data_8VYB
# 
_entry.id   8VYB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8VYB         pdb_00008vyb 10.2210/pdb8vyb/pdb 
WWPDB D_1000281436 ?            ?                   
EMDB  EMD-43655    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VYB 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                    EMD-43645 'consensus EM volume'  
EMDB 'Cryo-EM structure of human core Rab3GAP1/2 complex' EMD-43655 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              calvin.yip@ubc.ca 
_pdbx_contact_author.name_first         Calvin 
_pdbx_contact_author.name_last          Yip 
_pdbx_contact_author.name_mi            K 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1779-9501 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nguyen, K.M.' 1 0009-0007-7487-2222 
'Yip, C.K.'    2 0000-0003-1779-9501 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                479 
_citation.page_last                 479 
_citation.title                     
'Biochemical and structural characterization of Rab3GAP reveals insights into Rab18 nucleotide exchange activity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-55828-8 
_citation.pdbx_database_id_PubMed   39779760 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fairlie, G.M.J.' 1  ?                   
primary 'Nguyen, K.M.'    2  ?                   
primary 'Nam, S.E.'       3  ?                   
primary 'Shaw, A.L.'      4  0000-0002-0615-599X 
primary 'Parson, M.A.H.'  5  0000-0001-6270-559X 
primary 'Shariati, H.R.'  6  ?                   
primary 'Wang, X.'        7  0009-0004-9053-458X 
primary 'Jenkins, M.L.'   8  ?                   
primary 'Gong, M.'        9  ?                   
primary 'Burke, J.E.'     10 0000-0001-7904-9859 
primary 'Yip, C.K.'       11 0000-0003-1779-9501 
# 
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 'Isoform 2 of Rab3 GTPase-activating protein catalytic subunit' 116747.188 1 ? ? ? ? 
2 polymer man 'Rab3 GTPase-activating protein non-catalytic subunit'          65121.422  1 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'RAB3 GTPase-activating protein 130 kDa subunit,Rab3-GAP p130,Rab3-GAP'                                         
2 'RGAP-iso,Rab3 GTPase-activating protein 150 kDa subunit,Rab3-GAP p150,Rab3-GAP150,Rab3-GAP regulatory subunit' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MWSHPQFEKGGGSGGGSGGGSWSHPQFEKLEVLFQGPRSEARGIQRPTSTMAADSEPESEVFEITDFTTASEWERFISKV
EEVLNDWKLIGNSLGKPLEKGIFTSGTWEEKSDEISFADFKFSVTHHYLVQESTDKEGKDELLEDVVPQSMQDLLGMNND
FPPRAHCLVRWYGLREFVVIAPAAHSDAVLSESKCNLLLSSVSIALGNTGCQVPLFVQIHHKWRRMYVGECQGPGVRTDF
EMVHLRKVPNQYTHLSGLLDIFKSKIGCPLTPLPPVSIAIRFTYVLQDWQQYFWPQQPPDIDALVGGEVGGLEFGKLPFG
ACEDPISELHLATTWPHLTEGIIVDNDVYSDLDPIQAPHWSVRVRKAENPQCLLGDFVTEFFKICRRKESTDEILGRSAF
EEEGKETADITHALSKLTEPASVPIHKLSVSNMVHTAKKKIRKHRGVEESPLNNDVLNTILLFLFPDAVSEKPLDGTTST
DNNNPPSESEDYNLYNQFKSAPSDSLTYKLALCLCMINFYHGGLKGVAHLWQEFVLEMRFRWENNFLIPGLASGPPDLRC
CLLHQKLQMLNCCIERKKARDEGKKTSASDVTNIYPGDAGKAGDQLVPDNLKETDKEKGEVGKSWDSWSDSEEEFFECLS
DTEELKGNGQESGKKGGPKEMANLRPEGRLYQHGKLTLLHNGEPLYIPVTQEPAPMTEDLLEEQSEVLAKLGTSAEGAHL
RARMQSACLLSDMESFKAANPGCSLEDFVRWYSPRDYIEEEVIDEKGNVVLKGELSARMKIPSNMWVEAWETAKPIPARR
QRRLFDDTREAEKVLHYLAIQKPADLARHLLPCVIHAAVLKVKEEESLENISSVKKIIKQIISHSSKVLHFPNPEDKKLE
EIIHQITNVEALIARARSLKAKFGTEKCEQEEEKEDLERFVSCLLEQPEVLVTGAGRGHAGRIIHKLFVNAQRLTESSDE
AAAMTPPEEELKRMGSPEERRQNSVSDFPPPAGREFILRTTVPRPAPYSKALPQRMYSVLTKEDFRLAGAFSSDTSFF
;
;MWSHPQFEKGGGSGGGSGGGSWSHPQFEKLEVLFQGPRSEARGIQRPTSTMAADSEPESEVFEITDFTTASEWERFISKV
EEVLNDWKLIGNSLGKPLEKGIFTSGTWEEKSDEISFADFKFSVTHHYLVQESTDKEGKDELLEDVVPQSMQDLLGMNND
FPPRAHCLVRWYGLREFVVIAPAAHSDAVLSESKCNLLLSSVSIALGNTGCQVPLFVQIHHKWRRMYVGECQGPGVRTDF
EMVHLRKVPNQYTHLSGLLDIFKSKIGCPLTPLPPVSIAIRFTYVLQDWQQYFWPQQPPDIDALVGGEVGGLEFGKLPFG
ACEDPISELHLATTWPHLTEGIIVDNDVYSDLDPIQAPHWSVRVRKAENPQCLLGDFVTEFFKICRRKESTDEILGRSAF
EEEGKETADITHALSKLTEPASVPIHKLSVSNMVHTAKKKIRKHRGVEESPLNNDVLNTILLFLFPDAVSEKPLDGTTST
DNNNPPSESEDYNLYNQFKSAPSDSLTYKLALCLCMINFYHGGLKGVAHLWQEFVLEMRFRWENNFLIPGLASGPPDLRC
CLLHQKLQMLNCCIERKKARDEGKKTSASDVTNIYPGDAGKAGDQLVPDNLKETDKEKGEVGKSWDSWSDSEEEFFECLS
DTEELKGNGQESGKKGGPKEMANLRPEGRLYQHGKLTLLHNGEPLYIPVTQEPAPMTEDLLEEQSEVLAKLGTSAEGAHL
RARMQSACLLSDMESFKAANPGCSLEDFVRWYSPRDYIEEEVIDEKGNVVLKGELSARMKIPSNMWVEAWETAKPIPARR
QRRLFDDTREAEKVLHYLAIQKPADLARHLLPCVIHAAVLKVKEEESLENISSVKKIIKQIISHSSKVLHFPNPEDKKLE
EIIHQITNVEALIARARSLKAKFGTEKCEQEEEKEDLERFVSCLLEQPEVLVTGAGRGHAGRIIHKLFVNAQRLTESSDE
AAAMTPPEEELKRMGSPEERRQNSVSDFPPPAGREFILRTTVPRPAPYSKALPQRMYSVLTKEDFRLAGAFSSDTSFF
;
A ? 
2 'polypeptide(L)' no no 
;MACSIVQFCYFQDLQAARDFLFPHLREEILSGALRRDPSKSTDWEDDGWGAWEENEPQEPEEEGNTCKTQKTSWLQDCVL
SLSPTNDLMVIAREQKAVFLVPKWKYSDKGKEEMQFAVGWSGSLNVEEGECVTSALCIPLASQKRSSTGRPDWTCIVVGF
TSGYVRFYTENGVLLLAQLLNEDPVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAA
SGNENIQPPPLAYKKWGLQDIDTIIDHASVGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSNPFTGFFYALE
GSTQPLLSHVALAVASKLTSALFNAASGWLGWKSKHEEEAVQKQKPKVEPATPLAVRFGLPDSRRHGESICLSPCNTLAA
VTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQTVEDLHERVPEKADFSPFGNSQGPSRVAQFLVIYAPRRGILEVWST
QQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSGSVKTVNVPFHLALSDKKLREQKLELGGSGG
RQLDYKDHDGDYKDHDIDYKDDDDK
;
;MACSIVQFCYFQDLQAARDFLFPHLREEILSGALRRDPSKSTDWEDDGWGAWEENEPQEPEEEGNTCKTQKTSWLQDCVL
SLSPTNDLMVIAREQKAVFLVPKWKYSDKGKEEMQFAVGWSGSLNVEEGECVTSALCIPLASQKRSSTGRPDWTCIVVGF
TSGYVRFYTENGVLLLAQLLNEDPVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAA
SGNENIQPPPLAYKKWGLQDIDTIIDHASVGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSNPFTGFFYALE
GSTQPLLSHVALAVASKLTSALFNAASGWLGWKSKHEEEAVQKQKPKVEPATPLAVRFGLPDSRRHGESICLSPCNTLAA
VTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQTVEDLHERVPEKADFSPFGNSQGPSRVAQFLVIYAPRRGILEVWST
QQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSGSVKTVNVPFHLALSDKKLREQKLELGGSGG
RQLDYKDHDGDYKDHDIDYKDDDDK
;
B ? 
# 
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    TRP n 
1 3    SER n 
1 4    HIS n 
1 5    PRO n 
1 6    GLN n 
1 7    PHE n 
1 8    GLU n 
1 9    LYS n 
1 10   GLY n 
1 11   GLY n 
1 12   GLY n 
1 13   SER n 
1 14   GLY n 
1 15   GLY n 
1 16   GLY n 
1 17   SER n 
1 18   GLY n 
1 19   GLY n 
1 20   GLY n 
1 21   SER n 
1 22   TRP n 
1 23   SER n 
1 24   HIS n 
1 25   PRO n 
1 26   GLN n 
1 27   PHE n 
1 28   GLU n 
1 29   LYS n 
1 30   LEU n 
1 31   GLU n 
1 32   VAL n 
1 33   LEU n 
1 34   PHE n 
1 35   GLN n 
1 36   GLY n 
1 37   PRO n 
1 38   ARG n 
1 39   SER n 
1 40   GLU n 
1 41   ALA n 
1 42   ARG n 
1 43   GLY n 
1 44   ILE n 
1 45   GLN n 
1 46   ARG n 
1 47   PRO n 
1 48   THR n 
1 49   SER n 
1 50   THR n 
1 51   MET n 
1 52   ALA n 
1 53   ALA n 
1 54   ASP n 
1 55   SER n 
1 56   GLU n 
1 57   PRO n 
1 58   GLU n 
1 59   SER n 
1 60   GLU n 
1 61   VAL n 
1 62   PHE n 
1 63   GLU n 
1 64   ILE n 
1 65   THR n 
1 66   ASP n 
1 67   PHE n 
1 68   THR n 
1 69   THR n 
1 70   ALA n 
1 71   SER n 
1 72   GLU n 
1 73   TRP n 
1 74   GLU n 
1 75   ARG n 
1 76   PHE n 
1 77   ILE n 
1 78   SER n 
1 79   LYS n 
1 80   VAL n 
1 81   GLU n 
1 82   GLU n 
1 83   VAL n 
1 84   LEU n 
1 85   ASN n 
1 86   ASP n 
1 87   TRP n 
1 88   LYS n 
1 89   LEU n 
1 90   ILE n 
1 91   GLY n 
1 92   ASN n 
1 93   SER n 
1 94   LEU n 
1 95   GLY n 
1 96   LYS n 
1 97   PRO n 
1 98   LEU n 
1 99   GLU n 
1 100  LYS n 
1 101  GLY n 
1 102  ILE n 
1 103  PHE n 
1 104  THR n 
1 105  SER n 
1 106  GLY n 
1 107  THR n 
1 108  TRP n 
1 109  GLU n 
1 110  GLU n 
1 111  LYS n 
1 112  SER n 
1 113  ASP n 
1 114  GLU n 
1 115  ILE n 
1 116  SER n 
1 117  PHE n 
1 118  ALA n 
1 119  ASP n 
1 120  PHE n 
1 121  LYS n 
1 122  PHE n 
1 123  SER n 
1 124  VAL n 
1 125  THR n 
1 126  HIS n 
1 127  HIS n 
1 128  TYR n 
1 129  LEU n 
1 130  VAL n 
1 131  GLN n 
1 132  GLU n 
1 133  SER n 
1 134  THR n 
1 135  ASP n 
1 136  LYS n 
1 137  GLU n 
1 138  GLY n 
1 139  LYS n 
1 140  ASP n 
1 141  GLU n 
1 142  LEU n 
1 143  LEU n 
1 144  GLU n 
1 145  ASP n 
1 146  VAL n 
1 147  VAL n 
1 148  PRO n 
1 149  GLN n 
1 150  SER n 
1 151  MET n 
1 152  GLN n 
1 153  ASP n 
1 154  LEU n 
1 155  LEU n 
1 156  GLY n 
1 157  MET n 
1 158  ASN n 
1 159  ASN n 
1 160  ASP n 
1 161  PHE n 
1 162  PRO n 
1 163  PRO n 
1 164  ARG n 
1 165  ALA n 
1 166  HIS n 
1 167  CYS n 
1 168  LEU n 
1 169  VAL n 
1 170  ARG n 
1 171  TRP n 
1 172  TYR n 
1 173  GLY n 
1 174  LEU n 
1 175  ARG n 
1 176  GLU n 
1 177  PHE n 
1 178  VAL n 
1 179  VAL n 
1 180  ILE n 
1 181  ALA n 
1 182  PRO n 
1 183  ALA n 
1 184  ALA n 
1 185  HIS n 
1 186  SER n 
1 187  ASP n 
1 188  ALA n 
1 189  VAL n 
1 190  LEU n 
1 191  SER n 
1 192  GLU n 
1 193  SER n 
1 194  LYS n 
1 195  CYS n 
1 196  ASN n 
1 197  LEU n 
1 198  LEU n 
1 199  LEU n 
1 200  SER n 
1 201  SER n 
1 202  VAL n 
1 203  SER n 
1 204  ILE n 
1 205  ALA n 
1 206  LEU n 
1 207  GLY n 
1 208  ASN n 
1 209  THR n 
1 210  GLY n 
1 211  CYS n 
1 212  GLN n 
1 213  VAL n 
1 214  PRO n 
1 215  LEU n 
1 216  PHE n 
1 217  VAL n 
1 218  GLN n 
1 219  ILE n 
1 220  HIS n 
1 221  HIS n 
1 222  LYS n 
1 223  TRP n 
1 224  ARG n 
1 225  ARG n 
1 226  MET n 
1 227  TYR n 
1 228  VAL n 
1 229  GLY n 
1 230  GLU n 
1 231  CYS n 
1 232  GLN n 
1 233  GLY n 
1 234  PRO n 
1 235  GLY n 
1 236  VAL n 
1 237  ARG n 
1 238  THR n 
1 239  ASP n 
1 240  PHE n 
1 241  GLU n 
1 242  MET n 
1 243  VAL n 
1 244  HIS n 
1 245  LEU n 
1 246  ARG n 
1 247  LYS n 
1 248  VAL n 
1 249  PRO n 
1 250  ASN n 
1 251  GLN n 
1 252  TYR n 
1 253  THR n 
1 254  HIS n 
1 255  LEU n 
1 256  SER n 
1 257  GLY n 
1 258  LEU n 
1 259  LEU n 
1 260  ASP n 
1 261  ILE n 
1 262  PHE n 
1 263  LYS n 
1 264  SER n 
1 265  LYS n 
1 266  ILE n 
1 267  GLY n 
1 268  CYS n 
1 269  PRO n 
1 270  LEU n 
1 271  THR n 
1 272  PRO n 
1 273  LEU n 
1 274  PRO n 
1 275  PRO n 
1 276  VAL n 
1 277  SER n 
1 278  ILE n 
1 279  ALA n 
1 280  ILE n 
1 281  ARG n 
1 282  PHE n 
1 283  THR n 
1 284  TYR n 
1 285  VAL n 
1 286  LEU n 
1 287  GLN n 
1 288  ASP n 
1 289  TRP n 
1 290  GLN n 
1 291  GLN n 
1 292  TYR n 
1 293  PHE n 
1 294  TRP n 
1 295  PRO n 
1 296  GLN n 
1 297  GLN n 
1 298  PRO n 
1 299  PRO n 
1 300  ASP n 
1 301  ILE n 
1 302  ASP n 
1 303  ALA n 
1 304  LEU n 
1 305  VAL n 
1 306  GLY n 
1 307  GLY n 
1 308  GLU n 
1 309  VAL n 
1 310  GLY n 
1 311  GLY n 
1 312  LEU n 
1 313  GLU n 
1 314  PHE n 
1 315  GLY n 
1 316  LYS n 
1 317  LEU n 
1 318  PRO n 
1 319  PHE n 
1 320  GLY n 
1 321  ALA n 
1 322  CYS n 
1 323  GLU n 
1 324  ASP n 
1 325  PRO n 
1 326  ILE n 
1 327  SER n 
1 328  GLU n 
1 329  LEU n 
1 330  HIS n 
1 331  LEU n 
1 332  ALA n 
1 333  THR n 
1 334  THR n 
1 335  TRP n 
1 336  PRO n 
1 337  HIS n 
1 338  LEU n 
1 339  THR n 
1 340  GLU n 
1 341  GLY n 
1 342  ILE n 
1 343  ILE n 
1 344  VAL n 
1 345  ASP n 
1 346  ASN n 
1 347  ASP n 
1 348  VAL n 
1 349  TYR n 
1 350  SER n 
1 351  ASP n 
1 352  LEU n 
1 353  ASP n 
1 354  PRO n 
1 355  ILE n 
1 356  GLN n 
1 357  ALA n 
1 358  PRO n 
1 359  HIS n 
1 360  TRP n 
1 361  SER n 
1 362  VAL n 
1 363  ARG n 
1 364  VAL n 
1 365  ARG n 
1 366  LYS n 
1 367  ALA n 
1 368  GLU n 
1 369  ASN n 
1 370  PRO n 
1 371  GLN n 
1 372  CYS n 
1 373  LEU n 
1 374  LEU n 
1 375  GLY n 
1 376  ASP n 
1 377  PHE n 
1 378  VAL n 
1 379  THR n 
1 380  GLU n 
1 381  PHE n 
1 382  PHE n 
1 383  LYS n 
1 384  ILE n 
1 385  CYS n 
1 386  ARG n 
1 387  ARG n 
1 388  LYS n 
1 389  GLU n 
1 390  SER n 
1 391  THR n 
1 392  ASP n 
1 393  GLU n 
1 394  ILE n 
1 395  LEU n 
1 396  GLY n 
1 397  ARG n 
1 398  SER n 
1 399  ALA n 
1 400  PHE n 
1 401  GLU n 
1 402  GLU n 
1 403  GLU n 
1 404  GLY n 
1 405  LYS n 
1 406  GLU n 
1 407  THR n 
1 408  ALA n 
1 409  ASP n 
1 410  ILE n 
1 411  THR n 
1 412  HIS n 
1 413  ALA n 
1 414  LEU n 
1 415  SER n 
1 416  LYS n 
1 417  LEU n 
1 418  THR n 
1 419  GLU n 
1 420  PRO n 
1 421  ALA n 
1 422  SER n 
1 423  VAL n 
1 424  PRO n 
1 425  ILE n 
1 426  HIS n 
1 427  LYS n 
1 428  LEU n 
1 429  SER n 
1 430  VAL n 
1 431  SER n 
1 432  ASN n 
1 433  MET n 
1 434  VAL n 
1 435  HIS n 
1 436  THR n 
1 437  ALA n 
1 438  LYS n 
1 439  LYS n 
1 440  LYS n 
1 441  ILE n 
1 442  ARG n 
1 443  LYS n 
1 444  HIS n 
1 445  ARG n 
1 446  GLY n 
1 447  VAL n 
1 448  GLU n 
1 449  GLU n 
1 450  SER n 
1 451  PRO n 
1 452  LEU n 
1 453  ASN n 
1 454  ASN n 
1 455  ASP n 
1 456  VAL n 
1 457  LEU n 
1 458  ASN n 
1 459  THR n 
1 460  ILE n 
1 461  LEU n 
1 462  LEU n 
1 463  PHE n 
1 464  LEU n 
1 465  PHE n 
1 466  PRO n 
1 467  ASP n 
1 468  ALA n 
1 469  VAL n 
1 470  SER n 
1 471  GLU n 
1 472  LYS n 
1 473  PRO n 
1 474  LEU n 
1 475  ASP n 
1 476  GLY n 
1 477  THR n 
1 478  THR n 
1 479  SER n 
1 480  THR n 
1 481  ASP n 
1 482  ASN n 
1 483  ASN n 
1 484  ASN n 
1 485  PRO n 
1 486  PRO n 
1 487  SER n 
1 488  GLU n 
1 489  SER n 
1 490  GLU n 
1 491  ASP n 
1 492  TYR n 
1 493  ASN n 
1 494  LEU n 
1 495  TYR n 
1 496  ASN n 
1 497  GLN n 
1 498  PHE n 
1 499  LYS n 
1 500  SER n 
1 501  ALA n 
1 502  PRO n 
1 503  SER n 
1 504  ASP n 
1 505  SER n 
1 506  LEU n 
1 507  THR n 
1 508  TYR n 
1 509  LYS n 
1 510  LEU n 
1 511  ALA n 
1 512  LEU n 
1 513  CYS n 
1 514  LEU n 
1 515  CYS n 
1 516  MET n 
1 517  ILE n 
1 518  ASN n 
1 519  PHE n 
1 520  TYR n 
1 521  HIS n 
1 522  GLY n 
1 523  GLY n 
1 524  LEU n 
1 525  LYS n 
1 526  GLY n 
1 527  VAL n 
1 528  ALA n 
1 529  HIS n 
1 530  LEU n 
1 531  TRP n 
1 532  GLN n 
1 533  GLU n 
1 534  PHE n 
1 535  VAL n 
1 536  LEU n 
1 537  GLU n 
1 538  MET n 
1 539  ARG n 
1 540  PHE n 
1 541  ARG n 
1 542  TRP n 
1 543  GLU n 
1 544  ASN n 
1 545  ASN n 
1 546  PHE n 
1 547  LEU n 
1 548  ILE n 
1 549  PRO n 
1 550  GLY n 
1 551  LEU n 
1 552  ALA n 
1 553  SER n 
1 554  GLY n 
1 555  PRO n 
1 556  PRO n 
1 557  ASP n 
1 558  LEU n 
1 559  ARG n 
1 560  CYS n 
1 561  CYS n 
1 562  LEU n 
1 563  LEU n 
1 564  HIS n 
1 565  GLN n 
1 566  LYS n 
1 567  LEU n 
1 568  GLN n 
1 569  MET n 
1 570  LEU n 
1 571  ASN n 
1 572  CYS n 
1 573  CYS n 
1 574  ILE n 
1 575  GLU n 
1 576  ARG n 
1 577  LYS n 
1 578  LYS n 
1 579  ALA n 
1 580  ARG n 
1 581  ASP n 
1 582  GLU n 
1 583  GLY n 
1 584  LYS n 
1 585  LYS n 
1 586  THR n 
1 587  SER n 
1 588  ALA n 
1 589  SER n 
1 590  ASP n 
1 591  VAL n 
1 592  THR n 
1 593  ASN n 
1 594  ILE n 
1 595  TYR n 
1 596  PRO n 
1 597  GLY n 
1 598  ASP n 
1 599  ALA n 
1 600  GLY n 
1 601  LYS n 
1 602  ALA n 
1 603  GLY n 
1 604  ASP n 
1 605  GLN n 
1 606  LEU n 
1 607  VAL n 
1 608  PRO n 
1 609  ASP n 
1 610  ASN n 
1 611  LEU n 
1 612  LYS n 
1 613  GLU n 
1 614  THR n 
1 615  ASP n 
1 616  LYS n 
1 617  GLU n 
1 618  LYS n 
1 619  GLY n 
1 620  GLU n 
1 621  VAL n 
1 622  GLY n 
1 623  LYS n 
1 624  SER n 
1 625  TRP n 
1 626  ASP n 
1 627  SER n 
1 628  TRP n 
1 629  SER n 
1 630  ASP n 
1 631  SER n 
1 632  GLU n 
1 633  GLU n 
1 634  GLU n 
1 635  PHE n 
1 636  PHE n 
1 637  GLU n 
1 638  CYS n 
1 639  LEU n 
1 640  SER n 
1 641  ASP n 
1 642  THR n 
1 643  GLU n 
1 644  GLU n 
1 645  LEU n 
1 646  LYS n 
1 647  GLY n 
1 648  ASN n 
1 649  GLY n 
1 650  GLN n 
1 651  GLU n 
1 652  SER n 
1 653  GLY n 
1 654  LYS n 
1 655  LYS n 
1 656  GLY n 
1 657  GLY n 
1 658  PRO n 
1 659  LYS n 
1 660  GLU n 
1 661  MET n 
1 662  ALA n 
1 663  ASN n 
1 664  LEU n 
1 665  ARG n 
1 666  PRO n 
1 667  GLU n 
1 668  GLY n 
1 669  ARG n 
1 670  LEU n 
1 671  TYR n 
1 672  GLN n 
1 673  HIS n 
1 674  GLY n 
1 675  LYS n 
1 676  LEU n 
1 677  THR n 
1 678  LEU n 
1 679  LEU n 
1 680  HIS n 
1 681  ASN n 
1 682  GLY n 
1 683  GLU n 
1 684  PRO n 
1 685  LEU n 
1 686  TYR n 
1 687  ILE n 
1 688  PRO n 
1 689  VAL n 
1 690  THR n 
1 691  GLN n 
1 692  GLU n 
1 693  PRO n 
1 694  ALA n 
1 695  PRO n 
1 696  MET n 
1 697  THR n 
1 698  GLU n 
1 699  ASP n 
1 700  LEU n 
1 701  LEU n 
1 702  GLU n 
1 703  GLU n 
1 704  GLN n 
1 705  SER n 
1 706  GLU n 
1 707  VAL n 
1 708  LEU n 
1 709  ALA n 
1 710  LYS n 
1 711  LEU n 
1 712  GLY n 
1 713  THR n 
1 714  SER n 
1 715  ALA n 
1 716  GLU n 
1 717  GLY n 
1 718  ALA n 
1 719  HIS n 
1 720  LEU n 
1 721  ARG n 
1 722  ALA n 
1 723  ARG n 
1 724  MET n 
1 725  GLN n 
1 726  SER n 
1 727  ALA n 
1 728  CYS n 
1 729  LEU n 
1 730  LEU n 
1 731  SER n 
1 732  ASP n 
1 733  MET n 
1 734  GLU n 
1 735  SER n 
1 736  PHE n 
1 737  LYS n 
1 738  ALA n 
1 739  ALA n 
1 740  ASN n 
1 741  PRO n 
1 742  GLY n 
1 743  CYS n 
1 744  SER n 
1 745  LEU n 
1 746  GLU n 
1 747  ASP n 
1 748  PHE n 
1 749  VAL n 
1 750  ARG n 
1 751  TRP n 
1 752  TYR n 
1 753  SER n 
1 754  PRO n 
1 755  ARG n 
1 756  ASP n 
1 757  TYR n 
1 758  ILE n 
1 759  GLU n 
1 760  GLU n 
1 761  GLU n 
1 762  VAL n 
1 763  ILE n 
1 764  ASP n 
1 765  GLU n 
1 766  LYS n 
1 767  GLY n 
1 768  ASN n 
1 769  VAL n 
1 770  VAL n 
1 771  LEU n 
1 772  LYS n 
1 773  GLY n 
1 774  GLU n 
1 775  LEU n 
1 776  SER n 
1 777  ALA n 
1 778  ARG n 
1 779  MET n 
1 780  LYS n 
1 781  ILE n 
1 782  PRO n 
1 783  SER n 
1 784  ASN n 
1 785  MET n 
1 786  TRP n 
1 787  VAL n 
1 788  GLU n 
1 789  ALA n 
1 790  TRP n 
1 791  GLU n 
1 792  THR n 
1 793  ALA n 
1 794  LYS n 
1 795  PRO n 
1 796  ILE n 
1 797  PRO n 
1 798  ALA n 
1 799  ARG n 
1 800  ARG n 
1 801  GLN n 
1 802  ARG n 
1 803  ARG n 
1 804  LEU n 
1 805  PHE n 
1 806  ASP n 
1 807  ASP n 
1 808  THR n 
1 809  ARG n 
1 810  GLU n 
1 811  ALA n 
1 812  GLU n 
1 813  LYS n 
1 814  VAL n 
1 815  LEU n 
1 816  HIS n 
1 817  TYR n 
1 818  LEU n 
1 819  ALA n 
1 820  ILE n 
1 821  GLN n 
1 822  LYS n 
1 823  PRO n 
1 824  ALA n 
1 825  ASP n 
1 826  LEU n 
1 827  ALA n 
1 828  ARG n 
1 829  HIS n 
1 830  LEU n 
1 831  LEU n 
1 832  PRO n 
1 833  CYS n 
1 834  VAL n 
1 835  ILE n 
1 836  HIS n 
1 837  ALA n 
1 838  ALA n 
1 839  VAL n 
1 840  LEU n 
1 841  LYS n 
1 842  VAL n 
1 843  LYS n 
1 844  GLU n 
1 845  GLU n 
1 846  GLU n 
1 847  SER n 
1 848  LEU n 
1 849  GLU n 
1 850  ASN n 
1 851  ILE n 
1 852  SER n 
1 853  SER n 
1 854  VAL n 
1 855  LYS n 
1 856  LYS n 
1 857  ILE n 
1 858  ILE n 
1 859  LYS n 
1 860  GLN n 
1 861  ILE n 
1 862  ILE n 
1 863  SER n 
1 864  HIS n 
1 865  SER n 
1 866  SER n 
1 867  LYS n 
1 868  VAL n 
1 869  LEU n 
1 870  HIS n 
1 871  PHE n 
1 872  PRO n 
1 873  ASN n 
1 874  PRO n 
1 875  GLU n 
1 876  ASP n 
1 877  LYS n 
1 878  LYS n 
1 879  LEU n 
1 880  GLU n 
1 881  GLU n 
1 882  ILE n 
1 883  ILE n 
1 884  HIS n 
1 885  GLN n 
1 886  ILE n 
1 887  THR n 
1 888  ASN n 
1 889  VAL n 
1 890  GLU n 
1 891  ALA n 
1 892  LEU n 
1 893  ILE n 
1 894  ALA n 
1 895  ARG n 
1 896  ALA n 
1 897  ARG n 
1 898  SER n 
1 899  LEU n 
1 900  LYS n 
1 901  ALA n 
1 902  LYS n 
1 903  PHE n 
1 904  GLY n 
1 905  THR n 
1 906  GLU n 
1 907  LYS n 
1 908  CYS n 
1 909  GLU n 
1 910  GLN n 
1 911  GLU n 
1 912  GLU n 
1 913  GLU n 
1 914  LYS n 
1 915  GLU n 
1 916  ASP n 
1 917  LEU n 
1 918  GLU n 
1 919  ARG n 
1 920  PHE n 
1 921  VAL n 
1 922  SER n 
1 923  CYS n 
1 924  LEU n 
1 925  LEU n 
1 926  GLU n 
1 927  GLN n 
1 928  PRO n 
1 929  GLU n 
1 930  VAL n 
1 931  LEU n 
1 932  VAL n 
1 933  THR n 
1 934  GLY n 
1 935  ALA n 
1 936  GLY n 
1 937  ARG n 
1 938  GLY n 
1 939  HIS n 
1 940  ALA n 
1 941  GLY n 
1 942  ARG n 
1 943  ILE n 
1 944  ILE n 
1 945  HIS n 
1 946  LYS n 
1 947  LEU n 
1 948  PHE n 
1 949  VAL n 
1 950  ASN n 
1 951  ALA n 
1 952  GLN n 
1 953  ARG n 
1 954  LEU n 
1 955  THR n 
1 956  GLU n 
1 957  SER n 
1 958  SER n 
1 959  ASP n 
1 960  GLU n 
1 961  ALA n 
1 962  ALA n 
1 963  ALA n 
1 964  MET n 
1 965  THR n 
1 966  PRO n 
1 967  PRO n 
1 968  GLU n 
1 969  GLU n 
1 970  GLU n 
1 971  LEU n 
1 972  LYS n 
1 973  ARG n 
1 974  MET n 
1 975  GLY n 
1 976  SER n 
1 977  PRO n 
1 978  GLU n 
1 979  GLU n 
1 980  ARG n 
1 981  ARG n 
1 982  GLN n 
1 983  ASN n 
1 984  SER n 
1 985  VAL n 
1 986  SER n 
1 987  ASP n 
1 988  PHE n 
1 989  PRO n 
1 990  PRO n 
1 991  PRO n 
1 992  ALA n 
1 993  GLY n 
1 994  ARG n 
1 995  GLU n 
1 996  PHE n 
1 997  ILE n 
1 998  LEU n 
1 999  ARG n 
1 1000 THR n 
1 1001 THR n 
1 1002 VAL n 
1 1003 PRO n 
1 1004 ARG n 
1 1005 PRO n 
1 1006 ALA n 
1 1007 PRO n 
1 1008 TYR n 
1 1009 SER n 
1 1010 LYS n 
1 1011 ALA n 
1 1012 LEU n 
1 1013 PRO n 
1 1014 GLN n 
1 1015 ARG n 
1 1016 MET n 
1 1017 TYR n 
1 1018 SER n 
1 1019 VAL n 
1 1020 LEU n 
1 1021 THR n 
1 1022 LYS n 
1 1023 GLU n 
1 1024 ASP n 
1 1025 PHE n 
1 1026 ARG n 
1 1027 LEU n 
1 1028 ALA n 
1 1029 GLY n 
1 1030 ALA n 
1 1031 PHE n 
1 1032 SER n 
1 1033 SER n 
1 1034 ASP n 
1 1035 THR n 
1 1036 SER n 
1 1037 PHE n 
1 1038 PHE n 
2 1    MET n 
2 2    ALA n 
2 3    CYS n 
2 4    SER n 
2 5    ILE n 
2 6    VAL n 
2 7    GLN n 
2 8    PHE n 
2 9    CYS n 
2 10   TYR n 
2 11   PHE n 
2 12   GLN n 
2 13   ASP n 
2 14   LEU n 
2 15   GLN n 
2 16   ALA n 
2 17   ALA n 
2 18   ARG n 
2 19   ASP n 
2 20   PHE n 
2 21   LEU n 
2 22   PHE n 
2 23   PRO n 
2 24   HIS n 
2 25   LEU n 
2 26   ARG n 
2 27   GLU n 
2 28   GLU n 
2 29   ILE n 
2 30   LEU n 
2 31   SER n 
2 32   GLY n 
2 33   ALA n 
2 34   LEU n 
2 35   ARG n 
2 36   ARG n 
2 37   ASP n 
2 38   PRO n 
2 39   SER n 
2 40   LYS n 
2 41   SER n 
2 42   THR n 
2 43   ASP n 
2 44   TRP n 
2 45   GLU n 
2 46   ASP n 
2 47   ASP n 
2 48   GLY n 
2 49   TRP n 
2 50   GLY n 
2 51   ALA n 
2 52   TRP n 
2 53   GLU n 
2 54   GLU n 
2 55   ASN n 
2 56   GLU n 
2 57   PRO n 
2 58   GLN n 
2 59   GLU n 
2 60   PRO n 
2 61   GLU n 
2 62   GLU n 
2 63   GLU n 
2 64   GLY n 
2 65   ASN n 
2 66   THR n 
2 67   CYS n 
2 68   LYS n 
2 69   THR n 
2 70   GLN n 
2 71   LYS n 
2 72   THR n 
2 73   SER n 
2 74   TRP n 
2 75   LEU n 
2 76   GLN n 
2 77   ASP n 
2 78   CYS n 
2 79   VAL n 
2 80   LEU n 
2 81   SER n 
2 82   LEU n 
2 83   SER n 
2 84   PRO n 
2 85   THR n 
2 86   ASN n 
2 87   ASP n 
2 88   LEU n 
2 89   MET n 
2 90   VAL n 
2 91   ILE n 
2 92   ALA n 
2 93   ARG n 
2 94   GLU n 
2 95   GLN n 
2 96   LYS n 
2 97   ALA n 
2 98   VAL n 
2 99   PHE n 
2 100  LEU n 
2 101  VAL n 
2 102  PRO n 
2 103  LYS n 
2 104  TRP n 
2 105  LYS n 
2 106  TYR n 
2 107  SER n 
2 108  ASP n 
2 109  LYS n 
2 110  GLY n 
2 111  LYS n 
2 112  GLU n 
2 113  GLU n 
2 114  MET n 
2 115  GLN n 
2 116  PHE n 
2 117  ALA n 
2 118  VAL n 
2 119  GLY n 
2 120  TRP n 
2 121  SER n 
2 122  GLY n 
2 123  SER n 
2 124  LEU n 
2 125  ASN n 
2 126  VAL n 
2 127  GLU n 
2 128  GLU n 
2 129  GLY n 
2 130  GLU n 
2 131  CYS n 
2 132  VAL n 
2 133  THR n 
2 134  SER n 
2 135  ALA n 
2 136  LEU n 
2 137  CYS n 
2 138  ILE n 
2 139  PRO n 
2 140  LEU n 
2 141  ALA n 
2 142  SER n 
2 143  GLN n 
2 144  LYS n 
2 145  ARG n 
2 146  SER n 
2 147  SER n 
2 148  THR n 
2 149  GLY n 
2 150  ARG n 
2 151  PRO n 
2 152  ASP n 
2 153  TRP n 
2 154  THR n 
2 155  CYS n 
2 156  ILE n 
2 157  VAL n 
2 158  VAL n 
2 159  GLY n 
2 160  PHE n 
2 161  THR n 
2 162  SER n 
2 163  GLY n 
2 164  TYR n 
2 165  VAL n 
2 166  ARG n 
2 167  PHE n 
2 168  TYR n 
2 169  THR n 
2 170  GLU n 
2 171  ASN n 
2 172  GLY n 
2 173  VAL n 
2 174  LEU n 
2 175  LEU n 
2 176  LEU n 
2 177  ALA n 
2 178  GLN n 
2 179  LEU n 
2 180  LEU n 
2 181  ASN n 
2 182  GLU n 
2 183  ASP n 
2 184  PRO n 
2 185  VAL n 
2 186  LEU n 
2 187  GLN n 
2 188  LEU n 
2 189  LYS n 
2 190  CYS n 
2 191  ARG n 
2 192  THR n 
2 193  TYR n 
2 194  GLU n 
2 195  ILE n 
2 196  PRO n 
2 197  ARG n 
2 198  HIS n 
2 199  PRO n 
2 200  GLY n 
2 201  VAL n 
2 202  THR n 
2 203  GLU n 
2 204  GLN n 
2 205  ASN n 
2 206  GLU n 
2 207  GLU n 
2 208  LEU n 
2 209  SER n 
2 210  ILE n 
2 211  LEU n 
2 212  TYR n 
2 213  PRO n 
2 214  ALA n 
2 215  ALA n 
2 216  ILE n 
2 217  VAL n 
2 218  THR n 
2 219  ILE n 
2 220  ASP n 
2 221  GLY n 
2 222  PHE n 
2 223  SER n 
2 224  LEU n 
2 225  PHE n 
2 226  GLN n 
2 227  SER n 
2 228  LEU n 
2 229  ARG n 
2 230  ALA n 
2 231  CYS n 
2 232  ARG n 
2 233  ASN n 
2 234  GLN n 
2 235  VAL n 
2 236  ALA n 
2 237  LYS n 
2 238  ALA n 
2 239  ALA n 
2 240  ALA n 
2 241  SER n 
2 242  GLY n 
2 243  ASN n 
2 244  GLU n 
2 245  ASN n 
2 246  ILE n 
2 247  GLN n 
2 248  PRO n 
2 249  PRO n 
2 250  PRO n 
2 251  LEU n 
2 252  ALA n 
2 253  TYR n 
2 254  LYS n 
2 255  LYS n 
2 256  TRP n 
2 257  GLY n 
2 258  LEU n 
2 259  GLN n 
2 260  ASP n 
2 261  ILE n 
2 262  ASP n 
2 263  THR n 
2 264  ILE n 
2 265  ILE n 
2 266  ASP n 
2 267  HIS n 
2 268  ALA n 
2 269  SER n 
2 270  VAL n 
2 271  GLY n 
2 272  ILE n 
2 273  MET n 
2 274  THR n 
2 275  LEU n 
2 276  SER n 
2 277  PRO n 
2 278  PHE n 
2 279  ASP n 
2 280  GLN n 
2 281  MET n 
2 282  LYS n 
2 283  THR n 
2 284  ALA n 
2 285  SER n 
2 286  ASN n 
2 287  ILE n 
2 288  GLY n 
2 289  GLY n 
2 290  PHE n 
2 291  ASN n 
2 292  ALA n 
2 293  ALA n 
2 294  ILE n 
2 295  LYS n 
2 296  ASN n 
2 297  SER n 
2 298  PRO n 
2 299  PRO n 
2 300  ALA n 
2 301  MET n 
2 302  SER n 
2 303  GLN n 
2 304  TYR n 
2 305  ILE n 
2 306  THR n 
2 307  VAL n 
2 308  GLY n 
2 309  SER n 
2 310  ASN n 
2 311  PRO n 
2 312  PHE n 
2 313  THR n 
2 314  GLY n 
2 315  PHE n 
2 316  PHE n 
2 317  TYR n 
2 318  ALA n 
2 319  LEU n 
2 320  GLU n 
2 321  GLY n 
2 322  SER n 
2 323  THR n 
2 324  GLN n 
2 325  PRO n 
2 326  LEU n 
2 327  LEU n 
2 328  SER n 
2 329  HIS n 
2 330  VAL n 
2 331  ALA n 
2 332  LEU n 
2 333  ALA n 
2 334  VAL n 
2 335  ALA n 
2 336  SER n 
2 337  LYS n 
2 338  LEU n 
2 339  THR n 
2 340  SER n 
2 341  ALA n 
2 342  LEU n 
2 343  PHE n 
2 344  ASN n 
2 345  ALA n 
2 346  ALA n 
2 347  SER n 
2 348  GLY n 
2 349  TRP n 
2 350  LEU n 
2 351  GLY n 
2 352  TRP n 
2 353  LYS n 
2 354  SER n 
2 355  LYS n 
2 356  HIS n 
2 357  GLU n 
2 358  GLU n 
2 359  GLU n 
2 360  ALA n 
2 361  VAL n 
2 362  GLN n 
2 363  LYS n 
2 364  GLN n 
2 365  LYS n 
2 366  PRO n 
2 367  LYS n 
2 368  VAL n 
2 369  GLU n 
2 370  PRO n 
2 371  ALA n 
2 372  THR n 
2 373  PRO n 
2 374  LEU n 
2 375  ALA n 
2 376  VAL n 
2 377  ARG n 
2 378  PHE n 
2 379  GLY n 
2 380  LEU n 
2 381  PRO n 
2 382  ASP n 
2 383  SER n 
2 384  ARG n 
2 385  ARG n 
2 386  HIS n 
2 387  GLY n 
2 388  GLU n 
2 389  SER n 
2 390  ILE n 
2 391  CYS n 
2 392  LEU n 
2 393  SER n 
2 394  PRO n 
2 395  CYS n 
2 396  ASN n 
2 397  THR n 
2 398  LEU n 
2 399  ALA n 
2 400  ALA n 
2 401  VAL n 
2 402  THR n 
2 403  ASP n 
2 404  ASP n 
2 405  PHE n 
2 406  GLY n 
2 407  ARG n 
2 408  VAL n 
2 409  ILE n 
2 410  LEU n 
2 411  LEU n 
2 412  ASP n 
2 413  VAL n 
2 414  ALA n 
2 415  ARG n 
2 416  GLY n 
2 417  ILE n 
2 418  ALA n 
2 419  ILE n 
2 420  ARG n 
2 421  MET n 
2 422  TRP n 
2 423  LYS n 
2 424  GLY n 
2 425  TYR n 
2 426  ARG n 
2 427  ASP n 
2 428  ALA n 
2 429  GLN n 
2 430  ILE n 
2 431  GLY n 
2 432  TRP n 
2 433  ILE n 
2 434  GLN n 
2 435  THR n 
2 436  VAL n 
2 437  GLU n 
2 438  ASP n 
2 439  LEU n 
2 440  HIS n 
2 441  GLU n 
2 442  ARG n 
2 443  VAL n 
2 444  PRO n 
2 445  GLU n 
2 446  LYS n 
2 447  ALA n 
2 448  ASP n 
2 449  PHE n 
2 450  SER n 
2 451  PRO n 
2 452  PHE n 
2 453  GLY n 
2 454  ASN n 
2 455  SER n 
2 456  GLN n 
2 457  GLY n 
2 458  PRO n 
2 459  SER n 
2 460  ARG n 
2 461  VAL n 
2 462  ALA n 
2 463  GLN n 
2 464  PHE n 
2 465  LEU n 
2 466  VAL n 
2 467  ILE n 
2 468  TYR n 
2 469  ALA n 
2 470  PRO n 
2 471  ARG n 
2 472  ARG n 
2 473  GLY n 
2 474  ILE n 
2 475  LEU n 
2 476  GLU n 
2 477  VAL n 
2 478  TRP n 
2 479  SER n 
2 480  THR n 
2 481  GLN n 
2 482  GLN n 
2 483  GLY n 
2 484  PRO n 
2 485  ARG n 
2 486  VAL n 
2 487  GLY n 
2 488  ALA n 
2 489  PHE n 
2 490  ASN n 
2 491  VAL n 
2 492  GLY n 
2 493  LYS n 
2 494  HIS n 
2 495  CYS n 
2 496  ARG n 
2 497  LEU n 
2 498  LEU n 
2 499  TYR n 
2 500  PRO n 
2 501  GLY n 
2 502  TYR n 
2 503  LYS n 
2 504  ILE n 
2 505  MET n 
2 506  GLY n 
2 507  LEU n 
2 508  ASN n 
2 509  ASN n 
2 510  VAL n 
2 511  THR n 
2 512  SER n 
2 513  GLN n 
2 514  SER n 
2 515  TRP n 
2 516  GLN n 
2 517  PRO n 
2 518  GLN n 
2 519  THR n 
2 520  TYR n 
2 521  GLN n 
2 522  ILE n 
2 523  CYS n 
2 524  LEU n 
2 525  VAL n 
2 526  ASP n 
2 527  PRO n 
2 528  VAL n 
2 529  SER n 
2 530  GLY n 
2 531  SER n 
2 532  VAL n 
2 533  LYS n 
2 534  THR n 
2 535  VAL n 
2 536  ASN n 
2 537  VAL n 
2 538  PRO n 
2 539  PHE n 
2 540  HIS n 
2 541  LEU n 
2 542  ALA n 
2 543  LEU n 
2 544  SER n 
2 545  ASP n 
2 546  LYS n 
2 547  LYS n 
2 548  LEU n 
2 549  ARG n 
2 550  GLU n 
2 551  GLN n 
2 552  LYS n 
2 553  LEU n 
2 554  GLU n 
2 555  LEU n 
2 556  GLY n 
2 557  GLY n 
2 558  SER n 
2 559  GLY n 
2 560  GLY n 
2 561  ARG n 
2 562  GLN n 
2 563  LEU n 
2 564  ASP n 
2 565  TYR n 
2 566  LYS n 
2 567  ASP n 
2 568  HIS n 
2 569  ASP n 
2 570  GLY n 
2 571  ASP n 
2 572  TYR n 
2 573  LYS n 
2 574  ASP n 
2 575  HIS n 
2 576  ASP n 
2 577  ILE n 
2 578  ASP n 
2 579  TYR n 
2 580  LYS n 
2 581  ASP n 
2 582  ASP n 
2 583  ASP n 
2 584  ASP n 
2 585  LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 1038 human ? 'RAB3GAP1, KIAA0066, RAB3GAP' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? pBIG1A ? ? 
2 1 sample 'Biological sequence' 1 585  human ? 'RAB3GAP2, KIAA0839'          ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? pBIG1A ? ? 
# 
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 
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    -49 ?   ?   ?   A . n 
A 1 2    TRP 2    -48 ?   ?   ?   A . n 
A 1 3    SER 3    -47 ?   ?   ?   A . n 
A 1 4    HIS 4    -46 ?   ?   ?   A . n 
A 1 5    PRO 5    -45 ?   ?   ?   A . n 
A 1 6    GLN 6    -44 ?   ?   ?   A . n 
A 1 7    PHE 7    -43 ?   ?   ?   A . n 
A 1 8    GLU 8    -42 ?   ?   ?   A . n 
A 1 9    LYS 9    -41 ?   ?   ?   A . n 
A 1 10   GLY 10   -40 ?   ?   ?   A . n 
A 1 11   GLY 11   -39 ?   ?   ?   A . n 
A 1 12   GLY 12   -38 ?   ?   ?   A . n 
A 1 13   SER 13   -37 ?   ?   ?   A . n 
A 1 14   GLY 14   -36 ?   ?   ?   A . n 
A 1 15   GLY 15   -35 ?   ?   ?   A . n 
A 1 16   GLY 16   -34 ?   ?   ?   A . n 
A 1 17   SER 17   -33 ?   ?   ?   A . n 
A 1 18   GLY 18   -32 ?   ?   ?   A . n 
A 1 19   GLY 19   -31 ?   ?   ?   A . n 
A 1 20   GLY 20   -30 ?   ?   ?   A . n 
A 1 21   SER 21   -29 ?   ?   ?   A . n 
A 1 22   TRP 22   -28 ?   ?   ?   A . n 
A 1 23   SER 23   -27 ?   ?   ?   A . n 
A 1 24   HIS 24   -26 ?   ?   ?   A . n 
A 1 25   PRO 25   -25 ?   ?   ?   A . n 
A 1 26   GLN 26   -24 ?   ?   ?   A . n 
A 1 27   PHE 27   -23 ?   ?   ?   A . n 
A 1 28   GLU 28   -22 ?   ?   ?   A . n 
A 1 29   LYS 29   -21 ?   ?   ?   A . n 
A 1 30   LEU 30   -20 ?   ?   ?   A . n 
A 1 31   GLU 31   -19 ?   ?   ?   A . n 
A 1 32   VAL 32   -18 ?   ?   ?   A . n 
A 1 33   LEU 33   -17 ?   ?   ?   A . n 
A 1 34   PHE 34   -16 ?   ?   ?   A . n 
A 1 35   GLN 35   -15 ?   ?   ?   A . n 
A 1 36   GLY 36   -14 ?   ?   ?   A . n 
A 1 37   PRO 37   -13 ?   ?   ?   A . n 
A 1 38   ARG 38   -12 ?   ?   ?   A . n 
A 1 39   SER 39   -11 ?   ?   ?   A . n 
A 1 40   GLU 40   -10 ?   ?   ?   A . n 
A 1 41   ALA 41   -9  ?   ?   ?   A . n 
A 1 42   ARG 42   -8  ?   ?   ?   A . n 
A 1 43   GLY 43   -7  ?   ?   ?   A . n 
A 1 44   ILE 44   -6  ?   ?   ?   A . n 
A 1 45   GLN 45   -5  ?   ?   ?   A . n 
A 1 46   ARG 46   -4  ?   ?   ?   A . n 
A 1 47   PRO 47   -3  ?   ?   ?   A . n 
A 1 48   THR 48   -2  ?   ?   ?   A . n 
A 1 49   SER 49   -1  ?   ?   ?   A . n 
A 1 50   THR 50   0   ?   ?   ?   A . n 
A 1 51   MET 51   1   ?   ?   ?   A . n 
A 1 52   ALA 52   2   ?   ?   ?   A . n 
A 1 53   ALA 53   3   ?   ?   ?   A . n 
A 1 54   ASP 54   4   ?   ?   ?   A . n 
A 1 55   SER 55   5   ?   ?   ?   A . n 
A 1 56   GLU 56   6   ?   ?   ?   A . n 
A 1 57   PRO 57   7   ?   ?   ?   A . n 
A 1 58   GLU 58   8   ?   ?   ?   A . n 
A 1 59   SER 59   9   ?   ?   ?   A . n 
A 1 60   GLU 60   10  ?   ?   ?   A . n 
A 1 61   VAL 61   11  ?   ?   ?   A . n 
A 1 62   PHE 62   12  ?   ?   ?   A . n 
A 1 63   GLU 63   13  ?   ?   ?   A . n 
A 1 64   ILE 64   14  ?   ?   ?   A . n 
A 1 65   THR 65   15  ?   ?   ?   A . n 
A 1 66   ASP 66   16  ?   ?   ?   A . n 
A 1 67   PHE 67   17  ?   ?   ?   A . n 
A 1 68   THR 68   18  ?   ?   ?   A . n 
A 1 69   THR 69   19  19  THR THR A . n 
A 1 70   ALA 70   20  20  ALA ALA A . n 
A 1 71   SER 71   21  21  SER SER A . n 
A 1 72   GLU 72   22  22  GLU GLU A . n 
A 1 73   TRP 73   23  23  TRP TRP A . n 
A 1 74   GLU 74   24  24  GLU GLU A . n 
A 1 75   ARG 75   25  25  ARG ARG A . n 
A 1 76   PHE 76   26  26  PHE PHE A . n 
A 1 77   ILE 77   27  27  ILE ILE A . n 
A 1 78   SER 78   28  28  SER SER A . n 
A 1 79   LYS 79   29  29  LYS LYS A . n 
A 1 80   VAL 80   30  30  VAL VAL A . n 
A 1 81   GLU 81   31  31  GLU GLU A . n 
A 1 82   GLU 82   32  32  GLU GLU A . n 
A 1 83   VAL 83   33  33  VAL VAL A . n 
A 1 84   LEU 84   34  34  LEU LEU A . n 
A 1 85   ASN 85   35  35  ASN ASN A . n 
A 1 86   ASP 86   36  36  ASP ASP A . n 
A 1 87   TRP 87   37  37  TRP TRP A . n 
A 1 88   LYS 88   38  38  LYS LYS A . n 
A 1 89   LEU 89   39  39  LEU LEU A . n 
A 1 90   ILE 90   40  40  ILE ILE A . n 
A 1 91   GLY 91   41  41  GLY GLY A . n 
A 1 92   ASN 92   42  42  ASN ASN A . n 
A 1 93   SER 93   43  43  SER SER A . n 
A 1 94   LEU 94   44  44  LEU LEU A . n 
A 1 95   GLY 95   45  45  GLY GLY A . n 
A 1 96   LYS 96   46  46  LYS LYS A . n 
A 1 97   PRO 97   47  47  PRO PRO A . n 
A 1 98   LEU 98   48  48  LEU LEU A . n 
A 1 99   GLU 99   49  49  GLU GLU A . n 
A 1 100  LYS 100  50  50  LYS LYS A . n 
A 1 101  GLY 101  51  51  GLY GLY A . n 
A 1 102  ILE 102  52  52  ILE ILE A . n 
A 1 103  PHE 103  53  53  PHE PHE A . n 
A 1 104  THR 104  54  54  THR THR A . n 
A 1 105  SER 105  55  55  SER SER A . n 
A 1 106  GLY 106  56  56  GLY GLY A . n 
A 1 107  THR 107  57  57  THR THR A . n 
A 1 108  TRP 108  58  58  TRP TRP A . n 
A 1 109  GLU 109  59  59  GLU GLU A . n 
A 1 110  GLU 110  60  60  GLU GLU A . n 
A 1 111  LYS 111  61  61  LYS LYS A . n 
A 1 112  SER 112  62  62  SER SER A . n 
A 1 113  ASP 113  63  63  ASP ASP A . n 
A 1 114  GLU 114  64  64  GLU GLU A . n 
A 1 115  ILE 115  65  65  ILE ILE A . n 
A 1 116  SER 116  66  66  SER SER A . n 
A 1 117  PHE 117  67  67  PHE PHE A . n 
A 1 118  ALA 118  68  68  ALA ALA A . n 
A 1 119  ASP 119  69  69  ASP ASP A . n 
A 1 120  PHE 120  70  70  PHE PHE A . n 
A 1 121  LYS 121  71  71  LYS LYS A . n 
A 1 122  PHE 122  72  72  PHE PHE A . n 
A 1 123  SER 123  73  73  SER SER A . n 
A 1 124  VAL 124  74  74  VAL VAL A . n 
A 1 125  THR 125  75  75  THR THR A . n 
A 1 126  HIS 126  76  76  HIS HIS A . n 
A 1 127  HIS 127  77  77  HIS HIS A . n 
A 1 128  TYR 128  78  78  TYR TYR A . n 
A 1 129  LEU 129  79  79  LEU LEU A . n 
A 1 130  VAL 130  80  80  VAL VAL A . n 
A 1 131  GLN 131  81  81  GLN GLN A . n 
A 1 132  GLU 132  82  82  GLU GLU A . n 
A 1 133  SER 133  83  83  SER SER A . n 
A 1 134  THR 134  84  84  THR THR A . n 
A 1 135  ASP 135  85  85  ASP ASP A . n 
A 1 136  LYS 136  86  86  LYS LYS A . n 
A 1 137  GLU 137  87  87  GLU GLU A . n 
A 1 138  GLY 138  88  88  GLY GLY A . n 
A 1 139  LYS 139  89  89  LYS LYS A . n 
A 1 140  ASP 140  90  90  ASP ASP A . n 
A 1 141  GLU 141  91  91  GLU GLU A . n 
A 1 142  LEU 142  92  92  LEU LEU A . n 
A 1 143  LEU 143  93  93  LEU LEU A . n 
A 1 144  GLU 144  94  94  GLU GLU A . n 
A 1 145  ASP 145  95  95  ASP ASP A . n 
A 1 146  VAL 146  96  96  VAL VAL A . n 
A 1 147  VAL 147  97  97  VAL VAL A . n 
A 1 148  PRO 148  98  98  PRO PRO A . n 
A 1 149  GLN 149  99  99  GLN GLN A . n 
A 1 150  SER 150  100 100 SER SER A . n 
A 1 151  MET 151  101 101 MET MET A . n 
A 1 152  GLN 152  102 102 GLN GLN A . n 
A 1 153  ASP 153  103 103 ASP ASP A . n 
A 1 154  LEU 154  104 104 LEU LEU A . n 
A 1 155  LEU 155  105 105 LEU LEU A . n 
A 1 156  GLY 156  106 106 GLY GLY A . n 
A 1 157  MET 157  107 107 MET MET A . n 
A 1 158  ASN 158  108 108 ASN ASN A . n 
A 1 159  ASN 159  109 109 ASN ASN A . n 
A 1 160  ASP 160  110 110 ASP ASP A . n 
A 1 161  PHE 161  111 111 PHE PHE A . n 
A 1 162  PRO 162  112 112 PRO PRO A . n 
A 1 163  PRO 163  113 113 PRO PRO A . n 
A 1 164  ARG 164  114 114 ARG ARG A . n 
A 1 165  ALA 165  115 115 ALA ALA A . n 
A 1 166  HIS 166  116 116 HIS HIS A . n 
A 1 167  CYS 167  117 117 CYS CYS A . n 
A 1 168  LEU 168  118 118 LEU LEU A . n 
A 1 169  VAL 169  119 119 VAL VAL A . n 
A 1 170  ARG 170  120 120 ARG ARG A . n 
A 1 171  TRP 171  121 121 TRP TRP A . n 
A 1 172  TYR 172  122 122 TYR TYR A . n 
A 1 173  GLY 173  123 123 GLY GLY A . n 
A 1 174  LEU 174  124 124 LEU LEU A . n 
A 1 175  ARG 175  125 125 ARG ARG A . n 
A 1 176  GLU 176  126 126 GLU GLU A . n 
A 1 177  PHE 177  127 127 PHE PHE A . n 
A 1 178  VAL 178  128 128 VAL VAL A . n 
A 1 179  VAL 179  129 129 VAL VAL A . n 
A 1 180  ILE 180  130 130 ILE ILE A . n 
A 1 181  ALA 181  131 131 ALA ALA A . n 
A 1 182  PRO 182  132 132 PRO PRO A . n 
A 1 183  ALA 183  133 133 ALA ALA A . n 
A 1 184  ALA 184  134 134 ALA ALA A . n 
A 1 185  HIS 185  135 135 HIS HIS A . n 
A 1 186  SER 186  136 136 SER SER A . n 
A 1 187  ASP 187  137 137 ASP ASP A . n 
A 1 188  ALA 188  138 138 ALA ALA A . n 
A 1 189  VAL 189  139 139 VAL VAL A . n 
A 1 190  LEU 190  140 140 LEU LEU A . n 
A 1 191  SER 191  141 141 SER SER A . n 
A 1 192  GLU 192  142 142 GLU GLU A . n 
A 1 193  SER 193  143 143 SER SER A . n 
A 1 194  LYS 194  144 144 LYS LYS A . n 
A 1 195  CYS 195  145 145 CYS CYS A . n 
A 1 196  ASN 196  146 146 ASN ASN A . n 
A 1 197  LEU 197  147 147 LEU LEU A . n 
A 1 198  LEU 198  148 148 LEU LEU A . n 
A 1 199  LEU 199  149 149 LEU LEU A . n 
A 1 200  SER 200  150 150 SER SER A . n 
A 1 201  SER 201  151 151 SER SER A . n 
A 1 202  VAL 202  152 152 VAL VAL A . n 
A 1 203  SER 203  153 153 SER SER A . n 
A 1 204  ILE 204  154 154 ILE ILE A . n 
A 1 205  ALA 205  155 155 ALA ALA A . n 
A 1 206  LEU 206  156 156 LEU LEU A . n 
A 1 207  GLY 207  157 157 GLY GLY A . n 
A 1 208  ASN 208  158 158 ASN ASN A . n 
A 1 209  THR 209  159 159 THR THR A . n 
A 1 210  GLY 210  160 160 GLY GLY A . n 
A 1 211  CYS 211  161 161 CYS CYS A . n 
A 1 212  GLN 212  162 162 GLN GLN A . n 
A 1 213  VAL 213  163 163 VAL VAL A . n 
A 1 214  PRO 214  164 164 PRO PRO A . n 
A 1 215  LEU 215  165 165 LEU LEU A . n 
A 1 216  PHE 216  166 166 PHE PHE A . n 
A 1 217  VAL 217  167 167 VAL VAL A . n 
A 1 218  GLN 218  168 168 GLN GLN A . n 
A 1 219  ILE 219  169 169 ILE ILE A . n 
A 1 220  HIS 220  170 170 HIS HIS A . n 
A 1 221  HIS 221  171 171 HIS HIS A . n 
A 1 222  LYS 222  172 172 LYS LYS A . n 
A 1 223  TRP 223  173 173 TRP TRP A . n 
A 1 224  ARG 224  174 174 ARG ARG A . n 
A 1 225  ARG 225  175 175 ARG ARG A . n 
A 1 226  MET 226  176 176 MET MET A . n 
A 1 227  TYR 227  177 177 TYR TYR A . n 
A 1 228  VAL 228  178 178 VAL VAL A . n 
A 1 229  GLY 229  179 179 GLY GLY A . n 
A 1 230  GLU 230  180 180 GLU GLU A . n 
A 1 231  CYS 231  181 181 CYS CYS A . n 
A 1 232  GLN 232  182 182 GLN GLN A . n 
A 1 233  GLY 233  183 183 GLY GLY A . n 
A 1 234  PRO 234  184 184 PRO PRO A . n 
A 1 235  GLY 235  185 185 GLY GLY A . n 
A 1 236  VAL 236  186 186 VAL VAL A . n 
A 1 237  ARG 237  187 187 ARG ARG A . n 
A 1 238  THR 238  188 188 THR THR A . n 
A 1 239  ASP 239  189 189 ASP ASP A . n 
A 1 240  PHE 240  190 190 PHE PHE A . n 
A 1 241  GLU 241  191 191 GLU GLU A . n 
A 1 242  MET 242  192 192 MET MET A . n 
A 1 243  VAL 243  193 193 VAL VAL A . n 
A 1 244  HIS 244  194 194 HIS HIS A . n 
A 1 245  LEU 245  195 195 LEU LEU A . n 
A 1 246  ARG 246  196 196 ARG ARG A . n 
A 1 247  LYS 247  197 197 LYS LYS A . n 
A 1 248  VAL 248  198 198 VAL VAL A . n 
A 1 249  PRO 249  199 199 PRO PRO A . n 
A 1 250  ASN 250  200 200 ASN ASN A . n 
A 1 251  GLN 251  201 201 GLN GLN A . n 
A 1 252  TYR 252  202 202 TYR TYR A . n 
A 1 253  THR 253  203 203 THR THR A . n 
A 1 254  HIS 254  204 204 HIS HIS A . n 
A 1 255  LEU 255  205 205 LEU LEU A . n 
A 1 256  SER 256  206 206 SER SER A . n 
A 1 257  GLY 257  207 207 GLY GLY A . n 
A 1 258  LEU 258  208 208 LEU LEU A . n 
A 1 259  LEU 259  209 209 LEU LEU A . n 
A 1 260  ASP 260  210 210 ASP ASP A . n 
A 1 261  ILE 261  211 211 ILE ILE A . n 
A 1 262  PHE 262  212 212 PHE PHE A . n 
A 1 263  LYS 263  213 213 LYS LYS A . n 
A 1 264  SER 264  214 214 SER SER A . n 
A 1 265  LYS 265  215 215 LYS LYS A . n 
A 1 266  ILE 266  216 216 ILE ILE A . n 
A 1 267  GLY 267  217 217 GLY GLY A . n 
A 1 268  CYS 268  218 218 CYS CYS A . n 
A 1 269  PRO 269  219 219 PRO PRO A . n 
A 1 270  LEU 270  220 220 LEU LEU A . n 
A 1 271  THR 271  221 221 THR THR A . n 
A 1 272  PRO 272  222 222 PRO PRO A . n 
A 1 273  LEU 273  223 223 LEU LEU A . n 
A 1 274  PRO 274  224 224 PRO PRO A . n 
A 1 275  PRO 275  225 225 PRO PRO A . n 
A 1 276  VAL 276  226 226 VAL VAL A . n 
A 1 277  SER 277  227 227 SER SER A . n 
A 1 278  ILE 278  228 228 ILE ILE A . n 
A 1 279  ALA 279  229 229 ALA ALA A . n 
A 1 280  ILE 280  230 230 ILE ILE A . n 
A 1 281  ARG 281  231 231 ARG ARG A . n 
A 1 282  PHE 282  232 232 PHE PHE A . n 
A 1 283  THR 283  233 233 THR THR A . n 
A 1 284  TYR 284  234 234 TYR TYR A . n 
A 1 285  VAL 285  235 235 VAL VAL A . n 
A 1 286  LEU 286  236 236 LEU LEU A . n 
A 1 287  GLN 287  237 237 GLN GLN A . n 
A 1 288  ASP 288  238 238 ASP ASP A . n 
A 1 289  TRP 289  239 239 TRP TRP A . n 
A 1 290  GLN 290  240 240 GLN GLN A . n 
A 1 291  GLN 291  241 241 GLN GLN A . n 
A 1 292  TYR 292  242 ?   ?   ?   A . n 
A 1 293  PHE 293  243 ?   ?   ?   A . n 
A 1 294  TRP 294  244 ?   ?   ?   A . n 
A 1 295  PRO 295  245 ?   ?   ?   A . n 
A 1 296  GLN 296  246 ?   ?   ?   A . n 
A 1 297  GLN 297  247 ?   ?   ?   A . n 
A 1 298  PRO 298  248 ?   ?   ?   A . n 
A 1 299  PRO 299  249 ?   ?   ?   A . n 
A 1 300  ASP 300  250 ?   ?   ?   A . n 
A 1 301  ILE 301  251 ?   ?   ?   A . n 
A 1 302  ASP 302  252 ?   ?   ?   A . n 
A 1 303  ALA 303  253 ?   ?   ?   A . n 
A 1 304  LEU 304  254 ?   ?   ?   A . n 
A 1 305  VAL 305  255 ?   ?   ?   A . n 
A 1 306  GLY 306  256 ?   ?   ?   A . n 
A 1 307  GLY 307  257 ?   ?   ?   A . n 
A 1 308  GLU 308  258 ?   ?   ?   A . n 
A 1 309  VAL 309  259 ?   ?   ?   A . n 
A 1 310  GLY 310  260 ?   ?   ?   A . n 
A 1 311  GLY 311  261 ?   ?   ?   A . n 
A 1 312  LEU 312  262 ?   ?   ?   A . n 
A 1 313  GLU 313  263 ?   ?   ?   A . n 
A 1 314  PHE 314  264 264 PHE PHE A . n 
A 1 315  GLY 315  265 265 GLY GLY A . n 
A 1 316  LYS 316  266 266 LYS LYS A . n 
A 1 317  LEU 317  267 267 LEU LEU A . n 
A 1 318  PRO 318  268 268 PRO PRO A . n 
A 1 319  PHE 319  269 269 PHE PHE A . n 
A 1 320  GLY 320  270 270 GLY GLY A . n 
A 1 321  ALA 321  271 271 ALA ALA A . n 
A 1 322  CYS 322  272 272 CYS CYS A . n 
A 1 323  GLU 323  273 273 GLU GLU A . n 
A 1 324  ASP 324  274 274 ASP ASP A . n 
A 1 325  PRO 325  275 275 PRO PRO A . n 
A 1 326  ILE 326  276 276 ILE ILE A . n 
A 1 327  SER 327  277 277 SER SER A . n 
A 1 328  GLU 328  278 278 GLU GLU A . n 
A 1 329  LEU 329  279 279 LEU LEU A . n 
A 1 330  HIS 330  280 280 HIS HIS A . n 
A 1 331  LEU 331  281 281 LEU LEU A . n 
A 1 332  ALA 332  282 282 ALA ALA A . n 
A 1 333  THR 333  283 283 THR THR A . n 
A 1 334  THR 334  284 284 THR THR A . n 
A 1 335  TRP 335  285 285 TRP TRP A . n 
A 1 336  PRO 336  286 286 PRO PRO A . n 
A 1 337  HIS 337  287 287 HIS HIS A . n 
A 1 338  LEU 338  288 288 LEU LEU A . n 
A 1 339  THR 339  289 289 THR THR A . n 
A 1 340  GLU 340  290 290 GLU GLU A . n 
A 1 341  GLY 341  291 291 GLY GLY A . n 
A 1 342  ILE 342  292 292 ILE ILE A . n 
A 1 343  ILE 343  293 293 ILE ILE A . n 
A 1 344  VAL 344  294 294 VAL VAL A . n 
A 1 345  ASP 345  295 295 ASP ASP A . n 
A 1 346  ASN 346  296 296 ASN ASN A . n 
A 1 347  ASP 347  297 297 ASP ASP A . n 
A 1 348  VAL 348  298 298 VAL VAL A . n 
A 1 349  TYR 349  299 299 TYR TYR A . n 
A 1 350  SER 350  300 300 SER SER A . n 
A 1 351  ASP 351  301 301 ASP ASP A . n 
A 1 352  LEU 352  302 302 LEU LEU A . n 
A 1 353  ASP 353  303 303 ASP ASP A . n 
A 1 354  PRO 354  304 304 PRO PRO A . n 
A 1 355  ILE 355  305 305 ILE ILE A . n 
A 1 356  GLN 356  306 306 GLN GLN A . n 
A 1 357  ALA 357  307 307 ALA ALA A . n 
A 1 358  PRO 358  308 308 PRO PRO A . n 
A 1 359  HIS 359  309 309 HIS HIS A . n 
A 1 360  TRP 360  310 310 TRP TRP A . n 
A 1 361  SER 361  311 311 SER SER A . n 
A 1 362  VAL 362  312 312 VAL VAL A . n 
A 1 363  ARG 363  313 313 ARG ARG A . n 
A 1 364  VAL 364  314 314 VAL VAL A . n 
A 1 365  ARG 365  315 315 ARG ARG A . n 
A 1 366  LYS 366  316 316 LYS LYS A . n 
A 1 367  ALA 367  317 317 ALA ALA A . n 
A 1 368  GLU 368  318 318 GLU GLU A . n 
A 1 369  ASN 369  319 319 ASN ASN A . n 
A 1 370  PRO 370  320 320 PRO PRO A . n 
A 1 371  GLN 371  321 321 GLN GLN A . n 
A 1 372  CYS 372  322 322 CYS CYS A . n 
A 1 373  LEU 373  323 323 LEU LEU A . n 
A 1 374  LEU 374  324 324 LEU LEU A . n 
A 1 375  GLY 375  325 325 GLY GLY A . n 
A 1 376  ASP 376  326 326 ASP ASP A . n 
A 1 377  PHE 377  327 327 PHE PHE A . n 
A 1 378  VAL 378  328 328 VAL VAL A . n 
A 1 379  THR 379  329 329 THR THR A . n 
A 1 380  GLU 380  330 330 GLU GLU A . n 
A 1 381  PHE 381  331 331 PHE PHE A . n 
A 1 382  PHE 382  332 332 PHE PHE A . n 
A 1 383  LYS 383  333 ?   ?   ?   A . n 
A 1 384  ILE 384  334 ?   ?   ?   A . n 
A 1 385  CYS 385  335 ?   ?   ?   A . n 
A 1 386  ARG 386  336 ?   ?   ?   A . n 
A 1 387  ARG 387  337 ?   ?   ?   A . n 
A 1 388  LYS 388  338 ?   ?   ?   A . n 
A 1 389  GLU 389  339 ?   ?   ?   A . n 
A 1 390  SER 390  340 ?   ?   ?   A . n 
A 1 391  THR 391  341 ?   ?   ?   A . n 
A 1 392  ASP 392  342 ?   ?   ?   A . n 
A 1 393  GLU 393  343 ?   ?   ?   A . n 
A 1 394  ILE 394  344 ?   ?   ?   A . n 
A 1 395  LEU 395  345 ?   ?   ?   A . n 
A 1 396  GLY 396  346 ?   ?   ?   A . n 
A 1 397  ARG 397  347 ?   ?   ?   A . n 
A 1 398  SER 398  348 ?   ?   ?   A . n 
A 1 399  ALA 399  349 ?   ?   ?   A . n 
A 1 400  PHE 400  350 ?   ?   ?   A . n 
A 1 401  GLU 401  351 ?   ?   ?   A . n 
A 1 402  GLU 402  352 ?   ?   ?   A . n 
A 1 403  GLU 403  353 ?   ?   ?   A . n 
A 1 404  GLY 404  354 ?   ?   ?   A . n 
A 1 405  LYS 405  355 ?   ?   ?   A . n 
A 1 406  GLU 406  356 ?   ?   ?   A . n 
A 1 407  THR 407  357 ?   ?   ?   A . n 
A 1 408  ALA 408  358 ?   ?   ?   A . n 
A 1 409  ASP 409  359 ?   ?   ?   A . n 
A 1 410  ILE 410  360 ?   ?   ?   A . n 
A 1 411  THR 411  361 ?   ?   ?   A . n 
A 1 412  HIS 412  362 ?   ?   ?   A . n 
A 1 413  ALA 413  363 ?   ?   ?   A . n 
A 1 414  LEU 414  364 ?   ?   ?   A . n 
A 1 415  SER 415  365 ?   ?   ?   A . n 
A 1 416  LYS 416  366 ?   ?   ?   A . n 
A 1 417  LEU 417  367 ?   ?   ?   A . n 
A 1 418  THR 418  368 ?   ?   ?   A . n 
A 1 419  GLU 419  369 ?   ?   ?   A . n 
A 1 420  PRO 420  370 ?   ?   ?   A . n 
A 1 421  ALA 421  371 ?   ?   ?   A . n 
A 1 422  SER 422  372 ?   ?   ?   A . n 
A 1 423  VAL 423  373 ?   ?   ?   A . n 
A 1 424  PRO 424  374 ?   ?   ?   A . n 
A 1 425  ILE 425  375 ?   ?   ?   A . n 
A 1 426  HIS 426  376 ?   ?   ?   A . n 
A 1 427  LYS 427  377 ?   ?   ?   A . n 
A 1 428  LEU 428  378 ?   ?   ?   A . n 
A 1 429  SER 429  379 ?   ?   ?   A . n 
A 1 430  VAL 430  380 ?   ?   ?   A . n 
A 1 431  SER 431  381 ?   ?   ?   A . n 
A 1 432  ASN 432  382 ?   ?   ?   A . n 
A 1 433  MET 433  383 ?   ?   ?   A . n 
A 1 434  VAL 434  384 ?   ?   ?   A . n 
A 1 435  HIS 435  385 ?   ?   ?   A . n 
A 1 436  THR 436  386 ?   ?   ?   A . n 
A 1 437  ALA 437  387 ?   ?   ?   A . n 
A 1 438  LYS 438  388 ?   ?   ?   A . n 
A 1 439  LYS 439  389 ?   ?   ?   A . n 
A 1 440  LYS 440  390 ?   ?   ?   A . n 
A 1 441  ILE 441  391 ?   ?   ?   A . n 
A 1 442  ARG 442  392 ?   ?   ?   A . n 
A 1 443  LYS 443  393 ?   ?   ?   A . n 
A 1 444  HIS 444  394 ?   ?   ?   A . n 
A 1 445  ARG 445  395 ?   ?   ?   A . n 
A 1 446  GLY 446  396 ?   ?   ?   A . n 
A 1 447  VAL 447  397 ?   ?   ?   A . n 
A 1 448  GLU 448  398 ?   ?   ?   A . n 
A 1 449  GLU 449  399 ?   ?   ?   A . n 
A 1 450  SER 450  400 ?   ?   ?   A . n 
A 1 451  PRO 451  401 ?   ?   ?   A . n 
A 1 452  LEU 452  402 ?   ?   ?   A . n 
A 1 453  ASN 453  403 ?   ?   ?   A . n 
A 1 454  ASN 454  404 ?   ?   ?   A . n 
A 1 455  ASP 455  405 ?   ?   ?   A . n 
A 1 456  VAL 456  406 ?   ?   ?   A . n 
A 1 457  LEU 457  407 ?   ?   ?   A . n 
A 1 458  ASN 458  408 ?   ?   ?   A . n 
A 1 459  THR 459  409 ?   ?   ?   A . n 
A 1 460  ILE 460  410 ?   ?   ?   A . n 
A 1 461  LEU 461  411 ?   ?   ?   A . n 
A 1 462  LEU 462  412 ?   ?   ?   A . n 
A 1 463  PHE 463  413 ?   ?   ?   A . n 
A 1 464  LEU 464  414 ?   ?   ?   A . n 
A 1 465  PHE 465  415 ?   ?   ?   A . n 
A 1 466  PRO 466  416 ?   ?   ?   A . n 
A 1 467  ASP 467  417 ?   ?   ?   A . n 
A 1 468  ALA 468  418 ?   ?   ?   A . n 
A 1 469  VAL 469  419 ?   ?   ?   A . n 
A 1 470  SER 470  420 ?   ?   ?   A . n 
A 1 471  GLU 471  421 ?   ?   ?   A . n 
A 1 472  LYS 472  422 ?   ?   ?   A . n 
A 1 473  PRO 473  423 ?   ?   ?   A . n 
A 1 474  LEU 474  424 ?   ?   ?   A . n 
A 1 475  ASP 475  425 ?   ?   ?   A . n 
A 1 476  GLY 476  426 ?   ?   ?   A . n 
A 1 477  THR 477  427 ?   ?   ?   A . n 
A 1 478  THR 478  428 ?   ?   ?   A . n 
A 1 479  SER 479  429 ?   ?   ?   A . n 
A 1 480  THR 480  430 ?   ?   ?   A . n 
A 1 481  ASP 481  431 ?   ?   ?   A . n 
A 1 482  ASN 482  432 ?   ?   ?   A . n 
A 1 483  ASN 483  433 ?   ?   ?   A . n 
A 1 484  ASN 484  434 ?   ?   ?   A . n 
A 1 485  PRO 485  435 ?   ?   ?   A . n 
A 1 486  PRO 486  436 ?   ?   ?   A . n 
A 1 487  SER 487  437 ?   ?   ?   A . n 
A 1 488  GLU 488  438 ?   ?   ?   A . n 
A 1 489  SER 489  439 ?   ?   ?   A . n 
A 1 490  GLU 490  440 ?   ?   ?   A . n 
A 1 491  ASP 491  441 ?   ?   ?   A . n 
A 1 492  TYR 492  442 ?   ?   ?   A . n 
A 1 493  ASN 493  443 ?   ?   ?   A . n 
A 1 494  LEU 494  444 ?   ?   ?   A . n 
A 1 495  TYR 495  445 ?   ?   ?   A . n 
A 1 496  ASN 496  446 ?   ?   ?   A . n 
A 1 497  GLN 497  447 ?   ?   ?   A . n 
A 1 498  PHE 498  448 ?   ?   ?   A . n 
A 1 499  LYS 499  449 ?   ?   ?   A . n 
A 1 500  SER 500  450 ?   ?   ?   A . n 
A 1 501  ALA 501  451 ?   ?   ?   A . n 
A 1 502  PRO 502  452 ?   ?   ?   A . n 
A 1 503  SER 503  453 ?   ?   ?   A . n 
A 1 504  ASP 504  454 ?   ?   ?   A . n 
A 1 505  SER 505  455 ?   ?   ?   A . n 
A 1 506  LEU 506  456 ?   ?   ?   A . n 
A 1 507  THR 507  457 ?   ?   ?   A . n 
A 1 508  TYR 508  458 ?   ?   ?   A . n 
A 1 509  LYS 509  459 ?   ?   ?   A . n 
A 1 510  LEU 510  460 ?   ?   ?   A . n 
A 1 511  ALA 511  461 ?   ?   ?   A . n 
A 1 512  LEU 512  462 ?   ?   ?   A . n 
A 1 513  CYS 513  463 ?   ?   ?   A . n 
A 1 514  LEU 514  464 ?   ?   ?   A . n 
A 1 515  CYS 515  465 ?   ?   ?   A . n 
A 1 516  MET 516  466 ?   ?   ?   A . n 
A 1 517  ILE 517  467 ?   ?   ?   A . n 
A 1 518  ASN 518  468 ?   ?   ?   A . n 
A 1 519  PHE 519  469 ?   ?   ?   A . n 
A 1 520  TYR 520  470 ?   ?   ?   A . n 
A 1 521  HIS 521  471 ?   ?   ?   A . n 
A 1 522  GLY 522  472 ?   ?   ?   A . n 
A 1 523  GLY 523  473 ?   ?   ?   A . n 
A 1 524  LEU 524  474 ?   ?   ?   A . n 
A 1 525  LYS 525  475 ?   ?   ?   A . n 
A 1 526  GLY 526  476 ?   ?   ?   A . n 
A 1 527  VAL 527  477 ?   ?   ?   A . n 
A 1 528  ALA 528  478 ?   ?   ?   A . n 
A 1 529  HIS 529  479 ?   ?   ?   A . n 
A 1 530  LEU 530  480 ?   ?   ?   A . n 
A 1 531  TRP 531  481 ?   ?   ?   A . n 
A 1 532  GLN 532  482 ?   ?   ?   A . n 
A 1 533  GLU 533  483 ?   ?   ?   A . n 
A 1 534  PHE 534  484 ?   ?   ?   A . n 
A 1 535  VAL 535  485 ?   ?   ?   A . n 
A 1 536  LEU 536  486 ?   ?   ?   A . n 
A 1 537  GLU 537  487 ?   ?   ?   A . n 
A 1 538  MET 538  488 ?   ?   ?   A . n 
A 1 539  ARG 539  489 ?   ?   ?   A . n 
A 1 540  PHE 540  490 ?   ?   ?   A . n 
A 1 541  ARG 541  491 ?   ?   ?   A . n 
A 1 542  TRP 542  492 ?   ?   ?   A . n 
A 1 543  GLU 543  493 ?   ?   ?   A . n 
A 1 544  ASN 544  494 ?   ?   ?   A . n 
A 1 545  ASN 545  495 ?   ?   ?   A . n 
A 1 546  PHE 546  496 ?   ?   ?   A . n 
A 1 547  LEU 547  497 ?   ?   ?   A . n 
A 1 548  ILE 548  498 ?   ?   ?   A . n 
A 1 549  PRO 549  499 ?   ?   ?   A . n 
A 1 550  GLY 550  500 ?   ?   ?   A . n 
A 1 551  LEU 551  501 ?   ?   ?   A . n 
A 1 552  ALA 552  502 ?   ?   ?   A . n 
A 1 553  SER 553  503 ?   ?   ?   A . n 
A 1 554  GLY 554  504 ?   ?   ?   A . n 
A 1 555  PRO 555  505 ?   ?   ?   A . n 
A 1 556  PRO 556  506 ?   ?   ?   A . n 
A 1 557  ASP 557  507 ?   ?   ?   A . n 
A 1 558  LEU 558  508 ?   ?   ?   A . n 
A 1 559  ARG 559  509 ?   ?   ?   A . n 
A 1 560  CYS 560  510 ?   ?   ?   A . n 
A 1 561  CYS 561  511 ?   ?   ?   A . n 
A 1 562  LEU 562  512 ?   ?   ?   A . n 
A 1 563  LEU 563  513 ?   ?   ?   A . n 
A 1 564  HIS 564  514 ?   ?   ?   A . n 
A 1 565  GLN 565  515 ?   ?   ?   A . n 
A 1 566  LYS 566  516 ?   ?   ?   A . n 
A 1 567  LEU 567  517 ?   ?   ?   A . n 
A 1 568  GLN 568  518 ?   ?   ?   A . n 
A 1 569  MET 569  519 ?   ?   ?   A . n 
A 1 570  LEU 570  520 ?   ?   ?   A . n 
A 1 571  ASN 571  521 ?   ?   ?   A . n 
A 1 572  CYS 572  522 ?   ?   ?   A . n 
A 1 573  CYS 573  523 ?   ?   ?   A . n 
A 1 574  ILE 574  524 ?   ?   ?   A . n 
A 1 575  GLU 575  525 ?   ?   ?   A . n 
A 1 576  ARG 576  526 ?   ?   ?   A . n 
A 1 577  LYS 577  527 ?   ?   ?   A . n 
A 1 578  LYS 578  528 ?   ?   ?   A . n 
A 1 579  ALA 579  529 ?   ?   ?   A . n 
A 1 580  ARG 580  530 ?   ?   ?   A . n 
A 1 581  ASP 581  531 ?   ?   ?   A . n 
A 1 582  GLU 582  532 ?   ?   ?   A . n 
A 1 583  GLY 583  533 ?   ?   ?   A . n 
A 1 584  LYS 584  534 ?   ?   ?   A . n 
A 1 585  LYS 585  535 ?   ?   ?   A . n 
A 1 586  THR 586  536 ?   ?   ?   A . n 
A 1 587  SER 587  537 ?   ?   ?   A . n 
A 1 588  ALA 588  538 ?   ?   ?   A . n 
A 1 589  SER 589  539 ?   ?   ?   A . n 
A 1 590  ASP 590  540 ?   ?   ?   A . n 
A 1 591  VAL 591  541 ?   ?   ?   A . n 
A 1 592  THR 592  542 ?   ?   ?   A . n 
A 1 593  ASN 593  543 ?   ?   ?   A . n 
A 1 594  ILE 594  544 ?   ?   ?   A . n 
A 1 595  TYR 595  545 ?   ?   ?   A . n 
A 1 596  PRO 596  546 ?   ?   ?   A . n 
A 1 597  GLY 597  547 ?   ?   ?   A . n 
A 1 598  ASP 598  548 ?   ?   ?   A . n 
A 1 599  ALA 599  549 ?   ?   ?   A . n 
A 1 600  GLY 600  550 ?   ?   ?   A . n 
A 1 601  LYS 601  551 ?   ?   ?   A . n 
A 1 602  ALA 602  552 ?   ?   ?   A . n 
A 1 603  GLY 603  553 ?   ?   ?   A . n 
A 1 604  ASP 604  554 ?   ?   ?   A . n 
A 1 605  GLN 605  555 ?   ?   ?   A . n 
A 1 606  LEU 606  556 ?   ?   ?   A . n 
A 1 607  VAL 607  557 ?   ?   ?   A . n 
A 1 608  PRO 608  558 ?   ?   ?   A . n 
A 1 609  ASP 609  559 ?   ?   ?   A . n 
A 1 610  ASN 610  560 ?   ?   ?   A . n 
A 1 611  LEU 611  561 ?   ?   ?   A . n 
A 1 612  LYS 612  562 ?   ?   ?   A . n 
A 1 613  GLU 613  563 ?   ?   ?   A . n 
A 1 614  THR 614  564 ?   ?   ?   A . n 
A 1 615  ASP 615  565 ?   ?   ?   A . n 
A 1 616  LYS 616  566 ?   ?   ?   A . n 
A 1 617  GLU 617  567 ?   ?   ?   A . n 
A 1 618  LYS 618  568 ?   ?   ?   A . n 
A 1 619  GLY 619  569 ?   ?   ?   A . n 
A 1 620  GLU 620  570 ?   ?   ?   A . n 
A 1 621  VAL 621  571 ?   ?   ?   A . n 
A 1 622  GLY 622  572 ?   ?   ?   A . n 
A 1 623  LYS 623  573 ?   ?   ?   A . n 
A 1 624  SER 624  574 ?   ?   ?   A . n 
A 1 625  TRP 625  575 ?   ?   ?   A . n 
A 1 626  ASP 626  576 ?   ?   ?   A . n 
A 1 627  SER 627  577 ?   ?   ?   A . n 
A 1 628  TRP 628  578 ?   ?   ?   A . n 
A 1 629  SER 629  579 ?   ?   ?   A . n 
A 1 630  ASP 630  580 ?   ?   ?   A . n 
A 1 631  SER 631  581 ?   ?   ?   A . n 
A 1 632  GLU 632  582 ?   ?   ?   A . n 
A 1 633  GLU 633  583 ?   ?   ?   A . n 
A 1 634  GLU 634  584 ?   ?   ?   A . n 
A 1 635  PHE 635  585 ?   ?   ?   A . n 
A 1 636  PHE 636  586 ?   ?   ?   A . n 
A 1 637  GLU 637  587 ?   ?   ?   A . n 
A 1 638  CYS 638  588 ?   ?   ?   A . n 
A 1 639  LEU 639  589 ?   ?   ?   A . n 
A 1 640  SER 640  590 ?   ?   ?   A . n 
A 1 641  ASP 641  591 ?   ?   ?   A . n 
A 1 642  THR 642  592 ?   ?   ?   A . n 
A 1 643  GLU 643  593 ?   ?   ?   A . n 
A 1 644  GLU 644  594 ?   ?   ?   A . n 
A 1 645  LEU 645  595 ?   ?   ?   A . n 
A 1 646  LYS 646  596 ?   ?   ?   A . n 
A 1 647  GLY 647  597 ?   ?   ?   A . n 
A 1 648  ASN 648  598 ?   ?   ?   A . n 
A 1 649  GLY 649  599 ?   ?   ?   A . n 
A 1 650  GLN 650  600 ?   ?   ?   A . n 
A 1 651  GLU 651  601 ?   ?   ?   A . n 
A 1 652  SER 652  602 ?   ?   ?   A . n 
A 1 653  GLY 653  603 ?   ?   ?   A . n 
A 1 654  LYS 654  604 ?   ?   ?   A . n 
A 1 655  LYS 655  605 ?   ?   ?   A . n 
A 1 656  GLY 656  606 ?   ?   ?   A . n 
A 1 657  GLY 657  607 ?   ?   ?   A . n 
A 1 658  PRO 658  608 ?   ?   ?   A . n 
A 1 659  LYS 659  609 ?   ?   ?   A . n 
A 1 660  GLU 660  610 ?   ?   ?   A . n 
A 1 661  MET 661  611 ?   ?   ?   A . n 
A 1 662  ALA 662  612 ?   ?   ?   A . n 
A 1 663  ASN 663  613 ?   ?   ?   A . n 
A 1 664  LEU 664  614 ?   ?   ?   A . n 
A 1 665  ARG 665  615 ?   ?   ?   A . n 
A 1 666  PRO 666  616 ?   ?   ?   A . n 
A 1 667  GLU 667  617 ?   ?   ?   A . n 
A 1 668  GLY 668  618 ?   ?   ?   A . n 
A 1 669  ARG 669  619 ?   ?   ?   A . n 
A 1 670  LEU 670  620 ?   ?   ?   A . n 
A 1 671  TYR 671  621 ?   ?   ?   A . n 
A 1 672  GLN 672  622 ?   ?   ?   A . n 
A 1 673  HIS 673  623 ?   ?   ?   A . n 
A 1 674  GLY 674  624 ?   ?   ?   A . n 
A 1 675  LYS 675  625 ?   ?   ?   A . n 
A 1 676  LEU 676  626 ?   ?   ?   A . n 
A 1 677  THR 677  627 ?   ?   ?   A . n 
A 1 678  LEU 678  628 ?   ?   ?   A . n 
A 1 679  LEU 679  629 ?   ?   ?   A . n 
A 1 680  HIS 680  630 ?   ?   ?   A . n 
A 1 681  ASN 681  631 ?   ?   ?   A . n 
A 1 682  GLY 682  632 ?   ?   ?   A . n 
A 1 683  GLU 683  633 ?   ?   ?   A . n 
A 1 684  PRO 684  634 ?   ?   ?   A . n 
A 1 685  LEU 685  635 ?   ?   ?   A . n 
A 1 686  TYR 686  636 ?   ?   ?   A . n 
A 1 687  ILE 687  637 ?   ?   ?   A . n 
A 1 688  PRO 688  638 ?   ?   ?   A . n 
A 1 689  VAL 689  639 ?   ?   ?   A . n 
A 1 690  THR 690  640 ?   ?   ?   A . n 
A 1 691  GLN 691  641 ?   ?   ?   A . n 
A 1 692  GLU 692  642 ?   ?   ?   A . n 
A 1 693  PRO 693  643 ?   ?   ?   A . n 
A 1 694  ALA 694  644 ?   ?   ?   A . n 
A 1 695  PRO 695  645 ?   ?   ?   A . n 
A 1 696  MET 696  646 ?   ?   ?   A . n 
A 1 697  THR 697  647 ?   ?   ?   A . n 
A 1 698  GLU 698  648 ?   ?   ?   A . n 
A 1 699  ASP 699  649 ?   ?   ?   A . n 
A 1 700  LEU 700  650 ?   ?   ?   A . n 
A 1 701  LEU 701  651 ?   ?   ?   A . n 
A 1 702  GLU 702  652 ?   ?   ?   A . n 
A 1 703  GLU 703  653 ?   ?   ?   A . n 
A 1 704  GLN 704  654 ?   ?   ?   A . n 
A 1 705  SER 705  655 ?   ?   ?   A . n 
A 1 706  GLU 706  656 ?   ?   ?   A . n 
A 1 707  VAL 707  657 ?   ?   ?   A . n 
A 1 708  LEU 708  658 ?   ?   ?   A . n 
A 1 709  ALA 709  659 ?   ?   ?   A . n 
A 1 710  LYS 710  660 ?   ?   ?   A . n 
A 1 711  LEU 711  661 ?   ?   ?   A . n 
A 1 712  GLY 712  662 ?   ?   ?   A . n 
A 1 713  THR 713  663 ?   ?   ?   A . n 
A 1 714  SER 714  664 ?   ?   ?   A . n 
A 1 715  ALA 715  665 ?   ?   ?   A . n 
A 1 716  GLU 716  666 ?   ?   ?   A . n 
A 1 717  GLY 717  667 ?   ?   ?   A . n 
A 1 718  ALA 718  668 ?   ?   ?   A . n 
A 1 719  HIS 719  669 ?   ?   ?   A . n 
A 1 720  LEU 720  670 ?   ?   ?   A . n 
A 1 721  ARG 721  671 ?   ?   ?   A . n 
A 1 722  ALA 722  672 ?   ?   ?   A . n 
A 1 723  ARG 723  673 ?   ?   ?   A . n 
A 1 724  MET 724  674 ?   ?   ?   A . n 
A 1 725  GLN 725  675 ?   ?   ?   A . n 
A 1 726  SER 726  676 ?   ?   ?   A . n 
A 1 727  ALA 727  677 ?   ?   ?   A . n 
A 1 728  CYS 728  678 ?   ?   ?   A . n 
A 1 729  LEU 729  679 ?   ?   ?   A . n 
A 1 730  LEU 730  680 ?   ?   ?   A . n 
A 1 731  SER 731  681 ?   ?   ?   A . n 
A 1 732  ASP 732  682 ?   ?   ?   A . n 
A 1 733  MET 733  683 ?   ?   ?   A . n 
A 1 734  GLU 734  684 ?   ?   ?   A . n 
A 1 735  SER 735  685 ?   ?   ?   A . n 
A 1 736  PHE 736  686 ?   ?   ?   A . n 
A 1 737  LYS 737  687 ?   ?   ?   A . n 
A 1 738  ALA 738  688 ?   ?   ?   A . n 
A 1 739  ALA 739  689 ?   ?   ?   A . n 
A 1 740  ASN 740  690 ?   ?   ?   A . n 
A 1 741  PRO 741  691 ?   ?   ?   A . n 
A 1 742  GLY 742  692 ?   ?   ?   A . n 
A 1 743  CYS 743  693 ?   ?   ?   A . n 
A 1 744  SER 744  694 ?   ?   ?   A . n 
A 1 745  LEU 745  695 ?   ?   ?   A . n 
A 1 746  GLU 746  696 ?   ?   ?   A . n 
A 1 747  ASP 747  697 ?   ?   ?   A . n 
A 1 748  PHE 748  698 ?   ?   ?   A . n 
A 1 749  VAL 749  699 ?   ?   ?   A . n 
A 1 750  ARG 750  700 ?   ?   ?   A . n 
A 1 751  TRP 751  701 ?   ?   ?   A . n 
A 1 752  TYR 752  702 ?   ?   ?   A . n 
A 1 753  SER 753  703 ?   ?   ?   A . n 
A 1 754  PRO 754  704 ?   ?   ?   A . n 
A 1 755  ARG 755  705 ?   ?   ?   A . n 
A 1 756  ASP 756  706 ?   ?   ?   A . n 
A 1 757  TYR 757  707 ?   ?   ?   A . n 
A 1 758  ILE 758  708 ?   ?   ?   A . n 
A 1 759  GLU 759  709 ?   ?   ?   A . n 
A 1 760  GLU 760  710 ?   ?   ?   A . n 
A 1 761  GLU 761  711 ?   ?   ?   A . n 
A 1 762  VAL 762  712 ?   ?   ?   A . n 
A 1 763  ILE 763  713 ?   ?   ?   A . n 
A 1 764  ASP 764  714 ?   ?   ?   A . n 
A 1 765  GLU 765  715 ?   ?   ?   A . n 
A 1 766  LYS 766  716 ?   ?   ?   A . n 
A 1 767  GLY 767  717 ?   ?   ?   A . n 
A 1 768  ASN 768  718 ?   ?   ?   A . n 
A 1 769  VAL 769  719 ?   ?   ?   A . n 
A 1 770  VAL 770  720 ?   ?   ?   A . n 
A 1 771  LEU 771  721 ?   ?   ?   A . n 
A 1 772  LYS 772  722 ?   ?   ?   A . n 
A 1 773  GLY 773  723 ?   ?   ?   A . n 
A 1 774  GLU 774  724 ?   ?   ?   A . n 
A 1 775  LEU 775  725 ?   ?   ?   A . n 
A 1 776  SER 776  726 ?   ?   ?   A . n 
A 1 777  ALA 777  727 ?   ?   ?   A . n 
A 1 778  ARG 778  728 ?   ?   ?   A . n 
A 1 779  MET 779  729 ?   ?   ?   A . n 
A 1 780  LYS 780  730 ?   ?   ?   A . n 
A 1 781  ILE 781  731 ?   ?   ?   A . n 
A 1 782  PRO 782  732 ?   ?   ?   A . n 
A 1 783  SER 783  733 ?   ?   ?   A . n 
A 1 784  ASN 784  734 ?   ?   ?   A . n 
A 1 785  MET 785  735 ?   ?   ?   A . n 
A 1 786  TRP 786  736 ?   ?   ?   A . n 
A 1 787  VAL 787  737 ?   ?   ?   A . n 
A 1 788  GLU 788  738 ?   ?   ?   A . n 
A 1 789  ALA 789  739 ?   ?   ?   A . n 
A 1 790  TRP 790  740 ?   ?   ?   A . n 
A 1 791  GLU 791  741 ?   ?   ?   A . n 
A 1 792  THR 792  742 ?   ?   ?   A . n 
A 1 793  ALA 793  743 ?   ?   ?   A . n 
A 1 794  LYS 794  744 ?   ?   ?   A . n 
A 1 795  PRO 795  745 ?   ?   ?   A . n 
A 1 796  ILE 796  746 ?   ?   ?   A . n 
A 1 797  PRO 797  747 ?   ?   ?   A . n 
A 1 798  ALA 798  748 ?   ?   ?   A . n 
A 1 799  ARG 799  749 ?   ?   ?   A . n 
A 1 800  ARG 800  750 ?   ?   ?   A . n 
A 1 801  GLN 801  751 ?   ?   ?   A . n 
A 1 802  ARG 802  752 ?   ?   ?   A . n 
A 1 803  ARG 803  753 ?   ?   ?   A . n 
A 1 804  LEU 804  754 ?   ?   ?   A . n 
A 1 805  PHE 805  755 ?   ?   ?   A . n 
A 1 806  ASP 806  756 ?   ?   ?   A . n 
A 1 807  ASP 807  757 ?   ?   ?   A . n 
A 1 808  THR 808  758 ?   ?   ?   A . n 
A 1 809  ARG 809  759 ?   ?   ?   A . n 
A 1 810  GLU 810  760 ?   ?   ?   A . n 
A 1 811  ALA 811  761 ?   ?   ?   A . n 
A 1 812  GLU 812  762 ?   ?   ?   A . n 
A 1 813  LYS 813  763 ?   ?   ?   A . n 
A 1 814  VAL 814  764 ?   ?   ?   A . n 
A 1 815  LEU 815  765 ?   ?   ?   A . n 
A 1 816  HIS 816  766 ?   ?   ?   A . n 
A 1 817  TYR 817  767 ?   ?   ?   A . n 
A 1 818  LEU 818  768 ?   ?   ?   A . n 
A 1 819  ALA 819  769 ?   ?   ?   A . n 
A 1 820  ILE 820  770 ?   ?   ?   A . n 
A 1 821  GLN 821  771 ?   ?   ?   A . n 
A 1 822  LYS 822  772 ?   ?   ?   A . n 
A 1 823  PRO 823  773 ?   ?   ?   A . n 
A 1 824  ALA 824  774 ?   ?   ?   A . n 
A 1 825  ASP 825  775 ?   ?   ?   A . n 
A 1 826  LEU 826  776 ?   ?   ?   A . n 
A 1 827  ALA 827  777 ?   ?   ?   A . n 
A 1 828  ARG 828  778 ?   ?   ?   A . n 
A 1 829  HIS 829  779 ?   ?   ?   A . n 
A 1 830  LEU 830  780 ?   ?   ?   A . n 
A 1 831  LEU 831  781 ?   ?   ?   A . n 
A 1 832  PRO 832  782 782 PRO PRO A . n 
A 1 833  CYS 833  783 783 CYS CYS A . n 
A 1 834  VAL 834  784 784 VAL VAL A . n 
A 1 835  ILE 835  785 785 ILE ILE A . n 
A 1 836  HIS 836  786 786 HIS HIS A . n 
A 1 837  ALA 837  787 787 ALA ALA A . n 
A 1 838  ALA 838  788 788 ALA ALA A . n 
A 1 839  VAL 839  789 789 VAL VAL A . n 
A 1 840  LEU 840  790 790 LEU LEU A . n 
A 1 841  LYS 841  791 791 LYS LYS A . n 
A 1 842  VAL 842  792 792 VAL VAL A . n 
A 1 843  LYS 843  793 793 LYS LYS A . n 
A 1 844  GLU 844  794 794 GLU GLU A . n 
A 1 845  GLU 845  795 795 GLU GLU A . n 
A 1 846  GLU 846  796 796 GLU GLU A . n 
A 1 847  SER 847  797 797 SER SER A . n 
A 1 848  LEU 848  798 798 LEU LEU A . n 
A 1 849  GLU 849  799 799 GLU GLU A . n 
A 1 850  ASN 850  800 800 ASN ASN A . n 
A 1 851  ILE 851  801 801 ILE ILE A . n 
A 1 852  SER 852  802 802 SER SER A . n 
A 1 853  SER 853  803 803 SER SER A . n 
A 1 854  VAL 854  804 804 VAL VAL A . n 
A 1 855  LYS 855  805 805 LYS LYS A . n 
A 1 856  LYS 856  806 806 LYS LYS A . n 
A 1 857  ILE 857  807 807 ILE ILE A . n 
A 1 858  ILE 858  808 808 ILE ILE A . n 
A 1 859  LYS 859  809 809 LYS LYS A . n 
A 1 860  GLN 860  810 810 GLN GLN A . n 
A 1 861  ILE 861  811 811 ILE ILE A . n 
A 1 862  ILE 862  812 812 ILE ILE A . n 
A 1 863  SER 863  813 813 SER SER A . n 
A 1 864  HIS 864  814 814 HIS HIS A . n 
A 1 865  SER 865  815 815 SER SER A . n 
A 1 866  SER 866  816 816 SER SER A . n 
A 1 867  LYS 867  817 817 LYS LYS A . n 
A 1 868  VAL 868  818 818 VAL VAL A . n 
A 1 869  LEU 869  819 819 LEU LEU A . n 
A 1 870  HIS 870  820 820 HIS HIS A . n 
A 1 871  PHE 871  821 821 PHE PHE A . n 
A 1 872  PRO 872  822 822 PRO PRO A . n 
A 1 873  ASN 873  823 823 ASN ASN A . n 
A 1 874  PRO 874  824 824 PRO PRO A . n 
A 1 875  GLU 875  825 825 GLU GLU A . n 
A 1 876  ASP 876  826 826 ASP ASP A . n 
A 1 877  LYS 877  827 827 LYS LYS A . n 
A 1 878  LYS 878  828 828 LYS LYS A . n 
A 1 879  LEU 879  829 829 LEU LEU A . n 
A 1 880  GLU 880  830 830 GLU GLU A . n 
A 1 881  GLU 881  831 831 GLU GLU A . n 
A 1 882  ILE 882  832 832 ILE ILE A . n 
A 1 883  ILE 883  833 833 ILE ILE A . n 
A 1 884  HIS 884  834 834 HIS HIS A . n 
A 1 885  GLN 885  835 835 GLN GLN A . n 
A 1 886  ILE 886  836 836 ILE ILE A . n 
A 1 887  THR 887  837 837 THR THR A . n 
A 1 888  ASN 888  838 838 ASN ASN A . n 
A 1 889  VAL 889  839 839 VAL VAL A . n 
A 1 890  GLU 890  840 840 GLU GLU A . n 
A 1 891  ALA 891  841 841 ALA ALA A . n 
A 1 892  LEU 892  842 842 LEU LEU A . n 
A 1 893  ILE 893  843 843 ILE ILE A . n 
A 1 894  ALA 894  844 844 ALA ALA A . n 
A 1 895  ARG 895  845 845 ARG ARG A . n 
A 1 896  ALA 896  846 846 ALA ALA A . n 
A 1 897  ARG 897  847 847 ARG ARG A . n 
A 1 898  SER 898  848 848 SER SER A . n 
A 1 899  LEU 899  849 849 LEU LEU A . n 
A 1 900  LYS 900  850 850 LYS LYS A . n 
A 1 901  ALA 901  851 851 ALA ALA A . n 
A 1 902  LYS 902  852 852 LYS LYS A . n 
A 1 903  PHE 903  853 853 PHE PHE A . n 
A 1 904  GLY 904  854 854 GLY GLY A . n 
A 1 905  THR 905  855 855 THR THR A . n 
A 1 906  GLU 906  856 856 GLU GLU A . n 
A 1 907  LYS 907  857 857 LYS LYS A . n 
A 1 908  CYS 908  858 858 CYS CYS A . n 
A 1 909  GLU 909  859 859 GLU GLU A . n 
A 1 910  GLN 910  860 860 GLN GLN A . n 
A 1 911  GLU 911  861 861 GLU GLU A . n 
A 1 912  GLU 912  862 862 GLU GLU A . n 
A 1 913  GLU 913  863 863 GLU GLU A . n 
A 1 914  LYS 914  864 864 LYS LYS A . n 
A 1 915  GLU 915  865 865 GLU GLU A . n 
A 1 916  ASP 916  866 866 ASP ASP A . n 
A 1 917  LEU 917  867 867 LEU LEU A . n 
A 1 918  GLU 918  868 868 GLU GLU A . n 
A 1 919  ARG 919  869 869 ARG ARG A . n 
A 1 920  PHE 920  870 870 PHE PHE A . n 
A 1 921  VAL 921  871 871 VAL VAL A . n 
A 1 922  SER 922  872 872 SER SER A . n 
A 1 923  CYS 923  873 873 CYS CYS A . n 
A 1 924  LEU 924  874 874 LEU LEU A . n 
A 1 925  LEU 925  875 875 LEU LEU A . n 
A 1 926  GLU 926  876 876 GLU GLU A . n 
A 1 927  GLN 927  877 877 GLN GLN A . n 
A 1 928  PRO 928  878 878 PRO PRO A . n 
A 1 929  GLU 929  879 879 GLU GLU A . n 
A 1 930  VAL 930  880 880 VAL VAL A . n 
A 1 931  LEU 931  881 881 LEU LEU A . n 
A 1 932  VAL 932  882 882 VAL VAL A . n 
A 1 933  THR 933  883 883 THR THR A . n 
A 1 934  GLY 934  884 884 GLY GLY A . n 
A 1 935  ALA 935  885 885 ALA ALA A . n 
A 1 936  GLY 936  886 886 GLY GLY A . n 
A 1 937  ARG 937  887 887 ARG ARG A . n 
A 1 938  GLY 938  888 888 GLY GLY A . n 
A 1 939  HIS 939  889 889 HIS HIS A . n 
A 1 940  ALA 940  890 890 ALA ALA A . n 
A 1 941  GLY 941  891 891 GLY GLY A . n 
A 1 942  ARG 942  892 892 ARG ARG A . n 
A 1 943  ILE 943  893 893 ILE ILE A . n 
A 1 944  ILE 944  894 894 ILE ILE A . n 
A 1 945  HIS 945  895 895 HIS HIS A . n 
A 1 946  LYS 946  896 896 LYS LYS A . n 
A 1 947  LEU 947  897 897 LEU LEU A . n 
A 1 948  PHE 948  898 898 PHE PHE A . n 
A 1 949  VAL 949  899 899 VAL VAL A . n 
A 1 950  ASN 950  900 900 ASN ASN A . n 
A 1 951  ALA 951  901 901 ALA ALA A . n 
A 1 952  GLN 952  901 ?   ?   ?   A A n 
A 1 953  ARG 953  901 ?   ?   ?   A B n 
A 1 954  LEU 954  901 ?   ?   ?   A C n 
A 1 955  THR 955  901 ?   ?   ?   A D n 
A 1 956  GLU 956  901 ?   ?   ?   A E n 
A 1 957  SER 957  901 ?   ?   ?   A F n 
A 1 958  SER 958  901 ?   ?   ?   A G n 
A 1 959  ASP 959  901 ?   ?   ?   A H n 
A 1 960  GLU 960  901 ?   ?   ?   A I n 
A 1 961  ALA 961  901 ?   ?   ?   A J n 
A 1 962  ALA 962  901 ?   ?   ?   A K n 
A 1 963  ALA 963  901 ?   ?   ?   A L n 
A 1 964  MET 964  901 ?   ?   ?   A M n 
A 1 965  THR 965  901 ?   ?   ?   A N n 
A 1 966  PRO 966  901 ?   ?   ?   A O n 
A 1 967  PRO 967  901 ?   ?   ?   A P n 
A 1 968  GLU 968  901 ?   ?   ?   A Q n 
A 1 969  GLU 969  901 ?   ?   ?   A R n 
A 1 970  GLU 970  901 ?   ?   ?   A S n 
A 1 971  LEU 971  901 ?   ?   ?   A T n 
A 1 972  LYS 972  901 ?   ?   ?   A U n 
A 1 973  ARG 973  901 ?   ?   ?   A V n 
A 1 974  MET 974  901 ?   ?   ?   A W n 
A 1 975  GLY 975  901 ?   ?   ?   A X n 
A 1 976  SER 976  901 ?   ?   ?   A Y n 
A 1 977  PRO 977  901 ?   ?   ?   A Z n 
A 1 978  GLU 978  902 ?   ?   ?   A A n 
A 1 979  GLU 979  902 ?   ?   ?   A B n 
A 1 980  ARG 980  902 ?   ?   ?   A C n 
A 1 981  ARG 981  902 ?   ?   ?   A D n 
A 1 982  GLN 982  902 ?   ?   ?   A E n 
A 1 983  ASN 983  902 ?   ?   ?   A F n 
A 1 984  SER 984  902 ?   ?   ?   A G n 
A 1 985  VAL 985  902 ?   ?   ?   A H n 
A 1 986  SER 986  902 ?   ?   ?   A I n 
A 1 987  ASP 987  930 930 ASP ASP A . n 
A 1 988  PHE 988  931 931 PHE PHE A . n 
A 1 989  PRO 989  932 932 PRO PRO A . n 
A 1 990  PRO 990  933 933 PRO PRO A . n 
A 1 991  PRO 991  934 934 PRO PRO A . n 
A 1 992  ALA 992  935 935 ALA ALA A . n 
A 1 993  GLY 993  936 936 GLY GLY A . n 
A 1 994  ARG 994  937 937 ARG ARG A . n 
A 1 995  GLU 995  938 938 GLU GLU A . n 
A 1 996  PHE 996  939 939 PHE PHE A . n 
A 1 997  ILE 997  940 940 ILE ILE A . n 
A 1 998  LEU 998  941 941 LEU LEU A . n 
A 1 999  ARG 999  942 942 ARG ARG A . n 
A 1 1000 THR 1000 943 943 THR THR A . n 
A 1 1001 THR 1001 944 944 THR THR A . n 
A 1 1002 VAL 1002 945 945 VAL VAL A . n 
A 1 1003 PRO 1003 946 946 PRO PRO A . n 
A 1 1004 ARG 1004 947 947 ARG ARG A . n 
A 1 1005 PRO 1005 948 948 PRO PRO A . n 
A 1 1006 ALA 1006 949 949 ALA ALA A . n 
A 1 1007 PRO 1007 950 950 PRO PRO A . n 
A 1 1008 TYR 1008 951 951 TYR TYR A . n 
A 1 1009 SER 1009 952 952 SER SER A . n 
A 1 1010 LYS 1010 953 953 LYS LYS A . n 
A 1 1011 ALA 1011 954 954 ALA ALA A . n 
A 1 1012 LEU 1012 955 955 LEU LEU A . n 
A 1 1013 PRO 1013 956 956 PRO PRO A . n 
A 1 1014 GLN 1014 957 957 GLN GLN A . n 
A 1 1015 ARG 1015 958 958 ARG ARG A . n 
A 1 1016 MET 1016 959 959 MET MET A . n 
A 1 1017 TYR 1017 960 960 TYR TYR A . n 
A 1 1018 SER 1018 961 961 SER SER A . n 
A 1 1019 VAL 1019 962 962 VAL VAL A . n 
A 1 1020 LEU 1020 963 963 LEU LEU A . n 
A 1 1021 THR 1021 964 964 THR THR A . n 
A 1 1022 LYS 1022 965 965 LYS LYS A . n 
A 1 1023 GLU 1023 966 966 GLU GLU A . n 
A 1 1024 ASP 1024 967 967 ASP ASP A . n 
A 1 1025 PHE 1025 968 968 PHE PHE A . n 
A 1 1026 ARG 1026 969 969 ARG ARG A . n 
A 1 1027 LEU 1027 970 970 LEU LEU A . n 
A 1 1028 ALA 1028 971 971 ALA ALA A . n 
A 1 1029 GLY 1029 972 972 GLY GLY A . n 
A 1 1030 ALA 1030 973 973 ALA ALA A . n 
A 1 1031 PHE 1031 974 974 PHE PHE A . n 
A 1 1032 SER 1032 975 975 SER SER A . n 
A 1 1033 SER 1033 976 976 SER SER A . n 
A 1 1034 ASP 1034 977 977 ASP ASP A . n 
A 1 1035 THR 1035 978 978 THR THR A . n 
A 1 1036 SER 1036 979 979 SER SER A . n 
A 1 1037 PHE 1037 980 980 PHE PHE A . n 
A 1 1038 PHE 1038 981 981 PHE PHE A . n 
B 2 1    MET 1    1   ?   ?   ?   B . n 
B 2 2    ALA 2    2   2   ALA ALA B . n 
B 2 3    CYS 3    3   3   CYS CYS B . n 
B 2 4    SER 4    4   4   SER SER B . n 
B 2 5    ILE 5    5   5   ILE ILE B . n 
B 2 6    VAL 6    6   6   VAL VAL B . n 
B 2 7    GLN 7    7   7   GLN GLN B . n 
B 2 8    PHE 8    8   8   PHE PHE B . n 
B 2 9    CYS 9    9   9   CYS CYS B . n 
B 2 10   TYR 10   10  10  TYR TYR B . n 
B 2 11   PHE 11   11  11  PHE PHE B . n 
B 2 12   GLN 12   12  12  GLN GLN B . n 
B 2 13   ASP 13   13  13  ASP ASP B . n 
B 2 14   LEU 14   14  14  LEU LEU B . n 
B 2 15   GLN 15   15  15  GLN GLN B . n 
B 2 16   ALA 16   16  16  ALA ALA B . n 
B 2 17   ALA 17   17  17  ALA ALA B . n 
B 2 18   ARG 18   18  18  ARG ARG B . n 
B 2 19   ASP 19   19  19  ASP ASP B . n 
B 2 20   PHE 20   20  20  PHE PHE B . n 
B 2 21   LEU 21   21  21  LEU LEU B . n 
B 2 22   PHE 22   22  22  PHE PHE B . n 
B 2 23   PRO 23   23  23  PRO PRO B . n 
B 2 24   HIS 24   24  24  HIS HIS B . n 
B 2 25   LEU 25   25  25  LEU LEU B . n 
B 2 26   ARG 26   26  26  ARG ARG B . n 
B 2 27   GLU 27   27  ?   ?   ?   B . n 
B 2 28   GLU 28   28  ?   ?   ?   B . n 
B 2 29   ILE 29   29  ?   ?   ?   B . n 
B 2 30   LEU 30   30  ?   ?   ?   B . n 
B 2 31   SER 31   31  ?   ?   ?   B . n 
B 2 32   GLY 32   32  ?   ?   ?   B . n 
B 2 33   ALA 33   33  ?   ?   ?   B . n 
B 2 34   LEU 34   34  ?   ?   ?   B . n 
B 2 35   ARG 35   35  ?   ?   ?   B . n 
B 2 36   ARG 36   36  ?   ?   ?   B . n 
B 2 37   ASP 37   37  ?   ?   ?   B . n 
B 2 38   PRO 38   38  ?   ?   ?   B . n 
B 2 39   SER 39   39  ?   ?   ?   B . n 
B 2 40   LYS 40   40  ?   ?   ?   B . n 
B 2 41   SER 41   41  ?   ?   ?   B . n 
B 2 42   THR 42   42  ?   ?   ?   B . n 
B 2 43   ASP 43   43  ?   ?   ?   B . n 
B 2 44   TRP 44   44  ?   ?   ?   B . n 
B 2 45   GLU 45   45  ?   ?   ?   B . n 
B 2 46   ASP 46   46  ?   ?   ?   B . n 
B 2 47   ASP 47   47  ?   ?   ?   B . n 
B 2 48   GLY 48   48  ?   ?   ?   B . n 
B 2 49   TRP 49   49  ?   ?   ?   B . n 
B 2 50   GLY 50   50  ?   ?   ?   B . n 
B 2 51   ALA 51   51  ?   ?   ?   B . n 
B 2 52   TRP 52   52  ?   ?   ?   B . n 
B 2 53   GLU 53   53  ?   ?   ?   B . n 
B 2 54   GLU 54   54  ?   ?   ?   B . n 
B 2 55   ASN 55   55  ?   ?   ?   B . n 
B 2 56   GLU 56   56  ?   ?   ?   B . n 
B 2 57   PRO 57   57  ?   ?   ?   B . n 
B 2 58   GLN 58   58  ?   ?   ?   B . n 
B 2 59   GLU 59   59  ?   ?   ?   B . n 
B 2 60   PRO 60   60  ?   ?   ?   B . n 
B 2 61   GLU 61   61  61  GLU GLU B . n 
B 2 62   GLU 62   62  62  GLU GLU B . n 
B 2 63   GLU 63   63  63  GLU GLU B . n 
B 2 64   GLY 64   64  64  GLY GLY B . n 
B 2 65   ASN 65   65  65  ASN ASN B . n 
B 2 66   THR 66   66  66  THR THR B . n 
B 2 67   CYS 67   67  67  CYS CYS B . n 
B 2 68   LYS 68   68  68  LYS LYS B . n 
B 2 69   THR 69   69  69  THR THR B . n 
B 2 70   GLN 70   70  70  GLN GLN B . n 
B 2 71   LYS 71   71  71  LYS LYS B . n 
B 2 72   THR 72   72  72  THR THR B . n 
B 2 73   SER 73   73  73  SER SER B . n 
B 2 74   TRP 74   74  74  TRP TRP B . n 
B 2 75   LEU 75   75  75  LEU LEU B . n 
B 2 76   GLN 76   76  76  GLN GLN B . n 
B 2 77   ASP 77   77  77  ASP ASP B . n 
B 2 78   CYS 78   78  78  CYS CYS B . n 
B 2 79   VAL 79   79  79  VAL VAL B . n 
B 2 80   LEU 80   80  80  LEU LEU B . n 
B 2 81   SER 81   81  81  SER SER B . n 
B 2 82   LEU 82   82  82  LEU LEU B . n 
B 2 83   SER 83   83  83  SER SER B . n 
B 2 84   PRO 84   84  84  PRO PRO B . n 
B 2 85   THR 85   85  85  THR THR B . n 
B 2 86   ASN 86   86  86  ASN ASN B . n 
B 2 87   ASP 87   87  87  ASP ASP B . n 
B 2 88   LEU 88   88  88  LEU LEU B . n 
B 2 89   MET 89   89  89  MET MET B . n 
B 2 90   VAL 90   90  90  VAL VAL B . n 
B 2 91   ILE 91   91  91  ILE ILE B . n 
B 2 92   ALA 92   92  92  ALA ALA B . n 
B 2 93   ARG 93   93  93  ARG ARG B . n 
B 2 94   GLU 94   94  94  GLU GLU B . n 
B 2 95   GLN 95   95  95  GLN GLN B . n 
B 2 96   LYS 96   96  96  LYS LYS B . n 
B 2 97   ALA 97   97  97  ALA ALA B . n 
B 2 98   VAL 98   98  98  VAL VAL B . n 
B 2 99   PHE 99   99  99  PHE PHE B . n 
B 2 100  LEU 100  100 100 LEU LEU B . n 
B 2 101  VAL 101  101 101 VAL VAL B . n 
B 2 102  PRO 102  102 102 PRO PRO B . n 
B 2 103  LYS 103  103 103 LYS LYS B . n 
B 2 104  TRP 104  104 104 TRP TRP B . n 
B 2 105  LYS 105  105 105 LYS LYS B . n 
B 2 106  TYR 106  106 106 TYR TYR B . n 
B 2 107  SER 107  107 107 SER SER B . n 
B 2 108  ASP 108  108 108 ASP ASP B . n 
B 2 109  LYS 109  109 109 LYS LYS B . n 
B 2 110  GLY 110  110 110 GLY GLY B . n 
B 2 111  LYS 111  111 111 LYS LYS B . n 
B 2 112  GLU 112  112 112 GLU GLU B . n 
B 2 113  GLU 113  113 113 GLU GLU B . n 
B 2 114  MET 114  114 114 MET MET B . n 
B 2 115  GLN 115  115 115 GLN GLN B . n 
B 2 116  PHE 116  116 116 PHE PHE B . n 
B 2 117  ALA 117  117 117 ALA ALA B . n 
B 2 118  VAL 118  118 118 VAL VAL B . n 
B 2 119  GLY 119  119 119 GLY GLY B . n 
B 2 120  TRP 120  120 120 TRP TRP B . n 
B 2 121  SER 121  121 121 SER SER B . n 
B 2 122  GLY 122  122 122 GLY GLY B . n 
B 2 123  SER 123  123 123 SER SER B . n 
B 2 124  LEU 124  124 124 LEU LEU B . n 
B 2 125  ASN 125  125 125 ASN ASN B . n 
B 2 126  VAL 126  126 126 VAL VAL B . n 
B 2 127  GLU 127  127 127 GLU GLU B . n 
B 2 128  GLU 128  128 128 GLU GLU B . n 
B 2 129  GLY 129  129 129 GLY GLY B . n 
B 2 130  GLU 130  130 130 GLU GLU B . n 
B 2 131  CYS 131  131 131 CYS CYS B . n 
B 2 132  VAL 132  132 132 VAL VAL B . n 
B 2 133  THR 133  133 133 THR THR B . n 
B 2 134  SER 134  134 134 SER SER B . n 
B 2 135  ALA 135  135 135 ALA ALA B . n 
B 2 136  LEU 136  136 136 LEU LEU B . n 
B 2 137  CYS 137  137 137 CYS CYS B . n 
B 2 138  ILE 138  138 138 ILE ILE B . n 
B 2 139  PRO 139  139 139 PRO PRO B . n 
B 2 140  LEU 140  140 140 LEU LEU B . n 
B 2 141  ALA 141  141 141 ALA ALA B . n 
B 2 142  SER 142  142 142 SER SER B . n 
B 2 143  GLN 143  143 143 GLN GLN B . n 
B 2 144  LYS 144  144 144 LYS LYS B . n 
B 2 145  ARG 145  145 145 ARG ARG B . n 
B 2 146  SER 146  146 146 SER SER B . n 
B 2 147  SER 147  147 147 SER SER B . n 
B 2 148  THR 148  148 148 THR THR B . n 
B 2 149  GLY 149  149 149 GLY GLY B . n 
B 2 150  ARG 150  150 150 ARG ARG B . n 
B 2 151  PRO 151  151 151 PRO PRO B . n 
B 2 152  ASP 152  152 152 ASP ASP B . n 
B 2 153  TRP 153  153 153 TRP TRP B . n 
B 2 154  THR 154  154 154 THR THR B . n 
B 2 155  CYS 155  155 155 CYS CYS B . n 
B 2 156  ILE 156  156 156 ILE ILE B . n 
B 2 157  VAL 157  157 157 VAL VAL B . n 
B 2 158  VAL 158  158 158 VAL VAL B . n 
B 2 159  GLY 159  159 159 GLY GLY B . n 
B 2 160  PHE 160  160 160 PHE PHE B . n 
B 2 161  THR 161  161 161 THR THR B . n 
B 2 162  SER 162  162 162 SER SER B . n 
B 2 163  GLY 163  163 163 GLY GLY B . n 
B 2 164  TYR 164  164 164 TYR TYR B . n 
B 2 165  VAL 165  165 165 VAL VAL B . n 
B 2 166  ARG 166  166 166 ARG ARG B . n 
B 2 167  PHE 167  167 167 PHE PHE B . n 
B 2 168  TYR 168  168 168 TYR TYR B . n 
B 2 169  THR 169  169 169 THR THR B . n 
B 2 170  GLU 170  170 170 GLU GLU B . n 
B 2 171  ASN 171  171 171 ASN ASN B . n 
B 2 172  GLY 172  172 172 GLY GLY B . n 
B 2 173  VAL 173  173 173 VAL VAL B . n 
B 2 174  LEU 174  174 174 LEU LEU B . n 
B 2 175  LEU 175  175 175 LEU LEU B . n 
B 2 176  LEU 176  176 176 LEU LEU B . n 
B 2 177  ALA 177  177 177 ALA ALA B . n 
B 2 178  GLN 178  178 178 GLN GLN B . n 
B 2 179  LEU 179  179 179 LEU LEU B . n 
B 2 180  LEU 180  180 180 LEU LEU B . n 
B 2 181  ASN 181  181 181 ASN ASN B . n 
B 2 182  GLU 182  182 182 GLU GLU B . n 
B 2 183  ASP 183  183 183 ASP ASP B . n 
B 2 184  PRO 184  184 184 PRO PRO B . n 
B 2 185  VAL 185  185 185 VAL VAL B . n 
B 2 186  LEU 186  186 186 LEU LEU B . n 
B 2 187  GLN 187  187 187 GLN GLN B . n 
B 2 188  LEU 188  188 188 LEU LEU B . n 
B 2 189  LYS 189  189 189 LYS LYS B . n 
B 2 190  CYS 190  190 190 CYS CYS B . n 
B 2 191  ARG 191  191 191 ARG ARG B . n 
B 2 192  THR 192  192 192 THR THR B . n 
B 2 193  TYR 193  193 193 TYR TYR B . n 
B 2 194  GLU 194  194 194 GLU GLU B . n 
B 2 195  ILE 195  195 195 ILE ILE B . n 
B 2 196  PRO 196  196 196 PRO PRO B . n 
B 2 197  ARG 197  197 197 ARG ARG B . n 
B 2 198  HIS 198  198 198 HIS HIS B . n 
B 2 199  PRO 199  199 199 PRO PRO B . n 
B 2 200  GLY 200  200 200 GLY GLY B . n 
B 2 201  VAL 201  201 201 VAL VAL B . n 
B 2 202  THR 202  202 202 THR THR B . n 
B 2 203  GLU 203  203 203 GLU GLU B . n 
B 2 204  GLN 204  204 204 GLN GLN B . n 
B 2 205  ASN 205  205 205 ASN ASN B . n 
B 2 206  GLU 206  206 206 GLU GLU B . n 
B 2 207  GLU 207  207 207 GLU GLU B . n 
B 2 208  LEU 208  208 208 LEU LEU B . n 
B 2 209  SER 209  209 209 SER SER B . n 
B 2 210  ILE 210  210 210 ILE ILE B . n 
B 2 211  LEU 211  211 211 LEU LEU B . n 
B 2 212  TYR 212  212 212 TYR TYR B . n 
B 2 213  PRO 213  213 213 PRO PRO B . n 
B 2 214  ALA 214  214 214 ALA ALA B . n 
B 2 215  ALA 215  215 215 ALA ALA B . n 
B 2 216  ILE 216  216 216 ILE ILE B . n 
B 2 217  VAL 217  217 217 VAL VAL B . n 
B 2 218  THR 218  218 218 THR THR B . n 
B 2 219  ILE 219  219 219 ILE ILE B . n 
B 2 220  ASP 220  220 220 ASP ASP B . n 
B 2 221  GLY 221  221 221 GLY GLY B . n 
B 2 222  PHE 222  222 222 PHE PHE B . n 
B 2 223  SER 223  223 223 SER SER B . n 
B 2 224  LEU 224  224 224 LEU LEU B . n 
B 2 225  PHE 225  225 225 PHE PHE B . n 
B 2 226  GLN 226  226 226 GLN GLN B . n 
B 2 227  SER 227  227 227 SER SER B . n 
B 2 228  LEU 228  228 228 LEU LEU B . n 
B 2 229  ARG 229  229 229 ARG ARG B . n 
B 2 230  ALA 230  230 230 ALA ALA B . n 
B 2 231  CYS 231  231 231 CYS CYS B . n 
B 2 232  ARG 232  232 232 ARG ARG B . n 
B 2 233  ASN 233  233 233 ASN ASN B . n 
B 2 234  GLN 234  234 234 GLN GLN B . n 
B 2 235  VAL 235  235 235 VAL VAL B . n 
B 2 236  ALA 236  236 236 ALA ALA B . n 
B 2 237  LYS 237  237 237 LYS LYS B . n 
B 2 238  ALA 238  238 238 ALA ALA B . n 
B 2 239  ALA 239  239 239 ALA ALA B . n 
B 2 240  ALA 240  240 240 ALA ALA B . n 
B 2 241  SER 241  241 241 SER SER B . n 
B 2 242  GLY 242  242 242 GLY GLY B . n 
B 2 243  ASN 243  243 243 ASN ASN B . n 
B 2 244  GLU 244  244 244 GLU GLU B . n 
B 2 245  ASN 245  245 245 ASN ASN B . n 
B 2 246  ILE 246  246 246 ILE ILE B . n 
B 2 247  GLN 247  247 247 GLN GLN B . n 
B 2 248  PRO 248  248 248 PRO PRO B . n 
B 2 249  PRO 249  249 249 PRO PRO B . n 
B 2 250  PRO 250  250 250 PRO PRO B . n 
B 2 251  LEU 251  251 251 LEU LEU B . n 
B 2 252  ALA 252  252 252 ALA ALA B . n 
B 2 253  TYR 253  253 253 TYR TYR B . n 
B 2 254  LYS 254  254 254 LYS LYS B . n 
B 2 255  LYS 255  255 255 LYS LYS B . n 
B 2 256  TRP 256  256 256 TRP TRP B . n 
B 2 257  GLY 257  257 257 GLY GLY B . n 
B 2 258  LEU 258  258 258 LEU LEU B . n 
B 2 259  GLN 259  259 259 GLN GLN B . n 
B 2 260  ASP 260  260 260 ASP ASP B . n 
B 2 261  ILE 261  261 261 ILE ILE B . n 
B 2 262  ASP 262  262 262 ASP ASP B . n 
B 2 263  THR 263  263 263 THR THR B . n 
B 2 264  ILE 264  264 264 ILE ILE B . n 
B 2 265  ILE 265  265 265 ILE ILE B . n 
B 2 266  ASP 266  266 266 ASP ASP B . n 
B 2 267  HIS 267  267 267 HIS HIS B . n 
B 2 268  ALA 268  268 268 ALA ALA B . n 
B 2 269  SER 269  269 269 SER SER B . n 
B 2 270  VAL 270  270 270 VAL VAL B . n 
B 2 271  GLY 271  271 271 GLY GLY B . n 
B 2 272  ILE 272  272 272 ILE ILE B . n 
B 2 273  MET 273  273 273 MET MET B . n 
B 2 274  THR 274  274 274 THR THR B . n 
B 2 275  LEU 275  275 275 LEU LEU B . n 
B 2 276  SER 276  276 276 SER SER B . n 
B 2 277  PRO 277  277 277 PRO PRO B . n 
B 2 278  PHE 278  278 278 PHE PHE B . n 
B 2 279  ASP 279  279 279 ASP ASP B . n 
B 2 280  GLN 280  280 280 GLN GLN B . n 
B 2 281  MET 281  281 281 MET MET B . n 
B 2 282  LYS 282  282 282 LYS LYS B . n 
B 2 283  THR 283  283 283 THR THR B . n 
B 2 284  ALA 284  284 284 ALA ALA B . n 
B 2 285  SER 285  285 285 SER SER B . n 
B 2 286  ASN 286  286 286 ASN ASN B . n 
B 2 287  ILE 287  287 287 ILE ILE B . n 
B 2 288  GLY 288  288 288 GLY GLY B . n 
B 2 289  GLY 289  289 289 GLY GLY B . n 
B 2 290  PHE 290  290 290 PHE PHE B . n 
B 2 291  ASN 291  291 291 ASN ASN B . n 
B 2 292  ALA 292  292 292 ALA ALA B . n 
B 2 293  ALA 293  293 293 ALA ALA B . n 
B 2 294  ILE 294  294 294 ILE ILE B . n 
B 2 295  LYS 295  295 295 LYS LYS B . n 
B 2 296  ASN 296  296 296 ASN ASN B . n 
B 2 297  SER 297  297 297 SER SER B . n 
B 2 298  PRO 298  298 298 PRO PRO B . n 
B 2 299  PRO 299  299 299 PRO PRO B . n 
B 2 300  ALA 300  300 300 ALA ALA B . n 
B 2 301  MET 301  301 301 MET MET B . n 
B 2 302  SER 302  302 302 SER SER B . n 
B 2 303  GLN 303  303 303 GLN GLN B . n 
B 2 304  TYR 304  304 304 TYR TYR B . n 
B 2 305  ILE 305  305 305 ILE ILE B . n 
B 2 306  THR 306  306 306 THR THR B . n 
B 2 307  VAL 307  307 307 VAL VAL B . n 
B 2 308  GLY 308  308 308 GLY GLY B . n 
B 2 309  SER 309  309 309 SER SER B . n 
B 2 310  ASN 310  310 310 ASN ASN B . n 
B 2 311  PRO 311  311 311 PRO PRO B . n 
B 2 312  PHE 312  312 312 PHE PHE B . n 
B 2 313  THR 313  313 313 THR THR B . n 
B 2 314  GLY 314  314 314 GLY GLY B . n 
B 2 315  PHE 315  315 315 PHE PHE B . n 
B 2 316  PHE 316  316 316 PHE PHE B . n 
B 2 317  TYR 317  317 317 TYR TYR B . n 
B 2 318  ALA 318  318 318 ALA ALA B . n 
B 2 319  LEU 319  319 319 LEU LEU B . n 
B 2 320  GLU 320  320 320 GLU GLU B . n 
B 2 321  GLY 321  321 321 GLY GLY B . n 
B 2 322  SER 322  322 322 SER SER B . n 
B 2 323  THR 323  323 323 THR THR B . n 
B 2 324  GLN 324  324 324 GLN GLN B . n 
B 2 325  PRO 325  325 325 PRO PRO B . n 
B 2 326  LEU 326  326 326 LEU LEU B . n 
B 2 327  LEU 327  327 327 LEU LEU B . n 
B 2 328  SER 328  328 ?   ?   ?   B . n 
B 2 329  HIS 329  329 ?   ?   ?   B . n 
B 2 330  VAL 330  330 ?   ?   ?   B . n 
B 2 331  ALA 331  331 ?   ?   ?   B . n 
B 2 332  LEU 332  332 ?   ?   ?   B . n 
B 2 333  ALA 333  333 ?   ?   ?   B . n 
B 2 334  VAL 334  334 ?   ?   ?   B . n 
B 2 335  ALA 335  335 ?   ?   ?   B . n 
B 2 336  SER 336  336 ?   ?   ?   B . n 
B 2 337  LYS 337  337 ?   ?   ?   B . n 
B 2 338  LEU 338  338 ?   ?   ?   B . n 
B 2 339  THR 339  339 ?   ?   ?   B . n 
B 2 340  SER 340  340 ?   ?   ?   B . n 
B 2 341  ALA 341  341 ?   ?   ?   B . n 
B 2 342  LEU 342  342 ?   ?   ?   B . n 
B 2 343  PHE 343  343 ?   ?   ?   B . n 
B 2 344  ASN 344  344 ?   ?   ?   B . n 
B 2 345  ALA 345  345 ?   ?   ?   B . n 
B 2 346  ALA 346  346 ?   ?   ?   B . n 
B 2 347  SER 347  347 ?   ?   ?   B . n 
B 2 348  GLY 348  348 ?   ?   ?   B . n 
B 2 349  TRP 349  349 ?   ?   ?   B . n 
B 2 350  LEU 350  350 ?   ?   ?   B . n 
B 2 351  GLY 351  351 ?   ?   ?   B . n 
B 2 352  TRP 352  352 ?   ?   ?   B . n 
B 2 353  LYS 353  353 ?   ?   ?   B . n 
B 2 354  SER 354  354 ?   ?   ?   B . n 
B 2 355  LYS 355  355 ?   ?   ?   B . n 
B 2 356  HIS 356  356 ?   ?   ?   B . n 
B 2 357  GLU 357  357 ?   ?   ?   B . n 
B 2 358  GLU 358  358 ?   ?   ?   B . n 
B 2 359  GLU 359  359 ?   ?   ?   B . n 
B 2 360  ALA 360  360 ?   ?   ?   B . n 
B 2 361  VAL 361  361 ?   ?   ?   B . n 
B 2 362  GLN 362  362 ?   ?   ?   B . n 
B 2 363  LYS 363  363 ?   ?   ?   B . n 
B 2 364  GLN 364  364 364 GLN GLN B . n 
B 2 365  LYS 365  365 365 LYS LYS B . n 
B 2 366  PRO 366  366 366 PRO PRO B . n 
B 2 367  LYS 367  367 367 LYS LYS B . n 
B 2 368  VAL 368  368 368 VAL VAL B . n 
B 2 369  GLU 369  369 369 GLU GLU B . n 
B 2 370  PRO 370  370 370 PRO PRO B . n 
B 2 371  ALA 371  371 371 ALA ALA B . n 
B 2 372  THR 372  372 372 THR THR B . n 
B 2 373  PRO 373  373 373 PRO PRO B . n 
B 2 374  LEU 374  374 374 LEU LEU B . n 
B 2 375  ALA 375  375 375 ALA ALA B . n 
B 2 376  VAL 376  376 376 VAL VAL B . n 
B 2 377  ARG 377  377 377 ARG ARG B . n 
B 2 378  PHE 378  378 378 PHE PHE B . n 
B 2 379  GLY 379  379 379 GLY GLY B . n 
B 2 380  LEU 380  380 380 LEU LEU B . n 
B 2 381  PRO 381  381 381 PRO PRO B . n 
B 2 382  ASP 382  382 382 ASP ASP B . n 
B 2 383  SER 383  383 383 SER SER B . n 
B 2 384  ARG 384  384 384 ARG ARG B . n 
B 2 385  ARG 385  385 385 ARG ARG B . n 
B 2 386  HIS 386  386 386 HIS HIS B . n 
B 2 387  GLY 387  387 387 GLY GLY B . n 
B 2 388  GLU 388  388 388 GLU GLU B . n 
B 2 389  SER 389  389 389 SER SER B . n 
B 2 390  ILE 390  390 390 ILE ILE B . n 
B 2 391  CYS 391  391 391 CYS CYS B . n 
B 2 392  LEU 392  392 392 LEU LEU B . n 
B 2 393  SER 393  393 393 SER SER B . n 
B 2 394  PRO 394  394 394 PRO PRO B . n 
B 2 395  CYS 395  395 395 CYS CYS B . n 
B 2 396  ASN 396  396 396 ASN ASN B . n 
B 2 397  THR 397  397 397 THR THR B . n 
B 2 398  LEU 398  398 398 LEU LEU B . n 
B 2 399  ALA 399  399 399 ALA ALA B . n 
B 2 400  ALA 400  400 400 ALA ALA B . n 
B 2 401  VAL 401  401 401 VAL VAL B . n 
B 2 402  THR 402  402 402 THR THR B . n 
B 2 403  ASP 403  403 403 ASP ASP B . n 
B 2 404  ASP 404  404 404 ASP ASP B . n 
B 2 405  PHE 405  405 405 PHE PHE B . n 
B 2 406  GLY 406  406 406 GLY GLY B . n 
B 2 407  ARG 407  407 407 ARG ARG B . n 
B 2 408  VAL 408  408 408 VAL VAL B . n 
B 2 409  ILE 409  409 409 ILE ILE B . n 
B 2 410  LEU 410  410 410 LEU LEU B . n 
B 2 411  LEU 411  411 411 LEU LEU B . n 
B 2 412  ASP 412  412 412 ASP ASP B . n 
B 2 413  VAL 413  413 413 VAL VAL B . n 
B 2 414  ALA 414  414 414 ALA ALA B . n 
B 2 415  ARG 415  415 415 ARG ARG B . n 
B 2 416  GLY 416  416 416 GLY GLY B . n 
B 2 417  ILE 417  417 417 ILE ILE B . n 
B 2 418  ALA 418  418 418 ALA ALA B . n 
B 2 419  ILE 419  419 419 ILE ILE B . n 
B 2 420  ARG 420  420 420 ARG ARG B . n 
B 2 421  MET 421  421 421 MET MET B . n 
B 2 422  TRP 422  422 422 TRP TRP B . n 
B 2 423  LYS 423  423 423 LYS LYS B . n 
B 2 424  GLY 424  424 424 GLY GLY B . n 
B 2 425  TYR 425  425 425 TYR TYR B . n 
B 2 426  ARG 426  426 426 ARG ARG B . n 
B 2 427  ASP 427  427 427 ASP ASP B . n 
B 2 428  ALA 428  428 428 ALA ALA B . n 
B 2 429  GLN 429  429 429 GLN GLN B . n 
B 2 430  ILE 430  430 430 ILE ILE B . n 
B 2 431  GLY 431  431 431 GLY GLY B . n 
B 2 432  TRP 432  432 432 TRP TRP B . n 
B 2 433  ILE 433  433 433 ILE ILE B . n 
B 2 434  GLN 434  434 434 GLN GLN B . n 
B 2 435  THR 435  435 435 THR THR B . n 
B 2 436  VAL 436  436 436 VAL VAL B . n 
B 2 437  GLU 437  437 437 GLU GLU B . n 
B 2 438  ASP 438  438 438 ASP ASP B . n 
B 2 439  LEU 439  439 439 LEU LEU B . n 
B 2 440  HIS 440  440 ?   ?   ?   B . n 
B 2 441  GLU 441  441 ?   ?   ?   B . n 
B 2 442  ARG 442  442 ?   ?   ?   B . n 
B 2 443  VAL 443  443 ?   ?   ?   B . n 
B 2 444  PRO 444  444 ?   ?   ?   B . n 
B 2 445  GLU 445  445 ?   ?   ?   B . n 
B 2 446  LYS 446  446 ?   ?   ?   B . n 
B 2 447  ALA 447  447 ?   ?   ?   B . n 
B 2 448  ASP 448  448 ?   ?   ?   B . n 
B 2 449  PHE 449  449 ?   ?   ?   B . n 
B 2 450  SER 450  450 ?   ?   ?   B . n 
B 2 451  PRO 451  451 ?   ?   ?   B . n 
B 2 452  PHE 452  452 ?   ?   ?   B . n 
B 2 453  GLY 453  453 ?   ?   ?   B . n 
B 2 454  ASN 454  454 ?   ?   ?   B . n 
B 2 455  SER 455  455 ?   ?   ?   B . n 
B 2 456  GLN 456  456 ?   ?   ?   B . n 
B 2 457  GLY 457  457 457 GLY GLY B . n 
B 2 458  PRO 458  458 458 PRO PRO B . n 
B 2 459  SER 459  459 459 SER SER B . n 
B 2 460  ARG 460  460 460 ARG ARG B . n 
B 2 461  VAL 461  461 461 VAL VAL B . n 
B 2 462  ALA 462  462 462 ALA ALA B . n 
B 2 463  GLN 463  463 463 GLN GLN B . n 
B 2 464  PHE 464  464 464 PHE PHE B . n 
B 2 465  LEU 465  465 465 LEU LEU B . n 
B 2 466  VAL 466  466 466 VAL VAL B . n 
B 2 467  ILE 467  467 467 ILE ILE B . n 
B 2 468  TYR 468  468 468 TYR TYR B . n 
B 2 469  ALA 469  469 469 ALA ALA B . n 
B 2 470  PRO 470  470 470 PRO PRO B . n 
B 2 471  ARG 471  471 471 ARG ARG B . n 
B 2 472  ARG 472  472 472 ARG ARG B . n 
B 2 473  GLY 473  473 473 GLY GLY B . n 
B 2 474  ILE 474  474 474 ILE ILE B . n 
B 2 475  LEU 475  475 475 LEU LEU B . n 
B 2 476  GLU 476  476 476 GLU GLU B . n 
B 2 477  VAL 477  477 477 VAL VAL B . n 
B 2 478  TRP 478  478 478 TRP TRP B . n 
B 2 479  SER 479  479 479 SER SER B . n 
B 2 480  THR 480  480 480 THR THR B . n 
B 2 481  GLN 481  481 481 GLN GLN B . n 
B 2 482  GLN 482  482 482 GLN GLN B . n 
B 2 483  GLY 483  483 483 GLY GLY B . n 
B 2 484  PRO 484  484 484 PRO PRO B . n 
B 2 485  ARG 485  485 485 ARG ARG B . n 
B 2 486  VAL 486  486 486 VAL VAL B . n 
B 2 487  GLY 487  487 487 GLY GLY B . n 
B 2 488  ALA 488  488 488 ALA ALA B . n 
B 2 489  PHE 489  489 489 PHE PHE B . n 
B 2 490  ASN 490  490 490 ASN ASN B . n 
B 2 491  VAL 491  491 491 VAL VAL B . n 
B 2 492  GLY 492  492 492 GLY GLY B . n 
B 2 493  LYS 493  493 493 LYS LYS B . n 
B 2 494  HIS 494  494 494 HIS HIS B . n 
B 2 495  CYS 495  495 495 CYS CYS B . n 
B 2 496  ARG 496  496 496 ARG ARG B . n 
B 2 497  LEU 497  497 497 LEU LEU B . n 
B 2 498  LEU 498  498 498 LEU LEU B . n 
B 2 499  TYR 499  499 499 TYR TYR B . n 
B 2 500  PRO 500  500 500 PRO PRO B . n 
B 2 501  GLY 501  501 501 GLY GLY B . n 
B 2 502  TYR 502  502 502 TYR TYR B . n 
B 2 503  LYS 503  503 503 LYS LYS B . n 
B 2 504  ILE 504  504 504 ILE ILE B . n 
B 2 505  MET 505  505 505 MET MET B . n 
B 2 506  GLY 506  506 506 GLY GLY B . n 
B 2 507  LEU 507  507 507 LEU LEU B . n 
B 2 508  ASN 508  508 508 ASN ASN B . n 
B 2 509  ASN 509  509 509 ASN ASN B . n 
B 2 510  VAL 510  510 510 VAL VAL B . n 
B 2 511  THR 511  511 511 THR THR B . n 
B 2 512  SER 512  512 512 SER SER B . n 
B 2 513  GLN 513  513 513 GLN GLN B . n 
B 2 514  SER 514  514 514 SER SER B . n 
B 2 515  TRP 515  515 515 TRP TRP B . n 
B 2 516  GLN 516  516 516 GLN GLN B . n 
B 2 517  PRO 517  517 517 PRO PRO B . n 
B 2 518  GLN 518  518 518 GLN GLN B . n 
B 2 519  THR 519  519 519 THR THR B . n 
B 2 520  TYR 520  520 520 TYR TYR B . n 
B 2 521  GLN 521  521 521 GLN GLN B . n 
B 2 522  ILE 522  522 522 ILE ILE B . n 
B 2 523  CYS 523  523 523 CYS CYS B . n 
B 2 524  LEU 524  524 524 LEU LEU B . n 
B 2 525  VAL 525  525 525 VAL VAL B . n 
B 2 526  ASP 526  526 526 ASP ASP B . n 
B 2 527  PRO 527  527 527 PRO PRO B . n 
B 2 528  VAL 528  528 528 VAL VAL B . n 
B 2 529  SER 529  529 529 SER SER B . n 
B 2 530  GLY 530  530 530 GLY GLY B . n 
B 2 531  SER 531  531 531 SER SER B . n 
B 2 532  VAL 532  532 532 VAL VAL B . n 
B 2 533  LYS 533  533 533 LYS LYS B . n 
B 2 534  THR 534  534 534 THR THR B . n 
B 2 535  VAL 535  535 535 VAL VAL B . n 
B 2 536  ASN 536  536 536 ASN ASN B . n 
B 2 537  VAL 537  537 537 VAL VAL B . n 
B 2 538  PRO 538  538 538 PRO PRO B . n 
B 2 539  PHE 539  539 539 PHE PHE B . n 
B 2 540  HIS 540  540 540 HIS HIS B . n 
B 2 541  LEU 541  541 541 LEU LEU B . n 
B 2 542  ALA 542  542 542 ALA ALA B . n 
B 2 543  LEU 543  543 543 LEU LEU B . n 
B 2 544  SER 544  544 544 SER SER B . n 
B 2 545  ASP 545  545 ?   ?   ?   B . n 
B 2 546  LYS 546  546 ?   ?   ?   B . n 
B 2 547  LYS 547  547 ?   ?   ?   B . n 
B 2 548  LEU 548  548 ?   ?   ?   B . n 
B 2 549  ARG 549  549 ?   ?   ?   B . n 
B 2 550  GLU 550  550 ?   ?   ?   B . n 
B 2 551  GLN 551  551 ?   ?   ?   B . n 
B 2 552  LYS 552  552 ?   ?   ?   B . n 
B 2 553  LEU 553  553 ?   ?   ?   B . n 
B 2 554  GLU 554  554 ?   ?   ?   B . n 
B 2 555  LEU 555  555 ?   ?   ?   B . n 
B 2 556  GLY 556  556 ?   ?   ?   B . n 
B 2 557  GLY 557  557 ?   ?   ?   B . n 
B 2 558  SER 558  558 ?   ?   ?   B . n 
B 2 559  GLY 559  559 ?   ?   ?   B . n 
B 2 560  GLY 560  560 ?   ?   ?   B . n 
B 2 561  ARG 561  561 ?   ?   ?   B . n 
B 2 562  GLN 562  562 ?   ?   ?   B . n 
B 2 563  LEU 563  563 ?   ?   ?   B . n 
B 2 564  ASP 564  564 ?   ?   ?   B . n 
B 2 565  TYR 565  565 ?   ?   ?   B . n 
B 2 566  LYS 566  566 ?   ?   ?   B . n 
B 2 567  ASP 567  567 ?   ?   ?   B . n 
B 2 568  HIS 568  568 ?   ?   ?   B . n 
B 2 569  ASP 569  569 ?   ?   ?   B . n 
B 2 570  GLY 570  570 ?   ?   ?   B . n 
B 2 571  ASP 571  571 ?   ?   ?   B . n 
B 2 572  TYR 572  572 ?   ?   ?   B . n 
B 2 573  LYS 573  573 ?   ?   ?   B . n 
B 2 574  ASP 574  574 ?   ?   ?   B . n 
B 2 575  HIS 575  575 ?   ?   ?   B . n 
B 2 576  ASP 576  576 ?   ?   ?   B . n 
B 2 577  ILE 577  577 ?   ?   ?   B . n 
B 2 578  ASP 578  578 ?   ?   ?   B . n 
B 2 579  TYR 579  579 ?   ?   ?   B . n 
B 2 580  LYS 580  580 ?   ?   ?   B . n 
B 2 581  ASP 581  581 ?   ?   ?   B . n 
B 2 582  ASP 582  582 ?   ?   ?   B . n 
B 2 583  ASP 583  583 ?   ?   ?   B . n 
B 2 584  ASP 584  584 ?   ?   ?   B . n 
B 2 585  LYS 585  585 ?   ?   ?   B . n 
# 
_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                     8VYB 
_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                         8VYB 
_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                   8VYB 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8VYB 
_struct.title                        'Cryo-EM structure of human core Rab3GAP1/2 complex' 
_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        8VYB 
_struct_keywords.text            
'Complex, GAP, GEF, Rab3GAP, Lipid droplet, ER, Rab regulator, membrane trafficking, CYTOSOLIC PROTEIN' 
_struct_keywords.pdbx_keywords   'CYTOSOLIC 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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RB3GP_HUMAN Q15042 Q15042-3 1 
;MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGNSLGKPLEKGIFTSGTWEEKSDEISFADFKFSVTHHYLV
QESTDKEGKDELLEDVVPQSMQDLLGMNNDFPPRAHCLVRWYGLREFVVIAPAAHSDAVLSESKCNLLLSSVSIALGNTG
CQVPLFVQIHHKWRRMYVGECQGPGVRTDFEMVHLRKVPNQYTHLSGLLDIFKSKIGCPLTPLPPVSIAIRFTYVLQDWQ
QYFWPQQPPDIDALVGGEVGGLEFGKLPFGACEDPISELHLATTWPHLTEGIIVDNDVYSDLDPIQAPHWSVRVRKAENP
QCLLGDFVTEFFKICRRKESTDEILGRSAFEEEGKETADITHALSKLTEPASVPIHKLSVSNMVHTAKKKIRKHRGVEES
PLNNDVLNTILLFLFPDAVSEKPLDGTTSTDNNNPPSESEDYNLYNQFKSAPSDSLTYKLALCLCMINFYHGGLKGVAHL
WQEFVLEMRFRWENNFLIPGLASGPPDLRCCLLHQKLQMLNCCIERKKARDEGKKTSASDVTNIYPGDAGKAGDQLVPDN
LKETDKEKGEVGKSWDSWSDSEEEFFECLSDTEELKGNGQESGKKGGPKEMANLRPEGRLYQHGKLTLLHNGEPLYIPVT
QEPAPMTEDLLEEQSEVLAKLGTSAEGAHLRARMQSACLLSDMESFKAANPGCSLEDFVRWYSPRDYIEEEVIDEKGNVV
LKGELSARMKIPSNMWVEAWETAKPIPARRQRRLFDDTREAEKVLHYLAIQKPADLARHLLPCVIHAAVLKVKEEESLEN
ISSVKKIIKQIISHSSKVLHFPNPEDKKLEEIIHQITNVEALIARARSLKAKFGTEKCEQEEEKEDLERFVSCLLEQPEV
LVTGAGRGHAGRIIHKLFVNAQRLTESSDEAAAMTPPEEELKRMGSPEERRQNSVSDFPPPAGREFILRTTVPRPAPYSK
ALPQRMYSVLTKEDFRLAGAF
;
1 
2 UNP RBGPR_HUMAN Q9H2M9 ?        2 
;MACSIVQFCYFQDLQAARDFLFPHLREEILSGALRRDPSKSTDWEDDGWGAWEENEPQEPEEEGNTCKTQKTSWLQDCVL
SLSPTNDLMVIAREQKAVFLVPKWKYSDKGKEEMQFAVGWSGSLNVEEGECVTSALCIPLASQKRSSTGRPDWTCIVVGF
TSGYVRFYTENGVLLLAQLLNEDPVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAA
SGNENIQPPPLAYKKWGLQDIDTIIDHASVGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSNPFTGFFYALE
GSTQPLLSHVALAVASKLTSALFNAASGWLGWKSKHEEEAVQKQKPKVEPATPLAVRFGLPDSRRHGESICLSPCNTLAA
VTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQTVEDLHERVPEKADFSPFGNSQGPSRVAQFLVIYAPRRGILEVWST
QQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSGSVKTVNVPFHLALSDKK
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8VYB A 51 ? 1031 ? Q15042 1 ? 981 ? 1 974 
2 2 8VYB B 1  ? 547  ? Q9H2M9 1 ? 547 ? 1 547 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8VYB MET A 1    ? UNP Q15042 ? ? 'initiating methionine' -49 1  
1 8VYB TRP A 2    ? UNP Q15042 ? ? 'expression tag'        -48 2  
1 8VYB SER A 3    ? UNP Q15042 ? ? 'expression tag'        -47 3  
1 8VYB HIS A 4    ? UNP Q15042 ? ? 'expression tag'        -46 4  
1 8VYB PRO A 5    ? UNP Q15042 ? ? 'expression tag'        -45 5  
1 8VYB GLN A 6    ? UNP Q15042 ? ? 'expression tag'        -44 6  
1 8VYB PHE A 7    ? UNP Q15042 ? ? 'expression tag'        -43 7  
1 8VYB GLU A 8    ? UNP Q15042 ? ? 'expression tag'        -42 8  
1 8VYB LYS A 9    ? UNP Q15042 ? ? 'expression tag'        -41 9  
1 8VYB GLY A 10   ? UNP Q15042 ? ? 'expression tag'        -40 10 
1 8VYB GLY A 11   ? UNP Q15042 ? ? 'expression tag'        -39 11 
1 8VYB GLY A 12   ? UNP Q15042 ? ? 'expression tag'        -38 12 
1 8VYB SER A 13   ? UNP Q15042 ? ? 'expression tag'        -37 13 
1 8VYB GLY A 14   ? UNP Q15042 ? ? 'expression tag'        -36 14 
1 8VYB GLY A 15   ? UNP Q15042 ? ? 'expression tag'        -35 15 
1 8VYB GLY A 16   ? UNP Q15042 ? ? 'expression tag'        -34 16 
1 8VYB SER A 17   ? UNP Q15042 ? ? 'expression tag'        -33 17 
1 8VYB GLY A 18   ? UNP Q15042 ? ? 'expression tag'        -32 18 
1 8VYB GLY A 19   ? UNP Q15042 ? ? 'expression tag'        -31 19 
1 8VYB GLY A 20   ? UNP Q15042 ? ? 'expression tag'        -30 20 
1 8VYB SER A 21   ? UNP Q15042 ? ? 'expression tag'        -29 21 
1 8VYB TRP A 22   ? UNP Q15042 ? ? 'expression tag'        -28 22 
1 8VYB SER A 23   ? UNP Q15042 ? ? 'expression tag'        -27 23 
1 8VYB HIS A 24   ? UNP Q15042 ? ? 'expression tag'        -26 24 
1 8VYB PRO A 25   ? UNP Q15042 ? ? 'expression tag'        -25 25 
1 8VYB GLN A 26   ? UNP Q15042 ? ? 'expression tag'        -24 26 
1 8VYB PHE A 27   ? UNP Q15042 ? ? 'expression tag'        -23 27 
1 8VYB GLU A 28   ? UNP Q15042 ? ? 'expression tag'        -22 28 
1 8VYB LYS A 29   ? UNP Q15042 ? ? 'expression tag'        -21 29 
1 8VYB LEU A 30   ? UNP Q15042 ? ? 'expression tag'        -20 30 
1 8VYB GLU A 31   ? UNP Q15042 ? ? 'expression tag'        -19 31 
1 8VYB VAL A 32   ? UNP Q15042 ? ? 'expression tag'        -18 32 
1 8VYB LEU A 33   ? UNP Q15042 ? ? 'expression tag'        -17 33 
1 8VYB PHE A 34   ? UNP Q15042 ? ? 'expression tag'        -16 34 
1 8VYB GLN A 35   ? UNP Q15042 ? ? 'expression tag'        -15 35 
1 8VYB GLY A 36   ? UNP Q15042 ? ? 'expression tag'        -14 36 
1 8VYB PRO A 37   ? UNP Q15042 ? ? 'expression tag'        -13 37 
1 8VYB ARG A 38   ? UNP Q15042 ? ? 'expression tag'        -12 38 
1 8VYB SER A 39   ? UNP Q15042 ? ? 'expression tag'        -11 39 
1 8VYB GLU A 40   ? UNP Q15042 ? ? 'expression tag'        -10 40 
1 8VYB ALA A 41   ? UNP Q15042 ? ? 'expression tag'        -9  41 
1 8VYB ARG A 42   ? UNP Q15042 ? ? 'expression tag'        -8  42 
1 8VYB GLY A 43   ? UNP Q15042 ? ? 'expression tag'        -7  43 
1 8VYB ILE A 44   ? UNP Q15042 ? ? 'expression tag'        -6  44 
1 8VYB GLN A 45   ? UNP Q15042 ? ? 'expression tag'        -5  45 
1 8VYB ARG A 46   ? UNP Q15042 ? ? 'expression tag'        -4  46 
1 8VYB PRO A 47   ? UNP Q15042 ? ? 'expression tag'        -3  47 
1 8VYB THR A 48   ? UNP Q15042 ? ? 'expression tag'        -2  48 
1 8VYB SER A 49   ? UNP Q15042 ? ? 'expression tag'        -1  49 
1 8VYB THR A 50   ? UNP Q15042 ? ? 'expression tag'        0   50 
1 8VYB SER A 1032 ? UNP Q15042 ? ? 'expression tag'        975 51 
1 8VYB SER A 1033 ? UNP Q15042 ? ? 'expression tag'        976 52 
1 8VYB ASP A 1034 ? UNP Q15042 ? ? 'expression tag'        977 53 
1 8VYB THR A 1035 ? UNP Q15042 ? ? 'expression tag'        978 54 
1 8VYB SER A 1036 ? UNP Q15042 ? ? 'expression tag'        979 55 
1 8VYB PHE A 1037 ? UNP Q15042 ? ? 'expression tag'        980 56 
1 8VYB PHE A 1038 ? UNP Q15042 ? ? 'expression tag'        981 57 
2 8VYB LEU B 548  ? UNP Q9H2M9 ? ? 'expression tag'        548 58 
2 8VYB ARG B 549  ? UNP Q9H2M9 ? ? 'expression tag'        549 59 
2 8VYB GLU B 550  ? UNP Q9H2M9 ? ? 'expression tag'        550 60 
2 8VYB GLN B 551  ? UNP Q9H2M9 ? ? 'expression tag'        551 61 
2 8VYB LYS B 552  ? UNP Q9H2M9 ? ? 'expression tag'        552 62 
2 8VYB LEU B 553  ? UNP Q9H2M9 ? ? 'expression tag'        553 63 
2 8VYB GLU B 554  ? UNP Q9H2M9 ? ? 'expression tag'        554 64 
2 8VYB LEU B 555  ? UNP Q9H2M9 ? ? 'expression tag'        555 65 
2 8VYB GLY B 556  ? UNP Q9H2M9 ? ? 'expression tag'        556 66 
2 8VYB GLY B 557  ? UNP Q9H2M9 ? ? 'expression tag'        557 67 
2 8VYB SER B 558  ? UNP Q9H2M9 ? ? 'expression tag'        558 68 
2 8VYB GLY B 559  ? UNP Q9H2M9 ? ? 'expression tag'        559 69 
2 8VYB GLY B 560  ? UNP Q9H2M9 ? ? 'expression tag'        560 70 
2 8VYB ARG B 561  ? UNP Q9H2M9 ? ? 'expression tag'        561 71 
2 8VYB GLN B 562  ? UNP Q9H2M9 ? ? 'expression tag'        562 72 
2 8VYB LEU B 563  ? UNP Q9H2M9 ? ? 'expression tag'        563 73 
2 8VYB ASP B 564  ? UNP Q9H2M9 ? ? 'expression tag'        564 74 
2 8VYB TYR B 565  ? UNP Q9H2M9 ? ? 'expression tag'        565 75 
2 8VYB LYS B 566  ? UNP Q9H2M9 ? ? 'expression tag'        566 76 
2 8VYB ASP B 567  ? UNP Q9H2M9 ? ? 'expression tag'        567 77 
2 8VYB HIS B 568  ? UNP Q9H2M9 ? ? 'expression tag'        568 78 
2 8VYB ASP B 569  ? UNP Q9H2M9 ? ? 'expression tag'        569 79 
2 8VYB GLY B 570  ? UNP Q9H2M9 ? ? 'expression tag'        570 80 
2 8VYB ASP B 571  ? UNP Q9H2M9 ? ? 'expression tag'        571 81 
2 8VYB TYR B 572  ? UNP Q9H2M9 ? ? 'expression tag'        572 82 
2 8VYB LYS B 573  ? UNP Q9H2M9 ? ? 'expression tag'        573 83 
2 8VYB ASP B 574  ? UNP Q9H2M9 ? ? 'expression tag'        574 84 
2 8VYB HIS B 575  ? UNP Q9H2M9 ? ? 'expression tag'        575 85 
2 8VYB ASP B 576  ? UNP Q9H2M9 ? ? 'expression tag'        576 86 
2 8VYB ILE B 577  ? UNP Q9H2M9 ? ? 'expression tag'        577 87 
2 8VYB ASP B 578  ? UNP Q9H2M9 ? ? 'expression tag'        578 88 
2 8VYB TYR B 579  ? UNP Q9H2M9 ? ? 'expression tag'        579 89 
2 8VYB LYS B 580  ? UNP Q9H2M9 ? ? 'expression tag'        580 90 
2 8VYB ASP B 581  ? UNP Q9H2M9 ? ? 'expression tag'        581 91 
2 8VYB ASP B 582  ? UNP Q9H2M9 ? ? 'expression tag'        582 92 
2 8VYB ASP B 583  ? UNP Q9H2M9 ? ? 'expression tag'        583 93 
2 8VYB ASP B 584  ? UNP Q9H2M9 ? ? 'expression tag'        584 94 
2 8VYB LYS B 585  ? UNP Q9H2M9 ? ? 'expression tag'        585 95 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 71  ? TRP A 87  ? SER A 21  TRP A 37  1 ? 17 
HELX_P HELX_P2  AA2 GLY A 101 ? GLY A 106 ? GLY A 51  GLY A 56  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 148 ? LEU A 154 ? PRO A 98  LEU A 104 1 ? 7  
HELX_P HELX_P4  AA4 HIS A 166 ? GLY A 173 ? HIS A 116 GLY A 123 1 ? 8  
HELX_P HELX_P5  AA5 SER A 191 ? GLY A 210 ? SER A 141 GLY A 160 1 ? 20 
HELX_P HELX_P6  AA6 PRO A 249 ? THR A 253 ? PRO A 199 THR A 203 5 ? 5  
HELX_P HELX_P7  AA7 HIS A 254 ? GLY A 267 ? HIS A 204 GLY A 217 1 ? 14 
HELX_P HELX_P8  AA8 ASP A 353 ? ALA A 357 ? ASP A 303 ALA A 307 5 ? 5  
HELX_P HELX_P9  AA9 LEU A 373 ? VAL A 378 ? LEU A 323 VAL A 328 1 ? 6  
HELX_P HELX_P10 AB1 THR A 379 ? PHE A 382 ? THR A 329 PHE A 332 5 ? 4  
HELX_P HELX_P11 AB2 PRO A 832 ? PRO A 832 ? PRO A 782 PRO A 782 5 ? 1  
HELX_P HELX_P12 AB3 CYS A 833 ? ASN A 850 ? CYS A 783 ASN A 800 1 ? 18 
HELX_P HELX_P13 AB4 SER A 853 ? LYS A 867 ? SER A 803 LYS A 817 1 ? 15 
HELX_P HELX_P14 AB5 GLU A 875 ? GLY A 904 ? GLU A 825 GLY A 854 1 ? 30 
HELX_P HELX_P15 AB6 GLN A 910 ? VAL A 921 ? GLN A 860 VAL A 871 1 ? 12 
HELX_P HELX_P16 AB7 GLY A 938 ? ALA A 951 ? GLY A 888 ALA A 901 1 ? 14 
HELX_P HELX_P17 AB8 LEU B 14  ? PHE B 22  ? LEU B 14  PHE B 22  1 ? 9  
HELX_P HELX_P18 AB9 SER B 73  ? CYS B 78  ? SER B 73  CYS B 78  1 ? 6  
HELX_P HELX_P19 AC1 GLY B 221 ? SER B 241 ? GLY B 221 SER B 241 1 ? 21 
HELX_P HELX_P20 AC2 SER B 276 ? GLY B 288 ? SER B 276 GLY B 288 1 ? 13 
HELX_P HELX_P21 AC3 ASN B 508 ? TRP B 515 ? ASN B 508 TRP B 515 1 ? 8  
HELX_P HELX_P22 AC4 PHE B 539 ? SER B 544 ? PHE B 539 SER B 544 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ARG 1004 A . ? ARG 947 A PRO 1005 A ? PRO 948 A 1 -8.46 
2 ASN 310  B . ? ASN 310 B PRO 311  B ? PRO 311 B 1 2.41  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 13 ? 
AA3 ? 4  ? 
AA4 ? 4  ? 
AA5 ? 2  ? 
AA6 ? 4  ? 
AA7 ? 5  ? 
AA8 ? 4  ? 
AA9 ? 4  ? 
AB1 ? 4  ? 
# 
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 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? parallel      
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? anti-parallel 
AA2 12 13 ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA4 2  3  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA5 1  2  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA6 2  3  ? anti-parallel 
AA6 3  4  ? anti-parallel 
AA7 1  2  ? anti-parallel 
AA7 2  3  ? anti-parallel 
AA7 3  4  ? anti-parallel 
AA7 4  5  ? parallel      
AA8 1  2  ? anti-parallel 
AA8 2  3  ? anti-parallel 
AA8 3  4  ? anti-parallel 
AA9 1  2  ? anti-parallel 
AA9 2  3  ? anti-parallel 
AA9 3  4  ? anti-parallel 
AB1 1  2  ? anti-parallel 
AB1 2  3  ? anti-parallel 
AB1 3  4  ? anti-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  TRP A 108  ? LYS A 111  ? TRP A 58  LYS A 61  
AA1 2  LYS A 121  ? LEU A 129  ? LYS A 71  LEU A 79  
AA1 3  GLU A 114  ? SER A 116  ? GLU A 64  SER A 66  
AA2 1  TRP A 108  ? LYS A 111  ? TRP A 58  LYS A 61  
AA2 2  LYS A 121  ? LEU A 129  ? LYS A 71  LEU A 79  
AA2 3  GLU A 176  ? PRO A 182  ? GLU A 126 PRO A 132 
AA2 4  LEU A 215  ? ILE A 219  ? LEU A 165 ILE A 169 
AA2 5  MET A 226  ? GLY A 233  ? MET A 176 GLY A 183 
AA2 6  VAL A 236  ? LEU A 245  ? VAL A 186 LEU A 195 
AA2 7  PHE A 1025 ? ASP A 1034 ? PHE A 968 ASP A 977 
AA2 8  LEU A 1012 ? THR A 1021 ? LEU A 955 THR A 964 
AA2 9  GLY A 993  ? VAL A 1002 ? GLY A 936 VAL A 945 
AA2 10 SER A 277  ? LEU A 286  ? SER A 227 LEU A 236 
AA2 11 ILE A 326  ? TRP A 335  ? ILE A 276 TRP A 285 
AA2 12 HIS A 359  ? LYS A 366  ? HIS A 309 LYS A 316 
AA2 13 VAL A 930  ? LEU A 931  ? VAL A 880 LEU A 881 
AA3 1  SER B 4    ? TYR B 10   ? SER B 4   TYR B 10  
AA3 2  SER B 531  ? ASN B 536  ? SER B 531 ASN B 536 
AA3 3  CYS B 523  ? ASP B 526  ? CYS B 523 ASP B 526 
AA3 4  ARG B 496  ? LEU B 498  ? ARG B 496 LEU B 498 
AA4 1  VAL B 79   ? LEU B 82   ? VAL B 79  LEU B 82  
AA4 2  MET B 89   ? ALA B 92   ? MET B 89  ALA B 92  
AA4 3  LYS B 96   ? VAL B 101  ? LYS B 96  VAL B 101 
AA4 4  ALA B 117  ? SER B 123  ? ALA B 117 SER B 123 
AA5 1  TRP B 104  ? TYR B 106  ? TRP B 104 TYR B 106 
AA5 2  GLU B 112  ? MET B 114  ? GLU B 112 MET B 114 
AA6 1  VAL B 132  ? PRO B 139  ? VAL B 132 PRO B 139 
AA6 2  THR B 154  ? PHE B 160  ? THR B 154 PHE B 160 
AA6 3  TYR B 164  ? TYR B 168  ? TYR B 164 TYR B 168 
AA6 4  LEU B 174  ? LEU B 179  ? LEU B 174 LEU B 179 
AA7 1  GLN B 187  ? ARG B 191  ? GLN B 187 ARG B 191 
AA7 2  GLU B 207  ? TYR B 212  ? GLU B 207 TYR B 212 
AA7 3  ALA B 215  ? ASP B 220  ? ALA B 215 ASP B 220 
AA7 4  LYS B 254  ? LEU B 258  ? LYS B 254 LEU B 258 
AA7 5  THR B 372  ? LEU B 374  ? THR B 372 LEU B 374 
AA8 1  THR B 263  ? GLY B 271  ? THR B 263 GLY B 271 
AA8 2  MET B 301  ? SER B 309  ? MET B 301 SER B 309 
AA8 3  THR B 313  ? LEU B 319  ? THR B 313 LEU B 319 
AA8 4  PHE B 378  ? LEU B 380  ? PHE B 378 LEU B 380 
AA9 1  GLY B 387  ? LEU B 392  ? GLY B 387 LEU B 392 
AA9 2  LEU B 398  ? ASP B 403  ? LEU B 398 ASP B 403 
AA9 3  ARG B 407  ? ASP B 412  ? ARG B 407 ASP B 412 
AA9 4  ALA B 418  ? LYS B 423  ? ALA B 418 LYS B 423 
AB1 1  GLN B 429  ? THR B 435  ? GLN B 429 THR B 435 
AB1 2  ALA B 462  ? ALA B 469  ? ALA B 462 ALA B 469 
AB1 3  ILE B 474  ? SER B 479  ? ILE B 474 SER B 479 
AB1 4  GLY B 487  ? ASN B 490  ? GLY B 487 ASN B 490 
# 
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 GLU A 109  ? N GLU A 59  O TYR A 128  ? O TYR A 78  
AA1 2  3  O PHE A 122  ? O PHE A 72  N ILE A 115  ? N ILE A 65  
AA2 1  2  N GLU A 109  ? N GLU A 59  O TYR A 128  ? O TYR A 78  
AA2 2  3  N SER A 123  ? N SER A 73  O ALA A 181  ? O ALA A 131 
AA2 3  4  N ILE A 180  ? N ILE A 130 O PHE A 216  ? O PHE A 166 
AA2 4  5  N ILE A 219  ? N ILE A 169 O MET A 226  ? O MET A 176 
AA2 5  6  N GLY A 233  ? N GLY A 183 O VAL A 236  ? O VAL A 186 
AA2 6  7  N ASP A 239  ? N ASP A 189 O PHE A 1031 ? O PHE A 974 
AA2 7  8  O ALA A 1030 ? O ALA A 973 N ARG A 1015 ? N ARG A 958 
AA2 8  9  O MET A 1016 ? O MET A 959 N LEU A 998  ? N LEU A 941 
AA2 9  10 O GLU A 995  ? O GLU A 938 N ARG A 281  ? N ARG A 231 
AA2 10 11 N ILE A 280  ? N ILE A 230 O TRP A 335  ? O TRP A 285 
AA2 11 12 N HIS A 330  ? N HIS A 280 O ARG A 363  ? O ARG A 313 
AA2 12 13 N VAL A 362  ? N VAL A 312 O VAL A 930  ? O VAL A 880 
AA3 1  2  N SER B 4    ? N SER B 4   O ASN B 536  ? O ASN B 536 
AA3 2  3  O SER B 531  ? O SER B 531 N ASP B 526  ? N ASP B 526 
AA3 3  4  O CYS B 523  ? O CYS B 523 N LEU B 498  ? N LEU B 498 
AA4 1  2  N VAL B 79   ? N VAL B 79  O ALA B 92   ? O ALA B 92  
AA4 2  3  N ILE B 91   ? N ILE B 91  O VAL B 98   ? O VAL B 98  
AA4 3  4  N PHE B 99   ? N PHE B 99  O TRP B 120  ? O TRP B 120 
AA5 1  2  N LYS B 105  ? N LYS B 105 O GLU B 113  ? O GLU B 113 
AA6 1  2  N THR B 133  ? N THR B 133 O GLY B 159  ? O GLY B 159 
AA6 2  3  N VAL B 158  ? N VAL B 158 O ARG B 166  ? O ARG B 166 
AA6 3  4  N VAL B 165  ? N VAL B 165 O GLN B 178  ? O GLN B 178 
AA7 1  2  N ARG B 191  ? N ARG B 191 O GLU B 207  ? O GLU B 207 
AA7 2  3  N LEU B 208  ? N LEU B 208 O ILE B 219  ? O ILE B 219 
AA7 3  4  N ILE B 216  ? N ILE B 216 O TRP B 256  ? O TRP B 256 
AA7 4  5  N GLY B 257  ? N GLY B 257 O LEU B 374  ? O LEU B 374 
AA8 1  2  N THR B 263  ? N THR B 263 O SER B 309  ? O SER B 309 
AA8 2  3  N TYR B 304  ? N TYR B 304 O PHE B 316  ? O PHE B 316 
AA8 3  4  N PHE B 315  ? N PHE B 315 O PHE B 378  ? O PHE B 378 
AA9 1  2  N GLU B 388  ? N GLU B 388 O THR B 402  ? O THR B 402 
AA9 2  3  N VAL B 401  ? N VAL B 401 O ILE B 409  ? O ILE B 409 
AA9 3  4  N LEU B 410  ? N LEU B 410 O ILE B 419  ? O ILE B 419 
AB1 1  2  N GLY B 431  ? N GLY B 431 O VAL B 466  ? O VAL B 466 
AB1 2  3  N LEU B 465  ? N LEU B 465 O TRP B 478  ? O TRP B 478 
AB1 3  4  N VAL B 477  ? N VAL B 477 O GLY B 487  ? O GLY B 487 
# 
_pdbx_entry_details.entry_id                   8VYB 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_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 LYS A 89  ? ? -90.68  51.02   
2  1 ALA A 134 ? ? 56.12   -130.53 
3  1 HIS A 170 ? ? 55.09   -126.42 
4  1 HIS A 171 ? ? -106.10 -155.34 
5  1 GLN A 240 ? ? 57.33   -117.90 
6  1 ASN A 823 ? ? 52.90   73.67   
7  1 LYS A 857 ? ? -82.43  47.13   
8  1 SER A 872 ? ? 82.23   -17.13  
9  1 PRO A 878 ? ? -93.60  48.28   
10 1 GLU A 879 ? ? -170.25 112.14  
11 1 ALA A 885 ? ? 52.93   -137.52 
12 1 GLU B 63  ? ? -84.41  46.28   
13 1 LYS B 68  ? ? -149.05 -157.43 
14 1 ARG B 93  ? ? -95.85  -66.69  
15 1 GLU B 94  ? ? -122.60 -54.56  
16 1 GLN B 95  ? ? -140.67 11.22   
17 1 LYS B 103 ? ? -161.54 116.83  
18 1 SER B 107 ? ? -79.41  -168.78 
19 1 THR B 192 ? ? -111.52 -152.77 
20 1 ASN B 310 ? ? 52.59   74.82   
21 1 GLN B 481 ? ? -129.04 -76.86  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8VYB 
_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_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_em_3d_fitting_list.pdb_chain_id                  . 
_em_3d_fitting_list.pdb_chain_residue_range       . 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   AlphaFold 
_em_3d_fitting_list.type                          'in silico model' 
_em_3d_fitting_list.accession_code                ? 
_em_3d_fitting_list.initial_refinement_model_id   ? 
# 
_em_3d_reconstruction.entry_id                    8VYB 
_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                  3.37 
_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               170636 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_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 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 RECOMBINANT COMPLEX 'Core Rab3GAP1/2 complex' ? ? ? '1, 2' 
2 1 RECOMBINANT COMPLEX Rab3GAP1                  ? ? ? 1      
3 1 RECOMBINANT COMPLEX Rab3GAP2                  ? ? ? 2      
# 
_em_imaging.entry_id                        8VYB 
_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               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             500 
_em_imaging.nominal_defocus_max             2500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           215000 
_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_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        C-flat-2/1 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8VYB 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               '2s blot time, 5s blot force' 
# 
_em_experiment.entry_id                8VYB 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              8VYB 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
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 -49 ? A MET 1   
2   1 Y 1 A TRP -48 ? A TRP 2   
3   1 Y 1 A SER -47 ? A SER 3   
4   1 Y 1 A HIS -46 ? A HIS 4   
5   1 Y 1 A PRO -45 ? A PRO 5   
6   1 Y 1 A GLN -44 ? A GLN 6   
7   1 Y 1 A PHE -43 ? A PHE 7   
8   1 Y 1 A GLU -42 ? A GLU 8   
9   1 Y 1 A LYS -41 ? A LYS 9   
10  1 Y 1 A GLY -40 ? A GLY 10  
11  1 Y 1 A GLY -39 ? A GLY 11  
12  1 Y 1 A GLY -38 ? A GLY 12  
13  1 Y 1 A SER -37 ? A SER 13  
14  1 Y 1 A GLY -36 ? A GLY 14  
15  1 Y 1 A GLY -35 ? A GLY 15  
16  1 Y 1 A GLY -34 ? A GLY 16  
17  1 Y 1 A SER -33 ? A SER 17  
18  1 Y 1 A GLY -32 ? A GLY 18  
19  1 Y 1 A GLY -31 ? A GLY 19  
20  1 Y 1 A GLY -30 ? A GLY 20  
21  1 Y 1 A SER -29 ? A SER 21  
22  1 Y 1 A TRP -28 ? A TRP 22  
23  1 Y 1 A SER -27 ? A SER 23  
24  1 Y 1 A HIS -26 ? A HIS 24  
25  1 Y 1 A PRO -25 ? A PRO 25  
26  1 Y 1 A GLN -24 ? A GLN 26  
27  1 Y 1 A PHE -23 ? A PHE 27  
28  1 Y 1 A GLU -22 ? A GLU 28  
29  1 Y 1 A LYS -21 ? A LYS 29  
30  1 Y 1 A LEU -20 ? A LEU 30  
31  1 Y 1 A GLU -19 ? A GLU 31  
32  1 Y 1 A VAL -18 ? A VAL 32  
33  1 Y 1 A LEU -17 ? A LEU 33  
34  1 Y 1 A PHE -16 ? A PHE 34  
35  1 Y 1 A GLN -15 ? A GLN 35  
36  1 Y 1 A GLY -14 ? A GLY 36  
37  1 Y 1 A PRO -13 ? A PRO 37  
38  1 Y 1 A ARG -12 ? A ARG 38  
39  1 Y 1 A SER -11 ? A SER 39  
40  1 Y 1 A GLU -10 ? A GLU 40  
41  1 Y 1 A ALA -9  ? A ALA 41  
42  1 Y 1 A ARG -8  ? A ARG 42  
43  1 Y 1 A GLY -7  ? A GLY 43  
44  1 Y 1 A ILE -6  ? A ILE 44  
45  1 Y 1 A GLN -5  ? A GLN 45  
46  1 Y 1 A ARG -4  ? A ARG 46  
47  1 Y 1 A PRO -3  ? A PRO 47  
48  1 Y 1 A THR -2  ? A THR 48  
49  1 Y 1 A SER -1  ? A SER 49  
50  1 Y 1 A THR 0   ? A THR 50  
51  1 Y 1 A MET 1   ? A MET 51  
52  1 Y 1 A ALA 2   ? A ALA 52  
53  1 Y 1 A ALA 3   ? A ALA 53  
54  1 Y 1 A ASP 4   ? A ASP 54  
55  1 Y 1 A SER 5   ? A SER 55  
56  1 Y 1 A GLU 6   ? A GLU 56  
57  1 Y 1 A PRO 7   ? A PRO 57  
58  1 Y 1 A GLU 8   ? A GLU 58  
59  1 Y 1 A SER 9   ? A SER 59  
60  1 Y 1 A GLU 10  ? A GLU 60  
61  1 Y 1 A VAL 11  ? A VAL 61  
62  1 Y 1 A PHE 12  ? A PHE 62  
63  1 Y 1 A GLU 13  ? A GLU 63  
64  1 Y 1 A ILE 14  ? A ILE 64  
65  1 Y 1 A THR 15  ? A THR 65  
66  1 Y 1 A ASP 16  ? A ASP 66  
67  1 Y 1 A PHE 17  ? A PHE 67  
68  1 Y 1 A THR 18  ? A THR 68  
69  1 Y 1 A TYR 242 ? A TYR 292 
70  1 Y 1 A PHE 243 ? A PHE 293 
71  1 Y 1 A TRP 244 ? A TRP 294 
72  1 Y 1 A PRO 245 ? A PRO 295 
73  1 Y 1 A GLN 246 ? A GLN 296 
74  1 Y 1 A GLN 247 ? A GLN 297 
75  1 Y 1 A PRO 248 ? A PRO 298 
76  1 Y 1 A PRO 249 ? A PRO 299 
77  1 Y 1 A ASP 250 ? A ASP 300 
78  1 Y 1 A ILE 251 ? A ILE 301 
79  1 Y 1 A ASP 252 ? A ASP 302 
80  1 Y 1 A ALA 253 ? A ALA 303 
81  1 Y 1 A LEU 254 ? A LEU 304 
82  1 Y 1 A VAL 255 ? A VAL 305 
83  1 Y 1 A GLY 256 ? A GLY 306 
84  1 Y 1 A GLY 257 ? A GLY 307 
85  1 Y 1 A GLU 258 ? A GLU 308 
86  1 Y 1 A VAL 259 ? A VAL 309 
87  1 Y 1 A GLY 260 ? A GLY 310 
88  1 Y 1 A GLY 261 ? A GLY 311 
89  1 Y 1 A LEU 262 ? A LEU 312 
90  1 Y 1 A GLU 263 ? A GLU 313 
91  1 Y 1 A LYS 333 ? A LYS 383 
92  1 Y 1 A ILE 334 ? A ILE 384 
93  1 Y 1 A CYS 335 ? A CYS 385 
94  1 Y 1 A ARG 336 ? A ARG 386 
95  1 Y 1 A ARG 337 ? A ARG 387 
96  1 Y 1 A LYS 338 ? A LYS 388 
97  1 Y 1 A GLU 339 ? A GLU 389 
98  1 Y 1 A SER 340 ? A SER 390 
99  1 Y 1 A THR 341 ? A THR 391 
100 1 Y 1 A ASP 342 ? A ASP 392 
101 1 Y 1 A GLU 343 ? A GLU 393 
102 1 Y 1 A ILE 344 ? A ILE 394 
103 1 Y 1 A LEU 345 ? A LEU 395 
104 1 Y 1 A GLY 346 ? A GLY 396 
105 1 Y 1 A ARG 347 ? A ARG 397 
106 1 Y 1 A SER 348 ? A SER 398 
107 1 Y 1 A ALA 349 ? A ALA 399 
108 1 Y 1 A PHE 350 ? A PHE 400 
109 1 Y 1 A GLU 351 ? A GLU 401 
110 1 Y 1 A GLU 352 ? A GLU 402 
111 1 Y 1 A GLU 353 ? A GLU 403 
112 1 Y 1 A GLY 354 ? A GLY 404 
113 1 Y 1 A LYS 355 ? A LYS 405 
114 1 Y 1 A GLU 356 ? A GLU 406 
115 1 Y 1 A THR 357 ? A THR 407 
116 1 Y 1 A ALA 358 ? A ALA 408 
117 1 Y 1 A ASP 359 ? A ASP 409 
118 1 Y 1 A ILE 360 ? A ILE 410 
119 1 Y 1 A THR 361 ? A THR 411 
120 1 Y 1 A HIS 362 ? A HIS 412 
121 1 Y 1 A ALA 363 ? A ALA 413 
122 1 Y 1 A LEU 364 ? A LEU 414 
123 1 Y 1 A SER 365 ? A SER 415 
124 1 Y 1 A LYS 366 ? A LYS 416 
125 1 Y 1 A LEU 367 ? A LEU 417 
126 1 Y 1 A THR 368 ? A THR 418 
127 1 Y 1 A GLU 369 ? A GLU 419 
128 1 Y 1 A PRO 370 ? A PRO 420 
129 1 Y 1 A ALA 371 ? A ALA 421 
130 1 Y 1 A SER 372 ? A SER 422 
131 1 Y 1 A VAL 373 ? A VAL 423 
132 1 Y 1 A PRO 374 ? A PRO 424 
133 1 Y 1 A ILE 375 ? A ILE 425 
134 1 Y 1 A HIS 376 ? A HIS 426 
135 1 Y 1 A LYS 377 ? A LYS 427 
136 1 Y 1 A LEU 378 ? A LEU 428 
137 1 Y 1 A SER 379 ? A SER 429 
138 1 Y 1 A VAL 380 ? A VAL 430 
139 1 Y 1 A SER 381 ? A SER 431 
140 1 Y 1 A ASN 382 ? A ASN 432 
141 1 Y 1 A MET 383 ? A MET 433 
142 1 Y 1 A VAL 384 ? A VAL 434 
143 1 Y 1 A HIS 385 ? A HIS 435 
144 1 Y 1 A THR 386 ? A THR 436 
145 1 Y 1 A ALA 387 ? A ALA 437 
146 1 Y 1 A LYS 388 ? A LYS 438 
147 1 Y 1 A LYS 389 ? A LYS 439 
148 1 Y 1 A LYS 390 ? A LYS 440 
149 1 Y 1 A ILE 391 ? A ILE 441 
150 1 Y 1 A ARG 392 ? A ARG 442 
151 1 Y 1 A LYS 393 ? A LYS 443 
152 1 Y 1 A HIS 394 ? A HIS 444 
153 1 Y 1 A ARG 395 ? A ARG 445 
154 1 Y 1 A GLY 396 ? A GLY 446 
155 1 Y 1 A VAL 397 ? A VAL 447 
156 1 Y 1 A GLU 398 ? A GLU 448 
157 1 Y 1 A GLU 399 ? A GLU 449 
158 1 Y 1 A SER 400 ? A SER 450 
159 1 Y 1 A PRO 401 ? A PRO 451 
160 1 Y 1 A LEU 402 ? A LEU 452 
161 1 Y 1 A ASN 403 ? A ASN 453 
162 1 Y 1 A ASN 404 ? A ASN 454 
163 1 Y 1 A ASP 405 ? A ASP 455 
164 1 Y 1 A VAL 406 ? A VAL 456 
165 1 Y 1 A LEU 407 ? A LEU 457 
166 1 Y 1 A ASN 408 ? A ASN 458 
167 1 Y 1 A THR 409 ? A THR 459 
168 1 Y 1 A ILE 410 ? A ILE 460 
169 1 Y 1 A LEU 411 ? A LEU 461 
170 1 Y 1 A LEU 412 ? A LEU 462 
171 1 Y 1 A PHE 413 ? A PHE 463 
172 1 Y 1 A LEU 414 ? A LEU 464 
173 1 Y 1 A PHE 415 ? A PHE 465 
174 1 Y 1 A PRO 416 ? A PRO 466 
175 1 Y 1 A ASP 417 ? A ASP 467 
176 1 Y 1 A ALA 418 ? A ALA 468 
177 1 Y 1 A VAL 419 ? A VAL 469 
178 1 Y 1 A SER 420 ? A SER 470 
179 1 Y 1 A GLU 421 ? A GLU 471 
180 1 Y 1 A LYS 422 ? A LYS 472 
181 1 Y 1 A PRO 423 ? A PRO 473 
182 1 Y 1 A LEU 424 ? A LEU 474 
183 1 Y 1 A ASP 425 ? A ASP 475 
184 1 Y 1 A GLY 426 ? A GLY 476 
185 1 Y 1 A THR 427 ? A THR 477 
186 1 Y 1 A THR 428 ? A THR 478 
187 1 Y 1 A SER 429 ? A SER 479 
188 1 Y 1 A THR 430 ? A THR 480 
189 1 Y 1 A ASP 431 ? A ASP 481 
190 1 Y 1 A ASN 432 ? A ASN 482 
191 1 Y 1 A ASN 433 ? A ASN 483 
192 1 Y 1 A ASN 434 ? A ASN 484 
193 1 Y 1 A PRO 435 ? A PRO 485 
194 1 Y 1 A PRO 436 ? A PRO 486 
195 1 Y 1 A SER 437 ? A SER 487 
196 1 Y 1 A GLU 438 ? A GLU 488 
197 1 Y 1 A SER 439 ? A SER 489 
198 1 Y 1 A GLU 440 ? A GLU 490 
199 1 Y 1 A ASP 441 ? A ASP 491 
200 1 Y 1 A TYR 442 ? A TYR 492 
201 1 Y 1 A ASN 443 ? A ASN 493 
202 1 Y 1 A LEU 444 ? A LEU 494 
203 1 Y 1 A TYR 445 ? A TYR 495 
204 1 Y 1 A ASN 446 ? A ASN 496 
205 1 Y 1 A GLN 447 ? A GLN 497 
206 1 Y 1 A PHE 448 ? A PHE 498 
207 1 Y 1 A LYS 449 ? A LYS 499 
208 1 Y 1 A SER 450 ? A SER 500 
209 1 Y 1 A ALA 451 ? A ALA 501 
210 1 Y 1 A PRO 452 ? A PRO 502 
211 1 Y 1 A SER 453 ? A SER 503 
212 1 Y 1 A ASP 454 ? A ASP 504 
213 1 Y 1 A SER 455 ? A SER 505 
214 1 Y 1 A LEU 456 ? A LEU 506 
215 1 Y 1 A THR 457 ? A THR 507 
216 1 Y 1 A TYR 458 ? A TYR 508 
217 1 Y 1 A LYS 459 ? A LYS 509 
218 1 Y 1 A LEU 460 ? A LEU 510 
219 1 Y 1 A ALA 461 ? A ALA 511 
220 1 Y 1 A LEU 462 ? A LEU 512 
221 1 Y 1 A CYS 463 ? A CYS 513 
222 1 Y 1 A LEU 464 ? A LEU 514 
223 1 Y 1 A CYS 465 ? A CYS 515 
224 1 Y 1 A MET 466 ? A MET 516 
225 1 Y 1 A ILE 467 ? A ILE 517 
226 1 Y 1 A ASN 468 ? A ASN 518 
227 1 Y 1 A PHE 469 ? A PHE 519 
228 1 Y 1 A TYR 470 ? A TYR 520 
229 1 Y 1 A HIS 471 ? A HIS 521 
230 1 Y 1 A GLY 472 ? A GLY 522 
231 1 Y 1 A GLY 473 ? A GLY 523 
232 1 Y 1 A LEU 474 ? A LEU 524 
233 1 Y 1 A LYS 475 ? A LYS 525 
234 1 Y 1 A GLY 476 ? A GLY 526 
235 1 Y 1 A VAL 477 ? A VAL 527 
236 1 Y 1 A ALA 478 ? A ALA 528 
237 1 Y 1 A HIS 479 ? A HIS 529 
238 1 Y 1 A LEU 480 ? A LEU 530 
239 1 Y 1 A TRP 481 ? A TRP 531 
240 1 Y 1 A GLN 482 ? A GLN 532 
241 1 Y 1 A GLU 483 ? A GLU 533 
242 1 Y 1 A PHE 484 ? A PHE 534 
243 1 Y 1 A VAL 485 ? A VAL 535 
244 1 Y 1 A LEU 486 ? A LEU 536 
245 1 Y 1 A GLU 487 ? A GLU 537 
246 1 Y 1 A MET 488 ? A MET 538 
247 1 Y 1 A ARG 489 ? A ARG 539 
248 1 Y 1 A PHE 490 ? A PHE 540 
249 1 Y 1 A ARG 491 ? A ARG 541 
250 1 Y 1 A TRP 492 ? A TRP 542 
251 1 Y 1 A GLU 493 ? A GLU 543 
252 1 Y 1 A ASN 494 ? A ASN 544 
253 1 Y 1 A ASN 495 ? A ASN 545 
254 1 Y 1 A PHE 496 ? A PHE 546 
255 1 Y 1 A LEU 497 ? A LEU 547 
256 1 Y 1 A ILE 498 ? A ILE 548 
257 1 Y 1 A PRO 499 ? A PRO 549 
258 1 Y 1 A GLY 500 ? A GLY 550 
259 1 Y 1 A LEU 501 ? A LEU 551 
260 1 Y 1 A ALA 502 ? A ALA 552 
261 1 Y 1 A SER 503 ? A SER 553 
262 1 Y 1 A GLY 504 ? A GLY 554 
263 1 Y 1 A PRO 505 ? A PRO 555 
264 1 Y 1 A PRO 506 ? A PRO 556 
265 1 Y 1 A ASP 507 ? A ASP 557 
266 1 Y 1 A LEU 508 ? A LEU 558 
267 1 Y 1 A ARG 509 ? A ARG 559 
268 1 Y 1 A CYS 510 ? A CYS 560 
269 1 Y 1 A CYS 511 ? A CYS 561 
270 1 Y 1 A LEU 512 ? A LEU 562 
271 1 Y 1 A LEU 513 ? A LEU 563 
272 1 Y 1 A HIS 514 ? A HIS 564 
273 1 Y 1 A GLN 515 ? A GLN 565 
274 1 Y 1 A LYS 516 ? A LYS 566 
275 1 Y 1 A LEU 517 ? A LEU 567 
276 1 Y 1 A GLN 518 ? A GLN 568 
277 1 Y 1 A MET 519 ? A MET 569 
278 1 Y 1 A LEU 520 ? A LEU 570 
279 1 Y 1 A ASN 521 ? A ASN 571 
280 1 Y 1 A CYS 522 ? A CYS 572 
281 1 Y 1 A CYS 523 ? A CYS 573 
282 1 Y 1 A ILE 524 ? A ILE 574 
283 1 Y 1 A GLU 525 ? A GLU 575 
284 1 Y 1 A ARG 526 ? A ARG 576 
285 1 Y 1 A LYS 527 ? A LYS 577 
286 1 Y 1 A LYS 528 ? A LYS 578 
287 1 Y 1 A ALA 529 ? A ALA 579 
288 1 Y 1 A ARG 530 ? A ARG 580 
289 1 Y 1 A ASP 531 ? A ASP 581 
290 1 Y 1 A GLU 532 ? A GLU 582 
291 1 Y 1 A GLY 533 ? A GLY 583 
292 1 Y 1 A LYS 534 ? A LYS 584 
293 1 Y 1 A LYS 535 ? A LYS 585 
294 1 Y 1 A THR 536 ? A THR 586 
295 1 Y 1 A SER 537 ? A SER 587 
296 1 Y 1 A ALA 538 ? A ALA 588 
297 1 Y 1 A SER 539 ? A SER 589 
298 1 Y 1 A ASP 540 ? A ASP 590 
299 1 Y 1 A VAL 541 ? A VAL 591 
300 1 Y 1 A THR 542 ? A THR 592 
301 1 Y 1 A ASN 543 ? A ASN 593 
302 1 Y 1 A ILE 544 ? A ILE 594 
303 1 Y 1 A TYR 545 ? A TYR 595 
304 1 Y 1 A PRO 546 ? A PRO 596 
305 1 Y 1 A GLY 547 ? A GLY 597 
306 1 Y 1 A ASP 548 ? A ASP 598 
307 1 Y 1 A ALA 549 ? A ALA 599 
308 1 Y 1 A GLY 550 ? A GLY 600 
309 1 Y 1 A LYS 551 ? A LYS 601 
310 1 Y 1 A ALA 552 ? A ALA 602 
311 1 Y 1 A GLY 553 ? A GLY 603 
312 1 Y 1 A ASP 554 ? A ASP 604 
313 1 Y 1 A GLN 555 ? A GLN 605 
314 1 Y 1 A LEU 556 ? A LEU 606 
315 1 Y 1 A VAL 557 ? A VAL 607 
316 1 Y 1 A PRO 558 ? A PRO 608 
317 1 Y 1 A ASP 559 ? A ASP 609 
318 1 Y 1 A ASN 560 ? A ASN 610 
319 1 Y 1 A LEU 561 ? A LEU 611 
320 1 Y 1 A LYS 562 ? A LYS 612 
321 1 Y 1 A GLU 563 ? A GLU 613 
322 1 Y 1 A THR 564 ? A THR 614 
323 1 Y 1 A ASP 565 ? A ASP 615 
324 1 Y 1 A LYS 566 ? A LYS 616 
325 1 Y 1 A GLU 567 ? A GLU 617 
326 1 Y 1 A LYS 568 ? A LYS 618 
327 1 Y 1 A GLY 569 ? A GLY 619 
328 1 Y 1 A GLU 570 ? A GLU 620 
329 1 Y 1 A VAL 571 ? A VAL 621 
330 1 Y 1 A GLY 572 ? A GLY 622 
331 1 Y 1 A LYS 573 ? A LYS 623 
332 1 Y 1 A SER 574 ? A SER 624 
333 1 Y 1 A TRP 575 ? A TRP 625 
334 1 Y 1 A ASP 576 ? A ASP 626 
335 1 Y 1 A SER 577 ? A SER 627 
336 1 Y 1 A TRP 578 ? A TRP 628 
337 1 Y 1 A SER 579 ? A SER 629 
338 1 Y 1 A ASP 580 ? A ASP 630 
339 1 Y 1 A SER 581 ? A SER 631 
340 1 Y 1 A GLU 582 ? A GLU 632 
341 1 Y 1 A GLU 583 ? A GLU 633 
342 1 Y 1 A GLU 584 ? A GLU 634 
343 1 Y 1 A PHE 585 ? A PHE 635 
344 1 Y 1 A PHE 586 ? A PHE 636 
345 1 Y 1 A GLU 587 ? A GLU 637 
346 1 Y 1 A CYS 588 ? A CYS 638 
347 1 Y 1 A LEU 589 ? A LEU 639 
348 1 Y 1 A SER 590 ? A SER 640 
349 1 Y 1 A ASP 591 ? A ASP 641 
350 1 Y 1 A THR 592 ? A THR 642 
351 1 Y 1 A GLU 593 ? A GLU 643 
352 1 Y 1 A GLU 594 ? A GLU 644 
353 1 Y 1 A LEU 595 ? A LEU 645 
354 1 Y 1 A LYS 596 ? A LYS 646 
355 1 Y 1 A GLY 597 ? A GLY 647 
356 1 Y 1 A ASN 598 ? A ASN 648 
357 1 Y 1 A GLY 599 ? A GLY 649 
358 1 Y 1 A GLN 600 ? A GLN 650 
359 1 Y 1 A GLU 601 ? A GLU 651 
360 1 Y 1 A SER 602 ? A SER 652 
361 1 Y 1 A GLY 603 ? A GLY 653 
362 1 Y 1 A LYS 604 ? A LYS 654 
363 1 Y 1 A LYS 605 ? A LYS 655 
364 1 Y 1 A GLY 606 ? A GLY 656 
365 1 Y 1 A GLY 607 ? A GLY 657 
366 1 Y 1 A PRO 608 ? A PRO 658 
367 1 Y 1 A LYS 609 ? A LYS 659 
368 1 Y 1 A GLU 610 ? A GLU 660 
369 1 Y 1 A MET 611 ? A MET 661 
370 1 Y 1 A ALA 612 ? A ALA 662 
371 1 Y 1 A ASN 613 ? A ASN 663 
372 1 Y 1 A LEU 614 ? A LEU 664 
373 1 Y 1 A ARG 615 ? A ARG 665 
374 1 Y 1 A PRO 616 ? A PRO 666 
375 1 Y 1 A GLU 617 ? A GLU 667 
376 1 Y 1 A GLY 618 ? A GLY 668 
377 1 Y 1 A ARG 619 ? A ARG 669 
378 1 Y 1 A LEU 620 ? A LEU 670 
379 1 Y 1 A TYR 621 ? A TYR 671 
380 1 Y 1 A GLN 622 ? A GLN 672 
381 1 Y 1 A HIS 623 ? A HIS 673 
382 1 Y 1 A GLY 624 ? A GLY 674 
383 1 Y 1 A LYS 625 ? A LYS 675 
384 1 Y 1 A LEU 626 ? A LEU 676 
385 1 Y 1 A THR 627 ? A THR 677 
386 1 Y 1 A LEU 628 ? A LEU 678 
387 1 Y 1 A LEU 629 ? A LEU 679 
388 1 Y 1 A HIS 630 ? A HIS 680 
389 1 Y 1 A ASN 631 ? A ASN 681 
390 1 Y 1 A GLY 632 ? A GLY 682 
391 1 Y 1 A GLU 633 ? A GLU 683 
392 1 Y 1 A PRO 634 ? A PRO 684 
393 1 Y 1 A LEU 635 ? A LEU 685 
394 1 Y 1 A TYR 636 ? A TYR 686 
395 1 Y 1 A ILE 637 ? A ILE 687 
396 1 Y 1 A PRO 638 ? A PRO 688 
397 1 Y 1 A VAL 639 ? A VAL 689 
398 1 Y 1 A THR 640 ? A THR 690 
399 1 Y 1 A GLN 641 ? A GLN 691 
400 1 Y 1 A GLU 642 ? A GLU 692 
401 1 Y 1 A PRO 643 ? A PRO 693 
402 1 Y 1 A ALA 644 ? A ALA 694 
403 1 Y 1 A PRO 645 ? A PRO 695 
404 1 Y 1 A MET 646 ? A MET 696 
405 1 Y 1 A THR 647 ? A THR 697 
406 1 Y 1 A GLU 648 ? A GLU 698 
407 1 Y 1 A ASP 649 ? A ASP 699 
408 1 Y 1 A LEU 650 ? A LEU 700 
409 1 Y 1 A LEU 651 ? A LEU 701 
410 1 Y 1 A GLU 652 ? A GLU 702 
411 1 Y 1 A GLU 653 ? A GLU 703 
412 1 Y 1 A GLN 654 ? A GLN 704 
413 1 Y 1 A SER 655 ? A SER 705 
414 1 Y 1 A GLU 656 ? A GLU 706 
415 1 Y 1 A VAL 657 ? A VAL 707 
416 1 Y 1 A LEU 658 ? A LEU 708 
417 1 Y 1 A ALA 659 ? A ALA 709 
418 1 Y 1 A LYS 660 ? A LYS 710 
419 1 Y 1 A LEU 661 ? A LEU 711 
420 1 Y 1 A GLY 662 ? A GLY 712 
421 1 Y 1 A THR 663 ? A THR 713 
422 1 Y 1 A SER 664 ? A SER 714 
423 1 Y 1 A ALA 665 ? A ALA 715 
424 1 Y 1 A GLU 666 ? A GLU 716 
425 1 Y 1 A GLY 667 ? A GLY 717 
426 1 Y 1 A ALA 668 ? A ALA 718 
427 1 Y 1 A HIS 669 ? A HIS 719 
428 1 Y 1 A LEU 670 ? A LEU 720 
429 1 Y 1 A ARG 671 ? A ARG 721 
430 1 Y 1 A ALA 672 ? A ALA 722 
431 1 Y 1 A ARG 673 ? A ARG 723 
432 1 Y 1 A MET 674 ? A MET 724 
433 1 Y 1 A GLN 675 ? A GLN 725 
434 1 Y 1 A SER 676 ? A SER 726 
435 1 Y 1 A ALA 677 ? A ALA 727 
436 1 Y 1 A CYS 678 ? A CYS 728 
437 1 Y 1 A LEU 679 ? A LEU 729 
438 1 Y 1 A LEU 680 ? A LEU 730 
439 1 Y 1 A SER 681 ? A SER 731 
440 1 Y 1 A ASP 682 ? A ASP 732 
441 1 Y 1 A MET 683 ? A MET 733 
442 1 Y 1 A GLU 684 ? A GLU 734 
443 1 Y 1 A SER 685 ? A SER 735 
444 1 Y 1 A PHE 686 ? A PHE 736 
445 1 Y 1 A LYS 687 ? A LYS 737 
446 1 Y 1 A ALA 688 ? A ALA 738 
447 1 Y 1 A ALA 689 ? A ALA 739 
448 1 Y 1 A ASN 690 ? A ASN 740 
449 1 Y 1 A PRO 691 ? A PRO 741 
450 1 Y 1 A GLY 692 ? A GLY 742 
451 1 Y 1 A CYS 693 ? A CYS 743 
452 1 Y 1 A SER 694 ? A SER 744 
453 1 Y 1 A LEU 695 ? A LEU 745 
454 1 Y 1 A GLU 696 ? A GLU 746 
455 1 Y 1 A ASP 697 ? A ASP 747 
456 1 Y 1 A PHE 698 ? A PHE 748 
457 1 Y 1 A VAL 699 ? A VAL 749 
458 1 Y 1 A ARG 700 ? A ARG 750 
459 1 Y 1 A TRP 701 ? A TRP 751 
460 1 Y 1 A TYR 702 ? A TYR 752 
461 1 Y 1 A SER 703 ? A SER 753 
462 1 Y 1 A PRO 704 ? A PRO 754 
463 1 Y 1 A ARG 705 ? A ARG 755 
464 1 Y 1 A ASP 706 ? A ASP 756 
465 1 Y 1 A TYR 707 ? A TYR 757 
466 1 Y 1 A ILE 708 ? A ILE 758 
467 1 Y 1 A GLU 709 ? A GLU 759 
468 1 Y 1 A GLU 710 ? A GLU 760 
469 1 Y 1 A GLU 711 ? A GLU 761 
470 1 Y 1 A VAL 712 ? A VAL 762 
471 1 Y 1 A ILE 713 ? A ILE 763 
472 1 Y 1 A ASP 714 ? A ASP 764 
473 1 Y 1 A GLU 715 ? A GLU 765 
474 1 Y 1 A LYS 716 ? A LYS 766 
475 1 Y 1 A GLY 717 ? A GLY 767 
476 1 Y 1 A ASN 718 ? A ASN 768 
477 1 Y 1 A VAL 719 ? A VAL 769 
478 1 Y 1 A VAL 720 ? A VAL 770 
479 1 Y 1 A LEU 721 ? A LEU 771 
480 1 Y 1 A LYS 722 ? A LYS 772 
481 1 Y 1 A GLY 723 ? A GLY 773 
482 1 Y 1 A GLU 724 ? A GLU 774 
483 1 Y 1 A LEU 725 ? A LEU 775 
484 1 Y 1 A SER 726 ? A SER 776 
485 1 Y 1 A ALA 727 ? A ALA 777 
486 1 Y 1 A ARG 728 ? A ARG 778 
487 1 Y 1 A MET 729 ? A MET 779 
488 1 Y 1 A LYS 730 ? A LYS 780 
489 1 Y 1 A ILE 731 ? A ILE 781 
490 1 Y 1 A PRO 732 ? A PRO 782 
491 1 Y 1 A SER 733 ? A SER 783 
492 1 Y 1 A ASN 734 ? A ASN 784 
493 1 Y 1 A MET 735 ? A MET 785 
494 1 Y 1 A TRP 736 ? A TRP 786 
495 1 Y 1 A VAL 737 ? A VAL 787 
496 1 Y 1 A GLU 738 ? A GLU 788 
497 1 Y 1 A ALA 739 ? A ALA 789 
498 1 Y 1 A TRP 740 ? A TRP 790 
499 1 Y 1 A GLU 741 ? A GLU 791 
500 1 Y 1 A THR 742 ? A THR 792 
501 1 Y 1 A ALA 743 ? A ALA 793 
502 1 Y 1 A LYS 744 ? A LYS 794 
503 1 Y 1 A PRO 745 ? A PRO 795 
504 1 Y 1 A ILE 746 ? A ILE 796 
505 1 Y 1 A PRO 747 ? A PRO 797 
506 1 Y 1 A ALA 748 ? A ALA 798 
507 1 Y 1 A ARG 749 ? A ARG 799 
508 1 Y 1 A ARG 750 ? A ARG 800 
509 1 Y 1 A GLN 751 ? A GLN 801 
510 1 Y 1 A ARG 752 ? A ARG 802 
511 1 Y 1 A ARG 753 ? A ARG 803 
512 1 Y 1 A LEU 754 ? A LEU 804 
513 1 Y 1 A PHE 755 ? A PHE 805 
514 1 Y 1 A ASP 756 ? A ASP 806 
515 1 Y 1 A ASP 757 ? A ASP 807 
516 1 Y 1 A THR 758 ? A THR 808 
517 1 Y 1 A ARG 759 ? A ARG 809 
518 1 Y 1 A GLU 760 ? A GLU 810 
519 1 Y 1 A ALA 761 ? A ALA 811 
520 1 Y 1 A GLU 762 ? A GLU 812 
521 1 Y 1 A LYS 763 ? A LYS 813 
522 1 Y 1 A VAL 764 ? A VAL 814 
523 1 Y 1 A LEU 765 ? A LEU 815 
524 1 Y 1 A HIS 766 ? A HIS 816 
525 1 Y 1 A TYR 767 ? A TYR 817 
526 1 Y 1 A LEU 768 ? A LEU 818 
527 1 Y 1 A ALA 769 ? A ALA 819 
528 1 Y 1 A ILE 770 ? A ILE 820 
529 1 Y 1 A GLN 771 ? A GLN 821 
530 1 Y 1 A LYS 772 ? A LYS 822 
531 1 Y 1 A PRO 773 ? A PRO 823 
532 1 Y 1 A ALA 774 ? A ALA 824 
533 1 Y 1 A ASP 775 ? A ASP 825 
534 1 Y 1 A LEU 776 ? A LEU 826 
535 1 Y 1 A ALA 777 ? A ALA 827 
536 1 Y 1 A ARG 778 ? A ARG 828 
537 1 Y 1 A HIS 779 ? A HIS 829 
538 1 Y 1 A LEU 780 ? A LEU 830 
539 1 Y 1 A LEU 781 ? A LEU 831 
540 1 Y 1 A GLN 901 A A GLN 952 
541 1 Y 1 A ARG 901 B A ARG 953 
542 1 Y 1 A LEU 901 C A LEU 954 
543 1 Y 1 A THR 901 D A THR 955 
544 1 Y 1 A GLU 901 E A GLU 956 
545 1 Y 1 A SER 901 F A SER 957 
546 1 Y 1 A SER 901 G A SER 958 
547 1 Y 1 A ASP 901 H A ASP 959 
548 1 Y 1 A GLU 901 I A GLU 960 
549 1 Y 1 A ALA 901 J A ALA 961 
550 1 Y 1 A ALA 901 K A ALA 962 
551 1 Y 1 A ALA 901 L A ALA 963 
552 1 Y 1 A MET 901 M A MET 964 
553 1 Y 1 A THR 901 N A THR 965 
554 1 Y 1 A PRO 901 O A PRO 966 
555 1 Y 1 A PRO 901 P A PRO 967 
556 1 Y 1 A GLU 901 Q A GLU 968 
557 1 Y 1 A GLU 901 R A GLU 969 
558 1 Y 1 A GLU 901 S A GLU 970 
559 1 Y 1 A LEU 901 T A LEU 971 
560 1 Y 1 A LYS 901 U A LYS 972 
561 1 Y 1 A ARG 901 V A ARG 973 
562 1 Y 1 A MET 901 W A MET 974 
563 1 Y 1 A GLY 901 X A GLY 975 
564 1 Y 1 A SER 901 Y A SER 976 
565 1 Y 1 A PRO 901 Z A PRO 977 
566 1 Y 1 A GLU 902 A A GLU 978 
567 1 Y 1 A GLU 902 B A GLU 979 
568 1 Y 1 A ARG 902 C A ARG 980 
569 1 Y 1 A ARG 902 D A ARG 981 
570 1 Y 1 A GLN 902 E A GLN 982 
571 1 Y 1 A ASN 902 F A ASN 983 
572 1 Y 1 A SER 902 G A SER 984 
573 1 Y 1 A VAL 902 H A VAL 985 
574 1 Y 1 A SER 902 I A SER 986 
575 1 Y 1 B MET 1   ? B MET 1   
576 1 Y 1 B GLU 27  ? B GLU 27  
577 1 Y 1 B GLU 28  ? B GLU 28  
578 1 Y 1 B ILE 29  ? B ILE 29  
579 1 Y 1 B LEU 30  ? B LEU 30  
580 1 Y 1 B SER 31  ? B SER 31  
581 1 Y 1 B GLY 32  ? B GLY 32  
582 1 Y 1 B ALA 33  ? B ALA 33  
583 1 Y 1 B LEU 34  ? B LEU 34  
584 1 Y 1 B ARG 35  ? B ARG 35  
585 1 Y 1 B ARG 36  ? B ARG 36  
586 1 Y 1 B ASP 37  ? B ASP 37  
587 1 Y 1 B PRO 38  ? B PRO 38  
588 1 Y 1 B SER 39  ? B SER 39  
589 1 Y 1 B LYS 40  ? B LYS 40  
590 1 Y 1 B SER 41  ? B SER 41  
591 1 Y 1 B THR 42  ? B THR 42  
592 1 Y 1 B ASP 43  ? B ASP 43  
593 1 Y 1 B TRP 44  ? B TRP 44  
594 1 Y 1 B GLU 45  ? B GLU 45  
595 1 Y 1 B ASP 46  ? B ASP 46  
596 1 Y 1 B ASP 47  ? B ASP 47  
597 1 Y 1 B GLY 48  ? B GLY 48  
598 1 Y 1 B TRP 49  ? B TRP 49  
599 1 Y 1 B GLY 50  ? B GLY 50  
600 1 Y 1 B ALA 51  ? B ALA 51  
601 1 Y 1 B TRP 52  ? B TRP 52  
602 1 Y 1 B GLU 53  ? B GLU 53  
603 1 Y 1 B GLU 54  ? B GLU 54  
604 1 Y 1 B ASN 55  ? B ASN 55  
605 1 Y 1 B GLU 56  ? B GLU 56  
606 1 Y 1 B PRO 57  ? B PRO 57  
607 1 Y 1 B GLN 58  ? B GLN 58  
608 1 Y 1 B GLU 59  ? B GLU 59  
609 1 Y 1 B PRO 60  ? B PRO 60  
610 1 Y 1 B SER 328 ? B SER 328 
611 1 Y 1 B HIS 329 ? B HIS 329 
612 1 Y 1 B VAL 330 ? B VAL 330 
613 1 Y 1 B ALA 331 ? B ALA 331 
614 1 Y 1 B LEU 332 ? B LEU 332 
615 1 Y 1 B ALA 333 ? B ALA 333 
616 1 Y 1 B VAL 334 ? B VAL 334 
617 1 Y 1 B ALA 335 ? B ALA 335 
618 1 Y 1 B SER 336 ? B SER 336 
619 1 Y 1 B LYS 337 ? B LYS 337 
620 1 Y 1 B LEU 338 ? B LEU 338 
621 1 Y 1 B THR 339 ? B THR 339 
622 1 Y 1 B SER 340 ? B SER 340 
623 1 Y 1 B ALA 341 ? B ALA 341 
624 1 Y 1 B LEU 342 ? B LEU 342 
625 1 Y 1 B PHE 343 ? B PHE 343 
626 1 Y 1 B ASN 344 ? B ASN 344 
627 1 Y 1 B ALA 345 ? B ALA 345 
628 1 Y 1 B ALA 346 ? B ALA 346 
629 1 Y 1 B SER 347 ? B SER 347 
630 1 Y 1 B GLY 348 ? B GLY 348 
631 1 Y 1 B TRP 349 ? B TRP 349 
632 1 Y 1 B LEU 350 ? B LEU 350 
633 1 Y 1 B GLY 351 ? B GLY 351 
634 1 Y 1 B TRP 352 ? B TRP 352 
635 1 Y 1 B LYS 353 ? B LYS 353 
636 1 Y 1 B SER 354 ? B SER 354 
637 1 Y 1 B LYS 355 ? B LYS 355 
638 1 Y 1 B HIS 356 ? B HIS 356 
639 1 Y 1 B GLU 357 ? B GLU 357 
640 1 Y 1 B GLU 358 ? B GLU 358 
641 1 Y 1 B GLU 359 ? B GLU 359 
642 1 Y 1 B ALA 360 ? B ALA 360 
643 1 Y 1 B VAL 361 ? B VAL 361 
644 1 Y 1 B GLN 362 ? B GLN 362 
645 1 Y 1 B LYS 363 ? B LYS 363 
646 1 Y 1 B HIS 440 ? B HIS 440 
647 1 Y 1 B GLU 441 ? B GLU 441 
648 1 Y 1 B ARG 442 ? B ARG 442 
649 1 Y 1 B VAL 443 ? B VAL 443 
650 1 Y 1 B PRO 444 ? B PRO 444 
651 1 Y 1 B GLU 445 ? B GLU 445 
652 1 Y 1 B LYS 446 ? B LYS 446 
653 1 Y 1 B ALA 447 ? B ALA 447 
654 1 Y 1 B ASP 448 ? B ASP 448 
655 1 Y 1 B PHE 449 ? B PHE 449 
656 1 Y 1 B SER 450 ? B SER 450 
657 1 Y 1 B PRO 451 ? B PRO 451 
658 1 Y 1 B PHE 452 ? B PHE 452 
659 1 Y 1 B GLY 453 ? B GLY 453 
660 1 Y 1 B ASN 454 ? B ASN 454 
661 1 Y 1 B SER 455 ? B SER 455 
662 1 Y 1 B GLN 456 ? B GLN 456 
663 1 Y 1 B ASP 545 ? B ASP 545 
664 1 Y 1 B LYS 546 ? B LYS 546 
665 1 Y 1 B LYS 547 ? B LYS 547 
666 1 Y 1 B LEU 548 ? B LEU 548 
667 1 Y 1 B ARG 549 ? B ARG 549 
668 1 Y 1 B GLU 550 ? B GLU 550 
669 1 Y 1 B GLN 551 ? B GLN 551 
670 1 Y 1 B LYS 552 ? B LYS 552 
671 1 Y 1 B LEU 553 ? B LEU 553 
672 1 Y 1 B GLU 554 ? B GLU 554 
673 1 Y 1 B LEU 555 ? B LEU 555 
674 1 Y 1 B GLY 556 ? B GLY 556 
675 1 Y 1 B GLY 557 ? B GLY 557 
676 1 Y 1 B SER 558 ? B SER 558 
677 1 Y 1 B GLY 559 ? B GLY 559 
678 1 Y 1 B GLY 560 ? B GLY 560 
679 1 Y 1 B ARG 561 ? B ARG 561 
680 1 Y 1 B GLN 562 ? B GLN 562 
681 1 Y 1 B LEU 563 ? B LEU 563 
682 1 Y 1 B ASP 564 ? B ASP 564 
683 1 Y 1 B TYR 565 ? B TYR 565 
684 1 Y 1 B LYS 566 ? B LYS 566 
685 1 Y 1 B ASP 567 ? B ASP 567 
686 1 Y 1 B HIS 568 ? B HIS 568 
687 1 Y 1 B ASP 569 ? B ASP 569 
688 1 Y 1 B GLY 570 ? B GLY 570 
689 1 Y 1 B ASP 571 ? B ASP 571 
690 1 Y 1 B TYR 572 ? B TYR 572 
691 1 Y 1 B LYS 573 ? B LYS 573 
692 1 Y 1 B ASP 574 ? B ASP 574 
693 1 Y 1 B HIS 575 ? B HIS 575 
694 1 Y 1 B ASP 576 ? B ASP 576 
695 1 Y 1 B ILE 577 ? B ILE 577 
696 1 Y 1 B ASP 578 ? B ASP 578 
697 1 Y 1 B TYR 579 ? B TYR 579 
698 1 Y 1 B LYS 580 ? B LYS 580 
699 1 Y 1 B ASP 581 ? B ASP 581 
700 1 Y 1 B ASP 582 ? B ASP 582 
701 1 Y 1 B ASP 583 ? B ASP 583 
702 1 Y 1 B ASP 584 ? B ASP 584 
703 1 Y 1 B LYS 585 ? B LYS 585 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-02-07 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           8VYB 
_em_admin.last_update        2025-01-15 
_em_admin.map_release_date   2025-01-15 
_em_admin.title              'Cryo-EM structure of human core Rab3GAP1/2 complex, local refinement' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM C8H18N2O4S 1 HEPES             
1 150 mM NaCl       2 'Sodium chloride' 
1 1   mM C9H15O6P   3 TCEP              
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_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 
? ? 1 2 9606 'Homo sapiens' ? ? ? ? ? 
? ? 2 3 9606 'Homo sapiens' ? ? ? ? ? 
? ? 3 4 9606 'Homo sapiens' ? ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 1 2 7108 'Spodoptera frugiperda' pBIG1A ? 
? 2 3 7108 'Spodoptera frugiperda' pBIG1A ? 
? 3 4 7108 'Spodoptera frugiperda' pBIG1A ? 
# 
_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         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (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                     ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   12427326 
_em_particle_selection.reference_model          ? 
# 
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 ? ? cryoSPARC 4.2.1       
'IMAGE ACQUISITION'        ? 2  ? ? 1 ?         ?           
MASKING                    ? 3  ? ? ? ?         ?           
'CTF CORRECTION'           ? 4  1 ? ? cryoSPARC 4.2.1       
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ?           
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ?           
'MODEL FITTING'            ? 7  ? 1 ? PHENIX    1.20.1-4487 
OTHER                      ? 8  ? ? ? ?         ?           
'MODEL REFINEMENT'         ? 9  ? 1 ? Coot      0.9.8.8     
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? cryoSPARC 4.2.1       
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4.2.1       
CLASSIFICATION             ? 12 1 ? ? cryoSPARC 4.2.1       
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4.2.1       
# 
_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 
'Canadian Institutes of Health Research (CIHR)'                     Canada PJT-168907       1 
'Natural Sciences and Engineering Research Council (NSERC, Canada)' Canada RGPIN-2018-03951 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
# 
_atom_sites.entry_id                    8VYB 
_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 
N 
O 
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   . THR A 1 69   ? 193.478 211.457 167.689 1.00 19.96 ? 19  THR A N   1 
ATOM 2    C CA  . THR A 1 69   ? 192.440 210.448 167.862 1.00 18.16 ? 19  THR A CA  1 
ATOM 3    C C   . THR A 1 69   ? 191.855 210.513 169.266 1.00 12.58 ? 19  THR A C   1 
ATOM 4    O O   . THR A 1 69   ? 191.009 211.359 169.556 1.00 18.55 ? 19  THR A O   1 
ATOM 5    C CB  . THR A 1 69   ? 192.985 209.039 167.606 1.00 18.94 ? 19  THR A CB  1 
ATOM 6    O OG1 . THR A 1 69   ? 194.167 208.837 168.390 1.00 15.80 ? 19  THR A OG1 1 
ATOM 7    C CG2 . THR A 1 69   ? 193.320 208.860 166.133 1.00 16.77 ? 19  THR A CG2 1 
ATOM 8    N N   . ALA A 1 70   ? 192.311 209.601 170.126 1.00 14.13 ? 20  ALA A N   1 
ATOM 9    C CA  . ALA A 1 70   ? 191.956 209.590 171.546 1.00 20.57 ? 20  ALA A CA  1 
ATOM 10   C C   . ALA A 1 70   ? 190.445 209.566 171.764 1.00 21.95 ? 20  ALA A C   1 
ATOM 11   O O   . ALA A 1 70   ? 189.927 210.211 172.680 1.00 22.64 ? 20  ALA A O   1 
ATOM 12   C CB  . ALA A 1 70   ? 192.586 210.778 172.279 1.00 19.58 ? 20  ALA A CB  1 
ATOM 13   N N   . SER A 1 71   ? 189.724 208.821 170.929 1.00 19.96 ? 21  SER A N   1 
ATOM 14   C CA  . SER A 1 71   ? 188.308 208.590 171.178 1.00 18.09 ? 21  SER A CA  1 
ATOM 15   C C   . SER A 1 71   ? 188.136 207.745 172.438 1.00 17.28 ? 21  SER A C   1 
ATOM 16   O O   . SER A 1 71   ? 189.110 207.264 173.022 1.00 12.66 ? 21  SER A O   1 
ATOM 17   C CB  . SER A 1 71   ? 187.659 207.910 169.971 1.00 14.73 ? 21  SER A CB  1 
ATOM 18   O OG  . SER A 1 71   ? 187.669 206.500 170.105 1.00 24.37 ? 21  SER A OG  1 
ATOM 19   N N   . GLU A 1 72   ? 186.881 207.565 172.862 1.00 15.69 ? 22  GLU A N   1 
ATOM 20   C CA  . GLU A 1 72   ? 186.617 206.925 174.149 1.00 22.83 ? 22  GLU A CA  1 
ATOM 21   C C   . GLU A 1 72   ? 187.221 205.526 174.243 1.00 27.99 ? 22  GLU A C   1 
ATOM 22   O O   . GLU A 1 72   ? 187.843 205.175 175.252 1.00 37.13 ? 22  GLU A O   1 
ATOM 23   C CB  . GLU A 1 72   ? 185.109 206.879 174.415 1.00 23.80 ? 22  GLU A CB  1 
ATOM 24   C CG  . GLU A 1 72   ? 184.492 208.240 174.698 1.00 23.09 ? 22  GLU A CG  1 
ATOM 25   C CD  . GLU A 1 72   ? 183.011 208.162 175.012 1.00 26.37 ? 22  GLU A CD  1 
ATOM 26   O OE1 . GLU A 1 72   ? 182.423 207.070 174.864 1.00 29.01 ? 22  GLU A OE1 1 
ATOM 27   O OE2 . GLU A 1 72   ? 182.434 209.195 175.410 1.00 29.80 ? 22  GLU A OE2 1 
ATOM 28   N N   . TRP A 1 73   ? 187.051 204.726 173.188 1.00 8.14  ? 23  TRP A N   1 
ATOM 29   C CA  . TRP A 1 73   ? 187.674 203.377 173.184 1.00 1.95  ? 23  TRP A CA  1 
ATOM 30   C C   . TRP A 1 73   ? 189.197 203.525 173.246 1.00 8.12  ? 23  TRP A C   1 
ATOM 31   O O   . TRP A 1 73   ? 189.829 202.844 174.082 1.00 22.70 ? 23  TRP A O   1 
ATOM 32   C CB  . TRP A 1 73   ? 187.238 202.567 171.957 1.00 7.97  ? 23  TRP A CB  1 
ATOM 33   C CG  . TRP A 1 73   ? 187.193 201.084 172.218 1.00 15.57 ? 23  TRP A CG  1 
ATOM 34   C CD1 . TRP A 1 73   ? 187.150 200.473 173.436 1.00 9.59  ? 23  TRP A CD1 1 
ATOM 35   C CD2 . TRP A 1 73   ? 187.193 200.025 171.237 1.00 11.63 ? 23  TRP A CD2 1 
ATOM 36   N NE1 . TRP A 1 73   ? 187.121 199.112 173.286 1.00 5.11  ? 23  TRP A NE1 1 
ATOM 37   C CE2 . TRP A 1 73   ? 187.147 198.807 171.950 1.00 2.92  ? 23  TRP A CE2 1 
ATOM 38   C CE3 . TRP A 1 73   ? 187.227 199.986 169.839 1.00 4.15  ? 23  TRP A CE3 1 
ATOM 39   C CZ2 . TRP A 1 73   ? 187.134 197.571 171.309 1.00 4.88  ? 23  TRP A CZ2 1 
ATOM 40   C CZ3 . TRP A 1 73   ? 187.214 198.762 169.208 1.00 7.78  ? 23  TRP A CZ3 1 
ATOM 41   C CH2 . TRP A 1 73   ? 187.169 197.574 169.935 1.00 16.32 ? 23  TRP A CH2 1 
ATOM 42   N N   . GLU A 1 74   ? 189.761 204.408 172.417 1.00 0.00  ? 24  GLU A N   1 
ATOM 43   C CA  . GLU A 1 74   ? 191.233 204.620 172.394 1.00 0.00  ? 24  GLU A CA  1 
ATOM 44   C C   . GLU A 1 74   ? 191.688 205.175 173.748 1.00 12.42 ? 24  GLU A C   1 
ATOM 45   O O   . GLU A 1 74   ? 192.747 204.738 174.236 1.00 22.85 ? 24  GLU A O   1 
ATOM 46   C CB  . GLU A 1 74   ? 191.612 205.579 171.266 1.00 8.99  ? 24  GLU A CB  1 
ATOM 47   C CG  . GLU A 1 74   ? 190.754 205.407 170.030 1.00 12.99 ? 24  GLU A CG  1 
ATOM 48   C CD  . GLU A 1 74   ? 191.197 206.248 168.847 1.00 11.16 ? 24  GLU A CD  1 
ATOM 49   O OE1 . GLU A 1 74   ? 190.425 207.132 168.431 1.00 12.82 ? 24  GLU A OE1 1 
ATOM 50   O OE2 . GLU A 1 74   ? 192.306 206.002 168.336 1.00 5.06  ? 24  GLU A OE2 1 
ATOM 51   N N   . ARG A 1 75   ? 190.914 206.103 174.315 1.00 13.74 ? 25  ARG A N   1 
ATOM 52   C CA  . ARG A 1 75   ? 191.230 206.662 175.655 1.00 13.82 ? 25  ARG A CA  1 
ATOM 53   C C   . ARG A 1 75   ? 191.365 205.497 176.635 1.00 9.02  ? 25  ARG A C   1 
ATOM 54   O O   . ARG A 1 75   ? 192.366 205.457 177.376 1.00 11.99 ? 25  ARG A O   1 
ATOM 55   C CB  . ARG A 1 75   ? 190.097 207.593 176.087 1.00 15.28 ? 25  ARG A CB  1 
ATOM 56   C CG  . ARG A 1 75   ? 190.502 208.699 177.049 1.00 14.87 ? 25  ARG A CG  1 
ATOM 57   C CD  . ARG A 1 75   ? 189.313 209.628 177.192 1.00 15.73 ? 25  ARG A CD  1 
ATOM 58   N NE  . ARG A 1 75   ? 188.699 209.844 175.889 1.00 15.83 ? 25  ARG A NE  1 
ATOM 59   C CZ  . ARG A 1 75   ? 187.604 210.564 175.676 1.00 13.48 ? 25  ARG A CZ  1 
ATOM 60   N NH1 . ARG A 1 75   ? 186.968 211.117 176.693 1.00 15.71 ? 25  ARG A NH1 1 
ATOM 61   N NH2 . ARG A 1 75   ? 187.147 210.724 174.446 1.00 11.18 ? 25  ARG A NH2 1 
ATOM 62   N N   . PHE A 1 76   ? 190.388 204.586 176.627 1.00 6.42  ? 26  PHE A N   1 
ATOM 63   C CA  . PHE A 1 76   ? 190.442 203.397 177.515 1.00 11.23 ? 26  PHE A CA  1 
ATOM 64   C C   . PHE A 1 76   ? 191.741 202.635 177.242 1.00 5.44  ? 26  PHE A C   1 
ATOM 65   O O   . PHE A 1 76   ? 192.443 202.281 178.208 1.00 15.63 ? 26  PHE A O   1 
ATOM 66   C CB  . PHE A 1 76   ? 189.230 202.497 177.272 1.00 5.99  ? 26  PHE A CB  1 
ATOM 67   C CG  . PHE A 1 76   ? 189.202 201.254 178.122 1.00 8.44  ? 26  PHE A CG  1 
ATOM 68   C CD1 . PHE A 1 76   ? 189.087 201.339 179.499 1.00 13.40 ? 26  PHE A CD1 1 
ATOM 69   C CD2 . PHE A 1 76   ? 189.315 200.000 177.547 1.00 12.78 ? 26  PHE A CD2 1 
ATOM 70   C CE1 . PHE A 1 76   ? 189.067 200.195 180.279 1.00 13.25 ? 26  PHE A CE1 1 
ATOM 71   C CE2 . PHE A 1 76   ? 189.301 198.857 178.330 1.00 11.89 ? 26  PHE A CE2 1 
ATOM 72   C CZ  . PHE A 1 76   ? 189.179 198.957 179.695 1.00 9.85  ? 26  PHE A CZ  1 
ATOM 73   N N   . ILE A 1 77   ? 192.050 202.399 175.963 1.00 0.08  ? 27  ILE A N   1 
ATOM 74   C CA  . ILE A 1 77   ? 193.248 201.649 175.608 1.00 3.92  ? 27  ILE A CA  1 
ATOM 75   C C   . ILE A 1 77   ? 194.487 202.363 176.131 1.00 4.45  ? 27  ILE A C   1 
ATOM 76   O O   . ILE A 1 77   ? 195.330 201.753 176.784 1.00 13.13 ? 27  ILE A O   1 
ATOM 77   C CB  . ILE A 1 77   ? 193.295 201.428 174.084 1.00 10.72 ? 27  ILE A CB  1 
ATOM 78   C CG1 . ILE A 1 77   ? 192.149 200.518 173.643 1.00 8.67  ? 27  ILE A CG1 1 
ATOM 79   C CG2 . ILE A 1 77   ? 194.592 200.826 173.645 1.00 1.81  ? 27  ILE A CG2 1 
ATOM 80   C CD1 . ILE A 1 77   ? 191.721 200.757 172.217 1.00 2.66  ? 27  ILE A CD1 1 
ATOM 81   N N   . SER A 1 78   ? 194.574 203.679 175.935 1.00 0.00  ? 28  SER A N   1 
ATOM 82   C CA  . SER A 1 78   ? 195.732 204.435 176.412 1.00 0.92  ? 28  SER A CA  1 
ATOM 83   C C   . SER A 1 78   ? 195.839 204.404 177.929 1.00 5.29  ? 28  SER A C   1 
ATOM 84   O O   . SER A 1 78   ? 196.942 204.304 178.484 1.00 4.09  ? 28  SER A O   1 
ATOM 85   C CB  . SER A 1 78   ? 195.667 205.867 175.902 1.00 5.23  ? 28  SER A CB  1 
ATOM 86   O OG  . SER A 1 78   ? 194.554 206.532 176.462 1.00 4.73  ? 28  SER A OG  1 
ATOM 87   N N   . LYS A 1 79   ? 194.702 204.496 178.619 1.00 9.78  ? 29  LYS A N   1 
ATOM 88   C CA  . LYS A 1 79   ? 194.721 204.411 180.074 1.00 8.85  ? 29  LYS A CA  1 
ATOM 89   C C   . LYS A 1 79   ? 195.233 203.054 180.539 1.00 8.40  ? 29  LYS A C   1 
ATOM 90   O O   . LYS A 1 79   ? 195.977 202.965 181.525 1.00 2.89  ? 29  LYS A O   1 
ATOM 91   C CB  . LYS A 1 79   ? 193.326 204.686 180.634 1.00 5.70  ? 29  LYS A CB  1 
ATOM 92   C CG  . LYS A 1 79   ? 193.139 206.116 181.105 1.00 4.55  ? 29  LYS A CG  1 
ATOM 93   C CD  . LYS A 1 79   ? 191.675 206.492 181.178 1.00 7.91  ? 29  LYS A CD  1 
ATOM 94   C CE  . LYS A 1 79   ? 191.502 207.999 181.230 1.00 9.00  ? 29  LYS A CE  1 
ATOM 95   N NZ  . LYS A 1 79   ? 190.166 208.419 180.730 1.00 14.09 ? 29  LYS A NZ  1 
ATOM 96   N N   . VAL A 1 80   ? 194.842 201.984 179.845 1.00 10.03 ? 30  VAL A N   1 
ATOM 97   C CA  . VAL A 1 80   ? 195.318 200.657 180.221 1.00 0.00  ? 30  VAL A CA  1 
ATOM 98   C C   . VAL A 1 80   ? 196.823 200.542 180.008 1.00 0.00  ? 30  VAL A C   1 
ATOM 99   O O   . VAL A 1 80   ? 197.538 199.976 180.848 1.00 3.21  ? 30  VAL A O   1 
ATOM 100  C CB  . VAL A 1 80   ? 194.540 199.575 179.455 1.00 0.00  ? 30  VAL A CB  1 
ATOM 101  C CG1 . VAL A 1 80   ? 195.224 198.241 179.593 1.00 3.97  ? 30  VAL A CG1 1 
ATOM 102  C CG2 . VAL A 1 80   ? 193.135 199.485 179.995 1.00 0.91  ? 30  VAL A CG2 1 
ATOM 103  N N   . GLU A 1 81   ? 197.307 201.097 178.894 1.00 2.12  ? 31  GLU A N   1 
ATOM 104  C CA  . GLU A 1 81   ? 198.773 201.109 178.648 1.00 0.10  ? 31  GLU A CA  1 
ATOM 105  C C   . GLU A 1 81   ? 199.452 201.783 179.843 1.00 3.80  ? 31  GLU A C   1 
ATOM 106  O O   . GLU A 1 81   ? 200.470 201.248 180.323 1.00 8.85  ? 31  GLU A O   1 
ATOM 107  C CB  . GLU A 1 81   ? 199.092 201.868 177.360 1.00 8.09  ? 31  GLU A CB  1 
ATOM 108  C CG  . GLU A 1 81   ? 198.587 201.178 176.109 1.00 16.01 ? 31  GLU A CG  1 
ATOM 109  C CD  . GLU A 1 81   ? 198.829 201.948 174.824 1.00 9.39  ? 31  GLU A CD  1 
ATOM 110  O OE1 . GLU A 1 81   ? 199.229 203.124 174.911 1.00 7.36  ? 31  GLU A OE1 1 
ATOM 111  O OE2 . GLU A 1 81   ? 198.620 201.368 173.740 1.00 0.80  ? 31  GLU A OE2 1 
ATOM 112  N N   . GLU A 1 82   ? 198.896 202.909 180.303 1.00 4.19  ? 32  GLU A N   1 
ATOM 113  C CA  . GLU A 1 82   ? 199.499 203.659 181.437 1.00 5.89  ? 32  GLU A CA  1 
ATOM 114  C C   . GLU A 1 82   ? 199.495 202.782 182.693 1.00 8.30  ? 32  GLU A C   1 
ATOM 115  O O   . GLU A 1 82   ? 200.567 202.646 183.315 1.00 6.97  ? 32  GLU A O   1 
ATOM 116  C CB  . GLU A 1 82   ? 198.725 204.952 181.693 1.00 8.77  ? 32  GLU A CB  1 
ATOM 117  C CG  . GLU A 1 82   ? 199.323 205.811 182.791 1.00 8.19  ? 32  GLU A CG  1 
ATOM 118  C CD  . GLU A 1 82   ? 198.594 207.123 183.026 1.00 8.73  ? 32  GLU A CD  1 
ATOM 119  O OE1 . GLU A 1 82   ? 197.576 207.359 182.347 1.00 7.60  ? 32  GLU A OE1 1 
ATOM 120  O OE2 . GLU A 1 82   ? 199.048 207.904 183.884 1.00 9.78  ? 32  GLU A OE2 1 
ATOM 121  N N   . VAL A 1 83   ? 198.335 202.217 183.043 1.00 10.15 ? 33  VAL A N   1 
ATOM 122  C CA  . VAL A 1 83   ? 198.228 201.413 184.298 1.00 8.09  ? 33  VAL A CA  1 
ATOM 123  C C   . VAL A 1 83   ? 199.214 200.237 184.231 1.00 3.04  ? 33  VAL A C   1 
ATOM 124  O O   . VAL A 1 83   ? 199.700 199.822 185.303 1.00 0.40  ? 33  VAL A O   1 
ATOM 125  C CB  . VAL A 1 83   ? 196.782 200.946 184.567 1.00 5.73  ? 33  VAL A CB  1 
ATOM 126  C CG1 . VAL A 1 83   ? 196.402 199.722 183.749 1.00 0.00  ? 33  VAL A CG1 1 
ATOM 127  C CG2 . VAL A 1 83   ? 196.544 200.690 186.047 1.00 9.06  ? 33  VAL A CG2 1 
ATOM 128  N N   . LEU A 1 84   ? 199.509 199.729 183.029 1.00 7.56  ? 34  LEU A N   1 
ATOM 129  C CA  . LEU A 1 84   ? 200.437 198.606 182.949 1.00 5.34  ? 34  LEU A CA  1 
ATOM 130  C C   . LEU A 1 84   ? 201.889 199.068 182.932 1.00 5.13  ? 34  LEU A C   1 
ATOM 131  O O   . LEU A 1 84   ? 202.765 198.363 183.445 1.00 13.57 ? 34  LEU A O   1 
ATOM 132  C CB  . LEU A 1 84   ? 200.137 197.758 181.713 1.00 2.90  ? 34  LEU A CB  1 
ATOM 133  C CG  . LEU A 1 84   ? 198.756 197.100 181.646 1.00 2.21  ? 34  LEU A CG  1 
ATOM 134  C CD1 . LEU A 1 84   ? 198.732 196.013 180.585 1.00 1.15  ? 34  LEU A CD1 1 
ATOM 135  C CD2 . LEU A 1 84   ? 198.346 196.542 182.998 1.00 1.36  ? 34  LEU A CD2 1 
ATOM 136  N N   . ASN A 1 85   ? 202.170 200.233 182.348 1.00 0.23  ? 35  ASN A N   1 
ATOM 137  C CA  . ASN A 1 85   ? 203.548 200.699 182.279 1.00 0.00  ? 35  ASN A CA  1 
ATOM 138  C C   . ASN A 1 85   ? 204.030 201.260 183.608 1.00 2.31  ? 35  ASN A C   1 
ATOM 139  O O   . ASN A 1 85   ? 205.223 201.158 183.919 1.00 4.33  ? 35  ASN A O   1 
ATOM 140  C CB  . ASN A 1 85   ? 203.697 201.750 181.177 1.00 11.96 ? 35  ASN A CB  1 
ATOM 141  C CG  . ASN A 1 85   ? 205.025 202.481 181.243 1.00 13.51 ? 35  ASN A CG  1 
ATOM 142  O OD1 . ASN A 1 85   ? 206.081 201.892 181.016 1.00 10.82 ? 35  ASN A OD1 1 
ATOM 143  N ND2 . ASN A 1 85   ? 204.978 203.772 181.551 1.00 12.70 ? 35  ASN A ND2 1 
ATOM 144  N N   . ASP A 1 86   ? 203.134 201.854 184.401 1.00 5.41  ? 36  ASP A N   1 
ATOM 145  C CA  . ASP A 1 86   ? 203.552 202.387 185.695 1.00 7.93  ? 36  ASP A CA  1 
ATOM 146  C C   . ASP A 1 86   ? 204.045 201.281 186.624 1.00 10.37 ? 36  ASP A C   1 
ATOM 147  O O   . ASP A 1 86   ? 204.952 201.500 187.435 1.00 4.44  ? 36  ASP A O   1 
ATOM 148  C CB  . ASP A 1 86   ? 202.406 203.163 186.342 1.00 1.03  ? 36  ASP A CB  1 
ATOM 149  C CG  . ASP A 1 86   ? 202.440 204.636 185.998 1.00 7.18  ? 36  ASP A CG  1 
ATOM 150  O OD1 . ASP A 1 86   ? 203.442 205.078 185.398 1.00 9.10  ? 36  ASP A OD1 1 
ATOM 151  O OD2 . ASP A 1 86   ? 201.471 205.351 186.327 1.00 13.73 ? 36  ASP A OD2 1 
ATOM 152  N N   . TRP A 1 87   ? 203.471 200.078 186.492 1.00 11.04 ? 37  TRP A N   1 
ATOM 153  C CA  . TRP A 1 87   ? 203.817 198.959 187.413 1.00 0.00  ? 37  TRP A CA  1 
ATOM 154  C C   . TRP A 1 87   ? 205.067 198.205 186.945 1.00 0.00  ? 37  TRP A C   1 
ATOM 155  O O   . TRP A 1 87   ? 205.481 197.267 187.662 1.00 11.33 ? 37  TRP A O   1 
ATOM 156  C CB  . TRP A 1 87   ? 202.620 198.009 187.556 1.00 0.00  ? 37  TRP A CB  1 
ATOM 157  C CG  . TRP A 1 87   ? 201.572 198.504 188.516 1.00 0.05  ? 37  TRP A CG  1 
ATOM 158  C CD1 . TRP A 1 87   ? 201.727 199.456 189.479 1.00 4.37  ? 37  TRP A CD1 1 
ATOM 159  C CD2 . TRP A 1 87   ? 200.198 198.067 188.601 1.00 0.00  ? 37  TRP A CD2 1 
ATOM 160  N NE1 . TRP A 1 87   ? 200.553 199.644 190.157 1.00 8.55  ? 37  TRP A NE1 1 
ATOM 161  C CE2 . TRP A 1 87   ? 199.598 198.807 189.643 1.00 2.13  ? 37  TRP A CE2 1 
ATOM 162  C CE3 . TRP A 1 87   ? 199.424 197.132 187.906 1.00 0.00  ? 37  TRP A CE3 1 
ATOM 163  C CZ2 . TRP A 1 87   ? 198.263 198.638 190.001 1.00 0.00  ? 37  TRP A CZ2 1 
ATOM 164  C CZ3 . TRP A 1 87   ? 198.104 196.967 188.262 1.00 0.00  ? 37  TRP A CZ3 1 
ATOM 165  C CH2 . TRP A 1 87   ? 197.534 197.709 189.296 1.00 0.64  ? 37  TRP A CH2 1 
ATOM 166  N N   . LYS A 1 88   ? 205.632 198.574 185.792 1.00 1.93  ? 38  LYS A N   1 
ATOM 167  C CA  . LYS A 1 88   ? 206.865 197.963 185.288 1.00 6.38  ? 38  LYS A CA  1 
ATOM 168  C C   . LYS A 1 88   ? 206.687 196.473 184.990 1.00 3.42  ? 38  LYS A C   1 
ATOM 169  O O   . LYS A 1 88   ? 207.602 195.670 185.182 1.00 2.81  ? 38  LYS A O   1 
ATOM 170  C CB  . LYS A 1 88   ? 208.027 198.186 186.260 1.00 2.53  ? 38  LYS A CB  1 
ATOM 171  C CG  . LYS A 1 88   ? 208.482 199.630 186.373 1.00 5.62  ? 38  LYS A CG  1 
ATOM 172  C CD  . LYS A 1 88   ? 209.764 199.739 187.175 1.00 7.92  ? 38  LYS A CD  1 
ATOM 173  C CE  . LYS A 1 88   ? 209.526 199.386 188.633 1.00 8.48  ? 38  LYS A CE  1 
ATOM 174  N NZ  . LYS A 1 88   ? 210.748 199.605 189.454 1.00 7.98  ? 38  LYS A NZ  1 
ATOM 175  N N   . LEU A 1 89   ? 205.506 196.100 184.499 1.00 0.94  ? 39  LEU A N   1 
ATOM 176  C CA  . LEU A 1 89   ? 205.257 194.724 184.084 1.00 1.55  ? 39  LEU A CA  1 
ATOM 177  C C   . LEU A 1 89   ? 205.764 194.432 182.679 1.00 8.57  ? 39  LEU A C   1 
ATOM 178  O O   . LEU A 1 89   ? 205.641 193.292 182.217 1.00 8.80  ? 39  LEU A O   1 
ATOM 179  C CB  . LEU A 1 89   ? 203.761 194.403 184.156 1.00 3.02  ? 39  LEU A CB  1 
ATOM 180  C CG  . LEU A 1 89   ? 202.934 194.959 185.314 1.00 3.74  ? 39  LEU A CG  1 
ATOM 181  C CD1 . LEU A 1 89   ? 201.505 194.456 185.224 1.00 0.00  ? 39  LEU A CD1 1 
ATOM 182  C CD2 . LEU A 1 89   ? 203.548 194.562 186.639 1.00 8.31  ? 39  LEU A CD2 1 
ATOM 183  N N   . ILE A 1 90   ? 206.324 195.428 181.992 1.00 11.03 ? 40  ILE A N   1 
ATOM 184  C CA  . ILE A 1 90   ? 206.775 195.249 180.619 1.00 7.16  ? 40  ILE A CA  1 
ATOM 185  C C   . ILE A 1 90   ? 208.080 194.464 180.593 1.00 10.72 ? 40  ILE A C   1 
ATOM 186  O O   . ILE A 1 90   ? 208.961 194.654 181.442 1.00 17.29 ? 40  ILE A O   1 
ATOM 187  C CB  . ILE A 1 90   ? 206.937 196.618 179.939 1.00 6.17  ? 40  ILE A CB  1 
ATOM 188  C CG1 . ILE A 1 90   ? 208.002 197.441 180.665 1.00 9.50  ? 40  ILE A CG1 1 
ATOM 189  C CG2 . ILE A 1 90   ? 205.608 197.354 179.881 1.00 9.09  ? 40  ILE A CG2 1 
ATOM 190  C CD1 . ILE A 1 90   ? 209.349 197.432 179.988 1.00 9.30  ? 40  ILE A CD1 1 
ATOM 191  N N   . GLY A 1 91   ? 208.208 193.575 179.613 1.00 10.13 ? 41  GLY A N   1 
ATOM 192  C CA  . GLY A 1 91   ? 209.436 192.836 179.395 1.00 12.83 ? 41  GLY A CA  1 
ATOM 193  C C   . GLY A 1 91   ? 209.327 191.387 179.825 1.00 10.09 ? 41  GLY A C   1 
ATOM 194  O O   . GLY A 1 91   ? 208.326 190.932 180.387 1.00 11.41 ? 41  GLY A O   1 
ATOM 195  N N   . ASN A 1 92   ? 210.400 190.655 179.543 1.00 10.59 ? 42  ASN A N   1 
ATOM 196  C CA  . ASN A 1 92   ? 210.491 189.249 179.897 1.00 18.24 ? 42  ASN A CA  1 
ATOM 197  C C   . ASN A 1 92   ? 210.849 189.085 181.371 1.00 19.30 ? 42  ASN A C   1 
ATOM 198  O O   . ASN A 1 92   ? 211.405 189.983 182.009 1.00 20.06 ? 42  ASN A O   1 
ATOM 199  C CB  . ASN A 1 92   ? 211.531 188.543 179.026 1.00 24.45 ? 42  ASN A CB  1 
ATOM 200  C CG  . ASN A 1 92   ? 211.081 187.168 178.580 1.00 23.06 ? 42  ASN A CG  1 
ATOM 201  O OD1 . ASN A 1 92   ? 209.951 186.987 178.126 1.00 19.76 ? 42  ASN A OD1 1 
ATOM 202  N ND2 . ASN A 1 92   ? 211.966 186.186 178.710 1.00 21.02 ? 42  ASN A ND2 1 
ATOM 203  N N   . SER A 1 93   ? 210.521 187.913 181.909 1.00 22.52 ? 43  SER A N   1 
ATOM 204  C CA  . SER A 1 93   ? 210.850 187.562 183.281 1.00 25.40 ? 43  SER A CA  1 
ATOM 205  C C   . SER A 1 93   ? 211.428 186.156 183.321 1.00 28.11 ? 43  SER A C   1 
ATOM 206  O O   . SER A 1 93   ? 211.078 185.301 182.503 1.00 29.44 ? 43  SER A O   1 
ATOM 207  C CB  . SER A 1 93   ? 209.622 187.648 184.196 1.00 24.11 ? 43  SER A CB  1 
ATOM 208  O OG  . SER A 1 93   ? 209.814 186.892 185.379 1.00 25.69 ? 43  SER A OG  1 
ATOM 209  N N   . LEU A 1 94   ? 212.323 185.924 184.282 1.00 28.51 ? 44  LEU A N   1 
ATOM 210  C CA  . LEU A 1 94   ? 212.923 184.602 184.464 1.00 27.85 ? 44  LEU A CA  1 
ATOM 211  C C   . LEU A 1 94   ? 213.192 184.418 185.956 1.00 30.71 ? 44  LEU A C   1 
ATOM 212  O O   . LEU A 1 94   ? 213.890 185.229 186.572 1.00 34.52 ? 44  LEU A O   1 
ATOM 213  C CB  . LEU A 1 94   ? 214.188 184.446 183.626 1.00 30.77 ? 44  LEU A CB  1 
ATOM 214  C CG  . LEU A 1 94   ? 215.345 185.442 183.756 1.00 33.28 ? 44  LEU A CG  1 
ATOM 215  C CD1 . LEU A 1 94   ? 216.409 184.938 184.726 1.00 30.86 ? 44  LEU A CD1 1 
ATOM 216  C CD2 . LEU A 1 94   ? 215.955 185.727 182.392 1.00 29.37 ? 44  LEU A CD2 1 
ATOM 217  N N   . GLY A 1 95   ? 212.614 183.366 186.529 1.00 31.20 ? 45  GLY A N   1 
ATOM 218  C CA  . GLY A 1 95   ? 212.783 183.085 187.940 1.00 31.26 ? 45  GLY A CA  1 
ATOM 219  C C   . GLY A 1 95   ? 213.143 181.642 188.222 1.00 34.38 ? 45  GLY A C   1 
ATOM 220  O O   . GLY A 1 95   ? 213.849 181.004 187.435 1.00 35.52 ? 45  GLY A O   1 
ATOM 221  N N   . LYS A 1 96   ? 212.656 181.114 189.347 1.00 33.91 ? 46  LYS A N   1 
ATOM 222  C CA  . LYS A 1 96   ? 212.925 179.750 189.767 1.00 30.92 ? 46  LYS A CA  1 
ATOM 223  C C   . LYS A 1 96   ? 211.636 178.938 189.822 1.00 29.39 ? 46  LYS A C   1 
ATOM 224  O O   . LYS A 1 96   ? 210.569 179.491 190.113 1.00 27.05 ? 46  LYS A O   1 
ATOM 225  C CB  . LYS A 1 96   ? 213.598 179.728 191.144 1.00 27.98 ? 46  LYS A CB  1 
ATOM 226  C CG  . LYS A 1 96   ? 212.747 180.319 192.257 1.00 32.71 ? 46  LYS A CG  1 
ATOM 227  C CD  . LYS A 1 96   ? 213.471 180.266 193.591 1.00 36.92 ? 46  LYS A CD  1 
ATOM 228  C CE  . LYS A 1 96   ? 212.622 180.857 194.706 1.00 34.42 ? 46  LYS A CE  1 
ATOM 229  N NZ  . LYS A 1 96   ? 212.379 182.313 194.505 1.00 32.63 ? 46  LYS A NZ  1 
ATOM 230  N N   . PRO A 1 97   ? 211.698 177.641 189.529 1.00 29.90 ? 47  PRO A N   1 
ATOM 231  C CA  . PRO A 1 97   ? 210.502 176.798 189.647 1.00 29.99 ? 47  PRO A CA  1 
ATOM 232  C C   . PRO A 1 97   ? 209.972 176.781 191.073 1.00 28.81 ? 47  PRO A C   1 
ATOM 233  O O   . PRO A 1 97   ? 210.735 176.782 192.041 1.00 26.33 ? 47  PRO A O   1 
ATOM 234  C CB  . PRO A 1 97   ? 211.002 175.417 189.211 1.00 31.29 ? 47  PRO A CB  1 
ATOM 235  C CG  . PRO A 1 97   ? 212.163 175.705 188.323 1.00 31.96 ? 47  PRO A CG  1 
ATOM 236  C CD  . PRO A 1 97   ? 212.822 176.923 188.905 1.00 30.41 ? 47  PRO A CD  1 
ATOM 237  N N   . LEU A 1 98   ? 208.649 176.763 191.197 1.00 22.65 ? 48  LEU A N   1 
ATOM 238  C CA  . LEU A 1 98   ? 208.020 176.842 192.507 1.00 17.16 ? 48  LEU A CA  1 
ATOM 239  C C   . LEU A 1 98   ? 208.041 175.484 193.198 1.00 20.77 ? 48  LEU A C   1 
ATOM 240  O O   . LEU A 1 98   ? 207.719 174.456 192.596 1.00 24.27 ? 48  LEU A O   1 
ATOM 241  C CB  . LEU A 1 98   ? 206.584 177.349 192.369 1.00 16.82 ? 48  LEU A CB  1 
ATOM 242  C CG  . LEU A 1 98   ? 206.354 178.471 191.350 1.00 20.23 ? 48  LEU A CG  1 
ATOM 243  C CD1 . LEU A 1 98   ? 204.905 178.929 191.366 1.00 14.94 ? 48  LEU A CD1 1 
ATOM 244  C CD2 . LEU A 1 98   ? 207.282 179.645 191.617 1.00 21.13 ? 48  LEU A CD2 1 
ATOM 245  N N   . GLU A 1 99   ? 208.422 175.485 194.474 1.00 22.23 ? 49  GLU A N   1 
ATOM 246  C CA  . GLU A 1 99   ? 208.495 174.261 195.262 1.00 22.26 ? 49  GLU A CA  1 
ATOM 247  C C   . GLU A 1 99   ? 207.112 173.920 195.812 1.00 21.01 ? 49  GLU A C   1 
ATOM 248  O O   . GLU A 1 99   ? 206.125 174.616 195.560 1.00 21.18 ? 49  GLU A O   1 
ATOM 249  C CB  . GLU A 1 99   ? 209.529 174.405 196.375 1.00 15.76 ? 49  GLU A CB  1 
ATOM 250  C CG  . GLU A 1 99   ? 210.903 174.844 195.900 1.00 20.12 ? 49  GLU A CG  1 
ATOM 251  C CD  . GLU A 1 99   ? 211.690 173.709 195.278 1.00 25.30 ? 49  GLU A CD  1 
ATOM 252  O OE1 . GLU A 1 99   ? 211.480 172.548 195.685 1.00 25.30 ? 49  GLU A OE1 1 
ATOM 253  O OE2 . GLU A 1 99   ? 212.519 173.977 194.384 1.00 24.45 ? 49  GLU A OE2 1 
ATOM 254  N N   . LYS A 1 100  ? 207.027 172.837 196.579 1.00 15.43 ? 50  LYS A N   1 
ATOM 255  C CA  . LYS A 1 100  ? 205.744 172.384 197.095 1.00 13.82 ? 50  LYS A CA  1 
ATOM 256  C C   . LYS A 1 100  ? 205.247 173.320 198.187 1.00 8.14  ? 50  LYS A C   1 
ATOM 257  O O   . LYS A 1 100  ? 206.011 173.728 199.066 1.00 14.17 ? 50  LYS A O   1 
ATOM 258  C CB  . LYS A 1 100  ? 205.858 170.963 197.642 1.00 15.59 ? 50  LYS A CB  1 
ATOM 259  C CG  . LYS A 1 100  ? 206.876 170.091 196.931 1.00 14.32 ? 50  LYS A CG  1 
ATOM 260  C CD  . LYS A 1 100  ? 206.752 168.637 197.362 1.00 17.26 ? 50  LYS A CD  1 
ATOM 261  C CE  . LYS A 1 100  ? 206.524 168.515 198.862 1.00 14.64 ? 50  LYS A CE  1 
ATOM 262  N NZ  . LYS A 1 100  ? 206.496 167.095 199.310 1.00 13.19 ? 50  LYS A NZ  1 
ATOM 263  N N   . GLY A 1 101  ? 203.964 173.667 198.124 1.00 4.53  ? 51  GLY A N   1 
ATOM 264  C CA  . GLY A 1 101  ? 203.343 174.425 199.189 1.00 14.25 ? 51  GLY A CA  1 
ATOM 265  C C   . GLY A 1 101  ? 203.732 175.881 199.269 1.00 18.85 ? 51  GLY A C   1 
ATOM 266  O O   . GLY A 1 101  ? 203.379 176.542 200.250 1.00 24.90 ? 51  GLY A O   1 
ATOM 267  N N   . ILE A 1 102  ? 204.452 176.375 198.259 1.00 12.75 ? 52  ILE A N   1 
ATOM 268  C CA  . ILE A 1 102  ? 204.839 177.817 198.232 1.00 7.23  ? 52  ILE A CA  1 
ATOM 269  C C   . ILE A 1 102  ? 203.558 178.660 198.263 1.00 2.77  ? 52  ILE A C   1 
ATOM 270  O O   . ILE A 1 102  ? 203.539 179.674 198.989 1.00 13.93 ? 52  ILE A O   1 
ATOM 271  C CB  . ILE A 1 102  ? 205.720 178.126 197.005 1.00 6.97  ? 52  ILE A CB  1 
ATOM 272  C CG1 . ILE A 1 102  ? 207.024 177.322 197.023 1.00 8.87  ? 52  ILE A CG1 1 
ATOM 273  C CG2 . ILE A 1 102  ? 205.982 179.619 196.885 1.00 7.70  ? 52  ILE A CG2 1 
ATOM 274  C CD1 . ILE A 1 102  ? 207.820 177.436 198.308 1.00 10.72 ? 52  ILE A CD1 1 
ATOM 275  N N   . PHE A 1 103  ? 202.522 178.242 197.527 1.00 1.15  ? 53  PHE A N   1 
ATOM 276  C CA  . PHE A 1 103  ? 201.269 178.987 197.490 1.00 14.98 ? 53  PHE A CA  1 
ATOM 277  C C   . PHE A 1 103  ? 200.656 179.125 198.877 1.00 12.70 ? 53  PHE A C   1 
ATOM 278  O O   . PHE A 1 103  ? 199.982 180.121 199.161 1.00 15.79 ? 53  PHE A O   1 
ATOM 279  C CB  . PHE A 1 103  ? 200.278 178.302 196.549 1.00 17.19 ? 53  PHE A CB  1 
ATOM 280  C CG  . PHE A 1 103  ? 200.559 178.534 195.093 1.00 5.38  ? 53  PHE A CG  1 
ATOM 281  C CD1 . PHE A 1 103  ? 201.679 179.239 194.689 1.00 7.48  ? 53  PHE A CD1 1 
ATOM 282  C CD2 . PHE A 1 103  ? 199.702 178.038 194.127 1.00 1.54  ? 53  PHE A CD2 1 
ATOM 283  C CE1 . PHE A 1 103  ? 201.937 179.445 193.355 1.00 4.87  ? 53  PHE A CE1 1 
ATOM 284  C CE2 . PHE A 1 103  ? 199.956 178.242 192.792 1.00 11.84 ? 53  PHE A CE2 1 
ATOM 285  C CZ  . PHE A 1 103  ? 201.075 178.947 192.405 1.00 12.53 ? 53  PHE A CZ  1 
ATOM 286  N N   . THR A 1 104  ? 200.878 178.143 199.751 1.00 9.70  ? 54  THR A N   1 
ATOM 287  C CA  . THR A 1 104  ? 200.309 178.164 201.095 1.00 20.92 ? 54  THR A CA  1 
ATOM 288  C C   . THR A 1 104  ? 201.230 178.865 202.091 1.00 17.70 ? 54  THR A C   1 
ATOM 289  O O   . THR A 1 104  ? 200.833 179.846 202.729 1.00 13.87 ? 54  THR A O   1 
ATOM 290  C CB  . THR A 1 104  ? 200.015 176.735 201.561 1.00 18.83 ? 54  THR A CB  1 
ATOM 291  O OG1 . THR A 1 104  ? 199.230 176.062 200.571 1.00 13.58 ? 54  THR A OG1 1 
ATOM 292  C CG2 . THR A 1 104  ? 199.260 176.754 202.878 1.00 13.88 ? 54  THR A CG2 1 
ATOM 293  N N   . SER A 1 105  ? 202.461 178.371 202.234 1.00 14.57 ? 55  SER A N   1 
ATOM 294  C CA  . SER A 1 105  ? 203.387 178.944 203.203 1.00 15.05 ? 55  SER A CA  1 
ATOM 295  C C   . SER A 1 105  ? 203.799 180.366 202.848 1.00 14.97 ? 55  SER A C   1 
ATOM 296  O O   . SER A 1 105  ? 204.186 181.126 203.741 1.00 17.22 ? 55  SER A O   1 
ATOM 297  C CB  . SER A 1 105  ? 204.631 178.065 203.330 1.00 14.16 ? 55  SER A CB  1 
ATOM 298  O OG  . SER A 1 105  ? 205.283 177.922 202.081 1.00 6.25  ? 55  SER A OG  1 
ATOM 299  N N   . GLY A 1 106  ? 203.732 180.741 201.574 1.00 13.42 ? 56  GLY A N   1 
ATOM 300  C CA  . GLY A 1 106  ? 204.091 182.079 201.162 1.00 12.08 ? 56  GLY A CA  1 
ATOM 301  C C   . GLY A 1 106  ? 202.985 183.075 201.437 1.00 13.85 ? 56  GLY A C   1 
ATOM 302  O O   . GLY A 1 106  ? 201.908 182.744 201.931 1.00 16.72 ? 56  GLY A O   1 
ATOM 303  N N   . THR A 1 107  ? 203.254 184.337 201.086 1.00 15.42 ? 57  THR A N   1 
ATOM 304  C CA  . THR A 1 107  ? 202.229 185.402 201.248 1.00 17.20 ? 57  THR A CA  1 
ATOM 305  C C   . THR A 1 107  ? 202.012 186.072 199.887 1.00 14.20 ? 57  THR A C   1 
ATOM 306  O O   . THR A 1 107  ? 202.899 185.942 199.021 1.00 4.70  ? 57  THR A O   1 
ATOM 307  C CB  . THR A 1 107  ? 202.645 186.416 202.321 1.00 13.24 ? 57  THR A CB  1 
ATOM 308  O OG1 . THR A 1 107  ? 202.776 185.724 203.563 1.00 14.36 ? 57  THR A OG1 1 
ATOM 309  C CG2 . THR A 1 107  ? 201.657 187.552 202.472 1.00 12.99 ? 57  THR A CG2 1 
ATOM 310  N N   . TRP A 1 108  ? 200.877 186.753 199.704 1.00 13.50 ? 58  TRP A N   1 
ATOM 311  C CA  . TRP A 1 108  ? 200.567 187.373 198.390 1.00 12.37 ? 58  TRP A CA  1 
ATOM 312  C C   . TRP A 1 108  ? 200.308 188.871 198.567 1.00 10.87 ? 58  TRP A C   1 
ATOM 313  O O   . TRP A 1 108  ? 199.389 189.234 199.334 1.00 12.50 ? 58  TRP A O   1 
ATOM 314  C CB  . TRP A 1 108  ? 199.367 186.669 197.742 1.00 12.37 ? 58  TRP A CB  1 
ATOM 315  C CG  . TRP A 1 108  ? 199.598 185.205 197.472 1.00 14.10 ? 58  TRP A CG  1 
ATOM 316  C CD1 . TRP A 1 108  ? 199.710 184.206 198.393 1.00 12.87 ? 58  TRP A CD1 1 
ATOM 317  C CD2 . TRP A 1 108  ? 199.749 184.576 196.180 1.00 17.13 ? 58  TRP A CD2 1 
ATOM 318  N NE1 . TRP A 1 108  ? 199.921 183.004 197.772 1.00 19.08 ? 58  TRP A NE1 1 
ATOM 319  C CE2 . TRP A 1 108  ? 199.948 183.198 196.416 1.00 13.86 ? 58  TRP A CE2 1 
ATOM 320  C CE3 . TRP A 1 108  ? 199.733 185.038 194.860 1.00 14.11 ? 58  TRP A CE3 1 
ATOM 321  C CZ2 . TRP A 1 108  ? 200.130 182.286 195.381 1.00 5.48  ? 58  TRP A CZ2 1 
ATOM 322  C CZ3 . TRP A 1 108  ? 199.910 184.133 193.838 1.00 13.85 ? 58  TRP A CZ3 1 
ATOM 323  C CH2 . TRP A 1 108  ? 200.110 182.778 194.096 1.00 11.73 ? 58  TRP A CH2 1 
ATOM 324  N N   . GLU A 1 109  ? 201.106 189.706 197.896 1.00 5.98  ? 59  GLU A N   1 
ATOM 325  C CA  . GLU A 1 109  ? 200.923 191.179 197.987 1.00 0.22  ? 59  GLU A CA  1 
ATOM 326  C C   . GLU A 1 109  ? 199.970 191.630 196.876 1.00 1.87  ? 59  GLU A C   1 
ATOM 327  O O   . GLU A 1 109  ? 199.747 190.844 195.934 1.00 5.21  ? 59  GLU A O   1 
ATOM 328  C CB  . GLU A 1 109  ? 202.268 191.899 197.888 1.00 1.06  ? 59  GLU A CB  1 
ATOM 329  C CG  . GLU A 1 109  ? 203.180 191.643 199.072 1.00 1.85  ? 59  GLU A CG  1 
ATOM 330  C CD  . GLU A 1 109  ? 204.548 192.293 198.954 1.00 6.63  ? 59  GLU A CD  1 
ATOM 331  O OE1 . GLU A 1 109  ? 204.869 192.797 197.860 1.00 10.57 ? 59  GLU A OE1 1 
ATOM 332  O OE2 . GLU A 1 109  ? 205.287 192.295 199.958 1.00 11.33 ? 59  GLU A OE2 1 
ATOM 333  N N   . GLU A 1 110  ? 199.439 192.850 196.986 1.00 3.41  ? 60  GLU A N   1 
ATOM 334  C CA  . GLU A 1 110  ? 198.457 193.352 195.985 1.00 4.43  ? 60  GLU A CA  1 
ATOM 335  C C   . GLU A 1 110  ? 198.599 194.872 195.838 1.00 4.92  ? 60  GLU A C   1 
ATOM 336  O O   . GLU A 1 110  ? 199.021 195.518 196.817 1.00 13.10 ? 60  GLU A O   1 
ATOM 337  C CB  . GLU A 1 110  ? 197.027 192.988 196.391 1.00 0.08  ? 60  GLU A CB  1 
ATOM 338  C CG  . GLU A 1 110  ? 196.577 193.619 197.695 1.00 4.33  ? 60  GLU A CG  1 
ATOM 339  C CD  . GLU A 1 110  ? 195.204 193.168 198.164 1.00 9.20  ? 60  GLU A CD  1 
ATOM 340  O OE1 . GLU A 1 110  ? 194.444 192.633 197.333 1.00 8.96  ? 60  GLU A OE1 1 
ATOM 341  O OE2 . GLU A 1 110  ? 194.901 193.350 199.359 1.00 12.67 ? 60  GLU A OE2 1 
ATOM 342  N N   . LYS A 1 111  ? 198.259 195.416 194.663 1.00 0.00  ? 61  LYS A N   1 
ATOM 343  C CA  . LYS A 1 111  ? 198.307 196.886 194.441 1.00 0.00  ? 61  LYS A CA  1 
ATOM 344  C C   . LYS A 1 111  ? 197.066 197.290 193.638 1.00 0.00  ? 61  LYS A C   1 
ATOM 345  O O   . LYS A 1 111  ? 196.982 196.905 192.455 1.00 3.35  ? 61  LYS A O   1 
ATOM 346  C CB  . LYS A 1 111  ? 199.588 197.281 193.701 1.00 0.00  ? 61  LYS A CB  1 
ATOM 347  C CG  . LYS A 1 111  ? 200.876 197.127 194.498 1.00 0.00  ? 61  LYS A CG  1 
ATOM 348  C CD  . LYS A 1 111  ? 202.118 197.392 193.676 1.00 0.00  ? 61  LYS A CD  1 
ATOM 349  C CE  . LYS A 1 111  ? 202.221 198.825 193.198 1.00 0.00  ? 61  LYS A CE  1 
ATOM 350  N NZ  . LYS A 1 111  ? 203.503 199.079 192.499 1.00 0.00  ? 61  LYS A NZ  1 
ATOM 351  N N   . SER A 1 112  ? 196.238 198.241 194.105 1.00 4.51  ? 62  SER A N   1 
ATOM 352  C CA  . SER A 1 112  ? 195.063 198.688 193.286 1.00 2.09  ? 62  SER A CA  1 
ATOM 353  C C   . SER A 1 112  ? 195.254 200.039 192.562 1.00 4.40  ? 62  SER A C   1 
ATOM 354  O O   . SER A 1 112  ? 196.327 200.647 192.745 1.00 11.51 ? 62  SER A O   1 
ATOM 355  C CB  . SER A 1 112  ? 193.811 198.709 194.130 1.00 3.57  ? 62  SER A CB  1 
ATOM 356  O OG  . SER A 1 112  ? 192.653 198.633 193.312 1.00 0.00  ? 62  SER A OG  1 
ATOM 357  N N   . ASP A 1 113  ? 194.274 200.446 191.740 1.00 4.73  ? 63  ASP A N   1 
ATOM 358  C CA  . ASP A 1 113  ? 194.343 201.711 190.952 1.00 7.49  ? 63  ASP A CA  1 
ATOM 359  C C   . ASP A 1 113  ? 192.977 201.902 190.279 1.00 9.97  ? 63  ASP A C   1 
ATOM 360  O O   . ASP A 1 113  ? 192.245 200.896 190.185 1.00 10.72 ? 63  ASP A O   1 
ATOM 361  C CB  . ASP A 1 113  ? 195.482 201.670 189.931 1.00 4.56  ? 63  ASP A CB  1 
ATOM 362  C CG  . ASP A 1 113  ? 195.533 202.884 189.019 1.00 4.59  ? 63  ASP A CG  1 
ATOM 363  O OD1 . ASP A 1 113  ? 196.143 203.893 189.422 1.00 2.81  ? 63  ASP A OD1 1 
ATOM 364  O OD2 . ASP A 1 113  ? 194.960 202.810 187.913 1.00 5.50  ? 63  ASP A OD2 1 
ATOM 365  N N   . GLU A 1 114  ? 192.627 203.113 189.820 1.00 9.45  ? 64  GLU A N   1 
ATOM 366  C CA  . GLU A 1 114  ? 191.254 203.259 189.262 1.00 11.89 ? 64  GLU A CA  1 
ATOM 367  C C   . GLU A 1 114  ? 191.314 203.756 187.802 1.00 14.53 ? 64  GLU A C   1 
ATOM 368  O O   . GLU A 1 114  ? 192.222 204.557 187.492 1.00 14.31 ? 64  GLU A O   1 
ATOM 369  C CB  . GLU A 1 114  ? 190.395 204.143 190.166 1.00 10.98 ? 64  GLU A CB  1 
ATOM 370  C CG  . GLU A 1 114  ? 188.933 203.749 190.188 1.00 14.37 ? 64  GLU A CG  1 
ATOM 371  C CD  . GLU A 1 114  ? 188.069 204.442 189.147 1.00 18.27 ? 64  GLU A CD  1 
ATOM 372  O OE1 . GLU A 1 114  ? 187.809 205.654 189.309 1.00 17.93 ? 64  GLU A OE1 1 
ATOM 373  O OE2 . GLU A 1 114  ? 187.657 203.768 188.169 1.00 18.60 ? 64  GLU A OE2 1 
ATOM 374  N N   . ILE A 1 115  ? 190.404 203.279 186.923 1.00 10.53 ? 65  ILE A N   1 
ATOM 375  C CA  . ILE A 1 115  ? 190.408 203.842 185.539 1.00 7.90  ? 65  ILE A CA  1 
ATOM 376  C C   . ILE A 1 115  ? 188.956 203.963 185.064 1.00 12.03 ? 65  ILE A C   1 
ATOM 377  O O   . ILE A 1 115  ? 188.136 203.108 185.457 1.00 12.02 ? 65  ILE A O   1 
ATOM 378  C CB  . ILE A 1 115  ? 191.264 202.967 184.599 1.00 15.72 ? 65  ILE A CB  1 
ATOM 379  C CG1 . ILE A 1 115  ? 190.701 201.549 184.481 1.00 13.22 ? 65  ILE A CG1 1 
ATOM 380  C CG2 . ILE A 1 115  ? 192.725 202.957 185.023 1.00 12.60 ? 65  ILE A CG2 1 
ATOM 381  C CD1 . ILE A 1 115  ? 189.892 201.313 183.228 1.00 3.56  ? 65  ILE A CD1 1 
ATOM 382  N N   . SER A 1 116  ? 188.646 204.995 184.272 1.00 8.21  ? 66  SER A N   1 
ATOM 383  C CA  . SER A 1 116  ? 187.293 205.143 183.735 1.00 12.32 ? 66  SER A CA  1 
ATOM 384  C C   . SER A 1 116  ? 187.401 205.890 182.414 1.00 14.77 ? 66  SER A C   1 
ATOM 385  O O   . SER A 1 116  ? 187.938 207.001 182.383 1.00 19.92 ? 66  SER A O   1 
ATOM 386  C CB  . SER A 1 116  ? 186.389 205.884 184.711 1.00 17.53 ? 66  SER A CB  1 
ATOM 387  O OG  . SER A 1 116  ? 185.031 205.731 184.345 1.00 22.57 ? 66  SER A OG  1 
ATOM 388  N N   . PHE A 1 117  ? 186.892 205.297 181.332 1.00 17.79 ? 67  PHE A N   1 
ATOM 389  C CA  . PHE A 1 117  ? 187.076 205.927 180.028 1.00 22.55 ? 67  PHE A CA  1 
ATOM 390  C C   . PHE A 1 117  ? 185.986 206.957 179.735 1.00 23.25 ? 67  PHE A C   1 
ATOM 391  O O   . PHE A 1 117  ? 186.299 208.117 179.444 1.00 16.98 ? 67  PHE A O   1 
ATOM 392  C CB  . PHE A 1 117  ? 187.181 204.867 178.923 1.00 20.59 ? 67  PHE A CB  1 
ATOM 393  C CG  . PHE A 1 117  ? 185.980 203.966 178.787 1.00 26.65 ? 67  PHE A CG  1 
ATOM 394  C CD1 . PHE A 1 117  ? 185.776 202.913 179.666 1.00 22.49 ? 67  PHE A CD1 1 
ATOM 395  C CD2 . PHE A 1 117  ? 185.077 204.148 177.751 1.00 24.11 ? 67  PHE A CD2 1 
ATOM 396  C CE1 . PHE A 1 117  ? 184.683 202.077 179.529 1.00 21.65 ? 67  PHE A CE1 1 
ATOM 397  C CE2 . PHE A 1 117  ? 183.983 203.315 177.608 1.00 23.20 ? 67  PHE A CE2 1 
ATOM 398  C CZ  . PHE A 1 117  ? 183.786 202.279 178.498 1.00 22.83 ? 67  PHE A CZ  1 
ATOM 399  N N   . ALA A 1 118  ? 184.709 206.570 179.791 1.00 29.78 ? 68  ALA A N   1 
ATOM 400  C CA  . ALA A 1 118  ? 183.667 207.579 179.617 1.00 27.25 ? 68  ALA A CA  1 
ATOM 401  C C   . ALA A 1 118  ? 182.777 207.753 180.844 1.00 27.50 ? 68  ALA A C   1 
ATOM 402  O O   . ALA A 1 118  ? 182.753 208.829 181.450 1.00 24.34 ? 68  ALA A O   1 
ATOM 403  C CB  . ALA A 1 118  ? 182.803 207.233 178.404 1.00 22.74 ? 68  ALA A CB  1 
ATOM 404  N N   . ASP A 1 119  ? 182.053 206.701 181.229 1.00 29.48 ? 69  ASP A N   1 
ATOM 405  C CA  . ASP A 1 119  ? 181.217 206.739 182.425 1.00 30.36 ? 69  ASP A CA  1 
ATOM 406  C C   . ASP A 1 119  ? 181.580 205.617 183.386 1.00 33.21 ? 69  ASP A C   1 
ATOM 407  O O   . ASP A 1 119  ? 181.736 205.841 184.590 1.00 28.15 ? 69  ASP A O   1 
ATOM 408  C CB  . ASP A 1 119  ? 179.732 206.643 182.063 1.00 28.28 ? 69  ASP A CB  1 
ATOM 409  C CG  . ASP A 1 119  ? 179.164 207.956 181.569 1.00 30.66 ? 69  ASP A CG  1 
ATOM 410  O OD1 . ASP A 1 119  ? 179.787 209.008 181.825 1.00 31.80 ? 69  ASP A OD1 1 
ATOM 411  O OD2 . ASP A 1 119  ? 178.091 207.937 180.930 1.00 32.40 ? 69  ASP A OD2 1 
ATOM 412  N N   . PHE A 1 120  ? 181.656 204.398 182.828 1.00 22.58 ? 70  PHE A N   1 
ATOM 413  C CA  . PHE A 1 120  ? 181.911 203.178 183.641 1.00 13.37 ? 70  PHE A CA  1 
ATOM 414  C C   . PHE A 1 120  ? 183.240 203.266 184.385 1.00 16.01 ? 70  PHE A C   1 
ATOM 415  O O   . PHE A 1 120  ? 184.261 203.597 183.757 1.00 15.32 ? 70  PHE A O   1 
ATOM 416  C CB  . PHE A 1 120  ? 181.890 201.930 182.753 1.00 20.06 ? 70  PHE A CB  1 
ATOM 417  C CG  . PHE A 1 120  ? 181.474 200.658 183.449 1.00 23.79 ? 70  PHE A CG  1 
ATOM 418  C CD1 . PHE A 1 120  ? 182.243 200.115 184.466 1.00 22.13 ? 70  PHE A CD1 1 
ATOM 419  C CD2 . PHE A 1 120  ? 180.312 199.997 183.084 1.00 24.01 ? 70  PHE A CD2 1 
ATOM 420  C CE1 . PHE A 1 120  ? 181.860 198.946 185.104 1.00 17.26 ? 70  PHE A CE1 1 
ATOM 421  C CE2 . PHE A 1 120  ? 179.929 198.827 183.722 1.00 24.23 ? 70  PHE A CE2 1 
ATOM 422  C CZ  . PHE A 1 120  ? 180.704 198.303 184.729 1.00 18.93 ? 70  PHE A CZ  1 
ATOM 423  N N   . LYS A 1 121  ? 183.223 202.905 185.666 1.00 21.92 ? 71  LYS A N   1 
ATOM 424  C CA  . LYS A 1 121  ? 184.411 202.970 186.504 1.00 19.66 ? 71  LYS A CA  1 
ATOM 425  C C   . LYS A 1 121  ? 184.955 201.571 186.757 1.00 20.82 ? 71  LYS A C   1 
ATOM 426  O O   . LYS A 1 121  ? 184.198 200.639 187.044 1.00 16.48 ? 71  LYS A O   1 
ATOM 427  C CB  . LYS A 1 121  ? 184.083 203.660 187.827 1.00 17.22 ? 71  LYS A CB  1 
ATOM 428  C CG  . LYS A 1 121  ? 183.242 204.908 187.654 1.00 21.40 ? 71  LYS A CG  1 
ATOM 429  C CD  . LYS A 1 121  ? 182.189 205.018 188.738 1.00 22.29 ? 71  LYS A CD  1 
ATOM 430  C CE  . LYS A 1 121  ? 181.319 206.244 188.528 1.00 21.69 ? 71  LYS A CE  1 
ATOM 431  N NZ  . LYS A 1 121  ? 180.746 206.287 187.154 1.00 19.34 ? 71  LYS A NZ  1 
ATOM 432  N N   . PHE A 1 122  ? 186.270 201.404 186.576 1.00 18.28 ? 72  PHE A N   1 
ATOM 433  C CA  . PHE A 1 122  ? 186.876 200.052 186.706 1.00 17.63 ? 72  PHE A CA  1 
ATOM 434  C C   . PHE A 1 122  ? 188.013 200.071 187.732 1.00 16.33 ? 72  PHE A C   1 
ATOM 435  O O   . PHE A 1 122  ? 188.732 201.085 187.816 1.00 14.83 ? 72  PHE A O   1 
ATOM 436  C CB  . PHE A 1 122  ? 187.415 199.571 185.357 1.00 15.75 ? 72  PHE A CB  1 
ATOM 437  C CG  . PHE A 1 122  ? 186.367 199.145 184.361 1.00 10.64 ? 72  PHE A CG  1 
ATOM 438  C CD1 . PHE A 1 122  ? 185.724 197.924 184.484 1.00 15.93 ? 72  PHE A CD1 1 
ATOM 439  C CD2 . PHE A 1 122  ? 186.031 199.962 183.293 1.00 6.05  ? 72  PHE A CD2 1 
ATOM 440  C CE1 . PHE A 1 122  ? 184.766 197.531 183.563 1.00 18.90 ? 72  PHE A CE1 1 
ATOM 441  C CE2 . PHE A 1 122  ? 185.073 199.568 182.373 1.00 13.39 ? 72  PHE A CE2 1 
ATOM 442  C CZ  . PHE A 1 122  ? 184.442 198.354 182.509 1.00 19.94 ? 72  PHE A CZ  1 
ATOM 443  N N   . SER A 1 123  ? 188.175 198.971 188.474 1.00 12.93 ? 73  SER A N   1 
ATOM 444  C CA  . SER A 1 123  ? 189.268 198.874 189.475 1.00 10.80 ? 73  SER A CA  1 
ATOM 445  C C   . SER A 1 123  ? 190.342 197.907 188.968 1.00 5.16  ? 73  SER A C   1 
ATOM 446  O O   . SER A 1 123  ? 190.022 196.716 188.784 1.00 4.32  ? 73  SER A O   1 
ATOM 447  C CB  . SER A 1 123  ? 188.731 198.438 190.812 1.00 13.60 ? 73  SER A CB  1 
ATOM 448  O OG  . SER A 1 123  ? 187.829 197.351 190.659 1.00 12.04 ? 73  SER A OG  1 
ATOM 449  N N   . VAL A 1 124  ? 191.564 198.404 188.757 1.00 3.36  ? 74  VAL A N   1 
ATOM 450  C CA  . VAL A 1 124  ? 192.685 197.534 188.290 1.00 7.03  ? 74  VAL A CA  1 
ATOM 451  C C   . VAL A 1 124  ? 193.394 196.957 189.518 1.00 0.86  ? 74  VAL A C   1 
ATOM 452  O O   . VAL A 1 124  ? 194.031 197.739 190.250 1.00 5.31  ? 74  VAL A O   1 
ATOM 453  C CB  . VAL A 1 124  ? 193.664 198.307 187.388 1.00 7.83  ? 74  VAL A CB  1 
ATOM 454  C CG1 . VAL A 1 124  ? 194.548 197.364 186.587 1.00 12.60 ? 74  VAL A CG1 1 
ATOM 455  C CG2 . VAL A 1 124  ? 192.936 199.274 186.468 1.00 1.70  ? 74  VAL A CG2 1 
ATOM 456  N N   . THR A 1 125  ? 193.291 195.641 189.725 1.00 0.00  ? 75  THR A N   1 
ATOM 457  C CA  . THR A 1 125  ? 193.900 194.998 190.920 1.00 1.96  ? 75  THR A CA  1 
ATOM 458  C C   . THR A 1 125  ? 194.968 193.992 190.481 1.00 8.96  ? 75  THR A C   1 
ATOM 459  O O   . THR A 1 125  ? 194.601 192.993 189.833 1.00 9.16  ? 75  THR A O   1 
ATOM 460  C CB  . THR A 1 125  ? 192.828 194.322 191.782 1.00 8.68  ? 75  THR A CB  1 
ATOM 461  O OG1 . THR A 1 125  ? 192.212 193.300 190.997 1.00 11.50 ? 75  THR A OG1 1 
ATOM 462  C CG2 . THR A 1 125  ? 191.775 195.289 192.277 1.00 3.39  ? 75  THR A CG2 1 
ATOM 463  N N   . HIS A 1 126  ? 196.233 194.248 190.827 1.00 0.00  ? 76  HIS A N   1 
ATOM 464  C CA  . HIS A 1 126  ? 197.335 193.307 190.483 1.00 0.00  ? 76  HIS A CA  1 
ATOM 465  C C   . HIS A 1 126  ? 197.697 192.488 191.725 1.00 0.00  ? 76  HIS A C   1 
ATOM 466  O O   . HIS A 1 126  ? 197.974 193.086 192.786 1.00 13.60 ? 76  HIS A O   1 
ATOM 467  C CB  . HIS A 1 126  ? 198.556 194.059 189.946 1.00 0.00  ? 76  HIS A CB  1 
ATOM 468  C CG  . HIS A 1 126  ? 199.791 193.222 189.883 1.00 2.89  ? 76  HIS A CG  1 
ATOM 469  N ND1 . HIS A 1 126  ? 200.988 193.610 190.445 1.00 0.00  ? 76  HIS A ND1 1 
ATOM 470  C CD2 . HIS A 1 126  ? 200.014 192.021 189.332 1.00 1.36  ? 76  HIS A CD2 1 
ATOM 471  C CE1 . HIS A 1 126  ? 201.896 192.669 190.231 1.00 0.00  ? 76  HIS A CE1 1 
ATOM 472  N NE2 . HIS A 1 126  ? 201.325 191.694 189.558 1.00 0.00  ? 76  HIS A NE2 1 
ATOM 473  N N   . HIS A 1 127  ? 197.702 191.160 191.591 1.00 1.16  ? 77  HIS A N   1 
ATOM 474  C CA  . HIS A 1 127  ? 198.037 190.266 192.733 1.00 0.00  ? 77  HIS A CA  1 
ATOM 475  C C   . HIS A 1 127  ? 199.308 189.488 192.380 1.00 0.00  ? 77  HIS A C   1 
ATOM 476  O O   . HIS A 1 127  ? 199.439 189.063 191.211 1.00 6.59  ? 77  HIS A O   1 
ATOM 477  C CB  . HIS A 1 127  ? 196.853 189.345 193.044 1.00 0.27  ? 77  HIS A CB  1 
ATOM 478  C CG  . HIS A 1 127  ? 195.632 190.086 193.481 1.00 4.20  ? 77  HIS A CG  1 
ATOM 479  N ND1 . HIS A 1 127  ? 194.385 189.502 193.519 1.00 3.30  ? 77  HIS A ND1 1 
ATOM 480  C CD2 . HIS A 1 127  ? 195.464 191.345 193.908 1.00 1.50  ? 77  HIS A CD2 1 
ATOM 481  C CE1 . HIS A 1 127  ? 193.500 190.390 193.949 1.00 6.21  ? 77  HIS A CE1 1 
ATOM 482  N NE2 . HIS A 1 127  ? 194.135 191.516 194.192 1.00 2.63  ? 77  HIS A NE2 1 
ATOM 483  N N   . TYR A 1 128  ? 200.220 189.320 193.342 1.00 1.88  ? 78  TYR A N   1 
ATOM 484  C CA  . TYR A 1 128  ? 201.519 188.663 193.025 1.00 0.00  ? 78  TYR A CA  1 
ATOM 485  C C   . TYR A 1 128  ? 202.045 187.922 194.254 1.00 4.23  ? 78  TYR A C   1 
ATOM 486  O O   . TYR A 1 128  ? 201.724 188.318 195.396 1.00 15.48 ? 78  TYR A O   1 
ATOM 487  C CB  . TYR A 1 128  ? 202.516 189.704 192.504 1.00 0.00  ? 78  TYR A CB  1 
ATOM 488  C CG  . TYR A 1 128  ? 202.642 190.988 193.315 1.00 4.91  ? 78  TYR A CG  1 
ATOM 489  C CD1 . TYR A 1 128  ? 201.626 191.938 193.330 1.00 5.67  ? 78  TYR A CD1 1 
ATOM 490  C CD2 . TYR A 1 128  ? 203.789 191.260 194.049 1.00 6.24  ? 78  TYR A CD2 1 
ATOM 491  C CE1 . TYR A 1 128  ? 201.741 193.110 194.058 1.00 1.29  ? 78  TYR A CE1 1 
ATOM 492  C CE2 . TYR A 1 128  ? 203.918 192.430 194.780 1.00 3.08  ? 78  TYR A CE2 1 
ATOM 493  C CZ  . TYR A 1 128  ? 202.890 193.356 194.786 1.00 0.16  ? 78  TYR A CZ  1 
ATOM 494  O OH  . TYR A 1 128  ? 203.011 194.508 195.509 1.00 0.00  ? 78  TYR A OH  1 
ATOM 495  N N   . LEU A 1 129  ? 202.838 186.871 194.023 1.00 4.82  ? 79  LEU A N   1 
ATOM 496  C CA  . LEU A 1 129  ? 203.416 186.078 195.140 1.00 6.36  ? 79  LEU A CA  1 
ATOM 497  C C   . LEU A 1 129  ? 204.824 186.599 195.445 1.00 14.74 ? 79  LEU A C   1 
ATOM 498  O O   . LEU A 1 129  ? 205.562 186.894 194.485 1.00 17.36 ? 79  LEU A O   1 
ATOM 499  C CB  . LEU A 1 129  ? 203.456 184.606 194.722 1.00 2.35  ? 79  LEU A CB  1 
ATOM 500  C CG  . LEU A 1 129  ? 204.353 183.699 195.562 1.00 5.86  ? 79  LEU A CG  1 
ATOM 501  C CD1 . LEU A 1 129  ? 203.597 183.147 196.761 1.00 10.31 ? 79  LEU A CD1 1 
ATOM 502  C CD2 . LEU A 1 129  ? 204.914 182.566 194.717 1.00 1.44  ? 79  LEU A CD2 1 
ATOM 503  N N   . VAL A 1 130  ? 205.174 186.707 196.730 1.00 12.60 ? 80  VAL A N   1 
ATOM 504  C CA  . VAL A 1 130  ? 206.535 187.178 197.124 1.00 9.57  ? 80  VAL A CA  1 
ATOM 505  C C   . VAL A 1 130  ? 207.573 186.186 196.588 1.00 13.33 ? 80  VAL A C   1 
ATOM 506  O O   . VAL A 1 130  ? 207.357 184.966 196.731 1.00 11.88 ? 80  VAL A O   1 
ATOM 507  C CB  . VAL A 1 130  ? 206.649 187.351 198.651 1.00 7.96  ? 80  VAL A CB  1 
ATOM 508  C CG1 . VAL A 1 130  ? 205.888 188.577 199.133 1.00 8.39  ? 80  VAL A CG1 1 
ATOM 509  C CG2 . VAL A 1 130  ? 206.190 186.109 199.400 1.00 7.06  ? 80  VAL A CG2 1 
ATOM 510  N N   . GLN A 1 131  ? 208.652 186.695 195.983 1.00 14.25 ? 81  GLN A N   1 
ATOM 511  C CA  . GLN A 1 131  ? 209.724 185.816 195.442 1.00 16.24 ? 81  GLN A CA  1 
ATOM 512  C C   . GLN A 1 131  ? 211.087 186.362 195.878 1.00 14.40 ? 81  GLN A C   1 
ATOM 513  O O   . GLN A 1 131  ? 211.447 187.469 195.433 1.00 9.09  ? 81  GLN A O   1 
ATOM 514  C CB  . GLN A 1 131  ? 209.630 185.725 193.918 1.00 13.73 ? 81  GLN A CB  1 
ATOM 515  C CG  . GLN A 1 131  ? 208.294 185.196 193.416 1.00 12.00 ? 81  GLN A CG  1 
ATOM 516  C CD  . GLN A 1 131  ? 208.239 183.688 193.378 1.00 12.04 ? 81  GLN A CD  1 
ATOM 517  O OE1 . GLN A 1 131  ? 208.703 183.004 194.288 1.00 10.45 ? 81  GLN A OE1 1 
ATOM 518  N NE2 . GLN A 1 131  ? 207.661 183.155 192.314 1.00 13.84 ? 81  GLN A NE2 1 
ATOM 519  N N   . GLU A 1 132  ? 211.810 185.612 196.714 1.00 21.39 ? 82  GLU A N   1 
ATOM 520  C CA  . GLU A 1 132  ? 213.113 186.063 197.202 1.00 23.87 ? 82  GLU A CA  1 
ATOM 521  C C   . GLU A 1 132  ? 214.184 185.744 196.158 1.00 25.70 ? 82  GLU A C   1 
ATOM 522  O O   . GLU A 1 132  ? 215.043 184.878 196.332 1.00 26.29 ? 82  GLU A O   1 
ATOM 523  C CB  . GLU A 1 132  ? 213.432 185.419 198.544 1.00 22.81 ? 82  GLU A CB  1 
ATOM 524  C CG  . GLU A 1 132  ? 212.356 185.601 199.601 1.00 22.35 ? 82  GLU A CG  1 
ATOM 525  C CD  . GLU A 1 132  ? 212.007 187.057 199.830 1.00 25.94 ? 82  GLU A CD  1 
ATOM 526  O OE1 . GLU A 1 132  ? 212.908 187.831 200.213 1.00 22.84 ? 82  GLU A OE1 1 
ATOM 527  O OE2 . GLU A 1 132  ? 210.831 187.427 199.633 1.00 25.20 ? 82  GLU A OE2 1 
ATOM 528  N N   . SER A 1 133  ? 214.114 186.472 195.043 1.00 24.93 ? 83  SER A N   1 
ATOM 529  C CA  . SER A 1 133  ? 215.097 186.322 193.978 1.00 28.08 ? 83  SER A CA  1 
ATOM 530  C C   . SER A 1 133  ? 216.480 186.712 194.483 1.00 29.32 ? 83  SER A C   1 
ATOM 531  O O   . SER A 1 133  ? 216.730 187.882 194.788 1.00 25.96 ? 83  SER A O   1 
ATOM 532  C CB  . SER A 1 133  ? 214.710 187.167 192.763 1.00 24.16 ? 83  SER A CB  1 
ATOM 533  O OG  . SER A 1 133  ? 215.445 186.776 191.617 1.00 21.31 ? 83  SER A OG  1 
ATOM 534  N N   . THR A 1 134  ? 217.383 185.736 194.579 1.00 32.93 ? 84  THR A N   1 
ATOM 535  C CA  . THR A 1 134  ? 218.695 185.985 195.167 1.00 29.30 ? 84  THR A CA  1 
ATOM 536  C C   . THR A 1 134  ? 219.666 186.570 194.146 1.00 29.39 ? 84  THR A C   1 
ATOM 537  O O   . THR A 1 134  ? 220.227 187.651 194.355 1.00 27.30 ? 84  THR A O   1 
ATOM 538  C CB  . THR A 1 134  ? 219.257 184.691 195.761 1.00 27.90 ? 84  THR A CB  1 
ATOM 539  O OG1 . THR A 1 134  ? 219.245 183.661 194.764 1.00 28.57 ? 84  THR A OG1 1 
ATOM 540  C CG2 . THR A 1 134  ? 218.419 184.246 196.950 1.00 26.24 ? 84  THR A CG2 1 
ATOM 541  N N   . ASP A 1 135  ? 219.876 185.868 193.035 1.00 31.41 ? 85  ASP A N   1 
ATOM 542  C CA  . ASP A 1 135  ? 220.851 186.297 192.042 1.00 32.62 ? 85  ASP A CA  1 
ATOM 543  C C   . ASP A 1 135  ? 220.246 187.349 191.122 1.00 34.64 ? 85  ASP A C   1 
ATOM 544  O O   . ASP A 1 135  ? 219.193 187.127 190.515 1.00 32.20 ? 85  ASP A O   1 
ATOM 545  C CB  . ASP A 1 135  ? 221.344 185.101 191.227 1.00 32.09 ? 85  ASP A CB  1 
ATOM 546  C CG  . ASP A 1 135  ? 222.475 185.465 190.280 1.00 31.84 ? 85  ASP A CG  1 
ATOM 547  O OD1 . ASP A 1 135  ? 222.200 186.065 189.219 1.00 25.01 ? 85  ASP A OD1 1 
ATOM 548  O OD2 . ASP A 1 135  ? 223.641 185.151 190.598 1.00 33.15 ? 85  ASP A OD2 1 
ATOM 549  N N   . LYS A 1 136  ? 220.918 188.497 191.020 1.00 36.19 ? 86  LYS A N   1 
ATOM 550  C CA  . LYS A 1 136  ? 220.517 189.558 190.112 1.00 32.11 ? 86  LYS A CA  1 
ATOM 551  C C   . LYS A 1 136  ? 221.594 189.934 189.105 1.00 31.41 ? 86  LYS A C   1 
ATOM 552  O O   . LYS A 1 136  ? 221.352 190.815 188.272 1.00 30.71 ? 86  LYS A O   1 
ATOM 553  C CB  . LYS A 1 136  ? 220.108 190.815 190.898 1.00 30.56 ? 86  LYS A CB  1 
ATOM 554  C CG  . LYS A 1 136  ? 219.113 190.552 192.017 1.00 32.06 ? 86  LYS A CG  1 
ATOM 555  C CD  . LYS A 1 136  ? 217.831 189.930 191.487 1.00 33.47 ? 86  LYS A CD  1 
ATOM 556  C CE  . LYS A 1 136  ? 217.097 190.880 190.557 1.00 34.50 ? 86  LYS A CE  1 
ATOM 557  N NZ  . LYS A 1 136  ? 215.624 190.670 190.609 1.00 33.96 ? 86  LYS A NZ  1 
ATOM 558  N N   . GLU A 1 137  ? 222.768 189.299 189.156 1.00 33.22 ? 87  GLU A N   1 
ATOM 559  C CA  . GLU A 1 137  ? 223.827 189.604 188.198 1.00 32.93 ? 87  GLU A CA  1 
ATOM 560  C C   . GLU A 1 137  ? 223.418 189.227 186.780 1.00 33.78 ? 87  GLU A C   1 
ATOM 561  O O   . GLU A 1 137  ? 223.938 189.783 185.806 1.00 31.25 ? 87  GLU A O   1 
ATOM 562  C CB  . GLU A 1 137  ? 225.115 188.881 188.595 1.00 32.12 ? 87  GLU A CB  1 
ATOM 563  C CG  . GLU A 1 137  ? 226.364 189.383 187.887 1.00 33.36 ? 87  GLU A CG  1 
ATOM 564  C CD  . GLU A 1 137  ? 226.686 188.584 186.639 1.00 36.66 ? 87  GLU A CD  1 
ATOM 565  O OE1 . GLU A 1 137  ? 226.071 187.516 186.441 1.00 37.00 ? 87  GLU A OE1 1 
ATOM 566  O OE2 . GLU A 1 137  ? 227.557 189.021 185.858 1.00 34.98 ? 87  GLU A OE2 1 
ATOM 567  N N   . GLY A 1 138  ? 222.494 188.277 186.644 1.00 31.11 ? 88  GLY A N   1 
ATOM 568  C CA  . GLY A 1 138  ? 222.001 187.882 185.340 1.00 30.18 ? 88  GLY A CA  1 
ATOM 569  C C   . GLY A 1 138  ? 221.383 189.038 184.582 1.00 28.72 ? 88  GLY A C   1 
ATOM 570  O O   . GLY A 1 138  ? 220.458 189.691 185.073 1.00 27.45 ? 88  GLY A O   1 
ATOM 571  N N   . LYS A 1 139  ? 221.889 189.297 183.379 1.00 29.12 ? 89  LYS A N   1 
ATOM 572  C CA  . LYS A 1 139  ? 221.457 190.447 182.584 1.00 29.57 ? 89  LYS A CA  1 
ATOM 573  C C   . LYS A 1 139  ? 220.286 190.066 181.676 1.00 31.37 ? 89  LYS A C   1 
ATOM 574  O O   . LYS A 1 139  ? 220.273 190.331 180.473 1.00 30.68 ? 89  LYS A O   1 
ATOM 575  C CB  . LYS A 1 139  ? 222.633 190.994 181.784 1.00 29.30 ? 89  LYS A CB  1 
ATOM 576  C CG  . LYS A 1 139  ? 223.320 189.952 180.917 1.00 27.67 ? 89  LYS A CG  1 
ATOM 577  C CD  . LYS A 1 139  ? 224.514 190.532 180.186 1.00 27.96 ? 89  LYS A CD  1 
ATOM 578  C CE  . LYS A 1 139  ? 225.173 189.483 179.309 1.00 26.82 ? 89  LYS A CE  1 
ATOM 579  N NZ  . LYS A 1 139  ? 225.691 188.343 180.112 1.00 26.68 ? 89  LYS A NZ  1 
ATOM 580  N N   . ASP A 1 140  ? 219.275 189.458 182.297 1.00 33.19 ? 90  ASP A N   1 
ATOM 581  C CA  . ASP A 1 140  ? 218.079 188.988 181.600 1.00 34.95 ? 90  ASP A CA  1 
ATOM 582  C C   . ASP A 1 140  ? 218.457 188.123 180.399 1.00 34.88 ? 90  ASP A C   1 
ATOM 583  O O   . ASP A 1 140  ? 218.124 188.423 179.249 1.00 33.60 ? 90  ASP A O   1 
ATOM 584  C CB  . ASP A 1 140  ? 217.192 190.165 181.184 1.00 34.28 ? 90  ASP A CB  1 
ATOM 585  C CG  . ASP A 1 140  ? 215.834 189.722 180.674 1.00 36.53 ? 90  ASP A CG  1 
ATOM 586  O OD1 . ASP A 1 140  ? 215.048 189.172 181.473 1.00 36.20 ? 90  ASP A OD1 1 
ATOM 587  O OD2 . ASP A 1 140  ? 215.553 189.926 179.474 1.00 34.87 ? 90  ASP A OD2 1 
ATOM 588  N N   . GLU A 1 141  ? 219.186 187.043 180.679 1.00 31.07 ? 91  GLU A N   1 
ATOM 589  C CA  . GLU A 1 141  ? 219.643 186.143 179.628 1.00 31.75 ? 91  GLU A CA  1 
ATOM 590  C C   . GLU A 1 141  ? 218.452 185.584 178.862 1.00 32.79 ? 91  GLU A C   1 
ATOM 591  O O   . GLU A 1 141  ? 217.501 185.075 179.461 1.00 33.67 ? 91  GLU A O   1 
ATOM 592  C CB  . GLU A 1 141  ? 220.470 185.009 180.232 1.00 32.49 ? 91  GLU A CB  1 
ATOM 593  C CG  . GLU A 1 141  ? 221.769 185.463 180.876 1.00 32.27 ? 91  GLU A CG  1 
ATOM 594  C CD  . GLU A 1 141  ? 222.672 186.198 179.905 1.00 33.14 ? 91  GLU A CD  1 
ATOM 595  O OE1 . GLU A 1 141  ? 222.759 185.772 178.734 1.00 31.06 ? 91  GLU A OE1 1 
ATOM 596  O OE2 . GLU A 1 141  ? 223.291 187.202 180.312 1.00 31.98 ? 91  GLU A OE2 1 
ATOM 597  N N   . LEU A 1 142  ? 218.507 185.679 177.538 1.00 32.46 ? 92  LEU A N   1 
ATOM 598  C CA  . LEU A 1 142  ? 217.402 185.286 176.678 1.00 34.53 ? 92  LEU A CA  1 
ATOM 599  C C   . LEU A 1 142  ? 217.878 184.267 175.653 1.00 36.33 ? 92  LEU A C   1 
ATOM 600  O O   . LEU A 1 142  ? 218.972 184.395 175.096 1.00 36.43 ? 92  LEU A O   1 
ATOM 601  C CB  . LEU A 1 142  ? 216.799 186.503 175.970 1.00 34.41 ? 92  LEU A CB  1 
ATOM 602  C CG  . LEU A 1 142  ? 216.123 187.547 176.860 1.00 35.82 ? 92  LEU A CG  1 
ATOM 603  C CD1 . LEU A 1 142  ? 215.711 188.752 176.033 1.00 32.90 ? 92  LEU A CD1 1 
ATOM 604  C CD2 . LEU A 1 142  ? 214.924 186.945 177.571 1.00 33.95 ? 92  LEU A CD2 1 
ATOM 605  N N   . LEU A 1 143  ? 217.050 183.258 175.413 1.00 35.02 ? 93  LEU A N   1 
ATOM 606  C CA  . LEU A 1 143  ? 217.324 182.219 174.433 1.00 31.98 ? 93  LEU A CA  1 
ATOM 607  C C   . LEU A 1 143  ? 216.469 182.445 173.189 1.00 27.91 ? 93  LEU A C   1 
ATOM 608  O O   . LEU A 1 143  ? 215.513 183.222 173.193 1.00 25.75 ? 93  LEU A O   1 
ATOM 609  C CB  . LEU A 1 143  ? 217.059 180.836 175.044 1.00 30.29 ? 93  LEU A CB  1 
ATOM 610  C CG  . LEU A 1 143  ? 217.391 179.568 174.250 1.00 29.53 ? 93  LEU A CG  1 
ATOM 611  C CD1 . LEU A 1 143  ? 218.887 179.460 174.006 1.00 27.34 ? 93  LEU A CD1 1 
ATOM 612  C CD2 . LEU A 1 143  ? 216.870 178.332 174.964 1.00 31.81 ? 93  LEU A CD2 1 
ATOM 613  N N   . GLU A 1 144  ? 216.842 181.768 172.100 1.00 27.53 ? 94  GLU A N   1 
ATOM 614  C CA  . GLU A 1 144  ? 216.034 181.834 170.887 1.00 32.43 ? 94  GLU A CA  1 
ATOM 615  C C   . GLU A 1 144  ? 214.638 181.271 171.120 1.00 31.34 ? 94  GLU A C   1 
ATOM 616  O O   . GLU A 1 144  ? 213.652 181.829 170.624 1.00 25.77 ? 94  GLU A O   1 
ATOM 617  C CB  . GLU A 1 144  ? 216.731 181.089 169.747 1.00 29.62 ? 94  GLU A CB  1 
ATOM 618  C CG  . GLU A 1 144  ? 215.980 181.128 168.425 1.00 27.38 ? 94  GLU A CG  1 
ATOM 619  C CD  . GLU A 1 144  ? 215.285 179.819 168.107 1.00 29.15 ? 94  GLU A CD  1 
ATOM 620  O OE1 . GLU A 1 144  ? 215.984 178.801 167.918 1.00 31.66 ? 94  GLU A OE1 1 
ATOM 621  O OE2 . GLU A 1 144  ? 214.037 179.808 168.044 1.00 28.75 ? 94  GLU A OE2 1 
ATOM 622  N N   . ASP A 1 145  ? 214.532 180.177 171.872 1.00 30.91 ? 95  ASP A N   1 
ATOM 623  C CA  . ASP A 1 145  ? 213.253 179.568 172.228 1.00 30.06 ? 95  ASP A CA  1 
ATOM 624  C C   . ASP A 1 145  ? 212.952 179.926 173.680 1.00 31.21 ? 95  ASP A C   1 
ATOM 625  O O   . ASP A 1 145  ? 213.529 179.343 174.603 1.00 29.68 ? 95  ASP A O   1 
ATOM 626  C CB  . ASP A 1 145  ? 213.294 178.056 172.024 1.00 27.60 ? 95  ASP A CB  1 
ATOM 627  C CG  . ASP A 1 145  ? 211.976 177.385 172.359 1.00 26.46 ? 95  ASP A CG  1 
ATOM 628  O OD1 . ASP A 1 145  ? 210.977 177.652 171.661 1.00 27.05 ? 95  ASP A OD1 1 
ATOM 629  O OD2 . ASP A 1 145  ? 211.942 176.588 173.321 1.00 25.81 ? 95  ASP A OD2 1 
ATOM 630  N N   . VAL A 1 146  ? 212.057 180.891 173.883 1.00 26.06 ? 96  VAL A N   1 
ATOM 631  C CA  . VAL A 1 146  ? 211.649 181.322 175.218 1.00 20.98 ? 96  VAL A CA  1 
ATOM 632  C C   . VAL A 1 146  ? 210.122 181.327 175.276 1.00 24.69 ? 96  VAL A C   1 
ATOM 633  O O   . VAL A 1 146  ? 209.461 182.304 174.903 1.00 21.94 ? 96  VAL A O   1 
ATOM 634  C CB  . VAL A 1 146  ? 212.254 182.680 175.605 1.00 18.11 ? 96  VAL A CB  1 
ATOM 635  C CG1 . VAL A 1 146  ? 211.699 183.128 176.941 1.00 17.32 ? 96  VAL A CG1 1 
ATOM 636  C CG2 . VAL A 1 146  ? 213.771 182.609 175.723 1.00 22.48 ? 96  VAL A CG2 1 
ATOM 637  N N   . VAL A 1 147  ? 209.556 180.262 175.851 1.00 21.40 ? 97  VAL A N   1 
ATOM 638  C CA  . VAL A 1 147  ? 208.078 180.231 176.063 1.00 14.63 ? 97  VAL A CA  1 
ATOM 639  C C   . VAL A 1 147  ? 207.790 180.982 177.370 1.00 12.52 ? 97  VAL A C   1 
ATOM 640  O O   . VAL A 1 147  ? 208.553 180.783 178.338 1.00 10.66 ? 97  VAL A O   1 
ATOM 641  C CB  . VAL A 1 147  ? 207.549 178.783 176.089 1.00 14.21 ? 97  VAL A CB  1 
ATOM 642  C CG1 . VAL A 1 147  ? 208.131 177.992 177.251 1.00 11.68 ? 97  VAL A CG1 1 
ATOM 643  C CG2 . VAL A 1 147  ? 206.030 178.719 176.105 1.00 11.00 ? 97  VAL A CG2 1 
ATOM 644  N N   . PRO A 1 148  ? 206.761 181.857 177.440 1.00 10.40 ? 98  PRO A N   1 
ATOM 645  C CA  . PRO A 1 148  ? 206.496 182.666 178.644 1.00 11.51 ? 98  PRO A CA  1 
ATOM 646  C C   . PRO A 1 148  ? 206.521 181.894 179.972 1.00 4.24  ? 98  PRO A C   1 
ATOM 647  O O   . PRO A 1 148  ? 206.173 180.727 179.980 1.00 9.69  ? 98  PRO A O   1 
ATOM 648  C CB  . PRO A 1 148  ? 205.072 183.185 178.390 1.00 11.35 ? 98  PRO A CB  1 
ATOM 649  C CG  . PRO A 1 148  ? 205.001 183.312 176.886 1.00 0.00  ? 98  PRO A CG  1 
ATOM 650  C CD  . PRO A 1 148  ? 205.811 182.144 176.361 1.00 2.14  ? 98  PRO A CD  1 
ATOM 651  N N   . GLN A 1 149  ? 206.912 182.566 181.061 1.00 0.00  ? 99  GLN A N   1 
ATOM 652  C CA  . GLN A 1 149  ? 206.959 181.925 182.373 1.00 3.53  ? 99  GLN A CA  1 
ATOM 653  C C   . GLN A 1 149  ? 205.598 181.379 182.786 1.00 5.67  ? 99  GLN A C   1 
ATOM 654  O O   . GLN A 1 149  ? 205.501 180.253 183.291 1.00 13.76 ? 99  GLN A O   1 
ATOM 655  C CB  . GLN A 1 149  ? 207.470 182.919 183.415 1.00 12.40 ? 99  GLN A CB  1 
ATOM 656  C CG  . GLN A 1 149  ? 207.493 182.384 184.835 1.00 5.85  ? 99  GLN A CG  1 
ATOM 657  C CD  . GLN A 1 149  ? 208.689 181.493 185.097 1.00 9.25  ? 99  GLN A CD  1 
ATOM 658  O OE1 . GLN A 1 149  ? 209.806 181.976 185.284 1.00 13.03 ? 99  GLN A OE1 1 
ATOM 659  N NE2 . GLN A 1 149  ? 208.461 180.185 185.114 1.00 7.92  ? 99  GLN A NE2 1 
ATOM 660  N N   . SER A 1 150  ? 204.535 182.164 182.596 1.00 5.00  ? 100 SER A N   1 
ATOM 661  C CA  . SER A 1 150  ? 203.202 181.687 182.946 1.00 3.82  ? 100 SER A CA  1 
ATOM 662  C C   . SER A 1 150  ? 202.803 180.491 182.095 1.00 4.06  ? 100 SER A C   1 
ATOM 663  O O   . SER A 1 150  ? 202.083 179.602 182.567 1.00 16.68 ? 100 SER A O   1 
ATOM 664  C CB  . SER A 1 150  ? 202.181 182.812 182.793 1.00 9.89  ? 100 SER A CB  1 
ATOM 665  O OG  . SER A 1 150  ? 202.213 183.351 181.484 1.00 13.16 ? 100 SER A OG  1 
ATOM 666  N N   . MET A 1 151  ? 203.275 180.444 180.849 1.00 0.00  ? 101 MET A N   1 
ATOM 667  C CA  . MET A 1 151  ? 202.980 179.312 179.980 1.00 0.00  ? 101 MET A CA  1 
ATOM 668  C C   . MET A 1 151  ? 203.538 178.015 180.554 1.00 0.00  ? 101 MET A C   1 
ATOM 669  O O   . MET A 1 151  ? 202.848 176.991 180.590 1.00 3.79  ? 101 MET A O   1 
ATOM 670  C CB  . MET A 1 151  ? 203.545 179.575 178.589 1.00 5.53  ? 101 MET A CB  1 
ATOM 671  C CG  . MET A 1 151  ? 202.659 180.437 177.724 1.00 4.36  ? 101 MET A CG  1 
ATOM 672  S SD  . MET A 1 151  ? 202.869 180.015 175.995 1.00 17.92 ? 101 MET A SD  1 
ATOM 673  C CE  . MET A 1 151  ? 201.488 178.908 175.770 1.00 8.22  ? 101 MET A CE  1 
ATOM 674  N N   . GLN A 1 152  ? 204.794 178.039 181.005 1.00 0.02  ? 102 GLN A N   1 
ATOM 675  C CA  . GLN A 1 152  ? 205.355 176.864 181.664 1.00 0.63  ? 102 GLN A CA  1 
ATOM 676  C C   . GLN A 1 152  ? 204.633 176.571 182.972 1.00 1.13  ? 102 GLN A C   1 
ATOM 677  O O   . GLN A 1 152  ? 204.311 175.414 183.266 1.00 5.38  ? 102 GLN A O   1 
ATOM 678  C CB  . GLN A 1 152  ? 206.847 177.058 181.920 1.00 5.66  ? 102 GLN A CB  1 
ATOM 679  C CG  . GLN A 1 152  ? 207.680 177.238 180.674 1.00 7.49  ? 102 GLN A CG  1 
ATOM 680  C CD  . GLN A 1 152  ? 209.137 177.494 180.992 1.00 9.56  ? 102 GLN A CD  1 
ATOM 681  O OE1 . GLN A 1 152  ? 209.681 176.949 181.951 1.00 11.25 ? 102 GLN A OE1 1 
ATOM 682  N NE2 . GLN A 1 152  ? 209.780 178.327 180.182 1.00 8.81  ? 102 GLN A NE2 1 
ATOM 683  N N   . ASP A 1 153  ? 204.361 177.610 183.766 1.00 0.00  ? 103 ASP A N   1 
ATOM 684  C CA  . ASP A 1 153  ? 203.716 177.410 185.059 1.00 2.52  ? 103 ASP A CA  1 
ATOM 685  C C   . ASP A 1 153  ? 202.308 176.852 184.922 1.00 1.05  ? 103 ASP A C   1 
ATOM 686  O O   . ASP A 1 153  ? 201.748 176.366 185.911 1.00 1.87  ? 103 ASP A O   1 
ATOM 687  C CB  . ASP A 1 153  ? 203.684 178.725 185.836 1.00 0.00  ? 103 ASP A CB  1 
ATOM 688  C CG  . ASP A 1 153  ? 205.059 179.158 186.299 1.00 4.25  ? 103 ASP A CG  1 
ATOM 689  O OD1 . ASP A 1 153  ? 206.045 178.479 185.943 1.00 4.00  ? 103 ASP A OD1 1 
ATOM 690  O OD2 . ASP A 1 153  ? 205.154 180.174 187.019 1.00 6.54  ? 103 ASP A OD2 1 
ATOM 691  N N   . LEU A 1 154  ? 201.716 176.930 183.729 1.00 0.85  ? 104 LEU A N   1 
ATOM 692  C CA  . LEU A 1 154  ? 200.440 176.259 183.508 1.00 0.00  ? 104 LEU A CA  1 
ATOM 693  C C   . LEU A 1 154  ? 200.539 174.762 183.775 1.00 3.61  ? 104 LEU A C   1 
ATOM 694  O O   . LEU A 1 154  ? 199.541 174.132 184.143 1.00 11.31 ? 104 LEU A O   1 
ATOM 695  C CB  . LEU A 1 154  ? 199.950 176.492 182.079 1.00 0.00  ? 104 LEU A CB  1 
ATOM 696  C CG  . LEU A 1 154  ? 199.550 177.904 181.653 1.00 0.00  ? 104 LEU A CG  1 
ATOM 697  C CD1 . LEU A 1 154  ? 198.767 177.851 180.355 1.00 0.55  ? 104 LEU A CD1 1 
ATOM 698  C CD2 . LEU A 1 154  ? 198.756 178.609 182.740 1.00 0.00  ? 104 LEU A CD2 1 
ATOM 699  N N   . LEU A 1 155  ? 201.726 174.178 183.604 1.00 5.63  ? 105 LEU A N   1 
ATOM 700  C CA  . LEU A 1 155  ? 201.921 172.738 183.708 1.00 5.52  ? 105 LEU A CA  1 
ATOM 701  C C   . LEU A 1 155  ? 202.502 172.303 185.048 1.00 4.66  ? 105 LEU A C   1 
ATOM 702  O O   . LEU A 1 155  ? 202.937 171.155 185.176 1.00 3.48  ? 105 LEU A O   1 
ATOM 703  C CB  . LEU A 1 155  ? 202.826 172.247 182.577 1.00 0.93  ? 105 LEU A CB  1 
ATOM 704  C CG  . LEU A 1 155  ? 202.217 172.155 181.178 1.00 0.53  ? 105 LEU A CG  1 
ATOM 705  C CD1 . LEU A 1 155  ? 203.189 171.472 180.231 1.00 4.47  ? 105 LEU A CD1 1 
ATOM 706  C CD2 . LEU A 1 155  ? 200.890 171.424 181.209 1.00 0.00  ? 105 LEU A CD2 1 
ATOM 707  N N   . GLY A 1 156  ? 202.532 173.188 186.041 1.00 6.76  ? 106 GLY A N   1 
ATOM 708  C CA  . GLY A 1 156  ? 203.057 172.813 187.340 1.00 8.23  ? 106 GLY A CA  1 
ATOM 709  C C   . GLY A 1 156  ? 202.152 171.834 188.065 1.00 4.49  ? 106 GLY A C   1 
ATOM 710  O O   . GLY A 1 156  ? 200.926 171.888 187.968 1.00 0.00  ? 106 GLY A O   1 
ATOM 711  N N   . MET A 1 157  ? 202.778 170.924 188.815 1.00 3.61  ? 107 MET A N   1 
ATOM 712  C CA  . MET A 1 157  ? 202.053 169.881 189.526 1.00 3.61  ? 107 MET A CA  1 
ATOM 713  C C   . MET A 1 157  ? 202.366 169.817 191.015 1.00 6.40  ? 107 MET A C   1 
ATOM 714  O O   . MET A 1 157  ? 201.735 169.029 191.727 1.00 4.24  ? 107 MET A O   1 
ATOM 715  C CB  . MET A 1 157  ? 202.338 168.508 188.899 1.00 6.08  ? 107 MET A CB  1 
ATOM 716  C CG  . MET A 1 157  ? 201.395 168.133 187.771 1.00 10.37 ? 107 MET A CG  1 
ATOM 717  S SD  . MET A 1 157  ? 201.464 166.382 187.359 1.00 11.60 ? 107 MET A SD  1 
ATOM 718  C CE  . MET A 1 157  ? 201.293 166.458 185.581 1.00 0.00  ? 107 MET A CE  1 
ATOM 719  N N   . ASN A 1 158  ? 203.316 170.613 191.506 1.00 10.88 ? 108 ASN A N   1 
ATOM 720  C CA  . ASN A 1 158  ? 203.683 170.549 192.915 1.00 10.29 ? 108 ASN A CA  1 
ATOM 721  C C   . ASN A 1 158  ? 202.633 171.170 193.825 1.00 10.73 ? 108 ASN A C   1 
ATOM 722  O O   . ASN A 1 158  ? 202.503 170.747 194.978 1.00 15.36 ? 108 ASN A O   1 
ATOM 723  C CB  . ASN A 1 158  ? 205.024 171.246 193.141 1.00 12.43 ? 108 ASN A CB  1 
ATOM 724  C CG  . ASN A 1 158  ? 206.147 170.618 192.349 1.00 12.98 ? 108 ASN A CG  1 
ATOM 725  O OD1 . ASN A 1 158  ? 206.097 169.437 192.011 1.00 13.20 ? 108 ASN A OD1 1 
ATOM 726  N ND2 . ASN A 1 158  ? 207.169 171.408 192.045 1.00 12.15 ? 108 ASN A ND2 1 
ATOM 727  N N   . ASN A 1 159  ? 201.879 172.153 193.336 1.00 5.19  ? 109 ASN A N   1 
ATOM 728  C CA  . ASN A 1 159  ? 201.007 172.963 194.177 1.00 1.66  ? 109 ASN A CA  1 
ATOM 729  C C   . ASN A 1 159  ? 199.533 172.758 193.843 1.00 4.42  ? 109 ASN A C   1 
ATOM 730  O O   . ASN A 1 159  ? 198.749 173.707 193.878 1.00 8.39  ? 109 ASN A O   1 
ATOM 731  C CB  . ASN A 1 159  ? 201.377 174.439 194.052 1.00 2.17  ? 109 ASN A CB  1 
ATOM 732  C CG  . ASN A 1 159  ? 202.856 174.682 194.238 1.00 1.92  ? 109 ASN A CG  1 
ATOM 733  O OD1 . ASN A 1 159  ? 203.370 174.611 195.352 1.00 8.40  ? 109 ASN A OD1 1 
ATOM 734  N ND2 . ASN A 1 159  ? 203.552 174.967 193.146 1.00 0.00  ? 109 ASN A ND2 1 
ATOM 735  N N   . ASP A 1 160  ? 199.138 171.530 193.523 1.00 8.49  ? 110 ASP A N   1 
ATOM 736  C CA  . ASP A 1 160  ? 197.749 171.276 193.165 1.00 7.63  ? 110 ASP A CA  1 
ATOM 737  C C   . ASP A 1 160  ? 196.840 171.431 194.377 1.00 0.77  ? 110 ASP A C   1 
ATOM 738  O O   . ASP A 1 160  ? 197.144 170.944 195.470 1.00 0.00  ? 110 ASP A O   1 
ATOM 739  C CB  . ASP A 1 160  ? 197.593 169.878 192.568 1.00 9.64  ? 110 ASP A CB  1 
ATOM 740  C CG  . ASP A 1 160  ? 198.089 169.796 191.138 1.00 6.06  ? 110 ASP A CG  1 
ATOM 741  O OD1 . ASP A 1 160  ? 197.404 170.320 190.235 1.00 1.55  ? 110 ASP A OD1 1 
ATOM 742  O OD2 . ASP A 1 160  ? 199.160 169.199 190.914 1.00 3.06  ? 110 ASP A OD2 1 
ATOM 743  N N   . PHE A 1 161  ? 195.705 172.102 194.141 1.00 1.92  ? 111 PHE A N   1 
ATOM 744  C CA  . PHE A 1 161  ? 194.678 172.281 195.200 1.00 4.16  ? 111 PHE A CA  1 
ATOM 745  C C   . PHE A 1 161  ? 195.263 172.978 196.430 1.00 13.07 ? 111 PHE A C   1 
ATOM 746  O O   . PHE A 1 161  ? 195.390 172.314 197.478 1.00 18.27 ? 111 PHE A O   1 
ATOM 747  C CB  . PHE A 1 161  ? 194.047 170.932 195.555 1.00 4.98  ? 111 PHE A CB  1 
ATOM 748  C CG  . PHE A 1 161  ? 193.609 170.122 194.362 1.00 3.22  ? 111 PHE A CG  1 
ATOM 749  C CD1 . PHE A 1 161  ? 192.544 170.534 193.577 1.00 4.50  ? 111 PHE A CD1 1 
ATOM 750  C CD2 . PHE A 1 161  ? 194.260 168.946 194.023 1.00 6.01  ? 111 PHE A CD2 1 
ATOM 751  C CE1 . PHE A 1 161  ? 192.138 169.787 192.483 1.00 8.10  ? 111 PHE A CE1 1 
ATOM 752  C CE2 . PHE A 1 161  ? 193.854 168.201 192.927 1.00 6.36  ? 111 PHE A CE2 1 
ATOM 753  C CZ  . PHE A 1 161  ? 192.792 168.621 192.161 1.00 6.28  ? 111 PHE A CZ  1 
ATOM 754  N N   . PRO A 1 162  ? 195.613 174.283 196.376 1.00 8.81  ? 112 PRO A N   1 
ATOM 755  C CA  . PRO A 1 162  ? 196.047 174.982 197.589 1.00 10.46 ? 112 PRO A CA  1 
ATOM 756  C C   . PRO A 1 162  ? 194.880 175.180 198.540 1.00 16.08 ? 112 PRO A C   1 
ATOM 757  O O   . PRO A 1 162  ? 193.755 175.465 198.100 1.00 14.43 ? 112 PRO A O   1 
ATOM 758  C CB  . PRO A 1 162  ? 196.572 176.323 197.056 1.00 1.65  ? 112 PRO A CB  1 
ATOM 759  C CG  . PRO A 1 162  ? 195.835 176.531 195.791 1.00 6.30  ? 112 PRO A CG  1 
ATOM 760  C CD  . PRO A 1 162  ? 195.600 175.171 195.201 1.00 6.93  ? 112 PRO A CD  1 
ATOM 761  N N   . PRO A 1 163  ? 195.101 175.021 199.850 1.00 15.34 ? 113 PRO A N   1 
ATOM 762  C CA  . PRO A 1 163  ? 193.979 175.146 200.797 1.00 13.23 ? 113 PRO A CA  1 
ATOM 763  C C   . PRO A 1 163  ? 193.315 176.509 200.777 1.00 14.48 ? 113 PRO A C   1 
ATOM 764  O O   . PRO A 1 163  ? 192.085 176.597 200.869 1.00 14.58 ? 113 PRO A O   1 
ATOM 765  C CB  . PRO A 1 163  ? 194.636 174.853 202.153 1.00 13.35 ? 113 PRO A CB  1 
ATOM 766  C CG  . PRO A 1 163  ? 196.079 175.156 201.949 1.00 12.79 ? 113 PRO A CG  1 
ATOM 767  C CD  . PRO A 1 163  ? 196.377 174.765 200.536 1.00 11.09 ? 113 PRO A CD  1 
ATOM 768  N N   . ARG A 1 164  ? 194.095 177.580 200.657 1.00 18.22 ? 114 ARG A N   1 
ATOM 769  C CA  . ARG A 1 164  ? 193.544 178.924 200.564 1.00 19.15 ? 114 ARG A CA  1 
ATOM 770  C C   . ARG A 1 164  ? 194.336 179.695 199.520 1.00 25.24 ? 114 ARG A C   1 
ATOM 771  O O   . ARG A 1 164  ? 195.571 179.664 199.519 1.00 29.02 ? 114 ARG A O   1 
ATOM 772  C CB  . ARG A 1 164  ? 193.558 179.633 201.930 1.00 18.40 ? 114 ARG A CB  1 
ATOM 773  C CG  . ARG A 1 164  ? 194.783 180.483 202.243 1.00 23.53 ? 114 ARG A CG  1 
ATOM 774  C CD  . ARG A 1 164  ? 194.907 180.747 203.735 1.00 28.50 ? 114 ARG A CD  1 
ATOM 775  N NE  . ARG A 1 164  ? 195.099 179.514 204.490 1.00 26.85 ? 114 ARG A NE  1 
ATOM 776  C CZ  . ARG A 1 164  ? 196.268 178.909 204.650 1.00 26.01 ? 114 ARG A CZ  1 
ATOM 777  N NH1 . ARG A 1 164  ? 197.380 179.407 204.136 1.00 25.88 ? 114 ARG A NH1 1 
ATOM 778  N NH2 . ARG A 1 164  ? 196.322 177.775 205.343 1.00 23.67 ? 114 ARG A NH2 1 
ATOM 779  N N   . ALA A 1 165  ? 193.615 180.347 198.612 1.00 23.35 ? 115 ALA A N   1 
ATOM 780  C CA  . ALA A 1 165  ? 194.197 181.091 197.503 1.00 14.95 ? 115 ALA A CA  1 
ATOM 781  C C   . ALA A 1 165  ? 193.055 181.764 196.759 1.00 18.61 ? 115 ALA A C   1 
ATOM 782  O O   . ALA A 1 165  ? 191.882 181.439 196.962 1.00 23.35 ? 115 ALA A O   1 
ATOM 783  C CB  . ALA A 1 165  ? 194.998 180.188 196.561 1.00 11.72 ? 115 ALA A CB  1 
ATOM 784  N N   . HIS A 1 166  ? 193.409 182.705 195.889 1.00 19.93 ? 116 HIS A N   1 
ATOM 785  C CA  . HIS A 1 166  ? 192.407 183.311 195.028 1.00 19.02 ? 116 HIS A CA  1 
ATOM 786  C C   . HIS A 1 166  ? 191.884 182.281 194.035 1.00 12.68 ? 116 HIS A C   1 
ATOM 787  O O   . HIS A 1 166  ? 192.549 181.289 193.727 1.00 5.49  ? 116 HIS A O   1 
ATOM 788  C CB  . HIS A 1 166  ? 192.981 184.517 194.288 1.00 12.91 ? 116 HIS A CB  1 
ATOM 789  C CG  . HIS A 1 166  ? 191.936 185.397 193.675 1.00 13.11 ? 116 HIS A CG  1 
ATOM 790  N ND1 . HIS A 1 166  ? 191.737 185.480 192.314 1.00 9.77  ? 116 HIS A ND1 1 
ATOM 791  C CD2 . HIS A 1 166  ? 191.021 186.220 194.240 1.00 18.41 ? 116 HIS A CD2 1 
ATOM 792  C CE1 . HIS A 1 166  ? 190.750 186.323 192.066 1.00 12.61 ? 116 HIS A CE1 1 
ATOM 793  N NE2 . HIS A 1 166  ? 190.298 186.786 193.217 1.00 16.68 ? 116 HIS A NE2 1 
ATOM 794  N N   . CYS A 1 167  ? 190.666 182.520 193.543 1.00 8.77  ? 117 CYS A N   1 
ATOM 795  C CA  . CYS A 1 167  ? 190.045 181.571 192.626 1.00 9.38  ? 117 CYS A CA  1 
ATOM 796  C C   . CYS A 1 167  ? 190.907 181.358 191.390 1.00 3.82  ? 117 CYS A C   1 
ATOM 797  O O   . CYS A 1 167  ? 191.049 180.228 190.910 1.00 4.09  ? 117 CYS A O   1 
ATOM 798  C CB  . CYS A 1 167  ? 188.651 182.057 192.230 1.00 10.66 ? 117 CYS A CB  1 
ATOM 799  S SG  . CYS A 1 167  ? 187.493 182.223 193.607 1.00 16.57 ? 117 CYS A SG  1 
ATOM 800  N N   . LEU A 1 168  ? 191.501 182.430 190.867 1.00 7.28  ? 118 LEU A N   1 
ATOM 801  C CA  . LEU A 1 168  ? 192.335 182.299 189.679 1.00 6.79  ? 118 LEU A CA  1 
ATOM 802  C C   . LEU A 1 168  ? 193.646 181.584 189.984 1.00 10.13 ? 118 LEU A C   1 
ATOM 803  O O   . LEU A 1 168  ? 194.162 180.857 189.128 1.00 16.55 ? 118 LEU A O   1 
ATOM 804  C CB  . LEU A 1 168  ? 192.591 183.677 189.071 1.00 4.75  ? 118 LEU A CB  1 
ATOM 805  C CG  . LEU A 1 168  ? 191.317 184.473 188.777 1.00 0.50  ? 118 LEU A CG  1 
ATOM 806  C CD1 . LEU A 1 168  ? 191.634 185.784 188.084 1.00 0.00  ? 118 LEU A CD1 1 
ATOM 807  C CD2 . LEU A 1 168  ? 190.346 183.650 187.948 1.00 0.32  ? 118 LEU A CD2 1 
ATOM 808  N N   . VAL A 1 169  ? 194.194 181.765 191.189 1.00 0.00  ? 119 VAL A N   1 
ATOM 809  C CA  . VAL A 1 169  ? 195.406 181.041 191.566 1.00 0.00  ? 119 VAL A CA  1 
ATOM 810  C C   . VAL A 1 169  ? 195.121 179.551 191.697 1.00 10.09 ? 119 VAL A C   1 
ATOM 811  O O   . VAL A 1 169  ? 195.918 178.711 191.260 1.00 11.64 ? 119 VAL A O   1 
ATOM 812  C CB  . VAL A 1 169  ? 195.995 181.611 192.868 1.00 1.20  ? 119 VAL A CB  1 
ATOM 813  C CG1 . VAL A 1 169  ? 197.292 180.902 193.208 1.00 8.29  ? 119 VAL A CG1 1 
ATOM 814  C CG2 . VAL A 1 169  ? 196.220 183.098 192.745 1.00 5.51  ? 119 VAL A CG2 1 
ATOM 815  N N   . ARG A 1 170  ? 193.998 179.196 192.322 1.00 14.73 ? 120 ARG A N   1 
ATOM 816  C CA  . ARG A 1 170  ? 193.631 177.790 192.437 1.00 7.82  ? 120 ARG A CA  1 
ATOM 817  C C   . ARG A 1 170  ? 193.341 177.180 191.073 1.00 3.25  ? 120 ARG A C   1 
ATOM 818  O O   . ARG A 1 170  ? 193.737 176.042 190.799 1.00 10.21 ? 120 ARG A O   1 
ATOM 819  C CB  . ARG A 1 170  ? 192.418 177.634 193.352 1.00 3.62  ? 120 ARG A CB  1 
ATOM 820  C CG  . ARG A 1 170  ? 191.786 176.257 193.296 1.00 0.00  ? 120 ARG A CG  1 
ATOM 821  C CD  . ARG A 1 170  ? 190.596 176.154 194.228 1.00 0.00  ? 120 ARG A CD  1 
ATOM 822  N NE  . ARG A 1 170  ? 190.134 174.778 194.363 1.00 15.22 ? 120 ARG A NE  1 
ATOM 823  C CZ  . ARG A 1 170  ? 190.679 173.880 195.172 1.00 18.08 ? 120 ARG A CZ  1 
ATOM 824  N NH1 . ARG A 1 170  ? 191.707 174.182 195.949 1.00 9.39  ? 120 ARG A NH1 1 
ATOM 825  N NH2 . ARG A 1 170  ? 190.178 172.649 195.206 1.00 13.46 ? 120 ARG A NH2 1 
ATOM 826  N N   . TRP A 1 171  ? 192.655 177.925 190.205 1.00 0.00  ? 121 TRP A N   1 
ATOM 827  C CA  . TRP A 1 171  ? 192.187 177.369 188.941 1.00 0.00  ? 121 TRP A CA  1 
ATOM 828  C C   . TRP A 1 171  ? 193.317 177.248 187.925 1.00 0.00  ? 121 TRP A C   1 
ATOM 829  O O   . TRP A 1 171  ? 193.563 176.165 187.386 1.00 16.21 ? 121 TRP A O   1 
ATOM 830  C CB  . TRP A 1 171  ? 191.047 178.226 188.386 1.00 0.00  ? 121 TRP A CB  1 
ATOM 831  C CG  . TRP A 1 171  ? 189.729 177.950 189.044 1.00 1.06  ? 121 TRP A CG  1 
ATOM 832  C CD1 . TRP A 1 171  ? 189.364 176.807 189.692 1.00 0.00  ? 121 TRP A CD1 1 
ATOM 833  C CD2 . TRP A 1 171  ? 188.604 178.832 189.122 1.00 8.01  ? 121 TRP A CD2 1 
ATOM 834  N NE1 . TRP A 1 171  ? 188.081 176.921 190.167 1.00 0.00  ? 121 TRP A NE1 1 
ATOM 835  C CE2 . TRP A 1 171  ? 187.592 178.156 189.830 1.00 3.27  ? 121 TRP A CE2 1 
ATOM 836  C CE3 . TRP A 1 171  ? 188.353 180.128 188.662 1.00 5.74  ? 121 TRP A CE3 1 
ATOM 837  C CZ2 . TRP A 1 171  ? 186.352 178.729 190.088 1.00 4.93  ? 121 TRP A CZ2 1 
ATOM 838  C CZ3 . TRP A 1 171  ? 187.120 180.694 188.920 1.00 0.00  ? 121 TRP A CZ3 1 
ATOM 839  C CH2 . TRP A 1 171  ? 186.136 179.996 189.625 1.00 1.45  ? 121 TRP A CH2 1 
ATOM 840  N N   . TYR A 1 172  ? 194.014 178.345 187.646 1.00 2.02  ? 122 TYR A N   1 
ATOM 841  C CA  . TYR A 1 172  ? 195.022 178.339 186.595 1.00 3.08  ? 122 TYR A CA  1 
ATOM 842  C C   . TYR A 1 172  ? 196.434 178.095 187.107 1.00 3.56  ? 122 TYR A C   1 
ATOM 843  O O   . TYR A 1 172  ? 197.365 178.054 186.299 1.00 2.23  ? 122 TYR A O   1 
ATOM 844  C CB  . TYR A 1 172  ? 194.982 179.656 185.817 1.00 10.96 ? 122 TYR A CB  1 
ATOM 845  C CG  . TYR A 1 172  ? 193.638 179.959 185.204 1.00 6.54  ? 122 TYR A CG  1 
ATOM 846  C CD1 . TYR A 1 172  ? 193.009 179.047 184.369 1.00 0.34  ? 122 TYR A CD1 1 
ATOM 847  C CD2 . TYR A 1 172  ? 192.998 181.160 185.458 1.00 6.48  ? 122 TYR A CD2 1 
ATOM 848  C CE1 . TYR A 1 172  ? 191.780 179.324 183.810 1.00 6.09  ? 122 TYR A CE1 1 
ATOM 849  C CE2 . TYR A 1 172  ? 191.773 181.445 184.904 1.00 8.58  ? 122 TYR A CE2 1 
ATOM 850  C CZ  . TYR A 1 172  ? 191.167 180.528 184.081 1.00 10.75 ? 122 TYR A CZ  1 
ATOM 851  O OH  . TYR A 1 172  ? 189.942 180.826 183.532 1.00 7.93  ? 122 TYR A OH  1 
ATOM 852  N N   . GLY A 1 173  ? 196.621 177.933 188.412 1.00 0.00  ? 123 GLY A N   1 
ATOM 853  C CA  . GLY A 1 173  ? 197.961 177.707 188.931 1.00 0.00  ? 123 GLY A CA  1 
ATOM 854  C C   . GLY A 1 173  ? 198.921 178.839 188.638 1.00 0.00  ? 123 GLY A C   1 
ATOM 855  O O   . GLY A 1 173  ? 200.069 178.592 188.246 1.00 0.00  ? 123 GLY A O   1 
ATOM 856  N N   . LEU A 1 174  ? 198.450 180.083 188.784 1.00 3.39  ? 124 LEU A N   1 
ATOM 857  C CA  . LEU A 1 174  ? 199.291 181.257 188.422 1.00 1.24  ? 124 LEU A CA  1 
ATOM 858  C C   . LEU A 1 174  ? 199.957 181.842 189.672 1.00 2.77  ? 124 LEU A C   1 
ATOM 859  O O   . LEU A 1 174  ? 199.601 181.415 190.787 1.00 0.21  ? 124 LEU A O   1 
ATOM 860  C CB  . LEU A 1 174  ? 198.406 182.304 187.739 1.00 0.24  ? 124 LEU A CB  1 
ATOM 861  C CG  . LEU A 1 174  ? 197.836 181.894 186.382 1.00 0.00  ? 124 LEU A CG  1 
ATOM 862  C CD1 . LEU A 1 174  ? 197.002 183.016 185.782 1.00 3.64  ? 124 LEU A CD1 1 
ATOM 863  C CD2 . LEU A 1 174  ? 198.948 181.487 185.428 1.00 0.00  ? 124 LEU A CD2 1 
ATOM 864  N N   . ARG A 1 175  ? 201.001 182.685 189.425 1.00 3.84  ? 125 ARG A N   1 
ATOM 865  C CA  . ARG A 1 175  ? 201.860 183.309 190.484 1.00 2.78  ? 125 ARG A CA  1 
ATOM 866  C C   . ARG A 1 175  ? 201.697 184.844 190.509 1.00 4.86  ? 125 ARG A C   1 
ATOM 867  O O   . ARG A 1 175  ? 201.767 185.403 191.621 1.00 6.71  ? 125 ARG A O   1 
ATOM 868  C CB  . ARG A 1 175  ? 203.346 182.898 190.295 1.00 2.63  ? 125 ARG A CB  1 
ATOM 869  C CG  . ARG A 1 175  ? 204.059 183.072 188.939 1.00 0.00  ? 125 ARG A CG  1 
ATOM 870  C CD  . ARG A 1 175  ? 205.566 183.153 189.089 1.00 5.14  ? 125 ARG A CD  1 
ATOM 871  N NE  . ARG A 1 175  ? 206.209 181.854 188.950 1.00 12.78 ? 125 ARG A NE  1 
ATOM 872  C CZ  . ARG A 1 175  ? 207.490 181.677 188.646 1.00 11.02 ? 125 ARG A CZ  1 
ATOM 873  N NH1 . ARG A 1 175  ? 207.930 180.478 188.310 1.00 12.22 ? 125 ARG A NH1 1 
ATOM 874  N NH2 . ARG A 1 175  ? 208.326 182.700 188.680 1.00 4.69  ? 125 ARG A NH2 1 
ATOM 875  N N   . GLU A 1 176  ? 201.503 185.510 189.362 1.00 6.10  ? 126 GLU A N   1 
ATOM 876  C CA  . GLU A 1 176  ? 201.341 186.980 189.203 1.00 0.00  ? 126 GLU A CA  1 
ATOM 877  C C   . GLU A 1 176  ? 200.217 187.233 188.195 1.00 0.00  ? 126 GLU A C   1 
ATOM 878  O O   . GLU A 1 176  ? 200.307 186.696 187.073 1.00 2.45  ? 126 GLU A O   1 
ATOM 879  C CB  . GLU A 1 176  ? 202.660 187.608 188.749 1.00 0.83  ? 126 GLU A CB  1 
ATOM 880  C CG  . GLU A 1 176  ? 202.492 188.957 188.075 1.00 1.43  ? 126 GLU A CG  1 
ATOM 881  C CD  . GLU A 1 176  ? 203.601 189.950 188.371 1.00 7.62  ? 126 GLU A CD  1 
ATOM 882  O OE1 . GLU A 1 176  ? 204.398 189.688 189.294 1.00 9.75  ? 126 GLU A OE1 1 
ATOM 883  O OE2 . GLU A 1 176  ? 203.663 190.988 187.682 1.00 9.29  ? 126 GLU A OE2 1 
ATOM 884  N N   . PHE A 1 177  ? 199.197 188.007 188.580 1.00 0.00  ? 127 PHE A N   1 
ATOM 885  C CA  . PHE A 1 177  ? 198.039 188.198 187.667 1.00 0.00  ? 127 PHE A CA  1 
ATOM 886  C C   . PHE A 1 177  ? 197.335 189.532 187.932 1.00 5.88  ? 127 PHE A C   1 
ATOM 887  O O   . PHE A 1 177  ? 197.087 189.863 189.109 1.00 16.37 ? 127 PHE A O   1 
ATOM 888  C CB  . PHE A 1 177  ? 197.069 187.015 187.771 1.00 0.00  ? 127 PHE A CB  1 
ATOM 889  C CG  . PHE A 1 177  ? 196.339 186.889 189.085 1.00 0.00  ? 127 PHE A CG  1 
ATOM 890  C CD1 . PHE A 1 177  ? 196.984 186.409 190.213 1.00 0.00  ? 127 PHE A CD1 1 
ATOM 891  C CD2 . PHE A 1 177  ? 195.003 187.241 189.191 1.00 2.08  ? 127 PHE A CD2 1 
ATOM 892  C CE1 . PHE A 1 177  ? 196.311 186.293 191.419 1.00 6.17  ? 127 PHE A CE1 1 
ATOM 893  C CE2 . PHE A 1 177  ? 194.331 187.124 190.397 1.00 0.00  ? 127 PHE A CE2 1 
ATOM 894  C CZ  . PHE A 1 177  ? 194.986 186.648 191.508 1.00 3.66  ? 127 PHE A CZ  1 
ATOM 895  N N   . VAL A 1 178  ? 197.042 190.280 186.866 1.00 0.00  ? 128 VAL A N   1 
ATOM 896  C CA  . VAL A 1 178  ? 196.302 191.532 186.978 1.00 0.00  ? 128 VAL A CA  1 
ATOM 897  C C   . VAL A 1 178  ? 194.838 191.241 186.684 1.00 0.00  ? 128 VAL A C   1 
ATOM 898  O O   . VAL A 1 178  ? 194.524 190.329 185.913 1.00 7.00  ? 128 VAL A O   1 
ATOM 899  C CB  . VAL A 1 178  ? 196.859 192.595 186.009 1.00 0.00  ? 128 VAL A CB  1 
ATOM 900  C CG1 . VAL A 1 178  ? 196.226 193.944 186.269 1.00 0.00  ? 128 VAL A CG1 1 
ATOM 901  C CG2 . VAL A 1 178  ? 198.369 192.686 186.123 1.00 0.00  ? 128 VAL A CG2 1 
ATOM 902  N N   . VAL A 1 179  ? 193.940 191.998 187.311 1.00 0.00  ? 129 VAL A N   1 
ATOM 903  C CA  . VAL A 1 179  ? 192.506 191.867 187.084 1.00 0.00  ? 129 VAL A CA  1 
ATOM 904  C C   . VAL A 1 179  ? 191.917 193.261 186.925 1.00 7.72  ? 129 VAL A C   1 
ATOM 905  O O   . VAL A 1 179  ? 192.224 194.161 187.712 1.00 17.30 ? 129 VAL A O   1 
ATOM 906  C CB  . VAL A 1 179  ? 191.810 191.113 188.234 1.00 0.00  ? 129 VAL A CB  1 
ATOM 907  C CG1 . VAL A 1 179  ? 190.308 191.092 188.024 1.00 0.00  ? 129 VAL A CG1 1 
ATOM 908  C CG2 . VAL A 1 179  ? 192.345 189.700 188.343 1.00 0.00  ? 129 VAL A CG2 1 
ATOM 909  N N   . ILE A 1 180  ? 191.095 193.418 185.878 1.00 8.65  ? 130 ILE A N   1 
ATOM 910  C CA  . ILE A 1 180  ? 190.352 194.692 185.658 1.00 1.81  ? 130 ILE A CA  1 
ATOM 911  C C   . ILE A 1 180  ? 188.893 194.371 185.984 1.00 5.99  ? 130 ILE A C   1 
ATOM 912  O O   . ILE A 1 180  ? 188.286 193.587 185.227 1.00 10.47 ? 130 ILE A O   1 
ATOM 913  C CB  . ILE A 1 180  ? 190.528 195.203 184.216 1.00 0.00  ? 130 ILE A CB  1 
ATOM 914  C CG1 . ILE A 1 180  ? 191.976 195.610 183.932 1.00 0.00  ? 130 ILE A CG1 1 
ATOM 915  C CG2 . ILE A 1 180  ? 189.555 196.335 183.924 1.00 5.33  ? 130 ILE A CG2 1 
ATOM 916  C CD1 . ILE A 1 180  ? 192.266 195.868 182.472 1.00 1.73  ? 130 ILE A CD1 1 
ATOM 917  N N   . ALA A 1 181  ? 188.356 194.938 187.062 1.00 9.62  ? 131 ALA A N   1 
ATOM 918  C CA  . ALA A 1 181  ? 187.021 194.609 187.530 1.00 10.91 ? 131 ALA A CA  1 
ATOM 919  C C   . ALA A 1 181  ? 186.176 195.870 187.630 1.00 18.83 ? 131 ALA A C   1 
ATOM 920  O O   . ALA A 1 181  ? 186.712 196.983 187.623 1.00 13.09 ? 131 ALA A O   1 
ATOM 921  C CB  . ALA A 1 181  ? 187.084 193.910 188.897 1.00 10.83 ? 131 ALA A CB  1 
ATOM 922  N N   . PRO A 1 182  ? 184.851 195.743 187.675 1.00 21.95 ? 132 PRO A N   1 
ATOM 923  C CA  . PRO A 1 182  ? 184.017 196.930 187.907 1.00 19.18 ? 132 PRO A CA  1 
ATOM 924  C C   . PRO A 1 182  ? 184.364 197.582 189.237 1.00 18.61 ? 132 PRO A C   1 
ATOM 925  O O   . PRO A 1 182  ? 184.329 196.940 190.290 1.00 17.52 ? 132 PRO A O   1 
ATOM 926  C CB  . PRO A 1 182  ? 182.592 196.367 187.902 1.00 15.02 ? 132 PRO A CB  1 
ATOM 927  C CG  . PRO A 1 182  ? 182.687 195.133 187.077 1.00 15.98 ? 132 PRO A CG  1 
ATOM 928  C CD  . PRO A 1 182  ? 184.035 194.552 187.378 1.00 14.39 ? 132 PRO A CD  1 
ATOM 929  N N   . ALA A 1 183  ? 184.709 198.868 189.182 1.00 20.16 ? 133 ALA A N   1 
ATOM 930  C CA  . ALA A 1 183  ? 185.083 199.588 190.392 1.00 21.71 ? 133 ALA A CA  1 
ATOM 931  C C   . ALA A 1 183  ? 183.903 199.663 191.351 1.00 19.56 ? 133 ALA A C   1 
ATOM 932  O O   . ALA A 1 183  ? 182.753 199.829 190.935 1.00 19.38 ? 133 ALA A O   1 
ATOM 933  C CB  . ALA A 1 183  ? 185.574 200.995 190.055 1.00 23.38 ? 133 ALA A CB  1 
ATOM 934  N N   . ALA A 1 184  ? 184.202 199.541 192.643 1.00 22.00 ? 134 ALA A N   1 
ATOM 935  C CA  . ALA A 1 184  ? 183.194 199.463 193.705 1.00 29.14 ? 134 ALA A CA  1 
ATOM 936  C C   . ALA A 1 184  ? 182.270 198.292 193.367 1.00 26.02 ? 134 ALA A C   1 
ATOM 937  O O   . ALA A 1 184  ? 182.765 197.198 193.063 1.00 22.41 ? 134 ALA A O   1 
ATOM 938  C CB  . ALA A 1 184  ? 182.514 200.815 193.871 1.00 25.81 ? 134 ALA A CB  1 
ATOM 939  N N   . HIS A 1 185  ? 180.955 198.470 193.389 1.00 23.94 ? 135 HIS A N   1 
ATOM 940  C CA  . HIS A 1 185  ? 180.019 197.388 193.108 1.00 23.87 ? 135 HIS A CA  1 
ATOM 941  C C   . HIS A 1 185  ? 178.818 197.997 192.393 1.00 25.40 ? 135 HIS A C   1 
ATOM 942  O O   . HIS A 1 185  ? 178.880 199.122 191.884 1.00 26.37 ? 135 HIS A O   1 
ATOM 943  C CB  . HIS A 1 185  ? 179.650 196.643 194.400 1.00 24.19 ? 135 HIS A CB  1 
ATOM 944  C CG  . HIS A 1 185  ? 180.816 195.982 195.069 1.00 25.20 ? 135 HIS A CG  1 
ATOM 945  N ND1 . HIS A 1 185  ? 181.337 196.425 196.266 1.00 28.88 ? 135 HIS A ND1 1 
ATOM 946  C CD2 . HIS A 1 185  ? 181.565 194.915 194.705 1.00 21.00 ? 135 HIS A CD2 1 
ATOM 947  C CE1 . HIS A 1 185  ? 182.355 195.658 196.611 1.00 26.59 ? 135 HIS A CE1 1 
ATOM 948  N NE2 . HIS A 1 185  ? 182.515 194.734 195.681 1.00 23.31 ? 135 HIS A NE2 1 
ATOM 949  N N   . SER A 1 186  ? 177.719 197.241 192.335 1.00 29.56 ? 136 SER A N   1 
ATOM 950  C CA  . SER A 1 186  ? 176.503 197.651 191.629 1.00 29.43 ? 136 SER A CA  1 
ATOM 951  C C   . SER A 1 186  ? 176.775 197.907 190.150 1.00 26.28 ? 136 SER A C   1 
ATOM 952  O O   . SER A 1 186  ? 176.083 198.698 189.505 1.00 22.17 ? 136 SER A O   1 
ATOM 953  C CB  . SER A 1 186  ? 175.863 198.882 192.279 1.00 28.34 ? 136 SER A CB  1 
ATOM 954  O OG  . SER A 1 186  ? 176.717 200.009 192.191 1.00 27.90 ? 136 SER A OG  1 
ATOM 955  N N   . ASP A 1 187  ? 177.811 197.247 189.621 1.00 25.72 ? 137 ASP A N   1 
ATOM 956  C CA  . ASP A 1 187  ? 178.181 197.422 188.190 1.00 27.16 ? 137 ASP A CA  1 
ATOM 957  C C   . ASP A 1 187  ? 178.508 196.049 187.595 1.00 26.26 ? 137 ASP A C   1 
ATOM 958  O O   . ASP A 1 187  ? 179.347 195.341 188.184 1.00 19.15 ? 137 ASP A O   1 
ATOM 959  C CB  . ASP A 1 187  ? 179.356 198.390 188.035 1.00 26.13 ? 137 ASP A CB  1 
ATOM 960  C CG  . ASP A 1 187  ? 178.957 199.849 188.164 1.00 27.50 ? 137 ASP A CG  1 
ATOM 961  O OD1 . ASP A 1 187  ? 178.248 200.342 187.265 1.00 31.68 ? 137 ASP A OD1 1 
ATOM 962  O OD2 . ASP A 1 187  ? 179.358 200.479 189.162 1.00 27.80 ? 137 ASP A OD2 1 
ATOM 963  N N   . ALA A 1 188  ? 177.867 195.688 186.478 1.00 21.81 ? 138 ALA A N   1 
ATOM 964  C CA  . ALA A 1 188  ? 178.080 194.349 185.881 1.00 17.54 ? 138 ALA A CA  1 
ATOM 965  C C   . ALA A 1 188  ? 178.003 194.427 184.353 1.00 13.49 ? 138 ALA A C   1 
ATOM 966  O O   . ALA A 1 188  ? 176.984 194.930 183.840 1.00 16.52 ? 138 ALA A O   1 
ATOM 967  C CB  . ALA A 1 188  ? 177.060 193.382 186.432 1.00 17.49 ? 138 ALA A CB  1 
ATOM 968  N N   . VAL A 1 189  ? 179.034 193.936 183.659 1.00 10.05 ? 139 VAL A N   1 
ATOM 969  C CA  . VAL A 1 189  ? 179.010 193.896 182.166 1.00 10.68 ? 139 VAL A CA  1 
ATOM 970  C C   . VAL A 1 189  ? 178.143 192.707 181.747 1.00 8.49  ? 139 VAL A C   1 
ATOM 971  O O   . VAL A 1 189  ? 178.509 191.569 182.099 1.00 16.13 ? 139 VAL A O   1 
ATOM 972  C CB  . VAL A 1 189  ? 180.434 193.784 181.591 1.00 5.13  ? 139 VAL A CB  1 
ATOM 973  C CG1 . VAL A 1 189  ? 180.472 194.107 180.107 1.00 12.60 ? 139 VAL A CG1 1 
ATOM 974  C CG2 . VAL A 1 189  ? 181.422 194.652 182.356 1.00 5.22  ? 139 VAL A CG2 1 
ATOM 975  N N   . LEU A 1 190  ? 177.041 192.952 181.029 1.00 9.22  ? 140 LEU A N   1 
ATOM 976  C CA  . LEU A 1 190  ? 176.139 191.858 180.696 1.00 9.73  ? 140 LEU A CA  1 
ATOM 977  C C   . LEU A 1 190  ? 176.086 191.557 179.206 1.00 11.23 ? 140 LEU A C   1 
ATOM 978  O O   . LEU A 1 190  ? 176.224 190.397 178.808 1.00 5.25  ? 140 LEU A O   1 
ATOM 979  C CB  . LEU A 1 190  ? 174.729 192.172 181.217 1.00 9.42  ? 140 LEU A CB  1 
ATOM 980  C CG  . LEU A 1 190  ? 174.607 192.355 182.731 1.00 8.01  ? 140 LEU A CG  1 
ATOM 981  C CD1 . LEU A 1 190  ? 173.180 192.701 183.117 1.00 10.60 ? 140 LEU A CD1 1 
ATOM 982  C CD2 . LEU A 1 190  ? 175.071 191.109 183.462 1.00 8.76  ? 140 LEU A CD2 1 
ATOM 983  N N   . SER A 1 191  ? 175.883 192.571 178.369 1.00 18.81 ? 141 SER A N   1 
ATOM 984  C CA  . SER A 1 191  ? 175.766 192.344 176.934 1.00 17.60 ? 141 SER A CA  1 
ATOM 985  C C   . SER A 1 191  ? 177.107 191.933 176.337 1.00 17.07 ? 141 SER A C   1 
ATOM 986  O O   . SER A 1 191  ? 178.169 192.376 176.783 1.00 10.79 ? 141 SER A O   1 
ATOM 987  C CB  . SER A 1 191  ? 175.238 193.597 176.238 1.00 11.96 ? 141 SER A CB  1 
ATOM 988  O OG  . SER A 1 191  ? 176.090 194.704 176.462 1.00 7.79  ? 141 SER A OG  1 
ATOM 989  N N   . GLU A 1 192  ? 177.046 191.083 175.307 1.00 13.64 ? 142 GLU A N   1 
ATOM 990  C CA  . GLU A 1 192  ? 178.254 190.505 174.727 1.00 10.16 ? 142 GLU A CA  1 
ATOM 991  C C   . GLU A 1 192  ? 179.130 191.558 174.058 1.00 12.24 ? 142 GLU A C   1 
ATOM 992  O O   . GLU A 1 192  ? 180.359 191.413 174.024 1.00 6.07  ? 142 GLU A O   1 
ATOM 993  C CB  . GLU A 1 192  ? 177.871 189.417 173.724 1.00 5.55  ? 142 GLU A CB  1 
ATOM 994  C CG  . GLU A 1 192  ? 178.982 188.438 173.395 1.00 9.95  ? 142 GLU A CG  1 
ATOM 995  C CD  . GLU A 1 192  ? 178.477 187.014 173.267 1.00 16.42 ? 142 GLU A CD  1 
ATOM 996  O OE1 . GLU A 1 192  ? 178.376 186.322 174.301 1.00 15.66 ? 142 GLU A OE1 1 
ATOM 997  O OE2 . GLU A 1 192  ? 178.173 186.587 172.133 1.00 10.53 ? 142 GLU A OE2 1 
ATOM 998  N N   . SER A 1 193  ? 178.521 192.618 173.520 1.00 14.59 ? 143 SER A N   1 
ATOM 999  C CA  . SER A 1 193  ? 179.297 193.648 172.837 1.00 6.40  ? 143 SER A CA  1 
ATOM 1000 C C   . SER A 1 193  ? 180.258 194.349 173.791 1.00 13.52 ? 143 SER A C   1 
ATOM 1001 O O   . SER A 1 193  ? 181.406 194.624 173.430 1.00 10.66 ? 143 SER A O   1 
ATOM 1002 C CB  . SER A 1 193  ? 178.361 194.658 172.173 1.00 1.69  ? 143 SER A CB  1 
ATOM 1003 O OG  . SER A 1 193  ? 177.442 195.195 173.106 1.00 4.41  ? 143 SER A OG  1 
ATOM 1004 N N   . LYS A 1 194  ? 179.811 194.641 175.015 1.00 14.63 ? 144 LYS A N   1 
ATOM 1005 C CA  . LYS A 1 194  ? 180.675 195.335 175.967 1.00 5.94  ? 144 LYS A CA  1 
ATOM 1006 C C   . LYS A 1 194  ? 181.825 194.448 176.434 1.00 5.57  ? 144 LYS A C   1 
ATOM 1007 O O   . LYS A 1 194  ? 182.968 194.913 176.546 1.00 5.84  ? 144 LYS A O   1 
ATOM 1008 C CB  . LYS A 1 194  ? 179.855 195.827 177.157 1.00 6.68  ? 144 LYS A CB  1 
ATOM 1009 C CG  . LYS A 1 194  ? 178.587 196.563 176.765 1.00 10.80 ? 144 LYS A CG  1 
ATOM 1010 C CD  . LYS A 1 194  ? 178.674 198.043 177.099 1.00 10.40 ? 144 LYS A CD  1 
ATOM 1011 C CE  . LYS A 1 194  ? 177.442 198.791 176.617 1.00 13.04 ? 144 LYS A CE  1 
ATOM 1012 N NZ  . LYS A 1 194  ? 177.471 200.226 177.010 1.00 11.89 ? 144 LYS A NZ  1 
ATOM 1013 N N   . CYS A 1 195  ? 181.547 193.171 176.709 1.00 6.96  ? 145 CYS A N   1 
ATOM 1014 C CA  . CYS A 1 195  ? 182.621 192.251 177.073 1.00 6.90  ? 145 CYS A CA  1 
ATOM 1015 C C   . CYS A 1 195  ? 183.631 192.123 175.942 1.00 16.40 ? 145 CYS A C   1 
ATOM 1016 O O   . CYS A 1 195  ? 184.844 192.090 176.181 1.00 9.50  ? 145 CYS A O   1 
ATOM 1017 C CB  . CYS A 1 195  ? 182.054 190.878 177.432 1.00 2.21  ? 145 CYS A CB  1 
ATOM 1018 S SG  . CYS A 1 195  ? 180.465 190.902 178.279 1.00 18.21 ? 145 CYS A SG  1 
ATOM 1019 N N   . ASN A 1 196  ? 183.145 192.056 174.700 1.00 20.95 ? 146 ASN A N   1 
ATOM 1020 C CA  . ASN A 1 196  ? 184.043 191.927 173.558 1.00 2.90  ? 146 ASN A CA  1 
ATOM 1021 C C   . ASN A 1 196  ? 184.859 193.197 173.343 1.00 4.70  ? 146 ASN A C   1 
ATOM 1022 O O   . ASN A 1 196  ? 186.028 193.125 172.952 1.00 2.26  ? 146 ASN A O   1 
ATOM 1023 C CB  . ASN A 1 196  ? 183.237 191.568 172.313 1.00 0.00  ? 146 ASN A CB  1 
ATOM 1024 C CG  . ASN A 1 196  ? 182.773 190.127 172.326 1.00 7.80  ? 146 ASN A CG  1 
ATOM 1025 O OD1 . ASN A 1 196  ? 183.495 189.235 172.771 1.00 12.12 ? 146 ASN A OD1 1 
ATOM 1026 N ND2 . ASN A 1 196  ? 181.554 189.893 171.860 1.00 7.67  ? 146 ASN A ND2 1 
ATOM 1027 N N   . LEU A 1 197  ? 184.266 194.367 173.601 1.00 8.11  ? 147 LEU A N   1 
ATOM 1028 C CA  . LEU A 1 197  ? 185.029 195.613 173.555 1.00 12.28 ? 147 LEU A CA  1 
ATOM 1029 C C   . LEU A 1 197  ? 186.136 195.620 174.601 1.00 6.27  ? 147 LEU A C   1 
ATOM 1030 O O   . LEU A 1 197  ? 187.278 196.006 174.313 1.00 12.93 ? 147 LEU A O   1 
ATOM 1031 C CB  . LEU A 1 197  ? 184.099 196.808 173.767 1.00 9.62  ? 147 LEU A CB  1 
ATOM 1032 C CG  . LEU A 1 197  ? 183.664 197.592 172.530 1.00 5.47  ? 147 LEU A CG  1 
ATOM 1033 C CD1 . LEU A 1 197  ? 182.906 196.692 171.585 1.00 4.92  ? 147 LEU A CD1 1 
ATOM 1034 C CD2 . LEU A 1 197  ? 182.824 198.798 172.918 1.00 5.67  ? 147 LEU A CD2 1 
ATOM 1035 N N   . LEU A 1 198  ? 185.814 195.195 175.824 1.00 0.00  ? 148 LEU A N   1 
ATOM 1036 C CA  . LEU A 1 198  ? 186.827 195.139 176.871 1.00 3.67  ? 148 LEU A CA  1 
ATOM 1037 C C   . LEU A 1 198  ? 187.952 194.181 176.496 1.00 5.61  ? 148 LEU A C   1 
ATOM 1038 O O   . LEU A 1 198  ? 189.136 194.503 176.661 1.00 10.08 ? 148 LEU A O   1 
ATOM 1039 C CB  . LEU A 1 198  ? 186.183 194.726 178.196 1.00 17.02 ? 148 LEU A CB  1 
ATOM 1040 C CG  . LEU A 1 198  ? 185.532 195.829 179.037 1.00 12.57 ? 148 LEU A CG  1 
ATOM 1041 C CD1 . LEU A 1 198  ? 184.864 195.245 180.272 1.00 0.00  ? 148 LEU A CD1 1 
ATOM 1042 C CD2 . LEU A 1 198  ? 186.551 196.870 179.435 1.00 7.68  ? 148 LEU A CD2 1 
ATOM 1043 N N   . LEU A 1 199  ? 187.603 193.002 175.976 1.00 0.00  ? 149 LEU A N   1 
ATOM 1044 C CA  . LEU A 1 199  ? 188.623 192.020 175.620 1.00 0.00  ? 149 LEU A CA  1 
ATOM 1045 C C   . LEU A 1 199  ? 189.468 192.495 174.443 1.00 5.86  ? 149 LEU A C   1 
ATOM 1046 O O   . LEU A 1 199  ? 190.676 192.235 174.396 1.00 5.18  ? 149 LEU A O   1 
ATOM 1047 C CB  . LEU A 1 199  ? 187.971 190.673 175.312 1.00 0.99  ? 149 LEU A CB  1 
ATOM 1048 C CG  . LEU A 1 199  ? 188.899 189.459 175.340 1.00 0.00  ? 149 LEU A CG  1 
ATOM 1049 C CD1 . LEU A 1 199  ? 189.631 189.393 176.662 1.00 1.24  ? 149 LEU A CD1 1 
ATOM 1050 C CD2 . LEU A 1 199  ? 188.111 188.185 175.107 1.00 2.80  ? 149 LEU A CD2 1 
ATOM 1051 N N   . SER A 1 200  ? 188.854 193.190 173.483 1.00 7.01  ? 150 SER A N   1 
ATOM 1052 C CA  . SER A 1 200  ? 189.614 193.766 172.380 1.00 0.00  ? 150 SER A CA  1 
ATOM 1053 C C   . SER A 1 200  ? 190.615 194.793 172.888 1.00 0.00  ? 150 SER A C   1 
ATOM 1054 O O   . SER A 1 200  ? 191.773 194.814 172.453 1.00 0.00  ? 150 SER A O   1 
ATOM 1055 C CB  . SER A 1 200  ? 188.662 194.409 171.377 1.00 0.00  ? 150 SER A CB  1 
ATOM 1056 O OG  . SER A 1 200  ? 187.590 193.539 171.067 1.00 0.00  ? 150 SER A OG  1 
ATOM 1057 N N   . SER A 1 201  ? 190.181 195.652 173.815 1.00 16.31 ? 151 SER A N   1 
ATOM 1058 C CA  . SER A 1 201  ? 191.089 196.636 174.395 1.00 7.72  ? 151 SER A CA  1 
ATOM 1059 C C   . SER A 1 201  ? 192.235 195.958 175.134 1.00 5.10  ? 151 SER A C   1 
ATOM 1060 O O   . SER A 1 201  ? 193.391 196.383 175.029 1.00 0.00  ? 151 SER A O   1 
ATOM 1061 C CB  . SER A 1 201  ? 190.318 197.566 175.329 1.00 6.32  ? 151 SER A CB  1 
ATOM 1062 O OG  . SER A 1 201  ? 189.113 197.997 174.720 1.00 10.52 ? 151 SER A OG  1 
ATOM 1063 N N   . VAL A 1 202  ? 191.931 194.889 175.874 1.00 0.00  ? 152 VAL A N   1 
ATOM 1064 C CA  . VAL A 1 202  ? 192.973 194.135 176.570 1.00 8.78  ? 152 VAL A CA  1 
ATOM 1065 C C   . VAL A 1 202  ? 193.977 193.565 175.572 1.00 9.84  ? 152 VAL A C   1 
ATOM 1066 O O   . VAL A 1 202  ? 195.196 193.674 175.756 1.00 9.10  ? 152 VAL A O   1 
ATOM 1067 C CB  . VAL A 1 202  ? 192.337 193.026 177.431 1.00 6.84  ? 152 VAL A CB  1 
ATOM 1068 C CG1 . VAL A 1 202  ? 193.342 191.935 177.738 1.00 1.28  ? 152 VAL A CG1 1 
ATOM 1069 C CG2 . VAL A 1 202  ? 191.772 193.606 178.716 1.00 4.72  ? 152 VAL A CG2 1 
ATOM 1070 N N   . SER A 1 203  ? 193.477 192.949 174.498 1.00 4.62  ? 153 SER A N   1 
ATOM 1071 C CA  . SER A 1 203  ? 194.363 192.319 173.525 1.00 0.00  ? 153 SER A CA  1 
ATOM 1072 C C   . SER A 1 203  ? 195.266 193.348 172.855 1.00 0.00  ? 153 SER A C   1 
ATOM 1073 O O   . SER A 1 203  ? 196.471 193.117 172.691 1.00 0.00  ? 153 SER A O   1 
ATOM 1074 C CB  . SER A 1 203  ? 193.539 191.560 172.487 1.00 0.51  ? 153 SER A CB  1 
ATOM 1075 O OG  . SER A 1 203  ? 192.844 190.480 173.082 1.00 8.21  ? 153 SER A OG  1 
ATOM 1076 N N   . ILE A 1 204  ? 194.705 194.503 172.487 1.00 3.51  ? 154 ILE A N   1 
ATOM 1077 C CA  . ILE A 1 204  ? 195.513 195.558 171.881 1.00 1.60  ? 154 ILE A CA  1 
ATOM 1078 C C   . ILE A 1 204  ? 196.536 196.089 172.879 1.00 9.34  ? 154 ILE A C   1 
ATOM 1079 O O   . ILE A 1 204  ? 197.675 196.401 172.513 1.00 8.39  ? 154 ILE A O   1 
ATOM 1080 C CB  . ILE A 1 204  ? 194.611 196.681 171.338 1.00 0.00  ? 154 ILE A CB  1 
ATOM 1081 C CG1 . ILE A 1 204  ? 193.628 196.117 170.317 1.00 0.00  ? 154 ILE A CG1 1 
ATOM 1082 C CG2 . ILE A 1 204  ? 195.445 197.763 170.683 1.00 0.00  ? 154 ILE A CG2 1 
ATOM 1083 C CD1 . ILE A 1 204  ? 192.359 196.918 170.190 1.00 2.09  ? 154 ILE A CD1 1 
ATOM 1084 N N   . ALA A 1 205  ? 196.121 196.200 174.144 1.00 5.89  ? 155 ALA A N   1 
ATOM 1085 C CA  . ALA A 1 205  ? 197.047 196.677 175.195 1.00 0.00  ? 155 ALA A CA  1 
ATOM 1086 C C   . ALA A 1 205  ? 198.269 195.755 175.240 1.00 0.00  ? 155 ALA A C   1 
ATOM 1087 O O   . ALA A 1 205  ? 199.394 196.256 175.051 1.00 0.00  ? 155 ALA A O   1 
ATOM 1088 C CB  . ALA A 1 205  ? 196.342 196.722 176.527 1.00 0.00  ? 155 ALA A CB  1 
ATOM 1089 N N   . LEU A 1 206  ? 198.050 194.457 175.469 1.00 5.07  ? 156 LEU A N   1 
ATOM 1090 C CA  . LEU A 1 206  ? 199.174 193.527 175.575 1.00 2.68  ? 156 LEU A CA  1 
ATOM 1091 C C   . LEU A 1 206  ? 199.988 193.480 174.287 1.00 8.21  ? 156 LEU A C   1 
ATOM 1092 O O   . LEU A 1 206  ? 201.213 193.322 174.330 1.00 12.39 ? 156 LEU A O   1 
ATOM 1093 C CB  . LEU A 1 206  ? 198.711 192.123 175.969 1.00 0.00  ? 156 LEU A CB  1 
ATOM 1094 C CG  . LEU A 1 206  ? 198.263 191.872 177.413 1.00 0.00  ? 156 LEU A CG  1 
ATOM 1095 C CD1 . LEU A 1 206  ? 196.855 192.291 177.690 1.00 0.57  ? 156 LEU A CD1 1 
ATOM 1096 C CD2 . LEU A 1 206  ? 198.438 190.408 177.761 1.00 3.56  ? 156 LEU A CD2 1 
ATOM 1097 N N   . GLY A 1 207  ? 199.337 193.612 173.129 1.00 4.31  ? 157 GLY A N   1 
ATOM 1098 C CA  . GLY A 1 207  ? 200.092 193.650 171.888 1.00 0.00  ? 157 GLY A CA  1 
ATOM 1099 C C   . GLY A 1 207  ? 200.991 194.869 171.789 1.00 5.87  ? 157 GLY A C   1 
ATOM 1100 O O   . GLY A 1 207  ? 202.105 194.791 171.263 1.00 2.74  ? 157 GLY A O   1 
ATOM 1101 N N   . ASN A 1 208  ? 200.525 196.007 172.305 1.00 9.75  ? 158 ASN A N   1 
ATOM 1102 C CA  . ASN A 1 208  ? 201.270 197.254 172.169 1.00 7.25  ? 158 ASN A CA  1 
ATOM 1103 C C   . ASN A 1 208  ? 202.419 197.330 173.169 1.00 5.08  ? 158 ASN A C   1 
ATOM 1104 O O   . ASN A 1 208  ? 203.582 197.498 172.782 1.00 10.78 ? 158 ASN A O   1 
ATOM 1105 C CB  . ASN A 1 208  ? 200.324 198.442 172.341 1.00 5.29  ? 158 ASN A CB  1 
ATOM 1106 C CG  . ASN A 1 208  ? 199.588 198.785 171.064 1.00 8.94  ? 158 ASN A CG  1 
ATOM 1107 O OD1 . ASN A 1 208  ? 199.026 197.910 170.404 1.00 3.57  ? 158 ASN A OD1 1 
ATOM 1108 N ND2 . ASN A 1 208  ? 199.587 200.064 170.706 1.00 10.37 ? 158 ASN A ND2 1 
ATOM 1109 N N   . THR A 1 209  ? 202.112 197.223 174.466 1.00 0.00  ? 159 THR A N   1 
ATOM 1110 C CA  . THR A 1 209  ? 203.161 197.377 175.472 1.00 3.89  ? 159 THR A CA  1 
ATOM 1111 C C   . THR A 1 209  ? 204.203 196.272 175.368 1.00 6.80  ? 159 THR A C   1 
ATOM 1112 O O   . THR A 1 209  ? 205.409 196.538 175.406 1.00 6.65  ? 159 THR A O   1 
ATOM 1113 C CB  . THR A 1 209  ? 202.564 197.389 176.877 1.00 7.95  ? 159 THR A CB  1 
ATOM 1114 O OG1 . THR A 1 209  ? 202.339 196.041 177.308 1.00 8.86  ? 159 THR A OG1 1 
ATOM 1115 C CG2 . THR A 1 209  ? 201.258 198.149 176.898 1.00 10.99 ? 159 THR A CG2 1 
ATOM 1116 N N   . GLY A 1 210  ? 203.757 195.030 175.220 1.00 8.31  ? 160 GLY A N   1 
ATOM 1117 C CA  . GLY A 1 210  ? 204.632 193.885 175.323 1.00 7.60  ? 160 GLY A CA  1 
ATOM 1118 C C   . GLY A 1 210  ? 204.569 193.154 176.644 1.00 2.66  ? 160 GLY A C   1 
ATOM 1119 O O   . GLY A 1 210  ? 205.393 192.262 176.876 1.00 0.00  ? 160 GLY A O   1 
ATOM 1120 N N   . CYS A 1 211  ? 203.630 193.508 177.518 1.00 0.00  ? 161 CYS A N   1 
ATOM 1121 C CA  . CYS A 1 211  ? 203.496 192.828 178.797 1.00 1.27  ? 161 CYS A CA  1 
ATOM 1122 C C   . CYS A 1 211  ? 203.086 191.377 178.586 1.00 8.09  ? 161 CYS A C   1 
ATOM 1123 O O   . CYS A 1 211  ? 202.236 191.071 177.745 1.00 7.43  ? 161 CYS A O   1 
ATOM 1124 C CB  . CYS A 1 211  ? 202.466 193.548 179.668 1.00 1.56  ? 161 CYS A CB  1 
ATOM 1125 S SG  . CYS A 1 211  ? 201.999 192.679 181.180 1.00 5.06  ? 161 CYS A SG  1 
ATOM 1126 N N   . GLN A 1 212  ? 203.701 190.479 179.356 1.00 9.90  ? 162 GLN A N   1 
ATOM 1127 C CA  . GLN A 1 212  ? 203.410 189.056 179.275 1.00 0.00  ? 162 GLN A CA  1 
ATOM 1128 C C   . GLN A 1 212  ? 202.589 188.540 180.445 1.00 2.00  ? 162 GLN A C   1 
ATOM 1129 O O   . GLN A 1 212  ? 202.145 187.389 180.405 1.00 5.08  ? 162 GLN A O   1 
ATOM 1130 C CB  . GLN A 1 212  ? 204.714 188.251 179.184 1.00 0.00  ? 162 GLN A CB  1 
ATOM 1131 C CG  . GLN A 1 212  ? 205.675 188.755 178.129 1.00 0.79  ? 162 GLN A CG  1 
ATOM 1132 C CD  . GLN A 1 212  ? 206.809 187.789 177.873 1.00 6.87  ? 162 GLN A CD  1 
ATOM 1133 O OE1 . GLN A 1 212  ? 206.787 186.652 178.342 1.00 9.36  ? 162 GLN A OE1 1 
ATOM 1134 N NE2 . GLN A 1 212  ? 207.810 188.236 177.126 1.00 5.85  ? 162 GLN A NE2 1 
ATOM 1135 N N   . VAL A 1 213  ? 202.386 189.345 181.478 1.00 0.00  ? 163 VAL A N   1 
ATOM 1136 C CA  . VAL A 1 213  ? 201.566 188.921 182.617 1.00 1.20  ? 163 VAL A CA  1 
ATOM 1137 C C   . VAL A 1 213  ? 200.129 188.721 182.149 1.00 2.93  ? 163 VAL A C   1 
ATOM 1138 O O   . VAL A 1 213  ? 199.597 189.572 181.415 1.00 7.78  ? 163 VAL A O   1 
ATOM 1139 C CB  . VAL A 1 213  ? 201.641 189.957 183.739 1.00 1.03  ? 163 VAL A CB  1 
ATOM 1140 C CG1 . VAL A 1 213  ? 200.614 189.658 184.813 1.00 1.64  ? 163 VAL A CG1 1 
ATOM 1141 C CG2 . VAL A 1 213  ? 203.036 189.987 184.333 1.00 1.58  ? 163 VAL A CG2 1 
ATOM 1142 N N   . PRO A 1 214  ? 199.474 187.620 182.514 1.00 0.00  ? 164 PRO A N   1 
ATOM 1143 C CA  . PRO A 1 214  ? 198.080 187.423 182.102 1.00 0.00  ? 164 PRO A CA  1 
ATOM 1144 C C   . PRO A 1 214  ? 197.186 188.548 182.600 1.00 0.00  ? 164 PRO A C   1 
ATOM 1145 O O   . PRO A 1 214  ? 197.315 189.011 183.735 1.00 0.20  ? 164 PRO A O   1 
ATOM 1146 C CB  . PRO A 1 214  ? 197.708 186.087 182.752 1.00 0.00  ? 164 PRO A CB  1 
ATOM 1147 C CG  . PRO A 1 214  ? 199.001 185.378 182.899 1.00 0.00  ? 164 PRO A CG  1 
ATOM 1148 C CD  . PRO A 1 214  ? 200.025 186.433 183.186 1.00 0.00  ? 164 PRO A CD  1 
ATOM 1149 N N   . LEU A 1 215  ? 196.270 188.982 181.740 1.00 1.47  ? 165 LEU A N   1 
ATOM 1150 C CA  . LEU A 1 215  ? 195.268 189.967 182.117 1.00 0.00  ? 165 LEU A CA  1 
ATOM 1151 C C   . LEU A 1 215  ? 193.886 189.338 182.074 1.00 1.01  ? 165 LEU A C   1 
ATOM 1152 O O   . LEU A 1 215  ? 193.605 188.475 181.238 1.00 16.13 ? 165 LEU A O   1 
ATOM 1153 C CB  . LEU A 1 215  ? 195.298 191.188 181.201 1.00 0.00  ? 165 LEU A CB  1 
ATOM 1154 C CG  . LEU A 1 215  ? 195.983 192.410 181.800 1.00 0.00  ? 165 LEU A CG  1 
ATOM 1155 C CD1 . LEU A 1 215  ? 197.492 192.252 181.718 1.00 0.00  ? 165 LEU A CD1 1 
ATOM 1156 C CD2 . LEU A 1 215  ? 195.522 193.674 181.102 1.00 1.00  ? 165 LEU A CD2 1 
ATOM 1157 N N   . PHE A 1 216  ? 193.023 189.787 182.984 1.00 0.68  ? 166 PHE A N   1 
ATOM 1158 C CA  . PHE A 1 216  ? 191.692 189.227 183.150 1.00 0.00  ? 166 PHE A CA  1 
ATOM 1159 C C   . PHE A 1 216  ? 190.660 190.343 183.193 1.00 2.65  ? 166 PHE A C   1 
ATOM 1160 O O   . PHE A 1 216  ? 190.955 191.473 183.586 1.00 0.00  ? 166 PHE A O   1 
ATOM 1161 C CB  . PHE A 1 216  ? 191.598 188.384 184.423 1.00 0.00  ? 166 PHE A CB  1 
ATOM 1162 C CG  . PHE A 1 216  ? 192.322 187.074 184.337 1.00 0.00  ? 166 PHE A CG  1 
ATOM 1163 C CD1 . PHE A 1 216  ? 193.702 187.020 184.435 1.00 1.43  ? 166 PHE A CD1 1 
ATOM 1164 C CD2 . PHE A 1 216  ? 191.621 185.894 184.164 1.00 0.00  ? 166 PHE A CD2 1 
ATOM 1165 C CE1 . PHE A 1 216  ? 194.368 185.816 184.358 1.00 0.00  ? 166 PHE A CE1 1 
ATOM 1166 C CE2 . PHE A 1 216  ? 192.281 184.690 184.087 1.00 2.80  ? 166 PHE A CE2 1 
ATOM 1167 C CZ  . PHE A 1 216  ? 193.657 184.650 184.185 1.00 3.18  ? 166 PHE A CZ  1 
ATOM 1168 N N   . VAL A 1 217  ? 189.441 190.010 182.780 1.00 0.00  ? 167 VAL A N   1 
ATOM 1169 C CA  . VAL A 1 217  ? 188.329 190.948 182.744 1.00 0.00  ? 167 VAL A CA  1 
ATOM 1170 C C   . VAL A 1 217  ? 187.120 190.247 183.343 1.00 5.29  ? 167 VAL A C   1 
ATOM 1171 O O   . VAL A 1 217  ? 186.750 189.153 182.895 1.00 19.29 ? 167 VAL A O   1 
ATOM 1172 C CB  . VAL A 1 217  ? 188.030 191.424 181.312 1.00 0.00  ? 167 VAL A CB  1 
ATOM 1173 C CG1 . VAL A 1 217  ? 186.603 191.934 181.197 1.00 0.49  ? 167 VAL A CG1 1 
ATOM 1174 C CG2 . VAL A 1 217  ? 189.027 192.492 180.884 1.00 5.21  ? 167 VAL A CG2 1 
ATOM 1175 N N   . GLN A 1 218  ? 186.521 190.864 184.362 1.00 0.00  ? 168 GLN A N   1 
ATOM 1176 C CA  . GLN A 1 218  ? 185.328 190.309 184.985 1.00 2.44  ? 168 GLN A CA  1 
ATOM 1177 C C   . GLN A 1 218  ? 184.113 190.552 184.103 1.00 6.74  ? 168 GLN A C   1 
ATOM 1178 O O   . GLN A 1 218  ? 183.897 191.666 183.618 1.00 7.60  ? 168 GLN A O   1 
ATOM 1179 C CB  . GLN A 1 218  ? 185.105 190.940 186.358 1.00 5.91  ? 168 GLN A CB  1 
ATOM 1180 C CG  . GLN A 1 218  ? 186.155 190.602 187.397 1.00 4.29  ? 168 GLN A CG  1 
ATOM 1181 C CD  . GLN A 1 218  ? 185.539 190.149 188.704 1.00 3.25  ? 168 GLN A CD  1 
ATOM 1182 O OE1 . GLN A 1 218  ? 184.444 189.589 188.725 1.00 7.15  ? 168 GLN A OE1 1 
ATOM 1183 N NE2 . GLN A 1 218  ? 186.238 190.395 189.804 1.00 3.20  ? 168 GLN A NE2 1 
ATOM 1184 N N   . ILE A 1 219  ? 183.313 189.500 183.905 1.00 0.00  ? 169 ILE A N   1 
ATOM 1185 C CA  . ILE A 1 219  ? 182.086 189.620 183.063 1.00 0.00  ? 169 ILE A CA  1 
ATOM 1186 C C   . ILE A 1 219  ? 180.892 189.080 183.857 1.00 3.55  ? 169 ILE A C   1 
ATOM 1187 O O   . ILE A 1 219  ? 181.097 188.673 185.019 1.00 5.57  ? 169 ILE A O   1 
ATOM 1188 C CB  . ILE A 1 219  ? 182.270 188.872 181.728 1.00 0.00  ? 169 ILE A CB  1 
ATOM 1189 C CG1 . ILE A 1 219  ? 182.798 187.451 181.944 1.00 2.91  ? 169 ILE A CG1 1 
ATOM 1190 C CG2 . ILE A 1 219  ? 183.162 189.664 180.785 1.00 0.00  ? 169 ILE A CG2 1 
ATOM 1191 C CD1 . ILE A 1 219  ? 182.170 186.419 181.038 1.00 1.40  ? 169 ILE A CD1 1 
ATOM 1192 N N   . HIS A 1 220  ? 179.698 189.085 183.254 1.00 4.34  ? 170 HIS A N   1 
ATOM 1193 C CA  . HIS A 1 220  ? 178.475 188.562 183.928 1.00 0.00  ? 170 HIS A CA  1 
ATOM 1194 C C   . HIS A 1 220  ? 178.276 189.271 185.272 1.00 0.00  ? 170 HIS A C   1 
ATOM 1195 O O   . HIS A 1 220  ? 178.270 190.521 185.298 1.00 5.43  ? 170 HIS A O   1 
ATOM 1196 C CB  . HIS A 1 220  ? 178.551 187.039 184.085 1.00 1.34  ? 170 HIS A CB  1 
ATOM 1197 C CG  . HIS A 1 220  ? 178.125 186.294 182.865 1.00 4.07  ? 170 HIS A CG  1 
ATOM 1198 N ND1 . HIS A 1 220  ? 177.125 185.346 182.878 1.00 14.65 ? 170 HIS A ND1 1 
ATOM 1199 C CD2 . HIS A 1 220  ? 178.561 186.354 181.601 1.00 3.49  ? 170 HIS A CD2 1 
ATOM 1200 C CE1 . HIS A 1 220  ? 176.971 184.856 181.656 1.00 14.53 ? 170 HIS A CE1 1 
ATOM 1201 N NE2 . HIS A 1 220  ? 177.834 185.455 180.865 1.00 11.51 ? 170 HIS A NE2 1 
ATOM 1202 N N   . HIS A 1 221  ? 178.138 188.597 186.357 1.00 3.99  ? 171 HIS A N   1 
ATOM 1203 C CA  . HIS A 1 221  ? 177.962 189.404 187.578 1.00 1.16  ? 171 HIS A CA  1 
ATOM 1204 C C   . HIS A 1 221  ? 179.230 189.383 188.418 1.00 0.84  ? 171 HIS A C   1 
ATOM 1205 O O   . HIS A 1 221  ? 180.314 189.375 187.827 1.00 4.85  ? 171 HIS A O   1 
ATOM 1206 C CB  . HIS A 1 221  ? 176.789 188.812 188.337 1.00 2.80  ? 171 HIS A CB  1 
ATOM 1207 C CG  . HIS A 1 221  ? 175.462 189.402 188.051 1.00 5.76  ? 171 HIS A CG  1 
ATOM 1208 N ND1 . HIS A 1 221  ? 174.438 188.647 187.531 1.00 5.91  ? 171 HIS A ND1 1 
ATOM 1209 C CD2 . HIS A 1 221  ? 174.974 190.625 188.236 1.00 9.56  ? 171 HIS A CD2 1 
ATOM 1210 C CE1 . HIS A 1 221  ? 173.370 189.412 187.390 1.00 8.62  ? 171 HIS A CE1 1 
ATOM 1211 N NE2 . HIS A 1 221  ? 173.673 190.617 187.811 1.00 11.64 ? 171 HIS A NE2 1 
ATOM 1212 N N   . LYS A 1 222  ? 179.115 189.607 189.716 1.00 2.81  ? 172 LYS A N   1 
ATOM 1213 C CA  . LYS A 1 222  ? 180.197 189.419 190.675 1.00 3.25  ? 172 LYS A CA  1 
ATOM 1214 C C   . LYS A 1 222  ? 180.053 188.093 191.414 1.00 2.04  ? 172 LYS A C   1 
ATOM 1215 O O   . LYS A 1 222  ? 181.048 187.407 191.678 1.00 1.53  ? 172 LYS A O   1 
ATOM 1216 C CB  . LYS A 1 222  ? 180.237 190.587 191.660 1.00 5.54  ? 172 LYS A CB  1 
ATOM 1217 C CG  . LYS A 1 222  ? 181.107 190.332 192.878 1.00 2.04  ? 172 LYS A CG  1 
ATOM 1218 C CD  . LYS A 1 222  ? 181.544 191.626 193.532 1.00 3.83  ? 172 LYS A CD  1 
ATOM 1219 C CE  . LYS A 1 222  ? 182.252 191.358 194.849 1.00 6.17  ? 172 LYS A CE  1 
ATOM 1220 N NZ  . LYS A 1 222  ? 183.724 191.225 194.676 1.00 6.61  ? 172 LYS A NZ  1 
ATOM 1221 N N   . TRP A 1 223  ? 178.819 187.713 191.757 1.00 0.96  ? 173 TRP A N   1 
ATOM 1222 C CA  . TRP A 1 223  ? 178.618 186.469 192.494 1.00 5.93  ? 173 TRP A CA  1 
ATOM 1223 C C   . TRP A 1 223  ? 178.877 185.249 191.622 1.00 7.11  ? 173 TRP A C   1 
ATOM 1224 O O   . TRP A 1 223  ? 179.255 184.190 192.135 1.00 1.75  ? 173 TRP A O   1 
ATOM 1225 C CB  . TRP A 1 223  ? 177.209 186.428 193.094 1.00 1.79  ? 173 TRP A CB  1 
ATOM 1226 C CG  . TRP A 1 223  ? 176.128 185.895 192.194 1.00 3.72  ? 173 TRP A CG  1 
ATOM 1227 C CD1 . TRP A 1 223  ? 175.267 186.628 191.432 1.00 6.83  ? 173 TRP A CD1 1 
ATOM 1228 C CD2 . TRP A 1 223  ? 175.777 184.520 191.982 1.00 3.10  ? 173 TRP A CD2 1 
ATOM 1229 N NE1 . TRP A 1 223  ? 174.409 185.799 190.754 1.00 12.16 ? 173 TRP A NE1 1 
ATOM 1230 C CE2 . TRP A 1 223  ? 174.702 184.500 191.073 1.00 3.54  ? 173 TRP A CE2 1 
ATOM 1231 C CE3 . TRP A 1 223  ? 176.272 183.306 192.467 1.00 1.12  ? 173 TRP A CE3 1 
ATOM 1232 C CZ2 . TRP A 1 223  ? 174.114 183.315 190.640 1.00 1.48  ? 173 TRP A CZ2 1 
ATOM 1233 C CZ3 . TRP A 1 223  ? 175.686 182.131 192.035 1.00 2.62  ? 173 TRP A CZ3 1 
ATOM 1234 C CH2 . TRP A 1 223  ? 174.618 182.144 191.132 1.00 3.23  ? 173 TRP A CH2 1 
ATOM 1235 N N   . ARG A 1 224  ? 178.720 185.394 190.301 1.00 3.32  ? 174 ARG A N   1 
ATOM 1236 C CA  . ARG A 1 224  ? 178.978 184.264 189.363 1.00 0.00  ? 174 ARG A CA  1 
ATOM 1237 C C   . ARG A 1 224  ? 180.489 184.090 189.176 1.00 4.01  ? 174 ARG A C   1 
ATOM 1238 O O   . ARG A 1 224  ? 180.904 182.972 188.811 1.00 10.99 ? 174 ARG A O   1 
ATOM 1239 C CB  . ARG A 1 224  ? 178.282 184.510 188.022 1.00 0.00  ? 174 ARG A CB  1 
ATOM 1240 C CG  . ARG A 1 224  ? 176.790 184.778 188.141 1.00 0.00  ? 174 ARG A CG  1 
ATOM 1241 C CD  . ARG A 1 224  ? 176.068 184.507 186.836 1.00 6.97  ? 174 ARG A CD  1 
ATOM 1242 N NE  . ARG A 1 224  ? 176.131 183.098 186.477 1.00 8.51  ? 174 ARG A NE  1 
ATOM 1243 C CZ  . ARG A 1 224  ? 175.614 182.581 185.369 1.00 1.38  ? 174 ARG A CZ  1 
ATOM 1244 N NH1 . ARG A 1 224  ? 175.100 183.376 184.449 1.00 0.00  ? 174 ARG A NH1 1 
ATOM 1245 N NH2 . ARG A 1 224  ? 175.622 181.272 185.181 1.00 1.25  ? 174 ARG A NH2 1 
ATOM 1246 N N   . ARG A 1 225  ? 181.269 185.151 189.396 1.00 4.85  ? 175 ARG A N   1 
ATOM 1247 C CA  . ARG A 1 225  ? 182.725 185.106 189.291 1.00 4.63  ? 175 ARG A CA  1 
ATOM 1248 C C   . ARG A 1 225  ? 183.222 184.593 187.946 1.00 2.85  ? 175 ARG A C   1 
ATOM 1249 O O   . ARG A 1 225  ? 184.032 183.662 187.905 1.00 11.43 ? 175 ARG A O   1 
ATOM 1250 C CB  . ARG A 1 225  ? 183.319 184.234 190.401 1.00 0.00  ? 175 ARG A CB  1 
ATOM 1251 C CG  . ARG A 1 225  ? 182.686 184.409 191.768 1.00 6.81  ? 175 ARG A CG  1 
ATOM 1252 C CD  . ARG A 1 225  ? 183.318 183.463 192.780 1.00 10.27 ? 175 ARG A CD  1 
ATOM 1253 N NE  . ARG A 1 225  ? 182.571 182.217 192.910 1.00 9.15  ? 175 ARG A NE  1 
ATOM 1254 C CZ  . ARG A 1 225  ? 183.083 181.084 193.370 1.00 0.60  ? 175 ARG A CZ  1 
ATOM 1255 N NH1 . ARG A 1 225  ? 184.347 181.001 193.751 1.00 0.00  ? 175 ARG A NH1 1 
ATOM 1256 N NH2 . ARG A 1 225  ? 182.307 180.007 193.447 1.00 1.01  ? 175 ARG A NH2 1 
ATOM 1257 N N   . MET A 1 226  ? 182.759 185.177 186.845 1.00 0.00  ? 176 MET A N   1 
ATOM 1258 C CA  . MET A 1 226  ? 183.244 184.814 185.520 1.00 0.00  ? 176 MET A CA  1 
ATOM 1259 C C   . MET A 1 226  ? 184.305 185.803 185.063 1.00 0.00  ? 176 MET A C   1 
ATOM 1260 O O   . MET A 1 226  ? 184.114 187.019 185.161 1.00 13.81 ? 176 MET A O   1 
ATOM 1261 C CB  . MET A 1 226  ? 182.111 184.764 184.498 1.00 0.00  ? 176 MET A CB  1 
ATOM 1262 C CG  . MET A 1 226  ? 181.187 183.590 184.668 1.00 0.00  ? 176 MET A CG  1 
ATOM 1263 S SD  . MET A 1 226  ? 179.943 183.543 183.376 1.00 0.00  ? 176 MET A SD  1 
ATOM 1264 C CE  . MET A 1 226  ? 178.858 182.309 184.054 1.00 3.15  ? 176 MET A CE  1 
ATOM 1265 N N   . TYR A 1 227  ? 185.410 185.275 184.553 1.00 1.65  ? 177 TYR A N   1 
ATOM 1266 C CA  . TYR A 1 227  ? 186.508 186.082 184.052 1.00 0.00  ? 177 TYR A CA  1 
ATOM 1267 C C   . TYR A 1 227  ? 186.915 185.558 182.685 1.00 4.23  ? 177 TYR A C   1 
ATOM 1268 O O   . TYR A 1 227  ? 186.785 184.365 182.401 1.00 17.53 ? 177 TYR A O   1 
ATOM 1269 C CB  . TYR A 1 227  ? 187.721 186.045 184.994 1.00 0.00  ? 177 TYR A CB  1 
ATOM 1270 C CG  . TYR A 1 227  ? 187.391 186.116 186.469 1.00 4.11  ? 177 TYR A CG  1 
ATOM 1271 C CD1 . TYR A 1 227  ? 186.931 184.997 187.153 1.00 4.12  ? 177 TYR A CD1 1 
ATOM 1272 C CD2 . TYR A 1 227  ? 187.571 187.289 187.186 1.00 7.01  ? 177 TYR A CD2 1 
ATOM 1273 C CE1 . TYR A 1 227  ? 186.638 185.051 188.498 1.00 0.00  ? 177 TYR A CE1 1 
ATOM 1274 C CE2 . TYR A 1 227  ? 187.281 187.350 188.536 1.00 5.92  ? 177 TYR A CE2 1 
ATOM 1275 C CZ  . TYR A 1 227  ? 186.813 186.226 189.185 1.00 6.16  ? 177 TYR A CZ  1 
ATOM 1276 O OH  . TYR A 1 227  ? 186.521 186.273 190.528 1.00 12.95 ? 177 TYR A OH  1 
ATOM 1277 N N   . VAL A 1 228  ? 187.393 186.459 181.834 1.00 0.00  ? 178 VAL A N   1 
ATOM 1278 C CA  . VAL A 1 228  ? 187.985 186.080 180.554 1.00 0.00  ? 178 VAL A CA  1 
ATOM 1279 C C   . VAL A 1 228  ? 189.309 186.811 180.419 1.00 0.00  ? 178 VAL A C   1 
ATOM 1280 O O   . VAL A 1 228  ? 189.389 188.010 180.705 1.00 0.78  ? 178 VAL A O   1 
ATOM 1281 C CB  . VAL A 1 228  ? 187.060 186.399 179.364 1.00 0.00  ? 178 VAL A CB  1 
ATOM 1282 C CG1 . VAL A 1 228  ? 185.973 185.343 179.242 1.00 0.00  ? 178 VAL A CG1 1 
ATOM 1283 C CG2 . VAL A 1 228  ? 186.454 187.782 179.514 1.00 0.00  ? 178 VAL A CG2 1 
ATOM 1284 N N   . GLY A 1 229  ? 190.353 186.097 180.003 1.00 0.00  ? 179 GLY A N   1 
ATOM 1285 C CA  . GLY A 1 229  ? 191.663 186.713 180.024 1.00 0.00  ? 179 GLY A CA  1 
ATOM 1286 C C   . GLY A 1 229  ? 192.581 186.198 178.941 1.00 0.00  ? 179 GLY A C   1 
ATOM 1287 O O   . GLY A 1 229  ? 192.348 185.154 178.328 1.00 15.85 ? 179 GLY A O   1 
ATOM 1288 N N   . GLU A 1 230  ? 193.661 186.946 178.739 1.00 0.00  ? 180 GLU A N   1 
ATOM 1289 C CA  . GLU A 1 230  ? 194.637 186.604 177.717 1.00 0.00  ? 180 GLU A CA  1 
ATOM 1290 C C   . GLU A 1 230  ? 196.051 186.776 178.247 1.00 0.00  ? 180 GLU A C   1 
ATOM 1291 O O   . GLU A 1 230  ? 196.324 187.642 179.087 1.00 10.41 ? 180 GLU A O   1 
ATOM 1292 C CB  . GLU A 1 230  ? 194.457 187.453 176.451 1.00 3.25  ? 180 GLU A CB  1 
ATOM 1293 C CG  . GLU A 1 230  ? 195.042 186.810 175.200 1.00 0.88  ? 180 GLU A CG  1 
ATOM 1294 C CD  . GLU A 1 230  ? 195.342 187.814 174.106 1.00 0.00  ? 180 GLU A CD  1 
ATOM 1295 O OE1 . GLU A 1 230  ? 194.788 188.930 174.152 1.00 11.23 ? 180 GLU A OE1 1 
ATOM 1296 O OE2 . GLU A 1 230  ? 196.139 187.489 173.202 1.00 0.00  ? 180 GLU A OE2 1 
ATOM 1297 N N   . CYS A 1 231  ? 196.944 185.925 177.742 1.00 2.00  ? 181 CYS A N   1 
ATOM 1298 C CA  . CYS A 1 231  ? 198.377 186.021 177.969 1.00 1.48  ? 181 CYS A CA  1 
ATOM 1299 C C   . CYS A 1 231  ? 199.074 185.946 176.620 1.00 9.13  ? 181 CYS A C   1 
ATOM 1300 O O   . CYS A 1 231  ? 198.641 185.208 175.732 1.00 0.60  ? 181 CYS A O   1 
ATOM 1301 C CB  . CYS A 1 231  ? 198.875 184.902 178.892 1.00 6.05  ? 181 CYS A CB  1 
ATOM 1302 S SG  . CYS A 1 231  ? 200.664 184.649 178.897 1.00 7.41  ? 181 CYS A SG  1 
ATOM 1303 N N   . GLN A 1 232  ? 200.102 186.784 176.455 1.00 0.00  ? 182 GLN A N   1 
ATOM 1304 C CA  . GLN A 1 232  ? 200.765 186.872 175.129 1.00 0.00  ? 182 GLN A CA  1 
ATOM 1305 C C   . GLN A 1 232  ? 202.278 186.709 175.247 1.00 10.22 ? 182 GLN A C   1 
ATOM 1306 O O   . GLN A 1 232  ? 202.848 187.172 176.255 1.00 8.68  ? 182 GLN A O   1 
ATOM 1307 C CB  . GLN A 1 232  ? 200.464 188.223 174.475 1.00 3.22  ? 182 GLN A CB  1 
ATOM 1308 C CG  . GLN A 1 232  ? 198.982 188.549 174.378 1.00 1.10  ? 182 GLN A CG  1 
ATOM 1309 C CD  . GLN A 1 232  ? 198.724 189.737 173.484 1.00 0.00  ? 182 GLN A CD  1 
ATOM 1310 O OE1 . GLN A 1 232  ? 199.633 190.275 172.856 1.00 4.39  ? 182 GLN A OE1 1 
ATOM 1311 N NE2 . GLN A 1 232  ? 197.472 190.161 173.422 1.00 0.00  ? 182 GLN A NE2 1 
ATOM 1312 N N   . GLY A 1 233  ? 202.893 186.076 174.251 1.00 0.00  ? 183 GLY A N   1 
ATOM 1313 C CA  . GLY A 1 233  ? 204.322 185.912 174.186 1.00 1.38  ? 183 GLY A CA  1 
ATOM 1314 C C   . GLY A 1 233  ? 204.754 185.897 172.739 1.00 10.31 ? 183 GLY A C   1 
ATOM 1315 O O   . GLY A 1 233  ? 203.921 185.843 171.829 1.00 10.69 ? 183 GLY A O   1 
ATOM 1316 N N   . PRO A 1 234  ? 206.062 185.930 172.490 1.00 3.40  ? 184 PRO A N   1 
ATOM 1317 C CA  . PRO A 1 234  ? 206.534 186.008 171.102 1.00 7.72  ? 184 PRO A CA  1 
ATOM 1318 C C   . PRO A 1 234  ? 206.101 184.798 170.293 1.00 17.66 ? 184 PRO A C   1 
ATOM 1319 O O   . PRO A 1 234  ? 206.591 183.683 170.500 1.00 11.01 ? 184 PRO A O   1 
ATOM 1320 C CB  . PRO A 1 234  ? 208.059 186.073 171.250 1.00 3.28  ? 184 PRO A CB  1 
ATOM 1321 C CG  . PRO A 1 234  ? 208.289 186.543 172.645 1.00 1.81  ? 184 PRO A CG  1 
ATOM 1322 C CD  . PRO A 1 234  ? 207.173 185.968 173.453 1.00 4.39  ? 184 PRO A CD  1 
ATOM 1323 N N   . GLY A 1 235  ? 205.176 185.020 169.364 1.00 9.94  ? 185 GLY A N   1 
ATOM 1324 C CA  . GLY A 1 235  ? 204.639 183.949 168.556 1.00 6.30  ? 185 GLY A CA  1 
ATOM 1325 C C   . GLY A 1 235  ? 203.648 183.039 169.245 1.00 6.46  ? 185 GLY A C   1 
ATOM 1326 O O   . GLY A 1 235  ? 203.298 182.001 168.679 1.00 10.16 ? 185 GLY A O   1 
ATOM 1327 N N   . VAL A 1 236  ? 203.204 183.412 170.452 1.00 2.42  ? 186 VAL A N   1 
ATOM 1328 C CA  . VAL A 1 236  ? 202.311 182.495 171.225 1.00 6.23  ? 186 VAL A CA  1 
ATOM 1329 C C   . VAL A 1 236  ? 201.200 183.262 171.948 1.00 0.00  ? 186 VAL A C   1 
ATOM 1330 O O   . VAL A 1 236  ? 201.511 184.286 172.586 1.00 3.65  ? 186 VAL A O   1 
ATOM 1331 C CB  . VAL A 1 236  ? 203.103 181.644 172.239 1.00 0.50  ? 186 VAL A CB  1 
ATOM 1332 C CG1 . VAL A 1 236  ? 204.073 180.712 171.535 1.00 0.00  ? 186 VAL A CG1 1 
ATOM 1333 C CG2 . VAL A 1 236  ? 203.824 182.483 173.282 1.00 0.98  ? 186 VAL A CG2 1 
ATOM 1334 N N   . ARG A 1 237  ? 199.957 182.779 171.857 1.00 8.69  ? 187 ARG A N   1 
ATOM 1335 C CA  . ARG A 1 237  ? 198.842 183.353 172.599 1.00 0.00  ? 187 ARG A CA  1 
ATOM 1336 C C   . ARG A 1 237  ? 198.207 182.279 173.469 1.00 0.00  ? 187 ARG A C   1 
ATOM 1337 O O   . ARG A 1 237  ? 198.158 181.108 173.085 1.00 2.85  ? 187 ARG A O   1 
ATOM 1338 C CB  . ARG A 1 237  ? 197.789 183.957 171.659 1.00 0.00  ? 187 ARG A CB  1 
ATOM 1339 C CG  . ARG A 1 237  ? 197.274 182.999 170.603 1.00 2.77  ? 187 ARG A CG  1 
ATOM 1340 C CD  . ARG A 1 237  ? 196.278 183.675 169.674 1.00 0.00  ? 187 ARG A CD  1 
ATOM 1341 N NE  . ARG A 1 237  ? 194.955 183.794 170.271 1.00 1.45  ? 187 ARG A NE  1 
ATOM 1342 C CZ  . ARG A 1 237  ? 193.994 182.893 170.124 1.00 2.34  ? 187 ARG A CZ  1 
ATOM 1343 N NH1 . ARG A 1 237  ? 194.167 181.816 169.378 1.00 9.39  ? 187 ARG A NH1 1 
ATOM 1344 N NH2 . ARG A 1 237  ? 192.828 183.081 170.734 1.00 0.53  ? 187 ARG A NH2 1 
ATOM 1345 N N   . THR A 1 238  ? 197.734 182.679 174.648 1.00 1.94  ? 188 THR A N   1 
ATOM 1346 C CA  . THR A 1 238  ? 197.063 181.777 175.573 1.00 0.00  ? 188 THR A CA  1 
ATOM 1347 C C   . THR A 1 238  ? 195.755 182.412 176.010 1.00 0.00  ? 188 THR A C   1 
ATOM 1348 O O   . THR A 1 238  ? 195.745 183.549 176.493 1.00 11.06 ? 188 THR A O   1 
ATOM 1349 C CB  . THR A 1 238  ? 197.929 181.480 176.800 1.00 0.00  ? 188 THR A CB  1 
ATOM 1350 O OG1 . THR A 1 238  ? 199.210 181.000 176.379 1.00 5.87  ? 188 THR A OG1 1 
ATOM 1351 C CG2 . THR A 1 238  ? 197.268 180.437 177.676 1.00 0.43  ? 188 THR A CG2 1 
ATOM 1352 N N   . ASP A 1 239  ? 194.664 181.648 175.864 1.00 0.00  ? 189 ASP A N   1 
ATOM 1353 C CA  . ASP A 1 239  ? 193.313 182.180 176.187 1.00 0.00  ? 189 ASP A CA  1 
ATOM 1354 C C   . ASP A 1 239  ? 192.730 181.489 177.421 1.00 0.00  ? 189 ASP A C   1 
ATOM 1355 O O   . ASP A 1 239  ? 192.483 180.269 177.352 1.00 8.39  ? 189 ASP A O   1 
ATOM 1356 C CB  . ASP A 1 239  ? 192.377 182.054 174.983 1.00 0.00  ? 189 ASP A CB  1 
ATOM 1357 C CG  . ASP A 1 239  ? 193.076 182.351 173.670 1.00 13.24 ? 189 ASP A CG  1 
ATOM 1358 O OD1 . ASP A 1 239  ? 193.252 183.546 173.358 1.00 10.98 ? 189 ASP A OD1 1 
ATOM 1359 O OD2 . ASP A 1 239  ? 193.448 181.386 172.974 1.00 11.61 ? 189 ASP A OD2 1 
ATOM 1360 N N   . PHE A 1 240  ? 192.521 182.243 178.499 1.00 5.98  ? 190 PHE A N   1 
ATOM 1361 C CA  . PHE A 1 240  ? 191.914 181.745 179.724 1.00 0.00  ? 190 PHE A CA  1 
ATOM 1362 C C   . PHE A 1 240  ? 190.421 182.018 179.619 1.00 0.00  ? 190 PHE A C   1 
ATOM 1363 O O   . PHE A 1 240  ? 189.992 183.178 179.648 1.00 8.89  ? 190 PHE A O   1 
ATOM 1364 C CB  . PHE A 1 240  ? 192.507 182.425 180.955 1.00 0.00  ? 190 PHE A CB  1 
ATOM 1365 C CG  . PHE A 1 240  ? 194.006 182.401 181.005 1.00 0.00  ? 190 PHE A CG  1 
ATOM 1366 C CD1 . PHE A 1 240  ? 194.675 181.335 181.573 1.00 7.93  ? 190 PHE A CD1 1 
ATOM 1367 C CD2 . PHE A 1 240  ? 194.744 183.454 180.500 1.00 0.00  ? 190 PHE A CD2 1 
ATOM 1368 C CE1 . PHE A 1 240  ? 196.052 181.316 181.627 1.00 8.54  ? 190 PHE A CE1 1 
ATOM 1369 C CE2 . PHE A 1 240  ? 196.119 183.438 180.552 1.00 0.00  ? 190 PHE A CE2 1 
ATOM 1370 C CZ  . PHE A 1 240  ? 196.773 182.367 181.116 1.00 3.73  ? 190 PHE A CZ  1 
ATOM 1371 N N   . GLU A 1 241  ? 189.639 180.953 179.483 1.00 0.00  ? 191 GLU A N   1 
ATOM 1372 C CA  . GLU A 1 241  ? 188.199 181.058 179.316 1.00 0.00  ? 191 GLU A CA  1 
ATOM 1373 C C   . GLU A 1 241  ? 187.515 180.201 180.369 1.00 0.00  ? 191 GLU A C   1 
ATOM 1374 O O   . GLU A 1 241  ? 188.133 179.328 180.981 1.00 8.81  ? 191 GLU A O   1 
ATOM 1375 C CB  . GLU A 1 241  ? 187.768 180.631 177.909 1.00 2.44  ? 191 GLU A CB  1 
ATOM 1376 C CG  . GLU A 1 241  ? 188.452 181.415 176.802 1.00 6.18  ? 191 GLU A CG  1 
ATOM 1377 C CD  . GLU A 1 241  ? 187.990 181.006 175.420 1.00 4.53  ? 191 GLU A CD  1 
ATOM 1378 O OE1 . GLU A 1 241  ? 187.077 180.162 175.321 1.00 0.56  ? 191 GLU A OE1 1 
ATOM 1379 O OE2 . GLU A 1 241  ? 188.537 181.533 174.430 1.00 7.22  ? 191 GLU A OE2 1 
ATOM 1380 N N   . MET A 1 242  ? 186.246 180.524 180.648 1.00 0.00  ? 192 MET A N   1 
ATOM 1381 C CA  . MET A 1 242  ? 185.566 179.821 181.769 1.00 2.45  ? 192 MET A CA  1 
ATOM 1382 C C   . MET A 1 242  ? 184.053 179.719 181.559 1.00 0.00  ? 192 MET A C   1 
ATOM 1383 O O   . MET A 1 242  ? 183.439 180.739 181.188 1.00 0.00  ? 192 MET A O   1 
ATOM 1384 C CB  . MET A 1 242  ? 185.834 180.560 183.085 1.00 4.66  ? 192 MET A CB  1 
ATOM 1385 C CG  . MET A 1 242  ? 185.151 179.939 184.288 1.00 0.00  ? 192 MET A CG  1 
ATOM 1386 S SD  . MET A 1 242  ? 185.460 180.888 185.797 1.00 0.00  ? 192 MET A SD  1 
ATOM 1387 C CE  . MET A 1 242  ? 186.845 181.896 185.271 1.00 0.00  ? 192 MET A CE  1 
ATOM 1388 N N   . VAL A 1 243  ? 183.486 178.536 181.791 1.00 0.00  ? 193 VAL A N   1 
ATOM 1389 C CA  . VAL A 1 243  ? 182.051 178.295 181.717 1.00 0.00  ? 193 VAL A CA  1 
ATOM 1390 C C   . VAL A 1 243  ? 181.567 177.854 183.092 1.00 0.00  ? 193 VAL A C   1 
ATOM 1391 O O   . VAL A 1 243  ? 182.227 177.057 183.769 1.00 5.31  ? 193 VAL A O   1 
ATOM 1392 C CB  . VAL A 1 243  ? 181.693 177.253 180.634 1.00 0.00  ? 193 VAL A CB  1 
ATOM 1393 C CG1 . VAL A 1 243  ? 182.496 175.998 180.818 1.00 0.00  ? 193 VAL A CG1 1 
ATOM 1394 C CG2 . VAL A 1 243  ? 180.206 176.933 180.667 1.00 0.00  ? 193 VAL A CG2 1 
ATOM 1395 N N   . HIS A 1 244  ? 180.429 178.398 183.517 1.00 1.45  ? 194 HIS A N   1 
ATOM 1396 C CA  . HIS A 1 244  ? 179.857 178.103 184.829 1.00 0.00  ? 194 HIS A CA  1 
ATOM 1397 C C   . HIS A 1 244  ? 178.356 177.929 184.653 1.00 0.00  ? 194 HIS A C   1 
ATOM 1398 O O   . HIS A 1 244  ? 177.646 178.897 184.367 1.00 12.37 ? 194 HIS A O   1 
ATOM 1399 C CB  . HIS A 1 244  ? 180.181 179.217 185.826 1.00 0.95  ? 194 HIS A CB  1 
ATOM 1400 C CG  . HIS A 1 244  ? 179.143 179.414 186.888 1.00 0.00  ? 194 HIS A CG  1 
ATOM 1401 N ND1 . HIS A 1 244  ? 179.001 178.559 187.960 1.00 3.17  ? 194 HIS A ND1 1 
ATOM 1402 C CD2 . HIS A 1 244  ? 178.214 180.383 187.055 1.00 0.00  ? 194 HIS A CD2 1 
ATOM 1403 C CE1 . HIS A 1 244  ? 178.020 178.988 188.734 1.00 0.00  ? 194 HIS A CE1 1 
ATOM 1404 N NE2 . HIS A 1 244  ? 177.526 180.093 188.208 1.00 0.00  ? 194 HIS A NE2 1 
ATOM 1405 N N   . LEU A 1 245  ? 177.874 176.699 184.812 1.00 0.00  ? 195 LEU A N   1 
ATOM 1406 C CA  . LEU A 1 245  ? 176.472 176.392 184.568 1.00 0.00  ? 195 LEU A CA  1 
ATOM 1407 C C   . LEU A 1 245  ? 175.944 175.516 185.694 1.00 8.37  ? 195 LEU A C   1 
ATOM 1408 O O   . LEU A 1 245  ? 176.699 175.055 186.553 1.00 14.30 ? 195 LEU A O   1 
ATOM 1409 C CB  . LEU A 1 245  ? 176.275 175.701 183.211 1.00 7.66  ? 195 LEU A CB  1 
ATOM 1410 C CG  . LEU A 1 245  ? 174.956 175.965 182.479 1.00 10.10 ? 195 LEU A CG  1 
ATOM 1411 C CD1 . LEU A 1 245  ? 174.880 177.405 182.001 1.00 7.02  ? 195 LEU A CD1 1 
ATOM 1412 C CD2 . LEU A 1 245  ? 174.778 175.002 181.316 1.00 10.47 ? 195 LEU A CD2 1 
ATOM 1413 N N   . ARG A 1 246  ? 174.630 175.289 185.681 1.00 11.00 ? 196 ARG A N   1 
ATOM 1414 C CA  . ARG A 1 246  ? 173.999 174.485 186.721 1.00 18.25 ? 196 ARG A CA  1 
ATOM 1415 C C   . ARG A 1 246  ? 173.672 173.069 186.252 1.00 25.75 ? 196 ARG A C   1 
ATOM 1416 O O   . ARG A 1 246  ? 173.886 172.106 186.995 1.00 28.29 ? 196 ARG A O   1 
ATOM 1417 C CB  . ARG A 1 246  ? 172.729 175.178 187.229 1.00 10.44 ? 196 ARG A CB  1 
ATOM 1418 C CG  . ARG A 1 246  ? 171.668 175.435 186.174 1.00 10.27 ? 196 ARG A CG  1 
ATOM 1419 C CD  . ARG A 1 246  ? 170.469 176.154 186.768 1.00 18.33 ? 196 ARG A CD  1 
ATOM 1420 N NE  . ARG A 1 246  ? 170.185 175.716 188.129 1.00 23.05 ? 196 ARG A NE  1 
ATOM 1421 C CZ  . ARG A 1 246  ? 169.530 174.606 188.438 1.00 19.84 ? 196 ARG A CZ  1 
ATOM 1422 N NH1 . ARG A 1 246  ? 169.059 173.798 187.502 1.00 15.78 ? 196 ARG A NH1 1 
ATOM 1423 N NH2 . ARG A 1 246  ? 169.339 174.299 189.718 1.00 17.25 ? 196 ARG A NH2 1 
ATOM 1424 N N   . LYS A 1 247  ? 173.157 172.918 185.034 1.00 18.53 ? 197 LYS A N   1 
ATOM 1425 C CA  . LYS A 1 247  ? 172.702 171.625 184.544 1.00 14.59 ? 197 LYS A CA  1 
ATOM 1426 C C   . LYS A 1 247  ? 173.261 171.360 183.155 1.00 16.77 ? 197 LYS A C   1 
ATOM 1427 O O   . LYS A 1 247  ? 173.209 172.225 182.277 1.00 17.82 ? 197 LYS A O   1 
ATOM 1428 C CB  . LYS A 1 247  ? 171.173 171.555 184.513 1.00 17.45 ? 197 LYS A CB  1 
ATOM 1429 C CG  . LYS A 1 247  ? 170.616 170.143 184.504 1.00 21.90 ? 197 LYS A CG  1 
ATOM 1430 C CD  . LYS A 1 247  ? 169.134 170.141 184.174 1.00 21.55 ? 197 LYS A CD  1 
ATOM 1431 C CE  . LYS A 1 247  ? 168.384 171.171 185.001 1.00 17.00 ? 197 LYS A CE  1 
ATOM 1432 N NZ  . LYS A 1 247  ? 168.573 170.955 186.462 1.00 15.89 ? 197 LYS A NZ  1 
ATOM 1433 N N   . VAL A 1 248  ? 173.786 170.154 182.966 1.00 20.10 ? 198 VAL A N   1 
ATOM 1434 C CA  . VAL A 1 248  ? 174.367 169.733 181.692 1.00 23.19 ? 198 VAL A CA  1 
ATOM 1435 C C   . VAL A 1 248  ? 173.850 168.338 181.372 1.00 18.09 ? 198 VAL A C   1 
ATOM 1436 O O   . VAL A 1 248  ? 173.333 167.635 182.254 1.00 17.62 ? 198 VAL A O   1 
ATOM 1437 C CB  . VAL A 1 248  ? 175.914 169.750 181.735 1.00 22.66 ? 198 VAL A CB  1 
ATOM 1438 C CG1 . VAL A 1 248  ? 176.433 171.148 182.035 1.00 14.11 ? 198 VAL A CG1 1 
ATOM 1439 C CG2 . VAL A 1 248  ? 176.421 168.749 182.760 1.00 18.47 ? 198 VAL A CG2 1 
ATOM 1440 N N   . PRO A 1 249  ? 173.955 167.914 180.111 1.00 12.75 ? 199 PRO A N   1 
ATOM 1441 C CA  . PRO A 1 249  ? 173.630 166.522 179.782 1.00 16.74 ? 199 PRO A CA  1 
ATOM 1442 C C   . PRO A 1 249  ? 174.469 165.558 180.607 1.00 18.76 ? 199 PRO A C   1 
ATOM 1443 O O   . PRO A 1 249  ? 175.643 165.809 180.888 1.00 21.81 ? 199 PRO A O   1 
ATOM 1444 C CB  . PRO A 1 249  ? 173.964 166.426 178.290 1.00 16.57 ? 199 PRO A CB  1 
ATOM 1445 C CG  . PRO A 1 249  ? 173.765 167.804 177.785 1.00 17.80 ? 199 PRO A CG  1 
ATOM 1446 C CD  . PRO A 1 249  ? 174.168 168.728 178.901 1.00 13.64 ? 199 PRO A CD  1 
ATOM 1447 N N   . ASN A 1 250  ? 173.851 164.443 180.993 1.00 17.05 ? 200 ASN A N   1 
ATOM 1448 C CA  . ASN A 1 250  ? 174.441 163.514 181.952 1.00 16.99 ? 200 ASN A CA  1 
ATOM 1449 C C   . ASN A 1 250  ? 175.713 162.853 181.432 1.00 16.43 ? 200 ASN A C   1 
ATOM 1450 O O   . ASN A 1 250  ? 176.342 162.067 182.147 1.00 20.95 ? 200 ASN A O   1 
ATOM 1451 C CB  . ASN A 1 250  ? 173.419 162.444 182.340 1.00 22.36 ? 200 ASN A CB  1 
ATOM 1452 C CG  . ASN A 1 250  ? 172.375 162.962 183.308 1.00 23.00 ? 200 ASN A CG  1 
ATOM 1453 O OD1 . ASN A 1 250  ? 172.610 163.927 184.035 1.00 23.09 ? 200 ASN A OD1 1 
ATOM 1454 N ND2 . ASN A 1 250  ? 171.212 162.323 183.321 1.00 21.97 ? 200 ASN A ND2 1 
ATOM 1455 N N   . GLN A 1 251  ? 176.103 163.159 180.199 1.00 12.71 ? 201 GLN A N   1 
ATOM 1456 C CA  . GLN A 1 251  ? 177.328 162.629 179.619 1.00 16.11 ? 201 GLN A CA  1 
ATOM 1457 C C   . GLN A 1 251  ? 178.555 163.459 179.979 1.00 14.15 ? 201 GLN A C   1 
ATOM 1458 O O   . GLN A 1 251  ? 179.636 163.213 179.436 1.00 13.51 ? 201 GLN A O   1 
ATOM 1459 C CB  . GLN A 1 251  ? 177.189 162.528 178.096 1.00 14.26 ? 201 GLN A CB  1 
ATOM 1460 C CG  . GLN A 1 251  ? 177.047 163.865 177.388 1.00 18.29 ? 201 GLN A CG  1 
ATOM 1461 C CD  . GLN A 1 251  ? 176.100 163.800 176.204 1.00 24.01 ? 201 GLN A CD  1 
ATOM 1462 O OE1 . GLN A 1 251  ? 175.147 163.021 176.198 1.00 23.48 ? 201 GLN A OE1 1 
ATOM 1463 N NE2 . GLN A 1 251  ? 176.356 164.624 175.195 1.00 22.62 ? 201 GLN A NE2 1 
ATOM 1464 N N   . TYR A 1 252  ? 178.413 164.433 180.876 1.00 10.15 ? 202 TYR A N   1 
ATOM 1465 C CA  . TYR A 1 252  ? 179.517 165.291 181.284 1.00 12.13 ? 202 TYR A CA  1 
ATOM 1466 C C   . TYR A 1 252  ? 179.900 165.111 182.749 1.00 15.60 ? 202 TYR A C   1 
ATOM 1467 O O   . TYR A 1 252  ? 180.714 165.883 183.264 1.00 13.87 ? 202 TYR A O   1 
ATOM 1468 C CB  . TYR A 1 252  ? 179.172 166.758 181.017 1.00 14.77 ? 202 TYR A CB  1 
ATOM 1469 C CG  . TYR A 1 252  ? 178.887 167.084 179.568 1.00 14.51 ? 202 TYR A CG  1 
ATOM 1470 C CD1 . TYR A 1 252  ? 179.832 166.843 178.583 1.00 14.53 ? 202 TYR A CD1 1 
ATOM 1471 C CD2 . TYR A 1 252  ? 177.678 167.649 179.189 1.00 15.24 ? 202 TYR A CD2 1 
ATOM 1472 C CE1 . TYR A 1 252  ? 179.579 167.145 177.259 1.00 11.34 ? 202 TYR A CE1 1 
ATOM 1473 C CE2 . TYR A 1 252  ? 177.416 167.954 177.867 1.00 15.95 ? 202 TYR A CE2 1 
ATOM 1474 C CZ  . TYR A 1 252  ? 178.370 167.701 176.908 1.00 15.03 ? 202 TYR A CZ  1 
ATOM 1475 O OH  . TYR A 1 252  ? 178.111 168.004 175.591 1.00 20.23 ? 202 TYR A OH  1 
ATOM 1476 N N   . THR A 1 253  ? 179.340 164.116 183.432 1.00 14.58 ? 203 THR A N   1 
ATOM 1477 C CA  . THR A 1 253  ? 179.577 163.934 184.859 1.00 17.27 ? 203 THR A CA  1 
ATOM 1478 C C   . THR A 1 253  ? 180.729 162.985 185.168 1.00 18.17 ? 203 THR A C   1 
ATOM 1479 O O   . THR A 1 253  ? 181.048 162.793 186.346 1.00 25.51 ? 203 THR A O   1 
ATOM 1480 C CB  . THR A 1 253  ? 178.307 163.427 185.548 1.00 18.48 ? 203 THR A CB  1 
ATOM 1481 O OG1 . THR A 1 253  ? 178.006 162.103 185.089 1.00 17.10 ? 203 THR A OG1 1 
ATOM 1482 C CG2 . THR A 1 253  ? 177.134 164.344 185.241 1.00 14.86 ? 203 THR A CG2 1 
ATOM 1483 N N   . HIS A 1 254  ? 181.355 162.389 184.161 1.00 8.56  ? 204 HIS A N   1 
ATOM 1484 C CA  . HIS A 1 254  ? 182.468 161.471 184.364 1.00 0.00  ? 204 HIS A CA  1 
ATOM 1485 C C   . HIS A 1 254  ? 183.724 162.035 183.709 1.00 1.77  ? 204 HIS A C   1 
ATOM 1486 O O   . HIS A 1 254  ? 183.707 163.101 183.093 1.00 11.75 ? 204 HIS A O   1 
ATOM 1487 C CB  . HIS A 1 254  ? 182.137 160.079 183.820 1.00 4.99  ? 204 HIS A CB  1 
ATOM 1488 C CG  . HIS A 1 254  ? 181.210 160.090 182.645 1.00 12.94 ? 204 HIS A CG  1 
ATOM 1489 N ND1 . HIS A 1 254  ? 181.647 160.285 181.353 1.00 10.94 ? 204 HIS A ND1 1 
ATOM 1490 C CD2 . HIS A 1 254  ? 179.869 159.922 182.567 1.00 17.52 ? 204 HIS A CD2 1 
ATOM 1491 C CE1 . HIS A 1 254  ? 180.615 160.239 180.529 1.00 7.75  ? 204 HIS A CE1 1 
ATOM 1492 N NE2 . HIS A 1 254  ? 179.525 160.020 181.241 1.00 14.12 ? 204 HIS A NE2 1 
ATOM 1493 N N   . LEU A 1 255  ? 184.837 161.313 183.846 1.00 0.00  ? 205 LEU A N   1 
ATOM 1494 C CA  . LEU A 1 255  ? 186.124 161.801 183.282 1.00 0.00  ? 205 LEU A CA  1 
ATOM 1495 C C   . LEU A 1 255  ? 186.098 161.656 181.758 1.00 3.86  ? 205 LEU A C   1 
ATOM 1496 O O   . LEU A 1 255  ? 186.689 162.516 181.078 1.00 4.63  ? 205 LEU A O   1 
ATOM 1497 C CB  . LEU A 1 255  ? 187.273 160.991 183.890 1.00 3.36  ? 205 LEU A CB  1 
ATOM 1498 C CG  . LEU A 1 255  ? 188.679 161.484 183.553 1.00 2.85  ? 205 LEU A CG  1 
ATOM 1499 C CD1 . LEU A 1 255  ? 188.793 162.987 183.757 1.00 6.23  ? 205 LEU A CD1 1 
ATOM 1500 C CD2 . LEU A 1 255  ? 189.719 160.751 184.386 1.00 5.01  ? 205 LEU A CD2 1 
ATOM 1501 N N   . SER A 1 256  ? 185.434 160.617 181.241 1.00 12.00 ? 206 SER A N   1 
ATOM 1502 C CA  . SER A 1 256  ? 185.467 160.395 179.797 1.00 0.00  ? 206 SER A CA  1 
ATOM 1503 C C   . SER A 1 256  ? 184.855 161.566 179.037 1.00 1.18  ? 206 SER A C   1 
ATOM 1504 O O   . SER A 1 256  ? 185.401 162.003 178.018 1.00 3.90  ? 206 SER A O   1 
ATOM 1505 C CB  . SER A 1 256  ? 184.746 159.095 179.447 1.00 0.22  ? 206 SER A CB  1 
ATOM 1506 O OG  . SER A 1 256  ? 183.374 159.172 179.786 1.00 10.44 ? 206 SER A OG  1 
ATOM 1507 N N   . GLY A 1 257  ? 183.721 162.084 179.512 1.00 1.94  ? 207 GLY A N   1 
ATOM 1508 C CA  . GLY A 1 257  ? 183.138 163.253 178.873 1.00 0.00  ? 207 GLY A CA  1 
ATOM 1509 C C   . GLY A 1 257  ? 184.043 164.466 178.959 1.00 0.00  ? 207 GLY A C   1 
ATOM 1510 O O   . GLY A 1 257  ? 184.158 165.240 178.004 1.00 5.01  ? 207 GLY A O   1 
ATOM 1511 N N   . LEU A 1 258  ? 184.704 164.643 180.104 1.00 5.17  ? 208 LEU A N   1 
ATOM 1512 C CA  . LEU A 1 258  ? 185.643 165.748 180.264 1.00 9.85  ? 208 LEU A CA  1 
ATOM 1513 C C   . LEU A 1 258  ? 186.813 165.622 179.296 1.00 3.20  ? 208 LEU A C   1 
ATOM 1514 O O   . LEU A 1 258  ? 187.252 166.616 178.707 1.00 6.85  ? 208 LEU A O   1 
ATOM 1515 C CB  . LEU A 1 258  ? 186.146 165.793 181.705 1.00 4.02  ? 208 LEU A CB  1 
ATOM 1516 C CG  . LEU A 1 258  ? 185.385 166.617 182.743 1.00 0.00  ? 208 LEU A CG  1 
ATOM 1517 C CD1 . LEU A 1 258  ? 183.904 166.291 182.751 1.00 0.84  ? 208 LEU A CD1 1 
ATOM 1518 C CD2 . LEU A 1 258  ? 185.988 166.358 184.102 1.00 0.00  ? 208 LEU A CD2 1 
ATOM 1519 N N   . LEU A 1 259  ? 187.314 164.394 179.135 1.00 2.88  ? 209 LEU A N   1 
ATOM 1520 C CA  . LEU A 1 259  ? 188.437 164.155 178.190 1.00 3.09  ? 209 LEU A CA  1 
ATOM 1521 C C   . LEU A 1 259  ? 187.958 164.457 176.767 1.00 9.20  ? 209 LEU A C   1 
ATOM 1522 O O   . LEU A 1 259  ? 188.722 165.085 176.009 1.00 22.50 ? 209 LEU A O   1 
ATOM 1523 C CB  . LEU A 1 259  ? 188.899 162.701 178.321 1.00 1.78  ? 209 LEU A CB  1 
ATOM 1524 C CG  . LEU A 1 259  ? 189.833 162.417 179.495 1.00 1.30  ? 209 LEU A CG  1 
ATOM 1525 C CD1 . LEU A 1 259  ? 189.938 160.923 179.752 1.00 2.18  ? 209 LEU A CD1 1 
ATOM 1526 C CD2 . LEU A 1 259  ? 191.210 163.015 179.249 1.00 0.00  ? 209 LEU A CD2 1 
ATOM 1527 N N   . ASP A 1 260  ? 186.738 164.029 176.426 1.00 5.47  ? 210 ASP A N   1 
ATOM 1528 C CA  . ASP A 1 260  ? 186.207 164.294 175.094 1.00 3.22  ? 210 ASP A CA  1 
ATOM 1529 C C   . ASP A 1 260  ? 186.093 165.790 174.839 1.00 4.65  ? 210 ASP A C   1 
ATOM 1530 O O   . ASP A 1 260  ? 186.440 166.267 173.755 1.00 3.19  ? 210 ASP A O   1 
ATOM 1531 C CB  . ASP A 1 260  ? 184.851 163.613 174.919 1.00 2.01  ? 210 ASP A CB  1 
ATOM 1532 C CG  . ASP A 1 260  ? 184.604 163.175 173.489 1.00 6.01  ? 210 ASP A CG  1 
ATOM 1533 O OD1 . ASP A 1 260  ? 185.268 163.715 172.580 1.00 4.92  ? 210 ASP A OD1 1 
ATOM 1534 O OD2 . ASP A 1 260  ? 183.747 162.292 173.274 1.00 8.71  ? 210 ASP A OD2 1 
ATOM 1535 N N   . ILE A 1 261  ? 185.616 166.547 175.832 1.00 2.21  ? 211 ILE A N   1 
ATOM 1536 C CA  . ILE A 1 261  ? 185.536 168.000 175.695 1.00 3.06  ? 211 ILE A CA  1 
ATOM 1537 C C   . ILE A 1 261  ? 186.926 168.597 175.518 1.00 0.00  ? 211 ILE A C   1 
ATOM 1538 O O   . ILE A 1 261  ? 187.145 169.470 174.669 1.00 13.23 ? 211 ILE A O   1 
ATOM 1539 C CB  . ILE A 1 261  ? 184.819 168.613 176.911 1.00 0.00  ? 211 ILE A CB  1 
ATOM 1540 C CG1 . ILE A 1 261  ? 183.323 168.313 176.867 1.00 0.00  ? 211 ILE A CG1 1 
ATOM 1541 C CG2 . ILE A 1 261  ? 185.060 170.107 176.968 1.00 5.19  ? 211 ILE A CG2 1 
ATOM 1542 C CD1 . ILE A 1 261  ? 182.581 168.830 178.073 1.00 0.00  ? 211 ILE A CD1 1 
ATOM 1543 N N   . PHE A 1 262  ? 187.881 168.137 176.325 1.00 5.11  ? 212 PHE A N   1 
ATOM 1544 C CA  . PHE A 1 262  ? 189.255 168.618 176.235 1.00 0.94  ? 212 PHE A CA  1 
ATOM 1545 C C   . PHE A 1 262  ? 189.818 168.413 174.833 1.00 4.60  ? 212 PHE A C   1 
ATOM 1546 O O   . PHE A 1 262  ? 190.340 169.349 174.214 1.00 4.54  ? 212 PHE A O   1 
ATOM 1547 C CB  . PHE A 1 262  ? 190.097 167.885 177.281 1.00 8.19  ? 212 PHE A CB  1 
ATOM 1548 C CG  . PHE A 1 262  ? 191.464 168.455 177.484 1.00 0.00  ? 212 PHE A CG  1 
ATOM 1549 C CD1 . PHE A 1 262  ? 191.643 169.798 177.736 1.00 2.11  ? 212 PHE A CD1 1 
ATOM 1550 C CD2 . PHE A 1 262  ? 192.572 167.632 177.446 1.00 0.00  ? 212 PHE A CD2 1 
ATOM 1551 C CE1 . PHE A 1 262  ? 192.902 170.308 177.932 1.00 1.56  ? 212 PHE A CE1 1 
ATOM 1552 C CE2 . PHE A 1 262  ? 193.829 168.137 177.640 1.00 0.00  ? 212 PHE A CE2 1 
ATOM 1553 C CZ  . PHE A 1 262  ? 193.996 169.476 177.883 1.00 2.36  ? 212 PHE A CZ  1 
ATOM 1554 N N   . LYS A 1 263  ? 189.692 167.194 174.303 1.00 0.00  ? 213 LYS A N   1 
ATOM 1555 C CA  . LYS A 1 263  ? 190.298 166.883 173.012 1.00 0.00  ? 213 LYS A CA  1 
ATOM 1556 C C   . LYS A 1 263  ? 189.521 167.494 171.852 1.00 4.77  ? 213 LYS A C   1 
ATOM 1557 O O   . LYS A 1 263  ? 190.105 167.768 170.797 1.00 9.56  ? 213 LYS A O   1 
ATOM 1558 C CB  . LYS A 1 263  ? 190.414 165.370 172.843 1.00 0.00  ? 213 LYS A CB  1 
ATOM 1559 C CG  . LYS A 1 263  ? 191.400 164.727 173.802 1.00 0.00  ? 213 LYS A CG  1 
ATOM 1560 C CD  . LYS A 1 263  ? 191.317 163.214 173.744 1.00 2.10  ? 213 LYS A CD  1 
ATOM 1561 C CE  . LYS A 1 263  ? 192.361 162.569 174.635 1.00 4.34  ? 213 LYS A CE  1 
ATOM 1562 N NZ  . LYS A 1 263  ? 192.497 161.112 174.358 1.00 0.00  ? 213 LYS A NZ  1 
ATOM 1563 N N   . SER A 1 264  ? 188.221 167.725 172.055 1.00 7.10  ? 214 SER A N   1 
ATOM 1564 C CA  . SER A 1 264  ? 187.413 168.401 171.007 1.00 0.52  ? 214 SER A CA  1 
ATOM 1565 C C   . SER A 1 264  ? 187.852 169.866 170.915 1.00 0.58  ? 214 SER A C   1 
ATOM 1566 O O   . SER A 1 264  ? 188.000 170.369 169.784 1.00 7.51  ? 214 SER A O   1 
ATOM 1567 C CB  . SER A 1 264  ? 185.941 168.287 171.293 1.00 0.74  ? 214 SER A CB  1 
ATOM 1568 O OG  . SER A 1 264  ? 185.183 168.960 170.299 1.00 4.79  ? 214 SER A OG  1 
ATOM 1569 N N   . LYS A 1 265  ? 188.044 170.551 172.050 1.00 3.25  ? 215 LYS A N   1 
ATOM 1570 C CA  . LYS A 1 265  ? 188.500 171.972 172.015 1.00 1.18  ? 215 LYS A CA  1 
ATOM 1571 C C   . LYS A 1 265  ? 189.936 172.034 171.474 1.00 0.00  ? 215 LYS A C   1 
ATOM 1572 O O   . LYS A 1 265  ? 190.208 172.938 170.660 1.00 0.00  ? 215 LYS A O   1 
ATOM 1573 C CB  . LYS A 1 265  ? 188.359 172.673 173.374 1.00 7.87  ? 215 LYS A CB  1 
ATOM 1574 C CG  . LYS A 1 265  ? 188.839 174.125 173.430 1.00 6.66  ? 215 LYS A CG  1 
ATOM 1575 C CD  . LYS A 1 265  ? 187.875 175.194 172.906 1.00 0.00  ? 215 LYS A CD  1 
ATOM 1576 C CE  . LYS A 1 265  ? 188.267 176.601 173.304 1.00 0.00  ? 215 LYS A CE  1 
ATOM 1577 N NZ  . LYS A 1 265  ? 187.234 177.588 172.912 1.00 0.00  ? 215 LYS A NZ  1 
ATOM 1578 N N   . ILE A 1 266  ? 190.816 171.116 171.894 1.00 6.80  ? 216 ILE A N   1 
ATOM 1579 C CA  . ILE A 1 266  ? 192.192 171.082 171.314 1.00 8.11  ? 216 ILE A CA  1 
ATOM 1580 C C   . ILE A 1 266  ? 192.070 171.199 169.792 1.00 3.63  ? 216 ILE A C   1 
ATOM 1581 O O   . ILE A 1 266  ? 192.690 172.115 169.218 1.00 3.61  ? 216 ILE A O   1 
ATOM 1582 C CB  . ILE A 1 266  ? 192.929 169.796 171.739 1.00 10.78 ? 216 ILE A CB  1 
ATOM 1583 C CG1 . ILE A 1 266  ? 193.301 169.825 173.224 1.00 0.29  ? 216 ILE A CG1 1 
ATOM 1584 C CG2 . ILE A 1 266  ? 194.148 169.551 170.864 1.00 13.39 ? 216 ILE A CG2 1 
ATOM 1585 C CD1 . ILE A 1 266  ? 193.840 168.515 173.745 1.00 0.00  ? 216 ILE A CD1 1 
ATOM 1586 N N   . GLY A 1 267  ? 191.295 170.308 169.169 1.00 1.41  ? 217 GLY A N   1 
ATOM 1587 C CA  . GLY A 1 267  ? 191.078 170.377 167.731 1.00 8.31  ? 217 GLY A CA  1 
ATOM 1588 C C   . GLY A 1 267  ? 192.336 170.320 166.892 1.00 17.27 ? 217 GLY A C   1 
ATOM 1589 O O   . GLY A 1 267  ? 192.394 170.943 165.824 1.00 17.14 ? 217 GLY A O   1 
ATOM 1590 N N   . CYS A 1 268  ? 193.342 169.591 167.345 1.00 15.51 ? 218 CYS A N   1 
ATOM 1591 C CA  . CYS A 1 268  ? 194.571 169.465 166.571 1.00 16.92 ? 218 CYS A CA  1 
ATOM 1592 C C   . CYS A 1 268  ? 194.360 168.492 165.416 1.00 21.28 ? 218 CYS A C   1 
ATOM 1593 O O   . CYS A 1 268  ? 193.803 167.409 165.622 1.00 23.65 ? 218 CYS A O   1 
ATOM 1594 C CB  . CYS A 1 268  ? 195.718 168.988 167.456 1.00 10.13 ? 218 CYS A CB  1 
ATOM 1595 S SG  . CYS A 1 268  ? 197.248 168.639 166.569 1.00 17.39 ? 218 CYS A SG  1 
ATOM 1596 N N   . PRO A 1 269  ? 194.777 168.841 164.194 1.00 17.27 ? 219 PRO A N   1 
ATOM 1597 C CA  . PRO A 1 269  ? 194.645 167.902 163.070 1.00 17.91 ? 219 PRO A CA  1 
ATOM 1598 C C   . PRO A 1 269  ? 195.461 166.631 163.231 1.00 19.71 ? 219 PRO A C   1 
ATOM 1599 O O   . PRO A 1 269  ? 195.134 165.622 162.596 1.00 22.88 ? 219 PRO A O   1 
ATOM 1600 C CB  . PRO A 1 269  ? 195.140 168.725 161.873 1.00 12.62 ? 219 PRO A CB  1 
ATOM 1601 C CG  . PRO A 1 269  ? 196.061 169.721 162.466 1.00 11.64 ? 219 PRO A CG  1 
ATOM 1602 C CD  . PRO A 1 269  ? 195.497 170.066 163.812 1.00 9.69  ? 219 PRO A CD  1 
ATOM 1603 N N   . LEU A 1 270  ? 196.508 166.647 164.055 1.00 17.66 ? 220 LEU A N   1 
ATOM 1604 C CA  . LEU A 1 270  ? 197.319 165.457 164.308 1.00 16.69 ? 220 LEU A CA  1 
ATOM 1605 C C   . LEU A 1 270  ? 196.573 164.552 165.288 1.00 16.20 ? 220 LEU A C   1 
ATOM 1606 O O   . LEU A 1 270  ? 196.793 164.563 166.499 1.00 17.14 ? 220 LEU A O   1 
ATOM 1607 C CB  . LEU A 1 270  ? 198.692 165.854 164.835 1.00 19.40 ? 220 LEU A CB  1 
ATOM 1608 C CG  . LEU A 1 270  ? 199.615 166.597 163.867 1.00 19.72 ? 220 LEU A CG  1 
ATOM 1609 C CD1 . LEU A 1 270  ? 201.024 166.689 164.432 1.00 14.63 ? 220 LEU A CD1 1 
ATOM 1610 C CD2 . LEU A 1 270  ? 199.623 165.926 162.502 1.00 18.78 ? 220 LEU A CD2 1 
ATOM 1611 N N   . THR A 1 271  ? 195.663 163.758 164.723 1.00 19.36 ? 221 THR A N   1 
ATOM 1612 C CA  . THR A 1 271  ? 194.747 162.911 165.482 1.00 21.20 ? 221 THR A CA  1 
ATOM 1613 C C   . THR A 1 271  ? 195.473 161.996 166.469 1.00 24.56 ? 221 THR A C   1 
ATOM 1614 O O   . THR A 1 271  ? 194.998 161.837 167.601 1.00 27.02 ? 221 THR A O   1 
ATOM 1615 C CB  . THR A 1 271  ? 193.868 162.090 164.531 1.00 24.10 ? 221 THR A CB  1 
ATOM 1616 O OG1 . THR A 1 271  ? 193.259 162.962 163.571 1.00 25.74 ? 221 THR A OG1 1 
ATOM 1617 C CG2 . THR A 1 271  ? 192.779 161.363 165.305 1.00 22.63 ? 221 THR A CG2 1 
ATOM 1618 N N   . PRO A 1 272  ? 196.606 161.356 166.101 1.00 25.64 ? 222 PRO A N   1 
ATOM 1619 C CA  . PRO A 1 272  ? 197.386 160.650 167.128 1.00 25.94 ? 222 PRO A CA  1 
ATOM 1620 C C   . PRO A 1 272  ? 197.901 161.596 168.203 1.00 23.47 ? 222 PRO A C   1 
ATOM 1621 O O   . PRO A 1 272  ? 198.690 162.500 167.913 1.00 23.49 ? 222 PRO A O   1 
ATOM 1622 C CB  . PRO A 1 272  ? 198.537 160.024 166.330 1.00 22.54 ? 222 PRO A CB  1 
ATOM 1623 C CG  . PRO A 1 272  ? 197.995 159.868 164.964 1.00 22.17 ? 222 PRO A CG  1 
ATOM 1624 C CD  . PRO A 1 272  ? 197.117 161.062 164.748 1.00 21.36 ? 222 PRO A CD  1 
ATOM 1625 N N   . LEU A 1 273  ? 197.458 161.402 169.446 1.00 17.90 ? 223 LEU A N   1 
ATOM 1626 C CA  . LEU A 1 273  ? 197.828 162.284 170.540 1.00 19.47 ? 223 LEU A CA  1 
ATOM 1627 C C   . LEU A 1 273  ? 198.305 161.482 171.742 1.00 21.15 ? 223 LEU A C   1 
ATOM 1628 O O   . LEU A 1 273  ? 197.825 160.367 171.981 1.00 18.81 ? 223 LEU A O   1 
ATOM 1629 C CB  . LEU A 1 273  ? 196.645 163.170 170.958 1.00 20.07 ? 223 LEU A CB  1 
ATOM 1630 C CG  . LEU A 1 273  ? 195.869 163.873 169.847 1.00 17.21 ? 223 LEU A CG  1 
ATOM 1631 C CD1 . LEU A 1 273  ? 194.394 163.956 170.197 1.00 18.01 ? 223 LEU A CD1 1 
ATOM 1632 C CD2 . LEU A 1 273  ? 196.442 165.259 169.608 1.00 20.23 ? 223 LEU A CD2 1 
ATOM 1633 N N   . PRO A 1 274  ? 199.245 162.022 172.516 1.00 22.32 ? 224 PRO A N   1 
ATOM 1634 C CA  . PRO A 1 274  ? 199.646 161.352 173.747 1.00 18.84 ? 224 PRO A CA  1 
ATOM 1635 C C   . PRO A 1 274  ? 198.530 161.403 174.764 1.00 17.79 ? 224 PRO A C   1 
ATOM 1636 O O   . PRO A 1 274  ? 197.641 162.275 174.699 1.00 14.15 ? 224 PRO A O   1 
ATOM 1637 C CB  . PRO A 1 274  ? 200.868 162.161 174.208 1.00 18.22 ? 224 PRO A CB  1 
ATOM 1638 C CG  . PRO A 1 274  ? 201.319 162.916 173.003 1.00 22.59 ? 224 PRO A CG  1 
ATOM 1639 C CD  . PRO A 1 274  ? 200.075 163.204 172.235 1.00 23.98 ? 224 PRO A CD  1 
ATOM 1640 N N   . PRO A 1 275  ? 198.517 160.477 175.723 1.00 14.35 ? 225 PRO A N   1 
ATOM 1641 C CA  . PRO A 1 275  ? 197.493 160.519 176.772 1.00 8.84  ? 225 PRO A CA  1 
ATOM 1642 C C   . PRO A 1 275  ? 197.590 161.798 177.590 1.00 9.43  ? 225 PRO A C   1 
ATOM 1643 O O   . PRO A 1 275  ? 198.678 162.323 177.838 1.00 7.44  ? 225 PRO A O   1 
ATOM 1644 C CB  . PRO A 1 275  ? 197.806 159.281 177.620 1.00 8.58  ? 225 PRO A CB  1 
ATOM 1645 C CG  . PRO A 1 275  ? 198.562 158.377 176.697 1.00 10.47 ? 225 PRO A CG  1 
ATOM 1646 C CD  . PRO A 1 275  ? 199.394 159.303 175.864 1.00 10.83 ? 225 PRO A CD  1 
ATOM 1647 N N   . VAL A 1 276  ? 196.431 162.276 178.052 1.00 5.88  ? 226 VAL A N   1 
ATOM 1648 C CA  . VAL A 1 276  ? 196.391 163.514 178.884 1.00 0.00  ? 226 VAL A CA  1 
ATOM 1649 C C   . VAL A 1 276  ? 196.555 163.120 180.356 1.00 5.34  ? 226 VAL A C   1 
ATOM 1650 O O   . VAL A 1 276  ? 195.790 162.250 180.817 1.00 12.46 ? 226 VAL A O   1 
ATOM 1651 C CB  . VAL A 1 276  ? 195.074 164.276 178.650 1.00 0.00  ? 226 VAL A CB  1 
ATOM 1652 C CG1 . VAL A 1 276  ? 194.851 165.371 179.680 1.00 9.72  ? 226 VAL A CG1 1 
ATOM 1653 C CG2 . VAL A 1 276  ? 194.990 164.833 177.237 1.00 0.89  ? 226 VAL A CG2 1 
ATOM 1654 N N   . SER A 1 277  ? 197.517 163.727 181.059 1.00 1.98  ? 227 SER A N   1 
ATOM 1655 C CA  . SER A 1 277  ? 197.700 163.450 182.509 1.00 0.00  ? 227 SER A CA  1 
ATOM 1656 C C   . SER A 1 277  ? 196.486 163.975 183.282 1.00 4.17  ? 227 SER A C   1 
ATOM 1657 O O   . SER A 1 277  ? 196.007 165.075 182.944 1.00 9.61  ? 227 SER A O   1 
ATOM 1658 C CB  . SER A 1 277  ? 198.978 164.056 183.024 1.00 0.82  ? 227 SER A CB  1 
ATOM 1659 O OG  . SER A 1 277  ? 199.065 163.920 184.435 1.00 0.60  ? 227 SER A OG  1 
ATOM 1660 N N   . ILE A 1 278  ? 196.012 163.222 184.280 1.00 0.00  ? 228 ILE A N   1 
ATOM 1661 C CA  . ILE A 1 278  ? 194.776 163.633 185.013 1.00 0.00  ? 228 ILE A CA  1 
ATOM 1662 C C   . ILE A 1 278  ? 195.038 163.657 186.523 1.00 4.67  ? 228 ILE A C   1 
ATOM 1663 O O   . ILE A 1 278  ? 195.638 162.688 187.030 1.00 14.70 ? 228 ILE A O   1 
ATOM 1664 C CB  . ILE A 1 278  ? 193.599 162.698 184.671 1.00 0.00  ? 228 ILE A CB  1 
ATOM 1665 C CG1 . ILE A 1 278  ? 193.326 162.646 183.165 1.00 0.00  ? 228 ILE A CG1 1 
ATOM 1666 C CG2 . ILE A 1 278  ? 192.360 163.097 185.456 1.00 0.00  ? 228 ILE A CG2 1 
ATOM 1667 C CD1 . ILE A 1 278  ? 193.150 161.247 182.623 1.00 1.94  ? 228 ILE A CD1 1 
ATOM 1668 N N   . ALA A 1 279  ? 194.597 164.718 187.209 1.00 3.38  ? 229 ALA A N   1 
ATOM 1669 C CA  . ALA A 1 279  ? 194.723 164.786 188.685 1.00 5.99  ? 229 ALA A CA  1 
ATOM 1670 C C   . ALA A 1 279  ? 193.316 164.715 189.288 1.00 2.31  ? 229 ALA A C   1 
ATOM 1671 O O   . ALA A 1 279  ? 192.513 165.626 189.005 1.00 12.37 ? 229 ALA A O   1 
ATOM 1672 C CB  . ALA A 1 279  ? 195.438 166.051 189.087 1.00 0.00  ? 229 ALA A CB  1 
ATOM 1673 N N   . ILE A 1 280  ? 193.025 163.678 190.080 1.00 0.00  ? 230 ILE A N   1 
ATOM 1674 C CA  . ILE A 1 280  ? 191.638 163.495 190.608 1.00 0.00  ? 230 ILE A CA  1 
ATOM 1675 C C   . ILE A 1 280  ? 191.591 163.876 192.091 1.00 0.00  ? 230 ILE A C   1 
ATOM 1676 O O   . ILE A 1 280  ? 192.535 163.519 192.823 1.00 7.93  ? 230 ILE A O   1 
ATOM 1677 C CB  . ILE A 1 280  ? 191.158 162.048 190.381 1.00 0.00  ? 230 ILE A CB  1 
ATOM 1678 C CG1 . ILE A 1 280  ? 191.003 161.732 188.891 1.00 1.56  ? 230 ILE A CG1 1 
ATOM 1679 C CG2 . ILE A 1 280  ? 189.876 161.774 191.153 1.00 0.00  ? 230 ILE A CG2 1 
ATOM 1680 C CD1 . ILE A 1 280  ? 190.793 160.268 188.596 1.00 0.99  ? 230 ILE A CD1 1 
ATOM 1681 N N   . ARG A 1 281  ? 190.528 164.571 192.512 1.00 3.69  ? 231 ARG A N   1 
ATOM 1682 C CA  . ARG A 1 281  ? 190.365 164.950 193.942 1.00 4.25  ? 231 ARG A CA  1 
ATOM 1683 C C   . ARG A 1 281  ? 188.878 164.886 194.308 1.00 2.19  ? 231 ARG A C   1 
ATOM 1684 O O   . ARG A 1 281  ? 188.064 165.457 193.556 1.00 19.30 ? 231 ARG A O   1 
ATOM 1685 C CB  . ARG A 1 281  ? 190.933 166.350 194.191 1.00 3.41  ? 231 ARG A CB  1 
ATOM 1686 C CG  . ARG A 1 281  ? 190.730 166.861 195.609 1.00 0.00  ? 231 ARG A CG  1 
ATOM 1687 C CD  . ARG A 1 281  ? 190.578 168.369 195.644 1.00 0.82  ? 231 ARG A CD  1 
ATOM 1688 N NE  . ARG A 1 281  ? 190.715 168.912 196.987 1.00 6.16  ? 231 ARG A NE  1 
ATOM 1689 C CZ  . ARG A 1 281  ? 189.710 169.395 197.706 1.00 7.57  ? 231 ARG A CZ  1 
ATOM 1690 N NH1 . ARG A 1 281  ? 188.474 169.327 197.244 1.00 0.00  ? 231 ARG A NH1 1 
ATOM 1691 N NH2 . ARG A 1 281  ? 189.943 169.945 198.885 1.00 11.45 ? 231 ARG A NH2 1 
ATOM 1692 N N   . PHE A 1 282  ? 188.543 164.216 195.416 1.00 0.00  ? 232 PHE A N   1 
ATOM 1693 C CA  . PHE A 1 282  ? 187.126 164.080 195.847 1.00 0.00  ? 232 PHE A CA  1 
ATOM 1694 C C   . PHE A 1 282  ? 186.932 164.796 197.187 1.00 7.67  ? 232 PHE A C   1 
ATOM 1695 O O   . PHE A 1 282  ? 187.910 164.899 197.953 1.00 21.36 ? 232 PHE A O   1 
ATOM 1696 C CB  . PHE A 1 282  ? 186.733 162.604 195.945 1.00 0.72  ? 232 PHE A CB  1 
ATOM 1697 C CG  . PHE A 1 282  ? 186.202 162.005 194.667 1.00 4.69  ? 232 PHE A CG  1 
ATOM 1698 C CD1 . PHE A 1 282  ? 186.371 162.653 193.454 1.00 4.90  ? 232 PHE A CD1 1 
ATOM 1699 C CD2 . PHE A 1 282  ? 185.533 160.792 194.676 1.00 6.33  ? 232 PHE A CD2 1 
ATOM 1700 C CE1 . PHE A 1 282  ? 185.884 162.101 192.280 1.00 0.13  ? 232 PHE A CE1 1 
ATOM 1701 C CE2 . PHE A 1 282  ? 185.045 160.242 193.502 1.00 2.74  ? 232 PHE A CE2 1 
ATOM 1702 C CZ  . PHE A 1 282  ? 185.220 160.898 192.306 1.00 0.00  ? 232 PHE A CZ  1 
ATOM 1703 N N   . THR A 1 283  ? 185.713 165.274 197.457 1.00 9.07  ? 233 THR A N   1 
ATOM 1704 C CA  . THR A 1 283  ? 185.444 166.026 198.713 1.00 14.67 ? 233 THR A CA  1 
ATOM 1705 C C   . THR A 1 283  ? 184.187 165.475 199.396 1.00 16.78 ? 233 THR A C   1 
ATOM 1706 O O   . THR A 1 283  ? 183.113 165.524 198.768 1.00 13.74 ? 233 THR A O   1 
ATOM 1707 C CB  . THR A 1 283  ? 185.305 167.529 198.440 1.00 9.85  ? 233 THR A CB  1 
ATOM 1708 O OG1 . THR A 1 283  ? 186.280 167.901 197.464 1.00 8.17  ? 233 THR A OG1 1 
ATOM 1709 C CG2 . THR A 1 283  ? 185.480 168.369 199.685 1.00 12.02 ? 233 THR A CG2 1 
ATOM 1710 N N   . TYR A 1 284  ? 184.320 164.987 200.633 1.00 12.12 ? 234 TYR A N   1 
ATOM 1711 C CA  . TYR A 1 284  ? 183.182 164.449 201.369 1.00 10.12 ? 234 TYR A CA  1 
ATOM 1712 C C   . TYR A 1 284  ? 182.950 165.295 202.613 1.00 13.70 ? 234 TYR A C   1 
ATOM 1713 O O   . TYR A 1 284  ? 183.903 165.791 203.221 1.00 17.41 ? 234 TYR A O   1 
ATOM 1714 C CB  . TYR A 1 284  ? 183.414 162.990 201.790 1.00 9.01  ? 234 TYR A CB  1 
ATOM 1715 C CG  . TYR A 1 284  ? 183.928 162.085 200.696 1.00 15.52 ? 234 TYR A CG  1 
ATOM 1716 C CD1 . TYR A 1 284  ? 185.287 161.982 200.433 1.00 7.76  ? 234 TYR A CD1 1 
ATOM 1717 C CD2 . TYR A 1 284  ? 183.056 161.318 199.939 1.00 21.97 ? 234 TYR A CD2 1 
ATOM 1718 C CE1 . TYR A 1 284  ? 185.760 161.153 199.439 1.00 4.11  ? 234 TYR A CE1 1 
ATOM 1719 C CE2 . TYR A 1 284  ? 183.521 160.487 198.943 1.00 22.44 ? 234 TYR A CE2 1 
ATOM 1720 C CZ  . TYR A 1 284  ? 184.873 160.408 198.698 1.00 17.50 ? 234 TYR A CZ  1 
ATOM 1721 O OH  . TYR A 1 284  ? 185.337 159.579 197.705 1.00 24.57 ? 234 TYR A OH  1 
ATOM 1722 N N   . VAL A 1 285  ? 181.670 165.469 202.964 1.00 19.60 ? 235 VAL A N   1 
ATOM 1723 C CA  . VAL A 1 285  ? 181.309 166.308 204.145 1.00 21.85 ? 235 VAL A CA  1 
ATOM 1724 C C   . VAL A 1 285  ? 180.449 165.484 205.108 1.00 20.17 ? 235 VAL A C   1 
ATOM 1725 O O   . VAL A 1 285  ? 179.444 164.906 204.652 1.00 22.31 ? 235 VAL A O   1 
ATOM 1726 C CB  . VAL A 1 285  ? 180.589 167.604 203.725 1.00 22.05 ? 235 VAL A CB  1 
ATOM 1727 C CG1 . VAL A 1 285  ? 180.584 168.631 204.846 1.00 18.49 ? 235 VAL A CG1 1 
ATOM 1728 C CG2 . VAL A 1 285  ? 181.182 168.199 202.456 1.00 17.97 ? 235 VAL A CG2 1 
ATOM 1729 N N   . LEU A 1 286  ? 180.833 165.436 206.384 1.00 20.41 ? 236 LEU A N   1 
ATOM 1730 C CA  . LEU A 1 286  ? 180.097 164.713 207.413 1.00 22.63 ? 236 LEU A CA  1 
ATOM 1731 C C   . LEU A 1 286  ? 179.674 165.686 208.504 1.00 25.59 ? 236 LEU A C   1 
ATOM 1732 O O   . LEU A 1 286  ? 180.516 166.380 209.081 1.00 24.01 ? 236 LEU A O   1 
ATOM 1733 C CB  . LEU A 1 286  ? 180.945 163.579 208.000 1.00 22.42 ? 236 LEU A CB  1 
ATOM 1734 C CG  . LEU A 1 286  ? 180.369 162.777 209.170 1.00 24.13 ? 236 LEU A CG  1 
ATOM 1735 C CD1 . LEU A 1 286  ? 180.568 161.289 208.940 1.00 25.60 ? 236 LEU A CD1 1 
ATOM 1736 C CD2 . LEU A 1 286  ? 181.013 163.198 210.478 1.00 21.78 ? 236 LEU A CD2 1 
ATOM 1737 N N   . GLN A 1 287  ? 178.374 165.731 208.789 1.00 33.59 ? 237 GLN A N   1 
ATOM 1738 C CA  . GLN A 1 287  ? 177.820 166.648 209.779 1.00 35.08 ? 237 GLN A CA  1 
ATOM 1739 C C   . GLN A 1 287  ? 177.343 165.954 211.045 1.00 34.70 ? 237 GLN A C   1 
ATOM 1740 O O   . GLN A 1 287  ? 177.605 166.445 212.146 1.00 30.18 ? 237 GLN A O   1 
ATOM 1741 C CB  . GLN A 1 287  ? 176.660 167.444 209.166 1.00 33.05 ? 237 GLN A CB  1 
ATOM 1742 C CG  . GLN A 1 287  ? 175.457 166.604 208.753 1.00 32.20 ? 237 GLN A CG  1 
ATOM 1743 C CD  . GLN A 1 287  ? 174.340 167.435 208.154 1.00 33.26 ? 237 GLN A CD  1 
ATOM 1744 O OE1 . GLN A 1 287  ? 174.559 168.559 207.702 1.00 31.18 ? 237 GLN A OE1 1 
ATOM 1745 N NE2 . GLN A 1 287  ? 173.131 166.885 208.149 1.00 32.39 ? 237 GLN A NE2 1 
ATOM 1746 N N   . ASP A 1 288  ? 176.647 164.828 210.920 1.00 32.54 ? 238 ASP A N   1 
ATOM 1747 C CA  . ASP A 1 288  ? 176.199 164.089 212.092 1.00 32.95 ? 238 ASP A CA  1 
ATOM 1748 C C   . ASP A 1 288  ? 177.389 163.492 212.831 1.00 31.70 ? 238 ASP A C   1 
ATOM 1749 O O   . ASP A 1 288  ? 178.345 163.012 212.218 1.00 34.32 ? 238 ASP A O   1 
ATOM 1750 C CB  . ASP A 1 288  ? 175.227 162.983 211.680 1.00 33.41 ? 238 ASP A CB  1 
ATOM 1751 C CG  . ASP A 1 288  ? 173.884 163.523 211.227 1.00 36.39 ? 238 ASP A CG  1 
ATOM 1752 O OD1 . ASP A 1 288  ? 173.594 164.709 211.492 1.00 33.88 ? 238 ASP A OD1 1 
ATOM 1753 O OD2 . ASP A 1 288  ? 173.116 162.759 210.607 1.00 37.43 ? 238 ASP A OD2 1 
ATOM 1754 N N   . TRP A 1 289  ? 177.328 163.524 214.162 1.00 29.00 ? 239 TRP A N   1 
ATOM 1755 C CA  . TRP A 1 289  ? 178.391 162.982 215.001 1.00 30.50 ? 239 TRP A CA  1 
ATOM 1756 C C   . TRP A 1 289  ? 177.940 161.777 215.817 1.00 33.77 ? 239 TRP A C   1 
ATOM 1757 O O   . TRP A 1 289  ? 178.691 161.319 216.688 1.00 31.79 ? 239 TRP A O   1 
ATOM 1758 C CB  . TRP A 1 289  ? 178.940 164.069 215.928 1.00 27.16 ? 239 TRP A CB  1 
ATOM 1759 C CG  . TRP A 1 289  ? 179.220 165.359 215.224 1.00 31.55 ? 239 TRP A CG  1 
ATOM 1760 C CD1 . TRP A 1 289  ? 178.501 166.515 215.311 1.00 32.32 ? 239 TRP A CD1 1 
ATOM 1761 C CD2 . TRP A 1 289  ? 180.301 165.625 214.324 1.00 34.98 ? 239 TRP A CD2 1 
ATOM 1762 N NE1 . TRP A 1 289  ? 179.067 167.485 214.519 1.00 32.65 ? 239 TRP A NE1 1 
ATOM 1763 C CE2 . TRP A 1 289  ? 180.174 166.963 213.903 1.00 33.63 ? 239 TRP A CE2 1 
ATOM 1764 C CE3 . TRP A 1 289  ? 181.365 164.863 213.833 1.00 31.04 ? 239 TRP A CE3 1 
ATOM 1765 C CZ2 . TRP A 1 289  ? 181.069 167.553 213.016 1.00 27.03 ? 239 TRP A CZ2 1 
ATOM 1766 C CZ3 . TRP A 1 289  ? 182.251 165.451 212.953 1.00 29.43 ? 239 TRP A CZ3 1 
ATOM 1767 C CH2 . TRP A 1 289  ? 182.098 166.782 212.553 1.00 27.90 ? 239 TRP A CH2 1 
ATOM 1768 N N   . GLN A 1 290  ? 176.741 161.252 215.555 1.00 36.01 ? 240 GLN A N   1 
ATOM 1769 C CA  . GLN A 1 290  ? 176.186 160.086 216.251 1.00 34.32 ? 240 GLN A CA  1 
ATOM 1770 C C   . GLN A 1 290  ? 176.149 160.394 217.744 1.00 35.01 ? 240 GLN A C   1 
ATOM 1771 O O   . GLN A 1 290  ? 175.449 161.342 218.140 1.00 37.39 ? 240 GLN A O   1 
ATOM 1772 C CB  . GLN A 1 290  ? 176.979 158.841 215.842 1.00 32.70 ? 240 GLN A CB  1 
ATOM 1773 C CG  . GLN A 1 290  ? 176.321 157.519 216.219 1.00 32.37 ? 240 GLN A CG  1 
ATOM 1774 C CD  . GLN A 1 290  ? 174.818 157.528 216.019 1.00 39.00 ? 240 GLN A CD  1 
ATOM 1775 O OE1 . GLN A 1 290  ? 174.321 157.868 214.944 1.00 42.35 ? 240 GLN A OE1 1 
ATOM 1776 N NE2 . GLN A 1 290  ? 174.083 157.153 217.059 1.00 36.25 ? 240 GLN A NE2 1 
ATOM 1777 N N   . GLN A 1 291  ? 176.859 159.657 218.592 1.00 32.72 ? 241 GLN A N   1 
ATOM 1778 C CA  . GLN A 1 291  ? 176.828 159.893 220.030 1.00 34.46 ? 241 GLN A CA  1 
ATOM 1779 C C   . GLN A 1 291  ? 177.639 161.129 220.402 1.00 33.63 ? 241 GLN A C   1 
ATOM 1780 O O   . GLN A 1 291  ? 178.869 161.118 220.341 1.00 33.36 ? 241 GLN A O   1 
ATOM 1781 C CB  . GLN A 1 291  ? 177.355 158.670 220.783 1.00 31.95 ? 241 GLN A CB  1 
ATOM 1782 C CG  . GLN A 1 291  ? 176.840 157.341 220.251 1.00 32.62 ? 241 GLN A CG  1 
ATOM 1783 C CD  . GLN A 1 291  ? 177.923 156.518 219.580 1.00 33.73 ? 241 GLN A CD  1 
ATOM 1784 O OE1 . GLN A 1 291  ? 178.544 156.959 218.613 1.00 35.72 ? 241 GLN A OE1 1 
ATOM 1785 N NE2 . GLN A 1 291  ? 178.155 155.316 220.092 1.00 32.76 ? 241 GLN A NE2 1 
ATOM 1786 N N   . PHE A 1 314  ? 181.652 177.152 247.847 1.00 35.62 ? 264 PHE A N   1 
ATOM 1787 C CA  . PHE A 1 314  ? 180.690 177.683 246.889 1.00 37.76 ? 264 PHE A CA  1 
ATOM 1788 C C   . PHE A 1 314  ? 181.357 178.655 245.927 1.00 39.08 ? 264 PHE A C   1 
ATOM 1789 O O   . PHE A 1 314  ? 182.584 178.734 245.863 1.00 38.47 ? 264 PHE A O   1 
ATOM 1790 C CB  . PHE A 1 314  ? 179.533 178.372 247.614 1.00 35.85 ? 264 PHE A CB  1 
ATOM 1791 C CG  . PHE A 1 314  ? 179.133 177.697 248.892 1.00 39.21 ? 264 PHE A CG  1 
ATOM 1792 C CD1 . PHE A 1 314  ? 178.512 176.458 248.869 1.00 37.84 ? 264 PHE A CD1 1 
ATOM 1793 C CD2 . PHE A 1 314  ? 179.376 178.298 250.115 1.00 36.32 ? 264 PHE A CD2 1 
ATOM 1794 C CE1 . PHE A 1 314  ? 178.142 175.831 250.043 1.00 37.50 ? 264 PHE A CE1 1 
ATOM 1795 C CE2 . PHE A 1 314  ? 179.008 177.676 251.293 1.00 35.98 ? 264 PHE A CE2 1 
ATOM 1796 C CZ  . PHE A 1 314  ? 178.390 176.441 251.257 1.00 38.22 ? 264 PHE A CZ  1 
ATOM 1797 N N   . GLY A 1 315  ? 180.540 179.398 245.184 1.00 36.55 ? 265 GLY A N   1 
ATOM 1798 C CA  . GLY A 1 315  ? 181.058 180.359 244.231 1.00 36.11 ? 265 GLY A CA  1 
ATOM 1799 C C   . GLY A 1 315  ? 181.873 179.720 243.127 1.00 33.58 ? 265 GLY A C   1 
ATOM 1800 O O   . GLY A 1 315  ? 182.977 180.177 242.818 1.00 33.01 ? 265 GLY A O   1 
ATOM 1801 N N   . LYS A 1 316  ? 181.336 178.635 242.560 1.00 30.64 ? 266 LYS A N   1 
ATOM 1802 C CA  . LYS A 1 316  ? 182.054 177.901 241.484 1.00 30.78 ? 266 LYS A CA  1 
ATOM 1803 C C   . LYS A 1 316  ? 181.656 178.488 240.128 1.00 31.58 ? 266 LYS A C   1 
ATOM 1804 O O   . LYS A 1 316  ? 180.467 178.388 239.766 1.00 30.41 ? 266 LYS A O   1 
ATOM 1805 C CB  . LYS A 1 316  ? 181.730 176.406 241.556 1.00 30.75 ? 266 LYS A CB  1 
ATOM 1806 C CG  . LYS A 1 316  ? 181.892 175.776 242.933 1.00 32.08 ? 266 LYS A CG  1 
ATOM 1807 C CD  . LYS A 1 316  ? 183.287 175.934 243.499 1.00 30.98 ? 266 LYS A CD  1 
ATOM 1808 C CE  . LYS A 1 316  ? 183.397 175.485 244.940 1.00 29.01 ? 266 LYS A CE  1 
ATOM 1809 N NZ  . LYS A 1 316  ? 184.167 176.452 245.757 1.00 27.63 ? 266 LYS A NZ  1 
ATOM 1810 N N   . LEU A 1 317  ? 182.619 179.073 239.413 1.00 32.08 ? 267 LEU A N   1 
ATOM 1811 C CA  . LEU A 1 317  ? 182.342 179.682 238.088 1.00 33.39 ? 267 LEU A CA  1 
ATOM 1812 C C   . LEU A 1 317  ? 181.840 178.577 237.158 1.00 30.09 ? 267 LEU A C   1 
ATOM 1813 O O   . LEU A 1 317  ? 182.489 177.519 237.085 1.00 28.73 ? 267 LEU A O   1 
ATOM 1814 C CB  . LEU A 1 317  ? 183.626 180.321 237.550 1.00 31.02 ? 267 LEU A CB  1 
ATOM 1815 C CG  . LEU A 1 317  ? 183.690 181.845 237.644 1.00 29.90 ? 267 LEU A CG  1 
ATOM 1816 C CD1 . LEU A 1 317  ? 182.787 182.492 236.605 1.00 28.34 ? 267 LEU A CD1 1 
ATOM 1817 C CD2 . LEU A 1 317  ? 183.318 182.320 239.040 1.00 26.77 ? 267 LEU A CD2 1 
ATOM 1818 N N   . PRO A 1 318  ? 180.705 178.768 236.457 1.00 27.70 ? 268 PRO A N   1 
ATOM 1819 C CA  . PRO A 1 318  ? 180.211 177.771 235.503 1.00 32.63 ? 268 PRO A CA  1 
ATOM 1820 C C   . PRO A 1 318  ? 180.893 177.904 234.151 1.00 32.61 ? 268 PRO A C   1 
ATOM 1821 O O   . PRO A 1 318  ? 180.741 178.917 233.462 1.00 29.52 ? 268 PRO A O   1 
ATOM 1822 C CB  . PRO A 1 318  ? 178.711 178.074 235.427 1.00 33.31 ? 268 PRO A CB  1 
ATOM 1823 C CG  . PRO A 1 318  ? 178.574 179.514 235.843 1.00 27.60 ? 268 PRO A CG  1 
ATOM 1824 C CD  . PRO A 1 318  ? 179.858 179.969 236.490 1.00 24.92 ? 268 PRO A CD  1 
ATOM 1825 N N   . PHE A 1 319  ? 181.643 176.871 233.757 1.00 33.49 ? 269 PHE A N   1 
ATOM 1826 C CA  . PHE A 1 319  ? 182.379 176.919 232.465 1.00 35.03 ? 269 PHE A CA  1 
ATOM 1827 C C   . PHE A 1 319  ? 181.907 175.777 231.557 1.00 31.17 ? 269 PHE A C   1 
ATOM 1828 O O   . PHE A 1 319  ? 181.582 174.694 232.083 1.00 31.18 ? 269 PHE A O   1 
ATOM 1829 C CB  . PHE A 1 319  ? 183.889 176.857 232.714 1.00 35.08 ? 269 PHE A CB  1 
ATOM 1830 C CG  . PHE A 1 319  ? 184.691 176.219 231.608 1.00 32.05 ? 269 PHE A CG  1 
ATOM 1831 C CD1 . PHE A 1 319  ? 185.058 176.947 230.487 1.00 31.32 ? 269 PHE A CD1 1 
ATOM 1832 C CD2 . PHE A 1 319  ? 185.080 174.892 231.687 1.00 29.40 ? 269 PHE A CD2 1 
ATOM 1833 C CE1 . PHE A 1 319  ? 185.793 176.359 229.469 1.00 33.02 ? 269 PHE A CE1 1 
ATOM 1834 C CE2 . PHE A 1 319  ? 185.814 174.305 230.669 1.00 28.86 ? 269 PHE A CE2 1 
ATOM 1835 C CZ  . PHE A 1 319  ? 186.170 175.040 229.563 1.00 33.43 ? 269 PHE A CZ  1 
ATOM 1836 N N   . GLY A 1 320  ? 181.872 176.011 230.240 1.00 26.85 ? 270 GLY A N   1 
ATOM 1837 C CA  . GLY A 1 320  ? 181.488 174.950 229.287 1.00 28.32 ? 270 GLY A CA  1 
ATOM 1838 C C   . GLY A 1 320  ? 180.643 175.483 228.143 1.00 31.38 ? 270 GLY A C   1 
ATOM 1839 O O   . GLY A 1 320  ? 179.940 176.488 228.351 1.00 29.66 ? 270 GLY A O   1 
ATOM 1840 N N   . ALA A 1 321  ? 180.645 174.713 227.041 1.00 32.14 ? 271 ALA A N   1 
ATOM 1841 C CA  . ALA A 1 321  ? 179.889 175.080 225.824 1.00 29.93 ? 271 ALA A CA  1 
ATOM 1842 C C   . ALA A 1 321  ? 178.668 174.186 225.640 1.00 31.54 ? 271 ALA A C   1 
ATOM 1843 O O   . ALA A 1 321  ? 178.834 172.953 225.573 1.00 30.97 ? 271 ALA A O   1 
ATOM 1844 C CB  . ALA A 1 321  ? 180.800 175.011 224.621 1.00 29.30 ? 271 ALA A CB  1 
ATOM 1845 N N   . CYS A 1 322  ? 177.489 174.801 225.566 1.00 36.84 ? 272 CYS A N   1 
ATOM 1846 C CA  . CYS A 1 322  ? 176.286 173.932 225.456 1.00 37.37 ? 272 CYS A CA  1 
ATOM 1847 C C   . CYS A 1 322  ? 176.317 173.153 224.137 1.00 38.24 ? 272 CYS A C   1 
ATOM 1848 O O   . CYS A 1 322  ? 176.361 171.909 224.193 1.00 39.81 ? 272 CYS A O   1 
ATOM 1849 C CB  . CYS A 1 322  ? 175.012 174.765 225.516 1.00 37.42 ? 272 CYS A CB  1 
ATOM 1850 S SG  . CYS A 1 322  ? 174.765 175.592 227.110 1.00 46.07 ? 272 CYS A SG  1 
ATOM 1851 N N   . GLU A 1 323  ? 176.294 173.855 223.001 1.00 36.82 ? 273 GLU A N   1 
ATOM 1852 C CA  . GLU A 1 323  ? 176.258 173.191 221.707 1.00 36.94 ? 273 GLU A CA  1 
ATOM 1853 C C   . GLU A 1 323  ? 177.664 172.785 221.281 1.00 38.17 ? 273 GLU A C   1 
ATOM 1854 O O   . GLU A 1 323  ? 178.666 173.245 221.833 1.00 36.57 ? 273 GLU A O   1 
ATOM 1855 C CB  . GLU A 1 323  ? 175.629 174.100 220.647 1.00 34.79 ? 273 GLU A CB  1 
ATOM 1856 C CG  . GLU A 1 323  ? 174.421 174.880 221.136 1.00 37.50 ? 273 GLU A CG  1 
ATOM 1857 C CD  . GLU A 1 323  ? 174.718 176.354 221.321 1.00 38.24 ? 273 GLU A CD  1 
ATOM 1858 O OE1 . GLU A 1 323  ? 175.909 176.712 221.437 1.00 38.31 ? 273 GLU A OE1 1 
ATOM 1859 O OE2 . GLU A 1 323  ? 173.761 177.155 221.349 1.00 35.29 ? 273 GLU A OE2 1 
ATOM 1860 N N   . ASP A 1 324  ? 177.723 171.911 220.288 1.00 34.22 ? 274 ASP A N   1 
ATOM 1861 C CA  . ASP A 1 324  ? 179.001 171.435 219.774 1.00 31.71 ? 274 ASP A CA  1 
ATOM 1862 C C   . ASP A 1 324  ? 179.714 172.567 219.044 1.00 31.77 ? 274 ASP A C   1 
ATOM 1863 O O   . ASP A 1 324  ? 179.137 173.153 218.119 1.00 30.59 ? 274 ASP A O   1 
ATOM 1864 C CB  . ASP A 1 324  ? 178.778 170.250 218.837 1.00 30.33 ? 274 ASP A CB  1 
ATOM 1865 C CG  . ASP A 1 324  ? 179.961 169.301 218.798 1.00 32.60 ? 274 ASP A CG  1 
ATOM 1866 O OD1 . ASP A 1 324  ? 181.070 169.702 219.205 1.00 32.49 ? 274 ASP A OD1 1 
ATOM 1867 O OD2 . ASP A 1 324  ? 179.779 168.147 218.357 1.00 30.93 ? 274 ASP A OD2 1 
ATOM 1868 N N   . PRO A 1 325  ? 180.946 172.975 219.446 1.00 31.55 ? 275 PRO A N   1 
ATOM 1869 C CA  . PRO A 1 325  ? 181.612 174.119 218.812 1.00 28.90 ? 275 PRO A CA  1 
ATOM 1870 C C   . PRO A 1 325  ? 182.028 173.800 217.369 1.00 32.07 ? 275 PRO A C   1 
ATOM 1871 O O   . PRO A 1 325  ? 182.186 174.726 216.598 1.00 29.62 ? 275 PRO A O   1 
ATOM 1872 C CB  . PRO A 1 325  ? 182.854 174.363 219.682 1.00 25.56 ? 275 PRO A CB  1 
ATOM 1873 C CG  . PRO A 1 325  ? 183.145 173.013 220.289 1.00 24.53 ? 275 PRO A CG  1 
ATOM 1874 C CD  . PRO A 1 325  ? 181.778 172.408 220.524 1.00 27.30 ? 275 PRO A CD  1 
ATOM 1875 N N   . ILE A 1 326  ? 182.197 172.514 217.045 1.00 32.87 ? 276 ILE A N   1 
ATOM 1876 C CA  . ILE A 1 326  ? 182.540 172.113 215.648 1.00 32.91 ? 276 ILE A CA  1 
ATOM 1877 C C   . ILE A 1 326  ? 181.233 171.957 214.863 1.00 31.20 ? 276 ILE A C   1 
ATOM 1878 O O   . ILE A 1 326  ? 180.194 171.684 215.498 1.00 27.77 ? 276 ILE A O   1 
ATOM 1879 C CB  . ILE A 1 326  ? 183.385 170.823 215.634 1.00 28.47 ? 276 ILE A CB  1 
ATOM 1880 C CG1 . ILE A 1 326  ? 182.571 169.600 216.065 1.00 26.03 ? 276 ILE A CG1 1 
ATOM 1881 C CG2 . ILE A 1 326  ? 184.637 170.993 216.480 1.00 30.88 ? 276 ILE A CG2 1 
ATOM 1882 C CD1 . ILE A 1 326  ? 183.342 168.304 216.013 1.00 30.52 ? 276 ILE A CD1 1 
ATOM 1883 N N   . SER A 1 327  ? 181.283 172.131 213.540 1.00 31.00 ? 277 SER A N   1 
ATOM 1884 C CA  . SER A 1 327  ? 180.043 172.072 212.723 1.00 30.92 ? 277 SER A CA  1 
ATOM 1885 C C   . SER A 1 327  ? 180.110 170.907 211.731 1.00 34.57 ? 277 SER A C   1 
ATOM 1886 O O   . SER A 1 327  ? 179.147 170.117 211.691 1.00 35.60 ? 277 SER A O   1 
ATOM 1887 C CB  . SER A 1 327  ? 179.804 173.380 212.016 1.00 29.92 ? 277 SER A CB  1 
ATOM 1888 O OG  . SER A 1 327  ? 178.884 173.213 210.948 1.00 32.76 ? 277 SER A OG  1 
ATOM 1889 N N   . GLU A 1 328  ? 181.200 170.804 210.963 1.00 31.14 ? 278 GLU A N   1 
ATOM 1890 C CA  . GLU A 1 328  ? 181.271 169.751 209.915 1.00 32.76 ? 278 GLU A CA  1 
ATOM 1891 C C   . GLU A 1 328  ? 182.710 169.266 209.725 1.00 28.03 ? 278 GLU A C   1 
ATOM 1892 O O   . GLU A 1 328  ? 183.638 170.059 209.979 1.00 22.23 ? 278 GLU A O   1 
ATOM 1893 C CB  . GLU A 1 328  ? 180.733 170.293 208.590 1.00 31.00 ? 278 GLU A CB  1 
ATOM 1894 C CG  . GLU A 1 328  ? 179.361 169.757 208.233 1.00 28.40 ? 278 GLU A CG  1 
ATOM 1895 C CD  . GLU A 1 328  ? 178.552 170.663 207.322 1.00 29.83 ? 278 GLU A CD  1 
ATOM 1896 O OE1 . GLU A 1 328  ? 179.112 171.669 206.843 1.00 30.29 ? 278 GLU A OE1 1 
ATOM 1897 O OE2 . GLU A 1 328  ? 177.365 170.359 207.092 1.00 29.01 ? 278 GLU A OE2 1 
ATOM 1898 N N   . LEU A 1 329  ? 182.881 168.013 209.292 1.00 18.53 ? 279 LEU A N   1 
ATOM 1899 C CA  . LEU A 1 329  ? 184.209 167.483 209.013 1.00 12.95 ? 279 LEU A CA  1 
ATOM 1900 C C   . LEU A 1 329  ? 184.326 167.217 207.520 1.00 12.47 ? 279 LEU A C   1 
ATOM 1901 O O   . LEU A 1 329  ? 183.494 166.505 206.946 1.00 11.89 ? 279 LEU A O   1 
ATOM 1902 C CB  . LEU A 1 329  ? 184.472 166.198 209.806 1.00 16.74 ? 279 LEU A CB  1 
ATOM 1903 C CG  . LEU A 1 329  ? 185.726 165.397 209.452 1.00 13.95 ? 279 LEU A CG  1 
ATOM 1904 C CD1 . LEU A 1 329  ? 186.875 165.772 210.370 1.00 13.01 ? 279 LEU A CD1 1 
ATOM 1905 C CD2 . LEU A 1 329  ? 185.452 163.905 209.528 1.00 10.61 ? 279 LEU A CD2 1 
ATOM 1906 N N   . HIS A 1 330  ? 185.357 167.785 206.899 1.00 14.49 ? 280 HIS A N   1 
ATOM 1907 C CA  . HIS A 1 330  ? 185.597 167.665 205.467 1.00 10.49 ? 280 HIS A CA  1 
ATOM 1908 C C   . HIS A 1 330  ? 186.768 166.723 205.234 1.00 10.38 ? 280 HIS A C   1 
ATOM 1909 O O   . HIS A 1 330  ? 187.820 166.872 205.864 1.00 16.42 ? 280 HIS A O   1 
ATOM 1910 C CB  . HIS A 1 330  ? 185.900 169.029 204.845 1.00 11.52 ? 280 HIS A CB  1 
ATOM 1911 C CG  . HIS A 1 330  ? 184.763 169.997 204.923 1.00 15.07 ? 280 HIS A CG  1 
ATOM 1912 N ND1 . HIS A 1 330  ? 183.942 170.268 203.850 1.00 13.69 ? 280 HIS A ND1 1 
ATOM 1913 C CD2 . HIS A 1 330  ? 184.299 170.747 205.950 1.00 15.76 ? 280 HIS A CD2 1 
ATOM 1914 C CE1 . HIS A 1 330  ? 183.028 171.151 204.210 1.00 12.00 ? 280 HIS A CE1 1 
ATOM 1915 N NE2 . HIS A 1 330  ? 183.223 171.459 205.479 1.00 19.16 ? 280 HIS A NE2 1 
ATOM 1916 N N   . LEU A 1 331  ? 186.557 165.742 204.349 1.00 6.34  ? 281 LEU A N   1 
ATOM 1917 C CA  . LEU A 1 331  ? 187.615 164.746 204.031 1.00 5.08  ? 281 LEU A CA  1 
ATOM 1918 C C   . LEU A 1 331  ? 187.914 164.813 202.531 1.00 12.31 ? 281 LEU A C   1 
ATOM 1919 O O   . LEU A 1 331  ? 186.985 164.572 201.735 1.00 8.38  ? 281 LEU A O   1 
ATOM 1920 C CB  . LEU A 1 331  ? 187.117 163.355 204.435 1.00 0.00  ? 281 LEU A CB  1 
ATOM 1921 C CG  . LEU A 1 331  ? 188.113 162.211 204.244 1.00 0.19  ? 281 LEU A CG  1 
ATOM 1922 C CD1 . LEU A 1 331  ? 189.462 162.556 204.854 1.00 1.51  ? 281 LEU A CD1 1 
ATOM 1923 C CD2 . LEU A 1 331  ? 187.575 160.925 204.849 1.00 4.16  ? 281 LEU A CD2 1 
ATOM 1924 N N   . ALA A 1 332  ? 189.157 165.132 202.167 1.00 10.12 ? 282 ALA A N   1 
ATOM 1925 C CA  . ALA A 1 332  ? 189.554 165.257 200.749 1.00 2.62  ? 282 ALA A CA  1 
ATOM 1926 C C   . ALA A 1 332  ? 190.510 164.124 200.372 1.00 7.38  ? 282 ALA A C   1 
ATOM 1927 O O   . ALA A 1 332  ? 191.558 163.987 201.035 1.00 14.14 ? 282 ALA A O   1 
ATOM 1928 C CB  . ALA A 1 332  ? 190.188 166.602 200.523 1.00 4.19  ? 282 ALA A CB  1 
ATOM 1929 N N   . THR A 1 333  ? 190.156 163.350 199.349 1.00 4.44  ? 283 THR A N   1 
ATOM 1930 C CA  . THR A 1 333  ? 190.983 162.251 198.864 1.00 0.00  ? 283 THR A CA  1 
ATOM 1931 C C   . THR A 1 333  ? 191.620 162.652 197.542 1.00 0.00  ? 283 THR A C   1 
ATOM 1932 O O   . THR A 1 333  ? 190.922 163.089 196.622 1.00 10.86 ? 283 THR A O   1 
ATOM 1933 C CB  . THR A 1 333  ? 190.155 160.981 198.686 1.00 0.00  ? 283 THR A CB  1 
ATOM 1934 O OG1 . THR A 1 333  ? 189.389 161.080 197.480 1.00 0.00  ? 283 THR A OG1 1 
ATOM 1935 C CG2 . THR A 1 333  ? 189.213 160.807 199.855 1.00 6.96  ? 283 THR A CG2 1 
ATOM 1936 N N   . THR A 1 334  ? 192.937 162.490 197.441 1.00 0.00  ? 284 THR A N   1 
ATOM 1937 C CA  . THR A 1 334  ? 193.717 163.086 196.364 1.00 0.00  ? 284 THR A CA  1 
ATOM 1938 C C   . THR A 1 334  ? 194.480 162.017 195.596 1.00 2.29  ? 284 THR A C   1 
ATOM 1939 O O   . THR A 1 334  ? 195.302 161.300 196.176 1.00 9.15  ? 284 THR A O   1 
ATOM 1940 C CB  . THR A 1 334  ? 194.696 164.119 196.921 1.00 5.45  ? 284 THR A CB  1 
ATOM 1941 O OG1 . THR A 1 334  ? 195.371 163.564 198.055 1.00 11.00 ? 284 THR A OG1 1 
ATOM 1942 C CG2 . THR A 1 334  ? 193.963 165.367 197.352 1.00 7.92  ? 284 THR A CG2 1 
ATOM 1943 N N   . TRP A 1 335  ? 194.234 161.955 194.279 1.00 0.00  ? 285 TRP A N   1 
ATOM 1944 C CA  . TRP A 1 335  ? 195.051 161.101 193.380 1.00 0.00  ? 285 TRP A CA  1 
ATOM 1945 C C   . TRP A 1 335  ? 195.980 162.104 192.707 1.00 3.56  ? 285 TRP A C   1 
ATOM 1946 O O   . TRP A 1 335  ? 195.475 162.930 191.914 1.00 16.06 ? 285 TRP A O   1 
ATOM 1947 C CB  . TRP A 1 335  ? 194.171 160.357 192.371 1.00 0.00  ? 285 TRP A CB  1 
ATOM 1948 C CG  . TRP A 1 335  ? 193.322 159.281 192.992 1.00 0.00  ? 285 TRP A CG  1 
ATOM 1949 C CD1 . TRP A 1 335  ? 193.596 157.946 193.045 1.00 5.82  ? 285 TRP A CD1 1 
ATOM 1950 C CD2 . TRP A 1 335  ? 192.050 159.456 193.654 1.00 0.00  ? 285 TRP A CD2 1 
ATOM 1951 N NE1 . TRP A 1 335  ? 192.590 157.279 193.690 1.00 6.16  ? 285 TRP A NE1 1 
ATOM 1952 C CE2 . TRP A 1 335  ? 191.628 158.176 194.074 1.00 3.90  ? 285 TRP A CE2 1 
ATOM 1953 C CE3 . TRP A 1 335  ? 191.235 160.558 193.931 1.00 0.00  ? 285 TRP A CE3 1 
ATOM 1954 C CZ2 . TRP A 1 335  ? 190.429 157.976 194.752 1.00 6.30  ? 285 TRP A CZ2 1 
ATOM 1955 C CZ3 . TRP A 1 335  ? 190.047 160.357 194.597 1.00 0.11  ? 285 TRP A CZ3 1 
ATOM 1956 C CH2 . TRP A 1 335  ? 189.652 159.083 195.003 1.00 0.00  ? 285 TRP A CH2 1 
ATOM 1957 N N   . PRO A 1 336  ? 197.304 162.096 192.967 1.00 0.00  ? 286 PRO A N   1 
ATOM 1958 C CA  . PRO A 1 336  ? 198.189 163.183 192.528 1.00 0.66  ? 286 PRO A CA  1 
ATOM 1959 C C   . PRO A 1 336  ? 198.601 163.112 191.068 1.00 4.89  ? 286 PRO A C   1 
ATOM 1960 O O   . PRO A 1 336  ? 198.768 164.153 190.426 1.00 13.39 ? 286 PRO A O   1 
ATOM 1961 C CB  . PRO A 1 336  ? 199.404 163.027 193.449 1.00 0.11  ? 286 PRO A CB  1 
ATOM 1962 C CG  . PRO A 1 336  ? 199.449 161.573 193.744 1.00 2.24  ? 286 PRO A CG  1 
ATOM 1963 C CD  . PRO A 1 336  ? 198.018 161.094 193.776 1.00 8.18  ? 286 PRO A CD  1 
ATOM 1964 N N   . HIS A 1 337  ? 198.779 161.908 190.530 1.00 6.28  ? 287 HIS A N   1 
ATOM 1965 C CA  . HIS A 1 337  ? 199.241 161.765 189.153 1.00 7.29  ? 287 HIS A CA  1 
ATOM 1966 C C   . HIS A 1 337  ? 198.766 160.434 188.596 1.00 2.22  ? 287 HIS A C   1 
ATOM 1967 O O   . HIS A 1 337  ? 199.173 159.376 189.083 1.00 9.28  ? 287 HIS A O   1 
ATOM 1968 C CB  . HIS A 1 337  ? 200.766 161.866 189.074 1.00 6.44  ? 287 HIS A CB  1 
ATOM 1969 C CG  . HIS A 1 337  ? 201.318 161.586 187.713 1.00 3.71  ? 287 HIS A CG  1 
ATOM 1970 N ND1 . HIS A 1 337  ? 200.662 161.945 186.556 1.00 1.37  ? 287 HIS A ND1 1 
ATOM 1971 C CD2 . HIS A 1 337  ? 202.467 160.986 187.323 1.00 4.02  ? 287 HIS A CD2 1 
ATOM 1972 C CE1 . HIS A 1 337  ? 201.382 161.576 185.511 1.00 1.10  ? 287 HIS A CE1 1 
ATOM 1973 N NE2 . HIS A 1 337  ? 202.482 160.992 185.950 1.00 5.57  ? 287 HIS A NE2 1 
ATOM 1974 N N   . LEU A 1 338  ? 197.918 160.492 187.573 1.00 1.75  ? 288 LEU A N   1 
ATOM 1975 C CA  . LEU A 1 338  ? 197.432 159.316 186.870 1.00 0.00  ? 288 LEU A CA  1 
ATOM 1976 C C   . LEU A 1 338  ? 197.767 159.459 185.391 1.00 3.58  ? 288 LEU A C   1 
ATOM 1977 O O   . LEU A 1 338  ? 198.512 160.355 184.985 1.00 9.29  ? 288 LEU A O   1 
ATOM 1978 C CB  . LEU A 1 338  ? 195.924 159.125 187.075 1.00 0.00  ? 288 LEU A CB  1 
ATOM 1979 C CG  . LEU A 1 338  ? 195.441 159.009 188.519 1.00 0.00  ? 288 LEU A CG  1 
ATOM 1980 C CD1 . LEU A 1 338  ? 193.957 158.709 188.555 1.00 0.00  ? 288 LEU A CD1 1 
ATOM 1981 C CD2 . LEU A 1 338  ? 196.219 157.936 189.251 1.00 8.48  ? 288 LEU A CD2 1 
ATOM 1982 N N   . THR A 1 339  ? 197.224 158.555 184.580 1.00 9.67  ? 289 THR A N   1 
ATOM 1983 C CA  . THR A 1 339  ? 197.402 158.603 183.137 1.00 6.77  ? 289 THR A CA  1 
ATOM 1984 C C   . THR A 1 339  ? 196.141 158.070 182.473 1.00 0.97  ? 289 THR A C   1 
ATOM 1985 O O   . THR A 1 339  ? 195.450 157.209 183.024 1.00 0.58  ? 289 THR A O   1 
ATOM 1986 C CB  . THR A 1 339  ? 198.642 157.801 182.702 1.00 5.51  ? 289 THR A CB  1 
ATOM 1987 O OG1 . THR A 1 339  ? 199.819 158.426 183.229 1.00 6.00  ? 289 THR A OG1 1 
ATOM 1988 C CG2 . THR A 1 339  ? 198.764 157.743 181.189 1.00 0.05  ? 289 THR A CG2 1 
ATOM 1989 N N   . GLU A 1 340  ? 195.858 158.609 181.281 1.00 0.85  ? 290 GLU A N   1 
ATOM 1990 C CA  . GLU A 1 340  ? 194.671 158.174 180.504 1.00 9.55  ? 290 GLU A CA  1 
ATOM 1991 C C   . GLU A 1 340  ? 194.800 156.691 180.159 1.00 20.61 ? 290 GLU A C   1 
ATOM 1992 O O   . GLU A 1 340  ? 195.870 156.290 179.662 1.00 18.95 ? 290 GLU A O   1 
ATOM 1993 C CB  . GLU A 1 340  ? 194.552 159.014 179.231 1.00 6.85  ? 290 GLU A CB  1 
ATOM 1994 C CG  . GLU A 1 340  ? 193.123 159.205 178.762 1.00 6.09  ? 290 GLU A CG  1 
ATOM 1995 C CD  . GLU A 1 340  ? 192.961 160.252 177.674 1.00 9.82  ? 290 GLU A CD  1 
ATOM 1996 O OE1 . GLU A 1 340  ? 193.880 161.079 177.510 1.00 9.18  ? 290 GLU A OE1 1 
ATOM 1997 O OE2 . GLU A 1 340  ? 191.917 160.237 176.992 1.00 9.42  ? 290 GLU A OE2 1 
ATOM 1998 N N   . GLY A 1 341  ? 193.747 155.917 180.413 1.00 25.47 ? 291 GLY A N   1 
ATOM 1999 C CA  . GLY A 1 341  ? 193.729 154.503 180.116 1.00 15.29 ? 291 GLY A CA  1 
ATOM 2000 C C   . GLY A 1 341  ? 194.207 153.601 181.233 1.00 17.79 ? 291 GLY A C   1 
ATOM 2001 O O   . GLY A 1 341  ? 194.015 152.381 181.145 1.00 23.37 ? 291 GLY A O   1 
ATOM 2002 N N   . ILE A 1 342  ? 194.823 154.155 182.280 1.00 14.31 ? 292 ILE A N   1 
ATOM 2003 C CA  . ILE A 1 342  ? 195.266 153.326 183.396 1.00 14.85 ? 292 ILE A CA  1 
ATOM 2004 C C   . ILE A 1 342  ? 194.066 152.783 184.163 1.00 18.50 ? 292 ILE A C   1 
ATOM 2005 O O   . ILE A 1 342  ? 194.112 151.670 184.700 1.00 17.67 ? 292 ILE A O   1 
ATOM 2006 C CB  . ILE A 1 342  ? 196.234 154.117 184.301 1.00 15.15 ? 292 ILE A CB  1 
ATOM 2007 C CG1 . ILE A 1 342  ? 197.287 153.186 184.904 1.00 17.37 ? 292 ILE A CG1 1 
ATOM 2008 C CG2 . ILE A 1 342  ? 195.496 154.856 185.406 1.00 17.82 ? 292 ILE A CG2 1 
ATOM 2009 C CD1 . ILE A 1 342  ? 198.477 152.950 183.999 1.00 15.59 ? 292 ILE A CD1 1 
ATOM 2010 N N   . ILE A 1 343  ? 192.978 153.549 184.222 1.00 19.88 ? 293 ILE A N   1 
ATOM 2011 C CA  . ILE A 1 343  ? 191.718 153.138 184.820 1.00 18.68 ? 293 ILE A CA  1 
ATOM 2012 C C   . ILE A 1 343  ? 190.594 153.651 183.929 1.00 20.28 ? 293 ILE A C   1 
ATOM 2013 O O   . ILE A 1 343  ? 190.834 154.275 182.892 1.00 17.12 ? 293 ILE A O   1 
ATOM 2014 C CB  . ILE A 1 343  ? 191.551 153.659 186.263 1.00 17.64 ? 293 ILE A CB  1 
ATOM 2015 C CG1 . ILE A 1 343  ? 191.752 155.176 186.311 1.00 21.52 ? 293 ILE A CG1 1 
ATOM 2016 C CG2 . ILE A 1 343  ? 192.509 152.949 187.208 1.00 13.32 ? 293 ILE A CG2 1 
ATOM 2017 C CD1 . ILE A 1 343  ? 191.760 155.752 187.712 1.00 19.92 ? 293 ILE A CD1 1 
ATOM 2018 N N   . VAL A 1 344  ? 189.357 153.386 184.335 1.00 18.57 ? 294 VAL A N   1 
ATOM 2019 C CA  . VAL A 1 344  ? 188.196 153.864 183.600 1.00 18.84 ? 294 VAL A CA  1 
ATOM 2020 C C   . VAL A 1 344  ? 187.283 154.618 184.554 1.00 16.67 ? 294 VAL A C   1 
ATOM 2021 O O   . VAL A 1 344  ? 187.269 154.371 185.765 1.00 8.51  ? 294 VAL A O   1 
ATOM 2022 C CB  . VAL A 1 344  ? 187.424 152.720 182.905 1.00 14.46 ? 294 VAL A CB  1 
ATOM 2023 C CG1 . VAL A 1 344  ? 188.371 151.846 182.094 1.00 16.03 ? 294 VAL A CG1 1 
ATOM 2024 C CG2 . VAL A 1 344  ? 186.666 151.895 183.923 1.00 14.08 ? 294 VAL A CG2 1 
ATOM 2025 N N   . ASP A 1 345  ? 186.526 155.560 183.993 1.00 20.18 ? 295 ASP A N   1 
ATOM 2026 C CA  . ASP A 1 345  ? 185.511 156.294 184.744 1.00 17.51 ? 295 ASP A CA  1 
ATOM 2027 C C   . ASP A 1 345  ? 184.473 156.766 183.731 1.00 14.07 ? 295 ASP A C   1 
ATOM 2028 O O   . ASP A 1 345  ? 184.701 157.746 183.016 1.00 10.42 ? 295 ASP A O   1 
ATOM 2029 C CB  . ASP A 1 345  ? 186.115 157.461 185.510 1.00 13.43 ? 295 ASP A CB  1 
ATOM 2030 C CG  . ASP A 1 345  ? 185.065 158.430 186.008 1.00 15.74 ? 295 ASP A CG  1 
ATOM 2031 O OD1 . ASP A 1 345  ? 184.416 158.128 187.030 1.00 14.67 ? 295 ASP A OD1 1 
ATOM 2032 O OD2 . ASP A 1 345  ? 184.884 159.489 185.373 1.00 11.20 ? 295 ASP A OD2 1 
ATOM 2033 N N   . ASN A 1 346  ? 183.347 156.063 183.672 1.00 16.57 ? 296 ASN A N   1 
ATOM 2034 C CA  . ASN A 1 346  ? 182.291 156.372 182.721 1.00 14.09 ? 296 ASN A CA  1 
ATOM 2035 C C   . ASN A 1 346  ? 180.952 156.183 183.422 1.00 19.68 ? 296 ASN A C   1 
ATOM 2036 O O   . ASN A 1 346  ? 180.881 156.051 184.648 1.00 14.15 ? 296 ASN A O   1 
ATOM 2037 C CB  . ASN A 1 346  ? 182.424 155.502 181.464 1.00 15.95 ? 296 ASN A CB  1 
ATOM 2038 C CG  . ASN A 1 346  ? 182.860 154.085 181.781 1.00 19.58 ? 296 ASN A CG  1 
ATOM 2039 O OD1 . ASN A 1 346  ? 182.308 153.437 182.669 1.00 19.57 ? 296 ASN A OD1 1 
ATOM 2040 N ND2 . ASN A 1 346  ? 183.856 153.596 181.052 1.00 23.14 ? 296 ASN A ND2 1 
ATOM 2041 N N   . ASP A 1 347  ? 179.874 156.133 182.636 1.00 23.46 ? 297 ASP A N   1 
ATOM 2042 C CA  . ASP A 1 347  ? 178.514 156.025 183.233 1.00 23.83 ? 297 ASP A CA  1 
ATOM 2043 C C   . ASP A 1 347  ? 178.277 154.618 183.797 1.00 21.05 ? 297 ASP A C   1 
ATOM 2044 O O   . ASP A 1 347  ? 177.237 154.427 184.456 1.00 21.97 ? 297 ASP A O   1 
ATOM 2045 C CB  . ASP A 1 347  ? 177.435 156.412 182.218 1.00 23.54 ? 297 ASP A CB  1 
ATOM 2046 C CG  . ASP A 1 347  ? 177.080 157.888 182.259 1.00 26.17 ? 297 ASP A CG  1 
ATOM 2047 O OD1 . ASP A 1 347  ? 176.888 158.414 183.373 1.00 22.95 ? 297 ASP A OD1 1 
ATOM 2048 O OD2 . ASP A 1 347  ? 177.002 158.502 181.176 1.00 26.74 ? 297 ASP A OD2 1 
ATOM 2049 N N   . VAL A 1 348  ? 179.191 153.672 183.553 1.00 23.40 ? 298 VAL A N   1 
ATOM 2050 C CA  . VAL A 1 348  ? 178.976 152.305 184.011 1.00 24.76 ? 298 VAL A CA  1 
ATOM 2051 C C   . VAL A 1 348  ? 180.024 151.910 185.045 1.00 25.47 ? 298 VAL A C   1 
ATOM 2052 O O   . VAL A 1 348  ? 179.690 151.609 186.196 1.00 24.49 ? 298 VAL A O   1 
ATOM 2053 C CB  . VAL A 1 348  ? 178.984 151.322 182.825 1.00 22.93 ? 298 VAL A CB  1 
ATOM 2054 C CG1 . VAL A 1 348  ? 178.538 149.942 183.277 1.00 22.00 ? 298 VAL A CG1 1 
ATOM 2055 C CG2 . VAL A 1 348  ? 178.095 151.835 181.702 1.00 19.32 ? 298 VAL A CG2 1 
ATOM 2056 N N   . TYR A 1 349  ? 181.295 151.912 184.648 1.00 24.81 ? 299 TYR A N   1 
ATOM 2057 C CA  . TYR A 1 349  ? 182.381 151.387 185.467 1.00 21.10 ? 299 TYR A CA  1 
ATOM 2058 C C   . TYR A 1 349  ? 183.261 152.524 185.968 1.00 18.10 ? 299 TYR A C   1 
ATOM 2059 O O   . TYR A 1 349  ? 183.675 153.385 185.184 1.00 17.53 ? 299 TYR A O   1 
ATOM 2060 C CB  . TYR A 1 349  ? 183.222 150.383 184.674 1.00 20.66 ? 299 TYR A CB  1 
ATOM 2061 C CG  . TYR A 1 349  ? 183.954 149.378 185.535 1.00 22.31 ? 299 TYR A CG  1 
ATOM 2062 C CD1 . TYR A 1 349  ? 183.293 148.684 186.538 1.00 22.32 ? 299 TYR A CD1 1 
ATOM 2063 C CD2 . TYR A 1 349  ? 185.304 149.122 185.342 1.00 20.65 ? 299 TYR A CD2 1 
ATOM 2064 C CE1 . TYR A 1 349  ? 183.957 147.764 187.326 1.00 20.72 ? 299 TYR A CE1 1 
ATOM 2065 C CE2 . TYR A 1 349  ? 185.976 148.206 186.125 1.00 18.79 ? 299 TYR A CE2 1 
ATOM 2066 C CZ  . TYR A 1 349  ? 185.298 147.530 187.115 1.00 20.73 ? 299 TYR A CZ  1 
ATOM 2067 O OH  . TYR A 1 349  ? 185.963 146.615 187.898 1.00 24.71 ? 299 TYR A OH  1 
ATOM 2068 N N   . SER A 1 350  ? 183.550 152.519 187.269 1.00 19.82 ? 300 SER A N   1 
ATOM 2069 C CA  . SER A 1 350  ? 184.397 153.531 187.883 1.00 20.98 ? 300 SER A CA  1 
ATOM 2070 C C   . SER A 1 350  ? 185.373 152.870 188.848 1.00 18.69 ? 300 SER A C   1 
ATOM 2071 O O   . SER A 1 350  ? 185.048 151.875 189.501 1.00 17.82 ? 300 SER A O   1 
ATOM 2072 C CB  . SER A 1 350  ? 183.566 154.589 188.622 1.00 20.89 ? 300 SER A CB  1 
ATOM 2073 O OG  . SER A 1 350  ? 183.124 155.602 187.735 1.00 20.84 ? 300 SER A OG  1 
ATOM 2074 N N   . ASP A 1 351  ? 186.576 153.441 188.931 1.00 16.86 ? 301 ASP A N   1 
ATOM 2075 C CA  . ASP A 1 351  ? 187.615 152.968 189.839 1.00 16.96 ? 301 ASP A CA  1 
ATOM 2076 C C   . ASP A 1 351  ? 187.915 153.966 190.951 1.00 19.67 ? 301 ASP A C   1 
ATOM 2077 O O   . ASP A 1 351  ? 188.806 153.718 191.773 1.00 21.55 ? 301 ASP A O   1 
ATOM 2078 C CB  . ASP A 1 351  ? 188.899 152.655 189.063 1.00 14.69 ? 301 ASP A CB  1 
ATOM 2079 C CG  . ASP A 1 351  ? 189.896 151.851 189.879 1.00 19.20 ? 301 ASP A CG  1 
ATOM 2080 O OD1 . ASP A 1 351  ? 189.513 150.794 190.422 1.00 18.73 ? 301 ASP A OD1 1 
ATOM 2081 O OD2 . ASP A 1 351  ? 191.059 152.289 189.994 1.00 20.40 ? 301 ASP A OD2 1 
ATOM 2082 N N   . LEU A 1 352  ? 187.192 155.084 191.008 1.00 15.80 ? 302 LEU A N   1 
ATOM 2083 C CA  . LEU A 1 352  ? 187.499 156.154 191.955 1.00 13.60 ? 302 LEU A CA  1 
ATOM 2084 C C   . LEU A 1 352  ? 186.951 155.780 193.330 1.00 15.38 ? 302 LEU A C   1 
ATOM 2085 O O   . LEU A 1 352  ? 185.886 156.226 193.763 1.00 21.81 ? 302 LEU A O   1 
ATOM 2086 C CB  . LEU A 1 352  ? 186.940 157.479 191.455 1.00 14.95 ? 302 LEU A CB  1 
ATOM 2087 C CG  . LEU A 1 352  ? 187.382 157.826 190.033 1.00 12.22 ? 302 LEU A CG  1 
ATOM 2088 C CD1 . LEU A 1 352  ? 186.776 159.138 189.579 1.00 8.18  ? 302 LEU A CD1 1 
ATOM 2089 C CD2 . LEU A 1 352  ? 188.896 157.876 189.949 1.00 12.13 ? 302 LEU A CD2 1 
ATOM 2090 N N   . ASP A 1 353  ? 187.712 154.930 194.028 1.00 14.57 ? 303 ASP A N   1 
ATOM 2091 C CA  . ASP A 1 353  ? 187.450 154.513 195.401 1.00 20.54 ? 303 ASP A CA  1 
ATOM 2092 C C   . ASP A 1 353  ? 188.257 155.370 196.362 1.00 21.06 ? 303 ASP A C   1 
ATOM 2093 O O   . ASP A 1 353  ? 189.482 155.472 196.204 1.00 21.87 ? 303 ASP A O   1 
ATOM 2094 C CB  . ASP A 1 353  ? 187.813 153.043 195.591 1.00 21.30 ? 303 ASP A CB  1 
ATOM 2095 C CG  . ASP A 1 353  ? 186.860 152.323 196.521 1.00 22.77 ? 303 ASP A CG  1 
ATOM 2096 O OD1 . ASP A 1 353  ? 185.745 152.836 196.749 1.00 24.60 ? 303 ASP A OD1 1 
ATOM 2097 O OD2 . ASP A 1 353  ? 187.227 151.242 197.028 1.00 21.78 ? 303 ASP A OD2 1 
ATOM 2098 N N   . PRO A 1 354  ? 187.630 156.005 197.357 1.00 16.36 ? 304 PRO A N   1 
ATOM 2099 C CA  . PRO A 1 354  ? 188.400 156.858 198.278 1.00 13.88 ? 304 PRO A CA  1 
ATOM 2100 C C   . PRO A 1 354  ? 189.423 156.099 199.100 1.00 12.90 ? 304 PRO A C   1 
ATOM 2101 O O   . PRO A 1 354  ? 190.441 156.690 199.482 1.00 10.73 ? 304 PRO A O   1 
ATOM 2102 C CB  . PRO A 1 354  ? 187.325 157.483 199.174 1.00 14.21 ? 304 PRO A CB  1 
ATOM 2103 C CG  . PRO A 1 354  ? 186.145 156.593 199.069 1.00 16.25 ? 304 PRO A CG  1 
ATOM 2104 C CD  . PRO A 1 354  ? 186.260 155.753 197.831 1.00 16.76 ? 304 PRO A CD  1 
ATOM 2105 N N   . ILE A 1 355  ? 189.187 154.817 199.387 1.00 15.48 ? 305 ILE A N   1 
ATOM 2106 C CA  . ILE A 1 355  ? 190.112 154.050 200.215 1.00 19.19 ? 305 ILE A CA  1 
ATOM 2107 C C   . ILE A 1 355  ? 191.464 153.904 199.532 1.00 18.71 ? 305 ILE A C   1 
ATOM 2108 O O   . ILE A 1 355  ? 192.502 153.822 200.200 1.00 7.00  ? 305 ILE A O   1 
ATOM 2109 C CB  . ILE A 1 355  ? 189.502 152.678 200.551 1.00 16.73 ? 305 ILE A CB  1 
ATOM 2110 C CG1 . ILE A 1 355  ? 188.026 152.829 200.922 1.00 15.48 ? 305 ILE A CG1 1 
ATOM 2111 C CG2 . ILE A 1 355  ? 190.273 152.018 201.679 1.00 19.99 ? 305 ILE A CG2 1 
ATOM 2112 C CD1 . ILE A 1 355  ? 187.372 151.541 201.358 1.00 12.68 ? 305 ILE A CD1 1 
ATOM 2113 N N   . GLN A 1 356  ? 191.478 153.872 198.203 1.00 21.87 ? 306 GLN A N   1 
ATOM 2114 C CA  . GLN A 1 356  ? 192.696 153.687 197.429 1.00 22.77 ? 306 GLN A CA  1 
ATOM 2115 C C   . GLN A 1 356  ? 193.454 154.984 197.183 1.00 16.17 ? 306 GLN A C   1 
ATOM 2116 O O   . GLN A 1 356  ? 194.508 154.952 196.540 1.00 17.83 ? 306 GLN A O   1 
ATOM 2117 C CB  . GLN A 1 356  ? 192.367 153.024 196.088 1.00 17.36 ? 306 GLN A CB  1 
ATOM 2118 C CG  . GLN A 1 356  ? 192.405 151.508 196.127 1.00 14.32 ? 306 GLN A CG  1 
ATOM 2119 C CD  . GLN A 1 356  ? 191.408 150.926 197.109 1.00 14.76 ? 306 GLN A CD  1 
ATOM 2120 O OE1 . GLN A 1 356  ? 190.338 151.491 197.333 1.00 15.24 ? 306 GLN A OE1 1 
ATOM 2121 N NE2 . GLN A 1 356  ? 191.759 149.792 197.705 1.00 16.60 ? 306 GLN A NE2 1 
ATOM 2122 N N   . ALA A 1 357  ? 192.954 156.111 197.667 1.00 0.00  ? 307 ALA A N   1 
ATOM 2123 C CA  . ALA A 1 357  ? 193.652 157.373 197.475 1.00 0.00  ? 307 ALA A CA  1 
ATOM 2124 C C   . ALA A 1 357  ? 194.962 157.354 198.250 1.00 5.77  ? 307 ALA A C   1 
ATOM 2125 O O   . ALA A 1 357  ? 194.939 157.189 199.476 1.00 21.84 ? 307 ALA A O   1 
ATOM 2126 C CB  . ALA A 1 357  ? 192.782 158.531 197.937 1.00 4.83  ? 307 ALA A CB  1 
ATOM 2127 N N   . PRO A 1 358  ? 196.113 157.516 197.593 1.00 3.41  ? 308 PRO A N   1 
ATOM 2128 C CA  . PRO A 1 358  ? 197.393 157.438 198.319 1.00 11.03 ? 308 PRO A CA  1 
ATOM 2129 C C   . PRO A 1 358  ? 197.587 158.521 199.369 1.00 14.69 ? 308 PRO A C   1 
ATOM 2130 O O   . PRO A 1 358  ? 198.396 158.326 200.285 1.00 18.63 ? 308 PRO A O   1 
ATOM 2131 C CB  . PRO A 1 358  ? 198.442 157.547 197.203 1.00 4.62  ? 308 PRO A CB  1 
ATOM 2132 C CG  . PRO A 1 358  ? 197.720 158.090 196.027 1.00 0.48  ? 308 PRO A CG  1 
ATOM 2133 C CD  . PRO A 1 358  ? 196.306 157.634 196.140 1.00 0.00  ? 308 PRO A CD  1 
ATOM 2134 N N   . HIS A 1 359  ? 196.892 159.654 199.272 1.00 6.57  ? 309 HIS A N   1 
ATOM 2135 C CA  . HIS A 1 359  ? 197.004 160.725 200.254 1.00 5.86  ? 309 HIS A CA  1 
ATOM 2136 C C   . HIS A 1 359  ? 195.621 161.088 200.775 1.00 9.93  ? 309 HIS A C   1 
ATOM 2137 O O   . HIS A 1 359  ? 194.661 161.163 200.004 1.00 11.75 ? 309 HIS A O   1 
ATOM 2138 C CB  . HIS A 1 359  ? 197.675 161.972 199.658 1.00 4.74  ? 309 HIS A CB  1 
ATOM 2139 C CG  . HIS A 1 359  ? 199.084 161.750 199.200 1.00 9.38  ? 309 HIS A CG  1 
ATOM 2140 N ND1 . HIS A 1 359  ? 199.806 160.621 199.519 1.00 15.79 ? 309 HIS A ND1 1 
ATOM 2141 C CD2 . HIS A 1 359  ? 199.905 162.519 198.446 1.00 9.55  ? 309 HIS A CD2 1 
ATOM 2142 C CE1 . HIS A 1 359  ? 201.009 160.701 198.980 1.00 11.95 ? 309 HIS A CE1 1 
ATOM 2143 N NE2 . HIS A 1 359  ? 201.095 161.844 198.323 1.00 10.30 ? 309 HIS A NE2 1 
ATOM 2144 N N   . TRP A 1 360  ? 195.525 161.318 202.086 1.00 11.84 ? 310 TRP A N   1 
ATOM 2145 C CA  . TRP A 1 360  ? 194.277 161.713 202.731 1.00 7.20  ? 310 TRP A CA  1 
ATOM 2146 C C   . TRP A 1 360  ? 194.502 162.973 203.556 1.00 4.95  ? 310 TRP A C   1 
ATOM 2147 O O   . TRP A 1 360  ? 195.447 163.040 204.350 1.00 15.64 ? 310 TRP A O   1 
ATOM 2148 C CB  . TRP A 1 360  ? 193.731 160.594 203.622 1.00 6.19  ? 310 TRP A CB  1 
ATOM 2149 C CG  . TRP A 1 360  ? 192.795 159.666 202.916 1.00 8.22  ? 310 TRP A CG  1 
ATOM 2150 C CD1 . TRP A 1 360  ? 192.799 159.356 201.590 1.00 8.77  ? 310 TRP A CD1 1 
ATOM 2151 C CD2 . TRP A 1 360  ? 191.718 158.925 203.498 1.00 5.70  ? 310 TRP A CD2 1 
ATOM 2152 N NE1 . TRP A 1 360  ? 191.790 158.470 201.309 1.00 8.93  ? 310 TRP A NE1 1 
ATOM 2153 C CE2 . TRP A 1 360  ? 191.111 158.189 202.464 1.00 8.90  ? 310 TRP A CE2 1 
ATOM 2154 C CE3 . TRP A 1 360  ? 191.206 158.813 204.793 1.00 8.82  ? 310 TRP A CE3 1 
ATOM 2155 C CZ2 . TRP A 1 360  ? 190.022 157.353 202.684 1.00 10.24 ? 310 TRP A CZ2 1 
ATOM 2156 C CZ3 . TRP A 1 360  ? 190.125 157.983 205.009 1.00 10.75 ? 310 TRP A CZ3 1 
ATOM 2157 C CH2 . TRP A 1 360  ? 189.545 157.263 203.961 1.00 11.83 ? 310 TRP A CH2 1 
ATOM 2158 N N   . SER A 1 361  ? 193.623 163.957 203.377 1.00 5.25  ? 311 SER A N   1 
ATOM 2159 C CA  . SER A 1 361  ? 193.700 165.235 204.069 1.00 13.95 ? 311 SER A CA  1 
ATOM 2160 C C   . SER A 1 361  ? 192.382 165.518 204.779 1.00 19.07 ? 311 SER A C   1 
ATOM 2161 O O   . SER A 1 361  ? 191.315 165.092 204.330 1.00 19.98 ? 311 SER A O   1 
ATOM 2162 C CB  . SER A 1 361  ? 194.015 166.372 203.095 1.00 13.21 ? 311 SER A CB  1 
ATOM 2163 O OG  . SER A 1 361  ? 194.925 165.946 202.097 1.00 13.35 ? 311 SER A OG  1 
ATOM 2164 N N   . VAL A 1 362  ? 192.457 166.231 205.908 1.00 21.43 ? 312 VAL A N   1 
ATOM 2165 C CA  . VAL A 1 362  ? 191.224 166.484 206.714 1.00 19.09 ? 312 VAL A CA  1 
ATOM 2166 C C   . VAL A 1 362  ? 191.067 167.988 206.962 1.00 23.66 ? 312 VAL A C   1 
ATOM 2167 O O   . VAL A 1 362  ? 192.046 168.614 207.416 1.00 29.05 ? 312 VAL A O   1 
ATOM 2168 C CB  . VAL A 1 362  ? 191.255 165.699 208.040 1.00 6.28  ? 312 VAL A CB  1 
ATOM 2169 C CG1 . VAL A 1 362  ? 190.186 166.183 209.007 1.00 5.79  ? 312 VAL A CG1 1 
ATOM 2170 C CG2 . VAL A 1 362  ? 191.128 164.201 207.813 1.00 12.56 ? 312 VAL A CG2 1 
ATOM 2171 N N   . ARG A 1 363  ? 189.872 168.531 206.708 1.00 17.49 ? 313 ARG A N   1 
ATOM 2172 C CA  . ARG A 1 363  ? 189.594 169.961 207.005 1.00 15.76 ? 313 ARG A CA  1 
ATOM 2173 C C   . ARG A 1 363  ? 188.358 170.014 207.908 1.00 15.96 ? 313 ARG A C   1 
ATOM 2174 O O   . ARG A 1 363  ? 187.397 169.279 207.621 1.00 17.42 ? 313 ARG A O   1 
ATOM 2175 C CB  . ARG A 1 363  ? 189.363 170.736 205.706 1.00 18.10 ? 313 ARG A CB  1 
ATOM 2176 C CG  . ARG A 1 363  ? 189.038 172.209 205.905 1.00 19.14 ? 313 ARG A CG  1 
ATOM 2177 C CD  . ARG A 1 363  ? 189.067 172.948 204.582 1.00 19.06 ? 313 ARG A CD  1 
ATOM 2178 N NE  . ARG A 1 363  ? 190.160 172.471 203.747 1.00 26.35 ? 313 ARG A NE  1 
ATOM 2179 C CZ  . ARG A 1 363  ? 191.175 173.217 203.327 1.00 23.41 ? 313 ARG A CZ  1 
ATOM 2180 N NH1 . ARG A 1 363  ? 192.129 172.678 202.591 1.00 19.00 ? 313 ARG A NH1 1 
ATOM 2181 N NH2 . ARG A 1 363  ? 191.236 174.497 203.652 1.00 18.61 ? 313 ARG A NH2 1 
ATOM 2182 N N   . VAL A 1 364  ? 188.381 170.825 208.969 1.00 11.56 ? 314 VAL A N   1 
ATOM 2183 C CA  . VAL A 1 364  ? 187.228 170.811 209.914 1.00 15.13 ? 314 VAL A CA  1 
ATOM 2184 C C   . VAL A 1 364  ? 186.468 172.134 209.782 1.00 26.14 ? 314 VAL A C   1 
ATOM 2185 O O   . VAL A 1 364  ? 187.058 173.107 209.272 1.00 30.62 ? 314 VAL A O   1 
ATOM 2186 C CB  . VAL A 1 364  ? 187.711 170.581 211.355 1.00 22.35 ? 314 VAL A CB  1 
ATOM 2187 C CG1 . VAL A 1 364  ? 188.519 171.769 211.836 1.00 24.93 ? 314 VAL A CG1 1 
ATOM 2188 C CG2 . VAL A 1 364  ? 186.568 170.273 212.311 1.00 21.41 ? 314 VAL A CG2 1 
ATOM 2189 N N   . ARG A 1 365  ? 185.206 172.176 210.225 1.00 29.66 ? 315 ARG A N   1 
ATOM 2190 C CA  . ARG A 1 365  ? 184.403 173.428 210.173 1.00 27.88 ? 315 ARG A CA  1 
ATOM 2191 C C   . ARG A 1 365  ? 184.023 173.848 211.598 1.00 25.08 ? 315 ARG A C   1 
ATOM 2192 O O   . ARG A 1 365  ? 183.686 172.957 212.402 1.00 27.44 ? 315 ARG A O   1 
ATOM 2193 C CB  . ARG A 1 365  ? 183.153 173.222 209.312 1.00 30.07 ? 315 ARG A CB  1 
ATOM 2194 C CG  . ARG A 1 365  ? 182.261 174.449 209.204 1.00 28.80 ? 315 ARG A CG  1 
ATOM 2195 C CD  . ARG A 1 365  ? 180.975 174.159 208.454 1.00 27.19 ? 315 ARG A CD  1 
ATOM 2196 N NE  . ARG A 1 365  ? 181.216 173.625 207.122 1.00 28.33 ? 315 ARG A NE  1 
ATOM 2197 C CZ  . ARG A 1 365  ? 180.822 174.210 205.997 1.00 27.62 ? 315 ARG A CZ  1 
ATOM 2198 N NH1 . ARG A 1 365  ? 180.400 175.461 206.015 1.00 25.06 ? 315 ARG A NH1 1 
ATOM 2199 N NH2 . ARG A 1 365  ? 180.852 173.541 204.857 1.00 27.46 ? 315 ARG A NH2 1 
ATOM 2200 N N   . LYS A 1 366  ? 184.081 175.146 211.904 1.00 27.58 ? 316 LYS A N   1 
ATOM 2201 C CA  . LYS A 1 366  ? 183.777 175.618 213.283 1.00 33.14 ? 316 LYS A CA  1 
ATOM 2202 C C   . LYS A 1 366  ? 182.346 176.166 213.328 1.00 36.17 ? 316 LYS A C   1 
ATOM 2203 O O   . LYS A 1 366  ? 182.054 177.114 212.573 1.00 35.17 ? 316 LYS A O   1 
ATOM 2204 C CB  . LYS A 1 366  ? 184.801 176.666 213.728 1.00 30.72 ? 316 LYS A CB  1 
ATOM 2205 C CG  . LYS A 1 366  ? 186.231 176.155 213.845 1.00 32.73 ? 316 LYS A CG  1 
ATOM 2206 C CD  . LYS A 1 366  ? 187.197 177.181 214.397 1.00 29.71 ? 316 LYS A CD  1 
ATOM 2207 C CE  . LYS A 1 366  ? 188.595 176.632 214.587 1.00 30.86 ? 316 LYS A CE  1 
ATOM 2208 N NZ  . LYS A 1 366  ? 189.504 177.638 215.185 1.00 32.07 ? 316 LYS A NZ  1 
ATOM 2209 N N   . ALA A 1 367  ? 181.494 175.587 214.182 1.00 30.56 ? 317 ALA A N   1 
ATOM 2210 C CA  . ALA A 1 367  ? 180.092 176.051 214.303 1.00 30.75 ? 317 ALA A CA  1 
ATOM 2211 C C   . ALA A 1 367  ? 180.074 177.501 214.797 1.00 33.32 ? 317 ALA A C   1 
ATOM 2212 O O   . ALA A 1 367  ? 180.857 177.825 215.712 1.00 30.61 ? 317 ALA A O   1 
ATOM 2213 C CB  . ALA A 1 367  ? 179.321 175.145 215.232 1.00 29.64 ? 317 ALA A CB  1 
ATOM 2214 N N   . GLU A 1 368  ? 179.209 178.332 214.211 1.00 35.60 ? 318 GLU A N   1 
ATOM 2215 C CA  . GLU A 1 368  ? 179.122 179.762 214.611 1.00 34.99 ? 318 GLU A CA  1 
ATOM 2216 C C   . GLU A 1 368  ? 178.339 179.875 215.922 1.00 37.70 ? 318 GLU A C   1 
ATOM 2217 O O   . GLU A 1 368  ? 177.530 178.969 216.204 1.00 39.31 ? 318 GLU A O   1 
ATOM 2218 C CB  . GLU A 1 368  ? 178.456 180.582 213.505 1.00 33.17 ? 318 GLU A CB  1 
ATOM 2219 C CG  . GLU A 1 368  ? 179.176 180.488 212.173 1.00 32.88 ? 318 GLU A CG  1 
ATOM 2220 C CD  . GLU A 1 368  ? 178.536 181.290 211.054 1.00 37.46 ? 318 GLU A CD  1 
ATOM 2221 O OE1 . GLU A 1 368  ? 177.362 181.019 210.732 1.00 39.91 ? 318 GLU A OE1 1 
ATOM 2222 O OE2 . GLU A 1 368  ? 179.212 182.184 210.508 1.00 36.79 ? 318 GLU A OE2 1 
ATOM 2223 N N   . ASN A 1 369  ? 178.612 180.928 216.687 1.00 37.89 ? 319 ASN A N   1 
ATOM 2224 C CA  . ASN A 1 369  ? 177.887 181.149 217.963 1.00 35.54 ? 319 ASN A CA  1 
ATOM 2225 C C   . ASN A 1 369  ? 177.910 179.893 218.830 1.00 37.70 ? 319 ASN A C   1 
ATOM 2226 O O   . ASN A 1 369  ? 176.825 179.350 219.119 1.00 39.52 ? 319 ASN A O   1 
ATOM 2227 C CB  . ASN A 1 369  ? 176.448 181.612 217.716 1.00 36.47 ? 319 ASN A CB  1 
ATOM 2228 C CG  . ASN A 1 369  ? 176.365 182.808 216.791 1.00 38.22 ? 319 ASN A CG  1 
ATOM 2229 O OD1 . ASN A 1 369  ? 177.384 183.308 216.321 1.00 36.11 ? 319 ASN A OD1 1 
ATOM 2230 N ND2 . ASN A 1 369  ? 175.155 183.271 216.523 1.00 40.21 ? 319 ASN A ND2 1 
ATOM 2231 N N   . PRO A 1 370  ? 179.090 179.417 219.269 1.00 38.71 ? 320 PRO A N   1 
ATOM 2232 C CA  . PRO A 1 370  ? 179.168 178.277 220.183 1.00 38.62 ? 320 PRO A CA  1 
ATOM 2233 C C   . PRO A 1 370  ? 178.881 178.798 221.596 1.00 36.32 ? 320 PRO A C   1 
ATOM 2234 O O   . PRO A 1 370  ? 179.816 178.935 222.363 1.00 33.21 ? 320 PRO A O   1 
ATOM 2235 C CB  . PRO A 1 370  ? 180.621 177.792 220.080 1.00 37.55 ? 320 PRO A CB  1 
ATOM 2236 C CG  . PRO A 1 370  ? 181.256 178.651 219.000 1.00 40.13 ? 320 PRO A CG  1 
ATOM 2237 C CD  . PRO A 1 370  ? 180.421 179.912 218.924 1.00 38.17 ? 320 PRO A CD  1 
ATOM 2238 N N   . GLN A 1 371  ? 177.610 179.077 221.903 1.00 39.64 ? 321 GLN A N   1 
ATOM 2239 C CA  . GLN A 1 371  ? 177.259 179.674 223.220 1.00 42.02 ? 321 GLN A CA  1 
ATOM 2240 C C   . GLN A 1 371  ? 178.003 178.943 224.341 1.00 42.18 ? 321 GLN A C   1 
ATOM 2241 O O   . GLN A 1 371  ? 177.698 177.757 224.571 1.00 43.57 ? 321 GLN A O   1 
ATOM 2242 C CB  . GLN A 1 371  ? 175.747 179.615 223.439 1.00 42.53 ? 321 GLN A CB  1 
ATOM 2243 C CG  . GLN A 1 371  ? 174.948 180.271 222.323 1.00 42.43 ? 321 GLN A CG  1 
ATOM 2244 C CD  . GLN A 1 371  ? 173.463 180.071 222.495 1.00 44.71 ? 321 GLN A CD  1 
ATOM 2245 O OE1 . GLN A 1 371  ? 173.002 179.517 223.491 1.00 45.49 ? 321 GLN A OE1 1 
ATOM 2246 N NE2 . GLN A 1 371  ? 172.697 180.523 221.515 1.00 43.82 ? 321 GLN A NE2 1 
ATOM 2247 N N   . CYS A 1 372  ? 178.926 179.635 225.017 1.00 43.12 ? 322 CYS A N   1 
ATOM 2248 C CA  . CYS A 1 372  ? 179.662 179.033 226.161 1.00 44.81 ? 322 CYS A CA  1 
ATOM 2249 C C   . CYS A 1 372  ? 179.054 179.563 227.464 1.00 41.88 ? 322 CYS A C   1 
ATOM 2250 O O   . CYS A 1 372  ? 178.149 180.414 227.382 1.00 43.98 ? 322 CYS A O   1 
ATOM 2251 C CB  . CYS A 1 372  ? 181.141 179.391 226.104 1.00 45.20 ? 322 CYS A CB  1 
ATOM 2252 S SG  . CYS A 1 372  ? 181.951 178.882 224.566 1.00 59.06 ? 322 CYS A SG  1 
ATOM 2253 N N   . LEU A 1 373  ? 179.528 179.076 228.615 1.00 30.00 ? 323 LEU A N   1 
ATOM 2254 C CA  . LEU A 1 373  ? 178.931 179.503 229.912 1.00 30.00 ? 323 LEU A CA  1 
ATOM 2255 C C   . LEU A 1 373  ? 179.862 180.445 230.686 1.00 30.00 ? 323 LEU A C   1 
ATOM 2256 O O   . LEU A 1 373  ? 179.411 180.986 231.715 1.00 30.00 ? 323 LEU A O   1 
ATOM 2257 C CB  . LEU A 1 373  ? 178.637 178.246 230.738 1.00 30.00 ? 323 LEU A CB  1 
ATOM 2258 C CG  . LEU A 1 373  ? 177.472 178.361 231.720 1.00 30.00 ? 323 LEU A CG  1 
ATOM 2259 C CD1 . LEU A 1 373  ? 176.370 179.242 231.152 1.00 30.00 ? 323 LEU A CD1 1 
ATOM 2260 C CD2 . LEU A 1 373  ? 176.927 176.986 232.074 1.00 30.00 ? 323 LEU A CD2 1 
ATOM 2261 N N   . LEU A 1 374  ? 181.071 180.653 230.193 1.00 34.78 ? 324 LEU A N   1 
ATOM 2262 C CA  . LEU A 1 374  ? 181.988 181.459 231.026 1.00 32.09 ? 324 LEU A CA  1 
ATOM 2263 C C   . LEU A 1 374  ? 182.266 182.817 230.372 1.00 31.70 ? 324 LEU A C   1 
ATOM 2264 O O   . LEU A 1 374  ? 182.675 183.747 231.096 1.00 27.60 ? 324 LEU A O   1 
ATOM 2265 C CB  . LEU A 1 374  ? 183.245 180.623 231.249 1.00 31.08 ? 324 LEU A CB  1 
ATOM 2266 C CG  . LEU A 1 374  ? 184.154 181.285 232.285 1.00 32.64 ? 324 LEU A CG  1 
ATOM 2267 C CD1 . LEU A 1 374  ? 183.990 180.621 233.644 1.00 29.65 ? 324 LEU A CD1 1 
ATOM 2268 C CD2 . LEU A 1 374  ? 185.608 181.233 231.842 1.00 33.79 ? 324 LEU A CD2 1 
ATOM 2269 N N   . GLY A 1 375  ? 182.027 182.936 229.067 1.00 31.94 ? 325 GLY A N   1 
ATOM 2270 C CA  . GLY A 1 375  ? 182.186 184.231 228.380 1.00 34.06 ? 325 GLY A CA  1 
ATOM 2271 C C   . GLY A 1 375  ? 180.948 185.096 228.521 1.00 33.00 ? 325 GLY A C   1 
ATOM 2272 O O   . GLY A 1 375  ? 180.913 186.177 227.902 1.00 30.30 ? 325 GLY A O   1 
ATOM 2273 N N   . ASP A 1 376  ? 179.964 184.639 229.302 1.00 33.82 ? 326 ASP A N   1 
ATOM 2274 C CA  . ASP A 1 376  ? 178.693 185.403 229.424 1.00 33.87 ? 326 ASP A CA  1 
ATOM 2275 C C   . ASP A 1 376  ? 178.375 185.615 230.908 1.00 34.30 ? 326 ASP A C   1 
ATOM 2276 O O   . ASP A 1 376  ? 177.841 186.687 231.250 1.00 34.83 ? 326 ASP A O   1 
ATOM 2277 C CB  . ASP A 1 376  ? 177.547 184.696 228.698 1.00 30.14 ? 326 ASP A CB  1 
ATOM 2278 C CG  . ASP A 1 376  ? 177.405 183.228 229.067 1.00 31.66 ? 326 ASP A CG  1 
ATOM 2279 O OD1 . ASP A 1 376  ? 178.174 182.763 229.931 1.00 32.56 ? 326 ASP A OD1 1 
ATOM 2280 O OD2 . ASP A 1 376  ? 176.525 182.562 228.488 1.00 30.07 ? 326 ASP A OD2 1 
ATOM 2281 N N   . PHE A 1 377  ? 178.689 184.625 231.747 1.00 29.51 ? 327 PHE A N   1 
ATOM 2282 C CA  . PHE A 1 377  ? 178.397 184.717 233.202 1.00 31.44 ? 327 PHE A CA  1 
ATOM 2283 C C   . PHE A 1 377  ? 178.970 186.019 233.772 1.00 29.26 ? 327 PHE A C   1 
ATOM 2284 O O   . PHE A 1 377  ? 178.227 186.750 234.456 1.00 27.14 ? 327 PHE A O   1 
ATOM 2285 C CB  . PHE A 1 377  ? 178.961 183.494 233.930 1.00 32.36 ? 327 PHE A CB  1 
ATOM 2286 C CG  . PHE A 1 377  ? 178.666 183.447 235.408 1.00 30.35 ? 327 PHE A CG  1 
ATOM 2287 C CD1 . PHE A 1 377  ? 177.436 183.012 235.872 1.00 30.86 ? 327 PHE A CD1 1 
ATOM 2288 C CD2 . PHE A 1 377  ? 179.618 183.839 236.334 1.00 30.18 ? 327 PHE A CD2 1 
ATOM 2289 C CE1 . PHE A 1 377  ? 177.166 182.968 237.231 1.00 31.85 ? 327 PHE A CE1 1 
ATOM 2290 C CE2 . PHE A 1 377  ? 179.347 183.795 237.692 1.00 31.03 ? 327 PHE A CE2 1 
ATOM 2291 C CZ  . PHE A 1 377  ? 178.122 183.360 238.138 1.00 30.94 ? 327 PHE A CZ  1 
ATOM 2292 N N   . VAL A 1 378  ? 180.248 186.299 233.497 1.00 28.11 ? 328 VAL A N   1 
ATOM 2293 C CA  . VAL A 1 378  ? 180.893 187.548 234.002 1.00 29.96 ? 328 VAL A CA  1 
ATOM 2294 C C   . VAL A 1 378  ? 180.395 188.725 233.157 1.00 29.02 ? 328 VAL A C   1 
ATOM 2295 O O   . VAL A 1 378  ? 180.214 189.820 233.722 1.00 27.03 ? 328 VAL A O   1 
ATOM 2296 C CB  . VAL A 1 378  ? 182.430 187.439 233.984 1.00 30.85 ? 328 VAL A CB  1 
ATOM 2297 C CG1 . VAL A 1 378  ? 182.944 186.590 235.136 1.00 27.56 ? 328 VAL A CG1 1 
ATOM 2298 C CG2 . VAL A 1 378  ? 182.945 186.905 232.657 1.00 29.79 ? 328 VAL A CG2 1 
ATOM 2299 N N   . THR A 1 379  ? 180.178 188.498 231.858 1.00 28.58 ? 329 THR A N   1 
ATOM 2300 C CA  . THR A 1 379  ? 179.660 189.561 230.956 1.00 31.08 ? 329 THR A CA  1 
ATOM 2301 C C   . THR A 1 379  ? 178.405 190.181 231.577 1.00 31.90 ? 329 THR A C   1 
ATOM 2302 O O   . THR A 1 379  ? 178.218 191.404 231.420 1.00 27.06 ? 329 THR A O   1 
ATOM 2303 C CB  . THR A 1 379  ? 179.397 189.010 229.549 1.00 30.45 ? 329 THR A CB  1 
ATOM 2304 O OG1 . THR A 1 379  ? 180.643 188.560 229.017 1.00 30.59 ? 329 THR A OG1 1 
ATOM 2305 C CG2 . THR A 1 379  ? 178.784 190.030 228.615 1.00 31.84 ? 329 THR A CG2 1 
ATOM 2306 N N   . GLU A 1 380  ? 177.592 189.381 232.275 1.00 34.21 ? 330 GLU A N   1 
ATOM 2307 C CA  . GLU A 1 380  ? 176.338 189.905 232.810 1.00 35.81 ? 330 GLU A CA  1 
ATOM 2308 C C   . GLU A 1 380  ? 176.585 191.055 233.779 1.00 36.98 ? 330 GLU A C   1 
ATOM 2309 O O   . GLU A 1 380  ? 175.673 191.837 234.070 1.00 33.30 ? 330 GLU A O   1 
ATOM 2310 C CB  . GLU A 1 380  ? 175.552 188.788 233.498 1.00 33.43 ? 330 GLU A CB  1 
ATOM 2311 C CG  . GLU A 1 380  ? 174.995 187.739 232.551 1.00 33.60 ? 330 GLU A CG  1 
ATOM 2312 C CD  . GLU A 1 380  ? 174.110 188.332 231.474 1.00 36.59 ? 330 GLU A CD  1 
ATOM 2313 O OE1 . GLU A 1 380  ? 173.284 189.212 231.798 1.00 36.90 ? 330 GLU A OE1 1 
ATOM 2314 O OE2 . GLU A 1 380  ? 174.244 187.922 230.302 1.00 35.72 ? 330 GLU A OE2 1 
ATOM 2315 N N   . PHE A 1 381  ? 177.810 191.173 234.290 1.00 32.55 ? 331 PHE A N   1 
ATOM 2316 C CA  . PHE A 1 381  ? 178.158 192.205 235.258 1.00 29.04 ? 331 PHE A CA  1 
ATOM 2317 C C   . PHE A 1 381  ? 179.027 193.304 234.658 1.00 30.62 ? 331 PHE A C   1 
ATOM 2318 O O   . PHE A 1 381  ? 179.696 194.033 235.397 1.00 34.16 ? 331 PHE A O   1 
ATOM 2319 C CB  . PHE A 1 381  ? 178.847 191.579 236.469 1.00 33.68 ? 331 PHE A CB  1 
ATOM 2320 C CG  . PHE A 1 381  ? 177.894 191.159 237.543 1.00 37.91 ? 331 PHE A CG  1 
ATOM 2321 C CD1 . PHE A 1 381  ? 176.616 190.742 237.217 1.00 34.80 ? 331 PHE A CD1 1 
ATOM 2322 C CD2 . PHE A 1 381  ? 178.268 191.187 238.875 1.00 37.34 ? 331 PHE A CD2 1 
ATOM 2323 C CE1 . PHE A 1 381  ? 175.728 190.362 238.194 1.00 35.21 ? 331 PHE A CE1 1 
ATOM 2324 C CE2 . PHE A 1 381  ? 177.383 190.803 239.859 1.00 35.09 ? 331 PHE A CE2 1 
ATOM 2325 C CZ  . PHE A 1 381  ? 176.112 190.389 239.516 1.00 36.00 ? 331 PHE A CZ  1 
ATOM 2326 N N   . PHE A 1 382  ? 179.039 193.394 233.324 1.00 33.54 ? 332 PHE A N   1 
ATOM 2327 C CA  . PHE A 1 382  ? 179.866 194.418 232.633 1.00 35.98 ? 332 PHE A CA  1 
ATOM 2328 C C   . PHE A 1 382  ? 178.953 195.333 231.810 1.00 39.23 ? 332 PHE A C   1 
ATOM 2329 O O   . PHE A 1 382  ? 178.173 194.783 231.008 1.00 38.19 ? 332 PHE A O   1 
ATOM 2330 C CB  . PHE A 1 382  ? 180.919 193.749 231.746 1.00 34.71 ? 332 PHE A CB  1 
ATOM 2331 C CG  . PHE A 1 382  ? 181.928 192.905 232.485 1.00 36.36 ? 332 PHE A CG  1 
ATOM 2332 C CD1 . PHE A 1 382  ? 182.458 193.324 233.694 1.00 36.79 ? 332 PHE A CD1 1 
ATOM 2333 C CD2 . PHE A 1 382  ? 182.352 191.692 231.967 1.00 36.71 ? 332 PHE A CD2 1 
ATOM 2334 C CE1 . PHE A 1 382  ? 183.385 192.547 234.370 1.00 38.85 ? 332 PHE A CE1 1 
ATOM 2335 C CE2 . PHE A 1 382  ? 183.281 190.917 232.642 1.00 34.64 ? 332 PHE A CE2 1 
ATOM 2336 C CZ  . PHE A 1 382  ? 183.794 191.345 233.843 1.00 37.03 ? 332 PHE A CZ  1 
ATOM 2337 N N   . PRO A 1 832  ? 185.686 194.438 239.035 1.00 31.82 ? 782 PRO A N   1 
ATOM 2338 C CA  . PRO A 1 832  ? 187.092 194.212 239.382 1.00 30.21 ? 782 PRO A CA  1 
ATOM 2339 C C   . PRO A 1 832  ? 187.353 192.807 239.917 1.00 31.22 ? 782 PRO A C   1 
ATOM 2340 O O   . PRO A 1 832  ? 188.352 192.189 239.552 1.00 29.80 ? 782 PRO A O   1 
ATOM 2341 C CB  . PRO A 1 832  ? 187.359 195.268 240.465 1.00 33.12 ? 782 PRO A CB  1 
ATOM 2342 C CG  . PRO A 1 832  ? 186.002 195.662 240.964 1.00 31.43 ? 782 PRO A CG  1 
ATOM 2343 C CD  . PRO A 1 832  ? 185.131 195.594 239.756 1.00 31.08 ? 782 PRO A CD  1 
ATOM 2344 N N   . CYS A 1 833  ? 186.457 192.316 240.776 1.00 30.65 ? 783 CYS A N   1 
ATOM 2345 C CA  . CYS A 1 833  ? 186.638 190.989 241.357 1.00 33.33 ? 783 CYS A CA  1 
ATOM 2346 C C   . CYS A 1 833  ? 186.512 189.900 240.299 1.00 36.27 ? 783 CYS A C   1 
ATOM 2347 O O   . CYS A 1 833  ? 187.333 188.977 240.240 1.00 34.57 ? 783 CYS A O   1 
ATOM 2348 C CB  . CYS A 1 833  ? 185.623 190.768 242.479 1.00 32.29 ? 783 CYS A CB  1 
ATOM 2349 S SG  . CYS A 1 833  ? 183.905 190.708 241.923 1.00 38.02 ? 783 CYS A SG  1 
ATOM 2350 N N   . VAL A 1 834  ? 185.489 189.996 239.443 1.00 29.06 ? 784 VAL A N   1 
ATOM 2351 C CA  . VAL A 1 834  ? 185.241 188.969 238.431 1.00 26.59 ? 784 VAL A CA  1 
ATOM 2352 C C   . VAL A 1 834  ? 186.245 189.001 237.293 1.00 30.47 ? 784 VAL A C   1 
ATOM 2353 O O   . VAL A 1 834  ? 186.176 188.148 236.398 1.00 26.08 ? 784 VAL A O   1 
ATOM 2354 C CB  . VAL A 1 834  ? 183.820 189.103 237.850 1.00 25.18 ? 784 VAL A CB  1 
ATOM 2355 C CG1 . VAL A 1 834  ? 182.799 188.528 238.817 1.00 25.70 ? 784 VAL A CG1 1 
ATOM 2356 C CG2 . VAL A 1 834  ? 183.510 190.558 237.547 1.00 24.82 ? 784 VAL A CG2 1 
ATOM 2357 N N   . ILE A 1 835  ? 187.197 189.937 237.334 1.00 29.44 ? 785 ILE A N   1 
ATOM 2358 C CA  . ILE A 1 835  ? 188.232 190.044 236.260 1.00 28.79 ? 785 ILE A CA  1 
ATOM 2359 C C   . ILE A 1 835  ? 189.298 188.966 236.480 1.00 26.45 ? 785 ILE A C   1 
ATOM 2360 O O   . ILE A 1 835  ? 189.869 188.491 235.478 1.00 24.99 ? 785 ILE A O   1 
ATOM 2361 C CB  . ILE A 1 835  ? 188.848 191.457 236.249 1.00 29.70 ? 785 ILE A CB  1 
ATOM 2362 C CG1 . ILE A 1 835  ? 187.770 192.544 236.252 1.00 30.97 ? 785 ILE A CG1 1 
ATOM 2363 C CG2 . ILE A 1 835  ? 189.813 191.625 235.086 1.00 30.59 ? 785 ILE A CG2 1 
ATOM 2364 C CD1 . ILE A 1 835  ? 186.939 192.585 234.994 1.00 30.46 ? 785 ILE A CD1 1 
ATOM 2365 N N   . HIS A 1 836  ? 189.540 188.578 237.733 1.00 24.94 ? 786 HIS A N   1 
ATOM 2366 C CA  . HIS A 1 836  ? 190.573 187.610 238.069 1.00 27.15 ? 786 HIS A CA  1 
ATOM 2367 C C   . HIS A 1 836  ? 190.062 186.177 238.114 1.00 27.82 ? 786 HIS A C   1 
ATOM 2368 O O   . HIS A 1 836  ? 190.864 185.246 237.974 1.00 21.47 ? 786 HIS A O   1 
ATOM 2369 C CB  . HIS A 1 836  ? 191.195 187.989 239.418 1.00 27.34 ? 786 HIS A CB  1 
ATOM 2370 C CG  . HIS A 1 836  ? 191.563 186.821 240.277 1.00 30.18 ? 786 HIS A CG  1 
ATOM 2371 N ND1 . HIS A 1 836  ? 192.778 186.179 240.177 1.00 30.05 ? 786 HIS A ND1 1 
ATOM 2372 C CD2 . HIS A 1 836  ? 190.872 186.171 241.243 1.00 31.31 ? 786 HIS A CD2 1 
ATOM 2373 C CE1 . HIS A 1 836  ? 192.824 185.189 241.050 1.00 30.29 ? 786 HIS A CE1 1 
ATOM 2374 N NE2 . HIS A 1 836  ? 191.680 185.163 241.710 1.00 31.83 ? 786 HIS A NE2 1 
ATOM 2375 N N   . ALA A 1 837  ? 188.754 186.005 238.326 1.00 32.06 ? 787 ALA A N   1 
ATOM 2376 C CA  . ALA A 1 837  ? 188.168 184.649 238.454 1.00 31.37 ? 787 ALA A CA  1 
ATOM 2377 C C   . ALA A 1 837  ? 188.634 183.753 237.301 1.00 28.47 ? 787 ALA A C   1 
ATOM 2378 O O   . ALA A 1 837  ? 189.225 182.692 237.583 1.00 26.65 ? 787 ALA A O   1 
ATOM 2379 C CB  . ALA A 1 837  ? 186.663 184.747 238.497 1.00 29.41 ? 787 ALA A CB  1 
ATOM 2380 N N   . ALA A 1 838  ? 188.353 184.154 236.057 1.00 27.74 ? 788 ALA A N   1 
ATOM 2381 C CA  . ALA A 1 838  ? 188.694 183.312 234.885 1.00 27.13 ? 788 ALA A CA  1 
ATOM 2382 C C   . ALA A 1 838  ? 190.202 183.044 234.837 1.00 29.27 ? 788 ALA A C   1 
ATOM 2383 O O   . ALA A 1 838  ? 190.583 181.917 234.478 1.00 26.48 ? 788 ALA A O   1 
ATOM 2384 C CB  . ALA A 1 838  ? 188.216 183.981 233.620 1.00 24.68 ? 788 ALA A CB  1 
ATOM 2385 N N   . VAL A 1 839  ? 191.024 184.031 235.206 1.00 30.64 ? 789 VAL A N   1 
ATOM 2386 C CA  . VAL A 1 839  ? 192.504 183.866 235.094 1.00 31.30 ? 789 VAL A CA  1 
ATOM 2387 C C   . VAL A 1 839  ? 192.901 182.514 235.699 1.00 34.69 ? 789 VAL A C   1 
ATOM 2388 O O   . VAL A 1 839  ? 193.677 181.784 235.050 1.00 31.56 ? 789 VAL A O   1 
ATOM 2389 C CB  . VAL A 1 839  ? 193.253 185.029 235.773 1.00 31.07 ? 789 VAL A CB  1 
ATOM 2390 C CG1 . VAL A 1 839  ? 194.762 184.880 235.649 1.00 28.84 ? 789 VAL A CG1 1 
ATOM 2391 C CG2 . VAL A 1 839  ? 192.802 186.378 235.235 1.00 31.62 ? 789 VAL A CG2 1 
ATOM 2392 N N   . LEU A 1 840  ? 192.376 182.193 236.884 1.00 32.95 ? 790 LEU A N   1 
ATOM 2393 C CA  . LEU A 1 840  ? 192.722 180.915 237.562 1.00 30.90 ? 790 LEU A CA  1 
ATOM 2394 C C   . LEU A 1 840  ? 191.825 179.792 237.032 1.00 31.46 ? 790 LEU A C   1 
ATOM 2395 O O   . LEU A 1 840  ? 192.338 178.675 236.837 1.00 31.77 ? 790 LEU A O   1 
ATOM 2396 C CB  . LEU A 1 840  ? 192.543 181.092 239.073 1.00 28.42 ? 790 LEU A CB  1 
ATOM 2397 C CG  . LEU A 1 840  ? 193.064 179.941 239.932 1.00 31.95 ? 790 LEU A CG  1 
ATOM 2398 C CD1 . LEU A 1 840  ? 193.996 180.455 241.018 1.00 30.66 ? 790 LEU A CD1 1 
ATOM 2399 C CD2 . LEU A 1 840  ? 191.914 179.155 240.543 1.00 29.59 ? 790 LEU A CD2 1 
ATOM 2400 N N   . LYS A 1 841  ? 190.531 180.081 236.866 1.00 28.19 ? 791 LYS A N   1 
ATOM 2401 C CA  . LYS A 1 841  ? 189.568 179.060 236.377 1.00 32.06 ? 791 LYS A CA  1 
ATOM 2402 C C   . LYS A 1 841  ? 190.100 178.471 235.068 1.00 32.63 ? 791 LYS A C   1 
ATOM 2403 O O   . LYS A 1 841  ? 190.309 177.245 235.012 1.00 34.36 ? 791 LYS A O   1 
ATOM 2404 C CB  . LYS A 1 841  ? 188.188 179.687 236.166 1.00 34.45 ? 791 LYS A CB  1 
ATOM 2405 C CG  . LYS A 1 841  ? 187.042 178.695 236.029 1.00 34.85 ? 791 LYS A CG  1 
ATOM 2406 C CD  . LYS A 1 841  ? 187.136 177.548 237.012 1.00 34.91 ? 791 LYS A CD  1 
ATOM 2407 C CE  . LYS A 1 841  ? 185.820 176.826 237.205 1.00 32.68 ? 791 LYS A CE  1 
ATOM 2408 N NZ  . LYS A 1 841  ? 184.894 177.070 236.074 1.00 31.58 ? 791 LYS A NZ  1 
ATOM 2409 N N   . VAL A 1 842  ? 190.312 179.326 234.064 1.00 30.77 ? 792 VAL A N   1 
ATOM 2410 C CA  . VAL A 1 842  ? 190.833 178.847 232.751 1.00 34.02 ? 792 VAL A CA  1 
ATOM 2411 C C   . VAL A 1 842  ? 192.086 178.007 233.009 1.00 31.97 ? 792 VAL A C   1 
ATOM 2412 O O   . VAL A 1 842  ? 192.184 176.905 232.434 1.00 26.43 ? 792 VAL A O   1 
ATOM 2413 C CB  . VAL A 1 842  ? 191.120 180.029 231.806 1.00 34.52 ? 792 VAL A CB  1 
ATOM 2414 C CG1 . VAL A 1 842  ? 191.851 179.583 230.551 1.00 31.25 ? 792 VAL A CG1 1 
ATOM 2415 C CG2 . VAL A 1 842  ? 189.849 180.780 231.444 1.00 31.80 ? 792 VAL A CG2 1 
ATOM 2416 N N   . LYS A 1 843  ? 192.991 178.495 233.864 1.00 33.35 ? 793 LYS A N   1 
ATOM 2417 C CA  . LYS A 1 843  ? 194.241 177.788 234.126 1.00 35.50 ? 793 LYS A CA  1 
ATOM 2418 C C   . LYS A 1 843  ? 193.981 176.363 234.598 1.00 35.95 ? 793 LYS A C   1 
ATOM 2419 O O   . LYS A 1 843  ? 194.687 175.427 234.204 1.00 31.60 ? 793 LYS A O   1 
ATOM 2420 C CB  . LYS A 1 843  ? 195.066 178.554 235.162 1.00 35.70 ? 793 LYS A CB  1 
ATOM 2421 C CG  . LYS A 1 843  ? 196.439 177.955 235.427 1.00 38.09 ? 793 LYS A CG  1 
ATOM 2422 C CD  . LYS A 1 843  ? 197.221 178.775 236.440 1.00 37.08 ? 793 LYS A CD  1 
ATOM 2423 C CE  . LYS A 1 843  ? 198.582 178.153 236.719 1.00 37.93 ? 793 LYS A CE  1 
ATOM 2424 N NZ  . LYS A 1 843  ? 199.360 178.932 237.722 1.00 35.35 ? 793 LYS A NZ  1 
ATOM 2425 N N   . GLU A 1 844  ? 192.960 176.192 235.442 1.00 36.00 ? 794 GLU A N   1 
ATOM 2426 C CA  . GLU A 1 844  ? 192.677 174.848 236.016 1.00 33.84 ? 794 GLU A CA  1 
ATOM 2427 C C   . GLU A 1 844  ? 192.333 173.855 234.901 1.00 35.23 ? 794 GLU A C   1 
ATOM 2428 O O   . GLU A 1 844  ? 192.934 172.764 234.885 1.00 32.59 ? 794 GLU A O   1 
ATOM 2429 C CB  . GLU A 1 844  ? 191.538 174.935 237.034 1.00 31.24 ? 794 GLU A CB  1 
ATOM 2430 C CG  . GLU A 1 844  ? 191.850 175.836 238.215 1.00 31.01 ? 794 GLU A CG  1 
ATOM 2431 C CD  . GLU A 1 844  ? 193.297 175.805 238.677 1.00 36.31 ? 794 GLU A CD  1 
ATOM 2432 O OE1 . GLU A 1 844  ? 193.684 174.818 239.333 1.00 39.56 ? 794 GLU A OE1 1 
ATOM 2433 O OE2 . GLU A 1 844  ? 194.033 176.769 238.382 1.00 34.36 ? 794 GLU A OE2 1 
ATOM 2434 N N   . GLU A 1 845  ? 191.407 174.213 234.006 1.00 35.78 ? 795 GLU A N   1 
ATOM 2435 C CA  . GLU A 1 845  ? 190.954 173.254 232.960 1.00 36.95 ? 795 GLU A CA  1 
ATOM 2436 C C   . GLU A 1 845  ? 192.106 172.910 232.008 1.00 37.31 ? 795 GLU A C   1 
ATOM 2437 O O   . GLU A 1 845  ? 192.184 171.739 231.589 1.00 37.74 ? 795 GLU A O   1 
ATOM 2438 C CB  . GLU A 1 845  ? 189.759 173.817 232.185 1.00 37.05 ? 795 GLU A CB  1 
ATOM 2439 C CG  . GLU A 1 845  ? 188.512 173.998 233.030 1.00 36.94 ? 795 GLU A CG  1 
ATOM 2440 C CD  . GLU A 1 845  ? 188.001 172.737 233.703 1.00 36.56 ? 795 GLU A CD  1 
ATOM 2441 O OE1 . GLU A 1 845  ? 188.032 171.670 233.060 1.00 37.18 ? 795 GLU A OE1 1 
ATOM 2442 O OE2 . GLU A 1 845  ? 187.574 172.825 234.871 1.00 35.29 ? 795 GLU A OE2 1 
ATOM 2443 N N   . GLU A 1 846  ? 192.964 173.881 231.679 1.00 37.47 ? 796 GLU A N   1 
ATOM 2444 C CA  . GLU A 1 846  ? 194.036 173.624 230.677 1.00 35.62 ? 796 GLU A CA  1 
ATOM 2445 C C   . GLU A 1 846  ? 195.299 173.073 231.349 1.00 36.56 ? 796 GLU A C   1 
ATOM 2446 O O   . GLU A 1 846  ? 196.315 172.932 230.645 1.00 33.67 ? 796 GLU A O   1 
ATOM 2447 C CB  . GLU A 1 846  ? 194.368 174.905 229.910 1.00 34.57 ? 796 GLU A CB  1 
ATOM 2448 C CG  . GLU A 1 846  ? 195.019 175.972 230.769 1.00 40.57 ? 796 GLU A CG  1 
ATOM 2449 C CD  . GLU A 1 846  ? 194.710 177.386 230.312 1.00 40.37 ? 796 GLU A CD  1 
ATOM 2450 O OE1 . GLU A 1 846  ? 193.955 177.530 229.332 1.00 39.10 ? 796 GLU A OE1 1 
ATOM 2451 O OE2 . GLU A 1 846  ? 195.223 178.335 230.936 1.00 35.34 ? 796 GLU A OE2 1 
ATOM 2452 N N   . SER A 1 847  ? 195.245 172.764 232.647 1.00 33.84 ? 797 SER A N   1 
ATOM 2453 C CA  . SER A 1 847  ? 196.413 172.179 233.297 1.00 33.98 ? 797 SER A CA  1 
ATOM 2454 C C   . SER A 1 847  ? 196.715 170.800 232.722 1.00 33.50 ? 797 SER A C   1 
ATOM 2455 O O   . SER A 1 847  ? 197.881 170.425 232.554 1.00 35.72 ? 797 SER A O   1 
ATOM 2456 C CB  . SER A 1 847  ? 196.192 172.107 234.808 1.00 35.01 ? 797 SER A CB  1 
ATOM 2457 O OG  . SER A 1 847  ? 196.223 173.400 235.388 1.00 30.13 ? 797 SER A OG  1 
ATOM 2458 N N   . LEU A 1 848  ? 195.670 170.031 232.413 1.00 31.17 ? 798 LEU A N   1 
ATOM 2459 C CA  . LEU A 1 848  ? 195.859 168.767 231.709 1.00 34.83 ? 798 LEU A CA  1 
ATOM 2460 C C   . LEU A 1 848  ? 196.006 168.991 230.207 1.00 34.89 ? 798 LEU A C   1 
ATOM 2461 O O   . LEU A 1 848  ? 196.731 168.256 229.527 1.00 34.31 ? 798 LEU A O   1 
ATOM 2462 C CB  . LEU A 1 848  ? 194.693 167.822 232.013 1.00 37.44 ? 798 LEU A CB  1 
ATOM 2463 C CG  . LEU A 1 848  ? 193.275 168.294 231.671 1.00 36.58 ? 798 LEU A CG  1 
ATOM 2464 C CD1 . LEU A 1 848  ? 192.835 167.801 230.298 1.00 32.48 ? 798 LEU A CD1 1 
ATOM 2465 C CD2 . LEU A 1 848  ? 192.288 167.856 232.743 1.00 32.35 ? 798 LEU A CD2 1 
ATOM 2466 N N   . GLU A 1 849  ? 195.335 170.017 229.674 1.00 33.38 ? 799 GLU A N   1 
ATOM 2467 C CA  . GLU A 1 849  ? 195.366 170.265 228.204 1.00 33.51 ? 799 GLU A CA  1 
ATOM 2468 C C   . GLU A 1 849  ? 196.724 170.846 227.798 1.00 36.16 ? 799 GLU A C   1 
ATOM 2469 O O   . GLU A 1 849  ? 197.274 170.382 226.780 1.00 36.59 ? 799 GLU A O   1 
ATOM 2470 C CB  . GLU A 1 849  ? 194.239 171.221 227.806 1.00 32.27 ? 799 GLU A CB  1 
ATOM 2471 C CG  . GLU A 1 849  ? 194.156 171.469 226.312 1.00 31.67 ? 799 GLU A CG  1 
ATOM 2472 C CD  . GLU A 1 849  ? 193.793 170.243 225.492 1.00 33.89 ? 799 GLU A CD  1 
ATOM 2473 O OE1 . GLU A 1 849  ? 193.362 169.239 226.093 1.00 36.44 ? 799 GLU A OE1 1 
ATOM 2474 O OE2 . GLU A 1 849  ? 193.944 170.295 224.256 1.00 35.95 ? 799 GLU A OE2 1 
ATOM 2475 N N   . ASN A 1 850  ? 197.230 171.825 228.551 1.00 36.78 ? 800 ASN A N   1 
ATOM 2476 C CA  . ASN A 1 850  ? 198.511 172.473 228.260 1.00 38.91 ? 800 ASN A CA  1 
ATOM 2477 C C   . ASN A 1 850  ? 198.540 173.036 226.839 1.00 38.89 ? 800 ASN A C   1 
ATOM 2478 O O   . ASN A 1 850  ? 199.357 172.647 226.002 1.00 35.13 ? 800 ASN A O   1 
ATOM 2479 C CB  . ASN A 1 850  ? 199.678 171.512 228.496 1.00 36.50 ? 800 ASN A CB  1 
ATOM 2480 C CG  . ASN A 1 850  ? 200.873 172.191 229.136 1.00 38.66 ? 800 ASN A CG  1 
ATOM 2481 O OD1 . ASN A 1 850  ? 201.396 173.175 228.613 1.00 38.07 ? 800 ASN A OD1 1 
ATOM 2482 N ND2 . ASN A 1 850  ? 201.311 171.668 230.275 1.00 36.28 ? 800 ASN A ND2 1 
ATOM 2483 N N   . ILE A 1 851  ? 197.626 173.971 226.569 1.00 38.47 ? 801 ILE A N   1 
ATOM 2484 C CA  . ILE A 1 851  ? 197.574 174.647 225.279 1.00 38.93 ? 801 ILE A CA  1 
ATOM 2485 C C   . ILE A 1 851  ? 198.810 175.501 225.027 1.00 38.15 ? 801 ILE A C   1 
ATOM 2486 O O   . ILE A 1 851  ? 199.252 175.616 223.879 1.00 34.35 ? 801 ILE A O   1 
ATOM 2487 C CB  . ILE A 1 851  ? 196.286 175.494 225.178 1.00 39.25 ? 801 ILE A CB  1 
ATOM 2488 C CG1 . ILE A 1 851  ? 195.053 174.604 225.342 1.00 38.80 ? 801 ILE A CG1 1 
ATOM 2489 C CG2 . ILE A 1 851  ? 196.216 176.223 223.847 1.00 38.17 ? 801 ILE A CG2 1 
ATOM 2490 C CD1 . ILE A 1 851  ? 193.761 175.373 225.500 1.00 34.60 ? 801 ILE A CD1 1 
ATOM 2491 N N   . SER A 1 852  ? 199.369 176.109 226.076 1.00 36.78 ? 802 SER A N   1 
ATOM 2492 C CA  . SER A 1 852  ? 200.636 176.844 226.005 1.00 35.69 ? 802 SER A CA  1 
ATOM 2493 C C   . SER A 1 852  ? 200.519 178.097 225.139 1.00 37.66 ? 802 SER A C   1 
ATOM 2494 O O   . SER A 1 852  ? 201.461 178.494 224.451 1.00 40.72 ? 802 SER A O   1 
ATOM 2495 C CB  . SER A 1 852  ? 201.772 175.944 225.513 1.00 34.46 ? 802 SER A CB  1 
ATOM 2496 O OG  . SER A 1 852  ? 201.637 174.626 226.016 1.00 30.43 ? 802 SER A OG  1 
ATOM 2497 N N   . SER A 1 853  ? 199.348 178.730 225.177 1.00 35.81 ? 803 SER A N   1 
ATOM 2498 C CA  . SER A 1 853  ? 199.158 180.027 224.539 1.00 37.12 ? 803 SER A CA  1 
ATOM 2499 C C   . SER A 1 853  ? 198.558 181.001 225.543 1.00 34.55 ? 803 SER A C   1 
ATOM 2500 O O   . SER A 1 853  ? 198.858 182.204 225.535 1.00 30.01 ? 803 SER A O   1 
ATOM 2501 C CB  . SER A 1 853  ? 198.257 179.900 223.309 1.00 31.05 ? 803 SER A CB  1 
ATOM 2502 O OG  . SER A 1 853  ? 197.507 181.084 223.102 1.00 31.34 ? 803 SER A OG  1 
ATOM 2503 N N   . VAL A 1 854  ? 197.652 180.481 226.375 1.00 36.24 ? 804 VAL A N   1 
ATOM 2504 C CA  . VAL A 1 854  ? 196.964 181.348 227.375 1.00 36.77 ? 804 VAL A CA  1 
ATOM 2505 C C   . VAL A 1 854  ? 198.025 181.976 228.283 1.00 38.36 ? 804 VAL A C   1 
ATOM 2506 O O   . VAL A 1 854  ? 197.943 183.194 228.524 1.00 37.61 ? 804 VAL A O   1 
ATOM 2507 C CB  . VAL A 1 854  ? 195.916 180.554 228.176 1.00 38.71 ? 804 VAL A CB  1 
ATOM 2508 C CG1 . VAL A 1 854  ? 195.017 181.471 228.990 1.00 36.77 ? 804 VAL A CG1 1 
ATOM 2509 C CG2 . VAL A 1 854  ? 195.086 179.668 227.260 1.00 35.81 ? 804 VAL A CG2 1 
ATOM 2510 N N   . LYS A 1 855  ? 198.979 181.173 228.764 1.00 39.72 ? 805 LYS A N   1 
ATOM 2511 C CA  . LYS A 1 855  ? 199.991 181.728 229.698 1.00 40.33 ? 805 LYS A CA  1 
ATOM 2512 C C   . LYS A 1 855  ? 200.575 183.025 229.126 1.00 38.48 ? 805 LYS A C   1 
ATOM 2513 O O   . LYS A 1 855  ? 200.567 184.043 229.842 1.00 30.24 ? 805 LYS A O   1 
ATOM 2514 C CB  . LYS A 1 855  ? 201.117 180.712 229.881 1.00 37.89 ? 805 LYS A CB  1 
ATOM 2515 C CG  . LYS A 1 855  ? 200.759 179.443 230.640 1.00 37.16 ? 805 LYS A CG  1 
ATOM 2516 C CD  . LYS A 1 855  ? 201.892 178.441 230.643 1.00 39.47 ? 805 LYS A CD  1 
ATOM 2517 C CE  . LYS A 1 855  ? 203.112 178.933 231.393 1.00 39.43 ? 805 LYS A CE  1 
ATOM 2518 N NZ  . LYS A 1 855  ? 204.166 177.896 231.488 1.00 36.62 ? 805 LYS A NZ  1 
ATOM 2519 N N   . LYS A 1 856  ? 201.084 182.978 227.883 1.00 39.82 ? 806 LYS A N   1 
ATOM 2520 C CA  . LYS A 1 856  ? 201.662 184.161 227.257 1.00 38.64 ? 806 LYS A CA  1 
ATOM 2521 C C   . LYS A 1 856  ? 200.619 185.259 227.094 1.00 41.18 ? 806 LYS A C   1 
ATOM 2522 O O   . LYS A 1 856  ? 200.905 186.441 227.322 1.00 39.42 ? 806 LYS A O   1 
ATOM 2523 C CB  . LYS A 1 856  ? 202.276 183.789 225.907 1.00 36.44 ? 806 LYS A CB  1 
ATOM 2524 C CG  . LYS A 1 856  ? 203.162 182.554 225.953 1.00 40.32 ? 806 LYS A CG  1 
ATOM 2525 C CD  . LYS A 1 856  ? 204.258 182.703 226.997 1.00 44.46 ? 806 LYS A CD  1 
ATOM 2526 C CE  . LYS A 1 856  ? 205.305 183.715 226.563 1.00 42.12 ? 806 LYS A CE  1 
ATOM 2527 N NZ  . LYS A 1 856  ? 206.476 183.724 227.482 1.00 39.36 ? 806 LYS A NZ  1 
ATOM 2528 N N   . ILE A 1 857  ? 199.395 184.871 226.729 1.00 36.39 ? 807 ILE A N   1 
ATOM 2529 C CA  . ILE A 1 857  ? 198.320 185.884 226.506 1.00 32.41 ? 807 ILE A CA  1 
ATOM 2530 C C   . ILE A 1 857  ? 197.939 186.514 227.853 1.00 33.41 ? 807 ILE A C   1 
ATOM 2531 O O   . ILE A 1 857  ? 197.606 187.712 227.860 1.00 32.73 ? 807 ILE A O   1 
ATOM 2532 C CB  . ILE A 1 857  ? 197.113 185.267 225.767 1.00 31.06 ? 807 ILE A CB  1 
ATOM 2533 C CG1 . ILE A 1 857  ? 197.479 184.848 224.341 1.00 31.28 ? 807 ILE A CG1 1 
ATOM 2534 C CG2 . ILE A 1 857  ? 195.912 186.197 225.785 1.00 30.81 ? 807 ILE A CG2 1 
ATOM 2535 C CD1 . ILE A 1 857  ? 196.425 184.006 223.661 1.00 30.47 ? 807 ILE A CD1 1 
ATOM 2536 N N   . ILE A 1 858  ? 198.005 185.732 228.935 1.00 34.26 ? 808 ILE A N   1 
ATOM 2537 C CA  . ILE A 1 858  ? 197.683 186.261 230.292 1.00 34.91 ? 808 ILE A CA  1 
ATOM 2538 C C   . ILE A 1 858  ? 198.791 187.239 230.692 1.00 36.55 ? 808 ILE A C   1 
ATOM 2539 O O   . ILE A 1 858  ? 198.458 188.339 231.175 1.00 34.91 ? 808 ILE A O   1 
ATOM 2540 C CB  . ILE A 1 858  ? 197.520 185.112 231.308 1.00 35.70 ? 808 ILE A CB  1 
ATOM 2541 C CG1 . ILE A 1 858  ? 196.089 184.566 231.314 1.00 37.22 ? 808 ILE A CG1 1 
ATOM 2542 C CG2 . ILE A 1 858  ? 197.962 185.539 232.699 1.00 32.64 ? 808 ILE A CG2 1 
ATOM 2543 C CD1 . ILE A 1 858  ? 195.907 183.339 232.175 1.00 36.93 ? 808 ILE A CD1 1 
ATOM 2544 N N   . LYS A 1 859  ? 200.055 186.865 230.469 1.00 37.58 ? 809 LYS A N   1 
ATOM 2545 C CA  . LYS A 1 859  ? 201.140 187.795 230.773 1.00 37.82 ? 809 LYS A CA  1 
ATOM 2546 C C   . LYS A 1 859  ? 200.982 189.091 229.984 1.00 36.84 ? 809 LYS A C   1 
ATOM 2547 O O   . LYS A 1 859  ? 201.209 190.187 230.516 1.00 33.11 ? 809 LYS A O   1 
ATOM 2548 C CB  . LYS A 1 859  ? 202.492 187.143 230.484 1.00 33.32 ? 809 LYS A CB  1 
ATOM 2549 C CG  . LYS A 1 859  ? 203.684 188.015 230.840 1.00 34.22 ? 809 LYS A CG  1 
ATOM 2550 C CD  . LYS A 1 859  ? 204.996 187.298 230.578 1.00 37.97 ? 809 LYS A CD  1 
ATOM 2551 C CE  . LYS A 1 859  ? 206.185 188.184 230.913 1.00 36.08 ? 809 LYS A CE  1 
ATOM 2552 N NZ  . LYS A 1 859  ? 207.481 187.497 230.661 1.00 34.30 ? 809 LYS A NZ  1 
ATOM 2553 N N   . GLN A 1 860  ? 200.584 188.983 228.713 1.00 31.69 ? 810 GLN A N   1 
ATOM 2554 C CA  . GLN A 1 860  ? 200.332 190.176 227.909 1.00 30.99 ? 810 GLN A CA  1 
ATOM 2555 C C   . GLN A 1 860  ? 199.198 191.007 228.495 1.00 30.33 ? 810 GLN A C   1 
ATOM 2556 O O   . GLN A 1 860  ? 199.285 192.237 228.540 1.00 26.20 ? 810 GLN A O   1 
ATOM 2557 C CB  . GLN A 1 860  ? 200.016 189.781 226.466 1.00 30.23 ? 810 GLN A CB  1 
ATOM 2558 C CG  . GLN A 1 860  ? 199.569 190.940 225.580 1.00 33.03 ? 810 GLN A CG  1 
ATOM 2559 C CD  . GLN A 1 860  ? 198.061 191.110 225.542 1.00 32.55 ? 810 GLN A CD  1 
ATOM 2560 O OE1 . GLN A 1 860  ? 197.316 190.134 225.455 1.00 31.50 ? 810 GLN A OE1 1 
ATOM 2561 N NE2 . GLN A 1 860  ? 197.604 192.355 225.611 1.00 30.08 ? 810 GLN A NE2 1 
ATOM 2562 N N   . ILE A 1 861  ? 198.127 190.338 228.928 1.00 32.01 ? 811 ILE A N   1 
ATOM 2563 C CA  . ILE A 1 861  ? 196.984 191.064 229.556 1.00 34.95 ? 811 ILE A CA  1 
ATOM 2564 C C   . ILE A 1 861  ? 197.499 191.763 230.817 1.00 34.46 ? 811 ILE A C   1 
ATOM 2565 O O   . ILE A 1 861  ? 197.172 192.951 231.008 1.00 33.01 ? 811 ILE A O   1 
ATOM 2566 C CB  . ILE A 1 861  ? 195.828 190.092 229.868 1.00 34.79 ? 811 ILE A CB  1 
ATOM 2567 C CG1 . ILE A 1 861  ? 195.067 189.692 228.601 1.00 31.33 ? 811 ILE A CG1 1 
ATOM 2568 C CG2 . ILE A 1 861  ? 194.899 190.673 230.922 1.00 33.73 ? 811 ILE A CG2 1 
ATOM 2569 C CD1 . ILE A 1 861  ? 194.667 190.862 227.732 1.00 29.16 ? 811 ILE A CD1 1 
ATOM 2570 N N   . ILE A 1 862  ? 198.293 191.059 231.627 1.00 30.43 ? 812 ILE A N   1 
ATOM 2571 C CA  . ILE A 1 862  ? 198.805 191.621 232.874 1.00 32.31 ? 812 ILE A CA  1 
ATOM 2572 C C   . ILE A 1 862  ? 199.603 192.887 232.596 1.00 36.42 ? 812 ILE A C   1 
ATOM 2573 O O   . ILE A 1 862  ? 199.442 193.909 233.274 1.00 30.85 ? 812 ILE A O   1 
ATOM 2574 C CB  . ILE A 1 862  ? 199.659 190.577 233.617 1.00 32.09 ? 812 ILE A CB  1 
ATOM 2575 C CG1 . ILE A 1 862  ? 198.774 189.582 234.369 1.00 32.46 ? 812 ILE A CG1 1 
ATOM 2576 C CG2 . ILE A 1 862  ? 200.643 191.251 234.560 1.00 33.30 ? 812 ILE A CG2 1 
ATOM 2577 C CD1 . ILE A 1 862  ? 199.462 188.268 234.660 1.00 28.96 ? 812 ILE A CD1 1 
ATOM 2578 N N   . SER A 1 863  ? 200.491 192.830 231.602 1.00 37.69 ? 813 SER A N   1 
ATOM 2579 C CA  . SER A 1 863  ? 201.283 194.007 231.252 1.00 33.95 ? 813 SER A CA  1 
ATOM 2580 C C   . SER A 1 863  ? 200.398 195.122 230.707 1.00 35.88 ? 813 SER A C   1 
ATOM 2581 O O   . SER A 1 863  ? 200.573 196.297 231.053 1.00 37.21 ? 813 SER A O   1 
ATOM 2582 C CB  . SER A 1 863  ? 202.363 193.630 230.237 1.00 32.79 ? 813 SER A CB  1 
ATOM 2583 O OG  . SER A 1 863  ? 201.817 192.876 229.170 1.00 30.03 ? 813 SER A OG  1 
ATOM 2584 N N   . HIS A 1 864  ? 199.444 194.747 229.850 1.00 35.03 ? 814 HIS A N   1 
ATOM 2585 C CA  . HIS A 1 864  ? 198.536 195.750 229.228 1.00 34.88 ? 814 HIS A CA  1 
ATOM 2586 C C   . HIS A 1 864  ? 197.691 196.425 230.312 1.00 38.43 ? 814 HIS A C   1 
ATOM 2587 O O   . HIS A 1 864  ? 197.285 197.590 230.121 1.00 35.70 ? 814 HIS A O   1 
ATOM 2588 C CB  . HIS A 1 864  ? 197.655 195.077 228.171 1.00 33.31 ? 814 HIS A CB  1 
ATOM 2589 C CG  . HIS A 1 864  ? 196.746 196.012 227.446 1.00 39.39 ? 814 HIS A CG  1 
ATOM 2590 N ND1 . HIS A 1 864  ? 197.106 197.300 227.114 1.00 36.85 ? 814 HIS A ND1 1 
ATOM 2591 C CD2 . HIS A 1 864  ? 195.498 195.847 226.992 1.00 41.61 ? 814 HIS A CD2 1 
ATOM 2592 C CE1 . HIS A 1 864  ? 196.101 197.885 226.480 1.00 35.19 ? 814 HIS A CE1 1 
ATOM 2593 N NE2 . HIS A 1 864  ? 195.114 197.020 226.394 1.00 40.62 ? 814 HIS A NE2 1 
ATOM 2594 N N   . SER A 1 865  ? 197.433 195.718 231.416 1.00 38.03 ? 815 SER A N   1 
ATOM 2595 C CA  . SER A 1 865  ? 196.567 196.270 232.490 1.00 36.35 ? 815 SER A CA  1 
ATOM 2596 C C   . SER A 1 865  ? 197.434 196.966 233.542 1.00 37.57 ? 815 SER A C   1 
ATOM 2597 O O   . SER A 1 865  ? 196.926 197.898 234.186 1.00 37.05 ? 815 SER A O   1 
ATOM 2598 C CB  . SER A 1 865  ? 195.723 195.189 233.111 1.00 35.77 ? 815 SER A CB  1 
ATOM 2599 O OG  . SER A 1 865  ? 196.534 194.252 233.804 1.00 32.78 ? 815 SER A OG  1 
ATOM 2600 N N   . SER A 1 866  ? 198.704 196.564 233.623 1.00 36.93 ? 816 SER A N   1 
ATOM 2601 C CA  . SER A 1 866  ? 199.638 197.124 234.631 1.00 37.00 ? 816 SER A CA  1 
ATOM 2602 C C   . SER A 1 866  ? 199.428 198.625 234.848 1.00 35.38 ? 816 SER A C   1 
ATOM 2603 O O   . SER A 1 866  ? 199.472 199.044 236.021 1.00 31.76 ? 816 SER A O   1 
ATOM 2604 C CB  . SER A 1 866  ? 201.069 196.827 234.254 1.00 36.41 ? 816 SER A CB  1 
ATOM 2605 O OG  . SER A 1 866  ? 201.358 195.448 234.429 1.00 39.38 ? 816 SER A OG  1 
ATOM 2606 N N   . LYS A 1 867  ? 199.216 199.402 233.780 1.00 39.77 ? 817 LYS A N   1 
ATOM 2607 C CA  . LYS A 1 867  ? 199.139 200.881 233.937 1.00 41.14 ? 817 LYS A CA  1 
ATOM 2608 C C   . LYS A 1 867  ? 197.705 201.395 233.756 1.00 38.98 ? 817 LYS A C   1 
ATOM 2609 O O   . LYS A 1 867  ? 197.469 202.575 234.073 1.00 35.64 ? 817 LYS A O   1 
ATOM 2610 C CB  . LYS A 1 867  ? 200.066 201.564 232.927 1.00 41.72 ? 817 LYS A CB  1 
ATOM 2611 C CG  . LYS A 1 867  ? 201.554 201.331 233.155 1.00 37.99 ? 817 LYS A CG  1 
ATOM 2612 C CD  . LYS A 1 867  ? 202.429 202.003 232.120 1.00 36.34 ? 817 LYS A CD  1 
ATOM 2613 C CE  . LYS A 1 867  ? 203.908 201.789 232.364 1.00 36.85 ? 817 LYS A CE  1 
ATOM 2614 N NZ  . LYS A 1 867  ? 204.737 202.439 231.322 1.00 37.76 ? 817 LYS A NZ  1 
ATOM 2615 N N   . VAL A 1 868  ? 196.791 200.561 233.255 1.00 35.46 ? 818 VAL A N   1 
ATOM 2616 C CA  . VAL A 1 868  ? 195.409 201.054 232.971 1.00 36.01 ? 818 VAL A CA  1 
ATOM 2617 C C   . VAL A 1 868  ? 194.460 200.569 234.073 1.00 34.44 ? 818 VAL A C   1 
ATOM 2618 O O   . VAL A 1 868  ? 193.364 201.149 234.202 1.00 31.63 ? 818 VAL A O   1 
ATOM 2619 C CB  . VAL A 1 868  ? 194.936 200.606 231.574 1.00 35.12 ? 818 VAL A CB  1 
ATOM 2620 C CG1 . VAL A 1 868  ? 193.768 201.443 231.076 1.00 36.45 ? 818 VAL A CG1 1 
ATOM 2621 C CG2 . VAL A 1 868  ? 196.075 200.630 230.567 1.00 30.59 ? 818 VAL A CG2 1 
ATOM 2622 N N   . LEU A 1 869  ? 194.874 199.563 234.848 1.00 34.76 ? 819 LEU A N   1 
ATOM 2623 C CA  . LEU A 1 869  ? 193.975 198.985 235.885 1.00 35.63 ? 819 LEU A CA  1 
ATOM 2624 C C   . LEU A 1 869  ? 193.604 200.052 236.921 1.00 36.27 ? 819 LEU A C   1 
ATOM 2625 O O   . LEU A 1 869  ? 192.733 199.761 237.764 1.00 42.36 ? 819 LEU A O   1 
ATOM 2626 C CB  . LEU A 1 869  ? 194.676 197.796 236.552 1.00 36.35 ? 819 LEU A CB  1 
ATOM 2627 C CG  . LEU A 1 869  ? 195.883 198.133 237.429 1.00 35.34 ? 819 LEU A CG  1 
ATOM 2628 C CD1 . LEU A 1 869  ? 195.484 198.237 238.893 1.00 34.35 ? 819 LEU A CD1 1 
ATOM 2629 C CD2 . LEU A 1 869  ? 196.977 197.090 237.262 1.00 33.71 ? 819 LEU A CD2 1 
ATOM 2630 N N   . HIS A 1 870  ? 194.223 201.236 236.867 1.00 34.11 ? 820 HIS A N   1 
ATOM 2631 C CA  . HIS A 1 870  ? 193.960 202.238 237.939 1.00 36.40 ? 820 HIS A CA  1 
ATOM 2632 C C   . HIS A 1 870  ? 193.483 203.578 237.364 1.00 41.28 ? 820 HIS A C   1 
ATOM 2633 O O   . HIS A 1 870  ? 192.968 204.405 238.147 1.00 40.85 ? 820 HIS A O   1 
ATOM 2634 C CB  . HIS A 1 870  ? 195.221 202.444 238.784 1.00 35.08 ? 820 HIS A CB  1 
ATOM 2635 C CG  . HIS A 1 870  ? 196.473 202.476 237.974 1.00 40.01 ? 820 HIS A CG  1 
ATOM 2636 N ND1 . HIS A 1 870  ? 197.431 201.488 238.039 1.00 39.77 ? 820 HIS A ND1 1 
ATOM 2637 C CD2 . HIS A 1 870  ? 196.921 203.369 237.082 1.00 40.25 ? 820 HIS A CD2 1 
ATOM 2638 C CE1 . HIS A 1 870  ? 198.422 201.787 237.212 1.00 40.04 ? 820 HIS A CE1 1 
ATOM 2639 N NE2 . HIS A 1 870  ? 198.132 202.925 236.620 1.00 40.36 ? 820 HIS A NE2 1 
ATOM 2640 N N   . PHE A 1 871  ? 193.653 203.797 236.057 1.00 35.11 ? 821 PHE A N   1 
ATOM 2641 C CA  . PHE A 1 871  ? 193.286 205.103 235.444 1.00 35.92 ? 821 PHE A CA  1 
ATOM 2642 C C   . PHE A 1 871  ? 191.901 205.547 235.934 1.00 37.00 ? 821 PHE A C   1 
ATOM 2643 O O   . PHE A 1 871  ? 190.967 204.719 235.922 1.00 33.86 ? 821 PHE A O   1 
ATOM 2644 C CB  . PHE A 1 871  ? 193.331 204.999 233.918 1.00 36.10 ? 821 PHE A CB  1 
ATOM 2645 C CG  . PHE A 1 871  ? 194.710 205.135 233.324 1.00 38.29 ? 821 PHE A CG  1 
ATOM 2646 C CD1 . PHE A 1 871  ? 195.746 205.689 234.058 1.00 38.38 ? 821 PHE A CD1 1 
ATOM 2647 C CD2 . PHE A 1 871  ? 194.972 204.713 232.031 1.00 35.26 ? 821 PHE A CD2 1 
ATOM 2648 C CE1 . PHE A 1 871  ? 197.014 205.816 233.513 1.00 36.99 ? 821 PHE A CE1 1 
ATOM 2649 C CE2 . PHE A 1 871  ? 196.240 204.841 231.486 1.00 36.73 ? 821 PHE A CE2 1 
ATOM 2650 C CZ  . PHE A 1 871  ? 197.258 205.392 232.228 1.00 36.62 ? 821 PHE A CZ  1 
ATOM 2651 N N   . PRO A 1 872  ? 191.713 206.824 236.347 1.00 38.93 ? 822 PRO A N   1 
ATOM 2652 C CA  . PRO A 1 872  ? 190.419 207.288 236.867 1.00 40.46 ? 822 PRO A CA  1 
ATOM 2653 C C   . PRO A 1 872  ? 189.275 206.996 235.906 1.00 40.16 ? 822 PRO A C   1 
ATOM 2654 O O   . PRO A 1 872  ? 189.382 207.213 234.697 1.00 37.23 ? 822 PRO A O   1 
ATOM 2655 C CB  . PRO A 1 872  ? 190.632 208.797 237.052 1.00 41.42 ? 822 PRO A CB  1 
ATOM 2656 C CG  . PRO A 1 872  ? 191.855 209.129 236.241 1.00 38.89 ? 822 PRO A CG  1 
ATOM 2657 C CD  . PRO A 1 872  ? 192.707 207.907 236.293 1.00 37.98 ? 822 PRO A CD  1 
ATOM 2658 N N   . ASN A 1 873  ? 188.163 206.512 236.467 1.00 36.18 ? 823 ASN A N   1 
ATOM 2659 C CA  . ASN A 1 873  ? 186.989 206.077 235.717 1.00 36.80 ? 823 ASN A CA  1 
ATOM 2660 C C   . ASN A 1 873  ? 187.388 205.067 234.646 1.00 35.48 ? 823 ASN A C   1 
ATOM 2661 O O   . ASN A 1 873  ? 187.433 205.411 233.457 1.00 29.14 ? 823 ASN A O   1 
ATOM 2662 C CB  . ASN A 1 873  ? 186.270 207.274 235.090 1.00 35.69 ? 823 ASN A CB  1 
ATOM 2663 C CG  . ASN A 1 873  ? 184.977 206.883 234.401 1.00 36.31 ? 823 ASN A CG  1 
ATOM 2664 O OD1 . ASN A 1 873  ? 184.743 207.239 233.246 1.00 38.01 ? 823 ASN A OD1 1 
ATOM 2665 N ND2 . ASN A 1 873  ? 184.128 206.147 235.110 1.00 35.22 ? 823 ASN A ND2 1 
ATOM 2666 N N   . PRO A 1 874  ? 187.712 203.831 235.026 1.00 37.14 ? 824 PRO A N   1 
ATOM 2667 C CA  . PRO A 1 874  ? 188.130 202.834 234.032 1.00 36.64 ? 824 PRO A CA  1 
ATOM 2668 C C   . PRO A 1 874  ? 187.089 202.650 232.936 1.00 36.41 ? 824 PRO A C   1 
ATOM 2669 O O   . PRO A 1 874  ? 185.896 202.489 233.204 1.00 34.30 ? 824 PRO A O   1 
ATOM 2670 C CB  . PRO A 1 874  ? 188.306 201.560 234.866 1.00 31.87 ? 824 PRO A CB  1 
ATOM 2671 C CG  . PRO A 1 874  ? 188.575 202.048 236.251 1.00 32.46 ? 824 PRO A CG  1 
ATOM 2672 C CD  . PRO A 1 874  ? 187.764 203.301 236.400 1.00 33.07 ? 824 PRO A CD  1 
ATOM 2673 N N   . GLU A 1 875  ? 187.555 202.675 231.689 1.00 41.18 ? 825 GLU A N   1 
ATOM 2674 C CA  . GLU A 1 875  ? 186.677 202.548 230.536 1.00 38.51 ? 825 GLU A CA  1 
ATOM 2675 C C   . GLU A 1 875  ? 186.318 201.087 230.283 1.00 37.88 ? 825 GLU A C   1 
ATOM 2676 O O   . GLU A 1 875  ? 186.937 200.161 230.814 1.00 36.34 ? 825 GLU A O   1 
ATOM 2677 C CB  . GLU A 1 875  ? 187.330 203.147 229.289 1.00 34.53 ? 825 GLU A CB  1 
ATOM 2678 C CG  . GLU A 1 875  ? 187.557 204.647 229.367 1.00 38.05 ? 825 GLU A CG  1 
ATOM 2679 C CD  . GLU A 1 875  ? 186.277 205.417 229.625 1.00 40.41 ? 825 GLU A CD  1 
ATOM 2680 O OE1 . GLU A 1 875  ? 185.236 205.053 229.039 1.00 43.53 ? 825 GLU A OE1 1 
ATOM 2681 O OE2 . GLU A 1 875  ? 186.311 206.383 230.415 1.00 36.91 ? 825 GLU A OE2 1 
ATOM 2682 N N   . ASP A 1 876  ? 185.296 200.892 229.447 1.00 40.52 ? 826 ASP A N   1 
ATOM 2683 C CA  . ASP A 1 876  ? 184.810 199.554 229.135 1.00 40.28 ? 826 ASP A CA  1 
ATOM 2684 C C   . ASP A 1 876  ? 185.657 198.851 228.084 1.00 39.53 ? 826 ASP A C   1 
ATOM 2685 O O   . ASP A 1 876  ? 185.425 197.667 227.819 1.00 39.00 ? 826 ASP A O   1 
ATOM 2686 C CB  . ASP A 1 876  ? 183.353 199.623 228.672 1.00 39.09 ? 826 ASP A CB  1 
ATOM 2687 C CG  . ASP A 1 876  ? 182.385 199.840 229.822 1.00 40.86 ? 826 ASP A CG  1 
ATOM 2688 O OD1 . ASP A 1 876  ? 182.789 200.457 230.831 1.00 41.94 ? 826 ASP A OD1 1 
ATOM 2689 O OD2 . ASP A 1 876  ? 181.224 199.392 229.721 1.00 38.57 ? 826 ASP A OD2 1 
ATOM 2690 N N   . LYS A 1 877  ? 186.620 199.575 227.504 1.00 41.09 ? 827 LYS A N   1 
ATOM 2691 C CA  . LYS A 1 877  ? 187.504 198.993 226.458 1.00 40.82 ? 827 LYS A CA  1 
ATOM 2692 C C   . LYS A 1 877  ? 188.190 197.742 227.016 1.00 39.86 ? 827 LYS A C   1 
ATOM 2693 O O   . LYS A 1 877  ? 188.079 196.676 226.380 1.00 34.95 ? 827 LYS A O   1 
ATOM 2694 C CB  . LYS A 1 877  ? 188.541 200.024 226.005 1.00 37.93 ? 827 LYS A CB  1 
ATOM 2695 C CG  . LYS A 1 877  ? 189.054 200.952 227.098 1.00 36.26 ? 827 LYS A CG  1 
ATOM 2696 C CD  . LYS A 1 877  ? 190.205 201.827 226.654 1.00 38.22 ? 827 LYS A CD  1 
ATOM 2697 C CE  . LYS A 1 877  ? 191.207 202.093 227.759 1.00 39.05 ? 827 LYS A CE  1 
ATOM 2698 N NZ  . LYS A 1 877  ? 190.734 203.141 228.692 1.00 39.52 ? 827 LYS A NZ  1 
ATOM 2699 N N   . LYS A 1 878  ? 188.889 197.886 228.146 1.00 39.45 ? 828 LYS A N   1 
ATOM 2700 C CA  . LYS A 1 878  ? 189.577 196.732 228.781 1.00 37.88 ? 828 LYS A CA  1 
ATOM 2701 C C   . LYS A 1 878  ? 188.559 195.612 228.993 1.00 37.07 ? 828 LYS A C   1 
ATOM 2702 O O   . LYS A 1 878  ? 188.826 194.479 228.551 1.00 35.77 ? 828 LYS A O   1 
ATOM 2703 C CB  . LYS A 1 878  ? 190.192 197.153 230.118 1.00 35.77 ? 828 LYS A CB  1 
ATOM 2704 C CG  . LYS A 1 878  ? 191.430 198.031 230.011 1.00 37.91 ? 828 LYS A CG  1 
ATOM 2705 C CD  . LYS A 1 878  ? 192.447 197.496 229.029 1.00 36.47 ? 828 LYS A CD  1 
ATOM 2706 C CE  . LYS A 1 878  ? 193.680 198.367 228.931 1.00 36.29 ? 828 LYS A CE  1 
ATOM 2707 N NZ  . LYS A 1 878  ? 193.490 199.477 227.967 1.00 37.49 ? 828 LYS A NZ  1 
ATOM 2708 N N   . LEU A 1 879  ? 187.436 195.930 229.643 1.00 36.08 ? 829 LEU A N   1 
ATOM 2709 C CA  . LEU A 1 879  ? 186.379 194.914 229.885 1.00 36.55 ? 829 LEU A CA  1 
ATOM 2710 C C   . LEU A 1 879  ? 186.149 194.132 228.590 1.00 37.56 ? 829 LEU A C   1 
ATOM 2711 O O   . LEU A 1 879  ? 186.131 192.892 228.649 1.00 38.39 ? 829 LEU A O   1 
ATOM 2712 C CB  . LEU A 1 879  ? 185.095 195.621 230.329 1.00 33.20 ? 829 LEU A CB  1 
ATOM 2713 C CG  . LEU A 1 879  ? 185.180 196.361 231.662 1.00 37.70 ? 829 LEU A CG  1 
ATOM 2714 C CD1 . LEU A 1 879  ? 183.838 196.980 232.022 1.00 38.76 ? 829 LEU A CD1 1 
ATOM 2715 C CD2 . LEU A 1 879  ? 185.649 195.429 232.768 1.00 36.97 ? 829 LEU A CD2 1 
ATOM 2716 N N   . GLU A 1 880  ? 185.997 194.836 227.466 1.00 34.43 ? 830 GLU A N   1 
ATOM 2717 C CA  . GLU A 1 880  ? 185.712 194.163 226.202 1.00 33.27 ? 830 GLU A CA  1 
ATOM 2718 C C   . GLU A 1 880  ? 186.898 193.325 225.740 1.00 34.69 ? 830 GLU A C   1 
ATOM 2719 O O   . GLU A 1 880  ? 186.720 192.206 225.243 1.00 32.23 ? 830 GLU A O   1 
ATOM 2720 C CB  . GLU A 1 880  ? 185.319 195.180 225.131 1.00 35.12 ? 830 GLU A CB  1 
ATOM 2721 C CG  . GLU A 1 880  ? 183.894 195.694 225.266 1.00 35.50 ? 830 GLU A CG  1 
ATOM 2722 C CD  . GLU A 1 880  ? 183.821 197.201 225.382 1.00 36.05 ? 830 GLU A CD  1 
ATOM 2723 O OE1 . GLU A 1 880  ? 184.817 197.870 225.045 1.00 34.79 ? 830 GLU A OE1 1 
ATOM 2724 O OE2 . GLU A 1 880  ? 182.770 197.717 225.816 1.00 36.69 ? 830 GLU A OE2 1 
ATOM 2725 N N   . GLU A 1 881  ? 188.115 193.845 225.896 1.00 35.38 ? 831 GLU A N   1 
ATOM 2726 C CA  . GLU A 1 881  ? 189.307 193.110 225.487 1.00 37.74 ? 831 GLU A CA  1 
ATOM 2727 C C   . GLU A 1 881  ? 189.475 191.820 226.284 1.00 37.30 ? 831 GLU A C   1 
ATOM 2728 O O   . GLU A 1 881  ? 189.727 190.754 225.705 1.00 37.14 ? 831 GLU A O   1 
ATOM 2729 C CB  . GLU A 1 881  ? 190.551 193.989 225.628 1.00 37.41 ? 831 GLU A CB  1 
ATOM 2730 C CG  . GLU A 1 881  ? 190.561 195.193 224.697 1.00 39.06 ? 831 GLU A CG  1 
ATOM 2731 C CD  . GLU A 1 881  ? 190.459 194.801 223.240 1.00 39.56 ? 831 GLU A CD  1 
ATOM 2732 O OE1 . GLU A 1 881  ? 191.093 193.801 222.851 1.00 37.69 ? 831 GLU A OE1 1 
ATOM 2733 O OE2 . GLU A 1 881  ? 189.745 195.492 222.483 1.00 38.78 ? 831 GLU A OE2 1 
ATOM 2734 N N   . ILE A 1 882  ? 189.330 191.895 227.611 1.00 33.80 ? 832 ILE A N   1 
ATOM 2735 C CA  . ILE A 1 882  ? 189.488 190.687 228.420 1.00 32.78 ? 832 ILE A CA  1 
ATOM 2736 C C   . ILE A 1 882  ? 188.335 189.723 228.170 1.00 32.26 ? 832 ILE A C   1 
ATOM 2737 O O   . ILE A 1 882  ? 188.512 188.501 228.218 1.00 32.60 ? 832 ILE A O   1 
ATOM 2738 C CB  . ILE A 1 882  ? 189.634 191.036 229.914 1.00 34.04 ? 832 ILE A CB  1 
ATOM 2739 C CG1 . ILE A 1 882  ? 190.066 189.817 230.723 1.00 31.96 ? 832 ILE A CG1 1 
ATOM 2740 C CG2 . ILE A 1 882  ? 188.332 191.615 230.451 1.00 35.90 ? 832 ILE A CG2 1 
ATOM 2741 C CD1 . ILE A 1 882  ? 191.450 189.325 230.389 1.00 29.45 ? 832 ILE A CD1 1 
ATOM 2742 N N   . ILE A 1 883  ? 187.155 190.273 227.870 1.00 31.22 ? 833 ILE A N   1 
ATOM 2743 C CA  . ILE A 1 883  ? 185.996 189.398 227.524 1.00 33.60 ? 833 ILE A CA  1 
ATOM 2744 C C   . ILE A 1 883  ? 186.369 188.610 226.266 1.00 34.43 ? 833 ILE A C   1 
ATOM 2745 O O   . ILE A 1 883  ? 186.200 187.375 226.271 1.00 32.92 ? 833 ILE A O   1 
ATOM 2746 C CB  . ILE A 1 883  ? 184.715 190.231 227.319 1.00 37.26 ? 833 ILE A CB  1 
ATOM 2747 C CG1 . ILE A 1 883  ? 184.046 190.587 228.649 1.00 35.46 ? 833 ILE A CG1 1 
ATOM 2748 C CG2 . ILE A 1 883  ? 183.749 189.524 226.380 1.00 33.70 ? 833 ILE A CG2 1 
ATOM 2749 C CD1 . ILE A 1 883  ? 183.004 191.675 228.532 1.00 32.75 ? 833 ILE A CD1 1 
ATOM 2750 N N   . HIS A 1 884  ? 186.882 189.299 225.240 1.00 35.36 ? 834 HIS A N   1 
ATOM 2751 C CA  . HIS A 1 884  ? 187.210 188.628 223.988 1.00 35.43 ? 834 HIS A CA  1 
ATOM 2752 C C   . HIS A 1 884  ? 188.300 187.585 224.194 1.00 35.52 ? 834 HIS A C   1 
ATOM 2753 O O   . HIS A 1 884  ? 188.220 186.478 223.648 1.00 32.33 ? 834 HIS A O   1 
ATOM 2754 C CB  . HIS A 1 884  ? 187.632 189.654 222.937 1.00 32.33 ? 834 HIS A CB  1 
ATOM 2755 C CG  . HIS A 1 884  ? 187.053 189.397 221.581 1.00 33.59 ? 834 HIS A CG  1 
ATOM 2756 N ND1 . HIS A 1 884  ? 187.181 188.187 220.934 1.00 29.32 ? 834 HIS A ND1 1 
ATOM 2757 C CD2 . HIS A 1 884  ? 186.336 190.192 220.752 1.00 34.43 ? 834 HIS A CD2 1 
ATOM 2758 C CE1 . HIS A 1 884  ? 186.572 188.248 219.764 1.00 30.46 ? 834 HIS A CE1 1 
ATOM 2759 N NE2 . HIS A 1 884  ? 186.051 189.455 219.629 1.00 32.72 ? 834 HIS A NE2 1 
ATOM 2760 N N   . GLN A 1 885  ? 189.305 187.920 225.005 1.00 33.29 ? 835 GLN A N   1 
ATOM 2761 C CA  . GLN A 1 885  ? 190.390 186.946 225.300 1.00 31.69 ? 835 GLN A CA  1 
ATOM 2762 C C   . GLN A 1 885  ? 189.792 185.718 225.992 1.00 32.06 ? 835 GLN A C   1 
ATOM 2763 O O   . GLN A 1 885  ? 190.100 184.592 225.557 1.00 32.08 ? 835 GLN A O   1 
ATOM 2764 C CB  . GLN A 1 885  ? 191.460 187.602 226.175 1.00 33.16 ? 835 GLN A CB  1 
ATOM 2765 C CG  . GLN A 1 885  ? 192.533 186.638 226.659 1.00 32.91 ? 835 GLN A CG  1 
ATOM 2766 C CD  . GLN A 1 885  ? 192.318 186.218 228.092 1.00 30.10 ? 835 GLN A CD  1 
ATOM 2767 O OE1 . GLN A 1 885  ? 191.725 186.943 228.889 1.00 27.47 ? 835 GLN A OE1 1 
ATOM 2768 N NE2 . GLN A 1 885  ? 192.798 185.033 228.431 1.00 26.61 ? 835 GLN A NE2 1 
ATOM 2769 N N   . ILE A 1 886  ? 188.953 185.925 227.011 1.00 27.63 ? 836 ILE A N   1 
ATOM 2770 C CA  . ILE A 1 886  ? 188.394 184.818 227.781 1.00 29.31 ? 836 ILE A CA  1 
ATOM 2771 C C   . ILE A 1 886  ? 187.533 183.935 226.890 1.00 31.18 ? 836 ILE A C   1 
ATOM 2772 O O   . ILE A 1 886  ? 187.629 182.702 226.928 1.00 28.59 ? 836 ILE A O   1 
ATOM 2773 C CB  . ILE A 1 886  ? 187.595 185.354 228.984 1.00 28.94 ? 836 ILE A CB  1 
ATOM 2774 C CG1 . ILE A 1 886  ? 188.540 185.825 230.091 1.00 28.77 ? 836 ILE A CG1 1 
ATOM 2775 C CG2 . ILE A 1 886  ? 186.640 184.295 229.513 1.00 27.96 ? 836 ILE A CG2 1 
ATOM 2776 C CD1 . ILE A 1 886  ? 187.945 186.895 230.983 1.00 30.19 ? 836 ILE A CD1 1 
ATOM 2777 N N   . THR A 1 887  ? 186.680 184.553 226.068 1.00 31.25 ? 837 THR A N   1 
ATOM 2778 C CA  . THR A 1 887  ? 185.792 183.760 225.226 1.00 29.61 ? 837 THR A CA  1 
ATOM 2779 C C   . THR A 1 887  ? 186.575 183.012 224.152 1.00 29.23 ? 837 THR A C   1 
ATOM 2780 O O   . THR A 1 887  ? 186.257 181.858 223.845 1.00 27.21 ? 837 THR A O   1 
ATOM 2781 C CB  . THR A 1 887  ? 184.691 184.640 224.620 1.00 27.15 ? 837 THR A CB  1 
ATOM 2782 O OG1 . THR A 1 887  ? 183.654 183.806 224.085 1.00 24.48 ? 837 THR A OG1 1 
ATOM 2783 C CG2 . THR A 1 887  ? 185.221 185.547 223.520 1.00 28.65 ? 837 THR A CG2 1 
ATOM 2784 N N   . ASN A 1 888  ? 187.630 183.625 223.602 1.00 27.07 ? 838 ASN A N   1 
ATOM 2785 C CA  . ASN A 1 888  ? 188.447 182.923 222.619 1.00 30.69 ? 838 ASN A CA  1 
ATOM 2786 C C   . ASN A 1 888  ? 189.141 181.717 223.241 1.00 34.83 ? 838 ASN A C   1 
ATOM 2787 O O   . ASN A 1 888  ? 189.148 180.627 222.655 1.00 31.17 ? 838 ASN A O   1 
ATOM 2788 C CB  . ASN A 1 888  ? 189.469 183.879 222.005 1.00 31.02 ? 838 ASN A CB  1 
ATOM 2789 C CG  . ASN A 1 888  ? 188.850 184.816 220.985 1.00 35.12 ? 838 ASN A CG  1 
ATOM 2790 O OD1 . ASN A 1 888  ? 187.821 184.506 220.385 1.00 33.08 ? 838 ASN A OD1 1 
ATOM 2791 N ND2 . ASN A 1 888  ? 189.477 185.969 220.782 1.00 34.47 ? 838 ASN A ND2 1 
ATOM 2792 N N   . VAL A 1 889  ? 189.709 181.910 224.432 1.00 34.41 ? 839 VAL A N   1 
ATOM 2793 C CA  . VAL A 1 889  ? 190.430 180.795 225.112 1.00 32.69 ? 839 VAL A CA  1 
ATOM 2794 C C   . VAL A 1 889  ? 189.432 179.673 225.418 1.00 33.21 ? 839 VAL A C   1 
ATOM 2795 O O   . VAL A 1 889  ? 189.737 178.510 225.087 1.00 32.27 ? 839 VAL A O   1 
ATOM 2796 C CB  . VAL A 1 889  ? 191.141 181.279 226.389 1.00 27.38 ? 839 VAL A CB  1 
ATOM 2797 C CG1 . VAL A 1 889  ? 191.769 180.119 227.139 1.00 26.37 ? 839 VAL A CG1 1 
ATOM 2798 C CG2 . VAL A 1 889  ? 192.184 182.343 226.082 1.00 27.53 ? 839 VAL A CG2 1 
ATOM 2799 N N   . GLU A 1 890  ? 188.285 180.011 226.018 1.00 30.07 ? 840 GLU A N   1 
ATOM 2800 C CA  . GLU A 1 890  ? 187.297 178.971 226.422 1.00 28.39 ? 840 GLU A CA  1 
ATOM 2801 C C   . GLU A 1 890  ? 186.760 178.253 225.177 1.00 32.11 ? 840 GLU A C   1 
ATOM 2802 O O   . GLU A 1 890  ? 186.583 177.023 225.247 1.00 35.82 ? 840 GLU A O   1 
ATOM 2803 C CB  . GLU A 1 890  ? 186.185 179.583 227.282 1.00 29.41 ? 840 GLU A CB  1 
ATOM 2804 C CG  . GLU A 1 890  ? 185.153 180.376 226.502 1.00 34.34 ? 840 GLU A CG  1 
ATOM 2805 C CD  . GLU A 1 890  ? 184.392 181.398 227.329 1.00 36.52 ? 840 GLU A CD  1 
ATOM 2806 O OE1 . GLU A 1 890  ? 184.787 181.630 228.486 1.00 32.48 ? 840 GLU A OE1 1 
ATOM 2807 O OE2 . GLU A 1 890  ? 183.409 181.962 226.810 1.00 31.09 ? 840 GLU A OE2 1 
ATOM 2808 N N   . ALA A 1 891  ? 186.513 178.982 224.084 1.00 25.74 ? 841 ALA A N   1 
ATOM 2809 C CA  . ALA A 1 891  ? 186.079 178.331 222.853 1.00 29.78 ? 841 ALA A CA  1 
ATOM 2810 C C   . ALA A 1 891  ? 187.155 177.396 222.320 1.00 33.81 ? 841 ALA A C   1 
ATOM 2811 O O   . ALA A 1 891  ? 186.852 176.295 221.849 1.00 30.31 ? 841 ALA A O   1 
ATOM 2812 C CB  . ALA A 1 891  ? 185.711 179.382 221.806 1.00 29.45 ? 841 ALA A CB  1 
ATOM 2813 N N   . LEU A 1 892  ? 188.421 177.817 222.390 1.00 33.68 ? 842 LEU A N   1 
ATOM 2814 C CA  . LEU A 1 892  ? 189.511 176.971 221.916 1.00 35.00 ? 842 LEU A CA  1 
ATOM 2815 C C   . LEU A 1 892  ? 189.591 175.678 222.719 1.00 30.40 ? 842 LEU A C   1 
ATOM 2816 O O   . LEU A 1 892  ? 189.738 174.587 222.154 1.00 30.74 ? 842 LEU A O   1 
ATOM 2817 C CB  . LEU A 1 892  ? 190.832 177.737 221.993 1.00 29.89 ? 842 LEU A CB  1 
ATOM 2818 C CG  . LEU A 1 892  ? 191.380 178.332 220.693 1.00 31.59 ? 842 LEU A CG  1 
ATOM 2819 C CD1 . LEU A 1 892  ? 191.906 177.235 219.782 1.00 29.46 ? 842 LEU A CD1 1 
ATOM 2820 C CD2 . LEU A 1 892  ? 190.326 179.168 219.982 1.00 30.76 ? 842 LEU A CD2 1 
ATOM 2821 N N   . ILE A 1 893  ? 189.479 175.787 224.045 1.00 23.74 ? 843 ILE A N   1 
ATOM 2822 C CA  . ILE A 1 893  ? 189.623 174.569 224.899 1.00 24.90 ? 843 ILE A CA  1 
ATOM 2823 C C   . ILE A 1 893  ? 188.381 173.683 224.724 1.00 27.88 ? 843 ILE A C   1 
ATOM 2824 O O   . ILE A 1 893  ? 188.531 172.449 224.802 1.00 28.19 ? 843 ILE A O   1 
ATOM 2825 C CB  . ILE A 1 893  ? 189.893 174.943 226.372 1.00 28.19 ? 843 ILE A CB  1 
ATOM 2826 C CG1 . ILE A 1 893  ? 190.561 173.795 227.133 1.00 32.21 ? 843 ILE A CG1 1 
ATOM 2827 C CG2 . ILE A 1 893  ? 188.625 175.413 227.063 1.00 27.65 ? 843 ILE A CG2 1 
ATOM 2828 C CD1 . ILE A 1 893  ? 190.777 174.078 228.600 1.00 29.12 ? 843 ILE A CD1 1 
ATOM 2829 N N   . ALA A 1 894  ? 187.210 174.281 224.473 1.00 26.95 ? 844 ALA A N   1 
ATOM 2830 C CA  . ALA A 1 894  ? 185.984 173.487 224.229 1.00 30.96 ? 844 ALA A CA  1 
ATOM 2831 C C   . ALA A 1 894  ? 186.151 172.697 222.928 1.00 31.64 ? 844 ALA A C   1 
ATOM 2832 O O   . ALA A 1 894  ? 185.846 171.489 222.925 1.00 25.81 ? 844 ALA A O   1 
ATOM 2833 C CB  . ALA A 1 894  ? 184.783 174.396 224.171 1.00 30.98 ? 844 ALA A CB  1 
ATOM 2834 N N   . ARG A 1 895  ? 186.624 173.363 221.871 1.00 30.22 ? 845 ARG A N   1 
ATOM 2835 C CA  . ARG A 1 895  ? 186.813 172.690 220.558 1.00 30.12 ? 845 ARG A CA  1 
ATOM 2836 C C   . ARG A 1 895  ? 187.843 171.567 220.716 1.00 29.77 ? 845 ARG A C   1 
ATOM 2837 O O   . ARG A 1 895  ? 187.593 170.463 220.196 1.00 31.59 ? 845 ARG A O   1 
ATOM 2838 C CB  . ARG A 1 895  ? 187.244 173.711 219.501 1.00 27.62 ? 845 ARG A CB  1 
ATOM 2839 C CG  . ARG A 1 895  ? 187.221 173.178 218.076 1.00 28.11 ? 845 ARG A CG  1 
ATOM 2840 C CD  . ARG A 1 895  ? 186.946 174.287 217.078 1.00 28.68 ? 845 ARG A CD  1 
ATOM 2841 N NE  . ARG A 1 895  ? 185.635 174.887 217.283 1.00 34.71 ? 845 ARG A NE  1 
ATOM 2842 C CZ  . ARG A 1 895  ? 185.431 176.164 217.586 1.00 35.18 ? 845 ARG A CZ  1 
ATOM 2843 N NH1 . ARG A 1 895  ? 184.208 176.662 217.565 1.00 32.00 ? 845 ARG A NH1 1 
ATOM 2844 N NH2 . ARG A 1 895  ? 186.453 176.940 217.902 1.00 33.80 ? 845 ARG A NH2 1 
ATOM 2845 N N   . ALA A 1 896  ? 188.951 171.841 221.411 1.00 28.23 ? 846 ALA A N   1 
ATOM 2846 C CA  . ALA A 1 896  ? 189.975 170.798 221.652 1.00 30.52 ? 846 ALA A CA  1 
ATOM 2847 C C   . ALA A 1 896  ? 189.303 169.572 222.278 1.00 26.41 ? 846 ALA A C   1 
ATOM 2848 O O   . ALA A 1 896  ? 189.456 168.467 221.723 1.00 26.15 ? 846 ALA A O   1 
ATOM 2849 C CB  . ALA A 1 896  ? 191.067 171.343 222.537 1.00 29.56 ? 846 ALA A CB  1 
ATOM 2850 N N   . ARG A 1 897  ? 188.582 169.769 223.386 1.00 22.98 ? 847 ARG A N   1 
ATOM 2851 C CA  . ARG A 1 897  ? 187.906 168.660 224.052 1.00 25.27 ? 847 ARG A CA  1 
ATOM 2852 C C   . ARG A 1 897  ? 186.946 167.953 223.105 1.00 26.84 ? 847 ARG A C   1 
ATOM 2853 O O   . ARG A 1 897  ? 186.884 166.719 223.078 1.00 29.74 ? 847 ARG A O   1 
ATOM 2854 C CB  . ARG A 1 897  ? 187.155 169.154 225.288 1.00 27.71 ? 847 ARG A CB  1 
ATOM 2855 C CG  . ARG A 1 897  ? 188.031 169.704 226.399 1.00 30.15 ? 847 ARG A CG  1 
ATOM 2856 C CD  . ARG A 1 897  ? 187.162 170.248 227.519 1.00 30.16 ? 847 ARG A CD  1 
ATOM 2857 N NE  . ARG A 1 897  ? 186.361 169.220 228.170 1.00 28.16 ? 847 ARG A NE  1 
ATOM 2858 C CZ  . ARG A 1 897  ? 185.444 169.465 229.095 1.00 27.17 ? 847 ARG A CZ  1 
ATOM 2859 N NH1 . ARG A 1 897  ? 185.197 170.695 229.514 1.00 27.52 ? 847 ARG A NH1 1 
ATOM 2860 N NH2 . ARG A 1 897  ? 184.758 168.453 229.613 1.00 26.11 ? 847 ARG A NH2 1 
ATOM 2861 N N   . SER A 1 898  ? 186.192 168.719 222.316 1.00 23.16 ? 848 SER A N   1 
ATOM 2862 C CA  . SER A 1 898  ? 185.250 168.113 221.381 1.00 24.35 ? 848 SER A CA  1 
ATOM 2863 C C   . SER A 1 898  ? 185.971 167.285 220.325 1.00 24.47 ? 848 SER A C   1 
ATOM 2864 O O   . SER A 1 898  ? 185.511 166.198 219.964 1.00 22.20 ? 848 SER A O   1 
ATOM 2865 C CB  . SER A 1 898  ? 184.393 169.196 220.726 1.00 25.30 ? 848 SER A CB  1 
ATOM 2866 O OG  . SER A 1 898  ? 185.096 169.836 219.676 1.00 29.65 ? 848 SER A OG  1 
ATOM 2867 N N   . LEU A 1 899  ? 187.098 167.781 219.814 1.00 21.78 ? 849 LEU A N   1 
ATOM 2868 C CA  . LEU A 1 899  ? 187.843 167.039 218.802 1.00 21.41 ? 849 LEU A CA  1 
ATOM 2869 C C   . LEU A 1 899  ? 188.374 165.727 219.368 1.00 25.56 ? 849 LEU A C   1 
ATOM 2870 O O   . LEU A 1 899  ? 188.216 164.659 218.756 1.00 22.96 ? 849 LEU A O   1 
ATOM 2871 C CB  . LEU A 1 899  ? 188.986 167.902 218.266 1.00 21.67 ? 849 LEU A CB  1 
ATOM 2872 C CG  . LEU A 1 899  ? 189.543 167.574 216.881 1.00 29.20 ? 849 LEU A CG  1 
ATOM 2873 C CD1 . LEU A 1 899  ? 188.416 167.533 215.868 1.00 25.72 ? 849 LEU A CD1 1 
ATOM 2874 C CD2 . LEU A 1 899  ? 190.595 168.593 216.474 1.00 28.10 ? 849 LEU A CD2 1 
ATOM 2875 N N   . LYS A 1 900  ? 189.015 165.813 220.537 1.00 26.53 ? 850 LYS A N   1 
ATOM 2876 C CA  . LYS A 1 900  ? 189.548 164.593 221.197 1.00 22.71 ? 850 LYS A CA  1 
ATOM 2877 C C   . LYS A 1 900  ? 188.394 163.617 221.432 1.00 21.32 ? 850 LYS A C   1 
ATOM 2878 O O   . LYS A 1 900  ? 188.609 162.403 221.261 1.00 22.90 ? 850 LYS A O   1 
ATOM 2879 C CB  . LYS A 1 900  ? 190.218 164.958 222.524 1.00 21.58 ? 850 LYS A CB  1 
ATOM 2880 C CG  . LYS A 1 900  ? 191.461 165.828 222.408 1.00 22.03 ? 850 LYS A CG  1 
ATOM 2881 C CD  . LYS A 1 900  ? 192.085 166.160 223.743 1.00 26.60 ? 850 LYS A CD  1 
ATOM 2882 C CE  . LYS A 1 900  ? 193.291 167.065 223.616 1.00 25.50 ? 850 LYS A CE  1 
ATOM 2883 N NZ  . LYS A 1 900  ? 194.385 166.418 222.854 1.00 24.41 ? 850 LYS A NZ  1 
ATOM 2884 N N   . ALA A 1 901  ? 187.221 164.133 221.809 1.00 21.12 ? 851 ALA A N   1 
ATOM 2885 C CA  . ALA A 1 901  ? 186.082 163.268 222.096 1.00 21.14 ? 851 ALA A CA  1 
ATOM 2886 C C   . ALA A 1 901  ? 185.548 162.604 220.834 1.00 26.74 ? 851 ALA A C   1 
ATOM 2887 O O   . ALA A 1 901  ? 185.159 161.430 220.870 1.00 28.38 ? 851 ALA A O   1 
ATOM 2888 C CB  . ALA A 1 901  ? 184.977 164.067 222.785 1.00 17.19 ? 851 ALA A CB  1 
ATOM 2889 N N   . LYS A 1 902  ? 185.586 163.322 219.708 1.00 21.85 ? 852 LYS A N   1 
ATOM 2890 C CA  . LYS A 1 902  ? 185.098 162.746 218.425 1.00 20.89 ? 852 LYS A CA  1 
ATOM 2891 C C   . LYS A 1 902  ? 186.070 161.665 217.931 1.00 21.62 ? 852 LYS A C   1 
ATOM 2892 O O   . LYS A 1 902  ? 185.585 160.639 217.415 1.00 14.94 ? 852 LYS A O   1 
ATOM 2893 C CB  . LYS A 1 902  ? 184.900 163.839 217.369 1.00 22.49 ? 852 LYS A CB  1 
ATOM 2894 C CG  . LYS A 1 902  ? 183.776 164.832 217.651 1.00 19.76 ? 852 LYS A CG  1 
ATOM 2895 C CD  . LYS A 1 902  ? 182.410 164.209 217.899 1.00 23.33 ? 852 LYS A CD  1 
ATOM 2896 C CE  . LYS A 1 902  ? 181.495 165.100 218.711 1.00 22.17 ? 852 LYS A CE  1 
ATOM 2897 N NZ  . LYS A 1 902  ? 180.318 164.358 219.220 1.00 21.40 ? 852 LYS A NZ  1 
ATOM 2898 N N   . PHE A 1 903  ? 187.383 161.882 218.075 1.00 24.65 ? 853 PHE A N   1 
ATOM 2899 C CA  . PHE A 1 903  ? 188.359 160.914 217.585 1.00 22.43 ? 853 PHE A CA  1 
ATOM 2900 C C   . PHE A 1 903  ? 188.889 159.989 218.672 1.00 24.61 ? 853 PHE A C   1 
ATOM 2901 O O   . PHE A 1 903  ? 189.710 159.114 218.376 1.00 20.35 ? 853 PHE A O   1 
ATOM 2902 C CB  . PHE A 1 903  ? 189.509 161.634 216.884 1.00 18.14 ? 853 PHE A CB  1 
ATOM 2903 C CG  . PHE A 1 903  ? 189.088 162.344 215.637 1.00 17.19 ? 853 PHE A CG  1 
ATOM 2904 C CD1 . PHE A 1 903  ? 189.012 161.664 214.435 1.00 17.47 ? 853 PHE A CD1 1 
ATOM 2905 C CD2 . PHE A 1 903  ? 188.739 163.681 215.670 1.00 19.30 ? 853 PHE A CD2 1 
ATOM 2906 C CE1 . PHE A 1 903  ? 188.615 162.309 213.286 1.00 22.67 ? 853 PHE A CE1 1 
ATOM 2907 C CE2 . PHE A 1 903  ? 188.339 164.330 214.523 1.00 18.74 ? 853 PHE A CE2 1 
ATOM 2908 C CZ  . PHE A 1 903  ? 188.278 163.644 213.329 1.00 25.15 ? 853 PHE A CZ  1 
ATOM 2909 N N   . GLY A 1 904  ? 188.440 160.156 219.914 1.00 26.20 ? 854 GLY A N   1 
ATOM 2910 C CA  . GLY A 1 904  ? 188.723 159.196 220.965 1.00 23.40 ? 854 GLY A CA  1 
ATOM 2911 C C   . GLY A 1 904  ? 190.192 158.912 221.194 1.00 20.33 ? 854 GLY A C   1 
ATOM 2912 O O   . GLY A 1 904  ? 190.604 157.748 221.196 1.00 24.34 ? 854 GLY A O   1 
ATOM 2913 N N   . THR A 1 905  ? 190.996 159.963 221.373 1.00 17.22 ? 855 THR A N   1 
ATOM 2914 C CA  . THR A 1 905  ? 192.428 159.767 221.571 1.00 23.68 ? 855 THR A CA  1 
ATOM 2915 C C   . THR A 1 905  ? 192.707 158.898 222.791 1.00 26.23 ? 855 THR A C   1 
ATOM 2916 O O   . THR A 1 905  ? 193.646 158.094 222.789 1.00 26.66 ? 855 THR A O   1 
ATOM 2917 C CB  . THR A 1 905  ? 193.138 161.117 221.700 1.00 25.33 ? 855 THR A CB  1 
ATOM 2918 O OG1 . THR A 1 905  ? 194.524 160.900 221.988 1.00 24.03 ? 855 THR A OG1 1 
ATOM 2919 C CG2 . THR A 1 905  ? 192.516 161.962 222.804 1.00 24.30 ? 855 THR A CG2 1 
ATOM 2920 N N   . GLU A 1 906  ? 191.893 159.062 223.837 1.00 25.31 ? 856 GLU A N   1 
ATOM 2921 C CA  . GLU A 1 906  ? 192.100 158.276 225.082 1.00 25.63 ? 856 GLU A CA  1 
ATOM 2922 C C   . GLU A 1 906  ? 191.267 156.994 225.004 1.00 23.12 ? 856 GLU A C   1 
ATOM 2923 O O   . GLU A 1 906  ? 191.458 156.113 225.865 1.00 22.08 ? 856 GLU A O   1 
ATOM 2924 C CB  . GLU A 1 906  ? 191.742 159.109 226.313 1.00 26.41 ? 856 GLU A CB  1 
ATOM 2925 C CG  . GLU A 1 906  ? 192.684 160.279 226.538 1.00 27.86 ? 856 GLU A CG  1 
ATOM 2926 C CD  . GLU A 1 906  ? 192.324 161.176 227.710 1.00 30.02 ? 856 GLU A CD  1 
ATOM 2927 O OE1 . GLU A 1 906  ? 191.217 161.011 228.262 1.00 30.41 ? 856 GLU A OE1 1 
ATOM 2928 O OE2 . GLU A 1 906  ? 193.148 162.043 228.066 1.00 28.63 ? 856 GLU A OE2 1 
ATOM 2929 N N   . LYS A 1 907  ? 190.386 156.898 224.004 1.00 25.67 ? 857 LYS A N   1 
ATOM 2930 C CA  . LYS A 1 907  ? 189.569 155.668 223.829 1.00 28.89 ? 857 LYS A CA  1 
ATOM 2931 C C   . LYS A 1 907  ? 190.411 154.632 223.078 1.00 27.14 ? 857 LYS A C   1 
ATOM 2932 O O   . LYS A 1 907  ? 189.891 154.036 222.114 1.00 24.16 ? 857 LYS A O   1 
ATOM 2933 C CB  . LYS A 1 907  ? 188.270 155.991 223.085 1.00 31.12 ? 857 LYS A CB  1 
ATOM 2934 C CG  . LYS A 1 907  ? 187.289 156.871 223.847 1.00 28.48 ? 857 LYS A CG  1 
ATOM 2935 C CD  . LYS A 1 907  ? 186.031 157.186 223.066 1.00 24.98 ? 857 LYS A CD  1 
ATOM 2936 C CE  . LYS A 1 907  ? 185.049 158.042 223.838 1.00 23.36 ? 857 LYS A CE  1 
ATOM 2937 N NZ  . LYS A 1 907  ? 183.841 158.350 223.038 1.00 22.25 ? 857 LYS A NZ  1 
ATOM 2938 N N   . CYS A 1 908  ? 191.661 154.436 223.506 1.00 27.10 ? 858 CYS A N   1 
ATOM 2939 C CA  . CYS A 1 908  ? 192.568 153.459 222.846 1.00 30.21 ? 858 CYS A CA  1 
ATOM 2940 C C   . CYS A 1 908  ? 193.520 152.873 223.893 1.00 33.50 ? 858 CYS A C   1 
ATOM 2941 O O   . CYS A 1 908  ? 193.877 153.604 224.837 1.00 30.37 ? 858 CYS A O   1 
ATOM 2942 C CB  . CYS A 1 908  ? 193.369 154.128 221.736 1.00 27.84 ? 858 CYS A CB  1 
ATOM 2943 S SG  . CYS A 1 908  ? 194.744 153.117 221.127 1.00 37.79 ? 858 CYS A SG  1 
ATOM 2944 N N   . GLU A 1 909  ? 193.903 151.605 223.733 1.00 32.82 ? 859 GLU A N   1 
ATOM 2945 C CA  . GLU A 1 909  ? 194.812 150.935 224.695 1.00 25.45 ? 859 GLU A CA  1 
ATOM 2946 C C   . GLU A 1 909  ? 196.271 151.135 224.281 1.00 28.34 ? 859 GLU A C   1 
ATOM 2947 O O   . GLU A 1 909  ? 197.130 151.253 225.163 1.00 28.99 ? 859 GLU A O   1 
ATOM 2948 C CB  . GLU A 1 909  ? 194.423 149.463 224.694 1.00 24.09 ? 859 GLU A CB  1 
ATOM 2949 C CG  . GLU A 1 909  ? 193.019 149.209 225.229 1.00 25.58 ? 859 GLU A CG  1 
ATOM 2950 C CD  . GLU A 1 909  ? 191.886 149.348 224.226 1.00 32.27 ? 859 GLU A CD  1 
ATOM 2951 O OE1 . GLU A 1 909  ? 192.164 149.710 223.066 1.00 32.35 ? 859 GLU A OE1 1 
ATOM 2952 O OE2 . GLU A 1 909  ? 190.729 149.086 224.608 1.00 33.67 ? 859 GLU A OE2 1 
ATOM 2953 N N   . GLN A 1 910  ? 196.523 151.207 222.985 1.00 32.28 ? 860 GLN A N   1 
ATOM 2954 C CA  . GLN A 1 910  ? 197.929 151.274 222.501 1.00 33.59 ? 860 GLN A CA  1 
ATOM 2955 C C   . GLN A 1 910  ? 198.491 152.666 222.798 1.00 34.05 ? 860 GLN A C   1 
ATOM 2956 O O   . GLN A 1 910  ? 198.045 153.627 222.145 1.00 28.06 ? 860 GLN A O   1 
ATOM 2957 C CB  . GLN A 1 910  ? 198.006 150.958 221.006 1.00 34.09 ? 860 GLN A CB  1 
ATOM 2958 C CG  . GLN A 1 910  ? 199.432 150.815 220.495 1.00 31.58 ? 860 GLN A CG  1 
ATOM 2959 C CD  . GLN A 1 910  ? 199.495 150.731 218.990 1.00 34.78 ? 860 GLN A CD  1 
ATOM 2960 O OE1 . GLN A 1 910  ? 198.652 150.110 218.347 1.00 33.16 ? 860 GLN A OE1 1 
ATOM 2961 N NE2 . GLN A 1 910  ? 200.502 151.366 218.412 1.00 34.57 ? 860 GLN A NE2 1 
ATOM 2962 N N   . GLU A 1 911  ? 199.449 152.759 223.726 1.00 35.84 ? 861 GLU A N   1 
ATOM 2963 C CA  . GLU A 1 911  ? 200.007 154.078 224.129 1.00 35.31 ? 861 GLU A CA  1 
ATOM 2964 C C   . GLU A 1 911  ? 200.561 154.802 222.899 1.00 33.76 ? 861 GLU A C   1 
ATOM 2965 O O   . GLU A 1 911  ? 200.237 155.992 222.723 1.00 32.69 ? 861 GLU A O   1 
ATOM 2966 C CB  . GLU A 1 911  ? 201.101 153.888 225.181 1.00 30.99 ? 861 GLU A CB  1 
ATOM 2967 C CG  . GLU A 1 911  ? 200.577 153.362 226.504 1.00 30.10 ? 861 GLU A CG  1 
ATOM 2968 C CD  . GLU A 1 911  ? 201.652 153.097 227.543 1.00 33.94 ? 861 GLU A CD  1 
ATOM 2969 O OE1 . GLU A 1 911  ? 202.844 153.141 227.182 1.00 32.06 ? 861 GLU A OE1 1 
ATOM 2970 O OE2 . GLU A 1 911  ? 201.294 152.849 228.711 1.00 37.48 ? 861 GLU A OE2 1 
ATOM 2971 N N   . GLU A 1 912  ? 201.255 154.045 222.022 1.00 31.01 ? 862 GLU A N   1 
ATOM 2972 C CA  . GLU A 1 912  ? 201.974 154.639 220.851 1.00 33.17 ? 862 GLU A CA  1 
ATOM 2973 C C   . GLU A 1 912  ? 200.997 155.031 219.746 1.00 34.27 ? 862 GLU A C   1 
ATOM 2974 O O   . GLU A 1 912  ? 201.383 155.799 218.863 1.00 31.32 ? 862 GLU A O   1 
ATOM 2975 C CB  . GLU A 1 912  ? 203.040 153.669 220.349 1.00 33.51 ? 862 GLU A CB  1 
ATOM 2976 C CG  . GLU A 1 912  ? 203.601 152.760 221.428 1.00 32.91 ? 862 GLU A CG  1 
ATOM 2977 C CD  . GLU A 1 912  ? 204.600 151.721 220.944 1.00 34.05 ? 862 GLU A CD  1 
ATOM 2978 O OE1 . GLU A 1 912  ? 204.876 151.685 219.730 1.00 33.87 ? 862 GLU A OE1 1 
ATOM 2979 O OE2 . GLU A 1 912  ? 205.101 150.948 221.784 1.00 32.97 ? 862 GLU A OE2 1 
ATOM 2980 N N   . GLU A 1 913  ? 199.818 154.468 219.756 1.00 31.90 ? 863 GLU A N   1 
ATOM 2981 C CA  . GLU A 1 913  ? 198.735 154.864 218.817 1.00 31.00 ? 863 GLU A CA  1 
ATOM 2982 C C   . GLU A 1 913  ? 197.882 155.972 219.443 1.00 31.80 ? 863 GLU A C   1 
ATOM 2983 O O   . GLU A 1 913  ? 197.519 156.913 218.712 1.00 29.50 ? 863 GLU A O   1 
ATOM 2984 C CB  . GLU A 1 913  ? 197.867 153.658 218.455 1.00 29.83 ? 863 GLU A CB  1 
ATOM 2985 C CG  . GLU A 1 913  ? 196.925 153.917 217.293 1.00 29.43 ? 863 GLU A CG  1 
ATOM 2986 C CD  . GLU A 1 913  ? 197.602 154.427 216.033 1.00 30.36 ? 863 GLU A CD  1 
ATOM 2987 O OE1 . GLU A 1 913  ? 198.473 153.710 215.501 1.00 34.51 ? 863 GLU A OE1 1 
ATOM 2988 O OE2 . GLU A 1 913  ? 197.255 155.537 215.586 1.00 29.41 ? 863 GLU A OE2 1 
ATOM 2989 N N   . LYS A 1 914  ? 197.520 155.826 220.722 1.00 27.08 ? 864 LYS A N   1 
ATOM 2990 C CA  . LYS A 1 914  ? 196.681 156.847 221.407 1.00 29.67 ? 864 LYS A CA  1 
ATOM 2991 C C   . LYS A 1 914  ? 197.455 158.169 221.401 1.00 28.94 ? 864 LYS A C   1 
ATOM 2992 O O   . LYS A 1 914  ? 196.815 159.225 221.232 1.00 24.19 ? 864 LYS A O   1 
ATOM 2993 C CB  . LYS A 1 914  ? 196.295 156.368 222.811 1.00 28.34 ? 864 LYS A CB  1 
ATOM 2994 C CG  . LYS A 1 914  ? 197.199 156.819 223.949 1.00 28.91 ? 864 LYS A CG  1 
ATOM 2995 C CD  . LYS A 1 914  ? 197.023 155.992 225.203 1.00 29.83 ? 864 LYS A CD  1 
ATOM 2996 C CE  . LYS A 1 914  ? 197.953 156.409 226.323 1.00 29.29 ? 864 LYS A CE  1 
ATOM 2997 N NZ  . LYS A 1 914  ? 197.893 155.465 227.464 1.00 29.67 ? 864 LYS A NZ  1 
ATOM 2998 N N   . GLU A 1 915  ? 198.778 158.106 221.574 1.00 27.28 ? 865 GLU A N   1 
ATOM 2999 C CA  . GLU A 1 915  ? 199.628 159.323 221.484 1.00 27.82 ? 865 GLU A CA  1 
ATOM 3000 C C   . GLU A 1 915  ? 199.573 159.845 220.045 1.00 29.83 ? 865 GLU A C   1 
ATOM 3001 O O   . GLU A 1 915  ? 199.323 161.053 219.866 1.00 25.19 ? 865 GLU A O   1 
ATOM 3002 C CB  . GLU A 1 915  ? 201.059 159.002 221.919 1.00 25.65 ? 865 GLU A CB  1 
ATOM 3003 C CG  . GLU A 1 915  ? 201.981 160.208 221.927 1.00 26.16 ? 865 GLU A CG  1 
ATOM 3004 C CD  . GLU A 1 915  ? 202.518 160.596 220.560 1.00 30.36 ? 865 GLU A CD  1 
ATOM 3005 O OE1 . GLU A 1 915  ? 202.587 159.713 219.682 1.00 29.44 ? 865 GLU A OE1 1 
ATOM 3006 O OE2 . GLU A 1 915  ? 202.871 161.778 220.379 1.00 33.97 ? 865 GLU A OE2 1 
ATOM 3007 N N   . ASP A 1 916  ? 199.788 158.963 219.063 1.00 28.35 ? 866 ASP A N   1 
ATOM 3008 C CA  . ASP A 1 916  ? 199.683 159.384 217.642 1.00 25.96 ? 866 ASP A CA  1 
ATOM 3009 C C   . ASP A 1 916  ? 198.354 160.122 217.461 1.00 23.97 ? 866 ASP A C   1 
ATOM 3010 O O   . ASP A 1 916  ? 198.355 161.191 216.820 1.00 22.03 ? 866 ASP A O   1 
ATOM 3011 C CB  . ASP A 1 916  ? 199.803 158.190 216.693 1.00 26.36 ? 866 ASP A CB  1 
ATOM 3012 C CG  . ASP A 1 916  ? 199.496 158.543 215.249 1.00 28.82 ? 866 ASP A CG  1 
ATOM 3013 O OD1 . ASP A 1 916  ? 200.389 159.101 214.581 1.00 26.73 ? 866 ASP A OD1 1 
ATOM 3014 O OD2 . ASP A 1 916  ? 198.365 158.264 214.805 1.00 29.61 ? 866 ASP A OD2 1 
ATOM 3015 N N   . LEU A 1 917  ? 197.269 159.574 218.020 1.00 22.00 ? 867 LEU A N   1 
ATOM 3016 C CA  . LEU A 1 917  ? 195.961 160.205 217.885 1.00 21.42 ? 867 LEU A CA  1 
ATOM 3017 C C   . LEU A 1 917  ? 195.917 161.559 218.581 1.00 25.18 ? 867 LEU A C   1 
ATOM 3018 O O   . LEU A 1 917  ? 195.314 162.505 218.064 1.00 20.99 ? 867 LEU A O   1 
ATOM 3019 C CB  . LEU A 1 917  ? 194.873 159.286 218.436 1.00 18.34 ? 867 LEU A CB  1 
ATOM 3020 C CG  . LEU A 1 917  ? 194.035 158.550 217.391 1.00 19.55 ? 867 LEU A CG  1 
ATOM 3021 C CD1 . LEU A 1 917  ? 194.930 157.930 216.331 1.00 25.15 ? 867 LEU A CD1 1 
ATOM 3022 C CD2 . LEU A 1 917  ? 193.160 157.493 218.045 1.00 22.93 ? 867 LEU A CD2 1 
ATOM 3023 N N   . GLU A 1 918  ? 196.539 161.680 219.756 1.00 23.22 ? 868 GLU A N   1 
ATOM 3024 C CA  . GLU A 1 918  ? 196.498 162.973 220.430 1.00 24.49 ? 868 GLU A CA  1 
ATOM 3025 C C   . GLU A 1 918  ? 197.313 164.015 219.678 1.00 24.63 ? 868 GLU A C   1 
ATOM 3026 O O   . GLU A 1 918  ? 196.948 165.195 219.677 1.00 27.08 ? 868 GLU A O   1 
ATOM 3027 C CB  . GLU A 1 918  ? 196.983 162.873 221.878 1.00 25.83 ? 868 GLU A CB  1 
ATOM 3028 C CG  . GLU A 1 918  ? 196.907 164.158 222.678 1.00 24.91 ? 868 GLU A CG  1 
ATOM 3029 C CD  . GLU A 1 918  ? 197.357 163.982 224.120 1.00 27.08 ? 868 GLU A CD  1 
ATOM 3030 O OE1 . GLU A 1 918  ? 197.766 162.860 224.489 1.00 28.25 ? 868 GLU A OE1 1 
ATOM 3031 O OE2 . GLU A 1 918  ? 197.305 164.972 224.880 1.00 26.57 ? 868 GLU A OE2 1 
ATOM 3032 N N   . ARG A 1 919  ? 198.415 163.613 219.041 1.00 21.89 ? 869 ARG A N   1 
ATOM 3033 C CA  . ARG A 1 919  ? 199.174 164.567 218.244 1.00 25.27 ? 869 ARG A CA  1 
ATOM 3034 C C   . ARG A 1 919  ? 198.489 164.888 216.922 1.00 21.48 ? 869 ARG A C   1 
ATOM 3035 O O   . ARG A 1 919  ? 198.644 166.004 216.412 1.00 20.12 ? 869 ARG A O   1 
ATOM 3036 C CB  . ARG A 1 919  ? 200.595 164.045 218.001 1.00 27.25 ? 869 ARG A CB  1 
ATOM 3037 C CG  . ARG A 1 919  ? 201.487 164.996 217.214 1.00 26.45 ? 869 ARG A CG  1 
ATOM 3038 C CD  . ARG A 1 919  ? 202.890 164.449 216.933 1.00 22.42 ? 869 ARG A CD  1 
ATOM 3039 N NE  . ARG A 1 919  ? 202.906 163.278 216.063 1.00 24.00 ? 869 ARG A NE  1 
ATOM 3040 C CZ  . ARG A 1 919  ? 203.920 162.432 215.944 1.00 23.07 ? 869 ARG A CZ  1 
ATOM 3041 N NH1 . ARG A 1 919  ? 205.062 162.624 216.581 1.00 15.40 ? 869 ARG A NH1 1 
ATOM 3042 N NH2 . ARG A 1 919  ? 203.790 161.373 215.149 1.00 27.30 ? 869 ARG A NH2 1 
ATOM 3043 N N   . PHE A 1 920  ? 197.729 163.943 216.365 1.00 19.72 ? 870 PHE A N   1 
ATOM 3044 C CA  . PHE A 1 920  ? 196.878 164.232 215.218 1.00 22.53 ? 870 PHE A CA  1 
ATOM 3045 C C   . PHE A 1 920  ? 195.789 165.234 215.582 1.00 24.75 ? 870 PHE A C   1 
ATOM 3046 O O   . PHE A 1 920  ? 195.481 166.139 214.799 1.00 29.10 ? 870 PHE A O   1 
ATOM 3047 C CB  . PHE A 1 920  ? 196.264 162.933 214.692 1.00 21.39 ? 870 PHE A CB  1 
ATOM 3048 C CG  . PHE A 1 920  ? 195.275 163.130 213.581 1.00 17.22 ? 870 PHE A CG  1 
ATOM 3049 C CD1 . PHE A 1 920  ? 195.698 163.212 212.268 1.00 12.88 ? 870 PHE A CD1 1 
ATOM 3050 C CD2 . PHE A 1 920  ? 193.919 163.222 213.848 1.00 19.86 ? 870 PHE A CD2 1 
ATOM 3051 C CE1 . PHE A 1 920  ? 194.790 163.388 211.247 1.00 16.29 ? 870 PHE A CE1 1 
ATOM 3052 C CE2 . PHE A 1 920  ? 193.008 163.400 212.830 1.00 15.61 ? 870 PHE A CE2 1 
ATOM 3053 C CZ  . PHE A 1 920  ? 193.443 163.483 211.530 1.00 14.88 ? 870 PHE A CZ  1 
ATOM 3054 N N   . VAL A 1 921  ? 195.196 165.077 216.761 1.00 20.47 ? 871 VAL A N   1 
ATOM 3055 C CA  . VAL A 1 921  ? 194.214 166.031 217.255 1.00 24.39 ? 871 VAL A CA  1 
ATOM 3056 C C   . VAL A 1 921  ? 194.934 167.272 217.778 1.00 24.25 ? 871 VAL A C   1 
ATOM 3057 O O   . VAL A 1 921  ? 196.107 167.227 218.156 1.00 24.90 ? 871 VAL A O   1 
ATOM 3058 C CB  . VAL A 1 921  ? 193.331 165.373 218.336 1.00 25.37 ? 871 VAL A CB  1 
ATOM 3059 C CG1 . VAL A 1 921  ? 192.403 166.375 219.014 1.00 22.28 ? 871 VAL A CG1 1 
ATOM 3060 C CG2 . VAL A 1 921  ? 192.526 164.231 217.729 1.00 23.57 ? 871 VAL A CG2 1 
ATOM 3061 N N   . SER A 1 922  ? 194.230 168.414 217.765 1.00 23.44 ? 872 SER A N   1 
ATOM 3062 C CA  . SER A 1 922  ? 194.794 169.707 218.254 1.00 26.77 ? 872 SER A CA  1 
ATOM 3063 C C   . SER A 1 922  ? 195.650 170.373 217.169 1.00 27.40 ? 872 SER A C   1 
ATOM 3064 O O   . SER A 1 922  ? 195.912 171.579 217.306 1.00 26.19 ? 872 SER A O   1 
ATOM 3065 C CB  . SER A 1 922  ? 195.537 169.572 219.569 1.00 26.16 ? 872 SER A CB  1 
ATOM 3066 O OG  . SER A 1 922  ? 194.707 168.983 220.559 1.00 30.45 ? 872 SER A OG  1 
ATOM 3067 N N   . CYS A 1 923  ? 196.070 169.628 216.140 1.00 26.98 ? 873 CYS A N   1 
ATOM 3068 C CA  . CYS A 1 923  ? 196.799 170.235 215.035 1.00 30.41 ? 873 CYS A CA  1 
ATOM 3069 C C   . CYS A 1 923  ? 195.835 170.824 214.014 1.00 31.00 ? 873 CYS A C   1 
ATOM 3070 O O   . CYS A 1 923  ? 196.166 171.786 213.315 1.00 31.83 ? 873 CYS A O   1 
ATOM 3071 C CB  . CYS A 1 923  ? 197.717 169.204 214.371 1.00 33.48 ? 873 CYS A CB  1 
ATOM 3072 S SG  . CYS A 1 923  ? 198.745 169.868 213.040 1.00 42.82 ? 873 CYS A SG  1 
ATOM 3073 N N   . LEU A 1 924  ? 194.632 170.254 213.933 1.00 24.26 ? 874 LEU A N   1 
ATOM 3074 C CA  . LEU A 1 924  ? 193.598 170.771 213.049 1.00 28.96 ? 874 LEU A CA  1 
ATOM 3075 C C   . LEU A 1 924  ? 193.046 172.106 213.529 1.00 30.89 ? 874 LEU A C   1 
ATOM 3076 O O   . LEU A 1 924  ? 192.399 172.815 212.750 1.00 26.92 ? 874 LEU A O   1 
ATOM 3077 C CB  . LEU A 1 924  ? 192.473 169.741 212.934 1.00 25.14 ? 874 LEU A CB  1 
ATOM 3078 C CG  . LEU A 1 924  ? 191.438 169.905 211.825 1.00 28.71 ? 874 LEU A CG  1 
ATOM 3079 C CD1 . LEU A 1 924  ? 192.101 170.359 210.537 1.00 25.43 ? 874 LEU A CD1 1 
ATOM 3080 C CD2 . LEU A 1 924  ? 190.711 168.590 211.621 1.00 30.63 ? 874 LEU A CD2 1 
ATOM 3081 N N   . LEU A 1 925  ? 193.330 172.477 214.777 1.00 31.32 ? 875 LEU A N   1 
ATOM 3082 C CA  . LEU A 1 925  ? 192.732 173.719 215.338 1.00 25.89 ? 875 LEU A CA  1 
ATOM 3083 C C   . LEU A 1 925  ? 193.396 174.961 214.738 1.00 25.58 ? 875 LEU A C   1 
ATOM 3084 O O   . LEU A 1 925  ? 192.705 175.991 214.620 1.00 25.23 ? 875 LEU A O   1 
ATOM 3085 C CB  . LEU A 1 925  ? 192.922 173.696 216.854 1.00 20.09 ? 875 LEU A CB  1 
ATOM 3086 C CG  . LEU A 1 925  ? 192.166 172.590 217.584 1.00 24.03 ? 875 LEU A CG  1 
ATOM 3087 C CD1 . LEU A 1 925  ? 191.800 173.056 218.975 1.00 23.62 ? 875 LEU A CD1 1 
ATOM 3088 C CD2 . LEU A 1 925  ? 190.916 172.188 216.818 1.00 25.10 ? 875 LEU A CD2 1 
ATOM 3089 N N   . GLU A 1 926  ? 194.677 174.871 214.379 1.00 22.86 ? 876 GLU A N   1 
ATOM 3090 C CA  . GLU A 1 926  ? 195.403 176.041 213.893 1.00 24.74 ? 876 GLU A CA  1 
ATOM 3091 C C   . GLU A 1 926  ? 195.272 176.206 212.380 1.00 26.39 ? 876 GLU A C   1 
ATOM 3092 O O   . GLU A 1 926  ? 194.758 177.223 211.903 1.00 28.17 ? 876 GLU A O   1 
ATOM 3093 C CB  . GLU A 1 926  ? 196.879 175.944 214.298 1.00 23.40 ? 876 GLU A CB  1 
ATOM 3094 C CG  . GLU A 1 926  ? 197.137 176.205 215.775 1.00 26.11 ? 876 GLU A CG  1 
ATOM 3095 C CD  . GLU A 1 926  ? 196.595 175.105 216.668 1.00 27.25 ? 876 GLU A CD  1 
ATOM 3096 O OE1 . GLU A 1 926  ? 196.351 173.994 216.155 1.00 25.77 ? 876 GLU A OE1 1 
ATOM 3097 O OE2 . GLU A 1 926  ? 196.407 175.352 217.877 1.00 27.47 ? 876 GLU A OE2 1 
ATOM 3098 N N   . GLN A 1 927  ? 195.733 175.196 211.637 1.00 27.97 ? 877 GLN A N   1 
ATOM 3099 C CA  . GLN A 1 927  ? 195.616 175.229 210.154 1.00 28.00 ? 877 GLN A CA  1 
ATOM 3100 C C   . GLN A 1 927  ? 194.426 174.355 209.741 1.00 23.84 ? 877 GLN A C   1 
ATOM 3101 O O   . GLN A 1 927  ? 194.157 173.353 210.435 1.00 22.90 ? 877 GLN A O   1 
ATOM 3102 C CB  . GLN A 1 927  ? 196.930 174.777 209.510 1.00 24.11 ? 877 GLN A CB  1 
ATOM 3103 C CG  . GLN A 1 927  ? 197.303 173.332 209.805 1.00 24.53 ? 877 GLN A CG  1 
ATOM 3104 C CD  . GLN A 1 927  ? 198.602 172.924 209.154 1.00 26.51 ? 877 GLN A CD  1 
ATOM 3105 O OE1 . GLN A 1 927  ? 199.424 173.760 208.786 1.00 30.80 ? 877 GLN A OE1 1 
ATOM 3106 N NE2 . GLN A 1 927  ? 198.798 171.624 209.010 1.00 22.66 ? 877 GLN A NE2 1 
ATOM 3107 N N   . PRO A 1 928  ? 193.665 174.686 208.668 1.00 21.29 ? 878 PRO A N   1 
ATOM 3108 C CA  . PRO A 1 928  ? 192.487 173.909 208.290 1.00 25.20 ? 878 PRO A CA  1 
ATOM 3109 C C   . PRO A 1 928  ? 192.847 172.844 207.245 1.00 23.16 ? 878 PRO A C   1 
ATOM 3110 O O   . PRO A 1 928  ? 192.157 172.752 206.252 1.00 24.09 ? 878 PRO A O   1 
ATOM 3111 C CB  . PRO A 1 928  ? 191.580 174.982 207.676 1.00 26.03 ? 878 PRO A CB  1 
ATOM 3112 C CG  . PRO A 1 928  ? 192.544 175.919 206.978 1.00 26.93 ? 878 PRO A CG  1 
ATOM 3113 C CD  . PRO A 1 928  ? 193.846 175.822 207.747 1.00 28.13 ? 878 PRO A CD  1 
ATOM 3114 N N   . GLU A 1 929  ? 193.916 172.082 207.491 1.00 17.52 ? 879 GLU A N   1 
ATOM 3115 C CA  . GLU A 1 929  ? 194.332 171.003 206.556 1.00 16.93 ? 879 GLU A CA  1 
ATOM 3116 C C   . GLU A 1 929  ? 195.424 170.163 207.223 1.00 14.70 ? 879 GLU A C   1 
ATOM 3117 O O   . GLU A 1 929  ? 196.532 170.697 207.428 1.00 21.93 ? 879 GLU A O   1 
ATOM 3118 C CB  . GLU A 1 929  ? 194.832 171.606 205.242 1.00 20.32 ? 879 GLU A CB  1 
ATOM 3119 C CG  . GLU A 1 929  ? 195.446 170.588 204.300 1.00 18.92 ? 879 GLU A CG  1 
ATOM 3120 C CD  . GLU A 1 929  ? 196.765 171.026 203.687 1.00 21.42 ? 879 GLU A CD  1 
ATOM 3121 O OE1 . GLU A 1 929  ? 197.186 172.170 203.953 1.00 26.19 ? 879 GLU A OE1 1 
ATOM 3122 O OE2 . GLU A 1 929  ? 197.366 170.224 202.946 1.00 15.30 ? 879 GLU A OE2 1 
ATOM 3123 N N   . VAL A 1 930  ? 195.122 168.903 207.552 1.00 12.78 ? 880 VAL A N   1 
ATOM 3124 C CA  . VAL A 1 930  ? 196.148 168.043 208.132 1.00 14.98 ? 880 VAL A CA  1 
ATOM 3125 C C   . VAL A 1 930  ? 196.212 166.742 207.344 1.00 10.49 ? 880 VAL A C   1 
ATOM 3126 O O   . VAL A 1 930  ? 195.203 166.278 206.802 1.00 5.46  ? 880 VAL A O   1 
ATOM 3127 C CB  . VAL A 1 930  ? 195.895 167.782 209.630 1.00 15.93 ? 880 VAL A CB  1 
ATOM 3128 C CG1 . VAL A 1 930  ? 194.941 166.617 209.829 1.00 18.55 ? 880 VAL A CG1 1 
ATOM 3129 C CG2 . VAL A 1 930  ? 197.210 167.526 210.346 1.00 13.16 ? 880 VAL A CG2 1 
ATOM 3130 N N   . LEU A 1 931  ? 197.404 166.163 207.246 1.00 15.75 ? 881 LEU A N   1 
ATOM 3131 C CA  . LEU A 1 931  ? 197.555 164.882 206.575 1.00 18.49 ? 881 LEU A CA  1 
ATOM 3132 C C   . LEU A 1 931  ? 197.189 163.743 207.518 1.00 10.16 ? 881 LEU A C   1 
ATOM 3133 O O   . LEU A 1 931  ? 197.281 163.866 208.742 1.00 7.88  ? 881 LEU A O   1 
ATOM 3134 C CB  . LEU A 1 931  ? 198.988 164.705 206.072 1.00 18.26 ? 881 LEU A CB  1 
ATOM 3135 C CG  . LEU A 1 931  ? 199.441 165.664 204.970 1.00 15.19 ? 881 LEU A CG  1 
ATOM 3136 C CD1 . LEU A 1 931  ? 200.924 165.494 204.691 1.00 15.20 ? 881 LEU A CD1 1 
ATOM 3137 C CD2 . LEU A 1 931  ? 198.629 165.446 203.704 1.00 11.17 ? 881 LEU A CD2 1 
ATOM 3138 N N   . VAL A 1 932  ? 196.762 162.626 206.938 1.00 6.66  ? 882 VAL A N   1 
ATOM 3139 C CA  . VAL A 1 932  ? 196.446 161.422 207.694 1.00 6.01  ? 882 VAL A CA  1 
ATOM 3140 C C   . VAL A 1 932  ? 197.496 160.369 207.375 1.00 6.18  ? 882 VAL A C   1 
ATOM 3141 O O   . VAL A 1 932  ? 197.799 160.121 206.202 1.00 11.08 ? 882 VAL A O   1 
ATOM 3142 C CB  . VAL A 1 932  ? 195.033 160.909 207.378 1.00 5.74  ? 882 VAL A CB  1 
ATOM 3143 C CG1 . VAL A 1 932  ? 194.647 159.823 208.348 1.00 8.18  ? 882 VAL A CG1 1 
ATOM 3144 C CG2 . VAL A 1 932  ? 194.045 162.044 207.460 1.00 6.67  ? 882 VAL A CG2 1 
ATOM 3145 N N   . THR A 1 933  ? 198.053 159.759 208.417 1.00 7.97  ? 883 THR A N   1 
ATOM 3146 C CA  . THR A 1 933  ? 199.102 158.766 208.232 1.00 6.68  ? 883 THR A CA  1 
ATOM 3147 C C   . THR A 1 933  ? 198.540 157.496 207.606 1.00 6.49  ? 883 THR A C   1 
ATOM 3148 O O   . THR A 1 933  ? 197.562 156.924 208.098 1.00 5.19  ? 883 THR A O   1 
ATOM 3149 C CB  . THR A 1 933  ? 199.761 158.444 209.574 1.00 12.20 ? 883 THR A CB  1 
ATOM 3150 O OG1 . THR A 1 933  ? 200.609 159.531 209.964 1.00 20.74 ? 883 THR A OG1 1 
ATOM 3151 C CG2 . THR A 1 933  ? 200.588 157.172 209.471 1.00 11.32 ? 883 THR A CG2 1 
ATOM 3152 N N   . GLY A 1 934  ? 199.169 157.055 206.518 1.00 10.87 ? 884 GLY A N   1 
ATOM 3153 C CA  . GLY A 1 934  ? 198.770 155.824 205.857 1.00 12.45 ? 884 GLY A CA  1 
ATOM 3154 C C   . GLY A 1 934  ? 197.447 155.903 205.129 1.00 12.31 ? 884 GLY A C   1 
ATOM 3155 O O   . GLY A 1 934  ? 196.831 154.864 204.868 1.00 10.39 ? 884 GLY A O   1 
ATOM 3156 N N   . ALA A 1 935  ? 196.998 157.111 204.786 1.00 14.03 ? 885 ALA A N   1 
ATOM 3157 C CA  . ALA A 1 935  ? 195.708 157.354 204.122 1.00 11.53 ? 885 ALA A CA  1 
ATOM 3158 C C   . ALA A 1 935  ? 194.612 156.675 204.946 1.00 11.33 ? 885 ALA A C   1 
ATOM 3159 O O   . ALA A 1 935  ? 194.641 156.758 206.181 1.00 14.92 ? 885 ALA A O   1 
ATOM 3160 C CB  . ALA A 1 935  ? 195.803 156.916 202.669 1.00 9.69  ? 885 ALA A CB  1 
ATOM 3161 N N   . GLY A 1 936  ? 193.645 156.001 204.322 1.00 10.79 ? 886 GLY A N   1 
ATOM 3162 C CA  . GLY A 1 936  ? 192.591 155.361 205.091 1.00 10.10 ? 886 GLY A CA  1 
ATOM 3163 C C   . GLY A 1 936  ? 193.010 154.023 205.670 1.00 17.83 ? 886 GLY A C   1 
ATOM 3164 O O   . GLY A 1 936  ? 192.328 153.475 206.541 1.00 24.63 ? 886 GLY A O   1 
ATOM 3165 N N   . ARG A 1 937  ? 194.126 153.473 205.188 1.00 18.11 ? 887 ARG A N   1 
ATOM 3166 C CA  . ARG A 1 937  ? 194.604 152.191 205.697 1.00 16.74 ? 887 ARG A CA  1 
ATOM 3167 C C   . ARG A 1 937  ? 195.092 152.310 207.136 1.00 18.22 ? 887 ARG A C   1 
ATOM 3168 O O   . ARG A 1 937  ? 194.875 151.405 207.951 1.00 16.56 ? 887 ARG A O   1 
ATOM 3169 C CB  . ARG A 1 937  ? 195.716 151.654 204.795 1.00 16.29 ? 887 ARG A CB  1 
ATOM 3170 C CG  . ARG A 1 937  ? 195.227 150.661 203.753 1.00 15.77 ? 887 ARG A CG  1 
ATOM 3171 C CD  . ARG A 1 937  ? 196.328 150.090 202.844 1.00 17.00 ? 887 ARG A CD  1 
ATOM 3172 N NE  . ARG A 1 937  ? 196.887 151.046 201.892 1.00 15.79 ? 887 ARG A NE  1 
ATOM 3173 C CZ  . ARG A 1 937  ? 197.845 151.924 202.161 1.00 17.82 ? 887 ARG A CZ  1 
ATOM 3174 N NH1 . ARG A 1 937  ? 198.453 151.950 203.335 1.00 12.68 ? 887 ARG A NH1 1 
ATOM 3175 N NH2 . ARG A 1 937  ? 198.223 152.781 201.216 1.00 22.06 ? 887 ARG A NH2 1 
ATOM 3176 N N   . GLY A 1 938  ? 195.747 153.419 207.468 1.00 18.49 ? 888 GLY A N   1 
ATOM 3177 C CA  . GLY A 1 938  ? 196.342 153.547 208.787 1.00 22.30 ? 888 GLY A CA  1 
ATOM 3178 C C   . GLY A 1 938  ? 195.287 153.646 209.876 1.00 18.76 ? 888 GLY A C   1 
ATOM 3179 O O   . GLY A 1 938  ? 194.127 153.979 209.622 1.00 17.09 ? 888 GLY A O   1 
ATOM 3180 N N   . HIS A 1 939  ? 195.708 153.348 211.109 1.00 17.86 ? 889 HIS A N   1 
ATOM 3181 C CA  . HIS A 1 939  ? 194.797 153.395 212.248 1.00 23.56 ? 889 HIS A CA  1 
ATOM 3182 C C   . HIS A 1 939  ? 194.277 154.806 212.487 1.00 27.67 ? 889 HIS A C   1 
ATOM 3183 O O   . HIS A 1 939  ? 193.132 154.988 212.920 1.00 28.35 ? 889 HIS A O   1 
ATOM 3184 C CB  . HIS A 1 939  ? 195.500 152.871 213.499 1.00 24.20 ? 889 HIS A CB  1 
ATOM 3185 C CG  . HIS A 1 939  ? 195.949 151.448 213.389 1.00 26.78 ? 889 HIS A CG  1 
ATOM 3186 N ND1 . HIS A 1 939  ? 195.068 150.388 213.375 1.00 27.36 ? 889 HIS A ND1 1 
ATOM 3187 C CD2 . HIS A 1 939  ? 197.186 150.910 213.280 1.00 26.50 ? 889 HIS A CD2 1 
ATOM 3188 C CE1 . HIS A 1 939  ? 195.744 149.258 213.268 1.00 26.39 ? 889 HIS A CE1 1 
ATOM 3189 N NE2 . HIS A 1 939  ? 197.031 149.547 213.207 1.00 27.53 ? 889 HIS A NE2 1 
ATOM 3190 N N   . ALA A 1 940  ? 195.110 155.817 212.234 1.00 22.86 ? 890 ALA A N   1 
ATOM 3191 C CA  . ALA A 1 940  ? 194.659 157.197 212.378 1.00 16.76 ? 890 ALA A CA  1 
ATOM 3192 C C   . ALA A 1 940  ? 193.522 157.500 211.412 1.00 18.97 ? 890 ALA A C   1 
ATOM 3193 O O   . ALA A 1 940  ? 192.574 158.214 211.758 1.00 15.58 ? 890 ALA A O   1 
ATOM 3194 C CB  . ALA A 1 940  ? 195.826 158.160 212.158 1.00 13.33 ? 890 ALA A CB  1 
ATOM 3195 N N   . GLY A 1 941  ? 193.602 156.966 210.196 1.00 19.29 ? 891 GLY A N   1 
ATOM 3196 C CA  . GLY A 1 941  ? 192.542 157.129 209.223 1.00 16.88 ? 891 GLY A CA  1 
ATOM 3197 C C   . GLY A 1 941  ? 191.445 156.096 209.363 1.00 16.85 ? 891 GLY A C   1 
ATOM 3198 O O   . GLY A 1 941  ? 190.345 156.274 208.831 1.00 16.60 ? 891 GLY A O   1 
ATOM 3199 N N   . ARG A 1 942  ? 191.734 155.008 210.080 1.00 20.22 ? 892 ARG A N   1 
ATOM 3200 C CA  . ARG A 1 942  ? 190.731 153.967 210.275 1.00 19.80 ? 892 ARG A CA  1 
ATOM 3201 C C   . ARG A 1 942  ? 189.528 154.500 211.039 1.00 18.30 ? 892 ARG A C   1 
ATOM 3202 O O   . ARG A 1 942  ? 188.382 154.166 210.718 1.00 13.15 ? 892 ARG A O   1 
ATOM 3203 C CB  . ARG A 1 942  ? 191.343 152.774 211.004 1.00 18.58 ? 892 ARG A CB  1 
ATOM 3204 C CG  . ARG A 1 942  ? 190.480 151.527 210.972 1.00 19.44 ? 892 ARG A CG  1 
ATOM 3205 C CD  . ARG A 1 942  ? 190.912 150.585 209.862 1.00 19.48 ? 892 ARG A CD  1 
ATOM 3206 N NE  . ARG A 1 942  ? 192.339 150.294 209.913 1.00 21.65 ? 892 ARG A NE  1 
ATOM 3207 C CZ  . ARG A 1 942  ? 192.950 149.407 209.140 1.00 21.80 ? 892 ARG A CZ  1 
ATOM 3208 N NH1 . ARG A 1 942  ? 192.285 148.697 208.243 1.00 21.09 ? 892 ARG A NH1 1 
ATOM 3209 N NH2 . ARG A 1 942  ? 194.261 149.228 209.269 1.00 24.08 ? 892 ARG A NH2 1 
ATOM 3210 N N   . ILE A 1 943  ? 189.768 155.330 212.056 1.00 23.54 ? 893 ILE A N   1 
ATOM 3211 C CA  . ILE A 1 943  ? 188.664 155.919 212.807 1.00 22.14 ? 893 ILE A CA  1 
ATOM 3212 C C   . ILE A 1 943  ? 187.803 156.783 211.894 1.00 23.65 ? 893 ILE A C   1 
ATOM 3213 O O   . ILE A 1 943  ? 186.570 156.694 211.915 1.00 24.78 ? 893 ILE A O   1 
ATOM 3214 C CB  . ILE A 1 943  ? 189.198 156.718 214.009 1.00 16.83 ? 893 ILE A CB  1 
ATOM 3215 C CG1 . ILE A 1 943  ? 189.962 155.797 214.959 1.00 17.91 ? 893 ILE A CG1 1 
ATOM 3216 C CG2 . ILE A 1 943  ? 188.057 157.399 214.743 1.00 19.38 ? 893 ILE A CG2 1 
ATOM 3217 C CD1 . ILE A 1 943  ? 189.067 154.933 215.819 1.00 21.69 ? 893 ILE A CD1 1 
ATOM 3218 N N   . ILE A 1 944  ? 188.457 157.625 211.090 1.00 23.57 ? 894 ILE A N   1 
ATOM 3219 C CA  . ILE A 1 944  ? 187.704 158.468 210.116 1.00 19.51 ? 894 ILE A CA  1 
ATOM 3220 C C   . ILE A 1 944  ? 186.845 157.537 209.256 1.00 18.65 ? 894 ILE A C   1 
ATOM 3221 O O   . ILE A 1 944  ? 185.657 157.853 209.048 1.00 18.67 ? 894 ILE A O   1 
ATOM 3222 C CB  . ILE A 1 944  ? 188.667 159.315 209.263 1.00 11.37 ? 894 ILE A CB  1 
ATOM 3223 C CG1 . ILE A 1 944  ? 189.869 159.797 210.080 1.00 13.94 ? 894 ILE A CG1 1 
ATOM 3224 C CG2 . ILE A 1 944  ? 187.932 160.473 208.605 1.00 11.64 ? 894 ILE A CG2 1 
ATOM 3225 C CD1 . ILE A 1 944  ? 190.873 160.594 209.282 1.00 8.08  ? 894 ILE A CD1 1 
ATOM 3226 N N   . HIS A 1 945  ? 187.426 156.426 208.791 1.00 16.07 ? 895 HIS A N   1 
ATOM 3227 C CA  . HIS A 1 945  ? 186.671 155.472 207.990 1.00 22.05 ? 895 HIS A CA  1 
ATOM 3228 C C   . HIS A 1 945  ? 185.455 154.961 208.751 1.00 24.38 ? 895 HIS A C   1 
ATOM 3229 O O   . HIS A 1 945  ? 184.378 154.786 208.169 1.00 21.77 ? 895 HIS A O   1 
ATOM 3230 C CB  . HIS A 1 945  ? 187.578 154.310 207.584 1.00 24.52 ? 895 HIS A CB  1 
ATOM 3231 C CG  . HIS A 1 945  ? 187.041 153.477 206.462 1.00 22.82 ? 895 HIS A CG  1 
ATOM 3232 N ND1 . HIS A 1 945  ? 185.695 153.372 206.185 1.00 19.27 ? 895 HIS A ND1 1 
ATOM 3233 C CD2 . HIS A 1 945  ? 187.672 152.690 205.559 1.00 23.58 ? 895 HIS A CD2 1 
ATOM 3234 C CE1 . HIS A 1 945  ? 185.521 152.566 205.153 1.00 24.46 ? 895 HIS A CE1 1 
ATOM 3235 N NE2 . HIS A 1 945  ? 186.705 152.138 204.755 1.00 24.84 ? 895 HIS A NE2 1 
ATOM 3236 N N   . LYS A 1 946  ? 185.608 154.714 210.054 1.00 24.68 ? 896 LYS A N   1 
ATOM 3237 C CA  . LYS A 1 946  ? 184.519 154.118 210.820 1.00 22.98 ? 896 LYS A CA  1 
ATOM 3238 C C   . LYS A 1 946  ? 183.391 155.115 211.061 1.00 20.97 ? 896 LYS A C   1 
ATOM 3239 O O   . LYS A 1 946  ? 182.213 154.739 211.036 1.00 20.03 ? 896 LYS A O   1 
ATOM 3240 C CB  . LYS A 1 946  ? 185.047 153.564 212.143 1.00 17.87 ? 896 LYS A CB  1 
ATOM 3241 C CG  . LYS A 1 946  ? 186.072 152.445 211.988 1.00 18.80 ? 896 LYS A CG  1 
ATOM 3242 C CD  . LYS A 1 946  ? 185.752 151.532 210.808 1.00 21.11 ? 896 LYS A CD  1 
ATOM 3243 C CE  . LYS A 1 946  ? 184.763 150.445 211.188 1.00 21.48 ? 896 LYS A CE  1 
ATOM 3244 N NZ  . LYS A 1 946  ? 185.226 149.664 212.366 1.00 24.03 ? 896 LYS A NZ  1 
ATOM 3245 N N   . LEU A 1 947  ? 183.724 156.387 211.303 1.00 22.49 ? 897 LEU A N   1 
ATOM 3246 C CA  . LEU A 1 947  ? 182.677 157.391 211.469 1.00 23.20 ? 897 LEU A CA  1 
ATOM 3247 C C   . LEU A 1 947  ? 181.857 157.543 210.196 1.00 20.09 ? 897 LEU A C   1 
ATOM 3248 O O   . LEU A 1 947  ? 180.626 157.647 210.250 1.00 25.16 ? 897 LEU A O   1 
ATOM 3249 C CB  . LEU A 1 947  ? 183.277 158.740 211.873 1.00 23.22 ? 897 LEU A CB  1 
ATOM 3250 C CG  . LEU A 1 947  ? 183.564 159.027 213.349 1.00 22.14 ? 897 LEU A CG  1 
ATOM 3251 C CD1 . LEU A 1 947  ? 184.660 158.116 213.877 1.00 17.05 ? 897 LEU A CD1 1 
ATOM 3252 C CD2 . LEU A 1 947  ? 183.946 160.485 213.538 1.00 24.76 ? 897 LEU A CD2 1 
ATOM 3253 N N   . PHE A 1 948  ? 182.543 157.558 209.050 1.00 17.21 ? 898 PHE A N   1 
ATOM 3254 C CA  . PHE A 1 948  ? 181.840 157.680 207.746 1.00 24.96 ? 898 PHE A CA  1 
ATOM 3255 C C   . PHE A 1 948  ? 180.926 156.466 207.556 1.00 29.22 ? 898 PHE A C   1 
ATOM 3256 O O   . PHE A 1 948  ? 179.766 156.649 207.141 1.00 30.56 ? 898 PHE A O   1 
ATOM 3257 C CB  . PHE A 1 948  ? 182.851 157.813 206.604 1.00 25.41 ? 898 PHE A CB  1 
ATOM 3258 C CG  . PHE A 1 948  ? 183.149 159.234 206.199 1.00 22.25 ? 898 PHE A CG  1 
ATOM 3259 C CD1 . PHE A 1 948  ? 183.955 160.043 206.985 1.00 21.71 ? 898 PHE A CD1 1 
ATOM 3260 C CD2 . PHE A 1 948  ? 182.618 159.767 205.037 1.00 24.82 ? 898 PHE A CD2 1 
ATOM 3261 C CE1 . PHE A 1 948  ? 184.226 161.350 206.613 1.00 21.07 ? 898 PHE A CE1 1 
ATOM 3262 C CE2 . PHE A 1 948  ? 182.889 161.074 204.666 1.00 23.54 ? 898 PHE A CE2 1 
ATOM 3263 C CZ  . PHE A 1 948  ? 183.693 161.864 205.454 1.00 20.31 ? 898 PHE A CZ  1 
ATOM 3264 N N   . VAL A 1 949  ? 181.436 155.267 207.851 1.00 25.54 ? 899 VAL A N   1 
ATOM 3265 C CA  . VAL A 1 949  ? 180.622 154.060 207.739 1.00 24.62 ? 899 VAL A CA  1 
ATOM 3266 C C   . VAL A 1 949  ? 179.431 154.135 208.686 1.00 21.63 ? 899 VAL A C   1 
ATOM 3267 O O   . VAL A 1 949  ? 178.295 153.823 208.308 1.00 20.82 ? 899 VAL A O   1 
ATOM 3268 C CB  . VAL A 1 949  ? 181.481 152.810 208.005 1.00 23.72 ? 899 VAL A CB  1 
ATOM 3269 C CG1 . VAL A 1 949  ? 180.600 151.614 208.334 1.00 20.46 ? 899 VAL A CG1 1 
ATOM 3270 C CG2 . VAL A 1 949  ? 182.368 152.512 206.809 1.00 23.58 ? 899 VAL A CG2 1 
ATOM 3271 N N   . ASN A 1 950  ? 179.670 154.565 209.927 1.00 19.61 ? 900 ASN A N   1 
ATOM 3272 C CA  . ASN A 1 950  ? 178.601 154.649 210.915 1.00 20.22 ? 900 ASN A CA  1 
ATOM 3273 C C   . ASN A 1 950  ? 177.573 155.720 210.576 1.00 22.80 ? 900 ASN A C   1 
ATOM 3274 O O   . ASN A 1 950  ? 176.477 155.709 211.146 1.00 24.18 ? 900 ASN A O   1 
ATOM 3275 C CB  . ASN A 1 950  ? 179.189 154.913 212.301 1.00 17.66 ? 900 ASN A CB  1 
ATOM 3276 C CG  . ASN A 1 950  ? 179.628 153.642 212.997 1.00 21.68 ? 900 ASN A CG  1 
ATOM 3277 O OD1 . ASN A 1 950  ? 179.946 152.644 212.349 1.00 22.99 ? 900 ASN A OD1 1 
ATOM 3278 N ND2 . ASN A 1 950  ? 179.649 153.670 214.324 1.00 23.61 ? 900 ASN A ND2 1 
ATOM 3279 N N   . ALA A 1 951  ? 177.899 156.642 209.676 1.00 23.03 ? 901 ALA A N   1 
ATOM 3280 C CA  . ALA A 1 951  ? 176.965 157.690 209.283 1.00 21.94 ? 901 ALA A CA  1 
ATOM 3281 C C   . ALA A 1 951  ? 175.886 157.137 208.358 1.00 21.88 ? 901 ALA A C   1 
ATOM 3282 O O   . ALA A 1 951  ? 175.064 156.318 208.767 1.00 22.70 ? 901 ALA A O   1 
ATOM 3283 C CB  . ALA A 1 951  ? 177.706 158.838 208.611 1.00 18.39 ? 901 ALA A CB  1 
ATOM 3284 N N   . ASP A 1 987  ? 180.256 152.654 200.470 1.00 41.73 ? 930 ASP A N   1 
ATOM 3285 C CA  . ASP A 1 987  ? 181.461 152.850 201.320 1.00 43.43 ? 930 ASP A CA  1 
ATOM 3286 C C   . ASP A 1 987  ? 181.464 154.281 201.867 1.00 42.17 ? 930 ASP A C   1 
ATOM 3287 O O   . ASP A 1 987  ? 181.397 154.440 203.102 1.00 39.68 ? 930 ASP A O   1 
ATOM 3288 C CB  . ASP A 1 987  ? 182.745 152.535 200.548 1.00 41.59 ? 930 ASP A CB  1 
ATOM 3289 C CG  . ASP A 1 987  ? 182.938 151.055 200.265 1.00 41.18 ? 930 ASP A CG  1 
ATOM 3290 O OD1 . ASP A 1 987  ? 182.239 150.242 200.901 1.00 43.21 ? 930 ASP A OD1 1 
ATOM 3291 O OD2 . ASP A 1 987  ? 183.787 150.728 199.412 1.00 39.80 ? 930 ASP A OD2 1 
ATOM 3292 N N   . PHE A 1 988  ? 181.541 155.275 200.975 1.00 35.92 ? 931 PHE A N   1 
ATOM 3293 C CA  . PHE A 1 988  ? 181.580 156.698 201.404 1.00 32.71 ? 931 PHE A CA  1 
ATOM 3294 C C   . PHE A 1 988  ? 180.402 157.461 200.792 1.00 32.55 ? 931 PHE A C   1 
ATOM 3295 O O   . PHE A 1 988  ? 180.058 157.207 199.621 1.00 32.64 ? 931 PHE A O   1 
ATOM 3296 C CB  . PHE A 1 988  ? 182.906 157.347 201.002 1.00 32.09 ? 931 PHE A CB  1 
ATOM 3297 C CG  . PHE A 1 988  ? 183.934 157.341 202.102 1.00 35.78 ? 931 PHE A CG  1 
ATOM 3298 C CD1 . PHE A 1 988  ? 183.986 156.290 203.001 1.00 35.21 ? 931 PHE A CD1 1 
ATOM 3299 C CD2 . PHE A 1 988  ? 184.835 158.382 202.250 1.00 35.15 ? 931 PHE A CD2 1 
ATOM 3300 C CE1 . PHE A 1 988  ? 184.920 156.273 204.020 1.00 33.21 ? 931 PHE A CE1 1 
ATOM 3301 C CE2 . PHE A 1 988  ? 185.772 158.364 203.271 1.00 35.45 ? 931 PHE A CE2 1 
ATOM 3302 C CZ  . PHE A 1 988  ? 185.813 157.311 204.154 1.00 33.05 ? 931 PHE A CZ  1 
ATOM 3303 N N   . PRO A 1 989  ? 179.769 158.393 201.537 1.00 25.86 ? 932 PRO A N   1 
ATOM 3304 C CA  . PRO A 1 989  ? 178.666 159.195 200.997 1.00 25.49 ? 932 PRO A CA  1 
ATOM 3305 C C   . PRO A 1 989  ? 179.074 159.918 199.706 1.00 23.63 ? 932 PRO A C   1 
ATOM 3306 O O   . PRO A 1 989  ? 180.211 160.333 199.605 1.00 22.30 ? 932 PRO A O   1 
ATOM 3307 C CB  . PRO A 1 989  ? 178.410 160.229 202.102 1.00 22.29 ? 932 PRO A CB  1 
ATOM 3308 C CG  . PRO A 1 989  ? 178.863 159.536 203.367 1.00 22.14 ? 932 PRO A CG  1 
ATOM 3309 C CD  . PRO A 1 989  ? 180.050 158.699 202.940 1.00 25.08 ? 932 PRO A CD  1 
ATOM 3310 N N   . PRO A 1 990  ? 178.164 160.086 198.721 1.00 22.64 ? 933 PRO A N   1 
ATOM 3311 C CA  . PRO A 1 990  ? 178.503 160.718 197.443 1.00 22.22 ? 933 PRO A CA  1 
ATOM 3312 C C   . PRO A 1 990  ? 179.320 162.003 197.645 1.00 16.15 ? 933 PRO A C   1 
ATOM 3313 O O   . PRO A 1 990  ? 178.892 162.864 198.393 1.00 16.86 ? 933 PRO A O   1 
ATOM 3314 C CB  . PRO A 1 990  ? 177.140 161.048 196.810 1.00 21.99 ? 933 PRO A CB  1 
ATOM 3315 C CG  . PRO A 1 990  ? 176.118 160.759 197.895 1.00 23.73 ? 933 PRO A CG  1 
ATOM 3316 C CD  . PRO A 1 990  ? 176.754 159.711 198.783 1.00 19.27 ? 933 PRO A CD  1 
ATOM 3317 N N   . PRO A 1 991  ? 180.488 162.148 196.980 1.00 6.88  ? 934 PRO A N   1 
ATOM 3318 C CA  . PRO A 1 991  ? 181.331 163.338 197.134 1.00 6.61  ? 934 PRO A CA  1 
ATOM 3319 C C   . PRO A 1 991  ? 180.598 164.614 196.699 1.00 15.05 ? 934 PRO A C   1 
ATOM 3320 O O   . PRO A 1 991  ? 180.250 164.720 195.536 1.00 15.95 ? 934 PRO A O   1 
ATOM 3321 C CB  . PRO A 1 991  ? 182.519 163.070 196.197 1.00 4.06  ? 934 PRO A CB  1 
ATOM 3322 C CG  . PRO A 1 991  ? 181.997 162.042 195.218 1.00 13.96 ? 934 PRO A CG  1 
ATOM 3323 C CD  . PRO A 1 991  ? 181.047 161.187 196.029 1.00 7.37  ? 934 PRO A CD  1 
ATOM 3324 N N   . ALA A 1 992  ? 180.384 165.545 197.633 1.00 13.02 ? 935 ALA A N   1 
ATOM 3325 C CA  . ALA A 1 992  ? 179.701 166.787 197.304 1.00 9.20  ? 935 ALA A CA  1 
ATOM 3326 C C   . ALA A 1 992  ? 180.490 167.657 196.337 1.00 14.95 ? 935 ALA A C   1 
ATOM 3327 O O   . ALA A 1 992  ? 179.972 168.687 195.893 1.00 14.55 ? 935 ALA A O   1 
ATOM 3328 C CB  . ALA A 1 992  ? 179.402 167.581 198.579 1.00 13.34 ? 935 ALA A CB  1 
ATOM 3329 N N   . GLY A 1 993  ? 181.725 167.281 196.016 1.00 18.46 ? 936 GLY A N   1 
ATOM 3330 C CA  . GLY A 1 993  ? 182.517 168.013 195.049 1.00 10.05 ? 936 GLY A CA  1 
ATOM 3331 C C   . GLY A 1 993  ? 183.654 167.199 194.468 1.00 5.41  ? 936 GLY A C   1 
ATOM 3332 O O   . GLY A 1 993  ? 184.465 166.625 195.207 1.00 9.84  ? 936 GLY A O   1 
ATOM 3333 N N   . ARG A 1 994  ? 183.734 167.151 193.141 1.00 0.00  ? 937 ARG A N   1 
ATOM 3334 C CA  . ARG A 1 994  ? 184.807 166.448 192.449 1.00 0.00  ? 937 ARG A CA  1 
ATOM 3335 C C   . ARG A 1 994  ? 185.606 167.445 191.626 1.00 0.00  ? 937 ARG A C   1 
ATOM 3336 O O   . ARG A 1 994  ? 185.026 168.256 190.896 1.00 10.38 ? 937 ARG A O   1 
ATOM 3337 C CB  . ARG A 1 994  ? 184.254 165.338 191.554 1.00 0.00  ? 937 ARG A CB  1 
ATOM 3338 C CG  . ARG A 1 994  ? 183.114 164.561 192.178 1.00 2.25  ? 937 ARG A CG  1 
ATOM 3339 C CD  . ARG A 1 994  ? 182.165 164.019 191.122 1.00 12.93 ? 937 ARG A CD  1 
ATOM 3340 N NE  . ARG A 1 994  ? 182.683 162.828 190.459 1.00 11.07 ? 937 ARG A NE  1 
ATOM 3341 C CZ  . ARG A 1 994  ? 182.053 162.182 189.488 1.00 0.00  ? 937 ARG A CZ  1 
ATOM 3342 N NH1 . ARG A 1 994  ? 180.884 162.596 189.029 1.00 0.00  ? 937 ARG A NH1 1 
ATOM 3343 N NH2 . ARG A 1 994  ? 182.609 161.093 188.964 1.00 3.82  ? 937 ARG A NH2 1 
ATOM 3344 N N   . GLU A 1 995  ? 186.931 167.391 191.746 1.00 0.00  ? 938 GLU A N   1 
ATOM 3345 C CA  . GLU A 1 995  ? 187.828 168.277 191.019 1.00 0.00  ? 938 GLU A CA  1 
ATOM 3346 C C   . GLU A 1 995  ? 188.739 167.447 190.128 1.00 0.00  ? 938 GLU A C   1 
ATOM 3347 O O   . GLU A 1 995  ? 189.390 166.511 190.602 1.00 8.88  ? 938 GLU A O   1 
ATOM 3348 C CB  . GLU A 1 995  ? 188.664 169.123 191.981 1.00 0.00  ? 938 GLU A CB  1 
ATOM 3349 C CG  . GLU A 1 995  ? 187.859 170.102 192.819 1.00 8.07  ? 938 GLU A CG  1 
ATOM 3350 C CD  . GLU A 1 995  ? 187.388 169.501 194.127 1.00 3.26  ? 938 GLU A CD  1 
ATOM 3351 O OE1 . GLU A 1 995  ? 187.475 168.266 194.277 1.00 3.32  ? 938 GLU A OE1 1 
ATOM 3352 O OE2 . GLU A 1 995  ? 186.932 170.261 195.006 1.00 0.00  ? 938 GLU A OE2 1 
ATOM 3353 N N   . PHE A 1 996  ? 188.786 167.796 188.845 1.00 0.00  ? 939 PHE A N   1 
ATOM 3354 C CA  . PHE A 1 996  ? 189.650 167.143 187.871 1.00 0.41  ? 939 PHE A CA  1 
ATOM 3355 C C   . PHE A 1 996  ? 190.595 168.172 187.270 1.00 5.06  ? 939 PHE A C   1 
ATOM 3356 O O   . PHE A 1 996  ? 190.215 169.329 187.063 1.00 9.65  ? 939 PHE A O   1 
ATOM 3357 C CB  . PHE A 1 996  ? 188.842 166.486 186.743 1.00 0.00  ? 939 PHE A CB  1 
ATOM 3358 C CG  . PHE A 1 996  ? 187.858 165.450 187.208 1.00 0.00  ? 939 PHE A CG  1 
ATOM 3359 C CD1 . PHE A 1 996  ? 186.595 165.816 187.637 1.00 0.00  ? 939 PHE A CD1 1 
ATOM 3360 C CD2 . PHE A 1 996  ? 188.186 164.107 187.187 1.00 1.70  ? 939 PHE A CD2 1 
ATOM 3361 C CE1 . PHE A 1 996  ? 185.686 164.864 188.052 1.00 0.00  ? 939 PHE A CE1 1 
ATOM 3362 C CE2 . PHE A 1 996  ? 187.279 163.153 187.602 1.00 1.93  ? 939 PHE A CE2 1 
ATOM 3363 C CZ  . PHE A 1 996  ? 186.029 163.534 188.034 1.00 0.00  ? 939 PHE A CZ  1 
ATOM 3364 N N   . ILE A 1 997  ? 191.830 167.738 186.990 1.00 0.00  ? 940 ILE A N   1 
ATOM 3365 C CA  . ILE A 1 997  ? 192.818 168.638 186.322 1.00 0.00  ? 940 ILE A CA  1 
ATOM 3366 C C   . ILE A 1 997  ? 193.468 167.863 185.170 1.00 5.55  ? 940 ILE A C   1 
ATOM 3367 O O   . ILE A 1 997  ? 194.091 166.819 185.443 1.00 18.77 ? 940 ILE A O   1 
ATOM 3368 C CB  . ILE A 1 997  ? 193.853 169.197 187.317 1.00 0.00  ? 940 ILE A CB  1 
ATOM 3369 C CG1 . ILE A 1 997  ? 193.184 169.726 188.589 1.00 0.52  ? 940 ILE A CG1 1 
ATOM 3370 C CG2 . ILE A 1 997  ? 194.714 170.259 186.652 1.00 0.00  ? 940 ILE A CG2 1 
ATOM 3371 C CD1 . ILE A 1 997  ? 194.128 170.476 189.499 1.00 6.56  ? 940 ILE A CD1 1 
ATOM 3372 N N   . LEU A 1 998  ? 193.330 168.360 183.942 1.00 4.58  ? 941 LEU A N   1 
ATOM 3373 C CA  . LEU A 1 998  ? 193.845 167.690 182.720 1.00 0.00  ? 941 LEU A CA  1 
ATOM 3374 C C   . LEU A 1 998  ? 194.932 168.571 182.099 1.00 0.00  ? 941 LEU A C   1 
ATOM 3375 O O   . LEU A 1 998  ? 194.723 169.799 182.043 1.00 12.40 ? 941 LEU A O   1 
ATOM 3376 C CB  . LEU A 1 998  ? 192.681 167.549 181.735 1.00 0.00  ? 941 LEU A CB  1 
ATOM 3377 C CG  . LEU A 1 998  ? 191.893 166.240 181.763 1.00 0.00  ? 941 LEU A CG  1 
ATOM 3378 C CD1 . LEU A 1 998  ? 191.475 165.870 183.176 1.00 0.00  ? 941 LEU A CD1 1 
ATOM 3379 C CD2 . LEU A 1 998  ? 190.667 166.349 180.870 1.00 0.00  ? 941 LEU A CD2 1 
ATOM 3380 N N   . ARG A 1 999  ? 196.036 167.975 181.641 1.00 0.00  ? 942 ARG A N   1 
ATOM 3381 C CA  . ARG A 1 999  ? 197.106 168.719 180.989 1.00 0.00  ? 942 ARG A CA  1 
ATOM 3382 C C   . ARG A 1 999  ? 197.650 167.936 179.803 1.00 7.10  ? 942 ARG A C   1 
ATOM 3383 O O   . ARG A 1 999  ? 197.730 166.704 179.849 1.00 14.81 ? 942 ARG A O   1 
ATOM 3384 C CB  . ARG A 1 999  ? 198.255 169.023 181.954 1.00 0.00  ? 942 ARG A CB  1 
ATOM 3385 C CG  . ARG A 1 999  ? 197.885 169.873 183.152 1.00 0.00  ? 942 ARG A CG  1 
ATOM 3386 C CD  . ARG A 1 999  ? 199.068 169.974 184.098 1.00 3.24  ? 942 ARG A CD  1 
ATOM 3387 N NE  . ARG A 1 999  ? 198.737 170.639 185.351 1.00 1.99  ? 942 ARG A NE  1 
ATOM 3388 C CZ  . ARG A 1 999  ? 198.284 170.012 186.427 1.00 0.00  ? 942 ARG A CZ  1 
ATOM 3389 N NH1 . ARG A 1 999  ? 198.055 168.710 186.421 1.00 0.28  ? 942 ARG A NH1 1 
ATOM 3390 N NH2 . ARG A 1 999  ? 198.048 170.710 187.533 1.00 4.97  ? 942 ARG A NH2 1 
ATOM 3391 N N   . THR A 1 1000 ? 198.016 168.684 178.757 1.00 5.35  ? 943 THR A N   1 
ATOM 3392 C CA  . THR A 1 1000 ? 198.577 168.057 177.536 1.00 0.00  ? 943 THR A CA  1 
ATOM 3393 C C   . THR A 1 1000 ? 199.473 169.069 176.818 1.00 0.00  ? 943 THR A C   1 
ATOM 3394 O O   . THR A 1 1000 ? 199.314 170.279 177.070 1.00 2.85  ? 943 THR A O   1 
ATOM 3395 C CB  . THR A 1 1000 ? 197.466 167.558 176.605 1.00 0.00  ? 943 THR A CB  1 
ATOM 3396 O OG1 . THR A 1 1000 ? 198.006 166.511 175.798 1.00 14.16 ? 943 THR A OG1 1 
ATOM 3397 C CG2 . THR A 1 1000 ? 196.909 168.651 175.720 1.00 0.86  ? 943 THR A CG2 1 
ATOM 3398 N N   . THR A 1 1001 ? 200.384 168.588 175.975 1.00 0.25  ? 944 THR A N   1 
ATOM 3399 C CA  . THR A 1 1001 ? 201.290 169.435 175.197 1.00 6.56  ? 944 THR A CA  1 
ATOM 3400 C C   . THR A 1 1001 ? 201.188 169.022 173.731 1.00 11.07 ? 944 THR A C   1 
ATOM 3401 O O   . THR A 1 1001 ? 201.760 168.004 173.330 1.00 12.14 ? 944 THR A O   1 
ATOM 3402 C CB  . THR A 1 1001 ? 202.723 169.318 175.704 1.00 1.85  ? 944 THR A CB  1 
ATOM 3403 O OG1 . THR A 1 1001 ? 202.762 169.627 177.102 1.00 2.57  ? 944 THR A OG1 1 
ATOM 3404 C CG2 . THR A 1 1001 ? 203.632 170.274 174.955 1.00 0.00  ? 944 THR A CG2 1 
ATOM 3405 N N   . VAL A 1 1002 ? 200.429 169.769 172.927 1.00 4.53  ? 945 VAL A N   1 
ATOM 3406 C CA  . VAL A 1 1002 ? 200.230 169.331 171.512 1.00 0.18  ? 945 VAL A CA  1 
ATOM 3407 C C   . VAL A 1 1002 ? 200.507 170.510 170.571 1.00 2.04  ? 945 VAL A C   1 
ATOM 3408 O O   . VAL A 1 1002 ? 200.406 171.668 171.025 1.00 3.74  ? 945 VAL A O   1 
ATOM 3409 C CB  . VAL A 1 1002 ? 198.825 168.733 171.294 1.00 0.00  ? 945 VAL A CB  1 
ATOM 3410 C CG1 . VAL A 1 1002 ? 198.647 167.411 172.026 1.00 5.73  ? 945 VAL A CG1 1 
ATOM 3411 C CG2 . VAL A 1 1002 ? 197.727 169.712 171.678 1.00 0.00  ? 945 VAL A CG2 1 
ATOM 3412 N N   . PRO A 1 1003 ? 200.854 170.268 169.286 1.00 5.71  ? 946 PRO A N   1 
ATOM 3413 C CA  . PRO A 1 1003 ? 201.149 171.346 168.332 1.00 6.24  ? 946 PRO A CA  1 
ATOM 3414 C C   . PRO A 1 1003 ? 199.894 171.972 167.703 1.00 4.94  ? 946 PRO A C   1 
ATOM 3415 O O   . PRO A 1 1003 ? 199.635 171.719 166.540 1.00 7.78  ? 946 PRO A O   1 
ATOM 3416 C CB  . PRO A 1 1003 ? 201.975 170.631 167.253 1.00 0.00  ? 946 PRO A CB  1 
ATOM 3417 C CG  . PRO A 1 1003 ? 201.402 169.232 167.218 1.00 0.00  ? 946 PRO A CG  1 
ATOM 3418 C CD  . PRO A 1 1003 ? 200.943 168.948 168.634 1.00 4.50  ? 946 PRO A CD  1 
ATOM 3419 N N   . ARG A 1 1004 ? 199.212 172.832 168.442 1.00 0.00  ? 947 ARG A N   1 
ATOM 3420 C CA  . ARG A 1 1004 ? 197.964 173.448 167.934 1.00 4.07  ? 947 ARG A CA  1 
ATOM 3421 C C   . ARG A 1 1004 ? 198.341 174.749 167.212 1.00 1.05  ? 947 ARG A C   1 
ATOM 3422 O O   . ARG A 1 1004 ? 199.412 175.298 167.558 1.00 5.15  ? 947 ARG A O   1 
ATOM 3423 C CB  . ARG A 1 1004 ? 197.099 173.576 169.185 1.00 0.00  ? 947 ARG A CB  1 
ATOM 3424 C CG  . ARG A 1 1004 ? 195.715 174.193 169.026 1.00 0.00  ? 947 ARG A CG  1 
ATOM 3425 C CD  . ARG A 1 1004 ? 194.926 173.997 170.318 1.00 0.00  ? 947 ARG A CD  1 
ATOM 3426 N NE  . ARG A 1 1004 ? 193.721 174.810 170.379 1.00 0.87  ? 947 ARG A NE  1 
ATOM 3427 C CZ  . ARG A 1 1004 ? 192.868 174.802 171.397 1.00 1.37  ? 947 ARG A CZ  1 
ATOM 3428 N NH1 . ARG A 1 1004 ? 193.121 174.066 172.463 1.00 0.00  ? 947 ARG A NH1 1 
ATOM 3429 N NH2 . ARG A 1 1004 ? 191.764 175.528 171.344 1.00 0.00  ? 947 ARG A NH2 1 
ATOM 3430 N N   . PRO A 1 1005 ? 197.550 175.268 166.237 1.00 2.61  ? 948 PRO A N   1 
ATOM 3431 C CA  . PRO A 1 1005 ? 196.396 174.555 165.678 1.00 1.79  ? 948 PRO A CA  1 
ATOM 3432 C C   . PRO A 1 1005 ? 196.710 173.843 164.355 1.00 7.54  ? 948 PRO A C   1 
ATOM 3433 O O   . PRO A 1 1005 ? 195.811 173.243 163.799 1.00 11.11 ? 948 PRO A O   1 
ATOM 3434 C CB  . PRO A 1 1005 ? 195.429 175.715 165.415 1.00 2.53  ? 948 PRO A CB  1 
ATOM 3435 C CG  . PRO A 1 1005 ? 196.337 176.844 164.973 1.00 2.53  ? 948 PRO A CG  1 
ATOM 3436 C CD  . PRO A 1 1005 ? 197.629 176.645 165.740 1.00 3.86  ? 948 PRO A CD  1 
ATOM 3437 N N   . ALA A 1 1006 ? 197.955 173.937 163.881 1.00 9.56  ? 949 ALA A N   1 
ATOM 3438 C CA  . ALA A 1 1006 ? 198.356 173.282 162.646 1.00 3.09  ? 949 ALA A CA  1 
ATOM 3439 C C   . ALA A 1 1006 ? 199.638 172.493 162.869 1.00 0.00  ? 949 ALA A C   1 
ATOM 3440 O O   . ALA A 1 1006 ? 200.441 172.844 163.738 1.00 6.29  ? 949 ALA A O   1 
ATOM 3441 C CB  . ALA A 1 1006 ? 198.567 174.308 161.523 1.00 0.62  ? 949 ALA A CB  1 
ATOM 3442 N N   . PRO A 1 1007 ? 199.861 171.427 162.094 1.00 0.80  ? 950 PRO A N   1 
ATOM 3443 C CA  . PRO A 1 1007 ? 201.012 170.548 162.366 1.00 6.20  ? 950 PRO A CA  1 
ATOM 3444 C C   . PRO A 1 1007 ? 202.367 171.218 162.221 1.00 4.33  ? 950 PRO A C   1 
ATOM 3445 O O   . PRO A 1 1007 ? 203.348 170.711 162.778 1.00 7.02  ? 950 PRO A O   1 
ATOM 3446 C CB  . PRO A 1 1007 ? 200.840 169.417 161.342 1.00 7.47  ? 950 PRO A CB  1 
ATOM 3447 C CG  . PRO A 1 1007 ? 199.402 169.461 160.961 1.00 6.78  ? 950 PRO A CG  1 
ATOM 3448 C CD  . PRO A 1 1007 ? 199.032 170.907 160.995 1.00 7.80  ? 950 PRO A CD  1 
ATOM 3449 N N   . TYR A 1 1008 ? 202.466 172.329 161.493 1.00 0.00  ? 951 TYR A N   1 
ATOM 3450 C CA  . TYR A 1 1008 ? 203.733 173.025 161.312 1.00 1.59  ? 951 TYR A CA  1 
ATOM 3451 C C   . TYR A 1 1008 ? 203.929 174.145 162.327 1.00 2.13  ? 951 TYR A C   1 
ATOM 3452 O O   . TYR A 1 1008 ? 204.757 175.036 162.106 1.00 1.93  ? 951 TYR A O   1 
ATOM 3453 C CB  . TYR A 1 1008 ? 203.840 173.576 159.890 1.00 7.28  ? 951 TYR A CB  1 
ATOM 3454 C CG  . TYR A 1 1008 ? 202.587 174.256 159.396 1.00 3.32  ? 951 TYR A CG  1 
ATOM 3455 C CD1 . TYR A 1 1008 ? 201.594 173.538 158.747 1.00 2.63  ? 951 TYR A CD1 1 
ATOM 3456 C CD2 . TYR A 1 1008 ? 202.398 175.615 159.578 1.00 0.39  ? 951 TYR A CD2 1 
ATOM 3457 C CE1 . TYR A 1 1008 ? 200.452 174.153 158.298 1.00 0.00  ? 951 TYR A CE1 1 
ATOM 3458 C CE2 . TYR A 1 1008 ? 201.259 176.238 159.131 1.00 1.77  ? 951 TYR A CE2 1 
ATOM 3459 C CZ  . TYR A 1 1008 ? 200.290 175.502 158.493 1.00 1.47  ? 951 TYR A CZ  1 
ATOM 3460 O OH  . TYR A 1 1008 ? 199.151 176.123 158.045 1.00 12.49 ? 951 TYR A OH  1 
ATOM 3461 N N   . SER A 1 1009 ? 203.147 174.087 163.407 1.00 1.00  ? 952 SER A N   1 
ATOM 3462 C CA  . SER A 1 1009 ? 203.230 175.133 164.453 1.00 1.17  ? 952 SER A CA  1 
ATOM 3463 C C   . SER A 1 1009 ? 203.961 174.586 165.679 1.00 2.11  ? 952 SER A C   1 
ATOM 3464 O O   . SER A 1 1009 ? 204.271 173.379 165.695 1.00 2.54  ? 952 SER A O   1 
ATOM 3465 C CB  . SER A 1 1009 ? 201.858 175.632 164.819 1.00 3.51  ? 952 SER A CB  1 
ATOM 3466 O OG  . SER A 1 1009 ? 201.153 174.654 165.568 1.00 11.65 ? 952 SER A OG  1 
ATOM 3467 N N   . LYS A 1 1010 ? 204.211 175.445 166.664 1.00 2.94  ? 953 LYS A N   1 
ATOM 3468 C CA  . LYS A 1 1010 ? 204.902 175.057 167.885 1.00 6.59  ? 953 LYS A CA  1 
ATOM 3469 C C   . LYS A 1 1010 ? 204.029 174.150 168.746 1.00 7.16  ? 953 LYS A C   1 
ATOM 3470 O O   . LYS A 1 1010 ? 202.798 174.189 168.682 1.00 4.86  ? 953 LYS A O   1 
ATOM 3471 C CB  . LYS A 1 1010 ? 205.300 176.296 168.687 1.00 4.50  ? 953 LYS A CB  1 
ATOM 3472 C CG  . LYS A 1 1010 ? 206.357 177.169 168.026 1.00 3.23  ? 953 LYS A CG  1 
ATOM 3473 C CD  . LYS A 1 1010 ? 206.681 178.390 168.869 1.00 8.21  ? 953 LYS A CD  1 
ATOM 3474 C CE  . LYS A 1 1010 ? 207.755 179.240 168.211 1.00 7.93  ? 953 LYS A CE  1 
ATOM 3475 N NZ  . LYS A 1 1010 ? 208.069 180.453 169.011 1.00 11.10 ? 953 LYS A NZ  1 
ATOM 3476 N N   . ALA A 1 1011 ? 204.687 173.321 169.553 1.00 2.89  ? 954 ALA A N   1 
ATOM 3477 C CA  . ALA A 1 1011 ? 203.997 172.483 170.525 1.00 0.00  ? 954 ALA A CA  1 
ATOM 3478 C C   . ALA A 1 1011 ? 203.790 173.275 171.809 1.00 0.00  ? 954 ALA A C   1 
ATOM 3479 O O   . ALA A 1 1011 ? 204.760 173.667 172.467 1.00 10.38 ? 954 ALA A O   1 
ATOM 3480 C CB  . ALA A 1 1011 ? 204.797 171.212 170.797 1.00 0.00  ? 954 ALA A CB  1 
ATOM 3481 N N   . LEU A 1 1012 ? 202.530 173.504 172.170 1.00 5.32  ? 955 LEU A N   1 
ATOM 3482 C CA  . LEU A 1 1012 ? 202.171 174.349 173.292 1.00 3.84  ? 955 LEU A CA  1 
ATOM 3483 C C   . LEU A 1 1012 ? 201.326 173.577 174.300 1.00 1.72  ? 955 LEU A C   1 
ATOM 3484 O O   . LEU A 1 1012 ? 200.662 172.596 173.942 1.00 5.59  ? 955 LEU A O   1 
ATOM 3485 C CB  . LEU A 1 1012 ? 201.403 175.585 172.808 1.00 1.43  ? 955 LEU A CB  1 
ATOM 3486 C CG  . LEU A 1 1012 ? 202.056 176.322 171.638 1.00 0.38  ? 955 LEU A CG  1 
ATOM 3487 C CD1 . LEU A 1 1012 ? 201.113 177.351 171.055 1.00 1.87  ? 955 LEU A CD1 1 
ATOM 3488 C CD2 . LEU A 1 1012 ? 203.351 176.976 172.079 1.00 0.00  ? 955 LEU A CD2 1 
ATOM 3489 N N   . PRO A 1 1013 ? 201.367 173.977 175.583 1.00 0.00  ? 956 PRO A N   1 
ATOM 3490 C CA  . PRO A 1 1013 ? 200.628 173.245 176.622 1.00 0.00  ? 956 PRO A CA  1 
ATOM 3491 C C   . PRO A 1 1013 ? 199.197 173.716 176.838 1.00 0.00  ? 956 PRO A C   1 
ATOM 3492 O O   . PRO A 1 1013 ? 198.956 174.881 177.166 1.00 8.88  ? 956 PRO A O   1 
ATOM 3493 C CB  . PRO A 1 1013 ? 201.474 173.491 177.874 1.00 0.00  ? 956 PRO A CB  1 
ATOM 3494 C CG  . PRO A 1 1013 ? 202.097 174.815 177.640 1.00 1.26  ? 956 PRO A CG  1 
ATOM 3495 C CD  . PRO A 1 1013 ? 202.333 174.929 176.161 1.00 0.00  ? 956 PRO A CD  1 
ATOM 3496 N N   . GLN A 1 1014 ? 198.252 172.786 176.649 1.00 0.00  ? 957 GLN A N   1 
ATOM 3497 C CA  . GLN A 1 1014 ? 196.823 173.091 176.920 1.00 0.00  ? 957 GLN A CA  1 
ATOM 3498 C C   . GLN A 1 1014 ? 196.487 172.538 178.306 1.00 2.03  ? 957 GLN A C   1 
ATOM 3499 O O   . GLN A 1 1014 ? 196.885 171.392 178.594 1.00 7.82  ? 957 GLN A O   1 
ATOM 3500 C CB  . GLN A 1 1014 ? 195.908 172.456 175.873 1.00 0.00  ? 957 GLN A CB  1 
ATOM 3501 C CG  . GLN A 1 1014 ? 195.731 173.283 174.607 1.00 0.00  ? 957 GLN A CG  1 
ATOM 3502 C CD  . GLN A 1 1014 ? 197.008 173.402 173.814 1.00 0.00  ? 957 GLN A CD  1 
ATOM 3503 O OE1 . GLN A 1 1014 ? 197.408 174.491 173.410 1.00 0.00  ? 957 GLN A OE1 1 
ATOM 3504 N NE2 . GLN A 1 1014 ? 197.644 172.274 173.551 1.00 0.00  ? 957 GLN A NE2 1 
ATOM 3505 N N   . ARG A 1 1015 ? 195.784 173.318 179.125 1.00 0.00  ? 958 ARG A N   1 
ATOM 3506 C CA  . ARG A 1 1015 ? 195.446 172.905 180.512 1.00 0.00  ? 958 ARG A CA  1 
ATOM 3507 C C   . ARG A 1 1015 ? 193.971 173.192 180.804 1.00 0.00  ? 958 ARG A C   1 
ATOM 3508 O O   . ARG A 1 1015 ? 193.474 174.242 180.352 1.00 10.68 ? 958 ARG A O   1 
ATOM 3509 C CB  . ARG A 1 1015 ? 196.356 173.636 181.505 1.00 0.00  ? 958 ARG A CB  1 
ATOM 3510 C CG  . ARG A 1 1015 ? 196.001 173.413 182.968 1.00 0.35  ? 958 ARG A CG  1 
ATOM 3511 C CD  . ARG A 1 1015 ? 195.982 174.712 183.753 1.00 0.00  ? 958 ARG A CD  1 
ATOM 3512 N NE  . ARG A 1 1015 ? 195.374 174.558 185.067 1.00 0.00  ? 958 ARG A NE  1 
ATOM 3513 C CZ  . ARG A 1 1015 ? 196.043 174.262 186.175 1.00 0.00  ? 958 ARG A CZ  1 
ATOM 3514 N NH1 . ARG A 1 1015 ? 197.352 174.089 186.132 1.00 0.00  ? 958 ARG A NH1 1 
ATOM 3515 N NH2 . ARG A 1 1015 ? 195.400 174.140 187.323 1.00 0.00  ? 958 ARG A NH2 1 
ATOM 3516 N N   . MET A 1 1016 ? 193.321 172.276 181.538 1.00 0.00  ? 959 MET A N   1 
ATOM 3517 C CA  . MET A 1 1016 ? 191.870 172.411 181.843 1.00 0.00  ? 959 MET A CA  1 
ATOM 3518 C C   . MET A 1 1016 ? 191.571 171.977 183.283 1.00 0.00  ? 959 MET A C   1 
ATOM 3519 O O   . MET A 1 1016 ? 192.002 170.870 183.661 1.00 0.75  ? 959 MET A O   1 
ATOM 3520 C CB  . MET A 1 1016 ? 191.040 171.555 180.881 1.00 0.00  ? 959 MET A CB  1 
ATOM 3521 C CG  . MET A 1 1016 ? 189.544 171.687 181.087 1.00 0.13  ? 959 MET A CG  1 
ATOM 3522 S SD  . MET A 1 1016 ? 188.626 170.300 180.373 1.00 16.01 ? 959 MET A SD  1 
ATOM 3523 C CE  . MET A 1 1016 ? 187.029 171.067 180.106 1.00 7.59  ? 959 MET A CE  1 
ATOM 3524 N N   . TYR A 1 1017 ? 190.864 172.811 184.048 1.00 0.00  ? 960 TYR A N   1 
ATOM 3525 C CA  . TYR A 1 1017 ? 190.455 172.530 185.415 1.00 1.90  ? 960 TYR A CA  1 
ATOM 3526 C C   . TYR A 1 1017 ? 188.939 172.422 185.431 1.00 0.00  ? 960 TYR A C   1 
ATOM 3527 O O   . TYR A 1 1017 ? 188.254 173.202 184.766 1.00 13.01 ? 960 TYR A O   1 
ATOM 3528 C CB  . TYR A 1 1017 ? 190.923 173.646 186.365 1.00 0.00  ? 960 TYR A CB  1 
ATOM 3529 C CG  . TYR A 1 1017 ? 190.695 173.391 187.841 1.00 0.00  ? 960 TYR A CG  1 
ATOM 3530 C CD1 . TYR A 1 1017 ? 189.425 173.474 188.399 1.00 0.00  ? 960 TYR A CD1 1 
ATOM 3531 C CD2 . TYR A 1 1017 ? 191.758 173.100 188.682 1.00 0.00  ? 960 TYR A CD2 1 
ATOM 3532 C CE1 . TYR A 1 1017 ? 189.218 173.248 189.742 1.00 0.00  ? 960 TYR A CE1 1 
ATOM 3533 C CE2 . TYR A 1 1017 ? 191.561 172.875 190.027 1.00 2.32  ? 960 TYR A CE2 1 
ATOM 3534 C CZ  . TYR A 1 1017 ? 190.289 172.950 190.552 1.00 4.02  ? 960 TYR A CZ  1 
ATOM 3535 O OH  . TYR A 1 1017 ? 190.089 172.728 191.895 1.00 0.00  ? 960 TYR A OH  1 
ATOM 3536 N N   . SER A 1 1018 ? 188.406 171.456 186.173 1.00 0.00  ? 961 SER A N   1 
ATOM 3537 C CA  . SER A 1 1018 ? 186.960 171.303 186.242 1.00 4.01  ? 961 SER A CA  1 
ATOM 3538 C C   . SER A 1 1018 ? 186.538 170.966 187.661 1.00 0.00  ? 961 SER A C   1 
ATOM 3539 O O   . SER A 1 1018 ? 187.182 170.155 188.330 1.00 16.96 ? 961 SER A O   1 
ATOM 3540 C CB  . SER A 1 1018 ? 186.471 170.215 185.285 1.00 0.00  ? 961 SER A CB  1 
ATOM 3541 O OG  . SER A 1 1018 ? 186.781 168.932 185.791 1.00 3.13  ? 961 SER A OG  1 
ATOM 3542 N N   . VAL A 1 1019 ? 185.456 171.591 188.118 1.00 0.00  ? 962 VAL A N   1 
ATOM 3543 C CA  . VAL A 1 1019 ? 184.869 171.278 189.415 1.00 0.00  ? 962 VAL A CA  1 
ATOM 3544 C C   . VAL A 1 1019 ? 183.378 171.030 189.231 1.00 7.56  ? 962 VAL A C   1 
ATOM 3545 O O   . VAL A 1 1019 ? 182.671 171.843 188.618 1.00 25.91 ? 962 VAL A O   1 
ATOM 3546 C CB  . VAL A 1 1019 ? 185.124 172.386 190.456 1.00 0.00  ? 962 VAL A CB  1 
ATOM 3547 C CG1 . VAL A 1 1019 ? 184.709 173.738 189.927 1.00 8.10  ? 962 VAL A CG1 1 
ATOM 3548 C CG2 . VAL A 1 1019 ? 184.386 172.075 191.745 1.00 0.00  ? 962 VAL A CG2 1 
ATOM 3549 N N   . LEU A 1 1020 ? 182.907 169.900 189.750 1.00 3.61  ? 963 LEU A N   1 
ATOM 3550 C CA  . LEU A 1 1020 ? 181.513 169.495 189.636 1.00 5.00  ? 963 LEU A CA  1 
ATOM 3551 C C   . LEU A 1 1020 ? 180.921 169.319 191.026 1.00 11.12 ? 963 LEU A C   1 
ATOM 3552 O O   . LEU A 1 1020 ? 181.485 168.602 191.864 1.00 18.33 ? 963 LEU A O   1 
ATOM 3553 C CB  . LEU A 1 1020 ? 181.374 168.200 188.830 1.00 3.35  ? 963 LEU A CB  1 
ATOM 3554 C CG  . LEU A 1 1020 ? 182.093 168.148 187.481 1.00 5.89  ? 963 LEU A CG  1 
ATOM 3555 C CD1 . LEU A 1 1020 ? 183.469 167.528 187.619 1.00 7.87  ? 963 LEU A CD1 1 
ATOM 3556 C CD2 . LEU A 1 1020 ? 181.264 167.379 186.471 1.00 8.16  ? 963 LEU A CD2 1 
ATOM 3557 N N   . THR A 1 1021 ? 179.790 169.985 191.263 1.00 2.57  ? 964 THR A N   1 
ATOM 3558 C CA  . THR A 1 1021 ? 179.034 169.855 192.501 1.00 8.41  ? 964 THR A CA  1 
ATOM 3559 C C   . THR A 1 1021 ? 177.594 169.482 192.178 1.00 6.93  ? 964 THR A C   1 
ATOM 3560 O O   . THR A 1 1021 ? 177.277 169.157 191.030 1.00 6.70  ? 964 THR A O   1 
ATOM 3561 C CB  . THR A 1 1021 ? 179.071 171.151 193.315 1.00 14.56 ? 964 THR A CB  1 
ATOM 3562 O OG1 . THR A 1 1021 ? 178.057 172.042 192.839 1.00 16.53 ? 964 THR A OG1 1 
ATOM 3563 C CG2 . THR A 1 1021 ? 180.428 171.828 193.197 1.00 12.12 ? 964 THR A CG2 1 
ATOM 3564 N N   . LYS A 1 1022 ? 176.713 169.522 193.178 1.00 10.62 ? 965 LYS A N   1 
ATOM 3565 C CA  . LYS A 1 1022 ? 175.322 169.152 192.939 1.00 11.88 ? 965 LYS A CA  1 
ATOM 3566 C C   . LYS A 1 1022 ? 174.564 170.234 192.178 1.00 16.95 ? 965 LYS A C   1 
ATOM 3567 O O   . LYS A 1 1022 ? 173.653 169.919 191.405 1.00 20.29 ? 965 LYS A O   1 
ATOM 3568 C CB  . LYS A 1 1022 ? 174.624 168.844 194.263 1.00 10.45 ? 965 LYS A CB  1 
ATOM 3569 C CG  . LYS A 1 1022 ? 175.560 168.405 195.375 1.00 16.83 ? 965 LYS A CG  1 
ATOM 3570 C CD  . LYS A 1 1022 ? 174.786 168.080 196.642 1.00 18.35 ? 965 LYS A CD  1 
ATOM 3571 C CE  . LYS A 1 1022 ? 175.706 167.575 197.741 1.00 17.57 ? 965 LYS A CE  1 
ATOM 3572 N NZ  . LYS A 1 1022 ? 175.145 166.376 198.424 1.00 15.50 ? 965 LYS A NZ  1 
ATOM 3573 N N   . GLU A 1 1023 ? 174.914 171.504 192.382 1.00 17.87 ? 966 GLU A N   1 
ATOM 3574 C CA  . GLU A 1 1023 ? 174.241 172.607 191.712 1.00 15.39 ? 966 GLU A CA  1 
ATOM 3575 C C   . GLU A 1 1023 ? 175.174 173.463 190.867 1.00 13.54 ? 966 GLU A C   1 
ATOM 3576 O O   . GLU A 1 1023 ? 174.705 174.398 190.209 1.00 9.07  ? 966 GLU A O   1 
ATOM 3577 C CB  . GLU A 1 1023 ? 173.530 173.500 192.738 1.00 14.96 ? 966 GLU A CB  1 
ATOM 3578 C CG  . GLU A 1 1023 ? 174.223 173.567 194.088 1.00 16.27 ? 966 GLU A CG  1 
ATOM 3579 C CD  . GLU A 1 1023 ? 173.537 172.715 195.135 1.00 16.87 ? 966 GLU A CD  1 
ATOM 3580 O OE1 . GLU A 1 1023 ? 173.047 171.621 194.784 1.00 13.54 ? 966 GLU A OE1 1 
ATOM 3581 O OE2 . GLU A 1 1023 ? 173.488 173.138 196.309 1.00 18.13 ? 966 GLU A OE2 1 
ATOM 3582 N N   . ASP A 1 1024 ? 176.474 173.155 190.919 1.00 16.98 ? 967 ASP A N   1 
ATOM 3583 C CA  . ASP A 1 1024 ? 177.473 173.986 190.198 1.00 6.74  ? 967 ASP A CA  1 
ATOM 3584 C C   . ASP A 1 1024 ? 178.290 173.117 189.238 1.00 12.12 ? 967 ASP A C   1 
ATOM 3585 O O   . ASP A 1 1024 ? 178.505 171.930 189.553 1.00 22.00 ? 967 ASP A O   1 
ATOM 3586 C CB  . ASP A 1 1024 ? 178.373 174.741 191.180 1.00 4.33  ? 967 ASP A CB  1 
ATOM 3587 C CG  . ASP A 1 1024 ? 179.571 175.397 190.517 1.00 6.76  ? 967 ASP A CG  1 
ATOM 3588 O OD1 . ASP A 1 1024 ? 179.354 176.249 189.634 1.00 11.21 ? 967 ASP A OD1 1 
ATOM 3589 O OD2 . ASP A 1 1024 ? 180.710 175.045 190.885 1.00 11.49 ? 967 ASP A OD2 1 
ATOM 3590 N N   . PHE A 1 1025 ? 178.728 173.697 188.120 1.00 4.61  ? 968 PHE A N   1 
ATOM 3591 C CA  . PHE A 1 1025 ? 179.524 172.987 187.121 1.00 8.18  ? 968 PHE A CA  1 
ATOM 3592 C C   . PHE A 1 1025 ? 180.431 174.030 186.474 1.00 1.45  ? 968 PHE A C   1 
ATOM 3593 O O   . PHE A 1 1025 ? 179.963 174.837 185.665 1.00 2.50  ? 968 PHE A O   1 
ATOM 3594 C CB  . PHE A 1 1025 ? 178.626 172.297 186.100 1.00 7.50  ? 968 PHE A CB  1 
ATOM 3595 C CG  . PHE A 1 1025 ? 179.361 171.726 184.918 1.00 4.22  ? 968 PHE A CG  1 
ATOM 3596 C CD1 . PHE A 1 1025 ? 180.083 170.551 185.034 1.00 5.64  ? 968 PHE A CD1 1 
ATOM 3597 C CD2 . PHE A 1 1025 ? 179.311 172.353 183.687 1.00 4.87  ? 968 PHE A CD2 1 
ATOM 3598 C CE1 . PHE A 1 1025 ? 180.752 170.024 183.949 1.00 6.59  ? 968 PHE A CE1 1 
ATOM 3599 C CE2 . PHE A 1 1025 ? 179.978 171.829 182.600 1.00 2.46  ? 968 PHE A CE2 1 
ATOM 3600 C CZ  . PHE A 1 1025 ? 180.698 170.664 182.732 1.00 3.73  ? 968 PHE A CZ  1 
ATOM 3601 N N   . ARG A 1 1026 ? 181.708 174.031 186.852 1.00 0.00  ? 969 ARG A N   1 
ATOM 3602 C CA  . ARG A 1 1026 ? 182.642 175.050 186.395 1.00 0.00  ? 969 ARG A CA  1 
ATOM 3603 C C   . ARG A 1 1026 ? 183.787 174.402 185.638 1.00 0.00  ? 969 ARG A C   1 
ATOM 3604 O O   . ARG A 1 1026 ? 184.406 173.452 186.131 1.00 11.17 ? 969 ARG A O   1 
ATOM 3605 C CB  . ARG A 1 1026 ? 183.203 175.861 187.565 1.00 0.00  ? 969 ARG A CB  1 
ATOM 3606 C CG  . ARG A 1 1026 ? 182.187 176.710 188.297 1.00 6.85  ? 969 ARG A CG  1 
ATOM 3607 C CD  . ARG A 1 1026 ? 182.875 177.763 189.147 1.00 3.86  ? 969 ARG A CD  1 
ATOM 3608 N NE  . ARG A 1 1026 ? 183.293 178.905 188.345 1.00 5.64  ? 969 ARG A NE  1 
ATOM 3609 C CZ  . ARG A 1 1026 ? 182.588 180.019 188.210 1.00 1.04  ? 969 ARG A CZ  1 
ATOM 3610 N NH1 . ARG A 1 1026 ? 181.437 180.188 188.838 1.00 1.41  ? 969 ARG A NH1 1 
ATOM 3611 N NH2 . ARG A 1 1026 ? 183.048 180.985 187.422 1.00 1.38  ? 969 ARG A NH2 1 
ATOM 3612 N N   . LEU A 1 1027 ? 184.072 174.923 184.450 1.00 3.87  ? 970 LEU A N   1 
ATOM 3613 C CA  . LEU A 1 1027 ? 185.258 174.558 183.691 1.00 1.19  ? 970 LEU A CA  1 
ATOM 3614 C C   . LEU A 1 1027 ? 186.073 175.819 183.442 1.00 2.89  ? 970 LEU A C   1 
ATOM 3615 O O   . LEU A 1 1027 ? 185.526 176.838 183.008 1.00 19.55 ? 970 LEU A O   1 
ATOM 3616 C CB  . LEU A 1 1027 ? 184.896 173.886 182.362 1.00 0.13  ? 970 LEU A CB  1 
ATOM 3617 C CG  . LEU A 1 1027 ? 183.753 172.865 182.310 1.00 1.11  ? 970 LEU A CG  1 
ATOM 3618 C CD1 . LEU A 1 1027 ? 183.368 172.554 180.873 1.00 1.65  ? 970 LEU A CD1 1 
ATOM 3619 C CD2 . LEU A 1 1027 ? 184.130 171.589 183.025 1.00 3.92  ? 970 LEU A CD2 1 
ATOM 3620 N N   . ALA A 1 1028 ? 187.371 175.752 183.727 1.00 0.00  ? 971 ALA A N   1 
ATOM 3621 C CA  . ALA A 1 1028 ? 188.287 176.861 183.495 1.00 0.00  ? 971 ALA A CA  1 
ATOM 3622 C C   . ALA A 1 1028 ? 189.450 176.350 182.659 1.00 0.46  ? 971 ALA A C   1 
ATOM 3623 O O   . ALA A 1 1028 ? 190.217 175.498 183.118 1.00 18.33 ? 971 ALA A O   1 
ATOM 3624 C CB  . ALA A 1 1028 ? 188.785 177.451 184.815 1.00 0.00  ? 971 ALA A CB  1 
ATOM 3625 N N   . GLY A 1 1029 ? 189.580 176.863 181.439 1.00 0.00  ? 972 GLY A N   1 
ATOM 3626 C CA  . GLY A 1 1029 ? 190.566 176.328 180.523 1.00 0.00  ? 972 GLY A CA  1 
ATOM 3627 C C   . GLY A 1 1029 ? 191.557 177.332 179.978 1.00 0.00  ? 972 GLY A C   1 
ATOM 3628 O O   . GLY A 1 1029 ? 191.183 178.447 179.595 1.00 22.89 ? 972 GLY A O   1 
ATOM 3629 N N   . ALA A 1 1030 ? 192.828 176.939 179.931 1.00 0.00  ? 973 ALA A N   1 
ATOM 3630 C CA  . ALA A 1 1030 ? 193.898 177.747 179.357 1.00 0.00  ? 973 ALA A CA  1 
ATOM 3631 C C   . ALA A 1 1030 ? 194.388 177.022 178.110 1.00 0.00  ? 973 ALA A C   1 
ATOM 3632 O O   . ALA A 1 1030 ? 195.120 176.030 178.202 1.00 6.37  ? 973 ALA A O   1 
ATOM 3633 C CB  . ALA A 1 1030 ? 195.025 177.962 180.359 1.00 0.52  ? 973 ALA A CB  1 
ATOM 3634 N N   . PHE A 1 1031 ? 193.976 177.518 176.948 1.00 1.26  ? 974 PHE A N   1 
ATOM 3635 C CA  . PHE A 1 1031 ? 194.280 176.885 175.671 1.00 0.00  ? 974 PHE A CA  1 
ATOM 3636 C C   . PHE A 1 1031 ? 195.222 177.778 174.881 1.00 0.00  ? 974 PHE A C   1 
ATOM 3637 O O   . PHE A 1 1031 ? 194.995 178.987 174.775 1.00 26.28 ? 974 PHE A O   1 
ATOM 3638 C CB  . PHE A 1 1031 ? 193.005 176.622 174.867 1.00 0.00  ? 974 PHE A CB  1 
ATOM 3639 C CG  . PHE A 1 1031 ? 192.078 175.631 175.507 1.00 0.00  ? 974 PHE A CG  1 
ATOM 3640 C CD1 . PHE A 1 1031 ? 192.423 174.295 175.595 1.00 5.04  ? 974 PHE A CD1 1 
ATOM 3641 C CD2 . PHE A 1 1031 ? 190.858 176.034 176.016 1.00 0.00  ? 974 PHE A CD2 1 
ATOM 3642 C CE1 . PHE A 1 1031 ? 191.574 173.385 176.184 1.00 1.26  ? 974 PHE A CE1 1 
ATOM 3643 C CE2 . PHE A 1 1031 ? 190.007 175.126 176.605 1.00 0.00  ? 974 PHE A CE2 1 
ATOM 3644 C CZ  . PHE A 1 1031 ? 190.366 173.800 176.687 1.00 1.53  ? 974 PHE A CZ  1 
ATOM 3645 N N   . SER A 1 1032 ? 196.290 177.163 174.372 1.00 0.00  ? 975 SER A N   1 
ATOM 3646 C CA  . SER A 1 1032 ? 197.335 177.954 173.681 1.00 0.00  ? 975 SER A CA  1 
ATOM 3647 C C   . SER A 1 1032 ? 197.269 177.765 172.168 1.00 2.49  ? 975 SER A C   1 
ATOM 3648 O O   . SER A 1 1032 ? 196.812 176.694 171.720 1.00 6.31  ? 975 SER A O   1 
ATOM 3649 C CB  . SER A 1 1032 ? 198.695 177.586 174.211 1.00 0.00  ? 975 SER A CB  1 
ATOM 3650 O OG  . SER A 1 1032 ? 198.656 177.426 175.622 1.00 0.00  ? 975 SER A OG  1 
ATOM 3651 N N   . SER A 1 1033 ? 197.713 178.772 171.423 1.00 1.81  ? 976 SER A N   1 
ATOM 3652 C CA  . SER A 1 1033 ? 197.746 178.739 169.970 1.00 0.00  ? 976 SER A CA  1 
ATOM 3653 C C   . SER A 1 1033 ? 198.944 179.539 169.480 1.00 7.83  ? 976 SER A C   1 
ATOM 3654 O O   . SER A 1 1033 ? 199.516 180.359 170.208 1.00 7.27  ? 976 SER A O   1 
ATOM 3655 C CB  . SER A 1 1033 ? 196.448 179.279 169.363 1.00 0.00  ? 976 SER A CB  1 
ATOM 3656 O OG  . SER A 1 1033 ? 195.331 178.556 169.848 1.00 0.00  ? 976 SER A OG  1 
ATOM 3657 N N   . ASP A 1 1034 ? 199.320 179.279 168.230 1.00 0.00  ? 977 ASP A N   1 
ATOM 3658 C CA  . ASP A 1 1034 ? 200.494 179.877 167.605 1.00 0.00  ? 977 ASP A CA  1 
ATOM 3659 C C   . ASP A 1 1034 ? 200.041 181.029 166.715 1.00 16.72 ? 977 ASP A C   1 
ATOM 3660 O O   . ASP A 1 1034 ? 199.331 180.816 165.728 1.00 10.12 ? 977 ASP A O   1 
ATOM 3661 C CB  . ASP A 1 1034 ? 201.261 178.830 166.802 1.00 0.00  ? 977 ASP A CB  1 
ATOM 3662 C CG  . ASP A 1 1034 ? 202.693 179.230 166.540 1.00 0.00  ? 977 ASP A CG  1 
ATOM 3663 O OD1 . ASP A 1 1034 ? 202.972 180.442 166.466 1.00 6.24  ? 977 ASP A OD1 1 
ATOM 3664 O OD2 . ASP A 1 1034 ? 203.544 178.330 166.403 1.00 3.46  ? 977 ASP A OD2 1 
ATOM 3665 N N   . THR A 1 1035 ? 200.451 182.248 167.063 1.00 7.42  ? 978 THR A N   1 
ATOM 3666 C CA  . THR A 1 1035 ? 200.085 183.412 166.268 1.00 0.59  ? 978 THR A CA  1 
ATOM 3667 C C   . THR A 1 1035 ? 200.892 183.533 164.986 1.00 10.68 ? 978 THR A C   1 
ATOM 3668 O O   . THR A 1 1035 ? 200.402 184.119 164.016 1.00 10.40 ? 978 THR A O   1 
ATOM 3669 C CB  . THR A 1 1035 ? 200.264 184.696 167.078 1.00 2.46  ? 978 THR A CB  1 
ATOM 3670 O OG1 . THR A 1 1035 ? 201.626 184.802 167.507 1.00 5.80  ? 978 THR A OG1 1 
ATOM 3671 C CG2 . THR A 1 1035 ? 199.360 184.691 168.285 1.00 0.13  ? 978 THR A CG2 1 
ATOM 3672 N N   . SER A 1 1036 ? 202.114 183.008 164.956 1.00 1.26  ? 979 SER A N   1 
ATOM 3673 C CA  . SER A 1 1036 ? 202.985 183.245 163.811 1.00 4.02  ? 979 SER A CA  1 
ATOM 3674 C C   . SER A 1 1036 ? 202.590 182.375 162.621 1.00 9.71  ? 979 SER A C   1 
ATOM 3675 O O   . SER A 1 1036 ? 202.303 182.887 161.534 1.00 6.98  ? 979 SER A O   1 
ATOM 3676 C CB  . SER A 1 1036 ? 204.442 183.005 164.208 1.00 6.83  ? 979 SER A CB  1 
ATOM 3677 O OG  . SER A 1 1036 ? 205.323 183.611 163.282 1.00 4.90  ? 979 SER A OG  1 
ATOM 3678 N N   . PHE A 1 1037 ? 202.567 181.058 162.811 1.00 14.58 ? 980 PHE A N   1 
ATOM 3679 C CA  . PHE A 1 1037 ? 202.228 180.095 161.763 1.00 0.00  ? 980 PHE A CA  1 
ATOM 3680 C C   . PHE A 1 1037 ? 200.990 179.342 162.240 1.00 7.64  ? 980 PHE A C   1 
ATOM 3681 O O   . PHE A 1 1037 ? 201.094 178.270 162.841 1.00 1.31  ? 980 PHE A O   1 
ATOM 3682 C CB  . PHE A 1 1037 ? 203.389 179.134 161.471 1.00 0.00  ? 980 PHE A CB  1 
ATOM 3683 C CG  . PHE A 1 1037 ? 204.663 179.813 161.042 1.00 0.00  ? 980 PHE A CG  1 
ATOM 3684 C CD1 . PHE A 1 1037 ? 205.371 180.620 161.913 1.00 0.00  ? 980 PHE A CD1 1 
ATOM 3685 C CD2 . PHE A 1 1037 ? 205.157 179.633 159.766 1.00 0.00  ? 980 PHE A CD2 1 
ATOM 3686 C CE1 . PHE A 1 1037 ? 206.539 181.238 161.520 1.00 0.00  ? 980 PHE A CE1 1 
ATOM 3687 C CE2 . PHE A 1 1037 ? 206.326 180.248 159.370 1.00 4.16  ? 980 PHE A CE2 1 
ATOM 3688 C CZ  . PHE A 1 1037 ? 207.017 181.052 160.248 1.00 0.00  ? 980 PHE A CZ  1 
ATOM 3689 N N   . PHE A 1 1038 ? 199.806 179.893 161.958 1.00 2.69  ? 981 PHE A N   1 
ATOM 3690 C CA  . PHE A 1 1038 ? 198.551 179.186 162.329 1.00 0.00  ? 981 PHE A CA  1 
ATOM 3691 C C   . PHE A 1 1038 ? 197.990 178.461 161.099 1.00 7.36  ? 981 PHE A C   1 
ATOM 3692 O O   . PHE A 1 1038 ? 198.580 178.572 160.024 1.00 18.78 ? 981 PHE A O   1 
ATOM 3693 C CB  . PHE A 1 1038 ? 197.532 180.157 162.932 1.00 0.43  ? 981 PHE A CB  1 
ATOM 3694 C CG  . PHE A 1 1038 ? 197.351 181.446 162.172 1.00 0.99  ? 981 PHE A CG  1 
ATOM 3695 C CD1 . PHE A 1 1038 ? 196.612 181.484 161.001 1.00 5.59  ? 981 PHE A CD1 1 
ATOM 3696 C CD2 . PHE A 1 1038 ? 197.913 182.626 162.634 1.00 0.10  ? 981 PHE A CD2 1 
ATOM 3697 C CE1 . PHE A 1 1038 ? 196.445 182.671 160.306 1.00 0.00  ? 981 PHE A CE1 1 
ATOM 3698 C CE2 . PHE A 1 1038 ? 197.744 183.812 161.938 1.00 0.00  ? 981 PHE A CE2 1 
ATOM 3699 C CZ  . PHE A 1 1038 ? 197.009 183.832 160.776 1.00 0.00  ? 981 PHE A CZ  1 
ATOM 3700 O OXT . PHE A 1 1038 ? 196.958 177.791 161.248 1.00 7.50  ? 981 PHE A OXT 1 
ATOM 3701 N N   . ALA B 2 2    ? 214.807 189.107 149.805 1.00 24.31 ? 2   ALA B N   1 
ATOM 3702 C CA  . ALA B 2 2    ? 214.298 190.469 149.909 1.00 26.90 ? 2   ALA B CA  1 
ATOM 3703 C C   . ALA B 2 2    ? 213.046 190.647 149.060 1.00 27.10 ? 2   ALA B C   1 
ATOM 3704 O O   . ALA B 2 2    ? 212.919 190.048 147.993 1.00 29.24 ? 2   ALA B O   1 
ATOM 3705 C CB  . ALA B 2 2    ? 215.366 191.467 149.493 1.00 23.68 ? 2   ALA B CB  1 
ATOM 3706 N N   . CYS B 2 3    ? 212.121 191.473 149.541 1.00 23.70 ? 3   CYS B N   1 
ATOM 3707 C CA  . CYS B 2 3    ? 210.907 191.757 148.793 1.00 18.62 ? 3   CYS B CA  1 
ATOM 3708 C C   . CYS B 2 3    ? 211.228 192.530 147.521 1.00 19.78 ? 3   CYS B C   1 
ATOM 3709 O O   . CYS B 2 3    ? 212.175 193.318 147.467 1.00 25.34 ? 3   CYS B O   1 
ATOM 3710 C CB  . CYS B 2 3    ? 209.924 192.556 149.644 1.00 20.12 ? 3   CYS B CB  1 
ATOM 3711 S SG  . CYS B 2 3    ? 209.213 191.638 151.012 1.00 38.14 ? 3   CYS B SG  1 
ATOM 3712 N N   . SER B 2 4    ? 210.425 192.293 146.488 1.00 19.95 ? 4   SER B N   1 
ATOM 3713 C CA  . SER B 2 4    ? 210.581 193.001 145.228 1.00 18.89 ? 4   SER B CA  1 
ATOM 3714 C C   . SER B 2 4    ? 209.279 192.907 144.450 1.00 19.59 ? 4   SER B C   1 
ATOM 3715 O O   . SER B 2 4    ? 208.546 191.921 144.560 1.00 15.90 ? 4   SER B O   1 
ATOM 3716 C CB  . SER B 2 4    ? 211.740 192.432 144.402 1.00 18.73 ? 4   SER B CB  1 
ATOM 3717 O OG  . SER B 2 4    ? 211.485 191.092 144.022 1.00 20.38 ? 4   SER B OG  1 
ATOM 3718 N N   . ILE B 2 5    ? 209.007 193.959 143.646 1.00 19.50 ? 5   ILE B N   1 
ATOM 3719 C CA  . ILE B 2 5    ? 207.782 194.048 142.785 1.00 19.00 ? 5   ILE B CA  1 
ATOM 3720 C C   . ILE B 2 5    ? 208.239 194.050 141.331 1.00 14.62 ? 5   ILE B C   1 
ATOM 3721 O O   . ILE B 2 5    ? 209.079 194.887 141.008 1.00 17.16 ? 5   ILE B O   1 
ATOM 3722 C CB  . ILE B 2 5    ? 206.904 195.276 143.113 1.00 14.04 ? 5   ILE B CB  1 
ATOM 3723 C CG1 . ILE B 2 5    ? 207.592 196.626 142.918 1.00 13.78 ? 5   ILE B CG1 1 
ATOM 3724 C CG2 . ILE B 2 5    ? 206.340 195.174 144.517 1.00 14.79 ? 5   ILE B CG2 1 
ATOM 3725 C CD1 . ILE B 2 5    ? 206.638 197.790 143.040 1.00 13.94 ? 5   ILE B CD1 1 
ATOM 3726 N N   . VAL B 2 6    ? 207.689 193.161 140.499 1.00 13.89 ? 6   VAL B N   1 
ATOM 3727 C CA  . VAL B 2 6    ? 208.155 193.050 139.084 1.00 14.45 ? 6   VAL B CA  1 
ATOM 3728 C C   . VAL B 2 6    ? 207.004 193.399 138.135 1.00 9.34  ? 6   VAL B C   1 
ATOM 3729 O O   . VAL B 2 6    ? 205.860 192.990 138.419 1.00 15.22 ? 6   VAL B O   1 
ATOM 3730 C CB  . VAL B 2 6    ? 208.713 191.644 138.791 1.00 16.76 ? 6   VAL B CB  1 
ATOM 3731 C CG1 . VAL B 2 6    ? 209.078 191.480 137.324 1.00 15.03 ? 6   VAL B CG1 1 
ATOM 3732 C CG2 . VAL B 2 6    ? 209.904 191.315 139.678 1.00 14.11 ? 6   VAL B CG2 1 
ATOM 3733 N N   . GLN B 2 7    ? 207.298 194.134 137.056 1.00 13.50 ? 7   GLN B N   1 
ATOM 3734 C CA  . GLN B 2 7    ? 206.255 194.458 136.045 1.00 21.24 ? 7   GLN B CA  1 
ATOM 3735 C C   . GLN B 2 7    ? 205.939 193.196 135.238 1.00 19.00 ? 7   GLN B C   1 
ATOM 3736 O O   . GLN B 2 7    ? 206.866 192.396 135.009 1.00 19.34 ? 7   GLN B O   1 
ATOM 3737 C CB  . GLN B 2 7    ? 206.717 195.581 135.114 1.00 20.74 ? 7   GLN B CB  1 
ATOM 3738 C CG  . GLN B 2 7    ? 205.609 196.105 134.211 1.00 18.11 ? 7   GLN B CG  1 
ATOM 3739 C CD  . GLN B 2 7    ? 206.077 197.206 133.292 1.00 20.87 ? 7   GLN B CD  1 
ATOM 3740 O OE1 . GLN B 2 7    ? 206.974 197.978 133.624 1.00 21.52 ? 7   GLN B OE1 1 
ATOM 3741 N NE2 . GLN B 2 7    ? 205.465 197.287 132.122 1.00 20.43 ? 7   GLN B NE2 1 
ATOM 3742 N N   . PHE B 2 8    ? 204.681 193.035 134.821 1.00 14.01 ? 8   PHE B N   1 
ATOM 3743 C CA  . PHE B 2 8    ? 204.286 191.800 134.093 1.00 19.32 ? 8   PHE B CA  1 
ATOM 3744 C C   . PHE B 2 8    ? 203.337 192.142 132.937 1.00 23.98 ? 8   PHE B C   1 
ATOM 3745 O O   . PHE B 2 8    ? 203.128 191.260 132.080 1.00 21.67 ? 8   PHE B O   1 
ATOM 3746 C CB  . PHE B 2 8    ? 203.707 190.762 135.062 1.00 17.44 ? 8   PHE B CB  1 
ATOM 3747 C CG  . PHE B 2 8    ? 202.247 190.923 135.401 1.00 18.88 ? 8   PHE B CG  1 
ATOM 3748 C CD1 . PHE B 2 8    ? 201.262 190.384 134.588 1.00 15.38 ? 8   PHE B CD1 1 
ATOM 3749 C CD2 . PHE B 2 8    ? 201.857 191.589 136.551 1.00 15.89 ? 8   PHE B CD2 1 
ATOM 3750 C CE1 . PHE B 2 8    ? 199.921 190.528 134.904 1.00 17.45 ? 8   PHE B CE1 1 
ATOM 3751 C CE2 . PHE B 2 8    ? 200.516 191.730 136.868 1.00 15.44 ? 8   PHE B CE2 1 
ATOM 3752 C CZ  . PHE B 2 8    ? 199.551 191.198 136.045 1.00 16.04 ? 8   PHE B CZ  1 
ATOM 3753 N N   . CYS B 2 9    ? 202.793 193.364 132.894 1.00 27.05 ? 9   CYS B N   1 
ATOM 3754 C CA  . CYS B 2 9    ? 201.956 193.699 131.752 1.00 25.35 ? 9   CYS B CA  1 
ATOM 3755 C C   . CYS B 2 9    ? 202.054 195.183 131.439 1.00 21.82 ? 9   CYS B C   1 
ATOM 3756 O O   . CYS B 2 9    ? 202.204 196.014 132.336 1.00 22.13 ? 9   CYS B O   1 
ATOM 3757 C CB  . CYS B 2 9    ? 200.494 193.322 131.994 1.00 25.76 ? 9   CYS B CB  1 
ATOM 3758 S SG  . CYS B 2 9    ? 199.450 193.610 130.563 1.00 21.32 ? 9   CYS B SG  1 
ATOM 3759 N N   . TYR B 2 10   ? 201.934 195.504 130.152 1.00 18.12 ? 10  TYR B N   1 
ATOM 3760 C CA  . TYR B 2 10   ? 201.886 196.880 129.679 1.00 23.86 ? 10  TYR B CA  1 
ATOM 3761 C C   . TYR B 2 10   ? 200.623 197.076 128.856 1.00 25.71 ? 10  TYR B C   1 
ATOM 3762 O O   . TYR B 2 10   ? 200.355 196.301 127.934 1.00 24.75 ? 10  TYR B O   1 
ATOM 3763 C CB  . TYR B 2 10   ? 203.119 197.222 128.838 1.00 24.44 ? 10  TYR B CB  1 
ATOM 3764 C CG  . TYR B 2 10   ? 203.082 198.606 128.239 1.00 23.36 ? 10  TYR B CG  1 
ATOM 3765 C CD1 . TYR B 2 10   ? 203.352 199.726 129.013 1.00 25.03 ? 10  TYR B CD1 1 
ATOM 3766 C CD2 . TYR B 2 10   ? 202.770 198.794 126.900 1.00 23.65 ? 10  TYR B CD2 1 
ATOM 3767 C CE1 . TYR B 2 10   ? 203.316 200.995 128.470 1.00 24.05 ? 10  TYR B CE1 1 
ATOM 3768 C CE2 . TYR B 2 10   ? 202.733 200.059 126.348 1.00 27.15 ? 10  TYR B CE2 1 
ATOM 3769 C CZ  . TYR B 2 10   ? 203.006 201.154 127.137 1.00 26.42 ? 10  TYR B CZ  1 
ATOM 3770 O OH  . TYR B 2 10   ? 202.968 202.416 126.589 1.00 24.64 ? 10  TYR B OH  1 
ATOM 3771 N N   . PHE B 2 11   ? 199.850 198.107 129.191 1.00 20.86 ? 11  PHE B N   1 
ATOM 3772 C CA  . PHE B 2 11   ? 198.679 198.448 128.396 1.00 18.95 ? 11  PHE B CA  1 
ATOM 3773 C C   . PHE B 2 11   ? 199.116 198.983 127.039 1.00 21.44 ? 11  PHE B C   1 
ATOM 3774 O O   . PHE B 2 11   ? 200.026 199.815 126.954 1.00 25.09 ? 11  PHE B O   1 
ATOM 3775 C CB  . PHE B 2 11   ? 197.824 199.490 129.117 1.00 21.78 ? 11  PHE B CB  1 
ATOM 3776 C CG  . PHE B 2 11   ? 196.895 198.915 130.148 1.00 28.41 ? 11  PHE B CG  1 
ATOM 3777 C CD1 . PHE B 2 11   ? 195.921 197.999 129.790 1.00 19.81 ? 11  PHE B CD1 1 
ATOM 3778 C CD2 . PHE B 2 11   ? 196.984 199.305 131.473 1.00 22.82 ? 11  PHE B CD2 1 
ATOM 3779 C CE1 . PHE B 2 11   ? 195.063 197.473 130.737 1.00 16.41 ? 11  PHE B CE1 1 
ATOM 3780 C CE2 . PHE B 2 11   ? 196.127 198.784 132.423 1.00 16.37 ? 11  PHE B CE2 1 
ATOM 3781 C CZ  . PHE B 2 11   ? 195.166 197.867 132.053 1.00 20.67 ? 11  PHE B CZ  1 
ATOM 3782 N N   . GLN B 2 12   ? 198.479 198.496 125.974 1.00 21.22 ? 12  GLN B N   1 
ATOM 3783 C CA  . GLN B 2 12   ? 198.755 199.039 124.648 1.00 20.41 ? 12  GLN B CA  1 
ATOM 3784 C C   . GLN B 2 12   ? 198.277 200.481 124.543 1.00 20.08 ? 12  GLN B C   1 
ATOM 3785 O O   . GLN B 2 12   ? 199.033 201.368 124.131 1.00 19.00 ? 12  GLN B O   1 
ATOM 3786 C CB  . GLN B 2 12   ? 198.093 198.175 123.576 1.00 23.03 ? 12  GLN B CB  1 
ATOM 3787 C CG  . GLN B 2 12   ? 198.369 198.638 122.156 1.00 21.85 ? 12  GLN B CG  1 
ATOM 3788 C CD  . GLN B 2 12   ? 197.365 198.094 121.162 1.00 22.80 ? 12  GLN B CD  1 
ATOM 3789 O OE1 . GLN B 2 12   ? 196.190 197.918 121.484 1.00 19.85 ? 12  GLN B OE1 1 
ATOM 3790 N NE2 . GLN B 2 12   ? 197.822 197.823 119.945 1.00 24.24 ? 12  GLN B NE2 1 
ATOM 3791 N N   . ASP B 2 13   ? 197.028 200.732 124.927 1.00 24.77 ? 13  ASP B N   1 
ATOM 3792 C CA  . ASP B 2 13   ? 196.460 202.078 124.894 1.00 25.18 ? 13  ASP B CA  1 
ATOM 3793 C C   . ASP B 2 13   ? 195.329 202.142 125.906 1.00 28.57 ? 13  ASP B C   1 
ATOM 3794 O O   . ASP B 2 13   ? 194.339 201.415 125.772 1.00 30.16 ? 13  ASP B O   1 
ATOM 3795 C CB  . ASP B 2 13   ? 195.951 202.428 123.496 1.00 23.61 ? 13  ASP B CB  1 
ATOM 3796 C CG  . ASP B 2 13   ? 197.041 202.961 122.593 1.00 25.80 ? 13  ASP B CG  1 
ATOM 3797 O OD1 . ASP B 2 13   ? 197.304 204.181 122.634 1.00 26.45 ? 13  ASP B OD1 1 
ATOM 3798 O OD2 . ASP B 2 13   ? 197.633 202.161 121.840 1.00 26.21 ? 13  ASP B OD2 1 
ATOM 3799 N N   . LEU B 2 14   ? 195.458 203.051 126.877 1.00 22.90 ? 14  LEU B N   1 
ATOM 3800 C CA  . LEU B 2 14   ? 194.387 203.240 127.890 1.00 21.67 ? 14  LEU B CA  1 
ATOM 3801 C C   . LEU B 2 14   ? 193.762 204.628 127.707 1.00 22.53 ? 14  LEU B C   1 
ATOM 3802 O O   . LEU B 2 14   ? 192.623 204.826 128.173 1.00 21.14 ? 14  LEU B O   1 
ATOM 3803 C CB  . LEU B 2 14   ? 194.992 203.088 129.288 1.00 12.63 ? 14  LEU B CB  1 
ATOM 3804 C CG  . LEU B 2 14   ? 194.084 202.431 130.326 1.00 21.49 ? 14  LEU B CG  1 
ATOM 3805 C CD1 . LEU B 2 14   ? 193.555 201.099 129.817 1.00 24.81 ? 14  LEU B CD1 1 
ATOM 3806 C CD2 . LEU B 2 14   ? 194.815 202.246 131.646 1.00 20.69 ? 14  LEU B CD2 1 
ATOM 3807 N N   . GLN B 2 15   ? 194.480 205.550 127.053 1.00 19.60 ? 15  GLN B N   1 
ATOM 3808 C CA  . GLN B 2 15   ? 193.915 206.901 126.795 1.00 13.75 ? 15  GLN B CA  1 
ATOM 3809 C C   . GLN B 2 15   ? 192.613 206.740 126.001 1.00 16.01 ? 15  GLN B C   1 
ATOM 3810 O O   . GLN B 2 15   ? 191.697 207.555 126.211 1.00 21.36 ? 15  GLN B O   1 
ATOM 3811 C CB  . GLN B 2 15   ? 194.936 207.794 126.083 1.00 16.61 ? 15  GLN B CB  1 
ATOM 3812 C CG  . GLN B 2 15   ? 194.964 207.626 124.572 1.00 19.03 ? 15  GLN B CG  1 
ATOM 3813 C CD  . GLN B 2 15   ? 195.552 206.298 124.164 1.00 21.75 ? 15  GLN B CD  1 
ATOM 3814 O OE1 . GLN B 2 15   ? 196.354 205.706 124.883 1.00 20.12 ? 15  GLN B OE1 1 
ATOM 3815 N NE2 . GLN B 2 15   ? 195.146 205.815 123.001 1.00 19.37 ? 15  GLN B NE2 1 
ATOM 3816 N N   . ALA B 2 16   ? 192.529 205.713 125.147 1.00 15.68 ? 16  ALA B N   1 
ATOM 3817 C CA  . ALA B 2 16   ? 191.296 205.475 124.403 1.00 18.30 ? 16  ALA B CA  1 
ATOM 3818 C C   . ALA B 2 16   ? 190.145 205.130 125.339 1.00 17.90 ? 16  ALA B C   1 
ATOM 3819 O O   . ALA B 2 16   ? 189.026 205.629 125.167 1.00 14.48 ? 16  ALA B O   1 
ATOM 3820 C CB  . ALA B 2 16   ? 191.508 204.362 123.378 1.00 19.35 ? 16  ALA B CB  1 
ATOM 3821 N N   . ALA B 2 17   ? 190.400 204.279 126.336 1.00 14.97 ? 17  ALA B N   1 
ATOM 3822 C CA  . ALA B 2 17   ? 189.369 203.956 127.316 1.00 11.85 ? 17  ALA B CA  1 
ATOM 3823 C C   . ALA B 2 17   ? 188.986 205.181 128.135 1.00 13.39 ? 17  ALA B C   1 
ATOM 3824 O O   . ALA B 2 17   ? 187.802 205.404 128.420 1.00 19.51 ? 17  ALA B O   1 
ATOM 3825 C CB  . ALA B 2 17   ? 189.844 202.825 128.227 1.00 8.80  ? 17  ALA B CB  1 
ATOM 3826 N N   . ARG B 2 18   ? 189.975 205.991 128.520 1.00 10.72 ? 18  ARG B N   1 
ATOM 3827 C CA  . ARG B 2 18   ? 189.671 207.222 129.243 1.00 12.65 ? 18  ARG B CA  1 
ATOM 3828 C C   . ARG B 2 18   ? 188.795 208.146 128.404 1.00 10.84 ? 18  ARG B C   1 
ATOM 3829 O O   . ARG B 2 18   ? 187.811 208.709 128.899 1.00 1.75  ? 18  ARG B O   1 
ATOM 3830 C CB  . ARG B 2 18   ? 190.965 207.931 129.646 1.00 18.25 ? 18  ARG B CB  1 
ATOM 3831 C CG  . ARG B 2 18   ? 190.756 209.323 130.226 1.00 15.84 ? 18  ARG B CG  1 
ATOM 3832 C CD  . ARG B 2 18   ? 192.054 210.113 130.268 1.00 14.79 ? 18  ARG B CD  1 
ATOM 3833 N NE  . ARG B 2 18   ? 192.545 210.444 128.936 1.00 18.11 ? 18  ARG B NE  1 
ATOM 3834 C CZ  . ARG B 2 18   ? 193.633 211.164 128.697 1.00 17.17 ? 18  ARG B CZ  1 
ATOM 3835 N NH1 . ARG B 2 18   ? 194.382 211.633 129.681 1.00 5.91  ? 18  ARG B NH1 1 
ATOM 3836 N NH2 . ARG B 2 18   ? 193.977 211.422 127.438 1.00 19.57 ? 18  ARG B NH2 1 
ATOM 3837 N N   . ASP B 2 19   ? 189.133 208.302 127.121 1.00 18.22 ? 19  ASP B N   1 
ATOM 3838 C CA  . ASP B 2 19   ? 188.383 209.200 126.250 1.00 19.27 ? 19  ASP B CA  1 
ATOM 3839 C C   . ASP B 2 19   ? 186.969 208.691 126.008 1.00 15.57 ? 19  ASP B C   1 
ATOM 3840 O O   . ASP B 2 19   ? 186.024 209.485 125.937 1.00 17.98 ? 19  ASP B O   1 
ATOM 3841 C CB  . ASP B 2 19   ? 189.126 209.384 124.930 1.00 13.94 ? 19  ASP B CB  1 
ATOM 3842 C CG  . ASP B 2 19   ? 190.449 210.099 125.106 1.00 16.97 ? 19  ASP B CG  1 
ATOM 3843 O OD1 . ASP B 2 19   ? 190.694 210.631 126.208 1.00 14.18 ? 19  ASP B OD1 1 
ATOM 3844 O OD2 . ASP B 2 19   ? 191.245 210.128 124.146 1.00 15.86 ? 19  ASP B OD2 1 
ATOM 3845 N N   . PHE B 2 20   ? 186.817 207.368 125.909 1.00 12.81 ? 20  PHE B N   1 
ATOM 3846 C CA  . PHE B 2 20   ? 185.468 206.775 125.711 1.00 13.06 ? 20  PHE B CA  1 
ATOM 3847 C C   . PHE B 2 20   ? 184.624 206.993 126.970 1.00 13.04 ? 20  PHE B C   1 
ATOM 3848 O O   . PHE B 2 20   ? 183.449 207.390 126.839 1.00 7.20  ? 20  PHE B O   1 
ATOM 3849 C CB  . PHE B 2 20   ? 185.569 205.284 125.380 1.00 5.77  ? 20  PHE B CB  1 
ATOM 3850 C CG  . PHE B 2 20   ? 184.250 204.554 125.386 1.00 9.52  ? 20  PHE B CG  1 
ATOM 3851 C CD1 . PHE B 2 20   ? 183.281 204.827 124.435 1.00 12.50 ? 20  PHE B CD1 1 
ATOM 3852 C CD2 . PHE B 2 20   ? 183.972 203.596 126.348 1.00 13.73 ? 20  PHE B CD2 1 
ATOM 3853 C CE1 . PHE B 2 20   ? 182.067 204.157 124.444 1.00 12.99 ? 20  PHE B CE1 1 
ATOM 3854 C CE2 . PHE B 2 20   ? 182.758 202.927 126.357 1.00 10.94 ? 20  PHE B CE2 1 
ATOM 3855 C CZ  . PHE B 2 20   ? 181.808 203.209 125.405 1.00 8.51  ? 20  PHE B CZ  1 
ATOM 3856 N N   . LEU B 2 21   ? 185.202 206.746 128.149 1.00 17.43 ? 21  LEU B N   1 
ATOM 3857 C CA  . LEU B 2 21   ? 184.445 206.865 129.388 1.00 8.83  ? 21  LEU B CA  1 
ATOM 3858 C C   . LEU B 2 21   ? 184.368 208.296 129.906 1.00 10.75 ? 21  LEU B C   1 
ATOM 3859 O O   . LEU B 2 21   ? 183.465 208.605 130.691 1.00 6.02  ? 21  LEU B O   1 
ATOM 3860 C CB  . LEU B 2 21   ? 185.047 205.953 130.456 1.00 3.88  ? 21  LEU B CB  1 
ATOM 3861 C CG  . LEU B 2 21   ? 185.101 204.467 130.105 1.00 0.00  ? 21  LEU B CG  1 
ATOM 3862 C CD1 . LEU B 2 21   ? 185.795 203.691 131.199 1.00 7.23  ? 21  LEU B CD1 1 
ATOM 3863 C CD2 . LEU B 2 21   ? 183.711 203.936 129.874 1.00 0.00  ? 21  LEU B CD2 1 
ATOM 3864 N N   . PHE B 2 22   ? 185.281 209.174 129.487 1.00 16.53 ? 22  PHE B N   1 
ATOM 3865 C CA  . PHE B 2 22   ? 185.240 210.598 129.827 1.00 20.49 ? 22  PHE B CA  1 
ATOM 3866 C C   . PHE B 2 22   ? 185.316 211.405 128.539 1.00 23.31 ? 22  PHE B C   1 
ATOM 3867 O O   . PHE B 2 22   ? 186.397 211.862 128.141 1.00 20.46 ? 22  PHE B O   1 
ATOM 3868 C CB  . PHE B 2 22   ? 186.373 210.995 130.777 1.00 16.85 ? 22  PHE B CB  1 
ATOM 3869 C CG  . PHE B 2 22   ? 186.031 210.845 132.232 1.00 16.74 ? 22  PHE B CG  1 
ATOM 3870 C CD1 . PHE B 2 22   ? 184.732 211.018 132.673 1.00 15.57 ? 22  PHE B CD1 1 
ATOM 3871 C CD2 . PHE B 2 22   ? 187.020 210.580 133.164 1.00 18.95 ? 22  PHE B CD2 1 
ATOM 3872 C CE1 . PHE B 2 22   ? 184.419 210.890 134.011 1.00 20.59 ? 22  PHE B CE1 1 
ATOM 3873 C CE2 . PHE B 2 22   ? 186.714 210.446 134.502 1.00 15.72 ? 22  PHE B CE2 1 
ATOM 3874 C CZ  . PHE B 2 22   ? 185.412 210.606 134.927 1.00 18.99 ? 22  PHE B CZ  1 
ATOM 3875 N N   . PRO B 2 23   ? 184.186 211.595 127.855 1.00 23.29 ? 23  PRO B N   1 
ATOM 3876 C CA  . PRO B 2 23   ? 184.215 212.370 126.604 1.00 20.37 ? 23  PRO B CA  1 
ATOM 3877 C C   . PRO B 2 23   ? 184.686 213.800 126.791 1.00 23.84 ? 23  PRO B C   1 
ATOM 3878 O O   . PRO B 2 23   ? 185.359 214.340 125.905 1.00 25.97 ? 23  PRO B O   1 
ATOM 3879 C CB  . PRO B 2 23   ? 182.758 212.316 126.118 1.00 19.57 ? 23  PRO B CB  1 
ATOM 3880 C CG  . PRO B 2 23   ? 182.097 211.243 126.925 1.00 21.86 ? 23  PRO B CG  1 
ATOM 3881 C CD  . PRO B 2 23   ? 182.823 211.182 128.224 1.00 21.59 ? 23  PRO B CD  1 
ATOM 3882 N N   . HIS B 2 24   ? 184.360 214.429 127.923 1.00 22.56 ? 24  HIS B N   1 
ATOM 3883 C CA  . HIS B 2 24   ? 184.746 215.821 128.129 1.00 24.59 ? 24  HIS B CA  1 
ATOM 3884 C C   . HIS B 2 24   ? 186.250 215.970 128.318 1.00 27.98 ? 24  HIS B C   1 
ATOM 3885 O O   . HIS B 2 24   ? 186.804 217.038 128.035 1.00 28.41 ? 24  HIS B O   1 
ATOM 3886 C CB  . HIS B 2 24   ? 184.001 216.406 129.329 1.00 24.20 ? 24  HIS B CB  1 
ATOM 3887 C CG  . HIS B 2 24   ? 184.132 215.594 130.580 1.00 25.95 ? 24  HIS B CG  1 
ATOM 3888 N ND1 . HIS B 2 24   ? 183.231 214.611 130.926 1.00 26.97 ? 24  HIS B ND1 1 
ATOM 3889 C CD2 . HIS B 2 24   ? 185.056 215.623 131.569 1.00 27.66 ? 24  HIS B CD2 1 
ATOM 3890 C CE1 . HIS B 2 24   ? 183.594 214.069 132.075 1.00 27.09 ? 24  HIS B CE1 1 
ATOM 3891 N NE2 . HIS B 2 24   ? 184.699 214.664 132.485 1.00 27.50 ? 24  HIS B NE2 1 
ATOM 3892 N N   . LEU B 2 25   ? 186.922 214.922 128.798 1.00 26.27 ? 25  LEU B N   1 
ATOM 3893 C CA  . LEU B 2 25   ? 188.368 214.994 128.980 1.00 26.41 ? 25  LEU B CA  1 
ATOM 3894 C C   . LEU B 2 25   ? 189.089 215.145 127.647 1.00 26.55 ? 25  LEU B C   1 
ATOM 3895 O O   . LEU B 2 25   ? 190.060 215.903 127.542 1.00 21.39 ? 25  LEU B O   1 
ATOM 3896 C CB  . LEU B 2 25   ? 188.865 213.756 129.724 1.00 25.33 ? 25  LEU B CB  1 
ATOM 3897 C CG  . LEU B 2 25   ? 188.830 213.819 131.252 1.00 22.74 ? 25  LEU B CG  1 
ATOM 3898 C CD1 . LEU B 2 25   ? 189.687 212.714 131.845 1.00 25.82 ? 25  LEU B CD1 1 
ATOM 3899 C CD2 . LEU B 2 25   ? 189.285 215.183 131.751 1.00 22.52 ? 25  LEU B CD2 1 
ATOM 3900 N N   . ARG B 2 26   ? 188.634 214.432 126.621 1.00 24.26 ? 26  ARG B N   1 
ATOM 3901 C CA  . ARG B 2 26   ? 189.269 214.488 125.308 1.00 24.17 ? 26  ARG B CA  1 
ATOM 3902 C C   . ARG B 2 26   ? 189.049 215.843 124.647 1.00 26.31 ? 26  ARG B C   1 
ATOM 3903 O O   . ARG B 2 26   ? 189.998 216.484 124.196 1.00 30.72 ? 26  ARG B O   1 
ATOM 3904 C CB  . ARG B 2 26   ? 188.739 213.371 124.405 1.00 23.83 ? 26  ARG B CB  1 
ATOM 3905 C CG  . ARG B 2 26   ? 188.864 213.667 122.918 1.00 26.83 ? 26  ARG B CG  1 
ATOM 3906 C CD  . ARG B 2 26   ? 188.039 212.702 122.077 1.00 30.34 ? 26  ARG B CD  1 
ATOM 3907 N NE  . ARG B 2 26   ? 186.615 212.767 122.386 1.00 30.04 ? 26  ARG B NE  1 
ATOM 3908 C CZ  . ARG B 2 26   ? 185.905 211.755 122.864 1.00 29.78 ? 26  ARG B CZ  1 
ATOM 3909 N NH1 . ARG B 2 26   ? 186.454 210.575 123.098 1.00 25.25 ? 26  ARG B NH1 1 
ATOM 3910 N NH2 . ARG B 2 26   ? 184.610 211.930 123.112 1.00 31.13 ? 26  ARG B NH2 1 
ATOM 3911 N N   . GLU B 2 61   ? 197.963 223.640 121.726 1.00 32.05 ? 61  GLU B N   1 
ATOM 3912 C CA  . GLU B 2 61   ? 198.415 224.947 121.266 1.00 33.40 ? 61  GLU B CA  1 
ATOM 3913 C C   . GLU B 2 61   ? 197.999 226.040 122.243 1.00 35.79 ? 61  GLU B C   1 
ATOM 3914 O O   . GLU B 2 61   ? 196.819 226.186 122.556 1.00 36.76 ? 61  GLU B O   1 
ATOM 3915 C CB  . GLU B 2 61   ? 197.859 225.248 119.874 1.00 31.27 ? 61  GLU B CB  1 
ATOM 3916 C CG  . GLU B 2 61   ? 197.755 224.032 118.971 1.00 30.35 ? 61  GLU B CG  1 
ATOM 3917 C CD  . GLU B 2 61   ? 197.097 224.348 117.644 1.00 34.48 ? 61  GLU B CD  1 
ATOM 3918 O OE1 . GLU B 2 61   ? 196.205 225.221 117.615 1.00 36.53 ? 61  GLU B OE1 1 
ATOM 3919 O OE2 . GLU B 2 61   ? 197.470 223.723 116.630 1.00 35.91 ? 61  GLU B OE2 1 
ATOM 3920 N N   . GLU B 2 62   ? 198.999 226.755 122.765 1.00 31.82 ? 62  GLU B N   1 
ATOM 3921 C CA  . GLU B 2 62   ? 198.735 227.834 123.751 1.00 29.29 ? 62  GLU B CA  1 
ATOM 3922 C C   . GLU B 2 62   ? 199.904 228.819 123.701 1.00 28.07 ? 62  GLU B C   1 
ATOM 3923 O O   . GLU B 2 62   ? 200.995 228.419 123.248 1.00 28.87 ? 62  GLU B O   1 
ATOM 3924 C CB  . GLU B 2 62   ? 198.589 227.251 125.156 1.00 28.09 ? 62  GLU B CB  1 
ATOM 3925 C CG  . GLU B 2 62   ? 197.356 226.384 125.328 1.00 30.95 ? 62  GLU B CG  1 
ATOM 3926 C CD  . GLU B 2 62   ? 197.232 225.738 126.696 1.00 32.15 ? 62  GLU B CD  1 
ATOM 3927 O OE1 . GLU B 2 62   ? 198.207 225.806 127.471 1.00 28.50 ? 62  GLU B OE1 1 
ATOM 3928 O OE2 . GLU B 2 62   ? 196.160 225.171 126.986 1.00 31.16 ? 62  GLU B OE2 1 
ATOM 3929 N N   . GLU B 2 63   ? 199.682 230.053 124.152 1.00 27.21 ? 63  GLU B N   1 
ATOM 3930 C CA  . GLU B 2 63   ? 200.745 231.094 124.127 1.00 26.94 ? 63  GLU B CA  1 
ATOM 3931 C C   . GLU B 2 63   ? 201.620 230.950 125.375 1.00 24.40 ? 63  GLU B C   1 
ATOM 3932 O O   . GLU B 2 63   ? 201.899 231.979 126.021 1.00 24.84 ? 63  GLU B O   1 
ATOM 3933 C CB  . GLU B 2 63   ? 200.118 232.488 124.051 1.00 26.92 ? 63  GLU B CB  1 
ATOM 3934 C CG  . GLU B 2 63   ? 198.878 232.544 123.178 1.00 26.38 ? 63  GLU B CG  1 
ATOM 3935 C CD  . GLU B 2 63   ? 199.095 232.099 121.742 1.00 26.97 ? 63  GLU B CD  1 
ATOM 3936 O OE1 . GLU B 2 63   ? 199.828 232.796 121.014 1.00 29.19 ? 63  GLU B OE1 1 
ATOM 3937 O OE2 . GLU B 2 63   ? 198.532 231.055 121.357 1.00 24.39 ? 63  GLU B OE2 1 
ATOM 3938 N N   . GLY B 2 64   ? 202.029 229.720 125.697 1.00 23.52 ? 64  GLY B N   1 
ATOM 3939 C CA  . GLY B 2 64   ? 202.905 229.489 126.861 1.00 25.46 ? 64  GLY B CA  1 
ATOM 3940 C C   . GLY B 2 64   ? 202.146 229.570 128.174 1.00 26.93 ? 64  GLY B C   1 
ATOM 3941 O O   . GLY B 2 64   ? 202.803 229.756 129.217 1.00 29.54 ? 64  GLY B O   1 
ATOM 3942 N N   . ASN B 2 65   ? 200.815 229.437 128.136 1.00 25.09 ? 65  ASN B N   1 
ATOM 3943 C CA  . ASN B 2 65   ? 200.024 229.415 129.398 1.00 25.67 ? 65  ASN B CA  1 
ATOM 3944 C C   . ASN B 2 65   ? 200.595 228.305 130.285 1.00 24.90 ? 65  ASN B C   1 
ATOM 3945 O O   . ASN B 2 65   ? 201.013 227.269 129.730 1.00 24.89 ? 65  ASN B O   1 
ATOM 3946 C CB  . ASN B 2 65   ? 198.522 229.276 129.139 1.00 27.41 ? 65  ASN B CB  1 
ATOM 3947 C CG  . ASN B 2 65   ? 197.900 230.521 128.543 1.00 27.11 ? 65  ASN B CG  1 
ATOM 3948 O OD1 . ASN B 2 65   ? 198.429 231.621 128.689 1.00 25.39 ? 65  ASN B OD1 1 
ATOM 3949 N ND2 . ASN B 2 65   ? 196.773 230.359 127.869 1.00 28.02 ? 65  ASN B ND2 1 
ATOM 3950 N N   . THR B 2 66   ? 200.613 228.520 131.604 1.00 26.63 ? 66  THR B N   1 
ATOM 3951 C CA  . THR B 2 66   ? 201.176 227.515 132.545 1.00 29.07 ? 66  THR B CA  1 
ATOM 3952 C C   . THR B 2 66   ? 200.185 226.355 132.701 1.00 26.58 ? 66  THR B C   1 
ATOM 3953 O O   . THR B 2 66   ? 199.251 226.483 133.517 1.00 27.63 ? 66  THR B O   1 
ATOM 3954 C CB  . THR B 2 66   ? 201.531 228.162 133.890 1.00 31.18 ? 66  THR B CB  1 
ATOM 3955 O OG1 . THR B 2 66   ? 202.519 229.168 133.661 1.00 30.79 ? 66  THR B OG1 1 
ATOM 3956 C CG2 . THR B 2 66   ? 202.043 227.164 134.906 1.00 26.69 ? 66  THR B CG2 1 
ATOM 3957 N N   . CYS B 2 67   ? 200.383 225.273 131.942 1.00 28.89 ? 67  CYS B N   1 
ATOM 3958 C CA  . CYS B 2 67   ? 199.496 224.083 132.048 1.00 29.94 ? 67  CYS B CA  1 
ATOM 3959 C C   . CYS B 2 67   ? 200.172 223.034 132.937 1.00 31.76 ? 67  CYS B C   1 
ATOM 3960 O O   . CYS B 2 67   ? 201.185 222.456 132.496 1.00 33.32 ? 67  CYS B O   1 
ATOM 3961 C CB  . CYS B 2 67   ? 199.217 223.493 130.671 1.00 30.22 ? 67  CYS B CB  1 
ATOM 3962 S SG  . CYS B 2 67   ? 200.719 223.086 129.744 1.00 41.80 ? 67  CYS B SG  1 
ATOM 3963 N N   . LYS B 2 68   ? 199.631 222.802 134.137 1.00 34.33 ? 68  LYS B N   1 
ATOM 3964 C CA  . LYS B 2 68   ? 200.252 221.842 135.090 1.00 33.86 ? 68  LYS B CA  1 
ATOM 3965 C C   . LYS B 2 68   ? 199.159 221.195 135.947 1.00 34.28 ? 68  LYS B C   1 
ATOM 3966 O O   . LYS B 2 68   ? 197.995 221.180 135.500 1.00 31.91 ? 68  LYS B O   1 
ATOM 3967 C CB  . LYS B 2 68   ? 201.281 222.554 135.974 1.00 30.43 ? 68  LYS B CB  1 
ATOM 3968 C CG  . LYS B 2 68   ? 202.487 223.128 135.241 1.00 30.89 ? 68  LYS B CG  1 
ATOM 3969 C CD  . LYS B 2 68   ? 203.402 222.069 134.664 1.00 30.93 ? 68  LYS B CD  1 
ATOM 3970 C CE  . LYS B 2 68   ? 204.646 222.646 134.022 1.00 31.48 ? 68  LYS B CE  1 
ATOM 3971 N NZ  . LYS B 2 68   ? 204.334 223.350 132.756 1.00 31.45 ? 68  LYS B NZ  1 
ATOM 3972 N N   . THR B 2 69   ? 199.527 220.683 137.126 1.00 35.00 ? 69  THR B N   1 
ATOM 3973 C CA  . THR B 2 69   ? 198.548 220.021 138.032 1.00 36.02 ? 69  THR B CA  1 
ATOM 3974 C C   . THR B 2 69   ? 197.807 218.923 137.261 1.00 35.94 ? 69  THR B C   1 
ATOM 3975 O O   . THR B 2 69   ? 196.561 218.902 137.314 1.00 32.92 ? 69  THR B O   1 
ATOM 3976 C CB  . THR B 2 69   ? 197.588 221.039 138.664 1.00 36.06 ? 69  THR B CB  1 
ATOM 3977 O OG1 . THR B 2 69   ? 196.894 221.718 137.617 1.00 33.93 ? 69  THR B OG1 1 
ATOM 3978 C CG2 . THR B 2 69   ? 198.297 222.050 139.537 1.00 34.04 ? 69  THR B CG2 1 
ATOM 3979 N N   . GLN B 2 70   ? 198.548 218.053 136.569 1.00 36.00 ? 70  GLN B N   1 
ATOM 3980 C CA  . GLN B 2 70   ? 197.924 216.931 135.818 1.00 33.44 ? 70  GLN B CA  1 
ATOM 3981 C C   . GLN B 2 70   ? 198.047 215.651 136.649 1.00 33.32 ? 70  GLN B C   1 
ATOM 3982 O O   . GLN B 2 70   ? 199.190 215.241 136.930 1.00 33.08 ? 70  GLN B O   1 
ATOM 3983 C CB  . GLN B 2 70   ? 198.589 216.773 134.449 1.00 34.07 ? 70  GLN B CB  1 
ATOM 3984 C CG  . GLN B 2 70   ? 198.354 217.954 133.518 1.00 33.88 ? 70  GLN B CG  1 
ATOM 3985 C CD  . GLN B 2 70   ? 196.889 218.182 133.237 1.00 33.81 ? 70  GLN B CD  1 
ATOM 3986 O OE1 . GLN B 2 70   ? 196.117 217.243 133.055 1.00 34.31 ? 70  GLN B OE1 1 
ATOM 3987 N NE2 . GLN B 2 70   ? 196.492 219.443 133.200 1.00 33.22 ? 70  GLN B NE2 1 
ATOM 3988 N N   . LYS B 2 71   ? 196.913 215.071 137.053 1.00 33.40 ? 71  LYS B N   1 
ATOM 3989 C CA  . LYS B 2 71   ? 196.928 213.851 137.905 1.00 30.92 ? 71  LYS B CA  1 
ATOM 3990 C C   . LYS B 2 71   ? 195.892 212.858 137.371 1.00 31.39 ? 71  LYS B C   1 
ATOM 3991 O O   . LYS B 2 71   ? 195.111 213.244 136.478 1.00 33.16 ? 71  LYS B O   1 
ATOM 3992 C CB  . LYS B 2 71   ? 196.627 214.220 139.360 1.00 27.09 ? 71  LYS B CB  1 
ATOM 3993 C CG  . LYS B 2 71   ? 197.690 215.060 140.056 1.00 30.84 ? 71  LYS B CG  1 
ATOM 3994 C CD  . LYS B 2 71   ? 197.335 215.419 141.484 1.00 34.09 ? 71  LYS B CD  1 
ATOM 3995 C CE  . LYS B 2 71   ? 198.408 216.233 142.175 1.00 33.77 ? 71  LYS B CE  1 
ATOM 3996 N NZ  . LYS B 2 71   ? 198.021 216.587 143.561 1.00 30.65 ? 71  LYS B NZ  1 
ATOM 3997 N N   . THR B 2 72   ? 195.887 211.632 137.901 1.00 20.33 ? 72  THR B N   1 
ATOM 3998 C CA  . THR B 2 72   ? 194.894 210.615 137.464 1.00 20.34 ? 72  THR B CA  1 
ATOM 3999 C C   . THR B 2 72   ? 193.952 210.276 138.622 1.00 20.00 ? 72  THR B C   1 
ATOM 4000 O O   . THR B 2 72   ? 194.432 209.738 139.636 1.00 22.32 ? 72  THR B O   1 
ATOM 4001 C CB  . THR B 2 72   ? 195.578 209.348 136.937 1.00 23.05 ? 72  THR B CB  1 
ATOM 4002 O OG1 . THR B 2 72   ? 196.172 209.657 135.676 1.00 20.60 ? 72  THR B OG1 1 
ATOM 4003 C CG2 . THR B 2 72   ? 194.616 208.191 136.782 1.00 18.73 ? 72  THR B CG2 1 
ATOM 4004 N N   . SER B 2 73   ? 192.661 210.578 138.471 1.00 14.32 ? 73  SER B N   1 
ATOM 4005 C CA  . SER B 2 73   ? 191.669 210.212 139.513 1.00 17.45 ? 73  SER B CA  1 
ATOM 4006 C C   . SER B 2 73   ? 190.594 209.326 138.878 1.00 10.48 ? 73  SER B C   1 
ATOM 4007 O O   . SER B 2 73   ? 189.813 208.711 139.629 1.00 9.47  ? 73  SER B O   1 
ATOM 4008 C CB  . SER B 2 73   ? 191.069 211.438 140.147 1.00 17.03 ? 73  SER B CB  1 
ATOM 4009 O OG  . SER B 2 73   ? 190.330 212.190 139.196 1.00 22.90 ? 73  SER B OG  1 
ATOM 4010 N N   . TRP B 2 74   ? 190.571 209.263 137.543 1.00 1.87  ? 74  TRP B N   1 
ATOM 4011 C CA  . TRP B 2 74   ? 189.513 208.484 136.850 1.00 8.74  ? 74  TRP B CA  1 
ATOM 4012 C C   . TRP B 2 74   ? 189.664 206.989 137.155 1.00 14.44 ? 74  TRP B C   1 
ATOM 4013 O O   . TRP B 2 74   ? 188.636 206.281 137.122 1.00 20.70 ? 74  TRP B O   1 
ATOM 4014 C CB  . TRP B 2 74   ? 189.520 208.766 135.339 1.00 13.01 ? 74  TRP B CB  1 
ATOM 4015 C CG  . TRP B 2 74   ? 190.768 208.349 134.607 1.00 14.93 ? 74  TRP B CG  1 
ATOM 4016 C CD1 . TRP B 2 74   ? 191.968 208.998 134.584 1.00 18.44 ? 74  TRP B CD1 1 
ATOM 4017 C CD2 . TRP B 2 74   ? 190.922 207.192 133.757 1.00 7.37  ? 74  TRP B CD2 1 
ATOM 4018 N NE1 . TRP B 2 74   ? 192.859 208.323 133.792 1.00 12.76 ? 74  TRP B NE1 1 
ATOM 4019 C CE2 . TRP B 2 74   ? 192.247 207.213 133.272 1.00 11.65 ? 74  TRP B CE2 1 
ATOM 4020 C CE3 . TRP B 2 74   ? 190.078 206.148 133.367 1.00 3.85  ? 74  TRP B CE3 1 
ATOM 4021 C CZ2 . TRP B 2 74   ? 192.741 206.229 132.418 1.00 13.33 ? 74  TRP B CZ2 1 
ATOM 4022 C CZ3 . TRP B 2 74   ? 190.567 205.178 132.521 1.00 6.94  ? 74  TRP B CZ3 1 
ATOM 4023 C CH2 . TRP B 2 74   ? 191.879 205.220 132.054 1.00 10.33 ? 74  TRP B CH2 1 
ATOM 4024 N N   . LEU B 2 75   ? 190.880 206.522 137.461 1.00 11.20 ? 75  LEU B N   1 
ATOM 4025 C CA  . LEU B 2 75   ? 191.006 205.116 137.833 1.00 3.54  ? 75  LEU B CA  1 
ATOM 4026 C C   . LEU B 2 75   ? 190.429 204.842 139.215 1.00 9.32  ? 75  LEU B C   1 
ATOM 4027 O O   . LEU B 2 75   ? 189.860 203.770 139.447 1.00 8.38  ? 75  LEU B O   1 
ATOM 4028 C CB  . LEU B 2 75   ? 192.466 204.675 137.772 1.00 1.26  ? 75  LEU B CB  1 
ATOM 4029 C CG  . LEU B 2 75   ? 193.065 204.705 136.368 1.00 0.00  ? 75  LEU B CG  1 
ATOM 4030 C CD1 . LEU B 2 75   ? 194.542 204.399 136.406 1.00 6.45  ? 75  LEU B CD1 1 
ATOM 4031 C CD2 . LEU B 2 75   ? 192.345 203.719 135.483 1.00 0.87  ? 75  LEU B CD2 1 
ATOM 4032 N N   . GLN B 2 76   ? 190.565 205.789 140.144 1.00 9.57  ? 76  GLN B N   1 
ATOM 4033 C CA  . GLN B 2 76   ? 189.953 205.648 141.458 1.00 1.60  ? 76  GLN B CA  1 
ATOM 4034 C C   . GLN B 2 76   ? 188.454 205.910 141.438 1.00 6.32  ? 76  GLN B C   1 
ATOM 4035 O O   . GLN B 2 76   ? 187.778 205.632 142.434 1.00 0.84  ? 76  GLN B O   1 
ATOM 4036 C CB  . GLN B 2 76   ? 190.631 206.589 142.454 1.00 3.58  ? 76  GLN B CB  1 
ATOM 4037 C CG  . GLN B 2 76   ? 192.137 206.662 142.293 1.00 2.23  ? 76  GLN B CG  1 
ATOM 4038 C CD  . GLN B 2 76   ? 192.875 206.255 143.550 1.00 10.28 ? 76  GLN B CD  1 
ATOM 4039 O OE1 . GLN B 2 76   ? 192.550 205.245 144.175 1.00 11.28 ? 76  GLN B OE1 1 
ATOM 4040 N NE2 . GLN B 2 76   ? 193.875 207.041 143.930 1.00 13.82 ? 76  GLN B NE2 1 
ATOM 4041 N N   . ASP B 2 77   ? 187.926 206.437 140.333 1.00 13.50 ? 77  ASP B N   1 
ATOM 4042 C CA  . ASP B 2 77   ? 186.497 206.660 140.165 1.00 12.75 ? 77  ASP B CA  1 
ATOM 4043 C C   . ASP B 2 77   ? 185.801 205.487 139.487 1.00 12.91 ? 77  ASP B C   1 
ATOM 4044 O O   . ASP B 2 77   ? 184.628 205.227 139.778 1.00 11.37 ? 77  ASP B O   1 
ATOM 4045 C CB  . ASP B 2 77   ? 186.277 207.949 139.353 1.00 5.40  ? 77  ASP B CB  1 
ATOM 4046 C CG  . ASP B 2 77   ? 186.618 209.219 140.124 1.00 10.36 ? 77  ASP B CG  1 
ATOM 4047 O OD1 . ASP B 2 77   ? 186.760 209.181 141.363 1.00 9.93  ? 77  ASP B OD1 1 
ATOM 4048 O OD2 . ASP B 2 77   ? 186.703 210.285 139.479 1.00 11.49 ? 77  ASP B OD2 1 
ATOM 4049 N N   . CYS B 2 78   ? 186.505 204.752 138.631 1.00 7.44  ? 78  CYS B N   1 
ATOM 4050 C CA  . CYS B 2 78   ? 185.907 203.699 137.825 1.00 1.08  ? 78  CYS B CA  1 
ATOM 4051 C C   . CYS B 2 78   ? 185.723 202.418 138.620 1.00 0.00  ? 78  CYS B C   1 
ATOM 4052 O O   . CYS B 2 78   ? 186.389 202.196 139.635 1.00 2.75  ? 78  CYS B O   1 
ATOM 4053 C CB  . CYS B 2 78   ? 186.776 203.399 136.607 1.00 8.59  ? 78  CYS B CB  1 
ATOM 4054 S SG  . CYS B 2 78   ? 186.897 204.734 135.451 1.00 1.19  ? 78  CYS B SG  1 
ATOM 4055 N N   . VAL B 2 79   ? 184.816 201.577 138.142 1.00 0.00  ? 79  VAL B N   1 
ATOM 4056 C CA  . VAL B 2 79   ? 184.719 200.202 138.608 1.00 2.60  ? 79  VAL B CA  1 
ATOM 4057 C C   . VAL B 2 79   ? 185.640 199.339 137.759 1.00 1.57  ? 79  VAL B C   1 
ATOM 4058 O O   . VAL B 2 79   ? 185.478 199.254 136.536 1.00 5.96  ? 79  VAL B O   1 
ATOM 4059 C CB  . VAL B 2 79   ? 183.270 199.703 138.528 1.00 3.32  ? 79  VAL B CB  1 
ATOM 4060 C CG1 . VAL B 2 79   ? 183.074 198.541 139.467 1.00 5.71  ? 79  VAL B CG1 1 
ATOM 4061 C CG2 . VAL B 2 79   ? 182.303 200.833 138.842 1.00 0.00  ? 79  VAL B CG2 1 
ATOM 4062 N N   . LEU B 2 80   ? 186.605 198.691 138.401 1.00 0.00  ? 80  LEU B N   1 
ATOM 4063 C CA  . LEU B 2 80   ? 187.586 197.876 137.704 1.00 0.00  ? 80  LEU B CA  1 
ATOM 4064 C C   . LEU B 2 80   ? 187.495 196.428 138.156 1.00 0.00  ? 80  LEU B C   1 
ATOM 4065 O O   . LEU B 2 80   ? 187.110 196.134 139.291 1.00 13.80 ? 80  LEU B O   1 
ATOM 4066 C CB  . LEU B 2 80   ? 189.013 198.369 137.940 1.00 0.00  ? 80  LEU B CB  1 
ATOM 4067 C CG  . LEU B 2 80   ? 189.584 199.377 136.951 1.00 0.00  ? 80  LEU B CG  1 
ATOM 4068 C CD1 . LEU B 2 80   ? 188.989 200.742 137.201 1.00 0.00  ? 80  LEU B CD1 1 
ATOM 4069 C CD2 . LEU B 2 80   ? 191.097 199.406 137.050 1.00 0.00  ? 80  LEU B CD2 1 
ATOM 4070 N N   . SER B 2 81   ? 187.857 195.528 137.248 1.00 0.00  ? 81  SER B N   1 
ATOM 4071 C CA  . SER B 2 81   ? 188.027 194.129 137.599 1.00 0.00  ? 81  SER B CA  1 
ATOM 4072 C C   . SER B 2 81   ? 188.982 193.497 136.600 1.00 0.00  ? 81  SER B C   1 
ATOM 4073 O O   . SER B 2 81   ? 188.919 193.790 135.405 1.00 12.12 ? 81  SER B O   1 
ATOM 4074 C CB  . SER B 2 81   ? 186.694 193.379 137.608 1.00 0.00  ? 81  SER B CB  1 
ATOM 4075 O OG  . SER B 2 81   ? 186.909 191.991 137.442 1.00 0.00  ? 81  SER B OG  1 
ATOM 4076 N N   . LEU B 2 82   ? 189.912 192.693 137.126 1.00 0.00  ? 82  LEU B N   1 
ATOM 4077 C CA  . LEU B 2 82   ? 190.878 191.960 136.268 1.00 0.00  ? 82  LEU B CA  1 
ATOM 4078 C C   . LEU B 2 82   ? 190.737 190.479 136.620 1.00 1.69  ? 82  LEU B C   1 
ATOM 4079 O O   . LEU B 2 82   ? 190.759 190.161 137.826 1.00 3.08  ? 82  LEU B O   1 
ATOM 4080 C CB  . LEU B 2 82   ? 192.295 192.467 136.547 1.00 0.00  ? 82  LEU B CB  1 
ATOM 4081 C CG  . LEU B 2 82   ? 193.422 191.619 135.961 1.00 3.62  ? 82  LEU B CG  1 
ATOM 4082 C CD1 . LEU B 2 82   ? 193.430 191.704 134.442 1.00 6.90  ? 82  LEU B CD1 1 
ATOM 4083 C CD2 . LEU B 2 82   ? 194.769 192.042 136.526 1.00 1.93  ? 82  LEU B CD2 1 
ATOM 4084 N N   . SER B 2 83   ? 190.601 189.611 135.619 1.00 0.00  ? 83  SER B N   1 
ATOM 4085 C CA  . SER B 2 83   ? 190.353 188.203 135.879 1.00 0.00  ? 83  SER B CA  1 
ATOM 4086 C C   . SER B 2 83   ? 191.540 187.591 136.618 1.00 2.10  ? 83  SER B C   1 
ATOM 4087 O O   . SER B 2 83   ? 192.691 187.952 136.349 1.00 0.66  ? 83  SER B O   1 
ATOM 4088 C CB  . SER B 2 83   ? 190.103 187.448 134.575 1.00 3.67  ? 83  SER B CB  1 
ATOM 4089 O OG  . SER B 2 83   ? 191.298 186.858 134.099 1.00 5.97  ? 83  SER B OG  1 
ATOM 4090 N N   . PRO B 2 84   ? 191.339 186.652 137.578 1.00 5.10  ? 84  PRO B N   1 
ATOM 4091 C CA  . PRO B 2 84   ? 192.456 186.085 138.340 1.00 2.15  ? 84  PRO B CA  1 
ATOM 4092 C C   . PRO B 2 84   ? 193.453 185.352 137.429 1.00 7.41  ? 84  PRO B C   1 
ATOM 4093 O O   . PRO B 2 84   ? 194.618 185.295 137.776 1.00 10.10 ? 84  PRO B O   1 
ATOM 4094 C CB  . PRO B 2 84   ? 191.801 185.073 139.292 1.00 4.69  ? 84  PRO B CB  1 
ATOM 4095 C CG  . PRO B 2 84   ? 190.376 185.550 139.410 1.00 3.91  ? 84  PRO B CG  1 
ATOM 4096 C CD  . PRO B 2 84   ? 190.054 186.093 138.035 1.00 6.01  ? 84  PRO B CD  1 
ATOM 4097 N N   . THR B 2 85   ? 192.980 184.806 136.304 1.00 8.96  ? 85  THR B N   1 
ATOM 4098 C CA  . THR B 2 85   ? 193.855 184.089 135.389 1.00 5.61  ? 85  THR B CA  1 
ATOM 4099 C C   . THR B 2 85   ? 194.418 184.979 134.288 1.00 11.77 ? 85  THR B C   1 
ATOM 4100 O O   . THR B 2 85   ? 195.057 184.466 133.363 1.00 12.12 ? 85  THR B O   1 
ATOM 4101 C CB  . THR B 2 85   ? 193.111 182.901 134.774 1.00 0.00  ? 85  THR B CB  1 
ATOM 4102 O OG1 . THR B 2 85   ? 193.916 182.311 133.746 1.00 5.14  ? 85  THR B OG1 1 
ATOM 4103 C CG2 . THR B 2 85   ? 191.785 183.347 134.189 1.00 0.00  ? 85  THR B CG2 1 
ATOM 4104 N N   . ASN B 2 86   ? 194.191 186.294 134.366 1.00 11.57 ? 86  ASN B N   1 
ATOM 4105 C CA  . ASN B 2 86   ? 194.727 187.262 133.405 1.00 8.63  ? 86  ASN B CA  1 
ATOM 4106 C C   . ASN B 2 86   ? 194.226 186.969 131.993 1.00 7.97  ? 86  ASN B C   1 
ATOM 4107 O O   . ASN B 2 86   ? 195.000 186.786 131.052 1.00 10.06 ? 86  ASN B O   1 
ATOM 4108 C CB  . ASN B 2 86   ? 196.255 187.297 133.452 1.00 6.71  ? 86  ASN B CB  1 
ATOM 4109 C CG  . ASN B 2 86   ? 196.779 188.295 134.457 1.00 12.09 ? 86  ASN B CG  1 
ATOM 4110 O OD1 . ASN B 2 86   ? 196.349 189.448 134.488 1.00 14.39 ? 86  ASN B OD1 1 
ATOM 4111 N ND2 . ASN B 2 86   ? 197.703 187.853 135.298 1.00 13.60 ? 86  ASN B ND2 1 
ATOM 4112 N N   . ASP B 2 87   ? 192.897 186.924 131.846 1.00 0.60  ? 87  ASP B N   1 
ATOM 4113 C CA  . ASP B 2 87   ? 192.303 186.575 130.526 1.00 0.00  ? 87  ASP B CA  1 
ATOM 4114 C C   . ASP B 2 87   ? 191.481 187.748 129.979 1.00 7.52  ? 87  ASP B C   1 
ATOM 4115 O O   . ASP B 2 87   ? 191.260 187.778 128.754 1.00 14.20 ? 87  ASP B O   1 
ATOM 4116 C CB  . ASP B 2 87   ? 191.449 185.309 130.625 1.00 0.12  ? 87  ASP B CB  1 
ATOM 4117 C CG  . ASP B 2 87   ? 192.246 184.025 130.477 1.00 5.55  ? 87  ASP B CG  1 
ATOM 4118 O OD1 . ASP B 2 87   ? 193.393 183.988 130.963 1.00 4.63  ? 87  ASP B OD1 1 
ATOM 4119 O OD2 . ASP B 2 87   ? 191.713 183.072 129.877 1.00 12.35 ? 87  ASP B OD2 1 
ATOM 4120 N N   . LEU B 2 88   ? 191.027 188.658 130.848 1.00 3.46  ? 88  LEU B N   1 
ATOM 4121 C CA  . LEU B 2 88   ? 190.163 189.781 130.390 1.00 0.00  ? 88  LEU B CA  1 
ATOM 4122 C C   . LEU B 2 88   ? 190.188 190.923 131.412 1.00 0.00  ? 88  LEU B C   1 
ATOM 4123 O O   . LEU B 2 88   ? 190.660 190.692 132.543 1.00 3.03  ? 88  LEU B O   1 
ATOM 4124 C CB  . LEU B 2 88   ? 188.735 189.265 130.185 1.00 1.53  ? 88  LEU B CB  1 
ATOM 4125 C CG  . LEU B 2 88   ? 187.911 190.032 129.152 1.00 8.18  ? 88  LEU B CG  1 
ATOM 4126 C CD1 . LEU B 2 88   ? 188.201 189.530 127.745 1.00 4.82  ? 88  LEU B CD1 1 
ATOM 4127 C CD2 . LEU B 2 88   ? 186.426 189.937 129.462 1.00 0.00  ? 88  LEU B CD2 1 
ATOM 4128 N N   . MET B 2 89   ? 189.688 192.102 131.024 1.00 0.00  ? 89  MET B N   1 
ATOM 4129 C CA  . MET B 2 89   ? 189.675 193.280 131.934 1.00 0.00  ? 89  MET B CA  1 
ATOM 4130 C C   . MET B 2 89   ? 188.367 194.058 131.751 1.00 0.00  ? 89  MET B C   1 
ATOM 4131 O O   . MET B 2 89   ? 187.996 194.314 130.589 1.00 8.57  ? 89  MET B O   1 
ATOM 4132 C CB  . MET B 2 89   ? 190.866 194.200 131.645 1.00 4.68  ? 89  MET B CB  1 
ATOM 4133 C CG  . MET B 2 89   ? 190.588 195.669 131.911 1.00 2.16  ? 89  MET B CG  1 
ATOM 4134 S SD  . MET B 2 89   ? 190.634 196.083 133.673 1.00 1.99  ? 89  MET B SD  1 
ATOM 4135 C CE  . MET B 2 89   ? 192.388 195.923 134.001 1.00 5.72  ? 89  MET B CE  1 
ATOM 4136 N N   . VAL B 2 90   ? 187.693 194.404 132.852 1.00 0.00  ? 90  VAL B N   1 
ATOM 4137 C CA  . VAL B 2 90   ? 186.459 195.180 132.790 1.00 0.00  ? 90  VAL B CA  1 
ATOM 4138 C C   . VAL B 2 90   ? 186.726 196.519 133.457 1.00 1.35  ? 90  VAL B C   1 
ATOM 4139 O O   . VAL B 2 90   ? 187.225 196.557 134.589 1.00 16.52 ? 90  VAL B O   1 
ATOM 4140 C CB  . VAL B 2 90   ? 185.291 194.459 133.483 1.00 0.00  ? 90  VAL B CB  1 
ATOM 4141 C CG1 . VAL B 2 90   ? 184.143 195.420 133.743 1.00 0.00  ? 90  VAL B CG1 1 
ATOM 4142 C CG2 . VAL B 2 90   ? 184.824 193.294 132.648 1.00 1.25  ? 90  VAL B CG2 1 
ATOM 4143 N N   . ILE B 2 91   ? 186.406 197.613 132.766 1.00 0.00  ? 91  ILE B N   1 
ATOM 4144 C CA  . ILE B 2 91   ? 186.548 198.955 133.328 1.00 0.00  ? 91  ILE B CA  1 
ATOM 4145 C C   . ILE B 2 91   ? 185.300 199.744 132.945 1.00 0.00  ? 91  ILE B C   1 
ATOM 4146 O O   . ILE B 2 91   ? 185.111 200.095 131.778 1.00 11.14 ? 91  ILE B O   1 
ATOM 4147 C CB  . ILE B 2 91   ? 187.833 199.645 132.851 1.00 0.00  ? 91  ILE B CB  1 
ATOM 4148 C CG1 . ILE B 2 91   ? 187.791 201.150 133.113 1.00 0.00  ? 91  ILE B CG1 1 
ATOM 4149 C CG2 . ILE B 2 91   ? 188.105 199.341 131.393 1.00 5.64  ? 91  ILE B CG2 1 
ATOM 4150 C CD1 . ILE B 2 91   ? 189.100 201.841 132.804 1.00 0.00  ? 91  ILE B CD1 1 
ATOM 4151 N N   . ALA B 2 92   ? 184.433 200.017 133.916 1.00 0.00  ? 92  ALA B N   1 
ATOM 4152 C CA  . ALA B 2 92   ? 183.163 200.687 133.656 1.00 0.00  ? 92  ALA B CA  1 
ATOM 4153 C C   . ALA B 2 92   ? 183.069 201.969 134.472 1.00 0.00  ? 92  ALA B C   1 
ATOM 4154 O O   . ALA B 2 92   ? 183.390 201.971 135.663 1.00 8.77  ? 92  ALA B O   1 
ATOM 4155 C CB  . ALA B 2 92   ? 181.985 199.770 133.986 1.00 0.00  ? 92  ALA B CB  1 
ATOM 4156 N N   . ARG B 2 93   ? 182.626 203.055 133.834 1.00 2.69  ? 93  ARG B N   1 
ATOM 4157 C CA  . ARG B 2 93   ? 182.611 204.338 134.537 1.00 7.72  ? 93  ARG B CA  1 
ATOM 4158 C C   . ARG B 2 93   ? 181.274 204.700 135.174 1.00 5.18  ? 93  ARG B C   1 
ATOM 4159 O O   . ARG B 2 93   ? 181.173 204.770 136.403 1.00 19.75 ? 93  ARG B O   1 
ATOM 4160 C CB  . ARG B 2 93   ? 183.024 205.467 133.592 1.00 10.23 ? 93  ARG B CB  1 
ATOM 4161 C CG  . ARG B 2 93   ? 182.968 206.855 134.219 1.00 10.35 ? 93  ARG B CG  1 
ATOM 4162 C CD  . ARG B 2 93   ? 183.963 206.980 135.360 1.00 12.26 ? 93  ARG B CD  1 
ATOM 4163 N NE  . ARG B 2 93   ? 183.927 208.299 135.976 1.00 9.59  ? 93  ARG B NE  1 
ATOM 4164 C CZ  . ARG B 2 93   ? 183.096 208.659 136.946 1.00 16.59 ? 93  ARG B CZ  1 
ATOM 4165 N NH1 . ARG B 2 93   ? 182.150 207.849 137.384 1.00 22.77 ? 93  ARG B NH1 1 
ATOM 4166 N NH2 . ARG B 2 93   ? 183.208 209.874 137.475 1.00 8.74  ? 93  ARG B NH2 1 
ATOM 4167 N N   . GLU B 2 94   ? 180.243 204.946 134.366 1.00 0.48  ? 94  GLU B N   1 
ATOM 4168 C CA  . GLU B 2 94   ? 178.923 205.265 134.902 1.00 7.63  ? 94  GLU B CA  1 
ATOM 4169 C C   . GLU B 2 94   ? 177.865 204.294 134.403 1.00 10.32 ? 94  GLU B C   1 
ATOM 4170 O O   . GLU B 2 94   ? 177.150 203.690 135.209 1.00 9.32  ? 94  GLU B O   1 
ATOM 4171 C CB  . GLU B 2 94   ? 178.552 206.714 134.555 1.00 16.99 ? 94  GLU B CB  1 
ATOM 4172 C CG  . GLU B 2 94   ? 177.223 207.194 135.121 1.00 18.42 ? 94  GLU B CG  1 
ATOM 4173 C CD  . GLU B 2 94   ? 176.937 208.642 134.786 1.00 19.21 ? 94  GLU B CD  1 
ATOM 4174 O OE1 . GLU B 2 94   ? 177.759 209.262 134.078 1.00 15.59 ? 94  GLU B OE1 1 
ATOM 4175 O OE2 . GLU B 2 94   ? 175.891 209.160 135.228 1.00 14.11 ? 94  GLU B OE2 1 
ATOM 4176 N N   . GLN B 2 95   ? 177.744 204.137 133.085 1.00 12.84 ? 95  GLN B N   1 
ATOM 4177 C CA  . GLN B 2 95   ? 176.925 203.097 132.476 1.00 18.69 ? 95  GLN B CA  1 
ATOM 4178 C C   . GLN B 2 95   ? 177.628 202.522 131.253 1.00 16.27 ? 95  GLN B C   1 
ATOM 4179 O O   . GLN B 2 95   ? 177.010 201.777 130.483 1.00 10.86 ? 95  GLN B O   1 
ATOM 4180 C CB  . GLN B 2 95   ? 175.543 203.636 132.099 1.00 16.67 ? 95  GLN B CB  1 
ATOM 4181 C CG  . GLN B 2 95   ? 175.586 204.842 131.179 1.00 18.69 ? 95  GLN B CG  1 
ATOM 4182 C CD  . GLN B 2 95   ? 174.226 205.482 130.991 1.00 19.33 ? 95  GLN B CD  1 
ATOM 4183 O OE1 . GLN B 2 95   ? 173.309 205.260 131.781 1.00 22.63 ? 95  GLN B OE1 1 
ATOM 4184 N NE2 . GLN B 2 95   ? 174.089 206.281 129.942 1.00 17.01 ? 95  GLN B NE2 1 
ATOM 4185 N N   . LYS B 2 96   ? 178.906 202.854 131.067 1.00 7.22  ? 96  LYS B N   1 
ATOM 4186 C CA  . LYS B 2 96   ? 179.688 202.450 129.906 1.00 2.89  ? 96  LYS B CA  1 
ATOM 4187 C C   . LYS B 2 96   ? 180.854 201.601 130.382 1.00 8.41  ? 96  LYS B C   1 
ATOM 4188 O O   . LYS B 2 96   ? 181.617 202.029 131.257 1.00 14.12 ? 96  LYS B O   1 
ATOM 4189 C CB  . LYS B 2 96   ? 180.194 203.675 129.144 1.00 2.05  ? 96  LYS B CB  1 
ATOM 4190 C CG  . LYS B 2 96   ? 179.088 204.526 128.564 1.00 9.96  ? 96  LYS B CG  1 
ATOM 4191 C CD  . LYS B 2 96   ? 179.645 205.696 127.780 1.00 6.89  ? 96  LYS B CD  1 
ATOM 4192 C CE  . LYS B 2 96   ? 178.529 206.505 127.150 1.00 5.45  ? 96  LYS B CE  1 
ATOM 4193 N NZ  . LYS B 2 96   ? 179.057 207.647 126.358 1.00 10.33 ? 96  LYS B NZ  1 
ATOM 4194 N N   . ALA B 2 97   ? 180.974 200.396 129.808 1.00 4.67  ? 97  ALA B N   1 
ATOM 4195 C CA  . ALA B 2 97   ? 182.021 199.450 130.262 1.00 0.00  ? 97  ALA B CA  1 
ATOM 4196 C C   . ALA B 2 97   ? 182.915 198.998 129.106 1.00 0.00  ? 97  ALA B C   1 
ATOM 4197 O O   . ALA B 2 97   ? 182.385 198.412 128.142 1.00 0.00  ? 97  ALA B O   1 
ATOM 4198 C CB  . ALA B 2 97   ? 181.382 198.259 130.932 1.00 0.00  ? 97  ALA B CB  1 
ATOM 4199 N N   . VAL B 2 98   ? 184.218 199.257 129.208 1.00 0.00  ? 98  VAL B N   1 
ATOM 4200 C CA  . VAL B 2 98   ? 185.193 198.805 128.226 1.00 0.00  ? 98  VAL B CA  1 
ATOM 4201 C C   . VAL B 2 98   ? 185.723 197.441 128.655 1.00 8.97  ? 98  VAL B C   1 
ATOM 4202 O O   . VAL B 2 98   ? 186.124 197.246 129.812 1.00 15.07 ? 98  VAL B O   1 
ATOM 4203 C CB  . VAL B 2 98   ? 186.327 199.826 128.078 1.00 0.00  ? 98  VAL B CB  1 
ATOM 4204 C CG1 . VAL B 2 98   ? 187.132 199.542 126.832 1.00 0.00  ? 98  VAL B CG1 1 
ATOM 4205 C CG2 . VAL B 2 98   ? 185.760 201.228 128.036 1.00 0.00  ? 98  VAL B CG2 1 
ATOM 4206 N N   . PHE B 2 99   ? 185.700 196.485 127.726 1.00 7.08  ? 99  PHE B N   1 
ATOM 4207 C CA  . PHE B 2 99   ? 186.271 195.160 127.941 1.00 0.00  ? 99  PHE B CA  1 
ATOM 4208 C C   . PHE B 2 99   ? 187.588 195.082 127.178 1.00 0.00  ? 99  PHE B C   1 
ATOM 4209 O O   . PHE B 2 99   ? 187.622 195.345 125.970 1.00 7.79  ? 99  PHE B O   1 
ATOM 4210 C CB  . PHE B 2 99   ? 185.329 194.054 127.460 1.00 0.00  ? 99  PHE B CB  1 
ATOM 4211 C CG  . PHE B 2 99   ? 183.978 194.043 128.128 1.00 0.00  ? 99  PHE B CG  1 
ATOM 4212 C CD1 . PHE B 2 99   ? 183.738 194.761 129.284 1.00 0.00  ? 99  PHE B CD1 1 
ATOM 4213 C CD2 . PHE B 2 99   ? 182.943 193.299 127.587 1.00 0.00  ? 99  PHE B CD2 1 
ATOM 4214 C CE1 . PHE B 2 99   ? 182.491 194.738 129.881 1.00 0.00  ? 99  PHE B CE1 1 
ATOM 4215 C CE2 . PHE B 2 99   ? 181.699 193.274 128.181 1.00 0.00  ? 99  PHE B CE2 1 
ATOM 4216 C CZ  . PHE B 2 99   ? 181.472 193.992 129.327 1.00 0.00  ? 99  PHE B CZ  1 
ATOM 4217 N N   . LEU B 2 100  ? 188.658 194.709 127.876 1.00 0.00  ? 100 LEU B N   1 
ATOM 4218 C CA  . LEU B 2 100  ? 190.004 194.654 127.321 1.00 0.00  ? 100 LEU B CA  1 
ATOM 4219 C C   . LEU B 2 100  ? 190.482 193.209 127.251 1.00 11.64 ? 100 LEU B C   1 
ATOM 4220 O O   . LEU B 2 100  ? 190.339 192.449 128.216 1.00 17.27 ? 100 LEU B O   1 
ATOM 4221 C CB  . LEU B 2 100  ? 190.983 195.479 128.162 1.00 0.00  ? 100 LEU B CB  1 
ATOM 4222 C CG  . LEU B 2 100  ? 191.158 196.966 127.844 1.00 4.36  ? 100 LEU B CG  1 
ATOM 4223 C CD1 . LEU B 2 100  ? 189.887 197.732 128.131 1.00 0.00  ? 100 LEU B CD1 1 
ATOM 4224 C CD2 . LEU B 2 100  ? 192.308 197.549 128.637 1.00 10.62 ? 100 LEU B CD2 1 
ATOM 4225 N N   . VAL B 2 101  ? 191.074 192.851 126.113 1.00 17.52 ? 101 VAL B N   1 
ATOM 4226 C CA  . VAL B 2 101  ? 191.462 191.480 125.781 1.00 16.19 ? 101 VAL B CA  1 
ATOM 4227 C C   . VAL B 2 101  ? 192.968 191.435 125.532 1.00 19.51 ? 101 VAL B C   1 
ATOM 4228 O O   . VAL B 2 101  ? 193.517 192.358 124.914 1.00 22.35 ? 101 VAL B O   1 
ATOM 4229 C CB  . VAL B 2 101  ? 190.673 190.979 124.558 1.00 14.37 ? 101 VAL B CB  1 
ATOM 4230 C CG1 . VAL B 2 101  ? 190.981 191.799 123.314 1.00 17.62 ? 101 VAL B CG1 1 
ATOM 4231 C CG2 . VAL B 2 101  ? 190.957 189.507 124.313 1.00 5.88  ? 101 VAL B CG2 1 
ATOM 4232 N N   . PRO B 2 102  ? 193.673 190.403 125.989 1.00 18.18 ? 102 PRO B N   1 
ATOM 4233 C CA  . PRO B 2 102  ? 195.123 190.346 125.779 1.00 20.48 ? 102 PRO B CA  1 
ATOM 4234 C C   . PRO B 2 102  ? 195.479 190.105 124.322 1.00 19.89 ? 102 PRO B C   1 
ATOM 4235 O O   . PRO B 2 102  ? 194.643 189.745 123.493 1.00 21.67 ? 102 PRO B O   1 
ATOM 4236 C CB  . PRO B 2 102  ? 195.548 189.164 126.635 1.00 22.53 ? 102 PRO B CB  1 
ATOM 4237 C CG  . PRO B 2 102  ? 194.342 188.333 126.801 1.00 19.57 ? 102 PRO B CG  1 
ATOM 4238 C CD  . PRO B 2 102  ? 193.203 189.301 126.844 1.00 15.28 ? 102 PRO B CD  1 
ATOM 4239 N N   . LYS B 2 103  ? 196.760 190.310 124.020 1.00 27.46 ? 103 LYS B N   1 
ATOM 4240 C CA  . LYS B 2 103  ? 197.285 190.022 122.688 1.00 29.23 ? 103 LYS B CA  1 
ATOM 4241 C C   . LYS B 2 103  ? 198.798 189.915 122.791 1.00 31.47 ? 103 LYS B C   1 
ATOM 4242 O O   . LYS B 2 103  ? 199.463 190.896 123.140 1.00 30.51 ? 103 LYS B O   1 
ATOM 4243 C CB  . LYS B 2 103  ? 196.860 191.109 121.691 1.00 25.81 ? 103 LYS B CB  1 
ATOM 4244 C CG  . LYS B 2 103  ? 197.287 190.886 120.244 1.00 28.60 ? 103 LYS B CG  1 
ATOM 4245 C CD  . LYS B 2 103  ? 196.793 191.974 119.302 1.00 30.16 ? 103 LYS B CD  1 
ATOM 4246 C CE  . LYS B 2 103  ? 197.267 191.713 117.885 1.00 32.21 ? 103 LYS B CE  1 
ATOM 4247 N NZ  . LYS B 2 103  ? 196.800 192.760 116.939 1.00 30.83 ? 103 LYS B NZ  1 
ATOM 4248 N N   . TRP B 2 104  ? 199.340 188.734 122.496 1.00 33.81 ? 104 TRP B N   1 
ATOM 4249 C CA  . TRP B 2 104  ? 200.779 188.496 122.581 1.00 33.30 ? 104 TRP B CA  1 
ATOM 4250 C C   . TRP B 2 104  ? 201.439 188.961 121.288 1.00 32.92 ? 104 TRP B C   1 
ATOM 4251 O O   . TRP B 2 104  ? 201.160 188.424 120.211 1.00 32.27 ? 104 TRP B O   1 
ATOM 4252 C CB  . TRP B 2 104  ? 201.068 187.019 122.842 1.00 30.51 ? 104 TRP B CB  1 
ATOM 4253 C CG  . TRP B 2 104  ? 200.423 186.476 124.081 1.00 29.49 ? 104 TRP B CG  1 
ATOM 4254 C CD1 . TRP B 2 104  ? 201.005 186.323 125.304 1.00 29.21 ? 104 TRP B CD1 1 
ATOM 4255 C CD2 . TRP B 2 104  ? 199.077 186.004 124.215 1.00 30.96 ? 104 TRP B CD2 1 
ATOM 4256 N NE1 . TRP B 2 104  ? 200.105 185.790 126.194 1.00 32.71 ? 104 TRP B NE1 1 
ATOM 4257 C CE2 . TRP B 2 104  ? 198.913 185.585 125.550 1.00 31.69 ? 104 TRP B CE2 1 
ATOM 4258 C CE3 . TRP B 2 104  ? 197.994 185.898 123.337 1.00 30.19 ? 104 TRP B CE3 1 
ATOM 4259 C CZ2 . TRP B 2 104  ? 197.711 185.068 126.028 1.00 28.31 ? 104 TRP B CZ2 1 
ATOM 4260 C CZ3 . TRP B 2 104  ? 196.800 185.384 123.815 1.00 29.40 ? 104 TRP B CZ3 1 
ATOM 4261 C CH2 . TRP B 2 104  ? 196.669 184.976 125.147 1.00 26.10 ? 104 TRP B CH2 1 
ATOM 4262 N N   . LYS B 2 105  ? 202.320 189.952 121.392 1.00 33.90 ? 105 LYS B N   1 
ATOM 4263 C CA  . LYS B 2 105  ? 202.993 190.542 120.242 1.00 33.86 ? 105 LYS B CA  1 
ATOM 4264 C C   . LYS B 2 105  ? 204.488 190.277 120.326 1.00 35.67 ? 105 LYS B C   1 
ATOM 4265 O O   . LYS B 2 105  ? 205.105 190.503 121.372 1.00 30.33 ? 105 LYS B O   1 
ATOM 4266 C CB  . LYS B 2 105  ? 202.740 192.049 120.174 1.00 31.90 ? 105 LYS B CB  1 
ATOM 4267 C CG  . LYS B 2 105  ? 203.467 192.764 119.038 1.00 34.83 ? 105 LYS B CG  1 
ATOM 4268 C CD  . LYS B 2 105  ? 203.090 192.186 117.678 1.00 33.63 ? 105 LYS B CD  1 
ATOM 4269 C CE  . LYS B 2 105  ? 204.217 192.332 116.664 1.00 30.63 ? 105 LYS B CE  1 
ATOM 4270 N NZ  . LYS B 2 105  ? 204.895 191.035 116.386 1.00 31.73 ? 105 LYS B NZ  1 
ATOM 4271 N N   . TYR B 2 106  ? 205.068 189.811 119.224 1.00 38.95 ? 106 TYR B N   1 
ATOM 4272 C CA  . TYR B 2 106  ? 206.512 189.634 119.156 1.00 38.20 ? 106 TYR B CA  1 
ATOM 4273 C C   . TYR B 2 106  ? 207.188 190.997 119.075 1.00 36.23 ? 106 TYR B C   1 
ATOM 4274 O O   . TYR B 2 106  ? 206.946 191.763 118.137 1.00 34.23 ? 106 TYR B O   1 
ATOM 4275 C CB  . TYR B 2 106  ? 206.886 188.777 117.949 1.00 38.12 ? 106 TYR B CB  1 
ATOM 4276 C CG  . TYR B 2 106  ? 206.229 187.417 117.929 1.00 37.30 ? 106 TYR B CG  1 
ATOM 4277 C CD1 . TYR B 2 106  ? 204.983 187.235 117.344 1.00 36.35 ? 106 TYR B CD1 1 
ATOM 4278 C CD2 . TYR B 2 106  ? 206.853 186.315 118.499 1.00 34.59 ? 106 TYR B CD2 1 
ATOM 4279 C CE1 . TYR B 2 106  ? 204.377 185.994 117.325 1.00 37.91 ? 106 TYR B CE1 1 
ATOM 4280 C CE2 . TYR B 2 106  ? 206.256 185.069 118.482 1.00 35.79 ? 106 TYR B CE2 1 
ATOM 4281 C CZ  . TYR B 2 106  ? 205.018 184.915 117.895 1.00 37.20 ? 106 TYR B CZ  1 
ATOM 4282 O OH  . TYR B 2 106  ? 204.419 183.677 117.877 1.00 35.71 ? 106 TYR B OH  1 
ATOM 4283 N N   . SER B 2 107  ? 208.034 191.301 120.054 1.00 35.43 ? 107 SER B N   1 
ATOM 4284 C CA  . SER B 2 107  ? 208.732 192.578 120.087 1.00 36.17 ? 107 SER B CA  1 
ATOM 4285 C C   . SER B 2 107  ? 209.920 192.531 119.128 1.00 36.16 ? 107 SER B C   1 
ATOM 4286 O O   . SER B 2 107  ? 210.070 191.603 118.328 1.00 33.64 ? 107 SER B O   1 
ATOM 4287 C CB  . SER B 2 107  ? 209.157 192.912 121.514 1.00 36.69 ? 107 SER B CB  1 
ATOM 4288 O OG  . SER B 2 107  ? 210.379 192.276 121.846 1.00 34.26 ? 107 SER B OG  1 
ATOM 4289 N N   . ASP B 2 108  ? 210.792 193.539 119.216 1.00 37.51 ? 108 ASP B N   1 
ATOM 4290 C CA  . ASP B 2 108  ? 212.001 193.570 118.348 1.00 36.17 ? 108 ASP B CA  1 
ATOM 4291 C C   . ASP B 2 108  ? 212.904 192.383 118.700 1.00 37.68 ? 108 ASP B C   1 
ATOM 4292 O O   . ASP B 2 108  ? 213.612 191.897 117.797 1.00 37.00 ? 108 ASP B O   1 
ATOM 4293 C CB  . ASP B 2 108  ? 212.739 194.906 118.467 1.00 34.66 ? 108 ASP B CB  1 
ATOM 4294 C CG  . ASP B 2 108  ? 212.004 196.070 117.825 1.00 38.43 ? 108 ASP B CG  1 
ATOM 4295 O OD1 . ASP B 2 108  ? 211.067 195.815 117.043 1.00 37.82 ? 108 ASP B OD1 1 
ATOM 4296 O OD2 . ASP B 2 108  ? 212.375 197.225 118.114 1.00 40.74 ? 108 ASP B OD2 1 
ATOM 4297 N N   . LYS B 2 109  ? 212.877 191.938 119.959 1.00 37.34 ? 109 LYS B N   1 
ATOM 4298 C CA  . LYS B 2 109  ? 213.699 190.819 120.399 1.00 37.51 ? 109 LYS B CA  1 
ATOM 4299 C C   . LYS B 2 109  ? 212.981 189.480 120.292 1.00 39.51 ? 109 LYS B C   1 
ATOM 4300 O O   . LYS B 2 109  ? 213.562 188.452 120.655 1.00 38.33 ? 109 LYS B O   1 
ATOM 4301 C CB  . LYS B 2 109  ? 214.167 191.040 121.842 1.00 37.39 ? 109 LYS B CB  1 
ATOM 4302 C CG  . LYS B 2 109  ? 215.445 191.861 121.972 1.00 38.66 ? 109 LYS B CG  1 
ATOM 4303 C CD  . LYS B 2 109  ? 215.202 193.331 121.663 1.00 35.51 ? 109 LYS B CD  1 
ATOM 4304 C CE  . LYS B 2 109  ? 216.477 194.147 121.787 1.00 37.06 ? 109 LYS B CE  1 
ATOM 4305 N NZ  . LYS B 2 109  ? 216.184 195.591 122.000 1.00 36.57 ? 109 LYS B NZ  1 
ATOM 4306 N N   . GLY B 2 110  ? 211.742 189.467 119.807 1.00 38.92 ? 110 GLY B N   1 
ATOM 4307 C CA  . GLY B 2 110  ? 210.991 188.241 119.644 1.00 37.94 ? 110 GLY B CA  1 
ATOM 4308 C C   . GLY B 2 110  ? 210.146 187.832 120.830 1.00 38.79 ? 110 GLY B C   1 
ATOM 4309 O O   . GLY B 2 110  ? 209.395 186.854 120.723 1.00 36.76 ? 110 GLY B O   1 
ATOM 4310 N N   . LYS B 2 111  ? 210.239 188.540 121.952 1.00 35.08 ? 111 LYS B N   1 
ATOM 4311 C CA  . LYS B 2 111  ? 209.438 188.196 123.118 1.00 36.83 ? 111 LYS B CA  1 
ATOM 4312 C C   . LYS B 2 111  ? 207.977 188.551 122.873 1.00 38.06 ? 111 LYS B C   1 
ATOM 4313 O O   . LYS B 2 111  ? 207.659 189.669 122.455 1.00 33.46 ? 111 LYS B O   1 
ATOM 4314 C CB  . LYS B 2 111  ? 209.966 188.922 124.356 1.00 36.55 ? 111 LYS B CB  1 
ATOM 4315 C CG  . LYS B 2 111  ? 208.928 189.174 125.443 1.00 33.53 ? 111 LYS B CG  1 
ATOM 4316 C CD  . LYS B 2 111  ? 208.501 187.883 126.129 1.00 32.01 ? 111 LYS B CD  1 
ATOM 4317 C CE  . LYS B 2 111  ? 209.692 187.130 126.695 1.00 36.16 ? 111 LYS B CE  1 
ATOM 4318 N NZ  . LYS B 2 111  ? 209.272 186.077 127.660 1.00 35.75 ? 111 LYS B NZ  1 
ATOM 4319 N N   . GLU B 2 112  ? 207.086 187.596 123.135 1.00 39.65 ? 112 GLU B N   1 
ATOM 4320 C CA  . GLU B 2 112  ? 205.648 187.821 122.998 1.00 39.08 ? 112 GLU B CA  1 
ATOM 4321 C C   . GLU B 2 112  ? 205.110 188.429 124.294 1.00 38.35 ? 112 GLU B C   1 
ATOM 4322 O O   . GLU B 2 112  ? 204.447 187.780 125.106 1.00 36.44 ? 112 GLU B O   1 
ATOM 4323 C CB  . GLU B 2 112  ? 204.938 186.520 122.645 1.00 35.85 ? 112 GLU B CB  1 
ATOM 4324 C CG  . GLU B 2 112  ? 204.505 186.426 121.191 1.00 31.14 ? 112 GLU B CG  1 
ATOM 4325 C CD  . GLU B 2 112  ? 203.649 185.205 120.913 1.00 32.62 ? 112 GLU B CD  1 
ATOM 4326 O OE1 . GLU B 2 112  ? 204.052 184.092 121.310 1.00 35.79 ? 112 GLU B OE1 1 
ATOM 4327 O OE2 . GLU B 2 112  ? 202.575 185.358 120.293 1.00 30.75 ? 112 GLU B OE2 1 
ATOM 4328 N N   . GLU B 2 113  ? 205.417 189.712 124.478 1.00 36.47 ? 113 GLU B N   1 
ATOM 4329 C CA  . GLU B 2 113  ? 205.036 190.401 125.702 1.00 36.27 ? 113 GLU B CA  1 
ATOM 4330 C C   . GLU B 2 113  ? 203.524 190.587 125.766 1.00 36.16 ? 113 GLU B C   1 
ATOM 4331 O O   . GLU B 2 113  ? 202.852 190.741 124.743 1.00 33.20 ? 113 GLU B O   1 
ATOM 4332 C CB  . GLU B 2 113  ? 205.754 191.749 125.805 1.00 33.97 ? 113 GLU B CB  1 
ATOM 4333 C CG  . GLU B 2 113  ? 205.047 192.909 125.129 1.00 32.38 ? 113 GLU B CG  1 
ATOM 4334 C CD  . GLU B 2 113  ? 205.322 192.966 123.642 1.00 38.22 ? 113 GLU B CD  1 
ATOM 4335 O OE1 . GLU B 2 113  ? 206.446 192.608 123.234 1.00 36.36 ? 113 GLU B OE1 1 
ATOM 4336 O OE2 . GLU B 2 113  ? 204.418 193.372 122.883 1.00 42.15 ? 113 GLU B OE2 1 
ATOM 4337 N N   . MET B 2 114  ? 202.990 190.549 126.983 1.00 34.50 ? 114 MET B N   1 
ATOM 4338 C CA  . MET B 2 114  ? 201.552 190.637 127.195 1.00 33.05 ? 114 MET B CA  1 
ATOM 4339 C C   . MET B 2 114  ? 201.109 192.094 127.134 1.00 34.33 ? 114 MET B C   1 
ATOM 4340 O O   . MET B 2 114  ? 201.679 192.952 127.815 1.00 37.08 ? 114 MET B O   1 
ATOM 4341 C CB  . MET B 2 114  ? 201.197 190.016 128.546 1.00 33.84 ? 114 MET B CB  1 
ATOM 4342 C CG  . MET B 2 114  ? 199.722 189.971 128.875 1.00 34.68 ? 114 MET B CG  1 
ATOM 4343 S SD  . MET B 2 114  ? 199.393 189.124 130.423 1.00 32.84 ? 114 MET B SD  1 
ATOM 4344 C CE  . MET B 2 114  ? 199.553 187.419 129.885 1.00 23.46 ? 114 MET B CE  1 
ATOM 4345 N N   . GLN B 2 115  ? 200.097 192.379 126.313 1.00 28.60 ? 115 GLN B N   1 
ATOM 4346 C CA  . GLN B 2 115  ? 199.608 193.745 126.129 1.00 27.64 ? 115 GLN B CA  1 
ATOM 4347 C C   . GLN B 2 115  ? 198.096 193.711 125.960 1.00 26.35 ? 115 GLN B C   1 
ATOM 4348 O O   . GLN B 2 115  ? 197.594 193.174 124.968 1.00 29.94 ? 115 GLN B O   1 
ATOM 4349 C CB  . GLN B 2 115  ? 200.271 194.418 124.925 1.00 26.75 ? 115 GLN B CB  1 
ATOM 4350 C CG  . GLN B 2 115  ? 201.665 194.961 125.203 1.00 22.38 ? 115 GLN B CG  1 
ATOM 4351 C CD  . GLN B 2 115  ? 202.122 195.970 124.167 1.00 28.06 ? 115 GLN B CD  1 
ATOM 4352 O OE1 . GLN B 2 115  ? 201.315 196.511 123.412 1.00 31.19 ? 115 GLN B OE1 1 
ATOM 4353 N NE2 . GLN B 2 115  ? 203.423 196.234 124.132 1.00 26.12 ? 115 GLN B NE2 1 
ATOM 4354 N N   . PHE B 2 116  ? 197.374 194.284 126.919 1.00 21.47 ? 116 PHE B N   1 
ATOM 4355 C CA  . PHE B 2 116  ? 195.929 194.404 126.791 1.00 17.14 ? 116 PHE B CA  1 
ATOM 4356 C C   . PHE B 2 116  ? 195.577 195.384 125.680 1.00 15.44 ? 116 PHE B C   1 
ATOM 4357 O O   . PHE B 2 116  ? 196.225 196.421 125.516 1.00 21.44 ? 116 PHE B O   1 
ATOM 4358 C CB  . PHE B 2 116  ? 195.305 194.871 128.106 1.00 25.35 ? 116 PHE B CB  1 
ATOM 4359 C CG  . PHE B 2 116  ? 195.330 193.838 129.192 1.00 22.49 ? 116 PHE B CG  1 
ATOM 4360 C CD1 . PHE B 2 116  ? 194.525 192.717 129.119 1.00 16.55 ? 116 PHE B CD1 1 
ATOM 4361 C CD2 . PHE B 2 116  ? 196.146 193.999 130.296 1.00 15.57 ? 116 PHE B CD2 1 
ATOM 4362 C CE1 . PHE B 2 116  ? 194.544 191.770 130.120 1.00 17.98 ? 116 PHE B CE1 1 
ATOM 4363 C CE2 . PHE B 2 116  ? 196.170 193.054 131.299 1.00 14.10 ? 116 PHE B CE2 1 
ATOM 4364 C CZ  . PHE B 2 116  ? 195.368 191.939 131.211 1.00 18.58 ? 116 PHE B CZ  1 
ATOM 4365 N N   . ALA B 2 117  ? 194.524 195.047 124.930 1.00 13.85 ? 117 ALA B N   1 
ATOM 4366 C CA  . ALA B 2 117  ? 194.036 195.939 123.855 1.00 15.89 ? 117 ALA B CA  1 
ATOM 4367 C C   . ALA B 2 117  ? 192.508 195.972 123.942 1.00 13.34 ? 117 ALA B C   1 
ATOM 4368 O O   . ALA B 2 117  ? 191.910 194.892 124.111 1.00 13.61 ? 117 ALA B O   1 
ATOM 4369 C CB  . ALA B 2 117  ? 194.502 195.430 122.516 1.00 14.89 ? 117 ALA B CB  1 
ATOM 4370 N N   . VAL B 2 118  ? 191.901 197.158 123.848 1.00 6.68  ? 118 VAL B N   1 
ATOM 4371 C CA  . VAL B 2 118  ? 190.420 197.257 124.017 1.00 7.33  ? 118 VAL B CA  1 
ATOM 4372 C C   . VAL B 2 118  ? 189.759 196.189 123.140 1.00 2.60  ? 118 VAL B C   1 
ATOM 4373 O O   . VAL B 2 118  ? 189.902 196.272 121.904 1.00 7.62  ? 118 VAL B O   1 
ATOM 4374 C CB  . VAL B 2 118  ? 189.903 198.667 123.674 1.00 7.83  ? 118 VAL B CB  1 
ATOM 4375 C CG1 . VAL B 2 118  ? 188.386 198.701 123.565 1.00 0.00  ? 118 VAL B CG1 1 
ATOM 4376 C CG2 . VAL B 2 118  ? 190.394 199.704 124.672 1.00 11.96 ? 118 VAL B CG2 1 
ATOM 4377 N N   . GLY B 2 119  ? 189.071 195.225 123.759 1.00 1.36  ? 119 GLY B N   1 
ATOM 4378 C CA  . GLY B 2 119  ? 188.366 194.178 122.994 1.00 6.49  ? 119 GLY B CA  1 
ATOM 4379 C C   . GLY B 2 119  ? 186.945 194.600 122.674 1.00 0.69  ? 119 GLY B C   1 
ATOM 4380 O O   . GLY B 2 119  ? 186.496 194.346 121.539 1.00 10.39 ? 119 GLY B O   1 
ATOM 4381 N N   . TRP B 2 120  ? 186.262 195.225 123.638 1.00 0.00  ? 120 TRP B N   1 
ATOM 4382 C CA  . TRP B 2 120  ? 184.879 195.716 123.408 1.00 0.00  ? 120 TRP B CA  1 
ATOM 4383 C C   . TRP B 2 120  ? 184.641 196.986 124.226 1.00 2.03  ? 120 TRP B C   1 
ATOM 4384 O O   . TRP B 2 120  ? 185.248 197.121 125.307 1.00 10.54 ? 120 TRP B O   1 
ATOM 4385 C CB  . TRP B 2 120  ? 183.854 194.635 123.773 1.00 1.06  ? 120 TRP B CB  1 
ATOM 4386 C CG  . TRP B 2 120  ? 182.429 195.062 123.540 1.00 4.98  ? 120 TRP B CG  1 
ATOM 4387 C CD1 . TRP B 2 120  ? 181.742 195.016 122.363 1.00 7.01  ? 120 TRP B CD1 1 
ATOM 4388 C CD2 . TRP B 2 120  ? 181.519 195.617 124.514 1.00 1.07  ? 120 TRP B CD2 1 
ATOM 4389 N NE1 . TRP B 2 120  ? 180.471 195.493 122.535 1.00 3.60  ? 120 TRP B NE1 1 
ATOM 4390 C CE2 . TRP B 2 120  ? 180.305 195.871 123.841 1.00 4.20  ? 120 TRP B CE2 1 
ATOM 4391 C CE3 . TRP B 2 120  ? 181.611 195.921 125.876 1.00 0.05  ? 120 TRP B CE3 1 
ATOM 4392 C CZ2 . TRP B 2 120  ? 179.196 196.411 124.487 1.00 2.93  ? 120 TRP B CZ2 1 
ATOM 4393 C CZ3 . TRP B 2 120  ? 180.513 196.454 126.513 1.00 3.19  ? 120 TRP B CZ3 1 
ATOM 4394 C CH2 . TRP B 2 120  ? 179.324 196.696 125.827 1.00 0.00  ? 120 TRP B CH2 1 
ATOM 4395 N N   . SER B 2 121  ? 183.787 197.883 123.725 1.00 3.56  ? 121 SER B N   1 
ATOM 4396 C CA  . SER B 2 121  ? 183.454 199.126 124.468 1.00 3.38  ? 121 SER B CA  1 
ATOM 4397 C C   . SER B 2 121  ? 182.052 199.596 124.067 1.00 11.03 ? 121 SER B C   1 
ATOM 4398 O O   . SER B 2 121  ? 181.831 199.819 122.861 1.00 13.52 ? 121 SER B O   1 
ATOM 4399 C CB  . SER B 2 121  ? 184.490 200.189 124.216 1.00 5.88  ? 121 SER B CB  1 
ATOM 4400 O OG  . SER B 2 121  ? 184.369 200.710 122.901 1.00 9.57  ? 121 SER B OG  1 
ATOM 4401 N N   . GLY B 2 122  ? 181.144 199.734 125.038 1.00 12.28 ? 122 GLY B N   1 
ATOM 4402 C CA  . GLY B 2 122  ? 179.759 200.141 124.730 1.00 9.33  ? 122 GLY B CA  1 
ATOM 4403 C C   . GLY B 2 122  ? 178.962 200.477 125.978 1.00 5.06  ? 122 GLY B C   1 
ATOM 4404 O O   . GLY B 2 122  ? 179.525 200.362 127.085 1.00 4.83  ? 122 GLY B O   1 
ATOM 4405 N N   . SER B 2 123  ? 177.700 200.883 125.807 1.00 3.29  ? 123 SER B N   1 
ATOM 4406 C CA  . SER B 2 123  ? 176.824 201.220 126.960 1.00 3.54  ? 123 SER B CA  1 
ATOM 4407 C C   . SER B 2 123  ? 176.047 199.975 127.401 1.00 4.89  ? 123 SER B C   1 
ATOM 4408 O O   . SER B 2 123  ? 175.696 199.162 126.524 1.00 2.67  ? 123 SER B O   1 
ATOM 4409 C CB  . SER B 2 123  ? 175.897 202.356 126.617 1.00 10.43 ? 123 SER B CB  1 
ATOM 4410 O OG  . SER B 2 123  ? 176.633 203.529 126.305 1.00 16.73 ? 123 SER B OG  1 
ATOM 4411 N N   . LEU B 2 124  ? 175.787 199.850 128.708 1.00 12.42 ? 124 LEU B N   1 
ATOM 4412 C CA  . LEU B 2 124  ? 175.117 198.641 129.261 1.00 15.58 ? 124 LEU B CA  1 
ATOM 4413 C C   . LEU B 2 124  ? 173.777 199.042 129.885 1.00 13.74 ? 124 LEU B C   1 
ATOM 4414 O O   . LEU B 2 124  ? 173.139 198.169 130.507 1.00 10.30 ? 124 LEU B O   1 
ATOM 4415 C CB  . LEU B 2 124  ? 176.033 198.050 130.338 1.00 9.86  ? 124 LEU B CB  1 
ATOM 4416 C CG  . LEU B 2 124  ? 177.208 197.191 129.867 1.00 5.74  ? 124 LEU B CG  1 
ATOM 4417 C CD1 . LEU B 2 124  ? 178.175 197.986 129.004 1.00 8.87  ? 124 LEU B CD1 1 
ATOM 4418 C CD2 . LEU B 2 124  ? 177.946 196.608 131.061 1.00 2.37  ? 124 LEU B CD2 1 
ATOM 4419 N N   . ASN B 2 125  ? 173.367 200.304 129.731 1.00 15.60 ? 125 ASN B N   1 
ATOM 4420 C CA  . ASN B 2 125  ? 172.127 200.804 130.382 1.00 16.88 ? 125 ASN B CA  1 
ATOM 4421 C C   . ASN B 2 125  ? 170.916 200.452 129.514 1.00 17.52 ? 125 ASN B C   1 
ATOM 4422 O O   . ASN B 2 125  ? 170.815 200.992 128.395 1.00 13.50 ? 125 ASN B O   1 
ATOM 4423 C CB  . ASN B 2 125  ? 172.192 202.309 130.648 1.00 14.79 ? 125 ASN B CB  1 
ATOM 4424 C CG  . ASN B 2 125  ? 172.698 203.089 129.454 1.00 17.73 ? 125 ASN B CG  1 
ATOM 4425 O OD1 . ASN B 2 125  ? 173.833 202.901 129.022 1.00 17.88 ? 125 ASN B OD1 1 
ATOM 4426 N ND2 . ASN B 2 125  ? 171.864 203.961 128.912 1.00 18.88 ? 125 ASN B ND2 1 
ATOM 4427 N N   . VAL B 2 126  ? 170.037 199.575 130.007 1.00 21.68 ? 126 VAL B N   1 
ATOM 4428 C CA  . VAL B 2 126  ? 168.828 199.242 129.269 1.00 29.44 ? 126 VAL B CA  1 
ATOM 4429 C C   . VAL B 2 126  ? 167.682 200.180 129.625 1.00 25.83 ? 126 VAL B C   1 
ATOM 4430 O O   . VAL B 2 126  ? 166.914 200.586 128.754 1.00 24.40 ? 126 VAL B O   1 
ATOM 4431 C CB  . VAL B 2 126  ? 168.440 197.768 129.521 1.00 27.01 ? 126 VAL B CB  1 
ATOM 4432 C CG1 . VAL B 2 126  ? 167.272 197.363 128.635 1.00 24.33 ? 126 VAL B CG1 1 
ATOM 4433 C CG2 . VAL B 2 126  ? 169.634 196.858 129.282 1.00 24.76 ? 126 VAL B CG2 1 
ATOM 4434 N N   . GLU B 2 127  ? 167.562 200.539 130.899 1.00 19.34 ? 127 GLU B N   1 
ATOM 4435 C CA  . GLU B 2 127  ? 166.536 201.464 131.349 1.00 23.11 ? 127 GLU B CA  1 
ATOM 4436 C C   . GLU B 2 127  ? 167.079 202.891 131.283 1.00 22.64 ? 127 GLU B C   1 
ATOM 4437 O O   . GLU B 2 127  ? 168.148 203.147 130.722 1.00 19.53 ? 127 GLU B O   1 
ATOM 4438 C CB  . GLU B 2 127  ? 166.071 201.093 132.756 1.00 27.86 ? 127 GLU B CB  1 
ATOM 4439 C CG  . GLU B 2 127  ? 165.561 199.665 132.899 1.00 26.64 ? 127 GLU B CG  1 
ATOM 4440 C CD  . GLU B 2 127  ? 164.759 199.201 131.699 1.00 26.50 ? 127 GLU B CD  1 
ATOM 4441 O OE1 . GLU B 2 127  ? 163.624 199.687 131.515 1.00 24.45 ? 127 GLU B OE1 1 
ATOM 4442 O OE2 . GLU B 2 127  ? 165.262 198.345 130.942 1.00 24.49 ? 127 GLU B OE2 1 
ATOM 4443 N N   . GLU B 2 128  ? 166.345 203.837 131.861 1.00 22.16 ? 128 GLU B N   1 
ATOM 4444 C CA  . GLU B 2 128  ? 166.740 205.239 131.895 1.00 23.34 ? 128 GLU B CA  1 
ATOM 4445 C C   . GLU B 2 128  ? 167.180 205.604 133.305 1.00 22.06 ? 128 GLU B C   1 
ATOM 4446 O O   . GLU B 2 128  ? 166.466 205.325 134.273 1.00 23.19 ? 128 GLU B O   1 
ATOM 4447 C CB  . GLU B 2 128  ? 165.590 206.141 131.445 1.00 23.57 ? 128 GLU B CB  1 
ATOM 4448 C CG  . GLU B 2 128  ? 165.790 207.609 131.765 1.00 19.87 ? 128 GLU B CG  1 
ATOM 4449 C CD  . GLU B 2 128  ? 165.211 208.517 130.701 1.00 22.82 ? 128 GLU B CD  1 
ATOM 4450 O OE1 . GLU B 2 128  ? 165.470 208.270 129.504 1.00 22.09 ? 128 GLU B OE1 1 
ATOM 4451 O OE2 . GLU B 2 128  ? 164.495 209.475 131.060 1.00 23.77 ? 128 GLU B OE2 1 
ATOM 4452 N N   . GLY B 2 129  ? 168.347 206.233 133.417 1.00 18.47 ? 129 GLY B N   1 
ATOM 4453 C CA  . GLY B 2 129  ? 168.916 206.528 134.715 1.00 18.28 ? 129 GLY B CA  1 
ATOM 4454 C C   . GLY B 2 129  ? 169.611 205.364 135.378 1.00 20.28 ? 129 GLY B C   1 
ATOM 4455 O O   . GLY B 2 129  ? 170.009 205.481 136.542 1.00 18.17 ? 129 GLY B O   1 
ATOM 4456 N N   . GLU B 2 130  ? 169.769 204.246 134.675 1.00 21.56 ? 130 GLU B N   1 
ATOM 4457 C CA  . GLU B 2 130  ? 170.397 203.058 135.235 1.00 16.88 ? 130 GLU B CA  1 
ATOM 4458 C C   . GLU B 2 130  ? 171.913 203.202 135.198 1.00 15.32 ? 130 GLU B C   1 
ATOM 4459 O O   . GLU B 2 130  ? 172.488 203.528 134.155 1.00 16.04 ? 130 GLU B O   1 
ATOM 4460 C CB  . GLU B 2 130  ? 169.958 201.822 134.451 1.00 15.70 ? 130 GLU B CB  1 
ATOM 4461 C CG  . GLU B 2 130  ? 170.332 200.494 135.073 1.00 11.89 ? 130 GLU B CG  1 
ATOM 4462 C CD  . GLU B 2 130  ? 169.724 199.322 134.323 1.00 20.95 ? 130 GLU B CD  1 
ATOM 4463 O OE1 . GLU B 2 130  ? 170.022 199.162 133.121 1.00 22.36 ? 130 GLU B OE1 1 
ATOM 4464 O OE2 . GLU B 2 130  ? 168.940 198.567 134.932 1.00 21.32 ? 130 GLU B OE2 1 
ATOM 4465 N N   . CYS B 2 131  ? 172.562 202.967 136.343 1.00 18.87 ? 131 CYS B N   1 
ATOM 4466 C CA  . CYS B 2 131  ? 174.041 203.119 136.422 1.00 20.48 ? 131 CYS B CA  1 
ATOM 4467 C C   . CYS B 2 131  ? 174.655 201.888 137.097 1.00 23.76 ? 131 CYS B C   1 
ATOM 4468 O O   . CYS B 2 131  ? 173.974 201.283 137.943 1.00 16.41 ? 131 CYS B O   1 
ATOM 4469 C CB  . CYS B 2 131  ? 174.414 204.369 137.210 1.00 15.01 ? 131 CYS B CB  1 
ATOM 4470 S SG  . CYS B 2 131  ? 173.888 205.908 136.413 1.00 28.19 ? 131 CYS B SG  1 
ATOM 4471 N N   . VAL B 2 132  ? 175.896 201.534 136.751 1.00 24.52 ? 132 VAL B N   1 
ATOM 4472 C CA  . VAL B 2 132  ? 176.530 200.301 137.312 1.00 10.12 ? 132 VAL B CA  1 
ATOM 4473 C C   . VAL B 2 132  ? 176.966 200.562 138.760 1.00 4.61  ? 132 VAL B C   1 
ATOM 4474 O O   . VAL B 2 132  ? 177.202 201.739 139.100 1.00 9.29  ? 132 VAL B O   1 
ATOM 4475 C CB  . VAL B 2 132  ? 177.712 199.832 136.440 1.00 5.60  ? 132 VAL B CB  1 
ATOM 4476 C CG1 . VAL B 2 132  ? 177.290 199.615 134.995 1.00 2.98  ? 132 VAL B CG1 1 
ATOM 4477 C CG2 . VAL B 2 132  ? 178.889 200.792 136.514 1.00 9.08  ? 132 VAL B CG2 1 
ATOM 4478 N N   . THR B 2 133  ? 177.057 199.507 139.580 1.00 2.05  ? 133 THR B N   1 
ATOM 4479 C CA  . THR B 2 133  ? 177.520 199.658 140.989 1.00 10.28 ? 133 THR B CA  1 
ATOM 4480 C C   . THR B 2 133  ? 178.692 198.703 141.263 1.00 14.69 ? 133 THR B C   1 
ATOM 4481 O O   . THR B 2 133  ? 179.362 198.898 142.297 1.00 10.78 ? 133 THR B O   1 
ATOM 4482 C CB  . THR B 2 133  ? 176.368 199.477 141.993 1.00 7.11  ? 133 THR B CB  1 
ATOM 4483 O OG1 . THR B 2 133  ? 175.810 198.176 141.807 1.00 8.10  ? 133 THR B OG1 1 
ATOM 4484 C CG2 . THR B 2 133  ? 175.287 200.524 141.842 1.00 9.99  ? 133 THR B CG2 1 
ATOM 4485 N N   . SER B 2 134  ? 178.941 197.734 140.373 1.00 15.56 ? 134 SER B N   1 
ATOM 4486 C CA  . SER B 2 134  ? 180.061 196.772 140.568 1.00 7.50  ? 134 SER B CA  1 
ATOM 4487 C C   . SER B 2 134  ? 180.307 195.938 139.306 1.00 7.76  ? 134 SER B C   1 
ATOM 4488 O O   . SER B 2 134  ? 179.431 195.940 138.419 1.00 0.00  ? 134 SER B O   1 
ATOM 4489 C CB  . SER B 2 134  ? 179.800 195.881 141.753 1.00 0.00  ? 134 SER B CB  1 
ATOM 4490 O OG  . SER B 2 134  ? 178.435 195.497 141.795 1.00 0.00  ? 134 SER B OG  1 
ATOM 4491 N N   . ALA B 2 135  ? 181.453 195.248 139.239 1.00 12.41 ? 135 ALA B N   1 
ATOM 4492 C CA  . ALA B 2 135  ? 181.760 194.398 138.097 1.00 0.00  ? 135 ALA B CA  1 
ATOM 4493 C C   . ALA B 2 135  ? 182.566 193.208 138.595 1.00 0.00  ? 135 ALA B C   1 
ATOM 4494 O O   . ALA B 2 135  ? 183.143 193.242 139.684 1.00 0.00  ? 135 ALA B O   1 
ATOM 4495 C CB  . ALA B 2 135  ? 182.524 195.159 137.010 1.00 0.00  ? 135 ALA B CB  1 
ATOM 4496 N N   . LEU B 2 136  ? 182.537 192.127 137.804 1.00 1.21  ? 136 LEU B N   1 
ATOM 4497 C CA  . LEU B 2 136  ? 183.221 190.873 138.218 1.00 1.52  ? 136 LEU B CA  1 
ATOM 4498 C C   . LEU B 2 136  ? 183.616 190.056 136.984 1.00 0.00  ? 136 LEU B C   1 
ATOM 4499 O O   . LEU B 2 136  ? 182.801 189.982 136.046 1.00 0.00  ? 136 LEU B O   1 
ATOM 4500 C CB  . LEU B 2 136  ? 182.269 190.072 139.111 1.00 2.16  ? 136 LEU B CB  1 
ATOM 4501 C CG  . LEU B 2 136  ? 182.932 189.267 140.228 1.00 2.18  ? 136 LEU B CG  1 
ATOM 4502 C CD1 . LEU B 2 136  ? 183.659 190.186 141.197 1.00 0.00  ? 136 LEU B CD1 1 
ATOM 4503 C CD2 . LEU B 2 136  ? 181.905 188.423 140.966 1.00 0.00  ? 136 LEU B CD2 1 
ATOM 4504 N N   . CYS B 2 137  ? 184.813 189.467 136.992 1.00 0.00  ? 137 CYS B N   1 
ATOM 4505 C CA  . CYS B 2 137  ? 185.309 188.629 135.905 1.00 0.00  ? 137 CYS B CA  1 
ATOM 4506 C C   . CYS B 2 137  ? 185.666 187.261 136.473 1.00 0.74  ? 137 CYS B C   1 
ATOM 4507 O O   . CYS B 2 137  ? 186.691 187.112 137.146 1.00 0.00  ? 137 CYS B O   1 
ATOM 4508 C CB  . CYS B 2 137  ? 186.517 189.269 135.228 1.00 0.09  ? 137 CYS B CB  1 
ATOM 4509 S SG  . CYS B 2 137  ? 186.104 190.277 133.801 1.00 17.52 ? 137 CYS B SG  1 
ATOM 4510 N N   . ILE B 2 138  ? 184.832 186.266 136.194 1.00 2.20  ? 138 ILE B N   1 
ATOM 4511 C CA  . ILE B 2 138  ? 184.974 184.925 136.747 1.00 1.70  ? 138 ILE B CA  1 
ATOM 4512 C C   . ILE B 2 138  ? 185.433 183.998 135.624 1.00 7.20  ? 138 ILE B C   1 
ATOM 4513 O O   . ILE B 2 138  ? 184.688 183.788 134.657 1.00 13.65 ? 138 ILE B O   1 
ATOM 4514 C CB  . ILE B 2 138  ? 183.659 184.428 137.362 1.00 0.59  ? 138 ILE B CB  1 
ATOM 4515 C CG1 . ILE B 2 138  ? 183.235 185.318 138.528 1.00 0.00  ? 138 ILE B CG1 1 
ATOM 4516 C CG2 . ILE B 2 138  ? 183.791 182.982 137.804 1.00 1.72  ? 138 ILE B CG2 1 
ATOM 4517 C CD1 . ILE B 2 138  ? 181.750 185.287 138.786 1.00 0.00  ? 138 ILE B CD1 1 
ATOM 4518 N N   . PRO B 2 139  ? 186.635 183.432 135.694 1.00 1.79  ? 139 PRO B N   1 
ATOM 4519 C CA  . PRO B 2 139  ? 186.985 182.352 134.767 1.00 1.25  ? 139 PRO B CA  1 
ATOM 4520 C C   . PRO B 2 139  ? 186.177 181.101 135.066 1.00 0.00  ? 139 PRO B C   1 
ATOM 4521 O O   . PRO B 2 139  ? 185.754 180.862 136.199 1.00 8.09  ? 139 PRO B O   1 
ATOM 4522 C CB  . PRO B 2 139  ? 188.480 182.128 135.022 1.00 0.00  ? 139 PRO B CB  1 
ATOM 4523 C CG  . PRO B 2 139  ? 188.718 182.655 136.380 1.00 0.00  ? 139 PRO B CG  1 
ATOM 4524 C CD  . PRO B 2 139  ? 187.750 183.780 136.588 1.00 0.00  ? 139 PRO B CD  1 
ATOM 4525 N N   . LEU B 2 140  ? 185.954 180.301 134.029 1.00 0.00  ? 140 LEU B N   1 
ATOM 4526 C CA  . LEU B 2 140  ? 185.189 179.067 134.141 1.00 0.00  ? 140 LEU B CA  1 
ATOM 4527 C C   . LEU B 2 140  ? 186.081 177.894 133.766 1.00 9.68  ? 140 LEU B C   1 
ATOM 4528 O O   . LEU B 2 140  ? 186.685 177.891 132.689 1.00 14.79 ? 140 LEU B O   1 
ATOM 4529 C CB  . LEU B 2 140  ? 183.957 179.094 133.236 1.00 2.48  ? 140 LEU B CB  1 
ATOM 4530 C CG  . LEU B 2 140  ? 182.672 179.735 133.762 1.00 4.47  ? 140 LEU B CG  1 
ATOM 4531 C CD1 . LEU B 2 140  ? 182.207 179.061 135.037 1.00 4.33  ? 140 LEU B CD1 1 
ATOM 4532 C CD2 . LEU B 2 140  ? 182.844 181.229 133.969 1.00 4.33  ? 140 LEU B CD2 1 
ATOM 4533 N N   . ALA B 2 141  ? 186.160 176.903 134.647 1.00 10.07 ? 141 ALA B N   1 
ATOM 4534 C CA  . ALA B 2 141  ? 186.981 175.737 134.374 1.00 4.58  ? 141 ALA B CA  1 
ATOM 4535 C C   . ALA B 2 141  ? 186.322 174.849 133.325 1.00 11.75 ? 141 ALA B C   1 
ATOM 4536 O O   . ALA B 2 141  ? 185.097 174.800 133.190 1.00 13.36 ? 141 ALA B O   1 
ATOM 4537 C CB  . ALA B 2 141  ? 187.233 174.940 135.652 1.00 6.43  ? 141 ALA B CB  1 
ATOM 4538 N N   . SER B 2 142  ? 187.161 174.132 132.582 1.00 27.27 ? 142 SER B N   1 
ATOM 4539 C CA  . SER B 2 142  ? 186.688 173.293 131.491 1.00 27.84 ? 142 SER B CA  1 
ATOM 4540 C C   . SER B 2 142  ? 186.347 171.898 131.998 1.00 24.89 ? 142 SER B C   1 
ATOM 4541 O O   . SER B 2 142  ? 187.101 171.309 132.779 1.00 26.11 ? 142 SER B O   1 
ATOM 4542 C CB  . SER B 2 142  ? 187.745 173.207 130.391 1.00 25.41 ? 142 SER B CB  1 
ATOM 4543 O OG  . SER B 2 142  ? 187.402 172.220 129.434 1.00 15.38 ? 142 SER B OG  1 
ATOM 4544 N N   . GLN B 2 143  ? 185.212 171.370 131.545 1.00 23.68 ? 143 GLN B N   1 
ATOM 4545 C CA  . GLN B 2 143  ? 184.809 170.009 131.867 1.00 28.88 ? 143 GLN B CA  1 
ATOM 4546 C C   . GLN B 2 143  ? 185.448 168.971 130.955 1.00 33.15 ? 143 GLN B C   1 
ATOM 4547 O O   . GLN B 2 143  ? 185.218 167.773 131.149 1.00 34.89 ? 143 GLN B O   1 
ATOM 4548 C CB  . GLN B 2 143  ? 183.285 169.876 131.794 1.00 29.39 ? 143 GLN B CB  1 
ATOM 4549 C CG  . GLN B 2 143  ? 182.566 170.246 133.077 1.00 31.23 ? 143 GLN B CG  1 
ATOM 4550 C CD  . GLN B 2 143  ? 181.665 169.135 133.574 1.00 31.91 ? 143 GLN B CD  1 
ATOM 4551 O OE1 . GLN B 2 143  ? 180.980 168.479 132.789 1.00 25.90 ? 143 GLN B OE1 1 
ATOM 4552 N NE2 . GLN B 2 143  ? 181.661 168.917 134.883 1.00 31.85 ? 143 GLN B NE2 1 
ATOM 4553 N N   . LYS B 2 144  ? 186.243 169.399 129.976 1.00 34.31 ? 144 LYS B N   1 
ATOM 4554 C CA  . LYS B 2 144  ? 186.860 168.508 129.005 1.00 33.29 ? 144 LYS B CA  1 
ATOM 4555 C C   . LYS B 2 144  ? 188.189 167.938 129.481 1.00 33.24 ? 144 LYS B C   1 
ATOM 4556 O O   . LYS B 2 144  ? 188.856 167.243 128.705 1.00 33.37 ? 144 LYS B O   1 
ATOM 4557 C CB  . LYS B 2 144  ? 187.057 169.240 127.675 1.00 29.19 ? 144 LYS B CB  1 
ATOM 4558 C CG  . LYS B 2 144  ? 185.823 169.978 127.183 1.00 31.88 ? 144 LYS B CG  1 
ATOM 4559 C CD  . LYS B 2 144  ? 186.191 171.048 126.168 1.00 32.71 ? 144 LYS B CD  1 
ATOM 4560 C CE  . LYS B 2 144  ? 185.288 172.263 126.290 1.00 28.70 ? 144 LYS B CE  1 
ATOM 4561 N NZ  . LYS B 2 144  ? 185.615 173.294 125.269 1.00 31.10 ? 144 LYS B NZ  1 
ATOM 4562 N N   . ARG B 2 145  ? 188.578 168.217 130.724 1.00 31.42 ? 145 ARG B N   1 
ATOM 4563 C CA  . ARG B 2 145  ? 189.852 167.768 131.284 1.00 33.02 ? 145 ARG B CA  1 
ATOM 4564 C C   . ARG B 2 145  ? 191.021 168.268 130.438 1.00 35.80 ? 145 ARG B C   1 
ATOM 4565 O O   . ARG B 2 145  ? 191.985 167.551 130.162 1.00 33.34 ? 145 ARG B O   1 
ATOM 4566 C CB  . ARG B 2 145  ? 189.883 166.245 131.421 1.00 33.36 ? 145 ARG B CB  1 
ATOM 4567 C CG  . ARG B 2 145  ? 188.806 165.681 132.334 1.00 33.70 ? 145 ARG B CG  1 
ATOM 4568 C CD  . ARG B 2 145  ? 189.179 165.794 133.805 1.00 35.68 ? 145 ARG B CD  1 
ATOM 4569 N NE  . ARG B 2 145  ? 190.468 165.180 134.098 1.00 34.71 ? 145 ARG B NE  1 
ATOM 4570 C CZ  . ARG B 2 145  ? 190.953 165.006 135.319 1.00 31.97 ? 145 ARG B CZ  1 
ATOM 4571 N NH1 . ARG B 2 145  ? 190.274 165.377 136.392 1.00 28.29 ? 145 ARG B NH1 1 
ATOM 4572 N NH2 . ARG B 2 145  ? 192.147 164.441 135.469 1.00 33.09 ? 145 ARG B NH2 1 
ATOM 4573 N N   . SER B 2 146  ? 190.922 169.529 130.023 1.00 37.64 ? 146 SER B N   1 
ATOM 4574 C CA  . SER B 2 146  ? 191.937 170.140 129.174 1.00 33.39 ? 146 SER B CA  1 
ATOM 4575 C C   . SER B 2 146  ? 193.182 170.442 129.999 1.00 33.57 ? 146 SER B C   1 
ATOM 4576 O O   . SER B 2 146  ? 193.144 171.278 130.909 1.00 33.05 ? 146 SER B O   1 
ATOM 4577 C CB  . SER B 2 146  ? 191.394 171.413 128.530 1.00 30.77 ? 146 SER B CB  1 
ATOM 4578 O OG  . SER B 2 146  ? 191.051 172.376 129.513 1.00 28.91 ? 146 SER B OG  1 
ATOM 4579 N N   . SER B 2 147  ? 194.285 169.762 129.679 1.00 28.75 ? 147 SER B N   1 
ATOM 4580 C CA  . SER B 2 147  ? 195.524 169.976 130.419 1.00 31.89 ? 147 SER B CA  1 
ATOM 4581 C C   . SER B 2 147  ? 196.089 171.368 130.163 1.00 30.89 ? 147 SER B C   1 
ATOM 4582 O O   . SER B 2 147  ? 196.831 171.907 130.992 1.00 26.03 ? 147 SER B O   1 
ATOM 4583 C CB  . SER B 2 147  ? 196.548 168.902 130.049 1.00 30.34 ? 147 SER B CB  1 
ATOM 4584 O OG  . SER B 2 147  ? 197.297 169.281 128.907 1.00 28.42 ? 147 SER B OG  1 
ATOM 4585 N N   . THR B 2 148  ? 195.758 171.961 129.019 1.00 29.26 ? 148 THR B N   1 
ATOM 4586 C CA  . THR B 2 148  ? 196.242 173.299 128.706 1.00 31.69 ? 148 THR B CA  1 
ATOM 4587 C C   . THR B 2 148  ? 195.542 174.339 129.572 1.00 27.57 ? 148 THR B C   1 
ATOM 4588 O O   . THR B 2 148  ? 194.416 174.135 130.033 1.00 26.61 ? 148 THR B O   1 
ATOM 4589 C CB  . THR B 2 148  ? 196.021 173.611 127.226 1.00 27.06 ? 148 THR B CB  1 
ATOM 4590 O OG1 . THR B 2 148  ? 194.633 173.457 126.904 1.00 26.30 ? 148 THR B OG1 1 
ATOM 4591 C CG2 . THR B 2 148  ? 196.845 172.671 126.358 1.00 25.80 ? 148 THR B CG2 1 
ATOM 4592 N N   . GLY B 2 149  ? 196.219 175.464 129.791 1.00 24.24 ? 149 GLY B N   1 
ATOM 4593 C CA  . GLY B 2 149  ? 195.673 176.528 130.609 1.00 27.78 ? 149 GLY B CA  1 
ATOM 4594 C C   . GLY B 2 149  ? 194.683 177.403 129.872 1.00 27.47 ? 149 GLY B C   1 
ATOM 4595 O O   . GLY B 2 149  ? 194.888 178.614 129.740 1.00 22.02 ? 149 GLY B O   1 
ATOM 4596 N N   . ARG B 2 150  ? 193.600 176.799 129.388 1.00 27.01 ? 150 ARG B N   1 
ATOM 4597 C CA  . ARG B 2 150  ? 192.553 177.528 128.682 1.00 26.24 ? 150 ARG B CA  1 
ATOM 4598 C C   . ARG B 2 150  ? 191.228 177.336 129.402 1.00 27.42 ? 150 ARG B C   1 
ATOM 4599 O O   . ARG B 2 150  ? 190.529 176.340 129.159 1.00 24.51 ? 150 ARG B O   1 
ATOM 4600 C CB  . ARG B 2 150  ? 192.444 177.057 127.228 1.00 23.02 ? 150 ARG B CB  1 
ATOM 4601 C CG  . ARG B 2 150  ? 191.424 177.831 126.400 1.00 22.31 ? 150 ARG B CG  1 
ATOM 4602 C CD  . ARG B 2 150  ? 191.373 177.330 124.963 1.00 26.56 ? 150 ARG B CD  1 
ATOM 4603 N NE  . ARG B 2 150  ? 190.471 178.123 124.134 1.00 33.01 ? 150 ARG B NE  1 
ATOM 4604 C CZ  . ARG B 2 150  ? 189.178 177.874 123.982 1.00 27.95 ? 150 ARG B CZ  1 
ATOM 4605 N NH1 . ARG B 2 150  ? 188.593 176.856 124.591 1.00 25.64 ? 150 ARG B NH1 1 
ATOM 4606 N NH2 . ARG B 2 150  ? 188.452 178.667 123.198 1.00 19.99 ? 150 ARG B NH2 1 
ATOM 4607 N N   . PRO B 2 151  ? 190.841 178.238 130.300 1.00 22.09 ? 151 PRO B N   1 
ATOM 4608 C CA  . PRO B 2 151  ? 189.471 178.203 130.818 1.00 17.75 ? 151 PRO B CA  1 
ATOM 4609 C C   . PRO B 2 151  ? 188.486 178.447 129.687 1.00 20.74 ? 151 PRO B C   1 
ATOM 4610 O O   . PRO B 2 151  ? 188.825 179.049 128.666 1.00 25.67 ? 151 PRO B O   1 
ATOM 4611 C CB  . PRO B 2 151  ? 189.448 179.333 131.855 1.00 12.30 ? 151 PRO B CB  1 
ATOM 4612 C CG  . PRO B 2 151  ? 190.601 180.209 131.503 1.00 11.43 ? 151 PRO B CG  1 
ATOM 4613 C CD  . PRO B 2 151  ? 191.642 179.303 130.925 1.00 15.98 ? 151 PRO B CD  1 
ATOM 4614 N N   . ASP B 2 152  ? 187.264 177.933 129.847 1.00 15.12 ? 152 ASP B N   1 
ATOM 4615 C CA  . ASP B 2 152  ? 186.252 178.055 128.764 1.00 14.41 ? 152 ASP B CA  1 
ATOM 4616 C C   . ASP B 2 152  ? 186.044 179.531 128.415 1.00 8.51  ? 152 ASP B C   1 
ATOM 4617 O O   . ASP B 2 152  ? 186.137 179.864 127.217 1.00 13.91 ? 152 ASP B O   1 
ATOM 4618 C CB  . ASP B 2 152  ? 184.935 177.383 129.161 1.00 13.77 ? 152 ASP B CB  1 
ATOM 4619 C CG  . ASP B 2 152  ? 185.051 175.877 129.315 1.00 15.71 ? 152 ASP B CG  1 
ATOM 4620 O OD1 . ASP B 2 152  ? 185.826 175.270 128.550 1.00 17.16 ? 152 ASP B OD1 1 
ATOM 4621 O OD2 . ASP B 2 152  ? 184.363 175.325 130.195 1.00 18.03 ? 152 ASP B OD2 1 
ATOM 4622 N N   . TRP B 2 153  ? 185.785 180.375 129.418 1.00 0.49  ? 153 TRP B N   1 
ATOM 4623 C CA  . TRP B 2 153  ? 185.504 181.782 129.172 1.00 0.00  ? 153 TRP B CA  1 
ATOM 4624 C C   . TRP B 2 153  ? 185.462 182.509 130.506 1.00 11.81 ? 153 TRP B C   1 
ATOM 4625 O O   . TRP B 2 153  ? 185.388 181.878 131.564 1.00 20.04 ? 153 TRP B O   1 
ATOM 4626 C CB  . TRP B 2 153  ? 184.185 181.970 128.409 1.00 1.40  ? 153 TRP B CB  1 
ATOM 4627 C CG  . TRP B 2 153  ? 182.978 181.355 129.065 1.00 8.83  ? 153 TRP B CG  1 
ATOM 4628 C CD1 . TRP B 2 153  ? 182.802 180.043 129.400 1.00 3.04  ? 153 TRP B CD1 1 
ATOM 4629 C CD2 . TRP B 2 153  ? 181.767 182.026 129.433 1.00 11.56 ? 153 TRP B CD2 1 
ATOM 4630 N NE1 . TRP B 2 153  ? 181.565 179.860 129.966 1.00 0.00  ? 153 TRP B NE1 1 
ATOM 4631 C CE2 . TRP B 2 153  ? 180.909 181.061 129.997 1.00 4.59  ? 153 TRP B CE2 1 
ATOM 4632 C CE3 . TRP B 2 153  ? 181.327 183.350 129.344 1.00 7.57  ? 153 TRP B CE3 1 
ATOM 4633 C CZ2 . TRP B 2 153  ? 179.641 181.378 130.470 1.00 8.28  ? 153 TRP B CZ2 1 
ATOM 4634 C CZ3 . TRP B 2 153  ? 180.067 183.662 129.815 1.00 1.16  ? 153 TRP B CZ3 1 
ATOM 4635 C CH2 . TRP B 2 153  ? 179.239 182.681 130.371 1.00 9.40  ? 153 TRP B CH2 1 
ATOM 4636 N N   . THR B 2 154  ? 185.522 183.838 130.445 1.00 8.11  ? 154 THR B N   1 
ATOM 4637 C CA  . THR B 2 154  ? 185.471 184.678 131.640 1.00 0.16  ? 154 THR B CA  1 
ATOM 4638 C C   . THR B 2 154  ? 184.163 185.458 131.625 1.00 1.39  ? 154 THR B C   1 
ATOM 4639 O O   . THR B 2 154  ? 184.049 186.487 130.957 1.00 3.68  ? 154 THR B O   1 
ATOM 4640 C CB  . THR B 2 154  ? 186.669 185.618 131.693 1.00 0.00  ? 154 THR B CB  1 
ATOM 4641 O OG1 . THR B 2 154  ? 186.751 186.351 130.466 1.00 5.79  ? 154 THR B OG1 1 
ATOM 4642 C CG2 . THR B 2 154  ? 187.944 184.829 131.875 1.00 0.00  ? 154 THR B CG2 1 
ATOM 4643 N N   . CYS B 2 155  ? 183.171 184.971 132.366 1.00 0.00  ? 155 CYS B N   1 
ATOM 4644 C CA  . CYS B 2 155  ? 181.886 185.651 132.429 1.00 0.00  ? 155 CYS B CA  1 
ATOM 4645 C C   . CYS B 2 155  ? 182.011 186.975 133.170 1.00 1.74  ? 155 CYS B C   1 
ATOM 4646 O O   . CYS B 2 155  ? 182.811 187.117 134.097 1.00 4.49  ? 155 CYS B O   1 
ATOM 4647 C CB  . CYS B 2 155  ? 180.847 184.780 133.127 1.00 0.00  ? 155 CYS B CB  1 
ATOM 4648 S SG  . CYS B 2 155  ? 179.211 185.535 133.159 1.00 3.17  ? 155 CYS B SG  1 
ATOM 4649 N N   . ILE B 2 156  ? 181.199 187.948 132.763 1.00 0.24  ? 156 ILE B N   1 
ATOM 4650 C CA  . ILE B 2 156  ? 181.207 189.276 133.364 1.00 0.00  ? 156 ILE B CA  1 
ATOM 4651 C C   . ILE B 2 156  ? 179.886 189.472 134.088 1.00 0.00  ? 156 ILE B C   1 
ATOM 4652 O O   . ILE B 2 156  ? 178.821 189.455 133.460 1.00 2.47  ? 156 ILE B O   1 
ATOM 4653 C CB  . ILE B 2 156  ? 181.420 190.376 132.316 1.00 0.00  ? 156 ILE B CB  1 
ATOM 4654 C CG1 . ILE B 2 156  ? 182.834 190.302 131.753 1.00 0.00  ? 156 ILE B CG1 1 
ATOM 4655 C CG2 . ILE B 2 156  ? 181.172 191.730 132.927 1.00 0.00  ? 156 ILE B CG2 1 
ATOM 4656 C CD1 . ILE B 2 156  ? 182.899 189.578 130.450 1.00 0.00  ? 156 ILE B CD1 1 
ATOM 4657 N N   . VAL B 2 157  ? 179.959 189.672 135.401 1.00 0.00  ? 157 VAL B N   1 
ATOM 4658 C CA  . VAL B 2 157  ? 178.791 189.848 136.256 1.00 0.00  ? 157 VAL B CA  1 
ATOM 4659 C C   . VAL B 2 157  ? 178.758 191.300 136.707 1.00 9.93  ? 157 VAL B C   1 
ATOM 4660 O O   . VAL B 2 157  ? 179.692 191.772 137.365 1.00 24.11 ? 157 VAL B O   1 
ATOM 4661 C CB  . VAL B 2 157  ? 178.833 188.902 137.463 1.00 0.00  ? 157 VAL B CB  1 
ATOM 4662 C CG1 . VAL B 2 157  ? 177.511 188.924 138.195 1.00 0.00  ? 157 VAL B CG1 1 
ATOM 4663 C CG2 . VAL B 2 157  ? 179.183 187.500 137.015 1.00 0.00  ? 157 VAL B CG2 1 
ATOM 4664 N N   . VAL B 2 158  ? 177.682 192.008 136.371 1.00 5.29  ? 158 VAL B N   1 
ATOM 4665 C CA  . VAL B 2 158  ? 177.572 193.436 136.632 1.00 2.35  ? 158 VAL B CA  1 
ATOM 4666 C C   . VAL B 2 158  ? 176.300 193.688 137.427 1.00 0.00  ? 158 VAL B C   1 
ATOM 4667 O O   . VAL B 2 158  ? 175.287 193.010 137.225 1.00 3.32  ? 158 VAL B O   1 
ATOM 4668 C CB  . VAL B 2 158  ? 177.579 194.248 135.319 1.00 0.00  ? 158 VAL B CB  1 
ATOM 4669 C CG1 . VAL B 2 158  ? 177.446 195.733 135.597 1.00 2.12  ? 158 VAL B CG1 1 
ATOM 4670 C CG2 . VAL B 2 158  ? 178.851 193.975 134.543 1.00 0.00  ? 158 VAL B CG2 1 
ATOM 4671 N N   . GLY B 2 159  ? 176.363 194.638 138.350 1.00 5.47  ? 159 GLY B N   1 
ATOM 4672 C CA  . GLY B 2 159  ? 175.208 195.035 139.141 1.00 2.62  ? 159 GLY B CA  1 
ATOM 4673 C C   . GLY B 2 159  ? 174.926 196.515 138.974 1.00 6.53  ? 159 GLY B C   1 
ATOM 4674 O O   . GLY B 2 159  ? 175.849 197.335 138.986 1.00 18.30 ? 159 GLY B O   1 
ATOM 4675 N N   . PHE B 2 160  ? 173.648 196.850 138.831 1.00 3.05  ? 160 PHE B N   1 
ATOM 4676 C CA  . PHE B 2 160  ? 173.220 198.202 138.501 1.00 9.21  ? 160 PHE B CA  1 
ATOM 4677 C C   . PHE B 2 160  ? 172.509 198.852 139.682 1.00 3.90  ? 160 PHE B C   1 
ATOM 4678 O O   . PHE B 2 160  ? 172.174 198.206 140.678 1.00 2.19  ? 160 PHE B O   1 
ATOM 4679 C CB  . PHE B 2 160  ? 172.308 198.195 137.268 1.00 14.45 ? 160 PHE B CB  1 
ATOM 4680 C CG  . PHE B 2 160  ? 172.968 197.661 136.030 1.00 9.61  ? 160 PHE B CG  1 
ATOM 4681 C CD1 . PHE B 2 160  ? 173.084 196.299 135.825 1.00 4.62  ? 160 PHE B CD1 1 
ATOM 4682 C CD2 . PHE B 2 160  ? 173.478 198.520 135.076 1.00 8.80  ? 160 PHE B CD2 1 
ATOM 4683 C CE1 . PHE B 2 160  ? 173.692 195.807 134.695 1.00 2.41  ? 160 PHE B CE1 1 
ATOM 4684 C CE2 . PHE B 2 160  ? 174.086 198.028 133.942 1.00 12.75 ? 160 PHE B CE2 1 
ATOM 4685 C CZ  . PHE B 2 160  ? 174.193 196.671 133.753 1.00 4.46  ? 160 PHE B CZ  1 
ATOM 4686 N N   . THR B 2 161  ? 172.261 200.159 139.560 1.00 0.00  ? 161 THR B N   1 
ATOM 4687 C CA  . THR B 2 161  ? 171.602 200.913 140.660 1.00 3.84  ? 161 THR B CA  1 
ATOM 4688 C C   . THR B 2 161  ? 170.115 200.550 140.729 1.00 5.58  ? 161 THR B C   1 
ATOM 4689 O O   . THR B 2 161  ? 169.545 200.625 141.832 1.00 10.74 ? 161 THR B O   1 
ATOM 4690 C CB  . THR B 2 161  ? 171.780 202.425 140.474 1.00 4.00  ? 161 THR B CB  1 
ATOM 4691 O OG1 . THR B 2 161  ? 171.618 202.719 139.086 1.00 12.14 ? 161 THR B OG1 1 
ATOM 4692 C CG2 . THR B 2 161  ? 173.126 202.922 140.951 1.00 8.95  ? 161 THR B CG2 1 
ATOM 4693 N N   . SER B 2 162  ? 169.506 200.194 139.595 1.00 7.48  ? 162 SER B N   1 
ATOM 4694 C CA  . SER B 2 162  ? 168.080 199.898 139.607 1.00 8.05  ? 162 SER B CA  1 
ATOM 4695 C C   . SER B 2 162  ? 167.752 198.603 140.332 1.00 4.15  ? 162 SER B C   1 
ATOM 4696 O O   . SER B 2 162  ? 166.596 198.407 140.722 1.00 7.30  ? 162 SER B O   1 
ATOM 4697 C CB  . SER B 2 162  ? 167.543 199.825 138.177 1.00 13.82 ? 162 SER B CB  1 
ATOM 4698 O OG  . SER B 2 162  ? 167.979 198.642 137.532 1.00 1.82  ? 162 SER B OG  1 
ATOM 4699 N N   . GLY B 2 163  ? 168.728 197.731 140.527 1.00 3.00  ? 163 GLY B N   1 
ATOM 4700 C CA  . GLY B 2 163  ? 168.510 196.431 141.109 1.00 2.23  ? 163 GLY B CA  1 
ATOM 4701 C C   . GLY B 2 163  ? 168.699 195.265 140.163 1.00 2.78  ? 163 GLY B C   1 
ATOM 4702 O O   . GLY B 2 163  ? 168.095 194.210 140.390 1.00 10.48 ? 163 GLY B O   1 
ATOM 4703 N N   . TYR B 2 164  ? 169.507 195.417 139.120 1.00 0.99  ? 164 TYR B N   1 
ATOM 4704 C CA  . TYR B 2 164  ? 169.685 194.386 138.109 1.00 4.62  ? 164 TYR B CA  1 
ATOM 4705 C C   . TYR B 2 164  ? 171.061 193.747 138.231 1.00 0.43  ? 164 TYR B C   1 
ATOM 4706 O O   . TYR B 2 164  ? 172.059 194.434 138.468 1.00 0.00  ? 164 TYR B O   1 
ATOM 4707 C CB  . TYR B 2 164  ? 169.516 194.966 136.702 1.00 5.81  ? 164 TYR B CB  1 
ATOM 4708 C CG  . TYR B 2 164  ? 168.112 194.877 136.150 1.00 2.84  ? 164 TYR B CG  1 
ATOM 4709 C CD1 . TYR B 2 164  ? 167.551 193.652 135.820 1.00 3.54  ? 164 TYR B CD1 1 
ATOM 4710 C CD2 . TYR B 2 164  ? 167.353 196.019 135.950 1.00 7.28  ? 164 TYR B CD2 1 
ATOM 4711 C CE1 . TYR B 2 164  ? 166.272 193.568 135.314 1.00 4.28  ? 164 TYR B CE1 1 
ATOM 4712 C CE2 . TYR B 2 164  ? 166.073 195.945 135.444 1.00 8.50  ? 164 TYR B CE2 1 
ATOM 4713 C CZ  . TYR B 2 164  ? 165.537 194.718 135.127 1.00 6.42  ? 164 TYR B CZ  1 
ATOM 4714 O OH  . TYR B 2 164  ? 164.260 194.644 134.622 1.00 7.19  ? 164 TYR B OH  1 
ATOM 4715 N N   . VAL B 2 165  ? 171.102 192.427 138.072 1.00 0.00  ? 165 VAL B N   1 
ATOM 4716 C CA  . VAL B 2 165  ? 172.341 191.676 137.924 1.00 0.00  ? 165 VAL B CA  1 
ATOM 4717 C C   . VAL B 2 165  ? 172.339 191.086 136.521 1.00 0.00  ? 165 VAL B C   1 
ATOM 4718 O O   . VAL B 2 165  ? 171.406 190.367 136.139 1.00 3.59  ? 165 VAL B O   1 
ATOM 4719 C CB  . VAL B 2 165  ? 172.482 190.582 138.994 1.00 2.53  ? 165 VAL B CB  1 
ATOM 4720 C CG1 . VAL B 2 165  ? 173.847 189.926 138.906 1.00 3.77  ? 165 VAL B CG1 1 
ATOM 4721 C CG2 . VAL B 2 165  ? 172.281 191.173 140.372 1.00 6.37  ? 165 VAL B CG2 1 
ATOM 4722 N N   . ARG B 2 166  ? 173.374 191.405 135.749 1.00 0.00  ? 166 ARG B N   1 
ATOM 4723 C CA  . ARG B 2 166  ? 173.442 191.042 134.343 1.00 0.47  ? 166 ARG B CA  1 
ATOM 4724 C C   . ARG B 2 166  ? 174.766 190.358 134.046 1.00 3.61  ? 166 ARG B C   1 
ATOM 4725 O O   . ARG B 2 166  ? 175.822 190.791 134.516 1.00 6.68  ? 166 ARG B O   1 
ATOM 4726 C CB  . ARG B 2 166  ? 173.276 192.270 133.449 1.00 1.64  ? 166 ARG B CB  1 
ATOM 4727 C CG  . ARG B 2 166  ? 171.932 192.954 133.600 1.00 1.16  ? 166 ARG B CG  1 
ATOM 4728 C CD  . ARG B 2 166  ? 171.705 193.979 132.509 1.00 7.00  ? 166 ARG B CD  1 
ATOM 4729 N NE  . ARG B 2 166  ? 170.315 194.413 132.452 1.00 11.52 ? 166 ARG B NE  1 
ATOM 4730 C CZ  . ARG B 2 166  ? 169.834 195.472 133.088 1.00 10.28 ? 166 ARG B CZ  1 
ATOM 4731 N NH1 . ARG B 2 166  ? 170.606 196.232 133.847 1.00 3.39  ? 166 ARG B NH1 1 
ATOM 4732 N NH2 . ARG B 2 166  ? 168.547 195.778 132.959 1.00 9.44  ? 166 ARG B NH2 1 
ATOM 4733 N N   . PHE B 2 167  ? 174.698 189.298 133.247 1.00 0.00  ? 167 PHE B N   1 
ATOM 4734 C CA  . PHE B 2 167  ? 175.840 188.460 132.911 1.00 0.00  ? 167 PHE B CA  1 
ATOM 4735 C C   . PHE B 2 167  ? 176.080 188.554 131.412 1.00 1.44  ? 167 PHE B C   1 
ATOM 4736 O O   . PHE B 2 167  ? 175.202 188.180 130.622 1.00 0.00  ? 167 PHE B O   1 
ATOM 4737 C CB  . PHE B 2 167  ? 175.596 187.004 133.321 1.00 0.17  ? 167 PHE B CB  1 
ATOM 4738 C CG  . PHE B 2 167  ? 175.242 186.822 134.775 1.00 0.74  ? 167 PHE B CG  1 
ATOM 4739 C CD1 . PHE B 2 167  ? 173.986 187.159 135.251 1.00 7.78  ? 167 PHE B CD1 1 
ATOM 4740 C CD2 . PHE B 2 167  ? 176.160 186.290 135.660 1.00 8.54  ? 167 PHE B CD2 1 
ATOM 4741 C CE1 . PHE B 2 167  ? 173.663 186.987 136.582 1.00 4.89  ? 167 PHE B CE1 1 
ATOM 4742 C CE2 . PHE B 2 167  ? 175.838 186.112 136.992 1.00 2.75  ? 167 PHE B CE2 1 
ATOM 4743 C CZ  . PHE B 2 167  ? 174.590 186.462 137.452 1.00 0.00  ? 167 PHE B CZ  1 
ATOM 4744 N N   . TYR B 2 168  ? 177.261 189.049 131.037 1.00 0.00  ? 168 TYR B N   1 
ATOM 4745 C CA  . TYR B 2 168  ? 177.725 189.153 129.660 1.00 1.20  ? 168 TYR B CA  1 
ATOM 4746 C C   . TYR B 2 168  ? 178.883 188.192 129.415 1.00 2.95  ? 168 TYR B C   1 
ATOM 4747 O O   . TYR B 2 168  ? 179.539 187.719 130.348 1.00 0.05  ? 168 TYR B O   1 
ATOM 4748 C CB  . TYR B 2 168  ? 178.211 190.570 129.316 1.00 0.83  ? 168 TYR B CB  1 
ATOM 4749 C CG  . TYR B 2 168  ? 177.300 191.733 129.653 1.00 1.84  ? 168 TYR B CG  1 
ATOM 4750 C CD1 . TYR B 2 168  ? 176.307 192.140 128.777 1.00 0.00  ? 168 TYR B CD1 1 
ATOM 4751 C CD2 . TYR B 2 168  ? 177.481 192.465 130.816 1.00 0.00  ? 168 TYR B CD2 1 
ATOM 4752 C CE1 . TYR B 2 168  ? 175.495 193.212 129.071 1.00 0.00  ? 168 TYR B CE1 1 
ATOM 4753 C CE2 . TYR B 2 168  ? 176.674 193.538 131.116 1.00 0.00  ? 168 TYR B CE2 1 
ATOM 4754 C CZ  . TYR B 2 168  ? 175.684 193.908 130.240 1.00 0.00  ? 168 TYR B CZ  1 
ATOM 4755 O OH  . TYR B 2 168  ? 174.875 194.979 130.534 1.00 2.17  ? 168 TYR B OH  1 
ATOM 4756 N N   . THR B 2 169  ? 179.145 187.929 128.134 1.00 0.39  ? 169 THR B N   1 
ATOM 4757 C CA  . THR B 2 169  ? 180.341 187.213 127.714 1.00 0.12  ? 169 THR B CA  1 
ATOM 4758 C C   . THR B 2 169  ? 181.469 188.214 127.479 1.00 9.27  ? 169 THR B C   1 
ATOM 4759 O O   . THR B 2 169  ? 181.322 189.414 127.719 1.00 11.00 ? 169 THR B O   1 
ATOM 4760 C CB  . THR B 2 169  ? 180.076 186.393 126.454 1.00 0.00  ? 169 THR B CB  1 
ATOM 4761 O OG1 . THR B 2 169  ? 181.199 185.545 126.190 1.00 8.34  ? 169 THR B OG1 1 
ATOM 4762 C CG2 . THR B 2 169  ? 179.834 187.291 125.269 1.00 5.40  ? 169 THR B CG2 1 
ATOM 4763 N N   . GLU B 2 170  ? 182.633 187.702 127.069 1.00 0.00  ? 170 GLU B N   1 
ATOM 4764 C CA  . GLU B 2 170  ? 183.813 188.584 126.860 1.00 0.22  ? 170 GLU B CA  1 
ATOM 4765 C C   . GLU B 2 170  ? 183.545 189.511 125.671 1.00 10.16 ? 170 GLU B C   1 
ATOM 4766 O O   . GLU B 2 170  ? 183.953 190.687 125.735 1.00 7.97  ? 170 GLU B O   1 
ATOM 4767 C CB  . GLU B 2 170  ? 185.068 187.742 126.626 1.00 0.00  ? 170 GLU B CB  1 
ATOM 4768 C CG  . GLU B 2 170  ? 184.997 186.891 125.371 1.00 2.88  ? 170 GLU B CG  1 
ATOM 4769 C CD  . GLU B 2 170  ? 186.178 185.956 125.178 1.00 4.32  ? 170 GLU B CD  1 
ATOM 4770 O OE1 . GLU B 2 170  ? 187.223 186.187 125.818 1.00 0.77  ? 170 GLU B OE1 1 
ATOM 4771 O OE2 . GLU B 2 170  ? 186.051 185.001 124.388 1.00 5.52  ? 170 GLU B OE2 1 
ATOM 4772 N N   . ASN B 2 171  ? 182.879 188.995 124.634 1.00 0.00  ? 171 ASN B N   1 
ATOM 4773 C CA  . ASN B 2 171  ? 182.578 189.806 123.424 1.00 3.48  ? 171 ASN B CA  1 
ATOM 4774 C C   . ASN B 2 171  ? 181.665 190.974 123.811 1.00 0.00  ? 171 ASN B C   1 
ATOM 4775 O O   . ASN B 2 171  ? 181.788 192.044 123.189 1.00 3.47  ? 171 ASN B O   1 
ATOM 4776 C CB  . ASN B 2 171  ? 181.958 188.953 122.316 1.00 3.34  ? 171 ASN B CB  1 
ATOM 4777 C CG  . ASN B 2 171  ? 182.950 188.001 121.684 1.00 5.53  ? 171 ASN B CG  1 
ATOM 4778 O OD1 . ASN B 2 171  ? 184.157 188.227 121.740 1.00 8.87  ? 171 ASN B OD1 1 
ATOM 4779 N ND2 . ASN B 2 171  ? 182.454 186.932 121.083 1.00 2.58  ? 171 ASN B ND2 1 
ATOM 4780 N N   . GLY B 2 172  ? 180.783 190.769 124.794 1.00 0.00  ? 172 GLY B N   1 
ATOM 4781 C CA  . GLY B 2 172  ? 179.832 191.822 125.201 1.00 5.22  ? 172 GLY B CA  1 
ATOM 4782 C C   . GLY B 2 172  ? 178.400 191.346 125.052 1.00 6.00  ? 172 GLY B C   1 
ATOM 4783 O O   . GLY B 2 172  ? 177.503 191.990 125.631 1.00 18.21 ? 172 GLY B O   1 
ATOM 4784 N N   . VAL B 2 173  ? 178.190 190.258 124.303 1.00 3.14  ? 173 VAL B N   1 
ATOM 4785 C CA  . VAL B 2 173  ? 176.856 189.701 124.132 1.00 3.80  ? 173 VAL B CA  1 
ATOM 4786 C C   . VAL B 2 173  ? 176.212 189.531 125.499 1.00 0.00  ? 173 VAL B C   1 
ATOM 4787 O O   . VAL B 2 173  ? 176.847 189.047 126.444 1.00 6.14  ? 173 VAL B O   1 
ATOM 4788 C CB  . VAL B 2 173  ? 176.923 188.366 123.378 1.00 1.16  ? 173 VAL B CB  1 
ATOM 4789 C CG1 . VAL B 2 173  ? 175.549 187.988 122.849 1.00 0.85  ? 173 VAL B CG1 1 
ATOM 4790 C CG2 . VAL B 2 173  ? 177.936 188.446 122.249 1.00 3.53  ? 173 VAL B CG2 1 
ATOM 4791 N N   . LEU B 2 174  ? 174.953 189.943 125.618 1.00 0.46  ? 174 LEU B N   1 
ATOM 4792 C CA  . LEU B 2 174  ? 174.233 189.790 126.874 1.00 0.43  ? 174 LEU B CA  1 
ATOM 4793 C C   . LEU B 2 174  ? 173.697 188.369 126.995 1.00 2.69  ? 174 LEU B C   1 
ATOM 4794 O O   . LEU B 2 174  ? 173.013 187.876 126.094 1.00 2.31  ? 174 LEU B O   1 
ATOM 4795 C CB  . LEU B 2 174  ? 173.089 190.797 126.970 1.00 3.15  ? 174 LEU B CB  1 
ATOM 4796 C CG  . LEU B 2 174  ? 172.086 190.513 128.088 1.00 0.00  ? 174 LEU B CG  1 
ATOM 4797 C CD1 . LEU B 2 174  ? 172.704 190.845 129.425 1.00 0.00  ? 174 LEU B CD1 1 
ATOM 4798 C CD2 . LEU B 2 174  ? 170.810 191.301 127.889 1.00 0.00  ? 174 LEU B CD2 1 
ATOM 4799 N N   . LEU B 2 175  ? 174.012 187.712 128.111 1.00 6.23  ? 175 LEU B N   1 
ATOM 4800 C CA  . LEU B 2 175  ? 173.562 186.347 128.361 1.00 6.52  ? 175 LEU B CA  1 
ATOM 4801 C C   . LEU B 2 175  ? 172.362 186.298 129.299 1.00 2.96  ? 175 LEU B C   1 
ATOM 4802 O O   . LEU B 2 175  ? 171.323 185.728 128.954 1.00 4.02  ? 175 LEU B O   1 
ATOM 4803 C CB  . LEU B 2 175  ? 174.704 185.507 128.939 1.00 1.27  ? 175 LEU B CB  1 
ATOM 4804 C CG  . LEU B 2 175  ? 175.830 185.096 128.001 1.00 0.00  ? 175 LEU B CG  1 
ATOM 4805 C CD1 . LEU B 2 175  ? 176.420 183.783 128.478 1.00 2.10  ? 175 LEU B CD1 1 
ATOM 4806 C CD2 . LEU B 2 175  ? 175.335 184.980 126.573 1.00 1.60  ? 175 LEU B CD2 1 
ATOM 4807 N N   . LEU B 2 176  ? 172.508 186.879 130.494 1.00 5.82  ? 176 LEU B N   1 
ATOM 4808 C CA  . LEU B 2 176  ? 171.415 186.780 131.500 1.00 2.56  ? 176 LEU B CA  1 
ATOM 4809 C C   . LEU B 2 176  ? 171.208 188.123 132.207 1.00 0.82  ? 176 LEU B C   1 
ATOM 4810 O O   . LEU B 2 176  ? 172.209 188.828 132.427 1.00 0.34  ? 176 LEU B O   1 
ATOM 4811 C CB  . LEU B 2 176  ? 171.786 185.690 132.512 1.00 1.37  ? 176 LEU B CB  1 
ATOM 4812 C CG  . LEU B 2 176  ? 170.624 185.115 133.321 1.00 2.07  ? 176 LEU B CG  1 
ATOM 4813 C CD1 . LEU B 2 176  ? 170.737 183.603 133.429 1.00 0.22  ? 176 LEU B CD1 1 
ATOM 4814 C CD2 . LEU B 2 176  ? 170.561 185.743 134.705 1.00 2.50  ? 176 LEU B CD2 1 
ATOM 4815 N N   . ALA B 2 177  ? 169.957 188.456 132.542 1.00 2.30  ? 177 ALA B N   1 
ATOM 4816 C CA  . ALA B 2 177  ? 169.661 189.695 133.301 1.00 1.65  ? 177 ALA B CA  1 
ATOM 4817 C C   . ALA B 2 177  ? 168.684 189.344 134.427 1.00 2.43  ? 177 ALA B C   1 
ATOM 4818 O O   . ALA B 2 177  ? 167.605 188.804 134.115 1.00 8.71  ? 177 ALA B O   1 
ATOM 4819 C CB  . ALA B 2 177  ? 169.096 190.746 132.379 1.00 4.00  ? 177 ALA B CB  1 
ATOM 4820 N N   . GLN B 2 178  ? 169.044 189.629 135.683 1.00 2.54  ? 178 GLN B N   1 
ATOM 4821 C CA  . GLN B 2 178  ? 168.183 189.220 136.826 1.00 1.94  ? 178 GLN B CA  1 
ATOM 4822 C C   . GLN B 2 178  ? 167.967 190.404 137.775 1.00 6.95  ? 178 GLN B C   1 
ATOM 4823 O O   . GLN B 2 178  ? 168.944 191.124 138.047 1.00 11.64 ? 178 GLN B O   1 
ATOM 4824 C CB  . GLN B 2 178  ? 168.824 188.038 137.557 1.00 3.92  ? 178 GLN B CB  1 
ATOM 4825 C CG  . GLN B 2 178  ? 168.539 188.007 139.052 1.00 7.52  ? 178 GLN B CG  1 
ATOM 4826 C CD  . GLN B 2 178  ? 167.279 187.241 139.374 1.00 8.29  ? 178 GLN B CD  1 
ATOM 4827 O OE1 . GLN B 2 178  ? 167.082 186.115 138.923 1.00 5.61  ? 178 GLN B OE1 1 
ATOM 4828 N NE2 . GLN B 2 178  ? 166.410 187.852 140.162 1.00 7.65  ? 178 GLN B NE2 1 
ATOM 4829 N N   . LEU B 2 179  ? 166.733 190.593 138.255 1.00 1.96  ? 179 LEU B N   1 
ATOM 4830 C CA  . LEU B 2 179  ? 166.450 191.672 139.239 1.00 5.52  ? 179 LEU B CA  1 
ATOM 4831 C C   . LEU B 2 179  ? 166.081 191.029 140.580 1.00 13.56 ? 179 LEU B C   1 
ATOM 4832 O O   . LEU B 2 179  ? 164.987 190.436 140.668 1.00 15.09 ? 179 LEU B O   1 
ATOM 4833 C CB  . LEU B 2 179  ? 165.305 192.542 138.710 1.00 7.05  ? 179 LEU B CB  1 
ATOM 4834 C CG  . LEU B 2 179  ? 165.016 193.809 139.512 1.00 6.50  ? 179 LEU B CG  1 
ATOM 4835 C CD1 . LEU B 2 179  ? 164.535 194.929 138.602 1.00 7.30  ? 179 LEU B CD1 1 
ATOM 4836 C CD2 . LEU B 2 179  ? 163.992 193.536 140.604 1.00 4.69  ? 179 LEU B CD2 1 
ATOM 4837 N N   . LEU B 2 180  ? 166.965 191.130 141.577 1.00 17.65 ? 180 LEU B N   1 
ATOM 4838 C CA  . LEU B 2 180  ? 166.708 190.498 142.900 1.00 11.60 ? 180 LEU B CA  1 
ATOM 4839 C C   . LEU B 2 180  ? 165.871 191.448 143.762 1.00 10.58 ? 180 LEU B C   1 
ATOM 4840 O O   . LEU B 2 180  ? 164.794 191.026 144.226 1.00 15.36 ? 180 LEU B O   1 
ATOM 4841 C CB  . LEU B 2 180  ? 168.048 190.187 143.574 1.00 8.20  ? 180 LEU B CB  1 
ATOM 4842 C CG  . LEU B 2 180  ? 169.052 189.419 142.717 1.00 10.92 ? 180 LEU B CG  1 
ATOM 4843 C CD1 . LEU B 2 180  ? 170.477 189.747 143.134 1.00 4.89  ? 180 LEU B CD1 1 
ATOM 4844 C CD2 . LEU B 2 180  ? 168.804 187.922 142.805 1.00 9.74  ? 180 LEU B CD2 1 
ATOM 4845 N N   . ASN B 2 181  ? 166.352 192.679 143.960 1.00 10.63 ? 181 ASN B N   1 
ATOM 4846 C CA  . ASN B 2 181  ? 165.618 193.672 144.790 1.00 13.24 ? 181 ASN B CA  1 
ATOM 4847 C C   . ASN B 2 181  ? 165.654 195.035 144.092 1.00 18.93 ? 181 ASN B C   1 
ATOM 4848 O O   . ASN B 2 181  ? 166.608 195.278 143.331 1.00 20.11 ? 181 ASN B O   1 
ATOM 4849 C CB  . ASN B 2 181  ? 166.176 193.747 146.213 1.00 12.27 ? 181 ASN B CB  1 
ATOM 4850 C CG  . ASN B 2 181  ? 165.225 194.419 147.181 1.00 20.10 ? 181 ASN B CG  1 
ATOM 4851 O OD1 . ASN B 2 181  ? 164.019 194.192 147.130 1.00 28.56 ? 181 ASN B OD1 1 
ATOM 4852 N ND2 . ASN B 2 181  ? 165.759 195.248 148.063 1.00 16.68 ? 181 ASN B ND2 1 
ATOM 4853 N N   . GLU B 2 182  ? 164.655 195.884 144.347 1.00 17.06 ? 182 GLU B N   1 
ATOM 4854 C CA  . GLU B 2 182  ? 164.575 197.209 143.675 1.00 17.42 ? 182 GLU B CA  1 
ATOM 4855 C C   . GLU B 2 182  ? 165.698 198.122 144.181 1.00 17.61 ? 182 GLU B C   1 
ATOM 4856 O O   . GLU B 2 182  ? 166.004 199.111 143.486 1.00 20.54 ? 182 GLU B O   1 
ATOM 4857 C CB  . GLU B 2 182  ? 163.205 197.845 143.922 1.00 15.80 ? 182 GLU B CB  1 
ATOM 4858 C CG  . GLU B 2 182  ? 163.021 198.356 145.340 1.00 16.46 ? 182 GLU B CG  1 
ATOM 4859 C CD  . GLU B 2 182  ? 162.751 197.275 146.373 1.00 18.87 ? 182 GLU B CD  1 
ATOM 4860 O OE1 . GLU B 2 182  ? 161.891 196.411 146.110 1.00 21.33 ? 182 GLU B OE1 1 
ATOM 4861 O OE2 . GLU B 2 182  ? 163.403 197.298 147.434 1.00 17.35 ? 182 GLU B OE2 1 
ATOM 4862 N N   . ASP B 2 183  ? 166.283 197.810 145.341 1.00 10.52 ? 183 ASP B N   1 
ATOM 4863 C CA  . ASP B 2 183  ? 167.316 198.670 145.895 1.00 8.86  ? 183 ASP B CA  1 
ATOM 4864 C C   . ASP B 2 183  ? 168.624 198.505 145.117 1.00 10.10 ? 183 ASP B C   1 
ATOM 4865 O O   . ASP B 2 183  ? 168.846 197.475 144.476 1.00 16.86 ? 183 ASP B O   1 
ATOM 4866 C CB  . ASP B 2 183  ? 167.534 198.345 147.370 1.00 15.38 ? 183 ASP B CB  1 
ATOM 4867 C CG  . ASP B 2 183  ? 166.331 198.695 148.225 1.00 21.43 ? 183 ASP B CG  1 
ATOM 4868 O OD1 . ASP B 2 183  ? 165.760 199.788 148.031 1.00 18.24 ? 183 ASP B OD1 1 
ATOM 4869 O OD2 . ASP B 2 183  ? 165.952 197.875 149.087 1.00 22.20 ? 183 ASP B OD2 1 
ATOM 4870 N N   . PRO B 2 184  ? 169.497 199.514 145.145 1.00 0.00  ? 184 PRO B N   1 
ATOM 4871 C CA  . PRO B 2 184  ? 170.759 199.421 144.399 1.00 0.00  ? 184 PRO B CA  1 
ATOM 4872 C C   . PRO B 2 184  ? 171.635 198.276 144.885 1.00 6.17  ? 184 PRO B C   1 
ATOM 4873 O O   . PRO B 2 184  ? 171.622 197.910 146.061 1.00 24.88 ? 184 PRO B O   1 
ATOM 4874 C CB  . PRO B 2 184  ? 171.428 200.775 144.662 1.00 0.00  ? 184 PRO B CB  1 
ATOM 4875 C CG  . PRO B 2 184  ? 170.315 201.685 145.014 1.00 8.68  ? 184 PRO B CG  1 
ATOM 4876 C CD  . PRO B 2 184  ? 169.305 200.849 145.734 1.00 4.63  ? 184 PRO B CD  1 
ATOM 4877 N N   . VAL B 2 185  ? 172.403 197.711 143.958 1.00 7.26  ? 185 VAL B N   1 
ATOM 4878 C CA  . VAL B 2 185  ? 173.336 196.636 144.282 1.00 10.74 ? 185 VAL B CA  1 
ATOM 4879 C C   . VAL B 2 185  ? 174.610 197.253 144.847 1.00 9.12  ? 185 VAL B C   1 
ATOM 4880 O O   . VAL B 2 185  ? 175.250 198.087 144.197 1.00 7.56  ? 185 VAL B O   1 
ATOM 4881 C CB  . VAL B 2 185  ? 173.637 195.772 143.050 1.00 4.88  ? 185 VAL B CB  1 
ATOM 4882 C CG1 . VAL B 2 185  ? 174.726 194.765 143.362 1.00 0.00  ? 185 VAL B CG1 1 
ATOM 4883 C CG2 . VAL B 2 185  ? 172.382 195.065 142.585 1.00 7.96  ? 185 VAL B CG2 1 
ATOM 4884 N N   . LEU B 2 186  ? 174.986 196.835 146.056 1.00 0.00  ? 186 LEU B N   1 
ATOM 4885 C CA  . LEU B 2 186  ? 176.105 197.445 146.767 1.00 3.61  ? 186 LEU B CA  1 
ATOM 4886 C C   . LEU B 2 186  ? 177.430 196.747 146.463 1.00 6.50  ? 186 LEU B C   1 
ATOM 4887 O O   . LEU B 2 186  ? 178.392 197.394 146.039 1.00 13.28 ? 186 LEU B O   1 
ATOM 4888 C CB  . LEU B 2 186  ? 175.827 197.447 148.276 1.00 3.73  ? 186 LEU B CB  1 
ATOM 4889 C CG  . LEU B 2 186  ? 175.034 198.618 148.864 1.00 0.90  ? 186 LEU B CG  1 
ATOM 4890 C CD1 . LEU B 2 186  ? 174.847 198.435 150.356 1.00 2.14  ? 186 LEU B CD1 1 
ATOM 4891 C CD2 . LEU B 2 186  ? 175.733 199.934 148.588 1.00 0.00  ? 186 LEU B CD2 1 
ATOM 4892 N N   . GLN B 2 187  ? 177.500 195.434 146.687 1.00 0.00  ? 187 GLN B N   1 
ATOM 4893 C CA  . GLN B 2 187  ? 178.737 194.687 146.500 1.00 1.53  ? 187 GLN B CA  1 
ATOM 4894 C C   . GLN B 2 187  ? 178.442 193.319 145.901 1.00 1.32  ? 187 GLN B C   1 
ATOM 4895 O O   . GLN B 2 187  ? 177.334 192.791 146.016 1.00 7.14  ? 187 GLN B O   1 
ATOM 4896 C CB  . GLN B 2 187  ? 179.504 194.506 147.819 1.00 2.87  ? 187 GLN B CB  1 
ATOM 4897 C CG  . GLN B 2 187  ? 179.792 195.788 148.576 1.00 0.00  ? 187 GLN B CG  1 
ATOM 4898 C CD  . GLN B 2 187  ? 180.937 196.573 147.972 1.00 3.60  ? 187 GLN B CD  1 
ATOM 4899 O OE1 . GLN B 2 187  ? 181.998 196.022 147.682 1.00 2.56  ? 187 GLN B OE1 1 
ATOM 4900 N NE2 . GLN B 2 187  ? 180.729 197.869 147.781 1.00 6.00  ? 187 GLN B NE2 1 
ATOM 4901 N N   . LEU B 2 188  ? 179.487 192.737 145.288 1.00 0.00  ? 188 LEU B N   1 
ATOM 4902 C CA  . LEU B 2 188  ? 179.403 191.371 144.707 1.00 0.07  ? 188 LEU B CA  1 
ATOM 4903 C C   . LEU B 2 188  ? 180.654 190.608 145.163 1.00 0.00  ? 188 LEU B C   1 
ATOM 4904 O O   . LEU B 2 188  ? 181.763 191.126 144.927 1.00 7.89  ? 188 LEU B O   1 
ATOM 4905 C CB  . LEU B 2 188  ? 179.386 191.467 143.179 1.00 0.00  ? 188 LEU B CB  1 
ATOM 4906 C CG  . LEU B 2 188  ? 178.181 192.163 142.549 1.00 2.51  ? 188 LEU B CG  1 
ATOM 4907 C CD1 . LEU B 2 188  ? 178.436 192.436 141.074 1.00 0.00  ? 188 LEU B CD1 1 
ATOM 4908 C CD2 . LEU B 2 188  ? 176.930 191.319 142.714 1.00 3.32  ? 188 LEU B CD2 1 
ATOM 4909 N N   . LYS B 2 189  ? 180.495 189.435 145.783 1.00 0.00  ? 189 LYS B N   1 
ATOM 4910 C CA  . LYS B 2 189  ? 181.635 188.636 146.308 1.00 0.00  ? 189 LYS B CA  1 
ATOM 4911 C C   . LYS B 2 189  ? 181.476 187.186 145.838 1.00 0.00  ? 189 LYS B C   1 
ATOM 4912 O O   . LYS B 2 189  ? 180.423 186.586 146.132 1.00 6.29  ? 189 LYS B O   1 
ATOM 4913 C CB  . LYS B 2 189  ? 181.684 188.716 147.837 1.00 0.00  ? 189 LYS B CB  1 
ATOM 4914 C CG  . LYS B 2 189  ? 181.879 190.113 148.412 1.00 3.11  ? 189 LYS B CG  1 
ATOM 4915 C CD  . LYS B 2 189  ? 183.210 190.734 148.044 1.00 0.00  ? 189 LYS B CD  1 
ATOM 4916 C CE  . LYS B 2 189  ? 183.432 192.091 148.675 1.00 0.49  ? 189 LYS B CE  1 
ATOM 4917 N NZ  . LYS B 2 189  ? 184.733 192.677 148.274 1.00 0.24  ? 189 LYS B NZ  1 
ATOM 4918 N N   . CYS B 2 190  ? 182.480 186.652 145.135 1.00 3.16  ? 190 CYS B N   1 
ATOM 4919 C CA  . CYS B 2 190  ? 182.398 185.265 144.600 1.00 0.00  ? 190 CYS B CA  1 
ATOM 4920 C C   . CYS B 2 190  ? 183.335 184.345 145.390 1.00 0.00  ? 190 CYS B C   1 
ATOM 4921 O O   . CYS B 2 190  ? 184.487 184.751 145.639 1.00 5.34  ? 190 CYS B O   1 
ATOM 4922 C CB  . CYS B 2 190  ? 182.783 185.230 143.126 1.00 0.00  ? 190 CYS B CB  1 
ATOM 4923 S SG  . CYS B 2 190  ? 182.751 183.564 142.414 1.00 10.88 ? 190 CYS B SG  1 
ATOM 4924 N N   . ARG B 2 191  ? 182.855 183.154 145.763 1.00 0.00  ? 191 ARG B N   1 
ATOM 4925 C CA  . ARG B 2 191  ? 183.687 182.178 146.517 1.00 0.00  ? 191 ARG B CA  1 
ATOM 4926 C C   . ARG B 2 191  ? 183.974 180.977 145.610 1.00 5.96  ? 191 ARG B C   1 
ATOM 4927 O O   . ARG B 2 191  ? 183.003 180.347 145.148 1.00 10.68 ? 191 ARG B O   1 
ATOM 4928 C CB  . ARG B 2 191  ? 182.960 181.748 147.794 1.00 4.14  ? 191 ARG B CB  1 
ATOM 4929 C CG  . ARG B 2 191  ? 182.302 182.899 148.543 1.00 5.14  ? 191 ARG B CG  1 
ATOM 4930 C CD  . ARG B 2 191  ? 181.457 182.460 149.724 1.00 1.19  ? 191 ARG B CD  1 
ATOM 4931 N NE  . ARG B 2 191  ? 182.244 182.052 150.880 1.00 1.69  ? 191 ARG B NE  1 
ATOM 4932 C CZ  . ARG B 2 191  ? 182.185 180.853 151.448 1.00 3.49  ? 191 ARG B CZ  1 
ATOM 4933 N NH1 . ARG B 2 191  ? 181.598 179.850 150.819 1.00 6.81  ? 191 ARG B NH1 1 
ATOM 4934 N NH2 . ARG B 2 191  ? 182.716 180.662 152.643 1.00 4.24  ? 191 ARG B NH2 1 
ATOM 4935 N N   . THR B 2 192  ? 185.253 180.669 145.375 1.00 2.79  ? 192 THR B N   1 
ATOM 4936 C CA  . THR B 2 192  ? 185.607 179.563 144.444 1.00 0.00  ? 192 THR B CA  1 
ATOM 4937 C C   . THR B 2 192  ? 186.224 178.395 145.220 1.00 10.76 ? 192 THR B C   1 
ATOM 4938 O O   . THR B 2 192  ? 185.895 178.245 146.413 1.00 16.64 ? 192 THR B O   1 
ATOM 4939 C CB  . THR B 2 192  ? 186.520 180.065 143.320 1.00 2.19  ? 192 THR B CB  1 
ATOM 4940 O OG1 . THR B 2 192  ? 187.715 180.572 143.914 1.00 3.71  ? 192 THR B OG1 1 
ATOM 4941 C CG2 . THR B 2 192  ? 185.857 181.137 142.485 1.00 4.91  ? 192 THR B CG2 1 
ATOM 4942 N N   . TYR B 2 193  ? 187.077 177.600 144.566 1.00 10.48 ? 193 TYR B N   1 
ATOM 4943 C CA  . TYR B 2 193  ? 187.645 176.394 145.231 1.00 11.16 ? 193 TYR B CA  1 
ATOM 4944 C C   . TYR B 2 193  ? 189.107 176.628 145.600 1.00 15.00 ? 193 TYR B C   1 
ATOM 4945 O O   . TYR B 2 193  ? 189.856 177.199 144.777 1.00 26.21 ? 193 TYR B O   1 
ATOM 4946 C CB  . TYR B 2 193  ? 187.504 175.164 144.327 1.00 15.12 ? 193 TYR B CB  1 
ATOM 4947 C CG  . TYR B 2 193  ? 188.278 173.951 144.827 1.00 21.36 ? 193 TYR B CG  1 
ATOM 4948 C CD1 . TYR B 2 193  ? 187.937 173.327 146.021 1.00 20.98 ? 193 TYR B CD1 1 
ATOM 4949 C CD2 . TYR B 2 193  ? 189.355 173.442 144.114 1.00 17.78 ? 193 TYR B CD2 1 
ATOM 4950 C CE1 . TYR B 2 193  ? 188.640 172.229 146.488 1.00 18.00 ? 193 TYR B CE1 1 
ATOM 4951 C CE2 . TYR B 2 193  ? 190.066 172.344 144.570 1.00 14.70 ? 193 TYR B CE2 1 
ATOM 4952 C CZ  . TYR B 2 193  ? 189.707 171.736 145.759 1.00 18.41 ? 193 TYR B CZ  1 
ATOM 4953 O OH  . TYR B 2 193  ? 190.404 170.654 146.213 1.00 19.79 ? 193 TYR B OH  1 
ATOM 4954 N N   . GLU B 2 194  ? 189.506 176.198 146.801 1.00 9.51  ? 194 GLU B N   1 
ATOM 4955 C CA  . GLU B 2 194  ? 190.887 176.319 147.244 1.00 13.50 ? 194 GLU B CA  1 
ATOM 4956 C C   . GLU B 2 194  ? 191.298 175.041 147.957 1.00 20.26 ? 194 GLU B C   1 
ATOM 4957 O O   . GLU B 2 194  ? 190.547 174.512 148.782 1.00 23.84 ? 194 GLU B O   1 
ATOM 4958 C CB  . GLU B 2 194  ? 191.081 177.526 148.170 1.00 13.60 ? 194 GLU B CB  1 
ATOM 4959 C CG  . GLU B 2 194  ? 191.029 178.867 147.460 1.00 10.53 ? 194 GLU B CG  1 
ATOM 4960 C CD  . GLU B 2 194  ? 190.479 179.972 148.341 1.00 15.72 ? 194 GLU B CD  1 
ATOM 4961 O OE1 . GLU B 2 194  ? 190.820 179.998 149.542 1.00 19.03 ? 194 GLU B OE1 1 
ATOM 4962 O OE2 . GLU B 2 194  ? 189.708 180.814 147.832 1.00 10.90 ? 194 GLU B OE2 1 
ATOM 4963 N N   . ILE B 2 195  ? 192.488 174.552 147.633 1.00 17.97 ? 195 ILE B N   1 
ATOM 4964 C CA  . ILE B 2 195  ? 192.982 173.301 148.219 1.00 17.31 ? 195 ILE B CA  1 
ATOM 4965 C C   . ILE B 2 195  ? 193.409 173.551 149.660 1.00 21.74 ? 195 ILE B C   1 
ATOM 4966 O O   . ILE B 2 195  ? 193.969 174.621 149.960 1.00 19.28 ? 195 ILE B O   1 
ATOM 4967 C CB  . ILE B 2 195  ? 194.139 172.748 147.387 1.00 19.50 ? 195 ILE B CB  1 
ATOM 4968 C CG1 . ILE B 2 195  ? 195.066 173.884 146.950 1.00 18.47 ? 195 ILE B CG1 1 
ATOM 4969 C CG2 . ILE B 2 195  ? 193.604 171.995 146.180 1.00 20.00 ? 195 ILE B CG2 1 
ATOM 4970 C CD1 . ILE B 2 195  ? 196.146 173.457 145.984 1.00 22.34 ? 195 ILE B CD1 1 
ATOM 4971 N N   . PRO B 2 196  ? 193.172 172.614 150.576 1.00 22.69 ? 196 PRO B N   1 
ATOM 4972 C CA  . PRO B 2 196  ? 193.509 172.852 151.984 1.00 15.78 ? 196 PRO B CA  1 
ATOM 4973 C C   . PRO B 2 196  ? 195.010 172.948 152.210 1.00 11.55 ? 196 PRO B C   1 
ATOM 4974 O O   . PRO B 2 196  ? 195.811 172.311 151.524 1.00 10.12 ? 196 PRO B O   1 
ATOM 4975 C CB  . PRO B 2 196  ? 192.922 171.630 152.702 1.00 14.81 ? 196 PRO B CB  1 
ATOM 4976 C CG  . PRO B 2 196  ? 191.932 171.048 151.738 1.00 19.76 ? 196 PRO B CG  1 
ATOM 4977 C CD  . PRO B 2 196  ? 192.493 171.324 150.384 1.00 19.93 ? 196 PRO B CD  1 
ATOM 4978 N N   . ARG B 2 197  ? 195.385 173.747 153.215 1.00 11.79 ? 197 ARG B N   1 
ATOM 4979 C CA  . ARG B 2 197  ? 196.822 173.878 153.571 1.00 15.41 ? 197 ARG B CA  1 
ATOM 4980 C C   . ARG B 2 197  ? 197.255 172.616 154.324 1.00 14.78 ? 197 ARG B C   1 
ATOM 4981 O O   . ARG B 2 197  ? 198.340 172.088 154.013 1.00 16.80 ? 197 ARG B O   1 
ATOM 4982 C CB  . ARG B 2 197  ? 197.056 175.126 154.427 1.00 10.96 ? 197 ARG B CB  1 
ATOM 4983 C CG  . ARG B 2 197  ? 196.146 176.297 154.087 1.00 8.22  ? 197 ARG B CG  1 
ATOM 4984 C CD  . ARG B 2 197  ? 196.442 177.512 154.944 1.00 12.31 ? 197 ARG B CD  1 
ATOM 4985 N NE  . ARG B 2 197  ? 196.874 177.149 156.287 1.00 15.38 ? 197 ARG B NE  1 
ATOM 4986 C CZ  . ARG B 2 197  ? 196.099 177.198 157.364 1.00 13.35 ? 197 ARG B CZ  1 
ATOM 4987 N NH1 . ARG B 2 197  ? 194.836 177.567 157.255 1.00 13.26 ? 197 ARG B NH1 1 
ATOM 4988 N NH2 . ARG B 2 197  ? 196.592 176.876 158.548 1.00 7.80  ? 197 ARG B NH2 1 
ATOM 4989 N N   . HIS B 2 198  ? 196.431 172.157 155.274 1.00 14.88 ? 198 HIS B N   1 
ATOM 4990 C CA  . HIS B 2 198  ? 196.787 170.943 156.060 1.00 10.19 ? 198 HIS B CA  1 
ATOM 4991 C C   . HIS B 2 198  ? 195.501 170.155 156.343 1.00 13.71 ? 198 HIS B C   1 
ATOM 4992 O O   . HIS B 2 198  ? 194.402 170.679 156.058 1.00 15.75 ? 198 HIS B O   1 
ATOM 4993 C CB  . HIS B 2 198  ? 197.567 171.348 157.318 1.00 5.69  ? 198 HIS B CB  1 
ATOM 4994 C CG  . HIS B 2 198  ? 196.797 172.191 158.277 1.00 8.76  ? 198 HIS B CG  1 
ATOM 4995 N ND1 . HIS B 2 198  ? 195.984 171.658 159.254 1.00 7.02  ? 198 HIS B ND1 1 
ATOM 4996 C CD2 . HIS B 2 198  ? 196.723 173.520 158.418 1.00 11.34 ? 198 HIS B CD2 1 
ATOM 4997 C CE1 . HIS B 2 198  ? 195.437 172.642 159.952 1.00 11.51 ? 198 HIS B CE1 1 
ATOM 4998 N NE2 . HIS B 2 198  ? 195.871 173.782 159.461 1.00 8.24  ? 198 HIS B NE2 1 
ATOM 4999 N N   . PRO B 2 199  ? 195.567 168.917 156.883 1.00 10.70 ? 199 PRO B N   1 
ATOM 5000 C CA  . PRO B 2 199  ? 194.364 168.103 157.094 1.00 7.41  ? 199 PRO B CA  1 
ATOM 5001 C C   . PRO B 2 199  ? 193.269 168.863 157.855 1.00 11.00 ? 199 PRO B C   1 
ATOM 5002 O O   . PRO B 2 199  ? 192.113 168.715 157.506 1.00 3.67  ? 199 PRO B O   1 
ATOM 5003 C CB  . PRO B 2 199  ? 194.873 166.944 157.962 1.00 8.55  ? 199 PRO B CB  1 
ATOM 5004 C CG  . PRO B 2 199  ? 196.322 166.799 157.563 1.00 10.51 ? 199 PRO B CG  1 
ATOM 5005 C CD  . PRO B 2 199  ? 196.789 168.213 157.288 1.00 10.29 ? 199 PRO B CD  1 
ATOM 5006 N N   . GLY B 2 200  ? 193.655 169.655 158.861 1.00 17.96 ? 200 GLY B N   1 
ATOM 5007 C CA  . GLY B 2 200  ? 192.669 170.397 159.671 1.00 16.41 ? 200 GLY B CA  1 
ATOM 5008 C C   . GLY B 2 200  ? 191.816 171.323 158.822 1.00 16.77 ? 200 GLY B C   1 
ATOM 5009 O O   . GLY B 2 200  ? 190.611 171.445 159.116 1.00 19.32 ? 200 GLY B O   1 
ATOM 5010 N N   . VAL B 2 201  ? 192.413 171.953 157.806 1.00 20.74 ? 201 VAL B N   1 
ATOM 5011 C CA  . VAL B 2 201  ? 191.667 172.921 156.946 1.00 20.11 ? 201 VAL B CA  1 
ATOM 5012 C C   . VAL B 2 201  ? 190.459 172.211 156.326 1.00 20.99 ? 201 VAL B C   1 
ATOM 5013 O O   . VAL B 2 201  ? 190.650 171.129 155.736 1.00 25.93 ? 201 VAL B O   1 
ATOM 5014 C CB  . VAL B 2 201  ? 192.578 173.521 155.859 1.00 15.56 ? 201 VAL B CB  1 
ATOM 5015 C CG1 . VAL B 2 201  ? 191.805 174.414 154.901 1.00 18.49 ? 201 VAL B CG1 1 
ATOM 5016 C CG2 . VAL B 2 201  ? 193.747 174.274 156.469 1.00 15.68 ? 201 VAL B CG2 1 
ATOM 5017 N N   . THR B 2 202  ? 189.269 172.806 156.452 1.00 21.95 ? 202 THR B N   1 
ATOM 5018 C CA  . THR B 2 202  ? 188.039 172.213 155.860 1.00 20.90 ? 202 THR B CA  1 
ATOM 5019 C C   . THR B 2 202  ? 187.760 172.868 154.503 1.00 17.07 ? 202 THR B C   1 
ATOM 5020 O O   . THR B 2 202  ? 188.636 173.613 154.018 1.00 20.32 ? 202 THR B O   1 
ATOM 5021 C CB  . THR B 2 202  ? 186.841 172.362 156.807 1.00 26.31 ? 202 THR B CB  1 
ATOM 5022 O OG1 . THR B 2 202  ? 186.206 173.610 156.528 1.00 29.84 ? 202 THR B OG1 1 
ATOM 5023 C CG2 . THR B 2 202  ? 187.235 172.304 158.267 1.00 21.47 ? 202 THR B CG2 1 
ATOM 5024 N N   . GLU B 2 203  ? 186.589 172.596 153.920 1.00 18.66 ? 203 GLU B N   1 
ATOM 5025 C CA  . GLU B 2 203  ? 186.223 173.186 152.604 1.00 26.78 ? 203 GLU B CA  1 
ATOM 5026 C C   . GLU B 2 203  ? 184.884 173.919 152.734 1.00 28.71 ? 203 GLU B C   1 
ATOM 5027 O O   . GLU B 2 203  ? 184.030 173.452 153.513 1.00 31.69 ? 203 GLU B O   1 
ATOM 5028 C CB  . GLU B 2 203  ? 186.139 172.101 151.529 1.00 24.83 ? 203 GLU B CB  1 
ATOM 5029 C CG  . GLU B 2 203  ? 187.477 171.463 151.202 1.00 30.17 ? 203 GLU B CG  1 
ATOM 5030 C CD  . GLU B 2 203  ? 187.401 170.334 150.189 1.00 30.58 ? 203 GLU B CD  1 
ATOM 5031 O OE1 . GLU B 2 203  ? 186.275 169.906 149.867 1.00 28.44 ? 203 GLU B OE1 1 
ATOM 5032 O OE2 . GLU B 2 203  ? 188.469 169.889 149.723 1.00 22.54 ? 203 GLU B OE2 1 
ATOM 5033 N N   . GLN B 2 204  ? 184.715 175.021 151.998 1.00 24.61 ? 204 GLN B N   1 
ATOM 5034 C CA  . GLN B 2 204  ? 183.438 175.784 152.029 1.00 18.66 ? 204 GLN B CA  1 
ATOM 5035 C C   . GLN B 2 204  ? 182.770 175.688 150.653 1.00 19.04 ? 204 GLN B C   1 
ATOM 5036 O O   . GLN B 2 204  ? 183.505 175.568 149.653 1.00 16.77 ? 204 GLN B O   1 
ATOM 5037 C CB  . GLN B 2 204  ? 183.702 177.236 152.431 1.00 14.80 ? 204 GLN B CB  1 
ATOM 5038 C CG  . GLN B 2 204  ? 184.013 177.410 153.910 1.00 16.73 ? 204 GLN B CG  1 
ATOM 5039 C CD  . GLN B 2 204  ? 182.860 178.015 154.673 1.00 20.96 ? 204 GLN B CD  1 
ATOM 5040 O OE1 . GLN B 2 204  ? 181.718 178.008 154.220 1.00 19.65 ? 204 GLN B OE1 1 
ATOM 5041 N NE2 . GLN B 2 204  ? 183.155 178.549 155.847 1.00 20.90 ? 204 GLN B NE2 1 
ATOM 5042 N N   . ASN B 2 205  ? 181.435 175.741 150.604 1.00 20.83 ? 205 ASN B N   1 
ATOM 5043 C CA  . ASN B 2 205  ? 180.728 175.593 149.340 1.00 16.88 ? 205 ASN B CA  1 
ATOM 5044 C C   . ASN B 2 205  ? 181.050 176.742 148.393 1.00 13.73 ? 205 ASN B C   1 
ATOM 5045 O O   . ASN B 2 205  ? 181.304 177.874 148.811 1.00 19.45 ? 205 ASN B O   1 
ATOM 5046 C CB  . ASN B 2 205  ? 179.220 175.531 149.580 1.00 13.85 ? 205 ASN B CB  1 
ATOM 5047 C CG  . ASN B 2 205  ? 178.807 174.322 150.391 1.00 18.21 ? 205 ASN B CG  1 
ATOM 5048 O OD1 . ASN B 2 205  ? 179.298 173.215 150.170 1.00 18.62 ? 205 ASN B OD1 1 
ATOM 5049 N ND2 . ASN B 2 205  ? 177.899 174.526 151.337 1.00 20.95 ? 205 ASN B ND2 1 
ATOM 5050 N N   . GLU B 2 206  ? 181.010 176.418 147.092 1.00 8.76  ? 206 GLU B N   1 
ATOM 5051 C CA  . GLU B 2 206  ? 181.185 177.471 146.060 1.00 5.13  ? 206 GLU B CA  1 
ATOM 5052 C C   . GLU B 2 206  ? 179.949 178.360 146.152 1.00 10.87 ? 206 GLU B C   1 
ATOM 5053 O O   . GLU B 2 206  ? 178.833 177.806 146.165 1.00 19.68 ? 206 GLU B O   1 
ATOM 5054 C CB  . GLU B 2 206  ? 181.345 176.851 144.671 1.00 13.15 ? 206 GLU B CB  1 
ATOM 5055 C CG  . GLU B 2 206  ? 182.390 175.751 144.620 1.00 14.18 ? 206 GLU B CG  1 
ATOM 5056 C CD  . GLU B 2 206  ? 183.532 176.001 143.650 1.00 17.51 ? 206 GLU B CD  1 
ATOM 5057 O OE1 . GLU B 2 206  ? 183.862 177.180 143.420 1.00 11.05 ? 206 GLU B OE1 1 
ATOM 5058 O OE2 . GLU B 2 206  ? 184.089 175.016 143.127 1.00 17.76 ? 206 GLU B OE2 1 
ATOM 5059 N N   . GLU B 2 207  ? 180.134 179.675 146.181 1.00 4.07  ? 207 GLU B N   1 
ATOM 5060 C CA  . GLU B 2 207  ? 179.034 180.601 146.411 1.00 1.68  ? 207 GLU B CA  1 
ATOM 5061 C C   . GLU B 2 207  ? 179.322 181.922 145.716 1.00 2.68  ? 207 GLU B C   1 
ATOM 5062 O O   . GLU B 2 207  ? 180.474 182.260 145.434 1.00 12.48 ? 207 GLU B O   1 
ATOM 5063 C CB  . GLU B 2 207  ? 178.805 180.829 147.910 1.00 4.22  ? 207 GLU B CB  1 
ATOM 5064 C CG  . GLU B 2 207  ? 177.347 181.020 148.316 1.00 9.01  ? 207 GLU B CG  1 
ATOM 5065 C CD  . GLU B 2 207  ? 176.583 179.710 148.435 1.00 15.34 ? 207 GLU B CD  1 
ATOM 5066 O OE1 . GLU B 2 207  ? 175.370 179.748 148.728 1.00 8.27  ? 207 GLU B OE1 1 
ATOM 5067 O OE2 . GLU B 2 207  ? 177.193 178.639 148.254 1.00 21.56 ? 207 GLU B OE2 1 
ATOM 5068 N N   . LEU B 2 208  ? 178.249 182.659 145.438 1.00 4.18  ? 208 LEU B N   1 
ATOM 5069 C CA  . LEU B 2 208  ? 178.315 184.046 144.995 1.00 0.00  ? 208 LEU B CA  1 
ATOM 5070 C C   . LEU B 2 208  ? 177.293 184.829 145.803 1.00 0.00  ? 208 LEU B C   1 
ATOM 5071 O O   . LEU B 2 208  ? 176.136 184.413 145.910 1.00 6.22  ? 208 LEU B O   1 
ATOM 5072 C CB  . LEU B 2 208  ? 178.045 184.169 143.488 1.00 0.00  ? 208 LEU B CB  1 
ATOM 5073 C CG  . LEU B 2 208  ? 177.877 185.554 142.854 1.00 0.00  ? 208 LEU B CG  1 
ATOM 5074 C CD1 . LEU B 2 208  ? 178.368 185.538 141.427 1.00 0.00  ? 208 LEU B CD1 1 
ATOM 5075 C CD2 . LEU B 2 208  ? 176.431 185.992 142.868 1.00 0.00  ? 208 LEU B CD2 1 
ATOM 5076 N N   . SER B 2 209  ? 177.721 185.950 146.392 1.00 0.00  ? 209 SER B N   1 
ATOM 5077 C CA  . SER B 2 209  ? 176.807 186.727 147.272 1.00 0.00  ? 209 SER B CA  1 
ATOM 5078 C C   . SER B 2 209  ? 176.632 188.157 146.751 1.00 0.00  ? 209 SER B C   1 
ATOM 5079 O O   . SER B 2 209  ? 177.607 188.709 146.204 1.00 0.00  ? 209 SER B O   1 
ATOM 5080 C CB  . SER B 2 209  ? 177.302 186.723 148.696 1.00 2.06  ? 209 SER B CB  1 
ATOM 5081 O OG  . SER B 2 209  ? 177.503 185.395 149.157 1.00 5.45  ? 209 SER B OG  1 
ATOM 5082 N N   . ILE B 2 210  ? 175.435 188.726 146.921 1.00 2.74  ? 210 ILE B N   1 
ATOM 5083 C CA  . ILE B 2 210  ? 175.165 190.129 146.488 1.00 0.24  ? 210 ILE B CA  1 
ATOM 5084 C C   . ILE B 2 210  ? 174.752 190.936 147.722 1.00 2.84  ? 210 ILE B C   1 
ATOM 5085 O O   . ILE B 2 210  ? 173.753 190.557 148.366 1.00 15.80 ? 210 ILE B O   1 
ATOM 5086 C CB  . ILE B 2 210  ? 174.073 190.168 145.400 1.00 0.00  ? 210 ILE B CB  1 
ATOM 5087 C CG1 . ILE B 2 210  ? 174.405 189.245 144.226 1.00 0.00  ? 210 ILE B CG1 1 
ATOM 5088 C CG2 . ILE B 2 210  ? 173.818 191.596 144.942 1.00 8.34  ? 210 ILE B CG2 1 
ATOM 5089 C CD1 . ILE B 2 210  ? 173.639 187.946 144.235 1.00 1.54  ? 210 ILE B CD1 1 
ATOM 5090 N N   . LEU B 2 211  ? 175.493 192.003 148.035 1.00 0.00  ? 211 LEU B N   1 
ATOM 5091 C CA  . LEU B 2 211  ? 175.188 192.817 149.242 1.00 0.00  ? 211 LEU B CA  1 
ATOM 5092 C C   . LEU B 2 211  ? 174.109 193.851 148.903 1.00 6.42  ? 211 LEU B C   1 
ATOM 5093 O O   . LEU B 2 211  ? 174.220 194.490 147.838 1.00 7.15  ? 211 LEU B O   1 
ATOM 5094 C CB  . LEU B 2 211  ? 176.468 193.504 149.728 1.00 4.60  ? 211 LEU B CB  1 
ATOM 5095 C CG  . LEU B 2 211  ? 176.284 194.458 150.907 1.00 1.19  ? 211 LEU B CG  1 
ATOM 5096 C CD1 . LEU B 2 211  ? 175.710 193.729 152.112 1.00 0.70  ? 211 LEU B CD1 1 
ATOM 5097 C CD2 . LEU B 2 211  ? 177.596 195.132 151.271 1.00 0.00  ? 211 LEU B CD2 1 
ATOM 5098 N N   . TYR B 2 212  ? 173.108 194.001 149.774 1.00 8.94  ? 212 TYR B N   1 
ATOM 5099 C CA  . TYR B 2 212  ? 172.055 195.032 149.567 1.00 6.70  ? 212 TYR B CA  1 
ATOM 5100 C C   . TYR B 2 212  ? 172.079 195.972 150.773 1.00 13.46 ? 212 TYR B C   1 
ATOM 5101 O O   . TYR B 2 212  ? 172.668 195.599 151.812 1.00 19.75 ? 212 TYR B O   1 
ATOM 5102 C CB  . TYR B 2 212  ? 170.713 194.328 149.343 1.00 6.75  ? 212 TYR B CB  1 
ATOM 5103 C CG  . TYR B 2 212  ? 170.406 194.031 147.882 1.00 8.71  ? 212 TYR B CG  1 
ATOM 5104 C CD1 . TYR B 2 212  ? 169.949 195.028 147.029 1.00 5.52  ? 212 TYR B CD1 1 
ATOM 5105 C CD2 . TYR B 2 212  ? 170.580 192.757 147.356 1.00 7.50  ? 212 TYR B CD2 1 
ATOM 5106 C CE1 . TYR B 2 212  ? 169.670 194.765 145.698 1.00 0.00  ? 212 TYR B CE1 1 
ATOM 5107 C CE2 . TYR B 2 212  ? 170.303 192.482 146.027 1.00 11.54 ? 212 TYR B CE2 1 
ATOM 5108 C CZ  . TYR B 2 212  ? 169.847 193.488 145.196 1.00 7.34  ? 212 TYR B CZ  1 
ATOM 5109 O OH  . TYR B 2 212  ? 169.571 193.228 143.884 1.00 7.32  ? 212 TYR B OH  1 
ATOM 5110 N N   . PRO B 2 213  ? 171.470 197.178 150.705 1.00 6.51  ? 213 PRO B N   1 
ATOM 5111 C CA  . PRO B 2 213  ? 171.547 198.143 151.808 1.00 10.54 ? 213 PRO B CA  1 
ATOM 5112 C C   . PRO B 2 213  ? 171.167 197.505 153.153 1.00 4.68  ? 213 PRO B C   1 
ATOM 5113 O O   . PRO B 2 213  ? 171.882 197.719 154.116 1.00 0.70  ? 213 PRO B O   1 
ATOM 5114 C CB  . PRO B 2 213  ? 170.529 199.231 151.427 1.00 9.39  ? 213 PRO B CB  1 
ATOM 5115 C CG  . PRO B 2 213  ? 169.735 198.643 150.276 1.00 1.12  ? 213 PRO B CG  1 
ATOM 5116 C CD  . PRO B 2 213  ? 170.684 197.688 149.583 1.00 0.00  ? 213 PRO B CD  1 
ATOM 5117 N N   . ALA B 2 214  ? 170.069 196.745 153.186 1.00 6.34  ? 214 ALA B N   1 
ATOM 5118 C CA  . ALA B 2 214  ? 169.633 196.078 154.435 1.00 12.78 ? 214 ALA B CA  1 
ATOM 5119 C C   . ALA B 2 214  ? 169.171 194.650 154.125 1.00 11.07 ? 214 ALA B C   1 
ATOM 5120 O O   . ALA B 2 214  ? 168.189 194.198 154.747 1.00 16.37 ? 214 ALA B O   1 
ATOM 5121 C CB  . ALA B 2 214  ? 168.538 196.882 155.092 1.00 13.84 ? 214 ALA B CB  1 
ATOM 5122 N N   . ALA B 2 215  ? 169.855 193.972 153.197 1.00 4.56  ? 215 ALA B N   1 
ATOM 5123 C CA  . ALA B 2 215  ? 169.466 192.594 152.813 1.00 6.38  ? 215 ALA B CA  1 
ATOM 5124 C C   . ALA B 2 215  ? 170.699 191.801 152.368 1.00 8.79  ? 215 ALA B C   1 
ATOM 5125 O O   . ALA B 2 215  ? 171.687 192.432 151.945 1.00 5.39  ? 215 ALA B O   1 
ATOM 5126 C CB  . ALA B 2 215  ? 168.420 192.639 151.726 1.00 4.16  ? 215 ALA B CB  1 
ATOM 5127 N N   . ILE B 2 216  ? 170.658 190.470 152.487 1.00 12.89 ? 216 ILE B N   1 
ATOM 5128 C CA  . ILE B 2 216  ? 171.787 189.618 151.999 1.00 7.73  ? 216 ILE B CA  1 
ATOM 5129 C C   . ILE B 2 216  ? 171.224 188.637 150.964 1.00 5.90  ? 216 ILE B C   1 
ATOM 5130 O O   . ILE B 2 216  ? 170.298 187.879 151.312 1.00 13.75 ? 216 ILE B O   1 
ATOM 5131 C CB  . ILE B 2 216  ? 172.493 188.885 153.160 1.00 0.00  ? 216 ILE B CB  1 
ATOM 5132 C CG1 . ILE B 2 216  ? 173.574 189.748 153.817 1.00 3.33  ? 216 ILE B CG1 1 
ATOM 5133 C CG2 . ILE B 2 216  ? 173.059 187.551 152.699 1.00 0.85  ? 216 ILE B CG2 1 
ATOM 5134 C CD1 . ILE B 2 216  ? 174.678 190.192 152.881 1.00 0.92  ? 216 ILE B CD1 1 
ATOM 5135 N N   . VAL B 2 217  ? 171.749 188.672 149.736 1.00 4.01  ? 217 VAL B N   1 
ATOM 5136 C CA  . VAL B 2 217  ? 171.293 187.724 148.677 1.00 0.00  ? 217 VAL B CA  1 
ATOM 5137 C C   . VAL B 2 217  ? 172.460 186.801 148.314 1.00 5.02  ? 217 VAL B C   1 
ATOM 5138 O O   . VAL B 2 217  ? 173.555 187.322 148.030 1.00 14.73 ? 217 VAL B O   1 
ATOM 5139 C CB  . VAL B 2 217  ? 170.767 188.479 147.441 1.00 0.00  ? 217 VAL B CB  1 
ATOM 5140 C CG1 . VAL B 2 217  ? 170.586 187.552 146.250 1.00 3.88  ? 217 VAL B CG1 1 
ATOM 5141 C CG2 . VAL B 2 217  ? 169.477 189.223 147.746 1.00 0.00  ? 217 VAL B CG2 1 
ATOM 5142 N N   . THR B 2 218  ? 172.230 185.486 148.332 1.00 1.07  ? 218 THR B N   1 
ATOM 5143 C CA  . THR B 2 218  ? 173.299 184.503 148.012 1.00 0.00  ? 218 THR B CA  1 
ATOM 5144 C C   . THR B 2 218  ? 172.853 183.618 146.844 1.00 0.00  ? 218 THR B C   1 
ATOM 5145 O O   . THR B 2 218  ? 171.699 183.145 146.873 1.00 4.07  ? 218 THR B O   1 
ATOM 5146 C CB  . THR B 2 218  ? 173.657 183.653 149.236 1.00 2.94  ? 218 THR B CB  1 
ATOM 5147 O OG1 . THR B 2 218  ? 172.473 182.975 149.657 1.00 0.00  ? 218 THR B OG1 1 
ATOM 5148 C CG2 . THR B 2 218  ? 174.219 184.471 150.378 1.00 3.71  ? 218 THR B CG2 1 
ATOM 5149 N N   . ILE B 2 219  ? 173.733 183.409 145.861 1.00 0.00  ? 219 ILE B N   1 
ATOM 5150 C CA  . ILE B 2 219  ? 173.410 182.519 144.705 1.00 0.80  ? 219 ILE B CA  1 
ATOM 5151 C C   . ILE B 2 219  ? 174.384 181.336 144.713 1.00 10.74 ? 219 ILE B C   1 
ATOM 5152 O O   . ILE B 2 219  ? 175.607 181.579 144.739 1.00 20.78 ? 219 ILE B O   1 
ATOM 5153 C CB  . ILE B 2 219  ? 173.470 183.300 143.377 1.00 0.00  ? 219 ILE B CB  1 
ATOM 5154 C CG1 . ILE B 2 219  ? 172.376 184.367 143.299 1.00 0.78  ? 219 ILE B CG1 1 
ATOM 5155 C CG2 . ILE B 2 219  ? 173.419 182.350 142.190 1.00 8.87  ? 219 ILE B CG2 1 
ATOM 5156 C CD1 . ILE B 2 219  ? 172.542 185.334 142.149 1.00 0.00  ? 219 ILE B CD1 1 
ATOM 5157 N N   . ASP B 2 220  ? 173.857 180.109 144.693 1.00 12.94 ? 220 ASP B N   1 
ATOM 5158 C CA  . ASP B 2 220  ? 174.717 178.895 144.705 1.00 12.41 ? 220 ASP B CA  1 
ATOM 5159 C C   . ASP B 2 220  ? 175.598 178.889 143.452 1.00 14.60 ? 220 ASP B C   1 
ATOM 5160 O O   . ASP B 2 220  ? 175.045 179.019 142.341 1.00 10.34 ? 220 ASP B O   1 
ATOM 5161 C CB  . ASP B 2 220  ? 173.874 177.623 144.826 1.00 13.95 ? 220 ASP B CB  1 
ATOM 5162 C CG  . ASP B 2 220  ? 173.243 177.439 146.195 1.00 16.08 ? 220 ASP B CG  1 
ATOM 5163 O OD1 . ASP B 2 220  ? 173.675 178.132 147.137 1.00 11.71 ? 220 ASP B OD1 1 
ATOM 5164 O OD2 . ASP B 2 220  ? 172.323 176.605 146.305 1.00 18.86 ? 220 ASP B OD2 1 
ATOM 5165 N N   . GLY B 2 221  ? 176.915 178.744 143.627 1.00 10.60 ? 221 GLY B N   1 
ATOM 5166 C CA  . GLY B 2 221  ? 177.820 178.714 142.493 1.00 12.74 ? 221 GLY B CA  1 
ATOM 5167 C C   . GLY B 2 221  ? 177.541 177.611 141.494 1.00 16.47 ? 221 GLY B C   1 
ATOM 5168 O O   . GLY B 2 221  ? 177.798 177.780 140.297 1.00 17.66 ? 221 GLY B O   1 
ATOM 5169 N N   . PHE B 2 222  ? 177.023 176.470 141.959 1.00 20.18 ? 222 PHE B N   1 
ATOM 5170 C CA  . PHE B 2 222  ? 176.710 175.377 141.043 1.00 19.72 ? 222 PHE B CA  1 
ATOM 5171 C C   . PHE B 2 222  ? 175.580 175.758 140.096 1.00 15.79 ? 222 PHE B C   1 
ATOM 5172 O O   . PHE B 2 222  ? 175.604 175.397 138.914 1.00 11.80 ? 222 PHE B O   1 
ATOM 5173 C CB  . PHE B 2 222  ? 176.350 174.116 141.827 1.00 19.86 ? 222 PHE B CB  1 
ATOM 5174 C CG  . PHE B 2 222  ? 176.448 172.852 141.020 1.00 18.93 ? 222 PHE B CG  1 
ATOM 5175 C CD1 . PHE B 2 222  ? 177.617 172.529 140.352 1.00 21.40 ? 222 PHE B CD1 1 
ATOM 5176 C CD2 . PHE B 2 222  ? 175.369 171.989 140.925 1.00 19.50 ? 222 PHE B CD2 1 
ATOM 5177 C CE1 . PHE B 2 222  ? 177.711 171.368 139.608 1.00 22.27 ? 222 PHE B CE1 1 
ATOM 5178 C CE2 . PHE B 2 222  ? 175.457 170.827 140.182 1.00 21.64 ? 222 PHE B CE2 1 
ATOM 5179 C CZ  . PHE B 2 222  ? 176.630 170.516 139.523 1.00 20.27 ? 222 PHE B CZ  1 
ATOM 5180 N N   . SER B 2 223  ? 174.577 176.481 140.599 1.00 16.07 ? 223 SER B N   1 
ATOM 5181 C CA  . SER B 2 223  ? 173.501 176.945 139.730 1.00 18.93 ? 223 SER B CA  1 
ATOM 5182 C C   . SER B 2 223  ? 174.032 177.889 138.661 1.00 20.49 ? 223 SER B C   1 
ATOM 5183 O O   . SER B 2 223  ? 173.611 177.825 137.501 1.00 18.39 ? 223 SER B O   1 
ATOM 5184 C CB  . SER B 2 223  ? 172.413 177.630 140.554 1.00 20.93 ? 223 SER B CB  1 
ATOM 5185 O OG  . SER B 2 223  ? 172.627 179.029 140.606 1.00 25.63 ? 223 SER B OG  1 
ATOM 5186 N N   . LEU B 2 224  ? 174.956 178.778 139.033 1.00 21.61 ? 224 LEU B N   1 
ATOM 5187 C CA  . LEU B 2 224  ? 175.569 179.651 138.039 1.00 20.25 ? 224 LEU B CA  1 
ATOM 5188 C C   . LEU B 2 224  ? 176.355 178.846 137.013 1.00 17.48 ? 224 LEU B C   1 
ATOM 5189 O O   . LEU B 2 224  ? 176.304 179.141 135.815 1.00 17.38 ? 224 LEU B O   1 
ATOM 5190 C CB  . LEU B 2 224  ? 176.468 180.684 138.717 1.00 14.53 ? 224 LEU B CB  1 
ATOM 5191 C CG  . LEU B 2 224  ? 176.489 182.080 138.086 1.00 12.01 ? 224 LEU B CG  1 
ATOM 5192 C CD1 . LEU B 2 224  ? 175.125 182.461 137.531 1.00 9.92  ? 224 LEU B CD1 1 
ATOM 5193 C CD2 . LEU B 2 224  ? 176.966 183.116 139.089 1.00 9.52  ? 224 LEU B CD2 1 
ATOM 5194 N N   . PHE B 2 225  ? 177.082 177.819 137.461 1.00 15.57 ? 225 PHE B N   1 
ATOM 5195 C CA  . PHE B 2 225  ? 177.844 177.004 136.518 1.00 17.42 ? 225 PHE B CA  1 
ATOM 5196 C C   . PHE B 2 225  ? 176.935 176.218 135.582 1.00 21.04 ? 225 PHE B C   1 
ATOM 5197 O O   . PHE B 2 225  ? 177.318 175.940 134.440 1.00 16.34 ? 225 PHE B O   1 
ATOM 5198 C CB  . PHE B 2 225  ? 178.773 176.049 137.266 1.00 17.61 ? 225 PHE B CB  1 
ATOM 5199 C CG  . PHE B 2 225  ? 179.771 175.361 136.379 1.00 21.02 ? 225 PHE B CG  1 
ATOM 5200 C CD1 . PHE B 2 225  ? 180.488 176.079 135.438 1.00 15.40 ? 225 PHE B CD1 1 
ATOM 5201 C CD2 . PHE B 2 225  ? 179.991 173.999 136.484 1.00 21.70 ? 225 PHE B CD2 1 
ATOM 5202 C CE1 . PHE B 2 225  ? 181.408 175.455 134.622 1.00 14.97 ? 225 PHE B CE1 1 
ATOM 5203 C CE2 . PHE B 2 225  ? 180.911 173.368 135.669 1.00 17.95 ? 225 PHE B CE2 1 
ATOM 5204 C CZ  . PHE B 2 225  ? 181.620 174.098 134.737 1.00 16.75 ? 225 PHE B CZ  1 
ATOM 5205 N N   . GLN B 2 226  ? 175.744 175.838 136.045 1.00 22.40 ? 226 GLN B N   1 
ATOM 5206 C CA  . GLN B 2 226  ? 174.822 175.085 135.206 1.00 13.96 ? 226 GLN B CA  1 
ATOM 5207 C C   . GLN B 2 226  ? 173.897 175.963 134.373 1.00 18.09 ? 226 GLN B C   1 
ATOM 5208 O O   . GLN B 2 226  ? 173.245 175.452 133.456 1.00 21.49 ? 226 GLN B O   1 
ATOM 5209 C CB  . GLN B 2 226  ? 173.979 174.130 136.060 1.00 14.35 ? 226 GLN B CB  1 
ATOM 5210 C CG  . GLN B 2 226  ? 174.744 172.999 136.772 1.00 20.06 ? 226 GLN B CG  1 
ATOM 5211 C CD  . GLN B 2 226  ? 175.407 171.962 135.854 1.00 20.59 ? 226 GLN B CD  1 
ATOM 5212 O OE1 . GLN B 2 226  ? 176.609 171.995 135.585 1.00 19.52 ? 226 GLN B OE1 1 
ATOM 5213 N NE2 . GLN B 2 226  ? 174.600 171.030 135.364 1.00 15.15 ? 226 GLN B NE2 1 
ATOM 5214 N N   . SER B 2 227  ? 173.814 177.258 134.668 1.00 20.57 ? 227 SER B N   1 
ATOM 5215 C CA  . SER B 2 227  ? 173.025 178.171 133.849 1.00 13.11 ? 227 SER B CA  1 
ATOM 5216 C C   . SER B 2 227  ? 173.861 178.942 132.837 1.00 13.63 ? 227 SER B C   1 
ATOM 5217 O O   . SER B 2 227  ? 173.402 179.174 131.714 1.00 20.61 ? 227 SER B O   1 
ATOM 5218 C CB  . SER B 2 227  ? 172.267 179.163 134.735 1.00 11.17 ? 227 SER B CB  1 
ATOM 5219 O OG  . SER B 2 227  ? 171.178 178.533 135.383 1.00 21.89 ? 227 SER B OG  1 
ATOM 5220 N N   . LEU B 2 228  ? 175.061 179.373 133.240 1.00 11.90 ? 228 LEU B N   1 
ATOM 5221 C CA  . LEU B 2 228  ? 175.911 180.202 132.341 1.00 10.25 ? 228 LEU B CA  1 
ATOM 5222 C C   . LEU B 2 228  ? 176.278 179.402 131.087 1.00 15.53 ? 228 LEU B C   1 
ATOM 5223 O O   . LEU B 2 228  ? 176.041 179.910 129.974 1.00 23.23 ? 228 LEU B O   1 
ATOM 5224 C CB  . LEU B 2 228  ? 177.170 180.637 133.098 1.00 10.63 ? 228 LEU B CB  1 
ATOM 5225 C CG  . LEU B 2 228  ? 176.967 181.757 134.116 1.00 15.36 ? 228 LEU B CG  1 
ATOM 5226 C CD1 . LEU B 2 228  ? 178.303 182.252 134.648 1.00 17.40 ? 228 LEU B CD1 1 
ATOM 5227 C CD2 . LEU B 2 228  ? 176.176 182.904 133.508 1.00 12.14 ? 228 LEU B CD2 1 
ATOM 5228 N N   . ARG B 2 229  ? 176.903 178.256 131.290 1.00 10.70 ? 229 ARG B N   1 
ATOM 5229 C CA  . ARG B 2 229  ? 177.250 177.375 130.159 1.00 12.30 ? 229 ARG B CA  1 
ATOM 5230 C C   . ARG B 2 229  ? 176.049 177.230 129.226 1.00 14.59 ? 229 ARG B C   1 
ATOM 5231 O O   . ARG B 2 229  ? 176.200 177.508 128.021 1.00 11.32 ? 229 ARG B O   1 
ATOM 5232 C CB  . ARG B 2 229  ? 177.560 176.041 130.816 1.00 10.69 ? 229 ARG B CB  1 
ATOM 5233 C CG  . ARG B 2 229  ? 177.686 174.886 129.836 1.00 14.00 ? 229 ARG B CG  1 
ATOM 5234 C CD  . ARG B 2 229  ? 178.020 173.562 130.530 1.00 14.60 ? 229 ARG B CD  1 
ATOM 5235 N NE  . ARG B 2 229  ? 177.191 173.253 131.684 1.00 14.61 ? 229 ARG B NE  1 
ATOM 5236 C CZ  . ARG B 2 229  ? 175.881 173.037 131.636 1.00 18.18 ? 229 ARG B CZ  1 
ATOM 5237 N NH1 . ARG B 2 229  ? 175.270 172.906 130.471 1.00 17.55 ? 229 ARG B NH1 1 
ATOM 5238 N NH2 . ARG B 2 229  ? 175.185 172.942 132.755 1.00 18.17 ? 229 ARG B NH2 1 
ATOM 5239 N N   . ALA B 2 230  ? 174.906 176.806 129.768 1.00 15.17 ? 230 ALA B N   1 
ATOM 5240 C CA  . ALA B 2 230  ? 173.683 176.580 128.964 1.00 18.38 ? 230 ALA B CA  1 
ATOM 5241 C C   . ALA B 2 230  ? 173.376 177.834 128.139 1.00 15.66 ? 230 ALA B C   1 
ATOM 5242 O O   . ALA B 2 230  ? 173.277 177.718 126.902 1.00 18.41 ? 230 ALA B O   1 
ATOM 5243 C CB  . ALA B 2 230  ? 172.533 176.223 129.872 1.00 14.66 ? 230 ALA B CB  1 
ATOM 5244 N N   . CYS B 2 231  ? 173.231 178.985 128.802 1.00 6.84  ? 231 CYS B N   1 
ATOM 5245 C CA  . CYS B 2 231  ? 172.928 180.227 128.099 1.00 9.71  ? 231 CYS B CA  1 
ATOM 5246 C C   . CYS B 2 231  ? 173.939 180.499 126.990 1.00 17.51 ? 231 CYS B C   1 
ATOM 5247 O O   . CYS B 2 231  ? 173.561 180.901 125.882 1.00 20.82 ? 231 CYS B O   1 
ATOM 5248 C CB  . CYS B 2 231  ? 172.883 181.388 129.089 1.00 15.58 ? 231 CYS B CB  1 
ATOM 5249 S SG  . CYS B 2 231  ? 171.433 181.374 130.166 1.00 31.40 ? 231 CYS B SG  1 
ATOM 5250 N N   . ARG B 2 232  ? 175.229 180.282 127.264 1.00 10.52 ? 232 ARG B N   1 
ATOM 5251 C CA  . ARG B 2 232  ? 176.241 180.496 126.233 1.00 11.35 ? 232 ARG B CA  1 
ATOM 5252 C C   . ARG B 2 232  ? 176.072 179.517 125.079 1.00 20.57 ? 232 ARG B C   1 
ATOM 5253 O O   . ARG B 2 232  ? 176.222 179.896 123.913 1.00 14.77 ? 232 ARG B O   1 
ATOM 5254 C CB  . ARG B 2 232  ? 177.643 180.379 126.830 1.00 3.31  ? 232 ARG B CB  1 
ATOM 5255 C CG  . ARG B 2 232  ? 178.753 180.367 125.791 1.00 0.80  ? 232 ARG B CG  1 
ATOM 5256 C CD  . ARG B 2 232  ? 180.045 180.904 126.369 1.00 3.09  ? 232 ARG B CD  1 
ATOM 5257 N NE  . ARG B 2 232  ? 181.182 180.699 125.481 1.00 7.33  ? 232 ARG B NE  1 
ATOM 5258 C CZ  . ARG B 2 232  ? 181.988 181.665 125.062 1.00 9.43  ? 232 ARG B CZ  1 
ATOM 5259 N NH1 . ARG B 2 232  ? 181.795 182.926 125.410 1.00 10.88 ? 232 ARG B NH1 1 
ATOM 5260 N NH2 . ARG B 2 232  ? 183.016 181.358 124.276 1.00 9.34  ? 232 ARG B NH2 1 
ATOM 5261 N N   . ASN B 2 233  ? 175.768 178.253 125.383 1.00 19.01 ? 233 ASN B N   1 
ATOM 5262 C CA  . ASN B 2 233  ? 175.561 177.265 124.331 1.00 15.95 ? 233 ASN B CA  1 
ATOM 5263 C C   . ASN B 2 233  ? 174.361 177.630 123.470 1.00 16.45 ? 233 ASN B C   1 
ATOM 5264 O O   . ASN B 2 233  ? 174.419 177.538 122.236 1.00 20.88 ? 233 ASN B O   1 
ATOM 5265 C CB  . ASN B 2 233  ? 175.384 175.881 124.953 1.00 13.67 ? 233 ASN B CB  1 
ATOM 5266 C CG  . ASN B 2 233  ? 175.791 174.764 124.019 1.00 17.01 ? 233 ASN B CG  1 
ATOM 5267 O OD1 . ASN B 2 233  ? 175.318 174.680 122.886 1.00 18.42 ? 233 ASN B OD1 1 
ATOM 5268 N ND2 . ASN B 2 233  ? 176.678 173.896 124.491 1.00 16.74 ? 233 ASN B ND2 1 
ATOM 5269 N N   . GLN B 2 234  ? 173.266 178.060 124.103 1.00 16.08 ? 234 GLN B N   1 
ATOM 5270 C CA  . GLN B 2 234  ? 172.095 178.488 123.348 1.00 18.58 ? 234 GLN B CA  1 
ATOM 5271 C C   . GLN B 2 234  ? 172.418 179.683 122.461 1.00 19.76 ? 234 GLN B C   1 
ATOM 5272 O O   . GLN B 2 234  ? 172.008 179.727 121.297 1.00 18.11 ? 234 GLN B O   1 
ATOM 5273 C CB  . GLN B 2 234  ? 170.948 178.818 124.304 1.00 18.74 ? 234 GLN B CB  1 
ATOM 5274 C CG  . GLN B 2 234  ? 169.825 179.640 123.689 1.00 19.57 ? 234 GLN B CG  1 
ATOM 5275 C CD  . GLN B 2 234  ? 170.043 181.137 123.837 1.00 21.35 ? 234 GLN B CD  1 
ATOM 5276 O OE1 . GLN B 2 234  ? 170.190 181.650 124.945 1.00 17.72 ? 234 GLN B OE1 1 
ATOM 5277 N NE2 . GLN B 2 234  ? 170.069 181.843 122.713 1.00 19.93 ? 234 GLN B NE2 1 
ATOM 5278 N N   . VAL B 2 235  ? 173.153 180.664 122.993 1.00 17.32 ? 235 VAL B N   1 
ATOM 5279 C CA  . VAL B 2 235  ? 173.486 181.850 122.206 1.00 20.65 ? 235 VAL B CA  1 
ATOM 5280 C C   . VAL B 2 235  ? 174.381 181.479 121.029 1.00 19.76 ? 235 VAL B C   1 
ATOM 5281 O O   . VAL B 2 235  ? 174.192 181.967 119.907 1.00 18.05 ? 235 VAL B O   1 
ATOM 5282 C CB  . VAL B 2 235  ? 174.136 182.920 123.104 1.00 16.38 ? 235 VAL B CB  1 
ATOM 5283 C CG1 . VAL B 2 235  ? 174.788 184.006 122.262 1.00 17.39 ? 235 VAL B CG1 1 
ATOM 5284 C CG2 . VAL B 2 235  ? 173.102 183.522 124.041 1.00 14.92 ? 235 VAL B CG2 1 
ATOM 5285 N N   . ALA B 2 236  ? 175.375 180.626 121.294 1.00 15.18 ? 236 ALA B N   1 
ATOM 5286 C CA  . ALA B 2 236  ? 176.290 180.181 120.218 1.00 22.47 ? 236 ALA B CA  1 
ATOM 5287 C C   . ALA B 2 236  ? 175.484 179.414 119.168 1.00 24.03 ? 236 ALA B C   1 
ATOM 5288 O O   . ALA B 2 236  ? 175.672 179.679 117.965 1.00 17.77 ? 236 ALA B O   1 
ATOM 5289 C CB  . ALA B 2 236  ? 177.393 179.331 120.797 1.00 21.59 ? 236 ALA B CB  1 
ATOM 5290 N N   . LYS B 2 237  ? 174.617 178.501 119.615 1.00 22.89 ? 237 LYS B N   1 
ATOM 5291 C CA  . LYS B 2 237  ? 173.770 177.721 118.675 1.00 19.73 ? 237 LYS B CA  1 
ATOM 5292 C C   . LYS B 2 237  ? 172.818 178.677 117.948 1.00 23.76 ? 237 LYS B C   1 
ATOM 5293 O O   . LYS B 2 237  ? 172.650 178.518 116.727 1.00 17.69 ? 237 LYS B O   1 
ATOM 5294 C CB  . LYS B 2 237  ? 172.992 176.642 119.434 1.00 17.45 ? 237 LYS B CB  1 
ATOM 5295 C CG  . LYS B 2 237  ? 173.829 175.502 119.997 1.00 17.16 ? 237 LYS B CG  1 
ATOM 5296 C CD  . LYS B 2 237  ? 173.023 174.550 120.855 1.00 22.49 ? 237 LYS B CD  1 
ATOM 5297 C CE  . LYS B 2 237  ? 171.962 173.805 120.073 1.00 23.12 ? 237 LYS B CE  1 
ATOM 5298 N NZ  . LYS B 2 237  ? 171.270 172.797 120.911 1.00 27.45 ? 237 LYS B NZ  1 
ATOM 5299 N N   . ALA B 2 238  ? 172.246 179.645 118.672 1.00 22.40 ? 238 ALA B N   1 
ATOM 5300 C CA  . ALA B 2 238  ? 171.347 180.642 118.045 1.00 21.42 ? 238 ALA B CA  1 
ATOM 5301 C C   . ALA B 2 238  ? 172.113 181.417 116.969 1.00 23.32 ? 238 ALA B C   1 
ATOM 5302 O O   . ALA B 2 238  ? 171.497 181.784 115.951 1.00 23.63 ? 238 ALA B O   1 
ATOM 5303 C CB  . ALA B 2 238  ? 170.786 181.570 119.094 1.00 16.97 ? 238 ALA B CB  1 
ATOM 5304 N N   . ALA B 2 239  ? 173.407 181.660 117.196 1.00 21.17 ? 239 ALA B N   1 
ATOM 5305 C CA  . ALA B 2 239  ? 174.228 182.407 116.216 1.00 20.19 ? 239 ALA B CA  1 
ATOM 5306 C C   . ALA B 2 239  ? 174.312 181.613 114.908 1.00 24.23 ? 239 ALA B C   1 
ATOM 5307 O O   . ALA B 2 239  ? 174.268 182.242 113.833 1.00 20.41 ? 239 ALA B O   1 
ATOM 5308 C CB  . ALA B 2 239  ? 175.598 182.679 116.788 1.00 18.38 ? 239 ALA B CB  1 
ATOM 5309 N N   . ALA B 2 240  ? 174.447 180.285 114.994 1.00 25.18 ? 240 ALA B N   1 
ATOM 5310 C CA  . ALA B 2 240  ? 174.627 179.464 113.772 1.00 23.56 ? 240 ALA B CA  1 
ATOM 5311 C C   . ALA B 2 240  ? 173.384 178.604 113.516 1.00 26.52 ? 240 ALA B C   1 
ATOM 5312 O O   . ALA B 2 240  ? 172.679 178.871 112.523 1.00 25.32 ? 240 ALA B O   1 
ATOM 5313 C CB  . ALA B 2 240  ? 175.863 178.611 113.911 1.00 19.17 ? 240 ALA B CB  1 
ATOM 5314 N N   . SER B 2 241  ? 173.127 177.619 114.382 1.00 26.29 ? 241 SER B N   1 
ATOM 5315 C CA  . SER B 2 241  ? 171.971 176.702 114.191 1.00 27.33 ? 241 SER B CA  1 
ATOM 5316 C C   . SER B 2 241  ? 170.666 177.502 114.150 1.00 25.11 ? 241 SER B C   1 
ATOM 5317 O O   . SER B 2 241  ? 169.684 176.995 113.575 1.00 22.02 ? 241 SER B O   1 
ATOM 5318 C CB  . SER B 2 241  ? 171.932 175.654 115.273 1.00 26.26 ? 241 SER B CB  1 
ATOM 5319 O OG  . SER B 2 241  ? 171.225 176.130 116.409 1.00 26.11 ? 241 SER B OG  1 
ATOM 5320 N N   . GLY B 2 242  ? 170.658 178.698 114.746 1.00 24.54 ? 242 GLY B N   1 
ATOM 5321 C CA  . GLY B 2 242  ? 169.435 179.523 114.786 1.00 24.69 ? 242 GLY B CA  1 
ATOM 5322 C C   . GLY B 2 242  ? 168.518 179.108 115.923 1.00 24.23 ? 242 GLY B C   1 
ATOM 5323 O O   . GLY B 2 242  ? 167.302 179.364 115.821 1.00 23.04 ? 242 GLY B O   1 
ATOM 5324 N N   . ASN B 2 243  ? 169.077 178.487 116.968 1.00 23.07 ? 243 ASN B N   1 
ATOM 5325 C CA  . ASN B 2 243  ? 168.273 178.060 118.145 1.00 25.61 ? 243 ASN B CA  1 
ATOM 5326 C C   . ASN B 2 243  ? 167.292 179.175 118.523 1.00 27.56 ? 243 ASN B C   1 
ATOM 5327 O O   . ASN B 2 243  ? 167.746 180.319 118.719 1.00 26.10 ? 243 ASN B O   1 
ATOM 5328 C CB  . ASN B 2 243  ? 169.166 177.683 119.329 1.00 26.21 ? 243 ASN B CB  1 
ATOM 5329 C CG  . ASN B 2 243  ? 168.395 177.085 120.486 1.00 24.47 ? 243 ASN B CG  1 
ATOM 5330 O OD1 . ASN B 2 243  ? 167.996 177.796 121.406 1.00 23.82 ? 243 ASN B OD1 1 
ATOM 5331 N ND2 . ASN B 2 243  ? 168.181 175.780 120.450 1.00 24.87 ? 243 ASN B ND2 1 
ATOM 5332 N N   . GLU B 2 244  ? 166.000 178.847 118.637 1.00 26.34 ? 244 GLU B N   1 
ATOM 5333 C CA  . GLU B 2 244  ? 164.974 179.861 119.002 1.00 25.65 ? 244 GLU B CA  1 
ATOM 5334 C C   . GLU B 2 244  ? 165.222 180.345 120.434 1.00 29.08 ? 244 GLU B C   1 
ATOM 5335 O O   . GLU B 2 244  ? 165.909 179.630 121.191 1.00 30.09 ? 244 GLU B O   1 
ATOM 5336 C CB  . GLU B 2 244  ? 163.569 179.271 118.861 1.00 24.07 ? 244 GLU B CB  1 
ATOM 5337 C CG  . GLU B 2 244  ? 162.504 180.308 118.552 1.00 25.69 ? 244 GLU B CG  1 
ATOM 5338 C CD  . GLU B 2 244  ? 162.998 181.516 117.775 1.00 27.57 ? 244 GLU B CD  1 
ATOM 5339 O OE1 . GLU B 2 244  ? 163.177 182.584 118.394 1.00 26.86 ? 244 GLU B OE1 1 
ATOM 5340 O OE2 . GLU B 2 244  ? 163.200 181.387 116.551 1.00 28.34 ? 244 GLU B OE2 1 
ATOM 5341 N N   . ASN B 2 245  ? 164.669 181.509 120.792 1.00 28.74 ? 245 ASN B N   1 
ATOM 5342 C CA  . ASN B 2 245  ? 164.839 182.053 122.166 1.00 27.62 ? 245 ASN B CA  1 
ATOM 5343 C C   . ASN B 2 245  ? 164.400 180.998 123.187 1.00 26.64 ? 245 ASN B C   1 
ATOM 5344 O O   . ASN B 2 245  ? 163.495 180.202 122.863 1.00 27.53 ? 245 ASN B O   1 
ATOM 5345 C CB  . ASN B 2 245  ? 164.071 183.364 122.355 1.00 23.26 ? 245 ASN B CB  1 
ATOM 5346 C CG  . ASN B 2 245  ? 162.571 183.187 122.246 1.00 25.43 ? 245 ASN B CG  1 
ATOM 5347 O OD1 . ASN B 2 245  ? 162.072 182.679 121.244 1.00 25.96 ? 245 ASN B OD1 1 
ATOM 5348 N ND2 . ASN B 2 245  ? 161.846 183.599 123.272 1.00 24.11 ? 245 ASN B ND2 1 
ATOM 5349 N N   . ILE B 2 246  ? 165.006 181.003 124.377 1.00 22.43 ? 246 ILE B N   1 
ATOM 5350 C CA  . ILE B 2 246  ? 164.689 179.961 125.397 1.00 23.49 ? 246 ILE B CA  1 
ATOM 5351 C C   . ILE B 2 246  ? 164.119 180.636 126.649 1.00 22.14 ? 246 ILE B C   1 
ATOM 5352 O O   . ILE B 2 246  ? 164.742 181.603 127.131 1.00 23.46 ? 246 ILE B O   1 
ATOM 5353 C CB  . ILE B 2 246  ? 165.946 179.128 125.719 1.00 23.68 ? 246 ILE B CB  1 
ATOM 5354 C CG1 . ILE B 2 246  ? 165.637 177.954 126.650 1.00 25.60 ? 246 ILE B CG1 1 
ATOM 5355 C CG2 . ILE B 2 246  ? 167.047 180.013 126.282 1.00 20.06 ? 246 ILE B CG2 1 
ATOM 5356 C CD1 . ILE B 2 246  ? 166.750 176.937 126.747 1.00 25.97 ? 246 ILE B CD1 1 
ATOM 5357 N N   . GLN B 2 247  ? 162.973 180.158 127.143 1.00 25.26 ? 247 GLN B N   1 
ATOM 5358 C CA  . GLN B 2 247  ? 162.417 180.698 128.413 1.00 27.32 ? 247 GLN B CA  1 
ATOM 5359 C C   . GLN B 2 247  ? 163.555 180.851 129.427 1.00 22.92 ? 247 GLN B C   1 
ATOM 5360 O O   . GLN B 2 247  ? 164.213 179.837 129.731 1.00 21.29 ? 247 GLN B O   1 
ATOM 5361 C CB  . GLN B 2 247  ? 161.325 179.774 128.954 1.00 27.81 ? 247 GLN B CB  1 
ATOM 5362 C CG  . GLN B 2 247  ? 160.080 179.725 128.080 1.00 26.73 ? 247 GLN B CG  1 
ATOM 5363 C CD  . GLN B 2 247  ? 159.053 178.751 128.602 1.00 27.50 ? 247 GLN B CD  1 
ATOM 5364 O OE1 . GLN B 2 247  ? 159.375 177.796 129.306 1.00 24.37 ? 247 GLN B OE1 1 
ATOM 5365 N NE2 . GLN B 2 247  ? 157.798 178.985 128.255 1.00 25.57 ? 247 GLN B NE2 1 
ATOM 5366 N N   . PRO B 2 248  ? 163.817 182.064 129.964 1.00 22.52 ? 248 PRO B N   1 
ATOM 5367 C CA  . PRO B 2 248  ? 164.937 182.280 130.884 1.00 27.65 ? 248 PRO B CA  1 
ATOM 5368 C C   . PRO B 2 248  ? 164.698 181.572 132.204 1.00 25.62 ? 248 PRO B C   1 
ATOM 5369 O O   . PRO B 2 248  ? 163.747 181.895 132.931 1.00 27.03 ? 248 PRO B O   1 
ATOM 5370 C CB  . PRO B 2 248  ? 164.958 183.807 131.066 1.00 28.92 ? 248 PRO B CB  1 
ATOM 5371 C CG  . PRO B 2 248  ? 164.077 184.354 129.969 1.00 26.20 ? 248 PRO B CG  1 
ATOM 5372 C CD  . PRO B 2 248  ? 163.054 183.298 129.730 1.00 24.75 ? 248 PRO B CD  1 
ATOM 5373 N N   . PRO B 2 249  ? 165.537 180.602 132.551 1.00 25.44 ? 249 PRO B N   1 
ATOM 5374 C CA  . PRO B 2 249  ? 165.342 179.861 133.800 1.00 27.18 ? 249 PRO B CA  1 
ATOM 5375 C C   . PRO B 2 249  ? 165.759 180.691 135.000 1.00 23.79 ? 249 PRO B C   1 
ATOM 5376 O O   . PRO B 2 249  ? 166.787 181.384 134.965 1.00 20.98 ? 249 PRO B O   1 
ATOM 5377 C CB  . PRO B 2 249  ? 166.247 178.633 133.626 1.00 29.98 ? 249 PRO B CB  1 
ATOM 5378 C CG  . PRO B 2 249  ? 167.314 179.084 132.690 1.00 29.83 ? 249 PRO B CG  1 
ATOM 5379 C CD  . PRO B 2 249  ? 166.696 180.113 131.782 1.00 25.03 ? 249 PRO B CD  1 
ATOM 5380 N N   . PRO B 2 250  ? 164.976 180.663 136.076 1.00 27.41 ? 250 PRO B N   1 
ATOM 5381 C CA  . PRO B 2 250  ? 165.373 181.366 137.300 1.00 27.98 ? 250 PRO B CA  1 
ATOM 5382 C C   . PRO B 2 250  ? 166.526 180.666 138.007 1.00 27.49 ? 250 PRO B C   1 
ATOM 5383 O O   . PRO B 2 250  ? 166.773 179.470 137.832 1.00 23.13 ? 250 PRO B O   1 
ATOM 5384 C CB  . PRO B 2 250  ? 164.100 181.339 138.157 1.00 24.13 ? 250 PRO B CB  1 
ATOM 5385 C CG  . PRO B 2 250  ? 162.988 181.043 137.193 1.00 27.10 ? 250 PRO B CG  1 
ATOM 5386 C CD  . PRO B 2 250  ? 163.598 180.156 136.157 1.00 25.95 ? 250 PRO B CD  1 
ATOM 5387 N N   . LEU B 2 251  ? 167.234 181.441 138.822 1.00 23.53 ? 251 LEU B N   1 
ATOM 5388 C CA  . LEU B 2 251  ? 168.370 180.956 139.593 1.00 21.93 ? 251 LEU B CA  1 
ATOM 5389 C C   . LEU B 2 251  ? 167.975 180.728 141.048 1.00 15.55 ? 251 LEU B C   1 
ATOM 5390 O O   . LEU B 2 251  ? 166.866 181.047 141.480 1.00 13.46 ? 251 LEU B O   1 
ATOM 5391 C CB  . LEU B 2 251  ? 169.535 181.948 139.521 1.00 16.04 ? 251 LEU B CB  1 
ATOM 5392 C CG  . LEU B 2 251  ? 170.007 182.416 138.147 1.00 21.76 ? 251 LEU B CG  1 
ATOM 5393 C CD1 . LEU B 2 251  ? 169.598 183.857 137.917 1.00 19.76 ? 251 LEU B CD1 1 
ATOM 5394 C CD2 . LEU B 2 251  ? 171.511 182.264 138.034 1.00 22.05 ? 251 LEU B CD2 1 
ATOM 5395 N N   . ALA B 2 252  ? 168.912 180.162 141.807 1.00 12.93 ? 252 ALA B N   1 
ATOM 5396 C CA  . ALA B 2 252  ? 168.749 180.072 143.250 1.00 19.04 ? 252 ALA B CA  1 
ATOM 5397 C C   . ALA B 2 252  ? 168.768 181.470 143.852 1.00 19.31 ? 252 ALA B C   1 
ATOM 5398 O O   . ALA B 2 252  ? 169.448 182.369 143.349 1.00 24.31 ? 252 ALA B O   1 
ATOM 5399 C CB  . ALA B 2 252  ? 169.852 179.212 143.863 1.00 18.75 ? 252 ALA B CB  1 
ATOM 5400 N N   . TYR B 2 253  ? 168.007 181.661 144.928 1.00 16.25 ? 253 TYR B N   1 
ATOM 5401 C CA  . TYR B 2 253  ? 167.789 183.009 145.445 1.00 16.15 ? 253 TYR B CA  1 
ATOM 5402 C C   . TYR B 2 253  ? 167.337 182.906 146.896 1.00 19.65 ? 253 TYR B C   1 
ATOM 5403 O O   . TYR B 2 253  ? 166.213 182.472 147.160 1.00 27.26 ? 253 TYR B O   1 
ATOM 5404 C CB  . TYR B 2 253  ? 166.758 183.725 144.578 1.00 14.78 ? 253 TYR B CB  1 
ATOM 5405 C CG  . TYR B 2 253  ? 166.459 185.154 144.949 1.00 13.18 ? 253 TYR B CG  1 
ATOM 5406 C CD1 . TYR B 2 253  ? 167.365 185.916 145.670 1.00 14.66 ? 253 TYR B CD1 1 
ATOM 5407 C CD2 . TYR B 2 253  ? 165.270 185.750 144.553 1.00 21.01 ? 253 TYR B CD2 1 
ATOM 5408 C CE1 . TYR B 2 253  ? 167.086 187.225 146.002 1.00 21.06 ? 253 TYR B CE1 1 
ATOM 5409 C CE2 . TYR B 2 253  ? 164.984 187.057 144.877 1.00 23.69 ? 253 TYR B CE2 1 
ATOM 5410 C CZ  . TYR B 2 253  ? 165.894 187.790 145.603 1.00 23.58 ? 253 TYR B CZ  1 
ATOM 5411 O OH  . TYR B 2 253  ? 165.611 189.097 145.928 1.00 26.69 ? 253 TYR B OH  1 
ATOM 5412 N N   . LYS B 2 254  ? 168.203 183.308 147.826 1.00 14.90 ? 254 LYS B N   1 
ATOM 5413 C CA  . LYS B 2 254  ? 167.887 183.328 149.253 1.00 13.07 ? 254 LYS B CA  1 
ATOM 5414 C C   . LYS B 2 254  ? 168.117 184.740 149.774 1.00 13.28 ? 254 LYS B C   1 
ATOM 5415 O O   . LYS B 2 254  ? 169.265 185.160 149.951 1.00 16.28 ? 254 LYS B O   1 
ATOM 5416 C CB  . LYS B 2 254  ? 168.738 182.322 150.025 1.00 13.07 ? 254 LYS B CB  1 
ATOM 5417 C CG  . LYS B 2 254  ? 168.848 180.959 149.371 1.00 14.42 ? 254 LYS B CG  1 
ATOM 5418 C CD  . LYS B 2 254  ? 169.775 180.048 150.160 1.00 18.72 ? 254 LYS B CD  1 
ATOM 5419 C CE  . LYS B 2 254  ? 169.465 180.097 151.648 1.00 20.76 ? 254 LYS B CE  1 
ATOM 5420 N NZ  . LYS B 2 254  ? 168.058 179.709 151.946 1.00 19.51 ? 254 LYS B NZ  1 
ATOM 5421 N N   . LYS B 2 255  ? 167.028 185.472 150.023 1.00 16.84 ? 255 LYS B N   1 
ATOM 5422 C CA  . LYS B 2 255  ? 167.154 186.878 150.493 1.00 10.00 ? 255 LYS B CA  1 
ATOM 5423 C C   . LYS B 2 255  ? 167.060 186.923 152.022 1.00 14.93 ? 255 LYS B C   1 
ATOM 5424 O O   . LYS B 2 255  ? 166.007 186.530 152.559 1.00 23.22 ? 255 LYS B O   1 
ATOM 5425 C CB  . LYS B 2 255  ? 166.076 187.760 149.856 1.00 8.71  ? 255 LYS B CB  1 
ATOM 5426 C CG  . LYS B 2 255  ? 166.160 189.238 150.216 1.00 16.69 ? 255 LYS B CG  1 
ATOM 5427 C CD  . LYS B 2 255  ? 165.108 190.077 149.529 1.00 19.21 ? 255 LYS B CD  1 
ATOM 5428 C CE  . LYS B 2 255  ? 165.184 191.539 149.911 1.00 18.70 ? 255 LYS B CE  1 
ATOM 5429 N NZ  . LYS B 2 255  ? 164.144 192.342 149.225 1.00 17.74 ? 255 LYS B NZ  1 
ATOM 5430 N N   . TRP B 2 256  ? 168.119 187.389 152.690 1.00 16.39 ? 256 TRP B N   1 
ATOM 5431 C CA  . TRP B 2 256  ? 168.099 187.518 154.170 1.00 13.81 ? 256 TRP B CA  1 
ATOM 5432 C C   . TRP B 2 256  ? 167.753 188.957 154.551 1.00 14.67 ? 256 TRP B C   1 
ATOM 5433 O O   . TRP B 2 256  ? 168.386 189.883 154.005 1.00 18.63 ? 256 TRP B O   1 
ATOM 5434 C CB  . TRP B 2 256  ? 169.456 187.120 154.763 1.00 8.98  ? 256 TRP B CB  1 
ATOM 5435 C CG  . TRP B 2 256  ? 169.570 185.656 155.093 1.00 11.79 ? 256 TRP B CG  1 
ATOM 5436 C CD1 . TRP B 2 256  ? 169.037 185.008 156.168 1.00 15.45 ? 256 TRP B CD1 1 
ATOM 5437 C CD2 . TRP B 2 256  ? 170.276 184.656 154.329 1.00 12.44 ? 256 TRP B CD2 1 
ATOM 5438 N NE1 . TRP B 2 256  ? 169.358 183.678 156.127 1.00 12.83 ? 256 TRP B NE1 1 
ATOM 5439 C CE2 . TRP B 2 256  ? 170.117 183.432 155.013 1.00 10.84 ? 256 TRP B CE2 1 
ATOM 5440 C CE3 . TRP B 2 256  ? 171.019 184.677 153.144 1.00 14.94 ? 256 TRP B CE3 1 
ATOM 5441 C CZ2 . TRP B 2 256  ? 170.676 182.245 154.547 1.00 15.92 ? 256 TRP B CZ2 1 
ATOM 5442 C CZ3 . TRP B 2 256  ? 171.571 183.502 152.686 1.00 15.59 ? 256 TRP B CZ3 1 
ATOM 5443 C CH2 . TRP B 2 256  ? 171.403 182.306 153.380 1.00 15.80 ? 256 TRP B CH2 1 
ATOM 5444 N N   . GLY B 2 257  ? 166.788 189.134 155.457 1.00 11.50 ? 257 GLY B N   1 
ATOM 5445 C CA  . GLY B 2 257  ? 166.407 190.486 155.909 1.00 11.70 ? 257 GLY B CA  1 
ATOM 5446 C C   . GLY B 2 257  ? 167.257 190.938 157.082 1.00 11.45 ? 257 GLY B C   1 
ATOM 5447 O O   . GLY B 2 257  ? 166.913 190.585 158.225 1.00 16.88 ? 257 GLY B O   1 
ATOM 5448 N N   . LEU B 2 258  ? 168.290 191.757 156.847 1.00 10.38 ? 258 LEU B N   1 
ATOM 5449 C CA  . LEU B 2 258  ? 169.199 192.226 157.936 1.00 12.11 ? 258 LEU B CA  1 
ATOM 5450 C C   . LEU B 2 258  ? 168.430 193.100 158.940 1.00 11.50 ? 258 LEU B C   1 
ATOM 5451 O O   . LEU B 2 258  ? 167.386 193.654 158.541 1.00 15.41 ? 258 LEU B O   1 
ATOM 5452 C CB  . LEU B 2 258  ? 170.365 192.996 157.307 1.00 11.37 ? 258 LEU B CB  1 
ATOM 5453 C CG  . LEU B 2 258  ? 171.211 192.196 156.319 1.00 12.03 ? 258 LEU B CG  1 
ATOM 5454 C CD1 . LEU B 2 258  ? 172.392 193.017 155.825 1.00 7.45  ? 258 LEU B CD1 1 
ATOM 5455 C CD2 . LEU B 2 258  ? 171.689 190.895 156.946 1.00 13.07 ? 258 LEU B CD2 1 
ATOM 5456 N N   . GLN B 2 259  ? 168.929 193.244 160.180 1.00 6.81  ? 259 GLN B N   1 
ATOM 5457 C CA  . GLN B 2 259  ? 168.167 193.991 161.224 1.00 7.87  ? 259 GLN B CA  1 
ATOM 5458 C C   . GLN B 2 259  ? 169.075 194.617 162.295 1.00 14.99 ? 259 GLN B C   1 
ATOM 5459 O O   . GLN B 2 259  ? 170.280 194.295 162.300 1.00 18.29 ? 259 GLN B O   1 
ATOM 5460 C CB  . GLN B 2 259  ? 167.186 193.049 161.925 1.00 9.38  ? 259 GLN B CB  1 
ATOM 5461 C CG  . GLN B 2 259  ? 166.060 192.548 161.033 1.00 12.52 ? 259 GLN B CG  1 
ATOM 5462 C CD  . GLN B 2 259  ? 165.166 191.568 161.752 1.00 17.27 ? 259 GLN B CD  1 
ATOM 5463 O OE1 . GLN B 2 259  ? 165.575 190.907 162.704 1.00 21.48 ? 259 GLN B OE1 1 
ATOM 5464 N NE2 . GLN B 2 259  ? 163.928 191.466 161.296 1.00 17.55 ? 259 GLN B NE2 1 
ATOM 5465 N N   . ASP B 2 260  ? 168.484 195.452 163.175 1.00 21.68 ? 260 ASP B N   1 
ATOM 5466 C CA  . ASP B 2 260  ? 169.206 196.201 164.254 1.00 20.08 ? 260 ASP B CA  1 
ATOM 5467 C C   . ASP B 2 260  ? 170.500 196.807 163.731 1.00 19.87 ? 260 ASP B C   1 
ATOM 5468 O O   . ASP B 2 260  ? 171.511 196.800 164.461 1.00 17.04 ? 260 ASP B O   1 
ATOM 5469 C CB  . ASP B 2 260  ? 169.467 195.395 165.512 1.00 17.80 ? 260 ASP B CB  1 
ATOM 5470 C CG  . ASP B 2 260  ? 168.208 195.117 166.316 1.00 21.39 ? 260 ASP B CG  1 
ATOM 5471 O OD1 . ASP B 2 260  ? 167.188 195.784 166.053 1.00 23.27 ? 260 ASP B OD1 1 
ATOM 5472 O OD2 . ASP B 2 260  ? 168.256 194.234 167.194 1.00 20.14 ? 260 ASP B OD2 1 
ATOM 5473 N N   . ILE B 2 261  ? 170.461 197.302 162.488 1.00 22.01 ? 261 ILE B N   1 
ATOM 5474 C CA  . ILE B 2 261  ? 171.633 197.995 161.876 1.00 21.86 ? 261 ILE B CA  1 
ATOM 5475 C C   . ILE B 2 261  ? 171.102 199.296 161.261 1.00 20.63 ? 261 ILE B C   1 
ATOM 5476 O O   . ILE B 2 261  ? 169.943 199.298 160.800 1.00 16.87 ? 261 ILE B O   1 
ATOM 5477 C CB  . ILE B 2 261  ? 172.335 197.100 160.832 1.00 21.19 ? 261 ILE B CB  1 
ATOM 5478 C CG1 . ILE B 2 261  ? 171.350 196.421 159.873 1.00 24.72 ? 261 ILE B CG1 1 
ATOM 5479 C CG2 . ILE B 2 261  ? 173.230 196.081 161.519 1.00 9.04  ? 261 ILE B CG2 1 
ATOM 5480 C CD1 . ILE B 2 261  ? 171.001 197.225 158.643 1.00 21.49 ? 261 ILE B CD1 1 
ATOM 5481 N N   . ASP B 2 262  ? 171.901 200.366 161.282 1.00 20.46 ? 262 ASP B N   1 
ATOM 5482 C CA  . ASP B 2 262  ? 171.455 201.666 160.712 1.00 20.96 ? 262 ASP B CA  1 
ATOM 5483 C C   . ASP B 2 262  ? 172.041 201.832 159.305 1.00 23.17 ? 262 ASP B C   1 
ATOM 5484 O O   . ASP B 2 262  ? 171.261 202.101 158.371 1.00 26.06 ? 262 ASP B O   1 
ATOM 5485 C CB  . ASP B 2 262  ? 171.804 202.837 161.633 1.00 22.41 ? 262 ASP B CB  1 
ATOM 5486 C CG  . ASP B 2 262  ? 171.042 202.806 162.947 1.00 27.35 ? 262 ASP B CG  1 
ATOM 5487 O OD1 . ASP B 2 262  ? 170.280 201.842 163.159 1.00 28.49 ? 262 ASP B OD1 1 
ATOM 5488 O OD2 . ASP B 2 262  ? 171.206 203.753 163.742 1.00 27.51 ? 262 ASP B OD2 1 
ATOM 5489 N N   . THR B 2 263  ? 173.361 201.677 159.167 1.00 20.13 ? 263 THR B N   1 
ATOM 5490 C CA  . THR B 2 263  ? 174.020 201.841 157.843 1.00 19.78 ? 263 THR B CA  1 
ATOM 5491 C C   . THR B 2 263  ? 175.011 200.694 157.622 1.00 20.93 ? 263 THR B C   1 
ATOM 5492 O O   . THR B 2 263  ? 175.821 200.439 158.535 1.00 23.54 ? 263 THR B O   1 
ATOM 5493 C CB  . THR B 2 263  ? 174.713 203.207 157.745 1.00 15.55 ? 263 THR B CB  1 
ATOM 5494 O OG1 . THR B 2 263  ? 173.716 204.219 157.889 1.00 14.29 ? 263 THR B OG1 1 
ATOM 5495 C CG2 . THR B 2 263  ? 175.457 203.405 156.443 1.00 15.72 ? 263 THR B CG2 1 
ATOM 5496 N N   . ILE B 2 264  ? 174.939 200.021 156.469 1.00 13.32 ? 264 ILE B N   1 
ATOM 5497 C CA  . ILE B 2 264  ? 175.914 198.936 156.145 1.00 9.92  ? 264 ILE B CA  1 
ATOM 5498 C C   . ILE B 2 264  ? 176.606 199.292 154.825 1.00 7.85  ? 264 ILE B C   1 
ATOM 5499 O O   . ILE B 2 264  ? 175.896 199.673 153.873 1.00 9.47  ? 264 ILE B O   1 
ATOM 5500 C CB  . ILE B 2 264  ? 175.217 197.561 156.084 1.00 9.38  ? 264 ILE B CB  1 
ATOM 5501 C CG1 . ILE B 2 264  ? 174.493 197.232 157.393 1.00 9.01  ? 264 ILE B CG1 1 
ATOM 5502 C CG2 . ILE B 2 264  ? 176.202 196.466 155.701 1.00 9.19  ? 264 ILE B CG2 1 
ATOM 5503 C CD1 . ILE B 2 264  ? 175.392 197.205 158.606 1.00 5.15  ? 264 ILE B CD1 1 
ATOM 5504 N N   . ILE B 2 265  ? 177.937 199.185 154.778 1.00 0.52  ? 265 ILE B N   1 
ATOM 5505 C CA  . ILE B 2 265  ? 178.695 199.576 153.551 1.00 0.00  ? 265 ILE B CA  1 
ATOM 5506 C C   . ILE B 2 265  ? 179.259 198.322 152.880 1.00 4.43  ? 265 ILE B C   1 
ATOM 5507 O O   . ILE B 2 265  ? 179.060 198.171 151.658 1.00 13.18 ? 265 ILE B O   1 
ATOM 5508 C CB  . ILE B 2 265  ? 179.816 200.571 153.911 1.00 1.89  ? 265 ILE B CB  1 
ATOM 5509 C CG1 . ILE B 2 265  ? 179.268 201.810 154.623 1.00 11.01 ? 265 ILE B CG1 1 
ATOM 5510 C CG2 . ILE B 2 265  ? 180.630 200.940 152.681 1.00 7.55  ? 265 ILE B CG2 1 
ATOM 5511 C CD1 . ILE B 2 265  ? 178.322 202.631 153.779 1.00 11.17 ? 265 ILE B CD1 1 
ATOM 5512 N N   . ASP B 2 266  ? 179.931 197.459 153.646 1.00 1.25  ? 266 ASP B N   1 
ATOM 5513 C CA  . ASP B 2 266  ? 180.564 196.278 153.079 1.00 4.06  ? 266 ASP B CA  1 
ATOM 5514 C C   . ASP B 2 266  ? 180.163 195.047 153.877 1.00 3.61  ? 266 ASP B C   1 
ATOM 5515 O O   . ASP B 2 266  ? 179.564 195.139 154.951 1.00 6.24  ? 266 ASP B O   1 
ATOM 5516 C CB  . ASP B 2 266  ? 182.091 196.414 153.054 1.00 6.89  ? 266 ASP B CB  1 
ATOM 5517 C CG  . ASP B 2 266  ? 182.621 196.761 151.682 1.00 9.06  ? 266 ASP B CG  1 
ATOM 5518 O OD1 . ASP B 2 266  ? 181.800 196.998 150.775 1.00 0.96  ? 266 ASP B OD1 1 
ATOM 5519 O OD2 . ASP B 2 266  ? 183.856 196.785 151.506 1.00 12.75 ? 266 ASP B OD2 1 
ATOM 5520 N N   . HIS B 2 267  ? 180.500 193.881 153.334 1.00 0.00  ? 267 HIS B N   1 
ATOM 5521 C CA  . HIS B 2 267  ? 180.206 192.624 153.999 1.00 0.00  ? 267 HIS B CA  1 
ATOM 5522 C C   . HIS B 2 267  ? 181.207 191.577 153.543 1.00 5.79  ? 267 HIS B C   1 
ATOM 5523 O O   . HIS B 2 267  ? 181.852 191.715 152.502 1.00 1.41  ? 267 HIS B O   1 
ATOM 5524 C CB  . HIS B 2 267  ? 178.768 192.163 153.727 1.00 0.00  ? 267 HIS B CB  1 
ATOM 5525 C CG  . HIS B 2 267  ? 178.631 191.237 152.557 1.00 0.00  ? 267 HIS B CG  1 
ATOM 5526 N ND1 . HIS B 2 267  ? 179.028 191.579 151.283 1.00 0.00  ? 267 HIS B ND1 1 
ATOM 5527 C CD2 . HIS B 2 267  ? 178.116 189.988 152.467 1.00 0.00  ? 267 HIS B CD2 1 
ATOM 5528 C CE1 . HIS B 2 267  ? 178.775 190.577 150.460 1.00 0.00  ? 267 HIS B CE1 1 
ATOM 5529 N NE2 . HIS B 2 267  ? 178.220 189.600 151.153 1.00 0.00  ? 267 HIS B NE2 1 
ATOM 5530 N N   . ALA B 2 268  ? 181.341 190.532 154.354 1.00 0.00  ? 268 ALA B N   1 
ATOM 5531 C CA  . ALA B 2 268  ? 182.191 189.397 154.039 1.00 0.00  ? 268 ALA B CA  1 
ATOM 5532 C C   . ALA B 2 268  ? 181.475 188.129 154.468 1.00 0.00  ? 268 ALA B C   1 
ATOM 5533 O O   . ALA B 2 268  ? 180.894 188.073 155.554 1.00 0.00  ? 268 ALA B O   1 
ATOM 5534 C CB  . ALA B 2 268  ? 183.555 189.494 154.732 1.00 0.00  ? 268 ALA B CB  1 
ATOM 5535 N N   . SER B 2 269  ? 181.518 187.116 153.611 1.00 3.65  ? 269 SER B N   1 
ATOM 5536 C CA  . SER B 2 269  ? 180.827 185.855 153.858 1.00 3.54  ? 269 SER B CA  1 
ATOM 5537 C C   . SER B 2 269  ? 181.832 184.881 154.461 1.00 7.60  ? 269 SER B C   1 
ATOM 5538 O O   . SER B 2 269  ? 182.554 184.182 153.749 1.00 4.44  ? 269 SER B O   1 
ATOM 5539 C CB  . SER B 2 269  ? 180.210 185.315 152.575 1.00 0.11  ? 269 SER B CB  1 
ATOM 5540 O OG  . SER B 2 269  ? 181.122 185.404 151.495 1.00 1.07  ? 269 SER B OG  1 
ATOM 5541 N N   . VAL B 2 270  ? 181.879 184.846 155.795 1.00 10.60 ? 270 VAL B N   1 
ATOM 5542 C CA  . VAL B 2 270  ? 182.708 183.863 156.487 1.00 7.56  ? 270 VAL B CA  1 
ATOM 5543 C C   . VAL B 2 270  ? 182.228 182.456 156.165 1.00 8.30  ? 270 VAL B C   1 
ATOM 5544 O O   . VAL B 2 270  ? 183.034 181.547 155.924 1.00 0.00  ? 270 VAL B O   1 
ATOM 5545 C CB  . VAL B 2 270  ? 182.705 184.133 158.003 1.00 0.00  ? 270 VAL B CB  1 
ATOM 5546 C CG1 . VAL B 2 270  ? 183.501 183.068 158.731 1.00 4.00  ? 270 VAL B CG1 1 
ATOM 5547 C CG2 . VAL B 2 270  ? 183.271 185.507 158.291 1.00 0.00  ? 270 VAL B CG2 1 
ATOM 5548 N N   . GLY B 2 271  ? 180.914 182.251 156.156 1.00 7.12  ? 271 GLY B N   1 
ATOM 5549 C CA  . GLY B 2 271  ? 180.378 180.994 155.669 1.00 6.34  ? 271 GLY B CA  1 
ATOM 5550 C C   . GLY B 2 271  ? 179.966 180.029 156.758 1.00 12.75 ? 271 GLY B C   1 
ATOM 5551 O O   . GLY B 2 271  ? 179.630 180.450 157.866 1.00 13.95 ? 271 GLY B O   1 
ATOM 5552 N N   . ILE B 2 272  ? 179.982 178.735 156.455 1.00 13.81 ? 272 ILE B N   1 
ATOM 5553 C CA  . ILE B 2 272  ? 179.510 177.724 157.394 1.00 15.59 ? 272 ILE B CA  1 
ATOM 5554 C C   . ILE B 2 272  ? 180.632 177.359 158.356 1.00 11.82 ? 272 ILE B C   1 
ATOM 5555 O O   . ILE B 2 272  ? 181.809 177.324 157.981 1.00 7.20  ? 272 ILE B O   1 
ATOM 5556 C CB  . ILE B 2 272  ? 178.982 176.492 156.636 1.00 14.47 ? 272 ILE B CB  1 
ATOM 5557 C CG1 . ILE B 2 272  ? 178.102 175.643 157.551 1.00 15.01 ? 272 ILE B CG1 1 
ATOM 5558 C CG2 . ILE B 2 272  ? 180.123 175.666 156.060 1.00 15.99 ? 272 ILE B CG2 1 
ATOM 5559 C CD1 . ILE B 2 272  ? 176.942 176.402 158.130 1.00 15.52 ? 272 ILE B CD1 1 
ATOM 5560 N N   . MET B 2 273  ? 180.240 177.168 159.620 1.00 13.63 ? 273 MET B N   1 
ATOM 5561 C CA  . MET B 2 273  ? 181.228 176.841 160.677 1.00 18.77 ? 273 MET B CA  1 
ATOM 5562 C C   . MET B 2 273  ? 180.585 175.882 161.679 1.00 15.79 ? 273 MET B C   1 
ATOM 5563 O O   . MET B 2 273  ? 179.340 175.804 161.706 1.00 17.52 ? 273 MET B O   1 
ATOM 5564 C CB  . MET B 2 273  ? 181.667 178.104 161.424 1.00 18.45 ? 273 MET B CB  1 
ATOM 5565 C CG  . MET B 2 273  ? 182.532 179.040 160.601 1.00 18.33 ? 273 MET B CG  1 
ATOM 5566 S SD  . MET B 2 273  ? 184.160 178.338 160.234 1.00 24.91 ? 273 MET B SD  1 
ATOM 5567 C CE  . MET B 2 273  ? 184.713 179.448 158.941 1.00 12.15 ? 273 MET B CE  1 
ATOM 5568 N N   . THR B 2 274  ? 181.401 175.186 162.467 1.00 10.54 ? 274 THR B N   1 
ATOM 5569 C CA  . THR B 2 274  ? 180.937 174.254 163.483 1.00 15.22 ? 274 THR B CA  1 
ATOM 5570 C C   . THR B 2 274  ? 181.522 174.634 164.835 1.00 15.33 ? 274 THR B C   1 
ATOM 5571 O O   . THR B 2 274  ? 182.629 175.173 164.921 1.00 17.10 ? 274 THR B O   1 
ATOM 5572 C CB  . THR B 2 274  ? 181.325 172.808 163.145 1.00 19.10 ? 274 THR B CB  1 
ATOM 5573 O OG1 . THR B 2 274  ? 182.740 172.730 162.934 1.00 23.12 ? 274 THR B OG1 1 
ATOM 5574 C CG2 . THR B 2 274  ? 180.606 172.341 161.890 1.00 14.93 ? 274 THR B CG2 1 
ATOM 5575 N N   . LEU B 2 275  ? 180.769 174.342 165.893 1.00 12.98 ? 275 LEU B N   1 
ATOM 5576 C CA  . LEU B 2 275  ? 181.144 174.708 167.251 1.00 11.70 ? 275 LEU B CA  1 
ATOM 5577 C C   . LEU B 2 275  ? 181.495 173.471 168.067 1.00 10.30 ? 275 LEU B C   1 
ATOM 5578 O O   . LEU B 2 275  ? 180.805 172.449 168.000 1.00 2.86  ? 275 LEU B O   1 
ATOM 5579 C CB  . LEU B 2 275  ? 180.017 175.472 167.954 1.00 6.91  ? 275 LEU B CB  1 
ATOM 5580 C CG  . LEU B 2 275  ? 179.777 176.931 167.569 1.00 3.94  ? 275 LEU B CG  1 
ATOM 5581 C CD1 . LEU B 2 275  ? 178.355 177.339 167.914 1.00 5.29  ? 275 LEU B CD1 1 
ATOM 5582 C CD2 . LEU B 2 275  ? 180.775 177.836 168.262 1.00 5.61  ? 275 LEU B CD2 1 
ATOM 5583 N N   . SER B 2 276  ? 182.574 173.579 168.837 1.00 8.00  ? 276 SER B N   1 
ATOM 5584 C CA  . SER B 2 276  ? 182.930 172.564 169.807 1.00 1.63  ? 276 SER B CA  1 
ATOM 5585 C C   . SER B 2 276  ? 181.933 172.583 170.966 1.00 8.44  ? 276 SER B C   1 
ATOM 5586 O O   . SER B 2 276  ? 181.255 173.588 171.193 1.00 7.18  ? 276 SER B O   1 
ATOM 5587 C CB  . SER B 2 276  ? 184.348 172.813 170.317 1.00 0.31  ? 276 SER B CB  1 
ATOM 5588 O OG  . SER B 2 276  ? 184.957 171.626 170.793 1.00 1.82  ? 276 SER B OG  1 
ATOM 5589 N N   . PRO B 2 277  ? 181.805 171.472 171.700 1.00 11.01 ? 277 PRO B N   1 
ATOM 5590 C CA  . PRO B 2 277  ? 180.956 171.499 172.906 1.00 6.42  ? 277 PRO B CA  1 
ATOM 5591 C C   . PRO B 2 277  ? 181.370 172.558 173.915 1.00 8.04  ? 277 PRO B C   1 
ATOM 5592 O O   . PRO B 2 277  ? 180.502 173.173 174.547 1.00 7.78  ? 277 PRO B O   1 
ATOM 5593 C CB  . PRO B 2 277  ? 181.112 170.081 173.469 1.00 2.50  ? 277 PRO B CB  1 
ATOM 5594 C CG  . PRO B 2 277  ? 181.422 169.245 172.284 1.00 0.00  ? 277 PRO B CG  1 
ATOM 5595 C CD  . PRO B 2 277  ? 182.244 170.106 171.366 1.00 7.85  ? 277 PRO B CD  1 
ATOM 5596 N N   . PHE B 2 278  ? 182.675 172.793 174.080 1.00 5.21  ? 278 PHE B N   1 
ATOM 5597 C CA  . PHE B 2 278  ? 183.136 173.860 174.965 1.00 0.34  ? 278 PHE B CA  1 
ATOM 5598 C C   . PHE B 2 278  ? 182.613 175.216 174.502 1.00 7.16  ? 278 PHE B C   1 
ATOM 5599 O O   . PHE B 2 278  ? 182.069 175.991 175.298 1.00 4.77  ? 278 PHE B O   1 
ATOM 5600 C CB  . PHE B 2 278  ? 184.665 173.861 175.018 1.00 0.00  ? 278 PHE B CB  1 
ATOM 5601 C CG  . PHE B 2 278  ? 185.243 174.623 176.182 1.00 0.21  ? 278 PHE B CG  1 
ATOM 5602 C CD1 . PHE B 2 278  ? 185.131 176.001 176.259 1.00 5.12  ? 278 PHE B CD1 1 
ATOM 5603 C CD2 . PHE B 2 278  ? 185.921 173.958 177.189 1.00 2.35  ? 278 PHE B CD2 1 
ATOM 5604 C CE1 . PHE B 2 278  ? 185.668 176.696 177.323 1.00 6.24  ? 278 PHE B CE1 1 
ATOM 5605 C CE2 . PHE B 2 278  ? 186.460 174.651 178.254 1.00 6.94  ? 278 PHE B CE2 1 
ATOM 5606 C CZ  . PHE B 2 278  ? 186.334 176.020 178.319 1.00 2.89  ? 278 PHE B CZ  1 
ATOM 5607 N N   . ASP B 2 279  ? 182.797 175.501 173.210 1.00 1.27  ? 279 ASP B N   1 
ATOM 5608 C CA  . ASP B 2 279  ? 182.311 176.787 172.645 1.00 0.00  ? 279 ASP B CA  1 
ATOM 5609 C C   . ASP B 2 279  ? 180.790 176.848 172.800 1.00 0.00  ? 279 ASP B C   1 
ATOM 5610 O O   . ASP B 2 279  ? 180.285 177.894 173.250 1.00 5.62  ? 279 ASP B O   1 
ATOM 5611 C CB  . ASP B 2 279  ? 182.736 176.945 171.184 1.00 0.00  ? 279 ASP B CB  1 
ATOM 5612 C CG  . ASP B 2 279  ? 184.237 177.086 171.012 1.00 0.00  ? 279 ASP B CG  1 
ATOM 5613 O OD1 . ASP B 2 279  ? 184.738 178.219 171.154 1.00 0.00  ? 279 ASP B OD1 1 
ATOM 5614 O OD2 . ASP B 2 279  ? 184.895 176.063 170.742 1.00 3.99  ? 279 ASP B OD2 1 
ATOM 5615 N N   . GLN B 2 280  ? 180.094 175.764 172.445 1.00 3.57  ? 280 GLN B N   1 
ATOM 5616 C CA  . GLN B 2 280  ? 178.639 175.761 172.535 1.00 0.00  ? 280 GLN B CA  1 
ATOM 5617 C C   . GLN B 2 280  ? 178.187 176.128 173.940 1.00 2.57  ? 280 GLN B C   1 
ATOM 5618 O O   . GLN B 2 280  ? 177.311 176.983 174.123 1.00 3.60  ? 280 GLN B O   1 
ATOM 5619 C CB  . GLN B 2 280  ? 178.087 174.393 172.139 1.00 0.00  ? 280 GLN B CB  1 
ATOM 5620 C CG  . GLN B 2 280  ? 176.595 174.253 172.393 1.00 0.47  ? 280 GLN B CG  1 
ATOM 5621 C CD  . GLN B 2 280  ? 176.114 172.823 172.299 1.00 7.53  ? 280 GLN B CD  1 
ATOM 5622 O OE1 . GLN B 2 280  ? 176.911 171.887 172.286 1.00 12.16 ? 280 GLN B OE1 1 
ATOM 5623 N NE2 . GLN B 2 280  ? 174.800 172.645 172.234 1.00 9.88  ? 280 GLN B NE2 1 
ATOM 5624 N N   . MET B 2 281  ? 178.795 175.502 174.950 1.00 9.10  ? 281 MET B N   1 
ATOM 5625 C CA  . MET B 2 281  ? 178.426 175.790 176.330 1.00 0.00  ? 281 MET B CA  1 
ATOM 5626 C C   . MET B 2 281  ? 178.768 177.226 176.708 1.00 4.70  ? 281 MET B C   1 
ATOM 5627 O O   . MET B 2 281  ? 177.987 177.889 177.396 1.00 5.11  ? 281 MET B O   1 
ATOM 5628 C CB  . MET B 2 281  ? 179.108 174.801 177.273 1.00 0.69  ? 281 MET B CB  1 
ATOM 5629 C CG  . MET B 2 281  ? 178.325 173.515 177.474 1.00 1.24  ? 281 MET B CG  1 
ATOM 5630 S SD  . MET B 2 281  ? 179.272 172.220 178.295 1.00 25.43 ? 281 MET B SD  1 
ATOM 5631 C CE  . MET B 2 281  ? 180.931 172.596 177.740 1.00 3.57  ? 281 MET B CE  1 
ATOM 5632 N N   . LYS B 2 282  ? 179.924 177.727 176.262 1.00 5.50  ? 282 LYS B N   1 
ATOM 5633 C CA  . LYS B 2 282  ? 180.306 179.105 176.565 1.00 8.26  ? 282 LYS B CA  1 
ATOM 5634 C C   . LYS B 2 282  ? 179.296 180.100 176.005 1.00 3.91  ? 282 LYS B C   1 
ATOM 5635 O O   . LYS B 2 282  ? 178.802 180.982 176.725 1.00 0.00  ? 282 LYS B O   1 
ATOM 5636 C CB  . LYS B 2 282  ? 181.694 179.393 175.998 1.00 0.00  ? 282 LYS B CB  1 
ATOM 5637 C CG  . LYS B 2 282  ? 182.776 179.571 177.034 1.00 0.62  ? 282 LYS B CG  1 
ATOM 5638 C CD  . LYS B 2 282  ? 184.095 179.889 176.367 1.00 0.00  ? 282 LYS B CD  1 
ATOM 5639 C CE  . LYS B 2 282  ? 183.926 180.998 175.349 1.00 0.00  ? 282 LYS B CE  1 
ATOM 5640 N NZ  . LYS B 2 282  ? 185.090 181.085 174.431 1.00 0.00  ? 282 LYS B NZ  1 
ATOM 5641 N N   . THR B 2 283  ? 178.990 179.982 174.710 1.00 3.35  ? 283 THR B N   1 
ATOM 5642 C CA  . THR B 2 283  ? 178.063 180.918 174.086 1.00 0.31  ? 283 THR B CA  1 
ATOM 5643 C C   . THR B 2 283  ? 176.667 180.791 174.678 1.00 7.30  ? 283 THR B C   1 
ATOM 5644 O O   . THR B 2 283  ? 175.985 181.801 174.880 1.00 11.10 ? 283 THR B O   1 
ATOM 5645 C CB  . THR B 2 283  ? 178.024 180.708 172.574 1.00 3.34  ? 283 THR B CB  1 
ATOM 5646 O OG1 . THR B 2 283  ? 177.543 179.390 172.283 1.00 8.02  ? 283 THR B OG1 1 
ATOM 5647 C CG2 . THR B 2 283  ? 179.411 180.887 171.978 1.00 4.41  ? 283 THR B CG2 1 
ATOM 5648 N N   . ALA B 2 284  ? 176.220 179.565 174.965 1.00 12.15 ? 284 ALA B N   1 
ATOM 5649 C CA  . ALA B 2 284  ? 174.912 179.398 175.587 1.00 9.92  ? 284 ALA B CA  1 
ATOM 5650 C C   . ALA B 2 284  ? 174.875 180.043 176.965 1.00 6.97  ? 284 ALA B C   1 
ATOM 5651 O O   . ALA B 2 284  ? 173.903 180.725 177.312 1.00 7.21  ? 284 ALA B O   1 
ATOM 5652 C CB  . ALA B 2 284  ? 174.555 177.916 175.676 1.00 9.05  ? 284 ALA B CB  1 
ATOM 5653 N N   . SER B 2 285  ? 175.933 179.854 177.758 1.00 1.34  ? 285 SER B N   1 
ATOM 5654 C CA  . SER B 2 285  ? 175.997 180.455 179.084 1.00 9.63  ? 285 SER B CA  1 
ATOM 5655 C C   . SER B 2 285  ? 175.904 181.972 179.003 1.00 14.24 ? 285 SER B C   1 
ATOM 5656 O O   . SER B 2 285  ? 175.087 182.589 179.698 1.00 13.46 ? 285 SER B O   1 
ATOM 5657 C CB  . SER B 2 285  ? 177.288 180.029 179.783 1.00 7.88  ? 285 SER B CB  1 
ATOM 5658 O OG  . SER B 2 285  ? 177.542 180.831 180.922 1.00 11.54 ? 285 SER B OG  1 
ATOM 5659 N N   . ASN B 2 286  ? 176.706 182.574 178.122 1.00 13.68 ? 286 ASN B N   1 
ATOM 5660 C CA  . ASN B 2 286  ? 176.716 184.057 177.992 1.00 5.93  ? 286 ASN B CA  1 
ATOM 5661 C C   . ASN B 2 286  ? 175.356 184.552 177.488 1.00 7.90  ? 286 ASN B C   1 
ATOM 5662 O O   . ASN B 2 286  ? 174.853 185.543 178.051 1.00 9.61  ? 286 ASN B O   1 
ATOM 5663 C CB  . ASN B 2 286  ? 177.852 184.532 177.083 1.00 1.67  ? 286 ASN B CB  1 
ATOM 5664 C CG  . ASN B 2 286  ? 179.202 183.992 177.503 1.00 1.37  ? 286 ASN B CG  1 
ATOM 5665 O OD1 . ASN B 2 286  ? 179.983 183.544 176.667 1.00 5.13  ? 286 ASN B OD1 1 
ATOM 5666 N ND2 . ASN B 2 286  ? 179.487 184.037 178.794 1.00 0.00  ? 286 ASN B ND2 1 
ATOM 5667 N N   . ILE B 2 287  ? 174.784 183.892 176.477 1.00 8.55  ? 287 ILE B N   1 
ATOM 5668 C CA  . ILE B 2 287  ? 173.529 184.348 175.891 1.00 12.47 ? 287 ILE B CA  1 
ATOM 5669 C C   . ILE B 2 287  ? 172.383 184.211 176.884 1.00 10.51 ? 287 ILE B C   1 
ATOM 5670 O O   . ILE B 2 287  ? 171.464 185.039 176.905 1.00 11.53 ? 287 ILE B O   1 
ATOM 5671 C CB  . ILE B 2 287  ? 173.259 183.576 174.584 1.00 16.18 ? 287 ILE B CB  1 
ATOM 5672 C CG1 . ILE B 2 287  ? 174.168 184.089 173.462 1.00 10.30 ? 287 ILE B CG1 1 
ATOM 5673 C CG2 . ILE B 2 287  ? 171.797 183.674 174.170 1.00 9.58  ? 287 ILE B CG2 1 
ATOM 5674 C CD1 . ILE B 2 287  ? 174.459 185.573 173.530 1.00 4.76  ? 287 ILE B CD1 1 
ATOM 5675 N N   . GLY B 2 288  ? 172.435 183.202 177.747 1.00 6.43  ? 288 GLY B N   1 
ATOM 5676 C CA  . GLY B 2 288  ? 171.398 182.895 178.708 1.00 10.52 ? 288 GLY B CA  1 
ATOM 5677 C C   . GLY B 2 288  ? 171.770 183.441 180.065 1.00 11.72 ? 288 GLY B C   1 
ATOM 5678 O O   . GLY B 2 288  ? 171.484 184.606 180.401 1.00 12.19 ? 288 GLY B O   1 
ATOM 5679 N N   . GLY B 2 289  ? 172.400 182.622 180.879 1.00 13.02 ? 289 GLY B N   1 
ATOM 5680 C CA  . GLY B 2 289  ? 172.571 182.914 182.283 1.00 11.76 ? 289 GLY B CA  1 
ATOM 5681 C C   . GLY B 2 289  ? 172.667 181.619 183.072 1.00 13.49 ? 289 GLY B C   1 
ATOM 5682 O O   . GLY B 2 289  ? 173.167 180.613 182.572 1.00 8.64  ? 289 GLY B O   1 
ATOM 5683 N N   . PHE B 2 290  ? 172.184 181.676 184.313 1.00 12.15 ? 290 PHE B N   1 
ATOM 5684 C CA  . PHE B 2 290  ? 172.237 180.498 185.171 1.00 7.31  ? 290 PHE B CA  1 
ATOM 5685 C C   . PHE B 2 290  ? 171.214 179.454 184.746 1.00 14.05 ? 290 PHE B C   1 
ATOM 5686 O O   . PHE B 2 290  ? 171.535 178.264 184.659 1.00 20.02 ? 290 PHE B O   1 
ATOM 5687 C CB  . PHE B 2 290  ? 172.027 180.906 186.626 1.00 7.78  ? 290 PHE B CB  1 
ATOM 5688 C CG  . PHE B 2 290  ? 172.645 179.963 187.614 1.00 11.50 ? 290 PHE B CG  1 
ATOM 5689 C CD1 . PHE B 2 290  ? 173.982 180.075 187.953 1.00 13.34 ? 290 PHE B CD1 1 
ATOM 5690 C CD2 . PHE B 2 290  ? 171.890 178.974 188.212 1.00 10.53 ? 290 PHE B CD2 1 
ATOM 5691 C CE1 . PHE B 2 290  ? 174.553 179.213 188.863 1.00 7.15  ? 290 PHE B CE1 1 
ATOM 5692 C CE2 . PHE B 2 290  ? 172.457 178.111 189.123 1.00 13.60 ? 290 PHE B CE2 1 
ATOM 5693 C CZ  . PHE B 2 290  ? 173.792 178.231 189.447 1.00 10.76 ? 290 PHE B CZ  1 
ATOM 5694 N N   . ASN B 2 291  ? 169.989 179.879 184.453 1.00 17.45 ? 291 ASN B N   1 
ATOM 5695 C CA  . ASN B 2 291  ? 168.895 178.960 184.174 1.00 16.17 ? 291 ASN B CA  1 
ATOM 5696 C C   . ASN B 2 291  ? 168.830 178.521 182.717 1.00 21.89 ? 291 ASN B C   1 
ATOM 5697 O O   . ASN B 2 291  ? 167.931 177.753 182.359 1.00 21.70 ? 291 ASN B O   1 
ATOM 5698 C CB  . ASN B 2 291  ? 167.562 179.596 184.577 1.00 15.00 ? 291 ASN B CB  1 
ATOM 5699 C CG  . ASN B 2 291  ? 167.407 179.717 186.077 1.00 18.88 ? 291 ASN B CG  1 
ATOM 5700 O OD1 . ASN B 2 291  ? 168.130 179.076 186.839 1.00 17.20 ? 291 ASN B OD1 1 
ATOM 5701 N ND2 . ASN B 2 291  ? 166.464 180.544 186.510 1.00 21.71 ? 291 ASN B ND2 1 
ATOM 5702 N N   . ALA B 2 292  ? 169.810 178.963 181.922 1.00 25.20 ? 292 ALA B N   1 
ATOM 5703 C CA  . ALA B 2 292  ? 169.851 178.619 180.482 1.00 21.40 ? 292 ALA B CA  1 
ATOM 5704 C C   . ALA B 2 292  ? 170.021 177.109 180.292 1.00 20.68 ? 292 ALA B C   1 
ATOM 5705 O O   . ALA B 2 292  ? 170.680 176.475 181.140 1.00 20.78 ? 292 ALA B O   1 
ATOM 5706 C CB  . ALA B 2 292  ? 170.967 179.380 179.809 1.00 16.27 ? 292 ALA B CB  1 
ATOM 5707 N N   . ALA B 2 293  ? 169.457 176.566 179.212 1.00 17.64 ? 293 ALA B N   1 
ATOM 5708 C CA  . ALA B 2 293  ? 169.565 175.146 178.911 1.00 24.53 ? 293 ALA B CA  1 
ATOM 5709 C C   . ALA B 2 293  ? 170.559 174.917 177.780 1.00 22.62 ? 293 ALA B C   1 
ATOM 5710 O O   . ALA B 2 293  ? 170.964 175.843 177.072 1.00 20.15 ? 293 ALA B O   1 
ATOM 5711 C CB  . ALA B 2 293  ? 168.196 174.561 178.547 1.00 20.57 ? 293 ALA B CB  1 
ATOM 5712 N N   . ILE B 2 294  ? 170.951 173.656 177.620 1.00 14.57 ? 294 ILE B N   1 
ATOM 5713 C CA  . ILE B 2 294  ? 171.904 173.239 176.600 1.00 14.51 ? 294 ILE B CA  1 
ATOM 5714 C C   . ILE B 2 294  ? 171.239 172.192 175.720 1.00 19.22 ? 294 ILE B C   1 
ATOM 5715 O O   . ILE B 2 294  ? 170.708 171.196 176.225 1.00 20.83 ? 294 ILE B O   1 
ATOM 5716 C CB  . ILE B 2 294  ? 173.197 172.683 177.225 1.00 15.57 ? 294 ILE B CB  1 
ATOM 5717 C CG1 . ILE B 2 294  ? 174.069 173.823 177.751 1.00 14.90 ? 294 ILE B CG1 1 
ATOM 5718 C CG2 . ILE B 2 294  ? 173.965 171.845 176.215 1.00 11.80 ? 294 ILE B CG2 1 
ATOM 5719 C CD1 . ILE B 2 294  ? 174.878 174.508 176.682 1.00 6.11  ? 294 ILE B CD1 1 
ATOM 5720 N N   . LYS B 2 295  ? 171.263 172.422 174.411 1.00 21.50 ? 295 LYS B N   1 
ATOM 5721 C CA  . LYS B 2 295  ? 170.761 171.445 173.460 1.00 15.40 ? 295 LYS B CA  1 
ATOM 5722 C C   . LYS B 2 295  ? 171.791 170.345 173.235 1.00 15.06 ? 295 LYS B C   1 
ATOM 5723 O O   . LYS B 2 295  ? 173.000 170.561 173.355 1.00 16.93 ? 295 LYS B O   1 
ATOM 5724 C CB  . LYS B 2 295  ? 170.415 172.116 172.131 1.00 13.17 ? 295 LYS B CB  1 
ATOM 5725 C CG  . LYS B 2 295  ? 169.773 173.487 172.276 1.00 14.89 ? 295 LYS B CG  1 
ATOM 5726 C CD  . LYS B 2 295  ? 169.863 174.291 170.986 1.00 19.93 ? 295 LYS B CD  1 
ATOM 5727 C CE  . LYS B 2 295  ? 169.357 173.500 169.787 1.00 19.09 ? 295 LYS B CE  1 
ATOM 5728 N NZ  . LYS B 2 295  ? 168.064 172.809 170.057 1.00 17.19 ? 295 LYS B NZ  1 
ATOM 5729 N N   . ASN B 2 296  ? 171.298 169.153 172.905 1.00 17.09 ? 296 ASN B N   1 
ATOM 5730 C CA  . ASN B 2 296  ? 172.150 168.000 172.655 1.00 17.10 ? 296 ASN B CA  1 
ATOM 5731 C C   . ASN B 2 296  ? 172.462 167.813 171.174 1.00 17.75 ? 296 ASN B C   1 
ATOM 5732 O O   . ASN B 2 296  ? 172.927 166.739 170.778 1.00 18.32 ? 296 ASN B O   1 
ATOM 5733 C CB  . ASN B 2 296  ? 171.505 166.734 173.222 1.00 18.82 ? 296 ASN B CB  1 
ATOM 5734 C CG  . ASN B 2 296  ? 170.040 166.616 172.860 1.00 21.36 ? 296 ASN B CG  1 
ATOM 5735 O OD1 . ASN B 2 296  ? 169.306 167.604 172.863 1.00 22.56 ? 296 ASN B OD1 1 
ATOM 5736 N ND2 . ASN B 2 296  ? 169.605 165.402 172.546 1.00 17.43 ? 296 ASN B ND2 1 
ATOM 5737 N N   . SER B 2 297  ? 172.222 168.860 170.377 1.00 17.02 ? 297 SER B N   1 
ATOM 5738 C CA  . SER B 2 297  ? 172.521 168.803 168.922 1.00 21.39 ? 297 SER B CA  1 
ATOM 5739 C C   . SER B 2 297  ? 172.926 170.198 168.431 1.00 24.58 ? 297 SER B C   1 
ATOM 5740 O O   . SER B 2 297  ? 172.036 170.947 167.982 1.00 23.12 ? 297 SER B O   1 
ATOM 5741 C CB  . SER B 2 297  ? 171.345 168.268 168.148 1.00 19.79 ? 297 SER B CB  1 
ATOM 5742 O OG  . SER B 2 297  ? 171.459 168.591 166.770 1.00 24.29 ? 297 SER B OG  1 
ATOM 5743 N N   . PRO B 2 298  ? 174.220 170.581 168.501 1.00 20.07 ? 298 PRO B N   1 
ATOM 5744 C CA  . PRO B 2 298  ? 174.652 171.924 168.105 1.00 18.81 ? 298 PRO B CA  1 
ATOM 5745 C C   . PRO B 2 298  ? 174.316 172.200 166.633 1.00 26.30 ? 298 PRO B C   1 
ATOM 5746 O O   . PRO B 2 298  ? 174.737 171.438 165.782 1.00 16.00 ? 298 PRO B O   1 
ATOM 5747 C CB  . PRO B 2 298  ? 176.177 171.892 168.282 1.00 11.11 ? 298 PRO B CB  1 
ATOM 5748 C CG  . PRO B 2 298  ? 176.422 170.757 169.253 1.00 11.32 ? 298 PRO B CG  1 
ATOM 5749 C CD  . PRO B 2 298  ? 175.329 169.748 168.967 1.00 16.47 ? 298 PRO B CD  1 
ATOM 5750 N N   . PRO B 2 299  ? 173.566 173.280 166.320 1.00 31.66 ? 299 PRO B N   1 
ATOM 5751 C CA  . PRO B 2 299  ? 173.208 173.606 164.937 1.00 24.13 ? 299 PRO B CA  1 
ATOM 5752 C C   . PRO B 2 299  ? 174.319 174.367 164.197 1.00 21.56 ? 299 PRO B C   1 
ATOM 5753 O O   . PRO B 2 299  ? 175.006 175.154 164.824 1.00 18.53 ? 299 PRO B O   1 
ATOM 5754 C CB  . PRO B 2 299  ? 171.982 174.513 165.118 1.00 23.73 ? 299 PRO B CB  1 
ATOM 5755 C CG  . PRO B 2 299  ? 172.237 175.223 166.431 1.00 23.17 ? 299 PRO B CG  1 
ATOM 5756 C CD  . PRO B 2 299  ? 173.001 174.229 167.284 1.00 21.12 ? 299 PRO B CD  1 
ATOM 5757 N N   . ALA B 2 300  ? 174.406 174.153 162.889 1.00 22.87 ? 300 ALA B N   1 
ATOM 5758 C CA  . ALA B 2 300  ? 175.420 174.840 162.065 1.00 20.48 ? 300 ALA B CA  1 
ATOM 5759 C C   . ALA B 2 300  ? 174.928 176.254 161.744 1.00 23.01 ? 300 ALA B C   1 
ATOM 5760 O O   . ALA B 2 300  ? 173.734 176.390 161.406 1.00 23.58 ? 300 ALA B O   1 
ATOM 5761 C CB  . ALA B 2 300  ? 175.591 174.007 160.835 1.00 18.49 ? 300 ALA B CB  1 
ATOM 5762 N N   . MET B 2 301  ? 175.796 177.270 161.842 1.00 24.40 ? 301 MET B N   1 
ATOM 5763 C CA  . MET B 2 301  ? 175.317 178.631 161.639 1.00 17.74 ? 301 MET B CA  1 
ATOM 5764 C C   . MET B 2 301  ? 176.254 179.354 160.684 1.00 18.01 ? 301 MET B C   1 
ATOM 5765 O O   . MET B 2 301  ? 177.450 179.487 160.965 1.00 17.60 ? 301 MET B O   1 
ATOM 5766 C CB  . MET B 2 301  ? 175.233 179.380 162.970 1.00 14.86 ? 301 MET B CB  1 
ATOM 5767 C CG  . MET B 2 301  ? 173.868 179.344 163.629 1.00 19.18 ? 301 MET B CG  1 
ATOM 5768 S SD  . MET B 2 301  ? 174.003 179.353 165.426 1.00 26.59 ? 301 MET B SD  1 
ATOM 5769 C CE  . MET B 2 301  ? 172.315 179.716 165.897 1.00 22.06 ? 301 MET B CE  1 
ATOM 5770 N N   . SER B 2 302  ? 175.709 179.828 159.567 1.00 14.14 ? 302 SER B N   1 
ATOM 5771 C CA  . SER B 2 302  ? 176.495 180.614 158.626 1.00 9.45  ? 302 SER B CA  1 
ATOM 5772 C C   . SER B 2 302  ? 176.752 182.002 159.193 1.00 14.24 ? 302 SER B C   1 
ATOM 5773 O O   . SER B 2 302  ? 175.833 182.663 159.686 1.00 15.86 ? 302 SER B O   1 
ATOM 5774 C CB  . SER B 2 302  ? 175.777 180.715 157.282 1.00 10.51 ? 302 SER B CB  1 
ATOM 5775 O OG  . SER B 2 302  ? 175.891 179.509 156.551 1.00 16.09 ? 302 SER B OG  1 
ATOM 5776 N N   . GLN B 2 303  ? 178.001 182.444 159.116 1.00 11.96 ? 303 GLN B N   1 
ATOM 5777 C CA  . GLN B 2 303  ? 178.430 183.712 159.685 1.00 6.21  ? 303 GLN B CA  1 
ATOM 5778 C C   . GLN B 2 303  ? 178.725 184.708 158.575 1.00 4.16  ? 303 GLN B C   1 
ATOM 5779 O O   . GLN B 2 303  ? 179.444 184.387 157.618 1.00 5.50  ? 303 GLN B O   1 
ATOM 5780 C CB  . GLN B 2 303  ? 179.669 183.528 160.565 1.00 10.02 ? 303 GLN B CB  1 
ATOM 5781 C CG  . GLN B 2 303  ? 180.199 184.822 161.168 1.00 10.74 ? 303 GLN B CG  1 
ATOM 5782 C CD  . GLN B 2 303  ? 181.295 184.587 162.190 1.00 7.95  ? 303 GLN B CD  1 
ATOM 5783 O OE1 . GLN B 2 303  ? 181.398 185.305 163.184 1.00 0.00  ? 303 GLN B OE1 1 
ATOM 5784 N NE2 . GLN B 2 303  ? 182.120 183.576 161.949 1.00 16.75 ? 303 GLN B NE2 1 
ATOM 5785 N N   . TYR B 2 304  ? 178.156 185.905 158.710 1.00 9.36  ? 304 TYR B N   1 
ATOM 5786 C CA  . TYR B 2 304  ? 178.472 187.070 157.900 1.00 7.55  ? 304 TYR B CA  1 
ATOM 5787 C C   . TYR B 2 304  ? 178.963 188.188 158.812 1.00 11.03 ? 304 TYR B C   1 
ATOM 5788 O O   . TYR B 2 304  ? 178.637 188.236 160.000 1.00 10.81 ? 304 TYR B O   1 
ATOM 5789 C CB  . TYR B 2 304  ? 177.254 187.564 157.105 1.00 0.66  ? 304 TYR B CB  1 
ATOM 5790 C CG  . TYR B 2 304  ? 176.569 186.511 156.266 1.00 3.99  ? 304 TYR B CG  1 
ATOM 5791 C CD1 . TYR B 2 304  ? 177.077 186.141 155.030 1.00 0.00  ? 304 TYR B CD1 1 
ATOM 5792 C CD2 . TYR B 2 304  ? 175.401 185.902 156.703 1.00 9.66  ? 304 TYR B CD2 1 
ATOM 5793 C CE1 . TYR B 2 304  ? 176.450 185.187 154.260 1.00 0.00  ? 304 TYR B CE1 1 
ATOM 5794 C CE2 . TYR B 2 304  ? 174.767 184.947 155.939 1.00 2.55  ? 304 TYR B CE2 1 
ATOM 5795 C CZ  . TYR B 2 304  ? 175.296 184.595 154.720 1.00 0.60  ? 304 TYR B CZ  1 
ATOM 5796 O OH  . TYR B 2 304  ? 174.666 183.643 153.956 1.00 12.27 ? 304 TYR B OH  1 
ATOM 5797 N N   . ILE B 2 305  ? 179.757 189.092 158.248 1.00 4.86  ? 305 ILE B N   1 
ATOM 5798 C CA  . ILE B 2 305  ? 180.259 190.257 158.966 1.00 0.56  ? 305 ILE B CA  1 
ATOM 5799 C C   . ILE B 2 305  ? 179.917 191.493 158.153 1.00 4.17  ? 305 ILE B C   1 
ATOM 5800 O O   . ILE B 2 305  ? 180.088 191.500 156.930 1.00 17.43 ? 305 ILE B O   1 
ATOM 5801 C CB  . ILE B 2 305  ? 181.780 190.170 159.205 1.00 0.00  ? 305 ILE B CB  1 
ATOM 5802 C CG1 . ILE B 2 305  ? 182.142 188.847 159.877 1.00 0.00  ? 305 ILE B CG1 1 
ATOM 5803 C CG2 . ILE B 2 305  ? 182.250 191.339 160.046 1.00 5.73  ? 305 ILE B CG2 1 
ATOM 5804 C CD1 . ILE B 2 305  ? 183.615 188.698 160.152 1.00 0.00  ? 305 ILE B CD1 1 
ATOM 5805 N N   . THR B 2 306  ? 179.411 192.530 158.832 1.00 0.53  ? 306 THR B N   1 
ATOM 5806 C CA  . THR B 2 306  ? 178.976 193.759 158.116 1.00 1.92  ? 306 THR B CA  1 
ATOM 5807 C C   . THR B 2 306  ? 179.534 195.013 158.795 1.00 2.97  ? 306 THR B C   1 
ATOM 5808 O O   . THR B 2 306  ? 179.258 195.199 159.997 1.00 8.10  ? 306 THR B O   1 
ATOM 5809 C CB  . THR B 2 306  ? 177.447 193.845 158.040 1.00 2.05  ? 306 THR B CB  1 
ATOM 5810 O OG1 . THR B 2 306  ? 176.956 193.991 159.372 1.00 1.93  ? 306 THR B OG1 1 
ATOM 5811 C CG2 . THR B 2 306  ? 176.813 192.637 157.385 1.00 2.34  ? 306 THR B CG2 1 
ATOM 5812 N N   . VAL B 2 307  ? 180.286 195.833 158.057 1.00 2.07  ? 307 VAL B N   1 
ATOM 5813 C CA  . VAL B 2 307  ? 180.803 197.090 158.578 1.00 1.50  ? 307 VAL B CA  1 
ATOM 5814 C C   . VAL B 2 307  ? 179.902 198.220 158.100 1.00 8.34  ? 307 VAL B C   1 
ATOM 5815 O O   . VAL B 2 307  ? 179.115 198.073 157.161 1.00 19.53 ? 307 VAL B O   1 
ATOM 5816 C CB  . VAL B 2 307  ? 182.268 197.343 158.165 1.00 0.00  ? 307 VAL B CB  1 
ATOM 5817 C CG1 . VAL B 2 307  ? 183.092 196.089 158.351 1.00 0.00  ? 307 VAL B CG1 1 
ATOM 5818 C CG2 . VAL B 2 307  ? 182.343 197.828 156.734 1.00 4.62  ? 307 VAL B CG2 1 
ATOM 5819 N N   . GLY B 2 308  ? 180.029 199.370 158.755 1.00 4.88  ? 308 GLY B N   1 
ATOM 5820 C CA  . GLY B 2 308  ? 179.159 200.488 158.450 1.00 10.08 ? 308 GLY B CA  1 
ATOM 5821 C C   . GLY B 2 308  ? 179.066 201.500 159.571 1.00 11.73 ? 308 GLY B C   1 
ATOM 5822 O O   . GLY B 2 308  ? 180.084 202.024 160.028 1.00 10.63 ? 308 GLY B O   1 
ATOM 5823 N N   . SER B 2 309  ? 177.844 201.803 160.003 1.00 11.64 ? 309 SER B N   1 
ATOM 5824 C CA  . SER B 2 309  ? 177.615 202.745 161.085 1.00 11.03 ? 309 SER B CA  1 
ATOM 5825 C C   . SER B 2 309  ? 176.407 202.318 161.903 1.00 14.51 ? 309 SER B C   1 
ATOM 5826 O O   . SER B 2 309  ? 175.350 201.993 161.346 1.00 7.11  ? 309 SER B O   1 
ATOM 5827 C CB  . SER B 2 309  ? 177.404 204.161 160.550 1.00 12.63 ? 309 SER B CB  1 
ATOM 5828 O OG  . SER B 2 309  ? 177.138 205.056 161.609 1.00 13.15 ? 309 SER B OG  1 
ATOM 5829 N N   . ASN B 2 310  ? 176.611 202.382 163.226 1.00 21.66 ? 310 ASN B N   1 
ATOM 5830 C CA  . ASN B 2 310  ? 175.535 202.041 164.190 1.00 20.90 ? 310 ASN B CA  1 
ATOM 5831 C C   . ASN B 2 310  ? 174.973 200.657 163.847 1.00 22.28 ? 310 ASN B C   1 
ATOM 5832 O O   . ASN B 2 310  ? 173.843 200.579 163.314 1.00 22.63 ? 310 ASN B O   1 
ATOM 5833 C CB  . ASN B 2 310  ? 174.538 203.196 164.282 1.00 20.10 ? 310 ASN B CB  1 
ATOM 5834 C CG  . ASN B 2 310  ? 175.176 204.517 164.652 1.00 22.10 ? 310 ASN B CG  1 
ATOM 5835 O OD1 . ASN B 2 310  ? 176.082 204.988 163.970 1.00 20.91 ? 310 ASN B OD1 1 
ATOM 5836 N ND2 . ASN B 2 310  ? 174.704 205.122 165.730 1.00 22.45 ? 310 ASN B ND2 1 
ATOM 5837 N N   . PRO B 2 311  ? 175.727 199.580 164.166 1.00 12.85 ? 311 PRO B N   1 
ATOM 5838 C CA  . PRO B 2 311  ? 177.007 199.723 164.861 1.00 6.71  ? 311 PRO B CA  1 
ATOM 5839 C C   . PRO B 2 311  ? 178.189 199.767 163.884 1.00 9.91  ? 311 PRO B C   1 
ATOM 5840 O O   . PRO B 2 311  ? 177.968 199.656 162.690 1.00 20.24 ? 311 PRO B O   1 
ATOM 5841 C CB  . PRO B 2 311  ? 177.064 198.420 165.665 1.00 8.58  ? 311 PRO B CB  1 
ATOM 5842 C CG  . PRO B 2 311  ? 176.437 197.404 164.734 1.00 5.23  ? 311 PRO B CG  1 
ATOM 5843 C CD  . PRO B 2 311  ? 175.392 198.170 163.946 1.00 9.42  ? 311 PRO B CD  1 
ATOM 5844 N N   . PHE B 2 312  ? 179.406 199.926 164.409 1.00 0.00  ? 312 PHE B N   1 
ATOM 5845 C CA  . PHE B 2 312  ? 180.610 199.929 163.538 1.00 0.00  ? 312 PHE B CA  1 
ATOM 5846 C C   . PHE B 2 312  ? 180.720 198.577 162.826 1.00 1.27  ? 312 PHE B C   1 
ATOM 5847 O O   . PHE B 2 312  ? 180.814 198.565 161.583 1.00 14.83 ? 312 PHE B O   1 
ATOM 5848 C CB  . PHE B 2 312  ? 181.868 200.244 164.350 1.00 0.00  ? 312 PHE B CB  1 
ATOM 5849 C CG  . PHE B 2 312  ? 183.159 199.985 163.616 1.00 0.00  ? 312 PHE B CG  1 
ATOM 5850 C CD1 . PHE B 2 312  ? 183.419 200.597 162.400 1.00 0.00  ? 312 PHE B CD1 1 
ATOM 5851 C CD2 . PHE B 2 312  ? 184.112 199.127 164.138 1.00 2.86  ? 312 PHE B CD2 1 
ATOM 5852 C CE1 . PHE B 2 312  ? 184.605 200.358 161.725 1.00 0.01  ? 312 PHE B CE1 1 
ATOM 5853 C CE2 . PHE B 2 312  ? 185.297 198.888 163.461 1.00 1.15  ? 312 PHE B CE2 1 
ATOM 5854 C CZ  . PHE B 2 312  ? 185.542 199.505 162.257 1.00 0.00  ? 312 PHE B CZ  1 
ATOM 5855 N N   . THR B 2 313  ? 180.706 197.478 163.588 1.00 5.69  ? 313 THR B N   1 
ATOM 5856 C CA  . THR B 2 313  ? 180.806 196.156 162.988 1.00 3.95  ? 313 THR B CA  1 
ATOM 5857 C C   . THR B 2 313  ? 179.780 195.239 163.636 1.00 0.00  ? 313 THR B C   1 
ATOM 5858 O O   . THR B 2 313  ? 179.612 195.243 164.856 1.00 7.60  ? 313 THR B O   1 
ATOM 5859 C CB  . THR B 2 313  ? 182.212 195.560 163.154 1.00 0.00  ? 313 THR B CB  1 
ATOM 5860 O OG1 . THR B 2 313  ? 183.168 196.381 162.472 1.00 0.00  ? 313 THR B OG1 1 
ATOM 5861 C CG2 . THR B 2 313  ? 182.268 194.160 162.579 1.00 0.00  ? 313 THR B CG2 1 
ATOM 5862 N N   . GLY B 2 314  ? 179.088 194.458 162.809 1.00 0.00  ? 314 GLY B N   1 
ATOM 5863 C CA  . GLY B 2 314  ? 178.081 193.537 163.300 1.00 0.00  ? 314 GLY B CA  1 
ATOM 5864 C C   . GLY B 2 314  ? 178.250 192.135 162.753 1.00 8.11  ? 314 GLY B C   1 
ATOM 5865 O O   . GLY B 2 314  ? 178.467 191.953 161.548 1.00 18.54 ? 314 GLY B O   1 
ATOM 5866 N N   . PHE B 2 315  ? 178.146 191.134 163.626 1.00 4.74  ? 315 PHE B N   1 
ATOM 5867 C CA  . PHE B 2 315  ? 178.372 189.739 163.272 1.00 5.00  ? 315 PHE B CA  1 
ATOM 5868 C C   . PHE B 2 315  ? 177.030 189.019 163.231 1.00 8.70  ? 315 PHE B C   1 
ATOM 5869 O O   . PHE B 2 315  ? 176.376 188.860 164.267 1.00 2.42  ? 315 PHE B O   1 
ATOM 5870 C CB  . PHE B 2 315  ? 179.310 189.069 164.279 1.00 3.02  ? 315 PHE B CB  1 
ATOM 5871 C CG  . PHE B 2 315  ? 180.692 189.669 164.330 1.00 3.47  ? 315 PHE B CG  1 
ATOM 5872 C CD1 . PHE B 2 315  ? 180.899 190.947 164.816 1.00 5.77  ? 315 PHE B CD1 1 
ATOM 5873 C CD2 . PHE B 2 315  ? 181.789 188.935 163.924 1.00 7.58  ? 315 PHE B CD2 1 
ATOM 5874 C CE1 . PHE B 2 315  ? 182.166 191.487 164.866 1.00 4.74  ? 315 PHE B CE1 1 
ATOM 5875 C CE2 . PHE B 2 315  ? 183.059 189.471 163.978 1.00 0.00  ? 315 PHE B CE2 1 
ATOM 5876 C CZ  . PHE B 2 315  ? 183.246 190.748 164.449 1.00 0.00  ? 315 PHE B CZ  1 
ATOM 5877 N N   . PHE B 2 316  ? 176.628 188.576 162.042 1.00 13.24 ? 316 PHE B N   1 
ATOM 5878 C CA  . PHE B 2 316  ? 175.338 187.939 161.823 1.00 11.68 ? 316 PHE B CA  1 
ATOM 5879 C C   . PHE B 2 316  ? 175.512 186.430 161.719 1.00 14.52 ? 316 PHE B C   1 
ATOM 5880 O O   . PHE B 2 316  ? 176.418 185.946 161.035 1.00 13.16 ? 316 PHE B O   1 
ATOM 5881 C CB  . PHE B 2 316  ? 174.670 188.464 160.547 1.00 4.89  ? 316 PHE B CB  1 
ATOM 5882 C CG  . PHE B 2 316  ? 174.224 189.894 160.635 1.00 6.68  ? 316 PHE B CG  1 
ATOM 5883 C CD1 . PHE B 2 316  ? 175.143 190.926 160.579 1.00 2.77  ? 316 PHE B CD1 1 
ATOM 5884 C CD2 . PHE B 2 316  ? 172.885 190.206 160.767 1.00 8.40  ? 316 PHE B CD2 1 
ATOM 5885 C CE1 . PHE B 2 316  ? 174.733 192.239 160.660 1.00 0.00  ? 316 PHE B CE1 1 
ATOM 5886 C CE2 . PHE B 2 316  ? 172.473 191.519 160.848 1.00 9.65  ? 316 PHE B CE2 1 
ATOM 5887 C CZ  . PHE B 2 316  ? 173.399 192.536 160.793 1.00 2.44  ? 316 PHE B CZ  1 
ATOM 5888 N N   . TYR B 2 317  ? 174.638 185.693 162.399 1.00 13.95 ? 317 TYR B N   1 
ATOM 5889 C CA  . TYR B 2 317  ? 174.615 184.238 162.343 1.00 12.49 ? 317 TYR B CA  1 
ATOM 5890 C C   . TYR B 2 317  ? 173.237 183.788 161.884 1.00 14.33 ? 317 TYR B C   1 
ATOM 5891 O O   . TYR B 2 317  ? 172.223 184.212 162.448 1.00 12.16 ? 317 TYR B O   1 
ATOM 5892 C CB  . TYR B 2 317  ? 174.953 183.631 163.707 1.00 10.64 ? 317 TYR B CB  1 
ATOM 5893 C CG  . TYR B 2 317  ? 176.323 184.020 164.212 1.00 11.36 ? 317 TYR B CG  1 
ATOM 5894 C CD1 . TYR B 2 317  ? 177.468 183.472 163.657 1.00 9.83  ? 317 TYR B CD1 1 
ATOM 5895 C CD2 . TYR B 2 317  ? 176.471 184.949 165.231 1.00 14.13 ? 317 TYR B CD2 1 
ATOM 5896 C CE1 . TYR B 2 317  ? 178.720 183.828 164.111 1.00 7.62  ? 317 TYR B CE1 1 
ATOM 5897 C CE2 . TYR B 2 317  ? 177.721 185.314 165.689 1.00 15.05 ? 317 TYR B CE2 1 
ATOM 5898 C CZ  . TYR B 2 317  ? 178.842 184.750 165.123 1.00 14.91 ? 317 TYR B CZ  1 
ATOM 5899 O OH  . TYR B 2 317  ? 180.090 185.107 165.575 1.00 15.88 ? 317 TYR B OH  1 
ATOM 5900 N N   . ALA B 2 318  ? 173.201 182.936 160.864 1.00 19.01 ? 318 ALA B N   1 
ATOM 5901 C CA  . ALA B 2 318  ? 171.955 182.459 160.282 1.00 19.66 ? 318 ALA B CA  1 
ATOM 5902 C C   . ALA B 2 318  ? 171.906 180.939 160.327 1.00 20.91 ? 318 ALA B C   1 
ATOM 5903 O O   . ALA B 2 318  ? 172.901 180.268 160.040 1.00 16.67 ? 318 ALA B O   1 
ATOM 5904 C CB  . ALA B 2 318  ? 171.798 182.942 158.839 1.00 19.85 ? 318 ALA B CB  1 
ATOM 5905 N N   . LEU B 2 319  ? 170.739 180.401 160.672 1.00 27.67 ? 319 LEU B N   1 
ATOM 5906 C CA  . LEU B 2 319  ? 170.581 178.957 160.799 1.00 30.57 ? 319 LEU B CA  1 
ATOM 5907 C C   . LEU B 2 319  ? 170.584 178.306 159.421 1.00 31.57 ? 319 LEU B C   1 
ATOM 5908 O O   . LEU B 2 319  ? 169.732 178.609 158.580 1.00 27.70 ? 319 LEU B O   1 
ATOM 5909 C CB  . LEU B 2 319  ? 169.288 178.637 161.543 1.00 27.07 ? 319 LEU B CB  1 
ATOM 5910 C CG  . LEU B 2 319  ? 169.378 178.667 163.069 1.00 24.34 ? 319 LEU B CG  1 
ATOM 5911 C CD1 . LEU B 2 319  ? 168.010 178.912 163.681 1.00 25.67 ? 319 LEU B CD1 1 
ATOM 5912 C CD2 . LEU B 2 319  ? 169.976 177.372 163.590 1.00 27.39 ? 319 LEU B CD2 1 
ATOM 5913 N N   . GLU B 2 320  ? 171.538 177.405 159.192 1.00 27.09 ? 320 GLU B N   1 
ATOM 5914 C CA  . GLU B 2 320  ? 171.654 176.729 157.907 1.00 25.04 ? 320 GLU B CA  1 
ATOM 5915 C C   . GLU B 2 320  ? 170.767 175.492 157.875 1.00 26.82 ? 320 GLU B C   1 
ATOM 5916 O O   . GLU B 2 320  ? 170.760 174.695 158.818 1.00 24.68 ? 320 GLU B O   1 
ATOM 5917 C CB  . GLU B 2 320  ? 173.107 176.345 157.631 1.00 20.38 ? 320 GLU B CB  1 
ATOM 5918 C CG  . GLU B 2 320  ? 173.322 175.698 156.273 1.00 23.06 ? 320 GLU B CG  1 
ATOM 5919 C CD  . GLU B 2 320  ? 173.032 176.641 155.120 1.00 27.46 ? 320 GLU B CD  1 
ATOM 5920 O OE1 . GLU B 2 320  ? 172.904 177.859 155.364 1.00 28.71 ? 320 GLU B OE1 1 
ATOM 5921 O OE2 . GLU B 2 320  ? 172.926 176.165 153.970 1.00 22.64 ? 320 GLU B OE2 1 
ATOM 5922 N N   . GLY B 2 321  ? 170.022 175.334 156.781 1.00 29.17 ? 321 GLY B N   1 
ATOM 5923 C CA  . GLY B 2 321  ? 169.086 174.243 156.631 1.00 26.06 ? 321 GLY B CA  1 
ATOM 5924 C C   . GLY B 2 321  ? 167.715 174.495 157.218 1.00 30.39 ? 321 GLY B C   1 
ATOM 5925 O O   . GLY B 2 321  ? 166.826 173.649 157.059 1.00 29.96 ? 321 GLY B O   1 
ATOM 5926 N N   . SER B 2 322  ? 167.514 175.630 157.891 1.00 33.46 ? 322 SER B N   1 
ATOM 5927 C CA  . SER B 2 322  ? 166.219 175.924 158.494 1.00 31.56 ? 322 SER B CA  1 
ATOM 5928 C C   . SER B 2 322  ? 165.183 176.318 157.447 1.00 33.21 ? 322 SER B C   1 
ATOM 5929 O O   . SER B 2 322  ? 164.021 175.907 157.537 1.00 31.61 ? 322 SER B O   1 
ATOM 5930 C CB  . SER B 2 322  ? 166.369 177.030 159.539 1.00 25.28 ? 322 SER B CB  1 
ATOM 5931 O OG  . SER B 2 322  ? 167.023 178.160 158.989 1.00 23.31 ? 322 SER B OG  1 
ATOM 5932 N N   . THR B 2 323  ? 165.580 177.111 156.455 1.00 29.82 ? 323 THR B N   1 
ATOM 5933 C CA  . THR B 2 323  ? 164.683 177.573 155.404 1.00 28.32 ? 323 THR B CA  1 
ATOM 5934 C C   . THR B 2 323  ? 165.193 177.091 154.055 1.00 26.52 ? 323 THR B C   1 
ATOM 5935 O O   . THR B 2 323  ? 166.377 177.255 153.739 1.00 29.50 ? 323 THR B O   1 
ATOM 5936 C CB  . THR B 2 323  ? 164.564 179.099 155.407 1.00 30.20 ? 323 THR B CB  1 
ATOM 5937 O OG1 . THR B 2 323  ? 164.193 179.550 156.716 1.00 27.49 ? 323 THR B OG1 1 
ATOM 5938 C CG2 . THR B 2 323  ? 163.511 179.551 154.407 1.00 27.63 ? 323 THR B CG2 1 
ATOM 5939 N N   . GLN B 2 324  ? 164.299 176.503 153.265 1.00 28.93 ? 324 GLN B N   1 
ATOM 5940 C CA  . GLN B 2 324  ? 164.678 176.001 151.953 1.00 33.35 ? 324 GLN B CA  1 
ATOM 5941 C C   . GLN B 2 324  ? 165.010 177.161 151.016 1.00 32.78 ? 324 GLN B C   1 
ATOM 5942 O O   . GLN B 2 324  ? 164.379 178.220 151.088 1.00 29.32 ? 324 GLN B O   1 
ATOM 5943 C CB  . GLN B 2 324  ? 163.552 175.157 151.359 1.00 30.89 ? 324 GLN B CB  1 
ATOM 5944 C CG  . GLN B 2 324  ? 163.277 173.870 152.115 1.00 32.38 ? 324 GLN B CG  1 
ATOM 5945 C CD  . GLN B 2 324  ? 164.401 172.863 151.979 1.00 32.35 ? 324 GLN B CD  1 
ATOM 5946 O OE1 . GLN B 2 324  ? 165.179 172.907 151.025 1.00 34.15 ? 324 GLN B OE1 1 
ATOM 5947 N NE2 . GLN B 2 324  ? 164.491 171.945 152.934 1.00 30.45 ? 324 GLN B NE2 1 
ATOM 5948 N N   . PRO B 2 325  ? 165.990 176.993 150.129 1.00 29.14 ? 325 PRO B N   1 
ATOM 5949 C CA  . PRO B 2 325  ? 166.325 178.069 149.186 1.00 24.81 ? 325 PRO B CA  1 
ATOM 5950 C C   . PRO B 2 325  ? 165.232 178.238 148.141 1.00 23.88 ? 325 PRO B C   1 
ATOM 5951 O O   . PRO B 2 325  ? 164.718 177.260 147.595 1.00 26.33 ? 325 PRO B O   1 
ATOM 5952 C CB  . PRO B 2 325  ? 167.641 177.597 148.552 1.00 29.33 ? 325 PRO B CB  1 
ATOM 5953 C CG  . PRO B 2 325  ? 168.106 176.429 149.390 1.00 26.83 ? 325 PRO B CG  1 
ATOM 5954 C CD  . PRO B 2 325  ? 166.875 175.828 149.978 1.00 25.54 ? 325 PRO B CD  1 
ATOM 5955 N N   . LEU B 2 326  ? 164.883 179.491 147.863 1.00 22.86 ? 326 LEU B N   1 
ATOM 5956 C CA  . LEU B 2 326  ? 163.885 179.785 146.849 1.00 24.79 ? 326 LEU B CA  1 
ATOM 5957 C C   . LEU B 2 326  ? 164.470 179.602 145.451 1.00 21.46 ? 326 LEU B C   1 
ATOM 5958 O O   . LEU B 2 326  ? 165.684 179.671 145.240 1.00 22.09 ? 326 LEU B O   1 
ATOM 5959 C CB  . LEU B 2 326  ? 163.354 181.210 147.008 1.00 20.20 ? 326 LEU B CB  1 
ATOM 5960 C CG  . LEU B 2 326  ? 162.924 181.640 148.410 1.00 22.48 ? 326 LEU B CG  1 
ATOM 5961 C CD1 . LEU B 2 326  ? 163.065 183.144 148.568 1.00 22.48 ? 326 LEU B CD1 1 
ATOM 5962 C CD2 . LEU B 2 326  ? 161.496 181.199 148.686 1.00 24.95 ? 326 LEU B CD2 1 
ATOM 5963 N N   . LEU B 2 327  ? 163.584 179.367 144.490 1.00 20.41 ? 327 LEU B N   1 
ATOM 5964 C CA  . LEU B 2 327  ? 163.992 179.188 143.103 1.00 23.82 ? 327 LEU B CA  1 
ATOM 5965 C C   . LEU B 2 327  ? 163.395 180.272 142.211 1.00 23.44 ? 327 LEU B C   1 
ATOM 5966 O O   . LEU B 2 327  ? 162.983 181.329 142.691 1.00 25.33 ? 327 LEU B O   1 
ATOM 5967 C CB  . LEU B 2 327  ? 163.581 177.804 142.599 1.00 25.03 ? 327 LEU B CB  1 
ATOM 5968 C CG  . LEU B 2 327  ? 164.311 176.616 143.230 1.00 23.78 ? 327 LEU B CG  1 
ATOM 5969 C CD1 . LEU B 2 327  ? 163.698 175.304 142.770 1.00 22.64 ? 327 LEU B CD1 1 
ATOM 5970 C CD2 . LEU B 2 327  ? 165.794 176.664 142.898 1.00 24.33 ? 327 LEU B CD2 1 
ATOM 5971 N N   . GLN B 2 364  ? 162.045 189.558 137.455 1.00 29.35 ? 364 GLN B N   1 
ATOM 5972 C CA  . GLN B 2 364  ? 161.076 190.566 137.041 1.00 30.27 ? 364 GLN B CA  1 
ATOM 5973 C C   . GLN B 2 364  ? 160.369 191.179 138.243 1.00 27.76 ? 364 GLN B C   1 
ATOM 5974 O O   . GLN B 2 364  ? 159.739 192.231 138.132 1.00 26.11 ? 364 GLN B O   1 
ATOM 5975 C CB  . GLN B 2 364  ? 160.045 189.960 136.086 1.00 30.15 ? 364 GLN B CB  1 
ATOM 5976 C CG  . GLN B 2 364  ? 159.082 190.977 135.493 1.00 31.33 ? 364 GLN B CG  1 
ATOM 5977 C CD  . GLN B 2 364  ? 158.185 190.380 134.426 1.00 32.15 ? 364 GLN B CD  1 
ATOM 5978 O OE1 . GLN B 2 364  ? 158.335 189.217 134.053 1.00 30.86 ? 364 GLN B OE1 1 
ATOM 5979 N NE2 . GLN B 2 364  ? 157.245 191.176 133.930 1.00 30.41 ? 364 GLN B NE2 1 
ATOM 5980 N N   . LYS B 2 365  ? 160.476 190.518 139.393 1.00 29.22 ? 365 LYS B N   1 
ATOM 5981 C CA  . LYS B 2 365  ? 159.801 190.953 140.600 1.00 31.76 ? 365 LYS B CA  1 
ATOM 5982 C C   . LYS B 2 365  ? 160.808 191.180 141.719 1.00 30.45 ? 365 LYS B C   1 
ATOM 5983 O O   . LYS B 2 365  ? 161.582 190.268 142.044 1.00 28.55 ? 365 LYS B O   1 
ATOM 5984 C CB  . LYS B 2 365  ? 158.756 189.920 141.047 1.00 32.78 ? 365 LYS B CB  1 
ATOM 5985 C CG  . LYS B 2 365  ? 157.617 189.731 140.066 1.00 29.80 ? 365 LYS B CG  1 
ATOM 5986 C CD  . LYS B 2 365  ? 156.753 190.976 139.989 1.00 28.87 ? 365 LYS B CD  1 
ATOM 5987 C CE  . LYS B 2 365  ? 155.619 190.791 138.997 1.00 31.00 ? 365 LYS B CE  1 
ATOM 5988 N NZ  . LYS B 2 365  ? 154.692 189.707 139.423 1.00 32.25 ? 365 LYS B NZ  1 
ATOM 5989 N N   . PRO B 2 366  ? 160.833 192.364 142.328 1.00 29.91 ? 366 PRO B N   1 
ATOM 5990 C CA  . PRO B 2 366  ? 161.702 192.576 143.491 1.00 30.44 ? 366 PRO B CA  1 
ATOM 5991 C C   . PRO B 2 366  ? 161.040 192.117 144.779 1.00 30.31 ? 366 PRO B C   1 
ATOM 5992 O O   . PRO B 2 366  ? 161.685 192.040 145.829 1.00 29.28 ? 366 PRO B O   1 
ATOM 5993 C CB  . PRO B 2 366  ? 161.922 194.091 143.484 1.00 28.61 ? 366 PRO B CB  1 
ATOM 5994 C CG  . PRO B 2 366  ? 160.651 194.635 142.902 1.00 26.89 ? 366 PRO B CG  1 
ATOM 5995 C CD  . PRO B 2 366  ? 160.107 193.590 141.949 1.00 26.52 ? 366 PRO B CD  1 
ATOM 5996 N N   . LYS B 2 367  ? 159.749 191.804 144.702 1.00 36.82 ? 367 LYS B N   1 
ATOM 5997 C CA  . LYS B 2 367  ? 158.948 191.478 145.872 1.00 37.21 ? 367 LYS B CA  1 
ATOM 5998 C C   . LYS B 2 367  ? 158.962 189.993 146.211 1.00 36.16 ? 367 LYS B C   1 
ATOM 5999 O O   . LYS B 2 367  ? 158.001 189.500 146.811 1.00 39.03 ? 367 LYS B O   1 
ATOM 6000 C CB  . LYS B 2 367  ? 157.507 191.954 145.671 1.00 33.87 ? 367 LYS B CB  1 
ATOM 6001 C CG  . LYS B 2 367  ? 157.352 193.468 145.676 1.00 33.20 ? 367 LYS B CG  1 
ATOM 6002 C CD  . LYS B 2 367  ? 155.902 193.881 145.484 1.00 34.23 ? 367 LYS B CD  1 
ATOM 6003 C CE  . LYS B 2 367  ? 155.750 195.394 145.520 1.00 35.81 ? 367 LYS B CE  1 
ATOM 6004 N NZ  . LYS B 2 367  ? 154.338 195.817 145.308 1.00 34.62 ? 367 LYS B NZ  1 
ATOM 6005 N N   . VAL B 2 368  ? 160.017 189.268 145.833 1.00 32.26 ? 368 VAL B N   1 
ATOM 6006 C CA  . VAL B 2 368  ? 160.160 187.886 146.273 1.00 33.16 ? 368 VAL B CA  1 
ATOM 6007 C C   . VAL B 2 368  ? 160.272 187.863 147.788 1.00 30.53 ? 368 VAL B C   1 
ATOM 6008 O O   . VAL B 2 368  ? 160.990 188.673 148.383 1.00 25.25 ? 368 VAL B O   1 
ATOM 6009 C CB  . VAL B 2 368  ? 161.380 187.231 145.600 1.00 31.11 ? 368 VAL B CB  1 
ATOM 6010 C CG1 . VAL B 2 368  ? 161.429 185.744 145.921 1.00 25.68 ? 368 VAL B CG1 1 
ATOM 6011 C CG2 . VAL B 2 368  ? 161.344 187.457 144.094 1.00 29.22 ? 368 VAL B CG2 1 
ATOM 6012 N N   . GLU B 2 369  ? 159.552 186.939 148.416 1.00 31.10 ? 369 GLU B N   1 
ATOM 6013 C CA  . GLU B 2 369  ? 159.496 186.887 149.868 1.00 30.65 ? 369 GLU B CA  1 
ATOM 6014 C C   . GLU B 2 369  ? 160.889 186.619 150.439 1.00 28.76 ? 369 GLU B C   1 
ATOM 6015 O O   . GLU B 2 369  ? 161.608 185.751 149.923 1.00 29.06 ? 369 GLU B O   1 
ATOM 6016 C CB  . GLU B 2 369  ? 158.513 185.805 150.329 1.00 29.39 ? 369 GLU B CB  1 
ATOM 6017 C CG  . GLU B 2 369  ? 158.858 184.373 149.913 1.00 26.82 ? 369 GLU B CG  1 
ATOM 6018 C CD  . GLU B 2 369  ? 158.571 184.078 148.448 1.00 29.15 ? 369 GLU B CD  1 
ATOM 6019 O OE1 . GLU B 2 369  ? 158.682 182.899 148.051 1.00 28.58 ? 369 GLU B OE1 1 
ATOM 6020 O OE2 . GLU B 2 369  ? 158.237 185.016 147.694 1.00 29.32 ? 369 GLU B OE2 1 
ATOM 6021 N N   . PRO B 2 370  ? 161.316 187.357 151.462 1.00 24.11 ? 370 PRO B N   1 
ATOM 6022 C CA  . PRO B 2 370  ? 162.622 187.083 152.070 1.00 24.29 ? 370 PRO B CA  1 
ATOM 6023 C C   . PRO B 2 370  ? 162.685 185.666 152.617 1.00 25.49 ? 370 PRO B C   1 
ATOM 6024 O O   . PRO B 2 370  ? 161.708 185.144 153.157 1.00 29.65 ? 370 PRO B O   1 
ATOM 6025 C CB  . PRO B 2 370  ? 162.717 188.126 153.188 1.00 21.17 ? 370 PRO B CB  1 
ATOM 6026 C CG  . PRO B 2 370  ? 161.821 189.230 152.743 1.00 21.65 ? 370 PRO B CG  1 
ATOM 6027 C CD  . PRO B 2 370  ? 160.685 188.561 152.026 1.00 22.10 ? 370 PRO B CD  1 
ATOM 6028 N N   . ALA B 2 371  ? 163.851 185.039 152.457 1.00 24.45 ? 371 ALA B N   1 
ATOM 6029 C CA  . ALA B 2 371  ? 164.019 183.666 152.922 1.00 22.66 ? 371 ALA B CA  1 
ATOM 6030 C C   . ALA B 2 371  ? 163.901 183.582 154.438 1.00 22.39 ? 371 ALA B C   1 
ATOM 6031 O O   . ALA B 2 371  ? 163.180 182.730 154.971 1.00 23.41 ? 371 ALA B O   1 
ATOM 6032 C CB  . ALA B 2 371  ? 165.366 183.117 152.454 1.00 22.15 ? 371 ALA B CB  1 
ATOM 6033 N N   . THR B 2 372  ? 164.596 184.468 155.153 1.00 13.97 ? 372 THR B N   1 
ATOM 6034 C CA  . THR B 2 372  ? 164.630 184.438 156.605 1.00 17.37 ? 372 THR B CA  1 
ATOM 6035 C C   . THR B 2 372  ? 165.074 185.800 157.116 1.00 22.37 ? 372 THR B C   1 
ATOM 6036 O O   . THR B 2 372  ? 166.050 186.358 156.594 1.00 19.15 ? 372 THR B O   1 
ATOM 6037 C CB  . THR B 2 372  ? 165.584 183.355 157.129 1.00 19.31 ? 372 THR B CB  1 
ATOM 6038 O OG1 . THR B 2 372  ? 165.195 182.074 156.616 1.00 18.38 ? 372 THR B OG1 1 
ATOM 6039 C CG2 . THR B 2 372  ? 165.568 183.307 158.649 1.00 17.64 ? 372 THR B CG2 1 
ATOM 6040 N N   . PRO B 2 373  ? 164.382 186.367 158.102 1.00 26.38 ? 373 PRO B N   1 
ATOM 6041 C CA  . PRO B 2 373  ? 164.898 187.572 158.757 1.00 18.84 ? 373 PRO B CA  1 
ATOM 6042 C C   . PRO B 2 373  ? 166.188 187.276 159.505 1.00 14.06 ? 373 PRO B C   1 
ATOM 6043 O O   . PRO B 2 373  ? 166.392 186.179 160.031 1.00 9.23  ? 373 PRO B O   1 
ATOM 6044 C CB  . PRO B 2 373  ? 163.773 187.970 159.720 1.00 12.78 ? 373 PRO B CB  1 
ATOM 6045 C CG  . PRO B 2 373  ? 162.557 187.256 159.218 1.00 17.81 ? 373 PRO B CG  1 
ATOM 6046 C CD  . PRO B 2 373  ? 163.054 185.985 158.608 1.00 21.42 ? 373 PRO B CD  1 
ATOM 6047 N N   . LEU B 2 374  ? 167.086 188.270 159.521 1.00 11.27 ? 374 LEU B N   1 
ATOM 6048 C CA  . LEU B 2 374  ? 168.417 188.080 160.159 1.00 6.98  ? 374 LEU B CA  1 
ATOM 6049 C C   . LEU B 2 374  ? 168.713 189.238 161.115 1.00 7.93  ? 374 LEU B C   1 
ATOM 6050 O O   . LEU B 2 374  ? 168.858 190.378 160.632 1.00 13.16 ? 374 LEU B O   1 
ATOM 6051 C CB  . LEU B 2 374  ? 169.477 187.998 159.056 1.00 11.34 ? 374 LEU B CB  1 
ATOM 6052 C CG  . LEU B 2 374  ? 170.831 187.435 159.484 1.00 11.86 ? 374 LEU B CG  1 
ATOM 6053 C CD1 . LEU B 2 374  ? 170.654 186.305 160.485 1.00 10.63 ? 374 LEU B CD1 1 
ATOM 6054 C CD2 . LEU B 2 374  ? 171.626 186.959 158.278 1.00 11.36 ? 374 LEU B CD2 1 
ATOM 6055 N N   . ALA B 2 375  ? 168.802 188.954 162.416 1.00 10.17 ? 375 ALA B N   1 
ATOM 6056 C CA  . ALA B 2 375  ? 169.116 189.956 163.421 1.00 11.05 ? 375 ALA B CA  1 
ATOM 6057 C C   . ALA B 2 375  ? 170.559 189.803 163.885 1.00 6.38  ? 375 ALA B C   1 
ATOM 6058 O O   . ALA B 2 375  ? 171.090 188.693 163.972 1.00 8.05  ? 375 ALA B O   1 
ATOM 6059 C CB  . ALA B 2 375  ? 168.171 189.847 164.617 1.00 10.59 ? 375 ALA B CB  1 
ATOM 6060 N N   . VAL B 2 376  ? 171.190 190.933 164.185 1.00 5.92  ? 376 VAL B N   1 
ATOM 6061 C CA  . VAL B 2 376  ? 172.599 190.940 164.564 1.00 8.80  ? 376 VAL B CA  1 
ATOM 6062 C C   . VAL B 2 376  ? 172.734 190.431 165.997 1.00 7.50  ? 376 VAL B C   1 
ATOM 6063 O O   . VAL B 2 376  ? 172.088 190.942 166.918 1.00 4.49  ? 376 VAL B O   1 
ATOM 6064 C CB  . VAL B 2 376  ? 173.213 192.340 164.395 1.00 9.57  ? 376 VAL B CB  1 
ATOM 6065 C CG1 . VAL B 2 376  ? 172.496 193.377 165.253 1.00 10.10 ? 376 VAL B CG1 1 
ATOM 6066 C CG2 . VAL B 2 376  ? 174.696 192.311 164.710 1.00 6.10  ? 376 VAL B CG2 1 
ATOM 6067 N N   . ARG B 2 377  ? 173.549 189.390 166.179 1.00 7.43  ? 377 ARG B N   1 
ATOM 6068 C CA  . ARG B 2 377  ? 173.754 188.839 167.515 1.00 6.40  ? 377 ARG B CA  1 
ATOM 6069 C C   . ARG B 2 377  ? 174.584 189.780 168.377 1.00 6.85  ? 377 ARG B C   1 
ATOM 6070 O O   . ARG B 2 377  ? 174.215 190.080 169.518 1.00 6.09  ? 377 ARG B O   1 
ATOM 6071 C CB  . ARG B 2 377  ? 174.419 187.466 167.418 1.00 7.52  ? 377 ARG B CB  1 
ATOM 6072 C CG  . ARG B 2 377  ? 174.051 186.516 168.544 1.00 3.16  ? 377 ARG B CG  1 
ATOM 6073 C CD  . ARG B 2 377  ? 174.530 185.106 168.246 1.00 7.41  ? 377 ARG B CD  1 
ATOM 6074 N NE  . ARG B 2 377  ? 175.817 184.823 168.869 1.00 8.38  ? 377 ARG B NE  1 
ATOM 6075 C CZ  . ARG B 2 377  ? 176.478 183.682 168.737 1.00 9.20  ? 377 ARG B CZ  1 
ATOM 6076 N NH1 . ARG B 2 377  ? 175.996 182.683 168.017 1.00 7.26  ? 377 ARG B NH1 1 
ATOM 6077 N NH2 . ARG B 2 377  ? 177.655 183.540 169.339 1.00 13.32 ? 377 ARG B NH2 1 
ATOM 6078 N N   . PHE B 2 378  ? 175.703 190.264 167.847 1.00 10.71 ? 378 PHE B N   1 
ATOM 6079 C CA  . PHE B 2 378  ? 176.563 191.171 168.593 1.00 2.12  ? 378 PHE B CA  1 
ATOM 6080 C C   . PHE B 2 378  ? 177.444 191.933 167.616 1.00 7.02  ? 378 PHE B C   1 
ATOM 6081 O O   . PHE B 2 378  ? 177.409 191.708 166.403 1.00 13.60 ? 378 PHE B O   1 
ATOM 6082 C CB  . PHE B 2 378  ? 177.396 190.421 169.642 1.00 3.25  ? 378 PHE B CB  1 
ATOM 6083 C CG  . PHE B 2 378  ? 178.651 189.788 169.104 1.00 7.25  ? 378 PHE B CG  1 
ATOM 6084 C CD1 . PHE B 2 378  ? 178.622 188.512 168.567 1.00 11.25 ? 378 PHE B CD1 1 
ATOM 6085 C CD2 . PHE B 2 378  ? 179.867 190.450 169.173 1.00 5.06  ? 378 PHE B CD2 1 
ATOM 6086 C CE1 . PHE B 2 378  ? 179.774 187.920 168.088 1.00 6.15  ? 378 PHE B CE1 1 
ATOM 6087 C CE2 . PHE B 2 378  ? 181.020 189.865 168.693 1.00 3.83  ? 378 PHE B CE2 1 
ATOM 6088 C CZ  . PHE B 2 378  ? 180.974 188.598 168.152 1.00 8.19  ? 378 PHE B CZ  1 
ATOM 6089 N N   . GLY B 2 379  ? 178.220 192.859 168.164 1.00 5.36  ? 379 GLY B N   1 
ATOM 6090 C CA  . GLY B 2 379  ? 179.105 193.669 167.352 1.00 9.60  ? 379 GLY B CA  1 
ATOM 6091 C C   . GLY B 2 379  ? 179.929 194.585 168.227 1.00 0.93  ? 379 GLY B C   1 
ATOM 6092 O O   . GLY B 2 379  ? 180.028 194.405 169.444 1.00 9.34  ? 379 GLY B O   1 
ATOM 6093 N N   . LEU B 2 380  ? 180.527 195.578 167.576 1.00 5.09  ? 380 LEU B N   1 
ATOM 6094 C CA  . LEU B 2 380  ? 181.346 196.570 168.256 1.00 12.40 ? 380 LEU B CA  1 
ATOM 6095 C C   . LEU B 2 380  ? 180.659 197.924 168.164 1.00 11.57 ? 380 LEU B C   1 
ATOM 6096 O O   . LEU B 2 380  ? 180.774 198.602 167.132 1.00 13.88 ? 380 LEU B O   1 
ATOM 6097 C CB  . LEU B 2 380  ? 182.746 196.633 167.639 1.00 4.88  ? 380 LEU B CB  1 
ATOM 6098 C CG  . LEU B 2 380  ? 183.814 195.686 168.191 1.00 5.50  ? 380 LEU B CG  1 
ATOM 6099 C CD1 . LEU B 2 380  ? 183.400 194.227 168.064 1.00 0.00  ? 380 LEU B CD1 1 
ATOM 6100 C CD2 . LEU B 2 380  ? 185.142 195.928 167.494 1.00 4.76  ? 380 LEU B CD2 1 
ATOM 6101 N N   . PRO B 2 381  ? 179.862 198.347 169.180 1.00 14.82 ? 381 PRO B N   1 
ATOM 6102 C CA  . PRO B 2 381  ? 179.077 199.590 169.076 1.00 8.03  ? 381 PRO B CA  1 
ATOM 6103 C C   . PRO B 2 381  ? 179.922 200.871 169.034 1.00 4.83  ? 381 PRO B C   1 
ATOM 6104 O O   . PRO B 2 381  ? 180.398 201.291 170.074 1.00 11.41 ? 381 PRO B O   1 
ATOM 6105 C CB  . PRO B 2 381  ? 178.205 199.593 170.343 1.00 14.09 ? 381 PRO B CB  1 
ATOM 6106 C CG  . PRO B 2 381  ? 178.978 198.754 171.331 1.00 20.61 ? 381 PRO B CG  1 
ATOM 6107 C CD  . PRO B 2 381  ? 179.647 197.694 170.484 1.00 19.56 ? 381 PRO B CD  1 
ATOM 6108 N N   . ASP B 2 382  ? 180.072 201.461 167.851 1.00 5.19  ? 382 ASP B N   1 
ATOM 6109 C CA  . ASP B 2 382  ? 180.807 202.748 167.751 1.00 9.98  ? 382 ASP B CA  1 
ATOM 6110 C C   . ASP B 2 382  ? 180.015 203.653 166.801 1.00 21.63 ? 382 ASP B C   1 
ATOM 6111 O O   . ASP B 2 382  ? 180.212 203.536 165.577 1.00 16.96 ? 382 ASP B O   1 
ATOM 6112 C CB  . ASP B 2 382  ? 182.267 202.503 167.366 1.00 12.63 ? 382 ASP B CB  1 
ATOM 6113 C CG  . ASP B 2 382  ? 183.004 201.540 168.280 1.00 12.61 ? 382 ASP B CG  1 
ATOM 6114 O OD1 . ASP B 2 382  ? 183.165 201.869 169.472 1.00 26.19 ? 382 ASP B OD1 1 
ATOM 6115 O OD2 . ASP B 2 382  ? 183.406 200.465 167.793 1.00 0.00  ? 382 ASP B OD2 1 
ATOM 6116 N N   . SER B 2 383  ? 179.142 204.502 167.349 1.00 24.80 ? 383 SER B N   1 
ATOM 6117 C CA  . SER B 2 383  ? 178.255 205.359 166.515 1.00 25.39 ? 383 SER B CA  1 
ATOM 6118 C C   . SER B 2 383  ? 179.083 206.323 165.659 1.00 21.41 ? 383 SER B C   1 
ATOM 6119 O O   . SER B 2 383  ? 178.902 206.321 164.426 1.00 18.12 ? 383 SER B O   1 
ATOM 6120 C CB  . SER B 2 383  ? 177.275 206.109 167.377 1.00 22.44 ? 383 SER B CB  1 
ATOM 6121 O OG  . SER B 2 383  ? 177.954 206.975 168.274 1.00 22.01 ? 383 SER B OG  1 
ATOM 6122 N N   . ARG B 2 384  ? 179.971 207.097 166.288 1.00 19.51 ? 384 ARG B N   1 
ATOM 6123 C CA  . ARG B 2 384  ? 180.787 208.099 165.549 1.00 18.91 ? 384 ARG B CA  1 
ATOM 6124 C C   . ARG B 2 384  ? 181.641 207.399 164.486 1.00 19.08 ? 384 ARG B C   1 
ATOM 6125 O O   . ARG B 2 384  ? 181.935 208.038 163.458 1.00 24.62 ? 384 ARG B O   1 
ATOM 6126 C CB  . ARG B 2 384  ? 181.668 208.881 166.527 1.00 15.77 ? 384 ARG B CB  1 
ATOM 6127 C CG  . ARG B 2 384  ? 180.894 209.552 167.652 1.00 21.74 ? 384 ARG B CG  1 
ATOM 6128 C CD  . ARG B 2 384  ? 181.796 210.298 168.615 1.00 22.52 ? 384 ARG B CD  1 
ATOM 6129 N NE  . ARG B 2 384  ? 181.041 210.941 169.680 1.00 23.67 ? 384 ARG B NE  1 
ATOM 6130 C CZ  . ARG B 2 384  ? 181.581 211.662 170.656 1.00 22.98 ? 384 ARG B CZ  1 
ATOM 6131 N NH1 . ARG B 2 384  ? 182.890 211.834 170.705 1.00 18.70 ? 384 ARG B NH1 1 
ATOM 6132 N NH2 . ARG B 2 384  ? 180.810 212.210 171.579 1.00 25.49 ? 384 ARG B NH2 1 
ATOM 6133 N N   . ARG B 2 385  ? 182.026 206.143 164.736 1.00 7.81  ? 385 ARG B N   1 
ATOM 6134 C CA  . ARG B 2 385  ? 182.885 205.379 163.790 1.00 8.95  ? 385 ARG B CA  1 
ATOM 6135 C C   . ARG B 2 385  ? 182.052 204.957 162.575 1.00 12.86 ? 385 ARG B C   1 
ATOM 6136 O O   . ARG B 2 385  ? 180.889 204.552 162.773 1.00 15.40 ? 385 ARG B O   1 
ATOM 6137 C CB  . ARG B 2 385  ? 183.462 204.154 164.505 1.00 8.60  ? 385 ARG B CB  1 
ATOM 6138 C CG  . ARG B 2 385  ? 184.592 203.459 163.762 1.00 12.96 ? 385 ARG B CG  1 
ATOM 6139 C CD  . ARG B 2 385  ? 185.823 204.340 163.688 1.00 13.06 ? 385 ARG B CD  1 
ATOM 6140 N NE  . ARG B 2 385  ? 186.484 204.578 164.963 1.00 10.24 ? 385 ARG B NE  1 
ATOM 6141 C CZ  . ARG B 2 385  ? 187.103 203.648 165.680 1.00 9.99  ? 385 ARG B CZ  1 
ATOM 6142 N NH1 . ARG B 2 385  ? 187.403 202.482 165.137 1.00 1.81  ? 385 ARG B NH1 1 
ATOM 6143 N NH2 . ARG B 2 385  ? 187.437 203.895 166.935 1.00 10.25 ? 385 ARG B NH2 1 
ATOM 6144 N N   . HIS B 2 386  ? 182.626 205.042 161.369 1.00 5.30  ? 386 HIS B N   1 
ATOM 6145 C CA  . HIS B 2 386  ? 181.895 204.603 160.148 1.00 0.35  ? 386 HIS B CA  1 
ATOM 6146 C C   . HIS B 2 386  ? 182.816 203.730 159.289 1.00 5.14  ? 386 HIS B C   1 
ATOM 6147 O O   . HIS B 2 386  ? 183.703 204.278 158.598 1.00 9.10  ? 386 HIS B O   1 
ATOM 6148 C CB  . HIS B 2 386  ? 181.366 205.814 159.372 1.00 9.56  ? 386 HIS B CB  1 
ATOM 6149 C CG  . HIS B 2 386  ? 180.670 206.821 160.226 1.00 11.05 ? 386 HIS B CG  1 
ATOM 6150 N ND1 . HIS B 2 386  ? 179.585 206.514 161.017 1.00 13.09 ? 386 HIS B ND1 1 
ATOM 6151 C CD2 . HIS B 2 386  ? 180.910 208.123 160.422 1.00 8.95  ? 386 HIS B CD2 1 
ATOM 6152 C CE1 . HIS B 2 386  ? 179.187 207.603 161.658 1.00 8.50  ? 386 HIS B CE1 1 
ATOM 6153 N NE2 . HIS B 2 386  ? 179.980 208.593 161.312 1.00 7.14  ? 386 HIS B NE2 1 
ATOM 6154 N N   . GLY B 2 387  ? 182.609 202.409 159.322 1.00 1.62  ? 387 GLY B N   1 
ATOM 6155 C CA  . GLY B 2 387  ? 183.429 201.507 158.535 1.00 0.02  ? 387 GLY B CA  1 
ATOM 6156 C C   . GLY B 2 387  ? 183.159 201.656 157.050 1.00 9.68  ? 387 GLY B C   1 
ATOM 6157 O O   . GLY B 2 387  ? 182.079 202.069 156.629 1.00 15.92 ? 387 GLY B O   1 
ATOM 6158 N N   . GLU B 2 388  ? 184.160 201.311 156.233 1.00 10.23 ? 388 GLU B N   1 
ATOM 6159 C CA  . GLU B 2 388  ? 184.010 201.473 154.794 1.00 1.06  ? 388 GLU B CA  1 
ATOM 6160 C C   . GLU B 2 388  ? 184.545 200.322 153.950 1.00 4.49  ? 388 GLU B C   1 
ATOM 6161 O O   . GLU B 2 388  ? 184.428 200.391 152.723 1.00 8.26  ? 388 GLU B O   1 
ATOM 6162 C CB  . GLU B 2 388  ? 184.672 202.783 154.341 1.00 0.00  ? 388 GLU B CB  1 
ATOM 6163 C CG  . GLU B 2 388  ? 183.686 203.928 154.190 1.00 1.99  ? 388 GLU B CG  1 
ATOM 6164 C CD  . GLU B 2 388  ? 184.274 205.269 154.573 1.00 9.07  ? 388 GLU B CD  1 
ATOM 6165 O OE1 . GLU B 2 388  ? 185.516 205.397 154.581 1.00 11.38 ? 388 GLU B OE1 1 
ATOM 6166 O OE2 . GLU B 2 388  ? 183.492 206.198 154.866 1.00 2.87  ? 388 GLU B OE2 1 
ATOM 6167 N N   . SER B 2 389  ? 185.116 199.277 154.547 1.00 1.27  ? 389 SER B N   1 
ATOM 6168 C CA  . SER B 2 389  ? 185.614 198.137 153.783 1.00 0.00  ? 389 SER B CA  1 
ATOM 6169 C C   . SER B 2 389  ? 185.909 196.991 154.738 1.00 0.07  ? 389 SER B C   1 
ATOM 6170 O O   . SER B 2 389  ? 186.039 197.193 155.948 1.00 8.54  ? 389 SER B O   1 
ATOM 6171 C CB  . SER B 2 389  ? 186.868 198.499 152.983 1.00 8.13  ? 389 SER B CB  1 
ATOM 6172 O OG  . SER B 2 389  ? 187.952 198.784 153.847 1.00 16.52 ? 389 SER B OG  1 
ATOM 6173 N N   . ILE B 2 390  ? 185.999 195.780 154.181 1.00 1.36  ? 390 ILE B N   1 
ATOM 6174 C CA  . ILE B 2 390  ? 186.414 194.604 154.942 1.00 4.92  ? 390 ILE B CA  1 
ATOM 6175 C C   . ILE B 2 390  ? 186.876 193.505 153.992 1.00 0.00  ? 390 ILE B C   1 
ATOM 6176 O O   . ILE B 2 390  ? 186.166 193.151 153.045 1.00 9.04  ? 390 ILE B O   1 
ATOM 6177 C CB  . ILE B 2 390  ? 185.277 194.107 155.853 1.00 0.00  ? 390 ILE B CB  1 
ATOM 6178 C CG1 . ILE B 2 390  ? 185.549 192.687 156.338 1.00 0.00  ? 390 ILE B CG1 1 
ATOM 6179 C CG2 . ILE B 2 390  ? 183.958 194.139 155.124 1.00 6.99  ? 390 ILE B CG2 1 
ATOM 6180 C CD1 . ILE B 2 390  ? 184.674 192.276 157.490 1.00 0.00  ? 390 ILE B CD1 1 
ATOM 6181 N N   . CYS B 2 391  ? 188.054 192.937 154.255 1.00 0.00  ? 391 CYS B N   1 
ATOM 6182 C CA  . CYS B 2 391  ? 188.637 191.890 153.428 1.00 0.00  ? 391 CYS B CA  1 
ATOM 6183 C C   . CYS B 2 391  ? 189.099 190.741 154.310 1.00 1.21  ? 391 CYS B C   1 
ATOM 6184 O O   . CYS B 2 391  ? 189.674 190.962 155.379 1.00 10.99 ? 391 CYS B O   1 
ATOM 6185 C CB  . CYS B 2 391  ? 189.822 192.413 152.607 1.00 0.00  ? 391 CYS B CB  1 
ATOM 6186 S SG  . CYS B 2 391  ? 189.416 193.719 151.429 1.00 12.16 ? 391 CYS B SG  1 
ATOM 6187 N N   . LEU B 2 392  ? 188.862 189.518 153.853 1.00 0.00  ? 392 LEU B N   1 
ATOM 6188 C CA  . LEU B 2 392  ? 189.173 188.319 154.614 1.00 0.00  ? 392 LEU B CA  1 
ATOM 6189 C C   . LEU B 2 392  ? 190.530 187.764 154.198 1.00 0.00  ? 392 LEU B C   1 
ATOM 6190 O O   . LEU B 2 392  ? 190.973 187.946 153.062 1.00 0.13  ? 392 LEU B O   1 
ATOM 6191 C CB  . LEU B 2 392  ? 188.085 187.262 154.406 1.00 0.00  ? 392 LEU B CB  1 
ATOM 6192 C CG  . LEU B 2 392  ? 187.726 186.293 155.533 1.00 0.00  ? 392 LEU B CG  1 
ATOM 6193 C CD1 . LEU B 2 392  ? 187.165 187.040 156.720 1.00 0.00  ? 392 LEU B CD1 1 
ATOM 6194 C CD2 . LEU B 2 392  ? 186.720 185.275 155.037 1.00 2.88  ? 392 LEU B CD2 1 
ATOM 6195 N N   . SER B 2 393  ? 191.211 187.129 155.158 1.00 2.30  ? 393 SER B N   1 
ATOM 6196 C CA  . SER B 2 393  ? 192.544 186.534 154.884 1.00 3.93  ? 393 SER B CA  1 
ATOM 6197 C C   . SER B 2 393  ? 192.358 185.233 154.097 1.00 16.56 ? 393 SER B C   1 
ATOM 6198 O O   . SER B 2 393  ? 191.283 184.614 154.220 1.00 10.79 ? 393 SER B O   1 
ATOM 6199 C CB  . SER B 2 393  ? 193.286 186.288 156.170 1.00 0.00  ? 393 SER B CB  1 
ATOM 6200 O OG  . SER B 2 393  ? 192.603 185.333 156.969 1.00 0.00  ? 393 SER B OG  1 
ATOM 6201 N N   . PRO B 2 394  ? 193.354 184.791 153.299 1.00 14.50 ? 394 PRO B N   1 
ATOM 6202 C CA  . PRO B 2 394  ? 193.234 183.547 152.519 1.00 2.35  ? 394 PRO B CA  1 
ATOM 6203 C C   . PRO B 2 394  ? 192.833 182.350 153.359 1.00 7.29  ? 394 PRO B C   1 
ATOM 6204 O O   . PRO B 2 394  ? 192.111 181.472 152.870 1.00 11.94 ? 394 PRO B O   1 
ATOM 6205 C CB  . PRO B 2 394  ? 194.639 183.370 151.926 1.00 2.38  ? 394 PRO B CB  1 
ATOM 6206 C CG  . PRO B 2 394  ? 195.215 184.731 151.898 1.00 5.35  ? 394 PRO B CG  1 
ATOM 6207 C CD  . PRO B 2 394  ? 194.656 185.448 153.088 1.00 13.31 ? 394 PRO B CD  1 
ATOM 6208 N N   . CYS B 2 395  ? 193.276 182.291 154.613 1.00 12.63 ? 395 CYS B N   1 
ATOM 6209 C CA  . CYS B 2 395  ? 192.921 181.205 155.515 1.00 7.47  ? 395 CYS B CA  1 
ATOM 6210 C C   . CYS B 2 395  ? 191.548 181.383 156.147 1.00 14.26 ? 395 CYS B C   1 
ATOM 6211 O O   . CYS B 2 395  ? 191.077 180.463 156.825 1.00 9.52  ? 395 CYS B O   1 
ATOM 6212 C CB  . CYS B 2 395  ? 193.971 181.087 156.617 1.00 0.45  ? 395 CYS B CB  1 
ATOM 6213 S SG  . CYS B 2 395  ? 194.193 182.610 157.553 1.00 0.00  ? 395 CYS B SG  1 
ATOM 6214 N N   . ASN B 2 396  ? 190.916 182.538 155.906 1.00 15.94 ? 396 ASN B N   1 
ATOM 6215 C CA  . ASN B 2 396  ? 189.549 182.809 156.432 1.00 6.78  ? 396 ASN B CA  1 
ATOM 6216 C C   . ASN B 2 396  ? 189.562 182.782 157.964 1.00 3.35  ? 396 ASN B C   1 
ATOM 6217 O O   . ASN B 2 396  ? 188.567 182.312 158.550 1.00 6.60  ? 396 ASN B O   1 
ATOM 6218 C CB  . ASN B 2 396  ? 188.510 181.842 155.855 1.00 5.13  ? 396 ASN B CB  1 
ATOM 6219 C CG  . ASN B 2 396  ? 188.312 182.013 154.364 1.00 7.57  ? 396 ASN B CG  1 
ATOM 6220 O OD1 . ASN B 2 396  ? 189.249 182.345 153.642 1.00 2.95  ? 396 ASN B OD1 1 
ATOM 6221 N ND2 . ASN B 2 396  ? 187.095 181.791 153.895 1.00 17.23 ? 396 ASN B ND2 1 
ATOM 6222 N N   . THR B 2 397  ? 190.642 183.268 158.582 1.00 6.33  ? 397 THR B N   1 
ATOM 6223 C CA  . THR B 2 397  ? 190.705 183.339 160.066 1.00 12.90 ? 397 THR B CA  1 
ATOM 6224 C C   . THR B 2 397  ? 190.831 184.801 160.501 1.00 15.37 ? 397 THR B C   1 
ATOM 6225 O O   . THR B 2 397  ? 190.561 185.084 161.686 1.00 7.26  ? 397 THR B O   1 
ATOM 6226 C CB  . THR B 2 397  ? 191.872 182.512 160.618 1.00 0.00  ? 397 THR B CB  1 
ATOM 6227 O OG1 . THR B 2 397  ? 193.086 183.167 160.248 1.00 0.89  ? 397 THR B OG1 1 
ATOM 6228 C CG2 . THR B 2 397  ? 191.879 181.086 160.111 1.00 4.52  ? 397 THR B CG2 1 
ATOM 6229 N N   . LEU B 2 398  ? 191.222 185.690 159.582 1.00 7.32  ? 398 LEU B N   1 
ATOM 6230 C CA  . LEU B 2 398  ? 191.451 187.111 159.955 1.00 0.19  ? 398 LEU B CA  1 
ATOM 6231 C C   . LEU B 2 398  ? 190.713 188.044 158.992 1.00 4.37  ? 398 LEU B C   1 
ATOM 6232 O O   . LEU B 2 398  ? 190.567 187.674 157.811 1.00 9.05  ? 398 LEU B O   1 
ATOM 6233 C CB  . LEU B 2 398  ? 192.956 187.396 159.919 1.00 1.31  ? 398 LEU B CB  1 
ATOM 6234 C CG  . LEU B 2 398  ? 193.791 186.679 160.978 1.00 0.00  ? 398 LEU B CG  1 
ATOM 6235 C CD1 . LEU B 2 398  ? 195.273 186.920 160.741 1.00 0.00  ? 398 LEU B CD1 1 
ATOM 6236 C CD2 . LEU B 2 398  ? 193.395 187.128 162.376 1.00 4.81  ? 398 LEU B CD2 1 
ATOM 6237 N N   . ALA B 2 399  ? 190.272 189.205 159.483 1.00 0.00  ? 399 ALA B N   1 
ATOM 6238 C CA  . ALA B 2 399  ? 189.624 190.192 158.631 1.00 0.00  ? 399 ALA B CA  1 
ATOM 6239 C C   . ALA B 2 399  ? 190.282 191.539 158.865 1.00 0.00  ? 399 ALA B C   1 
ATOM 6240 O O   . ALA B 2 399  ? 190.753 191.817 159.968 1.00 25.30 ? 399 ALA B O   1 
ATOM 6241 C CB  . ALA B 2 399  ? 188.120 190.282 158.909 1.00 0.00  ? 399 ALA B CB  1 
ATOM 6242 N N   . ALA B 2 400  ? 190.329 192.369 157.831 1.00 0.00  ? 400 ALA B N   1 
ATOM 6243 C CA  . ALA B 2 400  ? 190.911 193.702 157.926 1.00 0.00  ? 400 ALA B CA  1 
ATOM 6244 C C   . ALA B 2 400  ? 189.846 194.727 157.567 1.00 3.19  ? 400 ALA B C   1 
ATOM 6245 O O   . ALA B 2 400  ? 189.271 194.669 156.475 1.00 11.46 ? 400 ALA B O   1 
ATOM 6246 C CB  . ALA B 2 400  ? 192.126 193.838 157.010 1.00 0.00  ? 400 ALA B CB  1 
ATOM 6247 N N   . VAL B 2 401  ? 189.591 195.668 158.473 1.00 0.00  ? 401 VAL B N   1 
ATOM 6248 C CA  . VAL B 2 401  ? 188.506 196.631 158.317 1.00 0.00  ? 401 VAL B CA  1 
ATOM 6249 C C   . VAL B 2 401  ? 189.072 198.040 158.421 1.00 0.00  ? 401 VAL B C   1 
ATOM 6250 O O   . VAL B 2 401  ? 189.862 198.334 159.323 1.00 0.00  ? 401 VAL B O   1 
ATOM 6251 C CB  . VAL B 2 401  ? 187.391 196.401 159.354 1.00 0.00  ? 401 VAL B CB  1 
ATOM 6252 C CG1 . VAL B 2 401  ? 187.970 196.276 160.746 1.00 0.00  ? 401 VAL B CG1 1 
ATOM 6253 C CG2 . VAL B 2 401  ? 186.371 197.523 159.297 1.00 1.43  ? 401 VAL B CG2 1 
ATOM 6254 N N   . THR B 2 402  ? 188.672 198.906 157.494 1.00 6.89  ? 402 THR B N   1 
ATOM 6255 C CA  . THR B 2 402  ? 189.109 200.294 157.462 1.00 0.00  ? 402 THR B CA  1 
ATOM 6256 C C   . THR B 2 402  ? 187.949 201.204 157.847 1.00 7.29  ? 402 THR B C   1 
ATOM 6257 O O   . THR B 2 402  ? 186.811 200.989 157.415 1.00 11.95 ? 402 THR B O   1 
ATOM 6258 C CB  . THR B 2 402  ? 189.634 200.671 156.073 1.00 0.00  ? 402 THR B CB  1 
ATOM 6259 O OG1 . THR B 2 402  ? 190.807 199.903 155.778 1.00 6.13  ? 402 THR B OG1 1 
ATOM 6260 C CG2 . THR B 2 402  ? 189.982 202.148 156.009 1.00 0.00  ? 402 THR B CG2 1 
ATOM 6261 N N   . ASP B 2 403  ? 188.231 202.205 158.678 1.00 4.58  ? 403 ASP B N   1 
ATOM 6262 C CA  . ASP B 2 403  ? 187.208 203.157 159.090 1.00 0.00  ? 403 ASP B CA  1 
ATOM 6263 C C   . ASP B 2 403  ? 187.510 204.532 158.501 1.00 1.78  ? 403 ASP B C   1 
ATOM 6264 O O   . ASP B 2 403  ? 188.511 204.731 157.808 1.00 8.45  ? 403 ASP B O   1 
ATOM 6265 C CB  . ASP B 2 403  ? 187.102 203.206 160.615 1.00 13.78 ? 403 ASP B CB  1 
ATOM 6266 C CG  . ASP B 2 403  ? 188.434 203.457 161.283 1.00 18.49 ? 403 ASP B CG  1 
ATOM 6267 O OD1 . ASP B 2 403  ? 189.151 204.383 160.852 1.00 14.25 ? 403 ASP B OD1 1 
ATOM 6268 O OD2 . ASP B 2 403  ? 188.769 202.725 162.239 1.00 11.78 ? 403 ASP B OD2 1 
ATOM 6269 N N   . ASP B 2 404  ? 186.629 205.489 158.784 1.00 1.86  ? 404 ASP B N   1 
ATOM 6270 C CA  . ASP B 2 404  ? 186.765 206.838 158.250 1.00 6.39  ? 404 ASP B CA  1 
ATOM 6271 C C   . ASP B 2 404  ? 187.660 207.730 159.100 1.00 9.17  ? 404 ASP B C   1 
ATOM 6272 O O   . ASP B 2 404  ? 187.917 208.873 158.708 1.00 6.81  ? 404 ASP B O   1 
ATOM 6273 C CB  . ASP B 2 404  ? 185.392 207.496 158.099 1.00 5.83  ? 404 ASP B CB  1 
ATOM 6274 C CG  . ASP B 2 404  ? 184.591 207.461 159.376 1.00 8.48  ? 404 ASP B CG  1 
ATOM 6275 O OD1 . ASP B 2 404  ? 184.771 206.514 160.167 1.00 5.36  ? 404 ASP B OD1 1 
ATOM 6276 O OD2 . ASP B 2 404  ? 183.790 208.391 159.595 1.00 9.96  ? 404 ASP B OD2 1 
ATOM 6277 N N   . PHE B 2 405  ? 188.139 207.200 160.231 1.00 8.87  ? 405 PHE B N   1 
ATOM 6278 C CA  . PHE B 2 405  ? 189.080 207.960 161.096 1.00 5.86  ? 405 PHE B CA  1 
ATOM 6279 C C   . PHE B 2 405  ? 190.502 207.783 160.558 1.00 4.56  ? 405 PHE B C   1 
ATOM 6280 O O   . PHE B 2 405  ? 191.460 208.149 161.267 1.00 2.28  ? 405 PHE B O   1 
ATOM 6281 C CB  . PHE B 2 405  ? 189.010 207.466 162.542 1.00 6.72  ? 405 PHE B CB  1 
ATOM 6282 C CG  . PHE B 2 405  ? 187.863 208.006 163.358 1.00 9.53  ? 405 PHE B CG  1 
ATOM 6283 C CD1 . PHE B 2 405  ? 186.549 207.725 163.018 1.00 3.11  ? 405 PHE B CD1 1 
ATOM 6284 C CD2 . PHE B 2 405  ? 188.100 208.800 164.468 1.00 7.55  ? 405 PHE B CD2 1 
ATOM 6285 C CE1 . PHE B 2 405  ? 185.500 208.224 163.774 1.00 0.52  ? 405 PHE B CE1 1 
ATOM 6286 C CE2 . PHE B 2 405  ? 187.052 209.300 165.224 1.00 5.00  ? 405 PHE B CE2 1 
ATOM 6287 C CZ  . PHE B 2 405  ? 185.753 209.010 164.875 1.00 0.40  ? 405 PHE B CZ  1 
ATOM 6288 N N   . GLY B 2 406  ? 190.634 207.229 159.349 1.00 12.08 ? 406 GLY B N   1 
ATOM 6289 C CA  . GLY B 2 406  ? 191.965 206.977 158.764 1.00 9.97  ? 406 GLY B CA  1 
ATOM 6290 C C   . GLY B 2 406  ? 192.749 205.948 159.559 1.00 4.75  ? 406 GLY B C   1 
ATOM 6291 O O   . GLY B 2 406  ? 193.952 206.176 159.790 1.00 9.69  ? 406 GLY B O   1 
ATOM 6292 N N   . ARG B 2 407  ? 192.100 204.853 159.971 1.00 0.00  ? 407 ARG B N   1 
ATOM 6293 C CA  . ARG B 2 407  ? 192.781 203.786 160.756 1.00 0.00  ? 407 ARG B CA  1 
ATOM 6294 C C   . ARG B 2 407  ? 192.306 202.410 160.273 1.00 5.03  ? 407 ARG B C   1 
ATOM 6295 O O   . ARG B 2 407  ? 191.189 202.331 159.724 1.00 9.16  ? 407 ARG B O   1 
ATOM 6296 C CB  . ARG B 2 407  ? 192.506 203.961 162.253 1.00 2.59  ? 407 ARG B CB  1 
ATOM 6297 C CG  . ARG B 2 407  ? 193.276 205.105 162.897 1.00 0.68  ? 407 ARG B CG  1 
ATOM 6298 C CD  . ARG B 2 407  ? 192.939 205.299 164.363 1.00 4.47  ? 407 ARG B CD  1 
ATOM 6299 N NE  . ARG B 2 407  ? 191.602 205.833 164.576 1.00 11.96 ? 407 ARG B NE  1 
ATOM 6300 C CZ  . ARG B 2 407  ? 190.653 205.229 165.281 1.00 9.96  ? 407 ARG B CZ  1 
ATOM 6301 N NH1 . ARG B 2 407  ? 190.787 203.960 165.621 1.00 5.10  ? 407 ARG B NH1 1 
ATOM 6302 N NH2 . ARG B 2 407  ? 189.573 205.898 165.646 1.00 15.83 ? 407 ARG B NH2 1 
ATOM 6303 N N   . VAL B 2 408  ? 193.128 201.372 160.471 1.00 5.29  ? 408 VAL B N   1 
ATOM 6304 C CA  . VAL B 2 408  ? 192.752 199.997 160.021 1.00 2.07  ? 408 VAL B CA  1 
ATOM 6305 C C   . VAL B 2 408  ? 192.852 199.032 161.207 1.00 5.00  ? 408 VAL B C   1 
ATOM 6306 O O   . VAL B 2 408  ? 193.832 199.137 161.968 1.00 10.16 ? 408 VAL B O   1 
ATOM 6307 C CB  . VAL B 2 408  ? 193.615 199.539 158.829 1.00 0.00  ? 408 VAL B CB  1 
ATOM 6308 C CG1 . VAL B 2 408  ? 193.329 198.098 158.437 1.00 3.47  ? 408 VAL B CG1 1 
ATOM 6309 C CG2 . VAL B 2 408  ? 193.482 200.465 157.630 1.00 0.00  ? 408 VAL B CG2 1 
ATOM 6310 N N   . ILE B 2 409  ? 191.875 198.133 161.353 1.00 5.00  ? 409 ILE B N   1 
ATOM 6311 C CA  . ILE B 2 409  ? 191.849 197.182 162.455 1.00 0.00  ? 409 ILE B CA  1 
ATOM 6312 C C   . ILE B 2 409  ? 191.891 195.774 161.883 1.00 1.61  ? 409 ILE B C   1 
ATOM 6313 O O   . ILE B 2 409  ? 191.410 195.519 160.772 1.00 23.96 ? 409 ILE B O   1 
ATOM 6314 C CB  . ILE B 2 409  ? 190.593 197.380 163.328 1.00 0.00  ? 409 ILE B CB  1 
ATOM 6315 C CG1 . ILE B 2 409  ? 190.211 198.858 163.381 1.00 0.00  ? 409 ILE B CG1 1 
ATOM 6316 C CG2 . ILE B 2 409  ? 190.823 196.851 164.721 1.00 5.15  ? 409 ILE B CG2 1 
ATOM 6317 C CD1 . ILE B 2 409  ? 188.822 199.105 163.911 1.00 6.88  ? 409 ILE B CD1 1 
ATOM 6318 N N   . LEU B 2 410  ? 192.471 194.854 162.648 1.00 0.00  ? 410 LEU B N   1 
ATOM 6319 C CA  . LEU B 2 410  ? 192.529 193.448 162.273 1.00 0.00  ? 410 LEU B CA  1 
ATOM 6320 C C   . LEU B 2 410  ? 191.757 192.634 163.300 1.00 0.00  ? 410 LEU B C   1 
ATOM 6321 O O   . LEU B 2 410  ? 192.004 192.758 164.503 1.00 20.27 ? 410 LEU B O   1 
ATOM 6322 C CB  . LEU B 2 410  ? 193.978 192.968 162.181 1.00 0.00  ? 410 LEU B CB  1 
ATOM 6323 C CG  . LEU B 2 410  ? 194.217 191.485 161.912 1.00 0.00  ? 410 LEU B CG  1 
ATOM 6324 C CD1 . LEU B 2 410  ? 195.199 191.318 160.772 1.00 2.90  ? 410 LEU B CD1 1 
ATOM 6325 C CD2 . LEU B 2 410  ? 194.738 190.801 163.157 1.00 0.00  ? 410 LEU B CD2 1 
ATOM 6326 N N   . LEU B 2 411  ? 190.831 191.804 162.830 1.00 0.00  ? 411 LEU B N   1 
ATOM 6327 C CA  . LEU B 2 411  ? 189.930 191.056 163.695 1.00 0.00  ? 411 LEU B CA  1 
ATOM 6328 C C   . LEU B 2 411  ? 190.134 189.560 163.515 1.00 2.46  ? 411 LEU B C   1 
ATOM 6329 O O   . LEU B 2 411  ? 190.404 189.089 162.406 1.00 23.99 ? 411 LEU B O   1 
ATOM 6330 C CB  . LEU B 2 411  ? 188.464 191.387 163.399 1.00 0.00  ? 411 LEU B CB  1 
ATOM 6331 C CG  . LEU B 2 411  ? 188.024 192.844 163.321 1.00 0.00  ? 411 LEU B CG  1 
ATOM 6332 C CD1 . LEU B 2 411  ? 186.686 192.923 162.631 1.00 0.00  ? 411 LEU B CD1 1 
ATOM 6333 C CD2 . LEU B 2 411  ? 187.926 193.435 164.704 1.00 8.70  ? 411 LEU B CD2 1 
ATOM 6334 N N   . ASP B 2 412  ? 189.988 188.820 164.614 1.00 0.00  ? 412 ASP B N   1 
ATOM 6335 C CA  . ASP B 2 412  ? 189.896 187.364 164.581 1.00 9.52  ? 412 ASP B CA  1 
ATOM 6336 C C   . ASP B 2 412  ? 188.419 186.996 164.498 1.00 7.69  ? 412 ASP B C   1 
ATOM 6337 O O   . ASP B 2 412  ? 187.661 187.238 165.443 1.00 7.91  ? 412 ASP B O   1 
ATOM 6338 C CB  . ASP B 2 412  ? 190.552 186.752 165.816 1.00 3.01  ? 412 ASP B CB  1 
ATOM 6339 C CG  . ASP B 2 412  ? 190.865 185.273 165.646 1.00 4.46  ? 412 ASP B CG  1 
ATOM 6340 O OD1 . ASP B 2 412  ? 189.985 184.520 165.178 1.00 1.96  ? 412 ASP B OD1 1 
ATOM 6341 O OD2 . ASP B 2 412  ? 191.996 184.861 165.982 1.00 6.27  ? 412 ASP B OD2 1 
ATOM 6342 N N   . VAL B 2 413  ? 188.007 186.414 163.369 1.00 6.48  ? 413 VAL B N   1 
ATOM 6343 C CA  . VAL B 2 413  ? 186.584 186.181 163.142 1.00 0.61  ? 413 VAL B CA  1 
ATOM 6344 C C   . VAL B 2 413  ? 186.029 185.134 164.102 1.00 6.01  ? 413 VAL B C   1 
ATOM 6345 O O   . VAL B 2 413  ? 184.844 185.177 164.455 1.00 3.68  ? 413 VAL B O   1 
ATOM 6346 C CB  . VAL B 2 413  ? 186.329 185.798 161.672 1.00 0.00  ? 413 VAL B CB  1 
ATOM 6347 C CG1 . VAL B 2 413  ? 187.045 186.765 160.749 1.00 6.09  ? 413 VAL B CG1 1 
ATOM 6348 C CG2 . VAL B 2 413  ? 186.771 184.372 161.394 1.00 0.00  ? 413 VAL B CG2 1 
ATOM 6349 N N   . ALA B 2 414  ? 186.859 184.189 164.547 1.00 15.42 ? 414 ALA B N   1 
ATOM 6350 C CA  . ALA B 2 414  ? 186.394 183.126 165.429 1.00 3.97  ? 414 ALA B CA  1 
ATOM 6351 C C   . ALA B 2 414  ? 186.148 183.597 166.855 1.00 6.16  ? 414 ALA B C   1 
ATOM 6352 O O   . ALA B 2 414  ? 185.592 182.835 167.654 1.00 8.88  ? 414 ALA B O   1 
ATOM 6353 C CB  . ALA B 2 414  ? 187.398 181.972 165.438 1.00 3.10  ? 414 ALA B CB  1 
ATOM 6354 N N   . ARG B 2 415  ? 186.550 184.823 167.196 1.00 0.20  ? 415 ARG B N   1 
ATOM 6355 C CA  . ARG B 2 415  ? 186.353 185.369 168.529 1.00 4.74  ? 415 ARG B CA  1 
ATOM 6356 C C   . ARG B 2 415  ? 185.623 186.703 168.546 1.00 11.36 ? 415 ARG B C   1 
ATOM 6357 O O   . ARG B 2 415  ? 185.057 187.058 169.585 1.00 11.35 ? 415 ARG B O   1 
ATOM 6358 C CB  . ARG B 2 415  ? 187.703 185.545 169.241 1.00 5.11  ? 415 ARG B CB  1 
ATOM 6359 C CG  . ARG B 2 415  ? 188.276 184.264 169.813 1.00 1.79  ? 415 ARG B CG  1 
ATOM 6360 C CD  . ARG B 2 415  ? 189.373 184.561 170.816 1.00 5.65  ? 415 ARG B CD  1 
ATOM 6361 N NE  . ARG B 2 415  ? 190.476 185.300 170.213 1.00 0.16  ? 415 ARG B NE  1 
ATOM 6362 C CZ  . ARG B 2 415  ? 191.449 185.881 170.901 1.00 1.82  ? 415 ARG B CZ  1 
ATOM 6363 N NH1 . ARG B 2 415  ? 191.487 185.832 172.222 1.00 9.33  ? 415 ARG B NH1 1 
ATOM 6364 N NH2 . ARG B 2 415  ? 192.411 186.526 170.246 1.00 0.43  ? 415 ARG B NH2 1 
ATOM 6365 N N   . GLY B 2 416  ? 185.614 187.441 167.442 1.00 2.15  ? 416 GLY B N   1 
ATOM 6366 C CA  . GLY B 2 416  ? 184.966 188.739 167.407 1.00 4.78  ? 416 GLY B CA  1 
ATOM 6367 C C   . GLY B 2 416  ? 185.680 189.824 168.185 1.00 0.00  ? 416 GLY B C   1 
ATOM 6368 O O   . GLY B 2 416  ? 185.025 190.729 168.718 1.00 0.00  ? 416 GLY B O   1 
ATOM 6369 N N   . ILE B 2 417  ? 187.010 189.760 168.264 1.00 0.51  ? 417 ILE B N   1 
ATOM 6370 C CA  . ILE B 2 417  ? 187.808 190.772 168.941 1.00 0.00  ? 417 ILE B CA  1 
ATOM 6371 C C   . ILE B 2 417  ? 188.894 191.249 167.988 1.00 7.05  ? 417 ILE B C   1 
ATOM 6372 O O   . ILE B 2 417  ? 189.212 190.597 166.992 1.00 3.28  ? 417 ILE B O   1 
ATOM 6373 C CB  . ILE B 2 417  ? 188.441 190.260 170.256 1.00 0.00  ? 417 ILE B CB  1 
ATOM 6374 C CG1 . ILE B 2 417  ? 189.803 189.621 169.985 1.00 0.00  ? 417 ILE B CG1 1 
ATOM 6375 C CG2 . ILE B 2 417  ? 187.525 189.271 170.952 1.00 0.00  ? 417 ILE B CG2 1 
ATOM 6376 C CD1 . ILE B 2 417  ? 190.623 189.391 171.230 1.00 0.00  ? 417 ILE B CD1 1 
ATOM 6377 N N   . ALA B 2 418  ? 189.451 192.426 168.292 1.00 0.00  ? 418 ALA B N   1 
ATOM 6378 C CA  . ALA B 2 418  ? 190.519 192.999 167.440 1.00 0.00  ? 418 ALA B CA  1 
ATOM 6379 C C   . ALA B 2 418  ? 191.886 192.559 167.973 1.00 0.00  ? 418 ALA B C   1 
ATOM 6380 O O   . ALA B 2 418  ? 191.997 192.324 169.193 1.00 21.92 ? 418 ALA B O   1 
ATOM 6381 C CB  . ALA B 2 418  ? 190.401 194.502 167.415 1.00 0.00  ? 418 ALA B CB  1 
ATOM 6382 N N   . ILE B 2 419  ? 192.876 192.428 167.086 1.00 0.00  ? 419 ILE B N   1 
ATOM 6383 C CA  . ILE B 2 419  ? 194.223 191.941 167.509 1.00 1.36  ? 419 ILE B CA  1 
ATOM 6384 C C   . ILE B 2 419  ? 195.224 193.092 167.367 1.00 1.71  ? 419 ILE B C   1 
ATOM 6385 O O   . ILE B 2 419  ? 195.935 193.379 168.351 1.00 12.65 ? 419 ILE B O   1 
ATOM 6386 C CB  . ILE B 2 419  ? 194.640 190.712 166.677 1.00 3.76  ? 419 ILE B CB  1 
ATOM 6387 C CG1 . ILE B 2 419  ? 193.491 189.712 166.519 1.00 8.51  ? 419 ILE B CG1 1 
ATOM 6388 C CG2 . ILE B 2 419  ? 195.881 190.057 167.264 1.00 0.00  ? 419 ILE B CG2 1 
ATOM 6389 C CD1 . ILE B 2 419  ? 193.048 189.075 167.815 1.00 7.13  ? 419 ILE B CD1 1 
ATOM 6390 N N   . ARG B 2 420  ? 195.264 193.730 166.193 1.00 0.00  ? 420 ARG B N   1 
ATOM 6391 C CA  . ARG B 2 420  ? 196.234 194.831 165.947 1.00 0.00  ? 420 ARG B CA  1 
ATOM 6392 C C   . ARG B 2 420  ? 195.549 195.947 165.150 1.00 2.44  ? 420 ARG B C   1 
ATOM 6393 O O   . ARG B 2 420  ? 194.827 195.624 164.186 1.00 17.54 ? 420 ARG B O   1 
ATOM 6394 C CB  . ARG B 2 420  ? 197.459 194.292 165.202 1.00 0.00  ? 420 ARG B CB  1 
ATOM 6395 C CG  . ARG B 2 420  ? 198.581 195.303 165.024 1.00 1.66  ? 420 ARG B CG  1 
ATOM 6396 C CD  . ARG B 2 420  ? 199.802 194.649 164.408 1.00 3.40  ? 420 ARG B CD  1 
ATOM 6397 N NE  . ARG B 2 420  ? 200.847 195.597 164.053 1.00 3.90  ? 420 ARG B NE  1 
ATOM 6398 C CZ  . ARG B 2 420  ? 201.985 195.269 163.453 1.00 3.47  ? 420 ARG B CZ  1 
ATOM 6399 N NH1 . ARG B 2 420  ? 202.149 194.053 162.964 1.00 1.81  ? 420 ARG B NH1 1 
ATOM 6400 N NH2 . ARG B 2 420  ? 202.953 196.162 163.338 1.00 3.08  ? 420 ARG B NH2 1 
ATOM 6401 N N   . MET B 2 421  ? 195.772 197.207 165.532 1.00 1.09  ? 421 MET B N   1 
ATOM 6402 C CA  . MET B 2 421  ? 195.116 198.343 164.831 1.00 5.29  ? 421 MET B CA  1 
ATOM 6403 C C   . MET B 2 421  ? 196.185 199.337 164.363 1.00 8.12  ? 421 MET B C   1 
ATOM 6404 O O   . MET B 2 421  ? 196.807 199.986 165.228 1.00 4.44  ? 421 MET B O   1 
ATOM 6405 C CB  . MET B 2 421  ? 194.112 199.047 165.751 1.00 0.00  ? 421 MET B CB  1 
ATOM 6406 C CG  . MET B 2 421  ? 193.709 200.431 165.279 1.00 5.87  ? 421 MET B CG  1 
ATOM 6407 S SD  . MET B 2 421  ? 192.369 201.120 166.281 1.00 12.84 ? 421 MET B SD  1 
ATOM 6408 C CE  . MET B 2 421  ? 193.262 201.551 167.774 1.00 0.27  ? 421 MET B CE  1 
ATOM 6409 N N   . TRP B 2 422  ? 196.483 199.315 163.059 1.00 12.26 ? 422 TRP B N   1 
ATOM 6410 C CA  . TRP B 2 422  ? 197.535 200.199 162.498 1.00 2.69  ? 422 TRP B CA  1 
ATOM 6411 C C   . TRP B 2 422  ? 196.981 201.614 162.400 1.00 5.52  ? 422 TRP B C   1 
ATOM 6412 O O   . TRP B 2 422  ? 195.743 201.780 162.481 1.00 16.97 ? 422 TRP B O   1 
ATOM 6413 C CB  . TRP B 2 422  ? 197.994 199.702 161.120 1.00 0.02  ? 422 TRP B CB  1 
ATOM 6414 C CG  . TRP B 2 422  ? 198.605 198.326 161.111 1.00 1.47  ? 422 TRP B CG  1 
ATOM 6415 C CD1 . TRP B 2 422  ? 199.930 198.023 161.004 1.00 3.92  ? 422 TRP B CD1 1 
ATOM 6416 C CD2 . TRP B 2 422  ? 197.908 197.061 161.159 1.00 0.00  ? 422 TRP B CD2 1 
ATOM 6417 N NE1 . TRP B 2 422  ? 200.111 196.666 161.012 1.00 4.27  ? 422 TRP B NE1 1 
ATOM 6418 C CE2 . TRP B 2 422  ? 198.891 196.050 161.099 1.00 0.00  ? 422 TRP B CE2 1 
ATOM 6419 C CE3 . TRP B 2 422  ? 196.563 196.688 161.254 1.00 0.69  ? 422 TRP B CE3 1 
ATOM 6420 C CZ2 . TRP B 2 422  ? 198.568 194.696 161.130 1.00 1.81  ? 422 TRP B CZ2 1 
ATOM 6421 C CZ3 . TRP B 2 422  ? 196.246 195.349 161.281 1.00 4.35  ? 422 TRP B CZ3 1 
ATOM 6422 C CH2 . TRP B 2 422  ? 197.235 194.369 161.220 1.00 0.00  ? 422 TRP B CH2 1 
ATOM 6423 N N   . LYS B 2 423  ? 197.857 202.602 162.216 1.00 8.10  ? 423 LYS B N   1 
ATOM 6424 C CA  . LYS B 2 423  ? 197.353 203.999 162.231 1.00 1.11  ? 423 LYS B CA  1 
ATOM 6425 C C   . LYS B 2 423  ? 197.938 204.827 161.080 1.00 0.00  ? 423 LYS B C   1 
ATOM 6426 O O   . LYS B 2 423  ? 199.029 204.474 160.592 1.00 0.98  ? 423 LYS B O   1 
ATOM 6427 C CB  . LYS B 2 423  ? 197.639 204.658 163.586 1.00 7.09  ? 423 LYS B CB  1 
ATOM 6428 C CG  . LYS B 2 423  ? 196.778 204.157 164.738 1.00 5.86  ? 423 LYS B CG  1 
ATOM 6429 C CD  . LYS B 2 423  ? 196.623 205.158 165.862 1.00 0.60  ? 423 LYS B CD  1 
ATOM 6430 C CE  . LYS B 2 423  ? 195.600 204.731 166.892 1.00 2.72  ? 423 LYS B CE  1 
ATOM 6431 N NZ  . LYS B 2 423  ? 195.334 205.801 167.882 1.00 5.56  ? 423 LYS B NZ  1 
ATOM 6432 N N   . GLY B 2 424  ? 197.234 205.892 160.679 1.00 1.15  ? 424 GLY B N   1 
ATOM 6433 C CA  . GLY B 2 424  ? 197.723 206.783 159.607 1.00 1.45  ? 424 GLY B CA  1 
ATOM 6434 C C   . GLY B 2 424  ? 197.373 206.270 158.221 1.00 3.14  ? 424 GLY B C   1 
ATOM 6435 O O   . GLY B 2 424  ? 198.236 206.378 157.328 1.00 4.22  ? 424 GLY B O   1 
ATOM 6436 N N   . TYR B 2 425  ? 196.151 205.761 158.025 1.00 5.10  ? 425 TYR B N   1 
ATOM 6437 C CA  . TYR B 2 425  ? 195.800 205.156 156.707 1.00 4.20  ? 425 TYR B CA  1 
ATOM 6438 C C   . TYR B 2 425  ? 194.405 205.589 156.269 1.00 1.44  ? 425 TYR B C   1 
ATOM 6439 O O   . TYR B 2 425  ? 193.462 204.771 156.343 1.00 1.74  ? 425 TYR B O   1 
ATOM 6440 C CB  . TYR B 2 425  ? 195.995 203.639 156.797 1.00 6.62  ? 425 TYR B CB  1 
ATOM 6441 C CG  . TYR B 2 425  ? 197.468 203.337 157.020 1.00 1.90  ? 425 TYR B CG  1 
ATOM 6442 C CD1 . TYR B 2 425  ? 198.412 203.656 156.051 1.00 4.13  ? 425 TYR B CD1 1 
ATOM 6443 C CD2 . TYR B 2 425  ? 197.916 202.821 158.230 1.00 1.36  ? 425 TYR B CD2 1 
ATOM 6444 C CE1 . TYR B 2 425  ? 199.760 203.420 156.269 1.00 3.71  ? 425 TYR B CE1 1 
ATOM 6445 C CE2 . TYR B 2 425  ? 199.261 202.588 158.460 1.00 2.57  ? 425 TYR B CE2 1 
ATOM 6446 C CZ  . TYR B 2 425  ? 200.183 202.885 157.475 1.00 4.57  ? 425 TYR B CZ  1 
ATOM 6447 O OH  . TYR B 2 425  ? 201.503 202.646 157.719 1.00 7.43  ? 425 TYR B OH  1 
ATOM 6448 N N   . ARG B 2 426  ? 194.273 206.840 155.818 1.00 1.51  ? 426 ARG B N   1 
ATOM 6449 C CA  . ARG B 2 426  ? 192.997 207.299 155.286 1.00 1.49  ? 426 ARG B CA  1 
ATOM 6450 C C   . ARG B 2 426  ? 192.831 206.782 153.864 1.00 1.47  ? 426 ARG B C   1 
ATOM 6451 O O   . ARG B 2 426  ? 193.747 206.891 153.039 1.00 2.96  ? 426 ARG B O   1 
ATOM 6452 C CB  . ARG B 2 426  ? 192.909 208.830 155.288 1.00 6.11  ? 426 ARG B CB  1 
ATOM 6453 C CG  . ARG B 2 426  ? 192.870 209.462 156.660 1.00 2.77  ? 426 ARG B CG  1 
ATOM 6454 C CD  . ARG B 2 426  ? 192.734 210.962 156.532 1.00 3.74  ? 426 ARG B CD  1 
ATOM 6455 N NE  . ARG B 2 426  ? 192.763 211.616 157.834 1.00 8.31  ? 426 ARG B NE  1 
ATOM 6456 C CZ  . ARG B 2 426  ? 192.778 212.930 158.019 1.00 7.05  ? 426 ARG B CZ  1 
ATOM 6457 N NH1 . ARG B 2 426  ? 192.789 213.772 156.998 1.00 6.45  ? 426 ARG B NH1 1 
ATOM 6458 N NH2 . ARG B 2 426  ? 192.789 213.411 159.258 1.00 3.65  ? 426 ARG B NH2 1 
ATOM 6459 N N   . ASP B 2 427  ? 191.652 206.230 153.585 1.00 1.28  ? 427 ASP B N   1 
ATOM 6460 C CA  . ASP B 2 427  ? 191.316 205.691 152.266 1.00 1.67  ? 427 ASP B CA  1 
ATOM 6461 C C   . ASP B 2 427  ? 192.341 204.655 151.812 1.00 1.20  ? 427 ASP B C   1 
ATOM 6462 O O   . ASP B 2 427  ? 192.715 204.590 150.639 1.00 0.00  ? 427 ASP B O   1 
ATOM 6463 C CB  . ASP B 2 427  ? 191.177 206.809 151.231 1.00 3.35  ? 427 ASP B CB  1 
ATOM 6464 C CG  . ASP B 2 427  ? 190.574 208.070 151.812 1.00 7.74  ? 427 ASP B CG  1 
ATOM 6465 O OD1 . ASP B 2 427  ? 189.506 207.977 152.450 1.00 12.96 ? 427 ASP B OD1 1 
ATOM 6466 O OD2 . ASP B 2 427  ? 191.166 209.153 151.628 1.00 6.05  ? 427 ASP B OD2 1 
ATOM 6467 N N   . ALA B 2 428  ? 192.718 203.807 152.757 1.00 3.12  ? 428 ALA B N   1 
ATOM 6468 C CA  . ALA B 2 428  ? 193.711 202.780 152.412 1.00 0.00  ? 428 ALA B CA  1 
ATOM 6469 C C   . ALA B 2 428  ? 193.042 201.605 151.728 1.00 0.00  ? 428 ALA B C   1 
ATOM 6470 O O   . ALA B 2 428  ? 191.806 201.463 151.804 1.00 0.00  ? 428 ALA B O   1 
ATOM 6471 C CB  . ALA B 2 428  ? 194.439 202.339 153.660 1.00 0.00  ? 428 ALA B CB  1 
ATOM 6472 N N   . GLN B 2 429  ? 193.873 200.801 151.097 1.00 0.00  ? 429 GLN B N   1 
ATOM 6473 C CA  . GLN B 2 429  ? 193.377 199.631 150.387 1.00 0.00  ? 429 GLN B CA  1 
ATOM 6474 C C   . GLN B 2 429  ? 194.132 198.395 150.852 1.00 0.20  ? 429 GLN B C   1 
ATOM 6475 O O   . GLN B 2 429  ? 195.351 198.435 151.025 1.00 8.18  ? 429 GLN B O   1 
ATOM 6476 C CB  . GLN B 2 429  ? 193.526 199.824 148.880 1.00 0.00  ? 429 GLN B CB  1 
ATOM 6477 C CG  . GLN B 2 429  ? 192.678 200.965 148.353 1.00 0.00  ? 429 GLN B CG  1 
ATOM 6478 C CD  . GLN B 2 429  ? 193.035 201.357 146.944 1.00 0.00  ? 429 GLN B CD  1 
ATOM 6479 O OE1 . GLN B 2 429  ? 194.169 201.181 146.511 1.00 0.00  ? 429 GLN B OE1 1 
ATOM 6480 N NE2 . GLN B 2 429  ? 192.070 201.904 146.220 1.00 0.00  ? 429 GLN B NE2 1 
ATOM 6481 N N   . ILE B 2 430  ? 193.413 197.299 151.057 1.00 4.18  ? 430 ILE B N   1 
ATOM 6482 C CA  . ILE B 2 430  ? 193.967 196.127 151.726 1.00 0.00  ? 430 ILE B CA  1 
ATOM 6483 C C   . ILE B 2 430  ? 194.146 195.003 150.713 1.00 0.00  ? 430 ILE B C   1 
ATOM 6484 O O   . ILE B 2 430  ? 193.422 194.912 149.716 1.00 9.64  ? 430 ILE B O   1 
ATOM 6485 C CB  . ILE B 2 430  ? 193.065 195.685 152.900 1.00 0.00  ? 430 ILE B CB  1 
ATOM 6486 C CG1 . ILE B 2 430  ? 192.788 196.855 153.844 1.00 0.00  ? 430 ILE B CG1 1 
ATOM 6487 C CG2 . ILE B 2 430  ? 193.704 194.561 153.691 1.00 0.32  ? 430 ILE B CG2 1 
ATOM 6488 C CD1 . ILE B 2 430  ? 194.019 197.615 154.256 1.00 0.00  ? 430 ILE B CD1 1 
ATOM 6489 N N   . GLY B 2 431  ? 195.142 194.153 150.969 1.00 0.00  ? 431 GLY B N   1 
ATOM 6490 C CA  . GLY B 2 431  ? 195.378 192.965 150.175 1.00 0.00  ? 431 GLY B CA  1 
ATOM 6491 C C   . GLY B 2 431  ? 196.126 191.952 151.014 1.00 0.00  ? 431 GLY B C   1 
ATOM 6492 O O   . GLY B 2 431  ? 196.636 192.267 152.088 1.00 1.17  ? 431 GLY B O   1 
ATOM 6493 N N   . TRP B 2 432  ? 196.140 190.709 150.516 1.00 0.00  ? 432 TRP B N   1 
ATOM 6494 C CA  . TRP B 2 432  ? 196.776 189.600 151.266 1.00 0.00  ? 432 TRP B CA  1 
ATOM 6495 C C   . TRP B 2 432  ? 197.661 188.766 150.343 1.00 3.03  ? 432 TRP B C   1 
ATOM 6496 O O   . TRP B 2 432  ? 197.268 188.550 149.175 1.00 0.00  ? 432 TRP B O   1 
ATOM 6497 C CB  . TRP B 2 432  ? 195.696 188.707 151.891 1.00 5.82  ? 432 TRP B CB  1 
ATOM 6498 C CG  . TRP B 2 432  ? 194.995 189.297 153.086 1.00 3.39  ? 432 TRP B CG  1 
ATOM 6499 C CD1 . TRP B 2 432  ? 193.883 190.087 153.082 1.00 2.44  ? 432 TRP B CD1 1 
ATOM 6500 C CD2 . TRP B 2 432  ? 195.354 189.116 154.473 1.00 0.09  ? 432 TRP B CD2 1 
ATOM 6501 N NE1 . TRP B 2 432  ? 193.530 190.418 154.363 1.00 3.85  ? 432 TRP B NE1 1 
ATOM 6502 C CE2 . TRP B 2 432  ? 194.411 189.837 155.237 1.00 0.65  ? 432 TRP B CE2 1 
ATOM 6503 C CE3 . TRP B 2 432  ? 196.373 188.423 155.136 1.00 0.00  ? 432 TRP B CE3 1 
ATOM 6504 C CZ2 . TRP B 2 432  ? 194.461 189.880 156.628 1.00 3.18  ? 432 TRP B CZ2 1 
ATOM 6505 C CZ3 . TRP B 2 432  ? 196.421 188.468 156.512 1.00 3.21  ? 432 TRP B CZ3 1 
ATOM 6506 C CH2 . TRP B 2 432  ? 195.477 189.186 157.245 1.00 5.88  ? 432 TRP B CH2 1 
ATOM 6507 N N   . ILE B 2 433  ? 198.806 188.306 150.846 1.00 0.00  ? 433 ILE B N   1 
ATOM 6508 C CA  . ILE B 2 433  ? 199.716 187.443 150.101 1.00 0.00  ? 433 ILE B CA  1 
ATOM 6509 C C   . ILE B 2 433  ? 200.092 186.257 150.976 1.00 5.76  ? 433 ILE B C   1 
ATOM 6510 O O   . ILE B 2 433  ? 200.608 186.437 152.082 1.00 0.97  ? 433 ILE B O   1 
ATOM 6511 C CB  . ILE B 2 433  ? 200.982 188.198 149.654 1.00 1.13  ? 433 ILE B CB  1 
ATOM 6512 C CG1 . ILE B 2 433  ? 200.630 189.280 148.634 1.00 2.72  ? 433 ILE B CG1 1 
ATOM 6513 C CG2 . ILE B 2 433  ? 202.006 187.234 149.088 1.00 0.00  ? 433 ILE B CG2 1 
ATOM 6514 C CD1 . ILE B 2 433  ? 201.763 190.231 148.356 1.00 1.30  ? 433 ILE B CD1 1 
ATOM 6515 N N   . GLN B 2 434  ? 199.860 185.049 150.475 1.00 0.31  ? 434 GLN B N   1 
ATOM 6516 C CA  . GLN B 2 434  ? 200.188 183.828 151.199 1.00 0.00  ? 434 GLN B CA  1 
ATOM 6517 C C   . GLN B 2 434  ? 201.411 183.174 150.572 1.00 0.00  ? 434 GLN B C   1 
ATOM 6518 O O   . GLN B 2 434  ? 201.456 182.978 149.353 1.00 9.45  ? 434 GLN B O   1 
ATOM 6519 C CB  . GLN B 2 434  ? 199.008 182.857 151.193 1.00 0.48  ? 434 GLN B CB  1 
ATOM 6520 C CG  . GLN B 2 434  ? 199.382 181.430 151.539 1.00 0.00  ? 434 GLN B CG  1 
ATOM 6521 C CD  . GLN B 2 434  ? 198.190 180.501 151.518 1.00 2.34  ? 434 GLN B CD  1 
ATOM 6522 O OE1 . GLN B 2 434  ? 197.077 180.894 151.864 1.00 0.00  ? 434 GLN B OE1 1 
ATOM 6523 N NE2 . GLN B 2 434  ? 198.414 179.262 151.105 1.00 10.47 ? 434 GLN B NE2 1 
ATOM 6524 N N   . THR B 2 435  ? 202.396 182.834 151.400 1.00 0.99  ? 435 THR B N   1 
ATOM 6525 C CA  . THR B 2 435  ? 203.653 182.267 150.936 1.00 0.00  ? 435 THR B CA  1 
ATOM 6526 C C   . THR B 2 435  ? 203.868 180.918 151.607 1.00 4.49  ? 435 THR B C   1 
ATOM 6527 O O   . THR B 2 435  ? 203.815 180.821 152.837 1.00 12.33 ? 435 THR B O   1 
ATOM 6528 C CB  . THR B 2 435  ? 204.821 183.205 151.248 1.00 1.59  ? 435 THR B CB  1 
ATOM 6529 O OG1 . THR B 2 435  ? 204.480 184.539 150.853 1.00 0.00  ? 435 THR B OG1 1 
ATOM 6530 C CG2 . THR B 2 435  ? 206.055 182.778 150.491 1.00 8.63  ? 435 THR B CG2 1 
ATOM 6531 N N   . VAL B 2 436  ? 204.124 179.887 150.805 1.00 6.30  ? 436 VAL B N   1 
ATOM 6532 C CA  . VAL B 2 436  ? 204.277 178.521 151.297 1.00 5.38  ? 436 VAL B CA  1 
ATOM 6533 C C   . VAL B 2 436  ? 205.758 178.176 151.342 1.00 0.57  ? 436 VAL B C   1 
ATOM 6534 O O   . VAL B 2 436  ? 206.504 178.478 150.402 1.00 0.00  ? 436 VAL B O   1 
ATOM 6535 C CB  . VAL B 2 436  ? 203.507 177.518 150.420 1.00 6.81  ? 436 VAL B CB  1 
ATOM 6536 C CG1 . VAL B 2 436  ? 203.764 176.096 150.887 1.00 9.93  ? 436 VAL B CG1 1 
ATOM 6537 C CG2 . VAL B 2 436  ? 202.021 177.819 150.450 1.00 3.94  ? 436 VAL B CG2 1 
ATOM 6538 N N   . GLU B 2 437  ? 206.186 177.597 152.468 1.00 7.69  ? 437 GLU B N   1 
ATOM 6539 C CA  . GLU B 2 437  ? 207.615 177.228 152.645 1.00 16.03 ? 437 GLU B CA  1 
ATOM 6540 C C   . GLU B 2 437  ? 207.965 176.105 151.665 1.00 21.12 ? 437 GLU B C   1 
ATOM 6541 O O   . GLU B 2 437  ? 207.537 174.959 151.903 1.00 20.76 ? 437 GLU B O   1 
ATOM 6542 C CB  . GLU B 2 437  ? 207.853 176.806 154.095 1.00 13.83 ? 437 GLU B CB  1 
ATOM 6543 C CG  . GLU B 2 437  ? 209.250 176.283 154.366 1.00 13.65 ? 437 GLU B CG  1 
ATOM 6544 C CD  . GLU B 2 437  ? 209.431 175.736 155.771 1.00 19.19 ? 437 GLU B CD  1 
ATOM 6545 O OE1 . GLU B 2 437  ? 208.711 174.783 156.128 1.00 20.80 ? 437 GLU B OE1 1 
ATOM 6546 O OE2 . GLU B 2 437  ? 210.284 176.270 156.507 1.00 19.46 ? 437 GLU B OE2 1 
ATOM 6547 N N   . ASP B 2 438  ? 208.705 176.431 150.602 1.00 33.39 ? 438 ASP B N   1 
ATOM 6548 C CA  . ASP B 2 438  ? 209.117 175.403 149.610 1.00 33.79 ? 438 ASP B CA  1 
ATOM 6549 C C   . ASP B 2 438  ? 209.951 174.337 150.327 1.00 34.27 ? 438 ASP B C   1 
ATOM 6550 O O   . ASP B 2 438  ? 210.938 174.711 150.990 1.00 30.73 ? 438 ASP B O   1 
ATOM 6551 C CB  . ASP B 2 438  ? 209.877 176.035 148.442 1.00 33.61 ? 438 ASP B CB  1 
ATOM 6552 C CG  . ASP B 2 438  ? 210.298 175.024 147.389 1.00 36.61 ? 438 ASP B CG  1 
ATOM 6553 O OD1 . ASP B 2 438  ? 209.402 174.439 146.750 1.00 35.19 ? 438 ASP B OD1 1 
ATOM 6554 O OD2 . ASP B 2 438  ? 211.518 174.835 147.214 1.00 37.57 ? 438 ASP B OD2 1 
ATOM 6555 N N   . LEU B 2 439  ? 209.564 173.065 150.196 1.00 38.82 ? 439 LEU B N   1 
ATOM 6556 C CA  . LEU B 2 439  ? 210.288 171.962 150.884 1.00 37.33 ? 439 LEU B CA  1 
ATOM 6557 C C   . LEU B 2 439  ? 210.590 170.850 149.874 1.00 35.21 ? 439 LEU B C   1 
ATOM 6558 O O   . LEU B 2 439  ? 211.048 171.197 148.767 1.00 35.66 ? 439 LEU B O   1 
ATOM 6559 C CB  . LEU B 2 439  ? 209.421 171.443 152.035 1.00 34.09 ? 439 LEU B CB  1 
ATOM 6560 C CG  . LEU B 2 439  ? 209.994 170.253 152.803 1.00 35.44 ? 439 LEU B CG  1 
ATOM 6561 C CD1 . LEU B 2 439  ? 211.298 170.628 153.489 1.00 34.30 ? 439 LEU B CD1 1 
ATOM 6562 C CD2 . LEU B 2 439  ? 208.990 169.728 153.817 1.00 34.95 ? 439 LEU B CD2 1 
ATOM 6563 N N   . GLY B 2 457  ? 204.700 169.864 159.931 1.00 6.64  ? 457 GLY B N   1 
ATOM 6564 C CA  . GLY B 2 457  ? 203.514 169.948 159.056 1.00 1.36  ? 457 GLY B CA  1 
ATOM 6565 C C   . GLY B 2 457  ? 203.894 169.946 157.586 1.00 9.66  ? 457 GLY B C   1 
ATOM 6566 O O   . GLY B 2 457  ? 205.096 169.803 157.287 1.00 9.90  ? 457 GLY B O   1 
ATOM 6567 N N   . PRO B 2 458  ? 202.932 170.102 156.650 1.00 17.60 ? 458 PRO B N   1 
ATOM 6568 C CA  . PRO B 2 458  ? 203.231 170.042 155.216 1.00 14.02 ? 458 PRO B CA  1 
ATOM 6569 C C   . PRO B 2 458  ? 204.233 171.136 154.824 1.00 12.11 ? 458 PRO B C   1 
ATOM 6570 O O   . PRO B 2 458  ? 205.182 170.825 154.128 1.00 11.49 ? 458 PRO B O   1 
ATOM 6571 C CB  . PRO B 2 458  ? 201.872 170.296 154.544 1.00 7.01  ? 458 PRO B CB  1 
ATOM 6572 C CG  . PRO B 2 458  ? 201.032 170.957 155.618 1.00 7.05  ? 458 PRO B CG  1 
ATOM 6573 C CD  . PRO B 2 458  ? 201.516 170.354 156.919 1.00 7.19  ? 458 PRO B CD  1 
ATOM 6574 N N   . SER B 2 459  ? 204.007 172.369 155.288 1.00 14.47 ? 459 SER B N   1 
ATOM 6575 C CA  . SER B 2 459  ? 204.921 173.501 154.985 1.00 13.92 ? 459 SER B CA  1 
ATOM 6576 C C   . SER B 2 459  ? 204.568 174.681 155.895 1.00 10.51 ? 459 SER B C   1 
ATOM 6577 O O   . SER B 2 459  ? 203.368 174.868 156.173 1.00 20.41 ? 459 SER B O   1 
ATOM 6578 C CB  . SER B 2 459  ? 204.843 173.892 153.534 1.00 15.52 ? 459 SER B CB  1 
ATOM 6579 O OG  . SER B 2 459  ? 205.315 172.841 152.703 1.00 15.52 ? 459 SER B OG  1 
ATOM 6580 N N   . ARG B 2 460  ? 205.572 175.439 156.343 1.00 1.65  ? 460 ARG B N   1 
ATOM 6581 C CA  . ARG B 2 460  ? 205.298 176.538 157.265 1.00 2.11  ? 460 ARG B CA  1 
ATOM 6582 C C   . ARG B 2 460  ? 204.782 177.726 156.464 1.00 4.22  ? 460 ARG B C   1 
ATOM 6583 O O   . ARG B 2 460  ? 205.500 178.692 156.208 1.00 8.63  ? 460 ARG B O   1 
ATOM 6584 C CB  . ARG B 2 460  ? 206.546 176.894 158.058 1.00 7.39  ? 460 ARG B CB  1 
ATOM 6585 C CG  . ARG B 2 460  ? 206.962 175.836 159.062 1.00 7.93  ? 460 ARG B CG  1 
ATOM 6586 C CD  . ARG B 2 460  ? 207.788 176.453 160.171 1.00 5.19  ? 460 ARG B CD  1 
ATOM 6587 N NE  . ARG B 2 460  ? 209.055 176.961 159.660 1.00 8.80  ? 460 ARG B NE  1 
ATOM 6588 C CZ  . ARG B 2 460  ? 210.167 177.059 160.374 1.00 10.75 ? 460 ARG B CZ  1 
ATOM 6589 N NH1 . ARG B 2 460  ? 210.205 176.698 161.646 1.00 8.71  ? 460 ARG B NH1 1 
ATOM 6590 N NH2 . ARG B 2 460  ? 211.268 177.531 159.797 1.00 5.98  ? 460 ARG B NH2 1 
ATOM 6591 N N   . VAL B 2 461  ? 203.510 177.656 156.067 1.00 0.44  ? 461 VAL B N   1 
ATOM 6592 C CA  . VAL B 2 461  ? 202.898 178.753 155.329 1.00 0.00  ? 461 VAL B CA  1 
ATOM 6593 C C   . VAL B 2 461  ? 202.914 180.014 156.185 1.00 1.54  ? 461 VAL B C   1 
ATOM 6594 O O   . VAL B 2 461  ? 203.050 179.961 157.414 1.00 6.84  ? 461 VAL B O   1 
ATOM 6595 C CB  . VAL B 2 461  ? 201.465 178.390 154.901 1.00 6.23  ? 461 VAL B CB  1 
ATOM 6596 C CG1 . VAL B 2 461  ? 201.426 176.994 154.307 1.00 7.00  ? 461 VAL B CG1 1 
ATOM 6597 C CG2 . VAL B 2 461  ? 200.516 178.488 156.081 1.00 1.90  ? 461 VAL B CG2 1 
ATOM 6598 N N   . ALA B 2 462  ? 202.792 181.165 155.531 1.00 0.00  ? 462 ALA B N   1 
ATOM 6599 C CA  . ALA B 2 462  ? 202.822 182.444 156.229 1.00 0.00  ? 462 ALA B CA  1 
ATOM 6600 C C   . ALA B 2 462  ? 202.039 183.464 155.422 1.00 4.94  ? 462 ALA B C   1 
ATOM 6601 O O   . ALA B 2 462  ? 202.197 183.544 154.201 1.00 17.72 ? 462 ALA B O   1 
ATOM 6602 C CB  . ALA B 2 462  ? 204.260 182.920 156.447 1.00 1.99  ? 462 ALA B CB  1 
ATOM 6603 N N   . GLN B 2 463  ? 201.208 184.246 156.096 1.00 0.00  ? 463 GLN B N   1 
ATOM 6604 C CA  . GLN B 2 463  ? 200.429 185.277 155.432 1.00 0.00  ? 463 GLN B CA  1 
ATOM 6605 C C   . GLN B 2 463  ? 201.030 186.649 155.699 1.00 0.00  ? 463 GLN B C   1 
ATOM 6606 O O   . GLN B 2 463  ? 201.634 186.893 156.745 1.00 2.54  ? 463 GLN B O   1 
ATOM 6607 C CB  . GLN B 2 463  ? 198.970 185.238 155.885 1.00 0.00  ? 463 GLN B CB  1 
ATOM 6608 C CG  . GLN B 2 463  ? 198.159 184.171 155.176 1.00 0.00  ? 463 GLN B CG  1 
ATOM 6609 C CD  . GLN B 2 463  ? 197.370 183.310 156.130 1.00 0.56  ? 463 GLN B CD  1 
ATOM 6610 O OE1 . GLN B 2 463  ? 197.081 183.715 157.252 1.00 4.30  ? 463 GLN B OE1 1 
ATOM 6611 N NE2 . GLN B 2 463  ? 197.026 182.106 155.693 1.00 3.35  ? 463 GLN B NE2 1 
ATOM 6612 N N   . PHE B 2 464  ? 200.848 187.560 154.736 1.00 0.00  ? 464 PHE B N   1 
ATOM 6613 C CA  . PHE B 2 464  ? 201.380 188.940 154.881 1.00 4.53  ? 464 PHE B CA  1 
ATOM 6614 C C   . PHE B 2 464  ? 200.297 189.944 154.470 1.00 0.60  ? 464 PHE B C   1 
ATOM 6615 O O   . PHE B 2 464  ? 199.735 189.798 153.367 1.00 0.98  ? 464 PHE B O   1 
ATOM 6616 C CB  . PHE B 2 464  ? 202.635 189.125 154.026 1.00 3.69  ? 464 PHE B CB  1 
ATOM 6617 C CG  . PHE B 2 464  ? 203.730 188.121 154.284 1.00 5.58  ? 464 PHE B CG  1 
ATOM 6618 C CD1 . PHE B 2 464  ? 204.574 188.257 155.374 1.00 1.45  ? 464 PHE B CD1 1 
ATOM 6619 C CD2 . PHE B 2 464  ? 203.916 187.040 153.438 1.00 5.19  ? 464 PHE B CD2 1 
ATOM 6620 C CE1 . PHE B 2 464  ? 205.579 187.333 155.612 1.00 0.03  ? 464 PHE B CE1 1 
ATOM 6621 C CE2 . PHE B 2 464  ? 204.921 186.117 153.677 1.00 1.81  ? 464 PHE B CE2 1 
ATOM 6622 C CZ  . PHE B 2 464  ? 205.751 186.265 154.763 1.00 0.00  ? 464 PHE B CZ  1 
ATOM 6623 N N   . LEU B 2 465  ? 200.019 190.928 155.330 1.00 2.18  ? 465 LEU B N   1 
ATOM 6624 C CA  . LEU B 2 465  ? 198.991 191.958 155.021 1.00 0.00  ? 465 LEU B CA  1 
ATOM 6625 C C   . LEU B 2 465  ? 199.631 193.076 154.190 1.00 0.00  ? 465 LEU B C   1 
ATOM 6626 O O   . LEU B 2 465  ? 200.741 193.503 154.542 1.00 0.00  ? 465 LEU B O   1 
ATOM 6627 C CB  . LEU B 2 465  ? 198.431 192.506 156.337 1.00 0.00  ? 465 LEU B CB  1 
ATOM 6628 C CG  . LEU B 2 465  ? 196.986 192.999 156.287 1.00 0.00  ? 465 LEU B CG  1 
ATOM 6629 C CD1 . LEU B 2 465  ? 196.334 192.895 157.657 1.00 0.00  ? 465 LEU B CD1 1 
ATOM 6630 C CD2 . LEU B 2 465  ? 196.917 194.431 155.780 1.00 0.34  ? 465 LEU B CD2 1 
ATOM 6631 N N   . VAL B 2 466  ? 198.952 193.531 153.134 1.00 1.66  ? 466 VAL B N   1 
ATOM 6632 C CA  . VAL B 2 466  ? 199.474 194.658 152.304 1.00 0.54  ? 466 VAL B CA  1 
ATOM 6633 C C   . VAL B 2 466  ? 198.643 195.910 152.610 1.00 4.99  ? 466 VAL B C   1 
ATOM 6634 O O   . VAL B 2 466  ? 197.401 195.810 152.566 1.00 16.91 ? 466 VAL B O   1 
ATOM 6635 C CB  . VAL B 2 466  ? 199.438 194.314 150.803 1.00 0.00  ? 466 VAL B CB  1 
ATOM 6636 C CG1 . VAL B 2 466  ? 200.350 195.222 149.993 1.00 0.00  ? 466 VAL B CG1 1 
ATOM 6637 C CG2 . VAL B 2 466  ? 199.773 192.852 150.551 1.00 0.00  ? 466 VAL B CG2 1 
ATOM 6638 N N   . ILE B 2 467  ? 199.300 197.039 152.901 1.00 0.00  ? 467 ILE B N   1 
ATOM 6639 C CA  . ILE B 2 467  ? 198.538 198.303 153.135 1.00 0.00  ? 467 ILE B CA  1 
ATOM 6640 C C   . ILE B 2 467  ? 198.987 199.325 152.085 1.00 2.12  ? 467 ILE B C   1 
ATOM 6641 O O   . ILE B 2 467  ? 200.203 199.586 151.999 1.00 14.86 ? 467 ILE B O   1 
ATOM 6642 C CB  . ILE B 2 467  ? 198.761 198.821 154.571 1.00 0.00  ? 467 ILE B CB  1 
ATOM 6643 C CG1 . ILE B 2 467  ? 197.869 198.095 155.581 1.00 0.00  ? 467 ILE B CG1 1 
ATOM 6644 C CG2 . ILE B 2 467  ? 198.573 200.330 154.644 1.00 4.30  ? 467 ILE B CG2 1 
ATOM 6645 C CD1 . ILE B 2 467  ? 197.915 198.682 156.972 1.00 0.00  ? 467 ILE B CD1 1 
ATOM 6646 N N   . TYR B 2 468  ? 198.043 199.866 151.308 1.00 2.51  ? 468 TYR B N   1 
ATOM 6647 C CA  . TYR B 2 468  ? 198.391 200.894 150.289 1.00 0.00  ? 468 TYR B CA  1 
ATOM 6648 C C   . TYR B 2 468  ? 197.816 202.242 150.714 1.00 0.00  ? 468 TYR B C   1 
ATOM 6649 O O   . TYR B 2 468  ? 196.577 202.409 150.677 1.00 5.25  ? 468 TYR B O   1 
ATOM 6650 C CB  . TYR B 2 468  ? 197.881 200.513 148.895 1.00 0.00  ? 468 TYR B CB  1 
ATOM 6651 C CG  . TYR B 2 468  ? 198.057 201.611 147.855 1.00 0.00  ? 468 TYR B CG  1 
ATOM 6652 C CD1 . TYR B 2 468  ? 199.320 201.986 147.413 1.00 3.52  ? 468 TYR B CD1 1 
ATOM 6653 C CD2 . TYR B 2 468  ? 196.962 202.280 147.321 1.00 0.00  ? 468 TYR B CD2 1 
ATOM 6654 C CE1 . TYR B 2 468  ? 199.487 202.988 146.472 1.00 2.23  ? 468 TYR B CE1 1 
ATOM 6655 C CE2 . TYR B 2 468  ? 197.115 203.281 146.377 1.00 0.00  ? 468 TYR B CE2 1 
ATOM 6656 C CZ  . TYR B 2 468  ? 198.382 203.637 145.951 1.00 4.05  ? 468 TYR B CZ  1 
ATOM 6657 O OH  . TYR B 2 468  ? 198.539 204.624 145.022 1.00 6.83  ? 468 TYR B OH  1 
ATOM 6658 N N   . ALA B 2 469  ? 198.685 203.178 151.107 1.00 0.00  ? 469 ALA B N   1 
ATOM 6659 C CA  . ALA B 2 469  ? 198.219 204.541 151.451 1.00 0.00  ? 469 ALA B CA  1 
ATOM 6660 C C   . ALA B 2 469  ? 198.302 205.404 150.190 1.00 2.27  ? 469 ALA B C   1 
ATOM 6661 O O   . ALA B 2 469  ? 199.433 205.713 149.767 1.00 0.30  ? 469 ALA B O   1 
ATOM 6662 C CB  . ALA B 2 469  ? 199.060 205.107 152.568 1.00 8.32  ? 469 ALA B CB  1 
ATOM 6663 N N   . PRO B 2 470  ? 197.173 205.806 149.565 1.00 0.00  ? 470 PRO B N   1 
ATOM 6664 C CA  . PRO B 2 470  ? 197.228 206.542 148.295 1.00 1.32  ? 470 PRO B CA  1 
ATOM 6665 C C   . PRO B 2 470  ? 197.706 207.978 148.426 1.00 12.02 ? 470 PRO B C   1 
ATOM 6666 O O   . PRO B 2 470  ? 198.363 208.492 147.516 1.00 15.86 ? 470 PRO B O   1 
ATOM 6667 C CB  . PRO B 2 470  ? 195.777 206.488 147.804 1.00 4.20  ? 470 PRO B CB  1 
ATOM 6668 C CG  . PRO B 2 470  ? 194.967 206.354 149.036 1.00 1.92  ? 470 PRO B CG  1 
ATOM 6669 C CD  . PRO B 2 470  ? 195.794 205.612 150.042 1.00 0.00  ? 470 PRO B CD  1 
ATOM 6670 N N   . ARG B 2 471  ? 197.371 208.643 149.533 1.00 10.16 ? 471 ARG B N   1 
ATOM 6671 C CA  . ARG B 2 471  ? 197.761 210.040 149.698 1.00 12.84 ? 471 ARG B CA  1 
ATOM 6672 C C   . ARG B 2 471  ? 199.273 210.171 149.816 1.00 10.09 ? 471 ARG B C   1 
ATOM 6673 O O   . ARG B 2 471  ? 199.898 210.976 149.115 1.00 8.84  ? 471 ARG B O   1 
ATOM 6674 C CB  . ARG B 2 471  ? 197.080 210.623 150.931 1.00 7.18  ? 471 ARG B CB  1 
ATOM 6675 C CG  . ARG B 2 471  ? 197.402 212.077 151.175 1.00 2.76  ? 471 ARG B CG  1 
ATOM 6676 C CD  . ARG B 2 471  ? 196.608 212.525 152.369 1.00 9.02  ? 471 ARG B CD  1 
ATOM 6677 N NE  . ARG B 2 471  ? 197.057 211.806 153.556 1.00 5.18  ? 471 ARG B NE  1 
ATOM 6678 C CZ  . ARG B 2 471  ? 198.104 212.149 154.283 1.00 3.85  ? 471 ARG B CZ  1 
ATOM 6679 N NH1 . ARG B 2 471  ? 198.871 213.141 153.928 1.00 4.89  ? 471 ARG B NH1 1 
ATOM 6680 N NH2 . ARG B 2 471  ? 198.422 211.428 155.353 1.00 1.58  ? 471 ARG B NH2 1 
ATOM 6681 N N   . ARG B 2 472  ? 199.878 209.380 150.704 1.00 4.40  ? 472 ARG B N   1 
ATOM 6682 C CA  . ARG B 2 472  ? 201.328 209.324 150.796 1.00 7.59  ? 472 ARG B CA  1 
ATOM 6683 C C   . ARG B 2 472  ? 201.941 208.571 149.625 1.00 7.35  ? 472 ARG B C   1 
ATOM 6684 O O   . ARG B 2 472  ? 203.150 208.680 149.398 1.00 12.05 ? 472 ARG B O   1 
ATOM 6685 C CB  . ARG B 2 472  ? 201.744 208.664 152.111 1.00 3.53  ? 472 ARG B CB  1 
ATOM 6686 C CG  . ARG B 2 472  ? 201.152 209.304 153.356 1.00 2.73  ? 472 ARG B CG  1 
ATOM 6687 C CD  . ARG B 2 472  ? 201.011 208.283 154.474 1.00 4.15  ? 472 ARG B CD  1 
ATOM 6688 N NE  . ARG B 2 472  ? 202.292 207.990 155.104 1.00 11.67 ? 472 ARG B NE  1 
ATOM 6689 C CZ  . ARG B 2 472  ? 202.515 206.961 155.910 1.00 8.34  ? 472 ARG B CZ  1 
ATOM 6690 N NH1 . ARG B 2 472  ? 201.558 206.099 156.211 1.00 6.36  ? 472 ARG B NH1 1 
ATOM 6691 N NH2 . ARG B 2 472  ? 203.729 206.791 156.426 1.00 3.58  ? 472 ARG B NH2 1 
ATOM 6692 N N   . GLY B 2 473  ? 201.135 207.822 148.877 1.00 3.68  ? 473 GLY B N   1 
ATOM 6693 C CA  . GLY B 2 473  ? 201.635 207.065 147.748 1.00 7.43  ? 473 GLY B CA  1 
ATOM 6694 C C   . GLY B 2 473  ? 202.601 205.968 148.138 1.00 12.86 ? 473 GLY B C   1 
ATOM 6695 O O   . GLY B 2 473  ? 203.672 205.841 147.537 1.00 15.64 ? 473 GLY B O   1 
ATOM 6696 N N   . ILE B 2 474  ? 202.218 205.200 149.161 1.00 7.11  ? 474 ILE B N   1 
ATOM 6697 C CA  . ILE B 2 474  ? 203.144 204.154 149.682 1.00 2.76  ? 474 ILE B CA  1 
ATOM 6698 C C   . ILE B 2 474  ? 202.444 202.794 149.713 1.00 4.67  ? 474 ILE B C   1 
ATOM 6699 O O   . ILE B 2 474  ? 201.203 202.764 149.842 1.00 6.66  ? 474 ILE B O   1 
ATOM 6700 C CB  . ILE B 2 474  ? 203.689 204.557 151.069 1.00 5.85  ? 474 ILE B CB  1 
ATOM 6701 C CG1 . ILE B 2 474  ? 204.583 205.797 150.987 1.00 9.55  ? 474 ILE B CG1 1 
ATOM 6702 C CG2 . ILE B 2 474  ? 204.400 203.393 151.742 1.00 3.63  ? 474 ILE B CG2 1 
ATOM 6703 C CD1 . ILE B 2 474  ? 204.930 206.390 152.333 1.00 7.22  ? 474 ILE B CD1 1 
ATOM 6704 N N   . LEU B 2 475  ? 203.216 201.720 149.571 1.00 2.78  ? 475 LEU B N   1 
ATOM 6705 C CA  . LEU B 2 475  ? 202.706 200.355 149.624 1.00 2.93  ? 475 LEU B CA  1 
ATOM 6706 C C   . LEU B 2 475  ? 203.488 199.604 150.688 1.00 1.30  ? 475 LEU B C   1 
ATOM 6707 O O   . LEU B 2 475  ? 204.707 199.450 150.569 1.00 3.42  ? 475 LEU B O   1 
ATOM 6708 C CB  . LEU B 2 475  ? 202.833 199.657 148.266 1.00 0.00  ? 475 LEU B CB  1 
ATOM 6709 C CG  . LEU B 2 475  ? 202.221 198.260 148.140 1.00 0.00  ? 475 LEU B CG  1 
ATOM 6710 C CD1 . LEU B 2 475  ? 201.343 198.178 146.910 1.00 0.00  ? 475 LEU B CD1 1 
ATOM 6711 C CD2 . LEU B 2 475  ? 203.298 197.194 148.086 1.00 0.00  ? 475 LEU B CD2 1 
ATOM 6712 N N   . GLU B 2 476  ? 202.793 199.133 151.717 1.00 0.00  ? 476 GLU B N   1 
ATOM 6713 C CA  . GLU B 2 476  ? 203.419 198.527 152.880 1.00 0.00  ? 476 GLU B CA  1 
ATOM 6714 C C   . GLU B 2 476  ? 203.038 197.058 152.970 1.00 1.03  ? 476 GLU B C   1 
ATOM 6715 O O   . GLU B 2 476  ? 201.902 196.685 152.671 1.00 10.68 ? 476 GLU B O   1 
ATOM 6716 C CB  . GLU B 2 476  ? 202.993 199.254 154.155 1.00 1.16  ? 476 GLU B CB  1 
ATOM 6717 C CG  . GLU B 2 476  ? 202.983 200.764 154.018 1.00 6.44  ? 476 GLU B CG  1 
ATOM 6718 C CD  . GLU B 2 476  ? 202.596 201.462 155.303 1.00 5.46  ? 476 GLU B CD  1 
ATOM 6719 O OE1 . GLU B 2 476  ? 202.102 200.782 156.225 1.00 4.88  ? 476 GLU B OE1 1 
ATOM 6720 O OE2 . GLU B 2 476  ? 202.786 202.692 155.391 1.00 3.95  ? 476 GLU B OE2 1 
ATOM 6721 N N   . VAL B 2 477  ? 203.990 196.229 153.411 1.00 0.00  ? 477 VAL B N   1 
ATOM 6722 C CA  . VAL B 2 477  ? 203.715 194.773 153.593 1.00 1.91  ? 477 VAL B CA  1 
ATOM 6723 C C   . VAL B 2 477  ? 203.842 194.445 155.085 1.00 5.96  ? 477 VAL B C   1 
ATOM 6724 O O   . VAL B 2 477  ? 204.983 194.423 155.587 1.00 4.05  ? 477 VAL B O   1 
ATOM 6725 C CB  . VAL B 2 477  ? 204.666 193.906 152.747 1.00 1.64  ? 477 VAL B CB  1 
ATOM 6726 C CG1 . VAL B 2 477  ? 204.348 192.425 152.881 1.00 2.85  ? 477 VAL B CG1 1 
ATOM 6727 C CG2 . VAL B 2 477  ? 204.662 194.326 151.285 1.00 6.70  ? 477 VAL B CG2 1 
ATOM 6728 N N   . TRP B 2 478  ? 202.714 194.212 155.761 1.00 0.00  ? 478 TRP B N   1 
ATOM 6729 C CA  . TRP B 2 478  ? 202.728 193.898 157.213 1.00 0.00  ? 478 TRP B CA  1 
ATOM 6730 C C   . TRP B 2 478  ? 202.664 192.383 157.421 1.00 7.16  ? 478 TRP B C   1 
ATOM 6731 O O   . TRP B 2 478  ? 202.527 191.646 156.420 1.00 15.00 ? 478 TRP B O   1 
ATOM 6732 C CB  . TRP B 2 478  ? 201.561 194.602 157.919 1.00 2.08  ? 478 TRP B CB  1 
ATOM 6733 C CG  . TRP B 2 478  ? 201.673 196.103 157.912 1.00 0.11  ? 478 TRP B CG  1 
ATOM 6734 C CD1 . TRP B 2 478  ? 201.043 196.974 157.072 1.00 0.70  ? 478 TRP B CD1 1 
ATOM 6735 C CD2 . TRP B 2 478  ? 202.480 196.911 158.796 1.00 0.58  ? 478 TRP B CD2 1 
ATOM 6736 N NE1 . TRP B 2 478  ? 201.396 198.262 157.371 1.00 0.00  ? 478 TRP B NE1 1 
ATOM 6737 C CE2 . TRP B 2 478  ? 202.275 198.257 158.421 1.00 2.35  ? 478 TRP B CE2 1 
ATOM 6738 C CE3 . TRP B 2 478  ? 203.347 196.631 159.858 1.00 4.77  ? 478 TRP B CE3 1 
ATOM 6739 C CZ2 . TRP B 2 478  ? 202.907 199.312 159.074 1.00 8.91  ? 478 TRP B CZ2 1 
ATOM 6740 C CZ3 . TRP B 2 478  ? 203.970 197.676 160.501 1.00 5.14  ? 478 TRP B CZ3 1 
ATOM 6741 C CH2 . TRP B 2 478  ? 203.752 198.997 160.112 1.00 3.95  ? 478 TRP B CH2 1 
ATOM 6742 N N   . SER B 2 479  ? 202.782 191.934 158.672 1.00 0.00  ? 479 SER B N   1 
ATOM 6743 C CA  . SER B 2 479  ? 202.696 190.482 158.971 1.00 0.00  ? 479 SER B CA  1 
ATOM 6744 C C   . SER B 2 479  ? 201.225 190.056 159.002 1.00 0.00  ? 479 SER B C   1 
ATOM 6745 O O   . SER B 2 479  ? 200.351 190.945 158.969 1.00 1.80  ? 479 SER B O   1 
ATOM 6746 C CB  . SER B 2 479  ? 203.392 190.156 160.263 1.00 2.45  ? 479 SER B CB  1 
ATOM 6747 O OG  . SER B 2 479  ? 204.752 190.562 160.217 1.00 2.11  ? 479 SER B OG  1 
ATOM 6748 N N   . THR B 2 480  ? 200.963 188.747 159.073 1.00 0.00  ? 480 THR B N   1 
ATOM 6749 C CA  . THR B 2 480  ? 199.563 188.251 159.156 1.00 0.00  ? 480 THR B CA  1 
ATOM 6750 C C   . THR B 2 480  ? 198.884 188.873 160.382 1.00 7.28  ? 480 THR B C   1 
ATOM 6751 O O   . THR B 2 480  ? 197.729 189.317 160.244 1.00 8.27  ? 480 THR B O   1 
ATOM 6752 C CB  . THR B 2 480  ? 199.515 186.717 159.167 1.00 7.81  ? 480 THR B CB  1 
ATOM 6753 O OG1 . THR B 2 480  ? 198.148 186.325 159.297 1.00 12.60 ? 480 THR B OG1 1 
ATOM 6754 C CG2 . THR B 2 480  ? 200.340 186.098 160.274 1.00 13.31 ? 480 THR B CG2 1 
ATOM 6755 N N   . GLN B 2 481  ? 199.574 188.903 161.527 1.00 13.46 ? 481 GLN B N   1 
ATOM 6756 C CA  . GLN B 2 481  ? 199.021 189.534 162.754 1.00 14.61 ? 481 GLN B CA  1 
ATOM 6757 C C   . GLN B 2 481  ? 200.053 190.515 163.319 1.00 8.82  ? 481 GLN B C   1 
ATOM 6758 O O   . GLN B 2 481  ? 199.874 191.734 163.127 1.00 16.04 ? 481 GLN B O   1 
ATOM 6759 C CB  . GLN B 2 481  ? 198.676 188.466 163.793 1.00 6.84  ? 481 GLN B CB  1 
ATOM 6760 C CG  . GLN B 2 481  ? 197.459 187.629 163.429 1.00 0.74  ? 481 GLN B CG  1 
ATOM 6761 C CD  . GLN B 2 481  ? 197.020 186.743 164.568 1.00 3.68  ? 481 GLN B CD  1 
ATOM 6762 O OE1 . GLN B 2 481  ? 197.239 187.049 165.738 1.00 4.07  ? 481 GLN B OE1 1 
ATOM 6763 N NE2 . GLN B 2 481  ? 196.391 185.629 164.230 1.00 6.10  ? 481 GLN B NE2 1 
ATOM 6764 N N   . GLN B 2 482  ? 201.090 189.996 163.985 1.00 0.00  ? 482 GLN B N   1 
ATOM 6765 C CA  . GLN B 2 482  ? 202.127 190.867 164.601 1.00 2.20  ? 482 GLN B CA  1 
ATOM 6766 C C   . GLN B 2 482  ? 203.481 190.591 163.940 1.00 1.41  ? 482 GLN B C   1 
ATOM 6767 O O   . GLN B 2 482  ? 203.667 189.469 163.430 1.00 5.18  ? 482 GLN B O   1 
ATOM 6768 C CB  . GLN B 2 482  ? 202.186 190.632 166.112 1.00 15.17 ? 482 GLN B CB  1 
ATOM 6769 C CG  . GLN B 2 482  ? 201.152 191.431 166.893 1.00 18.31 ? 482 GLN B CG  1 
ATOM 6770 C CD  . GLN B 2 482  ? 199.770 190.834 166.792 1.00 13.66 ? 482 GLN B CD  1 
ATOM 6771 O OE1 . GLN B 2 482  ? 198.794 191.522 166.498 1.00 13.34 ? 482 GLN B OE1 1 
ATOM 6772 N NE2 . GLN B 2 482  ? 199.676 189.539 167.042 1.00 7.15  ? 482 GLN B NE2 1 
ATOM 6773 N N   . GLY B 2 483  ? 204.390 191.571 163.961 1.00 2.00  ? 483 GLY B N   1 
ATOM 6774 C CA  . GLY B 2 483  ? 205.708 191.421 163.310 1.00 2.85  ? 483 GLY B CA  1 
ATOM 6775 C C   . GLY B 2 483  ? 206.110 192.718 162.630 1.00 8.44  ? 483 GLY B C   1 
ATOM 6776 O O   . GLY B 2 483  ? 205.214 193.562 162.422 1.00 8.60  ? 483 GLY B O   1 
ATOM 6777 N N   . PRO B 2 484  ? 207.393 192.947 162.265 1.00 10.05 ? 484 PRO B N   1 
ATOM 6778 C CA  . PRO B 2 484  ? 207.795 194.239 161.701 1.00 0.00  ? 484 PRO B CA  1 
ATOM 6779 C C   . PRO B 2 484  ? 207.275 194.416 160.283 1.00 0.87  ? 484 PRO B C   1 
ATOM 6780 O O   . PRO B 2 484  ? 206.822 193.476 159.627 1.00 4.20  ? 484 PRO B O   1 
ATOM 6781 C CB  . PRO B 2 484  ? 209.323 194.174 161.731 1.00 0.08  ? 484 PRO B CB  1 
ATOM 6782 C CG  . PRO B 2 484  ? 209.626 192.725 161.623 1.00 1.09  ? 484 PRO B CG  1 
ATOM 6783 C CD  . PRO B 2 484  ? 208.520 192.004 162.346 1.00 3.61  ? 484 PRO B CD  1 
ATOM 6784 N N   . ARG B 2 485  ? 207.341 195.661 159.816 1.00 11.61 ? 485 ARG B N   1 
ATOM 6785 C CA  . ARG B 2 485  ? 206.966 195.986 158.444 1.00 6.67  ? 485 ARG B CA  1 
ATOM 6786 C C   . ARG B 2 485  ? 207.945 195.317 157.492 1.00 0.00  ? 485 ARG B C   1 
ATOM 6787 O O   . ARG B 2 485  ? 209.094 195.751 157.363 1.00 2.68  ? 485 ARG B O   1 
ATOM 6788 C CB  . ARG B 2 485  ? 206.957 197.496 158.242 1.00 1.22  ? 485 ARG B CB  1 
ATOM 6789 C CG  . ARG B 2 485  ? 206.223 197.948 157.002 1.00 0.00  ? 485 ARG B CG  1 
ATOM 6790 C CD  . ARG B 2 485  ? 206.229 199.456 156.904 1.00 0.00  ? 485 ARG B CD  1 
ATOM 6791 N NE  . ARG B 2 485  ? 207.592 199.967 156.834 1.00 5.70  ? 485 ARG B NE  1 
ATOM 6792 C CZ  . ARG B 2 485  ? 207.909 201.218 156.534 1.00 6.06  ? 485 ARG B CZ  1 
ATOM 6793 N NH1 . ARG B 2 485  ? 206.980 202.119 156.262 1.00 4.84  ? 485 ARG B NH1 1 
ATOM 6794 N NH2 . ARG B 2 485  ? 209.190 201.572 156.501 1.00 2.23  ? 485 ARG B NH2 1 
ATOM 6795 N N   . VAL B 2 486  ? 207.488 194.260 156.820 1.00 8.12  ? 486 VAL B N   1 
ATOM 6796 C CA  . VAL B 2 486  ? 208.378 193.463 155.983 1.00 4.91  ? 486 VAL B CA  1 
ATOM 6797 C C   . VAL B 2 486  ? 208.891 194.281 154.805 1.00 8.59  ? 486 VAL B C   1 
ATOM 6798 O O   . VAL B 2 486  ? 210.061 194.169 154.417 1.00 7.64  ? 486 VAL B O   1 
ATOM 6799 C CB  . VAL B 2 486  ? 207.663 192.184 155.517 1.00 6.22  ? 486 VAL B CB  1 
ATOM 6800 C CG1 . VAL B 2 486  ? 208.474 191.508 154.451 1.00 5.23  ? 486 VAL B CG1 1 
ATOM 6801 C CG2 . VAL B 2 486  ? 207.445 191.246 156.691 1.00 6.02  ? 486 VAL B CG2 1 
ATOM 6802 N N   . GLY B 2 487  ? 208.034 195.108 154.215 1.00 5.21  ? 487 GLY B N   1 
ATOM 6803 C CA  . GLY B 2 487  ? 208.465 195.882 153.063 1.00 1.78  ? 487 GLY B CA  1 
ATOM 6804 C C   . GLY B 2 487  ? 207.724 197.191 152.936 1.00 7.08  ? 487 GLY B C   1 
ATOM 6805 O O   . GLY B 2 487  ? 206.608 197.345 153.435 1.00 17.79 ? 487 GLY B O   1 
ATOM 6806 N N   . ALA B 2 488  ? 208.354 198.138 152.247 1.00 3.77  ? 488 ALA B N   1 
ATOM 6807 C CA  . ALA B 2 488  ? 207.730 199.434 151.999 1.00 0.70  ? 488 ALA B CA  1 
ATOM 6808 C C   . ALA B 2 488  ? 208.264 199.993 150.691 1.00 8.41  ? 488 ALA B C   1 
ATOM 6809 O O   . ALA B 2 488  ? 209.464 200.258 150.573 1.00 13.48 ? 488 ALA B O   1 
ATOM 6810 C CB  . ALA B 2 488  ? 207.994 200.406 153.147 1.00 0.00  ? 488 ALA B CB  1 
ATOM 6811 N N   . PHE B 2 489  ? 207.372 200.182 149.723 1.00 10.89 ? 489 PHE B N   1 
ATOM 6812 C CA  . PHE B 2 489  ? 207.734 200.646 148.394 1.00 9.82  ? 489 PHE B CA  1 
ATOM 6813 C C   . PHE B 2 489  ? 207.017 201.952 148.089 1.00 10.64 ? 489 PHE B C   1 
ATOM 6814 O O   . PHE B 2 489  ? 205.880 202.172 148.517 1.00 6.86  ? 489 PHE B O   1 
ATOM 6815 C CB  . PHE B 2 489  ? 207.385 199.600 147.326 1.00 2.34  ? 489 PHE B CB  1 
ATOM 6816 C CG  . PHE B 2 489  ? 208.190 198.338 147.431 1.00 7.38  ? 489 PHE B CG  1 
ATOM 6817 C CD1 . PHE B 2 489  ? 207.859 197.366 148.358 1.00 10.95 ? 489 PHE B CD1 1 
ATOM 6818 C CD2 . PHE B 2 489  ? 209.282 198.127 146.609 1.00 9.33  ? 489 PHE B CD2 1 
ATOM 6819 C CE1 . PHE B 2 489  ? 208.598 196.206 148.460 1.00 8.48  ? 489 PHE B CE1 1 
ATOM 6820 C CE2 . PHE B 2 489  ? 210.024 196.969 146.707 1.00 12.17 ? 489 PHE B CE2 1 
ATOM 6821 C CZ  . PHE B 2 489  ? 209.681 196.008 147.634 1.00 11.28 ? 489 PHE B CZ  1 
ATOM 6822 N N   . ASN B 2 490  ? 207.696 202.825 147.353 1.00 11.68 ? 490 ASN B N   1 
ATOM 6823 C CA  . ASN B 2 490  ? 207.128 204.098 146.934 1.00 10.79 ? 490 ASN B CA  1 
ATOM 6824 C C   . ASN B 2 490  ? 206.641 203.974 145.497 1.00 13.99 ? 490 ASN B C   1 
ATOM 6825 O O   . ASN B 2 490  ? 207.449 203.886 144.566 1.00 13.61 ? 490 ASN B O   1 
ATOM 6826 C CB  . ASN B 2 490  ? 208.148 205.228 147.059 1.00 13.64 ? 490 ASN B CB  1 
ATOM 6827 C CG  . ASN B 2 490  ? 207.493 206.589 147.175 1.00 16.89 ? 490 ASN B CG  1 
ATOM 6828 O OD1 . ASN B 2 490  ? 206.303 206.741 146.900 1.00 11.87 ? 490 ASN B OD1 1 
ATOM 6829 N ND2 . ASN B 2 490  ? 208.265 207.586 147.590 1.00 18.36 ? 490 ASN B ND2 1 
ATOM 6830 N N   . VAL B 2 491  ? 205.323 203.975 145.323 1.00 10.39 ? 491 VAL B N   1 
ATOM 6831 C CA  . VAL B 2 491  ? 204.705 203.917 144.006 1.00 4.72  ? 491 VAL B CA  1 
ATOM 6832 C C   . VAL B 2 491  ? 203.929 205.211 143.820 1.00 13.55 ? 491 VAL B C   1 
ATOM 6833 O O   . VAL B 2 491  ? 203.971 206.095 144.682 1.00 16.39 ? 491 VAL B O   1 
ATOM 6834 C CB  . VAL B 2 491  ? 203.794 202.685 143.859 1.00 3.60  ? 491 VAL B CB  1 
ATOM 6835 C CG1 . VAL B 2 491  ? 204.618 201.413 143.901 1.00 4.34  ? 491 VAL B CG1 1 
ATOM 6836 C CG2 . VAL B 2 491  ? 202.747 202.675 144.951 1.00 3.21  ? 491 VAL B CG2 1 
ATOM 6837 N N   . GLY B 2 492  ? 203.237 205.347 142.695 1.00 17.84 ? 492 GLY B N   1 
ATOM 6838 C CA  . GLY B 2 492  ? 202.494 206.561 142.441 1.00 20.66 ? 492 GLY B CA  1 
ATOM 6839 C C   . GLY B 2 492  ? 201.362 206.768 143.430 1.00 18.48 ? 492 GLY B C   1 
ATOM 6840 O O   . GLY B 2 492  ? 200.890 205.846 144.094 1.00 19.47 ? 492 GLY B O   1 
ATOM 6841 N N   . LYS B 2 493  ? 200.930 208.023 143.538 1.00 11.67 ? 493 LYS B N   1 
ATOM 6842 C CA  . LYS B 2 493  ? 199.779 208.350 144.367 1.00 15.44 ? 493 LYS B CA  1 
ATOM 6843 C C   . LYS B 2 493  ? 198.457 207.947 143.728 1.00 15.15 ? 493 LYS B C   1 
ATOM 6844 O O   . LYS B 2 493  ? 197.425 207.985 144.406 1.00 18.04 ? 493 LYS B O   1 
ATOM 6845 C CB  . LYS B 2 493  ? 199.758 209.849 144.672 1.00 11.59 ? 493 LYS B CB  1 
ATOM 6846 C CG  . LYS B 2 493  ? 200.958 210.338 145.458 1.00 12.93 ? 493 LYS B CG  1 
ATOM 6847 C CD  . LYS B 2 493  ? 200.864 211.825 145.751 1.00 15.58 ? 493 LYS B CD  1 
ATOM 6848 C CE  . LYS B 2 493  ? 202.077 212.301 146.535 1.00 15.90 ? 493 LYS B CE  1 
ATOM 6849 N NZ  . LYS B 2 493  ? 202.013 213.754 146.845 1.00 14.11 ? 493 LYS B NZ  1 
ATOM 6850 N N   . HIS B 2 494  ? 198.463 207.560 142.451 1.00 5.59  ? 494 HIS B N   1 
ATOM 6851 C CA  . HIS B 2 494  ? 197.236 207.303 141.705 1.00 11.35 ? 494 HIS B CA  1 
ATOM 6852 C C   . HIS B 2 494  ? 197.134 205.859 141.226 1.00 17.35 ? 494 HIS B C   1 
ATOM 6853 O O   . HIS B 2 494  ? 196.385 205.575 140.287 1.00 22.46 ? 494 HIS B O   1 
ATOM 6854 C CB  . HIS B 2 494  ? 197.131 208.258 140.515 1.00 16.81 ? 494 HIS B CB  1 
ATOM 6855 C CG  . HIS B 2 494  ? 197.413 209.687 140.857 1.00 18.20 ? 494 HIS B CG  1 
ATOM 6856 N ND1 . HIS B 2 494  ? 198.592 210.315 140.519 1.00 20.92 ? 494 HIS B ND1 1 
ATOM 6857 C CD2 . HIS B 2 494  ? 196.666 210.614 141.503 1.00 17.72 ? 494 HIS B CD2 1 
ATOM 6858 C CE1 . HIS B 2 494  ? 198.561 211.565 140.944 1.00 20.63 ? 494 HIS B CE1 1 
ATOM 6859 N NE2 . HIS B 2 494  ? 197.403 211.772 141.545 1.00 20.87 ? 494 HIS B NE2 1 
ATOM 6860 N N   . CYS B 2 495  ? 197.863 204.940 141.850 1.00 11.63 ? 495 CYS B N   1 
ATOM 6861 C CA  . CYS B 2 495  ? 197.807 203.541 141.457 1.00 3.91  ? 495 CYS B CA  1 
ATOM 6862 C C   . CYS B 2 495  ? 196.494 202.916 141.924 1.00 2.11  ? 495 CYS B C   1 
ATOM 6863 O O   . CYS B 2 495  ? 195.604 203.585 142.455 1.00 11.18 ? 495 CYS B O   1 
ATOM 6864 C CB  . CYS B 2 495  ? 198.997 202.780 142.032 1.00 2.34  ? 495 CYS B CB  1 
ATOM 6865 S SG  . CYS B 2 495  ? 200.528 202.967 141.100 1.00 3.07  ? 495 CYS B SG  1 
ATOM 6866 N N   . ARG B 2 496  ? 196.366 201.611 141.709 1.00 0.00  ? 496 ARG B N   1 
ATOM 6867 C CA  . ARG B 2 496  ? 195.241 200.880 142.274 1.00 0.00  ? 496 ARG B CA  1 
ATOM 6868 C C   . ARG B 2 496  ? 195.680 199.468 142.634 1.00 5.48  ? 496 ARG B C   1 
ATOM 6869 O O   . ARG B 2 496  ? 196.343 198.795 141.840 1.00 6.37  ? 496 ARG B O   1 
ATOM 6870 C CB  . ARG B 2 496  ? 194.053 200.836 141.309 1.00 0.00  ? 496 ARG B CB  1 
ATOM 6871 C CG  . ARG B 2 496  ? 193.055 201.955 141.499 1.00 0.00  ? 496 ARG B CG  1 
ATOM 6872 C CD  . ARG B 2 496  ? 192.145 201.677 142.675 1.00 3.53  ? 496 ARG B CD  1 
ATOM 6873 N NE  . ARG B 2 496  ? 191.238 200.564 142.423 1.00 0.25  ? 496 ARG B NE  1 
ATOM 6874 C CZ  . ARG B 2 496  ? 190.006 200.692 141.949 1.00 0.00  ? 496 ARG B CZ  1 
ATOM 6875 N NH1 . ARG B 2 496  ? 189.504 201.876 141.640 1.00 0.00  ? 496 ARG B NH1 1 
ATOM 6876 N NH2 . ARG B 2 496  ? 189.258 199.606 141.785 1.00 0.00  ? 496 ARG B NH2 1 
ATOM 6877 N N   . LEU B 2 497  ? 195.291 199.051 143.848 1.00 1.27  ? 497 LEU B N   1 
ATOM 6878 C CA  . LEU B 2 497  ? 195.623 197.689 144.341 1.00 0.00  ? 497 LEU B CA  1 
ATOM 6879 C C   . LEU B 2 497  ? 194.402 196.786 144.159 1.00 6.00  ? 497 LEU B C   1 
ATOM 6880 O O   . LEU B 2 497  ? 193.380 197.037 144.826 1.00 6.30  ? 497 LEU B O   1 
ATOM 6881 C CB  . LEU B 2 497  ? 196.027 197.773 145.817 1.00 0.00  ? 497 LEU B CB  1 
ATOM 6882 C CG  . LEU B 2 497  ? 197.036 196.725 146.286 1.00 0.00  ? 497 LEU B CG  1 
ATOM 6883 C CD1 . LEU B 2 497  ? 197.678 197.143 147.600 1.00 0.00  ? 497 LEU B CD1 1 
ATOM 6884 C CD2 . LEU B 2 497  ? 196.382 195.359 146.429 1.00 3.38  ? 497 LEU B CD2 1 
ATOM 6885 N N   . LEU B 2 498  ? 194.509 195.782 143.294 1.00 9.81  ? 498 LEU B N   1 
ATOM 6886 C CA  . LEU B 2 498  ? 193.440 194.834 143.019 1.00 5.62  ? 498 LEU B CA  1 
ATOM 6887 C C   . LEU B 2 498  ? 193.734 193.521 143.728 1.00 6.04  ? 498 LEU B C   1 
ATOM 6888 O O   . LEU B 2 498  ? 194.835 192.971 143.604 1.00 2.85  ? 498 LEU B O   1 
ATOM 6889 C CB  . LEU B 2 498  ? 193.281 194.596 141.515 1.00 0.00  ? 498 LEU B CB  1 
ATOM 6890 C CG  . LEU B 2 498  ? 192.789 195.766 140.663 1.00 0.00  ? 498 LEU B CG  1 
ATOM 6891 C CD1 . LEU B 2 498  ? 192.740 195.362 139.208 1.00 1.28  ? 498 LEU B CD1 1 
ATOM 6892 C CD2 . LEU B 2 498  ? 191.424 196.220 141.128 1.00 0.00  ? 498 LEU B CD2 1 
ATOM 6893 N N   . TYR B 2 499  ? 192.742 193.029 144.465 1.00 5.23  ? 499 TYR B N   1 
ATOM 6894 C CA  . TYR B 2 499  ? 192.832 191.783 145.222 1.00 2.96  ? 499 TYR B CA  1 
ATOM 6895 C C   . TYR B 2 499  ? 191.532 191.025 144.990 1.00 9.78  ? 499 TYR B C   1 
ATOM 6896 O O   . TYR B 2 499  ? 190.515 191.316 145.644 1.00 5.00  ? 499 TYR B O   1 
ATOM 6897 C CB  . TYR B 2 499  ? 193.066 192.071 146.700 1.00 0.18  ? 499 TYR B CB  1 
ATOM 6898 C CG  . TYR B 2 499  ? 192.829 190.914 147.639 1.00 0.00  ? 499 TYR B CG  1 
ATOM 6899 C CD1 . TYR B 2 499  ? 193.702 189.840 147.682 1.00 0.00  ? 499 TYR B CD1 1 
ATOM 6900 C CD2 . TYR B 2 499  ? 191.745 190.911 148.500 1.00 1.24  ? 499 TYR B CD2 1 
ATOM 6901 C CE1 . TYR B 2 499  ? 193.492 188.788 148.546 1.00 2.14  ? 499 TYR B CE1 1 
ATOM 6902 C CE2 . TYR B 2 499  ? 191.526 189.866 149.364 1.00 0.20  ? 499 TYR B CE2 1 
ATOM 6903 C CZ  . TYR B 2 499  ? 192.402 188.807 149.385 1.00 1.55  ? 499 TYR B CZ  1 
ATOM 6904 O OH  . TYR B 2 499  ? 192.186 187.760 150.249 1.00 0.00  ? 499 TYR B OH  1 
ATOM 6905 N N   . PRO B 2 500  ? 191.507 190.075 144.051 1.00 1.57  ? 500 PRO B N   1 
ATOM 6906 C CA  . PRO B 2 500  ? 190.241 189.416 143.702 1.00 2.40  ? 500 PRO B CA  1 
ATOM 6907 C C   . PRO B 2 500  ? 189.691 188.553 144.824 1.00 6.63  ? 500 PRO B C   1 
ATOM 6908 O O   . PRO B 2 500  ? 188.523 188.685 145.204 1.00 0.00  ? 500 PRO B O   1 
ATOM 6909 C CB  . PRO B 2 500  ? 190.609 188.568 142.475 1.00 4.91  ? 500 PRO B CB  1 
ATOM 6910 C CG  . PRO B 2 500  ? 191.921 189.102 141.999 1.00 4.52  ? 500 PRO B CG  1 
ATOM 6911 C CD  . PRO B 2 500  ? 192.621 189.595 143.220 1.00 7.07  ? 500 PRO B CD  1 
ATOM 6912 N N   . GLY B 2 501  ? 190.526 187.670 145.364 1.00 3.75  ? 501 GLY B N   1 
ATOM 6913 C CA  . GLY B 2 501  ? 190.084 186.778 146.414 1.00 5.45  ? 501 GLY B CA  1 
ATOM 6914 C C   . GLY B 2 501  ? 189.391 185.523 145.941 1.00 8.03  ? 501 GLY B C   1 
ATOM 6915 O O   . GLY B 2 501  ? 188.682 184.890 146.729 1.00 7.77  ? 501 GLY B O   1 
ATOM 6916 N N   . TYR B 2 502  ? 189.566 185.142 144.677 1.00 12.14 ? 502 TYR B N   1 
ATOM 6917 C CA  . TYR B 2 502  ? 188.980 183.912 144.165 1.00 11.13 ? 502 TYR B CA  1 
ATOM 6918 C C   . TYR B 2 502  ? 189.861 183.359 143.052 1.00 9.96  ? 502 TYR B C   1 
ATOM 6919 O O   . TYR B 2 502  ? 190.847 183.976 142.643 1.00 9.63  ? 502 TYR B O   1 
ATOM 6920 C CB  . TYR B 2 502  ? 187.537 184.125 143.685 1.00 8.74  ? 502 TYR B CB  1 
ATOM 6921 C CG  . TYR B 2 502  ? 187.303 185.336 142.807 1.00 0.63  ? 502 TYR B CG  1 
ATOM 6922 C CD1 . TYR B 2 502  ? 187.060 186.582 143.364 1.00 3.62  ? 502 TYR B CD1 1 
ATOM 6923 C CD2 . TYR B 2 502  ? 187.288 185.224 141.424 1.00 1.74  ? 502 TYR B CD2 1 
ATOM 6924 C CE1 . TYR B 2 502  ? 186.832 187.685 142.573 1.00 5.50  ? 502 TYR B CE1 1 
ATOM 6925 C CE2 . TYR B 2 502  ? 187.059 186.324 140.623 1.00 0.28  ? 502 TYR B CE2 1 
ATOM 6926 C CZ  . TYR B 2 502  ? 186.832 187.552 141.204 1.00 3.85  ? 502 TYR B CZ  1 
ATOM 6927 O OH  . TYR B 2 502  ? 186.604 188.657 140.418 1.00 0.00  ? 502 TYR B OH  1 
ATOM 6928 N N   . LYS B 2 503  ? 189.487 182.179 142.569 1.00 8.25  ? 503 LYS B N   1 
ATOM 6929 C CA  . LYS B 2 503  ? 190.290 181.418 141.616 1.00 4.51  ? 503 LYS B CA  1 
ATOM 6930 C C   . LYS B 2 503  ? 189.359 180.902 140.523 1.00 5.13  ? 503 LYS B C   1 
ATOM 6931 O O   . LYS B 2 503  ? 188.226 181.370 140.367 1.00 10.89 ? 503 LYS B O   1 
ATOM 6932 C CB  . LYS B 2 503  ? 191.052 180.286 142.325 1.00 1.49  ? 503 LYS B CB  1 
ATOM 6933 C CG  . LYS B 2 503  ? 192.474 180.640 142.725 1.00 7.79  ? 503 LYS B CG  1 
ATOM 6934 C CD  . LYS B 2 503  ? 193.041 179.613 143.690 1.00 5.75  ? 503 LYS B CD  1 
ATOM 6935 C CE  . LYS B 2 503  ? 194.159 180.201 144.536 1.00 2.71  ? 503 LYS B CE  1 
ATOM 6936 N NZ  . LYS B 2 503  ? 194.888 181.290 143.830 1.00 3.04  ? 503 LYS B NZ  1 
ATOM 6937 N N   . ILE B 2 504  ? 189.846 179.940 139.737 1.00 2.22  ? 504 ILE B N   1 
ATOM 6938 C CA  . ILE B 2 504  ? 189.059 179.400 138.635 1.00 2.01  ? 504 ILE B CA  1 
ATOM 6939 C C   . ILE B 2 504  ? 187.835 178.676 139.175 1.00 1.97  ? 504 ILE B C   1 
ATOM 6940 O O   . ILE B 2 504  ? 187.937 177.794 140.037 1.00 8.49  ? 504 ILE B O   1 
ATOM 6941 C CB  . ILE B 2 504  ? 189.927 178.476 137.771 1.00 2.90  ? 504 ILE B CB  1 
ATOM 6942 C CG1 . ILE B 2 504  ? 191.224 179.188 137.390 1.00 4.64  ? 504 ILE B CG1 1 
ATOM 6943 C CG2 . ILE B 2 504  ? 189.169 178.041 136.532 1.00 0.00  ? 504 ILE B CG2 1 
ATOM 6944 C CD1 . ILE B 2 504  ? 192.182 178.327 136.624 1.00 3.69  ? 504 ILE B CD1 1 
ATOM 6945 N N   . MET B 2 505  ? 186.669 179.041 138.654 1.00 0.00  ? 505 MET B N   1 
ATOM 6946 C CA  . MET B 2 505  ? 185.397 178.535 139.143 1.00 0.00  ? 505 MET B CA  1 
ATOM 6947 C C   . MET B 2 505  ? 185.067 177.187 138.513 1.00 2.25  ? 505 MET B C   1 
ATOM 6948 O O   . MET B 2 505  ? 185.412 176.917 137.361 1.00 15.25 ? 505 MET B O   1 
ATOM 6949 C CB  . MET B 2 505  ? 184.289 179.539 138.833 1.00 0.00  ? 505 MET B CB  1 
ATOM 6950 C CG  . MET B 2 505  ? 182.892 179.045 139.103 1.00 6.02  ? 505 MET B CG  1 
ATOM 6951 S SD  . MET B 2 505  ? 182.633 178.753 140.855 1.00 23.06 ? 505 MET B SD  1 
ATOM 6952 C CE  . MET B 2 505  ? 180.902 179.159 140.994 1.00 5.62  ? 505 MET B CE  1 
ATOM 6953 N N   . GLY B 2 506  ? 184.390 176.337 139.283 1.00 5.10  ? 506 GLY B N   1 
ATOM 6954 C CA  . GLY B 2 506  ? 183.936 175.054 138.793 1.00 10.56 ? 506 GLY B CA  1 
ATOM 6955 C C   . GLY B 2 506  ? 184.903 173.906 138.985 1.00 7.61  ? 506 GLY B C   1 
ATOM 6956 O O   . GLY B 2 506  ? 184.528 172.756 138.726 1.00 5.41  ? 506 GLY B O   1 
ATOM 6957 N N   . LEU B 2 507  ? 186.126 174.173 139.431 1.00 10.19 ? 507 LEU B N   1 
ATOM 6958 C CA  . LEU B 2 507  ? 187.082 173.109 139.688 1.00 7.25  ? 507 LEU B CA  1 
ATOM 6959 C C   . LEU B 2 507  ? 186.649 172.289 140.900 1.00 10.21 ? 507 LEU B C   1 
ATOM 6960 O O   . LEU B 2 507  ? 185.829 172.718 141.715 1.00 10.92 ? 507 LEU B O   1 
ATOM 6961 C CB  . LEU B 2 507  ? 188.478 173.688 139.924 1.00 10.33 ? 507 LEU B CB  1 
ATOM 6962 C CG  . LEU B 2 507  ? 189.362 174.004 138.715 1.00 2.32  ? 507 LEU B CG  1 
ATOM 6963 C CD1 . LEU B 2 507  ? 190.782 174.314 139.159 1.00 2.01  ? 507 LEU B CD1 1 
ATOM 6964 C CD2 . LEU B 2 507  ? 189.355 172.857 137.727 1.00 10.26 ? 507 LEU B CD2 1 
ATOM 6965 N N   . ASN B 2 508  ? 187.209 171.087 141.009 1.00 18.13 ? 508 ASN B N   1 
ATOM 6966 C CA  . ASN B 2 508  ? 186.969 170.223 142.157 1.00 17.24 ? 508 ASN B CA  1 
ATOM 6967 C C   . ASN B 2 508  ? 188.309 169.644 142.598 1.00 18.18 ? 508 ASN B C   1 
ATOM 6968 O O   . ASN B 2 508  ? 189.373 170.082 142.150 1.00 14.91 ? 508 ASN B O   1 
ATOM 6969 C CB  . ASN B 2 508  ? 185.926 169.142 141.835 1.00 13.62 ? 508 ASN B CB  1 
ATOM 6970 C CG  . ASN B 2 508  ? 184.523 169.700 141.696 1.00 19.54 ? 508 ASN B CG  1 
ATOM 6971 O OD1 . ASN B 2 508  ? 183.868 170.021 142.686 1.00 20.86 ? 508 ASN B OD1 1 
ATOM 6972 N ND2 . ASN B 2 508  ? 184.054 169.818 140.459 1.00 17.52 ? 508 ASN B ND2 1 
ATOM 6973 N N   . ASN B 2 509  ? 188.265 168.719 143.554 1.00 22.11 ? 509 ASN B N   1 
ATOM 6974 C CA  . ASN B 2 509  ? 189.532 168.225 144.155 1.00 21.05 ? 509 ASN B CA  1 
ATOM 6975 C C   . ASN B 2 509  ? 190.475 167.589 143.134 1.00 22.47 ? 509 ASN B C   1 
ATOM 6976 O O   . ASN B 2 509  ? 191.573 168.140 142.945 1.00 21.24 ? 509 ASN B O   1 
ATOM 6977 C CB  . ASN B 2 509  ? 189.257 167.238 145.295 1.00 16.68 ? 509 ASN B CB  1 
ATOM 6978 C CG  . ASN B 2 509  ? 188.264 166.158 144.923 1.00 15.90 ? 509 ASN B CG  1 
ATOM 6979 O OD1 . ASN B 2 509  ? 187.499 166.308 143.973 1.00 15.07 ? 509 ASN B OD1 1 
ATOM 6980 N ND2 . ASN B 2 509  ? 188.271 165.061 145.663 1.00 19.14 ? 509 ASN B ND2 1 
ATOM 6981 N N   . VAL B 2 510  ? 190.055 166.518 142.461 1.00 26.02 ? 510 VAL B N   1 
ATOM 6982 C CA  . VAL B 2 510  ? 190.997 165.763 141.636 1.00 24.04 ? 510 VAL B CA  1 
ATOM 6983 C C   . VAL B 2 510  ? 191.533 166.625 140.498 1.00 24.09 ? 510 VAL B C   1 
ATOM 6984 O O   . VAL B 2 510  ? 192.699 166.504 140.103 1.00 19.92 ? 510 VAL B O   1 
ATOM 6985 C CB  . VAL B 2 510  ? 190.333 164.473 141.119 1.00 21.19 ? 510 VAL B CB  1 
ATOM 6986 C CG1 . VAL B 2 510  ? 189.015 164.786 140.422 1.00 19.29 ? 510 VAL B CG1 1 
ATOM 6987 C CG2 . VAL B 2 510  ? 191.276 163.711 140.198 1.00 18.35 ? 510 VAL B CG2 1 
ATOM 6988 N N   . THR B 2 511  ? 190.696 167.514 139.959 1.00 21.54 ? 511 THR B N   1 
ATOM 6989 C CA  . THR B 2 511  ? 191.141 168.392 138.881 1.00 20.88 ? 511 THR B CA  1 
ATOM 6990 C C   . THR B 2 511  ? 192.219 169.364 139.343 1.00 23.51 ? 511 THR B C   1 
ATOM 6991 O O   . THR B 2 511  ? 193.117 169.704 138.565 1.00 19.38 ? 511 THR B O   1 
ATOM 6992 C CB  . THR B 2 511  ? 189.953 169.165 138.310 1.00 20.49 ? 511 THR B CB  1 
ATOM 6993 O OG1 . THR B 2 511  ? 189.127 169.628 139.385 1.00 21.37 ? 511 THR B OG1 1 
ATOM 6994 C CG2 . THR B 2 511  ? 189.129 168.278 137.394 1.00 20.53 ? 511 THR B CG2 1 
ATOM 6995 N N   . SER B 2 512  ? 192.146 169.825 140.595 1.00 20.01 ? 512 SER B N   1 
ATOM 6996 C CA  . SER B 2 512  ? 193.063 170.861 141.064 1.00 20.02 ? 512 SER B CA  1 
ATOM 6997 C C   . SER B 2 512  ? 194.502 170.357 141.121 1.00 21.96 ? 512 SER B C   1 
ATOM 6998 O O   . SER B 2 512  ? 195.416 171.006 140.599 1.00 20.92 ? 512 SER B O   1 
ATOM 6999 C CB  . SER B 2 512  ? 192.616 171.369 142.434 1.00 22.59 ? 512 SER B CB  1 
ATOM 7000 O OG  . SER B 2 512  ? 193.000 172.719 142.627 1.00 27.77 ? 512 SER B OG  1 
ATOM 7001 N N   . GLN B 2 513  ? 194.726 169.204 141.757 1.00 24.43 ? 513 GLN B N   1 
ATOM 7002 C CA  . GLN B 2 513  ? 196.082 168.687 141.905 1.00 24.24 ? 513 GLN B CA  1 
ATOM 7003 C C   . GLN B 2 513  ? 196.608 168.021 140.641 1.00 22.58 ? 513 GLN B C   1 
ATOM 7004 O O   . GLN B 2 513  ? 197.828 167.900 140.488 1.00 24.64 ? 513 GLN B O   1 
ATOM 7005 C CB  . GLN B 2 513  ? 196.156 167.695 143.069 1.00 22.85 ? 513 GLN B CB  1 
ATOM 7006 C CG  . GLN B 2 513  ? 195.348 168.098 144.289 1.00 21.78 ? 513 GLN B CG  1 
ATOM 7007 C CD  . GLN B 2 513  ? 194.007 167.402 144.350 1.00 19.79 ? 513 GLN B CD  1 
ATOM 7008 O OE1 . GLN B 2 513  ? 193.749 166.459 143.601 1.00 20.51 ? 513 GLN B OE1 1 
ATOM 7009 N NE2 . GLN B 2 513  ? 193.137 167.870 145.236 1.00 16.44 ? 513 GLN B NE2 1 
ATOM 7010 N N   . SER B 2 514  ? 195.727 167.580 139.741 1.00 19.93 ? 514 SER B N   1 
ATOM 7011 C CA  . SER B 2 514  ? 196.190 166.987 138.491 1.00 24.99 ? 514 SER B CA  1 
ATOM 7012 C C   . SER B 2 514  ? 196.956 168.006 137.657 1.00 28.75 ? 514 SER B C   1 
ATOM 7013 O O   . SER B 2 514  ? 198.056 167.725 137.166 1.00 32.33 ? 514 SER B O   1 
ATOM 7014 C CB  . SER B 2 514  ? 195.006 166.424 137.707 1.00 28.79 ? 514 SER B CB  1 
ATOM 7015 O OG  . SER B 2 514  ? 194.448 167.410 136.857 1.00 28.36 ? 514 SER B OG  1 
ATOM 7016 N N   . TRP B 2 515  ? 196.393 169.202 137.498 1.00 27.21 ? 515 TRP B N   1 
ATOM 7017 C CA  . TRP B 2 515  ? 197.064 170.292 136.804 1.00 25.42 ? 515 TRP B CA  1 
ATOM 7018 C C   . TRP B 2 515  ? 196.291 171.575 137.065 1.00 27.97 ? 515 TRP B C   1 
ATOM 7019 O O   . TRP B 2 515  ? 195.069 171.554 137.233 1.00 31.94 ? 515 TRP B O   1 
ATOM 7020 C CB  . TRP B 2 515  ? 197.172 170.028 135.297 1.00 29.36 ? 515 TRP B CB  1 
ATOM 7021 C CG  . TRP B 2 515  ? 197.815 171.148 134.538 1.00 32.44 ? 515 TRP B CG  1 
ATOM 7022 C CD1 . TRP B 2 515  ? 197.188 172.059 133.738 1.00 34.07 ? 515 TRP B CD1 1 
ATOM 7023 C CD2 . TRP B 2 515  ? 199.208 171.481 134.509 1.00 34.04 ? 515 TRP B CD2 1 
ATOM 7024 N NE1 . TRP B 2 515  ? 198.104 172.936 133.211 1.00 34.47 ? 515 TRP B NE1 1 
ATOM 7025 C CE2 . TRP B 2 515  ? 199.351 172.603 133.669 1.00 33.63 ? 515 TRP B CE2 1 
ATOM 7026 C CE3 . TRP B 2 515  ? 200.347 170.937 135.109 1.00 31.88 ? 515 TRP B CE3 1 
ATOM 7027 C CZ2 . TRP B 2 515  ? 200.586 173.192 133.415 1.00 30.94 ? 515 TRP B CZ2 1 
ATOM 7028 C CZ3 . TRP B 2 515  ? 201.573 171.525 134.857 1.00 31.12 ? 515 TRP B CZ3 1 
ATOM 7029 C CH2 . TRP B 2 515  ? 201.682 172.640 134.016 1.00 32.22 ? 515 TRP B CH2 1 
ATOM 7030 N N   . GLN B 2 516  ? 197.019 172.696 137.099 1.00 25.37 ? 516 GLN B N   1 
ATOM 7031 C CA  . GLN B 2 516  ? 196.383 173.989 137.308 1.00 26.50 ? 516 GLN B CA  1 
ATOM 7032 C C   . GLN B 2 516  ? 197.219 175.069 136.647 1.00 26.62 ? 516 GLN B C   1 
ATOM 7033 O O   . GLN B 2 516  ? 198.455 174.996 136.699 1.00 23.25 ? 516 GLN B O   1 
ATOM 7034 C CB  . GLN B 2 516  ? 196.206 174.290 138.803 1.00 29.69 ? 516 GLN B CB  1 
ATOM 7035 C CG  . GLN B 2 516  ? 195.420 175.557 139.111 1.00 30.16 ? 516 GLN B CG  1 
ATOM 7036 C CD  . GLN B 2 516  ? 195.126 175.724 140.590 1.00 29.04 ? 516 GLN B CD  1 
ATOM 7037 O OE1 . GLN B 2 516  ? 195.428 174.846 141.398 1.00 34.50 ? 516 GLN B OE1 1 
ATOM 7038 N NE2 . GLN B 2 516  ? 194.536 176.856 140.952 1.00 23.48 ? 516 GLN B NE2 1 
ATOM 7039 N N   . PRO B 2 517  ? 196.600 176.064 136.009 1.00 31.68 ? 517 PRO B N   1 
ATOM 7040 C CA  . PRO B 2 517  ? 197.381 177.154 135.409 1.00 27.24 ? 517 PRO B CA  1 
ATOM 7041 C C   . PRO B 2 517  ? 197.743 178.234 136.416 1.00 30.42 ? 517 PRO B C   1 
ATOM 7042 O O   . PRO B 2 517  ? 197.455 178.103 137.611 1.00 29.11 ? 517 PRO B O   1 
ATOM 7043 C CB  . PRO B 2 517  ? 196.451 177.689 134.314 1.00 17.90 ? 517 PRO B CB  1 
ATOM 7044 C CG  . PRO B 2 517  ? 195.079 177.368 134.792 1.00 24.95 ? 517 PRO B CG  1 
ATOM 7045 C CD  . PRO B 2 517  ? 195.161 176.178 135.716 1.00 31.80 ? 517 PRO B CD  1 
ATOM 7046 N N   . GLN B 2 518  ? 198.372 179.306 135.941 1.00 27.02 ? 518 GLN B N   1 
ATOM 7047 C CA  . GLN B 2 518  ? 198.891 180.356 136.807 1.00 25.54 ? 518 GLN B CA  1 
ATOM 7048 C C   . GLN B 2 518  ? 197.782 181.324 137.199 1.00 21.67 ? 518 GLN B C   1 
ATOM 7049 O O   . GLN B 2 518  ? 196.993 181.753 136.352 1.00 18.91 ? 518 GLN B O   1 
ATOM 7050 C CB  . GLN B 2 518  ? 200.028 181.110 136.115 1.00 23.86 ? 518 GLN B CB  1 
ATOM 7051 C CG  . GLN B 2 518  ? 201.103 180.214 135.517 1.00 24.73 ? 518 GLN B CG  1 
ATOM 7052 C CD  . GLN B 2 518  ? 200.736 179.683 134.144 1.00 23.54 ? 518 GLN B CD  1 
ATOM 7053 O OE1 . GLN B 2 518  ? 199.654 179.963 133.626 1.00 17.52 ? 518 GLN B OE1 1 
ATOM 7054 N NE2 . GLN B 2 518  ? 201.638 178.913 133.546 1.00 27.27 ? 518 GLN B NE2 1 
ATOM 7055 N N   . THR B 2 519  ? 197.728 181.662 138.485 1.00 15.27 ? 519 THR B N   1 
ATOM 7056 C CA  . THR B 2 519  ? 196.768 182.618 139.018 1.00 13.24 ? 519 THR B CA  1 
ATOM 7057 C C   . THR B 2 519  ? 197.474 183.489 140.047 1.00 11.36 ? 519 THR B C   1 
ATOM 7058 O O   . THR B 2 519  ? 198.210 182.974 140.895 1.00 11.55 ? 519 THR B O   1 
ATOM 7059 C CB  . THR B 2 519  ? 195.568 181.903 139.649 1.00 15.28 ? 519 THR B CB  1 
ATOM 7060 O OG1 . THR B 2 519  ? 194.871 181.161 138.641 1.00 14.12 ? 519 THR B OG1 1 
ATOM 7061 C CG2 . THR B 2 519  ? 194.614 182.904 140.277 1.00 7.39  ? 519 THR B CG2 1 
ATOM 7062 N N   . TYR B 2 520  ? 197.256 184.800 139.971 1.00 6.29  ? 520 TYR B N   1 
ATOM 7063 C CA  . TYR B 2 520  ? 197.938 185.732 140.856 1.00 2.62  ? 520 TYR B CA  1 
ATOM 7064 C C   . TYR B 2 520  ? 197.134 185.939 142.139 1.00 4.99  ? 520 TYR B C   1 
ATOM 7065 O O   . TYR B 2 520  ? 196.034 185.409 142.313 1.00 8.68  ? 520 TYR B O   1 
ATOM 7066 C CB  . TYR B 2 520  ? 198.183 187.060 140.142 1.00 5.87  ? 520 TYR B CB  1 
ATOM 7067 C CG  . TYR B 2 520  ? 196.943 187.904 139.939 1.00 11.95 ? 520 TYR B CG  1 
ATOM 7068 C CD1 . TYR B 2 520  ? 196.542 188.825 140.897 1.00 8.14  ? 520 TYR B CD1 1 
ATOM 7069 C CD2 . TYR B 2 520  ? 196.182 187.789 138.787 1.00 7.69  ? 520 TYR B CD2 1 
ATOM 7070 C CE1 . TYR B 2 520  ? 195.418 189.599 140.719 1.00 4.15  ? 520 TYR B CE1 1 
ATOM 7071 C CE2 . TYR B 2 520  ? 195.055 188.562 138.600 1.00 7.30  ? 520 TYR B CE2 1 
ATOM 7072 C CZ  . TYR B 2 520  ? 194.680 189.466 139.571 1.00 7.30  ? 520 TYR B CZ  1 
ATOM 7073 O OH  . TYR B 2 520  ? 193.560 190.244 139.400 1.00 5.87  ? 520 TYR B OH  1 
ATOM 7074 N N   . GLN B 2 521  ? 197.694 186.733 143.051 1.00 3.00  ? 521 GLN B N   1 
ATOM 7075 C CA  . GLN B 2 521  ? 197.028 187.078 144.301 1.00 0.00  ? 521 GLN B CA  1 
ATOM 7076 C C   . GLN B 2 521  ? 196.649 188.548 144.372 1.00 3.17  ? 521 GLN B C   1 
ATOM 7077 O O   . GLN B 2 521  ? 195.487 188.865 144.644 1.00 7.19  ? 521 GLN B O   1 
ATOM 7078 C CB  . GLN B 2 521  ? 197.915 186.699 145.497 1.00 0.00  ? 521 GLN B CB  1 
ATOM 7079 C CG  . GLN B 2 521  ? 198.287 185.226 145.533 1.00 0.25  ? 521 GLN B CG  1 
ATOM 7080 C CD  . GLN B 2 521  ? 198.240 184.643 146.930 1.00 0.00  ? 521 GLN B CD  1 
ATOM 7081 O OE1 . GLN B 2 521  ? 199.263 184.537 147.604 1.00 0.00  ? 521 GLN B OE1 1 
ATOM 7082 N NE2 . GLN B 2 521  ? 197.048 184.261 147.372 1.00 0.00  ? 521 GLN B NE2 1 
ATOM 7083 N N   . ILE B 2 522  ? 197.595 189.462 144.143 1.00 6.29  ? 522 ILE B N   1 
ATOM 7084 C CA  . ILE B 2 522  ? 197.293 190.886 144.053 1.00 10.76 ? 522 ILE B CA  1 
ATOM 7085 C C   . ILE B 2 522  ? 198.011 191.473 142.846 1.00 9.85  ? 522 ILE B C   1 
ATOM 7086 O O   . ILE B 2 522  ? 199.037 190.961 142.392 1.00 1.21  ? 522 ILE B O   1 
ATOM 7087 C CB  . ILE B 2 522  ? 197.688 191.670 145.327 1.00 1.25  ? 522 ILE B CB  1 
ATOM 7088 C CG1 . ILE B 2 522  ? 199.206 191.688 145.502 1.00 0.00  ? 522 ILE B CG1 1 
ATOM 7089 C CG2 . ILE B 2 522  ? 197.009 191.093 146.557 1.00 0.77  ? 522 ILE B CG2 1 
ATOM 7090 C CD1 . ILE B 2 522  ? 199.674 192.632 146.580 1.00 0.00  ? 522 ILE B CD1 1 
ATOM 7091 N N   . CYS B 2 523  ? 197.456 192.569 142.328 1.00 9.30  ? 523 CYS B N   1 
ATOM 7092 C CA  . CYS B 2 523  ? 198.080 193.328 141.254 1.00 3.36  ? 523 CYS B CA  1 
ATOM 7093 C C   . CYS B 2 523  ? 198.008 194.817 141.557 1.00 6.36  ? 523 CYS B C   1 
ATOM 7094 O O   . CYS B 2 523  ? 197.138 195.277 142.297 1.00 6.42  ? 523 CYS B O   1 
ATOM 7095 C CB  . CYS B 2 523  ? 197.427 193.057 139.894 1.00 3.23  ? 523 CYS B CB  1 
ATOM 7096 S SG  . CYS B 2 523  ? 197.804 191.446 139.183 1.00 26.81 ? 523 CYS B SG  1 
ATOM 7097 N N   . LEU B 2 524  ? 198.940 195.566 140.978 1.00 4.47  ? 524 LEU B N   1 
ATOM 7098 C CA  . LEU B 2 524  ? 198.998 197.017 141.117 1.00 6.76  ? 524 LEU B CA  1 
ATOM 7099 C C   . LEU B 2 524  ? 198.957 197.612 139.717 1.00 13.22 ? 524 LEU B C   1 
ATOM 7100 O O   . LEU B 2 524  ? 199.878 197.393 138.922 1.00 20.34 ? 524 LEU B O   1 
ATOM 7101 C CB  . LEU B 2 524  ? 200.263 197.445 141.861 1.00 4.20  ? 524 LEU B CB  1 
ATOM 7102 C CG  . LEU B 2 524  ? 200.394 198.910 142.285 1.00 4.10  ? 524 LEU B CG  1 
ATOM 7103 C CD1 . LEU B 2 524  ? 199.205 199.347 143.113 1.00 4.28  ? 524 LEU B CD1 1 
ATOM 7104 C CD2 . LEU B 2 524  ? 201.680 199.127 143.052 1.00 6.39  ? 524 LEU B CD2 1 
ATOM 7105 N N   . VAL B 2 525  ? 197.890 198.345 139.407 1.00 9.62  ? 525 VAL B N   1 
ATOM 7106 C CA  . VAL B 2 525  ? 197.729 198.959 138.093 1.00 4.72  ? 525 VAL B CA  1 
ATOM 7107 C C   . VAL B 2 525  ? 198.126 200.425 138.194 1.00 4.68  ? 525 VAL B C   1 
ATOM 7108 O O   . VAL B 2 525  ? 197.745 201.122 139.145 1.00 18.56 ? 525 VAL B O   1 
ATOM 7109 C CB  . VAL B 2 525  ? 196.297 198.787 137.548 1.00 6.11  ? 525 VAL B CB  1 
ATOM 7110 C CG1 . VAL B 2 525  ? 195.873 197.327 137.621 1.00 11.94 ? 525 VAL B CG1 1 
ATOM 7111 C CG2 . VAL B 2 525  ? 195.299 199.667 138.268 1.00 5.21  ? 525 VAL B CG2 1 
ATOM 7112 N N   . ASP B 2 526  ? 198.945 200.891 137.245 1.00 0.00  ? 526 ASP B N   1 
ATOM 7113 C CA  . ASP B 2 526  ? 199.460 202.285 137.329 1.00 5.36  ? 526 ASP B CA  1 
ATOM 7114 C C   . ASP B 2 526  ? 199.070 203.074 136.076 1.00 4.70  ? 526 ASP B C   1 
ATOM 7115 O O   . ASP B 2 526  ? 199.308 202.569 134.966 1.00 10.26 ? 526 ASP B O   1 
ATOM 7116 C CB  . ASP B 2 526  ? 200.977 202.306 137.532 1.00 10.42 ? 526 ASP B CB  1 
ATOM 7117 C CG  . ASP B 2 526  ? 201.552 203.710 137.582 1.00 15.08 ? 526 ASP B CG  1 
ATOM 7118 O OD1 . ASP B 2 526  ? 201.308 204.408 138.585 1.00 17.55 ? 526 ASP B OD1 1 
ATOM 7119 O OD2 . ASP B 2 526  ? 202.235 204.097 136.615 1.00 12.99 ? 526 ASP B OD2 1 
ATOM 7120 N N   . PRO B 2 527  ? 198.487 204.286 136.210 1.00 6.79  ? 527 PRO B N   1 
ATOM 7121 C CA  . PRO B 2 527  ? 198.150 205.121 135.051 1.00 8.74  ? 527 PRO B CA  1 
ATOM 7122 C C   . PRO B 2 527  ? 199.375 205.762 134.385 1.00 13.15 ? 527 PRO B C   1 
ATOM 7123 O O   . PRO B 2 527  ? 199.440 205.753 133.170 1.00 13.52 ? 527 PRO B O   1 
ATOM 7124 C CB  . PRO B 2 527  ? 197.295 206.239 135.663 1.00 7.05  ? 527 PRO B CB  1 
ATOM 7125 C CG  . PRO B 2 527  ? 197.770 206.331 137.097 1.00 1.26  ? 527 PRO B CG  1 
ATOM 7126 C CD  . PRO B 2 527  ? 198.115 204.909 137.483 1.00 9.75  ? 527 PRO B CD  1 
ATOM 7127 N N   . VAL B 2 528  ? 200.306 206.294 135.183 1.00 10.85 ? 528 VAL B N   1 
ATOM 7128 C CA  . VAL B 2 528  ? 201.485 207.015 134.616 1.00 8.16  ? 528 VAL B CA  1 
ATOM 7129 C C   . VAL B 2 528  ? 202.240 206.073 133.673 1.00 11.44 ? 528 VAL B C   1 
ATOM 7130 O O   . VAL B 2 528  ? 202.590 206.511 132.560 1.00 13.25 ? 528 VAL B O   1 
ATOM 7131 C CB  . VAL B 2 528  ? 202.405 207.546 135.732 1.00 10.97 ? 528 VAL B CB  1 
ATOM 7132 C CG1 . VAL B 2 528  ? 203.669 208.175 135.169 1.00 10.85 ? 528 VAL B CG1 1 
ATOM 7133 C CG2 . VAL B 2 528  ? 201.679 208.524 136.643 1.00 9.00  ? 528 VAL B CG2 1 
ATOM 7134 N N   . SER B 2 529  ? 202.475 204.832 134.107 1.00 9.01  ? 529 SER B N   1 
ATOM 7135 C CA  . SER B 2 529  ? 203.208 203.849 133.268 1.00 11.50 ? 529 SER B CA  1 
ATOM 7136 C C   . SER B 2 529  ? 202.215 203.017 132.452 1.00 13.86 ? 529 SER B C   1 
ATOM 7137 O O   . SER B 2 529  ? 202.675 202.211 131.619 1.00 16.83 ? 529 SER B O   1 
ATOM 7138 C CB  . SER B 2 529  ? 204.085 202.967 134.117 1.00 10.62 ? 529 SER B CB  1 
ATOM 7139 O OG  . SER B 2 529  ? 203.298 202.087 134.907 1.00 7.96  ? 529 SER B OG  1 
ATOM 7140 N N   . GLY B 2 530  ? 200.911 203.198 132.685 1.00 10.52 ? 530 GLY B N   1 
ATOM 7141 C CA  . GLY B 2 530  ? 199.910 202.365 131.991 1.00 7.14  ? 530 GLY B CA  1 
ATOM 7142 C C   . GLY B 2 530  ? 200.322 200.907 132.055 1.00 10.45 ? 530 GLY B C   1 
ATOM 7143 O O   . GLY B 2 530  ? 200.398 200.271 130.986 1.00 13.27 ? 530 GLY B O   1 
ATOM 7144 N N   . SER B 2 531  ? 200.591 200.394 133.261 1.00 14.36 ? 531 SER B N   1 
ATOM 7145 C CA  . SER B 2 531  ? 201.113 199.006 133.370 1.00 14.05 ? 531 SER B CA  1 
ATOM 7146 C C   . SER B 2 531  ? 200.502 198.260 134.560 1.00 13.94 ? 531 SER B C   1 
ATOM 7147 O O   . SER B 2 531  ? 199.905 198.923 135.431 1.00 15.54 ? 531 SER B O   1 
ATOM 7148 C CB  . SER B 2 531  ? 202.619 199.015 133.452 1.00 13.49 ? 531 SER B CB  1 
ATOM 7149 O OG  . SER B 2 531  ? 203.188 199.508 132.248 1.00 14.11 ? 531 SER B OG  1 
ATOM 7150 N N   . VAL B 2 532  ? 200.656 196.933 134.588 1.00 8.57  ? 532 VAL B N   1 
ATOM 7151 C CA  . VAL B 2 532  ? 200.140 196.099 135.666 1.00 11.64 ? 532 VAL B CA  1 
ATOM 7152 C C   . VAL B 2 532  ? 201.303 195.295 136.227 1.00 13.40 ? 532 VAL B C   1 
ATOM 7153 O O   . VAL B 2 532  ? 201.980 194.570 135.483 1.00 7.13  ? 532 VAL B O   1 
ATOM 7154 C CB  . VAL B 2 532  ? 199.010 195.168 135.198 1.00 11.82 ? 532 VAL B CB  1 
ATOM 7155 C CG1 . VAL B 2 532  ? 198.384 194.470 136.387 1.00 11.25 ? 532 VAL B CG1 1 
ATOM 7156 C CG2 . VAL B 2 532  ? 197.959 195.954 134.440 1.00 9.66  ? 532 VAL B CG2 1 
ATOM 7157 N N   . LYS B 2 533  ? 201.531 195.478 137.528 1.00 16.65 ? 533 LYS B N   1 
ATOM 7158 C CA  . LYS B 2 533  ? 202.683 194.805 138.171 1.00 14.10 ? 533 LYS B CA  1 
ATOM 7159 C C   . LYS B 2 533  ? 202.203 193.898 139.300 1.00 8.08  ? 533 LYS B C   1 
ATOM 7160 O O   . LYS B 2 533  ? 201.033 194.024 139.710 1.00 7.47  ? 533 LYS B O   1 
ATOM 7161 C CB  . LYS B 2 533  ? 203.666 195.844 138.719 1.00 10.49 ? 533 LYS B CB  1 
ATOM 7162 C CG  . LYS B 2 533  ? 203.980 197.003 137.782 1.00 11.01 ? 533 LYS B CG  1 
ATOM 7163 C CD  . LYS B 2 533  ? 205.319 197.647 138.065 1.00 7.69  ? 533 LYS B CD  1 
ATOM 7164 C CE  . LYS B 2 533  ? 205.604 198.837 137.173 1.00 9.77  ? 533 LYS B CE  1 
ATOM 7165 N NZ  . LYS B 2 533  ? 206.946 198.749 136.551 1.00 8.74  ? 533 LYS B NZ  1 
ATOM 7166 N N   . THR B 2 534  ? 203.083 193.026 139.773 1.00 9.22  ? 534 THR B N   1 
ATOM 7167 C CA  . THR B 2 534  ? 202.805 192.096 140.854 1.00 9.80  ? 534 THR B CA  1 
ATOM 7168 C C   . THR B 2 534  ? 203.872 192.248 141.930 1.00 11.62 ? 534 THR B C   1 
ATOM 7169 O O   . THR B 2 534  ? 204.952 192.793 141.691 1.00 13.34 ? 534 THR B O   1 
ATOM 7170 C CB  . THR B 2 534  ? 202.753 190.646 140.353 1.00 9.26  ? 534 THR B CB  1 
ATOM 7171 O OG1 . THR B 2 534  ? 202.151 189.812 141.351 1.00 11.72 ? 534 THR B OG1 1 
ATOM 7172 C CG2 . THR B 2 534  ? 204.150 190.136 140.048 1.00 9.81  ? 534 THR B CG2 1 
ATOM 7173 N N   . VAL B 2 535  ? 203.487 191.792 143.130 1.00 12.81 ? 535 VAL B N   1 
ATOM 7174 C CA  . VAL B 2 535  ? 204.380 191.886 144.316 1.00 10.66 ? 535 VAL B CA  1 
ATOM 7175 C C   . VAL B 2 535  ? 204.776 190.473 144.733 1.00 16.49 ? 535 VAL B C   1 
ATOM 7176 O O   . VAL B 2 535  ? 203.875 189.620 144.859 1.00 20.61 ? 535 VAL B O   1 
ATOM 7177 C CB  . VAL B 2 535  ? 203.653 192.582 145.481 1.00 10.46 ? 535 VAL B CB  1 
ATOM 7178 C CG1 . VAL B 2 535  ? 204.572 192.809 146.671 1.00 16.06 ? 535 VAL B CG1 1 
ATOM 7179 C CG2 . VAL B 2 535  ? 202.998 193.884 145.046 1.00 10.40 ? 535 VAL B CG2 1 
ATOM 7180 N N   . ASN B 2 536  ? 206.067 190.242 144.940 1.00 16.09 ? 536 ASN B N   1 
ATOM 7181 C CA  . ASN B 2 536  ? 206.568 188.954 145.400 1.00 18.09 ? 536 ASN B CA  1 
ATOM 7182 C C   . ASN B 2 536  ? 207.304 189.142 146.717 1.00 25.49 ? 536 ASN B C   1 
ATOM 7183 O O   . ASN B 2 536  ? 208.132 190.050 146.844 1.00 29.75 ? 536 ASN B O   1 
ATOM 7184 C CB  . ASN B 2 536  ? 207.498 188.322 144.363 1.00 19.22 ? 536 ASN B CB  1 
ATOM 7185 C CG  . ASN B 2 536  ? 208.027 186.973 144.805 1.00 24.51 ? 536 ASN B CG  1 
ATOM 7186 O OD1 . ASN B 2 536  ? 207.287 186.152 145.347 1.00 24.25 ? 536 ASN B OD1 1 
ATOM 7187 N ND2 . ASN B 2 536  ? 209.315 186.741 144.582 1.00 28.21 ? 536 ASN B ND2 1 
ATOM 7188 N N   . VAL B 2 537  ? 207.004 188.283 147.693 1.00 26.99 ? 537 VAL B N   1 
ATOM 7189 C CA  . VAL B 2 537  ? 207.611 188.346 149.013 1.00 26.89 ? 537 VAL B CA  1 
ATOM 7190 C C   . VAL B 2 537  ? 208.150 186.968 149.373 1.00 22.83 ? 537 VAL B C   1 
ATOM 7191 O O   . VAL B 2 537  ? 207.383 186.001 149.429 1.00 18.13 ? 537 VAL B O   1 
ATOM 7192 C CB  . VAL B 2 537  ? 206.623 188.825 150.091 1.00 22.29 ? 537 VAL B CB  1 
ATOM 7193 C CG1 . VAL B 2 537  ? 207.260 188.726 151.465 1.00 15.36 ? 537 VAL B CG1 1 
ATOM 7194 C CG2 . VAL B 2 537  ? 206.168 190.249 149.811 1.00 14.86 ? 537 VAL B CG2 1 
ATOM 7195 N N   . PRO B 2 538  ? 209.448 186.820 149.632 1.00 24.59 ? 538 PRO B N   1 
ATOM 7196 C CA  . PRO B 2 538  ? 209.975 185.515 150.045 1.00 23.92 ? 538 PRO B CA  1 
ATOM 7197 C C   . PRO B 2 538  ? 209.447 185.119 151.413 1.00 21.48 ? 538 PRO B C   1 
ATOM 7198 O O   . PRO B 2 538  ? 209.071 185.965 152.226 1.00 24.78 ? 538 PRO B O   1 
ATOM 7199 C CB  . PRO B 2 538  ? 211.493 185.735 150.080 1.00 25.94 ? 538 PRO B CB  1 
ATOM 7200 C CG  . PRO B 2 538  ? 211.730 187.037 149.376 1.00 23.38 ? 538 PRO B CG  1 
ATOM 7201 C CD  . PRO B 2 538  ? 210.498 187.846 149.571 1.00 21.95 ? 538 PRO B CD  1 
ATOM 7202 N N   . PHE B 2 539  ? 209.409 183.809 151.659 1.00 17.18 ? 539 PHE B N   1 
ATOM 7203 C CA  . PHE B 2 539  ? 208.915 183.330 152.945 1.00 20.85 ? 539 PHE B CA  1 
ATOM 7204 C C   . PHE B 2 539  ? 209.937 183.496 154.064 1.00 19.44 ? 539 PHE B C   1 
ATOM 7205 O O   . PHE B 2 539  ? 209.548 183.668 155.224 1.00 16.90 ? 539 PHE B O   1 
ATOM 7206 C CB  . PHE B 2 539  ? 208.506 181.860 152.852 1.00 15.88 ? 539 PHE B CB  1 
ATOM 7207 C CG  . PHE B 2 539  ? 208.625 181.125 154.152 1.00 10.13 ? 539 PHE B CG  1 
ATOM 7208 C CD1 . PHE B 2 539  ? 207.674 181.291 155.141 1.00 5.38  ? 539 PHE B CD1 1 
ATOM 7209 C CD2 . PHE B 2 539  ? 209.693 180.279 154.392 1.00 13.96 ? 539 PHE B CD2 1 
ATOM 7210 C CE1 . PHE B 2 539  ? 207.787 180.630 156.339 1.00 10.94 ? 539 PHE B CE1 1 
ATOM 7211 C CE2 . PHE B 2 539  ? 209.807 179.612 155.590 1.00 15.83 ? 539 PHE B CE2 1 
ATOM 7212 C CZ  . PHE B 2 539  ? 208.851 179.786 156.564 1.00 13.40 ? 539 PHE B CZ  1 
ATOM 7213 N N   . HIS B 2 540  ? 211.232 183.443 153.745 1.00 16.57 ? 540 HIS B N   1 
ATOM 7214 C CA  . HIS B 2 540  ? 212.260 183.381 154.780 1.00 18.87 ? 540 HIS B CA  1 
ATOM 7215 C C   . HIS B 2 540  ? 212.231 184.579 155.721 1.00 22.31 ? 540 HIS B C   1 
ATOM 7216 O O   . HIS B 2 540  ? 212.493 184.419 156.919 1.00 21.07 ? 540 HIS B O   1 
ATOM 7217 C CB  . HIS B 2 540  ? 213.640 183.244 154.128 1.00 19.74 ? 540 HIS B CB  1 
ATOM 7218 C CG  . HIS B 2 540  ? 214.239 184.542 153.683 1.00 24.37 ? 540 HIS B CG  1 
ATOM 7219 N ND1 . HIS B 2 540  ? 214.875 185.407 154.549 1.00 24.28 ? 540 HIS B ND1 1 
ATOM 7220 C CD2 . HIS B 2 540  ? 214.305 185.119 152.460 1.00 22.33 ? 540 HIS B CD2 1 
ATOM 7221 C CE1 . HIS B 2 540  ? 215.304 186.461 153.878 1.00 24.69 ? 540 HIS B CE1 1 
ATOM 7222 N NE2 . HIS B 2 540  ? 214.971 186.311 152.609 1.00 25.02 ? 540 HIS B NE2 1 
ATOM 7223 N N   . LEU B 2 541  ? 211.873 185.756 155.196 1.00 19.94 ? 541 LEU B N   1 
ATOM 7224 C CA  . LEU B 2 541  ? 211.857 186.994 156.023 1.00 21.75 ? 541 LEU B CA  1 
ATOM 7225 C C   . LEU B 2 541  ? 210.988 186.777 157.266 1.00 22.72 ? 541 LEU B C   1 
ATOM 7226 O O   . LEU B 2 541  ? 211.305 187.373 158.313 1.00 20.85 ? 541 LEU B O   1 
ATOM 7227 C CB  . LEU B 2 541  ? 211.309 188.151 155.183 1.00 15.36 ? 541 LEU B CB  1 
ATOM 7228 C CG  . LEU B 2 541  ? 212.160 188.564 153.985 1.00 16.03 ? 541 LEU B CG  1 
ATOM 7229 C CD1 . LEU B 2 541  ? 211.437 189.613 153.158 1.00 13.51 ? 541 LEU B CD1 1 
ATOM 7230 C CD2 . LEU B 2 541  ? 213.510 189.094 154.440 1.00 24.07 ? 541 LEU B CD2 1 
ATOM 7231 N N   . ALA B 2 542  ? 209.939 185.956 157.155 1.00 19.68 ? 542 ALA B N   1 
ATOM 7232 C CA  . ALA B 2 542  ? 209.005 185.756 158.289 1.00 19.51 ? 542 ALA B CA  1 
ATOM 7233 C C   . ALA B 2 542  ? 209.770 185.255 159.518 1.00 18.52 ? 542 ALA B C   1 
ATOM 7234 O O   . ALA B 2 542  ? 209.451 185.708 160.634 1.00 17.72 ? 542 ALA B O   1 
ATOM 7235 C CB  . ALA B 2 542  ? 207.914 184.794 157.890 1.00 11.67 ? 542 ALA B CB  1 
ATOM 7236 N N   . LEU B 2 543  ? 210.739 184.358 159.319 1.00 17.56 ? 543 LEU B N   1 
ATOM 7237 C CA  . LEU B 2 543  ? 211.489 183.767 160.462 1.00 17.91 ? 543 LEU B CA  1 
ATOM 7238 C C   . LEU B 2 543  ? 212.029 184.882 161.367 1.00 22.14 ? 543 LEU B C   1 
ATOM 7239 O O   . LEU B 2 543  ? 211.976 184.705 162.600 1.00 24.94 ? 543 LEU B O   1 
ATOM 7240 C CB  . LEU B 2 543  ? 212.622 182.896 159.910 1.00 18.68 ? 543 LEU B CB  1 
ATOM 7241 C CG  . LEU B 2 543  ? 212.191 181.830 158.905 1.00 18.71 ? 543 LEU B CG  1 
ATOM 7242 C CD1 . LEU B 2 543  ? 213.359 180.933 158.528 1.00 19.89 ? 543 LEU B CD1 1 
ATOM 7243 C CD2 . LEU B 2 543  ? 211.036 181.003 159.450 1.00 13.19 ? 543 LEU B CD2 1 
ATOM 7244 N N   . SER B 2 544  ? 212.528 185.977 160.783 1.00 25.81 ? 544 SER B N   1 
ATOM 7245 C CA  . SER B 2 544  ? 213.087 187.076 161.573 1.00 28.56 ? 544 SER B CA  1 
ATOM 7246 C C   . SER B 2 544  ? 213.854 186.579 162.798 1.00 21.69 ? 544 SER B C   1 
ATOM 7247 O O   . SER B 2 544  ? 214.992 186.121 162.689 1.00 21.25 ? 544 SER B O   1 
ATOM 7248 C CB  . SER B 2 544  ? 211.980 188.041 162.008 1.00 27.39 ? 544 SER B CB  1 
ATOM 7249 O OG  . SER B 2 544  ? 211.263 188.531 160.889 1.00 24.62 ? 544 SER B OG  1 
# 
