data_9BTC
# 
_entry.id   9BTC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9BTC         pdb_00009btc 10.2210/pdb9btc/pdb 
WWPDB D_1000282840 ?            ?                   
EMDB  EMD-44887    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 2 'Structure model' em_admin 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BTC 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        
'Cryo-EM density map of HKU1 spike glycoprotein D1 domain in complex with 9O-acetyl GD3 sialoglycan (Up state, locally refined)' 
_pdbx_database_related.db_id          EMD-44887 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              james.rini@utoronto.ca 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Rini 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0952-2409 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jin, M.'    1 0009-0009-1155-9890 
'Rini, J.M.' 2 0000-0002-0952-2409 
# 
_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                4158 
_citation.page_last                 4158 
_citation.title                     
;Human coronavirus HKU1 spike structures reveal the basis for sialoglycan specificity and carbohydrate-promoted conformational changes.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59137-y 
_citation.pdbx_database_id_PubMed   40324974 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jin, M.'           1  ? 
primary 'Hassan, Z.'        2  ? 
primary 'Li, Z.'            3  ? 
primary 'Liu, Y.'           4  ? 
primary 'Marakhovskaia, A.' 5  ? 
primary 'Wong, A.H.M.'      6  ? 
primary 'Forman, A.'        7  ? 
primary 'Nitz, M.'          8  ? 
primary 'Gilbert, M.'       9  ? 
primary 'Yu, H.'            10 ? 
primary 'Chen, X.'          11 ? 
primary 'Rini, J.M.'        12 ? 
# 
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 'Spike glycoprotein' 133185.500 1 ? ? 'ectodomain (UNP residues 14-1298)' ? 
2 branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823    1 ? ? ?                                   ? 
3 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    1 ? ? ? ? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    6 ? ? ?                                   ? 
5 non-polymer syn 
;5-acetamido-8-O-(5-acetamido-9-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranonosyl)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid
;
642.561    1 ? ? ?                                   ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'S glycoprotein,E2,Peplomer protein' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;VIGDFNCTNFAINDLNTTVPRISEYVVDVSYGLGTYYILDRVYLNTTILFTGYFPKSGANFRDLSLKGTTYLSTLWYQKP
FLSDFNNGIFSRVKNTKLYVNKTLYSEFSTIVIGSVFINNSYTIVVQPHNGVLEITACQYTMCEYPHTICKSKGSSRNES
WHFDKSEPLCLFKKNFTYNVSTDWLYFHFYQERGTFYAYYADSGMPTTFLFSLYLGTLLSHYYVLPLTCNAISSNTDNET
LQYWVTPLSKRQYLLKFDNRGVITNAVDCSSSFFSEIQCKTKSLLPNTGVYDLSGFTVKPVATVHRRIPDLPDCDIDKWL
NNFNVPSPLNWERKIFSNCNFNLSTLLRLVHTDSFSCNNFDESKIYGSCFKSIVLDKFAIPNSRRSDLQLGSSGFLQSSN
YKIDTTSSSCQLYYSLPAINVTINNYNPSSWNRRYGFNNFNLSSHSVVYSRYCFSVNNTFCPCAKPSFASSCKSHKPPSA
SCPIGTNYRSCESTTVLDHTDWCRCSCLPDPITAYDPRSCSQKKSLVGVGEHCAGFGVDEEKCGVLDGSYNVSCLCSTDA
FLGWSYDTCVSNNRCNIFSNFILNGINSGTTCSNDLLQPNTEVFTDVCVDYDLYGITGQGIFKEVSAVYYNSWQNLLYDS
NGNIIGFKDFVTNKTYNIFPCYAGRVSAAFHQNASSLALLYRNLKCSYVLNNISLTTQPYFDSYLGCVFNADNLTDYSVS
SCALRMGSGFCVDYNSYRFVTFEPFNVSFVNDSIESVGGLYEIKIPTNFTIVGQEEFIQTNSPKVTIDCSLFVCSNYAAC
HDLLSEYGTFCDNINSILDEVNGLLDTTQLHVADTLMQGVTLSSNLNTNLHFDVDNINFKSLVGCLGPHCGSSSRSFFED
LLFDKVKLSDVGFVEAYNNCTGGSEIRDLLCVQSFNGIKVLPPILSESQISGYTTAATVAAMFPPWSAAAGIPFSLNVQY
RINGLGVTMDVLNKNQKLIATAFNNALLSIQNGFSAPNSALAKIQSVVNSNAQALNSLLQQLFNKFGAISSSLQEILSRL
DPPEAQVQIDRLINGRLTALNAYVSQQLSDISLVKFGAALAMEKVNECVKSQSPRINFCGNGNHILSLVQNAPYGLLFMH
FSYKPISFKTVLVSPGLCISGDVGIAPKQGYFIKHNDHWMFTGSSYYYPEPISDKNVVFMNTCSVNFTKAPLVY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VIGDFNCTNFAINDLNTTVPRISEYVVDVSYGLGTYYILDRVYLNTTILFTGYFPKSGANFRDLSLKGTTYLSTLWYQKP
FLSDFNNGIFSRVKNTKLYVNKTLYSEFSTIVIGSVFINNSYTIVVQPHNGVLEITACQYTMCEYPHTICKSKGSSRNES
WHFDKSEPLCLFKKNFTYNVSTDWLYFHFYQERGTFYAYYADSGMPTTFLFSLYLGTLLSHYYVLPLTCNAISSNTDNET
LQYWVTPLSKRQYLLKFDNRGVITNAVDCSSSFFSEIQCKTKSLLPNTGVYDLSGFTVKPVATVHRRIPDLPDCDIDKWL
NNFNVPSPLNWERKIFSNCNFNLSTLLRLVHTDSFSCNNFDESKIYGSCFKSIVLDKFAIPNSRRSDLQLGSSGFLQSSN
YKIDTTSSSCQLYYSLPAINVTINNYNPSSWNRRYGFNNFNLSSHSVVYSRYCFSVNNTFCPCAKPSFASSCKSHKPPSA
SCPIGTNYRSCESTTVLDHTDWCRCSCLPDPITAYDPRSCSQKKSLVGVGEHCAGFGVDEEKCGVLDGSYNVSCLCSTDA
FLGWSYDTCVSNNRCNIFSNFILNGINSGTTCSNDLLQPNTEVFTDVCVDYDLYGITGQGIFKEVSAVYYNSWQNLLYDS
NGNIIGFKDFVTNKTYNIFPCYAGRVSAAFHQNASSLALLYRNLKCSYVLNNISLTTQPYFDSYLGCVFNADNLTDYSVS
SCALRMGSGFCVDYNSYRFVTFEPFNVSFVNDSIESVGGLYEIKIPTNFTIVGQEEFIQTNSPKVTIDCSLFVCSNYAAC
HDLLSEYGTFCDNINSILDEVNGLLDTTQLHVADTLMQGVTLSSNLNTNLHFDVDNINFKSLVGCLGPHCGSSSRSFFED
LLFDKVKLSDVGFVEAYNNCTGGSEIRDLLCVQSFNGIKVLPPILSESQISGYTTAATVAAMFPPWSAAAGIPFSLNVQY
RINGLGVTMDVLNKNQKLIATAFNNALLSIQNGFSAPNSALAKIQSVVNSNAQALNSLLQQLFNKFGAISSSLQEILSRL
DPPEAQVQIDRLINGRLTALNAYVSQQLSDISLVKFGAALAMEKVNECVKSQSPRINFCGNGNHILSLVQNAPYGLLFMH
FSYKPISFKTVLVSPGLCISGDVGIAPKQGYFIKHNDHWMFTGSSYYYPEPISDKNVVFMNTCSVNFTKAPLVY
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
5 
;5-acetamido-8-O-(5-acetamido-9-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranonosyl)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid
;
A1AR1 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    VAL n 
1 2    ILE n 
1 3    GLY n 
1 4    ASP n 
1 5    PHE n 
1 6    ASN n 
1 7    CYS n 
1 8    THR n 
1 9    ASN n 
1 10   PHE n 
1 11   ALA n 
1 12   ILE n 
1 13   ASN n 
1 14   ASP n 
1 15   LEU n 
1 16   ASN n 
1 17   THR n 
1 18   THR n 
1 19   VAL n 
1 20   PRO n 
1 21   ARG n 
1 22   ILE n 
1 23   SER n 
1 24   GLU n 
1 25   TYR n 
1 26   VAL n 
1 27   VAL n 
1 28   ASP n 
1 29   VAL n 
1 30   SER n 
1 31   TYR n 
1 32   GLY n 
1 33   LEU n 
1 34   GLY n 
1 35   THR n 
1 36   TYR n 
1 37   TYR n 
1 38   ILE n 
1 39   LEU n 
1 40   ASP n 
1 41   ARG n 
1 42   VAL n 
1 43   TYR n 
1 44   LEU n 
1 45   ASN n 
1 46   THR n 
1 47   THR n 
1 48   ILE n 
1 49   LEU n 
1 50   PHE n 
1 51   THR n 
1 52   GLY n 
1 53   TYR n 
1 54   PHE n 
1 55   PRO n 
1 56   LYS n 
1 57   SER n 
1 58   GLY n 
1 59   ALA n 
1 60   ASN n 
1 61   PHE n 
1 62   ARG n 
1 63   ASP n 
1 64   LEU n 
1 65   SER n 
1 66   LEU n 
1 67   LYS n 
1 68   GLY n 
1 69   THR n 
1 70   THR n 
1 71   TYR n 
1 72   LEU n 
1 73   SER n 
1 74   THR n 
1 75   LEU n 
1 76   TRP n 
1 77   TYR n 
1 78   GLN n 
1 79   LYS n 
1 80   PRO n 
1 81   PHE n 
1 82   LEU n 
1 83   SER n 
1 84   ASP n 
1 85   PHE n 
1 86   ASN n 
1 87   ASN n 
1 88   GLY n 
1 89   ILE n 
1 90   PHE n 
1 91   SER n 
1 92   ARG n 
1 93   VAL n 
1 94   LYS n 
1 95   ASN n 
1 96   THR n 
1 97   LYS n 
1 98   LEU n 
1 99   TYR n 
1 100  VAL n 
1 101  ASN n 
1 102  LYS n 
1 103  THR n 
1 104  LEU n 
1 105  TYR n 
1 106  SER n 
1 107  GLU n 
1 108  PHE n 
1 109  SER n 
1 110  THR n 
1 111  ILE n 
1 112  VAL n 
1 113  ILE n 
1 114  GLY n 
1 115  SER n 
1 116  VAL n 
1 117  PHE n 
1 118  ILE n 
1 119  ASN n 
1 120  ASN n 
1 121  SER n 
1 122  TYR n 
1 123  THR n 
1 124  ILE n 
1 125  VAL n 
1 126  VAL n 
1 127  GLN n 
1 128  PRO n 
1 129  HIS n 
1 130  ASN n 
1 131  GLY n 
1 132  VAL n 
1 133  LEU n 
1 134  GLU n 
1 135  ILE n 
1 136  THR n 
1 137  ALA n 
1 138  CYS n 
1 139  GLN n 
1 140  TYR n 
1 141  THR n 
1 142  MET n 
1 143  CYS n 
1 144  GLU n 
1 145  TYR n 
1 146  PRO n 
1 147  HIS n 
1 148  THR n 
1 149  ILE n 
1 150  CYS n 
1 151  LYS n 
1 152  SER n 
1 153  LYS n 
1 154  GLY n 
1 155  SER n 
1 156  SER n 
1 157  ARG n 
1 158  ASN n 
1 159  GLU n 
1 160  SER n 
1 161  TRP n 
1 162  HIS n 
1 163  PHE n 
1 164  ASP n 
1 165  LYS n 
1 166  SER n 
1 167  GLU n 
1 168  PRO n 
1 169  LEU n 
1 170  CYS n 
1 171  LEU n 
1 172  PHE n 
1 173  LYS n 
1 174  LYS n 
1 175  ASN n 
1 176  PHE n 
1 177  THR n 
1 178  TYR n 
1 179  ASN n 
1 180  VAL n 
1 181  SER n 
1 182  THR n 
1 183  ASP n 
1 184  TRP n 
1 185  LEU n 
1 186  TYR n 
1 187  PHE n 
1 188  HIS n 
1 189  PHE n 
1 190  TYR n 
1 191  GLN n 
1 192  GLU n 
1 193  ARG n 
1 194  GLY n 
1 195  THR n 
1 196  PHE n 
1 197  TYR n 
1 198  ALA n 
1 199  TYR n 
1 200  TYR n 
1 201  ALA n 
1 202  ASP n 
1 203  SER n 
1 204  GLY n 
1 205  MET n 
1 206  PRO n 
1 207  THR n 
1 208  THR n 
1 209  PHE n 
1 210  LEU n 
1 211  PHE n 
1 212  SER n 
1 213  LEU n 
1 214  TYR n 
1 215  LEU n 
1 216  GLY n 
1 217  THR n 
1 218  LEU n 
1 219  LEU n 
1 220  SER n 
1 221  HIS n 
1 222  TYR n 
1 223  TYR n 
1 224  VAL n 
1 225  LEU n 
1 226  PRO n 
1 227  LEU n 
1 228  THR n 
1 229  CYS n 
1 230  ASN n 
1 231  ALA n 
1 232  ILE n 
1 233  SER n 
1 234  SER n 
1 235  ASN n 
1 236  THR n 
1 237  ASP n 
1 238  ASN n 
1 239  GLU n 
1 240  THR n 
1 241  LEU n 
1 242  GLN n 
1 243  TYR n 
1 244  TRP n 
1 245  VAL n 
1 246  THR n 
1 247  PRO n 
1 248  LEU n 
1 249  SER n 
1 250  LYS n 
1 251  ARG n 
1 252  GLN n 
1 253  TYR n 
1 254  LEU n 
1 255  LEU n 
1 256  LYS n 
1 257  PHE n 
1 258  ASP n 
1 259  ASN n 
1 260  ARG n 
1 261  GLY n 
1 262  VAL n 
1 263  ILE n 
1 264  THR n 
1 265  ASN n 
1 266  ALA n 
1 267  VAL n 
1 268  ASP n 
1 269  CYS n 
1 270  SER n 
1 271  SER n 
1 272  SER n 
1 273  PHE n 
1 274  PHE n 
1 275  SER n 
1 276  GLU n 
1 277  ILE n 
1 278  GLN n 
1 279  CYS n 
1 280  LYS n 
1 281  THR n 
1 282  LYS n 
1 283  SER n 
1 284  LEU n 
1 285  LEU n 
1 286  PRO n 
1 287  ASN n 
1 288  THR n 
1 289  GLY n 
1 290  VAL n 
1 291  TYR n 
1 292  ASP n 
1 293  LEU n 
1 294  SER n 
1 295  GLY n 
1 296  PHE n 
1 297  THR n 
1 298  VAL n 
1 299  LYS n 
1 300  PRO n 
1 301  VAL n 
1 302  ALA n 
1 303  THR n 
1 304  VAL n 
1 305  HIS n 
1 306  ARG n 
1 307  ARG n 
1 308  ILE n 
1 309  PRO n 
1 310  ASP n 
1 311  LEU n 
1 312  PRO n 
1 313  ASP n 
1 314  CYS n 
1 315  ASP n 
1 316  ILE n 
1 317  ASP n 
1 318  LYS n 
1 319  TRP n 
1 320  LEU n 
1 321  ASN n 
1 322  ASN n 
1 323  PHE n 
1 324  ASN n 
1 325  VAL n 
1 326  PRO n 
1 327  SER n 
1 328  PRO n 
1 329  LEU n 
1 330  ASN n 
1 331  TRP n 
1 332  GLU n 
1 333  ARG n 
1 334  LYS n 
1 335  ILE n 
1 336  PHE n 
1 337  SER n 
1 338  ASN n 
1 339  CYS n 
1 340  ASN n 
1 341  PHE n 
1 342  ASN n 
1 343  LEU n 
1 344  SER n 
1 345  THR n 
1 346  LEU n 
1 347  LEU n 
1 348  ARG n 
1 349  LEU n 
1 350  VAL n 
1 351  HIS n 
1 352  THR n 
1 353  ASP n 
1 354  SER n 
1 355  PHE n 
1 356  SER n 
1 357  CYS n 
1 358  ASN n 
1 359  ASN n 
1 360  PHE n 
1 361  ASP n 
1 362  GLU n 
1 363  SER n 
1 364  LYS n 
1 365  ILE n 
1 366  TYR n 
1 367  GLY n 
1 368  SER n 
1 369  CYS n 
1 370  PHE n 
1 371  LYS n 
1 372  SER n 
1 373  ILE n 
1 374  VAL n 
1 375  LEU n 
1 376  ASP n 
1 377  LYS n 
1 378  PHE n 
1 379  ALA n 
1 380  ILE n 
1 381  PRO n 
1 382  ASN n 
1 383  SER n 
1 384  ARG n 
1 385  ARG n 
1 386  SER n 
1 387  ASP n 
1 388  LEU n 
1 389  GLN n 
1 390  LEU n 
1 391  GLY n 
1 392  SER n 
1 393  SER n 
1 394  GLY n 
1 395  PHE n 
1 396  LEU n 
1 397  GLN n 
1 398  SER n 
1 399  SER n 
1 400  ASN n 
1 401  TYR n 
1 402  LYS n 
1 403  ILE n 
1 404  ASP n 
1 405  THR n 
1 406  THR n 
1 407  SER n 
1 408  SER n 
1 409  SER n 
1 410  CYS n 
1 411  GLN n 
1 412  LEU n 
1 413  TYR n 
1 414  TYR n 
1 415  SER n 
1 416  LEU n 
1 417  PRO n 
1 418  ALA n 
1 419  ILE n 
1 420  ASN n 
1 421  VAL n 
1 422  THR n 
1 423  ILE n 
1 424  ASN n 
1 425  ASN n 
1 426  TYR n 
1 427  ASN n 
1 428  PRO n 
1 429  SER n 
1 430  SER n 
1 431  TRP n 
1 432  ASN n 
1 433  ARG n 
1 434  ARG n 
1 435  TYR n 
1 436  GLY n 
1 437  PHE n 
1 438  ASN n 
1 439  ASN n 
1 440  PHE n 
1 441  ASN n 
1 442  LEU n 
1 443  SER n 
1 444  SER n 
1 445  HIS n 
1 446  SER n 
1 447  VAL n 
1 448  VAL n 
1 449  TYR n 
1 450  SER n 
1 451  ARG n 
1 452  TYR n 
1 453  CYS n 
1 454  PHE n 
1 455  SER n 
1 456  VAL n 
1 457  ASN n 
1 458  ASN n 
1 459  THR n 
1 460  PHE n 
1 461  CYS n 
1 462  PRO n 
1 463  CYS n 
1 464  ALA n 
1 465  LYS n 
1 466  PRO n 
1 467  SER n 
1 468  PHE n 
1 469  ALA n 
1 470  SER n 
1 471  SER n 
1 472  CYS n 
1 473  LYS n 
1 474  SER n 
1 475  HIS n 
1 476  LYS n 
1 477  PRO n 
1 478  PRO n 
1 479  SER n 
1 480  ALA n 
1 481  SER n 
1 482  CYS n 
1 483  PRO n 
1 484  ILE n 
1 485  GLY n 
1 486  THR n 
1 487  ASN n 
1 488  TYR n 
1 489  ARG n 
1 490  SER n 
1 491  CYS n 
1 492  GLU n 
1 493  SER n 
1 494  THR n 
1 495  THR n 
1 496  VAL n 
1 497  LEU n 
1 498  ASP n 
1 499  HIS n 
1 500  THR n 
1 501  ASP n 
1 502  TRP n 
1 503  CYS n 
1 504  ARG n 
1 505  CYS n 
1 506  SER n 
1 507  CYS n 
1 508  LEU n 
1 509  PRO n 
1 510  ASP n 
1 511  PRO n 
1 512  ILE n 
1 513  THR n 
1 514  ALA n 
1 515  TYR n 
1 516  ASP n 
1 517  PRO n 
1 518  ARG n 
1 519  SER n 
1 520  CYS n 
1 521  SER n 
1 522  GLN n 
1 523  LYS n 
1 524  LYS n 
1 525  SER n 
1 526  LEU n 
1 527  VAL n 
1 528  GLY n 
1 529  VAL n 
1 530  GLY n 
1 531  GLU n 
1 532  HIS n 
1 533  CYS n 
1 534  ALA n 
1 535  GLY n 
1 536  PHE n 
1 537  GLY n 
1 538  VAL n 
1 539  ASP n 
1 540  GLU n 
1 541  GLU n 
1 542  LYS n 
1 543  CYS n 
1 544  GLY n 
1 545  VAL n 
1 546  LEU n 
1 547  ASP n 
1 548  GLY n 
1 549  SER n 
1 550  TYR n 
1 551  ASN n 
1 552  VAL n 
1 553  SER n 
1 554  CYS n 
1 555  LEU n 
1 556  CYS n 
1 557  SER n 
1 558  THR n 
1 559  ASP n 
1 560  ALA n 
1 561  PHE n 
1 562  LEU n 
1 563  GLY n 
1 564  TRP n 
1 565  SER n 
1 566  TYR n 
1 567  ASP n 
1 568  THR n 
1 569  CYS n 
1 570  VAL n 
1 571  SER n 
1 572  ASN n 
1 573  ASN n 
1 574  ARG n 
1 575  CYS n 
1 576  ASN n 
1 577  ILE n 
1 578  PHE n 
1 579  SER n 
1 580  ASN n 
1 581  PHE n 
1 582  ILE n 
1 583  LEU n 
1 584  ASN n 
1 585  GLY n 
1 586  ILE n 
1 587  ASN n 
1 588  SER n 
1 589  GLY n 
1 590  THR n 
1 591  THR n 
1 592  CYS n 
1 593  SER n 
1 594  ASN n 
1 595  ASP n 
1 596  LEU n 
1 597  LEU n 
1 598  GLN n 
1 599  PRO n 
1 600  ASN n 
1 601  THR n 
1 602  GLU n 
1 603  VAL n 
1 604  PHE n 
1 605  THR n 
1 606  ASP n 
1 607  VAL n 
1 608  CYS n 
1 609  VAL n 
1 610  ASP n 
1 611  TYR n 
1 612  ASP n 
1 613  LEU n 
1 614  TYR n 
1 615  GLY n 
1 616  ILE n 
1 617  THR n 
1 618  GLY n 
1 619  GLN n 
1 620  GLY n 
1 621  ILE n 
1 622  PHE n 
1 623  LYS n 
1 624  GLU n 
1 625  VAL n 
1 626  SER n 
1 627  ALA n 
1 628  VAL n 
1 629  TYR n 
1 630  TYR n 
1 631  ASN n 
1 632  SER n 
1 633  TRP n 
1 634  GLN n 
1 635  ASN n 
1 636  LEU n 
1 637  LEU n 
1 638  TYR n 
1 639  ASP n 
1 640  SER n 
1 641  ASN n 
1 642  GLY n 
1 643  ASN n 
1 644  ILE n 
1 645  ILE n 
1 646  GLY n 
1 647  PHE n 
1 648  LYS n 
1 649  ASP n 
1 650  PHE n 
1 651  VAL n 
1 652  THR n 
1 653  ASN n 
1 654  LYS n 
1 655  THR n 
1 656  TYR n 
1 657  ASN n 
1 658  ILE n 
1 659  PHE n 
1 660  PRO n 
1 661  CYS n 
1 662  TYR n 
1 663  ALA n 
1 664  GLY n 
1 665  ARG n 
1 666  VAL n 
1 667  SER n 
1 668  ALA n 
1 669  ALA n 
1 670  PHE n 
1 671  HIS n 
1 672  GLN n 
1 673  ASN n 
1 674  ALA n 
1 675  SER n 
1 676  SER n 
1 677  LEU n 
1 678  ALA n 
1 679  LEU n 
1 680  LEU n 
1 681  TYR n 
1 682  ARG n 
1 683  ASN n 
1 684  LEU n 
1 685  LYS n 
1 686  CYS n 
1 687  SER n 
1 688  TYR n 
1 689  VAL n 
1 690  LEU n 
1 691  ASN n 
1 692  ASN n 
1 693  ILE n 
1 694  SER n 
1 695  LEU n 
1 696  THR n 
1 697  THR n 
1 698  GLN n 
1 699  PRO n 
1 700  TYR n 
1 701  PHE n 
1 702  ASP n 
1 703  SER n 
1 704  TYR n 
1 705  LEU n 
1 706  GLY n 
1 707  CYS n 
1 708  VAL n 
1 709  PHE n 
1 710  ASN n 
1 711  ALA n 
1 712  ASP n 
1 713  ASN n 
1 714  LEU n 
1 715  THR n 
1 716  ASP n 
1 717  TYR n 
1 718  SER n 
1 719  VAL n 
1 720  SER n 
1 721  SER n 
1 722  CYS n 
1 723  ALA n 
1 724  LEU n 
1 725  ARG n 
1 726  MET n 
1 727  GLY n 
1 728  SER n 
1 729  GLY n 
1 730  PHE n 
1 731  CYS n 
1 732  VAL n 
1 733  ASP n 
1 734  TYR n 
1 735  ASN n 
1 736  SER n 
1 737  TYR n 
1 738  ARG n 
1 739  PHE n 
1 740  VAL n 
1 741  THR n 
1 742  PHE n 
1 743  GLU n 
1 744  PRO n 
1 745  PHE n 
1 746  ASN n 
1 747  VAL n 
1 748  SER n 
1 749  PHE n 
1 750  VAL n 
1 751  ASN n 
1 752  ASP n 
1 753  SER n 
1 754  ILE n 
1 755  GLU n 
1 756  SER n 
1 757  VAL n 
1 758  GLY n 
1 759  GLY n 
1 760  LEU n 
1 761  TYR n 
1 762  GLU n 
1 763  ILE n 
1 764  LYS n 
1 765  ILE n 
1 766  PRO n 
1 767  THR n 
1 768  ASN n 
1 769  PHE n 
1 770  THR n 
1 771  ILE n 
1 772  VAL n 
1 773  GLY n 
1 774  GLN n 
1 775  GLU n 
1 776  GLU n 
1 777  PHE n 
1 778  ILE n 
1 779  GLN n 
1 780  THR n 
1 781  ASN n 
1 782  SER n 
1 783  PRO n 
1 784  LYS n 
1 785  VAL n 
1 786  THR n 
1 787  ILE n 
1 788  ASP n 
1 789  CYS n 
1 790  SER n 
1 791  LEU n 
1 792  PHE n 
1 793  VAL n 
1 794  CYS n 
1 795  SER n 
1 796  ASN n 
1 797  TYR n 
1 798  ALA n 
1 799  ALA n 
1 800  CYS n 
1 801  HIS n 
1 802  ASP n 
1 803  LEU n 
1 804  LEU n 
1 805  SER n 
1 806  GLU n 
1 807  TYR n 
1 808  GLY n 
1 809  THR n 
1 810  PHE n 
1 811  CYS n 
1 812  ASP n 
1 813  ASN n 
1 814  ILE n 
1 815  ASN n 
1 816  SER n 
1 817  ILE n 
1 818  LEU n 
1 819  ASP n 
1 820  GLU n 
1 821  VAL n 
1 822  ASN n 
1 823  GLY n 
1 824  LEU n 
1 825  LEU n 
1 826  ASP n 
1 827  THR n 
1 828  THR n 
1 829  GLN n 
1 830  LEU n 
1 831  HIS n 
1 832  VAL n 
1 833  ALA n 
1 834  ASP n 
1 835  THR n 
1 836  LEU n 
1 837  MET n 
1 838  GLN n 
1 839  GLY n 
1 840  VAL n 
1 841  THR n 
1 842  LEU n 
1 843  SER n 
1 844  SER n 
1 845  ASN n 
1 846  LEU n 
1 847  ASN n 
1 848  THR n 
1 849  ASN n 
1 850  LEU n 
1 851  HIS n 
1 852  PHE n 
1 853  ASP n 
1 854  VAL n 
1 855  ASP n 
1 856  ASN n 
1 857  ILE n 
1 858  ASN n 
1 859  PHE n 
1 860  LYS n 
1 861  SER n 
1 862  LEU n 
1 863  VAL n 
1 864  GLY n 
1 865  CYS n 
1 866  LEU n 
1 867  GLY n 
1 868  PRO n 
1 869  HIS n 
1 870  CYS n 
1 871  GLY n 
1 872  SER n 
1 873  SER n 
1 874  SER n 
1 875  ARG n 
1 876  SER n 
1 877  PHE n 
1 878  PHE n 
1 879  GLU n 
1 880  ASP n 
1 881  LEU n 
1 882  LEU n 
1 883  PHE n 
1 884  ASP n 
1 885  LYS n 
1 886  VAL n 
1 887  LYS n 
1 888  LEU n 
1 889  SER n 
1 890  ASP n 
1 891  VAL n 
1 892  GLY n 
1 893  PHE n 
1 894  VAL n 
1 895  GLU n 
1 896  ALA n 
1 897  TYR n 
1 898  ASN n 
1 899  ASN n 
1 900  CYS n 
1 901  THR n 
1 902  GLY n 
1 903  GLY n 
1 904  SER n 
1 905  GLU n 
1 906  ILE n 
1 907  ARG n 
1 908  ASP n 
1 909  LEU n 
1 910  LEU n 
1 911  CYS n 
1 912  VAL n 
1 913  GLN n 
1 914  SER n 
1 915  PHE n 
1 916  ASN n 
1 917  GLY n 
1 918  ILE n 
1 919  LYS n 
1 920  VAL n 
1 921  LEU n 
1 922  PRO n 
1 923  PRO n 
1 924  ILE n 
1 925  LEU n 
1 926  SER n 
1 927  GLU n 
1 928  SER n 
1 929  GLN n 
1 930  ILE n 
1 931  SER n 
1 932  GLY n 
1 933  TYR n 
1 934  THR n 
1 935  THR n 
1 936  ALA n 
1 937  ALA n 
1 938  THR n 
1 939  VAL n 
1 940  ALA n 
1 941  ALA n 
1 942  MET n 
1 943  PHE n 
1 944  PRO n 
1 945  PRO n 
1 946  TRP n 
1 947  SER n 
1 948  ALA n 
1 949  ALA n 
1 950  ALA n 
1 951  GLY n 
1 952  ILE n 
1 953  PRO n 
1 954  PHE n 
1 955  SER n 
1 956  LEU n 
1 957  ASN n 
1 958  VAL n 
1 959  GLN n 
1 960  TYR n 
1 961  ARG n 
1 962  ILE n 
1 963  ASN n 
1 964  GLY n 
1 965  LEU n 
1 966  GLY n 
1 967  VAL n 
1 968  THR n 
1 969  MET n 
1 970  ASP n 
1 971  VAL n 
1 972  LEU n 
1 973  ASN n 
1 974  LYS n 
1 975  ASN n 
1 976  GLN n 
1 977  LYS n 
1 978  LEU n 
1 979  ILE n 
1 980  ALA n 
1 981  THR n 
1 982  ALA n 
1 983  PHE n 
1 984  ASN n 
1 985  ASN n 
1 986  ALA n 
1 987  LEU n 
1 988  LEU n 
1 989  SER n 
1 990  ILE n 
1 991  GLN n 
1 992  ASN n 
1 993  GLY n 
1 994  PHE n 
1 995  SER n 
1 996  ALA n 
1 997  PRO n 
1 998  ASN n 
1 999  SER n 
1 1000 ALA n 
1 1001 LEU n 
1 1002 ALA n 
1 1003 LYS n 
1 1004 ILE n 
1 1005 GLN n 
1 1006 SER n 
1 1007 VAL n 
1 1008 VAL n 
1 1009 ASN n 
1 1010 SER n 
1 1011 ASN n 
1 1012 ALA n 
1 1013 GLN n 
1 1014 ALA n 
1 1015 LEU n 
1 1016 ASN n 
1 1017 SER n 
1 1018 LEU n 
1 1019 LEU n 
1 1020 GLN n 
1 1021 GLN n 
1 1022 LEU n 
1 1023 PHE n 
1 1024 ASN n 
1 1025 LYS n 
1 1026 PHE n 
1 1027 GLY n 
1 1028 ALA n 
1 1029 ILE n 
1 1030 SER n 
1 1031 SER n 
1 1032 SER n 
1 1033 LEU n 
1 1034 GLN n 
1 1035 GLU n 
1 1036 ILE n 
1 1037 LEU n 
1 1038 SER n 
1 1039 ARG n 
1 1040 LEU n 
1 1041 ASP n 
1 1042 PRO n 
1 1043 PRO n 
1 1044 GLU n 
1 1045 ALA n 
1 1046 GLN n 
1 1047 VAL n 
1 1048 GLN n 
1 1049 ILE n 
1 1050 ASP n 
1 1051 ARG n 
1 1052 LEU n 
1 1053 ILE n 
1 1054 ASN n 
1 1055 GLY n 
1 1056 ARG n 
1 1057 LEU n 
1 1058 THR n 
1 1059 ALA n 
1 1060 LEU n 
1 1061 ASN n 
1 1062 ALA n 
1 1063 TYR n 
1 1064 VAL n 
1 1065 SER n 
1 1066 GLN n 
1 1067 GLN n 
1 1068 LEU n 
1 1069 SER n 
1 1070 ASP n 
1 1071 ILE n 
1 1072 SER n 
1 1073 LEU n 
1 1074 VAL n 
1 1075 LYS n 
1 1076 PHE n 
1 1077 GLY n 
1 1078 ALA n 
1 1079 ALA n 
1 1080 LEU n 
1 1081 ALA n 
1 1082 MET n 
1 1083 GLU n 
1 1084 LYS n 
1 1085 VAL n 
1 1086 ASN n 
1 1087 GLU n 
1 1088 CYS n 
1 1089 VAL n 
1 1090 LYS n 
1 1091 SER n 
1 1092 GLN n 
1 1093 SER n 
1 1094 PRO n 
1 1095 ARG n 
1 1096 ILE n 
1 1097 ASN n 
1 1098 PHE n 
1 1099 CYS n 
1 1100 GLY n 
1 1101 ASN n 
1 1102 GLY n 
1 1103 ASN n 
1 1104 HIS n 
1 1105 ILE n 
1 1106 LEU n 
1 1107 SER n 
1 1108 LEU n 
1 1109 VAL n 
1 1110 GLN n 
1 1111 ASN n 
1 1112 ALA n 
1 1113 PRO n 
1 1114 TYR n 
1 1115 GLY n 
1 1116 LEU n 
1 1117 LEU n 
1 1118 PHE n 
1 1119 MET n 
1 1120 HIS n 
1 1121 PHE n 
1 1122 SER n 
1 1123 TYR n 
1 1124 LYS n 
1 1125 PRO n 
1 1126 ILE n 
1 1127 SER n 
1 1128 PHE n 
1 1129 LYS n 
1 1130 THR n 
1 1131 VAL n 
1 1132 LEU n 
1 1133 VAL n 
1 1134 SER n 
1 1135 PRO n 
1 1136 GLY n 
1 1137 LEU n 
1 1138 CYS n 
1 1139 ILE n 
1 1140 SER n 
1 1141 GLY n 
1 1142 ASP n 
1 1143 VAL n 
1 1144 GLY n 
1 1145 ILE n 
1 1146 ALA n 
1 1147 PRO n 
1 1148 LYS n 
1 1149 GLN n 
1 1150 GLY n 
1 1151 TYR n 
1 1152 PHE n 
1 1153 ILE n 
1 1154 LYS n 
1 1155 HIS n 
1 1156 ASN n 
1 1157 ASP n 
1 1158 HIS n 
1 1159 TRP n 
1 1160 MET n 
1 1161 PHE n 
1 1162 THR n 
1 1163 GLY n 
1 1164 SER n 
1 1165 SER n 
1 1166 TYR n 
1 1167 TYR n 
1 1168 TYR n 
1 1169 PRO n 
1 1170 GLU n 
1 1171 PRO n 
1 1172 ILE n 
1 1173 SER n 
1 1174 ASP n 
1 1175 LYS n 
1 1176 ASN n 
1 1177 VAL n 
1 1178 VAL n 
1 1179 PHE n 
1 1180 MET n 
1 1181 ASN n 
1 1182 THR n 
1 1183 CYS n 
1 1184 SER n 
1 1185 VAL n 
1 1186 ASN n 
1 1187 PHE n 
1 1188 THR n 
1 1189 LYS n 
1 1190 ALA n 
1 1191 PRO n 
1 1192 LEU n 
1 1193 VAL n 
1 1194 TYR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1194 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'S, 3' 
_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      'Human coronavirus HKU1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     290028 
_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               human 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH'                                                   
'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1' WURCS PDB2Glycan 
1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}'    LINUCS PDB-CARE   
?     
4 3 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                                  
'Glycam Condensed Sequence' GMML       1.0   
5 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                                       WURCS PDB2Glycan 
1.1.0 
6 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                             LINUCS PDB-CARE   
?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 2 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
4 2 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
5 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
# 
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 
A1AR1 non-polymer                   . 
;5-acetamido-8-O-(5-acetamido-9-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranonosyl)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosonic acid
;
? 'C24 H38 N2 O18' 642.561 
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 
BMA   'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
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 
MAN   'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
MET   'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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    VAL 1    14   14  VAL VAL A . n 
A 1 2    ILE 2    15   15  ILE ILE A . n 
A 1 3    GLY 3    16   16  GLY GLY A . n 
A 1 4    ASP 4    17   17  ASP ASP A . n 
A 1 5    PHE 5    18   18  PHE PHE A . n 
A 1 6    ASN 6    19   19  ASN ASN A . n 
A 1 7    CYS 7    20   20  CYS CYS A . n 
A 1 8    THR 8    21   21  THR THR A . n 
A 1 9    ASN 9    22   22  ASN ASN A . n 
A 1 10   PHE 10   23   23  PHE PHE A . n 
A 1 11   ALA 11   24   24  ALA ALA A . n 
A 1 12   ILE 12   25   25  ILE ILE A . n 
A 1 13   ASN 13   26   26  ASN ASN A . n 
A 1 14   ASP 14   27   27  ASP ASP A . n 
A 1 15   LEU 15   28   28  LEU LEU A . n 
A 1 16   ASN 16   29   29  ASN ASN A . n 
A 1 17   THR 17   30   30  THR THR A . n 
A 1 18   THR 18   31   31  THR THR A . n 
A 1 19   VAL 19   32   32  VAL VAL A . n 
A 1 20   PRO 20   33   33  PRO PRO A . n 
A 1 21   ARG 21   34   34  ARG ARG A . n 
A 1 22   ILE 22   35   35  ILE ILE A . n 
A 1 23   SER 23   36   36  SER SER A . n 
A 1 24   GLU 24   37   37  GLU GLU A . n 
A 1 25   TYR 25   38   38  TYR TYR A . n 
A 1 26   VAL 26   39   39  VAL VAL A . n 
A 1 27   VAL 27   40   40  VAL VAL A . n 
A 1 28   ASP 28   41   41  ASP ASP A . n 
A 1 29   VAL 29   42   42  VAL VAL A . n 
A 1 30   SER 30   43   43  SER SER A . n 
A 1 31   TYR 31   44   44  TYR TYR A . n 
A 1 32   GLY 32   45   45  GLY GLY A . n 
A 1 33   LEU 33   46   46  LEU LEU A . n 
A 1 34   GLY 34   47   47  GLY GLY A . n 
A 1 35   THR 35   48   48  THR THR A . n 
A 1 36   TYR 36   49   49  TYR TYR A . n 
A 1 37   TYR 37   50   50  TYR TYR A . n 
A 1 38   ILE 38   51   51  ILE ILE A . n 
A 1 39   LEU 39   52   52  LEU LEU A . n 
A 1 40   ASP 40   53   53  ASP ASP A . n 
A 1 41   ARG 41   54   54  ARG ARG A . n 
A 1 42   VAL 42   55   55  VAL VAL A . n 
A 1 43   TYR 43   56   56  TYR TYR A . n 
A 1 44   LEU 44   57   57  LEU LEU A . n 
A 1 45   ASN 45   58   58  ASN ASN A . n 
A 1 46   THR 46   59   59  THR THR A . n 
A 1 47   THR 47   60   60  THR THR A . n 
A 1 48   ILE 48   61   61  ILE ILE A . n 
A 1 49   LEU 49   62   62  LEU LEU A . n 
A 1 50   PHE 50   63   63  PHE PHE A . n 
A 1 51   THR 51   64   64  THR THR A . n 
A 1 52   GLY 52   65   65  GLY GLY A . n 
A 1 53   TYR 53   66   66  TYR TYR A . n 
A 1 54   PHE 54   67   67  PHE PHE A . n 
A 1 55   PRO 55   68   68  PRO PRO A . n 
A 1 56   LYS 56   69   69  LYS LYS A . n 
A 1 57   SER 57   70   70  SER SER A . n 
A 1 58   GLY 58   71   71  GLY GLY A . n 
A 1 59   ALA 59   72   72  ALA ALA A . n 
A 1 60   ASN 60   73   73  ASN ASN A . n 
A 1 61   PHE 61   74   74  PHE PHE A . n 
A 1 62   ARG 62   75   75  ARG ARG A . n 
A 1 63   ASP 63   76   76  ASP ASP A . n 
A 1 64   LEU 64   77   77  LEU LEU A . n 
A 1 65   SER 65   78   78  SER SER A . n 
A 1 66   LEU 66   79   79  LEU LEU A . n 
A 1 67   LYS 67   80   80  LYS LYS A . n 
A 1 68   GLY 68   81   81  GLY GLY A . n 
A 1 69   THR 69   82   82  THR THR A . n 
A 1 70   THR 70   83   83  THR THR A . n 
A 1 71   TYR 71   84   84  TYR TYR A . n 
A 1 72   LEU 72   85   85  LEU LEU A . n 
A 1 73   SER 73   86   86  SER SER A . n 
A 1 74   THR 74   87   87  THR THR A . n 
A 1 75   LEU 75   88   88  LEU LEU A . n 
A 1 76   TRP 76   89   89  TRP TRP A . n 
A 1 77   TYR 77   90   90  TYR TYR A . n 
A 1 78   GLN 78   91   91  GLN GLN A . n 
A 1 79   LYS 79   92   92  LYS LYS A . n 
A 1 80   PRO 80   93   93  PRO PRO A . n 
A 1 81   PHE 81   94   94  PHE PHE A . n 
A 1 82   LEU 82   95   95  LEU LEU A . n 
A 1 83   SER 83   96   96  SER SER A . n 
A 1 84   ASP 84   97   97  ASP ASP A . n 
A 1 85   PHE 85   98   98  PHE PHE A . n 
A 1 86   ASN 86   99   99  ASN ASN A . n 
A 1 87   ASN 87   100  100 ASN ASN A . n 
A 1 88   GLY 88   101  101 GLY GLY A . n 
A 1 89   ILE 89   102  102 ILE ILE A . n 
A 1 90   PHE 90   103  103 PHE PHE A . n 
A 1 91   SER 91   104  104 SER SER A . n 
A 1 92   ARG 92   105  105 ARG ARG A . n 
A 1 93   VAL 93   106  106 VAL VAL A . n 
A 1 94   LYS 94   107  107 LYS LYS A . n 
A 1 95   ASN 95   108  108 ASN ASN A . n 
A 1 96   THR 96   109  109 THR THR A . n 
A 1 97   LYS 97   110  110 LYS LYS A . n 
A 1 98   LEU 98   111  111 LEU LEU A . n 
A 1 99   TYR 99   112  112 TYR TYR A . n 
A 1 100  VAL 100  113  113 VAL VAL A . n 
A 1 101  ASN 101  114  114 ASN ASN A . n 
A 1 102  LYS 102  115  115 LYS LYS A . n 
A 1 103  THR 103  116  116 THR THR A . n 
A 1 104  LEU 104  117  117 LEU LEU A . n 
A 1 105  TYR 105  118  118 TYR TYR A . n 
A 1 106  SER 106  119  119 SER SER A . n 
A 1 107  GLU 107  120  120 GLU GLU A . n 
A 1 108  PHE 108  121  121 PHE PHE A . n 
A 1 109  SER 109  122  122 SER SER A . n 
A 1 110  THR 110  123  123 THR THR A . n 
A 1 111  ILE 111  124  124 ILE ILE A . n 
A 1 112  VAL 112  125  125 VAL VAL A . n 
A 1 113  ILE 113  126  126 ILE ILE A . n 
A 1 114  GLY 114  127  127 GLY GLY A . n 
A 1 115  SER 115  128  128 SER SER A . n 
A 1 116  VAL 116  129  129 VAL VAL A . n 
A 1 117  PHE 117  130  130 PHE PHE A . n 
A 1 118  ILE 118  131  131 ILE ILE A . n 
A 1 119  ASN 119  132  132 ASN ASN A . n 
A 1 120  ASN 120  133  133 ASN ASN A . n 
A 1 121  SER 121  134  134 SER SER A . n 
A 1 122  TYR 122  135  135 TYR TYR A . n 
A 1 123  THR 123  136  136 THR THR A . n 
A 1 124  ILE 124  137  137 ILE ILE A . n 
A 1 125  VAL 125  138  138 VAL VAL A . n 
A 1 126  VAL 126  139  139 VAL VAL A . n 
A 1 127  GLN 127  140  140 GLN GLN A . n 
A 1 128  PRO 128  141  141 PRO PRO A . n 
A 1 129  HIS 129  142  142 HIS HIS A . n 
A 1 130  ASN 130  143  143 ASN ASN A . n 
A 1 131  GLY 131  144  144 GLY GLY A . n 
A 1 132  VAL 132  145  145 VAL VAL A . n 
A 1 133  LEU 133  146  146 LEU LEU A . n 
A 1 134  GLU 134  147  147 GLU GLU A . n 
A 1 135  ILE 135  148  148 ILE ILE A . n 
A 1 136  THR 136  149  149 THR THR A . n 
A 1 137  ALA 137  150  150 ALA ALA A . n 
A 1 138  CYS 138  151  151 CYS CYS A . n 
A 1 139  GLN 139  152  152 GLN GLN A . n 
A 1 140  TYR 140  153  153 TYR TYR A . n 
A 1 141  THR 141  154  154 THR THR A . n 
A 1 142  MET 142  155  155 MET MET A . n 
A 1 143  CYS 143  156  156 CYS CYS A . n 
A 1 144  GLU 144  157  157 GLU GLU A . n 
A 1 145  TYR 145  158  158 TYR TYR A . n 
A 1 146  PRO 146  159  159 PRO PRO A . n 
A 1 147  HIS 147  160  160 HIS HIS A . n 
A 1 148  THR 148  161  161 THR THR A . n 
A 1 149  ILE 149  162  162 ILE ILE A . n 
A 1 150  CYS 150  163  163 CYS CYS A . n 
A 1 151  LYS 151  164  164 LYS LYS A . n 
A 1 152  SER 152  165  165 SER SER A . n 
A 1 153  LYS 153  166  166 LYS LYS A . n 
A 1 154  GLY 154  167  167 GLY GLY A . n 
A 1 155  SER 155  168  168 SER SER A . n 
A 1 156  SER 156  169  169 SER SER A . n 
A 1 157  ARG 157  170  170 ARG ARG A . n 
A 1 158  ASN 158  171  171 ASN ASN A . n 
A 1 159  GLU 159  172  172 GLU GLU A . n 
A 1 160  SER 160  173  173 SER SER A . n 
A 1 161  TRP 161  174  174 TRP TRP A . n 
A 1 162  HIS 162  175  175 HIS HIS A . n 
A 1 163  PHE 163  176  176 PHE PHE A . n 
A 1 164  ASP 164  177  177 ASP ASP A . n 
A 1 165  LYS 165  178  178 LYS LYS A . n 
A 1 166  SER 166  179  179 SER SER A . n 
A 1 167  GLU 167  180  180 GLU GLU A . n 
A 1 168  PRO 168  181  181 PRO PRO A . n 
A 1 169  LEU 169  182  182 LEU LEU A . n 
A 1 170  CYS 170  183  183 CYS CYS A . n 
A 1 171  LEU 171  184  184 LEU LEU A . n 
A 1 172  PHE 172  185  185 PHE PHE A . n 
A 1 173  LYS 173  186  186 LYS LYS A . n 
A 1 174  LYS 174  187  187 LYS LYS A . n 
A 1 175  ASN 175  188  188 ASN ASN A . n 
A 1 176  PHE 176  189  189 PHE PHE A . n 
A 1 177  THR 177  190  190 THR THR A . n 
A 1 178  TYR 178  191  191 TYR TYR A . n 
A 1 179  ASN 179  192  192 ASN ASN A . n 
A 1 180  VAL 180  193  193 VAL VAL A . n 
A 1 181  SER 181  194  194 SER SER A . n 
A 1 182  THR 182  195  195 THR THR A . n 
A 1 183  ASP 183  196  196 ASP ASP A . n 
A 1 184  TRP 184  197  197 TRP TRP A . n 
A 1 185  LEU 185  198  198 LEU LEU A . n 
A 1 186  TYR 186  199  199 TYR TYR A . n 
A 1 187  PHE 187  200  200 PHE PHE A . n 
A 1 188  HIS 188  201  201 HIS HIS A . n 
A 1 189  PHE 189  202  202 PHE PHE A . n 
A 1 190  TYR 190  203  203 TYR TYR A . n 
A 1 191  GLN 191  204  204 GLN GLN A . n 
A 1 192  GLU 192  205  205 GLU GLU A . n 
A 1 193  ARG 193  206  206 ARG ARG A . n 
A 1 194  GLY 194  207  207 GLY GLY A . n 
A 1 195  THR 195  208  208 THR THR A . n 
A 1 196  PHE 196  209  209 PHE PHE A . n 
A 1 197  TYR 197  210  210 TYR TYR A . n 
A 1 198  ALA 198  211  211 ALA ALA A . n 
A 1 199  TYR 199  212  212 TYR TYR A . n 
A 1 200  TYR 200  213  213 TYR TYR A . n 
A 1 201  ALA 201  214  214 ALA ALA A . n 
A 1 202  ASP 202  215  215 ASP ASP A . n 
A 1 203  SER 203  216  216 SER SER A . n 
A 1 204  GLY 204  217  217 GLY GLY A . n 
A 1 205  MET 205  218  218 MET MET A . n 
A 1 206  PRO 206  219  219 PRO PRO A . n 
A 1 207  THR 207  220  220 THR THR A . n 
A 1 208  THR 208  221  221 THR THR A . n 
A 1 209  PHE 209  222  222 PHE PHE A . n 
A 1 210  LEU 210  223  223 LEU LEU A . n 
A 1 211  PHE 211  224  224 PHE PHE A . n 
A 1 212  SER 212  225  225 SER SER A . n 
A 1 213  LEU 213  226  226 LEU LEU A . n 
A 1 214  TYR 214  227  227 TYR TYR A . n 
A 1 215  LEU 215  228  228 LEU LEU A . n 
A 1 216  GLY 216  229  229 GLY GLY A . n 
A 1 217  THR 217  230  230 THR THR A . n 
A 1 218  LEU 218  231  231 LEU LEU A . n 
A 1 219  LEU 219  232  232 LEU LEU A . n 
A 1 220  SER 220  233  233 SER SER A . n 
A 1 221  HIS 221  234  234 HIS HIS A . n 
A 1 222  TYR 222  235  235 TYR TYR A . n 
A 1 223  TYR 223  236  236 TYR TYR A . n 
A 1 224  VAL 224  237  237 VAL VAL A . n 
A 1 225  LEU 225  238  238 LEU LEU A . n 
A 1 226  PRO 226  239  239 PRO PRO A . n 
A 1 227  LEU 227  240  240 LEU LEU A . n 
A 1 228  THR 228  241  241 THR THR A . n 
A 1 229  CYS 229  242  242 CYS CYS A . n 
A 1 230  ASN 230  243  243 ASN ASN A . n 
A 1 231  ALA 231  244  244 ALA ALA A . n 
A 1 232  ILE 232  245  245 ILE ILE A . n 
A 1 233  SER 233  246  246 SER SER A . n 
A 1 234  SER 234  247  247 SER SER A . n 
A 1 235  ASN 235  248  248 ASN ASN A . n 
A 1 236  THR 236  249  249 THR THR A . n 
A 1 237  ASP 237  250  250 ASP ASP A . n 
A 1 238  ASN 238  251  251 ASN ASN A . n 
A 1 239  GLU 239  252  252 GLU GLU A . n 
A 1 240  THR 240  253  253 THR THR A . n 
A 1 241  LEU 241  254  254 LEU LEU A . n 
A 1 242  GLN 242  255  255 GLN GLN A . n 
A 1 243  TYR 243  256  256 TYR TYR A . n 
A 1 244  TRP 244  257  257 TRP TRP A . n 
A 1 245  VAL 245  258  258 VAL VAL A . n 
A 1 246  THR 246  259  259 THR THR A . n 
A 1 247  PRO 247  260  260 PRO PRO A . n 
A 1 248  LEU 248  261  261 LEU LEU A . n 
A 1 249  SER 249  262  262 SER SER A . n 
A 1 250  LYS 250  263  263 LYS LYS A . n 
A 1 251  ARG 251  264  264 ARG ARG A . n 
A 1 252  GLN 252  265  265 GLN GLN A . n 
A 1 253  TYR 253  266  266 TYR TYR A . n 
A 1 254  LEU 254  267  267 LEU LEU A . n 
A 1 255  LEU 255  268  268 LEU LEU A . n 
A 1 256  LYS 256  269  269 LYS LYS A . n 
A 1 257  PHE 257  270  270 PHE PHE A . n 
A 1 258  ASP 258  271  271 ASP ASP A . n 
A 1 259  ASN 259  272  272 ASN ASN A . n 
A 1 260  ARG 260  273  273 ARG ARG A . n 
A 1 261  GLY 261  274  274 GLY GLY A . n 
A 1 262  VAL 262  275  275 VAL VAL A . n 
A 1 263  ILE 263  276  276 ILE ILE A . n 
A 1 264  THR 264  277  277 THR THR A . n 
A 1 265  ASN 265  278  278 ASN ASN A . n 
A 1 266  ALA 266  279  279 ALA ALA A . n 
A 1 267  VAL 267  280  280 VAL VAL A . n 
A 1 268  ASP 268  281  281 ASP ASP A . n 
A 1 269  CYS 269  282  ?   ?   ?   A . n 
A 1 270  SER 270  283  ?   ?   ?   A . n 
A 1 271  SER 271  284  ?   ?   ?   A . n 
A 1 272  SER 272  285  ?   ?   ?   A . n 
A 1 273  PHE 273  286  ?   ?   ?   A . n 
A 1 274  PHE 274  287  ?   ?   ?   A . n 
A 1 275  SER 275  288  ?   ?   ?   A . n 
A 1 276  GLU 276  289  ?   ?   ?   A . n 
A 1 277  ILE 277  290  ?   ?   ?   A . n 
A 1 278  GLN 278  291  ?   ?   ?   A . n 
A 1 279  CYS 279  292  ?   ?   ?   A . n 
A 1 280  LYS 280  293  ?   ?   ?   A . n 
A 1 281  THR 281  294  ?   ?   ?   A . n 
A 1 282  LYS 282  295  ?   ?   ?   A . n 
A 1 283  SER 283  296  ?   ?   ?   A . n 
A 1 284  LEU 284  297  ?   ?   ?   A . n 
A 1 285  LEU 285  298  ?   ?   ?   A . n 
A 1 286  PRO 286  299  ?   ?   ?   A . n 
A 1 287  ASN 287  300  ?   ?   ?   A . n 
A 1 288  THR 288  301  ?   ?   ?   A . n 
A 1 289  GLY 289  302  ?   ?   ?   A . n 
A 1 290  VAL 290  303  ?   ?   ?   A . n 
A 1 291  TYR 291  304  ?   ?   ?   A . n 
A 1 292  ASP 292  305  ?   ?   ?   A . n 
A 1 293  LEU 293  306  ?   ?   ?   A . n 
A 1 294  SER 294  307  ?   ?   ?   A . n 
A 1 295  GLY 295  308  ?   ?   ?   A . n 
A 1 296  PHE 296  309  ?   ?   ?   A . n 
A 1 297  THR 297  310  ?   ?   ?   A . n 
A 1 298  VAL 298  311  ?   ?   ?   A . n 
A 1 299  LYS 299  312  ?   ?   ?   A . n 
A 1 300  PRO 300  313  ?   ?   ?   A . n 
A 1 301  VAL 301  314  ?   ?   ?   A . n 
A 1 302  ALA 302  315  ?   ?   ?   A . n 
A 1 303  THR 303  316  ?   ?   ?   A . n 
A 1 304  VAL 304  317  ?   ?   ?   A . n 
A 1 305  HIS 305  318  ?   ?   ?   A . n 
A 1 306  ARG 306  319  ?   ?   ?   A . n 
A 1 307  ARG 307  320  ?   ?   ?   A . n 
A 1 308  ILE 308  321  ?   ?   ?   A . n 
A 1 309  PRO 309  322  ?   ?   ?   A . n 
A 1 310  ASP 310  323  ?   ?   ?   A . n 
A 1 311  LEU 311  324  ?   ?   ?   A . n 
A 1 312  PRO 312  325  ?   ?   ?   A . n 
A 1 313  ASP 313  326  ?   ?   ?   A . n 
A 1 314  CYS 314  327  ?   ?   ?   A . n 
A 1 315  ASP 315  328  ?   ?   ?   A . n 
A 1 316  ILE 316  329  ?   ?   ?   A . n 
A 1 317  ASP 317  330  ?   ?   ?   A . n 
A 1 318  LYS 318  331  ?   ?   ?   A . n 
A 1 319  TRP 319  332  ?   ?   ?   A . n 
A 1 320  LEU 320  333  ?   ?   ?   A . n 
A 1 321  ASN 321  334  ?   ?   ?   A . n 
A 1 322  ASN 322  335  ?   ?   ?   A . n 
A 1 323  PHE 323  336  ?   ?   ?   A . n 
A 1 324  ASN 324  337  ?   ?   ?   A . n 
A 1 325  VAL 325  338  ?   ?   ?   A . n 
A 1 326  PRO 326  339  ?   ?   ?   A . n 
A 1 327  SER 327  340  ?   ?   ?   A . n 
A 1 328  PRO 328  341  ?   ?   ?   A . n 
A 1 329  LEU 329  342  ?   ?   ?   A . n 
A 1 330  ASN 330  343  ?   ?   ?   A . n 
A 1 331  TRP 331  344  ?   ?   ?   A . n 
A 1 332  GLU 332  345  ?   ?   ?   A . n 
A 1 333  ARG 333  346  ?   ?   ?   A . n 
A 1 334  LYS 334  347  ?   ?   ?   A . n 
A 1 335  ILE 335  348  ?   ?   ?   A . n 
A 1 336  PHE 336  349  ?   ?   ?   A . n 
A 1 337  SER 337  350  ?   ?   ?   A . n 
A 1 338  ASN 338  351  ?   ?   ?   A . n 
A 1 339  CYS 339  352  ?   ?   ?   A . n 
A 1 340  ASN 340  353  ?   ?   ?   A . n 
A 1 341  PHE 341  354  ?   ?   ?   A . n 
A 1 342  ASN 342  355  ?   ?   ?   A . n 
A 1 343  LEU 343  356  ?   ?   ?   A . n 
A 1 344  SER 344  357  ?   ?   ?   A . n 
A 1 345  THR 345  358  ?   ?   ?   A . n 
A 1 346  LEU 346  359  ?   ?   ?   A . n 
A 1 347  LEU 347  360  ?   ?   ?   A . n 
A 1 348  ARG 348  361  ?   ?   ?   A . n 
A 1 349  LEU 349  362  ?   ?   ?   A . n 
A 1 350  VAL 350  363  ?   ?   ?   A . n 
A 1 351  HIS 351  364  ?   ?   ?   A . n 
A 1 352  THR 352  365  ?   ?   ?   A . n 
A 1 353  ASP 353  366  ?   ?   ?   A . n 
A 1 354  SER 354  367  ?   ?   ?   A . n 
A 1 355  PHE 355  368  ?   ?   ?   A . n 
A 1 356  SER 356  369  ?   ?   ?   A . n 
A 1 357  CYS 357  370  ?   ?   ?   A . n 
A 1 358  ASN 358  371  ?   ?   ?   A . n 
A 1 359  ASN 359  372  ?   ?   ?   A . n 
A 1 360  PHE 360  373  ?   ?   ?   A . n 
A 1 361  ASP 361  374  ?   ?   ?   A . n 
A 1 362  GLU 362  375  ?   ?   ?   A . n 
A 1 363  SER 363  376  ?   ?   ?   A . n 
A 1 364  LYS 364  377  ?   ?   ?   A . n 
A 1 365  ILE 365  378  ?   ?   ?   A . n 
A 1 366  TYR 366  379  ?   ?   ?   A . n 
A 1 367  GLY 367  380  ?   ?   ?   A . n 
A 1 368  SER 368  381  ?   ?   ?   A . n 
A 1 369  CYS 369  382  ?   ?   ?   A . n 
A 1 370  PHE 370  383  ?   ?   ?   A . n 
A 1 371  LYS 371  384  ?   ?   ?   A . n 
A 1 372  SER 372  385  ?   ?   ?   A . n 
A 1 373  ILE 373  386  ?   ?   ?   A . n 
A 1 374  VAL 374  387  ?   ?   ?   A . n 
A 1 375  LEU 375  388  ?   ?   ?   A . n 
A 1 376  ASP 376  389  ?   ?   ?   A . n 
A 1 377  LYS 377  390  ?   ?   ?   A . n 
A 1 378  PHE 378  391  ?   ?   ?   A . n 
A 1 379  ALA 379  392  ?   ?   ?   A . n 
A 1 380  ILE 380  393  ?   ?   ?   A . n 
A 1 381  PRO 381  394  ?   ?   ?   A . n 
A 1 382  ASN 382  395  ?   ?   ?   A . n 
A 1 383  SER 383  396  ?   ?   ?   A . n 
A 1 384  ARG 384  397  ?   ?   ?   A . n 
A 1 385  ARG 385  398  ?   ?   ?   A . n 
A 1 386  SER 386  399  ?   ?   ?   A . n 
A 1 387  ASP 387  400  ?   ?   ?   A . n 
A 1 388  LEU 388  401  ?   ?   ?   A . n 
A 1 389  GLN 389  402  ?   ?   ?   A . n 
A 1 390  LEU 390  403  ?   ?   ?   A . n 
A 1 391  GLY 391  404  ?   ?   ?   A . n 
A 1 392  SER 392  405  ?   ?   ?   A . n 
A 1 393  SER 393  406  ?   ?   ?   A . n 
A 1 394  GLY 394  407  ?   ?   ?   A . n 
A 1 395  PHE 395  408  ?   ?   ?   A . n 
A 1 396  LEU 396  409  ?   ?   ?   A . n 
A 1 397  GLN 397  410  ?   ?   ?   A . n 
A 1 398  SER 398  411  ?   ?   ?   A . n 
A 1 399  SER 399  412  ?   ?   ?   A . n 
A 1 400  ASN 400  413  ?   ?   ?   A . n 
A 1 401  TYR 401  414  ?   ?   ?   A . n 
A 1 402  LYS 402  415  ?   ?   ?   A . n 
A 1 403  ILE 403  416  ?   ?   ?   A . n 
A 1 404  ASP 404  417  ?   ?   ?   A . n 
A 1 405  THR 405  418  ?   ?   ?   A . n 
A 1 406  THR 406  419  ?   ?   ?   A . n 
A 1 407  SER 407  420  ?   ?   ?   A . n 
A 1 408  SER 408  421  ?   ?   ?   A . n 
A 1 409  SER 409  422  ?   ?   ?   A . n 
A 1 410  CYS 410  423  ?   ?   ?   A . n 
A 1 411  GLN 411  424  ?   ?   ?   A . n 
A 1 412  LEU 412  425  ?   ?   ?   A . n 
A 1 413  TYR 413  426  ?   ?   ?   A . n 
A 1 414  TYR 414  427  ?   ?   ?   A . n 
A 1 415  SER 415  428  ?   ?   ?   A . n 
A 1 416  LEU 416  429  ?   ?   ?   A . n 
A 1 417  PRO 417  430  ?   ?   ?   A . n 
A 1 418  ALA 418  431  ?   ?   ?   A . n 
A 1 419  ILE 419  432  ?   ?   ?   A . n 
A 1 420  ASN 420  433  ?   ?   ?   A . n 
A 1 421  VAL 421  434  ?   ?   ?   A . n 
A 1 422  THR 422  435  ?   ?   ?   A . n 
A 1 423  ILE 423  436  ?   ?   ?   A . n 
A 1 424  ASN 424  437  ?   ?   ?   A . n 
A 1 425  ASN 425  438  ?   ?   ?   A . n 
A 1 426  TYR 426  439  ?   ?   ?   A . n 
A 1 427  ASN 427  440  ?   ?   ?   A . n 
A 1 428  PRO 428  441  ?   ?   ?   A . n 
A 1 429  SER 429  442  ?   ?   ?   A . n 
A 1 430  SER 430  443  ?   ?   ?   A . n 
A 1 431  TRP 431  444  ?   ?   ?   A . n 
A 1 432  ASN 432  445  ?   ?   ?   A . n 
A 1 433  ARG 433  446  ?   ?   ?   A . n 
A 1 434  ARG 434  447  ?   ?   ?   A . n 
A 1 435  TYR 435  448  ?   ?   ?   A . n 
A 1 436  GLY 436  449  ?   ?   ?   A . n 
A 1 437  PHE 437  450  ?   ?   ?   A . n 
A 1 438  ASN 438  451  ?   ?   ?   A . n 
A 1 439  ASN 439  452  ?   ?   ?   A . n 
A 1 440  PHE 440  453  ?   ?   ?   A . n 
A 1 441  ASN 441  454  ?   ?   ?   A . n 
A 1 442  LEU 442  455  ?   ?   ?   A . n 
A 1 443  SER 443  456  ?   ?   ?   A . n 
A 1 444  SER 444  457  ?   ?   ?   A . n 
A 1 445  HIS 445  458  ?   ?   ?   A . n 
A 1 446  SER 446  459  ?   ?   ?   A . n 
A 1 447  VAL 447  460  ?   ?   ?   A . n 
A 1 448  VAL 448  461  ?   ?   ?   A . n 
A 1 449  TYR 449  462  ?   ?   ?   A . n 
A 1 450  SER 450  463  ?   ?   ?   A . n 
A 1 451  ARG 451  464  ?   ?   ?   A . n 
A 1 452  TYR 452  465  ?   ?   ?   A . n 
A 1 453  CYS 453  466  ?   ?   ?   A . n 
A 1 454  PHE 454  467  ?   ?   ?   A . n 
A 1 455  SER 455  468  ?   ?   ?   A . n 
A 1 456  VAL 456  469  ?   ?   ?   A . n 
A 1 457  ASN 457  470  ?   ?   ?   A . n 
A 1 458  ASN 458  471  ?   ?   ?   A . n 
A 1 459  THR 459  472  ?   ?   ?   A . n 
A 1 460  PHE 460  473  ?   ?   ?   A . n 
A 1 461  CYS 461  474  ?   ?   ?   A . n 
A 1 462  PRO 462  475  ?   ?   ?   A . n 
A 1 463  CYS 463  476  ?   ?   ?   A . n 
A 1 464  ALA 464  477  ?   ?   ?   A . n 
A 1 465  LYS 465  478  ?   ?   ?   A . n 
A 1 466  PRO 466  479  ?   ?   ?   A . n 
A 1 467  SER 467  480  ?   ?   ?   A . n 
A 1 468  PHE 468  481  ?   ?   ?   A . n 
A 1 469  ALA 469  482  ?   ?   ?   A . n 
A 1 470  SER 470  483  ?   ?   ?   A . n 
A 1 471  SER 471  484  ?   ?   ?   A . n 
A 1 472  CYS 472  485  ?   ?   ?   A . n 
A 1 473  LYS 473  486  ?   ?   ?   A . n 
A 1 474  SER 474  487  ?   ?   ?   A . n 
A 1 475  HIS 475  488  ?   ?   ?   A . n 
A 1 476  LYS 476  489  ?   ?   ?   A . n 
A 1 477  PRO 477  490  ?   ?   ?   A . n 
A 1 478  PRO 478  491  ?   ?   ?   A . n 
A 1 479  SER 479  492  ?   ?   ?   A . n 
A 1 480  ALA 480  493  ?   ?   ?   A . n 
A 1 481  SER 481  494  ?   ?   ?   A . n 
A 1 482  CYS 482  495  ?   ?   ?   A . n 
A 1 483  PRO 483  496  ?   ?   ?   A . n 
A 1 484  ILE 484  497  ?   ?   ?   A . n 
A 1 485  GLY 485  498  ?   ?   ?   A . n 
A 1 486  THR 486  499  ?   ?   ?   A . n 
A 1 487  ASN 487  500  ?   ?   ?   A . n 
A 1 488  TYR 488  501  ?   ?   ?   A . n 
A 1 489  ARG 489  502  ?   ?   ?   A . n 
A 1 490  SER 490  503  ?   ?   ?   A . n 
A 1 491  CYS 491  504  ?   ?   ?   A . n 
A 1 492  GLU 492  505  ?   ?   ?   A . n 
A 1 493  SER 493  506  ?   ?   ?   A . n 
A 1 494  THR 494  507  ?   ?   ?   A . n 
A 1 495  THR 495  508  ?   ?   ?   A . n 
A 1 496  VAL 496  509  ?   ?   ?   A . n 
A 1 497  LEU 497  510  ?   ?   ?   A . n 
A 1 498  ASP 498  511  ?   ?   ?   A . n 
A 1 499  HIS 499  512  ?   ?   ?   A . n 
A 1 500  THR 500  513  ?   ?   ?   A . n 
A 1 501  ASP 501  514  ?   ?   ?   A . n 
A 1 502  TRP 502  515  ?   ?   ?   A . n 
A 1 503  CYS 503  516  ?   ?   ?   A . n 
A 1 504  ARG 504  517  ?   ?   ?   A . n 
A 1 505  CYS 505  518  ?   ?   ?   A . n 
A 1 506  SER 506  519  ?   ?   ?   A . n 
A 1 507  CYS 507  520  ?   ?   ?   A . n 
A 1 508  LEU 508  521  ?   ?   ?   A . n 
A 1 509  PRO 509  522  ?   ?   ?   A . n 
A 1 510  ASP 510  523  ?   ?   ?   A . n 
A 1 511  PRO 511  524  ?   ?   ?   A . n 
A 1 512  ILE 512  525  ?   ?   ?   A . n 
A 1 513  THR 513  526  ?   ?   ?   A . n 
A 1 514  ALA 514  527  ?   ?   ?   A . n 
A 1 515  TYR 515  528  ?   ?   ?   A . n 
A 1 516  ASP 516  529  ?   ?   ?   A . n 
A 1 517  PRO 517  530  ?   ?   ?   A . n 
A 1 518  ARG 518  531  ?   ?   ?   A . n 
A 1 519  SER 519  532  ?   ?   ?   A . n 
A 1 520  CYS 520  533  ?   ?   ?   A . n 
A 1 521  SER 521  534  ?   ?   ?   A . n 
A 1 522  GLN 522  535  ?   ?   ?   A . n 
A 1 523  LYS 523  536  ?   ?   ?   A . n 
A 1 524  LYS 524  537  ?   ?   ?   A . n 
A 1 525  SER 525  538  ?   ?   ?   A . n 
A 1 526  LEU 526  539  ?   ?   ?   A . n 
A 1 527  VAL 527  540  ?   ?   ?   A . n 
A 1 528  GLY 528  541  ?   ?   ?   A . n 
A 1 529  VAL 529  542  ?   ?   ?   A . n 
A 1 530  GLY 530  543  ?   ?   ?   A . n 
A 1 531  GLU 531  544  ?   ?   ?   A . n 
A 1 532  HIS 532  545  ?   ?   ?   A . n 
A 1 533  CYS 533  546  ?   ?   ?   A . n 
A 1 534  ALA 534  547  ?   ?   ?   A . n 
A 1 535  GLY 535  548  ?   ?   ?   A . n 
A 1 536  PHE 536  549  ?   ?   ?   A . n 
A 1 537  GLY 537  550  ?   ?   ?   A . n 
A 1 538  VAL 538  551  ?   ?   ?   A . n 
A 1 539  ASP 539  552  ?   ?   ?   A . n 
A 1 540  GLU 540  553  ?   ?   ?   A . n 
A 1 541  GLU 541  554  ?   ?   ?   A . n 
A 1 542  LYS 542  555  ?   ?   ?   A . n 
A 1 543  CYS 543  556  ?   ?   ?   A . n 
A 1 544  GLY 544  557  ?   ?   ?   A . n 
A 1 545  VAL 545  558  ?   ?   ?   A . n 
A 1 546  LEU 546  559  ?   ?   ?   A . n 
A 1 547  ASP 547  560  ?   ?   ?   A . n 
A 1 548  GLY 548  561  ?   ?   ?   A . n 
A 1 549  SER 549  562  ?   ?   ?   A . n 
A 1 550  TYR 550  563  ?   ?   ?   A . n 
A 1 551  ASN 551  564  ?   ?   ?   A . n 
A 1 552  VAL 552  565  ?   ?   ?   A . n 
A 1 553  SER 553  566  ?   ?   ?   A . n 
A 1 554  CYS 554  567  ?   ?   ?   A . n 
A 1 555  LEU 555  568  ?   ?   ?   A . n 
A 1 556  CYS 556  569  ?   ?   ?   A . n 
A 1 557  SER 557  570  ?   ?   ?   A . n 
A 1 558  THR 558  571  ?   ?   ?   A . n 
A 1 559  ASP 559  572  ?   ?   ?   A . n 
A 1 560  ALA 560  573  ?   ?   ?   A . n 
A 1 561  PHE 561  574  ?   ?   ?   A . n 
A 1 562  LEU 562  575  ?   ?   ?   A . n 
A 1 563  GLY 563  576  ?   ?   ?   A . n 
A 1 564  TRP 564  577  ?   ?   ?   A . n 
A 1 565  SER 565  578  ?   ?   ?   A . n 
A 1 566  TYR 566  579  ?   ?   ?   A . n 
A 1 567  ASP 567  580  ?   ?   ?   A . n 
A 1 568  THR 568  581  ?   ?   ?   A . n 
A 1 569  CYS 569  582  ?   ?   ?   A . n 
A 1 570  VAL 570  583  ?   ?   ?   A . n 
A 1 571  SER 571  584  ?   ?   ?   A . n 
A 1 572  ASN 572  585  ?   ?   ?   A . n 
A 1 573  ASN 573  586  ?   ?   ?   A . n 
A 1 574  ARG 574  587  ?   ?   ?   A . n 
A 1 575  CYS 575  588  ?   ?   ?   A . n 
A 1 576  ASN 576  589  ?   ?   ?   A . n 
A 1 577  ILE 577  590  ?   ?   ?   A . n 
A 1 578  PHE 578  591  ?   ?   ?   A . n 
A 1 579  SER 579  592  ?   ?   ?   A . n 
A 1 580  ASN 580  593  ?   ?   ?   A . n 
A 1 581  PHE 581  594  ?   ?   ?   A . n 
A 1 582  ILE 582  595  ?   ?   ?   A . n 
A 1 583  LEU 583  596  ?   ?   ?   A . n 
A 1 584  ASN 584  597  ?   ?   ?   A . n 
A 1 585  GLY 585  598  ?   ?   ?   A . n 
A 1 586  ILE 586  599  ?   ?   ?   A . n 
A 1 587  ASN 587  600  ?   ?   ?   A . n 
A 1 588  SER 588  601  ?   ?   ?   A . n 
A 1 589  GLY 589  602  ?   ?   ?   A . n 
A 1 590  THR 590  603  ?   ?   ?   A . n 
A 1 591  THR 591  604  ?   ?   ?   A . n 
A 1 592  CYS 592  605  ?   ?   ?   A . n 
A 1 593  SER 593  606  ?   ?   ?   A . n 
A 1 594  ASN 594  607  ?   ?   ?   A . n 
A 1 595  ASP 595  608  ?   ?   ?   A . n 
A 1 596  LEU 596  609  ?   ?   ?   A . n 
A 1 597  LEU 597  610  ?   ?   ?   A . n 
A 1 598  GLN 598  611  ?   ?   ?   A . n 
A 1 599  PRO 599  612  ?   ?   ?   A . n 
A 1 600  ASN 600  613  ?   ?   ?   A . n 
A 1 601  THR 601  614  ?   ?   ?   A . n 
A 1 602  GLU 602  615  ?   ?   ?   A . n 
A 1 603  VAL 603  616  ?   ?   ?   A . n 
A 1 604  PHE 604  617  ?   ?   ?   A . n 
A 1 605  THR 605  618  ?   ?   ?   A . n 
A 1 606  ASP 606  619  ?   ?   ?   A . n 
A 1 607  VAL 607  620  ?   ?   ?   A . n 
A 1 608  CYS 608  621  ?   ?   ?   A . n 
A 1 609  VAL 609  622  ?   ?   ?   A . n 
A 1 610  ASP 610  623  ?   ?   ?   A . n 
A 1 611  TYR 611  624  ?   ?   ?   A . n 
A 1 612  ASP 612  625  ?   ?   ?   A . n 
A 1 613  LEU 613  626  ?   ?   ?   A . n 
A 1 614  TYR 614  627  ?   ?   ?   A . n 
A 1 615  GLY 615  628  ?   ?   ?   A . n 
A 1 616  ILE 616  629  ?   ?   ?   A . n 
A 1 617  THR 617  630  ?   ?   ?   A . n 
A 1 618  GLY 618  631  ?   ?   ?   A . n 
A 1 619  GLN 619  632  ?   ?   ?   A . n 
A 1 620  GLY 620  633  ?   ?   ?   A . n 
A 1 621  ILE 621  634  ?   ?   ?   A . n 
A 1 622  PHE 622  635  ?   ?   ?   A . n 
A 1 623  LYS 623  636  ?   ?   ?   A . n 
A 1 624  GLU 624  637  ?   ?   ?   A . n 
A 1 625  VAL 625  638  ?   ?   ?   A . n 
A 1 626  SER 626  639  ?   ?   ?   A . n 
A 1 627  ALA 627  640  ?   ?   ?   A . n 
A 1 628  VAL 628  641  ?   ?   ?   A . n 
A 1 629  TYR 629  642  ?   ?   ?   A . n 
A 1 630  TYR 630  643  ?   ?   ?   A . n 
A 1 631  ASN 631  644  ?   ?   ?   A . n 
A 1 632  SER 632  645  ?   ?   ?   A . n 
A 1 633  TRP 633  646  ?   ?   ?   A . n 
A 1 634  GLN 634  647  ?   ?   ?   A . n 
A 1 635  ASN 635  648  ?   ?   ?   A . n 
A 1 636  LEU 636  649  ?   ?   ?   A . n 
A 1 637  LEU 637  650  ?   ?   ?   A . n 
A 1 638  TYR 638  651  ?   ?   ?   A . n 
A 1 639  ASP 639  652  ?   ?   ?   A . n 
A 1 640  SER 640  653  ?   ?   ?   A . n 
A 1 641  ASN 641  654  ?   ?   ?   A . n 
A 1 642  GLY 642  655  ?   ?   ?   A . n 
A 1 643  ASN 643  656  ?   ?   ?   A . n 
A 1 644  ILE 644  657  ?   ?   ?   A . n 
A 1 645  ILE 645  658  ?   ?   ?   A . n 
A 1 646  GLY 646  659  ?   ?   ?   A . n 
A 1 647  PHE 647  660  ?   ?   ?   A . n 
A 1 648  LYS 648  661  ?   ?   ?   A . n 
A 1 649  ASP 649  662  ?   ?   ?   A . n 
A 1 650  PHE 650  663  ?   ?   ?   A . n 
A 1 651  VAL 651  664  ?   ?   ?   A . n 
A 1 652  THR 652  665  ?   ?   ?   A . n 
A 1 653  ASN 653  666  ?   ?   ?   A . n 
A 1 654  LYS 654  667  ?   ?   ?   A . n 
A 1 655  THR 655  668  ?   ?   ?   A . n 
A 1 656  TYR 656  669  ?   ?   ?   A . n 
A 1 657  ASN 657  670  ?   ?   ?   A . n 
A 1 658  ILE 658  671  ?   ?   ?   A . n 
A 1 659  PHE 659  672  ?   ?   ?   A . n 
A 1 660  PRO 660  673  ?   ?   ?   A . n 
A 1 661  CYS 661  674  ?   ?   ?   A . n 
A 1 662  TYR 662  675  ?   ?   ?   A . n 
A 1 663  ALA 663  676  ?   ?   ?   A . n 
A 1 664  GLY 664  677  ?   ?   ?   A . n 
A 1 665  ARG 665  678  ?   ?   ?   A . n 
A 1 666  VAL 666  679  ?   ?   ?   A . n 
A 1 667  SER 667  680  ?   ?   ?   A . n 
A 1 668  ALA 668  681  ?   ?   ?   A . n 
A 1 669  ALA 669  682  ?   ?   ?   A . n 
A 1 670  PHE 670  683  ?   ?   ?   A . n 
A 1 671  HIS 671  684  ?   ?   ?   A . n 
A 1 672  GLN 672  685  ?   ?   ?   A . n 
A 1 673  ASN 673  686  ?   ?   ?   A . n 
A 1 674  ALA 674  687  ?   ?   ?   A . n 
A 1 675  SER 675  688  ?   ?   ?   A . n 
A 1 676  SER 676  689  ?   ?   ?   A . n 
A 1 677  LEU 677  690  ?   ?   ?   A . n 
A 1 678  ALA 678  691  ?   ?   ?   A . n 
A 1 679  LEU 679  692  ?   ?   ?   A . n 
A 1 680  LEU 680  693  ?   ?   ?   A . n 
A 1 681  TYR 681  694  ?   ?   ?   A . n 
A 1 682  ARG 682  695  ?   ?   ?   A . n 
A 1 683  ASN 683  696  ?   ?   ?   A . n 
A 1 684  LEU 684  697  ?   ?   ?   A . n 
A 1 685  LYS 685  698  ?   ?   ?   A . n 
A 1 686  CYS 686  699  ?   ?   ?   A . n 
A 1 687  SER 687  700  ?   ?   ?   A . n 
A 1 688  TYR 688  701  ?   ?   ?   A . n 
A 1 689  VAL 689  702  ?   ?   ?   A . n 
A 1 690  LEU 690  703  ?   ?   ?   A . n 
A 1 691  ASN 691  704  ?   ?   ?   A . n 
A 1 692  ASN 692  705  ?   ?   ?   A . n 
A 1 693  ILE 693  706  ?   ?   ?   A . n 
A 1 694  SER 694  707  ?   ?   ?   A . n 
A 1 695  LEU 695  708  ?   ?   ?   A . n 
A 1 696  THR 696  709  ?   ?   ?   A . n 
A 1 697  THR 697  710  ?   ?   ?   A . n 
A 1 698  GLN 698  711  ?   ?   ?   A . n 
A 1 699  PRO 699  712  ?   ?   ?   A . n 
A 1 700  TYR 700  713  ?   ?   ?   A . n 
A 1 701  PHE 701  714  ?   ?   ?   A . n 
A 1 702  ASP 702  715  ?   ?   ?   A . n 
A 1 703  SER 703  716  ?   ?   ?   A . n 
A 1 704  TYR 704  717  ?   ?   ?   A . n 
A 1 705  LEU 705  718  ?   ?   ?   A . n 
A 1 706  GLY 706  719  ?   ?   ?   A . n 
A 1 707  CYS 707  720  ?   ?   ?   A . n 
A 1 708  VAL 708  721  ?   ?   ?   A . n 
A 1 709  PHE 709  722  ?   ?   ?   A . n 
A 1 710  ASN 710  723  ?   ?   ?   A . n 
A 1 711  ALA 711  724  ?   ?   ?   A . n 
A 1 712  ASP 712  725  ?   ?   ?   A . n 
A 1 713  ASN 713  726  ?   ?   ?   A . n 
A 1 714  LEU 714  727  ?   ?   ?   A . n 
A 1 715  THR 715  728  ?   ?   ?   A . n 
A 1 716  ASP 716  729  ?   ?   ?   A . n 
A 1 717  TYR 717  730  ?   ?   ?   A . n 
A 1 718  SER 718  731  ?   ?   ?   A . n 
A 1 719  VAL 719  732  ?   ?   ?   A . n 
A 1 720  SER 720  733  ?   ?   ?   A . n 
A 1 721  SER 721  734  ?   ?   ?   A . n 
A 1 722  CYS 722  735  ?   ?   ?   A . n 
A 1 723  ALA 723  736  ?   ?   ?   A . n 
A 1 724  LEU 724  737  ?   ?   ?   A . n 
A 1 725  ARG 725  738  ?   ?   ?   A . n 
A 1 726  MET 726  739  ?   ?   ?   A . n 
A 1 727  GLY 727  740  ?   ?   ?   A . n 
A 1 728  SER 728  741  ?   ?   ?   A . n 
A 1 729  GLY 729  742  ?   ?   ?   A . n 
A 1 730  PHE 730  743  ?   ?   ?   A . n 
A 1 731  CYS 731  744  ?   ?   ?   A . n 
A 1 732  VAL 732  745  ?   ?   ?   A . n 
A 1 733  ASP 733  746  ?   ?   ?   A . n 
A 1 734  TYR 734  747  ?   ?   ?   A . n 
A 1 735  ASN 735  748  ?   ?   ?   A . n 
A 1 736  SER 736  749  ?   ?   ?   A . n 
A 1 737  TYR 737  750  ?   ?   ?   A . n 
A 1 738  ARG 738  751  ?   ?   ?   A . n 
A 1 739  PHE 739  752  ?   ?   ?   A . n 
A 1 740  VAL 740  753  ?   ?   ?   A . n 
A 1 741  THR 741  754  ?   ?   ?   A . n 
A 1 742  PHE 742  755  ?   ?   ?   A . n 
A 1 743  GLU 743  756  ?   ?   ?   A . n 
A 1 744  PRO 744  757  ?   ?   ?   A . n 
A 1 745  PHE 745  758  ?   ?   ?   A . n 
A 1 746  ASN 746  759  ?   ?   ?   A . n 
A 1 747  VAL 747  760  ?   ?   ?   A . n 
A 1 748  SER 748  761  ?   ?   ?   A . n 
A 1 749  PHE 749  762  ?   ?   ?   A . n 
A 1 750  VAL 750  763  ?   ?   ?   A . n 
A 1 751  ASN 751  764  ?   ?   ?   A . n 
A 1 752  ASP 752  765  ?   ?   ?   A . n 
A 1 753  SER 753  766  ?   ?   ?   A . n 
A 1 754  ILE 754  767  ?   ?   ?   A . n 
A 1 755  GLU 755  768  ?   ?   ?   A . n 
A 1 756  SER 756  769  ?   ?   ?   A . n 
A 1 757  VAL 757  770  ?   ?   ?   A . n 
A 1 758  GLY 758  771  ?   ?   ?   A . n 
A 1 759  GLY 759  772  ?   ?   ?   A . n 
A 1 760  LEU 760  773  ?   ?   ?   A . n 
A 1 761  TYR 761  774  ?   ?   ?   A . n 
A 1 762  GLU 762  775  ?   ?   ?   A . n 
A 1 763  ILE 763  776  ?   ?   ?   A . n 
A 1 764  LYS 764  777  ?   ?   ?   A . n 
A 1 765  ILE 765  778  ?   ?   ?   A . n 
A 1 766  PRO 766  779  ?   ?   ?   A . n 
A 1 767  THR 767  780  ?   ?   ?   A . n 
A 1 768  ASN 768  781  ?   ?   ?   A . n 
A 1 769  PHE 769  782  ?   ?   ?   A . n 
A 1 770  THR 770  783  ?   ?   ?   A . n 
A 1 771  ILE 771  784  ?   ?   ?   A . n 
A 1 772  VAL 772  785  ?   ?   ?   A . n 
A 1 773  GLY 773  786  ?   ?   ?   A . n 
A 1 774  GLN 774  787  ?   ?   ?   A . n 
A 1 775  GLU 775  788  ?   ?   ?   A . n 
A 1 776  GLU 776  789  ?   ?   ?   A . n 
A 1 777  PHE 777  790  ?   ?   ?   A . n 
A 1 778  ILE 778  791  ?   ?   ?   A . n 
A 1 779  GLN 779  792  ?   ?   ?   A . n 
A 1 780  THR 780  793  ?   ?   ?   A . n 
A 1 781  ASN 781  794  ?   ?   ?   A . n 
A 1 782  SER 782  795  ?   ?   ?   A . n 
A 1 783  PRO 783  796  ?   ?   ?   A . n 
A 1 784  LYS 784  797  ?   ?   ?   A . n 
A 1 785  VAL 785  798  ?   ?   ?   A . n 
A 1 786  THR 786  799  ?   ?   ?   A . n 
A 1 787  ILE 787  800  ?   ?   ?   A . n 
A 1 788  ASP 788  801  ?   ?   ?   A . n 
A 1 789  CYS 789  802  ?   ?   ?   A . n 
A 1 790  SER 790  803  ?   ?   ?   A . n 
A 1 791  LEU 791  804  ?   ?   ?   A . n 
A 1 792  PHE 792  805  ?   ?   ?   A . n 
A 1 793  VAL 793  806  ?   ?   ?   A . n 
A 1 794  CYS 794  807  ?   ?   ?   A . n 
A 1 795  SER 795  808  ?   ?   ?   A . n 
A 1 796  ASN 796  809  ?   ?   ?   A . n 
A 1 797  TYR 797  810  ?   ?   ?   A . n 
A 1 798  ALA 798  811  ?   ?   ?   A . n 
A 1 799  ALA 799  812  ?   ?   ?   A . n 
A 1 800  CYS 800  813  ?   ?   ?   A . n 
A 1 801  HIS 801  814  ?   ?   ?   A . n 
A 1 802  ASP 802  815  ?   ?   ?   A . n 
A 1 803  LEU 803  816  ?   ?   ?   A . n 
A 1 804  LEU 804  817  ?   ?   ?   A . n 
A 1 805  SER 805  818  ?   ?   ?   A . n 
A 1 806  GLU 806  819  ?   ?   ?   A . n 
A 1 807  TYR 807  820  ?   ?   ?   A . n 
A 1 808  GLY 808  821  ?   ?   ?   A . n 
A 1 809  THR 809  822  ?   ?   ?   A . n 
A 1 810  PHE 810  823  ?   ?   ?   A . n 
A 1 811  CYS 811  824  ?   ?   ?   A . n 
A 1 812  ASP 812  825  ?   ?   ?   A . n 
A 1 813  ASN 813  826  ?   ?   ?   A . n 
A 1 814  ILE 814  827  ?   ?   ?   A . n 
A 1 815  ASN 815  828  ?   ?   ?   A . n 
A 1 816  SER 816  829  ?   ?   ?   A . n 
A 1 817  ILE 817  830  ?   ?   ?   A . n 
A 1 818  LEU 818  831  ?   ?   ?   A . n 
A 1 819  ASP 819  832  ?   ?   ?   A . n 
A 1 820  GLU 820  833  ?   ?   ?   A . n 
A 1 821  VAL 821  834  ?   ?   ?   A . n 
A 1 822  ASN 822  835  ?   ?   ?   A . n 
A 1 823  GLY 823  836  ?   ?   ?   A . n 
A 1 824  LEU 824  837  ?   ?   ?   A . n 
A 1 825  LEU 825  838  ?   ?   ?   A . n 
A 1 826  ASP 826  839  ?   ?   ?   A . n 
A 1 827  THR 827  840  ?   ?   ?   A . n 
A 1 828  THR 828  841  ?   ?   ?   A . n 
A 1 829  GLN 829  842  ?   ?   ?   A . n 
A 1 830  LEU 830  843  ?   ?   ?   A . n 
A 1 831  HIS 831  844  ?   ?   ?   A . n 
A 1 832  VAL 832  845  ?   ?   ?   A . n 
A 1 833  ALA 833  846  ?   ?   ?   A . n 
A 1 834  ASP 834  847  ?   ?   ?   A . n 
A 1 835  THR 835  848  ?   ?   ?   A . n 
A 1 836  LEU 836  849  ?   ?   ?   A . n 
A 1 837  MET 837  850  ?   ?   ?   A . n 
A 1 838  GLN 838  851  ?   ?   ?   A . n 
A 1 839  GLY 839  852  ?   ?   ?   A . n 
A 1 840  VAL 840  853  ?   ?   ?   A . n 
A 1 841  THR 841  854  ?   ?   ?   A . n 
A 1 842  LEU 842  855  ?   ?   ?   A . n 
A 1 843  SER 843  856  ?   ?   ?   A . n 
A 1 844  SER 844  857  ?   ?   ?   A . n 
A 1 845  ASN 845  858  ?   ?   ?   A . n 
A 1 846  LEU 846  859  ?   ?   ?   A . n 
A 1 847  ASN 847  860  ?   ?   ?   A . n 
A 1 848  THR 848  861  ?   ?   ?   A . n 
A 1 849  ASN 849  862  ?   ?   ?   A . n 
A 1 850  LEU 850  863  ?   ?   ?   A . n 
A 1 851  HIS 851  864  ?   ?   ?   A . n 
A 1 852  PHE 852  865  ?   ?   ?   A . n 
A 1 853  ASP 853  866  ?   ?   ?   A . n 
A 1 854  VAL 854  867  ?   ?   ?   A . n 
A 1 855  ASP 855  868  ?   ?   ?   A . n 
A 1 856  ASN 856  869  ?   ?   ?   A . n 
A 1 857  ILE 857  870  ?   ?   ?   A . n 
A 1 858  ASN 858  871  ?   ?   ?   A . n 
A 1 859  PHE 859  872  ?   ?   ?   A . n 
A 1 860  LYS 860  873  ?   ?   ?   A . n 
A 1 861  SER 861  874  ?   ?   ?   A . n 
A 1 862  LEU 862  875  ?   ?   ?   A . n 
A 1 863  VAL 863  876  ?   ?   ?   A . n 
A 1 864  GLY 864  877  ?   ?   ?   A . n 
A 1 865  CYS 865  878  ?   ?   ?   A . n 
A 1 866  LEU 866  879  ?   ?   ?   A . n 
A 1 867  GLY 867  880  ?   ?   ?   A . n 
A 1 868  PRO 868  881  ?   ?   ?   A . n 
A 1 869  HIS 869  882  ?   ?   ?   A . n 
A 1 870  CYS 870  883  ?   ?   ?   A . n 
A 1 871  GLY 871  884  ?   ?   ?   A . n 
A 1 872  SER 872  885  ?   ?   ?   A . n 
A 1 873  SER 873  886  ?   ?   ?   A . n 
A 1 874  SER 874  887  ?   ?   ?   A . n 
A 1 875  ARG 875  888  ?   ?   ?   A . n 
A 1 876  SER 876  889  ?   ?   ?   A . n 
A 1 877  PHE 877  890  ?   ?   ?   A . n 
A 1 878  PHE 878  891  ?   ?   ?   A . n 
A 1 879  GLU 879  892  ?   ?   ?   A . n 
A 1 880  ASP 880  893  ?   ?   ?   A . n 
A 1 881  LEU 881  894  ?   ?   ?   A . n 
A 1 882  LEU 882  895  ?   ?   ?   A . n 
A 1 883  PHE 883  896  ?   ?   ?   A . n 
A 1 884  ASP 884  897  ?   ?   ?   A . n 
A 1 885  LYS 885  898  ?   ?   ?   A . n 
A 1 886  VAL 886  899  ?   ?   ?   A . n 
A 1 887  LYS 887  900  ?   ?   ?   A . n 
A 1 888  LEU 888  901  ?   ?   ?   A . n 
A 1 889  SER 889  902  ?   ?   ?   A . n 
A 1 890  ASP 890  903  ?   ?   ?   A . n 
A 1 891  VAL 891  904  ?   ?   ?   A . n 
A 1 892  GLY 892  905  ?   ?   ?   A . n 
A 1 893  PHE 893  906  ?   ?   ?   A . n 
A 1 894  VAL 894  907  ?   ?   ?   A . n 
A 1 895  GLU 895  908  ?   ?   ?   A . n 
A 1 896  ALA 896  909  ?   ?   ?   A . n 
A 1 897  TYR 897  910  ?   ?   ?   A . n 
A 1 898  ASN 898  911  ?   ?   ?   A . n 
A 1 899  ASN 899  912  ?   ?   ?   A . n 
A 1 900  CYS 900  913  ?   ?   ?   A . n 
A 1 901  THR 901  914  ?   ?   ?   A . n 
A 1 902  GLY 902  915  ?   ?   ?   A . n 
A 1 903  GLY 903  916  ?   ?   ?   A . n 
A 1 904  SER 904  917  ?   ?   ?   A . n 
A 1 905  GLU 905  918  ?   ?   ?   A . n 
A 1 906  ILE 906  919  ?   ?   ?   A . n 
A 1 907  ARG 907  920  ?   ?   ?   A . n 
A 1 908  ASP 908  921  ?   ?   ?   A . n 
A 1 909  LEU 909  922  ?   ?   ?   A . n 
A 1 910  LEU 910  923  ?   ?   ?   A . n 
A 1 911  CYS 911  924  ?   ?   ?   A . n 
A 1 912  VAL 912  925  ?   ?   ?   A . n 
A 1 913  GLN 913  926  ?   ?   ?   A . n 
A 1 914  SER 914  927  ?   ?   ?   A . n 
A 1 915  PHE 915  928  ?   ?   ?   A . n 
A 1 916  ASN 916  929  ?   ?   ?   A . n 
A 1 917  GLY 917  930  ?   ?   ?   A . n 
A 1 918  ILE 918  931  ?   ?   ?   A . n 
A 1 919  LYS 919  932  ?   ?   ?   A . n 
A 1 920  VAL 920  933  ?   ?   ?   A . n 
A 1 921  LEU 921  934  ?   ?   ?   A . n 
A 1 922  PRO 922  935  ?   ?   ?   A . n 
A 1 923  PRO 923  936  ?   ?   ?   A . n 
A 1 924  ILE 924  937  ?   ?   ?   A . n 
A 1 925  LEU 925  938  ?   ?   ?   A . n 
A 1 926  SER 926  939  ?   ?   ?   A . n 
A 1 927  GLU 927  940  ?   ?   ?   A . n 
A 1 928  SER 928  941  ?   ?   ?   A . n 
A 1 929  GLN 929  942  ?   ?   ?   A . n 
A 1 930  ILE 930  943  ?   ?   ?   A . n 
A 1 931  SER 931  944  ?   ?   ?   A . n 
A 1 932  GLY 932  945  ?   ?   ?   A . n 
A 1 933  TYR 933  946  ?   ?   ?   A . n 
A 1 934  THR 934  947  ?   ?   ?   A . n 
A 1 935  THR 935  948  ?   ?   ?   A . n 
A 1 936  ALA 936  949  ?   ?   ?   A . n 
A 1 937  ALA 937  950  ?   ?   ?   A . n 
A 1 938  THR 938  951  ?   ?   ?   A . n 
A 1 939  VAL 939  952  ?   ?   ?   A . n 
A 1 940  ALA 940  953  ?   ?   ?   A . n 
A 1 941  ALA 941  954  ?   ?   ?   A . n 
A 1 942  MET 942  955  ?   ?   ?   A . n 
A 1 943  PHE 943  956  ?   ?   ?   A . n 
A 1 944  PRO 944  957  ?   ?   ?   A . n 
A 1 945  PRO 945  958  ?   ?   ?   A . n 
A 1 946  TRP 946  959  ?   ?   ?   A . n 
A 1 947  SER 947  960  ?   ?   ?   A . n 
A 1 948  ALA 948  961  ?   ?   ?   A . n 
A 1 949  ALA 949  962  ?   ?   ?   A . n 
A 1 950  ALA 950  963  ?   ?   ?   A . n 
A 1 951  GLY 951  964  ?   ?   ?   A . n 
A 1 952  ILE 952  965  ?   ?   ?   A . n 
A 1 953  PRO 953  966  ?   ?   ?   A . n 
A 1 954  PHE 954  967  ?   ?   ?   A . n 
A 1 955  SER 955  968  ?   ?   ?   A . n 
A 1 956  LEU 956  969  ?   ?   ?   A . n 
A 1 957  ASN 957  970  ?   ?   ?   A . n 
A 1 958  VAL 958  971  ?   ?   ?   A . n 
A 1 959  GLN 959  972  ?   ?   ?   A . n 
A 1 960  TYR 960  973  ?   ?   ?   A . n 
A 1 961  ARG 961  974  ?   ?   ?   A . n 
A 1 962  ILE 962  975  ?   ?   ?   A . n 
A 1 963  ASN 963  976  ?   ?   ?   A . n 
A 1 964  GLY 964  977  ?   ?   ?   A . n 
A 1 965  LEU 965  978  ?   ?   ?   A . n 
A 1 966  GLY 966  979  ?   ?   ?   A . n 
A 1 967  VAL 967  980  ?   ?   ?   A . n 
A 1 968  THR 968  981  ?   ?   ?   A . n 
A 1 969  MET 969  982  ?   ?   ?   A . n 
A 1 970  ASP 970  983  ?   ?   ?   A . n 
A 1 971  VAL 971  984  ?   ?   ?   A . n 
A 1 972  LEU 972  985  ?   ?   ?   A . n 
A 1 973  ASN 973  986  ?   ?   ?   A . n 
A 1 974  LYS 974  987  ?   ?   ?   A . n 
A 1 975  ASN 975  988  ?   ?   ?   A . n 
A 1 976  GLN 976  989  ?   ?   ?   A . n 
A 1 977  LYS 977  990  ?   ?   ?   A . n 
A 1 978  LEU 978  991  ?   ?   ?   A . n 
A 1 979  ILE 979  992  ?   ?   ?   A . n 
A 1 980  ALA 980  993  ?   ?   ?   A . n 
A 1 981  THR 981  994  ?   ?   ?   A . n 
A 1 982  ALA 982  995  ?   ?   ?   A . n 
A 1 983  PHE 983  996  ?   ?   ?   A . n 
A 1 984  ASN 984  997  ?   ?   ?   A . n 
A 1 985  ASN 985  998  ?   ?   ?   A . n 
A 1 986  ALA 986  999  ?   ?   ?   A . n 
A 1 987  LEU 987  1000 ?   ?   ?   A . n 
A 1 988  LEU 988  1001 ?   ?   ?   A . n 
A 1 989  SER 989  1002 ?   ?   ?   A . n 
A 1 990  ILE 990  1003 ?   ?   ?   A . n 
A 1 991  GLN 991  1004 ?   ?   ?   A . n 
A 1 992  ASN 992  1005 ?   ?   ?   A . n 
A 1 993  GLY 993  1006 ?   ?   ?   A . n 
A 1 994  PHE 994  1007 ?   ?   ?   A . n 
A 1 995  SER 995  1008 ?   ?   ?   A . n 
A 1 996  ALA 996  1009 ?   ?   ?   A . n 
A 1 997  PRO 997  1010 ?   ?   ?   A . n 
A 1 998  ASN 998  1011 ?   ?   ?   A . n 
A 1 999  SER 999  1012 ?   ?   ?   A . n 
A 1 1000 ALA 1000 1013 ?   ?   ?   A . n 
A 1 1001 LEU 1001 1014 ?   ?   ?   A . n 
A 1 1002 ALA 1002 1015 ?   ?   ?   A . n 
A 1 1003 LYS 1003 1016 ?   ?   ?   A . n 
A 1 1004 ILE 1004 1017 ?   ?   ?   A . n 
A 1 1005 GLN 1005 1018 ?   ?   ?   A . n 
A 1 1006 SER 1006 1019 ?   ?   ?   A . n 
A 1 1007 VAL 1007 1020 ?   ?   ?   A . n 
A 1 1008 VAL 1008 1021 ?   ?   ?   A . n 
A 1 1009 ASN 1009 1022 ?   ?   ?   A . n 
A 1 1010 SER 1010 1023 ?   ?   ?   A . n 
A 1 1011 ASN 1011 1024 ?   ?   ?   A . n 
A 1 1012 ALA 1012 1025 ?   ?   ?   A . n 
A 1 1013 GLN 1013 1026 ?   ?   ?   A . n 
A 1 1014 ALA 1014 1027 ?   ?   ?   A . n 
A 1 1015 LEU 1015 1028 ?   ?   ?   A . n 
A 1 1016 ASN 1016 1029 ?   ?   ?   A . n 
A 1 1017 SER 1017 1030 ?   ?   ?   A . n 
A 1 1018 LEU 1018 1031 ?   ?   ?   A . n 
A 1 1019 LEU 1019 1032 ?   ?   ?   A . n 
A 1 1020 GLN 1020 1033 ?   ?   ?   A . n 
A 1 1021 GLN 1021 1034 ?   ?   ?   A . n 
A 1 1022 LEU 1022 1035 ?   ?   ?   A . n 
A 1 1023 PHE 1023 1036 ?   ?   ?   A . n 
A 1 1024 ASN 1024 1037 ?   ?   ?   A . n 
A 1 1025 LYS 1025 1038 ?   ?   ?   A . n 
A 1 1026 PHE 1026 1039 ?   ?   ?   A . n 
A 1 1027 GLY 1027 1040 ?   ?   ?   A . n 
A 1 1028 ALA 1028 1041 ?   ?   ?   A . n 
A 1 1029 ILE 1029 1042 ?   ?   ?   A . n 
A 1 1030 SER 1030 1043 ?   ?   ?   A . n 
A 1 1031 SER 1031 1044 ?   ?   ?   A . n 
A 1 1032 SER 1032 1045 ?   ?   ?   A . n 
A 1 1033 LEU 1033 1046 ?   ?   ?   A . n 
A 1 1034 GLN 1034 1047 ?   ?   ?   A . n 
A 1 1035 GLU 1035 1048 ?   ?   ?   A . n 
A 1 1036 ILE 1036 1049 ?   ?   ?   A . n 
A 1 1037 LEU 1037 1050 ?   ?   ?   A . n 
A 1 1038 SER 1038 1051 ?   ?   ?   A . n 
A 1 1039 ARG 1039 1052 ?   ?   ?   A . n 
A 1 1040 LEU 1040 1053 ?   ?   ?   A . n 
A 1 1041 ASP 1041 1054 ?   ?   ?   A . n 
A 1 1042 PRO 1042 1055 ?   ?   ?   A . n 
A 1 1043 PRO 1043 1056 ?   ?   ?   A . n 
A 1 1044 GLU 1044 1057 ?   ?   ?   A . n 
A 1 1045 ALA 1045 1058 ?   ?   ?   A . n 
A 1 1046 GLN 1046 1059 ?   ?   ?   A . n 
A 1 1047 VAL 1047 1060 ?   ?   ?   A . n 
A 1 1048 GLN 1048 1061 ?   ?   ?   A . n 
A 1 1049 ILE 1049 1062 ?   ?   ?   A . n 
A 1 1050 ASP 1050 1063 ?   ?   ?   A . n 
A 1 1051 ARG 1051 1064 ?   ?   ?   A . n 
A 1 1052 LEU 1052 1065 ?   ?   ?   A . n 
A 1 1053 ILE 1053 1066 ?   ?   ?   A . n 
A 1 1054 ASN 1054 1067 ?   ?   ?   A . n 
A 1 1055 GLY 1055 1068 ?   ?   ?   A . n 
A 1 1056 ARG 1056 1069 ?   ?   ?   A . n 
A 1 1057 LEU 1057 1070 ?   ?   ?   A . n 
A 1 1058 THR 1058 1071 ?   ?   ?   A . n 
A 1 1059 ALA 1059 1072 ?   ?   ?   A . n 
A 1 1060 LEU 1060 1073 ?   ?   ?   A . n 
A 1 1061 ASN 1061 1074 ?   ?   ?   A . n 
A 1 1062 ALA 1062 1075 ?   ?   ?   A . n 
A 1 1063 TYR 1063 1076 ?   ?   ?   A . n 
A 1 1064 VAL 1064 1077 ?   ?   ?   A . n 
A 1 1065 SER 1065 1078 ?   ?   ?   A . n 
A 1 1066 GLN 1066 1079 ?   ?   ?   A . n 
A 1 1067 GLN 1067 1080 ?   ?   ?   A . n 
A 1 1068 LEU 1068 1081 ?   ?   ?   A . n 
A 1 1069 SER 1069 1082 ?   ?   ?   A . n 
A 1 1070 ASP 1070 1083 ?   ?   ?   A . n 
A 1 1071 ILE 1071 1084 ?   ?   ?   A . n 
A 1 1072 SER 1072 1085 ?   ?   ?   A . n 
A 1 1073 LEU 1073 1086 ?   ?   ?   A . n 
A 1 1074 VAL 1074 1087 ?   ?   ?   A . n 
A 1 1075 LYS 1075 1088 ?   ?   ?   A . n 
A 1 1076 PHE 1076 1089 ?   ?   ?   A . n 
A 1 1077 GLY 1077 1090 ?   ?   ?   A . n 
A 1 1078 ALA 1078 1091 ?   ?   ?   A . n 
A 1 1079 ALA 1079 1092 ?   ?   ?   A . n 
A 1 1080 LEU 1080 1093 ?   ?   ?   A . n 
A 1 1081 ALA 1081 1094 ?   ?   ?   A . n 
A 1 1082 MET 1082 1095 ?   ?   ?   A . n 
A 1 1083 GLU 1083 1096 ?   ?   ?   A . n 
A 1 1084 LYS 1084 1097 ?   ?   ?   A . n 
A 1 1085 VAL 1085 1098 ?   ?   ?   A . n 
A 1 1086 ASN 1086 1099 ?   ?   ?   A . n 
A 1 1087 GLU 1087 1100 ?   ?   ?   A . n 
A 1 1088 CYS 1088 1101 ?   ?   ?   A . n 
A 1 1089 VAL 1089 1102 ?   ?   ?   A . n 
A 1 1090 LYS 1090 1103 ?   ?   ?   A . n 
A 1 1091 SER 1091 1104 ?   ?   ?   A . n 
A 1 1092 GLN 1092 1105 ?   ?   ?   A . n 
A 1 1093 SER 1093 1106 ?   ?   ?   A . n 
A 1 1094 PRO 1094 1107 ?   ?   ?   A . n 
A 1 1095 ARG 1095 1108 ?   ?   ?   A . n 
A 1 1096 ILE 1096 1109 ?   ?   ?   A . n 
A 1 1097 ASN 1097 1110 ?   ?   ?   A . n 
A 1 1098 PHE 1098 1111 ?   ?   ?   A . n 
A 1 1099 CYS 1099 1112 ?   ?   ?   A . n 
A 1 1100 GLY 1100 1113 ?   ?   ?   A . n 
A 1 1101 ASN 1101 1114 ?   ?   ?   A . n 
A 1 1102 GLY 1102 1115 ?   ?   ?   A . n 
A 1 1103 ASN 1103 1116 ?   ?   ?   A . n 
A 1 1104 HIS 1104 1117 ?   ?   ?   A . n 
A 1 1105 ILE 1105 1118 ?   ?   ?   A . n 
A 1 1106 LEU 1106 1119 ?   ?   ?   A . n 
A 1 1107 SER 1107 1120 ?   ?   ?   A . n 
A 1 1108 LEU 1108 1121 ?   ?   ?   A . n 
A 1 1109 VAL 1109 1122 ?   ?   ?   A . n 
A 1 1110 GLN 1110 1123 ?   ?   ?   A . n 
A 1 1111 ASN 1111 1124 ?   ?   ?   A . n 
A 1 1112 ALA 1112 1125 ?   ?   ?   A . n 
A 1 1113 PRO 1113 1126 ?   ?   ?   A . n 
A 1 1114 TYR 1114 1127 ?   ?   ?   A . n 
A 1 1115 GLY 1115 1128 ?   ?   ?   A . n 
A 1 1116 LEU 1116 1129 ?   ?   ?   A . n 
A 1 1117 LEU 1117 1130 ?   ?   ?   A . n 
A 1 1118 PHE 1118 1131 ?   ?   ?   A . n 
A 1 1119 MET 1119 1132 ?   ?   ?   A . n 
A 1 1120 HIS 1120 1133 ?   ?   ?   A . n 
A 1 1121 PHE 1121 1134 ?   ?   ?   A . n 
A 1 1122 SER 1122 1135 ?   ?   ?   A . n 
A 1 1123 TYR 1123 1136 ?   ?   ?   A . n 
A 1 1124 LYS 1124 1137 ?   ?   ?   A . n 
A 1 1125 PRO 1125 1138 ?   ?   ?   A . n 
A 1 1126 ILE 1126 1139 ?   ?   ?   A . n 
A 1 1127 SER 1127 1140 ?   ?   ?   A . n 
A 1 1128 PHE 1128 1141 ?   ?   ?   A . n 
A 1 1129 LYS 1129 1142 ?   ?   ?   A . n 
A 1 1130 THR 1130 1143 ?   ?   ?   A . n 
A 1 1131 VAL 1131 1144 ?   ?   ?   A . n 
A 1 1132 LEU 1132 1145 ?   ?   ?   A . n 
A 1 1133 VAL 1133 1146 ?   ?   ?   A . n 
A 1 1134 SER 1134 1147 ?   ?   ?   A . n 
A 1 1135 PRO 1135 1148 ?   ?   ?   A . n 
A 1 1136 GLY 1136 1149 ?   ?   ?   A . n 
A 1 1137 LEU 1137 1150 ?   ?   ?   A . n 
A 1 1138 CYS 1138 1151 ?   ?   ?   A . n 
A 1 1139 ILE 1139 1152 ?   ?   ?   A . n 
A 1 1140 SER 1140 1153 ?   ?   ?   A . n 
A 1 1141 GLY 1141 1154 ?   ?   ?   A . n 
A 1 1142 ASP 1142 1155 ?   ?   ?   A . n 
A 1 1143 VAL 1143 1156 ?   ?   ?   A . n 
A 1 1144 GLY 1144 1157 ?   ?   ?   A . n 
A 1 1145 ILE 1145 1158 ?   ?   ?   A . n 
A 1 1146 ALA 1146 1159 ?   ?   ?   A . n 
A 1 1147 PRO 1147 1160 ?   ?   ?   A . n 
A 1 1148 LYS 1148 1161 ?   ?   ?   A . n 
A 1 1149 GLN 1149 1162 ?   ?   ?   A . n 
A 1 1150 GLY 1150 1163 ?   ?   ?   A . n 
A 1 1151 TYR 1151 1164 ?   ?   ?   A . n 
A 1 1152 PHE 1152 1165 ?   ?   ?   A . n 
A 1 1153 ILE 1153 1166 ?   ?   ?   A . n 
A 1 1154 LYS 1154 1167 ?   ?   ?   A . n 
A 1 1155 HIS 1155 1168 ?   ?   ?   A . n 
A 1 1156 ASN 1156 1169 ?   ?   ?   A . n 
A 1 1157 ASP 1157 1170 ?   ?   ?   A . n 
A 1 1158 HIS 1158 1171 ?   ?   ?   A . n 
A 1 1159 TRP 1159 1172 ?   ?   ?   A . n 
A 1 1160 MET 1160 1173 ?   ?   ?   A . n 
A 1 1161 PHE 1161 1174 ?   ?   ?   A . n 
A 1 1162 THR 1162 1175 ?   ?   ?   A . n 
A 1 1163 GLY 1163 1176 ?   ?   ?   A . n 
A 1 1164 SER 1164 1177 ?   ?   ?   A . n 
A 1 1165 SER 1165 1178 ?   ?   ?   A . n 
A 1 1166 TYR 1166 1179 ?   ?   ?   A . n 
A 1 1167 TYR 1167 1180 ?   ?   ?   A . n 
A 1 1168 TYR 1168 1181 ?   ?   ?   A . n 
A 1 1169 PRO 1169 1182 ?   ?   ?   A . n 
A 1 1170 GLU 1170 1183 ?   ?   ?   A . n 
A 1 1171 PRO 1171 1184 ?   ?   ?   A . n 
A 1 1172 ILE 1172 1185 ?   ?   ?   A . n 
A 1 1173 SER 1173 1186 ?   ?   ?   A . n 
A 1 1174 ASP 1174 1187 ?   ?   ?   A . n 
A 1 1175 LYS 1175 1188 ?   ?   ?   A . n 
A 1 1176 ASN 1176 1189 ?   ?   ?   A . n 
A 1 1177 VAL 1177 1190 ?   ?   ?   A . n 
A 1 1178 VAL 1178 1191 ?   ?   ?   A . n 
A 1 1179 PHE 1179 1192 ?   ?   ?   A . n 
A 1 1180 MET 1180 1193 ?   ?   ?   A . n 
A 1 1181 ASN 1181 1194 ?   ?   ?   A . n 
A 1 1182 THR 1182 1195 ?   ?   ?   A . n 
A 1 1183 CYS 1183 1196 ?   ?   ?   A . n 
A 1 1184 SER 1184 1197 ?   ?   ?   A . n 
A 1 1185 VAL 1185 1198 ?   ?   ?   A . n 
A 1 1186 ASN 1186 1199 ?   ?   ?   A . n 
A 1 1187 PHE 1187 1200 ?   ?   ?   A . n 
A 1 1188 THR 1188 1201 ?   ?   ?   A . n 
A 1 1189 LYS 1189 1202 ?   ?   ?   A . n 
A 1 1190 ALA 1190 1203 ?   ?   ?   A . n 
A 1 1191 PRO 1191 1204 ?   ?   ?   A . n 
A 1 1192 LEU 1192 1205 ?   ?   ?   A . n 
A 1 1193 VAL 1193 1206 ?   ?   ?   A . n 
A 1 1194 TYR 1194 1207 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 A NAG 1227 n 
B 2 NAG 2 B NAG 2 A NAG 1228 n 
B 2 BMA 3 B BMA 3 A BMA 1229 n 
B 2 MAN 4 B MAN 4 A MAN 1230 n 
B 2 MAN 5 B MAN 5 A MAN 1231 n 
C 3 NAG 1 C NAG 1 A NAG 1233 n 
C 3 NAG 2 C NAG 2 A NAG 1234 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AR1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AR1 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 NAG   1 1301 1224 NAG   NAG A . 
E 4 NAG   1 1302 1225 NAG   NAG A . 
F 4 NAG   1 1303 1226 NAG   NAG A . 
G 4 NAG   1 1304 1232 NAG   NAG A . 
H 4 NAG   1 1305 1235 NAG   NAG A . 
I 4 NAG   1 1306 1236 NAG   NAG A . 
J 5 A1AR1 1 1307 1    A1AR1 DSA A . 
# 
_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                     9BTC 
_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                         9BTC 
_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                   9BTC 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BTC 
_struct.title                        
'Cryo-EM density map of HKU1 spike glycoprotein D1 domain in complex with 9O-acetyl GD3 sialoglycan (Up state, locally refined)' 
_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        9BTC 
_struct_keywords.text            'HKU1 spike glycoprotein ectodomain, proline stablized, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SPIKE_CVHN1 
_struct_ref.pdbx_db_accession          Q5MQD0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VIGDFNCTNFAINDLNTTVPRISEYVVDVSYGLGTYYILDRVYLNTTILFTGYFPKSGANFRDLSLKGTTYLSTLWYQKP
FLSDFNNGIFSRVKNTKLYVNKTLYSEFSTIVIGSVFINNSYTIVVQPHNGVLEITACQYTMCEYPHTICKSKGSSRNES
WHFDKSEPLCLFKKNFTYNVSTDWLYFHFYQERGTFYAYYADSGMPTTFLFSLYLGTLLSHYYVLPLTCNAISSNTDNET
LQYWVTPLSKRQYLLKFDNRGVITNAVDCSSSFFSEIQCKTKSLLPNTGVYDLSGFTVKPVATVHRRIPDLPDCDIDKWL
NNFNVPSPLNWERKIFSNCNFNLSTLLRLVHTDSFSCNNFDESKIYGSCFKSIVLDKFAIPNSRRSDLQLGSSGFLQSSN
YKIDTTSSSCQLYYSLPAINVTINNYNPSSWNRRYGFNNFNLSSHSVVYSRYCFSVNNTFCPCAKPSFASSCKSHKPPSA
SCPIGTNYRSCESTTVLDHTDWCRCSCLPDPITAYDPRSCSQKKSLVGVGEHCAGFGVDEEKCGVLDGSYNVSCLCSTDA
FLGWSYDTCVSNNRCNIFSNFILNGINSGTTCSNDLLQPNTEVFTDVCVDYDLYGITGQGIFKEVSAVYYNSWQNLLYDS
NGNIIGFKDFVTNKTYNIFPCYAGRVSAAFHQNASSLALLYRNLKCSYVLNNISLTTQPYFDSYLGCVFNADNLTDYSVS
SCALRMGSGFCVDYNSPSSSSSRRKRRSISASYRFVTFEPFNVSFVNDSIESVGGLYEIKIPTNFTIVGQEEFIQTNSPK
VTIDCSLFVCSNYAACHDLLSEYGTFCDNINSILDEVNGLLDTTQLHVADTLMQGVTLSSNLNTNLHFDVDNINFKSLVG
CLGPHCGSSSRSFFEDLLFDKVKLSDVGFVEAYNNCTGGSEIRDLLCVQSFNGIKVLPPILSESQISGYTTAATVAAMFP
PWSAAAGIPFSLNVQYRINGLGVTMDVLNKNQKLIATAFNNALLSIQNGFSATNSALAKIQSVVNSNAQALNSLLQQLFN
KFGAISSSLQEILSRLDALEAQVQIDRLINGRLTALNAYVSQQLSDISLVKFGAALAMEKVNECVKSQSPRINFCGNGNH
ILSLVQNAPYGLLFMHFSYKPISFKTVLVSPGLCISGDVGIAPKQGYFIKHNDHWMFTGSSYYYPEPISDKNVVFMNTCS
VNFTKAPLVY
;
_struct_ref.pdbx_align_begin           14 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BTC 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1194 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q5MQD0 
_struct_ref_seq.db_align_beg                  14 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1223 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       14 
_struct_ref_seq.pdbx_auth_seq_align_end       1207 
# 
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 9BTC ?   A ?    ? UNP Q5MQD0 SER 749  deletion ?    1  
1 9BTC ?   A ?    ? UNP Q5MQD0 PRO 750  deletion ?    2  
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 751  deletion ?    3  
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 752  deletion ?    4  
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 753  deletion ?    5  
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 754  deletion ?    6  
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 755  deletion ?    7  
1 9BTC ?   A ?    ? UNP Q5MQD0 ARG 756  deletion ?    8  
1 9BTC ?   A ?    ? UNP Q5MQD0 ARG 757  deletion ?    9  
1 9BTC ?   A ?    ? UNP Q5MQD0 LYS 758  deletion ?    10 
1 9BTC ?   A ?    ? UNP Q5MQD0 ARG 759  deletion ?    11 
1 9BTC ?   A ?    ? UNP Q5MQD0 ARG 760  deletion ?    12 
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 761  deletion ?    13 
1 9BTC ?   A ?    ? UNP Q5MQD0 ILE 762  deletion ?    14 
1 9BTC ?   A ?    ? UNP Q5MQD0 SER 763  deletion ?    15 
1 9BTC ?   A ?    ? UNP Q5MQD0 ALA 764  deletion ?    16 
1 9BTC PRO A 997  ? UNP Q5MQD0 THR 1026 conflict 1010 17 
1 9BTC PRO A 1042 ? UNP Q5MQD0 ALA 1071 conflict 1055 18 
1 9BTC PRO A 1043 ? UNP Q5MQD0 LEU 1072 conflict 1056 19 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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 
# 
_struct_conf.conf_type_id            HELX_P 
_struct_conf.id                      HELX_P1 
_struct_conf.pdbx_PDB_helix_id       AA1 
_struct_conf.beg_label_comp_id       LEU 
_struct_conf.beg_label_asym_id       A 
_struct_conf.beg_label_seq_id        75 
_struct_conf.pdbx_beg_PDB_ins_code   ? 
_struct_conf.end_label_comp_id       GLN 
_struct_conf.end_label_asym_id       A 
_struct_conf.end_label_seq_id        78 
_struct_conf.pdbx_end_PDB_ins_code   ? 
_struct_conf.beg_auth_comp_id        LEU 
_struct_conf.beg_auth_asym_id        A 
_struct_conf.beg_auth_seq_id         88 
_struct_conf.end_auth_comp_id        GLN 
_struct_conf.end_auth_asym_id        A 
_struct_conf.end_auth_seq_id         91 
_struct_conf.pdbx_PDB_helix_class    5 
_struct_conf.details                 ? 
_struct_conf.pdbx_PDB_helix_length   4 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 7   SG  ? ? ? 1_555 A CYS 143 SG ? ? A CYS 20  A CYS 156  1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf2  disulf ?    ? A CYS 138 SG  ? ? ? 1_555 A CYS 170 SG ? ? A CYS 151 A CYS 183  1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf3  disulf ?    ? A CYS 150 SG  ? ? ? 1_555 A CYS 229 SG ? ? A CYS 163 A CYS 242  1_555 ? ? ? ? ? ? ? 2.018 ? ?               
covale1  covale one  ? A ASN 6   ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 19  A NAG 1301 1_555 ? ? ? ? ? ? ? 1.454 ? N-Glycosylation 
covale2  covale one  ? A ASN 16  ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 29  A NAG 1302 1_555 ? ? ? ? ? ? ? 1.453 ? N-Glycosylation 
covale3  covale one  ? A ASN 45  ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 58  A NAG 1303 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale4  covale one  ? A ASN 119 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 132 B NAG 1    1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale5  covale one  ? A ASN 158 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 171 A NAG 1304 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale6  covale one  ? A ASN 175 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 188 C NAG 1    1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale7  covale one  ? A ASN 179 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 192 A NAG 1305 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale8  covale one  ? A ASN 238 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 251 A NAG 1306 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale9  covale both ? B NAG .   O4  ? ? ? 1_555 B NAG .   C1 ? ? B NAG 1   B NAG 2    1_555 ? ? ? ? ? ? ? 1.458 ? ?               
covale10 covale both ? B NAG .   O4  ? ? ? 1_555 B BMA .   C1 ? ? B NAG 2   B BMA 3    1_555 ? ? ? ? ? ? ? 1.468 ? ?               
covale11 covale both ? B BMA .   O3  ? ? ? 1_555 B MAN .   C1 ? ? B BMA 3   B MAN 4    1_555 ? ? ? ? ? ? ? 1.465 ? ?               
covale12 covale both ? B BMA .   O6  ? ? ? 1_555 B MAN .   C1 ? ? B BMA 3   B MAN 5    1_555 ? ? ? ? ? ? ? 1.460 ? ?               
covale13 covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2    1_555 ? ? ? ? ? ? ? 1.469 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG B .   ? ASN A 119 ? NAG B 1    ? 1_555 ASN A 132 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG C .   ? ASN A 175 ? NAG C 1    ? 1_555 ASN A 188 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG D .   ? ASN A 6   ? NAG A 1301 ? 1_555 ASN A 19  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG E .   ? ASN A 16  ? NAG A 1302 ? 1_555 ASN A 29  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG F .   ? ASN A 45  ? NAG A 1303 ? 1_555 ASN A 58  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G .   ? ASN A 158 ? NAG A 1304 ? 1_555 ASN A 171 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H .   ? ASN A 179 ? NAG A 1305 ? 1_555 ASN A 192 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG I .   ? ASN A 238 ? NAG A 1306 ? 1_555 ASN A 251 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  CYS A 7   ? CYS A 143 ? CYS A 20   ? 1_555 CYS A 156 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS A 138 ? CYS A 170 ? CYS A 151  ? 1_555 CYS A 183 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS A 150 ? CYS A 229 ? CYS A 163  ? 1_555 CYS A 242 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LYS 
_struct_mon_prot_cis.label_seq_id           79 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LYS 
_struct_mon_prot_cis.auth_seq_id            92 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    80 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     93 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       9.94 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? 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 ILE A 12  ? ASN A 13  ? ILE A 25  ASN A 26  
AA1 2 LEU A 72  ? SER A 73  ? LEU A 85  SER A 86  
AA2 1 ARG A 21  ? ILE A 22  ? ARG A 34  ILE A 35  
AA2 2 ARG A 62  ? ASP A 63  ? ARG A 75  ASP A 76  
AA2 3 TYR A 243 ? PRO A 247 ? TYR A 256 PRO A 260 
AA2 4 GLY A 88  ? LYS A 94  ? GLY A 101 LYS A 107 
AA2 5 TRP A 184 ? GLU A 192 ? TRP A 197 GLU A 205 
AA2 6 THR A 195 ? ALA A 201 ? THR A 208 ALA A 214 
AA2 7 THR A 208 ? TYR A 214 ? THR A 221 TYR A 227 
AA3 1 THR A 46  ? PHE A 54  ? THR A 59  PHE A 67  
AA3 2 SER A 249 ? PHE A 257 ? SER A 262 PHE A 270 
AA3 3 ILE A 263 ? VAL A 267 ? ILE A 276 VAL A 280 
AA4 1 LYS A 67  ? GLY A 68  ? LYS A 80  GLY A 81  
AA4 2 LEU A 227 ? THR A 228 ? LEU A 240 THR A 241 
AA4 3 MET A 142 ? ILE A 149 ? MET A 155 ILE A 162 
AA4 4 SER A 160 ? HIS A 162 ? SER A 173 HIS A 175 
AA5 1 SER A 83  ? ASP A 84  ? SER A 96  ASP A 97  
AA5 2 HIS A 221 ? VAL A 224 ? HIS A 234 VAL A 237 
AA5 3 ILE A 111 ? GLY A 114 ? ILE A 124 GLY A 127 
AA5 4 THR A 123 ? HIS A 129 ? THR A 136 HIS A 142 
AA5 5 VAL A 132 ? CYS A 138 ? VAL A 145 CYS A 151 
AA5 6 CYS A 170 ? THR A 177 ? CYS A 183 THR A 190 
AA6 1 THR A 96  ? TYR A 99  ? THR A 109 TYR A 112 
AA6 2 LEU A 104 ? GLU A 107 ? LEU A 117 GLU A 120 
# 
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 ASN A 13  ? N ASN A 26  O LEU A 72  ? O LEU A 85  
AA2 1 2 N ARG A 21  ? N ARG A 34  O ASP A 63  ? O ASP A 76  
AA2 2 3 N ARG A 62  ? N ARG A 75  O VAL A 245 ? O VAL A 258 
AA2 3 4 O THR A 246 ? O THR A 259 N PHE A 90  ? N PHE A 103 
AA2 4 5 N VAL A 93  ? N VAL A 106 O LEU A 185 ? O LEU A 198 
AA2 5 6 N TYR A 186 ? N TYR A 199 O ALA A 201 ? O ALA A 214 
AA2 6 7 N TYR A 200 ? N TYR A 213 O THR A 208 ? O THR A 221 
AA3 1 2 N THR A 46  ? N THR A 59  O PHE A 257 ? O PHE A 270 
AA3 2 3 N LYS A 256 ? N LYS A 269 O ASN A 265 ? O ASN A 278 
AA4 1 2 N GLY A 68  ? N GLY A 81  O LEU A 227 ? O LEU A 240 
AA4 2 3 O THR A 228 ? O THR A 241 N THR A 148 ? N THR A 161 
AA4 3 4 N CYS A 143 ? N CYS A 156 O TRP A 161 ? O TRP A 174 
AA5 1 2 N SER A 83  ? N SER A 96  O TYR A 222 ? O TYR A 235 
AA5 2 3 O HIS A 221 ? O HIS A 234 N GLY A 114 ? N GLY A 127 
AA5 3 4 N ILE A 113 ? N ILE A 126 O ILE A 124 ? O ILE A 137 
AA5 4 5 N HIS A 129 ? N HIS A 142 O VAL A 132 ? O VAL A 145 
AA5 5 6 N LEU A 133 ? N LEU A 146 O PHE A 176 ? O PHE A 189 
AA6 1 2 N LEU A 98  ? N LEU A 111 O TYR A 105 ? O TYR A 118 
# 
_pdbx_entry_details.entry_id                   9BTC 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ILE A 15  ? ? -85.69  -82.38  
2  1 LEU A 52  ? ? 51.38   -134.95 
3  1 ASN A 58  ? ? 39.60   63.00   
4  1 THR A 82  ? ? -115.41 -97.04  
5  1 ASN A 99  ? ? 51.19   -122.49 
6  1 ASN A 114 ? ? -101.97 -127.67 
7  1 SER A 128 ? ? -130.41 -87.55  
8  1 ASN A 132 ? ? -69.36  10.17   
9  1 LYS A 186 ? ? -162.25 108.56  
10 1 ASN A 243 ? ? -86.71  40.64   
11 1 ASP A 250 ? ? -151.22 -5.00   
12 1 ASN A 251 ? ? 56.30   13.74   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     49 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.072 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BTC 
_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      'FLEXIBLE FIT' 
# 
_em_3d_reconstruction.entry_id                    9BTC 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     
;Symmetry-expanded particles are classified focused at D1 domain. Particles with D1 domain in up state are used in final local refinement and reconstruction with D1-only Mask.
;
_em_3d_reconstruction.resolution                  2.41 
_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               3576676 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Human coronavirus HKU1 spike glycoprotein' 
_em_entity_assembly.details              'Ectodomain generated by recombinant expression in HEK293 Freestyle cells' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BTC 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_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                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             1800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           75000 
_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                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    ? 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        C-flat-2/2 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_virus_entity.id                    1 
_em_virus_entity.virus_host_category   ? 
_em_virus_entity.virus_type            VIRION 
_em_virus_entity.virus_isolate         ? 
_em_virus_entity.entity_assembly_id    1 
_em_virus_entity.enveloped             ? 
_em_virus_entity.empty                 ? 
_em_virus_entity.details               ? 
# 
_em_vitrification.entry_id              9BTC 
_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               ? 
# 
_em_experiment.entry_id                9BTC 
_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              9BTC 
_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 CYS 282  ? A CYS 269  
2   1 Y 1 A SER 283  ? A SER 270  
3   1 Y 1 A SER 284  ? A SER 271  
4   1 Y 1 A SER 285  ? A SER 272  
5   1 Y 1 A PHE 286  ? A PHE 273  
6   1 Y 1 A PHE 287  ? A PHE 274  
7   1 Y 1 A SER 288  ? A SER 275  
8   1 Y 1 A GLU 289  ? A GLU 276  
9   1 Y 1 A ILE 290  ? A ILE 277  
10  1 Y 1 A GLN 291  ? A GLN 278  
11  1 Y 1 A CYS 292  ? A CYS 279  
12  1 Y 1 A LYS 293  ? A LYS 280  
13  1 Y 1 A THR 294  ? A THR 281  
14  1 Y 1 A LYS 295  ? A LYS 282  
15  1 Y 1 A SER 296  ? A SER 283  
16  1 Y 1 A LEU 297  ? A LEU 284  
17  1 Y 1 A LEU 298  ? A LEU 285  
18  1 Y 1 A PRO 299  ? A PRO 286  
19  1 Y 1 A ASN 300  ? A ASN 287  
20  1 Y 1 A THR 301  ? A THR 288  
21  1 Y 1 A GLY 302  ? A GLY 289  
22  1 Y 1 A VAL 303  ? A VAL 290  
23  1 Y 1 A TYR 304  ? A TYR 291  
24  1 Y 1 A ASP 305  ? A ASP 292  
25  1 Y 1 A LEU 306  ? A LEU 293  
26  1 Y 1 A SER 307  ? A SER 294  
27  1 Y 1 A GLY 308  ? A GLY 295  
28  1 Y 1 A PHE 309  ? A PHE 296  
29  1 Y 1 A THR 310  ? A THR 297  
30  1 Y 1 A VAL 311  ? A VAL 298  
31  1 Y 1 A LYS 312  ? A LYS 299  
32  1 Y 1 A PRO 313  ? A PRO 300  
33  1 Y 1 A VAL 314  ? A VAL 301  
34  1 Y 1 A ALA 315  ? A ALA 302  
35  1 Y 1 A THR 316  ? A THR 303  
36  1 Y 1 A VAL 317  ? A VAL 304  
37  1 Y 1 A HIS 318  ? A HIS 305  
38  1 Y 1 A ARG 319  ? A ARG 306  
39  1 Y 1 A ARG 320  ? A ARG 307  
40  1 Y 1 A ILE 321  ? A ILE 308  
41  1 Y 1 A PRO 322  ? A PRO 309  
42  1 Y 1 A ASP 323  ? A ASP 310  
43  1 Y 1 A LEU 324  ? A LEU 311  
44  1 Y 1 A PRO 325  ? A PRO 312  
45  1 Y 1 A ASP 326  ? A ASP 313  
46  1 Y 1 A CYS 327  ? A CYS 314  
47  1 Y 1 A ASP 328  ? A ASP 315  
48  1 Y 1 A ILE 329  ? A ILE 316  
49  1 Y 1 A ASP 330  ? A ASP 317  
50  1 Y 1 A LYS 331  ? A LYS 318  
51  1 Y 1 A TRP 332  ? A TRP 319  
52  1 Y 1 A LEU 333  ? A LEU 320  
53  1 Y 1 A ASN 334  ? A ASN 321  
54  1 Y 1 A ASN 335  ? A ASN 322  
55  1 Y 1 A PHE 336  ? A PHE 323  
56  1 Y 1 A ASN 337  ? A ASN 324  
57  1 Y 1 A VAL 338  ? A VAL 325  
58  1 Y 1 A PRO 339  ? A PRO 326  
59  1 Y 1 A SER 340  ? A SER 327  
60  1 Y 1 A PRO 341  ? A PRO 328  
61  1 Y 1 A LEU 342  ? A LEU 329  
62  1 Y 1 A ASN 343  ? A ASN 330  
63  1 Y 1 A TRP 344  ? A TRP 331  
64  1 Y 1 A GLU 345  ? A GLU 332  
65  1 Y 1 A ARG 346  ? A ARG 333  
66  1 Y 1 A LYS 347  ? A LYS 334  
67  1 Y 1 A ILE 348  ? A ILE 335  
68  1 Y 1 A PHE 349  ? A PHE 336  
69  1 Y 1 A SER 350  ? A SER 337  
70  1 Y 1 A ASN 351  ? A ASN 338  
71  1 Y 1 A CYS 352  ? A CYS 339  
72  1 Y 1 A ASN 353  ? A ASN 340  
73  1 Y 1 A PHE 354  ? A PHE 341  
74  1 Y 1 A ASN 355  ? A ASN 342  
75  1 Y 1 A LEU 356  ? A LEU 343  
76  1 Y 1 A SER 357  ? A SER 344  
77  1 Y 1 A THR 358  ? A THR 345  
78  1 Y 1 A LEU 359  ? A LEU 346  
79  1 Y 1 A LEU 360  ? A LEU 347  
80  1 Y 1 A ARG 361  ? A ARG 348  
81  1 Y 1 A LEU 362  ? A LEU 349  
82  1 Y 1 A VAL 363  ? A VAL 350  
83  1 Y 1 A HIS 364  ? A HIS 351  
84  1 Y 1 A THR 365  ? A THR 352  
85  1 Y 1 A ASP 366  ? A ASP 353  
86  1 Y 1 A SER 367  ? A SER 354  
87  1 Y 1 A PHE 368  ? A PHE 355  
88  1 Y 1 A SER 369  ? A SER 356  
89  1 Y 1 A CYS 370  ? A CYS 357  
90  1 Y 1 A ASN 371  ? A ASN 358  
91  1 Y 1 A ASN 372  ? A ASN 359  
92  1 Y 1 A PHE 373  ? A PHE 360  
93  1 Y 1 A ASP 374  ? A ASP 361  
94  1 Y 1 A GLU 375  ? A GLU 362  
95  1 Y 1 A SER 376  ? A SER 363  
96  1 Y 1 A LYS 377  ? A LYS 364  
97  1 Y 1 A ILE 378  ? A ILE 365  
98  1 Y 1 A TYR 379  ? A TYR 366  
99  1 Y 1 A GLY 380  ? A GLY 367  
100 1 Y 1 A SER 381  ? A SER 368  
101 1 Y 1 A CYS 382  ? A CYS 369  
102 1 Y 1 A PHE 383  ? A PHE 370  
103 1 Y 1 A LYS 384  ? A LYS 371  
104 1 Y 1 A SER 385  ? A SER 372  
105 1 Y 1 A ILE 386  ? A ILE 373  
106 1 Y 1 A VAL 387  ? A VAL 374  
107 1 Y 1 A LEU 388  ? A LEU 375  
108 1 Y 1 A ASP 389  ? A ASP 376  
109 1 Y 1 A LYS 390  ? A LYS 377  
110 1 Y 1 A PHE 391  ? A PHE 378  
111 1 Y 1 A ALA 392  ? A ALA 379  
112 1 Y 1 A ILE 393  ? A ILE 380  
113 1 Y 1 A PRO 394  ? A PRO 381  
114 1 Y 1 A ASN 395  ? A ASN 382  
115 1 Y 1 A SER 396  ? A SER 383  
116 1 Y 1 A ARG 397  ? A ARG 384  
117 1 Y 1 A ARG 398  ? A ARG 385  
118 1 Y 1 A SER 399  ? A SER 386  
119 1 Y 1 A ASP 400  ? A ASP 387  
120 1 Y 1 A LEU 401  ? A LEU 388  
121 1 Y 1 A GLN 402  ? A GLN 389  
122 1 Y 1 A LEU 403  ? A LEU 390  
123 1 Y 1 A GLY 404  ? A GLY 391  
124 1 Y 1 A SER 405  ? A SER 392  
125 1 Y 1 A SER 406  ? A SER 393  
126 1 Y 1 A GLY 407  ? A GLY 394  
127 1 Y 1 A PHE 408  ? A PHE 395  
128 1 Y 1 A LEU 409  ? A LEU 396  
129 1 Y 1 A GLN 410  ? A GLN 397  
130 1 Y 1 A SER 411  ? A SER 398  
131 1 Y 1 A SER 412  ? A SER 399  
132 1 Y 1 A ASN 413  ? A ASN 400  
133 1 Y 1 A TYR 414  ? A TYR 401  
134 1 Y 1 A LYS 415  ? A LYS 402  
135 1 Y 1 A ILE 416  ? A ILE 403  
136 1 Y 1 A ASP 417  ? A ASP 404  
137 1 Y 1 A THR 418  ? A THR 405  
138 1 Y 1 A THR 419  ? A THR 406  
139 1 Y 1 A SER 420  ? A SER 407  
140 1 Y 1 A SER 421  ? A SER 408  
141 1 Y 1 A SER 422  ? A SER 409  
142 1 Y 1 A CYS 423  ? A CYS 410  
143 1 Y 1 A GLN 424  ? A GLN 411  
144 1 Y 1 A LEU 425  ? A LEU 412  
145 1 Y 1 A TYR 426  ? A TYR 413  
146 1 Y 1 A TYR 427  ? A TYR 414  
147 1 Y 1 A SER 428  ? A SER 415  
148 1 Y 1 A LEU 429  ? A LEU 416  
149 1 Y 1 A PRO 430  ? A PRO 417  
150 1 Y 1 A ALA 431  ? A ALA 418  
151 1 Y 1 A ILE 432  ? A ILE 419  
152 1 Y 1 A ASN 433  ? A ASN 420  
153 1 Y 1 A VAL 434  ? A VAL 421  
154 1 Y 1 A THR 435  ? A THR 422  
155 1 Y 1 A ILE 436  ? A ILE 423  
156 1 Y 1 A ASN 437  ? A ASN 424  
157 1 Y 1 A ASN 438  ? A ASN 425  
158 1 Y 1 A TYR 439  ? A TYR 426  
159 1 Y 1 A ASN 440  ? A ASN 427  
160 1 Y 1 A PRO 441  ? A PRO 428  
161 1 Y 1 A SER 442  ? A SER 429  
162 1 Y 1 A SER 443  ? A SER 430  
163 1 Y 1 A TRP 444  ? A TRP 431  
164 1 Y 1 A ASN 445  ? A ASN 432  
165 1 Y 1 A ARG 446  ? A ARG 433  
166 1 Y 1 A ARG 447  ? A ARG 434  
167 1 Y 1 A TYR 448  ? A TYR 435  
168 1 Y 1 A GLY 449  ? A GLY 436  
169 1 Y 1 A PHE 450  ? A PHE 437  
170 1 Y 1 A ASN 451  ? A ASN 438  
171 1 Y 1 A ASN 452  ? A ASN 439  
172 1 Y 1 A PHE 453  ? A PHE 440  
173 1 Y 1 A ASN 454  ? A ASN 441  
174 1 Y 1 A LEU 455  ? A LEU 442  
175 1 Y 1 A SER 456  ? A SER 443  
176 1 Y 1 A SER 457  ? A SER 444  
177 1 Y 1 A HIS 458  ? A HIS 445  
178 1 Y 1 A SER 459  ? A SER 446  
179 1 Y 1 A VAL 460  ? A VAL 447  
180 1 Y 1 A VAL 461  ? A VAL 448  
181 1 Y 1 A TYR 462  ? A TYR 449  
182 1 Y 1 A SER 463  ? A SER 450  
183 1 Y 1 A ARG 464  ? A ARG 451  
184 1 Y 1 A TYR 465  ? A TYR 452  
185 1 Y 1 A CYS 466  ? A CYS 453  
186 1 Y 1 A PHE 467  ? A PHE 454  
187 1 Y 1 A SER 468  ? A SER 455  
188 1 Y 1 A VAL 469  ? A VAL 456  
189 1 Y 1 A ASN 470  ? A ASN 457  
190 1 Y 1 A ASN 471  ? A ASN 458  
191 1 Y 1 A THR 472  ? A THR 459  
192 1 Y 1 A PHE 473  ? A PHE 460  
193 1 Y 1 A CYS 474  ? A CYS 461  
194 1 Y 1 A PRO 475  ? A PRO 462  
195 1 Y 1 A CYS 476  ? A CYS 463  
196 1 Y 1 A ALA 477  ? A ALA 464  
197 1 Y 1 A LYS 478  ? A LYS 465  
198 1 Y 1 A PRO 479  ? A PRO 466  
199 1 Y 1 A SER 480  ? A SER 467  
200 1 Y 1 A PHE 481  ? A PHE 468  
201 1 Y 1 A ALA 482  ? A ALA 469  
202 1 Y 1 A SER 483  ? A SER 470  
203 1 Y 1 A SER 484  ? A SER 471  
204 1 Y 1 A CYS 485  ? A CYS 472  
205 1 Y 1 A LYS 486  ? A LYS 473  
206 1 Y 1 A SER 487  ? A SER 474  
207 1 Y 1 A HIS 488  ? A HIS 475  
208 1 Y 1 A LYS 489  ? A LYS 476  
209 1 Y 1 A PRO 490  ? A PRO 477  
210 1 Y 1 A PRO 491  ? A PRO 478  
211 1 Y 1 A SER 492  ? A SER 479  
212 1 Y 1 A ALA 493  ? A ALA 480  
213 1 Y 1 A SER 494  ? A SER 481  
214 1 Y 1 A CYS 495  ? A CYS 482  
215 1 Y 1 A PRO 496  ? A PRO 483  
216 1 Y 1 A ILE 497  ? A ILE 484  
217 1 Y 1 A GLY 498  ? A GLY 485  
218 1 Y 1 A THR 499  ? A THR 486  
219 1 Y 1 A ASN 500  ? A ASN 487  
220 1 Y 1 A TYR 501  ? A TYR 488  
221 1 Y 1 A ARG 502  ? A ARG 489  
222 1 Y 1 A SER 503  ? A SER 490  
223 1 Y 1 A CYS 504  ? A CYS 491  
224 1 Y 1 A GLU 505  ? A GLU 492  
225 1 Y 1 A SER 506  ? A SER 493  
226 1 Y 1 A THR 507  ? A THR 494  
227 1 Y 1 A THR 508  ? A THR 495  
228 1 Y 1 A VAL 509  ? A VAL 496  
229 1 Y 1 A LEU 510  ? A LEU 497  
230 1 Y 1 A ASP 511  ? A ASP 498  
231 1 Y 1 A HIS 512  ? A HIS 499  
232 1 Y 1 A THR 513  ? A THR 500  
233 1 Y 1 A ASP 514  ? A ASP 501  
234 1 Y 1 A TRP 515  ? A TRP 502  
235 1 Y 1 A CYS 516  ? A CYS 503  
236 1 Y 1 A ARG 517  ? A ARG 504  
237 1 Y 1 A CYS 518  ? A CYS 505  
238 1 Y 1 A SER 519  ? A SER 506  
239 1 Y 1 A CYS 520  ? A CYS 507  
240 1 Y 1 A LEU 521  ? A LEU 508  
241 1 Y 1 A PRO 522  ? A PRO 509  
242 1 Y 1 A ASP 523  ? A ASP 510  
243 1 Y 1 A PRO 524  ? A PRO 511  
244 1 Y 1 A ILE 525  ? A ILE 512  
245 1 Y 1 A THR 526  ? A THR 513  
246 1 Y 1 A ALA 527  ? A ALA 514  
247 1 Y 1 A TYR 528  ? A TYR 515  
248 1 Y 1 A ASP 529  ? A ASP 516  
249 1 Y 1 A PRO 530  ? A PRO 517  
250 1 Y 1 A ARG 531  ? A ARG 518  
251 1 Y 1 A SER 532  ? A SER 519  
252 1 Y 1 A CYS 533  ? A CYS 520  
253 1 Y 1 A SER 534  ? A SER 521  
254 1 Y 1 A GLN 535  ? A GLN 522  
255 1 Y 1 A LYS 536  ? A LYS 523  
256 1 Y 1 A LYS 537  ? A LYS 524  
257 1 Y 1 A SER 538  ? A SER 525  
258 1 Y 1 A LEU 539  ? A LEU 526  
259 1 Y 1 A VAL 540  ? A VAL 527  
260 1 Y 1 A GLY 541  ? A GLY 528  
261 1 Y 1 A VAL 542  ? A VAL 529  
262 1 Y 1 A GLY 543  ? A GLY 530  
263 1 Y 1 A GLU 544  ? A GLU 531  
264 1 Y 1 A HIS 545  ? A HIS 532  
265 1 Y 1 A CYS 546  ? A CYS 533  
266 1 Y 1 A ALA 547  ? A ALA 534  
267 1 Y 1 A GLY 548  ? A GLY 535  
268 1 Y 1 A PHE 549  ? A PHE 536  
269 1 Y 1 A GLY 550  ? A GLY 537  
270 1 Y 1 A VAL 551  ? A VAL 538  
271 1 Y 1 A ASP 552  ? A ASP 539  
272 1 Y 1 A GLU 553  ? A GLU 540  
273 1 Y 1 A GLU 554  ? A GLU 541  
274 1 Y 1 A LYS 555  ? A LYS 542  
275 1 Y 1 A CYS 556  ? A CYS 543  
276 1 Y 1 A GLY 557  ? A GLY 544  
277 1 Y 1 A VAL 558  ? A VAL 545  
278 1 Y 1 A LEU 559  ? A LEU 546  
279 1 Y 1 A ASP 560  ? A ASP 547  
280 1 Y 1 A GLY 561  ? A GLY 548  
281 1 Y 1 A SER 562  ? A SER 549  
282 1 Y 1 A TYR 563  ? A TYR 550  
283 1 Y 1 A ASN 564  ? A ASN 551  
284 1 Y 1 A VAL 565  ? A VAL 552  
285 1 Y 1 A SER 566  ? A SER 553  
286 1 Y 1 A CYS 567  ? A CYS 554  
287 1 Y 1 A LEU 568  ? A LEU 555  
288 1 Y 1 A CYS 569  ? A CYS 556  
289 1 Y 1 A SER 570  ? A SER 557  
290 1 Y 1 A THR 571  ? A THR 558  
291 1 Y 1 A ASP 572  ? A ASP 559  
292 1 Y 1 A ALA 573  ? A ALA 560  
293 1 Y 1 A PHE 574  ? A PHE 561  
294 1 Y 1 A LEU 575  ? A LEU 562  
295 1 Y 1 A GLY 576  ? A GLY 563  
296 1 Y 1 A TRP 577  ? A TRP 564  
297 1 Y 1 A SER 578  ? A SER 565  
298 1 Y 1 A TYR 579  ? A TYR 566  
299 1 Y 1 A ASP 580  ? A ASP 567  
300 1 Y 1 A THR 581  ? A THR 568  
301 1 Y 1 A CYS 582  ? A CYS 569  
302 1 Y 1 A VAL 583  ? A VAL 570  
303 1 Y 1 A SER 584  ? A SER 571  
304 1 Y 1 A ASN 585  ? A ASN 572  
305 1 Y 1 A ASN 586  ? A ASN 573  
306 1 Y 1 A ARG 587  ? A ARG 574  
307 1 Y 1 A CYS 588  ? A CYS 575  
308 1 Y 1 A ASN 589  ? A ASN 576  
309 1 Y 1 A ILE 590  ? A ILE 577  
310 1 Y 1 A PHE 591  ? A PHE 578  
311 1 Y 1 A SER 592  ? A SER 579  
312 1 Y 1 A ASN 593  ? A ASN 580  
313 1 Y 1 A PHE 594  ? A PHE 581  
314 1 Y 1 A ILE 595  ? A ILE 582  
315 1 Y 1 A LEU 596  ? A LEU 583  
316 1 Y 1 A ASN 597  ? A ASN 584  
317 1 Y 1 A GLY 598  ? A GLY 585  
318 1 Y 1 A ILE 599  ? A ILE 586  
319 1 Y 1 A ASN 600  ? A ASN 587  
320 1 Y 1 A SER 601  ? A SER 588  
321 1 Y 1 A GLY 602  ? A GLY 589  
322 1 Y 1 A THR 603  ? A THR 590  
323 1 Y 1 A THR 604  ? A THR 591  
324 1 Y 1 A CYS 605  ? A CYS 592  
325 1 Y 1 A SER 606  ? A SER 593  
326 1 Y 1 A ASN 607  ? A ASN 594  
327 1 Y 1 A ASP 608  ? A ASP 595  
328 1 Y 1 A LEU 609  ? A LEU 596  
329 1 Y 1 A LEU 610  ? A LEU 597  
330 1 Y 1 A GLN 611  ? A GLN 598  
331 1 Y 1 A PRO 612  ? A PRO 599  
332 1 Y 1 A ASN 613  ? A ASN 600  
333 1 Y 1 A THR 614  ? A THR 601  
334 1 Y 1 A GLU 615  ? A GLU 602  
335 1 Y 1 A VAL 616  ? A VAL 603  
336 1 Y 1 A PHE 617  ? A PHE 604  
337 1 Y 1 A THR 618  ? A THR 605  
338 1 Y 1 A ASP 619  ? A ASP 606  
339 1 Y 1 A VAL 620  ? A VAL 607  
340 1 Y 1 A CYS 621  ? A CYS 608  
341 1 Y 1 A VAL 622  ? A VAL 609  
342 1 Y 1 A ASP 623  ? A ASP 610  
343 1 Y 1 A TYR 624  ? A TYR 611  
344 1 Y 1 A ASP 625  ? A ASP 612  
345 1 Y 1 A LEU 626  ? A LEU 613  
346 1 Y 1 A TYR 627  ? A TYR 614  
347 1 Y 1 A GLY 628  ? A GLY 615  
348 1 Y 1 A ILE 629  ? A ILE 616  
349 1 Y 1 A THR 630  ? A THR 617  
350 1 Y 1 A GLY 631  ? A GLY 618  
351 1 Y 1 A GLN 632  ? A GLN 619  
352 1 Y 1 A GLY 633  ? A GLY 620  
353 1 Y 1 A ILE 634  ? A ILE 621  
354 1 Y 1 A PHE 635  ? A PHE 622  
355 1 Y 1 A LYS 636  ? A LYS 623  
356 1 Y 1 A GLU 637  ? A GLU 624  
357 1 Y 1 A VAL 638  ? A VAL 625  
358 1 Y 1 A SER 639  ? A SER 626  
359 1 Y 1 A ALA 640  ? A ALA 627  
360 1 Y 1 A VAL 641  ? A VAL 628  
361 1 Y 1 A TYR 642  ? A TYR 629  
362 1 Y 1 A TYR 643  ? A TYR 630  
363 1 Y 1 A ASN 644  ? A ASN 631  
364 1 Y 1 A SER 645  ? A SER 632  
365 1 Y 1 A TRP 646  ? A TRP 633  
366 1 Y 1 A GLN 647  ? A GLN 634  
367 1 Y 1 A ASN 648  ? A ASN 635  
368 1 Y 1 A LEU 649  ? A LEU 636  
369 1 Y 1 A LEU 650  ? A LEU 637  
370 1 Y 1 A TYR 651  ? A TYR 638  
371 1 Y 1 A ASP 652  ? A ASP 639  
372 1 Y 1 A SER 653  ? A SER 640  
373 1 Y 1 A ASN 654  ? A ASN 641  
374 1 Y 1 A GLY 655  ? A GLY 642  
375 1 Y 1 A ASN 656  ? A ASN 643  
376 1 Y 1 A ILE 657  ? A ILE 644  
377 1 Y 1 A ILE 658  ? A ILE 645  
378 1 Y 1 A GLY 659  ? A GLY 646  
379 1 Y 1 A PHE 660  ? A PHE 647  
380 1 Y 1 A LYS 661  ? A LYS 648  
381 1 Y 1 A ASP 662  ? A ASP 649  
382 1 Y 1 A PHE 663  ? A PHE 650  
383 1 Y 1 A VAL 664  ? A VAL 651  
384 1 Y 1 A THR 665  ? A THR 652  
385 1 Y 1 A ASN 666  ? A ASN 653  
386 1 Y 1 A LYS 667  ? A LYS 654  
387 1 Y 1 A THR 668  ? A THR 655  
388 1 Y 1 A TYR 669  ? A TYR 656  
389 1 Y 1 A ASN 670  ? A ASN 657  
390 1 Y 1 A ILE 671  ? A ILE 658  
391 1 Y 1 A PHE 672  ? A PHE 659  
392 1 Y 1 A PRO 673  ? A PRO 660  
393 1 Y 1 A CYS 674  ? A CYS 661  
394 1 Y 1 A TYR 675  ? A TYR 662  
395 1 Y 1 A ALA 676  ? A ALA 663  
396 1 Y 1 A GLY 677  ? A GLY 664  
397 1 Y 1 A ARG 678  ? A ARG 665  
398 1 Y 1 A VAL 679  ? A VAL 666  
399 1 Y 1 A SER 680  ? A SER 667  
400 1 Y 1 A ALA 681  ? A ALA 668  
401 1 Y 1 A ALA 682  ? A ALA 669  
402 1 Y 1 A PHE 683  ? A PHE 670  
403 1 Y 1 A HIS 684  ? A HIS 671  
404 1 Y 1 A GLN 685  ? A GLN 672  
405 1 Y 1 A ASN 686  ? A ASN 673  
406 1 Y 1 A ALA 687  ? A ALA 674  
407 1 Y 1 A SER 688  ? A SER 675  
408 1 Y 1 A SER 689  ? A SER 676  
409 1 Y 1 A LEU 690  ? A LEU 677  
410 1 Y 1 A ALA 691  ? A ALA 678  
411 1 Y 1 A LEU 692  ? A LEU 679  
412 1 Y 1 A LEU 693  ? A LEU 680  
413 1 Y 1 A TYR 694  ? A TYR 681  
414 1 Y 1 A ARG 695  ? A ARG 682  
415 1 Y 1 A ASN 696  ? A ASN 683  
416 1 Y 1 A LEU 697  ? A LEU 684  
417 1 Y 1 A LYS 698  ? A LYS 685  
418 1 Y 1 A CYS 699  ? A CYS 686  
419 1 Y 1 A SER 700  ? A SER 687  
420 1 Y 1 A TYR 701  ? A TYR 688  
421 1 Y 1 A VAL 702  ? A VAL 689  
422 1 Y 1 A LEU 703  ? A LEU 690  
423 1 Y 1 A ASN 704  ? A ASN 691  
424 1 Y 1 A ASN 705  ? A ASN 692  
425 1 Y 1 A ILE 706  ? A ILE 693  
426 1 Y 1 A SER 707  ? A SER 694  
427 1 Y 1 A LEU 708  ? A LEU 695  
428 1 Y 1 A THR 709  ? A THR 696  
429 1 Y 1 A THR 710  ? A THR 697  
430 1 Y 1 A GLN 711  ? A GLN 698  
431 1 Y 1 A PRO 712  ? A PRO 699  
432 1 Y 1 A TYR 713  ? A TYR 700  
433 1 Y 1 A PHE 714  ? A PHE 701  
434 1 Y 1 A ASP 715  ? A ASP 702  
435 1 Y 1 A SER 716  ? A SER 703  
436 1 Y 1 A TYR 717  ? A TYR 704  
437 1 Y 1 A LEU 718  ? A LEU 705  
438 1 Y 1 A GLY 719  ? A GLY 706  
439 1 Y 1 A CYS 720  ? A CYS 707  
440 1 Y 1 A VAL 721  ? A VAL 708  
441 1 Y 1 A PHE 722  ? A PHE 709  
442 1 Y 1 A ASN 723  ? A ASN 710  
443 1 Y 1 A ALA 724  ? A ALA 711  
444 1 Y 1 A ASP 725  ? A ASP 712  
445 1 Y 1 A ASN 726  ? A ASN 713  
446 1 Y 1 A LEU 727  ? A LEU 714  
447 1 Y 1 A THR 728  ? A THR 715  
448 1 Y 1 A ASP 729  ? A ASP 716  
449 1 Y 1 A TYR 730  ? A TYR 717  
450 1 Y 1 A SER 731  ? A SER 718  
451 1 Y 1 A VAL 732  ? A VAL 719  
452 1 Y 1 A SER 733  ? A SER 720  
453 1 Y 1 A SER 734  ? A SER 721  
454 1 Y 1 A CYS 735  ? A CYS 722  
455 1 Y 1 A ALA 736  ? A ALA 723  
456 1 Y 1 A LEU 737  ? A LEU 724  
457 1 Y 1 A ARG 738  ? A ARG 725  
458 1 Y 1 A MET 739  ? A MET 726  
459 1 Y 1 A GLY 740  ? A GLY 727  
460 1 Y 1 A SER 741  ? A SER 728  
461 1 Y 1 A GLY 742  ? A GLY 729  
462 1 Y 1 A PHE 743  ? A PHE 730  
463 1 Y 1 A CYS 744  ? A CYS 731  
464 1 Y 1 A VAL 745  ? A VAL 732  
465 1 Y 1 A ASP 746  ? A ASP 733  
466 1 Y 1 A TYR 747  ? A TYR 734  
467 1 Y 1 A ASN 748  ? A ASN 735  
468 1 Y 1 A SER 749  ? A SER 736  
469 1 Y 1 A TYR 750  ? A TYR 737  
470 1 Y 1 A ARG 751  ? A ARG 738  
471 1 Y 1 A PHE 752  ? A PHE 739  
472 1 Y 1 A VAL 753  ? A VAL 740  
473 1 Y 1 A THR 754  ? A THR 741  
474 1 Y 1 A PHE 755  ? A PHE 742  
475 1 Y 1 A GLU 756  ? A GLU 743  
476 1 Y 1 A PRO 757  ? A PRO 744  
477 1 Y 1 A PHE 758  ? A PHE 745  
478 1 Y 1 A ASN 759  ? A ASN 746  
479 1 Y 1 A VAL 760  ? A VAL 747  
480 1 Y 1 A SER 761  ? A SER 748  
481 1 Y 1 A PHE 762  ? A PHE 749  
482 1 Y 1 A VAL 763  ? A VAL 750  
483 1 Y 1 A ASN 764  ? A ASN 751  
484 1 Y 1 A ASP 765  ? A ASP 752  
485 1 Y 1 A SER 766  ? A SER 753  
486 1 Y 1 A ILE 767  ? A ILE 754  
487 1 Y 1 A GLU 768  ? A GLU 755  
488 1 Y 1 A SER 769  ? A SER 756  
489 1 Y 1 A VAL 770  ? A VAL 757  
490 1 Y 1 A GLY 771  ? A GLY 758  
491 1 Y 1 A GLY 772  ? A GLY 759  
492 1 Y 1 A LEU 773  ? A LEU 760  
493 1 Y 1 A TYR 774  ? A TYR 761  
494 1 Y 1 A GLU 775  ? A GLU 762  
495 1 Y 1 A ILE 776  ? A ILE 763  
496 1 Y 1 A LYS 777  ? A LYS 764  
497 1 Y 1 A ILE 778  ? A ILE 765  
498 1 Y 1 A PRO 779  ? A PRO 766  
499 1 Y 1 A THR 780  ? A THR 767  
500 1 Y 1 A ASN 781  ? A ASN 768  
501 1 Y 1 A PHE 782  ? A PHE 769  
502 1 Y 1 A THR 783  ? A THR 770  
503 1 Y 1 A ILE 784  ? A ILE 771  
504 1 Y 1 A VAL 785  ? A VAL 772  
505 1 Y 1 A GLY 786  ? A GLY 773  
506 1 Y 1 A GLN 787  ? A GLN 774  
507 1 Y 1 A GLU 788  ? A GLU 775  
508 1 Y 1 A GLU 789  ? A GLU 776  
509 1 Y 1 A PHE 790  ? A PHE 777  
510 1 Y 1 A ILE 791  ? A ILE 778  
511 1 Y 1 A GLN 792  ? A GLN 779  
512 1 Y 1 A THR 793  ? A THR 780  
513 1 Y 1 A ASN 794  ? A ASN 781  
514 1 Y 1 A SER 795  ? A SER 782  
515 1 Y 1 A PRO 796  ? A PRO 783  
516 1 Y 1 A LYS 797  ? A LYS 784  
517 1 Y 1 A VAL 798  ? A VAL 785  
518 1 Y 1 A THR 799  ? A THR 786  
519 1 Y 1 A ILE 800  ? A ILE 787  
520 1 Y 1 A ASP 801  ? A ASP 788  
521 1 Y 1 A CYS 802  ? A CYS 789  
522 1 Y 1 A SER 803  ? A SER 790  
523 1 Y 1 A LEU 804  ? A LEU 791  
524 1 Y 1 A PHE 805  ? A PHE 792  
525 1 Y 1 A VAL 806  ? A VAL 793  
526 1 Y 1 A CYS 807  ? A CYS 794  
527 1 Y 1 A SER 808  ? A SER 795  
528 1 Y 1 A ASN 809  ? A ASN 796  
529 1 Y 1 A TYR 810  ? A TYR 797  
530 1 Y 1 A ALA 811  ? A ALA 798  
531 1 Y 1 A ALA 812  ? A ALA 799  
532 1 Y 1 A CYS 813  ? A CYS 800  
533 1 Y 1 A HIS 814  ? A HIS 801  
534 1 Y 1 A ASP 815  ? A ASP 802  
535 1 Y 1 A LEU 816  ? A LEU 803  
536 1 Y 1 A LEU 817  ? A LEU 804  
537 1 Y 1 A SER 818  ? A SER 805  
538 1 Y 1 A GLU 819  ? A GLU 806  
539 1 Y 1 A TYR 820  ? A TYR 807  
540 1 Y 1 A GLY 821  ? A GLY 808  
541 1 Y 1 A THR 822  ? A THR 809  
542 1 Y 1 A PHE 823  ? A PHE 810  
543 1 Y 1 A CYS 824  ? A CYS 811  
544 1 Y 1 A ASP 825  ? A ASP 812  
545 1 Y 1 A ASN 826  ? A ASN 813  
546 1 Y 1 A ILE 827  ? A ILE 814  
547 1 Y 1 A ASN 828  ? A ASN 815  
548 1 Y 1 A SER 829  ? A SER 816  
549 1 Y 1 A ILE 830  ? A ILE 817  
550 1 Y 1 A LEU 831  ? A LEU 818  
551 1 Y 1 A ASP 832  ? A ASP 819  
552 1 Y 1 A GLU 833  ? A GLU 820  
553 1 Y 1 A VAL 834  ? A VAL 821  
554 1 Y 1 A ASN 835  ? A ASN 822  
555 1 Y 1 A GLY 836  ? A GLY 823  
556 1 Y 1 A LEU 837  ? A LEU 824  
557 1 Y 1 A LEU 838  ? A LEU 825  
558 1 Y 1 A ASP 839  ? A ASP 826  
559 1 Y 1 A THR 840  ? A THR 827  
560 1 Y 1 A THR 841  ? A THR 828  
561 1 Y 1 A GLN 842  ? A GLN 829  
562 1 Y 1 A LEU 843  ? A LEU 830  
563 1 Y 1 A HIS 844  ? A HIS 831  
564 1 Y 1 A VAL 845  ? A VAL 832  
565 1 Y 1 A ALA 846  ? A ALA 833  
566 1 Y 1 A ASP 847  ? A ASP 834  
567 1 Y 1 A THR 848  ? A THR 835  
568 1 Y 1 A LEU 849  ? A LEU 836  
569 1 Y 1 A MET 850  ? A MET 837  
570 1 Y 1 A GLN 851  ? A GLN 838  
571 1 Y 1 A GLY 852  ? A GLY 839  
572 1 Y 1 A VAL 853  ? A VAL 840  
573 1 Y 1 A THR 854  ? A THR 841  
574 1 Y 1 A LEU 855  ? A LEU 842  
575 1 Y 1 A SER 856  ? A SER 843  
576 1 Y 1 A SER 857  ? A SER 844  
577 1 Y 1 A ASN 858  ? A ASN 845  
578 1 Y 1 A LEU 859  ? A LEU 846  
579 1 Y 1 A ASN 860  ? A ASN 847  
580 1 Y 1 A THR 861  ? A THR 848  
581 1 Y 1 A ASN 862  ? A ASN 849  
582 1 Y 1 A LEU 863  ? A LEU 850  
583 1 Y 1 A HIS 864  ? A HIS 851  
584 1 Y 1 A PHE 865  ? A PHE 852  
585 1 Y 1 A ASP 866  ? A ASP 853  
586 1 Y 1 A VAL 867  ? A VAL 854  
587 1 Y 1 A ASP 868  ? A ASP 855  
588 1 Y 1 A ASN 869  ? A ASN 856  
589 1 Y 1 A ILE 870  ? A ILE 857  
590 1 Y 1 A ASN 871  ? A ASN 858  
591 1 Y 1 A PHE 872  ? A PHE 859  
592 1 Y 1 A LYS 873  ? A LYS 860  
593 1 Y 1 A SER 874  ? A SER 861  
594 1 Y 1 A LEU 875  ? A LEU 862  
595 1 Y 1 A VAL 876  ? A VAL 863  
596 1 Y 1 A GLY 877  ? A GLY 864  
597 1 Y 1 A CYS 878  ? A CYS 865  
598 1 Y 1 A LEU 879  ? A LEU 866  
599 1 Y 1 A GLY 880  ? A GLY 867  
600 1 Y 1 A PRO 881  ? A PRO 868  
601 1 Y 1 A HIS 882  ? A HIS 869  
602 1 Y 1 A CYS 883  ? A CYS 870  
603 1 Y 1 A GLY 884  ? A GLY 871  
604 1 Y 1 A SER 885  ? A SER 872  
605 1 Y 1 A SER 886  ? A SER 873  
606 1 Y 1 A SER 887  ? A SER 874  
607 1 Y 1 A ARG 888  ? A ARG 875  
608 1 Y 1 A SER 889  ? A SER 876  
609 1 Y 1 A PHE 890  ? A PHE 877  
610 1 Y 1 A PHE 891  ? A PHE 878  
611 1 Y 1 A GLU 892  ? A GLU 879  
612 1 Y 1 A ASP 893  ? A ASP 880  
613 1 Y 1 A LEU 894  ? A LEU 881  
614 1 Y 1 A LEU 895  ? A LEU 882  
615 1 Y 1 A PHE 896  ? A PHE 883  
616 1 Y 1 A ASP 897  ? A ASP 884  
617 1 Y 1 A LYS 898  ? A LYS 885  
618 1 Y 1 A VAL 899  ? A VAL 886  
619 1 Y 1 A LYS 900  ? A LYS 887  
620 1 Y 1 A LEU 901  ? A LEU 888  
621 1 Y 1 A SER 902  ? A SER 889  
622 1 Y 1 A ASP 903  ? A ASP 890  
623 1 Y 1 A VAL 904  ? A VAL 891  
624 1 Y 1 A GLY 905  ? A GLY 892  
625 1 Y 1 A PHE 906  ? A PHE 893  
626 1 Y 1 A VAL 907  ? A VAL 894  
627 1 Y 1 A GLU 908  ? A GLU 895  
628 1 Y 1 A ALA 909  ? A ALA 896  
629 1 Y 1 A TYR 910  ? A TYR 897  
630 1 Y 1 A ASN 911  ? A ASN 898  
631 1 Y 1 A ASN 912  ? A ASN 899  
632 1 Y 1 A CYS 913  ? A CYS 900  
633 1 Y 1 A THR 914  ? A THR 901  
634 1 Y 1 A GLY 915  ? A GLY 902  
635 1 Y 1 A GLY 916  ? A GLY 903  
636 1 Y 1 A SER 917  ? A SER 904  
637 1 Y 1 A GLU 918  ? A GLU 905  
638 1 Y 1 A ILE 919  ? A ILE 906  
639 1 Y 1 A ARG 920  ? A ARG 907  
640 1 Y 1 A ASP 921  ? A ASP 908  
641 1 Y 1 A LEU 922  ? A LEU 909  
642 1 Y 1 A LEU 923  ? A LEU 910  
643 1 Y 1 A CYS 924  ? A CYS 911  
644 1 Y 1 A VAL 925  ? A VAL 912  
645 1 Y 1 A GLN 926  ? A GLN 913  
646 1 Y 1 A SER 927  ? A SER 914  
647 1 Y 1 A PHE 928  ? A PHE 915  
648 1 Y 1 A ASN 929  ? A ASN 916  
649 1 Y 1 A GLY 930  ? A GLY 917  
650 1 Y 1 A ILE 931  ? A ILE 918  
651 1 Y 1 A LYS 932  ? A LYS 919  
652 1 Y 1 A VAL 933  ? A VAL 920  
653 1 Y 1 A LEU 934  ? A LEU 921  
654 1 Y 1 A PRO 935  ? A PRO 922  
655 1 Y 1 A PRO 936  ? A PRO 923  
656 1 Y 1 A ILE 937  ? A ILE 924  
657 1 Y 1 A LEU 938  ? A LEU 925  
658 1 Y 1 A SER 939  ? A SER 926  
659 1 Y 1 A GLU 940  ? A GLU 927  
660 1 Y 1 A SER 941  ? A SER 928  
661 1 Y 1 A GLN 942  ? A GLN 929  
662 1 Y 1 A ILE 943  ? A ILE 930  
663 1 Y 1 A SER 944  ? A SER 931  
664 1 Y 1 A GLY 945  ? A GLY 932  
665 1 Y 1 A TYR 946  ? A TYR 933  
666 1 Y 1 A THR 947  ? A THR 934  
667 1 Y 1 A THR 948  ? A THR 935  
668 1 Y 1 A ALA 949  ? A ALA 936  
669 1 Y 1 A ALA 950  ? A ALA 937  
670 1 Y 1 A THR 951  ? A THR 938  
671 1 Y 1 A VAL 952  ? A VAL 939  
672 1 Y 1 A ALA 953  ? A ALA 940  
673 1 Y 1 A ALA 954  ? A ALA 941  
674 1 Y 1 A MET 955  ? A MET 942  
675 1 Y 1 A PHE 956  ? A PHE 943  
676 1 Y 1 A PRO 957  ? A PRO 944  
677 1 Y 1 A PRO 958  ? A PRO 945  
678 1 Y 1 A TRP 959  ? A TRP 946  
679 1 Y 1 A SER 960  ? A SER 947  
680 1 Y 1 A ALA 961  ? A ALA 948  
681 1 Y 1 A ALA 962  ? A ALA 949  
682 1 Y 1 A ALA 963  ? A ALA 950  
683 1 Y 1 A GLY 964  ? A GLY 951  
684 1 Y 1 A ILE 965  ? A ILE 952  
685 1 Y 1 A PRO 966  ? A PRO 953  
686 1 Y 1 A PHE 967  ? A PHE 954  
687 1 Y 1 A SER 968  ? A SER 955  
688 1 Y 1 A LEU 969  ? A LEU 956  
689 1 Y 1 A ASN 970  ? A ASN 957  
690 1 Y 1 A VAL 971  ? A VAL 958  
691 1 Y 1 A GLN 972  ? A GLN 959  
692 1 Y 1 A TYR 973  ? A TYR 960  
693 1 Y 1 A ARG 974  ? A ARG 961  
694 1 Y 1 A ILE 975  ? A ILE 962  
695 1 Y 1 A ASN 976  ? A ASN 963  
696 1 Y 1 A GLY 977  ? A GLY 964  
697 1 Y 1 A LEU 978  ? A LEU 965  
698 1 Y 1 A GLY 979  ? A GLY 966  
699 1 Y 1 A VAL 980  ? A VAL 967  
700 1 Y 1 A THR 981  ? A THR 968  
701 1 Y 1 A MET 982  ? A MET 969  
702 1 Y 1 A ASP 983  ? A ASP 970  
703 1 Y 1 A VAL 984  ? A VAL 971  
704 1 Y 1 A LEU 985  ? A LEU 972  
705 1 Y 1 A ASN 986  ? A ASN 973  
706 1 Y 1 A LYS 987  ? A LYS 974  
707 1 Y 1 A ASN 988  ? A ASN 975  
708 1 Y 1 A GLN 989  ? A GLN 976  
709 1 Y 1 A LYS 990  ? A LYS 977  
710 1 Y 1 A LEU 991  ? A LEU 978  
711 1 Y 1 A ILE 992  ? A ILE 979  
712 1 Y 1 A ALA 993  ? A ALA 980  
713 1 Y 1 A THR 994  ? A THR 981  
714 1 Y 1 A ALA 995  ? A ALA 982  
715 1 Y 1 A PHE 996  ? A PHE 983  
716 1 Y 1 A ASN 997  ? A ASN 984  
717 1 Y 1 A ASN 998  ? A ASN 985  
718 1 Y 1 A ALA 999  ? A ALA 986  
719 1 Y 1 A LEU 1000 ? A LEU 987  
720 1 Y 1 A LEU 1001 ? A LEU 988  
721 1 Y 1 A SER 1002 ? A SER 989  
722 1 Y 1 A ILE 1003 ? A ILE 990  
723 1 Y 1 A GLN 1004 ? A GLN 991  
724 1 Y 1 A ASN 1005 ? A ASN 992  
725 1 Y 1 A GLY 1006 ? A GLY 993  
726 1 Y 1 A PHE 1007 ? A PHE 994  
727 1 Y 1 A SER 1008 ? A SER 995  
728 1 Y 1 A ALA 1009 ? A ALA 996  
729 1 Y 1 A PRO 1010 ? A PRO 997  
730 1 Y 1 A ASN 1011 ? A ASN 998  
731 1 Y 1 A SER 1012 ? A SER 999  
732 1 Y 1 A ALA 1013 ? A ALA 1000 
733 1 Y 1 A LEU 1014 ? A LEU 1001 
734 1 Y 1 A ALA 1015 ? A ALA 1002 
735 1 Y 1 A LYS 1016 ? A LYS 1003 
736 1 Y 1 A ILE 1017 ? A ILE 1004 
737 1 Y 1 A GLN 1018 ? A GLN 1005 
738 1 Y 1 A SER 1019 ? A SER 1006 
739 1 Y 1 A VAL 1020 ? A VAL 1007 
740 1 Y 1 A VAL 1021 ? A VAL 1008 
741 1 Y 1 A ASN 1022 ? A ASN 1009 
742 1 Y 1 A SER 1023 ? A SER 1010 
743 1 Y 1 A ASN 1024 ? A ASN 1011 
744 1 Y 1 A ALA 1025 ? A ALA 1012 
745 1 Y 1 A GLN 1026 ? A GLN 1013 
746 1 Y 1 A ALA 1027 ? A ALA 1014 
747 1 Y 1 A LEU 1028 ? A LEU 1015 
748 1 Y 1 A ASN 1029 ? A ASN 1016 
749 1 Y 1 A SER 1030 ? A SER 1017 
750 1 Y 1 A LEU 1031 ? A LEU 1018 
751 1 Y 1 A LEU 1032 ? A LEU 1019 
752 1 Y 1 A GLN 1033 ? A GLN 1020 
753 1 Y 1 A GLN 1034 ? A GLN 1021 
754 1 Y 1 A LEU 1035 ? A LEU 1022 
755 1 Y 1 A PHE 1036 ? A PHE 1023 
756 1 Y 1 A ASN 1037 ? A ASN 1024 
757 1 Y 1 A LYS 1038 ? A LYS 1025 
758 1 Y 1 A PHE 1039 ? A PHE 1026 
759 1 Y 1 A GLY 1040 ? A GLY 1027 
760 1 Y 1 A ALA 1041 ? A ALA 1028 
761 1 Y 1 A ILE 1042 ? A ILE 1029 
762 1 Y 1 A SER 1043 ? A SER 1030 
763 1 Y 1 A SER 1044 ? A SER 1031 
764 1 Y 1 A SER 1045 ? A SER 1032 
765 1 Y 1 A LEU 1046 ? A LEU 1033 
766 1 Y 1 A GLN 1047 ? A GLN 1034 
767 1 Y 1 A GLU 1048 ? A GLU 1035 
768 1 Y 1 A ILE 1049 ? A ILE 1036 
769 1 Y 1 A LEU 1050 ? A LEU 1037 
770 1 Y 1 A SER 1051 ? A SER 1038 
771 1 Y 1 A ARG 1052 ? A ARG 1039 
772 1 Y 1 A LEU 1053 ? A LEU 1040 
773 1 Y 1 A ASP 1054 ? A ASP 1041 
774 1 Y 1 A PRO 1055 ? A PRO 1042 
775 1 Y 1 A PRO 1056 ? A PRO 1043 
776 1 Y 1 A GLU 1057 ? A GLU 1044 
777 1 Y 1 A ALA 1058 ? A ALA 1045 
778 1 Y 1 A GLN 1059 ? A GLN 1046 
779 1 Y 1 A VAL 1060 ? A VAL 1047 
780 1 Y 1 A GLN 1061 ? A GLN 1048 
781 1 Y 1 A ILE 1062 ? A ILE 1049 
782 1 Y 1 A ASP 1063 ? A ASP 1050 
783 1 Y 1 A ARG 1064 ? A ARG 1051 
784 1 Y 1 A LEU 1065 ? A LEU 1052 
785 1 Y 1 A ILE 1066 ? A ILE 1053 
786 1 Y 1 A ASN 1067 ? A ASN 1054 
787 1 Y 1 A GLY 1068 ? A GLY 1055 
788 1 Y 1 A ARG 1069 ? A ARG 1056 
789 1 Y 1 A LEU 1070 ? A LEU 1057 
790 1 Y 1 A THR 1071 ? A THR 1058 
791 1 Y 1 A ALA 1072 ? A ALA 1059 
792 1 Y 1 A LEU 1073 ? A LEU 1060 
793 1 Y 1 A ASN 1074 ? A ASN 1061 
794 1 Y 1 A ALA 1075 ? A ALA 1062 
795 1 Y 1 A TYR 1076 ? A TYR 1063 
796 1 Y 1 A VAL 1077 ? A VAL 1064 
797 1 Y 1 A SER 1078 ? A SER 1065 
798 1 Y 1 A GLN 1079 ? A GLN 1066 
799 1 Y 1 A GLN 1080 ? A GLN 1067 
800 1 Y 1 A LEU 1081 ? A LEU 1068 
801 1 Y 1 A SER 1082 ? A SER 1069 
802 1 Y 1 A ASP 1083 ? A ASP 1070 
803 1 Y 1 A ILE 1084 ? A ILE 1071 
804 1 Y 1 A SER 1085 ? A SER 1072 
805 1 Y 1 A LEU 1086 ? A LEU 1073 
806 1 Y 1 A VAL 1087 ? A VAL 1074 
807 1 Y 1 A LYS 1088 ? A LYS 1075 
808 1 Y 1 A PHE 1089 ? A PHE 1076 
809 1 Y 1 A GLY 1090 ? A GLY 1077 
810 1 Y 1 A ALA 1091 ? A ALA 1078 
811 1 Y 1 A ALA 1092 ? A ALA 1079 
812 1 Y 1 A LEU 1093 ? A LEU 1080 
813 1 Y 1 A ALA 1094 ? A ALA 1081 
814 1 Y 1 A MET 1095 ? A MET 1082 
815 1 Y 1 A GLU 1096 ? A GLU 1083 
816 1 Y 1 A LYS 1097 ? A LYS 1084 
817 1 Y 1 A VAL 1098 ? A VAL 1085 
818 1 Y 1 A ASN 1099 ? A ASN 1086 
819 1 Y 1 A GLU 1100 ? A GLU 1087 
820 1 Y 1 A CYS 1101 ? A CYS 1088 
821 1 Y 1 A VAL 1102 ? A VAL 1089 
822 1 Y 1 A LYS 1103 ? A LYS 1090 
823 1 Y 1 A SER 1104 ? A SER 1091 
824 1 Y 1 A GLN 1105 ? A GLN 1092 
825 1 Y 1 A SER 1106 ? A SER 1093 
826 1 Y 1 A PRO 1107 ? A PRO 1094 
827 1 Y 1 A ARG 1108 ? A ARG 1095 
828 1 Y 1 A ILE 1109 ? A ILE 1096 
829 1 Y 1 A ASN 1110 ? A ASN 1097 
830 1 Y 1 A PHE 1111 ? A PHE 1098 
831 1 Y 1 A CYS 1112 ? A CYS 1099 
832 1 Y 1 A GLY 1113 ? A GLY 1100 
833 1 Y 1 A ASN 1114 ? A ASN 1101 
834 1 Y 1 A GLY 1115 ? A GLY 1102 
835 1 Y 1 A ASN 1116 ? A ASN 1103 
836 1 Y 1 A HIS 1117 ? A HIS 1104 
837 1 Y 1 A ILE 1118 ? A ILE 1105 
838 1 Y 1 A LEU 1119 ? A LEU 1106 
839 1 Y 1 A SER 1120 ? A SER 1107 
840 1 Y 1 A LEU 1121 ? A LEU 1108 
841 1 Y 1 A VAL 1122 ? A VAL 1109 
842 1 Y 1 A GLN 1123 ? A GLN 1110 
843 1 Y 1 A ASN 1124 ? A ASN 1111 
844 1 Y 1 A ALA 1125 ? A ALA 1112 
845 1 Y 1 A PRO 1126 ? A PRO 1113 
846 1 Y 1 A TYR 1127 ? A TYR 1114 
847 1 Y 1 A GLY 1128 ? A GLY 1115 
848 1 Y 1 A LEU 1129 ? A LEU 1116 
849 1 Y 1 A LEU 1130 ? A LEU 1117 
850 1 Y 1 A PHE 1131 ? A PHE 1118 
851 1 Y 1 A MET 1132 ? A MET 1119 
852 1 Y 1 A HIS 1133 ? A HIS 1120 
853 1 Y 1 A PHE 1134 ? A PHE 1121 
854 1 Y 1 A SER 1135 ? A SER 1122 
855 1 Y 1 A TYR 1136 ? A TYR 1123 
856 1 Y 1 A LYS 1137 ? A LYS 1124 
857 1 Y 1 A PRO 1138 ? A PRO 1125 
858 1 Y 1 A ILE 1139 ? A ILE 1126 
859 1 Y 1 A SER 1140 ? A SER 1127 
860 1 Y 1 A PHE 1141 ? A PHE 1128 
861 1 Y 1 A LYS 1142 ? A LYS 1129 
862 1 Y 1 A THR 1143 ? A THR 1130 
863 1 Y 1 A VAL 1144 ? A VAL 1131 
864 1 Y 1 A LEU 1145 ? A LEU 1132 
865 1 Y 1 A VAL 1146 ? A VAL 1133 
866 1 Y 1 A SER 1147 ? A SER 1134 
867 1 Y 1 A PRO 1148 ? A PRO 1135 
868 1 Y 1 A GLY 1149 ? A GLY 1136 
869 1 Y 1 A LEU 1150 ? A LEU 1137 
870 1 Y 1 A CYS 1151 ? A CYS 1138 
871 1 Y 1 A ILE 1152 ? A ILE 1139 
872 1 Y 1 A SER 1153 ? A SER 1140 
873 1 Y 1 A GLY 1154 ? A GLY 1141 
874 1 Y 1 A ASP 1155 ? A ASP 1142 
875 1 Y 1 A VAL 1156 ? A VAL 1143 
876 1 Y 1 A GLY 1157 ? A GLY 1144 
877 1 Y 1 A ILE 1158 ? A ILE 1145 
878 1 Y 1 A ALA 1159 ? A ALA 1146 
879 1 Y 1 A PRO 1160 ? A PRO 1147 
880 1 Y 1 A LYS 1161 ? A LYS 1148 
881 1 Y 1 A GLN 1162 ? A GLN 1149 
882 1 Y 1 A GLY 1163 ? A GLY 1150 
883 1 Y 1 A TYR 1164 ? A TYR 1151 
884 1 Y 1 A PHE 1165 ? A PHE 1152 
885 1 Y 1 A ILE 1166 ? A ILE 1153 
886 1 Y 1 A LYS 1167 ? A LYS 1154 
887 1 Y 1 A HIS 1168 ? A HIS 1155 
888 1 Y 1 A ASN 1169 ? A ASN 1156 
889 1 Y 1 A ASP 1170 ? A ASP 1157 
890 1 Y 1 A HIS 1171 ? A HIS 1158 
891 1 Y 1 A TRP 1172 ? A TRP 1159 
892 1 Y 1 A MET 1173 ? A MET 1160 
893 1 Y 1 A PHE 1174 ? A PHE 1161 
894 1 Y 1 A THR 1175 ? A THR 1162 
895 1 Y 1 A GLY 1176 ? A GLY 1163 
896 1 Y 1 A SER 1177 ? A SER 1164 
897 1 Y 1 A SER 1178 ? A SER 1165 
898 1 Y 1 A TYR 1179 ? A TYR 1166 
899 1 Y 1 A TYR 1180 ? A TYR 1167 
900 1 Y 1 A TYR 1181 ? A TYR 1168 
901 1 Y 1 A PRO 1182 ? A PRO 1169 
902 1 Y 1 A GLU 1183 ? A GLU 1170 
903 1 Y 1 A PRO 1184 ? A PRO 1171 
904 1 Y 1 A ILE 1185 ? A ILE 1172 
905 1 Y 1 A SER 1186 ? A SER 1173 
906 1 Y 1 A ASP 1187 ? A ASP 1174 
907 1 Y 1 A LYS 1188 ? A LYS 1175 
908 1 Y 1 A ASN 1189 ? A ASN 1176 
909 1 Y 1 A VAL 1190 ? A VAL 1177 
910 1 Y 1 A VAL 1191 ? A VAL 1178 
911 1 Y 1 A PHE 1192 ? A PHE 1179 
912 1 Y 1 A MET 1193 ? A MET 1180 
913 1 Y 1 A ASN 1194 ? A ASN 1181 
914 1 Y 1 A THR 1195 ? A THR 1182 
915 1 Y 1 A CYS 1196 ? A CYS 1183 
916 1 Y 1 A SER 1197 ? A SER 1184 
917 1 Y 1 A VAL 1198 ? A VAL 1185 
918 1 Y 1 A ASN 1199 ? A ASN 1186 
919 1 Y 1 A PHE 1200 ? A PHE 1187 
920 1 Y 1 A THR 1201 ? A THR 1188 
921 1 Y 1 A LYS 1202 ? A LYS 1189 
922 1 Y 1 A ALA 1203 ? A ALA 1190 
923 1 Y 1 A PRO 1204 ? A PRO 1191 
924 1 Y 1 A LEU 1205 ? A LEU 1192 
925 1 Y 1 A VAL 1206 ? A VAL 1193 
926 1 Y 1 A TYR 1207 ? A TYR 1194 
# 
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 
A1AR1 C21  C N R 1   
A1AR1 C6   C N R 2   
A1AR1 C7   C N R 3   
A1AR1 C8   C N R 4   
A1AR1 C11  C N N 5   
A1AR1 C10  C N N 6   
A1AR1 C9   C N N 7   
A1AR1 C5   C N R 8   
A1AR1 C4   C N S 9   
A1AR1 C3   C N N 10  
A1AR1 C2   C N S 11  
A1AR1 O6   O N N 12  
A1AR1 C1   C N N 13  
A1AR1 C12  C N N 14  
A1AR1 C31  C N N 15  
A1AR1 C41  C N S 16  
A1AR1 C51  C N R 17  
A1AR1 C61  C N R 18  
A1AR1 C71  C N S 19  
A1AR1 C81  C N R 20  
A1AR1 C91  C N N 21  
A1AR1 CA9  C N N 22  
A1AR1 CM9  C N N 23  
A1AR1 N5   N N N 24  
A1AR1 N51  N N N 25  
A1AR1 O10  O N N 26  
A1AR1 O1A  O N N 27  
A1AR1 O1B  O N N 28  
A1AR1 O3   O N N 29  
A1AR1 O4   O N N 30  
A1AR1 O41  O N N 31  
A1AR1 O61  O N N 32  
A1AR1 O7   O N N 33  
A1AR1 O71  O N N 34  
A1AR1 O8   O N N 35  
A1AR1 O81  O N N 36  
A1AR1 O9   O N N 37  
A1AR1 O91  O N N 38  
A1AR1 OA9  O N N 39  
A1AR1 C101 C N N 40  
A1AR1 C111 C N N 41  
A1AR1 O101 O N N 42  
A1AR1 O1A1 O N N 43  
A1AR1 O1B1 O N N 44  
A1AR1 H1   H N N 45  
A1AR1 H2   H N N 46  
A1AR1 H3   H N N 47  
A1AR1 H4   H N N 48  
A1AR1 H5   H N N 49  
A1AR1 H6   H N N 50  
A1AR1 H7   H N N 51  
A1AR1 H8   H N N 52  
A1AR1 H9   H N N 53  
A1AR1 H10  H N N 54  
A1AR1 H11  H N N 55  
A1AR1 H12  H N N 56  
A1AR1 H13  H N N 57  
A1AR1 H14  H N N 58  
A1AR1 H15  H N N 59  
A1AR1 H16  H N N 60  
A1AR1 H17  H N N 61  
A1AR1 H18  H N N 62  
A1AR1 H19  H N N 63  
A1AR1 H20  H N N 64  
A1AR1 H21  H N N 65  
A1AR1 H22  H N N 66  
A1AR1 H23  H N N 67  
A1AR1 H24  H N N 68  
A1AR1 H25  H N N 69  
A1AR1 H26  H N N 70  
A1AR1 H27  H N N 71  
A1AR1 H28  H N N 72  
A1AR1 H29  H N N 73  
A1AR1 H30  H N N 74  
A1AR1 H31  H N N 75  
A1AR1 H32  H N N 76  
A1AR1 H33  H N N 77  
A1AR1 H34  H N N 78  
A1AR1 H35  H N N 79  
A1AR1 H36  H N N 80  
A1AR1 H37  H N N 81  
A1AR1 H38  H N N 82  
ALA   N    N N N 83  
ALA   CA   C N S 84  
ALA   C    C N N 85  
ALA   O    O N N 86  
ALA   CB   C N N 87  
ALA   OXT  O N N 88  
ALA   H    H N N 89  
ALA   H2   H N N 90  
ALA   HA   H N N 91  
ALA   HB1  H N N 92  
ALA   HB2  H N N 93  
ALA   HB3  H N N 94  
ALA   HXT  H N N 95  
ARG   N    N N N 96  
ARG   CA   C N S 97  
ARG   C    C N N 98  
ARG   O    O N N 99  
ARG   CB   C N N 100 
ARG   CG   C N N 101 
ARG   CD   C N N 102 
ARG   NE   N N N 103 
ARG   CZ   C N N 104 
ARG   NH1  N N N 105 
ARG   NH2  N N N 106 
ARG   OXT  O N N 107 
ARG   H    H N N 108 
ARG   H2   H N N 109 
ARG   HA   H N N 110 
ARG   HB2  H N N 111 
ARG   HB3  H N N 112 
ARG   HG2  H N N 113 
ARG   HG3  H N N 114 
ARG   HD2  H N N 115 
ARG   HD3  H N N 116 
ARG   HE   H N N 117 
ARG   HH11 H N N 118 
ARG   HH12 H N N 119 
ARG   HH21 H N N 120 
ARG   HH22 H N N 121 
ARG   HXT  H N N 122 
ASN   N    N N N 123 
ASN   CA   C N S 124 
ASN   C    C N N 125 
ASN   O    O N N 126 
ASN   CB   C N N 127 
ASN   CG   C N N 128 
ASN   OD1  O N N 129 
ASN   ND2  N N N 130 
ASN   OXT  O N N 131 
ASN   H    H N N 132 
ASN   H2   H N N 133 
ASN   HA   H N N 134 
ASN   HB2  H N N 135 
ASN   HB3  H N N 136 
ASN   HD21 H N N 137 
ASN   HD22 H N N 138 
ASN   HXT  H N N 139 
ASP   N    N N N 140 
ASP   CA   C N S 141 
ASP   C    C N N 142 
ASP   O    O N N 143 
ASP   CB   C N N 144 
ASP   CG   C N N 145 
ASP   OD1  O N N 146 
ASP   OD2  O N N 147 
ASP   OXT  O N N 148 
ASP   H    H N N 149 
ASP   H2   H N N 150 
ASP   HA   H N N 151 
ASP   HB2  H N N 152 
ASP   HB3  H N N 153 
ASP   HD2  H N N 154 
ASP   HXT  H N N 155 
BMA   C1   C N R 156 
BMA   C2   C N S 157 
BMA   C3   C N S 158 
BMA   C4   C N S 159 
BMA   C5   C N R 160 
BMA   C6   C N N 161 
BMA   O1   O N N 162 
BMA   O2   O N N 163 
BMA   O3   O N N 164 
BMA   O4   O N N 165 
BMA   O5   O N N 166 
BMA   O6   O N N 167 
BMA   H1   H N N 168 
BMA   H2   H N N 169 
BMA   H3   H N N 170 
BMA   H4   H N N 171 
BMA   H5   H N N 172 
BMA   H61  H N N 173 
BMA   H62  H N N 174 
BMA   HO1  H N N 175 
BMA   HO2  H N N 176 
BMA   HO3  H N N 177 
BMA   HO4  H N N 178 
BMA   HO6  H N N 179 
CYS   N    N N N 180 
CYS   CA   C N R 181 
CYS   C    C N N 182 
CYS   O    O N N 183 
CYS   CB   C N N 184 
CYS   SG   S N N 185 
CYS   OXT  O N N 186 
CYS   H    H N N 187 
CYS   H2   H N N 188 
CYS   HA   H N N 189 
CYS   HB2  H N N 190 
CYS   HB3  H N N 191 
CYS   HG   H N N 192 
CYS   HXT  H N N 193 
GLN   N    N N N 194 
GLN   CA   C N S 195 
GLN   C    C N N 196 
GLN   O    O N N 197 
GLN   CB   C N N 198 
GLN   CG   C N N 199 
GLN   CD   C N N 200 
GLN   OE1  O N N 201 
GLN   NE2  N N N 202 
GLN   OXT  O N N 203 
GLN   H    H N N 204 
GLN   H2   H N N 205 
GLN   HA   H N N 206 
GLN   HB2  H N N 207 
GLN   HB3  H N N 208 
GLN   HG2  H N N 209 
GLN   HG3  H N N 210 
GLN   HE21 H N N 211 
GLN   HE22 H N N 212 
GLN   HXT  H N N 213 
GLU   N    N N N 214 
GLU   CA   C N S 215 
GLU   C    C N N 216 
GLU   O    O N N 217 
GLU   CB   C N N 218 
GLU   CG   C N N 219 
GLU   CD   C N N 220 
GLU   OE1  O N N 221 
GLU   OE2  O N N 222 
GLU   OXT  O N N 223 
GLU   H    H N N 224 
GLU   H2   H N N 225 
GLU   HA   H N N 226 
GLU   HB2  H N N 227 
GLU   HB3  H N N 228 
GLU   HG2  H N N 229 
GLU   HG3  H N N 230 
GLU   HE2  H N N 231 
GLU   HXT  H N N 232 
GLY   N    N N N 233 
GLY   CA   C N N 234 
GLY   C    C N N 235 
GLY   O    O N N 236 
GLY   OXT  O N N 237 
GLY   H    H N N 238 
GLY   H2   H N N 239 
GLY   HA2  H N N 240 
GLY   HA3  H N N 241 
GLY   HXT  H N N 242 
HIS   N    N N N 243 
HIS   CA   C N S 244 
HIS   C    C N N 245 
HIS   O    O N N 246 
HIS   CB   C N N 247 
HIS   CG   C Y N 248 
HIS   ND1  N Y N 249 
HIS   CD2  C Y N 250 
HIS   CE1  C Y N 251 
HIS   NE2  N Y N 252 
HIS   OXT  O N N 253 
HIS   H    H N N 254 
HIS   H2   H N N 255 
HIS   HA   H N N 256 
HIS   HB2  H N N 257 
HIS   HB3  H N N 258 
HIS   HD1  H N N 259 
HIS   HD2  H N N 260 
HIS   HE1  H N N 261 
HIS   HE2  H N N 262 
HIS   HXT  H N N 263 
ILE   N    N N N 264 
ILE   CA   C N S 265 
ILE   C    C N N 266 
ILE   O    O N N 267 
ILE   CB   C N S 268 
ILE   CG1  C N N 269 
ILE   CG2  C N N 270 
ILE   CD1  C N N 271 
ILE   OXT  O N N 272 
ILE   H    H N N 273 
ILE   H2   H N N 274 
ILE   HA   H N N 275 
ILE   HB   H N N 276 
ILE   HG12 H N N 277 
ILE   HG13 H N N 278 
ILE   HG21 H N N 279 
ILE   HG22 H N N 280 
ILE   HG23 H N N 281 
ILE   HD11 H N N 282 
ILE   HD12 H N N 283 
ILE   HD13 H N N 284 
ILE   HXT  H N N 285 
LEU   N    N N N 286 
LEU   CA   C N S 287 
LEU   C    C N N 288 
LEU   O    O N N 289 
LEU   CB   C N N 290 
LEU   CG   C N N 291 
LEU   CD1  C N N 292 
LEU   CD2  C N N 293 
LEU   OXT  O N N 294 
LEU   H    H N N 295 
LEU   H2   H N N 296 
LEU   HA   H N N 297 
LEU   HB2  H N N 298 
LEU   HB3  H N N 299 
LEU   HG   H N N 300 
LEU   HD11 H N N 301 
LEU   HD12 H N N 302 
LEU   HD13 H N N 303 
LEU   HD21 H N N 304 
LEU   HD22 H N N 305 
LEU   HD23 H N N 306 
LEU   HXT  H N N 307 
LYS   N    N N N 308 
LYS   CA   C N S 309 
LYS   C    C N N 310 
LYS   O    O N N 311 
LYS   CB   C N N 312 
LYS   CG   C N N 313 
LYS   CD   C N N 314 
LYS   CE   C N N 315 
LYS   NZ   N N N 316 
LYS   OXT  O N N 317 
LYS   H    H N N 318 
LYS   H2   H N N 319 
LYS   HA   H N N 320 
LYS   HB2  H N N 321 
LYS   HB3  H N N 322 
LYS   HG2  H N N 323 
LYS   HG3  H N N 324 
LYS   HD2  H N N 325 
LYS   HD3  H N N 326 
LYS   HE2  H N N 327 
LYS   HE3  H N N 328 
LYS   HZ1  H N N 329 
LYS   HZ2  H N N 330 
LYS   HZ3  H N N 331 
LYS   HXT  H N N 332 
MAN   C1   C N S 333 
MAN   C2   C N S 334 
MAN   C3   C N S 335 
MAN   C4   C N S 336 
MAN   C5   C N R 337 
MAN   C6   C N N 338 
MAN   O1   O N N 339 
MAN   O2   O N N 340 
MAN   O3   O N N 341 
MAN   O4   O N N 342 
MAN   O5   O N N 343 
MAN   O6   O N N 344 
MAN   H1   H N N 345 
MAN   H2   H N N 346 
MAN   H3   H N N 347 
MAN   H4   H N N 348 
MAN   H5   H N N 349 
MAN   H61  H N N 350 
MAN   H62  H N N 351 
MAN   HO1  H N N 352 
MAN   HO2  H N N 353 
MAN   HO3  H N N 354 
MAN   HO4  H N N 355 
MAN   HO6  H N N 356 
MET   N    N N N 357 
MET   CA   C N S 358 
MET   C    C N N 359 
MET   O    O N N 360 
MET   CB   C N N 361 
MET   CG   C N N 362 
MET   SD   S N N 363 
MET   CE   C N N 364 
MET   OXT  O N N 365 
MET   H    H N N 366 
MET   H2   H N N 367 
MET   HA   H N N 368 
MET   HB2  H N N 369 
MET   HB3  H N N 370 
MET   HG2  H N N 371 
MET   HG3  H N N 372 
MET   HE1  H N N 373 
MET   HE2  H N N 374 
MET   HE3  H N N 375 
MET   HXT  H N N 376 
NAG   C1   C N R 377 
NAG   C2   C N R 378 
NAG   C3   C N R 379 
NAG   C4   C N S 380 
NAG   C5   C N R 381 
NAG   C6   C N N 382 
NAG   C7   C N N 383 
NAG   C8   C N N 384 
NAG   N2   N N N 385 
NAG   O1   O N N 386 
NAG   O3   O N N 387 
NAG   O4   O N N 388 
NAG   O5   O N N 389 
NAG   O6   O N N 390 
NAG   O7   O N N 391 
NAG   H1   H N N 392 
NAG   H2   H N N 393 
NAG   H3   H N N 394 
NAG   H4   H N N 395 
NAG   H5   H N N 396 
NAG   H61  H N N 397 
NAG   H62  H N N 398 
NAG   H81  H N N 399 
NAG   H82  H N N 400 
NAG   H83  H N N 401 
NAG   HN2  H N N 402 
NAG   HO1  H N N 403 
NAG   HO3  H N N 404 
NAG   HO4  H N N 405 
NAG   HO6  H N N 406 
PHE   N    N N N 407 
PHE   CA   C N S 408 
PHE   C    C N N 409 
PHE   O    O N N 410 
PHE   CB   C N N 411 
PHE   CG   C Y N 412 
PHE   CD1  C Y N 413 
PHE   CD2  C Y N 414 
PHE   CE1  C Y N 415 
PHE   CE2  C Y N 416 
PHE   CZ   C Y N 417 
PHE   OXT  O N N 418 
PHE   H    H N N 419 
PHE   H2   H N N 420 
PHE   HA   H N N 421 
PHE   HB2  H N N 422 
PHE   HB3  H N N 423 
PHE   HD1  H N N 424 
PHE   HD2  H N N 425 
PHE   HE1  H N N 426 
PHE   HE2  H N N 427 
PHE   HZ   H N N 428 
PHE   HXT  H N N 429 
PRO   N    N N N 430 
PRO   CA   C N S 431 
PRO   C    C N N 432 
PRO   O    O N N 433 
PRO   CB   C N N 434 
PRO   CG   C N N 435 
PRO   CD   C N N 436 
PRO   OXT  O N N 437 
PRO   H    H N N 438 
PRO   HA   H N N 439 
PRO   HB2  H N N 440 
PRO   HB3  H N N 441 
PRO   HG2  H N N 442 
PRO   HG3  H N N 443 
PRO   HD2  H N N 444 
PRO   HD3  H N N 445 
PRO   HXT  H N N 446 
SER   N    N N N 447 
SER   CA   C N S 448 
SER   C    C N N 449 
SER   O    O N N 450 
SER   CB   C N N 451 
SER   OG   O N N 452 
SER   OXT  O N N 453 
SER   H    H N N 454 
SER   H2   H N N 455 
SER   HA   H N N 456 
SER   HB2  H N N 457 
SER   HB3  H N N 458 
SER   HG   H N N 459 
SER   HXT  H N N 460 
THR   N    N N N 461 
THR   CA   C N S 462 
THR   C    C N N 463 
THR   O    O N N 464 
THR   CB   C N R 465 
THR   OG1  O N N 466 
THR   CG2  C N N 467 
THR   OXT  O N N 468 
THR   H    H N N 469 
THR   H2   H N N 470 
THR   HA   H N N 471 
THR   HB   H N N 472 
THR   HG1  H N N 473 
THR   HG21 H N N 474 
THR   HG22 H N N 475 
THR   HG23 H N N 476 
THR   HXT  H N N 477 
TRP   N    N N N 478 
TRP   CA   C N S 479 
TRP   C    C N N 480 
TRP   O    O N N 481 
TRP   CB   C N N 482 
TRP   CG   C Y N 483 
TRP   CD1  C Y N 484 
TRP   CD2  C Y N 485 
TRP   NE1  N Y N 486 
TRP   CE2  C Y N 487 
TRP   CE3  C Y N 488 
TRP   CZ2  C Y N 489 
TRP   CZ3  C Y N 490 
TRP   CH2  C Y N 491 
TRP   OXT  O N N 492 
TRP   H    H N N 493 
TRP   H2   H N N 494 
TRP   HA   H N N 495 
TRP   HB2  H N N 496 
TRP   HB3  H N N 497 
TRP   HD1  H N N 498 
TRP   HE1  H N N 499 
TRP   HE3  H N N 500 
TRP   HZ2  H N N 501 
TRP   HZ3  H N N 502 
TRP   HH2  H N N 503 
TRP   HXT  H N N 504 
TYR   N    N N N 505 
TYR   CA   C N S 506 
TYR   C    C N N 507 
TYR   O    O N N 508 
TYR   CB   C N N 509 
TYR   CG   C Y N 510 
TYR   CD1  C Y N 511 
TYR   CD2  C Y N 512 
TYR   CE1  C Y N 513 
TYR   CE2  C Y N 514 
TYR   CZ   C Y N 515 
TYR   OH   O N N 516 
TYR   OXT  O N N 517 
TYR   H    H N N 518 
TYR   H2   H N N 519 
TYR   HA   H N N 520 
TYR   HB2  H N N 521 
TYR   HB3  H N N 522 
TYR   HD1  H N N 523 
TYR   HD2  H N N 524 
TYR   HE1  H N N 525 
TYR   HE2  H N N 526 
TYR   HH   H N N 527 
TYR   HXT  H N N 528 
VAL   N    N N N 529 
VAL   CA   C N S 530 
VAL   C    C N N 531 
VAL   O    O N N 532 
VAL   CB   C N N 533 
VAL   CG1  C N N 534 
VAL   CG2  C N N 535 
VAL   OXT  O N N 536 
VAL   H    H N N 537 
VAL   H2   H N N 538 
VAL   HA   H N N 539 
VAL   HB   H N N 540 
VAL   HG11 H N N 541 
VAL   HG12 H N N 542 
VAL   HG13 H N N 543 
VAL   HG21 H N N 544 
VAL   HG22 H N N 545 
VAL   HG23 H N N 546 
VAL   HXT  H N N 547 
# 
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 
A1AR1 OA9  CA9  doub N N 1   
A1AR1 CM9  CA9  sing N N 2   
A1AR1 O1B1 C12  doub N N 3   
A1AR1 CA9  O9   sing N N 4   
A1AR1 C12  O1A1 sing N N 5   
A1AR1 C12  C21  sing N N 6   
A1AR1 O9   C9   sing N N 7   
A1AR1 O41  C41  sing N N 8   
A1AR1 C31  C41  sing N N 9   
A1AR1 C31  C21  sing N N 10  
A1AR1 C41  C51  sing N N 11  
A1AR1 C9   C8   sing N N 12  
A1AR1 O3   C21  sing N N 13  
A1AR1 C21  O61  sing N N 14  
A1AR1 O8   C8   sing N N 15  
A1AR1 C8   C7   sing N N 16  
A1AR1 C51  N51  sing N N 17  
A1AR1 C51  C61  sing N N 18  
A1AR1 O61  C61  sing N N 19  
A1AR1 N51  C101 sing N N 20  
A1AR1 C61  C71  sing N N 21  
A1AR1 O1B  C1   doub N N 22  
A1AR1 C7   O7   sing N N 23  
A1AR1 C7   C6   sing N N 24  
A1AR1 C101 C111 sing N N 25  
A1AR1 C101 O101 doub N N 26  
A1AR1 C1   O1A  sing N N 27  
A1AR1 C1   C2   sing N N 28  
A1AR1 C6   O6   sing N N 29  
A1AR1 C6   C5   sing N N 30  
A1AR1 C71  C81  sing N N 31  
A1AR1 C71  O71  sing N N 32  
A1AR1 C81  C91  sing N N 33  
A1AR1 C81  O81  sing N N 34  
A1AR1 O6   C2   sing N N 35  
A1AR1 C11  C10  sing N N 36  
A1AR1 C91  O91  sing N N 37  
A1AR1 C10  O10  doub N N 38  
A1AR1 C10  N5   sing N N 39  
A1AR1 C2   O81  sing N N 40  
A1AR1 C2   C3   sing N N 41  
A1AR1 N5   C5   sing N N 42  
A1AR1 C5   C4   sing N N 43  
A1AR1 C4   C3   sing N N 44  
A1AR1 C4   O4   sing N N 45  
A1AR1 C6   H1   sing N N 46  
A1AR1 C7   H2   sing N N 47  
A1AR1 C8   H3   sing N N 48  
A1AR1 C11  H4   sing N N 49  
A1AR1 C11  H5   sing N N 50  
A1AR1 C11  H6   sing N N 51  
A1AR1 C9   H7   sing N N 52  
A1AR1 C9   H8   sing N N 53  
A1AR1 C5   H9   sing N N 54  
A1AR1 C4   H10  sing N N 55  
A1AR1 C3   H11  sing N N 56  
A1AR1 C3   H12  sing N N 57  
A1AR1 C31  H13  sing N N 58  
A1AR1 C31  H14  sing N N 59  
A1AR1 C41  H15  sing N N 60  
A1AR1 C51  H16  sing N N 61  
A1AR1 C61  H17  sing N N 62  
A1AR1 C71  H18  sing N N 63  
A1AR1 C81  H19  sing N N 64  
A1AR1 C91  H20  sing N N 65  
A1AR1 C91  H21  sing N N 66  
A1AR1 CM9  H22  sing N N 67  
A1AR1 CM9  H23  sing N N 68  
A1AR1 CM9  H24  sing N N 69  
A1AR1 N5   H25  sing N N 70  
A1AR1 N51  H26  sing N N 71  
A1AR1 O1A  H27  sing N N 72  
A1AR1 O3   H28  sing N N 73  
A1AR1 O4   H29  sing N N 74  
A1AR1 O41  H30  sing N N 75  
A1AR1 O7   H31  sing N N 76  
A1AR1 O71  H32  sing N N 77  
A1AR1 O8   H33  sing N N 78  
A1AR1 O91  H34  sing N N 79  
A1AR1 C111 H35  sing N N 80  
A1AR1 C111 H36  sing N N 81  
A1AR1 C111 H37  sing N N 82  
A1AR1 O1A1 H38  sing N N 83  
ALA   N    CA   sing N N 84  
ALA   N    H    sing N N 85  
ALA   N    H2   sing N N 86  
ALA   CA   C    sing N N 87  
ALA   CA   CB   sing N N 88  
ALA   CA   HA   sing N N 89  
ALA   C    O    doub N N 90  
ALA   C    OXT  sing N N 91  
ALA   CB   HB1  sing N N 92  
ALA   CB   HB2  sing N N 93  
ALA   CB   HB3  sing N N 94  
ALA   OXT  HXT  sing N N 95  
ARG   N    CA   sing N N 96  
ARG   N    H    sing N N 97  
ARG   N    H2   sing N N 98  
ARG   CA   C    sing N N 99  
ARG   CA   CB   sing N N 100 
ARG   CA   HA   sing N N 101 
ARG   C    O    doub N N 102 
ARG   C    OXT  sing N N 103 
ARG   CB   CG   sing N N 104 
ARG   CB   HB2  sing N N 105 
ARG   CB   HB3  sing N N 106 
ARG   CG   CD   sing N N 107 
ARG   CG   HG2  sing N N 108 
ARG   CG   HG3  sing N N 109 
ARG   CD   NE   sing N N 110 
ARG   CD   HD2  sing N N 111 
ARG   CD   HD3  sing N N 112 
ARG   NE   CZ   sing N N 113 
ARG   NE   HE   sing N N 114 
ARG   CZ   NH1  sing N N 115 
ARG   CZ   NH2  doub N N 116 
ARG   NH1  HH11 sing N N 117 
ARG   NH1  HH12 sing N N 118 
ARG   NH2  HH21 sing N N 119 
ARG   NH2  HH22 sing N N 120 
ARG   OXT  HXT  sing N N 121 
ASN   N    CA   sing N N 122 
ASN   N    H    sing N N 123 
ASN   N    H2   sing N N 124 
ASN   CA   C    sing N N 125 
ASN   CA   CB   sing N N 126 
ASN   CA   HA   sing N N 127 
ASN   C    O    doub N N 128 
ASN   C    OXT  sing N N 129 
ASN   CB   CG   sing N N 130 
ASN   CB   HB2  sing N N 131 
ASN   CB   HB3  sing N N 132 
ASN   CG   OD1  doub N N 133 
ASN   CG   ND2  sing N N 134 
ASN   ND2  HD21 sing N N 135 
ASN   ND2  HD22 sing N N 136 
ASN   OXT  HXT  sing N N 137 
ASP   N    CA   sing N N 138 
ASP   N    H    sing N N 139 
ASP   N    H2   sing N N 140 
ASP   CA   C    sing N N 141 
ASP   CA   CB   sing N N 142 
ASP   CA   HA   sing N N 143 
ASP   C    O    doub N N 144 
ASP   C    OXT  sing N N 145 
ASP   CB   CG   sing N N 146 
ASP   CB   HB2  sing N N 147 
ASP   CB   HB3  sing N N 148 
ASP   CG   OD1  doub N N 149 
ASP   CG   OD2  sing N N 150 
ASP   OD2  HD2  sing N N 151 
ASP   OXT  HXT  sing N N 152 
BMA   C1   C2   sing N N 153 
BMA   C1   O1   sing N N 154 
BMA   C1   O5   sing N N 155 
BMA   C1   H1   sing N N 156 
BMA   C2   C3   sing N N 157 
BMA   C2   O2   sing N N 158 
BMA   C2   H2   sing N N 159 
BMA   C3   C4   sing N N 160 
BMA   C3   O3   sing N N 161 
BMA   C3   H3   sing N N 162 
BMA   C4   C5   sing N N 163 
BMA   C4   O4   sing N N 164 
BMA   C4   H4   sing N N 165 
BMA   C5   C6   sing N N 166 
BMA   C5   O5   sing N N 167 
BMA   C5   H5   sing N N 168 
BMA   C6   O6   sing N N 169 
BMA   C6   H61  sing N N 170 
BMA   C6   H62  sing N N 171 
BMA   O1   HO1  sing N N 172 
BMA   O2   HO2  sing N N 173 
BMA   O3   HO3  sing N N 174 
BMA   O4   HO4  sing N N 175 
BMA   O6   HO6  sing N N 176 
CYS   N    CA   sing N N 177 
CYS   N    H    sing N N 178 
CYS   N    H2   sing N N 179 
CYS   CA   C    sing N N 180 
CYS   CA   CB   sing N N 181 
CYS   CA   HA   sing N N 182 
CYS   C    O    doub N N 183 
CYS   C    OXT  sing N N 184 
CYS   CB   SG   sing N N 185 
CYS   CB   HB2  sing N N 186 
CYS   CB   HB3  sing N N 187 
CYS   SG   HG   sing N N 188 
CYS   OXT  HXT  sing N N 189 
GLN   N    CA   sing N N 190 
GLN   N    H    sing N N 191 
GLN   N    H2   sing N N 192 
GLN   CA   C    sing N N 193 
GLN   CA   CB   sing N N 194 
GLN   CA   HA   sing N N 195 
GLN   C    O    doub N N 196 
GLN   C    OXT  sing N N 197 
GLN   CB   CG   sing N N 198 
GLN   CB   HB2  sing N N 199 
GLN   CB   HB3  sing N N 200 
GLN   CG   CD   sing N N 201 
GLN   CG   HG2  sing N N 202 
GLN   CG   HG3  sing N N 203 
GLN   CD   OE1  doub N N 204 
GLN   CD   NE2  sing N N 205 
GLN   NE2  HE21 sing N N 206 
GLN   NE2  HE22 sing N N 207 
GLN   OXT  HXT  sing N N 208 
GLU   N    CA   sing N N 209 
GLU   N    H    sing N N 210 
GLU   N    H2   sing N N 211 
GLU   CA   C    sing N N 212 
GLU   CA   CB   sing N N 213 
GLU   CA   HA   sing N N 214 
GLU   C    O    doub N N 215 
GLU   C    OXT  sing N N 216 
GLU   CB   CG   sing N N 217 
GLU   CB   HB2  sing N N 218 
GLU   CB   HB3  sing N N 219 
GLU   CG   CD   sing N N 220 
GLU   CG   HG2  sing N N 221 
GLU   CG   HG3  sing N N 222 
GLU   CD   OE1  doub N N 223 
GLU   CD   OE2  sing N N 224 
GLU   OE2  HE2  sing N N 225 
GLU   OXT  HXT  sing N N 226 
GLY   N    CA   sing N N 227 
GLY   N    H    sing N N 228 
GLY   N    H2   sing N N 229 
GLY   CA   C    sing N N 230 
GLY   CA   HA2  sing N N 231 
GLY   CA   HA3  sing N N 232 
GLY   C    O    doub N N 233 
GLY   C    OXT  sing N N 234 
GLY   OXT  HXT  sing N N 235 
HIS   N    CA   sing N N 236 
HIS   N    H    sing N N 237 
HIS   N    H2   sing N N 238 
HIS   CA   C    sing N N 239 
HIS   CA   CB   sing N N 240 
HIS   CA   HA   sing N N 241 
HIS   C    O    doub N N 242 
HIS   C    OXT  sing N N 243 
HIS   CB   CG   sing N N 244 
HIS   CB   HB2  sing N N 245 
HIS   CB   HB3  sing N N 246 
HIS   CG   ND1  sing Y N 247 
HIS   CG   CD2  doub Y N 248 
HIS   ND1  CE1  doub Y N 249 
HIS   ND1  HD1  sing N N 250 
HIS   CD2  NE2  sing Y N 251 
HIS   CD2  HD2  sing N N 252 
HIS   CE1  NE2  sing Y N 253 
HIS   CE1  HE1  sing N N 254 
HIS   NE2  HE2  sing N N 255 
HIS   OXT  HXT  sing N N 256 
ILE   N    CA   sing N N 257 
ILE   N    H    sing N N 258 
ILE   N    H2   sing N N 259 
ILE   CA   C    sing N N 260 
ILE   CA   CB   sing N N 261 
ILE   CA   HA   sing N N 262 
ILE   C    O    doub N N 263 
ILE   C    OXT  sing N N 264 
ILE   CB   CG1  sing N N 265 
ILE   CB   CG2  sing N N 266 
ILE   CB   HB   sing N N 267 
ILE   CG1  CD1  sing N N 268 
ILE   CG1  HG12 sing N N 269 
ILE   CG1  HG13 sing N N 270 
ILE   CG2  HG21 sing N N 271 
ILE   CG2  HG22 sing N N 272 
ILE   CG2  HG23 sing N N 273 
ILE   CD1  HD11 sing N N 274 
ILE   CD1  HD12 sing N N 275 
ILE   CD1  HD13 sing N N 276 
ILE   OXT  HXT  sing N N 277 
LEU   N    CA   sing N N 278 
LEU   N    H    sing N N 279 
LEU   N    H2   sing N N 280 
LEU   CA   C    sing N N 281 
LEU   CA   CB   sing N N 282 
LEU   CA   HA   sing N N 283 
LEU   C    O    doub N N 284 
LEU   C    OXT  sing N N 285 
LEU   CB   CG   sing N N 286 
LEU   CB   HB2  sing N N 287 
LEU   CB   HB3  sing N N 288 
LEU   CG   CD1  sing N N 289 
LEU   CG   CD2  sing N N 290 
LEU   CG   HG   sing N N 291 
LEU   CD1  HD11 sing N N 292 
LEU   CD1  HD12 sing N N 293 
LEU   CD1  HD13 sing N N 294 
LEU   CD2  HD21 sing N N 295 
LEU   CD2  HD22 sing N N 296 
LEU   CD2  HD23 sing N N 297 
LEU   OXT  HXT  sing N N 298 
LYS   N    CA   sing N N 299 
LYS   N    H    sing N N 300 
LYS   N    H2   sing N N 301 
LYS   CA   C    sing N N 302 
LYS   CA   CB   sing N N 303 
LYS   CA   HA   sing N N 304 
LYS   C    O    doub N N 305 
LYS   C    OXT  sing N N 306 
LYS   CB   CG   sing N N 307 
LYS   CB   HB2  sing N N 308 
LYS   CB   HB3  sing N N 309 
LYS   CG   CD   sing N N 310 
LYS   CG   HG2  sing N N 311 
LYS   CG   HG3  sing N N 312 
LYS   CD   CE   sing N N 313 
LYS   CD   HD2  sing N N 314 
LYS   CD   HD3  sing N N 315 
LYS   CE   NZ   sing N N 316 
LYS   CE   HE2  sing N N 317 
LYS   CE   HE3  sing N N 318 
LYS   NZ   HZ1  sing N N 319 
LYS   NZ   HZ2  sing N N 320 
LYS   NZ   HZ3  sing N N 321 
LYS   OXT  HXT  sing N N 322 
MAN   C1   C2   sing N N 323 
MAN   C1   O1   sing N N 324 
MAN   C1   O5   sing N N 325 
MAN   C1   H1   sing N N 326 
MAN   C2   C3   sing N N 327 
MAN   C2   O2   sing N N 328 
MAN   C2   H2   sing N N 329 
MAN   C3   C4   sing N N 330 
MAN   C3   O3   sing N N 331 
MAN   C3   H3   sing N N 332 
MAN   C4   C5   sing N N 333 
MAN   C4   O4   sing N N 334 
MAN   C4   H4   sing N N 335 
MAN   C5   C6   sing N N 336 
MAN   C5   O5   sing N N 337 
MAN   C5   H5   sing N N 338 
MAN   C6   O6   sing N N 339 
MAN   C6   H61  sing N N 340 
MAN   C6   H62  sing N N 341 
MAN   O1   HO1  sing N N 342 
MAN   O2   HO2  sing N N 343 
MAN   O3   HO3  sing N N 344 
MAN   O4   HO4  sing N N 345 
MAN   O6   HO6  sing N N 346 
MET   N    CA   sing N N 347 
MET   N    H    sing N N 348 
MET   N    H2   sing N N 349 
MET   CA   C    sing N N 350 
MET   CA   CB   sing N N 351 
MET   CA   HA   sing N N 352 
MET   C    O    doub N N 353 
MET   C    OXT  sing N N 354 
MET   CB   CG   sing N N 355 
MET   CB   HB2  sing N N 356 
MET   CB   HB3  sing N N 357 
MET   CG   SD   sing N N 358 
MET   CG   HG2  sing N N 359 
MET   CG   HG3  sing N N 360 
MET   SD   CE   sing N N 361 
MET   CE   HE1  sing N N 362 
MET   CE   HE2  sing N N 363 
MET   CE   HE3  sing N N 364 
MET   OXT  HXT  sing N N 365 
NAG   C1   C2   sing N N 366 
NAG   C1   O1   sing N N 367 
NAG   C1   O5   sing N N 368 
NAG   C1   H1   sing N N 369 
NAG   C2   C3   sing N N 370 
NAG   C2   N2   sing N N 371 
NAG   C2   H2   sing N N 372 
NAG   C3   C4   sing N N 373 
NAG   C3   O3   sing N N 374 
NAG   C3   H3   sing N N 375 
NAG   C4   C5   sing N N 376 
NAG   C4   O4   sing N N 377 
NAG   C4   H4   sing N N 378 
NAG   C5   C6   sing N N 379 
NAG   C5   O5   sing N N 380 
NAG   C5   H5   sing N N 381 
NAG   C6   O6   sing N N 382 
NAG   C6   H61  sing N N 383 
NAG   C6   H62  sing N N 384 
NAG   C7   C8   sing N N 385 
NAG   C7   N2   sing N N 386 
NAG   C7   O7   doub N N 387 
NAG   C8   H81  sing N N 388 
NAG   C8   H82  sing N N 389 
NAG   C8   H83  sing N N 390 
NAG   N2   HN2  sing N N 391 
NAG   O1   HO1  sing N N 392 
NAG   O3   HO3  sing N N 393 
NAG   O4   HO4  sing N N 394 
NAG   O6   HO6  sing N N 395 
PHE   N    CA   sing N N 396 
PHE   N    H    sing N N 397 
PHE   N    H2   sing N N 398 
PHE   CA   C    sing N N 399 
PHE   CA   CB   sing N N 400 
PHE   CA   HA   sing N N 401 
PHE   C    O    doub N N 402 
PHE   C    OXT  sing N N 403 
PHE   CB   CG   sing N N 404 
PHE   CB   HB2  sing N N 405 
PHE   CB   HB3  sing N N 406 
PHE   CG   CD1  doub Y N 407 
PHE   CG   CD2  sing Y N 408 
PHE   CD1  CE1  sing Y N 409 
PHE   CD1  HD1  sing N N 410 
PHE   CD2  CE2  doub Y N 411 
PHE   CD2  HD2  sing N N 412 
PHE   CE1  CZ   doub Y N 413 
PHE   CE1  HE1  sing N N 414 
PHE   CE2  CZ   sing Y N 415 
PHE   CE2  HE2  sing N N 416 
PHE   CZ   HZ   sing N N 417 
PHE   OXT  HXT  sing N N 418 
PRO   N    CA   sing N N 419 
PRO   N    CD   sing N N 420 
PRO   N    H    sing N N 421 
PRO   CA   C    sing N N 422 
PRO   CA   CB   sing N N 423 
PRO   CA   HA   sing N N 424 
PRO   C    O    doub N N 425 
PRO   C    OXT  sing N N 426 
PRO   CB   CG   sing N N 427 
PRO   CB   HB2  sing N N 428 
PRO   CB   HB3  sing N N 429 
PRO   CG   CD   sing N N 430 
PRO   CG   HG2  sing N N 431 
PRO   CG   HG3  sing N N 432 
PRO   CD   HD2  sing N N 433 
PRO   CD   HD3  sing N N 434 
PRO   OXT  HXT  sing N N 435 
SER   N    CA   sing N N 436 
SER   N    H    sing N N 437 
SER   N    H2   sing N N 438 
SER   CA   C    sing N N 439 
SER   CA   CB   sing N N 440 
SER   CA   HA   sing N N 441 
SER   C    O    doub N N 442 
SER   C    OXT  sing N N 443 
SER   CB   OG   sing N N 444 
SER   CB   HB2  sing N N 445 
SER   CB   HB3  sing N N 446 
SER   OG   HG   sing N N 447 
SER   OXT  HXT  sing N N 448 
THR   N    CA   sing N N 449 
THR   N    H    sing N N 450 
THR   N    H2   sing N N 451 
THR   CA   C    sing N N 452 
THR   CA   CB   sing N N 453 
THR   CA   HA   sing N N 454 
THR   C    O    doub N N 455 
THR   C    OXT  sing N N 456 
THR   CB   OG1  sing N N 457 
THR   CB   CG2  sing N N 458 
THR   CB   HB   sing N N 459 
THR   OG1  HG1  sing N N 460 
THR   CG2  HG21 sing N N 461 
THR   CG2  HG22 sing N N 462 
THR   CG2  HG23 sing N N 463 
THR   OXT  HXT  sing N N 464 
TRP   N    CA   sing N N 465 
TRP   N    H    sing N N 466 
TRP   N    H2   sing N N 467 
TRP   CA   C    sing N N 468 
TRP   CA   CB   sing N N 469 
TRP   CA   HA   sing N N 470 
TRP   C    O    doub N N 471 
TRP   C    OXT  sing N N 472 
TRP   CB   CG   sing N N 473 
TRP   CB   HB2  sing N N 474 
TRP   CB   HB3  sing N N 475 
TRP   CG   CD1  doub Y N 476 
TRP   CG   CD2  sing Y N 477 
TRP   CD1  NE1  sing Y N 478 
TRP   CD1  HD1  sing N N 479 
TRP   CD2  CE2  doub Y N 480 
TRP   CD2  CE3  sing Y N 481 
TRP   NE1  CE2  sing Y N 482 
TRP   NE1  HE1  sing N N 483 
TRP   CE2  CZ2  sing Y N 484 
TRP   CE3  CZ3  doub Y N 485 
TRP   CE3  HE3  sing N N 486 
TRP   CZ2  CH2  doub Y N 487 
TRP   CZ2  HZ2  sing N N 488 
TRP   CZ3  CH2  sing Y N 489 
TRP   CZ3  HZ3  sing N N 490 
TRP   CH2  HH2  sing N N 491 
TRP   OXT  HXT  sing N N 492 
TYR   N    CA   sing N N 493 
TYR   N    H    sing N N 494 
TYR   N    H2   sing N N 495 
TYR   CA   C    sing N N 496 
TYR   CA   CB   sing N N 497 
TYR   CA   HA   sing N N 498 
TYR   C    O    doub N N 499 
TYR   C    OXT  sing N N 500 
TYR   CB   CG   sing N N 501 
TYR   CB   HB2  sing N N 502 
TYR   CB   HB3  sing N N 503 
TYR   CG   CD1  doub Y N 504 
TYR   CG   CD2  sing Y N 505 
TYR   CD1  CE1  sing Y N 506 
TYR   CD1  HD1  sing N N 507 
TYR   CD2  CE2  doub Y N 508 
TYR   CD2  HD2  sing N N 509 
TYR   CE1  CZ   doub Y N 510 
TYR   CE1  HE1  sing N N 511 
TYR   CE2  CZ   sing Y N 512 
TYR   CE2  HE2  sing N N 513 
TYR   CZ   OH   sing N N 514 
TYR   OH   HH   sing N N 515 
TYR   OXT  HXT  sing N N 516 
VAL   N    CA   sing N N 517 
VAL   N    H    sing N N 518 
VAL   N    H2   sing N N 519 
VAL   CA   C    sing N N 520 
VAL   CA   CB   sing N N 521 
VAL   CA   HA   sing N N 522 
VAL   C    O    doub N N 523 
VAL   C    OXT  sing N N 524 
VAL   CB   CG1  sing N N 525 
VAL   CB   CG2  sing N N 526 
VAL   CB   HB   sing N N 527 
VAL   CG1  HG11 sing N N 528 
VAL   CG1  HG12 sing N N 529 
VAL   CG1  HG13 sing N N 530 
VAL   CG2  HG21 sing N N 531 
VAL   CG2  HG22 sing N N 532 
VAL   CG2  HG23 sing N N 533 
VAL   OXT  HXT  sing N N 534 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-14 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BTC 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-05-14 
_em_admin.title              
'Cryo-EM density map of HKU1 spike glycoprotein D1 domain in complex with 9O-acetyl GD3 sialoglycan (Up state, locally refined)' 
# 
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 10 mM C4H11NO3 1 Tris 
1 50 mM NaCl     2 NaCl 
# 
_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' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.152531 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          290028 
_em_entity_assembly_naturalsource.organism             'Human coronavirus HKU1' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         36 
_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                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?      ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ?      ? 
MASKING                    ? 3  ? ? ? ?      ? 
'CTF CORRECTION'           ? 4  1 ? ? ?      ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?      ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?      ? 
'MODEL FITTING'            ? 7  ? 1 ? Coot   ? 
OTHER                      ? 8  ? ? ? ?      ? 
'MODEL REFINEMENT'         ? 9  ? 1 ? PHENIX ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?      ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?      ? 
CLASSIFICATION             ? 12 1 ? ? ?      ? 
RECONSTRUCTION             ? 13 1 ? ? ?      ? 
# 
_em_specimen.concentration           1.15 
_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 
# 
_pdbx_audit_support.funding_organization   'Canadian Institutes of Health Research (CIHR)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 BMA 3 n 
2 MAN 4 n 
2 MAN 5 n 
3 NAG 1 n 
3 NAG 2 n 
# 
_atom_sites.entry_id                    9BTC 
_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    . VAL   A 1 1   ? 221.826 183.872 156.659 1.00 94.55  ? 14   VAL   A N    1 
ATOM   2    C CA   . VAL   A 1 1   ? 221.565 185.251 156.168 1.00 92.78  ? 14   VAL   A CA   1 
ATOM   3    C C    . VAL   A 1 1   ? 220.513 185.928 157.034 1.00 96.64  ? 14   VAL   A C    1 
ATOM   4    O O    . VAL   A 1 1   ? 219.715 185.235 157.655 1.00 95.49  ? 14   VAL   A O    1 
ATOM   5    C CB   . VAL   A 1 1   ? 221.119 185.279 154.698 1.00 97.85  ? 14   VAL   A CB   1 
ATOM   6    C CG1  . VAL   A 1 1   ? 222.249 184.810 153.782 1.00 96.98  ? 14   VAL   A CG1  1 
ATOM   7    C CG2  . VAL   A 1 1   ? 219.862 184.458 154.392 1.00 95.43  ? 14   VAL   A CG2  1 
ATOM   8    N N    . ILE   A 1 2   ? 220.503 187.259 157.106 1.00 95.36  ? 15   ILE   A N    1 
ATOM   9    C CA   . ILE   A 1 2   ? 219.493 187.998 157.875 1.00 90.52  ? 15   ILE   A CA   1 
ATOM   10   C C    . ILE   A 1 2   ? 218.251 188.221 157.016 1.00 92.44  ? 15   ILE   A C    1 
ATOM   11   O O    . ILE   A 1 2   ? 217.321 187.423 157.086 1.00 93.37  ? 15   ILE   A O    1 
ATOM   12   C CB   . ILE   A 1 2   ? 220.079 189.277 158.501 1.00 87.59  ? 15   ILE   A CB   1 
ATOM   13   C CG1  . ILE   A 1 2   ? 221.330 188.962 159.342 1.00 89.50  ? 15   ILE   A CG1  1 
ATOM   14   C CG2  . ILE   A 1 2   ? 219.046 190.029 159.346 1.00 89.45  ? 15   ILE   A CG2  1 
ATOM   15   C CD1  . ILE   A 1 2   ? 221.133 187.982 160.499 1.00 89.81  ? 15   ILE   A CD1  1 
ATOM   16   N N    . GLY   A 1 3   ? 218.249 189.241 156.162 1.00 98.26  ? 16   GLY   A N    1 
ATOM   17   C CA   . GLY   A 1 3   ? 217.266 189.379 155.092 1.00 99.01  ? 16   GLY   A CA   1 
ATOM   18   C C    . GLY   A 1 3   ? 217.647 188.545 153.872 1.00 104.40 ? 16   GLY   A C    1 
ATOM   19   O O    . GLY   A 1 3   ? 218.483 187.648 153.952 1.00 108.17 ? 16   GLY   A O    1 
ATOM   20   N N    . ASP   A 1 4   ? 217.055 188.847 152.721 1.00 111.16 ? 17   ASP   A N    1 
ATOM   21   C CA   . ASP   A 1 4   ? 217.299 188.117 151.472 1.00 110.42 ? 17   ASP   A CA   1 
ATOM   22   C C    . ASP   A 1 4   ? 217.840 188.993 150.325 1.00 109.25 ? 17   ASP   A C    1 
ATOM   23   O O    . ASP   A 1 4   ? 218.110 188.478 149.240 1.00 112.32 ? 17   ASP   A O    1 
ATOM   24   C CB   . ASP   A 1 4   ? 216.026 187.359 151.063 1.00 108.51 ? 17   ASP   A CB   1 
ATOM   25   C CG   . ASP   A 1 4   ? 214.856 188.247 150.627 1.00 114.53 ? 17   ASP   A CG   1 
ATOM   26   O OD1  . ASP   A 1 4   ? 214.949 189.489 150.732 1.00 116.52 ? 17   ASP   A OD1  1 
ATOM   27   O OD2  . ASP   A 1 4   ? 213.850 187.684 150.141 1.00 116.49 ? 17   ASP   A OD2  1 
ATOM   28   N N    . PHE   A 1 5   ? 218.004 190.303 150.532 1.00 106.64 ? 18   PHE   A N    1 
ATOM   29   C CA   . PHE   A 1 5   ? 218.439 191.218 149.481 1.00 111.27 ? 18   PHE   A CA   1 
ATOM   30   C C    . PHE   A 1 5   ? 219.953 191.159 149.260 1.00 116.00 ? 18   PHE   A C    1 
ATOM   31   O O    . PHE   A 1 5   ? 220.726 191.384 150.193 1.00 118.33 ? 18   PHE   A O    1 
ATOM   32   C CB   . PHE   A 1 5   ? 217.969 192.634 149.801 1.00 111.03 ? 18   PHE   A CB   1 
ATOM   33   C CG   . PHE   A 1 5   ? 217.992 193.525 148.583 1.00 113.65 ? 18   PHE   A CG   1 
ATOM   34   C CD1  . PHE   A 1 5   ? 219.192 194.118 148.159 1.00 113.66 ? 18   PHE   A CD1  1 
ATOM   35   C CD2  . PHE   A 1 5   ? 216.815 193.718 147.840 1.00 113.47 ? 18   PHE   A CD2  1 
ATOM   36   C CE1  . PHE   A 1 5   ? 219.219 194.889 146.990 1.00 112.52 ? 18   PHE   A CE1  1 
ATOM   37   C CE2  . PHE   A 1 5   ? 216.837 194.501 146.677 1.00 113.14 ? 18   PHE   A CE2  1 
ATOM   38   C CZ   . PHE   A 1 5   ? 218.042 195.076 146.244 1.00 111.31 ? 18   PHE   A CZ   1 
ATOM   39   N N    . ASN   A 1 6   ? 220.400 190.900 148.030 1.00 121.78 ? 19   ASN   A N    1 
ATOM   40   C CA   . ASN   A 1 6   ? 221.817 190.925 147.664 1.00 121.60 ? 19   ASN   A CA   1 
ATOM   41   C C    . ASN   A 1 6   ? 222.341 192.370 147.576 1.00 124.28 ? 19   ASN   A C    1 
ATOM   42   O O    . ASN   A 1 6   ? 222.403 192.964 146.502 1.00 126.27 ? 19   ASN   A O    1 
ATOM   43   C CB   . ASN   A 1 6   ? 222.025 190.135 146.361 1.00 122.38 ? 19   ASN   A CB   1 
ATOM   44   C CG   . ASN   A 1 6   ? 223.480 190.084 145.908 1.00 126.10 ? 19   ASN   A CG   1 
ATOM   45   O OD1  . ASN   A 1 6   ? 224.388 190.525 146.606 1.00 127.10 ? 19   ASN   A OD1  1 
ATOM   46   N ND2  . ASN   A 1 6   ? 223.692 189.567 144.705 1.00 127.36 ? 19   ASN   A ND2  1 
ATOM   47   N N    . CYS   A 1 7   ? 222.668 192.963 148.722 1.00 128.04 ? 20   CYS   A N    1 
ATOM   48   C CA   . CYS   A 1 7   ? 223.274 194.290 148.805 1.00 128.15 ? 20   CYS   A CA   1 
ATOM   49   C C    . CYS   A 1 7   ? 224.733 194.305 148.333 1.00 129.31 ? 20   CYS   A C    1 
ATOM   50   O O    . CYS   A 1 7   ? 225.216 195.340 147.875 1.00 129.48 ? 20   CYS   A O    1 
ATOM   51   C CB   . CYS   A 1 7   ? 223.219 194.769 150.257 1.00 131.50 ? 20   CYS   A CB   1 
ATOM   52   S SG   . CYS   A 1 7   ? 221.550 195.059 150.883 1.00 147.22 ? 20   CYS   A SG   1 
ATOM   53   N N    . THR   A 1 8   ? 225.461 193.197 148.482 1.00 128.89 ? 21   THR   A N    1 
ATOM   54   C CA   . THR   A 1 8   ? 226.883 193.117 148.133 1.00 130.07 ? 21   THR   A CA   1 
ATOM   55   C C    . THR   A 1 8   ? 227.379 191.679 147.978 1.00 128.57 ? 21   THR   A C    1 
ATOM   56   O O    . THR   A 1 8   ? 226.859 190.761 148.608 1.00 126.52 ? 21   THR   A O    1 
ATOM   57   C CB   . THR   A 1 8   ? 227.712 193.838 149.209 1.00 129.23 ? 21   THR   A CB   1 
ATOM   58   O OG1  . THR   A 1 8   ? 229.042 193.982 148.776 1.00 129.37 ? 21   THR   A OG1  1 
ATOM   59   C CG2  . THR   A 1 8   ? 227.755 193.108 150.549 1.00 126.51 ? 21   THR   A CG2  1 
ATOM   60   N N    . ASN   A 1 9   ? 228.470 191.501 147.232 1.00 133.85 ? 22   ASN   A N    1 
ATOM   61   C CA   . ASN   A 1 9   ? 229.327 190.315 147.281 1.00 133.49 ? 22   ASN   A CA   1 
ATOM   62   C C    . ASN   A 1 9   ? 230.809 190.663 147.545 1.00 133.98 ? 22   ASN   A C    1 
ATOM   63   O O    . ASN   A 1 9   ? 231.686 189.822 147.356 1.00 133.01 ? 22   ASN   A O    1 
ATOM   64   C CB   . ASN   A 1 9   ? 229.123 189.464 146.014 1.00 131.57 ? 22   ASN   A CB   1 
ATOM   65   C CG   . ASN   A 1 9   ? 229.743 190.071 144.771 1.00 135.26 ? 22   ASN   A CG   1 
ATOM   66   O OD1  . ASN   A 1 9   ? 229.862 191.278 144.626 1.00 134.33 ? 22   ASN   A OD1  1 
ATOM   67   N ND2  . ASN   A 1 9   ? 230.159 189.257 143.834 1.00 133.78 ? 22   ASN   A ND2  1 
ATOM   68   N N    . PHE   A 1 10  ? 231.110 191.894 147.972 1.00 126.35 ? 23   PHE   A N    1 
ATOM   69   C CA   . PHE   A 1 10  ? 232.475 192.335 148.273 1.00 124.41 ? 23   PHE   A CA   1 
ATOM   70   C C    . PHE   A 1 10  ? 233.008 191.701 149.564 1.00 126.86 ? 23   PHE   A C    1 
ATOM   71   O O    . PHE   A 1 10  ? 232.419 191.861 150.634 1.00 128.43 ? 23   PHE   A O    1 
ATOM   72   C CB   . PHE   A 1 10  ? 232.505 193.866 148.354 1.00 123.24 ? 23   PHE   A CB   1 
ATOM   73   C CG   . PHE   A 1 10  ? 233.836 194.441 148.788 1.00 127.57 ? 23   PHE   A CG   1 
ATOM   74   C CD1  . PHE   A 1 10  ? 234.999 194.156 148.051 1.00 127.85 ? 23   PHE   A CD1  1 
ATOM   75   C CD2  . PHE   A 1 10  ? 233.916 195.252 149.935 1.00 127.11 ? 23   PHE   A CD2  1 
ATOM   76   C CE1  . PHE   A 1 10  ? 236.237 194.673 148.462 1.00 127.55 ? 23   PHE   A CE1  1 
ATOM   77   C CE2  . PHE   A 1 10  ? 235.156 195.768 150.344 1.00 127.13 ? 23   PHE   A CE2  1 
ATOM   78   C CZ   . PHE   A 1 10  ? 236.314 195.479 149.609 1.00 126.58 ? 23   PHE   A CZ   1 
ATOM   79   N N    . ALA   A 1 11  ? 234.150 191.018 149.474 1.00 120.42 ? 24   ALA   A N    1 
ATOM   80   C CA   . ALA   A 1 11  ? 234.895 190.455 150.601 1.00 120.54 ? 24   ALA   A CA   1 
ATOM   81   C C    . ALA   A 1 11  ? 234.032 189.619 151.571 1.00 120.77 ? 24   ALA   A C    1 
ATOM   82   O O    . ALA   A 1 11  ? 234.049 189.824 152.782 1.00 123.39 ? 24   ALA   A O    1 
ATOM   83   C CB   . ALA   A 1 11  ? 235.734 191.562 151.257 1.00 120.43 ? 24   ALA   A CB   1 
ATOM   84   N N    . ILE   A 1 12  ? 233.273 188.659 151.044 1.00 115.70 ? 25   ILE   A N    1 
ATOM   85   C CA   . ILE   A 1 12  ? 232.524 187.680 151.845 1.00 117.73 ? 25   ILE   A CA   1 
ATOM   86   C C    . ILE   A 1 12  ? 233.292 186.354 151.867 1.00 117.64 ? 25   ILE   A C    1 
ATOM   87   O O    . ILE   A 1 12  ? 233.720 185.877 150.815 1.00 119.79 ? 25   ILE   A O    1 
ATOM   88   C CB   . ILE   A 1 12  ? 231.100 187.475 151.291 1.00 115.50 ? 25   ILE   A CB   1 
ATOM   89   C CG1  . ILE   A 1 12  ? 230.310 188.777 151.053 1.00 115.04 ? 25   ILE   A CG1  1 
ATOM   90   C CG2  . ILE   A 1 12  ? 230.312 186.535 152.213 1.00 113.21 ? 25   ILE   A CG2  1 
ATOM   91   C CD1  . ILE   A 1 12  ? 230.083 189.639 152.294 1.00 116.11 ? 25   ILE   A CD1  1 
ATOM   92   N N    . ASN   A 1 13  ? 233.451 185.733 153.033 1.00 116.56 ? 26   ASN   A N    1 
ATOM   93   C CA   . ASN   A 1 13  ? 234.066 184.407 153.174 1.00 114.10 ? 26   ASN   A CA   1 
ATOM   94   C C    . ASN   A 1 13  ? 233.295 183.519 154.163 1.00 113.66 ? 26   ASN   A C    1 
ATOM   95   O O    . ASN   A 1 13  ? 232.254 183.919 154.668 1.00 117.24 ? 26   ASN   A O    1 
ATOM   96   C CB   . ASN   A 1 13  ? 235.563 184.571 153.493 1.00 116.91 ? 26   ASN   A CB   1 
ATOM   97   C CG   . ASN   A 1 13  ? 235.883 185.060 154.894 1.00 118.76 ? 26   ASN   A CG   1 
ATOM   98   O OD1  . ASN   A 1 13  ? 235.265 184.684 155.875 1.00 118.04 ? 26   ASN   A OD1  1 
ATOM   99   N ND2  . ASN   A 1 13  ? 236.916 185.853 155.039 1.00 116.26 ? 26   ASN   A ND2  1 
ATOM   100  N N    . ASP   A 1 14  ? 233.776 182.304 154.434 1.00 116.18 ? 27   ASP   A N    1 
ATOM   101  C CA   . ASP   A 1 14  ? 233.110 181.338 155.323 1.00 118.30 ? 27   ASP   A CA   1 
ATOM   102  C C    . ASP   A 1 14  ? 233.919 181.010 156.591 1.00 120.05 ? 27   ASP   A C    1 
ATOM   103  O O    . ASP   A 1 14  ? 233.715 179.963 157.205 1.00 119.63 ? 27   ASP   A O    1 
ATOM   104  C CB   . ASP   A 1 14  ? 232.757 180.065 154.535 1.00 119.32 ? 27   ASP   A CB   1 
ATOM   105  C CG   . ASP   A 1 14  ? 231.874 180.309 153.310 1.00 122.93 ? 27   ASP   A CG   1 
ATOM   106  O OD1  . ASP   A 1 14  ? 230.956 181.156 153.378 1.00 125.88 ? 27   ASP   A OD1  1 
ATOM   107  O OD2  . ASP   A 1 14  ? 232.075 179.605 152.295 1.00 122.11 ? 27   ASP   A OD2  1 
ATOM   108  N N    . LEU   A 1 15  ? 234.877 181.852 156.989 1.00 119.49 ? 28   LEU   A N    1 
ATOM   109  C CA   . LEU   A 1 15  ? 235.790 181.539 158.095 1.00 121.03 ? 28   LEU   A CA   1 
ATOM   110  C C    . LEU   A 1 15  ? 235.076 181.535 159.453 1.00 123.48 ? 28   LEU   A C    1 
ATOM   111  O O    . LEU   A 1 15  ? 234.333 182.461 159.783 1.00 127.69 ? 28   LEU   A O    1 
ATOM   112  C CB   . LEU   A 1 15  ? 236.976 182.518 158.096 1.00 121.08 ? 28   LEU   A CB   1 
ATOM   113  C CG   . LEU   A 1 15  ? 238.156 182.076 157.216 1.00 123.45 ? 28   LEU   A CG   1 
ATOM   114  C CD1  . LEU   A 1 15  ? 237.795 181.832 155.752 1.00 119.56 ? 28   LEU   A CD1  1 
ATOM   115  C CD2  . LEU   A 1 15  ? 239.243 183.147 157.267 1.00 120.93 ? 28   LEU   A CD2  1 
ATOM   116  N N    . ASN   A 1 16  ? 235.349 180.520 160.273 1.00 120.81 ? 29   ASN   A N    1 
ATOM   117  C CA   . ASN   A 1 16  ? 234.869 180.421 161.648 1.00 121.49 ? 29   ASN   A CA   1 
ATOM   118  C C    . ASN   A 1 16  ? 235.782 181.207 162.604 1.00 123.39 ? 29   ASN   A C    1 
ATOM   119  O O    . ASN   A 1 16  ? 236.634 180.634 163.285 1.00 124.09 ? 29   ASN   A O    1 
ATOM   120  C CB   . ASN   A 1 16  ? 234.768 178.935 162.031 1.00 119.85 ? 29   ASN   A CB   1 
ATOM   121  C CG   . ASN   A 1 16  ? 234.190 178.746 163.424 1.00 122.27 ? 29   ASN   A CG   1 
ATOM   122  O OD1  . ASN   A 1 16  ? 233.608 179.673 163.975 1.00 124.04 ? 29   ASN   A OD1  1 
ATOM   123  N ND2  . ASN   A 1 16  ? 234.296 177.553 163.986 1.00 121.75 ? 29   ASN   A ND2  1 
ATOM   124  N N    . THR   A 1 17  ? 235.724 182.538 162.550 1.00 124.25 ? 30   THR   A N    1 
ATOM   125  C CA   . THR   A 1 17  ? 236.686 183.398 163.258 1.00 126.59 ? 30   THR   A CA   1 
ATOM   126  C C    . THR   A 1 17  ? 236.468 183.470 164.772 1.00 127.04 ? 30   THR   A C    1 
ATOM   127  O O    . THR   A 1 17  ? 237.410 183.761 165.504 1.00 125.49 ? 30   THR   A O    1 
ATOM   128  C CB   . THR   A 1 17  ? 236.671 184.825 162.701 1.00 126.18 ? 30   THR   A CB   1 
ATOM   129  O OG1  . THR   A 1 17  ? 235.458 185.476 162.994 1.00 128.45 ? 30   THR   A OG1  1 
ATOM   130  C CG2  . THR   A 1 17  ? 236.864 184.901 161.190 1.00 125.65 ? 30   THR   A CG2  1 
ATOM   131  N N    . THR   A 1 18  ? 235.244 183.257 165.258 1.00 122.13 ? 31   THR   A N    1 
ATOM   132  C CA   . THR   A 1 18  ? 234.872 183.425 166.674 1.00 123.21 ? 31   THR   A CA   1 
ATOM   133  C C    . THR   A 1 18  ? 233.551 182.724 167.001 1.00 122.53 ? 31   THR   A C    1 
ATOM   134  O O    . THR   A 1 18  ? 232.749 182.457 166.111 1.00 123.55 ? 31   THR   A O    1 
ATOM   135  C CB   . THR   A 1 18  ? 234.789 184.930 167.015 1.00 123.59 ? 31   THR   A CB   1 
ATOM   136  O OG1  . THR   A 1 18  ? 234.742 185.149 168.409 1.00 122.59 ? 31   THR   A OG1  1 
ATOM   137  C CG2  . THR   A 1 18  ? 233.585 185.659 166.413 1.00 118.38 ? 31   THR   A CG2  1 
ATOM   138  N N    . VAL   A 1 19  ? 233.274 182.516 168.287 1.00 111.99 ? 32   VAL   A N    1 
ATOM   139  C CA   . VAL   A 1 19  ? 231.926 182.248 168.833 1.00 111.30 ? 32   VAL   A CA   1 
ATOM   140  C C    . VAL   A 1 19  ? 231.631 183.242 169.964 1.00 111.55 ? 32   VAL   A C    1 
ATOM   141  O O    . VAL   A 1 19  ? 232.583 183.792 170.521 1.00 109.85 ? 32   VAL   A O    1 
ATOM   142  C CB   . VAL   A 1 19  ? 231.764 180.798 169.315 1.00 107.84 ? 32   VAL   A CB   1 
ATOM   143  C CG1  . VAL   A 1 19  ? 231.838 179.825 168.143 1.00 106.35 ? 32   VAL   A CG1  1 
ATOM   144  C CG2  . VAL   A 1 19  ? 232.788 180.386 170.374 1.00 108.16 ? 32   VAL   A CG2  1 
ATOM   145  N N    . PRO   A 1 20  ? 230.362 183.539 170.299 1.00 106.34 ? 33   PRO   A N    1 
ATOM   146  C CA   . PRO   A 1 20  ? 230.018 184.476 171.360 1.00 104.64 ? 33   PRO   A CA   1 
ATOM   147  C C    . PRO   A 1 20  ? 230.722 184.171 172.682 1.00 105.05 ? 33   PRO   A C    1 
ATOM   148  O O    . PRO   A 1 20  ? 230.635 183.056 173.193 1.00 102.10 ? 33   PRO   A O    1 
ATOM   149  C CB   . PRO   A 1 20  ? 228.504 184.378 171.520 1.00 103.11 ? 33   PRO   A CB   1 
ATOM   150  C CG   . PRO   A 1 20  ? 228.048 183.996 170.121 1.00 101.92 ? 33   PRO   A CG   1 
ATOM   151  C CD   . PRO   A 1 20  ? 229.155 183.060 169.657 1.00 102.91 ? 33   PRO   A CD   1 
ATOM   152  N N    . ARG   A 1 21  ? 231.407 185.161 173.256 1.00 105.72 ? 34   ARG   A N    1 
ATOM   153  C CA   . ARG   A 1 21  ? 232.047 185.050 174.577 1.00 102.31 ? 34   ARG   A CA   1 
ATOM   154  C C    . ARG   A 1 21  ? 230.986 185.001 175.669 1.00 101.15 ? 34   ARG   A C    1 
ATOM   155  O O    . ARG   A 1 21  ? 229.968 185.674 175.547 1.00 107.45 ? 34   ARG   A O    1 
ATOM   156  C CB   . ARG   A 1 21  ? 232.994 186.235 174.808 1.00 100.58 ? 34   ARG   A CB   1 
ATOM   157  C CG   . ARG   A 1 21  ? 234.226 186.189 173.894 1.00 104.23 ? 34   ARG   A CG   1 
ATOM   158  C CD   . ARG   A 1 21  ? 234.915 187.558 173.803 1.00 105.97 ? 34   ARG   A CD   1 
ATOM   159  N NE   . ARG   A 1 21  ? 234.188 188.481 172.903 1.00 114.10 ? 34   ARG   A NE   1 
ATOM   160  C CZ   . ARG   A 1 21  ? 234.278 188.549 171.587 1.00 113.79 ? 34   ARG   A CZ   1 
ATOM   161  N NH1  . ARG   A 1 21  ? 233.547 189.407 170.945 1.00 107.42 ? 34   ARG   A NH1  1 
ATOM   162  N NH2  . ARG   A 1 21  ? 235.071 187.784 170.898 1.00 113.49 ? 34   ARG   A NH2  1 
ATOM   163  N N    . ILE   A 1 22  ? 231.234 184.262 176.747 1.00 93.22  ? 35   ILE   A N    1 
ATOM   164  C CA   . ILE   A 1 22  ? 230.369 184.235 177.933 1.00 90.11  ? 35   ILE   A CA   1 
ATOM   165  C C    . ILE   A 1 22  ? 230.984 185.126 179.003 1.00 92.39  ? 35   ILE   A C    1 
ATOM   166  O O    . ILE   A 1 22  ? 232.173 185.018 179.294 1.00 98.84  ? 35   ILE   A O    1 
ATOM   167  C CB   . ILE   A 1 22  ? 230.175 182.800 178.451 1.00 90.69  ? 35   ILE   A CB   1 
ATOM   168  C CG1  . ILE   A 1 22  ? 229.627 181.849 177.370 1.00 91.62  ? 35   ILE   A CG1  1 
ATOM   169  C CG2  . ILE   A 1 22  ? 229.265 182.783 179.683 1.00 89.54  ? 35   ILE   A CG2  1 
ATOM   170  C CD1  . ILE   A 1 22  ? 228.289 182.252 176.751 1.00 92.61  ? 35   ILE   A CD1  1 
ATOM   171  N N    . SER   A 1 23  ? 230.200 186.031 179.572 1.00 94.08  ? 36   SER   A N    1 
ATOM   172  C CA   . SER   A 1 23  ? 230.700 187.001 180.540 1.00 94.81  ? 36   SER   A CA   1 
ATOM   173  C C    . SER   A 1 23  ? 231.143 186.334 181.841 1.00 100.64 ? 36   SER   A C    1 
ATOM   174  O O    . SER   A 1 23  ? 230.484 185.430 182.354 1.00 100.00 ? 36   SER   A O    1 
ATOM   175  C CB   . SER   A 1 23  ? 229.641 188.069 180.820 1.00 96.46  ? 36   SER   A CB   1 
ATOM   176  O OG   . SER   A 1 23  ? 228.470 187.514 181.379 1.00 101.58 ? 36   SER   A OG   1 
ATOM   177  N N    . GLU   A 1 24  ? 232.236 186.823 182.421 1.00 112.18 ? 37   GLU   A N    1 
ATOM   178  C CA   . GLU   A 1 24  ? 232.575 186.546 183.821 1.00 111.21 ? 37   GLU   A CA   1 
ATOM   179  C C    . GLU   A 1 24  ? 231.629 187.326 184.753 1.00 112.15 ? 37   GLU   A C    1 
ATOM   180  O O    . GLU   A 1 24  ? 231.208 186.820 185.790 1.00 112.25 ? 37   GLU   A O    1 
ATOM   181  C CB   . GLU   A 1 24  ? 234.053 186.897 184.041 1.00 111.85 ? 37   GLU   A CB   1 
ATOM   182  C CG   . GLU   A 1 24  ? 234.564 186.539 185.445 1.00 113.83 ? 37   GLU   A CG   1 
ATOM   183  C CD   . GLU   A 1 24  ? 236.031 186.942 185.674 1.00 118.99 ? 37   GLU   A CD   1 
ATOM   184  O OE1  . GLU   A 1 24  ? 236.832 186.954 184.713 1.00 116.66 ? 37   GLU   A OE1  1 
ATOM   185  O OE2  . GLU   A 1 24  ? 236.396 187.227 186.833 1.00 117.32 ? 37   GLU   A OE2  1 
ATOM   186  N N    . TYR   A 1 25  ? 231.233 188.534 184.346 1.00 99.46  ? 38   TYR   A N    1 
ATOM   187  C CA   . TYR   A 1 25  ? 230.181 189.334 184.977 1.00 97.93  ? 38   TYR   A CA   1 
ATOM   188  C C    . TYR   A 1 25  ? 228.836 188.607 184.951 1.00 97.64  ? 38   TYR   A C    1 
ATOM   189  O O    . TYR   A 1 25  ? 228.492 187.986 183.946 1.00 99.79  ? 38   TYR   A O    1 
ATOM   190  C CB   . TYR   A 1 25  ? 230.081 190.672 184.235 1.00 96.12  ? 38   TYR   A CB   1 
ATOM   191  C CG   . TYR   A 1 25  ? 229.005 191.604 184.746 1.00 98.90  ? 38   TYR   A CG   1 
ATOM   192  C CD1  . TYR   A 1 25  ? 229.258 192.414 185.864 1.00 99.95  ? 38   TYR   A CD1  1 
ATOM   193  C CD2  . TYR   A 1 25  ? 227.767 191.685 184.085 1.00 99.07  ? 38   TYR   A CD2  1 
ATOM   194  C CE1  . TYR   A 1 25  ? 228.270 193.300 186.325 1.00 101.66 ? 38   TYR   A CE1  1 
ATOM   195  C CE2  . TYR   A 1 25  ? 226.780 192.576 184.538 1.00 100.72 ? 38   TYR   A CE2  1 
ATOM   196  C CZ   . TYR   A 1 25  ? 227.030 193.384 185.664 1.00 103.04 ? 38   TYR   A CZ   1 
ATOM   197  O OH   . TYR   A 1 25  ? 226.089 194.253 186.113 1.00 103.03 ? 38   TYR   A OH   1 
ATOM   198  N N    . VAL   A 1 26  ? 228.041 188.728 186.010 1.00 83.12  ? 39   VAL   A N    1 
ATOM   199  C CA   . VAL   A 1 26  ? 226.690 188.154 186.091 1.00 83.37  ? 39   VAL   A CA   1 
ATOM   200  C C    . VAL   A 1 26  ? 225.683 189.177 186.588 1.00 87.93  ? 39   VAL   A C    1 
ATOM   201  O O    . VAL   A 1 26  ? 226.032 190.120 187.292 1.00 91.49  ? 39   VAL   A O    1 
ATOM   202  C CB   . VAL   A 1 26  ? 226.634 186.889 186.959 1.00 80.84  ? 39   VAL   A CB   1 
ATOM   203  C CG1  . VAL   A 1 26  ? 227.497 185.768 186.387 1.00 83.65  ? 39   VAL   A CG1  1 
ATOM   204  C CG2  . VAL   A 1 26  ? 227.021 187.129 188.419 1.00 83.94  ? 39   VAL   A CG2  1 
ATOM   205  N N    . VAL   A 1 27  ? 224.421 188.979 186.226 1.00 83.16  ? 40   VAL   A N    1 
ATOM   206  C CA   . VAL   A 1 27  ? 223.301 189.849 186.599 1.00 82.22  ? 40   VAL   A CA   1 
ATOM   207  C C    . VAL   A 1 27  ? 223.208 189.984 188.127 1.00 89.87  ? 40   VAL   A C    1 
ATOM   208  O O    . VAL   A 1 27  ? 223.021 188.994 188.821 1.00 92.06  ? 40   VAL   A O    1 
ATOM   209  C CB   . VAL   A 1 27  ? 221.996 189.280 186.022 1.00 76.84  ? 40   VAL   A CB   1 
ATOM   210  C CG1  . VAL   A 1 27  ? 220.767 190.068 186.461 1.00 76.54  ? 40   VAL   A CG1  1 
ATOM   211  C CG2  . VAL   A 1 27  ? 221.998 189.285 184.494 1.00 81.03  ? 40   VAL   A CG2  1 
ATOM   212  N N    . ASP   A 1 28  ? 223.283 191.198 188.663 1.00 95.01  ? 41   ASP   A N    1 
ATOM   213  C CA   . ASP   A 1 28  ? 223.093 191.486 190.087 1.00 92.84  ? 41   ASP   A CA   1 
ATOM   214  C C    . ASP   A 1 28  ? 222.139 192.668 190.230 1.00 94.83  ? 41   ASP   A C    1 
ATOM   215  O O    . ASP   A 1 28  ? 222.514 193.815 189.998 1.00 95.94  ? 41   ASP   A O    1 
ATOM   216  C CB   . ASP   A 1 28  ? 224.438 191.768 190.771 1.00 95.39  ? 41   ASP   A CB   1 
ATOM   217  C CG   . ASP   A 1 28  ? 224.301 192.256 192.226 1.00 100.66 ? 41   ASP   A CG   1 
ATOM   218  O OD1  . ASP   A 1 28  ? 223.182 192.290 192.791 1.00 103.34 ? 41   ASP   A OD1  1 
ATOM   219  O OD2  . ASP   A 1 28  ? 225.340 192.607 192.825 1.00 101.96 ? 41   ASP   A OD2  1 
ATOM   220  N N    . VAL   A 1 29  ? 220.894 192.379 190.597 1.00 79.85  ? 42   VAL   A N    1 
ATOM   221  C CA   . VAL   A 1 29  ? 219.815 193.369 190.629 1.00 79.94  ? 42   VAL   A CA   1 
ATOM   222  C C    . VAL   A 1 29  ? 219.662 194.069 191.970 1.00 81.07  ? 42   VAL   A C    1 
ATOM   223  O O    . VAL   A 1 29  ? 218.789 194.914 192.108 1.00 86.76  ? 42   VAL   A O    1 
ATOM   224  C CB   . VAL   A 1 29  ? 218.494 192.759 190.151 1.00 78.08  ? 42   VAL   A CB   1 
ATOM   225  C CG1  . VAL   A 1 29  ? 218.677 192.138 188.763 1.00 76.32  ? 42   VAL   A CG1  1 
ATOM   226  C CG2  . VAL   A 1 29  ? 217.958 191.701 191.116 1.00 82.71  ? 42   VAL   A CG2  1 
ATOM   227  N N    . SER   A 1 30  ? 220.499 193.774 192.962 1.00 85.62  ? 43   SER   A N    1 
ATOM   228  C CA   . SER   A 1 30  ? 220.324 194.261 194.338 1.00 82.25  ? 43   SER   A CA   1 
ATOM   229  C C    . SER   A 1 30  ? 220.259 195.786 194.477 1.00 83.23  ? 43   SER   A C    1 
ATOM   230  O O    . SER   A 1 30  ? 219.582 196.278 195.377 1.00 85.16  ? 43   SER   A O    1 
ATOM   231  C CB   . SER   A 1 30  ? 221.435 193.692 195.219 1.00 84.61  ? 43   SER   A CB   1 
ATOM   232  O OG   . SER   A 1 30  ? 222.707 194.027 194.714 1.00 95.31  ? 43   SER   A OG   1 
ATOM   233  N N    . TYR   A 1 31  ? 220.857 196.542 193.548 1.00 79.99  ? 44   TYR   A N    1 
ATOM   234  C CA   . TYR   A 1 31  ? 220.797 198.009 193.471 1.00 81.88  ? 44   TYR   A CA   1 
ATOM   235  C C    . TYR   A 1 31  ? 220.036 198.532 192.241 1.00 87.52  ? 44   TYR   A C    1 
ATOM   236  O O    . TYR   A 1 31  ? 220.238 199.658 191.796 1.00 90.80  ? 44   TYR   A O    1 
ATOM   237  C CB   . TYR   A 1 31  ? 222.210 198.587 193.580 1.00 85.01  ? 44   TYR   A CB   1 
ATOM   238  C CG   . TYR   A 1 31  ? 222.890 198.211 194.877 1.00 88.03  ? 44   TYR   A CG   1 
ATOM   239  C CD1  . TYR   A 1 31  ? 222.557 198.902 196.055 1.00 86.26  ? 44   TYR   A CD1  1 
ATOM   240  C CD2  . TYR   A 1 31  ? 223.811 197.155 194.917 1.00 87.60  ? 44   TYR   A CD2  1 
ATOM   241  C CE1  . TYR   A 1 31  ? 223.149 198.538 197.276 1.00 89.18  ? 44   TYR   A CE1  1 
ATOM   242  C CE2  . TYR   A 1 31  ? 224.402 196.785 196.137 1.00 91.79  ? 44   TYR   A CE2  1 
ATOM   243  C CZ   . TYR   A 1 31  ? 224.074 197.473 197.318 1.00 95.96  ? 44   TYR   A CZ   1 
ATOM   244  O OH   . TYR   A 1 31  ? 224.651 197.113 198.493 1.00 94.64  ? 44   TYR   A OH   1 
ATOM   245  N N    . GLY   A 1 32  ? 219.154 197.720 191.664 1.00 84.48  ? 45   GLY   A N    1 
ATOM   246  C CA   . GLY   A 1 32  ? 218.230 198.130 190.606 1.00 83.20  ? 45   GLY   A CA   1 
ATOM   247  C C    . GLY   A 1 32  ? 218.761 197.987 189.179 1.00 79.22  ? 45   GLY   A C    1 
ATOM   248  O O    . GLY   A 1 32  ? 217.965 198.011 188.245 1.00 80.88  ? 45   GLY   A O    1 
ATOM   249  N N    . LEU   A 1 33  ? 220.059 197.787 188.967 1.00 81.21  ? 46   LEU   A N    1 
ATOM   250  C CA   . LEU   A 1 33  ? 220.626 197.512 187.643 1.00 80.88  ? 46   LEU   A CA   1 
ATOM   251  C C    . LEU   A 1 33  ? 220.063 196.189 187.105 1.00 82.56  ? 46   LEU   A C    1 
ATOM   252  O O    . LEU   A 1 33  ? 220.111 195.183 187.791 1.00 89.99  ? 46   LEU   A O    1 
ATOM   253  C CB   . LEU   A 1 33  ? 222.157 197.525 187.779 1.00 82.77  ? 46   LEU   A CB   1 
ATOM   254  C CG   . LEU   A 1 33  ? 222.951 197.464 186.463 1.00 81.13  ? 46   LEU   A CG   1 
ATOM   255  C CD1  . LEU   A 1 33  ? 224.374 197.944 186.732 1.00 83.29  ? 46   LEU   A CD1  1 
ATOM   256  C CD2  . LEU   A 1 33  ? 223.067 196.057 185.887 1.00 82.84  ? 46   LEU   A CD2  1 
ATOM   257  N N    . GLY   A 1 34  ? 219.485 196.176 185.908 1.00 77.08  ? 47   GLY   A N    1 
ATOM   258  C CA   . GLY   A 1 34  ? 218.727 195.023 185.397 1.00 69.82  ? 47   GLY   A CA   1 
ATOM   259  C C    . GLY   A 1 34  ? 217.220 195.113 185.641 1.00 69.68  ? 47   GLY   A C    1 
ATOM   260  O O    . GLY   A 1 34  ? 216.470 194.315 185.088 1.00 76.60  ? 47   GLY   A O    1 
ATOM   261  N N    . THR   A 1 35  ? 216.741 196.103 186.391 1.00 68.13  ? 48   THR   A N    1 
ATOM   262  C CA   . THR   A 1 35  ? 215.319 196.481 186.461 1.00 64.81  ? 48   THR   A CA   1 
ATOM   263  C C    . THR   A 1 35  ? 215.014 197.688 185.575 1.00 72.63  ? 48   THR   A C    1 
ATOM   264  O O    . THR   A 1 35  ? 215.919 198.282 184.995 1.00 77.57  ? 48   THR   A O    1 
ATOM   265  C CB   . THR   A 1 35  ? 214.860 196.756 187.895 1.00 69.65  ? 48   THR   A CB   1 
ATOM   266  O OG1  . THR   A 1 35  ? 215.329 197.983 188.381 1.00 81.72  ? 48   THR   A OG1  1 
ATOM   267  C CG2  . THR   A 1 35  ? 215.308 195.668 188.849 1.00 70.69  ? 48   THR   A CG2  1 
ATOM   268  N N    . TYR   A 1 36  ? 213.746 198.074 185.479 1.00 65.99  ? 49   TYR   A N    1 
ATOM   269  C CA   . TYR   A 1 36  ? 213.281 199.237 184.735 1.00 60.49  ? 49   TYR   A CA   1 
ATOM   270  C C    . TYR   A 1 36  ? 212.247 200.031 185.529 1.00 65.65  ? 49   TYR   A C    1 
ATOM   271  O O    . TYR   A 1 36  ? 211.456 199.449 186.266 1.00 73.86  ? 49   TYR   A O    1 
ATOM   272  C CB   . TYR   A 1 36  ? 212.693 198.781 183.398 1.00 58.18  ? 49   TYR   A CB   1 
ATOM   273  C CG   . TYR   A 1 36  ? 211.660 197.683 183.389 1.00 56.25  ? 49   TYR   A CG   1 
ATOM   274  C CD1  . TYR   A 1 36  ? 212.084 196.355 183.237 1.00 62.95  ? 49   TYR   A CD1  1 
ATOM   275  C CD2  . TYR   A 1 36  ? 210.291 197.985 183.394 1.00 61.15  ? 49   TYR   A CD2  1 
ATOM   276  C CE1  . TYR   A 1 36  ? 211.147 195.329 183.053 1.00 68.91  ? 49   TYR   A CE1  1 
ATOM   277  C CE2  . TYR   A 1 36  ? 209.347 196.958 183.193 1.00 60.15  ? 49   TYR   A CE2  1 
ATOM   278  C CZ   . TYR   A 1 36  ? 209.778 195.631 183.004 1.00 68.17  ? 49   TYR   A CZ   1 
ATOM   279  O OH   . TYR   A 1 36  ? 208.878 194.653 182.718 1.00 71.90  ? 49   TYR   A OH   1 
ATOM   280  N N    . TYR   A 1 37  ? 212.207 201.349 185.358 1.00 65.51  ? 50   TYR   A N    1 
ATOM   281  C CA   . TYR   A 1 37  ? 211.078 202.149 185.834 1.00 61.00  ? 50   TYR   A CA   1 
ATOM   282  C C    . TYR   A 1 37  ? 209.815 201.789 185.040 1.00 72.30  ? 50   TYR   A C    1 
ATOM   283  O O    . TYR   A 1 37  ? 209.876 201.631 183.822 1.00 80.15  ? 50   TYR   A O    1 
ATOM   284  C CB   . TYR   A 1 37  ? 211.390 203.637 185.706 1.00 64.05  ? 50   TYR   A CB   1 
ATOM   285  C CG   . TYR   A 1 37  ? 212.482 204.110 186.631 1.00 66.16  ? 50   TYR   A CG   1 
ATOM   286  C CD1  . TYR   A 1 37  ? 212.156 204.469 187.946 1.00 69.28  ? 50   TYR   A CD1  1 
ATOM   287  C CD2  . TYR   A 1 37  ? 213.809 204.197 186.187 1.00 70.36  ? 50   TYR   A CD2  1 
ATOM   288  C CE1  . TYR   A 1 37  ? 213.158 204.906 188.822 1.00 69.07  ? 50   TYR   A CE1  1 
ATOM   289  C CE2  . TYR   A 1 37  ? 214.814 204.649 187.060 1.00 70.14  ? 50   TYR   A CE2  1 
ATOM   290  C CZ   . TYR   A 1 37  ? 214.484 204.993 188.380 1.00 72.01  ? 50   TYR   A CZ   1 
ATOM   291  O OH   . TYR   A 1 37  ? 215.445 205.407 189.239 1.00 72.84  ? 50   TYR   A OH   1 
ATOM   292  N N    . ILE   A 1 38  ? 208.669 201.625 185.702 1.00 65.21  ? 51   ILE   A N    1 
ATOM   293  C CA   . ILE   A 1 38  ? 207.460 201.110 185.050 1.00 65.24  ? 51   ILE   A CA   1 
ATOM   294  C C    . ILE   A 1 38  ? 206.808 202.196 184.187 1.00 74.51  ? 51   ILE   A C    1 
ATOM   295  O O    . ILE   A 1 38  ? 206.117 203.073 184.699 1.00 81.46  ? 51   ILE   A O    1 
ATOM   296  C CB   . ILE   A 1 38  ? 206.456 200.530 186.059 1.00 64.77  ? 51   ILE   A CB   1 
ATOM   297  C CG1  . ILE   A 1 38  ? 207.066 199.395 186.897 1.00 66.57  ? 51   ILE   A CG1  1 
ATOM   298  C CG2  . ILE   A 1 38  ? 205.258 199.937 185.300 1.00 74.75  ? 51   ILE   A CG2  1 
ATOM   299  C CD1  . ILE   A 1 38  ? 207.719 199.879 188.186 1.00 72.89  ? 51   ILE   A CD1  1 
ATOM   300  N N    . LEU   A 1 39  ? 206.972 202.105 182.866 1.00 79.94  ? 52   LEU   A N    1 
ATOM   301  C CA   . LEU   A 1 39  ? 206.338 202.999 181.893 1.00 73.70  ? 52   LEU   A CA   1 
ATOM   302  C C    . LEU   A 1 39  ? 206.580 204.480 182.252 1.00 79.37  ? 52   LEU   A C    1 
ATOM   303  O O    . LEU   A 1 39  ? 207.701 204.858 182.583 1.00 85.70  ? 52   LEU   A O    1 
ATOM   304  C CB   . LEU   A 1 39  ? 204.852 202.614 181.715 1.00 76.35  ? 52   LEU   A CB   1 
ATOM   305  C CG   . LEU   A 1 39  ? 204.594 201.140 181.375 1.00 81.14  ? 52   LEU   A CG   1 
ATOM   306  C CD1  . LEU   A 1 39  ? 203.095 200.869 181.342 1.00 77.97  ? 52   LEU   A CD1  1 
ATOM   307  C CD2  . LEU   A 1 39  ? 205.178 200.766 180.019 1.00 79.76  ? 52   LEU   A CD2  1 
ATOM   308  N N    . ASP   A 1 40  ? 205.557 205.330 182.192 1.00 80.80  ? 53   ASP   A N    1 
ATOM   309  C CA   . ASP   A 1 40  ? 205.590 206.733 182.616 1.00 79.10  ? 53   ASP   A CA   1 
ATOM   310  C C    . ASP   A 1 40  ? 205.188 206.952 184.085 1.00 85.38  ? 53   ASP   A C    1 
ATOM   311  O O    . ASP   A 1 40  ? 205.007 208.093 184.509 1.00 92.31  ? 53   ASP   A O    1 
ATOM   312  C CB   . ASP   A 1 40  ? 204.775 207.593 181.633 1.00 84.14  ? 53   ASP   A CB   1 
ATOM   313  C CG   . ASP   A 1 40  ? 203.338 207.130 181.366 1.00 95.41  ? 53   ASP   A CG   1 
ATOM   314  O OD1  . ASP   A 1 40  ? 202.871 206.150 181.983 1.00 95.41  ? 53   ASP   A OD1  1 
ATOM   315  O OD2  . ASP   A 1 40  ? 202.681 207.741 180.496 1.00 96.74  ? 53   ASP   A OD2  1 
ATOM   316  N N    . ARG   A 1 41  ? 205.056 205.891 184.890 1.00 78.40  ? 54   ARG   A N    1 
ATOM   317  C CA   . ARG   A 1 41  ? 204.666 205.994 186.302 1.00 75.95  ? 54   ARG   A CA   1 
ATOM   318  C C    . ARG   A 1 41  ? 205.792 206.529 187.174 1.00 76.11  ? 54   ARG   A C    1 
ATOM   319  O O    . ARG   A 1 41  ? 206.964 206.233 186.956 1.00 80.34  ? 54   ARG   A O    1 
ATOM   320  C CB   . ARG   A 1 41  ? 204.200 204.636 186.841 1.00 69.05  ? 54   ARG   A CB   1 
ATOM   321  C CG   . ARG   A 1 41  ? 202.972 204.082 186.121 1.00 76.93  ? 54   ARG   A CG   1 
ATOM   322  C CD   . ARG   A 1 41  ? 202.745 202.651 186.590 1.00 80.06  ? 54   ARG   A CD   1 
ATOM   323  N NE   . ARG   A 1 41  ? 201.822 201.936 185.702 1.00 82.97  ? 54   ARG   A NE   1 
ATOM   324  C CZ   . ARG   A 1 41  ? 201.455 200.679 185.818 1.00 85.83  ? 54   ARG   A CZ   1 
ATOM   325  N NH1  . ARG   A 1 41  ? 200.700 200.137 184.912 1.00 84.84  ? 54   ARG   A NH1  1 
ATOM   326  N NH2  . ARG   A 1 41  ? 201.821 199.939 186.820 1.00 81.40  ? 54   ARG   A NH2  1 
ATOM   327  N N    . VAL   A 1 42  ? 205.418 207.244 188.225 1.00 67.58  ? 55   VAL   A N    1 
ATOM   328  C CA   . VAL   A 1 42  ? 206.293 207.613 189.337 1.00 65.89  ? 55   VAL   A CA   1 
ATOM   329  C C    . VAL   A 1 42  ? 205.750 206.982 190.611 1.00 71.11  ? 55   VAL   A C    1 
ATOM   330  O O    . VAL   A 1 42  ? 204.608 207.239 190.975 1.00 75.89  ? 55   VAL   A O    1 
ATOM   331  C CB   . VAL   A 1 42  ? 206.387 209.141 189.472 1.00 68.29  ? 55   VAL   A CB   1 
ATOM   332  C CG1  . VAL   A 1 42  ? 207.256 209.559 190.651 1.00 69.23  ? 55   VAL   A CG1  1 
ATOM   333  C CG2  . VAL   A 1 42  ? 206.986 209.774 188.219 1.00 70.70  ? 55   VAL   A CG2  1 
ATOM   334  N N    . TYR   A 1 43  ? 206.544 206.179 191.308 1.00 67.38  ? 56   TYR   A N    1 
ATOM   335  C CA   . TYR   A 1 43  ? 206.223 205.653 192.635 1.00 68.01  ? 56   TYR   A CA   1 
ATOM   336  C C    . TYR   A 1 43  ? 207.123 206.321 193.669 1.00 74.88  ? 56   TYR   A C    1 
ATOM   337  O O    . TYR   A 1 43  ? 208.334 206.336 193.499 1.00 81.37  ? 56   TYR   A O    1 
ATOM   338  C CB   . TYR   A 1 43  ? 206.418 204.137 192.663 1.00 70.10  ? 56   TYR   A CB   1 
ATOM   339  C CG   . TYR   A 1 43  ? 205.448 203.340 191.822 1.00 63.70  ? 56   TYR   A CG   1 
ATOM   340  C CD1  . TYR   A 1 43  ? 204.253 202.879 192.391 1.00 66.77  ? 56   TYR   A CD1  1 
ATOM   341  C CD2  . TYR   A 1 43  ? 205.763 203.011 190.496 1.00 64.91  ? 56   TYR   A CD2  1 
ATOM   342  C CE1  . TYR   A 1 43  ? 203.374 202.081 191.640 1.00 69.31  ? 56   TYR   A CE1  1 
ATOM   343  C CE2  . TYR   A 1 43  ? 204.881 202.224 189.738 1.00 71.95  ? 56   TYR   A CE2  1 
ATOM   344  C CZ   . TYR   A 1 43  ? 203.688 201.752 190.309 1.00 73.08  ? 56   TYR   A CZ   1 
ATOM   345  O OH   . TYR   A 1 43  ? 202.845 200.979 189.580 1.00 78.84  ? 56   TYR   A OH   1 
ATOM   346  N N    . LEU   A 1 44  ? 206.557 206.878 194.735 1.00 70.92  ? 57   LEU   A N    1 
ATOM   347  C CA   . LEU   A 1 44  ? 207.309 207.599 195.760 1.00 71.93  ? 57   LEU   A CA   1 
ATOM   348  C C    . LEU   A 1 44  ? 207.293 206.854 197.089 1.00 78.27  ? 57   LEU   A C    1 
ATOM   349  O O    . LEU   A 1 44  ? 206.248 206.375 197.512 1.00 87.73  ? 57   LEU   A O    1 
ATOM   350  C CB   . LEU   A 1 44  ? 206.740 209.011 195.935 1.00 71.97  ? 57   LEU   A CB   1 
ATOM   351  C CG   . LEU   A 1 44  ? 206.759 209.881 194.672 1.00 71.18  ? 57   LEU   A CG   1 
ATOM   352  C CD1  . LEU   A 1 44  ? 206.173 211.249 194.988 1.00 74.84  ? 57   LEU   A CD1  1 
ATOM   353  C CD2  . LEU   A 1 44  ? 208.173 210.084 194.147 1.00 73.11  ? 57   LEU   A CD2  1 
ATOM   354  N N    . ASN   A 1 45  ? 208.439 206.809 197.761 1.00 84.85  ? 58   ASN   A N    1 
ATOM   355  C CA   . ASN   A 1 45  ? 208.640 206.265 199.106 1.00 85.70  ? 58   ASN   A CA   1 
ATOM   356  C C    . ASN   A 1 45  ? 207.853 204.975 199.394 1.00 85.37  ? 58   ASN   A C    1 
ATOM   357  O O    . ASN   A 1 45  ? 206.919 204.963 200.193 1.00 86.82  ? 58   ASN   A O    1 
ATOM   358  C CB   . ASN   A 1 45  ? 208.347 207.376 200.122 1.00 88.30  ? 58   ASN   A CB   1 
ATOM   359  C CG   . ASN   A 1 45  ? 208.711 206.960 201.533 1.00 95.08  ? 58   ASN   A CG   1 
ATOM   360  O OD1  . ASN   A 1 45  ? 209.656 206.203 201.728 1.00 97.13  ? 58   ASN   A OD1  1 
ATOM   361  N ND2  . ASN   A 1 45  ? 207.994 207.464 202.520 1.00 94.62  ? 58   ASN   A ND2  1 
ATOM   362  N N    . THR   A 1 46  ? 208.141 203.901 198.663 1.00 78.12  ? 59   THR   A N    1 
ATOM   363  C CA   . THR   A 1 46  ? 207.324 202.683 198.700 1.00 78.75  ? 59   THR   A CA   1 
ATOM   364  C C    . THR   A 1 46  ? 208.093 201.454 198.226 1.00 76.40  ? 59   THR   A C    1 
ATOM   365  O O    . THR   A 1 46  ? 209.114 201.576 197.557 1.00 77.53  ? 59   THR   A O    1 
ATOM   366  C CB   . THR   A 1 46  ? 206.042 202.890 197.872 1.00 82.78  ? 59   THR   A CB   1 
ATOM   367  O OG1  . THR   A 1 46  ? 205.128 201.849 198.116 1.00 88.34  ? 59   THR   A OG1  1 
ATOM   368  C CG2  . THR   A 1 46  ? 206.272 202.926 196.365 1.00 76.53  ? 59   THR   A CG2  1 
ATOM   369  N N    . THR   A 1 47  ? 207.608 200.257 198.539 1.00 76.95  ? 60   THR   A N    1 
ATOM   370  C CA   . THR   A 1 47  ? 208.006 199.013 197.875 1.00 74.91  ? 60   THR   A CA   1 
ATOM   371  C C    . THR   A 1 47  ? 206.819 198.406 197.159 1.00 79.38  ? 60   THR   A C    1 
ATOM   372  O O    . THR   A 1 47  ? 205.768 198.231 197.772 1.00 86.21  ? 60   THR   A O    1 
ATOM   373  C CB   . THR   A 1 47  ? 208.540 197.955 198.839 1.00 79.20  ? 60   THR   A CB   1 
ATOM   374  O OG1  . THR   A 1 47  ? 207.636 197.711 199.887 1.00 88.05  ? 60   THR   A OG1  1 
ATOM   375  C CG2  . THR   A 1 47  ? 209.863 198.352 199.453 1.00 81.88  ? 60   THR   A CG2  1 
ATOM   376  N N    . ILE   A 1 48  ? 206.992 197.991 195.911 1.00 70.06  ? 61   ILE   A N    1 
ATOM   377  C CA   . ILE   A 1 48  ? 205.970 197.239 195.180 1.00 70.77  ? 61   ILE   A CA   1 
ATOM   378  C C    . ILE   A 1 48  ? 206.522 195.881 194.764 1.00 73.14  ? 61   ILE   A C    1 
ATOM   379  O O    . ILE   A 1 48  ? 207.686 195.770 194.395 1.00 70.39  ? 61   ILE   A O    1 
ATOM   380  C CB   . ILE   A 1 48  ? 205.408 198.040 193.987 1.00 69.21  ? 61   ILE   A CB   1 
ATOM   381  C CG1  . ILE   A 1 48  ? 206.406 198.139 192.827 1.00 69.14  ? 61   ILE   A CG1  1 
ATOM   382  C CG2  . ILE   A 1 48  ? 204.921 199.421 194.447 1.00 71.69  ? 61   ILE   A CG2  1 
ATOM   383  C CD1  . ILE   A 1 48  ? 205.906 198.934 191.624 1.00 70.23  ? 61   ILE   A CD1  1 
ATOM   384  N N    . LEU   A 1 49  ? 205.695 194.844 194.797 1.00 72.50  ? 62   LEU   A N    1 
ATOM   385  C CA   . LEU   A 1 49  ? 205.930 193.657 193.988 1.00 71.20  ? 62   LEU   A CA   1 
ATOM   386  C C    . LEU   A 1 49  ? 205.369 193.940 192.603 1.00 77.34  ? 62   LEU   A C    1 
ATOM   387  O O    . LEU   A 1 49  ? 204.212 194.325 192.467 1.00 85.17  ? 62   LEU   A O    1 
ATOM   388  C CB   . LEU   A 1 49  ? 205.258 192.430 194.613 1.00 70.63  ? 62   LEU   A CB   1 
ATOM   389  C CG   . LEU   A 1 49  ? 205.977 191.906 195.861 1.00 71.58  ? 62   LEU   A CG   1 
ATOM   390  C CD1  . LEU   A 1 49  ? 205.093 190.899 196.582 1.00 75.45  ? 62   LEU   A CD1  1 
ATOM   391  C CD2  . LEU   A 1 49  ? 207.281 191.199 195.503 1.00 71.19  ? 62   LEU   A CD2  1 
ATOM   392  N N    . PHE   A 1 50  ? 206.174 193.738 191.576 1.00 66.57  ? 63   PHE   A N    1 
ATOM   393  C CA   . PHE   A 1 50  ? 205.800 193.961 190.189 1.00 61.63  ? 63   PHE   A CA   1 
ATOM   394  C C    . PHE   A 1 50  ? 206.205 192.752 189.357 1.00 68.70  ? 63   PHE   A C    1 
ATOM   395  O O    . PHE   A 1 50  ? 207.311 192.241 189.510 1.00 77.13  ? 63   PHE   A O    1 
ATOM   396  C CB   . PHE   A 1 50  ? 206.453 195.257 189.706 1.00 61.11  ? 63   PHE   A CB   1 
ATOM   397  C CG   . PHE   A 1 50  ? 206.219 195.547 188.243 1.00 66.40  ? 63   PHE   A CG   1 
ATOM   398  C CD1  . PHE   A 1 50  ? 205.007 196.104 187.806 1.00 70.56  ? 63   PHE   A CD1  1 
ATOM   399  C CD2  . PHE   A 1 50  ? 207.213 195.236 187.310 1.00 67.47  ? 63   PHE   A CD2  1 
ATOM   400  C CE1  . PHE   A 1 50  ? 204.794 196.334 186.438 1.00 70.42  ? 63   PHE   A CE1  1 
ATOM   401  C CE2  . PHE   A 1 50  ? 207.007 195.480 185.946 1.00 69.69  ? 63   PHE   A CE2  1 
ATOM   402  C CZ   . PHE   A 1 50  ? 205.793 196.021 185.507 1.00 70.47  ? 63   PHE   A CZ   1 
ATOM   403  N N    . THR   A 1 51  ? 205.329 192.280 188.479 1.00 72.44  ? 64   THR   A N    1 
ATOM   404  C CA   . THR   A 1 51  ? 205.628 191.160 187.580 1.00 72.58  ? 64   THR   A CA   1 
ATOM   405  C C    . THR   A 1 51  ? 205.852 191.678 186.173 1.00 73.60  ? 64   THR   A C    1 
ATOM   406  O O    . THR   A 1 51  ? 205.052 192.439 185.631 1.00 80.27  ? 64   THR   A O    1 
ATOM   407  C CB   . THR   A 1 51  ? 204.580 190.050 187.679 1.00 78.99  ? 64   THR   A CB   1 
ATOM   408  O OG1  . THR   A 1 51  ? 204.986 188.959 186.901 1.00 80.34  ? 64   THR   A OG1  1 
ATOM   409  C CG2  . THR   A 1 51  ? 203.187 190.435 187.200 1.00 83.58  ? 64   THR   A CG2  1 
ATOM   410  N N    . GLY   A 1 52  ? 206.989 191.317 185.598 1.00 68.59  ? 65   GLY   A N    1 
ATOM   411  C CA   . GLY   A 1 52  ? 207.531 191.943 184.406 1.00 72.10  ? 65   GLY   A CA   1 
ATOM   412  C C    . GLY   A 1 52  ? 208.552 191.056 183.730 1.00 75.76  ? 65   GLY   A C    1 
ATOM   413  O O    . GLY   A 1 52  ? 208.741 189.909 184.119 1.00 79.75  ? 65   GLY   A O    1 
ATOM   414  N N    . TYR   A 1 53  ? 209.197 191.566 182.691 1.00 69.12  ? 66   TYR   A N    1 
ATOM   415  C CA   . TYR   A 1 53  ? 210.180 190.808 181.937 1.00 62.35  ? 66   TYR   A CA   1 
ATOM   416  C C    . TYR   A 1 53  ? 211.571 191.171 182.410 1.00 68.31  ? 66   TYR   A C    1 
ATOM   417  O O    . TYR   A 1 53  ? 212.140 192.170 181.994 1.00 77.05  ? 66   TYR   A O    1 
ATOM   418  C CB   . TYR   A 1 53  ? 209.956 191.025 180.446 1.00 65.00  ? 66   TYR   A CB   1 
ATOM   419  C CG   . TYR   A 1 53  ? 208.717 190.302 179.983 1.00 70.42  ? 66   TYR   A CG   1 
ATOM   420  C CD1  . TYR   A 1 53  ? 208.790 188.938 179.661 1.00 78.51  ? 66   TYR   A CD1  1 
ATOM   421  C CD2  . TYR   A 1 53  ? 207.482 190.962 179.977 1.00 68.01  ? 66   TYR   A CD2  1 
ATOM   422  C CE1  . TYR   A 1 53  ? 207.628 188.232 179.305 1.00 78.32  ? 66   TYR   A CE1  1 
ATOM   423  C CE2  . TYR   A 1 53  ? 206.321 190.261 179.626 1.00 72.96  ? 66   TYR   A CE2  1 
ATOM   424  C CZ   . TYR   A 1 53  ? 206.391 188.902 179.272 1.00 81.61  ? 66   TYR   A CZ   1 
ATOM   425  O OH   . TYR   A 1 53  ? 205.255 188.228 178.967 1.00 84.62  ? 66   TYR   A OH   1 
ATOM   426  N N    . PHE   A 1 54  ? 212.123 190.349 183.291 1.00 71.39  ? 67   PHE   A N    1 
ATOM   427  C CA   . PHE   A 1 54  ? 213.388 190.613 183.964 1.00 62.60  ? 67   PHE   A CA   1 
ATOM   428  C C    . PHE   A 1 54  ? 214.411 189.519 183.660 1.00 67.38  ? 67   PHE   A C    1 
ATOM   429  O O    . PHE   A 1 54  ? 214.032 188.380 183.375 1.00 78.52  ? 67   PHE   A O    1 
ATOM   430  C CB   . PHE   A 1 54  ? 213.147 190.745 185.468 1.00 63.17  ? 67   PHE   A CB   1 
ATOM   431  C CG   . PHE   A 1 54  ? 212.294 191.924 185.864 1.00 65.96  ? 67   PHE   A CG   1 
ATOM   432  C CD1  . PHE   A 1 54  ? 212.839 193.216 185.818 1.00 64.35  ? 67   PHE   A CD1  1 
ATOM   433  C CD2  . PHE   A 1 54  ? 210.975 191.736 186.308 1.00 63.83  ? 67   PHE   A CD2  1 
ATOM   434  C CE1  . PHE   A 1 54  ? 212.061 194.316 186.206 1.00 69.46  ? 67   PHE   A CE1  1 
ATOM   435  C CE2  . PHE   A 1 54  ? 210.202 192.837 186.705 1.00 65.51  ? 67   PHE   A CE2  1 
ATOM   436  C CZ   . PHE   A 1 54  ? 210.745 194.127 186.644 1.00 69.78  ? 67   PHE   A CZ   1 
ATOM   437  N N    . PRO   A 1 55  ? 215.709 189.829 183.712 1.00 58.25  ? 68   PRO   A N    1 
ATOM   438  C CA   . PRO   A 1 55  ? 216.736 188.807 183.678 1.00 61.26  ? 68   PRO   A CA   1 
ATOM   439  C C    . PRO   A 1 55  ? 216.690 187.961 184.956 1.00 65.24  ? 68   PRO   A C    1 
ATOM   440  O O    . PRO   A 1 55  ? 216.236 188.424 186.004 1.00 69.14  ? 68   PRO   A O    1 
ATOM   441  C CB   . PRO   A 1 55  ? 218.036 189.593 183.552 1.00 59.45  ? 68   PRO   A CB   1 
ATOM   442  C CG   . PRO   A 1 55  ? 217.749 190.888 184.306 1.00 53.49  ? 68   PRO   A CG   1 
ATOM   443  C CD   . PRO   A 1 55  ? 216.291 191.141 183.954 1.00 50.82  ? 68   PRO   A CD   1 
ATOM   444  N N    . LYS   A 1 56  ? 217.191 186.727 184.901 1.00 80.15  ? 69   LYS   A N    1 
ATOM   445  C CA   . LYS   A 1 56  ? 217.466 185.934 186.106 1.00 76.40  ? 69   LYS   A CA   1 
ATOM   446  C C    . LYS   A 1 56  ? 218.613 186.567 186.883 1.00 83.93  ? 69   LYS   A C    1 
ATOM   447  O O    . LYS   A 1 56  ? 219.667 186.812 186.306 1.00 92.49  ? 69   LYS   A O    1 
ATOM   448  C CB   . LYS   A 1 56  ? 217.854 184.500 185.724 1.00 77.29  ? 69   LYS   A CB   1 
ATOM   449  C CG   . LYS   A 1 56  ? 216.654 183.558 185.669 1.00 84.77  ? 69   LYS   A CG   1 
ATOM   450  C CD   . LYS   A 1 56  ? 217.041 182.164 185.154 1.00 88.81  ? 69   LYS   A CD   1 
ATOM   451  C CE   . LYS   A 1 56  ? 218.164 181.457 185.931 1.00 86.42  ? 69   LYS   A CE   1 
ATOM   452  N NZ   . LYS   A 1 56  ? 217.757 181.049 187.296 1.00 84.09  ? 69   LYS   A NZ   1 
ATOM   453  N N    . SER   A 1 57  ? 218.469 186.760 188.189 1.00 80.45  ? 70   SER   A N    1 
ATOM   454  C CA   . SER   A 1 57  ? 219.608 187.106 189.038 1.00 80.78  ? 70   SER   A CA   1 
ATOM   455  C C    . SER   A 1 57  ? 220.685 186.022 188.926 1.00 83.96  ? 70   SER   A C    1 
ATOM   456  O O    . SER   A 1 57  ? 220.378 184.832 188.892 1.00 81.80  ? 70   SER   A O    1 
ATOM   457  C CB   . SER   A 1 57  ? 219.144 187.300 190.478 1.00 80.07  ? 70   SER   A CB   1 
ATOM   458  O OG   . SER   A 1 57  ? 220.238 187.663 191.291 1.00 83.11  ? 70   SER   A OG   1 
ATOM   459  N N    . GLY   A 1 58  ? 221.950 186.409 188.811 1.00 78.73  ? 71   GLY   A N    1 
ATOM   460  C CA   . GLY   A 1 58  ? 223.078 185.495 188.655 1.00 77.54  ? 71   GLY   A CA   1 
ATOM   461  C C    . GLY   A 1 58  ? 223.279 184.901 187.259 1.00 83.57  ? 71   GLY   A C    1 
ATOM   462  O O    . GLY   A 1 58  ? 224.169 184.072 187.101 1.00 88.35  ? 71   GLY   A O    1 
ATOM   463  N N    . ALA   A 1 59  ? 222.503 185.284 186.240 1.00 86.72  ? 72   ALA   A N    1 
ATOM   464  C CA   . ALA   A 1 59  ? 222.723 184.822 184.868 1.00 83.01  ? 72   ALA   A CA   1 
ATOM   465  C C    . ALA   A 1 59  ? 223.977 185.436 184.223 1.00 84.39  ? 72   ALA   A C    1 
ATOM   466  O O    . ALA   A 1 59  ? 224.319 186.582 184.500 1.00 86.67  ? 72   ALA   A O    1 
ATOM   467  C CB   . ALA   A 1 59  ? 221.482 185.133 184.038 1.00 81.04  ? 72   ALA   A CB   1 
ATOM   468  N N    . ASN   A 1 60  ? 224.638 184.706 183.319 1.00 83.47  ? 73   ASN   A N    1 
ATOM   469  C CA   . ASN   A 1 60  ? 225.669 185.253 182.434 1.00 86.33  ? 73   ASN   A CA   1 
ATOM   470  C C    . ASN   A 1 60  ? 225.045 186.008 181.246 1.00 84.92  ? 73   ASN   A C    1 
ATOM   471  O O    . ASN   A 1 60  ? 223.841 185.944 180.987 1.00 87.15  ? 73   ASN   A O    1 
ATOM   472  C CB   . ASN   A 1 60  ? 226.594 184.138 181.906 1.00 90.50  ? 73   ASN   A CB   1 
ATOM   473  C CG   . ASN   A 1 60  ? 227.224 183.291 182.988 1.00 95.07  ? 73   ASN   A CG   1 
ATOM   474  O OD1  . ASN   A 1 60  ? 226.611 182.367 183.500 1.00 94.02  ? 73   ASN   A OD1  1 
ATOM   475  N ND2  . ASN   A 1 60  ? 228.455 183.544 183.364 1.00 94.72  ? 73   ASN   A ND2  1 
ATOM   476  N N    . PHE   A 1 61  ? 225.898 186.658 180.467 1.00 75.61  ? 74   PHE   A N    1 
ATOM   477  C CA   . PHE   A 1 61  ? 225.581 187.275 179.188 1.00 75.80  ? 74   PHE   A CA   1 
ATOM   478  C C    . PHE   A 1 61  ? 226.440 186.670 178.071 1.00 79.06  ? 74   PHE   A C    1 
ATOM   479  O O    . PHE   A 1 61  ? 227.570 186.251 178.311 1.00 88.53  ? 74   PHE   A O    1 
ATOM   480  C CB   . PHE   A 1 61  ? 225.853 188.776 179.249 1.00 72.40  ? 74   PHE   A CB   1 
ATOM   481  C CG   . PHE   A 1 61  ? 225.094 189.608 180.263 1.00 71.78  ? 74   PHE   A CG   1 
ATOM   482  C CD1  . PHE   A 1 61  ? 225.426 189.546 181.625 1.00 79.30  ? 74   PHE   A CD1  1 
ATOM   483  C CD2  . PHE   A 1 61  ? 224.139 190.543 179.828 1.00 74.11  ? 74   PHE   A CD2  1 
ATOM   484  C CE1  . PHE   A 1 61  ? 224.780 190.381 182.545 1.00 84.26  ? 74   PHE   A CE1  1 
ATOM   485  C CE2  . PHE   A 1 61  ? 223.504 191.389 180.747 1.00 75.54  ? 74   PHE   A CE2  1 
ATOM   486  C CZ   . PHE   A 1 61  ? 223.819 191.301 182.109 1.00 79.36  ? 74   PHE   A CZ   1 
ATOM   487  N N    . ARG   A 1 62  ? 225.941 186.697 176.836 1.00 79.30  ? 75   ARG   A N    1 
ATOM   488  C CA   . ARG   A 1 62  ? 226.702 186.424 175.605 1.00 75.38  ? 75   ARG   A CA   1 
ATOM   489  C C    . ARG   A 1 62  ? 227.122 187.737 174.969 1.00 77.85  ? 75   ARG   A C    1 
ATOM   490  O O    . ARG   A 1 62  ? 226.262 188.578 174.749 1.00 84.46  ? 75   ARG   A O    1 
ATOM   491  C CB   . ARG   A 1 62  ? 225.799 185.672 174.622 1.00 74.19  ? 75   ARG   A CB   1 
ATOM   492  C CG   . ARG   A 1 62  ? 225.610 184.206 175.009 1.00 78.57  ? 75   ARG   A CG   1 
ATOM   493  C CD   . ARG   A 1 62  ? 224.298 183.640 174.473 1.00 83.61  ? 75   ARG   A CD   1 
ATOM   494  N NE   . ARG   A 1 62  ? 224.177 183.741 173.005 1.00 86.26  ? 75   ARG   A NE   1 
ATOM   495  C CZ   . ARG   A 1 62  ? 223.146 184.211 172.329 1.00 80.86  ? 75   ARG   A CZ   1 
ATOM   496  N NH1  . ARG   A 1 62  ? 223.096 184.126 171.040 1.00 77.77  ? 75   ARG   A NH1  1 
ATOM   497  N NH2  . ARG   A 1 62  ? 222.129 184.768 172.908 1.00 81.05  ? 75   ARG   A NH2  1 
ATOM   498  N N    . ASP   A 1 63  ? 228.393 187.941 174.649 1.00 83.86  ? 76   ASP   A N    1 
ATOM   499  C CA   . ASP   A 1 63  ? 228.816 189.086 173.832 1.00 83.63  ? 76   ASP   A CA   1 
ATOM   500  C C    . ASP   A 1 63  ? 228.592 188.789 172.355 1.00 90.32  ? 76   ASP   A C    1 
ATOM   501  O O    . ASP   A 1 63  ? 229.317 187.996 171.758 1.00 90.35  ? 76   ASP   A O    1 
ATOM   502  C CB   . ASP   A 1 63  ? 230.284 189.428 174.073 1.00 85.33  ? 76   ASP   A CB   1 
ATOM   503  C CG   . ASP   A 1 63  ? 230.820 190.510 173.137 1.00 90.54  ? 76   ASP   A CG   1 
ATOM   504  O OD1  . ASP   A 1 63  ? 230.028 191.326 172.611 1.00 92.04  ? 76   ASP   A OD1  1 
ATOM   505  O OD2  . ASP   A 1 63  ? 232.051 190.535 172.930 1.00 96.26  ? 76   ASP   A OD2  1 
ATOM   506  N N    . LEU   A 1 64  ? 227.598 189.437 171.761 1.00 86.22  ? 77   LEU   A N    1 
ATOM   507  C CA   . LEU   A 1 64  ? 227.249 189.271 170.354 1.00 75.24  ? 77   LEU   A CA   1 
ATOM   508  C C    . LEU   A 1 64  ? 227.873 190.315 169.435 1.00 80.02  ? 77   LEU   A C    1 
ATOM   509  O O    . LEU   A 1 64  ? 227.595 190.316 168.242 1.00 92.97  ? 77   LEU   A O    1 
ATOM   510  C CB   . LEU   A 1 64  ? 225.724 189.258 170.221 1.00 75.93  ? 77   LEU   A CB   1 
ATOM   511  C CG   . LEU   A 1 64  ? 225.044 188.135 170.999 1.00 79.83  ? 77   LEU   A CG   1 
ATOM   512  C CD1  . LEU   A 1 64  ? 223.547 188.220 170.770 1.00 80.95  ? 77   LEU   A CD1  1 
ATOM   513  C CD2  . LEU   A 1 64  ? 225.519 186.763 170.542 1.00 81.12  ? 77   LEU   A CD2  1 
ATOM   514  N N    . SER   A 1 65  ? 228.707 191.220 169.952 1.00 83.06  ? 78   SER   A N    1 
ATOM   515  C CA   . SER   A 1 65  ? 229.370 192.204 169.102 1.00 85.35  ? 78   SER   A CA   1 
ATOM   516  C C    . SER   A 1 65  ? 230.374 191.528 168.169 1.00 90.37  ? 78   SER   A C    1 
ATOM   517  O O    . SER   A 1 65  ? 231.140 190.649 168.563 1.00 92.27  ? 78   SER   A O    1 
ATOM   518  C CB   . SER   A 1 65  ? 230.031 193.296 169.932 1.00 87.81  ? 78   SER   A CB   1 
ATOM   519  O OG   . SER   A 1 65  ? 231.078 192.794 170.724 1.00 92.97  ? 78   SER   A OG   1 
ATOM   520  N N    . LEU   A 1 66  ? 230.358 191.937 166.904 1.00 92.31  ? 79   LEU   A N    1 
ATOM   521  C CA   . LEU   A 1 66  ? 231.264 191.460 165.865 1.00 90.40  ? 79   LEU   A CA   1 
ATOM   522  C C    . LEU   A 1 66  ? 231.972 192.657 165.240 1.00 94.03  ? 79   LEU   A C    1 
ATOM   523  O O    . LEU   A 1 66  ? 231.320 193.534 164.679 1.00 98.03  ? 79   LEU   A O    1 
ATOM   524  C CB   . LEU   A 1 66  ? 230.452 190.674 164.823 1.00 88.91  ? 79   LEU   A CB   1 
ATOM   525  C CG   . LEU   A 1 66  ? 229.881 189.350 165.352 1.00 90.29  ? 79   LEU   A CG   1 
ATOM   526  C CD1  . LEU   A 1 66  ? 228.774 188.874 164.430 1.00 90.91  ? 79   LEU   A CD1  1 
ATOM   527  C CD2  . LEU   A 1 66  ? 230.950 188.267 165.410 1.00 94.68  ? 79   LEU   A CD2  1 
ATOM   528  N N    . LYS   A 1 67  ? 233.301 192.699 165.307 1.00 112.26 ? 80   LYS   A N    1 
ATOM   529  C CA   . LYS   A 1 67  ? 234.100 193.746 164.668 1.00 114.12 ? 80   LYS   A CA   1 
ATOM   530  C C    . LYS   A 1 67  ? 234.755 193.177 163.422 1.00 115.66 ? 80   LYS   A C    1 
ATOM   531  O O    . LYS   A 1 67  ? 235.507 192.216 163.527 1.00 118.04 ? 80   LYS   A O    1 
ATOM   532  C CB   . LYS   A 1 67  ? 235.108 194.304 165.685 1.00 113.72 ? 80   LYS   A CB   1 
ATOM   533  C CG   . LYS   A 1 67  ? 235.862 195.541 165.181 1.00 113.78 ? 80   LYS   A CG   1 
ATOM   534  C CD   . LYS   A 1 67  ? 237.096 195.198 164.338 1.00 116.74 ? 80   LYS   A CD   1 
ATOM   535  C CE   . LYS   A 1 67  ? 237.764 196.476 163.858 1.00 117.54 ? 80   LYS   A CE   1 
ATOM   536  N NZ   . LYS   A 1 67  ? 238.719 196.234 162.764 1.00 118.83 ? 80   LYS   A NZ   1 
ATOM   537  N N    . GLY   A 1 68  ? 234.529 193.776 162.262 1.00 113.55 ? 81   GLY   A N    1 
ATOM   538  C CA   . GLY   A 1 68  ? 235.213 193.399 161.020 1.00 114.10 ? 81   GLY   A CA   1 
ATOM   539  C C    . GLY   A 1 68  ? 236.264 194.414 160.579 1.00 118.77 ? 81   GLY   A C    1 
ATOM   540  O O    . GLY   A 1 68  ? 236.351 195.517 161.119 1.00 119.35 ? 81   GLY   A O    1 
ATOM   541  N N    . THR   A 1 69  ? 237.048 194.072 159.564 1.00 126.64 ? 82   THR   A N    1 
ATOM   542  C CA   . THR   A 1 69  ? 237.855 195.052 158.823 1.00 127.81 ? 82   THR   A CA   1 
ATOM   543  C C    . THR   A 1 69  ? 237.358 195.122 157.381 1.00 127.37 ? 82   THR   A C    1 
ATOM   544  O O    . THR   A 1 69  ? 236.345 195.774 157.146 1.00 127.63 ? 82   THR   A O    1 
ATOM   545  C CB   . THR   A 1 69  ? 239.362 194.851 159.019 1.00 128.70 ? 82   THR   A CB   1 
ATOM   546  O OG1  . THR   A 1 69  ? 239.687 194.882 160.391 1.00 131.45 ? 82   THR   A OG1  1 
ATOM   547  C CG2  . THR   A 1 69  ? 240.148 195.991 158.382 1.00 127.01 ? 82   THR   A CG2  1 
ATOM   548  N N    . THR   A 1 70  ? 237.968 194.426 156.421 1.00 124.44 ? 83   THR   A N    1 
ATOM   549  C CA   . THR   A 1 70  ? 237.428 194.329 155.051 1.00 124.86 ? 83   THR   A CA   1 
ATOM   550  C C    . THR   A 1 70  ? 236.417 193.197 154.917 1.00 123.81 ? 83   THR   A C    1 
ATOM   551  O O    . THR   A 1 70  ? 235.329 193.402 154.385 1.00 124.85 ? 83   THR   A O    1 
ATOM   552  C CB   . THR   A 1 70  ? 238.546 194.117 154.022 1.00 128.97 ? 83   THR   A CB   1 
ATOM   553  O OG1  . THR   A 1 70  ? 239.419 193.100 154.455 1.00 130.98 ? 83   THR   A OG1  1 
ATOM   554  C CG2  . THR   A 1 70  ? 239.378 195.372 153.807 1.00 125.92 ? 83   THR   A CG2  1 
ATOM   555  N N    . TYR   A 1 71  ? 236.759 191.995 155.384 1.00 118.32 ? 84   TYR   A N    1 
ATOM   556  C CA   . TYR   A 1 71  ? 235.949 190.796 155.185 1.00 118.97 ? 84   TYR   A CA   1 
ATOM   557  C C    . TYR   A 1 71  ? 234.785 190.660 156.166 1.00 119.66 ? 84   TYR   A C    1 
ATOM   558  O O    . TYR   A 1 71  ? 234.880 191.068 157.320 1.00 120.89 ? 84   TYR   A O    1 
ATOM   559  C CB   . TYR   A 1 71  ? 236.828 189.541 155.235 1.00 118.53 ? 84   TYR   A CB   1 
ATOM   560  C CG   . TYR   A 1 71  ? 237.587 189.279 153.953 1.00 120.92 ? 84   TYR   A CG   1 
ATOM   561  C CD1  . TYR   A 1 71  ? 236.989 188.501 152.945 1.00 117.11 ? 84   TYR   A CD1  1 
ATOM   562  C CD2  . TYR   A 1 71  ? 238.879 189.801 153.768 1.00 121.55 ? 84   TYR   A CD2  1 
ATOM   563  C CE1  . TYR   A 1 71  ? 237.673 188.255 151.744 1.00 119.97 ? 84   TYR   A CE1  1 
ATOM   564  C CE2  . TYR   A 1 71  ? 239.567 189.562 152.564 1.00 121.69 ? 84   TYR   A CE2  1 
ATOM   565  C CZ   . TYR   A 1 71  ? 238.962 188.792 151.550 1.00 123.86 ? 84   TYR   A CZ   1 
ATOM   566  O OH   . TYR   A 1 71  ? 239.618 188.557 150.385 1.00 122.09 ? 84   TYR   A OH   1 
ATOM   567  N N    . LEU   A 1 72  ? 233.725 189.988 155.723 1.00 110.86 ? 85   LEU   A N    1 
ATOM   568  C CA   . LEU   A 1 72  ? 232.631 189.471 156.546 1.00 106.80 ? 85   LEU   A CA   1 
ATOM   569  C C    . LEU   A 1 72  ? 232.542 187.950 156.385 1.00 105.69 ? 85   LEU   A C    1 
ATOM   570  O O    . LEU   A 1 72  ? 232.765 187.440 155.291 1.00 111.65 ? 85   LEU   A O    1 
ATOM   571  C CB   . LEU   A 1 72  ? 231.303 190.105 156.114 1.00 105.69 ? 85   LEU   A CB   1 
ATOM   572  C CG   . LEU   A 1 72  ? 231.241 191.638 156.118 1.00 108.55 ? 85   LEU   A CG   1 
ATOM   573  C CD1  . LEU   A 1 72  ? 229.915 192.068 155.506 1.00 107.26 ? 85   LEU   A CD1  1 
ATOM   574  C CD2  . LEU   A 1 72  ? 231.338 192.222 157.520 1.00 109.17 ? 85   LEU   A CD2  1 
ATOM   575  N N    . SER   A 1 73  ? 232.190 187.218 157.439 1.00 101.40 ? 86   SER   A N    1 
ATOM   576  C CA   . SER   A 1 73  ? 231.993 185.765 157.354 1.00 103.79 ? 86   SER   A CA   1 
ATOM   577  C C    . SER   A 1 73  ? 230.512 185.427 157.239 1.00 102.62 ? 86   SER   A C    1 
ATOM   578  O O    . SER   A 1 73  ? 229.702 185.953 157.993 1.00 107.46 ? 86   SER   A O    1 
ATOM   579  C CB   . SER   A 1 73  ? 232.603 185.066 158.562 1.00 108.38 ? 86   SER   A CB   1 
ATOM   580  O OG   . SER   A 1 73  ? 232.298 183.689 158.536 1.00 110.34 ? 86   SER   A OG   1 
ATOM   581  N N    . THR   A 1 74  ? 230.114 184.520 156.351 1.00 104.69 ? 87   THR   A N    1 
ATOM   582  C CA   . THR   A 1 74  ? 228.735 184.018 156.305 1.00 106.66 ? 87   THR   A CA   1 
ATOM   583  C C    . THR   A 1 74  ? 228.322 183.387 157.633 1.00 108.33 ? 87   THR   A C    1 
ATOM   584  O O    . THR   A 1 74  ? 227.170 183.528 158.038 1.00 109.03 ? 87   THR   A O    1 
ATOM   585  C CB   . THR   A 1 74  ? 228.531 182.990 155.193 1.00 104.31 ? 87   THR   A CB   1 
ATOM   586  O OG1  . THR   A 1 74  ? 229.378 181.889 155.382 1.00 106.74 ? 87   THR   A OG1  1 
ATOM   587  C CG2  . THR   A 1 74  ? 228.805 183.553 153.810 1.00 105.23 ? 87   THR   A CG2  1 
ATOM   588  N N    . LEU   A 1 75  ? 229.254 182.784 158.378 1.00 103.55 ? 88   LEU   A N    1 
ATOM   589  C CA   . LEU   A 1 75  ? 228.977 182.213 159.694 1.00 101.51 ? 88   LEU   A CA   1 
ATOM   590  C C    . LEU   A 1 75  ? 228.619 183.267 160.746 1.00 103.36 ? 88   LEU   A C    1 
ATOM   591  O O    . LEU   A 1 75  ? 228.033 182.921 161.763 1.00 107.02 ? 88   LEU   A O    1 
ATOM   592  C CB   . LEU   A 1 75  ? 230.157 181.360 160.176 1.00 101.20 ? 88   LEU   A CB   1 
ATOM   593  C CG   . LEU   A 1 75  ? 230.519 180.164 159.283 1.00 104.33 ? 88   LEU   A CG   1 
ATOM   594  C CD1  . LEU   A 1 75  ? 231.669 179.398 159.921 1.00 103.71 ? 88   LEU   A CD1  1 
ATOM   595  C CD2  . LEU   A 1 75  ? 229.353 179.198 159.104 1.00 102.03 ? 88   LEU   A CD2  1 
ATOM   596  N N    . TRP   A 1 76  ? 228.909 184.548 160.521 1.00 97.95  ? 89   TRP   A N    1 
ATOM   597  C CA   . TRP   A 1 76  ? 228.436 185.624 161.398 1.00 95.98  ? 89   TRP   A CA   1 
ATOM   598  C C    . TRP   A 1 76  ? 226.933 185.885 161.271 1.00 100.43 ? 89   TRP   A C    1 
ATOM   599  O O    . TRP   A 1 76  ? 226.365 186.562 162.117 1.00 106.81 ? 89   TRP   A O    1 
ATOM   600  C CB   . TRP   A 1 76  ? 229.198 186.915 161.098 1.00 94.40  ? 89   TRP   A CB   1 
ATOM   601  C CG   . TRP   A 1 76  ? 230.668 186.940 161.394 1.00 98.73  ? 89   TRP   A CG   1 
ATOM   602  C CD1  . TRP   A 1 76  ? 231.404 185.969 161.981 1.00 100.04 ? 89   TRP   A CD1  1 
ATOM   603  C CD2  . TRP   A 1 76  ? 231.601 188.025 161.123 1.00 98.36  ? 89   TRP   A CD2  1 
ATOM   604  N NE1  . TRP   A 1 76  ? 232.728 186.354 162.035 1.00 101.86 ? 89   TRP   A NE1  1 
ATOM   605  C CE2  . TRP   A 1 76  ? 232.904 187.611 161.513 1.00 99.26  ? 89   TRP   A CE2  1 
ATOM   606  C CE3  . TRP   A 1 76  ? 231.473 189.316 160.579 1.00 97.60  ? 89   TRP   A CE3  1 
ATOM   607  C CZ2  . TRP   A 1 76  ? 234.032 188.418 161.340 1.00 99.96  ? 89   TRP   A CZ2  1 
ATOM   608  C CZ3  . TRP   A 1 76  ? 232.594 190.152 160.434 1.00 99.77  ? 89   TRP   A CZ3  1 
ATOM   609  C CH2  . TRP   A 1 76  ? 233.871 189.699 160.793 1.00 101.81 ? 89   TRP   A CH2  1 
ATOM   610  N N    . TYR   A 1 77  ? 226.268 185.368 160.242 1.00 93.70  ? 90   TYR   A N    1 
ATOM   611  C CA   . TYR   A 1 77  ? 224.861 185.645 159.935 1.00 89.04  ? 90   TYR   A CA   1 
ATOM   612  C C    . TYR   A 1 77  ? 223.959 184.422 160.138 1.00 91.90  ? 90   TYR   A C    1 
ATOM   613  O O    . TYR   A 1 77  ? 223.004 184.198 159.396 1.00 101.26 ? 90   TYR   A O    1 
ATOM   614  C CB   . TYR   A 1 77  ? 224.794 186.235 158.531 1.00 92.96  ? 90   TYR   A CB   1 
ATOM   615  C CG   . TYR   A 1 77  ? 225.548 187.534 158.407 1.00 91.75  ? 90   TYR   A CG   1 
ATOM   616  C CD1  . TYR   A 1 77  ? 224.986 188.687 158.960 1.00 90.44  ? 90   TYR   A CD1  1 
ATOM   617  C CD2  . TYR   A 1 77  ? 226.805 187.594 157.783 1.00 93.77  ? 90   TYR   A CD2  1 
ATOM   618  C CE1  . TYR   A 1 77  ? 225.650 189.911 158.868 1.00 90.72  ? 90   TYR   A CE1  1 
ATOM   619  C CE2  . TYR   A 1 77  ? 227.476 188.825 157.686 1.00 95.60  ? 90   TYR   A CE2  1 
ATOM   620  C CZ   . TYR   A 1 77  ? 226.890 189.987 158.221 1.00 93.69  ? 90   TYR   A CZ   1 
ATOM   621  O OH   . TYR   A 1 77  ? 227.500 191.187 158.113 1.00 97.91  ? 90   TYR   A OH   1 
ATOM   622  N N    . GLN   A 1 78  ? 224.309 183.602 161.121 1.00 94.13  ? 91   GLN   A N    1 
ATOM   623  C CA   . GLN   A 1 78  ? 223.708 182.314 161.464 1.00 96.40  ? 91   GLN   A CA   1 
ATOM   624  C C    . GLN   A 1 78  ? 223.687 182.144 162.983 1.00 98.40  ? 91   GLN   A C    1 
ATOM   625  O O    . GLN   A 1 78  ? 224.312 182.917 163.712 1.00 102.89 ? 91   GLN   A O    1 
ATOM   626  C CB   . GLN   A 1 78  ? 224.513 181.171 160.824 1.00 98.51  ? 91   GLN   A CB   1 
ATOM   627  C CG   . GLN   A 1 78  ? 224.532 181.208 159.291 1.00 101.91 ? 91   GLN   A CG   1 
ATOM   628  C CD   . GLN   A 1 78  ? 225.183 179.978 158.668 1.00 106.42 ? 91   GLN   A CD   1 
ATOM   629  O OE1  . GLN   A 1 78  ? 225.507 179.000 159.322 1.00 106.57 ? 91   GLN   A OE1  1 
ATOM   630  N NE2  . GLN   A 1 78  ? 225.393 179.969 157.374 1.00 104.95 ? 91   GLN   A NE2  1 
ATOM   631  N N    . LYS   A 1 79  ? 222.996 181.126 163.496 1.00 94.96  ? 92   LYS   A N    1 
ATOM   632  C CA   . LYS   A 1 79  ? 223.230 180.644 164.865 1.00 95.38  ? 92   LYS   A CA   1 
ATOM   633  C C    . LYS   A 1 79  ? 224.721 180.327 165.047 1.00 99.84  ? 92   LYS   A C    1 
ATOM   634  O O    . LYS   A 1 79  ? 225.322 179.762 164.132 1.00 101.42 ? 92   LYS   A O    1 
ATOM   635  C CB   . LYS   A 1 79  ? 222.372 179.397 165.120 1.00 93.41  ? 92   LYS   A CB   1 
ATOM   636  C CG   . LYS   A 1 79  ? 220.908 179.775 165.361 1.00 96.88  ? 92   LYS   A CG   1 
ATOM   637  C CD   . LYS   A 1 79  ? 220.019 178.531 165.468 1.00 99.07  ? 92   LYS   A CD   1 
ATOM   638  C CE   . LYS   A 1 79  ? 218.607 178.899 165.932 1.00 99.21  ? 92   LYS   A CE   1 
ATOM   639  N NZ   . LYS   A 1 79  ? 218.563 179.158 167.391 1.00 100.23 ? 92   LYS   A NZ   1 
ATOM   640  N N    . PRO   A 1 80  ? 225.338 180.672 166.188 1.00 96.75  ? 93   PRO   A N    1 
ATOM   641  C CA   . PRO   A 1 80  ? 224.727 181.161 167.420 1.00 97.21  ? 93   PRO   A CA   1 
ATOM   642  C C    . PRO   A 1 80  ? 224.477 182.674 167.497 1.00 96.80  ? 93   PRO   A C    1 
ATOM   643  O O    . PRO   A 1 80  ? 224.023 183.140 168.535 1.00 100.20 ? 93   PRO   A O    1 
ATOM   644  C CB   . PRO   A 1 80  ? 225.724 180.747 168.501 1.00 95.12  ? 93   PRO   A CB   1 
ATOM   645  C CG   . PRO   A 1 80  ? 227.058 180.927 167.799 1.00 93.74  ? 93   PRO   A CG   1 
ATOM   646  C CD   . PRO   A 1 80  ? 226.748 180.406 166.407 1.00 92.89  ? 93   PRO   A CD   1 
ATOM   647  N N    . PHE   A 1 81  ? 224.799 183.468 166.478 1.00 88.49  ? 94   PHE   A N    1 
ATOM   648  C CA   . PHE   A 1 81  ? 224.650 184.928 166.528 1.00 85.82  ? 94   PHE   A CA   1 
ATOM   649  C C    . PHE   A 1 81  ? 223.215 185.374 166.241 1.00 90.60  ? 94   PHE   A C    1 
ATOM   650  O O    . PHE   A 1 81  ? 222.610 186.085 167.037 1.00 92.50  ? 94   PHE   A O    1 
ATOM   651  C CB   . PHE   A 1 81  ? 225.630 185.587 165.560 1.00 84.54  ? 94   PHE   A CB   1 
ATOM   652  C CG   . PHE   A 1 81  ? 227.060 185.130 165.716 1.00 88.66  ? 94   PHE   A CG   1 
ATOM   653  C CD1  . PHE   A 1 81  ? 227.860 185.657 166.741 1.00 90.70  ? 94   PHE   A CD1  1 
ATOM   654  C CD2  . PHE   A 1 81  ? 227.585 184.177 164.832 1.00 88.71  ? 94   PHE   A CD2  1 
ATOM   655  C CE1  . PHE   A 1 81  ? 229.189 185.234 166.877 1.00 93.56  ? 94   PHE   A CE1  1 
ATOM   656  C CE2  . PHE   A 1 81  ? 228.913 183.753 164.967 1.00 90.29  ? 94   PHE   A CE2  1 
ATOM   657  C CZ   . PHE   A 1 81  ? 229.715 184.284 165.989 1.00 92.83  ? 94   PHE   A CZ   1 
ATOM   658  N N    . LEU   A 1 82  ? 222.634 184.917 165.133 1.00 89.66  ? 95   LEU   A N    1 
ATOM   659  C CA   . LEU   A 1 82  ? 221.210 185.088 164.847 1.00 88.33  ? 95   LEU   A CA   1 
ATOM   660  C C    . LEU   A 1 82  ? 220.416 184.332 165.910 1.00 88.79  ? 95   LEU   A C    1 
ATOM   661  O O    . LEU   A 1 82  ? 220.487 183.108 165.982 1.00 89.97  ? 95   LEU   A O    1 
ATOM   662  C CB   . LEU   A 1 82  ? 220.927 184.593 163.422 1.00 88.92  ? 95   LEU   A CB   1 
ATOM   663  C CG   . LEU   A 1 82  ? 219.443 184.580 163.043 1.00 87.80  ? 95   LEU   A CG   1 
ATOM   664  C CD1  . LEU   A 1 82  ? 218.821 185.967 163.077 1.00 89.68  ? 95   LEU   A CD1  1 
ATOM   665  C CD2  . LEU   A 1 82  ? 219.278 184.018 161.638 1.00 86.60  ? 95   LEU   A CD2  1 
ATOM   666  N N    . SER   A 1 83  ? 219.714 185.056 166.771 1.00 81.39  ? 96   SER   A N    1 
ATOM   667  C CA   . SER   A 1 83  ? 219.218 184.534 168.044 1.00 81.48  ? 96   SER   A CA   1 
ATOM   668  C C    . SER   A 1 83  ? 217.706 184.585 168.140 1.00 76.98  ? 96   SER   A C    1 
ATOM   669  O O    . SER   A 1 83  ? 217.100 185.580 167.765 1.00 82.56  ? 96   SER   A O    1 
ATOM   670  C CB   . SER   A 1 83  ? 219.787 185.375 169.179 1.00 84.23  ? 96   SER   A CB   1 
ATOM   671  O OG   . SER   A 1 83  ? 221.188 185.237 169.246 1.00 84.45  ? 96   SER   A OG   1 
ATOM   672  N N    . ASP   A 1 84  ? 217.085 183.562 168.721 1.00 84.23  ? 97   ASP   A N    1 
ATOM   673  C CA   . ASP   A 1 84  ? 215.664 183.613 169.054 1.00 85.25  ? 97   ASP   A CA   1 
ATOM   674  C C    . ASP   A 1 84  ? 215.402 184.686 170.114 1.00 89.27  ? 97   ASP   A C    1 
ATOM   675  O O    . ASP   A 1 84  ? 216.045 184.701 171.159 1.00 96.04  ? 97   ASP   A O    1 
ATOM   676  C CB   . ASP   A 1 84  ? 215.155 182.256 169.546 1.00 89.46  ? 97   ASP   A CB   1 
ATOM   677  C CG   . ASP   A 1 84  ? 215.411 181.120 168.560 1.00 101.39 ? 97   ASP   A CG   1 
ATOM   678  O OD1  . ASP   A 1 84  ? 216.510 180.522 168.599 1.00 101.43 ? 97   ASP   A OD1  1 
ATOM   679  O OD2  . ASP   A 1 84  ? 214.510 180.804 167.758 1.00 102.29 ? 97   ASP   A OD2  1 
ATOM   680  N N    . PHE   A 1 85  ? 214.448 185.576 169.861 1.00 79.15  ? 98   PHE   A N    1 
ATOM   681  C CA   . PHE   A 1 85  ? 214.091 186.655 170.782 1.00 71.30  ? 98   PHE   A CA   1 
ATOM   682  C C    . PHE   A 1 85  ? 213.286 186.154 171.983 1.00 72.68  ? 98   PHE   A C    1 
ATOM   683  O O    . PHE   A 1 85  ? 213.461 186.654 173.091 1.00 80.66  ? 98   PHE   A O    1 
ATOM   684  C CB   . PHE   A 1 85  ? 213.346 187.735 169.984 1.00 68.02  ? 98   PHE   A CB   1 
ATOM   685  C CG   . PHE   A 1 85  ? 213.029 189.007 170.742 1.00 68.22  ? 98   PHE   A CG   1 
ATOM   686  C CD1  . PHE   A 1 85  ? 214.057 189.878 171.136 1.00 70.98  ? 98   PHE   A CD1  1 
ATOM   687  C CD2  . PHE   A 1 85  ? 211.696 189.349 171.012 1.00 71.06  ? 98   PHE   A CD2  1 
ATOM   688  C CE1  . PHE   A 1 85  ? 213.752 191.073 171.803 1.00 73.09  ? 98   PHE   A CE1  1 
ATOM   689  C CE2  . PHE   A 1 85  ? 211.392 190.538 171.688 1.00 68.53  ? 98   PHE   A CE2  1 
ATOM   690  C CZ   . PHE   A 1 85  ? 212.421 191.398 172.086 1.00 67.86  ? 98   PHE   A CZ   1 
ATOM   691  N N    . ASN   A 1 86  ? 212.452 185.128 171.793 1.00 75.73  ? 99   ASN   A N    1 
ATOM   692  C CA   . ASN   A 1 86  ? 211.575 184.576 172.826 1.00 76.06  ? 99   ASN   A CA   1 
ATOM   693  C C    . ASN   A 1 86  ? 210.755 185.692 173.492 1.00 80.81  ? 99   ASN   A C    1 
ATOM   694  O O    . ASN   A 1 86  ? 210.024 186.418 172.819 1.00 86.89  ? 99   ASN   A O    1 
ATOM   695  C CB   . ASN   A 1 86  ? 212.386 183.684 173.788 1.00 74.89  ? 99   ASN   A CB   1 
ATOM   696  C CG   . ASN   A 1 86  ? 213.003 182.490 173.095 1.00 86.07  ? 99   ASN   A CG   1 
ATOM   697  O OD1  . ASN   A 1 86  ? 212.344 181.758 172.376 1.00 88.00  ? 99   ASN   A OD1  1 
ATOM   698  N ND2  . ASN   A 1 86  ? 214.272 182.237 173.288 1.00 85.76  ? 99   ASN   A ND2  1 
ATOM   699  N N    . ASN   A 1 87  ? 210.860 185.843 174.810 1.00 72.94  ? 100  ASN   A N    1 
ATOM   700  C CA   . ASN   A 1 87  ? 210.180 186.897 175.548 1.00 70.33  ? 100  ASN   A CA   1 
ATOM   701  C C    . ASN   A 1 87  ? 210.868 188.259 175.400 1.00 75.48  ? 100  ASN   A C    1 
ATOM   702  O O    . ASN   A 1 87  ? 210.198 189.287 175.411 1.00 84.54  ? 100  ASN   A O    1 
ATOM   703  C CB   . ASN   A 1 87  ? 210.103 186.480 177.019 1.00 72.70  ? 100  ASN   A CB   1 
ATOM   704  C CG   . ASN   A 1 87  ? 209.392 185.158 177.207 1.00 81.53  ? 100  ASN   A CG   1 
ATOM   705  O OD1  . ASN   A 1 87  ? 210.003 184.130 177.437 1.00 88.96  ? 100  ASN   A OD1  1 
ATOM   706  N ND2  . ASN   A 1 87  ? 208.090 185.134 177.079 1.00 79.75  ? 100  ASN   A ND2  1 
ATOM   707  N N    . GLY   A 1 88  ? 212.193 188.276 175.272 1.00 59.99  ? 101  GLY   A N    1 
ATOM   708  C CA   . GLY   A 1 88  ? 212.988 189.492 175.202 1.00 57.17  ? 101  GLY   A CA   1 
ATOM   709  C C    . GLY   A 1 88  ? 214.404 189.316 175.731 1.00 59.28  ? 101  GLY   A C    1 
ATOM   710  O O    . GLY   A 1 88  ? 214.811 188.218 176.109 1.00 71.68  ? 101  GLY   A O    1 
ATOM   711  N N    . ILE   A 1 89  ? 215.146 190.413 175.821 1.00 58.66  ? 102  ILE   A N    1 
ATOM   712  C CA   . ILE   A 1 89  ? 216.538 190.462 176.272 1.00 61.45  ? 102  ILE   A CA   1 
ATOM   713  C C    . ILE   A 1 89  ? 216.829 191.678 177.151 1.00 61.73  ? 102  ILE   A C    1 
ATOM   714  O O    . ILE   A 1 89  ? 216.278 192.753 176.942 1.00 68.62  ? 102  ILE   A O    1 
ATOM   715  C CB   . ILE   A 1 89  ? 217.502 190.445 175.079 1.00 54.59  ? 102  ILE   A CB   1 
ATOM   716  C CG1  . ILE   A 1 89  ? 217.221 191.575 174.069 1.00 59.44  ? 102  ILE   A CG1  1 
ATOM   717  C CG2  . ILE   A 1 89  ? 217.496 189.069 174.407 1.00 63.80  ? 102  ILE   A CG2  1 
ATOM   718  C CD1  . ILE   A 1 89  ? 218.349 191.814 173.074 1.00 63.44  ? 102  ILE   A CD1  1 
ATOM   719  N N    . PHE   A 1 90  ? 217.746 191.518 178.100 1.00 61.72  ? 103  PHE   A N    1 
ATOM   720  C CA   . PHE   A 1 90  ? 218.466 192.615 178.738 1.00 56.34  ? 103  PHE   A CA   1 
ATOM   721  C C    . PHE   A 1 90  ? 219.861 192.650 178.129 1.00 62.64  ? 103  PHE   A C    1 
ATOM   722  O O    . PHE   A 1 90  ? 220.491 191.603 177.991 1.00 74.85  ? 103  PHE   A O    1 
ATOM   723  C CB   . PHE   A 1 90  ? 218.528 192.415 180.259 1.00 60.77  ? 103  PHE   A CB   1 
ATOM   724  C CG   . PHE   A 1 90  ? 219.366 193.412 181.033 1.00 61.74  ? 103  PHE   A CG   1 
ATOM   725  C CD1  . PHE   A 1 90  ? 219.055 194.773 180.965 1.00 58.03  ? 103  PHE   A CD1  1 
ATOM   726  C CD2  . PHE   A 1 90  ? 220.409 192.987 181.872 1.00 67.30  ? 103  PHE   A CD2  1 
ATOM   727  C CE1  . PHE   A 1 90  ? 219.766 195.710 181.726 1.00 61.36  ? 103  PHE   A CE1  1 
ATOM   728  C CE2  . PHE   A 1 90  ? 221.130 193.923 182.628 1.00 65.03  ? 103  PHE   A CE2  1 
ATOM   729  C CZ   . PHE   A 1 90  ? 220.812 195.284 182.554 1.00 65.86  ? 103  PHE   A CZ   1 
ATOM   730  N N    . SER   A 1 91  ? 220.353 193.818 177.738 1.00 63.70  ? 104  SER   A N    1 
ATOM   731  C CA   . SER   A 1 91  ? 221.709 193.960 177.210 1.00 61.40  ? 104  SER   A CA   1 
ATOM   732  C C    . SER   A 1 91  ? 222.526 194.980 177.979 1.00 66.85  ? 104  SER   A C    1 
ATOM   733  O O    . SER   A 1 91  ? 222.002 195.981 178.455 1.00 78.99  ? 104  SER   A O    1 
ATOM   734  C CB   . SER   A 1 91  ? 221.708 194.237 175.707 1.00 67.33  ? 104  SER   A CB   1 
ATOM   735  O OG   . SER   A 1 91  ? 221.196 195.507 175.400 1.00 74.02  ? 104  SER   A OG   1 
ATOM   736  N N    . ARG   A 1 92  ? 223.825 194.716 178.101 1.00 82.69  ? 105  ARG   A N    1 
ATOM   737  C CA   . ARG   A 1 92  ? 224.838 195.624 178.638 1.00 82.30  ? 105  ARG   A CA   1 
ATOM   738  C C    . ARG   A 1 92  ? 225.833 195.915 177.528 1.00 83.84  ? 105  ARG   A C    1 
ATOM   739  O O    . ARG   A 1 92  ? 226.495 195.017 177.021 1.00 89.90  ? 105  ARG   A O    1 
ATOM   740  C CB   . ARG   A 1 92  ? 225.476 194.975 179.874 1.00 85.32  ? 105  ARG   A CB   1 
ATOM   741  C CG   . ARG   A 1 92  ? 226.669 195.782 180.394 1.00 93.17  ? 105  ARG   A CG   1 
ATOM   742  C CD   . ARG   A 1 92  ? 227.266 195.166 181.659 1.00 89.63  ? 105  ARG   A CD   1 
ATOM   743  N NE   . ARG   A 1 92  ? 228.205 194.079 181.334 1.00 95.94  ? 105  ARG   A NE   1 
ATOM   744  C CZ   . ARG   A 1 92  ? 229.453 193.970 181.751 1.00 98.42  ? 105  ARG   A CZ   1 
ATOM   745  N NH1  . ARG   A 1 92  ? 230.218 193.028 181.284 1.00 95.97  ? 105  ARG   A NH1  1 
ATOM   746  N NH2  . ARG   A 1 92  ? 229.972 194.785 182.620 1.00 91.04  ? 105  ARG   A NH2  1 
ATOM   747  N N    . VAL   A 1 93  ? 225.940 197.166 177.129 1.00 80.48  ? 106  VAL   A N    1 
ATOM   748  C CA   . VAL   A 1 93  ? 226.620 197.569 175.906 1.00 80.08  ? 106  VAL   A CA   1 
ATOM   749  C C    . VAL   A 1 93  ? 227.769 198.492 176.247 1.00 83.24  ? 106  VAL   A C    1 
ATOM   750  O O    . VAL   A 1 93  ? 227.555 199.548 176.834 1.00 86.57  ? 106  VAL   A O    1 
ATOM   751  C CB   . VAL   A 1 93  ? 225.618 198.237 174.959 1.00 80.58  ? 106  VAL   A CB   1 
ATOM   752  C CG1  . VAL   A 1 93  ? 226.280 198.574 173.628 1.00 81.81  ? 106  VAL   A CG1  1 
ATOM   753  C CG2  . VAL   A 1 93  ? 224.424 197.323 174.692 1.00 80.28  ? 106  VAL   A CG2  1 
ATOM   754  N N    . LYS   A 1 94  ? 228.996 198.114 175.900 1.00 93.06  ? 107  LYS   A N    1 
ATOM   755  C CA   . LYS   A 1 94  ? 230.144 198.994 176.075 1.00 94.84  ? 107  LYS   A CA   1 
ATOM   756  C C    . LYS   A 1 94  ? 230.013 200.136 175.091 1.00 94.68  ? 107  LYS   A C    1 
ATOM   757  O O    . LYS   A 1 94  ? 229.906 199.906 173.894 1.00 97.69  ? 107  LYS   A O    1 
ATOM   758  C CB   . LYS   A 1 94  ? 231.440 198.209 175.870 1.00 93.44  ? 107  LYS   A CB   1 
ATOM   759  C CG   . LYS   A 1 94  ? 232.703 199.075 175.916 1.00 91.46  ? 107  LYS   A CG   1 
ATOM   760  C CD   . LYS   A 1 94  ? 233.950 198.190 175.951 1.00 95.34  ? 107  LYS   A CD   1 
ATOM   761  C CE   . LYS   A 1 94  ? 235.217 198.903 175.481 1.00 97.48  ? 107  LYS   A CE   1 
ATOM   762  N NZ   . LYS   A 1 94  ? 235.681 199.979 176.383 1.00 98.65  ? 107  LYS   A NZ   1 
ATOM   763  N N    . ASN   A 1 95  ? 230.052 201.363 175.579 1.00 98.10  ? 108  ASN   A N    1 
ATOM   764  C CA   . ASN   A 1 95  ? 230.200 202.524 174.725 1.00 97.36  ? 108  ASN   A CA   1 
ATOM   765  C C    . ASN   A 1 95  ? 231.670 202.634 174.312 1.00 103.04 ? 108  ASN   A C    1 
ATOM   766  O O    . ASN   A 1 95  ? 232.521 202.970 175.131 1.00 106.54 ? 108  ASN   A O    1 
ATOM   767  C CB   . ASN   A 1 95  ? 229.722 203.737 175.513 1.00 97.19  ? 108  ASN   A CB   1 
ATOM   768  C CG   . ASN   A 1 95  ? 229.989 205.026 174.783 1.00 101.31 ? 108  ASN   A CG   1 
ATOM   769  O OD1  . ASN   A 1 95  ? 230.050 205.074 173.571 1.00 105.04 ? 108  ASN   A OD1  1 
ATOM   770  N ND2  . ASN   A 1 95  ? 230.161 206.100 175.498 1.00 102.60 ? 108  ASN   A ND2  1 
ATOM   771  N N    . THR   A 1 96  ? 232.008 202.299 173.073 1.00 109.44 ? 109  THR   A N    1 
ATOM   772  C CA   . THR   A 1 96  ? 233.392 202.304 172.610 1.00 108.42 ? 109  THR   A CA   1 
ATOM   773  C C    . THR   A 1 96  ? 233.811 203.727 172.279 1.00 109.97 ? 109  THR   A C    1 
ATOM   774  O O    . THR   A 1 96  ? 233.311 204.332 171.334 1.00 112.26 ? 109  THR   A O    1 
ATOM   775  C CB   . THR   A 1 96  ? 233.578 201.346 171.436 1.00 107.72 ? 109  THR   A CB   1 
ATOM   776  O OG1  . THR   A 1 96  ? 233.302 200.034 171.863 1.00 108.99 ? 109  THR   A OG1  1 
ATOM   777  C CG2  . THR   A 1 96  ? 234.996 201.357 170.904 1.00 108.90 ? 109  THR   A CG2  1 
ATOM   778  N N    . LYS   A 1 97  ? 234.718 204.277 173.087 1.00 113.95 ? 110  LYS   A N    1 
ATOM   779  C CA   . LYS   A 1 97  ? 235.128 205.682 173.068 1.00 114.23 ? 110  LYS   A CA   1 
ATOM   780  C C    . LYS   A 1 97  ? 236.432 205.820 172.284 1.00 118.46 ? 110  LYS   A C    1 
ATOM   781  O O    . LYS   A 1 97  ? 237.443 205.232 172.657 1.00 117.43 ? 110  LYS   A O    1 
ATOM   782  C CB   . LYS   A 1 97  ? 235.251 206.144 174.530 1.00 112.86 ? 110  LYS   A CB   1 
ATOM   783  C CG   . LYS   A 1 97  ? 233.867 206.436 175.143 1.00 113.36 ? 110  LYS   A CG   1 
ATOM   784  C CD   . LYS   A 1 97  ? 233.767 206.226 176.658 1.00 112.69 ? 110  LYS   A CD   1 
ATOM   785  C CE   . LYS   A 1 97  ? 234.867 206.922 177.463 1.00 113.46 ? 110  LYS   A CE   1 
ATOM   786  N NZ   . LYS   A 1 97  ? 234.621 206.816 178.925 1.00 111.35 ? 110  LYS   A NZ   1 
ATOM   787  N N    . LEU   A 1 98  ? 236.395 206.587 171.198 1.00 127.29 ? 111  LEU   A N    1 
ATOM   788  C CA   . LEU   A 1 98  ? 237.483 206.766 170.229 1.00 124.33 ? 111  LEU   A CA   1 
ATOM   789  C C    . LEU   A 1 98  ? 237.860 208.236 170.085 1.00 127.97 ? 111  LEU   A C    1 
ATOM   790  O O    . LEU   A 1 98  ? 237.000 209.102 170.159 1.00 128.74 ? 111  LEU   A O    1 
ATOM   791  C CB   . LEU   A 1 98  ? 237.063 206.226 168.852 1.00 121.20 ? 111  LEU   A CB   1 
ATOM   792  C CG   . LEU   A 1 98  ? 236.638 204.758 168.839 1.00 124.20 ? 111  LEU   A CG   1 
ATOM   793  C CD1  . LEU   A 1 98  ? 236.257 204.355 167.423 1.00 122.61 ? 111  LEU   A CD1  1 
ATOM   794  C CD2  . LEU   A 1 98  ? 237.755 203.846 169.318 1.00 123.71 ? 111  LEU   A CD2  1 
ATOM   795  N N    . TYR   A 1 99  ? 239.128 208.523 169.821 1.00 135.15 ? 112  TYR   A N    1 
ATOM   796  C CA   . TYR   A 1 99  ? 239.615 209.886 169.632 1.00 135.04 ? 112  TYR   A CA   1 
ATOM   797  C C    . TYR   A 1 99  ? 240.171 210.057 168.219 1.00 136.32 ? 112  TYR   A C    1 
ATOM   798  O O    . TYR   A 1 99  ? 241.026 209.274 167.803 1.00 135.26 ? 112  TYR   A O    1 
ATOM   799  C CB   . TYR   A 1 99  ? 240.638 210.209 170.722 1.00 133.79 ? 112  TYR   A CB   1 
ATOM   800  C CG   . TYR   A 1 99  ? 240.125 209.932 172.120 1.00 135.39 ? 112  TYR   A CG   1 
ATOM   801  C CD1  . TYR   A 1 99  ? 239.366 210.898 172.801 1.00 135.20 ? 112  TYR   A CD1  1 
ATOM   802  C CD2  . TYR   A 1 99  ? 240.373 208.684 172.720 1.00 133.61 ? 112  TYR   A CD2  1 
ATOM   803  C CE1  . TYR   A 1 99  ? 238.856 210.616 174.079 1.00 133.70 ? 112  TYR   A CE1  1 
ATOM   804  C CE2  . TYR   A 1 99  ? 239.858 208.398 173.994 1.00 133.86 ? 112  TYR   A CE2  1 
ATOM   805  C CZ   . TYR   A 1 99  ? 239.094 209.363 174.675 1.00 134.38 ? 112  TYR   A CZ   1 
ATOM   806  O OH   . TYR   A 1 99  ? 238.583 209.085 175.902 1.00 134.05 ? 112  TYR   A OH   1 
ATOM   807  N N    . VAL   A 1 100 ? 239.676 211.037 167.462 1.00 138.80 ? 113  VAL   A N    1 
ATOM   808  C CA   . VAL   A 1 100 ? 240.142 211.292 166.082 1.00 139.12 ? 113  VAL   A CA   1 
ATOM   809  C C    . VAL   A 1 100 ? 241.295 212.296 166.083 1.00 141.03 ? 113  VAL   A C    1 
ATOM   810  O O    . VAL   A 1 100 ? 242.404 211.966 165.672 1.00 139.09 ? 113  VAL   A O    1 
ATOM   811  C CB   . VAL   A 1 100 ? 238.984 211.708 165.163 1.00 137.61 ? 113  VAL   A CB   1 
ATOM   812  C CG1  . VAL   A 1 100 ? 239.460 212.028 163.745 1.00 136.63 ? 113  VAL   A CG1  1 
ATOM   813  C CG2  . VAL   A 1 100 ? 237.954 210.580 165.047 1.00 136.63 ? 113  VAL   A CG2  1 
ATOM   814  N N    . ASN   A 1 101 ? 241.062 213.493 166.619 1.00 143.67 ? 114  ASN   A N    1 
ATOM   815  C CA   . ASN   A 1 101 ? 242.120 214.363 167.135 1.00 142.45 ? 114  ASN   A CA   1 
ATOM   816  C C    . ASN   A 1 101 ? 242.114 214.242 168.667 1.00 139.99 ? 114  ASN   A C    1 
ATOM   817  O O    . ASN   A 1 101 ? 242.102 213.130 169.195 1.00 138.53 ? 114  ASN   A O    1 
ATOM   818  C CB   . ASN   A 1 101 ? 241.925 215.784 166.568 1.00 141.80 ? 114  ASN   A CB   1 
ATOM   819  C CG   . ASN   A 1 101 ? 242.138 215.832 165.063 1.00 142.63 ? 114  ASN   A CG   1 
ATOM   820  O OD1  . ASN   A 1 101 ? 243.186 215.471 164.550 1.00 140.54 ? 114  ASN   A OD1  1 
ATOM   821  N ND2  . ASN   A 1 101 ? 241.167 216.289 164.308 1.00 139.51 ? 114  ASN   A ND2  1 
ATOM   822  N N    . LYS   A 1 102 ? 242.052 215.352 169.407 1.00 142.51 ? 115  LYS   A N    1 
ATOM   823  C CA   . LYS   A 1 102 ? 241.700 215.333 170.838 1.00 145.36 ? 115  LYS   A CA   1 
ATOM   824  C C    . LYS   A 1 102 ? 240.205 215.063 171.082 1.00 145.75 ? 115  LYS   A C    1 
ATOM   825  O O    . LYS   A 1 102 ? 239.823 214.707 172.193 1.00 144.59 ? 115  LYS   A O    1 
ATOM   826  C CB   . LYS   A 1 102 ? 242.115 216.665 171.485 1.00 144.23 ? 115  LYS   A CB   1 
ATOM   827  C CG   . LYS   A 1 102 ? 243.614 216.993 171.378 1.00 143.41 ? 115  LYS   A CG   1 
ATOM   828  C CD   . LYS   A 1 102 ? 244.560 215.943 171.978 1.00 143.16 ? 115  LYS   A CD   1 
ATOM   829  C CE   . LYS   A 1 102 ? 244.290 215.727 173.470 1.00 143.21 ? 115  LYS   A CE   1 
ATOM   830  N NZ   . LYS   A 1 102 ? 245.288 214.823 174.080 1.00 143.09 ? 115  LYS   A NZ   1 
ATOM   831  N N    . THR   A 1 103 ? 239.355 215.250 170.071 1.00 141.00 ? 116  THR   A N    1 
ATOM   832  C CA   . THR   A 1 103 ? 237.890 215.103 170.144 1.00 139.36 ? 116  THR   A CA   1 
ATOM   833  C C    . THR   A 1 103 ? 237.439 213.653 170.310 1.00 138.78 ? 116  THR   A C    1 
ATOM   834  O O    . THR   A 1 103 ? 237.896 212.761 169.595 1.00 135.24 ? 116  THR   A O    1 
ATOM   835  C CB   . THR   A 1 103 ? 237.216 215.694 168.901 1.00 138.28 ? 116  THR   A CB   1 
ATOM   836  O OG1  . THR   A 1 103 ? 237.886 215.306 167.720 1.00 138.65 ? 116  THR   A OG1  1 
ATOM   837  C CG2  . THR   A 1 103 ? 237.223 217.218 168.938 1.00 136.59 ? 116  THR   A CG2  1 
ATOM   838  N N    . LEU   A 1 104 ? 236.518 213.428 171.247 1.00 133.44 ? 117  LEU   A N    1 
ATOM   839  C CA   . LEU   A 1 104 ? 235.915 212.131 171.553 1.00 132.92 ? 117  LEU   A CA   1 
ATOM   840  C C    . LEU   A 1 104 ? 234.749 211.794 170.613 1.00 133.10 ? 117  LEU   A C    1 
ATOM   841  O O    . LEU   A 1 104 ? 233.918 212.646 170.305 1.00 130.92 ? 117  LEU   A O    1 
ATOM   842  C CB   . LEU   A 1 104 ? 235.450 212.157 173.021 1.00 130.20 ? 117  LEU   A CB   1 
ATOM   843  C CG   . LEU   A 1 104 ? 234.608 210.953 173.476 1.00 130.09 ? 117  LEU   A CG   1 
ATOM   844  C CD1  . LEU   A 1 104 ? 235.376 209.645 173.399 1.00 128.37 ? 117  LEU   A CD1  1 
ATOM   845  C CD2  . LEU   A 1 104 ? 234.175 211.135 174.924 1.00 129.49 ? 117  LEU   A CD2  1 
ATOM   846  N N    . TYR   A 1 105 ? 234.633 210.523 170.248 1.00 133.36 ? 118  TYR   A N    1 
ATOM   847  C CA   . TYR   A 1 105 ? 233.513 209.929 169.533 1.00 131.34 ? 118  TYR   A CA   1 
ATOM   848  C C    . TYR   A 1 105 ? 233.063 208.623 170.190 1.00 130.92 ? 118  TYR   A C    1 
ATOM   849  O O    . TYR   A 1 105 ? 233.873 207.870 170.723 1.00 129.47 ? 118  TYR   A O    1 
ATOM   850  C CB   . TYR   A 1 105 ? 233.885 209.650 168.082 1.00 129.11 ? 118  TYR   A CB   1 
ATOM   851  C CG   . TYR   A 1 105 ? 234.183 210.865 167.231 1.00 131.73 ? 118  TYR   A CG   1 
ATOM   852  C CD1  . TYR   A 1 105 ? 235.404 211.542 167.375 1.00 133.51 ? 118  TYR   A CD1  1 
ATOM   853  C CD2  . TYR   A 1 105 ? 233.238 211.317 166.292 1.00 130.24 ? 118  TYR   A CD2  1 
ATOM   854  C CE1  . TYR   A 1 105 ? 235.665 212.693 166.614 1.00 135.23 ? 118  TYR   A CE1  1 
ATOM   855  C CE2  . TYR   A 1 105 ? 233.499 212.460 165.518 1.00 131.36 ? 118  TYR   A CE2  1 
ATOM   856  C CZ   . TYR   A 1 105 ? 234.714 213.156 165.686 1.00 135.50 ? 118  TYR   A CZ   1 
ATOM   857  O OH   . TYR   A 1 105 ? 234.966 214.275 164.962 1.00 134.41 ? 118  TYR   A OH   1 
ATOM   858  N N    . SER   A 1 106 ? 231.768 208.338 170.120 1.00 117.52 ? 119  SER   A N    1 
ATOM   859  C CA   . SER   A 1 106 ? 231.121 207.146 170.659 1.00 114.52 ? 119  SER   A CA   1 
ATOM   860  C C    . SER   A 1 106 ? 230.640 206.223 169.540 1.00 114.30 ? 119  SER   A C    1 
ATOM   861  O O    . SER   A 1 106 ? 229.889 206.648 168.665 1.00 113.46 ? 119  SER   A O    1 
ATOM   862  C CB   . SER   A 1 106 ? 229.951 207.605 171.529 1.00 116.44 ? 119  SER   A CB   1 
ATOM   863  O OG   . SER   A 1 106 ? 229.032 206.571 171.772 1.00 120.58 ? 119  SER   A OG   1 
ATOM   864  N N    . GLU   A 1 107 ? 231.037 204.954 169.584 1.00 116.76 ? 120  GLU   A N    1 
ATOM   865  C CA   . GLU   A 1 107 ? 230.576 203.885 168.692 1.00 117.34 ? 120  GLU   A CA   1 
ATOM   866  C C    . GLU   A 1 107 ? 230.073 202.695 169.525 1.00 118.05 ? 120  GLU   A C    1 
ATOM   867  O O    . GLU   A 1 107 ? 230.656 202.385 170.556 1.00 121.87 ? 120  GLU   A O    1 
ATOM   868  C CB   . GLU   A 1 107 ? 231.725 203.404 167.776 1.00 117.33 ? 120  GLU   A CB   1 
ATOM   869  C CG   . GLU   A 1 107 ? 232.469 204.457 166.930 1.00 122.94 ? 120  GLU   A CG   1 
ATOM   870  C CD   . GLU   A 1 107 ? 231.697 205.014 165.710 1.00 125.44 ? 120  GLU   A CD   1 
ATOM   871  O OE1  . GLU   A 1 107 ? 230.493 204.720 165.558 1.00 124.52 ? 120  GLU   A OE1  1 
ATOM   872  O OE2  . GLU   A 1 107 ? 232.319 205.740 164.887 1.00 126.71 ? 120  GLU   A OE2  1 
ATOM   873  N N    . PHE   A 1 108 ? 229.041 201.978 169.084 1.00 92.45  ? 121  PHE   A N    1 
ATOM   874  C CA   . PHE   A 1 108 ? 228.720 200.626 169.561 1.00 91.34  ? 121  PHE   A CA   1 
ATOM   875  C C    . PHE   A 1 108 ? 227.815 199.902 168.558 1.00 90.18  ? 121  PHE   A C    1 
ATOM   876  O O    . PHE   A 1 108 ? 227.300 200.518 167.629 1.00 93.40  ? 121  PHE   A O    1 
ATOM   877  C CB   . PHE   A 1 108 ? 228.129 200.628 170.979 1.00 89.11  ? 121  PHE   A CB   1 
ATOM   878  C CG   . PHE   A 1 108 ? 226.853 201.406 171.218 1.00 87.69  ? 121  PHE   A CG   1 
ATOM   879  C CD1  . PHE   A 1 108 ? 225.606 200.828 170.932 1.00 89.45  ? 121  PHE   A CD1  1 
ATOM   880  C CD2  . PHE   A 1 108 ? 226.905 202.670 171.824 1.00 91.38  ? 121  PHE   A CD2  1 
ATOM   881  C CE1  . PHE   A 1 108 ? 224.420 201.510 171.241 1.00 91.72  ? 121  PHE   A CE1  1 
ATOM   882  C CE2  . PHE   A 1 108 ? 225.722 203.344 172.147 1.00 91.83  ? 121  PHE   A CE2  1 
ATOM   883  C CZ   . PHE   A 1 108 ? 224.482 202.764 171.857 1.00 89.00  ? 121  PHE   A CZ   1 
ATOM   884  N N    . SER   A 1 109 ? 227.654 198.586 168.685 1.00 84.53  ? 122  SER   A N    1 
ATOM   885  C CA   . SER   A 1 109 ? 226.909 197.794 167.706 1.00 87.74  ? 122  SER   A CA   1 
ATOM   886  C C    . SER   A 1 109 ? 225.423 198.149 167.642 1.00 89.92  ? 122  SER   A C    1 
ATOM   887  O O    . SER   A 1 109 ? 224.745 198.250 168.658 1.00 92.80  ? 122  SER   A O    1 
ATOM   888  C CB   . SER   A 1 109 ? 227.035 196.301 167.999 1.00 88.90  ? 122  SER   A CB   1 
ATOM   889  O OG   . SER   A 1 109 ? 228.380 195.872 167.961 1.00 95.96  ? 122  SER   A OG   1 
ATOM   890  N N    . THR   A 1 110 ? 224.886 198.246 166.430 1.00 86.54  ? 123  THR   A N    1 
ATOM   891  C CA   . THR   A 1 110 ? 223.443 198.288 166.176 1.00 83.11  ? 123  THR   A CA   1 
ATOM   892  C C    . THR   A 1 110 ? 222.817 196.934 166.468 1.00 82.52  ? 123  THR   A C    1 
ATOM   893  O O    . THR   A 1 110 ? 223.373 195.911 166.082 1.00 90.99  ? 123  THR   A O    1 
ATOM   894  C CB   . THR   A 1 110 ? 223.191 198.647 164.712 1.00 85.12  ? 123  THR   A CB   1 
ATOM   895  O OG1  . THR   A 1 110 ? 223.626 199.955 164.493 1.00 93.01  ? 123  THR   A OG1  1 
ATOM   896  C CG2  . THR   A 1 110 ? 221.745 198.597 164.234 1.00 82.39  ? 123  THR   A CG2  1 
ATOM   897  N N    . ILE   A 1 111 ? 221.632 196.902 167.066 1.00 69.43  ? 124  ILE   A N    1 
ATOM   898  C CA   . ILE   A 1 111 ? 220.822 195.687 167.188 1.00 65.60  ? 124  ILE   A CA   1 
ATOM   899  C C    . ILE   A 1 111 ? 219.595 195.792 166.289 1.00 71.91  ? 124  ILE   A C    1 
ATOM   900  O O    . ILE   A 1 111 ? 218.987 196.854 166.187 1.00 81.43  ? 124  ILE   A O    1 
ATOM   901  C CB   . ILE   A 1 111 ? 220.489 195.372 168.659 1.00 68.18  ? 124  ILE   A CB   1 
ATOM   902  C CG1  . ILE   A 1 111 ? 219.733 194.039 168.770 1.00 69.64  ? 124  ILE   A CG1  1 
ATOM   903  C CG2  . ILE   A 1 111 ? 219.690 196.498 169.317 1.00 68.66  ? 124  ILE   A CG2  1 
ATOM   904  C CD1  . ILE   A 1 111 ? 219.631 193.511 170.198 1.00 72.57  ? 124  ILE   A CD1  1 
ATOM   905  N N    . VAL   A 1 112 ? 219.237 194.695 165.628 1.00 71.44  ? 125  VAL   A N    1 
ATOM   906  C CA   . VAL   A 1 112 ? 217.989 194.565 164.877 1.00 65.76  ? 125  VAL   A CA   1 
ATOM   907  C C    . VAL   A 1 112 ? 217.135 193.481 165.509 1.00 66.74  ? 125  VAL   A C    1 
ATOM   908  O O    . VAL   A 1 112 ? 217.646 192.446 165.920 1.00 78.97  ? 125  VAL   A O    1 
ATOM   909  C CB   . VAL   A 1 112 ? 218.215 194.332 163.378 1.00 67.96  ? 125  VAL   A CB   1 
ATOM   910  C CG1  . VAL   A 1 112 ? 219.122 195.419 162.810 1.00 68.58  ? 125  VAL   A CG1  1 
ATOM   911  C CG2  . VAL   A 1 112 ? 218.831 192.984 163.017 1.00 70.98  ? 125  VAL   A CG2  1 
ATOM   912  N N    . ILE   A 1 113 ? 215.833 193.703 165.608 1.00 64.64  ? 126  ILE   A N    1 
ATOM   913  C CA   . ILE   A 1 113 ? 214.873 192.767 166.195 1.00 65.31  ? 126  ILE   A CA   1 
ATOM   914  C C    . ILE   A 1 113 ? 213.714 192.630 165.214 1.00 71.79  ? 126  ILE   A C    1 
ATOM   915  O O    . ILE   A 1 113 ? 213.234 193.628 164.685 1.00 82.74  ? 126  ILE   A O    1 
ATOM   916  C CB   . ILE   A 1 113 ? 214.392 193.258 167.578 1.00 64.74  ? 126  ILE   A CB   1 
ATOM   917  C CG1  . ILE   A 1 113 ? 215.538 193.556 168.568 1.00 69.05  ? 126  ILE   A CG1  1 
ATOM   918  C CG2  . ILE   A 1 113 ? 213.434 192.231 168.188 1.00 66.46  ? 126  ILE   A CG2  1 
ATOM   919  C CD1  . ILE   A 1 113 ? 215.111 194.460 169.720 1.00 67.37  ? 126  ILE   A CD1  1 
ATOM   920  N N    . GLY   A 1 114 ? 213.249 191.423 164.938 1.00 72.68  ? 127  GLY   A N    1 
ATOM   921  C CA   . GLY   A 1 114 ? 212.281 191.187 163.880 1.00 67.00  ? 127  GLY   A CA   1 
ATOM   922  C C    . GLY   A 1 114 ? 211.805 189.749 163.855 1.00 77.55  ? 127  GLY   A C    1 
ATOM   923  O O    . GLY   A 1 114 ? 211.809 189.060 164.870 1.00 85.94  ? 127  GLY   A O    1 
ATOM   924  N N    . SER   A 1 115 ? 211.392 189.281 162.687 1.00 82.17  ? 128  SER   A N    1 
ATOM   925  C CA   . SER   A 1 115 ? 211.011 187.888 162.470 1.00 87.50  ? 128  SER   A CA   1 
ATOM   926  C C    . SER   A 1 115 ? 211.708 187.326 161.240 1.00 91.70  ? 128  SER   A C    1 
ATOM   927  O O    . SER   A 1 115 ? 212.800 186.782 161.351 1.00 95.86  ? 128  SER   A O    1 
ATOM   928  C CB   . SER   A 1 115 ? 209.488 187.747 162.454 1.00 86.30  ? 128  SER   A CB   1 
ATOM   929  O OG   . SER   A 1 115 ? 208.909 188.586 161.472 1.00 81.82  ? 128  SER   A OG   1 
ATOM   930  N N    . VAL   A 1 116 ? 211.126 187.485 160.057 1.00 87.52  ? 129  VAL   A N    1 
ATOM   931  C CA   . VAL   A 1 116 ? 211.710 187.031 158.784 1.00 80.88  ? 129  VAL   A CA   1 
ATOM   932  C C    . VAL   A 1 116 ? 212.684 188.034 158.162 1.00 85.82  ? 129  VAL   A C    1 
ATOM   933  O O    . VAL   A 1 116 ? 213.342 187.698 157.185 1.00 91.55  ? 129  VAL   A O    1 
ATOM   934  C CB   . VAL   A 1 116 ? 210.611 186.636 157.787 1.00 85.15  ? 129  VAL   A CB   1 
ATOM   935  C CG1  . VAL   A 1 116 ? 209.911 185.357 158.243 1.00 83.88  ? 129  VAL   A CG1  1 
ATOM   936  C CG2  . VAL   A 1 116 ? 209.555 187.728 157.594 1.00 88.70  ? 129  VAL   A CG2  1 
ATOM   937  N N    . PHE   A 1 117 ? 212.793 189.249 158.709 1.00 83.55  ? 130  PHE   A N    1 
ATOM   938  C CA   . PHE   A 1 117 ? 213.683 190.316 158.234 1.00 81.91  ? 130  PHE   A CA   1 
ATOM   939  C C    . PHE   A 1 117 ? 213.543 190.619 156.732 1.00 84.63  ? 130  PHE   A C    1 
ATOM   940  O O    . PHE   A 1 117 ? 214.529 190.811 156.027 1.00 89.66  ? 130  PHE   A O    1 
ATOM   941  C CB   . PHE   A 1 117 ? 215.131 190.040 158.653 1.00 82.96  ? 130  PHE   A CB   1 
ATOM   942  C CG   . PHE   A 1 117 ? 215.382 189.975 160.140 1.00 84.77  ? 130  PHE   A CG   1 
ATOM   943  C CD1  . PHE   A 1 117 ? 215.248 191.130 160.925 1.00 82.31  ? 130  PHE   A CD1  1 
ATOM   944  C CD2  . PHE   A 1 117 ? 215.839 188.787 160.730 1.00 83.47  ? 130  PHE   A CD2  1 
ATOM   945  C CE1  . PHE   A 1 117 ? 215.576 191.101 162.285 1.00 80.35  ? 130  PHE   A CE1  1 
ATOM   946  C CE2  . PHE   A 1 117 ? 216.178 188.762 162.088 1.00 84.69  ? 130  PHE   A CE2  1 
ATOM   947  C CZ   . PHE   A 1 117 ? 216.045 189.919 162.869 1.00 82.49  ? 130  PHE   A CZ   1 
ATOM   948  N N    . ILE   A 1 118 ? 212.312 190.691 156.231 1.00 92.42  ? 131  ILE   A N    1 
ATOM   949  C CA   . ILE   A 1 118 ? 212.005 191.120 154.859 1.00 91.39  ? 131  ILE   A CA   1 
ATOM   950  C C    . ILE   A 1 118 ? 210.852 192.126 154.878 1.00 95.13  ? 131  ILE   A C    1 
ATOM   951  O O    . ILE   A 1 118 ? 210.063 192.159 155.821 1.00 96.99  ? 131  ILE   A O    1 
ATOM   952  C CB   . ILE   A 1 118 ? 211.747 189.927 153.913 1.00 88.79  ? 131  ILE   A CB   1 
ATOM   953  C CG1  . ILE   A 1 118 ? 210.612 189.016 154.402 1.00 91.88  ? 131  ILE   A CG1  1 
ATOM   954  C CG2  . ILE   A 1 118 ? 213.028 189.118 153.680 1.00 89.38  ? 131  ILE   A CG2  1 
ATOM   955  C CD1  . ILE   A 1 118 ? 210.013 188.154 153.288 1.00 94.27  ? 131  ILE   A CD1  1 
ATOM   956  N N    . ASN   A 1 119 ? 210.748 192.955 153.844 1.00 92.70  ? 132  ASN   A N    1 
ATOM   957  C CA   . ASN   A 1 119 ? 209.902 194.155 153.818 1.00 92.64  ? 132  ASN   A CA   1 
ATOM   958  C C    . ASN   A 1 119 ? 208.372 193.935 153.796 1.00 94.10  ? 132  ASN   A C    1 
ATOM   959  O O    . ASN   A 1 119 ? 207.632 194.902 153.665 1.00 93.78  ? 132  ASN   A O    1 
ATOM   960  C CB   . ASN   A 1 119 ? 210.367 195.051 152.662 1.00 90.26  ? 132  ASN   A CB   1 
ATOM   961  C CG   . ASN   A 1 119 ? 210.177 194.422 151.298 1.00 97.03  ? 132  ASN   A CG   1 
ATOM   962  O OD1  . ASN   A 1 119 ? 209.249 193.649 151.075 1.00 100.22 ? 132  ASN   A OD1  1 
ATOM   963  N ND2  . ASN   A 1 119 ? 211.098 194.697 150.393 1.00 97.77  ? 132  ASN   A ND2  1 
ATOM   964  N N    . ASN   A 1 120 ? 207.862 192.719 154.004 1.00 92.12  ? 133  ASN   A N    1 
ATOM   965  C CA   . ASN   A 1 120 ? 206.458 192.501 154.389 1.00 89.79  ? 133  ASN   A CA   1 
ATOM   966  C C    . ASN   A 1 120 ? 206.271 192.354 155.915 1.00 99.50  ? 133  ASN   A C    1 
ATOM   967  O O    . ASN   A 1 120 ? 205.174 192.054 156.382 1.00 101.30 ? 133  ASN   A O    1 
ATOM   968  C CB   . ASN   A 1 120 ? 205.860 191.345 153.572 1.00 91.59  ? 133  ASN   A CB   1 
ATOM   969  C CG   . ASN   A 1 120 ? 206.484 189.993 153.844 1.00 99.32  ? 133  ASN   A CG   1 
ATOM   970  O OD1  . ASN   A 1 120 ? 207.165 189.774 154.826 1.00 98.58  ? 133  ASN   A OD1  1 
ATOM   971  N ND2  . ASN   A 1 120 ? 206.280 189.041 152.972 1.00 100.70 ? 133  ASN   A ND2  1 
ATOM   972  N N    . SER   A 1 121 ? 207.332 192.576 156.694 1.00 95.85  ? 134  SER   A N    1 
ATOM   973  C CA   . SER   A 1 121 ? 207.365 192.475 158.153 1.00 91.90  ? 134  SER   A CA   1 
ATOM   974  C C    . SER   A 1 121 ? 208.134 193.640 158.766 1.00 94.18  ? 134  SER   A C    1 
ATOM   975  O O    . SER   A 1 121 ? 209.133 194.090 158.210 1.00 96.05  ? 134  SER   A O    1 
ATOM   976  C CB   . SER   A 1 121 ? 208.004 191.149 158.556 1.00 91.40  ? 134  SER   A CB   1 
ATOM   977  O OG   . SER   A 1 121 ? 209.384 191.148 158.251 1.00 91.63  ? 134  SER   A OG   1 
ATOM   978  N N    . TYR   A 1 122 ? 207.693 194.154 159.908 1.00 88.54  ? 135  TYR   A N    1 
ATOM   979  C CA   . TYR   A 1 122 ? 208.421 195.209 160.607 1.00 86.70  ? 135  TYR   A CA   1 
ATOM   980  C C    . TYR   A 1 122 ? 209.677 194.668 161.288 1.00 85.32  ? 135  TYR   A C    1 
ATOM   981  O O    . TYR   A 1 122 ? 209.643 193.650 161.975 1.00 86.87  ? 135  TYR   A O    1 
ATOM   982  C CB   . TYR   A 1 122 ? 207.509 195.946 161.588 1.00 84.49  ? 135  TYR   A CB   1 
ATOM   983  C CG   . TYR   A 1 122 ? 206.488 196.793 160.870 1.00 85.98  ? 135  TYR   A CG   1 
ATOM   984  C CD1  . TYR   A 1 122 ? 206.845 198.086 160.456 1.00 83.50  ? 135  TYR   A CD1  1 
ATOM   985  C CD2  . TYR   A 1 122 ? 205.218 196.281 160.562 1.00 86.75  ? 135  TYR   A CD2  1 
ATOM   986  C CE1  . TYR   A 1 122 ? 205.935 198.870 159.730 1.00 88.76  ? 135  TYR   A CE1  1 
ATOM   987  C CE2  . TYR   A 1 122 ? 204.293 197.071 159.854 1.00 88.49  ? 135  TYR   A CE2  1 
ATOM   988  C CZ   . TYR   A 1 122 ? 204.651 198.370 159.443 1.00 93.97  ? 135  TYR   A CZ   1 
ATOM   989  O OH   . TYR   A 1 122 ? 203.761 199.155 158.787 1.00 95.64  ? 135  TYR   A OH   1 
ATOM   990  N N    . THR   A 1 123 ? 210.780 195.384 161.117 1.00 76.71  ? 136  THR   A N    1 
ATOM   991  C CA   . THR   A 1 123 ? 212.034 195.197 161.840 1.00 73.76  ? 136  THR   A CA   1 
ATOM   992  C C    . THR   A 1 123 ? 212.262 196.415 162.719 1.00 73.16  ? 136  THR   A C    1 
ATOM   993  O O    . THR   A 1 123 ? 212.233 197.536 162.220 1.00 78.79  ? 136  THR   A O    1 
ATOM   994  C CB   . THR   A 1 123 ? 213.185 195.016 160.848 1.00 73.81  ? 136  THR   A CB   1 
ATOM   995  O OG1  . THR   A 1 123 ? 212.971 193.852 160.090 1.00 82.09  ? 136  THR   A OG1  1 
ATOM   996  C CG2  . THR   A 1 123 ? 214.533 194.868 161.530 1.00 71.08  ? 136  THR   A CG2  1 
ATOM   997  N N    . ILE   A 1 124 ? 212.478 196.229 164.016 1.00 67.11  ? 137  ILE   A N    1 
ATOM   998  C CA   . ILE   A 1 124 ? 212.965 197.288 164.899 1.00 63.89  ? 137  ILE   A CA   1 
ATOM   999  C C    . ILE   A 1 124 ? 214.483 197.377 164.751 1.00 67.73  ? 137  ILE   A C    1 
ATOM   1000 O O    . ILE   A 1 124 ? 215.157 196.351 164.750 1.00 76.05  ? 137  ILE   A O    1 
ATOM   1001 C CB   . ILE   A 1 124 ? 212.572 197.034 166.364 1.00 59.59  ? 137  ILE   A CB   1 
ATOM   1002 C CG1  . ILE   A 1 124 ? 211.095 196.693 166.602 1.00 63.59  ? 137  ILE   A CG1  1 
ATOM   1003 C CG2  . ILE   A 1 124 ? 212.987 198.201 167.265 1.00 62.90  ? 137  ILE   A CG2  1 
ATOM   1004 C CD1  . ILE   A 1 124 ? 210.037 197.627 166.131 1.00 65.85  ? 137  ILE   A CD1  1 
ATOM   1005 N N    . VAL   A 1 125 ? 215.049 198.576 164.661 1.00 71.60  ? 138  VAL   A N    1 
ATOM   1006 C CA   . VAL   A 1 125 ? 216.495 198.810 164.584 1.00 68.16  ? 138  VAL   A CA   1 
ATOM   1007 C C    . VAL   A 1 125 ? 216.881 199.855 165.615 1.00 74.87  ? 138  VAL   A C    1 
ATOM   1008 O O    . VAL   A 1 125 ? 216.240 200.898 165.694 1.00 85.26  ? 138  VAL   A O    1 
ATOM   1009 C CB   . VAL   A 1 125 ? 216.910 199.261 163.176 1.00 66.94  ? 138  VAL   A CB   1 
ATOM   1010 C CG1  . VAL   A 1 125 ? 218.419 199.491 163.085 1.00 65.78  ? 138  VAL   A CG1  1 
ATOM   1011 C CG2  . VAL   A 1 125 ? 216.486 198.240 162.122 1.00 68.19  ? 138  VAL   A CG2  1 
ATOM   1012 N N    . VAL   A 1 126 ? 217.916 199.594 166.406 1.00 72.82  ? 139  VAL   A N    1 
ATOM   1013 C CA   . VAL   A 1 126 ? 218.451 200.534 167.395 1.00 72.68  ? 139  VAL   A CA   1 
ATOM   1014 C C    . VAL   A 1 126 ? 219.915 200.791 167.081 1.00 73.90  ? 139  VAL   A C    1 
ATOM   1015 O O    . VAL   A 1 126 ? 220.730 199.880 167.200 1.00 76.54  ? 139  VAL   A O    1 
ATOM   1016 C CB   . VAL   A 1 126 ? 218.288 199.967 168.812 1.00 72.13  ? 139  VAL   A CB   1 
ATOM   1017 C CG1  . VAL   A 1 126 ? 218.914 200.865 169.876 1.00 70.82  ? 139  VAL   A CG1  1 
ATOM   1018 C CG2  . VAL   A 1 126 ? 216.820 199.743 169.162 1.00 68.75  ? 139  VAL   A CG2  1 
ATOM   1019 N N    . GLN   A 1 127 ? 220.258 202.018 166.692 1.00 87.80  ? 140  GLN   A N    1 
ATOM   1020 C CA   . GLN   A 1 127 ? 221.578 202.378 166.172 1.00 87.78  ? 140  GLN   A CA   1 
ATOM   1021 C C    . GLN   A 1 127 ? 222.108 203.663 166.818 1.00 91.43  ? 140  GLN   A C    1 
ATOM   1022 O O    . GLN   A 1 127 ? 221.407 204.670 166.824 1.00 95.90  ? 140  GLN   A O    1 
ATOM   1023 C CB   . GLN   A 1 127 ? 221.462 202.541 164.650 1.00 88.15  ? 140  GLN   A CB   1 
ATOM   1024 C CG   . GLN   A 1 127 ? 222.747 203.077 164.005 1.00 91.74  ? 140  GLN   A CG   1 
ATOM   1025 C CD   . GLN   A 1 127 ? 222.767 202.905 162.495 1.00 94.79  ? 140  GLN   A CD   1 
ATOM   1026 O OE1  . GLN   A 1 127 ? 221.753 202.744 161.840 1.00 94.69  ? 140  GLN   A OE1  1 
ATOM   1027 N NE2  . GLN   A 1 127 ? 223.926 202.923 161.886 1.00 94.78  ? 140  GLN   A NE2  1 
ATOM   1028 N N    . PRO   A 1 128 ? 223.351 203.699 167.313 1.00 94.12  ? 141  PRO   A N    1 
ATOM   1029 C CA   . PRO   A 1 128 ? 223.975 204.925 167.783 1.00 95.22  ? 141  PRO   A CA   1 
ATOM   1030 C C    . PRO   A 1 128 ? 224.560 205.759 166.643 1.00 99.23  ? 141  PRO   A C    1 
ATOM   1031 O O    . PRO   A 1 128 ? 225.075 205.232 165.660 1.00 95.69  ? 141  PRO   A O    1 
ATOM   1032 C CB   . PRO   A 1 128 ? 225.071 204.463 168.726 1.00 91.88  ? 141  PRO   A CB   1 
ATOM   1033 C CG   . PRO   A 1 128 ? 225.523 203.157 168.085 1.00 93.58  ? 141  PRO   A CG   1 
ATOM   1034 C CD   . PRO   A 1 128 ? 224.231 202.571 167.536 1.00 91.71  ? 141  PRO   A CD   1 
ATOM   1035 N N    . HIS   A 1 129 ? 224.571 207.071 166.833 1.00 103.96 ? 142  HIS   A N    1 
ATOM   1036 C CA   . HIS   A 1 129 ? 225.197 208.079 165.979 1.00 98.64  ? 142  HIS   A CA   1 
ATOM   1037 C C    . HIS   A 1 129 ? 225.896 209.119 166.855 1.00 100.87 ? 142  HIS   A C    1 
ATOM   1038 O O    . HIS   A 1 129 ? 225.486 210.273 166.928 1.00 99.32  ? 142  HIS   A O    1 
ATOM   1039 C CB   . HIS   A 1 129 ? 224.149 208.723 165.064 1.00 95.70  ? 142  HIS   A CB   1 
ATOM   1040 C CG   . HIS   A 1 129 ? 223.482 207.787 164.101 1.00 99.24  ? 142  HIS   A CG   1 
ATOM   1041 N ND1  . HIS   A 1 129 ? 224.058 207.257 162.945 1.00 101.44 ? 142  HIS   A ND1  1 
ATOM   1042 C CD2  . HIS   A 1 129 ? 222.175 207.437 164.147 1.00 98.71  ? 142  HIS   A CD2  1 
ATOM   1043 C CE1  . HIS   A 1 129 ? 223.070 206.596 162.324 1.00 99.85  ? 142  HIS   A CE1  1 
ATOM   1044 N NE2  . HIS   A 1 129 ? 221.931 206.698 163.019 1.00 99.13  ? 142  HIS   A NE2  1 
ATOM   1045 N N    . ASN   A 1 130 ? 226.933 208.694 167.576 1.00 110.82 ? 143  ASN   A N    1 
ATOM   1046 C CA   . ASN   A 1 130 ? 227.777 209.552 168.402 1.00 112.56 ? 143  ASN   A CA   1 
ATOM   1047 C C    . ASN   A 1 130 ? 227.001 210.463 169.377 1.00 112.83 ? 143  ASN   A C    1 
ATOM   1048 O O    . ASN   A 1 130 ? 227.063 211.686 169.293 1.00 114.68 ? 143  ASN   A O    1 
ATOM   1049 C CB   . ASN   A 1 130 ? 228.743 210.308 167.481 1.00 111.76 ? 143  ASN   A CB   1 
ATOM   1050 C CG   . ASN   A 1 130 ? 229.774 211.072 168.275 1.00 113.51 ? 143  ASN   A CG   1 
ATOM   1051 O OD1  . ASN   A 1 130 ? 230.226 210.620 169.311 1.00 114.53 ? 143  ASN   A OD1  1 
ATOM   1052 N ND2  . ASN   A 1 130 ? 230.187 212.227 167.822 1.00 110.08 ? 143  ASN   A ND2  1 
ATOM   1053 N N    . GLY   A 1 131 ? 226.247 209.872 170.304 1.00 103.04 ? 144  GLY   A N    1 
ATOM   1054 C CA   . GLY   A 1 131 ? 225.486 210.588 171.339 1.00 103.31 ? 144  GLY   A CA   1 
ATOM   1055 C C    . GLY   A 1 131 ? 224.000 210.749 171.045 1.00 103.72 ? 144  GLY   A C    1 
ATOM   1056 O O    . GLY   A 1 131 ? 223.223 211.056 171.943 1.00 103.45 ? 144  GLY   A O    1 
ATOM   1057 N N    . VAL   A 1 132 ? 223.588 210.479 169.813 1.00 95.57  ? 145  VAL   A N    1 
ATOM   1058 C CA   . VAL   A 1 132 ? 222.193 210.302 169.423 1.00 98.64  ? 145  VAL   A CA   1 
ATOM   1059 C C    . VAL   A 1 132 ? 221.941 208.817 169.209 1.00 99.67  ? 145  VAL   A C    1 
ATOM   1060 O O    . VAL   A 1 132 ? 222.701 208.158 168.513 1.00 99.88  ? 145  VAL   A O    1 
ATOM   1061 C CB   . VAL   A 1 132 ? 221.886 211.108 168.153 1.00 96.89  ? 145  VAL   A CB   1 
ATOM   1062 C CG1  . VAL   A 1 132 ? 220.494 210.808 167.605 1.00 95.82  ? 145  VAL   A CG1  1 
ATOM   1063 C CG2  . VAL   A 1 132 ? 221.960 212.606 168.449 1.00 94.93  ? 145  VAL   A CG2  1 
ATOM   1064 N N    . LEU   A 1 133 ? 220.886 208.278 169.794 1.00 92.29  ? 146  LEU   A N    1 
ATOM   1065 C CA   . LEU   A 1 133 ? 220.426 206.918 169.571 1.00 90.44  ? 146  LEU   A CA   1 
ATOM   1066 C C    . LEU   A 1 133 ? 219.217 206.955 168.646 1.00 90.91  ? 146  LEU   A C    1 
ATOM   1067 O O    . LEU   A 1 133 ? 218.141 207.379 169.060 1.00 94.71  ? 146  LEU   A O    1 
ATOM   1068 C CB   . LEU   A 1 133 ? 220.085 206.329 170.937 1.00 92.67  ? 146  LEU   A CB   1 
ATOM   1069 C CG   . LEU   A 1 133 ? 219.691 204.856 170.864 1.00 93.84  ? 146  LEU   A CG   1 
ATOM   1070 C CD1  . LEU   A 1 133 ? 220.931 203.976 170.798 1.00 87.79  ? 146  LEU   A CD1  1 
ATOM   1071 C CD2  . LEU   A 1 133 ? 218.922 204.494 172.126 1.00 92.27  ? 146  LEU   A CD2  1 
ATOM   1072 N N    . GLU   A 1 134 ? 219.381 206.540 167.399 1.00 93.41  ? 147  GLU   A N    1 
ATOM   1073 C CA   . GLU   A 1 134 ? 218.285 206.447 166.440 1.00 95.18  ? 147  GLU   A CA   1 
ATOM   1074 C C    . GLU   A 1 134 ? 217.568 205.112 166.599 1.00 91.40  ? 147  GLU   A C    1 
ATOM   1075 O O    . GLU   A 1 134 ? 218.196 204.056 166.554 1.00 93.24  ? 147  GLU   A O    1 
ATOM   1076 C CB   . GLU   A 1 134 ? 218.796 206.630 165.004 1.00 94.52  ? 147  GLU   A CB   1 
ATOM   1077 C CG   . GLU   A 1 134 ? 217.693 206.409 163.956 1.00 99.88  ? 147  GLU   A CG   1 
ATOM   1078 C CD   . GLU   A 1 134 ? 218.151 206.687 162.518 1.00 106.04 ? 147  GLU   A CD   1 
ATOM   1079 O OE1  . GLU   A 1 134 ? 219.331 206.441 162.191 1.00 103.31 ? 147  GLU   A OE1  1 
ATOM   1080 O OE2  . GLU   A 1 134 ? 217.317 207.105 161.688 1.00 104.40 ? 147  GLU   A OE2  1 
ATOM   1081 N N    . ILE   A 1 135 ? 216.246 205.159 166.730 1.00 78.26  ? 148  ILE   A N    1 
ATOM   1082 C CA   . ILE   A 1 135 ? 215.413 203.968 166.814 1.00 78.22  ? 148  ILE   A CA   1 
ATOM   1083 C C    . ILE   A 1 135 ? 214.292 204.047 165.806 1.00 82.96  ? 148  ILE   A C    1 
ATOM   1084 O O    . ILE   A 1 135 ? 213.595 205.056 165.697 1.00 90.39  ? 148  ILE   A O    1 
ATOM   1085 C CB   . ILE   A 1 135 ? 214.850 203.770 168.221 1.00 82.58  ? 148  ILE   A CB   1 
ATOM   1086 C CG1  . ILE   A 1 135 ? 215.998 203.714 169.241 1.00 81.59  ? 148  ILE   A CG1  1 
ATOM   1087 C CG2  . ILE   A 1 135 ? 213.978 202.507 168.266 1.00 78.72  ? 148  ILE   A CG2  1 
ATOM   1088 C CD1  . ILE   A 1 135 ? 215.551 203.375 170.660 1.00 80.26  ? 148  ILE   A CD1  1 
ATOM   1089 N N    . THR   A 1 136 ? 214.071 202.949 165.105 1.00 83.98  ? 149  THR   A N    1 
ATOM   1090 C CA   . THR   A 1 136 ? 213.040 202.840 164.083 1.00 81.97  ? 149  THR   A CA   1 
ATOM   1091 C C    . THR   A 1 136 ? 212.377 201.478 164.120 1.00 81.97  ? 149  THR   A C    1 
ATOM   1092 O O    . THR   A 1 136 ? 212.940 200.515 164.621 1.00 91.40  ? 149  THR   A O    1 
ATOM   1093 C CB   . THR   A 1 136 ? 213.629 203.080 162.694 1.00 82.23  ? 149  THR   A CB   1 
ATOM   1094 O OG1  . THR   A 1 136 ? 214.665 202.180 162.428 1.00 82.37  ? 149  THR   A OG1  1 
ATOM   1095 C CG2  . THR   A 1 136 ? 214.193 204.479 162.510 1.00 81.88  ? 149  THR   A CG2  1 
ATOM   1096 N N    . ALA   A 1 137 ? 211.172 201.391 163.582 1.00 77.66  ? 150  ALA   A N    1 
ATOM   1097 C CA   . ALA   A 1 137 ? 210.430 200.162 163.396 1.00 79.32  ? 150  ALA   A CA   1 
ATOM   1098 C C    . ALA   A 1 137 ? 209.792 200.229 162.021 1.00 86.69  ? 150  ALA   A C    1 
ATOM   1099 O O    . ALA   A 1 137 ? 208.752 200.862 161.852 1.00 95.08  ? 150  ALA   A O    1 
ATOM   1100 C CB   . ALA   A 1 137 ? 209.370 200.070 164.477 1.00 77.68  ? 150  ALA   A CB   1 
ATOM   1101 N N    . CYS   A 1 138 ? 210.430 199.627 161.031 1.00 89.93  ? 151  CYS   A N    1 
ATOM   1102 C CA   . CYS   A 1 138 ? 210.061 199.840 159.643 1.00 85.09  ? 151  CYS   A CA   1 
ATOM   1103 C C    . CYS   A 1 138 ? 210.066 198.549 158.850 1.00 90.00  ? 151  CYS   A C    1 
ATOM   1104 O O    . CYS   A 1 138 ? 210.705 197.571 159.229 1.00 99.63  ? 151  CYS   A O    1 
ATOM   1105 C CB   . CYS   A 1 138 ? 211.005 200.846 158.987 1.00 89.88  ? 151  CYS   A CB   1 
ATOM   1106 S SG   . CYS   A 1 138 ? 211.264 202.409 159.853 1.00 111.66 ? 151  CYS   A SG   1 
ATOM   1107 N N    . GLN   A 1 139 ? 209.387 198.545 157.716 1.00 94.05  ? 152  GLN   A N    1 
ATOM   1108 C CA   . GLN   A 1 139 ? 209.425 197.450 156.757 1.00 91.05  ? 152  GLN   A CA   1 
ATOM   1109 C C    . GLN   A 1 139 ? 210.731 197.453 155.943 1.00 93.93  ? 152  GLN   A C    1 
ATOM   1110 O O    . GLN   A 1 139 ? 210.711 197.495 154.719 1.00 100.84 ? 152  GLN   A O    1 
ATOM   1111 C CB   . GLN   A 1 139 ? 208.158 197.480 155.902 1.00 90.55  ? 152  GLN   A CB   1 
ATOM   1112 C CG   . GLN   A 1 139 ? 206.904 197.309 156.766 1.00 92.52  ? 152  GLN   A CG   1 
ATOM   1113 C CD   . GLN   A 1 139 ? 205.682 196.801 156.016 1.00 96.38  ? 152  GLN   A CD   1 
ATOM   1114 O OE1  . GLN   A 1 139 ? 205.525 196.950 154.816 1.00 95.34  ? 152  GLN   A OE1  1 
ATOM   1115 N NE2  . GLN   A 1 139 ? 204.747 196.194 156.707 1.00 97.14  ? 152  GLN   A NE2  1 
ATOM   1116 N N    . TYR   A 1 140 ? 211.877 197.445 156.616 1.00 91.14  ? 153  TYR   A N    1 
ATOM   1117 C CA   . TYR   A 1 140 ? 213.188 197.482 155.971 1.00 88.05  ? 153  TYR   A CA   1 
ATOM   1118 C C    . TYR   A 1 140 ? 213.425 196.306 155.034 1.00 91.93  ? 153  TYR   A C    1 
ATOM   1119 O O    . TYR   A 1 140 ? 213.219 195.149 155.398 1.00 93.09  ? 153  TYR   A O    1 
ATOM   1120 C CB   . TYR   A 1 140 ? 214.302 197.500 157.023 1.00 89.70  ? 153  TYR   A CB   1 
ATOM   1121 C CG   . TYR   A 1 140 ? 214.436 198.812 157.752 1.00 86.90  ? 153  TYR   A CG   1 
ATOM   1122 C CD1  . TYR   A 1 140 ? 214.797 199.956 157.030 1.00 90.15  ? 153  TYR   A CD1  1 
ATOM   1123 C CD2  . TYR   A 1 140 ? 214.236 198.894 159.138 1.00 86.67  ? 153  TYR   A CD2  1 
ATOM   1124 C CE1  . TYR   A 1 140 ? 214.954 201.188 157.682 1.00 91.42  ? 153  TYR   A CE1  1 
ATOM   1125 C CE2  . TYR   A 1 140 ? 214.399 200.122 159.798 1.00 89.00  ? 153  TYR   A CE2  1 
ATOM   1126 C CZ   . TYR   A 1 140 ? 214.759 201.270 159.071 1.00 92.19  ? 153  TYR   A CZ   1 
ATOM   1127 O OH   . TYR   A 1 140 ? 214.930 202.455 159.705 1.00 95.74  ? 153  TYR   A OH   1 
ATOM   1128 N N    . THR   A 1 141 ? 213.961 196.586 153.851 1.00 102.00 ? 154  THR   A N    1 
ATOM   1129 C CA   . THR   A 1 141 ? 214.520 195.568 152.965 1.00 101.18 ? 154  THR   A CA   1 
ATOM   1130 C C    . THR   A 1 141 ? 215.923 195.230 153.447 1.00 100.83 ? 154  THR   A C    1 
ATOM   1131 O O    . THR   A 1 141 ? 216.908 195.762 152.943 1.00 103.77 ? 154  THR   A O    1 
ATOM   1132 C CB   . THR   A 1 141 ? 214.523 196.036 151.503 1.00 104.78 ? 154  THR   A CB   1 
ATOM   1133 O OG1  . THR   A 1 141 ? 213.224 196.416 151.124 1.00 107.22 ? 154  THR   A OG1  1 
ATOM   1134 C CG2  . THR   A 1 141 ? 214.949 194.921 150.549 1.00 103.44 ? 154  THR   A CG2  1 
ATOM   1135 N N    . MET   A 1 142 ? 216.026 194.402 154.485 1.00 96.37  ? 155  MET   A N    1 
ATOM   1136 C CA   . MET   A 1 142 ? 217.307 194.016 155.075 1.00 96.89  ? 155  MET   A CA   1 
ATOM   1137 C C    . MET   A 1 142 ? 218.201 193.266 154.085 1.00 99.61  ? 155  MET   A C    1 
ATOM   1138 O O    . MET   A 1 142 ? 217.735 192.434 153.305 1.00 103.98 ? 155  MET   A O    1 
ATOM   1139 C CB   . MET   A 1 142 ? 217.089 193.143 156.311 1.00 95.74  ? 155  MET   A CB   1 
ATOM   1140 C CG   . MET   A 1 142 ? 216.302 193.828 157.428 1.00 93.37  ? 155  MET   A CG   1 
ATOM   1141 S SD   . MET   A 1 142 ? 217.147 195.188 158.243 1.00 99.71  ? 155  MET   A SD   1 
ATOM   1142 C CE   . MET   A 1 142 ? 218.564 194.338 158.963 1.00 97.12  ? 155  MET   A CE   1 
ATOM   1143 N N    . CYS   A 1 143 ? 219.503 193.513 154.146 1.00 101.44 ? 156  CYS   A N    1 
ATOM   1144 C CA   . CYS   A 1 143 ? 220.489 192.782 153.361 1.00 101.66 ? 156  CYS   A CA   1 
ATOM   1145 C C    . CYS   A 1 143 ? 220.651 191.325 153.823 1.00 105.09 ? 156  CYS   A C    1 
ATOM   1146 O O    . CYS   A 1 143 ? 220.313 190.971 154.949 1.00 109.33 ? 156  CYS   A O    1 
ATOM   1147 C CB   . CYS   A 1 143 ? 221.824 193.518 153.462 1.00 99.44  ? 156  CYS   A CB   1 
ATOM   1148 S SG   . CYS   A 1 143 ? 221.775 195.229 152.891 1.00 124.82 ? 156  CYS   A SG   1 
ATOM   1149 N N    . GLU   A 1 144 ? 221.257 190.477 152.996 1.00 102.48 ? 157  GLU   A N    1 
ATOM   1150 C CA   . GLU   A 1 144 ? 221.706 189.146 153.419 1.00 103.39 ? 157  GLU   A CA   1 
ATOM   1151 C C    . GLU   A 1 144 ? 222.779 189.209 154.511 1.00 106.59 ? 157  GLU   A C    1 
ATOM   1152 O O    . GLU   A 1 144 ? 222.712 188.462 155.487 1.00 104.67 ? 157  GLU   A O    1 
ATOM   1153 C CB   . GLU   A 1 144 ? 222.279 188.381 152.224 1.00 103.04 ? 157  GLU   A CB   1 
ATOM   1154 C CG   . GLU   A 1 144 ? 221.184 187.904 151.273 1.00 104.83 ? 157  GLU   A CG   1 
ATOM   1155 C CD   . GLU   A 1 144 ? 221.756 187.021 150.158 1.00 109.75 ? 157  GLU   A CD   1 
ATOM   1156 O OE1  . GLU   A 1 144 ? 222.777 187.401 149.545 1.00 110.93 ? 157  GLU   A OE1  1 
ATOM   1157 O OE2  . GLU   A 1 144 ? 221.187 185.939 149.889 1.00 108.64 ? 157  GLU   A OE2  1 
ATOM   1158 N N    . TYR   A 1 145 ? 223.736 190.124 154.352 1.00 100.40 ? 158  TYR   A N    1 
ATOM   1159 C CA   . TYR   A 1 145 ? 224.915 190.297 155.200 1.00 98.22  ? 158  TYR   A CA   1 
ATOM   1160 C C    . TYR   A 1 145 ? 225.007 191.735 155.745 1.00 97.93  ? 158  TYR   A C    1 
ATOM   1161 O O    . TYR   A 1 145 ? 225.898 192.493 155.365 1.00 98.07  ? 158  TYR   A O    1 
ATOM   1162 C CB   . TYR   A 1 145 ? 226.168 189.911 154.396 1.00 96.41  ? 158  TYR   A CB   1 
ATOM   1163 C CG   . TYR   A 1 145 ? 226.129 188.560 153.713 1.00 98.20  ? 158  TYR   A CG   1 
ATOM   1164 C CD1  . TYR   A 1 145 ? 225.803 187.405 154.440 1.00 98.74  ? 158  TYR   A CD1  1 
ATOM   1165 C CD2  . TYR   A 1 145 ? 226.437 188.463 152.344 1.00 97.57  ? 158  TYR   A CD2  1 
ATOM   1166 C CE1  . TYR   A 1 145 ? 225.768 186.155 153.803 1.00 98.99  ? 158  TYR   A CE1  1 
ATOM   1167 C CE2  . TYR   A 1 145 ? 226.384 187.216 151.700 1.00 100.82 ? 158  TYR   A CE2  1 
ATOM   1168 C CZ   . TYR   A 1 145 ? 226.036 186.061 152.426 1.00 102.20 ? 158  TYR   A CZ   1 
ATOM   1169 O OH   . TYR   A 1 145 ? 225.965 184.856 151.808 1.00 99.01  ? 158  TYR   A OH   1 
ATOM   1170 N N    . PRO   A 1 146 ? 224.058 192.173 156.587 1.00 96.45  ? 159  PRO   A N    1 
ATOM   1171 C CA   . PRO   A 1 146 ? 223.985 193.551 157.047 1.00 93.34  ? 159  PRO   A CA   1 
ATOM   1172 C C    . PRO   A 1 146 ? 225.150 193.913 157.968 1.00 96.03  ? 159  PRO   A C    1 
ATOM   1173 O O    . PRO   A 1 146 ? 225.601 193.085 158.750 1.00 102.94 ? 159  PRO   A O    1 
ATOM   1174 C CB   . PRO   A 1 146 ? 222.641 193.658 157.767 1.00 90.83  ? 159  PRO   A CB   1 
ATOM   1175 C CG   . PRO   A 1 146 ? 222.395 192.246 158.269 1.00 90.63  ? 159  PRO   A CG   1 
ATOM   1176 C CD   . PRO   A 1 146 ? 222.980 191.391 157.152 1.00 96.93  ? 159  PRO   A CD   1 
ATOM   1177 N N    . HIS   A 1 147 ? 225.629 195.154 157.933 1.00 96.36  ? 160  HIS   A N    1 
ATOM   1178 C CA   . HIS   A 1 147 ? 226.626 195.657 158.877 1.00 94.27  ? 160  HIS   A CA   1 
ATOM   1179 C C    . HIS   A 1 147 ? 226.617 197.188 158.949 1.00 95.48  ? 160  HIS   A C    1 
ATOM   1180 O O    . HIS   A 1 147 ? 226.131 197.870 158.049 1.00 103.69 ? 160  HIS   A O    1 
ATOM   1181 C CB   . HIS   A 1 147 ? 228.017 195.125 158.499 1.00 95.79  ? 160  HIS   A CB   1 
ATOM   1182 C CG   . HIS   A 1 147 ? 228.629 195.783 157.304 1.00 98.56  ? 160  HIS   A CG   1 
ATOM   1183 N ND1  . HIS   A 1 147 ? 229.420 196.900 157.333 1.00 101.76 ? 160  HIS   A ND1  1 
ATOM   1184 C CD2  . HIS   A 1 147 ? 228.484 195.412 155.998 1.00 98.94  ? 160  HIS   A CD2  1 
ATOM   1185 C CE1  . HIS   A 1 147 ? 229.764 197.187 156.074 1.00 102.53 ? 160  HIS   A CE1  1 
ATOM   1186 N NE2  . HIS   A 1 147 ? 229.235 196.296 155.218 1.00 101.43 ? 160  HIS   A NE2  1 
ATOM   1187 N N    . THR   A 1 148 ? 227.190 197.743 160.009 1.00 94.67  ? 161  THR   A N    1 
ATOM   1188 C CA   . THR   A 1 148 ? 227.467 199.180 160.148 1.00 97.35  ? 161  THR   A CA   1 
ATOM   1189 C C    . THR   A 1 148 ? 228.969 199.458 160.085 1.00 103.28 ? 161  THR   A C    1 
ATOM   1190 O O    . THR   A 1 148 ? 229.766 198.566 159.784 1.00 105.61 ? 161  THR   A O    1 
ATOM   1191 C CB   . THR   A 1 148 ? 226.816 199.756 161.411 1.00 99.32  ? 161  THR   A CB   1 
ATOM   1192 O OG1  . THR   A 1 148 ? 227.359 199.193 162.575 1.00 107.36 ? 161  THR   A OG1  1 
ATOM   1193 C CG2  . THR   A 1 148 ? 225.320 199.499 161.445 1.00 97.83  ? 161  THR   A CG2  1 
ATOM   1194 N N    . ILE   A 1 149 ? 229.382 200.704 160.304 1.00 112.50 ? 162  ILE   A N    1 
ATOM   1195 C CA   . ILE   A 1 149 ? 230.777 201.144 160.209 1.00 113.03 ? 162  ILE   A CA   1 
ATOM   1196 C C    . ILE   A 1 149 ? 231.124 202.122 161.329 1.00 113.99 ? 162  ILE   A C    1 
ATOM   1197 O O    . ILE   A 1 149 ? 230.240 202.782 161.867 1.00 115.08 ? 162  ILE   A O    1 
ATOM   1198 C CB   . ILE   A 1 149 ? 231.063 201.785 158.836 1.00 112.56 ? 162  ILE   A CB   1 
ATOM   1199 C CG1  . ILE   A 1 149 ? 230.343 203.133 158.634 1.00 113.67 ? 162  ILE   A CG1  1 
ATOM   1200 C CG2  . ILE   A 1 149 ? 230.743 200.810 157.700 1.00 111.80 ? 162  ILE   A CG2  1 
ATOM   1201 C CD1  . ILE   A 1 149 ? 230.732 203.864 157.346 1.00 114.05 ? 162  ILE   A CD1  1 
ATOM   1202 N N    . CYS   A 1 150 ? 232.410 202.308 161.617 1.00 127.21 ? 163  CYS   A N    1 
ATOM   1203 C CA   . CYS   A 1 150 ? 232.846 203.544 162.263 1.00 128.32 ? 163  CYS   A CA   1 
ATOM   1204 C C    . CYS   A 1 150 ? 232.499 204.736 161.368 1.00 130.79 ? 163  CYS   A C    1 
ATOM   1205 O O    . CYS   A 1 150 ? 232.907 204.760 160.208 1.00 132.39 ? 163  CYS   A O    1 
ATOM   1206 C CB   . CYS   A 1 150 ? 234.361 203.554 162.478 1.00 131.09 ? 163  CYS   A CB   1 
ATOM   1207 S SG   . CYS   A 1 150 ? 234.969 202.596 163.867 1.00 144.90 ? 163  CYS   A SG   1 
ATOM   1208 N N    . LYS   A 1 151 ? 231.813 205.752 161.892 1.00 127.14 ? 164  LYS   A N    1 
ATOM   1209 C CA   . LYS   A 1 151 ? 231.821 207.073 161.240 1.00 126.91 ? 164  LYS   A CA   1 
ATOM   1210 C C    . LYS   A 1 151 ? 233.087 207.845 161.612 1.00 128.56 ? 164  LYS   A C    1 
ATOM   1211 O O    . LYS   A 1 151 ? 233.545 208.690 160.849 1.00 128.20 ? 164  LYS   A O    1 
ATOM   1212 C CB   . LYS   A 1 151 ? 230.585 207.887 161.646 1.00 126.00 ? 164  LYS   A CB   1 
ATOM   1213 C CG   . LYS   A 1 151 ? 229.230 207.286 161.245 1.00 127.50 ? 164  LYS   A CG   1 
ATOM   1214 C CD   . LYS   A 1 151 ? 229.111 206.971 159.748 1.00 128.08 ? 164  LYS   A CD   1 
ATOM   1215 C CE   . LYS   A 1 151 ? 227.650 206.932 159.273 1.00 127.84 ? 164  LYS   A CE   1 
ATOM   1216 N NZ   . LYS   A 1 151 ? 226.827 205.894 159.945 1.00 127.89 ? 164  LYS   A NZ   1 
ATOM   1217 N N    . SER   A 1 152 ? 233.626 207.569 162.799 1.00 134.20 ? 165  SER   A N    1 
ATOM   1218 C CA   . SER   A 1 152 ? 234.671 208.362 163.445 1.00 134.81 ? 165  SER   A CA   1 
ATOM   1219 C C    . SER   A 1 152 ? 236.043 208.120 162.809 1.00 134.80 ? 165  SER   A C    1 
ATOM   1220 O O    . SER   A 1 152 ? 236.574 208.977 162.107 1.00 134.34 ? 165  SER   A O    1 
ATOM   1221 C CB   . SER   A 1 152 ? 234.679 208.067 164.949 1.00 132.41 ? 165  SER   A CB   1 
ATOM   1222 O OG   . SER   A 1 152 ? 233.357 208.066 165.444 1.00 133.41 ? 165  SER   A OG   1 
ATOM   1223 N N    . LYS   A 1 153 ? 236.599 206.922 163.009 1.00 130.91 ? 166  LYS   A N    1 
ATOM   1224 C CA   . LYS   A 1 153 ? 237.708 206.378 162.216 1.00 129.77 ? 166  LYS   A CA   1 
ATOM   1225 C C    . LYS   A 1 153 ? 237.183 205.860 160.874 1.00 131.34 ? 166  LYS   A C    1 
ATOM   1226 O O    . LYS   A 1 153 ? 235.978 205.695 160.700 1.00 132.47 ? 166  LYS   A O    1 
ATOM   1227 C CB   . LYS   A 1 153 ? 238.422 205.283 163.025 1.00 127.92 ? 166  LYS   A CB   1 
ATOM   1228 C CG   . LYS   A 1 153 ? 239.060 205.789 164.332 1.00 130.28 ? 166  LYS   A CG   1 
ATOM   1229 C CD   . LYS   A 1 153 ? 240.203 206.783 164.083 1.00 128.92 ? 166  LYS   A CD   1 
ATOM   1230 C CE   . LYS   A 1 153 ? 240.924 207.207 165.368 1.00 130.26 ? 166  LYS   A CE   1 
ATOM   1231 N NZ   . LYS   A 1 153 ? 241.839 206.161 165.891 1.00 129.72 ? 166  LYS   A NZ   1 
ATOM   1232 N N    . GLY   A 1 154 ? 238.066 205.601 159.919 1.00 134.69 ? 167  GLY   A N    1 
ATOM   1233 C CA   . GLY   A 1 154 ? 237.667 205.120 158.594 1.00 133.61 ? 167  GLY   A CA   1 
ATOM   1234 C C    . GLY   A 1 154 ? 237.074 203.708 158.592 1.00 135.07 ? 167  GLY   A C    1 
ATOM   1235 O O    . GLY   A 1 154 ? 237.260 202.927 159.528 1.00 135.71 ? 167  GLY   A O    1 
ATOM   1236 N N    . SER   A 1 155 ? 236.408 203.350 157.498 1.00 127.30 ? 168  SER   A N    1 
ATOM   1237 C CA   . SER   A 1 155 ? 236.008 201.976 157.185 1.00 127.88 ? 168  SER   A CA   1 
ATOM   1238 C C    . SER   A 1 155 ? 236.277 201.650 155.720 1.00 127.40 ? 168  SER   A C    1 
ATOM   1239 O O    . SER   A 1 155 ? 235.943 202.429 154.831 1.00 126.10 ? 168  SER   A O    1 
ATOM   1240 C CB   . SER   A 1 155 ? 234.535 201.773 157.531 1.00 126.24 ? 168  SER   A CB   1 
ATOM   1241 O OG   . SER   A 1 155 ? 234.072 200.514 157.078 1.00 129.90 ? 168  SER   A OG   1 
ATOM   1242 N N    . SER   A 1 156 ? 236.846 200.475 155.457 1.00 126.47 ? 169  SER   A N    1 
ATOM   1243 C CA   . SER   A 1 156 ? 237.116 199.952 154.109 1.00 127.48 ? 169  SER   A CA   1 
ATOM   1244 C C    . SER   A 1 156 ? 235.903 199.286 153.442 1.00 128.57 ? 169  SER   A C    1 
ATOM   1245 O O    . SER   A 1 156 ? 235.991 198.822 152.309 1.00 128.25 ? 169  SER   A O    1 
ATOM   1246 C CB   . SER   A 1 156 ? 238.328 199.017 154.159 1.00 125.69 ? 169  SER   A CB   1 
ATOM   1247 O OG   . SER   A 1 156 ? 238.273 198.156 155.282 1.00 125.54 ? 169  SER   A OG   1 
ATOM   1248 N N    . ARG   A 1 157 ? 234.748 199.293 154.117 1.00 121.13 ? 170  ARG   A N    1 
ATOM   1249 C CA   . ARG   A 1 157 ? 233.411 199.009 153.571 1.00 118.63 ? 170  ARG   A CA   1 
ATOM   1250 C C    . ARG   A 1 157 ? 232.504 200.219 153.796 1.00 120.15 ? 170  ARG   A C    1 
ATOM   1251 O O    . ARG   A 1 157 ? 232.661 200.894 154.812 1.00 121.68 ? 170  ARG   A O    1 
ATOM   1252 C CB   . ARG   A 1 157 ? 232.780 197.807 154.281 1.00 114.13 ? 170  ARG   A CB   1 
ATOM   1253 C CG   . ARG   A 1 157 ? 233.613 196.521 154.315 1.00 116.89 ? 170  ARG   A CG   1 
ATOM   1254 C CD   . ARG   A 1 157 ? 232.791 195.418 154.989 1.00 115.15 ? 170  ARG   A CD   1 
ATOM   1255 N NE   . ARG   A 1 157 ? 231.709 194.940 154.118 1.00 116.98 ? 170  ARG   A NE   1 
ATOM   1256 C CZ   . ARG   A 1 157 ? 231.807 194.022 153.181 1.00 121.28 ? 170  ARG   A CZ   1 
ATOM   1257 N NH1  . ARG   A 1 157 ? 230.805 193.763 152.404 1.00 123.10 ? 170  ARG   A NH1  1 
ATOM   1258 N NH2  . ARG   A 1 157 ? 232.889 193.340 152.981 1.00 120.71 ? 170  ARG   A NH2  1 
ATOM   1259 N N    . ASN   A 1 158 ? 231.530 200.467 152.926 1.00 128.90 ? 171  ASN   A N    1 
ATOM   1260 C CA   . ASN   A 1 158 ? 230.445 201.412 153.218 1.00 128.63 ? 171  ASN   A CA   1 
ATOM   1261 C C    . ASN   A 1 158 ? 229.443 200.791 154.205 1.00 128.05 ? 171  ASN   A C    1 
ATOM   1262 O O    . ASN   A 1 158 ? 229.324 199.573 154.265 1.00 127.50 ? 171  ASN   A O    1 
ATOM   1263 C CB   . ASN   A 1 158 ? 229.747 201.793 151.905 1.00 127.86 ? 171  ASN   A CB   1 
ATOM   1264 C CG   . ASN   A 1 158 ? 230.664 202.539 150.952 1.00 132.67 ? 171  ASN   A CG   1 
ATOM   1265 O OD1  . ASN   A 1 158 ? 231.469 203.361 151.378 1.00 131.70 ? 171  ASN   A OD1  1 
ATOM   1266 N ND2  . ASN   A 1 158 ? 230.570 202.230 149.671 1.00 133.33 ? 171  ASN   A ND2  1 
ATOM   1267 N N    . GLU   A 1 159 ? 228.600 201.592 154.856 1.00 119.71 ? 172  GLU   A N    1 
ATOM   1268 C CA   . GLU   A 1 159 ? 227.485 201.069 155.654 1.00 119.96 ? 172  GLU   A CA   1 
ATOM   1269 C C    . GLU   A 1 159 ? 226.429 200.427 154.758 1.00 118.49 ? 172  GLU   A C    1 
ATOM   1270 O O    . GLU   A 1 159 ? 226.005 201.021 153.765 1.00 118.11 ? 172  GLU   A O    1 
ATOM   1271 C CB   . GLU   A 1 159 ? 226.886 202.185 156.520 1.00 119.19 ? 172  GLU   A CB   1 
ATOM   1272 C CG   . GLU   A 1 159 ? 225.693 201.714 157.369 1.00 118.42 ? 172  GLU   A CG   1 
ATOM   1273 C CD   . GLU   A 1 159 ? 225.385 202.618 158.580 1.00 123.44 ? 172  GLU   A CD   1 
ATOM   1274 O OE1  . GLU   A 1 159 ? 226.298 203.302 159.093 1.00 125.43 ? 172  GLU   A OE1  1 
ATOM   1275 O OE2  . GLU   A 1 159 ? 224.224 202.613 159.047 1.00 124.01 ? 172  GLU   A OE2  1 
ATOM   1276 N N    . SER   A 1 160 ? 225.983 199.221 155.096 1.00 103.07 ? 173  SER   A N    1 
ATOM   1277 C CA   . SER   A 1 160 ? 224.993 198.502 154.304 1.00 102.51 ? 173  SER   A CA   1 
ATOM   1278 C C    . SER   A 1 160 ? 224.266 197.477 155.165 1.00 103.44 ? 173  SER   A C    1 
ATOM   1279 O O    . SER   A 1 160 ? 224.809 196.426 155.486 1.00 105.45 ? 173  SER   A O    1 
ATOM   1280 C CB   . SER   A 1 160 ? 225.686 197.825 153.116 1.00 102.01 ? 173  SER   A CB   1 
ATOM   1281 O OG   . SER   A 1 160 ? 224.732 197.229 152.261 1.00 100.64 ? 173  SER   A OG   1 
ATOM   1282 N N    . TRP   A 1 161 ? 223.034 197.780 155.565 1.00 93.51  ? 174  TRP   A N    1 
ATOM   1283 C CA   . TRP   A 1 161 ? 222.182 196.836 156.292 1.00 95.26  ? 174  TRP   A CA   1 
ATOM   1284 C C    . TRP   A 1 161 ? 220.748 196.764 155.779 1.00 98.96  ? 174  TRP   A C    1 
ATOM   1285 O O    . TRP   A 1 161 ? 220.111 195.728 155.948 1.00 104.04 ? 174  TRP   A O    1 
ATOM   1286 C CB   . TRP   A 1 161 ? 222.253 197.093 157.793 1.00 93.94  ? 174  TRP   A CB   1 
ATOM   1287 C CG   . TRP   A 1 161 ? 221.917 198.467 158.257 1.00 92.30  ? 174  TRP   A CG   1 
ATOM   1288 C CD1  . TRP   A 1 161 ? 222.817 199.444 158.485 1.00 94.95  ? 174  TRP   A CD1  1 
ATOM   1289 C CD2  . TRP   A 1 161 ? 220.618 199.042 158.556 1.00 91.22  ? 174  TRP   A CD2  1 
ATOM   1290 N NE1  . TRP   A 1 161 ? 222.171 200.582 158.909 1.00 93.62  ? 174  TRP   A NE1  1 
ATOM   1291 C CE2  . TRP   A 1 161 ? 220.812 200.386 158.991 1.00 92.60  ? 174  TRP   A CE2  1 
ATOM   1292 C CE3  . TRP   A 1 161 ? 219.297 198.559 158.519 1.00 87.29  ? 174  TRP   A CE3  1 
ATOM   1293 C CZ2  . TRP   A 1 161 ? 219.747 201.203 159.382 1.00 92.29  ? 174  TRP   A CZ2  1 
ATOM   1294 C CZ3  . TRP   A 1 161 ? 218.220 199.385 158.875 1.00 89.07  ? 174  TRP   A CZ3  1 
ATOM   1295 C CH2  . TRP   A 1 161 ? 218.441 200.699 159.316 1.00 92.49  ? 174  TRP   A CH2  1 
ATOM   1296 N N    . HIS   A 1 162 ? 220.285 197.771 155.050 1.00 100.91 ? 175  HIS   A N    1 
ATOM   1297 C CA   . HIS   A 1 162 ? 219.072 197.710 154.248 1.00 99.77  ? 175  HIS   A CA   1 
ATOM   1298 C C    . HIS   A 1 162 ? 219.305 198.318 152.866 1.00 104.89 ? 175  HIS   A C    1 
ATOM   1299 O O    . HIS   A 1 162 ? 220.246 199.083 152.666 1.00 101.05 ? 175  HIS   A O    1 
ATOM   1300 C CB   . HIS   A 1 162 ? 217.926 198.406 154.983 1.00 100.22 ? 175  HIS   A CB   1 
ATOM   1301 C CG   . HIS   A 1 162 ? 218.063 199.908 155.073 1.00 101.07 ? 175  HIS   A CG   1 
ATOM   1302 N ND1  . HIS   A 1 162 ? 219.120 200.602 155.657 1.00 102.60 ? 175  HIS   A ND1  1 
ATOM   1303 C CD2  . HIS   A 1 162 ? 217.146 200.810 154.629 1.00 101.30 ? 175  HIS   A CD2  1 
ATOM   1304 C CE1  . HIS   A 1 162 ? 218.799 201.901 155.582 1.00 100.62 ? 175  HIS   A CE1  1 
ATOM   1305 N NE2  . HIS   A 1 162 ? 217.620 202.056 154.965 1.00 101.24 ? 175  HIS   A NE2  1 
ATOM   1306 N N    . PHE   A 1 163 ? 218.435 197.995 151.913 1.00 118.36 ? 176  PHE   A N    1 
ATOM   1307 C CA   . PHE   A 1 163 ? 218.433 198.593 150.577 1.00 115.43 ? 176  PHE   A CA   1 
ATOM   1308 C C    . PHE   A 1 163 ? 217.036 199.100 150.216 1.00 117.50 ? 176  PHE   A C    1 
ATOM   1309 O O    . PHE   A 1 163 ? 216.301 198.480 149.456 1.00 120.86 ? 176  PHE   A O    1 
ATOM   1310 C CB   . PHE   A 1 163 ? 219.004 197.608 149.555 1.00 118.38 ? 176  PHE   A CB   1 
ATOM   1311 C CG   . PHE   A 1 163 ? 219.271 198.230 148.197 1.00 120.59 ? 176  PHE   A CG   1 
ATOM   1312 C CD1  . PHE   A 1 163 ? 220.513 198.841 147.956 1.00 118.26 ? 176  PHE   A CD1  1 
ATOM   1313 C CD2  . PHE   A 1 163 ? 218.325 198.140 147.160 1.00 118.73 ? 176  PHE   A CD2  1 
ATOM   1314 C CE1  . PHE   A 1 163 ? 220.814 199.344 146.681 1.00 118.13 ? 176  PHE   A CE1  1 
ATOM   1315 C CE2  . PHE   A 1 163 ? 218.622 198.650 145.888 1.00 119.90 ? 176  PHE   A CE2  1 
ATOM   1316 C CZ   . PHE   A 1 163 ? 219.871 199.244 145.645 1.00 120.35 ? 176  PHE   A CZ   1 
ATOM   1317 N N    . ASP   A 1 164 ? 216.657 200.242 150.776 1.00 116.04 ? 177  ASP   A N    1 
ATOM   1318 C CA   . ASP   A 1 164 ? 215.441 200.953 150.396 1.00 119.89 ? 177  ASP   A CA   1 
ATOM   1319 C C    . ASP   A 1 164 ? 215.820 202.316 149.808 1.00 120.98 ? 177  ASP   A C    1 
ATOM   1320 O O    . ASP   A 1 164 ? 216.381 203.166 150.497 1.00 119.45 ? 177  ASP   A O    1 
ATOM   1321 C CB   . ASP   A 1 164 ? 214.507 201.065 151.605 1.00 118.70 ? 177  ASP   A CB   1 
ATOM   1322 C CG   . ASP   A 1 164 ? 214.056 199.689 152.107 1.00 121.50 ? 177  ASP   A CG   1 
ATOM   1323 O OD1  . ASP   A 1 164 ? 213.295 199.011 151.382 1.00 121.02 ? 177  ASP   A OD1  1 
ATOM   1324 O OD2  . ASP   A 1 164 ? 214.454 199.289 153.221 1.00 121.70 ? 177  ASP   A OD2  1 
ATOM   1325 N N    . LYS   A 1 165 ? 215.533 202.521 148.516 1.00 131.10 ? 178  LYS   A N    1 
ATOM   1326 C CA   . LYS   A 1 165 ? 215.894 203.746 147.775 1.00 131.81 ? 178  LYS   A CA   1 
ATOM   1327 C C    . LYS   A 1 165 ? 214.980 204.938 148.076 1.00 131.82 ? 178  LYS   A C    1 
ATOM   1328 O O    . LYS   A 1 165 ? 215.344 206.081 147.803 1.00 129.11 ? 178  LYS   A O    1 
ATOM   1329 C CB   . LYS   A 1 165 ? 215.937 203.434 146.271 1.00 130.18 ? 178  LYS   A CB   1 
ATOM   1330 C CG   . LYS   A 1 165 ? 217.181 202.636 145.852 1.00 132.98 ? 178  LYS   A CG   1 
ATOM   1331 C CD   . LYS   A 1 165 ? 218.459 203.485 145.904 1.00 134.07 ? 178  LYS   A CD   1 
ATOM   1332 C CE   . LYS   A 1 165 ? 219.652 202.682 145.386 1.00 130.82 ? 178  LYS   A CE   1 
ATOM   1333 N NZ   . LYS   A 1 165 ? 220.885 203.504 145.380 1.00 128.65 ? 178  LYS   A NZ   1 
ATOM   1334 N N    . SER   A 1 166 ? 213.832 204.681 148.685 1.00 133.16 ? 179  SER   A N    1 
ATOM   1335 C CA   . SER   A 1 166 ? 212.953 205.662 149.328 1.00 132.70 ? 179  SER   A CA   1 
ATOM   1336 C C    . SER   A 1 166 ? 212.439 205.063 150.635 1.00 132.35 ? 179  SER   A C    1 
ATOM   1337 O O    . SER   A 1 166 ? 212.407 203.842 150.794 1.00 131.76 ? 179  SER   A O    1 
ATOM   1338 C CB   . SER   A 1 166 ? 211.812 206.069 148.391 1.00 131.76 ? 179  SER   A CB   1 
ATOM   1339 O OG   . SER   A 1 166 ? 211.051 204.951 147.969 1.00 130.27 ? 179  SER   A OG   1 
ATOM   1340 N N    . GLU   A 1 167 ? 212.098 205.895 151.613 1.00 134.37 ? 180  GLU   A N    1 
ATOM   1341 C CA   . GLU   A 1 167 ? 211.886 205.443 152.988 1.00 134.00 ? 180  GLU   A CA   1 
ATOM   1342 C C    . GLU   A 1 167 ? 210.716 204.444 153.113 1.00 134.36 ? 180  GLU   A C    1 
ATOM   1343 O O    . GLU   A 1 167 ? 209.617 204.719 152.622 1.00 134.71 ? 180  GLU   A O    1 
ATOM   1344 C CB   . GLU   A 1 167 ? 211.661 206.631 153.930 1.00 132.72 ? 180  GLU   A CB   1 
ATOM   1345 C CG   . GLU   A 1 167 ? 212.900 207.518 154.147 1.00 133.74 ? 180  GLU   A CG   1 
ATOM   1346 C CD   . GLU   A 1 167 ? 213.165 208.598 153.078 1.00 139.25 ? 180  GLU   A CD   1 
ATOM   1347 O OE1  . GLU   A 1 167 ? 212.500 208.620 152.018 1.00 138.73 ? 180  GLU   A OE1  1 
ATOM   1348 O OE2  . GLU   A 1 167 ? 214.059 209.445 153.308 1.00 138.16 ? 180  GLU   A OE2  1 
ATOM   1349 N N    . PRO   A 1 168 ? 210.914 203.296 153.785 1.00 115.50 ? 181  PRO   A N    1 
ATOM   1350 C CA   . PRO   A 1 168 ? 209.888 202.271 153.968 1.00 109.67 ? 181  PRO   A CA   1 
ATOM   1351 C C    . PRO   A 1 168 ? 208.796 202.725 154.941 1.00 110.21 ? 181  PRO   A C    1 
ATOM   1352 O O    . PRO   A 1 168 ? 208.970 203.694 155.677 1.00 110.73 ? 181  PRO   A O    1 
ATOM   1353 C CB   . PRO   A 1 168 ? 210.645 201.056 154.502 1.00 107.10 ? 181  PRO   A CB   1 
ATOM   1354 C CG   . PRO   A 1 168 ? 211.787 201.693 155.281 1.00 109.49 ? 181  PRO   A CG   1 
ATOM   1355 C CD   . PRO   A 1 168 ? 212.150 202.893 154.428 1.00 112.14 ? 181  PRO   A CD   1 
ATOM   1356 N N    . LEU   A 1 169 ? 207.680 201.995 154.991 1.00 99.87  ? 182  LEU   A N    1 
ATOM   1357 C CA   . LEU   A 1 169 ? 206.651 202.205 156.012 1.00 101.00 ? 182  LEU   A CA   1 
ATOM   1358 C C    . LEU   A 1 169 ? 207.247 202.015 157.407 1.00 104.89 ? 182  LEU   A C    1 
ATOM   1359 O O    . LEU   A 1 169 ? 207.854 200.979 157.676 1.00 112.05 ? 182  LEU   A O    1 
ATOM   1360 C CB   . LEU   A 1 169 ? 205.482 201.225 155.821 1.00 104.08 ? 182  LEU   A CB   1 
ATOM   1361 C CG   . LEU   A 1 169 ? 204.671 201.418 154.535 1.00 108.67 ? 182  LEU   A CG   1 
ATOM   1362 C CD1  . LEU   A 1 169 ? 203.627 200.314 154.426 1.00 106.02 ? 182  LEU   A CD1  1 
ATOM   1363 C CD2  . LEU   A 1 169 ? 203.944 202.761 154.523 1.00 103.97 ? 182  LEU   A CD2  1 
ATOM   1364 N N    . CYS   A 1 170 ? 207.053 202.985 158.291 1.00 100.07 ? 183  CYS   A N    1 
ATOM   1365 C CA   . CYS   A 1 170 ? 207.523 202.934 159.670 1.00 96.76  ? 183  CYS   A CA   1 
ATOM   1366 C C    . CYS   A 1 170 ? 206.375 203.130 160.653 1.00 99.90  ? 183  CYS   A C    1 
ATOM   1367 O O    . CYS   A 1 170 ? 205.653 204.124 160.579 1.00 103.24 ? 183  CYS   A O    1 
ATOM   1368 C CB   . CYS   A 1 170 ? 208.607 203.981 159.906 1.00 97.09  ? 183  CYS   A CB   1 
ATOM   1369 S SG   . CYS   A 1 170 ? 210.102 203.789 158.913 1.00 128.54 ? 183  CYS   A SG   1 
ATOM   1370 N N    . LEU   A 1 171 ? 206.231 202.216 161.609 1.00 85.47  ? 184  LEU   A N    1 
ATOM   1371 C CA   . LEU   A 1 171 ? 205.303 202.376 162.726 1.00 81.98  ? 184  LEU   A CA   1 
ATOM   1372 C C    . LEU   A 1 171 ? 205.855 203.317 163.793 1.00 87.27  ? 184  LEU   A C    1 
ATOM   1373 O O    . LEU   A 1 171 ? 205.094 203.976 164.497 1.00 92.26  ? 184  LEU   A O    1 
ATOM   1374 C CB   . LEU   A 1 171 ? 205.053 201.014 163.373 1.00 80.10  ? 184  LEU   A CB   1 
ATOM   1375 C CG   . LEU   A 1 171 ? 204.221 200.063 162.513 1.00 83.22  ? 184  LEU   A CG   1 
ATOM   1376 C CD1  . LEU   A 1 171 ? 204.285 198.656 163.091 1.00 85.03  ? 184  LEU   A CD1  1 
ATOM   1377 C CD2  . LEU   A 1 171 ? 202.758 200.495 162.458 1.00 88.23  ? 184  LEU   A CD2  1 
ATOM   1378 N N    . PHE   A 1 172 ? 207.177 203.369 163.915 1.00 83.69  ? 185  PHE   A N    1 
ATOM   1379 C CA   . PHE   A 1 172 ? 207.878 204.184 164.892 1.00 84.20  ? 185  PHE   A CA   1 
ATOM   1380 C C    . PHE   A 1 172 ? 209.213 204.659 164.319 1.00 85.14  ? 185  PHE   A C    1 
ATOM   1381 O O    . PHE   A 1 172 ? 209.876 203.926 163.588 1.00 89.92  ? 185  PHE   A O    1 
ATOM   1382 C CB   . PHE   A 1 172 ? 208.056 203.354 166.163 1.00 82.73  ? 185  PHE   A CB   1 
ATOM   1383 C CG   . PHE   A 1 172 ? 208.729 204.088 167.288 1.00 87.50  ? 185  PHE   A CG   1 
ATOM   1384 C CD1  . PHE   A 1 172 ? 207.959 204.849 168.177 1.00 88.95  ? 185  PHE   A CD1  1 
ATOM   1385 C CD2  . PHE   A 1 172 ? 210.117 204.005 167.447 1.00 84.26  ? 185  PHE   A CD2  1 
ATOM   1386 C CE1  . PHE   A 1 172 ? 208.582 205.532 169.232 1.00 87.56  ? 185  PHE   A CE1  1 
ATOM   1387 C CE2  . PHE   A 1 172 ? 210.740 204.691 168.501 1.00 83.77  ? 185  PHE   A CE2  1 
ATOM   1388 C CZ   . PHE   A 1 172 ? 209.971 205.447 169.389 1.00 87.48  ? 185  PHE   A CZ   1 
ATOM   1389 N N    . LYS   A 1 173 ? 209.611 205.879 164.667 1.00 85.13  ? 186  LYS   A N    1 
ATOM   1390 C CA   . LYS   A 1 173 ? 210.861 206.528 164.263 1.00 88.43  ? 186  LYS   A CA   1 
ATOM   1391 C C    . LYS   A 1 173 ? 211.121 207.688 165.207 1.00 91.98  ? 186  LYS   A C    1 
ATOM   1392 O O    . LYS   A 1 173 ? 210.388 208.674 165.174 1.00 95.74  ? 186  LYS   A O    1 
ATOM   1393 C CB   . LYS   A 1 173 ? 210.745 206.965 162.791 1.00 92.20  ? 186  LYS   A CB   1 
ATOM   1394 C CG   . LYS   A 1 173 ? 211.964 207.739 162.276 1.00 95.63  ? 186  LYS   A CG   1 
ATOM   1395 C CD   . LYS   A 1 173 ? 212.051 207.677 160.747 1.00 95.03  ? 186  LYS   A CD   1 
ATOM   1396 C CE   . LYS   A 1 173 ? 213.328 208.377 160.281 1.00 98.05  ? 186  LYS   A CE   1 
ATOM   1397 N NZ   . LYS   A 1 173 ? 213.498 208.280 158.814 1.00 95.37  ? 186  LYS   A NZ   1 
ATOM   1398 N N    . LYS   A 1 174 ? 212.116 207.557 166.082 1.00 91.18  ? 187  LYS   A N    1 
ATOM   1399 C CA   . LYS   A 1 174 ? 212.428 208.548 167.121 1.00 87.91  ? 187  LYS   A CA   1 
ATOM   1400 C C    . LYS   A 1 174 ? 213.895 208.487 167.520 1.00 89.95  ? 187  LYS   A C    1 
ATOM   1401 O O    . LYS   A 1 174 ? 214.513 207.432 167.436 1.00 96.48  ? 187  LYS   A O    1 
ATOM   1402 C CB   . LYS   A 1 174 ? 211.500 208.307 168.319 1.00 89.25  ? 187  LYS   A CB   1 
ATOM   1403 C CG   . LYS   A 1 174 ? 211.484 209.455 169.332 1.00 94.22  ? 187  LYS   A CG   1 
ATOM   1404 C CD   . LYS   A 1 174 ? 210.277 209.323 170.268 1.00 95.23  ? 187  LYS   A CD   1 
ATOM   1405 C CE   . LYS   A 1 174 ? 210.278 210.462 171.287 1.00 95.08  ? 187  LYS   A CE   1 
ATOM   1406 N NZ   . LYS   A 1 174 ? 209.055 210.440 172.119 1.00 94.71  ? 187  LYS   A NZ   1 
ATOM   1407 N N    . ASN   A 1 175 ? 214.428 209.603 168.003 1.00 93.88  ? 188  ASN   A N    1 
ATOM   1408 C CA   . ASN   A 1 175 ? 215.800 209.704 168.484 1.00 94.56  ? 188  ASN   A CA   1 
ATOM   1409 C C    . ASN   A 1 175 ? 215.823 210.074 169.965 1.00 95.61  ? 188  ASN   A C    1 
ATOM   1410 O O    . ASN   A 1 175 ? 215.056 210.925 170.411 1.00 98.07  ? 188  ASN   A O    1 
ATOM   1411 C CB   . ASN   A 1 175 ? 216.568 210.748 167.669 1.00 93.52  ? 188  ASN   A CB   1 
ATOM   1412 C CG   . ASN   A 1 175 ? 216.853 210.335 166.241 1.00 98.17  ? 188  ASN   A CG   1 
ATOM   1413 O OD1  . ASN   A 1 175 ? 216.490 209.261 165.786 1.00 99.01  ? 188  ASN   A OD1  1 
ATOM   1414 N ND2  . ASN   A 1 175 ? 217.480 211.250 165.527 1.00 101.08 ? 188  ASN   A ND2  1 
ATOM   1415 N N    . PHE   A 1 176 ? 216.833 209.579 170.667 1.00 82.46  ? 189  PHE   A N    1 
ATOM   1416 C CA   . PHE   A 1 176 ? 217.035 209.796 172.089 1.00 80.95  ? 189  PHE   A CA   1 
ATOM   1417 C C    . PHE   A 1 176 ? 218.496 210.176 172.323 1.00 83.81  ? 189  PHE   A C    1 
ATOM   1418 O O    . PHE   A 1 176 ? 219.377 209.628 171.676 1.00 87.80  ? 189  PHE   A O    1 
ATOM   1419 C CB   . PHE   A 1 176 ? 216.647 208.518 172.842 1.00 83.29  ? 189  PHE   A CB   1 
ATOM   1420 C CG   . PHE   A 1 176 ? 215.235 208.025 172.580 1.00 82.86  ? 189  PHE   A CG   1 
ATOM   1421 C CD1  . PHE   A 1 176 ? 214.958 207.206 171.469 1.00 80.24  ? 189  PHE   A CD1  1 
ATOM   1422 C CD2  . PHE   A 1 176 ? 214.206 208.356 173.472 1.00 80.81  ? 189  PHE   A CD2  1 
ATOM   1423 C CE1  . PHE   A 1 176 ? 213.654 206.739 171.246 1.00 77.97  ? 189  PHE   A CE1  1 
ATOM   1424 C CE2  . PHE   A 1 176 ? 212.906 207.876 173.258 1.00 82.99  ? 189  PHE   A CE2  1 
ATOM   1425 C CZ   . PHE   A 1 176 ? 212.631 207.066 172.145 1.00 81.45  ? 189  PHE   A CZ   1 
ATOM   1426 N N    . THR   A 1 177 ? 218.800 211.116 173.205 1.00 91.63  ? 190  THR   A N    1 
ATOM   1427 C CA   . THR   A 1 177 ? 220.199 211.431 173.534 1.00 93.34  ? 190  THR   A CA   1 
ATOM   1428 C C    . THR   A 1 177 ? 220.778 210.419 174.512 1.00 93.02  ? 190  THR   A C    1 
ATOM   1429 O O    . THR   A 1 177 ? 220.058 209.873 175.346 1.00 99.05  ? 190  THR   A O    1 
ATOM   1430 C CB   . THR   A 1 177 ? 220.334 212.844 174.110 1.00 97.11  ? 190  THR   A CB   1 
ATOM   1431 O OG1  . THR   A 1 177 ? 219.411 213.065 175.153 1.00 96.17  ? 190  THR   A OG1  1 
ATOM   1432 C CG2  . THR   A 1 177 ? 220.077 213.899 173.043 1.00 94.39  ? 190  THR   A CG2  1 
ATOM   1433 N N    . TYR   A 1 178 ? 222.091 210.215 174.485 1.00 92.40  ? 191  TYR   A N    1 
ATOM   1434 C CA   . TYR   A 1 178 ? 222.816 209.520 175.544 1.00 95.92  ? 191  TYR   A CA   1 
ATOM   1435 C C    . TYR   A 1 178 ? 224.161 210.195 175.817 1.00 98.45  ? 191  TYR   A C    1 
ATOM   1436 O O    . TYR   A 1 178 ? 224.755 210.814 174.936 1.00 100.02 ? 191  TYR   A O    1 
ATOM   1437 C CB   . TYR   A 1 178 ? 222.962 208.031 175.211 1.00 94.13  ? 191  TYR   A CB   1 
ATOM   1438 C CG   . TYR   A 1 178 ? 223.907 207.693 174.084 1.00 92.05  ? 191  TYR   A CG   1 
ATOM   1439 C CD1  . TYR   A 1 178 ? 225.263 207.441 174.349 1.00 89.35  ? 191  TYR   A CD1  1 
ATOM   1440 C CD2  . TYR   A 1 178 ? 223.418 207.604 172.775 1.00 95.51  ? 191  TYR   A CD2  1 
ATOM   1441 C CE1  . TYR   A 1 178 ? 226.141 207.143 173.296 1.00 90.37  ? 191  TYR   A CE1  1 
ATOM   1442 C CE2  . TYR   A 1 178 ? 224.287 207.282 171.722 1.00 98.54  ? 191  TYR   A CE2  1 
ATOM   1443 C CZ   . TYR   A 1 178 ? 225.653 207.076 171.979 1.00 94.22  ? 191  TYR   A CZ   1 
ATOM   1444 O OH   . TYR   A 1 178 ? 226.499 206.872 170.943 1.00 98.69  ? 191  TYR   A OH   1 
ATOM   1445 N N    . ASN   A 1 179 ? 224.645 210.106 177.050 1.00 106.92 ? 192  ASN   A N    1 
ATOM   1446 C CA   . ASN   A 1 179 ? 225.921 210.669 177.456 1.00 105.38 ? 192  ASN   A CA   1 
ATOM   1447 C C    . ASN   A 1 179 ? 227.088 209.928 176.786 1.00 107.84 ? 192  ASN   A C    1 
ATOM   1448 O O    . ASN   A 1 179 ? 227.509 208.860 177.234 1.00 110.15 ? 192  ASN   A O    1 
ATOM   1449 C CB   . ASN   A 1 179 ? 225.989 210.662 178.987 1.00 105.72 ? 192  ASN   A CB   1 
ATOM   1450 C CG   . ASN   A 1 179 ? 227.306 211.185 179.537 1.00 109.68 ? 192  ASN   A CG   1 
ATOM   1451 O OD1  . ASN   A 1 179 ? 228.198 211.588 178.798 1.00 111.16 ? 192  ASN   A OD1  1 
ATOM   1452 N ND2  . ASN   A 1 179 ? 227.437 211.140 180.847 1.00 112.10 ? 192  ASN   A ND2  1 
ATOM   1453 N N    . VAL   A 1 180 ? 227.689 210.577 175.790 1.00 105.12 ? 193  VAL   A N    1 
ATOM   1454 C CA   . VAL   A 1 180 ? 228.855 210.124 175.016 1.00 103.38 ? 193  VAL   A CA   1 
ATOM   1455 C C    . VAL   A 1 180 ? 230.043 209.703 175.879 1.00 105.83 ? 193  VAL   A C    1 
ATOM   1456 O O    . VAL   A 1 180 ? 230.811 208.845 175.457 1.00 105.92 ? 193  VAL   A O    1 
ATOM   1457 C CB   . VAL   A 1 180 ? 229.266 211.257 174.056 1.00 103.67 ? 193  VAL   A CB   1 
ATOM   1458 C CG1  . VAL   A 1 180 ? 230.612 211.080 173.359 1.00 106.41 ? 193  VAL   A CG1  1 
ATOM   1459 C CG2  . VAL   A 1 180 ? 228.212 211.395 172.962 1.00 103.31 ? 193  VAL   A CG2  1 
ATOM   1460 N N    . SER   A 1 181 ? 230.206 210.255 177.081 1.00 110.11 ? 194  SER   A N    1 
ATOM   1461 C CA   . SER   A 1 181 ? 231.344 209.956 177.953 1.00 107.84 ? 194  SER   A CA   1 
ATOM   1462 C C    . SER   A 1 181 ? 231.188 208.690 178.802 1.00 111.24 ? 194  SER   A C    1 
ATOM   1463 O O    . SER   A 1 181 ? 232.164 208.248 179.406 1.00 113.52 ? 194  SER   A O    1 
ATOM   1464 C CB   . SER   A 1 181 ? 231.636 211.147 178.866 1.00 110.06 ? 194  SER   A CB   1 
ATOM   1465 O OG   . SER   A 1 181 ? 231.925 212.288 178.083 1.00 111.20 ? 194  SER   A OG   1 
ATOM   1466 N N    . THR   A 1 182 ? 229.998 208.094 178.876 1.00 106.64 ? 195  THR   A N    1 
ATOM   1467 C CA   . THR   A 1 182 ? 229.721 206.906 179.715 1.00 103.69 ? 195  THR   A CA   1 
ATOM   1468 C C    . THR   A 1 182 ? 230.485 205.672 179.273 1.00 102.64 ? 195  THR   A C    1 
ATOM   1469 O O    . THR   A 1 182 ? 230.795 205.534 178.102 1.00 107.34 ? 195  THR   A O    1 
ATOM   1470 C CB   . THR   A 1 182 ? 228.236 206.541 179.707 1.00 101.01 ? 195  THR   A CB   1 
ATOM   1471 O OG1  . THR   A 1 182 ? 227.737 206.367 178.403 1.00 102.98 ? 195  THR   A OG1  1 
ATOM   1472 C CG2  . THR   A 1 182 ? 227.444 207.621 180.411 1.00 102.59 ? 195  THR   A CG2  1 
ATOM   1473 N N    . ASP   A 1 183 ? 230.771 204.738 180.177 1.00 99.28  ? 196  ASP   A N    1 
ATOM   1474 C CA   . ASP   A 1 183 ? 231.395 203.467 179.795 1.00 101.77 ? 196  ASP   A CA   1 
ATOM   1475 C C    . ASP   A 1 183 ? 230.382 202.419 179.320 1.00 101.29 ? 196  ASP   A C    1 
ATOM   1476 O O    . ASP   A 1 183 ? 230.717 201.572 178.495 1.00 103.87 ? 196  ASP   A O    1 
ATOM   1477 C CB   . ASP   A 1 183 ? 232.235 202.935 180.957 1.00 105.05 ? 196  ASP   A CB   1 
ATOM   1478 C CG   . ASP   A 1 183 ? 233.450 203.816 181.276 1.00 111.43 ? 196  ASP   A CG   1 
ATOM   1479 O OD1  . ASP   A 1 183 ? 233.950 204.538 180.382 1.00 111.99 ? 196  ASP   A OD1  1 
ATOM   1480 O OD2  . ASP   A 1 183 ? 233.934 203.756 182.428 1.00 111.35 ? 196  ASP   A OD2  1 
ATOM   1481 N N    . TRP   A 1 184 ? 229.137 202.488 179.797 1.00 90.14  ? 197  TRP   A N    1 
ATOM   1482 C CA   . TRP   A 1 184 ? 228.106 201.486 179.528 1.00 88.77  ? 197  TRP   A CA   1 
ATOM   1483 C C    . TRP   A 1 184 ? 226.738 202.089 179.239 1.00 91.20  ? 197  TRP   A C    1 
ATOM   1484 O O    . TRP   A 1 184 ? 226.315 203.024 179.909 1.00 91.77  ? 197  TRP   A O    1 
ATOM   1485 C CB   . TRP   A 1 184 ? 227.987 200.536 180.720 1.00 84.91  ? 197  TRP   A CB   1 
ATOM   1486 C CG   . TRP   A 1 184 ? 229.251 199.835 181.080 1.00 87.47  ? 197  TRP   A CG   1 
ATOM   1487 C CD1  . TRP   A 1 184 ? 230.108 200.211 182.050 1.00 86.74  ? 197  TRP   A CD1  1 
ATOM   1488 C CD2  . TRP   A 1 184 ? 229.845 198.670 180.448 1.00 91.75  ? 197  TRP   A CD2  1 
ATOM   1489 N NE1  . TRP   A 1 184 ? 231.199 199.368 182.053 1.00 87.80  ? 197  TRP   A NE1  1 
ATOM   1490 C CE2  . TRP   A 1 184 ? 231.091 198.407 181.079 1.00 89.95  ? 197  TRP   A CE2  1 
ATOM   1491 C CE3  . TRP   A 1 184 ? 229.450 197.805 179.413 1.00 90.45  ? 197  TRP   A CE3  1 
ATOM   1492 C CZ2  . TRP   A 1 184 ? 231.918 197.348 180.691 1.00 89.98  ? 197  TRP   A CZ2  1 
ATOM   1493 C CZ3  . TRP   A 1 184 ? 230.258 196.723 179.031 1.00 88.78  ? 197  TRP   A CZ3  1 
ATOM   1494 C CH2  . TRP   A 1 184 ? 231.491 196.498 179.665 1.00 89.46  ? 197  TRP   A CH2  1 
ATOM   1495 N N    . LEU   A 1 185 ? 226.014 201.482 178.304 1.00 82.94  ? 198  LEU   A N    1 
ATOM   1496 C CA   . LEU   A 1 185 ? 224.575 201.625 178.149 1.00 75.39  ? 198  LEU   A CA   1 
ATOM   1497 C C    . LEU   A 1 185 ? 223.903 200.289 178.460 1.00 76.35  ? 198  LEU   A C    1 
ATOM   1498 O O    . LEU   A 1 185 ? 224.469 199.231 178.212 1.00 83.26  ? 198  LEU   A O    1 
ATOM   1499 C CB   . LEU   A 1 185 ? 224.198 202.076 176.734 1.00 76.05  ? 198  LEU   A CB   1 
ATOM   1500 C CG   . LEU   A 1 185 ? 224.463 203.554 176.435 1.00 80.14  ? 198  LEU   A CG   1 
ATOM   1501 C CD1  . LEU   A 1 185 ? 225.896 203.807 176.002 1.00 79.66  ? 198  LEU   A CD1  1 
ATOM   1502 C CD2  . LEU   A 1 185 ? 223.537 204.003 175.315 1.00 82.71  ? 198  LEU   A CD2  1 
ATOM   1503 N N    . TYR   A 1 186 ? 222.683 200.334 178.966 1.00 69.56  ? 199  TYR   A N    1 
ATOM   1504 C CA   . TYR   A 1 186 ? 221.882 199.163 179.276 1.00 68.74  ? 199  TYR   A CA   1 
ATOM   1505 C C    . TYR   A 1 186 ? 220.548 199.259 178.558 1.00 72.22  ? 199  TYR   A C    1 
ATOM   1506 O O    . TYR   A 1 186 ? 220.004 200.350 178.475 1.00 78.16  ? 199  TYR   A O    1 
ATOM   1507 C CB   . TYR   A 1 186 ? 221.697 199.068 180.785 1.00 69.30  ? 199  TYR   A CB   1 
ATOM   1508 C CG   . TYR   A 1 186 ? 222.987 198.893 181.552 1.00 72.58  ? 199  TYR   A CG   1 
ATOM   1509 C CD1  . TYR   A 1 186 ? 223.713 200.010 181.991 1.00 72.09  ? 199  TYR   A CD1  1 
ATOM   1510 C CD2  . TYR   A 1 186 ? 223.457 197.600 181.824 1.00 72.23  ? 199  TYR   A CD2  1 
ATOM   1511 C CE1  . TYR   A 1 186 ? 224.930 199.842 182.676 1.00 75.16  ? 199  TYR   A CE1  1 
ATOM   1512 C CE2  . TYR   A 1 186 ? 224.647 197.428 182.544 1.00 78.72  ? 199  TYR   A CE2  1 
ATOM   1513 C CZ   . TYR   A 1 186 ? 225.402 198.545 182.947 1.00 86.02  ? 199  TYR   A CZ   1 
ATOM   1514 O OH   . TYR   A 1 186 ? 226.585 198.359 183.582 1.00 91.73  ? 199  TYR   A OH   1 
ATOM   1515 N N    . PHE   A 1 187 ? 219.994 198.152 178.072 1.00 67.17  ? 200  PHE   A N    1 
ATOM   1516 C CA   . PHE   A 1 187 ? 218.687 198.134 177.413 1.00 58.94  ? 200  PHE   A CA   1 
ATOM   1517 C C    . PHE   A 1 187 ? 217.848 196.944 177.848 1.00 61.02  ? 200  PHE   A C    1 
ATOM   1518 O O    . PHE   A 1 187 ? 218.374 195.847 177.989 1.00 74.13  ? 200  PHE   A O    1 
ATOM   1519 C CB   . PHE   A 1 187 ? 218.803 198.085 175.886 1.00 55.49  ? 200  PHE   A CB   1 
ATOM   1520 C CG   . PHE   A 1 187 ? 219.651 199.146 175.235 1.00 64.41  ? 200  PHE   A CG   1 
ATOM   1521 C CD1  . PHE   A 1 187 ? 221.047 199.000 175.157 1.00 64.21  ? 200  PHE   A CD1  1 
ATOM   1522 C CD2  . PHE   A 1 187 ? 219.043 200.274 174.668 1.00 62.30  ? 200  PHE   A CD2  1 
ATOM   1523 C CE1  . PHE   A 1 187 ? 221.827 199.981 174.529 1.00 70.65  ? 200  PHE   A CE1  1 
ATOM   1524 C CE2  . PHE   A 1 187 ? 219.824 201.252 174.045 1.00 62.95  ? 200  PHE   A CE2  1 
ATOM   1525 C CZ   . PHE   A 1 187 ? 221.215 201.109 173.973 1.00 66.87  ? 200  PHE   A CZ   1 
ATOM   1526 N N    . HIS   A 1 188 ? 216.536 197.127 177.959 1.00 56.01  ? 201  HIS   A N    1 
ATOM   1527 C CA   . HIS   A 1 188 ? 215.565 196.028 177.964 1.00 54.03  ? 201  HIS   A CA   1 
ATOM   1528 C C    . HIS   A 1 188 ? 214.768 196.086 176.682 1.00 60.99  ? 201  HIS   A C    1 
ATOM   1529 O O    . HIS   A 1 188 ? 214.218 197.136 176.370 1.00 77.12  ? 201  HIS   A O    1 
ATOM   1530 C CB   . HIS   A 1 188 ? 214.589 196.108 179.138 1.00 50.90  ? 201  HIS   A CB   1 
ATOM   1531 C CG   . HIS   A 1 188 ? 215.174 195.795 180.479 1.00 61.96  ? 201  HIS   A CG   1 
ATOM   1532 N ND1  . HIS   A 1 188 ? 216.213 196.480 181.088 1.00 73.00  ? 201  HIS   A ND1  1 
ATOM   1533 C CD2  . HIS   A 1 188 ? 214.755 194.804 181.310 1.00 60.88  ? 201  HIS   A CD2  1 
ATOM   1534 C CE1  . HIS   A 1 188 ? 216.377 195.921 182.288 1.00 66.94  ? 201  HIS   A CE1  1 
ATOM   1535 N NE2  . HIS   A 1 188 ? 215.525 194.899 182.444 1.00 63.06  ? 201  HIS   A NE2  1 
ATOM   1536 N N    . PHE   A 1 189 ? 214.654 194.970 175.977 1.00 59.05  ? 202  PHE   A N    1 
ATOM   1537 C CA   . PHE   A 1 189 ? 213.743 194.816 174.855 1.00 57.35  ? 202  PHE   A CA   1 
ATOM   1538 C C    . PHE   A 1 189 ? 212.859 193.602 175.095 1.00 58.29  ? 202  PHE   A C    1 
ATOM   1539 O O    . PHE   A 1 189 ? 213.386 192.508 175.262 1.00 72.93  ? 202  PHE   A O    1 
ATOM   1540 C CB   . PHE   A 1 189 ? 214.544 194.650 173.564 1.00 55.05  ? 202  PHE   A CB   1 
ATOM   1541 C CG   . PHE   A 1 189 ? 215.479 195.794 173.239 1.00 54.79  ? 202  PHE   A CG   1 
ATOM   1542 C CD1  . PHE   A 1 189 ? 214.949 197.059 172.944 1.00 56.87  ? 202  PHE   A CD1  1 
ATOM   1543 C CD2  . PHE   A 1 189 ? 216.866 195.593 173.204 1.00 57.15  ? 202  PHE   A CD2  1 
ATOM   1544 C CE1  . PHE   A 1 189 ? 215.802 198.118 172.612 1.00 59.57  ? 202  PHE   A CE1  1 
ATOM   1545 C CE2  . PHE   A 1 189 ? 217.719 196.657 172.885 1.00 60.05  ? 202  PHE   A CE2  1 
ATOM   1546 C CZ   . PHE   A 1 189 ? 217.189 197.919 172.588 1.00 62.68  ? 202  PHE   A CZ   1 
ATOM   1547 N N    . TYR   A 1 190 ? 211.539 193.742 175.091 1.00 53.16  ? 203  TYR   A N    1 
ATOM   1548 C CA   . TYR   A 1 190 ? 210.636 192.608 175.284 1.00 55.02  ? 203  TYR   A CA   1 
ATOM   1549 C C    . TYR   A 1 190 ? 209.319 192.778 174.548 1.00 66.27  ? 203  TYR   A C    1 
ATOM   1550 O O    . TYR   A 1 190 ? 208.980 193.866 174.098 1.00 79.82  ? 203  TYR   A O    1 
ATOM   1551 C CB   . TYR   A 1 190 ? 210.432 192.323 176.775 1.00 59.92  ? 203  TYR   A CB   1 
ATOM   1552 C CG   . TYR   A 1 190 ? 209.670 193.332 177.595 1.00 65.26  ? 203  TYR   A CG   1 
ATOM   1553 C CD1  . TYR   A 1 190 ? 208.265 193.303 177.614 1.00 64.29  ? 203  TYR   A CD1  1 
ATOM   1554 C CD2  . TYR   A 1 190 ? 210.361 194.209 178.445 1.00 63.34  ? 203  TYR   A CD2  1 
ATOM   1555 C CE1  . TYR   A 1 190 ? 207.552 194.167 178.460 1.00 64.61  ? 203  TYR   A CE1  1 
ATOM   1556 C CE2  . TYR   A 1 190 ? 209.650 195.049 179.317 1.00 62.95  ? 203  TYR   A CE2  1 
ATOM   1557 C CZ   . TYR   A 1 190 ? 208.241 195.044 179.313 1.00 66.05  ? 203  TYR   A CZ   1 
ATOM   1558 O OH   . TYR   A 1 190 ? 207.548 195.863 180.144 1.00 66.12  ? 203  TYR   A OH   1 
ATOM   1559 N N    . GLN   A 1 191 ? 208.566 191.690 174.429 1.00 71.95  ? 204  GLN   A N    1 
ATOM   1560 C CA   . GLN   A 1 191 ? 207.212 191.722 173.895 1.00 65.71  ? 204  GLN   A CA   1 
ATOM   1561 C C    . GLN   A 1 191 ? 206.212 191.078 174.851 1.00 69.05  ? 204  GLN   A C    1 
ATOM   1562 O O    . GLN   A 1 191 ? 206.497 190.053 175.457 1.00 77.81  ? 204  GLN   A O    1 
ATOM   1563 C CB   . GLN   A 1 191 ? 207.181 191.095 172.503 1.00 68.93  ? 204  GLN   A CB   1 
ATOM   1564 C CG   . GLN   A 1 191 ? 207.513 189.599 172.499 1.00 70.56  ? 204  GLN   A CG   1 
ATOM   1565 C CD   . GLN   A 1 191 ? 207.648 189.035 171.098 1.00 79.06  ? 204  GLN   A CD   1 
ATOM   1566 O OE1  . GLN   A 1 191 ? 207.115 189.553 170.127 1.00 86.13  ? 204  GLN   A OE1  1 
ATOM   1567 N NE2  . GLN   A 1 191 ? 208.355 187.946 170.943 1.00 79.69  ? 204  GLN   A NE2  1 
ATOM   1568 N N    . GLU   A 1 192 ? 205.021 191.654 174.961 1.00 79.52  ? 205  GLU   A N    1 
ATOM   1569 C CA   . GLU   A 1 192 ? 203.891 191.067 175.682 1.00 81.43  ? 205  GLU   A CA   1 
ATOM   1570 C C    . GLU   A 1 192 ? 202.590 191.325 174.924 1.00 86.84  ? 205  GLU   A C    1 
ATOM   1571 O O    . GLU   A 1 192 ? 202.347 192.456 174.511 1.00 94.57  ? 205  GLU   A O    1 
ATOM   1572 C CB   . GLU   A 1 192 ? 203.837 191.623 177.110 1.00 86.43  ? 205  GLU   A CB   1 
ATOM   1573 C CG   . GLU   A 1 192 ? 202.743 190.930 177.929 1.00 93.04  ? 205  GLU   A CG   1 
ATOM   1574 C CD   . GLU   A 1 192 ? 202.724 191.334 179.409 1.00 100.12 ? 205  GLU   A CD   1 
ATOM   1575 O OE1  . GLU   A 1 192 ? 203.116 192.468 179.748 1.00 98.53  ? 205  GLU   A OE1  1 
ATOM   1576 O OE2  . GLU   A 1 192 ? 202.259 190.513 180.238 1.00 95.97  ? 205  GLU   A OE2  1 
ATOM   1577 N N    . ARG   A 1 193 ? 201.748 190.303 174.726 1.00 85.48  ? 206  ARG   A N    1 
ATOM   1578 C CA   . ARG   A 1 193 ? 200.441 190.403 174.041 1.00 85.03  ? 206  ARG   A CA   1 
ATOM   1579 C C    . ARG   A 1 193 ? 200.497 191.213 172.738 1.00 91.13  ? 206  ARG   A C    1 
ATOM   1580 O O    . ARG   A 1 193 ? 199.684 192.100 172.496 1.00 90.03  ? 206  ARG   A O    1 
ATOM   1581 C CB   . ARG   A 1 193 ? 199.348 190.880 175.018 1.00 86.52  ? 206  ARG   A CB   1 
ATOM   1582 C CG   . ARG   A 1 193 ? 199.019 189.796 176.054 1.00 87.85  ? 206  ARG   A CG   1 
ATOM   1583 C CD   . ARG   A 1 193 ? 197.881 190.210 176.997 1.00 93.46  ? 206  ARG   A CD   1 
ATOM   1584 N NE   . ARG   A 1 193 ? 198.249 191.353 177.852 1.00 100.50 ? 206  ARG   A NE   1 
ATOM   1585 C CZ   . ARG   A 1 193 ? 199.087 191.343 178.868 1.00 98.58  ? 206  ARG   A CZ   1 
ATOM   1586 N NH1  . ARG   A 1 193 ? 199.424 192.455 179.448 1.00 97.54  ? 206  ARG   A NH1  1 
ATOM   1587 N NH2  . ARG   A 1 193 ? 199.623 190.245 179.314 1.00 89.99  ? 206  ARG   A NH2  1 
ATOM   1588 N N    . GLY   A 1 194 ? 201.501 190.940 171.907 1.00 79.60  ? 207  GLY   A N    1 
ATOM   1589 C CA   . GLY   A 1 194 ? 201.693 191.601 170.616 1.00 71.37  ? 207  GLY   A CA   1 
ATOM   1590 C C    . GLY   A 1 194 ? 202.192 193.044 170.693 1.00 70.79  ? 207  GLY   A C    1 
ATOM   1591 O O    . GLY   A 1 194 ? 202.236 193.720 169.671 1.00 77.28  ? 207  GLY   A O    1 
ATOM   1592 N N    . THR   A 1 195 ? 202.574 193.540 171.867 1.00 68.52  ? 208  THR   A N    1 
ATOM   1593 C CA   . THR   A 1 195 ? 203.142 194.880 172.053 1.00 66.61  ? 208  THR   A CA   1 
ATOM   1594 C C    . THR   A 1 195 ? 204.621 194.779 172.380 1.00 67.93  ? 208  THR   A C    1 
ATOM   1595 O O    . THR   A 1 195 ? 204.987 194.068 173.308 1.00 78.97  ? 208  THR   A O    1 
ATOM   1596 C CB   . THR   A 1 195 ? 202.431 195.612 173.192 1.00 71.58  ? 208  THR   A CB   1 
ATOM   1597 O OG1  . THR   A 1 195 ? 201.047 195.650 172.957 1.00 80.78  ? 208  THR   A OG1  1 
ATOM   1598 C CG2  . THR   A 1 195 ? 202.889 197.052 173.323 1.00 60.88  ? 208  THR   A CG2  1 
ATOM   1599 N N    . PHE   A 1 196 ? 205.471 195.486 171.651 1.00 60.01  ? 209  PHE   A N    1 
ATOM   1600 C CA   . PHE   A 1 196 ? 206.887 195.603 171.961 1.00 54.98  ? 209  PHE   A CA   1 
ATOM   1601 C C    . PHE   A 1 196 ? 207.155 196.743 172.942 1.00 64.62  ? 209  PHE   A C    1 
ATOM   1602 O O    . PHE   A 1 196 ? 206.476 197.773 172.927 1.00 75.02  ? 209  PHE   A O    1 
ATOM   1603 C CB   . PHE   A 1 196 ? 207.650 195.801 170.664 1.00 54.69  ? 209  PHE   A CB   1 
ATOM   1604 C CG   . PHE   A 1 196 ? 209.150 195.910 170.826 1.00 59.51  ? 209  PHE   A CG   1 
ATOM   1605 C CD1  . PHE   A 1 196 ? 209.924 194.751 170.987 1.00 63.94  ? 209  PHE   A CD1  1 
ATOM   1606 C CD2  . PHE   A 1 196 ? 209.787 197.160 170.756 1.00 61.82  ? 209  PHE   A CD2  1 
ATOM   1607 C CE1  . PHE   A 1 196 ? 211.322 194.830 171.011 1.00 61.70  ? 209  PHE   A CE1  1 
ATOM   1608 C CE2  . PHE   A 1 196 ? 211.183 197.240 170.821 1.00 59.72  ? 209  PHE   A CE2  1 
ATOM   1609 C CZ   . PHE   A 1 196 ? 211.954 196.077 170.930 1.00 62.82  ? 209  PHE   A CZ   1 
ATOM   1610 N N    . TYR   A 1 197 ? 208.174 196.581 173.779 1.00 63.96  ? 210  TYR   A N    1 
ATOM   1611 C CA   . TYR   A 1 197 ? 208.624 197.568 174.750 1.00 56.94  ? 210  TYR   A CA   1 
ATOM   1612 C C    . TYR   A 1 197 ? 210.139 197.694 174.726 1.00 58.37  ? 210  TYR   A C    1 
ATOM   1613 O O    . TYR   A 1 197 ? 210.846 196.690 174.677 1.00 69.19  ? 210  TYR   A O    1 
ATOM   1614 C CB   . TYR   A 1 197 ? 208.179 197.170 176.153 1.00 53.83  ? 210  TYR   A CB   1 
ATOM   1615 C CG   . TYR   A 1 197 ? 206.690 197.020 176.348 1.00 56.36  ? 210  TYR   A CG   1 
ATOM   1616 C CD1  . TYR   A 1 197 ? 206.037 195.833 175.987 1.00 57.90  ? 210  TYR   A CD1  1 
ATOM   1617 C CD2  . TYR   A 1 197 ? 205.962 198.067 176.940 1.00 56.82  ? 210  TYR   A CD2  1 
ATOM   1618 C CE1  . TYR   A 1 197 ? 204.656 195.692 176.197 1.00 62.29  ? 210  TYR   A CE1  1 
ATOM   1619 C CE2  . TYR   A 1 197 ? 204.582 197.933 177.153 1.00 60.92  ? 210  TYR   A CE2  1 
ATOM   1620 C CZ   . TYR   A 1 197 ? 203.925 196.748 176.785 1.00 70.69  ? 210  TYR   A CZ   1 
ATOM   1621 O OH   . TYR   A 1 197 ? 202.596 196.624 177.017 1.00 76.93  ? 210  TYR   A OH   1 
ATOM   1622 N N    . ALA   A 1 198 ? 210.638 198.924 174.828 1.00 61.05  ? 211  ALA   A N    1 
ATOM   1623 C CA   . ALA   A 1 198 ? 212.056 199.222 174.907 1.00 57.50  ? 211  ALA   A CA   1 
ATOM   1624 C C    . ALA   A 1 198 ? 212.360 200.186 176.048 1.00 68.09  ? 211  ALA   A C    1 
ATOM   1625 O O    . ALA   A 1 198 ? 211.635 201.153 176.280 1.00 78.74  ? 211  ALA   A O    1 
ATOM   1626 C CB   . ALA   A 1 198 ? 212.533 199.805 173.584 1.00 56.54  ? 211  ALA   A CB   1 
ATOM   1627 N N    . TYR   A 1 199 ? 213.485 199.975 176.710 1.00 62.00  ? 212  TYR   A N    1 
ATOM   1628 C CA   . TYR   A 1 199 ? 213.988 200.826 177.779 1.00 53.03  ? 212  TYR   A CA   1 
ATOM   1629 C C    . TYR   A 1 199 ? 215.496 200.971 177.624 1.00 58.42  ? 212  TYR   A C    1 
ATOM   1630 O O    . TYR   A 1 199 ? 216.136 200.024 177.176 1.00 73.74  ? 212  TYR   A O    1 
ATOM   1631 C CB   . TYR   A 1 199 ? 213.698 200.219 179.146 1.00 54.22  ? 212  TYR   A CB   1 
ATOM   1632 C CG   . TYR   A 1 199 ? 212.269 199.847 179.458 1.00 53.49  ? 212  TYR   A CG   1 
ATOM   1633 C CD1  . TYR   A 1 199 ? 211.711 198.719 178.845 1.00 59.41  ? 212  TYR   A CD1  1 
ATOM   1634 C CD2  . TYR   A 1 199 ? 211.521 200.587 180.383 1.00 58.35  ? 212  TYR   A CD2  1 
ATOM   1635 C CE1  . TYR   A 1 199 ? 210.382 198.363 179.107 1.00 56.99  ? 212  TYR   A CE1  1 
ATOM   1636 C CE2  . TYR   A 1 199 ? 210.191 200.219 180.665 1.00 60.19  ? 212  TYR   A CE2  1 
ATOM   1637 C CZ   . TYR   A 1 199 ? 209.625 199.102 180.025 1.00 63.50  ? 212  TYR   A CZ   1 
ATOM   1638 O OH   . TYR   A 1 199 ? 208.349 198.706 180.285 1.00 71.50  ? 212  TYR   A OH   1 
ATOM   1639 N N    . TYR   A 1 200 ? 216.067 202.099 178.041 1.00 60.33  ? 213  TYR   A N    1 
ATOM   1640 C CA   . TYR   A 1 200 ? 217.512 202.241 178.145 1.00 63.46  ? 213  TYR   A CA   1 
ATOM   1641 C C    . TYR   A 1 200 ? 217.987 203.021 179.362 1.00 70.23  ? 213  TYR   A C    1 
ATOM   1642 O O    . TYR   A 1 200 ? 217.257 203.819 179.933 1.00 77.89  ? 213  TYR   A O    1 
ATOM   1643 C CB   . TYR   A 1 200 ? 218.087 202.874 176.890 1.00 64.45  ? 213  TYR   A CB   1 
ATOM   1644 C CG   . TYR   A 1 200 ? 218.130 204.391 176.869 1.00 71.33  ? 213  TYR   A CG   1 
ATOM   1645 C CD1  . TYR   A 1 200 ? 217.008 205.154 177.247 1.00 75.09  ? 213  TYR   A CD1  1 
ATOM   1646 C CD2  . TYR   A 1 200 ? 219.306 205.056 176.471 1.00 65.65  ? 213  TYR   A CD2  1 
ATOM   1647 C CE1  . TYR   A 1 200 ? 217.060 206.554 177.241 1.00 76.97  ? 213  TYR   A CE1  1 
ATOM   1648 C CE2  . TYR   A 1 200 ? 219.365 206.459 176.470 1.00 71.34  ? 213  TYR   A CE2  1 
ATOM   1649 C CZ   . TYR   A 1 200 ? 218.239 207.216 176.854 1.00 82.26  ? 213  TYR   A CZ   1 
ATOM   1650 O OH   . TYR   A 1 200 ? 218.268 208.570 176.862 1.00 86.13  ? 213  TYR   A OH   1 
ATOM   1651 N N    . ALA   A 1 201 ? 219.259 202.873 179.704 1.00 74.34  ? 214  ALA   A N    1 
ATOM   1652 C CA   . ALA   A 1 201 ? 219.977 203.832 180.526 1.00 69.38  ? 214  ALA   A CA   1 
ATOM   1653 C C    . ALA   A 1 201 ? 221.414 203.970 180.038 1.00 77.26  ? 214  ALA   A C    1 
ATOM   1654 O O    . ALA   A 1 201 ? 221.988 203.037 179.493 1.00 83.02  ? 214  ALA   A O    1 
ATOM   1655 C CB   . ALA   A 1 201 ? 219.943 203.406 181.994 1.00 71.90  ? 214  ALA   A CB   1 
ATOM   1656 N N    . ASP   A 1 202 ? 222.011 205.122 180.293 1.00 98.10  ? 215  ASP   A N    1 
ATOM   1657 C CA   . ASP   A 1 202 ? 223.415 205.434 180.059 1.00 98.37  ? 215  ASP   A CA   1 
ATOM   1658 C C    . ASP   A 1 202 ? 224.142 205.610 181.399 1.00 102.47 ? 215  ASP   A C    1 
ATOM   1659 O O    . ASP   A 1 202 ? 224.868 206.566 181.627 1.00 106.51 ? 215  ASP   A O    1 
ATOM   1660 C CB   . ASP   A 1 202 ? 223.523 206.646 179.126 1.00 98.02  ? 215  ASP   A CB   1 
ATOM   1661 C CG   . ASP   A 1 202 ? 222.831 207.922 179.626 1.00 104.16 ? 215  ASP   A CG   1 
ATOM   1662 O OD1  . ASP   A 1 202 ? 222.126 207.888 180.659 1.00 103.95 ? 215  ASP   A OD1  1 
ATOM   1663 O OD2  . ASP   A 1 202 ? 222.965 208.964 178.951 1.00 104.42 ? 215  ASP   A OD2  1 
ATOM   1664 N N    . SER   A 1 203 ? 223.889 204.714 182.348 1.00 101.57 ? 216  SER   A N    1 
ATOM   1665 C CA   . SER   A 1 203 ? 224.560 204.620 183.651 1.00 100.78 ? 216  SER   A CA   1 
ATOM   1666 C C    . SER   A 1 203 ? 224.254 203.262 184.270 1.00 103.12 ? 216  SER   A C    1 
ATOM   1667 O O    . SER   A 1 203 ? 223.309 202.597 183.853 1.00 105.16 ? 216  SER   A O    1 
ATOM   1668 C CB   . SER   A 1 203 ? 224.071 205.727 184.591 1.00 96.62  ? 216  SER   A CB   1 
ATOM   1669 O OG   . SER   A 1 203 ? 224.701 206.942 184.256 1.00 103.16 ? 216  SER   A OG   1 
ATOM   1670 N N    . GLY   A 1 204 ? 224.994 202.848 185.294 1.00 108.00 ? 217  GLY   A N    1 
ATOM   1671 C CA   . GLY   A 1 204 ? 224.643 201.679 186.107 1.00 107.03 ? 217  GLY   A CA   1 
ATOM   1672 C C    . GLY   A 1 204 ? 223.426 201.962 186.992 1.00 109.43 ? 217  GLY   A C    1 
ATOM   1673 O O    . GLY   A 1 204 ? 223.571 202.315 188.159 1.00 111.93 ? 217  GLY   A O    1 
ATOM   1674 N N    . MET   A 1 205 ? 222.228 201.853 186.426 1.00 96.79  ? 218  MET   A N    1 
ATOM   1675 C CA   . MET   A 1 205 ? 220.958 202.257 187.039 1.00 96.54  ? 218  MET   A CA   1 
ATOM   1676 C C    . MET   A 1 205 ? 219.788 201.498 186.386 1.00 92.76  ? 218  MET   A C    1 
ATOM   1677 O O    . MET   A 1 205 ? 219.983 200.868 185.345 1.00 92.48  ? 218  MET   A O    1 
ATOM   1678 C CB   . MET   A 1 205 ? 220.809 203.786 186.908 1.00 92.96  ? 218  MET   A CB   1 
ATOM   1679 C CG   . MET   A 1 205 ? 220.617 204.261 185.469 1.00 95.98  ? 218  MET   A CG   1 
ATOM   1680 S SD   . MET   A 1 205 ? 220.214 206.013 185.316 1.00 111.76 ? 218  MET   A SD   1 
ATOM   1681 C CE   . MET   A 1 205 ? 218.427 205.949 185.586 1.00 99.06  ? 218  MET   A CE   1 
ATOM   1682 N N    . PRO   A 1 206 ? 218.571 201.525 186.953 1.00 72.62  ? 219  PRO   A N    1 
ATOM   1683 C CA   . PRO   A 1 206 ? 217.395 201.009 186.271 1.00 71.16  ? 219  PRO   A CA   1 
ATOM   1684 C C    . PRO   A 1 206 ? 217.177 201.708 184.937 1.00 73.69  ? 219  PRO   A C    1 
ATOM   1685 O O    . PRO   A 1 206 ? 217.346 202.915 184.809 1.00 78.18  ? 219  PRO   A O    1 
ATOM   1686 C CB   . PRO   A 1 206 ? 216.200 201.254 187.184 1.00 73.02  ? 219  PRO   A CB   1 
ATOM   1687 C CG   . PRO   A 1 206 ? 216.807 201.667 188.514 1.00 75.24  ? 219  PRO   A CG   1 
ATOM   1688 C CD   . PRO   A 1 206 ? 218.218 202.121 188.221 1.00 74.23  ? 219  PRO   A CD   1 
ATOM   1689 N N    . THR   A 1 207 ? 216.771 200.947 183.937 1.00 68.93  ? 220  THR   A N    1 
ATOM   1690 C CA   . THR   A 1 207 ? 216.547 201.461 182.591 1.00 64.58  ? 220  THR   A CA   1 
ATOM   1691 C C    . THR   A 1 207 ? 215.253 202.274 182.539 1.00 67.98  ? 220  THR   A C    1 
ATOM   1692 O O    . THR   A 1 207 ? 214.287 201.991 183.249 1.00 69.31  ? 220  THR   A O    1 
ATOM   1693 C CB   . THR   A 1 207 ? 216.647 200.277 181.637 1.00 59.79  ? 220  THR   A CB   1 
ATOM   1694 O OG1  . THR   A 1 207 ? 216.763 200.512 180.299 1.00 72.75  ? 220  THR   A OG1  1 
ATOM   1695 C CG2  . THR   A 1 207 ? 215.470 199.361 181.752 1.00 61.37  ? 220  THR   A CG2  1 
ATOM   1696 N N    . THR   A 1 208 ? 215.230 203.314 181.720 1.00 73.59  ? 221  THR   A N    1 
ATOM   1697 C CA   . THR   A 1 208 ? 214.138 204.276 181.544 1.00 65.43  ? 221  THR   A CA   1 
ATOM   1698 C C    . THR   A 1 208 ? 213.439 204.004 180.224 1.00 71.40  ? 221  THR   A C    1 
ATOM   1699 O O    . THR   A 1 208 ? 214.083 203.694 179.229 1.00 79.37  ? 221  THR   A O    1 
ATOM   1700 C CB   . THR   A 1 208 ? 214.690 205.709 181.542 1.00 74.81  ? 221  THR   A CB   1 
ATOM   1701 O OG1  . THR   A 1 208 ? 215.356 205.991 182.746 1.00 75.73  ? 221  THR   A OG1  1 
ATOM   1702 C CG2  . THR   A 1 208 ? 213.608 206.773 181.398 1.00 80.52  ? 221  THR   A CG2  1 
ATOM   1703 N N    . PHE   A 1 209 ? 212.118 204.088 180.188 1.00 71.07  ? 222  PHE   A N    1 
ATOM   1704 C CA   . PHE   A 1 209 ? 211.331 203.798 178.993 1.00 69.50  ? 222  PHE   A CA   1 
ATOM   1705 C C    . PHE   A 1 209 ? 211.738 204.631 177.787 1.00 69.73  ? 222  PHE   A C    1 
ATOM   1706 O O    . PHE   A 1 209 ? 211.738 205.858 177.838 1.00 77.92  ? 222  PHE   A O    1 
ATOM   1707 C CB   . PHE   A 1 209 ? 209.888 204.088 179.361 1.00 70.02  ? 222  PHE   A CB   1 
ATOM   1708 C CG   . PHE   A 1 209 ? 208.849 203.775 178.329 1.00 69.30  ? 222  PHE   A CG   1 
ATOM   1709 C CD1  . PHE   A 1 209 ? 208.593 202.441 177.984 1.00 71.24  ? 222  PHE   A CD1  1 
ATOM   1710 C CD2  . PHE   A 1 209 ? 208.011 204.796 177.849 1.00 74.11  ? 222  PHE   A CD2  1 
ATOM   1711 C CE1  . PHE   A 1 209 ? 207.496 202.126 177.177 1.00 68.49  ? 222  PHE   A CE1  1 
ATOM   1712 C CE2  . PHE   A 1 209 ? 206.916 204.480 177.039 1.00 75.66  ? 222  PHE   A CE2  1 
ATOM   1713 C CZ   . PHE   A 1 209 ? 206.648 203.143 176.714 1.00 71.60  ? 222  PHE   A CZ   1 
ATOM   1714 N N    . LEU   A 1 210 ? 212.054 203.964 176.682 1.00 63.58  ? 223  LEU   A N    1 
ATOM   1715 C CA   . LEU   A 1 210 ? 212.236 204.608 175.394 1.00 64.28  ? 223  LEU   A CA   1 
ATOM   1716 C C    . LEU   A 1 210 ? 210.883 204.764 174.705 1.00 77.92  ? 223  LEU   A C    1 
ATOM   1717 O O    . LEU   A 1 210 ? 210.438 205.874 174.430 1.00 85.31  ? 223  LEU   A O    1 
ATOM   1718 C CB   . LEU   A 1 210 ? 213.171 203.760 174.529 1.00 62.20  ? 223  LEU   A CB   1 
ATOM   1719 C CG   . LEU   A 1 210 ? 214.654 203.799 174.904 1.00 71.48  ? 223  LEU   A CG   1 
ATOM   1720 C CD1  . LEU   A 1 210 ? 215.351 202.648 174.183 1.00 71.37  ? 223  LEU   A CD1  1 
ATOM   1721 C CD2  . LEU   A 1 210 ? 215.293 205.104 174.454 1.00 69.58  ? 223  LEU   A CD2  1 
ATOM   1722 N N    . PHE   A 1 211 ? 210.227 203.644 174.416 1.00 68.49  ? 224  PHE   A N    1 
ATOM   1723 C CA   . PHE   A 1 211 ? 208.972 203.605 173.677 1.00 64.39  ? 224  PHE   A CA   1 
ATOM   1724 C C    . PHE   A 1 211 ? 208.263 202.264 173.839 1.00 69.86  ? 224  PHE   A C    1 
ATOM   1725 O O    . PHE   A 1 211 ? 208.857 201.267 174.243 1.00 79.88  ? 224  PHE   A O    1 
ATOM   1726 C CB   . PHE   A 1 211 ? 209.236 203.886 172.197 1.00 66.67  ? 224  PHE   A CB   1 
ATOM   1727 C CG   . PHE   A 1 211 ? 209.775 202.729 171.384 1.00 67.32  ? 224  PHE   A CG   1 
ATOM   1728 C CD1  . PHE   A 1 211 ? 211.130 202.366 171.466 1.00 66.22  ? 224  PHE   A CD1  1 
ATOM   1729 C CD2  . PHE   A 1 211 ? 208.931 202.025 170.508 1.00 71.93  ? 224  PHE   A CD2  1 
ATOM   1730 C CE1  . PHE   A 1 211 ? 211.627 201.303 170.700 1.00 68.79  ? 224  PHE   A CE1  1 
ATOM   1731 C CE2  . PHE   A 1 211 ? 209.437 200.979 169.721 1.00 69.65  ? 224  PHE   A CE2  1 
ATOM   1732 C CZ   . PHE   A 1 211 ? 210.788 200.623 169.811 1.00 66.77  ? 224  PHE   A CZ   1 
ATOM   1733 N N    . SER   A 1 212 ? 206.993 202.226 173.450 1.00 72.15  ? 225  SER   A N    1 
ATOM   1734 C CA   . SER   A 1 212 ? 206.242 200.995 173.242 1.00 69.47  ? 225  SER   A CA   1 
ATOM   1735 C C    . SER   A 1 212 ? 205.484 201.062 171.927 1.00 77.62  ? 225  SER   A C    1 
ATOM   1736 O O    . SER   A 1 212 ? 205.108 202.144 171.474 1.00 85.96  ? 225  SER   A O    1 
ATOM   1737 C CB   . SER   A 1 212 ? 205.311 200.735 174.416 1.00 72.06  ? 225  SER   A CB   1 
ATOM   1738 O OG   . SER   A 1 212 ? 204.537 199.590 174.173 1.00 81.42  ? 225  SER   A OG   1 
ATOM   1739 N N    . LEU   A 1 213 ? 205.277 199.914 171.298 1.00 71.28  ? 226  LEU   A N    1 
ATOM   1740 C CA   . LEU   A 1 213 ? 204.752 199.802 169.949 1.00 69.81  ? 226  LEU   A CA   1 
ATOM   1741 C C    . LEU   A 1 213 ? 203.853 198.568 169.815 1.00 73.79  ? 226  LEU   A C    1 
ATOM   1742 O O    . LEU   A 1 213 ? 204.304 197.451 170.034 1.00 83.62  ? 226  LEU   A O    1 
ATOM   1743 C CB   . LEU   A 1 213 ? 205.968 199.781 169.009 1.00 69.25  ? 226  LEU   A CB   1 
ATOM   1744 C CG   . LEU   A 1 213 ? 205.646 199.413 167.565 1.00 75.10  ? 226  LEU   A CG   1 
ATOM   1745 C CD1  . LEU   A 1 213 ? 204.626 200.354 166.949 1.00 75.77  ? 226  LEU   A CD1  1 
ATOM   1746 C CD2  . LEU   A 1 213 ? 206.910 199.475 166.728 1.00 75.49  ? 226  LEU   A CD2  1 
ATOM   1747 N N    . TYR   A 1 214 ? 202.584 198.731 169.440 1.00 74.65  ? 227  TYR   A N    1 
ATOM   1748 C CA   . TYR   A 1 214 ? 201.731 197.591 169.114 1.00 73.84  ? 227  TYR   A CA   1 
ATOM   1749 C C    . TYR   A 1 214 ? 202.082 197.022 167.739 1.00 76.45  ? 227  TYR   A C    1 
ATOM   1750 O O    . TYR   A 1 214 ? 201.997 197.729 166.741 1.00 82.02  ? 227  TYR   A O    1 
ATOM   1751 C CB   . TYR   A 1 214 ? 200.259 197.986 169.179 1.00 69.96  ? 227  TYR   A CB   1 
ATOM   1752 C CG   . TYR   A 1 214 ? 199.356 196.793 168.970 1.00 68.83  ? 227  TYR   A CG   1 
ATOM   1753 C CD1  . TYR   A 1 214 ? 199.019 195.986 170.066 1.00 71.30  ? 227  TYR   A CD1  1 
ATOM   1754 C CD2  . TYR   A 1 214 ? 198.921 196.445 167.680 1.00 65.52  ? 227  TYR   A CD2  1 
ATOM   1755 C CE1  . TYR   A 1 214 ? 198.257 194.820 169.880 1.00 75.56  ? 227  TYR   A CE1  1 
ATOM   1756 C CE2  . TYR   A 1 214 ? 198.160 195.279 167.488 1.00 72.91  ? 227  TYR   A CE2  1 
ATOM   1757 C CZ   . TYR   A 1 214 ? 197.832 194.463 168.585 1.00 79.64  ? 227  TYR   A CZ   1 
ATOM   1758 O OH   . TYR   A 1 214 ? 197.105 193.333 168.396 1.00 77.49  ? 227  TYR   A OH   1 
ATOM   1759 N N    . LEU   A 1 215 ? 202.437 195.742 167.678 1.00 73.09  ? 228  LEU   A N    1 
ATOM   1760 C CA   . LEU   A 1 215 ? 202.760 195.025 166.443 1.00 73.22  ? 228  LEU   A CA   1 
ATOM   1761 C C    . LEU   A 1 215 ? 201.698 193.991 166.058 1.00 74.98  ? 228  LEU   A C    1 
ATOM   1762 O O    . LEU   A 1 215 ? 201.545 193.673 164.882 1.00 80.91  ? 228  LEU   A O    1 
ATOM   1763 C CB   . LEU   A 1 215 ? 204.112 194.320 166.622 1.00 69.07  ? 228  LEU   A CB   1 
ATOM   1764 C CG   . LEU   A 1 215 ? 205.314 195.249 166.835 1.00 70.77  ? 228  LEU   A CG   1 
ATOM   1765 C CD1  . LEU   A 1 215 ? 206.559 194.409 167.073 1.00 71.86  ? 228  LEU   A CD1  1 
ATOM   1766 C CD2  . LEU   A 1 215 ? 205.583 196.127 165.619 1.00 69.69  ? 228  LEU   A CD2  1 
ATOM   1767 N N    . GLY   A 1 216 ? 200.989 193.428 167.036 1.00 71.88  ? 229  GLY   A N    1 
ATOM   1768 C CA   . GLY   A 1 216 ? 200.073 192.303 166.872 1.00 74.59  ? 229  GLY   A CA   1 
ATOM   1769 C C    . GLY   A 1 216 ? 200.789 190.973 166.641 1.00 80.00  ? 229  GLY   A C    1 
ATOM   1770 O O    . GLY   A 1 216 ? 200.500 189.990 167.319 1.00 86.06  ? 229  GLY   A O    1 
ATOM   1771 N N    . THR   A 1 217 ? 201.747 190.927 165.718 1.00 81.30  ? 230  THR   A N    1 
ATOM   1772 C CA   . THR   A 1 217 ? 202.581 189.751 165.432 1.00 80.76  ? 230  THR   A CA   1 
ATOM   1773 C C    . THR   A 1 217 ? 203.677 189.544 166.477 1.00 83.86  ? 230  THR   A C    1 
ATOM   1774 O O    . THR   A 1 217 ? 204.085 190.476 167.163 1.00 89.83  ? 230  THR   A O    1 
ATOM   1775 C CB   . THR   A 1 217 ? 203.227 189.870 164.047 1.00 79.03  ? 230  THR   A CB   1 
ATOM   1776 O OG1  . THR   A 1 217 ? 204.006 191.039 163.971 1.00 83.33  ? 230  THR   A OG1  1 
ATOM   1777 C CG2  . THR   A 1 217 ? 202.194 189.934 162.926 1.00 79.05  ? 230  THR   A CG2  1 
ATOM   1778 N N    . LEU   A 1 218 ? 204.184 188.316 166.594 1.00 82.25  ? 231  LEU   A N    1 
ATOM   1779 C CA   . LEU   A 1 218 ? 205.372 188.021 167.394 1.00 77.36  ? 231  LEU   A CA   1 
ATOM   1780 C C    . LEU   A 1 218 ? 206.648 188.392 166.643 1.00 80.31  ? 231  LEU   A C    1 
ATOM   1781 O O    . LEU   A 1 218 ? 206.891 187.916 165.536 1.00 83.75  ? 231  LEU   A O    1 
ATOM   1782 C CB   . LEU   A 1 218 ? 205.426 186.532 167.768 1.00 73.08  ? 231  LEU   A CB   1 
ATOM   1783 C CG   . LEU   A 1 218 ? 204.361 186.082 168.770 1.00 84.77  ? 231  LEU   A CG   1 
ATOM   1784 C CD1  . LEU   A 1 218 ? 204.500 184.579 168.977 1.00 82.86  ? 231  LEU   A CD1  1 
ATOM   1785 C CD2  . LEU   A 1 218 ? 204.514 186.764 170.127 1.00 83.87  ? 231  LEU   A CD2  1 
ATOM   1786 N N    . LEU   A 1 219 ? 207.517 189.154 167.292 1.00 77.38  ? 232  LEU   A N    1 
ATOM   1787 C CA   . LEU   A 1 219 ? 208.935 189.171 166.971 1.00 71.44  ? 232  LEU   A CA   1 
ATOM   1788 C C    . LEU   A 1 219 ? 209.509 187.809 167.344 1.00 78.12  ? 232  LEU   A C    1 
ATOM   1789 O O    . LEU   A 1 219 ? 209.101 187.231 168.347 1.00 85.09  ? 232  LEU   A O    1 
ATOM   1790 C CB   . LEU   A 1 219 ? 209.617 190.289 167.761 1.00 68.87  ? 232  LEU   A CB   1 
ATOM   1791 C CG   . LEU   A 1 219 ? 209.033 191.680 167.474 1.00 74.07  ? 232  LEU   A CG   1 
ATOM   1792 C CD1  . LEU   A 1 219 ? 209.494 192.649 168.544 1.00 74.98  ? 232  LEU   A CD1  1 
ATOM   1793 C CD2  . LEU   A 1 219 ? 209.473 192.207 166.114 1.00 70.23  ? 232  LEU   A CD2  1 
ATOM   1794 N N    . SER   A 1 220 ? 210.445 187.269 166.578 1.00 74.06  ? 233  SER   A N    1 
ATOM   1795 C CA   . SER   A 1 220 ? 210.965 185.925 166.825 1.00 75.08  ? 233  SER   A CA   1 
ATOM   1796 C C    . SER   A 1 220 ? 212.477 185.848 166.788 1.00 81.27  ? 233  SER   A C    1 
ATOM   1797 O O    . SER   A 1 220 ? 213.029 184.976 167.451 1.00 91.43  ? 233  SER   A O    1 
ATOM   1798 C CB   . SER   A 1 220 ? 210.344 184.920 165.858 1.00 81.60  ? 233  SER   A CB   1 
ATOM   1799 O OG   . SER   A 1 220 ? 210.677 185.204 164.517 1.00 85.21  ? 233  SER   A OG   1 
ATOM   1800 N N    . HIS   A 1 221 ? 213.165 186.774 166.127 1.00 71.91  ? 234  HIS   A N    1 
ATOM   1801 C CA   . HIS   A 1 221 ? 214.620 186.803 166.046 1.00 70.04  ? 234  HIS   A CA   1 
ATOM   1802 C C    . HIS   A 1 221 ? 215.175 188.173 166.381 1.00 72.28  ? 234  HIS   A C    1 
ATOM   1803 O O    . HIS   A 1 221 ? 214.551 189.193 166.117 1.00 83.27  ? 234  HIS   A O    1 
ATOM   1804 C CB   . HIS   A 1 221 ? 215.080 186.366 164.661 1.00 71.86  ? 234  HIS   A CB   1 
ATOM   1805 C CG   . HIS   A 1 221 ? 214.802 184.921 164.382 1.00 77.87  ? 234  HIS   A CG   1 
ATOM   1806 N ND1  . HIS   A 1 221 ? 215.555 183.857 164.864 1.00 85.50  ? 234  HIS   A ND1  1 
ATOM   1807 C CD2  . HIS   A 1 221 ? 213.760 184.437 163.659 1.00 75.65  ? 234  HIS   A CD2  1 
ATOM   1808 C CE1  . HIS   A 1 221 ? 214.946 182.748 164.425 1.00 83.60  ? 234  HIS   A CE1  1 
ATOM   1809 N NE2  . HIS   A 1 221 ? 213.869 183.069 163.693 1.00 81.06  ? 234  HIS   A NE2  1 
ATOM   1810 N N    . TYR   A 1 222 ? 216.389 188.210 166.902 1.00 75.96  ? 235  TYR   A N    1 
ATOM   1811 C CA   . TYR   A 1 222 ? 217.187 189.420 166.973 1.00 77.20  ? 235  TYR   A CA   1 
ATOM   1812 C C    . TYR   A 1 222 ? 218.618 189.112 166.580 1.00 72.37  ? 235  TYR   A C    1 
ATOM   1813 O O    . TYR   A 1 222 ? 219.075 187.970 166.630 1.00 75.55  ? 235  TYR   A O    1 
ATOM   1814 C CB   . TYR   A 1 222 ? 217.109 190.061 168.357 1.00 73.73  ? 235  TYR   A CB   1 
ATOM   1815 C CG   . TYR   A 1 222 ? 217.893 189.335 169.417 1.00 72.52  ? 235  TYR   A CG   1 
ATOM   1816 C CD1  . TYR   A 1 222 ? 217.321 188.240 170.073 1.00 74.59  ? 235  TYR   A CD1  1 
ATOM   1817 C CD2  . TYR   A 1 222 ? 219.206 189.723 169.721 1.00 68.52  ? 235  TYR   A CD2  1 
ATOM   1818 C CE1  . TYR   A 1 222 ? 218.044 187.545 171.055 1.00 71.58  ? 235  TYR   A CE1  1 
ATOM   1819 C CE2  . TYR   A 1 222 ? 219.939 189.023 170.691 1.00 71.86  ? 235  TYR   A CE2  1 
ATOM   1820 C CZ   . TYR   A 1 222 ? 219.359 187.927 171.355 1.00 77.14  ? 235  TYR   A CZ   1 
ATOM   1821 O OH   . TYR   A 1 222 ? 220.072 187.225 172.269 1.00 83.74  ? 235  TYR   A OH   1 
ATOM   1822 N N    . TYR   A 1 223 ? 219.329 190.137 166.152 1.00 70.80  ? 236  TYR   A N    1 
ATOM   1823 C CA   . TYR   A 1 223 ? 220.693 190.012 165.690 1.00 72.70  ? 236  TYR   A CA   1 
ATOM   1824 C C    . TYR   A 1 223 ? 221.458 191.306 165.958 1.00 80.43  ? 236  TYR   A C    1 
ATOM   1825 O O    . TYR   A 1 223 ? 220.904 192.393 165.835 1.00 86.74  ? 236  TYR   A O    1 
ATOM   1826 C CB   . TYR   A 1 223 ? 220.629 189.644 164.211 1.00 78.68  ? 236  TYR   A CB   1 
ATOM   1827 C CG   . TYR   A 1 223 ? 221.979 189.507 163.578 1.00 80.45  ? 236  TYR   A CG   1 
ATOM   1828 C CD1  . TYR   A 1 223 ? 222.837 188.494 164.017 1.00 82.88  ? 236  TYR   A CD1  1 
ATOM   1829 C CD2  . TYR   A 1 223 ? 222.380 190.401 162.578 1.00 79.90  ? 236  TYR   A CD2  1 
ATOM   1830 C CE1  . TYR   A 1 223 ? 224.116 188.383 163.463 1.00 84.44  ? 236  TYR   A CE1  1 
ATOM   1831 C CE2  . TYR   A 1 223 ? 223.667 190.302 162.031 1.00 83.04  ? 236  TYR   A CE2  1 
ATOM   1832 C CZ   . TYR   A 1 223 ? 224.536 189.291 162.480 1.00 86.24  ? 236  TYR   A CZ   1 
ATOM   1833 O OH   . TYR   A 1 223 ? 225.763 189.149 161.938 1.00 90.04  ? 236  TYR   A OH   1 
ATOM   1834 N N    . VAL   A 1 224 ? 222.731 191.217 166.322 1.00 79.84  ? 237  VAL   A N    1 
ATOM   1835 C CA   . VAL   A 1 224 ? 223.576 192.384 166.584 1.00 75.02  ? 237  VAL   A CA   1 
ATOM   1836 C C    . VAL   A 1 224 ? 224.488 192.564 165.386 1.00 77.97  ? 237  VAL   A C    1 
ATOM   1837 O O    . VAL   A 1 224 ? 225.255 191.667 165.053 1.00 82.28  ? 237  VAL   A O    1 
ATOM   1838 C CB   . VAL   A 1 224 ? 224.354 192.206 167.888 1.00 73.81  ? 237  VAL   A CB   1 
ATOM   1839 C CG1  . VAL   A 1 224 ? 225.319 193.360 168.139 1.00 74.83  ? 237  VAL   A CG1  1 
ATOM   1840 C CG2  . VAL   A 1 224 ? 223.385 192.145 169.070 1.00 76.88  ? 237  VAL   A CG2  1 
ATOM   1841 N N    . LEU   A 1 225 ? 224.374 193.691 164.693 1.00 82.92  ? 238  LEU   A N    1 
ATOM   1842 C CA   . LEU   A 1 225 ? 225.058 193.895 163.425 1.00 80.80  ? 238  LEU   A CA   1 
ATOM   1843 C C    . LEU   A 1 225 ? 226.574 193.960 163.619 1.00 85.63  ? 238  LEU   A C    1 
ATOM   1844 O O    . LEU   A 1 225 ? 227.040 194.698 164.492 1.00 88.58  ? 238  LEU   A O    1 
ATOM   1845 C CB   . LEU   A 1 225 ? 224.574 195.180 162.735 1.00 81.49  ? 238  LEU   A CB   1 
ATOM   1846 C CG   . LEU   A 1 225 ? 223.078 195.253 162.420 1.00 82.64  ? 238  LEU   A CG   1 
ATOM   1847 C CD1  . LEU   A 1 225 ? 222.783 196.448 161.521 1.00 84.25  ? 238  LEU   A CD1  1 
ATOM   1848 C CD2  . LEU   A 1 225 ? 222.600 194.013 161.679 1.00 83.19  ? 238  LEU   A CD2  1 
ATOM   1849 N N    . PRO   A 1 226 ? 227.362 193.277 162.779 1.00 86.75  ? 239  PRO   A N    1 
ATOM   1850 C CA   . PRO   A 1 226 ? 228.777 193.544 162.655 1.00 87.15  ? 239  PRO   A CA   1 
ATOM   1851 C C    . PRO   A 1 226 ? 229.042 195.015 162.376 1.00 88.98  ? 239  PRO   A C    1 
ATOM   1852 O O    . PRO   A 1 226 ? 228.262 195.675 161.695 1.00 95.58  ? 239  PRO   A O    1 
ATOM   1853 C CB   . PRO   A 1 226 ? 229.278 192.650 161.522 1.00 85.18  ? 239  PRO   A CB   1 
ATOM   1854 C CG   . PRO   A 1 226 ? 228.277 191.508 161.533 1.00 86.19  ? 239  PRO   A CG   1 
ATOM   1855 C CD   . PRO   A 1 226 ? 226.977 192.214 161.885 1.00 84.61  ? 239  PRO   A CD   1 
ATOM   1856 N N    . LEU   A 1 227 ? 230.152 195.528 162.880 1.00 97.64  ? 240  LEU   A N    1 
ATOM   1857 C CA   . LEU   A 1 227 ? 230.583 196.904 162.671 1.00 96.60  ? 240  LEU   A CA   1 
ATOM   1858 C C    . LEU   A 1 227 ? 232.022 196.883 162.162 1.00 102.37 ? 240  LEU   A C    1 
ATOM   1859 O O    . LEU   A 1 227 ? 232.880 196.239 162.760 1.00 107.29 ? 240  LEU   A O    1 
ATOM   1860 C CB   . LEU   A 1 227 ? 230.348 197.648 163.994 1.00 94.99  ? 240  LEU   A CB   1 
ATOM   1861 C CG   . LEU   A 1 227 ? 230.584 199.162 163.986 1.00 96.33  ? 240  LEU   A CG   1 
ATOM   1862 C CD1  . LEU   A 1 227 ? 229.845 199.823 165.142 1.00 100.72 ? 240  LEU   A CD1  1 
ATOM   1863 C CD2  . LEU   A 1 227 ? 232.046 199.514 164.170 1.00 98.13  ? 240  LEU   A CD2  1 
ATOM   1864 N N    . THR   A 1 228 ? 232.307 197.547 161.045 1.00 115.95 ? 241  THR   A N    1 
ATOM   1865 C CA   . THR   A 1 228 ? 233.632 197.491 160.407 1.00 116.72 ? 241  THR   A CA   1 
ATOM   1866 C C    . THR   A 1 228 ? 234.387 198.808 160.523 1.00 119.26 ? 241  THR   A C    1 
ATOM   1867 O O    . THR   A 1 228 ? 233.819 199.873 160.296 1.00 121.56 ? 241  THR   A O    1 
ATOM   1868 C CB   . THR   A 1 228 ? 233.552 197.015 158.954 1.00 116.80 ? 241  THR   A CB   1 
ATOM   1869 O OG1  . THR   A 1 228 ? 232.838 197.925 158.157 1.00 120.81 ? 241  THR   A OG1  1 
ATOM   1870 C CG2  . THR   A 1 228 ? 232.843 195.669 158.861 1.00 112.42 ? 241  THR   A CG2  1 
ATOM   1871 N N    . CYS   A 1 229 ? 235.676 198.749 160.856 1.00 131.66 ? 242  CYS   A N    1 
ATOM   1872 C CA   . CYS   A 1 229 ? 236.534 199.924 161.014 1.00 132.64 ? 242  CYS   A CA   1 
ATOM   1873 C C    . CYS   A 1 229 ? 237.988 199.603 160.690 1.00 135.39 ? 242  CYS   A C    1 
ATOM   1874 O O    . CYS   A 1 229 ? 238.443 198.490 160.945 1.00 136.47 ? 242  CYS   A O    1 
ATOM   1875 C CB   . CYS   A 1 229 ? 236.526 200.405 162.463 1.00 131.48 ? 242  CYS   A CB   1 
ATOM   1876 S SG   . CYS   A 1 229 ? 234.914 200.703 163.171 1.00 148.89 ? 242  CYS   A SG   1 
ATOM   1877 N N    . ASN   A 1 230 ? 238.753 200.618 160.304 1.00 137.17 ? 243  ASN   A N    1 
ATOM   1878 C CA   . ASN   A 1 230 ? 240.214 200.591 160.268 1.00 137.08 ? 243  ASN   A CA   1 
ATOM   1879 C C    . ASN   A 1 230 ? 240.809 200.988 161.643 1.00 137.96 ? 243  ASN   A C    1 
ATOM   1880 O O    . ASN   A 1 230 ? 241.737 201.788 161.730 1.00 138.50 ? 243  ASN   A O    1 
ATOM   1881 C CB   . ASN   A 1 230 ? 240.681 201.490 159.111 1.00 135.51 ? 243  ASN   A CB   1 
ATOM   1882 C CG   . ASN   A 1 230 ? 240.069 201.163 157.756 1.00 137.53 ? 243  ASN   A CG   1 
ATOM   1883 O OD1  . ASN   A 1 230 ? 239.604 200.068 157.471 1.00 136.05 ? 243  ASN   A OD1  1 
ATOM   1884 N ND2  . ASN   A 1 230 ? 240.047 202.126 156.865 1.00 137.57 ? 243  ASN   A ND2  1 
ATOM   1885 N N    . ALA   A 1 231 ? 240.198 200.505 162.725 1.00 135.06 ? 244  ALA   A N    1 
ATOM   1886 C CA   . ALA   A 1 231 ? 240.437 200.870 164.127 1.00 134.24 ? 244  ALA   A CA   1 
ATOM   1887 C C    . ALA   A 1 231 ? 239.879 199.766 165.047 1.00 133.03 ? 244  ALA   A C    1 
ATOM   1888 O O    . ALA   A 1 231 ? 239.459 198.733 164.534 1.00 134.10 ? 244  ALA   A O    1 
ATOM   1889 C CB   . ALA   A 1 231 ? 239.742 202.207 164.392 1.00 133.24 ? 244  ALA   A CB   1 
ATOM   1890 N N    . ILE   A 1 232 ? 239.810 199.974 166.365 1.00 129.01 ? 245  ILE   A N    1 
ATOM   1891 C CA   . ILE   A 1 232 ? 239.178 199.070 167.345 1.00 128.90 ? 245  ILE   A CA   1 
ATOM   1892 C C    . ILE   A 1 232 ? 239.658 197.622 167.219 1.00 127.05 ? 245  ILE   A C    1 
ATOM   1893 O O    . ILE   A 1 232 ? 238.876 196.696 167.004 1.00 125.90 ? 245  ILE   A O    1 
ATOM   1894 C CB   . ILE   A 1 232 ? 237.644 199.252 167.465 1.00 126.67 ? 245  ILE   A CB   1 
ATOM   1895 C CG1  . ILE   A 1 232 ? 236.851 199.159 166.158 1.00 128.05 ? 245  ILE   A CG1  1 
ATOM   1896 C CG2  . ILE   A 1 232 ? 237.355 200.603 168.109 1.00 127.66 ? 245  ILE   A CG2  1 
ATOM   1897 C CD1  . ILE   A 1 232 ? 235.336 199.186 166.348 1.00 126.99 ? 245  ILE   A CD1  1 
ATOM   1898 N N    . SER   A 1 233 ? 240.977 197.437 167.305 1.00 136.92 ? 246  SER   A N    1 
ATOM   1899 C CA   . SER   A 1 233 ? 241.636 196.126 167.334 1.00 137.70 ? 246  SER   A CA   1 
ATOM   1900 C C    . SER   A 1 233 ? 243.044 196.209 167.936 1.00 138.84 ? 246  SER   A C    1 
ATOM   1901 O O    . SER   A 1 233 ? 243.636 197.283 168.079 1.00 137.69 ? 246  SER   A O    1 
ATOM   1902 C CB   . SER   A 1 233 ? 241.652 195.480 165.942 1.00 136.62 ? 246  SER   A CB   1 
ATOM   1903 O OG   . SER   A 1 233 ? 242.384 196.233 165.005 1.00 137.65 ? 246  SER   A OG   1 
ATOM   1904 N N    . SER   A 1 234 ? 243.599 195.065 168.334 1.00 143.49 ? 247  SER   A N    1 
ATOM   1905 C CA   . SER   A 1 234 ? 244.822 194.993 169.148 1.00 144.30 ? 247  SER   A CA   1 
ATOM   1906 C C    . SER   A 1 234 ? 246.064 195.594 168.484 1.00 145.06 ? 247  SER   A C    1 
ATOM   1907 O O    . SER   A 1 234 ? 246.907 196.165 169.173 1.00 144.39 ? 247  SER   A O    1 
ATOM   1908 C CB   . SER   A 1 234 ? 245.090 193.537 169.543 1.00 142.40 ? 247  SER   A CB   1 
ATOM   1909 O OG   . SER   A 1 234 ? 245.251 192.730 168.390 1.00 141.49 ? 247  SER   A OG   1 
ATOM   1910 N N    . ASN   A 1 235 ? 246.178 195.537 167.156 1.00 144.35 ? 248  ASN   A N    1 
ATOM   1911 C CA   . ASN   A 1 235 ? 247.333 196.081 166.442 1.00 143.06 ? 248  ASN   A CA   1 
ATOM   1912 C C    . ASN   A 1 235 ? 247.273 197.600 166.189 1.00 143.11 ? 248  ASN   A C    1 
ATOM   1913 O O    . ASN   A 1 235 ? 248.221 198.152 165.632 1.00 143.64 ? 248  ASN   A O    1 
ATOM   1914 C CB   . ASN   A 1 235 ? 247.576 195.272 165.157 1.00 143.21 ? 248  ASN   A CB   1 
ATOM   1915 C CG   . ASN   A 1 235 ? 246.682 195.671 164.000 1.00 145.17 ? 248  ASN   A CG   1 
ATOM   1916 O OD1  . ASN   A 1 235 ? 245.558 195.215 163.867 1.00 146.20 ? 248  ASN   A OD1  1 
ATOM   1917 N ND2  . ASN   A 1 235 ? 247.153 196.522 163.122 1.00 144.41 ? 248  ASN   A ND2  1 
ATOM   1918 N N    . THR   A 1 236 ? 246.181 198.280 166.557 1.00 142.43 ? 249  THR   A N    1 
ATOM   1919 C CA   . THR   A 1 236 ? 245.962 199.706 166.234 1.00 144.90 ? 249  THR   A CA   1 
ATOM   1920 C C    . THR   A 1 236 ? 245.598 200.575 167.439 1.00 144.77 ? 249  THR   A C    1 
ATOM   1921 O O    . THR   A 1 236 ? 246.126 201.679 167.555 1.00 143.53 ? 249  THR   A O    1 
ATOM   1922 C CB   . THR   A 1 236 ? 244.960 199.853 165.078 1.00 143.20 ? 249  THR   A CB   1 
ATOM   1923 O OG1  . THR   A 1 236 ? 244.793 201.201 164.709 1.00 142.93 ? 249  THR   A OG1  1 
ATOM   1924 C CG2  . THR   A 1 236 ? 243.561 199.340 165.392 1.00 141.25 ? 249  THR   A CG2  1 
ATOM   1925 N N    . ASP   A 1 237 ? 244.780 200.097 168.380 1.00 143.25 ? 250  ASP   A N    1 
ATOM   1926 C CA   . ASP   A 1 237 ? 244.411 200.881 169.571 1.00 142.58 ? 250  ASP   A CA   1 
ATOM   1927 C C    . ASP   A 1 237 ? 244.080 200.058 170.833 1.00 143.71 ? 250  ASP   A C    1 
ATOM   1928 O O    . ASP   A 1 237 ? 243.889 200.650 171.894 1.00 139.47 ? 250  ASP   A O    1 
ATOM   1929 C CB   . ASP   A 1 237 ? 243.264 201.846 169.220 1.00 139.64 ? 250  ASP   A CB   1 
ATOM   1930 C CG   . ASP   A 1 237 ? 242.017 201.164 168.657 1.00 141.11 ? 250  ASP   A CG   1 
ATOM   1931 O OD1  . ASP   A 1 237 ? 241.815 199.963 168.938 1.00 142.85 ? 250  ASP   A OD1  1 
ATOM   1932 O OD2  . ASP   A 1 237 ? 241.264 201.841 167.920 1.00 141.19 ? 250  ASP   A OD2  1 
ATOM   1933 N N    . ASN   A 1 238 ? 244.042 198.719 170.767 1.00 146.36 ? 251  ASN   A N    1 
ATOM   1934 C CA   . ASN   A 1 238 ? 243.603 197.837 171.863 1.00 144.88 ? 251  ASN   A CA   1 
ATOM   1935 C C    . ASN   A 1 238 ? 242.182 198.126 172.390 1.00 144.53 ? 251  ASN   A C    1 
ATOM   1936 O O    . ASN   A 1 238 ? 241.776 197.569 173.408 1.00 142.53 ? 251  ASN   A O    1 
ATOM   1937 C CB   . ASN   A 1 238 ? 244.666 197.776 172.986 1.00 143.35 ? 251  ASN   A CB   1 
ATOM   1938 C CG   . ASN   A 1 238 ? 245.742 196.735 172.755 1.00 145.39 ? 251  ASN   A CG   1 
ATOM   1939 O OD1  . ASN   A 1 238 ? 245.447 195.587 172.432 1.00 144.12 ? 251  ASN   A OD1  1 
ATOM   1940 N ND2  . ASN   A 1 238 ? 246.989 197.112 172.984 1.00 145.90 ? 251  ASN   A ND2  1 
ATOM   1941 N N    . GLU   A 1 239 ? 241.377 198.908 171.682 1.00 135.20 ? 252  GLU   A N    1 
ATOM   1942 C CA   . GLU   A 1 239 ? 239.986 199.157 172.039 1.00 130.74 ? 252  GLU   A CA   1 
ATOM   1943 C C    . GLU   A 1 239 ? 239.066 198.093 171.412 1.00 131.15 ? 252  GLU   A C    1 
ATOM   1944 O O    . GLU   A 1 239 ? 239.423 197.459 170.423 1.00 133.83 ? 252  GLU   A O    1 
ATOM   1945 C CB   . GLU   A 1 239 ? 239.645 200.592 171.628 1.00 128.27 ? 252  GLU   A CB   1 
ATOM   1946 C CG   . GLU   A 1 239 ? 238.379 201.119 172.301 1.00 130.55 ? 252  GLU   A CG   1 
ATOM   1947 C CD   . GLU   A 1 239 ? 238.494 201.233 173.831 1.00 134.19 ? 252  GLU   A CD   1 
ATOM   1948 O OE1  . GLU   A 1 239 ? 239.569 201.602 174.344 1.00 133.51 ? 252  GLU   A OE1  1 
ATOM   1949 O OE2  . GLU   A 1 239 ? 237.498 200.934 174.527 1.00 134.52 ? 252  GLU   A OE2  1 
ATOM   1950 N N    . THR   A 1 240 ? 237.877 197.857 171.971 1.00 114.89 ? 253  THR   A N    1 
ATOM   1951 C CA   . THR   A 1 240 ? 236.974 196.797 171.495 1.00 115.42 ? 253  THR   A CA   1 
ATOM   1952 C C    . THR   A 1 240 ? 235.505 197.176 171.625 1.00 113.38 ? 253  THR   A C    1 
ATOM   1953 O O    . THR   A 1 240 ? 235.129 197.949 172.503 1.00 115.43 ? 253  THR   A O    1 
ATOM   1954 C CB   . THR   A 1 240 ? 237.282 195.473 172.216 1.00 113.99 ? 253  THR   A CB   1 
ATOM   1955 O OG1  . THR   A 1 240 ? 236.537 194.406 171.675 1.00 111.95 ? 253  THR   A OG1  1 
ATOM   1956 C CG2  . THR   A 1 240 ? 237.010 195.492 173.718 1.00 109.24 ? 253  THR   A CG2  1 
ATOM   1957 N N    . LEU   A 1 241 ? 234.658 196.603 170.772 1.00 99.65  ? 254  LEU   A N    1 
ATOM   1958 C CA   . LEU   A 1 241 ? 233.212 196.532 170.989 1.00 96.87  ? 254  LEU   A CA   1 
ATOM   1959 C C    . LEU   A 1 241 ? 232.908 195.469 172.046 1.00 100.65 ? 254  LEU   A C    1 
ATOM   1960 O O    . LEU   A 1 241 ? 233.654 194.497 172.160 1.00 103.21 ? 254  LEU   A O    1 
ATOM   1961 C CB   . LEU   A 1 241 ? 232.494 196.149 169.685 1.00 94.37  ? 254  LEU   A CB   1 
ATOM   1962 C CG   . LEU   A 1 241 ? 232.794 197.037 168.479 1.00 97.47  ? 254  LEU   A CG   1 
ATOM   1963 C CD1  . LEU   A 1 241 ? 232.161 196.441 167.230 1.00 100.82 ? 254  LEU   A CD1  1 
ATOM   1964 C CD2  . LEU   A 1 241 ? 232.249 198.448 168.652 1.00 96.86  ? 254  LEU   A CD2  1 
ATOM   1965 N N    . GLN   A 1 242 ? 231.814 195.629 172.787 1.00 94.53  ? 255  GLN   A N    1 
ATOM   1966 C CA   . GLN   A 1 242 ? 231.194 194.563 173.576 1.00 93.25  ? 255  GLN   A CA   1 
ATOM   1967 C C    . GLN   A 1 242 ? 229.687 194.805 173.620 1.00 92.38  ? 255  GLN   A C    1 
ATOM   1968 O O    . GLN   A 1 242 ? 229.253 195.886 174.013 1.00 94.40  ? 255  GLN   A O    1 
ATOM   1969 C CB   . GLN   A 1 242 ? 231.737 194.502 175.010 1.00 93.86  ? 255  GLN   A CB   1 
ATOM   1970 C CG   . GLN   A 1 242 ? 233.249 194.296 175.156 1.00 94.88  ? 255  GLN   A CG   1 
ATOM   1971 C CD   . GLN   A 1 242 ? 233.716 194.282 176.606 1.00 96.62  ? 255  GLN   A CD   1 
ATOM   1972 O OE1  . GLN   A 1 242 ? 232.940 194.266 177.546 1.00 94.77  ? 255  GLN   A OE1  1 
ATOM   1973 N NE2  . GLN   A 1 242 ? 235.003 194.297 176.849 1.00 98.16  ? 255  GLN   A NE2  1 
ATOM   1974 N N    . TYR   A 1 243 ? 228.879 193.822 173.241 1.00 77.05  ? 256  TYR   A N    1 
ATOM   1975 C CA   . TYR   A 1 243 ? 227.420 193.907 173.280 1.00 75.39  ? 256  TYR   A CA   1 
ATOM   1976 C C    . TYR   A 1 243 ? 226.884 192.670 173.989 1.00 78.12  ? 256  TYR   A C    1 
ATOM   1977 O O    . TYR   A 1 243 ? 226.565 191.662 173.366 1.00 84.76  ? 256  TYR   A O    1 
ATOM   1978 C CB   . TYR   A 1 243 ? 226.847 194.117 171.870 1.00 76.85  ? 256  TYR   A CB   1 
ATOM   1979 C CG   . TYR   A 1 243 ? 225.407 194.584 171.868 1.00 76.42  ? 256  TYR   A CG   1 
ATOM   1980 C CD1  . TYR   A 1 243 ? 224.375 193.692 172.186 1.00 73.43  ? 256  TYR   A CD1  1 
ATOM   1981 C CD2  . TYR   A 1 243 ? 225.096 195.919 171.567 1.00 78.23  ? 256  TYR   A CD2  1 
ATOM   1982 C CE1  . TYR   A 1 243 ? 223.048 194.142 172.274 1.00 69.27  ? 256  TYR   A CE1  1 
ATOM   1983 C CE2  . TYR   A 1 243 ? 223.768 196.373 171.642 1.00 76.29  ? 256  TYR   A CE2  1 
ATOM   1984 C CZ   . TYR   A 1 243 ? 222.747 195.489 172.030 1.00 75.80  ? 256  TYR   A CZ   1 
ATOM   1985 O OH   . TYR   A 1 243 ? 221.478 195.927 172.179 1.00 83.89  ? 256  TYR   A OH   1 
ATOM   1986 N N    . TRP   A 1 244 ? 226.876 192.712 175.314 1.00 79.91  ? 257  TRP   A N    1 
ATOM   1987 C CA   . TRP   A 1 244 ? 226.471 191.605 176.159 1.00 78.87  ? 257  TRP   A CA   1 
ATOM   1988 C C    . TRP   A 1 244 ? 224.957 191.472 176.189 1.00 75.92  ? 257  TRP   A C    1 
ATOM   1989 O O    . TRP   A 1 244 ? 224.265 192.462 176.385 1.00 85.16  ? 257  TRP   A O    1 
ATOM   1990 C CB   . TRP   A 1 244 ? 227.018 191.848 177.561 1.00 82.04  ? 257  TRP   A CB   1 
ATOM   1991 C CG   . TRP   A 1 244 ? 228.497 191.916 177.656 1.00 81.23  ? 257  TRP   A CG   1 
ATOM   1992 C CD1  . TRP   A 1 244 ? 229.225 193.040 177.794 1.00 78.18  ? 257  TRP   A CD1  1 
ATOM   1993 C CD2  . TRP   A 1 244 ? 229.452 190.822 177.585 1.00 85.43  ? 257  TRP   A CD2  1 
ATOM   1994 N NE1  . TRP   A 1 244 ? 230.562 192.715 177.823 1.00 84.19  ? 257  TRP   A NE1  1 
ATOM   1995 C CE2  . TRP   A 1 244 ? 230.761 191.366 177.658 1.00 86.93  ? 257  TRP   A CE2  1 
ATOM   1996 C CE3  . TRP   A 1 244 ? 229.344 189.424 177.454 1.00 81.36  ? 257  TRP   A CE3  1 
ATOM   1997 C CZ2  . TRP   A 1 244 ? 231.910 190.575 177.572 1.00 84.78  ? 257  TRP   A CZ2  1 
ATOM   1998 C CZ3  . TRP   A 1 244 ? 230.492 188.616 177.377 1.00 86.08  ? 257  TRP   A CZ3  1 
ATOM   1999 C CH2  . TRP   A 1 244 ? 231.771 189.188 177.427 1.00 87.95  ? 257  TRP   A CH2  1 
ATOM   2000 N N    . VAL   A 1 245 ? 224.426 190.264 176.058 1.00 63.93  ? 258  VAL   A N    1 
ATOM   2001 C CA   . VAL   A 1 245 ? 222.983 189.996 176.046 1.00 59.86  ? 258  VAL   A CA   1 
ATOM   2002 C C    . VAL   A 1 245 ? 222.625 188.839 176.966 1.00 67.81  ? 258  VAL   A C    1 
ATOM   2003 O O    . VAL   A 1 245 ? 223.324 187.831 176.978 1.00 78.60  ? 258  VAL   A O    1 
ATOM   2004 C CB   . VAL   A 1 245 ? 222.503 189.712 174.618 1.00 63.81  ? 258  VAL   A CB   1 
ATOM   2005 C CG1  . VAL   A 1 245 ? 220.987 189.676 174.572 1.00 70.79  ? 258  VAL   A CG1  1 
ATOM   2006 C CG2  . VAL   A 1 245 ? 222.942 190.808 173.654 1.00 71.14  ? 258  VAL   A CG2  1 
ATOM   2007 N N    . THR   A 1 246 ? 221.539 188.956 177.721 1.00 66.14  ? 259  THR   A N    1 
ATOM   2008 C CA   . THR   A 1 246 ? 221.000 187.900 178.589 1.00 67.43  ? 259  THR   A CA   1 
ATOM   2009 C C    . THR   A 1 246 ? 219.476 187.824 178.418 1.00 68.12  ? 259  THR   A C    1 
ATOM   2010 O O    . THR   A 1 246 ? 218.838 188.865 178.264 1.00 73.46  ? 259  THR   A O    1 
ATOM   2011 C CB   . THR   A 1 246 ? 221.457 188.129 180.042 1.00 70.72  ? 259  THR   A CB   1 
ATOM   2012 O OG1  . THR   A 1 246 ? 221.264 186.981 180.821 1.00 79.09  ? 259  THR   A OG1  1 
ATOM   2013 C CG2  . THR   A 1 246 ? 220.741 189.263 180.753 1.00 63.17  ? 259  THR   A CG2  1 
ATOM   2014 N N    . PRO   A 1 247 ? 218.850 186.638 178.369 1.00 57.36  ? 260  PRO   A N    1 
ATOM   2015 C CA   . PRO   A 1 247 ? 217.423 186.522 178.100 1.00 58.46  ? 260  PRO   A CA   1 
ATOM   2016 C C    . PRO   A 1 247 ? 216.556 187.001 179.264 1.00 64.22  ? 260  PRO   A C    1 
ATOM   2017 O O    . PRO   A 1 247 ? 216.889 186.803 180.429 1.00 73.02  ? 260  PRO   A O    1 
ATOM   2018 C CB   . PRO   A 1 247 ? 217.183 185.047 177.799 1.00 56.08  ? 260  PRO   A CB   1 
ATOM   2019 C CG   . PRO   A 1 247 ? 218.292 184.349 178.569 1.00 59.88  ? 260  PRO   A CG   1 
ATOM   2020 C CD   . PRO   A 1 247 ? 219.455 185.324 178.444 1.00 55.30  ? 260  PRO   A CD   1 
ATOM   2021 N N    . LEU   A 1 248 ? 215.408 187.590 178.947 1.00 66.97  ? 261  LEU   A N    1 
ATOM   2022 C CA   . LEU   A 1 248 ? 214.356 187.916 179.909 1.00 59.36  ? 261  LEU   A CA   1 
ATOM   2023 C C    . LEU   A 1 248 ? 213.396 186.743 180.121 1.00 66.52  ? 261  LEU   A C    1 
ATOM   2024 O O    . LEU   A 1 248 ? 213.284 185.851 179.285 1.00 77.31  ? 261  LEU   A O    1 
ATOM   2025 C CB   . LEU   A 1 248 ? 213.576 189.149 179.431 1.00 59.99  ? 261  LEU   A CB   1 
ATOM   2026 C CG   . LEU   A 1 248 ? 214.440 190.399 179.280 1.00 58.68  ? 261  LEU   A CG   1 
ATOM   2027 C CD1  . LEU   A 1 248 ? 213.614 191.548 178.740 1.00 63.89  ? 261  LEU   A CD1  1 
ATOM   2028 C CD2  . LEU   A 1 248 ? 215.053 190.844 180.588 1.00 63.69  ? 261  LEU   A CD2  1 
ATOM   2029 N N    . SER   A 1 249 ? 212.640 186.777 181.211 1.00 69.19  ? 262  SER   A N    1 
ATOM   2030 C CA   . SER   A 1 249 ? 211.512 185.876 181.464 1.00 71.90  ? 262  SER   A CA   1 
ATOM   2031 C C    . SER   A 1 249 ? 210.428 186.609 182.253 1.00 73.02  ? 262  SER   A C    1 
ATOM   2032 O O    . SER   A 1 249 ? 210.737 187.580 182.943 1.00 79.23  ? 262  SER   A O    1 
ATOM   2033 C CB   . SER   A 1 249 ? 212.005 184.625 182.195 1.00 76.50  ? 262  SER   A CB   1 
ATOM   2034 O OG   . SER   A 1 249 ? 212.756 184.960 183.348 1.00 86.68  ? 262  SER   A OG   1 
ATOM   2035 N N    . LYS   A 1 250 ? 209.163 186.186 182.146 1.00 81.29  ? 263  LYS   A N    1 
ATOM   2036 C CA   . LYS   A 1 250 ? 208.056 186.727 182.956 1.00 79.10  ? 263  LYS   A CA   1 
ATOM   2037 C C    . LYS   A 1 250 ? 208.290 186.326 184.406 1.00 83.80  ? 263  LYS   A C    1 
ATOM   2038 O O    . LYS   A 1 250 ? 208.290 185.138 184.728 1.00 89.10  ? 263  LYS   A O    1 
ATOM   2039 C CB   . LYS   A 1 250 ? 206.699 186.234 182.427 1.00 82.16  ? 263  LYS   A CB   1 
ATOM   2040 C CG   . LYS   A 1 250 ? 205.484 186.585 183.309 1.00 82.17  ? 263  LYS   A CG   1 
ATOM   2041 C CD   . LYS   A 1 250 ? 205.244 188.080 183.569 1.00 81.68  ? 263  LYS   A CD   1 
ATOM   2042 C CE   . LYS   A 1 250 ? 204.775 188.883 182.352 1.00 87.72  ? 263  LYS   A CE   1 
ATOM   2043 N NZ   . LYS   A 1 250 ? 203.345 188.642 182.032 1.00 89.07  ? 263  LYS   A NZ   1 
ATOM   2044 N N    . ARG   A 1 251 ? 208.551 187.310 185.256 1.00 76.81  ? 264  ARG   A N    1 
ATOM   2045 C CA   . ARG   A 1 251 ? 209.216 187.137 186.546 1.00 69.94  ? 264  ARG   A CA   1 
ATOM   2046 C C    . ARG   A 1 251 ? 208.745 188.206 187.516 1.00 73.68  ? 264  ARG   A C    1 
ATOM   2047 O O    . ARG   A 1 251 ? 208.436 189.315 187.097 1.00 83.23  ? 264  ARG   A O    1 
ATOM   2048 C CB   . ARG   A 1 251 ? 210.710 187.210 186.217 1.00 65.09  ? 264  ARG   A CB   1 
ATOM   2049 C CG   . ARG   A 1 251 ? 211.693 187.052 187.371 1.00 72.83  ? 264  ARG   A CG   1 
ATOM   2050 C CD   . ARG   A 1 251 ? 213.085 186.789 186.776 1.00 69.91  ? 264  ARG   A CD   1 
ATOM   2051 N NE   . ARG   A 1 251 ? 213.190 185.410 186.286 1.00 71.44  ? 264  ARG   A NE   1 
ATOM   2052 C CZ   . ARG   A 1 251 ? 213.399 184.349 187.037 1.00 84.54  ? 264  ARG   A CZ   1 
ATOM   2053 N NH1  . ARG   A 1 251 ? 213.283 183.167 186.520 1.00 81.09  ? 264  ARG   A NH1  1 
ATOM   2054 N NH2  . ARG   A 1 251 ? 213.709 184.421 188.298 1.00 80.63  ? 264  ARG   A NH2  1 
ATOM   2055 N N    . GLN   A 1 252 ? 208.704 187.906 188.809 1.00 73.89  ? 265  GLN   A N    1 
ATOM   2056 C CA   . GLN   A 1 252 ? 208.233 188.849 189.818 1.00 67.80  ? 265  GLN   A CA   1 
ATOM   2057 C C    . GLN   A 1 252 ? 209.406 189.428 190.588 1.00 71.28  ? 265  GLN   A C    1 
ATOM   2058 O O    . GLN   A 1 252 ? 210.224 188.681 191.118 1.00 80.18  ? 265  GLN   A O    1 
ATOM   2059 C CB   . GLN   A 1 252 ? 207.232 188.159 190.742 1.00 67.25  ? 265  GLN   A CB   1 
ATOM   2060 C CG   . GLN   A 1 252 ? 206.588 189.137 191.733 1.00 72.35  ? 265  GLN   A CG   1 
ATOM   2061 C CD   . GLN   A 1 252 ? 205.550 188.433 192.591 1.00 81.66  ? 265  GLN   A CD   1 
ATOM   2062 O OE1  . GLN   A 1 252 ? 205.703 187.291 192.991 1.00 81.54  ? 265  GLN   A OE1  1 
ATOM   2063 N NE2  . GLN   A 1 252 ? 204.449 189.072 192.908 1.00 81.58  ? 265  GLN   A NE2  1 
ATOM   2064 N N    . TYR   A 1 253 ? 209.484 190.751 190.657 1.00 69.43  ? 266  TYR   A N    1 
ATOM   2065 C CA   . TYR   A 1 253 ? 210.522 191.486 191.365 1.00 63.60  ? 266  TYR   A CA   1 
ATOM   2066 C C    . TYR   A 1 253 ? 209.903 192.372 192.437 1.00 66.97  ? 266  TYR   A C    1 
ATOM   2067 O O    . TYR   A 1 253 ? 208.884 193.017 192.207 1.00 78.15  ? 266  TYR   A O    1 
ATOM   2068 C CB   . TYR   A 1 253 ? 211.318 192.367 190.396 1.00 57.27  ? 266  TYR   A CB   1 
ATOM   2069 C CG   . TYR   A 1 253 ? 212.571 191.762 189.798 1.00 62.98  ? 266  TYR   A CG   1 
ATOM   2070 C CD1  . TYR   A 1 253 ? 212.594 190.461 189.273 1.00 64.36  ? 266  TYR   A CD1  1 
ATOM   2071 C CD2  . TYR   A 1 253 ? 213.731 192.543 189.741 1.00 68.01  ? 266  TYR   A CD2  1 
ATOM   2072 C CE1  . TYR   A 1 253 ? 213.764 189.949 188.691 1.00 64.52  ? 266  TYR   A CE1  1 
ATOM   2073 C CE2  . TYR   A 1 253 ? 214.895 192.035 189.151 1.00 63.97  ? 266  TYR   A CE2  1 
ATOM   2074 C CZ   . TYR   A 1 253 ? 214.918 190.737 188.623 1.00 66.84  ? 266  TYR   A CZ   1 
ATOM   2075 O OH   . TYR   A 1 253 ? 216.043 190.255 188.046 1.00 81.34  ? 266  TYR   A OH   1 
ATOM   2076 N N    . LEU   A 1 254 ? 210.551 192.463 193.591 1.00 63.20  ? 267  LEU   A N    1 
ATOM   2077 C CA   . LEU   A 1 254 ? 210.332 193.557 194.522 1.00 64.65  ? 267  LEU   A CA   1 
ATOM   2078 C C    . LEU   A 1 254 ? 211.116 194.767 194.026 1.00 68.50  ? 267  LEU   A C    1 
ATOM   2079 O O    . LEU   A 1 254 ? 212.297 194.626 193.726 1.00 73.18  ? 267  LEU   A O    1 
ATOM   2080 C CB   . LEU   A 1 254 ? 210.809 193.133 195.918 1.00 68.49  ? 267  LEU   A CB   1 
ATOM   2081 C CG   . LEU   A 1 254 ? 210.437 194.125 197.025 1.00 71.49  ? 267  LEU   A CG   1 
ATOM   2082 C CD1  . LEU   A 1 254 ? 208.960 194.021 197.372 1.00 73.88  ? 267  LEU   A CD1  1 
ATOM   2083 C CD2  . LEU   A 1 254 ? 211.251 193.822 198.273 1.00 69.80  ? 267  LEU   A CD2  1 
ATOM   2084 N N    . LEU   A 1 255 ? 210.501 195.943 193.983 1.00 65.63  ? 268  LEU   A N    1 
ATOM   2085 C CA   . LEU   A 1 255 ? 211.148 197.205 193.641 1.00 62.54  ? 268  LEU   A CA   1 
ATOM   2086 C C    . LEU   A 1 255 ? 210.994 198.201 194.795 1.00 69.38  ? 268  LEU   A C    1 
ATOM   2087 O O    . LEU   A 1 255 ? 209.877 198.435 195.249 1.00 82.70  ? 268  LEU   A O    1 
ATOM   2088 C CB   . LEU   A 1 255 ? 210.533 197.746 192.339 1.00 64.97  ? 268  LEU   A CB   1 
ATOM   2089 C CG   . LEU   A 1 255 ? 210.610 196.788 191.141 1.00 65.67  ? 268  LEU   A CG   1 
ATOM   2090 C CD1  . LEU   A 1 255 ? 209.876 197.405 189.965 1.00 70.83  ? 268  LEU   A CD1  1 
ATOM   2091 C CD2  . LEU   A 1 255 ? 212.046 196.541 190.699 1.00 62.97  ? 268  LEU   A CD2  1 
ATOM   2092 N N    . LYS   A 1 256 ? 212.089 198.796 195.273 1.00 65.23  ? 269  LYS   A N    1 
ATOM   2093 C CA   . LYS   A 1 256 ? 212.113 199.777 196.372 1.00 66.28  ? 269  LYS   A CA   1 
ATOM   2094 C C    . LYS   A 1 256 ? 212.356 201.168 195.808 1.00 71.01  ? 269  LYS   A C    1 
ATOM   2095 O O    . LYS   A 1 256 ? 213.413 201.405 195.239 1.00 75.51  ? 269  LYS   A O    1 
ATOM   2096 C CB   . LYS   A 1 256 ? 213.236 199.361 197.339 1.00 74.75  ? 269  LYS   A CB   1 
ATOM   2097 C CG   . LYS   A 1 256 ? 213.576 200.324 198.489 1.00 77.07  ? 269  LYS   A CG   1 
ATOM   2098 C CD   . LYS   A 1 256 ? 212.545 200.328 199.619 1.00 74.52  ? 269  LYS   A CD   1 
ATOM   2099 C CE   . LYS   A 1 256 ? 213.031 201.073 200.866 1.00 79.46  ? 269  LYS   A CE   1 
ATOM   2100 N NZ   . LYS   A 1 256 ? 213.166 202.531 200.653 1.00 82.31  ? 269  LYS   A NZ   1 
ATOM   2101 N N    . PHE   A 1 257 ? 211.432 202.095 196.019 1.00 76.97  ? 270  PHE   A N    1 
ATOM   2102 C CA   . PHE   A 1 257 ? 211.522 203.492 195.597 1.00 72.15  ? 270  PHE   A CA   1 
ATOM   2103 C C    . PHE   A 1 257 ? 211.752 204.414 196.792 1.00 76.87  ? 270  PHE   A C    1 
ATOM   2104 O O    . PHE   A 1 257 ? 211.058 204.297 197.802 1.00 80.24  ? 270  PHE   A O    1 
ATOM   2105 C CB   . PHE   A 1 257 ? 210.234 203.904 194.894 1.00 71.38  ? 270  PHE   A CB   1 
ATOM   2106 C CG   . PHE   A 1 257 ? 209.935 203.156 193.620 1.00 72.86  ? 270  PHE   A CG   1 
ATOM   2107 C CD1  . PHE   A 1 257 ? 209.236 201.940 193.658 1.00 72.23  ? 270  PHE   A CD1  1 
ATOM   2108 C CD2  . PHE   A 1 257 ? 210.299 203.711 192.384 1.00 76.43  ? 270  PHE   A CD2  1 
ATOM   2109 C CE1  . PHE   A 1 257 ? 208.908 201.288 192.463 1.00 70.03  ? 270  PHE   A CE1  1 
ATOM   2110 C CE2  . PHE   A 1 257 ? 209.954 203.064 191.189 1.00 72.33  ? 270  PHE   A CE2  1 
ATOM   2111 C CZ   . PHE   A 1 257 ? 209.263 201.846 191.229 1.00 68.70  ? 270  PHE   A CZ   1 
ATOM   2112 N N    . ASP   A 1 258 ? 212.699 205.342 196.702 1.00 85.24  ? 271  ASP   A N    1 
ATOM   2113 C CA   . ASP   A 1 258 ? 212.873 206.383 197.723 1.00 87.21  ? 271  ASP   A CA   1 
ATOM   2114 C C    . ASP   A 1 258 ? 211.863 207.534 197.561 1.00 93.73  ? 271  ASP   A C    1 
ATOM   2115 O O    . ASP   A 1 258 ? 210.996 207.518 196.689 1.00 95.94  ? 271  ASP   A O    1 
ATOM   2116 C CB   . ASP   A 1 258 ? 214.331 206.868 197.745 1.00 89.54  ? 271  ASP   A CB   1 
ATOM   2117 C CG   . ASP   A 1 258 ? 214.770 207.732 196.557 1.00 97.65  ? 271  ASP   A CG   1 
ATOM   2118 O OD1  . ASP   A 1 258 ? 213.915 208.104 195.723 1.00 101.82 ? 271  ASP   A OD1  1 
ATOM   2119 O OD2  . ASP   A 1 258 ? 215.963 208.113 196.523 1.00 102.67 ? 271  ASP   A OD2  1 
ATOM   2120 N N    . ASN   A 1 259 ? 211.947 208.562 198.403 1.00 97.99  ? 272  ASN   A N    1 
ATOM   2121 C CA   . ASN   A 1 259 ? 211.047 209.718 198.360 1.00 94.74  ? 272  ASN   A CA   1 
ATOM   2122 C C    . ASN   A 1 259 ? 211.238 210.649 197.146 1.00 91.79  ? 272  ASN   A C    1 
ATOM   2123 O O    . ASN   A 1 259 ? 210.417 211.541 196.945 1.00 94.02  ? 272  ASN   A O    1 
ATOM   2124 C CB   . ASN   A 1 259 ? 211.141 210.478 199.692 1.00 97.94  ? 272  ASN   A CB   1 
ATOM   2125 C CG   . ASN   A 1 259 ? 212.507 211.090 199.931 1.00 105.28 ? 272  ASN   A CG   1 
ATOM   2126 O OD1  . ASN   A 1 259 ? 213.511 210.401 200.002 1.00 103.76 ? 272  ASN   A OD1  1 
ATOM   2127 N ND2  . ASN   A 1 259 ? 212.598 212.392 200.047 1.00 102.50 ? 272  ASN   A ND2  1 
ATOM   2128 N N    . ARG   A 1 260 ? 212.277 210.457 196.325 1.00 87.69  ? 273  ARG   A N    1 
ATOM   2129 C CA   . ARG   A 1 260 ? 212.435 211.129 195.021 1.00 90.90  ? 273  ARG   A CA   1 
ATOM   2130 C C    . ARG   A 1 260 ? 211.788 210.323 193.894 1.00 93.52  ? 273  ARG   A C    1 
ATOM   2131 O O    . ARG   A 1 260 ? 211.534 210.856 192.818 1.00 91.52  ? 273  ARG   A O    1 
ATOM   2132 C CB   . ARG   A 1 260 ? 213.922 211.316 194.704 1.00 90.87  ? 273  ARG   A CB   1 
ATOM   2133 C CG   . ARG   A 1 260 ? 214.708 212.072 195.785 1.00 93.55  ? 273  ARG   A CG   1 
ATOM   2134 C CD   . ARG   A 1 260 ? 216.205 212.065 195.464 1.00 95.05  ? 273  ARG   A CD   1 
ATOM   2135 N NE   . ARG   A 1 260 ? 216.758 210.697 195.526 1.00 105.06 ? 273  ARG   A NE   1 
ATOM   2136 C CZ   . ARG   A 1 260 ? 217.920 210.280 195.075 1.00 101.85 ? 273  ARG   A CZ   1 
ATOM   2137 N NH1  . ARG   A 1 260 ? 218.215 209.025 195.209 1.00 95.89  ? 273  ARG   A NH1  1 
ATOM   2138 N NH2  . ARG   A 1 260 ? 218.780 211.069 194.502 1.00 98.57  ? 273  ARG   A NH2  1 
ATOM   2139 N N    . GLY   A 1 261 ? 211.543 209.040 194.126 1.00 87.65  ? 274  GLY   A N    1 
ATOM   2140 C CA   . GLY   A 1 261 ? 211.062 208.090 193.139 1.00 80.84  ? 274  GLY   A CA   1 
ATOM   2141 C C    . GLY   A 1 261 ? 212.167 207.324 192.422 1.00 81.33  ? 274  GLY   A C    1 
ATOM   2142 O O    . GLY   A 1 261 ? 211.911 206.771 191.361 1.00 88.26  ? 274  GLY   A O    1 
ATOM   2143 N N    . VAL   A 1 262 ? 213.392 207.291 192.948 1.00 75.74  ? 275  VAL   A N    1 
ATOM   2144 C CA   . VAL   A 1 262 ? 214.498 206.498 192.390 1.00 79.16  ? 275  VAL   A CA   1 
ATOM   2145 C C    . VAL   A 1 262 ? 214.407 205.064 192.898 1.00 84.61  ? 275  VAL   A C    1 
ATOM   2146 O O    . VAL   A 1 262 ? 214.227 204.864 194.097 1.00 89.57  ? 275  VAL   A O    1 
ATOM   2147 C CB   . VAL   A 1 262 ? 215.849 207.116 192.780 1.00 78.76  ? 275  VAL   A CB   1 
ATOM   2148 C CG1  . VAL   A 1 262 ? 217.052 206.281 192.325 1.00 80.68  ? 275  VAL   A CG1  1 
ATOM   2149 C CG2  . VAL   A 1 262 ? 215.993 208.507 192.160 1.00 81.87  ? 275  VAL   A CG2  1 
ATOM   2150 N N    . ILE   A 1 263 ? 214.581 204.056 192.038 1.00 73.63  ? 276  ILE   A N    1 
ATOM   2151 C CA   . ILE   A 1 263 ? 214.699 202.665 192.503 1.00 70.56  ? 276  ILE   A CA   1 
ATOM   2152 C C    . ILE   A 1 263 ? 216.056 202.503 193.180 1.00 74.69  ? 276  ILE   A C    1 
ATOM   2153 O O    . ILE   A 1 263 ? 217.083 202.573 192.516 1.00 75.20  ? 276  ILE   A O    1 
ATOM   2154 C CB   . ILE   A 1 263 ? 214.489 201.631 191.381 1.00 69.67  ? 276  ILE   A CB   1 
ATOM   2155 C CG1  . ILE   A 1 263 ? 213.066 201.704 190.802 1.00 75.21  ? 276  ILE   A CG1  1 
ATOM   2156 C CG2  . ILE   A 1 263 ? 214.791 200.205 191.859 1.00 70.40  ? 276  ILE   A CG2  1 
ATOM   2157 C CD1  . ILE   A 1 263 ? 212.899 200.958 189.477 1.00 73.75  ? 276  ILE   A CD1  1 
ATOM   2158 N N    . THR   A 1 264 ? 216.084 202.289 194.492 1.00 71.31  ? 277  THR   A N    1 
ATOM   2159 C CA   . THR   A 1 264 ? 217.330 202.109 195.252 1.00 67.56  ? 277  THR   A CA   1 
ATOM   2160 C C    . THR   A 1 264 ? 217.728 200.648 195.407 1.00 70.19  ? 277  THR   A C    1 
ATOM   2161 O O    . THR   A 1 264 ? 218.911 200.358 195.550 1.00 76.87  ? 277  THR   A O    1 
ATOM   2162 C CB   . THR   A 1 264 ? 217.261 202.750 196.643 1.00 74.04  ? 277  THR   A CB   1 
ATOM   2163 O OG1  . THR   A 1 264 ? 216.330 202.105 197.471 1.00 76.97  ? 277  THR   A OG1  1 
ATOM   2164 C CG2  . THR   A 1 264 ? 216.860 204.214 196.582 1.00 73.48  ? 277  THR   A CG2  1 
ATOM   2165 N N    . ASN   A 1 265 ? 216.771 199.719 195.377 1.00 71.04  ? 278  ASN   A N    1 
ATOM   2166 C CA   . ASN   A 1 265 ? 217.011 198.287 195.531 1.00 72.51  ? 278  ASN   A CA   1 
ATOM   2167 C C    . ASN   A 1 265 ? 215.974 197.473 194.764 1.00 73.84  ? 278  ASN   A C    1 
ATOM   2168 O O    . ASN   A 1 265 ? 214.869 197.953 194.514 1.00 79.83  ? 278  ASN   A O    1 
ATOM   2169 C CB   . ASN   A 1 265 ? 216.984 197.877 197.014 1.00 71.80  ? 278  ASN   A CB   1 
ATOM   2170 C CG   . ASN   A 1 265 ? 217.897 198.689 197.903 1.00 81.05  ? 278  ASN   A CG   1 
ATOM   2171 O OD1  . ASN   A 1 265 ? 217.540 199.763 198.367 1.00 83.79  ? 278  ASN   A OD1  1 
ATOM   2172 N ND2  . ASN   A 1 265 ? 219.079 198.203 198.185 1.00 83.23  ? 278  ASN   A ND2  1 
ATOM   2173 N N    . ALA   A 1 266 ? 216.300 196.223 194.459 1.00 66.44  ? 279  ALA   A N    1 
ATOM   2174 C CA   . ALA   A 1 266 ? 215.353 195.255 193.922 1.00 65.01  ? 279  ALA   A CA   1 
ATOM   2175 C C    . ALA   A 1 266 ? 215.693 193.818 194.337 1.00 73.88  ? 279  ALA   A C    1 
ATOM   2176 O O    . ALA   A 1 266 ? 216.823 193.532 194.729 1.00 80.28  ? 279  ALA   A O    1 
ATOM   2177 C CB   . ALA   A 1 266 ? 215.294 195.397 192.406 1.00 70.16  ? 279  ALA   A CB   1 
ATOM   2178 N N    . VAL   A 1 267 ? 214.720 192.911 194.261 1.00 71.18  ? 280  VAL   A N    1 
ATOM   2179 C CA   . VAL   A 1 267 ? 214.889 191.492 194.608 1.00 67.80  ? 280  VAL   A CA   1 
ATOM   2180 C C    . VAL   A 1 267 ? 214.208 190.622 193.562 1.00 68.92  ? 280  VAL   A C    1 
ATOM   2181 O O    . VAL   A 1 267 ? 213.102 190.948 193.149 1.00 76.93  ? 280  VAL   A O    1 
ATOM   2182 C CB   . VAL   A 1 267 ? 214.326 191.180 196.003 1.00 68.72  ? 280  VAL   A CB   1 
ATOM   2183 C CG1  . VAL   A 1 267 ? 214.756 189.785 196.452 1.00 69.93  ? 280  VAL   A CG1  1 
ATOM   2184 C CG2  . VAL   A 1 267 ? 214.775 192.172 197.076 1.00 69.87  ? 280  VAL   A CG2  1 
ATOM   2185 N N    . ASP   A 1 268 ? 214.827 189.517 193.147 1.00 73.71  ? 281  ASP   A N    1 
ATOM   2186 C CA   . ASP   A 1 268 ? 214.312 188.614 192.109 1.00 77.68  ? 281  ASP   A CA   1 
ATOM   2187 C C    . ASP   A 1 268 ? 213.145 187.728 192.586 1.00 79.43  ? 281  ASP   A C    1 
ATOM   2188 O O    . ASP   A 1 268 ? 213.233 187.018 193.594 1.00 89.32  ? 281  ASP   A O    1 
ATOM   2189 C CB   . ASP   A 1 268 ? 215.486 187.804 191.546 1.00 76.60  ? 281  ASP   A CB   1 
ATOM   2190 C CG   . ASP   A 1 268 ? 215.157 186.921 190.335 1.00 85.45  ? 281  ASP   A CG   1 
ATOM   2191 O OD1  . ASP   A 1 268 ? 213.970 186.759 189.977 1.00 90.47  ? 281  ASP   A OD1  1 
ATOM   2192 O OD2  . ASP   A 1 268 ? 216.105 186.354 189.753 1.00 85.15  ? 281  ASP   A OD2  1 
HETATM 2193 C C1   . NAG   B 2 .   ? 211.139 194.014 149.124 1.00 110.26 ? 1    NAG   B C1   1 
HETATM 2194 C C2   . NAG   B 2 .   ? 211.578 194.925 147.959 1.00 108.90 ? 1    NAG   B C2   1 
HETATM 2195 C C3   . NAG   B 2 .   ? 211.781 194.058 146.706 1.00 108.77 ? 1    NAG   B C3   1 
HETATM 2196 C C4   . NAG   B 2 .   ? 212.667 192.841 146.971 1.00 113.64 ? 1    NAG   B C4   1 
HETATM 2197 C C5   . NAG   B 2 .   ? 212.152 192.032 148.158 1.00 112.83 ? 1    NAG   B C5   1 
HETATM 2198 C C6   . NAG   B 2 .   ? 212.986 190.804 148.518 1.00 111.74 ? 1    NAG   B C6   1 
HETATM 2199 C C7   . NAG   B 2 .   ? 210.657 197.207 148.006 1.00 112.73 ? 1    NAG   B C7   1 
HETATM 2200 C C8   . NAG   B 2 .   ? 209.393 198.050 147.866 1.00 109.44 ? 1    NAG   B C8   1 
HETATM 2201 N N2   . NAG   B 2 .   ? 210.529 195.918 147.725 1.00 106.78 ? 1    NAG   B N2   1 
HETATM 2202 O O3   . NAG   B 2 .   ? 212.382 194.827 145.636 1.00 110.23 ? 1    NAG   B O3   1 
HETATM 2203 O O4   . NAG   B 2 .   ? 212.572 192.007 145.771 1.00 115.45 ? 1    NAG   B O4   1 
HETATM 2204 O O5   . NAG   B 2 .   ? 212.083 192.926 149.320 1.00 113.95 ? 1    NAG   B O5   1 
HETATM 2205 O O6   . NAG   B 2 .   ? 214.330 191.189 148.822 1.00 114.10 ? 1    NAG   B O6   1 
HETATM 2206 O O7   . NAG   B 2 .   ? 211.723 197.684 148.370 1.00 113.73 ? 1    NAG   B O7   1 
HETATM 2207 C C1   . NAG   B 2 .   ? 213.839 191.711 145.113 1.00 124.66 ? 2    NAG   B C1   1 
HETATM 2208 C C2   . NAG   B 2 .   ? 213.641 190.518 144.158 1.00 123.62 ? 2    NAG   B C2   1 
HETATM 2209 C C3   . NAG   B 2 .   ? 214.960 190.244 143.413 1.00 125.47 ? 2    NAG   B C3   1 
HETATM 2210 C C4   . NAG   B 2 .   ? 215.386 191.499 142.650 1.00 127.87 ? 2    NAG   B C4   1 
HETATM 2211 C C5   . NAG   B 2 .   ? 215.550 192.681 143.612 1.00 123.92 ? 2    NAG   B C5   1 
HETATM 2212 C C6   . NAG   B 2 .   ? 215.929 193.986 142.906 1.00 123.73 ? 2    NAG   B C6   1 
HETATM 2213 C C7   . NAG   B 2 .   ? 211.917 188.993 145.022 1.00 127.15 ? 2    NAG   B C7   1 
HETATM 2214 C C8   . NAG   B 2 .   ? 211.640 187.700 145.801 1.00 125.69 ? 2    NAG   B C8   1 
HETATM 2215 N N2   . NAG   B 2 .   ? 213.196 189.333 144.894 1.00 124.19 ? 2    NAG   B N2   1 
HETATM 2216 O O3   . NAG   B 2 .   ? 214.807 189.143 142.479 1.00 125.79 ? 2    NAG   B O3   1 
HETATM 2217 O O4   . NAG   B 2 .   ? 216.678 191.232 141.980 1.00 133.35 ? 2    NAG   B O4   1 
HETATM 2218 O O5   . NAG   B 2 .   ? 214.285 192.885 144.354 1.00 122.32 ? 2    NAG   B O5   1 
HETATM 2219 O O6   . NAG   B 2 .   ? 214.950 194.300 141.900 1.00 124.72 ? 2    NAG   B O6   1 
HETATM 2220 O O7   . NAG   B 2 .   ? 211.009 189.670 144.547 1.00 125.77 ? 2    NAG   B O7   1 
HETATM 2221 C C1   . BMA   B 2 .   ? 216.620 191.304 140.515 1.00 156.17 ? 3    BMA   B C1   1 
HETATM 2222 C C2   . BMA   B 2 .   ? 218.054 191.403 139.969 1.00 155.57 ? 3    BMA   B C2   1 
HETATM 2223 C C3   . BMA   B 2 .   ? 218.050 191.405 138.430 1.00 156.08 ? 3    BMA   B C3   1 
HETATM 2224 C C4   . BMA   B 2 .   ? 217.333 190.148 137.905 1.00 157.39 ? 3    BMA   B C4   1 
HETATM 2225 C C5   . BMA   B 2 .   ? 215.925 189.999 138.509 1.00 155.46 ? 3    BMA   B C5   1 
HETATM 2226 C C6   . BMA   B 2 .   ? 215.264 188.666 138.155 1.00 153.74 ? 3    BMA   B C6   1 
HETATM 2227 O O2   . BMA   B 2 .   ? 218.815 190.269 140.451 1.00 153.81 ? 3    BMA   B O2   1 
HETATM 2228 O O3   . BMA   B 2 .   ? 219.426 191.447 137.868 1.00 155.67 ? 3    BMA   B O3   1 
HETATM 2229 O O4   . BMA   B 2 .   ? 217.211 190.228 136.463 1.00 156.43 ? 3    BMA   B O4   1 
HETATM 2230 O O5   . BMA   B 2 .   ? 215.987 190.094 139.986 1.00 157.31 ? 3    BMA   B O5   1 
HETATM 2231 O O6   . BMA   B 2 .   ? 216.057 187.547 138.699 1.00 156.37 ? 3    BMA   B O6   1 
HETATM 2232 C C1   . MAN   B 2 .   ? 220.203 192.661 138.129 1.00 157.53 ? 4    MAN   B C1   1 
HETATM 2233 C C2   . MAN   B 2 .   ? 221.228 192.875 136.995 1.00 157.12 ? 4    MAN   B C2   1 
HETATM 2234 C C3   . MAN   B 2 .   ? 222.295 191.777 137.023 1.00 158.32 ? 4    MAN   B C3   1 
HETATM 2235 C C4   . MAN   B 2 .   ? 222.965 191.665 138.401 1.00 159.37 ? 4    MAN   B C4   1 
HETATM 2236 C C5   . MAN   B 2 .   ? 221.908 191.479 139.503 1.00 159.63 ? 4    MAN   B C5   1 
HETATM 2237 C C6   . MAN   B 2 .   ? 222.485 191.489 140.924 1.00 157.17 ? 4    MAN   B C6   1 
HETATM 2238 O O2   . MAN   B 2 .   ? 221.892 194.162 137.148 1.00 154.42 ? 4    MAN   B O2   1 
HETATM 2239 O O3   . MAN   B 2 .   ? 223.301 192.087 136.022 1.00 157.24 ? 4    MAN   B O3   1 
HETATM 2240 O O4   . MAN   B 2 .   ? 223.839 190.513 138.358 1.00 154.73 ? 4    MAN   B O4   1 
HETATM 2241 O O5   . MAN   B 2 .   ? 220.897 192.564 139.422 1.00 158.86 ? 4    MAN   B O5   1 
HETATM 2242 O O6   . MAN   B 2 .   ? 222.911 192.821 141.277 1.00 155.46 ? 4    MAN   B O6   1 
HETATM 2243 C C1   . MAN   B 2 .   ? 215.980 186.352 137.864 1.00 166.74 ? 5    MAN   B C1   1 
HETATM 2244 C C2   . MAN   B 2 .   ? 216.364 185.102 138.693 1.00 166.09 ? 5    MAN   B C2   1 
HETATM 2245 C C3   . MAN   B 2 .   ? 217.878 185.024 138.942 1.00 165.76 ? 5    MAN   B C3   1 
HETATM 2246 C C4   . MAN   B 2 .   ? 218.684 185.184 137.642 1.00 166.46 ? 5    MAN   B C4   1 
HETATM 2247 C C5   . MAN   B 2 .   ? 218.316 186.527 136.998 1.00 167.88 ? 5    MAN   B C5   1 
HETATM 2248 C C6   . MAN   B 2 .   ? 219.084 186.854 135.711 1.00 165.22 ? 5    MAN   B C6   1 
HETATM 2249 O O2   . MAN   B 2 .   ? 215.953 183.891 137.990 1.00 164.01 ? 5    MAN   B O2   1 
HETATM 2250 O O3   . MAN   B 2 .   ? 218.176 183.737 139.541 1.00 162.42 ? 5    MAN   B O3   1 
HETATM 2251 O O4   . MAN   B 2 .   ? 220.095 185.159 137.972 1.00 162.63 ? 5    MAN   B O4   1 
HETATM 2252 O O5   . MAN   B 2 .   ? 216.860 186.515 136.697 1.00 168.61 ? 5    MAN   B O5   1 
HETATM 2253 O O6   . MAN   B 2 .   ? 218.721 188.178 135.253 1.00 164.39 ? 5    MAN   B O6   1 
HETATM 2254 C C1   . NAG   C 3 .   ? 217.808 211.056 164.127 1.00 118.87 ? 1    NAG   C C1   1 
HETATM 2255 C C2   . NAG   C 3 .   ? 217.324 212.226 163.245 1.00 119.08 ? 1    NAG   C C2   1 
HETATM 2256 C C3   . NAG   C 3 .   ? 217.802 212.014 161.798 1.00 119.55 ? 1    NAG   C C3   1 
HETATM 2257 C C4   . NAG   C 3 .   ? 219.335 211.909 161.787 1.00 119.11 ? 1    NAG   C C4   1 
HETATM 2258 C C5   . NAG   C 3 .   ? 219.838 210.811 162.734 1.00 116.77 ? 1    NAG   C C5   1 
HETATM 2259 C C6   . NAG   C 3 .   ? 221.363 210.793 162.868 1.00 118.75 ? 1    NAG   C C6   1 
HETATM 2260 C C7   . NAG   C 3 .   ? 214.948 211.553 163.136 1.00 120.54 ? 1    NAG   C C7   1 
HETATM 2261 C C8   . NAG   C 3 .   ? 213.539 211.929 163.536 1.00 116.55 ? 1    NAG   C C8   1 
HETATM 2262 N N2   . NAG   C 3 .   ? 215.884 212.466 163.368 1.00 120.31 ? 1    NAG   C N2   1 
HETATM 2263 O O3   . NAG   C 3 .   ? 217.383 213.131 160.973 1.00 121.83 ? 1    NAG   C O3   1 
HETATM 2264 O O4   . NAG   C 3 .   ? 219.799 211.570 160.427 1.00 121.71 ? 1    NAG   C O4   1 
HETATM 2265 O O5   . NAG   C 3 .   ? 219.263 210.997 164.083 1.00 116.99 ? 1    NAG   C O5   1 
HETATM 2266 O O6   . NAG   C 3 .   ? 221.828 212.067 163.349 1.00 118.91 ? 1    NAG   C O6   1 
HETATM 2267 O O7   . NAG   C 3 .   ? 215.214 210.459 162.654 1.00 119.00 ? 1    NAG   C O7   1 
HETATM 2268 C C1   . NAG   C 3 .   ? 220.310 212.680 159.611 1.00 136.60 ? 2    NAG   C C1   1 
HETATM 2269 C C2   . NAG   C 3 .   ? 221.264 212.134 158.528 1.00 138.41 ? 2    NAG   C C2   1 
HETATM 2270 C C3   . NAG   C 3 .   ? 221.708 213.267 157.592 1.00 138.68 ? 2    NAG   C C3   1 
HETATM 2271 C C4   . NAG   C 3 .   ? 220.494 213.981 156.983 1.00 138.94 ? 2    NAG   C C4   1 
HETATM 2272 C C5   . NAG   C 3 .   ? 219.549 214.508 158.076 1.00 136.89 ? 2    NAG   C C5   1 
HETATM 2273 C C6   . NAG   C 3 .   ? 218.239 215.091 157.527 1.00 135.23 ? 2    NAG   C C6   1 
HETATM 2274 C C7   . NAG   C 3 .   ? 222.650 210.207 159.152 1.00 137.20 ? 2    NAG   C C7   1 
HETATM 2275 C C8   . NAG   C 3 .   ? 223.929 209.741 159.845 1.00 133.67 ? 2    NAG   C C8   1 
HETATM 2276 N N2   . NAG   C 3 .   ? 222.433 211.515 159.160 1.00 136.67 ? 2    NAG   C N2   1 
HETATM 2277 O O3   . NAG   C 3 .   ? 222.538 212.756 156.515 1.00 134.39 ? 2    NAG   C O3   1 
HETATM 2278 O O4   . NAG   C 3 .   ? 220.999 215.096 156.214 1.00 136.02 ? 2    NAG   C O4   1 
HETATM 2279 O O5   . NAG   C 3 .   ? 219.187 213.386 158.973 1.00 136.64 ? 2    NAG   C O5   1 
HETATM 2280 O O6   . NAG   C 3 .   ? 218.521 216.221 156.677 1.00 136.96 ? 2    NAG   C O6   1 
HETATM 2281 O O7   . NAG   C 3 .   ? 221.873 209.416 158.623 1.00 137.65 ? 2    NAG   C O7   1 
HETATM 2282 C C1   . NAG   D 4 .   ? 225.015 189.490 144.108 1.00 135.29 ? 1301 NAG   A C1   1 
HETATM 2283 C C2   . NAG   D 4 .   ? 225.205 188.232 143.221 1.00 135.51 ? 1301 NAG   A C2   1 
HETATM 2284 C C3   . NAG   D 4 .   ? 226.553 188.303 142.482 1.00 136.26 ? 1301 NAG   A C3   1 
HETATM 2285 C C4   . NAG   D 4 .   ? 226.673 189.624 141.701 1.00 138.06 ? 1301 NAG   A C4   1 
HETATM 2286 C C5   . NAG   D 4 .   ? 226.483 190.820 142.649 1.00 135.04 ? 1301 NAG   A C5   1 
HETATM 2287 C C6   . NAG   D 4 .   ? 226.604 192.201 141.993 1.00 133.98 ? 1301 NAG   A C6   1 
HETATM 2288 C C7   . NAG   D 4 .   ? 223.970 186.388 144.243 1.00 134.56 ? 1301 NAG   A C7   1 
HETATM 2289 C C8   . NAG   D 4 .   ? 224.026 185.137 145.125 1.00 132.21 ? 1301 NAG   A C8   1 
HETATM 2290 N N2   . NAG   D 4 .   ? 225.128 187.006 144.021 1.00 133.90 ? 1301 NAG   A N2   1 
HETATM 2291 O O3   . NAG   D 4 .   ? 226.685 187.195 141.549 1.00 133.12 ? 1301 NAG   A O3   1 
HETATM 2292 O O4   . NAG   D 4 .   ? 227.992 189.666 141.110 1.00 135.59 ? 1301 NAG   A O4   1 
HETATM 2293 O O5   . NAG   D 4 .   ? 225.152 190.698 143.289 1.00 133.41 ? 1301 NAG   A O5   1 
HETATM 2294 O O6   . NAG   D 4 .   ? 225.645 192.354 140.936 1.00 135.28 ? 1301 NAG   A O6   1 
HETATM 2295 O O7   . NAG   D 4 .   ? 222.916 186.806 143.764 1.00 134.23 ? 1301 NAG   A O7   1 
HETATM 2296 C C1   . NAG   E 4 .   ? 233.703 177.247 165.277 1.00 123.25 ? 1302 NAG   A C1   1 
HETATM 2297 C C2   . NAG   E 4 .   ? 232.984 175.884 165.293 1.00 124.16 ? 1302 NAG   A C2   1 
HETATM 2298 C C3   . NAG   E 4 .   ? 232.460 175.609 166.712 1.00 124.83 ? 1302 NAG   A C3   1 
HETATM 2299 C C4   . NAG   E 4 .   ? 233.635 175.620 167.701 1.00 123.62 ? 1302 NAG   A C4   1 
HETATM 2300 C C5   . NAG   E 4 .   ? 234.433 176.933 167.629 1.00 123.32 ? 1302 NAG   A C5   1 
HETATM 2301 C C6   . NAG   E 4 .   ? 235.704 176.926 168.488 1.00 121.28 ? 1302 NAG   A C6   1 
HETATM 2302 C C7   . NAG   E 4 .   ? 230.891 176.576 164.149 1.00 123.23 ? 1302 NAG   A C7   1 
HETATM 2303 C C8   . NAG   E 4 .   ? 230.027 176.384 162.905 1.00 120.00 ? 1302 NAG   A C8   1 
HETATM 2304 N N2   . NAG   E 4 .   ? 231.947 175.777 164.254 1.00 123.16 ? 1302 NAG   A N2   1 
HETATM 2305 O O3   . NAG   E 4 .   ? 231.800 174.315 166.779 1.00 124.26 ? 1302 NAG   A O3   1 
HETATM 2306 O O4   . NAG   E 4 .   ? 233.084 175.474 169.028 1.00 118.16 ? 1302 NAG   A O4   1 
HETATM 2307 O O5   . NAG   E 4 .   ? 234.817 177.215 166.222 1.00 122.18 ? 1302 NAG   A O5   1 
HETATM 2308 O O6   . NAG   E 4 .   ? 236.610 175.903 168.029 1.00 120.84 ? 1302 NAG   A O6   1 
HETATM 2309 O O7   . NAG   E 4 .   ? 230.624 177.414 165.001 1.00 124.21 ? 1302 NAG   A O7   1 
HETATM 2310 C C1   . NAG   F 4 .   ? 208.364 207.315 203.915 1.00 114.93 ? 1303 NAG   A C1   1 
HETATM 2311 C C2   . NAG   F 4 .   ? 207.906 208.513 204.771 1.00 116.09 ? 1303 NAG   A C2   1 
HETATM 2312 C C3   . NAG   F 4 .   ? 208.234 208.238 206.245 1.00 117.96 ? 1303 NAG   A C3   1 
HETATM 2313 C C4   . NAG   F 4 .   ? 207.600 206.922 206.711 1.00 119.23 ? 1303 NAG   A C4   1 
HETATM 2314 C C5   . NAG   F 4 .   ? 207.972 205.744 205.794 1.00 118.42 ? 1303 NAG   A C5   1 
HETATM 2315 C C6   . NAG   F 4 .   ? 207.209 204.456 206.132 1.00 117.29 ? 1303 NAG   A C6   1 
HETATM 2316 C C7   . NAG   F 4 .   ? 208.060 210.500 203.354 1.00 116.33 ? 1303 NAG   A C7   1 
HETATM 2317 C C8   . NAG   F 4 .   ? 208.872 211.740 202.965 1.00 111.88 ? 1303 NAG   A C8   1 
HETATM 2318 N N2   . NAG   F 4 .   ? 208.562 209.745 204.325 1.00 116.27 ? 1303 NAG   A N2   1 
HETATM 2319 O O3   . NAG   F 4 .   ? 207.741 209.317 207.088 1.00 117.63 ? 1303 NAG   A O3   1 
HETATM 2320 O O4   . NAG   F 4 .   ? 208.097 206.660 208.043 1.00 111.97 ? 1303 NAG   A O4   1 
HETATM 2321 O O5   . NAG   F 4 .   ? 207.698 206.101 204.381 1.00 114.85 ? 1303 NAG   A O5   1 
HETATM 2322 O O6   . NAG   F 4 .   ? 205.791 204.640 205.942 1.00 116.22 ? 1303 NAG   A O6   1 
HETATM 2323 O O7   . NAG   F 4 .   ? 207.014 210.196 202.783 1.00 114.70 ? 1303 NAG   A O7   1 
HETATM 2324 C C1   . NAG   G 4 .   ? 231.494 202.742 148.676 1.00 148.15 ? 1304 NAG   A C1   1 
HETATM 2325 C C2   . NAG   G 4 .   ? 231.707 201.771 147.489 1.00 148.42 ? 1304 NAG   A C2   1 
HETATM 2326 C C3   . NAG   G 4 .   ? 232.605 202.441 146.431 1.00 149.22 ? 1304 NAG   A C3   1 
HETATM 2327 C C4   . NAG   G 4 .   ? 231.990 203.777 145.983 1.00 149.27 ? 1304 NAG   A C4   1 
HETATM 2328 C C5   . NAG   G 4 .   ? 231.684 204.705 147.172 1.00 148.59 ? 1304 NAG   A C5   1 
HETATM 2329 C C6   . NAG   G 4 .   ? 230.933 205.985 146.774 1.00 147.03 ? 1304 NAG   A C6   1 
HETATM 2330 C C7   . NAG   G 4 .   ? 233.312 200.225 148.594 1.00 146.96 ? 1304 NAG   A C7   1 
HETATM 2331 C C8   . NAG   G 4 .   ? 233.632 198.776 148.904 1.00 145.02 ? 1304 NAG   A C8   1 
HETATM 2332 N N2   . NAG   G 4 .   ? 232.204 200.444 147.892 1.00 147.34 ? 1304 NAG   A N2   1 
HETATM 2333 O O3   . NAG   G 4 .   ? 232.755 201.585 145.264 1.00 147.17 ? 1304 NAG   A O3   1 
HETATM 2334 O O4   . NAG   G 4 .   ? 232.946 204.428 145.117 1.00 145.58 ? 1304 NAG   A O4   1 
HETATM 2335 O O5   . NAG   G 4 .   ? 230.878 203.973 148.182 1.00 148.20 ? 1304 NAG   A O5   1 
HETATM 2336 O O6   . NAG   G 4 .   ? 229.640 205.657 146.226 1.00 146.44 ? 1304 NAG   A O6   1 
HETATM 2337 O O7   . NAG   G 4 .   ? 234.036 201.144 148.962 1.00 145.84 ? 1304 NAG   A O7   1 
HETATM 2338 C C1   . NAG   H 4 .   ? 228.623 211.600 181.545 1.00 116.03 ? 1305 NAG   A C1   1 
HETATM 2339 C C2   . NAG   H 4 .   ? 228.259 212.348 182.845 1.00 116.60 ? 1305 NAG   A C2   1 
HETATM 2340 C C3   . NAG   H 4 .   ? 229.519 212.586 183.684 1.00 117.73 ? 1305 NAG   A C3   1 
HETATM 2341 C C4   . NAG   H 4 .   ? 230.226 211.258 183.970 1.00 118.32 ? 1305 NAG   A C4   1 
HETATM 2342 C C5   . NAG   H 4 .   ? 230.606 210.552 182.665 1.00 118.89 ? 1305 NAG   A C5   1 
HETATM 2343 C C6   . NAG   H 4 .   ? 231.248 209.177 182.888 1.00 117.52 ? 1305 NAG   A C6   1 
HETATM 2344 C C7   . NAG   H 4 .   ? 226.319 213.743 182.320 1.00 116.58 ? 1305 NAG   A C7   1 
HETATM 2345 C C8   . NAG   H 4 .   ? 225.824 215.114 181.860 1.00 114.03 ? 1305 NAG   A C8   1 
HETATM 2346 N N2   . NAG   H 4 .   ? 227.626 213.628 182.519 1.00 117.69 ? 1305 NAG   A N2   1 
HETATM 2347 O O3   . NAG   H 4 .   ? 229.182 213.216 184.950 1.00 115.52 ? 1305 NAG   A O3   1 
HETATM 2348 O O4   . NAG   H 4 .   ? 231.424 211.563 184.714 1.00 113.31 ? 1305 NAG   A O4   1 
HETATM 2349 O O5   . NAG   H 4 .   ? 229.397 210.390 181.827 1.00 116.13 ? 1305 NAG   A O5   1 
HETATM 2350 O O6   . NAG   H 4 .   ? 230.298 208.270 183.477 1.00 118.52 ? 1305 NAG   A O6   1 
HETATM 2351 O O7   . NAG   H 4 .   ? 225.556 212.794 182.476 1.00 115.15 ? 1305 NAG   A O7   1 
HETATM 2352 C C1   . NAG   I 4 .   ? 248.114 196.202 172.905 1.00 149.20 ? 1306 NAG   A C1   1 
HETATM 2353 C C2   . NAG   I 4 .   ? 249.419 196.916 172.490 1.00 149.13 ? 1306 NAG   A C2   1 
HETATM 2354 C C3   . NAG   I 4 .   ? 250.580 195.914 172.564 1.00 149.56 ? 1306 NAG   A C3   1 
HETATM 2355 C C4   . NAG   I 4 .   ? 250.692 195.329 173.978 1.00 152.09 ? 1306 NAG   A C4   1 
HETATM 2356 C C5   . NAG   I 4 .   ? 249.370 194.696 174.448 1.00 150.74 ? 1306 NAG   A C5   1 
HETATM 2357 C C6   . NAG   I 4 .   ? 249.382 194.259 175.920 1.00 148.07 ? 1306 NAG   A C6   1 
HETATM 2358 C C7   . NAG   I 4 .   ? 248.817 198.694 170.918 1.00 148.96 ? 1306 NAG   A C7   1 
HETATM 2359 C C8   . NAG   I 4 .   ? 248.633 199.112 169.455 1.00 146.30 ? 1306 NAG   A C8   1 
HETATM 2360 N N2   . NAG   I 4 .   ? 249.297 197.473 171.138 1.00 149.36 ? 1306 NAG   A N2   1 
HETATM 2361 O O3   . NAG   I 4 .   ? 251.838 196.560 172.223 1.00 147.59 ? 1306 NAG   A O3   1 
HETATM 2362 O O4   . NAG   I 4 .   ? 251.712 194.308 173.928 1.00 148.96 ? 1306 NAG   A O4   1 
HETATM 2363 O O5   . NAG   I 4 .   ? 248.256 195.656 174.254 1.00 150.02 ? 1306 NAG   A O5   1 
HETATM 2364 O O6   . NAG   I 4 .   ? 249.496 195.411 176.780 1.00 147.65 ? 1306 NAG   A O6   1 
HETATM 2365 O O7   . NAG   I 4 .   ? 248.531 199.448 171.848 1.00 148.54 ? 1306 NAG   A O7   1 
HETATM 2366 C C21  . A1AR1 J 5 .   ? 244.675 192.458 159.164 1.00 136.44 ? 1307 A1AR1 A C21  1 
HETATM 2367 C C6   . A1AR1 J 5 .   ? 238.473 190.198 163.187 1.00 130.90 ? 1307 A1AR1 A C6   1 
HETATM 2368 C C7   . A1AR1 J 5 .   ? 238.211 189.059 162.182 1.00 129.62 ? 1307 A1AR1 A C7   1 
HETATM 2369 C C8   . A1AR1 J 5 .   ? 239.000 189.360 160.870 1.00 129.18 ? 1307 A1AR1 A C8   1 
HETATM 2370 C C11  . A1AR1 J 5 .   ? 234.291 188.838 164.594 1.00 127.26 ? 1307 A1AR1 A C11  1 
HETATM 2371 C C10  . A1AR1 J 5 .   ? 235.789 188.709 164.497 1.00 128.65 ? 1307 A1AR1 A C10  1 
HETATM 2372 C C9   . A1AR1 J 5 .   ? 238.762 188.297 159.773 1.00 129.83 ? 1307 A1AR1 A C9   1 
HETATM 2373 C C5   . A1AR1 J 5 .   ? 237.911 190.044 164.613 1.00 130.52 ? 1307 A1AR1 A C5   1 
HETATM 2374 C C4   . A1AR1 J 5 .   ? 238.280 191.348 165.370 1.00 129.81 ? 1307 A1AR1 A C4   1 
HETATM 2375 C C3   . A1AR1 J 5 .   ? 239.790 191.644 165.311 1.00 131.14 ? 1307 A1AR1 A C3   1 
HETATM 2376 C C2   . A1AR1 J 5 .   ? 240.330 191.592 163.858 1.00 134.51 ? 1307 A1AR1 A C2   1 
HETATM 2377 O O6   . A1AR1 J 5 .   ? 239.901 190.334 163.310 1.00 134.14 ? 1307 A1AR1 A O6   1 
HETATM 2378 C C1   . A1AR1 J 5 .   ? 239.921 192.844 162.954 1.00 131.92 ? 1307 A1AR1 A C1   1 
HETATM 2379 C C12  . A1AR1 J 5 .   ? 243.424 191.885 158.335 1.00 134.98 ? 1307 A1AR1 A C12  1 
HETATM 2380 C C31  . A1AR1 J 5 .   ? 245.009 193.934 158.820 1.00 132.76 ? 1307 A1AR1 A C31  1 
HETATM 2381 C C41  . A1AR1 J 5 .   ? 243.882 194.875 159.282 1.00 132.08 ? 1307 A1AR1 A C41  1 
HETATM 2382 C C51  . A1AR1 J 5 .   ? 243.597 194.707 160.803 1.00 130.19 ? 1307 A1AR1 A C51  1 
HETATM 2383 C C61  . A1AR1 J 5 .   ? 243.360 193.203 161.087 1.00 129.07 ? 1307 A1AR1 A C61  1 
HETATM 2384 C C71  . A1AR1 J 5 .   ? 243.162 192.870 162.583 1.00 129.98 ? 1307 A1AR1 A C71  1 
HETATM 2385 C C81  . A1AR1 J 5 .   ? 242.469 191.493 162.721 1.00 133.77 ? 1307 A1AR1 A C81  1 
HETATM 2386 C C91  . A1AR1 J 5 .   ? 243.381 190.260 162.679 1.00 131.24 ? 1307 A1AR1 A C91  1 
HETATM 2387 C CA9  . A1AR1 J 5 .   ? 236.961 187.511 158.397 1.00 132.07 ? 1307 A1AR1 A CA9  1 
HETATM 2388 C CM9  . A1AR1 J 5 .   ? 235.462 187.501 158.277 1.00 130.71 ? 1307 A1AR1 A CM9  1 
HETATM 2389 N N5   . A1AR1 J 5 .   ? 236.456 189.886 164.603 1.00 128.62 ? 1307 A1AR1 A N5   1 
HETATM 2390 N N51  . A1AR1 J 5 .   ? 242.415 195.498 161.224 1.00 131.59 ? 1307 A1AR1 A N51  1 
HETATM 2391 O O10  . A1AR1 J 5 .   ? 236.360 187.647 164.323 1.00 130.45 ? 1307 A1AR1 A O10  1 
HETATM 2392 O O1A  . A1AR1 J 5 .   ? 239.852 193.930 163.489 1.00 130.69 ? 1307 A1AR1 A O1A  1 
HETATM 2393 O O1B  . A1AR1 J 5 .   ? 239.558 192.662 161.791 1.00 132.18 ? 1307 A1AR1 A O1B  1 
HETATM 2394 O O3   . A1AR1 J 5 .   ? 245.845 191.666 158.950 1.00 137.44 ? 1307 A1AR1 A O3   1 
HETATM 2395 O O4   . A1AR1 J 5 .   ? 237.852 191.287 166.726 1.00 130.10 ? 1307 A1AR1 A O4   1 
HETATM 2396 O O41  . A1AR1 J 5 .   ? 244.235 196.222 158.966 1.00 130.36 ? 1307 A1AR1 A O41  1 
HETATM 2397 O O61  . A1AR1 J 5 .   ? 244.475 192.423 160.591 1.00 134.80 ? 1307 A1AR1 A O61  1 
HETATM 2398 O O7   . A1AR1 J 5 .   ? 238.600 187.805 162.739 1.00 127.24 ? 1307 A1AR1 A O7   1 
HETATM 2399 O O71  . A1AR1 J 5 .   ? 244.378 192.903 163.337 1.00 131.15 ? 1307 A1AR1 A O71  1 
HETATM 2400 O O8   . A1AR1 J 5 .   ? 238.667 190.669 160.373 1.00 129.55 ? 1307 A1AR1 A O8   1 
HETATM 2401 O O81  . A1AR1 J 5 .   ? 241.761 191.466 163.977 1.00 136.95 ? 1307 A1AR1 A O81  1 
HETATM 2402 O O9   . A1AR1 J 5 .   ? 237.359 188.243 159.466 1.00 131.31 ? 1307 A1AR1 A O9   1 
HETATM 2403 O O91  . A1AR1 J 5 .   ? 242.548 189.115 162.847 1.00 129.73 ? 1307 A1AR1 A O91  1 
HETATM 2404 O OA9  . A1AR1 J 5 .   ? 237.713 186.936 157.629 1.00 132.68 ? 1307 A1AR1 A OA9  1 
HETATM 2405 C C101 . A1AR1 J 5 .   ? 242.397 196.705 161.870 1.00 132.78 ? 1307 A1AR1 A C101 1 
HETATM 2406 C C111 . A1AR1 J 5 .   ? 243.700 197.458 162.077 1.00 131.36 ? 1307 A1AR1 A C111 1 
HETATM 2407 O O101 . A1AR1 J 5 .   ? 241.344 197.148 162.280 1.00 135.67 ? 1307 A1AR1 A O101 1 
HETATM 2408 O O1A1 . A1AR1 J 5 .   ? 242.663 191.106 158.891 1.00 132.23 ? 1307 A1AR1 A O1A1 1 
HETATM 2409 O O1B1 . A1AR1 J 5 .   ? 243.158 192.389 157.255 1.00 134.19 ? 1307 A1AR1 A O1B1 1 
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