 165.411 199.856 168.524 1.00 62.56  ? 24   TYR A N     1 
ATOM   28   C CA    . TYR A 1 24   ? 164.408 199.183 169.332 1.00 53.60  ? 24   TYR A CA    1 
ATOM   29   C C     . TYR A 1 24   ? 164.016 200.048 170.521 1.00 58.90  ? 24   TYR A C     1 
ATOM   30   O O     . TYR A 1 24   ? 164.782 200.898 170.981 1.00 62.77  ? 24   TYR A O     1 
ATOM   31   C CB    . TYR A 1 24   ? 164.921 197.827 169.830 1.00 47.16  ? 24   TYR A CB    1 
ATOM   32   C CG    . TYR A 1 24   ? 166.319 197.882 170.405 1.00 48.83  ? 24   TYR A CG    1 
ATOM   33   C CD1   . TYR A 1 24   ? 166.539 198.287 171.714 1.00 53.28  ? 24   TYR A CD1   1 
ATOM   34   C CD2   . TYR A 1 24   ? 167.421 197.530 169.637 1.00 46.82  ? 24   TYR A CD2   1 
ATOM   35   C CE1   . TYR A 1 24   ? 167.812 198.342 172.241 1.00 49.74  ? 24   TYR A CE1   1 
ATOM   36   C CE2   . TYR A 1 24   ? 168.698 197.580 170.156 1.00 44.13  ? 24   TYR A CE2   1 
ATOM   37   C CZ    . TYR A 1 24   ? 168.887 197.987 171.458 1.00 48.04  ? 24   TYR A CZ    1 
ATOM   38   O OH    . TYR A 1 24   ? 170.157 198.040 171.982 1.00 52.02  ? 24   TYR A OH    1 
ATOM   39   N N     . GLN A 1 25   ? 162.804 199.819 171.014 1.00 58.72  ? 25   GLN A N     1 
ATOM   40   C CA    . GLN A 1 25   ? 162.334 200.419 172.254 1.00 55.42  ? 25   GLN A CA    1 
ATOM   41   C C     . GLN A 1 25   ? 162.380 199.355 173.342 1.00 52.37  ? 25   GLN A C     1 
ATOM   42   O O     . GLN A 1 25   ? 161.742 198.304 173.215 1.00 54.64  ? 25   GLN A O     1 
ATOM   43   C CB    . GLN A 1 25   ? 160.921 200.981 172.102 1.00 57.47  ? 25   GLN A CB    1 
ATOM   44   C CG    . GLN A 1 25   ? 160.804 202.136 171.115 1.00 65.00  ? 25   GLN A CG    1 
ATOM   45   C CD    . GLN A 1 25   ? 160.716 201.673 169.673 1.00 69.19  ? 25   GLN A CD    1 
ATOM   46   O OE1   . GLN A 1 25   ? 160.215 200.585 169.388 1.00 66.96  ? 25   GLN A OE1   1 
ATOM   47   N NE2   . GLN A 1 25   ? 161.206 202.499 168.756 1.00 64.61  ? 25   GLN A NE2   1 
ATOM   48   N N     . VAL A 1 26   ? 163.138 199.622 174.400 1.00 53.84  ? 26   VAL A N     1 
ATOM   49   C CA    . VAL A 1 26   ? 163.314 198.657 175.478 1.00 50.84  ? 26   VAL A CA    1 
ATOM   50   C C     . VAL A 1 26   ? 162.095 198.697 176.388 1.00 53.29  ? 26   VAL A C     1 
ATOM   51   O O     . VAL A 1 26   ? 161.653 199.773 176.809 1.00 53.43  ? 26   VAL A O     1 
ATOM   52   C CB    . VAL A 1 26   ? 164.603 198.945 176.263 1.00 45.14  ? 26   VAL A CB    1 
ATOM   53   C CG1   . VAL A 1 26   ? 164.814 197.894 177.339 1.00 44.63  ? 26   VAL A CG1   1 
ATOM   54   C CG2   . VAL A 1 26   ? 165.794 199.003 175.323 1.00 47.65  ? 26   VAL A CG2   1 
ATOM   55   N N     . GLU A 1 27   ? 161.549 197.524 176.696 1.00 49.90  ? 27   GLU A N     1 
ATOM   56   C CA    . GLU A 1 27   ? 160.429 197.419 177.618 1.00 52.92  ? 27   GLU A CA    1 
ATOM   57   C C     . GLU A 1 27   ? 160.686 196.241 178.550 1.00 51.68  ? 27   GLU A C     1 
ATOM   58   O O     . GLU A 1 27   ? 161.670 195.511 178.405 1.00 52.19  ? 27   GLU A O     1 
ATOM   59   C CB    . GLU A 1 27   ? 159.102 197.289 176.861 1.00 56.86  ? 27   GLU A CB    1 
ATOM   60   C CG    . GLU A 1 27   ? 158.924 195.998 176.088 1.00 54.75  ? 27   GLU A CG    1 
ATOM   61   C CD    . GLU A 1 27   ? 157.813 195.142 176.656 1.00 62.80  ? 27   GLU A CD    1 
ATOM   62   O OE1   . GLU A 1 27   ? 157.561 195.227 177.876 1.00 60.04  ? 27   GLU A OE1   1 
ATOM   63   O OE2   . GLU A 1 27   ? 157.183 194.390 175.883 1.00 64.68  ? 27   GLU A OE2   1 
ATOM   64   N N     . GLU A 1 28   ? 159.791 196.065 179.524 1.00 53.27  ? 28   GLU A N     1 
ATOM   65   C CA    . GLU A 1 28   ? 160.009 195.070 180.569 1.00 52.11  ? 28   GLU A CA    1 
ATOM   66   C C     . GLU A 1 28   ? 159.948 193.639 180.050 1.00 51.78  ? 28   GLU A C     1 
ATOM   67   O O     . GLU A 1 28   ? 160.413 192.727 180.742 1.00 53.83  ? 28   GLU A O     1 
ATOM   68   C CB    . GLU A 1 28   ? 158.987 195.251 181.693 1.00 53.55  ? 28   GLU A CB    1 
ATOM   69   C CG    . GLU A 1 28   ? 159.028 196.616 182.367 1.00 65.73  ? 28   GLU A CG    1 
ATOM   70   C CD    . GLU A 1 28   ? 160.277 196.830 183.206 1.00 68.02  ? 28   GLU A CD    1 
ATOM   71   O OE1   . GLU A 1 28   ? 160.942 195.835 183.563 1.00 66.34  ? 28   GLU A OE1   1 
ATOM   72   O OE2   . GLU A 1 28   ? 160.591 198.000 183.512 1.00 62.37  ? 28   GLU A OE2   1 
ATOM   73   N N     . ASN A 1 29   ? 159.391 193.415 178.862 1.00 48.39  ? 29   ASN A N     1 
ATOM   74   C CA    . ASN A 1 29   ? 159.240 192.071 178.325 1.00 44.62  ? 29   ASN A CA    1 
ATOM   75   C C     . ASN A 1 29   ? 160.211 191.758 177.195 1.00 44.20  ? 29   ASN A C     1 
ATOM   76   O O     . ASN A 1 29   ? 160.256 190.610 176.741 1.00 45.40  ? 29   ASN A O     1 
ATOM   77   C CB    . ASN A 1 29   ? 157.801 191.852 177.845 1.00 54.07  ? 29   ASN A CB    1 
ATOM   78   C CG    . ASN A 1 29   ? 156.802 191.838 178.985 1.00 59.35  ? 29   ASN A CG    1 
ATOM   79   O OD1   . ASN A 1 29   ? 156.530 190.792 179.574 1.00 60.19  ? 29   ASN A OD1   1 
ATOM   80   N ND2   . ASN A 1 29   ? 156.249 193.002 179.303 1.00 58.96  ? 29   ASN A ND2   1 
ATOM   81   N N     . GLY A 1 30   ? 160.981 192.728 176.733 1.00 45.68  ? 30   GLY A N     1 
ATOM   82   C CA    . GLY A 1 30   ? 161.956 192.491 175.690 1.00 43.23  ? 30   GLY A CA    1 
ATOM   83   C C     . GLY A 1 30   ? 162.216 193.757 174.900 1.00 44.02  ? 30   GLY A C     1 
ATOM   84   O O     . GLY A 1 30   ? 161.819 194.850 175.291 1.00 50.27  ? 30   GLY A O     1 
ATOM   85   N N     . LEU A 1 31   ? 162.909 193.582 173.779 1.00 43.22  ? 31   LEU A N     1 
ATOM   86   C CA    . LEU A 1 31   ? 163.149 194.667 172.840 1.00 42.87  ? 31   LEU A CA    1 
ATOM   87   C C     . LEU A 1 31   ? 162.031 194.696 171.808 1.00 44.78  ? 31   LEU A C     1 
ATOM   88   O O     . LEU A 1 31   ? 161.658 193.660 171.251 1.00 49.96  ? 31   LEU A O     1 
ATOM   89   C CB    . LEU A 1 31   ? 164.502 194.500 172.147 1.00 44.91  ? 31   LEU A CB    1 
ATOM   90   C CG    . LEU A 1 31   ? 165.726 194.350 173.053 1.00 39.26  ? 31   LEU A CG    1 
ATOM   91   C CD1   . LEU A 1 31   ? 166.985 194.144 172.226 1.00 40.06  ? 31   LEU A CD1   1 
ATOM   92   C CD2   . LEU A 1 31   ? 165.874 195.555 173.963 1.00 38.11  ? 31   LEU A CD2   1 
ATOM   93   N N     . SER A 1 32   ? 161.494 195.886 171.560 1.00 46.50  ? 32   SER A N     1 
ATOM   94   C CA    . SER A 1 32   ? 160.342 196.053 170.689 1.00 48.93  ? 32   SER A CA    1 
ATOM   95   C C     . SER A 1 32   ? 160.733 196.829 169.441 1.00 54.17  ? 32   SER A C     1 
ATOM   96   O O     . SER A 1 32   ? 161.438 197.839 169.522 1.00 57.79  ? 32   SER A O     1 
ATOM   97   C CB    . SER A 1 32   ? 159.200 196.769 171.412 1.00 58.16  ? 32   SER A CB    1 
ATOM   98   O OG    . SER A 1 32   ? 159.602 198.053 171.852 1.00 66.79  ? 32   SER A OG    1 
ATOM   99   N N     . PHE A 1 33   ? 160.266 196.353 168.291 1.00 55.30  ? 33   PHE A N     1 
ATOM   100  C CA    . PHE A 1 33   ? 160.547 196.968 167.010 1.00 51.55  ? 33   PHE A CA    1 
ATOM   101  C C     . PHE A 1 33   ? 159.244 197.382 166.342 1.00 59.15  ? 33   PHE A C     1 
ATOM   102  O O     . PHE A 1 33   ? 158.319 196.563 166.240 1.00 63.25  ? 33   PHE A O     1 
ATOM   103  C CB    . PHE A 1 33   ? 161.316 196.004 166.099 1.00 49.04  ? 33   PHE A CB    1 
ATOM   104  C CG    . PHE A 1 33   ? 162.632 195.562 166.664 1.00 47.62  ? 33   PHE A CG    1 
ATOM   105  C CD1   . PHE A 1 33   ? 163.776 196.308 166.448 1.00 45.10  ? 33   PHE A CD1   1 
ATOM   106  C CD2   . PHE A 1 33   ? 162.724 194.404 167.414 1.00 44.32  ? 33   PHE A CD2   1 
ATOM   107  C CE1   . PHE A 1 33   ? 164.986 195.907 166.968 1.00 41.79  ? 33   PHE A CE1   1 
ATOM   108  C CE2   . PHE A 1 33   ? 163.933 193.997 167.938 1.00 40.65  ? 33   PHE A CE2   1 
ATOM   109  C CZ    . PHE A 1 33   ? 165.066 194.750 167.715 1.00 37.41  ? 33   PHE A CZ    1 
ATOM   110  N N     . PRO A 1 34   ? 159.124 198.624 165.884 1.00 63.08  ? 34   PRO A N     1 
ATOM   111  C CA    . PRO A 1 34   ? 157.881 199.056 165.240 1.00 58.83  ? 34   PRO A CA    1 
ATOM   112  C C     . PRO A 1 34   ? 157.673 198.374 163.897 1.00 64.15  ? 34   PRO A C     1 
ATOM   113  O O     . PRO A 1 34   ? 158.615 197.975 163.211 1.00 66.97  ? 34   PRO A O     1 
ATOM   114  C CB    . PRO A 1 34   ? 158.079 200.565 165.070 1.00 58.34  ? 34   PRO A CB    1 
ATOM   115  C CG    . PRO A 1 34   ? 159.558 200.738 165.003 1.00 61.85  ? 34   PRO A CG    1 
ATOM   116  C CD    . PRO A 1 34   ? 160.132 199.697 165.924 1.00 63.47  ? 34   PRO A CD    1 
ATOM   117  N N     . LEU A 1 35   ? 156.398 198.243 163.527 1.00 69.60  ? 35   LEU A N     1 
ATOM   118  C CA    . LEU A 1 35   ? 156.045 197.712 162.217 1.00 71.64  ? 35   LEU A CA    1 
ATOM   119  C C     . LEU A 1 35   ? 156.311 198.702 161.091 1.00 70.56  ? 35   LEU A C     1 
ATOM   120  O O     . LEU A 1 35   ? 156.311 198.298 159.924 1.00 71.04  ? 35   LEU A O     1 
ATOM   121  C CB    . LEU A 1 35   ? 154.574 197.294 162.198 1.00 71.84  ? 35   LEU A CB    1 
ATOM   122  C CG    . LEU A 1 35   ? 154.271 195.797 162.277 1.00 68.56  ? 35   LEU A CG    1 
ATOM   123  C CD1   . LEU A 1 35   ? 154.880 195.063 161.092 1.00 64.54  ? 35   LEU A CD1   1 
ATOM   124  C CD2   . LEU A 1 35   ? 154.765 195.209 163.584 1.00 60.48  ? 35   LEU A CD2   1 
ATOM   125  N N     . SER A 1 36   ? 156.537 199.978 161.409 1.00 69.16  ? 36   SER A N     1 
ATOM   126  C CA    . SER A 1 36   ? 156.773 200.992 160.390 1.00 71.50  ? 36   SER A CA    1 
ATOM   127  C C     . SER A 1 36   ? 158.128 200.852 159.711 1.00 77.43  ? 36   SER A C     1 
ATOM   128  O O     . SER A 1 36   ? 158.374 201.542 158.716 1.00 80.46  ? 36   SER A O     1 
ATOM   129  C CB    . SER A 1 36   ? 156.653 202.388 161.003 1.00 72.65  ? 36   SER A CB    1 
ATOM   130  O OG    . SER A 1 36   ? 157.633 202.588 162.008 1.00 75.41  ? 36   SER A OG    1 
ATOM   131  N N     . LEU A 1 37   ? 159.012 199.992 160.224 1.00 74.10  ? 37   LEU A N     1 
ATOM   132  C CA    . LEU A 1 37   ? 160.321 199.822 159.604 1.00 73.48  ? 37   LEU A CA    1 
ATOM   133  C C     . LEU A 1 37   ? 160.212 199.216 158.210 1.00 75.02  ? 37   LEU A C     1 
ATOM   134  O O     . LEU A 1 37   ? 161.074 199.468 157.360 1.00 75.36  ? 37   LEU A O     1 
ATOM   135  C CB    . LEU A 1 37   ? 161.217 198.963 160.496 1.00 64.89  ? 37   LEU A CB    1 
ATOM   136  C CG    . LEU A 1 37   ? 161.551 199.582 161.854 1.00 69.25  ? 37   LEU A CG    1 
ATOM   137  C CD1   . LEU A 1 37   ? 162.470 198.678 162.655 1.00 62.54  ? 37   LEU A CD1   1 
ATOM   138  C CD2   . LEU A 1 37   ? 162.173 200.958 161.675 1.00 68.24  ? 37   LEU A CD2   1 
ATOM   139  N N     . VAL A 1 38   ? 159.171 198.420 157.955 1.00 74.90  ? 38   VAL A N     1 
ATOM   140  C CA    . VAL A 1 38   ? 158.978 197.865 156.621 1.00 79.79  ? 38   VAL A CA    1 
ATOM   141  C C     . VAL A 1 38   ? 158.635 198.949 155.609 1.00 83.44  ? 38   VAL A C     1 
ATOM   142  O O     . VAL A 1 38   ? 158.802 198.740 154.402 1.00 87.10  ? 38   VAL A O     1 
ATOM   143  C CB    . VAL A 1 38   ? 157.894 196.771 156.637 1.00 84.67  ? 38   VAL A CB    1 
ATOM   144  C CG1   . VAL A 1 38   ? 158.196 195.741 157.714 1.00 73.33  ? 38   VAL A CG1   1 
ATOM   145  C CG2   . VAL A 1 38   ? 156.516 197.381 156.840 1.00 84.79  ? 38   VAL A CG2   1 
ATOM   146  N N     . ASP A 1 39   ? 158.158 200.104 156.068 1.00 83.28  ? 39   ASP A N     1 
ATOM   147  C CA    . ASP A 1 39   ? 157.825 201.219 155.193 1.00 85.38  ? 39   ASP A CA    1 
ATOM   148  C C     . ASP A 1 39   ? 158.997 202.165 154.971 1.00 85.68  ? 39   ASP A C     1 
ATOM   149  O O     . ASP A 1 39   ? 158.845 203.160 154.255 1.00 82.38  ? 39   ASP A O     1 
ATOM   150  C CB    . ASP A 1 39   ? 156.635 201.998 155.762 1.00 83.45  ? 39   ASP A CB    1 
ATOM   151  C CG    . ASP A 1 39   ? 155.414 201.125 155.974 1.00 86.46  ? 39   ASP A CG    1 
ATOM   152  O OD1   . ASP A 1 39   ? 155.249 200.137 155.228 1.00 85.96  ? 39   ASP A OD1   1 
ATOM   153  O OD2   . ASP A 1 39   ? 154.618 201.427 156.887 1.00 85.79  ? 39   ASP A OD2   1 
ATOM   154  N N     . ASP A 1 40   ? 160.153 201.884 155.566 1.00 83.92  ? 40   ASP A N     1 
ATOM   155  C CA    . ASP A 1 40   ? 161.350 202.695 155.391 1.00 78.30  ? 40   ASP A CA    1 
ATOM   156  C C     . ASP A 1 40   ? 162.243 202.022 154.356 1.00 75.57  ? 40   ASP A C     1 
ATOM   157  O O     . ASP A 1 40   ? 162.622 200.857 154.520 1.00 66.81  ? 40   ASP A O     1 
ATOM   158  C CB    . ASP A 1 40   ? 162.088 202.868 156.718 1.00 74.52  ? 40   ASP A CB    1 
ATOM   159  C CG    . ASP A 1 40   ? 163.081 204.016 156.693 1.00 76.25  ? 40   ASP A CG    1 
ATOM   160  O OD1   . ASP A 1 40   ? 163.653 204.298 155.620 1.00 76.13  ? 40   ASP A OD1   1 
ATOM   161  O OD2   . ASP A 1 40   ? 163.289 204.640 157.755 1.00 77.07  ? 40   ASP A OD2   1 
ATOM   162  N N     . SER A 1 41   ? 162.569 202.753 153.289 1.00 75.53  ? 41   SER A N     1 
ATOM   163  C CA    . SER A 1 41   ? 163.396 202.193 152.227 1.00 72.16  ? 41   SER A CA    1 
ATOM   164  C C     . SER A 1 41   ? 164.867 202.123 152.615 1.00 66.80  ? 41   SER A C     1 
ATOM   165  O O     . SER A 1 41   ? 165.588 201.245 152.130 1.00 67.42  ? 41   SER A O     1 
ATOM   166  C CB    . SER A 1 41   ? 163.228 203.012 150.946 1.00 73.25  ? 41   SER A CB    1 
ATOM   167  O OG    . SER A 1 41   ? 163.556 204.373 151.163 1.00 74.31  ? 41   SER A OG    1 
ATOM   168  N N     . GLN A 1 42   ? 165.331 203.031 153.476 1.00 63.68  ? 42   GLN A N     1 
ATOM   169  C CA    . GLN A 1 42   ? 166.732 203.030 153.880 1.00 64.26  ? 42   GLN A CA    1 
ATOM   170  C C     . GLN A 1 42   ? 167.045 201.921 154.876 1.00 62.68  ? 42   GLN A C     1 
ATOM   171  O O     . GLN A 1 42   ? 168.210 201.528 155.003 1.00 60.33  ? 42   GLN A O     1 
ATOM   172  C CB    . GLN A 1 42   ? 167.100 204.394 154.469 1.00 68.76  ? 42   GLN A CB    1 
ATOM   173  C CG    . GLN A 1 42   ? 168.589 204.615 154.681 1.00 76.46  ? 42   GLN A CG    1 
ATOM   174  C CD    . GLN A 1 42   ? 168.911 206.044 155.069 1.00 81.37  ? 42   GLN A CD    1 
ATOM   175  O OE1   . GLN A 1 42   ? 168.720 206.971 154.282 1.00 79.11  ? 42   GLN A OE1   1 
ATOM   176  N NE2   . GLN A 1 42   ? 169.397 206.231 156.291 1.00 79.50  ? 42   GLN A NE2   1 
ATOM   177  N N     . LEU A 1 43   ? 166.037 201.402 155.573 1.00 58.63  ? 43   LEU A N     1 
ATOM   178  C CA    . LEU A 1 43   ? 166.203 200.320 156.541 1.00 53.35  ? 43   LEU A CA    1 
ATOM   179  C C     . LEU A 1 43   ? 165.704 198.991 155.991 1.00 46.01  ? 43   LEU A C     1 
ATOM   180  O O     . LEU A 1 43   ? 165.071 198.212 156.707 1.00 47.35  ? 43   LEU A O     1 
ATOM   181  C CB    . LEU A 1 43   ? 165.493 200.661 157.847 1.00 57.76  ? 43   LEU A CB    1 
ATOM   182  C CG    . LEU A 1 43   ? 166.017 201.882 158.607 1.00 55.32  ? 43   LEU A CG    1 
ATOM   183  C CD1   . LEU A 1 43   ? 165.223 202.096 159.881 1.00 61.75  ? 43   LEU A CD1   1 
ATOM   184  C CD2   . LEU A 1 43   ? 167.497 201.732 158.915 1.00 47.91  ? 43   LEU A CD2   1 
ATOM   185  N N     . TRP A 1 44   ? 165.963 198.722 154.709 1.00 42.11  ? 44   TRP A N     1 
ATOM   186  C CA    . TRP A 1 44   ? 165.465 197.498 154.089 1.00 35.25  ? 44   TRP A CA    1 
ATOM   187  C C     . TRP A 1 44   ? 166.055 196.257 154.748 1.00 36.55  ? 44   TRP A C     1 
ATOM   188  O O     . TRP A 1 44   ? 165.354 195.257 154.938 1.00 36.86  ? 44   TRP A O     1 
ATOM   189  C CB    . TRP A 1 44   ? 165.769 197.508 152.589 1.00 34.77  ? 44   TRP A CB    1 
ATOM   190  C CG    . TRP A 1 44   ? 167.233 197.546 152.265 1.00 34.78  ? 44   TRP A CG    1 
ATOM   191  C CD1   . TRP A 1 44   ? 168.001 198.656 152.071 1.00 35.05  ? 44   TRP A CD1   1 
ATOM   192  C CD2   . TRP A 1 44   ? 168.105 196.422 152.097 1.00 30.75  ? 44   TRP A CD2   1 
ATOM   193  N NE1   . TRP A 1 44   ? 169.296 198.293 151.794 1.00 35.42  ? 44   TRP A NE1   1 
ATOM   194  C CE2   . TRP A 1 44   ? 169.385 196.926 151.805 1.00 33.15  ? 44   TRP A CE2   1 
ATOM   195  C CE3   . TRP A 1 44   ? 167.926 195.037 152.167 1.00 27.96  ? 44   TRP A CE3   1 
ATOM   196  C CZ2   . TRP A 1 44   ? 170.480 196.096 151.582 1.00 32.76  ? 44   TRP A CZ2   1 
ATOM   197  C CZ3   . TRP A 1 44   ? 169.014 194.216 151.948 1.00 26.41  ? 44   TRP A CZ3   1 
ATOM   198  C CH2   . TRP A 1 44   ? 170.273 194.747 151.657 1.00 28.38  ? 44   TRP A CH2   1 
ATOM   199  N N     . ALA A 1 45   ? 167.343 196.300 155.097 1.00 35.52  ? 45   ALA A N     1 
ATOM   200  C CA    . ALA A 1 45   ? 167.987 195.141 155.706 1.00 26.86  ? 45   ALA A CA    1 
ATOM   201  C C     . ALA A 1 45   ? 167.381 194.825 157.066 1.00 32.23  ? 45   ALA A C     1 
ATOM   202  O O     . ALA A 1 45   ? 167.077 193.664 157.368 1.00 36.10  ? 45   ALA A O     1 
ATOM   203  C CB    . ALA A 1 45   ? 169.491 195.382 155.828 1.00 25.78  ? 45   ALA A CB    1 
ATOM   204  N N     . LEU A 1 46   ? 167.192 195.851 157.899 1.00 38.80  ? 46   LEU A N     1 
ATOM   205  C CA    . LEU A 1 46   ? 166.609 195.638 159.218 1.00 31.21  ? 46   LEU A CA    1 
ATOM   206  C C     . LEU A 1 46   ? 165.179 195.126 159.116 1.00 32.91  ? 46   LEU A C     1 
ATOM   207  O O     . LEU A 1 46   ? 164.790 194.207 159.844 1.00 38.95  ? 46   LEU A O     1 
ATOM   208  C CB    . LEU A 1 46   ? 166.661 196.933 160.026 1.00 34.93  ? 46   LEU A CB    1 
ATOM   209  C CG    . LEU A 1 46   ? 165.962 196.921 161.386 1.00 40.00  ? 46   LEU A CG    1 
ATOM   210  C CD1   . LEU A 1 46   ? 166.495 195.796 162.250 1.00 33.20  ? 46   LEU A CD1   1 
ATOM   211  C CD2   . LEU A 1 46   ? 166.134 198.259 162.082 1.00 46.27  ? 46   LEU A CD2   1 
ATOM   212  N N     . ALA A 1 47   ? 164.381 195.708 158.219 1.00 33.97  ? 47   ALA A N     1 
ATOM   213  C CA    . ALA A 1 47   ? 163.001 195.260 158.058 1.00 35.39  ? 47   ALA A CA    1 
ATOM   214  C C     . ALA A 1 47   ? 162.940 193.819 157.567 1.00 39.43  ? 47   ALA A C     1 
ATOM   215  O O     . ALA A 1 47   ? 162.128 193.021 158.053 1.00 40.69  ? 47   ALA A O     1 
ATOM   216  C CB    . ALA A 1 47   ? 162.261 196.188 157.097 1.00 44.23  ? 47   ALA A CB    1 
ATOM   217  N N     . SER A 1 48   ? 163.794 193.467 156.603 1.00 38.83  ? 48   SER A N     1 
ATOM   218  C CA    . SER A 1 48   ? 163.815 192.100 156.096 1.00 33.57  ? 48   SER A CA    1 
ATOM   219  C C     . SER A 1 48   ? 164.248 191.115 157.174 1.00 33.02  ? 48   SER A C     1 
ATOM   220  O O     . SER A 1 48   ? 163.681 190.021 157.284 1.00 39.05  ? 48   SER A O     1 
ATOM   221  C CB    . SER A 1 48   ? 164.733 192.011 154.878 1.00 33.45  ? 48   SER A CB    1 
ATOM   222  O OG    . SER A 1 48   ? 165.983 192.621 155.141 1.00 38.91  ? 48   SER A OG    1 
ATOM   223  N N     . TRP A 1 49   ? 165.240 191.483 157.988 1.00 29.24  ? 49   TRP A N     1 
ATOM   224  C CA    . TRP A 1 49   ? 165.663 190.582 159.054 1.00 25.96  ? 49   TRP A CA    1 
ATOM   225  C C     . TRP A 1 49   ? 164.595 190.456 160.132 1.00 29.16  ? 49   TRP A C     1 
ATOM   226  O O     . TRP A 1 49   ? 164.436 189.388 160.729 1.00 32.97  ? 49   TRP A O     1 
ATOM   227  C CB    . TRP A 1 49   ? 166.979 191.046 159.666 1.00 22.47  ? 49   TRP A CB    1 
ATOM   228  C CG    . TRP A 1 49   ? 167.479 190.093 160.701 1.00 23.44  ? 49   TRP A CG    1 
ATOM   229  C CD1   . TRP A 1 49   ? 167.602 188.741 160.574 1.00 25.48  ? 49   TRP A CD1   1 
ATOM   230  C CD2   . TRP A 1 49   ? 167.921 190.412 162.024 1.00 24.09  ? 49   TRP A CD2   1 
ATOM   231  N NE1   . TRP A 1 49   ? 168.091 188.198 161.734 1.00 23.89  ? 49   TRP A NE1   1 
ATOM   232  C CE2   . TRP A 1 49   ? 168.296 189.203 162.641 1.00 24.19  ? 49   TRP A CE2   1 
ATOM   233  C CE3   . TRP A 1 49   ? 168.034 191.601 162.749 1.00 26.42  ? 49   TRP A CE3   1 
ATOM   234  C CZ2   . TRP A 1 49   ? 168.779 189.150 163.943 1.00 25.82  ? 49   TRP A CZ2   1 
ATOM   235  C CZ3   . TRP A 1 49   ? 168.513 191.544 164.039 1.00 26.02  ? 49   TRP A CZ3   1 
ATOM   236  C CH2   . TRP A 1 49   ? 168.879 190.328 164.625 1.00 28.98  ? 49   TRP A CH2   1 
ATOM   237  N N     . LEU A 1 50   ? 163.862 191.536 160.408 1.00 31.73  ? 50   LEU A N     1 
ATOM   238  C CA    . LEU A 1 50   ? 162.755 191.441 161.353 1.00 30.61  ? 50   LEU A CA    1 
ATOM   239  C C     . LEU A 1 50   ? 161.661 190.525 160.823 1.00 32.73  ? 50   LEU A C     1 
ATOM   240  O O     . LEU A 1 50   ? 161.067 189.756 161.586 1.00 35.59  ? 50   LEU A O     1 
ATOM   241  C CB    . LEU A 1 50   ? 162.196 192.828 161.658 1.00 35.24  ? 50   LEU A CB    1 
ATOM   242  C CG    . LEU A 1 50   ? 163.085 193.728 162.516 1.00 34.91  ? 50   LEU A CG    1 
ATOM   243  C CD1   . LEU A 1 50   ? 162.397 195.050 162.779 1.00 40.01  ? 50   LEU A CD1   1 
ATOM   244  C CD2   . LEU A 1 50   ? 163.452 193.041 163.820 1.00 34.61  ? 50   LEU A CD2   1 
ATOM   245  N N     . GLU A 1 51   ? 161.381 190.592 159.520 1.00 34.67  ? 51   GLU A N     1 
ATOM   246  C CA    . GLU A 1 51   ? 160.429 189.657 158.927 1.00 35.41  ? 51   GLU A CA    1 
ATOM   247  C C     . GLU A 1 51   ? 160.930 188.221 159.032 1.00 31.26  ? 51   GLU A C     1 
ATOM   248  O O     . GLU A 1 51   ? 160.148 187.299 159.298 1.00 32.87  ? 51   GLU A O     1 
ATOM   249  C CB    . GLU A 1 51   ? 160.161 190.029 157.470 1.00 36.92  ? 51   GLU A CB    1 
ATOM   250  C CG    . GLU A 1 51   ? 159.458 191.361 157.292 1.00 38.71  ? 51   GLU A CG    1 
ATOM   251  C CD    . GLU A 1 51   ? 159.241 191.716 155.835 1.00 54.27  ? 51   GLU A CD    1 
ATOM   252  O OE1   . GLU A 1 51   ? 159.716 190.963 154.960 1.00 54.16  ? 51   GLU A OE1   1 
ATOM   253  O OE2   . GLU A 1 51   ? 158.593 192.749 155.565 1.00 60.05  ? 51   GLU A OE2   1 
ATOM   254  N N     . GLN A 1 52   ? 162.232 188.013 158.821 1.00 28.86  ? 52   GLN A N     1 
ATOM   255  C CA    . GLN A 1 52   ? 162.810 186.680 158.976 1.00 31.17  ? 52   GLN A CA    1 
ATOM   256  C C     . GLN A 1 52   ? 162.646 186.172 160.404 1.00 33.56  ? 52   GLN A C     1 
ATOM   257  O O     . GLN A 1 52   ? 162.248 185.023 160.626 1.00 40.38  ? 52   GLN A O     1 
ATOM   258  C CB    . GLN A 1 52   ? 164.289 186.698 158.589 1.00 32.28  ? 52   GLN A CB    1 
ATOM   259  C CG    . GLN A 1 52   ? 164.563 186.909 157.114 1.00 34.20  ? 52   GLN A CG    1 
ATOM   260  C CD    . GLN A 1 52   ? 166.045 187.026 156.817 1.00 27.19  ? 52   GLN A CD    1 
ATOM   261  O OE1   . GLN A 1 52   ? 166.838 187.367 157.691 1.00 27.58  ? 52   GLN A OE1   1 
ATOM   262  N NE2   . GLN A 1 52   ? 166.425 186.735 155.581 1.00 28.75  ? 52   GLN A NE2   1 
ATOM   263  N N     . LEU A 1 53   ? 162.952 187.021 161.386 1.00 30.55  ? 53   LEU A N     1 
ATOM   264  C CA    . LEU A 1 53   ? 162.817 186.630 162.786 1.00 31.75  ? 53   LEU A CA    1 
ATOM   265  C C     . LEU A 1 53   ? 161.367 186.330 163.138 1.00 37.25  ? 53   LEU A C     1 
ATOM   266  O O     . LEU A 1 53   ? 161.082 185.371 163.864 1.00 41.86  ? 53   LEU A O     1 
ATOM   267  C CB    . LEU A 1 53   ? 163.367 187.727 163.694 1.00 31.92  ? 53   LEU A CB    1 
ATOM   268  C CG    . LEU A 1 53   ? 164.862 188.023 163.621 1.00 23.78  ? 53   LEU A CG    1 
ATOM   269  C CD1   . LEU A 1 53   ? 165.213 189.148 164.573 1.00 23.11  ? 53   LEU A CD1   1 
ATOM   270  C CD2   . LEU A 1 53   ? 165.667 186.778 163.937 1.00 28.34  ? 53   LEU A CD2   1 
ATOM   271  N N     . ALA A 1 54   ? 160.436 187.147 162.640 1.00 34.21  ? 54   ALA A N     1 
ATOM   272  C CA    . ALA A 1 54   ? 159.021 186.888 162.872 1.00 34.82  ? 54   ALA A CA    1 
ATOM   273  C C     . ALA A 1 54   ? 158.609 185.547 162.284 1.00 42.19  ? 54   ALA A C     1 
ATOM   274  O O     . ALA A 1 54   ? 157.858 184.789 162.908 1.00 47.26  ? 54   ALA A O     1 
ATOM   275  C CB    . ALA A 1 54   ? 158.178 188.017 162.282 1.00 29.87  ? 54   ALA A CB    1 
ATOM   276  N N     . GLU A 1 55   ? 159.093 185.235 161.081 1.00 39.51  ? 55   GLU A N     1 
ATOM   277  C CA    . GLU A 1 55   ? 158.811 183.941 160.475 1.00 39.43  ? 55   GLU A CA    1 
ATOM   278  C C     . GLU A 1 55   ? 159.457 182.790 161.238 1.00 44.01  ? 55   GLU A C     1 
ATOM   279  O O     . GLU A 1 55   ? 158.918 181.679 161.231 1.00 54.72  ? 55   GLU A O     1 
ATOM   280  C CB    . GLU A 1 55   ? 159.273 183.950 159.016 1.00 40.98  ? 55   GLU A CB    1 
ATOM   281  C CG    . GLU A 1 55   ? 159.067 182.646 158.268 1.00 46.77  ? 55   GLU A CG    1 
ATOM   282  C CD    . GLU A 1 55   ? 160.363 181.892 158.063 1.00 53.68  ? 55   GLU A CD    1 
ATOM   283  O OE1   . GLU A 1 55   ? 161.438 182.526 158.125 1.00 51.69  ? 55   GLU A OE1   1 
ATOM   284  O OE2   . GLU A 1 55   ? 160.309 180.665 157.840 1.00 59.76  ? 55   GLU A OE2   1 
ATOM   285  N N     . GLU A 1 56   ? 160.581 183.034 161.915 1.00 44.81  ? 56   GLU A N     1 
ATOM   286  C CA    . GLU A 1 56   ? 161.305 181.999 162.641 1.00 46.38  ? 56   GLU A CA    1 
ATOM   287  C C     . GLU A 1 56   ? 160.961 181.967 164.127 1.00 50.04  ? 56   GLU A C     1 
ATOM   288  O O     . GLU A 1 56   ? 161.762 181.476 164.929 1.00 52.98  ? 56   GLU A O     1 
ATOM   289  C CB    . GLU A 1 56   ? 162.813 182.182 162.458 1.00 40.16  ? 56   GLU A CB    1 
ATOM   290  C CG    . GLU A 1 56   ? 163.289 182.063 161.023 1.00 41.07  ? 56   GLU A CG    1 
ATOM   291  C CD    . GLU A 1 56   ? 164.779 182.300 160.887 1.00 43.83  ? 56   GLU A CD    1 
ATOM   292  O OE1   . GLU A 1 56   ? 165.523 181.973 161.834 1.00 42.94  ? 56   GLU A OE1   1 
ATOM   293  O OE2   . GLU A 1 56   ? 165.206 182.822 159.838 1.00 48.86  ? 56   GLU A OE2   1 
ATOM   294  N N     . ASP A 1 57   ? 159.796 182.494 164.508 1.00 47.93  ? 57   ASP A N     1 
ATOM   295  C CA    . ASP A 1 57   ? 159.289 182.458 165.880 1.00 50.28  ? 57   ASP A CA    1 
ATOM   296  C C     . ASP A 1 57   ? 160.161 183.243 166.856 1.00 47.88  ? 57   ASP A C     1 
ATOM   297  O O     . ASP A 1 57   ? 160.077 183.035 168.070 1.00 50.17  ? 57   ASP A O     1 
ATOM   298  C CB    . ASP A 1 57   ? 159.121 181.018 166.379 1.00 64.01  ? 57   ASP A CB    1 
ATOM   299  C CG    . ASP A 1 57   ? 158.178 180.207 165.517 1.00 77.13  ? 57   ASP A CG    1 
ATOM   300  O OD1   . ASP A 1 57   ? 158.579 179.810 164.403 1.00 75.75  ? 57   ASP A OD1   1 
ATOM   301  O OD2   . ASP A 1 57   ? 157.033 179.967 165.953 1.00 85.60  ? 57   ASP A OD2   1 
ATOM   302  N N     . TYR A 1 58   ? 161.002 184.147 166.358 1.00 45.16  ? 58   TYR A N     1 
ATOM   303  C CA    . TYR A 1 58   ? 161.826 184.971 167.234 1.00 38.18  ? 58   TYR A CA    1 
ATOM   304  C C     . TYR A 1 58   ? 161.120 186.237 167.692 1.00 44.57  ? 58   TYR A C     1 
ATOM   305  O O     . TYR A 1 58   ? 161.476 186.788 168.740 1.00 53.31  ? 58   TYR A O     1 
ATOM   306  C CB    . TYR A 1 58   ? 163.133 185.351 166.537 1.00 38.61  ? 58   TYR A CB    1 
ATOM   307  C CG    . TYR A 1 58   ? 164.208 184.298 166.629 1.00 40.08  ? 58   TYR A CG    1 
ATOM   308  C CD1   . TYR A 1 58   ? 164.863 184.053 167.827 1.00 38.73  ? 58   TYR A CD1   1 
ATOM   309  C CD2   . TYR A 1 58   ? 164.579 183.557 165.516 1.00 38.01  ? 58   TYR A CD2   1 
ATOM   310  C CE1   . TYR A 1 58   ? 165.850 183.095 167.918 1.00 38.76  ? 58   TYR A CE1   1 
ATOM   311  C CE2   . TYR A 1 58   ? 165.566 182.597 165.597 1.00 36.66  ? 58   TYR A CE2   1 
ATOM   312  C CZ    . TYR A 1 58   ? 166.198 182.371 166.800 1.00 39.90  ? 58   TYR A CZ    1 
ATOM   313  O OH    . TYR A 1 58   ? 167.183 181.415 166.889 1.00 43.57  ? 58   TYR A OH    1 
ATOM   314  N N     . LEU A 1 59   ? 160.137 186.713 166.936 1.00 44.01  ? 59   LEU A N     1 
ATOM   315  C CA    . LEU A 1 59   ? 159.425 187.941 167.251 1.00 42.94  ? 59   LEU A CA    1 
ATOM   316  C C     . LEU A 1 59   ? 157.960 187.642 167.539 1.00 49.91  ? 59   LEU A C     1 
ATOM   317  O O     . LEU A 1 59   ? 157.364 186.751 166.926 1.00 49.12  ? 59   LEU A O     1 
ATOM   318  C CB    . LEU A 1 59   ? 159.534 188.950 166.107 1.00 42.73  ? 59   LEU A CB    1 
ATOM   319  C CG    . LEU A 1 59   ? 160.923 189.518 165.822 1.00 34.66  ? 59   LEU A CG    1 
ATOM   320  C CD1   . LEU A 1 59   ? 160.851 190.543 164.710 1.00 35.10  ? 59   LEU A CD1   1 
ATOM   321  C CD2   . LEU A 1 59   ? 161.520 190.130 167.071 1.00 35.25  ? 59   LEU A CD2   1 
ATOM   322  N N     . ILE A 1 60   ? 157.389 188.394 168.475 1.00 54.93  ? 60   ILE A N     1 
ATOM   323  C CA    . ILE A 1 60   ? 155.983 188.286 168.840 1.00 56.10  ? 60   ILE A CA    1 
ATOM   324  C C     . ILE A 1 60   ? 155.253 189.492 168.268 1.00 60.04  ? 60   ILE A C     1 
ATOM   325  O O     . ILE A 1 60   ? 155.708 190.632 168.422 1.00 61.12  ? 60   ILE A O     1 
ATOM   326  C CB    . ILE A 1 60   ? 155.803 188.203 170.367 1.00 55.67  ? 60   ILE A CB    1 
ATOM   327  C CG1   . ILE A 1 60   ? 156.422 186.917 170.922 1.00 57.70  ? 60   ILE A CG1   1 
ATOM   328  C CG2   . ILE A 1 60   ? 154.332 188.276 170.739 1.00 61.05  ? 60   ILE A CG2   1 
ATOM   329  C CD1   . ILE A 1 60   ? 157.868 187.057 171.358 1.00 55.35  ? 60   ILE A CD1   1 
ATOM   330  N N     . SER A 1 61   ? 154.128 189.245 167.602 1.00 65.74  ? 61   SER A N     1 
ATOM   331  C CA    . SER A 1 61   ? 153.365 190.313 166.963 1.00 69.81  ? 61   SER A CA    1 
ATOM   332  C C     . SER A 1 61   ? 152.462 190.972 167.998 1.00 71.12  ? 61   SER A C     1 
ATOM   333  O O     . SER A 1 61   ? 151.480 190.375 168.451 1.00 68.47  ? 61   SER A O     1 
ATOM   334  C CB    . SER A 1 61   ? 152.551 189.763 165.796 1.00 70.56  ? 61   SER A CB    1 
ATOM   335  O OG    . SER A 1 61   ? 151.630 188.781 166.235 1.00 79.55  ? 61   SER A OG    1 
ATOM   336  N N     . LEU A 1 62   ? 152.794 192.203 168.371 1.00 72.17  ? 62   LEU A N     1 
ATOM   337  C CA    . LEU A 1 62   ? 151.999 193.006 169.282 1.00 74.40  ? 62   LEU A CA    1 
ATOM   338  C C     . LEU A 1 62   ? 151.182 194.016 168.479 1.00 76.63  ? 62   LEU A C     1 
ATOM   339  O O     . LEU A 1 62   ? 151.092 193.942 167.250 1.00 75.93  ? 62   LEU A O     1 
ATOM   340  C CB    . LEU A 1 62   ? 152.898 193.693 170.312 1.00 70.86  ? 62   LEU A CB    1 
ATOM   341  C CG    . LEU A 1 62   ? 153.768 192.810 171.206 1.00 64.40  ? 62   LEU A CG    1 
ATOM   342  C CD1   . LEU A 1 62   ? 154.512 193.664 172.219 1.00 62.06  ? 62   LEU A CD1   1 
ATOM   343  C CD2   . LEU A 1 62   ? 152.932 191.752 171.904 1.00 61.68  ? 62   LEU A CD2   1 
ATOM   344  N N     . THR A 1 63   ? 150.566 194.965 169.176 1.00 76.87  ? 63   THR A N     1 
ATOM   345  C CA    . THR A 1 63   ? 149.792 196.016 168.521 1.00 84.90  ? 63   THR A CA    1 
ATOM   346  C C     . THR A 1 63   ? 150.751 196.952 167.795 1.00 80.99  ? 63   THR A C     1 
ATOM   347  O O     . THR A 1 63   ? 151.347 197.845 168.400 1.00 79.52  ? 63   THR A O     1 
ATOM   348  C CB    . THR A 1 63   ? 148.950 196.774 169.540 1.00 89.53  ? 63   THR A CB    1 
ATOM   349  O OG1   . THR A 1 63   ? 148.099 195.854 170.237 1.00 88.11  ? 63   THR A OG1   1 
ATOM   350  C CG2   . THR A 1 63   ? 148.091 197.822 168.848 1.00 84.52  ? 63   THR A CG2   1 
ATOM   351  N N     . ASP A 1 64   ? 150.902 196.739 166.486 1.00 74.25  ? 64   ASP A N     1 
ATOM   352  C CA    . ASP A 1 64   ? 151.738 197.573 165.621 1.00 75.07  ? 64   ASP A CA    1 
ATOM   353  C C     . ASP A 1 64   ? 153.193 197.621 166.085 1.00 74.26  ? 64   ASP A C     1 
ATOM   354  O O     . ASP A 1 64   ? 153.862 198.647 165.943 1.00 75.39  ? 64   ASP A O     1 
ATOM   355  C CB    . ASP A 1 64   ? 151.172 198.993 165.503 1.00 82.01  ? 64   ASP A CB    1 
ATOM   356  C CG    . ASP A 1 64   ? 149.872 199.040 164.721 1.00 83.85  ? 64   ASP A CG    1 
ATOM   357  O OD1   . ASP A 1 64   ? 149.696 198.206 163.808 1.00 83.66  ? 64   ASP A OD1   1 
ATOM   358  O OD2   . ASP A 1 64   ? 149.028 199.913 165.016 1.00 79.11  ? 64   ASP A OD2   1 
ATOM   359  N N     . ARG A 1 65   ? 153.700 196.517 166.634 1.00 73.84  ? 65   ARG A N     1 
ATOM   360  C CA    . ARG A 1 65   ? 155.107 196.438 167.005 1.00 67.54  ? 65   ARG A CA    1 
ATOM   361  C C     . ARG A 1 65   ? 155.491 194.978 167.205 1.00 60.90  ? 65   ARG A C     1 
ATOM   362  O O     . ARG A 1 65   ? 154.686 194.180 167.691 1.00 58.77  ? 65   ARG A O     1 
ATOM   363  C CB    . ARG A 1 65   ? 155.407 197.252 168.273 1.00 65.62  ? 65   ARG A CB    1 
ATOM   364  C CG    . ARG A 1 65   ? 154.790 196.705 169.550 1.00 72.71  ? 65   ARG A CG    1 
ATOM   365  C CD    . ARG A 1 65   ? 154.715 197.773 170.631 1.00 77.88  ? 65   ARG A CD    1 
ATOM   366  N NE    . ARG A 1 65   ? 154.321 197.220 171.921 1.00 83.54  ? 65   ARG A NE    1 
ATOM   367  C CZ    . ARG A 1 65   ? 155.129 197.109 172.967 1.00 79.94  ? 65   ARG A CZ    1 
ATOM   368  N NH1   . ARG A 1 65   ? 156.381 197.537 172.921 1.00 76.14  ? 65   ARG A NH1   1 
ATOM   369  N NH2   . ARG A 1 65   ? 154.670 196.561 174.088 1.00 73.89  ? 65   ARG A NH2   1 
ATOM   370  N N     . TRP A 1 66   ? 156.712 194.637 166.805 1.00 60.36  ? 66   TRP A N     1 
ATOM   371  C CA    . TRP A 1 66   ? 157.269 193.325 167.094 1.00 53.42  ? 66   TRP A CA    1 
ATOM   372  C C     . TRP A 1 66   ? 157.891 193.314 168.483 1.00 54.31  ? 66   TRP A C     1 
ATOM   373  O O     . TRP A 1 66   ? 158.386 194.332 168.970 1.00 58.67  ? 66   TRP A O     1 
ATOM   374  C CB    . TRP A 1 66   ? 158.329 192.937 166.064 1.00 52.51  ? 66   TRP A CB    1 
ATOM   375  C CG    . TRP A 1 66   ? 157.788 192.444 164.764 1.00 51.78  ? 66   TRP A CG    1 
ATOM   376  C CD1   . TRP A 1 66   ? 156.968 191.373 164.570 1.00 51.68  ? 66   TRP A CD1   1 
ATOM   377  C CD2   . TRP A 1 66   ? 158.057 192.984 163.466 1.00 52.31  ? 66   TRP A CD2   1 
ATOM   378  N NE1   . TRP A 1 66   ? 156.695 191.221 163.233 1.00 49.88  ? 66   TRP A NE1   1 
ATOM   379  C CE2   . TRP A 1 66   ? 157.354 192.198 162.533 1.00 54.09  ? 66   TRP A CE2   1 
ATOM   380  C CE3   . TRP A 1 66   ? 158.820 194.061 163.003 1.00 51.87  ? 66   TRP A CE3   1 
ATOM   381  C CZ2   . TRP A 1 66   ? 157.390 192.453 161.165 1.00 50.40  ? 66   TRP A CZ2   1 
ATOM   382  C CZ3   . TRP A 1 66   ? 158.854 194.313 161.645 1.00 57.30  ? 66   TRP A CZ3   1 
ATOM   383  C CH2   . TRP A 1 66   ? 158.143 193.513 160.742 1.00 57.71  ? 66   TRP A CH2   1 
ATOM   384  N N     . LEU A 1 67   ? 157.864 192.148 169.121 1.00 51.00  ? 67   LEU A N     1 
ATOM   385  C CA    . LEU A 1 67   ? 158.454 191.969 170.441 1.00 50.49  ? 67   LEU A CA    1 
ATOM   386  C C     . LEU A 1 67   ? 159.537 190.904 170.366 1.00 51.46  ? 67   LEU A C     1 
ATOM   387  O O     . LEU A 1 67   ? 159.265 189.764 169.975 1.00 55.32  ? 67   LEU A O     1 
ATOM   388  C CB    . LEU A 1 67   ? 157.397 191.579 171.474 1.00 50.04  ? 67   LEU A CB    1 
ATOM   389  C CG    . LEU A 1 67   ? 157.933 191.378 172.893 1.00 47.71  ? 67   LEU A CG    1 
ATOM   390  C CD1   . LEU A 1 67   ? 158.514 192.674 173.430 1.00 47.76  ? 67   LEU A CD1   1 
ATOM   391  C CD2   . LEU A 1 67   ? 156.850 190.851 173.816 1.00 50.10  ? 67   LEU A CD2   1 
ATOM   392  N N     . LEU A 1 68   ? 160.757 191.276 170.739 1.00 42.00  ? 68   LEU A N     1 
ATOM   393  C CA    . LEU A 1 68   ? 161.857 190.330 170.903 1.00 40.47  ? 68   LEU A CA    1 
ATOM   394  C C     . LEU A 1 68   ? 162.019 190.088 172.398 1.00 48.07  ? 68   LEU A C     1 
ATOM   395  O O     . LEU A 1 68   ? 162.685 190.860 173.092 1.00 48.90  ? 68   LEU A O     1 
ATOM   396  C CB    . LEU A 1 68   ? 163.141 190.865 170.277 1.00 38.86  ? 68   LEU A CB    1 
ATOM   397  C CG    . LEU A 1 68   ? 164.368 189.950 170.307 1.00 33.40  ? 68   LEU A CG    1 
ATOM   398  C CD1   . LEU A 1 68   ? 164.137 188.712 169.460 1.00 34.12  ? 68   LEU A CD1   1 
ATOM   399  C CD2   . LEU A 1 68   ? 165.601 190.698 169.837 1.00 35.22  ? 68   LEU A CD2   1 
ATOM   400  N N     . SER A 1 69   ? 161.409 189.016 172.895 1.00 47.07  ? 69   SER A N     1 
ATOM   401  C CA    . SER A 1 69   ? 161.470 188.723 174.318 1.00 41.16  ? 69   SER A CA    1 
ATOM   402  C C     . SER A 1 69   ? 162.898 188.387 174.734 1.00 40.23  ? 69   SER A C     1 
ATOM   403  O O     . SER A 1 69   ? 163.763 188.084 173.908 1.00 43.50  ? 69   SER A O     1 
ATOM   404  C CB    . SER A 1 69   ? 160.532 187.571 174.672 1.00 40.96  ? 69   SER A CB    1 
ATOM   405  O OG    . SER A 1 69   ? 160.883 186.396 173.966 1.00 42.32  ? 69   SER A OG    1 
ATOM   406  N N     . TRP A 1 70   ? 163.142 188.453 176.045 1.00 40.58  ? 70   TRP A N     1 
ATOM   407  C CA    . TRP A 1 70   ? 164.488 188.214 176.553 1.00 36.14  ? 70   TRP A CA    1 
ATOM   408  C C     . TRP A 1 70   ? 164.938 186.785 176.280 1.00 39.46  ? 70   TRP A C     1 
ATOM   409  O O     . TRP A 1 70   ? 166.094 186.553 175.909 1.00 45.47  ? 70   TRP A O     1 
ATOM   410  C CB    . TRP A 1 70   ? 164.552 188.526 178.047 1.00 36.27  ? 70   TRP A CB    1 
ATOM   411  C CG    . TRP A 1 70   ? 164.091 189.907 178.395 1.00 33.51  ? 70   TRP A CG    1 
ATOM   412  C CD1   . TRP A 1 70   ? 163.070 190.242 179.233 1.00 36.17  ? 70   TRP A CD1   1 
ATOM   413  C CD2   . TRP A 1 70   ? 164.630 191.142 177.908 1.00 34.09  ? 70   TRP A CD2   1 
ATOM   414  N NE1   . TRP A 1 70   ? 162.943 191.606 179.304 1.00 40.09  ? 70   TRP A NE1   1 
ATOM   415  C CE2   . TRP A 1 70   ? 163.889 192.181 178.499 1.00 36.89  ? 70   TRP A CE2   1 
ATOM   416  C CE3   . TRP A 1 70   ? 165.668 191.469 177.031 1.00 40.99  ? 70   TRP A CE3   1 
ATOM   417  C CZ2   . TRP A 1 70   ? 164.150 193.523 178.240 1.00 37.71  ? 70   TRP A CZ2   1 
ATOM   418  C CZ3   . TRP A 1 70   ? 165.926 192.799 176.777 1.00 40.44  ? 70   TRP A CZ3   1 
ATOM   419  C CH2   . TRP A 1 70   ? 165.171 193.810 177.378 1.00 38.11  ? 70   TRP A CH2   1 
ATOM   420  N N     . GLU A 1 71   ? 164.043 185.813 176.461 1.00 35.88  ? 71   GLU A N     1 
ATOM   421  C CA    . GLU A 1 71   ? 164.379 184.432 176.129 1.00 40.79  ? 71   GLU A CA    1 
ATOM   422  C C     . GLU A 1 71   ? 164.685 184.294 174.643 1.00 43.64  ? 71   GLU A C     1 
ATOM   423  O O     . GLU A 1 71   ? 165.673 183.657 174.253 1.00 46.17  ? 71   GLU A O     1 
ATOM   424  C CB    . GLU A 1 71   ? 163.233 183.504 176.532 1.00 48.57  ? 71   GLU A CB    1 
ATOM   425  C CG    . GLU A 1 71   ? 163.487 182.039 176.226 1.00 60.10  ? 71   GLU A CG    1 
ATOM   426  C CD    . GLU A 1 71   ? 162.263 181.177 176.457 1.00 70.50  ? 71   GLU A CD    1 
ATOM   427  O OE1   . GLU A 1 71   ? 161.137 181.711 176.382 1.00 70.35  ? 71   GLU A OE1   1 
ATOM   428  O OE2   . GLU A 1 71   ? 162.426 179.966 176.716 1.00 73.03  ? 71   GLU A OE2   1 
ATOM   429  N N     . ALA A 1 72   ? 163.848 184.901 173.798 1.00 43.20  ? 72   ALA A N     1 
ATOM   430  C CA    . ALA A 1 72   ? 164.115 184.908 172.366 1.00 37.98  ? 72   ALA A CA    1 
ATOM   431  C C     . ALA A 1 72   ? 165.395 185.668 172.051 1.00 34.60  ? 72   ALA A C     1 
ATOM   432  O O     . ALA A 1 72   ? 166.137 185.291 171.141 1.00 37.25  ? 72   ALA A O     1 
ATOM   433  C CB    . ALA A 1 72   ? 162.933 185.511 171.611 1.00 39.91  ? 72   ALA A CB    1 
ATOM   434  N N     . LEU A 1 73   ? 165.671 186.742 172.794 1.00 32.57  ? 73   LEU A N     1 
ATOM   435  C CA    . LEU A 1 73   ? 166.904 187.494 172.582 1.00 34.05  ? 73   LEU A CA    1 
ATOM   436  C C     . LEU A 1 73   ? 168.129 186.628 172.846 1.00 37.70  ? 73   LEU A C     1 
ATOM   437  O O     . LEU A 1 73   ? 169.087 186.631 172.065 1.00 45.55  ? 73   LEU A O     1 
ATOM   438  C CB    . LEU A 1 73   ? 166.923 188.734 173.476 1.00 36.70  ? 73   LEU A CB    1 
ATOM   439  C CG    . LEU A 1 73   ? 168.235 189.521 173.510 1.00 34.72  ? 73   LEU A CG    1 
ATOM   440  C CD1   . LEU A 1 73   ? 168.566 190.078 172.136 1.00 32.26  ? 73   LEU A CD1   1 
ATOM   441  C CD2   . LEU A 1 73   ? 168.173 190.633 174.543 1.00 33.58  ? 73   LEU A CD2   1 
ATOM   442  N N     . TYR A 1 74   ? 168.115 185.872 173.945 1.00 35.89  ? 74   TYR A N     1 
ATOM   443  C CA    . TYR A 1 74   ? 169.260 185.028 174.267 1.00 35.88  ? 74   TYR A CA    1 
ATOM   444  C C     . TYR A 1 74   ? 169.383 183.864 173.291 1.00 39.44  ? 74   TYR A C     1 
ATOM   445  O O     . TYR A 1 74   ? 170.496 183.497 172.890 1.00 47.57  ? 74   TYR A O     1 
ATOM   446  C CB    . TYR A 1 74   ? 169.157 184.530 175.707 1.00 39.22  ? 74   TYR A CB    1 
ATOM   447  C CG    . TYR A 1 74   ? 169.379 185.625 176.723 1.00 35.02  ? 74   TYR A CG    1 
ATOM   448  C CD1   . TYR A 1 74   ? 170.544 186.378 176.710 1.00 34.33  ? 74   TYR A CD1   1 
ATOM   449  C CD2   . TYR A 1 74   ? 168.429 185.906 177.694 1.00 35.62  ? 74   TYR A CD2   1 
ATOM   450  C CE1   . TYR A 1 74   ? 170.754 187.380 177.628 1.00 31.74  ? 74   TYR A CE1   1 
ATOM   451  C CE2   . TYR A 1 74   ? 168.631 186.909 178.619 1.00 40.88  ? 74   TYR A CE2   1 
ATOM   452  C CZ    . TYR A 1 74   ? 169.796 187.641 178.581 1.00 40.06  ? 74   TYR A CZ    1 
ATOM   453  O OH    . TYR A 1 74   ? 170.007 188.641 179.500 1.00 42.62  ? 74   TYR A OH    1 
ATOM   454  N N     . ARG A 1 75   ? 168.253 183.279 172.886 1.00 36.22  ? 75   ARG A N     1 
ATOM   455  C CA    . ARG A 1 75   ? 168.295 182.225 171.878 1.00 36.89  ? 75   ARG A CA    1 
ATOM   456  C C     . ARG A 1 75   ? 168.857 182.748 170.561 1.00 39.21  ? 75   ARG A C     1 
ATOM   457  O O     . ARG A 1 75   ? 169.629 182.057 169.887 1.00 43.57  ? 75   ARG A O     1 
ATOM   458  C CB    . ARG A 1 75   ? 166.899 181.638 171.682 1.00 39.25  ? 75   ARG A CB    1 
ATOM   459  C CG    . ARG A 1 75   ? 166.840 180.488 170.698 1.00 43.47  ? 75   ARG A CG    1 
ATOM   460  C CD    . ARG A 1 75   ? 165.461 179.843 170.665 1.00 43.22  ? 75   ARG A CD    1 
ATOM   461  N NE    . ARG A 1 75   ? 164.421 180.764 170.222 1.00 45.58  ? 75   ARG A NE    1 
ATOM   462  C CZ    . ARG A 1 75   ? 163.567 181.376 171.030 1.00 49.61  ? 75   ARG A CZ    1 
ATOM   463  N NH1   . ARG A 1 75   ? 163.597 181.188 172.339 1.00 51.20  ? 75   ARG A NH1   1 
ATOM   464  N NH2   . ARG A 1 75   ? 162.658 182.196 170.511 1.00 44.03  ? 75   ARG A NH2   1 
ATOM   465  N N     . LEU A 1 76   ? 168.477 183.970 170.178 1.00 39.20  ? 76   LEU A N     1 
ATOM   466  C CA    . LEU A 1 76   ? 169.012 184.592 168.972 1.00 38.66  ? 76   LEU A CA    1 
ATOM   467  C C     . LEU A 1 76   ? 170.509 184.841 169.097 1.00 38.01  ? 76   LEU A C     1 
ATOM   468  O O     . LEU A 1 76   ? 171.266 184.593 168.151 1.00 40.69  ? 76   LEU A O     1 
ATOM   469  C CB    . LEU A 1 76   ? 168.272 185.903 168.704 1.00 31.60  ? 76   LEU A CB    1 
ATOM   470  C CG    . LEU A 1 76   ? 167.924 186.313 167.274 1.00 32.12  ? 76   LEU A CG    1 
ATOM   471  C CD1   . LEU A 1 76   ? 167.200 187.644 167.290 1.00 30.45  ? 76   LEU A CD1   1 
ATOM   472  C CD2   . LEU A 1 76   ? 169.157 186.393 166.405 1.00 36.64  ? 76   LEU A CD2   1 
ATOM   473  N N     . LEU A 1 77   ? 170.952 185.343 170.251 1.00 31.77  ? 77   LEU A N     1 
ATOM   474  C CA    . LEU A 1 77   ? 172.377 185.582 170.454 1.00 36.37  ? 77   LEU A CA    1 
ATOM   475  C C     . LEU A 1 77   ? 173.172 184.285 170.417 1.00 40.31  ? 77   LEU A C     1 
ATOM   476  O O     . LEU A 1 77   ? 174.344 184.288 170.025 1.00 41.47  ? 77   LEU A O     1 
ATOM   477  C CB    . LEU A 1 77   ? 172.609 186.309 171.777 1.00 40.28  ? 77   LEU A CB    1 
ATOM   478  C CG    . LEU A 1 77   ? 172.089 187.742 171.879 1.00 38.67  ? 77   LEU A CG    1 
ATOM   479  C CD1   . LEU A 1 77   ? 172.379 188.311 173.255 1.00 35.62  ? 77   LEU A CD1   1 
ATOM   480  C CD2   . LEU A 1 77   ? 172.698 188.616 170.797 1.00 39.84  ? 77   LEU A CD2   1 
ATOM   481  N N     . GLU A 1 78   ? 172.562 183.172 170.823 1.00 39.93  ? 78   GLU A N     1 
ATOM   482  C CA    . GLU A 1 78   ? 173.225 181.879 170.725 1.00 40.49  ? 78   GLU A CA    1 
ATOM   483  C C     . GLU A 1 78   ? 173.064 181.230 169.356 1.00 41.08  ? 78   GLU A C     1 
ATOM   484  O O     . GLU A 1 78   ? 173.713 180.212 169.092 1.00 44.90  ? 78   GLU A O     1 
ATOM   485  C CB    . GLU A 1 78   ? 172.696 180.933 171.804 1.00 46.26  ? 78   GLU A CB    1 
ATOM   486  C CG    . GLU A 1 78   ? 172.985 181.388 173.221 1.00 53.52  ? 78   GLU A CG    1 
ATOM   487  C CD    . GLU A 1 78   ? 172.326 180.503 174.258 1.00 64.85  ? 78   GLU A CD    1 
ATOM   488  O OE1   . GLU A 1 78   ? 171.606 179.563 173.863 1.00 64.41  ? 78   GLU A OE1   1 
ATOM   489  O OE2   . GLU A 1 78   ? 172.524 180.748 175.467 1.00 66.98  ? 78   GLU A OE2   1 
ATOM   490  N N     . ASP A 1 79   ? 172.226 181.787 168.486 1.00 46.17  ? 79   ASP A N     1 
ATOM   491  C CA    . ASP A 1 79   ? 172.009 181.220 167.162 1.00 42.65  ? 79   ASP A CA    1 
ATOM   492  C C     . ASP A 1 79   ? 173.101 181.689 166.208 1.00 38.59  ? 79   ASP A C     1 
ATOM   493  O O     . ASP A 1 79   ? 173.376 182.888 166.106 1.00 36.26  ? 79   ASP A O     1 
ATOM   494  C CB    . ASP A 1 79   ? 170.633 181.619 166.633 1.00 39.53  ? 79   ASP A CB    1 
ATOM   495  C CG    . ASP A 1 79   ? 170.187 180.766 165.466 1.00 44.36  ? 79   ASP A CG    1 
ATOM   496  O OD1   . ASP A 1 79   ? 170.955 179.873 165.051 1.00 46.72  ? 79   ASP A OD1   1 
ATOM   497  O OD2   . ASP A 1 79   ? 169.064 180.983 164.966 1.00 48.97  ? 79   ASP A OD2   1 
ATOM   498  N N     . GLU A 1 80   ? 173.719 180.739 165.508 1.00 41.96  ? 80   GLU A N     1 
ATOM   499  C CA    . GLU A 1 80   ? 174.805 181.048 164.588 1.00 42.22  ? 80   GLU A CA    1 
ATOM   500  C C     . GLU A 1 80   ? 174.317 181.392 163.187 1.00 44.67  ? 80   GLU A C     1 
ATOM   501  O O     . GLU A 1 80   ? 175.031 182.082 162.451 1.00 43.35  ? 80   GLU A O     1 
ATOM   502  C CB    . GLU A 1 80   ? 175.783 179.870 164.519 1.00 41.64  ? 80   GLU A CB    1 
ATOM   503  C CG    . GLU A 1 80   ? 177.222 180.262 164.208 1.00 54.67  ? 80   GLU A CG    1 
ATOM   504  C CD    . GLU A 1 80   ? 177.501 180.363 162.721 1.00 68.27  ? 80   GLU A CD    1 
ATOM   505  O OE1   . GLU A 1 80   ? 176.858 179.629 161.942 1.00 73.38  ? 80   GLU A OE1   1 
ATOM   506  O OE2   . GLU A 1 80   ? 178.364 181.177 162.332 1.00 68.51  ? 80   GLU A OE2   1 
ATOM   507  N N     . GLU A 1 81   ? 173.123 180.936 162.803 1.00 43.38  ? 81   GLU A N     1 
ATOM   508  C CA    . GLU A 1 81   ? 172.580 181.285 161.496 1.00 36.63  ? 81   GLU A CA    1 
ATOM   509  C C     . GLU A 1 81   ? 172.245 182.765 161.390 1.00 37.87  ? 81   GLU A C     1 
ATOM   510  O O     . GLU A 1 81   ? 172.177 183.296 160.276 1.00 44.88  ? 81   GLU A O     1 
ATOM   511  C CB    . GLU A 1 81   ? 171.337 180.447 161.199 1.00 40.20  ? 81   GLU A CB    1 
ATOM   512  C CG    . GLU A 1 81   ? 171.534 178.956 161.404 1.00 52.95  ? 81   GLU A CG    1 
ATOM   513  C CD    . GLU A 1 81   ? 170.411 178.127 160.811 1.00 62.58  ? 81   GLU A CD    1 
ATOM   514  O OE1   . GLU A 1 81   ? 170.081 178.331 159.624 1.00 58.84  ? 81   GLU A OE1   1 
ATOM   515  O OE2   . GLU A 1 81   ? 169.856 177.273 161.532 1.00 66.28  ? 81   GLU A OE2   1 
ATOM   516  N N     . HIS A 1 82   ? 172.033 183.441 162.518 1.00 37.49  ? 82   HIS A N     1 
ATOM   517  C CA    . HIS A 1 82   ? 171.733 184.866 162.542 1.00 30.36  ? 82   HIS A CA    1 
ATOM   518  C C     . HIS A 1 82   ? 172.874 185.695 163.113 1.00 31.39  ? 82   HIS A C     1 
ATOM   519  O O     . HIS A 1 82   ? 172.672 186.871 163.427 1.00 35.83  ? 82   HIS A O     1 
ATOM   520  C CB    . HIS A 1 82   ? 170.456 185.124 163.344 1.00 28.08  ? 82   HIS A CB    1 
ATOM   521  C CG    . HIS A 1 82   ? 169.227 184.519 162.742 1.00 32.17  ? 82   HIS A CG    1 
ATOM   522  N ND1   . HIS A 1 82   ? 168.432 185.194 161.842 1.00 33.53  ? 82   HIS A ND1   1 
ATOM   523  C CD2   . HIS A 1 82   ? 168.653 183.307 162.917 1.00 34.57  ? 82   HIS A CD2   1 
ATOM   524  C CE1   . HIS A 1 82   ? 167.422 184.421 161.484 1.00 34.27  ? 82   HIS A CE1   1 
ATOM   525  N NE2   . HIS A 1 82   ? 167.533 183.271 162.123 1.00 37.96  ? 82   HIS A NE2   1 
ATOM   526  N N     . ALA A 1 83   ? 174.064 185.110 163.262 1.00 29.72  ? 83   ALA A N     1 
ATOM   527  C CA    . ALA A 1 83   ? 175.184 185.837 163.851 1.00 26.82  ? 83   ALA A CA    1 
ATOM   528  C C     . ALA A 1 83   ? 175.601 187.016 162.983 1.00 29.93  ? 83   ALA A C     1 
ATOM   529  O O     . ALA A 1 83   ? 175.961 188.080 163.500 1.00 30.79  ? 83   ALA A O     1 
ATOM   530  C CB    . ALA A 1 83   ? 176.364 184.893 164.074 1.00 34.31  ? 83   ALA A CB    1 
ATOM   531  N N     . SER A 1 84   ? 175.571 186.844 161.661 1.00 35.88  ? 84   SER A N     1 
ATOM   532  C CA    . SER A 1 84   ? 175.913 187.941 160.762 1.00 31.92  ? 84   SER A CA    1 
ATOM   533  C C     . SER A 1 84   ? 174.842 189.024 160.764 1.00 36.69  ? 84   SER A C     1 
ATOM   534  O O     . SER A 1 84   ? 175.145 190.193 160.504 1.00 34.27  ? 84   SER A O     1 
ATOM   535  C CB    . SER A 1 84   ? 176.126 187.408 159.347 1.00 30.27  ? 84   SER A CB    1 
ATOM   536  O OG    . SER A 1 84   ? 174.972 186.729 158.885 1.00 33.79  ? 84   SER A OG    1 
ATOM   537  N N     . SER A 1 85   ? 173.592 188.656 161.047 1.00 35.98  ? 85   SER A N     1 
ATOM   538  C CA    . SER A 1 85   ? 172.486 189.603 161.061 1.00 26.56  ? 85   SER A CA    1 
ATOM   539  C C     . SER A 1 85   ? 172.373 190.374 162.369 1.00 28.86  ? 85   SER A C     1 
ATOM   540  O O     . SER A 1 85   ? 171.643 191.369 162.418 1.00 32.51  ? 85   SER A O     1 
ATOM   541  C CB    . SER A 1 85   ? 171.173 188.870 160.789 1.00 28.07  ? 85   SER A CB    1 
ATOM   542  O OG    . SER A 1 85   ? 171.236 188.133 159.580 1.00 28.64  ? 85   SER A OG    1 
ATOM   543  N N     . LEU A 1 86   ? 173.064 189.938 163.421 1.00 35.76  ? 86   LEU A N     1 
ATOM   544  C CA    . LEU A 1 86   ? 172.972 190.621 164.710 1.00 37.20  ? 86   LEU A CA    1 
ATOM   545  C C     . LEU A 1 86   ? 173.385 192.090 164.672 1.00 39.59  ? 86   LEU A C     1 
ATOM   546  O O     . LEU A 1 86   ? 172.701 192.903 165.317 1.00 39.89  ? 86   LEU A O     1 
ATOM   547  C CB    . LEU A 1 86   ? 173.790 189.855 165.757 1.00 33.59  ? 86   LEU A CB    1 
ATOM   548  C CG    . LEU A 1 86   ? 173.164 188.558 166.269 1.00 29.31  ? 86   LEU A CG    1 
ATOM   549  C CD1   . LEU A 1 86   ? 174.097 187.861 167.242 1.00 31.12  ? 86   LEU A CD1   1 
ATOM   550  C CD2   . LEU A 1 86   ? 171.826 188.843 166.923 1.00 29.39  ? 86   LEU A CD2   1 
ATOM   551  N N     . PRO A 1 87   ? 174.461 192.501 163.987 1.00 40.68  ? 87   PRO A N     1 
ATOM   552  C CA    . PRO A 1 87   ? 174.822 193.931 163.983 1.00 37.71  ? 87   PRO A CA    1 
ATOM   553  C C     . PRO A 1 87   ? 173.747 194.857 163.429 1.00 37.75  ? 87   PRO A C     1 
ATOM   554  O O     . PRO A 1 87   ? 173.909 196.079 163.529 1.00 41.34  ? 87   PRO A O     1 
ATOM   555  C CB    . PRO A 1 87   ? 176.082 193.972 163.110 1.00 36.91  ? 87   PRO A CB    1 
ATOM   556  C CG    . PRO A 1 87   ? 176.676 192.634 163.269 1.00 36.72  ? 87   PRO A CG    1 
ATOM   557  C CD    . PRO A 1 87   ? 175.517 191.688 163.356 1.00 37.87  ? 87   PRO A CD    1 
ATOM   558  N N     . LEU A 1 88   ? 172.669 194.325 162.847 1.00 37.92  ? 88   LEU A N     1 
ATOM   559  C CA    . LEU A 1 88   ? 171.610 195.184 162.327 1.00 35.58  ? 88   LEU A CA    1 
ATOM   560  C C     . LEU A 1 88   ? 170.924 195.963 163.443 1.00 37.86  ? 88   LEU A C     1 
ATOM   561  O O     . LEU A 1 88   ? 170.607 197.147 163.277 1.00 40.30  ? 88   LEU A O     1 
ATOM   562  C CB    . LEU A 1 88   ? 170.593 194.349 161.548 1.00 34.12  ? 88   LEU A CB    1 
ATOM   563  C CG    . LEU A 1 88   ? 171.066 193.818 160.195 1.00 27.72  ? 88   LEU A CG    1 
ATOM   564  C CD1   . LEU A 1 88   ? 170.044 192.875 159.600 1.00 20.48  ? 88   LEU A CD1   1 
ATOM   565  C CD2   . LEU A 1 88   ? 171.346 194.964 159.240 1.00 28.32  ? 88   LEU A CD2   1 
ATOM   566  N N     . ILE A 1 89   ? 170.685 195.321 164.586 1.00 43.75  ? 89   ILE A N     1 
ATOM   567  C CA    . ILE A 1 89   ? 169.979 195.965 165.688 1.00 41.85  ? 89   ILE A CA    1 
ATOM   568  C C     . ILE A 1 89   ? 170.972 196.493 166.714 1.00 43.06  ? 89   ILE A C     1 
ATOM   569  O O     . ILE A 1 89   ? 170.731 197.526 167.350 1.00 45.35  ? 89   ILE A O     1 
ATOM   570  C CB    . ILE A 1 89   ? 168.967 195.006 166.342 1.00 36.12  ? 89   ILE A CB    1 
ATOM   571  C CG1   . ILE A 1 89   ? 169.643 193.707 166.778 1.00 36.85  ? 89   ILE A CG1   1 
ATOM   572  C CG2   . ILE A 1 89   ? 167.836 194.702 165.385 1.00 41.95  ? 89   ILE A CG2   1 
ATOM   573  C CD1   . ILE A 1 89   ? 168.688 192.710 167.393 1.00 34.53  ? 89   ILE A CD1   1 
ATOM   574  N N     . GLY A 1 90   ? 172.092 195.797 166.884 1.00 43.05  ? 90   GLY A N     1 
ATOM   575  C CA    . GLY A 1 90   ? 173.107 196.233 167.823 1.00 44.49  ? 90   GLY A CA    1 
ATOM   576  C C     . GLY A 1 90   ? 172.724 196.022 169.274 1.00 44.52  ? 90   GLY A C     1 
ATOM   577  O O     . GLY A 1 90   ? 172.576 196.987 170.030 1.00 39.18  ? 90   GLY A O     1 
ATOM   578  N N     . VAL A 1 91   ? 172.555 194.763 169.668 1.00 43.32  ? 91   VAL A N     1 
ATOM   579  C CA    . VAL A 1 91   ? 172.236 194.454 171.066 1.00 43.63  ? 91   VAL A CA    1 
ATOM   580  C C     . VAL A 1 91   ? 173.414 194.859 171.943 1.00 49.25  ? 91   VAL A C     1 
ATOM   581  O O     . VAL A 1 91   ? 174.579 194.689 171.527 1.00 47.03  ? 91   VAL A O     1 
ATOM   582  C CB    . VAL A 1 91   ? 171.919 192.957 171.225 1.00 45.13  ? 91   VAL A CB    1 
ATOM   583  C CG1   . VAL A 1 91   ? 171.202 192.687 172.533 1.00 43.18  ? 91   VAL A CG1   1 
ATOM   584  C CG2   . VAL A 1 91   ? 171.094 192.466 170.054 1.00 46.40  ? 91   VAL A CG2   1 
ATOM   585  N N     . PRO A 1 92   ? 173.192 195.406 173.139 1.00 48.31  ? 92   PRO A N     1 
ATOM   586  C CA    . PRO A 1 92   ? 174.323 195.757 174.004 1.00 43.20  ? 92   PRO A CA    1 
ATOM   587  C C     . PRO A 1 92   ? 175.119 194.527 174.410 1.00 48.17  ? 92   PRO A C     1 
ATOM   588  O O     . PRO A 1 92   ? 174.587 193.420 174.516 1.00 51.10  ? 92   PRO A O     1 
ATOM   589  C CB    . PRO A 1 92   ? 173.653 196.413 175.217 1.00 41.45  ? 92   PRO A CB    1 
ATOM   590  C CG    . PRO A 1 92   ? 172.342 196.887 174.714 1.00 47.83  ? 92   PRO A CG    1 
ATOM   591  C CD    . PRO A 1 92   ? 171.913 195.882 173.692 1.00 47.96  ? 92   PRO A CD    1 
ATOM   592  N N     . ASP A 1 93   ? 176.415 194.733 174.628 1.00 44.57  ? 93   ASP A N     1 
ATOM   593  C CA    . ASP A 1 93   ? 177.290 193.641 175.027 1.00 49.88  ? 93   ASP A CA    1 
ATOM   594  C C     . ASP A 1 93   ? 176.931 193.146 176.421 1.00 46.65  ? 93   ASP A C     1 
ATOM   595  O O     . ASP A 1 93   ? 176.531 193.923 177.292 1.00 46.50  ? 93   ASP A O     1 
ATOM   596  C CB    . ASP A 1 93   ? 178.751 194.089 174.994 1.00 56.61  ? 93   ASP A CB    1 
ATOM   597  C CG    . ASP A 1 93   ? 179.229 194.417 173.595 1.00 63.31  ? 93   ASP A CG    1 
ATOM   598  O OD1   . ASP A 1 93   ? 178.773 193.755 172.639 1.00 66.95  ? 93   ASP A OD1   1 
ATOM   599  O OD2   . ASP A 1 93   ? 180.061 195.337 173.451 1.00 68.54  ? 93   ASP A OD2   1 
ATOM   600  N N     . ILE A 1 94   ? 177.076 191.838 176.629 1.00 48.09  ? 94   ILE A N     1 
ATOM   601  C CA    . ILE A 1 94   ? 176.802 191.251 177.933 1.00 45.01  ? 94   ILE A CA    1 
ATOM   602  C C     . ILE A 1 94   ? 177.882 191.680 178.914 1.00 49.90  ? 94   ILE A C     1 
ATOM   603  O O     . ILE A 1 94   ? 179.082 191.512 178.658 1.00 52.46  ? 94   ILE A O     1 
ATOM   604  C CB    . ILE A 1 94   ? 176.716 189.722 177.827 1.00 40.47  ? 94   ILE A CB    1 
ATOM   605  C CG1   . ILE A 1 94   ? 175.437 189.312 177.096 1.00 42.85  ? 94   ILE A CG1   1 
ATOM   606  C CG2   . ILE A 1 94   ? 176.782 189.086 179.202 1.00 40.58  ? 94   ILE A CG2   1 
ATOM   607  C CD1   . ILE A 1 94   ? 175.238 187.818 177.002 1.00 39.04  ? 94   ILE A CD1   1 
ATOM   608  N N     . LEU A 1 95   ? 177.462 192.245 180.043 1.00 48.70  ? 95   LEU A N     1 
ATOM   609  C CA    . LEU A 1 95   ? 178.396 192.690 181.067 1.00 48.10  ? 95   LEU A CA    1 
ATOM   610  C C     . LEU A 1 95   ? 178.657 191.552 182.041 1.00 52.94  ? 95   LEU A C     1 
ATOM   611  O O     . LEU A 1 95   ? 177.708 191.059 182.665 1.00 56.55  ? 95   LEU A O     1 
ATOM   612  C CB    . LEU A 1 95   ? 177.846 193.897 181.807 1.00 47.54  ? 95   LEU A CB    1 
ATOM   613  C CG    . LEU A 1 95   ? 178.725 194.491 182.910 1.00 51.37  ? 95   LEU A CG    1 
ATOM   614  C CD1   . LEU A 1 95   ? 180.087 194.877 182.364 1.00 56.47  ? 95   LEU A CD1   1 
ATOM   615  C CD2   . LEU A 1 95   ? 178.045 195.691 183.542 1.00 47.10  ? 95   LEU A CD2   1 
ATOM   616  N N     . PRO A 1 96   ? 179.903 191.093 182.191 1.00 54.47  ? 96   PRO A N     1 
ATOM   617  C CA    . PRO A 1 96   ? 180.177 189.996 183.129 1.00 53.81  ? 96   PRO A CA    1 
ATOM   618  C C     . PRO A 1 96   ? 179.877 190.383 184.567 1.00 57.47  ? 96   PRO A C     1 
ATOM   619  O O     . PRO A 1 96   ? 180.546 191.249 185.140 1.00 60.47  ? 96   PRO A O     1 
ATOM   620  C CB    . PRO A 1 96   ? 181.671 189.719 182.920 1.00 57.47  ? 96   PRO A CB    1 
ATOM   621  C CG    . PRO A 1 96   ? 181.976 190.268 181.564 1.00 55.65  ? 96   PRO A CG    1 
ATOM   622  C CD    . PRO A 1 96   ? 181.096 191.469 181.418 1.00 54.76  ? 96   PRO A CD    1 
ATOM   623  N N     . LEU A 1 97   ? 178.869 189.744 185.158 1.00 55.20  ? 97   LEU A N     1 
ATOM   624  C CA    . LEU A 1 97   ? 178.423 190.053 186.508 1.00 51.18  ? 97   LEU A CA    1 
ATOM   625  C C     . LEU A 1 97   ? 178.212 188.769 187.293 1.00 54.64  ? 97   LEU A C     1 
ATOM   626  O O     . LEU A 1 97   ? 177.713 187.776 186.757 1.00 52.12  ? 97   LEU A O     1 
ATOM   627  C CB    . LEU A 1 97   ? 177.119 190.858 186.496 1.00 49.58  ? 97   LEU A CB    1 
ATOM   628  C CG    . LEU A 1 97   ? 177.167 192.281 185.949 1.00 50.00  ? 97   LEU A CG    1 
ATOM   629  C CD1   . LEU A 1 97   ? 175.768 192.857 185.904 1.00 44.20  ? 97   LEU A CD1   1 
ATOM   630  C CD2   . LEU A 1 97   ? 178.075 193.144 186.801 1.00 51.06  ? 97   LEU A CD2   1 
ATOM   631  N N     . ARG A 1 98   ? 178.590 188.801 188.568 1.00 55.21  ? 98   ARG A N     1 
ATOM   632  C CA    . ARG A 1 98   ? 178.319 187.719 189.502 1.00 53.45  ? 98   ARG A CA    1 
ATOM   633  C C     . ARG A 1 98   ? 177.463 188.260 190.636 1.00 53.71  ? 98   ARG A C     1 
ATOM   634  O O     . ARG A 1 98   ? 177.808 189.273 191.251 1.00 51.91  ? 98   ARG A O     1 
ATOM   635  C CB    . ARG A 1 98   ? 179.615 187.114 190.046 1.00 55.81  ? 98   ARG A CB    1 
ATOM   636  C CG    . ARG A 1 98   ? 180.432 186.361 189.009 1.00 63.09  ? 98   ARG A CG    1 
ATOM   637  C CD    . ARG A 1 98   ? 179.600 185.288 188.328 1.00 60.10  ? 98   ARG A CD    1 
ATOM   638  N NE    . ARG A 1 98   ? 180.401 184.441 187.454 1.00 66.18  ? 98   ARG A NE    1 
ATOM   639  C CZ    . ARG A 1 98   ? 180.676 184.716 186.186 1.00 75.91  ? 98   ARG A CZ    1 
ATOM   640  N NH1   . ARG A 1 98   ? 180.240 185.824 185.609 1.00 73.61  ? 98   ARG A NH1   1 
ATOM   641  N NH2   . ARG A 1 98   ? 181.411 183.861 185.481 1.00 77.48  ? 98   ARG A NH2   1 
ATOM   642  N N     . ALA A 1 99   ? 176.351 187.586 190.908 1.00 51.50  ? 99   ALA A N     1 
ATOM   643  C CA    . ALA A 1 99   ? 175.396 188.041 191.905 1.00 43.05  ? 99   ALA A CA    1 
ATOM   644  C C     . ALA A 1 99   ? 175.770 187.531 193.290 1.00 51.32  ? 99   ALA A C     1 
ATOM   645  O O     . ALA A 1 99   ? 176.396 186.480 193.443 1.00 58.91  ? 99   ALA A O     1 
ATOM   646  C CB    . ALA A 1 99   ? 173.983 187.580 191.549 1.00 37.84  ? 99   ALA A CB    1 
ATOM   647  N N     . SER A 1 100  ? 175.382 188.299 194.305 1.00 51.44  ? 100  SER A N     1 
ATOM   648  C CA    . SER A 1 100  ? 175.550 187.918 195.701 1.00 46.25  ? 100  SER A CA    1 
ATOM   649  C C     . SER A 1 100  ? 174.175 187.871 196.347 1.00 50.11  ? 100  SER A C     1 
ATOM   650  O O     . SER A 1 100  ? 173.462 188.880 196.369 1.00 53.34  ? 100  SER A O     1 
ATOM   651  C CB    . SER A 1 100  ? 176.461 188.900 196.437 1.00 50.11  ? 100  SER A CB    1 
ATOM   652  O OG    . SER A 1 100  ? 176.570 188.559 197.806 1.00 57.86  ? 100  SER A OG    1 
ATOM   653  N N     . LEU A 1 101  ? 173.805 186.707 196.869 1.00 46.16  ? 101  LEU A N     1 
ATOM   654  C CA    . LEU A 1 101  ? 172.474 186.484 197.412 1.00 43.10  ? 101  LEU A CA    1 
ATOM   655  C C     . LEU A 1 101  ? 172.490 186.613 198.928 1.00 45.12  ? 101  LEU A C     1 
ATOM   656  O O     . LEU A 1 101  ? 173.355 186.048 199.603 1.00 50.01  ? 101  LEU A O     1 
ATOM   657  C CB    . LEU A 1 101  ? 171.950 185.103 197.016 1.00 41.97  ? 101  LEU A CB    1 
ATOM   658  C CG    . LEU A 1 101  ? 172.056 184.731 195.538 1.00 35.62  ? 101  LEU A CG    1 
ATOM   659  C CD1   . LEU A 1 101  ? 171.386 183.392 195.281 1.00 37.05  ? 101  LEU A CD1   1 
ATOM   660  C CD2   . LEU A 1 101  ? 171.449 185.812 194.669 1.00 36.90  ? 101  LEU A CD2   1 
ATOM   661  N N     . SER A 1 102  ? 171.528 187.362 199.456 1.00 38.79  ? 102  SER A N     1 
ATOM   662  C CA    . SER A 1 102  ? 171.313 187.478 200.888 1.00 45.13  ? 102  SER A CA    1 
ATOM   663  C C     . SER A 1 102  ? 169.894 187.039 201.218 1.00 48.24  ? 102  SER A C     1 
ATOM   664  O O     . SER A 1 102  ? 169.037 186.924 200.339 1.00 52.31  ? 102  SER A O     1 
ATOM   665  C CB    . SER A 1 102  ? 171.553 188.909 201.382 1.00 54.17  ? 102  SER A CB    1 
ATOM   666  O OG    . SER A 1 102  ? 172.926 189.251 201.312 1.00 55.66  ? 102  SER A OG    1 
ATOM   667  N N     . SER A 1 103  ? 169.651 186.794 202.503 1.00 49.08  ? 103  SER A N     1 
ATOM   668  C CA    . SER A 1 103  ? 168.350 186.315 202.942 1.00 52.48  ? 103  SER A CA    1 
ATOM   669  C C     . SER A 1 103  ? 168.132 186.695 204.397 1.00 56.33  ? 103  SER A C     1 
ATOM   670  O O     . SER A 1 103  ? 169.072 187.026 205.124 1.00 56.44  ? 103  SER A O     1 
ATOM   671  C CB    . SER A 1 103  ? 168.223 184.799 202.763 1.00 51.63  ? 103  SER A CB    1 
ATOM   672  O OG    . SER A 1 103  ? 166.975 184.336 203.242 1.00 59.43  ? 103  SER A OG    1 
ATOM   673  N N     . ARG A 1 104  ? 166.868 186.650 204.811 1.00 55.64  ? 104  ARG A N     1 
ATOM   674  C CA    . ARG A 1 104  ? 166.483 186.853 206.198 1.00 58.14  ? 104  ARG A CA    1 
ATOM   675  C C     . ARG A 1 104  ? 165.499 185.766 206.603 1.00 60.31  ? 104  ARG A C     1 
ATOM   676  O O     . ARG A 1 104  ? 164.635 185.373 205.815 1.00 56.92  ? 104  ARG A O     1 
ATOM   677  C CB    . ARG A 1 104  ? 165.864 188.241 206.419 1.00 55.08  ? 104  ARG A CB    1 
ATOM   678  C CG    . ARG A 1 104  ? 164.625 188.519 205.587 1.00 63.92  ? 104  ARG A CG    1 
ATOM   679  C CD    . ARG A 1 104  ? 163.966 189.823 206.000 1.00 64.38  ? 104  ARG A CD    1 
ATOM   680  N NE    . ARG A 1 104  ? 162.797 190.122 205.182 1.00 73.19  ? 104  ARG A NE    1 
ATOM   681  C CZ    . ARG A 1 104  ? 161.574 189.677 205.433 1.00 78.40  ? 104  ARG A CZ    1 
ATOM   682  N NH1   . ARG A 1 104  ? 161.320 188.906 206.478 1.00 70.47  ? 104  ARG A NH1   1 
ATOM   683  N NH2   . ARG A 1 104  ? 160.580 190.011 204.614 1.00 78.90  ? 104  ARG A NH2   1 
ATOM   684  N N     . GLY A 1 105  ? 165.641 185.279 207.832 1.00 61.46  ? 105  GLY A N     1 
ATOM   685  C CA    . GLY A 1 105  ? 164.789 184.211 208.308 1.00 61.94  ? 105  GLY A CA    1 
ATOM   686  C C     . GLY A 1 105  ? 165.188 182.859 207.743 1.00 63.98  ? 105  GLY A C     1 
ATOM   687  O O     . GLY A 1 105  ? 166.296 182.656 207.238 1.00 65.85  ? 105  GLY A O     1 
ATOM   688  N N     . ALA A 1 106  ? 164.251 181.918 207.835 1.00 63.75  ? 106  ALA A N     1 
ATOM   689  C CA    . ALA A 1 106  ? 164.445 180.556 207.365 1.00 61.36  ? 106  ALA A CA    1 
ATOM   690  C C     . ALA A 1 106  ? 163.271 180.155 206.484 1.00 57.35  ? 106  ALA A C     1 
ATOM   691  O O     . ALA A 1 106  ? 162.266 180.863 206.394 1.00 64.08  ? 106  ALA A O     1 
ATOM   692  C CB    . ALA A 1 106  ? 164.596 179.575 208.536 1.00 65.34  ? 106  ALA A CB    1 
ATOM   693  N N     . LEU A 1 107  ? 163.408 178.999 205.829 1.00 50.68  ? 107  LEU A N     1 
ATOM   694  C CA    . LEU A 1 107  ? 162.351 178.521 204.942 1.00 51.27  ? 107  LEU A CA    1 
ATOM   695  C C     . LEU A 1 107  ? 161.044 178.299 205.689 1.00 64.96  ? 107  LEU A C     1 
ATOM   696  O O     . LEU A 1 107  ? 159.965 178.436 205.104 1.00 66.95  ? 107  LEU A O     1 
ATOM   697  C CB    . LEU A 1 107  ? 162.784 177.227 204.252 1.00 46.18  ? 107  LEU A CB    1 
ATOM   698  C CG    . LEU A 1 107  ? 164.000 177.273 203.327 1.00 48.41  ? 107  LEU A CG    1 
ATOM   699  C CD1   . LEU A 1 107  ? 164.334 175.877 202.841 1.00 49.57  ? 107  LEU A CD1   1 
ATOM   700  C CD2   . LEU A 1 107  ? 163.753 178.197 202.151 1.00 48.91  ? 107  LEU A CD2   1 
ATOM   701  N N     . SER A 1 108  ? 161.119 177.956 206.978 1.00 65.40  ? 108  SER A N     1 
ATOM   702  C CA    . SER A 1 108  ? 159.908 177.751 207.765 1.00 64.88  ? 108  SER A CA    1 
ATOM   703  C C     . SER A 1 108  ? 159.126 179.048 207.928 1.00 65.39  ? 108  SER A C     1 
ATOM   704  O O     . SER A 1 108  ? 157.890 179.041 207.911 1.00 66.64  ? 108  SER A O     1 
ATOM   705  C CB    . SER A 1 108  ? 160.263 177.164 209.130 1.00 70.74  ? 108  SER A CB    1 
ATOM   706  O OG    . SER A 1 108  ? 161.145 178.016 209.839 1.00 72.99  ? 108  SER A OG    1 
ATOM   707  N N     . ASP A 1 109  ? 159.828 180.166 208.094 1.00 67.07  ? 109  ASP A N     1 
ATOM   708  C CA    . ASP A 1 109  ? 159.166 181.448 208.289 1.00 69.58  ? 109  ASP A CA    1 
ATOM   709  C C     . ASP A 1 109  ? 158.380 181.844 207.045 1.00 69.69  ? 109  ASP A C     1 
ATOM   710  O O     . ASP A 1 109  ? 158.848 181.681 205.915 1.00 64.70  ? 109  ASP A O     1 
ATOM   711  C CB    . ASP A 1 109  ? 160.196 182.529 208.620 1.00 70.49  ? 109  ASP A CB    1 
ATOM   712  C CG    . ASP A 1 109  ? 161.116 182.131 209.757 1.00 72.84  ? 109  ASP A CG    1 
ATOM   713  O OD1   . ASP A 1 109  ? 160.668 181.395 210.661 1.00 77.15  ? 109  ASP A OD1   1 
ATOM   714  O OD2   . ASP A 1 109  ? 162.290 182.554 209.746 1.00 71.22  ? 109  ASP A OD2   1 
ATOM   715  N N     . SER A 1 110  ? 157.171 182.366 207.261 1.00 76.33  ? 110  SER A N     1 
ATOM   716  C CA    . SER A 1 110  ? 156.363 182.855 206.151 1.00 78.28  ? 110  SER A CA    1 
ATOM   717  C C     . SER A 1 110  ? 156.860 184.194 205.628 1.00 80.56  ? 110  SER A C     1 
ATOM   718  O O     . SER A 1 110  ? 156.445 184.614 204.542 1.00 81.09  ? 110  SER A O     1 
ATOM   719  C CB    . SER A 1 110  ? 154.899 182.968 206.574 1.00 76.42  ? 110  SER A CB    1 
ATOM   720  O OG    . SER A 1 110  ? 154.381 181.702 206.944 1.00 78.12  ? 110  SER A OG    1 
ATOM   721  N N     . ASP A 1 111  ? 157.736 184.870 206.372 1.00 75.43  ? 111  ASP A N     1 
ATOM   722  C CA    . ASP A 1 111  ? 158.354 186.113 205.937 1.00 73.29  ? 111  ASP A CA    1 
ATOM   723  C C     . ASP A 1 111  ? 159.713 185.888 205.286 1.00 68.69  ? 111  ASP A C     1 
ATOM   724  O O     . ASP A 1 111  ? 160.477 186.845 205.119 1.00 74.27  ? 111  ASP A O     1 
ATOM   725  C CB    . ASP A 1 111  ? 158.490 187.077 207.118 1.00 79.31  ? 111  ASP A CB    1 
ATOM   726  C CG    . ASP A 1 111  ? 157.152 187.607 207.595 1.00 84.68  ? 111  ASP A CG    1 
ATOM   727  O OD1   . ASP A 1 111  ? 156.254 187.804 206.749 1.00 82.50  ? 111  ASP A OD1   1 
ATOM   728  O OD2   . ASP A 1 111  ? 156.998 187.827 208.814 1.00 84.07  ? 111  ASP A OD2   1 
ATOM   729  N N     . PHE A 1 112  ? 160.030 184.646 204.930 1.00 64.21  ? 112  PHE A N     1 
ATOM   730  C CA    . PHE A 1 112  ? 161.286 184.345 204.258 1.00 59.28  ? 112  PHE A CA    1 
ATOM   731  C C     . PHE A 1 112  ? 161.360 185.071 202.922 1.00 60.30  ? 112  PHE A C     1 
ATOM   732  O O     . PHE A 1 112  ? 160.364 185.187 202.206 1.00 68.75  ? 112  PHE A O     1 
ATOM   733  C CB    . PHE A 1 112  ? 161.411 182.837 204.048 1.00 56.88  ? 112  PHE A CB    1 
ATOM   734  C CG    . PHE A 1 112  ? 162.660 182.419 203.330 1.00 51.55  ? 112  PHE A CG    1 
ATOM   735  C CD1   . PHE A 1 112  ? 163.866 182.343 204.002 1.00 55.10  ? 112  PHE A CD1   1 
ATOM   736  C CD2   . PHE A 1 112  ? 162.624 182.081 201.990 1.00 47.37  ? 112  PHE A CD2   1 
ATOM   737  C CE1   . PHE A 1 112  ? 165.013 181.949 203.349 1.00 53.28  ? 112  PHE A CE1   1 
ATOM   738  C CE2   . PHE A 1 112  ? 163.769 181.687 201.332 1.00 49.87  ? 112  PHE A CE2   1 
ATOM   739  C CZ    . PHE A 1 112  ? 164.965 181.620 202.015 1.00 52.54  ? 112  PHE A CZ    1 
ATOM   740  N N     . ARG A 1 113  ? 162.548 185.571 202.591 1.00 57.73  ? 113  ARG A N     1 
ATOM   741  C CA    . ARG A 1 113  ? 162.734 186.279 201.331 1.00 56.59  ? 113  ARG A CA    1 
ATOM   742  C C     . ARG A 1 113  ? 164.199 186.216 200.929 1.00 51.05  ? 113  ARG A C     1 
ATOM   743  O O     . ARG A 1 113  ? 165.084 186.411 201.768 1.00 47.53  ? 113  ARG A O     1 
ATOM   744  C CB    . ARG A 1 113  ? 162.270 187.734 201.444 1.00 59.79  ? 113  ARG A CB    1 
ATOM   745  C CG    . ARG A 1 113  ? 162.357 188.505 200.139 1.00 64.75  ? 113  ARG A CG    1 
ATOM   746  C CD    . ARG A 1 113  ? 161.884 189.936 200.298 1.00 59.84  ? 113  ARG A CD    1 
ATOM   747  N NE    . ARG A 1 113  ? 162.073 190.700 199.071 1.00 60.37  ? 113  ARG A NE    1 
ATOM   748  C CZ    . ARG A 1 113  ? 163.150 191.424 198.799 1.00 59.69  ? 113  ARG A CZ    1 
ATOM   749  N NH1   . ARG A 1 113  ? 164.156 191.513 199.652 1.00 58.26  ? 113  ARG A NH1   1 
ATOM   750  N NH2   . ARG A 1 113  ? 163.218 192.075 197.641 1.00 54.78  ? 113  ARG A NH2   1 
ATOM   751  N N     . VAL A 1 114  ? 164.446 185.940 199.651 1.00 49.33  ? 114  VAL A N     1 
ATOM   752  C CA    . VAL A 1 114  ? 165.786 185.917 199.077 1.00 47.36  ? 114  VAL A CA    1 
ATOM   753  C C     . VAL A 1 114  ? 165.872 187.014 198.027 1.00 48.62  ? 114  VAL A C     1 
ATOM   754  O O     . VAL A 1 114  ? 165.034 187.079 197.120 1.00 48.08  ? 114  VAL A O     1 
ATOM   755  C CB    . VAL A 1 114  ? 166.123 184.548 198.461 1.00 45.44  ? 114  VAL A CB    1 
ATOM   756  C CG1   . VAL A 1 114  ? 167.329 184.660 197.547 1.00 39.95  ? 114  VAL A CG1   1 
ATOM   757  C CG2   . VAL A 1 114  ? 166.388 183.536 199.550 1.00 47.54  ? 114  VAL A CG2   1 
ATOM   758  N N     . TRP A 1 115  ? 166.881 187.870 198.152 1.00 43.98  ? 115  TRP A N     1 
ATOM   759  C CA    . TRP A 1 115  ? 167.114 188.947 197.205 1.00 44.30  ? 115  TRP A CA    1 
ATOM   760  C C     . TRP A 1 115  ? 168.588 188.976 196.831 1.00 45.06  ? 115  TRP A C     1 
ATOM   761  O O     . TRP A 1 115  ? 169.452 188.529 197.589 1.00 48.77  ? 115  TRP A O     1 
ATOM   762  C CB    . TRP A 1 115  ? 166.689 190.305 197.779 1.00 49.09  ? 115  TRP A CB    1 
ATOM   763  C CG    . TRP A 1 115  ? 167.603 190.819 198.849 1.00 48.67  ? 115  TRP A CG    1 
ATOM   764  C CD1   . TRP A 1 115  ? 168.648 191.680 198.688 1.00 49.86  ? 115  TRP A CD1   1 
ATOM   765  C CD2   . TRP A 1 115  ? 167.554 190.505 200.245 1.00 47.23  ? 115  TRP A CD2   1 
ATOM   766  N NE1   . TRP A 1 115  ? 169.254 191.921 199.896 1.00 54.66  ? 115  TRP A NE1   1 
ATOM   767  C CE2   . TRP A 1 115  ? 168.600 191.211 200.868 1.00 53.28  ? 115  TRP A CE2   1 
ATOM   768  C CE3   . TRP A 1 115  ? 166.727 189.695 201.028 1.00 47.36  ? 115  TRP A CE3   1 
ATOM   769  C CZ2   . TRP A 1 115  ? 168.842 191.132 202.236 1.00 52.66  ? 115  TRP A CZ2   1 
ATOM   770  C CZ3   . TRP A 1 115  ? 166.969 189.619 202.385 1.00 51.70  ? 115  TRP A CZ3   1 
ATOM   771  C CH2   . TRP A 1 115  ? 168.017 190.333 202.976 1.00 52.40  ? 115  TRP A CH2   1 
ATOM   772  N N     . ILE A 1 116  ? 168.868 189.508 195.646 1.00 44.95  ? 116  ILE A N     1 
ATOM   773  C CA    . ILE A 1 116  ? 170.242 189.679 195.189 1.00 42.60  ? 116  ILE A CA    1 
ATOM   774  C C     . ILE A 1 116  ? 170.804 190.918 195.878 1.00 47.18  ? 116  ILE A C     1 
ATOM   775  O O     . ILE A 1 116  ? 170.428 192.046 195.553 1.00 46.32  ? 116  ILE A O     1 
ATOM   776  C CB    . ILE A 1 116  ? 170.319 189.802 193.665 1.00 38.44  ? 116  ILE A CB    1 
ATOM   777  C CG1   . ILE A 1 116  ? 169.729 188.552 193.012 1.00 32.83  ? 116  ILE A CG1   1 
ATOM   778  C CG2   . ILE A 1 116  ? 171.756 190.010 193.222 1.00 37.97  ? 116  ILE A CG2   1 
ATOM   779  C CD1   . ILE A 1 116  ? 169.731 188.584 191.512 1.00 29.84  ? 116  ILE A CD1   1 
ATOM   780  N N     . ALA A 1 117  ? 171.700 190.705 196.845 1.00 49.85  ? 117  ALA A N     1 
ATOM   781  C CA    . ALA A 1 117  ? 172.195 191.814 197.655 1.00 55.01  ? 117  ALA A CA    1 
ATOM   782  C C     . ALA A 1 117  ? 172.990 192.808 196.820 1.00 57.75  ? 117  ALA A C     1 
ATOM   783  O O     . ALA A 1 117  ? 172.830 194.024 196.973 1.00 57.38  ? 117  ALA A O     1 
ATOM   784  C CB    . ALA A 1 117  ? 173.046 191.283 198.807 1.00 52.48  ? 117  ALA A CB    1 
ATOM   785  N N     . GLU A 1 118  ? 173.851 192.314 195.935 1.00 53.41  ? 118  GLU A N     1 
ATOM   786  C CA    . GLU A 1 118  ? 174.697 193.194 195.144 1.00 52.16  ? 118  GLU A CA    1 
ATOM   787  C C     . GLU A 1 118  ? 175.148 192.464 193.889 1.00 50.85  ? 118  GLU A C     1 
ATOM   788  O O     . GLU A 1 118  ? 175.072 191.237 193.798 1.00 53.27  ? 118  GLU A O     1 
ATOM   789  C CB    . GLU A 1 118  ? 175.911 193.674 195.945 1.00 58.63  ? 118  GLU A CB    1 
ATOM   790  C CG    . GLU A 1 118  ? 176.829 192.553 196.399 1.00 64.03  ? 118  GLU A CG    1 
ATOM   791  C CD    . GLU A 1 118  ? 178.092 193.065 197.063 1.00 81.98  ? 118  GLU A CD    1 
ATOM   792  O OE1   . GLU A 1 118  ? 178.375 194.277 196.951 1.00 81.76  ? 118  GLU A OE1   1 
ATOM   793  O OE2   . GLU A 1 118  ? 178.801 192.256 197.697 1.00 84.17  ? 118  GLU A OE2   1 
ATOM   794  N N     . TRP A 1 119  ? 175.618 193.246 192.923 1.00 54.13  ? 119  TRP A N     1 
ATOM   795  C CA    . TRP A 1 119  ? 176.246 192.736 191.717 1.00 51.39  ? 119  TRP A CA    1 
ATOM   796  C C     . TRP A 1 119  ? 177.697 193.188 191.688 1.00 55.19  ? 119  TRP A C     1 
ATOM   797  O O     . TRP A 1 119  ? 178.034 194.271 192.174 1.00 59.45  ? 119  TRP A O     1 
ATOM   798  C CB    . TRP A 1 119  ? 175.532 193.225 190.453 1.00 46.78  ? 119  TRP A CB    1 
ATOM   799  C CG    . TRP A 1 119  ? 174.137 192.722 190.304 1.00 41.25  ? 119  TRP A CG    1 
ATOM   800  C CD1   . TRP A 1 119  ? 173.001 193.304 190.782 1.00 38.42  ? 119  TRP A CD1   1 
ATOM   801  C CD2   . TRP A 1 119  ? 173.723 191.537 189.619 1.00 34.52  ? 119  TRP A CD2   1 
ATOM   802  N NE1   . TRP A 1 119  ? 171.905 192.552 190.441 1.00 33.67  ? 119  TRP A NE1   1 
ATOM   803  C CE2   . TRP A 1 119  ? 172.322 191.461 189.725 1.00 35.41  ? 119  TRP A CE2   1 
ATOM   804  C CE3   . TRP A 1 119  ? 174.402 190.531 188.926 1.00 34.06  ? 119  TRP A CE3   1 
ATOM   805  C CZ2   . TRP A 1 119  ? 171.588 190.420 189.165 1.00 33.24  ? 119  TRP A CZ2   1 
ATOM   806  C CZ3   . TRP A 1 119  ? 173.671 189.498 188.373 1.00 33.55  ? 119  TRP A CZ3   1 
ATOM   807  C CH2   . TRP A 1 119  ? 172.279 189.450 188.497 1.00 30.99  ? 119  TRP A CH2   1 
ATOM   808  N N     . ALA A 1 120  ? 178.557 192.351 191.118 1.00 52.34  ? 120  ALA A N     1 
ATOM   809  C CA    . ALA A 1 120  ? 179.973 192.666 191.033 1.00 59.54  ? 120  ALA A CA    1 
ATOM   810  C C     . ALA A 1 120  ? 180.527 192.177 189.705 1.00 64.95  ? 120  ALA A C     1 
ATOM   811  O O     . ALA A 1 120  ? 180.016 191.223 189.113 1.00 62.60  ? 120  ALA A O     1 
ATOM   812  C CB    . ALA A 1 120  ? 180.760 192.045 192.193 1.00 66.04  ? 120  ALA A CB    1 
ATOM   813  N N     . THR A 1 121  ? 181.576 192.852 189.242 1.00 70.95  ? 121  THR A N     1 
ATOM   814  C CA    . THR A 1 121  ? 182.291 192.406 188.055 1.00 67.27  ? 121  THR A CA    1 
ATOM   815  C C     . THR A 1 121  ? 182.950 191.060 188.327 1.00 69.78  ? 121  THR A C     1 
ATOM   816  O O     . THR A 1 121  ? 183.487 190.824 189.411 1.00 76.98  ? 121  THR A O     1 
ATOM   817  C CB    . THR A 1 121  ? 183.342 193.441 187.655 1.00 74.60  ? 121  THR A CB    1 
ATOM   818  O OG1   . THR A 1 121  ? 182.798 194.757 187.802 1.00 69.07  ? 121  THR A OG1   1 
ATOM   819  C CG2   . THR A 1 121  ? 183.766 193.242 186.209 1.00 82.69  ? 121  THR A CG2   1 
ATOM   820  N N     . PHE A 1 122  ? 182.892 190.165 187.342 1.00 67.45  ? 122  PHE A N     1 
ATOM   821  C CA    . PHE A 1 122  ? 183.433 188.823 187.548 1.00 75.67  ? 122  PHE A CA    1 
ATOM   822  C C     . PHE A 1 122  ? 184.934 188.821 187.819 1.00 85.21  ? 122  PHE A C     1 
ATOM   823  O O     . PHE A 1 122  ? 185.355 188.194 188.807 1.00 85.93  ? 122  PHE A O     1 
ATOM   824  C CB    . PHE A 1 122  ? 183.066 187.931 186.357 1.00 73.04  ? 122  PHE A CB    1 
ATOM   825  C CG    . PHE A 1 122  ? 183.790 186.616 186.338 1.00 82.81  ? 122  PHE A CG    1 
ATOM   826  C CD1   . PHE A 1 122  ? 183.626 185.703 187.365 1.00 80.99  ? 122  PHE A CD1   1 
ATOM   827  C CD2   . PHE A 1 122  ? 184.630 186.290 185.287 1.00 83.20  ? 122  PHE A CD2   1 
ATOM   828  C CE1   . PHE A 1 122  ? 184.289 184.490 187.347 1.00 78.99  ? 122  PHE A CE1   1 
ATOM   829  C CE2   . PHE A 1 122  ? 185.296 185.080 185.263 1.00 81.44  ? 122  PHE A CE2   1 
ATOM   830  C CZ    . PHE A 1 122  ? 185.125 184.179 186.294 1.00 80.97  ? 122  PHE A CZ    1 
ATOM   831  N N     . PRO A 1 123  ? 185.793 189.481 187.019 1.00 83.61  ? 123  PRO A N     1 
ATOM   832  C CA    . PRO A 1 123  ? 187.223 189.485 187.357 1.00 83.27  ? 123  PRO A CA    1 
ATOM   833  C C     . PRO A 1 123  ? 187.588 190.502 188.430 1.00 87.71  ? 123  PRO A C     1 
ATOM   834  O O     . PRO A 1 123  ? 188.484 190.255 189.243 1.00 89.31  ? 123  PRO A O     1 
ATOM   835  C CB    . PRO A 1 123  ? 187.892 189.819 186.019 1.00 85.21  ? 123  PRO A CB    1 
ATOM   836  C CG    . PRO A 1 123  ? 186.899 190.664 185.324 1.00 86.81  ? 123  PRO A CG    1 
ATOM   837  C CD    . PRO A 1 123  ? 185.547 190.133 185.717 1.00 81.33  ? 123  PRO A CD    1 
ATOM   838  N N     . ALA A 1 124  ? 186.901 191.647 188.445 1.00 85.38  ? 124  ALA A N     1 
ATOM   839  C CA    . ALA A 1 124  ? 187.298 192.740 189.326 1.00 84.62  ? 124  ALA A CA    1 
ATOM   840  C C     . ALA A 1 124  ? 186.656 192.651 190.705 1.00 85.97  ? 124  ALA A C     1 
ATOM   841  O O     . ALA A 1 124  ? 187.227 193.159 191.677 1.00 86.32  ? 124  ALA A O     1 
ATOM   842  C CB    . ALA A 1 124  ? 186.955 194.083 188.680 1.00 82.41  ? 124  ALA A CB    1 
ATOM   843  N N     . ARG A 1 125  ? 185.482 192.022 190.809 1.00 83.98  ? 125  ARG A N     1 
ATOM   844  C CA    . ARG A 1 125  ? 184.743 191.915 192.071 1.00 80.55  ? 125  ARG A CA    1 
ATOM   845  C C     . ARG A 1 125  ? 184.442 193.292 192.661 1.00 79.31  ? 125  ARG A C     1 
ATOM   846  O O     . ARG A 1 125  ? 184.459 193.485 193.878 1.00 81.88  ? 125  ARG A O     1 
ATOM   847  C CB    . ARG A 1 125  ? 185.489 191.038 193.079 1.00 83.87  ? 125  ARG A CB    1 
ATOM   848  C CG    . ARG A 1 125  ? 185.770 189.634 192.577 1.00 88.15  ? 125  ARG A CG    1 
ATOM   849  C CD    . ARG A 1 125  ? 184.483 188.911 192.216 1.00 90.17  ? 125  ARG A CD    1 
ATOM   850  N NE    . ARG A 1 125  ? 184.740 187.645 191.539 1.00 96.14  ? 125  ARG A NE    1 
ATOM   851  C CZ    . ARG A 1 125  ? 184.921 186.487 192.158 1.00 98.95  ? 125  ARG A CZ    1 
ATOM   852  N NH1   . ARG A 1 125  ? 184.878 186.393 193.477 1.00 94.78  ? 125  ARG A NH1   1 
ATOM   853  N NH2   . ARG A 1 125  ? 185.153 185.395 191.435 1.00 98.25  ? 125  ARG A NH2   1 
ATOM   854  N N     . LYS A 1 126  ? 184.163 194.258 191.788 1.00 73.89  ? 126  LYS A N     1 
ATOM   855  C CA    . LYS A 1 126  ? 183.790 195.598 192.218 1.00 74.79  ? 126  LYS A CA    1 
ATOM   856  C C     . LYS A 1 126  ? 182.274 195.709 192.286 1.00 72.43  ? 126  LYS A C     1 
ATOM   857  O O     . LYS A 1 126  ? 181.602 195.414 191.290 1.00 71.39  ? 126  LYS A O     1 
ATOM   858  C CB    . LYS A 1 126  ? 184.333 196.644 191.261 1.00 80.03  ? 126  LYS A CB    1 
ATOM   859  C CG    . LYS A 1 126  ? 183.739 198.026 191.477 1.00 77.22  ? 126  LYS A CG    1 
ATOM   860  C CD    . LYS A 1 126  ? 183.600 198.782 190.168 1.00 79.83  ? 126  LYS A CD    1 
ATOM   861  C CE    . LYS A 1 126  ? 182.840 200.083 190.363 1.00 81.99  ? 126  LYS A CE    1 
ATOM   862  N NZ    . LYS A 1 126  ? 182.556 200.760 189.068 1.00 75.54  ? 126  LYS A NZ    1 
ATOM   863  N N     . PRO A 1 127  ? 181.698 196.103 193.420 1.00 70.63  ? 127  PRO A N     1 
ATOM   864  C CA    . PRO A 1 127  ? 180.245 196.304 193.473 1.00 67.20  ? 127  PRO A CA    1 
ATOM   865  C C     . PRO A 1 127  ? 179.797 197.368 192.482 1.00 69.02  ? 127  PRO A C     1 
ATOM   866  O O     . PRO A 1 127  ? 180.433 198.413 192.333 1.00 71.55  ? 127  PRO A O     1 
ATOM   867  C CB    . PRO A 1 127  ? 180.002 196.745 194.921 1.00 69.63  ? 127  PRO A CB    1 
ATOM   868  C CG    . PRO A 1 127  ? 181.180 196.225 195.679 1.00 68.76  ? 127  PRO A CG    1 
ATOM   869  C CD    . PRO A 1 127  ? 182.335 196.311 194.730 1.00 71.63  ? 127  PRO A CD    1 
ATOM   870  N N     . ILE A 1 128  ? 178.686 197.092 191.800 1.00 69.53  ? 128  ILE A N     1 
ATOM   871  C CA    . ILE A 1 128  ? 178.139 197.994 190.792 1.00 66.53  ? 128  ILE A CA    1 
ATOM   872  C C     . ILE A 1 128  ? 176.649 198.171 191.042 1.00 65.99  ? 128  ILE A C     1 
ATOM   873  O O     . ILE A 1 128  ? 175.954 197.222 191.419 1.00 69.63  ? 128  ILE A O     1 
ATOM   874  C CB    . ILE A 1 128  ? 178.367 197.480 189.355 1.00 62.98  ? 128  ILE A CB    1 
ATOM   875  C CG1   . ILE A 1 128  ? 179.745 196.849 189.197 1.00 66.08  ? 128  ILE A CG1   1 
ATOM   876  C CG2   . ILE A 1 128  ? 178.223 198.616 188.364 1.00 70.56  ? 128  ILE A CG2   1 
ATOM   877  C CD1   . ILE A 1 128  ? 179.980 196.282 187.822 1.00 62.71  ? 128  ILE A CD1   1 
ATOM   878  N N     . ARG A 1 129  ? 176.160 199.387 190.823 1.00 60.29  ? 129  ARG A N     1 
ATOM   879  C CA    . ARG A 1 129  ? 174.736 199.683 190.830 1.00 65.84  ? 129  ARG A CA    1 
ATOM   880  C C     . ARG A 1 129  ? 174.297 200.047 189.418 1.00 67.90  ? 129  ARG A C     1 
ATOM   881  O O     . ARG A 1 129  ? 175.015 200.747 188.697 1.00 68.49  ? 129  ARG A O     1 
ATOM   882  C CB    . ARG A 1 129  ? 174.415 200.823 191.799 1.00 70.13  ? 129  ARG A CB    1 
ATOM   883  C CG    . ARG A 1 129  ? 174.764 200.520 193.248 1.00 69.96  ? 129  ARG A CG    1 
ATOM   884  C CD    . ARG A 1 129  ? 173.939 199.359 193.780 1.00 72.02  ? 129  ARG A CD    1 
ATOM   885  N NE    . ARG A 1 129  ? 172.509 199.639 193.726 1.00 81.30  ? 129  ARG A NE    1 
ATOM   886  C CZ    . ARG A 1 129  ? 171.821 200.215 194.702 1.00 78.22  ? 129  ARG A CZ    1 
ATOM   887  N NH1   . ARG A 1 129  ? 172.400 200.581 195.833 1.00 75.33  ? 129  ARG A NH1   1 
ATOM   888  N NH2   . ARG A 1 129  ? 170.519 200.429 194.538 1.00 72.53  ? 129  ARG A NH2   1 
ATOM   889  N N     . PHE A 1 130  ? 173.121 199.567 189.022 1.00 66.39  ? 130  PHE A N     1 
ATOM   890  C CA    . PHE A 1 130  ? 172.623 199.751 187.667 1.00 62.85  ? 130  PHE A CA    1 
ATOM   891  C C     . PHE A 1 130  ? 171.230 200.364 187.692 1.00 65.01  ? 130  PHE A C     1 
ATOM   892  O O     . PHE A 1 130  ? 170.606 200.527 188.743 1.00 64.64  ? 130  PHE A O     1 
ATOM   893  C CB    . PHE A 1 130  ? 172.559 198.426 186.896 1.00 57.76  ? 130  PHE A CB    1 
ATOM   894  C CG    . PHE A 1 130  ? 173.839 197.651 186.897 1.00 61.37  ? 130  PHE A CG    1 
ATOM   895  C CD1   . PHE A 1 130  ? 174.846 197.953 186.000 1.00 65.91  ? 130  PHE A CD1   1 
ATOM   896  C CD2   . PHE A 1 130  ? 174.023 196.600 187.778 1.00 59.42  ? 130  PHE A CD2   1 
ATOM   897  C CE1   . PHE A 1 130  ? 176.021 197.234 185.991 1.00 65.28  ? 130  PHE A CE1   1 
ATOM   898  C CE2   . PHE A 1 130  ? 175.195 195.877 187.776 1.00 61.76  ? 130  PHE A CE2   1 
ATOM   899  C CZ    . PHE A 1 130  ? 176.195 196.194 186.881 1.00 65.06  ? 130  PHE A CZ    1 
ATOM   900  N N     . SER A 1 131  ? 170.754 200.701 186.497 1.00 59.27  ? 131  SER A N     1 
ATOM   901  C CA    . SER A 1 131  ? 169.345 200.960 186.233 1.00 58.82  ? 131  SER A CA    1 
ATOM   902  C C     . SER A 1 131  ? 168.896 199.930 185.209 1.00 57.83  ? 131  SER A C     1 
ATOM   903  O O     . SER A 1 131  ? 169.415 199.901 184.089 1.00 67.78  ? 131  SER A O     1 
ATOM   904  C CB    . SER A 1 131  ? 169.125 202.383 185.718 1.00 69.16  ? 131  SER A CB    1 
ATOM   905  O OG    . SER A 1 131  ? 167.770 202.597 185.364 1.00 73.31  ? 131  SER A OG    1 
ATOM   906  N N     . ARG A 1 132  ? 167.942 199.087 185.586 1.00 47.61  ? 132  ARG A N     1 
ATOM   907  C CA    . ARG A 1 132  ? 167.614 197.900 184.813 1.00 43.44  ? 132  ARG A CA    1 
ATOM   908  C C     . ARG A 1 132  ? 166.190 197.985 184.289 1.00 52.84  ? 132  ARG A C     1 
ATOM   909  O O     . ARG A 1 132  ? 165.262 198.296 185.042 1.00 53.43  ? 132  ARG A O     1 
ATOM   910  C CB    . ARG A 1 132  ? 167.786 196.637 185.657 1.00 43.83  ? 132  ARG A CB    1 
ATOM   911  C CG    . ARG A 1 132  ? 167.618 195.351 184.880 1.00 39.31  ? 132  ARG A CG    1 
ATOM   912  C CD    . ARG A 1 132  ? 167.723 194.147 185.791 1.00 38.37  ? 132  ARG A CD    1 
ATOM   913  N NE    . ARG A 1 132  ? 166.753 194.204 186.878 1.00 42.31  ? 132  ARG A NE    1 
ATOM   914  C CZ    . ARG A 1 132  ? 165.523 193.714 186.811 1.00 41.43  ? 132  ARG A CZ    1 
ATOM   915  N NH1   . ARG A 1 132  ? 165.075 193.119 185.719 1.00 42.51  ? 132  ARG A NH1   1 
ATOM   916  N NH2   . ARG A 1 132  ? 164.723 193.825 187.867 1.00 43.07  ? 132  ARG A NH2   1 
ATOM   917  N N     . THR A 1 133  ? 166.026 197.704 182.998 1.00 49.72  ? 133  THR A N     1 
ATOM   918  C CA    . THR A 1 133  ? 164.718 197.596 182.357 1.00 49.79  ? 133  THR A CA    1 
ATOM   919  C C     . THR A 1 133  ? 164.690 196.242 181.656 1.00 49.43  ? 133  THR A C     1 
ATOM   920  O O     . THR A 1 133  ? 165.270 196.085 180.578 1.00 52.88  ? 133  THR A O     1 
ATOM   921  C CB    . THR A 1 133  ? 164.478 198.738 181.376 1.00 49.81  ? 133  THR A CB    1 
ATOM   922  O OG1   . THR A 1 133  ? 164.586 199.992 182.062 1.00 46.12  ? 133  THR A OG1   1 
ATOM   923  C CG2   . THR A 1 133  ? 163.095 198.623 180.755 1.00 51.75  ? 133  THR A CG2   1 
ATOM   924  N N     . GLY A 1 134  ? 164.019 195.270 182.261 1.00 42.68  ? 134  GLY A N     1 
ATOM   925  C CA    . GLY A 1 134  ? 164.079 193.917 181.733 1.00 37.14  ? 134  GLY A CA    1 
ATOM   926  C C     . GLY A 1 134  ? 165.466 193.342 181.939 1.00 36.43  ? 134  GLY A C     1 
ATOM   927  O O     . GLY A 1 134  ? 166.006 193.356 183.049 1.00 41.85  ? 134  GLY A O     1 
ATOM   928  N N     . ALA A 1 135  ? 166.055 192.820 180.865 1.00 39.64  ? 135  ALA A N     1 
ATOM   929  C CA    . ALA A 1 135  ? 167.415 192.302 180.914 1.00 35.92  ? 135  ALA A CA    1 
ATOM   930  C C     . ALA A 1 135  ? 168.461 193.329 180.507 1.00 34.37  ? 135  ALA A C     1 
ATOM   931  O O     . ALA A 1 135  ? 169.658 193.045 180.615 1.00 34.50  ? 135  ALA A O     1 
ATOM   932  C CB    . ALA A 1 135  ? 167.545 191.066 180.020 1.00 33.62  ? 135  ALA A CB    1 
ATOM   933  N N     . ILE A 1 136  ? 168.048 194.504 180.044 1.00 39.86  ? 136  ILE A N     1 
ATOM   934  C CA    . ILE A 1 136  ? 168.988 195.530 179.608 1.00 43.48  ? 136  ILE A CA    1 
ATOM   935  C C     . ILE A 1 136  ? 169.405 196.369 180.807 1.00 47.28  ? 136  ILE A C     1 
ATOM   936  O O     . ILE A 1 136  ? 168.559 196.923 181.518 1.00 51.49  ? 136  ILE A O     1 
ATOM   937  C CB    . ILE A 1 136  ? 168.369 196.406 178.507 1.00 42.04  ? 136  ILE A CB    1 
ATOM   938  C CG1   . ILE A 1 136  ? 168.155 195.592 177.231 1.00 38.87  ? 136  ILE A CG1   1 
ATOM   939  C CG2   . ILE A 1 136  ? 169.249 197.611 178.225 1.00 47.02  ? 136  ILE A CG2   1 
ATOM   940  C CD1   . ILE A 1 136  ? 169.429 195.080 176.612 1.00 43.28  ? 136  ILE A CD1   1 
ATOM   941  N N     . LEU A 1 137  ? 170.709 196.465 181.034 1.00 46.19  ? 137  LEU A N     1 
ATOM   942  C CA    . LEU A 1 137  ? 171.245 197.268 182.120 1.00 45.31  ? 137  LEU A CA    1 
ATOM   943  C C     . LEU A 1 137  ? 171.496 198.699 181.656 1.00 52.89  ? 137  LEU A C     1 
ATOM   944  O O     . LEU A 1 137  ? 171.356 199.038 180.480 1.00 61.85  ? 137  LEU A O     1 
ATOM   945  C CB    . LEU A 1 137  ? 172.538 196.652 182.651 1.00 47.91  ? 137  LEU A CB    1 
ATOM   946  C CG    . LEU A 1 137  ? 172.467 195.199 183.113 1.00 45.35  ? 137  LEU A CG    1 
ATOM   947  C CD1   . LEU A 1 137  ? 173.861 194.668 183.375 1.00 44.17  ? 137  LEU A CD1   1 
ATOM   948  C CD2   . LEU A 1 137  ? 171.603 195.076 184.354 1.00 47.81  ? 137  LEU A CD2   1 
ATOM   949  N N     . THR A 1 138  ? 171.865 199.550 182.613 1.00 57.15  ? 138  THR A N     1 
ATOM   950  C CA    . THR A 1 138  ? 172.286 200.919 182.317 1.00 62.53  ? 138  THR A CA    1 
ATOM   951  C C     . THR A 1 138  ? 173.223 201.340 183.444 1.00 66.52  ? 138  THR A C     1 
ATOM   952  O O     . THR A 1 138  ? 172.763 201.740 184.517 1.00 66.39  ? 138  THR A O     1 
ATOM   953  C CB    . THR A 1 138  ? 171.095 201.862 182.199 1.00 62.14  ? 138  THR A CB    1 
ATOM   954  O OG1   . THR A 1 138  ? 170.193 201.378 181.195 1.00 64.21  ? 138  THR A OG1   1 
ATOM   955  C CG2   . THR A 1 138  ? 171.559 203.262 181.824 1.00 62.13  ? 138  THR A CG2   1 
ATOM   956  N N     . HIS A 1 139  ? 174.529 201.247 183.197 1.00 70.21  ? 139  HIS A N     1 
ATOM   957  C CA    . HIS A 1 139  ? 175.515 201.557 184.226 1.00 76.87  ? 139  HIS A CA    1 
ATOM   958  C C     . HIS A 1 139  ? 175.755 203.060 184.333 1.00 80.50  ? 139  HIS A C     1 
ATOM   959  O O     . HIS A 1 139  ? 175.461 203.672 185.365 1.00 79.75  ? 139  HIS A O     1 
ATOM   960  C CB    . HIS A 1 139  ? 176.826 200.819 183.929 1.00 74.65  ? 139  HIS A CB    1 
ATOM   961  C CG    . HIS A 1 139  ? 177.862 200.965 185.001 1.00 76.84  ? 139  HIS A CG    1 
ATOM   962  N ND1   . HIS A 1 139  ? 179.155 200.515 184.849 1.00 79.53  ? 139  HIS A ND1   1 
ATOM   963  C CD2   . HIS A 1 139  ? 177.795 201.504 186.241 1.00 77.25  ? 139  HIS A CD2   1 
ATOM   964  C CE1   . HIS A 1 139  ? 179.841 200.772 185.948 1.00 81.62  ? 139  HIS A CE1   1 
ATOM   965  N NE2   . HIS A 1 139  ? 179.039 201.374 186.808 1.00 83.46  ? 139  HIS A NE2   1 
ATOM   966  N N     . ASP A 1 140  ? 176.284 203.668 183.271 1.00 81.39  ? 140  ASP A N     1 
ATOM   967  C CA    . ASP A 1 140  ? 176.512 205.113 183.242 1.00 83.80  ? 140  ASP A CA    1 
ATOM   968  C C     . ASP A 1 140  ? 176.422 205.559 181.781 1.00 82.85  ? 140  ASP A C     1 
ATOM   969  O O     . ASP A 1 140  ? 177.410 205.516 181.046 1.00 81.80  ? 140  ASP A O     1 
ATOM   970  C CB    . ASP A 1 140  ? 177.851 205.477 183.868 1.00 82.91  ? 140  ASP A CB    1 
ATOM   971  C CG    . ASP A 1 140  ? 178.976 204.570 183.407 1.00 84.56  ? 140  ASP A CG    1 
ATOM   972  O OD1   . ASP A 1 140  ? 178.698 203.404 183.059 1.00 81.76  ? 140  ASP A OD1   1 
ATOM   973  O OD2   . ASP A 1 140  ? 180.139 205.025 183.394 1.00 85.54  ? 140  ASP A OD2   1 
ATOM   974  N N     . ASN A 1 141  ? 175.223 205.987 181.379 1.00 80.58  ? 141  ASN A N     1 
ATOM   975  C CA    . ASN A 1 141  ? 174.952 206.418 180.005 1.00 80.88  ? 141  ASN A CA    1 
ATOM   976  C C     . ASN A 1 141  ? 175.397 205.371 178.986 1.00 80.60  ? 141  ASN A C     1 
ATOM   977  O O     . ASN A 1 141  ? 175.729 205.695 177.844 1.00 79.75  ? 141  ASN A O     1 
ATOM   978  C CB    . ASN A 1 141  ? 175.608 207.769 179.712 1.00 83.30  ? 141  ASN A CB    1 
ATOM   979  C CG    . ASN A 1 141  ? 175.067 208.880 180.589 1.00 86.88  ? 141  ASN A CG    1 
ATOM   980  O OD1   . ASN A 1 141  ? 173.892 208.879 180.957 1.00 82.32  ? 141  ASN A OD1   1 
ATOM   981  N ND2   . ASN A 1 141  ? 175.924 209.835 180.931 1.00 87.26  ? 141  ASN A ND2   1 
ATOM   982  N N     . GLN A 1 142  ? 175.408 204.105 179.397 1.00 77.76  ? 142  GLN A N     1 
ATOM   983  C CA    . GLN A 1 142  ? 175.830 203.007 178.540 1.00 75.87  ? 142  GLN A CA    1 
ATOM   984  C C     . GLN A 1 142  ? 175.015 201.772 178.885 1.00 69.10  ? 142  GLN A C     1 
ATOM   985  O O     . GLN A 1 142  ? 175.105 201.262 180.005 1.00 70.14  ? 142  GLN A O     1 
ATOM   986  C CB    . GLN A 1 142  ? 177.328 202.720 178.704 1.00 70.66  ? 142  GLN A CB    1 
ATOM   987  C CG    . GLN A 1 142  ? 177.814 201.468 177.992 1.00 69.44  ? 142  GLN A CG    1 
ATOM   988  C CD    . GLN A 1 142  ? 177.795 201.597 176.481 1.00 77.28  ? 142  GLN A CD    1 
ATOM   989  O OE1   . GLN A 1 142  ? 177.651 202.692 175.939 1.00 81.17  ? 142  GLN A OE1   1 
ATOM   990  N NE2   . GLN A 1 142  ? 177.943 200.471 175.792 1.00 71.79  ? 142  GLN A NE2   1 
ATOM   991  N N     . GLN A 1 143  ? 174.229 201.295 177.925 1.00 61.85  ? 143  GLN A N     1 
ATOM   992  C CA    . GLN A 1 143  ? 173.379 200.132 178.133 1.00 57.33  ? 143  GLN A CA    1 
ATOM   993  C C     . GLN A 1 143  ? 174.186 198.852 177.973 1.00 54.68  ? 143  GLN A C     1 
ATOM   994  O O     . GLN A 1 143  ? 174.990 198.720 177.047 1.00 52.90  ? 143  GLN A O     1 
ATOM   995  C CB    . GLN A 1 143  ? 172.205 200.134 177.153 1.00 62.17  ? 143  GLN A CB    1 
ATOM   996  C CG    . GLN A 1 143  ? 171.254 201.306 177.317 1.00 63.17  ? 143  GLN A CG    1 
ATOM   997  C CD    . GLN A 1 143  ? 170.095 201.254 176.342 1.00 74.07  ? 143  GLN A CD    1 
ATOM   998  O OE1   . GLN A 1 143  ? 169.979 200.322 175.546 1.00 75.48  ? 143  GLN A OE1   1 
ATOM   999  N NE2   . GLN A 1 143  ? 169.229 202.258 176.399 1.00 73.18  ? 143  GLN A NE2   1 
ATOM   1000 N N     . TYR A 1 144  ? 173.963 197.911 178.886 1.00 51.93  ? 144  TYR A N     1 
ATOM   1001 C CA    . TYR A 1 144  ? 174.592 196.600 178.849 1.00 48.15  ? 144  TYR A CA    1 
ATOM   1002 C C     . TYR A 1 144  ? 173.512 195.529 178.822 1.00 44.02  ? 144  TYR A C     1 
ATOM   1003 O O     . TYR A 1 144  ? 172.314 195.819 178.842 1.00 44.91  ? 144  TYR A O     1 
ATOM   1004 C CB    . TYR A 1 144  ? 175.518 196.380 180.052 1.00 48.10  ? 144  TYR A CB    1 
ATOM   1005 C CG    . TYR A 1 144  ? 176.821 197.142 179.987 1.00 51.37  ? 144  TYR A CG    1 
ATOM   1006 C CD1   . TYR A 1 144  ? 177.911 196.629 179.300 1.00 49.17  ? 144  TYR A CD1   1 
ATOM   1007 C CD2   . TYR A 1 144  ? 176.964 198.368 180.622 1.00 56.41  ? 144  TYR A CD2   1 
ATOM   1008 C CE1   . TYR A 1 144  ? 179.105 197.317 179.241 1.00 57.50  ? 144  TYR A CE1   1 
ATOM   1009 C CE2   . TYR A 1 144  ? 178.154 199.063 180.569 1.00 58.66  ? 144  TYR A CE2   1 
ATOM   1010 C CZ    . TYR A 1 144  ? 179.222 198.533 179.877 1.00 62.32  ? 144  TYR A CZ    1 
ATOM   1011 O OH    . TYR A 1 144  ? 180.410 199.222 179.821 1.00 62.94  ? 144  TYR A OH    1 
ATOM   1012 N N     . LEU A 1 145  ? 173.949 194.276 178.776 1.00 40.37  ? 145  LEU A N     1 
ATOM   1013 C CA    . LEU A 1 145  ? 173.051 193.134 178.797 1.00 41.14  ? 145  LEU A CA    1 
ATOM   1014 C C     . LEU A 1 145  ? 173.397 192.218 179.962 1.00 42.85  ? 145  LEU A C     1 
ATOM   1015 O O     . LEU A 1 145  ? 174.568 192.032 180.303 1.00 46.73  ? 145  LEU A O     1 
ATOM   1016 C CB    . LEU A 1 145  ? 173.125 192.347 177.485 1.00 39.10  ? 145  LEU A CB    1 
ATOM   1017 C CG    . LEU A 1 145  ? 171.810 192.099 176.746 1.00 34.78  ? 145  LEU A CG    1 
ATOM   1018 C CD1   . LEU A 1 145  ? 172.006 191.065 175.657 1.00 35.80  ? 145  LEU A CD1   1 
ATOM   1019 C CD2   . LEU A 1 145  ? 170.717 191.667 177.701 1.00 39.34  ? 145  LEU A CD2   1 
ATOM   1020 N N     . LEU A 1 146  ? 172.363 191.646 180.571 1.00 34.99  ? 146  LEU A N     1 
ATOM   1021 C CA    . LEU A 1 146  ? 172.556 190.620 181.582 1.00 33.87  ? 146  LEU A CA    1 
ATOM   1022 C C     . LEU A 1 146  ? 172.847 189.283 180.917 1.00 36.94  ? 146  LEU A C     1 
ATOM   1023 O O     . LEU A 1 146  ? 172.284 188.961 179.868 1.00 36.68  ? 146  LEU A O     1 
ATOM   1024 C CB    . LEU A 1 146  ? 171.318 190.493 182.471 1.00 33.30  ? 146  LEU A CB    1 
ATOM   1025 C CG    . LEU A 1 146  ? 171.174 191.442 183.658 1.00 32.01  ? 146  LEU A CG    1 
ATOM   1026 C CD1   . LEU A 1 146  ? 169.850 191.199 184.358 1.00 32.35  ? 146  LEU A CD1   1 
ATOM   1027 C CD2   . LEU A 1 146  ? 172.331 191.270 184.627 1.00 30.15  ? 146  LEU A CD2   1 
ATOM   1028 N N     . SER A 1 147  ? 173.732 188.506 181.534 1.00 35.21  ? 147  SER A N     1 
ATOM   1029 C CA    . SER A 1 147  ? 173.967 187.149 181.075 1.00 32.20  ? 147  SER A CA    1 
ATOM   1030 C C     . SER A 1 147  ? 172.680 186.338 181.176 1.00 36.39  ? 147  SER A C     1 
ATOM   1031 O O     . SER A 1 147  ? 171.778 186.648 181.957 1.00 38.50  ? 147  SER A O     1 
ATOM   1032 C CB    . SER A 1 147  ? 175.072 186.486 181.895 1.00 35.75  ? 147  SER A CB    1 
ATOM   1033 O OG    . SER A 1 147  ? 176.256 187.262 181.878 1.00 42.28  ? 147  SER A OG    1 
ATOM   1034 N N     . ARG A 1 148  ? 172.595 185.289 180.358 1.00 35.95  ? 148  ARG A N     1 
ATOM   1035 C CA    . ARG A 1 148  ? 171.409 184.440 180.390 1.00 34.95  ? 148  ARG A CA    1 
ATOM   1036 C C     . ARG A 1 148  ? 171.243 183.794 181.758 1.00 36.11  ? 148  ARG A C     1 
ATOM   1037 O O     . ARG A 1 148  ? 170.125 183.693 182.276 1.00 38.29  ? 148  ARG A O     1 
ATOM   1038 C CB    . ARG A 1 148  ? 171.492 183.378 179.295 1.00 34.99  ? 148  ARG A CB    1 
ATOM   1039 C CG    . ARG A 1 148  ? 170.179 182.677 179.031 1.00 41.85  ? 148  ARG A CG    1 
ATOM   1040 C CD    . ARG A 1 148  ? 170.273 181.729 177.854 1.00 46.64  ? 148  ARG A CD    1 
ATOM   1041 N NE    . ARG A 1 148  ? 168.949 181.356 177.373 1.00 54.86  ? 148  ARG A NE    1 
ATOM   1042 C CZ    . ARG A 1 148  ? 168.719 180.504 176.384 1.00 55.72  ? 148  ARG A CZ    1 
ATOM   1043 N NH1   . ARG A 1 148  ? 169.708 179.896 175.751 1.00 51.04  ? 148  ARG A NH1   1 
ATOM   1044 N NH2   . ARG A 1 148  ? 167.464 180.253 176.022 1.00 54.62  ? 148  ARG A NH2   1 
ATOM   1045 N N     . GLU A 1 149  ? 172.351 183.365 182.365 1.00 36.74  ? 149  GLU A N     1 
ATOM   1046 C CA    . GLU A 1 149  ? 172.292 182.778 183.698 1.00 33.02  ? 149  GLU A CA    1 
ATOM   1047 C C     . GLU A 1 149  ? 171.914 183.817 184.746 1.00 34.17  ? 149  GLU A C     1 
ATOM   1048 O O     . GLU A 1 149  ? 171.090 183.547 185.627 1.00 38.96  ? 149  GLU A O     1 
ATOM   1049 C CB    . GLU A 1 149  ? 173.633 182.129 184.038 1.00 36.65  ? 149  GLU A CB    1 
ATOM   1050 C CG    . GLU A 1 149  ? 174.131 181.136 182.995 1.00 42.24  ? 149  GLU A CG    1 
ATOM   1051 C CD    . GLU A 1 149  ? 174.867 181.806 181.850 1.00 45.38  ? 149  GLU A CD    1 
ATOM   1052 O OE1   . GLU A 1 149  ? 175.364 182.935 182.043 1.00 43.42  ? 149  GLU A OE1   1 
ATOM   1053 O OE2   . GLU A 1 149  ? 174.943 181.208 180.756 1.00 42.42  ? 149  GLU A OE2   1 
ATOM   1054 N N     . ASN A 1 150  ? 172.503 185.013 184.669 1.00 31.00  ? 150  ASN A N     1 
ATOM   1055 C CA    . ASN A 1 150  ? 172.142 186.073 185.605 1.00 31.31  ? 150  ASN A CA    1 
ATOM   1056 C C     . ASN A 1 150  ? 170.694 186.507 185.419 1.00 31.59  ? 150  ASN A C     1 
ATOM   1057 O O     . ASN A 1 150  ? 169.990 186.775 186.401 1.00 36.49  ? 150  ASN A O     1 
ATOM   1058 C CB    . ASN A 1 150  ? 173.086 187.263 185.444 1.00 28.43  ? 150  ASN A CB    1 
ATOM   1059 C CG    . ASN A 1 150  ? 174.450 187.007 186.044 1.00 34.17  ? 150  ASN A CG    1 
ATOM   1060 O OD1   . ASN A 1 150  ? 174.583 186.265 187.017 1.00 43.61  ? 150  ASN A OD1   1 
ATOM   1061 N ND2   . ASN A 1 150  ? 175.475 187.622 185.470 1.00 43.95  ? 150  ASN A ND2   1 
ATOM   1062 N N     . TRP A 1 151  ? 170.233 186.590 184.169 1.00 31.48  ? 151  TRP A N     1 
ATOM   1063 C CA    . TRP A 1 151  ? 168.835 186.929 183.923 1.00 32.96  ? 151  TRP A CA    1 
ATOM   1064 C C     . TRP A 1 151  ? 167.903 185.860 184.478 1.00 34.06  ? 151  TRP A C     1 
ATOM   1065 O O     . TRP A 1 151  ? 166.855 186.180 185.048 1.00 35.19  ? 151  TRP A O     1 
ATOM   1066 C CB    . TRP A 1 151  ? 168.588 187.133 182.428 1.00 32.83  ? 151  TRP A CB    1 
ATOM   1067 C CG    . TRP A 1 151  ? 167.131 187.253 182.083 1.00 33.05  ? 151  TRP A CG    1 
ATOM   1068 C CD1   . TRP A 1 151  ? 166.389 186.380 181.342 1.00 34.05  ? 151  TRP A CD1   1 
ATOM   1069 C CD2   . TRP A 1 151  ? 166.238 188.298 182.482 1.00 31.63  ? 151  TRP A CD2   1 
ATOM   1070 N NE1   . TRP A 1 151  ? 165.093 186.823 181.247 1.00 29.81  ? 151  TRP A NE1   1 
ATOM   1071 C CE2   . TRP A 1 151  ? 164.975 187.998 181.940 1.00 30.67  ? 151  TRP A CE2   1 
ATOM   1072 C CE3   . TRP A 1 151  ? 166.386 189.461 183.243 1.00 31.67  ? 151  TRP A CE3   1 
ATOM   1073 C CZ2   . TRP A 1 151  ? 163.868 188.817 182.136 1.00 33.84  ? 151  TRP A CZ2   1 
ATOM   1074 C CZ3   . TRP A 1 151  ? 165.286 190.271 183.435 1.00 32.98  ? 151  TRP A CZ3   1 
ATOM   1075 C CH2   . TRP A 1 151  ? 164.044 189.947 182.884 1.00 34.62  ? 151  TRP A CH2   1 
ATOM   1076 N N     . ALA A 1 152  ? 168.263 184.584 184.318 1.00 32.66  ? 152  ALA A N     1 
ATOM   1077 C CA    . ALA A 1 152  ? 167.451 183.513 184.885 1.00 31.53  ? 152  ALA A CA    1 
ATOM   1078 C C     . ALA A 1 152  ? 167.429 183.572 186.406 1.00 35.24  ? 152  ALA A C     1 
ATOM   1079 O O     . ALA A 1 152  ? 166.388 183.321 187.022 1.00 39.74  ? 152  ALA A O     1 
ATOM   1080 C CB    . ALA A 1 152  ? 167.967 182.155 184.412 1.00 31.74  ? 152  ALA A CB    1 
ATOM   1081 N N     . LEU A 1 153  ? 168.565 183.893 187.028 1.00 32.23  ? 153  LEU A N     1 
ATOM   1082 C CA    . LEU A 1 153  ? 168.606 184.035 188.481 1.00 34.20  ? 153  LEU A CA    1 
ATOM   1083 C C     . LEU A 1 153  ? 167.713 185.178 188.950 1.00 36.80  ? 153  LEU A C     1 
ATOM   1084 O O     . LEU A 1 153  ? 166.969 185.041 189.931 1.00 40.35  ? 153  LEU A O     1 
ATOM   1085 C CB    . LEU A 1 153  ? 170.048 184.250 188.940 1.00 32.35  ? 153  LEU A CB    1 
ATOM   1086 C CG    . LEU A 1 153  ? 170.262 184.549 190.423 1.00 31.28  ? 153  LEU A CG    1 
ATOM   1087 C CD1   . LEU A 1 153  ? 169.723 183.421 191.285 1.00 29.90  ? 153  LEU A CD1   1 
ATOM   1088 C CD2   . LEU A 1 153  ? 171.732 184.782 190.701 1.00 34.16  ? 153  LEU A CD2   1 
ATOM   1089 N N     . LEU A 1 154  ? 167.780 186.320 188.261 1.00 33.87  ? 154  LEU A N     1 
ATOM   1090 C CA    . LEU A 1 154  ? 166.911 187.442 188.604 1.00 30.98  ? 154  LEU A CA    1 
ATOM   1091 C C     . LEU A 1 154  ? 165.445 187.077 188.417 1.00 35.35  ? 154  LEU A C     1 
ATOM   1092 O O     . LEU A 1 154  ? 164.595 187.448 189.234 1.00 42.54  ? 154  LEU A O     1 
ATOM   1093 C CB    . LEU A 1 154  ? 167.272 188.664 187.761 1.00 35.45  ? 154  LEU A CB    1 
ATOM   1094 C CG    . LEU A 1 154  ? 167.807 189.866 188.539 1.00 42.20  ? 154  LEU A CG    1 
ATOM   1095 C CD1   . LEU A 1 154  ? 168.161 190.997 187.599 1.00 36.07  ? 154  LEU A CD1   1 
ATOM   1096 C CD2   . LEU A 1 154  ? 166.793 190.325 189.573 1.00 44.92  ? 154  LEU A CD2   1 
ATOM   1097 N N     . GLN A 1 155  ? 165.132 186.352 187.341 1.00 31.85  ? 155  GLN A N     1 
ATOM   1098 C CA    . GLN A 1 155  ? 163.766 185.899 187.115 1.00 33.77  ? 155  GLN A CA    1 
ATOM   1099 C C     . GLN A 1 155  ? 163.293 184.994 188.243 1.00 35.27  ? 155  GLN A C     1 
ATOM   1100 O O     . GLN A 1 155  ? 162.155 185.113 188.704 1.00 38.83  ? 155  GLN A O     1 
ATOM   1101 C CB    . GLN A 1 155  ? 163.673 185.170 185.775 1.00 33.18  ? 155  GLN A CB    1 
ATOM   1102 C CG    . GLN A 1 155  ? 163.647 186.081 184.567 1.00 33.77  ? 155  GLN A CG    1 
ATOM   1103 C CD    . GLN A 1 155  ? 162.258 186.598 184.261 1.00 42.28  ? 155  GLN A CD    1 
ATOM   1104 O OE1   . GLN A 1 155  ? 161.526 186.007 183.468 1.00 43.34  ? 155  GLN A OE1   1 
ATOM   1105 N NE2   . GLN A 1 155  ? 161.886 187.707 184.889 1.00 38.43  ? 155  GLN A NE2   1 
ATOM   1106 N N     . ALA A 1 156  ? 164.153 184.081 188.697 1.00 36.58  ? 156  ALA A N     1 
ATOM   1107 C CA    . ALA A 1 156  ? 163.780 183.186 189.788 1.00 32.06  ? 156  ALA A CA    1 
ATOM   1108 C C     . ALA A 1 156  ? 163.539 183.953 191.083 1.00 33.51  ? 156  ALA A C     1 
ATOM   1109 O O     . ALA A 1 156  ? 162.570 183.679 191.801 1.00 34.81  ? 156  ALA A O     1 
ATOM   1110 C CB    . ALA A 1 156  ? 164.858 182.123 189.987 1.00 30.87  ? 156  ALA A CB    1 
ATOM   1111 N N     . THR A 1 157  ? 164.410 184.915 191.401 1.00 33.43  ? 157  THR A N     1 
ATOM   1112 C CA    . THR A 1 157  ? 164.215 185.696 192.622 1.00 33.62  ? 157  THR A CA    1 
ATOM   1113 C C     . THR A 1 157  ? 162.933 186.519 192.556 1.00 40.34  ? 157  THR A C     1 
ATOM   1114 O O     . THR A 1 157  ? 162.162 186.563 193.525 1.00 44.40  ? 157  THR A O     1 
ATOM   1115 C CB    . THR A 1 157  ? 165.418 186.605 192.875 1.00 28.39  ? 157  THR A CB    1 
ATOM   1116 O OG1   . THR A 1 157  ? 165.605 187.478 191.756 1.00 41.95  ? 157  THR A OG1   1 
ATOM   1117 C CG2   . THR A 1 157  ? 166.673 185.782 193.088 1.00 28.59  ? 157  THR A CG2   1 
ATOM   1118 N N     . GLU A 1 158  ? 162.679 187.166 191.416 1.00 41.38  ? 158  GLU A N     1 
ATOM   1119 C CA    . GLU A 1 158  ? 161.462 187.956 191.271 1.00 43.94  ? 158  GLU A CA    1 
ATOM   1120 C C     . GLU A 1 158  ? 160.222 187.072 191.300 1.00 43.58  ? 158  GLU A C     1 
ATOM   1121 O O     . GLU A 1 158  ? 159.181 187.475 191.829 1.00 49.26  ? 158  GLU A O     1 
ATOM   1122 C CB    . GLU A 1 158  ? 161.519 188.772 189.981 1.00 47.51  ? 158  GLU A CB    1 
ATOM   1123 C CG    . GLU A 1 158  ? 162.585 189.857 189.991 1.00 49.59  ? 158  GLU A CG    1 
ATOM   1124 C CD    . GLU A 1 158  ? 162.666 190.611 188.680 1.00 59.31  ? 158  GLU A CD    1 
ATOM   1125 O OE1   . GLU A 1 158  ? 162.106 190.125 187.675 1.00 51.23  ? 158  GLU A OE1   1 
ATOM   1126 O OE2   . GLU A 1 158  ? 163.290 191.692 188.654 1.00 60.40  ? 158  GLU A OE2   1 
ATOM   1127 N N     . GLN A 1 159  ? 160.313 185.861 190.746 1.00 43.64  ? 159  GLN A N     1 
ATOM   1128 C CA    . GLN A 1 159  ? 159.181 184.943 190.784 1.00 41.77  ? 159  GLN A CA    1 
ATOM   1129 C C     . GLN A 1 159  ? 158.904 184.467 192.203 1.00 44.92  ? 159  GLN A C     1 
ATOM   1130 O O     . GLN A 1 159  ? 157.742 184.331 192.597 1.00 52.43  ? 159  GLN A O     1 
ATOM   1131 C CB    . GLN A 1 159  ? 159.437 183.757 189.856 1.00 37.94  ? 159  GLN A CB    1 
ATOM   1132 C CG    . GLN A 1 159  ? 158.290 182.770 189.783 1.00 39.68  ? 159  GLN A CG    1 
ATOM   1133 C CD    . GLN A 1 159  ? 158.503 181.712 188.722 1.00 49.89  ? 159  GLN A CD    1 
ATOM   1134 O OE1   . GLN A 1 159  ? 159.439 181.794 187.927 1.00 50.54  ? 159  GLN A OE1   1 
ATOM   1135 N NE2   . GLN A 1 159  ? 157.633 180.709 188.702 1.00 50.88  ? 159  GLN A NE2   1 
ATOM   1136 N N     . LEU A 1 160  ? 159.954 184.210 192.988 1.00 45.91  ? 160  LEU A N     1 
ATOM   1137 C CA    . LEU A 1 160  ? 159.741 183.874 194.392 1.00 45.37  ? 160  LEU A CA    1 
ATOM   1138 C C     . LEU A 1 160  ? 159.092 185.032 195.137 1.00 53.31  ? 160  LEU A C     1 
ATOM   1139 O O     . LEU A 1 160  ? 158.168 184.829 195.934 1.00 61.71  ? 160  LEU A O     1 
ATOM   1140 C CB    . LEU A 1 160  ? 161.058 183.487 195.064 1.00 40.70  ? 160  LEU A CB    1 
ATOM   1141 C CG    . LEU A 1 160  ? 160.925 183.248 196.573 1.00 43.39  ? 160  LEU A CG    1 
ATOM   1142 C CD1   . LEU A 1 160  ? 159.990 182.083 196.853 1.00 43.63  ? 160  LEU A CD1   1 
ATOM   1143 C CD2   . LEU A 1 160  ? 162.271 183.027 197.241 1.00 46.14  ? 160  LEU A CD2   1 
ATOM   1144 N N     . SER A 1 161  ? 159.557 186.257 194.882 1.00 52.73  ? 161  SER A N     1 
ATOM   1145 C CA    . SER A 1 161  ? 158.965 187.418 195.540 1.00 53.31  ? 161  SER A CA    1 
ATOM   1146 C C     . SER A 1 161  ? 157.498 187.584 195.158 1.00 56.88  ? 161  SER A C     1 
ATOM   1147 O O     . SER A 1 161  ? 156.664 187.925 196.004 1.00 65.43  ? 161  SER A O     1 
ATOM   1148 C CB    . SER A 1 161  ? 159.757 188.677 195.195 1.00 54.91  ? 161  SER A CB    1 
ATOM   1149 O OG    . SER A 1 161  ? 161.101 188.565 195.623 1.00 53.56  ? 161  SER A OG    1 
ATOM   1150 N N     . ALA A 1 162  ? 157.165 187.348 193.888 1.00 55.69  ? 162  ALA A N     1 
ATOM   1151 C CA    . ALA A 1 162  ? 155.779 187.474 193.447 1.00 60.38  ? 162  ALA A CA    1 
ATOM   1152 C C     . ALA A 1 162  ? 154.909 186.357 194.010 1.00 65.31  ? 162  ALA A C     1 
ATOM   1153 O O     . ALA A 1 162  ? 153.734 186.577 194.322 1.00 74.55  ? 162  ALA A O     1 
ATOM   1154 C CB    . ALA A 1 162  ? 155.711 187.487 191.921 1.00 55.92  ? 162  ALA A CB    1 
ATOM   1155 N N     . GLN A 1 163  ? 155.460 185.151 194.137 1.00 61.02  ? 163  GLN A N     1 
ATOM   1156 C CA    . GLN A 1 163  ? 154.687 184.028 194.650 1.00 64.21  ? 163  GLN A CA    1 
ATOM   1157 C C     . GLN A 1 163  ? 154.482 184.114 196.156 1.00 66.36  ? 163  GLN A C     1 
ATOM   1158 O O     . GLN A 1 163  ? 153.477 183.613 196.670 1.00 73.47  ? 163  GLN A O     1 
ATOM   1159 C CB    . GLN A 1 163  ? 155.380 182.713 194.285 1.00 65.72  ? 163  GLN A CB    1 
ATOM   1160 C CG    . GLN A 1 163  ? 154.580 181.465 194.611 1.00 70.01  ? 163  GLN A CG    1 
ATOM   1161 C CD    . GLN A 1 163  ? 153.380 181.289 193.707 1.00 75.81  ? 163  GLN A CD    1 
ATOM   1162 O OE1   . GLN A 1 163  ? 153.355 181.790 192.584 1.00 73.15  ? 163  GLN A OE1   1 
ATOM   1163 N NE2   . GLN A 1 163  ? 152.373 180.574 194.195 1.00 80.15  ? 163  GLN A NE2   1 
ATOM   1164 N N     . GLN A 1 164  ? 155.412 184.744 196.877 1.00 62.81  ? 164  GLN A N     1 
ATOM   1165 C CA    . GLN A 1 164  ? 155.291 184.814 198.329 1.00 68.20  ? 164  GLN A CA    1 
ATOM   1166 C C     . GLN A 1 164  ? 154.142 185.720 198.755 1.00 74.73  ? 164  GLN A C     1 
ATOM   1167 O O     . GLN A 1 164  ? 153.437 185.420 199.724 1.00 79.19  ? 164  GLN A O     1 
ATOM   1168 C CB    . GLN A 1 164  ? 156.608 185.281 198.944 1.00 60.23  ? 164  GLN A CB    1 
ATOM   1169 C CG    . GLN A 1 164  ? 157.655 184.190 199.021 1.00 58.46  ? 164  GLN A CG    1 
ATOM   1170 C CD    . GLN A 1 164  ? 158.934 184.661 199.666 1.00 55.98  ? 164  GLN A CD    1 
ATOM   1171 O OE1   . GLN A 1 164  ? 159.268 185.842 199.615 1.00 62.35  ? 164  GLN A OE1   1 
ATOM   1172 N NE2   . GLN A 1 164  ? 159.655 183.738 200.290 1.00 56.48  ? 164  GLN A NE2   1 
ATOM   1173 N N     . ILE A 1 165  ? 153.936 186.835 198.049 1.00 74.01  ? 165  ILE A N     1 
ATOM   1174 C CA    . ILE A 1 165  ? 152.831 187.726 198.381 1.00 75.56  ? 165  ILE A CA    1 
ATOM   1175 C C     . ILE A 1 165  ? 151.480 187.149 197.990 1.00 76.38  ? 165  ILE A C     1 
ATOM   1176 O O     . ILE A 1 165  ? 150.444 187.719 198.353 1.00 75.29  ? 165  ILE A O     1 
ATOM   1177 C CB    . ILE A 1 165  ? 153.020 189.107 197.722 1.00 72.33  ? 165  ILE A CB    1 
ATOM   1178 C CG1   . ILE A 1 165  ? 153.058 188.976 196.201 1.00 70.68  ? 165  ILE A CG1   1 
ATOM   1179 C CG2   . ILE A 1 165  ? 154.289 189.768 198.231 1.00 70.79  ? 165  ILE A CG2   1 
ATOM   1180 C CD1   . ILE A 1 165  ? 153.269 190.288 195.481 1.00 72.18  ? 165  ILE A CD1   1 
ATOM   1181 N N     . GLN A 1 166  ? 151.462 186.034 197.260 1.00 74.97  ? 166  GLN A N     1 
ATOM   1182 C CA    . GLN A 1 166  ? 150.224 185.364 196.877 1.00 77.98  ? 166  GLN A CA    1 
ATOM   1183 C C     . GLN A 1 166  ? 149.910 184.186 197.795 1.00 83.25  ? 166  GLN A C     1 
ATOM   1184 O O     . GLN A 1 166  ? 148.828 184.123 198.385 1.00 84.71  ? 166  GLN A O     1 
ATOM   1185 C CB    . GLN A 1 166  ? 150.311 184.894 195.420 1.00 71.24  ? 166  GLN A CB    1 
ATOM   1186 C CG    . GLN A 1 166  ? 150.563 186.007 194.422 1.00 75.37  ? 166  GLN A CG    1 
ATOM   1187 C CD    . GLN A 1 166  ? 150.805 185.484 193.021 1.00 80.25  ? 166  GLN A CD    1 
ATOM   1188 O OE1   . GLN A 1 166  ? 150.631 184.296 192.752 1.00 76.99  ? 166  GLN A OE1   1 
ATOM   1189 N NE2   . GLN A 1 166  ? 151.214 186.370 192.120 1.00 76.41  ? 166  GLN A NE2   1 
ATOM   1190 N N     . THR A 1 167  ? 150.845 183.245 197.924 1.00 82.21  ? 167  THR A N     1 
ATOM   1191 C CA    . THR A 1 167  ? 150.672 182.053 198.754 1.00 81.04  ? 167  THR A CA    1 
ATOM   1192 C C     . THR A 1 167  ? 151.902 181.884 199.636 1.00 79.02  ? 167  THR A C     1 
ATOM   1193 O O     . THR A 1 167  ? 152.760 181.032 199.369 1.00 78.57  ? 167  THR A O     1 
ATOM   1194 C CB    . THR A 1 167  ? 150.442 180.810 197.893 1.00 80.41  ? 167  THR A CB    1 
ATOM   1195 O OG1   . THR A 1 167  ? 149.461 181.099 196.890 1.00 83.31  ? 167  THR A OG1   1 
ATOM   1196 C CG2   . THR A 1 167  ? 149.951 179.650 198.750 1.00 78.56  ? 167  THR A CG2   1 
ATOM   1197 N N     . PRO A 1 168  ? 152.030 182.687 200.690 1.00 79.73  ? 168  PRO A N     1 
ATOM   1198 C CA    . PRO A 1 168  ? 153.168 182.523 201.600 1.00 78.01  ? 168  PRO A CA    1 
ATOM   1199 C C     . PRO A 1 168  ? 153.087 181.207 202.355 1.00 78.67  ? 168  PRO A C     1 
ATOM   1200 O O     . PRO A 1 168  ? 152.003 180.706 202.664 1.00 83.78  ? 168  PRO A O     1 
ATOM   1201 C CB    . PRO A 1 168  ? 153.038 183.719 202.548 1.00 78.71  ? 168  PRO A CB    1 
ATOM   1202 C CG    . PRO A 1 168  ? 151.583 184.035 202.541 1.00 72.85  ? 168  PRO A CG    1 
ATOM   1203 C CD    . PRO A 1 168  ? 151.102 183.736 201.148 1.00 76.69  ? 168  PRO A CD    1 
ATOM   1204 N N     . GLY A 1 169  ? 154.251 180.647 202.650 1.00 75.61  ? 169  GLY A N     1 
ATOM   1205 C CA    . GLY A 1 169  ? 154.309 179.407 203.393 1.00 70.31  ? 169  GLY A CA    1 
ATOM   1206 C C     . GLY A 1 169  ? 155.620 178.683 203.156 1.00 66.18  ? 169  GLY A C     1 
ATOM   1207 O O     . GLY A 1 169  ? 156.525 179.190 202.496 1.00 69.54  ? 169  GLY A O     1 
ATOM   1208 N N     . GLU A 1 170  ? 155.689 177.475 203.718 1.00 64.45  ? 170  GLU A N     1 
ATOM   1209 C CA    . GLU A 1 170  ? 156.900 176.665 203.623 1.00 63.19  ? 170  GLU A CA    1 
ATOM   1210 C C     . GLU A 1 170  ? 157.124 176.160 202.202 1.00 61.63  ? 170  GLU A C     1 
ATOM   1211 O O     . GLU A 1 170  ? 158.241 176.236 201.675 1.00 63.20  ? 170  GLU A O     1 
ATOM   1212 C CB    . GLU A 1 170  ? 156.812 175.494 204.603 1.00 62.84  ? 170  GLU A CB    1 
ATOM   1213 C CG    . GLU A 1 170  ? 157.765 174.347 204.314 1.00 65.21  ? 170  GLU A CG    1 
ATOM   1214 C CD    . GLU A 1 170  ? 159.145 174.570 204.892 1.00 67.09  ? 170  GLU A CD    1 
ATOM   1215 O OE1   . GLU A 1 170  ? 159.418 175.690 205.366 1.00 68.16  ? 170  GLU A OE1   1 
ATOM   1216 O OE2   . GLU A 1 170  ? 159.957 173.622 204.882 1.00 65.97  ? 170  GLU A OE2   1 
ATOM   1217 N N     . THR A 1 171  ? 156.073 175.630 201.571 1.00 60.73  ? 171  THR A N     1 
ATOM   1218 C CA    . THR A 1 171  ? 156.217 175.040 200.243 1.00 61.08  ? 171  THR A CA    1 
ATOM   1219 C C     . THR A 1 171  ? 156.637 176.082 199.215 1.00 59.81  ? 171  THR A C     1 
ATOM   1220 O O     . THR A 1 171  ? 157.482 175.811 198.352 1.00 61.20  ? 171  THR A O     1 
ATOM   1221 C CB    . THR A 1 171  ? 154.906 174.373 199.824 1.00 62.94  ? 171  THR A CB    1 
ATOM   1222 O OG1   . THR A 1 171  ? 154.516 173.416 200.818 1.00 61.10  ? 171  THR A OG1   1 
ATOM   1223 C CG2   . THR A 1 171  ? 155.067 173.667 198.488 1.00 54.00  ? 171  THR A CG2   1 
ATOM   1224 N N     . THR A 1 172  ? 156.049 177.278 199.286 1.00 61.41  ? 172  THR A N     1 
ATOM   1225 C CA    . THR A 1 172  ? 156.416 178.344 198.361 1.00 58.33  ? 172  THR A CA    1 
ATOM   1226 C C     . THR A 1 172  ? 157.884 178.714 198.511 1.00 53.54  ? 172  THR A C     1 
ATOM   1227 O O     . THR A 1 172  ? 158.610 178.835 197.517 1.00 54.50  ? 172  THR A O     1 
ATOM   1228 C CB    . THR A 1 172  ? 155.527 179.566 198.593 1.00 61.81  ? 172  THR A CB    1 
ATOM   1229 O OG1   . THR A 1 172  ? 154.196 179.284 198.145 1.00 70.80  ? 172  THR A OG1   1 
ATOM   1230 C CG2   . THR A 1 172  ? 156.066 180.773 197.847 1.00 60.27  ? 172  THR A CG2   1 
ATOM   1231 N N     . ASN A 1 173  ? 158.343 178.883 199.753 1.00 50.01  ? 173  ASN A N     1 
ATOM   1232 C CA    . ASN A 1 173  ? 159.745 179.213 199.980 1.00 49.27  ? 173  ASN A CA    1 
ATOM   1233 C C     . ASN A 1 173  ? 160.658 178.115 199.457 1.00 49.63  ? 173  ASN A C     1 
ATOM   1234 O O     . ASN A 1 173  ? 161.659 178.397 198.788 1.00 52.85  ? 173  ASN A O     1 
ATOM   1235 C CB    . ASN A 1 173  ? 159.999 179.451 201.469 1.00 50.72  ? 173  ASN A CB    1 
ATOM   1236 C CG    . ASN A 1 173  ? 159.212 180.622 202.014 1.00 58.05  ? 173  ASN A CG    1 
ATOM   1237 O OD1   . ASN A 1 173  ? 158.888 181.560 201.288 1.00 62.06  ? 173  ASN A OD1   1 
ATOM   1238 N ND2   . ASN A 1 173  ? 158.903 180.575 203.304 1.00 64.19  ? 173  ASN A ND2   1 
ATOM   1239 N N     . GLN A 1 174  ? 160.315 176.854 199.729 1.00 46.44  ? 174  GLN A N     1 
ATOM   1240 C CA    . GLN A 1 174  ? 161.172 175.749 199.311 1.00 42.27  ? 174  GLN A CA    1 
ATOM   1241 C C     . GLN A 1 174  ? 161.265 175.660 197.793 1.00 41.67  ? 174  GLN A C     1 
ATOM   1242 O O     . GLN A 1 174  ? 162.364 175.556 197.242 1.00 42.27  ? 174  GLN A O     1 
ATOM   1243 C CB    . GLN A 1 174  ? 160.665 174.434 199.900 1.00 43.24  ? 174  GLN A CB    1 
ATOM   1244 C CG    . GLN A 1 174  ? 160.928 174.292 201.385 1.00 48.77  ? 174  GLN A CG    1 
ATOM   1245 C CD    . GLN A 1 174  ? 160.696 172.885 201.884 1.00 57.29  ? 174  GLN A CD    1 
ATOM   1246 O OE1   . GLN A 1 174  ? 160.184 172.034 201.158 1.00 61.54  ? 174  GLN A OE1   1 
ATOM   1247 N NE2   . GLN A 1 174  ? 161.076 172.629 203.128 1.00 61.74  ? 174  GLN A NE2   1 
ATOM   1248 N N     . LEU A 1 175  ? 160.127 175.717 197.097 1.00 40.69  ? 175  LEU A N     1 
ATOM   1249 C CA    . LEU A 1 175  ? 160.152 175.624 195.638 1.00 40.05  ? 175  LEU A CA    1 
ATOM   1250 C C     . LEU A 1 175  ? 160.861 176.824 195.017 1.00 37.22  ? 175  LEU A C     1 
ATOM   1251 O O     . LEU A 1 175  ? 161.714 176.672 194.127 1.00 35.24  ? 175  LEU A O     1 
ATOM   1252 C CB    . LEU A 1 175  ? 158.727 175.504 195.097 1.00 47.65  ? 175  LEU A CB    1 
ATOM   1253 C CG    . LEU A 1 175  ? 157.962 174.226 195.441 1.00 49.54  ? 175  LEU A CG    1 
ATOM   1254 C CD1   . LEU A 1 175  ? 156.546 174.287 194.895 1.00 52.21  ? 175  LEU A CD1   1 
ATOM   1255 C CD2   . LEU A 1 175  ? 158.690 173.013 194.899 1.00 41.12  ? 175  LEU A CD2   1 
ATOM   1256 N N     . GLY A 1 176  ? 160.519 178.029 195.477 1.00 39.15  ? 176  GLY A N     1 
ATOM   1257 C CA    . GLY A 1 176  ? 161.129 179.221 194.920 1.00 37.18  ? 176  GLY A CA    1 
ATOM   1258 C C     . GLY A 1 176  ? 162.630 179.241 195.111 1.00 33.74  ? 176  GLY A C     1 
ATOM   1259 O O     . GLY A 1 176  ? 163.380 179.543 194.182 1.00 34.59  ? 176  GLY A O     1 
ATOM   1260 N N     . TRP A 1 177  ? 163.097 178.890 196.310 1.00 34.94  ? 177  TRP A N     1 
ATOM   1261 C CA    . TRP A 1 177  ? 164.534 178.911 196.516 1.00 36.96  ? 177  TRP A CA    1 
ATOM   1262 C C     . TRP A 1 177  ? 165.232 177.687 195.942 1.00 37.69  ? 177  TRP A C     1 
ATOM   1263 O O     . TRP A 1 177  ? 166.436 177.751 195.703 1.00 39.49  ? 177  TRP A O     1 
ATOM   1264 C CB    . TRP A 1 177  ? 164.883 179.053 197.994 1.00 41.60  ? 177  TRP A CB    1 
ATOM   1265 C CG    . TRP A 1 177  ? 166.324 179.385 198.140 1.00 49.85  ? 177  TRP A CG    1 
ATOM   1266 C CD1   . TRP A 1 177  ? 166.923 180.575 197.849 1.00 49.41  ? 177  TRP A CD1   1 
ATOM   1267 C CD2   . TRP A 1 177  ? 167.366 178.503 198.556 1.00 43.82  ? 177  TRP A CD2   1 
ATOM   1268 N NE1   . TRP A 1 177  ? 168.272 180.494 198.078 1.00 44.21  ? 177  TRP A NE1   1 
ATOM   1269 C CE2   . TRP A 1 177  ? 168.570 179.231 198.513 1.00 44.12  ? 177  TRP A CE2   1 
ATOM   1270 C CE3   . TRP A 1 177  ? 167.396 177.171 198.971 1.00 38.31  ? 177  TRP A CE3   1 
ATOM   1271 C CZ2   . TRP A 1 177  ? 169.787 178.673 198.872 1.00 46.16  ? 177  TRP A CZ2   1 
ATOM   1272 C CZ3   . TRP A 1 177  ? 168.603 176.620 199.325 1.00 47.92  ? 177  TRP A CZ3   1 
ATOM   1273 C CH2   . TRP A 1 177  ? 169.783 177.369 199.275 1.00 49.71  ? 177  TRP A CH2   1 
ATOM   1274 N N     . ALA A 1 178  ? 164.518 176.595 195.670 1.00 35.83  ? 178  ALA A N     1 
ATOM   1275 C CA    . ALA A 1 178  ? 165.109 175.530 194.871 1.00 31.24  ? 178  ALA A CA    1 
ATOM   1276 C C     . ALA A 1 178  ? 165.430 176.036 193.473 1.00 37.58  ? 178  ALA A C     1 
ATOM   1277 O O     . ALA A 1 178  ? 166.542 175.838 192.960 1.00 47.51  ? 178  ALA A O     1 
ATOM   1278 C CB    . ALA A 1 178  ? 164.163 174.331 194.809 1.00 30.73  ? 178  ALA A CB    1 
ATOM   1279 N N     . ALA A 1 179  ? 164.467 176.723 192.853 1.00 36.70  ? 179  ALA A N     1 
ATOM   1280 C CA    . ALA A 1 179  ? 164.723 177.324 191.547 1.00 28.36  ? 179  ALA A CA    1 
ATOM   1281 C C     . ALA A 1 179  ? 165.841 178.358 191.626 1.00 28.76  ? 179  ALA A C     1 
ATOM   1282 O O     . ALA A 1 179  ? 166.721 178.406 190.755 1.00 34.66  ? 179  ALA A O     1 
ATOM   1283 C CB    . ALA A 1 179  ? 163.445 177.956 190.999 1.00 33.36  ? 179  ALA A CB    1 
ATOM   1284 N N     . ILE A 1 180  ? 165.828 179.185 192.674 1.00 31.72  ? 180  ILE A N     1 
ATOM   1285 C CA    . ILE A 1 180  ? 166.847 180.219 192.835 1.00 32.93  ? 180  ILE A CA    1 
ATOM   1286 C C     . ILE A 1 180  ? 168.228 179.597 192.983 1.00 38.87  ? 180  ILE A C     1 
ATOM   1287 O O     . ILE A 1 180  ? 169.201 180.073 192.393 1.00 42.64  ? 180  ILE A O     1 
ATOM   1288 C CB    . ILE A 1 180  ? 166.508 181.127 194.031 1.00 29.71  ? 180  ILE A CB    1 
ATOM   1289 C CG1   . ILE A 1 180  ? 165.280 181.979 193.732 1.00 28.27  ? 180  ILE A CG1   1 
ATOM   1290 C CG2   . ILE A 1 180  ? 167.686 182.021 194.376 1.00 35.80  ? 180  ILE A CG2   1 
ATOM   1291 C CD1   . ILE A 1 180  ? 164.902 182.890 194.866 1.00 28.77  ? 180  ILE A CD1   1 
ATOM   1292 N N     . ARG A 1 181  ? 168.341 178.532 193.779 1.00 38.01  ? 181  ARG A N     1 
ATOM   1293 C CA    . ARG A 1 181  ? 169.637 177.900 193.990 1.00 38.43  ? 181  ARG A CA    1 
ATOM   1294 C C     . ARG A 1 181  ? 170.138 177.229 192.721 1.00 40.55  ? 181  ARG A C     1 
ATOM   1295 O O     . ARG A 1 181  ? 171.336 177.277 192.424 1.00 45.88  ? 181  ARG A O     1 
ATOM   1296 C CB    . ARG A 1 181  ? 169.558 176.891 195.134 1.00 41.19  ? 181  ARG A CB    1 
ATOM   1297 C CG    . ARG A 1 181  ? 170.904 176.285 195.485 1.00 48.35  ? 181  ARG A CG    1 
ATOM   1298 C CD    . ARG A 1 181  ? 170.812 175.306 196.640 1.00 54.19  ? 181  ARG A CD    1 
ATOM   1299 N NE    . ARG A 1 181  ? 172.126 174.771 196.976 1.00 57.70  ? 181  ARG A NE    1 
ATOM   1300 C CZ    . ARG A 1 181  ? 172.985 175.357 197.797 1.00 56.56  ? 181  ARG A CZ    1 
ATOM   1301 N NH1   . ARG A 1 181  ? 172.691 176.489 198.414 1.00 54.05  ? 181  ARG A NH1   1 
ATOM   1302 N NH2   . ARG A 1 181  ? 174.173 174.796 198.001 1.00 64.26  ? 181  ARG A NH2   1 
ATOM   1303 N N     . LYS A 1 182  ? 169.243 176.596 191.957 1.00 40.22  ? 182  LYS A N     1 
ATOM   1304 C CA    . LYS A 1 182  ? 169.663 176.025 190.681 1.00 39.37  ? 182  LYS A CA    1 
ATOM   1305 C C     . LYS A 1 182  ? 170.187 177.110 189.747 1.00 43.71  ? 182  LYS A C     1 
ATOM   1306 O O     . LYS A 1 182  ? 171.258 176.965 189.139 1.00 45.72  ? 182  LYS A O     1 
ATOM   1307 C CB    . LYS A 1 182  ? 168.506 175.264 190.034 1.00 31.49  ? 182  LYS A CB    1 
ATOM   1308 C CG    . LYS A 1 182  ? 168.828 174.735 188.649 1.00 37.48  ? 182  LYS A CG    1 
ATOM   1309 C CD    . LYS A 1 182  ? 167.675 173.939 188.067 1.00 44.80  ? 182  LYS A CD    1 
ATOM   1310 C CE    . LYS A 1 182  ? 167.458 172.644 188.825 1.00 49.31  ? 182  LYS A CE    1 
ATOM   1311 N NZ    . LYS A 1 182  ? 166.409 171.803 188.188 1.00 51.63  ? 182  LYS A NZ    1 
ATOM   1312 N N     . CYS A 1 183  ? 169.458 178.225 189.646 1.00 42.03  ? 183  CYS A N     1 
ATOM   1313 C CA    . CYS A 1 183  ? 169.897 179.314 188.779 1.00 34.87  ? 183  CYS A CA    1 
ATOM   1314 C C     . CYS A 1 183  ? 171.208 179.920 189.264 1.00 39.09  ? 183  CYS A C     1 
ATOM   1315 O O     . CYS A 1 183  ? 172.056 180.312 188.455 1.00 43.39  ? 183  CYS A O     1 
ATOM   1316 C CB    . CYS A 1 183  ? 168.810 180.383 188.692 1.00 35.37  ? 183  CYS A CB    1 
ATOM   1317 S SG    . CYS A 1 183  ? 167.287 179.824 187.905 1.00 58.10  ? 183  CYS A SG    1 
ATOM   1318 N N     . ALA A 1 184  ? 171.391 180.008 190.583 1.00 35.40  ? 184  ALA A N     1 
ATOM   1319 C CA    . ALA A 1 184  ? 172.594 180.621 191.132 1.00 35.78  ? 184  ALA A CA    1 
ATOM   1320 C C     . ALA A 1 184  ? 173.808 179.722 190.950 1.00 42.42  ? 184  ALA A C     1 
ATOM   1321 O O     . ALA A 1 184  ? 174.922 180.212 190.735 1.00 44.89  ? 184  ALA A O     1 
ATOM   1322 C CB    . ALA A 1 184  ? 172.383 180.948 192.608 1.00 35.97  ? 184  ALA A CB    1 
ATOM   1323 N N     . LYS A 1 185  ? 173.618 178.405 191.051 1.00 44.88  ? 185  LYS A N     1 
ATOM   1324 C CA    . LYS A 1 185  ? 174.694 177.483 190.708 1.00 44.83  ? 185  LYS A CA    1 
ATOM   1325 C C     . LYS A 1 185  ? 175.043 177.589 189.231 1.00 44.45  ? 185  LYS A C     1 
ATOM   1326 O O     . LYS A 1 185  ? 176.222 177.559 188.859 1.00 42.00  ? 185  LYS A O     1 
ATOM   1327 C CB    . LYS A 1 185  ? 174.301 176.051 191.069 1.00 45.71  ? 185  LYS A CB    1 
ATOM   1328 C CG    . LYS A 1 185  ? 174.157 175.800 192.560 1.00 48.24  ? 185  LYS A CG    1 
ATOM   1329 C CD    . LYS A 1 185  ? 173.842 174.341 192.838 1.00 55.57  ? 185  LYS A CD    1 
ATOM   1330 C CE    . LYS A 1 185  ? 172.624 173.887 192.054 1.00 58.26  ? 185  LYS A CE    1 
ATOM   1331 N NZ    . LYS A 1 185  ? 172.372 172.430 192.212 1.00 62.97  ? 185  LYS A NZ    1 
ATOM   1332 N N     . LEU A 1 186  ? 174.028 177.715 188.371 1.00 45.60  ? 186  LEU A N     1 
ATOM   1333 C CA    . LEU A 1 186  ? 174.300 177.947 186.957 1.00 40.23  ? 186  LEU A CA    1 
ATOM   1334 C C     . LEU A 1 186  ? 174.938 179.311 186.722 1.00 40.27  ? 186  LEU A C     1 
ATOM   1335 O O     . LEU A 1 186  ? 175.783 179.450 185.830 1.00 43.29  ? 186  LEU A O     1 
ATOM   1336 C CB    . LEU A 1 186  ? 173.017 177.812 186.139 1.00 40.73  ? 186  LEU A CB    1 
ATOM   1337 C CG    . LEU A 1 186  ? 172.729 176.437 185.532 1.00 45.81  ? 186  LEU A CG    1 
ATOM   1338 C CD1   . LEU A 1 186  ? 173.841 176.036 184.578 1.00 47.13  ? 186  LEU A CD1   1 
ATOM   1339 C CD2   . LEU A 1 186  ? 172.545 175.384 186.611 1.00 45.18  ? 186  LEU A CD2   1 
ATOM   1340 N N     . ALA A 1 187  ? 174.555 180.322 187.500 1.00 38.79  ? 187  ALA A N     1 
ATOM   1341 C CA    . ALA A 1 187  ? 175.081 181.672 187.345 1.00 35.36  ? 187  ALA A CA    1 
ATOM   1342 C C     . ALA A 1 187  ? 176.302 181.947 188.210 1.00 41.86  ? 187  ALA A C     1 
ATOM   1343 O O     . ALA A 1 187  ? 176.809 183.073 188.189 1.00 42.11  ? 187  ALA A O     1 
ATOM   1344 C CB    . ALA A 1 187  ? 173.995 182.703 187.663 1.00 34.07  ? 187  ALA A CB    1 
ATOM   1345 N N     . ALA A 1 188  ? 176.780 180.954 188.964 1.00 46.44  ? 188  ALA A N     1 
ATOM   1346 C CA    . ALA A 1 188  ? 177.950 181.103 189.834 1.00 45.20  ? 188  ALA A CA    1 
ATOM   1347 C C     . ALA A 1 188  ? 177.770 182.248 190.829 1.00 49.34  ? 188  ALA A C     1 
ATOM   1348 O O     . ALA A 1 188  ? 178.690 183.029 191.079 1.00 50.30  ? 188  ALA A O     1 
ATOM   1349 C CB    . ALA A 1 188  ? 179.230 181.290 189.016 1.00 40.97  ? 188  ALA A CB    1 
ATOM   1350 N N     . ALA A 1 189  ? 176.575 182.349 191.403 1.00 45.90  ? 189  ALA A N     1 
ATOM   1351 C CA    . ALA A 1 189  ? 176.293 183.375 192.392 1.00 43.55  ? 189  ALA A CA    1 
ATOM   1352 C C     . ALA A 1 189  ? 176.754 182.931 193.777 1.00 51.79  ? 189  ALA A C     1 
ATOM   1353 O O     . ALA A 1 189  ? 176.867 181.739 194.073 1.00 51.69  ? 189  ALA A O     1 
ATOM   1354 C CB    . ALA A 1 189  ? 174.801 183.705 192.417 1.00 39.83  ? 189  ALA A CB    1 
ATOM   1355 N N     . LYS A 1 190  ? 177.022 183.914 194.632 1.00 55.68  ? 190  LYS A N     1 
ATOM   1356 C CA    . LYS A 1 190  ? 177.480 183.668 195.993 1.00 50.36  ? 190  LYS A CA    1 
ATOM   1357 C C     . LYS A 1 190  ? 176.306 183.740 196.960 1.00 46.77  ? 190  LYS A C     1 
ATOM   1358 O O     . LYS A 1 190  ? 175.545 184.713 196.950 1.00 49.10  ? 190  LYS A O     1 
ATOM   1359 C CB    . LYS A 1 190  ? 178.555 184.676 196.403 1.00 49.10  ? 190  LYS A CB    1 
ATOM   1360 C CG    . LYS A 1 190  ? 179.971 184.262 196.041 1.00 54.77  ? 190  LYS A CG    1 
ATOM   1361 C CD    . LYS A 1 190  ? 180.296 184.566 194.590 1.00 65.97  ? 190  LYS A CD    1 
ATOM   1362 C CE    . LYS A 1 190  ? 180.340 186.063 194.342 1.00 71.64  ? 190  LYS A CE    1 
ATOM   1363 N NZ    . LYS A 1 190  ? 180.862 186.382 192.988 1.00 69.51  ? 190  LYS A NZ    1 
ATOM   1364 N N     . PHE A 1 191  ? 176.167 182.713 197.791 1.00 46.18  ? 191  PHE A N     1 
ATOM   1365 C CA    . PHE A 1 191  ? 175.165 182.694 198.843 1.00 50.00  ? 191  PHE A CA    1 
ATOM   1366 C C     . PHE A 1 191  ? 175.751 183.244 200.138 1.00 52.44  ? 191  PHE A C     1 
ATOM   1367 O O     . PHE A 1 191  ? 176.969 183.289 200.329 1.00 53.95  ? 191  PHE A O     1 
ATOM   1368 C CB    . PHE A 1 191  ? 174.645 181.276 199.077 1.00 47.51  ? 191  PHE A CB    1 
ATOM   1369 C CG    . PHE A 1 191  ? 174.280 180.544 197.820 1.00 42.73  ? 191  PHE A CG    1 
ATOM   1370 C CD1   . PHE A 1 191  ? 173.039 180.714 197.238 1.00 47.23  ? 191  PHE A CD1   1 
ATOM   1371 C CD2   . PHE A 1 191  ? 175.175 179.675 197.228 1.00 45.39  ? 191  PHE A CD2   1 
ATOM   1372 C CE1   . PHE A 1 191  ? 172.702 180.037 196.084 1.00 50.99  ? 191  PHE A CE1   1 
ATOM   1373 C CE2   . PHE A 1 191  ? 174.843 178.996 196.074 1.00 44.66  ? 191  PHE A CE2   1 
ATOM   1374 C CZ    . PHE A 1 191  ? 173.606 179.176 195.503 1.00 48.01  ? 191  PHE A CZ    1 
ATOM   1375 N N     . ASP A 1 192  ? 174.864 183.661 201.036 1.00 49.75  ? 192  ASP A N     1 
ATOM   1376 C CA    . ASP A 1 192  ? 175.283 184.096 202.361 1.00 51.37  ? 192  ASP A CA    1 
ATOM   1377 C C     . ASP A 1 192  ? 175.416 182.869 203.262 1.00 55.17  ? 192  ASP A C     1 
ATOM   1378 O O     . ASP A 1 192  ? 175.402 181.725 202.800 1.00 53.96  ? 192  ASP A O     1 
ATOM   1379 C CB    . ASP A 1 192  ? 174.312 185.134 202.918 1.00 52.52  ? 192  ASP A CB    1 
ATOM   1380 C CG    . ASP A 1 192  ? 172.918 184.586 203.100 1.00 52.12  ? 192  ASP A CG    1 
ATOM   1381 O OD1   . ASP A 1 192  ? 172.557 183.647 202.367 1.00 56.18  ? 192  ASP A OD1   1 
ATOM   1382 O OD2   . ASP A 1 192  ? 172.184 185.093 203.974 1.00 48.32  ? 192  ASP A OD2   1 
ATOM   1383 N N     . ASP A 1 193  ? 175.555 183.097 204.570 1.00 59.13  ? 193  ASP A N     1 
ATOM   1384 C CA    . ASP A 1 193  ? 175.824 181.995 205.489 1.00 58.87  ? 193  ASP A CA    1 
ATOM   1385 C C     . ASP A 1 193  ? 174.669 180.999 205.531 1.00 59.49  ? 193  ASP A C     1 
ATOM   1386 O O     . ASP A 1 193  ? 174.892 179.783 205.508 1.00 58.49  ? 193  ASP A O     1 
ATOM   1387 C CB    . ASP A 1 193  ? 176.114 182.543 206.887 1.00 64.38  ? 193  ASP A CB    1 
ATOM   1388 C CG    . ASP A 1 193  ? 176.539 181.462 207.861 1.00 72.77  ? 193  ASP A CG    1 
ATOM   1389 O OD1   . ASP A 1 193  ? 177.643 180.904 207.689 1.00 77.65  ? 193  ASP A OD1   1 
ATOM   1390 O OD2   . ASP A 1 193  ? 175.771 181.173 208.803 1.00 68.40  ? 193  ASP A OD2   1 
ATOM   1391 N N     . TYR A 1 194  ? 173.430 181.490 205.594 1.00 56.34  ? 194  TYR A N     1 
ATOM   1392 C CA    . TYR A 1 194  ? 172.291 180.586 205.730 1.00 54.45  ? 194  TYR A CA    1 
ATOM   1393 C C     . TYR A 1 194  ? 172.011 179.836 204.434 1.00 50.61  ? 194  TYR A C     1 
ATOM   1394 O O     . TYR A 1 194  ? 171.789 178.620 204.445 1.00 55.79  ? 194  TYR A O     1 
ATOM   1395 C CB    . TYR A 1 194  ? 171.049 181.356 206.176 1.00 56.21  ? 194  TYR A CB    1 
ATOM   1396 C CG    . TYR A 1 194  ? 169.802 180.503 206.191 1.00 58.80  ? 194  TYR A CG    1 
ATOM   1397 C CD1   . TYR A 1 194  ? 169.578 179.588 207.210 1.00 58.58  ? 194  TYR A CD1   1 
ATOM   1398 C CD2   . TYR A 1 194  ? 168.854 180.604 205.182 1.00 57.19  ? 194  TYR A CD2   1 
ATOM   1399 C CE1   . TYR A 1 194  ? 168.444 178.802 207.226 1.00 61.00  ? 194  TYR A CE1   1 
ATOM   1400 C CE2   . TYR A 1 194  ? 167.718 179.821 205.190 1.00 57.80  ? 194  TYR A CE2   1 
ATOM   1401 C CZ    . TYR A 1 194  ? 167.518 178.923 206.214 1.00 59.85  ? 194  TYR A CZ    1 
ATOM   1402 O OH    . TYR A 1 194  ? 166.388 178.140 206.227 1.00 59.02  ? 194  TYR A OH    1 
ATOM   1403 N N     . LEU A 1 195  ? 172.004 180.547 203.304 1.00 48.20  ? 195  LEU A N     1 
ATOM   1404 C CA    . LEU A 1 195  ? 171.654 179.908 202.039 1.00 46.74  ? 195  LEU A CA    1 
ATOM   1405 C C     . LEU A 1 195  ? 172.709 178.901 201.603 1.00 50.79  ? 195  LEU A C     1 
ATOM   1406 O O     . LEU A 1 195  ? 172.390 177.946 200.887 1.00 53.06  ? 195  LEU A O     1 
ATOM   1407 C CB    . LEU A 1 195  ? 171.444 180.963 200.954 1.00 48.66  ? 195  LEU A CB    1 
ATOM   1408 C CG    . LEU A 1 195  ? 170.267 181.924 201.135 1.00 44.95  ? 195  LEU A CG    1 
ATOM   1409 C CD1   . LEU A 1 195  ? 170.137 182.835 199.927 1.00 45.53  ? 195  LEU A CD1   1 
ATOM   1410 C CD2   . LEU A 1 195  ? 168.975 181.168 201.385 1.00 47.48  ? 195  LEU A CD2   1 
ATOM   1411 N N     . GLU A 1 196  ? 173.965 179.099 202.008 1.00 50.30  ? 196  GLU A N     1 
ATOM   1412 C CA    . GLU A 1 196  ? 174.995 178.110 201.707 1.00 49.97  ? 196  GLU A CA    1 
ATOM   1413 C C     . GLU A 1 196  ? 174.722 176.798 202.431 1.00 55.49  ? 196  GLU A C     1 
ATOM   1414 O O     . GLU A 1 196  ? 174.883 175.716 201.855 1.00 60.37  ? 196  GLU A O     1 
ATOM   1415 C CB    . GLU A 1 196  ? 176.372 178.654 202.081 1.00 50.89  ? 196  GLU A CB    1 
ATOM   1416 C CG    . GLU A 1 196  ? 177.523 177.767 201.646 1.00 53.45  ? 196  GLU A CG    1 
ATOM   1417 C CD    . GLU A 1 196  ? 177.669 177.700 200.140 1.00 66.66  ? 196  GLU A CD    1 
ATOM   1418 O OE1   . GLU A 1 196  ? 177.422 178.726 199.473 1.00 68.63  ? 196  GLU A OE1   1 
ATOM   1419 O OE2   . GLU A 1 196  ? 178.023 176.621 199.621 1.00 70.71  ? 196  GLU A OE2   1 
ATOM   1420 N N     . LYS A 1 197  ? 174.305 176.873 203.697 1.00 55.65  ? 197  LYS A N     1 
ATOM   1421 C CA    . LYS A 1 197  ? 174.023 175.663 204.462 1.00 54.21  ? 197  LYS A CA    1 
ATOM   1422 C C     . LYS A 1 197  ? 172.704 175.025 204.047 1.00 56.89  ? 197  LYS A C     1 
ATOM   1423 O O     . LYS A 1 197  ? 172.551 173.804 204.148 1.00 65.63  ? 197  LYS A O     1 
ATOM   1424 C CB    . LYS A 1 197  ? 174.012 175.979 205.957 1.00 56.66  ? 197  LYS A CB    1 
ATOM   1425 C CG    . LYS A 1 197  ? 175.335 176.507 206.484 1.00 60.19  ? 197  LYS A CG    1 
ATOM   1426 C CD    . LYS A 1 197  ? 175.244 176.863 207.959 1.00 60.08  ? 197  LYS A CD    1 
ATOM   1427 C CE    . LYS A 1 197  ? 174.233 177.971 208.198 1.00 55.80  ? 197  LYS A CE    1 
ATOM   1428 N NZ    . LYS A 1 197  ? 174.157 178.359 209.633 1.00 59.82  ? 197  LYS A NZ    1 
ATOM   1429 N N     . THR A 1 198  ? 171.741 175.824 203.600 1.00 51.45  ? 198  THR A N     1 
ATOM   1430 C CA    . THR A 1 198  ? 170.456 175.291 203.173 1.00 48.05  ? 198  THR A CA    1 
ATOM   1431 C C     . THR A 1 198  ? 170.565 174.700 201.774 1.00 54.40  ? 198  THR A C     1 
ATOM   1432 O O     . THR A 1 198  ? 171.219 175.266 200.895 1.00 56.06  ? 198  THR A O     1 
ATOM   1433 C CB    . THR A 1 198  ? 169.388 176.384 203.198 1.00 47.05  ? 198  THR A CB    1 
ATOM   1434 O OG1   . THR A 1 198  ? 169.415 177.049 204.466 1.00 57.65  ? 198  THR A OG1   1 
ATOM   1435 C CG2   . THR A 1 198  ? 168.011 175.786 202.986 1.00 45.52  ? 198  THR A CG2   1 
ATOM   1436 N N     . HIS A 1 199  ? 169.936 173.544 201.577 1.00 52.25  ? 199  HIS A N     1 
ATOM   1437 C CA    . HIS A 1 199  ? 169.908 172.876 200.282 1.00 43.49  ? 199  HIS A CA    1 
ATOM   1438 C C     . HIS A 1 199  ? 168.485 172.429 199.999 1.00 40.45  ? 199  HIS A C     1 
ATOM   1439 O O     . HIS A 1 199  ? 167.898 171.690 200.795 1.00 50.40  ? 199  HIS A O     1 
ATOM   1440 C CB    . HIS A 1 199  ? 170.853 171.672 200.250 1.00 46.34  ? 199  HIS A CB    1 
ATOM   1441 C CG    . HIS A 1 199  ? 172.285 172.015 200.519 1.00 53.93  ? 199  HIS A CG    1 
ATOM   1442 N ND1   . HIS A 1 199  ? 173.204 172.210 199.512 1.00 55.21  ? 199  HIS A ND1   1 
ATOM   1443 C CD2   . HIS A 1 199  ? 172.957 172.187 201.681 1.00 54.50  ? 199  HIS A CD2   1 
ATOM   1444 C CE1   . HIS A 1 199  ? 174.381 172.492 200.042 1.00 54.87  ? 199  HIS A CE1   1 
ATOM   1445 N NE2   . HIS A 1 199  ? 174.257 172.486 201.356 1.00 54.94  ? 199  HIS A NE2   1 
ATOM   1446 N N     . VAL A 1 200  ? 167.931 172.878 198.878 1.00 39.42  ? 200  VAL A N     1 
ATOM   1447 C CA    . VAL A 1 200  ? 166.636 172.412 198.399 1.00 38.62  ? 200  VAL A CA    1 
ATOM   1448 C C     . VAL A 1 200  ? 166.812 171.977 196.954 1.00 39.24  ? 200  VAL A C     1 
ATOM   1449 O O     . VAL A 1 200  ? 167.205 172.783 196.103 1.00 44.25  ? 200  VAL A O     1 
ATOM   1450 C CB    . VAL A 1 200  ? 165.545 173.489 198.510 1.00 39.01  ? 200  VAL A CB    1 
ATOM   1451 C CG1   . VAL A 1 200  ? 164.189 172.894 198.172 1.00 37.92  ? 200  VAL A CG1   1 
ATOM   1452 C CG2   . VAL A 1 200  ? 165.530 174.092 199.900 1.00 40.49  ? 200  VAL A CG2   1 
ATOM   1453 N N     . ILE A 1 201  ? 166.526 170.708 196.677 1.00 40.84  ? 201  ILE A N     1 
ATOM   1454 C CA    . ILE A 1 201  ? 166.672 170.131 195.348 1.00 36.36  ? 201  ILE A CA    1 
ATOM   1455 C C     . ILE A 1 201  ? 165.327 169.562 194.930 1.00 34.34  ? 201  ILE A C     1 
ATOM   1456 O O     . ILE A 1 201  ? 164.714 168.796 195.681 1.00 37.82  ? 201  ILE A O     1 
ATOM   1457 C CB    . ILE A 1 201  ? 167.757 169.039 195.312 1.00 39.57  ? 201  ILE A CB    1 
ATOM   1458 C CG1   . ILE A 1 201  ? 169.091 169.577 195.834 1.00 42.82  ? 201  ILE A CG1   1 
ATOM   1459 C CG2   . ILE A 1 201  ? 167.920 168.495 193.904 1.00 45.75  ? 201  ILE A CG2   1 
ATOM   1460 C CD1   . ILE A 1 201  ? 169.349 169.265 197.293 1.00 44.40  ? 201  ILE A CD1   1 
ATOM   1461 N N     . LYS A 1 202  ? 164.866 169.938 193.742 1.00 33.75  ? 202  LYS A N     1 
ATOM   1462 C CA    . LYS A 1 202  ? 163.652 169.367 193.161 1.00 40.85  ? 202  LYS A CA    1 
ATOM   1463 C C     . LYS A 1 202  ? 164.023 168.675 191.860 1.00 47.82  ? 202  LYS A C     1 
ATOM   1464 O O     . LYS A 1 202  ? 164.119 169.335 190.810 1.00 47.37  ? 202  LYS A O     1 
ATOM   1465 C CB    . LYS A 1 202  ? 162.591 170.439 192.921 1.00 39.91  ? 202  LYS A CB    1 
ATOM   1466 C CG    . LYS A 1 202  ? 161.271 169.891 192.411 1.00 41.85  ? 202  LYS A CG    1 
ATOM   1467 C CD    . LYS A 1 202  ? 160.222 170.981 192.306 1.00 48.40  ? 202  LYS A CD    1 
ATOM   1468 C CE    . LYS A 1 202  ? 158.864 170.407 191.936 1.00 54.44  ? 202  LYS A CE    1 
ATOM   1469 N NZ    . LYS A 1 202  ? 157.810 171.455 191.857 1.00 57.45  ? 202  LYS A NZ    1 
ATOM   1470 N N     . PRO A 1 203  ? 164.261 167.364 191.878 1.00 47.05  ? 203  PRO A N     1 
ATOM   1471 C CA    . PRO A 1 203  ? 164.642 166.671 190.644 1.00 45.59  ? 203  PRO A CA    1 
ATOM   1472 C C     . PRO A 1 203  ? 163.552 166.768 189.589 1.00 55.52  ? 203  PRO A C     1 
ATOM   1473 O O     . PRO A 1 203  ? 162.363 166.626 189.880 1.00 58.00  ? 203  PRO A O     1 
ATOM   1474 C CB    . PRO A 1 203  ? 164.852 165.223 191.100 1.00 42.00  ? 203  PRO A CB    1 
ATOM   1475 C CG    . PRO A 1 203  ? 165.082 165.311 192.566 1.00 41.14  ? 203  PRO A CG    1 
ATOM   1476 C CD    . PRO A 1 203  ? 164.262 166.463 193.041 1.00 36.33  ? 203  PRO A CD    1 
ATOM   1477 N N     . THR A 1 204  ? 163.972 167.013 188.353 1.00 53.79  ? 204  THR A N     1 
ATOM   1478 C CA    . THR A 1 204  ? 163.087 166.981 187.197 1.00 54.64  ? 204  THR A CA    1 
ATOM   1479 C C     . THR A 1 204  ? 163.318 165.764 186.320 1.00 56.68  ? 204  THR A C     1 
ATOM   1480 O O     . THR A 1 204  ? 162.359 165.177 185.816 1.00 55.38  ? 204  THR A O     1 
ATOM   1481 C CB    . THR A 1 204  ? 163.262 168.251 186.356 1.00 60.77  ? 204  THR A CB    1 
ATOM   1482 O OG1   . THR A 1 204  ? 164.604 168.317 185.861 1.00 66.80  ? 204  THR A OG1   1 
ATOM   1483 C CG2   . THR A 1 204  ? 162.977 169.486 187.195 1.00 56.54  ? 204  THR A CG2   1 
ATOM   1484 N N     . SER A 1 205  ? 164.576 165.376 186.135 1.00 56.25  ? 205  SER A N     1 
ATOM   1485 C CA    . SER A 1 205  ? 164.950 164.171 185.418 1.00 52.85  ? 205  SER A CA    1 
ATOM   1486 C C     . SER A 1 205  ? 165.662 163.221 186.371 1.00 53.91  ? 205  SER A C     1 
ATOM   1487 O O     . SER A 1 205  ? 166.183 163.628 187.413 1.00 53.10  ? 205  SER A O     1 
ATOM   1488 C CB    . SER A 1 205  ? 165.850 164.492 184.218 1.00 53.85  ? 205  SER A CB    1 
ATOM   1489 O OG    . SER A 1 205  ? 167.032 165.154 184.632 1.00 63.82  ? 205  SER A OG    1 
ATOM   1490 N N     . LEU A 1 206  ? 165.684 161.943 186.002 1.00 53.18  ? 206  LEU A N     1 
ATOM   1491 C CA    . LEU A 1 206  ? 166.260 160.904 186.840 1.00 48.13  ? 206  LEU A CA    1 
ATOM   1492 C C     . LEU A 1 206  ? 167.272 160.098 186.040 1.00 51.92  ? 206  LEU A C     1 
ATOM   1493 O O     . LEU A 1 206  ? 167.109 159.884 184.836 1.00 60.95  ? 206  LEU A O     1 
ATOM   1494 C CB    . LEU A 1 206  ? 165.176 159.972 187.395 1.00 49.06  ? 206  LEU A CB    1 
ATOM   1495 C CG    . LEU A 1 206  ? 165.510 159.223 188.683 1.00 50.05  ? 206  LEU A CG    1 
ATOM   1496 C CD1   . LEU A 1 206  ? 165.626 160.199 189.832 1.00 40.50  ? 206  LEU A CD1   1 
ATOM   1497 C CD2   . LEU A 1 206  ? 164.456 158.176 188.977 1.00 45.00  ? 206  LEU A CD2   1 
ATOM   1498 N N     . SER A 1 207  ? 168.322 159.653 186.724 1.00 49.02  ? 207  SER A N     1 
ATOM   1499 C CA    . SER A 1 207  ? 169.364 158.828 186.129 1.00 48.20  ? 207  SER A CA    1 
ATOM   1500 C C     . SER A 1 207  ? 169.383 157.475 186.822 1.00 47.08  ? 207  SER A C     1 
ATOM   1501 O O     . SER A 1 207  ? 169.407 157.406 188.055 1.00 52.43  ? 207  SER A O     1 
ATOM   1502 C CB    . SER A 1 207  ? 170.732 159.505 186.241 1.00 48.23  ? 207  SER A CB    1 
ATOM   1503 O OG    . SER A 1 207  ? 171.754 158.684 185.707 1.00 48.53  ? 207  SER A OG    1 
ATOM   1504 N N     . LEU A 1 208  ? 169.373 156.405 186.032 1.00 48.38  ? 208  LEU A N     1 
ATOM   1505 C CA    . LEU A 1 208  ? 169.379 155.038 186.544 1.00 50.83  ? 208  LEU A CA    1 
ATOM   1506 C C     . LEU A 1 208  ? 170.770 154.455 186.338 1.00 51.81  ? 208  LEU A C     1 
ATOM   1507 O O     . LEU A 1 208  ? 171.218 154.288 185.199 1.00 53.42  ? 208  LEU A O     1 
ATOM   1508 C CB    . LEU A 1 208  ? 168.317 154.187 185.851 1.00 49.46  ? 208  LEU A CB    1 
ATOM   1509 C CG    . LEU A 1 208  ? 166.938 154.107 186.510 1.00 52.40  ? 208  LEU A CG    1 
ATOM   1510 C CD1   . LEU A 1 208  ? 166.367 155.491 186.762 1.00 50.11  ? 208  LEU A CD1   1 
ATOM   1511 C CD2   . LEU A 1 208  ? 165.986 153.283 185.655 1.00 48.75  ? 208  LEU A CD2   1 
ATOM   1512 N N     . ARG A 1 209  ? 171.449 154.146 187.439 1.00 48.87  ? 209  ARG A N     1 
ATOM   1513 C CA    . ARG A 1 209  ? 172.791 153.579 187.396 1.00 52.68  ? 209  ARG A CA    1 
ATOM   1514 C C     . ARG A 1 209  ? 172.682 152.063 187.490 1.00 55.49  ? 209  ARG A C     1 
ATOM   1515 O O     . ARG A 1 209  ? 172.326 151.522 188.542 1.00 64.61  ? 209  ARG A O     1 
ATOM   1516 C CB    . ARG A 1 209  ? 173.650 154.144 188.524 1.00 57.60  ? 209  ARG A CB    1 
ATOM   1517 C CG    . ARG A 1 209  ? 173.934 155.627 188.393 1.00 57.56  ? 209  ARG A CG    1 
ATOM   1518 C CD    . ARG A 1 209  ? 174.868 156.102 189.487 1.00 61.30  ? 209  ARG A CD    1 
ATOM   1519 N NE    . ARG A 1 209  ? 175.369 157.446 189.229 1.00 65.31  ? 209  ARG A NE    1 
ATOM   1520 C CZ    . ARG A 1 209  ? 176.187 158.107 190.035 1.00 66.87  ? 209  ARG A CZ    1 
ATOM   1521 N NH1   . ARG A 1 209  ? 176.616 157.579 191.170 1.00 64.53  ? 209  ARG A NH1   1 
ATOM   1522 N NH2   . ARG A 1 209  ? 176.585 159.329 189.695 1.00 65.53  ? 209  ARG A NH2   1 
ATOM   1523 N N     . LEU A 1 210  ? 172.990 151.380 186.393 1.00 48.99  ? 210  LEU A N     1 
ATOM   1524 C CA    . LEU A 1 210  ? 172.872 149.932 186.307 1.00 47.34  ? 210  LEU A CA    1 
ATOM   1525 C C     . LEU A 1 210  ? 174.246 149.296 186.461 1.00 55.43  ? 210  LEU A C     1 
ATOM   1526 O O     . LEU A 1 210  ? 175.221 149.756 185.858 1.00 56.36  ? 210  LEU A O     1 
ATOM   1527 C CB    . LEU A 1 210  ? 172.241 149.520 184.977 1.00 46.28  ? 210  LEU A CB    1 
ATOM   1528 C CG    . LEU A 1 210  ? 170.873 150.135 184.679 1.00 42.14  ? 210  LEU A CG    1 
ATOM   1529 C CD1   . LEU A 1 210  ? 170.416 149.766 183.285 1.00 43.01  ? 210  LEU A CD1   1 
ATOM   1530 C CD2   . LEU A 1 210  ? 169.856 149.690 185.710 1.00 46.82  ? 210  LEU A CD2   1 
ATOM   1531 N N     . ARG A 1 211  ? 174.319 148.242 187.269 1.00 56.64  ? 211  ARG A N     1 
ATOM   1532 C CA    . ARG A 1 211  ? 175.581 147.563 187.543 1.00 55.55  ? 211  ARG A CA    1 
ATOM   1533 C C     . ARG A 1 211  ? 175.275 146.112 187.878 1.00 60.55  ? 211  ARG A C     1 
ATOM   1534 O O     . ARG A 1 211  ? 174.549 145.840 188.838 1.00 65.44  ? 211  ARG A O     1 
ATOM   1535 C CB    . ARG A 1 211  ? 176.329 148.249 188.689 1.00 59.69  ? 211  ARG A CB    1 
ATOM   1536 C CG    . ARG A 1 211  ? 177.748 147.753 188.924 1.00 65.00  ? 211  ARG A CG    1 
ATOM   1537 C CD    . ARG A 1 211  ? 177.801 146.706 190.024 1.00 69.02  ? 211  ARG A CD    1 
ATOM   1538 N NE    . ARG A 1 211  ? 177.125 147.154 191.235 1.00 73.08  ? 211  ARG A NE    1 
ATOM   1539 C CZ    . ARG A 1 211  ? 177.044 146.447 192.354 1.00 77.90  ? 211  ARG A CZ    1 
ATOM   1540 N NH1   . ARG A 1 211  ? 177.601 145.252 192.457 1.00 77.37  ? 211  ARG A NH1   1 
ATOM   1541 N NH2   . ARG A 1 211  ? 176.389 146.953 193.395 1.00 74.47  ? 211  ARG A NH2   1 
ATOM   1542 N N     . LYS A 1 212  ? 175.819 145.190 187.089 1.00 59.01  ? 212  LYS A N     1 
ATOM   1543 C CA    . LYS A 1 212  ? 175.561 143.774 187.306 1.00 60.32  ? 212  LYS A CA    1 
ATOM   1544 C C     . LYS A 1 212  ? 176.254 143.286 188.573 1.00 66.47  ? 212  LYS A C     1 
ATOM   1545 O O     . LYS A 1 212  ? 177.394 143.658 188.860 1.00 69.28  ? 212  LYS A O     1 
ATOM   1546 C CB    . LYS A 1 212  ? 176.031 142.962 186.101 1.00 63.32  ? 212  LYS A CB    1 
ATOM   1547 C CG    . LYS A 1 212  ? 175.462 143.444 184.776 1.00 60.60  ? 212  LYS A CG    1 
ATOM   1548 C CD    . LYS A 1 212  ? 174.453 142.466 184.203 1.00 57.20  ? 212  LYS A CD    1 
ATOM   1549 C CE    . LYS A 1 212  ? 175.125 141.184 183.745 1.00 57.95  ? 212  LYS A CE    1 
ATOM   1550 N NZ    . LYS A 1 212  ? 174.168 140.253 183.088 1.00 59.03  ? 212  LYS A NZ    1 
ATOM   1551 N N     . ALA A 1 213  ? 175.555 142.444 189.331 1.00 69.54  ? 213  ALA A N     1 
ATOM   1552 C CA    . ALA A 1 213  ? 176.067 141.901 190.580 1.00 74.66  ? 213  ALA A CA    1 
ATOM   1553 C C     . ALA A 1 213  ? 175.669 140.436 190.684 1.00 78.65  ? 213  ALA A C     1 
ATOM   1554 O O     . ALA A 1 213  ? 174.857 139.935 189.905 1.00 81.14  ? 213  ALA A O     1 
ATOM   1555 C CB    . ALA A 1 213  ? 175.552 142.689 191.790 1.00 77.79  ? 213  ALA A CB    1 
ATOM   1556 N N     . THR A 1 214  ? 176.252 139.745 191.662 1.00 82.29  ? 214  THR A N     1 
ATOM   1557 C CA    . THR A 1 214  ? 176.011 138.321 191.883 1.00 91.08  ? 214  THR A CA    1 
ATOM   1558 C C     . THR A 1 214  ? 175.552 138.075 193.315 1.00 94.04  ? 214  THR A C     1 
ATOM   1559 O O     . THR A 1 214  ? 176.048 137.190 194.015 1.00 93.37  ? 214  THR A O     1 
ATOM   1560 C CB    . THR A 1 214  ? 177.257 137.495 191.571 1.00 89.62  ? 214  THR A CB    1 
ATOM   1561 O OG1   . THR A 1 214  ? 178.369 138.001 192.320 1.00 92.43  ? 214  THR A OG1   1 
ATOM   1562 C CG2   . THR A 1 214  ? 177.581 137.555 190.085 1.00 81.21  ? 214  THR A CG2   1 
ATOM   1563 N N     . VAL A 1 215  ? 174.585 138.875 193.770 1.00 92.60  ? 215  VAL A N     1 
ATOM   1564 C CA    . VAL A 1 215  ? 174.068 138.724 195.127 1.00 94.82  ? 215  VAL A CA    1 
ATOM   1565 C C     . VAL A 1 215  ? 173.351 137.388 195.289 1.00 101.37 ? 215  VAL A C     1 
ATOM   1566 O O     . VAL A 1 215  ? 173.560 136.672 196.276 1.00 99.94  ? 215  VAL A O     1 
ATOM   1567 C CB    . VAL A 1 215  ? 173.148 139.907 195.477 1.00 95.55  ? 215  VAL A CB    1 
ATOM   1568 C CG1   . VAL A 1 215  ? 172.466 139.675 196.817 1.00 94.01  ? 215  VAL A CG1   1 
ATOM   1569 C CG2   . VAL A 1 215  ? 173.941 141.203 195.495 1.00 92.27  ? 215  VAL A CG2   1 
ATOM   1570 N N     . ALA A 1 216  ? 172.506 137.027 194.328 1.00 102.87 ? 216  ALA A N     1 
ATOM   1571 C CA    . ALA A 1 216  ? 171.727 135.798 194.409 1.00 103.69 ? 216  ALA A CA    1 
ATOM   1572 C C     . ALA A 1 216  ? 172.573 134.617 193.936 1.00 106.36 ? 216  ALA A C     1 
ATOM   1573 O O     . ALA A 1 216  ? 173.789 134.723 193.753 1.00 104.55 ? 216  ALA A O     1 
ATOM   1574 C CB    . ALA A 1 216  ? 170.438 135.936 193.604 1.00 95.78  ? 216  ALA A CB    1 
ATOM   1575 N N     . ASP A 1 217  ? 171.927 133.463 193.745 1.00 106.34 ? 217  ASP A N     1 
ATOM   1576 C CA    . ASP A 1 217  ? 172.631 132.300 193.212 1.00 104.40 ? 217  ASP A CA    1 
ATOM   1577 C C     . ASP A 1 217  ? 173.171 132.586 191.817 1.00 103.17 ? 217  ASP A C     1 
ATOM   1578 O O     . ASP A 1 217  ? 174.309 132.224 191.496 1.00 101.26 ? 217  ASP A O     1 
ATOM   1579 C CB    . ASP A 1 217  ? 171.701 131.088 193.192 1.00 105.15 ? 217  ASP A CB    1 
ATOM   1580 C CG    . ASP A 1 217  ? 171.081 130.806 194.547 1.00 110.01 ? 217  ASP A CG    1 
ATOM   1581 O OD1   . ASP A 1 217  ? 171.351 131.570 195.497 1.00 106.85 ? 217  ASP A OD1   1 
ATOM   1582 O OD2   . ASP A 1 217  ? 170.322 129.821 194.662 1.00 110.19 ? 217  ASP A OD2   1 
ATOM   1583 N N     . THR A 1 218  ? 172.370 133.232 190.978 1.00 103.08 ? 218  THR A N     1 
ATOM   1584 C CA    . THR A 1 218  ? 172.814 133.732 189.690 1.00 101.44 ? 218  THR A CA    1 
ATOM   1585 C C     . THR A 1 218  ? 173.030 135.241 189.786 1.00 98.25  ? 218  THR A C     1 
ATOM   1586 O O     . THR A 1 218  ? 172.800 135.863 190.825 1.00 93.93  ? 218  THR A O     1 
ATOM   1587 C CB    . THR A 1 218  ? 171.805 133.378 188.595 1.00 98.03  ? 218  THR A CB    1 
ATOM   1588 O OG1   . THR A 1 218  ? 170.519 133.912 188.935 1.00 96.16  ? 218  THR A OG1   1 
ATOM   1589 C CG2   . THR A 1 218  ? 171.697 131.868 188.440 1.00 93.46  ? 218  THR A CG2   1 
ATOM   1590 N N     . ALA A 1 219  ? 173.481 135.835 188.686 1.00 88.63  ? 219  ALA A N     1 
ATOM   1591 C CA    . ALA A 1 219  ? 173.783 137.258 188.689 1.00 82.97  ? 219  ALA A CA    1 
ATOM   1592 C C     . ALA A 1 219  ? 172.509 138.089 188.788 1.00 82.79  ? 219  ALA A C     1 
ATOM   1593 O O     . ALA A 1 219  ? 171.431 137.674 188.355 1.00 82.28  ? 219  ALA A O     1 
ATOM   1594 C CB    . ALA A 1 219  ? 174.563 137.645 187.433 1.00 75.86  ? 219  ALA A CB    1 
ATOM   1595 N N     . VAL A 1 220  ? 172.645 139.279 189.374 1.00 80.11  ? 220  VAL A N     1 
ATOM   1596 C CA    . VAL A 1 220  ? 171.557 140.240 189.487 1.00 73.97  ? 220  VAL A CA    1 
ATOM   1597 C C     . VAL A 1 220  ? 172.048 141.591 188.984 1.00 66.27  ? 220  VAL A C     1 
ATOM   1598 O O     . VAL A 1 220  ? 173.226 141.780 188.682 1.00 72.33  ? 220  VAL A O     1 
ATOM   1599 C CB    . VAL A 1 220  ? 171.020 140.365 190.929 1.00 72.01  ? 220  VAL A CB    1 
ATOM   1600 C CG1   . VAL A 1 220  ? 170.386 139.059 191.380 1.00 76.82  ? 220  VAL A CG1   1 
ATOM   1601 C CG2   . VAL A 1 220  ? 172.133 140.785 191.877 1.00 73.72  ? 220  VAL A CG2   1 
ATOM   1602 N N     . ILE A 1 221  ? 171.117 142.533 188.891 1.00 55.14  ? 221  ILE A N     1 
ATOM   1603 C CA    . ILE A 1 221  ? 171.393 143.891 188.442 1.00 53.97  ? 221  ILE A CA    1 
ATOM   1604 C C     . ILE A 1 221  ? 170.909 144.847 189.521 1.00 56.22  ? 221  ILE A C     1 
ATOM   1605 O O     . ILE A 1 221  ? 169.793 144.697 190.030 1.00 61.49  ? 221  ILE A O     1 
ATOM   1606 C CB    . ILE A 1 221  ? 170.709 144.189 187.096 1.00 55.55  ? 221  ILE A CB    1 
ATOM   1607 C CG1   . ILE A 1 221  ? 171.146 143.168 186.045 1.00 52.39  ? 221  ILE A CG1   1 
ATOM   1608 C CG2   . ILE A 1 221  ? 171.017 145.604 186.636 1.00 51.68  ? 221  ILE A CG2   1 
ATOM   1609 C CD1   . ILE A 1 221  ? 170.475 143.346 184.712 1.00 48.77  ? 221  ILE A CD1   1 
ATOM   1610 N N     . GLU A 1 222  ? 171.744 145.816 189.879 1.00 54.28  ? 222  GLU A N     1 
ATOM   1611 C CA    . GLU A 1 222  ? 171.389 146.799 190.892 1.00 57.57  ? 222  GLU A CA    1 
ATOM   1612 C C     . GLU A 1 222  ? 170.992 148.107 190.219 1.00 57.64  ? 222  GLU A C     1 
ATOM   1613 O O     . GLU A 1 222  ? 171.669 148.569 189.294 1.00 57.40  ? 222  GLU A O     1 
ATOM   1614 C CB    . GLU A 1 222  ? 172.538 147.016 191.882 1.00 60.90  ? 222  GLU A CB    1 
ATOM   1615 C CG    . GLU A 1 222  ? 173.756 147.747 191.336 1.00 72.33  ? 222  GLU A CG    1 
ATOM   1616 C CD    . GLU A 1 222  ? 173.777 149.216 191.720 1.00 73.93  ? 222  GLU A CD    1 
ATOM   1617 O OE1   . GLU A 1 222  ? 173.190 149.566 192.766 1.00 67.04  ? 222  GLU A OE1   1 
ATOM   1618 O OE2   . GLU A 1 222  ? 174.377 150.020 190.977 1.00 68.39  ? 222  GLU A OE2   1 
ATOM   1619 N N     . ILE A 1 223  ? 169.875 148.678 190.661 1.00 55.55  ? 223  ILE A N     1 
ATOM   1620 C CA    . ILE A 1 223  ? 169.386 149.957 190.162 1.00 51.47  ? 223  ILE A CA    1 
ATOM   1621 C C     . ILE A 1 223  ? 169.632 151.011 191.229 1.00 54.73  ? 223  ILE A C     1 
ATOM   1622 O O     . ILE A 1 223  ? 169.290 150.812 192.401 1.00 58.86  ? 223  ILE A O     1 
ATOM   1623 C CB    . ILE A 1 223  ? 167.894 149.886 189.797 1.00 49.37  ? 223  ILE A CB    1 
ATOM   1624 C CG1   . ILE A 1 223  ? 167.684 149.009 188.566 1.00 58.03  ? 223  ILE A CG1   1 
ATOM   1625 C CG2   . ILE A 1 223  ? 167.339 151.276 189.544 1.00 49.60  ? 223  ILE A CG2   1 
ATOM   1626 C CD1   . ILE A 1 223  ? 166.267 149.041 188.041 1.00 61.33  ? 223  ILE A CD1   1 
ATOM   1627 N N     . GLU A 1 224  ? 170.226 152.132 190.828 1.00 47.73  ? 224  GLU A N     1 
ATOM   1628 C CA    . GLU A 1 224  ? 170.517 153.236 191.739 1.00 46.00  ? 224  GLU A CA    1 
ATOM   1629 C C     . GLU A 1 224  ? 170.042 154.537 191.106 1.00 52.94  ? 224  GLU A C     1 
ATOM   1630 O O     . GLU A 1 224  ? 170.718 155.076 190.213 1.00 57.95  ? 224  GLU A O     1 
ATOM   1631 C CB    . GLU A 1 224  ? 172.004 153.300 192.062 1.00 51.57  ? 224  GLU A CB    1 
ATOM   1632 C CG    . GLU A 1 224  ? 172.373 154.341 193.099 1.00 54.64  ? 224  GLU A CG    1 
ATOM   1633 C CD    . GLU A 1 224  ? 173.853 154.341 193.413 1.00 66.10  ? 224  GLU A CD    1 
ATOM   1634 O OE1   . GLU A 1 224  ? 174.634 153.823 192.588 1.00 67.95  ? 224  GLU A OE1   1 
ATOM   1635 O OE2   . GLU A 1 224  ? 174.237 154.851 194.486 1.00 65.99  ? 224  GLU A OE2   1 
ATOM   1636 N N     . PRO A 1 225  ? 168.893 155.065 191.527 1.00 49.82  ? 225  PRO A N     1 
ATOM   1637 C CA    . PRO A 1 225  ? 168.448 156.360 191.003 1.00 45.46  ? 225  PRO A CA    1 
ATOM   1638 C C     . PRO A 1 225  ? 169.413 157.466 191.400 1.00 44.89  ? 225  PRO A C     1 
ATOM   1639 O O     . PRO A 1 225  ? 170.040 157.423 192.460 1.00 46.11  ? 225  PRO A O     1 
ATOM   1640 C CB    . PRO A 1 225  ? 167.071 156.551 191.648 1.00 45.48  ? 225  PRO A CB    1 
ATOM   1641 C CG    . PRO A 1 225  ? 167.109 155.703 192.874 1.00 44.73  ? 225  PRO A CG    1 
ATOM   1642 C CD    . PRO A 1 225  ? 167.958 154.519 192.525 1.00 47.39  ? 225  PRO A CD    1 
ATOM   1643 N N     . HIS A 1 226  ? 169.533 158.465 190.528 1.00 41.40  ? 226  HIS A N     1 
ATOM   1644 C CA    . HIS A 1 226  ? 170.485 159.542 190.745 1.00 46.15  ? 226  HIS A CA    1 
ATOM   1645 C C     . HIS A 1 226  ? 169.900 160.847 190.226 1.00 48.16  ? 226  HIS A C     1 
ATOM   1646 O O     . HIS A 1 226  ? 169.299 160.881 189.149 1.00 51.56  ? 226  HIS A O     1 
ATOM   1647 C CB    . HIS A 1 226  ? 171.822 159.243 190.056 1.00 50.64  ? 226  HIS A CB    1 
ATOM   1648 C CG    . HIS A 1 226  ? 172.955 160.094 190.537 1.00 55.41  ? 226  HIS A CG    1 
ATOM   1649 N ND1   . HIS A 1 226  ? 173.361 161.235 189.880 1.00 57.80  ? 226  HIS A ND1   1 
ATOM   1650 C CD2   . HIS A 1 226  ? 173.772 159.967 191.610 1.00 53.04  ? 226  HIS A CD2   1 
ATOM   1651 C CE1   . HIS A 1 226  ? 174.377 161.776 190.528 1.00 60.65  ? 226  HIS A CE1   1 
ATOM   1652 N NE2   . HIS A 1 226  ? 174.646 161.026 191.582 1.00 61.03  ? 226  HIS A NE2   1 
ATOM   1653 N N     . PHE A 1 227  ? 170.077 161.914 191.000 1.00 45.30  ? 227  PHE A N     1 
ATOM   1654 C CA    . PHE A 1 227  ? 169.630 163.241 190.613 1.00 45.65  ? 227  PHE A CA    1 
ATOM   1655 C C     . PHE A 1 227  ? 170.766 163.989 189.929 1.00 54.99  ? 227  PHE A C     1 
ATOM   1656 O O     . PHE A 1 227  ? 171.887 163.493 189.794 1.00 65.53  ? 227  PHE A O     1 
ATOM   1657 C CB    . PHE A 1 227  ? 169.147 164.043 191.824 1.00 49.87  ? 227  PHE A CB    1 
ATOM   1658 C CG    . PHE A 1 227  ? 168.112 163.346 192.652 1.00 42.86  ? 227  PHE A CG    1 
ATOM   1659 C CD1   . PHE A 1 227  ? 167.237 162.439 192.086 1.00 39.79  ? 227  PHE A CD1   1 
ATOM   1660 C CD2   . PHE A 1 227  ? 168.013 163.611 194.005 1.00 40.39  ? 227  PHE A CD2   1 
ATOM   1661 C CE1   . PHE A 1 227  ? 166.291 161.805 192.856 1.00 40.16  ? 227  PHE A CE1   1 
ATOM   1662 C CE2   . PHE A 1 227  ? 167.071 162.982 194.775 1.00 43.38  ? 227  PHE A CE2   1 
ATOM   1663 C CZ    . PHE A 1 227  ? 166.206 162.079 194.200 1.00 44.65  ? 227  PHE A CZ    1 
ATOM   1664 N N     . GLU A 1 228  ? 170.466 165.212 189.493 1.00 60.45  ? 228  GLU A N     1 
ATOM   1665 C CA    . GLU A 1 228  ? 171.524 166.112 189.052 1.00 63.33  ? 228  GLU A CA    1 
ATOM   1666 C C     . GLU A 1 228  ? 172.399 166.537 190.225 1.00 64.30  ? 228  GLU A C     1 
ATOM   1667 O O     . GLU A 1 228  ? 173.629 166.587 190.104 1.00 66.01  ? 228  GLU A O     1 
ATOM   1668 C CB    . GLU A 1 228  ? 170.920 167.334 188.357 1.00 65.11  ? 228  GLU A CB    1 
ATOM   1669 C CG    . GLU A 1 228  ? 169.807 167.017 187.362 1.00 66.58  ? 228  GLU A CG    1 
ATOM   1670 C CD    . GLU A 1 228  ? 168.426 167.008 188.000 1.00 70.94  ? 228  GLU A CD    1 
ATOM   1671 O OE1   . GLU A 1 228  ? 168.343 166.997 189.246 1.00 66.70  ? 228  GLU A OE1   1 
ATOM   1672 O OE2   . GLU A 1 228  ? 167.424 167.019 187.254 1.00 66.16  ? 228  GLU A OE2   1 
ATOM   1673 N N     . ASP A 1 229  ? 171.784 166.834 191.368 1.00 58.74  ? 229  ASP A N     1 
ATOM   1674 C CA    . ASP A 1 229  ? 172.472 167.322 192.561 1.00 60.15  ? 229  ASP A CA    1 
ATOM   1675 C C     . ASP A 1 229  ? 171.984 166.575 193.797 1.00 57.40  ? 229  ASP A C     1 
ATOM   1676 O O     . ASP A 1 229  ? 171.611 167.170 194.810 1.00 58.27  ? 229  ASP A O     1 
ATOM   1677 C CB    . ASP A 1 229  ? 172.276 168.826 192.720 1.00 61.44  ? 229  ASP A CB    1 
ATOM   1678 C CG    . ASP A 1 229  ? 173.383 169.476 193.528 1.00 70.36  ? 229  ASP A CG    1 
ATOM   1679 O OD1   . ASP A 1 229  ? 173.995 168.784 194.368 1.00 76.39  ? 229  ASP A OD1   1 
ATOM   1680 O OD2   . ASP A 1 229  ? 173.642 170.680 193.322 1.00 69.15  ? 229  ASP A OD2   1 
ATOM   1681 N N     . GLN A 1 230  ? 171.972 165.249 193.716 1.00 53.66  ? 230  GLN A N     1 
ATOM   1682 C CA    . GLN A 1 230  ? 171.445 164.432 194.800 1.00 47.09  ? 230  GLN A CA    1 
ATOM   1683 C C     . GLN A 1 230  ? 172.276 164.617 196.068 1.00 48.22  ? 230  GLN A C     1 
ATOM   1684 O O     . GLN A 1 230  ? 173.509 164.690 195.999 1.00 53.30  ? 230  GLN A O     1 
ATOM   1685 C CB    . GLN A 1 230  ? 171.436 162.958 194.392 1.00 46.17  ? 230  GLN A CB    1 
ATOM   1686 C CG    . GLN A 1 230  ? 171.031 162.002 195.497 1.00 42.43  ? 230  GLN A CG    1 
ATOM   1687 C CD    . GLN A 1 230  ? 171.009 160.563 195.038 1.00 42.02  ? 230  GLN A CD    1 
ATOM   1688 O OE1   . GLN A 1 230  ? 170.700 160.274 193.885 1.00 45.10  ? 230  GLN A OE1   1 
ATOM   1689 N NE2   . GLN A 1 230  ? 171.343 159.649 195.940 1.00 44.30  ? 230  GLN A NE2   1 
ATOM   1690 N N     . PRO A 1 231  ? 171.641 164.696 197.236 1.00 46.15  ? 231  PRO A N     1 
ATOM   1691 C CA    . PRO A 1 231  ? 172.399 164.741 198.490 1.00 44.86  ? 231  PRO A CA    1 
ATOM   1692 C C     . PRO A 1 231  ? 173.161 163.446 198.726 1.00 51.42  ? 231  PRO A C     1 
ATOM   1693 O O     . PRO A 1 231  ? 172.832 162.386 198.190 1.00 58.09  ? 231  PRO A O     1 
ATOM   1694 C CB    . PRO A 1 231  ? 171.318 164.947 199.557 1.00 44.37  ? 231  PRO A CB    1 
ATOM   1695 C CG    . PRO A 1 231  ? 170.153 165.513 198.819 1.00 44.36  ? 231  PRO A CG    1 
ATOM   1696 C CD    . PRO A 1 231  ? 170.199 164.895 197.456 1.00 49.84  ? 231  PRO A CD    1 
ATOM   1697 N N     . ALA A 1 232  ? 174.207 163.552 199.547 1.00 55.41  ? 232  ALA A N     1 
ATOM   1698 C CA    . ALA A 1 232  ? 175.082 162.409 199.786 1.00 56.70  ? 232  ALA A CA    1 
ATOM   1699 C C     . ALA A 1 232  ? 174.364 161.271 200.503 1.00 57.56  ? 232  ALA A C     1 
ATOM   1700 O O     . ALA A 1 232  ? 174.721 160.103 200.314 1.00 57.22  ? 232  ALA A O     1 
ATOM   1701 C CB    . ALA A 1 232  ? 176.308 162.845 200.587 1.00 57.01  ? 232  ALA A CB    1 
ATOM   1702 N N     . ASN A 1 233  ? 173.360 161.582 201.325 1.00 58.39  ? 233  ASN A N     1 
ATOM   1703 C CA    . ASN A 1 233  ? 172.677 160.572 202.127 1.00 54.30  ? 233  ASN A CA    1 
ATOM   1704 C C     . ASN A 1 233  ? 171.210 160.410 201.743 1.00 49.95  ? 233  ASN A C     1 
ATOM   1705 O O     . ASN A 1 233  ? 170.427 159.877 202.534 1.00 47.48  ? 233  ASN A O     1 
ATOM   1706 C CB    . ASN A 1 233  ? 172.794 160.903 203.616 1.00 58.75  ? 233  ASN A CB    1 
ATOM   1707 C CG    . ASN A 1 233  ? 174.228 160.913 204.102 1.00 65.29  ? 233  ASN A CG    1 
ATOM   1708 O OD1   . ASN A 1 233  ? 175.065 160.147 203.624 1.00 65.73  ? 233  ASN A OD1   1 
ATOM   1709 N ND2   . ASN A 1 233  ? 174.520 161.782 205.061 1.00 61.26  ? 233  ASN A ND2   1 
ATOM   1710 N N     . TRP A 1 234  ? 170.814 160.860 200.550 1.00 47.85  ? 234  TRP A N     1 
ATOM   1711 C CA    . TRP A 1 234  ? 169.419 160.712 200.146 1.00 42.40  ? 234  TRP A CA    1 
ATOM   1712 C C     . TRP A 1 234  ? 169.060 159.253 199.899 1.00 42.12  ? 234  TRP A C     1 
ATOM   1713 O O     . TRP A 1 234  ? 167.946 158.823 200.217 1.00 45.70  ? 234  TRP A O     1 
ATOM   1714 C CB    . TRP A 1 234  ? 169.122 161.541 198.898 1.00 39.33  ? 234  TRP A CB    1 
ATOM   1715 C CG    . TRP A 1 234  ? 167.734 161.299 198.380 1.00 40.87  ? 234  TRP A CG    1 
ATOM   1716 C CD1   . TRP A 1 234  ? 166.587 161.905 198.799 1.00 37.34  ? 234  TRP A CD1   1 
ATOM   1717 C CD2   . TRP A 1 234  ? 167.345 160.366 197.364 1.00 40.71  ? 234  TRP A CD2   1 
ATOM   1718 N NE1   . TRP A 1 234  ? 165.510 161.415 198.103 1.00 35.29  ? 234  TRP A NE1   1 
ATOM   1719 C CE2   . TRP A 1 234  ? 165.949 160.469 197.216 1.00 34.68  ? 234  TRP A CE2   1 
ATOM   1720 C CE3   . TRP A 1 234  ? 168.043 159.457 196.564 1.00 39.30  ? 234  TRP A CE3   1 
ATOM   1721 C CZ2   . TRP A 1 234  ? 165.237 159.698 196.302 1.00 33.74  ? 234  TRP A CZ2   1 
ATOM   1722 C CZ3   . TRP A 1 234  ? 167.336 158.695 195.656 1.00 37.79  ? 234  TRP A CZ3   1 
ATOM   1723 C CH2   . TRP A 1 234  ? 165.948 158.821 195.531 1.00 37.46  ? 234  TRP A CH2   1 
ATOM   1724 N N     . LEU A 1 235  ? 169.981 158.482 199.318 1.00 42.98  ? 235  LEU A N     1 
ATOM   1725 C CA    . LEU A 1 235  ? 169.671 157.104 198.951 1.00 41.90  ? 235  LEU A CA    1 
ATOM   1726 C C     . LEU A 1 235  ? 169.403 156.247 200.181 1.00 44.17  ? 235  LEU A C     1 
ATOM   1727 O O     . LEU A 1 235  ? 168.547 155.356 200.148 1.00 47.86  ? 235  LEU A O     1 
ATOM   1728 C CB    . LEU A 1 235  ? 170.811 156.517 198.120 1.00 45.11  ? 235  LEU A CB    1 
ATOM   1729 C CG    . LEU A 1 235  ? 170.503 155.231 197.353 1.00 45.48  ? 235  LEU A CG    1 
ATOM   1730 C CD1   . LEU A 1 235  ? 169.422 155.472 196.314 1.00 43.11  ? 235  LEU A CD1   1 
ATOM   1731 C CD2   . LEU A 1 235  ? 171.761 154.689 196.703 1.00 49.93  ? 235  LEU A CD2   1 
ATOM   1732 N N     . GLY A 1 236  ? 170.120 156.501 201.277 1.00 42.47  ? 236  GLY A N     1 
ATOM   1733 C CA    . GLY A 1 236  ? 169.873 155.749 202.496 1.00 40.91  ? 236  GLY A CA    1 
ATOM   1734 C C     . GLY A 1 236  ? 168.471 155.959 203.033 1.00 46.28  ? 236  GLY A C     1 
ATOM   1735 O O     . GLY A 1 236  ? 167.777 155.003 203.387 1.00 50.92  ? 236  GLY A O     1 
ATOM   1736 N N     . SER A 1 237  ? 168.030 157.218 203.090 1.00 43.85  ? 237  SER A N     1 
ATOM   1737 C CA    . SER A 1 237  ? 166.674 157.508 203.549 1.00 42.88  ? 237  SER A CA    1 
ATOM   1738 C C     . SER A 1 237  ? 165.635 156.980 202.569 1.00 44.51  ? 237  SER A C     1 
ATOM   1739 O O     . SER A 1 237  ? 164.567 156.512 202.979 1.00 48.43  ? 237  SER A O     1 
ATOM   1740 C CB    . SER A 1 237  ? 166.499 159.011 203.758 1.00 45.66  ? 237  SER A CB    1 
ATOM   1741 O OG    . SER A 1 237  ? 166.635 159.714 202.537 1.00 50.50  ? 237  SER A OG    1 
ATOM   1742 N N     . PHE A 1 238  ? 165.930 157.051 201.269 1.00 36.62  ? 238  PHE A N     1 
ATOM   1743 C CA    . PHE A 1 238  ? 165.025 156.505 200.263 1.00 36.56  ? 238  PHE A CA    1 
ATOM   1744 C C     . PHE A 1 238  ? 164.836 155.006 200.454 1.00 41.04  ? 238  PHE A C     1 
ATOM   1745 O O     . PHE A 1 238  ? 163.719 154.491 200.329 1.00 49.88  ? 238  PHE A O     1 
ATOM   1746 C CB    . PHE A 1 238  ? 165.566 156.819 198.867 1.00 37.36  ? 238  PHE A CB    1 
ATOM   1747 C CG    . PHE A 1 238  ? 164.793 156.179 197.748 1.00 40.39  ? 238  PHE A CG    1 
ATOM   1748 C CD1   . PHE A 1 238  ? 163.545 156.655 197.384 1.00 39.96  ? 238  PHE A CD1   1 
ATOM   1749 C CD2   . PHE A 1 238  ? 165.329 155.117 197.041 1.00 41.21  ? 238  PHE A CD2   1 
ATOM   1750 C CE1   . PHE A 1 238  ? 162.840 156.072 196.350 1.00 35.52  ? 238  PHE A CE1   1 
ATOM   1751 C CE2   . PHE A 1 238  ? 164.628 154.530 196.005 1.00 39.53  ? 238  PHE A CE2   1 
ATOM   1752 C CZ    . PHE A 1 238  ? 163.382 155.009 195.660 1.00 32.66  ? 238  PHE A CZ    1 
ATOM   1753 N N     . ASP A 1 239  ? 165.918 154.289 200.763 1.00 41.17  ? 239  ASP A N     1 
ATOM   1754 C CA    . ASP A 1 239  ? 165.816 152.852 200.992 1.00 40.82  ? 239  ASP A CA    1 
ATOM   1755 C C     . ASP A 1 239  ? 165.121 152.542 202.314 1.00 45.37  ? 239  ASP A C     1 
ATOM   1756 O O     . ASP A 1 239  ? 164.331 151.594 202.395 1.00 46.07  ? 239  ASP A O     1 
ATOM   1757 C CB    . ASP A 1 239  ? 167.205 152.216 200.956 1.00 44.97  ? 239  ASP A CB    1 
ATOM   1758 C CG    . ASP A 1 239  ? 167.835 152.272 199.579 1.00 50.42  ? 239  ASP A CG    1 
ATOM   1759 O OD1   . ASP A 1 239  ? 167.164 152.742 198.637 1.00 55.85  ? 239  ASP A OD1   1 
ATOM   1760 O OD2   . ASP A 1 239  ? 169.000 151.846 199.439 1.00 46.05  ? 239  ASP A OD2   1 
ATOM   1761 N N     . LYS A 1 240  ? 165.408 153.321 203.362 1.00 49.36  ? 240  LYS A N     1 
ATOM   1762 C CA    . LYS A 1 240  ? 164.843 153.032 204.678 1.00 49.24  ? 240  LYS A CA    1 
ATOM   1763 C C     . LYS A 1 240  ? 163.325 153.148 204.679 1.00 51.63  ? 240  LYS A C     1 
ATOM   1764 O O     . LYS A 1 240  ? 162.632 152.304 205.260 1.00 52.75  ? 240  LYS A O     1 
ATOM   1765 C CB    . LYS A 1 240  ? 165.434 153.972 205.728 1.00 52.27  ? 240  LYS A CB    1 
ATOM   1766 C CG    . LYS A 1 240  ? 166.881 153.703 206.095 1.00 57.51  ? 240  LYS A CG    1 
ATOM   1767 C CD    . LYS A 1 240  ? 167.315 154.603 207.242 1.00 61.80  ? 240  LYS A CD    1 
ATOM   1768 C CE    . LYS A 1 240  ? 166.935 156.053 206.978 1.00 57.75  ? 240  LYS A CE    1 
ATOM   1769 N NZ    . LYS A 1 240  ? 167.219 156.930 208.146 1.00 57.58  ? 240  LYS A NZ    1 
ATOM   1770 N N     . ASN A 1 241  ? 162.791 154.188 204.046 1.00 50.90  ? 241  ASN A N     1 
ATOM   1771 C CA    . ASN A 1 241  ? 161.356 154.428 204.084 1.00 47.53  ? 241  ASN A CA    1 
ATOM   1772 C C     . ASN A 1 241  ? 160.606 153.363 203.297 1.00 48.51  ? 241  ASN A C     1 
ATOM   1773 O O     . ASN A 1 241  ? 161.056 152.915 202.239 1.00 50.91  ? 241  ASN A O     1 
ATOM   1774 C CB    . ASN A 1 241  ? 161.038 155.815 203.529 1.00 51.75  ? 241  ASN A CB    1 
ATOM   1775 C CG    . ASN A 1 241  ? 161.719 156.921 204.307 1.00 53.42  ? 241  ASN A CG    1 
ATOM   1776 O OD1   . ASN A 1 241  ? 162.251 157.865 203.727 1.00 55.53  ? 241  ASN A OD1   1 
ATOM   1777 N ND2   . ASN A 1 241  ? 161.709 156.806 205.629 1.00 47.18  ? 241  ASN A ND2   1 
ATOM   1778 N N     . LEU A 1 242  ? 159.450 152.956 203.821 1.00 53.42  ? 242  LEU A N     1 
ATOM   1779 C CA    . LEU A 1 242  ? 158.614 151.972 203.147 1.00 58.92  ? 242  LEU A CA    1 
ATOM   1780 C C     . LEU A 1 242  ? 157.888 152.545 201.938 1.00 56.26  ? 242  LEU A C     1 
ATOM   1781 O O     . LEU A 1 242  ? 157.376 151.773 201.120 1.00 55.40  ? 242  LEU A O     1 
ATOM   1782 C CB    . LEU A 1 242  ? 157.591 151.390 204.125 1.00 55.80  ? 242  LEU A CB    1 
ATOM   1783 C CG    . LEU A 1 242  ? 158.148 150.692 205.366 1.00 62.31  ? 242  LEU A CG    1 
ATOM   1784 C CD1   . LEU A 1 242  ? 157.017 150.176 206.239 1.00 66.22  ? 242  LEU A CD1   1 
ATOM   1785 C CD2   . LEU A 1 242  ? 159.084 149.561 204.972 1.00 54.28  ? 242  LEU A CD2   1 
ATOM   1786 N N     . GLN A 1 243  ? 157.827 153.868 201.810 1.00 51.89  ? 243  GLN A N     1 
ATOM   1787 C CA    . GLN A 1 243  ? 157.149 154.518 200.701 1.00 47.98  ? 243  GLN A CA    1 
ATOM   1788 C C     . GLN A 1 243  ? 158.024 155.647 200.183 1.00 47.67  ? 243  GLN A C     1 
ATOM   1789 O O     . GLN A 1 243  ? 158.884 156.170 200.895 1.00 53.98  ? 243  GLN A O     1 
ATOM   1790 C CB    . GLN A 1 243  ? 155.781 155.076 201.118 1.00 53.91  ? 243  GLN A CB    1 
ATOM   1791 C CG    . GLN A 1 243  ? 154.925 154.121 201.928 1.00 56.84  ? 243  GLN A CG    1 
ATOM   1792 C CD    . GLN A 1 243  ? 153.759 154.819 202.594 1.00 62.92  ? 243  GLN A CD    1 
ATOM   1793 O OE1   . GLN A 1 243  ? 153.260 155.829 202.100 1.00 61.38  ? 243  GLN A OE1   1 
ATOM   1794 N NE2   . GLN A 1 243  ? 153.316 154.281 203.725 1.00 60.54  ? 243  GLN A NE2   1 
ATOM   1795 N N     . VAL A 1 244  ? 157.799 156.019 198.929 1.00 43.40  ? 244  VAL A N     1 
ATOM   1796 C CA    . VAL A 1 244  ? 158.469 157.179 198.355 1.00 44.74  ? 244  VAL A CA    1 
ATOM   1797 C C     . VAL A 1 244  ? 157.753 158.435 198.830 1.00 51.83  ? 244  VAL A C     1 
ATOM   1798 O O     . VAL A 1 244  ? 156.529 158.553 198.702 1.00 53.38  ? 244  VAL A O     1 
ATOM   1799 C CB    . VAL A 1 244  ? 158.496 157.093 196.822 1.00 43.27  ? 244  VAL A CB    1 
ATOM   1800 C CG1   . VAL A 1 244  ? 159.155 158.327 196.233 1.00 43.95  ? 244  VAL A CG1   1 
ATOM   1801 C CG2   . VAL A 1 244  ? 159.225 155.839 196.379 1.00 41.20  ? 244  VAL A CG2   1 
ATOM   1802 N N     . HIS A 1 245  ? 158.512 159.372 199.385 1.00 48.66  ? 245  HIS A N     1 
ATOM   1803 C CA    . HIS A 1 245  ? 157.942 160.578 199.960 1.00 42.01  ? 245  HIS A CA    1 
ATOM   1804 C C     . HIS A 1 245  ? 157.948 161.716 198.949 1.00 46.06  ? 245  HIS A C     1 
ATOM   1805 O O     . HIS A 1 245  ? 158.823 161.804 198.084 1.00 49.57  ? 245  HIS A O     1 
ATOM   1806 C CB    . HIS A 1 245  ? 158.714 160.994 201.211 1.00 38.80  ? 245  HIS A CB    1 
ATOM   1807 C CG    . HIS A 1 245  ? 158.653 159.990 202.318 1.00 48.01  ? 245  HIS A CG    1 
ATOM   1808 N ND1   . HIS A 1 245  ? 159.426 160.087 203.455 1.00 51.55  ? 245  HIS A ND1   1 
ATOM   1809 C CD2   . HIS A 1 245  ? 157.909 158.869 202.464 1.00 48.92  ? 245  HIS A CD2   1 
ATOM   1810 C CE1   . HIS A 1 245  ? 159.161 159.068 204.252 1.00 54.51  ? 245  HIS A CE1   1 
ATOM   1811 N NE2   . HIS A 1 245  ? 158.244 158.314 203.674 1.00 52.64  ? 245  HIS A NE2   1 
ATOM   1812 N N     . ASP A 1 246  ? 156.946 162.590 199.064 1.00 48.49  ? 246  ASP A N     1 
ATOM   1813 C CA    . ASP A 1 246  ? 156.930 163.800 198.251 1.00 45.69  ? 246  ASP A CA    1 
ATOM   1814 C C     . ASP A 1 246  ? 158.054 164.746 198.647 1.00 46.20  ? 246  ASP A C     1 
ATOM   1815 O O     . ASP A 1 246  ? 158.471 165.587 197.843 1.00 49.41  ? 246  ASP A O     1 
ATOM   1816 C CB    . ASP A 1 246  ? 155.580 164.506 198.378 1.00 55.80  ? 246  ASP A CB    1 
ATOM   1817 C CG    . ASP A 1 246  ? 154.414 163.610 198.013 1.00 62.39  ? 246  ASP A CG    1 
ATOM   1818 O OD1   . ASP A 1 246  ? 154.646 162.423 197.708 1.00 65.08  ? 246  ASP A OD1   1 
ATOM   1819 O OD2   . ASP A 1 246  ? 153.263 164.095 198.033 1.00 63.91  ? 246  ASP A OD2   1 
ATOM   1820 N N     . SER A 1 247  ? 158.553 164.625 199.875 1.00 44.51  ? 247  SER A N     1 
ATOM   1821 C CA    . SER A 1 247  ? 159.614 165.489 200.367 1.00 38.32  ? 247  SER A CA    1 
ATOM   1822 C C     . SER A 1 247  ? 160.521 164.689 201.289 1.00 37.89  ? 247  SER A C     1 
ATOM   1823 O O     . SER A 1 247  ? 160.045 163.875 202.084 1.00 41.65  ? 247  SER A O     1 
ATOM   1824 C CB    . SER A 1 247  ? 159.047 166.704 201.106 1.00 42.16  ? 247  SER A CB    1 
ATOM   1825 O OG    . SER A 1 247  ? 158.262 166.303 202.216 1.00 46.99  ? 247  SER A OG    1 
ATOM   1826 N N     . TYR A 1 248  ? 161.824 164.931 201.178 1.00 39.17  ? 248  TYR A N     1 
ATOM   1827 C CA    . TYR A 1 248  ? 162.828 164.293 202.016 1.00 34.77  ? 248  TYR A CA    1 
ATOM   1828 C C     . TYR A 1 248  ? 163.657 165.359 202.715 1.00 33.86  ? 248  TYR A C     1 
ATOM   1829 O O     . TYR A 1 248  ? 164.020 166.371 202.110 1.00 43.34  ? 248  TYR A O     1 
ATOM   1830 C CB    . TYR A 1 248  ? 163.752 163.387 201.197 1.00 37.08  ? 248  TYR A CB    1 
ATOM   1831 C CG    . TYR A 1 248  ? 163.119 162.110 200.696 1.00 37.65  ? 248  TYR A CG    1 
ATOM   1832 C CD1   . TYR A 1 248  ? 162.541 162.047 199.437 1.00 38.42  ? 248  TYR A CD1   1 
ATOM   1833 C CD2   . TYR A 1 248  ? 163.118 160.962 201.476 1.00 37.00  ? 248  TYR A CD2   1 
ATOM   1834 C CE1   . TYR A 1 248  ? 161.970 160.880 198.974 1.00 38.32  ? 248  TYR A CE1   1 
ATOM   1835 C CE2   . TYR A 1 248  ? 162.549 159.792 201.022 1.00 39.32  ? 248  TYR A CE2   1 
ATOM   1836 C CZ    . TYR A 1 248  ? 161.978 159.755 199.770 1.00 38.15  ? 248  TYR A CZ    1 
ATOM   1837 O OH    . TYR A 1 248  ? 161.410 158.589 199.315 1.00 41.09  ? 248  TYR A OH    1 
ATOM   1838 N N     . ARG A 1 249  ? 163.955 165.128 203.990 1.00 37.00  ? 249  ARG A N     1 
ATOM   1839 C CA    . ARG A 1 249  ? 164.798 166.015 204.783 1.00 41.97  ? 249  ARG A CA    1 
ATOM   1840 C C     . ARG A 1 249  ? 166.031 165.228 205.212 1.00 48.50  ? 249  ARG A C     1 
ATOM   1841 O O     . ARG A 1 249  ? 165.945 164.353 206.080 1.00 54.32  ? 249  ARG A O     1 
ATOM   1842 C CB    . ARG A 1 249  ? 164.032 166.558 205.987 1.00 48.64  ? 249  ARG A CB    1 
ATOM   1843 C CG    . ARG A 1 249  ? 164.806 167.559 206.825 1.00 59.11  ? 249  ARG A CG    1 
ATOM   1844 C CD    . ARG A 1 249  ? 163.909 168.223 207.858 1.00 66.31  ? 249  ARG A CD    1 
ATOM   1845 N NE    . ARG A 1 249  ? 162.838 168.990 207.232 1.00 77.00  ? 249  ARG A NE    1 
ATOM   1846 C CZ    . ARG A 1 249  ? 161.937 169.703 207.895 1.00 82.50  ? 249  ARG A CZ    1 
ATOM   1847 N NH1   . ARG A 1 249  ? 161.944 169.769 209.216 1.00 83.54  ? 249  ARG A NH1   1 
ATOM   1848 N NH2   . ARG A 1 249  ? 161.006 170.366 207.214 1.00 75.86  ? 249  ARG A NH2   1 
ATOM   1849 N N     . ILE A 1 250  ? 167.174 165.539 204.607 1.00 49.12  ? 250  ILE A N     1 
ATOM   1850 C CA    . ILE A 1 250  ? 168.396 164.766 204.815 1.00 53.00  ? 250  ILE A CA    1 
ATOM   1851 C C     . ILE A 1 250  ? 169.457 165.627 205.491 1.00 60.60  ? 250  ILE A C     1 
ATOM   1852 O O     . ILE A 1 250  ? 170.011 166.536 204.856 1.00 60.80  ? 250  ILE A O     1 
ATOM   1853 C CB    . ILE A 1 250  ? 168.930 164.203 203.489 1.00 45.56  ? 250  ILE A CB    1 
ATOM   1854 C CG1   . ILE A 1 250  ? 167.892 163.290 202.837 1.00 46.25  ? 250  ILE A CG1   1 
ATOM   1855 C CG2   . ILE A 1 250  ? 170.233 163.461 203.712 1.00 49.52  ? 250  ILE A CG2   1 
ATOM   1856 C CD1   . ILE A 1 250  ? 167.294 163.870 201.586 1.00 42.15  ? 250  ILE A CD1   1 
ATOM   1857 N N     . PRO A 1 251  ? 169.762 165.390 206.766 1.00 65.26  ? 251  PRO A N     1 
ATOM   1858 C CA    . PRO A 1 251  ? 170.873 166.110 207.400 1.00 65.16  ? 251  PRO A CA    1 
ATOM   1859 C C     . PRO A 1 251  ? 172.194 165.804 206.708 1.00 65.20  ? 251  PRO A C     1 
ATOM   1860 O O     . PRO A 1 251  ? 172.430 164.687 206.244 1.00 65.50  ? 251  PRO A O     1 
ATOM   1861 C CB    . PRO A 1 251  ? 170.858 165.588 208.841 1.00 71.43  ? 251  PRO A CB    1 
ATOM   1862 C CG    . PRO A 1 251  ? 169.467 165.082 209.047 1.00 67.55  ? 251  PRO A CG    1 
ATOM   1863 C CD    . PRO A 1 251  ? 169.041 164.533 207.721 1.00 64.46  ? 251  PRO A CD    1 
ATOM   1864 N N     . GLY A 1 252  ? 173.058 166.813 206.645 1.00 75.17  ? 252  GLY A N     1 
ATOM   1865 C CA    . GLY A 1 252  ? 174.354 166.694 206.004 1.00 79.10  ? 252  GLY A CA    1 
ATOM   1866 C C     . GLY A 1 252  ? 175.470 166.610 207.028 1.00 85.81  ? 252  GLY A C     1 
ATOM   1867 O O     . GLY A 1 252  ? 175.351 167.129 208.140 1.00 83.93  ? 252  GLY A O     1 
ATOM   1868 N N     . GLU A 1 253  ? 176.564 165.952 206.642 1.00 92.19  ? 253  GLU A N     1 
ATOM   1869 C CA    . GLU A 1 253  ? 177.696 165.769 207.542 1.00 95.68  ? 253  GLU A CA    1 
ATOM   1870 C C     . GLU A 1 253  ? 178.478 167.053 207.786 1.00 98.69  ? 253  GLU A C     1 
ATOM   1871 O O     . GLU A 1 253  ? 179.313 167.083 208.696 1.00 95.01  ? 253  GLU A O     1 
ATOM   1872 C CB    . GLU A 1 253  ? 178.634 164.693 206.993 1.00 93.00  ? 253  GLU A CB    1 
ATOM   1873 C CG    . GLU A 1 253  ? 178.000 163.318 206.878 1.00 91.67  ? 253  GLU A CG    1 
ATOM   1874 C CD    . GLU A 1 253  ? 178.972 162.268 206.377 1.00 95.98  ? 253  GLU A CD    1 
ATOM   1875 O OE1   . GLU A 1 253  ? 180.113 162.633 206.025 1.00 99.62  ? 253  GLU A OE1   1 
ATOM   1876 O OE2   . GLU A 1 253  ? 178.595 161.078 206.339 1.00 92.42  ? 253  GLU A OE2   1 
ATOM   1877 N N     . ASN A 1 254  ? 178.233 168.105 207.005 1.00 95.96  ? 254  ASN A N     1 
ATOM   1878 C CA    . ASN A 1 254  ? 178.923 169.377 207.163 1.00 95.96  ? 254  ASN A CA    1 
ATOM   1879 C C     . ASN A 1 254  ? 178.136 170.361 208.022 1.00 90.79  ? 254  ASN A C     1 
ATOM   1880 O O     . ASN A 1 254  ? 178.353 171.573 207.922 1.00 91.62  ? 254  ASN A O     1 
ATOM   1881 C CB    . ASN A 1 254  ? 179.216 169.992 205.794 1.00 92.56  ? 254  ASN A CB    1 
ATOM   1882 C CG    . ASN A 1 254  ? 180.029 169.072 204.905 1.00 99.23  ? 254  ASN A CG    1 
ATOM   1883 O OD1   . ASN A 1 254  ? 180.758 168.206 205.389 1.00 99.05  ? 254  ASN A OD1   1 
ATOM   1884 N ND2   . ASN A 1 254  ? 179.910 169.258 203.595 1.00 95.02  ? 254  ASN A ND2   1 
ATOM   1885 N N     . GLY A 1 255  ? 177.230 169.866 208.862 1.00 82.44  ? 255  GLY A N     1 
ATOM   1886 C CA    . GLY A 1 255  ? 176.367 170.735 209.631 1.00 78.54  ? 255  GLY A CA    1 
ATOM   1887 C C     . GLY A 1 255  ? 175.238 171.354 208.843 1.00 82.17  ? 255  GLY A C     1 
ATOM   1888 O O     . GLY A 1 255  ? 174.595 172.287 209.337 1.00 76.20  ? 255  GLY A O     1 
ATOM   1889 N N     . GLU A 1 256  ? 174.979 170.866 207.635 1.00 81.43  ? 256  GLU A N     1 
ATOM   1890 C CA    . GLU A 1 256  ? 173.972 171.422 206.750 1.00 70.98  ? 256  GLU A CA    1 
ATOM   1891 C C     . GLU A 1 256  ? 172.711 170.562 206.777 1.00 72.92  ? 256  GLU A C     1 
ATOM   1892 O O     . GLU A 1 256  ? 172.640 169.528 207.445 1.00 74.45  ? 256  GLU A O     1 
ATOM   1893 C CB    . GLU A 1 256  ? 174.528 171.538 205.330 1.00 67.59  ? 256  GLU A CB    1 
ATOM   1894 C CG    . GLU A 1 256  ? 174.954 170.209 204.733 1.00 74.94  ? 256  GLU A CG    1 
ATOM   1895 C CD    . GLU A 1 256  ? 175.676 170.368 203.412 1.00 78.90  ? 256  GLU A CD    1 
ATOM   1896 O OE1   . GLU A 1 256  ? 175.924 171.522 203.006 1.00 78.10  ? 256  GLU A OE1   1 
ATOM   1897 O OE2   . GLU A 1 256  ? 175.996 169.339 202.780 1.00 79.49  ? 256  GLU A OE2   1 
ATOM   1898 N N     . LEU A 1 257  ? 171.699 171.008 206.037 1.00 69.33  ? 257  LEU A N     1 
ATOM   1899 C CA    . LEU A 1 257  ? 170.451 170.277 205.890 1.00 61.97  ? 257  LEU A CA    1 
ATOM   1900 C C     . LEU A 1 257  ? 170.022 170.339 204.433 1.00 58.22  ? 257  LEU A C     1 
ATOM   1901 O O     . LEU A 1 257  ? 170.072 171.403 203.810 1.00 56.67  ? 257  LEU A O     1 
ATOM   1902 C CB    . LEU A 1 257  ? 169.352 170.852 206.792 1.00 59.90  ? 257  LEU A CB    1 
ATOM   1903 C CG    . LEU A 1 257  ? 168.025 170.095 206.825 1.00 59.27  ? 257  LEU A CG    1 
ATOM   1904 C CD1   . LEU A 1 257  ? 168.228 168.699 207.382 1.00 64.26  ? 257  LEU A CD1   1 
ATOM   1905 C CD2   . LEU A 1 257  ? 166.996 170.856 207.643 1.00 60.37  ? 257  LEU A CD2   1 
ATOM   1906 N N     . SER A 1 258  ? 169.606 169.198 203.893 1.00 52.78  ? 258  SER A N     1 
ATOM   1907 C CA    . SER A 1 258  ? 169.227 169.083 202.493 1.00 46.07  ? 258  SER A CA    1 
ATOM   1908 C C     . SER A 1 258  ? 167.765 168.676 202.381 1.00 40.63  ? 258  SER A C     1 
ATOM   1909 O O     . SER A 1 258  ? 167.309 167.765 203.078 1.00 44.55  ? 258  SER A O     1 
ATOM   1910 C CB    . SER A 1 258  ? 170.110 168.067 201.763 1.00 48.27  ? 258  SER A CB    1 
ATOM   1911 O OG    . SER A 1 258  ? 171.479 168.417 201.864 1.00 48.16  ? 258  SER A OG    1 
ATOM   1912 N N     . HIS A 1 259  ? 167.037 169.359 201.503 1.00 40.07  ? 259  HIS A N     1 
ATOM   1913 C CA    . HIS A 1 259  ? 165.639 169.063 201.229 1.00 35.63  ? 259  HIS A CA    1 
ATOM   1914 C C     . HIS A 1 259  ? 165.509 168.582 199.793 1.00 40.02  ? 259  HIS A C     1 
ATOM   1915 O O     . HIS A 1 259  ? 166.103 169.168 198.883 1.00 42.83  ? 259  HIS A O     1 
ATOM   1916 C CB    . HIS A 1 259  ? 164.751 170.291 201.450 1.00 39.17  ? 259  HIS A CB    1 
ATOM   1917 C CG    . HIS A 1 259  ? 164.711 170.764 202.869 1.00 47.08  ? 259  HIS A CG    1 
ATOM   1918 N ND1   . HIS A 1 259  ? 165.665 171.606 203.400 1.00 52.05  ? 259  HIS A ND1   1 
ATOM   1919 C CD2   . HIS A 1 259  ? 163.828 170.520 203.865 1.00 48.39  ? 259  HIS A CD2   1 
ATOM   1920 C CE1   . HIS A 1 259  ? 165.373 171.857 204.664 1.00 51.19  ? 259  HIS A CE1   1 
ATOM   1921 N NE2   . HIS A 1 259  ? 164.263 171.210 204.971 1.00 50.89  ? 259  HIS A NE2   1 
ATOM   1922 N N     . VAL A 1 260  ? 164.737 167.517 199.593 1.00 41.73  ? 260  VAL A N     1 
ATOM   1923 C CA    . VAL A 1 260  ? 164.467 166.970 198.270 1.00 37.06  ? 260  VAL A CA    1 
ATOM   1924 C C     . VAL A 1 260  ? 162.960 166.928 198.073 1.00 37.98  ? 260  VAL A C     1 
ATOM   1925 O O     . VAL A 1 260  ? 162.242 166.324 198.877 1.00 44.25  ? 260  VAL A O     1 
ATOM   1926 C CB    . VAL A 1 260  ? 165.080 165.569 198.092 1.00 33.06  ? 260  VAL A CB    1 
ATOM   1927 C CG1   . VAL A 1 260  ? 164.848 165.069 196.681 1.00 32.82  ? 260  VAL A CG1   1 
ATOM   1928 C CG2   . VAL A 1 260  ? 166.561 165.595 198.406 1.00 38.11  ? 260  VAL A CG2   1 
ATOM   1929 N N     . ILE A 1 261  ? 162.484 167.562 197.005 1.00 35.63  ? 261  ILE A N     1 
ATOM   1930 C CA    . ILE A 1 261  ? 161.066 167.599 196.669 1.00 36.90  ? 261  ILE A CA    1 
ATOM   1931 C C     . ILE A 1 261  ? 160.866 166.775 195.406 1.00 38.17  ? 261  ILE A C     1 
ATOM   1932 O O     . ILE A 1 261  ? 161.480 167.056 194.369 1.00 39.57  ? 261  ILE A O     1 
ATOM   1933 C CB    . ILE A 1 261  ? 160.563 169.038 196.480 1.00 41.63  ? 261  ILE A CB    1 
ATOM   1934 C CG1   . ILE A 1 261  ? 160.692 169.817 197.789 1.00 42.05  ? 261  ILE A CG1   1 
ATOM   1935 C CG2   . ILE A 1 261  ? 159.122 169.037 195.997 1.00 44.42  ? 261  ILE A CG2   1 
ATOM   1936 C CD1   . ILE A 1 261  ? 160.193 171.236 197.704 1.00 43.10  ? 261  ILE A CD1   1 
ATOM   1937 N N     . ILE A 1 262  ? 160.006 165.765 195.488 1.00 38.70  ? 262  ILE A N     1 
ATOM   1938 C CA    . ILE A 1 262  ? 159.841 164.780 194.424 1.00 40.40  ? 262  ILE A CA    1 
ATOM   1939 C C     . ILE A 1 262  ? 158.549 165.103 193.674 1.00 47.60  ? 262  ILE A C     1 
ATOM   1940 O O     . ILE A 1 262  ? 157.458 164.938 194.244 1.00 50.75  ? 262  ILE A O     1 
ATOM   1941 C CB    . ILE A 1 262  ? 159.814 163.352 194.983 1.00 42.37  ? 262  ILE A CB    1 
ATOM   1942 C CG1   . ILE A 1 262  ? 161.083 163.073 195.789 1.00 40.73  ? 262  ILE A CG1   1 
ATOM   1943 C CG2   . ILE A 1 262  ? 159.675 162.349 193.858 1.00 42.72  ? 262  ILE A CG2   1 
ATOM   1944 C CD1   . ILE A 1 262  ? 162.346 163.094 194.964 1.00 38.92  ? 262  ILE A CD1   1 
ATOM   1945 N N     . PRO A 1 263  ? 158.618 165.550 192.424 1.00 48.01  ? 263  PRO A N     1 
ATOM   1946 C CA    . PRO A 1 263  ? 157.400 165.759 191.634 1.00 48.60  ? 263  PRO A CA    1 
ATOM   1947 C C     . PRO A 1 263  ? 156.718 164.437 191.335 1.00 55.02  ? 263  PRO A C     1 
ATOM   1948 O O     . PRO A 1 263  ? 157.364 163.379 191.365 1.00 59.15  ? 263  PRO A O     1 
ATOM   1949 C CB    . PRO A 1 263  ? 157.922 166.420 190.349 1.00 49.64  ? 263  PRO A CB    1 
ATOM   1950 C CG    . PRO A 1 263  ? 159.262 166.958 190.706 1.00 48.17  ? 263  PRO A CG    1 
ATOM   1951 C CD    . PRO A 1 263  ? 159.820 166.009 191.713 1.00 44.32  ? 263  PRO A CD    1 
ATOM   1952 N N     . PRO A 1 264  ? 155.412 164.451 191.053 1.00 56.66  ? 264  PRO A N     1 
ATOM   1953 C CA    . PRO A 1 264  ? 154.709 163.183 190.790 1.00 51.13  ? 264  PRO A CA    1 
ATOM   1954 C C     . PRO A 1 264  ? 155.267 162.395 189.616 1.00 53.70  ? 264  PRO A C     1 
ATOM   1955 O O     . PRO A 1 264  ? 155.272 161.158 189.665 1.00 58.62  ? 264  PRO A O     1 
ATOM   1956 C CB    . PRO A 1 264  ? 153.263 163.631 190.534 1.00 58.08  ? 264  PRO A CB    1 
ATOM   1957 C CG    . PRO A 1 264  ? 153.361 165.074 190.171 1.00 63.06  ? 264  PRO A CG    1 
ATOM   1958 C CD    . PRO A 1 264  ? 154.512 165.611 190.959 1.00 59.13  ? 264  PRO A CD    1 
ATOM   1959 N N     . GLU A 1 265  ? 155.736 163.065 188.560 1.00 53.85  ? 265  GLU A N     1 
ATOM   1960 C CA    . GLU A 1 265  ? 156.321 162.339 187.437 1.00 55.34  ? 265  GLU A CA    1 
ATOM   1961 C C     . GLU A 1 265  ? 157.593 161.612 187.857 1.00 51.03  ? 265  GLU A C     1 
ATOM   1962 O O     . GLU A 1 265  ? 157.833 160.474 187.439 1.00 50.90  ? 265  GLU A O     1 
ATOM   1963 C CB    . GLU A 1 265  ? 156.594 163.287 186.266 1.00 61.93  ? 265  GLU A CB    1 
ATOM   1964 C CG    . GLU A 1 265  ? 157.494 164.475 186.581 1.00 57.58  ? 265  GLU A CG    1 
ATOM   1965 C CD    . GLU A 1 265  ? 156.721 165.694 187.044 1.00 65.24  ? 265  GLU A CD    1 
ATOM   1966 O OE1   . GLU A 1 265  ? 155.494 165.583 187.246 1.00 65.62  ? 265  GLU A OE1   1 
ATOM   1967 O OE2   . GLU A 1 265  ? 157.341 166.767 187.199 1.00 72.98  ? 265  GLU A OE2   1 
ATOM   1968 N N     . VAL A 1 266  ? 158.425 162.259 188.675 1.00 48.53  ? 266  VAL A N     1 
ATOM   1969 C CA    . VAL A 1 266  ? 159.577 161.577 189.251 1.00 43.59  ? 266  VAL A CA    1 
ATOM   1970 C C     . VAL A 1 266  ? 159.130 160.579 190.311 1.00 41.67  ? 266  VAL A C     1 
ATOM   1971 O O     . VAL A 1 266  ? 159.775 159.543 190.511 1.00 46.10  ? 266  VAL A O     1 
ATOM   1972 C CB    . VAL A 1 266  ? 160.573 162.606 189.819 1.00 39.36  ? 266  VAL A CB    1 
ATOM   1973 C CG1   . VAL A 1 266  ? 161.830 161.920 190.323 1.00 39.03  ? 266  VAL A CG1   1 
ATOM   1974 C CG2   . VAL A 1 266  ? 160.916 163.643 188.764 1.00 45.15  ? 266  VAL A CG2   1 
ATOM   1975 N N     . LYS A 1 267  ? 158.025 160.869 191.002 1.00 41.64  ? 267  LYS A N     1 
ATOM   1976 C CA    . LYS A 1 267  ? 157.582 160.005 192.090 1.00 37.96  ? 267  LYS A CA    1 
ATOM   1977 C C     . LYS A 1 267  ? 157.101 158.651 191.589 1.00 43.73  ? 267  LYS A C     1 
ATOM   1978 O O     . LYS A 1 267  ? 157.301 157.646 192.270 1.00 45.26  ? 267  LYS A O     1 
ATOM   1979 C CB    . LYS A 1 267  ? 156.480 160.690 192.896 1.00 45.84  ? 267  LYS A CB    1 
ATOM   1980 C CG    . LYS A 1 267  ? 155.986 159.872 194.075 1.00 50.02  ? 267  LYS A CG    1 
ATOM   1981 C CD    . LYS A 1 267  ? 155.007 160.651 194.927 1.00 49.69  ? 267  LYS A CD    1 
ATOM   1982 C CE    . LYS A 1 267  ? 154.377 159.754 195.974 1.00 49.60  ? 267  LYS A CE    1 
ATOM   1983 N NZ    . LYS A 1 267  ? 155.409 159.008 196.741 1.00 51.10  ? 267  LYS A NZ    1 
ATOM   1984 N N     . GLU A 1 268  ? 156.464 158.595 190.418 1.00 47.13  ? 268  GLU A N     1 
ATOM   1985 C CA    . GLU A 1 268  ? 156.056 157.296 189.884 1.00 42.28  ? 268  GLU A CA    1 
ATOM   1986 C C     . GLU A 1 268  ? 157.266 156.436 189.533 1.00 40.35  ? 268  GLU A C     1 
ATOM   1987 O O     . GLU A 1 268  ? 157.285 155.227 189.812 1.00 41.12  ? 268  GLU A O     1 
ATOM   1988 C CB    . GLU A 1 268  ? 155.154 157.484 188.666 1.00 47.23  ? 268  GLU A CB    1 
ATOM   1989 C CG    . GLU A 1 268  ? 153.787 158.059 188.996 1.00 61.48  ? 268  GLU A CG    1 
ATOM   1990 C CD    . GLU A 1 268  ? 152.763 157.793 187.909 1.00 74.62  ? 268  GLU A CD    1 
ATOM   1991 O OE1   . GLU A 1 268  ? 153.092 157.071 186.944 1.00 69.67  ? 268  GLU A OE1   1 
ATOM   1992 O OE2   . GLU A 1 268  ? 151.629 158.303 188.021 1.00 69.72  ? 268  GLU A OE2   1 
ATOM   1993 N N     . VAL A 1 269  ? 158.289 157.043 188.929 1.00 39.33  ? 269  VAL A N     1 
ATOM   1994 C CA    . VAL A 1 269  ? 159.516 156.314 188.623 1.00 36.51  ? 269  VAL A CA    1 
ATOM   1995 C C     . VAL A 1 269  ? 160.185 155.838 189.905 1.00 36.90  ? 269  VAL A C     1 
ATOM   1996 O O     . VAL A 1 269  ? 160.678 154.706 189.983 1.00 41.81  ? 269  VAL A O     1 
ATOM   1997 C CB    . VAL A 1 269  ? 160.463 157.191 187.785 1.00 37.21  ? 269  VAL A CB    1 
ATOM   1998 C CG1   . VAL A 1 269  ? 161.708 156.411 187.415 1.00 43.01  ? 269  VAL A CG1   1 
ATOM   1999 C CG2   . VAL A 1 269  ? 159.754 157.701 186.541 1.00 35.95  ? 269  VAL A CG2   1 
ATOM   2000 N N     . LEU A 1 270  ? 160.222 156.696 190.926 1.00 34.07  ? 270  LEU A N     1 
ATOM   2001 C CA    . LEU A 1 270  ? 160.812 156.300 192.199 1.00 31.32  ? 270  LEU A CA    1 
ATOM   2002 C C     . LEU A 1 270  ? 159.993 155.220 192.893 1.00 33.28  ? 270  LEU A C     1 
ATOM   2003 O O     . LEU A 1 270  ? 160.554 154.397 193.619 1.00 39.28  ? 270  LEU A O     1 
ATOM   2004 C CB    . LEU A 1 270  ? 160.970 157.516 193.109 1.00 34.65  ? 270  LEU A CB    1 
ATOM   2005 C CG    . LEU A 1 270  ? 162.062 158.508 192.713 1.00 30.63  ? 270  LEU A CG    1 
ATOM   2006 C CD1   . LEU A 1 270  ? 162.169 159.616 193.738 1.00 33.28  ? 270  LEU A CD1   1 
ATOM   2007 C CD2   . LEU A 1 270  ? 163.396 157.800 192.552 1.00 31.87  ? 270  LEU A CD2   1 
ATOM   2008 N N     . ASN A 1 271  ? 158.672 155.214 192.703 1.00 35.25  ? 271  ASN A N     1 
ATOM   2009 C CA    . ASN A 1 271  ? 157.850 154.122 193.212 1.00 33.52  ? 271  ASN A CA    1 
ATOM   2010 C C     . ASN A 1 271  ? 158.216 152.810 192.534 1.00 38.95  ? 271  ASN A C     1 
ATOM   2011 O O     . ASN A 1 271  ? 158.344 151.770 193.190 1.00 41.06  ? 271  ASN A O     1 
ATOM   2012 C CB    . ASN A 1 271  ? 156.366 154.429 192.999 1.00 35.74  ? 271  ASN A CB    1 
ATOM   2013 C CG    . ASN A 1 271  ? 155.833 155.457 193.971 1.00 44.54  ? 271  ASN A CG    1 
ATOM   2014 O OD1   . ASN A 1 271  ? 156.241 155.505 195.129 1.00 51.42  ? 271  ASN A OD1   1 
ATOM   2015 N ND2   . ASN A 1 271  ? 154.906 156.284 193.505 1.00 46.56  ? 271  ASN A ND2   1 
ATOM   2016 N N     . SER A 1 272  ? 158.379 152.842 191.210 1.00 38.91  ? 272  SER A N     1 
ATOM   2017 C CA    . SER A 1 272  ? 158.748 151.628 190.487 1.00 32.34  ? 272  SER A CA    1 
ATOM   2018 C C     . SER A 1 272  ? 160.124 151.127 190.906 1.00 33.64  ? 272  SER A C     1 
ATOM   2019 O O     . SER A 1 272  ? 160.336 149.918 191.051 1.00 38.70  ? 272  SER A O     1 
ATOM   2020 C CB    . SER A 1 272  ? 158.698 151.875 188.982 1.00 33.73  ? 272  SER A CB    1 
ATOM   2021 O OG    . SER A 1 272  ? 157.360 151.874 188.523 1.00 44.67  ? 272  SER A OG    1 
ATOM   2022 N N     . ILE A 1 273  ? 161.075 152.042 191.098 1.00 37.03  ? 273  ILE A N     1 
ATOM   2023 C CA    . ILE A 1 273  ? 162.413 151.652 191.536 1.00 32.67  ? 273  ILE A CA    1 
ATOM   2024 C C     . ILE A 1 273  ? 162.392 151.142 192.972 1.00 35.70  ? 273  ILE A C     1 
ATOM   2025 O O     . ILE A 1 273  ? 163.121 150.205 193.319 1.00 42.50  ? 273  ILE A O     1 
ATOM   2026 C CB    . ILE A 1 273  ? 163.383 152.836 191.366 1.00 31.41  ? 273  ILE A CB    1 
ATOM   2027 C CG1   . ILE A 1 273  ? 163.496 153.217 189.891 1.00 33.39  ? 273  ILE A CG1   1 
ATOM   2028 C CG2   . ILE A 1 273  ? 164.752 152.502 191.930 1.00 38.29  ? 273  ILE A CG2   1 
ATOM   2029 C CD1   . ILE A 1 273  ? 164.278 154.479 189.656 1.00 42.02  ? 273  ILE A CD1   1 
ATOM   2030 N N     . HIS A 1 274  ? 161.557 151.737 193.825 1.00 35.35  ? 274  HIS A N     1 
ATOM   2031 C CA    . HIS A 1 274  ? 161.493 151.367 195.234 1.00 39.42  ? 274  HIS A CA    1 
ATOM   2032 C C     . HIS A 1 274  ? 160.760 150.051 195.450 1.00 43.27  ? 274  HIS A C     1 
ATOM   2033 O O     . HIS A 1 274  ? 161.054 149.336 196.414 1.00 48.25  ? 274  HIS A O     1 
ATOM   2034 C CB    . HIS A 1 274  ? 160.814 152.486 196.027 1.00 42.05  ? 274  HIS A CB    1 
ATOM   2035 C CG    . HIS A 1 274  ? 160.977 152.371 197.510 1.00 42.38  ? 274  HIS A CG    1 
ATOM   2036 N ND1   . HIS A 1 274  ? 160.217 151.517 198.278 1.00 51.74  ? 274  HIS A ND1   1 
ATOM   2037 C CD2   . HIS A 1 274  ? 161.803 153.015 198.368 1.00 40.02  ? 274  HIS A CD2   1 
ATOM   2038 C CE1   . HIS A 1 274  ? 160.573 151.633 199.545 1.00 48.89  ? 274  HIS A CE1   1 
ATOM   2039 N NE2   . HIS A 1 274  ? 161.533 152.536 199.626 1.00 40.32  ? 274  HIS A NE2   1 
ATOM   2040 N N     . SER A 1 275  ? 159.807 149.717 194.577 1.00 40.01  ? 275  SER A N     1 
ATOM   2041 C CA    . SER A 1 275  ? 159.086 148.457 194.704 1.00 43.53  ? 275  SER A CA    1 
ATOM   2042 C C     . SER A 1 275  ? 159.976 147.251 194.436 1.00 46.69  ? 275  SER A C     1 
ATOM   2043 O O     . SER A 1 275  ? 159.611 146.133 194.811 1.00 48.35  ? 275  SER A O     1 
ATOM   2044 C CB    . SER A 1 275  ? 157.887 148.435 193.756 1.00 48.67  ? 275  SER A CB    1 
ATOM   2045 O OG    . SER A 1 275  ? 156.947 149.437 194.102 1.00 54.80  ? 275  SER A OG    1 
ATOM   2046 N N     . ILE A 1 276  ? 161.124 147.450 193.797 1.00 45.98  ? 276  ILE A N     1 
ATOM   2047 C CA    . ILE A 1 276  ? 162.079 146.371 193.564 1.00 46.79  ? 276  ILE A CA    1 
ATOM   2048 C C     . ILE A 1 276  ? 162.803 146.088 194.874 1.00 52.47  ? 276  ILE A C     1 
ATOM   2049 O O     . ILE A 1 276  ? 163.440 146.992 195.436 1.00 51.59  ? 276  ILE A O     1 
ATOM   2050 C CB    . ILE A 1 276  ? 163.063 146.732 192.441 1.00 45.32  ? 276  ILE A CB    1 
ATOM   2051 C CG1   . ILE A 1 276  ? 162.301 147.097 191.168 1.00 41.73  ? 276  ILE A CG1   1 
ATOM   2052 C CG2   . ILE A 1 276  ? 164.013 145.580 192.180 1.00 48.71  ? 276  ILE A CG2   1 
ATOM   2053 C CD1   . ILE A 1 276  ? 163.192 147.495 190.018 1.00 43.66  ? 276  ILE A CD1   1 
ATOM   2054 N N     . PRO A 1 277  ? 162.732 144.864 195.400 1.00 58.63  ? 277  PRO A N     1 
ATOM   2055 C CA    . PRO A 1 277  ? 163.317 144.578 196.721 1.00 57.99  ? 277  PRO A CA    1 
ATOM   2056 C C     . PRO A 1 277  ? 164.829 144.745 196.703 1.00 58.10  ? 277  PRO A C     1 
ATOM   2057 O O     . PRO A 1 277  ? 165.528 144.116 195.906 1.00 61.47  ? 277  PRO A O     1 
ATOM   2058 C CB    . PRO A 1 277  ? 162.912 143.122 196.980 1.00 53.12  ? 277  PRO A CB    1 
ATOM   2059 C CG    . PRO A 1 277  ? 161.752 142.874 196.069 1.00 54.24  ? 277  PRO A CG    1 
ATOM   2060 C CD    . PRO A 1 277  ? 162.018 143.701 194.851 1.00 55.03  ? 277  PRO A CD    1 
ATOM   2061 N N     . GLY A 1 278  ? 165.332 145.599 197.592 1.00 56.18  ? 278  GLY A N     1 
ATOM   2062 C CA    . GLY A 1 278  ? 166.756 145.841 197.687 1.00 55.33  ? 278  GLY A CA    1 
ATOM   2063 C C     . GLY A 1 278  ? 167.367 146.538 196.495 1.00 55.68  ? 278  GLY A C     1 
ATOM   2064 O O     . GLY A 1 278  ? 168.596 146.625 196.415 1.00 57.28  ? 278  GLY A O     1 
ATOM   2065 N N     . ARG A 1 279  ? 166.545 147.041 195.572 1.00 52.57  ? 279  ARG A N     1 
ATOM   2066 C CA    . ARG A 1 279  ? 167.018 147.649 194.329 1.00 52.15  ? 279  ARG A CA    1 
ATOM   2067 C C     . ARG A 1 279  ? 167.939 146.698 193.569 1.00 55.39  ? 279  ARG A C     1 
ATOM   2068 O O     . ARG A 1 279  ? 168.922 147.108 192.953 1.00 54.64  ? 279  ARG A O     1 
ATOM   2069 C CB    . ARG A 1 279  ? 167.707 148.987 194.592 1.00 55.34  ? 279  ARG A CB    1 
ATOM   2070 C CG    . ARG A 1 279  ? 166.774 150.077 195.088 1.00 52.62  ? 279  ARG A CG    1 
ATOM   2071 C CD    . ARG A 1 279  ? 167.464 151.431 195.130 1.00 50.55  ? 279  ARG A CD    1 
ATOM   2072 N NE    . ARG A 1 279  ? 168.555 151.468 196.095 1.00 48.08  ? 279  ARG A NE    1 
ATOM   2073 C CZ    . ARG A 1 279  ? 169.839 151.364 195.781 1.00 49.03  ? 279  ARG A CZ    1 
ATOM   2074 N NH1   . ARG A 1 279  ? 170.234 151.219 194.528 1.00 48.35  ? 279  ARG A NH1   1 
ATOM   2075 N NH2   . ARG A 1 279  ? 170.749 151.407 196.750 1.00 51.64  ? 279  ARG A NH2   1 
ATOM   2076 N N     . ARG A 1 280  ? 167.613 145.409 193.620 1.00 59.33  ? 280  ARG A N     1 
ATOM   2077 C CA    . ARG A 1 280  ? 168.340 144.376 192.896 1.00 54.94  ? 280  ARG A CA    1 
ATOM   2078 C C     . ARG A 1 280  ? 167.388 143.705 191.920 1.00 50.46  ? 280  ARG A C     1 
ATOM   2079 O O     . ARG A 1 280  ? 166.309 143.249 192.311 1.00 48.95  ? 280  ARG A O     1 
ATOM   2080 C CB    . ARG A 1 280  ? 168.950 143.349 193.852 1.00 56.65  ? 280  ARG A CB    1 
ATOM   2081 C CG    . ARG A 1 280  ? 170.125 143.884 194.653 1.00 58.63  ? 280  ARG A CG    1 
ATOM   2082 C CD    . ARG A 1 280  ? 170.674 142.836 195.602 1.00 70.80  ? 280  ARG A CD    1 
ATOM   2083 N NE    . ARG A 1 280  ? 169.674 142.400 196.570 1.00 77.58  ? 280  ARG A NE    1 
ATOM   2084 C CZ    . ARG A 1 280  ? 169.459 142.985 197.740 1.00 81.44  ? 280  ARG A CZ    1 
ATOM   2085 N NH1   . ARG A 1 280  ? 170.158 144.040 198.124 1.00 80.63  ? 280  ARG A NH1   1 
ATOM   2086 N NH2   . ARG A 1 280  ? 168.519 142.499 198.545 1.00 75.77  ? 280  ARG A NH2   1 
ATOM   2087 N N     . VAL A 1 281  ? 167.792 143.646 190.654 1.00 52.93  ? 281  VAL A N     1 
ATOM   2088 C CA    . VAL A 1 281  ? 166.916 143.220 189.570 1.00 51.44  ? 281  VAL A CA    1 
ATOM   2089 C C     . VAL A 1 281  ? 167.075 141.713 189.401 1.00 52.63  ? 281  VAL A C     1 
ATOM   2090 O O     . VAL A 1 281  ? 168.051 141.235 188.823 1.00 55.84  ? 281  VAL A O     1 
ATOM   2091 C CB    . VAL A 1 281  ? 167.221 143.973 188.276 1.00 49.70  ? 281  VAL A CB    1 
ATOM   2092 C CG1   . VAL A 1 281  ? 166.367 143.451 187.145 1.00 47.69  ? 281  VAL A CG1   1 
ATOM   2093 C CG2   . VAL A 1 281  ? 166.997 145.456 188.483 1.00 47.69  ? 281  VAL A CG2   1 
ATOM   2094 N N     . ALA A 1 282  ? 166.103 140.963 189.913 1.00 53.19  ? 282  ALA A N     1 
ATOM   2095 C CA    . ALA A 1 282  ? 166.036 139.523 189.718 1.00 57.95  ? 282  ALA A CA    1 
ATOM   2096 C C     . ALA A 1 282  ? 164.602 139.157 189.378 1.00 59.32  ? 282  ALA A C     1 
ATOM   2097 O O     . ALA A 1 282  ? 163.671 139.602 190.055 1.00 62.02  ? 282  ALA A O     1 
ATOM   2098 C CB    . ALA A 1 282  ? 166.504 138.765 190.965 1.00 50.42  ? 282  ALA A CB    1 
ATOM   2099 N N     . GLY A 1 283  ? 164.426 138.356 188.340 1.00 51.38  ? 283  GLY A N     1 
ATOM   2100 C CA    . GLY A 1 283  ? 163.111 137.958 187.885 1.00 51.44  ? 283  GLY A CA    1 
ATOM   2101 C C     . GLY A 1 283  ? 162.751 138.599 186.556 1.00 52.52  ? 283  GLY A C     1 
ATOM   2102 O O     . GLY A 1 283  ? 163.459 139.452 186.021 1.00 55.26  ? 283  GLY A O     1 
ATOM   2103 N N     . SER A 1 284  ? 161.610 138.159 186.024 1.00 51.32  ? 284  SER A N     1 
ATOM   2104 C CA    . SER A 1 284  ? 161.180 138.613 184.707 1.00 47.89  ? 284  SER A CA    1 
ATOM   2105 C C     . SER A 1 284  ? 160.602 140.023 184.746 1.00 49.41  ? 284  SER A C     1 
ATOM   2106 O O     . SER A 1 284  ? 160.818 140.804 183.815 1.00 49.86  ? 284  SER A O     1 
ATOM   2107 C CB    . SER A 1 284  ? 160.159 137.638 184.128 1.00 54.00  ? 284  SER A CB    1 
ATOM   2108 O OG    . SER A 1 284  ? 160.705 136.334 184.049 1.00 57.44  ? 284  SER A OG    1 
ATOM   2109 N N     . GLU A 1 285  ? 159.868 140.369 185.805 1.00 51.98  ? 285  GLU A N     1 
ATOM   2110 C CA    . GLU A 1 285  ? 159.225 141.680 185.862 1.00 48.40  ? 285  GLU A CA    1 
ATOM   2111 C C     . GLU A 1 285  ? 160.250 142.795 186.037 1.00 46.09  ? 285  GLU A C     1 
ATOM   2112 O O     . GLU A 1 285  ? 160.203 143.813 185.336 1.00 47.26  ? 285  GLU A O     1 
ATOM   2113 C CB    . GLU A 1 285  ? 158.197 141.714 186.993 1.00 46.81  ? 285  GLU A CB    1 
ATOM   2114 C CG    . GLU A 1 285  ? 157.017 140.774 186.805 1.00 50.63  ? 285  GLU A CG    1 
ATOM   2115 C CD    . GLU A 1 285  ? 157.331 139.343 187.193 1.00 58.92  ? 285  GLU A CD    1 
ATOM   2116 O OE1   . GLU A 1 285  ? 158.467 139.078 187.638 1.00 62.55  ? 285  GLU A OE1   1 
ATOM   2117 O OE2   . GLU A 1 285  ? 156.437 138.482 187.054 1.00 63.65  ? 285  GLU A OE2   1 
ATOM   2118 N N     . ALA A 1 286  ? 161.184 142.623 186.975 1.00 45.39  ? 286  ALA A N     1 
ATOM   2119 C CA    . ALA A 1 286  ? 162.204 143.643 187.192 1.00 39.65  ? 286  ALA A CA    1 
ATOM   2120 C C     . ALA A 1 286  ? 163.115 143.781 185.979 1.00 43.70  ? 286  ALA A C     1 
ATOM   2121 O O     . ALA A 1 286  ? 163.479 144.898 185.590 1.00 45.74  ? 286  ALA A O     1 
ATOM   2122 C CB    . ALA A 1 286  ? 163.012 143.312 188.445 1.00 41.34  ? 286  ALA A CB    1 
ATOM   2123 N N     . LEU A 1 287  ? 163.490 142.658 185.363 1.00 42.05  ? 287  LEU A N     1 
ATOM   2124 C CA    . LEU A 1 287  ? 164.322 142.719 184.167 1.00 36.54  ? 287  LEU A CA    1 
ATOM   2125 C C     . LEU A 1 287  ? 163.569 143.315 182.986 1.00 38.22  ? 287  LEU A C     1 
ATOM   2126 O O     . LEU A 1 287  ? 164.185 143.941 182.119 1.00 38.44  ? 287  LEU A O     1 
ATOM   2127 C CB    . LEU A 1 287  ? 164.848 141.327 183.821 1.00 38.50  ? 287  LEU A CB    1 
ATOM   2128 C CG    . LEU A 1 287  ? 166.122 140.890 184.540 1.00 43.63  ? 287  LEU A CG    1 
ATOM   2129 C CD1   . LEU A 1 287  ? 166.365 139.413 184.335 1.00 49.56  ? 287  LEU A CD1   1 
ATOM   2130 C CD2   . LEU A 1 287  ? 167.302 141.695 184.036 1.00 45.10  ? 287  LEU A CD2   1 
ATOM   2131 N N     . SER A 1 288  ? 162.248 143.130 182.926 1.00 38.41  ? 288  SER A N     1 
ATOM   2132 C CA    . SER A 1 288  ? 161.457 143.790 181.893 1.00 33.13  ? 288  SER A CA    1 
ATOM   2133 C C     . SER A 1 288  ? 161.390 145.291 182.133 1.00 33.82  ? 288  SER A C     1 
ATOM   2134 O O     . SER A 1 288  ? 161.407 146.080 181.182 1.00 38.74  ? 288  SER A O     1 
ATOM   2135 C CB    . SER A 1 288  ? 160.053 143.194 181.843 1.00 33.11  ? 288  SER A CB    1 
ATOM   2136 O OG    . SER A 1 288  ? 160.092 141.821 181.514 1.00 39.17  ? 288  SER A OG    1 
ATOM   2137 N N     . PHE A 1 289  ? 161.300 145.700 183.400 1.00 33.87  ? 289  PHE A N     1 
ATOM   2138 C CA    . PHE A 1 289  ? 161.357 147.122 183.720 1.00 34.13  ? 289  PHE A CA    1 
ATOM   2139 C C     . PHE A 1 289  ? 162.701 147.716 183.321 1.00 34.68  ? 289  PHE A C     1 
ATOM   2140 O O     . PHE A 1 289  ? 162.765 148.839 182.809 1.00 37.55  ? 289  PHE A O     1 
ATOM   2141 C CB    . PHE A 1 289  ? 161.096 147.339 185.210 1.00 37.21  ? 289  PHE A CB    1 
ATOM   2142 C CG    . PHE A 1 289  ? 161.189 148.776 185.637 1.00 32.70  ? 289  PHE A CG    1 
ATOM   2143 C CD1   . PHE A 1 289  ? 160.139 149.647 185.410 1.00 32.65  ? 289  PHE A CD1   1 
ATOM   2144 C CD2   . PHE A 1 289  ? 162.326 149.256 186.264 1.00 35.42  ? 289  PHE A CD2   1 
ATOM   2145 C CE1   . PHE A 1 289  ? 160.222 150.967 185.799 1.00 33.58  ? 289  PHE A CE1   1 
ATOM   2146 C CE2   . PHE A 1 289  ? 162.412 150.577 186.654 1.00 35.80  ? 289  PHE A CE2   1 
ATOM   2147 C CZ    . PHE A 1 289  ? 161.359 151.433 186.421 1.00 32.66  ? 289  PHE A CZ    1 
ATOM   2148 N N     . VAL A 1 290  ? 163.786 146.982 183.561 1.00 37.52  ? 290  VAL A N     1 
ATOM   2149 C CA    . VAL A 1 290  ? 165.106 147.448 183.141 1.00 36.35  ? 290  VAL A CA    1 
ATOM   2150 C C     . VAL A 1 290  ? 165.192 147.516 181.621 1.00 34.56  ? 290  VAL A C     1 
ATOM   2151 O O     . VAL A 1 290  ? 165.754 148.463 181.058 1.00 38.25  ? 290  VAL A O     1 
ATOM   2152 C CB    . VAL A 1 290  ? 166.202 146.545 183.733 1.00 38.31  ? 290  VAL A CB    1 
ATOM   2153 C CG1   . VAL A 1 290  ? 167.567 146.947 183.204 1.00 34.52  ? 290  VAL A CG1   1 
ATOM   2154 C CG2   . VAL A 1 290  ? 166.180 146.627 185.239 1.00 36.49  ? 290  VAL A CG2   1 
ATOM   2155 N N     . ARG A 1 291  ? 164.640 146.513 180.935 1.00 33.65  ? 291  ARG A N     1 
ATOM   2156 C CA    . ARG A 1 291  ? 164.672 146.485 179.477 1.00 31.70  ? 291  ARG A CA    1 
ATOM   2157 C C     . ARG A 1 291  ? 163.942 147.683 178.885 1.00 35.57  ? 291  ARG A C     1 
ATOM   2158 O O     . ARG A 1 291  ? 164.477 148.388 178.023 1.00 41.75  ? 291  ARG A O     1 
ATOM   2159 C CB    . ARG A 1 291  ? 164.058 145.178 178.974 1.00 32.60  ? 291  ARG A CB    1 
ATOM   2160 C CG    . ARG A 1 291  ? 163.904 145.089 177.470 1.00 37.90  ? 291  ARG A CG    1 
ATOM   2161 C CD    . ARG A 1 291  ? 163.234 143.791 177.070 1.00 38.08  ? 291  ARG A CD    1 
ATOM   2162 N NE    . ARG A 1 291  ? 162.884 143.769 175.655 1.00 45.54  ? 291  ARG A NE    1 
ATOM   2163 C CZ    . ARG A 1 291  ? 161.738 144.217 175.161 1.00 48.80  ? 291  ARG A CZ    1 
ATOM   2164 N NH1   . ARG A 1 291  ? 160.805 144.736 175.941 1.00 40.04  ? 291  ARG A NH1   1 
ATOM   2165 N NH2   . ARG A 1 291  ? 161.522 144.141 173.851 1.00 48.58  ? 291  ARG A NH2   1 
ATOM   2166 N N     . ASN A 1 292  ? 162.716 147.933 179.343 1.00 34.60  ? 292  ASN A N     1 
ATOM   2167 C CA    . ASN A 1 292  ? 161.912 149.044 178.838 1.00 28.76  ? 292  ASN A CA    1 
ATOM   2168 C C     . ASN A 1 292  ? 161.013 149.534 179.960 1.00 33.42  ? 292  ASN A C     1 
ATOM   2169 O O     . ASN A 1 292  ? 159.901 149.025 180.155 1.00 38.61  ? 292  ASN A O     1 
ATOM   2170 C CB    . ASN A 1 292  ? 161.087 148.633 177.620 1.00 28.90  ? 292  ASN A CB    1 
ATOM   2171 C CG    . ASN A 1 292  ? 160.459 149.815 176.914 1.00 35.89  ? 292  ASN A CG    1 
ATOM   2172 O OD1   . ASN A 1 292  ? 160.894 150.952 177.081 1.00 42.08  ? 292  ASN A OD1   1 
ATOM   2173 N ND2   . ASN A 1 292  ? 159.433 149.552 176.116 1.00 29.73  ? 292  ASN A ND2   1 
ATOM   2174 N N     . PRO A 1 293  ? 161.469 150.521 180.735 1.00 34.45  ? 293  PRO A N     1 
ATOM   2175 C CA    . PRO A 1 293  ? 160.633 151.036 181.830 1.00 32.98  ? 293  PRO A CA    1 
ATOM   2176 C C     . PRO A 1 293  ? 159.447 151.854 181.357 1.00 35.09  ? 293  PRO A C     1 
ATOM   2177 O O     . PRO A 1 293  ? 158.539 152.115 182.155 1.00 38.81  ? 293  PRO A O     1 
ATOM   2178 C CB    . PRO A 1 293  ? 161.612 151.894 182.641 1.00 32.07  ? 293  PRO A CB    1 
ATOM   2179 C CG    . PRO A 1 293  ? 162.631 152.327 181.650 1.00 28.38  ? 293  PRO A CG    1 
ATOM   2180 C CD    . PRO A 1 293  ? 162.774 151.201 180.665 1.00 29.81  ? 293  PRO A CD    1 
ATOM   2181 N N     . TYR A 1 294  ? 159.424 152.263 180.089 1.00 34.12  ? 294  TYR A N     1 
ATOM   2182 C CA    . TYR A 1 294  ? 158.389 153.167 179.607 1.00 30.77  ? 294  TYR A CA    1 
ATOM   2183 C C     . TYR A 1 294  ? 157.065 152.457 179.364 1.00 33.12  ? 294  TYR A C     1 
ATOM   2184 O O     . TYR A 1 294  ? 156.012 153.103 179.381 1.00 41.51  ? 294  TYR A O     1 
ATOM   2185 C CB    . TYR A 1 294  ? 158.881 153.868 178.342 1.00 30.81  ? 294  TYR A CB    1 
ATOM   2186 C CG    . TYR A 1 294  ? 160.238 154.497 178.547 1.00 33.79  ? 294  TYR A CG    1 
ATOM   2187 C CD1   . TYR A 1 294  ? 160.364 155.719 179.188 1.00 38.63  ? 294  TYR A CD1   1 
ATOM   2188 C CD2   . TYR A 1 294  ? 161.395 153.855 178.129 1.00 31.57  ? 294  TYR A CD2   1 
ATOM   2189 C CE1   . TYR A 1 294  ? 161.599 156.291 179.393 1.00 39.06  ? 294  TYR A CE1   1 
ATOM   2190 C CE2   . TYR A 1 294  ? 162.635 154.421 178.330 1.00 31.46  ? 294  TYR A CE2   1 
ATOM   2191 C CZ    . TYR A 1 294  ? 162.729 155.640 178.963 1.00 33.45  ? 294  TYR A CZ    1 
ATOM   2192 O OH    . TYR A 1 294  ? 163.959 156.214 179.171 1.00 41.65  ? 294  TYR A OH    1 
ATOM   2193 N N     . THR A 1 295  ? 157.088 151.143 179.134 1.00 30.77  ? 295  THR A N     1 
ATOM   2194 C CA    . THR A 1 295  ? 155.838 150.394 179.078 1.00 32.03  ? 295  THR A CA    1 
ATOM   2195 C C     . THR A 1 295  ? 155.208 150.258 180.455 1.00 41.79  ? 295  THR A C     1 
ATOM   2196 O O     . THR A 1 295  ? 153.979 150.296 180.582 1.00 45.17  ? 295  THR A O     1 
ATOM   2197 C CB    . THR A 1 295  ? 156.070 149.012 178.471 1.00 30.68  ? 295  THR A CB    1 
ATOM   2198 O OG1   . THR A 1 295  ? 157.220 148.409 179.074 1.00 37.18  ? 295  THR A OG1   1 
ATOM   2199 C CG2   . THR A 1 295  ? 156.292 149.129 176.990 1.00 34.28  ? 295  THR A CG2   1 
ATOM   2200 N N     . PHE A 1 296  ? 156.028 150.092 181.492 1.00 43.31  ? 296  PHE A N     1 
ATOM   2201 C CA    . PHE A 1 296  ? 155.507 149.987 182.847 1.00 34.76  ? 296  PHE A CA    1 
ATOM   2202 C C     . PHE A 1 296  ? 155.054 151.341 183.375 1.00 36.53  ? 296  PHE A C     1 
ATOM   2203 O O     . PHE A 1 296  ? 154.042 151.426 184.077 1.00 45.42  ? 296  PHE A O     1 
ATOM   2204 C CB    . PHE A 1 296  ? 156.564 149.379 183.768 1.00 33.74  ? 296  PHE A CB    1 
ATOM   2205 C CG    . PHE A 1 296  ? 156.875 147.943 183.466 1.00 37.59  ? 296  PHE A CG    1 
ATOM   2206 C CD1   . PHE A 1 296  ? 157.779 147.611 182.474 1.00 33.11  ? 296  PHE A CD1   1 
ATOM   2207 C CD2   . PHE A 1 296  ? 156.263 146.925 184.174 1.00 43.02  ? 296  PHE A CD2   1 
ATOM   2208 C CE1   . PHE A 1 296  ? 158.063 146.291 182.195 1.00 39.77  ? 296  PHE A CE1   1 
ATOM   2209 C CE2   . PHE A 1 296  ? 156.544 145.604 183.899 1.00 38.35  ? 296  PHE A CE2   1 
ATOM   2210 C CZ    . PHE A 1 296  ? 157.443 145.286 182.909 1.00 39.51  ? 296  PHE A CZ    1 
ATOM   2211 N N     . LEU A 1 297  ? 155.784 152.406 183.045 1.00 35.31  ? 297  LEU A N     1 
ATOM   2212 C CA    . LEU A 1 297  ? 155.493 153.729 183.587 1.00 37.99  ? 297  LEU A CA    1 
ATOM   2213 C C     . LEU A 1 297  ? 154.543 154.519 182.690 1.00 42.54  ? 297  LEU A C     1 
ATOM   2214 O O     . LEU A 1 297  ? 153.450 154.902 183.119 1.00 44.58  ? 297  LEU A O     1 
ATOM   2215 C CB    . LEU A 1 297  ? 156.803 154.491 183.804 1.00 34.97  ? 297  LEU A CB    1 
ATOM   2216 C CG    . LEU A 1 297  ? 157.710 153.869 184.865 1.00 32.38  ? 297  LEU A CG    1 
ATOM   2217 C CD1   . LEU A 1 297  ? 159.089 154.501 184.856 1.00 41.40  ? 297  LEU A CD1   1 
ATOM   2218 C CD2   . LEU A 1 297  ? 157.068 154.010 186.229 1.00 36.09  ? 297  LEU A CD2   1 
ATOM   2219 N N     . GLY A 1 298  ? 154.940 154.764 181.450 1.00 42.53  ? 298  GLY A N     1 
ATOM   2220 C CA    . GLY A 1 298  ? 154.118 155.485 180.507 1.00 43.61  ? 298  GLY A CA    1 
ATOM   2221 C C     . GLY A 1 298  ? 154.944 156.495 179.745 1.00 45.89  ? 298  GLY A C     1 
ATOM   2222 O O     . GLY A 1 298  ? 156.171 156.428 179.727 1.00 45.84  ? 298  GLY A O     1 
ATOM   2223 N N     . GLU A 1 299  ? 154.248 157.439 179.108 1.00 52.24  ? 299  GLU A N     1 
ATOM   2224 C CA    . GLU A 1 299  ? 154.923 158.479 178.340 1.00 53.93  ? 299  GLU A CA    1 
ATOM   2225 C C     . GLU A 1 299  ? 155.563 159.536 179.227 1.00 57.28  ? 299  GLU A C     1 
ATOM   2226 O O     . GLU A 1 299  ? 156.458 160.253 178.768 1.00 53.48  ? 299  GLU A O     1 
ATOM   2227 C CB    . GLU A 1 299  ? 153.945 159.142 177.368 1.00 57.59  ? 299  GLU A CB    1 
ATOM   2228 C CG    . GLU A 1 299  ? 152.693 159.709 178.018 1.00 61.46  ? 299  GLU A CG    1 
ATOM   2229 C CD    . GLU A 1 299  ? 151.583 158.684 178.149 1.00 65.71  ? 299  GLU A CD    1 
ATOM   2230 O OE1   . GLU A 1 299  ? 151.820 157.501 177.826 1.00 58.91  ? 299  GLU A OE1   1 
ATOM   2231 O OE2   . GLU A 1 299  ? 150.471 159.062 178.573 1.00 68.50  ? 299  GLU A OE2   1 
ATOM   2232 N N     . ASP A 1 300  ? 155.124 159.656 180.482 1.00 56.79  ? 300  ASP A N     1 
ATOM   2233 C CA    . ASP A 1 300  ? 155.732 160.618 181.391 1.00 51.89  ? 300  ASP A CA    1 
ATOM   2234 C C     . ASP A 1 300  ? 157.143 160.216 181.796 1.00 55.60  ? 300  ASP A C     1 
ATOM   2235 O O     . ASP A 1 300  ? 157.940 161.085 182.164 1.00 58.99  ? 300  ASP A O     1 
ATOM   2236 C CB    . ASP A 1 300  ? 154.862 160.789 182.636 1.00 61.59  ? 300  ASP A CB    1 
ATOM   2237 C CG    . ASP A 1 300  ? 153.444 161.204 182.303 1.00 76.16  ? 300  ASP A CG    1 
ATOM   2238 O OD1   . ASP A 1 300  ? 152.680 160.357 181.793 1.00 71.46  ? 300  ASP A OD1   1 
ATOM   2239 O OD2   . ASP A 1 300  ? 153.092 162.376 182.549 1.00 81.48  ? 300  ASP A OD2   1 
ATOM   2240 N N     . ALA A 1 301  ? 157.467 158.921 181.738 1.00 54.49  ? 301  ALA A N     1 
ATOM   2241 C CA    . ALA A 1 301  ? 158.802 158.468 182.111 1.00 47.11  ? 301  ALA A CA    1 
ATOM   2242 C C     . ALA A 1 301  ? 159.867 158.986 181.155 1.00 50.48  ? 301  ALA A C     1 
ATOM   2243 O O     . ALA A 1 301  ? 161.012 159.202 181.567 1.00 52.88  ? 301  ALA A O     1 
ATOM   2244 C CB    . ALA A 1 301  ? 158.844 156.943 182.164 1.00 40.72  ? 301  ALA A CB    1 
ATOM   2245 N N     . ALA A 1 302  ? 159.517 159.180 179.881 1.00 46.73  ? 302  ALA A N     1 
ATOM   2246 C CA    . ALA A 1 302  ? 160.494 159.656 178.908 1.00 43.68  ? 302  ALA A CA    1 
ATOM   2247 C C     . ALA A 1 302  ? 161.013 161.041 179.264 1.00 50.54  ? 302  ALA A C     1 
ATOM   2248 O O     . ALA A 1 302  ? 162.182 161.351 179.009 1.00 53.05  ? 302  ALA A O     1 
ATOM   2249 C CB    . ALA A 1 302  ? 159.882 159.660 177.509 1.00 48.61  ? 302  ALA A CB    1 
ATOM   2250 N N     . SER A 1 303  ? 160.164 161.887 179.849 1.00 51.33  ? 303  SER A N     1 
ATOM   2251 C CA    . SER A 1 303  ? 160.618 163.187 180.324 1.00 46.34  ? 303  SER A CA    1 
ATOM   2252 C C     . SER A 1 303  ? 161.444 163.076 181.597 1.00 46.62  ? 303  SER A C     1 
ATOM   2253 O O     . SER A 1 303  ? 162.236 163.979 181.888 1.00 45.72  ? 303  SER A O     1 
ATOM   2254 C CB    . SER A 1 303  ? 159.421 164.109 180.557 1.00 50.24  ? 303  SER A CB    1 
ATOM   2255 O OG    . SER A 1 303  ? 158.503 163.531 181.468 1.00 56.19  ? 303  SER A OG    1 
ATOM   2256 N N     . VAL A 1 304  ? 161.281 161.997 182.357 1.00 48.82  ? 304  VAL A N     1 
ATOM   2257 C CA    . VAL A 1 304  ? 162.048 161.796 183.582 1.00 46.75  ? 304  VAL A CA    1 
ATOM   2258 C C     . VAL A 1 304  ? 163.362 161.080 183.299 1.00 50.65  ? 304  VAL A C     1 
ATOM   2259 O O     . VAL A 1 304  ? 164.427 161.515 183.742 1.00 53.14  ? 304  VAL A O     1 
ATOM   2260 C CB    . VAL A 1 304  ? 161.199 161.027 184.616 1.00 42.10  ? 304  VAL A CB    1 
ATOM   2261 C CG1   . VAL A 1 304  ? 161.954 160.895 185.927 1.00 43.63  ? 304  VAL A CG1   1 
ATOM   2262 C CG2   . VAL A 1 304  ? 159.866 161.722 184.826 1.00 44.05  ? 304  VAL A CG2   1 
ATOM   2263 N N     . ILE A 1 305  ? 163.311 159.973 182.565 1.00 47.31  ? 305  ILE A N     1 
ATOM   2264 C CA    . ILE A 1 305  ? 164.501 159.234 182.161 1.00 47.59  ? 305  ILE A CA    1 
ATOM   2265 C C     . ILE A 1 305  ? 164.626 159.347 180.650 1.00 47.86  ? 305  ILE A C     1 
ATOM   2266 O O     . ILE A 1 305  ? 163.714 158.950 179.914 1.00 50.39  ? 305  ILE A O     1 
ATOM   2267 C CB    . ILE A 1 305  ? 164.435 157.762 182.593 1.00 52.91  ? 305  ILE A CB    1 
ATOM   2268 C CG1   . ILE A 1 305  ? 163.877 157.638 184.007 1.00 49.99  ? 305  ILE A CG1   1 
ATOM   2269 C CG2   . ILE A 1 305  ? 165.815 157.127 182.521 1.00 50.88  ? 305  ILE A CG2   1 
ATOM   2270 C CD1   . ILE A 1 305  ? 163.647 156.210 184.424 1.00 49.42  ? 305  ILE A CD1   1 
ATOM   2271 N N     . ALA A 1 306  ? 165.746 159.883 180.189 1.00 47.05  ? 306  ALA A N     1 
ATOM   2272 C CA    . ALA A 1 306  ? 165.969 160.004 178.756 1.00 47.74  ? 306  ALA A CA    1 
ATOM   2273 C C     . ALA A 1 306  ? 166.172 158.620 178.151 1.00 49.16  ? 306  ALA A C     1 
ATOM   2274 O O     . ALA A 1 306  ? 167.015 157.857 178.635 1.00 50.06  ? 306  ALA A O     1 
ATOM   2275 C CB    . ALA A 1 306  ? 167.178 160.892 178.476 1.00 54.13  ? 306  ALA A CB    1 
ATOM   2276 N N     . PRO A 1 307  ? 165.411 158.251 177.116 1.00 49.02  ? 307  PRO A N     1 
ATOM   2277 C CA    . PRO A 1 307  ? 165.579 156.910 176.531 1.00 48.43  ? 307  PRO A CA    1 
ATOM   2278 C C     . PRO A 1 307  ? 166.982 156.640 176.015 1.00 51.25  ? 307  PRO A C     1 
ATOM   2279 O O     . PRO A 1 307  ? 167.481 155.517 176.155 1.00 53.66  ? 307  PRO A O     1 
ATOM   2280 C CB    . PRO A 1 307  ? 164.541 156.897 175.402 1.00 46.99  ? 307  PRO A CB    1 
ATOM   2281 C CG    . PRO A 1 307  ? 163.518 157.897 175.825 1.00 46.97  ? 307  PRO A CG    1 
ATOM   2282 C CD    . PRO A 1 307  ? 164.280 158.979 176.519 1.00 48.27  ? 307  PRO A CD    1 
ATOM   2283 N N     . GLU A 1 308  ? 167.639 157.642 175.428 1.00 51.37  ? 308  GLU A N     1 
ATOM   2284 C CA    . GLU A 1 308  ? 169.010 157.446 174.971 1.00 49.15  ? 308  GLU A CA    1 
ATOM   2285 C C     . GLU A 1 308  ? 169.953 157.222 176.147 1.00 48.92  ? 308  GLU A C     1 
ATOM   2286 O O     . GLU A 1 308  ? 170.872 156.397 176.065 1.00 48.40  ? 308  GLU A O     1 
ATOM   2287 C CB    . GLU A 1 308  ? 169.465 158.637 174.123 1.00 51.32  ? 308  GLU A CB    1 
ATOM   2288 C CG    . GLU A 1 308  ? 169.464 159.988 174.832 1.00 56.91  ? 308  GLU A CG    1 
ATOM   2289 C CD    . GLU A 1 308  ? 168.090 160.627 174.896 1.00 62.50  ? 308  GLU A CD    1 
ATOM   2290 O OE1   . GLU A 1 308  ? 167.114 160.004 174.428 1.00 59.82  ? 308  GLU A OE1   1 
ATOM   2291 O OE2   . GLU A 1 308  ? 167.987 161.759 175.414 1.00 63.82  ? 308  GLU A OE2   1 
ATOM   2292 N N     . GLU A 1 309  ? 169.734 157.933 177.255 1.00 49.88  ? 309  GLU A N     1 
ATOM   2293 C CA    . GLU A 1 309  ? 170.552 157.713 178.442 1.00 47.11  ? 309  GLU A CA    1 
ATOM   2294 C C     . GLU A 1 309  ? 170.312 156.328 179.027 1.00 44.00  ? 309  GLU A C     1 
ATOM   2295 O O     . GLU A 1 309  ? 171.249 155.683 179.508 1.00 46.56  ? 309  GLU A O     1 
ATOM   2296 C CB    . GLU A 1 309  ? 170.275 158.797 179.482 1.00 49.85  ? 309  GLU A CB    1 
ATOM   2297 C CG    . GLU A 1 309  ? 170.692 160.190 179.043 1.00 57.41  ? 309  GLU A CG    1 
ATOM   2298 C CD    . GLU A 1 309  ? 170.539 161.219 180.143 1.00 65.58  ? 309  GLU A CD    1 
ATOM   2299 O OE1   . GLU A 1 309  ? 170.388 160.818 181.317 1.00 66.29  ? 309  GLU A OE1   1 
ATOM   2300 O OE2   . GLU A 1 309  ? 170.567 162.429 179.835 1.00 66.48  ? 309  GLU A OE2   1 
ATOM   2301 N N     . HIS A 1 310  ? 169.066 155.851 178.991 1.00 42.68  ? 310  HIS A N     1 
ATOM   2302 C CA    . HIS A 1 310  ? 168.788 154.497 179.461 1.00 39.66  ? 310  HIS A CA    1 
ATOM   2303 C C     . HIS A 1 310  ? 169.463 153.456 178.578 1.00 42.47  ? 310  HIS A C     1 
ATOM   2304 O O     . HIS A 1 310  ? 169.998 152.462 179.080 1.00 47.00  ? 310  HIS A O     1 
ATOM   2305 C CB    . HIS A 1 310  ? 167.282 154.253 179.519 1.00 37.72  ? 310  HIS A CB    1 
ATOM   2306 C CG    . HIS A 1 310  ? 166.912 152.917 180.084 1.00 40.46  ? 310  HIS A CG    1 
ATOM   2307 N ND1   . HIS A 1 310  ? 167.262 152.527 181.359 1.00 41.73  ? 310  HIS A ND1   1 
ATOM   2308 C CD2   . HIS A 1 310  ? 166.226 151.880 179.549 1.00 40.31  ? 310  HIS A CD2   1 
ATOM   2309 C CE1   . HIS A 1 310  ? 166.806 151.308 181.585 1.00 36.11  ? 310  HIS A CE1   1 
ATOM   2310 N NE2   . HIS A 1 310  ? 166.174 150.893 180.502 1.00 39.42  ? 310  HIS A NE2   1 
ATOM   2311 N N     . GLU A 1 311  ? 169.440 153.661 177.259 1.00 46.38  ? 311  GLU A N     1 
ATOM   2312 C CA    . GLU A 1 311  ? 170.128 152.740 176.359 1.00 44.54  ? 311  GLU A CA    1 
ATOM   2313 C C     . GLU A 1 311  ? 171.630 152.742 176.614 1.00 47.19  ? 311  GLU A C     1 
ATOM   2314 O O     . GLU A 1 311  ? 172.273 151.684 176.606 1.00 49.83  ? 311  GLU A O     1 
ATOM   2315 C CB    . GLU A 1 311  ? 169.830 153.105 174.906 1.00 42.61  ? 311  GLU A CB    1 
ATOM   2316 C CG    . GLU A 1 311  ? 168.375 152.939 174.509 1.00 45.23  ? 311  GLU A CG    1 
ATOM   2317 C CD    . GLU A 1 311  ? 168.062 153.566 173.166 1.00 53.95  ? 311  GLU A CD    1 
ATOM   2318 O OE1   . GLU A 1 311  ? 168.998 154.072 172.513 1.00 54.80  ? 311  GLU A OE1   1 
ATOM   2319 O OE2   . GLU A 1 311  ? 166.879 153.558 172.765 1.00 59.70  ? 311  GLU A OE2   1 
ATOM   2320 N N     . GLN A 1 312  ? 172.208 153.923 176.842 1.00 47.31  ? 312  GLN A N     1 
ATOM   2321 C CA    . GLN A 1 312  ? 173.633 153.998 177.145 1.00 50.09  ? 312  GLN A CA    1 
ATOM   2322 C C     . GLN A 1 312  ? 173.954 153.317 178.470 1.00 51.00  ? 312  GLN A C     1 
ATOM   2323 O O     . GLN A 1 312  ? 175.002 152.677 178.604 1.00 55.39  ? 312  GLN A O     1 
ATOM   2324 C CB    . GLN A 1 312  ? 174.091 155.455 177.162 1.00 54.81  ? 312  GLN A CB    1 
ATOM   2325 C CG    . GLN A 1 312  ? 175.591 155.624 177.336 1.00 55.87  ? 312  GLN A CG    1 
ATOM   2326 C CD    . GLN A 1 312  ? 176.385 154.910 176.261 1.00 61.28  ? 312  GLN A CD    1 
ATOM   2327 O OE1   . GLN A 1 312  ? 177.398 154.272 176.543 1.00 62.03  ? 312  GLN A OE1   1 
ATOM   2328 N NE2   . GLN A 1 312  ? 175.929 155.017 175.018 1.00 60.52  ? 312  GLN A NE2   1 
ATOM   2329 N N     . ALA A 1 313  ? 173.073 153.455 179.463 1.00 49.90  ? 313  ALA A N     1 
ATOM   2330 C CA    . ALA A 1 313  ? 173.272 152.770 180.737 1.00 48.46  ? 313  ALA A CA    1 
ATOM   2331 C C     . ALA A 1 313  ? 173.191 151.258 180.570 1.00 51.18  ? 313  ALA A C     1 
ATOM   2332 O O     . ALA A 1 313  ? 173.946 150.516 181.208 1.00 54.00  ? 313  ALA A O     1 
ATOM   2333 C CB    . ALA A 1 313  ? 172.244 153.253 181.758 1.00 44.74  ? 313  ALA A CB    1 
ATOM   2334 N N     . LEU A 1 314  ? 172.267 150.785 179.733 1.00 49.46  ? 314  LEU A N     1 
ATOM   2335 C CA    . LEU A 1 314  ? 172.182 149.356 179.452 1.00 46.44  ? 314  LEU A CA    1 
ATOM   2336 C C     . LEU A 1 314  ? 173.442 148.856 178.761 1.00 50.51  ? 314  LEU A C     1 
ATOM   2337 O O     . LEU A 1 314  ? 173.940 147.767 179.071 1.00 52.08  ? 314  LEU A O     1 
ATOM   2338 C CB    . LEU A 1 314  ? 170.954 149.061 178.592 1.00 43.55  ? 314  LEU A CB    1 
ATOM   2339 C CG    . LEU A 1 314  ? 169.581 149.131 179.256 1.00 40.67  ? 314  LEU A CG    1 
ATOM   2340 C CD1   . LEU A 1 314  ? 168.490 149.076 178.205 1.00 40.64  ? 314  LEU A CD1   1 
ATOM   2341 C CD2   . LEU A 1 314  ? 169.423 147.996 180.245 1.00 40.16  ? 314  LEU A CD2   1 
ATOM   2342 N N     . PHE A 1 315  ? 173.965 149.633 177.810 1.00 52.82  ? 315  PHE A N     1 
ATOM   2343 C CA    . PHE A 1 315  ? 175.176 149.224 177.105 1.00 53.84  ? 315  PHE A CA    1 
ATOM   2344 C C     . PHE A 1 315  ? 176.386 149.217 178.032 1.00 53.89  ? 315  PHE A C     1 
ATOM   2345 O O     . PHE A 1 315  ? 177.183 148.273 178.012 1.00 57.99  ? 315  PHE A O     1 
ATOM   2346 C CB    . PHE A 1 315  ? 175.422 150.142 175.908 1.00 58.63  ? 315  PHE A CB    1 
ATOM   2347 C CG    . PHE A 1 315  ? 176.627 149.765 175.094 1.00 64.68  ? 315  PHE A CG    1 
ATOM   2348 C CD1   . PHE A 1 315  ? 177.843 150.395 175.298 1.00 67.47  ? 315  PHE A CD1   1 
ATOM   2349 C CD2   . PHE A 1 315  ? 176.545 148.777 174.128 1.00 68.28  ? 315  PHE A CD2   1 
ATOM   2350 C CE1   . PHE A 1 315  ? 178.952 150.048 174.554 1.00 70.31  ? 315  PHE A CE1   1 
ATOM   2351 C CE2   . PHE A 1 315  ? 177.651 148.426 173.380 1.00 72.38  ? 315  PHE A CE2   1 
ATOM   2352 C CZ    . PHE A 1 315  ? 178.856 149.063 173.594 1.00 74.20  ? 315  PHE A CZ    1 
ATOM   2353 N N     . ASP A 1 316  ? 176.539 150.261 178.851 1.00 53.99  ? 316  ASP A N     1 
ATOM   2354 C CA    . ASP A 1 316  ? 177.712 150.376 179.710 1.00 57.95  ? 316  ASP A CA    1 
ATOM   2355 C C     . ASP A 1 316  ? 177.750 149.289 180.775 1.00 56.64  ? 316  ASP A C     1 
ATOM   2356 O O     . ASP A 1 316  ? 178.835 148.888 181.210 1.00 59.25  ? 316  ASP A O     1 
ATOM   2357 C CB    . ASP A 1 316  ? 177.749 151.756 180.366 1.00 60.28  ? 316  ASP A CB    1 
ATOM   2358 C CG    . ASP A 1 316  ? 178.033 152.865 179.375 1.00 67.44  ? 316  ASP A CG    1 
ATOM   2359 O OD1   . ASP A 1 316  ? 178.808 152.630 178.425 1.00 71.63  ? 316  ASP A OD1   1 
ATOM   2360 O OD2   . ASP A 1 316  ? 177.482 153.973 179.545 1.00 65.02  ? 316  ASP A OD2   1 
ATOM   2361 N N     . ALA A 1 317  ? 176.591 148.804 181.207 1.00 53.49  ? 317  ALA A N     1 
ATOM   2362 C CA    . ALA A 1 317  ? 176.513 147.772 182.228 1.00 52.38  ? 317  ALA A CA    1 
ATOM   2363 C C     . ALA A 1 317  ? 176.562 146.368 181.646 1.00 56.54  ? 317  ALA A C     1 
ATOM   2364 O O     . ALA A 1 317  ? 176.364 145.399 182.386 1.00 62.41  ? 317  ALA A O     1 
ATOM   2365 C CB    . ALA A 1 317  ? 175.242 147.948 183.060 1.00 50.65  ? 317  ALA A CB    1 
ATOM   2366 N N     . ARG A 1 318  ? 176.812 146.241 180.340 1.00 54.88  ? 318  ARG A N     1 
ATOM   2367 C CA    . ARG A 1 318  ? 176.873 144.950 179.655 1.00 57.41  ? 318  ARG A CA    1 
ATOM   2368 C C     . ARG A 1 318  ? 175.565 144.176 179.790 1.00 56.23  ? 318  ARG A C     1 
ATOM   2369 O O     . ARG A 1 318  ? 175.564 142.947 179.876 1.00 59.44  ? 318  ARG A O     1 
ATOM   2370 C CB    . ARG A 1 318  ? 178.046 144.102 180.157 1.00 61.31  ? 318  ARG A CB    1 
ATOM   2371 C CG    . ARG A 1 318  ? 179.397 144.799 180.103 1.00 65.37  ? 318  ARG A CG    1 
ATOM   2372 C CD    . ARG A 1 318  ? 179.766 145.192 178.683 1.00 70.39  ? 318  ARG A CD    1 
ATOM   2373 N NE    . ARG A 1 318  ? 179.830 144.037 177.796 1.00 76.45  ? 318  ARG A NE    1 
ATOM   2374 C CZ    . ARG A 1 318  ? 180.158 144.095 176.513 1.00 80.45  ? 318  ARG A CZ    1 
ATOM   2375 N NH1   . ARG A 1 318  ? 180.467 145.242 175.930 1.00 78.78  ? 318  ARG A NH1   1 
ATOM   2376 N NH2   . ARG A 1 318  ? 180.174 142.975 175.796 1.00 73.49  ? 318  ARG A NH2   1 
ATOM   2377 N N     . ILE A 1 319  ? 174.444 144.888 179.812 1.00 51.50  ? 319  ILE A N     1 
ATOM   2378 C CA    . ILE A 1 319  ? 173.126 144.270 179.927 1.00 53.83  ? 319  ILE A CA    1 
ATOM   2379 C C     . ILE A 1 319  ? 172.582 144.159 178.507 1.00 56.13  ? 319  ILE A C     1 
ATOM   2380 O O     . ILE A 1 319  ? 171.974 145.087 177.971 1.00 51.81  ? 319  ILE A O     1 
ATOM   2381 C CB    . ILE A 1 319  ? 172.198 145.063 180.843 1.00 53.87  ? 319  ILE A CB    1 
ATOM   2382 C CG1   . ILE A 1 319  ? 172.853 145.277 182.207 1.00 53.58  ? 319  ILE A CG1   1 
ATOM   2383 C CG2   . ILE A 1 319  ? 170.873 144.338 181.008 1.00 45.16  ? 319  ILE A CG2   1 
ATOM   2384 C CD1   . ILE A 1 319  ? 172.072 146.192 183.115 1.00 46.19  ? 319  ILE A CD1   1 
ATOM   2385 N N     . PHE A 1 320  ? 172.812 143.006 177.888 1.00 61.12  ? 320  PHE A N     1 
ATOM   2386 C CA    . PHE A 1 320  ? 172.319 142.711 176.552 1.00 57.30  ? 320  PHE A CA    1 
ATOM   2387 C C     . PHE A 1 320  ? 171.328 141.562 176.635 1.00 51.30  ? 320  PHE A C     1 
ATOM   2388 O O     . PHE A 1 320  ? 171.591 140.557 177.303 1.00 53.24  ? 320  PHE A O     1 
ATOM   2389 C CB    . PHE A 1 320  ? 173.469 142.359 175.606 1.00 63.50  ? 320  PHE A CB    1 
ATOM   2390 C CG    . PHE A 1 320  ? 174.567 143.379 175.587 1.00 60.48  ? 320  PHE A CG    1 
ATOM   2391 C CD1   . PHE A 1 320  ? 174.381 144.603 174.967 1.00 62.88  ? 320  PHE A CD1   1 
ATOM   2392 C CD2   . PHE A 1 320  ? 175.784 143.116 176.187 1.00 56.10  ? 320  PHE A CD2   1 
ATOM   2393 C CE1   . PHE A 1 320  ? 175.388 145.546 174.949 1.00 61.97  ? 320  PHE A CE1   1 
ATOM   2394 C CE2   . PHE A 1 320  ? 176.794 144.055 176.170 1.00 63.22  ? 320  PHE A CE2   1 
ATOM   2395 C CZ    . PHE A 1 320  ? 176.596 145.271 175.550 1.00 66.98  ? 320  PHE A CZ    1 
ATOM   2396 N N     . PHE A 1 321  ? 170.192 141.714 175.965 1.00 46.86  ? 321  PHE A N     1 
ATOM   2397 C CA    . PHE A 1 321  ? 169.142 140.701 175.977 1.00 52.82  ? 321  PHE A CA    1 
ATOM   2398 C C     . PHE A 1 321  ? 169.347 139.809 174.761 1.00 54.65  ? 321  PHE A C     1 
ATOM   2399 O O     . PHE A 1 321  ? 168.943 140.148 173.647 1.00 56.09  ? 321  PHE A O     1 
ATOM   2400 C CB    . PHE A 1 321  ? 167.767 141.359 175.999 1.00 49.74  ? 321  PHE A CB    1 
ATOM   2401 C CG    . PHE A 1 321  ? 167.478 142.095 177.278 1.00 49.35  ? 321  PHE A CG    1 
ATOM   2402 C CD1   . PHE A 1 321  ? 168.016 143.351 177.506 1.00 47.75  ? 321  PHE A CD1   1 
ATOM   2403 C CD2   . PHE A 1 321  ? 166.683 141.524 178.256 1.00 48.28  ? 321  PHE A CD2   1 
ATOM   2404 C CE1   . PHE A 1 321  ? 167.763 144.024 178.684 1.00 43.15  ? 321  PHE A CE1   1 
ATOM   2405 C CE2   . PHE A 1 321  ? 166.428 142.192 179.435 1.00 44.07  ? 321  PHE A CE2   1 
ATOM   2406 C CZ    . PHE A 1 321  ? 166.969 143.444 179.649 1.00 44.56  ? 321  PHE A CZ    1 
ATOM   2407 N N     . HIS A 1 322  ? 169.985 138.663 174.982 1.00 56.08  ? 322  HIS A N     1 
ATOM   2408 C CA    . HIS A 1 322  ? 170.396 137.794 173.891 1.00 57.86  ? 322  HIS A CA    1 
ATOM   2409 C C     . HIS A 1 322  ? 169.213 137.029 173.310 1.00 55.75  ? 322  HIS A C     1 
ATOM   2410 O O     . HIS A 1 322  ? 168.229 136.742 173.995 1.00 54.05  ? 322  HIS A O     1 
ATOM   2411 C CB    . HIS A 1 322  ? 171.451 136.796 174.372 1.00 62.84  ? 322  HIS A CB    1 
ATOM   2412 C CG    . HIS A 1 322  ? 172.652 137.431 175.000 1.00 63.74  ? 322  HIS A CG    1 
ATOM   2413 N ND1   . HIS A 1 322  ? 172.599 138.100 176.203 1.00 63.47  ? 322  HIS A ND1   1 
ATOM   2414 C CD2   . HIS A 1 322  ? 173.943 137.487 174.596 1.00 65.68  ? 322  HIS A CD2   1 
ATOM   2415 C CE1   . HIS A 1 322  ? 173.803 138.547 176.510 1.00 64.57  ? 322  HIS A CE1   1 
ATOM   2416 N NE2   . HIS A 1 322  ? 174.636 138.189 175.551 1.00 68.41  ? 322  HIS A NE2   1 
ATOM   2417 N N     . HIS A 1 323  ? 169.324 136.697 172.028 1.00 60.36  ? 323  HIS A N     1 
ATOM   2418 C CA    . HIS A 1 323  ? 168.458 135.717 171.392 1.00 59.55  ? 323  HIS A CA    1 
ATOM   2419 C C     . HIS A 1 323  ? 169.151 134.363 171.448 1.00 65.14  ? 323  HIS A C     1 
ATOM   2420 O O     . HIS A 1 323  ? 170.352 134.266 171.178 1.00 69.84  ? 323  HIS A O     1 
ATOM   2421 C CB    . HIS A 1 323  ? 168.149 136.100 169.944 1.00 58.01  ? 323  HIS A CB    1 
ATOM   2422 C CG    . HIS A 1 323  ? 167.234 137.277 169.812 1.00 62.89  ? 323  HIS A CG    1 
ATOM   2423 N ND1   . HIS A 1 323  ? 167.690 138.577 169.806 1.00 67.71  ? 323  HIS A ND1   1 
ATOM   2424 C CD2   . HIS A 1 323  ? 165.889 137.349 169.683 1.00 59.54  ? 323  HIS A CD2   1 
ATOM   2425 C CE1   . HIS A 1 323  ? 166.665 139.400 169.679 1.00 66.84  ? 323  HIS A CE1   1 
ATOM   2426 N NE2   . HIS A 1 323  ? 165.560 138.681 169.602 1.00 62.82  ? 323  HIS A NE2   1 
ATOM   2427 N N     . PHE A 1 324  ? 168.401 133.327 171.803 1.00 64.83  ? 324  PHE A N     1 
ATOM   2428 C CA    . PHE A 1 324  ? 168.969 132.010 172.034 1.00 66.82  ? 324  PHE A CA    1 
ATOM   2429 C C     . PHE A 1 324  ? 168.416 131.006 171.034 1.00 70.29  ? 324  PHE A C     1 
ATOM   2430 O O     . PHE A 1 324  ? 167.293 131.144 170.541 1.00 71.35  ? 324  PHE A O     1 
ATOM   2431 C CB    . PHE A 1 324  ? 168.691 131.527 173.463 1.00 63.98  ? 324  PHE A CB    1 
ATOM   2432 C CG    . PHE A 1 324  ? 167.233 131.409 173.792 1.00 61.18  ? 324  PHE A CG    1 
ATOM   2433 C CD1   . PHE A 1 324  ? 166.532 132.497 174.276 1.00 57.32  ? 324  PHE A CD1   1 
ATOM   2434 C CD2   . PHE A 1 324  ? 166.565 130.209 173.625 1.00 66.03  ? 324  PHE A CD2   1 
ATOM   2435 C CE1   . PHE A 1 324  ? 165.196 132.392 174.581 1.00 58.86  ? 324  PHE A CE1   1 
ATOM   2436 C CE2   . PHE A 1 324  ? 165.224 130.099 173.927 1.00 63.19  ? 324  PHE A CE2   1 
ATOM   2437 C CZ    . PHE A 1 324  ? 164.540 131.193 174.407 1.00 63.54  ? 324  PHE A CZ    1 
ATOM   2438 N N     . ARG A 1 325  ? 169.228 129.996 170.734 1.00 73.35  ? 325  ARG A N     1 
ATOM   2439 C CA    . ARG A 1 325  ? 168.834 128.884 169.881 1.00 78.93  ? 325  ARG A CA    1 
ATOM   2440 C C     . ARG A 1 325  ? 169.255 127.585 170.549 1.00 83.33  ? 325  ARG A C     1 
ATOM   2441 O O     . ARG A 1 325  ? 170.381 127.475 171.043 1.00 86.59  ? 325  ARG A O     1 
ATOM   2442 C CB    . ARG A 1 325  ? 169.463 128.997 168.488 1.00 82.27  ? 325  ARG A CB    1 
ATOM   2443 C CG    . ARG A 1 325  ? 168.998 130.210 167.701 1.00 86.32  ? 325  ARG A CG    1 
ATOM   2444 C CD    . ARG A 1 325  ? 169.668 130.299 166.340 1.00 85.53  ? 325  ARG A CD    1 
ATOM   2445 N NE    . ARG A 1 325  ? 171.108 130.502 166.447 1.00 91.22  ? 325  ARG A NE    1 
ATOM   2446 C CZ    . ARG A 1 325  ? 172.013 129.552 166.261 1.00 94.14  ? 325  ARG A CZ    1 
ATOM   2447 N NH1   . ARG A 1 325  ? 171.662 128.316 165.947 1.00 90.87  ? 325  ARG A NH1   1 
ATOM   2448 N NH2   . ARG A 1 325  ? 173.303 129.850 166.388 1.00 95.70  ? 325  ARG A NH2   1 
ATOM   2449 N N     . LEU A 1 326  ? 168.351 126.608 170.567 1.00 85.79  ? 326  LEU A N     1 
ATOM   2450 C CA    . LEU A 1 326  ? 168.620 125.293 171.138 1.00 88.50  ? 326  LEU A CA    1 
ATOM   2451 C C     . LEU A 1 326  ? 168.869 124.315 169.996 1.00 94.19  ? 326  LEU A C     1 
ATOM   2452 O O     . LEU A 1 326  ? 167.962 124.026 169.209 1.00 94.13  ? 326  LEU A O     1 
ATOM   2453 C CB    . LEU A 1 326  ? 167.459 124.830 172.015 1.00 84.97  ? 326  LEU A CB    1 
ATOM   2454 C CG    . LEU A 1 326  ? 167.303 125.508 173.377 1.00 83.28  ? 326  LEU A CG    1 
ATOM   2455 C CD1   . LEU A 1 326  ? 166.031 125.042 174.061 1.00 79.42  ? 326  LEU A CD1   1 
ATOM   2456 C CD2   . LEU A 1 326  ? 168.511 125.221 174.250 1.00 86.83  ? 326  LEU A CD2   1 
ATOM   2457 N N     . ILE A 1 327  ? 170.094 123.807 169.908 1.00 96.43  ? 327  ILE A N     1 
ATOM   2458 C CA    . ILE A 1 327  ? 170.463 122.873 168.848 1.00 101.58 ? 327  ILE A CA    1 
ATOM   2459 C C     . ILE A 1 327  ? 170.720 121.499 169.455 1.00 106.38 ? 327  ILE A C     1 
ATOM   2460 O O     . ILE A 1 327  ? 171.795 121.268 170.028 1.00 107.52 ? 327  ILE A O     1 
ATOM   2461 C CB    . ILE A 1 327  ? 171.694 123.363 168.072 1.00 103.34 ? 327  ILE A CB    1 
ATOM   2462 C CG1   . ILE A 1 327  ? 171.446 124.755 167.493 1.00 101.09 ? 327  ILE A CG1   1 
ATOM   2463 C CG2   . ILE A 1 327  ? 172.051 122.381 166.966 1.00 105.38 ? 327  ILE A CG2   1 
ATOM   2464 C CD1   . ILE A 1 327  ? 172.597 125.272 166.659 1.00 104.40 ? 327  ILE A CD1   1 
ATOM   2465 N N     . PRO A 1 328  ? 169.775 120.567 169.363 1.00 106.56 ? 328  PRO A N     1 
ATOM   2466 C CA    . PRO A 1 328  ? 170.046 119.206 169.835 1.00 108.24 ? 328  PRO A CA    1 
ATOM   2467 C C     . PRO A 1 328  ? 171.011 118.488 168.906 1.00 111.02 ? 328  PRO A C     1 
ATOM   2468 O O     . PRO A 1 328  ? 170.911 118.583 167.680 1.00 106.99 ? 328  PRO A O     1 
ATOM   2469 C CB    . PRO A 1 328  ? 168.663 118.546 169.828 1.00 108.12 ? 328  PRO A CB    1 
ATOM   2470 C CG    . PRO A 1 328  ? 167.900 119.302 168.793 1.00 106.39 ? 328  PRO A CG    1 
ATOM   2471 C CD    . PRO A 1 328  ? 168.397 120.720 168.867 1.00 103.96 ? 328  PRO A CD    1 
ATOM   2472 N N     . GLN A 1 329  ? 171.954 117.767 169.502 1.00 114.50 ? 329  GLN A N     1 
ATOM   2473 C CA    . GLN A 1 329  ? 172.929 116.984 168.755 1.00 117.73 ? 329  GLN A CA    1 
ATOM   2474 C C     . GLN A 1 329  ? 172.439 115.546 168.659 1.00 120.14 ? 329  GLN A C     1 
ATOM   2475 O O     . GLN A 1 329  ? 172.215 114.891 169.682 1.00 119.48 ? 329  GLN A O     1 
ATOM   2476 C CB    . GLN A 1 329  ? 174.304 117.040 169.422 1.00 113.91 ? 329  GLN A CB    1 
ATOM   2477 C CG    . GLN A 1 329  ? 174.836 118.451 169.624 1.00 110.82 ? 329  GLN A CG    1 
ATOM   2478 C CD    . GLN A 1 329  ? 175.051 119.189 168.318 1.00 114.67 ? 329  GLN A CD    1 
ATOM   2479 O OE1   . GLN A 1 329  ? 175.473 118.602 167.321 1.00 115.95 ? 329  GLN A OE1   1 
ATOM   2480 N NE2   . GLN A 1 329  ? 174.757 120.484 168.315 1.00 110.12 ? 329  GLN A NE2   1 
ATOM   2481 N N     . LEU A 1 330  ? 172.278 115.062 167.433 1.00 120.02 ? 330  LEU A N     1 
ATOM   2482 C CA    . LEU A 1 330  ? 171.679 113.761 167.176 1.00 125.25 ? 330  LEU A CA    1 
ATOM   2483 C C     . LEU A 1 330  ? 172.751 112.683 167.107 1.00 126.94 ? 330  LEU A C     1 
ATOM   2484 O O     . LEU A 1 330  ? 173.842 112.908 166.573 1.00 123.69 ? 330  LEU A O     1 
ATOM   2485 C CB    . LEU A 1 330  ? 170.875 113.784 165.874 1.00 125.22 ? 330  LEU A CB    1 
ATOM   2486 C CG    . LEU A 1 330  ? 169.803 114.872 165.781 1.00 123.44 ? 330  LEU A CG    1 
ATOM   2487 C CD1   . LEU A 1 330  ? 169.042 114.773 164.467 1.00 117.93 ? 330  LEU A CD1   1 
ATOM   2488 C CD2   . LEU A 1 330  ? 168.854 114.792 166.966 1.00 121.17 ? 330  LEU A CD2   1 
ATOM   2489 N N     . ASN A 1 331  ? 172.432 111.512 167.650 1.00 127.01 ? 331  ASN A N     1 
ATOM   2490 C CA    . ASN A 1 331  ? 173.328 110.370 167.612 1.00 124.20 ? 331  ASN A CA    1 
ATOM   2491 C C     . ASN A 1 331  ? 173.049 109.539 166.360 1.00 124.75 ? 331  ASN A C     1 
ATOM   2492 O O     . ASN A 1 331  ? 172.161 109.849 165.561 1.00 122.57 ? 331  ASN A O     1 
ATOM   2493 C CB    . ASN A 1 331  ? 173.178 109.535 168.883 1.00 123.74 ? 331  ASN A CB    1 
ATOM   2494 C CG    . ASN A 1 331  ? 174.396 108.678 169.169 1.00 124.30 ? 331  ASN A CG    1 
ATOM   2495 O OD1   . ASN A 1 331  ? 175.066 108.204 168.252 1.00 126.75 ? 331  ASN A OD1   1 
ATOM   2496 N ND2   . ASN A 1 331  ? 174.690 108.476 170.448 1.00 119.20 ? 331  ASN A ND2   1 
ATOM   2497 N N     . THR A 1 332  ? 173.825 108.467 166.183 1.00 127.50 ? 332  THR A N     1 
ATOM   2498 C CA    . THR A 1 332  ? 173.624 107.586 165.038 1.00 125.65 ? 332  THR A CA    1 
ATOM   2499 C C     . THR A 1 332  ? 172.262 106.904 165.084 1.00 126.57 ? 332  THR A C     1 
ATOM   2500 O O     . THR A 1 332  ? 171.706 106.561 164.035 1.00 121.89 ? 332  THR A O     1 
ATOM   2501 C CB    . THR A 1 332  ? 174.737 106.540 164.977 1.00 124.53 ? 332  THR A CB    1 
ATOM   2502 O OG1   . THR A 1 332  ? 174.754 105.788 166.196 1.00 121.45 ? 332  THR A OG1   1 
ATOM   2503 C CG2   . THR A 1 332  ? 176.087 107.214 164.785 1.00 120.12 ? 332  THR A CG2   1 
ATOM   2504 N N     . GLU A 1 333  ? 171.711 106.701 166.281 1.00 129.49 ? 333  GLU A N     1 
ATOM   2505 C CA    . GLU A 1 333  ? 170.384 106.127 166.449 1.00 128.06 ? 333  GLU A CA    1 
ATOM   2506 C C     . GLU A 1 333  ? 169.298 107.190 166.573 1.00 128.30 ? 333  GLU A C     1 
ATOM   2507 O O     . GLU A 1 333  ? 168.243 106.917 167.157 1.00 124.99 ? 333  GLU A O     1 
ATOM   2508 C CB    . GLU A 1 333  ? 170.360 105.206 167.672 1.00 125.50 ? 333  GLU A CB    1 
ATOM   2509 C CG    . GLU A 1 333  ? 171.335 104.042 167.592 1.00 126.23 ? 333  GLU A CG    1 
ATOM   2510 C CD    . GLU A 1 333  ? 171.255 103.130 168.801 1.00 125.78 ? 333  GLU A CD    1 
ATOM   2511 O OE1   . GLU A 1 333  ? 170.391 103.367 169.670 1.00 126.19 ? 333  GLU A OE1   1 
ATOM   2512 O OE2   . GLU A 1 333  ? 172.058 102.177 168.881 1.00 119.91 ? 333  GLU A OE2   1 
ATOM   2513 N N     . ASN A 1 334  ? 169.534 108.387 166.029 1.00 129.74 ? 334  ASN A N     1 
ATOM   2514 C CA    . ASN A 1 334  ? 168.598 109.509 166.130 1.00 128.58 ? 334  ASN A CA    1 
ATOM   2515 C C     . ASN A 1 334  ? 168.253 109.815 167.586 1.00 128.30 ? 334  ASN A C     1 
ATOM   2516 O O     . ASN A 1 334  ? 167.096 110.062 167.933 1.00 127.36 ? 334  ASN A O     1 
ATOM   2517 C CB    . ASN A 1 334  ? 167.331 109.253 165.310 1.00 126.15 ? 334  ASN A CB    1 
ATOM   2518 C CG    . ASN A 1 334  ? 167.606 109.178 163.822 1.00 122.11 ? 334  ASN A CG    1 
ATOM   2519 O OD1   . ASN A 1 334  ? 168.526 109.821 163.316 1.00 116.10 ? 334  ASN A OD1   1 
ATOM   2520 N ND2   . ASN A 1 334  ? 166.808 108.389 163.112 1.00 121.94 ? 334  ASN A ND2   1 
ATOM   2521 N N     . LYS A 1 335  ? 169.268 109.800 168.445 1.00 125.77 ? 335  LYS A N     1 
ATOM   2522 C CA    . LYS A 1 335  ? 169.108 110.076 169.863 1.00 124.45 ? 335  LYS A CA    1 
ATOM   2523 C C     . LYS A 1 335  ? 169.892 111.325 170.239 1.00 124.25 ? 335  LYS A C     1 
ATOM   2524 O O     . LYS A 1 335  ? 170.908 111.652 169.618 1.00 124.84 ? 335  LYS A O     1 
ATOM   2525 C CB    . LYS A 1 335  ? 169.572 108.891 170.719 1.00 125.28 ? 335  LYS A CB    1 
ATOM   2526 C CG    . LYS A 1 335  ? 168.740 107.633 170.540 1.00 126.86 ? 335  LYS A CG    1 
ATOM   2527 C CD    . LYS A 1 335  ? 169.208 106.528 171.472 1.00 127.12 ? 335  LYS A CD    1 
ATOM   2528 C CE    . LYS A 1 335  ? 168.330 105.294 171.351 1.00 127.19 ? 335  LYS A CE    1 
ATOM   2529 N NZ    . LYS A 1 335  ? 168.774 104.205 172.264 1.00 120.79 ? 335  LYS A NZ    1 
ATOM   2530 N N     . ILE A 1 336  ? 169.409 112.023 171.260 1.00 123.76 ? 336  ILE A N     1 
ATOM   2531 C CA    . ILE A 1 336  ? 170.026 113.270 171.695 1.00 122.76 ? 336  ILE A CA    1 
ATOM   2532 C C     . ILE A 1 336  ? 171.229 112.956 172.574 1.00 122.68 ? 336  ILE A C     1 
ATOM   2533 O O     . ILE A 1 336  ? 171.119 112.220 173.562 1.00 119.79 ? 336  ILE A O     1 
ATOM   2534 C CB    . ILE A 1 336  ? 169.009 114.147 172.441 1.00 119.00 ? 336  ILE A CB    1 
ATOM   2535 C CG1   . ILE A 1 336  ? 167.831 114.485 171.528 1.00 117.01 ? 336  ILE A CG1   1 
ATOM   2536 C CG2   . ILE A 1 336  ? 169.672 115.418 172.948 1.00 118.19 ? 336  ILE A CG2   1 
ATOM   2537 C CD1   . ILE A 1 336  ? 166.771 115.326 172.195 1.00 113.77 ? 336  ILE A CD1   1 
ATOM   2538 N N     . THR A 1 337  ? 172.384 113.516 172.214 1.00 120.74 ? 337  THR A N     1 
ATOM   2539 C CA    . THR A 1 337  ? 173.600 113.398 173.009 1.00 118.79 ? 337  THR A CA    1 
ATOM   2540 C C     . THR A 1 337  ? 173.810 114.605 173.915 1.00 121.26 ? 337  THR A C     1 
ATOM   2541 O O     . THR A 1 337  ? 174.077 114.446 175.110 1.00 119.23 ? 337  THR A O     1 
ATOM   2542 C CB    . THR A 1 337  ? 174.817 113.217 172.095 1.00 116.84 ? 337  THR A CB    1 
ATOM   2543 O OG1   . THR A 1 337  ? 174.909 114.325 171.192 1.00 117.74 ? 337  THR A OG1   1 
ATOM   2544 C CG2   . THR A 1 337  ? 174.700 111.927 171.298 1.00 119.26 ? 337  THR A CG2   1 
ATOM   2545 N N     . GLU A 1 338  ? 173.699 115.811 173.365 1.00 118.74 ? 338  GLU A N     1 
ATOM   2546 C CA    . GLU A 1 338  ? 173.781 117.031 174.153 1.00 113.38 ? 338  GLU A CA    1 
ATOM   2547 C C     . GLU A 1 338  ? 173.073 118.144 173.396 1.00 112.10 ? 338  GLU A C     1 
ATOM   2548 O O     . GLU A 1 338  ? 172.958 118.101 172.169 1.00 112.32 ? 338  GLU A O     1 
ATOM   2549 C CB    . GLU A 1 338  ? 175.235 117.414 174.452 1.00 109.77 ? 338  GLU A CB    1 
ATOM   2550 C CG    . GLU A 1 338  ? 176.122 117.538 173.223 1.00 112.10 ? 338  GLU A CG    1 
ATOM   2551 C CD    . GLU A 1 338  ? 176.397 118.980 172.841 1.00 117.51 ? 338  GLU A CD    1 
ATOM   2552 O OE1   . GLU A 1 338  ? 175.867 119.887 173.516 1.00 113.45 ? 338  GLU A OE1   1 
ATOM   2553 O OE2   . GLU A 1 338  ? 177.146 119.205 171.867 1.00 117.22 ? 338  GLU A OE2   1 
ATOM   2554 N N     . VAL A 1 339  ? 172.596 119.136 174.143 1.00 110.13 ? 339  VAL A N     1 
ATOM   2555 C CA    . VAL A 1 339  ? 171.897 120.288 173.586 1.00 104.32 ? 339  VAL A CA    1 
ATOM   2556 C C     . VAL A 1 339  ? 172.777 121.514 173.778 1.00 102.68 ? 339  VAL A C     1 
ATOM   2557 O O     . VAL A 1 339  ? 173.219 121.799 174.897 1.00 103.34 ? 339  VAL A O     1 
ATOM   2558 C CB    . VAL A 1 339  ? 170.522 120.488 174.246 1.00 102.74 ? 339  VAL A CB    1 
ATOM   2559 C CG1   . VAL A 1 339  ? 169.854 121.743 173.712 1.00 98.44  ? 339  VAL A CG1   1 
ATOM   2560 C CG2   . VAL A 1 339  ? 169.641 119.273 174.009 1.00 107.07 ? 339  VAL A CG2   1 
ATOM   2561 N N     . THR A 1 340  ? 173.033 122.234 172.691 1.00 101.17 ? 340  THR A N     1 
ATOM   2562 C CA    . THR A 1 340  ? 173.890 123.411 172.721 1.00 100.68 ? 340  THR A CA    1 
ATOM   2563 C C     . THR A 1 340  ? 173.032 124.668 172.696 1.00 96.62  ? 340  THR A C     1 
ATOM   2564 O O     . THR A 1 340  ? 172.204 124.845 171.797 1.00 98.06  ? 340  THR A O     1 
ATOM   2565 C CB    . THR A 1 340  ? 174.865 123.414 171.543 1.00 101.01 ? 340  THR A CB    1 
ATOM   2566 O OG1   . THR A 1 340  ? 175.654 122.218 171.569 1.00 103.07 ? 340  THR A OG1   1 
ATOM   2567 C CG2   . THR A 1 340  ? 175.789 124.618 171.625 1.00 94.95  ? 340  THR A CG2   1 
ATOM   2568 N N     . LEU A 1 341  ? 173.235 125.535 173.684 1.00 90.41  ? 341  LEU A N     1 
ATOM   2569 C CA    . LEU A 1 341  ? 172.512 126.794 173.794 1.00 82.91  ? 341  LEU A CA    1 
ATOM   2570 C C     . LEU A 1 341  ? 173.434 127.931 173.375 1.00 84.84  ? 341  LEU A C     1 
ATOM   2571 O O     . LEU A 1 341  ? 174.430 128.207 174.051 1.00 88.70  ? 341  LEU A O     1 
ATOM   2572 C CB    . LEU A 1 341  ? 172.015 127.011 175.222 1.00 82.89  ? 341  LEU A CB    1 
ATOM   2573 C CG    . LEU A 1 341  ? 171.377 128.370 175.509 1.00 80.59  ? 341  LEU A CG    1 
ATOM   2574 C CD1   . LEU A 1 341  ? 170.042 128.486 174.802 1.00 76.04  ? 341  LEU A CD1   1 
ATOM   2575 C CD2   . LEU A 1 341  ? 171.223 128.588 177.004 1.00 78.48  ? 341  LEU A CD2   1 
ATOM   2576 N N     . ILE A 1 342  ? 173.097 128.592 172.272 1.00 80.17  ? 342  ILE A N     1 
ATOM   2577 C CA    . ILE A 1 342  ? 173.888 129.693 171.736 1.00 79.64  ? 342  ILE A CA    1 
ATOM   2578 C C     . ILE A 1 342  ? 173.140 130.987 172.016 1.00 74.24  ? 342  ILE A C     1 
ATOM   2579 O O     . ILE A 1 342  ? 171.993 131.154 171.586 1.00 76.91  ? 342  ILE A O     1 
ATOM   2580 C CB    . ILE A 1 342  ? 174.154 129.529 170.231 1.00 83.05  ? 342  ILE A CB    1 
ATOM   2581 C CG1   . ILE A 1 342  ? 174.910 128.229 169.951 1.00 88.58  ? 342  ILE A CG1   1 
ATOM   2582 C CG2   . ILE A 1 342  ? 174.927 130.722 169.695 1.00 80.36  ? 342  ILE A CG2   1 
ATOM   2583 C CD1   . ILE A 1 342  ? 174.016 127.075 169.553 1.00 90.14  ? 342  ILE A CD1   1 
ATOM   2584 N N     . LEU A 1 343  ? 173.787 131.900 172.733 1.00 75.59  ? 343  LEU A N     1 
ATOM   2585 C CA    . LEU A 1 343  ? 173.215 133.202 173.048 1.00 70.08  ? 343  LEU A CA    1 
ATOM   2586 C C     . LEU A 1 343  ? 173.775 134.229 172.073 1.00 73.19  ? 343  LEU A C     1 
ATOM   2587 O O     . LEU A 1 343  ? 174.990 134.449 172.026 1.00 81.05  ? 343  LEU A O     1 
ATOM   2588 C CB    . LEU A 1 343  ? 173.527 133.600 174.490 1.00 72.96  ? 343  LEU A CB    1 
ATOM   2589 C CG    . LEU A 1 343  ? 173.145 132.592 175.575 1.00 76.07  ? 343  LEU A CG    1 
ATOM   2590 C CD1   . LEU A 1 343  ? 173.460 133.147 176.951 1.00 80.67  ? 343  LEU A CD1   1 
ATOM   2591 C CD2   . LEU A 1 343  ? 171.678 132.213 175.475 1.00 67.96  ? 343  LEU A CD2   1 
ATOM   2592 N N     . GLU A 1 344  ? 172.890 134.859 171.301 1.00 69.77  ? 344  GLU A N     1 
ATOM   2593 C CA    . GLU A 1 344  ? 173.306 135.815 170.283 1.00 73.76  ? 344  GLU A CA    1 
ATOM   2594 C C     . GLU A 1 344  ? 173.200 137.225 170.846 1.00 75.77  ? 344  GLU A C     1 
ATOM   2595 O O     . GLU A 1 344  ? 172.079 137.701 171.083 1.00 76.35  ? 344  GLU A O     1 
ATOM   2596 C CB    . GLU A 1 344  ? 172.446 135.674 169.037 1.00 73.98  ? 344  GLU A CB    1 
ATOM   2597 C CG    . GLU A 1 344  ? 172.464 134.282 168.435 1.00 77.28  ? 344  GLU A CG    1 
ATOM   2598 C CD    . GLU A 1 344  ? 171.465 134.122 167.308 1.00 79.13  ? 344  GLU A CD    1 
ATOM   2599 O OE1   . GLU A 1 344  ? 170.659 135.050 167.090 1.00 78.93  ? 344  GLU A OE1   1 
ATOM   2600 O OE2   . GLU A 1 344  ? 171.487 133.067 166.640 1.00 80.29  ? 344  GLU A OE2   1 
ATOM   2601 N N     . PRO A 1 345  ? 174.311 137.926 171.067 1.00 81.86  ? 345  PRO A N     1 
ATOM   2602 C CA    . PRO A 1 345  ? 174.235 139.257 171.681 1.00 83.50  ? 345  PRO A CA    1 
ATOM   2603 C C     . PRO A 1 345  ? 173.503 140.254 170.797 1.00 82.46  ? 345  PRO A C     1 
ATOM   2604 O O     . PRO A 1 345  ? 173.613 140.224 169.569 1.00 77.25  ? 345  PRO A O     1 
ATOM   2605 C CB    . PRO A 1 345  ? 175.706 139.647 171.863 1.00 88.33  ? 345  PRO A CB    1 
ATOM   2606 C CG    . PRO A 1 345  ? 176.431 138.851 170.828 1.00 90.49  ? 345  PRO A CG    1 
ATOM   2607 C CD    . PRO A 1 345  ? 175.693 137.549 170.727 1.00 87.30  ? 345  PRO A CD    1 
ATOM   2608 N N     . VAL A 1 346  ? 172.756 141.148 171.440 1.00 77.84  ? 346  VAL A N     1 
ATOM   2609 C CA    . VAL A 1 346  ? 172.025 142.211 170.761 1.00 84.43  ? 346  VAL A CA    1 
ATOM   2610 C C     . VAL A 1 346  ? 172.662 143.537 171.153 1.00 85.32  ? 346  VAL A C     1 
ATOM   2611 O O     . VAL A 1 346  ? 172.689 143.896 172.337 1.00 78.17  ? 346  VAL A O     1 
ATOM   2612 C CB    . VAL A 1 346  ? 170.530 142.188 171.112 1.00 83.47  ? 346  VAL A CB    1 
ATOM   2613 C CG1   . VAL A 1 346  ? 169.810 143.348 170.442 1.00 71.86  ? 346  VAL A CG1   1 
ATOM   2614 C CG2   . VAL A 1 346  ? 169.916 140.866 170.693 1.00 79.23  ? 346  VAL A CG2   1 
ATOM   2615 N N     . SER A 1 347  ? 173.164 144.261 170.160 1.00 83.75  ? 347  SER A N     1 
ATOM   2616 C CA    . SER A 1 347  ? 173.856 145.526 170.363 1.00 80.62  ? 347  SER A CA    1 
ATOM   2617 C C     . SER A 1 347  ? 174.133 146.137 168.993 1.00 76.89  ? 347  SER A C     1 
ATOM   2618 O O     . SER A 1 347  ? 174.114 145.426 167.987 1.00 74.08  ? 347  SER A O     1 
ATOM   2619 C CB    . SER A 1 347  ? 175.169 145.328 171.142 1.00 81.22  ? 347  SER A CB    1 
ATOM   2620 O OG    . SER A 1 347  ? 176.041 144.444 170.461 1.00 74.34  ? 347  SER A OG    1 
ATOM   2621 N N     . PRO A 1 348  ? 174.372 147.450 168.928 1.00 77.86  ? 348  PRO A N     1 
ATOM   2622 C CA    . PRO A 1 348  ? 174.784 148.039 167.643 1.00 75.11  ? 348  PRO A CA    1 
ATOM   2623 C C     . PRO A 1 348  ? 176.100 147.484 167.130 1.00 77.63  ? 348  PRO A C     1 
ATOM   2624 O O     . PRO A 1 348  ? 176.285 147.374 165.912 1.00 76.62  ? 348  PRO A O     1 
ATOM   2625 C CB    . PRO A 1 348  ? 174.881 149.538 167.959 1.00 75.43  ? 348  PRO A CB    1 
ATOM   2626 C CG    . PRO A 1 348  ? 175.100 149.601 169.433 1.00 76.36  ? 348  PRO A CG    1 
ATOM   2627 C CD    . PRO A 1 348  ? 174.314 148.460 169.999 1.00 75.18  ? 348  PRO A CD    1 
ATOM   2628 N N     . VAL A 1 349  ? 177.017 147.131 168.022 1.00 79.16  ? 349  VAL A N     1 
ATOM   2629 C CA    . VAL A 1 349  ? 178.315 146.573 167.656 1.00 83.83  ? 349  VAL A CA    1 
ATOM   2630 C C     . VAL A 1 349  ? 178.206 145.053 167.710 1.00 83.86  ? 349  VAL A C     1 
ATOM   2631 O O     . VAL A 1 349  ? 177.823 144.511 168.758 1.00 81.82  ? 349  VAL A O     1 
ATOM   2632 C CB    . VAL A 1 349  ? 179.428 147.075 168.588 1.00 85.83  ? 349  VAL A CB    1 
ATOM   2633 C CG1   . VAL A 1 349  ? 180.774 146.504 168.163 1.00 81.55  ? 349  VAL A CG1   1 
ATOM   2634 C CG2   . VAL A 1 349  ? 179.464 148.595 168.601 1.00 84.02  ? 349  VAL A CG2   1 
ATOM   2635 N N     . PRO A 1 350  ? 178.503 144.338 166.625 1.00 83.46  ? 350  PRO A N     1 
ATOM   2636 C CA    . PRO A 1 350  ? 178.493 142.871 166.686 1.00 82.20  ? 350  PRO A CA    1 
ATOM   2637 C C     . PRO A 1 350  ? 179.484 142.357 167.720 1.00 89.31  ? 350  PRO A C     1 
ATOM   2638 O O     . PRO A 1 350  ? 180.592 142.879 167.860 1.00 91.20  ? 350  PRO A O     1 
ATOM   2639 C CB    . PRO A 1 350  ? 178.892 142.454 165.266 1.00 74.72  ? 350  PRO A CB    1 
ATOM   2640 C CG    . PRO A 1 350  ? 178.539 143.627 164.413 1.00 70.35  ? 350  PRO A CG    1 
ATOM   2641 C CD    . PRO A 1 350  ? 178.783 144.834 165.267 1.00 74.94  ? 350  PRO A CD    1 
ATOM   2642 N N     . GLN A 1 351  ? 179.075 141.321 168.445 1.00 89.95  ? 351  GLN A N     1 
ATOM   2643 C CA    . GLN A 1 351  ? 179.870 140.753 169.519 1.00 94.28  ? 351  GLN A CA    1 
ATOM   2644 C C     . GLN A 1 351  ? 179.925 139.239 169.389 1.00 99.97  ? 351  GLN A C     1 
ATOM   2645 O O     . GLN A 1 351  ? 179.020 138.628 168.812 1.00 98.45  ? 351  GLN A O     1 
ATOM   2646 C CB    . GLN A 1 351  ? 179.293 141.128 170.892 1.00 94.28  ? 351  GLN A CB    1 
ATOM   2647 C CG    . GLN A 1 351  ? 179.278 142.621 171.177 1.00 91.54  ? 351  GLN A CG    1 
ATOM   2648 C CD    . GLN A 1 351  ? 178.680 142.949 172.531 1.00 89.31  ? 351  GLN A CD    1 
ATOM   2649 O OE1   . GLN A 1 351  ? 179.370 142.920 173.551 1.00 87.69  ? 351  GLN A OE1   1 
ATOM   2650 N NE2   . GLN A 1 351  ? 177.391 143.263 172.548 1.00 83.39  ? 351  GLN A NE2   1 
ATOM   2651 N N     . PRO A 1 352  ? 180.984 138.610 169.903 1.00 103.69 ? 352  PRO A N     1 
ATOM   2652 C CA    . PRO A 1 352  ? 181.055 137.144 169.872 1.00 105.00 ? 352  PRO A CA    1 
ATOM   2653 C C     . PRO A 1 352  ? 179.908 136.516 170.652 1.00 103.58 ? 352  PRO A C     1 
ATOM   2654 O O     . PRO A 1 352  ? 179.464 137.041 171.675 1.00 97.67  ? 352  PRO A O     1 
ATOM   2655 C CB    . PRO A 1 352  ? 182.410 136.841 170.520 1.00 102.67 ? 352  PRO A CB    1 
ATOM   2656 C CG    . PRO A 1 352  ? 183.212 138.083 170.313 1.00 100.76 ? 352  PRO A CG    1 
ATOM   2657 C CD    . PRO A 1 352  ? 182.231 139.213 170.405 1.00 99.16  ? 352  PRO A CD    1 
ATOM   2658 N N     . GLU A 1 353  ? 179.430 135.380 170.153 1.00 101.01 ? 353  GLU A N     1 
ATOM   2659 C CA    . GLU A 1 353  ? 178.301 134.695 170.758 1.00 96.70  ? 353  GLU A CA    1 
ATOM   2660 C C     . GLU A 1 353  ? 178.726 133.957 172.025 1.00 98.07  ? 353  GLU A C     1 
ATOM   2661 O O     . GLU A 1 353  ? 179.912 133.722 172.276 1.00 95.62  ? 353  GLU A O     1 
ATOM   2662 C CB    . GLU A 1 353  ? 177.675 133.711 169.769 1.00 89.65  ? 353  GLU A CB    1 
ATOM   2663 C CG    . GLU A 1 353  ? 177.151 134.353 168.496 1.00 94.14  ? 353  GLU A CG    1 
ATOM   2664 C CD    . GLU A 1 353  ? 176.675 133.330 167.482 1.00 97.94  ? 353  GLU A CD    1 
ATOM   2665 O OE1   . GLU A 1 353  ? 177.046 132.144 167.613 1.00 97.55  ? 353  GLU A OE1   1 
ATOM   2666 O OE2   . GLU A 1 353  ? 175.929 133.709 166.555 1.00 92.99  ? 353  GLU A OE2   1 
ATOM   2667 N N     . ILE A 1 354  ? 177.731 133.590 172.827 1.00 92.36  ? 354  ILE A N     1 
ATOM   2668 C CA    . ILE A 1 354  ? 177.932 132.820 174.048 1.00 87.62  ? 354  ILE A CA    1 
ATOM   2669 C C     . ILE A 1 354  ? 177.245 131.475 173.859 1.00 83.73  ? 354  ILE A C     1 
ATOM   2670 O O     . ILE A 1 354  ? 176.039 131.419 173.588 1.00 86.68  ? 354  ILE A O     1 
ATOM   2671 C CB    . ILE A 1 354  ? 177.389 133.559 175.281 1.00 84.79  ? 354  ILE A CB    1 
ATOM   2672 C CG1   . ILE A 1 354  ? 178.035 134.941 175.397 1.00 81.74  ? 354  ILE A CG1   1 
ATOM   2673 C CG2   . ILE A 1 354  ? 177.639 132.750 176.541 1.00 83.43  ? 354  ILE A CG2   1 
ATOM   2674 C CD1   . ILE A 1 354  ? 179.541 134.904 175.548 1.00 88.97  ? 354  ILE A CD1   1 
ATOM   2675 N N     . THR A 1 355  ? 178.009 130.396 173.993 1.00 83.10  ? 355  THR A N     1 
ATOM   2676 C CA    . THR A 1 355  ? 177.519 129.045 173.753 1.00 86.70  ? 355  THR A CA    1 
ATOM   2677 C C     . THR A 1 355  ? 177.605 128.228 175.032 1.00 89.60  ? 355  THR A C     1 
ATOM   2678 O O     . THR A 1 355  ? 178.653 128.197 175.687 1.00 87.04  ? 355  THR A O     1 
ATOM   2679 C CB    . THR A 1 355  ? 178.316 128.355 172.642 1.00 90.16  ? 355  THR A CB    1 
ATOM   2680 O OG1   . THR A 1 355  ? 178.083 126.941 172.690 1.00 90.92  ? 355  THR A OG1   1 
ATOM   2681 C CG2   . THR A 1 355  ? 179.806 128.631 172.796 1.00 92.34  ? 355  THR A CG2   1 
ATOM   2682 N N     . PHE A 1 356  ? 176.510 127.560 175.376 1.00 88.73  ? 356  PHE A N     1 
ATOM   2683 C CA    . PHE A 1 356  ? 176.464 126.653 176.510 1.00 85.87  ? 356  PHE A CA    1 
ATOM   2684 C C     . PHE A 1 356  ? 176.288 125.223 176.019 1.00 93.07  ? 356  PHE A C     1 
ATOM   2685 O O     . PHE A 1 356  ? 175.890 124.977 174.878 1.00 94.47  ? 356  PHE A O     1 
ATOM   2686 C CB    . PHE A 1 356  ? 175.330 127.019 177.471 1.00 82.99  ? 356  PHE A CB    1 
ATOM   2687 C CG    . PHE A 1 356  ? 175.548 128.311 178.196 1.00 86.36  ? 356  PHE A CG    1 
ATOM   2688 C CD1   . PHE A 1 356  ? 176.819 128.842 178.325 1.00 90.12  ? 356  PHE A CD1   1 
ATOM   2689 C CD2   . PHE A 1 356  ? 174.481 128.997 178.750 1.00 89.02  ? 356  PHE A CD2   1 
ATOM   2690 C CE1   . PHE A 1 356  ? 177.023 130.034 178.992 1.00 93.98  ? 356  PHE A CE1   1 
ATOM   2691 C CE2   . PHE A 1 356  ? 174.678 130.187 179.418 1.00 89.36  ? 356  PHE A CE2   1 
ATOM   2692 C CZ    . PHE A 1 356  ? 175.950 130.707 179.540 1.00 92.31  ? 356  PHE A CZ    1 
ATOM   2693 N N     . VAL A 1 357  ? 176.598 124.277 176.901 1.00 97.68  ? 357  VAL A N     1 
ATOM   2694 C CA    . VAL A 1 357  ? 176.484 122.856 176.603 1.00 102.21 ? 357  VAL A CA    1 
ATOM   2695 C C     . VAL A 1 357  ? 175.600 122.221 177.665 1.00 100.01 ? 357  VAL A C     1 
ATOM   2696 O O     . VAL A 1 357  ? 175.926 122.266 178.857 1.00 96.43  ? 357  VAL A O     1 
ATOM   2697 C CB    . VAL A 1 357  ? 177.857 122.164 176.560 1.00 101.93 ? 357  VAL A CB    1 
ATOM   2698 C CG1   . VAL A 1 357  ? 177.691 120.679 176.285 1.00 103.74 ? 357  VAL A CG1   1 
ATOM   2699 C CG2   . VAL A 1 357  ? 178.747 122.813 175.510 1.00 95.10  ? 357  VAL A CG2   1 
ATOM   2700 N N     . PHE A 1 358  ? 174.483 121.638 177.238 1.00 99.77  ? 358  PHE A N     1 
ATOM   2701 C CA    . PHE A 1 358  ? 173.605 120.874 178.121 1.00 103.76 ? 358  PHE A CA    1 
ATOM   2702 C C     . PHE A 1 358  ? 173.932 119.400 177.914 1.00 109.77 ? 358  PHE A C     1 
ATOM   2703 O O     . PHE A 1 358  ? 173.474 118.780 176.951 1.00 110.77 ? 358  PHE A O     1 
ATOM   2704 C CB    . PHE A 1 358  ? 172.136 121.167 177.835 1.00 101.65 ? 358  PHE A CB    1 
ATOM   2705 C CG    . PHE A 1 358  ? 171.723 122.581 178.139 1.00 100.19 ? 358  PHE A CG    1 
ATOM   2706 C CD1   . PHE A 1 358  ? 172.448 123.355 179.029 1.00 98.05  ? 358  PHE A CD1   1 
ATOM   2707 C CD2   . PHE A 1 358  ? 170.605 123.134 177.536 1.00 98.34  ? 358  PHE A CD2   1 
ATOM   2708 C CE1   . PHE A 1 358  ? 172.069 124.654 179.309 1.00 90.19  ? 358  PHE A CE1   1 
ATOM   2709 C CE2   . PHE A 1 358  ? 170.221 124.432 177.812 1.00 91.20  ? 358  PHE A CE2   1 
ATOM   2710 C CZ    . PHE A 1 358  ? 170.954 125.192 178.701 1.00 85.90  ? 358  PHE A CZ    1 
ATOM   2711 N N     . SER A 1 359  ? 174.737 118.840 178.813 1.00 111.69 ? 359  SER A N     1 
ATOM   2712 C CA    . SER A 1 359  ? 175.141 117.444 178.725 1.00 109.62 ? 359  SER A CA    1 
ATOM   2713 C C     . SER A 1 359  ? 174.194 116.506 179.459 1.00 109.47 ? 359  SER A C     1 
ATOM   2714 O O     . SER A 1 359  ? 174.360 115.286 179.368 1.00 111.93 ? 359  SER A O     1 
ATOM   2715 C CB    . SER A 1 359  ? 176.561 117.270 179.271 1.00 110.35 ? 359  SER A CB    1 
ATOM   2716 O OG    . SER A 1 359  ? 176.645 117.697 180.619 1.00 114.15 ? 359  SER A OG    1 
ATOM   2717 N N     . ALA A 1 360  ? 173.214 117.040 180.179 1.00 107.44 ? 360  ALA A N     1 
ATOM   2718 C CA    . ALA A 1 360  ? 172.243 116.242 180.908 1.00 109.75 ? 360  ALA A CA    1 
ATOM   2719 C C     . ALA A 1 360  ? 170.879 116.905 180.808 1.00 112.12 ? 360  ALA A C     1 
ATOM   2720 O O     . ALA A 1 360  ? 170.790 118.130 180.658 1.00 111.82 ? 360  ALA A O     1 
ATOM   2721 C CB    . ALA A 1 360  ? 172.641 116.079 182.382 1.00 107.46 ? 360  ALA A CB    1 
ATOM   2722 N N     . PRO A 1 361  ? 169.799 116.122 180.876 1.00 108.86 ? 361  PRO A N     1 
ATOM   2723 C CA    . PRO A 1 361  ? 168.459 116.712 180.721 1.00 104.88 ? 361  PRO A CA    1 
ATOM   2724 C C     . PRO A 1 361  ? 168.081 117.708 181.804 1.00 103.64 ? 361  PRO A C     1 
ATOM   2725 O O     . PRO A 1 361  ? 167.207 118.547 181.565 1.00 102.62 ? 361  PRO A O     1 
ATOM   2726 C CB    . PRO A 1 361  ? 167.534 115.487 180.744 1.00 106.74 ? 361  PRO A CB    1 
ATOM   2727 C CG    . PRO A 1 361  ? 168.401 114.348 180.355 1.00 106.83 ? 361  PRO A CG    1 
ATOM   2728 C CD    . PRO A 1 361  ? 169.749 114.653 180.926 1.00 105.21 ? 361  PRO A CD    1 
ATOM   2729 N N     . TRP A 1 362  ? 168.695 117.647 182.990 1.00 104.21 ? 362  TRP A N     1 
ATOM   2730 C CA    . TRP A 1 362  ? 168.259 118.531 184.069 1.00 103.22 ? 362  TRP A CA    1 
ATOM   2731 C C     . TRP A 1 362  ? 168.715 119.971 183.854 1.00 102.94 ? 362  TRP A C     1 
ATOM   2732 O O     . TRP A 1 362  ? 168.031 120.903 184.288 1.00 102.61 ? 362  TRP A O     1 
ATOM   2733 C CB    . TRP A 1 362  ? 168.743 118.007 185.423 1.00 105.31 ? 362  TRP A CB    1 
ATOM   2734 C CG    . TRP A 1 362  ? 170.223 117.830 185.541 1.00 110.67 ? 362  TRP A CG    1 
ATOM   2735 C CD1   . TRP A 1 362  ? 170.936 116.701 185.269 1.00 110.49 ? 362  TRP A CD1   1 
ATOM   2736 C CD2   . TRP A 1 362  ? 171.173 118.807 185.985 1.00 109.94 ? 362  TRP A CD2   1 
ATOM   2737 N NE1   . TRP A 1 362  ? 172.271 116.915 185.506 1.00 107.67 ? 362  TRP A NE1   1 
ATOM   2738 C CE2   . TRP A 1 362  ? 172.443 118.201 185.946 1.00 108.97 ? 362  TRP A CE2   1 
ATOM   2739 C CE3   . TRP A 1 362  ? 171.072 120.136 186.406 1.00 108.94 ? 362  TRP A CE3   1 
ATOM   2740 C CZ2   . TRP A 1 362  ? 173.605 118.877 186.312 1.00 109.60 ? 362  TRP A CZ2   1 
ATOM   2741 C CZ3   . TRP A 1 362  ? 172.227 120.806 186.770 1.00 110.73 ? 362  TRP A CZ3   1 
ATOM   2742 C CH2   . TRP A 1 362  ? 173.476 120.175 186.720 1.00 111.22 ? 362  TRP A CH2   1 
ATOM   2743 N N     . GLU A 1 363  ? 169.851 120.180 183.187 1.00 101.48 ? 363  GLU A N     1 
ATOM   2744 C CA    . GLU A 1 363  ? 170.275 121.541 182.866 1.00 100.82 ? 363  GLU A CA    1 
ATOM   2745 C C     . GLU A 1 363  ? 169.310 122.193 181.880 1.00 98.64  ? 363  GLU A C     1 
ATOM   2746 O O     . GLU A 1 363  ? 168.874 123.339 182.076 1.00 97.65  ? 363  GLU A O     1 
ATOM   2747 C CB    . GLU A 1 363  ? 171.696 121.520 182.305 1.00 105.13 ? 363  GLU A CB    1 
ATOM   2748 C CG    . GLU A 1 363  ? 172.711 120.882 183.241 1.00 108.68 ? 363  GLU A CG    1 
ATOM   2749 C CD    . GLU A 1 363  ? 173.965 120.429 182.523 1.00 109.41 ? 363  GLU A CD    1 
ATOM   2750 O OE1   . GLU A 1 363  ? 173.924 120.292 181.283 1.00 107.18 ? 363  GLU A OE1   1 
ATOM   2751 O OE2   . GLU A 1 363  ? 174.992 120.208 183.198 1.00 111.12 ? 363  GLU A OE2   1 
ATOM   2752 N N     . LEU A 1 364  ? 168.958 121.470 180.814 1.00 97.05  ? 364  LEU A N     1 
ATOM   2753 C CA    . LEU A 1 364  ? 167.924 121.950 179.907 1.00 91.65  ? 364  LEU A CA    1 
ATOM   2754 C C     . LEU A 1 364  ? 166.597 122.120 180.629 1.00 88.49  ? 364  LEU A C     1 
ATOM   2755 O O     . LEU A 1 364  ? 165.827 123.023 180.300 1.00 87.81  ? 364  LEU A O     1 
ATOM   2756 C CB    . LEU A 1 364  ? 167.768 120.993 178.725 1.00 95.36  ? 364  LEU A CB    1 
ATOM   2757 C CG    . LEU A 1 364  ? 166.634 121.294 177.738 1.00 89.96  ? 364  LEU A CG    1 
ATOM   2758 C CD1   . LEU A 1 364  ? 166.823 122.656 177.088 1.00 81.63  ? 364  LEU A CD1   1 
ATOM   2759 C CD2   . LEU A 1 364  ? 166.525 120.205 176.683 1.00 91.44  ? 364  LEU A CD2   1 
ATOM   2760 N N     . ASP A 1 365  ? 166.318 121.271 181.621 1.00 91.27  ? 365  ASP A N     1 
ATOM   2761 C CA    . ASP A 1 365  ? 165.088 121.412 182.390 1.00 93.66  ? 365  ASP A CA    1 
ATOM   2762 C C     . ASP A 1 365  ? 165.075 122.716 183.178 1.00 92.59  ? 365  ASP A C     1 
ATOM   2763 O O     . ASP A 1 365  ? 164.049 123.397 183.237 1.00 92.68  ? 365  ASP A O     1 
ATOM   2764 C CB    . ASP A 1 365  ? 164.915 120.217 183.326 1.00 97.92  ? 365  ASP A CB    1 
ATOM   2765 C CG    . ASP A 1 365  ? 163.560 120.199 184.007 1.00 101.28 ? 365  ASP A CG    1 
ATOM   2766 O OD1   . ASP A 1 365  ? 162.649 120.922 183.551 1.00 93.52  ? 365  ASP A OD1   1 
ATOM   2767 O OD2   . ASP A 1 365  ? 163.407 119.461 185.002 1.00 105.78 ? 365  ASP A OD2   1 
ATOM   2768 N N     . LYS A 1 366  ? 166.203 123.077 183.793 1.00 89.22  ? 366  LYS A N     1 
ATOM   2769 C CA    . LYS A 1 366  ? 166.283 124.353 184.501 1.00 85.78  ? 366  LYS A CA    1 
ATOM   2770 C C     . LYS A 1 366  ? 166.130 125.526 183.540 1.00 80.78  ? 366  LYS A C     1 
ATOM   2771 O O     . LYS A 1 366  ? 165.451 126.516 183.852 1.00 80.97  ? 366  LYS A O     1 
ATOM   2772 C CB    . LYS A 1 366  ? 167.605 124.456 185.262 1.00 92.12  ? 366  LYS A CB    1 
ATOM   2773 C CG    . LYS A 1 366  ? 167.782 123.412 186.350 1.00 95.43  ? 366  LYS A CG    1 
ATOM   2774 C CD    . LYS A 1 366  ? 169.029 123.684 187.174 1.00 97.83  ? 366  LYS A CD    1 
ATOM   2775 C CE    . LYS A 1 366  ? 170.267 123.760 186.296 1.00 103.54 ? 366  LYS A CE    1 
ATOM   2776 N NZ    . LYS A 1 366  ? 171.497 124.023 187.092 1.00 100.45 ? 366  LYS A NZ    1 
ATOM   2777 N N     . PHE A 1 367  ? 166.758 125.436 182.365 1.00 78.01  ? 367  PHE A N     1 
ATOM   2778 C CA    . PHE A 1 367  ? 166.597 126.492 181.368 1.00 75.20  ? 367  PHE A CA    1 
ATOM   2779 C C     . PHE A 1 367  ? 165.139 126.625 180.939 1.00 75.22  ? 367  PHE A C     1 
ATOM   2780 O O     . PHE A 1 367  ? 164.614 127.740 180.808 1.00 75.29  ? 367  PHE A O     1 
ATOM   2781 C CB    . PHE A 1 367  ? 167.493 126.210 180.163 1.00 73.97  ? 367  PHE A CB    1 
ATOM   2782 C CG    . PHE A 1 367  ? 167.445 127.275 179.109 1.00 70.39  ? 367  PHE A CG    1 
ATOM   2783 C CD1   . PHE A 1 367  ? 168.067 128.493 179.311 1.00 71.53  ? 367  PHE A CD1   1 
ATOM   2784 C CD2   . PHE A 1 367  ? 166.787 127.054 177.913 1.00 70.39  ? 367  PHE A CD2   1 
ATOM   2785 C CE1   . PHE A 1 367  ? 168.029 129.474 178.343 1.00 65.90  ? 367  PHE A CE1   1 
ATOM   2786 C CE2   . PHE A 1 367  ? 166.748 128.032 176.941 1.00 69.76  ? 367  PHE A CE2   1 
ATOM   2787 C CZ    . PHE A 1 367  ? 167.369 129.244 177.157 1.00 64.36  ? 367  PHE A CZ    1 
ATOM   2788 N N     . ILE A 1 368  ? 164.468 125.492 180.730 1.00 77.39  ? 368  ILE A N     1 
ATOM   2789 C CA    . ILE A 1 368  ? 163.064 125.497 180.342 1.00 73.60  ? 368  ILE A CA    1 
ATOM   2790 C C     . ILE A 1 368  ? 162.198 126.043 181.469 1.00 74.55  ? 368  ILE A C     1 
ATOM   2791 O O     . ILE A 1 368  ? 161.197 126.718 181.221 1.00 77.27  ? 368  ILE A O     1 
ATOM   2792 C CB    . ILE A 1 368  ? 162.633 124.082 179.913 1.00 82.11  ? 368  ILE A CB    1 
ATOM   2793 C CG1   . ILE A 1 368  ? 163.320 123.697 178.602 1.00 83.72  ? 368  ILE A CG1   1 
ATOM   2794 C CG2   . ILE A 1 368  ? 161.122 123.980 179.772 1.00 82.49  ? 368  ILE A CG2   1 
ATOM   2795 C CD1   . ILE A 1 368  ? 163.203 124.748 177.527 1.00 77.87  ? 368  ILE A CD1   1 
ATOM   2796 N N     . GLN A 1 369  ? 162.561 125.760 182.721 1.00 76.06  ? 369  GLN A N     1 
ATOM   2797 C CA    . GLN A 1 369  ? 161.821 126.321 183.848 1.00 80.02  ? 369  GLN A CA    1 
ATOM   2798 C C     . GLN A 1 369  ? 161.944 127.839 183.884 1.00 76.44  ? 369  GLN A C     1 
ATOM   2799 O O     . GLN A 1 369  ? 160.960 128.544 184.139 1.00 72.89  ? 369  GLN A O     1 
ATOM   2800 C CB    . GLN A 1 369  ? 162.315 125.715 185.162 1.00 82.53  ? 369  GLN A CB    1 
ATOM   2801 C CG    . GLN A 1 369  ? 161.944 124.256 185.356 1.00 88.57  ? 369  GLN A CG    1 
ATOM   2802 C CD    . GLN A 1 369  ? 160.448 124.027 185.359 1.00 94.17  ? 369  GLN A CD    1 
ATOM   2803 O OE1   . GLN A 1 369  ? 159.957 123.062 184.777 1.00 96.55  ? 369  GLN A OE1   1 
ATOM   2804 N NE2   . GLN A 1 369  ? 159.714 124.914 186.022 1.00 92.34  ? 369  GLN A NE2   1 
ATOM   2805 N N     . GLN A 1 370  ? 163.147 128.358 183.639 1.00 72.72  ? 370  GLN A N     1 
ATOM   2806 C CA    . GLN A 1 370  ? 163.324 129.807 183.573 1.00 69.40  ? 370  GLN A CA    1 
ATOM   2807 C C     . GLN A 1 370  ? 162.489 130.410 182.448 1.00 67.66  ? 370  GLN A C     1 
ATOM   2808 O O     . GLN A 1 370  ? 161.802 131.426 182.638 1.00 67.09  ? 370  GLN A O     1 
ATOM   2809 C CB    . GLN A 1 370  ? 164.804 130.144 183.393 1.00 71.31  ? 370  GLN A CB    1 
ATOM   2810 C CG    . GLN A 1 370  ? 165.632 129.934 184.645 1.00 74.19  ? 370  GLN A CG    1 
ATOM   2811 C CD    . GLN A 1 370  ? 165.245 130.887 185.756 1.00 76.32  ? 370  GLN A CD    1 
ATOM   2812 O OE1   . GLN A 1 370  ? 165.088 132.086 185.532 1.00 76.17  ? 370  GLN A OE1   1 
ATOM   2813 N NE2   . GLN A 1 370  ? 165.079 130.356 186.961 1.00 73.89  ? 370  GLN A NE2   1 
ATOM   2814 N N     . LEU A 1 371  ? 162.522 129.783 181.269 1.00 66.52  ? 371  LEU A N     1 
ATOM   2815 C CA    . LEU A 1 371  ? 161.714 130.271 180.155 1.00 65.12  ? 371  LEU A CA    1 
ATOM   2816 C C     . LEU A 1 371  ? 160.226 130.215 180.482 1.00 61.33  ? 371  LEU A C     1 
ATOM   2817 O O     . LEU A 1 371  ? 159.471 131.125 180.127 1.00 57.51  ? 371  LEU A O     1 
ATOM   2818 C CB    . LEU A 1 371  ? 162.007 129.465 178.891 1.00 68.22  ? 371  LEU A CB    1 
ATOM   2819 C CG    . LEU A 1 371  ? 163.366 129.663 178.225 1.00 67.24  ? 371  LEU A CG    1 
ATOM   2820 C CD1   . LEU A 1 371  ? 163.393 128.930 176.897 1.00 69.45  ? 371  LEU A CD1   1 
ATOM   2821 C CD2   . LEU A 1 371  ? 163.663 131.140 178.035 1.00 59.75  ? 371  LEU A CD2   1 
ATOM   2822 N N     . GLY A 1 372  ? 159.786 129.147 181.147 1.00 63.60  ? 372  GLY A N     1 
ATOM   2823 C CA    . GLY A 1 372  ? 158.381 129.020 181.488 1.00 63.72  ? 372  GLY A CA    1 
ATOM   2824 C C     . GLY A 1 372  ? 157.933 130.059 182.492 1.00 60.65  ? 372  GLY A C     1 
ATOM   2825 O O     . GLY A 1 372  ? 156.831 130.598 182.385 1.00 59.69  ? 372  GLY A O     1 
ATOM   2826 N N     . ILE A 1 373  ? 158.779 130.357 183.478 1.00 63.11  ? 373  ILE A N     1 
ATOM   2827 C CA    . ILE A 1 373  ? 158.473 131.433 184.416 1.00 61.04  ? 373  ILE A CA    1 
ATOM   2828 C C     . ILE A 1 373  ? 158.348 132.755 183.670 1.00 60.69  ? 373  ILE A C     1 
ATOM   2829 O O     . ILE A 1 373  ? 157.399 133.524 183.879 1.00 60.23  ? 373  ILE A O     1 
ATOM   2830 C CB    . ILE A 1 373  ? 159.544 131.505 185.519 1.00 61.39  ? 373  ILE A CB    1 
ATOM   2831 C CG1   . ILE A 1 373  ? 159.448 130.285 186.436 1.00 64.43  ? 373  ILE A CG1   1 
ATOM   2832 C CG2   . ILE A 1 373  ? 159.411 132.794 186.314 1.00 62.86  ? 373  ILE A CG2   1 
ATOM   2833 C CD1   . ILE A 1 373  ? 158.105 130.140 187.122 1.00 64.28  ? 373  ILE A CD1   1 
ATOM   2834 N N     . SER A 1 374  ? 159.291 133.024 182.765 1.00 60.74  ? 374  SER A N     1 
ATOM   2835 C CA    . SER A 1 374  ? 159.278 134.297 182.051 1.00 54.73  ? 374  SER A CA    1 
ATOM   2836 C C     . SER A 1 374  ? 158.064 134.422 181.134 1.00 53.99  ? 374  SER A C     1 
ATOM   2837 O O     . SER A 1 374  ? 157.510 135.516 180.980 1.00 55.34  ? 374  SER A O     1 
ATOM   2838 C CB    . SER A 1 374  ? 160.573 134.464 181.261 1.00 57.02  ? 374  SER A CB    1 
ATOM   2839 O OG    . SER A 1 374  ? 161.697 134.473 182.123 1.00 61.16  ? 374  SER A OG    1 
ATOM   2840 N N     . VAL A 1 375  ? 157.634 133.321 180.514 1.00 61.69  ? 375  VAL A N     1 
ATOM   2841 C CA    . VAL A 1 375  ? 156.501 133.411 179.595 1.00 60.64  ? 375  VAL A CA    1 
ATOM   2842 C C     . VAL A 1 375  ? 155.171 133.366 180.342 1.00 58.37  ? 375  VAL A C     1 
ATOM   2843 O O     . VAL A 1 375  ? 154.172 133.915 179.864 1.00 60.15  ? 375  VAL A O     1 
ATOM   2844 C CB    . VAL A 1 375  ? 156.572 132.313 178.517 1.00 58.39  ? 375  VAL A CB    1 
ATOM   2845 C CG1   . VAL A 1 375  ? 157.859 132.433 177.715 1.00 53.04  ? 375  VAL A CG1   1 
ATOM   2846 C CG2   . VAL A 1 375  ? 156.441 130.934 179.134 1.00 57.06  ? 375  VAL A CG2   1 
ATOM   2847 N N     . ALA A 1 376  ? 155.121 132.719 181.510 1.00 59.82  ? 376  ALA A N     1 
ATOM   2848 C CA    . ALA A 1 376  ? 153.917 132.769 182.328 1.00 59.15  ? 376  ALA A CA    1 
ATOM   2849 C C     . ALA A 1 376  ? 153.732 134.144 182.948 1.00 61.89  ? 376  ALA A C     1 
ATOM   2850 O O     . ALA A 1 376  ? 152.595 134.586 183.146 1.00 61.02  ? 376  ALA A O     1 
ATOM   2851 C CB    . ALA A 1 376  ? 153.972 131.695 183.414 1.00 56.49  ? 376  ALA A CB    1 
ATOM   2852 N N     . ALA A 1 377  ? 154.833 134.831 183.258 1.00 60.77  ? 377  ALA A N     1 
ATOM   2853 C CA    . ALA A 1 377  ? 154.744 136.220 183.685 1.00 52.40  ? 377  ALA A CA    1 
ATOM   2854 C C     . ALA A 1 377  ? 154.374 137.157 182.544 1.00 52.36  ? 377  ALA A C     1 
ATOM   2855 O O     . ALA A 1 377  ? 154.109 138.336 182.799 1.00 52.68  ? 377  ALA A O     1 
ATOM   2856 C CB    . ALA A 1 377  ? 156.066 136.663 184.313 1.00 50.85  ? 377  ALA A CB    1 
ATOM   2857 N N     . GLN A 1 378  ? 154.351 136.660 181.304 1.00 56.16  ? 378  GLN A N     1 
ATOM   2858 C CA    . GLN A 1 378  ? 154.045 137.464 180.121 1.00 51.47  ? 378  GLN A CA    1 
ATOM   2859 C C     . GLN A 1 378  ? 155.024 138.629 179.985 1.00 48.87  ? 378  GLN A C     1 
ATOM   2860 O O     . GLN A 1 378  ? 154.646 139.761 179.680 1.00 48.40  ? 378  GLN A O     1 
ATOM   2861 C CB    . GLN A 1 378  ? 152.596 137.957 180.147 1.00 50.26  ? 378  GLN A CB    1 
ATOM   2862 C CG    . GLN A 1 378  ? 151.568 136.839 180.119 1.00 60.81  ? 378  GLN A CG    1 
ATOM   2863 C CD    . GLN A 1 378  ? 150.164 137.331 180.406 1.00 68.58  ? 378  GLN A CD    1 
ATOM   2864 O OE1   . GLN A 1 378  ? 149.970 138.455 180.867 1.00 72.05  ? 378  GLN A OE1   1 
ATOM   2865 N NE2   . GLN A 1 378  ? 149.175 136.489 180.132 1.00 61.63  ? 378  GLN A NE2   1 
ATOM   2866 N N     . MET A 1 379  ? 156.302 138.333 180.205 1.00 51.91  ? 379  MET A N     1 
ATOM   2867 C CA    . MET A 1 379  ? 157.364 139.321 180.173 1.00 48.75  ? 379  MET A CA    1 
ATOM   2868 C C     . MET A 1 379  ? 158.374 138.983 179.083 1.00 45.60  ? 379  MET A C     1 
ATOM   2869 O O     . MET A 1 379  ? 158.633 137.807 178.811 1.00 49.52  ? 379  MET A O     1 
ATOM   2870 C CB    . MET A 1 379  ? 158.081 139.394 181.527 1.00 45.12  ? 379  MET A CB    1 
ATOM   2871 C CG    . MET A 1 379  ? 157.186 139.753 182.709 1.00 48.75  ? 379  MET A CG    1 
ATOM   2872 S SD    . MET A 1 379  ? 156.967 141.526 182.965 1.00 60.89  ? 379  MET A SD    1 
ATOM   2873 C CE    . MET A 1 379  ? 155.519 141.861 181.971 1.00 46.32  ? 379  MET A CE    1 
ATOM   2874 N N     . PRO A 1 380  ? 158.956 139.992 178.438 1.00 41.52  ? 380  PRO A N     1 
ATOM   2875 C CA    . PRO A 1 380  ? 159.942 139.753 177.374 1.00 42.46  ? 380  PRO A CA    1 
ATOM   2876 C C     . PRO A 1 380  ? 161.394 139.714 177.830 1.00 47.85  ? 380  PRO A C     1 
ATOM   2877 O O     . PRO A 1 380  ? 162.283 139.761 176.975 1.00 51.00  ? 380  PRO A O     1 
ATOM   2878 C CB    . PRO A 1 380  ? 159.712 140.958 176.456 1.00 41.80  ? 380  PRO A CB    1 
ATOM   2879 C CG    . PRO A 1 380  ? 159.364 142.052 177.404 1.00 36.56  ? 380  PRO A CG    1 
ATOM   2880 C CD    . PRO A 1 380  ? 158.578 141.414 178.524 1.00 35.71  ? 380  PRO A CD    1 
ATOM   2881 N N     . ALA A 1 381  ? 161.667 139.632 179.132 1.00 43.08  ? 381  ALA A N     1 
ATOM   2882 C CA    . ALA A 1 381  ? 163.016 139.860 179.639 1.00 38.49  ? 381  ALA A CA    1 
ATOM   2883 C C     . ALA A 1 381  ? 163.833 138.576 179.758 1.00 52.85  ? 381  ALA A C     1 
ATOM   2884 O O     . ALA A 1 381  ? 164.907 138.465 179.163 1.00 67.98  ? 381  ALA A O     1 
ATOM   2885 C CB    . ALA A 1 381  ? 162.946 140.563 180.994 1.00 43.19  ? 381  ALA A CB    1 
ATOM   2886 N N     . GLY A 1 382  ? 163.360 137.620 180.553 1.00 42.35  ? 382  GLY A N     1 
ATOM   2887 C CA    . GLY A 1 382  ? 164.082 136.375 180.744 1.00 48.08  ? 382  GLY A CA    1 
ATOM   2888 C C     . GLY A 1 382  ? 165.434 136.528 181.416 1.00 49.43  ? 382  GLY A C     1 
ATOM   2889 O O     . GLY A 1 382  ? 165.923 137.646 181.597 1.00 49.28  ? 382  GLY A O     1 
ATOM   2890 N N     . SER A 1 383  ? 166.053 135.407 181.781 1.00 54.36  ? 383  SER A N     1 
ATOM   2891 C CA    . SER A 1 383  ? 167.351 135.411 182.444 1.00 55.63  ? 383  SER A CA    1 
ATOM   2892 C C     . SER A 1 383  ? 167.885 133.989 182.485 1.00 57.34  ? 383  SER A C     1 
ATOM   2893 O O     . SER A 1 383  ? 167.119 133.034 182.636 1.00 55.55  ? 383  SER A O     1 
ATOM   2894 C CB    . SER A 1 383  ? 167.254 135.977 183.867 1.00 58.85  ? 383  SER A CB    1 
ATOM   2895 O OG    . SER A 1 383  ? 168.513 135.959 184.513 1.00 67.73  ? 383  SER A OG    1 
ATOM   2896 N N     . TRP A 1 384  ? 169.206 133.857 182.354 1.00 62.64  ? 384  TRP A N     1 
ATOM   2897 C CA    . TRP A 1 384  ? 169.843 132.547 182.482 1.00 66.33  ? 384  TRP A CA    1 
ATOM   2898 C C     . TRP A 1 384  ? 171.312 132.735 182.839 1.00 68.01  ? 384  TRP A C     1 
ATOM   2899 O O     . TRP A 1 384  ? 172.107 133.135 181.982 1.00 67.64  ? 384  TRP A O     1 
ATOM   2900 C CB    . TRP A 1 384  ? 169.692 131.742 181.199 1.00 67.78  ? 384  TRP A CB    1 
ATOM   2901 C CG    . TRP A 1 384  ? 170.359 130.408 181.268 1.00 73.25  ? 384  TRP A CG    1 
ATOM   2902 C CD1   . TRP A 1 384  ? 171.448 129.998 180.557 1.00 74.84  ? 384  TRP A CD1   1 
ATOM   2903 C CD2   . TRP A 1 384  ? 169.993 129.309 182.110 1.00 71.85  ? 384  TRP A CD2   1 
ATOM   2904 N NE1   . TRP A 1 384  ? 171.777 128.709 180.897 1.00 75.32  ? 384  TRP A NE1   1 
ATOM   2905 C CE2   . TRP A 1 384  ? 170.899 128.264 181.850 1.00 77.00  ? 384  TRP A CE2   1 
ATOM   2906 C CE3   . TRP A 1 384  ? 168.984 129.108 183.057 1.00 69.98  ? 384  TRP A CE3   1 
ATOM   2907 C CZ2   . TRP A 1 384  ? 170.827 127.036 182.500 1.00 82.27  ? 384  TRP A CZ2   1 
ATOM   2908 C CZ3   . TRP A 1 384  ? 168.915 127.889 183.702 1.00 76.66  ? 384  TRP A CZ3   1 
ATOM   2909 C CH2   . TRP A 1 384  ? 169.830 126.868 183.420 1.00 83.23  ? 384  TRP A CH2   1 
ATOM   2910 N N     . GLN A 1 385  ? 171.661 132.433 184.090 1.00 67.57  ? 385  GLN A N     1 
ATOM   2911 C CA    . GLN A 1 385  ? 173.048 132.388 184.557 1.00 72.72  ? 385  GLN A CA    1 
ATOM   2912 C C     . GLN A 1 385  ? 173.807 133.669 184.215 1.00 70.91  ? 385  GLN A C     1 
ATOM   2913 O O     . GLN A 1 385  ? 174.909 133.642 183.663 1.00 70.47  ? 385  GLN A O     1 
ATOM   2914 C CB    . GLN A 1 385  ? 173.770 131.159 184.004 1.00 75.99  ? 385  GLN A CB    1 
ATOM   2915 C CG    . GLN A 1 385  ? 173.333 129.852 184.641 1.00 78.53  ? 385  GLN A CG    1 
ATOM   2916 C CD    . GLN A 1 385  ? 174.245 128.694 184.286 1.00 82.85  ? 385  GLN A CD    1 
ATOM   2917 O OE1   . GLN A 1 385  ? 175.202 128.852 183.528 1.00 83.13  ? 385  GLN A OE1   1 
ATOM   2918 N NE2   . GLN A 1 385  ? 173.953 127.521 184.836 1.00 77.11  ? 385  GLN A NE2   1 
ATOM   2919 N N     . GLY A 1 386  ? 173.207 134.804 184.555 1.00 64.90  ? 386  GLY A N     1 
ATOM   2920 C CA    . GLY A 1 386  ? 173.859 136.079 184.344 1.00 69.11  ? 386  GLY A CA    1 
ATOM   2921 C C     . GLY A 1 386  ? 173.731 136.648 182.953 1.00 72.84  ? 386  GLY A C     1 
ATOM   2922 O O     . GLY A 1 386  ? 174.380 137.656 182.652 1.00 73.29  ? 386  GLY A O     1 
ATOM   2923 N N     . TYR A 1 387  ? 172.923 136.035 182.094 1.00 68.55  ? 387  TYR A N     1 
ATOM   2924 C CA    . TYR A 1 387  ? 172.653 136.542 180.758 1.00 63.73  ? 387  TYR A CA    1 
ATOM   2925 C C     . TYR A 1 387  ? 171.154 136.728 180.593 1.00 64.33  ? 387  TYR A C     1 
ATOM   2926 O O     . TYR A 1 387  ? 170.364 135.887 181.032 1.00 65.18  ? 387  TYR A O     1 
ATOM   2927 C CB    . TYR A 1 387  ? 173.184 135.593 179.678 1.00 67.32  ? 387  TYR A CB    1 
ATOM   2928 C CG    . TYR A 1 387  ? 174.683 135.416 179.699 1.00 71.14  ? 387  TYR A CG    1 
ATOM   2929 C CD1   . TYR A 1 387  ? 175.522 136.399 179.194 1.00 70.05  ? 387  TYR A CD1   1 
ATOM   2930 C CD2   . TYR A 1 387  ? 175.259 134.265 180.218 1.00 71.55  ? 387  TYR A CD2   1 
ATOM   2931 C CE1   . TYR A 1 387  ? 176.891 136.244 179.210 1.00 73.34  ? 387  TYR A CE1   1 
ATOM   2932 C CE2   . TYR A 1 387  ? 176.627 134.100 180.238 1.00 73.83  ? 387  TYR A CE2   1 
ATOM   2933 C CZ    . TYR A 1 387  ? 177.439 135.093 179.732 1.00 80.87  ? 387  TYR A CZ    1 
ATOM   2934 O OH    . TYR A 1 387  ? 178.805 134.936 179.747 1.00 84.49  ? 387  TYR A OH    1 
ATOM   2935 N N     . GLU A 1 388  ? 170.767 137.832 179.968 1.00 59.87  ? 388  GLU A N     1 
ATOM   2936 C CA    . GLU A 1 388  ? 169.364 138.107 179.707 1.00 55.43  ? 388  GLU A CA    1 
ATOM   2937 C C     . GLU A 1 388  ? 168.959 137.507 178.368 1.00 52.88  ? 388  GLU A C     1 
ATOM   2938 O O     . GLU A 1 388  ? 169.782 137.347 177.464 1.00 57.62  ? 388  GLU A O     1 
ATOM   2939 C CB    . GLU A 1 388  ? 169.093 139.611 179.718 1.00 57.49  ? 388  GLU A CB    1 
ATOM   2940 C CG    . GLU A 1 388  ? 169.312 140.280 181.066 1.00 57.64  ? 388  GLU A CG    1 
ATOM   2941 C CD    . GLU A 1 388  ? 170.775 140.537 181.361 1.00 63.35  ? 388  GLU A CD    1 
ATOM   2942 O OE1   . GLU A 1 388  ? 171.580 140.549 180.408 1.00 63.11  ? 388  GLU A OE1   1 
ATOM   2943 O OE2   . GLU A 1 388  ? 171.121 140.723 182.547 1.00 62.19  ? 388  GLU A OE2   1 
ATOM   2944 N N     . LEU A 1 389  ? 167.675 137.176 178.246 1.00 47.77  ? 389  LEU A N     1 
ATOM   2945 C CA    . LEU A 1 389  ? 167.161 136.434 177.095 1.00 54.57  ? 389  LEU A CA    1 
ATOM   2946 C C     . LEU A 1 389  ? 165.942 137.158 176.533 1.00 53.61  ? 389  LEU A C     1 
ATOM   2947 O O     . LEU A 1 389  ? 164.828 136.979 177.031 1.00 56.45  ? 389  LEU A O     1 
ATOM   2948 C CB    . LEU A 1 389  ? 166.807 135.004 177.488 1.00 52.47  ? 389  LEU A CB    1 
ATOM   2949 C CG    . LEU A 1 389  ? 167.861 134.206 178.251 1.00 47.38  ? 389  LEU A CG    1 
ATOM   2950 C CD1   . LEU A 1 389  ? 167.278 132.885 178.708 1.00 51.68  ? 389  LEU A CD1   1 
ATOM   2951 C CD2   . LEU A 1 389  ? 169.090 133.986 177.392 1.00 48.87  ? 389  LEU A CD2   1 
ATOM   2952 N N     . GLU A 1 390  ? 166.149 137.948 175.479 1.00 51.20  ? 390  GLU A N     1 
ATOM   2953 C CA    . GLU A 1 390  ? 165.052 138.635 174.808 1.00 50.83  ? 390  GLU A CA    1 
ATOM   2954 C C     . GLU A 1 390  ? 163.974 137.644 174.389 1.00 55.88  ? 390  GLU A C     1 
ATOM   2955 O O     . GLU A 1 390  ? 164.209 136.789 173.530 1.00 63.14  ? 390  GLU A O     1 
ATOM   2956 C CB    . GLU A 1 390  ? 165.573 139.400 173.589 1.00 54.68  ? 390  GLU A CB    1 
ATOM   2957 C CG    . GLU A 1 390  ? 164.518 140.211 172.856 1.00 57.03  ? 390  GLU A CG    1 
ATOM   2958 C CD    . GLU A 1 390  ? 164.264 141.560 173.500 1.00 61.53  ? 390  GLU A CD    1 
ATOM   2959 O OE1   . GLU A 1 390  ? 165.163 142.065 174.204 1.00 59.19  ? 390  GLU A OE1   1 
ATOM   2960 O OE2   . GLU A 1 390  ? 163.164 142.117 173.302 1.00 60.87  ? 390  GLU A OE2   1 
ATOM   2961 N N     . LEU A 1 391  ? 162.788 137.749 174.992 1.00 52.73  ? 391  LEU A N     1 
ATOM   2962 C CA    . LEU A 1 391  ? 161.674 136.853 174.705 1.00 51.40  ? 391  LEU A CA    1 
ATOM   2963 C C     . LEU A 1 391  ? 160.544 137.555 173.964 1.00 54.26  ? 391  LEU A C     1 
ATOM   2964 O O     . LEU A 1 391  ? 159.403 137.086 173.993 1.00 53.69  ? 391  LEU A O     1 
ATOM   2965 C CB    . LEU A 1 391  ? 161.143 136.229 175.995 1.00 48.95  ? 391  LEU A CB    1 
ATOM   2966 C CG    . LEU A 1 391  ? 162.079 135.269 176.723 1.00 46.57  ? 391  LEU A CG    1 
ATOM   2967 C CD1   . LEU A 1 391  ? 161.359 134.617 177.876 1.00 44.79  ? 391  LEU A CD1   1 
ATOM   2968 C CD2   . LEU A 1 391  ? 162.594 134.220 175.770 1.00 51.66  ? 391  LEU A CD2   1 
ATOM   2969 N N     . SER A 1 392  ? 160.837 138.681 173.312 1.00 57.73  ? 392  SER A N     1 
ATOM   2970 C CA    . SER A 1 392  ? 159.808 139.391 172.562 1.00 54.59  ? 392  SER A CA    1 
ATOM   2971 C C     . SER A 1 392  ? 159.317 138.565 171.379 1.00 65.14  ? 392  SER A C     1 
ATOM   2972 O O     . SER A 1 392  ? 158.107 138.473 171.138 1.00 63.63  ? 392  SER A O     1 
ATOM   2973 C CB    . SER A 1 392  ? 160.348 140.738 172.092 1.00 49.85  ? 392  SER A CB    1 
ATOM   2974 O OG    . SER A 1 392  ? 160.816 141.504 173.188 1.00 47.99  ? 392  SER A OG    1 
ATOM   2975 N N     . GLN A 1 393  ? 160.236 137.958 170.633 1.00 64.06  ? 393  GLN A N     1 
ATOM   2976 C CA    . GLN A 1 393  ? 159.890 137.143 169.477 1.00 63.26  ? 393  GLN A CA    1 
ATOM   2977 C C     . GLN A 1 393  ? 159.757 135.666 169.815 1.00 68.76  ? 393  GLN A C     1 
ATOM   2978 O O     . GLN A 1 393  ? 159.509 134.859 168.914 1.00 78.17  ? 393  GLN A O     1 
ATOM   2979 C CB    . GLN A 1 393  ? 160.933 137.320 168.368 1.00 66.57  ? 393  GLN A CB    1 
ATOM   2980 C CG    . GLN A 1 393  ? 161.257 138.766 168.025 1.00 61.53  ? 393  GLN A CG    1 
ATOM   2981 C CD    . GLN A 1 393  ? 162.304 139.360 168.944 1.00 62.67  ? 393  GLN A CD    1 
ATOM   2982 O OE1   . GLN A 1 393  ? 163.011 138.637 169.645 1.00 68.23  ? 393  GLN A OE1   1 
ATOM   2983 N NE2   . GLN A 1 393  ? 162.405 140.683 168.951 1.00 55.15  ? 393  GLN A NE2   1 
ATOM   2984 N N     . PHE A 1 394  ? 159.920 135.292 171.082 1.00 67.18  ? 394  PHE A N     1 
ATOM   2985 C CA    . PHE A 1 394  ? 159.804 133.899 171.508 1.00 69.39  ? 394  PHE A CA    1 
ATOM   2986 C C     . PHE A 1 394  ? 158.323 133.544 171.551 1.00 73.47  ? 394  PHE A C     1 
ATOM   2987 O O     . PHE A 1 394  ? 157.644 133.716 172.564 1.00 69.02  ? 394  PHE A O     1 
ATOM   2988 C CB    . PHE A 1 394  ? 160.479 133.693 172.857 1.00 63.18  ? 394  PHE A CB    1 
ATOM   2989 C CG    . PHE A 1 394  ? 160.515 132.262 173.307 1.00 65.11  ? 394  PHE A CG    1 
ATOM   2990 C CD1   . PHE A 1 394  ? 161.431 131.377 172.770 1.00 68.92  ? 394  PHE A CD1   1 
ATOM   2991 C CD2   . PHE A 1 394  ? 159.639 131.805 174.276 1.00 67.82  ? 394  PHE A CD2   1 
ATOM   2992 C CE1   . PHE A 1 394  ? 161.468 130.062 173.183 1.00 70.03  ? 394  PHE A CE1   1 
ATOM   2993 C CE2   . PHE A 1 394  ? 159.673 130.492 174.694 1.00 68.76  ? 394  PHE A CE2   1 
ATOM   2994 C CZ    . PHE A 1 394  ? 160.589 129.620 174.147 1.00 72.67  ? 394  PHE A CZ    1 
ATOM   2995 N N     . THR A 1 395  ? 157.820 133.039 170.429 1.00 79.73  ? 395  THR A N     1 
ATOM   2996 C CA    . THR A 1 395  ? 156.403 132.750 170.289 1.00 85.16  ? 395  THR A CA    1 
ATOM   2997 C C     . THR A 1 395  ? 156.031 131.484 171.059 1.00 85.72  ? 395  THR A C     1 
ATOM   2998 O O     . THR A 1 395  ? 156.885 130.746 171.558 1.00 85.01  ? 395  THR A O     1 
ATOM   2999 C CB    . THR A 1 395  ? 156.033 132.597 168.815 1.00 89.77  ? 395  THR A CB    1 
ATOM   3000 O OG1   . THR A 1 395  ? 156.779 131.515 168.244 1.00 89.32  ? 395  THR A OG1   1 
ATOM   3001 C CG2   . THR A 1 395  ? 156.349 133.875 168.054 1.00 82.25  ? 395  THR A CG2   1 
ATOM   3002 N N     . GLU A 1 396  ? 154.721 131.241 171.153 1.00 83.56  ? 396  GLU A N     1 
ATOM   3003 C CA    . GLU A 1 396  ? 154.230 130.043 171.826 1.00 93.35  ? 396  GLU A CA    1 
ATOM   3004 C C     . GLU A 1 396  ? 154.688 128.775 171.118 1.00 94.94  ? 396  GLU A C     1 
ATOM   3005 O O     . GLU A 1 396  ? 154.917 127.748 171.768 1.00 91.91  ? 396  GLU A O     1 
ATOM   3006 C CB    . GLU A 1 396  ? 152.702 130.084 171.912 1.00 95.74  ? 396  GLU A CB    1 
ATOM   3007 C CG    . GLU A 1 396  ? 152.074 128.879 172.593 1.00 98.77  ? 396  GLU A CG    1 
ATOM   3008 C CD    . GLU A 1 396  ? 150.560 128.948 172.613 1.00 101.85 ? 396  GLU A CD    1 
ATOM   3009 O OE1   . GLU A 1 396  ? 150.004 129.949 172.115 1.00 100.40 ? 396  GLU A OE1   1 
ATOM   3010 O OE2   . GLU A 1 396  ? 149.926 128.002 173.126 1.00 102.29 ? 396  GLU A OE2   1 
ATOM   3011 N N     . GLN A 1 397  ? 154.824 128.826 169.790 1.00 92.62  ? 397  GLN A N     1 
ATOM   3012 C CA    . GLN A 1 397  ? 155.287 127.658 169.049 1.00 90.09  ? 397  GLN A CA    1 
ATOM   3013 C C     . GLN A 1 397  ? 156.700 127.271 169.462 1.00 91.57  ? 397  GLN A C     1 
ATOM   3014 O O     . GLN A 1 397  ? 157.005 126.084 169.613 1.00 92.90  ? 397  GLN A O     1 
ATOM   3015 C CB    . GLN A 1 397  ? 155.219 127.928 167.546 1.00 90.29  ? 397  GLN A CB    1 
ATOM   3016 C CG    . GLN A 1 397  ? 155.650 126.751 166.684 1.00 96.09  ? 397  GLN A CG    1 
ATOM   3017 C CD    . GLN A 1 397  ? 154.755 125.539 166.857 1.00 101.52 ? 397  GLN A CD    1 
ATOM   3018 O OE1   . GLN A 1 397  ? 153.575 125.664 167.187 1.00 99.53  ? 397  GLN A OE1   1 
ATOM   3019 N NE2   . GLN A 1 397  ? 155.314 124.355 166.637 1.00 101.05 ? 397  GLN A NE2   1 
ATOM   3020 N N     . GLN A 1 398  ? 157.576 128.260 169.653 1.00 89.37  ? 398  GLN A N     1 
ATOM   3021 C CA    . GLN A 1 398  ? 158.932 127.964 170.105 1.00 85.26  ? 398  GLN A CA    1 
ATOM   3022 C C     . GLN A 1 398  ? 158.928 127.367 171.506 1.00 85.74  ? 398  GLN A C     1 
ATOM   3023 O O     . GLN A 1 398  ? 159.716 126.463 171.807 1.00 86.63  ? 398  GLN A O     1 
ATOM   3024 C CB    . GLN A 1 398  ? 159.789 129.229 170.060 1.00 82.64  ? 398  GLN A CB    1 
ATOM   3025 C CG    . GLN A 1 398  ? 159.915 129.848 168.678 1.00 81.55  ? 398  GLN A CG    1 
ATOM   3026 C CD    . GLN A 1 398  ? 160.961 130.945 168.627 1.00 82.56  ? 398  GLN A CD    1 
ATOM   3027 O OE1   . GLN A 1 398  ? 161.803 131.057 169.518 1.00 74.82  ? 398  GLN A OE1   1 
ATOM   3028 N NE2   . GLN A 1 398  ? 160.912 131.762 167.582 1.00 83.69  ? 398  GLN A NE2   1 
ATOM   3029 N N     . TRP A 1 399  ? 158.051 127.866 172.380 1.00 85.16  ? 399  TRP A N     1 
ATOM   3030 C CA    . TRP A 1 399  ? 157.939 127.313 173.726 1.00 84.12  ? 399  TRP A CA    1 
ATOM   3031 C C     . TRP A 1 399  ? 157.487 125.857 173.691 1.00 87.78  ? 399  TRP A C     1 
ATOM   3032 O O     . TRP A 1 399  ? 158.046 125.005 174.396 1.00 89.44  ? 399  TRP A O     1 
ATOM   3033 C CB    . TRP A 1 399  ? 156.975 128.169 174.550 1.00 83.49  ? 399  TRP A CB    1 
ATOM   3034 C CG    . TRP A 1 399  ? 156.629 127.618 175.897 1.00 82.60  ? 399  TRP A CG    1 
ATOM   3035 C CD1   . TRP A 1 399  ? 155.379 127.351 176.375 1.00 80.74  ? 399  TRP A CD1   1 
ATOM   3036 C CD2   . TRP A 1 399  ? 157.541 127.271 176.946 1.00 80.40  ? 399  TRP A CD2   1 
ATOM   3037 N NE1   . TRP A 1 399  ? 155.455 126.861 177.654 1.00 78.07  ? 399  TRP A NE1   1 
ATOM   3038 C CE2   . TRP A 1 399  ? 156.771 126.800 178.028 1.00 79.75  ? 399  TRP A CE2   1 
ATOM   3039 C CE3   . TRP A 1 399  ? 158.932 127.311 177.075 1.00 75.19  ? 399  TRP A CE3   1 
ATOM   3040 C CZ2   . TRP A 1 399  ? 157.346 126.373 179.220 1.00 74.69  ? 399  TRP A CZ2   1 
ATOM   3041 C CZ3   . TRP A 1 399  ? 159.499 126.886 178.258 1.00 73.60  ? 399  TRP A CZ3   1 
ATOM   3042 C CH2   . TRP A 1 399  ? 158.708 126.422 179.314 1.00 73.14  ? 399  TRP A CH2   1 
ATOM   3043 N N     . HIS A 1 400  ? 156.485 125.551 172.864 1.00 92.35  ? 400  HIS A N     1 
ATOM   3044 C CA    . HIS A 1 400  ? 156.040 124.168 172.725 1.00 96.52  ? 400  HIS A CA    1 
ATOM   3045 C C     . HIS A 1 400  ? 157.132 123.293 172.124 1.00 92.70  ? 400  HIS A C     1 
ATOM   3046 O O     . HIS A 1 400  ? 157.288 122.133 172.517 1.00 91.90  ? 400  HIS A O     1 
ATOM   3047 C CB    . HIS A 1 400  ? 154.768 124.104 171.881 1.00 98.80  ? 400  HIS A CB    1 
ATOM   3048 C CG    . HIS A 1 400  ? 153.527 124.471 172.633 1.00 105.20 ? 400  HIS A CG    1 
ATOM   3049 N ND1   . HIS A 1 400  ? 153.479 124.520 174.009 1.00 105.07 ? 400  HIS A ND1   1 
ATOM   3050 C CD2   . HIS A 1 400  ? 152.288 124.806 172.201 1.00 105.32 ? 400  HIS A CD2   1 
ATOM   3051 C CE1   . HIS A 1 400  ? 152.264 124.869 174.393 1.00 102.14 ? 400  HIS A CE1   1 
ATOM   3052 N NE2   . HIS A 1 400  ? 151.522 125.050 173.315 1.00 105.39 ? 400  HIS A NE2   1 
ATOM   3053 N N     . ASP A 1 401  ? 157.898 123.829 171.169 1.00 90.83  ? 401  ASP A N     1 
ATOM   3054 C CA    . ASP A 1 401  ? 159.006 123.072 170.596 1.00 93.99  ? 401  ASP A CA    1 
ATOM   3055 C C     . ASP A 1 401  ? 160.066 122.761 171.646 1.00 94.63  ? 401  ASP A C     1 
ATOM   3056 O O     . ASP A 1 401  ? 160.602 121.649 171.684 1.00 94.94  ? 401  ASP A O     1 
ATOM   3057 C CB    . ASP A 1 401  ? 159.624 123.841 169.428 1.00 96.33  ? 401  ASP A CB    1 
ATOM   3058 C CG    . ASP A 1 401  ? 158.677 123.977 168.253 1.00 97.95  ? 401  ASP A CG    1 
ATOM   3059 O OD1   . ASP A 1 401  ? 157.531 123.490 168.351 1.00 98.97  ? 401  ASP A OD1   1 
ATOM   3060 O OD2   . ASP A 1 401  ? 159.079 124.571 167.231 1.00 95.17  ? 401  ASP A OD2   1 
ATOM   3061 N N     . CYS A 1 402  ? 160.388 123.735 172.500 1.00 93.53  ? 402  CYS A N     1 
ATOM   3062 C CA    . CYS A 1 402  ? 161.365 123.499 173.559 1.00 91.95  ? 402  CYS A CA    1 
ATOM   3063 C C     . CYS A 1 402  ? 160.862 122.459 174.553 1.00 92.23  ? 402  CYS A C     1 
ATOM   3064 O O     . CYS A 1 402  ? 161.621 121.582 174.987 1.00 89.96  ? 402  CYS A O     1 
ATOM   3065 C CB    . CYS A 1 402  ? 161.695 124.809 174.274 1.00 89.35  ? 402  CYS A CB    1 
ATOM   3066 S SG    . CYS A 1 402  ? 162.554 126.029 173.255 1.00 93.91  ? 402  CYS A SG    1 
ATOM   3067 N N     . GLN A 1 403  ? 159.582 122.543 174.929 1.00 91.86  ? 403  GLN A N     1 
ATOM   3068 C CA    . GLN A 1 403  ? 159.017 121.545 175.833 1.00 91.86  ? 403  GLN A CA    1 
ATOM   3069 C C     . GLN A 1 403  ? 159.035 120.157 175.204 1.00 95.26  ? 403  GLN A C     1 
ATOM   3070 O O     . GLN A 1 403  ? 159.344 119.165 175.876 1.00 95.08  ? 403  GLN A O     1 
ATOM   3071 C CB    . GLN A 1 403  ? 157.595 121.938 176.231 1.00 88.04  ? 403  GLN A CB    1 
ATOM   3072 C CG    . GLN A 1 403  ? 157.523 123.133 177.166 1.00 85.22  ? 403  GLN A CG    1 
ATOM   3073 C CD    . GLN A 1 403  ? 156.113 123.413 177.643 1.00 86.59  ? 403  GLN A CD    1 
ATOM   3074 O OE1   . GLN A 1 403  ? 155.227 123.728 176.849 1.00 90.17  ? 403  GLN A OE1   1 
ATOM   3075 N NE2   . GLN A 1 403  ? 155.895 123.293 178.948 1.00 82.64  ? 403  GLN A NE2   1 
ATOM   3076 N N     . ALA A 1 404  ? 158.709 120.067 173.913 1.00 96.36  ? 404  ALA A N     1 
ATOM   3077 C CA    . ALA A 1 404  ? 158.743 118.783 173.223 1.00 91.86  ? 404  ALA A CA    1 
ATOM   3078 C C     . ALA A 1 404  ? 160.162 118.237 173.147 1.00 93.10  ? 404  ALA A C     1 
ATOM   3079 O O     . ALA A 1 404  ? 160.375 117.029 173.287 1.00 96.38  ? 404  ALA A O     1 
ATOM   3080 C CB    . ALA A 1 404  ? 158.143 118.922 171.824 1.00 88.98  ? 404  ALA A CB    1 
ATOM   3081 N N     . LEU A 1 405  ? 161.144 119.110 172.915 1.00 95.37  ? 405  LEU A N     1 
ATOM   3082 C CA    . LEU A 1 405  ? 162.537 118.675 172.894 1.00 96.41  ? 405  LEU A CA    1 
ATOM   3083 C C     . LEU A 1 405  ? 162.966 118.136 174.252 1.00 93.61  ? 405  LEU A C     1 
ATOM   3084 O O     . LEU A 1 405  ? 163.639 117.099 174.336 1.00 93.83  ? 405  LEU A O     1 
ATOM   3085 C CB    . LEU A 1 405  ? 163.437 119.835 172.471 1.00 94.86  ? 405  LEU A CB    1 
ATOM   3086 C CG    . LEU A 1 405  ? 164.936 119.550 172.402 1.00 96.29  ? 405  LEU A CG    1 
ATOM   3087 C CD1   . LEU A 1 405  ? 165.230 118.543 171.306 1.00 103.97 ? 405  LEU A CD1   1 
ATOM   3088 C CD2   . LEU A 1 405  ? 165.715 120.836 172.179 1.00 91.18  ? 405  LEU A CD2   1 
ATOM   3089 N N     . LEU A 1 406  ? 162.583 118.827 175.329 1.00 94.60  ? 406  LEU A N     1 
ATOM   3090 C CA    . LEU A 1 406  ? 162.912 118.347 176.668 1.00 97.13  ? 406  LEU A CA    1 
ATOM   3091 C C     . LEU A 1 406  ? 162.259 116.999 176.946 1.00 104.54 ? 406  LEU A C     1 
ATOM   3092 O O     . LEU A 1 406  ? 162.902 116.086 177.481 1.00 109.21 ? 406  LEU A O     1 
ATOM   3093 C CB    . LEU A 1 406  ? 162.480 119.375 177.713 1.00 95.62  ? 406  LEU A CB    1 
ATOM   3094 C CG    . LEU A 1 406  ? 162.726 118.993 179.174 1.00 99.77  ? 406  LEU A CG    1 
ATOM   3095 C CD1   . LEU A 1 406  ? 164.216 118.919 179.469 1.00 97.08  ? 406  LEU A CD1   1 
ATOM   3096 C CD2   . LEU A 1 406  ? 162.034 119.971 180.111 1.00 98.19  ? 406  LEU A CD2   1 
ATOM   3097 N N     . THR A 1 407  ? 160.981 116.854 176.583 1.00 102.62 ? 407  THR A N     1 
ATOM   3098 C CA    . THR A 1 407  ? 160.288 115.587 176.794 1.00 104.66 ? 407  THR A CA    1 
ATOM   3099 C C     . THR A 1 407  ? 160.929 114.466 175.985 1.00 106.12 ? 407  THR A C     1 
ATOM   3100 O O     . THR A 1 407  ? 161.096 113.348 176.484 1.00 108.41 ? 407  THR A O     1 
ATOM   3101 C CB    . THR A 1 407  ? 158.810 115.731 176.433 1.00 100.39 ? 407  THR A CB    1 
ATOM   3102 O OG1   . THR A 1 407  ? 158.244 116.831 177.156 1.00 97.92  ? 407  THR A OG1   1 
ATOM   3103 C CG2   . THR A 1 407  ? 158.050 114.462 176.783 1.00 99.42  ? 407  THR A CG2   1 
ATOM   3104 N N     . ARG A 1 408  ? 161.292 114.749 174.733 1.00 103.31 ? 408  ARG A N     1 
ATOM   3105 C CA    . ARG A 1 408  ? 161.945 113.750 173.897 1.00 105.15 ? 408  ARG A CA    1 
ATOM   3106 C C     . ARG A 1 408  ? 163.274 113.314 174.494 1.00 108.29 ? 408  ARG A C     1 
ATOM   3107 O O     . ARG A 1 408  ? 163.580 112.118 174.535 1.00 112.46 ? 408  ARG A O     1 
ATOM   3108 C CB    . ARG A 1 408  ? 162.148 114.304 172.487 1.00 103.79 ? 408  ARG A CB    1 
ATOM   3109 C CG    . ARG A 1 408  ? 163.093 113.485 171.625 1.00 110.54 ? 408  ARG A CG    1 
ATOM   3110 C CD    . ARG A 1 408  ? 163.512 114.253 170.383 1.00 114.37 ? 408  ARG A CD    1 
ATOM   3111 N NE    . ARG A 1 408  ? 164.474 113.507 169.580 1.00 120.70 ? 408  ARG A NE    1 
ATOM   3112 C CZ    . ARG A 1 408  ? 165.069 113.979 168.493 1.00 122.18 ? 408  ARG A CZ    1 
ATOM   3113 N NH1   . ARG A 1 408  ? 164.830 115.202 168.050 1.00 117.46 ? 408  ARG A NH1   1 
ATOM   3114 N NH2   . ARG A 1 408  ? 165.925 113.204 167.834 1.00 123.01 ? 408  ARG A NH2   1 
ATOM   3115 N N     . TRP A 1 409  ? 164.080 114.271 174.963 1.00 107.17 ? 409  TRP A N     1 
ATOM   3116 C CA    . TRP A 1 409  ? 165.365 113.919 175.560 1.00 111.50 ? 409  TRP A CA    1 
ATOM   3117 C C     . TRP A 1 409  ? 165.175 113.084 176.821 1.00 112.21 ? 409  TRP A C     1 
ATOM   3118 O O     . TRP A 1 409  ? 165.887 112.091 177.033 1.00 115.05 ? 409  TRP A O     1 
ATOM   3119 C CB    . TRP A 1 409  ? 166.164 115.185 175.866 1.00 111.41 ? 409  TRP A CB    1 
ATOM   3120 C CG    . TRP A 1 409  ? 167.614 114.927 176.126 1.00 113.04 ? 409  TRP A CG    1 
ATOM   3121 C CD1   . TRP A 1 409  ? 168.275 113.742 175.983 1.00 114.70 ? 409  TRP A CD1   1 
ATOM   3122 C CD2   . TRP A 1 409  ? 168.586 115.877 176.575 1.00 112.84 ? 409  TRP A CD2   1 
ATOM   3123 N NE1   . TRP A 1 409  ? 169.599 113.895 176.315 1.00 115.14 ? 409  TRP A NE1   1 
ATOM   3124 C CE2   . TRP A 1 409  ? 169.815 115.197 176.682 1.00 114.67 ? 409  TRP A CE2   1 
ATOM   3125 C CE3   . TRP A 1 409  ? 168.537 117.236 176.897 1.00 110.27 ? 409  TRP A CE3   1 
ATOM   3126 C CZ2   . TRP A 1 409  ? 170.983 115.830 177.098 1.00 113.26 ? 409  TRP A CZ2   1 
ATOM   3127 C CZ3   . TRP A 1 409  ? 169.698 117.862 177.309 1.00 111.17 ? 409  TRP A CZ3   1 
ATOM   3128 C CH2   . TRP A 1 409  ? 170.904 117.159 177.406 1.00 112.05 ? 409  TRP A CH2   1 
ATOM   3129 N N     . GLN A 1 410  ? 164.213 113.465 177.667 1.00 109.50 ? 410  GLN A N     1 
ATOM   3130 C CA    . GLN A 1 410  ? 163.954 112.701 178.883 1.00 112.25 ? 410  GLN A CA    1 
ATOM   3131 C C     . GLN A 1 410  ? 163.494 111.284 178.562 1.00 115.68 ? 410  GLN A C     1 
ATOM   3132 O O     . GLN A 1 410  ? 163.922 110.323 179.212 1.00 116.64 ? 410  GLN A O     1 
ATOM   3133 C CB    . GLN A 1 410  ? 162.918 113.421 179.746 1.00 108.79 ? 410  GLN A CB    1 
ATOM   3134 C CG    . GLN A 1 410  ? 163.425 114.702 180.384 1.00 109.23 ? 410  GLN A CG    1 
ATOM   3135 C CD    . GLN A 1 410  ? 162.360 115.406 181.201 1.00 114.58 ? 410  GLN A CD    1 
ATOM   3136 O OE1   . GLN A 1 410  ? 161.171 115.117 181.072 1.00 116.39 ? 410  GLN A OE1   1 
ATOM   3137 N NE2   . GLN A 1 410  ? 162.783 116.335 182.050 1.00 108.07 ? 410  GLN A NE2   1 
ATOM   3138 N N     . GLN A 1 411  ? 162.618 111.134 177.566 1.00 115.73 ? 411  GLN A N     1 
ATOM   3139 C CA    . GLN A 1 411  ? 162.146 109.803 177.193 1.00 116.21 ? 411  GLN A CA    1 
ATOM   3140 C C     . GLN A 1 411  ? 163.267 108.964 176.593 1.00 114.86 ? 411  GLN A C     1 
ATOM   3141 O O     . GLN A 1 411  ? 163.343 107.755 176.840 1.00 116.12 ? 411  GLN A O     1 
ATOM   3142 C CB    . GLN A 1 411  ? 160.974 109.913 176.219 1.00 115.83 ? 411  GLN A CB    1 
ATOM   3143 C CG    . GLN A 1 411  ? 159.705 110.472 176.838 1.00 115.22 ? 411  GLN A CG    1 
ATOM   3144 C CD    . GLN A 1 411  ? 158.597 110.652 175.822 1.00 118.85 ? 411  GLN A CD    1 
ATOM   3145 O OE1   . GLN A 1 411  ? 158.787 110.406 174.631 1.00 114.99 ? 411  GLN A OE1   1 
ATOM   3146 N NE2   . GLN A 1 411  ? 157.431 111.083 176.288 1.00 114.29 ? 411  GLN A NE2   1 
ATOM   3147 N N     . GLU A 1 412  ? 164.138 109.581 175.790 1.00 113.71 ? 412  GLU A N     1 
ATOM   3148 C CA    . GLU A 1 412  ? 165.263 108.847 175.220 1.00 114.65 ? 412  GLU A CA    1 
ATOM   3149 C C     . GLU A 1 412  ? 166.204 108.355 176.312 1.00 112.93 ? 412  GLU A C     1 
ATOM   3150 O O     . GLU A 1 412  ? 166.634 107.196 176.301 1.00 110.03 ? 412  GLU A O     1 
ATOM   3151 C CB    . GLU A 1 412  ? 166.011 109.724 174.216 1.00 113.64 ? 412  GLU A CB    1 
ATOM   3152 C CG    . GLU A 1 412  ? 165.255 109.978 172.922 1.00 119.94 ? 412  GLU A CG    1 
ATOM   3153 C CD    . GLU A 1 412  ? 166.017 110.881 171.972 1.00 120.84 ? 412  GLU A CD    1 
ATOM   3154 O OE1   . GLU A 1 412  ? 167.169 111.240 172.289 1.00 120.61 ? 412  GLU A OE1   1 
ATOM   3155 O OE2   . GLU A 1 412  ? 165.463 111.232 170.909 1.00 119.57 ? 412  GLU A OE2   1 
ATOM   3156 N N     . ILE A 1 413  ? 166.535 109.223 177.270 1.00 114.36 ? 413  ILE A N     1 
ATOM   3157 C CA    . ILE A 1 413  ? 167.394 108.793 178.370 1.00 116.47 ? 413  ILE A CA    1 
ATOM   3158 C C     . ILE A 1 413  ? 166.643 107.845 179.300 1.00 118.01 ? 413  ILE A C     1 
ATOM   3159 O O     . ILE A 1 413  ? 167.176 106.807 179.712 1.00 118.23 ? 413  ILE A O     1 
ATOM   3160 C CB    . ILE A 1 413  ? 167.961 110.011 179.122 1.00 117.38 ? 413  ILE A CB    1 
ATOM   3161 C CG1   . ILE A 1 413  ? 169.149 110.589 178.347 1.00 116.60 ? 413  ILE A CG1   1 
ATOM   3162 C CG2   . ILE A 1 413  ? 168.356 109.633 180.544 1.00 114.00 ? 413  ILE A CG2   1 
ATOM   3163 C CD1   . ILE A 1 413  ? 170.087 111.434 179.180 1.00 114.83 ? 413  ILE A CD1   1 
ATOM   3164 N N     . GLU A 1 414  ? 165.399 108.173 179.633 1.00 119.92 ? 414  GLU A N     1 
ATOM   3165 C CA    . GLU A 1 414  ? 164.590 107.312 180.491 1.00 117.09 ? 414  GLU A CA    1 
ATOM   3166 C C     . GLU A 1 414  ? 163.414 106.719 179.723 1.00 114.31 ? 414  GLU A C     1 
ATOM   3167 O O     . GLU A 1 414  ? 162.255 106.995 180.032 1.00 113.29 ? 414  GLU A O     1 
ATOM   3168 C CB    . GLU A 1 414  ? 164.085 108.087 181.710 1.00 117.55 ? 414  GLU A CB    1 
ATOM   3169 C CG    . GLU A 1 414  ? 165.179 108.481 182.690 1.00 117.62 ? 414  GLU A CG    1 
ATOM   3170 C CD    . GLU A 1 414  ? 164.640 109.211 183.905 1.00 124.87 ? 414  GLU A CD    1 
ATOM   3171 O OE1   . GLU A 1 414  ? 163.475 109.661 183.862 1.00 125.05 ? 414  GLU A OE1   1 
ATOM   3172 O OE2   . GLU A 1 414  ? 165.380 109.333 184.903 1.00 124.95 ? 414  GLU A OE2   1 
ATOM   3173 N N     . ALA A 1 566  ? 153.007 140.411 137.488 1.00 53.93  ? 566  ALA A N     1 
ATOM   3174 C CA    . ALA A 1 566  ? 151.835 140.277 138.344 1.00 53.27  ? 566  ALA A CA    1 
ATOM   3175 C C     . ALA A 1 566  ? 150.954 141.517 138.256 1.00 57.78  ? 566  ALA A C     1 
ATOM   3176 O O     . ALA A 1 566  ? 151.419 142.635 138.463 1.00 52.70  ? 566  ALA A O     1 
ATOM   3177 C CB    . ALA A 1 566  ? 152.255 140.027 139.782 1.00 45.44  ? 566  ALA A CB    1 
ATOM   3178 N N     . GLU A 1 567  ? 149.681 141.310 137.943 1.00 62.76  ? 567  GLU A N     1 
ATOM   3179 C CA    . GLU A 1 567  ? 148.739 142.418 137.849 1.00 62.61  ? 567  GLU A CA    1 
ATOM   3180 C C     . GLU A 1 567  ? 148.282 142.825 139.245 1.00 62.12  ? 567  GLU A C     1 
ATOM   3181 O O     . GLU A 1 567  ? 147.773 141.979 139.989 1.00 60.36  ? 567  GLU A O     1 
ATOM   3182 C CB    . GLU A 1 567  ? 147.541 142.028 136.993 1.00 65.53  ? 567  GLU A CB    1 
ATOM   3183 C CG    . GLU A 1 567  ? 146.546 143.154 136.767 1.00 73.93  ? 567  GLU A CG    1 
ATOM   3184 C CD    . GLU A 1 567  ? 145.452 142.775 135.788 1.00 88.74  ? 567  GLU A CD    1 
ATOM   3185 O OE1   . GLU A 1 567  ? 145.555 141.695 135.169 1.00 93.83  ? 567  GLU A OE1   1 
ATOM   3186 O OE2   . GLU A 1 567  ? 144.489 143.555 135.637 1.00 87.47  ? 567  GLU A OE2   1 
ATOM   3187 N N     . PRO A 1 568  ? 148.448 144.085 139.641 1.00 55.35  ? 568  PRO A N     1 
ATOM   3188 C CA    . PRO A 1 568  ? 148.007 144.500 140.975 1.00 50.27  ? 568  PRO A CA    1 
ATOM   3189 C C     . PRO A 1 568  ? 146.492 144.488 141.096 1.00 55.08  ? 568  PRO A C     1 
ATOM   3190 O O     . PRO A 1 568  ? 145.763 144.673 140.118 1.00 57.68  ? 568  PRO A O     1 
ATOM   3191 C CB    . PRO A 1 568  ? 148.561 145.923 141.104 1.00 40.36  ? 568  PRO A CB    1 
ATOM   3192 C CG    . PRO A 1 568  ? 148.663 146.404 139.701 1.00 46.66  ? 568  PRO A CG    1 
ATOM   3193 C CD    . PRO A 1 568  ? 149.032 145.201 138.879 1.00 52.27  ? 568  PRO A CD    1 
ATOM   3194 N N     . GLU A 1 569  ? 146.023 144.264 142.319 1.00 45.65  ? 569  GLU A N     1 
ATOM   3195 C CA    . GLU A 1 569  ? 144.603 144.332 142.640 1.00 43.40  ? 569  GLU A CA    1 
ATOM   3196 C C     . GLU A 1 569  ? 144.329 145.696 143.262 1.00 47.62  ? 569  GLU A C     1 
ATOM   3197 O O     . GLU A 1 569  ? 144.677 145.939 144.421 1.00 49.11  ? 569  GLU A O     1 
ATOM   3198 C CB    . GLU A 1 569  ? 144.195 143.201 143.581 1.00 47.84  ? 569  GLU A CB    1 
ATOM   3199 C CG    . GLU A 1 569  ? 144.487 141.809 143.047 1.00 56.13  ? 569  GLU A CG    1 
ATOM   3200 C CD    . GLU A 1 569  ? 143.924 140.717 143.935 1.00 63.17  ? 569  GLU A CD    1 
ATOM   3201 O OE1   . GLU A 1 569  ? 142.966 140.994 144.686 1.00 53.26  ? 569  GLU A OE1   1 
ATOM   3202 O OE2   . GLU A 1 569  ? 144.442 139.582 143.884 1.00 63.21  ? 569  GLU A OE2   1 
ATOM   3203 N N     . ILE A 1 570  ? 143.717 146.581 142.488 1.00 49.70  ? 570  ILE A N     1 
ATOM   3204 C CA    . ILE A 1 570  ? 143.454 147.944 142.965 1.00 49.46  ? 570  ILE A CA    1 
ATOM   3205 C C     . ILE A 1 570  ? 142.296 147.915 143.955 1.00 51.03  ? 570  ILE A C     1 
ATOM   3206 O O     . ILE A 1 570  ? 141.300 147.207 143.715 1.00 50.28  ? 570  ILE A O     1 
ATOM   3207 C CB    . ILE A 1 570  ? 143.150 148.866 141.782 1.00 50.52  ? 570  ILE A CB    1 
ATOM   3208 C CG1   . ILE A 1 570  ? 144.237 148.729 140.715 1.00 48.66  ? 570  ILE A CG1   1 
ATOM   3209 C CG2   . ILE A 1 570  ? 143.048 150.311 142.235 1.00 45.72  ? 570  ILE A CG2   1 
ATOM   3210 C CD1   . ILE A 1 570  ? 145.627 149.032 141.220 1.00 45.01  ? 570  ILE A CD1   1 
ATOM   3211 N N     . PRO A 1 571  ? 142.377 148.637 145.073 1.00 49.44  ? 571  PRO A N     1 
ATOM   3212 C CA    . PRO A 1 571  ? 141.245 148.682 146.005 1.00 44.76  ? 571  PRO A CA    1 
ATOM   3213 C C     . PRO A 1 571  ? 140.001 149.263 145.352 1.00 47.80  ? 571  PRO A C     1 
ATOM   3214 O O     . PRO A 1 571  ? 140.072 150.167 144.517 1.00 43.94  ? 571  PRO A O     1 
ATOM   3215 C CB    . PRO A 1 571  ? 141.752 149.584 147.135 1.00 39.44  ? 571  PRO A CB    1 
ATOM   3216 C CG    . PRO A 1 571  ? 143.228 149.499 147.054 1.00 38.10  ? 571  PRO A CG    1 
ATOM   3217 C CD    . PRO A 1 571  ? 143.556 149.341 145.603 1.00 42.13  ? 571  PRO A CD    1 
ATOM   3218 N N     . LEU A 1 572  ? 138.845 148.728 145.748 1.00 50.28  ? 572  LEU A N     1 
ATOM   3219 C CA    . LEU A 1 572  ? 137.582 149.219 145.207 1.00 48.15  ? 572  LEU A CA    1 
ATOM   3220 C C     . LEU A 1 572  ? 137.238 150.602 145.745 1.00 48.85  ? 572  LEU A C     1 
ATOM   3221 O O     . LEU A 1 572  ? 136.499 151.350 145.095 1.00 52.33  ? 572  LEU A O     1 
ATOM   3222 C CB    . LEU A 1 572  ? 136.453 148.235 145.519 1.00 50.73  ? 572  LEU A CB    1 
ATOM   3223 C CG    . LEU A 1 572  ? 136.378 146.940 144.704 1.00 55.34  ? 572  LEU A CG    1 
ATOM   3224 C CD1   . LEU A 1 572  ? 136.542 147.226 143.218 1.00 55.20  ? 572  LEU A CD1   1 
ATOM   3225 C CD2   . LEU A 1 572  ? 137.392 145.907 145.178 1.00 50.50  ? 572  LEU A CD2   1 
ATOM   3226 N N     . SER A 1 573  ? 137.756 150.959 146.917 1.00 48.69  ? 573  SER A N     1 
ATOM   3227 C CA    . SER A 1 573  ? 137.446 152.236 147.544 1.00 48.53  ? 573  SER A CA    1 
ATOM   3228 C C     . SER A 1 573  ? 138.389 153.352 147.119 1.00 45.22  ? 573  SER A C     1 
ATOM   3229 O O     . SER A 1 573  ? 138.274 154.468 147.636 1.00 49.05  ? 573  SER A O     1 
ATOM   3230 C CB    . SER A 1 573  ? 137.471 152.096 149.068 1.00 52.38  ? 573  SER A CB    1 
ATOM   3231 O OG    . SER A 1 573  ? 138.752 151.699 149.519 1.00 49.02  ? 573  SER A OG    1 
ATOM   3232 N N     . LEU A 1 574  ? 139.322 153.080 146.212 1.00 42.58  ? 574  LEU A N     1 
ATOM   3233 C CA    . LEU A 1 574  ? 140.135 154.143 145.641 1.00 40.30  ? 574  LEU A CA    1 
ATOM   3234 C C     . LEU A 1 574  ? 139.264 155.055 144.787 1.00 46.41  ? 574  LEU A C     1 
ATOM   3235 O O     . LEU A 1 574  ? 138.426 154.591 144.010 1.00 48.59  ? 574  LEU A O     1 
ATOM   3236 C CB    . LEU A 1 574  ? 141.271 153.557 144.803 1.00 39.92  ? 574  LEU A CB    1 
ATOM   3237 C CG    . LEU A 1 574  ? 142.295 154.539 144.231 1.00 40.26  ? 574  LEU A CG    1 
ATOM   3238 C CD1   . LEU A 1 574  ? 143.118 155.171 145.338 1.00 36.44  ? 574  LEU A CD1   1 
ATOM   3239 C CD2   . LEU A 1 574  ? 143.198 153.852 143.223 1.00 39.60  ? 574  LEU A CD2   1 
ATOM   3240 N N     . LYS A 1 575  ? 139.461 156.361 144.941 1.00 49.11  ? 575  LYS A N     1 
ATOM   3241 C CA    . LYS A 1 575  ? 138.640 157.326 144.223 1.00 50.82  ? 575  LYS A CA    1 
ATOM   3242 C C     . LYS A 1 575  ? 138.872 157.221 142.721 1.00 59.97  ? 575  LYS A C     1 
ATOM   3243 O O     . LYS A 1 575  ? 139.997 157.007 142.261 1.00 62.04  ? 575  LYS A O     1 
ATOM   3244 C CB    . LYS A 1 575  ? 138.939 158.740 144.717 1.00 50.28  ? 575  LYS A CB    1 
ATOM   3245 C CG    . LYS A 1 575  ? 138.520 158.976 146.159 1.00 50.51  ? 575  LYS A CG    1 
ATOM   3246 C CD    . LYS A 1 575  ? 138.771 160.408 146.587 1.00 50.06  ? 575  LYS A CD    1 
ATOM   3247 C CE    . LYS A 1 575  ? 138.324 160.642 148.019 1.00 47.33  ? 575  LYS A CE    1 
ATOM   3248 N NZ    . LYS A 1 575  ? 138.640 162.023 148.474 1.00 49.65  ? 575  LYS A NZ    1 
ATOM   3249 N N     . GLU A 1 576  ? 137.788 157.373 141.955 1.00 63.92  ? 576  GLU A N     1 
ATOM   3250 C CA    . GLU A 1 576  ? 137.842 157.149 140.514 1.00 62.34  ? 576  GLU A CA    1 
ATOM   3251 C C     . GLU A 1 576  ? 138.745 158.143 139.795 1.00 64.01  ? 576  GLU A C     1 
ATOM   3252 O O     . GLU A 1 576  ? 139.218 157.845 138.692 1.00 67.53  ? 576  GLU A O     1 
ATOM   3253 C CB    . GLU A 1 576  ? 136.434 157.207 139.918 1.00 61.27  ? 576  GLU A CB    1 
ATOM   3254 C CG    . GLU A 1 576  ? 135.520 156.067 140.347 1.00 64.47  ? 576  GLU A CG    1 
ATOM   3255 C CD    . GLU A 1 576  ? 134.926 156.271 141.728 1.00 72.18  ? 576  GLU A CD    1 
ATOM   3256 O OE1   . GLU A 1 576  ? 135.091 157.373 142.292 1.00 68.38  ? 576  GLU A OE1   1 
ATOM   3257 O OE2   . GLU A 1 576  ? 134.291 155.329 142.248 1.00 69.66  ? 576  GLU A OE2   1 
ATOM   3258 N N     . HIS A 1 577  ? 139.000 159.308 140.384 1.00 60.20  ? 577  HIS A N     1 
ATOM   3259 C CA    . HIS A 1 577  ? 139.852 160.315 139.769 1.00 61.81  ? 577  HIS A CA    1 
ATOM   3260 C C     . HIS A 1 577  ? 141.320 160.139 140.129 1.00 60.15  ? 577  HIS A C     1 
ATOM   3261 O O     . HIS A 1 577  ? 142.145 160.974 139.745 1.00 60.68  ? 577  HIS A O     1 
ATOM   3262 C CB    . HIS A 1 577  ? 139.384 161.717 140.164 1.00 62.37  ? 577  HIS A CB    1 
ATOM   3263 C CG    . HIS A 1 577  ? 139.602 162.045 141.608 1.00 59.47  ? 577  HIS A CG    1 
ATOM   3264 N ND1   . HIS A 1 577  ? 140.700 162.748 142.054 1.00 59.67  ? 577  HIS A ND1   1 
ATOM   3265 C CD2   . HIS A 1 577  ? 138.862 161.767 142.707 1.00 58.72  ? 577  HIS A CD2   1 
ATOM   3266 C CE1   . HIS A 1 577  ? 140.627 162.890 143.365 1.00 60.21  ? 577  HIS A CE1   1 
ATOM   3267 N NE2   . HIS A 1 577  ? 139.521 162.302 143.786 1.00 60.27  ? 577  HIS A NE2   1 
ATOM   3268 N N     . ILE A 1 578  ? 141.662 159.079 140.857 1.00 60.63  ? 578  ILE A N     1 
ATOM   3269 C CA    . ILE A 1 578  ? 143.036 158.787 141.248 1.00 61.69  ? 578  ILE A CA    1 
ATOM   3270 C C     . ILE A 1 578  ? 143.521 157.597 140.435 1.00 62.07  ? 578  ILE A C     1 
ATOM   3271 O O     . ILE A 1 578  ? 142.889 156.534 140.442 1.00 61.15  ? 578  ILE A O     1 
ATOM   3272 C CB    . ILE A 1 578  ? 143.146 158.501 142.756 1.00 54.92  ? 578  ILE A CB    1 
ATOM   3273 C CG1   . ILE A 1 578  ? 142.753 159.736 143.567 1.00 52.88  ? 578  ILE A CG1   1 
ATOM   3274 C CG2   . ILE A 1 578  ? 144.554 158.048 143.109 1.00 54.29  ? 578  ILE A CG2   1 
ATOM   3275 C CD1   . ILE A 1 578  ? 143.613 160.946 143.289 1.00 53.32  ? 578  ILE A CD1   1 
ATOM   3276 N N     . ARG A 1 579  ? 144.636 157.777 139.733 1.00 57.80  ? 579  ARG A N     1 
ATOM   3277 C CA    . ARG A 1 579  ? 145.262 156.716 138.957 1.00 58.72  ? 579  ARG A CA    1 
ATOM   3278 C C     . ARG A 1 579  ? 146.649 156.438 139.512 1.00 60.63  ? 579  ARG A C     1 
ATOM   3279 O O     . ARG A 1 579  ? 147.449 157.364 139.684 1.00 61.48  ? 579  ARG A O     1 
ATOM   3280 C CB    . ARG A 1 579  ? 145.360 157.085 137.473 1.00 61.78  ? 579  ARG A CB    1 
ATOM   3281 C CG    . ARG A 1 579  ? 144.136 156.726 136.649 1.00 66.30  ? 579  ARG A CG    1 
ATOM   3282 C CD    . ARG A 1 579  ? 143.016 157.731 136.840 1.00 72.71  ? 579  ARG A CD    1 
ATOM   3283 N NE    . ARG A 1 579  ? 141.827 157.367 136.080 1.00 78.86  ? 579  ARG A NE    1 
ATOM   3284 C CZ    . ARG A 1 579  ? 140.771 158.153 135.923 1.00 80.33  ? 579  ARG A CZ    1 
ATOM   3285 N NH1   . ARG A 1 579  ? 140.726 159.364 136.453 1.00 82.28  ? 579  ARG A NH1   1 
ATOM   3286 N NH2   . ARG A 1 579  ? 139.735 157.713 135.214 1.00 74.94  ? 579  ARG A NH2   1 
ATOM   3287 N N     . LEU A 1 580  ? 146.929 155.170 139.792 1.00 54.98  ? 580  LEU A N     1 
ATOM   3288 C CA    . LEU A 1 580  ? 148.271 154.778 140.195 1.00 50.02  ? 580  LEU A CA    1 
ATOM   3289 C C     . LEU A 1 580  ? 149.217 154.843 139.004 1.00 47.33  ? 580  LEU A C     1 
ATOM   3290 O O     . LEU A 1 580  ? 148.846 154.510 137.876 1.00 49.22  ? 580  LEU A O     1 
ATOM   3291 C CB    . LEU A 1 580  ? 148.268 153.366 140.778 1.00 50.48  ? 580  LEU A CB    1 
ATOM   3292 C CG    . LEU A 1 580  ? 147.565 153.128 142.113 1.00 45.63  ? 580  LEU A CG    1 
ATOM   3293 C CD1   . LEU A 1 580  ? 147.747 151.687 142.544 1.00 44.76  ? 580  LEU A CD1   1 
ATOM   3294 C CD2   . LEU A 1 580  ? 148.103 154.065 143.168 1.00 43.83  ? 580  LEU A CD2   1 
ATOM   3295 N N     . LYS A 1 581  ? 150.449 155.273 139.259 1.00 45.22  ? 581  LYS A N     1 
ATOM   3296 C CA    . LYS A 1 581  ? 151.462 155.258 138.219 1.00 49.55  ? 581  LYS A CA    1 
ATOM   3297 C C     . LYS A 1 581  ? 151.873 153.819 137.916 1.00 49.60  ? 581  LYS A C     1 
ATOM   3298 O O     . LYS A 1 581  ? 151.520 152.878 138.631 1.00 49.38  ? 581  LYS A O     1 
ATOM   3299 C CB    . LYS A 1 581  ? 152.675 156.087 138.638 1.00 48.08  ? 581  LYS A CB    1 
ATOM   3300 C CG    . LYS A 1 581  ? 152.336 157.484 139.122 1.00 49.19  ? 581  LYS A CG    1 
ATOM   3301 C CD    . LYS A 1 581  ? 151.531 158.246 138.087 1.00 54.67  ? 581  LYS A CD    1 
ATOM   3302 C CE    . LYS A 1 581  ? 151.129 159.615 138.604 1.00 52.86  ? 581  LYS A CE    1 
ATOM   3303 N NZ    . LYS A 1 581  ? 150.263 160.338 137.634 1.00 56.85  ? 581  LYS A NZ    1 
ATOM   3304 N N     . ASP A 1 582  ? 152.625 153.650 136.826 1.00 52.95  ? 582  ASP A N     1 
ATOM   3305 C CA    . ASP A 1 582  ? 153.078 152.314 136.453 1.00 48.15  ? 582  ASP A CA    1 
ATOM   3306 C C     . ASP A 1 582  ? 153.972 151.717 137.532 1.00 44.81  ? 582  ASP A C     1 
ATOM   3307 O O     . ASP A 1 582  ? 153.826 150.543 137.894 1.00 49.44  ? 582  ASP A O     1 
ATOM   3308 C CB    . ASP A 1 582  ? 153.807 152.362 135.111 1.00 57.30  ? 582  ASP A CB    1 
ATOM   3309 C CG    . ASP A 1 582  ? 152.905 152.806 133.976 1.00 68.32  ? 582  ASP A CG    1 
ATOM   3310 O OD1   . ASP A 1 582  ? 151.706 153.045 134.228 1.00 66.59  ? 582  ASP A OD1   1 
ATOM   3311 O OD2   . ASP A 1 582  ? 153.394 152.918 132.833 1.00 69.49  ? 582  ASP A OD2   1 
ATOM   3312 N N     . HIS A 1 583  ? 154.893 152.517 138.073 1.00 43.61  ? 583  HIS A N     1 
ATOM   3313 C CA    . HIS A 1 583  ? 155.729 152.030 139.162 1.00 40.95  ? 583  HIS A CA    1 
ATOM   3314 C C     . HIS A 1 583  ? 154.917 151.811 140.430 1.00 43.07  ? 583  HIS A C     1 
ATOM   3315 O O     . HIS A 1 583  ? 155.211 150.891 141.197 1.00 44.84  ? 583  HIS A O     1 
ATOM   3316 C CB    . HIS A 1 583  ? 156.881 152.998 139.428 1.00 39.01  ? 583  HIS A CB    1 
ATOM   3317 C CG    . HIS A 1 583  ? 156.474 154.242 140.155 1.00 43.17  ? 583  HIS A CG    1 
ATOM   3318 N ND1   . HIS A 1 583  ? 155.908 155.325 139.519 1.00 47.48  ? 583  HIS A ND1   1 
ATOM   3319 C CD2   . HIS A 1 583  ? 156.560 154.576 141.463 1.00 40.81  ? 583  HIS A CD2   1 
ATOM   3320 C CE1   . HIS A 1 583  ? 155.660 156.272 140.405 1.00 47.75  ? 583  HIS A CE1   1 
ATOM   3321 N NE2   . HIS A 1 583  ? 156.045 155.842 141.593 1.00 47.49  ? 583  HIS A NE2   1 
ATOM   3322 N N     . GLN A 1 584  ? 153.892 152.631 140.664 1.00 41.94  ? 584  GLN A N     1 
ATOM   3323 C CA    . GLN A 1 584  ? 153.041 152.418 141.829 1.00 35.04  ? 584  GLN A CA    1 
ATOM   3324 C C     . GLN A 1 584  ? 152.230 151.137 141.692 1.00 34.63  ? 584  GLN A C     1 
ATOM   3325 O O     . GLN A 1 584  ? 152.063 150.397 142.667 1.00 39.07  ? 584  GLN A O     1 
ATOM   3326 C CB    . GLN A 1 584  ? 152.126 153.620 142.038 1.00 37.05  ? 584  GLN A CB    1 
ATOM   3327 C CG    . GLN A 1 584  ? 152.879 154.889 142.368 1.00 37.09  ? 584  GLN A CG    1 
ATOM   3328 C CD    . GLN A 1 584  ? 151.981 155.973 142.907 1.00 45.80  ? 584  GLN A CD    1 
ATOM   3329 O OE1   . GLN A 1 584  ? 150.852 156.146 142.453 1.00 55.15  ? 584  GLN A OE1   1 
ATOM   3330 N NE2   . GLN A 1 584  ? 152.476 156.707 143.892 1.00 50.26  ? 584  GLN A NE2   1 
ATOM   3331 N N     . ARG A 1 585  ? 151.720 150.857 140.491 1.00 39.46  ? 585  ARG A N     1 
ATOM   3332 C CA    . ARG A 1 585  ? 151.031 149.592 140.264 1.00 35.90  ? 585  ARG A CA    1 
ATOM   3333 C C     . ARG A 1 585  ? 151.979 148.414 140.446 1.00 33.71  ? 585  ARG A C     1 
ATOM   3334 O O     . ARG A 1 585  ? 151.610 147.397 141.046 1.00 33.31  ? 585  ARG A O     1 
ATOM   3335 C CB    . ARG A 1 585  ? 150.411 149.573 138.868 1.00 42.82  ? 585  ARG A CB    1 
ATOM   3336 C CG    . ARG A 1 585  ? 149.272 150.558 138.682 1.00 47.70  ? 585  ARG A CG    1 
ATOM   3337 C CD    . ARG A 1 585  ? 148.764 150.546 137.253 1.00 49.70  ? 585  ARG A CD    1 
ATOM   3338 N NE    . ARG A 1 585  ? 148.349 149.212 136.837 1.00 53.62  ? 585  ARG A NE    1 
ATOM   3339 C CZ    . ARG A 1 585  ? 147.112 148.746 136.940 1.00 56.52  ? 585  ARG A CZ    1 
ATOM   3340 N NH1   . ARG A 1 585  ? 146.134 149.484 137.439 1.00 49.66  ? 585  ARG A NH1   1 
ATOM   3341 N NH2   . ARG A 1 585  ? 146.849 147.508 136.531 1.00 60.97  ? 585  ARG A NH2   1 
ATOM   3342 N N     . GLU A 1 586  ? 153.208 148.536 139.939 1.00 38.76  ? 586  GLU A N     1 
ATOM   3343 C CA    . GLU A 1 586  ? 154.194 147.477 140.127 1.00 39.38  ? 586  GLU A CA    1 
ATOM   3344 C C     . GLU A 1 586  ? 154.491 147.261 141.606 1.00 36.40  ? 586  GLU A C     1 
ATOM   3345 O O     . GLU A 1 586  ? 154.601 146.120 142.064 1.00 41.01  ? 586  GLU A O     1 
ATOM   3346 C CB    . GLU A 1 586  ? 155.474 147.814 139.359 1.00 43.40  ? 586  GLU A CB    1 
ATOM   3347 C CG    . GLU A 1 586  ? 156.341 146.612 139.001 1.00 52.23  ? 586  GLU A CG    1 
ATOM   3348 C CD    . GLU A 1 586  ? 157.173 146.109 140.167 1.00 55.06  ? 586  GLU A CD    1 
ATOM   3349 O OE1   . GLU A 1 586  ? 157.447 146.903 141.089 1.00 55.32  ? 586  GLU A OE1   1 
ATOM   3350 O OE2   . GLU A 1 586  ? 157.552 144.918 140.159 1.00 51.45  ? 586  GLU A OE2   1 
ATOM   3351 N N     . GLY A 1 587  ? 154.617 148.348 142.368 1.00 34.87  ? 587  GLY A N     1 
ATOM   3352 C CA    . GLY A 1 587  ? 154.877 148.222 143.792 1.00 31.33  ? 587  GLY A CA    1 
ATOM   3353 C C     . GLY A 1 587  ? 153.725 147.596 144.553 1.00 27.36  ? 587  GLY A C     1 
ATOM   3354 O O     . GLY A 1 587  ? 153.936 146.768 145.443 1.00 30.92  ? 587  GLY A O     1 
ATOM   3355 N N     . VAL A 1 588  ? 152.493 147.986 144.221 1.00 26.14  ? 588  VAL A N     1 
ATOM   3356 C CA    . VAL A 1 588  ? 151.329 147.385 144.867 1.00 25.16  ? 588  VAL A CA    1 
ATOM   3357 C C     . VAL A 1 588  ? 151.257 145.897 144.552 1.00 29.76  ? 588  VAL A C     1 
ATOM   3358 O O     . VAL A 1 588  ? 150.993 145.072 145.436 1.00 36.12  ? 588  VAL A O     1 
ATOM   3359 C CB    . VAL A 1 588  ? 150.042 148.120 144.449 1.00 28.66  ? 588  VAL A CB    1 
ATOM   3360 C CG1   . VAL A 1 588  ? 148.816 147.369 144.937 1.00 28.90  ? 588  VAL A CG1   1 
ATOM   3361 C CG2   . VAL A 1 588  ? 150.043 149.536 144.993 1.00 27.11  ? 588  VAL A CG2   1 
ATOM   3362 N N     . ALA A 1 589  ? 151.494 145.528 143.290 1.00 30.31  ? 589  ALA A N     1 
ATOM   3363 C CA    . ALA A 1 589  ? 151.483 144.117 142.917 1.00 27.11  ? 589  ALA A CA    1 
ATOM   3364 C C     . ALA A 1 589  ? 152.576 143.344 143.642 1.00 28.60  ? 589  ALA A C     1 
ATOM   3365 O O     . ALA A 1 589  ? 152.352 142.217 144.095 1.00 36.17  ? 589  ALA A O     1 
ATOM   3366 C CB    . ALA A 1 589  ? 151.641 143.972 141.406 1.00 35.92  ? 589  ALA A CB    1 
ATOM   3367 N N     . TRP A 1 590  ? 153.768 143.933 143.757 1.00 28.23  ? 590  TRP A N     1 
ATOM   3368 C CA    . TRP A 1 590  ? 154.867 143.280 144.461 1.00 26.70  ? 590  TRP A CA    1 
ATOM   3369 C C     . TRP A 1 590  ? 154.528 143.070 145.931 1.00 31.74  ? 590  TRP A C     1 
ATOM   3370 O O     . TRP A 1 590  ? 154.764 141.990 146.489 1.00 38.53  ? 590  TRP A O     1 
ATOM   3371 C CB    . TRP A 1 590  ? 156.136 144.118 144.300 1.00 30.38  ? 590  TRP A CB    1 
ATOM   3372 C CG    . TRP A 1 590  ? 157.335 143.622 145.044 1.00 32.19  ? 590  TRP A CG    1 
ATOM   3373 C CD1   . TRP A 1 590  ? 158.171 142.612 144.673 1.00 29.03  ? 590  TRP A CD1   1 
ATOM   3374 C CD2   . TRP A 1 590  ? 157.854 144.142 146.272 1.00 32.01  ? 590  TRP A CD2   1 
ATOM   3375 N NE1   . TRP A 1 590  ? 159.172 142.461 145.601 1.00 27.66  ? 590  TRP A NE1   1 
ATOM   3376 C CE2   . TRP A 1 590  ? 158.999 143.389 146.593 1.00 30.28  ? 590  TRP A CE2   1 
ATOM   3377 C CE3   . TRP A 1 590  ? 157.457 145.166 147.137 1.00 32.28  ? 590  TRP A CE3   1 
ATOM   3378 C CZ2   . TRP A 1 590  ? 159.751 143.628 147.738 1.00 31.97  ? 590  TRP A CZ2   1 
ATOM   3379 C CZ3   . TRP A 1 590  ? 158.205 145.401 148.272 1.00 30.26  ? 590  TRP A CZ3   1 
ATOM   3380 C CH2   . TRP A 1 590  ? 159.338 144.637 148.562 1.00 31.64  ? 590  TRP A CH2   1 
ATOM   3381 N N     . LEU A 1 591  ? 153.958 144.093 146.573 1.00 30.27  ? 591  LEU A N     1 
ATOM   3382 C CA    . LEU A 1 591  ? 153.554 143.966 147.968 1.00 23.34  ? 591  LEU A CA    1 
ATOM   3383 C C     . LEU A 1 591  ? 152.498 142.883 148.140 1.00 28.71  ? 591  LEU A C     1 
ATOM   3384 O O     . LEU A 1 591  ? 152.578 142.073 149.069 1.00 36.94  ? 591  LEU A O     1 
ATOM   3385 C CB    . LEU A 1 591  ? 153.034 145.306 148.488 1.00 27.21  ? 591  LEU A CB    1 
ATOM   3386 C CG    . LEU A 1 591  ? 154.060 146.401 148.777 1.00 23.26  ? 591  LEU A CG    1 
ATOM   3387 C CD1   . LEU A 1 591  ? 153.381 147.748 148.930 1.00 21.16  ? 591  LEU A CD1   1 
ATOM   3388 C CD2   . LEU A 1 591  ? 154.843 146.065 150.026 1.00 25.25  ? 591  LEU A CD2   1 
ATOM   3389 N N     . GLN A 1 592  ? 151.506 142.845 147.246 1.00 27.66  ? 592  GLN A N     1 
ATOM   3390 C CA    . GLN A 1 592  ? 150.458 141.834 147.350 1.00 28.44  ? 592  GLN A CA    1 
ATOM   3391 C C     . GLN A 1 592  ? 151.015 140.430 147.150 1.00 32.10  ? 592  GLN A C     1 
ATOM   3392 O O     . GLN A 1 592  ? 150.639 139.497 147.871 1.00 34.68  ? 592  GLN A O     1 
ATOM   3393 C CB    . GLN A 1 592  ? 149.350 142.119 146.337 1.00 32.88  ? 592  GLN A CB    1 
ATOM   3394 C CG    . GLN A 1 592  ? 148.568 143.388 146.614 1.00 33.98  ? 592  GLN A CG    1 
ATOM   3395 C CD    . GLN A 1 592  ? 147.548 143.689 145.540 1.00 39.35  ? 592  GLN A CD    1 
ATOM   3396 O OE1   . GLN A 1 592  ? 147.407 142.939 144.576 1.00 40.23  ? 592  GLN A OE1   1 
ATOM   3397 N NE2   . GLN A 1 592  ? 146.829 144.792 145.700 1.00 38.93  ? 592  GLN A NE2   1 
ATOM   3398 N N     . GLN A 1 593  ? 151.909 140.257 146.174 1.00 31.84  ? 593  GLN A N     1 
ATOM   3399 C CA    . GLN A 1 593  ? 152.466 138.934 145.912 1.00 32.29  ? 593  GLN A CA    1 
ATOM   3400 C C     . GLN A 1 593  ? 153.353 138.469 147.058 1.00 34.20  ? 593  GLN A C     1 
ATOM   3401 O O     . GLN A 1 593  ? 153.360 137.281 147.398 1.00 42.85  ? 593  GLN A O     1 
ATOM   3402 C CB    . GLN A 1 593  ? 153.241 138.935 144.595 1.00 32.87  ? 593  GLN A CB    1 
ATOM   3403 C CG    . GLN A 1 593  ? 152.373 139.174 143.373 1.00 35.91  ? 593  GLN A CG    1 
ATOM   3404 C CD    . GLN A 1 593  ? 151.169 138.254 143.319 1.00 50.94  ? 593  GLN A CD    1 
ATOM   3405 O OE1   . GLN A 1 593  ? 151.285 137.045 143.519 1.00 55.11  ? 593  GLN A OE1   1 
ATOM   3406 N NE2   . GLN A 1 593  ? 150.002 138.827 143.054 1.00 39.83  ? 593  GLN A NE2   1 
ATOM   3407 N N     . LEU A 1 594  ? 154.113 139.384 147.662 1.00 33.22  ? 594  LEU A N     1 
ATOM   3408 C CA    . LEU A 1 594  ? 154.888 139.016 148.841 1.00 31.77  ? 594  LEU A CA    1 
ATOM   3409 C C     . LEU A 1 594  ? 153.988 138.720 150.034 1.00 31.89  ? 594  LEU A C     1 
ATOM   3410 O O     . LEU A 1 594  ? 154.330 137.876 150.869 1.00 37.81  ? 594  LEU A O     1 
ATOM   3411 C CB    . LEU A 1 594  ? 155.883 140.121 149.188 1.00 27.25  ? 594  LEU A CB    1 
ATOM   3412 C CG    . LEU A 1 594  ? 157.341 139.850 148.815 1.00 31.45  ? 594  LEU A CG    1 
ATOM   3413 C CD1   . LEU A 1 594  ? 157.511 139.761 147.310 1.00 36.64  ? 594  LEU A CD1   1 
ATOM   3414 C CD2   . LEU A 1 594  ? 158.241 140.917 149.396 1.00 26.95  ? 594  LEU A CD2   1 
ATOM   3415 N N     . PHE A 1 595  ? 152.843 139.397 150.133 1.00 31.04  ? 595  PHE A N     1 
ATOM   3416 C CA    . PHE A 1 595  ? 151.940 139.162 151.253 1.00 28.97  ? 595  PHE A CA    1 
ATOM   3417 C C     . PHE A 1 595  ? 151.188 137.846 151.112 1.00 32.86  ? 595  PHE A C     1 
ATOM   3418 O O     . PHE A 1 595  ? 150.828 137.232 152.121 1.00 38.98  ? 595  PHE A O     1 
ATOM   3419 C CB    . PHE A 1 595  ? 150.950 140.316 151.382 1.00 28.38  ? 595  PHE A CB    1 
ATOM   3420 C CG    . PHE A 1 595  ? 150.056 140.209 152.579 1.00 30.79  ? 595  PHE A CG    1 
ATOM   3421 C CD1   . PHE A 1 595  ? 150.484 140.655 153.815 1.00 28.75  ? 595  PHE A CD1   1 
ATOM   3422 C CD2   . PHE A 1 595  ? 148.793 139.658 152.472 1.00 31.04  ? 595  PHE A CD2   1 
ATOM   3423 C CE1   . PHE A 1 595  ? 149.672 140.554 154.921 1.00 28.13  ? 595  PHE A CE1   1 
ATOM   3424 C CE2   . PHE A 1 595  ? 147.978 139.554 153.575 1.00 35.98  ? 595  PHE A CE2   1 
ATOM   3425 C CZ    . PHE A 1 595  ? 148.419 140.003 154.801 1.00 32.79  ? 595  PHE A CZ    1 
ATOM   3426 N N     . LEU A 1 596  ? 150.930 137.401 149.882 1.00 34.98  ? 596  LEU A N     1 
ATOM   3427 C CA    . LEU A 1 596  ? 150.206 136.148 149.706 1.00 36.61  ? 596  LEU A CA    1 
ATOM   3428 C C     . LEU A 1 596  ? 151.009 134.936 150.161 1.00 39.45  ? 596  LEU A C     1 
ATOM   3429 O O     . LEU A 1 596  ? 150.435 133.850 150.292 1.00 44.81  ? 596  LEU A O     1 
ATOM   3430 C CB    . LEU A 1 596  ? 149.782 135.983 148.246 1.00 39.55  ? 596  LEU A CB    1 
ATOM   3431 C CG    . LEU A 1 596  ? 148.691 136.946 147.779 1.00 41.92  ? 596  LEU A CG    1 
ATOM   3432 C CD1   . LEU A 1 596  ? 148.203 136.580 146.386 1.00 47.06  ? 596  LEU A CD1   1 
ATOM   3433 C CD2   . LEU A 1 596  ? 147.536 136.973 148.768 1.00 37.67  ? 596  LEU A CD2   1 
ATOM   3434 N N     . ARG A 1 597  ? 152.310 135.093 150.403 1.00 41.53  ? 597  ARG A N     1 
ATOM   3435 C CA    . ARG A 1 597  ? 153.138 134.054 151.001 1.00 47.02  ? 597  ARG A CA    1 
ATOM   3436 C C     . ARG A 1 597  ? 153.824 134.565 152.265 1.00 44.50  ? 597  ARG A C     1 
ATOM   3437 O O     . ARG A 1 597  ? 154.936 134.149 152.594 1.00 43.56  ? 597  ARG A O     1 
ATOM   3438 C CB    . ARG A 1 597  ? 154.162 133.532 149.995 1.00 45.68  ? 597  ARG A CB    1 
ATOM   3439 C CG    . ARG A 1 597  ? 155.096 134.586 149.429 1.00 48.01  ? 597  ARG A CG    1 
ATOM   3440 C CD    . ARG A 1 597  ? 156.034 133.974 148.402 1.00 51.24  ? 597  ARG A CD    1 
ATOM   3441 N NE    . ARG A 1 597  ? 157.220 134.793 148.179 1.00 57.64  ? 597  ARG A NE    1 
ATOM   3442 C CZ    . ARG A 1 597  ? 157.326 135.722 147.240 1.00 54.73  ? 597  ARG A CZ    1 
ATOM   3443 N NH1   . ARG A 1 597  ? 156.329 135.984 146.412 1.00 51.42  ? 597  ARG A NH1   1 
ATOM   3444 N NH2   . ARG A 1 597  ? 158.462 136.404 147.128 1.00 43.88  ? 597  ARG A NH2   1 
ATOM   3445 N N     . SER A 1 598  ? 153.155 135.464 152.985 1.00 46.05  ? 598  SER A N     1 
ATOM   3446 C CA    . SER A 1 598  ? 153.696 136.145 154.157 1.00 38.43  ? 598  SER A CA    1 
ATOM   3447 C C     . SER A 1 598  ? 153.784 135.271 155.408 1.00 51.09  ? 598  SER A C     1 
ATOM   3448 O O     . SER A 1 598  ? 154.685 135.487 156.225 1.00 51.92  ? 598  SER A O     1 
ATOM   3449 C CB    . SER A 1 598  ? 152.867 137.392 154.470 1.00 35.69  ? 598  SER A CB    1 
ATOM   3450 O OG    . SER A 1 598  ? 153.354 138.039 155.630 1.00 39.88  ? 598  SER A OG    1 
ATOM   3451 N N     . PRO A 1 599  ? 152.861 134.324 155.651 1.00 54.61  ? 599  PRO A N     1 
ATOM   3452 C CA    . PRO A 1 599  ? 153.039 133.458 156.826 1.00 46.02  ? 599  PRO A CA    1 
ATOM   3453 C C     . PRO A 1 599  ? 154.170 132.451 156.674 1.00 55.65  ? 599  PRO A C     1 
ATOM   3454 O O     . PRO A 1 599  ? 154.953 132.255 157.608 1.00 53.78  ? 599  PRO A O     1 
ATOM   3455 C CB    . PRO A 1 599  ? 151.682 132.755 156.956 1.00 44.70  ? 599  PRO A CB    1 
ATOM   3456 C CG    . PRO A 1 599  ? 150.729 133.645 156.267 1.00 52.82  ? 599  PRO A CG    1 
ATOM   3457 C CD    . PRO A 1 599  ? 151.494 134.204 155.113 1.00 50.59  ? 599  PRO A CD    1 
ATOM   3458 N N     . GLU A 1 600  ? 154.278 131.815 155.505 1.00 58.77  ? 600  GLU A N     1 
ATOM   3459 C CA    . GLU A 1 600  ? 155.171 130.673 155.325 1.00 52.71  ? 600  GLU A CA    1 
ATOM   3460 C C     . GLU A 1 600  ? 156.504 131.054 154.687 1.00 54.37  ? 600  GLU A C     1 
ATOM   3461 O O     . GLU A 1 600  ? 157.563 130.829 155.280 1.00 57.52  ? 600  GLU A O     1 
ATOM   3462 C CB    . GLU A 1 600  ? 154.477 129.591 154.486 1.00 53.20  ? 600  GLU A CB    1 
ATOM   3463 C CG    . GLU A 1 600  ? 153.218 129.012 155.115 1.00 58.24  ? 600  GLU A CG    1 
ATOM   3464 C CD    . GLU A 1 600  ? 151.997 129.883 154.895 1.00 65.23  ? 600  GLU A CD    1 
ATOM   3465 O OE1   . GLU A 1 600  ? 152.033 130.740 153.987 1.00 61.65  ? 600  GLU A OE1   1 
ATOM   3466 O OE2   . GLU A 1 600  ? 151.003 129.712 155.631 1.00 62.67  ? 600  GLU A OE2   1 
ATOM   3467 N N     . GLU A 1 601  ? 156.474 131.627 153.483 1.00 51.14  ? 601  GLU A N     1 
ATOM   3468 C CA    . GLU A 1 601  ? 157.718 131.900 152.768 1.00 48.28  ? 601  GLU A CA    1 
ATOM   3469 C C     . GLU A 1 601  ? 158.374 133.183 153.263 1.00 48.14  ? 601  GLU A C     1 
ATOM   3470 O O     . GLU A 1 601  ? 159.487 133.157 153.797 1.00 49.23  ? 601  GLU A O     1 
ATOM   3471 C CB    . GLU A 1 601  ? 157.458 131.981 151.261 1.00 51.11  ? 601  GLU A CB    1 
ATOM   3472 C CG    . GLU A 1 601  ? 157.288 130.634 150.573 1.00 57.33  ? 601  GLU A CG    1 
ATOM   3473 C CD    . GLU A 1 601  ? 155.939 129.995 150.847 1.00 65.47  ? 601  GLU A CD    1 
ATOM   3474 O OE1   . GLU A 1 601  ? 155.037 130.693 151.356 1.00 66.29  ? 601  GLU A OE1   1 
ATOM   3475 O OE2   . GLU A 1 601  ? 155.782 128.793 150.553 1.00 63.02  ? 601  GLU A OE2   1 
ATOM   3476 N N     . THR A 1 602  ? 157.698 134.313 153.094 1.00 50.84  ? 602  THR A N     1 
ATOM   3477 C CA    . THR A 1 602  ? 158.238 135.594 153.515 1.00 45.87  ? 602  THR A CA    1 
ATOM   3478 C C     . THR A 1 602  ? 157.839 135.881 154.961 1.00 43.68  ? 602  THR A C     1 
ATOM   3479 O O     . THR A 1 602  ? 157.168 135.087 155.619 1.00 50.73  ? 602  THR A O     1 
ATOM   3480 C CB    . THR A 1 602  ? 157.766 136.707 152.580 1.00 43.94  ? 602  THR A CB    1 
ATOM   3481 O OG1   . THR A 1 602  ? 156.376 136.528 152.282 1.00 48.13  ? 602  THR A OG1   1 
ATOM   3482 C CG2   . THR A 1 602  ? 158.563 136.690 151.288 1.00 42.83  ? 602  THR A CG2   1 
ATOM   3483 N N     . ALA A 1 603  ? 158.315 137.009 155.480 1.00 38.75  ? 603  ALA A N     1 
ATOM   3484 C CA    . ALA A 1 603  ? 157.830 137.544 156.743 1.00 37.28  ? 603  ALA A CA    1 
ATOM   3485 C C     . ALA A 1 603  ? 157.749 139.061 156.737 1.00 34.67  ? 603  ALA A C     1 
ATOM   3486 O O     . ALA A 1 603  ? 157.434 139.649 157.776 1.00 33.37  ? 603  ALA A O     1 
ATOM   3487 C CB    . ALA A 1 603  ? 158.720 137.082 157.907 1.00 40.07  ? 603  ALA A CB    1 
ATOM   3488 N N     . GLY A 1 604  ? 158.023 139.704 155.615 1.00 33.17  ? 604  GLY A N     1 
ATOM   3489 C CA    . GLY A 1 604  ? 158.111 141.147 155.557 1.00 27.89  ? 604  GLY A CA    1 
ATOM   3490 C C     . GLY A 1 604  ? 158.874 141.564 154.320 1.00 33.44  ? 604  GLY A C     1 
ATOM   3491 O O     . GLY A 1 604  ? 159.291 140.737 153.510 1.00 40.13  ? 604  GLY A O     1 
ATOM   3492 N N     . CYS A 1 605  ? 159.050 142.875 154.189 1.00 31.13  ? 605  CYS A N     1 
ATOM   3493 C CA    . CYS A 1 605  ? 159.734 143.416 153.024 1.00 24.06  ? 605  CYS A CA    1 
ATOM   3494 C C     . CYS A 1 605  ? 160.302 144.784 153.361 1.00 28.21  ? 605  CYS A C     1 
ATOM   3495 O O     . CYS A 1 605  ? 159.966 145.385 154.384 1.00 33.75  ? 605  CYS A O     1 
ATOM   3496 C CB    . CYS A 1 605  ? 158.799 143.518 151.818 1.00 24.62  ? 605  CYS A CB    1 
ATOM   3497 S SG    . CYS A 1 605  ? 157.538 144.794 151.967 1.00 40.72  ? 605  CYS A SG    1 
ATOM   3498 N N     . LEU A 1 606  ? 161.179 145.261 152.482 1.00 30.89  ? 606  LEU A N     1 
ATOM   3499 C CA    . LEU A 1 606  ? 161.784 146.583 152.586 1.00 30.29  ? 606  LEU A CA    1 
ATOM   3500 C C     . LEU A 1 606  ? 161.408 147.376 151.341 1.00 34.57  ? 606  LEU A C     1 
ATOM   3501 O O     . LEU A 1 606  ? 161.903 147.091 150.246 1.00 42.54  ? 606  LEU A O     1 
ATOM   3502 C CB    . LEU A 1 606  ? 163.301 146.479 152.734 1.00 28.84  ? 606  LEU A CB    1 
ATOM   3503 C CG    . LEU A 1 606  ? 164.109 147.773 152.634 1.00 33.31  ? 606  LEU A CG    1 
ATOM   3504 C CD1   . LEU A 1 606  ? 163.783 148.714 153.779 1.00 35.25  ? 606  LEU A CD1   1 
ATOM   3505 C CD2   . LEU A 1 606  ? 165.596 147.468 152.600 1.00 42.72  ? 606  LEU A CD2   1 
ATOM   3506 N N     . LEU A 1 607  ? 160.531 148.363 151.505 1.00 35.95  ? 607  LEU A N     1 
ATOM   3507 C CA    . LEU A 1 607  ? 160.155 149.262 150.417 1.00 32.37  ? 607  LEU A CA    1 
ATOM   3508 C C     . LEU A 1 607  ? 161.100 150.455 150.469 1.00 39.01  ? 607  LEU A C     1 
ATOM   3509 O O     . LEU A 1 607  ? 160.925 151.367 151.279 1.00 40.98  ? 607  LEU A O     1 
ATOM   3510 C CB    . LEU A 1 607  ? 158.696 149.687 150.543 1.00 32.78  ? 607  LEU A CB    1 
ATOM   3511 C CG    . LEU A 1 607  ? 158.059 150.306 149.298 1.00 38.89  ? 607  LEU A CG    1 
ATOM   3512 C CD1   . LEU A 1 607  ? 157.966 149.279 148.186 1.00 38.64  ? 607  LEU A CD1   1 
ATOM   3513 C CD2   . LEU A 1 607  ? 156.688 150.870 149.617 1.00 44.46  ? 607  LEU A CD2   1 
ATOM   3514 N N     . ALA A 1 608  ? 162.110 150.450 149.599 1.00 40.54  ? 608  ALA A N     1 
ATOM   3515 C CA    . ALA A 1 608  ? 163.217 151.394 149.675 1.00 41.57  ? 608  ALA A CA    1 
ATOM   3516 C C     . ALA A 1 608  ? 163.228 152.386 148.516 1.00 47.87  ? 608  ALA A C     1 
ATOM   3517 O O     . ALA A 1 608  ? 164.289 152.883 148.133 1.00 55.34  ? 608  ALA A O     1 
ATOM   3518 C CB    . ALA A 1 608  ? 164.545 150.645 149.739 1.00 40.00  ? 608  ALA A CB    1 
ATOM   3519 N N     . ASP A 1 609  ? 162.062 152.693 147.955 1.00 47.35  ? 609  ASP A N     1 
ATOM   3520 C CA    . ASP A 1 609  ? 161.997 153.641 146.854 1.00 46.09  ? 609  ASP A CA    1 
ATOM   3521 C C     . ASP A 1 609  ? 162.425 155.031 147.318 1.00 50.90  ? 609  ASP A C     1 
ATOM   3522 O O     . ASP A 1 609  ? 162.349 155.375 148.500 1.00 53.62  ? 609  ASP A O     1 
ATOM   3523 C CB    . ASP A 1 609  ? 160.585 153.699 146.276 1.00 45.93  ? 609  ASP A CB    1 
ATOM   3524 C CG    . ASP A 1 609  ? 160.071 152.340 145.863 1.00 48.11  ? 609  ASP A CG    1 
ATOM   3525 O OD1   . ASP A 1 609  ? 159.841 151.497 146.752 1.00 45.65  ? 609  ASP A OD1   1 
ATOM   3526 O OD2   . ASP A 1 609  ? 159.897 152.113 144.649 1.00 51.62  ? 609  ASP A OD2   1 
ATOM   3527 N N     . ASP A 1 610  ? 162.887 155.834 146.364 1.00 57.37  ? 610  ASP A N     1 
ATOM   3528 C CA    . ASP A 1 610  ? 163.290 157.196 146.670 1.00 59.29  ? 610  ASP A CA    1 
ATOM   3529 C C     . ASP A 1 610  ? 162.076 158.035 147.060 1.00 59.38  ? 610  ASP A C     1 
ATOM   3530 O O     . ASP A 1 610  ? 160.923 157.674 146.807 1.00 59.18  ? 610  ASP A O     1 
ATOM   3531 C CB    . ASP A 1 610  ? 164.009 157.827 145.478 1.00 58.06  ? 610  ASP A CB    1 
ATOM   3532 C CG    . ASP A 1 610  ? 165.469 157.441 145.410 1.00 61.78  ? 610  ASP A CG    1 
ATOM   3533 O OD1   . ASP A 1 610  ? 165.936 156.722 146.317 1.00 61.65  ? 610  ASP A OD1   1 
ATOM   3534 O OD2   . ASP A 1 610  ? 166.151 157.858 144.452 1.00 63.07  ? 610  ASP A OD2   1 
ATOM   3535 N N     . MET A 1 611  ? 162.349 159.168 147.700 1.00 60.46  ? 611  MET A N     1 
ATOM   3536 C CA    . MET A 1 611  ? 161.292 160.088 148.082 1.00 63.20  ? 611  MET A CA    1 
ATOM   3537 C C     . MET A 1 611  ? 160.648 160.701 146.846 1.00 60.29  ? 611  MET A C     1 
ATOM   3538 O O     . MET A 1 611  ? 161.306 160.954 145.834 1.00 62.69  ? 611  MET A O     1 
ATOM   3539 C CB    . MET A 1 611  ? 161.835 161.192 148.988 1.00 67.86  ? 611  MET A CB    1 
ATOM   3540 C CG    . MET A 1 611  ? 162.242 160.725 150.377 1.00 74.37  ? 611  MET A CG    1 
ATOM   3541 S SD    . MET A 1 611  ? 160.840 160.245 151.407 1.00 90.78  ? 611  MET A SD    1 
ATOM   3542 C CE    . MET A 1 611  ? 160.916 158.458 151.296 1.00 66.63  ? 611  MET A CE    1 
ATOM   3543 N N     . GLY A 1 612  ? 159.346 160.941 146.940 1.00 59.24  ? 612  GLY A N     1 
ATOM   3544 C CA    . GLY A 1 612  ? 158.594 161.490 145.836 1.00 59.08  ? 612  GLY A CA    1 
ATOM   3545 C C     . GLY A 1 612  ? 158.046 160.478 144.859 1.00 58.73  ? 612  GLY A C     1 
ATOM   3546 O O     . GLY A 1 612  ? 157.497 160.877 143.826 1.00 68.74  ? 612  GLY A O     1 
ATOM   3547 N N     . LEU A 1 613  ? 158.174 159.184 145.145 1.00 53.44  ? 613  LEU A N     1 
ATOM   3548 C CA    . LEU A 1 613  ? 157.629 158.139 144.290 1.00 51.43  ? 613  LEU A CA    1 
ATOM   3549 C C     . LEU A 1 613  ? 156.264 157.657 144.756 1.00 51.91  ? 613  LEU A C     1 
ATOM   3550 O O     . LEU A 1 613  ? 155.751 156.669 144.221 1.00 51.02  ? 613  LEU A O     1 
ATOM   3551 C CB    . LEU A 1 613  ? 158.593 156.954 144.208 1.00 54.75  ? 613  LEU A CB    1 
ATOM   3552 C CG    . LEU A 1 613  ? 159.988 157.186 143.625 1.00 53.54  ? 613  LEU A CG    1 
ATOM   3553 C CD1   . LEU A 1 613  ? 160.548 155.885 143.079 1.00 47.65  ? 613  LEU A CD1   1 
ATOM   3554 C CD2   . LEU A 1 613  ? 159.973 158.259 142.551 1.00 56.41  ? 613  LEU A CD2   1 
ATOM   3555 N N     . GLY A 1 614  ? 155.667 158.327 145.735 1.00 59.99  ? 614  GLY A N     1 
ATOM   3556 C CA    . GLY A 1 614  ? 154.370 157.920 146.244 1.00 51.82  ? 614  GLY A CA    1 
ATOM   3557 C C     . GLY A 1 614  ? 154.366 156.586 146.956 1.00 44.31  ? 614  GLY A C     1 
ATOM   3558 O O     . GLY A 1 614  ? 153.464 155.771 146.730 1.00 42.35  ? 614  GLY A O     1 
ATOM   3559 N N     . LYS A 1 615  ? 155.358 156.339 147.816 1.00 47.89  ? 615  LYS A N     1 
ATOM   3560 C CA    . LYS A 1 615  ? 155.366 155.110 148.602 1.00 43.39  ? 615  LYS A CA    1 
ATOM   3561 C C     . LYS A 1 615  ? 154.173 155.059 149.545 1.00 42.14  ? 615  LYS A C     1 
ATOM   3562 O O     . LYS A 1 615  ? 153.615 153.984 149.796 1.00 41.01  ? 615  LYS A O     1 
ATOM   3563 C CB    . LYS A 1 615  ? 156.671 154.996 149.388 1.00 45.19  ? 615  LYS A CB    1 
ATOM   3564 C CG    . LYS A 1 615  ? 157.907 154.844 148.524 1.00 53.84  ? 615  LYS A CG    1 
ATOM   3565 C CD    . LYS A 1 615  ? 159.162 155.184 149.306 1.00 53.50  ? 615  LYS A CD    1 
ATOM   3566 C CE    . LYS A 1 615  ? 159.290 154.331 150.551 1.00 40.51  ? 615  LYS A CE    1 
ATOM   3567 N NZ    . LYS A 1 615  ? 160.500 154.699 151.332 1.00 49.08  ? 615  LYS A NZ    1 
ATOM   3568 N N     . THR A 1 616  ? 153.770 156.215 150.078 1.00 46.65  ? 616  THR A N     1 
ATOM   3569 C CA    . THR A 1 616  ? 152.607 156.263 150.956 1.00 38.62  ? 616  THR A CA    1 
ATOM   3570 C C     . THR A 1 616  ? 151.362 155.756 150.244 1.00 34.22  ? 616  THR A C     1 
ATOM   3571 O O     . THR A 1 616  ? 150.595 154.971 150.808 1.00 36.73  ? 616  THR A O     1 
ATOM   3572 C CB    . THR A 1 616  ? 152.390 157.689 151.465 1.00 41.89  ? 616  THR A CB    1 
ATOM   3573 O OG1   . THR A 1 616  ? 153.510 158.092 152.261 1.00 54.80  ? 616  THR A OG1   1 
ATOM   3574 C CG2   . THR A 1 616  ? 151.127 157.774 152.304 1.00 36.67  ? 616  THR A CG2   1 
ATOM   3575 N N     . LEU A 1 617  ? 151.155 156.179 148.995 1.00 39.36  ? 617  LEU A N     1 
ATOM   3576 C CA    . LEU A 1 617  ? 149.987 155.726 148.247 1.00 38.78  ? 617  LEU A CA    1 
ATOM   3577 C C     . LEU A 1 617  ? 150.060 154.234 147.945 1.00 37.11  ? 617  LEU A C     1 
ATOM   3578 O O     . LEU A 1 617  ? 149.040 153.541 147.996 1.00 37.01  ? 617  LEU A O     1 
ATOM   3579 C CB    . LEU A 1 617  ? 149.843 156.531 146.957 1.00 41.19  ? 617  LEU A CB    1 
ATOM   3580 C CG    . LEU A 1 617  ? 148.623 156.205 146.094 1.00 41.15  ? 617  LEU A CG    1 
ATOM   3581 C CD1   . LEU A 1 617  ? 147.352 156.200 146.929 1.00 43.18  ? 617  LEU A CD1   1 
ATOM   3582 C CD2   . LEU A 1 617  ? 148.501 157.196 144.955 1.00 42.95  ? 617  LEU A CD2   1 
ATOM   3583 N N     . GLN A 1 618  ? 151.250 153.719 147.630 1.00 33.46  ? 618  GLN A N     1 
ATOM   3584 C CA    . GLN A 1 618  ? 151.389 152.287 147.370 1.00 28.89  ? 618  GLN A CA    1 
ATOM   3585 C C     . GLN A 1 618  ? 151.055 151.468 148.611 1.00 30.75  ? 618  GLN A C     1 
ATOM   3586 O O     . GLN A 1 618  ? 150.311 150.481 148.538 1.00 33.56  ? 618  GLN A O     1 
ATOM   3587 C CB    . GLN A 1 618  ? 152.806 151.969 146.896 1.00 33.71  ? 618  GLN A CB    1 
ATOM   3588 C CG    . GLN A 1 618  ? 153.260 152.739 145.674 1.00 37.54  ? 618  GLN A CG    1 
ATOM   3589 C CD    . GLN A 1 618  ? 154.709 152.464 145.334 1.00 37.43  ? 618  GLN A CD    1 
ATOM   3590 O OE1   . GLN A 1 618  ? 155.229 151.386 145.617 1.00 36.39  ? 618  GLN A OE1   1 
ATOM   3591 N NE2   . GLN A 1 618  ? 155.372 153.442 144.731 1.00 41.18  ? 618  GLN A NE2   1 
ATOM   3592 N N     . ILE A 1 619  ? 151.594 151.867 149.765 1.00 32.93  ? 619  ILE A N     1 
ATOM   3593 C CA    . ILE A 1 619  ? 151.331 151.127 150.996 1.00 28.44  ? 619  ILE A CA    1 
ATOM   3594 C C     . ILE A 1 619  ? 149.869 151.262 151.398 1.00 24.39  ? 619  ILE A C     1 
ATOM   3595 O O     . ILE A 1 619  ? 149.259 150.310 151.894 1.00 29.22  ? 619  ILE A O     1 
ATOM   3596 C CB    . ILE A 1 619  ? 152.271 151.597 152.119 1.00 27.32  ? 619  ILE A CB    1 
ATOM   3597 C CG1   . ILE A 1 619  ? 153.727 151.450 151.688 1.00 27.40  ? 619  ILE A CG1   1 
ATOM   3598 C CG2   . ILE A 1 619  ? 152.020 150.801 153.387 1.00 30.65  ? 619  ILE A CG2   1 
ATOM   3599 C CD1   . ILE A 1 619  ? 154.653 152.389 152.403 1.00 34.41  ? 619  ILE A CD1   1 
ATOM   3600 N N     . LEU A 1 620  ? 149.284 152.444 151.195 1.00 23.45  ? 620  LEU A N     1 
ATOM   3601 C CA    . LEU A 1 620  ? 147.871 152.631 151.496 1.00 21.24  ? 620  LEU A CA    1 
ATOM   3602 C C     . LEU A 1 620  ? 146.999 151.758 150.606 1.00 21.98  ? 620  LEU A C     1 
ATOM   3603 O O     . LEU A 1 620  ? 146.027 151.163 151.078 1.00 25.84  ? 620  LEU A O     1 
ATOM   3604 C CB    . LEU A 1 620  ? 147.495 154.104 151.344 1.00 22.43  ? 620  LEU A CB    1 
ATOM   3605 C CG    . LEU A 1 620  ? 146.953 154.841 152.571 1.00 27.41  ? 620  LEU A CG    1 
ATOM   3606 C CD1   . LEU A 1 620  ? 147.060 153.995 153.830 1.00 31.52  ? 620  LEU A CD1   1 
ATOM   3607 C CD2   . LEU A 1 620  ? 147.679 156.162 152.754 1.00 33.33  ? 620  LEU A CD2   1 
ATOM   3608 N N     . SER A 1 621  ? 147.333 151.664 149.317 1.00 22.76  ? 621  SER A N     1 
ATOM   3609 C CA    . SER A 1 621  ? 146.587 150.792 148.419 1.00 23.62  ? 621  SER A CA    1 
ATOM   3610 C C     . SER A 1 621  ? 146.716 149.336 148.841 1.00 29.74  ? 621  SER A C     1 
ATOM   3611 O O     . SER A 1 621  ? 145.731 148.591 148.835 1.00 33.64  ? 621  SER A O     1 
ATOM   3612 C CB    . SER A 1 621  ? 147.074 150.979 146.983 1.00 23.72  ? 621  SER A CB    1 
ATOM   3613 O OG    . SER A 1 621  ? 147.026 152.341 146.599 1.00 31.82  ? 621  SER A OG    1 
ATOM   3614 N N     . PHE A 1 622  ? 147.923 148.920 149.226 1.00 30.65  ? 622  PHE A N     1 
ATOM   3615 C CA    . PHE A 1 622  ? 148.130 147.553 149.696 1.00 26.21  ? 622  PHE A CA    1 
ATOM   3616 C C     . PHE A 1 622  ? 147.300 147.267 150.946 1.00 28.56  ? 622  PHE A C     1 
ATOM   3617 O O     . PHE A 1 622  ? 146.614 146.239 151.033 1.00 31.04  ? 622  PHE A O     1 
ATOM   3618 C CB    . PHE A 1 622  ? 149.625 147.337 149.948 1.00 24.54  ? 622  PHE A CB    1 
ATOM   3619 C CG    . PHE A 1 622  ? 149.954 146.054 150.650 1.00 28.26  ? 622  PHE A CG    1 
ATOM   3620 C CD1   . PHE A 1 622  ? 149.458 144.847 150.194 1.00 31.59  ? 622  PHE A CD1   1 
ATOM   3621 C CD2   . PHE A 1 622  ? 150.793 146.055 151.750 1.00 20.94  ? 622  PHE A CD2   1 
ATOM   3622 C CE1   . PHE A 1 622  ? 149.771 143.672 150.839 1.00 26.71  ? 622  PHE A CE1   1 
ATOM   3623 C CE2   . PHE A 1 622  ? 151.113 144.883 152.392 1.00 25.52  ? 622  PHE A CE2   1 
ATOM   3624 C CZ    . PHE A 1 622  ? 150.600 143.691 151.938 1.00 25.25  ? 622  PHE A CZ    1 
ATOM   3625 N N     . LEU A 1 623  ? 147.325 148.188 151.913 1.00 26.43  ? 623  LEU A N     1 
ATOM   3626 C CA    . LEU A 1 623  ? 146.569 148.007 153.149 1.00 21.04  ? 623  LEU A CA    1 
ATOM   3627 C C     . LEU A 1 623  ? 145.069 147.966 152.890 1.00 29.98  ? 623  LEU A C     1 
ATOM   3628 O O     . LEU A 1 623  ? 144.359 147.125 153.450 1.00 34.02  ? 623  LEU A O     1 
ATOM   3629 C CB    . LEU A 1 623  ? 146.900 149.127 154.134 1.00 19.40  ? 623  LEU A CB    1 
ATOM   3630 C CG    . LEU A 1 623  ? 148.286 149.128 154.772 1.00 22.35  ? 623  LEU A CG    1 
ATOM   3631 C CD1   . LEU A 1 623  ? 148.506 150.416 155.535 1.00 23.29  ? 623  LEU A CD1   1 
ATOM   3632 C CD2   . LEU A 1 623  ? 148.445 147.936 155.691 1.00 24.67  ? 623  LEU A CD2   1 
ATOM   3633 N N     . VAL A 1 624  ? 144.565 148.873 152.052 1.00 30.97  ? 624  VAL A N     1 
ATOM   3634 C CA    . VAL A 1 624  ? 143.130 148.928 151.793 1.00 27.57  ? 624  VAL A CA    1 
ATOM   3635 C C     . VAL A 1 624  ? 142.679 147.703 151.009 1.00 32.90  ? 624  VAL A C     1 
ATOM   3636 O O     . VAL A 1 624  ? 141.592 147.161 151.251 1.00 36.82  ? 624  VAL A O     1 
ATOM   3637 C CB    . VAL A 1 624  ? 142.772 150.241 151.073 1.00 27.90  ? 624  VAL A CB    1 
ATOM   3638 C CG1   . VAL A 1 624  ? 141.310 150.247 150.682 1.00 42.25  ? 624  VAL A CG1   1 
ATOM   3639 C CG2   . VAL A 1 624  ? 143.077 151.429 151.968 1.00 25.78  ? 624  VAL A CG2   1 
ATOM   3640 N N     . TRP A 1 625  ? 143.502 147.239 150.064 1.00 33.81  ? 625  TRP A N     1 
ATOM   3641 C CA    . TRP A 1 625  ? 143.192 146.001 149.362 1.00 36.97  ? 625  TRP A CA    1 
ATOM   3642 C C     . TRP A 1 625  ? 143.126 144.831 150.329 1.00 38.91  ? 625  TRP A C     1 
ATOM   3643 O O     . TRP A 1 625  ? 142.237 143.980 150.224 1.00 41.37  ? 625  TRP A O     1 
ATOM   3644 C CB    . TRP A 1 625  ? 144.232 145.726 148.275 1.00 34.92  ? 625  TRP A CB    1 
ATOM   3645 C CG    . TRP A 1 625  ? 144.288 144.279 147.877 1.00 36.45  ? 625  TRP A CG    1 
ATOM   3646 C CD1   . TRP A 1 625  ? 143.500 143.649 146.961 1.00 40.91  ? 625  TRP A CD1   1 
ATOM   3647 C CD2   . TRP A 1 625  ? 145.176 143.279 148.396 1.00 38.98  ? 625  TRP A CD2   1 
ATOM   3648 N NE1   . TRP A 1 625  ? 143.842 142.322 146.873 1.00 46.81  ? 625  TRP A NE1   1 
ATOM   3649 C CE2   . TRP A 1 625  ? 144.867 142.069 147.746 1.00 41.34  ? 625  TRP A CE2   1 
ATOM   3650 C CE3   . TRP A 1 625  ? 146.200 143.290 149.348 1.00 36.36  ? 625  TRP A CE3   1 
ATOM   3651 C CZ2   . TRP A 1 625  ? 145.548 140.884 148.014 1.00 38.59  ? 625  TRP A CZ2   1 
ATOM   3652 C CZ3   . TRP A 1 625  ? 146.872 142.113 149.613 1.00 32.98  ? 625  TRP A CZ3   1 
ATOM   3653 C CH2   . TRP A 1 625  ? 146.544 140.927 148.949 1.00 36.53  ? 625  TRP A CH2   1 
ATOM   3654 N N     . PHE A 1 626  ? 144.066 144.766 151.275 1.00 37.69  ? 626  PHE A N     1 
ATOM   3655 C CA    . PHE A 1 626  ? 144.027 143.698 152.266 1.00 30.76  ? 626  PHE A CA    1 
ATOM   3656 C C     . PHE A 1 626  ? 142.771 143.782 153.125 1.00 34.59  ? 626  PHE A C     1 
ATOM   3657 O O     . PHE A 1 626  ? 142.139 142.760 153.415 1.00 40.96  ? 626  PHE A O     1 
ATOM   3658 C CB    . PHE A 1 626  ? 145.276 143.748 153.143 1.00 26.82  ? 626  PHE A CB    1 
ATOM   3659 C CG    . PHE A 1 626  ? 145.181 142.887 154.361 1.00 27.63  ? 626  PHE A CG    1 
ATOM   3660 C CD1   . PHE A 1 626  ? 145.322 141.517 154.265 1.00 29.38  ? 626  PHE A CD1   1 
ATOM   3661 C CD2   . PHE A 1 626  ? 144.932 143.444 155.600 1.00 28.40  ? 626  PHE A CD2   1 
ATOM   3662 C CE1   . PHE A 1 626  ? 145.223 140.720 155.380 1.00 30.36  ? 626  PHE A CE1   1 
ATOM   3663 C CE2   . PHE A 1 626  ? 144.831 142.650 156.715 1.00 31.29  ? 626  PHE A CE2   1 
ATOM   3664 C CZ    . PHE A 1 626  ? 144.981 141.286 156.604 1.00 32.65  ? 626  PHE A CZ    1 
ATOM   3665 N N     . ILE A 1 627  ? 142.400 144.992 153.547 1.00 35.09  ? 627  ILE A N     1 
ATOM   3666 C CA    . ILE A 1 627  ? 141.229 145.162 154.404 1.00 33.09  ? 627  ILE A CA    1 
ATOM   3667 C C     . ILE A 1 627  ? 139.962 144.734 153.674 1.00 43.86  ? 627  ILE A C     1 
ATOM   3668 O O     . ILE A 1 627  ? 139.110 144.035 154.235 1.00 53.20  ? 627  ILE A O     1 
ATOM   3669 C CB    . ILE A 1 627  ? 141.134 146.617 154.894 1.00 31.45  ? 627  ILE A CB    1 
ATOM   3670 C CG1   . ILE A 1 627  ? 142.300 146.940 155.825 1.00 29.49  ? 627  ILE A CG1   1 
ATOM   3671 C CG2   . ILE A 1 627  ? 139.810 146.860 155.595 1.00 32.23  ? 627  ILE A CG2   1 
ATOM   3672 C CD1   . ILE A 1 627  ? 142.374 148.390 156.207 1.00 27.85  ? 627  ILE A CD1   1 
ATOM   3673 N N     . GLU A 1 628  ? 139.814 145.149 152.415 1.00 40.27  ? 628  GLU A N     1 
ATOM   3674 C CA    . GLU A 1 628  ? 138.629 144.775 151.649 1.00 37.37  ? 628  GLU A CA    1 
ATOM   3675 C C     . GLU A 1 628  ? 138.618 143.284 151.332 1.00 42.68  ? 628  GLU A C     1 
ATOM   3676 O O     . GLU A 1 628  ? 137.557 142.650 151.341 1.00 48.67  ? 628  GLU A O     1 
ATOM   3677 C CB    . GLU A 1 628  ? 138.560 145.596 150.363 1.00 44.07  ? 628  GLU A CB    1 
ATOM   3678 C CG    . GLU A 1 628  ? 138.456 147.094 150.588 1.00 49.25  ? 628  GLU A CG    1 
ATOM   3679 C CD    . GLU A 1 628  ? 138.900 147.893 149.380 1.00 56.17  ? 628  GLU A CD    1 
ATOM   3680 O OE1   . GLU A 1 628  ? 139.580 147.319 148.504 1.00 54.91  ? 628  GLU A OE1   1 
ATOM   3681 O OE2   . GLU A 1 628  ? 138.571 149.095 149.306 1.00 51.79  ? 628  GLU A OE2   1 
ATOM   3682 N N     . LYS A 1 629  ? 139.788 142.711 151.045 1.00 43.05  ? 629  LYS A N     1 
ATOM   3683 C CA    . LYS A 1 629  ? 139.860 141.311 150.642 1.00 42.21  ? 629  LYS A CA    1 
ATOM   3684 C C     . LYS A 1 629  ? 139.645 140.378 151.827 1.00 43.36  ? 629  LYS A C     1 
ATOM   3685 O O     . LYS A 1 629  ? 138.932 139.375 151.713 1.00 48.76  ? 629  LYS A O     1 
ATOM   3686 C CB    . LYS A 1 629  ? 141.210 141.039 149.978 1.00 44.02  ? 629  LYS A CB    1 
ATOM   3687 C CG    . LYS A 1 629  ? 141.330 139.688 149.300 1.00 51.10  ? 629  LYS A CG    1 
ATOM   3688 C CD    . LYS A 1 629  ? 140.690 139.690 147.925 1.00 54.81  ? 629  LYS A CD    1 
ATOM   3689 C CE    . LYS A 1 629  ? 140.960 138.383 147.199 1.00 60.66  ? 629  LYS A CE    1 
ATOM   3690 N NZ    . LYS A 1 629  ? 140.392 138.380 145.824 1.00 60.33  ? 629  LYS A NZ    1 
ATOM   3691 N N     . PHE A 1 630  ? 140.251 140.692 152.971 1.00 42.10  ? 630  PHE A N     1 
ATOM   3692 C CA    . PHE A 1 630  ? 140.159 139.871 154.179 1.00 40.69  ? 630  PHE A CA    1 
ATOM   3693 C C     . PHE A 1 630  ? 139.694 140.762 155.323 1.00 46.79  ? 630  PHE A C     1 
ATOM   3694 O O     . PHE A 1 630  ? 140.508 141.251 156.118 1.00 50.00  ? 630  PHE A O     1 
ATOM   3695 C CB    . PHE A 1 630  ? 141.498 139.211 154.506 1.00 40.16  ? 630  PHE A CB    1 
ATOM   3696 C CG    . PHE A 1 630  ? 142.212 138.650 153.310 1.00 45.15  ? 630  PHE A CG    1 
ATOM   3697 C CD1   . PHE A 1 630  ? 141.870 137.410 152.797 1.00 45.68  ? 630  PHE A CD1   1 
ATOM   3698 C CD2   . PHE A 1 630  ? 143.236 139.359 152.705 1.00 41.41  ? 630  PHE A CD2   1 
ATOM   3699 C CE1   . PHE A 1 630  ? 142.531 136.895 151.700 1.00 46.17  ? 630  PHE A CE1   1 
ATOM   3700 C CE2   . PHE A 1 630  ? 143.900 138.849 151.609 1.00 42.58  ? 630  PHE A CE2   1 
ATOM   3701 C CZ    . PHE A 1 630  ? 143.548 137.615 151.105 1.00 46.90  ? 630  PHE A CZ    1 
ATOM   3702 N N     . PRO A 1 631  ? 138.384 140.999 155.434 1.00 48.31  ? 631  PRO A N     1 
ATOM   3703 C CA    . PRO A 1 631  ? 137.894 141.943 156.451 1.00 47.82  ? 631  PRO A CA    1 
ATOM   3704 C C     . PRO A 1 631  ? 137.999 141.435 157.879 1.00 53.31  ? 631  PRO A C     1 
ATOM   3705 O O     . PRO A 1 631  ? 137.983 142.254 158.807 1.00 54.79  ? 631  PRO A O     1 
ATOM   3706 C CB    . PRO A 1 631  ? 136.431 142.159 156.046 1.00 48.95  ? 631  PRO A CB    1 
ATOM   3707 C CG    . PRO A 1 631  ? 136.057 140.899 155.343 1.00 50.72  ? 631  PRO A CG    1 
ATOM   3708 C CD    . PRO A 1 631  ? 137.291 140.441 154.620 1.00 46.08  ? 631  PRO A CD    1 
ATOM   3709 N N     . GLN A 1 632  ? 138.105 140.126 158.092 1.00 51.77  ? 632  GLN A N     1 
ATOM   3710 C CA    . GLN A 1 632  ? 138.067 139.555 159.432 1.00 51.90  ? 632  GLN A CA    1 
ATOM   3711 C C     . GLN A 1 632  ? 139.444 139.389 160.059 1.00 49.16  ? 632  GLN A C     1 
ATOM   3712 O O     . GLN A 1 632  ? 139.536 138.924 161.199 1.00 54.63  ? 632  GLN A O     1 
ATOM   3713 C CB    . GLN A 1 632  ? 137.350 138.202 159.401 1.00 54.23  ? 632  GLN A CB    1 
ATOM   3714 C CG    . GLN A 1 632  ? 135.957 138.261 158.802 1.00 54.45  ? 632  GLN A CG    1 
ATOM   3715 C CD    . GLN A 1 632  ? 135.051 139.236 159.528 1.00 59.92  ? 632  GLN A CD    1 
ATOM   3716 O OE1   . GLN A 1 632  ? 135.118 139.375 160.749 1.00 60.92  ? 632  GLN A OE1   1 
ATOM   3717 N NE2   . GLN A 1 632  ? 134.198 139.922 158.776 1.00 57.54  ? 632  GLN A NE2   1 
ATOM   3718 N N     . GLU A 1 633  ? 140.507 139.752 159.354 1.00 45.83  ? 633  GLU A N     1 
ATOM   3719 C CA    . GLU A 1 633  ? 141.855 139.615 159.877 1.00 43.81  ? 633  GLU A CA    1 
ATOM   3720 C C     . GLU A 1 633  ? 142.146 140.692 160.918 1.00 42.87  ? 633  GLU A C     1 
ATOM   3721 O O     . GLU A 1 633  ? 141.438 141.699 160.998 1.00 47.11  ? 633  GLU A O     1 
ATOM   3722 C CB    . GLU A 1 633  ? 142.861 139.691 158.735 1.00 41.62  ? 633  GLU A CB    1 
ATOM   3723 C CG    . GLU A 1 633  ? 142.743 138.562 157.730 1.00 43.08  ? 633  GLU A CG    1 
ATOM   3724 C CD    . GLU A 1 633  ? 143.054 137.204 158.326 1.00 51.99  ? 633  GLU A CD    1 
ATOM   3725 O OE1   . GLU A 1 633  ? 143.834 137.140 159.299 1.00 51.22  ? 633  GLU A OE1   1 
ATOM   3726 O OE2   . GLU A 1 633  ? 142.515 136.197 157.821 1.00 56.19  ? 633  GLU A OE2   1 
ATOM   3727 N N     . PRO A 1 634  ? 143.174 140.495 161.742 1.00 35.50  ? 634  PRO A N     1 
ATOM   3728 C CA    . PRO A 1 634  ? 143.537 141.507 162.741 1.00 36.67  ? 634  PRO A CA    1 
ATOM   3729 C C     . PRO A 1 634  ? 143.878 142.833 162.088 1.00 37.45  ? 634  PRO A C     1 
ATOM   3730 O O     . PRO A 1 634  ? 144.251 142.876 160.906 1.00 37.83  ? 634  PRO A O     1 
ATOM   3731 C CB    . PRO A 1 634  ? 144.764 140.893 163.429 1.00 34.95  ? 634  PRO A CB    1 
ATOM   3732 C CG    . PRO A 1 634  ? 144.573 139.436 163.278 1.00 36.57  ? 634  PRO A CG    1 
ATOM   3733 C CD    . PRO A 1 634  ? 143.929 139.244 161.937 1.00 35.66  ? 634  PRO A CD    1 
ATOM   3734 N N     . PRO A 1 635  ? 143.750 143.938 162.819 1.00 32.31  ? 635  PRO A N     1 
ATOM   3735 C CA    . PRO A 1 635  ? 144.004 145.256 162.228 1.00 28.48  ? 635  PRO A CA    1 
ATOM   3736 C C     . PRO A 1 635  ? 145.461 145.428 161.827 1.00 30.14  ? 635  PRO A C     1 
ATOM   3737 O O     . PRO A 1 635  ? 146.330 144.602 162.109 1.00 33.47  ? 635  PRO A O     1 
ATOM   3738 C CB    . PRO A 1 635  ? 143.621 146.230 163.346 1.00 30.12  ? 635  PRO A CB    1 
ATOM   3739 C CG    . PRO A 1 635  ? 142.728 145.448 164.245 1.00 38.57  ? 635  PRO A CG    1 
ATOM   3740 C CD    . PRO A 1 635  ? 143.239 144.045 164.194 1.00 36.42  ? 635  PRO A CD    1 
ATOM   3741 N N     . ASN A 1 636  ? 145.718 146.546 161.157 1.00 28.95  ? 636  ASN A N     1 
ATOM   3742 C CA    . ASN A 1 636  ? 147.037 146.888 160.654 1.00 24.62  ? 636  ASN A CA    1 
ATOM   3743 C C     . ASN A 1 636  ? 147.618 148.039 161.463 1.00 22.67  ? 636  ASN A C     1 
ATOM   3744 O O     . ASN A 1 636  ? 146.890 148.904 161.956 1.00 27.39  ? 636  ASN A O     1 
ATOM   3745 C CB    . ASN A 1 636  ? 146.975 147.265 159.171 1.00 21.18  ? 636  ASN A CB    1 
ATOM   3746 C CG    . ASN A 1 636  ? 146.228 146.240 158.344 1.00 21.55  ? 636  ASN A CG    1 
ATOM   3747 O OD1   . ASN A 1 636  ? 146.787 145.221 157.946 1.00 24.51  ? 636  ASN A OD1   1 
ATOM   3748 N ND2   . ASN A 1 636  ? 144.955 146.505 158.082 1.00 25.32  ? 636  ASN A ND2   1 
ATOM   3749 N N     . LEU A 1 637  ? 148.940 148.039 161.600 1.00 21.80  ? 637  LEU A N     1 
ATOM   3750 C CA    . LEU A 1 637  ? 149.650 149.016 162.412 1.00 20.45  ? 637  LEU A CA    1 
ATOM   3751 C C     . LEU A 1 637  ? 150.590 149.821 161.528 1.00 23.17  ? 637  LEU A C     1 
ATOM   3752 O O     . LEU A 1 637  ? 151.378 149.248 160.770 1.00 25.80  ? 637  LEU A O     1 
ATOM   3753 C CB    . LEU A 1 637  ? 150.436 148.330 163.533 1.00 23.19  ? 637  LEU A CB    1 
ATOM   3754 C CG    . LEU A 1 637  ? 151.154 149.231 164.539 1.00 22.22  ? 637  LEU A CG    1 
ATOM   3755 C CD1   . LEU A 1 637  ? 150.150 150.064 165.313 1.00 25.92  ? 637  LEU A CD1   1 
ATOM   3756 C CD2   . LEU A 1 637  ? 152.007 148.407 165.484 1.00 23.71  ? 637  LEU A CD2   1 
ATOM   3757 N N     . ILE A 1 638  ? 150.500 151.143 161.620 1.00 22.08  ? 638  ILE A N     1 
ATOM   3758 C CA    . ILE A 1 638  ? 151.411 152.045 160.927 1.00 21.88  ? 638  ILE A CA    1 
ATOM   3759 C C     . ILE A 1 638  ? 152.173 152.826 161.983 1.00 21.98  ? 638  ILE A C     1 
ATOM   3760 O O     . ILE A 1 638  ? 151.565 153.512 162.813 1.00 22.76  ? 638  ILE A O     1 
ATOM   3761 C CB    . ILE A 1 638  ? 150.672 152.991 159.969 1.00 23.63  ? 638  ILE A CB    1 
ATOM   3762 C CG1   . ILE A 1 638  ? 149.922 152.197 158.904 1.00 19.24  ? 638  ILE A CG1   1 
ATOM   3763 C CG2   . ILE A 1 638  ? 151.650 153.946 159.310 1.00 25.93  ? 638  ILE A CG2   1 
ATOM   3764 C CD1   . ILE A 1 638  ? 149.217 153.065 157.900 1.00 21.76  ? 638  ILE A CD1   1 
ATOM   3765 N N     . VAL A 1 639  ? 153.496 152.719 161.955 1.00 26.79  ? 639  VAL A N     1 
ATOM   3766 C CA    . VAL A 1 639  ? 154.368 153.408 162.897 1.00 24.57  ? 639  VAL A CA    1 
ATOM   3767 C C     . VAL A 1 639  ? 155.181 154.426 162.114 1.00 30.37  ? 639  VAL A C     1 
ATOM   3768 O O     . VAL A 1 639  ? 155.899 154.068 161.174 1.00 34.56  ? 639  VAL A O     1 
ATOM   3769 C CB    . VAL A 1 639  ? 155.280 152.428 163.649 1.00 23.20  ? 639  VAL A CB    1 
ATOM   3770 C CG1   . VAL A 1 639  ? 155.930 153.120 164.828 1.00 26.33  ? 639  VAL A CG1   1 
ATOM   3771 C CG2   . VAL A 1 639  ? 154.492 151.215 164.106 1.00 23.59  ? 639  VAL A CG2   1 
ATOM   3772 N N     . ALA A 1 640  ? 155.063 155.693 162.496 1.00 32.53  ? 640  ALA A N     1 
ATOM   3773 C CA    . ALA A 1 640  ? 155.722 156.785 161.797 1.00 34.94  ? 640  ALA A CA    1 
ATOM   3774 C C     . ALA A 1 640  ? 155.771 157.985 162.728 1.00 41.87  ? 640  ALA A C     1 
ATOM   3775 O O     . ALA A 1 640  ? 155.022 158.040 163.709 1.00 45.52  ? 640  ALA A O     1 
ATOM   3776 C CB    . ALA A 1 640  ? 154.982 157.140 160.497 1.00 34.82  ? 640  ALA A CB    1 
ATOM   3777 N N     . PRO A 1 641  ? 156.643 158.955 162.457 1.00 45.20  ? 641  PRO A N     1 
ATOM   3778 C CA    . PRO A 1 641  ? 156.599 160.207 163.218 1.00 43.35  ? 641  PRO A CA    1 
ATOM   3779 C C     . PRO A 1 641  ? 155.265 160.915 163.029 1.00 51.43  ? 641  PRO A C     1 
ATOM   3780 O O     . PRO A 1 641  ? 154.579 160.734 162.021 1.00 55.90  ? 641  PRO A O     1 
ATOM   3781 C CB    . PRO A 1 641  ? 157.756 161.021 162.631 1.00 48.68  ? 641  PRO A CB    1 
ATOM   3782 C CG    . PRO A 1 641  ? 158.698 159.993 162.104 1.00 48.12  ? 641  PRO A CG    1 
ATOM   3783 C CD    . PRO A 1 641  ? 157.832 158.881 161.589 1.00 44.38  ? 641  PRO A CD    1 
ATOM   3784 N N     . VAL A 1 642  ? 154.893 161.714 164.033 1.00 54.42  ? 642  VAL A N     1 
ATOM   3785 C CA    . VAL A 1 642  ? 153.594 162.385 164.024 1.00 57.10  ? 642  VAL A CA    1 
ATOM   3786 C C     . VAL A 1 642  ? 153.445 163.257 162.785 1.00 61.05  ? 642  VAL A C     1 
ATOM   3787 O O     . VAL A 1 642  ? 152.374 163.307 162.163 1.00 60.37  ? 642  VAL A O     1 
ATOM   3788 C CB    . VAL A 1 642  ? 153.412 163.207 165.312 1.00 60.80  ? 642  VAL A CB    1 
ATOM   3789 C CG1   . VAL A 1 642  ? 152.061 163.898 165.310 1.00 59.64  ? 642  VAL A CG1   1 
ATOM   3790 C CG2   . VAL A 1 642  ? 153.570 162.315 166.528 1.00 58.43  ? 642  VAL A CG2   1 
ATOM   3791 N N     . SER A 1 643  ? 154.514 163.967 162.416 1.00 60.68  ? 643  SER A N     1 
ATOM   3792 C CA    . SER A 1 643  ? 154.497 164.760 161.193 1.00 60.99  ? 643  SER A CA    1 
ATOM   3793 C C     . SER A 1 643  ? 154.151 163.908 159.981 1.00 64.28  ? 643  SER A C     1 
ATOM   3794 O O     . SER A 1 643  ? 153.545 164.405 159.025 1.00 69.33  ? 643  SER A O     1 
ATOM   3795 C CB    . SER A 1 643  ? 155.852 165.437 160.997 1.00 68.50  ? 643  SER A CB    1 
ATOM   3796 O OG    . SER A 1 643  ? 156.900 164.484 160.980 1.00 63.63  ? 643  SER A OG    1 
ATOM   3797 N N     . LEU A 1 644  ? 154.520 162.629 160.003 1.00 54.74  ? 644  LEU A N     1 
ATOM   3798 C CA    . LEU A 1 644  ? 154.158 161.714 158.932 1.00 47.96  ? 644  LEU A CA    1 
ATOM   3799 C C     . LEU A 1 644  ? 152.847 160.988 159.195 1.00 49.41  ? 644  LEU A C     1 
ATOM   3800 O O     . LEU A 1 644  ? 152.189 160.565 158.242 1.00 56.91  ? 644  LEU A O     1 
ATOM   3801 C CB    . LEU A 1 644  ? 155.273 160.692 158.711 1.00 49.23  ? 644  LEU A CB    1 
ATOM   3802 C CG    . LEU A 1 644  ? 156.618 161.283 158.293 1.00 52.97  ? 644  LEU A CG    1 
ATOM   3803 C CD1   . LEU A 1 644  ? 157.552 160.178 157.857 1.00 54.88  ? 644  LEU A CD1   1 
ATOM   3804 C CD2   . LEU A 1 644  ? 156.439 162.304 157.183 1.00 58.05  ? 644  LEU A CD2   1 
ATOM   3805 N N     . LEU A 1 645  ? 152.450 160.828 160.459 1.00 48.95  ? 645  LEU A N     1 
ATOM   3806 C CA    . LEU A 1 645  ? 151.143 160.243 160.750 1.00 50.40  ? 645  LEU A CA    1 
ATOM   3807 C C     . LEU A 1 645  ? 150.020 161.134 160.238 1.00 51.46  ? 645  LEU A C     1 
ATOM   3808 O O     . LEU A 1 645  ? 149.018 160.643 159.696 1.00 50.26  ? 645  LEU A O     1 
ATOM   3809 C CB    . LEU A 1 645  ? 150.995 160.009 162.252 1.00 50.44  ? 645  LEU A CB    1 
ATOM   3810 C CG    . LEU A 1 645  ? 151.867 158.917 162.859 1.00 43.18  ? 645  LEU A CG    1 
ATOM   3811 C CD1   . LEU A 1 645  ? 151.735 158.932 164.369 1.00 49.94  ? 645  LEU A CD1   1 
ATOM   3812 C CD2   . LEU A 1 645  ? 151.476 157.564 162.293 1.00 35.53  ? 645  LEU A CD2   1 
ATOM   3813 N N     . ASP A 1 646  ? 150.168 162.449 160.412 1.00 57.38  ? 646  ASP A N     1 
ATOM   3814 C CA    . ASP A 1 646  ? 149.194 163.379 159.853 1.00 59.14  ? 646  ASP A CA    1 
ATOM   3815 C C     . ASP A 1 646  ? 149.113 163.236 158.341 1.00 58.59  ? 646  ASP A C     1 
ATOM   3816 O O     . ASP A 1 646  ? 148.018 163.227 157.769 1.00 59.41  ? 646  ASP A O     1 
ATOM   3817 C CB    . ASP A 1 646  ? 149.553 164.814 160.237 1.00 64.90  ? 646  ASP A CB    1 
ATOM   3818 C CG    . ASP A 1 646  ? 149.276 165.115 161.694 1.00 74.71  ? 646  ASP A CG    1 
ATOM   3819 O OD1   . ASP A 1 646  ? 148.702 164.248 162.384 1.00 72.14  ? 646  ASP A OD1   1 
ATOM   3820 O OD2   . ASP A 1 646  ? 149.631 166.222 162.151 1.00 79.68  ? 646  ASP A OD2   1 
ATOM   3821 N N     . ASN A 1 647  ? 150.266 163.110 157.679 1.00 56.95  ? 647  ASN A N     1 
ATOM   3822 C CA    . ASN A 1 647  ? 150.281 162.936 156.230 1.00 52.42  ? 647  ASN A CA    1 
ATOM   3823 C C     . ASN A 1 647  ? 149.627 161.622 155.822 1.00 51.07  ? 647  ASN A C     1 
ATOM   3824 O O     . ASN A 1 647  ? 148.930 161.559 154.806 1.00 58.35  ? 647  ASN A O     1 
ATOM   3825 C CB    . ASN A 1 647  ? 151.718 163.005 155.713 1.00 54.72  ? 647  ASN A CB    1 
ATOM   3826 C CG    . ASN A 1 647  ? 151.800 162.890 154.206 1.00 66.37  ? 647  ASN A CG    1 
ATOM   3827 O OD1   . ASN A 1 647  ? 151.688 163.885 153.490 1.00 68.26  ? 647  ASN A OD1   1 
ATOM   3828 N ND2   . ASN A 1 647  ? 151.999 161.673 153.714 1.00 64.64  ? 647  ASN A ND2   1 
ATOM   3829 N N     . TRP A 1 648  ? 149.854 160.560 156.596 1.00 49.43  ? 648  TRP A N     1 
ATOM   3830 C CA    . TRP A 1 648  ? 149.241 159.270 156.294 1.00 46.20  ? 648  TRP A CA    1 
ATOM   3831 C C     . TRP A 1 648  ? 147.724 159.355 156.364 1.00 49.01  ? 648  TRP A C     1 
ATOM   3832 O O     . TRP A 1 648  ? 147.021 158.907 155.449 1.00 49.34  ? 648  TRP A O     1 
ATOM   3833 C CB    . TRP A 1 648  ? 149.764 158.203 157.256 1.00 40.48  ? 648  TRP A CB    1 
ATOM   3834 C CG    . TRP A 1 648  ? 150.988 157.515 156.762 1.00 36.91  ? 648  TRP A CG    1 
ATOM   3835 C CD1   . TRP A 1 648  ? 152.282 157.870 156.997 1.00 38.68  ? 648  TRP A CD1   1 
ATOM   3836 C CD2   . TRP A 1 648  ? 151.035 156.351 155.934 1.00 35.63  ? 648  TRP A CD2   1 
ATOM   3837 N NE1   . TRP A 1 648  ? 153.133 156.998 156.368 1.00 38.45  ? 648  TRP A NE1   1 
ATOM   3838 C CE2   . TRP A 1 648  ? 152.391 156.055 155.706 1.00 34.70  ? 648  TRP A CE2   1 
ATOM   3839 C CE3   . TRP A 1 648  ? 150.061 155.529 155.362 1.00 33.61  ? 648  TRP A CE3   1 
ATOM   3840 C CZ2   . TRP A 1 648  ? 152.797 154.974 154.935 1.00 33.14  ? 648  TRP A CZ2   1 
ATOM   3841 C CZ3   . TRP A 1 648  ? 150.467 154.458 154.598 1.00 33.84  ? 648  TRP A CZ3   1 
ATOM   3842 C CH2   . TRP A 1 648  ? 151.822 154.189 154.391 1.00 34.16  ? 648  TRP A CH2   1 
ATOM   3843 N N     . GLU A 1 649  ? 147.200 159.939 157.444 1.00 54.50  ? 649  GLU A N     1 
ATOM   3844 C CA    . GLU A 1 649  ? 145.753 160.102 157.558 1.00 52.08  ? 649  GLU A CA    1 
ATOM   3845 C C     . GLU A 1 649  ? 145.212 161.006 156.455 1.00 55.59  ? 649  GLU A C     1 
ATOM   3846 O O     . GLU A 1 649  ? 144.160 160.725 155.864 1.00 56.43  ? 649  GLU A O     1 
ATOM   3847 C CB    . GLU A 1 649  ? 145.397 160.656 158.937 1.00 56.57  ? 649  GLU A CB    1 
ATOM   3848 C CG    . GLU A 1 649  ? 143.924 160.981 159.125 1.00 61.20  ? 649  GLU A CG    1 
ATOM   3849 C CD    . GLU A 1 649  ? 143.039 159.751 159.091 1.00 65.47  ? 649  GLU A CD    1 
ATOM   3850 O OE1   . GLU A 1 649  ? 143.551 158.640 159.337 1.00 67.84  ? 649  GLU A OE1   1 
ATOM   3851 O OE2   . GLU A 1 649  ? 141.829 159.896 158.817 1.00 66.75  ? 649  GLU A OE2   1 
ATOM   3852 N N     . ARG A 1 650  ? 145.934 162.088 156.152 1.00 55.54  ? 650  ARG A N     1 
ATOM   3853 C CA    . ARG A 1 650  ? 145.505 163.024 155.121 1.00 54.11  ? 650  ARG A CA    1 
ATOM   3854 C C     . ARG A 1 650  ? 145.409 162.344 153.763 1.00 54.26  ? 650  ARG A C     1 
ATOM   3855 O O     . ARG A 1 650  ? 144.417 162.502 153.047 1.00 58.06  ? 650  ARG A O     1 
ATOM   3856 C CB    . ARG A 1 650  ? 146.483 164.196 155.067 1.00 57.71  ? 650  ARG A CB    1 
ATOM   3857 C CG    . ARG A 1 650  ? 146.073 165.338 154.163 1.00 63.35  ? 650  ARG A CG    1 
ATOM   3858 C CD    . ARG A 1 650  ? 147.232 166.303 153.954 1.00 68.49  ? 650  ARG A CD    1 
ATOM   3859 N NE    . ARG A 1 650  ? 148.281 166.138 154.955 1.00 65.91  ? 650  ARG A NE    1 
ATOM   3860 C CZ    . ARG A 1 650  ? 148.322 166.777 156.116 1.00 67.76  ? 650  ARG A CZ    1 
ATOM   3861 N NH1   . ARG A 1 650  ? 147.375 167.630 156.469 1.00 64.89  ? 650  ARG A NH1   1 
ATOM   3862 N NH2   . ARG A 1 650  ? 149.337 166.550 156.946 1.00 66.52  ? 650  ARG A NH2   1 
ATOM   3863 N N     . GLU A 1 651  ? 146.430 161.571 153.395 1.00 51.69  ? 651  GLU A N     1 
ATOM   3864 C CA    . GLU A 1 651  ? 146.423 160.911 152.096 1.00 48.52  ? 651  GLU A CA    1 
ATOM   3865 C C     . GLU A 1 651  ? 145.431 159.757 152.047 1.00 44.07  ? 651  GLU A C     1 
ATOM   3866 O O     . GLU A 1 651  ? 144.859 159.488 150.986 1.00 51.00  ? 651  GLU A O     1 
ATOM   3867 C CB    . GLU A 1 651  ? 147.829 160.427 151.740 1.00 49.49  ? 651  GLU A CB    1 
ATOM   3868 C CG    . GLU A 1 651  ? 148.835 161.558 151.578 1.00 56.49  ? 651  GLU A CG    1 
ATOM   3869 C CD    . GLU A 1 651  ? 150.037 161.162 150.744 1.00 71.08  ? 651  GLU A CD    1 
ATOM   3870 O OE1   . GLU A 1 651  ? 149.914 160.219 149.935 1.00 72.38  ? 651  GLU A OE1   1 
ATOM   3871 O OE2   . GLU A 1 651  ? 151.103 161.795 150.896 1.00 69.19  ? 651  GLU A OE2   1 
ATOM   3872 N N     . LEU A 1 652  ? 145.202 159.074 153.171 1.00 41.92  ? 652  LEU A N     1 
ATOM   3873 C CA    . LEU A 1 652  ? 144.155 158.059 153.200 1.00 43.33  ? 652  LEU A CA    1 
ATOM   3874 C C     . LEU A 1 652  ? 142.786 158.683 152.970 1.00 46.88  ? 652  LEU A C     1 
ATOM   3875 O O     . LEU A 1 652  ? 141.937 158.100 152.286 1.00 49.06  ? 652  LEU A O     1 
ATOM   3876 C CB    . LEU A 1 652  ? 144.190 157.301 154.526 1.00 50.45  ? 652  LEU A CB    1 
ATOM   3877 C CG    . LEU A 1 652  ? 143.135 156.209 154.711 1.00 44.63  ? 652  LEU A CG    1 
ATOM   3878 C CD1   . LEU A 1 652  ? 143.169 155.217 153.562 1.00 37.81  ? 652  LEU A CD1   1 
ATOM   3879 C CD2   . LEU A 1 652  ? 143.349 155.497 156.028 1.00 44.25  ? 652  LEU A CD2   1 
ATOM   3880 N N     . ASN A 1 653  ? 142.550 159.867 153.538 1.00 52.60  ? 653  ASN A N     1 
ATOM   3881 C CA    . ASN A 1 653  ? 141.290 160.559 153.281 1.00 52.23  ? 653  ASN A CA    1 
ATOM   3882 C C     . ASN A 1 653  ? 141.226 161.090 151.851 1.00 49.98  ? 653  ASN A C     1 
ATOM   3883 O O     . ASN A 1 653  ? 140.152 161.114 151.240 1.00 49.67  ? 653  ASN A O     1 
ATOM   3884 C CB    . ASN A 1 653  ? 141.100 161.695 154.284 1.00 48.72  ? 653  ASN A CB    1 
ATOM   3885 C CG    . ASN A 1 653  ? 140.973 161.198 155.710 1.00 56.05  ? 653  ASN A CG    1 
ATOM   3886 O OD1   . ASN A 1 653  ? 140.523 160.078 155.953 1.00 54.58  ? 653  ASN A OD1   1 
ATOM   3887 N ND2   . ASN A 1 653  ? 141.367 162.033 156.664 1.00 62.62  ? 653  ASN A ND2   1 
ATOM   3888 N N     . ASN A 1 654  ? 142.365 161.519 151.304 1.00 49.08  ? 654  ASN A N     1 
ATOM   3889 C CA    . ASN A 1 654  ? 142.370 162.147 149.986 1.00 47.76  ? 654  ASN A CA    1 
ATOM   3890 C C     . ASN A 1 654  ? 142.182 161.129 148.868 1.00 49.23  ? 654  ASN A C     1 
ATOM   3891 O O     . ASN A 1 654  ? 141.491 161.408 147.882 1.00 51.84  ? 654  ASN A O     1 
ATOM   3892 C CB    . ASN A 1 654  ? 143.672 162.923 149.779 1.00 49.06  ? 654  ASN A CB    1 
ATOM   3893 C CG    . ASN A 1 654  ? 143.749 164.172 150.631 1.00 59.60  ? 654  ASN A CG    1 
ATOM   3894 O OD1   . ASN A 1 654  ? 142.934 164.377 151.530 1.00 55.35  ? 654  ASN A OD1   1 
ATOM   3895 N ND2   . ASN A 1 654  ? 144.738 165.015 150.356 1.00 63.44  ? 654  ASN A ND2   1 
ATOM   3896 N N     . PHE A 1 655  ? 142.794 159.950 148.991 1.00 44.86  ? 655  PHE A N     1 
ATOM   3897 C CA    . PHE A 1 655  ? 142.810 158.994 147.891 1.00 37.35  ? 655  PHE A CA    1 
ATOM   3898 C C     . PHE A 1 655  ? 141.721 157.933 147.973 1.00 37.54  ? 655  PHE A C     1 
ATOM   3899 O O     . PHE A 1 655  ? 141.379 157.348 146.941 1.00 38.89  ? 655  PHE A O     1 
ATOM   3900 C CB    . PHE A 1 655  ? 144.172 158.292 147.813 1.00 37.89  ? 655  PHE A CB    1 
ATOM   3901 C CG    . PHE A 1 655  ? 145.303 159.196 147.409 1.00 43.02  ? 655  PHE A CG    1 
ATOM   3902 C CD1   . PHE A 1 655  ? 145.368 159.719 146.131 1.00 52.34  ? 655  PHE A CD1   1 
ATOM   3903 C CD2   . PHE A 1 655  ? 146.314 159.505 148.300 1.00 46.36  ? 655  PHE A CD2   1 
ATOM   3904 C CE1   . PHE A 1 655  ? 146.409 160.545 145.755 1.00 47.50  ? 655  PHE A CE1   1 
ATOM   3905 C CE2   . PHE A 1 655  ? 147.357 160.330 147.928 1.00 52.52  ? 655  PHE A CE2   1 
ATOM   3906 C CZ    . PHE A 1 655  ? 147.403 160.850 146.655 1.00 47.19  ? 655  PHE A CZ    1 
ATOM   3907 N N     . PHE A 1 656  ? 141.164 157.670 149.153 1.00 38.39  ? 656  PHE A N     1 
ATOM   3908 C CA    . PHE A 1 656  ? 140.235 156.565 149.334 1.00 38.28  ? 656  PHE A CA    1 
ATOM   3909 C C     . PHE A 1 656  ? 138.938 157.052 149.961 1.00 42.44  ? 656  PHE A C     1 
ATOM   3910 O O     . PHE A 1 656  ? 138.916 158.040 150.699 1.00 48.00  ? 656  PHE A O     1 
ATOM   3911 C CB    . PHE A 1 656  ? 140.836 155.459 150.216 1.00 36.90  ? 656  PHE A CB    1 
ATOM   3912 C CG    . PHE A 1 656  ? 142.087 154.849 149.657 1.00 34.04  ? 656  PHE A CG    1 
ATOM   3913 C CD1   . PHE A 1 656  ? 143.325 155.407 149.922 1.00 28.48  ? 656  PHE A CD1   1 
ATOM   3914 C CD2   . PHE A 1 656  ? 142.027 153.714 148.870 1.00 34.45  ? 656  PHE A CD2   1 
ATOM   3915 C CE1   . PHE A 1 656  ? 144.474 154.849 149.410 1.00 26.49  ? 656  PHE A CE1   1 
ATOM   3916 C CE2   . PHE A 1 656  ? 143.175 153.150 148.355 1.00 27.62  ? 656  PHE A CE2   1 
ATOM   3917 C CZ    . PHE A 1 656  ? 144.399 153.719 148.626 1.00 26.47  ? 656  PHE A CZ    1 
ATOM   3918 N N     . TYR A 1 657  ? 137.853 156.341 149.656 1.00 42.08  ? 657  TYR A N     1 
ATOM   3919 C CA    . TYR A 1 657  ? 136.568 156.549 150.321 1.00 49.26  ? 657  TYR A CA    1 
ATOM   3920 C C     . TYR A 1 657  ? 136.664 155.912 151.700 1.00 57.30  ? 657  TYR A C     1 
ATOM   3921 O O     . TYR A 1 657  ? 136.428 154.717 151.879 1.00 53.96  ? 657  TYR A O     1 
ATOM   3922 C CB    . TYR A 1 657  ? 135.425 155.953 149.507 1.00 49.93  ? 657  TYR A CB    1 
ATOM   3923 C CG    . TYR A 1 657  ? 135.206 156.613 148.165 1.00 57.67  ? 657  TYR A CG    1 
ATOM   3924 C CD1   . TYR A 1 657  ? 134.574 157.845 148.071 1.00 57.47  ? 657  TYR A CD1   1 
ATOM   3925 C CD2   . TYR A 1 657  ? 135.620 155.999 146.991 1.00 55.78  ? 657  TYR A CD2   1 
ATOM   3926 C CE1   . TYR A 1 657  ? 134.369 158.451 146.847 1.00 57.40  ? 657  TYR A CE1   1 
ATOM   3927 C CE2   . TYR A 1 657  ? 135.420 156.597 145.763 1.00 59.35  ? 657  TYR A CE2   1 
ATOM   3928 C CZ    . TYR A 1 657  ? 134.794 157.823 145.697 1.00 63.31  ? 657  TYR A CZ    1 
ATOM   3929 O OH    . TYR A 1 657  ? 134.592 158.424 144.476 1.00 61.20  ? 657  TYR A OH    1 
ATOM   3930 N N     . THR A 1 658  ? 137.019 156.727 152.695 1.00 55.68  ? 658  THR A N     1 
ATOM   3931 C CA    . THR A 1 658  ? 137.293 156.237 154.045 1.00 49.33  ? 658  THR A CA    1 
ATOM   3932 C C     . THR A 1 658  ? 135.974 156.007 154.786 1.00 53.60  ? 658  THR A C     1 
ATOM   3933 O O     . THR A 1 658  ? 135.656 156.643 155.793 1.00 58.99  ? 658  THR A O     1 
ATOM   3934 C CB    . THR A 1 658  ? 138.196 157.210 154.791 1.00 48.72  ? 658  THR A CB    1 
ATOM   3935 O OG1   . THR A 1 658  ? 139.243 157.651 153.920 1.00 48.73  ? 658  THR A OG1   1 
ATOM   3936 C CG2   . THR A 1 658  ? 138.820 156.534 156.001 1.00 50.87  ? 658  THR A CG2   1 
ATOM   3937 N N     . ALA A 1 659  ? 135.193 155.071 154.255 1.00 54.56  ? 659  ALA A N     1 
ATOM   3938 C CA    . ALA A 1 659  ? 133.954 154.624 154.878 1.00 55.50  ? 659  ALA A CA    1 
ATOM   3939 C C     . ALA A 1 659  ? 134.048 153.214 155.433 1.00 56.73  ? 659  ALA A C     1 
ATOM   3940 O O     . ALA A 1 659  ? 133.563 152.956 156.537 1.00 55.56  ? 659  ALA A O     1 
ATOM   3941 C CB    . ALA A 1 659  ? 132.799 154.698 153.875 1.00 51.92  ? 659  ALA A CB    1 
ATOM   3942 N N     . GLY A 1 660  ? 134.660 152.298 154.693 1.00 54.03  ? 660  GLY A N     1 
ATOM   3943 C CA    . GLY A 1 660  ? 134.944 150.959 155.156 1.00 49.42  ? 660  GLY A CA    1 
ATOM   3944 C C     . GLY A 1 660  ? 136.320 150.777 155.754 1.00 46.98  ? 660  GLY A C     1 
ATOM   3945 O O     . GLY A 1 660  ? 136.729 149.637 155.997 1.00 48.53  ? 660  GLY A O     1 
ATOM   3946 N N     . ILE A 1 661  ? 137.049 151.862 155.999 1.00 41.64  ? 661  ILE A N     1 
ATOM   3947 C CA    . ILE A 1 661  ? 138.395 151.787 156.561 1.00 43.51  ? 661  ILE A CA    1 
ATOM   3948 C C     . ILE A 1 661  ? 138.452 152.659 157.809 1.00 45.46  ? 661  ILE A C     1 
ATOM   3949 O O     . ILE A 1 661  ? 138.964 153.786 157.752 1.00 46.34  ? 661  ILE A O     1 
ATOM   3950 C CB    . ILE A 1 661  ? 139.462 152.219 155.540 1.00 40.45  ? 661  ILE A CB    1 
ATOM   3951 C CG1   . ILE A 1 661  ? 139.260 151.510 154.199 1.00 44.16  ? 661  ILE A CG1   1 
ATOM   3952 C CG2   . ILE A 1 661  ? 140.858 151.928 156.070 1.00 38.63  ? 661  ILE A CG2   1 
ATOM   3953 C CD1   . ILE A 1 661  ? 138.552 152.351 153.155 1.00 50.51  ? 661  ILE A CD1   1 
ATOM   3954 N N     . PRO A 1 662  ? 137.925 152.202 158.943 1.00 44.78  ? 662  PRO A N     1 
ATOM   3955 C CA    . PRO A 1 662  ? 138.060 152.980 160.177 1.00 36.45  ? 662  PRO A CA    1 
ATOM   3956 C C     . PRO A 1 662  ? 139.516 153.088 160.595 1.00 36.51  ? 662  PRO A C     1 
ATOM   3957 O O     . PRO A 1 662  ? 140.314 152.169 160.399 1.00 39.68  ? 662  PRO A O     1 
ATOM   3958 C CB    . PRO A 1 662  ? 137.244 152.178 161.198 1.00 37.64  ? 662  PRO A CB    1 
ATOM   3959 C CG    . PRO A 1 662  ? 136.362 151.287 160.381 1.00 40.53  ? 662  PRO A CG    1 
ATOM   3960 C CD    . PRO A 1 662  ? 137.145 150.972 159.151 1.00 42.21  ? 662  PRO A CD    1 
ATOM   3961 N N     . VAL A 1 663  ? 139.859 154.232 161.181 1.00 30.92  ? 663  VAL A N     1 
ATOM   3962 C CA    . VAL A 1 663  ? 141.232 154.539 161.558 1.00 32.39  ? 663  VAL A CA    1 
ATOM   3963 C C     . VAL A 1 663  ? 141.262 154.978 163.014 1.00 37.55  ? 663  VAL A C     1 
ATOM   3964 O O     . VAL A 1 663  ? 140.396 155.737 163.463 1.00 41.77  ? 663  VAL A O     1 
ATOM   3965 C CB    . VAL A 1 663  ? 141.843 155.629 160.652 1.00 31.22  ? 663  VAL A CB    1 
ATOM   3966 C CG1   . VAL A 1 663  ? 143.293 155.886 161.027 1.00 27.52  ? 663  VAL A CG1   1 
ATOM   3967 C CG2   . VAL A 1 663  ? 141.734 155.228 159.197 1.00 38.55  ? 663  VAL A CG2   1 
ATOM   3968 N N     . LEU A 1 664  ? 142.253 154.488 163.752 1.00 32.21  ? 664  LEU A N     1 
ATOM   3969 C CA    . LEU A 1 664  ? 142.544 154.943 165.103 1.00 32.91  ? 664  LEU A CA    1 
ATOM   3970 C C     . LEU A 1 664  ? 143.961 155.494 165.134 1.00 30.44  ? 664  LEU A C     1 
ATOM   3971 O O     . LEU A 1 664  ? 144.903 154.810 164.726 1.00 31.91  ? 664  LEU A O     1 
ATOM   3972 C CB    . LEU A 1 664  ? 142.395 153.806 166.116 1.00 35.89  ? 664  LEU A CB    1 
ATOM   3973 C CG    . LEU A 1 664  ? 142.917 154.072 167.528 1.00 36.07  ? 664  LEU A CG    1 
ATOM   3974 C CD1   . LEU A 1 664  ? 142.061 155.106 168.230 1.00 37.63  ? 664  LEU A CD1   1 
ATOM   3975 C CD2   . LEU A 1 664  ? 142.976 152.786 168.331 1.00 40.61  ? 664  LEU A CD2   1 
ATOM   3976 N N     . LYS A 1 665  ? 144.112 156.726 165.608 1.00 31.49  ? 665  LYS A N     1 
ATOM   3977 C CA    . LYS A 1 665  ? 145.424 157.343 165.762 1.00 39.69  ? 665  LYS A CA    1 
ATOM   3978 C C     . LYS A 1 665  ? 145.759 157.386 167.247 1.00 51.16  ? 665  LYS A C     1 
ATOM   3979 O O     . LYS A 1 665  ? 145.172 158.169 167.999 1.00 55.44  ? 665  LYS A O     1 
ATOM   3980 C CB    . LYS A 1 665  ? 145.453 158.740 165.149 1.00 40.47  ? 665  LYS A CB    1 
ATOM   3981 C CG    . LYS A 1 665  ? 146.829 159.379 165.180 1.00 47.70  ? 665  LYS A CG    1 
ATOM   3982 C CD    . LYS A 1 665  ? 146.823 160.755 164.549 1.00 56.85  ? 665  LYS A CD    1 
ATOM   3983 C CE    . LYS A 1 665  ? 148.203 161.384 164.613 1.00 63.84  ? 665  LYS A CE    1 
ATOM   3984 N NZ    . LYS A 1 665  ? 148.213 162.755 164.040 1.00 58.63  ? 665  LYS A NZ    1 
ATOM   3985 N N     . LEU A 1 666  ? 146.708 156.547 167.667 1.00 43.67  ? 666  LEU A N     1 
ATOM   3986 C CA    . LEU A 1 666  ? 147.021 156.440 169.088 1.00 42.06  ? 666  LEU A CA    1 
ATOM   3987 C C     . LEU A 1 666  ? 147.652 157.718 169.626 1.00 53.67  ? 666  LEU A C     1 
ATOM   3988 O O     . LEU A 1 666  ? 147.426 158.082 170.784 1.00 67.04  ? 666  LEU A O     1 
ATOM   3989 C CB    . LEU A 1 666  ? 147.936 155.243 169.339 1.00 42.10  ? 666  LEU A CB    1 
ATOM   3990 C CG    . LEU A 1 666  ? 147.250 153.877 169.373 1.00 46.85  ? 666  LEU A CG    1 
ATOM   3991 C CD1   . LEU A 1 666  ? 148.244 152.784 169.726 1.00 43.55  ? 666  LEU A CD1   1 
ATOM   3992 C CD2   . LEU A 1 666  ? 146.090 153.885 170.356 1.00 43.65  ? 666  LEU A CD2   1 
ATOM   3993 N N     . TYR A 1 667  ? 148.442 158.411 168.810 1.00 53.20  ? 667  TYR A N     1 
ATOM   3994 C CA    . TYR A 1 667  ? 149.117 159.611 169.284 1.00 60.02  ? 667  TYR A CA    1 
ATOM   3995 C C     . TYR A 1 667  ? 148.110 160.689 169.671 1.00 62.74  ? 667  TYR A C     1 
ATOM   3996 O O     . TYR A 1 667  ? 147.040 160.819 169.070 1.00 60.59  ? 667  TYR A O     1 
ATOM   3997 C CB    . TYR A 1 667  ? 150.070 160.152 168.218 1.00 59.30  ? 667  TYR A CB    1 
ATOM   3998 C CG    . TYR A 1 667  ? 150.756 161.435 168.630 1.00 66.42  ? 667  TYR A CG    1 
ATOM   3999 C CD1   . TYR A 1 667  ? 150.289 162.668 168.194 1.00 66.13  ? 667  TYR A CD1   1 
ATOM   4000 C CD2   . TYR A 1 667  ? 151.859 161.413 169.472 1.00 67.08  ? 667  TYR A CD2   1 
ATOM   4001 C CE1   . TYR A 1 667  ? 150.909 163.842 168.577 1.00 70.35  ? 667  TYR A CE1   1 
ATOM   4002 C CE2   . TYR A 1 667  ? 152.486 162.582 169.859 1.00 71.46  ? 667  TYR A CE2   1 
ATOM   4003 C CZ    . TYR A 1 667  ? 152.008 163.793 169.407 1.00 76.03  ? 667  TYR A CZ    1 
ATOM   4004 O OH    . TYR A 1 667  ? 152.630 164.958 169.791 1.00 77.44  ? 667  TYR A OH    1 
ATOM   4005 N N     . GLY A 1 668  ? 148.465 161.463 170.694 1.00 64.87  ? 668  GLY A N     1 
ATOM   4006 C CA    . GLY A 1 668  ? 147.645 162.571 171.141 1.00 68.31  ? 668  GLY A CA    1 
ATOM   4007 C C     . GLY A 1 668  ? 146.803 162.241 172.355 1.00 70.75  ? 668  GLY A C     1 
ATOM   4008 O O     . GLY A 1 668  ? 147.199 161.422 173.188 1.00 70.31  ? 668  GLY A O     1 
ATOM   4009 N N     . GLU A 1 669  ? 145.637 162.877 172.469 1.00 71.75  ? 669  GLU A N     1 
ATOM   4010 C CA    . GLU A 1 669  ? 144.712 162.575 173.552 1.00 72.71  ? 669  GLU A CA    1 
ATOM   4011 C C     . GLU A 1 669  ? 143.939 161.286 173.319 1.00 70.14  ? 669  GLU A C     1 
ATOM   4012 O O     . GLU A 1 669  ? 143.260 160.812 174.238 1.00 73.12  ? 669  GLU A O     1 
ATOM   4013 C CB    . GLU A 1 669  ? 143.736 163.737 173.749 1.00 80.55  ? 669  GLU A CB    1 
ATOM   4014 C CG    . GLU A 1 669  ? 144.397 165.031 174.193 1.00 81.38  ? 669  GLU A CG    1 
ATOM   4015 C CD    . GLU A 1 669  ? 144.999 164.932 175.581 1.00 85.14  ? 669  GLU A CD    1 
ATOM   4016 O OE1   . GLU A 1 669  ? 144.512 164.110 176.386 1.00 82.75  ? 669  GLU A OE1   1 
ATOM   4017 O OE2   . GLU A 1 669  ? 145.961 165.675 175.868 1.00 85.30  ? 669  GLU A OE2   1 
ATOM   4018 N N     . THR A 1 670  ? 144.020 160.712 172.118 1.00 65.40  ? 670  THR A N     1 
ATOM   4019 C CA    . THR A 1 670  ? 143.357 159.439 171.869 1.00 66.80  ? 670  THR A CA    1 
ATOM   4020 C C     . THR A 1 670  ? 144.014 158.308 172.647 1.00 63.75  ? 670  THR A C     1 
ATOM   4021 O O     . THR A 1 670  ? 143.360 157.303 172.946 1.00 63.38  ? 670  THR A O     1 
ATOM   4022 C CB    . THR A 1 670  ? 143.357 159.128 170.375 1.00 65.46  ? 670  THR A CB    1 
ATOM   4023 O OG1   . THR A 1 670  ? 143.255 160.348 169.632 1.00 60.62  ? 670  THR A OG1   1 
ATOM   4024 C CG2   . THR A 1 670  ? 142.178 158.241 170.024 1.00 66.50  ? 670  THR A CG2   1 
ATOM   4025 N N     . ILE A 1 671  ? 145.301 158.445 172.979 1.00 62.66  ? 671  ILE A N     1 
ATOM   4026 C CA    . ILE A 1 671  ? 145.932 157.468 173.857 1.00 62.43  ? 671  ILE A CA    1 
ATOM   4027 C C     . ILE A 1 671  ? 145.328 157.552 175.253 1.00 63.58  ? 671  ILE A C     1 
ATOM   4028 O O     . ILE A 1 671  ? 145.175 156.532 175.932 1.00 63.08  ? 671  ILE A O     1 
ATOM   4029 C CB    . ILE A 1 671  ? 147.466 157.650 173.870 1.00 57.29  ? 671  ILE A CB    1 
ATOM   4030 C CG1   . ILE A 1 671  ? 148.160 156.349 174.271 1.00 54.36  ? 671  ILE A CG1   1 
ATOM   4031 C CG2   . ILE A 1 671  ? 147.898 158.774 174.800 1.00 70.21  ? 671  ILE A CG2   1 
ATOM   4032 C CD1   . ILE A 1 671  ? 148.013 155.247 173.253 1.00 58.38  ? 671  ILE A CD1   1 
ATOM   4033 N N     . LYS A 1 672  ? 144.958 158.758 175.698 1.00 63.37  ? 672  LYS A N     1 
ATOM   4034 C CA    . LYS A 1 672  ? 144.299 158.906 176.990 1.00 61.70  ? 672  LYS A CA    1 
ATOM   4035 C C     . LYS A 1 672  ? 142.863 158.409 176.940 1.00 61.69  ? 672  LYS A C     1 
ATOM   4036 O O     . LYS A 1 672  ? 142.359 157.872 177.932 1.00 64.51  ? 672  LYS A O     1 
ATOM   4037 C CB    . LYS A 1 672  ? 144.332 160.368 177.433 1.00 67.91  ? 672  LYS A CB    1 
ATOM   4038 C CG    . LYS A 1 672  ? 145.725 160.957 177.555 1.00 72.99  ? 672  LYS A CG    1 
ATOM   4039 C CD    . LYS A 1 672  ? 146.512 160.287 178.667 1.00 80.46  ? 672  LYS A CD    1 
ATOM   4040 C CE    . LYS A 1 672  ? 147.832 160.999 178.912 1.00 80.89  ? 672  LYS A CE    1 
ATOM   4041 N NZ    . LYS A 1 672  ? 147.628 162.423 179.292 1.00 72.07  ? 672  LYS A NZ    1 
ATOM   4042 N N     . ALA A 1 673  ? 142.190 158.584 175.802 1.00 62.05  ? 673  ALA A N     1 
ATOM   4043 C CA    . ALA A 1 673  ? 140.825 158.093 175.659 1.00 59.94  ? 673  ALA A CA    1 
ATOM   4044 C C     . ALA A 1 673  ? 140.744 156.575 175.744 1.00 61.60  ? 673  ALA A C     1 
ATOM   4045 O O     . ALA A 1 673  ? 139.690 156.044 176.108 1.00 58.92  ? 673  ALA A O     1 
ATOM   4046 C CB    . ALA A 1 673  ? 140.228 158.568 174.334 1.00 59.95  ? 673  ALA A CB    1 
ATOM   4047 N N     . VAL A 1 674  ? 141.826 155.869 175.419 1.00 59.69  ? 674  VAL A N     1 
ATOM   4048 C CA    . VAL A 1 674  ? 141.852 154.411 175.482 1.00 49.84  ? 674  VAL A CA    1 
ATOM   4049 C C     . VAL A 1 674  ? 142.744 153.886 176.593 1.00 49.02  ? 674  VAL A C     1 
ATOM   4050 O O     . VAL A 1 674  ? 142.780 152.663 176.809 1.00 49.85  ? 674  VAL A O     1 
ATOM   4051 C CB    . VAL A 1 674  ? 142.278 153.793 174.134 1.00 51.36  ? 674  VAL A CB    1 
ATOM   4052 C CG1   . VAL A 1 674  ? 141.338 154.237 173.026 1.00 56.98  ? 674  VAL A CG1   1 
ATOM   4053 C CG2   . VAL A 1 674  ? 143.713 154.170 173.806 1.00 51.74  ? 674  VAL A CG2   1 
ATOM   4054 N N     . LYS A 1 675  ? 143.464 154.753 177.300 1.00 52.71  ? 675  LYS A N     1 
ATOM   4055 C CA    . LYS A 1 675  ? 144.306 154.312 178.400 1.00 49.98  ? 675  LYS A CA    1 
ATOM   4056 C C     . LYS A 1 675  ? 143.462 153.818 179.567 1.00 51.73  ? 675  LYS A C     1 
ATOM   4057 O O     . LYS A 1 675  ? 142.338 154.274 179.792 1.00 58.68  ? 675  LYS A O     1 
ATOM   4058 C CB    . LYS A 1 675  ? 145.208 155.448 178.877 1.00 53.24  ? 675  LYS A CB    1 
ATOM   4059 C CG    . LYS A 1 675  ? 146.672 155.291 178.519 1.00 51.37  ? 675  LYS A CG    1 
ATOM   4060 C CD    . LYS A 1 675  ? 147.516 156.277 179.306 1.00 55.89  ? 675  LYS A CD    1 
ATOM   4061 C CE    . LYS A 1 675  ? 148.990 156.135 178.984 1.00 60.84  ? 675  LYS A CE    1 
ATOM   4062 N NZ    . LYS A 1 675  ? 149.838 156.862 179.966 1.00 61.55  ? 675  LYS A NZ    1 
ATOM   4063 N N     . TYR A 1 676  ? 144.019 152.870 180.311 1.00 49.88  ? 676  TYR A N     1 
ATOM   4064 C CA    . TYR A 1 676  ? 143.415 152.462 181.564 1.00 48.14  ? 676  TYR A CA    1 
ATOM   4065 C C     . TYR A 1 676  ? 143.504 153.600 182.578 1.00 58.54  ? 676  TYR A C     1 
ATOM   4066 O O     . TYR A 1 676  ? 144.469 154.369 182.575 1.00 57.36  ? 676  TYR A O     1 
ATOM   4067 C CB    . TYR A 1 676  ? 144.122 151.234 182.125 1.00 44.82  ? 676  TYR A CB    1 
ATOM   4068 C CG    . TYR A 1 676  ? 143.339 149.946 182.052 1.00 48.75  ? 676  TYR A CG    1 
ATOM   4069 C CD1   . TYR A 1 676  ? 142.153 149.790 182.754 1.00 50.58  ? 676  TYR A CD1   1 
ATOM   4070 C CD2   . TYR A 1 676  ? 143.805 148.873 181.308 1.00 47.04  ? 676  TYR A CD2   1 
ATOM   4071 C CE1   . TYR A 1 676  ? 141.444 148.609 182.698 1.00 51.69  ? 676  TYR A CE1   1 
ATOM   4072 C CE2   . TYR A 1 676  ? 143.104 147.689 181.247 1.00 46.64  ? 676  TYR A CE2   1 
ATOM   4073 C CZ    . TYR A 1 676  ? 141.925 147.562 181.944 1.00 52.34  ? 676  TYR A CZ    1 
ATOM   4074 O OH    . TYR A 1 676  ? 141.223 146.381 181.885 1.00 62.35  ? 676  TYR A OH    1 
ATOM   4075 N N     . PRO A 1 677  ? 142.504 153.742 183.444 1.00 69.32  ? 677  PRO A N     1 
ATOM   4076 C CA    . PRO A 1 677  ? 142.674 154.613 184.609 1.00 62.62  ? 677  PRO A CA    1 
ATOM   4077 C C     . PRO A 1 677  ? 143.817 154.106 185.475 1.00 66.47  ? 677  PRO A C     1 
ATOM   4078 O O     . PRO A 1 677  ? 144.058 152.901 185.575 1.00 65.40  ? 677  PRO A O     1 
ATOM   4079 C CB    . PRO A 1 677  ? 141.326 154.515 185.331 1.00 60.79  ? 677  PRO A CB    1 
ATOM   4080 C CG    . PRO A 1 677  ? 140.359 154.129 184.261 1.00 62.37  ? 677  PRO A CG    1 
ATOM   4081 C CD    . PRO A 1 677  ? 141.125 153.239 183.324 1.00 66.53  ? 677  PRO A CD    1 
ATOM   4082 N N     . LYS A 1 678  ? 144.529 155.051 186.096 1.00 65.12  ? 678  LYS A N     1 
ATOM   4083 C CA    . LYS A 1 678  ? 145.763 154.720 186.804 1.00 67.78  ? 678  LYS A CA    1 
ATOM   4084 C C     . LYS A 1 678  ? 145.550 153.622 187.840 1.00 71.54  ? 678  LYS A C     1 
ATOM   4085 O O     . LYS A 1 678  ? 146.420 152.767 188.038 1.00 67.18  ? 678  LYS A O     1 
ATOM   4086 C CB    . LYS A 1 678  ? 146.331 155.977 187.465 1.00 71.45  ? 678  LYS A CB    1 
ATOM   4087 C CG    . LYS A 1 678  ? 147.614 155.752 188.245 1.00 73.91  ? 678  LYS A CG    1 
ATOM   4088 C CD    . LYS A 1 678  ? 148.707 155.183 187.359 1.00 69.75  ? 678  LYS A CD    1 
ATOM   4089 C CE    . LYS A 1 678  ? 150.022 155.078 188.112 1.00 69.17  ? 678  LYS A CE    1 
ATOM   4090 N NZ    . LYS A 1 678  ? 149.888 154.267 189.353 1.00 68.87  ? 678  LYS A NZ    1 
ATOM   4091 N N     . GLN A 1 679  ? 144.397 153.623 188.503 1.00 74.57  ? 679  GLN A N     1 
ATOM   4092 C CA    . GLN A 1 679  ? 144.095 152.633 189.529 1.00 72.73  ? 679  GLN A CA    1 
ATOM   4093 C C     . GLN A 1 679  ? 143.207 151.500 189.030 1.00 69.84  ? 679  GLN A C     1 
ATOM   4094 O O     . GLN A 1 679  ? 142.864 150.613 189.818 1.00 68.21  ? 679  GLN A O     1 
ATOM   4095 C CB    . GLN A 1 679  ? 143.435 153.310 190.736 1.00 72.19  ? 679  GLN A CB    1 
ATOM   4096 C CG    . GLN A 1 679  ? 144.393 154.109 191.612 1.00 77.35  ? 679  GLN A CG    1 
ATOM   4097 C CD    . GLN A 1 679  ? 144.873 155.391 190.955 1.00 80.23  ? 679  GLN A CD    1 
ATOM   4098 O OE1   . GLN A 1 679  ? 144.266 155.880 190.002 1.00 76.79  ? 679  GLN A OE1   1 
ATOM   4099 N NE2   . GLN A 1 679  ? 145.970 155.941 191.462 1.00 76.61  ? 679  GLN A NE2   1 
ATOM   4100 N N     . ALA A 1 680  ? 142.827 151.500 187.753 1.00 64.80  ? 680  ALA A N     1 
ATOM   4101 C CA    . ALA A 1 680  ? 141.979 150.455 187.196 1.00 63.61  ? 680  ALA A CA    1 
ATOM   4102 C C     . ALA A 1 680  ? 142.764 149.351 186.501 1.00 61.37  ? 680  ALA A C     1 
ATOM   4103 O O     . ALA A 1 680  ? 142.152 148.439 185.937 1.00 57.41  ? 680  ALA A O     1 
ATOM   4104 C CB    . ALA A 1 680  ? 140.966 151.057 186.220 1.00 59.90  ? 680  ALA A CB    1 
ATOM   4105 N N     . ILE A 1 681  ? 144.094 149.414 186.520 1.00 59.86  ? 681  ILE A N     1 
ATOM   4106 C CA    . ILE A 1 681  ? 144.904 148.336 185.944 1.00 54.83  ? 681  ILE A CA    1 
ATOM   4107 C C     . ILE A 1 681  ? 144.599 147.044 186.691 1.00 55.87  ? 681  ILE A C     1 
ATOM   4108 O O     . ILE A 1 681  ? 144.404 147.076 187.923 1.00 62.12  ? 681  ILE A O     1 
ATOM   4109 C CB    . ILE A 1 681  ? 146.401 148.681 186.033 1.00 59.48  ? 681  ILE A CB    1 
ATOM   4110 C CG1   . ILE A 1 681  ? 146.643 150.161 185.722 1.00 59.41  ? 681  ILE A CG1   1 
ATOM   4111 C CG2   . ILE A 1 681  ? 147.225 147.796 185.108 1.00 53.66  ? 681  ILE A CG2   1 
ATOM   4112 C CD1   . ILE A 1 681  ? 146.836 150.465 184.262 1.00 51.32  ? 681  ILE A CD1   1 
ATOM   4113 N N     . PRO A 1 682  ? 144.517 145.894 186.020 1.00 56.26  ? 682  PRO A N     1 
ATOM   4114 C CA    . PRO A 1 682  ? 144.241 144.644 186.738 1.00 62.26  ? 682  PRO A CA    1 
ATOM   4115 C C     . PRO A 1 682  ? 145.300 144.349 187.791 1.00 62.83  ? 682  PRO A C     1 
ATOM   4116 O O     . PRO A 1 682  ? 146.478 144.676 187.631 1.00 65.36  ? 682  PRO A O     1 
ATOM   4117 C CB    . PRO A 1 682  ? 144.247 143.590 185.626 1.00 60.53  ? 682  PRO A CB    1 
ATOM   4118 C CG    . PRO A 1 682  ? 143.852 144.343 184.409 1.00 56.67  ? 682  PRO A CG    1 
ATOM   4119 C CD    . PRO A 1 682  ? 144.460 145.710 184.559 1.00 57.98  ? 682  PRO A CD    1 
ATOM   4120 N N     . ALA A 1 683  ? 144.854 143.729 188.887 1.00 59.91  ? 683  ALA A N     1 
ATOM   4121 C CA    . ALA A 1 683  ? 145.741 143.481 190.019 1.00 61.66  ? 683  ALA A CA    1 
ATOM   4122 C C     . ALA A 1 683  ? 146.887 142.551 189.643 1.00 61.71  ? 683  ALA A C     1 
ATOM   4123 O O     . ALA A 1 683  ? 148.031 142.763 190.064 1.00 62.02  ? 683  ALA A O     1 
ATOM   4124 C CB    . ALA A 1 683  ? 144.945 142.904 191.189 1.00 60.82  ? 683  ALA A CB    1 
ATOM   4125 N N     . HIS A 1 684  ? 146.602 141.512 188.855 1.00 60.08  ? 684  HIS A N     1 
ATOM   4126 C CA    . HIS A 1 684  ? 147.654 140.589 188.446 1.00 64.37  ? 684  HIS A CA    1 
ATOM   4127 C C     . HIS A 1 684  ? 148.681 141.256 187.543 1.00 61.80  ? 684  HIS A C     1 
ATOM   4128 O O     . HIS A 1 684  ? 149.788 140.731 187.391 1.00 59.97  ? 684  HIS A O     1 
ATOM   4129 C CB    . HIS A 1 684  ? 147.051 139.369 187.745 1.00 70.52  ? 684  HIS A CB    1 
ATOM   4130 C CG    . HIS A 1 684  ? 146.612 139.632 186.339 1.00 72.44  ? 684  HIS A CG    1 
ATOM   4131 N ND1   . HIS A 1 684  ? 145.419 140.249 186.033 1.00 70.44  ? 684  HIS A ND1   1 
ATOM   4132 C CD2   . HIS A 1 684  ? 147.206 139.353 185.154 1.00 69.41  ? 684  HIS A CD2   1 
ATOM   4133 C CE1   . HIS A 1 684  ? 145.298 140.344 184.721 1.00 69.88  ? 684  HIS A CE1   1 
ATOM   4134 N NE2   . HIS A 1 684  ? 146.369 139.807 184.164 1.00 70.54  ? 684  HIS A NE2   1 
ATOM   4135 N N     . LEU A 1 685  ? 148.340 142.396 186.945 1.00 58.95  ? 685  LEU A N     1 
ATOM   4136 C CA    . LEU A 1 685  ? 149.292 143.193 186.183 1.00 55.03  ? 685  LEU A CA    1 
ATOM   4137 C C     . LEU A 1 685  ? 149.894 144.329 186.993 1.00 53.43  ? 685  LEU A C     1 
ATOM   4138 O O     . LEU A 1 685  ? 151.027 144.736 186.719 1.00 56.62  ? 685  LEU A O     1 
ATOM   4139 C CB    . LEU A 1 685  ? 148.624 143.765 184.928 1.00 53.65  ? 685  LEU A CB    1 
ATOM   4140 C CG    . LEU A 1 685  ? 148.132 142.729 183.914 1.00 56.25  ? 685  LEU A CG    1 
ATOM   4141 C CD1   . LEU A 1 685  ? 147.488 143.409 182.725 1.00 52.55  ? 685  LEU A CD1   1 
ATOM   4142 C CD2   . LEU A 1 685  ? 149.273 141.834 183.464 1.00 60.57  ? 685  LEU A CD2   1 
ATOM   4143 N N     . GLN A 1 686  ? 149.164 144.854 187.980 1.00 55.81  ? 686  GLN A N     1 
ATOM   4144 C CA    . GLN A 1 686  ? 149.748 145.836 188.886 1.00 54.37  ? 686  GLN A CA    1 
ATOM   4145 C C     . GLN A 1 686  ? 150.835 145.216 189.751 1.00 58.83  ? 686  GLN A C     1 
ATOM   4146 O O     . GLN A 1 686  ? 151.787 145.905 190.136 1.00 60.60  ? 686  GLN A O     1 
ATOM   4147 C CB    . GLN A 1 686  ? 148.667 146.459 189.768 1.00 53.55  ? 686  GLN A CB    1 
ATOM   4148 C CG    . GLN A 1 686  ? 147.788 147.461 189.050 1.00 56.02  ? 686  GLN A CG    1 
ATOM   4149 C CD    . GLN A 1 686  ? 146.827 148.169 189.981 1.00 58.27  ? 686  GLN A CD    1 
ATOM   4150 O OE1   . GLN A 1 686  ? 146.530 147.682 191.071 1.00 64.96  ? 686  GLN A OE1   1 
ATOM   4151 N NE2   . GLN A 1 686  ? 146.340 149.329 189.558 1.00 56.30  ? 686  GLN A NE2   1 
ATOM   4152 N N     . SER A 1 687  ? 150.710 143.925 190.070 1.00 58.41  ? 687  SER A N     1 
ATOM   4153 C CA    . SER A 1 687  ? 151.747 143.244 190.835 1.00 53.27  ? 687  SER A CA    1 
ATOM   4154 C C     . SER A 1 687  ? 153.061 143.151 190.071 1.00 59.11  ? 687  SER A C     1 
ATOM   4155 O O     . SER A 1 687  ? 154.108 142.931 190.688 1.00 63.49  ? 687  SER A O     1 
ATOM   4156 C CB    . SER A 1 687  ? 151.276 141.845 191.233 1.00 59.44  ? 687  SER A CB    1 
ATOM   4157 O OG    . SER A 1 687  ? 150.980 141.064 190.089 1.00 65.02  ? 687  SER A OG    1 
ATOM   4158 N N     . LYS A 1 688  ? 153.029 143.314 188.751 1.00 56.48  ? 688  LYS A N     1 
ATOM   4159 C CA    . LYS A 1 688  ? 154.228 143.297 187.926 1.00 47.58  ? 688  LYS A CA    1 
ATOM   4160 C C     . LYS A 1 688  ? 154.838 144.679 187.742 1.00 45.07  ? 688  LYS A C     1 
ATOM   4161 O O     . LYS A 1 688  ? 155.812 144.816 186.994 1.00 48.56  ? 688  LYS A O     1 
ATOM   4162 C CB    . LYS A 1 688  ? 153.915 142.689 186.556 1.00 47.85  ? 688  LYS A CB    1 
ATOM   4163 C CG    . LYS A 1 688  ? 153.250 141.327 186.622 1.00 52.61  ? 688  LYS A CG    1 
ATOM   4164 C CD    . LYS A 1 688  ? 152.991 140.770 185.234 1.00 61.80  ? 688  LYS A CD    1 
ATOM   4165 C CE    . LYS A 1 688  ? 152.182 139.487 185.299 1.00 61.61  ? 688  LYS A CE    1 
ATOM   4166 N NZ    . LYS A 1 688  ? 152.826 138.465 186.168 1.00 62.47  ? 688  LYS A NZ    1 
ATOM   4167 N N     . GLY A 1 689  ? 154.296 145.700 188.400 1.00 46.91  ? 689  GLY A N     1 
ATOM   4168 C CA    . GLY A 1 689  ? 154.783 147.052 188.233 1.00 43.87  ? 689  GLY A CA    1 
ATOM   4169 C C     . GLY A 1 689  ? 154.221 147.791 187.043 1.00 42.63  ? 689  GLY A C     1 
ATOM   4170 O O     . GLY A 1 689  ? 154.692 148.893 186.740 1.00 42.57  ? 689  GLY A O     1 
ATOM   4171 N N     . ILE A 1 690  ? 153.231 147.224 186.359 1.00 43.88  ? 690  ILE A N     1 
ATOM   4172 C CA    . ILE A 1 690  ? 152.651 147.840 185.171 1.00 44.38  ? 690  ILE A CA    1 
ATOM   4173 C C     . ILE A 1 690  ? 151.700 148.945 185.619 1.00 43.57  ? 690  ILE A C     1 
ATOM   4174 O O     . ILE A 1 690  ? 150.622 148.672 186.151 1.00 50.96  ? 690  ILE A O     1 
ATOM   4175 C CB    . ILE A 1 690  ? 151.927 146.808 184.301 1.00 46.38  ? 690  ILE A CB    1 
ATOM   4176 C CG1   . ILE A 1 690  ? 152.910 145.751 183.800 1.00 36.52  ? 690  ILE A CG1   1 
ATOM   4177 C CG2   . ILE A 1 690  ? 151.231 147.484 183.133 1.00 43.03  ? 690  ILE A CG2   1 
ATOM   4178 C CD1   . ILE A 1 690  ? 152.254 144.635 183.037 1.00 41.64  ? 690  ILE A CD1   1 
ATOM   4179 N N     . LYS A 1 691  ? 152.102 150.197 185.406 1.00 39.97  ? 691  LYS A N     1 
ATOM   4180 C CA    . LYS A 1 691  ? 151.247 151.343 185.678 1.00 44.58  ? 691  LYS A CA    1 
ATOM   4181 C C     . LYS A 1 691  ? 150.617 151.921 184.420 1.00 48.39  ? 691  LYS A C     1 
ATOM   4182 O O     . LYS A 1 691  ? 149.618 152.641 184.520 1.00 56.90  ? 691  LYS A O     1 
ATOM   4183 C CB    . LYS A 1 691  ? 152.043 152.438 186.397 1.00 42.79  ? 691  LYS A CB    1 
ATOM   4184 C CG    . LYS A 1 691  ? 152.609 152.003 187.736 1.00 41.55  ? 691  LYS A CG    1 
ATOM   4185 C CD    . LYS A 1 691  ? 153.500 153.070 188.341 1.00 48.63  ? 691  LYS A CD    1 
ATOM   4186 C CE    . LYS A 1 691  ? 153.969 152.668 189.727 1.00 42.04  ? 691  LYS A CE    1 
ATOM   4187 N NZ    . LYS A 1 691  ? 154.712 151.379 189.709 1.00 38.21  ? 691  LYS A NZ    1 
ATOM   4188 N N     . ASN A 1 692  ? 151.168 151.614 183.250 1.00 45.67  ? 692  ASN A N     1 
ATOM   4189 C CA    . ASN A 1 692  ? 150.666 152.094 181.971 1.00 39.11  ? 692  ASN A CA    1 
ATOM   4190 C C     . ASN A 1 692  ? 150.068 150.925 181.203 1.00 37.97  ? 692  ASN A C     1 
ATOM   4191 O O     . ASN A 1 692  ? 150.730 149.900 181.011 1.00 40.49  ? 692  ASN A O     1 
ATOM   4192 C CB    . ASN A 1 692  ? 151.792 152.749 181.167 1.00 37.43  ? 692  ASN A CB    1 
ATOM   4193 C CG    . ASN A 1 692  ? 151.394 153.055 179.740 1.00 42.68  ? 692  ASN A CG    1 
ATOM   4194 O OD1   . ASN A 1 692  ? 150.221 153.259 179.437 1.00 51.85  ? 692  ASN A OD1   1 
ATOM   4195 N ND2   . ASN A 1 692  ? 152.378 153.090 178.851 1.00 40.47  ? 692  ASN A ND2   1 
ATOM   4196 N N     . LEU A 1 693  ? 148.820 151.079 180.767 1.00 36.60  ? 693  LEU A N     1 
ATOM   4197 C CA    . LEU A 1 693  ? 148.142 150.024 180.028 1.00 37.58  ? 693  LEU A CA    1 
ATOM   4198 C C     . LEU A 1 693  ? 147.006 150.640 179.225 1.00 38.98  ? 693  LEU A C     1 
ATOM   4199 O O     . LEU A 1 693  ? 146.537 151.741 179.523 1.00 46.43  ? 693  LEU A O     1 
ATOM   4200 C CB    . LEU A 1 693  ? 147.617 148.933 180.967 1.00 40.32  ? 693  LEU A CB    1 
ATOM   4201 C CG    . LEU A 1 693  ? 147.248 147.582 180.352 1.00 42.18  ? 693  LEU A CG    1 
ATOM   4202 C CD1   . LEU A 1 693  ? 148.467 146.934 179.723 1.00 38.24  ? 693  LEU A CD1   1 
ATOM   4203 C CD2   . LEU A 1 693  ? 146.631 146.670 181.395 1.00 42.97  ? 693  LEU A CD2   1 
ATOM   4204 N N     . LEU A 1 694  ? 146.575 149.914 178.197 1.00 38.19  ? 694  LEU A N     1 
ATOM   4205 C CA    . LEU A 1 694  ? 145.448 150.307 177.365 1.00 38.40  ? 694  LEU A CA    1 
ATOM   4206 C C     . LEU A 1 694  ? 144.252 149.419 177.679 1.00 42.32  ? 694  LEU A C     1 
ATOM   4207 O O     . LEU A 1 694  ? 144.397 148.204 177.843 1.00 45.99  ? 694  LEU A O     1 
ATOM   4208 C CB    . LEU A 1 694  ? 145.794 150.207 175.877 1.00 36.45  ? 694  LEU A CB    1 
ATOM   4209 C CG    . LEU A 1 694  ? 146.915 151.105 175.354 1.00 36.39  ? 694  LEU A CG    1 
ATOM   4210 C CD1   . LEU A 1 694  ? 147.137 150.866 173.872 1.00 36.05  ? 694  LEU A CD1   1 
ATOM   4211 C CD2   . LEU A 1 694  ? 146.607 152.565 175.621 1.00 40.47  ? 694  LEU A CD2   1 
ATOM   4212 N N     . LYS A 1 695  ? 143.075 150.032 177.767 1.00 40.84  ? 695  LYS A N     1 
ATOM   4213 C CA    . LYS A 1 695  ? 141.869 149.287 178.084 1.00 43.78  ? 695  LYS A CA    1 
ATOM   4214 C C     . LYS A 1 695  ? 141.572 148.265 176.989 1.00 49.85  ? 695  LYS A C     1 
ATOM   4215 O O     . LYS A 1 695  ? 141.857 148.504 175.814 1.00 54.18  ? 695  LYS A O     1 
ATOM   4216 C CB    . LYS A 1 695  ? 140.684 150.234 178.245 1.00 46.07  ? 695  LYS A CB    1 
ATOM   4217 C CG    . LYS A 1 695  ? 140.805 151.178 179.427 1.00 55.02  ? 695  LYS A CG    1 
ATOM   4218 C CD    . LYS A 1 695  ? 139.673 152.190 179.460 1.00 57.79  ? 695  LYS A CD    1 
ATOM   4219 C CE    . LYS A 1 695  ? 139.727 153.115 178.257 1.00 62.85  ? 695  LYS A CE    1 
ATOM   4220 N NZ    . LYS A 1 695  ? 138.677 154.167 178.315 1.00 65.51  ? 695  LYS A NZ    1 
ATOM   4221 N N     . PRO A 1 696  ? 141.023 147.106 177.352 1.00 54.30  ? 696  PRO A N     1 
ATOM   4222 C CA    . PRO A 1 696  ? 140.655 146.121 176.330 1.00 53.95  ? 696  PRO A CA    1 
ATOM   4223 C C     . PRO A 1 696  ? 139.619 146.690 175.373 1.00 52.89  ? 696  PRO A C     1 
ATOM   4224 O O     . PRO A 1 696  ? 138.702 147.409 175.775 1.00 51.69  ? 696  PRO A O     1 
ATOM   4225 C CB    . PRO A 1 696  ? 140.093 144.952 177.148 1.00 55.20  ? 696  PRO A CB    1 
ATOM   4226 C CG    . PRO A 1 696  ? 139.686 145.557 178.449 1.00 53.92  ? 696  PRO A CG    1 
ATOM   4227 C CD    . PRO A 1 696  ? 140.675 146.651 178.707 1.00 52.25  ? 696  PRO A CD    1 
ATOM   4228 N N     . GLY A 1 697  ? 139.767 146.354 174.096 1.00 48.66  ? 697  GLY A N     1 
ATOM   4229 C CA    . GLY A 1 697  ? 138.948 146.971 173.075 1.00 48.99  ? 697  GLY A CA    1 
ATOM   4230 C C     . GLY A 1 697  ? 139.397 148.354 172.673 1.00 49.42  ? 697  GLY A C     1 
ATOM   4231 O O     . GLY A 1 697  ? 138.625 149.085 172.044 1.00 52.88  ? 697  GLY A O     1 
ATOM   4232 N N     . TRP A 1 698  ? 140.625 148.741 173.028 1.00 45.89  ? 698  TRP A N     1 
ATOM   4233 C CA    . TRP A 1 698  ? 141.137 150.054 172.648 1.00 42.17  ? 698  TRP A CA    1 
ATOM   4234 C C     . TRP A 1 698  ? 141.221 150.209 171.137 1.00 48.63  ? 698  TRP A C     1 
ATOM   4235 O O     . TRP A 1 698  ? 141.138 151.329 170.623 1.00 49.65  ? 698  TRP A O     1 
ATOM   4236 C CB    . TRP A 1 698  ? 142.512 150.278 173.275 1.00 43.73  ? 698  TRP A CB    1 
ATOM   4237 C CG    . TRP A 1 698  ? 143.527 149.282 172.825 1.00 44.58  ? 698  TRP A CG    1 
ATOM   4238 C CD1   . TRP A 1 698  ? 143.807 148.078 173.400 1.00 38.31  ? 698  TRP A CD1   1 
ATOM   4239 C CD2   . TRP A 1 698  ? 144.398 149.398 171.695 1.00 48.55  ? 698  TRP A CD2   1 
ATOM   4240 N NE1   . TRP A 1 698  ? 144.799 147.438 172.701 1.00 43.23  ? 698  TRP A NE1   1 
ATOM   4241 C CE2   . TRP A 1 698  ? 145.179 148.229 171.648 1.00 47.96  ? 698  TRP A CE2   1 
ATOM   4242 C CE3   . TRP A 1 698  ? 144.594 150.379 170.718 1.00 43.82  ? 698  TRP A CE3   1 
ATOM   4243 C CZ2   . TRP A 1 698  ? 146.140 148.014 170.666 1.00 41.68  ? 698  TRP A CZ2   1 
ATOM   4244 C CZ3   . TRP A 1 698  ? 145.547 150.163 169.745 1.00 41.50  ? 698  TRP A CZ3   1 
ATOM   4245 C CH2   . TRP A 1 698  ? 146.307 148.991 169.725 1.00 39.77  ? 698  TRP A CH2   1 
ATOM   4246 N N     . GLN A 1 699  ? 141.402 149.102 170.412 1.00 51.88  ? 699  GLN A N     1 
ATOM   4247 C CA    . GLN A 1 699  ? 141.413 149.163 168.955 1.00 47.09  ? 699  GLN A CA    1 
ATOM   4248 C C     . GLN A 1 699  ? 140.067 149.611 168.406 1.00 49.06  ? 699  GLN A C     1 
ATOM   4249 O O     . GLN A 1 699  ? 140.015 150.369 167.433 1.00 55.27  ? 699  GLN A O     1 
ATOM   4250 C CB    . GLN A 1 699  ? 141.794 147.802 168.374 1.00 45.57  ? 699  GLN A CB    1 
ATOM   4251 C CG    . GLN A 1 699  ? 143.189 147.336 168.743 1.00 47.62  ? 699  GLN A CG    1 
ATOM   4252 C CD    . GLN A 1 699  ? 143.525 145.986 168.145 1.00 56.18  ? 699  GLN A CD    1 
ATOM   4253 O OE1   . GLN A 1 699  ? 142.649 145.145 167.952 1.00 61.45  ? 699  GLN A OE1   1 
ATOM   4254 N NE2   . GLN A 1 699  ? 144.800 145.774 167.842 1.00 47.27  ? 699  GLN A NE2   1 
ATOM   4255 N N     . GLY A 1 700  ? 138.973 149.162 169.017 1.00 49.33  ? 700  GLY A N     1 
ATOM   4256 C CA    . GLY A 1 700  ? 137.662 149.499 168.496 1.00 46.19  ? 700  GLY A CA    1 
ATOM   4257 C C     . GLY A 1 700  ? 137.406 148.792 167.181 1.00 52.62  ? 700  GLY A C     1 
ATOM   4258 O O     . GLY A 1 700  ? 137.829 147.651 166.966 1.00 52.16  ? 700  GLY A O     1 
ATOM   4259 N N     . GLU A 1 701  ? 136.701 149.475 166.286 1.00 53.24  ? 701  GLU A N     1 
ATOM   4260 C CA    . GLU A 1 701  ? 136.416 148.955 164.957 1.00 53.74  ? 701  GLU A CA    1 
ATOM   4261 C C     . GLU A 1 701  ? 137.447 149.393 163.927 1.00 50.19  ? 701  GLU A C     1 
ATOM   4262 O O     . GLU A 1 701  ? 137.264 149.132 162.733 1.00 53.01  ? 701  GLU A O     1 
ATOM   4263 C CB    . GLU A 1 701  ? 135.016 149.386 164.514 1.00 56.98  ? 701  GLU A CB    1 
ATOM   4264 C CG    . GLU A 1 701  ? 133.915 148.966 165.472 1.00 65.18  ? 701  GLU A CG    1 
ATOM   4265 C CD    . GLU A 1 701  ? 133.816 147.460 165.624 1.00 74.91  ? 701  GLU A CD    1 
ATOM   4266 O OE1   . GLU A 1 701  ? 134.106 146.739 164.646 1.00 78.01  ? 701  GLU A OE1   1 
ATOM   4267 O OE2   . GLU A 1 701  ? 133.450 146.996 166.725 1.00 70.39  ? 701  GLU A OE2   1 
ATOM   4268 N N     . ALA A 1 702  ? 138.517 150.052 164.361 1.00 41.91  ? 702  ALA A N     1 
ATOM   4269 C CA    . ALA A 1 702  ? 139.545 150.513 163.440 1.00 36.30  ? 702  ALA A CA    1 
ATOM   4270 C C     . ALA A 1 702  ? 140.272 149.338 162.803 1.00 38.27  ? 702  ALA A C     1 
ATOM   4271 O O     . ALA A 1 702  ? 140.604 148.354 163.469 1.00 38.18  ? 702  ALA A O     1 
ATOM   4272 C CB    . ALA A 1 702  ? 140.543 151.411 164.166 1.00 32.80  ? 702  ALA A CB    1 
ATOM   4273 N N     . LYS A 1 703  ? 140.517 149.447 161.498 1.00 38.80  ? 703  LYS A N     1 
ATOM   4274 C CA    . LYS A 1 703  ? 141.309 148.463 160.775 1.00 32.55  ? 703  LYS A CA    1 
ATOM   4275 C C     . LYS A 1 703  ? 142.743 148.913 160.548 1.00 26.62  ? 703  LYS A C     1 
ATOM   4276 O O     . LYS A 1 703  ? 143.630 148.064 160.417 1.00 25.95  ? 703  LYS A O     1 
ATOM   4277 C CB    . LYS A 1 703  ? 140.658 148.143 159.426 1.00 32.92  ? 703  LYS A CB    1 
ATOM   4278 C CG    . LYS A 1 703  ? 139.226 147.658 159.541 1.00 37.21  ? 703  LYS A CG    1 
ATOM   4279 C CD    . LYS A 1 703  ? 139.122 146.479 160.494 1.00 41.27  ? 703  LYS A CD    1 
ATOM   4280 C CE    . LYS A 1 703  ? 139.740 145.226 159.901 1.00 42.57  ? 703  LYS A CE    1 
ATOM   4281 N NZ    . LYS A 1 703  ? 138.967 144.740 158.728 1.00 47.25  ? 703  LYS A NZ    1 
ATOM   4282 N N     . ILE A 1 704  ? 142.986 150.220 160.502 1.00 24.35  ? 704  ILE A N     1 
ATOM   4283 C CA    . ILE A 1 704  ? 144.326 150.786 160.439 1.00 24.53  ? 704  ILE A CA    1 
ATOM   4284 C C     . ILE A 1 704  ? 144.537 151.608 161.700 1.00 26.17  ? 704  ILE A C     1 
ATOM   4285 O O     . ILE A 1 704  ? 143.690 152.435 162.054 1.00 32.83  ? 704  ILE A O     1 
ATOM   4286 C CB    . ILE A 1 704  ? 144.525 151.653 159.183 1.00 24.63  ? 704  ILE A CB    1 
ATOM   4287 C CG1   . ILE A 1 704  ? 144.407 150.801 157.921 1.00 24.93  ? 704  ILE A CG1   1 
ATOM   4288 C CG2   . ILE A 1 704  ? 145.871 152.352 159.226 1.00 21.93  ? 704  ILE A CG2   1 
ATOM   4289 C CD1   . ILE A 1 704  ? 144.542 151.587 156.638 1.00 24.99  ? 704  ILE A CD1   1 
ATOM   4290 N N     . ILE A 1 705  ? 145.652 151.372 162.381 1.00 26.01  ? 705  ILE A N     1 
ATOM   4291 C CA    . ILE A 1 705  ? 145.979 152.072 163.615 1.00 26.89  ? 705  ILE A CA    1 
ATOM   4292 C C     . ILE A 1 705  ? 147.268 152.845 163.391 1.00 25.72  ? 705  ILE A C     1 
ATOM   4293 O O     . ILE A 1 705  ? 148.305 152.256 163.065 1.00 28.06  ? 705  ILE A O     1 
ATOM   4294 C CB    . ILE A 1 705  ? 146.105 151.107 164.802 1.00 28.60  ? 705  ILE A CB    1 
ATOM   4295 C CG1   . ILE A 1 705  ? 144.755 150.438 165.062 1.00 29.36  ? 705  ILE A CG1   1 
ATOM   4296 C CG2   . ILE A 1 705  ? 146.595 151.840 166.040 1.00 27.99  ? 705  ILE A CG2   1 
ATOM   4297 C CD1   . ILE A 1 705  ? 144.720 149.594 166.299 1.00 38.43  ? 705  ILE A CD1   1 
ATOM   4298 N N     . LEU A 1 706  ? 147.199 154.160 163.561 1.00 27.55  ? 706  LEU A N     1 
ATOM   4299 C CA    . LEU A 1 706  ? 148.340 155.045 163.385 1.00 26.88  ? 706  LEU A CA    1 
ATOM   4300 C C     . LEU A 1 706  ? 148.973 155.319 164.740 1.00 30.16  ? 706  LEU A C     1 
ATOM   4301 O O     . LEU A 1 706  ? 148.277 155.680 165.693 1.00 35.76  ? 706  LEU A O     1 
ATOM   4302 C CB    . LEU A 1 706  ? 147.916 156.357 162.726 1.00 29.92  ? 706  LEU A CB    1 
ATOM   4303 C CG    . LEU A 1 706  ? 147.230 156.262 161.366 1.00 30.44  ? 706  LEU A CG    1 
ATOM   4304 C CD1   . LEU A 1 706  ? 146.710 157.623 160.941 1.00 37.84  ? 706  LEU A CD1   1 
ATOM   4305 C CD2   . LEU A 1 706  ? 148.191 155.714 160.332 1.00 31.07  ? 706  LEU A CD2   1 
ATOM   4306 N N     . THR A 1 707  ? 150.287 155.141 164.825 1.00 24.35  ? 707  THR A N     1 
ATOM   4307 C CA    . THR A 1 707  ? 150.996 155.351 166.077 1.00 27.23  ? 707  THR A CA    1 
ATOM   4308 C C     . THR A 1 707  ? 152.402 155.840 165.769 1.00 32.47  ? 707  THR A C     1 
ATOM   4309 O O     . THR A 1 707  ? 152.890 155.724 164.643 1.00 36.43  ? 707  THR A O     1 
ATOM   4310 C CB    . THR A 1 707  ? 151.041 154.072 166.924 1.00 27.51  ? 707  THR A CB    1 
ATOM   4311 O OG1   . THR A 1 707  ? 151.502 154.384 168.241 1.00 37.26  ? 707  THR A OG1   1 
ATOM   4312 C CG2   . THR A 1 707  ? 151.976 153.053 166.305 1.00 24.97  ? 707  THR A CG2   1 
ATOM   4313 N N     . THR A 1 708  ? 153.041 156.411 166.781 1.00 33.36  ? 708  THR A N     1 
ATOM   4314 C CA    . THR A 1 708  ? 154.395 156.927 166.667 1.00 34.61  ? 708  THR A CA    1 
ATOM   4315 C C     . THR A 1 708  ? 155.390 155.900 167.197 1.00 33.59  ? 708  THR A C     1 
ATOM   4316 O O     . THR A 1 708  ? 155.030 154.964 167.913 1.00 32.11  ? 708  THR A O     1 
ATOM   4317 C CB    . THR A 1 708  ? 154.532 158.248 167.431 1.00 41.10  ? 708  THR A CB    1 
ATOM   4318 O OG1   . THR A 1 708  ? 153.318 158.996 167.308 1.00 49.00  ? 708  THR A OG1   1 
ATOM   4319 C CG2   . THR A 1 708  ? 155.677 159.082 166.872 1.00 43.54  ? 708  THR A CG2   1 
ATOM   4320 N N     . TYR A 1 709  ? 156.659 156.081 166.821 1.00 31.54  ? 709  TYR A N     1 
ATOM   4321 C CA    . TYR A 1 709  ? 157.709 155.222 167.355 1.00 32.68  ? 709  TYR A CA    1 
ATOM   4322 C C     . TYR A 1 709  ? 157.835 155.385 168.864 1.00 34.96  ? 709  TYR A C     1 
ATOM   4323 O O     . TYR A 1 709  ? 158.061 154.407 169.586 1.00 33.74  ? 709  TYR A O     1 
ATOM   4324 C CB    . TYR A 1 709  ? 159.040 155.521 166.665 1.00 35.91  ? 709  TYR A CB    1 
ATOM   4325 C CG    . TYR A 1 709  ? 159.125 154.998 165.249 1.00 34.81  ? 709  TYR A CG    1 
ATOM   4326 C CD1   . TYR A 1 709  ? 159.394 153.660 164.998 1.00 34.20  ? 709  TYR A CD1   1 
ATOM   4327 C CD2   . TYR A 1 709  ? 158.942 155.843 164.165 1.00 37.56  ? 709  TYR A CD2   1 
ATOM   4328 C CE1   . TYR A 1 709  ? 159.473 153.177 163.710 1.00 31.06  ? 709  TYR A CE1   1 
ATOM   4329 C CE2   . TYR A 1 709  ? 159.020 155.369 162.872 1.00 33.02  ? 709  TYR A CE2   1 
ATOM   4330 C CZ    . TYR A 1 709  ? 159.286 154.036 162.651 1.00 29.99  ? 709  TYR A CZ    1 
ATOM   4331 O OH    . TYR A 1 709  ? 159.364 153.561 161.366 1.00 34.41  ? 709  TYR A OH    1 
ATOM   4332 N N     . GLU A 1 710  ? 157.690 156.616 169.361 1.00 37.53  ? 710  GLU A N     1 
ATOM   4333 C CA    . GLU A 1 710  ? 157.704 156.835 170.803 1.00 34.70  ? 710  GLU A CA    1 
ATOM   4334 C C     . GLU A 1 710  ? 156.492 156.199 171.472 1.00 31.92  ? 710  GLU A C     1 
ATOM   4335 O O     . GLU A 1 710  ? 156.611 155.608 172.550 1.00 37.28  ? 710  GLU A O     1 
ATOM   4336 C CB    . GLU A 1 710  ? 157.767 158.331 171.104 1.00 40.43  ? 710  GLU A CB    1 
ATOM   4337 C CG    . GLU A 1 710  ? 159.012 159.009 170.560 1.00 51.74  ? 710  GLU A CG    1 
ATOM   4338 C CD    . GLU A 1 710  ? 159.024 160.502 170.814 1.00 71.52  ? 710  GLU A CD    1 
ATOM   4339 O OE1   . GLU A 1 710  ? 158.054 161.014 171.411 1.00 66.98  ? 710  GLU A OE1   1 
ATOM   4340 O OE2   . GLU A 1 710  ? 160.004 161.165 170.415 1.00 78.88  ? 710  GLU A OE2   1 
ATOM   4341 N N     . THR A 1 711  ? 155.316 156.305 170.849 1.00 33.26  ? 711  THR A N     1 
ATOM   4342 C CA    . THR A 1 711  ? 154.140 155.620 171.376 1.00 30.90  ? 711  THR A CA    1 
ATOM   4343 C C     . THR A 1 711  ? 154.280 154.108 171.262 1.00 29.48  ? 711  THR A C     1 
ATOM   4344 O O     . THR A 1 711  ? 153.789 153.373 172.126 1.00 34.17  ? 711  THR A O     1 
ATOM   4345 C CB    . THR A 1 711  ? 152.882 156.097 170.649 1.00 33.76  ? 711  THR A CB    1 
ATOM   4346 O OG1   . THR A 1 711  ? 152.827 157.528 170.678 1.00 42.06  ? 711  THR A OG1   1 
ATOM   4347 C CG2   . THR A 1 711  ? 151.636 155.540 171.315 1.00 33.02  ? 711  THR A CG2   1 
ATOM   4348 N N     . LEU A 1 712  ? 154.941 153.628 170.207 1.00 33.58  ? 712  LEU A N     1 
ATOM   4349 C CA    . LEU A 1 712  ? 155.233 152.204 170.089 1.00 28.87  ? 712  LEU A CA    1 
ATOM   4350 C C     . LEU A 1 712  ? 156.117 151.730 171.234 1.00 32.75  ? 712  LEU A C     1 
ATOM   4351 O O     . LEU A 1 712  ? 155.895 150.653 171.798 1.00 35.50  ? 712  LEU A O     1 
ATOM   4352 C CB    . LEU A 1 712  ? 155.901 151.926 168.742 1.00 30.40  ? 712  LEU A CB    1 
ATOM   4353 C CG    . LEU A 1 712  ? 156.409 150.521 168.420 1.00 30.56  ? 712  LEU A CG    1 
ATOM   4354 C CD1   . LEU A 1 712  ? 155.261 149.585 168.104 1.00 32.09  ? 712  LEU A CD1   1 
ATOM   4355 C CD2   . LEU A 1 712  ? 157.390 150.576 167.263 1.00 28.34  ? 712  LEU A CD2   1 
ATOM   4356 N N     . ARG A 1 713  ? 157.132 152.522 171.585 1.00 34.86  ? 713  ARG A N     1 
ATOM   4357 C CA    . ARG A 1 713  ? 157.999 152.178 172.707 1.00 31.68  ? 713  ARG A CA    1 
ATOM   4358 C C     . ARG A 1 713  ? 157.247 152.234 174.031 1.00 35.12  ? 713  ARG A C     1 
ATOM   4359 O O     . ARG A 1 713  ? 157.428 151.365 174.891 1.00 38.41  ? 713  ARG A O     1 
ATOM   4360 C CB    . ARG A 1 713  ? 159.201 153.120 172.735 1.00 31.79  ? 713  ARG A CB    1 
ATOM   4361 C CG    . ARG A 1 713  ? 160.138 152.918 173.908 1.00 34.45  ? 713  ARG A CG    1 
ATOM   4362 C CD    . ARG A 1 713  ? 161.019 154.137 174.084 1.00 35.02  ? 713  ARG A CD    1 
ATOM   4363 N NE    . ARG A 1 713  ? 160.236 155.299 174.485 1.00 38.50  ? 713  ARG A NE    1 
ATOM   4364 C CZ    . ARG A 1 713  ? 160.537 156.551 174.171 1.00 44.67  ? 713  ARG A CZ    1 
ATOM   4365 N NH1   . ARG A 1 713  ? 161.588 156.841 173.422 1.00 47.90  ? 713  ARG A NH1   1 
ATOM   4366 N NH2   . ARG A 1 713  ? 159.759 157.535 174.611 1.00 38.49  ? 713  ARG A NH2   1 
ATOM   4367 N N     . ASP A 1 714  ? 156.400 153.249 174.214 1.00 36.05  ? 714  ASP A N     1 
ATOM   4368 C CA    . ASP A 1 714  ? 155.694 153.423 175.478 1.00 32.92  ? 714  ASP A CA    1 
ATOM   4369 C C     . ASP A 1 714  ? 154.552 152.431 175.646 1.00 32.67  ? 714  ASP A C     1 
ATOM   4370 O O     . ASP A 1 714  ? 154.258 152.021 176.773 1.00 38.96  ? 714  ASP A O     1 
ATOM   4371 C CB    . ASP A 1 714  ? 155.162 154.852 175.592 1.00 37.96  ? 714  ASP A CB    1 
ATOM   4372 C CG    . ASP A 1 714  ? 156.269 155.888 175.588 1.00 44.86  ? 714  ASP A CG    1 
ATOM   4373 O OD1   . ASP A 1 714  ? 157.453 155.496 175.618 1.00 40.37  ? 714  ASP A OD1   1 
ATOM   4374 O OD2   . ASP A 1 714  ? 155.953 157.094 175.549 1.00 48.61  ? 714  ASP A OD2   1 
ATOM   4375 N N     . GLN A 1 715  ? 153.896 152.043 174.555 1.00 33.16  ? 715  GLN A N     1 
ATOM   4376 C CA    . GLN A 1 715  ? 152.787 151.098 174.602 1.00 33.33  ? 715  GLN A CA    1 
ATOM   4377 C C     . GLN A 1 715  ? 153.170 149.746 174.011 1.00 35.18  ? 715  GLN A C     1 
ATOM   4378 O O     . GLN A 1 715  ? 152.318 149.036 173.473 1.00 36.13  ? 715  GLN A O     1 
ATOM   4379 C CB    . GLN A 1 715  ? 151.566 151.665 173.880 1.00 33.24  ? 715  GLN A CB    1 
ATOM   4380 C CG    . GLN A 1 715  ? 151.156 153.057 174.334 1.00 37.83  ? 715  GLN A CG    1 
ATOM   4381 C CD    . GLN A 1 715  ? 150.667 153.093 175.768 1.00 43.94  ? 715  GLN A CD    1 
ATOM   4382 O OE1   . GLN A 1 715  ? 150.799 154.107 176.452 1.00 46.32  ? 715  GLN A OE1   1 
ATOM   4383 N NE2   . GLN A 1 715  ? 150.091 151.989 176.229 1.00 39.98  ? 715  GLN A NE2   1 
ATOM   4384 N N     . GLU A 1 716  ? 154.449 149.377 174.109 1.00 33.66  ? 716  GLU A N     1 
ATOM   4385 C CA    . GLU A 1 716  ? 154.906 148.114 173.538 1.00 34.68  ? 716  GLU A CA    1 
ATOM   4386 C C     . GLU A 1 716  ? 154.210 146.928 174.192 1.00 38.19  ? 716  GLU A C     1 
ATOM   4387 O O     . GLU A 1 716  ? 153.842 145.963 173.511 1.00 48.62  ? 716  GLU A O     1 
ATOM   4388 C CB    . GLU A 1 716  ? 156.423 147.993 173.681 1.00 33.00  ? 716  GLU A CB    1 
ATOM   4389 C CG    . GLU A 1 716  ? 156.972 146.609 173.389 1.00 40.37  ? 716  GLU A CG    1 
ATOM   4390 C CD    . GLU A 1 716  ? 158.392 146.428 173.888 1.00 45.38  ? 716  GLU A CD    1 
ATOM   4391 O OE1   . GLU A 1 716  ? 158.994 147.421 174.344 1.00 48.46  ? 716  GLU A OE1   1 
ATOM   4392 O OE2   . GLU A 1 716  ? 158.904 145.292 173.828 1.00 45.89  ? 716  GLU A OE2   1 
ATOM   4393 N N     . PHE A 1 717  ? 154.015 146.982 175.510 1.00 32.07  ? 717  PHE A N     1 
ATOM   4394 C CA    . PHE A 1 717  ? 153.344 145.886 176.200 1.00 32.40  ? 717  PHE A CA    1 
ATOM   4395 C C     . PHE A 1 717  ? 151.915 145.714 175.702 1.00 35.26  ? 717  PHE A C     1 
ATOM   4396 O O     . PHE A 1 717  ? 151.454 144.588 175.495 1.00 39.11  ? 717  PHE A O     1 
ATOM   4397 C CB    . PHE A 1 717  ? 153.364 146.124 177.710 1.00 37.84  ? 717  PHE A CB    1 
ATOM   4398 C CG    . PHE A 1 717  ? 152.738 145.016 178.508 1.00 41.81  ? 717  PHE A CG    1 
ATOM   4399 C CD1   . PHE A 1 717  ? 153.457 143.874 178.815 1.00 46.33  ? 717  PHE A CD1   1 
ATOM   4400 C CD2   . PHE A 1 717  ? 151.431 145.116 178.950 1.00 39.27  ? 717  PHE A CD2   1 
ATOM   4401 C CE1   . PHE A 1 717  ? 152.882 142.853 179.546 1.00 40.85  ? 717  PHE A CE1   1 
ATOM   4402 C CE2   . PHE A 1 717  ? 150.853 144.098 179.681 1.00 41.88  ? 717  PHE A CE2   1 
ATOM   4403 C CZ    . PHE A 1 717  ? 151.579 142.965 179.978 1.00 37.75  ? 717  PHE A CZ    1 
ATOM   4404 N N     . SER A 1 718  ? 151.199 146.820 175.501 1.00 35.95  ? 718  SER A N     1 
ATOM   4405 C CA    . SER A 1 718  ? 149.827 146.745 175.011 1.00 34.87  ? 718  SER A CA    1 
ATOM   4406 C C     . SER A 1 718  ? 149.762 146.451 173.518 1.00 37.60  ? 718  SER A C     1 
ATOM   4407 O O     . SER A 1 718  ? 148.838 145.765 173.068 1.00 42.81  ? 718  SER A O     1 
ATOM   4408 C CB    . SER A 1 718  ? 149.089 148.047 175.321 1.00 37.73  ? 718  SER A CB    1 
ATOM   4409 O OG    . SER A 1 718  ? 149.111 148.325 176.709 1.00 37.80  ? 718  SER A OG    1 
ATOM   4410 N N     . LEU A 1 719  ? 150.719 146.960 172.737 1.00 33.66  ? 719  LEU A N     1 
ATOM   4411 C CA    . LEU A 1 719  ? 150.695 146.728 171.296 1.00 33.94  ? 719  LEU A CA    1 
ATOM   4412 C C     . LEU A 1 719  ? 151.106 145.305 170.943 1.00 39.59  ? 719  LEU A C     1 
ATOM   4413 O O     . LEU A 1 719  ? 150.694 144.786 169.901 1.00 47.61  ? 719  LEU A O     1 
ATOM   4414 C CB    . LEU A 1 719  ? 151.601 147.733 170.584 1.00 29.90  ? 719  LEU A CB    1 
ATOM   4415 C CG    . LEU A 1 719  ? 151.089 149.173 170.516 1.00 32.58  ? 719  LEU A CG    1 
ATOM   4416 C CD1   . LEU A 1 719  ? 152.136 150.092 169.917 1.00 31.87  ? 719  LEU A CD1   1 
ATOM   4417 C CD2   . LEU A 1 719  ? 149.802 149.242 169.717 1.00 29.26  ? 719  LEU A CD2   1 
ATOM   4418 N N     . ALA A 1 720  ? 151.910 144.663 171.786 1.00 37.42  ? 720  ALA A N     1 
ATOM   4419 C CA    . ALA A 1 720  ? 152.393 143.315 171.526 1.00 37.65  ? 720  ALA A CA    1 
ATOM   4420 C C     . ALA A 1 720  ? 151.488 142.230 172.097 1.00 45.46  ? 720  ALA A C     1 
ATOM   4421 O O     . ALA A 1 720  ? 151.803 141.045 171.952 1.00 48.05  ? 720  ALA A O     1 
ATOM   4422 C CB    . ALA A 1 720  ? 153.808 143.150 172.086 1.00 33.27  ? 720  ALA A CB    1 
ATOM   4423 N N     . ARG A 1 721  ? 150.379 142.596 172.736 1.00 43.26  ? 721  ARG A N     1 
ATOM   4424 C CA    . ARG A 1 721  ? 149.489 141.625 173.358 1.00 44.58  ? 721  ARG A CA    1 
ATOM   4425 C C     . ARG A 1 721  ? 148.453 141.052 172.400 1.00 50.26  ? 721  ARG A C     1 
ATOM   4426 O O     . ARG A 1 721  ? 147.759 140.099 172.765 1.00 55.63  ? 721  ARG A O     1 
ATOM   4427 C CB    . ARG A 1 721  ? 148.777 142.252 174.559 1.00 48.00  ? 721  ARG A CB    1 
ATOM   4428 C CG    . ARG A 1 721  ? 149.565 142.169 175.854 1.00 53.12  ? 721  ARG A CG    1 
ATOM   4429 C CD    . ARG A 1 721  ? 148.879 142.938 176.967 1.00 53.51  ? 721  ARG A CD    1 
ATOM   4430 N NE    . ARG A 1 721  ? 147.613 142.332 177.359 1.00 55.87  ? 721  ARG A NE    1 
ATOM   4431 C CZ    . ARG A 1 721  ? 146.793 142.839 178.269 1.00 63.20  ? 721  ARG A CZ    1 
ATOM   4432 N NH1   . ARG A 1 721  ? 147.071 143.970 178.896 1.00 62.08  ? 721  ARG A NH1   1 
ATOM   4433 N NH2   . ARG A 1 721  ? 145.666 142.195 178.558 1.00 67.69  ? 721  ARG A NH2   1 
ATOM   4434 N N     . GLN A 1 722  ? 148.328 141.601 171.192 1.00 50.82  ? 722  GLN A N     1 
ATOM   4435 C CA    . GLN A 1 722  ? 147.390 141.075 170.216 1.00 51.65  ? 722  GLN A CA    1 
ATOM   4436 C C     . GLN A 1 722  ? 148.087 140.948 168.868 1.00 51.84  ? 722  GLN A C     1 
ATOM   4437 O O     . GLN A 1 722  ? 148.960 141.765 168.539 1.00 45.33  ? 722  GLN A O     1 
ATOM   4438 C CB    . GLN A 1 722  ? 146.144 141.962 170.074 1.00 48.78  ? 722  GLN A CB    1 
ATOM   4439 C CG    . GLN A 1 722  ? 146.413 143.354 169.528 1.00 45.80  ? 722  GLN A CG    1 
ATOM   4440 C CD    . GLN A 1 722  ? 146.904 144.314 170.588 1.00 48.14  ? 722  GLN A CD    1 
ATOM   4441 O OE1   . GLN A 1 722  ? 147.940 144.958 170.427 1.00 41.57  ? 722  GLN A OE1   1 
ATOM   4442 N NE2   . GLN A 1 722  ? 146.159 144.419 171.680 1.00 53.28  ? 722  GLN A NE2   1 
ATOM   4443 N N     . PRO A 1 723  ? 147.745 139.928 168.085 1.00 56.97  ? 723  PRO A N     1 
ATOM   4444 C CA    . PRO A 1 723  ? 148.340 139.795 166.753 1.00 49.97  ? 723  PRO A CA    1 
ATOM   4445 C C     . PRO A 1 723  ? 147.863 140.888 165.813 1.00 47.43  ? 723  PRO A C     1 
ATOM   4446 O O     . PRO A 1 723  ? 146.749 141.404 165.930 1.00 39.47  ? 723  PRO A O     1 
ATOM   4447 C CB    . PRO A 1 723  ? 147.862 138.415 166.284 1.00 48.89  ? 723  PRO A CB    1 
ATOM   4448 C CG    . PRO A 1 723  ? 147.463 137.698 167.535 1.00 55.74  ? 723  PRO A CG    1 
ATOM   4449 C CD    . PRO A 1 723  ? 146.928 138.758 168.442 1.00 57.86  ? 723  PRO A CD    1 
ATOM   4450 N N     . TRP A 1 724  ? 148.729 141.237 164.872 1.00 42.34  ? 724  TRP A N     1 
ATOM   4451 C CA    . TRP A 1 724  ? 148.424 142.191 163.818 1.00 32.87  ? 724  TRP A CA    1 
ATOM   4452 C C     . TRP A 1 724  ? 148.499 141.484 162.470 1.00 33.00  ? 724  TRP A C     1 
ATOM   4453 O O     . TRP A 1 724  ? 148.856 140.307 162.379 1.00 36.92  ? 724  TRP A O     1 
ATOM   4454 C CB    . TRP A 1 724  ? 149.382 143.382 163.864 1.00 29.10  ? 724  TRP A CB    1 
ATOM   4455 C CG    . TRP A 1 724  ? 149.404 144.086 165.179 1.00 32.82  ? 724  TRP A CG    1 
ATOM   4456 C CD1   . TRP A 1 724  ? 150.142 143.752 166.275 1.00 37.23  ? 724  TRP A CD1   1 
ATOM   4457 C CD2   . TRP A 1 724  ? 148.658 145.252 165.539 1.00 36.17  ? 724  TRP A CD2   1 
ATOM   4458 N NE1   . TRP A 1 724  ? 149.901 144.637 167.296 1.00 34.29  ? 724  TRP A NE1   1 
ATOM   4459 C CE2   . TRP A 1 724  ? 148.993 145.568 166.868 1.00 36.06  ? 724  TRP A CE2   1 
ATOM   4460 C CE3   . TRP A 1 724  ? 147.738 146.060 164.865 1.00 36.16  ? 724  TRP A CE3   1 
ATOM   4461 C CZ2   . TRP A 1 724  ? 148.440 146.656 167.537 1.00 37.68  ? 724  TRP A CZ2   1 
ATOM   4462 C CZ3   . TRP A 1 724  ? 147.192 147.138 165.530 1.00 36.26  ? 724  TRP A CZ3   1 
ATOM   4463 C CH2   . TRP A 1 724  ? 147.544 147.427 166.851 1.00 37.97  ? 724  TRP A CH2   1 
ATOM   4464 N N     . SER A 1 725  ? 148.152 142.214 161.413 1.00 27.66  ? 725  SER A N     1 
ATOM   4465 C CA    . SER A 1 725  ? 148.250 141.697 160.055 1.00 27.06  ? 725  SER A CA    1 
ATOM   4466 C C     . SER A 1 725  ? 149.422 142.306 159.299 1.00 26.93  ? 725  SER A C     1 
ATOM   4467 O O     . SER A 1 725  ? 150.291 141.580 158.810 1.00 34.72  ? 725  SER A O     1 
ATOM   4468 C CB    . SER A 1 725  ? 146.942 141.955 159.301 1.00 27.97  ? 725  SER A CB    1 
ATOM   4469 O OG    . SER A 1 725  ? 145.864 141.245 159.877 1.00 32.89  ? 725  SER A OG    1 
ATOM   4470 N N     . ILE A 1 726  ? 149.469 143.630 159.190 1.00 22.44  ? 726  ILE A N     1 
ATOM   4471 C CA    . ILE A 1 726  ? 150.544 144.331 158.501 1.00 18.80  ? 726  ILE A CA    1 
ATOM   4472 C C     . ILE A 1 726  ? 151.053 145.430 159.419 1.00 19.73  ? 726  ILE A C     1 
ATOM   4473 O O     . ILE A 1 726  ? 150.269 146.257 159.895 1.00 23.75  ? 726  ILE A O     1 
ATOM   4474 C CB    . ILE A 1 726  ? 150.076 144.918 157.155 1.00 20.51  ? 726  ILE A CB    1 
ATOM   4475 C CG1   . ILE A 1 726  ? 149.465 143.824 156.277 1.00 18.27  ? 726  ILE A CG1   1 
ATOM   4476 C CG2   . ILE A 1 726  ? 151.233 145.593 156.435 1.00 22.70  ? 726  ILE A CG2   1 
ATOM   4477 C CD1   . ILE A 1 726  ? 148.811 144.340 155.021 1.00 16.41  ? 726  ILE A CD1   1 
ATOM   4478 N N     . MET A 1 727  ? 152.357 145.434 159.673 1.00 21.88  ? 727  MET A N     1 
ATOM   4479 C CA    . MET A 1 727  ? 153.004 146.486 160.444 1.00 21.14  ? 727  MET A CA    1 
ATOM   4480 C C     . MET A 1 727  ? 153.888 147.289 159.503 1.00 22.06  ? 727  MET A C     1 
ATOM   4481 O O     . MET A 1 727  ? 154.770 146.729 158.845 1.00 25.13  ? 727  MET A O     1 
ATOM   4482 C CB    . MET A 1 727  ? 153.823 145.911 161.598 1.00 21.34  ? 727  MET A CB    1 
ATOM   4483 C CG    . MET A 1 727  ? 154.486 146.970 162.461 1.00 19.26  ? 727  MET A CG    1 
ATOM   4484 S SD    . MET A 1 727  ? 155.425 146.282 163.831 1.00 45.40  ? 727  MET A SD    1 
ATOM   4485 C CE    . MET A 1 727  ? 156.072 147.771 164.577 1.00 33.20  ? 727  MET A CE    1 
ATOM   4486 N N     . VAL A 1 728  ? 153.649 148.593 159.437 1.00 22.54  ? 728  VAL A N     1 
ATOM   4487 C CA    . VAL A 1 728  ? 154.372 149.487 158.542 1.00 23.46  ? 728  VAL A CA    1 
ATOM   4488 C C     . VAL A 1 728  ? 155.217 150.421 159.393 1.00 25.22  ? 728  VAL A C     1 
ATOM   4489 O O     . VAL A 1 728  ? 154.692 151.123 160.265 1.00 29.22  ? 728  VAL A O     1 
ATOM   4490 C CB    . VAL A 1 728  ? 153.412 150.272 157.635 1.00 25.62  ? 728  VAL A CB    1 
ATOM   4491 C CG1   . VAL A 1 728  ? 154.188 151.150 156.680 1.00 21.92  ? 728  VAL A CG1   1 
ATOM   4492 C CG2   . VAL A 1 728  ? 152.508 149.320 156.870 1.00 23.40  ? 728  VAL A CG2   1 
ATOM   4493 N N     . CYS A 1 729  ? 156.522 150.426 159.147 1.00 26.01  ? 729  CYS A N     1 
ATOM   4494 C CA    . CYS A 1 729  ? 157.458 151.308 159.837 1.00 28.75  ? 729  CYS A CA    1 
ATOM   4495 C C     . CYS A 1 729  ? 157.978 152.320 158.820 1.00 36.40  ? 729  CYS A C     1 
ATOM   4496 O O     . CYS A 1 729  ? 158.954 152.068 158.112 1.00 42.21  ? 729  CYS A O     1 
ATOM   4497 C CB    . CYS A 1 729  ? 158.596 150.518 160.481 1.00 28.80  ? 729  CYS A CB    1 
ATOM   4498 S SG    . CYS A 1 729  ? 158.178 149.767 162.071 1.00 35.34  ? 729  CYS A SG    1 
ATOM   4499 N N     . ASP A 1 730  ? 157.311 153.469 158.750 1.00 33.10  ? 730  ASP A N     1 
ATOM   4500 C CA    . ASP A 1 730  ? 157.738 154.528 157.848 1.00 33.72  ? 730  ASP A CA    1 
ATOM   4501 C C     . ASP A 1 730  ? 158.989 155.205 158.386 1.00 37.83  ? 730  ASP A C     1 
ATOM   4502 O O     . ASP A 1 730  ? 159.145 155.381 159.597 1.00 35.54  ? 730  ASP A O     1 
ATOM   4503 C CB    . ASP A 1 730  ? 156.620 155.548 157.668 1.00 38.65  ? 730  ASP A CB    1 
ATOM   4504 C CG    . ASP A 1 730  ? 155.332 154.909 157.219 1.00 48.36  ? 730  ASP A CG    1 
ATOM   4505 O OD1   . ASP A 1 730  ? 155.377 154.100 156.271 1.00 53.32  ? 730  ASP A OD1   1 
ATOM   4506 O OD2   . ASP A 1 730  ? 154.280 155.198 157.826 1.00 49.49  ? 730  ASP A OD2   1 
ATOM   4507 N N     . GLU A 1 731  ? 159.872 155.601 157.474 1.00 41.53  ? 731  GLU A N     1 
ATOM   4508 C CA    . GLU A 1 731  ? 161.213 156.060 157.821 1.00 39.43  ? 731  GLU A CA    1 
ATOM   4509 C C     . GLU A 1 731  ? 161.881 155.052 158.751 1.00 39.71  ? 731  GLU A C     1 
ATOM   4510 O O     . GLU A 1 731  ? 162.215 155.339 159.901 1.00 44.08  ? 731  GLU A O     1 
ATOM   4511 C CB    . GLU A 1 731  ? 161.182 157.459 158.437 1.00 42.44  ? 731  GLU A CB    1 
ATOM   4512 C CG    . GLU A 1 731  ? 160.612 158.514 157.513 1.00 49.65  ? 731  GLU A CG    1 
ATOM   4513 C CD    . GLU A 1 731  ? 161.261 158.508 156.143 1.00 59.72  ? 731  GLU A CD    1 
ATOM   4514 O OE1   . GLU A 1 731  ? 162.507 158.446 156.070 1.00 60.32  ? 731  GLU A OE1   1 
ATOM   4515 O OE2   . GLU A 1 731  ? 160.523 158.561 155.137 1.00 60.97  ? 731  GLU A OE2   1 
ATOM   4516 N N     . ALA A 1 732  ? 162.065 153.845 158.219 1.00 35.89  ? 732  ALA A N     1 
ATOM   4517 C CA    . ALA A 1 732  ? 162.542 152.712 159.001 1.00 35.39  ? 732  ALA A CA    1 
ATOM   4518 C C     . ALA A 1 732  ? 163.948 152.941 159.538 1.00 41.38  ? 732  ALA A C     1 
ATOM   4519 O O     . ALA A 1 732  ? 164.461 152.118 160.299 1.00 48.06  ? 732  ALA A O     1 
ATOM   4520 C CB    . ALA A 1 732  ? 162.496 151.434 158.163 1.00 42.06  ? 732  ALA A CB    1 
ATOM   4521 N N     . GLN A 1 733  ? 164.576 154.061 159.178 1.00 44.82  ? 733  GLN A N     1 
ATOM   4522 C CA    . GLN A 1 733  ? 165.868 154.385 159.764 1.00 44.58  ? 733  GLN A CA    1 
ATOM   4523 C C     . GLN A 1 733  ? 165.761 154.713 161.247 1.00 47.88  ? 733  GLN A C     1 
ATOM   4524 O O     . GLN A 1 733  ? 166.793 154.851 161.909 1.00 52.41  ? 733  GLN A O     1 
ATOM   4525 C CB    . GLN A 1 733  ? 166.520 155.552 159.020 1.00 45.45  ? 733  GLN A CB    1 
ATOM   4526 C CG    . GLN A 1 733  ? 165.823 156.888 159.200 1.00 49.48  ? 733  GLN A CG    1 
ATOM   4527 C CD    . GLN A 1 733  ? 164.895 157.222 158.053 1.00 50.10  ? 733  GLN A CD    1 
ATOM   4528 O OE1   . GLN A 1 733  ? 164.673 156.405 157.160 1.00 46.05  ? 733  GLN A OE1   1 
ATOM   4529 N NE2   . GLN A 1 733  ? 164.350 158.432 158.067 1.00 50.47  ? 733  GLN A NE2   1 
ATOM   4530 N N     . LYS A 1 734  ? 164.545 154.851 161.779 1.00 47.10  ? 734  LYS A N     1 
ATOM   4531 C CA    . LYS A 1 734  ? 164.370 154.997 163.217 1.00 47.74  ? 734  LYS A CA    1 
ATOM   4532 C C     . LYS A 1 734  ? 164.709 153.718 163.972 1.00 47.82  ? 734  LYS A C     1 
ATOM   4533 O O     . LYS A 1 734  ? 164.989 153.780 165.173 1.00 52.46  ? 734  LYS A O     1 
ATOM   4534 C CB    . LYS A 1 734  ? 162.936 155.421 163.532 1.00 48.77  ? 734  LYS A CB    1 
ATOM   4535 C CG    . LYS A 1 734  ? 162.509 156.715 162.860 1.00 46.09  ? 734  LYS A CG    1 
ATOM   4536 C CD    . LYS A 1 734  ? 163.410 157.868 163.266 1.00 53.32  ? 734  LYS A CD    1 
ATOM   4537 C CE    . LYS A 1 734  ? 163.018 159.154 162.558 1.00 56.85  ? 734  LYS A CE    1 
ATOM   4538 N NZ    . LYS A 1 734  ? 163.894 160.291 162.955 1.00 54.38  ? 734  LYS A NZ    1 
ATOM   4539 N N     . ILE A 1 735  ? 164.692 152.567 163.301 1.00 45.38  ? 735  ILE A N     1 
ATOM   4540 C CA    . ILE A 1 735  ? 165.036 151.300 163.937 1.00 43.53  ? 735  ILE A CA    1 
ATOM   4541 C C     . ILE A 1 735  ? 166.353 150.791 163.364 1.00 47.06  ? 735  ILE A C     1 
ATOM   4542 O O     . ILE A 1 735  ? 166.607 149.582 163.331 1.00 51.67  ? 735  ILE A O     1 
ATOM   4543 C CB    . ILE A 1 735  ? 163.911 150.259 163.770 1.00 36.52  ? 735  ILE A CB    1 
ATOM   4544 C CG1   . ILE A 1 735  ? 163.689 149.918 162.297 1.00 36.06  ? 735  ILE A CG1   1 
ATOM   4545 C CG2   . ILE A 1 735  ? 162.620 150.768 164.391 1.00 38.08  ? 735  ILE A CG2   1 
ATOM   4546 C CD1   . ILE A 1 735  ? 162.641 148.860 162.064 1.00 35.93  ? 735  ILE A CD1   1 
ATOM   4547 N N     . LYS A 1 736  ? 167.206 151.716 162.918 1.00 46.39  ? 736  LYS A N     1 
ATOM   4548 C CA    . LYS A 1 736  ? 168.519 151.349 162.399 1.00 43.51  ? 736  LYS A CA    1 
ATOM   4549 C C     . LYS A 1 736  ? 169.433 150.785 163.479 1.00 48.51  ? 736  LYS A C     1 
ATOM   4550 O O     . LYS A 1 736  ? 170.375 150.053 163.155 1.00 49.97  ? 736  LYS A O     1 
ATOM   4551 C CB    . LYS A 1 736  ? 169.182 152.563 161.746 1.00 41.62  ? 736  LYS A CB    1 
ATOM   4552 C CG    . LYS A 1 736  ? 169.573 153.652 162.733 1.00 49.07  ? 736  LYS A CG    1 
ATOM   4553 C CD    . LYS A 1 736  ? 169.993 154.932 162.030 1.00 49.06  ? 736  LYS A CD    1 
ATOM   4554 C CE    . LYS A 1 736  ? 171.310 154.762 161.300 1.00 53.26  ? 736  LYS A CE    1 
ATOM   4555 N NZ    . LYS A 1 736  ? 172.426 154.441 162.230 1.00 57.69  ? 736  LYS A NZ    1 
ATOM   4556 N N     . ASN A 1 737  ? 169.181 151.109 164.745 1.00 49.43  ? 737  ASN A N     1 
ATOM   4557 C CA    . ASN A 1 737  ? 170.009 150.634 165.845 1.00 44.75  ? 737  ASN A CA    1 
ATOM   4558 C C     . ASN A 1 737  ? 169.401 149.361 166.415 1.00 48.55  ? 737  ASN A C     1 
ATOM   4559 O O     . ASN A 1 737  ? 168.262 149.397 166.894 1.00 53.41  ? 737  ASN A O     1 
ATOM   4560 C CB    . ASN A 1 737  ? 170.111 151.696 166.927 1.00 43.48  ? 737  ASN A CB    1 
ATOM   4561 C CG    . ASN A 1 737  ? 171.215 151.415 167.926 1.00 53.30  ? 737  ASN A CG    1 
ATOM   4562 O OD1   . ASN A 1 737  ? 171.692 150.288 168.050 1.00 56.84  ? 737  ASN A OD1   1 
ATOM   4563 N ND2   . ASN A 1 737  ? 171.623 152.447 168.654 1.00 53.72  ? 737  ASN A ND2   1 
ATOM   4564 N N     . PRO A 1 738  ? 170.103 148.225 166.375 1.00 48.53  ? 738  PRO A N     1 
ATOM   4565 C CA    . PRO A 1 738  ? 169.509 146.982 166.895 1.00 48.96  ? 738  PRO A CA    1 
ATOM   4566 C C     . PRO A 1 738  ? 169.161 147.034 168.373 1.00 53.77  ? 738  PRO A C     1 
ATOM   4567 O O     . PRO A 1 738  ? 168.188 146.395 168.791 1.00 51.97  ? 738  PRO A O     1 
ATOM   4568 C CB    . PRO A 1 738  ? 170.593 145.931 166.613 1.00 49.11  ? 738  PRO A CB    1 
ATOM   4569 C CG    . PRO A 1 738  ? 171.439 146.522 165.544 1.00 50.46  ? 738  PRO A CG    1 
ATOM   4570 C CD    . PRO A 1 738  ? 171.432 147.997 165.784 1.00 54.71  ? 738  PRO A CD    1 
ATOM   4571 N N     . ALA A 1 739  ? 169.923 147.771 169.178 1.00 53.93  ? 739  ALA A N     1 
ATOM   4572 C CA    . ALA A 1 739  ? 169.734 147.784 170.622 1.00 52.53  ? 739  ALA A CA    1 
ATOM   4573 C C     . ALA A 1 739  ? 168.826 148.907 171.105 1.00 52.13  ? 739  ALA A C     1 
ATOM   4574 O O     . ALA A 1 739  ? 168.623 149.038 172.316 1.00 54.82  ? 739  ALA A O     1 
ATOM   4575 C CB    . ALA A 1 739  ? 171.086 147.885 171.330 1.00 57.96  ? 739  ALA A CB    1 
ATOM   4576 N N     . ALA A 1 740  ? 168.286 149.720 170.202 1.00 49.93  ? 740  ALA A N     1 
ATOM   4577 C CA    . ALA A 1 740  ? 167.398 150.797 170.610 1.00 44.24  ? 740  ALA A CA    1 
ATOM   4578 C C     . ALA A 1 740  ? 166.095 150.234 171.166 1.00 43.32  ? 740  ALA A C     1 
ATOM   4579 O O     . ALA A 1 740  ? 165.606 149.189 170.729 1.00 43.20  ? 740  ALA A O     1 
ATOM   4580 C CB    . ALA A 1 740  ? 167.109 151.726 169.433 1.00 42.37  ? 740  ALA A CB    1 
ATOM   4581 N N     . LEU A 1 741  ? 165.534 150.940 172.151 1.00 40.63  ? 741  LEU A N     1 
ATOM   4582 C CA    . LEU A 1 741  ? 164.267 150.513 172.733 1.00 41.30  ? 741  LEU A CA    1 
ATOM   4583 C C     . LEU A 1 741  ? 163.136 150.581 171.717 1.00 42.08  ? 741  LEU A C     1 
ATOM   4584 O O     . LEU A 1 741  ? 162.214 149.758 171.760 1.00 42.77  ? 741  LEU A O     1 
ATOM   4585 C CB    . LEU A 1 741  ? 163.934 151.363 173.959 1.00 43.62  ? 741  LEU A CB    1 
ATOM   4586 C CG    . LEU A 1 741  ? 165.002 151.428 175.052 1.00 48.17  ? 741  LEU A CG    1 
ATOM   4587 C CD1   . LEU A 1 741  ? 164.481 152.163 176.274 1.00 42.83  ? 741  LEU A CD1   1 
ATOM   4588 C CD2   . LEU A 1 741  ? 165.488 150.038 175.424 1.00 44.78  ? 741  LEU A CD2   1 
ATOM   4589 N N     . ILE A 1 742  ? 163.189 151.548 170.800 1.00 42.63  ? 742  ILE A N     1 
ATOM   4590 C CA    . ILE A 1 742  ? 162.196 151.617 169.734 1.00 38.20  ? 742  ILE A CA    1 
ATOM   4591 C C     . ILE A 1 742  ? 162.317 150.408 168.815 1.00 37.88  ? 742  ILE A C     1 
ATOM   4592 O O     . ILE A 1 742  ? 161.309 149.830 168.391 1.00 40.91  ? 742  ILE A O     1 
ATOM   4593 C CB    . ILE A 1 742  ? 162.341 152.941 168.963 1.00 38.91  ? 742  ILE A CB    1 
ATOM   4594 C CG1   . ILE A 1 742  ? 161.993 154.119 169.873 1.00 37.63  ? 742  ILE A CG1   1 
ATOM   4595 C CG2   . ILE A 1 742  ? 161.463 152.942 167.727 1.00 41.19  ? 742  ILE A CG2   1 
ATOM   4596 C CD1   . ILE A 1 742  ? 162.063 155.462 169.188 1.00 39.38  ? 742  ILE A CD1   1 
ATOM   4597 N N     . THR A 1 743  ? 163.549 150.003 168.495 1.00 35.68  ? 743  THR A N     1 
ATOM   4598 C CA    . THR A 1 743  ? 163.751 148.813 167.674 1.00 36.05  ? 743  THR A CA    1 
ATOM   4599 C C     . THR A 1 743  ? 163.255 147.559 168.385 1.00 38.18  ? 743  THR A C     1 
ATOM   4600 O O     . THR A 1 743  ? 162.653 146.677 167.760 1.00 37.31  ? 743  THR A O     1 
ATOM   4601 C CB    . THR A 1 743  ? 165.229 148.669 167.316 1.00 37.69  ? 743  THR A CB    1 
ATOM   4602 O OG1   . THR A 1 743  ? 165.728 149.917 166.824 1.00 41.29  ? 743  THR A OG1   1 
ATOM   4603 C CG2   . THR A 1 743  ? 165.419 147.604 166.252 1.00 38.58  ? 743  THR A CG2   1 
ATOM   4604 N N     . HIS A 1 744  ? 163.512 147.457 169.691 1.00 38.69  ? 744  HIS A N     1 
ATOM   4605 C CA    . HIS A 1 744  ? 163.019 146.317 170.455 1.00 33.69  ? 744  HIS A CA    1 
ATOM   4606 C C     . HIS A 1 744  ? 161.498 146.286 170.475 1.00 39.76  ? 744  HIS A C     1 
ATOM   4607 O O     . HIS A 1 744  ? 160.891 145.216 170.368 1.00 42.25  ? 744  HIS A O     1 
ATOM   4608 C CB    . HIS A 1 744  ? 163.571 146.357 171.879 1.00 42.14  ? 744  HIS A CB    1 
ATOM   4609 C CG    . HIS A 1 744  ? 165.044 146.110 171.965 1.00 48.07  ? 744  HIS A CG    1 
ATOM   4610 N ND1   . HIS A 1 744  ? 165.769 146.332 173.116 1.00 49.29  ? 744  HIS A ND1   1 
ATOM   4611 C CD2   . HIS A 1 744  ? 165.928 145.655 171.046 1.00 49.25  ? 744  HIS A CD2   1 
ATOM   4612 C CE1   . HIS A 1 744  ? 167.036 146.028 172.901 1.00 51.67  ? 744  HIS A CE1   1 
ATOM   4613 N NE2   . HIS A 1 744  ? 167.159 145.615 171.653 1.00 55.54  ? 744  HIS A NE2   1 
ATOM   4614 N N     . ALA A 1 745  ? 160.865 147.452 170.623 1.00 44.46  ? 745  ALA A N     1 
ATOM   4615 C CA    . ALA A 1 745  ? 159.408 147.513 170.588 1.00 36.15  ? 745  ALA A CA    1 
ATOM   4616 C C     . ALA A 1 745  ? 158.869 147.120 169.219 1.00 37.65  ? 745  ALA A C     1 
ATOM   4617 O O     . ALA A 1 745  ? 157.855 146.420 169.123 1.00 42.36  ? 745  ALA A O     1 
ATOM   4618 C CB    . ALA A 1 745  ? 158.935 148.914 170.969 1.00 35.92  ? 745  ALA A CB    1 
ATOM   4619 N N     . ALA A 1 746  ? 159.529 147.570 168.150 1.00 36.30  ? 746  ALA A N     1 
ATOM   4620 C CA    . ALA A 1 746  ? 159.086 147.234 166.801 1.00 33.09  ? 746  ALA A CA    1 
ATOM   4621 C C     . ALA A 1 746  ? 159.220 145.743 166.524 1.00 34.58  ? 746  ALA A C     1 
ATOM   4622 O O     . ALA A 1 746  ? 158.353 145.145 165.877 1.00 34.17  ? 746  ALA A O     1 
ATOM   4623 C CB    . ALA A 1 746  ? 159.875 148.045 165.775 1.00 30.18  ? 746  ALA A CB    1 
ATOM   4624 N N     . ASN A 1 747  ? 160.306 145.125 166.994 1.00 36.16  ? 747  ASN A N     1 
ATOM   4625 C CA    . ASN A 1 747  ? 160.476 143.689 166.801 1.00 32.38  ? 747  ASN A CA    1 
ATOM   4626 C C     . ASN A 1 747  ? 159.574 142.885 167.729 1.00 35.37  ? 747  ASN A C     1 
ATOM   4627 O O     . ASN A 1 747  ? 159.242 141.734 167.423 1.00 38.73  ? 747  ASN A O     1 
ATOM   4628 C CB    . ASN A 1 747  ? 161.937 143.297 167.012 1.00 31.60  ? 747  ASN A CB    1 
ATOM   4629 C CG    . ASN A 1 747  ? 162.864 143.937 166.001 1.00 28.21  ? 747  ASN A CG    1 
ATOM   4630 O OD1   . ASN A 1 747  ? 162.485 144.177 164.857 1.00 33.75  ? 747  ASN A OD1   1 
ATOM   4631 N ND2   . ASN A 1 747  ? 164.092 144.212 166.418 1.00 37.95  ? 747  ASN A ND2   1 
ATOM   4632 N N     . ALA A 1 748  ? 159.173 143.467 168.861 1.00 38.54  ? 748  ALA A N     1 
ATOM   4633 C CA    . ALA A 1 748  ? 158.300 142.766 169.797 1.00 37.20  ? 748  ALA A CA    1 
ATOM   4634 C C     . ALA A 1 748  ? 156.893 142.603 169.244 1.00 36.89  ? 748  ALA A C     1 
ATOM   4635 O O     . ALA A 1 748  ? 156.213 141.624 169.566 1.00 39.99  ? 748  ALA A O     1 
ATOM   4636 C CB    . ALA A 1 748  ? 158.256 143.510 171.131 1.00 37.16  ? 748  ALA A CB    1 
ATOM   4637 N N     . VAL A 1 749  ? 156.440 143.551 168.424 1.00 33.73  ? 749  VAL A N     1 
ATOM   4638 C CA    . VAL A 1 749  ? 155.110 143.467 167.836 1.00 30.55  ? 749  VAL A CA    1 
ATOM   4639 C C     . VAL A 1 749  ? 155.066 142.302 166.859 1.00 35.26  ? 749  VAL A C     1 
ATOM   4640 O O     . VAL A 1 749  ? 155.930 142.173 165.984 1.00 40.44  ? 749  VAL A O     1 
ATOM   4641 C CB    . VAL A 1 749  ? 154.747 144.790 167.148 1.00 31.50  ? 749  VAL A CB    1 
ATOM   4642 C CG1   . VAL A 1 749  ? 153.389 144.689 166.485 1.00 32.95  ? 749  VAL A CG1   1 
ATOM   4643 C CG2   . VAL A 1 749  ? 154.772 145.930 168.151 1.00 33.63  ? 749  VAL A CG2   1 
ATOM   4644 N N     . GLN A 1 750  ? 154.064 141.444 167.008 1.00 38.47  ? 750  GLN A N     1 
ATOM   4645 C CA    . GLN A 1 750  ? 153.923 140.250 166.183 1.00 37.50  ? 750  GLN A CA    1 
ATOM   4646 C C     . GLN A 1 750  ? 152.921 140.539 165.072 1.00 37.32  ? 750  GLN A C     1 
ATOM   4647 O O     . GLN A 1 750  ? 151.716 140.636 165.322 1.00 38.84  ? 750  GLN A O     1 
ATOM   4648 C CB    . GLN A 1 750  ? 153.488 139.055 167.028 1.00 42.77  ? 750  GLN A CB    1 
ATOM   4649 C CG    . GLN A 1 750  ? 154.534 138.607 168.035 1.00 50.09  ? 750  GLN A CG    1 
ATOM   4650 C CD    . GLN A 1 750  ? 155.813 138.136 167.372 1.00 57.51  ? 750  GLN A CD    1 
ATOM   4651 O OE1   . GLN A 1 750  ? 156.841 138.811 167.429 1.00 54.71  ? 750  GLN A OE1   1 
ATOM   4652 N NE2   . GLN A 1 750  ? 155.756 136.971 166.739 1.00 61.11  ? 750  GLN A NE2   1 
ATOM   4653 N N     . ALA A 1 751  ? 153.424 140.671 163.847 1.00 39.66  ? 751  ALA A N     1 
ATOM   4654 C CA    . ALA A 1 751  ? 152.606 140.965 162.682 1.00 29.49  ? 751  ALA A CA    1 
ATOM   4655 C C     . ALA A 1 751  ? 152.879 139.935 161.598 1.00 32.06  ? 751  ALA A C     1 
ATOM   4656 O O     . ALA A 1 751  ? 153.997 139.429 161.470 1.00 41.78  ? 751  ALA A O     1 
ATOM   4657 C CB    . ALA A 1 751  ? 152.882 142.373 162.146 1.00 25.31  ? 751  ALA A CB    1 
ATOM   4658 N N     . ARG A 1 752  ? 151.841 139.627 160.818 1.00 27.98  ? 752  ARG A N     1 
ATOM   4659 C CA    . ARG A 1 752  ? 151.991 138.670 159.725 1.00 26.63  ? 752  ARG A CA    1 
ATOM   4660 C C     . ARG A 1 752  ? 152.983 139.176 158.685 1.00 30.60  ? 752  ARG A C     1 
ATOM   4661 O O     . ARG A 1 752  ? 153.843 138.425 158.211 1.00 37.99  ? 752  ARG A O     1 
ATOM   4662 C CB    . ARG A 1 752  ? 150.630 138.395 159.086 1.00 26.73  ? 752  ARG A CB    1 
ATOM   4663 C CG    . ARG A 1 752  ? 150.690 137.590 157.802 1.00 29.63  ? 752  ARG A CG    1 
ATOM   4664 C CD    . ARG A 1 752  ? 149.302 137.386 157.228 1.00 31.58  ? 752  ARG A CD    1 
ATOM   4665 N NE    . ARG A 1 752  ? 149.332 136.736 155.924 1.00 41.38  ? 752  ARG A NE    1 
ATOM   4666 C CZ    . ARG A 1 752  ? 148.252 136.428 155.218 1.00 43.71  ? 752  ARG A CZ    1 
ATOM   4667 N NH1   . ARG A 1 752  ? 147.036 136.694 155.664 1.00 40.00  ? 752  ARG A NH1   1 
ATOM   4668 N NH2   . ARG A 1 752  ? 148.397 135.835 154.036 1.00 39.19  ? 752  ARG A NH2   1 
ATOM   4669 N N     . PHE A 1 753  ? 152.882 140.452 158.324 1.00 26.15  ? 753  PHE A N     1 
ATOM   4670 C CA    . PHE A 1 753  ? 153.759 141.071 157.343 1.00 22.61  ? 753  PHE A CA    1 
ATOM   4671 C C     . PHE A 1 753  ? 154.266 142.390 157.903 1.00 23.04  ? 753  PHE A C     1 
ATOM   4672 O O     . PHE A 1 753  ? 153.500 143.154 158.495 1.00 24.61  ? 753  PHE A O     1 
ATOM   4673 C CB    . PHE A 1 753  ? 153.020 141.297 156.020 1.00 24.92  ? 753  PHE A CB    1 
ATOM   4674 C CG    . PHE A 1 753  ? 153.924 141.516 154.841 1.00 32.13  ? 753  PHE A CG    1 
ATOM   4675 C CD1   . PHE A 1 753  ? 154.657 140.471 154.309 1.00 29.82  ? 753  PHE A CD1   1 
ATOM   4676 C CD2   . PHE A 1 753  ? 154.025 142.763 154.253 1.00 29.21  ? 753  PHE A CD2   1 
ATOM   4677 C CE1   . PHE A 1 753  ? 155.483 140.668 153.224 1.00 28.08  ? 753  PHE A CE1   1 
ATOM   4678 C CE2   . PHE A 1 753  ? 154.849 142.965 153.168 1.00 26.02  ? 753  PHE A CE2   1 
ATOM   4679 C CZ    . PHE A 1 753  ? 155.578 141.917 152.653 1.00 29.06  ? 753  PHE A CZ    1 
ATOM   4680 N N     . LYS A 1 754  ? 155.556 142.655 157.724 1.00 24.68  ? 754  LYS A N     1 
ATOM   4681 C CA    . LYS A 1 754  ? 156.180 143.871 158.235 1.00 25.35  ? 754  LYS A CA    1 
ATOM   4682 C C     . LYS A 1 754  ? 156.868 144.595 157.089 1.00 28.22  ? 754  LYS A C     1 
ATOM   4683 O O     . LYS A 1 754  ? 157.811 144.069 156.494 1.00 29.91  ? 754  LYS A O     1 
ATOM   4684 C CB    . LYS A 1 754  ? 157.172 143.555 159.353 1.00 25.91  ? 754  LYS A CB    1 
ATOM   4685 C CG    . LYS A 1 754  ? 156.511 143.107 160.636 1.00 29.50  ? 754  LYS A CG    1 
ATOM   4686 C CD    . LYS A 1 754  ? 157.517 142.983 161.753 1.00 32.95  ? 754  LYS A CD    1 
ATOM   4687 C CE    . LYS A 1 754  ? 156.829 142.794 163.084 1.00 30.04  ? 754  LYS A CE    1 
ATOM   4688 N NZ    . LYS A 1 754  ? 157.801 142.774 164.209 1.00 29.55  ? 754  LYS A NZ    1 
ATOM   4689 N N     . VAL A 1 755  ? 156.407 145.804 156.791 1.00 28.78  ? 755  VAL A N     1 
ATOM   4690 C CA    . VAL A 1 755  ? 156.953 146.610 155.709 1.00 27.96  ? 755  VAL A CA    1 
ATOM   4691 C C     . VAL A 1 755  ? 157.867 147.663 156.316 1.00 30.81  ? 755  VAL A C     1 
ATOM   4692 O O     . VAL A 1 755  ? 157.431 148.473 157.142 1.00 35.41  ? 755  VAL A O     1 
ATOM   4693 C CB    . VAL A 1 755  ? 155.838 147.260 154.874 1.00 23.44  ? 755  VAL A CB    1 
ATOM   4694 C CG1   . VAL A 1 755  ? 156.410 147.858 153.602 1.00 28.09  ? 755  VAL A CG1   1 
ATOM   4695 C CG2   . VAL A 1 755  ? 154.755 146.247 154.556 1.00 25.82  ? 755  VAL A CG2   1 
ATOM   4696 N N     . ALA A 1 756  ? 159.133 147.651 155.914 1.00 28.98  ? 756  ALA A N     1 
ATOM   4697 C CA    . ALA A 1 756  ? 160.078 148.688 156.301 1.00 32.50  ? 756  ALA A CA    1 
ATOM   4698 C C     . ALA A 1 756  ? 160.191 149.685 155.156 1.00 36.53  ? 756  ALA A C     1 
ATOM   4699 O O     . ALA A 1 756  ? 160.623 149.327 154.056 1.00 37.62  ? 756  ALA A O     1 
ATOM   4700 C CB    . ALA A 1 756  ? 161.442 148.091 156.639 1.00 33.72  ? 756  ALA A CB    1 
ATOM   4701 N N     . CYS A 1 757  ? 159.797 150.929 155.410 1.00 37.95  ? 757  CYS A N     1 
ATOM   4702 C CA    . CYS A 1 757  ? 159.703 151.953 154.376 1.00 34.64  ? 757  CYS A CA    1 
ATOM   4703 C C     . CYS A 1 757  ? 160.696 153.061 154.690 1.00 35.87  ? 757  CYS A C     1 
ATOM   4704 O O     . CYS A 1 757  ? 160.498 153.827 155.637 1.00 40.98  ? 757  CYS A O     1 
ATOM   4705 C CB    . CYS A 1 757  ? 158.282 152.500 154.287 1.00 35.84  ? 757  CYS A CB    1 
ATOM   4706 S SG    . CYS A 1 757  ? 157.031 151.252 154.607 1.00 50.50  ? 757  CYS A SG    1 
ATOM   4707 N N     . THR A 1 758  ? 161.759 153.143 153.895 1.00 38.07  ? 758  THR A N     1 
ATOM   4708 C CA    . THR A 1 758  ? 162.728 154.219 154.024 1.00 40.98  ? 758  THR A CA    1 
ATOM   4709 C C     . THR A 1 758  ? 163.474 154.361 152.707 1.00 43.86  ? 758  THR A C     1 
ATOM   4710 O O     . THR A 1 758  ? 163.840 153.361 152.086 1.00 46.16  ? 758  THR A O     1 
ATOM   4711 C CB    . THR A 1 758  ? 163.712 153.965 155.175 1.00 41.72  ? 758  THR A CB    1 
ATOM   4712 O OG1   . THR A 1 758  ? 164.750 154.950 155.148 1.00 43.99  ? 758  THR A OG1   1 
ATOM   4713 C CG2   . THR A 1 758  ? 164.325 152.576 155.072 1.00 36.30  ? 758  THR A CG2   1 
ATOM   4714 N N     . GLY A 1 759  ? 163.681 155.604 152.281 1.00 48.51  ? 759  GLY A N     1 
ATOM   4715 C CA    . GLY A 1 759  ? 164.462 155.850 151.086 1.00 48.80  ? 759  GLY A CA    1 
ATOM   4716 C C     . GLY A 1 759  ? 165.953 155.694 151.261 1.00 53.43  ? 759  GLY A C     1 
ATOM   4717 O O     . GLY A 1 759  ? 166.676 155.596 150.265 1.00 58.27  ? 759  GLY A O     1 
ATOM   4718 N N     . THR A 1 760  ? 166.430 155.668 152.504 1.00 48.73  ? 760  THR A N     1 
ATOM   4719 C CA    . THR A 1 760  ? 167.847 155.492 152.819 1.00 49.61  ? 760  THR A CA    1 
ATOM   4720 C C     . THR A 1 760  ? 167.974 154.349 153.815 1.00 51.65  ? 760  THR A C     1 
ATOM   4721 O O     . THR A 1 760  ? 168.118 154.578 155.024 1.00 53.23  ? 760  THR A O     1 
ATOM   4722 C CB    . THR A 1 760  ? 168.459 156.776 153.382 1.00 52.07  ? 760  THR A CB    1 
ATOM   4723 O OG1   . THR A 1 760  ? 167.772 157.146 154.584 1.00 50.46  ? 760  THR A OG1   1 
ATOM   4724 C CG2   . THR A 1 760  ? 168.356 157.909 152.372 1.00 51.33  ? 760  THR A CG2   1 
ATOM   4725 N N     . PRO A 1 761  ? 167.909 153.101 153.344 1.00 52.56  ? 761  PRO A N     1 
ATOM   4726 C CA    . PRO A 1 761  ? 168.054 151.965 154.269 1.00 49.66  ? 761  PRO A CA    1 
ATOM   4727 C C     . PRO A 1 761  ? 169.373 151.964 155.016 1.00 51.32  ? 761  PRO A C     1 
ATOM   4728 O O     . PRO A 1 761  ? 169.415 151.552 156.182 1.00 55.63  ? 761  PRO A O     1 
ATOM   4729 C CB    . PRO A 1 761  ? 167.928 150.745 153.346 1.00 52.99  ? 761  PRO A CB    1 
ATOM   4730 C CG    . PRO A 1 761  ? 167.186 151.242 152.158 1.00 50.80  ? 761  PRO A CG    1 
ATOM   4731 C CD    . PRO A 1 761  ? 167.628 152.660 151.969 1.00 48.68  ? 761  PRO A CD    1 
ATOM   4732 N N     . VAL A 1 762  ? 170.451 152.415 154.383 1.00 56.06  ? 762  VAL A N     1 
ATOM   4733 C CA    . VAL A 1 762  ? 171.771 152.479 154.997 1.00 54.24  ? 762  VAL A CA    1 
ATOM   4734 C C     . VAL A 1 762  ? 172.146 153.946 155.148 1.00 58.43  ? 762  VAL A C     1 
ATOM   4735 O O     . VAL A 1 762  ? 172.230 154.678 154.155 1.00 61.52  ? 762  VAL A O     1 
ATOM   4736 C CB    . VAL A 1 762  ? 172.818 151.724 154.166 1.00 52.02  ? 762  VAL A CB    1 
ATOM   4737 C CG1   . VAL A 1 762  ? 174.199 151.896 154.772 1.00 51.53  ? 762  VAL A CG1   1 
ATOM   4738 C CG2   . VAL A 1 762  ? 172.452 150.253 154.066 1.00 51.09  ? 762  VAL A CG2   1 
ATOM   4739 N N     . GLU A 1 763  ? 172.370 154.375 156.388 1.00 57.10  ? 763  GLU A N     1 
ATOM   4740 C CA    . GLU A 1 763  ? 172.758 155.746 156.688 1.00 57.45  ? 763  GLU A CA    1 
ATOM   4741 C C     . GLU A 1 763  ? 174.208 155.867 157.130 1.00 63.19  ? 763  GLU A C     1 
ATOM   4742 O O     . GLU A 1 763  ? 174.916 156.774 156.683 1.00 69.27  ? 763  GLU A O     1 
ATOM   4743 C CB    . GLU A 1 763  ? 171.838 156.334 157.768 1.00 56.80  ? 763  GLU A CB    1 
ATOM   4744 C CG    . GLU A 1 763  ? 170.452 156.699 157.268 1.00 62.01  ? 763  GLU A CG    1 
ATOM   4745 C CD    . GLU A 1 763  ? 169.656 157.489 158.287 1.00 62.30  ? 763  GLU A CD    1 
ATOM   4746 O OE1   . GLU A 1 763  ? 169.898 157.312 159.499 1.00 62.90  ? 763  GLU A OE1   1 
ATOM   4747 O OE2   . GLU A 1 763  ? 168.795 158.295 157.877 1.00 61.57  ? 763  GLU A OE2   1 
ATOM   4748 N N     . ASN A 1 764  ? 174.670 154.979 158.006 1.00 58.64  ? 764  ASN A N     1 
ATOM   4749 C CA    . ASN A 1 764  ? 176.053 154.993 158.465 1.00 56.78  ? 764  ASN A CA    1 
ATOM   4750 C C     . ASN A 1 764  ? 176.797 153.716 158.113 1.00 58.43  ? 764  ASN A C     1 
ATOM   4751 O O     . ASN A 1 764  ? 177.896 153.780 157.550 1.00 62.98  ? 764  ASN A O     1 
ATOM   4752 C CB    . ASN A 1 764  ? 176.101 155.226 159.984 1.00 60.21  ? 764  ASN A CB    1 
ATOM   4753 C CG    . ASN A 1 764  ? 175.424 156.518 160.399 1.00 68.91  ? 764  ASN A CG    1 
ATOM   4754 O OD1   . ASN A 1 764  ? 174.232 156.538 160.702 1.00 67.72  ? 764  ASN A OD1   1 
ATOM   4755 N ND2   . ASN A 1 764  ? 176.185 157.606 160.414 1.00 73.25  ? 764  ASN A ND2   1 
ATOM   4756 N N     . THR A 1 765  ? 176.228 152.554 158.425 1.00 58.05  ? 765  THR A N     1 
ATOM   4757 C CA    . THR A 1 765  ? 176.858 151.271 158.151 1.00 55.61  ? 765  THR A CA    1 
ATOM   4758 C C     . THR A 1 765  ? 175.798 150.293 157.665 1.00 51.35  ? 765  THR A C     1 
ATOM   4759 O O     . THR A 1 765  ? 174.598 150.574 157.702 1.00 50.49  ? 765  THR A O     1 
ATOM   4760 C CB    . THR A 1 765  ? 177.570 150.707 159.390 1.00 57.90  ? 765  THR A CB    1 
ATOM   4761 O OG1   . THR A 1 765  ? 176.679 150.734 160.512 1.00 55.72  ? 765  THR A OG1   1 
ATOM   4762 C CG2   . THR A 1 765  ? 178.817 151.516 159.716 1.00 62.26  ? 765  THR A CG2   1 
ATOM   4763 N N     . LEU A 1 766  ? 176.255 149.127 157.205 1.00 50.52  ? 766  LEU A N     1 
ATOM   4764 C CA    . LEU A 1 766  ? 175.339 148.074 156.787 1.00 44.00  ? 766  LEU A CA    1 
ATOM   4765 C C     . LEU A 1 766  ? 174.602 147.440 157.958 1.00 44.93  ? 766  LEU A C     1 
ATOM   4766 O O     . LEU A 1 766  ? 173.662 146.669 157.734 1.00 49.80  ? 766  LEU A O     1 
ATOM   4767 C CB    . LEU A 1 766  ? 176.092 146.999 156.003 1.00 45.26  ? 766  LEU A CB    1 
ATOM   4768 C CG    . LEU A 1 766  ? 176.660 147.429 154.650 1.00 43.52  ? 766  LEU A CG    1 
ATOM   4769 C CD1   . LEU A 1 766  ? 177.291 146.249 153.933 1.00 53.22  ? 766  LEU A CD1   1 
ATOM   4770 C CD2   . LEU A 1 766  ? 175.578 148.060 153.791 1.00 41.68  ? 766  LEU A CD2   1 
ATOM   4771 N N     . VAL A 1 767  ? 175.006 147.739 159.195 1.00 43.98  ? 767  VAL A N     1 
ATOM   4772 C CA    . VAL A 1 767  ? 174.252 147.276 160.355 1.00 45.24  ? 767  VAL A CA    1 
ATOM   4773 C C     . VAL A 1 767  ? 172.852 147.871 160.346 1.00 46.91  ? 767  VAL A C     1 
ATOM   4774 O O     . VAL A 1 767  ? 171.908 147.266 160.867 1.00 48.36  ? 767  VAL A O     1 
ATOM   4775 C CB    . VAL A 1 767  ? 175.010 147.617 161.654 1.00 48.04  ? 767  VAL A CB    1 
ATOM   4776 C CG1   . VAL A 1 767  ? 174.375 146.916 162.844 1.00 51.95  ? 767  VAL A CG1   1 
ATOM   4777 C CG2   . VAL A 1 767  ? 176.476 147.236 161.525 1.00 49.61  ? 767  VAL A CG2   1 
ATOM   4778 N N     . ASP A 1 768  ? 172.687 149.051 159.745 1.00 48.94  ? 768  ASP A N     1 
ATOM   4779 C CA    . ASP A 1 768  ? 171.352 149.612 159.560 1.00 45.95  ? 768  ASP A CA    1 
ATOM   4780 C C     . ASP A 1 768  ? 170.496 148.698 158.693 1.00 41.48  ? 768  ASP A C     1 
ATOM   4781 O O     . ASP A 1 768  ? 169.343 148.400 159.029 1.00 45.18  ? 768  ASP A O     1 
ATOM   4782 C CB    . ASP A 1 768  ? 171.453 151.003 158.935 1.00 45.58  ? 768  ASP A CB    1 
ATOM   4783 C CG    . ASP A 1 768  ? 172.503 151.870 159.602 1.00 50.88  ? 768  ASP A CG    1 
ATOM   4784 O OD1   . ASP A 1 768  ? 173.048 151.455 160.645 1.00 53.93  ? 768  ASP A OD1   1 
ATOM   4785 O OD2   . ASP A 1 768  ? 172.787 152.965 159.077 1.00 54.33  ? 768  ASP A OD2   1 
ATOM   4786 N N     . LEU A 1 769  ? 171.052 148.235 157.570 1.00 38.62  ? 769  LEU A N     1 
ATOM   4787 C CA    . LEU A 1 769  ? 170.330 147.302 156.711 1.00 42.15  ? 769  LEU A CA    1 
ATOM   4788 C C     . LEU A 1 769  ? 170.050 145.996 157.438 1.00 42.93  ? 769  LEU A C     1 
ATOM   4789 O O     . LEU A 1 769  ? 168.976 145.401 157.276 1.00 46.64  ? 769  LEU A O     1 
ATOM   4790 C CB    . LEU A 1 769  ? 171.125 147.034 155.435 1.00 46.16  ? 769  LEU A CB    1 
ATOM   4791 C CG    . LEU A 1 769  ? 170.526 145.971 154.511 1.00 40.06  ? 769  LEU A CG    1 
ATOM   4792 C CD1   . LEU A 1 769  ? 169.364 146.542 153.717 1.00 45.98  ? 769  LEU A CD1   1 
ATOM   4793 C CD2   . LEU A 1 769  ? 171.581 145.385 153.592 1.00 39.48  ? 769  LEU A CD2   1 
ATOM   4794 N N     . TRP A 1 770  ? 171.014 145.525 158.232 1.00 37.96  ? 770  TRP A N     1 
ATOM   4795 C CA    . TRP A 1 770  ? 170.794 144.306 159.000 1.00 34.36  ? 770  TRP A CA    1 
ATOM   4796 C C     . TRP A 1 770  ? 169.627 144.471 159.963 1.00 36.21  ? 770  TRP A C     1 
ATOM   4797 O O     . TRP A 1 770  ? 168.791 143.572 160.092 1.00 37.07  ? 770  TRP A O     1 
ATOM   4798 C CB    . TRP A 1 770  ? 172.059 143.913 159.760 1.00 35.32  ? 770  TRP A CB    1 
ATOM   4799 C CG    . TRP A 1 770  ? 171.891 142.628 160.497 1.00 37.69  ? 770  TRP A CG    1 
ATOM   4800 C CD1   . TRP A 1 770  ? 172.154 141.376 160.028 1.00 38.02  ? 770  TRP A CD1   1 
ATOM   4801 C CD2   . TRP A 1 770  ? 171.391 142.461 161.829 1.00 38.84  ? 770  TRP A CD2   1 
ATOM   4802 N NE1   . TRP A 1 770  ? 171.859 140.440 160.987 1.00 39.06  ? 770  TRP A NE1   1 
ATOM   4803 C CE2   . TRP A 1 770  ? 171.388 141.081 162.102 1.00 39.33  ? 770  TRP A CE2   1 
ATOM   4804 C CE3   . TRP A 1 770  ? 170.949 143.345 162.818 1.00 37.79  ? 770  TRP A CE3   1 
ATOM   4805 C CZ2   . TRP A 1 770  ? 170.963 140.564 163.321 1.00 37.66  ? 770  TRP A CZ2   1 
ATOM   4806 C CZ3   . TRP A 1 770  ? 170.528 142.830 164.025 1.00 34.29  ? 770  TRP A CZ3   1 
ATOM   4807 C CH2   . TRP A 1 770  ? 170.538 141.453 164.268 1.00 33.93  ? 770  TRP A CH2   1 
ATOM   4808 N N     . SER A 1 771  ? 169.553 145.614 160.647 1.00 40.18  ? 771  SER A N     1 
ATOM   4809 C CA    . SER A 1 771  ? 168.440 145.874 161.555 1.00 35.69  ? 771  SER A CA    1 
ATOM   4810 C C     . SER A 1 771  ? 167.118 145.924 160.800 1.00 35.14  ? 771  SER A C     1 
ATOM   4811 O O     . SER A 1 771  ? 166.111 145.354 161.241 1.00 40.22  ? 771  SER A O     1 
ATOM   4812 C CB    . SER A 1 771  ? 168.673 147.184 162.305 1.00 37.75  ? 771  SER A CB    1 
ATOM   4813 O OG    . SER A 1 771  ? 169.986 147.246 162.824 1.00 52.16  ? 771  SER A OG    1 
ATOM   4814 N N     . LEU A 1 772  ? 167.105 146.605 159.651 1.00 36.75  ? 772  LEU A N     1 
ATOM   4815 C CA    . LEU A 1 772  ? 165.871 146.729 158.883 1.00 34.92  ? 772  LEU A CA    1 
ATOM   4816 C C     . LEU A 1 772  ? 165.368 145.370 158.425 1.00 36.02  ? 772  LEU A C     1 
ATOM   4817 O O     . LEU A 1 772  ? 164.165 145.093 158.483 1.00 38.81  ? 772  LEU A O     1 
ATOM   4818 C CB    . LEU A 1 772  ? 166.081 147.643 157.677 1.00 38.06  ? 772  LEU A CB    1 
ATOM   4819 C CG    . LEU A 1 772  ? 166.511 149.081 157.950 1.00 40.42  ? 772  LEU A CG    1 
ATOM   4820 C CD1   . LEU A 1 772  ? 166.231 149.956 156.745 1.00 43.90  ? 772  LEU A CD1   1 
ATOM   4821 C CD2   . LEU A 1 772  ? 165.824 149.618 159.184 1.00 36.47  ? 772  LEU A CD2   1 
ATOM   4822 N N     . PHE A 1 773  ? 166.271 144.503 157.969 1.00 33.22  ? 773  PHE A N     1 
ATOM   4823 C CA    . PHE A 1 773  ? 165.822 143.202 157.491 1.00 30.97  ? 773  PHE A CA    1 
ATOM   4824 C C     . PHE A 1 773  ? 165.553 142.227 158.628 1.00 34.46  ? 773  PHE A C     1 
ATOM   4825 O O     . PHE A 1 773  ? 164.732 141.320 158.469 1.00 35.29  ? 773  PHE A O     1 
ATOM   4826 C CB    . PHE A 1 773  ? 166.828 142.620 156.504 1.00 30.47  ? 773  PHE A CB    1 
ATOM   4827 C CG    . PHE A 1 773  ? 166.443 142.840 155.076 1.00 33.03  ? 773  PHE A CG    1 
ATOM   4828 C CD1   . PHE A 1 773  ? 165.452 142.074 154.494 1.00 37.18  ? 773  PHE A CD1   1 
ATOM   4829 C CD2   . PHE A 1 773  ? 167.045 143.830 154.324 1.00 35.85  ? 773  PHE A CD2   1 
ATOM   4830 C CE1   . PHE A 1 773  ? 165.080 142.277 153.186 1.00 37.05  ? 773  PHE A CE1   1 
ATOM   4831 C CE2   . PHE A 1 773  ? 166.676 144.037 153.014 1.00 37.42  ? 773  PHE A CE2   1 
ATOM   4832 C CZ    . PHE A 1 773  ? 165.693 143.258 152.447 1.00 38.15  ? 773  PHE A CZ    1 
ATOM   4833 N N     . ASP A 1 774  ? 166.210 142.395 159.777 1.00 38.20  ? 774  ASP A N     1 
ATOM   4834 C CA    . ASP A 1 774  ? 165.850 141.608 160.949 1.00 33.80  ? 774  ASP A CA    1 
ATOM   4835 C C     . ASP A 1 774  ? 164.450 141.967 161.424 1.00 33.18  ? 774  ASP A C     1 
ATOM   4836 O O     . ASP A 1 774  ? 163.713 141.107 161.919 1.00 37.24  ? 774  ASP A O     1 
ATOM   4837 C CB    . ASP A 1 774  ? 166.875 141.825 162.060 1.00 33.71  ? 774  ASP A CB    1 
ATOM   4838 C CG    . ASP A 1 774  ? 166.624 140.946 163.265 1.00 44.24  ? 774  ASP A CG    1 
ATOM   4839 O OD1   . ASP A 1 774  ? 166.687 139.707 163.123 1.00 43.17  ? 774  ASP A OD1   1 
ATOM   4840 O OD2   . ASP A 1 774  ? 166.370 141.493 164.357 1.00 49.71  ? 774  ASP A OD2   1 
ATOM   4841 N N     . PHE A 1 775  ? 164.070 143.239 161.292 1.00 32.77  ? 775  PHE A N     1 
ATOM   4842 C CA    . PHE A 1 775  ? 162.682 143.620 161.524 1.00 30.36  ? 775  PHE A CA    1 
ATOM   4843 C C     . PHE A 1 775  ? 161.764 143.007 160.472 1.00 37.28  ? 775  PHE A C     1 
ATOM   4844 O O     . PHE A 1 775  ? 160.751 142.381 160.805 1.00 37.26  ? 775  PHE A O     1 
ATOM   4845 C CB    . PHE A 1 775  ? 162.545 145.142 161.531 1.00 27.83  ? 775  PHE A CB    1 
ATOM   4846 C CG    . PHE A 1 775  ? 161.132 145.620 161.369 1.00 31.34  ? 775  PHE A CG    1 
ATOM   4847 C CD1   . PHE A 1 775  ? 160.260 145.621 162.443 1.00 30.03  ? 775  PHE A CD1   1 
ATOM   4848 C CD2   . PHE A 1 775  ? 160.671 146.065 160.140 1.00 34.30  ? 775  PHE A CD2   1 
ATOM   4849 C CE1   . PHE A 1 775  ? 158.960 146.056 162.297 1.00 28.64  ? 775  PHE A CE1   1 
ATOM   4850 C CE2   . PHE A 1 775  ? 159.369 146.498 159.989 1.00 33.05  ? 775  PHE A CE2   1 
ATOM   4851 C CZ    . PHE A 1 775  ? 158.513 146.491 161.068 1.00 24.17  ? 775  PHE A CZ    1 
ATOM   4852 N N     . ALA A 1 776  ? 162.113 143.167 159.195 1.00 37.47  ? 776  ALA A N     1 
ATOM   4853 C CA    . ALA A 1 776  ? 161.230 142.732 158.117 1.00 34.96  ? 776  ALA A CA    1 
ATOM   4854 C C     . ALA A 1 776  ? 161.222 141.214 157.983 1.00 37.93  ? 776  ALA A C     1 
ATOM   4855 O O     . ALA A 1 776  ? 160.182 140.568 158.148 1.00 40.72  ? 776  ALA A O     1 
ATOM   4856 C CB    . ALA A 1 776  ? 161.651 143.390 156.803 1.00 33.54  ? 776  ALA A CB    1 
ATOM   4857 N N     . GLN A 1 777  ? 162.379 140.624 157.685 1.00 39.47  ? 777  GLN A N     1 
ATOM   4858 C CA    . GLN A 1 777  ? 162.504 139.184 157.462 1.00 36.71  ? 777  GLN A CA    1 
ATOM   4859 C C     . GLN A 1 777  ? 163.574 138.642 158.397 1.00 36.15  ? 777  GLN A C     1 
ATOM   4860 O O     . GLN A 1 777  ? 164.757 138.578 158.034 1.00 35.53  ? 777  GLN A O     1 
ATOM   4861 C CB    . GLN A 1 777  ? 162.843 138.879 156.004 1.00 35.82  ? 777  GLN A CB    1 
ATOM   4862 C CG    . GLN A 1 777  ? 162.929 137.399 155.689 1.00 38.81  ? 777  GLN A CG    1 
ATOM   4863 C CD    . GLN A 1 777  ? 161.578 136.723 155.719 1.00 40.60  ? 777  GLN A CD    1 
ATOM   4864 O OE1   . GLN A 1 777  ? 160.624 137.199 155.109 1.00 44.34  ? 777  GLN A OE1   1 
ATOM   4865 N NE2   . GLN A 1 777  ? 161.486 135.611 156.437 1.00 37.79  ? 777  GLN A NE2   1 
ATOM   4866 N N     . PRO A 1 778  ? 163.201 138.258 159.617 1.00 34.23  ? 778  PRO A N     1 
ATOM   4867 C CA    . PRO A 1 778  ? 164.201 137.764 160.570 1.00 34.96  ? 778  PRO A CA    1 
ATOM   4868 C C     . PRO A 1 778  ? 164.905 136.520 160.048 1.00 40.19  ? 778  PRO A C     1 
ATOM   4869 O O     . PRO A 1 778  ? 164.279 135.609 159.504 1.00 42.12  ? 778  PRO A O     1 
ATOM   4870 C CB    . PRO A 1 778  ? 163.376 137.458 161.824 1.00 32.01  ? 778  PRO A CB    1 
ATOM   4871 C CG    . PRO A 1 778  ? 162.128 138.261 161.671 1.00 34.24  ? 778  PRO A CG    1 
ATOM   4872 C CD    . PRO A 1 778  ? 161.852 138.298 160.203 1.00 35.16  ? 778  PRO A CD    1 
ATOM   4873 N N     . GLY A 1 779  ? 166.223 136.491 160.227 1.00 37.23  ? 779  GLY A N     1 
ATOM   4874 C CA    . GLY A 1 779  ? 167.031 135.363 159.820 1.00 36.34  ? 779  GLY A CA    1 
ATOM   4875 C C     . GLY A 1 779  ? 167.479 135.368 158.376 1.00 39.40  ? 779  GLY A C     1 
ATOM   4876 O O     . GLY A 1 779  ? 168.246 134.480 157.985 1.00 41.09  ? 779  GLY A O     1 
ATOM   4877 N N     . LEU A 1 780  ? 167.024 136.329 157.567 1.00 40.90  ? 780  LEU A N     1 
ATOM   4878 C CA    . LEU A 1 780  ? 167.463 136.388 156.176 1.00 42.52  ? 780  LEU A CA    1 
ATOM   4879 C C     . LEU A 1 780  ? 168.957 136.661 156.079 1.00 41.43  ? 780  LEU A C     1 
ATOM   4880 O O     . LEU A 1 780  ? 169.665 136.019 155.295 1.00 41.87  ? 780  LEU A O     1 
ATOM   4881 C CB    . LEU A 1 780  ? 166.679 137.459 155.418 1.00 42.83  ? 780  LEU A CB    1 
ATOM   4882 C CG    . LEU A 1 780  ? 167.026 137.600 153.935 1.00 41.33  ? 780  LEU A CG    1 
ATOM   4883 C CD1   . LEU A 1 780  ? 166.479 136.423 153.143 1.00 44.30  ? 780  LEU A CD1   1 
ATOM   4884 C CD2   . LEU A 1 780  ? 166.513 138.913 153.375 1.00 36.76  ? 780  LEU A CD2   1 
ATOM   4885 N N     . LEU A 1 781  ? 169.453 137.612 156.866 1.00 37.80  ? 781  LEU A N     1 
ATOM   4886 C CA    . LEU A 1 781  ? 170.866 137.957 156.884 1.00 38.81  ? 781  LEU A CA    1 
ATOM   4887 C C     . LEU A 1 781  ? 171.635 137.237 157.982 1.00 44.61  ? 781  LEU A C     1 
ATOM   4888 O O     . LEU A 1 781  ? 172.836 137.481 158.138 1.00 52.91  ? 781  LEU A O     1 
ATOM   4889 C CB    . LEU A 1 781  ? 171.034 139.472 157.042 1.00 37.25  ? 781  LEU A CB    1 
ATOM   4890 C CG    . LEU A 1 781  ? 170.382 140.346 155.968 1.00 35.04  ? 781  LEU A CG    1 
ATOM   4891 C CD1   . LEU A 1 781  ? 170.599 141.817 156.264 1.00 34.99  ? 781  LEU A CD1   1 
ATOM   4892 C CD2   . LEU A 1 781  ? 170.917 139.996 154.592 1.00 40.06  ? 781  LEU A CD2   1 
ATOM   4893 N N     . GLY A 1 782  ? 170.982 136.361 158.738 1.00 41.49  ? 782  GLY A N     1 
ATOM   4894 C CA    . GLY A 1 782  ? 171.644 135.641 159.801 1.00 41.71  ? 782  GLY A CA    1 
ATOM   4895 C C     . GLY A 1 782  ? 171.868 136.500 161.031 1.00 47.73  ? 782  GLY A C     1 
ATOM   4896 O O     . GLY A 1 782  ? 171.282 137.571 161.206 1.00 47.23  ? 782  GLY A O     1 
ATOM   4897 N N     . ALA A 1 783  ? 172.742 136.003 161.901 1.00 51.81  ? 783  ALA A N     1 
ATOM   4898 C CA    . ALA A 1 783  ? 173.085 136.728 163.113 1.00 49.05  ? 783  ALA A CA    1 
ATOM   4899 C C     . ALA A 1 783  ? 173.890 137.979 162.776 1.00 48.18  ? 783  ALA A C     1 
ATOM   4900 O O     . ALA A 1 783  ? 174.491 138.097 161.705 1.00 52.42  ? 783  ALA A O     1 
ATOM   4901 C CB    . ALA A 1 783  ? 173.876 135.836 164.069 1.00 54.35  ? 783  ALA A CB    1 
ATOM   4902 N N     . LEU A 1 784  ? 173.888 138.930 163.713 1.00 44.36  ? 784  LEU A N     1 
ATOM   4903 C CA    . LEU A 1 784  ? 174.586 140.190 163.482 1.00 44.04  ? 784  LEU A CA    1 
ATOM   4904 C C     . LEU A 1 784  ? 176.092 139.985 163.393 1.00 56.75  ? 784  LEU A C     1 
ATOM   4905 O O     . LEU A 1 784  ? 176.766 140.656 162.604 1.00 63.48  ? 784  LEU A O     1 
ATOM   4906 C CB    . LEU A 1 784  ? 174.245 141.192 164.582 1.00 45.05  ? 784  LEU A CB    1 
ATOM   4907 C CG    . LEU A 1 784  ? 174.908 142.563 164.443 1.00 50.87  ? 784  LEU A CG    1 
ATOM   4908 C CD1   . LEU A 1 784  ? 174.629 143.164 163.076 1.00 44.08  ? 784  LEU A CD1   1 
ATOM   4909 C CD2   . LEU A 1 784  ? 174.438 143.495 165.537 1.00 55.53  ? 784  LEU A CD2   1 
ATOM   4910 N N     . ASN A 1 785  ? 176.643 139.078 164.201 1.00 60.84  ? 785  ASN A N     1 
ATOM   4911 C CA    . ASN A 1 785  ? 178.076 138.809 164.129 1.00 61.50  ? 785  ASN A CA    1 
ATOM   4912 C C     . ASN A 1 785  ? 178.456 138.185 162.791 1.00 62.77  ? 785  ASN A C     1 
ATOM   4913 O O     . ASN A 1 785  ? 179.479 138.548 162.199 1.00 63.49  ? 785  ASN A O     1 
ATOM   4914 C CB    . ASN A 1 785  ? 178.504 137.910 165.289 1.00 67.23  ? 785  ASN A CB    1 
ATOM   4915 C CG    . ASN A 1 785  ? 177.747 136.599 165.322 1.00 73.31  ? 785  ASN A CG    1 
ATOM   4916 O OD1   . ASN A 1 785  ? 178.187 135.600 164.753 1.00 72.35  ? 785  ASN A OD1   1 
ATOM   4917 N ND2   . ASN A 1 785  ? 176.602 136.594 165.994 1.00 76.04  ? 785  ASN A ND2   1 
ATOM   4918 N N     . GLU A 1 786  ? 177.643 137.246 162.299 1.00 62.60  ? 786  GLU A N     1 
ATOM   4919 C CA    . GLU A 1 786  ? 177.902 136.653 160.991 1.00 63.68  ? 786  GLU A CA    1 
ATOM   4920 C C     . GLU A 1 786  ? 177.814 137.699 159.887 1.00 66.00  ? 786  GLU A C     1 
ATOM   4921 O O     . GLU A 1 786  ? 178.653 137.728 158.979 1.00 71.69  ? 786  GLU A O     1 
ATOM   4922 C CB    . GLU A 1 786  ? 176.918 135.512 160.728 1.00 67.55  ? 786  GLU A CB    1 
ATOM   4923 C CG    . GLU A 1 786  ? 177.112 134.297 161.621 1.00 76.86  ? 786  GLU A CG    1 
ATOM   4924 C CD    . GLU A 1 786  ? 178.368 133.518 161.282 1.00 86.28  ? 786  GLU A CD    1 
ATOM   4925 O OE1   . GLU A 1 786  ? 178.840 133.619 160.130 1.00 82.18  ? 786  GLU A OE1   1 
ATOM   4926 O OE2   . GLU A 1 786  ? 178.886 132.807 162.169 1.00 82.45  ? 786  GLU A OE2   1 
ATOM   4927 N N     . PHE A 1 787  ? 176.804 138.569 159.953 1.00 60.52  ? 787  PHE A N     1 
ATOM   4928 C CA    . PHE A 1 787  ? 176.668 139.626 158.957 1.00 55.35  ? 787  PHE A CA    1 
ATOM   4929 C C     . PHE A 1 787  ? 177.857 140.577 158.996 1.00 56.74  ? 787  PHE A C     1 
ATOM   4930 O O     . PHE A 1 787  ? 178.359 140.998 157.948 1.00 64.32  ? 787  PHE A O     1 
ATOM   4931 C CB    . PHE A 1 787  ? 175.360 140.386 159.182 1.00 49.14  ? 787  PHE A CB    1 
ATOM   4932 C CG    . PHE A 1 787  ? 175.140 141.520 158.220 1.00 48.40  ? 787  PHE A CG    1 
ATOM   4933 C CD1   . PHE A 1 787  ? 174.625 141.284 156.959 1.00 44.83  ? 787  PHE A CD1   1 
ATOM   4934 C CD2   . PHE A 1 787  ? 175.439 142.822 158.582 1.00 46.59  ? 787  PHE A CD2   1 
ATOM   4935 C CE1   . PHE A 1 787  ? 174.419 142.323 156.074 1.00 40.86  ? 787  PHE A CE1   1 
ATOM   4936 C CE2   . PHE A 1 787  ? 175.234 143.864 157.700 1.00 42.49  ? 787  PHE A CE2   1 
ATOM   4937 C CZ    . PHE A 1 787  ? 174.723 143.613 156.445 1.00 37.59  ? 787  PHE A CZ    1 
ATOM   4938 N N     . GLY A 1 788  ? 178.318 140.928 160.197 1.00 55.35  ? 788  GLY A N     1 
ATOM   4939 C CA    . GLY A 1 788  ? 179.463 141.815 160.309 1.00 62.50  ? 788  GLY A CA    1 
ATOM   4940 C C     . GLY A 1 788  ? 180.740 141.194 159.779 1.00 73.74  ? 788  GLY A C     1 
ATOM   4941 O O     . GLY A 1 788  ? 181.490 141.834 159.037 1.00 78.47  ? 788  GLY A O     1 
ATOM   4942 N N     . LYS A 1 789  ? 181.003 139.937 160.140 1.00 73.03  ? 789  LYS A N     1 
ATOM   4943 C CA    . LYS A 1 789  ? 182.188 139.249 159.644 1.00 72.50  ? 789  LYS A CA    1 
ATOM   4944 C C     . LYS A 1 789  ? 182.075 138.867 158.176 1.00 71.70  ? 789  LYS A C     1 
ATOM   4945 O O     . LYS A 1 789  ? 183.085 138.484 157.576 1.00 76.27  ? 789  LYS A O     1 
ATOM   4946 C CB    . LYS A 1 789  ? 182.460 137.997 160.480 1.00 76.89  ? 789  LYS A CB    1 
ATOM   4947 C CG    . LYS A 1 789  ? 182.737 138.276 161.946 1.00 81.10  ? 789  LYS A CG    1 
ATOM   4948 C CD    . LYS A 1 789  ? 183.165 137.016 162.681 1.00 77.50  ? 789  LYS A CD    1 
ATOM   4949 C CE    . LYS A 1 789  ? 182.095 135.941 162.609 1.00 73.77  ? 789  LYS A CE    1 
ATOM   4950 N NZ    . LYS A 1 789  ? 182.503 134.705 163.332 1.00 68.70  ? 789  LYS A NZ    1 
ATOM   4951 N N     . GLN A 1 790  ? 180.884 138.955 157.587 1.00 70.30  ? 790  GLN A N     1 
ATOM   4952 C CA    . GLN A 1 790  ? 180.666 138.543 156.209 1.00 66.83  ? 790  GLN A CA    1 
ATOM   4953 C C     . GLN A 1 790  ? 180.384 139.696 155.258 1.00 69.84  ? 790  GLN A C     1 
ATOM   4954 O O     . GLN A 1 790  ? 180.749 139.609 154.085 1.00 75.11  ? 790  GLN A O     1 
ATOM   4955 C CB    . GLN A 1 790  ? 179.503 137.546 156.138 1.00 65.25  ? 790  GLN A CB    1 
ATOM   4956 C CG    . GLN A 1 790  ? 179.546 136.615 154.943 1.00 71.75  ? 790  GLN A CG    1 
ATOM   4957 C CD    . GLN A 1 790  ? 178.398 135.625 154.936 1.00 80.98  ? 790  GLN A CD    1 
ATOM   4958 O OE1   . GLN A 1 790  ? 177.364 135.851 155.564 1.00 82.51  ? 790  GLN A OE1   1 
ATOM   4959 N NE2   . GLN A 1 790  ? 178.578 134.515 154.229 1.00 80.60  ? 790  GLN A NE2   1 
ATOM   4960 N N     . TYR A 1 791  ? 179.747 140.769 155.728 1.00 68.99  ? 791  TYR A N     1 
ATOM   4961 C CA    . TYR A 1 791  ? 179.382 141.886 154.865 1.00 65.31  ? 791  TYR A CA    1 
ATOM   4962 C C     . TYR A 1 791  ? 179.794 143.255 155.384 1.00 69.41  ? 791  TYR A C     1 
ATOM   4963 O O     . TYR A 1 791  ? 179.803 144.205 154.594 1.00 74.23  ? 791  TYR A O     1 
ATOM   4964 C CB    . TYR A 1 791  ? 177.866 141.902 154.615 1.00 56.77  ? 791  TYR A CB    1 
ATOM   4965 C CG    . TYR A 1 791  ? 177.362 140.724 153.817 1.00 58.33  ? 791  TYR A CG    1 
ATOM   4966 C CD1   . TYR A 1 791  ? 177.590 140.638 152.451 1.00 60.22  ? 791  TYR A CD1   1 
ATOM   4967 C CD2   . TYR A 1 791  ? 176.650 139.702 154.427 1.00 62.67  ? 791  TYR A CD2   1 
ATOM   4968 C CE1   . TYR A 1 791  ? 177.129 139.566 151.717 1.00 62.28  ? 791  TYR A CE1   1 
ATOM   4969 C CE2   . TYR A 1 791  ? 176.184 138.626 153.702 1.00 66.00  ? 791  TYR A CE2   1 
ATOM   4970 C CZ    . TYR A 1 791  ? 176.426 138.562 152.348 1.00 66.17  ? 791  TYR A CZ    1 
ATOM   4971 O OH    . TYR A 1 791  ? 175.962 137.489 151.623 1.00 68.31  ? 791  TYR A OH    1 
ATOM   4972 N N     . VAL A 1 792  ? 180.121 143.401 156.665 1.00 68.89  ? 792  VAL A N     1 
ATOM   4973 C CA    . VAL A 1 792  ? 180.510 144.703 157.198 1.00 74.08  ? 792  VAL A CA    1 
ATOM   4974 C C     . VAL A 1 792  ? 182.027 144.823 157.197 1.00 82.16  ? 792  VAL A C     1 
ATOM   4975 O O     . VAL A 1 792  ? 182.585 145.759 156.614 1.00 84.15  ? 792  VAL A O     1 
ATOM   4976 C CB    . VAL A 1 792  ? 179.943 144.927 158.611 1.00 71.98  ? 792  VAL A CB    1 
ATOM   4977 C CG1   . VAL A 1 792  ? 180.583 146.148 159.249 1.00 76.16  ? 792  VAL A CG1   1 
ATOM   4978 C CG2   . VAL A 1 792  ? 178.436 145.089 158.554 1.00 62.47  ? 792  VAL A CG2   1 
ATOM   4979 N N     . ARG A 1 793  ? 182.703 143.881 157.853 1.00 80.76  ? 793  ARG A N     1 
ATOM   4980 C CA    . ARG A 1 793  ? 184.163 143.920 157.908 1.00 85.12  ? 793  ARG A CA    1 
ATOM   4981 C C     . ARG A 1 793  ? 184.812 143.815 156.532 1.00 88.95  ? 793  ARG A C     1 
ATOM   4982 O O     . ARG A 1 793  ? 185.747 144.589 156.260 1.00 93.80  ? 793  ARG A O     1 
ATOM   4983 C CB    . ARG A 1 793  ? 184.672 142.832 158.861 1.00 84.92  ? 793  ARG A CB    1 
ATOM   4984 C CG    . ARG A 1 793  ? 184.191 143.002 160.292 1.00 85.84  ? 793  ARG A CG    1 
ATOM   4985 C CD    . ARG A 1 793  ? 184.647 141.853 161.174 1.00 84.85  ? 793  ARG A CD    1 
ATOM   4986 N NE    . ARG A 1 793  ? 184.067 141.935 162.508 1.00 87.47  ? 793  ARG A NE    1 
ATOM   4987 C CZ    . ARG A 1 793  ? 184.331 141.088 163.494 1.00 91.84  ? 793  ARG A CZ    1 
ATOM   4988 N NH1   . ARG A 1 793  ? 185.169 140.078 163.332 1.00 89.90  ? 793  ARG A NH1   1 
ATOM   4989 N NH2   . ARG A 1 793  ? 183.740 141.261 164.673 1.00 91.70  ? 793  ARG A NH2   1 
ATOM   4990 N N     . PRO A 1 794  ? 184.408 142.902 155.638 1.00 87.33  ? 794  PRO A N     1 
ATOM   4991 C CA    . PRO A 1 794  ? 184.992 142.922 154.285 1.00 91.30  ? 794  PRO A CA    1 
ATOM   4992 C C     . PRO A 1 794  ? 184.743 144.219 153.536 1.00 92.25  ? 794  PRO A C     1 
ATOM   4993 O O     . PRO A 1 794  ? 185.599 144.642 152.748 1.00 93.51  ? 794  PRO A O     1 
ATOM   4994 C CB    . PRO A 1 794  ? 184.313 141.732 153.593 1.00 87.29  ? 794  PRO A CB    1 
ATOM   4995 C CG    . PRO A 1 794  ? 183.930 140.827 154.700 1.00 84.86  ? 794  PRO A CG    1 
ATOM   4996 C CD    . PRO A 1 794  ? 183.530 141.732 155.823 1.00 83.57  ? 794  PRO A CD    1 
ATOM   4997 N N     . ILE A 1 795  ? 183.600 144.862 153.754 1.00 88.40  ? 795  ILE A N     1 
ATOM   4998 C CA    . ILE A 1 795  ? 183.289 146.114 153.071 1.00 90.94  ? 795  ILE A CA    1 
ATOM   4999 C C     . ILE A 1 795  ? 183.863 147.312 153.816 1.00 92.48  ? 795  ILE A C     1 
ATOM   5000 O O     . ILE A 1 795  ? 184.449 148.208 153.203 1.00 89.36  ? 795  ILE A O     1 
ATOM   5001 C CB    . ILE A 1 795  ? 181.764 146.242 152.884 1.00 86.92  ? 795  ILE A CB    1 
ATOM   5002 C CG1   . ILE A 1 795  ? 181.264 145.187 151.899 1.00 80.34  ? 795  ILE A CG1   1 
ATOM   5003 C CG2   . ILE A 1 795  ? 181.394 147.636 152.403 1.00 85.40  ? 795  ILE A CG2   1 
ATOM   5004 C CD1   . ILE A 1 795  ? 181.951 145.248 150.560 1.00 82.31  ? 795  ILE A CD1   1 
ATOM   5005 N N     . GLU A 1 796  ? 183.712 147.346 155.135 1.00 90.68  ? 796  GLU A N     1 
ATOM   5006 C CA    . GLU A 1 796  ? 184.179 148.474 155.932 1.00 90.54  ? 796  GLU A CA    1 
ATOM   5007 C C     . GLU A 1 796  ? 185.436 148.110 156.714 1.00 93.45  ? 796  GLU A C     1 
ATOM   5008 O O     . GLU A 1 796  ? 186.350 148.923 156.851 1.00 95.07  ? 796  GLU A O     1 
ATOM   5009 C CB    . GLU A 1 796  ? 183.077 148.939 156.885 1.00 88.29  ? 796  GLU A CB    1 
ATOM   5010 C CG    . GLU A 1 796  ? 181.760 149.250 156.194 1.00 87.37  ? 796  GLU A CG    1 
ATOM   5011 C CD    . GLU A 1 796  ? 180.623 149.465 157.172 1.00 85.45  ? 796  GLU A CD    1 
ATOM   5012 O OE1   . GLU A 1 796  ? 180.853 149.328 158.391 1.00 82.33  ? 796  GLU A OE1   1 
ATOM   5013 O OE2   . GLU A 1 796  ? 179.500 149.770 156.719 1.00 74.56  ? 796  GLU A OE2   1 
ATOM   5014 N N     . THR A 1 803  ? 182.649 145.888 144.755 1.00 72.65  ? 803  THR A N     1 
ATOM   5015 C CA    . THR A 1 803  ? 183.062 144.743 145.556 1.00 82.46  ? 803  THR A CA    1 
ATOM   5016 C C     . THR A 1 803  ? 182.068 143.598 145.390 1.00 83.89  ? 803  THR A C     1 
ATOM   5017 O O     . THR A 1 803  ? 180.873 143.826 145.208 1.00 85.14  ? 803  THR A O     1 
ATOM   5018 C CB    . THR A 1 803  ? 183.182 145.110 147.048 1.00 86.44  ? 803  THR A CB    1 
ATOM   5019 O OG1   . THR A 1 803  ? 183.783 146.404 147.176 1.00 88.84  ? 803  THR A OG1   1 
ATOM   5020 C CG2   . THR A 1 803  ? 184.043 144.092 147.783 1.00 74.22  ? 803  THR A CG2   1 
ATOM   5021 N N     . GLU A 1 804  ? 182.569 142.362 145.451 1.00 81.02  ? 804  GLU A N     1 
ATOM   5022 C CA    . GLU A 1 804  ? 181.699 141.203 145.281 1.00 76.66  ? 804  GLU A CA    1 
ATOM   5023 C C     . GLU A 1 804  ? 180.820 140.972 146.503 1.00 78.22  ? 804  GLU A C     1 
ATOM   5024 O O     . GLU A 1 804  ? 179.724 140.411 146.378 1.00 76.28  ? 804  GLU A O     1 
ATOM   5025 C CB    . GLU A 1 804  ? 182.536 139.961 144.982 1.00 76.81  ? 804  GLU A CB    1 
ATOM   5026 C CG    . GLU A 1 804  ? 183.361 140.068 143.710 1.00 83.44  ? 804  GLU A CG    1 
ATOM   5027 C CD    . GLU A 1 804  ? 184.156 138.811 143.420 1.00 88.25  ? 804  GLU A CD    1 
ATOM   5028 O OE1   . GLU A 1 804  ? 184.166 137.901 144.276 1.00 83.68  ? 804  GLU A OE1   1 
ATOM   5029 O OE2   . GLU A 1 804  ? 184.769 138.731 142.335 1.00 87.23  ? 804  GLU A OE2   1 
ATOM   5030 N N     . ARG A 1 805  ? 181.278 141.388 147.686 1.00 79.43  ? 805  ARG A N     1 
ATOM   5031 C CA    . ARG A 1 805  ? 180.462 141.246 148.888 1.00 76.61  ? 805  ARG A CA    1 
ATOM   5032 C C     . ARG A 1 805  ? 179.172 142.048 148.766 1.00 72.31  ? 805  ARG A C     1 
ATOM   5033 O O     . ARG A 1 805  ? 178.086 141.559 149.103 1.00 69.29  ? 805  ARG A O     1 
ATOM   5034 C CB    . ARG A 1 805  ? 181.254 141.686 150.119 1.00 77.38  ? 805  ARG A CB    1 
ATOM   5035 C CG    . ARG A 1 805  ? 182.639 141.071 150.240 1.00 79.17  ? 805  ARG A CG    1 
ATOM   5036 C CD    . ARG A 1 805  ? 182.591 139.560 150.115 1.00 86.29  ? 805  ARG A CD    1 
ATOM   5037 N NE    . ARG A 1 805  ? 181.618 138.962 151.022 1.00 88.55  ? 805  ARG A NE    1 
ATOM   5038 C CZ    . ARG A 1 805  ? 181.310 137.673 151.039 1.00 85.69  ? 805  ARG A CZ    1 
ATOM   5039 N NH1   . ARG A 1 805  ? 181.888 136.813 150.216 1.00 84.76  ? 805  ARG A NH1   1 
ATOM   5040 N NH2   . ARG A 1 805  ? 180.397 137.235 151.900 1.00 76.56  ? 805  ARG A NH2   1 
ATOM   5041 N N     . LEU A 1 806  ? 179.274 143.289 148.286 1.00 72.21  ? 806  LEU A N     1 
ATOM   5042 C CA    . LEU A 1 806  ? 178.086 144.098 148.054 1.00 74.87  ? 806  LEU A CA    1 
ATOM   5043 C C     . LEU A 1 806  ? 177.174 143.500 146.996 1.00 72.46  ? 806  LEU A C     1 
ATOM   5044 O O     . LEU A 1 806  ? 175.952 143.541 147.167 1.00 72.96  ? 806  LEU A O     1 
ATOM   5045 C CB    . LEU A 1 806  ? 178.478 145.522 147.650 1.00 77.91  ? 806  LEU A CB    1 
ATOM   5046 C CG    . LEU A 1 806  ? 179.032 146.432 148.750 1.00 83.80  ? 806  LEU A CG    1 
ATOM   5047 C CD1   . LEU A 1 806  ? 179.248 147.845 148.229 1.00 81.07  ? 806  LEU A CD1   1 
ATOM   5048 C CD2   . LEU A 1 806  ? 178.114 146.440 149.961 1.00 70.41  ? 806  LEU A CD2   1 
ATOM   5049 N N     . GLU A 1 807  ? 177.726 142.937 145.921 1.00 73.43  ? 807  GLU A N     1 
ATOM   5050 C CA    . GLU A 1 807  ? 176.920 142.326 144.876 1.00 74.95  ? 807  GLU A CA    1 
ATOM   5051 C C     . GLU A 1 807  ? 176.276 141.017 145.302 1.00 68.17  ? 807  GLU A C     1 
ATOM   5052 O O     . GLU A 1 807  ? 175.284 140.610 144.689 1.00 65.53  ? 807  GLU A O     1 
ATOM   5053 C CB    . GLU A 1 807  ? 177.767 142.087 143.618 1.00 75.23  ? 807  GLU A CB    1 
ATOM   5054 C CG    . GLU A 1 807  ? 178.302 143.360 142.989 1.00 75.76  ? 807  GLU A CG    1 
ATOM   5055 C CD    . GLU A 1 807  ? 177.197 144.291 142.532 1.00 80.17  ? 807  GLU A CD    1 
ATOM   5056 O OE1   . GLU A 1 807  ? 176.133 143.793 142.107 1.00 82.49  ? 807  GLU A OE1   1 
ATOM   5057 O OE2   . GLU A 1 807  ? 177.390 145.522 142.603 1.00 80.31  ? 807  GLU A OE2   1 
ATOM   5058 N N     . SER A 1 808  ? 176.810 140.348 146.322 1.00 66.59  ? 808  SER A N     1 
ATOM   5059 C CA    . SER A 1 808  ? 176.134 139.202 146.911 1.00 64.56  ? 808  SER A CA    1 
ATOM   5060 C C     . SER A 1 808  ? 175.073 139.604 147.925 1.00 64.97  ? 808  SER A C     1 
ATOM   5061 O O     . SER A 1 808  ? 174.002 138.987 147.959 1.00 64.71  ? 808  SER A O     1 
ATOM   5062 C CB    . SER A 1 808  ? 177.150 138.269 147.581 1.00 67.64  ? 808  SER A CB    1 
ATOM   5063 O OG    . SER A 1 808  ? 177.868 138.943 148.599 1.00 74.09  ? 808  SER A OG    1 
ATOM   5064 N N     . LEU A 1 809  ? 175.339 140.632 148.733 1.00 62.86  ? 809  LEU A N     1 
ATOM   5065 C CA    . LEU A 1 809  ? 174.327 141.139 149.653 1.00 55.59  ? 809  LEU A CA    1 
ATOM   5066 C C     . LEU A 1 809  ? 173.125 141.688 148.894 1.00 53.60  ? 809  LEU A C     1 
ATOM   5067 O O     . LEU A 1 809  ? 171.973 141.481 149.297 1.00 53.90  ? 809  LEU A O     1 
ATOM   5068 C CB    . LEU A 1 809  ? 174.936 142.213 150.555 1.00 57.23  ? 809  LEU A CB    1 
ATOM   5069 C CG    . LEU A 1 809  ? 174.005 142.875 151.571 1.00 45.96  ? 809  LEU A CG    1 
ATOM   5070 C CD1   . LEU A 1 809  ? 173.448 141.845 152.536 1.00 49.50  ? 809  LEU A CD1   1 
ATOM   5071 C CD2   . LEU A 1 809  ? 174.733 143.975 152.318 1.00 46.11  ? 809  LEU A CD2   1 
ATOM   5072 N N     . ARG A 1 810  ? 173.377 142.395 147.793 1.00 56.85  ? 810  ARG A N     1 
ATOM   5073 C CA    . ARG A 1 810  ? 172.333 142.973 146.962 1.00 52.87  ? 810  ARG A CA    1 
ATOM   5074 C C     . ARG A 1 810  ? 171.479 141.920 146.277 1.00 55.43  ? 810  ARG A C     1 
ATOM   5075 O O     . ARG A 1 810  ? 170.295 142.171 146.033 1.00 56.24  ? 810  ARG A O     1 
ATOM   5076 C CB    . ARG A 1 810  ? 172.959 143.894 145.912 1.00 54.59  ? 810  ARG A CB    1 
ATOM   5077 C CG    . ARG A 1 810  ? 171.976 144.809 145.208 1.00 63.55  ? 810  ARG A CG    1 
ATOM   5078 C CD    . ARG A 1 810  ? 172.668 145.591 144.108 1.00 67.63  ? 810  ARG A CD    1 
ATOM   5079 N NE    . ARG A 1 810  ? 173.964 146.098 144.541 1.00 68.17  ? 810  ARG A NE    1 
ATOM   5080 C CZ    . ARG A 1 810  ? 174.151 147.267 145.137 1.00 67.79  ? 810  ARG A CZ    1 
ATOM   5081 N NH1   . ARG A 1 810  ? 173.142 148.084 145.387 1.00 65.33  ? 810  ARG A NH1   1 
ATOM   5082 N NH2   . ARG A 1 810  ? 175.382 147.626 145.488 1.00 65.61  ? 810  ARG A NH2   1 
ATOM   5083 N N     . ALA A 1 811  ? 172.043 140.753 145.972 1.00 56.96  ? 811  ALA A N     1 
ATOM   5084 C CA    . ALA A 1 811  ? 171.281 139.653 145.404 1.00 53.71  ? 811  ALA A CA    1 
ATOM   5085 C C     . ALA A 1 811  ? 170.577 138.827 146.467 1.00 52.68  ? 811  ALA A C     1 
ATOM   5086 O O     . ALA A 1 811  ? 169.544 138.215 146.173 1.00 52.18  ? 811  ALA A O     1 
ATOM   5087 C CB    . ALA A 1 811  ? 172.191 138.746 144.568 1.00 53.13  ? 811  ALA A CB    1 
ATOM   5088 N N     . LEU A 1 812  ? 171.100 138.799 147.692 1.00 52.75  ? 812  LEU A N     1 
ATOM   5089 C CA    . LEU A 1 812  ? 170.420 138.169 148.814 1.00 48.13  ? 812  LEU A CA    1 
ATOM   5090 C C     . LEU A 1 812  ? 169.217 138.955 149.306 1.00 47.92  ? 812  LEU A C     1 
ATOM   5091 O O     . LEU A 1 812  ? 168.217 138.347 149.690 1.00 49.90  ? 812  LEU A O     1 
ATOM   5092 C CB    . LEU A 1 812  ? 171.397 137.968 149.982 1.00 50.90  ? 812  LEU A CB    1 
ATOM   5093 C CG    . LEU A 1 812  ? 170.868 137.287 151.245 1.00 51.14  ? 812  LEU A CG    1 
ATOM   5094 C CD1   . LEU A 1 812  ? 170.378 135.881 150.941 1.00 47.10  ? 812  LEU A CD1   1 
ATOM   5095 C CD2   . LEU A 1 812  ? 171.938 137.260 152.322 1.00 51.33  ? 812  LEU A CD2   1 
ATOM   5096 N N     . ILE A 1 813  ? 169.285 140.284 149.298 1.00 49.02  ? 813  ILE A N     1 
ATOM   5097 C CA    . ILE A 1 813  ? 168.150 141.086 149.746 1.00 44.13  ? 813  ILE A CA    1 
ATOM   5098 C C     . ILE A 1 813  ? 167.214 141.453 148.596 1.00 48.46  ? 813  ILE A C     1 
ATOM   5099 O O     . ILE A 1 813  ? 166.131 141.995 148.835 1.00 49.60  ? 813  ILE A O     1 
ATOM   5100 C CB    . ILE A 1 813  ? 168.635 142.350 150.477 1.00 37.45  ? 813  ILE A CB    1 
ATOM   5101 C CG1   . ILE A 1 813  ? 169.275 143.326 149.490 1.00 40.18  ? 813  ILE A CG1   1 
ATOM   5102 C CG2   . ILE A 1 813  ? 169.613 141.991 151.581 1.00 36.87  ? 813  ILE A CG2   1 
ATOM   5103 C CD1   . ILE A 1 813  ? 169.772 144.594 150.135 1.00 39.60  ? 813  ILE A CD1   1 
ATOM   5104 N N     . GLU A 1 814  ? 167.606 141.168 147.354 1.00 49.42  ? 814  GLU A N     1 
ATOM   5105 C CA    . GLU A 1 814  ? 166.821 141.565 146.184 1.00 45.03  ? 814  GLU A CA    1 
ATOM   5106 C C     . GLU A 1 814  ? 165.393 141.028 146.170 1.00 42.96  ? 814  GLU A C     1 
ATOM   5107 O O     . GLU A 1 814  ? 164.477 141.804 145.855 1.00 44.98  ? 814  GLU A O     1 
ATOM   5108 C CB    . GLU A 1 814  ? 167.572 141.145 144.912 1.00 51.90  ? 814  GLU A CB    1 
ATOM   5109 C CG    . GLU A 1 814  ? 167.166 141.901 143.654 1.00 54.52  ? 814  GLU A CG    1 
ATOM   5110 C CD    . GLU A 1 814  ? 165.984 141.277 142.937 1.00 60.21  ? 814  GLU A CD    1 
ATOM   5111 O OE1   . GLU A 1 814  ? 165.634 140.121 143.254 1.00 62.19  ? 814  GLU A OE1   1 
ATOM   5112 O OE2   . GLU A 1 814  ? 165.408 141.943 142.052 1.00 58.35  ? 814  GLU A OE2   1 
ATOM   5113 N N     . PRO A 1 815  ? 165.122 139.750 146.468 1.00 43.77  ? 815  PRO A N     1 
ATOM   5114 C CA    . PRO A 1 815  ? 163.739 139.256 146.340 1.00 46.29  ? 815  PRO A CA    1 
ATOM   5115 C C     . PRO A 1 815  ? 162.735 139.961 147.236 1.00 44.16  ? 815  PRO A C     1 
ATOM   5116 O O     . PRO A 1 815  ? 161.539 139.954 146.919 1.00 38.90  ? 815  PRO A O     1 
ATOM   5117 C CB    . PRO A 1 815  ? 163.861 137.771 146.706 1.00 44.45  ? 815  PRO A CB    1 
ATOM   5118 C CG    . PRO A 1 815  ? 165.275 137.433 146.430 1.00 46.00  ? 815  PRO A CG    1 
ATOM   5119 C CD    . PRO A 1 815  ? 166.048 138.653 146.803 1.00 45.61  ? 815  PRO A CD    1 
ATOM   5120 N N     . GLN A 1 816  ? 163.171 140.565 148.342 1.00 46.11  ? 816  GLN A N     1 
ATOM   5121 C CA    . GLN A 1 816  ? 162.268 141.242 149.265 1.00 36.26  ? 816  GLN A CA    1 
ATOM   5122 C C     . GLN A 1 816  ? 162.592 142.725 149.405 1.00 36.12  ? 816  GLN A C     1 
ATOM   5123 O O     . GLN A 1 816  ? 162.250 143.337 150.420 1.00 38.01  ? 816  GLN A O     1 
ATOM   5124 C CB    . GLN A 1 816  ? 162.297 140.563 150.634 1.00 35.84  ? 816  GLN A CB    1 
ATOM   5125 C CG    . GLN A 1 816  ? 161.999 139.081 150.581 1.00 38.55  ? 816  GLN A CG    1 
ATOM   5126 C CD    . GLN A 1 816  ? 161.968 138.448 151.951 1.00 42.79  ? 816  GLN A CD    1 
ATOM   5127 O OE1   . GLN A 1 816  ? 161.548 139.070 152.925 1.00 39.08  ? 816  GLN A OE1   1 
ATOM   5128 N NE2   . GLN A 1 816  ? 162.420 137.204 152.036 1.00 45.87  ? 816  GLN A NE2   1 
ATOM   5129 N N     . THR A 1 817  ? 163.251 143.310 148.409 1.00 40.12  ? 817  THR A N     1 
ATOM   5130 C CA    . THR A 1 817  ? 163.536 144.738 148.380 1.00 36.83  ? 817  THR A CA    1 
ATOM   5131 C C     . THR A 1 817  ? 163.025 145.309 147.069 1.00 39.92  ? 817  THR A C     1 
ATOM   5132 O O     . THR A 1 817  ? 163.274 144.739 146.003 1.00 43.21  ? 817  THR A O     1 
ATOM   5133 C CB    . THR A 1 817  ? 165.034 145.017 148.519 1.00 37.42  ? 817  THR A CB    1 
ATOM   5134 O OG1   . THR A 1 817  ? 165.560 144.266 149.617 1.00 43.31  ? 817  THR A OG1   1 
ATOM   5135 C CG2   . THR A 1 817  ? 165.277 146.495 148.765 1.00 34.62  ? 817  THR A CG2   1 
ATOM   5136 N N     . LEU A 1 818  ? 162.309 146.426 147.148 1.00 31.70  ? 818  LEU A N     1 
ATOM   5137 C CA    . LEU A 1 818  ? 161.797 147.115 145.968 1.00 32.74  ? 818  LEU A CA    1 
ATOM   5138 C C     . LEU A 1 818  ? 162.431 148.500 145.949 1.00 38.73  ? 818  LEU A C     1 
ATOM   5139 O O     . LEU A 1 818  ? 161.900 149.449 146.530 1.00 41.59  ? 818  LEU A O     1 
ATOM   5140 C CB    . LEU A 1 818  ? 160.282 147.189 145.981 1.00 36.78  ? 818  LEU A CB    1 
ATOM   5141 C CG    . LEU A 1 818  ? 159.636 147.571 144.651 1.00 37.41  ? 818  LEU A CG    1 
ATOM   5142 C CD1   . LEU A 1 818  ? 159.886 146.505 143.598 1.00 28.77  ? 818  LEU A CD1   1 
ATOM   5143 C CD2   . LEU A 1 818  ? 158.161 147.791 144.846 1.00 33.05  ? 818  LEU A CD2   1 
ATOM   5144 N N     . ARG A 1 819  ? 163.572 148.610 145.279 1.00 45.96  ? 819  ARG A N     1 
ATOM   5145 C CA    . ARG A 1 819  ? 164.329 149.850 145.195 1.00 44.81  ? 819  ARG A CA    1 
ATOM   5146 C C     . ARG A 1 819  ? 164.142 150.447 143.809 1.00 53.43  ? 819  ARG A C     1 
ATOM   5147 O O     . ARG A 1 819  ? 164.570 149.856 142.811 1.00 60.58  ? 819  ARG A O     1 
ATOM   5148 C CB    . ARG A 1 819  ? 165.810 149.603 145.481 1.00 48.82  ? 819  ARG A CB    1 
ATOM   5149 C CG    . ARG A 1 819  ? 166.718 150.765 145.132 1.00 48.42  ? 819  ARG A CG    1 
ATOM   5150 C CD    . ARG A 1 819  ? 166.453 151.964 146.014 1.00 46.18  ? 819  ARG A CD    1 
ATOM   5151 N NE    . ARG A 1 819  ? 167.450 153.007 145.816 1.00 55.74  ? 819  ARG A NE    1 
ATOM   5152 C CZ    . ARG A 1 819  ? 167.502 154.134 146.512 1.00 61.62  ? 819  ARG A CZ    1 
ATOM   5153 N NH1   . ARG A 1 819  ? 166.618 154.402 147.459 1.00 55.99  ? 819  ARG A NH1   1 
ATOM   5154 N NH2   . ARG A 1 819  ? 168.464 155.014 146.252 1.00 66.49  ? 819  ARG A NH2   1 
ATOM   5155 N N     . ARG A 1 820  ? 163.504 151.610 143.751 1.00 51.89  ? 820  ARG A N     1 
ATOM   5156 C CA    . ARG A 1 820  ? 163.302 152.334 142.507 1.00 51.98  ? 820  ARG A CA    1 
ATOM   5157 C C     . ARG A 1 820  ? 163.674 153.792 142.720 1.00 54.41  ? 820  ARG A C     1 
ATOM   5158 O O     . ARG A 1 820  ? 163.327 154.388 143.744 1.00 52.69  ? 820  ARG A O     1 
ATOM   5159 C CB    . ARG A 1 820  ? 161.855 152.207 142.019 1.00 45.50  ? 820  ARG A CB    1 
ATOM   5160 C CG    . ARG A 1 820  ? 161.467 150.781 141.658 1.00 40.90  ? 820  ARG A CG    1 
ATOM   5161 C CD    . ARG A 1 820  ? 159.973 150.629 141.447 1.00 44.38  ? 820  ARG A CD    1 
ATOM   5162 N NE    . ARG A 1 820  ? 159.218 150.998 142.637 1.00 43.10  ? 820  ARG A NE    1 
ATOM   5163 C CZ    . ARG A 1 820  ? 157.926 150.756 142.809 1.00 41.64  ? 820  ARG A CZ    1 
ATOM   5164 N NH1   . ARG A 1 820  ? 157.215 150.120 141.893 1.00 43.56  ? 820  ARG A NH1   1 
ATOM   5165 N NH2   . ARG A 1 820  ? 157.334 151.159 143.929 1.00 36.46  ? 820  ARG A NH2   1 
ATOM   5166 N N     . THR A 1 821  ? 164.394 154.354 141.759 1.00 57.85  ? 821  THR A N     1 
ATOM   5167 C CA    . THR A 1 821  ? 164.861 155.730 141.818 1.00 59.70  ? 821  THR A CA    1 
ATOM   5168 C C     . THR A 1 821  ? 164.052 156.596 140.861 1.00 58.72  ? 821  THR A C     1 
ATOM   5169 O O     . THR A 1 821  ? 163.297 156.103 140.020 1.00 57.95  ? 821  THR A O     1 
ATOM   5170 C CB    . THR A 1 821  ? 166.356 155.808 141.487 1.00 61.15  ? 821  THR A CB    1 
ATOM   5171 O OG1   . THR A 1 821  ? 166.619 155.067 140.289 1.00 56.83  ? 821  THR A OG1   1 
ATOM   5172 C CG2   . THR A 1 821  ? 167.183 155.230 142.624 1.00 56.77  ? 821  THR A CG2   1 
ATOM   5173 N N     . LYS A 1 822  ? 164.218 157.912 141.004 1.00 58.97  ? 822  LYS A N     1 
ATOM   5174 C CA    . LYS A 1 822  ? 163.490 158.852 140.161 1.00 62.33  ? 822  LYS A CA    1 
ATOM   5175 C C     . LYS A 1 822  ? 163.951 158.821 138.711 1.00 59.15  ? 822  LYS A C     1 
ATOM   5176 O O     . LYS A 1 822  ? 163.207 159.272 137.834 1.00 60.92  ? 822  LYS A O     1 
ATOM   5177 C CB    . LYS A 1 822  ? 163.624 160.269 140.722 1.00 62.40  ? 822  LYS A CB    1 
ATOM   5178 C CG    . LYS A 1 822  ? 163.437 160.350 142.227 1.00 62.76  ? 822  LYS A CG    1 
ATOM   5179 C CD    . LYS A 1 822  ? 163.131 161.765 142.681 1.00 57.59  ? 822  LYS A CD    1 
ATOM   5180 C CE    . LYS A 1 822  ? 161.765 162.211 142.192 1.00 61.86  ? 822  LYS A CE    1 
ATOM   5181 N NZ    . LYS A 1 822  ? 161.391 163.551 142.720 1.00 60.81  ? 822  LYS A NZ    1 
ATOM   5182 N N     . GLU A 1 823  ? 165.153 158.309 138.438 1.00 57.37  ? 823  GLU A N     1 
ATOM   5183 C CA    . GLU A 1 823  ? 165.605 158.166 137.060 1.00 57.61  ? 823  GLU A CA    1 
ATOM   5184 C C     . GLU A 1 823  ? 164.950 156.978 136.367 1.00 62.22  ? 823  GLU A C     1 
ATOM   5185 O O     . GLU A 1 823  ? 164.721 157.025 135.154 1.00 59.82  ? 823  GLU A O     1 
ATOM   5186 C CB    . GLU A 1 823  ? 167.130 158.041 137.019 1.00 56.46  ? 823  GLU A CB    1 
ATOM   5187 C CG    . GLU A 1 823  ? 167.702 156.940 137.898 1.00 63.64  ? 823  GLU A CG    1 
ATOM   5188 C CD    . GLU A 1 823  ? 167.899 155.633 137.153 1.00 69.88  ? 823  GLU A CD    1 
ATOM   5189 O OE1   . GLU A 1 823  ? 167.748 155.623 135.913 1.00 70.35  ? 823  GLU A OE1   1 
ATOM   5190 O OE2   . GLU A 1 823  ? 168.210 154.616 137.807 1.00 65.76  ? 823  GLU A OE2   1 
ATOM   5191 N N     . GLU A 1 824  ? 164.646 155.912 137.112 1.00 62.82  ? 824  GLU A N     1 
ATOM   5192 C CA    . GLU A 1 824  ? 163.934 154.782 136.528 1.00 57.82  ? 824  GLU A CA    1 
ATOM   5193 C C     . GLU A 1 824  ? 162.499 155.146 136.175 1.00 60.23  ? 824  GLU A C     1 
ATOM   5194 O O     . GLU A 1 824  ? 161.937 154.599 135.220 1.00 65.07  ? 824  GLU A O     1 
ATOM   5195 C CB    . GLU A 1 824  ? 163.944 153.593 137.489 1.00 57.99  ? 824  GLU A CB    1 
ATOM   5196 C CG    . GLU A 1 824  ? 165.322 153.155 137.945 1.00 67.28  ? 824  GLU A CG    1 
ATOM   5197 C CD    . GLU A 1 824  ? 165.269 151.973 138.893 1.00 71.45  ? 824  GLU A CD    1 
ATOM   5198 O OE1   . GLU A 1 824  ? 164.229 151.283 138.926 1.00 69.10  ? 824  GLU A OE1   1 
ATOM   5199 O OE2   . GLU A 1 824  ? 166.264 151.735 139.609 1.00 72.02  ? 824  GLU A OE2   1 
ATOM   5200 N N     . VAL A 1 825  ? 161.895 156.060 136.930 1.00 58.93  ? 825  VAL A N     1 
ATOM   5201 C CA    . VAL A 1 825  ? 160.489 156.407 136.760 1.00 58.00  ? 825  VAL A CA    1 
ATOM   5202 C C     . VAL A 1 825  ? 160.378 157.832 136.237 1.00 63.59  ? 825  VAL A C     1 
ATOM   5203 O O     . VAL A 1 825  ? 159.396 158.533 136.508 1.00 68.17  ? 825  VAL A O     1 
ATOM   5204 C CB    . VAL A 1 825  ? 159.722 156.231 138.081 1.00 53.90  ? 825  VAL A CB    1 
ATOM   5205 C CG1   . VAL A 1 825  ? 159.798 154.786 138.532 1.00 51.93  ? 825  VAL A CG1   1 
ATOM   5206 C CG2   . VAL A 1 825  ? 160.295 157.138 139.148 1.00 56.86  ? 825  VAL A CG2   1 
ATOM   5207 N N     . ALA A 1 826  ? 161.378 158.263 135.468 1.00 63.61  ? 826  ALA A N     1 
ATOM   5208 C CA    . ALA A 1 826  ? 161.460 159.627 134.970 1.00 62.75  ? 826  ALA A CA    1 
ATOM   5209 C C     . ALA A 1 826  ? 160.352 159.963 133.977 1.00 66.35  ? 826  ALA A C     1 
ATOM   5210 O O     . ALA A 1 826  ? 160.154 161.142 133.663 1.00 72.03  ? 826  ALA A O     1 
ATOM   5211 C CB    . ALA A 1 826  ? 162.829 159.869 134.330 1.00 60.58  ? 826  ALA A CB    1 
ATOM   5212 N N     . ARG A 1 827  ? 159.625 158.961 133.486 1.00 69.28  ? 827  ARG A N     1 
ATOM   5213 C CA    . ARG A 1 827  ? 158.496 159.203 132.597 1.00 70.39  ? 827  ARG A CA    1 
ATOM   5214 C C     . ARG A 1 827  ? 157.190 159.423 133.346 1.00 68.38  ? 827  ARG A C     1 
ATOM   5215 O O     . ARG A 1 827  ? 156.302 160.110 132.830 1.00 70.25  ? 827  ARG A O     1 
ATOM   5216 C CB    . ARG A 1 827  ? 158.335 158.042 131.607 1.00 71.50  ? 827  ARG A CB    1 
ATOM   5217 C CG    . ARG A 1 827  ? 158.019 156.692 132.236 1.00 75.37  ? 827  ARG A CG    1 
ATOM   5218 C CD    . ARG A 1 827  ? 156.539 156.357 132.114 1.00 78.02  ? 827  ARG A CD    1 
ATOM   5219 N NE    . ARG A 1 827  ? 156.238 155.015 132.596 1.00 81.33  ? 827  ARG A NE    1 
ATOM   5220 C CZ    . ARG A 1 827  ? 156.218 153.932 131.832 1.00 81.63  ? 827  ARG A CZ    1 
ATOM   5221 N NH1   . ARG A 1 827  ? 156.475 153.995 130.536 1.00 75.15  ? 827  ARG A NH1   1 
ATOM   5222 N NH2   . ARG A 1 827  ? 155.933 152.755 132.382 1.00 79.09  ? 827  ARG A NH2   1 
ATOM   5223 N N     . ASP A 1 828  ? 157.050 158.860 134.545 1.00 67.65  ? 828  ASP A N     1 
ATOM   5224 C CA    . ASP A 1 828  ? 155.913 159.158 135.414 1.00 70.77  ? 828  ASP A CA    1 
ATOM   5225 C C     . ASP A 1 828  ? 156.282 160.320 136.335 1.00 67.02  ? 828  ASP A C     1 
ATOM   5226 O O     . ASP A 1 828  ? 156.111 160.282 137.554 1.00 57.53  ? 828  ASP A O     1 
ATOM   5227 C CB    . ASP A 1 828  ? 155.508 157.918 136.206 1.00 70.19  ? 828  ASP A CB    1 
ATOM   5228 C CG    . ASP A 1 828  ? 154.973 156.809 135.324 1.00 74.67  ? 828  ASP A CG    1 
ATOM   5229 O OD1   . ASP A 1 828  ? 154.261 157.114 134.346 1.00 72.64  ? 828  ASP A OD1   1 
ATOM   5230 O OD2   . ASP A 1 828  ? 155.267 155.630 135.612 1.00 71.75  ? 828  ASP A OD2   1 
ATOM   5231 N N     . LEU A 1 829  ? 156.789 161.375 135.704 1.00 69.69  ? 829  LEU A N     1 
ATOM   5232 C CA    . LEU A 1 829  ? 157.323 162.563 136.354 1.00 68.83  ? 829  LEU A CA    1 
ATOM   5233 C C     . LEU A 1 829  ? 157.498 163.648 135.300 1.00 66.58  ? 829  LEU A C     1 
ATOM   5234 O O     . LEU A 1 829  ? 157.523 163.342 134.101 1.00 64.57  ? 829  LEU A O     1 
ATOM   5235 C CB    . LEU A 1 829  ? 158.662 162.259 137.036 1.00 62.87  ? 829  LEU A CB    1 
ATOM   5236 C CG    . LEU A 1 829  ? 158.694 161.774 138.487 1.00 59.91  ? 829  LEU A CG    1 
ATOM   5237 C CD1   . LEU A 1 829  ? 160.082 161.270 138.847 1.00 60.65  ? 829  LEU A CD1   1 
ATOM   5238 C CD2   . LEU A 1 829  ? 158.268 162.881 139.435 1.00 61.99  ? 829  LEU A CD2   1 
ATOM   5239 N N     . PRO A 1 830  ? 157.621 164.918 135.688 1.00 67.28  ? 830  PRO A N     1 
ATOM   5240 C CA    . PRO A 1 830  ? 157.965 165.947 134.698 1.00 63.54  ? 830  PRO A CA    1 
ATOM   5241 C C     . PRO A 1 830  ? 159.400 165.791 134.224 1.00 65.13  ? 830  PRO A C     1 
ATOM   5242 O O     . PRO A 1 830  ? 160.150 164.974 134.767 1.00 66.33  ? 830  PRO A O     1 
ATOM   5243 C CB    . PRO A 1 830  ? 157.757 167.258 135.465 1.00 63.23  ? 830  PRO A CB    1 
ATOM   5244 C CG    . PRO A 1 830  ? 157.941 166.882 136.895 1.00 60.23  ? 830  PRO A CG    1 
ATOM   5245 C CD    . PRO A 1 830  ? 157.373 165.499 137.019 1.00 60.48  ? 830  PRO A CD    1 
ATOM   5246 N N     . GLN A 1 831  ? 159.797 166.559 133.218 1.00 59.41  ? 831  GLN A N     1 
ATOM   5247 C CA    . GLN A 1 831  ? 161.155 166.511 132.699 1.00 52.97  ? 831  GLN A CA    1 
ATOM   5248 C C     . GLN A 1 831  ? 162.025 167.471 133.495 1.00 49.65  ? 831  GLN A C     1 
ATOM   5249 O O     . GLN A 1 831  ? 161.796 168.684 133.474 1.00 55.38  ? 831  GLN A O     1 
ATOM   5250 C CB    . GLN A 1 831  ? 161.192 166.870 131.213 1.00 56.40  ? 831  GLN A CB    1 
ATOM   5251 C CG    . GLN A 1 831  ? 162.584 166.838 130.609 1.00 59.03  ? 831  GLN A CG    1 
ATOM   5252 C CD    . GLN A 1 831  ? 162.595 167.223 129.144 1.00 63.15  ? 831  GLN A CD    1 
ATOM   5253 O OE1   . GLN A 1 831  ? 161.552 167.508 128.556 1.00 65.86  ? 831  GLN A OE1   1 
ATOM   5254 N NE2   . GLN A 1 831  ? 163.780 167.232 128.545 1.00 53.30  ? 831  GLN A NE2   1 
ATOM   5255 N N     . LYS A 1 832  ? 163.018 166.928 134.194 1.00 46.03  ? 832  LYS A N     1 
ATOM   5256 C CA    . LYS A 1 832  ? 163.930 167.721 135.008 1.00 42.67  ? 832  LYS A CA    1 
ATOM   5257 C C     . LYS A 1 832  ? 165.131 168.090 134.149 1.00 44.61  ? 832  LYS A C     1 
ATOM   5258 O O     . LYS A 1 832  ? 165.920 167.221 133.765 1.00 50.06  ? 832  LYS A O     1 
ATOM   5259 C CB    . LYS A 1 832  ? 164.366 166.959 136.256 1.00 39.23  ? 832  LYS A CB    1 
ATOM   5260 C CG    . LYS A 1 832  ? 164.691 167.865 137.426 1.00 41.88  ? 832  LYS A CG    1 
ATOM   5261 C CD    . LYS A 1 832  ? 165.391 167.125 138.548 1.00 42.11  ? 832  LYS A CD    1 
ATOM   5262 C CE    . LYS A 1 832  ? 166.830 166.815 138.185 1.00 42.52  ? 832  LYS A CE    1 
ATOM   5263 N NZ    . LYS A 1 832  ? 167.589 166.287 139.351 1.00 45.16  ? 832  LYS A NZ    1 
ATOM   5264 N N     . ILE A 1 833  ? 165.266 169.375 133.846 1.00 41.83  ? 833  ILE A N     1 
ATOM   5265 C CA    . ILE A 1 833  ? 166.357 169.866 133.017 1.00 39.12  ? 833  ILE A CA    1 
ATOM   5266 C C     . ILE A 1 833  ? 167.358 170.584 133.911 1.00 34.79  ? 833  ILE A C     1 
ATOM   5267 O O     . ILE A 1 833  ? 167.030 171.599 134.533 1.00 40.77  ? 833  ILE A O     1 
ATOM   5268 C CB    . ILE A 1 833  ? 165.838 170.797 131.912 1.00 39.24  ? 833  ILE A CB    1 
ATOM   5269 C CG1   . ILE A 1 833  ? 164.769 170.082 131.084 1.00 43.87  ? 833  ILE A CG1   1 
ATOM   5270 C CG2   . ILE A 1 833  ? 166.987 171.276 131.039 1.00 33.88  ? 833  ILE A CG2   1 
ATOM   5271 C CD1   . ILE A 1 833  ? 164.143 170.945 130.020 1.00 49.23  ? 833  ILE A CD1   1 
ATOM   5272 N N     . GLU A 1 834  ? 168.577 170.060 133.976 1.00 33.83  ? 834  GLU A N     1 
ATOM   5273 C CA    . GLU A 1 834  ? 169.665 170.695 134.708 1.00 35.26  ? 834  GLU A CA    1 
ATOM   5274 C C     . GLU A 1 834  ? 170.386 171.628 133.744 1.00 37.07  ? 834  GLU A C     1 
ATOM   5275 O O     . GLU A 1 834  ? 171.077 171.173 132.827 1.00 34.29  ? 834  GLU A O     1 
ATOM   5276 C CB    . GLU A 1 834  ? 170.617 169.657 135.296 1.00 36.58  ? 834  GLU A CB    1 
ATOM   5277 C CG    . GLU A 1 834  ? 171.842 170.257 135.967 1.00 44.92  ? 834  GLU A CG    1 
ATOM   5278 C CD    . GLU A 1 834  ? 172.754 169.208 136.570 1.00 60.52  ? 834  GLU A CD    1 
ATOM   5279 O OE1   . GLU A 1 834  ? 172.241 168.174 137.047 1.00 57.11  ? 834  GLU A OE1   1 
ATOM   5280 O OE2   . GLU A 1 834  ? 173.985 169.415 136.563 1.00 61.26  ? 834  GLU A OE2   1 
ATOM   5281 N N     . VAL A 1 835  ? 170.217 172.933 133.949 1.00 39.70  ? 835  VAL A N     1 
ATOM   5282 C CA    . VAL A 1 835  ? 170.759 173.916 133.021 1.00 35.31  ? 835  VAL A CA    1 
ATOM   5283 C C     . VAL A 1 835  ? 172.273 173.962 133.156 1.00 38.06  ? 835  VAL A C     1 
ATOM   5284 O O     . VAL A 1 835  ? 172.814 174.063 134.264 1.00 41.67  ? 835  VAL A O     1 
ATOM   5285 C CB    . VAL A 1 835  ? 170.126 175.291 133.271 1.00 32.62  ? 835  VAL A CB    1 
ATOM   5286 C CG1   . VAL A 1 835  ? 170.603 176.292 132.236 1.00 37.16  ? 835  VAL A CG1   1 
ATOM   5287 C CG2   . VAL A 1 835  ? 168.613 175.178 133.248 1.00 30.03  ? 835  VAL A CG2   1 
ATOM   5288 N N     . GLU A 1 836  ? 172.967 173.876 132.022 1.00 38.40  ? 836  GLU A N     1 
ATOM   5289 C CA    . GLU A 1 836  ? 174.422 173.894 132.003 1.00 43.91  ? 836  GLU A CA    1 
ATOM   5290 C C     . GLU A 1 836  ? 174.994 175.299 131.872 1.00 44.79  ? 836  GLU A C     1 
ATOM   5291 O O     . GLU A 1 836  ? 176.141 175.527 132.272 1.00 49.29  ? 836  GLU A O     1 
ATOM   5292 C CB    . GLU A 1 836  ? 174.937 173.016 130.855 1.00 47.40  ? 836  GLU A CB    1 
ATOM   5293 C CG    . GLU A 1 836  ? 176.446 172.819 130.819 1.00 54.50  ? 836  GLU A CG    1 
ATOM   5294 C CD    . GLU A 1 836  ? 176.967 172.029 132.003 1.00 61.41  ? 836  GLU A CD    1 
ATOM   5295 O OE1   . GLU A 1 836  ? 176.190 171.248 132.591 1.00 59.98  ? 836  GLU A OE1   1 
ATOM   5296 O OE2   . GLU A 1 836  ? 178.157 172.190 132.347 1.00 58.74  ? 836  GLU A OE2   1 
ATOM   5297 N N     . SER A 1 837  ? 174.219 176.245 131.336 1.00 41.40  ? 837  SER A N     1 
ATOM   5298 C CA    . SER A 1 837  ? 174.727 177.598 131.140 1.00 40.84  ? 837  SER A CA    1 
ATOM   5299 C C     . SER A 1 837  ? 175.047 178.278 132.463 1.00 41.53  ? 837  SER A C     1 
ATOM   5300 O O     . SER A 1 837  ? 175.984 179.082 132.537 1.00 44.87  ? 837  SER A O     1 
ATOM   5301 C CB    . SER A 1 837  ? 173.712 178.427 130.353 1.00 48.38  ? 837  SER A CB    1 
ATOM   5302 O OG    . SER A 1 837  ? 173.327 177.765 129.161 1.00 53.64  ? 837  SER A OG    1 
ATOM   5303 N N     . CYS A 1 838  ? 174.286 177.973 133.515 1.00 43.67  ? 838  CYS A N     1 
ATOM   5304 C CA    . CYS A 1 838  ? 174.508 178.601 134.811 1.00 40.83  ? 838  CYS A CA    1 
ATOM   5305 C C     . CYS A 1 838  ? 175.791 178.130 135.479 1.00 38.15  ? 838  CYS A C     1 
ATOM   5306 O O     . CYS A 1 838  ? 176.312 178.831 136.352 1.00 45.50  ? 838  CYS A O     1 
ATOM   5307 C CB    . CYS A 1 838  ? 173.322 178.329 135.735 1.00 34.82  ? 838  CYS A CB    1 
ATOM   5308 S SG    . CYS A 1 838  ? 173.039 176.587 136.099 1.00 40.15  ? 838  CYS A SG    1 
ATOM   5309 N N     . LYS A 1 839  ? 176.315 176.974 135.089 1.00 39.49  ? 839  LYS A N     1 
ATOM   5310 C CA    . LYS A 1 839  ? 177.471 176.386 135.749 1.00 40.16  ? 839  LYS A CA    1 
ATOM   5311 C C     . LYS A 1 839  ? 178.794 176.871 135.176 1.00 45.87  ? 839  LYS A C     1 
ATOM   5312 O O     . LYS A 1 839  ? 179.849 176.385 135.595 1.00 49.42  ? 839  LYS A O     1 
ATOM   5313 C CB    . LYS A 1 839  ? 177.397 174.858 135.665 1.00 42.07  ? 839  LYS A CB    1 
ATOM   5314 C CG    . LYS A 1 839  ? 175.996 174.309 135.871 1.00 39.00  ? 839  LYS A CG    1 
ATOM   5315 C CD    . LYS A 1 839  ? 176.006 172.825 136.182 1.00 39.72  ? 839  LYS A CD    1 
ATOM   5316 C CE    . LYS A 1 839  ? 176.590 172.561 137.558 1.00 47.83  ? 839  LYS A CE    1 
ATOM   5317 N NZ    . LYS A 1 839  ? 176.492 171.126 137.944 1.00 49.39  ? 839  LYS A NZ    1 
ATOM   5318 N N     . GLN A 1 840  ? 178.768 177.818 134.239 1.00 48.30  ? 840  GLN A N     1 
ATOM   5319 C CA    . GLN A 1 840  ? 179.969 178.299 133.568 1.00 48.34  ? 840  GLN A CA    1 
ATOM   5320 C C     . GLN A 1 840  ? 180.285 179.750 133.921 1.00 49.44  ? 840  GLN A C     1 
ATOM   5321 O O     . GLN A 1 840  ? 180.888 180.469 133.122 1.00 53.45  ? 840  GLN A O     1 
ATOM   5322 C CB    . GLN A 1 840  ? 179.830 178.140 132.055 1.00 50.91  ? 840  GLN A CB    1 
ATOM   5323 C CG    . GLN A 1 840  ? 179.331 176.772 131.613 1.00 49.97  ? 840  GLN A CG    1 
ATOM   5324 C CD    . GLN A 1 840  ? 180.275 175.650 131.994 1.00 59.33  ? 840  GLN A CD    1 
ATOM   5325 O OE1   . GLN A 1 840  ? 181.485 175.850 132.108 1.00 62.59  ? 840  GLN A OE1   1 
ATOM   5326 N NE2   . GLN A 1 840  ? 179.726 174.459 132.196 1.00 56.67  ? 840  GLN A NE2   1 
ATOM   5327 N N     . LEU A 1 841  ? 179.880 180.195 135.108 1.00 42.30  ? 841  LEU A N     1 
ATOM   5328 C CA    . LEU A 1 841  ? 180.159 181.559 135.527 1.00 38.96  ? 841  LEU A CA    1 
ATOM   5329 C C     . LEU A 1 841  ? 181.641 181.724 135.852 1.00 42.34  ? 841  LEU A C     1 
ATOM   5330 O O     . LEU A 1 841  ? 182.346 180.764 136.173 1.00 48.40  ? 841  LEU A O     1 
ATOM   5331 C CB    . LEU A 1 841  ? 179.302 181.937 136.735 1.00 37.95  ? 841  LEU A CB    1 
ATOM   5332 C CG    . LEU A 1 841  ? 177.793 181.752 136.563 1.00 33.87  ? 841  LEU A CG    1 
ATOM   5333 C CD1   . LEU A 1 841  ? 177.047 182.207 137.804 1.00 32.95  ? 841  LEU A CD1   1 
ATOM   5334 C CD2   . LEU A 1 841  ? 177.291 182.488 135.334 1.00 32.32  ? 841  LEU A CD2   1 
ATOM   5335 N N     . THR A 1 842  ? 182.113 182.964 135.764 1.00 43.15  ? 842  THR A N     1 
ATOM   5336 C CA    . THR A 1 842  ? 183.530 183.272 135.884 1.00 50.07  ? 842  THR A CA    1 
ATOM   5337 C C     . THR A 1 842  ? 183.774 184.246 137.028 1.00 52.24  ? 842  THR A C     1 
ATOM   5338 O O     . THR A 1 842  ? 183.041 185.226 137.190 1.00 50.92  ? 842  THR A O     1 
ATOM   5339 C CB    . THR A 1 842  ? 184.071 183.861 134.577 1.00 51.02  ? 842  THR A CB    1 
ATOM   5340 O OG1   . THR A 1 842  ? 183.669 183.034 133.478 1.00 54.47  ? 842  THR A OG1   1 
ATOM   5341 C CG2   . THR A 1 842  ? 185.589 183.939 134.611 1.00 49.92  ? 842  THR A CG2   1 
ATOM   5342 N N     . LEU A 1 843  ? 184.808 183.968 137.823 1.00 50.68  ? 843  LEU A N     1 
ATOM   5343 C CA    . LEU A 1 843  ? 185.240 184.906 138.850 1.00 50.04  ? 843  LEU A CA    1 
ATOM   5344 C C     . LEU A 1 843  ? 185.635 186.233 138.220 1.00 56.87  ? 843  LEU A C     1 
ATOM   5345 O O     . LEU A 1 843  ? 186.370 186.270 137.229 1.00 60.20  ? 843  LEU A O     1 
ATOM   5346 C CB    . LEU A 1 843  ? 186.429 184.338 139.629 1.00 52.91  ? 843  LEU A CB    1 
ATOM   5347 C CG    . LEU A 1 843  ? 186.248 183.309 140.744 1.00 54.71  ? 843  LEU A CG    1 
ATOM   5348 C CD1   . LEU A 1 843  ? 187.608 182.885 141.263 1.00 49.49  ? 843  LEU A CD1   1 
ATOM   5349 C CD2   . LEU A 1 843  ? 185.414 183.874 141.873 1.00 50.44  ? 843  LEU A CD2   1 
ATOM   5350 N N     . SER A 1 844  ? 185.147 187.326 138.795 1.00 53.75  ? 844  SER A N     1 
ATOM   5351 C CA    . SER A 1 844  ? 185.632 188.633 138.390 1.00 55.21  ? 844  SER A CA    1 
ATOM   5352 C C     . SER A 1 844  ? 187.014 188.872 138.986 1.00 59.98  ? 844  SER A C     1 
ATOM   5353 O O     . SER A 1 844  ? 187.451 188.172 139.902 1.00 62.32  ? 844  SER A O     1 
ATOM   5354 C CB    . SER A 1 844  ? 184.664 189.733 138.825 1.00 56.56  ? 844  SER A CB    1 
ATOM   5355 O OG    . SER A 1 844  ? 184.524 189.765 140.233 1.00 59.23  ? 844  SER A OG    1 
ATOM   5356 N N     . GLY A 1 845  ? 187.712 189.872 138.444 1.00 60.29  ? 845  GLY A N     1 
ATOM   5357 C CA    . GLY A 1 845  ? 189.038 190.184 138.952 1.00 65.63  ? 845  GLY A CA    1 
ATOM   5358 C C     . GLY A 1 845  ? 189.025 190.540 140.425 1.00 67.34  ? 845  GLY A C     1 
ATOM   5359 O O     . GLY A 1 845  ? 189.883 190.095 141.191 1.00 66.22  ? 845  GLY A O     1 
ATOM   5360 N N     . VAL A 1 846  ? 188.039 191.334 140.844 1.00 66.25  ? 846  VAL A N     1 
ATOM   5361 C CA    . VAL A 1 846  ? 187.910 191.692 142.253 1.00 66.68  ? 846  VAL A CA    1 
ATOM   5362 C C     . VAL A 1 846  ? 187.579 190.460 143.088 1.00 65.46  ? 846  VAL A C     1 
ATOM   5363 O O     . VAL A 1 846  ? 188.171 190.231 144.150 1.00 71.11  ? 846  VAL A O     1 
ATOM   5364 C CB    . VAL A 1 846  ? 186.851 192.796 142.421 1.00 70.53  ? 846  VAL A CB    1 
ATOM   5365 C CG1   . VAL A 1 846  ? 186.808 193.275 143.851 1.00 76.72  ? 846  VAL A CG1   1 
ATOM   5366 C CG2   . VAL A 1 846  ? 187.144 193.952 141.480 1.00 76.04  ? 846  VAL A CG2   1 
ATOM   5367 N N     . GLN A 1 847  ? 186.633 189.646 142.618 1.00 58.35  ? 847  GLN A N     1 
ATOM   5368 C CA    . GLN A 1 847  ? 186.272 188.430 143.341 1.00 54.43  ? 847  GLN A CA    1 
ATOM   5369 C C     . GLN A 1 847  ? 187.434 187.444 143.379 1.00 58.23  ? 847  GLN A C     1 
ATOM   5370 O O     . GLN A 1 847  ? 187.688 186.813 144.413 1.00 60.35  ? 847  GLN A O     1 
ATOM   5371 C CB    . GLN A 1 847  ? 185.042 187.793 142.698 1.00 54.82  ? 847  GLN A CB    1 
ATOM   5372 C CG    . GLN A 1 847  ? 184.267 186.855 143.598 1.00 51.94  ? 847  GLN A CG    1 
ATOM   5373 C CD    . GLN A 1 847  ? 183.043 186.288 142.912 1.00 45.51  ? 847  GLN A CD    1 
ATOM   5374 O OE1   . GLN A 1 847  ? 182.980 186.228 141.687 1.00 48.27  ? 847  GLN A OE1   1 
ATOM   5375 N NE2   . GLN A 1 847  ? 182.058 185.877 143.700 1.00 43.74  ? 847  GLN A NE2   1 
ATOM   5376 N N     . LYS A 1 848  ? 188.151 187.301 142.261 1.00 60.18  ? 848  LYS A N     1 
ATOM   5377 C CA    . LYS A 1 848  ? 189.299 186.402 142.223 1.00 59.92  ? 848  LYS A CA    1 
ATOM   5378 C C     . LYS A 1 848  ? 190.384 186.853 143.192 1.00 62.37  ? 848  LYS A C     1 
ATOM   5379 O O     . LYS A 1 848  ? 190.958 186.036 143.922 1.00 65.07  ? 848  LYS A O     1 
ATOM   5380 C CB    . LYS A 1 848  ? 189.856 186.316 140.802 1.00 64.22  ? 848  LYS A CB    1 
ATOM   5381 C CG    . LYS A 1 848  ? 191.219 185.648 140.716 1.00 67.19  ? 848  LYS A CG    1 
ATOM   5382 C CD    . LYS A 1 848  ? 191.775 185.696 139.304 1.00 66.75  ? 848  LYS A CD    1 
ATOM   5383 C CE    . LYS A 1 848  ? 193.191 185.148 139.254 1.00 67.62  ? 848  LYS A CE    1 
ATOM   5384 N NZ    . LYS A 1 848  ? 193.261 183.747 139.753 1.00 73.63  ? 848  LYS A NZ    1 
ATOM   5385 N N     . GLN A 1 849  ? 190.683 188.155 143.212 1.00 62.67  ? 849  GLN A N     1 
ATOM   5386 C CA    . GLN A 1 849  ? 191.721 188.634 144.116 1.00 63.59  ? 849  GLN A CA    1 
ATOM   5387 C C     . GLN A 1 849  ? 191.285 188.521 145.571 1.00 64.61  ? 849  GLN A C     1 
ATOM   5388 O O     . GLN A 1 849  ? 192.112 188.215 146.435 1.00 67.43  ? 849  GLN A O     1 
ATOM   5389 C CB    . GLN A 1 849  ? 192.124 190.071 143.764 1.00 64.44  ? 849  GLN A CB    1 
ATOM   5390 C CG    . GLN A 1 849  ? 191.118 191.158 144.113 1.00 69.91  ? 849  GLN A CG    1 
ATOM   5391 C CD    . GLN A 1 849  ? 191.300 191.704 145.518 1.00 78.68  ? 849  GLN A CD    1 
ATOM   5392 O OE1   . GLN A 1 849  ? 192.290 191.411 146.187 1.00 81.22  ? 849  GLN A OE1   1 
ATOM   5393 N NE2   . GLN A 1 849  ? 190.340 192.502 145.972 1.00 75.55  ? 849  GLN A NE2   1 
ATOM   5394 N N     . LEU A 1 850  ? 189.998 188.734 145.862 1.00 64.67  ? 850  LEU A N     1 
ATOM   5395 C CA    . LEU A 1 850  ? 189.516 188.541 147.226 1.00 60.59  ? 850  LEU A CA    1 
ATOM   5396 C C     . LEU A 1 850  ? 189.651 187.086 147.656 1.00 61.18  ? 850  LEU A C     1 
ATOM   5397 O O     . LEU A 1 850  ? 190.086 186.800 148.777 1.00 65.36  ? 850  LEU A O     1 
ATOM   5398 C CB    . LEU A 1 850  ? 188.063 188.999 147.343 1.00 59.83  ? 850  LEU A CB    1 
ATOM   5399 C CG    . LEU A 1 850  ? 187.436 188.866 148.733 1.00 60.52  ? 850  LEU A CG    1 
ATOM   5400 C CD1   . LEU A 1 850  ? 188.032 189.880 149.693 1.00 64.63  ? 850  LEU A CD1   1 
ATOM   5401 C CD2   . LEU A 1 850  ? 185.924 189.003 148.668 1.00 61.01  ? 850  LEU A CD2   1 
ATOM   5402 N N     . TYR A 1 851  ? 189.290 186.150 146.775 1.00 62.74  ? 851  TYR A N     1 
ATOM   5403 C CA    . TYR A 1 851  ? 189.427 184.743 147.114 1.00 60.54  ? 851  TYR A CA    1 
ATOM   5404 C C     . TYR A 1 851  ? 190.873 184.330 147.316 1.00 64.05  ? 851  TYR A C     1 
ATOM   5405 O O     . TYR A 1 851  ? 191.198 183.606 148.263 1.00 69.28  ? 851  TYR A O     1 
ATOM   5406 N N     . LEU A 1 852  ? 191.762 184.788 146.431 1.00 64.92  ? 852  LEU A N     1 
ATOM   5407 C CA    . LEU A 1 852  ? 193.179 184.472 146.578 1.00 63.87  ? 852  LEU A CA    1 
ATOM   5408 C C     . LEU A 1 852  ? 193.747 185.068 147.859 1.00 68.78  ? 852  LEU A C     1 
ATOM   5409 O O     . LEU A 1 852  ? 194.531 184.416 148.558 1.00 72.58  ? 852  LEU A O     1 
ATOM   5410 C CB    . LEU A 1 852  ? 193.962 184.968 145.362 1.00 62.67  ? 852  LEU A CB    1 
ATOM   5411 C CG    . LEU A 1 852  ? 193.684 184.265 144.033 1.00 64.11  ? 852  LEU A CG    1 
ATOM   5412 C CD1   . LEU A 1 852  ? 194.623 184.780 142.954 1.00 62.70  ? 852  LEU A CD1   1 
ATOM   5413 C CD2   . LEU A 1 852  ? 193.806 182.757 144.180 1.00 63.28  ? 852  LEU A CD2   1 
ATOM   5414 N N     . SER A 1 853  ? 193.363 186.305 148.187 1.00 68.69  ? 853  SER A N     1 
ATOM   5415 C CA    . SER A 1 853  ? 193.827 186.921 149.425 1.00 67.17  ? 853  SER A CA    1 
ATOM   5416 C C     . SER A 1 853  ? 193.328 186.154 150.641 1.00 73.10  ? 853  SER A C     1 
ATOM   5417 O O     . SER A 1 853  ? 194.076 185.952 151.603 1.00 81.50  ? 853  SER A O     1 
ATOM   5418 C CB    . SER A 1 853  ? 193.375 188.379 149.489 1.00 65.70  ? 853  SER A CB    1 
ATOM   5419 O OG    . SER A 1 853  ? 193.868 189.117 148.385 1.00 71.62  ? 853  SER A OG    1 
ATOM   5420 N N     . SER A 1 854  ? 192.066 185.719 150.617 1.00 69.35  ? 854  SER A N     1 
ATOM   5421 C CA    . SER A 1 854  ? 191.530 184.953 151.738 1.00 69.64  ? 854  SER A CA    1 
ATOM   5422 C C     . SER A 1 854  ? 192.281 183.640 151.913 1.00 74.13  ? 854  SER A C     1 
ATOM   5423 O O     . SER A 1 854  ? 192.654 183.267 153.033 1.00 80.22  ? 854  SER A O     1 
ATOM   5424 C CB    . SER A 1 854  ? 190.038 184.696 151.528 1.00 65.24  ? 854  SER A CB    1 
ATOM   5425 O OG    . SER A 1 854  ? 189.317 185.914 151.470 1.00 67.24  ? 854  SER A OG    1 
ATOM   5426 N N     . VAL A 1 855  ? 192.519 182.926 150.810 1.00 74.17  ? 855  VAL A N     1 
ATOM   5427 C CA    . VAL A 1 855  ? 193.224 181.649 150.894 1.00 75.93  ? 855  VAL A CA    1 
ATOM   5428 C C     . VAL A 1 855  ? 194.649 181.859 151.390 1.00 79.20  ? 855  VAL A C     1 
ATOM   5429 O O     . VAL A 1 855  ? 195.148 181.100 152.232 1.00 82.77  ? 855  VAL A O     1 
ATOM   5430 C CB    . VAL A 1 855  ? 193.190 180.928 149.534 1.00 76.19  ? 855  VAL A CB    1 
ATOM   5431 C CG1   . VAL A 1 855  ? 194.061 179.683 149.568 1.00 81.52  ? 855  VAL A CG1   1 
ATOM   5432 C CG2   . VAL A 1 855  ? 191.762 180.560 149.168 1.00 68.29  ? 855  VAL A CG2   1 
ATOM   5433 N N     . ALA A 1 856  ? 195.324 182.895 150.885 1.00 78.47  ? 856  ALA A N     1 
ATOM   5434 C CA    . ALA A 1 856  ? 196.690 183.176 151.313 1.00 82.14  ? 856  ALA A CA    1 
ATOM   5435 C C     . ALA A 1 856  ? 196.748 183.529 152.794 1.00 87.96  ? 856  ALA A C     1 
ATOM   5436 O O     . ALA A 1 856  ? 197.642 183.068 153.513 1.00 91.47  ? 856  ALA A O     1 
ATOM   5437 C CB    . ALA A 1 856  ? 197.281 184.304 150.469 1.00 73.91  ? 856  ALA A CB    1 
ATOM   5438 N N     . ASN A 1 857  ? 195.807 184.349 153.269 1.00 83.68  ? 857  ASN A N     1 
ATOM   5439 C CA    . ASN A 1 857  ? 195.790 184.713 154.681 1.00 86.07  ? 857  ASN A CA    1 
ATOM   5440 C C     . ASN A 1 857  ? 195.521 183.499 155.560 1.00 87.39  ? 857  ASN A C     1 
ATOM   5441 O O     . ASN A 1 857  ? 196.142 183.341 156.618 1.00 93.53  ? 857  ASN A O     1 
ATOM   5442 C CB    . ASN A 1 857  ? 194.747 185.801 154.933 1.00 83.07  ? 857  ASN A CB    1 
ATOM   5443 C CG    . ASN A 1 857  ? 195.080 187.099 154.227 1.00 85.72  ? 857  ASN A CG    1 
ATOM   5444 O OD1   . ASN A 1 857  ? 196.246 187.392 153.958 1.00 89.60  ? 857  ASN A OD1   1 
ATOM   5445 N ND2   . ASN A 1 857  ? 194.056 187.887 153.923 1.00 76.24  ? 857  ASN A ND2   1 
ATOM   5446 N N     . TRP A 1 858  ? 194.598 182.630 155.141 1.00 83.70  ? 858  TRP A N     1 
ATOM   5447 C CA    . TRP A 1 858  ? 194.324 181.427 155.920 1.00 85.86  ? 858  TRP A CA    1 
ATOM   5448 C C     . TRP A 1 858  ? 195.544 180.516 155.973 1.00 90.41  ? 858  TRP A C     1 
ATOM   5449 O O     . TRP A 1 858  ? 195.872 179.965 157.032 1.00 94.06  ? 858  TRP A O     1 
ATOM   5450 C CB    . TRP A 1 858  ? 193.123 180.684 155.339 1.00 81.94  ? 858  TRP A CB    1 
ATOM   5451 C CG    . TRP A 1 858  ? 192.680 179.527 156.177 1.00 82.45  ? 858  TRP A CG    1 
ATOM   5452 C CD1   . TRP A 1 858  ? 191.762 179.550 157.186 1.00 79.53  ? 858  TRP A CD1   1 
ATOM   5453 C CD2   . TRP A 1 858  ? 193.137 178.174 156.081 1.00 82.59  ? 858  TRP A CD2   1 
ATOM   5454 N NE1   . TRP A 1 858  ? 191.616 178.295 157.722 1.00 79.62  ? 858  TRP A NE1   1 
ATOM   5455 C CE2   . TRP A 1 858  ? 192.450 177.431 157.062 1.00 81.43  ? 858  TRP A CE2   1 
ATOM   5456 C CE3   . TRP A 1 858  ? 194.058 177.517 155.261 1.00 83.65  ? 858  TRP A CE3   1 
ATOM   5457 C CZ2   . TRP A 1 858  ? 192.656 176.067 157.244 1.00 80.96  ? 858  TRP A CZ2   1 
ATOM   5458 C CZ3   . TRP A 1 858  ? 194.261 176.163 155.445 1.00 87.29  ? 858  TRP A CZ3   1 
ATOM   5459 C CH2   . TRP A 1 858  ? 193.563 175.452 156.427 1.00 85.40  ? 858  TRP A CH2   1 
ATOM   5460 N N     . GLN A 1 859  ? 196.233 180.348 154.841 1.00 90.80  ? 859  GLN A N     1 
ATOM   5461 C CA    . GLN A 1 859  ? 197.432 179.515 154.825 1.00 91.23  ? 859  GLN A CA    1 
ATOM   5462 C C     . GLN A 1 859  ? 198.535 180.112 155.691 1.00 94.70  ? 859  GLN A C     1 
ATOM   5463 O O     . GLN A 1 859  ? 199.245 179.379 156.389 1.00 96.06  ? 859  GLN A O     1 
ATOM   5464 C CB    . GLN A 1 859  ? 197.920 179.318 153.391 1.00 90.50  ? 859  GLN A CB    1 
ATOM   5465 C CG    . GLN A 1 859  ? 197.030 178.415 152.554 1.00 94.66  ? 859  GLN A CG    1 
ATOM   5466 C CD    . GLN A 1 859  ? 197.614 178.131 151.186 1.00 96.11  ? 859  GLN A CD    1 
ATOM   5467 O OE1   . GLN A 1 859  ? 198.634 178.705 150.804 1.00 95.46  ? 859  GLN A OE1   1 
ATOM   5468 N NE2   . GLN A 1 859  ? 196.972 177.240 150.441 1.00 92.36  ? 859  GLN A NE2   1 
ATOM   5469 N N     . GLN A 1 860  ? 198.699 181.437 155.655 1.00 92.43  ? 860  GLN A N     1 
ATOM   5470 C CA    . GLN A 1 860  ? 199.706 182.077 156.495 1.00 94.67  ? 860  GLN A CA    1 
ATOM   5471 C C     . GLN A 1 860  ? 199.380 181.913 157.974 1.00 96.40  ? 860  GLN A C     1 
ATOM   5472 O O     . GLN A 1 860  ? 200.276 181.668 158.790 1.00 100.07 ? 860  GLN A O     1 
ATOM   5473 C CB    . GLN A 1 860  ? 199.831 183.557 156.133 1.00 97.63  ? 860  GLN A CB    1 
ATOM   5474 C CG    . GLN A 1 860  ? 200.485 183.812 154.785 1.00 101.01 ? 860  GLN A CG    1 
ATOM   5475 C CD    . GLN A 1 860  ? 200.566 185.288 154.449 1.00 104.28 ? 860  GLN A CD    1 
ATOM   5476 O OE1   . GLN A 1 860  ? 200.045 186.132 155.178 1.00 101.33 ? 860  GLN A OE1   1 
ATOM   5477 N NE2   . GLN A 1 860  ? 201.223 185.607 153.340 1.00 101.84 ? 860  GLN A NE2   1 
ATOM   5478 N N     . GLN A 1 861  ? 198.104 182.055 158.341 1.00 95.59  ? 861  GLN A N     1 
ATOM   5479 C CA    . GLN A 1 861  ? 197.716 181.866 159.736 1.00 98.94  ? 861  GLN A CA    1 
ATOM   5480 C C     . GLN A 1 861  ? 197.934 180.426 160.183 1.00 99.29  ? 861  GLN A C     1 
ATOM   5481 O O     . GLN A 1 861  ? 198.392 180.180 161.305 1.00 100.07 ? 861  GLN A O     1 
ATOM   5482 C CB    . GLN A 1 861  ? 196.258 182.278 159.940 1.00 98.29  ? 861  GLN A CB    1 
ATOM   5483 C CG    . GLN A 1 861  ? 196.028 183.779 159.911 1.00 102.00 ? 861  GLN A CG    1 
ATOM   5484 C CD    . GLN A 1 861  ? 194.601 184.156 160.258 1.00 107.38 ? 861  GLN A CD    1 
ATOM   5485 O OE1   . GLN A 1 861  ? 193.701 183.318 160.224 1.00 110.24 ? 861  GLN A OE1   1 
ATOM   5486 N NE2   . GLN A 1 861  ? 194.390 185.422 160.599 1.00 105.01 ? 861  GLN A NE2   1 
ATOM   5487 N N     . GLN A 1 862  ? 197.605 179.459 159.323 1.00 96.58  ? 862  GLN A N     1 
ATOM   5488 C CA    . GLN A 1 862  ? 197.806 178.058 159.682 1.00 97.27  ? 862  GLN A CA    1 
ATOM   5489 C C     . GLN A 1 862  ? 199.286 177.717 159.794 1.00 100.66 ? 862  GLN A C     1 
ATOM   5490 O O     . GLN A 1 862  ? 199.681 176.921 160.654 1.00 98.65  ? 862  GLN A O     1 
ATOM   5491 C CB    . GLN A 1 862  ? 197.120 177.149 158.665 1.00 94.68  ? 862  GLN A CB    1 
ATOM   5492 C CG    . GLN A 1 862  ? 195.605 177.158 158.757 1.00 92.69  ? 862  GLN A CG    1 
ATOM   5493 C CD    . GLN A 1 862  ? 195.092 176.498 160.023 1.00 93.43  ? 862  GLN A CD    1 
ATOM   5494 O OE1   . GLN A 1 862  ? 195.802 175.727 160.668 1.00 98.73  ? 862  GLN A OE1   1 
ATOM   5495 N NE2   . GLN A 1 862  ? 193.850 176.798 160.383 1.00 82.90  ? 862  GLN A NE2   1 
ATOM   5496 N N     . ALA A 1 863  ? 200.119 178.299 158.927 1.00 100.62 ? 863  ALA A N     1 
ATOM   5497 C CA    . ALA A 1 863  ? 201.555 178.055 159.005 1.00 101.26 ? 863  ALA A CA    1 
ATOM   5498 C C     . ALA A 1 863  ? 202.129 178.565 160.320 1.00 104.82 ? 863  ALA A C     1 
ATOM   5499 O O     . ALA A 1 863  ? 202.968 177.900 160.940 1.00 105.24 ? 863  ALA A O     1 
ATOM   5500 C CB    . ALA A 1 863  ? 202.264 178.709 157.819 1.00 96.49  ? 863  ALA A CB    1 
ATOM   5501 N N     . LEU A 1 864  ? 201.688 179.738 160.763 1.00 104.91 ? 864  LEU A N     1 
ATOM   5502 C CA    . LEU A 1 864  ? 202.145 180.302 162.026 1.00 105.43 ? 864  LEU A CA    1 
ATOM   5503 C C     . LEU A 1 864  ? 201.429 179.652 163.205 1.00 101.61 ? 864  LEU A C     1 
ATOM   5504 O O     . LEU A 1 864  ? 200.992 180.335 164.132 1.00 99.34  ? 864  LEU A O     1 
ATOM   5505 C CB    . LEU A 1 864  ? 201.928 181.816 162.048 1.00 104.86 ? 864  LEU A CB    1 
ATOM   5506 C CG    . LEU A 1 864  ? 202.693 182.626 160.999 1.00 105.73 ? 864  LEU A CG    1 
ATOM   5507 C CD1   . LEU A 1 864  ? 202.383 184.109 161.133 1.00 104.21 ? 864  LEU A CD1   1 
ATOM   5508 C CD2   . LEU A 1 864  ? 204.188 182.374 161.114 1.00 99.74  ? 864  LEU A CD2   1 
ATOM   5509 N N     . GLY A 1 874  ? 188.928 175.676 161.838 1.00 64.99  ? 874  GLY A N     1 
ATOM   5510 C CA    . GLY A 1 874  ? 189.902 176.415 161.056 1.00 74.56  ? 874  GLY A CA    1 
ATOM   5511 C C     . GLY A 1 874  ? 189.617 176.385 159.568 1.00 77.76  ? 874  GLY A C     1 
ATOM   5512 O O     . GLY A 1 874  ? 189.402 177.425 158.946 1.00 74.28  ? 874  GLY A O     1 
ATOM   5513 N N     . MET A 1 875  ? 189.620 175.180 158.993 1.00 78.25  ? 875  MET A N     1 
ATOM   5514 C CA    . MET A 1 875  ? 189.320 175.038 157.573 1.00 69.77  ? 875  MET A CA    1 
ATOM   5515 C C     . MET A 1 875  ? 187.854 175.324 157.279 1.00 64.04  ? 875  MET A C     1 
ATOM   5516 O O     . MET A 1 875  ? 187.526 175.812 156.192 1.00 64.49  ? 875  MET A O     1 
ATOM   5517 C CB    . MET A 1 875  ? 189.696 173.636 157.095 1.00 69.58  ? 875  MET A CB    1 
ATOM   5518 C CG    . MET A 1 875  ? 189.579 173.431 155.594 1.00 71.53  ? 875  MET A CG    1 
ATOM   5519 S SD    . MET A 1 875  ? 190.666 174.516 154.654 1.00 94.84  ? 875  MET A SD    1 
ATOM   5520 C CE    . MET A 1 875  ? 190.359 173.941 152.986 1.00 79.46  ? 875  MET A CE    1 
ATOM   5521 N N     . LEU A 1 876  ? 186.963 175.029 158.228 1.00 65.30  ? 876  LEU A N     1 
ATOM   5522 C CA    . LEU A 1 876  ? 185.542 175.278 158.013 1.00 64.92  ? 876  LEU A CA    1 
ATOM   5523 C C     . LEU A 1 876  ? 185.264 176.766 157.841 1.00 61.75  ? 876  LEU A C     1 
ATOM   5524 O O     . LEU A 1 876  ? 184.435 177.159 157.011 1.00 60.16  ? 876  LEU A O     1 
ATOM   5525 C CB    . LEU A 1 876  ? 184.728 174.708 159.174 1.00 66.56  ? 876  LEU A CB    1 
ATOM   5526 C CG    . LEU A 1 876  ? 183.234 174.510 158.919 1.00 67.41  ? 876  LEU A CG    1 
ATOM   5527 C CD1   . LEU A 1 876  ? 183.016 173.463 157.840 1.00 60.86  ? 876  LEU A CD1   1 
ATOM   5528 C CD2   . LEU A 1 876  ? 182.510 174.123 160.199 1.00 64.27  ? 876  LEU A CD2   1 
ATOM   5529 N N     . GLY A 1 877  ? 185.947 177.610 158.618 1.00 63.83  ? 877  GLY A N     1 
ATOM   5530 C CA    . GLY A 1 877  ? 185.795 179.045 158.443 1.00 58.88  ? 877  GLY A CA    1 
ATOM   5531 C C     . GLY A 1 877  ? 186.265 179.519 157.082 1.00 56.81  ? 877  GLY A C     1 
ATOM   5532 O O     . GLY A 1 877  ? 185.623 180.365 156.452 1.00 56.77  ? 877  GLY A O     1 
ATOM   5533 N N     . LEU A 1 878  ? 187.389 178.979 156.605 1.00 60.43  ? 878  LEU A N     1 
ATOM   5534 C CA    . LEU A 1 878  ? 187.865 179.323 155.269 1.00 58.28  ? 878  LEU A CA    1 
ATOM   5535 C C     . LEU A 1 878  ? 186.873 178.883 154.201 1.00 52.47  ? 878  LEU A C     1 
ATOM   5536 O O     . LEU A 1 878  ? 186.622 179.616 153.239 1.00 51.04  ? 878  LEU A O     1 
ATOM   5537 C CB    . LEU A 1 878  ? 189.232 178.692 155.011 1.00 61.20  ? 878  LEU A CB    1 
ATOM   5538 C CG    . LEU A 1 878  ? 189.766 178.870 153.587 1.00 58.61  ? 878  LEU A CG    1 
ATOM   5539 C CD1   . LEU A 1 878  ? 190.048 180.335 153.295 1.00 61.84  ? 878  LEU A CD1   1 
ATOM   5540 C CD2   . LEU A 1 878  ? 191.005 178.025 153.351 1.00 68.16  ? 878  LEU A CD2   1 
ATOM   5541 N N     . LEU A 1 879  ? 186.306 177.685 154.348 1.00 50.03  ? 879  LEU A N     1 
ATOM   5542 C CA    . LEU A 1 879  ? 185.334 177.207 153.372 1.00 50.76  ? 879  LEU A CA    1 
ATOM   5543 C C     . LEU A 1 879  ? 184.080 178.072 153.374 1.00 50.72  ? 879  LEU A C     1 
ATOM   5544 O O     . LEU A 1 879  ? 183.521 178.369 152.313 1.00 52.79  ? 879  LEU A O     1 
ATOM   5545 C CB    . LEU A 1 879  ? 184.987 175.745 153.647 1.00 51.42  ? 879  LEU A CB    1 
ATOM   5546 C CG    . LEU A 1 879  ? 186.123 174.744 153.430 1.00 54.26  ? 879  LEU A CG    1 
ATOM   5547 C CD1   . LEU A 1 879  ? 185.665 173.333 153.745 1.00 55.12  ? 879  LEU A CD1   1 
ATOM   5548 C CD2   . LEU A 1 879  ? 186.655 174.832 152.010 1.00 53.64  ? 879  LEU A CD2   1 
ATOM   5549 N N     . HIS A 1 880  ? 183.626 178.493 154.558 1.00 48.77  ? 880  HIS A N     1 
ATOM   5550 C CA    . HIS A 1 880  ? 182.477 179.391 154.632 1.00 42.45  ? 880  HIS A CA    1 
ATOM   5551 C C     . HIS A 1 880  ? 182.784 180.733 153.978 1.00 43.87  ? 880  HIS A C     1 
ATOM   5552 O O     . HIS A 1 880  ? 181.947 181.289 153.254 1.00 48.91  ? 880  HIS A O     1 
ATOM   5553 C CB    . HIS A 1 880  ? 182.059 179.589 156.088 1.00 50.05  ? 880  HIS A CB    1 
ATOM   5554 C CG    . HIS A 1 880  ? 180.886 180.504 156.262 1.00 60.30  ? 880  HIS A CG    1 
ATOM   5555 N ND1   . HIS A 1 880  ? 179.600 180.138 155.929 1.00 60.05  ? 880  HIS A ND1   1 
ATOM   5556 C CD2   . HIS A 1 880  ? 180.806 181.770 156.736 1.00 59.37  ? 880  HIS A CD2   1 
ATOM   5557 C CE1   . HIS A 1 880  ? 178.778 181.138 156.190 1.00 54.13  ? 880  HIS A CE1   1 
ATOM   5558 N NE2   . HIS A 1 880  ? 179.484 182.141 156.680 1.00 52.99  ? 880  HIS A NE2   1 
ATOM   5559 N N     . ARG A 1 881  ? 183.981 181.269 154.221 1.00 45.78  ? 881  ARG A N     1 
ATOM   5560 C CA    . ARG A 1 881  ? 184.353 182.540 153.611 1.00 41.54  ? 881  ARG A CA    1 
ATOM   5561 C C     . ARG A 1 881  ? 184.430 182.423 152.095 1.00 43.48  ? 881  ARG A C     1 
ATOM   5562 O O     . ARG A 1 881  ? 184.005 183.330 151.376 1.00 44.19  ? 881  ARG A O     1 
ATOM   5563 C CB    . ARG A 1 881  ? 185.682 183.034 154.179 1.00 44.83  ? 881  ARG A CB    1 
ATOM   5564 C CG    . ARG A 1 881  ? 186.121 184.375 153.618 1.00 48.88  ? 881  ARG A CG    1 
ATOM   5565 C CD    . ARG A 1 881  ? 187.407 184.858 154.259 1.00 52.83  ? 881  ARG A CD    1 
ATOM   5566 N NE    . ARG A 1 881  ? 187.885 186.094 153.652 1.00 57.82  ? 881  ARG A NE    1 
ATOM   5567 C CZ    . ARG A 1 881  ? 187.551 187.309 154.063 1.00 57.80  ? 881  ARG A CZ    1 
ATOM   5568 N NH1   . ARG A 1 881  ? 186.732 187.492 155.085 1.00 52.49  ? 881  ARG A NH1   1 
ATOM   5569 N NH2   . ARG A 1 881  ? 188.051 188.368 153.432 1.00 57.88  ? 881  ARG A NH2   1 
ATOM   5570 N N     . LEU A 1 882  ? 184.966 181.310 151.589 1.00 47.95  ? 882  LEU A N     1 
ATOM   5571 C CA    . LEU A 1 882  ? 185.030 181.115 150.143 1.00 42.11  ? 882  LEU A CA    1 
ATOM   5572 C C     . LEU A 1 882  ? 183.639 180.939 149.545 1.00 40.39  ? 882  LEU A C     1 
ATOM   5573 O O     . LEU A 1 882  ? 183.367 181.420 148.438 1.00 40.27  ? 882  LEU A O     1 
ATOM   5574 C CB    . LEU A 1 882  ? 185.918 179.917 149.809 1.00 40.10  ? 882  LEU A CB    1 
ATOM   5575 C CG    . LEU A 1 882  ? 187.399 180.044 150.172 1.00 39.66  ? 882  LEU A CG    1 
ATOM   5576 C CD1   . LEU A 1 882  ? 188.169 178.808 149.738 1.00 44.06  ? 882  LEU A CD1   1 
ATOM   5577 C CD2   . LEU A 1 882  ? 188.004 181.296 149.563 1.00 45.24  ? 882  LEU A CD2   1 
ATOM   5578 N N     . LYS A 1 883  ? 182.745 180.250 150.261 1.00 40.12  ? 883  LYS A N     1 
ATOM   5579 C CA    . LYS A 1 883  ? 181.366 180.119 149.803 1.00 40.35  ? 883  LYS A CA    1 
ATOM   5580 C C     . LYS A 1 883  ? 180.683 181.477 149.723 1.00 44.03  ? 883  LYS A C     1 
ATOM   5581 O O     . LYS A 1 883  ? 179.918 181.743 148.788 1.00 43.19  ? 883  LYS A O     1 
ATOM   5582 C CB    . LYS A 1 883  ? 180.592 179.188 150.735 1.00 37.91  ? 883  LYS A CB    1 
ATOM   5583 C CG    . LYS A 1 883  ? 179.119 179.053 150.393 1.00 44.12  ? 883  LYS A CG    1 
ATOM   5584 C CD    . LYS A 1 883  ? 178.385 178.221 151.428 1.00 39.40  ? 883  LYS A CD    1 
ATOM   5585 C CE    . LYS A 1 883  ? 178.468 178.860 152.802 1.00 45.28  ? 883  LYS A CE    1 
ATOM   5586 N NZ    . LYS A 1 883  ? 177.770 178.047 153.833 1.00 51.47  ? 883  LYS A NZ    1 
ATOM   5587 N N     . LEU A 1 884  ? 180.938 182.346 150.702 1.00 45.12  ? 884  LEU A N     1 
ATOM   5588 C CA    . LEU A 1 884  ? 180.384 183.695 150.659 1.00 40.19  ? 884  LEU A CA    1 
ATOM   5589 C C     . LEU A 1 884  ? 181.018 184.545 149.564 1.00 38.69  ? 884  LEU A C     1 
ATOM   5590 O O     . LEU A 1 884  ? 180.327 185.362 148.946 1.00 42.74  ? 884  LEU A O     1 
ATOM   5591 C CB    . LEU A 1 884  ? 180.556 184.376 152.016 1.00 43.11  ? 884  LEU A CB    1 
ATOM   5592 C CG    . LEU A 1 884  ? 179.532 184.043 153.100 1.00 46.49  ? 884  LEU A CG    1 
ATOM   5593 C CD1   . LEU A 1 884  ? 179.965 184.634 154.430 1.00 48.09  ? 884  LEU A CD1   1 
ATOM   5594 C CD2   . LEU A 1 884  ? 178.166 184.569 152.703 1.00 49.01  ? 884  LEU A CD2   1 
ATOM   5595 N N     . ILE A 1 885  ? 182.318 184.377 149.314 1.00 37.85  ? 885  ILE A N     1 
ATOM   5596 C CA    . ILE A 1 885  ? 182.984 185.132 148.255 1.00 39.52  ? 885  ILE A CA    1 
ATOM   5597 C C     . ILE A 1 885  ? 182.420 184.747 146.895 1.00 40.01  ? 885  ILE A C     1 
ATOM   5598 O O     . ILE A 1 885  ? 182.126 185.607 146.056 1.00 45.04  ? 885  ILE A O     1 
ATOM   5599 C CB    . ILE A 1 885  ? 184.506 184.909 148.309 1.00 43.66  ? 885  ILE A CB    1 
ATOM   5600 C CG1   . ILE A 1 885  ? 185.108 185.587 149.538 1.00 49.28  ? 885  ILE A CG1   1 
ATOM   5601 C CG2   . ILE A 1 885  ? 185.168 185.426 147.044 1.00 44.55  ? 885  ILE A CG2   1 
ATOM   5602 C CD1   . ILE A 1 885  ? 186.580 185.322 149.712 1.00 50.93  ? 885  ILE A CD1   1 
ATOM   5603 N N     . CYS A 1 886  ? 182.263 183.445 146.655 1.00 38.90  ? 886  CYS A N     1 
ATOM   5604 C CA    . CYS A 1 886  ? 181.758 182.991 145.364 1.00 39.36  ? 886  CYS A CA    1 
ATOM   5605 C C     . CYS A 1 886  ? 180.301 183.388 145.165 1.00 40.69  ? 886  CYS A C     1 
ATOM   5606 O O     . CYS A 1 886  ? 179.907 183.788 144.064 1.00 41.34  ? 886  CYS A O     1 
ATOM   5607 C CB    . CYS A 1 886  ? 181.931 181.479 145.238 1.00 46.47  ? 886  CYS A CB    1 
ATOM   5608 S SG    . CYS A 1 886  ? 183.651 180.924 145.181 1.00 54.25  ? 886  CYS A SG    1 
ATOM   5609 N N     . ALA A 1 887  ? 179.486 183.289 146.216 1.00 42.14  ? 887  ALA A N     1 
ATOM   5610 C CA    . ALA A 1 887  ? 178.066 183.600 146.086 1.00 39.64  ? 887  ALA A CA    1 
ATOM   5611 C C     . ALA A 1 887  ? 177.840 185.101 145.953 1.00 43.41  ? 887  ALA A C     1 
ATOM   5612 O O     . ALA A 1 887  ? 177.292 185.573 144.951 1.00 50.53  ? 887  ALA A O     1 
ATOM   5613 C CB    . ALA A 1 887  ? 177.294 183.039 147.280 1.00 36.67  ? 887  ALA A CB    1 
ATOM   5614 N N     . HIS A 1 888  ? 178.258 185.869 146.953 1.00 42.34  ? 888  HIS A N     1 
ATOM   5615 C CA    . HIS A 1 888  ? 178.072 187.319 146.948 1.00 45.12  ? 888  HIS A CA    1 
ATOM   5616 C C     . HIS A 1 888  ? 179.273 187.954 147.629 1.00 44.54  ? 888  HIS A C     1 
ATOM   5617 O O     . HIS A 1 888  ? 179.330 188.031 148.866 1.00 46.34  ? 888  HIS A O     1 
ATOM   5618 C CB    . HIS A 1 888  ? 176.773 187.722 147.640 1.00 49.57  ? 888  HIS A CB    1 
ATOM   5619 C CG    . HIS A 1 888  ? 176.326 189.116 147.327 1.00 55.78  ? 888  HIS A CG    1 
ATOM   5620 N ND1   . HIS A 1 888  ? 176.070 189.544 146.043 1.00 55.25  ? 888  HIS A ND1   1 
ATOM   5621 C CD2   . HIS A 1 888  ? 176.086 190.177 148.132 1.00 55.74  ? 888  HIS A CD2   1 
ATOM   5622 C CE1   . HIS A 1 888  ? 175.694 190.810 146.069 1.00 59.25  ? 888  HIS A CE1   1 
ATOM   5623 N NE2   . HIS A 1 888  ? 175.694 191.217 147.325 1.00 62.14  ? 888  HIS A NE2   1 
ATOM   5624 N N     . PRO A 1 889  ? 180.259 188.421 146.860 1.00 44.95  ? 889  PRO A N     1 
ATOM   5625 C CA    . PRO A 1 889  ? 181.450 189.025 147.477 1.00 51.78  ? 889  PRO A CA    1 
ATOM   5626 C C     . PRO A 1 889  ? 181.158 190.287 148.268 1.00 59.88  ? 889  PRO A C     1 
ATOM   5627 O O     . PRO A 1 889  ? 181.977 190.670 149.114 1.00 60.97  ? 889  PRO A O     1 
ATOM   5628 C CB    . PRO A 1 889  ? 182.360 189.314 146.275 1.00 55.18  ? 889  PRO A CB    1 
ATOM   5629 C CG    . PRO A 1 889  ? 181.432 189.410 145.113 1.00 53.27  ? 889  PRO A CG    1 
ATOM   5630 C CD    . PRO A 1 889  ? 180.330 188.431 145.390 1.00 46.01  ? 889  PRO A CD    1 
ATOM   5631 N N     . ALA A 1 890  ? 180.027 190.952 148.018 1.00 61.26  ? 890  ALA A N     1 
ATOM   5632 C CA    . ALA A 1 890  ? 179.698 192.160 148.765 1.00 63.26  ? 890  ALA A CA    1 
ATOM   5633 C C     . ALA A 1 890  ? 179.434 191.861 150.235 1.00 60.52  ? 890  ALA A C     1 
ATOM   5634 O O     . ALA A 1 890  ? 179.674 192.719 151.092 1.00 65.45  ? 890  ALA A O     1 
ATOM   5635 C CB    . ALA A 1 890  ? 178.489 192.853 148.139 1.00 62.89  ? 890  ALA A CB    1 
ATOM   5636 N N     . ILE A 1 891  ? 178.934 190.664 150.543 1.00 58.56  ? 891  ILE A N     1 
ATOM   5637 C CA    . ILE A 1 891  ? 178.739 190.274 151.936 1.00 57.02  ? 891  ILE A CA    1 
ATOM   5638 C C     . ILE A 1 891  ? 180.078 190.184 152.657 1.00 60.55  ? 891  ILE A C     1 
ATOM   5639 O O     . ILE A 1 891  ? 180.217 190.643 153.797 1.00 63.78  ? 891  ILE A O     1 
ATOM   5640 C CB    . ILE A 1 891  ? 177.961 188.948 152.009 1.00 53.92  ? 891  ILE A CB    1 
ATOM   5641 C CG1   . ILE A 1 891  ? 176.547 189.133 151.462 1.00 50.22  ? 891  ILE A CG1   1 
ATOM   5642 C CG2   . ILE A 1 891  ? 177.914 188.430 153.434 1.00 55.24  ? 891  ILE A CG2   1 
ATOM   5643 C CD1   . ILE A 1 891  ? 175.718 187.880 151.508 1.00 47.75  ? 891  ILE A CD1   1 
ATOM   5644 N N     . VAL A 1 892  ? 181.082 189.589 152.009 1.00 60.45  ? 892  VAL A N     1 
ATOM   5645 C CA    . VAL A 1 892  ? 182.411 189.500 152.607 1.00 64.83  ? 892  VAL A CA    1 
ATOM   5646 C C     . VAL A 1 892  ? 183.039 190.882 152.724 1.00 68.59  ? 892  VAL A C     1 
ATOM   5647 O O     . VAL A 1 892  ? 183.651 191.219 153.746 1.00 63.74  ? 892  VAL A O     1 
ATOM   5648 C CB    . VAL A 1 892  ? 183.298 188.545 151.789 1.00 59.34  ? 892  VAL A CB    1 
ATOM   5649 C CG1   . VAL A 1 892  ? 184.659 188.391 152.442 1.00 55.99  ? 892  VAL A CG1   1 
ATOM   5650 C CG2   . VAL A 1 892  ? 182.620 187.202 151.643 1.00 53.73  ? 892  VAL A CG2   1 
ATOM   5651 N N     . ASN A 1 893  ? 182.903 191.700 151.685 1.00 70.77  ? 893  ASN A N     1 
ATOM   5652 C CA    . ASN A 1 893  ? 183.490 193.032 151.661 1.00 76.67  ? 893  ASN A CA    1 
ATOM   5653 C C     . ASN A 1 893  ? 182.477 194.033 151.120 1.00 81.20  ? 893  ASN A C     1 
ATOM   5654 O O     . ASN A 1 893  ? 182.089 193.952 149.948 1.00 79.34  ? 893  ASN A O     1 
ATOM   5655 C CB    . ASN A 1 893  ? 184.763 193.042 150.814 1.00 78.42  ? 893  ASN A CB    1 
ATOM   5656 C CG    . ASN A 1 893  ? 186.006 193.317 151.634 1.00 85.04  ? 893  ASN A CG    1 
ATOM   5657 O OD1   . ASN A 1 893  ? 186.005 193.164 152.855 1.00 86.26  ? 893  ASN A OD1   1 
ATOM   5658 N ND2   . ASN A 1 893  ? 187.076 193.729 150.964 1.00 84.28  ? 893  ASN A ND2   1 
ATOM   5659 N N     . PRO A 1 894  ? 182.036 194.995 151.932 1.00 84.20  ? 894  PRO A N     1 
ATOM   5660 C CA    . PRO A 1 894  ? 180.973 195.908 151.490 1.00 79.65  ? 894  PRO A CA    1 
ATOM   5661 C C     . PRO A 1 894  ? 181.466 197.021 150.577 1.00 83.82  ? 894  PRO A C     1 
ATOM   5662 O O     . PRO A 1 894  ? 180.753 198.006 150.360 1.00 85.22  ? 894  PRO A O     1 
ATOM   5663 C CB    . PRO A 1 894  ? 180.428 196.478 152.809 1.00 78.99  ? 894  PRO A CB    1 
ATOM   5664 C CG    . PRO A 1 894  ? 180.995 195.600 153.897 1.00 78.70  ? 894  PRO A CG    1 
ATOM   5665 C CD    . PRO A 1 894  ? 182.306 195.123 153.371 1.00 80.58  ? 894  PRO A CD    1 
ATOM   5666 N N     . GLU A 1 895  ? 182.676 196.882 150.040 1.00 87.21  ? 895  GLU A N     1 
ATOM   5667 C CA    . GLU A 1 895  ? 183.209 197.877 149.126 1.00 89.92  ? 895  GLU A CA    1 
ATOM   5668 C C     . GLU A 1 895  ? 182.375 197.929 147.848 1.00 93.59  ? 895  GLU A C     1 
ATOM   5669 O O     . GLU A 1 895  ? 181.780 196.929 147.440 1.00 94.57  ? 895  GLU A O     1 
ATOM   5670 C CB    . GLU A 1 895  ? 184.666 197.566 148.788 1.00 86.83  ? 895  GLU A CB    1 
ATOM   5671 C CG    . GLU A 1 895  ? 185.678 198.054 149.817 1.00 89.23  ? 895  GLU A CG    1 
ATOM   5672 C CD    . GLU A 1 895  ? 185.639 197.268 151.114 1.00 92.17  ? 895  GLU A CD    1 
ATOM   5673 O OE1   . GLU A 1 895  ? 184.984 196.207 151.156 1.00 88.78  ? 895  GLU A OE1   1 
ATOM   5674 O OE2   . GLU A 1 895  ? 186.269 197.714 152.095 1.00 97.17  ? 895  GLU A OE2   1 
ATOM   5675 N N     . PRO A 1 896  ? 182.303 199.099 147.206 1.00 94.69  ? 896  PRO A N     1 
ATOM   5676 C CA    . PRO A 1 896  ? 181.517 199.205 145.965 1.00 93.57  ? 896  PRO A CA    1 
ATOM   5677 C C     . PRO A 1 896  ? 182.013 198.303 144.849 1.00 90.57  ? 896  PRO A C     1 
ATOM   5678 O O     . PRO A 1 896  ? 181.225 197.938 143.967 1.00 89.05  ? 896  PRO A O     1 
ATOM   5679 C CB    . PRO A 1 896  ? 181.653 200.688 145.592 1.00 91.74  ? 896  PRO A CB    1 
ATOM   5680 C CG    . PRO A 1 896  ? 181.982 201.374 146.876 1.00 92.82  ? 896  PRO A CG    1 
ATOM   5681 C CD    . PRO A 1 896  ? 182.828 200.404 147.641 1.00 91.65  ? 896  PRO A CD    1 
ATOM   5682 N N     . ARG A 1 897  ? 183.298 197.942 144.851 1.00 87.08  ? 897  ARG A N     1 
ATOM   5683 C CA    . ARG A 1 897  ? 183.821 197.060 143.811 1.00 87.93  ? 897  ARG A CA    1 
ATOM   5684 C C     . ARG A 1 897  ? 183.136 195.700 143.845 1.00 86.07  ? 897  ARG A C     1 
ATOM   5685 O O     . ARG A 1 897  ? 182.789 195.144 142.797 1.00 84.20  ? 897  ARG A O     1 
ATOM   5686 C CB    . ARG A 1 897  ? 185.335 196.906 143.969 1.00 85.48  ? 897  ARG A CB    1 
ATOM   5687 C CG    . ARG A 1 897  ? 186.087 198.226 143.941 1.00 89.57  ? 897  ARG A CG    1 
ATOM   5688 C CD    . ARG A 1 897  ? 187.581 198.051 144.180 1.00 90.15  ? 897  ARG A CD    1 
ATOM   5689 N NE    . ARG A 1 897  ? 187.867 197.375 145.440 1.00 91.57  ? 897  ARG A NE    1 
ATOM   5690 C CZ    . ARG A 1 897  ? 188.542 196.238 145.543 1.00 89.27  ? 897  ARG A CZ    1 
ATOM   5691 N NH1   . ARG A 1 897  ? 189.051 195.637 144.481 1.00 84.36  ? 897  ARG A NH1   1 
ATOM   5692 N NH2   . ARG A 1 897  ? 188.720 195.697 146.745 1.00 86.09  ? 897  ARG A NH2   1 
ATOM   5693 N N     . PHE A 1 898  ? 182.928 195.151 145.043 1.00 83.98  ? 898  PHE A N     1 
ATOM   5694 C CA    . PHE A 1 898  ? 182.307 193.839 145.168 1.00 78.71  ? 898  PHE A CA    1 
ATOM   5695 C C     . PHE A 1 898  ? 180.804 193.877 144.927 1.00 79.17  ? 898  PHE A C     1 
ATOM   5696 O O     . PHE A 1 898  ? 180.211 192.834 144.634 1.00 75.94  ? 898  PHE A O     1 
ATOM   5697 C CB    . PHE A 1 898  ? 182.595 193.258 146.553 1.00 76.06  ? 898  PHE A CB    1 
ATOM   5698 C CG    . PHE A 1 898  ? 184.056 193.192 146.888 1.00 77.35  ? 898  PHE A CG    1 
ATOM   5699 C CD1   . PHE A 1 898  ? 184.791 192.053 146.616 1.00 75.75  ? 898  PHE A CD1   1 
ATOM   5700 C CD2   . PHE A 1 898  ? 184.695 194.271 147.475 1.00 84.50  ? 898  PHE A CD2   1 
ATOM   5701 C CE1   . PHE A 1 898  ? 186.135 191.991 146.926 1.00 78.67  ? 898  PHE A CE1   1 
ATOM   5702 C CE2   . PHE A 1 898  ? 186.039 194.215 147.784 1.00 85.91  ? 898  PHE A CE2   1 
ATOM   5703 C CZ    . PHE A 1 898  ? 186.760 193.073 147.509 1.00 80.75  ? 898  PHE A CZ    1 
ATOM   5704 N N     . ARG A 1 899  ? 180.177 195.048 145.047 1.00 80.76  ? 899  ARG A N     1 
ATOM   5705 C CA    . ARG A 1 899  ? 178.733 195.135 144.855 1.00 81.83  ? 899  ARG A CA    1 
ATOM   5706 C C     . ARG A 1 899  ? 178.357 194.981 143.387 1.00 81.06  ? 899  ARG A C     1 
ATOM   5707 O O     . ARG A 1 899  ? 177.354 194.336 143.061 1.00 79.59  ? 899  ARG A O     1 
ATOM   5708 C CB    . ARG A 1 899  ? 178.212 196.462 145.407 1.00 82.49  ? 899  ARG A CB    1 
ATOM   5709 C CG    . ARG A 1 899  ? 176.701 196.608 145.357 1.00 79.06  ? 899  ARG A CG    1 
ATOM   5710 C CD    . ARG A 1 899  ? 176.019 195.616 146.284 1.00 77.81  ? 899  ARG A CD    1 
ATOM   5711 N NE    . ARG A 1 899  ? 176.336 195.869 147.685 1.00 79.88  ? 899  ARG A NE    1 
ATOM   5712 C CZ    . ARG A 1 899  ? 175.885 195.143 148.698 1.00 74.72  ? 899  ARG A CZ    1 
ATOM   5713 N NH1   . ARG A 1 899  ? 175.095 194.099 148.503 1.00 69.45  ? 899  ARG A NH1   1 
ATOM   5714 N NH2   . ARG A 1 899  ? 176.236 195.470 149.938 1.00 68.65  ? 899  ARG A NH2   1 
ATOM   5715 N N     . ASP A 1 900  ? 179.148 195.564 142.489 1.00 81.31  ? 900  ASP A N     1 
ATOM   5716 C CA    . ASP A 1 900  ? 178.870 195.537 141.060 1.00 80.95  ? 900  ASP A CA    1 
ATOM   5717 C C     . ASP A 1 900  ? 179.593 194.415 140.329 1.00 77.79  ? 900  ASP A C     1 
ATOM   5718 O O     . ASP A 1 900  ? 179.483 194.324 139.102 1.00 78.44  ? 900  ASP A O     1 
ATOM   5719 C CB    . ASP A 1 900  ? 179.243 196.883 140.430 1.00 81.50  ? 900  ASP A CB    1 
ATOM   5720 C CG    . ASP A 1 900  ? 178.491 198.045 141.047 1.00 87.79  ? 900  ASP A CG    1 
ATOM   5721 O OD1   . ASP A 1 900  ? 177.299 197.875 141.380 1.00 88.60  ? 900  ASP A OD1   1 
ATOM   5722 O OD2   . ASP A 1 900  ? 179.092 199.129 141.203 1.00 87.96  ? 900  ASP A OD2   1 
ATOM   5723 N N     . ASN A 1 901  ? 180.321 193.561 141.042 1.00 73.11  ? 901  ASN A N     1 
ATOM   5724 C CA    . ASN A 1 901  ? 181.134 192.509 140.440 1.00 68.26  ? 901  ASN A CA    1 
ATOM   5725 C C     . ASN A 1 901  ? 180.775 191.153 141.032 1.00 64.64  ? 901  ASN A C     1 
ATOM   5726 O O     . ASN A 1 901  ? 181.638 190.375 141.445 1.00 66.80  ? 901  ASN A O     1 
ATOM   5727 C CB    . ASN A 1 901  ? 182.621 192.803 140.615 1.00 71.71  ? 901  ASN A CB    1 
ATOM   5728 C CG    . ASN A 1 901  ? 183.061 194.044 139.865 1.00 73.92  ? 901  ASN A CG    1 
ATOM   5729 O OD1   . ASN A 1 901  ? 182.549 194.345 138.787 1.00 71.00  ? 901  ASN A OD1   1 
ATOM   5730 N ND2   . ASN A 1 901  ? 184.012 194.773 140.434 1.00 78.64  ? 901  ASN A ND2   1 
ATOM   5731 N N     . SER A 1 902  ? 179.479 190.854 141.085 1.00 56.41  ? 902  SER A N     1 
ATOM   5732 C CA    . SER A 1 902  ? 179.005 189.548 141.528 1.00 47.35  ? 902  SER A CA    1 
ATOM   5733 C C     . SER A 1 902  ? 178.421 188.811 140.332 1.00 45.94  ? 902  SER A C     1 
ATOM   5734 O O     . SER A 1 902  ? 177.258 189.045 139.968 1.00 44.72  ? 902  SER A O     1 
ATOM   5735 C CB    . SER A 1 902  ? 177.959 189.692 142.637 1.00 51.43  ? 902  SER A CB    1 
ATOM   5736 O OG    . SER A 1 902  ? 177.518 188.424 143.088 1.00 53.87  ? 902  SER A OG    1 
ATOM   5737 N N     . PRO A 1 903  ? 179.181 187.926 139.682 1.00 46.37  ? 903  PRO A N     1 
ATOM   5738 C CA    . PRO A 1 903  ? 178.657 187.248 138.486 1.00 42.01  ? 903  PRO A CA    1 
ATOM   5739 C C     . PRO A 1 903  ? 177.420 186.412 138.747 1.00 37.75  ? 903  PRO A C     1 
ATOM   5740 O O     . PRO A 1 903  ? 176.548 186.328 137.874 1.00 41.21  ? 903  PRO A O     1 
ATOM   5741 C CB    . PRO A 1 903  ? 179.839 186.381 138.031 1.00 37.97  ? 903  PRO A CB    1 
ATOM   5742 C CG    . PRO A 1 903  ? 180.676 186.207 139.250 1.00 42.00  ? 903  PRO A CG    1 
ATOM   5743 C CD    . PRO A 1 903  ? 180.546 187.486 140.014 1.00 45.06  ? 903  PRO A CD    1 
ATOM   5744 N N     . LYS A 1 904  ? 177.310 185.791 139.922 1.00 33.80  ? 904  LYS A N     1 
ATOM   5745 C CA    . LYS A 1 904  ? 176.146 184.954 140.191 1.00 36.03  ? 904  LYS A CA    1 
ATOM   5746 C C     . LYS A 1 904  ? 174.886 185.795 140.352 1.00 38.75  ? 904  LYS A C     1 
ATOM   5747 O O     . LYS A 1 904  ? 173.813 185.406 139.882 1.00 38.41  ? 904  LYS A O     1 
ATOM   5748 C CB    . LYS A 1 904  ? 176.383 184.091 141.428 1.00 37.24  ? 904  LYS A CB    1 
ATOM   5749 C CG    . LYS A 1 904  ? 175.376 182.964 141.563 1.00 37.70  ? 904  LYS A CG    1 
ATOM   5750 C CD    . LYS A 1 904  ? 175.561 182.183 142.846 1.00 35.75  ? 904  LYS A CD    1 
ATOM   5751 C CE    . LYS A 1 904  ? 176.842 181.387 142.839 1.00 31.77  ? 904  LYS A CE    1 
ATOM   5752 N NZ    . LYS A 1 904  ? 176.931 180.543 144.059 1.00 32.86  ? 904  LYS A NZ    1 
ATOM   5753 N N     . LEU A 1 905  ? 174.996 186.955 141.004 1.00 40.38  ? 905  LEU A N     1 
ATOM   5754 C CA    . LEU A 1 905  ? 173.845 187.845 141.120 1.00 31.72  ? 905  LEU A CA    1 
ATOM   5755 C C     . LEU A 1 905  ? 173.430 188.395 139.760 1.00 35.44  ? 905  LEU A C     1 
ATOM   5756 O O     . LEU A 1 905  ? 172.233 188.514 139.471 1.00 40.00  ? 905  LEU A O     1 
ATOM   5757 C CB    . LEU A 1 905  ? 174.160 188.986 142.086 1.00 36.16  ? 905  LEU A CB    1 
ATOM   5758 C CG    . LEU A 1 905  ? 173.037 189.994 142.336 1.00 40.75  ? 905  LEU A CG    1 
ATOM   5759 C CD1   . LEU A 1 905  ? 171.842 189.318 142.987 1.00 33.62  ? 905  LEU A CD1   1 
ATOM   5760 C CD2   . LEU A 1 905  ? 173.536 191.149 143.189 1.00 42.70  ? 905  LEU A CD2   1 
ATOM   5761 N N     . ASN A 1 906  ? 174.405 188.748 138.918 1.00 36.89  ? 906  ASN A N     1 
ATOM   5762 C CA    . ASN A 1 906  ? 174.087 189.210 137.571 1.00 33.78  ? 906  ASN A CA    1 
ATOM   5763 C C     . ASN A 1 906  ? 173.384 188.124 136.770 1.00 33.52  ? 906  ASN A C     1 
ATOM   5764 O O     . ASN A 1 906  ? 172.397 188.393 136.075 1.00 37.96  ? 906  ASN A O     1 
ATOM   5765 C CB    . ASN A 1 906  ? 175.358 189.663 136.856 1.00 38.26  ? 906  ASN A CB    1 
ATOM   5766 C CG    . ASN A 1 906  ? 176.032 190.825 137.548 1.00 45.14  ? 906  ASN A CG    1 
ATOM   5767 O OD1   . ASN A 1 906  ? 175.384 191.614 138.234 1.00 44.57  ? 906  ASN A OD1   1 
ATOM   5768 N ND2   . ASN A 1 906  ? 177.341 190.940 137.370 1.00 45.51  ? 906  ASN A ND2   1 
ATOM   5769 N N     . TRP A 1 907  ? 173.880 186.887 136.858 1.00 31.42  ? 907  TRP A N     1 
ATOM   5770 C CA    . TRP A 1 907  ? 173.212 185.775 136.193 1.00 29.26  ? 907  TRP A CA    1 
ATOM   5771 C C     . TRP A 1 907  ? 171.798 185.592 136.721 1.00 33.49  ? 907  TRP A C     1 
ATOM   5772 O O     . TRP A 1 907  ? 170.866 185.343 135.948 1.00 39.10  ? 907  TRP A O     1 
ATOM   5773 C CB    . TRP A 1 907  ? 174.018 184.488 136.374 1.00 29.24  ? 907  TRP A CB    1 
ATOM   5774 C CG    . TRP A 1 907  ? 173.213 183.256 136.100 1.00 31.32  ? 907  TRP A CG    1 
ATOM   5775 C CD1   . TRP A 1 907  ? 173.044 182.636 134.897 1.00 30.72  ? 907  TRP A CD1   1 
ATOM   5776 C CD2   . TRP A 1 907  ? 172.453 182.500 137.050 1.00 30.00  ? 907  TRP A CD2   1 
ATOM   5777 N NE1   . TRP A 1 907  ? 172.229 181.540 135.040 1.00 31.72  ? 907  TRP A NE1   1 
ATOM   5778 C CE2   . TRP A 1 907  ? 171.852 181.437 136.353 1.00 30.69  ? 907  TRP A CE2   1 
ATOM   5779 C CE3   . TRP A 1 907  ? 172.224 182.621 138.423 1.00 30.29  ? 907  TRP A CE3   1 
ATOM   5780 C CZ2   . TRP A 1 907  ? 171.038 180.503 136.981 1.00 28.25  ? 907  TRP A CZ2   1 
ATOM   5781 C CZ3   . TRP A 1 907  ? 171.414 181.695 139.042 1.00 33.72  ? 907  TRP A CZ3   1 
ATOM   5782 C CH2   . TRP A 1 907  ? 170.832 180.648 138.323 1.00 29.48  ? 907  TRP A CH2   1 
ATOM   5783 N N     . LEU A 1 908  ? 171.620 185.698 138.040 1.00 34.23  ? 908  LEU A N     1 
ATOM   5784 C CA    . LEU A 1 908  ? 170.298 185.531 138.631 1.00 29.19  ? 908  LEU A CA    1 
ATOM   5785 C C     . LEU A 1 908  ? 169.330 186.576 138.102 1.00 31.83  ? 908  LEU A C     1 
ATOM   5786 O O     . LEU A 1 908  ? 168.212 186.251 137.692 1.00 36.74  ? 908  LEU A O     1 
ATOM   5787 C CB    . LEU A 1 908  ? 170.395 185.608 140.154 1.00 28.89  ? 908  LEU A CB    1 
ATOM   5788 C CG    . LEU A 1 908  ? 169.065 185.603 140.909 1.00 31.68  ? 908  LEU A CG    1 
ATOM   5789 C CD1   . LEU A 1 908  ? 168.323 184.300 140.677 1.00 26.11  ? 908  LEU A CD1   1 
ATOM   5790 C CD2   . LEU A 1 908  ? 169.287 185.839 142.389 1.00 25.45  ? 908  LEU A CD2   1 
ATOM   5791 N N     . LEU A 1 909  ? 169.753 187.841 138.089 1.00 33.21  ? 909  LEU A N     1 
ATOM   5792 C CA    . LEU A 1 909  ? 168.881 188.902 137.598 1.00 32.84  ? 909  LEU A CA    1 
ATOM   5793 C C     . LEU A 1 909  ? 168.567 188.719 136.119 1.00 32.60  ? 909  LEU A C     1 
ATOM   5794 O O     . LEU A 1 909  ? 167.417 188.890 135.694 1.00 34.36  ? 909  LEU A O     1 
ATOM   5795 C CB    . LEU A 1 909  ? 169.521 190.266 137.854 1.00 30.76  ? 909  LEU A CB    1 
ATOM   5796 C CG    . LEU A 1 909  ? 169.725 190.622 139.327 1.00 26.56  ? 909  LEU A CG    1 
ATOM   5797 C CD1   . LEU A 1 909  ? 170.329 192.007 139.471 1.00 26.80  ? 909  LEU A CD1   1 
ATOM   5798 C CD2   . LEU A 1 909  ? 168.414 190.525 140.087 1.00 27.33  ? 909  LEU A CD2   1 
ATOM   5799 N N     . LYS A 1 910  ? 169.572 188.350 135.321 1.00 38.02  ? 910  LYS A N     1 
ATOM   5800 C CA    . LYS A 1 910  ? 169.359 188.162 133.890 1.00 34.19  ? 910  LYS A CA    1 
ATOM   5801 C C     . LYS A 1 910  ? 168.367 187.036 133.619 1.00 38.92  ? 910  LYS A C     1 
ATOM   5802 O O     . LYS A 1 910  ? 167.430 187.194 132.826 1.00 43.83  ? 910  LYS A O     1 
ATOM   5803 C CB    . LYS A 1 910  ? 170.697 187.884 133.206 1.00 34.86  ? 910  LYS A CB    1 
ATOM   5804 C CG    . LYS A 1 910  ? 170.594 187.515 131.740 1.00 49.24  ? 910  LYS A CG    1 
ATOM   5805 C CD    . LYS A 1 910  ? 171.969 187.237 131.158 1.00 52.76  ? 910  LYS A CD    1 
ATOM   5806 C CE    . LYS A 1 910  ? 172.702 186.181 131.969 1.00 47.22  ? 910  LYS A CE    1 
ATOM   5807 N NZ    . LYS A 1 910  ? 174.083 185.945 131.465 1.00 43.93  ? 910  LYS A NZ    1 
ATOM   5808 N N     . ILE A 1 911  ? 168.547 185.891 134.279 1.00 35.39  ? 911  ILE A N     1 
ATOM   5809 C CA    . ILE A 1 911  ? 167.656 184.769 134.008 1.00 34.56  ? 911  ILE A CA    1 
ATOM   5810 C C     . ILE A 1 911  ? 166.273 185.013 134.595 1.00 40.15  ? 911  ILE A C     1 
ATOM   5811 O O     . ILE A 1 911  ? 165.276 184.533 134.050 1.00 45.68  ? 911  ILE A O     1 
ATOM   5812 C CB    . ILE A 1 911  ? 168.257 183.444 134.512 1.00 33.71  ? 911  ILE A CB    1 
ATOM   5813 C CG1   . ILE A 1 911  ? 168.320 183.423 136.036 1.00 31.57  ? 911  ILE A CG1   1 
ATOM   5814 C CG2   . ILE A 1 911  ? 169.627 183.215 133.899 1.00 35.65  ? 911  ILE A CG2   1 
ATOM   5815 C CD1   . ILE A 1 911  ? 167.987 182.083 136.613 1.00 29.64  ? 911  ILE A CD1   1 
ATOM   5816 N N     . LEU A 1 912  ? 166.173 185.755 135.702 1.00 37.58  ? 912  LEU A N     1 
ATOM   5817 C CA    . LEU A 1 912  ? 164.854 186.103 136.220 1.00 31.14  ? 912  LEU A CA    1 
ATOM   5818 C C     . LEU A 1 912  ? 164.120 187.029 135.262 1.00 37.67  ? 912  LEU A C     1 
ATOM   5819 O O     . LEU A 1 912  ? 162.910 186.886 135.059 1.00 44.88  ? 912  LEU A O     1 
ATOM   5820 C CB    . LEU A 1 912  ? 164.975 186.740 137.604 1.00 31.12  ? 912  LEU A CB    1 
ATOM   5821 C CG    . LEU A 1 912  ? 165.250 185.801 138.780 1.00 26.64  ? 912  LEU A CG    1 
ATOM   5822 C CD1   . LEU A 1 912  ? 165.287 186.580 140.082 1.00 27.28  ? 912  LEU A CD1   1 
ATOM   5823 C CD2   . LEU A 1 912  ? 164.213 184.696 138.844 1.00 28.68  ? 912  LEU A CD2   1 
ATOM   5824 N N     . ALA A 1 913  ? 164.837 187.979 134.655 1.00 38.61  ? 913  ALA A N     1 
ATOM   5825 C CA    . ALA A 1 913  ? 164.230 188.811 133.623 1.00 37.21  ? 913  ALA A CA    1 
ATOM   5826 C C     . ALA A 1 913  ? 163.779 187.969 132.437 1.00 44.18  ? 913  ALA A C     1 
ATOM   5827 O O     . ALA A 1 913  ? 162.692 188.186 131.887 1.00 52.32  ? 913  ALA A O     1 
ATOM   5828 C CB    . ALA A 1 913  ? 165.212 189.890 133.172 1.00 32.02  ? 913  ALA A CB    1 
ATOM   5829 N N     . GLU A 1 914  ? 164.606 187.002 132.027 1.00 44.30  ? 914  GLU A N     1 
ATOM   5830 C CA    . GLU A 1 914  ? 164.232 186.129 130.917 1.00 43.52  ? 914  GLU A CA    1 
ATOM   5831 C C     . GLU A 1 914  ? 162.982 185.319 131.242 1.00 44.54  ? 914  GLU A C     1 
ATOM   5832 O O     . GLU A 1 914  ? 162.089 185.178 130.400 1.00 51.78  ? 914  GLU A O     1 
ATOM   5833 C CB    . GLU A 1 914  ? 165.394 185.201 130.564 1.00 44.78  ? 914  GLU A CB    1 
ATOM   5834 C CG    . GLU A 1 914  ? 166.617 185.912 130.009 1.00 50.44  ? 914  GLU A CG    1 
ATOM   5835 C CD    . GLU A 1 914  ? 167.765 184.962 129.726 1.00 63.46  ? 914  GLU A CD    1 
ATOM   5836 O OE1   . GLU A 1 914  ? 167.589 183.740 129.916 1.00 64.52  ? 914  GLU A OE1   1 
ATOM   5837 O OE2   . GLU A 1 914  ? 168.844 185.436 129.313 1.00 61.24  ? 914  GLU A OE2   1 
ATOM   5838 N N     . ILE A 1 915  ? 162.903 184.776 132.458 1.00 43.05  ? 915  ILE A N     1 
ATOM   5839 C CA    . ILE A 1 915  ? 161.732 184.004 132.865 1.00 43.13  ? 915  ILE A CA    1 
ATOM   5840 C C     . ILE A 1 915  ? 160.496 184.893 132.921 1.00 48.49  ? 915  ILE A C     1 
ATOM   5841 O O     . ILE A 1 915  ? 159.406 184.492 132.496 1.00 54.15  ? 915  ILE A O     1 
ATOM   5842 C CB    . ILE A 1 915  ? 161.994 183.313 134.216 1.00 39.62  ? 915  ILE A CB    1 
ATOM   5843 C CG1   . ILE A 1 915  ? 163.109 182.277 134.078 1.00 35.85  ? 915  ILE A CG1   1 
ATOM   5844 C CG2   . ILE A 1 915  ? 160.728 182.659 134.740 1.00 43.66  ? 915  ILE A CG2   1 
ATOM   5845 C CD1   . ILE A 1 915  ? 163.562 181.699 135.395 1.00 33.76  ? 915  ILE A CD1   1 
ATOM   5846 N N     . LYS A 1 916  ? 160.644 186.110 133.449 1.00 46.74  ? 916  LYS A N     1 
ATOM   5847 C CA    . LYS A 1 916  ? 159.513 187.026 133.544 1.00 47.84  ? 916  LYS A CA    1 
ATOM   5848 C C     . LYS A 1 916  ? 158.993 187.412 132.167 1.00 53.53  ? 916  LYS A C     1 
ATOM   5849 O O     . LYS A 1 916  ? 157.778 187.474 131.949 1.00 60.69  ? 916  LYS A O     1 
ATOM   5850 C CB    . LYS A 1 916  ? 159.922 188.270 134.332 1.00 52.79  ? 916  LYS A CB    1 
ATOM   5851 C CG    . LYS A 1 916  ? 158.824 189.305 134.496 1.00 54.31  ? 916  LYS A CG    1 
ATOM   5852 C CD    . LYS A 1 916  ? 159.334 190.517 135.257 1.00 51.57  ? 916  LYS A CD    1 
ATOM   5853 C CE    . LYS A 1 916  ? 158.245 191.557 135.447 1.00 56.96  ? 916  LYS A CE    1 
ATOM   5854 N NZ    . LYS A 1 916  ? 158.735 192.731 136.221 1.00 53.80  ? 916  LYS A NZ    1 
ATOM   5855 N N     . HIS A 1 917  ? 159.895 187.676 131.224 1.00 55.70  ? 917  HIS A N     1 
ATOM   5856 C CA    . HIS A 1 917  ? 159.503 188.137 129.900 1.00 56.62  ? 917  HIS A CA    1 
ATOM   5857 C C     . HIS A 1 917  ? 159.198 187.004 128.929 1.00 58.95  ? 917  HIS A C     1 
ATOM   5858 O O     . HIS A 1 917  ? 158.699 187.273 127.831 1.00 68.87  ? 917  HIS A O     1 
ATOM   5859 C CB    . HIS A 1 917  ? 160.599 189.028 129.307 1.00 55.60  ? 917  HIS A CB    1 
ATOM   5860 C CG    . HIS A 1 917  ? 160.840 190.287 130.081 1.00 63.87  ? 917  HIS A CG    1 
ATOM   5861 N ND1   . HIS A 1 917  ? 161.300 190.287 131.381 1.00 57.98  ? 917  HIS A ND1   1 
ATOM   5862 C CD2   . HIS A 1 917  ? 160.688 191.588 129.737 1.00 68.71  ? 917  HIS A CD2   1 
ATOM   5863 C CE1   . HIS A 1 917  ? 161.418 191.533 131.804 1.00 60.75  ? 917  HIS A CE1   1 
ATOM   5864 N NE2   . HIS A 1 917  ? 161.054 192.341 130.825 1.00 67.58  ? 917  HIS A NE2   1 
ATOM   5865 N N     . THR A 1 918  ? 159.478 185.754 129.295 1.00 57.31  ? 918  THR A N     1 
ATOM   5866 C CA    . THR A 1 918  ? 159.298 184.627 128.390 1.00 59.61  ? 918  THR A CA    1 
ATOM   5867 C C     . THR A 1 918  ? 158.105 183.758 128.767 1.00 62.60  ? 918  THR A C     1 
ATOM   5868 O O     . THR A 1 918  ? 157.215 183.540 127.941 1.00 69.79  ? 918  THR A O     1 
ATOM   5869 C CB    . THR A 1 918  ? 160.579 183.781 128.351 1.00 59.67  ? 918  THR A CB    1 
ATOM   5870 O OG1   . THR A 1 918  ? 161.667 184.581 127.871 1.00 60.27  ? 918  THR A OG1   1 
ATOM   5871 C CG2   . THR A 1 918  ? 160.397 182.581 127.436 1.00 58.37  ? 918  THR A CG2   1 
ATOM   5872 N N     . SER A 1 919  ? 158.057 183.253 130.001 1.00 58.27  ? 919  SER A N     1 
ATOM   5873 C CA    . SER A 1 919  ? 157.052 182.271 130.379 1.00 60.57  ? 919  SER A CA    1 
ATOM   5874 C C     . SER A 1 919  ? 156.215 182.651 131.591 1.00 58.86  ? 919  SER A C     1 
ATOM   5875 O O     . SER A 1 919  ? 155.201 181.988 131.838 1.00 59.54  ? 919  SER A O     1 
ATOM   5876 C CB    . SER A 1 919  ? 157.712 180.910 130.646 1.00 59.84  ? 919  SER A CB    1 
ATOM   5877 O OG    . SER A 1 919  ? 158.705 181.013 131.652 1.00 58.15  ? 919  SER A OG    1 
ATOM   5878 N N     . LYS A 1 920  ? 156.595 183.683 132.346 1.00 55.96  ? 920  LYS A N     1 
ATOM   5879 C CA    . LYS A 1 920  ? 155.871 184.092 133.553 1.00 57.38  ? 920  LYS A CA    1 
ATOM   5880 C C     . LYS A 1 920  ? 155.752 182.937 134.545 1.00 55.97  ? 920  LYS A C     1 
ATOM   5881 O O     . LYS A 1 920  ? 154.697 182.709 135.139 1.00 57.18  ? 920  LYS A O     1 
ATOM   5882 C CB    . LYS A 1 920  ? 154.488 184.660 133.215 1.00 54.35  ? 920  LYS A CB    1 
ATOM   5883 C CG    . LYS A 1 920  ? 154.503 186.027 132.542 1.00 59.38  ? 920  LYS A CG    1 
ATOM   5884 C CD    . LYS A 1 920  ? 154.743 185.924 131.044 1.00 65.16  ? 920  LYS A CD    1 
ATOM   5885 C CE    . LYS A 1 920  ? 154.709 187.292 130.384 1.00 62.97  ? 920  LYS A CE    1 
ATOM   5886 N NZ    . LYS A 1 920  ? 154.938 187.206 128.916 1.00 67.17  ? 920  LYS A NZ    1 
ATOM   5887 N N     . ASP A 1 921  ? 156.842 182.197 134.718 1.00 51.59  ? 921  ASP A N     1 
ATOM   5888 C CA    . ASP A 1 921  ? 156.879 181.079 135.647 1.00 47.25  ? 921  ASP A CA    1 
ATOM   5889 C C     . ASP A 1 921  ? 157.296 181.548 137.037 1.00 47.84  ? 921  ASP A C     1 
ATOM   5890 O O     . ASP A 1 921  ? 157.816 182.649 137.224 1.00 49.29  ? 921  ASP A O     1 
ATOM   5891 C CB    . ASP A 1 921  ? 157.835 179.997 135.147 1.00 50.77  ? 921  ASP A CB    1 
ATOM   5892 C CG    . ASP A 1 921  ? 157.326 179.293 133.907 1.00 58.02  ? 921  ASP A CG    1 
ATOM   5893 O OD1   . ASP A 1 921  ? 156.093 179.179 133.746 1.00 57.87  ? 921  ASP A OD1   1 
ATOM   5894 O OD2   . ASP A 1 921  ? 158.163 178.847 133.095 1.00 59.47  ? 921  ASP A OD2   1 
ATOM   5895 N N     . LYS A 1 922  ? 157.064 180.687 138.022 1.00 46.37  ? 922  LYS A N     1 
ATOM   5896 C CA    . LYS A 1 922  ? 157.458 180.950 139.397 1.00 38.77  ? 922  LYS A CA    1 
ATOM   5897 C C     . LYS A 1 922  ? 158.800 180.293 139.684 1.00 36.10  ? 922  LYS A C     1 
ATOM   5898 O O     . LYS A 1 922  ? 159.080 179.189 139.210 1.00 35.87  ? 922  LYS A O     1 
ATOM   5899 C CB    . LYS A 1 922  ? 156.402 180.445 140.378 1.00 41.81  ? 922  LYS A CB    1 
ATOM   5900 C CG    . LYS A 1 922  ? 155.054 181.104 140.200 1.00 41.99  ? 922  LYS A CG    1 
ATOM   5901 C CD    . LYS A 1 922  ? 154.092 180.701 141.294 1.00 47.32  ? 922  LYS A CD    1 
ATOM   5902 C CE    . LYS A 1 922  ? 152.726 181.300 141.042 1.00 51.32  ? 922  LYS A CE    1 
ATOM   5903 N NZ    . LYS A 1 922  ? 152.813 182.770 140.835 1.00 57.07  ? 922  LYS A NZ    1 
ATOM   5904 N N     . VAL A 1 923  ? 159.626 180.982 140.465 1.00 33.37  ? 923  VAL A N     1 
ATOM   5905 C CA    . VAL A 1 923  ? 161.012 180.601 140.695 1.00 29.31  ? 923  VAL A CA    1 
ATOM   5906 C C     . VAL A 1 923  ? 161.229 180.391 142.186 1.00 29.39  ? 923  VAL A C     1 
ATOM   5907 O O     . VAL A 1 923  ? 160.774 181.193 143.008 1.00 32.43  ? 923  VAL A O     1 
ATOM   5908 C CB    . VAL A 1 923  ? 161.981 181.670 140.149 1.00 28.91  ? 923  VAL A CB    1 
ATOM   5909 C CG1   . VAL A 1 923  ? 163.418 181.275 140.414 1.00 30.82  ? 923  VAL A CG1   1 
ATOM   5910 C CG2   . VAL A 1 923  ? 161.747 181.889 138.665 1.00 30.21  ? 923  VAL A CG2   1 
ATOM   5911 N N     . ILE A 1 924  ? 161.918 179.307 142.531 1.00 31.90  ? 924  ILE A N     1 
ATOM   5912 C CA    . ILE A 1 924  ? 162.349 179.036 143.897 1.00 29.88  ? 924  ILE A CA    1 
ATOM   5913 C C     . ILE A 1 924  ? 163.859 179.206 143.946 1.00 27.04  ? 924  ILE A C     1 
ATOM   5914 O O     . ILE A 1 924  ? 164.588 178.551 143.193 1.00 30.20  ? 924  ILE A O     1 
ATOM   5915 C CB    . ILE A 1 924  ? 161.946 177.628 144.360 1.00 28.44  ? 924  ILE A CB    1 
ATOM   5916 C CG1   . ILE A 1 924  ? 160.465 177.377 144.098 1.00 34.78  ? 924  ILE A CG1   1 
ATOM   5917 C CG2   . ILE A 1 924  ? 162.249 177.452 145.835 1.00 27.04  ? 924  ILE A CG2   1 
ATOM   5918 C CD1   . ILE A 1 924  ? 160.029 175.972 144.432 1.00 34.87  ? 924  ILE A CD1   1 
ATOM   5919 N N     . ILE A 1 925  ? 164.328 180.083 144.826 1.00 27.82  ? 925  ILE A N     1 
ATOM   5920 C CA    . ILE A 1 925  ? 165.752 180.300 145.042 1.00 26.33  ? 925  ILE A CA    1 
ATOM   5921 C C     . ILE A 1 925  ? 166.107 179.698 146.391 1.00 29.78  ? 925  ILE A C     1 
ATOM   5922 O O     . ILE A 1 925  ? 165.568 180.110 147.425 1.00 31.17  ? 925  ILE A O     1 
ATOM   5923 C CB    . ILE A 1 925  ? 166.116 181.790 144.982 1.00 27.59  ? 925  ILE A CB    1 
ATOM   5924 C CG1   . ILE A 1 925  ? 165.648 182.393 143.659 1.00 30.73  ? 925  ILE A CG1   1 
ATOM   5925 C CG2   . ILE A 1 925  ? 167.616 181.979 145.155 1.00 25.18  ? 925  ILE A CG2   1 
ATOM   5926 C CD1   . ILE A 1 925  ? 165.977 183.852 143.509 1.00 27.37  ? 925  ILE A CD1   1 
ATOM   5927 N N     . PHE A 1 926  ? 167.006 178.719 146.382 1.00 31.39  ? 926  PHE A N     1 
ATOM   5928 C CA    . PHE A 1 926  ? 167.405 178.014 147.592 1.00 26.88  ? 926  PHE A CA    1 
ATOM   5929 C C     . PHE A 1 926  ? 168.721 178.583 148.101 1.00 31.89  ? 926  PHE A C     1 
ATOM   5930 O O     . PHE A 1 926  ? 169.741 178.517 147.408 1.00 33.68  ? 926  PHE A O     1 
ATOM   5931 C CB    . PHE A 1 926  ? 167.534 176.515 147.336 1.00 26.72  ? 926  PHE A CB    1 
ATOM   5932 C CG    . PHE A 1 926  ? 166.224 175.792 147.320 1.00 27.45  ? 926  PHE A CG    1 
ATOM   5933 C CD1   . PHE A 1 926  ? 165.542 175.552 148.497 1.00 29.96  ? 926  PHE A CD1   1 
ATOM   5934 C CD2   . PHE A 1 926  ? 165.674 175.352 146.132 1.00 26.39  ? 926  PHE A CD2   1 
ATOM   5935 C CE1   . PHE A 1 926  ? 164.338 174.891 148.492 1.00 30.70  ? 926  PHE A CE1   1 
ATOM   5936 C CE2   . PHE A 1 926  ? 164.469 174.687 146.122 1.00 29.52  ? 926  PHE A CE2   1 
ATOM   5937 C CZ    . PHE A 1 926  ? 163.800 174.458 147.305 1.00 32.55  ? 926  PHE A CZ    1 
ATOM   5938 N N     . THR A 1 927  ? 168.690 179.140 149.307 1.00 33.47  ? 927  THR A N     1 
ATOM   5939 C CA    . THR A 1 927  ? 169.890 179.617 149.974 1.00 32.08  ? 927  THR A CA    1 
ATOM   5940 C C     . THR A 1 927  ? 169.620 179.628 151.470 1.00 35.71  ? 927  THR A C     1 
ATOM   5941 O O     . THR A 1 927  ? 168.537 180.026 151.905 1.00 45.71  ? 927  THR A O     1 
ATOM   5942 C CB    . THR A 1 927  ? 170.302 181.011 149.479 1.00 33.21  ? 927  THR A CB    1 
ATOM   5943 O OG1   . THR A 1 927  ? 171.213 181.606 150.411 1.00 32.63  ? 927  THR A OG1   1 
ATOM   5944 C CG2   . THR A 1 927  ? 169.089 181.906 149.308 1.00 34.19  ? 927  THR A CG2   1 
ATOM   5945 N N     . GLU A 1 928  ? 170.603 179.176 152.247 1.00 37.10  ? 928  GLU A N     1 
ATOM   5946 C CA    . GLU A 1 928  ? 170.451 179.052 153.690 1.00 35.24  ? 928  GLU A CA    1 
ATOM   5947 C C     . GLU A 1 928  ? 170.950 180.267 154.457 1.00 37.67  ? 928  GLU A C     1 
ATOM   5948 O O     . GLU A 1 928  ? 170.585 180.433 155.625 1.00 43.78  ? 928  GLU A O     1 
ATOM   5949 C CB    . GLU A 1 928  ? 171.188 177.805 154.197 1.00 40.47  ? 928  GLU A CB    1 
ATOM   5950 C CG    . GLU A 1 928  ? 172.710 177.865 154.065 1.00 47.71  ? 928  GLU A CG    1 
ATOM   5951 C CD    . GLU A 1 928  ? 173.201 177.593 152.652 1.00 58.23  ? 928  GLU A CD    1 
ATOM   5952 O OE1   . GLU A 1 928  ? 172.393 177.149 151.810 1.00 55.45  ? 928  GLU A OE1   1 
ATOM   5953 O OE2   . GLU A 1 928  ? 174.399 177.823 152.384 1.00 59.24  ? 928  GLU A OE2   1 
ATOM   5954 N N     . LEU A 1 929  ? 171.765 181.113 153.833 1.00 37.28  ? 929  LEU A N     1 
ATOM   5955 C CA    . LEU A 1 929  ? 172.351 182.262 154.509 1.00 31.95  ? 929  LEU A CA    1 
ATOM   5956 C C     . LEU A 1 929  ? 171.325 183.385 154.591 1.00 31.13  ? 929  LEU A C     1 
ATOM   5957 O O     . LEU A 1 929  ? 170.793 183.821 153.565 1.00 36.74  ? 929  LEU A O     1 
ATOM   5958 C CB    . LEU A 1 929  ? 173.603 182.719 153.766 1.00 32.50  ? 929  LEU A CB    1 
ATOM   5959 C CG    . LEU A 1 929  ? 174.606 181.601 153.474 1.00 31.85  ? 929  LEU A CG    1 
ATOM   5960 C CD1   . LEU A 1 929  ? 175.636 182.046 152.457 1.00 31.51  ? 929  LEU A CD1   1 
ATOM   5961 C CD2   . LEU A 1 929  ? 175.283 181.142 154.752 1.00 31.61  ? 929  LEU A CD2   1 
ATOM   5962 N N     . ARG A 1 930  ? 171.052 183.855 155.811 1.00 29.97  ? 930  ARG A N     1 
ATOM   5963 C CA    . ARG A 1 930  ? 170.036 184.886 156.002 1.00 27.45  ? 930  ARG A CA    1 
ATOM   5964 C C     . ARG A 1 930  ? 170.436 186.195 155.334 1.00 25.28  ? 930  ARG A C     1 
ATOM   5965 O O     . ARG A 1 930  ? 169.611 186.845 154.680 1.00 29.83  ? 930  ARG A O     1 
ATOM   5966 C CB    . ARG A 1 930  ? 169.781 185.105 157.494 1.00 33.08  ? 930  ARG A CB    1 
ATOM   5967 C CG    . ARG A 1 930  ? 168.679 184.240 158.091 1.00 33.47  ? 930  ARG A CG    1 
ATOM   5968 C CD    . ARG A 1 930  ? 169.028 182.768 158.057 1.00 32.47  ? 930  ARG A CD    1 
ATOM   5969 N NE    . ARG A 1 930  ? 168.052 181.959 158.775 1.00 35.15  ? 930  ARG A NE    1 
ATOM   5970 C CZ    . ARG A 1 930  ? 168.104 180.638 158.870 1.00 45.05  ? 930  ARG A CZ    1 
ATOM   5971 N NH1   . ARG A 1 930  ? 169.068 179.942 158.291 1.00 43.81  ? 930  ARG A NH1   1 
ATOM   5972 N NH2   . ARG A 1 930  ? 167.166 180.000 159.564 1.00 48.75  ? 930  ARG A NH2   1 
ATOM   5973 N N     . ASP A 1 931  ? 171.697 186.602 155.490 1.00 25.46  ? 931  ASP A N     1 
ATOM   5974 C CA    . ASP A 1 931  ? 172.151 187.842 154.868 1.00 25.88  ? 931  ASP A CA    1 
ATOM   5975 C C     . ASP A 1 931  ? 172.102 187.745 153.350 1.00 29.35  ? 931  ASP A C     1 
ATOM   5976 O O     . ASP A 1 931  ? 171.716 188.704 152.670 1.00 30.33  ? 931  ASP A O     1 
ATOM   5977 C CB    . ASP A 1 931  ? 173.560 188.185 155.350 1.00 28.98  ? 931  ASP A CB    1 
ATOM   5978 C CG    . ASP A 1 931  ? 174.446 186.964 155.477 1.00 41.07  ? 931  ASP A CG    1 
ATOM   5979 O OD1   . ASP A 1 931  ? 173.907 185.854 155.658 1.00 36.57  ? 931  ASP A OD1   1 
ATOM   5980 O OD2   . ASP A 1 931  ? 175.683 187.115 155.403 1.00 50.45  ? 931  ASP A OD2   1 
ATOM   5981 N N     . LEU A 1 932  ? 172.481 186.591 152.798 1.00 29.21  ? 932  LEU A N     1 
ATOM   5982 C CA    . LEU A 1 932  ? 172.381 186.398 151.356 1.00 24.11  ? 932  LEU A CA    1 
ATOM   5983 C C     . LEU A 1 932  ? 170.929 186.390 150.900 1.00 26.73  ? 932  LEU A C     1 
ATOM   5984 O O     . LEU A 1 932  ? 170.612 186.899 149.820 1.00 31.19  ? 932  LEU A O     1 
ATOM   5985 C CB    . LEU A 1 932  ? 173.083 185.105 150.948 1.00 27.66  ? 932  LEU A CB    1 
ATOM   5986 C CG    . LEU A 1 932  ? 173.106 184.824 149.444 1.00 36.58  ? 932  LEU A CG    1 
ATOM   5987 C CD1   . LEU A 1 932  ? 173.791 185.955 148.700 1.00 33.14  ? 932  LEU A CD1   1 
ATOM   5988 C CD2   . LEU A 1 932  ? 173.788 183.505 149.157 1.00 31.57  ? 932  LEU A CD2   1 
ATOM   5989 N N     . GLN A 1 933  ? 170.031 185.815 151.704 1.00 25.43  ? 933  GLN A N     1 
ATOM   5990 C CA    . GLN A 1 933  ? 168.609 185.868 151.380 1.00 22.96  ? 933  GLN A CA    1 
ATOM   5991 C C     . GLN A 1 933  ? 168.112 187.306 151.326 1.00 27.71  ? 933  GLN A C     1 
ATOM   5992 O O     . GLN A 1 933  ? 167.367 187.680 150.412 1.00 30.03  ? 933  GLN A O     1 
ATOM   5993 C CB    . GLN A 1 933  ? 167.804 185.064 152.401 1.00 25.77  ? 933  GLN A CB    1 
ATOM   5994 C CG    . GLN A 1 933  ? 167.939 183.562 152.266 1.00 29.23  ? 933  GLN A CG    1 
ATOM   5995 C CD    . GLN A 1 933  ? 167.271 182.812 153.399 1.00 32.73  ? 933  GLN A CD    1 
ATOM   5996 O OE1   . GLN A 1 933  ? 167.054 183.360 154.477 1.00 35.03  ? 933  GLN A OE1   1 
ATOM   5997 N NE2   . GLN A 1 933  ? 166.940 181.550 153.159 1.00 36.80  ? 933  GLN A NE2   1 
ATOM   5998 N N     . ARG A 1 934  ? 168.524 188.131 152.291 1.00 27.78  ? 934  ARG A N     1 
ATOM   5999 C CA    . ARG A 1 934  ? 168.126 189.536 152.282 1.00 24.59  ? 934  ARG A CA    1 
ATOM   6000 C C     . ARG A 1 934  ? 168.700 190.269 151.075 1.00 26.20  ? 934  ARG A C     1 
ATOM   6001 O O     . ARG A 1 934  ? 168.017 191.097 150.461 1.00 30.52  ? 934  ARG A O     1 
ATOM   6002 C CB    . ARG A 1 934  ? 168.561 190.216 153.578 1.00 27.59  ? 934  ARG A CB    1 
ATOM   6003 C CG    . ARG A 1 934  ? 167.916 189.644 154.826 1.00 27.38  ? 934  ARG A CG    1 
ATOM   6004 C CD    . ARG A 1 934  ? 168.185 190.517 156.037 1.00 24.68  ? 934  ARG A CD    1 
ATOM   6005 N NE    . ARG A 1 934  ? 169.608 190.694 156.297 1.00 24.62  ? 934  ARG A NE    1 
ATOM   6006 C CZ    . ARG A 1 934  ? 170.315 189.948 157.133 1.00 24.04  ? 934  ARG A CZ    1 
ATOM   6007 N NH1   . ARG A 1 934  ? 169.763 188.950 157.802 1.00 20.71  ? 934  ARG A NH1   1 
ATOM   6008 N NH2   . ARG A 1 934  ? 171.608 190.209 157.301 1.00 23.52  ? 934  ARG A NH2   1 
ATOM   6009 N N     . GLU A 1 935  ? 169.956 189.983 150.721 1.00 27.89  ? 935  GLU A N     1 
ATOM   6010 C CA    . GLU A 1 935  ? 170.556 190.634 149.558 1.00 29.67  ? 935  GLU A CA    1 
ATOM   6011 C C     . GLU A 1 935  ? 169.836 190.249 148.270 1.00 30.33  ? 935  GLU A C     1 
ATOM   6012 O O     . GLU A 1 935  ? 169.562 191.107 147.421 1.00 32.22  ? 935  GLU A O     1 
ATOM   6013 C CB    . GLU A 1 935  ? 172.042 190.285 149.465 1.00 31.74  ? 935  GLU A CB    1 
ATOM   6014 C CG    . GLU A 1 935  ? 172.885 190.853 150.593 1.00 42.18  ? 935  GLU A CG    1 
ATOM   6015 C CD    . GLU A 1 935  ? 172.901 192.369 150.608 1.00 53.42  ? 935  GLU A CD    1 
ATOM   6016 O OE1   . GLU A 1 935  ? 172.756 192.981 149.529 1.00 51.26  ? 935  GLU A OE1   1 
ATOM   6017 O OE2   . GLU A 1 935  ? 173.057 192.949 151.702 1.00 53.34  ? 935  GLU A OE2   1 
ATOM   6018 N N     . LEU A 1 936  ? 169.525 188.961 148.106 1.00 30.20  ? 936  LEU A N     1 
ATOM   6019 C CA    . LEU A 1 936  ? 168.794 188.520 146.923 1.00 22.24  ? 936  LEU A CA    1 
ATOM   6020 C C     . LEU A 1 936  ? 167.408 189.142 146.874 1.00 25.48  ? 936  LEU A C     1 
ATOM   6021 O O     . LEU A 1 936  ? 166.945 189.562 145.807 1.00 29.89  ? 936  LEU A O     1 
ATOM   6022 C CB    . LEU A 1 936  ? 168.693 186.996 146.900 1.00 21.66  ? 936  LEU A CB    1 
ATOM   6023 C CG    . LEU A 1 936  ? 169.997 186.209 146.785 1.00 24.36  ? 936  LEU A CG    1 
ATOM   6024 C CD1   . LEU A 1 936  ? 169.703 184.726 146.687 1.00 24.79  ? 936  LEU A CD1   1 
ATOM   6025 C CD2   . LEU A 1 936  ? 170.814 186.681 145.597 1.00 26.18  ? 936  LEU A CD2   1 
ATOM   6026 N N     . GLN A 1 937  ? 166.729 189.209 148.022 1.00 27.07  ? 937  GLN A N     1 
ATOM   6027 C CA    . GLN A 1 937  ? 165.413 189.833 148.072 1.00 26.39  ? 937  GLN A CA    1 
ATOM   6028 C C     . GLN A 1 937  ? 165.485 191.301 147.677 1.00 27.43  ? 937  GLN A C     1 
ATOM   6029 O O     . GLN A 1 937  ? 164.634 191.790 146.927 1.00 28.16  ? 937  GLN A O     1 
ATOM   6030 C CB    . GLN A 1 937  ? 164.826 189.681 149.473 1.00 22.93  ? 937  GLN A CB    1 
ATOM   6031 C CG    . GLN A 1 937  ? 163.455 190.289 149.649 1.00 26.90  ? 937  GLN A CG    1 
ATOM   6032 C CD    . GLN A 1 937  ? 162.998 190.247 151.087 1.00 30.06  ? 937  GLN A CD    1 
ATOM   6033 O OE1   . GLN A 1 937  ? 163.704 190.701 151.985 1.00 31.85  ? 937  GLN A OE1   1 
ATOM   6034 N NE2   . GLN A 1 937  ? 161.817 189.689 151.317 1.00 33.42  ? 937  GLN A NE2   1 
ATOM   6035 N N     . HIS A 1 938  ? 166.498 192.018 148.167 1.00 28.82  ? 938  HIS A N     1 
ATOM   6036 C CA    . HIS A 1 938  ? 166.645 193.427 147.821 1.00 25.82  ? 938  HIS A CA    1 
ATOM   6037 C C     . HIS A 1 938  ? 166.922 193.611 146.334 1.00 32.13  ? 938  HIS A C     1 
ATOM   6038 O O     . HIS A 1 938  ? 166.358 194.508 145.698 1.00 36.55  ? 938  HIS A O     1 
ATOM   6039 C CB    . HIS A 1 938  ? 167.762 194.055 148.651 1.00 28.86  ? 938  HIS A CB    1 
ATOM   6040 C CG    . HIS A 1 938  ? 167.926 195.526 148.428 1.00 33.36  ? 938  HIS A CG    1 
ATOM   6041 N ND1   . HIS A 1 938  ? 166.882 196.417 148.549 1.00 29.56  ? 938  HIS A ND1   1 
ATOM   6042 C CD2   . HIS A 1 938  ? 169.013 196.262 148.097 1.00 31.30  ? 938  HIS A CD2   1 
ATOM   6043 C CE1   . HIS A 1 938  ? 167.318 197.638 148.299 1.00 30.81  ? 938  HIS A CE1   1 
ATOM   6044 N NE2   . HIS A 1 938  ? 168.607 197.572 148.023 1.00 31.56  ? 938  HIS A NE2   1 
ATOM   6045 N N     . ALA A 1 939  ? 167.796 192.778 145.764 1.00 34.13  ? 939  ALA A N     1 
ATOM   6046 C CA    . ALA A 1 939  ? 168.098 192.895 144.340 1.00 28.58  ? 939  ALA A CA    1 
ATOM   6047 C C     . ALA A 1 939  ? 166.873 192.588 143.487 1.00 29.55  ? 939  ALA A C     1 
ATOM   6048 O O     . ALA A 1 939  ? 166.599 193.287 142.501 1.00 37.61  ? 939  ALA A O     1 
ATOM   6049 C CB    . ALA A 1 939  ? 169.257 191.973 143.970 1.00 28.66  ? 939  ALA A CB    1 
ATOM   6050 N N     . ILE A 1 940  ? 166.118 191.549 143.853 1.00 27.74  ? 940  ILE A N     1 
ATOM   6051 C CA    . ILE A 1 940  ? 164.911 191.207 143.107 1.00 31.28  ? 940  ILE A CA    1 
ATOM   6052 C C     . ILE A 1 940  ? 163.873 192.314 143.236 1.00 35.91  ? 940  ILE A C     1 
ATOM   6053 O O     . ILE A 1 940  ? 163.172 192.638 142.273 1.00 38.83  ? 940  ILE A O     1 
ATOM   6054 C CB    . ILE A 1 940  ? 164.357 189.848 143.575 1.00 30.81  ? 940  ILE A CB    1 
ATOM   6055 C CG1   . ILE A 1 940  ? 165.333 188.727 143.224 1.00 31.25  ? 940  ILE A CG1   1 
ATOM   6056 C CG2   . ILE A 1 940  ? 163.001 189.575 142.947 1.00 28.66  ? 940  ILE A CG2   1 
ATOM   6057 C CD1   . ILE A 1 940  ? 164.958 187.392 143.814 1.00 26.20  ? 940  ILE A CD1   1 
ATOM   6058 N N     . HIS A 1 941  ? 163.757 192.912 144.424 1.00 37.98  ? 941  HIS A N     1 
ATOM   6059 C CA    . HIS A 1 941  ? 162.827 194.022 144.599 1.00 35.41  ? 941  HIS A CA    1 
ATOM   6060 C C     . HIS A 1 941  ? 163.228 195.216 143.744 1.00 38.12  ? 941  HIS A C     1 
ATOM   6061 O O     . HIS A 1 941  ? 162.374 195.856 143.119 1.00 43.72  ? 941  HIS A O     1 
ATOM   6062 C CB    . HIS A 1 941  ? 162.757 194.420 146.072 1.00 35.05  ? 941  HIS A CB    1 
ATOM   6063 C CG    . HIS A 1 941  ? 161.888 195.609 146.335 1.00 43.36  ? 941  HIS A CG    1 
ATOM   6064 N ND1   . HIS A 1 941  ? 160.525 195.594 146.131 1.00 46.13  ? 941  HIS A ND1   1 
ATOM   6065 C CD2   . HIS A 1 941  ? 162.187 196.851 146.784 1.00 38.81  ? 941  HIS A CD2   1 
ATOM   6066 C CE1   . HIS A 1 941  ? 160.022 196.774 146.444 1.00 43.06  ? 941  HIS A CE1   1 
ATOM   6067 N NE2   . HIS A 1 941  ? 161.009 197.555 146.843 1.00 48.09  ? 941  HIS A NE2   1 
ATOM   6068 N N     . GLN A 1 942  ? 164.523 195.532 143.706 1.00 34.40  ? 942  GLN A N     1 
ATOM   6069 C CA    . GLN A 1 942  ? 164.980 196.673 142.921 1.00 35.77  ? 942  GLN A CA    1 
ATOM   6070 C C     . GLN A 1 942  ? 164.754 196.453 141.431 1.00 41.81  ? 942  GLN A C     1 
ATOM   6071 O O     . GLN A 1 942  ? 164.310 197.364 140.724 1.00 47.21  ? 942  GLN A O     1 
ATOM   6072 C CB    . GLN A 1 942  ? 166.457 196.946 143.198 1.00 36.74  ? 942  GLN A CB    1 
ATOM   6073 C CG    . GLN A 1 942  ? 166.733 197.591 144.542 1.00 39.50  ? 942  GLN A CG    1 
ATOM   6074 C CD    . GLN A 1 942  ? 168.189 197.980 144.706 1.00 49.06  ? 942  GLN A CD    1 
ATOM   6075 O OE1   . GLN A 1 942  ? 169.083 197.318 144.180 1.00 38.48  ? 942  GLN A OE1   1 
ATOM   6076 N NE2   . GLN A 1 942  ? 168.433 199.066 145.429 1.00 49.38  ? 942  GLN A NE2   1 
ATOM   6077 N N     . ASN A 1 943  ? 165.054 195.254 140.934 1.00 41.01  ? 943  ASN A N     1 
ATOM   6078 C CA    . ASN A 1 943  ? 165.001 195.005 139.500 1.00 39.12  ? 943  ASN A CA    1 
ATOM   6079 C C     . ASN A 1 943  ? 163.643 194.519 139.008 1.00 40.27  ? 943  ASN A C     1 
ATOM   6080 O O     . ASN A 1 943  ? 163.434 194.454 137.792 1.00 39.41  ? 943  ASN A O     1 
ATOM   6081 C CB    . ASN A 1 943  ? 166.077 193.990 139.106 1.00 38.47  ? 943  ASN A CB    1 
ATOM   6082 C CG    . ASN A 1 943  ? 167.471 194.570 139.170 1.00 39.48  ? 943  ASN A CG    1 
ATOM   6083 O OD1   . ASN A 1 943  ? 168.033 194.973 138.154 1.00 42.44  ? 943  ASN A OD1   1 
ATOM   6084 N ND2   . ASN A 1 943  ? 168.034 194.627 140.371 1.00 37.64  ? 943  ASN A ND2   1 
ATOM   6085 N N     . PHE A 1 944  ? 162.719 194.181 139.904 1.00 39.53  ? 944  PHE A N     1 
ATOM   6086 C CA    . PHE A 1 944  ? 161.440 193.626 139.481 1.00 41.19  ? 944  PHE A CA    1 
ATOM   6087 C C     . PHE A 1 944  ? 160.233 194.190 140.215 1.00 52.69  ? 944  PHE A C     1 
ATOM   6088 O O     . PHE A 1 944  ? 159.106 193.862 139.833 1.00 56.89  ? 944  PHE A O     1 
ATOM   6089 C CB    . PHE A 1 944  ? 161.456 192.098 139.634 1.00 40.24  ? 944  PHE A CB    1 
ATOM   6090 C CG    . PHE A 1 944  ? 162.573 191.433 138.881 1.00 41.08  ? 944  PHE A CG    1 
ATOM   6091 C CD1   . PHE A 1 944  ? 162.417 191.081 137.552 1.00 42.71  ? 944  PHE A CD1   1 
ATOM   6092 C CD2   . PHE A 1 944  ? 163.787 191.178 139.496 1.00 36.23  ? 944  PHE A CD2   1 
ATOM   6093 C CE1   . PHE A 1 944  ? 163.445 190.480 136.858 1.00 37.96  ? 944  PHE A CE1   1 
ATOM   6094 C CE2   . PHE A 1 944  ? 164.818 190.577 138.804 1.00 32.57  ? 944  PHE A CE2   1 
ATOM   6095 C CZ    . PHE A 1 944  ? 164.647 190.229 137.484 1.00 31.97  ? 944  PHE A CZ    1 
ATOM   6096 N N     . GLY A 1 945  ? 160.414 195.018 141.241 1.00 50.47  ? 945  GLY A N     1 
ATOM   6097 C CA    . GLY A 1 945  ? 159.306 195.723 141.849 1.00 45.57  ? 945  GLY A CA    1 
ATOM   6098 C C     . GLY A 1 945  ? 158.524 194.967 142.898 1.00 53.32  ? 945  GLY A C     1 
ATOM   6099 O O     . GLY A 1 945  ? 157.468 195.451 143.319 1.00 61.21  ? 945  GLY A O     1 
ATOM   6100 N N     . PHE A 1 946  ? 158.992 193.799 143.332 1.00 44.66  ? 946  PHE A N     1 
ATOM   6101 C CA    . PHE A 1 946  ? 158.323 193.081 144.408 1.00 46.40  ? 946  PHE A CA    1 
ATOM   6102 C C     . PHE A 1 946  ? 159.362 192.350 145.244 1.00 43.17  ? 946  PHE A C     1 
ATOM   6103 O O     . PHE A 1 946  ? 160.405 191.930 144.738 1.00 44.59  ? 946  PHE A O     1 
ATOM   6104 C CB    . PHE A 1 946  ? 157.272 192.099 143.872 1.00 43.79  ? 946  PHE A CB    1 
ATOM   6105 C CG    . PHE A 1 946  ? 157.849 190.850 143.269 1.00 42.88  ? 946  PHE A CG    1 
ATOM   6106 C CD1   . PHE A 1 946  ? 158.353 190.855 141.983 1.00 44.53  ? 946  PHE A CD1   1 
ATOM   6107 C CD2   . PHE A 1 946  ? 157.866 189.664 143.984 1.00 38.77  ? 946  PHE A CD2   1 
ATOM   6108 C CE1   . PHE A 1 946  ? 158.877 189.707 141.427 1.00 46.18  ? 946  PHE A CE1   1 
ATOM   6109 C CE2   . PHE A 1 946  ? 158.387 188.515 143.433 1.00 29.76  ? 946  PHE A CE2   1 
ATOM   6110 C CZ    . PHE A 1 946  ? 158.893 188.536 142.154 1.00 37.17  ? 946  PHE A CZ    1 
ATOM   6111 N N     . ARG A 1 947  ? 159.063 192.202 146.533 1.00 35.74  ? 947  ARG A N     1 
ATOM   6112 C CA    . ARG A 1 947  ? 159.976 191.550 147.461 1.00 32.48  ? 947  ARG A CA    1 
ATOM   6113 C C     . ARG A 1 947  ? 159.621 190.076 147.581 1.00 33.98  ? 947  ARG A C     1 
ATOM   6114 O O     . ARG A 1 947  ? 158.531 189.753 148.070 1.00 36.59  ? 947  ARG A O     1 
ATOM   6115 C CB    . ARG A 1 947  ? 159.914 192.209 148.828 1.00 33.45  ? 947  ARG A CB    1 
ATOM   6116 C CG    . ARG A 1 947  ? 160.351 193.661 148.835 1.00 43.27  ? 947  ARG A CG    1 
ATOM   6117 C CD    . ARG A 1 947  ? 159.950 194.372 150.119 1.00 41.63  ? 947  ARG A CD    1 
ATOM   6118 N NE    . ARG A 1 947  ? 160.760 193.974 151.263 1.00 45.00  ? 947  ARG A NE    1 
ATOM   6119 C CZ    . ARG A 1 947  ? 160.381 193.100 152.185 1.00 45.81  ? 947  ARG A CZ    1 
ATOM   6120 N NH1   . ARG A 1 947  ? 159.210 192.490 152.120 1.00 46.13  ? 947  ARG A NH1   1 
ATOM   6121 N NH2   . ARG A 1 947  ? 161.197 192.834 153.201 1.00 38.48  ? 947  ARG A NH2   1 
ATOM   6122 N N     . PRO A 1 948  ? 160.486 189.160 147.150 1.00 30.71  ? 948  PRO A N     1 
ATOM   6123 C CA    . PRO A 1 948  ? 160.217 187.736 147.369 1.00 30.64  ? 948  PRO A CA    1 
ATOM   6124 C C     . PRO A 1 948  ? 160.151 187.412 148.855 1.00 34.85  ? 948  PRO A C     1 
ATOM   6125 O O     . PRO A 1 948  ? 160.880 187.983 149.668 1.00 31.92  ? 948  PRO A O     1 
ATOM   6126 C CB    . PRO A 1 948  ? 161.401 187.041 146.689 1.00 28.82  ? 948  PRO A CB    1 
ATOM   6127 C CG    . PRO A 1 948  ? 162.463 188.079 146.605 1.00 27.55  ? 948  PRO A CG    1 
ATOM   6128 C CD    . PRO A 1 948  ? 161.751 189.380 146.431 1.00 29.19  ? 948  PRO A CD    1 
ATOM   6129 N N     . VAL A 1 949  ? 159.264 186.486 149.203 1.00 38.23  ? 949  VAL A N     1 
ATOM   6130 C CA    . VAL A 1 949  ? 159.056 186.112 150.597 1.00 35.37  ? 949  VAL A CA    1 
ATOM   6131 C C     . VAL A 1 949  ? 160.133 185.115 151.007 1.00 37.17  ? 949  VAL A C     1 
ATOM   6132 O O     . VAL A 1 949  ? 160.312 184.079 150.361 1.00 44.02  ? 949  VAL A O     1 
ATOM   6133 C CB    . VAL A 1 949  ? 157.652 185.528 150.809 1.00 34.83  ? 949  VAL A CB    1 
ATOM   6134 C CG1   . VAL A 1 949  ? 157.504 185.011 152.228 1.00 41.79  ? 949  VAL A CG1   1 
ATOM   6135 C CG2   . VAL A 1 949  ? 156.596 186.578 150.512 1.00 33.69  ? 949  VAL A CG2   1 
ATOM   6136 N N     . ILE A 1 950  ? 160.849 185.429 152.080 1.00 41.33  ? 950  ILE A N     1 
ATOM   6137 C CA    . ILE A 1 950  ? 161.900 184.564 152.600 1.00 38.14  ? 950  ILE A CA    1 
ATOM   6138 C C     . ILE A 1 950  ? 161.306 183.657 153.667 1.00 43.05  ? 950  ILE A C     1 
ATOM   6139 O O     . ILE A 1 950  ? 160.685 184.132 154.624 1.00 49.92  ? 950  ILE A O     1 
ATOM   6140 C CB    . ILE A 1 950  ? 163.061 185.394 153.170 1.00 30.08  ? 950  ILE A CB    1 
ATOM   6141 C CG1   . ILE A 1 950  ? 163.661 186.288 152.089 1.00 28.33  ? 950  ILE A CG1   1 
ATOM   6142 C CG2   . ILE A 1 950  ? 164.118 184.485 153.760 1.00 33.28  ? 950  ILE A CG2   1 
ATOM   6143 C CD1   . ILE A 1 950  ? 164.736 187.204 152.602 1.00 31.71  ? 950  ILE A CD1   1 
ATOM   6144 N N     . ILE A 1 951  ? 161.498 182.350 153.508 1.00 39.24  ? 951  ILE A N     1 
ATOM   6145 C CA    . ILE A 1 951  ? 161.002 181.360 154.456 1.00 42.83  ? 951  ILE A CA    1 
ATOM   6146 C C     . ILE A 1 951  ? 162.163 180.466 154.865 1.00 42.24  ? 951  ILE A C     1 
ATOM   6147 O O     . ILE A 1 951  ? 162.762 179.794 154.017 1.00 43.68  ? 951  ILE A O     1 
ATOM   6148 C CB    . ILE A 1 951  ? 159.851 180.525 153.871 1.00 40.31  ? 951  ILE A CB    1 
ATOM   6149 C CG1   . ILE A 1 951  ? 158.630 181.411 153.624 1.00 43.90  ? 951  ILE A CG1   1 
ATOM   6150 C CG2   . ILE A 1 951  ? 159.502 179.374 154.797 1.00 47.33  ? 951  ILE A CG2   1 
ATOM   6151 C CD1   . ILE A 1 951  ? 157.433 180.665 153.093 1.00 54.69  ? 951  ILE A CD1   1 
ATOM   6152 N N     . ASN A 1 952  ? 162.478 180.458 156.161 1.00 44.17  ? 952  ASN A N     1 
ATOM   6153 C CA    . ASN A 1 952  ? 163.555 179.642 156.701 1.00 47.82  ? 952  ASN A CA    1 
ATOM   6154 C C     . ASN A 1 952  ? 163.099 178.608 157.717 1.00 56.77  ? 952  ASN A C     1 
ATOM   6155 O O     . ASN A 1 952  ? 163.855 177.671 157.993 1.00 62.22  ? 952  ASN A O     1 
ATOM   6156 C CB    . ASN A 1 952  ? 164.625 180.530 157.355 1.00 43.70  ? 952  ASN A CB    1 
ATOM   6157 C CG    . ASN A 1 952  ? 165.374 181.375 156.348 1.00 46.47  ? 952  ASN A CG    1 
ATOM   6158 O OD1   . ASN A 1 952  ? 165.835 180.876 155.323 1.00 45.26  ? 952  ASN A OD1   1 
ATOM   6159 N ND2   . ASN A 1 952  ? 165.496 182.665 156.633 1.00 47.75  ? 952  ASN A ND2   1 
ATOM   6160 N N     . GLY A 1 953  ? 161.898 178.745 158.281 1.00 57.75  ? 953  GLY A N     1 
ATOM   6161 C CA    . GLY A 1 953  ? 161.422 177.780 159.246 1.00 66.85  ? 953  GLY A CA    1 
ATOM   6162 C C     . GLY A 1 953  ? 160.837 176.540 158.598 1.00 77.63  ? 953  GLY A C     1 
ATOM   6163 O O     . GLY A 1 953  ? 160.442 176.534 157.433 1.00 73.78  ? 953  GLY A O     1 
ATOM   6164 N N     . ASP A 1 954  ? 160.781 175.468 159.382 1.00 83.55  ? 954  ASP A N     1 
ATOM   6165 C CA    . ASP A 1 954  ? 160.260 174.193 158.917 1.00 88.99  ? 954  ASP A CA    1 
ATOM   6166 C C     . ASP A 1 954  ? 158.743 174.159 159.104 1.00 97.32  ? 954  ASP A C     1 
ATOM   6167 O O     . ASP A 1 954  ? 158.108 175.171 159.412 1.00 94.54  ? 954  ASP A O     1 
ATOM   6168 C CB    . ASP A 1 954  ? 160.951 173.043 159.646 1.00 93.34  ? 954  ASP A CB    1 
ATOM   6169 C CG    . ASP A 1 954  ? 160.701 173.069 161.141 1.00 105.19 ? 954  ASP A CG    1 
ATOM   6170 O OD1   . ASP A 1 954  ? 160.456 174.166 161.687 1.00 99.12  ? 954  ASP A OD1   1 
ATOM   6171 O OD2   . ASP A 1 954  ? 160.751 171.992 161.771 1.00 107.64 ? 954  ASP A OD2   1 
ATOM   6172 N N     . SER A 1 955  ? 158.146 172.984 158.923 1.00 104.49 ? 955  SER A N     1 
ATOM   6173 C CA    . SER A 1 955  ? 156.705 172.798 159.039 1.00 108.35 ? 955  SER A CA    1 
ATOM   6174 C C     . SER A 1 955  ? 156.364 171.862 160.192 1.00 112.86 ? 955  SER A C     1 
ATOM   6175 O O     . SER A 1 955  ? 155.480 171.010 160.086 1.00 114.44 ? 955  SER A O     1 
ATOM   6176 C CB    . SER A 1 955  ? 156.119 172.273 157.731 1.00 107.03 ? 955  SER A CB    1 
ATOM   6177 O OG    . SER A 1 955  ? 156.697 171.029 157.376 1.00 105.89 ? 955  SER A OG    1 
ATOM   6178 N N     . SER A 1 956  ? 157.057 172.018 161.314 1.00 113.81 ? 956  SER A N     1 
ATOM   6179 C CA    . SER A 1 956  ? 156.829 171.177 162.482 1.00 116.71 ? 956  SER A CA    1 
ATOM   6180 C C     . SER A 1 956  ? 155.523 171.590 163.162 1.00 114.79 ? 956  SER A C     1 
ATOM   6181 O O     . SER A 1 956  ? 154.774 172.442 162.676 1.00 110.68 ? 956  SER A O     1 
ATOM   6182 C CB    . SER A 1 956  ? 158.019 171.262 163.432 1.00 113.33 ? 956  SER A CB    1 
ATOM   6183 O OG    . SER A 1 956  ? 158.222 172.592 163.878 1.00 108.35 ? 956  SER A OG    1 
ATOM   6184 N N     . THR A 1 957  ? 155.239 170.980 164.312 1.00 113.64 ? 957  THR A N     1 
ATOM   6185 C CA    . THR A 1 957  ? 154.023 171.287 165.054 1.00 114.54 ? 957  THR A CA    1 
ATOM   6186 C C     . THR A 1 957  ? 154.141 172.646 165.733 1.00 112.90 ? 957  THR A C     1 
ATOM   6187 O O     . THR A 1 957  ? 154.242 172.731 166.961 1.00 110.32 ? 957  THR A O     1 
ATOM   6188 C CB    . THR A 1 957  ? 153.731 170.199 166.091 1.00 116.67 ? 957  THR A CB    1 
ATOM   6189 O OG1   . THR A 1 957  ? 154.836 170.091 166.996 1.00 111.00 ? 957  THR A OG1   1 
ATOM   6190 C CG2   . THR A 1 957  ? 153.506 168.858 165.407 1.00 115.15 ? 957  THR A CG2   1 
ATOM   6191 N N     . LYS A 1 958  ? 154.131 173.710 164.936 1.00 113.23 ? 958  LYS A N     1 
ATOM   6192 C CA    . LYS A 1 958  ? 154.243 175.088 165.402 1.00 110.00 ? 958  LYS A CA    1 
ATOM   6193 C C     . LYS A 1 958  ? 153.193 175.950 164.715 1.00 105.21 ? 958  LYS A C     1 
ATOM   6194 O O     . LYS A 1 958  ? 153.486 177.005 164.148 1.00 103.21 ? 958  LYS A O     1 
ATOM   6195 C CB    . LYS A 1 958  ? 155.650 175.630 165.163 1.00 108.26 ? 958  LYS A CB    1 
ATOM   6196 C CG    . LYS A 1 958  ? 156.010 176.833 166.022 1.00 102.33 ? 958  LYS A CG    1 
ATOM   6197 C CD    . LYS A 1 958  ? 155.955 176.489 167.502 1.00 102.23 ? 958  LYS A CD    1 
ATOM   6198 C CE    . LYS A 1 958  ? 156.320 177.688 168.362 1.00 101.25 ? 958  LYS A CE    1 
ATOM   6199 N NZ    . LYS A 1 958  ? 155.395 178.833 168.141 1.00 104.05 ? 958  LYS A NZ    1 
ATOM   6200 N N     . SER A 1 959  ? 151.941 175.482 164.750 1.00 104.21 ? 959  SER A N     1 
ATOM   6201 C CA    . SER A 1 959  ? 150.854 176.098 163.993 1.00 104.80 ? 959  SER A CA    1 
ATOM   6202 C C     . SER A 1 959  ? 150.713 177.595 164.243 1.00 103.38 ? 959  SER A C     1 
ATOM   6203 O O     . SER A 1 959  ? 150.096 178.291 163.430 1.00 101.42 ? 959  SER A O     1 
ATOM   6204 C CB    . SER A 1 959  ? 149.533 175.397 164.319 1.00 106.84 ? 959  SER A CB    1 
ATOM   6205 O OG    . SER A 1 959  ? 149.577 174.030 163.947 1.00 108.61 ? 959  SER A OG    1 
ATOM   6206 N N     . GLN A 1 960  ? 151.258 178.109 165.348 1.00 105.25 ? 960  GLN A N     1 
ATOM   6207 C CA    . GLN A 1 960  ? 151.264 179.553 165.553 1.00 107.57 ? 960  GLN A CA    1 
ATOM   6208 C C     . GLN A 1 960  ? 152.054 180.265 164.462 1.00 104.70 ? 960  GLN A C     1 
ATOM   6209 O O     . GLN A 1 960  ? 151.718 181.394 164.087 1.00 100.97 ? 960  GLN A O     1 
ATOM   6210 C CB    . GLN A 1 960  ? 151.829 179.889 166.933 1.00 107.47 ? 960  GLN A CB    1 
ATOM   6211 C CG    . GLN A 1 960  ? 150.990 179.362 168.086 1.00 104.75 ? 960  GLN A CG    1 
ATOM   6212 C CD    . GLN A 1 960  ? 151.503 179.818 169.438 1.00 109.74 ? 960  GLN A CD    1 
ATOM   6213 O OE1   . GLN A 1 960  ? 152.506 180.526 169.528 1.00 107.92 ? 960  GLN A OE1   1 
ATOM   6214 N NE2   . GLN A 1 960  ? 150.814 179.413 170.499 1.00 113.22 ? 960  GLN A NE2   1 
ATOM   6215 N N     . SER A 1 961  ? 153.102 179.623 163.941 1.00 101.33 ? 961  SER A N     1 
ATOM   6216 C CA    . SER A 1 961  ? 153.861 180.146 162.816 1.00 93.92  ? 961  SER A CA    1 
ATOM   6217 C C     . SER A 1 961  ? 153.916 179.203 161.625 1.00 93.78  ? 961  SER A C     1 
ATOM   6218 O O     . SER A 1 961  ? 154.154 179.669 160.505 1.00 91.98  ? 961  SER A O     1 
ATOM   6219 C CB    . SER A 1 961  ? 155.299 180.478 163.243 1.00 87.68  ? 961  SER A CB    1 
ATOM   6220 O OG    . SER A 1 961  ? 155.981 179.310 163.664 1.00 92.76  ? 961  SER A OG    1 
ATOM   6221 N N     . GLN A 1 962  ? 153.710 177.899 161.830 1.00 96.01  ? 962  GLN A N     1 
ATOM   6222 C CA    . GLN A 1 962  ? 153.671 176.969 160.706 1.00 94.55  ? 962  GLN A CA    1 
ATOM   6223 C C     . GLN A 1 962  ? 152.495 177.274 159.788 1.00 93.48  ? 962  GLN A C     1 
ATOM   6224 O O     . GLN A 1 962  ? 152.617 177.192 158.559 1.00 91.57  ? 962  GLN A O     1 
ATOM   6225 C CB    . GLN A 1 962  ? 153.602 175.531 161.222 1.00 97.83  ? 962  GLN A CB    1 
ATOM   6226 C CG    . GLN A 1 962  ? 153.679 174.465 160.140 1.00 104.92 ? 962  GLN A CG    1 
ATOM   6227 C CD    . GLN A 1 962  ? 152.320 174.088 159.584 1.00 108.73 ? 962  GLN A CD    1 
ATOM   6228 O OE1   . GLN A 1 962  ? 151.285 174.462 160.136 1.00 107.94 ? 962  GLN A OE1   1 
ATOM   6229 N NE2   . GLN A 1 962  ? 152.316 173.343 158.485 1.00 110.04 ? 962  GLN A NE2   1 
ATOM   6230 N N     . ASN A 1 963  ? 151.345 177.625 160.368 1.00 95.45  ? 963  ASN A N     1 
ATOM   6231 C CA    . ASN A 1 963  ? 150.209 178.041 159.553 1.00 94.00  ? 963  ASN A CA    1 
ATOM   6232 C C     . ASN A 1 963  ? 150.532 179.307 158.772 1.00 89.24  ? 963  ASN A C     1 
ATOM   6233 O O     . ASN A 1 963  ? 150.128 179.447 157.614 1.00 88.76  ? 963  ASN A O     1 
ATOM   6234 C CB    . ASN A 1 963  ? 148.974 178.250 160.428 1.00 97.06  ? 963  ASN A CB    1 
ATOM   6235 C CG    . ASN A 1 963  ? 148.418 176.950 160.973 1.00 99.30  ? 963  ASN A CG    1 
ATOM   6236 O OD1   . ASN A 1 963  ? 148.623 175.883 160.395 1.00 95.58  ? 963  ASN A OD1   1 
ATOM   6237 N ND2   . ASN A 1 963  ? 147.704 177.035 162.088 1.00 101.40 ? 963  ASN A ND2   1 
ATOM   6238 N N     . SER A 1 964  ? 151.262 180.241 159.387 1.00 89.22  ? 964  SER A N     1 
ATOM   6239 C CA    . SER A 1 964  ? 151.655 181.455 158.678 1.00 87.71  ? 964  SER A CA    1 
ATOM   6240 C C     . SER A 1 964  ? 152.584 181.141 157.511 1.00 83.50  ? 964  SER A C     1 
ATOM   6241 O O     . SER A 1 964  ? 152.441 181.712 156.424 1.00 83.31  ? 964  SER A O     1 
ATOM   6242 C CB    . SER A 1 964  ? 152.322 182.434 159.644 1.00 87.13  ? 964  SER A CB    1 
ATOM   6243 O OG    . SER A 1 964  ? 151.441 182.799 160.691 1.00 88.65  ? 964  SER A OG    1 
ATOM   6244 N N     . ARG A 1 965  ? 153.546 180.237 157.717 1.00 79.93  ? 965  ARG A N     1 
ATOM   6245 C CA    . ARG A 1 965  ? 154.446 179.858 156.631 1.00 75.15  ? 965  ARG A CA    1 
ATOM   6246 C C     . ARG A 1 965  ? 153.693 179.162 155.504 1.00 77.14  ? 965  ARG A C     1 
ATOM   6247 O O     . ARG A 1 965  ? 153.944 179.430 154.321 1.00 78.65  ? 965  ARG A O     1 
ATOM   6248 C CB    . ARG A 1 965  ? 155.565 178.963 157.162 1.00 72.82  ? 965  ARG A CB    1 
ATOM   6249 C CG    . ARG A 1 965  ? 156.617 179.701 157.970 1.00 71.07  ? 965  ARG A CG    1 
ATOM   6250 C CD    . ARG A 1 965  ? 157.774 178.789 158.337 1.00 67.78  ? 965  ARG A CD    1 
ATOM   6251 N NE    . ARG A 1 965  ? 157.431 177.860 159.406 1.00 78.63  ? 965  ARG A NE    1 
ATOM   6252 C CZ    . ARG A 1 965  ? 157.694 178.066 160.688 1.00 79.58  ? 965  ARG A CZ    1 
ATOM   6253 N NH1   . ARG A 1 965  ? 158.302 179.167 161.100 1.00 70.53  ? 965  ARG A NH1   1 
ATOM   6254 N NH2   . ARG A 1 965  ? 157.340 177.146 161.580 1.00 84.59  ? 965  ARG A NH2   1 
ATOM   6255 N N     . GLN A 1 966  ? 152.767 178.265 155.848 1.00 81.48  ? 966  GLN A N     1 
ATOM   6256 C CA    . GLN A 1 966  ? 151.966 177.607 154.821 1.00 78.99  ? 966  GLN A CA    1 
ATOM   6257 C C     . GLN A 1 966  ? 151.097 178.613 154.078 1.00 75.69  ? 966  GLN A C     1 
ATOM   6258 O O     . GLN A 1 966  ? 150.905 178.500 152.862 1.00 73.12  ? 966  GLN A O     1 
ATOM   6259 C CB    . GLN A 1 966  ? 151.108 176.508 155.445 1.00 83.59  ? 966  GLN A CB    1 
ATOM   6260 C CG    . GLN A 1 966  ? 150.310 175.703 154.435 1.00 82.71  ? 966  GLN A CG    1 
ATOM   6261 C CD    . GLN A 1 966  ? 151.192 174.955 153.455 1.00 85.03  ? 966  GLN A CD    1 
ATOM   6262 O OE1   . GLN A 1 966  ? 152.316 174.573 153.780 1.00 90.22  ? 966  GLN A OE1   1 
ATOM   6263 N NE2   . GLN A 1 966  ? 150.687 174.744 152.246 1.00 80.10  ? 966  GLN A NE2   1 
ATOM   6264 N N     . ARG A 1 967  ? 150.561 179.604 154.793 1.00 78.35  ? 967  ARG A N     1 
ATOM   6265 C CA    . ARG A 1 967  ? 149.773 180.648 154.149 1.00 79.58  ? 967  ARG A CA    1 
ATOM   6266 C C     . ARG A 1 967  ? 150.624 181.469 153.191 1.00 77.95  ? 967  ARG A C     1 
ATOM   6267 O O     . ARG A 1 967  ? 150.166 181.829 152.103 1.00 77.01  ? 967  ARG A O     1 
ATOM   6268 C CB    . ARG A 1 967  ? 149.133 181.547 155.205 1.00 83.87  ? 967  ARG A CB    1 
ATOM   6269 C CG    . ARG A 1 967  ? 148.262 182.652 154.636 1.00 88.67  ? 967  ARG A CG    1 
ATOM   6270 C CD    . ARG A 1 967  ? 147.850 183.633 155.718 1.00 93.86  ? 967  ARG A CD    1 
ATOM   6271 N NE    . ARG A 1 967  ? 149.008 184.178 156.418 1.00 98.17  ? 967  ARG A NE    1 
ATOM   6272 C CZ    . ARG A 1 967  ? 149.726 185.207 155.991 1.00 94.39  ? 967  ARG A CZ    1 
ATOM   6273 N NH1   . ARG A 1 967  ? 149.435 185.832 154.862 1.00 88.36  ? 967  ARG A NH1   1 
ATOM   6274 N NH2   . ARG A 1 967  ? 150.763 185.619 156.714 1.00 94.58  ? 967  ARG A NH2   1 
ATOM   6275 N N     . LEU A 1 968  ? 151.861 181.782 153.582 1.00 77.76  ? 968  LEU A N     1 
ATOM   6276 C CA    . LEU A 1 968  ? 152.763 182.493 152.679 1.00 72.97  ? 968  LEU A CA    1 
ATOM   6277 C C     . LEU A 1 968  ? 153.055 181.667 151.433 1.00 68.86  ? 968  LEU A C     1 
ATOM   6278 O O     . LEU A 1 968  ? 153.058 182.194 150.313 1.00 69.17  ? 968  LEU A O     1 
ATOM   6279 C CB    . LEU A 1 968  ? 154.061 182.848 153.403 1.00 68.65  ? 968  LEU A CB    1 
ATOM   6280 C CG    . LEU A 1 968  ? 153.976 183.886 154.521 1.00 72.13  ? 968  LEU A CG    1 
ATOM   6281 C CD1   . LEU A 1 968  ? 155.313 184.016 155.230 1.00 66.71  ? 968  LEU A CD1   1 
ATOM   6282 C CD2   . LEU A 1 968  ? 153.528 185.230 153.971 1.00 67.39  ? 968  LEU A CD2   1 
ATOM   6283 N N     . ILE A 1 969  ? 153.293 180.366 151.610 1.00 68.41  ? 969  ILE A N     1 
ATOM   6284 C CA    . ILE A 1 969  ? 153.540 179.485 150.469 1.00 63.46  ? 969  ILE A CA    1 
ATOM   6285 C C     . ILE A 1 969  ? 152.332 179.472 149.538 1.00 65.35  ? 969  ILE A C     1 
ATOM   6286 O O     . ILE A 1 969  ? 152.465 179.573 148.311 1.00 65.56  ? 969  ILE A O     1 
ATOM   6287 C CB    . ILE A 1 969  ? 153.892 178.067 150.954 1.00 69.64  ? 969  ILE A CB    1 
ATOM   6288 C CG1   . ILE A 1 969  ? 155.285 178.039 151.585 1.00 64.56  ? 969  ILE A CG1   1 
ATOM   6289 C CG2   . ILE A 1 969  ? 153.798 177.068 149.812 1.00 69.81  ? 969  ILE A CG2   1 
ATOM   6290 C CD1   . ILE A 1 969  ? 156.410 178.160 150.585 1.00 58.65  ? 969  ILE A CD1   1 
ATOM   6291 N N     . ASP A 1 970  ? 151.134 179.349 150.114 1.00 72.02  ? 970  ASP A N     1 
ATOM   6292 C CA    . ASP A 1 970  ? 149.919 179.291 149.307 1.00 69.89  ? 970  ASP A CA    1 
ATOM   6293 C C     . ASP A 1 970  ? 149.661 180.610 148.591 1.00 67.80  ? 970  ASP A C     1 
ATOM   6294 O O     . ASP A 1 970  ? 149.200 180.617 147.445 1.00 68.96  ? 970  ASP A O     1 
ATOM   6295 C CB    . ASP A 1 970  ? 148.728 178.911 150.185 1.00 75.42  ? 970  ASP A CB    1 
ATOM   6296 C CG    . ASP A 1 970  ? 148.869 177.527 150.788 1.00 82.86  ? 970  ASP A CG    1 
ATOM   6297 O OD1   . ASP A 1 970  ? 149.554 176.679 150.179 1.00 78.44  ? 970  ASP A OD1   1 
ATOM   6298 O OD2   . ASP A 1 970  ? 148.296 177.288 151.872 1.00 83.88  ? 970  ASP A OD2   1 
ATOM   6299 N N     . ASP A 1 971  ? 149.938 181.736 149.251 1.00 67.61  ? 971  ASP A N     1 
ATOM   6300 C CA    . ASP A 1 971  ? 149.782 183.035 148.605 1.00 66.87  ? 971  ASP A CA    1 
ATOM   6301 C C     . ASP A 1 971  ? 150.765 183.198 147.453 1.00 66.74  ? 971  ASP A C     1 
ATOM   6302 O O     . ASP A 1 971  ? 150.417 183.762 146.409 1.00 68.62  ? 971  ASP A O     1 
ATOM   6303 C CB    . ASP A 1 971  ? 149.960 184.157 149.626 1.00 72.28  ? 971  ASP A CB    1 
ATOM   6304 C CG    . ASP A 1 971  ? 148.888 184.146 150.696 1.00 80.67  ? 971  ASP A CG    1 
ATOM   6305 O OD1   . ASP A 1 971  ? 147.764 183.683 150.409 1.00 83.95  ? 971  ASP A OD1   1 
ATOM   6306 O OD2   . ASP A 1 971  ? 149.168 184.600 151.826 1.00 81.60  ? 971  ASP A OD2   1 
ATOM   6307 N N     . PHE A 1 972  ? 152.001 182.722 147.628 1.00 63.03  ? 972  PHE A N     1 
ATOM   6308 C CA    . PHE A 1 972  ? 152.961 182.754 146.530 1.00 59.04  ? 972  PHE A CA    1 
ATOM   6309 C C     . PHE A 1 972  ? 152.490 181.898 145.361 1.00 57.74  ? 972  PHE A C     1 
ATOM   6310 O O     . PHE A 1 972  ? 152.579 182.315 144.200 1.00 56.24  ? 972  PHE A O     1 
ATOM   6311 C CB    . PHE A 1 972  ? 154.332 182.286 147.015 1.00 55.63  ? 972  PHE A CB    1 
ATOM   6312 C CG    . PHE A 1 972  ? 155.296 181.979 145.903 1.00 48.99  ? 972  PHE A CG    1 
ATOM   6313 C CD1   . PHE A 1 972  ? 155.924 182.999 145.211 1.00 39.35  ? 972  PHE A CD1   1 
ATOM   6314 C CD2   . PHE A 1 972  ? 155.577 180.669 145.553 1.00 50.42  ? 972  PHE A CD2   1 
ATOM   6315 C CE1   . PHE A 1 972  ? 156.810 182.719 144.190 1.00 35.80  ? 972  PHE A CE1   1 
ATOM   6316 C CE2   . PHE A 1 972  ? 156.462 180.383 144.532 1.00 47.74  ? 972  PHE A CE2   1 
ATOM   6317 C CZ    . PHE A 1 972  ? 157.080 181.410 143.852 1.00 35.97  ? 972  PHE A CZ    1 
ATOM   6318 N N     . GLN A 1 973  ? 151.982 180.698 145.648 1.00 61.66  ? 973  GLN A N     1 
ATOM   6319 C CA    . GLN A 1 973  ? 151.555 179.803 144.576 1.00 60.57  ? 973  GLN A CA    1 
ATOM   6320 C C     . GLN A 1 973  ? 150.313 180.329 143.866 1.00 65.74  ? 973  GLN A C     1 
ATOM   6321 O O     . GLN A 1 973  ? 150.156 180.135 142.655 1.00 69.16  ? 973  GLN A O     1 
ATOM   6322 C CB    . GLN A 1 973  ? 151.297 178.403 145.128 1.00 63.06  ? 973  GLN A CB    1 
ATOM   6323 C CG    . GLN A 1 973  ? 152.533 177.695 145.645 1.00 63.85  ? 973  GLN A CG    1 
ATOM   6324 C CD    . GLN A 1 973  ? 152.251 176.257 146.023 1.00 67.08  ? 973  GLN A CD    1 
ATOM   6325 O OE1   . GLN A 1 973  ? 152.766 175.754 147.020 1.00 69.24  ? 973  GLN A OE1   1 
ATOM   6326 N NE2   . GLN A 1 973  ? 151.431 175.585 145.225 1.00 64.67  ? 973  GLN A NE2   1 
ATOM   6327 N N     . ALA A 1 974  ? 149.414 180.985 144.599 1.00 66.17  ? 974  ALA A N     1 
ATOM   6328 C CA    . ALA A 1 974  ? 148.159 181.456 144.029 1.00 65.39  ? 974  ALA A CA    1 
ATOM   6329 C C     . ALA A 1 974  ? 148.298 182.764 143.264 1.00 70.55  ? 974  ALA A C     1 
ATOM   6330 O O     . ALA A 1 974  ? 147.375 183.128 142.528 1.00 78.70  ? 974  ALA A O     1 
ATOM   6331 C CB    . ALA A 1 974  ? 147.111 181.619 145.132 1.00 64.36  ? 974  ALA A CB    1 
ATOM   6332 N N     . GLN A 1 975  ? 149.406 183.473 143.418 1.00 70.37  ? 975  GLN A N     1 
ATOM   6333 C CA    . GLN A 1 975  ? 149.594 184.733 142.709 1.00 72.72  ? 975  GLN A CA    1 
ATOM   6334 C C     . GLN A 1 975  ? 149.766 184.465 141.220 1.00 75.33  ? 975  GLN A C     1 
ATOM   6335 O O     . GLN A 1 975  ? 150.664 183.705 140.838 1.00 74.88  ? 975  GLN A O     1 
ATOM   6336 C CB    . GLN A 1 975  ? 150.807 185.476 143.259 1.00 74.30  ? 975  GLN A CB    1 
ATOM   6337 C CG    . GLN A 1 975  ? 151.095 186.795 142.562 1.00 79.76  ? 975  GLN A CG    1 
ATOM   6338 C CD    . GLN A 1 975  ? 150.013 187.831 142.798 1.00 86.74  ? 975  GLN A CD    1 
ATOM   6339 O OE1   . GLN A 1 975  ? 149.298 187.784 143.799 1.00 85.85  ? 975  GLN A OE1   1 
ATOM   6340 N NE2   . GLN A 1 975  ? 149.886 188.775 141.872 1.00 85.10  ? 975  GLN A NE2   1 
ATOM   6341 N N     . PRO A 1 976  ? 148.945 185.054 140.354 1.00 79.07  ? 976  PRO A N     1 
ATOM   6342 C CA    . PRO A 1 976  ? 149.075 184.782 138.920 1.00 74.05  ? 976  PRO A CA    1 
ATOM   6343 C C     . PRO A 1 976  ? 150.356 185.365 138.345 1.00 71.93  ? 976  PRO A C     1 
ATOM   6344 O O     . PRO A 1 976  ? 150.886 186.369 138.828 1.00 70.51  ? 976  PRO A O     1 
ATOM   6345 C CB    . PRO A 1 976  ? 147.839 185.461 138.320 1.00 78.44  ? 976  PRO A CB    1 
ATOM   6346 C CG    . PRO A 1 976  ? 147.518 186.554 139.282 1.00 79.36  ? 976  PRO A CG    1 
ATOM   6347 C CD    . PRO A 1 976  ? 147.869 186.016 140.643 1.00 77.70  ? 976  PRO A CD    1 
ATOM   6348 N N     . GLY A 1 977  ? 150.854 184.712 137.298 1.00 69.46  ? 977  GLY A N     1 
ATOM   6349 C CA    . GLY A 1 977  ? 151.990 185.237 136.566 1.00 64.38  ? 977  GLY A CA    1 
ATOM   6350 C C     . GLY A 1 977  ? 153.326 184.957 137.236 1.00 59.04  ? 977  GLY A C     1 
ATOM   6351 O O     . GLY A 1 977  ? 153.501 183.979 137.965 1.00 53.60  ? 977  GLY A O     1 
ATOM   6352 N N     . PHE A 1 978  ? 154.281 185.843 136.969 1.00 57.28  ? 978  PHE A N     1 
ATOM   6353 C CA    . PHE A 1 978  ? 155.644 185.685 137.452 1.00 50.65  ? 978  PHE A CA    1 
ATOM   6354 C C     . PHE A 1 978  ? 155.714 185.860 138.965 1.00 50.96  ? 978  PHE A C     1 
ATOM   6355 O O     . PHE A 1 978  ? 154.947 186.619 139.564 1.00 54.44  ? 978  PHE A O     1 
ATOM   6356 C CB    . PHE A 1 978  ? 156.558 186.694 136.755 1.00 45.22  ? 978  PHE A CB    1 
ATOM   6357 C CG    . PHE A 1 978  ? 157.987 186.650 137.212 1.00 45.21  ? 978  PHE A CG    1 
ATOM   6358 C CD1   . PHE A 1 978  ? 158.807 185.591 136.868 1.00 48.97  ? 978  PHE A CD1   1 
ATOM   6359 C CD2   . PHE A 1 978  ? 158.518 187.685 137.965 1.00 44.93  ? 978  PHE A CD2   1 
ATOM   6360 C CE1   . PHE A 1 978  ? 160.125 185.556 137.280 1.00 42.92  ? 978  PHE A CE1   1 
ATOM   6361 C CE2   . PHE A 1 978  ? 159.834 187.655 138.377 1.00 45.64  ? 978  PHE A CE2   1 
ATOM   6362 C CZ    . PHE A 1 978  ? 160.638 186.589 138.034 1.00 40.61  ? 978  PHE A CZ    1 
ATOM   6363 N N     . GLY A 1 979  ? 156.646 185.141 139.582 1.00 44.24  ? 979  GLY A N     1 
ATOM   6364 C CA    . GLY A 1 979  ? 156.871 185.242 141.010 1.00 36.32  ? 979  GLY A CA    1 
ATOM   6365 C C     . GLY A 1 979  ? 158.150 184.562 141.448 1.00 36.39  ? 979  GLY A C     1 
ATOM   6366 O O     . GLY A 1 979  ? 158.606 183.613 140.807 1.00 40.29  ? 979  GLY A O     1 
ATOM   6367 N N     . VAL A 1 980  ? 158.747 185.045 142.535 1.00 35.32  ? 980  VAL A N     1 
ATOM   6368 C CA    . VAL A 1 980  ? 159.972 184.481 143.087 1.00 27.98  ? 980  VAL A CA    1 
ATOM   6369 C C     . VAL A 1 980  ? 159.796 184.319 144.589 1.00 30.78  ? 980  VAL A C     1 
ATOM   6370 O O     . VAL A 1 980  ? 159.249 185.202 145.258 1.00 37.05  ? 980  VAL A O     1 
ATOM   6371 C CB    . VAL A 1 980  ? 161.204 185.360 142.779 1.00 27.12  ? 980  VAL A CB    1 
ATOM   6372 C CG1   . VAL A 1 980  ? 162.451 184.758 143.391 1.00 25.78  ? 980  VAL A CG1   1 
ATOM   6373 C CG2   . VAL A 1 980  ? 161.384 185.526 141.284 1.00 30.00  ? 980  VAL A CG2   1 
ATOM   6374 N N     . ILE A 1 981  ? 160.246 183.183 145.116 1.00 31.08  ? 981  ILE A N     1 
ATOM   6375 C CA    . ILE A 1 981  ? 160.247 182.924 146.550 1.00 32.09  ? 981  ILE A CA    1 
ATOM   6376 C C     . ILE A 1 981  ? 161.634 182.434 146.938 1.00 29.65  ? 981  ILE A C     1 
ATOM   6377 O O     . ILE A 1 981  ? 162.277 181.695 146.184 1.00 28.92  ? 981  ILE A O     1 
ATOM   6378 C CB    . ILE A 1 981  ? 159.155 181.907 146.953 1.00 35.38  ? 981  ILE A CB    1 
ATOM   6379 C CG1   . ILE A 1 981  ? 158.987 181.869 148.471 1.00 35.14  ? 981  ILE A CG1   1 
ATOM   6380 C CG2   . ILE A 1 981  ? 159.466 180.518 146.418 1.00 33.91  ? 981  ILE A CG2   1 
ATOM   6381 C CD1   . ILE A 1 981  ? 157.769 181.105 148.925 1.00 35.60  ? 981  ILE A CD1   1 
ATOM   6382 N N     . ILE A 1 982  ? 162.111 182.874 148.096 1.00 27.26  ? 982  ILE A N     1 
ATOM   6383 C CA    . ILE A 1 982  ? 163.446 182.538 148.576 1.00 30.10  ? 982  ILE A CA    1 
ATOM   6384 C C     . ILE A 1 982  ? 163.277 181.586 149.752 1.00 34.54  ? 982  ILE A C     1 
ATOM   6385 O O     . ILE A 1 982  ? 163.118 182.015 150.900 1.00 37.41  ? 982  ILE A O     1 
ATOM   6386 C CB    . ILE A 1 982  ? 164.245 183.784 148.969 1.00 31.79  ? 982  ILE A CB    1 
ATOM   6387 C CG1   . ILE A 1 982  ? 164.303 184.767 147.801 1.00 27.00  ? 982  ILE A CG1   1 
ATOM   6388 C CG2   . ILE A 1 982  ? 165.647 183.396 149.404 1.00 27.60  ? 982  ILE A CG2   1 
ATOM   6389 C CD1   . ILE A 1 982  ? 165.107 186.008 148.092 1.00 24.40  ? 982  ILE A CD1   1 
ATOM   6390 N N     . LEU A 1 983  ? 163.311 180.289 149.470 1.00 36.00  ? 983  LEU A N     1 
ATOM   6391 C CA    . LEU A 1 983  ? 163.248 179.273 150.505 1.00 34.92  ? 983  LEU A CA    1 
ATOM   6392 C C     . LEU A 1 983  ? 164.653 178.894 150.962 1.00 40.31  ? 983  LEU A C     1 
ATOM   6393 O O     . LEU A 1 983  ? 165.659 179.401 150.463 1.00 41.55  ? 983  LEU A O     1 
ATOM   6394 C CB    . LEU A 1 983  ? 162.506 178.036 150.000 1.00 33.35  ? 983  LEU A CB    1 
ATOM   6395 C CG    . LEU A 1 983  ? 161.065 178.219 149.525 1.00 34.20  ? 983  LEU A CG    1 
ATOM   6396 C CD1   . LEU A 1 983  ? 160.482 176.890 149.078 1.00 38.62  ? 983  LEU A CD1   1 
ATOM   6397 C CD2   . LEU A 1 983  ? 160.215 178.835 150.618 1.00 34.18  ? 983  LEU A CD2   1 
ATOM   6398 N N     . SER A 1 984  ? 164.713 177.988 151.931 1.00 42.10  ? 984  SER A N     1 
ATOM   6399 C CA    . SER A 1 984  ? 165.963 177.385 152.358 1.00 45.45  ? 984  SER A CA    1 
ATOM   6400 C C     . SER A 1 984  ? 165.813 175.871 152.336 1.00 55.61  ? 984  SER A C     1 
ATOM   6401 O O     . SER A 1 984  ? 164.705 175.339 152.451 1.00 55.78  ? 984  SER A O     1 
ATOM   6402 C CB    . SER A 1 984  ? 166.379 177.857 153.756 1.00 46.15  ? 984  SER A CB    1 
ATOM   6403 O OG    . SER A 1 984  ? 165.567 177.278 154.758 1.00 54.14  ? 984  SER A OG    1 
ATOM   6404 N N     . THR A 1 985  ? 166.943 175.181 152.173 1.00 55.14  ? 985  THR A N     1 
ATOM   6405 C CA    . THR A 1 985  ? 166.913 173.725 152.082 1.00 56.03  ? 985  THR A CA    1 
ATOM   6406 C C     . THR A 1 985  ? 166.395 173.100 153.371 1.00 62.97  ? 985  THR A C     1 
ATOM   6407 O O     . THR A 1 985  ? 165.677 172.094 153.339 1.00 66.12  ? 985  THR A O     1 
ATOM   6408 C CB    . THR A 1 985  ? 168.305 173.195 151.748 1.00 62.14  ? 985  THR A CB    1 
ATOM   6409 O OG1   . THR A 1 985  ? 168.832 173.912 150.624 1.00 50.98  ? 985  THR A OG1   1 
ATOM   6410 C CG2   . THR A 1 985  ? 168.242 171.718 151.409 1.00 67.24  ? 985  THR A CG2   1 
ATOM   6411 N N     . VAL A 1 986  ? 166.753 173.679 154.519 1.00 65.88  ? 986  VAL A N     1 
ATOM   6412 C CA    . VAL A 1 986  ? 166.276 173.157 155.793 1.00 67.16  ? 986  VAL A CA    1 
ATOM   6413 C C     . VAL A 1 986  ? 164.798 173.455 156.012 1.00 67.21  ? 986  VAL A C     1 
ATOM   6414 O O     . VAL A 1 986  ? 164.135 172.742 156.774 1.00 71.08  ? 986  VAL A O     1 
ATOM   6415 C CB    . VAL A 1 986  ? 167.124 173.718 156.950 1.00 66.68  ? 986  VAL A CB    1 
ATOM   6416 C CG1   . VAL A 1 986  ? 168.590 173.380 156.740 1.00 60.46  ? 986  VAL A CG1   1 
ATOM   6417 C CG2   . VAL A 1 986  ? 166.936 175.222 157.073 1.00 66.82  ? 986  VAL A CG2   1 
ATOM   6418 N N     . ALA A 1 987  ? 164.259 174.491 155.364 1.00 62.99  ? 987  ALA A N     1 
ATOM   6419 C CA    . ALA A 1 987  ? 162.852 174.833 155.555 1.00 70.47  ? 987  ALA A CA    1 
ATOM   6420 C C     . ALA A 1 987  ? 161.935 173.803 154.910 1.00 75.53  ? 987  ALA A C     1 
ATOM   6421 O O     . ALA A 1 987  ? 160.910 173.426 155.490 1.00 79.56  ? 987  ALA A O     1 
ATOM   6422 C CB    . ALA A 1 987  ? 162.566 176.224 154.992 1.00 62.16  ? 987  ALA A CB    1 
ATOM   6423 N N     . VAL A 1 988  ? 162.285 173.337 153.709 1.00 73.81  ? 988  VAL A N     1 
ATOM   6424 C CA    . VAL A 1 988  ? 161.426 172.396 153.002 1.00 75.54  ? 988  VAL A CA    1 
ATOM   6425 C C     . VAL A 1 988  ? 161.464 171.032 153.684 1.00 81.22  ? 988  VAL A C     1 
ATOM   6426 O O     . VAL A 1 988  ? 162.378 170.705 154.451 1.00 77.09  ? 988  VAL A O     1 
ATOM   6427 C CB    . VAL A 1 988  ? 161.839 172.291 151.525 1.00 71.16  ? 988  VAL A CB    1 
ATOM   6428 C CG1   . VAL A 1 988  ? 161.873 173.670 150.885 1.00 63.97  ? 988  VAL A CG1   1 
ATOM   6429 C CG2   . VAL A 1 988  ? 163.187 171.601 151.396 1.00 61.36  ? 988  VAL A CG2   1 
ATOM   6430 N N     . GLY A 1 989  ? 160.446 170.224 153.398 1.00 86.35  ? 989  GLY A N     1 
ATOM   6431 C CA    . GLY A 1 989  ? 160.353 168.901 153.979 1.00 87.78  ? 989  GLY A CA    1 
ATOM   6432 C C     . GLY A 1 989  ? 158.983 168.268 153.850 1.00 93.05  ? 989  GLY A C     1 
ATOM   6433 O O     . GLY A 1 989  ? 158.331 168.381 152.807 1.00 87.04  ? 989  GLY A O     1 
ATOM   6434 N N     . PHE A 1 990  ? 158.542 167.596 154.910 1.00 100.52 ? 990  PHE A N     1 
ATOM   6435 C CA    . PHE A 1 990  ? 157.258 166.909 154.892 1.00 99.91  ? 990  PHE A CA    1 
ATOM   6436 C C     . PHE A 1 990  ? 156.108 167.902 154.769 1.00 100.56 ? 990  PHE A C     1 
ATOM   6437 O O     . PHE A 1 990  ? 156.138 168.991 155.350 1.00 98.49  ? 990  PHE A O     1 
ATOM   6438 C CB    . PHE A 1 990  ? 157.092 166.070 156.160 1.00 97.18  ? 990  PHE A CB    1 
ATOM   6439 C CG    . PHE A 1 990  ? 157.346 166.834 157.431 1.00 98.62  ? 990  PHE A CG    1 
ATOM   6440 C CD1   . PHE A 1 990  ? 158.600 166.831 158.018 1.00 98.69  ? 990  PHE A CD1   1 
ATOM   6441 C CD2   . PHE A 1 990  ? 156.331 167.555 158.039 1.00 97.18  ? 990  PHE A CD2   1 
ATOM   6442 C CE1   . PHE A 1 990  ? 158.837 167.534 159.185 1.00 98.15  ? 990  PHE A CE1   1 
ATOM   6443 C CE2   . PHE A 1 990  ? 156.563 168.263 159.202 1.00 101.49 ? 990  PHE A CE2   1 
ATOM   6444 C CZ    . PHE A 1 990  ? 157.817 168.250 159.778 1.00 102.42 ? 990  PHE A CZ    1 
ATOM   6445 N N     . GLY A 1 991  ? 155.095 167.523 153.992 1.00 99.93  ? 991  GLY A N     1 
ATOM   6446 C CA    . GLY A 1 991  ? 153.884 168.312 153.881 1.00 100.50 ? 991  GLY A CA    1 
ATOM   6447 C C     . GLY A 1 991  ? 154.047 169.676 153.255 1.00 101.49 ? 991  GLY A C     1 
ATOM   6448 O O     . GLY A 1 991  ? 153.120 170.489 153.331 1.00 102.01 ? 991  GLY A O     1 
ATOM   6449 N N     . VAL A 1 992  ? 155.192 169.958 152.639 1.00 97.34  ? 992  VAL A N     1 
ATOM   6450 C CA    . VAL A 1 992  ? 155.450 171.236 151.988 1.00 92.04  ? 992  VAL A CA    1 
ATOM   6451 C C     . VAL A 1 992  ? 155.841 170.961 150.545 1.00 83.66  ? 992  VAL A C     1 
ATOM   6452 O O     . VAL A 1 992  ? 156.733 170.147 150.285 1.00 77.54  ? 992  VAL A O     1 
ATOM   6453 C CB    . VAL A 1 992  ? 156.557 172.034 152.702 1.00 96.63  ? 992  VAL A CB    1 
ATOM   6454 C CG1   . VAL A 1 992  ? 156.886 173.300 151.924 1.00 86.83  ? 992  VAL A CG1   1 
ATOM   6455 C CG2   . VAL A 1 992  ? 156.137 172.372 154.120 1.00 100.14 ? 992  VAL A CG2   1 
ATOM   6456 N N     . ASN A 1 993  ? 155.174 171.633 149.611 1.00 79.90  ? 993  ASN A N     1 
ATOM   6457 C CA    . ASN A 1 993  ? 155.487 171.479 148.201 1.00 69.94  ? 993  ASN A CA    1 
ATOM   6458 C C     . ASN A 1 993  ? 155.118 172.758 147.469 1.00 69.79  ? 993  ASN A C     1 
ATOM   6459 O O     . ASN A 1 993  ? 154.171 173.454 147.843 1.00 71.35  ? 993  ASN A O     1 
ATOM   6460 C CB    . ASN A 1 993  ? 154.750 170.285 147.585 1.00 69.42  ? 993  ASN A CB    1 
ATOM   6461 C CG    . ASN A 1 993  ? 153.249 170.486 147.541 1.00 72.96  ? 993  ASN A CG    1 
ATOM   6462 O OD1   . ASN A 1 993  ? 152.711 171.024 146.574 1.00 68.08  ? 993  ASN A OD1   1 
ATOM   6463 N ND2   . ASN A 1 993  ? 152.564 170.051 148.591 1.00 74.13  ? 993  ASN A ND2   1 
ATOM   6464 N N     . VAL A 1 994  ? 155.885 173.067 146.426 1.00 67.21  ? 994  VAL A N     1 
ATOM   6465 C CA    . VAL A 1 994  ? 155.568 174.185 145.547 1.00 62.09  ? 994  VAL A CA    1 
ATOM   6466 C C     . VAL A 1 994  ? 155.501 173.664 144.118 1.00 61.12  ? 994  VAL A C     1 
ATOM   6467 O O     . VAL A 1 994  ? 156.509 173.646 143.404 1.00 63.53  ? 994  VAL A O     1 
ATOM   6468 C CB    . VAL A 1 994  ? 156.604 175.316 145.677 1.00 57.59  ? 994  VAL A CB    1 
ATOM   6469 C CG1   . VAL A 1 994  ? 156.119 176.562 144.955 1.00 59.64  ? 994  VAL A CG1   1 
ATOM   6470 C CG2   . VAL A 1 994  ? 156.894 175.617 147.140 1.00 53.59  ? 994  VAL A CG2   1 
ATOM   6471 N N     . GLN A 1 995  ? 154.313 173.248 143.689 1.00 61.56  ? 995  GLN A N     1 
ATOM   6472 C CA    . GLN A 1 995  ? 154.114 172.682 142.362 1.00 61.78  ? 995  GLN A CA    1 
ATOM   6473 C C     . GLN A 1 995  ? 153.756 173.733 141.323 1.00 66.78  ? 995  GLN A C     1 
ATOM   6474 O O     . GLN A 1 995  ? 153.644 173.405 140.138 1.00 65.21  ? 995  GLN A O     1 
ATOM   6475 C CB    . GLN A 1 995  ? 153.032 171.604 142.406 1.00 69.73  ? 995  GLN A CB    1 
ATOM   6476 C CG    . GLN A 1 995  ? 153.353 170.449 143.331 1.00 72.86  ? 995  GLN A CG    1 
ATOM   6477 C CD    . GLN A 1 995  ? 152.232 169.439 143.395 1.00 75.41  ? 995  GLN A CD    1 
ATOM   6478 O OE1   . GLN A 1 995  ? 151.180 169.620 142.783 1.00 74.43  ? 995  GLN A OE1   1 
ATOM   6479 N NE2   . GLN A 1 995  ? 152.451 168.362 144.139 1.00 71.01  ? 995  GLN A NE2   1 
ATOM   6480 N N     . LYS A 1 996  ? 153.559 174.981 141.738 1.00 66.70  ? 996  LYS A N     1 
ATOM   6481 C CA    . LYS A 1 996  ? 153.321 176.076 140.809 1.00 63.82  ? 996  LYS A CA    1 
ATOM   6482 C C     . LYS A 1 996  ? 154.612 176.706 140.308 1.00 58.53  ? 996  LYS A C     1 
ATOM   6483 O O     . LYS A 1 996  ? 154.562 177.568 139.425 1.00 55.85  ? 996  LYS A O     1 
ATOM   6484 C CB    . LYS A 1 996  ? 152.443 177.144 141.466 1.00 63.50  ? 996  LYS A CB    1 
ATOM   6485 C CG    . LYS A 1 996  ? 151.062 176.648 141.861 1.00 67.41  ? 996  LYS A CG    1 
ATOM   6486 C CD    . LYS A 1 996  ? 150.290 176.148 140.653 1.00 71.29  ? 996  LYS A CD    1 
ATOM   6487 C CE    . LYS A 1 996  ? 148.932 175.593 141.054 1.00 72.75  ? 996  LYS A CE    1 
ATOM   6488 N NZ    . LYS A 1 996  ? 148.085 176.615 141.728 1.00 65.39  ? 996  LYS A NZ    1 
ATOM   6489 N N     . ALA A 1 997  ? 155.757 176.293 140.841 1.00 53.58  ? 997  ALA A N     1 
ATOM   6490 C CA    . ALA A 1 997  ? 157.055 176.796 140.421 1.00 54.17  ? 997  ALA A CA    1 
ATOM   6491 C C     . ALA A 1 997  ? 157.791 175.723 139.633 1.00 55.88  ? 997  ALA A C     1 
ATOM   6492 O O     . ALA A 1 997  ? 157.772 174.545 140.002 1.00 54.24  ? 997  ALA A O     1 
ATOM   6493 C CB    . ALA A 1 997  ? 157.893 177.229 141.623 1.00 48.64  ? 997  ALA A CB    1 
ATOM   6494 N N     . ASN A 1 998  ? 158.428 176.135 138.539 1.00 53.43  ? 998  ASN A N     1 
ATOM   6495 C CA    . ASN A 1 998  ? 159.176 175.228 137.680 1.00 46.01  ? 998  ASN A CA    1 
ATOM   6496 C C     . ASN A 1 998  ? 160.681 175.405 137.770 1.00 42.20  ? 998  ASN A C     1 
ATOM   6497 O O     . ASN A 1 998  ? 161.416 174.445 137.539 1.00 42.78  ? 998  ASN A O     1 
ATOM   6498 C CB    . ASN A 1 998  ? 158.751 175.411 136.219 1.00 46.21  ? 998  ASN A CB    1 
ATOM   6499 C CG    . ASN A 1 998  ? 157.258 175.550 136.067 1.00 61.03  ? 998  ASN A CG    1 
ATOM   6500 O OD1   . ASN A 1 998  ? 156.766 176.553 135.553 1.00 63.24  ? 998  ASN A OD1   1 
ATOM   6501 N ND2   . ASN A 1 998  ? 156.522 174.545 136.526 1.00 66.14  ? 998  ASN A ND2   1 
ATOM   6502 N N     . HIS A 1 999  ? 161.154 176.601 138.095 1.00 38.54  ? 999  HIS A N     1 
ATOM   6503 C CA    . HIS A 1 999  ? 162.577 176.904 138.104 1.00 35.83  ? 999  HIS A CA    1 
ATOM   6504 C C     . HIS A 1 999  ? 163.098 176.826 139.531 1.00 33.22  ? 999  HIS A C     1 
ATOM   6505 O O     . HIS A 1 999  ? 162.596 177.523 140.419 1.00 30.40  ? 999  HIS A O     1 
ATOM   6506 C CB    . HIS A 1 999  ? 162.835 178.283 137.501 1.00 33.58  ? 999  HIS A CB    1 
ATOM   6507 C CG    . HIS A 1 999  ? 162.243 178.461 136.138 1.00 34.05  ? 999  HIS A CG    1 
ATOM   6508 N ND1   . HIS A 1 999  ? 162.992 178.375 134.984 1.00 32.61  ? 999  HIS A ND1   1 
ATOM   6509 C CD2   . HIS A 1 999  ? 160.973 178.710 135.745 1.00 35.84  ? 999  HIS A CD2   1 
ATOM   6510 C CE1   . HIS A 1 999  ? 162.209 178.569 133.939 1.00 34.20  ? 999  HIS A CE1   1 
ATOM   6511 N NE2   . HIS A 1 999  ? 160.979 178.774 134.373 1.00 38.51  ? 999  HIS A NE2   1 
ATOM   6512 N N     . VAL A 1 1000 ? 164.094 175.974 139.747 1.00 32.77  ? 1000 VAL A N     1 
ATOM   6513 C CA    . VAL A 1 1000 ? 164.721 175.788 141.048 1.00 27.12  ? 1000 VAL A CA    1 
ATOM   6514 C C     . VAL A 1 1000 ? 166.156 176.274 140.943 1.00 26.93  ? 1000 VAL A C     1 
ATOM   6515 O O     . VAL A 1 1000 ? 166.933 175.765 140.127 1.00 30.21  ? 1000 VAL A O     1 
ATOM   6516 C CB    . VAL A 1 1000 ? 164.665 174.321 141.500 1.00 27.51  ? 1000 VAL A CB    1 
ATOM   6517 C CG1   . VAL A 1 1000 ? 165.439 174.140 142.788 1.00 29.88  ? 1000 VAL A CG1   1 
ATOM   6518 C CG2   . VAL A 1 1000 ? 163.223 173.877 141.675 1.00 32.09  ? 1000 VAL A CG2   1 
ATOM   6519 N N     . ILE A 1 1001 ? 166.509 177.258 141.762 1.00 27.09  ? 1001 ILE A N     1 
ATOM   6520 C CA    . ILE A 1 1001 ? 167.835 177.859 141.748 1.00 27.50  ? 1001 ILE A CA    1 
ATOM   6521 C C     . ILE A 1 1001 ? 168.496 177.583 143.088 1.00 28.25  ? 1001 ILE A C     1 
ATOM   6522 O O     . ILE A 1 1001 ? 167.971 177.967 144.140 1.00 31.74  ? 1001 ILE A O     1 
ATOM   6523 C CB    . ILE A 1 1001 ? 167.771 179.366 141.467 1.00 26.40  ? 1001 ILE A CB    1 
ATOM   6524 C CG1   . ILE A 1 1001 ? 167.047 179.622 140.148 1.00 22.08  ? 1001 ILE A CG1   1 
ATOM   6525 C CG2   . ILE A 1 1001 ? 169.168 179.961 141.440 1.00 26.97  ? 1001 ILE A CG2   1 
ATOM   6526 C CD1   . ILE A 1 1001 ? 166.929 181.072 139.807 1.00 22.97  ? 1001 ILE A CD1   1 
ATOM   6527 N N     . HIS A 1 1002 ? 169.644 176.911 143.050 1.00 27.29  ? 1002 HIS A N     1 
ATOM   6528 C CA    . HIS A 1 1002 ? 170.443 176.662 144.245 1.00 28.90  ? 1002 HIS A CA    1 
ATOM   6529 C C     . HIS A 1 1002 ? 171.576 177.682 144.258 1.00 34.25  ? 1002 HIS A C     1 
ATOM   6530 O O     . HIS A 1 1002 ? 172.694 177.424 143.812 1.00 37.54  ? 1002 HIS A O     1 
ATOM   6531 C CB    . HIS A 1 1002 ? 170.952 175.225 144.262 1.00 31.06  ? 1002 HIS A CB    1 
ATOM   6532 C CG    . HIS A 1 1002 ? 169.863 174.200 144.315 1.00 32.28  ? 1002 HIS A CG    1 
ATOM   6533 N ND1   . HIS A 1 1002 ? 169.349 173.721 145.500 1.00 29.39  ? 1002 HIS A ND1   1 
ATOM   6534 C CD2   . HIS A 1 1002 ? 169.188 173.563 143.329 1.00 29.04  ? 1002 HIS A CD2   1 
ATOM   6535 C CE1   . HIS A 1 1002 ? 168.405 172.834 145.243 1.00 28.46  ? 1002 HIS A CE1   1 
ATOM   6536 N NE2   . HIS A 1 1002 ? 168.289 172.719 143.933 1.00 30.46  ? 1002 HIS A NE2   1 
ATOM   6537 N N     . PHE A 1 1003 ? 171.263 178.873 144.773 1.00 30.59  ? 1003 PHE A N     1 
ATOM   6538 C CA    . PHE A 1 1003 ? 172.241 179.955 144.791 1.00 31.08  ? 1003 PHE A CA    1 
ATOM   6539 C C     . PHE A 1 1003 ? 173.458 179.574 145.624 1.00 37.09  ? 1003 PHE A C     1 
ATOM   6540 O O     . PHE A 1 1003 ? 174.604 179.772 145.203 1.00 42.64  ? 1003 PHE A O     1 
ATOM   6541 C CB    . PHE A 1 1003 ? 171.593 181.231 145.325 1.00 27.44  ? 1003 PHE A CB    1 
ATOM   6542 C CG    . PHE A 1 1003 ? 172.255 182.487 144.851 1.00 26.30  ? 1003 PHE A CG    1 
ATOM   6543 C CD1   . PHE A 1 1003 ? 171.896 183.059 143.646 1.00 25.11  ? 1003 PHE A CD1   1 
ATOM   6544 C CD2   . PHE A 1 1003 ? 173.238 183.093 145.608 1.00 31.14  ? 1003 PHE A CD2   1 
ATOM   6545 C CE1   . PHE A 1 1003 ? 172.504 184.214 143.206 1.00 28.08  ? 1003 PHE A CE1   1 
ATOM   6546 C CE2   . PHE A 1 1003 ? 173.851 184.250 145.172 1.00 32.84  ? 1003 PHE A CE2   1 
ATOM   6547 C CZ    . PHE A 1 1003 ? 173.483 184.811 143.971 1.00 29.64  ? 1003 PHE A CZ    1 
ATOM   6548 N N     . THR A 1 1004 ? 173.227 179.021 146.810 1.00 31.24  ? 1004 THR A N     1 
ATOM   6549 C CA    . THR A 1 1004 ? 174.263 178.382 147.603 1.00 30.77  ? 1004 THR A CA    1 
ATOM   6550 C C     . THR A 1 1004 ? 173.894 176.920 147.788 1.00 38.25  ? 1004 THR A C     1 
ATOM   6551 O O     . THR A 1 1004 ? 172.735 176.591 148.058 1.00 41.66  ? 1004 THR A O     1 
ATOM   6552 C CB    . THR A 1 1004 ? 174.442 179.056 148.965 1.00 39.23  ? 1004 THR A CB    1 
ATOM   6553 O OG1   . THR A 1 1004 ? 173.164 179.429 149.491 1.00 41.86  ? 1004 THR A OG1   1 
ATOM   6554 C CG2   . THR A 1 1004 ? 175.320 180.285 148.836 1.00 42.33  ? 1004 THR A CG2   1 
ATOM   6555 N N     . ARG A 1 1005 ? 174.882 176.047 147.638 1.00 38.62  ? 1005 ARG A N     1 
ATOM   6556 C CA    . ARG A 1 1005 ? 174.654 174.613 147.633 1.00 40.45  ? 1005 ARG A CA    1 
ATOM   6557 C C     . ARG A 1 1005 ? 175.035 174.001 148.975 1.00 50.38  ? 1005 ARG A C     1 
ATOM   6558 O O     . ARG A 1 1005 ? 176.001 174.417 149.619 1.00 49.83  ? 1005 ARG A O     1 
ATOM   6559 C CB    . ARG A 1 1005 ? 175.448 173.949 146.508 1.00 46.43  ? 1005 ARG A CB    1 
ATOM   6560 C CG    . ARG A 1 1005 ? 175.107 174.475 145.125 1.00 46.13  ? 1005 ARG A CG    1 
ATOM   6561 C CD    . ARG A 1 1005 ? 175.781 173.658 144.039 1.00 41.82  ? 1005 ARG A CD    1 
ATOM   6562 N NE    . ARG A 1 1005 ? 175.276 172.291 143.995 1.00 42.17  ? 1005 ARG A NE    1 
ATOM   6563 C CZ    . ARG A 1 1005 ? 175.649 171.386 143.103 1.00 39.75  ? 1005 ARG A CZ    1 
ATOM   6564 N NH1   . ARG A 1 1005 ? 176.533 171.668 142.161 1.00 40.49  ? 1005 ARG A NH1   1 
ATOM   6565 N NH2   . ARG A 1 1005 ? 175.120 170.167 143.155 1.00 37.90  ? 1005 ARG A NH2   1 
ATOM   6566 N N     . CYS A 1 1006 ? 174.257 173.005 149.390 1.00 51.50  ? 1006 CYS A N     1 
ATOM   6567 C CA    . CYS A 1 1006 ? 174.528 172.292 150.626 1.00 47.54  ? 1006 CYS A CA    1 
ATOM   6568 C C     . CYS A 1 1006 ? 175.697 171.330 150.429 1.00 54.43  ? 1006 CYS A C     1 
ATOM   6569 O O     . CYS A 1 1006 ? 176.233 171.168 149.330 1.00 58.94  ? 1006 CYS A O     1 
ATOM   6570 C CB    . CYS A 1 1006 ? 173.284 171.539 151.091 1.00 52.40  ? 1006 CYS A CB    1 
ATOM   6571 S SG    . CYS A 1 1006 ? 171.806 172.559 151.253 1.00 82.08  ? 1006 CYS A SG    1 
ATOM   6572 N N     . TRP A 1 1007 ? 176.095 170.677 151.518 1.00 54.28  ? 1007 TRP A N     1 
ATOM   6573 C CA    . TRP A 1 1007 ? 177.150 169.676 151.486 1.00 50.13  ? 1007 TRP A CA    1 
ATOM   6574 C C     . TRP A 1 1007 ? 176.605 168.257 151.550 1.00 53.11  ? 1007 TRP A C     1 
ATOM   6575 O O     . TRP A 1 1007 ? 177.376 167.316 151.761 1.00 60.09  ? 1007 TRP A O     1 
ATOM   6576 C CB    . TRP A 1 1007 ? 178.136 169.913 152.629 1.00 51.98  ? 1007 TRP A CB    1 
ATOM   6577 C CG    . TRP A 1 1007 ? 178.956 171.150 152.458 1.00 57.63  ? 1007 TRP A CG    1 
ATOM   6578 C CD1   . TRP A 1 1007 ? 178.801 172.113 151.505 1.00 60.17  ? 1007 TRP A CD1   1 
ATOM   6579 C CD2   . TRP A 1 1007 ? 180.070 171.555 153.259 1.00 60.90  ? 1007 TRP A CD2   1 
ATOM   6580 N NE1   . TRP A 1 1007 ? 179.745 173.096 151.666 1.00 64.45  ? 1007 TRP A NE1   1 
ATOM   6581 C CE2   . TRP A 1 1007 ? 180.538 172.776 152.737 1.00 62.62  ? 1007 TRP A CE2   1 
ATOM   6582 C CE3   . TRP A 1 1007 ? 180.715 171.005 154.370 1.00 58.92  ? 1007 TRP A CE3   1 
ATOM   6583 C CZ2   . TRP A 1 1007 ? 181.620 173.455 153.287 1.00 60.10  ? 1007 TRP A CZ2   1 
ATOM   6584 C CZ3   . TRP A 1 1007 ? 181.788 171.680 154.913 1.00 64.17  ? 1007 TRP A CZ3   1 
ATOM   6585 C CH2   . TRP A 1 1007 ? 182.231 172.891 154.372 1.00 61.87  ? 1007 TRP A CH2   1 
ATOM   6586 N N     . ASN A 1 1008 ? 175.298 168.083 151.378 1.00 52.37  ? 1008 ASN A N     1 
ATOM   6587 C CA    . ASN A 1 1008 ? 174.675 166.765 151.368 1.00 53.51  ? 1008 ASN A CA    1 
ATOM   6588 C C     . ASN A 1 1008 ? 173.769 166.685 150.148 1.00 58.12  ? 1008 ASN A C     1 
ATOM   6589 O O     . ASN A 1 1008 ? 172.779 167.441 150.065 1.00 57.59  ? 1008 ASN A O     1 
ATOM   6590 C CB    . ASN A 1 1008 ? 173.895 166.516 152.660 1.00 56.97  ? 1008 ASN A CB    1 
ATOM   6591 C CG    . ASN A 1 1008 ? 173.308 165.124 152.725 1.00 62.01  ? 1008 ASN A CG    1 
ATOM   6592 O OD1   . ASN A 1 1008 ? 172.092 164.953 152.757 1.00 65.80  ? 1008 ASN A OD1   1 
ATOM   6593 N ND2   . ASN A 1 1008 ? 174.173 164.116 152.739 1.00 63.64  ? 1008 ASN A ND2   1 
ATOM   6594 N N     . PRO A 1 1009 ? 174.065 165.817 149.177 1.00 60.38  ? 1009 PRO A N     1 
ATOM   6595 C CA    . PRO A 1 1009 ? 173.215 165.740 147.978 1.00 54.93  ? 1009 PRO A CA    1 
ATOM   6596 C C     . PRO A 1 1009 ? 171.781 165.344 148.268 1.00 54.52  ? 1009 PRO A C     1 
ATOM   6597 O O     . PRO A 1 1009 ? 170.886 165.690 147.489 1.00 57.95  ? 1009 PRO A O     1 
ATOM   6598 C CB    . PRO A 1 1009 ? 173.925 164.688 147.116 1.00 49.48  ? 1009 PRO A CB    1 
ATOM   6599 C CG    . PRO A 1 1009 ? 175.332 164.704 147.588 1.00 49.26  ? 1009 PRO A CG    1 
ATOM   6600 C CD    . PRO A 1 1009 ? 175.257 164.962 149.061 1.00 54.85  ? 1009 PRO A CD    1 
ATOM   6601 N N     . ALA A 1 1010 ? 171.532 164.614 149.357 1.00 53.42  ? 1010 ALA A N     1 
ATOM   6602 C CA    . ALA A 1 1010 ? 170.164 164.234 149.691 1.00 50.75  ? 1010 ALA A CA    1 
ATOM   6603 C C     . ALA A 1 1010 ? 169.316 165.458 150.014 1.00 54.36  ? 1010 ALA A C     1 
ATOM   6604 O O     . ALA A 1 1010 ? 168.148 165.535 149.615 1.00 57.59  ? 1010 ALA A O     1 
ATOM   6605 C CB    . ALA A 1 1010 ? 170.161 163.251 150.861 1.00 57.03  ? 1010 ALA A CB    1 
ATOM   6606 N N     . LYS A 1 1011 ? 169.885 166.423 150.740 1.00 55.92  ? 1011 LYS A N     1 
ATOM   6607 C CA    . LYS A 1 1011 ? 169.153 167.651 151.038 1.00 53.51  ? 1011 LYS A CA    1 
ATOM   6608 C C     . LYS A 1 1011 ? 168.858 168.443 149.771 1.00 51.64  ? 1011 LYS A C     1 
ATOM   6609 O O     . LYS A 1 1011 ? 167.753 168.976 149.610 1.00 51.20  ? 1011 LYS A O     1 
ATOM   6610 C CB    . LYS A 1 1011 ? 169.938 168.503 152.034 1.00 55.90  ? 1011 LYS A CB    1 
ATOM   6611 C CG    . LYS A 1 1011 ? 170.026 167.909 153.428 1.00 59.73  ? 1011 LYS A CG    1 
ATOM   6612 C CD    . LYS A 1 1011 ? 170.719 168.864 154.385 1.00 69.98  ? 1011 LYS A CD    1 
ATOM   6613 C CE    . LYS A 1 1011 ? 170.001 170.202 154.443 1.00 70.37  ? 1011 LYS A CE    1 
ATOM   6614 N NZ    . LYS A 1 1011 ? 170.702 171.165 155.334 1.00 76.31  ? 1011 LYS A NZ    1 
ATOM   6615 N N     . GLU A 1 1012 ? 169.832 168.534 148.861 1.00 48.89  ? 1012 GLU A N     1 
ATOM   6616 C CA    . GLU A 1 1012 ? 169.596 169.220 147.594 1.00 45.42  ? 1012 GLU A CA    1 
ATOM   6617 C C     . GLU A 1 1012 ? 168.508 168.529 146.788 1.00 46.55  ? 1012 GLU A C     1 
ATOM   6618 O O     . GLU A 1 1012 ? 167.653 169.191 146.191 1.00 49.00  ? 1012 GLU A O     1 
ATOM   6619 C CB    . GLU A 1 1012 ? 170.883 169.292 146.777 1.00 48.34  ? 1012 GLU A CB    1 
ATOM   6620 C CG    . GLU A 1 1012 ? 171.813 170.411 147.178 1.00 53.41  ? 1012 GLU A CG    1 
ATOM   6621 C CD    . GLU A 1 1012 ? 172.843 170.703 146.111 1.00 52.30  ? 1012 GLU A CD    1 
ATOM   6622 O OE1   . GLU A 1 1012 ? 172.602 170.353 144.937 1.00 51.11  ? 1012 GLU A OE1   1 
ATOM   6623 O OE2   . GLU A 1 1012 ? 173.895 171.277 146.447 1.00 56.45  ? 1012 GLU A OE2   1 
ATOM   6624 N N     . ASP A 1 1013 ? 168.532 167.200 146.744 1.00 47.35  ? 1013 ASP A N     1 
ATOM   6625 C CA    . ASP A 1 1013 ? 167.492 166.462 146.046 1.00 44.63  ? 1013 ASP A CA    1 
ATOM   6626 C C     . ASP A 1 1013 ? 166.117 166.658 146.667 1.00 48.34  ? 1013 ASP A C     1 
ATOM   6627 O O     . ASP A 1 1013 ? 165.153 166.871 145.930 1.00 49.84  ? 1013 ASP A O     1 
ATOM   6628 C CB    . ASP A 1 1013 ? 167.846 164.974 146.003 1.00 51.54  ? 1013 ASP A CB    1 
ATOM   6629 C CG    . ASP A 1 1013 ? 169.088 164.698 145.177 1.00 57.19  ? 1013 ASP A CG    1 
ATOM   6630 O OD1   . ASP A 1 1013 ? 169.362 165.478 144.240 1.00 50.50  ? 1013 ASP A OD1   1 
ATOM   6631 O OD2   . ASP A 1 1013 ? 169.791 163.706 145.463 1.00 63.91  ? 1013 ASP A OD2   1 
ATOM   6632 N N     . GLN A 1 1014 ? 166.006 166.628 147.994 1.00 51.42  ? 1014 GLN A N     1 
ATOM   6633 C CA    . GLN A 1 1014 ? 164.733 166.870 148.661 1.00 48.44  ? 1014 GLN A CA    1 
ATOM   6634 C C     . GLN A 1 1014 ? 164.231 168.297 148.491 1.00 49.20  ? 1014 GLN A C     1 
ATOM   6635 O O     . GLN A 1 1014 ? 163.015 168.505 148.452 1.00 52.98  ? 1014 GLN A O     1 
ATOM   6636 C CB    . GLN A 1 1014 ? 164.839 166.543 150.155 1.00 53.79  ? 1014 GLN A CB    1 
ATOM   6637 C CG    . GLN A 1 1014 ? 165.072 165.070 150.451 1.00 67.90  ? 1014 GLN A CG    1 
ATOM   6638 C CD    . GLN A 1 1014 ? 164.004 164.174 149.853 1.00 72.56  ? 1014 GLN A CD    1 
ATOM   6639 O OE1   . GLN A 1 1014 ? 164.235 163.498 148.851 1.00 67.29  ? 1014 GLN A OE1   1 
ATOM   6640 N NE2   . GLN A 1 1014 ? 162.828 164.165 150.468 1.00 68.03  ? 1014 GLN A NE2   1 
ATOM   6641 N N     . ALA A 1 1015 ? 165.127 169.278 148.396 1.00 51.29  ? 1015 ALA A N     1 
ATOM   6642 C CA    . ALA A 1 1015 ? 164.741 170.654 148.113 1.00 42.64  ? 1015 ALA A CA    1 
ATOM   6643 C C     . ALA A 1 1015 ? 164.299 170.854 146.671 1.00 42.76  ? 1015 ALA A C     1 
ATOM   6644 O O     . ALA A 1 1015 ? 163.320 171.562 146.421 1.00 43.14  ? 1015 ALA A O     1 
ATOM   6645 C CB    . ALA A 1 1015 ? 165.899 171.605 148.428 1.00 40.79  ? 1015 ALA A CB    1 
ATOM   6646 N N     . THR A 1 1016 ? 165.002 170.245 145.714 1.00 39.77  ? 1016 THR A N     1 
ATOM   6647 C CA    . THR A 1 1016 ? 164.561 170.274 144.326 1.00 37.56  ? 1016 THR A CA    1 
ATOM   6648 C C     . THR A 1 1016 ? 163.259 169.511 144.129 1.00 43.09  ? 1016 THR A C     1 
ATOM   6649 O O     . THR A 1 1016 ? 162.496 169.832 143.211 1.00 47.84  ? 1016 THR A O     1 
ATOM   6650 C CB    . THR A 1 1016 ? 165.650 169.700 143.417 1.00 40.77  ? 1016 THR A CB    1 
ATOM   6651 O OG1   . THR A 1 1016 ? 166.904 170.321 143.722 1.00 40.04  ? 1016 THR A OG1   1 
ATOM   6652 C CG2   . THR A 1 1016 ? 165.320 169.950 141.957 1.00 39.92  ? 1016 THR A CG2   1 
ATOM   6653 N N     . ASP A 1 1017 ? 162.978 168.526 144.984 1.00 44.75  ? 1017 ASP A N     1 
ATOM   6654 C CA    . ASP A 1 1017 ? 161.739 167.761 144.924 1.00 44.47  ? 1017 ASP A CA    1 
ATOM   6655 C C     . ASP A 1 1017 ? 160.580 168.474 145.603 1.00 49.66  ? 1017 ASP A C     1 
ATOM   6656 O O     . ASP A 1 1017 ? 159.631 167.819 146.048 1.00 54.37  ? 1017 ASP A O     1 
ATOM   6657 C CB    . ASP A 1 1017 ? 161.940 166.375 145.537 1.00 47.31  ? 1017 ASP A CB    1 
ATOM   6658 C CG    . ASP A 1 1017 ? 162.862 165.502 144.713 1.00 57.83  ? 1017 ASP A CG    1 
ATOM   6659 O OD1   . ASP A 1 1017 ? 163.475 166.018 143.755 1.00 53.15  ? 1017 ASP A OD1   1 
ATOM   6660 O OD2   . ASP A 1 1017 ? 162.973 164.299 145.025 1.00 67.06  ? 1017 ASP A OD2   1 
ATOM   6661 N N     . ARG A 1 1018 ? 160.660 169.795 145.748 1.00 51.33  ? 1018 ARG A N     1 
ATOM   6662 C CA    . ARG A 1 1018 ? 159.493 170.610 146.053 1.00 49.40  ? 1018 ARG A CA    1 
ATOM   6663 C C     . ARG A 1 1018 ? 158.766 171.062 144.799 1.00 50.37  ? 1018 ARG A C     1 
ATOM   6664 O O     . ARG A 1 1018 ? 157.546 171.248 144.832 1.00 55.57  ? 1018 ARG A O     1 
ATOM   6665 C CB    . ARG A 1 1018 ? 159.897 171.836 146.877 1.00 49.85  ? 1018 ARG A CB    1 
ATOM   6666 C CG    . ARG A 1 1018 ? 160.562 171.493 148.196 1.00 53.33  ? 1018 ARG A CG    1 
ATOM   6667 C CD    . ARG A 1 1018 ? 159.613 170.741 149.112 1.00 60.79  ? 1018 ARG A CD    1 
ATOM   6668 N NE    . ARG A 1 1018 ? 160.250 169.584 149.730 1.00 63.81  ? 1018 ARG A NE    1 
ATOM   6669 C CZ    . ARG A 1 1018 ? 160.055 168.330 149.348 1.00 63.37  ? 1018 ARG A CZ    1 
ATOM   6670 N NH1   . ARG A 1 1018 ? 159.225 168.028 148.364 1.00 61.73  ? 1018 ARG A NH1   1 
ATOM   6671 N NH2   . ARG A 1 1018 ? 160.707 167.353 149.971 1.00 62.22  ? 1018 ARG A NH2   1 
ATOM   6672 N N     . ALA A 1 1019 ? 159.496 171.242 143.699 1.00 48.87  ? 1019 ALA A N     1 
ATOM   6673 C CA    . ALA A 1 1019 ? 158.908 171.522 142.394 1.00 47.27  ? 1019 ALA A CA    1 
ATOM   6674 C C     . ALA A 1 1019 ? 158.863 170.258 141.540 1.00 51.19  ? 1019 ALA A C     1 
ATOM   6675 O O     . ALA A 1 1019 ? 157.838 169.949 140.925 1.00 56.30  ? 1019 ALA A O     1 
ATOM   6676 C CB    . ALA A 1 1019 ? 159.697 172.629 141.689 1.00 47.31  ? 1019 ALA A CB    1 
ATOM   6677 N N     . TYR A 1 1020 ? 159.972 169.525 141.493 1.00 45.60  ? 1020 TYR A N     1 
ATOM   6678 C CA    . TYR A 1 1020 ? 160.016 168.262 140.770 1.00 46.72  ? 1020 TYR A CA    1 
ATOM   6679 C C     . TYR A 1 1020 ? 159.273 167.191 141.558 1.00 50.50  ? 1020 TYR A C     1 
ATOM   6680 O O     . TYR A 1 1020 ? 159.836 166.571 142.466 1.00 51.49  ? 1020 TYR A O     1 
ATOM   6681 C CB    . TYR A 1 1020 ? 161.471 167.858 140.534 1.00 44.96  ? 1020 TYR A CB    1 
ATOM   6682 C CG    . TYR A 1 1020 ? 161.656 166.636 139.670 1.00 49.74  ? 1020 TYR A CG    1 
ATOM   6683 C CD1   . TYR A 1 1020 ? 161.235 166.626 138.348 1.00 50.35  ? 1020 TYR A CD1   1 
ATOM   6684 C CD2   . TYR A 1 1020 ? 162.274 165.499 140.170 1.00 52.47  ? 1020 TYR A CD2   1 
ATOM   6685 C CE1   . TYR A 1 1020 ? 161.408 165.511 137.554 1.00 53.97  ? 1020 TYR A CE1   1 
ATOM   6686 C CE2   . TYR A 1 1020 ? 162.453 164.380 139.382 1.00 51.94  ? 1020 TYR A CE2   1 
ATOM   6687 C CZ    . TYR A 1 1020 ? 162.019 164.392 138.076 1.00 52.53  ? 1020 TYR A CZ    1 
ATOM   6688 O OH    . TYR A 1 1020 ? 162.196 163.279 137.289 1.00 53.52  ? 1020 TYR A OH    1 
ATOM   6689 N N     . ARG A 1 1021 ? 158.010 166.968 141.202 1.00 51.58  ? 1021 ARG A N     1 
ATOM   6690 C CA    . ARG A 1 1021 ? 157.104 166.139 141.988 1.00 55.70  ? 1021 ARG A CA    1 
ATOM   6691 C C     . ARG A 1 1021 ? 156.054 165.535 141.069 1.00 63.24  ? 1021 ARG A C     1 
ATOM   6692 O O     . ARG A 1 1021 ? 155.945 165.900 139.896 1.00 68.53  ? 1021 ARG A O     1 
ATOM   6693 C CB    . ARG A 1 1021 ? 156.401 166.942 143.085 1.00 60.48  ? 1021 ARG A CB    1 
ATOM   6694 C CG    . ARG A 1 1021 ? 157.255 167.271 144.278 1.00 58.64  ? 1021 ARG A CG    1 
ATOM   6695 C CD    . ARG A 1 1021 ? 156.518 168.188 145.231 1.00 62.08  ? 1021 ARG A CD    1 
ATOM   6696 N NE    . ARG A 1 1021 ? 155.307 167.569 145.754 1.00 67.40  ? 1021 ARG A NE    1 
ATOM   6697 C CZ    . ARG A 1 1021 ? 155.256 166.853 146.868 1.00 70.79  ? 1021 ARG A CZ    1 
ATOM   6698 N NH1   . ARG A 1 1021 ? 156.336 166.640 147.602 1.00 65.73  ? 1021 ARG A NH1   1 
ATOM   6699 N NH2   . ARG A 1 1021 ? 154.092 166.340 147.256 1.00 70.96  ? 1021 ARG A NH2   1 
ATOM   6700 N N     . ILE A 1 1022 ? 155.281 164.609 141.625 1.00 63.17  ? 1022 ILE A N     1 
ATOM   6701 C CA    . ILE A 1 1022 ? 154.062 164.141 140.978 1.00 65.69  ? 1022 ILE A CA    1 
ATOM   6702 C C     . ILE A 1 1022 ? 153.004 165.226 141.121 1.00 67.19  ? 1022 ILE A C     1 
ATOM   6703 O O     . ILE A 1 1022 ? 152.719 165.690 142.231 1.00 66.05  ? 1022 ILE A O     1 
ATOM   6704 C CB    . ILE A 1 1022 ? 153.590 162.815 141.593 1.00 60.83  ? 1022 ILE A CB    1 
ATOM   6705 C CG1   . ILE A 1 1022 ? 154.681 161.751 141.459 1.00 61.78  ? 1022 ILE A CG1   1 
ATOM   6706 C CG2   . ILE A 1 1022 ? 152.301 162.351 140.936 1.00 56.40  ? 1022 ILE A CG2   1 
ATOM   6707 C CD1   . ILE A 1 1022 ? 154.312 160.418 142.069 1.00 62.87  ? 1022 ILE A CD1   1 
ATOM   6708 N N     . GLY A 1 1023 ? 152.422 165.635 140.002 1.00 64.87  ? 1023 GLY A N     1 
ATOM   6709 C CA    . GLY A 1 1023 ? 151.551 166.784 139.968 1.00 62.27  ? 1023 GLY A CA    1 
ATOM   6710 C C     . GLY A 1 1023 ? 152.204 168.057 139.484 1.00 65.62  ? 1023 GLY A C     1 
ATOM   6711 O O     . GLY A 1 1023 ? 151.614 169.132 139.639 1.00 70.36  ? 1023 GLY A O     1 
ATOM   6712 N N     . GLN A 1 1024 ? 153.402 167.974 138.910 1.00 61.52  ? 1024 GLN A N     1 
ATOM   6713 C CA    . GLN A 1 1024 ? 154.086 169.114 138.308 1.00 59.85  ? 1024 GLN A CA    1 
ATOM   6714 C C     . GLN A 1 1024 ? 153.837 169.050 136.808 1.00 62.27  ? 1024 GLN A C     1 
ATOM   6715 O O     . GLN A 1 1024 ? 154.341 168.150 136.127 1.00 61.27  ? 1024 GLN A O     1 
ATOM   6716 C CB    . GLN A 1 1024 ? 155.580 169.092 138.627 1.00 57.72  ? 1024 GLN A CB    1 
ATOM   6717 C CG    . GLN A 1 1024 ? 156.402 170.121 137.871 1.00 61.86  ? 1024 GLN A CG    1 
ATOM   6718 C CD    . GLN A 1 1024 ? 156.221 171.529 138.399 1.00 63.68  ? 1024 GLN A CD    1 
ATOM   6719 O OE1   . GLN A 1 1024 ? 155.256 172.213 138.062 1.00 65.36  ? 1024 GLN A OE1   1 
ATOM   6720 N NE2   . GLN A 1 1024 ? 157.157 171.972 139.230 1.00 57.92  ? 1024 GLN A NE2   1 
ATOM   6721 N N     . THR A 1 1025 ? 153.061 170.002 136.299 1.00 60.07  ? 1025 THR A N     1 
ATOM   6722 C CA    . THR A 1 1025 ? 152.565 169.967 134.930 1.00 62.01  ? 1025 THR A CA    1 
ATOM   6723 C C     . THR A 1 1025 ? 153.507 170.623 133.928 1.00 66.15  ? 1025 THR A C     1 
ATOM   6724 O O     . THR A 1 1025 ? 153.173 170.683 132.740 1.00 66.02  ? 1025 THR A O     1 
ATOM   6725 C CB    . THR A 1 1025 ? 151.194 170.642 134.858 1.00 61.80  ? 1025 THR A CB    1 
ATOM   6726 O OG1   . THR A 1 1025 ? 151.320 172.018 135.235 1.00 54.90  ? 1025 THR A OG1   1 
ATOM   6727 C CG2   . THR A 1 1025 ? 150.217 169.957 135.801 1.00 55.59  ? 1025 THR A CG2   1 
ATOM   6728 N N     . LYS A 1 1026 ? 154.663 171.114 134.367 1.00 65.17  ? 1026 LYS A N     1 
ATOM   6729 C CA    . LYS A 1 1026 ? 155.601 171.774 133.474 1.00 61.70  ? 1026 LYS A CA    1 
ATOM   6730 C C     . LYS A 1 1026 ? 157.004 171.254 133.750 1.00 60.30  ? 1026 LYS A C     1 
ATOM   6731 O O     . LYS A 1 1026 ? 157.283 170.697 134.814 1.00 59.40  ? 1026 LYS A O     1 
ATOM   6732 C CB    . LYS A 1 1026 ? 155.545 173.301 133.631 1.00 60.60  ? 1026 LYS A CB    1 
ATOM   6733 C CG    . LYS A 1 1026 ? 156.140 174.071 132.458 1.00 69.29  ? 1026 LYS A CG    1 
ATOM   6734 C CD    . LYS A 1 1026 ? 155.884 175.564 132.575 1.00 69.66  ? 1026 LYS A CD    1 
ATOM   6735 C CE    . LYS A 1 1026 ? 156.443 176.310 131.374 1.00 66.17  ? 1026 LYS A CE    1 
ATOM   6736 N NZ    . LYS A 1 1026 ? 156.116 177.761 131.424 1.00 62.74  ? 1026 LYS A NZ    1 
ATOM   6737 N N     . ASN A 1 1027 ? 157.883 171.427 132.765 1.00 55.92  ? 1027 ASN A N     1 
ATOM   6738 C CA    . ASN A 1 1027 ? 159.270 171.014 132.917 1.00 53.22  ? 1027 ASN A CA    1 
ATOM   6739 C C     . ASN A 1 1027 ? 159.921 171.751 134.079 1.00 49.23  ? 1027 ASN A C     1 
ATOM   6740 O O     . ASN A 1 1027 ? 159.666 172.934 134.316 1.00 56.31  ? 1027 ASN A O     1 
ATOM   6741 C CB    . ASN A 1 1027 ? 160.052 171.282 131.631 1.00 55.05  ? 1027 ASN A CB    1 
ATOM   6742 C CG    . ASN A 1 1027 ? 159.500 170.524 130.444 1.00 63.48  ? 1027 ASN A CG    1 
ATOM   6743 O OD1   . ASN A 1 1027 ? 158.389 169.997 130.490 1.00 66.88  ? 1027 ASN A OD1   1 
ATOM   6744 N ND2   . ASN A 1 1027 ? 160.274 170.467 129.368 1.00 64.25  ? 1027 ASN A ND2   1 
ATOM   6745 N N     . VAL A 1 1028 ? 160.769 171.036 134.810 1.00 42.73  ? 1028 VAL A N     1 
ATOM   6746 C CA    . VAL A 1 1028 ? 161.487 171.593 135.949 1.00 42.78  ? 1028 VAL A CA    1 
ATOM   6747 C C     . VAL A 1 1028 ? 162.896 171.942 135.494 1.00 38.66  ? 1028 VAL A C     1 
ATOM   6748 O O     . VAL A 1 1028 ? 163.630 171.078 135.000 1.00 40.79  ? 1028 VAL A O     1 
ATOM   6749 C CB    . VAL A 1 1028 ? 161.511 170.615 137.133 1.00 38.47  ? 1028 VAL A CB    1 
ATOM   6750 C CG1   . VAL A 1 1028 ? 162.283 171.216 138.297 1.00 32.95  ? 1028 VAL A CG1   1 
ATOM   6751 C CG2   . VAL A 1 1028 ? 160.096 170.261 137.552 1.00 43.41  ? 1028 VAL A CG2   1 
ATOM   6752 N N     . TYR A 1 1029 ? 163.273 173.206 135.654 1.00 33.61  ? 1029 TYR A N     1 
ATOM   6753 C CA    . TYR A 1 1029 ? 164.596 173.694 135.285 1.00 34.69  ? 1029 TYR A CA    1 
ATOM   6754 C C     . TYR A 1 1029 ? 165.390 173.905 136.566 1.00 29.80  ? 1029 TYR A C     1 
ATOM   6755 O O     . TYR A 1 1029 ? 165.095 174.819 137.342 1.00 31.17  ? 1029 TYR A O     1 
ATOM   6756 C CB    . TYR A 1 1029 ? 164.500 174.986 134.478 1.00 36.96  ? 1029 TYR A CB    1 
ATOM   6757 C CG    . TYR A 1 1029 ? 163.635 174.879 133.244 1.00 38.92  ? 1029 TYR A CG    1 
ATOM   6758 C CD1   . TYR A 1 1029 ? 162.268 175.115 133.309 1.00 41.76  ? 1029 TYR A CD1   1 
ATOM   6759 C CD2   . TYR A 1 1029 ? 164.185 174.548 132.015 1.00 34.80  ? 1029 TYR A CD2   1 
ATOM   6760 C CE1   . TYR A 1 1029 ? 161.475 175.020 132.186 1.00 44.01  ? 1029 TYR A CE1   1 
ATOM   6761 C CE2   . TYR A 1 1029 ? 163.399 174.450 130.886 1.00 44.28  ? 1029 TYR A CE2   1 
ATOM   6762 C CZ    . TYR A 1 1029 ? 162.045 174.688 130.977 1.00 50.85  ? 1029 TYR A CZ    1 
ATOM   6763 O OH    . TYR A 1 1029 ? 161.259 174.592 129.852 1.00 50.18  ? 1029 TYR A OH    1 
ATOM   6764 N N     . VAL A 1 1030 ? 166.394 173.064 136.785 1.00 26.04  ? 1030 VAL A N     1 
ATOM   6765 C CA    . VAL A 1 1030 ? 167.212 173.114 137.989 1.00 31.04  ? 1030 VAL A CA    1 
ATOM   6766 C C     . VAL A 1 1030 ? 168.492 173.863 137.660 1.00 27.34  ? 1030 VAL A C     1 
ATOM   6767 O O     . VAL A 1 1030 ? 169.224 173.486 136.738 1.00 27.28  ? 1030 VAL A O     1 
ATOM   6768 C CB    . VAL A 1 1030 ? 167.511 171.706 138.523 1.00 32.01  ? 1030 VAL A CB    1 
ATOM   6769 C CG1   . VAL A 1 1030 ? 168.123 171.789 139.908 1.00 27.17  ? 1030 VAL A CG1   1 
ATOM   6770 C CG2   . VAL A 1 1030 ? 166.246 170.876 138.545 1.00 29.74  ? 1030 VAL A CG2   1 
ATOM   6771 N N     . TYR A 1 1031 ? 168.761 174.925 138.410 1.00 30.20  ? 1031 TYR A N     1 
ATOM   6772 C CA    . TYR A 1 1031 ? 169.915 175.780 138.186 1.00 29.55  ? 1031 TYR A CA    1 
ATOM   6773 C C     . TYR A 1 1031 ? 170.922 175.569 139.305 1.00 32.97  ? 1031 TYR A C     1 
ATOM   6774 O O     . TYR A 1 1031 ? 170.556 175.567 140.484 1.00 34.04  ? 1031 TYR A O     1 
ATOM   6775 C CB    . TYR A 1 1031 ? 169.505 177.252 138.118 1.00 25.66  ? 1031 TYR A CB    1 
ATOM   6776 C CG    . TYR A 1 1031 ? 168.495 177.570 137.040 1.00 23.13  ? 1031 TYR A CG    1 
ATOM   6777 C CD1   . TYR A 1 1031 ? 167.133 177.429 137.273 1.00 27.74  ? 1031 TYR A CD1   1 
ATOM   6778 C CD2   . TYR A 1 1031 ? 168.901 178.022 135.794 1.00 22.37  ? 1031 TYR A CD2   1 
ATOM   6779 C CE1   . TYR A 1 1031 ? 166.208 177.722 136.294 1.00 26.19  ? 1031 TYR A CE1   1 
ATOM   6780 C CE2   . TYR A 1 1031 ? 167.984 178.319 134.809 1.00 25.24  ? 1031 TYR A CE2   1 
ATOM   6781 C CZ    . TYR A 1 1031 ? 166.639 178.166 135.064 1.00 27.50  ? 1031 TYR A CZ    1 
ATOM   6782 O OH    . TYR A 1 1031 ? 165.721 178.461 134.084 1.00 31.67  ? 1031 TYR A OH    1 
ATOM   6783 N N     . TYR A 1 1032 ? 172.186 175.394 138.932 1.00 34.03  ? 1032 TYR A N     1 
ATOM   6784 C CA    . TYR A 1 1032 ? 173.292 175.274 139.881 1.00 33.57  ? 1032 TYR A CA    1 
ATOM   6785 C C     . TYR A 1 1032 ? 174.354 176.293 139.500 1.00 36.21  ? 1032 TYR A C     1 
ATOM   6786 O O     . TYR A 1 1032 ? 175.409 175.936 138.962 1.00 39.65  ? 1032 TYR A O     1 
ATOM   6787 C CB    . TYR A 1 1032 ? 173.881 173.863 139.885 1.00 33.52  ? 1032 TYR A CB    1 
ATOM   6788 C CG    . TYR A 1 1032 ? 172.941 172.774 140.342 1.00 31.48  ? 1032 TYR A CG    1 
ATOM   6789 C CD1   . TYR A 1 1032 ? 172.600 172.640 141.680 1.00 32.72  ? 1032 TYR A CD1   1 
ATOM   6790 C CD2   . TYR A 1 1032 ? 172.418 171.862 139.438 1.00 30.90  ? 1032 TYR A CD2   1 
ATOM   6791 C CE1   . TYR A 1 1032 ? 171.751 171.639 142.101 1.00 32.77  ? 1032 TYR A CE1   1 
ATOM   6792 C CE2   . TYR A 1 1032 ? 171.570 170.859 139.850 1.00 30.45  ? 1032 TYR A CE2   1 
ATOM   6793 C CZ    . TYR A 1 1032 ? 171.240 170.751 141.182 1.00 34.11  ? 1032 TYR A CZ    1 
ATOM   6794 O OH    . TYR A 1 1032 ? 170.392 169.750 141.594 1.00 43.00  ? 1032 TYR A OH    1 
ATOM   6795 N N     . PRO A 1 1033 ? 174.103 177.581 139.757 1.00 34.38  ? 1033 PRO A N     1 
ATOM   6796 C CA    . PRO A 1 1033 ? 175.082 178.605 139.373 1.00 32.87  ? 1033 PRO A CA    1 
ATOM   6797 C C     . PRO A 1 1033 ? 176.428 178.372 140.035 1.00 38.28  ? 1033 PRO A C     1 
ATOM   6798 O O     . PRO A 1 1033 ? 176.562 178.472 141.258 1.00 46.14  ? 1033 PRO A O     1 
ATOM   6799 C CB    . PRO A 1 1033 ? 174.432 179.911 139.843 1.00 32.26  ? 1033 PRO A CB    1 
ATOM   6800 C CG    . PRO A 1 1033 ? 173.463 179.499 140.897 1.00 31.86  ? 1033 PRO A CG    1 
ATOM   6801 C CD    . PRO A 1 1033 ? 172.953 178.159 140.472 1.00 32.08  ? 1033 PRO A CD    1 
ATOM   6802 N N     . THR A 1 1034 ? 177.431 178.049 139.225 1.00 35.60  ? 1034 THR A N     1 
ATOM   6803 C CA    . THR A 1 1034 ? 178.764 177.720 139.704 1.00 37.12  ? 1034 THR A CA    1 
ATOM   6804 C C     . THR A 1 1034 ? 179.759 178.700 139.107 1.00 38.38  ? 1034 THR A C     1 
ATOM   6805 O O     . THR A 1 1034 ? 179.803 178.880 137.886 1.00 42.12  ? 1034 THR A O     1 
ATOM   6806 C CB    . THR A 1 1034 ? 179.143 176.282 139.333 1.00 44.52  ? 1034 THR A CB    1 
ATOM   6807 O OG1   . THR A 1 1034 ? 178.205 175.372 139.919 1.00 43.65  ? 1034 THR A OG1   1 
ATOM   6808 C CG2   . THR A 1 1034 ? 180.534 175.950 139.835 1.00 50.82  ? 1034 THR A CG2   1 
ATOM   6809 N N     . VAL A 1 1035 ? 180.549 179.329 139.964 1.00 40.09  ? 1035 VAL A N     1 
ATOM   6810 C CA    . VAL A 1 1035 ? 181.582 180.258 139.527 1.00 45.69  ? 1035 VAL A CA    1 
ATOM   6811 C C     . VAL A 1 1035 ? 182.880 179.485 139.348 1.00 49.20  ? 1035 VAL A C     1 
ATOM   6812 O O     . VAL A 1 1035 ? 183.348 178.813 140.275 1.00 52.87  ? 1035 VAL A O     1 
ATOM   6813 C CB    . VAL A 1 1035 ? 181.751 181.407 140.534 1.00 41.82  ? 1035 VAL A CB    1 
ATOM   6814 C CG1   . VAL A 1 1035 ? 182.732 182.424 140.001 1.00 44.62  ? 1035 VAL A CG1   1 
ATOM   6815 C CG2   . VAL A 1 1035 ? 180.411 182.061 140.817 1.00 39.71  ? 1035 VAL A CG2   1 
ATOM   6816 N N     . ARG A 1 1036 ? 183.461 179.576 138.156 1.00 45.95  ? 1036 ARG A N     1 
ATOM   6817 C CA    . ARG A 1 1036 ? 184.672 178.850 137.816 1.00 49.58  ? 1036 ARG A CA    1 
ATOM   6818 C C     . ARG A 1 1036 ? 185.758 179.825 137.385 1.00 57.41  ? 1036 ARG A C     1 
ATOM   6819 O O     . ARG A 1 1036 ? 185.482 180.936 136.928 1.00 56.87  ? 1036 ARG A O     1 
ATOM   6820 C CB    . ARG A 1 1036 ? 184.414 177.832 136.699 1.00 50.63  ? 1036 ARG A CB    1 
ATOM   6821 C CG    . ARG A 1 1036 ? 183.279 176.867 136.984 1.00 52.82  ? 1036 ARG A CG    1 
ATOM   6822 C CD    . ARG A 1 1036 ? 183.067 175.921 135.818 1.00 58.13  ? 1036 ARG A CD    1 
ATOM   6823 N NE    . ARG A 1 1036 ? 181.872 175.104 135.985 1.00 60.05  ? 1036 ARG A NE    1 
ATOM   6824 C CZ    . ARG A 1 1036 ? 181.863 173.886 136.508 1.00 65.00  ? 1036 ARG A CZ    1 
ATOM   6825 N NH1   . ARG A 1 1036 ? 182.975 173.307 136.929 1.00 65.39  ? 1036 ARG A NH1   1 
ATOM   6826 N NH2   . ARG A 1 1036 ? 180.710 173.232 136.608 1.00 59.78  ? 1036 ARG A NH2   1 
ATOM   6827 N N     . ASP A 1 1037 ? 187.005 179.393 137.540 1.00 61.65  ? 1037 ASP A N     1 
ATOM   6828 C CA    . ASP A 1 1037 ? 188.159 180.175 137.131 1.00 62.49  ? 1037 ASP A CA    1 
ATOM   6829 C C     . ASP A 1 1037 ? 189.057 179.310 136.259 1.00 73.57  ? 1037 ASP A C     1 
ATOM   6830 O O     . ASP A 1 1037 ? 189.191 178.104 136.483 1.00 75.52  ? 1037 ASP A O     1 
ATOM   6831 C CB    . ASP A 1 1037 ? 188.937 180.702 138.347 1.00 68.76  ? 1037 ASP A CB    1 
ATOM   6832 C CG    . ASP A 1 1037 ? 189.862 181.854 138.001 1.00 72.11  ? 1037 ASP A CG    1 
ATOM   6833 O OD1   . ASP A 1 1037 ? 190.489 181.821 136.922 1.00 76.41  ? 1037 ASP A OD1   1 
ATOM   6834 O OD2   . ASP A 1 1037 ? 189.960 182.797 138.812 1.00 68.37  ? 1037 ASP A OD2   1 
ATOM   6835 N N     . THR A 1 1038 ? 189.671 179.939 135.257 1.00 79.19  ? 1038 THR A N     1 
ATOM   6836 C CA    . THR A 1 1038 ? 190.524 179.211 134.326 1.00 82.61  ? 1038 THR A CA    1 
ATOM   6837 C C     . THR A 1 1038 ? 191.858 178.806 134.938 1.00 83.15  ? 1038 THR A C     1 
ATOM   6838 O O     . THR A 1 1038 ? 192.511 177.896 134.417 1.00 83.21  ? 1038 THR A O     1 
ATOM   6839 C CB    . THR A 1 1038 ? 190.775 180.048 133.070 1.00 79.28  ? 1038 THR A CB    1 
ATOM   6840 O OG1   . THR A 1 1038 ? 191.389 181.289 133.435 1.00 79.78  ? 1038 THR A OG1   1 
ATOM   6841 C CG2   . THR A 1 1038 ? 189.466 180.328 132.348 1.00 79.11  ? 1038 THR A CG2   1 
ATOM   6842 N N     . GLU A 1 1039 ? 192.278 179.456 136.023 1.00 79.80  ? 1039 GLU A N     1 
ATOM   6843 C CA    . GLU A 1 1039 ? 193.523 179.118 136.693 1.00 82.23  ? 1039 GLU A CA    1 
ATOM   6844 C C     . GLU A 1 1039 ? 193.340 178.643 138.125 1.00 80.18  ? 1039 GLU A C     1 
ATOM   6845 O O     . GLU A 1 1039 ? 194.289 178.099 138.702 1.00 80.24  ? 1039 GLU A O     1 
ATOM   6846 C CB    . GLU A 1 1039 ? 194.479 180.322 136.695 1.00 92.08  ? 1039 GLU A CB    1 
ATOM   6847 C CG    . GLU A 1 1039 ? 194.946 180.756 135.316 1.00 95.43  ? 1039 GLU A CG    1 
ATOM   6848 C CD    . GLU A 1 1039 ? 195.938 181.902 135.373 1.00 100.35 ? 1039 GLU A CD    1 
ATOM   6849 O OE1   . GLU A 1 1039 ? 196.159 182.444 136.476 1.00 101.01 ? 1039 GLU A OE1   1 
ATOM   6850 O OE2   . GLU A 1 1039 ? 196.498 182.259 134.315 1.00 98.49  ? 1039 GLU A OE2   1 
ATOM   6851 N N     . ILE A 1 1040 ? 192.163 178.829 138.715 1.00 81.20  ? 1040 ILE A N     1 
ATOM   6852 C CA    . ILE A 1 1040 ? 191.913 178.498 140.111 1.00 79.62  ? 1040 ILE A CA    1 
ATOM   6853 C C     . ILE A 1 1040 ? 190.716 177.563 140.180 1.00 73.54  ? 1040 ILE A C     1 
ATOM   6854 O O     . ILE A 1 1040 ? 189.674 177.835 139.574 1.00 74.26  ? 1040 ILE A O     1 
ATOM   6855 C CB    . ILE A 1 1040 ? 191.663 179.761 140.957 1.00 76.53  ? 1040 ILE A CB    1 
ATOM   6856 C CG1   . ILE A 1 1040 ? 192.917 180.636 140.994 1.00 77.46  ? 1040 ILE A CG1   1 
ATOM   6857 C CG2   . ILE A 1 1040 ? 191.220 179.392 142.363 1.00 70.10  ? 1040 ILE A CG2   1 
ATOM   6858 C CD1   . ILE A 1 1040 ? 194.135 179.935 141.551 1.00 78.01  ? 1040 ILE A CD1   1 
ATOM   6859 N N     . THR A 1 1041 ? 190.865 176.462 140.910 1.00 71.17  ? 1041 THR A N     1 
ATOM   6860 C CA    . THR A 1 1041 ? 189.740 175.575 141.191 1.00 67.06  ? 1041 THR A CA    1 
ATOM   6861 C C     . THR A 1 1041 ? 188.979 176.164 142.369 1.00 62.76  ? 1041 THR A C     1 
ATOM   6862 O O     . THR A 1 1041 ? 189.367 175.991 143.527 1.00 64.50  ? 1041 THR A O     1 
ATOM   6863 C CB    . THR A 1 1041 ? 190.220 174.159 141.485 1.00 72.38  ? 1041 THR A CB    1 
ATOM   6864 O OG1   . THR A 1 1041 ? 191.035 173.696 140.402 1.00 75.13  ? 1041 THR A OG1   1 
ATOM   6865 C CG2   . THR A 1 1041 ? 189.032 173.225 141.649 1.00 68.06  ? 1041 THR A CG2   1 
ATOM   6866 N N     . THR A 1 1042 ? 187.891 176.870 142.073 1.00 60.30  ? 1042 THR A N     1 
ATOM   6867 C CA    . THR A 1 1042 ? 187.156 177.598 143.092 1.00 57.65  ? 1042 THR A CA    1 
ATOM   6868 C C     . THR A 1 1042 ? 186.457 176.634 144.047 1.00 53.87  ? 1042 THR A C     1 
ATOM   6869 O O     . THR A 1 1042 ? 186.375 175.425 143.813 1.00 53.50  ? 1042 THR A O     1 
ATOM   6870 C CB    . THR A 1 1042 ? 186.135 178.534 142.449 1.00 50.08  ? 1042 THR A CB    1 
ATOM   6871 O OG1   . THR A 1 1042 ? 185.099 177.762 141.832 1.00 58.06  ? 1042 THR A OG1   1 
ATOM   6872 C CG2   . THR A 1 1042 ? 186.800 179.391 141.396 1.00 49.74  ? 1042 THR A CG2   1 
ATOM   6873 N N     . PHE A 1 1043 ? 185.952 177.193 145.148 1.00 51.35  ? 1043 PHE A N     1 
ATOM   6874 C CA    . PHE A 1 1043 ? 185.206 176.388 146.108 1.00 51.20  ? 1043 PHE A CA    1 
ATOM   6875 C C     . PHE A 1 1043 ? 183.956 175.794 145.474 1.00 53.76  ? 1043 PHE A C     1 
ATOM   6876 O O     . PHE A 1 1043 ? 183.587 174.653 145.767 1.00 54.85  ? 1043 PHE A O     1 
ATOM   6877 C CB    . PHE A 1 1043 ? 184.837 177.229 147.330 1.00 50.06  ? 1043 PHE A CB    1 
ATOM   6878 C CG    . PHE A 1 1043 ? 183.831 176.573 148.233 1.00 50.78  ? 1043 PHE A CG    1 
ATOM   6879 C CD1   . PHE A 1 1043 ? 184.229 175.631 149.165 1.00 48.21  ? 1043 PHE A CD1   1 
ATOM   6880 C CD2   . PHE A 1 1043 ? 182.488 176.898 148.149 1.00 46.77  ? 1043 PHE A CD2   1 
ATOM   6881 C CE1   . PHE A 1 1043 ? 183.305 175.025 149.995 1.00 49.76  ? 1043 PHE A CE1   1 
ATOM   6882 C CE2   . PHE A 1 1043 ? 181.561 176.293 148.975 1.00 45.91  ? 1043 PHE A CE2   1 
ATOM   6883 C CZ    . PHE A 1 1043 ? 181.971 175.357 149.899 1.00 49.60  ? 1043 PHE A CZ    1 
ATOM   6884 N N     . GLU A 1 1044 ? 183.287 176.556 144.608 1.00 55.46  ? 1044 GLU A N     1 
ATOM   6885 C CA    . GLU A 1 1044 ? 182.036 176.082 144.028 1.00 51.45  ? 1044 GLU A CA    1 
ATOM   6886 C C     . GLU A 1 1044 ? 182.271 174.969 143.016 1.00 54.38  ? 1044 GLU A C     1 
ATOM   6887 O O     . GLU A 1 1044 ? 181.465 174.039 142.916 1.00 55.06  ? 1044 GLU A O     1 
ATOM   6888 C CB    . GLU A 1 1044 ? 181.279 177.245 143.393 1.00 43.07  ? 1044 GLU A CB    1 
ATOM   6889 C CG    . GLU A 1 1044 ? 180.704 178.201 144.415 1.00 45.82  ? 1044 GLU A CG    1 
ATOM   6890 C CD    . GLU A 1 1044 ? 179.781 179.227 143.805 1.00 46.98  ? 1044 GLU A CD    1 
ATOM   6891 O OE1   . GLU A 1 1044 ? 179.748 179.338 142.564 1.00 47.90  ? 1044 GLU A OE1   1 
ATOM   6892 O OE2   . GLU A 1 1044 ? 179.085 179.922 144.572 1.00 45.32  ? 1044 GLU A OE2   1 
ATOM   6893 N N     . GLU A 1 1045 ? 183.369 175.038 142.260 1.00 52.40  ? 1045 GLU A N     1 
ATOM   6894 C CA    . GLU A 1 1045 ? 183.686 173.966 141.320 1.00 51.78  ? 1045 GLU A CA    1 
ATOM   6895 C C     . GLU A 1 1045 ? 183.981 172.662 142.053 1.00 55.04  ? 1045 GLU A C     1 
ATOM   6896 O O     . GLU A 1 1045 ? 183.466 171.595 141.687 1.00 56.60  ? 1045 GLU A O     1 
ATOM   6897 C CB    . GLU A 1 1045 ? 184.869 174.384 140.447 1.00 55.13  ? 1045 GLU A CB    1 
ATOM   6898 C CG    . GLU A 1 1045 ? 185.247 173.386 139.371 1.00 65.24  ? 1045 GLU A CG    1 
ATOM   6899 C CD    . GLU A 1 1045 ? 186.270 173.946 138.404 1.00 70.55  ? 1045 GLU A CD    1 
ATOM   6900 O OE1   . GLU A 1 1045 ? 186.705 175.099 138.603 1.00 71.11  ? 1045 GLU A OE1   1 
ATOM   6901 O OE2   . GLU A 1 1045 ? 186.636 173.237 137.444 1.00 69.64  ? 1045 GLU A OE2   1 
ATOM   6902 N N     . THR A 1 1046 ? 184.803 172.734 143.103 1.00 53.74  ? 1046 THR A N     1 
ATOM   6903 C CA    . THR A 1 1046 ? 185.089 171.553 143.910 1.00 49.87  ? 1046 THR A CA    1 
ATOM   6904 C C     . THR A 1 1046 ? 183.827 171.028 144.576 1.00 48.62  ? 1046 THR A C     1 
ATOM   6905 O O     . THR A 1 1046 ? 183.613 169.814 144.646 1.00 53.69  ? 1046 THR A O     1 
ATOM   6906 C CB    . THR A 1 1046 ? 186.152 171.881 144.959 1.00 57.12  ? 1046 THR A CB    1 
ATOM   6907 O OG1   . THR A 1 1046 ? 187.353 172.309 144.307 1.00 60.73  ? 1046 THR A OG1   1 
ATOM   6908 C CG2   . THR A 1 1046 ? 186.456 170.663 145.813 1.00 57.36  ? 1046 THR A CG2   1 
ATOM   6909 N N     . LEU A 1 1047 ? 182.980 171.929 145.075 1.00 48.12  ? 1047 LEU A N     1 
ATOM   6910 C CA    . LEU A 1 1047 ? 181.730 171.511 145.699 1.00 46.62  ? 1047 LEU A CA    1 
ATOM   6911 C C     . LEU A 1 1047 ? 180.822 170.810 144.699 1.00 49.54  ? 1047 LEU A C     1 
ATOM   6912 O O     . LEU A 1 1047 ? 180.200 169.795 145.024 1.00 49.28  ? 1047 LEU A O     1 
ATOM   6913 C CB    . LEU A 1 1047 ? 181.027 172.721 146.314 1.00 47.36  ? 1047 LEU A CB    1 
ATOM   6914 C CG    . LEU A 1 1047 ? 179.657 172.490 146.954 1.00 49.66  ? 1047 LEU A CG    1 
ATOM   6915 C CD1   . LEU A 1 1047 ? 179.761 171.537 148.130 1.00 47.74  ? 1047 LEU A CD1   1 
ATOM   6916 C CD2   . LEU A 1 1047 ? 179.044 173.810 147.385 1.00 44.45  ? 1047 LEU A CD2   1 
ATOM   6917 N N     . ASP A 1 1048 ? 180.737 171.332 143.474 1.00 50.38  ? 1048 ASP A N     1 
ATOM   6918 C CA    . ASP A 1 1048 ? 179.915 170.700 142.447 1.00 45.26  ? 1048 ASP A CA    1 
ATOM   6919 C C     . ASP A 1 1048 ? 180.436 169.310 142.109 1.00 54.46  ? 1048 ASP A C     1 
ATOM   6920 O O     . ASP A 1 1048 ? 179.660 168.354 141.999 1.00 55.37  ? 1048 ASP A O     1 
ATOM   6921 C CB    . ASP A 1 1048 ? 179.874 171.580 141.198 1.00 52.47  ? 1048 ASP A CB    1 
ATOM   6922 C CG    . ASP A 1 1048 ? 179.003 170.998 140.101 1.00 62.10  ? 1048 ASP A CG    1 
ATOM   6923 O OD1   . ASP A 1 1048 ? 177.765 170.990 140.263 1.00 65.06  ? 1048 ASP A OD1   1 
ATOM   6924 O OD2   . ASP A 1 1048 ? 179.556 170.553 139.074 1.00 60.73  ? 1048 ASP A OD2   1 
ATOM   6925 N N     . ASP A 1 1049 ? 181.757 169.177 141.947 1.00 58.22  ? 1049 ASP A N     1 
ATOM   6926 C CA    . ASP A 1 1049 ? 182.327 167.865 141.647 1.00 53.88  ? 1049 ASP A CA    1 
ATOM   6927 C C     . ASP A 1 1049 ? 182.087 166.880 142.788 1.00 55.68  ? 1049 ASP A C     1 
ATOM   6928 O O     . ASP A 1 1049 ? 181.689 165.729 142.556 1.00 57.88  ? 1049 ASP A O     1 
ATOM   6929 C CB    . ASP A 1 1049 ? 183.822 167.996 141.360 1.00 52.63  ? 1049 ASP A CB    1 
ATOM   6930 C CG    . ASP A 1 1049 ? 184.111 168.883 140.166 1.00 62.94  ? 1049 ASP A CG    1 
ATOM   6931 O OD1   . ASP A 1 1049 ? 183.155 169.461 139.608 1.00 65.54  ? 1049 ASP A OD1   1 
ATOM   6932 O OD2   . ASP A 1 1049 ? 185.293 169.000 139.783 1.00 66.89  ? 1049 ASP A OD2   1 
ATOM   6933 N N     . LEU A 1 1050 ? 182.316 167.320 144.027 1.00 54.70  ? 1050 LEU A N     1 
ATOM   6934 C CA    . LEU A 1 1050 ? 182.105 166.457 145.184 1.00 47.51  ? 1050 LEU A CA    1 
ATOM   6935 C C     . LEU A 1 1050 ? 180.648 166.037 145.299 1.00 47.05  ? 1050 LEU A C     1 
ATOM   6936 O O     . LEU A 1 1050 ? 180.354 164.877 145.600 1.00 53.60  ? 1050 LEU A O     1 
ATOM   6937 C CB    . LEU A 1 1050 ? 182.553 167.170 146.460 1.00 48.37  ? 1050 LEU A CB    1 
ATOM   6938 C CG    . LEU A 1 1050 ? 183.985 166.992 146.970 1.00 51.05  ? 1050 LEU A CG    1 
ATOM   6939 C CD1   . LEU A 1 1050 ? 185.013 167.226 145.877 1.00 55.49  ? 1050 LEU A CD1   1 
ATOM   6940 C CD2   . LEU A 1 1050 ? 184.230 167.934 148.133 1.00 53.62  ? 1050 LEU A CD2   1 
ATOM   6941 N N     . LEU A 1 1051 ? 179.721 166.968 145.070 1.00 45.69  ? 1051 LEU A N     1 
ATOM   6942 C CA    . LEU A 1 1051 ? 178.305 166.640 145.174 1.00 46.35  ? 1051 LEU A CA    1 
ATOM   6943 C C     . LEU A 1 1051 ? 177.869 165.704 144.056 1.00 48.88  ? 1051 LEU A C     1 
ATOM   6944 O O     . LEU A 1 1051 ? 177.033 164.824 144.275 1.00 51.84  ? 1051 LEU A O     1 
ATOM   6945 C CB    . LEU A 1 1051 ? 177.471 167.919 145.175 1.00 47.53  ? 1051 LEU A CB    1 
ATOM   6946 C CG    . LEU A 1 1051 ? 177.581 168.748 146.455 1.00 43.89  ? 1051 LEU A CG    1 
ATOM   6947 C CD1   . LEU A 1 1051 ? 176.888 170.086 146.297 1.00 46.90  ? 1051 LEU A CD1   1 
ATOM   6948 C CD2   . LEU A 1 1051 ? 177.008 167.985 147.635 1.00 48.88  ? 1051 LEU A CD2   1 
ATOM   6949 N N     . GLN A 1 1052 ? 178.428 165.866 142.854 1.00 51.05  ? 1052 GLN A N     1 
ATOM   6950 C CA    . GLN A 1 1052 ? 178.134 164.925 141.778 1.00 54.97  ? 1052 GLN A CA    1 
ATOM   6951 C C     . GLN A 1 1052 ? 178.609 163.522 142.134 1.00 56.39  ? 1052 GLN A C     1 
ATOM   6952 O O     . GLN A 1 1052 ? 177.873 162.541 141.964 1.00 57.62  ? 1052 GLN A O     1 
ATOM   6953 C CB    . GLN A 1 1052 ? 178.778 165.394 140.473 1.00 58.51  ? 1052 GLN A CB    1 
ATOM   6954 C CG    . GLN A 1 1052 ? 178.088 166.578 139.822 1.00 64.66  ? 1052 GLN A CG    1 
ATOM   6955 C CD    . GLN A 1 1052 ? 178.738 166.979 138.513 1.00 69.55  ? 1052 GLN A CD    1 
ATOM   6956 O OE1   . GLN A 1 1052 ? 179.830 166.516 138.182 1.00 65.21  ? 1052 GLN A OE1   1 
ATOM   6957 N NE2   . GLN A 1 1052 ? 178.068 167.842 137.760 1.00 68.16  ? 1052 GLN A NE2   1 
ATOM   6958 N N     . ARG A 1 1053 ? 179.840 163.407 142.643 1.00 55.58  ? 1053 ARG A N     1 
ATOM   6959 C CA    . ARG A 1 1053 ? 180.350 162.094 143.028 1.00 49.68  ? 1053 ARG A CA    1 
ATOM   6960 C C     . ARG A 1 1053 ? 179.525 161.490 144.159 1.00 50.72  ? 1053 ARG A C     1 
ATOM   6961 O O     . ARG A 1 1053 ? 179.200 160.296 144.135 1.00 58.91  ? 1053 ARG A O     1 
ATOM   6962 C CB    . ARG A 1 1053 ? 181.820 162.190 143.436 1.00 53.95  ? 1053 ARG A CB    1 
ATOM   6963 C CG    . ARG A 1 1053 ? 182.736 162.743 142.362 1.00 55.88  ? 1053 ARG A CG    1 
ATOM   6964 C CD    . ARG A 1 1053 ? 184.188 162.430 142.673 1.00 65.87  ? 1053 ARG A CD    1 
ATOM   6965 N NE    . ARG A 1 1053 ? 185.091 163.451 142.156 1.00 77.14  ? 1053 ARG A NE    1 
ATOM   6966 C CZ    . ARG A 1 1053 ? 185.690 164.366 142.905 1.00 75.04  ? 1053 ARG A CZ    1 
ATOM   6967 N NH1   . ARG A 1 1053 ? 185.525 164.401 144.217 1.00 68.15  ? 1053 ARG A NH1   1 
ATOM   6968 N NH2   . ARG A 1 1053 ? 186.479 165.265 142.324 1.00 69.97  ? 1053 ARG A NH2   1 
ATOM   6969 N N     . ARG A 1 1054 ? 179.173 162.303 145.157 1.00 49.86  ? 1054 ARG A N     1 
ATOM   6970 C CA    . ARG A 1 1054 ? 178.402 161.802 146.288 1.00 49.07  ? 1054 ARG A CA    1 
ATOM   6971 C C     . ARG A 1 1054 ? 177.001 161.384 145.865 1.00 53.11  ? 1054 ARG A C     1 
ATOM   6972 O O     . ARG A 1 1054 ? 176.473 160.390 146.369 1.00 57.17  ? 1054 ARG A O     1 
ATOM   6973 C CB    . ARG A 1 1054 ? 178.341 162.854 147.393 1.00 53.54  ? 1054 ARG A CB    1 
ATOM   6974 C CG    . ARG A 1 1054 ? 179.655 163.067 148.122 1.00 57.95  ? 1054 ARG A CG    1 
ATOM   6975 C CD    . ARG A 1 1054 ? 180.182 161.764 148.696 1.00 62.11  ? 1054 ARG A CD    1 
ATOM   6976 N NE    . ARG A 1 1054 ? 181.367 161.975 149.517 1.00 64.61  ? 1054 ARG A NE    1 
ATOM   6977 C CZ    . ARG A 1 1054 ? 181.341 162.180 150.827 1.00 66.67  ? 1054 ARG A CZ    1 
ATOM   6978 N NH1   . ARG A 1 1054 ? 180.203 162.198 151.501 1.00 65.45  ? 1054 ARG A NH1   1 
ATOM   6979 N NH2   . ARG A 1 1054 ? 182.485 162.371 151.476 1.00 68.39  ? 1054 ARG A NH2   1 
ATOM   6980 N N     . ARG A 1 1055 ? 176.379 162.124 144.945 1.00 53.31  ? 1055 ARG A N     1 
ATOM   6981 C CA    . ARG A 1 1055 ? 175.071 161.724 144.438 1.00 55.62  ? 1055 ARG A CA    1 
ATOM   6982 C C     . ARG A 1 1055 ? 175.161 160.426 143.645 1.00 61.36  ? 1055 ARG A C     1 
ATOM   6983 O O     . ARG A 1 1055 ? 174.299 159.547 143.780 1.00 64.90  ? 1055 ARG A O     1 
ATOM   6984 C CB    . ARG A 1 1055 ? 174.475 162.840 143.580 1.00 55.29  ? 1055 ARG A CB    1 
ATOM   6985 C CG    . ARG A 1 1055 ? 173.170 162.460 142.901 1.00 60.64  ? 1055 ARG A CG    1 
ATOM   6986 C CD    . ARG A 1 1055 ? 172.566 163.622 142.131 1.00 59.00  ? 1055 ARG A CD    1 
ATOM   6987 N NE    . ARG A 1 1055 ? 171.956 164.613 143.010 1.00 60.90  ? 1055 ARG A NE    1 
ATOM   6988 C CZ    . ARG A 1 1055 ? 172.492 165.789 143.303 1.00 61.13  ? 1055 ARG A CZ    1 
ATOM   6989 N NH1   . ARG A 1 1055 ? 173.654 166.165 142.796 1.00 57.61  ? 1055 ARG A NH1   1 
ATOM   6990 N NH2   . ARG A 1 1055 ? 171.842 166.612 144.121 1.00 53.04  ? 1055 ARG A NH2   1 
ATOM   6991 N N     . ALA A 1 1056 ? 176.204 160.285 142.821 1.00 58.74  ? 1056 ALA A N     1 
ATOM   6992 C CA    . ALA A 1 1056 ? 176.386 159.044 142.075 1.00 58.19  ? 1056 ALA A CA    1 
ATOM   6993 C C     . ALA A 1 1056 ? 176.551 157.861 143.019 1.00 62.60  ? 1056 ALA A C     1 
ATOM   6994 O O     . ALA A 1 1056 ? 175.993 156.784 142.781 1.00 64.66  ? 1056 ALA A O     1 
ATOM   6995 C CB    . ALA A 1 1056 ? 177.591 159.163 141.143 1.00 49.18  ? 1056 ALA A CB    1 
ATOM   6996 N N     . LEU A 1 1057 ? 177.315 158.044 144.097 1.00 59.70  ? 1057 LEU A N     1 
ATOM   6997 C CA    . LEU A 1 1057 ? 177.424 156.995 145.107 1.00 60.14  ? 1057 LEU A CA    1 
ATOM   6998 C C     . LEU A 1 1057 ? 176.087 156.746 145.797 1.00 62.85  ? 1057 LEU A C     1 
ATOM   6999 O O     . LEU A 1 1057 ? 175.725 155.596 146.067 1.00 66.91  ? 1057 LEU A O     1 
ATOM   7000 C CB    . LEU A 1 1057 ? 178.497 157.362 146.132 1.00 59.91  ? 1057 LEU A CB    1 
ATOM   7001 C CG    . LEU A 1 1057 ? 179.926 157.482 145.600 1.00 64.10  ? 1057 LEU A CG    1 
ATOM   7002 C CD1   . LEU A 1 1057 ? 180.883 157.862 146.718 1.00 62.09  ? 1057 LEU A CD1   1 
ATOM   7003 C CD2   . LEU A 1 1057 ? 180.360 156.187 144.934 1.00 64.14  ? 1057 LEU A CD2   1 
ATOM   7004 N N     . ALA A 1 1058 ? 175.339 157.814 146.086 1.00 61.22  ? 1058 ALA A N     1 
ATOM   7005 C CA    . ALA A 1 1058 ? 174.069 157.699 146.790 1.00 61.72  ? 1058 ALA A CA    1 
ATOM   7006 C C     . ALA A 1 1058 ? 172.992 157.035 145.948 1.00 64.88  ? 1058 ALA A C     1 
ATOM   7007 O O     . ALA A 1 1058 ? 171.969 156.613 146.498 1.00 65.14  ? 1058 ALA A O     1 
ATOM   7008 C CB    . ALA A 1 1058 ? 173.593 159.081 147.237 1.00 56.76  ? 1058 ALA A CB    1 
ATOM   7009 N N     . ARG A 1 1059 ? 173.183 156.949 144.629 1.00 65.49  ? 1059 ARG A N     1 
ATOM   7010 C CA    . ARG A 1 1059 ? 172.265 156.156 143.818 1.00 68.09  ? 1059 ARG A CA    1 
ATOM   7011 C C     . ARG A 1 1059 ? 172.211 154.713 144.302 1.00 67.75  ? 1059 ARG A C     1 
ATOM   7012 O O     . ARG A 1 1059 ? 171.152 154.077 144.244 1.00 70.22  ? 1059 ARG A O     1 
ATOM   7013 C CB    . ARG A 1 1059 ? 172.672 156.207 142.344 1.00 72.49  ? 1059 ARG A CB    1 
ATOM   7014 C CG    . ARG A 1 1059 ? 172.812 157.613 141.788 1.00 72.18  ? 1059 ARG A CG    1 
ATOM   7015 C CD    . ARG A 1 1059 ? 172.966 157.611 140.276 1.00 71.64  ? 1059 ARG A CD    1 
ATOM   7016 N NE    . ARG A 1 1059 ? 173.586 158.840 139.796 1.00 78.47  ? 1059 ARG A NE    1 
ATOM   7017 C CZ    . ARG A 1 1059 ? 172.952 159.996 139.646 1.00 75.12  ? 1059 ARG A CZ    1 
ATOM   7018 N NH1   . ARG A 1 1059 ? 171.667 160.122 139.933 1.00 70.41  ? 1059 ARG A NH1   1 
ATOM   7019 N NH2   . ARG A 1 1059 ? 173.627 161.053 139.202 1.00 68.61  ? 1059 ARG A NH2   1 
ATOM   7020 N N     . ASP A 1 1060 ? 173.333 154.186 144.787 1.00 65.75  ? 1060 ASP A N     1 
ATOM   7021 C CA    . ASP A 1 1060 ? 173.364 152.846 145.357 1.00 63.67  ? 1060 ASP A CA    1 
ATOM   7022 C C     . ASP A 1 1060 ? 172.590 152.812 146.670 1.00 65.20  ? 1060 ASP A C     1 
ATOM   7023 O O     . ASP A 1 1060 ? 172.711 153.718 147.499 1.00 67.53  ? 1060 ASP A O     1 
ATOM   7024 C CB    . ASP A 1 1060 ? 174.810 152.405 145.580 1.00 61.44  ? 1060 ASP A CB    1 
ATOM   7025 C CG    . ASP A 1 1060 ? 174.927 150.944 145.964 1.00 63.80  ? 1060 ASP A CG    1 
ATOM   7026 O OD1   . ASP A 1 1060 ? 173.898 150.235 145.950 1.00 64.41  ? 1060 ASP A OD1   1 
ATOM   7027 O OD2   . ASP A 1 1060 ? 176.052 150.502 146.280 1.00 59.41  ? 1060 ASP A OD2   1 
ATOM   7028 N N     . MET A 1 1061 ? 171.793 151.758 146.857 1.00 62.06  ? 1061 MET A N     1 
ATOM   7029 C CA    . MET A 1 1061 ? 170.994 151.640 148.072 1.00 59.59  ? 1061 MET A CA    1 
ATOM   7030 C C     . MET A 1 1061 ? 171.839 151.236 149.273 1.00 63.86  ? 1061 MET A C     1 
ATOM   7031 O O     . MET A 1 1061 ? 171.538 151.636 150.403 1.00 63.44  ? 1061 MET A O     1 
ATOM   7032 C CB    . MET A 1 1061 ? 169.867 150.629 147.863 1.00 57.71  ? 1061 MET A CB    1 
ATOM   7033 C CG    . MET A 1 1061 ? 168.762 150.711 148.897 1.00 58.27  ? 1061 MET A CG    1 
ATOM   7034 S SD    . MET A 1 1061 ? 167.686 149.267 148.873 1.00 68.92  ? 1061 MET A SD    1 
ATOM   7035 C CE    . MET A 1 1061 ? 168.713 148.073 149.718 1.00 56.67  ? 1061 MET A CE    1 
ATOM   7036 N N     . LEU A 1 1062 ? 172.893 150.449 149.054 1.00 63.39  ? 1062 LEU A N     1 
ATOM   7037 C CA    . LEU A 1 1062 ? 173.710 149.900 150.127 1.00 56.17  ? 1062 LEU A CA    1 
ATOM   7038 C C     . LEU A 1 1062 ? 174.884 150.799 150.490 1.00 57.08  ? 1062 LEU A C     1 
ATOM   7039 O O     . LEU A 1 1062 ? 175.793 150.360 151.201 1.00 59.18  ? 1062 LEU A O     1 
ATOM   7040 C CB    . LEU A 1 1062 ? 174.219 148.511 149.742 1.00 55.95  ? 1062 LEU A CB    1 
ATOM   7041 C CG    . LEU A 1 1062 ? 173.152 147.459 149.439 1.00 53.94  ? 1062 LEU A CG    1 
ATOM   7042 C CD1   . LEU A 1 1062 ? 173.790 146.116 149.128 1.00 54.74  ? 1062 LEU A CD1   1 
ATOM   7043 C CD2   . LEU A 1 1062 ? 172.193 147.342 150.603 1.00 54.03  ? 1062 LEU A CD2   1 
ATOM   7044 N N     . CYS A 1 1063 ? 174.886 152.043 150.023 1.00 61.05  ? 1063 CYS A N     1 
ATOM   7045 C CA    . CYS A 1 1063 ? 175.988 152.965 150.256 1.00 67.27  ? 1063 CYS A CA    1 
ATOM   7046 C C     . CYS A 1 1063 ? 175.521 154.111 151.142 1.00 67.51  ? 1063 CYS A C     1 
ATOM   7047 O O     . CYS A 1 1063 ? 174.492 154.736 150.866 1.00 65.61  ? 1063 CYS A O     1 
ATOM   7048 C CB    . CYS A 1 1063 ? 176.535 153.507 148.933 1.00 68.24  ? 1063 CYS A CB    1 
ATOM   7049 S SG    . CYS A 1 1063 ? 177.999 154.552 149.102 1.00 88.65  ? 1063 CYS A SG    1 
ATOM   7050 N N     . ALA A 1 1064 ? 176.277 154.379 152.204 1.00 65.73  ? 1064 ALA A N     1 
ATOM   7051 C CA    . ALA A 1 1064 ? 175.975 155.494 153.085 1.00 66.09  ? 1064 ALA A CA    1 
ATOM   7052 C C     . ALA A 1 1064 ? 176.326 156.817 152.409 1.00 74.22  ? 1064 ALA A C     1 
ATOM   7053 O O     . ALA A 1 1064 ? 177.182 156.887 151.523 1.00 75.28  ? 1064 ALA A O     1 
ATOM   7054 C CB    . ALA A 1 1064 ? 176.735 155.358 154.403 1.00 64.10  ? 1064 ALA A CB    1 
ATOM   7055 N N     . THR A 1 1065 ? 175.650 157.881 152.844 1.00 73.00  ? 1065 THR A N     1 
ATOM   7056 C CA    . THR A 1 1065 ? 175.790 159.209 152.247 1.00 76.06  ? 1065 THR A CA    1 
ATOM   7057 C C     . THR A 1 1065 ? 176.154 160.215 153.331 1.00 77.49  ? 1065 THR A C     1 
ATOM   7058 O O     . THR A 1 1065 ? 175.310 161.010 153.766 1.00 74.30  ? 1065 THR A O     1 
ATOM   7059 C CB    . THR A 1 1065 ? 174.506 159.637 151.534 1.00 73.09  ? 1065 THR A CB    1 
ATOM   7060 O OG1   . THR A 1 1065 ? 173.550 160.086 152.502 1.00 76.56  ? 1065 THR A OG1   1 
ATOM   7061 C CG2   . THR A 1 1065 ? 173.911 158.474 150.758 1.00 72.20  ? 1065 THR A CG2   1 
ATOM   7062 N N     . PRO A 1 1066 ? 177.402 160.210 153.792 1.00 75.06  ? 1066 PRO A N     1 
ATOM   7063 C CA    . PRO A 1 1066 ? 177.824 161.225 154.760 1.00 75.45  ? 1066 PRO A CA    1 
ATOM   7064 C C     . PRO A 1 1066 ? 177.946 162.593 154.108 1.00 75.95  ? 1066 PRO A C     1 
ATOM   7065 O O     . PRO A 1 1066 ? 178.194 162.717 152.906 1.00 72.84  ? 1066 PRO A O     1 
ATOM   7066 C CB    . PRO A 1 1066 ? 179.187 160.713 155.236 1.00 74.03  ? 1066 PRO A CB    1 
ATOM   7067 C CG    . PRO A 1 1066 ? 179.706 159.939 154.076 1.00 70.97  ? 1066 PRO A CG    1 
ATOM   7068 C CD    . PRO A 1 1066 ? 178.503 159.300 153.432 1.00 71.41  ? 1066 PRO A CD    1 
ATOM   7069 N N     . ASP A 1 1067 ? 177.763 163.628 154.921 1.00 72.60  ? 1067 ASP A N     1 
ATOM   7070 C CA    . ASP A 1 1067 ? 177.933 164.989 154.437 1.00 66.50  ? 1067 ASP A CA    1 
ATOM   7071 C C     . ASP A 1 1067 ? 179.406 165.280 154.176 1.00 68.61  ? 1067 ASP A C     1 
ATOM   7072 O O     . ASP A 1 1067 ? 180.300 164.664 154.764 1.00 71.60  ? 1067 ASP A O     1 
ATOM   7073 C CB    . ASP A 1 1067 ? 177.373 165.993 155.444 1.00 68.11  ? 1067 ASP A CB    1 
ATOM   7074 C CG    . ASP A 1 1067 ? 175.885 165.825 155.668 1.00 73.06  ? 1067 ASP A CG    1 
ATOM   7075 O OD1   . ASP A 1 1067 ? 175.307 164.862 155.124 1.00 77.16  ? 1067 ASP A OD1   1 
ATOM   7076 O OD2   . ASP A 1 1067 ? 175.293 166.658 156.385 1.00 66.87  ? 1067 ASP A OD2   1 
ATOM   7077 N N     . LEU A 1 1068 ? 179.653 166.226 153.276 1.00 61.16  ? 1068 LEU A N     1 
ATOM   7078 C CA    . LEU A 1 1068 ? 181.014 166.655 153.000 1.00 60.42  ? 1068 LEU A CA    1 
ATOM   7079 C C     . LEU A 1 1068 ? 181.613 167.339 154.224 1.00 65.01  ? 1068 LEU A C     1 
ATOM   7080 O O     . LEU A 1 1068 ? 180.911 167.977 155.013 1.00 68.79  ? 1068 LEU A O     1 
ATOM   7081 C CB    . LEU A 1 1068 ? 181.043 167.605 151.804 1.00 59.95  ? 1068 LEU A CB    1 
ATOM   7082 C CG    . LEU A 1 1068 ? 180.488 167.063 150.487 1.00 51.63  ? 1068 LEU A CG    1 
ATOM   7083 C CD1   . LEU A 1 1068 ? 180.531 168.136 149.414 1.00 47.42  ? 1068 LEU A CD1   1 
ATOM   7084 C CD2   . LEU A 1 1068 ? 181.262 165.834 150.050 1.00 55.62  ? 1068 LEU A CD2   1 
ATOM   7085 N N     . ASN A 1 1069 ? 182.921 167.192 154.382 1.00 66.79  ? 1069 ASN A N     1 
ATOM   7086 C CA    . ASN A 1 1069 ? 183.658 167.804 155.479 1.00 66.86  ? 1069 ASN A CA    1 
ATOM   7087 C C     . ASN A 1 1069 ? 184.822 168.617 154.922 1.00 67.84  ? 1069 ASN A C     1 
ATOM   7088 O O     . ASN A 1 1069 ? 185.062 168.655 153.714 1.00 67.47  ? 1069 ASN A O     1 
ATOM   7089 C CB    . ASN A 1 1069 ? 184.141 166.742 156.473 1.00 71.76  ? 1069 ASN A CB    1 
ATOM   7090 C CG    . ASN A 1 1069 ? 184.843 165.579 155.796 1.00 77.30  ? 1069 ASN A CG    1 
ATOM   7091 O OD1   . ASN A 1 1069 ? 185.514 165.745 154.778 1.00 73.76  ? 1069 ASN A OD1   1 
ATOM   7092 N ND2   . ASN A 1 1069 ? 184.686 164.389 156.363 1.00 79.59  ? 1069 ASN A ND2   1 
ATOM   7093 N N     . CYS A 1 1070 ? 185.548 169.277 155.827 1.00 70.35  ? 1070 CYS A N     1 
ATOM   7094 C CA    . CYS A 1 1070 ? 186.687 170.090 155.410 1.00 73.48  ? 1070 CYS A CA    1 
ATOM   7095 C C     . CYS A 1 1070 ? 187.774 169.244 154.760 1.00 74.90  ? 1070 CYS A C     1 
ATOM   7096 O O     . CYS A 1 1070 ? 188.542 169.750 153.934 1.00 74.49  ? 1070 CYS A O     1 
ATOM   7097 C CB    . CYS A 1 1070 ? 187.251 170.852 156.609 1.00 78.26  ? 1070 CYS A CB    1 
ATOM   7098 S SG    . CYS A 1 1070 ? 187.861 169.800 157.946 1.00 95.03  ? 1070 CYS A SG    1 
ATOM   7099 N N     . ALA A 1 1071 ? 187.858 167.961 155.119 1.00 75.36  ? 1071 ALA A N     1 
ATOM   7100 C CA    . ALA A 1 1071 ? 188.851 167.085 154.509 1.00 77.46  ? 1071 ALA A CA    1 
ATOM   7101 C C     . ALA A 1 1071 ? 188.522 166.787 153.052 1.00 76.45  ? 1071 ALA A C     1 
ATOM   7102 O O     . ALA A 1 1071 ? 189.430 166.537 152.252 1.00 73.67  ? 1071 ALA A O     1 
ATOM   7103 C CB    . ALA A 1 1071 ? 188.963 165.784 155.304 1.00 81.13  ? 1071 ALA A CB    1 
ATOM   7104 N N     . ASP A 1 1072 ? 187.237 166.803 152.690 1.00 74.04  ? 1072 ASP A N     1 
ATOM   7105 C CA    . ASP A 1 1072 ? 186.851 166.574 151.303 1.00 66.07  ? 1072 ASP A CA    1 
ATOM   7106 C C     . ASP A 1 1072 ? 187.219 167.742 150.400 1.00 64.94  ? 1072 ASP A C     1 
ATOM   7107 O O     . ASP A 1 1072 ? 187.307 167.562 149.181 1.00 64.68  ? 1072 ASP A O     1 
ATOM   7108 C CB    . ASP A 1 1072 ? 185.349 166.302 151.211 1.00 62.94  ? 1072 ASP A CB    1 
ATOM   7109 C CG    . ASP A 1 1072 ? 184.963 164.958 151.792 1.00 71.85  ? 1072 ASP A CG    1 
ATOM   7110 O OD1   . ASP A 1 1072 ? 185.752 164.001 151.652 1.00 76.93  ? 1072 ASP A OD1   1 
ATOM   7111 O OD2   . ASP A 1 1072 ? 183.872 164.859 152.391 1.00 70.83  ? 1072 ASP A OD2   1 
ATOM   7112 N N     . PHE A 1 1073 ? 187.442 168.927 150.966 1.00 66.18  ? 1073 PHE A N     1 
ATOM   7113 C CA    . PHE A 1 1073 ? 187.803 170.112 150.200 1.00 64.37  ? 1073 PHE A CA    1 
ATOM   7114 C C     . PHE A 1 1073 ? 189.290 170.425 150.279 1.00 73.52  ? 1073 PHE A C     1 
ATOM   7115 O O     . PHE A 1 1073 ? 189.686 171.574 150.057 1.00 81.79  ? 1073 PHE A O     1 
ATOM   7116 C CB    . PHE A 1 1073 ? 186.996 171.320 150.675 1.00 62.01  ? 1073 PHE A CB    1 
ATOM   7117 C CG    . PHE A 1 1073 ? 185.523 171.205 150.422 1.00 55.46  ? 1073 PHE A CG    1 
ATOM   7118 C CD1   . PHE A 1 1073 ? 184.977 171.651 149.232 1.00 54.01  ? 1073 PHE A CD1   1 
ATOM   7119 C CD2   . PHE A 1 1073 ? 184.685 170.660 151.375 1.00 55.61  ? 1073 PHE A CD2   1 
ATOM   7120 C CE1   . PHE A 1 1073 ? 183.622 171.549 148.998 1.00 52.54  ? 1073 PHE A CE1   1 
ATOM   7121 C CE2   . PHE A 1 1073 ? 183.332 170.556 151.147 1.00 55.23  ? 1073 PHE A CE2   1 
ATOM   7122 C CZ    . PHE A 1 1073 ? 182.799 171.001 149.957 1.00 55.03  ? 1073 PHE A CZ    1 
ATOM   7123 N N     . GLU A 1 1074 ? 190.124 169.433 150.590 1.00 73.86  ? 1074 GLU A N     1 
ATOM   7124 C CA    . GLU A 1 1074 ? 191.556 169.680 150.709 1.00 77.35  ? 1074 GLU A CA    1 
ATOM   7125 C C     . GLU A 1 1074 ? 192.223 169.674 149.341 1.00 82.35  ? 1074 GLU A C     1 
ATOM   7126 O O     . GLU A 1 1074 ? 193.226 168.985 149.128 1.00 87.50  ? 1074 GLU A O     1 
ATOM   7127 C CB    . GLU A 1 1074 ? 192.206 168.647 151.631 1.00 76.65  ? 1074 GLU A CB    1 
ATOM   7128 C CG    . GLU A 1 1074 ? 191.827 168.806 153.093 1.00 83.36  ? 1074 GLU A CG    1 
ATOM   7129 C CD    . GLU A 1 1074 ? 192.549 167.827 153.995 1.00 91.27  ? 1074 GLU A CD    1 
ATOM   7130 O OE1   . GLU A 1 1074 ? 193.188 166.891 153.468 1.00 91.84  ? 1074 GLU A OE1   1 
ATOM   7131 O OE2   . GLU A 1 1074 ? 192.482 167.994 155.231 1.00 84.04  ? 1074 GLU A OE2   1 
ATOM   7132 N N     . THR A 1 1075 ? 191.664 170.444 148.410 1.00 79.67  ? 1075 THR A N     1 
ATOM   7133 C CA    . THR A 1 1075 ? 192.296 170.722 147.128 1.00 85.87  ? 1075 THR A CA    1 
ATOM   7134 C C     . THR A 1 1075 ? 192.379 172.206 146.813 1.00 87.56  ? 1075 THR A C     1 
ATOM   7135 O O     . THR A 1 1075 ? 193.159 172.586 145.932 1.00 88.11  ? 1075 THR A O     1 
ATOM   7136 C CB    . THR A 1 1075 ? 191.550 170.016 145.985 1.00 86.74  ? 1075 THR A CB    1 
ATOM   7137 O OG1   . THR A 1 1075 ? 190.188 170.457 145.954 1.00 81.80  ? 1075 THR A OG1   1 
ATOM   7138 C CG2   . THR A 1 1075 ? 191.587 168.506 146.171 1.00 80.44  ? 1075 THR A CG2   1 
ATOM   7139 N N     . ILE A 1 1076 ? 191.604 173.052 147.495 1.00 86.78  ? 1076 ILE A N     1 
ATOM   7140 C CA    . ILE A 1 1076 ? 191.721 174.494 147.312 1.00 90.69  ? 1076 ILE A CA    1 
ATOM   7141 C C     . ILE A 1 1076 ? 193.071 174.984 147.819 1.00 91.52  ? 1076 ILE A C     1 
ATOM   7142 O O     . ILE A 1 1076 ? 193.660 175.916 147.258 1.00 89.37  ? 1076 ILE A O     1 
ATOM   7143 C CB    . ILE A 1 1076 ? 190.553 175.213 148.010 1.00 89.22  ? 1076 ILE A CB    1 
ATOM   7144 C CG1   . ILE A 1 1076 ? 189.218 174.620 147.553 1.00 78.82  ? 1076 ILE A CG1   1 
ATOM   7145 C CG2   . ILE A 1 1076 ? 190.598 176.706 147.725 1.00 87.35  ? 1076 ILE A CG2   1 
ATOM   7146 C CD1   . ILE A 1 1076 ? 188.018 175.197 148.265 1.00 71.29  ? 1076 ILE A CD1   1 
ATOM   7147 N N     . LEU A 1 1077 ? 193.581 174.365 148.887 1.00 91.22  ? 1077 LEU A N     1 
ATOM   7148 C CA    . LEU A 1 1077 ? 194.899 174.719 149.399 1.00 95.76  ? 1077 LEU A CA    1 
ATOM   7149 C C     . LEU A 1 1077 ? 196.000 174.451 148.383 1.00 97.28  ? 1077 LEU A C     1 
ATOM   7150 O O     . LEU A 1 1077 ? 197.066 175.072 148.460 1.00 98.89  ? 1077 LEU A O     1 
ATOM   7151 C CB    . LEU A 1 1077 ? 195.182 173.951 150.691 1.00 91.40  ? 1077 LEU A CB    1 
ATOM   7152 C CG    . LEU A 1 1077 ? 194.116 174.070 151.782 1.00 93.37  ? 1077 LEU A CG    1 
ATOM   7153 C CD1   . LEU A 1 1077 ? 194.570 173.380 153.059 1.00 92.62  ? 1077 LEU A CD1   1 
ATOM   7154 C CD2   . LEU A 1 1077 ? 193.777 175.529 152.042 1.00 87.43  ? 1077 LEU A CD2   1 
ATOM   7155 N N     . LYS A 1 1078 ? 195.768 173.544 147.434 1.00 95.66  ? 1078 LYS A N     1 
ATOM   7156 C CA    . LYS A 1 1078 ? 196.711 173.306 146.351 1.00 94.57  ? 1078 LYS A CA    1 
ATOM   7157 C C     . LYS A 1 1078 ? 196.664 174.390 145.283 1.00 94.53  ? 1078 LYS A C     1 
ATOM   7158 O O     . LYS A 1 1078 ? 197.557 174.436 144.431 1.00 92.99  ? 1078 LYS A O     1 
ATOM   7159 C CB    . LYS A 1 1078 ? 196.436 171.946 145.705 1.00 93.39  ? 1078 LYS A CB    1 
ATOM   7160 C CG    . LYS A 1 1078 ? 196.317 170.797 146.692 1.00 93.31  ? 1078 LYS A CG    1 
ATOM   7161 C CD    . LYS A 1 1078 ? 195.901 169.514 145.989 1.00 92.55  ? 1078 LYS A CD    1 
ATOM   7162 C CE    . LYS A 1 1078 ? 195.717 168.376 146.978 1.00 91.69  ? 1078 LYS A CE    1 
ATOM   7163 N NZ    . LYS A 1 1078 ? 195.311 167.115 146.299 1.00 88.88  ? 1078 LYS A NZ    1 
ATOM   7164 N N     . GLY A 1 1079 ? 195.654 175.253 145.309 1.00 95.71  ? 1079 GLY A N     1 
ATOM   7165 C CA    . GLY A 1 1079 ? 195.497 176.289 144.307 1.00 96.74  ? 1079 GLY A CA    1 
ATOM   7166 C C     . GLY A 1 1079 ? 194.137 176.244 143.638 1.00 93.75  ? 1079 GLY A C     1 
ATOM   7167 O O     . GLY A 1 1079 ? 193.509 177.275 143.400 1.00 88.06  ? 1079 GLY A O     1 
HETATM 7168 P PG    . AGS B 2 .    ? 156.990 159.182 152.217 1.00 86.80  ? 1101 AGS A PG    1 
HETATM 7169 S S1G   . AGS B 2 .    ? 156.610 157.301 152.558 1.00 69.61  ? 1101 AGS A S1G   1 
HETATM 7170 O O2G   . AGS B 2 .    ? 157.947 159.725 153.318 1.00 73.13  ? 1101 AGS A O2G   1 
HETATM 7171 O O3G   . AGS B 2 .    ? 155.659 159.991 152.265 1.00 69.18  ? 1101 AGS A O3G   1 
HETATM 7172 P PB    . AGS B 2 .    ? 156.800 159.179 149.492 1.00 68.71  ? 1101 AGS A PB    1 
HETATM 7173 O O1B   . AGS B 2 .    ? 157.351 158.086 148.659 1.00 59.77  ? 1101 AGS A O1B   1 
HETATM 7174 O O2B   . AGS B 2 .    ? 155.364 158.913 149.949 1.00 62.38  ? 1101 AGS A O2B   1 
HETATM 7175 O O3B   . AGS B 2 .    ? 157.656 159.358 150.816 1.00 71.91  ? 1101 AGS A O3B   1 
HETATM 7176 P PA    . AGS B 2 .    ? 155.424 161.403 148.668 1.00 75.26  ? 1101 AGS A PA    1 
HETATM 7177 O O1A   . AGS B 2 .    ? 154.321 160.716 149.375 1.00 60.57  ? 1101 AGS A O1A   1 
HETATM 7178 O O2A   . AGS B 2 .    ? 155.804 162.754 149.279 1.00 73.27  ? 1101 AGS A O2A   1 
HETATM 7179 O O3A   . AGS B 2 .    ? 156.755 160.539 148.682 1.00 68.52  ? 1101 AGS A O3A   1 
HETATM 7180 O "O5'" . AGS B 2 .    ? 155.003 161.567 147.150 1.00 65.95  ? 1101 AGS A "O5'" 1 
HETATM 7181 C "C5'" . AGS B 2 .    ? 154.859 162.883 146.572 1.00 64.24  ? 1101 AGS A "C5'" 1 
HETATM 7182 C "C4'" . AGS B 2 .    ? 153.403 163.201 146.331 1.00 62.73  ? 1101 AGS A "C4'" 1 
HETATM 7183 O "O4'" . AGS B 2 .    ? 152.944 162.516 145.157 1.00 64.22  ? 1101 AGS A "O4'" 1 
HETATM 7184 C "C3'" . AGS B 2 .    ? 152.429 162.766 147.420 1.00 65.18  ? 1101 AGS A "C3'" 1 
HETATM 7185 O "O3'" . AGS B 2 .    ? 152.328 163.762 148.430 1.00 67.38  ? 1101 AGS A "O3'" 1 
HETATM 7186 C "C2'" . AGS B 2 .    ? 151.103 162.591 146.659 1.00 56.83  ? 1101 AGS A "C2'" 1 
HETATM 7187 O "O2'" . AGS B 2 .    ? 150.235 163.700 146.857 1.00 56.75  ? 1101 AGS A "O2'" 1 
HETATM 7188 C "C1'" . AGS B 2 .    ? 151.533 162.507 145.185 1.00 57.99  ? 1101 AGS A "C1'" 1 
HETATM 7189 N N9    . AGS B 2 .    ? 151.067 161.313 144.487 1.00 56.31  ? 1101 AGS A N9    1 
HETATM 7190 C C8    . AGS B 2 .    ? 151.578 160.045 144.590 1.00 55.12  ? 1101 AGS A C8    1 
HETATM 7191 N N7    . AGS B 2 .    ? 150.966 159.166 143.838 1.00 53.13  ? 1101 AGS A N7    1 
HETATM 7192 C C5    . AGS B 2 .    ? 149.985 159.901 143.189 1.00 50.83  ? 1101 AGS A C5    1 
HETATM 7193 C C6    . AGS B 2 .    ? 148.998 159.552 142.254 1.00 51.61  ? 1101 AGS A C6    1 
HETATM 7194 N N6    . AGS B 2 .    ? 148.826 158.314 141.784 1.00 49.98  ? 1101 AGS A N6    1 
HETATM 7195 N N1    . AGS B 2 .    ? 148.180 160.532 141.808 1.00 53.00  ? 1101 AGS A N1    1 
HETATM 7196 C C2    . AGS B 2 .    ? 148.349 161.772 142.275 1.00 52.86  ? 1101 AGS A C2    1 
HETATM 7197 N N3    . AGS B 2 .    ? 149.244 162.221 143.157 1.00 54.25  ? 1101 AGS A N3    1 
HETATM 7198 C C4    . AGS B 2 .    ? 150.042 161.230 143.583 1.00 53.50  ? 1101 AGS A C4    1 
# 
