data_9N15
# 
_entry.id   9N15 
# 
_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   9N15         pdb_00009n15 10.2210/pdb9n15/pdb 
WWPDB D_1000290934 ?            ?                   
EMDB  EMD-48806    ?            ?                   
# 
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                        9N15 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-24 
_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 structure of HCoV-HKU1 glycoprotein D1 Domain in complex with 9OAc-GD3(mutant T31VPR34 to GGGG)' 
_pdbx_database_related.db_id          EMD-48806 
_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' 150406.391 1 ? ? ? ? 
2 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    3 ? ? ? ? 
3 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 ? ? ? ? 
4 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542    1 
? ? ? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    2 ? ? ? ? 
6 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       
;VIGDFNCTNFAINDLNTGGGGISEYVVDVSYGLGTYYILDRVYLNTTILFTGYFPKSGANFRDLSLKGTTYLSTLWYQKP
FLSDFNNGIFSRVKNTKLYVNKTLYSEFSTIVIGSVFINNSYTIVVQPHNGVLEITACQYTMCEYPHTICKSKGSSRNES
WHFDKSEPLCLFKKNFTYNVSTDWLYFHFYQERGTFYAYYADSGMPTTFLFSLYLGTLLSHYYVLPLTCNAISSNTDNET
LQYWVTPLSKRQYLLKFDNRGVITNAVDCSSSFFSEIQCKTKSLLPNTGVYDLSGFTVKPVATVHRRIPDLPDCDIDKWL
NNFNVPSPLNWERKIFSNCNFNLSTLLRLVHTDSFSCNNFDESKIYGSCFKSIVLDKFAIPNSRRSDLQLGSSGFLQSSN
YKIDTTSSSCQLYYSLPAINVTINNYNPSSWNRRYGFNNFNLSSHSVVYSRYCFSVNNTFCPCAKPSFASSCKSHKPPSA
SCPIGTNYRSCESTTVLDHTDWCRCSCLPDPITAYDPRSCSQKKSLVGVGEHCAGFGVDEEKCGVLDGSYNVSCLCSTDA
FLGWSYDTCVSNNRCNIFSNFILNGINSGTTCSNDLLQPNTEVFTDVCVDYDLYGITGQGIFKEVSAVYYNSWQNLLYDS
NGNIIGFKDFVTNKTYNIFPCYAGRVSAAFHQNASSLALLYRNLKCSYVLNNISLTTQPYFDSYLGCVFNADNLTDYSVS
SCALRMGSGFCVDYNSPSSSSSRRKRRSISASYRFVTFEPFNVSFVNDSIESVGGLYEIKIPTNFTIVGQEEFIQTNSPK
VTIDCSLFVCSNYAACHDLLSEYGTFCDNINSILDEVNGLLDTTQLHVADTLMQGVTLSSNLNTNLHFDVDNINFKSLVG
CLGPHCGSSSRSFFEDLLFDKVKLSDVGFVEAYNNCTGGSEIRDLLCVQSFNGIKVLPPILSESQISGYTTAATVAAMFP
PWSAAAGIPFSLNVQYRINGLGVTMDVLNKNQKLIATAFNNALLSIQNGFSAPNSALAKIQSVVNSNAQALNSLLQQLFN
KFGAISSSLQEILSRLDPPEAQVQIDRLINGRLTALNAYVSQQLSDISLVKFGAALAMEKVNECVKSQSPRINFCGNGNH
ILSLVQNAPYGLLFMHFSYKPISFKTVLVSPGLCISGDVGIAPKQGYFIKHNDHWMFTGSSYYYPEPISDKNVVFMNTCS
VNFTKAPLVYLNHSVPKLSDFESELSHWFKNQTSIAPNLTLNLHTINATFLDLYYEMNLIQESIKSLNNSYINLKDIGTY
EMYVKSGGYIPEAPRDGQAYVRKDGEWVLLSTFLNSGRAHHHHHHGAGGLNDIFEAQKIEWHEDTAAA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VIGDFNCTNFAINDLNTGGGGISEYVVDVSYGLGTYYILDRVYLNTTILFTGYFPKSGANFRDLSLKGTTYLSTLWYQKP
FLSDFNNGIFSRVKNTKLYVNKTLYSEFSTIVIGSVFINNSYTIVVQPHNGVLEITACQYTMCEYPHTICKSKGSSRNES
WHFDKSEPLCLFKKNFTYNVSTDWLYFHFYQERGTFYAYYADSGMPTTFLFSLYLGTLLSHYYVLPLTCNAISSNTDNET
LQYWVTPLSKRQYLLKFDNRGVITNAVDCSSSFFSEIQCKTKSLLPNTGVYDLSGFTVKPVATVHRRIPDLPDCDIDKWL
NNFNVPSPLNWERKIFSNCNFNLSTLLRLVHTDSFSCNNFDESKIYGSCFKSIVLDKFAIPNSRRSDLQLGSSGFLQSSN
YKIDTTSSSCQLYYSLPAINVTINNYNPSSWNRRYGFNNFNLSSHSVVYSRYCFSVNNTFCPCAKPSFASSCKSHKPPSA
SCPIGTNYRSCESTTVLDHTDWCRCSCLPDPITAYDPRSCSQKKSLVGVGEHCAGFGVDEEKCGVLDGSYNVSCLCSTDA
FLGWSYDTCVSNNRCNIFSNFILNGINSGTTCSNDLLQPNTEVFTDVCVDYDLYGITGQGIFKEVSAVYYNSWQNLLYDS
NGNIIGFKDFVTNKTYNIFPCYAGRVSAAFHQNASSLALLYRNLKCSYVLNNISLTTQPYFDSYLGCVFNADNLTDYSVS
SCALRMGSGFCVDYNSPSSSSSRRKRRSISASYRFVTFEPFNVSFVNDSIESVGGLYEIKIPTNFTIVGQEEFIQTNSPK
VTIDCSLFVCSNYAACHDLLSEYGTFCDNINSILDEVNGLLDTTQLHVADTLMQGVTLSSNLNTNLHFDVDNINFKSLVG
CLGPHCGSSSRSFFEDLLFDKVKLSDVGFVEAYNNCTGGSEIRDLLCVQSFNGIKVLPPILSESQISGYTTAATVAAMFP
PWSAAAGIPFSLNVQYRINGLGVTMDVLNKNQKLIATAFNNALLSIQNGFSAPNSALAKIQSVVNSNAQALNSLLQQLFN
KFGAISSSLQEILSRLDPPEAQVQIDRLINGRLTALNAYVSQQLSDISLVKFGAALAMEKVNECVKSQSPRINFCGNGNH
ILSLVQNAPYGLLFMHFSYKPISFKTVLVSPGLCISGDVGIAPKQGYFIKHNDHWMFTGSSYYYPEPISDKNVVFMNTCS
VNFTKAPLVYLNHSVPKLSDFESELSHWFKNQTSIAPNLTLNLHTINATFLDLYYEMNLIQESIKSLNNSYINLKDIGTY
EMYVKSGGYIPEAPRDGQAYVRKDGEWVLLSTFLNSGRAHHHHHHGAGGLNDIFEAQKIEWHEDTAAA
;
_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 
5 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
6 
;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   GLY n 
1 19   GLY n 
1 20   GLY n 
1 21   GLY 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  PRO n 
1 738  SER n 
1 739  SER n 
1 740  SER n 
1 741  SER n 
1 742  SER n 
1 743  ARG n 
1 744  ARG n 
1 745  LYS n 
1 746  ARG n 
1 747  ARG n 
1 748  SER n 
1 749  ILE n 
1 750  SER n 
1 751  ALA n 
1 752  SER n 
1 753  TYR n 
1 754  ARG n 
1 755  PHE n 
1 756  VAL n 
1 757  THR n 
1 758  PHE n 
1 759  GLU n 
1 760  PRO n 
1 761  PHE n 
1 762  ASN n 
1 763  VAL n 
1 764  SER n 
1 765  PHE n 
1 766  VAL n 
1 767  ASN n 
1 768  ASP n 
1 769  SER n 
1 770  ILE n 
1 771  GLU n 
1 772  SER n 
1 773  VAL n 
1 774  GLY n 
1 775  GLY n 
1 776  LEU n 
1 777  TYR n 
1 778  GLU n 
1 779  ILE n 
1 780  LYS n 
1 781  ILE n 
1 782  PRO n 
1 783  THR n 
1 784  ASN n 
1 785  PHE n 
1 786  THR n 
1 787  ILE n 
1 788  VAL n 
1 789  GLY n 
1 790  GLN n 
1 791  GLU n 
1 792  GLU n 
1 793  PHE n 
1 794  ILE n 
1 795  GLN n 
1 796  THR n 
1 797  ASN n 
1 798  SER n 
1 799  PRO n 
1 800  LYS n 
1 801  VAL n 
1 802  THR n 
1 803  ILE n 
1 804  ASP n 
1 805  CYS n 
1 806  SER n 
1 807  LEU n 
1 808  PHE n 
1 809  VAL n 
1 810  CYS n 
1 811  SER n 
1 812  ASN n 
1 813  TYR n 
1 814  ALA n 
1 815  ALA n 
1 816  CYS n 
1 817  HIS n 
1 818  ASP n 
1 819  LEU n 
1 820  LEU n 
1 821  SER n 
1 822  GLU n 
1 823  TYR n 
1 824  GLY n 
1 825  THR n 
1 826  PHE n 
1 827  CYS n 
1 828  ASP n 
1 829  ASN n 
1 830  ILE n 
1 831  ASN n 
1 832  SER n 
1 833  ILE n 
1 834  LEU n 
1 835  ASP n 
1 836  GLU n 
1 837  VAL n 
1 838  ASN n 
1 839  GLY n 
1 840  LEU n 
1 841  LEU n 
1 842  ASP n 
1 843  THR n 
1 844  THR n 
1 845  GLN n 
1 846  LEU n 
1 847  HIS n 
1 848  VAL n 
1 849  ALA n 
1 850  ASP n 
1 851  THR n 
1 852  LEU n 
1 853  MET n 
1 854  GLN n 
1 855  GLY n 
1 856  VAL n 
1 857  THR n 
1 858  LEU n 
1 859  SER n 
1 860  SER n 
1 861  ASN n 
1 862  LEU n 
1 863  ASN n 
1 864  THR n 
1 865  ASN n 
1 866  LEU n 
1 867  HIS n 
1 868  PHE n 
1 869  ASP n 
1 870  VAL n 
1 871  ASP n 
1 872  ASN n 
1 873  ILE n 
1 874  ASN n 
1 875  PHE n 
1 876  LYS n 
1 877  SER n 
1 878  LEU n 
1 879  VAL n 
1 880  GLY n 
1 881  CYS n 
1 882  LEU n 
1 883  GLY n 
1 884  PRO n 
1 885  HIS n 
1 886  CYS n 
1 887  GLY n 
1 888  SER n 
1 889  SER n 
1 890  SER n 
1 891  ARG n 
1 892  SER n 
1 893  PHE n 
1 894  PHE n 
1 895  GLU n 
1 896  ASP n 
1 897  LEU n 
1 898  LEU n 
1 899  PHE n 
1 900  ASP n 
1 901  LYS n 
1 902  VAL n 
1 903  LYS n 
1 904  LEU n 
1 905  SER n 
1 906  ASP n 
1 907  VAL n 
1 908  GLY n 
1 909  PHE n 
1 910  VAL n 
1 911  GLU n 
1 912  ALA n 
1 913  TYR n 
1 914  ASN n 
1 915  ASN n 
1 916  CYS n 
1 917  THR n 
1 918  GLY n 
1 919  GLY n 
1 920  SER n 
1 921  GLU n 
1 922  ILE n 
1 923  ARG n 
1 924  ASP n 
1 925  LEU n 
1 926  LEU n 
1 927  CYS n 
1 928  VAL n 
1 929  GLN n 
1 930  SER n 
1 931  PHE n 
1 932  ASN n 
1 933  GLY n 
1 934  ILE n 
1 935  LYS n 
1 936  VAL n 
1 937  LEU n 
1 938  PRO n 
1 939  PRO n 
1 940  ILE n 
1 941  LEU n 
1 942  SER n 
1 943  GLU n 
1 944  SER n 
1 945  GLN n 
1 946  ILE n 
1 947  SER n 
1 948  GLY n 
1 949  TYR n 
1 950  THR n 
1 951  THR n 
1 952  ALA n 
1 953  ALA n 
1 954  THR n 
1 955  VAL n 
1 956  ALA n 
1 957  ALA n 
1 958  MET n 
1 959  PHE n 
1 960  PRO n 
1 961  PRO n 
1 962  TRP n 
1 963  SER n 
1 964  ALA n 
1 965  ALA n 
1 966  ALA n 
1 967  GLY n 
1 968  ILE n 
1 969  PRO n 
1 970  PHE n 
1 971  SER n 
1 972  LEU n 
1 973  ASN n 
1 974  VAL n 
1 975  GLN n 
1 976  TYR n 
1 977  ARG n 
1 978  ILE n 
1 979  ASN n 
1 980  GLY n 
1 981  LEU n 
1 982  GLY n 
1 983  VAL n 
1 984  THR n 
1 985  MET n 
1 986  ASP n 
1 987  VAL n 
1 988  LEU n 
1 989  ASN n 
1 990  LYS n 
1 991  ASN n 
1 992  GLN n 
1 993  LYS n 
1 994  LEU n 
1 995  ILE n 
1 996  ALA n 
1 997  THR n 
1 998  ALA n 
1 999  PHE n 
1 1000 ASN n 
1 1001 ASN n 
1 1002 ALA n 
1 1003 LEU n 
1 1004 LEU n 
1 1005 SER n 
1 1006 ILE n 
1 1007 GLN n 
1 1008 ASN n 
1 1009 GLY n 
1 1010 PHE n 
1 1011 SER n 
1 1012 ALA n 
1 1013 PRO n 
1 1014 ASN n 
1 1015 SER n 
1 1016 ALA n 
1 1017 LEU n 
1 1018 ALA n 
1 1019 LYS n 
1 1020 ILE n 
1 1021 GLN n 
1 1022 SER n 
1 1023 VAL n 
1 1024 VAL n 
1 1025 ASN n 
1 1026 SER n 
1 1027 ASN n 
1 1028 ALA n 
1 1029 GLN n 
1 1030 ALA n 
1 1031 LEU n 
1 1032 ASN n 
1 1033 SER n 
1 1034 LEU n 
1 1035 LEU n 
1 1036 GLN n 
1 1037 GLN n 
1 1038 LEU n 
1 1039 PHE n 
1 1040 ASN n 
1 1041 LYS n 
1 1042 PHE n 
1 1043 GLY n 
1 1044 ALA n 
1 1045 ILE n 
1 1046 SER n 
1 1047 SER n 
1 1048 SER n 
1 1049 LEU n 
1 1050 GLN n 
1 1051 GLU n 
1 1052 ILE n 
1 1053 LEU n 
1 1054 SER n 
1 1055 ARG n 
1 1056 LEU n 
1 1057 ASP n 
1 1058 PRO n 
1 1059 PRO n 
1 1060 GLU n 
1 1061 ALA n 
1 1062 GLN n 
1 1063 VAL n 
1 1064 GLN n 
1 1065 ILE n 
1 1066 ASP n 
1 1067 ARG n 
1 1068 LEU n 
1 1069 ILE n 
1 1070 ASN n 
1 1071 GLY n 
1 1072 ARG n 
1 1073 LEU n 
1 1074 THR n 
1 1075 ALA n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 ALA n 
1 1079 TYR n 
1 1080 VAL n 
1 1081 SER n 
1 1082 GLN n 
1 1083 GLN n 
1 1084 LEU n 
1 1085 SER n 
1 1086 ASP n 
1 1087 ILE n 
1 1088 SER n 
1 1089 LEU n 
1 1090 VAL n 
1 1091 LYS n 
1 1092 PHE n 
1 1093 GLY n 
1 1094 ALA n 
1 1095 ALA n 
1 1096 LEU n 
1 1097 ALA n 
1 1098 MET n 
1 1099 GLU n 
1 1100 LYS n 
1 1101 VAL n 
1 1102 ASN n 
1 1103 GLU n 
1 1104 CYS n 
1 1105 VAL n 
1 1106 LYS n 
1 1107 SER n 
1 1108 GLN n 
1 1109 SER n 
1 1110 PRO n 
1 1111 ARG n 
1 1112 ILE n 
1 1113 ASN n 
1 1114 PHE n 
1 1115 CYS n 
1 1116 GLY n 
1 1117 ASN n 
1 1118 GLY n 
1 1119 ASN n 
1 1120 HIS n 
1 1121 ILE n 
1 1122 LEU n 
1 1123 SER n 
1 1124 LEU n 
1 1125 VAL n 
1 1126 GLN n 
1 1127 ASN n 
1 1128 ALA n 
1 1129 PRO n 
1 1130 TYR n 
1 1131 GLY n 
1 1132 LEU n 
1 1133 LEU n 
1 1134 PHE n 
1 1135 MET n 
1 1136 HIS n 
1 1137 PHE n 
1 1138 SER n 
1 1139 TYR n 
1 1140 LYS n 
1 1141 PRO n 
1 1142 ILE n 
1 1143 SER n 
1 1144 PHE n 
1 1145 LYS n 
1 1146 THR n 
1 1147 VAL n 
1 1148 LEU n 
1 1149 VAL n 
1 1150 SER n 
1 1151 PRO n 
1 1152 GLY n 
1 1153 LEU n 
1 1154 CYS n 
1 1155 ILE n 
1 1156 SER n 
1 1157 GLY n 
1 1158 ASP n 
1 1159 VAL n 
1 1160 GLY n 
1 1161 ILE n 
1 1162 ALA n 
1 1163 PRO n 
1 1164 LYS n 
1 1165 GLN n 
1 1166 GLY n 
1 1167 TYR n 
1 1168 PHE n 
1 1169 ILE n 
1 1170 LYS n 
1 1171 HIS n 
1 1172 ASN n 
1 1173 ASP n 
1 1174 HIS n 
1 1175 TRP n 
1 1176 MET n 
1 1177 PHE n 
1 1178 THR n 
1 1179 GLY n 
1 1180 SER n 
1 1181 SER n 
1 1182 TYR n 
1 1183 TYR n 
1 1184 TYR n 
1 1185 PRO n 
1 1186 GLU n 
1 1187 PRO n 
1 1188 ILE n 
1 1189 SER n 
1 1190 ASP n 
1 1191 LYS n 
1 1192 ASN n 
1 1193 VAL n 
1 1194 VAL n 
1 1195 PHE n 
1 1196 MET n 
1 1197 ASN n 
1 1198 THR n 
1 1199 CYS n 
1 1200 SER n 
1 1201 VAL n 
1 1202 ASN n 
1 1203 PHE n 
1 1204 THR n 
1 1205 LYS n 
1 1206 ALA n 
1 1207 PRO n 
1 1208 LEU n 
1 1209 VAL n 
1 1210 TYR n 
1 1211 LEU n 
1 1212 ASN n 
1 1213 HIS n 
1 1214 SER n 
1 1215 VAL n 
1 1216 PRO n 
1 1217 LYS n 
1 1218 LEU n 
1 1219 SER n 
1 1220 ASP n 
1 1221 PHE n 
1 1222 GLU n 
1 1223 SER n 
1 1224 GLU n 
1 1225 LEU n 
1 1226 SER n 
1 1227 HIS n 
1 1228 TRP n 
1 1229 PHE n 
1 1230 LYS n 
1 1231 ASN n 
1 1232 GLN n 
1 1233 THR n 
1 1234 SER n 
1 1235 ILE n 
1 1236 ALA n 
1 1237 PRO n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 THR n 
1 1241 LEU n 
1 1242 ASN n 
1 1243 LEU n 
1 1244 HIS n 
1 1245 THR n 
1 1246 ILE n 
1 1247 ASN n 
1 1248 ALA n 
1 1249 THR n 
1 1250 PHE n 
1 1251 LEU n 
1 1252 ASP n 
1 1253 LEU n 
1 1254 TYR n 
1 1255 TYR n 
1 1256 GLU n 
1 1257 MET n 
1 1258 ASN n 
1 1259 LEU n 
1 1260 ILE n 
1 1261 GLN n 
1 1262 GLU n 
1 1263 SER n 
1 1264 ILE n 
1 1265 LYS n 
1 1266 SER n 
1 1267 LEU n 
1 1268 ASN n 
1 1269 ASN n 
1 1270 SER n 
1 1271 TYR n 
1 1272 ILE n 
1 1273 ASN n 
1 1274 LEU n 
1 1275 LYS n 
1 1276 ASP n 
1 1277 ILE n 
1 1278 GLY n 
1 1279 THR n 
1 1280 TYR n 
1 1281 GLU n 
1 1282 MET n 
1 1283 TYR n 
1 1284 VAL n 
1 1285 LYS n 
1 1286 SER n 
1 1287 GLY n 
1 1288 GLY n 
1 1289 TYR n 
1 1290 ILE n 
1 1291 PRO n 
1 1292 GLU n 
1 1293 ALA n 
1 1294 PRO n 
1 1295 ARG n 
1 1296 ASP n 
1 1297 GLY n 
1 1298 GLN n 
1 1299 ALA n 
1 1300 TYR n 
1 1301 VAL n 
1 1302 ARG n 
1 1303 LYS n 
1 1304 ASP n 
1 1305 GLY n 
1 1306 GLU n 
1 1307 TRP n 
1 1308 VAL n 
1 1309 LEU n 
1 1310 LEU n 
1 1311 SER n 
1 1312 THR n 
1 1313 PHE n 
1 1314 LEU n 
1 1315 ASN n 
1 1316 SER n 
1 1317 GLY n 
1 1318 ARG n 
1 1319 ALA n 
1 1320 HIS n 
1 1321 HIS n 
1 1322 HIS n 
1 1323 HIS n 
1 1324 HIS n 
1 1325 HIS n 
1 1326 GLY n 
1 1327 ALA n 
1 1328 GLY n 
1 1329 GLY n 
1 1330 LEU n 
1 1331 ASN n 
1 1332 ASP n 
1 1333 ILE n 
1 1334 PHE n 
1 1335 GLU n 
1 1336 ALA n 
1 1337 GLN n 
1 1338 LYS n 
1 1339 ILE n 
1 1340 GLU n 
1 1341 TRP n 
1 1342 HIS n 
1 1343 GLU n 
1 1344 ASP n 
1 1345 THR n 
1 1346 ALA n 
1 1347 ALA n 
1 1348 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1348 
_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 
4 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 DGlcpNAcb1-4DGlcpNAcb1-                                                                                     
'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                                       WURCS PDB2Glycan 
1.1.0 
3 2 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}'                                                          LINUCS PDB-CARE   
?     
4 3 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-'                                                      
'Glycam Condensed Sequence' GMML       1.0   
5 3 '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 
6 3 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}' LINUCS PDB-CARE   
?     
7 4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-                                                                            
'Glycam Condensed Sequence' GMML       1.0   
8 4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1'                                WURCS PDB2Glycan 
1.1.0 
9 4 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}'                                       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 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
3 3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
4 3 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
5 3 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
6 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
7 4 3 BMA C1 O1 2 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   GLY 18   31   31  GLY GLY A . n 
A 1 19   GLY 19   32   32  GLY GLY A . n 
A 1 20   GLY 20   33   33  GLY GLY A . n 
A 1 21   GLY 21   34   34  GLY GLY 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  PRO 737  750  ?   ?   ?   A . n 
A 1 738  SER 738  751  ?   ?   ?   A . n 
A 1 739  SER 739  752  ?   ?   ?   A . n 
A 1 740  SER 740  753  ?   ?   ?   A . n 
A 1 741  SER 741  754  ?   ?   ?   A . n 
A 1 742  SER 742  755  ?   ?   ?   A . n 
A 1 743  ARG 743  756  ?   ?   ?   A . n 
A 1 744  ARG 744  757  ?   ?   ?   A . n 
A 1 745  LYS 745  758  ?   ?   ?   A . n 
A 1 746  ARG 746  759  ?   ?   ?   A . n 
A 1 747  ARG 747  760  ?   ?   ?   A . n 
A 1 748  SER 748  761  ?   ?   ?   A . n 
A 1 749  ILE 749  762  ?   ?   ?   A . n 
A 1 750  SER 750  763  ?   ?   ?   A . n 
A 1 751  ALA 751  764  ?   ?   ?   A . n 
A 1 752  SER 752  765  ?   ?   ?   A . n 
A 1 753  TYR 753  766  ?   ?   ?   A . n 
A 1 754  ARG 754  767  ?   ?   ?   A . n 
A 1 755  PHE 755  768  ?   ?   ?   A . n 
A 1 756  VAL 756  769  ?   ?   ?   A . n 
A 1 757  THR 757  770  ?   ?   ?   A . n 
A 1 758  PHE 758  771  ?   ?   ?   A . n 
A 1 759  GLU 759  772  ?   ?   ?   A . n 
A 1 760  PRO 760  773  ?   ?   ?   A . n 
A 1 761  PHE 761  774  ?   ?   ?   A . n 
A 1 762  ASN 762  775  ?   ?   ?   A . n 
A 1 763  VAL 763  776  ?   ?   ?   A . n 
A 1 764  SER 764  777  ?   ?   ?   A . n 
A 1 765  PHE 765  778  ?   ?   ?   A . n 
A 1 766  VAL 766  779  ?   ?   ?   A . n 
A 1 767  ASN 767  780  ?   ?   ?   A . n 
A 1 768  ASP 768  781  ?   ?   ?   A . n 
A 1 769  SER 769  782  ?   ?   ?   A . n 
A 1 770  ILE 770  783  ?   ?   ?   A . n 
A 1 771  GLU 771  784  ?   ?   ?   A . n 
A 1 772  SER 772  785  ?   ?   ?   A . n 
A 1 773  VAL 773  786  ?   ?   ?   A . n 
A 1 774  GLY 774  787  ?   ?   ?   A . n 
A 1 775  GLY 775  788  ?   ?   ?   A . n 
A 1 776  LEU 776  789  ?   ?   ?   A . n 
A 1 777  TYR 777  790  ?   ?   ?   A . n 
A 1 778  GLU 778  791  ?   ?   ?   A . n 
A 1 779  ILE 779  792  ?   ?   ?   A . n 
A 1 780  LYS 780  793  ?   ?   ?   A . n 
A 1 781  ILE 781  794  ?   ?   ?   A . n 
A 1 782  PRO 782  795  ?   ?   ?   A . n 
A 1 783  THR 783  796  ?   ?   ?   A . n 
A 1 784  ASN 784  797  ?   ?   ?   A . n 
A 1 785  PHE 785  798  ?   ?   ?   A . n 
A 1 786  THR 786  799  ?   ?   ?   A . n 
A 1 787  ILE 787  800  ?   ?   ?   A . n 
A 1 788  VAL 788  801  ?   ?   ?   A . n 
A 1 789  GLY 789  802  ?   ?   ?   A . n 
A 1 790  GLN 790  803  ?   ?   ?   A . n 
A 1 791  GLU 791  804  ?   ?   ?   A . n 
A 1 792  GLU 792  805  ?   ?   ?   A . n 
A 1 793  PHE 793  806  ?   ?   ?   A . n 
A 1 794  ILE 794  807  ?   ?   ?   A . n 
A 1 795  GLN 795  808  ?   ?   ?   A . n 
A 1 796  THR 796  809  ?   ?   ?   A . n 
A 1 797  ASN 797  810  ?   ?   ?   A . n 
A 1 798  SER 798  811  ?   ?   ?   A . n 
A 1 799  PRO 799  812  ?   ?   ?   A . n 
A 1 800  LYS 800  813  ?   ?   ?   A . n 
A 1 801  VAL 801  814  ?   ?   ?   A . n 
A 1 802  THR 802  815  ?   ?   ?   A . n 
A 1 803  ILE 803  816  ?   ?   ?   A . n 
A 1 804  ASP 804  817  ?   ?   ?   A . n 
A 1 805  CYS 805  818  ?   ?   ?   A . n 
A 1 806  SER 806  819  ?   ?   ?   A . n 
A 1 807  LEU 807  820  ?   ?   ?   A . n 
A 1 808  PHE 808  821  ?   ?   ?   A . n 
A 1 809  VAL 809  822  ?   ?   ?   A . n 
A 1 810  CYS 810  823  ?   ?   ?   A . n 
A 1 811  SER 811  824  ?   ?   ?   A . n 
A 1 812  ASN 812  825  ?   ?   ?   A . n 
A 1 813  TYR 813  826  ?   ?   ?   A . n 
A 1 814  ALA 814  827  ?   ?   ?   A . n 
A 1 815  ALA 815  828  ?   ?   ?   A . n 
A 1 816  CYS 816  829  ?   ?   ?   A . n 
A 1 817  HIS 817  830  ?   ?   ?   A . n 
A 1 818  ASP 818  831  ?   ?   ?   A . n 
A 1 819  LEU 819  832  ?   ?   ?   A . n 
A 1 820  LEU 820  833  ?   ?   ?   A . n 
A 1 821  SER 821  834  ?   ?   ?   A . n 
A 1 822  GLU 822  835  ?   ?   ?   A . n 
A 1 823  TYR 823  836  ?   ?   ?   A . n 
A 1 824  GLY 824  837  ?   ?   ?   A . n 
A 1 825  THR 825  838  ?   ?   ?   A . n 
A 1 826  PHE 826  839  ?   ?   ?   A . n 
A 1 827  CYS 827  840  ?   ?   ?   A . n 
A 1 828  ASP 828  841  ?   ?   ?   A . n 
A 1 829  ASN 829  842  ?   ?   ?   A . n 
A 1 830  ILE 830  843  ?   ?   ?   A . n 
A 1 831  ASN 831  844  ?   ?   ?   A . n 
A 1 832  SER 832  845  ?   ?   ?   A . n 
A 1 833  ILE 833  846  ?   ?   ?   A . n 
A 1 834  LEU 834  847  ?   ?   ?   A . n 
A 1 835  ASP 835  848  ?   ?   ?   A . n 
A 1 836  GLU 836  849  ?   ?   ?   A . n 
A 1 837  VAL 837  850  ?   ?   ?   A . n 
A 1 838  ASN 838  851  ?   ?   ?   A . n 
A 1 839  GLY 839  852  ?   ?   ?   A . n 
A 1 840  LEU 840  853  ?   ?   ?   A . n 
A 1 841  LEU 841  854  ?   ?   ?   A . n 
A 1 842  ASP 842  855  ?   ?   ?   A . n 
A 1 843  THR 843  856  ?   ?   ?   A . n 
A 1 844  THR 844  857  ?   ?   ?   A . n 
A 1 845  GLN 845  858  ?   ?   ?   A . n 
A 1 846  LEU 846  859  ?   ?   ?   A . n 
A 1 847  HIS 847  860  ?   ?   ?   A . n 
A 1 848  VAL 848  861  ?   ?   ?   A . n 
A 1 849  ALA 849  862  ?   ?   ?   A . n 
A 1 850  ASP 850  863  ?   ?   ?   A . n 
A 1 851  THR 851  864  ?   ?   ?   A . n 
A 1 852  LEU 852  865  ?   ?   ?   A . n 
A 1 853  MET 853  866  ?   ?   ?   A . n 
A 1 854  GLN 854  867  ?   ?   ?   A . n 
A 1 855  GLY 855  868  ?   ?   ?   A . n 
A 1 856  VAL 856  869  ?   ?   ?   A . n 
A 1 857  THR 857  870  ?   ?   ?   A . n 
A 1 858  LEU 858  871  ?   ?   ?   A . n 
A 1 859  SER 859  872  ?   ?   ?   A . n 
A 1 860  SER 860  873  ?   ?   ?   A . n 
A 1 861  ASN 861  874  ?   ?   ?   A . n 
A 1 862  LEU 862  875  ?   ?   ?   A . n 
A 1 863  ASN 863  876  ?   ?   ?   A . n 
A 1 864  THR 864  877  ?   ?   ?   A . n 
A 1 865  ASN 865  878  ?   ?   ?   A . n 
A 1 866  LEU 866  879  ?   ?   ?   A . n 
A 1 867  HIS 867  880  ?   ?   ?   A . n 
A 1 868  PHE 868  881  ?   ?   ?   A . n 
A 1 869  ASP 869  882  ?   ?   ?   A . n 
A 1 870  VAL 870  883  ?   ?   ?   A . n 
A 1 871  ASP 871  884  ?   ?   ?   A . n 
A 1 872  ASN 872  885  ?   ?   ?   A . n 
A 1 873  ILE 873  886  ?   ?   ?   A . n 
A 1 874  ASN 874  887  ?   ?   ?   A . n 
A 1 875  PHE 875  888  ?   ?   ?   A . n 
A 1 876  LYS 876  889  ?   ?   ?   A . n 
A 1 877  SER 877  890  ?   ?   ?   A . n 
A 1 878  LEU 878  891  ?   ?   ?   A . n 
A 1 879  VAL 879  892  ?   ?   ?   A . n 
A 1 880  GLY 880  893  ?   ?   ?   A . n 
A 1 881  CYS 881  894  ?   ?   ?   A . n 
A 1 882  LEU 882  895  ?   ?   ?   A . n 
A 1 883  GLY 883  896  ?   ?   ?   A . n 
A 1 884  PRO 884  897  ?   ?   ?   A . n 
A 1 885  HIS 885  898  ?   ?   ?   A . n 
A 1 886  CYS 886  899  ?   ?   ?   A . n 
A 1 887  GLY 887  900  ?   ?   ?   A . n 
A 1 888  SER 888  901  ?   ?   ?   A . n 
A 1 889  SER 889  902  ?   ?   ?   A . n 
A 1 890  SER 890  903  ?   ?   ?   A . n 
A 1 891  ARG 891  904  ?   ?   ?   A . n 
A 1 892  SER 892  905  ?   ?   ?   A . n 
A 1 893  PHE 893  906  ?   ?   ?   A . n 
A 1 894  PHE 894  907  ?   ?   ?   A . n 
A 1 895  GLU 895  908  ?   ?   ?   A . n 
A 1 896  ASP 896  909  ?   ?   ?   A . n 
A 1 897  LEU 897  910  ?   ?   ?   A . n 
A 1 898  LEU 898  911  ?   ?   ?   A . n 
A 1 899  PHE 899  912  ?   ?   ?   A . n 
A 1 900  ASP 900  913  ?   ?   ?   A . n 
A 1 901  LYS 901  914  ?   ?   ?   A . n 
A 1 902  VAL 902  915  ?   ?   ?   A . n 
A 1 903  LYS 903  916  ?   ?   ?   A . n 
A 1 904  LEU 904  917  ?   ?   ?   A . n 
A 1 905  SER 905  918  ?   ?   ?   A . n 
A 1 906  ASP 906  919  ?   ?   ?   A . n 
A 1 907  VAL 907  920  ?   ?   ?   A . n 
A 1 908  GLY 908  921  ?   ?   ?   A . n 
A 1 909  PHE 909  922  ?   ?   ?   A . n 
A 1 910  VAL 910  923  ?   ?   ?   A . n 
A 1 911  GLU 911  924  ?   ?   ?   A . n 
A 1 912  ALA 912  925  ?   ?   ?   A . n 
A 1 913  TYR 913  926  ?   ?   ?   A . n 
A 1 914  ASN 914  927  ?   ?   ?   A . n 
A 1 915  ASN 915  928  ?   ?   ?   A . n 
A 1 916  CYS 916  929  ?   ?   ?   A . n 
A 1 917  THR 917  930  ?   ?   ?   A . n 
A 1 918  GLY 918  931  ?   ?   ?   A . n 
A 1 919  GLY 919  932  ?   ?   ?   A . n 
A 1 920  SER 920  933  ?   ?   ?   A . n 
A 1 921  GLU 921  934  ?   ?   ?   A . n 
A 1 922  ILE 922  935  ?   ?   ?   A . n 
A 1 923  ARG 923  936  ?   ?   ?   A . n 
A 1 924  ASP 924  937  ?   ?   ?   A . n 
A 1 925  LEU 925  938  ?   ?   ?   A . n 
A 1 926  LEU 926  939  ?   ?   ?   A . n 
A 1 927  CYS 927  940  ?   ?   ?   A . n 
A 1 928  VAL 928  941  ?   ?   ?   A . n 
A 1 929  GLN 929  942  ?   ?   ?   A . n 
A 1 930  SER 930  943  ?   ?   ?   A . n 
A 1 931  PHE 931  944  ?   ?   ?   A . n 
A 1 932  ASN 932  945  ?   ?   ?   A . n 
A 1 933  GLY 933  946  ?   ?   ?   A . n 
A 1 934  ILE 934  947  ?   ?   ?   A . n 
A 1 935  LYS 935  948  ?   ?   ?   A . n 
A 1 936  VAL 936  949  ?   ?   ?   A . n 
A 1 937  LEU 937  950  ?   ?   ?   A . n 
A 1 938  PRO 938  951  ?   ?   ?   A . n 
A 1 939  PRO 939  952  ?   ?   ?   A . n 
A 1 940  ILE 940  953  ?   ?   ?   A . n 
A 1 941  LEU 941  954  ?   ?   ?   A . n 
A 1 942  SER 942  955  ?   ?   ?   A . n 
A 1 943  GLU 943  956  ?   ?   ?   A . n 
A 1 944  SER 944  957  ?   ?   ?   A . n 
A 1 945  GLN 945  958  ?   ?   ?   A . n 
A 1 946  ILE 946  959  ?   ?   ?   A . n 
A 1 947  SER 947  960  ?   ?   ?   A . n 
A 1 948  GLY 948  961  ?   ?   ?   A . n 
A 1 949  TYR 949  962  ?   ?   ?   A . n 
A 1 950  THR 950  963  ?   ?   ?   A . n 
A 1 951  THR 951  964  ?   ?   ?   A . n 
A 1 952  ALA 952  965  ?   ?   ?   A . n 
A 1 953  ALA 953  966  ?   ?   ?   A . n 
A 1 954  THR 954  967  ?   ?   ?   A . n 
A 1 955  VAL 955  968  ?   ?   ?   A . n 
A 1 956  ALA 956  969  ?   ?   ?   A . n 
A 1 957  ALA 957  970  ?   ?   ?   A . n 
A 1 958  MET 958  971  ?   ?   ?   A . n 
A 1 959  PHE 959  972  ?   ?   ?   A . n 
A 1 960  PRO 960  973  ?   ?   ?   A . n 
A 1 961  PRO 961  974  ?   ?   ?   A . n 
A 1 962  TRP 962  975  ?   ?   ?   A . n 
A 1 963  SER 963  976  ?   ?   ?   A . n 
A 1 964  ALA 964  977  ?   ?   ?   A . n 
A 1 965  ALA 965  978  ?   ?   ?   A . n 
A 1 966  ALA 966  979  ?   ?   ?   A . n 
A 1 967  GLY 967  980  ?   ?   ?   A . n 
A 1 968  ILE 968  981  ?   ?   ?   A . n 
A 1 969  PRO 969  982  ?   ?   ?   A . n 
A 1 970  PHE 970  983  ?   ?   ?   A . n 
A 1 971  SER 971  984  ?   ?   ?   A . n 
A 1 972  LEU 972  985  ?   ?   ?   A . n 
A 1 973  ASN 973  986  ?   ?   ?   A . n 
A 1 974  VAL 974  987  ?   ?   ?   A . n 
A 1 975  GLN 975  988  ?   ?   ?   A . n 
A 1 976  TYR 976  989  ?   ?   ?   A . n 
A 1 977  ARG 977  990  ?   ?   ?   A . n 
A 1 978  ILE 978  991  ?   ?   ?   A . n 
A 1 979  ASN 979  992  ?   ?   ?   A . n 
A 1 980  GLY 980  993  ?   ?   ?   A . n 
A 1 981  LEU 981  994  ?   ?   ?   A . n 
A 1 982  GLY 982  995  ?   ?   ?   A . n 
A 1 983  VAL 983  996  ?   ?   ?   A . n 
A 1 984  THR 984  997  ?   ?   ?   A . n 
A 1 985  MET 985  998  ?   ?   ?   A . n 
A 1 986  ASP 986  999  ?   ?   ?   A . n 
A 1 987  VAL 987  1000 ?   ?   ?   A . n 
A 1 988  LEU 988  1001 ?   ?   ?   A . n 
A 1 989  ASN 989  1002 ?   ?   ?   A . n 
A 1 990  LYS 990  1003 ?   ?   ?   A . n 
A 1 991  ASN 991  1004 ?   ?   ?   A . n 
A 1 992  GLN 992  1005 ?   ?   ?   A . n 
A 1 993  LYS 993  1006 ?   ?   ?   A . n 
A 1 994  LEU 994  1007 ?   ?   ?   A . n 
A 1 995  ILE 995  1008 ?   ?   ?   A . n 
A 1 996  ALA 996  1009 ?   ?   ?   A . n 
A 1 997  THR 997  1010 ?   ?   ?   A . n 
A 1 998  ALA 998  1011 ?   ?   ?   A . n 
A 1 999  PHE 999  1012 ?   ?   ?   A . n 
A 1 1000 ASN 1000 1013 ?   ?   ?   A . n 
A 1 1001 ASN 1001 1014 ?   ?   ?   A . n 
A 1 1002 ALA 1002 1015 ?   ?   ?   A . n 
A 1 1003 LEU 1003 1016 ?   ?   ?   A . n 
A 1 1004 LEU 1004 1017 ?   ?   ?   A . n 
A 1 1005 SER 1005 1018 ?   ?   ?   A . n 
A 1 1006 ILE 1006 1019 ?   ?   ?   A . n 
A 1 1007 GLN 1007 1020 ?   ?   ?   A . n 
A 1 1008 ASN 1008 1021 ?   ?   ?   A . n 
A 1 1009 GLY 1009 1022 ?   ?   ?   A . n 
A 1 1010 PHE 1010 1023 ?   ?   ?   A . n 
A 1 1011 SER 1011 1024 ?   ?   ?   A . n 
A 1 1012 ALA 1012 1025 ?   ?   ?   A . n 
A 1 1013 PRO 1013 1026 ?   ?   ?   A . n 
A 1 1014 ASN 1014 1027 ?   ?   ?   A . n 
A 1 1015 SER 1015 1028 ?   ?   ?   A . n 
A 1 1016 ALA 1016 1029 ?   ?   ?   A . n 
A 1 1017 LEU 1017 1030 ?   ?   ?   A . n 
A 1 1018 ALA 1018 1031 ?   ?   ?   A . n 
A 1 1019 LYS 1019 1032 ?   ?   ?   A . n 
A 1 1020 ILE 1020 1033 ?   ?   ?   A . n 
A 1 1021 GLN 1021 1034 ?   ?   ?   A . n 
A 1 1022 SER 1022 1035 ?   ?   ?   A . n 
A 1 1023 VAL 1023 1036 ?   ?   ?   A . n 
A 1 1024 VAL 1024 1037 ?   ?   ?   A . n 
A 1 1025 ASN 1025 1038 ?   ?   ?   A . n 
A 1 1026 SER 1026 1039 ?   ?   ?   A . n 
A 1 1027 ASN 1027 1040 ?   ?   ?   A . n 
A 1 1028 ALA 1028 1041 ?   ?   ?   A . n 
A 1 1029 GLN 1029 1042 ?   ?   ?   A . n 
A 1 1030 ALA 1030 1043 ?   ?   ?   A . n 
A 1 1031 LEU 1031 1044 ?   ?   ?   A . n 
A 1 1032 ASN 1032 1045 ?   ?   ?   A . n 
A 1 1033 SER 1033 1046 ?   ?   ?   A . n 
A 1 1034 LEU 1034 1047 ?   ?   ?   A . n 
A 1 1035 LEU 1035 1048 ?   ?   ?   A . n 
A 1 1036 GLN 1036 1049 ?   ?   ?   A . n 
A 1 1037 GLN 1037 1050 ?   ?   ?   A . n 
A 1 1038 LEU 1038 1051 ?   ?   ?   A . n 
A 1 1039 PHE 1039 1052 ?   ?   ?   A . n 
A 1 1040 ASN 1040 1053 ?   ?   ?   A . n 
A 1 1041 LYS 1041 1054 ?   ?   ?   A . n 
A 1 1042 PHE 1042 1055 ?   ?   ?   A . n 
A 1 1043 GLY 1043 1056 ?   ?   ?   A . n 
A 1 1044 ALA 1044 1057 ?   ?   ?   A . n 
A 1 1045 ILE 1045 1058 ?   ?   ?   A . n 
A 1 1046 SER 1046 1059 ?   ?   ?   A . n 
A 1 1047 SER 1047 1060 ?   ?   ?   A . n 
A 1 1048 SER 1048 1061 ?   ?   ?   A . n 
A 1 1049 LEU 1049 1062 ?   ?   ?   A . n 
A 1 1050 GLN 1050 1063 ?   ?   ?   A . n 
A 1 1051 GLU 1051 1064 ?   ?   ?   A . n 
A 1 1052 ILE 1052 1065 ?   ?   ?   A . n 
A 1 1053 LEU 1053 1066 ?   ?   ?   A . n 
A 1 1054 SER 1054 1067 ?   ?   ?   A . n 
A 1 1055 ARG 1055 1068 ?   ?   ?   A . n 
A 1 1056 LEU 1056 1069 ?   ?   ?   A . n 
A 1 1057 ASP 1057 1070 ?   ?   ?   A . n 
A 1 1058 PRO 1058 1071 ?   ?   ?   A . n 
A 1 1059 PRO 1059 1072 ?   ?   ?   A . n 
A 1 1060 GLU 1060 1073 ?   ?   ?   A . n 
A 1 1061 ALA 1061 1074 ?   ?   ?   A . n 
A 1 1062 GLN 1062 1075 ?   ?   ?   A . n 
A 1 1063 VAL 1063 1076 ?   ?   ?   A . n 
A 1 1064 GLN 1064 1077 ?   ?   ?   A . n 
A 1 1065 ILE 1065 1078 ?   ?   ?   A . n 
A 1 1066 ASP 1066 1079 ?   ?   ?   A . n 
A 1 1067 ARG 1067 1080 ?   ?   ?   A . n 
A 1 1068 LEU 1068 1081 ?   ?   ?   A . n 
A 1 1069 ILE 1069 1082 ?   ?   ?   A . n 
A 1 1070 ASN 1070 1083 ?   ?   ?   A . n 
A 1 1071 GLY 1071 1084 ?   ?   ?   A . n 
A 1 1072 ARG 1072 1085 ?   ?   ?   A . n 
A 1 1073 LEU 1073 1086 ?   ?   ?   A . n 
A 1 1074 THR 1074 1087 ?   ?   ?   A . n 
A 1 1075 ALA 1075 1088 ?   ?   ?   A . n 
A 1 1076 LEU 1076 1089 ?   ?   ?   A . n 
A 1 1077 ASN 1077 1090 ?   ?   ?   A . n 
A 1 1078 ALA 1078 1091 ?   ?   ?   A . n 
A 1 1079 TYR 1079 1092 ?   ?   ?   A . n 
A 1 1080 VAL 1080 1093 ?   ?   ?   A . n 
A 1 1081 SER 1081 1094 ?   ?   ?   A . n 
A 1 1082 GLN 1082 1095 ?   ?   ?   A . n 
A 1 1083 GLN 1083 1096 ?   ?   ?   A . n 
A 1 1084 LEU 1084 1097 ?   ?   ?   A . n 
A 1 1085 SER 1085 1098 ?   ?   ?   A . n 
A 1 1086 ASP 1086 1099 ?   ?   ?   A . n 
A 1 1087 ILE 1087 1100 ?   ?   ?   A . n 
A 1 1088 SER 1088 1101 ?   ?   ?   A . n 
A 1 1089 LEU 1089 1102 ?   ?   ?   A . n 
A 1 1090 VAL 1090 1103 ?   ?   ?   A . n 
A 1 1091 LYS 1091 1104 ?   ?   ?   A . n 
A 1 1092 PHE 1092 1105 ?   ?   ?   A . n 
A 1 1093 GLY 1093 1106 ?   ?   ?   A . n 
A 1 1094 ALA 1094 1107 ?   ?   ?   A . n 
A 1 1095 ALA 1095 1108 ?   ?   ?   A . n 
A 1 1096 LEU 1096 1109 ?   ?   ?   A . n 
A 1 1097 ALA 1097 1110 ?   ?   ?   A . n 
A 1 1098 MET 1098 1111 ?   ?   ?   A . n 
A 1 1099 GLU 1099 1112 ?   ?   ?   A . n 
A 1 1100 LYS 1100 1113 ?   ?   ?   A . n 
A 1 1101 VAL 1101 1114 ?   ?   ?   A . n 
A 1 1102 ASN 1102 1115 ?   ?   ?   A . n 
A 1 1103 GLU 1103 1116 ?   ?   ?   A . n 
A 1 1104 CYS 1104 1117 ?   ?   ?   A . n 
A 1 1105 VAL 1105 1118 ?   ?   ?   A . n 
A 1 1106 LYS 1106 1119 ?   ?   ?   A . n 
A 1 1107 SER 1107 1120 ?   ?   ?   A . n 
A 1 1108 GLN 1108 1121 ?   ?   ?   A . n 
A 1 1109 SER 1109 1122 ?   ?   ?   A . n 
A 1 1110 PRO 1110 1123 ?   ?   ?   A . n 
A 1 1111 ARG 1111 1124 ?   ?   ?   A . n 
A 1 1112 ILE 1112 1125 ?   ?   ?   A . n 
A 1 1113 ASN 1113 1126 ?   ?   ?   A . n 
A 1 1114 PHE 1114 1127 ?   ?   ?   A . n 
A 1 1115 CYS 1115 1128 ?   ?   ?   A . n 
A 1 1116 GLY 1116 1129 ?   ?   ?   A . n 
A 1 1117 ASN 1117 1130 ?   ?   ?   A . n 
A 1 1118 GLY 1118 1131 ?   ?   ?   A . n 
A 1 1119 ASN 1119 1132 ?   ?   ?   A . n 
A 1 1120 HIS 1120 1133 ?   ?   ?   A . n 
A 1 1121 ILE 1121 1134 ?   ?   ?   A . n 
A 1 1122 LEU 1122 1135 ?   ?   ?   A . n 
A 1 1123 SER 1123 1136 ?   ?   ?   A . n 
A 1 1124 LEU 1124 1137 ?   ?   ?   A . n 
A 1 1125 VAL 1125 1138 ?   ?   ?   A . n 
A 1 1126 GLN 1126 1139 ?   ?   ?   A . n 
A 1 1127 ASN 1127 1140 ?   ?   ?   A . n 
A 1 1128 ALA 1128 1141 ?   ?   ?   A . n 
A 1 1129 PRO 1129 1142 ?   ?   ?   A . n 
A 1 1130 TYR 1130 1143 ?   ?   ?   A . n 
A 1 1131 GLY 1131 1144 ?   ?   ?   A . n 
A 1 1132 LEU 1132 1145 ?   ?   ?   A . n 
A 1 1133 LEU 1133 1146 ?   ?   ?   A . n 
A 1 1134 PHE 1134 1147 ?   ?   ?   A . n 
A 1 1135 MET 1135 1148 ?   ?   ?   A . n 
A 1 1136 HIS 1136 1149 ?   ?   ?   A . n 
A 1 1137 PHE 1137 1150 ?   ?   ?   A . n 
A 1 1138 SER 1138 1151 ?   ?   ?   A . n 
A 1 1139 TYR 1139 1152 ?   ?   ?   A . n 
A 1 1140 LYS 1140 1153 ?   ?   ?   A . n 
A 1 1141 PRO 1141 1154 ?   ?   ?   A . n 
A 1 1142 ILE 1142 1155 ?   ?   ?   A . n 
A 1 1143 SER 1143 1156 ?   ?   ?   A . n 
A 1 1144 PHE 1144 1157 ?   ?   ?   A . n 
A 1 1145 LYS 1145 1158 ?   ?   ?   A . n 
A 1 1146 THR 1146 1159 ?   ?   ?   A . n 
A 1 1147 VAL 1147 1160 ?   ?   ?   A . n 
A 1 1148 LEU 1148 1161 ?   ?   ?   A . n 
A 1 1149 VAL 1149 1162 ?   ?   ?   A . n 
A 1 1150 SER 1150 1163 ?   ?   ?   A . n 
A 1 1151 PRO 1151 1164 ?   ?   ?   A . n 
A 1 1152 GLY 1152 1165 ?   ?   ?   A . n 
A 1 1153 LEU 1153 1166 ?   ?   ?   A . n 
A 1 1154 CYS 1154 1167 ?   ?   ?   A . n 
A 1 1155 ILE 1155 1168 ?   ?   ?   A . n 
A 1 1156 SER 1156 1169 ?   ?   ?   A . n 
A 1 1157 GLY 1157 1170 ?   ?   ?   A . n 
A 1 1158 ASP 1158 1171 ?   ?   ?   A . n 
A 1 1159 VAL 1159 1172 ?   ?   ?   A . n 
A 1 1160 GLY 1160 1173 ?   ?   ?   A . n 
A 1 1161 ILE 1161 1174 ?   ?   ?   A . n 
A 1 1162 ALA 1162 1175 ?   ?   ?   A . n 
A 1 1163 PRO 1163 1176 ?   ?   ?   A . n 
A 1 1164 LYS 1164 1177 ?   ?   ?   A . n 
A 1 1165 GLN 1165 1178 ?   ?   ?   A . n 
A 1 1166 GLY 1166 1179 ?   ?   ?   A . n 
A 1 1167 TYR 1167 1180 ?   ?   ?   A . n 
A 1 1168 PHE 1168 1181 ?   ?   ?   A . n 
A 1 1169 ILE 1169 1182 ?   ?   ?   A . n 
A 1 1170 LYS 1170 1183 ?   ?   ?   A . n 
A 1 1171 HIS 1171 1184 ?   ?   ?   A . n 
A 1 1172 ASN 1172 1185 ?   ?   ?   A . n 
A 1 1173 ASP 1173 1186 ?   ?   ?   A . n 
A 1 1174 HIS 1174 1187 ?   ?   ?   A . n 
A 1 1175 TRP 1175 1188 ?   ?   ?   A . n 
A 1 1176 MET 1176 1189 ?   ?   ?   A . n 
A 1 1177 PHE 1177 1190 ?   ?   ?   A . n 
A 1 1178 THR 1178 1191 ?   ?   ?   A . n 
A 1 1179 GLY 1179 1192 ?   ?   ?   A . n 
A 1 1180 SER 1180 1193 ?   ?   ?   A . n 
A 1 1181 SER 1181 1194 ?   ?   ?   A . n 
A 1 1182 TYR 1182 1195 ?   ?   ?   A . n 
A 1 1183 TYR 1183 1196 ?   ?   ?   A . n 
A 1 1184 TYR 1184 1197 ?   ?   ?   A . n 
A 1 1185 PRO 1185 1198 ?   ?   ?   A . n 
A 1 1186 GLU 1186 1199 ?   ?   ?   A . n 
A 1 1187 PRO 1187 1200 ?   ?   ?   A . n 
A 1 1188 ILE 1188 1201 ?   ?   ?   A . n 
A 1 1189 SER 1189 1202 ?   ?   ?   A . n 
A 1 1190 ASP 1190 1203 ?   ?   ?   A . n 
A 1 1191 LYS 1191 1204 ?   ?   ?   A . n 
A 1 1192 ASN 1192 1205 ?   ?   ?   A . n 
A 1 1193 VAL 1193 1206 ?   ?   ?   A . n 
A 1 1194 VAL 1194 1207 ?   ?   ?   A . n 
A 1 1195 PHE 1195 1208 ?   ?   ?   A . n 
A 1 1196 MET 1196 1209 ?   ?   ?   A . n 
A 1 1197 ASN 1197 1210 ?   ?   ?   A . n 
A 1 1198 THR 1198 1211 ?   ?   ?   A . n 
A 1 1199 CYS 1199 1212 ?   ?   ?   A . n 
A 1 1200 SER 1200 1213 ?   ?   ?   A . n 
A 1 1201 VAL 1201 1214 ?   ?   ?   A . n 
A 1 1202 ASN 1202 1215 ?   ?   ?   A . n 
A 1 1203 PHE 1203 1216 ?   ?   ?   A . n 
A 1 1204 THR 1204 1217 ?   ?   ?   A . n 
A 1 1205 LYS 1205 1218 ?   ?   ?   A . n 
A 1 1206 ALA 1206 1219 ?   ?   ?   A . n 
A 1 1207 PRO 1207 1220 ?   ?   ?   A . n 
A 1 1208 LEU 1208 1221 ?   ?   ?   A . n 
A 1 1209 VAL 1209 1222 ?   ?   ?   A . n 
A 1 1210 TYR 1210 1223 ?   ?   ?   A . n 
A 1 1211 LEU 1211 1224 ?   ?   ?   A . n 
A 1 1212 ASN 1212 1225 ?   ?   ?   A . n 
A 1 1213 HIS 1213 1226 ?   ?   ?   A . n 
A 1 1214 SER 1214 1227 ?   ?   ?   A . n 
A 1 1215 VAL 1215 1228 ?   ?   ?   A . n 
A 1 1216 PRO 1216 1229 ?   ?   ?   A . n 
A 1 1217 LYS 1217 1230 ?   ?   ?   A . n 
A 1 1218 LEU 1218 1231 ?   ?   ?   A . n 
A 1 1219 SER 1219 1232 ?   ?   ?   A . n 
A 1 1220 ASP 1220 1233 ?   ?   ?   A . n 
A 1 1221 PHE 1221 1234 ?   ?   ?   A . n 
A 1 1222 GLU 1222 1235 ?   ?   ?   A . n 
A 1 1223 SER 1223 1236 ?   ?   ?   A . n 
A 1 1224 GLU 1224 1237 ?   ?   ?   A . n 
A 1 1225 LEU 1225 1238 ?   ?   ?   A . n 
A 1 1226 SER 1226 1239 ?   ?   ?   A . n 
A 1 1227 HIS 1227 1240 ?   ?   ?   A . n 
A 1 1228 TRP 1228 1241 ?   ?   ?   A . n 
A 1 1229 PHE 1229 1242 ?   ?   ?   A . n 
A 1 1230 LYS 1230 1243 ?   ?   ?   A . n 
A 1 1231 ASN 1231 1244 ?   ?   ?   A . n 
A 1 1232 GLN 1232 1245 ?   ?   ?   A . n 
A 1 1233 THR 1233 1246 ?   ?   ?   A . n 
A 1 1234 SER 1234 1247 ?   ?   ?   A . n 
A 1 1235 ILE 1235 1248 ?   ?   ?   A . n 
A 1 1236 ALA 1236 1249 ?   ?   ?   A . n 
A 1 1237 PRO 1237 1250 ?   ?   ?   A . n 
A 1 1238 ASN 1238 1251 ?   ?   ?   A . n 
A 1 1239 LEU 1239 1252 ?   ?   ?   A . n 
A 1 1240 THR 1240 1253 ?   ?   ?   A . n 
A 1 1241 LEU 1241 1254 ?   ?   ?   A . n 
A 1 1242 ASN 1242 1255 ?   ?   ?   A . n 
A 1 1243 LEU 1243 1256 ?   ?   ?   A . n 
A 1 1244 HIS 1244 1257 ?   ?   ?   A . n 
A 1 1245 THR 1245 1258 ?   ?   ?   A . n 
A 1 1246 ILE 1246 1259 ?   ?   ?   A . n 
A 1 1247 ASN 1247 1260 ?   ?   ?   A . n 
A 1 1248 ALA 1248 1261 ?   ?   ?   A . n 
A 1 1249 THR 1249 1262 ?   ?   ?   A . n 
A 1 1250 PHE 1250 1263 ?   ?   ?   A . n 
A 1 1251 LEU 1251 1264 ?   ?   ?   A . n 
A 1 1252 ASP 1252 1265 ?   ?   ?   A . n 
A 1 1253 LEU 1253 1266 ?   ?   ?   A . n 
A 1 1254 TYR 1254 1267 ?   ?   ?   A . n 
A 1 1255 TYR 1255 1268 ?   ?   ?   A . n 
A 1 1256 GLU 1256 1269 ?   ?   ?   A . n 
A 1 1257 MET 1257 1270 ?   ?   ?   A . n 
A 1 1258 ASN 1258 1271 ?   ?   ?   A . n 
A 1 1259 LEU 1259 1272 ?   ?   ?   A . n 
A 1 1260 ILE 1260 1273 ?   ?   ?   A . n 
A 1 1261 GLN 1261 1274 ?   ?   ?   A . n 
A 1 1262 GLU 1262 1275 ?   ?   ?   A . n 
A 1 1263 SER 1263 1276 ?   ?   ?   A . n 
A 1 1264 ILE 1264 1277 ?   ?   ?   A . n 
A 1 1265 LYS 1265 1278 ?   ?   ?   A . n 
A 1 1266 SER 1266 1279 ?   ?   ?   A . n 
A 1 1267 LEU 1267 1280 ?   ?   ?   A . n 
A 1 1268 ASN 1268 1281 ?   ?   ?   A . n 
A 1 1269 ASN 1269 1282 ?   ?   ?   A . n 
A 1 1270 SER 1270 1283 ?   ?   ?   A . n 
A 1 1271 TYR 1271 1284 ?   ?   ?   A . n 
A 1 1272 ILE 1272 1285 ?   ?   ?   A . n 
A 1 1273 ASN 1273 1286 ?   ?   ?   A . n 
A 1 1274 LEU 1274 1287 ?   ?   ?   A . n 
A 1 1275 LYS 1275 1288 ?   ?   ?   A . n 
A 1 1276 ASP 1276 1289 ?   ?   ?   A . n 
A 1 1277 ILE 1277 1290 ?   ?   ?   A . n 
A 1 1278 GLY 1278 1291 ?   ?   ?   A . n 
A 1 1279 THR 1279 1292 ?   ?   ?   A . n 
A 1 1280 TYR 1280 1293 ?   ?   ?   A . n 
A 1 1281 GLU 1281 1294 ?   ?   ?   A . n 
A 1 1282 MET 1282 1295 ?   ?   ?   A . n 
A 1 1283 TYR 1283 1296 ?   ?   ?   A . n 
A 1 1284 VAL 1284 1297 ?   ?   ?   A . n 
A 1 1285 LYS 1285 1298 ?   ?   ?   A . n 
A 1 1286 SER 1286 1299 ?   ?   ?   A . n 
A 1 1287 GLY 1287 1300 ?   ?   ?   A . n 
A 1 1288 GLY 1288 1301 ?   ?   ?   A . n 
A 1 1289 TYR 1289 1302 ?   ?   ?   A . n 
A 1 1290 ILE 1290 1303 ?   ?   ?   A . n 
A 1 1291 PRO 1291 1304 ?   ?   ?   A . n 
A 1 1292 GLU 1292 1305 ?   ?   ?   A . n 
A 1 1293 ALA 1293 1306 ?   ?   ?   A . n 
A 1 1294 PRO 1294 1307 ?   ?   ?   A . n 
A 1 1295 ARG 1295 1308 ?   ?   ?   A . n 
A 1 1296 ASP 1296 1309 ?   ?   ?   A . n 
A 1 1297 GLY 1297 1310 ?   ?   ?   A . n 
A 1 1298 GLN 1298 1311 ?   ?   ?   A . n 
A 1 1299 ALA 1299 1312 ?   ?   ?   A . n 
A 1 1300 TYR 1300 1313 ?   ?   ?   A . n 
A 1 1301 VAL 1301 1314 ?   ?   ?   A . n 
A 1 1302 ARG 1302 1315 ?   ?   ?   A . n 
A 1 1303 LYS 1303 1316 ?   ?   ?   A . n 
A 1 1304 ASP 1304 1317 ?   ?   ?   A . n 
A 1 1305 GLY 1305 1318 ?   ?   ?   A . n 
A 1 1306 GLU 1306 1319 ?   ?   ?   A . n 
A 1 1307 TRP 1307 1320 ?   ?   ?   A . n 
A 1 1308 VAL 1308 1321 ?   ?   ?   A . n 
A 1 1309 LEU 1309 1322 ?   ?   ?   A . n 
A 1 1310 LEU 1310 1323 ?   ?   ?   A . n 
A 1 1311 SER 1311 1324 ?   ?   ?   A . n 
A 1 1312 THR 1312 1325 ?   ?   ?   A . n 
A 1 1313 PHE 1313 1326 ?   ?   ?   A . n 
A 1 1314 LEU 1314 1327 ?   ?   ?   A . n 
A 1 1315 ASN 1315 1328 ?   ?   ?   A . n 
A 1 1316 SER 1316 1329 ?   ?   ?   A . n 
A 1 1317 GLY 1317 1330 ?   ?   ?   A . n 
A 1 1318 ARG 1318 1331 ?   ?   ?   A . n 
A 1 1319 ALA 1319 1332 ?   ?   ?   A . n 
A 1 1320 HIS 1320 1333 ?   ?   ?   A . n 
A 1 1321 HIS 1321 1334 ?   ?   ?   A . n 
A 1 1322 HIS 1322 1335 ?   ?   ?   A . n 
A 1 1323 HIS 1323 1336 ?   ?   ?   A . n 
A 1 1324 HIS 1324 1337 ?   ?   ?   A . n 
A 1 1325 HIS 1325 1338 ?   ?   ?   A . n 
A 1 1326 GLY 1326 1339 ?   ?   ?   A . n 
A 1 1327 ALA 1327 1340 ?   ?   ?   A . n 
A 1 1328 GLY 1328 1341 ?   ?   ?   A . n 
A 1 1329 GLY 1329 1342 ?   ?   ?   A . n 
A 1 1330 LEU 1330 1343 ?   ?   ?   A . n 
A 1 1331 ASN 1331 1344 ?   ?   ?   A . n 
A 1 1332 ASP 1332 1345 ?   ?   ?   A . n 
A 1 1333 ILE 1333 1346 ?   ?   ?   A . n 
A 1 1334 PHE 1334 1347 ?   ?   ?   A . n 
A 1 1335 GLU 1335 1348 ?   ?   ?   A . n 
A 1 1336 ALA 1336 1349 ?   ?   ?   A . n 
A 1 1337 GLN 1337 1350 ?   ?   ?   A . n 
A 1 1338 LYS 1338 1351 ?   ?   ?   A . n 
A 1 1339 ILE 1339 1352 ?   ?   ?   A . n 
A 1 1340 GLU 1340 1353 ?   ?   ?   A . n 
A 1 1341 TRP 1341 1354 ?   ?   ?   A . n 
A 1 1342 HIS 1342 1355 ?   ?   ?   A . n 
A 1 1343 GLU 1343 1356 ?   ?   ?   A . n 
A 1 1344 ASP 1344 1357 ?   ?   ?   A . n 
A 1 1345 THR 1345 1358 ?   ?   ?   A . n 
A 1 1346 ALA 1346 1359 ?   ?   ?   A . n 
A 1 1347 ALA 1347 1360 ?   ?   ?   A . n 
A 1 1348 ALA 1348 1361 ?   ?   ?   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 1224 n 
B 2 NAG 2 B NAG 2 A NAG 1225 n 
C 2 NAG 1 C NAG 1 A NAG 1227 n 
C 2 NAG 2 C NAG 2 A NAG 1228 n 
D 3 NAG 1 D NAG 1 A NAG 1229 n 
D 3 NAG 2 D NAG 2 A NAG 1230 n 
D 3 BMA 3 D BMA 3 A BMA 1231 n 
D 3 MAN 4 D MAN 4 A MAN 1232 n 
D 3 MAN 5 D MAN 5 A MAN 1233 n 
E 4 NAG 1 E NAG 1 A NAG 1235 n 
E 4 NAG 2 E NAG 2 A NAG 1236 n 
E 4 BMA 3 E BMA 3 A BMA 1237 n 
F 2 NAG 1 F NAG 1 A NAG 1238 n 
F 2 NAG 2 F NAG 2 A NAG 1239 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 
G 5 NAG   1 1401 1234 NAG   NAG A . 
H 5 NAG   1 1402 1240 NAG   NAG A . 
I 6 A1AR1 1 1403 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                     9N15 
_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                         9N15 
_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                   9N15 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9N15 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.20 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_struct.entry_id                     9N15 
_struct.title                        
'Cryo-EM structure of HCoV-HKU1 glycoprotein D1 Domain in complex with 9OAc-GD3(mutant T31VPR34 to GGGG)' 
_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        9N15 
_struct_keywords.text            'HCoV-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 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
# 
_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
VNFTKAPLVYLNHSVPKLSDFESELSHWFKNQTSIAPNLTLNLHTINATFLDLYYEMNLIQESIKSLNNSYINLKDIGTY
EMYVK
;
_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              9N15 
_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                 1285 
_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                  1298 
_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       1298 
# 
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 9N15 GLY A 18   ? UNP Q5MQD0 THR 31   'engineered mutation' 31   1  
1 9N15 GLY A 19   ? UNP Q5MQD0 VAL 32   'engineered mutation' 32   2  
1 9N15 GLY A 20   ? UNP Q5MQD0 PRO 33   'engineered mutation' 33   3  
1 9N15 GLY A 21   ? UNP Q5MQD0 ARG 34   'engineered mutation' 34   4  
1 9N15 PRO A 1013 ? UNP Q5MQD0 THR 1026 conflict              1026 5  
1 9N15 PRO A 1058 ? UNP Q5MQD0 ALA 1071 conflict              1071 6  
1 9N15 PRO A 1059 ? UNP Q5MQD0 LEU 1072 conflict              1072 7  
1 9N15 SER A 1286 ? UNP Q5MQD0 ?   ?    'expression tag'      1299 8  
1 9N15 GLY A 1287 ? UNP Q5MQD0 ?   ?    'expression tag'      1300 9  
1 9N15 GLY A 1288 ? UNP Q5MQD0 ?   ?    'expression tag'      1301 10 
1 9N15 TYR A 1289 ? UNP Q5MQD0 ?   ?    'expression tag'      1302 11 
1 9N15 ILE A 1290 ? UNP Q5MQD0 ?   ?    'expression tag'      1303 12 
1 9N15 PRO A 1291 ? UNP Q5MQD0 ?   ?    'expression tag'      1304 13 
1 9N15 GLU A 1292 ? UNP Q5MQD0 ?   ?    'expression tag'      1305 14 
1 9N15 ALA A 1293 ? UNP Q5MQD0 ?   ?    'expression tag'      1306 15 
1 9N15 PRO A 1294 ? UNP Q5MQD0 ?   ?    'expression tag'      1307 16 
1 9N15 ARG A 1295 ? UNP Q5MQD0 ?   ?    'expression tag'      1308 17 
1 9N15 ASP A 1296 ? UNP Q5MQD0 ?   ?    'expression tag'      1309 18 
1 9N15 GLY A 1297 ? UNP Q5MQD0 ?   ?    'expression tag'      1310 19 
1 9N15 GLN A 1298 ? UNP Q5MQD0 ?   ?    'expression tag'      1311 20 
1 9N15 ALA A 1299 ? UNP Q5MQD0 ?   ?    'expression tag'      1312 21 
1 9N15 TYR A 1300 ? UNP Q5MQD0 ?   ?    'expression tag'      1313 22 
1 9N15 VAL A 1301 ? UNP Q5MQD0 ?   ?    'expression tag'      1314 23 
1 9N15 ARG A 1302 ? UNP Q5MQD0 ?   ?    'expression tag'      1315 24 
1 9N15 LYS A 1303 ? UNP Q5MQD0 ?   ?    'expression tag'      1316 25 
1 9N15 ASP A 1304 ? UNP Q5MQD0 ?   ?    'expression tag'      1317 26 
1 9N15 GLY A 1305 ? UNP Q5MQD0 ?   ?    'expression tag'      1318 27 
1 9N15 GLU A 1306 ? UNP Q5MQD0 ?   ?    'expression tag'      1319 28 
1 9N15 TRP A 1307 ? UNP Q5MQD0 ?   ?    'expression tag'      1320 29 
1 9N15 VAL A 1308 ? UNP Q5MQD0 ?   ?    'expression tag'      1321 30 
1 9N15 LEU A 1309 ? UNP Q5MQD0 ?   ?    'expression tag'      1322 31 
1 9N15 LEU A 1310 ? UNP Q5MQD0 ?   ?    'expression tag'      1323 32 
1 9N15 SER A 1311 ? UNP Q5MQD0 ?   ?    'expression tag'      1324 33 
1 9N15 THR A 1312 ? UNP Q5MQD0 ?   ?    'expression tag'      1325 34 
1 9N15 PHE A 1313 ? UNP Q5MQD0 ?   ?    'expression tag'      1326 35 
1 9N15 LEU A 1314 ? UNP Q5MQD0 ?   ?    'expression tag'      1327 36 
1 9N15 ASN A 1315 ? UNP Q5MQD0 ?   ?    'expression tag'      1328 37 
1 9N15 SER A 1316 ? UNP Q5MQD0 ?   ?    'expression tag'      1329 38 
1 9N15 GLY A 1317 ? UNP Q5MQD0 ?   ?    'expression tag'      1330 39 
1 9N15 ARG A 1318 ? UNP Q5MQD0 ?   ?    'expression tag'      1331 40 
1 9N15 ALA A 1319 ? UNP Q5MQD0 ?   ?    'expression tag'      1332 41 
1 9N15 HIS A 1320 ? UNP Q5MQD0 ?   ?    'expression tag'      1333 42 
1 9N15 HIS A 1321 ? UNP Q5MQD0 ?   ?    'expression tag'      1334 43 
1 9N15 HIS A 1322 ? UNP Q5MQD0 ?   ?    'expression tag'      1335 44 
1 9N15 HIS A 1323 ? UNP Q5MQD0 ?   ?    'expression tag'      1336 45 
1 9N15 HIS A 1324 ? UNP Q5MQD0 ?   ?    'expression tag'      1337 46 
1 9N15 HIS A 1325 ? UNP Q5MQD0 ?   ?    'expression tag'      1338 47 
1 9N15 GLY A 1326 ? UNP Q5MQD0 ?   ?    'expression tag'      1339 48 
1 9N15 ALA A 1327 ? UNP Q5MQD0 ?   ?    'expression tag'      1340 49 
1 9N15 GLY A 1328 ? UNP Q5MQD0 ?   ?    'expression tag'      1341 50 
1 9N15 GLY A 1329 ? UNP Q5MQD0 ?   ?    'expression tag'      1342 51 
1 9N15 LEU A 1330 ? UNP Q5MQD0 ?   ?    'expression tag'      1343 52 
1 9N15 ASN A 1331 ? UNP Q5MQD0 ?   ?    'expression tag'      1344 53 
1 9N15 ASP A 1332 ? UNP Q5MQD0 ?   ?    'expression tag'      1345 54 
1 9N15 ILE A 1333 ? UNP Q5MQD0 ?   ?    'expression tag'      1346 55 
1 9N15 PHE A 1334 ? UNP Q5MQD0 ?   ?    'expression tag'      1347 56 
1 9N15 GLU A 1335 ? UNP Q5MQD0 ?   ?    'expression tag'      1348 57 
1 9N15 ALA A 1336 ? UNP Q5MQD0 ?   ?    'expression tag'      1349 58 
1 9N15 GLN A 1337 ? UNP Q5MQD0 ?   ?    'expression tag'      1350 59 
1 9N15 LYS A 1338 ? UNP Q5MQD0 ?   ?    'expression tag'      1351 60 
1 9N15 ILE A 1339 ? UNP Q5MQD0 ?   ?    'expression tag'      1352 61 
1 9N15 GLU A 1340 ? UNP Q5MQD0 ?   ?    'expression tag'      1353 62 
1 9N15 TRP A 1341 ? UNP Q5MQD0 ?   ?    'expression tag'      1354 63 
1 9N15 HIS A 1342 ? UNP Q5MQD0 ?   ?    'expression tag'      1355 64 
1 9N15 GLU A 1343 ? UNP Q5MQD0 ?   ?    'expression tag'      1356 65 
1 9N15 ASP A 1344 ? UNP Q5MQD0 ?   ?    'expression tag'      1357 66 
1 9N15 THR A 1345 ? UNP Q5MQD0 ?   ?    'expression tag'      1358 67 
1 9N15 ALA A 1346 ? UNP Q5MQD0 ?   ?    'expression tag'      1359 68 
1 9N15 ALA A 1347 ? UNP Q5MQD0 ?   ?    'expression tag'      1360 69 
1 9N15 ALA A 1348 ? UNP Q5MQD0 ?   ?    'expression tag'      1361 70 
# 
_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 
# 
_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 ? ? ? ? ? ? ? 2.026 ? ?               
disulf2  disulf ?    ? A CYS 138 SG  ? ? ? 1_555 A CYS 170 SG ? ? A CYS 151 A CYS 183  1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf3  disulf ?    ? A CYS 150 SG  ? ? ? 1_555 A CYS 229 SG ? ? A CYS 163 A CYS 242  1_555 ? ? ? ? ? ? ? 2.028 ? ?               
covale1  covale one  ? A ASN 6   ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 19  B NAG 1    1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale2  covale one  ? A ASN 45  ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 58  C NAG 1    1_555 ? ? ? ? ? ? ? 1.447 ? N-Glycosylation 
covale3  covale one  ? A ASN 119 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 132 D NAG 1    1_555 ? ? ? ? ? ? ? 1.446 ? N-Glycosylation 
covale4  covale one  ? A ASN 158 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 171 A NAG 1401 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale5  covale one  ? A ASN 175 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 188 E NAG 1    1_555 ? ? ? ? ? ? ? 1.448 ? N-Glycosylation 
covale6  covale one  ? A ASN 179 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 192 F NAG 1    1_555 ? ? ? ? ? ? ? 1.446 ? N-Glycosylation 
covale7  covale one  ? A ASN 238 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 251 A NAG 1402 1_555 ? ? ? ? ? ? ? 1.452 ? N-Glycosylation 
covale8  covale both ? B NAG .   O4  ? ? ? 1_555 B NAG .   C1 ? ? B NAG 1   B NAG 2    1_555 ? ? ? ? ? ? ? 1.466 ? ?               
covale9  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2    1_555 ? ? ? ? ? ? ? 1.466 ? ?               
covale10 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? D NAG 1   D NAG 2    1_555 ? ? ? ? ? ? ? 1.463 ? ?               
covale11 covale both ? D NAG .   O4  ? ? ? 1_555 D BMA .   C1 ? ? D NAG 2   D BMA 3    1_555 ? ? ? ? ? ? ? 1.470 ? ?               
covale12 covale both ? D BMA .   O3  ? ? ? 1_555 D MAN .   C1 ? ? D BMA 3   D MAN 4    1_555 ? ? ? ? ? ? ? 1.471 ? ?               
covale13 covale both ? D BMA .   O6  ? ? ? 1_555 D MAN .   C1 ? ? D BMA 3   D MAN 5    1_555 ? ? ? ? ? ? ? 1.457 ? ?               
covale14 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? E NAG 1   E NAG 2    1_555 ? ? ? ? ? ? ? 1.464 ? ?               
covale15 covale both ? E NAG .   O4  ? ? ? 1_555 E BMA .   C1 ? ? E NAG 2   E BMA 3    1_555 ? ? ? ? ? ? ? 1.465 ? ?               
covale16 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? F NAG 1   F NAG 2    1_555 ? ? ? ? ? ? ? 1.466 ? ?               
# 
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 6   ? NAG B 1    ? 1_555 ASN A 19  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG C .   ? ASN A 45  ? NAG C 1    ? 1_555 ASN A 58  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG D .   ? ASN A 119 ? NAG D 1    ? 1_555 ASN A 132 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG E .   ? ASN A 175 ? NAG E 1    ? 1_555 ASN A 188 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG F .   ? ASN A 179 ? NAG F 1    ? 1_555 ASN A 192 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G .   ? ASN A 158 ? NAG A 1401 ? 1_555 ASN A 171 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H .   ? ASN A 238 ? NAG A 1402 ? 1_555 ASN A 251 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  CYS A 7   ? CYS A 143 ? CYS A 20   ? 1_555 CYS A 156 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS A 138 ? CYS A 170 ? CYS A 151  ? 1_555 CYS A 183 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 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       9.72 
# 
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 SER A 23  ? VAL A 26  ? SER A 36  VAL A 39  
AA2 2 ASN A 60  ? ASP A 63  ? ASN A 73  ASP A 76  
AA2 3 TYR A 243 ? PHE A 257 ? TYR A 256 PHE A 270 
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  ? PRO A 55  ? THR A 59  PRO A 68  
AA3 2 TYR A 243 ? PHE A 257 ? TYR A 256 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  ? VAL A 100 ? THR A 109 VAL A 113 
AA6 2 THR A 103 ? GLU A 107 ? THR A 116 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 TYR A 25  ? N TYR A 38  O PHE A 61  ? O PHE A 74  
AA2 2 3 N ARG A 62  ? N ARG A 75  O VAL A 245 ? O VAL A 258 
AA2 3 4 O TRP A 244 ? O TRP A 257 N ARG A 92  ? N ARG A 105 
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 190 ? N TYR A 203 O TYR A 197 ? O TYR A 210 
AA2 6 7 N PHE A 196 ? N PHE A 209 O LEU A 213 ? O LEU A 226 
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                   9N15 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 170 ? ? CZ A ARG 170 ? ? NH2 A ARG 170 ? ? 123.46 120.30 3.16 0.50 N 
2 1 NE A ARG 264 ? ? CZ A ARG 264 ? ? NH2 A ARG 264 ? ? 123.66 120.30 3.36 0.50 N 
3 1 NE A ARG 273 ? ? CZ A ARG 273 ? ? NH2 A ARG 273 ? ? 124.42 120.30 4.12 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 15  ? ? -85.29  -79.60  
2  1 LEU A 52  ? ? 49.91   -133.44 
3  1 THR A 82  ? ? -120.75 -62.30  
4  1 THR A 83  ? ? -125.24 -55.97  
5  1 ASN A 99  ? ? 48.18   -124.30 
6  1 LYS A 115 ? ? 60.86   -1.76   
7  1 SER A 128 ? ? -138.00 -59.55  
8  1 ASN A 132 ? ? -65.71  13.82   
9  1 CYS A 163 ? ? -64.54  98.19   
10 1 ALA A 244 ? ? -106.33 -161.73 
11 1 THR A 249 ? ? -132.74 -37.20  
12 1 ASP A 250 ? ? -152.75 -4.33   
13 1 ASN A 251 ? ? 54.59   16.41   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     264 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.097 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9N15 
_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                    9N15 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.20 
_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               268011 
_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                 
'Cryo-EM structure of HCoV-HKU1 glycoprotein D1 Domain in complex with 9OAc-GD3(mutant T31VPR34 to GGGG)' 
_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                        9N15 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_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            200 
_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           92000 
_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-2/1 
_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              9N15 
_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                9N15 
_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              9N15 
_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 PRO 750  ? A PRO 737  
470  1 Y 1 A SER 751  ? A SER 738  
471  1 Y 1 A SER 752  ? A SER 739  
472  1 Y 1 A SER 753  ? A SER 740  
473  1 Y 1 A SER 754  ? A SER 741  
474  1 Y 1 A SER 755  ? A SER 742  
475  1 Y 1 A ARG 756  ? A ARG 743  
476  1 Y 1 A ARG 757  ? A ARG 744  
477  1 Y 1 A LYS 758  ? A LYS 745  
478  1 Y 1 A ARG 759  ? A ARG 746  
479  1 Y 1 A ARG 760  ? A ARG 747  
480  1 Y 1 A SER 761  ? A SER 748  
481  1 Y 1 A ILE 762  ? A ILE 749  
482  1 Y 1 A SER 763  ? A SER 750  
483  1 Y 1 A ALA 764  ? A ALA 751  
484  1 Y 1 A SER 765  ? A SER 752  
485  1 Y 1 A TYR 766  ? A TYR 753  
486  1 Y 1 A ARG 767  ? A ARG 754  
487  1 Y 1 A PHE 768  ? A PHE 755  
488  1 Y 1 A VAL 769  ? A VAL 756  
489  1 Y 1 A THR 770  ? A THR 757  
490  1 Y 1 A PHE 771  ? A PHE 758  
491  1 Y 1 A GLU 772  ? A GLU 759  
492  1 Y 1 A PRO 773  ? A PRO 760  
493  1 Y 1 A PHE 774  ? A PHE 761  
494  1 Y 1 A ASN 775  ? A ASN 762  
495  1 Y 1 A VAL 776  ? A VAL 763  
496  1 Y 1 A SER 777  ? A SER 764  
497  1 Y 1 A PHE 778  ? A PHE 765  
498  1 Y 1 A VAL 779  ? A VAL 766  
499  1 Y 1 A ASN 780  ? A ASN 767  
500  1 Y 1 A ASP 781  ? A ASP 768  
501  1 Y 1 A SER 782  ? A SER 769  
502  1 Y 1 A ILE 783  ? A ILE 770  
503  1 Y 1 A GLU 784  ? A GLU 771  
504  1 Y 1 A SER 785  ? A SER 772  
505  1 Y 1 A VAL 786  ? A VAL 773  
506  1 Y 1 A GLY 787  ? A GLY 774  
507  1 Y 1 A GLY 788  ? A GLY 775  
508  1 Y 1 A LEU 789  ? A LEU 776  
509  1 Y 1 A TYR 790  ? A TYR 777  
510  1 Y 1 A GLU 791  ? A GLU 778  
511  1 Y 1 A ILE 792  ? A ILE 779  
512  1 Y 1 A LYS 793  ? A LYS 780  
513  1 Y 1 A ILE 794  ? A ILE 781  
514  1 Y 1 A PRO 795  ? A PRO 782  
515  1 Y 1 A THR 796  ? A THR 783  
516  1 Y 1 A ASN 797  ? A ASN 784  
517  1 Y 1 A PHE 798  ? A PHE 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 VAL 801  ? A VAL 788  
521  1 Y 1 A GLY 802  ? A GLY 789  
522  1 Y 1 A GLN 803  ? A GLN 790  
523  1 Y 1 A GLU 804  ? A GLU 791  
524  1 Y 1 A GLU 805  ? A GLU 792  
525  1 Y 1 A PHE 806  ? A PHE 793  
526  1 Y 1 A ILE 807  ? A ILE 794  
527  1 Y 1 A GLN 808  ? A GLN 795  
528  1 Y 1 A THR 809  ? A THR 796  
529  1 Y 1 A ASN 810  ? A ASN 797  
530  1 Y 1 A SER 811  ? A SER 798  
531  1 Y 1 A PRO 812  ? A PRO 799  
532  1 Y 1 A LYS 813  ? A LYS 800  
533  1 Y 1 A VAL 814  ? A VAL 801  
534  1 Y 1 A THR 815  ? A THR 802  
535  1 Y 1 A ILE 816  ? A ILE 803  
536  1 Y 1 A ASP 817  ? A ASP 804  
537  1 Y 1 A CYS 818  ? A CYS 805  
538  1 Y 1 A SER 819  ? A SER 806  
539  1 Y 1 A LEU 820  ? A LEU 807  
540  1 Y 1 A PHE 821  ? A PHE 808  
541  1 Y 1 A VAL 822  ? A VAL 809  
542  1 Y 1 A CYS 823  ? A CYS 810  
543  1 Y 1 A SER 824  ? A SER 811  
544  1 Y 1 A ASN 825  ? A ASN 812  
545  1 Y 1 A TYR 826  ? A TYR 813  
546  1 Y 1 A ALA 827  ? A ALA 814  
547  1 Y 1 A ALA 828  ? A ALA 815  
548  1 Y 1 A CYS 829  ? A CYS 816  
549  1 Y 1 A HIS 830  ? A HIS 817  
550  1 Y 1 A ASP 831  ? A ASP 818  
551  1 Y 1 A LEU 832  ? A LEU 819  
552  1 Y 1 A LEU 833  ? A LEU 820  
553  1 Y 1 A SER 834  ? A SER 821  
554  1 Y 1 A GLU 835  ? A GLU 822  
555  1 Y 1 A TYR 836  ? A TYR 823  
556  1 Y 1 A GLY 837  ? A GLY 824  
557  1 Y 1 A THR 838  ? A THR 825  
558  1 Y 1 A PHE 839  ? A PHE 826  
559  1 Y 1 A CYS 840  ? A CYS 827  
560  1 Y 1 A ASP 841  ? A ASP 828  
561  1 Y 1 A ASN 842  ? A ASN 829  
562  1 Y 1 A ILE 843  ? A ILE 830  
563  1 Y 1 A ASN 844  ? A ASN 831  
564  1 Y 1 A SER 845  ? A SER 832  
565  1 Y 1 A ILE 846  ? A ILE 833  
566  1 Y 1 A LEU 847  ? A LEU 834  
567  1 Y 1 A ASP 848  ? A ASP 835  
568  1 Y 1 A GLU 849  ? A GLU 836  
569  1 Y 1 A VAL 850  ? A VAL 837  
570  1 Y 1 A ASN 851  ? A ASN 838  
571  1 Y 1 A GLY 852  ? A GLY 839  
572  1 Y 1 A LEU 853  ? A LEU 840  
573  1 Y 1 A LEU 854  ? A LEU 841  
574  1 Y 1 A ASP 855  ? A ASP 842  
575  1 Y 1 A THR 856  ? A THR 843  
576  1 Y 1 A THR 857  ? A THR 844  
577  1 Y 1 A GLN 858  ? A GLN 845  
578  1 Y 1 A LEU 859  ? A LEU 846  
579  1 Y 1 A HIS 860  ? A HIS 847  
580  1 Y 1 A VAL 861  ? A VAL 848  
581  1 Y 1 A ALA 862  ? A ALA 849  
582  1 Y 1 A ASP 863  ? A ASP 850  
583  1 Y 1 A THR 864  ? A THR 851  
584  1 Y 1 A LEU 865  ? A LEU 852  
585  1 Y 1 A MET 866  ? A MET 853  
586  1 Y 1 A GLN 867  ? A GLN 854  
587  1 Y 1 A GLY 868  ? A GLY 855  
588  1 Y 1 A VAL 869  ? A VAL 856  
589  1 Y 1 A THR 870  ? A THR 857  
590  1 Y 1 A LEU 871  ? A LEU 858  
591  1 Y 1 A SER 872  ? A SER 859  
592  1 Y 1 A SER 873  ? A SER 860  
593  1 Y 1 A ASN 874  ? A ASN 861  
594  1 Y 1 A LEU 875  ? A LEU 862  
595  1 Y 1 A ASN 876  ? A ASN 863  
596  1 Y 1 A THR 877  ? A THR 864  
597  1 Y 1 A ASN 878  ? A ASN 865  
598  1 Y 1 A LEU 879  ? A LEU 866  
599  1 Y 1 A HIS 880  ? A HIS 867  
600  1 Y 1 A PHE 881  ? A PHE 868  
601  1 Y 1 A ASP 882  ? A ASP 869  
602  1 Y 1 A VAL 883  ? A VAL 870  
603  1 Y 1 A ASP 884  ? A ASP 871  
604  1 Y 1 A ASN 885  ? A ASN 872  
605  1 Y 1 A ILE 886  ? A ILE 873  
606  1 Y 1 A ASN 887  ? A ASN 874  
607  1 Y 1 A PHE 888  ? A PHE 875  
608  1 Y 1 A LYS 889  ? A LYS 876  
609  1 Y 1 A SER 890  ? A SER 877  
610  1 Y 1 A LEU 891  ? A LEU 878  
611  1 Y 1 A VAL 892  ? A VAL 879  
612  1 Y 1 A GLY 893  ? A GLY 880  
613  1 Y 1 A CYS 894  ? A CYS 881  
614  1 Y 1 A LEU 895  ? A LEU 882  
615  1 Y 1 A GLY 896  ? A GLY 883  
616  1 Y 1 A PRO 897  ? A PRO 884  
617  1 Y 1 A HIS 898  ? A HIS 885  
618  1 Y 1 A CYS 899  ? A CYS 886  
619  1 Y 1 A GLY 900  ? A GLY 887  
620  1 Y 1 A SER 901  ? A SER 888  
621  1 Y 1 A SER 902  ? A SER 889  
622  1 Y 1 A SER 903  ? A SER 890  
623  1 Y 1 A ARG 904  ? A ARG 891  
624  1 Y 1 A SER 905  ? A SER 892  
625  1 Y 1 A PHE 906  ? A PHE 893  
626  1 Y 1 A PHE 907  ? A PHE 894  
627  1 Y 1 A GLU 908  ? A GLU 895  
628  1 Y 1 A ASP 909  ? A ASP 896  
629  1 Y 1 A LEU 910  ? A LEU 897  
630  1 Y 1 A LEU 911  ? A LEU 898  
631  1 Y 1 A PHE 912  ? A PHE 899  
632  1 Y 1 A ASP 913  ? A ASP 900  
633  1 Y 1 A LYS 914  ? A LYS 901  
634  1 Y 1 A VAL 915  ? A VAL 902  
635  1 Y 1 A LYS 916  ? A LYS 903  
636  1 Y 1 A LEU 917  ? A LEU 904  
637  1 Y 1 A SER 918  ? A SER 905  
638  1 Y 1 A ASP 919  ? A ASP 906  
639  1 Y 1 A VAL 920  ? A VAL 907  
640  1 Y 1 A GLY 921  ? A GLY 908  
641  1 Y 1 A PHE 922  ? A PHE 909  
642  1 Y 1 A VAL 923  ? A VAL 910  
643  1 Y 1 A GLU 924  ? A GLU 911  
644  1 Y 1 A ALA 925  ? A ALA 912  
645  1 Y 1 A TYR 926  ? A TYR 913  
646  1 Y 1 A ASN 927  ? A ASN 914  
647  1 Y 1 A ASN 928  ? A ASN 915  
648  1 Y 1 A CYS 929  ? A CYS 916  
649  1 Y 1 A THR 930  ? A THR 917  
650  1 Y 1 A GLY 931  ? A GLY 918  
651  1 Y 1 A GLY 932  ? A GLY 919  
652  1 Y 1 A SER 933  ? A SER 920  
653  1 Y 1 A GLU 934  ? A GLU 921  
654  1 Y 1 A ILE 935  ? A ILE 922  
655  1 Y 1 A ARG 936  ? A ARG 923  
656  1 Y 1 A ASP 937  ? A ASP 924  
657  1 Y 1 A LEU 938  ? A LEU 925  
658  1 Y 1 A LEU 939  ? A LEU 926  
659  1 Y 1 A CYS 940  ? A CYS 927  
660  1 Y 1 A VAL 941  ? A VAL 928  
661  1 Y 1 A GLN 942  ? A GLN 929  
662  1 Y 1 A SER 943  ? A SER 930  
663  1 Y 1 A PHE 944  ? A PHE 931  
664  1 Y 1 A ASN 945  ? A ASN 932  
665  1 Y 1 A GLY 946  ? A GLY 933  
666  1 Y 1 A ILE 947  ? A ILE 934  
667  1 Y 1 A LYS 948  ? A LYS 935  
668  1 Y 1 A VAL 949  ? A VAL 936  
669  1 Y 1 A LEU 950  ? A LEU 937  
670  1 Y 1 A PRO 951  ? A PRO 938  
671  1 Y 1 A PRO 952  ? A PRO 939  
672  1 Y 1 A ILE 953  ? A ILE 940  
673  1 Y 1 A LEU 954  ? A LEU 941  
674  1 Y 1 A SER 955  ? A SER 942  
675  1 Y 1 A GLU 956  ? A GLU 943  
676  1 Y 1 A SER 957  ? A SER 944  
677  1 Y 1 A GLN 958  ? A GLN 945  
678  1 Y 1 A ILE 959  ? A ILE 946  
679  1 Y 1 A SER 960  ? A SER 947  
680  1 Y 1 A GLY 961  ? A GLY 948  
681  1 Y 1 A TYR 962  ? A TYR 949  
682  1 Y 1 A THR 963  ? A THR 950  
683  1 Y 1 A THR 964  ? A THR 951  
684  1 Y 1 A ALA 965  ? A ALA 952  
685  1 Y 1 A ALA 966  ? A ALA 953  
686  1 Y 1 A THR 967  ? A THR 954  
687  1 Y 1 A VAL 968  ? A VAL 955  
688  1 Y 1 A ALA 969  ? A ALA 956  
689  1 Y 1 A ALA 970  ? A ALA 957  
690  1 Y 1 A MET 971  ? A MET 958  
691  1 Y 1 A PHE 972  ? A PHE 959  
692  1 Y 1 A PRO 973  ? A PRO 960  
693  1 Y 1 A PRO 974  ? A PRO 961  
694  1 Y 1 A TRP 975  ? A TRP 962  
695  1 Y 1 A SER 976  ? A SER 963  
696  1 Y 1 A ALA 977  ? A ALA 964  
697  1 Y 1 A ALA 978  ? A ALA 965  
698  1 Y 1 A ALA 979  ? A ALA 966  
699  1 Y 1 A GLY 980  ? A GLY 967  
700  1 Y 1 A ILE 981  ? A ILE 968  
701  1 Y 1 A PRO 982  ? A PRO 969  
702  1 Y 1 A PHE 983  ? A PHE 970  
703  1 Y 1 A SER 984  ? A SER 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 VAL 987  ? A VAL 974  
707  1 Y 1 A GLN 988  ? A GLN 975  
708  1 Y 1 A TYR 989  ? A TYR 976  
709  1 Y 1 A ARG 990  ? A ARG 977  
710  1 Y 1 A ILE 991  ? A ILE 978  
711  1 Y 1 A ASN 992  ? A ASN 979  
712  1 Y 1 A GLY 993  ? A GLY 980  
713  1 Y 1 A LEU 994  ? A LEU 981  
714  1 Y 1 A GLY 995  ? A GLY 982  
715  1 Y 1 A VAL 996  ? A VAL 983  
716  1 Y 1 A THR 997  ? A THR 984  
717  1 Y 1 A MET 998  ? A MET 985  
718  1 Y 1 A ASP 999  ? A ASP 986  
719  1 Y 1 A VAL 1000 ? A VAL 987  
720  1 Y 1 A LEU 1001 ? A LEU 988  
721  1 Y 1 A ASN 1002 ? A ASN 989  
722  1 Y 1 A LYS 1003 ? A LYS 990  
723  1 Y 1 A ASN 1004 ? A ASN 991  
724  1 Y 1 A GLN 1005 ? A GLN 992  
725  1 Y 1 A LYS 1006 ? A LYS 993  
726  1 Y 1 A LEU 1007 ? A LEU 994  
727  1 Y 1 A ILE 1008 ? A ILE 995  
728  1 Y 1 A ALA 1009 ? A ALA 996  
729  1 Y 1 A THR 1010 ? A THR 997  
730  1 Y 1 A ALA 1011 ? A ALA 998  
731  1 Y 1 A PHE 1012 ? A PHE 999  
732  1 Y 1 A ASN 1013 ? A ASN 1000 
733  1 Y 1 A ASN 1014 ? A ASN 1001 
734  1 Y 1 A ALA 1015 ? A ALA 1002 
735  1 Y 1 A LEU 1016 ? A LEU 1003 
736  1 Y 1 A LEU 1017 ? A LEU 1004 
737  1 Y 1 A SER 1018 ? A SER 1005 
738  1 Y 1 A ILE 1019 ? A ILE 1006 
739  1 Y 1 A GLN 1020 ? A GLN 1007 
740  1 Y 1 A ASN 1021 ? A ASN 1008 
741  1 Y 1 A GLY 1022 ? A GLY 1009 
742  1 Y 1 A PHE 1023 ? A PHE 1010 
743  1 Y 1 A SER 1024 ? A SER 1011 
744  1 Y 1 A ALA 1025 ? A ALA 1012 
745  1 Y 1 A PRO 1026 ? A PRO 1013 
746  1 Y 1 A ASN 1027 ? A ASN 1014 
747  1 Y 1 A SER 1028 ? A SER 1015 
748  1 Y 1 A ALA 1029 ? A ALA 1016 
749  1 Y 1 A LEU 1030 ? A LEU 1017 
750  1 Y 1 A ALA 1031 ? A ALA 1018 
751  1 Y 1 A LYS 1032 ? A LYS 1019 
752  1 Y 1 A ILE 1033 ? A ILE 1020 
753  1 Y 1 A GLN 1034 ? A GLN 1021 
754  1 Y 1 A SER 1035 ? A SER 1022 
755  1 Y 1 A VAL 1036 ? A VAL 1023 
756  1 Y 1 A VAL 1037 ? A VAL 1024 
757  1 Y 1 A ASN 1038 ? A ASN 1025 
758  1 Y 1 A SER 1039 ? A SER 1026 
759  1 Y 1 A ASN 1040 ? A ASN 1027 
760  1 Y 1 A ALA 1041 ? A ALA 1028 
761  1 Y 1 A GLN 1042 ? A GLN 1029 
762  1 Y 1 A ALA 1043 ? A ALA 1030 
763  1 Y 1 A LEU 1044 ? A LEU 1031 
764  1 Y 1 A ASN 1045 ? A ASN 1032 
765  1 Y 1 A SER 1046 ? A SER 1033 
766  1 Y 1 A LEU 1047 ? A LEU 1034 
767  1 Y 1 A LEU 1048 ? A LEU 1035 
768  1 Y 1 A GLN 1049 ? A GLN 1036 
769  1 Y 1 A GLN 1050 ? A GLN 1037 
770  1 Y 1 A LEU 1051 ? A LEU 1038 
771  1 Y 1 A PHE 1052 ? A PHE 1039 
772  1 Y 1 A ASN 1053 ? A ASN 1040 
773  1 Y 1 A LYS 1054 ? A LYS 1041 
774  1 Y 1 A PHE 1055 ? A PHE 1042 
775  1 Y 1 A GLY 1056 ? A GLY 1043 
776  1 Y 1 A ALA 1057 ? A ALA 1044 
777  1 Y 1 A ILE 1058 ? A ILE 1045 
778  1 Y 1 A SER 1059 ? A SER 1046 
779  1 Y 1 A SER 1060 ? A SER 1047 
780  1 Y 1 A SER 1061 ? A SER 1048 
781  1 Y 1 A LEU 1062 ? A LEU 1049 
782  1 Y 1 A GLN 1063 ? A GLN 1050 
783  1 Y 1 A GLU 1064 ? A GLU 1051 
784  1 Y 1 A ILE 1065 ? A ILE 1052 
785  1 Y 1 A LEU 1066 ? A LEU 1053 
786  1 Y 1 A SER 1067 ? A SER 1054 
787  1 Y 1 A ARG 1068 ? A ARG 1055 
788  1 Y 1 A LEU 1069 ? A LEU 1056 
789  1 Y 1 A ASP 1070 ? A ASP 1057 
790  1 Y 1 A PRO 1071 ? A PRO 1058 
791  1 Y 1 A PRO 1072 ? A PRO 1059 
792  1 Y 1 A GLU 1073 ? A GLU 1060 
793  1 Y 1 A ALA 1074 ? A ALA 1061 
794  1 Y 1 A GLN 1075 ? A GLN 1062 
795  1 Y 1 A VAL 1076 ? A VAL 1063 
796  1 Y 1 A GLN 1077 ? A GLN 1064 
797  1 Y 1 A ILE 1078 ? A ILE 1065 
798  1 Y 1 A ASP 1079 ? A ASP 1066 
799  1 Y 1 A ARG 1080 ? A ARG 1067 
800  1 Y 1 A LEU 1081 ? A LEU 1068 
801  1 Y 1 A ILE 1082 ? A ILE 1069 
802  1 Y 1 A ASN 1083 ? A ASN 1070 
803  1 Y 1 A GLY 1084 ? A GLY 1071 
804  1 Y 1 A ARG 1085 ? A ARG 1072 
805  1 Y 1 A LEU 1086 ? A LEU 1073 
806  1 Y 1 A THR 1087 ? A THR 1074 
807  1 Y 1 A ALA 1088 ? A ALA 1075 
808  1 Y 1 A LEU 1089 ? A LEU 1076 
809  1 Y 1 A ASN 1090 ? A ASN 1077 
810  1 Y 1 A ALA 1091 ? A ALA 1078 
811  1 Y 1 A TYR 1092 ? A TYR 1079 
812  1 Y 1 A VAL 1093 ? A VAL 1080 
813  1 Y 1 A SER 1094 ? A SER 1081 
814  1 Y 1 A GLN 1095 ? A GLN 1082 
815  1 Y 1 A GLN 1096 ? A GLN 1083 
816  1 Y 1 A LEU 1097 ? A LEU 1084 
817  1 Y 1 A SER 1098 ? A SER 1085 
818  1 Y 1 A ASP 1099 ? A ASP 1086 
819  1 Y 1 A ILE 1100 ? A ILE 1087 
820  1 Y 1 A SER 1101 ? A SER 1088 
821  1 Y 1 A LEU 1102 ? A LEU 1089 
822  1 Y 1 A VAL 1103 ? A VAL 1090 
823  1 Y 1 A LYS 1104 ? A LYS 1091 
824  1 Y 1 A PHE 1105 ? A PHE 1092 
825  1 Y 1 A GLY 1106 ? A GLY 1093 
826  1 Y 1 A ALA 1107 ? A ALA 1094 
827  1 Y 1 A ALA 1108 ? A ALA 1095 
828  1 Y 1 A LEU 1109 ? A LEU 1096 
829  1 Y 1 A ALA 1110 ? A ALA 1097 
830  1 Y 1 A MET 1111 ? A MET 1098 
831  1 Y 1 A GLU 1112 ? A GLU 1099 
832  1 Y 1 A LYS 1113 ? A LYS 1100 
833  1 Y 1 A VAL 1114 ? A VAL 1101 
834  1 Y 1 A ASN 1115 ? A ASN 1102 
835  1 Y 1 A GLU 1116 ? A GLU 1103 
836  1 Y 1 A CYS 1117 ? A CYS 1104 
837  1 Y 1 A VAL 1118 ? A VAL 1105 
838  1 Y 1 A LYS 1119 ? A LYS 1106 
839  1 Y 1 A SER 1120 ? A SER 1107 
840  1 Y 1 A GLN 1121 ? A GLN 1108 
841  1 Y 1 A SER 1122 ? A SER 1109 
842  1 Y 1 A PRO 1123 ? A PRO 1110 
843  1 Y 1 A ARG 1124 ? A ARG 1111 
844  1 Y 1 A ILE 1125 ? A ILE 1112 
845  1 Y 1 A ASN 1126 ? A ASN 1113 
846  1 Y 1 A PHE 1127 ? A PHE 1114 
847  1 Y 1 A CYS 1128 ? A CYS 1115 
848  1 Y 1 A GLY 1129 ? A GLY 1116 
849  1 Y 1 A ASN 1130 ? A ASN 1117 
850  1 Y 1 A GLY 1131 ? A GLY 1118 
851  1 Y 1 A ASN 1132 ? A ASN 1119 
852  1 Y 1 A HIS 1133 ? A HIS 1120 
853  1 Y 1 A ILE 1134 ? A ILE 1121 
854  1 Y 1 A LEU 1135 ? A LEU 1122 
855  1 Y 1 A SER 1136 ? A SER 1123 
856  1 Y 1 A LEU 1137 ? A LEU 1124 
857  1 Y 1 A VAL 1138 ? A VAL 1125 
858  1 Y 1 A GLN 1139 ? A GLN 1126 
859  1 Y 1 A ASN 1140 ? A ASN 1127 
860  1 Y 1 A ALA 1141 ? A ALA 1128 
861  1 Y 1 A PRO 1142 ? A PRO 1129 
862  1 Y 1 A TYR 1143 ? A TYR 1130 
863  1 Y 1 A GLY 1144 ? A GLY 1131 
864  1 Y 1 A LEU 1145 ? A LEU 1132 
865  1 Y 1 A LEU 1146 ? A LEU 1133 
866  1 Y 1 A PHE 1147 ? A PHE 1134 
867  1 Y 1 A MET 1148 ? A MET 1135 
868  1 Y 1 A HIS 1149 ? A HIS 1136 
869  1 Y 1 A PHE 1150 ? A PHE 1137 
870  1 Y 1 A SER 1151 ? A SER 1138 
871  1 Y 1 A TYR 1152 ? A TYR 1139 
872  1 Y 1 A LYS 1153 ? A LYS 1140 
873  1 Y 1 A PRO 1154 ? A PRO 1141 
874  1 Y 1 A ILE 1155 ? A ILE 1142 
875  1 Y 1 A SER 1156 ? A SER 1143 
876  1 Y 1 A PHE 1157 ? A PHE 1144 
877  1 Y 1 A LYS 1158 ? A LYS 1145 
878  1 Y 1 A THR 1159 ? A THR 1146 
879  1 Y 1 A VAL 1160 ? A VAL 1147 
880  1 Y 1 A LEU 1161 ? A LEU 1148 
881  1 Y 1 A VAL 1162 ? A VAL 1149 
882  1 Y 1 A SER 1163 ? A SER 1150 
883  1 Y 1 A PRO 1164 ? A PRO 1151 
884  1 Y 1 A GLY 1165 ? A GLY 1152 
885  1 Y 1 A LEU 1166 ? A LEU 1153 
886  1 Y 1 A CYS 1167 ? A CYS 1154 
887  1 Y 1 A ILE 1168 ? A ILE 1155 
888  1 Y 1 A SER 1169 ? A SER 1156 
889  1 Y 1 A GLY 1170 ? A GLY 1157 
890  1 Y 1 A ASP 1171 ? A ASP 1158 
891  1 Y 1 A VAL 1172 ? A VAL 1159 
892  1 Y 1 A GLY 1173 ? A GLY 1160 
893  1 Y 1 A ILE 1174 ? A ILE 1161 
894  1 Y 1 A ALA 1175 ? A ALA 1162 
895  1 Y 1 A PRO 1176 ? A PRO 1163 
896  1 Y 1 A LYS 1177 ? A LYS 1164 
897  1 Y 1 A GLN 1178 ? A GLN 1165 
898  1 Y 1 A GLY 1179 ? A GLY 1166 
899  1 Y 1 A TYR 1180 ? A TYR 1167 
900  1 Y 1 A PHE 1181 ? A PHE 1168 
901  1 Y 1 A ILE 1182 ? A ILE 1169 
902  1 Y 1 A LYS 1183 ? A LYS 1170 
903  1 Y 1 A HIS 1184 ? A HIS 1171 
904  1 Y 1 A ASN 1185 ? A ASN 1172 
905  1 Y 1 A ASP 1186 ? A ASP 1173 
906  1 Y 1 A HIS 1187 ? A HIS 1174 
907  1 Y 1 A TRP 1188 ? A TRP 1175 
908  1 Y 1 A MET 1189 ? A MET 1176 
909  1 Y 1 A PHE 1190 ? A PHE 1177 
910  1 Y 1 A THR 1191 ? A THR 1178 
911  1 Y 1 A GLY 1192 ? A GLY 1179 
912  1 Y 1 A SER 1193 ? A SER 1180 
913  1 Y 1 A SER 1194 ? A SER 1181 
914  1 Y 1 A TYR 1195 ? A TYR 1182 
915  1 Y 1 A TYR 1196 ? A TYR 1183 
916  1 Y 1 A TYR 1197 ? A TYR 1184 
917  1 Y 1 A PRO 1198 ? A PRO 1185 
918  1 Y 1 A GLU 1199 ? A GLU 1186 
919  1 Y 1 A PRO 1200 ? A PRO 1187 
920  1 Y 1 A ILE 1201 ? A ILE 1188 
921  1 Y 1 A SER 1202 ? A SER 1189 
922  1 Y 1 A ASP 1203 ? A ASP 1190 
923  1 Y 1 A LYS 1204 ? A LYS 1191 
924  1 Y 1 A ASN 1205 ? A ASN 1192 
925  1 Y 1 A VAL 1206 ? A VAL 1193 
926  1 Y 1 A VAL 1207 ? A VAL 1194 
927  1 Y 1 A PHE 1208 ? A PHE 1195 
928  1 Y 1 A MET 1209 ? A MET 1196 
929  1 Y 1 A ASN 1210 ? A ASN 1197 
930  1 Y 1 A THR 1211 ? A THR 1198 
931  1 Y 1 A CYS 1212 ? A CYS 1199 
932  1 Y 1 A SER 1213 ? A SER 1200 
933  1 Y 1 A VAL 1214 ? A VAL 1201 
934  1 Y 1 A ASN 1215 ? A ASN 1202 
935  1 Y 1 A PHE 1216 ? A PHE 1203 
936  1 Y 1 A THR 1217 ? A THR 1204 
937  1 Y 1 A LYS 1218 ? A LYS 1205 
938  1 Y 1 A ALA 1219 ? A ALA 1206 
939  1 Y 1 A PRO 1220 ? A PRO 1207 
940  1 Y 1 A LEU 1221 ? A LEU 1208 
941  1 Y 1 A VAL 1222 ? A VAL 1209 
942  1 Y 1 A TYR 1223 ? A TYR 1210 
943  1 Y 1 A LEU 1224 ? A LEU 1211 
944  1 Y 1 A ASN 1225 ? A ASN 1212 
945  1 Y 1 A HIS 1226 ? A HIS 1213 
946  1 Y 1 A SER 1227 ? A SER 1214 
947  1 Y 1 A VAL 1228 ? A VAL 1215 
948  1 Y 1 A PRO 1229 ? A PRO 1216 
949  1 Y 1 A LYS 1230 ? A LYS 1217 
950  1 Y 1 A LEU 1231 ? A LEU 1218 
951  1 Y 1 A SER 1232 ? A SER 1219 
952  1 Y 1 A ASP 1233 ? A ASP 1220 
953  1 Y 1 A PHE 1234 ? A PHE 1221 
954  1 Y 1 A GLU 1235 ? A GLU 1222 
955  1 Y 1 A SER 1236 ? A SER 1223 
956  1 Y 1 A GLU 1237 ? A GLU 1224 
957  1 Y 1 A LEU 1238 ? A LEU 1225 
958  1 Y 1 A SER 1239 ? A SER 1226 
959  1 Y 1 A HIS 1240 ? A HIS 1227 
960  1 Y 1 A TRP 1241 ? A TRP 1228 
961  1 Y 1 A PHE 1242 ? A PHE 1229 
962  1 Y 1 A LYS 1243 ? A LYS 1230 
963  1 Y 1 A ASN 1244 ? A ASN 1231 
964  1 Y 1 A GLN 1245 ? A GLN 1232 
965  1 Y 1 A THR 1246 ? A THR 1233 
966  1 Y 1 A SER 1247 ? A SER 1234 
967  1 Y 1 A ILE 1248 ? A ILE 1235 
968  1 Y 1 A ALA 1249 ? A ALA 1236 
969  1 Y 1 A PRO 1250 ? A PRO 1237 
970  1 Y 1 A ASN 1251 ? A ASN 1238 
971  1 Y 1 A LEU 1252 ? A LEU 1239 
972  1 Y 1 A THR 1253 ? A THR 1240 
973  1 Y 1 A LEU 1254 ? A LEU 1241 
974  1 Y 1 A ASN 1255 ? A ASN 1242 
975  1 Y 1 A LEU 1256 ? A LEU 1243 
976  1 Y 1 A HIS 1257 ? A HIS 1244 
977  1 Y 1 A THR 1258 ? A THR 1245 
978  1 Y 1 A ILE 1259 ? A ILE 1246 
979  1 Y 1 A ASN 1260 ? A ASN 1247 
980  1 Y 1 A ALA 1261 ? A ALA 1248 
981  1 Y 1 A THR 1262 ? A THR 1249 
982  1 Y 1 A PHE 1263 ? A PHE 1250 
983  1 Y 1 A LEU 1264 ? A LEU 1251 
984  1 Y 1 A ASP 1265 ? A ASP 1252 
985  1 Y 1 A LEU 1266 ? A LEU 1253 
986  1 Y 1 A TYR 1267 ? A TYR 1254 
987  1 Y 1 A TYR 1268 ? A TYR 1255 
988  1 Y 1 A GLU 1269 ? A GLU 1256 
989  1 Y 1 A MET 1270 ? A MET 1257 
990  1 Y 1 A ASN 1271 ? A ASN 1258 
991  1 Y 1 A LEU 1272 ? A LEU 1259 
992  1 Y 1 A ILE 1273 ? A ILE 1260 
993  1 Y 1 A GLN 1274 ? A GLN 1261 
994  1 Y 1 A GLU 1275 ? A GLU 1262 
995  1 Y 1 A SER 1276 ? A SER 1263 
996  1 Y 1 A ILE 1277 ? A ILE 1264 
997  1 Y 1 A LYS 1278 ? A LYS 1265 
998  1 Y 1 A SER 1279 ? A SER 1266 
999  1 Y 1 A LEU 1280 ? A LEU 1267 
1000 1 Y 1 A ASN 1281 ? A ASN 1268 
1001 1 Y 1 A ASN 1282 ? A ASN 1269 
1002 1 Y 1 A SER 1283 ? A SER 1270 
1003 1 Y 1 A TYR 1284 ? A TYR 1271 
1004 1 Y 1 A ILE 1285 ? A ILE 1272 
1005 1 Y 1 A ASN 1286 ? A ASN 1273 
1006 1 Y 1 A LEU 1287 ? A LEU 1274 
1007 1 Y 1 A LYS 1288 ? A LYS 1275 
1008 1 Y 1 A ASP 1289 ? A ASP 1276 
1009 1 Y 1 A ILE 1290 ? A ILE 1277 
1010 1 Y 1 A GLY 1291 ? A GLY 1278 
1011 1 Y 1 A THR 1292 ? A THR 1279 
1012 1 Y 1 A TYR 1293 ? A TYR 1280 
1013 1 Y 1 A GLU 1294 ? A GLU 1281 
1014 1 Y 1 A MET 1295 ? A MET 1282 
1015 1 Y 1 A TYR 1296 ? A TYR 1283 
1016 1 Y 1 A VAL 1297 ? A VAL 1284 
1017 1 Y 1 A LYS 1298 ? A LYS 1285 
1018 1 Y 1 A SER 1299 ? A SER 1286 
1019 1 Y 1 A GLY 1300 ? A GLY 1287 
1020 1 Y 1 A GLY 1301 ? A GLY 1288 
1021 1 Y 1 A TYR 1302 ? A TYR 1289 
1022 1 Y 1 A ILE 1303 ? A ILE 1290 
1023 1 Y 1 A PRO 1304 ? A PRO 1291 
1024 1 Y 1 A GLU 1305 ? A GLU 1292 
1025 1 Y 1 A ALA 1306 ? A ALA 1293 
1026 1 Y 1 A PRO 1307 ? A PRO 1294 
1027 1 Y 1 A ARG 1308 ? A ARG 1295 
1028 1 Y 1 A ASP 1309 ? A ASP 1296 
1029 1 Y 1 A GLY 1310 ? A GLY 1297 
1030 1 Y 1 A GLN 1311 ? A GLN 1298 
1031 1 Y 1 A ALA 1312 ? A ALA 1299 
1032 1 Y 1 A TYR 1313 ? A TYR 1300 
1033 1 Y 1 A VAL 1314 ? A VAL 1301 
1034 1 Y 1 A ARG 1315 ? A ARG 1302 
1035 1 Y 1 A LYS 1316 ? A LYS 1303 
1036 1 Y 1 A ASP 1317 ? A ASP 1304 
1037 1 Y 1 A GLY 1318 ? A GLY 1305 
1038 1 Y 1 A GLU 1319 ? A GLU 1306 
1039 1 Y 1 A TRP 1320 ? A TRP 1307 
1040 1 Y 1 A VAL 1321 ? A VAL 1308 
1041 1 Y 1 A LEU 1322 ? A LEU 1309 
1042 1 Y 1 A LEU 1323 ? A LEU 1310 
1043 1 Y 1 A SER 1324 ? A SER 1311 
1044 1 Y 1 A THR 1325 ? A THR 1312 
1045 1 Y 1 A PHE 1326 ? A PHE 1313 
1046 1 Y 1 A LEU 1327 ? A LEU 1314 
1047 1 Y 1 A ASN 1328 ? A ASN 1315 
1048 1 Y 1 A SER 1329 ? A SER 1316 
1049 1 Y 1 A GLY 1330 ? A GLY 1317 
1050 1 Y 1 A ARG 1331 ? A ARG 1318 
1051 1 Y 1 A ALA 1332 ? A ALA 1319 
1052 1 Y 1 A HIS 1333 ? A HIS 1320 
1053 1 Y 1 A HIS 1334 ? A HIS 1321 
1054 1 Y 1 A HIS 1335 ? A HIS 1322 
1055 1 Y 1 A HIS 1336 ? A HIS 1323 
1056 1 Y 1 A HIS 1337 ? A HIS 1324 
1057 1 Y 1 A HIS 1338 ? A HIS 1325 
1058 1 Y 1 A GLY 1339 ? A GLY 1326 
1059 1 Y 1 A ALA 1340 ? A ALA 1327 
1060 1 Y 1 A GLY 1341 ? A GLY 1328 
1061 1 Y 1 A GLY 1342 ? A GLY 1329 
1062 1 Y 1 A LEU 1343 ? A LEU 1330 
1063 1 Y 1 A ASN 1344 ? A ASN 1331 
1064 1 Y 1 A ASP 1345 ? A ASP 1332 
1065 1 Y 1 A ILE 1346 ? A ILE 1333 
1066 1 Y 1 A PHE 1347 ? A PHE 1334 
1067 1 Y 1 A GLU 1348 ? A GLU 1335 
1068 1 Y 1 A ALA 1349 ? A ALA 1336 
1069 1 Y 1 A GLN 1350 ? A GLN 1337 
1070 1 Y 1 A LYS 1351 ? A LYS 1338 
1071 1 Y 1 A ILE 1352 ? A ILE 1339 
1072 1 Y 1 A GLU 1353 ? A GLU 1340 
1073 1 Y 1 A TRP 1354 ? A TRP 1341 
1074 1 Y 1 A HIS 1355 ? A HIS 1342 
1075 1 Y 1 A GLU 1356 ? A GLU 1343 
1076 1 Y 1 A ASP 1357 ? A ASP 1344 
1077 1 Y 1 A THR 1358 ? A THR 1345 
1078 1 Y 1 A ALA 1359 ? A ALA 1346 
1079 1 Y 1 A ALA 1360 ? A ALA 1347 
1080 1 Y 1 A ALA 1361 ? A ALA 1348 
# 
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    2025-01-24 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9N15 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-05-14 
_em_admin.title              
'Cryo-EM structure of HCoV-HKU1 glycoprotein D1 Domain in complex with 9OAc-GD3(mutant T31VPR34 to GGGG)' 
# 
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                0.457593 
# 
_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 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
3 MAN 4 n 
3 MAN 5 n 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
# 
_atom_sites.entry_id                    9N15 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
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   ? 200.392 143.110 107.588 1.00 128.56 ? 14   VAL   A N    1 
ATOM   2    C CA   . VAL   A 1 1   ? 200.477 144.439 106.922 1.00 126.41 ? 14   VAL   A CA   1 
ATOM   3    C C    . VAL   A 1 1   ? 199.227 145.259 107.218 1.00 126.00 ? 14   VAL   A C    1 
ATOM   4    O O    . VAL   A 1 1   ? 198.188 144.671 107.496 1.00 124.52 ? 14   VAL   A O    1 
ATOM   5    C CB   . VAL   A 1 1   ? 200.664 144.323 105.401 1.00 126.97 ? 14   VAL   A CB   1 
ATOM   6    C CG1  . VAL   A 1 1   ? 202.007 143.684 105.054 1.00 124.12 ? 14   VAL   A CG1  1 
ATOM   7    C CG2  . VAL   A 1 1   ? 199.563 143.530 104.686 1.00 133.03 ? 14   VAL   A CG2  1 
ATOM   8    H H1   . VAL   A 1 1   ? 200.342 143.217 108.591 1.00 129.04 ? 14   VAL   A H1   1 
ATOM   9    H H2   . VAL   A 1 1   ? 199.554 142.631 107.291 1.00 128.40 ? 14   VAL   A H2   1 
ATOM   10   H H3   . VAL   A 1 1   ? 201.191 142.536 107.358 1.00 127.88 ? 14   VAL   A H3   1 
ATOM   11   H HA   . VAL   A 1 1   ? 201.331 144.990 107.315 1.00 128.34 ? 14   VAL   A HA   1 
ATOM   12   H HB   . VAL   A 1 1   ? 200.673 145.330 104.985 1.00 128.19 ? 14   VAL   A HB   1 
ATOM   13   H HG11 . VAL   A 1 1   ? 202.815 144.258 105.507 1.00 126.96 ? 14   VAL   A HG11 1 
ATOM   14   H HG12 . VAL   A 1 1   ? 202.057 142.645 105.380 1.00 127.50 ? 14   VAL   A HG12 1 
ATOM   15   H HG13 . VAL   A 1 1   ? 202.148 143.707 103.973 1.00 128.73 ? 14   VAL   A HG13 1 
ATOM   16   H HG21 . VAL   A 1 1   ? 198.584 143.972 104.873 1.00 128.88 ? 14   VAL   A HG21 1 
ATOM   17   H HG22 . VAL   A 1 1   ? 199.738 143.570 103.611 1.00 129.05 ? 14   VAL   A HG22 1 
ATOM   18   H HG23 . VAL   A 1 1   ? 199.561 142.483 104.990 1.00 128.81 ? 14   VAL   A HG23 1 
ATOM   19   N N    . ILE   A 1 2   ? 199.299 146.594 107.177 1.00 125.18 ? 15   ILE   A N    1 
ATOM   20   C CA   . ILE   A 1 2   ? 198.121 147.457 107.382 1.00 122.29 ? 15   ILE   A CA   1 
ATOM   21   C C    . ILE   A 1 2   ? 197.357 147.649 106.069 1.00 129.77 ? 15   ILE   A C    1 
ATOM   22   O O    . ILE   A 1 2   ? 196.369 146.958 105.837 1.00 131.38 ? 15   ILE   A O    1 
ATOM   23   C CB   . ILE   A 1 2   ? 198.484 148.779 108.080 1.00 124.35 ? 15   ILE   A CB   1 
ATOM   24   C CG1  . ILE   A 1 2   ? 199.245 148.543 109.396 1.00 132.59 ? 15   ILE   A CG1  1 
ATOM   25   C CG2  . ILE   A 1 2   ? 197.228 149.624 108.335 1.00 122.88 ? 15   ILE   A CG2  1 
ATOM   26   C CD1  . ILE   A 1 2   ? 198.508 147.705 110.445 1.00 134.47 ? 15   ILE   A CD1  1 
ATOM   27   H H    . ILE   A 1 2   ? 200.177 147.034 106.940 1.00 128.88 ? 15   ILE   A H    1 
ATOM   28   H HA   . ILE   A 1 2   ? 197.424 146.943 108.044 1.00 127.70 ? 15   ILE   A HA   1 
ATOM   29   H HB   . ILE   A 1 2   ? 199.143 149.349 107.425 1.00 128.60 ? 15   ILE   A HB   1 
ATOM   30   H HG12 . ILE   A 1 2   ? 200.191 148.053 109.166 1.00 129.83 ? 15   ILE   A HG12 1 
ATOM   31   H HG13 . ILE   A 1 2   ? 199.482 149.511 109.838 1.00 129.17 ? 15   ILE   A HG13 1 
ATOM   32   H HG21 . ILE   A 1 2   ? 196.791 149.956 107.393 1.00 128.47 ? 15   ILE   A HG21 1 
ATOM   33   H HG22 . ILE   A 1 2   ? 197.485 150.509 108.917 1.00 128.16 ? 15   ILE   A HG22 1 
ATOM   34   H HG23 . ILE   A 1 2   ? 196.481 149.047 108.881 1.00 127.60 ? 15   ILE   A HG23 1 
ATOM   35   H HD11 . ILE   A 1 2   ? 199.141 147.597 111.326 1.00 129.32 ? 15   ILE   A HD11 1 
ATOM   36   H HD12 . ILE   A 1 2   ? 197.585 148.204 110.742 1.00 129.69 ? 15   ILE   A HD12 1 
ATOM   37   H HD13 . ILE   A 1 2   ? 198.283 146.711 110.059 1.00 129.28 ? 15   ILE   A HD13 1 
ATOM   38   N N    . GLY   A 1 3   ? 197.822 148.537 105.188 1.00 144.84 ? 16   GLY   A N    1 
ATOM   39   C CA   . GLY   A 1 3   ? 197.363 148.597 103.799 1.00 141.76 ? 16   GLY   A CA   1 
ATOM   40   C C    . GLY   A 1 3   ? 198.081 147.558 102.940 1.00 141.60 ? 16   GLY   A C    1 
ATOM   41   O O    . GLY   A 1 3   ? 198.659 146.608 103.465 1.00 145.17 ? 16   GLY   A O    1 
ATOM   42   H H    . GLY   A 1 3   ? 198.665 149.049 105.409 1.00 141.81 ? 16   GLY   A H    1 
ATOM   43   H HA2  . GLY   A 1 3   ? 196.289 148.425 103.739 1.00 141.59 ? 16   GLY   A HA2  1 
ATOM   44   H HA3  . GLY   A 1 3   ? 197.572 149.588 103.396 1.00 141.49 ? 16   GLY   A HA3  1 
ATOM   45   N N    . ASP   A 1 4   ? 198.097 147.740 101.621 1.00 143.61 ? 17   ASP   A N    1 
ATOM   46   C CA   . ASP   A 1 4   ? 198.820 146.838 100.714 1.00 145.17 ? 17   ASP   A CA   1 
ATOM   47   C C    . ASP   A 1 4   ? 199.744 147.545 99.711  1.00 145.09 ? 17   ASP   A C    1 
ATOM   48   O O    . ASP   A 1 4   ? 200.384 146.879 98.897  1.00 144.57 ? 17   ASP   A O    1 
ATOM   49   C CB   . ASP   A 1 4   ? 197.847 145.870 100.032 1.00 147.33 ? 17   ASP   A CB   1 
ATOM   50   C CG   . ASP   A 1 4   ? 196.988 146.490 98.926  1.00 151.51 ? 17   ASP   A CG   1 
ATOM   51   O OD1  . ASP   A 1 4   ? 197.052 147.718 98.697  1.00 153.58 ? 17   ASP   A OD1  1 
ATOM   52   O OD2  . ASP   A 1 4   ? 196.249 145.725 98.267  1.00 150.70 ? 17   ASP   A OD2  1 
ATOM   53   H H    . ASP   A 1 4   ? 197.566 148.499 101.219 1.00 145.85 ? 17   ASP   A H    1 
ATOM   54   H HA   . ASP   A 1 4   ? 199.489 146.215 101.307 1.00 146.05 ? 17   ASP   A HA   1 
ATOM   55   H HB2  . ASP   A 1 4   ? 198.429 145.055 99.601  1.00 146.77 ? 17   ASP   A HB2  1 
ATOM   56   H HB3  . ASP   A 1 4   ? 197.196 145.434 100.790 1.00 146.07 ? 17   ASP   A HB3  1 
ATOM   57   N N    . PHE   A 1 5   ? 199.868 148.873 99.758  1.00 145.31 ? 18   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 5   ? 200.813 149.574 98.899  1.00 142.93 ? 18   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 5   ? 202.252 149.409 99.398  1.00 149.42 ? 18   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 5   ? 202.571 149.735 100.545 1.00 155.86 ? 18   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 5   ? 200.423 151.044 98.767  1.00 141.13 ? 18   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 5   ? 201.142 151.698 97.611  1.00 140.08 ? 18   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 5   ? 202.462 152.148 97.763  1.00 142.44 ? 18   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 5   ? 200.522 151.770 96.354  1.00 142.53 ? 18   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 5   ? 203.169 152.652 96.661  1.00 142.07 ? 18   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 5   ? 201.221 152.290 95.252  1.00 146.42 ? 18   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 5   ? 202.550 152.717 95.403  1.00 146.02 ? 18   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 5   ? 199.345 149.401 100.443 1.00 145.71 ? 18   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 5   ? 200.750 149.139 97.902  1.00 144.60 ? 18   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 5   ? 199.348 151.108 98.594  1.00 144.67 ? 18   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 5   ? 200.649 151.577 99.690  1.00 145.37 ? 18   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 5   ? 202.945 152.091 98.727  1.00 145.65 ? 18   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 5   ? 199.507 151.421 96.233  1.00 144.99 ? 18   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 5   ? 204.188 152.990 96.781  1.00 144.51 ? 18   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 5   ? 200.738 152.360 94.289  1.00 145.52 ? 18   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 5   ? 203.091 153.113 94.556  1.00 145.27 ? 18   PHE   A HZ   1 
ATOM   77   N N    . ASN   A 1 6   ? 203.144 148.939 98.531  1.00 157.93 ? 19   ASN   A N    1 
ATOM   78   C CA   . ASN   A 1 6   ? 204.566 148.795 98.824  1.00 159.64 ? 19   ASN   A CA   1 
ATOM   79   C C    . ASN   A 1 6   ? 205.294 150.155 98.791  1.00 162.39 ? 19   ASN   A C    1 
ATOM   80   O O    . ASN   A 1 6   ? 205.880 150.535 97.779  1.00 157.73 ? 19   ASN   A O    1 
ATOM   81   C CB   . ASN   A 1 6   ? 205.148 147.786 97.824  1.00 156.29 ? 19   ASN   A CB   1 
ATOM   82   C CG   . ASN   A 1 6   ? 206.635 147.558 98.028  1.00 162.10 ? 19   ASN   A CG   1 
ATOM   83   O OD1  . ASN   A 1 6   ? 207.196 147.900 99.063  1.00 166.00 ? 19   ASN   A OD1  1 
ATOM   84   N ND2  . ASN   A 1 6   ? 207.276 147.005 97.011  1.00 164.23 ? 19   ASN   A ND2  1 
ATOM   85   H H    . ASN   A 1 6   ? 202.824 148.681 97.609  1.00 158.88 ? 19   ASN   A H    1 
ATOM   86   H HA   . ASN   A 1 6   ? 204.680 148.380 99.825  1.00 159.98 ? 19   ASN   A HA   1 
ATOM   87   H HB2  . ASN   A 1 6   ? 204.639 146.829 97.934  1.00 159.44 ? 19   ASN   A HB2  1 
ATOM   88   H HB3  . ASN   A 1 6   ? 204.986 148.151 96.809  1.00 159.08 ? 19   ASN   A HB3  1 
ATOM   89   H HD21 . ASN   A 1 6   ? 206.730 146.692 96.221  1.00 160.31 ? 19   ASN   A HD21 1 
ATOM   90   N N    . CYS   A 1 7   ? 205.190 150.935 99.869  1.00 174.77 ? 20   CYS   A N    1 
ATOM   91   C CA   . CYS   A 1 7   ? 205.797 152.267 99.967  1.00 170.68 ? 20   CYS   A CA   1 
ATOM   92   C C    . CYS   A 1 7   ? 207.334 152.236 99.980  1.00 167.77 ? 20   CYS   A C    1 
ATOM   93   O O    . CYS   A 1 7   ? 207.970 153.124 99.413  1.00 164.47 ? 20   CYS   A O    1 
ATOM   94   C CB   . CYS   A 1 7   ? 205.261 152.963 101.226 1.00 172.17 ? 20   CYS   A CB   1 
ATOM   95   S SG   . CYS   A 1 7   ? 203.493 153.338 101.133 1.00 188.52 ? 20   CYS   A SG   1 
ATOM   96   H H    . CYS   A 1 7   ? 204.588 150.624 100.618 1.00 170.92 ? 20   CYS   A H    1 
ATOM   97   H HA   . CYS   A 1 7   ? 205.493 152.857 99.102  1.00 170.15 ? 20   CYS   A HA   1 
ATOM   98   H HB2  . CYS   A 1 7   ? 205.450 152.333 102.095 1.00 170.75 ? 20   CYS   A HB2  1 
ATOM   99   H HB3  . CYS   A 1 7   ? 205.798 153.902 101.367 1.00 171.13 ? 20   CYS   A HB3  1 
ATOM   100  N N    . THR   A 1 8   ? 207.947 151.238 100.622 1.00 166.67 ? 21   THR   A N    1 
ATOM   101  C CA   . THR   A 1 8   ? 209.407 151.043 100.656 1.00 169.79 ? 21   THR   A CA   1 
ATOM   102  C C    . THR   A 1 8   ? 209.783 149.632 101.118 1.00 168.35 ? 21   THR   A C    1 
ATOM   103  O O    . THR   A 1 8   ? 208.997 148.970 101.793 1.00 166.09 ? 21   THR   A O    1 
ATOM   104  C CB   . THR   A 1 8   ? 210.069 152.081 101.583 1.00 170.86 ? 21   THR   A CB   1 
ATOM   105  O OG1  . THR   A 1 8   ? 211.473 152.011 101.461 1.00 174.50 ? 21   THR   A OG1  1 
ATOM   106  C CG2  . THR   A 1 8   ? 209.750 151.887 103.065 1.00 167.39 ? 21   THR   A CG2  1 
ATOM   107  H H    . THR   A 1 8   ? 207.378 150.527 101.059 1.00 168.15 ? 21   THR   A H    1 
ATOM   108  H HA   . THR   A 1 8   ? 209.800 151.184 99.649  1.00 168.49 ? 21   THR   A HA   1 
ATOM   109  H HB   . THR   A 1 8   ? 209.750 153.082 101.292 1.00 168.43 ? 21   THR   A HB   1 
ATOM   110  H HG1  . THR   A 1 8   ? 211.725 152.620 100.762 1.00 168.83 ? 21   THR   A HG1  1 
ATOM   111  H HG21 . THR   A 1 8   ? 210.176 152.716 103.630 1.00 168.26 ? 21   THR   A HG21 1 
ATOM   112  H HG22 . THR   A 1 8   ? 210.172 150.952 103.434 1.00 168.08 ? 21   THR   A HG22 1 
ATOM   113  H HG23 . THR   A 1 8   ? 208.671 151.884 103.215 1.00 168.05 ? 21   THR   A HG23 1 
ATOM   114  N N    . ASN   A 1 9   ? 211.017 149.203 100.845 1.00 169.26 ? 22   ASN   A N    1 
ATOM   115  C CA   . ASN   A 1 9   ? 211.647 148.040 101.475 1.00 170.85 ? 22   ASN   A CA   1 
ATOM   116  C C    . ASN   A 1 9   ? 212.882 148.407 102.329 1.00 173.71 ? 22   ASN   A C    1 
ATOM   117  O O    . ASN   A 1 9   ? 213.625 147.517 102.746 1.00 175.70 ? 22   ASN   A O    1 
ATOM   118  C CB   . ASN   A 1 9   ? 211.959 146.981 100.404 1.00 171.82 ? 22   ASN   A CB   1 
ATOM   119  C CG   . ASN   A 1 9   ? 213.144 147.342 99.525  1.00 173.25 ? 22   ASN   A CG   1 
ATOM   120  O OD1  . ASN   A 1 9   ? 213.436 148.500 99.266  1.00 169.88 ? 22   ASN   A OD1  1 
ATOM   121  N ND2  . ASN   A 1 9   ? 213.876 146.360 99.058  1.00 174.97 ? 22   ASN   A ND2  1 
ATOM   122  H H    . ASN   A 1 9   ? 211.602 149.778 100.256 1.00 171.35 ? 22   ASN   A H    1 
ATOM   123  H HA   . ASN   A 1 9   ? 210.936 147.591 102.169 1.00 171.72 ? 22   ASN   A HA   1 
ATOM   124  H HB2  . ASN   A 1 9   ? 212.180 146.042 100.911 1.00 172.05 ? 22   ASN   A HB2  1 
ATOM   125  H HB3  . ASN   A 1 9   ? 211.084 146.815 99.775  1.00 171.57 ? 22   ASN   A HB3  1 
ATOM   126  H HD21 . ASN   A 1 9   ? 213.653 145.402 99.287  1.00 172.03 ? 22   ASN   A HD21 1 
ATOM   127  H HD22 . ASN   A 1 9   ? 214.677 146.589 98.487  1.00 172.12 ? 22   ASN   A HD22 1 
ATOM   128  N N    . PHE   A 1 10  ? 213.137 149.693 102.591 1.00 158.92 ? 23   PHE   A N    1 
ATOM   129  C CA   . PHE   A 1 10  ? 214.295 150.133 103.373 1.00 157.36 ? 23   PHE   A CA   1 
ATOM   130  C C    . PHE   A 1 10  ? 214.219 149.688 104.841 1.00 158.53 ? 23   PHE   A C    1 
ATOM   131  O O    . PHE   A 1 10  ? 213.260 150.014 105.542 1.00 157.15 ? 23   PHE   A O    1 
ATOM   132  C CB   . PHE   A 1 10  ? 214.415 151.656 103.281 1.00 155.19 ? 23   PHE   A CB   1 
ATOM   133  C CG   . PHE   A 1 10  ? 215.510 152.233 104.154 1.00 157.37 ? 23   PHE   A CG   1 
ATOM   134  C CD1  . PHE   A 1 10  ? 216.858 152.036 103.809 1.00 155.14 ? 23   PHE   A CD1  1 
ATOM   135  C CD2  . PHE   A 1 10  ? 215.186 152.947 105.321 1.00 156.70 ? 23   PHE   A CD2  1 
ATOM   136  C CE1  . PHE   A 1 10  ? 217.877 152.554 104.626 1.00 153.23 ? 23   PHE   A CE1  1 
ATOM   137  C CE2  . PHE   A 1 10  ? 216.205 153.467 106.136 1.00 155.29 ? 23   PHE   A CE2  1 
ATOM   138  C CZ   . PHE   A 1 10  ? 217.551 153.271 105.788 1.00 155.39 ? 23   PHE   A CZ   1 
ATOM   139  H H    . PHE   A 1 10  ? 212.507 150.400 102.241 1.00 157.34 ? 23   PHE   A H    1 
ATOM   140  H HA   . PHE   A 1 10  ? 215.195 149.702 102.935 1.00 156.58 ? 23   PHE   A HA   1 
ATOM   141  H HB2  . PHE   A 1 10  ? 214.613 151.933 102.245 1.00 156.11 ? 23   PHE   A HB2  1 
ATOM   142  H HB3  . PHE   A 1 10  ? 213.464 152.106 103.566 1.00 156.43 ? 23   PHE   A HB3  1 
ATOM   143  H HD1  . PHE   A 1 10  ? 217.113 151.488 102.914 1.00 156.09 ? 23   PHE   A HD1  1 
ATOM   144  H HD2  . PHE   A 1 10  ? 214.151 153.102 105.591 1.00 156.23 ? 23   PHE   A HD2  1 
ATOM   145  H HE1  . PHE   A 1 10  ? 218.912 152.402 104.359 1.00 155.73 ? 23   PHE   A HE1  1 
ATOM   146  H HE2  . PHE   A 1 10  ? 215.957 154.019 107.030 1.00 156.22 ? 23   PHE   A HE2  1 
ATOM   147  H HZ   . PHE   A 1 10  ? 218.334 153.670 106.415 1.00 156.57 ? 23   PHE   A HZ   1 
ATOM   148  N N    . ALA   A 1 11  ? 215.252 148.988 105.317 1.00 157.21 ? 24   ALA   A N    1 
ATOM   149  C CA   . ALA   A 1 11  ? 215.440 148.585 106.714 1.00 157.01 ? 24   ALA   A CA   1 
ATOM   150  C C    . ALA   A 1 11  ? 214.191 147.939 107.353 1.00 160.33 ? 24   ALA   A C    1 
ATOM   151  O O    . ALA   A 1 11  ? 213.685 148.392 108.379 1.00 163.83 ? 24   ALA   A O    1 
ATOM   152  C CB   . ALA   A 1 11  ? 216.035 149.766 107.493 1.00 156.63 ? 24   ALA   A CB   1 
ATOM   153  H H    . ALA   A 1 11  ? 215.998 148.764 104.673 1.00 157.28 ? 24   ALA   A H    1 
ATOM   154  H HA   . ALA   A 1 11  ? 216.199 147.803 106.717 1.00 157.29 ? 24   ALA   A HA   1 
ATOM   155  H HB1  . ALA   A 1 11  ? 216.224 149.476 108.527 1.00 157.53 ? 24   ALA   A HB1  1 
ATOM   156  H HB2  . ALA   A 1 11  ? 215.355 150.618 107.474 1.00 157.70 ? 24   ALA   A HB2  1 
ATOM   157  H HB3  . ALA   A 1 11  ? 216.979 150.066 107.038 1.00 157.34 ? 24   ALA   A HB3  1 
ATOM   158  N N    . ILE   A 1 12  ? 213.687 146.867 106.745 1.00 150.85 ? 25   ILE   A N    1 
ATOM   159  C CA   . ILE   A 1 12  ? 212.605 146.037 107.291 1.00 150.42 ? 25   ILE   A CA   1 
ATOM   160  C C    . ILE   A 1 12  ? 213.189 144.713 107.787 1.00 150.32 ? 25   ILE   A C    1 
ATOM   161  O O    . ILE   A 1 12  ? 213.993 144.101 107.083 1.00 151.60 ? 25   ILE   A O    1 
ATOM   162  C CB   . ILE   A 1 12  ? 211.514 145.795 106.231 1.00 147.42 ? 25   ILE   A CB   1 
ATOM   163  C CG1  . ILE   A 1 12  ? 210.970 147.087 105.589 1.00 149.19 ? 25   ILE   A CG1  1 
ATOM   164  C CG2  . ILE   A 1 12  ? 210.363 144.976 106.830 1.00 145.22 ? 25   ILE   A CG2  1 
ATOM   165  C CD1  . ILE   A 1 12  ? 210.331 148.080 106.562 1.00 148.25 ? 25   ILE   A CD1  1 
ATOM   166  H H    . ILE   A 1 12  ? 214.137 146.548 105.899 1.00 149.28 ? 25   ILE   A H    1 
ATOM   167  H HA   . ILE   A 1 12  ? 212.144 146.541 108.140 1.00 149.68 ? 25   ILE   A HA   1 
ATOM   168  H HB   . ILE   A 1 12  ? 211.950 145.204 105.426 1.00 149.22 ? 25   ILE   A HB   1 
ATOM   169  H HG12 . ILE   A 1 12  ? 211.778 147.593 105.062 1.00 149.92 ? 25   ILE   A HG12 1 
ATOM   170  H HG13 . ILE   A 1 12  ? 210.224 146.816 104.842 1.00 149.72 ? 25   ILE   A HG13 1 
ATOM   171  H HG21 . ILE   A 1 12  ? 210.703 143.967 107.062 1.00 148.87 ? 25   ILE   A HG21 1 
ATOM   172  H HG22 . ILE   A 1 12  ? 209.989 145.446 107.739 1.00 149.02 ? 25   ILE   A HG22 1 
ATOM   173  H HG23 . ILE   A 1 12  ? 209.550 144.896 106.108 1.00 148.51 ? 25   ILE   A HG23 1 
ATOM   174  H HD11 . ILE   A 1 12  ? 209.981 148.949 106.005 1.00 149.15 ? 25   ILE   A HD11 1 
ATOM   175  H HD12 . ILE   A 1 12  ? 211.065 148.409 107.298 1.00 149.29 ? 25   ILE   A HD12 1 
ATOM   176  H HD13 . ILE   A 1 12  ? 209.479 147.625 107.067 1.00 149.21 ? 25   ILE   A HD13 1 
ATOM   177  N N    . ASN   A 1 13  ? 212.804 144.249 108.976 1.00 147.06 ? 26   ASN   A N    1 
ATOM   178  C CA   . ASN   A 1 13  ? 213.193 142.929 109.487 1.00 145.97 ? 26   ASN   A CA   1 
ATOM   179  C C    . ASN   A 1 13  ? 212.068 142.278 110.308 1.00 147.98 ? 26   ASN   A C    1 
ATOM   180  O O    . ASN   A 1 13  ? 211.007 142.862 110.485 1.00 147.26 ? 26   ASN   A O    1 
ATOM   181  C CB   . ASN   A 1 13  ? 214.547 143.013 110.221 1.00 147.64 ? 26   ASN   A CB   1 
ATOM   182  C CG   . ASN   A 1 13  ? 214.506 143.706 111.567 1.00 151.82 ? 26   ASN   A CG   1 
ATOM   183  O OD1  . ASN   A 1 13  ? 213.623 143.480 112.376 1.00 151.81 ? 26   ASN   A OD1  1 
ATOM   184  N ND2  . ASN   A 1 13  ? 215.491 144.519 111.867 1.00 154.64 ? 26   ASN   A ND2  1 
ATOM   185  H H    . ASN   A 1 13  ? 212.119 144.773 109.503 1.00 149.19 ? 26   ASN   A H    1 
ATOM   186  H HA   . ASN   A 1 13  ? 213.341 142.269 108.632 1.00 149.08 ? 26   ASN   A HA   1 
ATOM   187  H HB2  . ASN   A 1 13  ? 214.930 142.006 110.386 1.00 149.35 ? 26   ASN   A HB2  1 
ATOM   188  H HB3  . ASN   A 1 13  ? 215.263 143.522 109.577 1.00 149.22 ? 26   ASN   A HB3  1 
ATOM   189  H HD21 . ASN   A 1 13  ? 216.239 144.683 111.207 1.00 149.70 ? 26   ASN   A HD21 1 
ATOM   190  H HD22 . ASN   A 1 13  ? 215.522 144.934 112.787 1.00 150.72 ? 26   ASN   A HD22 1 
ATOM   191  N N    . ASP   A 1 14  ? 212.272 141.046 110.770 1.00 157.74 ? 27   ASP   A N    1 
ATOM   192  C CA   . ASP   A 1 14  ? 211.241 140.245 111.445 1.00 158.01 ? 27   ASP   A CA   1 
ATOM   193  C C    . ASP   A 1 14  ? 211.476 140.068 112.959 1.00 156.16 ? 27   ASP   A C    1 
ATOM   194  O O    . ASP   A 1 14  ? 210.935 139.142 113.561 1.00 155.95 ? 27   ASP   A O    1 
ATOM   195  C CB   . ASP   A 1 14  ? 211.102 138.894 110.723 1.00 159.05 ? 27   ASP   A CB   1 
ATOM   196  C CG   . ASP   A 1 14  ? 210.745 139.015 109.239 1.00 160.76 ? 27   ASP   A CG   1 
ATOM   197  O OD1  . ASP   A 1 14  ? 210.013 139.957 108.863 1.00 160.45 ? 27   ASP   A OD1  1 
ATOM   198  O OD2  . ASP   A 1 14  ? 211.165 138.132 108.457 1.00 161.49 ? 27   ASP   A OD2  1 
ATOM   199  H H    . ASP   A 1 14  ? 213.162 140.606 110.586 1.00 156.93 ? 27   ASP   A H    1 
ATOM   200  H HA   . ASP   A 1 14  ? 210.280 140.752 111.357 1.00 157.21 ? 27   ASP   A HA   1 
ATOM   201  H HB2  . ASP   A 1 14  ? 212.038 138.344 110.831 1.00 157.40 ? 27   ASP   A HB2  1 
ATOM   202  H HB3  . ASP   A 1 14  ? 210.315 138.314 111.206 1.00 157.35 ? 27   ASP   A HB3  1 
ATOM   203  N N    . LEU   A 1 15  ? 212.308 140.897 113.598 1.00 157.82 ? 28   LEU   A N    1 
ATOM   204  C CA   . LEU   A 1 15  ? 212.676 140.705 115.008 1.00 158.32 ? 28   LEU   A CA   1 
ATOM   205  C C    . LEU   A 1 15  ? 211.488 140.903 115.956 1.00 159.41 ? 28   LEU   A C    1 
ATOM   206  O O    . LEU   A 1 15  ? 210.774 141.905 115.887 1.00 160.59 ? 28   LEU   A O    1 
ATOM   207  C CB   . LEU   A 1 15  ? 213.830 141.641 115.402 1.00 157.60 ? 28   LEU   A CB   1 
ATOM   208  C CG   . LEU   A 1 15  ? 215.223 141.032 115.175 1.00 158.91 ? 28   LEU   A CG   1 
ATOM   209  C CD1  . LEU   A 1 15  ? 215.507 140.646 113.725 1.00 157.17 ? 28   LEU   A CD1  1 
ATOM   210  C CD2  . LEU   A 1 15  ? 216.288 142.031 115.619 1.00 158.31 ? 28   LEU   A CD2  1 
ATOM   211  H H    . LEU   A 1 15  ? 212.716 141.669 113.091 1.00 157.36 ? 28   LEU   A H    1 
ATOM   212  H HA   . LEU   A 1 15  ? 213.018 139.678 115.134 1.00 157.45 ? 28   LEU   A HA   1 
ATOM   213  H HB2  . LEU   A 1 15  ? 213.742 142.588 114.869 1.00 157.65 ? 28   LEU   A HB2  1 
ATOM   214  H HB3  . LEU   A 1 15  ? 213.749 141.860 116.467 1.00 157.00 ? 28   LEU   A HB3  1 
ATOM   215  H HG   . LEU   A 1 15  ? 215.316 140.137 115.791 1.00 157.68 ? 28   LEU   A HG   1 
ATOM   216  H HD11 . LEU   A 1 15  ? 214.823 139.861 113.406 1.00 157.36 ? 28   LEU   A HD11 1 
ATOM   217  H HD12 . LEU   A 1 15  ? 215.397 141.518 113.080 1.00 157.30 ? 28   LEU   A HD12 1 
ATOM   218  H HD13 . LEU   A 1 15  ? 216.525 140.266 113.642 1.00 157.48 ? 28   LEU   A HD13 1 
ATOM   219  H HD21 . LEU   A 1 15  ? 216.136 142.289 116.667 1.00 157.72 ? 28   LEU   A HD21 1 
ATOM   220  H HD22 . LEU   A 1 15  ? 217.277 141.588 115.509 1.00 157.47 ? 28   LEU   A HD22 1 
ATOM   221  H HD23 . LEU   A 1 15  ? 216.229 142.935 115.012 1.00 157.73 ? 28   LEU   A HD23 1 
ATOM   222  N N    . ASN   A 1 16  ? 211.317 139.971 116.894 1.00 167.51 ? 29   ASN   A N    1 
ATOM   223  C CA   . ASN   A 1 16  ? 210.339 140.065 117.974 1.00 169.18 ? 29   ASN   A CA   1 
ATOM   224  C C    . ASN   A 1 16  ? 210.891 140.927 119.121 1.00 167.46 ? 29   ASN   A C    1 
ATOM   225  O O    . ASN   A 1 16  ? 211.457 140.416 120.088 1.00 165.55 ? 29   ASN   A O    1 
ATOM   226  C CB   . ASN   A 1 16  ? 209.951 138.646 118.424 1.00 167.97 ? 29   ASN   A CB   1 
ATOM   227  C CG   . ASN   A 1 16  ? 208.837 138.660 119.454 1.00 170.51 ? 29   ASN   A CG   1 
ATOM   228  O OD1  . ASN   A 1 16  ? 208.216 139.678 119.727 1.00 169.07 ? 29   ASN   A OD1  1 
ATOM   229  N ND2  . ASN   A 1 16  ? 208.540 137.531 120.052 1.00 169.72 ? 29   ASN   A ND2  1 
ATOM   230  H H    . ASN   A 1 16  ? 211.937 139.173 116.891 1.00 166.65 ? 29   ASN   A H    1 
ATOM   231  H HA   . ASN   A 1 16  ? 209.440 140.554 117.600 1.00 167.61 ? 29   ASN   A HA   1 
ATOM   232  H HB2  . ASN   A 1 16  ? 209.606 138.072 117.564 1.00 167.06 ? 29   ASN   A HB2  1 
ATOM   233  H HB3  . ASN   A 1 16  ? 210.818 138.140 118.848 1.00 166.92 ? 29   ASN   A HB3  1 
ATOM   234  H HD21 . ASN   A 1 16  ? 209.047 136.687 119.828 1.00 167.29 ? 29   ASN   A HD21 1 
ATOM   235  H HD22 . ASN   A 1 16  ? 207.801 137.535 120.741 1.00 167.49 ? 29   ASN   A HD22 1 
ATOM   236  N N    . THR   A 1 17  ? 210.759 142.248 119.007 1.00 172.19 ? 30   THR   A N    1 
ATOM   237  C CA   . THR   A 1 17  ? 211.273 143.191 120.019 1.00 173.02 ? 30   THR   A CA   1 
ATOM   238  C C    . THR   A 1 17  ? 210.504 143.115 121.339 1.00 174.51 ? 30   THR   A C    1 
ATOM   239  O O    . THR   A 1 17  ? 211.067 143.380 122.401 1.00 173.04 ? 30   THR   A O    1 
ATOM   240  C CB   . THR   A 1 17  ? 211.248 144.638 119.506 1.00 175.07 ? 30   THR   A CB   1 
ATOM   241  O OG1  . THR   A 1 17  ? 209.933 145.128 119.335 1.00 176.21 ? 30   THR   A OG1  1 
ATOM   242  C CG2  . THR   A 1 17  ? 211.949 144.777 118.159 1.00 173.11 ? 30   THR   A CG2  1 
ATOM   243  H H    . THR   A 1 17  ? 210.335 142.623 118.170 1.00 171.70 ? 30   THR   A H    1 
ATOM   244  H HA   . THR   A 1 17  ? 212.311 142.938 120.234 1.00 171.59 ? 30   THR   A HA   1 
ATOM   245  H HB   . THR   A 1 17  ? 211.766 145.268 120.229 1.00 172.12 ? 30   THR   A HB   1 
ATOM   246  H HG1  . THR   A 1 17  ? 209.654 145.491 120.179 1.00 172.16 ? 30   THR   A HG1  1 
ATOM   247  H HG21 . THR   A 1 17  ? 211.960 145.831 117.881 1.00 172.24 ? 30   THR   A HG21 1 
ATOM   248  H HG22 . THR   A 1 17  ? 211.419 144.221 117.386 1.00 171.69 ? 30   THR   A HG22 1 
ATOM   249  H HG23 . THR   A 1 17  ? 212.971 144.407 118.240 1.00 171.59 ? 30   THR   A HG23 1 
ATOM   250  N N    . GLY   A 1 18  ? 209.228 142.726 121.291 1.00 194.96 ? 31   GLY   A N    1 
ATOM   251  C CA   . GLY   A 1 18  ? 208.355 142.533 122.450 1.00 195.69 ? 31   GLY   A CA   1 
ATOM   252  C C    . GLY   A 1 18  ? 208.612 141.211 123.179 1.00 197.78 ? 31   GLY   A C    1 
ATOM   253  O O    . GLY   A 1 18  ? 207.688 140.417 123.364 1.00 197.00 ? 31   GLY   A O    1 
ATOM   254  H H    . GLY   A 1 18  ? 208.843 142.510 120.382 1.00 192.76 ? 31   GLY   A H    1 
ATOM   255  H HA2  . GLY   A 1 18  ? 208.507 143.349 123.158 1.00 193.62 ? 31   GLY   A HA2  1 
ATOM   256  H HA3  . GLY   A 1 18  ? 207.314 142.554 122.127 1.00 193.54 ? 31   GLY   A HA3  1 
ATOM   257  N N    . GLY   A 1 19  ? 209.861 140.954 123.585 1.00 206.28 ? 32   GLY   A N    1 
ATOM   258  C CA   . GLY   A 1 19  ? 210.213 139.795 124.415 1.00 205.85 ? 32   GLY   A CA   1 
ATOM   259  C C    . GLY   A 1 19  ? 209.464 139.811 125.751 1.00 207.35 ? 32   GLY   A C    1 
ATOM   260  O O    . GLY   A 1 19  ? 208.894 138.801 126.168 1.00 207.51 ? 32   GLY   A O    1 
ATOM   261  H H    . GLY   A 1 19  ? 210.575 141.638 123.375 1.00 203.50 ? 32   GLY   A H    1 
ATOM   262  H HA2  . GLY   A 1 19  ? 209.973 138.873 123.885 1.00 203.90 ? 32   GLY   A HA2  1 
ATOM   263  H HA3  . GLY   A 1 19  ? 211.283 139.811 124.622 1.00 203.99 ? 32   GLY   A HA3  1 
ATOM   264  N N    . GLY   A 1 20  ? 209.377 140.990 126.371 1.00 197.21 ? 33   GLY   A N    1 
ATOM   265  C CA   . GLY   A 1 20  ? 208.258 141.337 127.247 1.00 193.76 ? 33   GLY   A CA   1 
ATOM   266  C C    . GLY   A 1 20  ? 207.105 141.838 126.375 1.00 193.38 ? 33   GLY   A C    1 
ATOM   267  O O    . GLY   A 1 20  ? 207.322 142.670 125.492 1.00 195.50 ? 33   GLY   A O    1 
ATOM   268  H H    . GLY   A 1 20  ? 209.897 141.758 125.972 1.00 193.81 ? 33   GLY   A H    1 
ATOM   269  H HA2  . GLY   A 1 20  ? 207.942 140.471 127.828 1.00 193.30 ? 33   GLY   A HA2  1 
ATOM   270  H HA3  . GLY   A 1 20  ? 208.553 142.129 127.936 1.00 193.31 ? 33   GLY   A HA3  1 
ATOM   271  N N    . GLY   A 1 21  ? 205.900 141.304 126.572 1.00 157.89 ? 34   GLY   A N    1 
ATOM   272  C CA   . GLY   A 1 21  ? 204.757 141.542 125.683 1.00 155.20 ? 34   GLY   A CA   1 
ATOM   273  C C    . GLY   A 1 21  ? 204.180 142.961 125.735 1.00 156.02 ? 34   GLY   A C    1 
ATOM   274  O O    . GLY   A 1 21  ? 204.777 143.882 126.296 1.00 159.35 ? 34   GLY   A O    1 
ATOM   275  H H    . GLY   A 1 21  ? 205.788 140.631 127.317 1.00 158.24 ? 34   GLY   A H    1 
ATOM   276  H HA2  . GLY   A 1 21  ? 205.051 141.334 124.655 1.00 157.79 ? 34   GLY   A HA2  1 
ATOM   277  H HA3  . GLY   A 1 21  ? 203.962 140.844 125.945 1.00 157.42 ? 34   GLY   A HA3  1 
ATOM   278  N N    . ILE   A 1 22  ? 202.984 143.145 125.172 1.00 139.58 ? 35   ILE   A N    1 
ATOM   279  C CA   . ILE   A 1 22  ? 202.237 144.410 125.253 1.00 141.92 ? 35   ILE   A CA   1 
ATOM   280  C C    . ILE   A 1 22  ? 202.104 144.821 126.719 1.00 140.64 ? 35   ILE   A C    1 
ATOM   281  O O    . ILE   A 1 22  ? 201.614 144.040 127.534 1.00 138.66 ? 35   ILE   A O    1 
ATOM   282  C CB   . ILE   A 1 22  ? 200.841 144.253 124.619 1.00 134.77 ? 35   ILE   A CB   1 
ATOM   283  C CG1  . ILE   A 1 22  ? 200.873 143.735 123.171 1.00 134.29 ? 35   ILE   A CG1  1 
ATOM   284  C CG2  . ILE   A 1 22  ? 200.065 145.572 124.685 1.00 134.79 ? 35   ILE   A CG2  1 
ATOM   285  C CD1  . ILE   A 1 22  ? 201.619 144.634 122.187 1.00 136.94 ? 35   ILE   A CD1  1 
ATOM   286  H H    . ILE   A 1 22  ? 202.534 142.352 124.737 1.00 136.73 ? 35   ILE   A H    1 
ATOM   287  H HA   . ILE   A 1 22  ? 202.787 145.185 124.719 1.00 137.19 ? 35   ILE   A HA   1 
ATOM   288  H HB   . ILE   A 1 22  ? 200.284 143.518 125.200 1.00 135.76 ? 35   ILE   A HB   1 
ATOM   289  H HG12 . ILE   A 1 22  ? 201.329 142.746 123.148 1.00 136.25 ? 35   ILE   A HG12 1 
ATOM   290  H HG13 . ILE   A 1 22  ? 199.848 143.619 122.818 1.00 135.80 ? 35   ILE   A HG13 1 
ATOM   291  H HG21 . ILE   A 1 22  ? 199.142 145.480 124.114 1.00 135.74 ? 35   ILE   A HG21 1 
ATOM   292  H HG22 . ILE   A 1 22  ? 200.662 146.386 124.272 1.00 135.91 ? 35   ILE   A HG22 1 
ATOM   293  H HG23 . ILE   A 1 22  ? 199.809 145.807 125.718 1.00 136.30 ? 35   ILE   A HG23 1 
ATOM   294  H HD11 . ILE   A 1 22  ? 201.589 144.169 121.202 1.00 136.37 ? 35   ILE   A HD11 1 
ATOM   295  H HD12 . ILE   A 1 22  ? 201.144 145.613 122.124 1.00 135.75 ? 35   ILE   A HD12 1 
ATOM   296  H HD13 . ILE   A 1 22  ? 202.660 144.747 122.489 1.00 136.68 ? 35   ILE   A HD13 1 
ATOM   297  N N    . SER   A 1 23  ? 202.561 146.018 127.076 1.00 129.83 ? 36   SER   A N    1 
ATOM   298  C CA   . SER   A 1 23  ? 202.489 146.488 128.459 1.00 128.68 ? 36   SER   A CA   1 
ATOM   299  C C    . SER   A 1 23  ? 201.041 146.773 128.865 1.00 136.95 ? 36   SER   A C    1 
ATOM   300  O O    . SER   A 1 23  ? 200.241 147.195 128.030 1.00 141.22 ? 36   SER   A O    1 
ATOM   301  C CB   . SER   A 1 23  ? 203.382 147.710 128.644 1.00 129.86 ? 36   SER   A CB   1 
ATOM   302  O OG   . SER   A 1 23  ? 203.522 147.986 130.020 1.00 136.53 ? 36   SER   A OG   1 
ATOM   303  H H    . SER   A 1 23  ? 202.967 146.619 126.372 1.00 132.45 ? 36   SER   A H    1 
ATOM   304  H HA   . SER   A 1 23  ? 202.873 145.701 129.108 1.00 132.13 ? 36   SER   A HA   1 
ATOM   305  H HB2  . SER   A 1 23  ? 204.365 147.504 128.222 1.00 131.50 ? 36   SER   A HB2  1 
ATOM   306  H HB3  . SER   A 1 23  ? 202.946 148.570 128.135 1.00 132.57 ? 36   SER   A HB3  1 
ATOM   307  H HG   . SER   A 1 23  ? 204.190 148.669 130.120 1.00 133.06 ? 36   SER   A HG   1 
ATOM   308  N N    . GLU   A 1 24  ? 200.687 146.555 130.132 1.00 136.81 ? 37   GLU   A N    1 
ATOM   309  C CA   . GLU   A 1 24  ? 199.314 146.683 130.632 1.00 132.36 ? 37   GLU   A CA   1 
ATOM   310  C C    . GLU   A 1 24  ? 199.203 147.527 131.904 1.00 133.13 ? 37   GLU   A C    1 
ATOM   311  O O    . GLU   A 1 24  ? 200.119 147.599 132.721 1.00 139.49 ? 37   GLU   A O    1 
ATOM   312  C CB   . GLU   A 1 24  ? 198.687 145.310 130.869 1.00 132.24 ? 37   GLU   A CB   1 
ATOM   313  C CG   . GLU   A 1 24  ? 198.412 144.577 129.559 1.00 137.25 ? 37   GLU   A CG   1 
ATOM   314  C CD   . GLU   A 1 24  ? 197.707 143.246 129.827 1.00 143.64 ? 37   GLU   A CD   1 
ATOM   315  O OE1  . GLU   A 1 24  ? 198.292 142.381 130.518 1.00 145.96 ? 37   GLU   A OE1  1 
ATOM   316  O OE2  . GLU   A 1 24  ? 196.556 143.062 129.370 1.00 145.32 ? 37   GLU   A OE2  1 
ATOM   317  H H    . GLU   A 1 24  ? 201.402 146.277 130.788 1.00 136.07 ? 37   GLU   A H    1 
ATOM   318  H HA   . GLU   A 1 24  ? 198.710 147.186 129.877 1.00 135.92 ? 37   GLU   A HA   1 
ATOM   319  H HB2  . GLU   A 1 24  ? 199.346 144.716 131.502 1.00 136.08 ? 37   GLU   A HB2  1 
ATOM   320  H HB3  . GLU   A 1 24  ? 197.736 145.441 131.387 1.00 135.31 ? 37   GLU   A HB3  1 
ATOM   321  H HG2  . GLU   A 1 24  ? 197.792 145.207 128.922 1.00 136.09 ? 37   GLU   A HG2  1 
ATOM   322  H HG3  . GLU   A 1 24  ? 199.352 144.390 129.041 1.00 136.51 ? 37   GLU   A HG3  1 
ATOM   323  N N    . TYR   A 1 25  ? 198.044 148.152 132.073 1.00 123.66 ? 38   TYR   A N    1 
ATOM   324  C CA   . TYR   A 1 25  ? 197.698 149.065 133.161 1.00 123.74 ? 38   TYR   A CA   1 
ATOM   325  C C    . TYR   A 1 25  ? 196.198 148.933 133.437 1.00 125.59 ? 38   TYR   A C    1 
ATOM   326  O O    . TYR   A 1 25  ? 195.460 148.574 132.526 1.00 131.04 ? 38   TYR   A O    1 
ATOM   327  C CB   . TYR   A 1 25  ? 198.101 150.475 132.711 1.00 126.60 ? 38   TYR   A CB   1 
ATOM   328  C CG   . TYR   A 1 25  ? 197.696 151.612 133.618 1.00 126.10 ? 38   TYR   A CG   1 
ATOM   329  C CD1  . TYR   A 1 25  ? 198.231 151.689 134.914 1.00 125.62 ? 38   TYR   A CD1  1 
ATOM   330  C CD2  . TYR   A 1 25  ? 196.824 152.611 133.153 1.00 124.80 ? 38   TYR   A CD2  1 
ATOM   331  C CE1  . TYR   A 1 25  ? 197.866 152.751 135.759 1.00 131.13 ? 38   TYR   A CE1  1 
ATOM   332  C CE2  . TYR   A 1 25  ? 196.448 153.670 133.996 1.00 127.43 ? 38   TYR   A CE2  1 
ATOM   333  C CZ   . TYR   A 1 25  ? 196.962 153.735 135.307 1.00 135.52 ? 38   TYR   A CZ   1 
ATOM   334  O OH   . TYR   A 1 25  ? 196.594 154.744 136.138 1.00 137.68 ? 38   TYR   A OH   1 
ATOM   335  H H    . TYR   A 1 25  ? 197.330 148.008 131.374 1.00 126.78 ? 38   TYR   A H    1 
ATOM   336  H HA   . TYR   A 1 25  ? 198.244 148.801 134.067 1.00 126.08 ? 38   TYR   A HA   1 
ATOM   337  H HB2  . TYR   A 1 25  ? 199.185 150.504 132.607 1.00 127.37 ? 38   TYR   A HB2  1 
ATOM   338  H HB3  . TYR   A 1 25  ? 197.680 150.657 131.722 1.00 126.99 ? 38   TYR   A HB3  1 
ATOM   339  H HD1  . TYR   A 1 25  ? 198.925 150.938 135.261 1.00 125.79 ? 38   TYR   A HD1  1 
ATOM   340  H HD2  . TYR   A 1 25  ? 196.446 152.570 132.142 1.00 126.37 ? 38   TYR   A HD2  1 
ATOM   341  H HE1  . TYR   A 1 25  ? 198.264 152.816 136.761 1.00 126.93 ? 38   TYR   A HE1  1 
ATOM   342  H HE2  . TYR   A 1 25  ? 195.763 154.427 133.644 1.00 126.29 ? 38   TYR   A HE2  1 
ATOM   343  H HH   . TYR   A 1 25  ? 195.858 155.245 135.780 1.00 127.61 ? 38   TYR   A HH   1 
ATOM   344  N N    . VAL   A 1 26  ? 195.704 149.184 134.647 1.00 114.76 ? 39   VAL   A N    1 
ATOM   345  C CA   . VAL   A 1 26  ? 194.313 148.837 135.005 1.00 110.74 ? 39   VAL   A CA   1 
ATOM   346  C C    . VAL   A 1 26  ? 193.405 150.058 134.968 1.00 113.82 ? 39   VAL   A C    1 
ATOM   347  O O    . VAL   A 1 26  ? 193.714 151.082 135.570 1.00 117.46 ? 39   VAL   A O    1 
ATOM   348  C CB   . VAL   A 1 26  ? 194.241 148.150 136.374 1.00 106.08 ? 39   VAL   A CB   1 
ATOM   349  C CG1  . VAL   A 1 26  ? 192.810 147.720 136.704 1.00 104.57 ? 39   VAL   A CG1  1 
ATOM   350  C CG2  . VAL   A 1 26  ? 195.116 146.895 136.395 1.00 108.13 ? 39   VAL   A CG2  1 
ATOM   351  H H    . VAL   A 1 26  ? 196.319 149.535 135.368 1.00 112.99 ? 39   VAL   A H    1 
ATOM   352  H HA   . VAL   A 1 26  ? 193.924 148.118 134.285 1.00 111.10 ? 39   VAL   A HA   1 
ATOM   353  H HB   . VAL   A 1 26  ? 194.592 148.834 137.147 1.00 111.50 ? 39   VAL   A HB   1 
ATOM   354  H HG11 . VAL   A 1 26  ? 192.167 148.593 136.817 1.00 110.05 ? 39   VAL   A HG11 1 
ATOM   355  H HG12 . VAL   A 1 26  ? 192.799 147.171 137.645 1.00 111.47 ? 39   VAL   A HG12 1 
ATOM   356  H HG13 . VAL   A 1 26  ? 192.421 147.079 135.913 1.00 111.06 ? 39   VAL   A HG13 1 
ATOM   357  H HG21 . VAL   A 1 26  ? 196.165 147.161 136.263 1.00 111.68 ? 39   VAL   A HG21 1 
ATOM   358  H HG22 . VAL   A 1 26  ? 194.813 146.216 135.598 1.00 110.47 ? 39   VAL   A HG22 1 
ATOM   359  H HG23 . VAL   A 1 26  ? 195.013 146.390 137.356 1.00 111.91 ? 39   VAL   A HG23 1 
ATOM   360  N N    . VAL   A 1 27  ? 192.270 149.958 134.279 1.00 113.78 ? 40   VAL   A N    1 
ATOM   361  C CA   . VAL   A 1 27  ? 191.285 151.039 134.173 1.00 110.92 ? 40   VAL   A CA   1 
ATOM   362  C C    . VAL   A 1 27  ? 190.672 151.321 135.539 1.00 121.09 ? 40   VAL   A C    1 
ATOM   363  O O    . VAL   A 1 27  ? 190.093 150.429 136.155 1.00 128.34 ? 40   VAL   A O    1 
ATOM   364  C CB   . VAL   A 1 27  ? 190.177 150.669 133.178 1.00 112.30 ? 40   VAL   A CB   1 
ATOM   365  C CG1  . VAL   A 1 27  ? 189.091 151.743 133.089 1.00 114.75 ? 40   VAL   A CG1  1 
ATOM   366  C CG2  . VAL   A 1 27  ? 190.722 150.483 131.764 1.00 115.57 ? 40   VAL   A CG2  1 
ATOM   367  H H    . VAL   A 1 27  ? 192.053 149.078 133.833 1.00 117.23 ? 40   VAL   A H    1 
ATOM   368  H HA   . VAL   A 1 27  ? 191.782 151.941 133.814 1.00 116.49 ? 40   VAL   A HA   1 
ATOM   369  H HB   . VAL   A 1 27  ? 189.714 149.734 133.494 1.00 117.83 ? 40   VAL   A HB   1 
ATOM   370  H HG11 . VAL   A 1 27  ? 188.589 151.862 134.049 1.00 117.03 ? 40   VAL   A HG11 1 
ATOM   371  H HG12 . VAL   A 1 27  ? 188.345 151.435 132.357 1.00 117.90 ? 40   VAL   A HG12 1 
ATOM   372  H HG13 . VAL   A 1 27  ? 189.525 152.695 132.786 1.00 117.64 ? 40   VAL   A HG13 1 
ATOM   373  H HG21 . VAL   A 1 27  ? 191.548 149.772 131.756 1.00 117.54 ? 40   VAL   A HG21 1 
ATOM   374  H HG22 . VAL   A 1 27  ? 191.071 151.436 131.368 1.00 117.91 ? 40   VAL   A HG22 1 
ATOM   375  H HG23 . VAL   A 1 27  ? 189.930 150.093 131.124 1.00 117.36 ? 40   VAL   A HG23 1 
ATOM   376  N N    . ASP   A 1 28  ? 190.733 152.570 135.988 1.00 123.48 ? 41   ASP   A N    1 
ATOM   377  C CA   . ASP   A 1 28  ? 190.126 153.025 137.237 1.00 120.78 ? 41   ASP   A CA   1 
ATOM   378  C C    . ASP   A 1 28  ? 189.407 154.350 137.003 1.00 123.38 ? 41   ASP   A C    1 
ATOM   379  O O    . ASP   A 1 28  ? 190.033 155.397 136.863 1.00 128.17 ? 41   ASP   A O    1 
ATOM   380  C CB   . ASP   A 1 28  ? 191.202 153.140 138.319 1.00 121.55 ? 41   ASP   A CB   1 
ATOM   381  C CG   . ASP   A 1 28  ? 190.674 153.681 139.653 1.00 127.38 ? 41   ASP   A CG   1 
ATOM   382  O OD1  . ASP   A 1 28  ? 189.467 153.999 139.774 1.00 131.68 ? 41   ASP   A OD1  1 
ATOM   383  O OD2  . ASP   A 1 28  ? 191.480 153.791 140.601 1.00 130.05 ? 41   ASP   A OD2  1 
ATOM   384  H H    . ASP   A 1 28  ? 191.246 153.252 135.448 1.00 123.59 ? 41   ASP   A H    1 
ATOM   385  H HA   . ASP   A 1 28  ? 189.391 152.297 137.581 1.00 123.33 ? 41   ASP   A HA   1 
ATOM   386  H HB2  . ASP   A 1 28  ? 191.633 152.152 138.486 1.00 123.28 ? 41   ASP   A HB2  1 
ATOM   387  H HB3  . ASP   A 1 28  ? 191.997 153.796 137.964 1.00 124.01 ? 41   ASP   A HB3  1 
ATOM   388  N N    . VAL   A 1 29  ? 188.081 154.299 136.943 1.00 112.04 ? 42   VAL   A N    1 
ATOM   389  C CA   . VAL   A 1 29  ? 187.240 155.453 136.626 1.00 106.67 ? 42   VAL   A CA   1 
ATOM   390  C C    . VAL   A 1 29  ? 186.872 156.288 137.845 1.00 108.03 ? 42   VAL   A C    1 
ATOM   391  O O    . VAL   A 1 29  ? 186.156 157.275 137.713 1.00 113.02 ? 42   VAL   A O    1 
ATOM   392  C CB   . VAL   A 1 29  ? 185.994 155.019 135.854 1.00 112.27 ? 42   VAL   A CB   1 
ATOM   393  C CG1  . VAL   A 1 29  ? 186.412 154.239 134.610 1.00 120.57 ? 42   VAL   A CG1  1 
ATOM   394  C CG2  . VAL   A 1 29  ? 185.047 154.157 136.688 1.00 112.13 ? 42   VAL   A CG2  1 
ATOM   395  H H    . VAL   A 1 29  ? 187.629 153.405 137.073 1.00 114.40 ? 42   VAL   A H    1 
ATOM   396  H HA   . VAL   A 1 29  ? 187.799 156.114 135.964 1.00 113.42 ? 42   VAL   A HA   1 
ATOM   397  H HB   . VAL   A 1 29  ? 185.455 155.910 135.531 1.00 114.80 ? 42   VAL   A HB   1 
ATOM   398  H HG11 . VAL   A 1 29  ? 185.581 154.219 133.905 1.00 115.58 ? 42   VAL   A HG11 1 
ATOM   399  H HG12 . VAL   A 1 29  ? 186.694 153.217 134.864 1.00 115.16 ? 42   VAL   A HG12 1 
ATOM   400  H HG13 . VAL   A 1 29  ? 187.252 154.735 134.123 1.00 114.86 ? 42   VAL   A HG13 1 
ATOM   401  H HG21 . VAL   A 1 29  ? 184.675 154.728 137.540 1.00 114.05 ? 42   VAL   A HG21 1 
ATOM   402  H HG22 . VAL   A 1 29  ? 185.552 153.260 137.047 1.00 113.89 ? 42   VAL   A HG22 1 
ATOM   403  H HG23 . VAL   A 1 29  ? 184.195 153.862 136.075 1.00 114.45 ? 42   VAL   A HG23 1 
ATOM   404  N N    . SER   A 1 30  ? 187.349 155.948 139.040 1.00 107.10 ? 43   SER   A N    1 
ATOM   405  C CA   . SER   A 1 30  ? 186.900 156.590 140.279 1.00 103.21 ? 43   SER   A CA   1 
ATOM   406  C C    . SER   A 1 30  ? 187.171 158.094 140.359 1.00 107.42 ? 43   SER   A C    1 
ATOM   407  O O    . SER   A 1 30  ? 186.495 158.773 141.128 1.00 119.11 ? 43   SER   A O    1 
ATOM   408  C CB   . SER   A 1 30  ? 187.497 155.878 141.487 1.00 107.93 ? 43   SER   A CB   1 
ATOM   409  O OG   . SER   A 1 30  ? 188.902 155.920 141.441 1.00 118.33 ? 43   SER   A OG   1 
ATOM   410  H H    . SER   A 1 30  ? 187.992 155.172 139.110 1.00 112.64 ? 43   SER   A H    1 
ATOM   411  H HA   . SER   A 1 30  ? 185.819 156.466 140.343 1.00 110.87 ? 43   SER   A HA   1 
ATOM   412  H HB2  . SER   A 1 30  ? 187.148 156.361 142.400 1.00 110.95 ? 43   SER   A HB2  1 
ATOM   413  H HB3  . SER   A 1 30  ? 187.170 154.838 141.495 1.00 111.08 ? 43   SER   A HB3  1 
ATOM   414  H HG   . SER   A 1 30  ? 189.179 155.220 140.845 1.00 113.37 ? 43   SER   A HG   1 
ATOM   415  N N    . TYR   A 1 31  ? 188.065 158.647 139.533 1.00 109.39 ? 44   TYR   A N    1 
ATOM   416  C CA   . TYR   A 1 31  ? 188.306 160.092 139.409 1.00 110.73 ? 44   TYR   A CA   1 
ATOM   417  C C    . TYR   A 1 31  ? 187.853 160.693 138.071 1.00 117.67 ? 44   TYR   A C    1 
ATOM   418  O O    . TYR   A 1 31  ? 188.345 161.734 137.648 1.00 120.22 ? 44   TYR   A O    1 
ATOM   419  C CB   . TYR   A 1 31  ? 189.764 160.404 139.740 1.00 113.87 ? 44   TYR   A CB   1 
ATOM   420  C CG   . TYR   A 1 31  ? 190.117 160.035 141.160 1.00 121.77 ? 44   TYR   A CG   1 
ATOM   421  C CD1  . TYR   A 1 31  ? 189.632 160.823 142.216 1.00 117.26 ? 44   TYR   A CD1  1 
ATOM   422  C CD2  . TYR   A 1 31  ? 190.885 158.890 141.427 1.00 123.82 ? 44   TYR   A CD2  1 
ATOM   423  C CE1  . TYR   A 1 31  ? 189.909 160.464 143.546 1.00 122.17 ? 44   TYR   A CE1  1 
ATOM   424  C CE2  . TYR   A 1 31  ? 191.165 158.527 142.755 1.00 121.86 ? 44   TYR   A CE2  1 
ATOM   425  C CZ   . TYR   A 1 31  ? 190.673 159.313 143.816 1.00 126.69 ? 44   TYR   A CZ   1 
ATOM   426  O OH   . TYR   A 1 31  ? 190.939 158.967 145.101 1.00 130.27 ? 44   TYR   A OH   1 
ATOM   427  H H    . TYR   A 1 31  ? 188.614 158.022 138.961 1.00 117.75 ? 44   TYR   A H    1 
ATOM   428  H HA   . TYR   A 1 31  ? 187.706 160.606 140.160 1.00 117.68 ? 44   TYR   A HA   1 
ATOM   429  H HB2  . TYR   A 1 31  ? 190.416 159.877 139.044 1.00 118.16 ? 44   TYR   A HB2  1 
ATOM   430  H HB3  . TYR   A 1 31  ? 189.944 161.473 139.623 1.00 118.02 ? 44   TYR   A HB3  1 
ATOM   431  H HD1  . TYR   A 1 31  ? 189.040 161.701 142.007 1.00 117.30 ? 44   TYR   A HD1  1 
ATOM   432  H HD2  . TYR   A 1 31  ? 191.248 158.278 140.615 1.00 118.96 ? 44   TYR   A HD2  1 
ATOM   433  H HE1  . TYR   A 1 31  ? 189.539 161.063 144.365 1.00 118.81 ? 44   TYR   A HE1  1 
ATOM   434  H HE2  . TYR   A 1 31  ? 191.748 157.642 142.962 1.00 118.49 ? 44   TYR   A HE2  1 
ATOM   435  H HH   . TYR   A 1 31  ? 191.450 158.156 145.144 1.00 119.31 ? 44   TYR   A HH   1 
ATOM   436  N N    . GLY   A 1 32  ? 186.915 160.053 137.376 1.00 118.82 ? 45   GLY   A N    1 
ATOM   437  C CA   . GLY   A 1 32  ? 186.298 160.587 136.158 1.00 113.44 ? 45   GLY   A CA   1 
ATOM   438  C C    . GLY   A 1 32  ? 186.994 160.199 134.856 1.00 115.88 ? 45   GLY   A C    1 
ATOM   439  O O    . GLY   A 1 32  ? 186.460 160.476 133.784 1.00 121.80 ? 45   GLY   A O    1 
ATOM   440  H H    . GLY   A 1 32  ? 186.582 159.164 137.723 1.00 117.99 ? 45   GLY   A H    1 
ATOM   441  H HA2  . GLY   A 1 32  ? 185.271 160.226 136.103 1.00 117.30 ? 45   GLY   A HA2  1 
ATOM   442  H HA3  . GLY   A 1 32  ? 186.266 161.675 136.209 1.00 116.68 ? 45   GLY   A HA3  1 
ATOM   443  N N    . LEU   A 1 33  ? 188.139 159.517 134.912 1.00 117.51 ? 46   LEU   A N    1 
ATOM   444  C CA   . LEU   A 1 33  ? 188.768 158.906 133.741 1.00 119.09 ? 46   LEU   A CA   1 
ATOM   445  C C    . LEU   A 1 33  ? 187.759 158.037 132.984 1.00 120.60 ? 46   LEU   A C    1 
ATOM   446  O O    . LEU   A 1 33  ? 186.968 157.327 133.590 1.00 122.30 ? 46   LEU   A O    1 
ATOM   447  C CB   . LEU   A 1 33  ? 190.008 158.129 134.206 1.00 115.54 ? 46   LEU   A CB   1 
ATOM   448  C CG   . LEU   A 1 33  ? 190.712 157.324 133.103 1.00 110.84 ? 46   LEU   A CG   1 
ATOM   449  C CD1  . LEU   A 1 33  ? 192.212 157.266 133.363 1.00 113.60 ? 46   LEU   A CD1  1 
ATOM   450  C CD2  . LEU   A 1 33  ? 190.219 155.879 133.055 1.00 117.03 ? 46   LEU   A CD2  1 
ATOM   451  H H    . LEU   A 1 33  ? 188.542 159.339 135.820 1.00 117.31 ? 46   LEU   A H    1 
ATOM   452  H HA   . LEU   A 1 33  ? 189.096 159.696 133.066 1.00 117.53 ? 46   LEU   A HA   1 
ATOM   453  H HB2  . LEU   A 1 33  ? 190.711 158.859 134.608 1.00 117.38 ? 46   LEU   A HB2  1 
ATOM   454  H HB3  . LEU   A 1 33  ? 189.738 157.457 135.021 1.00 117.23 ? 46   LEU   A HB3  1 
ATOM   455  H HG   . LEU   A 1 33  ? 190.554 157.804 132.137 1.00 116.30 ? 46   LEU   A HG   1 
ATOM   456  H HD11 . LEU   A 1 33  ? 192.623 158.275 133.358 1.00 116.05 ? 46   LEU   A HD11 1 
ATOM   457  H HD12 . LEU   A 1 33  ? 192.404 156.806 134.332 1.00 117.41 ? 46   LEU   A HD12 1 
ATOM   458  H HD13 . LEU   A 1 33  ? 192.701 156.682 132.583 1.00 116.71 ? 46   LEU   A HD13 1 
ATOM   459  H HD21 . LEU   A 1 33  ? 189.160 155.836 132.804 1.00 117.31 ? 46   LEU   A HD21 1 
ATOM   460  H HD22 . LEU   A 1 33  ? 190.770 155.321 132.298 1.00 117.58 ? 46   LEU   A HD22 1 
ATOM   461  H HD23 . LEU   A 1 33  ? 190.372 155.403 134.023 1.00 117.87 ? 46   LEU   A HD23 1 
ATOM   462  N N    . GLY   A 1 34  ? 187.762 158.095 131.656 1.00 114.56 ? 47   GLY   A N    1 
ATOM   463  C CA   . GLY   A 1 34  ? 186.854 157.302 130.826 1.00 114.49 ? 47   GLY   A CA   1 
ATOM   464  C C    . GLY   A 1 34  ? 185.447 157.882 130.678 1.00 104.23 ? 47   GLY   A C    1 
ATOM   465  O O    . GLY   A 1 34  ? 184.673 157.356 129.888 1.00 110.15 ? 47   GLY   A O    1 
ATOM   466  H H    . GLY   A 1 34  ? 188.427 158.698 131.193 1.00 112.35 ? 47   GLY   A H    1 
ATOM   467  H HA2  . GLY   A 1 34  ? 187.279 157.193 129.828 1.00 112.95 ? 47   GLY   A HA2  1 
ATOM   468  H HA3  . GLY   A 1 34  ? 186.756 156.306 131.258 1.00 112.65 ? 47   GLY   A HA3  1 
ATOM   469  N N    . THR   A 1 35  ? 185.092 158.960 131.373 1.00 94.51  ? 48   THR   A N    1 
ATOM   470  C CA   . THR   A 1 35  ? 183.781 159.617 131.239 1.00 102.94 ? 48   THR   A CA   1 
ATOM   471  C C    . THR   A 1 35  ? 183.804 160.775 130.245 1.00 100.66 ? 48   THR   A C    1 
ATOM   472  O O    . THR   A 1 35  ? 184.874 161.225 129.839 1.00 113.21 ? 48   THR   A O    1 
ATOM   473  C CB   . THR   A 1 35  ? 183.275 160.124 132.585 1.00 116.00 ? 48   THR   A CB   1 
ATOM   474  O OG1  . THR   A 1 35  ? 184.023 161.220 133.030 1.00 120.83 ? 48   THR   A OG1  1 
ATOM   475  C CG2  . THR   A 1 35  ? 183.314 159.055 133.665 1.00 116.42 ? 48   THR   A CG2  1 
ATOM   476  H H    . THR   A 1 35  ? 185.764 159.364 132.010 1.00 109.83 ? 48   THR   A H    1 
ATOM   477  H HA   . THR   A 1 35  ? 183.052 158.889 130.881 1.00 110.41 ? 48   THR   A HA   1 
ATOM   478  H HB   . THR   A 1 35  ? 182.242 160.447 132.463 1.00 111.10 ? 48   THR   A HB   1 
ATOM   479  H HG1  . THR   A 1 35  ? 184.903 160.912 133.260 1.00 112.35 ? 48   THR   A HG1  1 
ATOM   480  H HG21 . THR   A 1 35  ? 182.857 159.457 134.569 1.00 111.50 ? 48   THR   A HG21 1 
ATOM   481  H HG22 . THR   A 1 35  ? 184.338 158.754 133.888 1.00 111.55 ? 48   THR   A HG22 1 
ATOM   482  H HG23 . THR   A 1 35  ? 182.747 158.185 133.332 1.00 110.89 ? 48   THR   A HG23 1 
ATOM   483  N N    . TYR   A 1 36  ? 182.636 161.288 129.853 1.00 97.87  ? 49   TYR   A N    1 
ATOM   484  C CA   . TYR   A 1 36  ? 182.517 162.432 128.951 1.00 109.28 ? 49   TYR   A CA   1 
ATOM   485  C C    . TYR   A 1 36  ? 181.306 163.301 129.280 1.00 110.75 ? 49   TYR   A C    1 
ATOM   486  O O    . TYR   A 1 36  ? 180.317 162.809 129.817 1.00 111.26 ? 49   TYR   A O    1 
ATOM   487  C CB   . TYR   A 1 36  ? 182.468 161.949 127.501 1.00 110.64 ? 49   TYR   A CB   1 
ATOM   488  C CG   . TYR   A 1 36  ? 181.329 161.028 127.120 1.00 104.52 ? 49   TYR   A CG   1 
ATOM   489  C CD1  . TYR   A 1 36  ? 180.109 161.547 126.659 1.00 108.97 ? 49   TYR   A CD1  1 
ATOM   490  C CD2  . TYR   A 1 36  ? 181.532 159.641 127.134 1.00 105.42 ? 49   TYR   A CD2  1 
ATOM   491  C CE1  . TYR   A 1 36  ? 179.099 160.679 126.203 1.00 112.18 ? 49   TYR   A CE1  1 
ATOM   492  C CE2  . TYR   A 1 36  ? 180.524 158.774 126.691 1.00 110.87 ? 49   TYR   A CE2  1 
ATOM   493  C CZ   . TYR   A 1 36  ? 179.311 159.287 126.211 1.00 113.56 ? 49   TYR   A CZ   1 
ATOM   494  O OH   . TYR   A 1 36  ? 178.361 158.434 125.749 1.00 116.97 ? 49   TYR   A OH   1 
ATOM   495  H H    . TYR   A 1 36  ? 181.774 160.910 130.221 1.00 110.49 ? 49   TYR   A H    1 
ATOM   496  H HA   . TYR   A 1 36  ? 183.402 163.058 129.062 1.00 111.34 ? 49   TYR   A HA   1 
ATOM   497  H HB2  . TYR   A 1 36  ? 182.455 162.816 126.842 1.00 111.48 ? 49   TYR   A HB2  1 
ATOM   498  H HB3  . TYR   A 1 36  ? 183.394 161.408 127.303 1.00 111.66 ? 49   TYR   A HB3  1 
ATOM   499  H HD1  . TYR   A 1 36  ? 179.958 162.615 126.621 1.00 111.28 ? 49   TYR   A HD1  1 
ATOM   500  H HD2  . TYR   A 1 36  ? 182.477 159.236 127.465 1.00 111.54 ? 49   TYR   A HD2  1 
ATOM   501  H HE1  . TYR   A 1 36  ? 178.169 161.084 125.832 1.00 111.37 ? 49   TYR   A HE1  1 
ATOM   502  H HE2  . TYR   A 1 36  ? 180.680 157.706 126.701 1.00 112.40 ? 49   TYR   A HE2  1 
ATOM   503  H HH   . TYR   A 1 36  ? 177.649 158.918 125.325 1.00 112.24 ? 49   TYR   A HH   1 
ATOM   504  N N    . TYR   A 1 37  ? 181.365 164.593 128.966 1.00 111.94 ? 50   TYR   A N    1 
ATOM   505  C CA   . TYR   A 1 37  ? 180.261 165.514 129.232 1.00 108.43 ? 50   TYR   A CA   1 
ATOM   506  C C    . TYR   A 1 37  ? 179.049 165.233 128.346 1.00 112.33 ? 50   TYR   A C    1 
ATOM   507  O O    . TYR   A 1 37  ? 179.179 164.995 127.148 1.00 115.25 ? 50   TYR   A O    1 
ATOM   508  C CB   . TYR   A 1 37  ? 180.724 166.957 129.078 1.00 110.39 ? 50   TYR   A CB   1 
ATOM   509  C CG   . TYR   A 1 37  ? 181.713 167.368 130.139 1.00 111.43 ? 50   TYR   A CG   1 
ATOM   510  C CD1  . TYR   A 1 37  ? 181.272 167.573 131.454 1.00 107.39 ? 50   TYR   A CD1  1 
ATOM   511  C CD2  . TYR   A 1 37  ? 183.068 167.534 129.819 1.00 116.83 ? 50   TYR   A CD2  1 
ATOM   512  C CE1  . TYR   A 1 37  ? 182.187 167.942 132.452 1.00 109.58 ? 50   TYR   A CE1  1 
ATOM   513  C CE2  . TYR   A 1 37  ? 183.986 167.915 130.811 1.00 113.44 ? 50   TYR   A CE2  1 
ATOM   514  C CZ   . TYR   A 1 37  ? 183.545 168.116 132.132 1.00 113.73 ? 50   TYR   A CZ   1 
ATOM   515  O OH   . TYR   A 1 37  ? 184.427 168.468 133.100 1.00 120.14 ? 50   TYR   A OH   1 
ATOM   516  H H    . TYR   A 1 37  ? 182.201 164.946 128.523 1.00 113.92 ? 50   TYR   A H    1 
ATOM   517  H HA   . TYR   A 1 37  ? 179.950 165.378 130.268 1.00 112.81 ? 50   TYR   A HA   1 
ATOM   518  H HB2  . TYR   A 1 37  ? 181.158 167.096 128.088 1.00 113.29 ? 50   TYR   A HB2  1 
ATOM   519  H HB3  . TYR   A 1 37  ? 179.857 167.615 129.153 1.00 113.43 ? 50   TYR   A HB3  1 
ATOM   520  H HD1  . TYR   A 1 37  ? 180.227 167.452 131.701 1.00 112.85 ? 50   TYR   A HD1  1 
ATOM   521  H HD2  . TYR   A 1 37  ? 183.408 167.368 128.808 1.00 114.76 ? 50   TYR   A HD2  1 
ATOM   522  H HE1  . TYR   A 1 37  ? 181.850 168.108 133.464 1.00 113.39 ? 50   TYR   A HE1  1 
ATOM   523  H HE2  . TYR   A 1 37  ? 185.029 168.038 130.562 1.00 113.70 ? 50   TYR   A HE2  1 
ATOM   524  H HH   . TYR   A 1 37  ? 185.273 168.720 132.722 1.00 114.15 ? 50   TYR   A HH   1 
ATOM   525  N N    . ILE   A 1 38  ? 177.857 165.260 128.936 1.00 117.94 ? 51   ILE   A N    1 
ATOM   526  C CA   . ILE   A 1 38  ? 176.624 164.826 128.280 1.00 120.39 ? 51   ILE   A CA   1 
ATOM   527  C C    . ILE   A 1 38  ? 176.064 165.936 127.389 1.00 122.54 ? 51   ILE   A C    1 
ATOM   528  O O    . ILE   A 1 38  ? 175.488 166.901 127.887 1.00 122.15 ? 51   ILE   A O    1 
ATOM   529  C CB   . ILE   A 1 38  ? 175.593 164.377 129.332 1.00 121.59 ? 51   ILE   A CB   1 
ATOM   530  C CG1  . ILE   A 1 38  ? 176.128 163.190 130.159 1.00 122.02 ? 51   ILE   A CG1  1 
ATOM   531  C CG2  . ILE   A 1 38  ? 174.272 163.978 128.649 1.00 122.23 ? 51   ILE   A CG2  1 
ATOM   532  C CD1  . ILE   A 1 38  ? 175.373 162.982 131.474 1.00 129.57 ? 51   ILE   A CD1  1 
ATOM   533  H H    . ILE   A 1 38  ? 177.810 165.513 129.913 1.00 120.82 ? 51   ILE   A H    1 
ATOM   534  H HA   . ILE   A 1 38  ? 176.843 163.963 127.651 1.00 121.08 ? 51   ILE   A HA   1 
ATOM   535  H HB   . ILE   A 1 38  ? 175.401 165.212 130.006 1.00 121.57 ? 51   ILE   A HB   1 
ATOM   536  H HG12 . ILE   A 1 38  ? 176.077 162.278 129.564 1.00 121.14 ? 51   ILE   A HG12 1 
ATOM   537  H HG13 . ILE   A 1 38  ? 177.173 163.348 130.424 1.00 121.16 ? 51   ILE   A HG13 1 
ATOM   538  H HG21 . ILE   A 1 38  ? 173.817 164.834 128.149 1.00 121.20 ? 51   ILE   A HG21 1 
ATOM   539  H HG22 . ILE   A 1 38  ? 174.455 163.193 127.916 1.00 122.10 ? 51   ILE   A HG22 1 
ATOM   540  H HG23 . ILE   A 1 38  ? 173.555 163.610 129.383 1.00 121.34 ? 51   ILE   A HG23 1 
ATOM   541  H HD11 . ILE   A 1 38  ? 175.792 162.121 131.993 1.00 122.90 ? 51   ILE   A HD11 1 
ATOM   542  H HD12 . ILE   A 1 38  ? 174.315 162.793 131.292 1.00 122.75 ? 51   ILE   A HD12 1 
ATOM   543  H HD13 . ILE   A 1 38  ? 175.484 163.863 132.107 1.00 122.44 ? 51   ILE   A HD13 1 
ATOM   544  N N    . LEU   A 1 39  ? 176.168 165.770 126.069 1.00 132.06 ? 52   LEU   A N    1 
ATOM   545  C CA   . LEU   A 1 39  ? 175.560 166.663 125.078 1.00 130.73 ? 52   LEU   A CA   1 
ATOM   546  C C    . LEU   A 1 39  ? 175.891 168.138 125.374 1.00 133.37 ? 52   LEU   A C    1 
ATOM   547  O O    . LEU   A 1 39  ? 177.041 168.474 125.644 1.00 136.64 ? 52   LEU   A O    1 
ATOM   548  C CB   . LEU   A 1 39  ? 174.048 166.364 124.981 1.00 132.77 ? 52   LEU   A CB   1 
ATOM   549  C CG   . LEU   A 1 39  ? 173.688 164.894 124.721 1.00 135.02 ? 52   LEU   A CG   1 
ATOM   550  C CD1  . LEU   A 1 39  ? 172.170 164.739 124.707 1.00 135.35 ? 52   LEU   A CD1  1 
ATOM   551  C CD2  . LEU   A 1 39  ? 174.234 164.406 123.382 1.00 133.60 ? 52   LEU   A CD2  1 
ATOM   552  H H    . LEU   A 1 39  ? 176.706 164.984 125.732 1.00 132.13 ? 52   LEU   A H    1 
ATOM   553  H HA   . LEU   A 1 39  ? 176.002 166.450 124.105 1.00 132.03 ? 52   LEU   A HA   1 
ATOM   554  H HB2  . LEU   A 1 39  ? 173.571 166.666 125.913 1.00 132.62 ? 52   LEU   A HB2  1 
ATOM   555  H HB3  . LEU   A 1 39  ? 173.624 166.963 124.175 1.00 132.50 ? 52   LEU   A HB3  1 
ATOM   556  H HG   . LEU   A 1 39  ? 174.083 164.263 125.517 1.00 132.90 ? 52   LEU   A HG   1 
ATOM   557  H HD11 . LEU   A 1 39  ? 171.762 165.056 125.667 1.00 132.89 ? 52   LEU   A HD11 1 
ATOM   558  H HD12 . LEU   A 1 39  ? 171.739 165.347 123.912 1.00 133.12 ? 52   LEU   A HD12 1 
ATOM   559  H HD13 . LEU   A 1 39  ? 171.910 163.694 124.543 1.00 133.13 ? 52   LEU   A HD13 1 
ATOM   560  H HD21 . LEU   A 1 39  ? 175.324 164.419 123.396 1.00 132.50 ? 52   LEU   A HD21 1 
ATOM   561  H HD22 . LEU   A 1 39  ? 173.874 165.045 122.576 1.00 133.25 ? 52   LEU   A HD22 1 
ATOM   562  H HD23 . LEU   A 1 39  ? 173.906 163.382 123.204 1.00 133.12 ? 52   LEU   A HD23 1 
ATOM   563  N N    . ASP   A 1 40  ? 174.902 169.025 125.332 1.00 145.95 ? 53   ASP   A N    1 
ATOM   564  C CA   . ASP   A 1 40  ? 175.007 170.433 125.718 1.00 148.48 ? 53   ASP   A CA   1 
ATOM   565  C C    . ASP   A 1 40  ? 174.482 170.706 127.140 1.00 148.13 ? 53   ASP   A C    1 
ATOM   566  O O    . ASP   A 1 40  ? 174.285 171.865 127.509 1.00 145.01 ? 53   ASP   A O    1 
ATOM   567  C CB   . ASP   A 1 40  ? 174.287 171.305 124.675 1.00 148.28 ? 53   ASP   A CB   1 
ATOM   568  C CG   . ASP   A 1 40  ? 172.787 171.016 124.520 1.00 149.97 ? 53   ASP   A CG   1 
ATOM   569  O OD1  . ASP   A 1 40  ? 172.287 170.007 125.066 1.00 146.96 ? 53   ASP   A OD1  1 
ATOM   570  O OD2  . ASP   A 1 40  ? 172.108 171.798 123.814 1.00 152.63 ? 53   ASP   A OD2  1 
ATOM   571  H H    . ASP   A 1 40  ? 173.973 168.702 125.106 1.00 145.35 ? 53   ASP   A H    1 
ATOM   572  H HA   . ASP   A 1 40  ? 176.057 170.727 125.714 1.00 146.21 ? 53   ASP   A HA   1 
ATOM   573  H HB2  . ASP   A 1 40  ? 174.428 172.354 124.934 1.00 145.96 ? 53   ASP   A HB2  1 
ATOM   574  H HB3  . ASP   A 1 40  ? 174.770 171.147 123.711 1.00 146.65 ? 53   ASP   A HB3  1 
ATOM   575  N N    . ARG   A 1 41  ? 174.232 169.668 127.945 1.00 128.26 ? 54   ARG   A N    1 
ATOM   576  C CA   . ARG   A 1 41  ? 173.673 169.797 129.299 1.00 122.95 ? 54   ARG   A CA   1 
ATOM   577  C C    . ARG   A 1 41  ? 174.712 170.226 130.323 1.00 123.07 ? 54   ARG   A C    1 
ATOM   578  O O    . ARG   A 1 41  ? 175.895 169.927 130.191 1.00 127.96 ? 54   ARG   A O    1 
ATOM   579  C CB   . ARG   A 1 41  ? 173.043 168.477 129.745 1.00 126.23 ? 54   ARG   A CB   1 
ATOM   580  C CG   . ARG   A 1 41  ? 171.879 168.070 128.843 1.00 126.84 ? 54   ARG   A CG   1 
ATOM   581  C CD   . ARG   A 1 41  ? 171.196 166.841 129.429 1.00 129.35 ? 54   ARG   A CD   1 
ATOM   582  N NE   . ARG   A 1 41  ? 170.069 166.420 128.591 1.00 131.47 ? 54   ARG   A NE   1 
ATOM   583  C CZ   . ARG   A 1 41  ? 169.157 165.524 128.907 1.00 134.82 ? 54   ARG   A CZ   1 
ATOM   584  N NH1  . ARG   A 1 41  ? 168.210 165.234 128.066 1.00 137.90 ? 54   ARG   A NH1  1 
ATOM   585  N NH2  . ARG   A 1 41  ? 169.159 164.902 130.050 1.00 133.49 ? 54   ARG   A NH2  1 
ATOM   586  H H    . ARG   A 1 41  ? 174.500 168.748 127.626 1.00 128.77 ? 54   ARG   A H    1 
ATOM   587  H HA   . ARG   A 1 41  ? 172.899 170.564 129.286 1.00 128.81 ? 54   ARG   A HA   1 
ATOM   588  H HB2  . ARG   A 1 41  ? 173.795 167.689 129.751 1.00 128.78 ? 54   ARG   A HB2  1 
ATOM   589  H HB3  . ARG   A 1 41  ? 172.667 168.596 130.761 1.00 128.83 ? 54   ARG   A HB3  1 
ATOM   590  H HG2  . ARG   A 1 41  ? 171.161 168.888 128.786 1.00 128.31 ? 54   ARG   A HG2  1 
ATOM   591  H HG3  . ARG   A 1 41  ? 172.246 167.838 127.843 1.00 128.47 ? 54   ARG   A HG3  1 
ATOM   592  H HD2  . ARG   A 1 41  ? 171.921 166.031 129.499 1.00 128.66 ? 54   ARG   A HD2  1 
ATOM   593  H HD3  . ARG   A 1 41  ? 170.838 167.088 130.429 1.00 128.31 ? 54   ARG   A HD3  1 
ATOM   594  H HE   . ARG   A 1 41  ? 169.971 166.862 127.688 1.00 128.92 ? 54   ARG   A HE   1 
ATOM   595  H HH11 . ARG   A 1 41  ? 168.167 165.703 127.173 1.00 129.45 ? 54   ARG   A HH11 1 
ATOM   596  H HH12 . ARG   A 1 41  ? 167.506 164.553 128.312 1.00 130.01 ? 54   ARG   A HH12 1 
ATOM   597  H HH21 . ARG   A 1 41  ? 169.859 165.128 130.742 1.00 129.18 ? 54   ARG   A HH21 1 
ATOM   598  H HH22 . ARG   A 1 41  ? 168.435 164.229 130.260 1.00 129.77 ? 54   ARG   A HH22 1 
ATOM   599  N N    . VAL   A 1 42  ? 174.247 170.849 131.399 1.00 112.40 ? 55   VAL   A N    1 
ATOM   600  C CA   . VAL   A 1 42  ? 175.031 171.089 132.613 1.00 109.65 ? 55   VAL   A CA   1 
ATOM   601  C C    . VAL   A 1 42  ? 174.276 170.526 133.805 1.00 115.23 ? 55   VAL   A C    1 
ATOM   602  O O    . VAL   A 1 42  ? 173.096 170.821 133.989 1.00 124.67 ? 55   VAL   A O    1 
ATOM   603  C CB   . VAL   A 1 42  ? 175.329 172.581 132.805 1.00 110.24 ? 55   VAL   A CB   1 
ATOM   604  C CG1  . VAL   A 1 42  ? 176.056 172.863 134.119 1.00 111.59 ? 55   VAL   A CG1  1 
ATOM   605  C CG2  . VAL   A 1 42  ? 176.213 173.100 131.672 1.00 115.31 ? 55   VAL   A CG2  1 
ATOM   606  H H    . VAL   A 1 42  ? 173.259 171.055 131.434 1.00 114.93 ? 55   VAL   A H    1 
ATOM   607  H HA   . VAL   A 1 42  ? 175.986 170.568 132.546 1.00 113.85 ? 55   VAL   A HA   1 
ATOM   608  H HB   . VAL   A 1 42  ? 174.393 173.141 132.802 1.00 114.37 ? 55   VAL   A HB   1 
ATOM   609  H HG11 . VAL   A 1 42  ? 175.416 172.622 134.968 1.00 113.94 ? 55   VAL   A HG11 1 
ATOM   610  H HG12 . VAL   A 1 42  ? 176.308 173.922 134.180 1.00 114.46 ? 55   VAL   A HG12 1 
ATOM   611  H HG13 . VAL   A 1 42  ? 176.972 172.275 134.174 1.00 114.93 ? 55   VAL   A HG13 1 
ATOM   612  H HG21 . VAL   A 1 42  ? 175.697 173.003 130.718 1.00 115.63 ? 55   VAL   A HG21 1 
ATOM   613  H HG22 . VAL   A 1 42  ? 177.145 172.535 131.636 1.00 113.72 ? 55   VAL   A HG22 1 
ATOM   614  H HG23 . VAL   A 1 42  ? 176.438 174.155 131.832 1.00 114.98 ? 55   VAL   A HG23 1 
ATOM   615  N N    . TYR   A 1 43  ? 174.968 169.755 134.636 1.00 106.33 ? 56   TYR   A N    1 
ATOM   616  C CA   . TYR   A 1 43  ? 174.490 169.273 135.926 1.00 109.47 ? 56   TYR   A CA   1 
ATOM   617  C C    . TYR   A 1 43  ? 175.385 169.856 137.017 1.00 110.91 ? 56   TYR   A C    1 
ATOM   618  O O    . TYR   A 1 43  ? 176.583 170.000 136.802 1.00 118.94 ? 56   TYR   A O    1 
ATOM   619  C CB   . TYR   A 1 43  ? 174.529 167.747 135.961 1.00 107.88 ? 56   TYR   A CB   1 
ATOM   620  C CG   . TYR   A 1 43  ? 173.672 167.057 134.927 1.00 107.29 ? 56   TYR   A CG   1 
ATOM   621  C CD1  . TYR   A 1 43  ? 172.326 166.775 135.205 1.00 113.70 ? 56   TYR   A CD1  1 
ATOM   622  C CD2  . TYR   A 1 43  ? 174.233 166.653 133.706 1.00 112.51 ? 56   TYR   A CD2  1 
ATOM   623  C CE1  . TYR   A 1 43  ? 171.546 166.070 134.272 1.00 114.30 ? 56   TYR   A CE1  1 
ATOM   624  C CE2  . TYR   A 1 43  ? 173.456 165.950 132.771 1.00 113.84 ? 56   TYR   A CE2  1 
ATOM   625  C CZ   . TYR   A 1 43  ? 172.114 165.645 133.059 1.00 115.07 ? 56   TYR   A CZ   1 
ATOM   626  O OH   . TYR   A 1 43  ? 171.381 164.916 132.181 1.00 121.13 ? 56   TYR   A OH   1 
ATOM   627  H H    . TYR   A 1 43  ? 175.942 169.586 134.427 1.00 112.99 ? 56   TYR   A H    1 
ATOM   628  H HA   . TYR   A 1 43  ? 173.465 169.599 136.101 1.00 114.49 ? 56   TYR   A HA   1 
ATOM   629  H HB2  . TYR   A 1 43  ? 175.561 167.420 135.830 1.00 113.49 ? 56   TYR   A HB2  1 
ATOM   630  H HB3  . TYR   A 1 43  ? 174.210 167.413 136.948 1.00 113.16 ? 56   TYR   A HB3  1 
ATOM   631  H HD1  . TYR   A 1 43  ? 171.893 167.082 136.146 1.00 113.95 ? 56   TYR   A HD1  1 
ATOM   632  H HD2  . TYR   A 1 43  ? 175.270 166.866 133.495 1.00 114.40 ? 56   TYR   A HD2  1 
ATOM   633  H HE1  . TYR   A 1 43  ? 170.515 165.833 134.490 1.00 114.14 ? 56   TYR   A HE1  1 
ATOM   634  H HE2  . TYR   A 1 43  ? 173.893 165.636 131.834 1.00 114.17 ? 56   TYR   A HE2  1 
ATOM   635  H HH   . TYR   A 1 43  ? 171.940 164.276 131.736 1.00 114.71 ? 56   TYR   A HH   1 
ATOM   636  N N    . LEU   A 1 44  ? 174.836 170.191 138.183 1.00 103.00 ? 57   LEU   A N    1 
ATOM   637  C CA   . LEU   A 1 44  ? 175.588 170.802 139.278 1.00 102.46 ? 57   LEU   A CA   1 
ATOM   638  C C    . LEU   A 1 44  ? 175.370 170.060 140.591 1.00 109.10 ? 57   LEU   A C    1 
ATOM   639  O O    . LEU   A 1 44  ? 174.240 169.724 140.932 1.00 111.03 ? 57   LEU   A O    1 
ATOM   640  C CB   . LEU   A 1 44  ? 175.170 172.264 139.463 1.00 102.41 ? 57   LEU   A CB   1 
ATOM   641  C CG   . LEU   A 1 44  ? 175.482 173.192 138.289 1.00 112.67 ? 57   LEU   A CG   1 
ATOM   642  C CD1  . LEU   A 1 44  ? 174.987 174.595 138.617 1.00 117.14 ? 57   LEU   A CD1  1 
ATOM   643  C CD2  . LEU   A 1 44  ? 176.978 173.282 138.029 1.00 115.59 ? 57   LEU   A CD2  1 
ATOM   644  H H    . LEU   A 1 44  ? 173.848 170.038 138.320 1.00 110.84 ? 57   LEU   A H    1 
ATOM   645  H HA   . LEU   A 1 44  ? 176.656 170.767 139.066 1.00 110.62 ? 57   LEU   A HA   1 
ATOM   646  H HB2  . LEU   A 1 44  ? 174.096 172.296 139.651 1.00 110.47 ? 57   LEU   A HB2  1 
ATOM   647  H HB3  . LEU   A 1 44  ? 175.669 172.657 140.349 1.00 110.15 ? 57   LEU   A HB3  1 
ATOM   648  H HG   . LEU   A 1 44  ? 174.976 172.840 137.390 1.00 111.72 ? 57   LEU   A HG   1 
ATOM   649  H HD11 . LEU   A 1 44  ? 173.912 174.571 138.796 1.00 111.99 ? 57   LEU   A HD11 1 
ATOM   650  H HD12 . LEU   A 1 44  ? 175.187 175.261 137.777 1.00 111.19 ? 57   LEU   A HD12 1 
ATOM   651  H HD13 . LEU   A 1 44  ? 175.492 174.975 139.505 1.00 111.92 ? 57   LEU   A HD13 1 
ATOM   652  H HD21 . LEU   A 1 44  ? 177.348 172.315 137.690 1.00 111.32 ? 57   LEU   A HD21 1 
ATOM   653  H HD22 . LEU   A 1 44  ? 177.502 173.581 138.937 1.00 111.39 ? 57   LEU   A HD22 1 
ATOM   654  H HD23 . LEU   A 1 44  ? 177.169 174.012 137.242 1.00 112.76 ? 57   LEU   A HD23 1 
ATOM   655  N N    . ASN   A 1 45  ? 176.449 169.891 141.352 1.00 121.91 ? 58   ASN   A N    1 
ATOM   656  C CA   . ASN   A 1 45  ? 176.476 169.368 142.713 1.00 117.67 ? 58   ASN   A CA   1 
ATOM   657  C C    . ASN   A 1 45  ? 175.566 168.148 142.930 1.00 120.42 ? 58   ASN   A C    1 
ATOM   658  O O    . ASN   A 1 45  ? 174.667 168.177 143.765 1.00 124.69 ? 58   ASN   A O    1 
ATOM   659  C CB   . ASN   A 1 45  ? 176.182 170.531 143.669 1.00 118.64 ? 58   ASN   A CB   1 
ATOM   660  C CG   . ASN   A 1 45  ? 176.454 170.157 145.111 1.00 127.75 ? 58   ASN   A CG   1 
ATOM   661  O OD1  . ASN   A 1 45  ? 177.297 169.307 145.376 1.00 131.39 ? 58   ASN   A OD1  1 
ATOM   662  N ND2  . ASN   A 1 45  ? 175.789 170.805 146.050 1.00 132.01 ? 58   ASN   A ND2  1 
ATOM   663  H H    . ASN   A 1 45  ? 177.336 170.165 140.954 1.00 125.08 ? 58   ASN   A H    1 
ATOM   664  H HA   . ASN   A 1 45  ? 177.494 169.027 142.905 1.00 124.41 ? 58   ASN   A HA   1 
ATOM   665  H HB2  . ASN   A 1 45  ? 176.808 171.389 143.426 1.00 124.13 ? 58   ASN   A HB2  1 
ATOM   666  H HB3  . ASN   A 1 45  ? 175.139 170.828 143.563 1.00 123.69 ? 58   ASN   A HB3  1 
ATOM   667  H HD21 . ASN   A 1 45  ? 175.186 171.568 145.780 1.00 125.15 ? 58   ASN   A HD21 1 
ATOM   668  N N    . THR   A 1 46  ? 175.665 167.144 142.061 1.00 124.84 ? 59   THR   A N    1 
ATOM   669  C CA   . THR   A 1 46  ? 174.680 166.057 141.971 1.00 126.94 ? 59   THR   A CA   1 
ATOM   670  C C    . THR   A 1 46  ? 175.266 164.785 141.375 1.00 124.70 ? 59   THR   A C    1 
ATOM   671  O O    . THR   A 1 46  ? 176.301 164.822 140.713 1.00 133.25 ? 59   THR   A O    1 
ATOM   672  C CB   . THR   A 1 46  ? 173.458 166.516 141.165 1.00 131.71 ? 59   THR   A CB   1 
ATOM   673  O OG1  . THR   A 1 46  ? 172.429 165.568 141.293 1.00 133.80 ? 59   THR   A OG1  1 
ATOM   674  C CG2  . THR   A 1 46  ? 173.718 166.674 139.669 1.00 124.88 ? 59   THR   A CG2  1 
ATOM   675  H H    . THR   A 1 46  ? 176.443 167.144 141.417 1.00 125.75 ? 59   THR   A H    1 
ATOM   676  H HA   . THR   A 1 46  ? 174.338 165.813 142.977 1.00 125.48 ? 59   THR   A HA   1 
ATOM   677  H HB   . THR   A 1 46  ? 173.100 167.463 141.570 1.00 126.77 ? 59   THR   A HB   1 
ATOM   678  H HG1  . THR   A 1 46  ? 171.635 165.961 140.923 1.00 126.46 ? 59   THR   A HG1  1 
ATOM   679  H HG21 . THR   A 1 46  ? 172.841 167.112 139.191 1.00 125.18 ? 59   THR   A HG21 1 
ATOM   680  H HG22 . THR   A 1 46  ? 174.569 167.336 139.510 1.00 124.48 ? 59   THR   A HG22 1 
ATOM   681  H HG23 . THR   A 1 46  ? 173.927 165.708 139.210 1.00 125.21 ? 59   THR   A HG23 1 
ATOM   682  N N    . THR   A 1 47  ? 174.608 163.651 141.589 1.00 107.87 ? 60   THR   A N    1 
ATOM   683  C CA   . THR   A 1 47  ? 174.985 162.356 141.019 1.00 110.19 ? 60   THR   A CA   1 
ATOM   684  C C    . THR   A 1 47  ? 173.918 161.850 140.064 1.00 110.63 ? 60   THR   A C    1 
ATOM   685  O O    . THR   A 1 47  ? 172.757 161.739 140.442 1.00 122.34 ? 60   THR   A O    1 
ATOM   686  C CB   . THR   A 1 47  ? 175.233 161.313 142.103 1.00 118.29 ? 60   THR   A CB   1 
ATOM   687  O OG1  . THR   A 1 47  ? 174.123 161.222 142.965 1.00 126.65 ? 60   THR   A OG1  1 
ATOM   688  C CG2  . THR   A 1 47  ? 176.454 161.642 142.950 1.00 116.35 ? 60   THR   A CG2  1 
ATOM   689  H H    . THR   A 1 47  ? 173.737 163.704 142.098 1.00 115.66 ? 60   THR   A H    1 
ATOM   690  H HA   . THR   A 1 47  ? 175.914 162.472 140.461 1.00 115.56 ? 60   THR   A HA   1 
ATOM   691  H HB   . THR   A 1 47  ? 175.397 160.345 141.628 1.00 116.52 ? 60   THR   A HB   1 
ATOM   692  H HG1  . THR   A 1 47  ? 173.345 161.110 142.414 1.00 117.83 ? 60   THR   A HG1  1 
ATOM   693  H HG21 . THR   A 1 47  ? 176.593 160.868 143.705 1.00 116.54 ? 60   THR   A HG21 1 
ATOM   694  H HG22 . THR   A 1 47  ? 177.335 161.666 142.309 1.00 115.58 ? 60   THR   A HG22 1 
ATOM   695  H HG23 . THR   A 1 47  ? 176.331 162.607 143.442 1.00 115.80 ? 60   THR   A HG23 1 
ATOM   696  N N    . ILE   A 1 48  ? 174.299 161.502 138.843 1.00 101.66 ? 61   ILE   A N    1 
ATOM   697  C CA   . ILE   A 1 48  ? 173.394 161.057 137.780 1.00 97.50  ? 61   ILE   A CA   1 
ATOM   698  C C    . ILE   A 1 48  ? 173.711 159.614 137.413 1.00 103.25 ? 61   ILE   A C    1 
ATOM   699  O O    . ILE   A 1 48  ? 174.879 159.281 137.258 1.00 119.46 ? 61   ILE   A O    1 
ATOM   700  C CB   . ILE   A 1 48  ? 173.570 161.981 136.561 1.00 103.46 ? 61   ILE   A CB   1 
ATOM   701  C CG1  . ILE   A 1 48  ? 173.228 163.448 136.871 1.00 111.18 ? 61   ILE   A CG1  1 
ATOM   702  C CG2  . ILE   A 1 48  ? 172.763 161.503 135.353 1.00 105.26 ? 61   ILE   A CG2  1 
ATOM   703  C CD1  . ILE   A 1 48  ? 171.787 163.702 137.324 1.00 113.87 ? 61   ILE   A CD1  1 
ATOM   704  H H    . ILE   A 1 48  ? 175.283 161.556 138.621 1.00 110.45 ? 61   ILE   A H    1 
ATOM   705  H HA   . ILE   A 1 48  ? 172.357 161.099 138.113 1.00 107.85 ? 61   ILE   A HA   1 
ATOM   706  H HB   . ILE   A 1 48  ? 174.620 161.953 136.269 1.00 108.73 ? 61   ILE   A HB   1 
ATOM   707  H HG12 . ILE   A 1 48  ? 173.903 163.819 137.643 1.00 109.90 ? 61   ILE   A HG12 1 
ATOM   708  H HG13 . ILE   A 1 48  ? 173.415 164.044 135.978 1.00 109.25 ? 61   ILE   A HG13 1 
ATOM   709  H HG21 . ILE   A 1 48  ? 173.184 160.574 134.968 1.00 108.87 ? 61   ILE   A HG21 1 
ATOM   710  H HG22 . ILE   A 1 48  ? 171.720 161.341 135.627 1.00 109.32 ? 61   ILE   A HG22 1 
ATOM   711  H HG23 . ILE   A 1 48  ? 172.814 162.245 134.557 1.00 108.50 ? 61   ILE   A HG23 1 
ATOM   712  H HD11 . ILE   A 1 48  ? 171.656 164.768 137.509 1.00 110.17 ? 61   ILE   A HD11 1 
ATOM   713  H HD12 . ILE   A 1 48  ? 171.575 163.163 138.248 1.00 109.95 ? 61   ILE   A HD12 1 
ATOM   714  H HD13 . ILE   A 1 48  ? 171.084 163.396 136.550 1.00 110.01 ? 61   ILE   A HD13 1 
ATOM   715  N N    . LEU   A 1 49  ? 172.714 158.753 137.227 1.00 101.45 ? 62   LEU   A N    1 
ATOM   716  C CA   . LEU   A 1 49  ? 172.907 157.504 136.487 1.00 104.59 ? 62   LEU   A CA   1 
ATOM   717  C C    . LEU   A 1 49  ? 172.761 157.782 134.996 1.00 114.43 ? 62   LEU   A C    1 
ATOM   718  O O    . LEU   A 1 49  ? 171.731 158.296 134.567 1.00 123.46 ? 62   LEU   A O    1 
ATOM   719  C CB   . LEU   A 1 49  ? 171.887 156.448 136.924 1.00 100.60 ? 62   LEU   A CB   1 
ATOM   720  C CG   . LEU   A 1 49  ? 172.138 155.888 138.326 1.00 109.50 ? 62   LEU   A CG   1 
ATOM   721  C CD1  . LEU   A 1 49  ? 170.943 155.043 138.754 1.00 112.57 ? 62   LEU   A CD1  1 
ATOM   722  C CD2  . LEU   A 1 49  ? 173.377 155.001 138.368 1.00 113.36 ? 62   LEU   A CD2  1 
ATOM   723  H H    . LEU   A 1 49  ? 171.767 159.071 137.374 1.00 109.31 ? 62   LEU   A H    1 
ATOM   724  H HA   . LEU   A 1 49  ? 173.912 157.118 136.659 1.00 109.64 ? 62   LEU   A HA   1 
ATOM   725  H HB2  . LEU   A 1 49  ? 170.892 156.892 136.889 1.00 109.64 ? 62   LEU   A HB2  1 
ATOM   726  H HB3  . LEU   A 1 49  ? 171.906 155.621 136.215 1.00 108.08 ? 62   LEU   A HB3  1 
ATOM   727  H HG   . LEU   A 1 49  ? 172.256 156.706 139.037 1.00 110.37 ? 62   LEU   A HG   1 
ATOM   728  H HD11 . LEU   A 1 49  ? 170.044 155.658 138.768 1.00 110.45 ? 62   LEU   A HD11 1 
ATOM   729  H HD12 . LEU   A 1 49  ? 170.802 154.214 138.061 1.00 110.11 ? 62   LEU   A HD12 1 
ATOM   730  H HD13 . LEU   A 1 49  ? 171.111 154.650 139.757 1.00 110.73 ? 62   LEU   A HD13 1 
ATOM   731  H HD21 . LEU   A 1 49  ? 174.269 155.582 138.133 1.00 110.39 ? 62   LEU   A HD21 1 
ATOM   732  H HD22 . LEU   A 1 49  ? 173.278 154.183 137.654 1.00 109.88 ? 62   LEU   A HD22 1 
ATOM   733  H HD23 . LEU   A 1 49  ? 173.495 154.587 139.370 1.00 111.31 ? 62   LEU   A HD23 1 
ATOM   734  N N    . PHE   A 1 50  ? 173.759 157.430 134.197 1.00 110.49 ? 63   PHE   A N    1 
ATOM   735  C CA   . PHE   A 1 50  ? 173.772 157.688 132.761 1.00 108.75 ? 63   PHE   A CA   1 
ATOM   736  C C    . PHE   A 1 50  ? 174.270 156.476 131.984 1.00 113.48 ? 63   PHE   A C    1 
ATOM   737  O O    . PHE   A 1 50  ? 175.192 155.802 132.430 1.00 114.00 ? 63   PHE   A O    1 
ATOM   738  C CB   . PHE   A 1 50  ? 174.636 158.914 132.492 1.00 104.77 ? 63   PHE   A CB   1 
ATOM   739  C CG   . PHE   A 1 50  ? 174.688 159.293 131.035 1.00 109.07 ? 63   PHE   A CG   1 
ATOM   740  C CD1  . PHE   A 1 50  ? 173.653 160.052 130.468 1.00 112.90 ? 63   PHE   A CD1  1 
ATOM   741  C CD2  . PHE   A 1 50  ? 175.762 158.875 130.242 1.00 109.91 ? 63   PHE   A CD2  1 
ATOM   742  C CE1  . PHE   A 1 50  ? 173.701 160.399 129.110 1.00 114.90 ? 63   PHE   A CE1  1 
ATOM   743  C CE2  . PHE   A 1 50  ? 175.816 159.228 128.886 1.00 112.98 ? 63   PHE   A CE2  1 
ATOM   744  C CZ   . PHE   A 1 50  ? 174.784 159.988 128.318 1.00 113.80 ? 63   PHE   A CZ   1 
ATOM   745  H H    . PHE   A 1 50  ? 174.586 157.020 134.607 1.00 111.28 ? 63   PHE   A H    1 
ATOM   746  H HA   . PHE   A 1 50  ? 172.761 157.907 132.415 1.00 111.29 ? 63   PHE   A HA   1 
ATOM   747  H HB2  . PHE   A 1 50  ? 174.243 159.762 133.054 1.00 110.95 ? 63   PHE   A HB2  1 
ATOM   748  H HB3  . PHE   A 1 50  ? 175.648 158.724 132.849 1.00 110.73 ? 63   PHE   A HB3  1 
ATOM   749  H HD1  . PHE   A 1 50  ? 172.821 160.374 131.077 1.00 111.80 ? 63   PHE   A HD1  1 
ATOM   750  H HD2  . PHE   A 1 50  ? 176.545 158.274 130.680 1.00 110.66 ? 63   PHE   A HD2  1 
ATOM   751  H HE1  . PHE   A 1 50  ? 172.906 160.986 128.673 1.00 112.54 ? 63   PHE   A HE1  1 
ATOM   752  H HE2  . PHE   A 1 50  ? 176.651 158.912 128.279 1.00 112.03 ? 63   PHE   A HE2  1 
ATOM   753  H HZ   . PHE   A 1 50  ? 174.822 160.259 127.273 1.00 112.52 ? 63   PHE   A HZ   1 
ATOM   754  N N    . THR   A 1 51  ? 173.689 156.191 130.819 1.00 121.17 ? 64   THR   A N    1 
ATOM   755  C CA   . THR   A 1 51  ? 174.145 155.100 129.949 1.00 117.44 ? 64   THR   A CA   1 
ATOM   756  C C    . THR   A 1 51  ? 174.838 155.662 128.723 1.00 121.19 ? 64   THR   A C    1 
ATOM   757  O O    . THR   A 1 51  ? 174.249 156.446 127.985 1.00 124.43 ? 64   THR   A O    1 
ATOM   758  C CB   . THR   A 1 51  ? 173.001 154.183 129.528 1.00 120.02 ? 64   THR   A CB   1 
ATOM   759  O OG1  . THR   A 1 51  ? 172.400 153.642 130.677 1.00 123.94 ? 64   THR   A OG1  1 
ATOM   760  C CG2  . THR   A 1 51  ? 173.461 152.998 128.690 1.00 120.33 ? 64   THR   A CG2  1 
ATOM   761  H H    . THR   A 1 51  ? 172.981 156.819 130.466 1.00 118.84 ? 64   THR   A H    1 
ATOM   762  H HA   . THR   A 1 51  ? 174.860 154.484 130.493 1.00 118.48 ? 64   THR   A HA   1 
ATOM   763  H HB   . THR   A 1 51  ? 172.259 154.751 128.967 1.00 119.45 ? 64   THR   A HB   1 
ATOM   764  H HG1  . THR   A 1 51  ? 171.939 154.360 131.117 1.00 120.08 ? 64   THR   A HG1  1 
ATOM   765  H HG21 . THR   A 1 51  ? 172.606 152.362 128.462 1.00 119.87 ? 64   THR   A HG21 1 
ATOM   766  H HG22 . THR   A 1 51  ? 173.894 153.345 127.751 1.00 119.05 ? 64   THR   A HG22 1 
ATOM   767  H HG23 . THR   A 1 51  ? 174.201 152.415 129.239 1.00 119.21 ? 64   THR   A HG23 1 
ATOM   768  N N    . GLY   A 1 52  ? 176.072 155.242 128.477 1.00 112.40 ? 65   GLY   A N    1 
ATOM   769  C CA   . GLY   A 1 52  ? 176.917 155.781 127.417 1.00 116.24 ? 65   GLY   A CA   1 
ATOM   770  C C    . GLY   A 1 52  ? 177.976 154.783 126.975 1.00 112.75 ? 65   GLY   A C    1 
ATOM   771  O O    . GLY   A 1 52  ? 178.016 153.653 127.459 1.00 112.26 ? 65   GLY   A O    1 
ATOM   772  H H    . GLY   A 1 52  ? 176.474 154.540 129.082 1.00 113.28 ? 65   GLY   A H    1 
ATOM   773  H HA2  . GLY   A 1 52  ? 176.315 156.051 126.549 1.00 114.53 ? 65   GLY   A HA2  1 
ATOM   774  H HA3  . GLY   A 1 52  ? 177.421 156.677 127.781 1.00 114.75 ? 65   GLY   A HA3  1 
ATOM   775  N N    . TYR   A 1 53  ? 178.822 155.177 126.030 1.00 113.49 ? 66   TYR   A N    1 
ATOM   776  C CA   . TYR   A 1 53  ? 179.955 154.361 125.618 1.00 114.70 ? 66   TYR   A CA   1 
ATOM   777  C C    . TYR   A 1 53  ? 181.122 154.583 126.568 1.00 117.15 ? 66   TYR   A C    1 
ATOM   778  O O    . TYR   A 1 53  ? 181.799 155.600 126.483 1.00 123.04 ? 66   TYR   A O    1 
ATOM   779  C CB   . TYR   A 1 53  ? 180.321 154.684 124.173 1.00 118.49 ? 66   TYR   A CB   1 
ATOM   780  C CG   . TYR   A 1 53  ? 179.277 154.183 123.208 1.00 119.27 ? 66   TYR   A CG   1 
ATOM   781  C CD1  . TYR   A 1 53  ? 179.281 152.832 122.827 1.00 117.47 ? 66   TYR   A CD1  1 
ATOM   782  C CD2  . TYR   A 1 53  ? 178.282 155.050 122.737 1.00 118.79 ? 66   TYR   A CD2  1 
ATOM   783  C CE1  . TYR   A 1 53  ? 178.285 152.344 121.969 1.00 117.70 ? 66   TYR   A CE1  1 
ATOM   784  C CE2  . TYR   A 1 53  ? 177.283 154.566 121.882 1.00 118.19 ? 66   TYR   A CE2  1 
ATOM   785  C CZ   . TYR   A 1 53  ? 177.287 153.213 121.495 1.00 121.91 ? 66   TYR   A CZ   1 
ATOM   786  O OH   . TYR   A 1 53  ? 176.304 152.729 120.699 1.00 131.14 ? 66   TYR   A OH   1 
ATOM   787  H H    . TYR   A 1 53  ? 178.759 156.122 125.680 1.00 118.16 ? 66   TYR   A H    1 
ATOM   788  H HA   . TYR   A 1 53  ? 179.679 153.307 125.657 1.00 118.56 ? 66   TYR   A HA   1 
ATOM   789  H HB2  . TYR   A 1 53  ? 180.453 155.759 124.054 1.00 118.81 ? 66   TYR   A HB2  1 
ATOM   790  H HB3  . TYR   A 1 53  ? 181.268 154.202 123.933 1.00 119.62 ? 66   TYR   A HB3  1 
ATOM   791  H HD1  . TYR   A 1 53  ? 180.045 152.166 123.200 1.00 119.54 ? 66   TYR   A HD1  1 
ATOM   792  H HD2  . TYR   A 1 53  ? 178.285 156.089 123.032 1.00 119.46 ? 66   TYR   A HD2  1 
ATOM   793  H HE1  . TYR   A 1 53  ? 178.271 151.305 121.675 1.00 119.58 ? 66   TYR   A HE1  1 
ATOM   794  H HE2  . TYR   A 1 53  ? 176.515 155.232 121.518 1.00 119.49 ? 66   TYR   A HE2  1 
ATOM   795  H HH   . TYR   A 1 53  ? 175.655 153.408 120.503 1.00 121.13 ? 66   TYR   A HH   1 
ATOM   796  N N    . PHE   A 1 54  ? 181.385 153.632 127.458 1.00 107.69 ? 67   PHE   A N    1 
ATOM   797  C CA   . PHE   A 1 54  ? 182.407 153.770 128.494 1.00 101.82 ? 67   PHE   A CA   1 
ATOM   798  C C    . PHE   A 1 54  ? 183.326 152.549 128.569 1.00 104.73 ? 67   PHE   A C    1 
ATOM   799  O O    . PHE   A 1 54  ? 182.948 151.469 128.112 1.00 112.85 ? 67   PHE   A O    1 
ATOM   800  C CB   . PHE   A 1 54  ? 181.734 153.990 129.845 1.00 102.99 ? 67   PHE   A CB   1 
ATOM   801  C CG   . PHE   A 1 54  ? 180.854 155.214 129.959 1.00 103.82 ? 67   PHE   A CG   1 
ATOM   802  C CD1  . PHE   A 1 54  ? 181.378 156.482 129.679 1.00 104.37 ? 67   PHE   A CD1  1 
ATOM   803  C CD2  . PHE   A 1 54  ? 179.532 155.098 130.412 1.00 112.94 ? 67   PHE   A CD2  1 
ATOM   804  C CE1  . PHE   A 1 54  ? 180.595 157.627 129.871 1.00 107.95 ? 67   PHE   A CE1  1 
ATOM   805  C CE2  . PHE   A 1 54  ? 178.745 156.244 130.596 1.00 106.33 ? 67   PHE   A CE2  1 
ATOM   806  C CZ   . PHE   A 1 54  ? 179.282 157.511 130.336 1.00 99.91  ? 67   PHE   A CZ   1 
ATOM   807  H H    . PHE   A 1 54  ? 180.819 152.796 127.456 1.00 109.32 ? 67   PHE   A H    1 
ATOM   808  H HA   . PHE   A 1 54  ? 183.022 154.643 128.278 1.00 107.80 ? 67   PHE   A HA   1 
ATOM   809  H HB2  . PHE   A 1 54  ? 181.154 153.102 130.095 1.00 108.95 ? 67   PHE   A HB2  1 
ATOM   810  H HB3  . PHE   A 1 54  ? 182.516 154.090 130.598 1.00 107.80 ? 67   PHE   A HB3  1 
ATOM   811  H HD1  . PHE   A 1 54  ? 182.393 156.580 129.322 1.00 108.66 ? 67   PHE   A HD1  1 
ATOM   812  H HD2  . PHE   A 1 54  ? 179.118 154.126 130.638 1.00 111.09 ? 67   PHE   A HD2  1 
ATOM   813  H HE1  . PHE   A 1 54  ? 181.001 158.605 129.657 1.00 109.79 ? 67   PHE   A HE1  1 
ATOM   814  H HE2  . PHE   A 1 54  ? 177.732 156.146 130.958 1.00 109.74 ? 67   PHE   A HE2  1 
ATOM   815  H HZ   . PHE   A 1 54  ? 178.695 158.404 130.491 1.00 107.77 ? 67   PHE   A HZ   1 
ATOM   816  N N    . PRO   A 1 55  ? 184.536 152.684 129.131 1.00 95.96  ? 68   PRO   A N    1 
ATOM   817  C CA   . PRO   A 1 55  ? 185.373 151.550 129.481 1.00 97.74  ? 68   PRO   A CA   1 
ATOM   818  C C    . PRO   A 1 55  ? 184.672 150.602 130.448 1.00 105.27 ? 68   PRO   A C    1 
ATOM   819  O O    . PRO   A 1 55  ? 183.781 151.016 131.185 1.00 115.95 ? 68   PRO   A O    1 
ATOM   820  C CB   . PRO   A 1 55  ? 186.602 152.151 130.160 1.00 98.13  ? 68   PRO   A CB   1 
ATOM   821  C CG   . PRO   A 1 55  ? 186.664 153.563 129.607 1.00 106.35 ? 68   PRO   A CG   1 
ATOM   822  C CD   . PRO   A 1 55  ? 185.193 153.923 129.491 1.00 103.59 ? 68   PRO   A CD   1 
ATOM   823  H HA   . PRO   A 1 55  ? 185.669 151.021 128.576 1.00 105.57 ? 68   PRO   A HA   1 
ATOM   824  H HB2  . PRO   A 1 55  ? 186.444 152.206 131.237 1.00 105.73 ? 68   PRO   A HB2  1 
ATOM   825  H HB3  . PRO   A 1 55  ? 187.506 151.586 129.934 1.00 105.30 ? 68   PRO   A HB3  1 
ATOM   826  H HG2  . PRO   A 1 55  ? 187.201 154.237 130.275 1.00 106.82 ? 68   PRO   A HG2  1 
ATOM   827  H HG3  . PRO   A 1 55  ? 187.121 153.550 128.617 1.00 106.93 ? 68   PRO   A HG3  1 
ATOM   828  H HD2  . PRO   A 1 55  ? 184.821 154.271 130.454 1.00 106.01 ? 68   PRO   A HD2  1 
ATOM   829  H HD3  . PRO   A 1 55  ? 185.064 154.693 128.730 1.00 107.09 ? 68   PRO   A HD3  1 
ATOM   830  N N    . LYS   A 1 56  ? 185.115 149.350 130.528 1.00 110.57 ? 69   LYS   A N    1 
ATOM   831  C CA   . LYS   A 1 56  ? 184.827 148.492 131.681 1.00 114.14 ? 69   LYS   A CA   1 
ATOM   832  C C    . LYS   A 1 56  ? 185.826 148.813 132.794 1.00 114.96 ? 69   LYS   A C    1 
ATOM   833  O O    . LYS   A 1 56  ? 187.029 148.719 132.577 1.00 124.44 ? 69   LYS   A O    1 
ATOM   834  C CB   . LYS   A 1 56  ? 184.900 147.026 131.239 1.00 116.40 ? 69   LYS   A CB   1 
ATOM   835  C CG   . LYS   A 1 56  ? 184.551 146.054 132.376 1.00 120.06 ? 69   LYS   A CG   1 
ATOM   836  C CD   . LYS   A 1 56  ? 184.897 144.594 132.062 1.00 120.61 ? 69   LYS   A CD   1 
ATOM   837  C CE   . LYS   A 1 56  ? 184.206 144.073 130.800 1.00 123.98 ? 69   LYS   A CE   1 
ATOM   838  N NZ   . LYS   A 1 56  ? 184.536 142.647 130.561 1.00 131.71 ? 69   LYS   A NZ   1 
ATOM   839  H H    . LYS   A 1 56  ? 185.851 149.065 129.897 1.00 117.63 ? 69   LYS   A H    1 
ATOM   840  H HA   . LYS   A 1 56  ? 183.823 148.691 132.056 1.00 118.71 ? 69   LYS   A HA   1 
ATOM   841  H HB2  . LYS   A 1 56  ? 184.201 146.872 130.417 1.00 118.19 ? 69   LYS   A HB2  1 
ATOM   842  H HB3  . LYS   A 1 56  ? 185.904 146.816 130.871 1.00 118.49 ? 69   LYS   A HB3  1 
ATOM   843  H HG2  . LYS   A 1 56  ? 185.110 146.326 133.271 1.00 119.21 ? 69   LYS   A HG2  1 
ATOM   844  H HG3  . LYS   A 1 56  ? 183.489 146.134 132.605 1.00 119.55 ? 69   LYS   A HG3  1 
ATOM   845  H HD2  . LYS   A 1 56  ? 185.977 144.504 131.944 1.00 119.57 ? 69   LYS   A HD2  1 
ATOM   846  H HD3  . LYS   A 1 56  ? 184.597 143.983 132.914 1.00 118.96 ? 69   LYS   A HD3  1 
ATOM   847  H HE2  . LYS   A 1 56  ? 183.129 144.190 130.920 1.00 119.66 ? 69   LYS   A HE2  1 
ATOM   848  H HE3  . LYS   A 1 56  ? 184.523 144.675 129.949 1.00 119.07 ? 69   LYS   A HE3  1 
ATOM   849  H HZ1  . LYS   A 1 56  ? 184.079 142.300 129.730 1.00 120.75 ? 69   LYS   A HZ1  1 
ATOM   850  H HZ2  . LYS   A 1 56  ? 185.530 142.517 130.440 1.00 120.41 ? 69   LYS   A HZ2  1 
ATOM   851  H HZ3  . LYS   A 1 56  ? 184.243 142.070 131.336 1.00 120.92 ? 69   LYS   A HZ3  1 
ATOM   852  N N    . SER   A 1 57  ? 185.369 149.170 133.986 1.00 115.83 ? 70   SER   A N    1 
ATOM   853  C CA   . SER   A 1 57  ? 186.264 149.385 135.125 1.00 119.80 ? 70   SER   A CA   1 
ATOM   854  C C    . SER   A 1 57  ? 186.945 148.079 135.532 1.00 121.68 ? 70   SER   A C    1 
ATOM   855  O O    . SER   A 1 57  ? 186.326 147.018 135.513 1.00 120.82 ? 70   SER   A O    1 
ATOM   856  C CB   . SER   A 1 57  ? 185.492 149.974 136.297 1.00 121.49 ? 70   SER   A CB   1 
ATOM   857  O OG   . SER   A 1 57  ? 186.373 150.224 137.372 1.00 126.49 ? 70   SER   A OG   1 
ATOM   858  H H    . SER   A 1 57  ? 184.371 149.174 134.141 1.00 120.38 ? 70   SER   A H    1 
ATOM   859  H HA   . SER   A 1 57  ? 187.034 150.101 134.837 1.00 120.18 ? 70   SER   A HA   1 
ATOM   860  H HB2  . SER   A 1 57  ? 185.028 150.910 135.987 1.00 120.36 ? 70   SER   A HB2  1 
ATOM   861  H HB3  . SER   A 1 57  ? 184.719 149.272 136.612 1.00 120.12 ? 70   SER   A HB3  1 
ATOM   862  H HG   . SER   A 1 57  ? 185.854 150.383 138.163 1.00 121.73 ? 70   SER   A HG   1 
ATOM   863  N N    . GLY   A 1 58  ? 188.230 148.114 135.871 1.00 124.17 ? 71   GLY   A N    1 
ATOM   864  C CA   . GLY   A 1 58  ? 188.997 146.901 136.158 1.00 122.87 ? 71   GLY   A CA   1 
ATOM   865  C C    . GLY   A 1 58  ? 189.358 146.052 134.931 1.00 122.12 ? 71   GLY   A C    1 
ATOM   866  O O    . GLY   A 1 58  ? 189.981 145.004 135.089 1.00 120.28 ? 71   GLY   A O    1 
ATOM   867  H H    . GLY   A 1 58  ? 188.702 149.005 135.939 1.00 122.10 ? 71   GLY   A H    1 
ATOM   868  H HA2  . GLY   A 1 58  ? 189.927 147.191 136.648 1.00 120.89 ? 71   GLY   A HA2  1 
ATOM   869  H HA3  . GLY   A 1 58  ? 188.435 146.275 136.851 1.00 121.87 ? 71   GLY   A HA3  1 
ATOM   870  N N    . ALA   A 1 59  ? 189.020 146.473 133.710 1.00 126.64 ? 72   ALA   A N    1 
ATOM   871  C CA   . ALA   A 1 59  ? 189.673 145.955 132.509 1.00 126.51 ? 72   ALA   A CA   1 
ATOM   872  C C    . ALA   A 1 59  ? 191.094 146.509 132.372 1.00 128.37 ? 72   ALA   A C    1 
ATOM   873  O O    . ALA   A 1 59  ? 191.472 147.473 133.037 1.00 130.64 ? 72   ALA   A O    1 
ATOM   874  C CB   . ALA   A 1 59  ? 188.840 146.314 131.279 1.00 124.33 ? 72   ALA   A CB   1 
ATOM   875  H H    . ALA   A 1 59  ? 188.485 147.326 133.618 1.00 125.22 ? 72   ALA   A H    1 
ATOM   876  H HA   . ALA   A 1 59  ? 189.736 144.869 132.572 1.00 124.74 ? 72   ALA   A HA   1 
ATOM   877  H HB1  . ALA   A 1 59  ? 189.288 145.884 130.383 1.00 124.99 ? 72   ALA   A HB1  1 
ATOM   878  H HB2  . ALA   A 1 59  ? 188.787 147.397 131.162 1.00 124.27 ? 72   ALA   A HB2  1 
ATOM   879  H HB3  . ALA   A 1 59  ? 187.837 145.903 131.394 1.00 124.74 ? 72   ALA   A HB3  1 
ATOM   880  N N    . ASN   A 1 60  ? 191.877 145.934 131.467 1.00 125.77 ? 73   ASN   A N    1 
ATOM   881  C CA   . ASN   A 1 60  ? 193.207 146.440 131.166 1.00 121.80 ? 73   ASN   A CA   1 
ATOM   882  C C    . ASN   A 1 60  ? 193.177 147.480 130.043 1.00 120.17 ? 73   ASN   A C    1 
ATOM   883  O O    . ASN   A 1 60  ? 192.456 147.350 129.054 1.00 120.65 ? 73   ASN   A O    1 
ATOM   884  C CB   . ASN   A 1 60  ? 194.144 145.276 130.821 1.00 117.84 ? 73   ASN   A CB   1 
ATOM   885  C CG   . ASN   A 1 60  ? 194.353 144.301 131.963 1.00 126.15 ? 73   ASN   A CG   1 
ATOM   886  O OD1  . ASN   A 1 60  ? 193.942 144.506 133.094 1.00 125.65 ? 73   ASN   A OD1  1 
ATOM   887  N ND2  . ASN   A 1 60  ? 195.001 143.194 131.706 1.00 128.70 ? 73   ASN   A ND2  1 
ATOM   888  H H    . ASN   A 1 60  ? 191.518 145.160 130.926 1.00 123.26 ? 73   ASN   A H    1 
ATOM   889  H HA   . ASN   A 1 60  ? 193.612 146.925 132.054 1.00 122.92 ? 73   ASN   A HA   1 
ATOM   890  H HB2  . ASN   A 1 60  ? 193.749 144.732 129.963 1.00 121.86 ? 73   ASN   A HB2  1 
ATOM   891  H HB3  . ASN   A 1 60  ? 195.120 145.673 130.544 1.00 122.18 ? 73   ASN   A HB3  1 
ATOM   892  H HD21 . ASN   A 1 60  ? 195.418 143.053 130.797 1.00 124.03 ? 73   ASN   A HD21 1 
ATOM   893  H HD22 . ASN   A 1 60  ? 195.162 142.541 132.459 1.00 123.35 ? 73   ASN   A HD22 1 
ATOM   894  N N    . PHE   A 1 61  ? 194.013 148.497 130.174 1.00 115.47 ? 74   PHE   A N    1 
ATOM   895  C CA   . PHE   A 1 61  ? 194.578 149.207 129.048 1.00 111.02 ? 74   PHE   A CA   1 
ATOM   896  C C    . PHE   A 1 61  ? 195.738 148.398 128.472 1.00 120.15 ? 74   PHE   A C    1 
ATOM   897  O O    . PHE   A 1 61  ? 196.472 147.754 129.219 1.00 126.10 ? 74   PHE   A O    1 
ATOM   898  C CB   . PHE   A 1 61  ? 195.155 150.537 129.509 1.00 112.56 ? 74   PHE   A CB   1 
ATOM   899  C CG   . PHE   A 1 61  ? 194.172 151.636 129.815 1.00 111.61 ? 74   PHE   A CG   1 
ATOM   900  C CD1  . PHE   A 1 61  ? 193.596 152.354 128.760 1.00 111.99 ? 74   PHE   A CD1  1 
ATOM   901  C CD2  . PHE   A 1 61  ? 193.941 152.037 131.136 1.00 116.08 ? 74   PHE   A CD2  1 
ATOM   902  C CE1  . PHE   A 1 61  ? 192.799 153.475 129.015 1.00 111.89 ? 74   PHE   A CE1  1 
ATOM   903  C CE2  . PHE   A 1 61  ? 193.165 153.176 131.395 1.00 116.35 ? 74   PHE   A CE2  1 
ATOM   904  C CZ   . PHE   A 1 61  ? 192.594 153.891 130.334 1.00 110.37 ? 74   PHE   A CZ   1 
ATOM   905  H H    . PHE   A 1 61  ? 194.535 148.553 131.037 1.00 117.57 ? 74   PHE   A H    1 
ATOM   906  H HA   . PHE   A 1 61  ? 193.823 149.372 128.280 1.00 115.83 ? 74   PHE   A HA   1 
ATOM   907  H HB2  . PHE   A 1 61  ? 195.791 150.371 130.378 1.00 116.92 ? 74   PHE   A HB2  1 
ATOM   908  H HB3  . PHE   A 1 61  ? 195.800 150.903 128.710 1.00 115.99 ? 74   PHE   A HB3  1 
ATOM   909  H HD1  . PHE   A 1 61  ? 193.804 152.070 127.739 1.00 116.43 ? 74   PHE   A HD1  1 
ATOM   910  H HD2  . PHE   A 1 61  ? 194.382 151.489 131.956 1.00 116.22 ? 74   PHE   A HD2  1 
ATOM   911  H HE1  . PHE   A 1 61  ? 192.376 154.035 128.194 1.00 116.18 ? 74   PHE   A HE1  1 
ATOM   912  H HE2  . PHE   A 1 61  ? 193.009 153.504 132.412 1.00 116.74 ? 74   PHE   A HE2  1 
ATOM   913  H HZ   . PHE   A 1 61  ? 192.002 154.772 130.533 1.00 115.45 ? 74   PHE   A HZ   1 
ATOM   914  N N    . ARG   A 1 62  ? 195.966 148.507 127.167 1.00 113.27 ? 75   ARG   A N    1 
ATOM   915  C CA   . ARG   A 1 62  ? 197.164 148.032 126.465 1.00 109.10 ? 75   ARG   A CA   1 
ATOM   916  C C    . ARG   A 1 62  ? 197.965 149.230 125.986 1.00 116.24 ? 75   ARG   A C    1 
ATOM   917  O O    . ARG   A 1 62  ? 197.369 150.126 125.400 1.00 130.41 ? 75   ARG   A O    1 
ATOM   918  C CB   . ARG   A 1 62  ? 196.706 147.181 125.278 1.00 111.91 ? 75   ARG   A CB   1 
ATOM   919  C CG   . ARG   A 1 62  ? 196.276 145.779 125.721 1.00 111.99 ? 75   ARG   A CG   1 
ATOM   920  C CD   . ARG   A 1 62  ? 195.226 145.156 124.799 1.00 114.05 ? 75   ARG   A CD   1 
ATOM   921  N NE   . ARG   A 1 62  ? 195.694 145.005 123.407 1.00 116.77 ? 75   ARG   A NE   1 
ATOM   922  C CZ   . ARG   A 1 62  ? 195.035 145.350 122.317 1.00 121.75 ? 75   ARG   A CZ   1 
ATOM   923  N NH1  . ARG   A 1 62  ? 195.523 145.117 121.138 1.00 125.03 ? 75   ARG   A NH1  1 
ATOM   924  N NH2  . ARG   A 1 62  ? 193.876 145.938 122.360 1.00 120.34 ? 75   ARG   A NH2  1 
ATOM   925  H H    . ARG   A 1 62  ? 195.298 149.039 126.627 1.00 117.56 ? 75   ARG   A H    1 
ATOM   926  H HA   . ARG   A 1 62  ? 197.798 147.437 127.123 1.00 117.19 ? 75   ARG   A HA   1 
ATOM   927  H HB2  . ARG   A 1 62  ? 195.877 147.685 124.780 1.00 117.11 ? 75   ARG   A HB2  1 
ATOM   928  H HB3  . ARG   A 1 62  ? 197.518 147.088 124.557 1.00 118.29 ? 75   ARG   A HB3  1 
ATOM   929  H HG2  . ARG   A 1 62  ? 197.151 145.132 125.774 1.00 117.34 ? 75   ARG   A HG2  1 
ATOM   930  H HG3  . ARG   A 1 62  ? 195.840 145.832 126.719 1.00 118.12 ? 75   ARG   A HG3  1 
ATOM   931  H HD2  . ARG   A 1 62  ? 194.970 144.172 125.191 1.00 117.49 ? 75   ARG   A HD2  1 
ATOM   932  H HD3  . ARG   A 1 62  ? 194.329 145.773 124.851 1.00 117.99 ? 75   ARG   A HD3  1 
ATOM   933  H HE   . ARG   A 1 62  ? 196.571 144.524 123.269 1.00 117.80 ? 75   ARG   A HE   1 
ATOM   934  H HH11 . ARG   A 1 62  ? 196.374 144.592 121.000 1.00 118.97 ? 75   ARG   A HH11 1 
ATOM   935  H HH12 . ARG   A 1 62  ? 195.040 145.434 120.310 1.00 119.10 ? 75   ARG   A HH12 1 
ATOM   936  H HH21 . ARG   A 1 62  ? 193.433 146.073 123.258 1.00 118.50 ? 75   ARG   A HH21 1 
ATOM   937  H HH22 . ARG   A 1 62  ? 193.367 146.119 121.507 1.00 118.27 ? 75   ARG   A HH22 1 
ATOM   938  N N    . ASP   A 1 63  ? 199.273 149.290 126.209 1.00 116.26 ? 76   ASP   A N    1 
ATOM   939  C CA   . ASP   A 1 63  ? 200.111 150.320 125.582 1.00 118.86 ? 76   ASP   A CA   1 
ATOM   940  C C    . ASP   A 1 63  ? 200.518 149.890 124.179 1.00 124.63 ? 76   ASP   A C    1 
ATOM   941  O O    . ASP   A 1 63  ? 201.380 149.030 124.018 1.00 125.07 ? 76   ASP   A O    1 
ATOM   942  C CB   . ASP   A 1 63  ? 201.364 150.620 126.404 1.00 114.44 ? 76   ASP   A CB   1 
ATOM   943  C CG   . ASP   A 1 63  ? 202.263 151.681 125.750 1.00 128.26 ? 76   ASP   A CG   1 
ATOM   944  O OD1  . ASP   A 1 63  ? 201.823 152.403 124.819 1.00 141.13 ? 76   ASP   A OD1  1 
ATOM   945  O OD2  . ASP   A 1 63  ? 203.430 151.790 126.179 1.00 123.66 ? 76   ASP   A OD2  1 
ATOM   946  H H    . ASP   A 1 63  ? 199.716 148.552 126.737 1.00 123.38 ? 76   ASP   A H    1 
ATOM   947  H HA   . ASP   A 1 63  ? 199.545 151.249 125.509 1.00 124.31 ? 76   ASP   A HA   1 
ATOM   948  H HB2  . ASP   A 1 63  ? 201.064 150.991 127.384 1.00 122.41 ? 76   ASP   A HB2  1 
ATOM   949  H HB3  . ASP   A 1 63  ? 201.927 149.697 126.543 1.00 122.59 ? 76   ASP   A HB3  1 
ATOM   950  N N    . LEU   A 1 64  ? 199.913 150.486 123.158 1.00 119.58 ? 77   LEU   A N    1 
ATOM   951  C CA   . LEU   A 1 64  ? 200.197 150.154 121.766 1.00 118.73 ? 77   LEU   A CA   1 
ATOM   952  C C    . LEU   A 1 64  ? 201.210 151.096 121.108 1.00 120.45 ? 77   LEU   A C    1 
ATOM   953  O O    . LEU   A 1 64  ? 201.445 150.994 119.909 1.00 125.88 ? 77   LEU   A O    1 
ATOM   954  C CB   . LEU   A 1 64  ? 198.882 150.086 120.985 1.00 116.10 ? 77   LEU   A CB   1 
ATOM   955  C CG   . LEU   A 1 64  ? 197.884 149.062 121.536 1.00 112.05 ? 77   LEU   A CG   1 
ATOM   956  C CD1  . LEU   A 1 64  ? 196.675 149.023 120.616 1.00 114.21 ? 77   LEU   A CD1  1 
ATOM   957  C CD2  . LEU   A 1 64  ? 198.461 147.652 121.603 1.00 115.82 ? 77   LEU   A CD2  1 
ATOM   958  H H    . LEU   A 1 64  ? 199.245 151.216 123.359 1.00 119.37 ? 77   LEU   A H    1 
ATOM   959  H HA   . LEU   A 1 64  ? 200.660 149.168 121.720 1.00 118.84 ? 77   LEU   A HA   1 
ATOM   960  H HB2  . LEU   A 1 64  ? 198.417 151.073 120.995 1.00 118.97 ? 77   LEU   A HB2  1 
ATOM   961  H HB3  . LEU   A 1 64  ? 199.103 149.825 119.951 1.00 118.85 ? 77   LEU   A HB3  1 
ATOM   962  H HG   . LEU   A 1 64  ? 197.555 149.361 122.531 1.00 118.59 ? 77   LEU   A HG   1 
ATOM   963  H HD11 . LEU   A 1 64  ? 195.917 148.363 121.038 1.00 118.48 ? 77   LEU   A HD11 1 
ATOM   964  H HD12 . LEU   A 1 64  ? 196.276 150.032 120.515 1.00 118.72 ? 77   LEU   A HD12 1 
ATOM   965  H HD13 . LEU   A 1 64  ? 196.965 148.654 119.633 1.00 118.72 ? 77   LEU   A HD13 1 
ATOM   966  H HD21 . LEU   A 1 64  ? 199.252 147.609 122.351 1.00 118.68 ? 77   LEU   A HD21 1 
ATOM   967  H HD22 . LEU   A 1 64  ? 197.680 146.950 121.892 1.00 118.80 ? 77   LEU   A HD22 1 
ATOM   968  H HD23 . LEU   A 1 64  ? 198.865 147.367 120.631 1.00 118.47 ? 77   LEU   A HD23 1 
ATOM   969  N N    . SER   A 1 65  ? 201.819 152.025 121.839 1.00 120.16 ? 78   SER   A N    1 
ATOM   970  C CA   . SER   A 1 65  ? 202.854 152.877 121.254 1.00 118.75 ? 78   SER   A CA   1 
ATOM   971  C C    . SER   A 1 65  ? 204.104 152.073 120.883 1.00 122.06 ? 78   SER   A C    1 
ATOM   972  O O    . SER   A 1 65  ? 204.451 151.098 121.546 1.00 124.30 ? 78   SER   A O    1 
ATOM   973  C CB   . SER   A 1 65  ? 203.195 154.017 122.204 1.00 126.12 ? 78   SER   A CB   1 
ATOM   974  O OG   . SER   A 1 65  ? 203.742 153.549 123.413 1.00 138.22 ? 78   SER   A OG   1 
ATOM   975  H H    . SER   A 1 65  ? 201.661 152.061 122.836 1.00 124.15 ? 78   SER   A H    1 
ATOM   976  H HA   . SER   A 1 65  ? 202.454 153.324 120.344 1.00 123.35 ? 78   SER   A HA   1 
ATOM   977  H HB2  . SER   A 1 65  ? 203.914 154.677 121.719 1.00 124.29 ? 78   SER   A HB2  1 
ATOM   978  H HB3  . SER   A 1 65  ? 202.293 154.590 122.423 1.00 123.78 ? 78   SER   A HB3  1 
ATOM   979  H HG   . SER   A 1 65  ? 203.055 153.128 123.934 1.00 126.16 ? 78   SER   A HG   1 
ATOM   980  N N    . LEU   A 1 66  ? 204.793 152.469 119.811 1.00 125.21 ? 79   LEU   A N    1 
ATOM   981  C CA   . LEU   A 1 66  ? 205.948 151.754 119.262 1.00 117.06 ? 79   LEU   A CA   1 
ATOM   982  C C    . LEU   A 1 66  ? 206.995 152.743 118.750 1.00 121.13 ? 79   LEU   A C    1 
ATOM   983  O O    . LEU   A 1 66  ? 206.917 153.220 117.620 1.00 132.26 ? 79   LEU   A O    1 
ATOM   984  C CB   . LEU   A 1 66  ? 205.479 150.832 118.125 1.00 122.62 ? 79   LEU   A CB   1 
ATOM   985  C CG   . LEU   A 1 66  ? 204.728 149.571 118.566 1.00 130.87 ? 79   LEU   A CG   1 
ATOM   986  C CD1  . LEU   A 1 66  ? 204.177 148.881 117.328 1.00 133.10 ? 79   LEU   A CD1  1 
ATOM   987  C CD2  . LEU   A 1 66  ? 205.672 148.592 119.253 1.00 132.69 ? 79   LEU   A CD2  1 
ATOM   988  H H    . LEU   A 1 66  ? 204.458 153.272 119.298 1.00 129.20 ? 79   LEU   A H    1 
ATOM   989  H HA   . LEU   A 1 66  ? 206.423 151.153 120.037 1.00 126.69 ? 79   LEU   A HA   1 
ATOM   990  H HB2  . LEU   A 1 66  ? 204.831 151.405 117.462 1.00 128.89 ? 79   LEU   A HB2  1 
ATOM   991  H HB3  . LEU   A 1 66  ? 206.347 150.522 117.544 1.00 127.58 ? 79   LEU   A HB3  1 
ATOM   992  H HG   . LEU   A 1 66  ? 203.898 149.819 119.227 1.00 129.32 ? 79   LEU   A HG   1 
ATOM   993  H HD11 . LEU   A 1 66  ? 203.447 149.526 116.839 1.00 129.22 ? 79   LEU   A HD11 1 
ATOM   994  H HD12 . LEU   A 1 66  ? 204.997 148.668 116.643 1.00 129.02 ? 79   LEU   A HD12 1 
ATOM   995  H HD13 . LEU   A 1 66  ? 203.688 147.947 117.606 1.00 129.27 ? 79   LEU   A HD13 1 
ATOM   996  H HD21 . LEU   A 1 66  ? 205.148 147.658 119.457 1.00 129.45 ? 79   LEU   A HD21 1 
ATOM   997  H HD22 . LEU   A 1 66  ? 206.522 148.376 118.605 1.00 128.82 ? 79   LEU   A HD22 1 
ATOM   998  H HD23 . LEU   A 1 66  ? 206.012 149.003 120.203 1.00 129.01 ? 79   LEU   A HD23 1 
ATOM   999  N N    . LYS   A 1 67  ? 207.980 153.081 119.578 1.00 136.71 ? 80   LYS   A N    1 
ATOM   1000 C CA   . LYS   A 1 67  ? 209.111 153.905 119.149 1.00 138.84 ? 80   LYS   A CA   1 
ATOM   1001 C C    . LYS   A 1 67  ? 210.115 153.053 118.390 1.00 141.04 ? 80   LYS   A C    1 
ATOM   1002 O O    . LYS   A 1 67  ? 210.612 152.077 118.942 1.00 142.40 ? 80   LYS   A O    1 
ATOM   1003 C CB   . LYS   A 1 67  ? 209.733 154.593 120.370 1.00 140.80 ? 80   LYS   A CB   1 
ATOM   1004 C CG   . LYS   A 1 67  ? 210.757 155.667 119.992 1.00 140.97 ? 80   LYS   A CG   1 
ATOM   1005 C CD   . LYS   A 1 67  ? 212.186 155.132 119.851 1.00 145.46 ? 80   LYS   A CD   1 
ATOM   1006 C CE   . LYS   A 1 67  ? 213.074 156.309 119.469 1.00 149.25 ? 80   LYS   A CE   1 
ATOM   1007 N NZ   . LYS   A 1 67  ? 214.484 155.923 119.291 1.00 154.11 ? 80   LYS   A NZ   1 
ATOM   1008 H H    . LYS   A 1 67  ? 207.983 152.697 120.512 1.00 144.61 ? 80   LYS   A H    1 
ATOM   1009 H HA   . LYS   A 1 67  ? 208.740 154.682 118.480 1.00 144.79 ? 80   LYS   A HA   1 
ATOM   1010 H HB2  . LYS   A 1 67  ? 208.935 155.086 120.926 1.00 145.01 ? 80   LYS   A HB2  1 
ATOM   1011 H HB3  . LYS   A 1 67  ? 210.188 153.858 121.034 1.00 145.27 ? 80   LYS   A HB3  1 
ATOM   1012 H HG2  . LYS   A 1 67  ? 210.449 156.158 119.069 1.00 145.03 ? 80   LYS   A HG2  1 
ATOM   1013 H HG3  . LYS   A 1 67  ? 210.757 156.415 120.785 1.00 145.36 ? 80   LYS   A HG3  1 
ATOM   1014 H HD2  . LYS   A 1 67  ? 212.517 154.721 120.805 1.00 145.89 ? 80   LYS   A HD2  1 
ATOM   1015 H HD3  . LYS   A 1 67  ? 212.253 154.360 119.085 1.00 145.68 ? 80   LYS   A HD3  1 
ATOM   1016 H HE2  . LYS   A 1 67  ? 212.705 156.760 118.548 1.00 146.42 ? 80   LYS   A HE2  1 
ATOM   1017 H HE3  . LYS   A 1 67  ? 213.010 157.045 120.271 1.00 145.88 ? 80   LYS   A HE3  1 
ATOM   1018 H HZ1  . LYS   A 1 67  ? 214.754 155.192 119.932 1.00 146.91 ? 80   LYS   A HZ1  1 
ATOM   1019 H HZ2  . LYS   A 1 67  ? 214.679 155.561 118.369 1.00 147.39 ? 80   LYS   A HZ2  1 
ATOM   1020 H HZ3  . LYS   A 1 67  ? 215.105 156.704 119.452 1.00 146.61 ? 80   LYS   A HZ3  1 
ATOM   1021 N N    . GLY   A 1 68  ? 210.468 153.443 117.173 1.00 146.34 ? 81   GLY   A N    1 
ATOM   1022 C CA   . GLY   A 1 68  ? 211.584 152.874 116.408 1.00 144.28 ? 81   GLY   A CA   1 
ATOM   1023 C C    . GLY   A 1 68  ? 212.734 153.867 116.232 1.00 147.95 ? 81   GLY   A C    1 
ATOM   1024 O O    . GLY   A 1 68  ? 212.613 155.040 116.587 1.00 155.41 ? 81   GLY   A O    1 
ATOM   1025 H H    . GLY   A 1 68  ? 210.000 154.256 116.799 1.00 149.14 ? 81   GLY   A H    1 
ATOM   1026 H HA2  . GLY   A 1 68  ? 211.974 151.985 116.903 1.00 148.16 ? 81   GLY   A HA2  1 
ATOM   1027 H HA3  . GLY   A 1 68  ? 211.231 152.576 115.421 1.00 148.43 ? 81   GLY   A HA3  1 
ATOM   1028 N N    . THR   A 1 69  ? 213.847 153.427 115.648 1.00 151.98 ? 82   THR   A N    1 
ATOM   1029 C CA   . THR   A 1 69  ? 214.967 154.320 115.295 1.00 154.98 ? 82   THR   A CA   1 
ATOM   1030 C C    . THR   A 1 69  ? 215.258 154.283 113.797 1.00 151.73 ? 82   THR   A C    1 
ATOM   1031 O O    . THR   A 1 69  ? 215.049 155.288 113.124 1.00 151.00 ? 82   THR   A O    1 
ATOM   1032 C CB   . THR   A 1 69  ? 216.214 154.051 116.151 1.00 157.35 ? 82   THR   A CB   1 
ATOM   1033 O OG1  . THR   A 1 69  ? 215.918 154.230 117.520 1.00 163.26 ? 82   THR   A OG1  1 
ATOM   1034 C CG2  . THR   A 1 69  ? 217.335 155.034 115.824 1.00 153.33 ? 82   THR   A CG2  1 
ATOM   1035 H H    . THR   A 1 69  ? 213.893 152.453 115.384 1.00 154.20 ? 82   THR   A H    1 
ATOM   1036 H HA   . THR   A 1 69  ? 214.687 155.352 115.504 1.00 155.11 ? 82   THR   A HA   1 
ATOM   1037 H HB   . THR   A 1 69  ? 216.569 153.032 115.998 1.00 154.93 ? 82   THR   A HB   1 
ATOM   1038 H HG1  . THR   A 1 69  ? 215.706 153.382 117.916 1.00 155.57 ? 82   THR   A HG1  1 
ATOM   1039 H HG21 . THR   A 1 69  ? 218.169 154.885 116.509 1.00 154.70 ? 82   THR   A HG21 1 
ATOM   1040 H HG22 . THR   A 1 69  ? 216.975 156.058 115.922 1.00 154.42 ? 82   THR   A HG22 1 
ATOM   1041 H HG23 . THR   A 1 69  ? 217.696 154.874 114.808 1.00 154.34 ? 82   THR   A HG23 1 
ATOM   1042 N N    . THR   A 1 70  ? 215.645 153.127 113.251 1.00 153.55 ? 83   THR   A N    1 
ATOM   1043 C CA   . THR   A 1 70  ? 215.861 152.943 111.800 1.00 156.07 ? 83   THR   A CA   1 
ATOM   1044 C C    . THR   A 1 70  ? 215.038 151.780 111.261 1.00 153.43 ? 83   THR   A C    1 
ATOM   1045 O O    . THR   A 1 70  ? 214.245 151.959 110.337 1.00 156.93 ? 83   THR   A O    1 
ATOM   1046 C CB   . THR   A 1 70  ? 217.348 152.738 111.471 1.00 155.27 ? 83   THR   A CB   1 
ATOM   1047 O OG1  . THR   A 1 70  ? 218.089 153.846 111.914 1.00 157.30 ? 83   THR   A OG1  1 
ATOM   1048 C CG2  . THR   A 1 70  ? 217.612 152.607 109.974 1.00 155.48 ? 83   THR   A CG2  1 
ATOM   1049 H H    . THR   A 1 70  ? 215.813 152.342 113.864 1.00 154.68 ? 83   THR   A H    1 
ATOM   1050 H HA   . THR   A 1 70  ? 215.533 153.832 111.261 1.00 155.43 ? 83   THR   A HA   1 
ATOM   1051 H HB   . THR   A 1 70  ? 217.716 151.845 111.976 1.00 154.53 ? 83   THR   A HB   1 
ATOM   1052 H HG1  . THR   A 1 70  ? 219.018 153.653 111.766 1.00 155.12 ? 83   THR   A HG1  1 
ATOM   1053 H HG21 . THR   A 1 70  ? 218.685 152.548 109.792 1.00 154.91 ? 83   THR   A HG21 1 
ATOM   1054 H HG22 . THR   A 1 70  ? 217.205 153.469 109.446 1.00 155.14 ? 83   THR   A HG22 1 
ATOM   1055 H HG23 . THR   A 1 70  ? 217.154 151.697 109.587 1.00 155.17 ? 83   THR   A HG23 1 
ATOM   1056 N N    . TYR   A 1 71  ? 215.200 150.588 111.833 1.00 139.27 ? 84   TYR   A N    1 
ATOM   1057 C CA   . TYR   A 1 71  ? 214.477 149.397 111.401 1.00 141.63 ? 84   TYR   A CA   1 
ATOM   1058 C C    . TYR   A 1 71  ? 213.021 149.383 111.859 1.00 140.64 ? 84   TYR   A C    1 
ATOM   1059 O O    . TYR   A 1 71  ? 212.714 149.790 112.976 1.00 144.02 ? 84   TYR   A O    1 
ATOM   1060 C CB   . TYR   A 1 71  ? 215.187 148.144 111.903 1.00 143.24 ? 84   TYR   A CB   1 
ATOM   1061 C CG   . TYR   A 1 71  ? 216.508 147.887 111.218 1.00 146.93 ? 84   TYR   A CG   1 
ATOM   1062 C CD1  . TYR   A 1 71  ? 216.538 147.145 110.026 1.00 148.21 ? 84   TYR   A CD1  1 
ATOM   1063 C CD2  . TYR   A 1 71  ? 217.702 148.376 111.776 1.00 145.70 ? 84   TYR   A CD2  1 
ATOM   1064 C CE1  . TYR   A 1 71  ? 217.762 146.901 109.379 1.00 147.46 ? 84   TYR   A CE1  1 
ATOM   1065 C CE2  . TYR   A 1 71  ? 218.928 148.135 111.132 1.00 148.35 ? 84   TYR   A CE2  1 
ATOM   1066 C CZ   . TYR   A 1 71  ? 218.959 147.399 109.931 1.00 149.91 ? 84   TYR   A CZ   1 
ATOM   1067 O OH   . TYR   A 1 71  ? 220.140 147.159 109.308 1.00 151.45 ? 84   TYR   A OH   1 
ATOM   1068 H H    . TYR   A 1 71  ? 215.865 150.482 112.585 1.00 145.46 ? 84   TYR   A H    1 
ATOM   1069 H HA   . TYR   A 1 71  ? 214.492 149.375 110.311 1.00 146.61 ? 84   TYR   A HA   1 
ATOM   1070 H HB2  . TYR   A 1 71  ? 215.342 148.226 112.979 1.00 145.93 ? 84   TYR   A HB2  1 
ATOM   1071 H HB3  . TYR   A 1 71  ? 214.542 147.282 111.730 1.00 145.92 ? 84   TYR   A HB3  1 
ATOM   1072 H HD1  . TYR   A 1 71  ? 215.619 146.764 109.605 1.00 146.74 ? 84   TYR   A HD1  1 
ATOM   1073 H HD2  . TYR   A 1 71  ? 217.686 148.923 112.707 1.00 145.87 ? 84   TYR   A HD2  1 
ATOM   1074 H HE1  . TYR   A 1 71  ? 217.796 146.333 108.462 1.00 146.39 ? 84   TYR   A HE1  1 
ATOM   1075 H HE2  . TYR   A 1 71  ? 219.847 148.507 111.562 1.00 146.28 ? 84   TYR   A HE2  1 
ATOM   1076 H HH   . TYR   A 1 71  ? 220.877 147.522 109.805 1.00 146.59 ? 84   TYR   A HH   1 
ATOM   1077 N N    . LEU   A 1 72  ? 212.137 148.845 111.022 1.00 139.40 ? 85   LEU   A N    1 
ATOM   1078 C CA   . LEU   A 1 72  ? 210.757 148.512 111.378 1.00 140.83 ? 85   LEU   A CA   1 
ATOM   1079 C C    . LEU   A 1 72  ? 210.594 146.991 111.418 1.00 142.78 ? 85   LEU   A C    1 
ATOM   1080 O O    . LEU   A 1 72  ? 210.984 146.305 110.473 1.00 142.95 ? 85   LEU   A O    1 
ATOM   1081 C CB   . LEU   A 1 72  ? 209.782 149.120 110.361 1.00 137.74 ? 85   LEU   A CB   1 
ATOM   1082 C CG   . LEU   A 1 72  ? 209.893 150.637 110.173 1.00 141.83 ? 85   LEU   A CG   1 
ATOM   1083 C CD1  . LEU   A 1 72  ? 209.011 151.080 109.015 1.00 140.58 ? 85   LEU   A CD1  1 
ATOM   1084 C CD2  . LEU   A 1 72  ? 209.459 151.397 111.420 1.00 145.35 ? 85   LEU   A CD2  1 
ATOM   1085 H H    . LEU   A 1 72  ? 212.473 148.528 110.123 1.00 142.85 ? 85   LEU   A H    1 
ATOM   1086 H HA   . LEU   A 1 72  ? 210.518 148.905 112.366 1.00 142.28 ? 85   LEU   A HA   1 
ATOM   1087 H HB2  . LEU   A 1 72  ? 209.956 148.642 109.397 1.00 142.32 ? 85   LEU   A HB2  1 
ATOM   1088 H HB3  . LEU   A 1 72  ? 208.764 148.881 110.669 1.00 140.89 ? 85   LEU   A HB3  1 
ATOM   1089 H HG   . LEU   A 1 72  ? 210.922 150.909 109.935 1.00 142.28 ? 85   LEU   A HG   1 
ATOM   1090 H HD11 . LEU   A 1 72  ? 209.298 150.549 108.108 1.00 141.89 ? 85   LEU   A HD11 1 
ATOM   1091 H HD12 . LEU   A 1 72  ? 209.143 152.150 108.849 1.00 141.72 ? 85   LEU   A HD12 1 
ATOM   1092 H HD13 . LEU   A 1 72  ? 207.964 150.870 109.237 1.00 142.02 ? 85   LEU   A HD13 1 
ATOM   1093 H HD21 . LEU   A 1 72  ? 210.169 151.208 112.225 1.00 143.04 ? 85   LEU   A HD21 1 
ATOM   1094 H HD22 . LEU   A 1 72  ? 208.460 151.082 111.722 1.00 142.14 ? 85   LEU   A HD22 1 
ATOM   1095 H HD23 . LEU   A 1 72  ? 209.448 152.467 111.213 1.00 143.08 ? 85   LEU   A HD23 1 
ATOM   1096 N N    . SER   A 1 73  ? 210.021 146.446 112.488 1.00 150.19 ? 86   SER   A N    1 
ATOM   1097 C CA   . SER   A 1 73  ? 209.708 145.017 112.522 1.00 150.55 ? 86   SER   A CA   1 
ATOM   1098 C C    . SER   A 1 73  ? 208.395 144.728 111.810 1.00 151.64 ? 86   SER   A C    1 
ATOM   1099 O O    . SER   A 1 73  ? 207.383 145.356 112.107 1.00 151.33 ? 86   SER   A O    1 
ATOM   1100 C CB   . SER   A 1 73  ? 209.641 144.486 113.951 1.00 152.15 ? 86   SER   A CB   1 
ATOM   1101 O OG   . SER   A 1 73  ? 209.328 143.105 113.933 1.00 153.85 ? 86   SER   A OG   1 
ATOM   1102 H H    . SER   A 1 73  ? 209.681 147.042 113.229 1.00 150.13 ? 86   SER   A H    1 
ATOM   1103 H HA   . SER   A 1 73  ? 210.515 144.475 112.030 1.00 149.64 ? 86   SER   A HA   1 
ATOM   1104 H HB2  . SER   A 1 73  ? 210.604 144.637 114.438 1.00 150.23 ? 86   SER   A HB2  1 
ATOM   1105 H HB3  . SER   A 1 73  ? 208.870 145.022 114.504 1.00 150.23 ? 86   SER   A HB3  1 
ATOM   1106 H HG   . SER   A 1 73  ? 209.824 142.684 114.638 1.00 151.01 ? 86   SER   A HG   1 
ATOM   1107 N N    . THR   A 1 74  ? 208.350 143.735 110.928 1.00 147.86 ? 87   THR   A N    1 
ATOM   1108 C CA   . THR   A 1 74  ? 207.090 143.287 110.319 1.00 143.38 ? 87   THR   A CA   1 
ATOM   1109 C C    . THR   A 1 74  ? 206.086 142.825 111.369 1.00 140.64 ? 87   THR   A C    1 
ATOM   1110 O O    . THR   A 1 74  ? 204.886 143.023 111.196 1.00 140.16 ? 87   THR   A O    1 
ATOM   1111 C CB   . THR   A 1 74  ? 207.324 142.137 109.341 1.00 142.28 ? 87   THR   A CB   1 
ATOM   1112 O OG1  . THR   A 1 74  ? 207.927 141.063 110.009 1.00 144.71 ? 87   THR   A OG1  1 
ATOM   1113 C CG2  . THR   A 1 74  ? 208.226 142.539 108.187 1.00 141.57 ? 87   THR   A CG2  1 
ATOM   1114 H H    . THR   A 1 74  ? 209.202 143.236 110.717 1.00 144.03 ? 87   THR   A H    1 
ATOM   1115 H HA   . THR   A 1 74  ? 206.645 144.114 109.767 1.00 143.15 ? 87   THR   A HA   1 
ATOM   1116 H HB   . THR   A 1 74  ? 206.365 141.814 108.937 1.00 142.66 ? 87   THR   A HB   1 
ATOM   1117 H HG1  . THR   A 1 74  ? 208.712 140.815 109.515 1.00 143.82 ? 87   THR   A HG1  1 
ATOM   1118 H HG21 . THR   A 1 74  ? 208.257 141.731 107.455 1.00 143.17 ? 87   THR   A HG21 1 
ATOM   1119 H HG22 . THR   A 1 74  ? 209.237 142.729 108.547 1.00 143.15 ? 87   THR   A HG22 1 
ATOM   1120 H HG23 . THR   A 1 74  ? 207.836 143.438 107.710 1.00 142.62 ? 87   THR   A HG23 1 
ATOM   1121 N N    . LEU   A 1 75  ? 206.544 142.282 112.500 1.00 133.41 ? 88   LEU   A N    1 
ATOM   1122 C CA   . LEU   A 1 75  ? 205.668 141.810 113.569 1.00 130.06 ? 88   LEU   A CA   1 
ATOM   1123 C C    . LEU   A 1 75  ? 204.892 142.942 114.243 1.00 132.22 ? 88   LEU   A C    1 
ATOM   1124 O O    . LEU   A 1 75  ? 203.855 142.688 114.845 1.00 132.38 ? 88   LEU   A O    1 
ATOM   1125 C CB   . LEU   A 1 75  ? 206.493 141.039 114.606 1.00 128.99 ? 88   LEU   A CB   1 
ATOM   1126 C CG   . LEU   A 1 75  ? 207.209 139.795 114.061 1.00 133.65 ? 88   LEU   A CG   1 
ATOM   1127 C CD1  . LEU   A 1 75  ? 208.032 139.166 115.176 1.00 133.03 ? 88   LEU   A CD1  1 
ATOM   1128 C CD2  . LEU   A 1 75  ? 206.221 138.743 113.561 1.00 136.03 ? 88   LEU   A CD2  1 
ATOM   1129 H H    . LEU   A 1 75  ? 207.543 142.184 112.610 1.00 135.45 ? 88   LEU   A H    1 
ATOM   1130 H HA   . LEU   A 1 75  ? 204.923 141.138 113.142 1.00 134.07 ? 88   LEU   A HA   1 
ATOM   1131 H HB2  . LEU   A 1 75  ? 207.235 141.715 115.032 1.00 134.47 ? 88   LEU   A HB2  1 
ATOM   1132 H HB3  . LEU   A 1 75  ? 205.830 140.728 115.413 1.00 133.97 ? 88   LEU   A HB3  1 
ATOM   1133 H HG   . LEU   A 1 75  ? 207.881 140.075 113.249 1.00 135.06 ? 88   LEU   A HG   1 
ATOM   1134 H HD11 . LEU   A 1 75  ? 208.784 139.883 115.507 1.00 135.96 ? 88   LEU   A HD11 1 
ATOM   1135 H HD12 . LEU   A 1 75  ? 208.544 138.279 114.801 1.00 135.57 ? 88   LEU   A HD12 1 
ATOM   1136 H HD13 . LEU   A 1 75  ? 207.391 138.889 116.013 1.00 134.61 ? 88   LEU   A HD13 1 
ATOM   1137 H HD21 . LEU   A 1 75  ? 205.680 139.119 112.693 1.00 134.84 ? 88   LEU   A HD21 1 
ATOM   1138 H HD22 . LEU   A 1 75  ? 205.512 138.488 114.349 1.00 134.32 ? 88   LEU   A HD22 1 
ATOM   1139 H HD23 . LEU   A 1 75  ? 206.762 137.846 113.261 1.00 135.22 ? 88   LEU   A HD23 1 
ATOM   1140 N N    . TRP   A 1 76  ? 205.333 144.195 114.117 1.00 134.33 ? 89   TRP   A N    1 
ATOM   1141 C CA   . TRP   A 1 76  ? 204.576 145.349 114.600 1.00 131.90 ? 89   TRP   A CA   1 
ATOM   1142 C C    . TRP   A 1 76  ? 203.297 145.603 113.802 1.00 134.06 ? 89   TRP   A C    1 
ATOM   1143 O O    . TRP   A 1 76  ? 202.437 146.346 114.261 1.00 140.87 ? 89   TRP   A O    1 
ATOM   1144 C CB   . TRP   A 1 76  ? 205.458 146.594 114.538 1.00 134.22 ? 89   TRP   A CB   1 
ATOM   1145 C CG   . TRP   A 1 76  ? 206.688 146.609 115.391 1.00 133.61 ? 89   TRP   A CG   1 
ATOM   1146 C CD1  . TRP   A 1 76  ? 207.007 145.739 116.375 1.00 135.18 ? 89   TRP   A CD1  1 
ATOM   1147 C CD2  . TRP   A 1 76  ? 207.769 147.582 115.364 1.00 132.71 ? 89   TRP   A CD2  1 
ATOM   1148 N NE1  . TRP   A 1 76  ? 208.222 146.088 116.928 1.00 136.71 ? 89   TRP   A NE1  1 
ATOM   1149 C CE2  . TRP   A 1 76  ? 208.738 147.214 116.336 1.00 136.61 ? 89   TRP   A CE2  1 
ATOM   1150 C CE3  . TRP   A 1 76  ? 208.032 148.737 114.605 1.00 132.88 ? 89   TRP   A CE3  1 
ATOM   1151 C CZ2  . TRP   A 1 76  ? 209.917 147.938 116.534 1.00 139.46 ? 89   TRP   A CZ2  1 
ATOM   1152 C CZ3  . TRP   A 1 76  ? 209.208 149.479 114.803 1.00 134.70 ? 89   TRP   A CZ3  1 
ATOM   1153 C CH2  . TRP   A 1 76  ? 210.157 149.078 115.755 1.00 138.58 ? 89   TRP   A CH2  1 
ATOM   1154 H H    . TRP   A 1 76  ? 206.181 144.369 113.596 1.00 137.33 ? 89   TRP   A H    1 
ATOM   1155 H HA   . TRP   A 1 76  ? 204.281 145.187 115.637 1.00 136.34 ? 89   TRP   A HA   1 
ATOM   1156 H HB2  . TRP   A 1 76  ? 205.756 146.762 113.503 1.00 137.30 ? 89   TRP   A HB2  1 
ATOM   1157 H HB3  . TRP   A 1 76  ? 204.850 147.454 114.821 1.00 137.13 ? 89   TRP   A HB3  1 
ATOM   1158 H HD1  . TRP   A 1 76  ? 206.405 144.897 116.682 1.00 137.00 ? 89   TRP   A HD1  1 
ATOM   1159 H HE1  . TRP   A 1 76  ? 208.658 145.586 117.688 1.00 138.09 ? 89   TRP   A HE1  1 
ATOM   1160 H HE3  . TRP   A 1 76  ? 207.313 149.053 113.864 1.00 137.06 ? 89   TRP   A HE3  1 
ATOM   1161 H HZ2  . TRP   A 1 76  ? 210.623 147.625 117.289 1.00 137.85 ? 89   TRP   A HZ2  1 
ATOM   1162 H HZ3  . TRP   A 1 76  ? 209.383 150.372 114.222 1.00 137.19 ? 89   TRP   A HZ3  1 
ATOM   1163 H HH2  . TRP   A 1 76  ? 211.059 149.655 115.895 1.00 137.75 ? 89   TRP   A HH2  1 
ATOM   1164 N N    . TYR   A 1 77  ? 203.147 145.015 112.616 1.00 132.83 ? 90   TYR   A N    1 
ATOM   1165 C CA   . TYR   A 1 77  ? 202.030 145.254 111.699 1.00 133.08 ? 90   TYR   A CA   1 
ATOM   1166 C C    . TYR   A 1 77  ? 201.092 144.046 111.593 1.00 135.76 ? 90   TYR   A C    1 
ATOM   1167 O O    . TYR   A 1 77  ? 200.643 143.674 110.507 1.00 140.68 ? 90   TYR   A O    1 
ATOM   1168 C CB   . TYR   A 1 77  ? 202.598 145.692 110.352 1.00 132.40 ? 90   TYR   A CB   1 
ATOM   1169 C CG   . TYR   A 1 77  ? 203.441 146.934 110.455 1.00 129.69 ? 90   TYR   A CG   1 
ATOM   1170 C CD1  . TYR   A 1 77  ? 202.808 148.163 110.652 1.00 132.10 ? 90   TYR   A CD1  1 
ATOM   1171 C CD2  . TYR   A 1 77  ? 204.839 146.863 110.377 1.00 134.12 ? 90   TYR   A CD2  1 
ATOM   1172 C CE1  . TYR   A 1 77  ? 203.567 149.336 110.726 1.00 138.55 ? 90   TYR   A CE1  1 
ATOM   1173 C CE2  . TYR   A 1 77  ? 205.604 148.037 110.449 1.00 134.23 ? 90   TYR   A CE2  1 
ATOM   1174 C CZ   . TYR   A 1 77  ? 204.964 149.278 110.609 1.00 139.23 ? 90   TYR   A CZ   1 
ATOM   1175 O OH   . TYR   A 1 77  ? 205.679 150.427 110.633 1.00 144.25 ? 90   TYR   A OH   1 
ATOM   1176 H H    . TYR   A 1 77  ? 203.893 144.418 112.287 1.00 135.78 ? 90   TYR   A H    1 
ATOM   1177 H HA   . TYR   A 1 77  ? 201.423 146.076 112.078 1.00 135.05 ? 90   TYR   A HA   1 
ATOM   1178 H HB2  . TYR   A 1 77  ? 203.194 144.884 109.929 1.00 136.23 ? 90   TYR   A HB2  1 
ATOM   1179 H HB3  . TYR   A 1 77  ? 201.776 145.902 109.668 1.00 135.04 ? 90   TYR   A HB3  1 
ATOM   1180 H HD1  . TYR   A 1 77  ? 201.735 148.210 110.769 1.00 135.29 ? 90   TYR   A HD1  1 
ATOM   1181 H HD2  . TYR   A 1 77  ? 205.330 145.909 110.254 1.00 136.08 ? 90   TYR   A HD2  1 
ATOM   1182 H HE1  . TYR   A 1 77  ? 203.073 150.282 110.891 1.00 136.54 ? 90   TYR   A HE1  1 
ATOM   1183 H HE2  . TYR   A 1 77  ? 206.681 147.992 110.372 1.00 135.11 ? 90   TYR   A HE2  1 
ATOM   1184 H HH   . TYR   A 1 77  ? 205.096 151.180 110.514 1.00 137.26 ? 90   TYR   A HH   1 
ATOM   1185 N N    . GLN   A 1 78  ? 200.836 143.399 112.724 1.00 131.18 ? 91   GLN   A N    1 
ATOM   1186 C CA   . GLN   A 1 78  ? 200.037 142.184 112.869 1.00 128.63 ? 91   GLN   A CA   1 
ATOM   1187 C C    . GLN   A 1 78  ? 199.244 142.239 114.177 1.00 133.57 ? 91   GLN   A C    1 
ATOM   1188 O O    . GLN   A 1 78  ? 199.473 143.116 115.013 1.00 138.59 ? 91   GLN   A O    1 
ATOM   1189 C CB   . GLN   A 1 78  ? 200.959 140.955 112.863 1.00 127.93 ? 91   GLN   A CB   1 
ATOM   1190 C CG   . GLN   A 1 78  ? 201.806 140.827 111.589 1.00 133.18 ? 91   GLN   A CG   1 
ATOM   1191 C CD   . GLN   A 1 78  ? 202.537 139.493 111.479 1.00 137.59 ? 91   GLN   A CD   1 
ATOM   1192 O OE1  . GLN   A 1 78  ? 202.373 138.575 112.270 1.00 138.67 ? 91   GLN   A OE1  1 
ATOM   1193 N NE2  . GLN   A 1 78  ? 203.371 139.326 110.479 1.00 136.59 ? 91   GLN   A NE2  1 
ATOM   1194 H H    . GLN   A 1 78  ? 201.231 143.778 113.572 1.00 134.10 ? 91   GLN   A H    1 
ATOM   1195 H HA   . GLN   A 1 78  ? 199.326 142.101 112.046 1.00 132.72 ? 91   GLN   A HA   1 
ATOM   1196 H HB2  . GLN   A 1 78  ? 201.624 140.996 113.726 1.00 132.42 ? 91   GLN   A HB2  1 
ATOM   1197 H HB3  . GLN   A 1 78  ? 200.335 140.065 112.953 1.00 132.78 ? 91   GLN   A HB3  1 
ATOM   1198 H HG2  . GLN   A 1 78  ? 201.156 140.927 110.719 1.00 133.53 ? 91   GLN   A HG2  1 
ATOM   1199 H HG3  . GLN   A 1 78  ? 202.548 141.625 111.565 1.00 133.47 ? 91   GLN   A HG3  1 
ATOM   1200 H HE21 . GLN   A 1 78  ? 203.530 140.068 109.812 1.00 133.24 ? 91   GLN   A HE21 1 
ATOM   1201 H HE22 . GLN   A 1 78  ? 203.850 138.440 110.401 1.00 134.04 ? 91   GLN   A HE22 1 
ATOM   1202 N N    . LYS   A 1 79  ? 198.331 141.294 114.413 1.00 138.11 ? 92   LYS   A N    1 
ATOM   1203 C CA   . LYS   A 1 79  ? 197.897 141.008 115.789 1.00 135.93 ? 92   LYS   A CA   1 
ATOM   1204 C C    . LYS   A 1 79  ? 199.129 140.658 116.639 1.00 137.07 ? 92   LYS   A C    1 
ATOM   1205 O O    . LYS   A 1 79  ? 200.024 139.979 116.132 1.00 138.25 ? 92   LYS   A O    1 
ATOM   1206 C CB   . LYS   A 1 79  ? 196.884 139.858 115.807 1.00 136.62 ? 92   LYS   A CB   1 
ATOM   1207 C CG   . LYS   A 1 79  ? 195.536 140.285 115.219 1.00 142.20 ? 92   LYS   A CG   1 
ATOM   1208 C CD   . LYS   A 1 79  ? 194.499 139.169 115.375 1.00 143.98 ? 92   LYS   A CD   1 
ATOM   1209 C CE   . LYS   A 1 79  ? 193.132 139.668 114.898 1.00 144.39 ? 92   LYS   A CE   1 
ATOM   1210 N NZ   . LYS   A 1 79  ? 192.073 138.654 115.121 1.00 143.16 ? 92   LYS   A NZ   1 
ATOM   1211 H H    . LYS   A 1 79  ? 198.154 140.603 113.698 1.00 138.58 ? 92   LYS   A H    1 
ATOM   1212 H HA   . LYS   A 1 79  ? 197.425 141.900 116.201 1.00 137.61 ? 92   LYS   A HA   1 
ATOM   1213 H HB2  . LYS   A 1 79  ? 197.276 139.006 115.250 1.00 138.11 ? 92   LYS   A HB2  1 
ATOM   1214 H HB3  . LYS   A 1 79  ? 196.727 139.546 116.840 1.00 138.00 ? 92   LYS   A HB3  1 
ATOM   1215 H HG2  . LYS   A 1 79  ? 195.183 141.166 115.755 1.00 139.22 ? 92   LYS   A HG2  1 
ATOM   1216 H HG3  . LYS   A 1 79  ? 195.651 140.530 114.163 1.00 138.98 ? 92   LYS   A HG3  1 
ATOM   1217 H HD2  . LYS   A 1 79  ? 194.804 138.303 114.789 1.00 139.00 ? 92   LYS   A HD2  1 
ATOM   1218 H HD3  . LYS   A 1 79  ? 194.432 138.887 116.426 1.00 139.27 ? 92   LYS   A HD3  1 
ATOM   1219 H HE2  . LYS   A 1 79  ? 192.886 140.581 115.440 1.00 139.14 ? 92   LYS   A HE2  1 
ATOM   1220 H HE3  . LYS   A 1 79  ? 193.199 139.914 113.838 1.00 139.42 ? 92   LYS   A HE3  1 
ATOM   1221 H HZ1  . LYS   A 1 79  ? 191.174 138.998 114.814 1.00 139.21 ? 92   LYS   A HZ1  1 
ATOM   1222 H HZ2  . LYS   A 1 79  ? 191.991 138.425 116.102 1.00 139.33 ? 92   LYS   A HZ2  1 
ATOM   1223 H HZ3  . LYS   A 1 79  ? 192.269 137.802 114.615 1.00 139.24 ? 92   LYS   A HZ3  1 
ATOM   1224 N N    . PRO   A 1 80  ? 199.212 141.089 117.905 1.00 129.56 ? 93   PRO   A N    1 
ATOM   1225 C CA   . PRO   A 1 80  ? 198.164 141.723 118.699 1.00 126.43 ? 93   PRO   A CA   1 
ATOM   1226 C C    . PRO   A 1 80  ? 198.067 143.249 118.568 1.00 129.77 ? 93   PRO   A C    1 
ATOM   1227 O O    . PRO   A 1 80  ? 197.227 143.840 119.237 1.00 133.52 ? 93   PRO   A O    1 
ATOM   1228 C CB   . PRO   A 1 80  ? 198.525 141.347 120.136 1.00 128.52 ? 93   PRO   A CB   1 
ATOM   1229 C CG   . PRO   A 1 80  ? 200.046 141.399 120.107 1.00 130.18 ? 93   PRO   A CG   1 
ATOM   1230 C CD   . PRO   A 1 80  ? 200.362 140.798 118.745 1.00 129.99 ? 93   PRO   A CD   1 
ATOM   1231 H HA   . PRO   A 1 80  ? 197.191 141.296 118.458 1.00 128.65 ? 93   PRO   A HA   1 
ATOM   1232 H HB2  . PRO   A 1 80  ? 198.111 142.030 120.878 1.00 129.46 ? 93   PRO   A HB2  1 
ATOM   1233 H HB3  . PRO   A 1 80  ? 198.199 140.327 120.340 1.00 129.86 ? 93   PRO   A HB3  1 
ATOM   1234 H HG2  . PRO   A 1 80  ? 200.385 142.434 120.140 1.00 129.94 ? 93   PRO   A HG2  1 
ATOM   1235 H HG3  . PRO   A 1 80  ? 200.489 140.820 120.917 1.00 129.83 ? 93   PRO   A HG3  1 
ATOM   1236 H HD2  . PRO   A 1 80  ? 201.273 141.238 118.338 1.00 129.38 ? 93   PRO   A HD2  1 
ATOM   1237 H HD3  . PRO   A 1 80  ? 200.478 139.718 118.842 1.00 129.54 ? 93   PRO   A HD3  1 
ATOM   1238 N N    . PHE   A 1 81  ? 198.909 143.915 117.775 1.00 125.06 ? 94   PHE   A N    1 
ATOM   1239 C CA   . PHE   A 1 81  ? 198.884 145.377 117.661 1.00 122.90 ? 94   PHE   A CA   1 
ATOM   1240 C C    . PHE   A 1 81  ? 197.727 145.873 116.790 1.00 122.02 ? 94   PHE   A C    1 
ATOM   1241 O O    . PHE   A 1 81  ? 196.940 146.717 117.216 1.00 119.23 ? 94   PHE   A O    1 
ATOM   1242 C CB   . PHE   A 1 81  ? 200.212 145.887 117.109 1.00 120.15 ? 94   PHE   A CB   1 
ATOM   1243 C CG   . PHE   A 1 81  ? 201.430 145.471 117.893 1.00 117.89 ? 94   PHE   A CG   1 
ATOM   1244 C CD1  . PHE   A 1 81  ? 201.870 146.262 118.963 1.00 115.31 ? 94   PHE   A CD1  1 
ATOM   1245 C CD2  . PHE   A 1 81  ? 202.146 144.320 117.529 1.00 123.63 ? 94   PHE   A CD2  1 
ATOM   1246 C CE1  . PHE   A 1 81  ? 203.037 145.913 119.657 1.00 118.49 ? 94   PHE   A CE1  1 
ATOM   1247 C CE2  . PHE   A 1 81  ? 203.306 143.964 118.233 1.00 125.55 ? 94   PHE   A CE2  1 
ATOM   1248 C CZ   . PHE   A 1 81  ? 203.754 144.764 119.295 1.00 121.61 ? 94   PHE   A CZ   1 
ATOM   1249 H H    . PHE   A 1 81  ? 199.584 143.405 117.223 1.00 123.65 ? 94   PHE   A H    1 
ATOM   1250 H HA   . PHE   A 1 81  ? 198.755 145.808 118.654 1.00 123.52 ? 94   PHE   A HA   1 
ATOM   1251 H HB2  . PHE   A 1 81  ? 200.330 145.549 116.079 1.00 124.57 ? 94   PHE   A HB2  1 
ATOM   1252 H HB3  . PHE   A 1 81  ? 200.174 146.976 117.099 1.00 122.53 ? 94   PHE   A HB3  1 
ATOM   1253 H HD1  . PHE   A 1 81  ? 201.324 147.150 119.244 1.00 122.41 ? 94   PHE   A HD1  1 
ATOM   1254 H HD2  . PHE   A 1 81  ? 201.820 143.715 116.696 1.00 124.23 ? 94   PHE   A HD2  1 
ATOM   1255 H HE1  . PHE   A 1 81  ? 203.376 146.524 120.481 1.00 123.19 ? 94   PHE   A HE1  1 
ATOM   1256 H HE2  . PHE   A 1 81  ? 203.858 143.080 117.951 1.00 124.13 ? 94   PHE   A HE2  1 
ATOM   1257 H HZ   . PHE   A 1 81  ? 204.650 144.494 119.835 1.00 123.34 ? 94   PHE   A HZ   1 
ATOM   1258 N N    . LEU   A 1 82  ? 197.576 145.331 115.582 1.00 132.01 ? 95   LEU   A N    1 
ATOM   1259 C CA   . LEU   A 1 82  ? 196.400 145.572 114.747 1.00 130.34 ? 95   LEU   A CA   1 
ATOM   1260 C C    . LEU   A 1 82  ? 195.174 145.007 115.466 1.00 130.35 ? 95   LEU   A C    1 
ATOM   1261 O O    . LEU   A 1 82  ? 195.149 143.824 115.789 1.00 131.54 ? 95   LEU   A O    1 
ATOM   1262 C CB   . LEU   A 1 82  ? 196.636 144.931 113.373 1.00 126.58 ? 95   LEU   A CB   1 
ATOM   1263 C CG   . LEU   A 1 82  ? 195.420 144.975 112.440 1.00 126.46 ? 95   LEU   A CG   1 
ATOM   1264 C CD1  . LEU   A 1 82  ? 195.000 146.402 112.114 1.00 127.32 ? 95   LEU   A CD1  1 
ATOM   1265 C CD2  . LEU   A 1 82  ? 195.766 144.274 111.132 1.00 129.07 ? 95   LEU   A CD2  1 
ATOM   1266 H H    . LEU   A 1 82  ? 198.236 144.624 115.294 1.00 129.69 ? 95   LEU   A H    1 
ATOM   1267 H HA   . LEU   A 1 82  ? 196.262 146.645 114.617 1.00 128.89 ? 95   LEU   A HA   1 
ATOM   1268 H HB2  . LEU   A 1 82  ? 197.475 145.433 112.890 1.00 128.57 ? 95   LEU   A HB2  1 
ATOM   1269 H HB3  . LEU   A 1 82  ? 196.905 143.885 113.521 1.00 128.67 ? 95   LEU   A HB3  1 
ATOM   1270 H HG   . LEU   A 1 82  ? 194.582 144.452 112.899 1.00 129.00 ? 95   LEU   A HG   1 
ATOM   1271 H HD11 . LEU   A 1 82  ? 194.646 146.907 113.013 1.00 128.98 ? 95   LEU   A HD11 1 
ATOM   1272 H HD12 . LEU   A 1 82  ? 194.186 146.381 111.389 1.00 129.24 ? 95   LEU   A HD12 1 
ATOM   1273 H HD13 . LEU   A 1 82  ? 195.840 146.953 111.692 1.00 129.11 ? 95   LEU   A HD13 1 
ATOM   1274 H HD21 . LEU   A 1 82  ? 196.049 143.241 111.332 1.00 129.12 ? 95   LEU   A HD21 1 
ATOM   1275 H HD22 . LEU   A 1 82  ? 196.590 144.787 110.636 1.00 128.98 ? 95   LEU   A HD22 1 
ATOM   1276 H HD23 . LEU   A 1 82  ? 194.896 144.274 110.475 1.00 129.54 ? 95   LEU   A HD23 1 
ATOM   1277 N N    . SER   A 1 83  ? 194.187 145.843 115.766 1.00 131.07 ? 96   SER   A N    1 
ATOM   1278 C CA   . SER   A 1 83  ? 193.184 145.549 116.793 1.00 129.96 ? 96   SER   A CA   1 
ATOM   1279 C C    . SER   A 1 83  ? 191.757 145.754 116.307 1.00 133.62 ? 96   SER   A C    1 
ATOM   1280 O O    . SER   A 1 83  ? 191.467 146.731 115.625 1.00 139.63 ? 96   SER   A O    1 
ATOM   1281 C CB   . SER   A 1 83  ? 193.410 146.484 117.973 1.00 129.87 ? 96   SER   A CB   1 
ATOM   1282 O OG   . SER   A 1 83  ? 194.632 146.223 118.631 1.00 134.07 ? 96   SER   A OG   1 
ATOM   1283 H H    . SER   A 1 83  ? 194.236 146.796 115.435 1.00 131.86 ? 96   SER   A H    1 
ATOM   1284 H HA   . SER   A 1 83  ? 193.279 144.522 117.147 1.00 130.73 ? 96   SER   A HA   1 
ATOM   1285 H HB2  . SER   A 1 83  ? 193.416 147.511 117.606 1.00 130.46 ? 96   SER   A HB2  1 
ATOM   1286 H HB3  . SER   A 1 83  ? 192.594 146.360 118.685 1.00 131.29 ? 96   SER   A HB3  1 
ATOM   1287 H HG   . SER   A 1 83  ? 195.349 146.476 118.045 1.00 130.91 ? 96   SER   A HG   1 
ATOM   1288 N N    . ASP   A 1 84  ? 190.840 144.873 116.697 1.00 137.98 ? 97   ASP   A N    1 
ATOM   1289 C CA   . ASP   A 1 84  ? 189.422 144.988 116.357 1.00 137.96 ? 97   ASP   A CA   1 
ATOM   1290 C C    . ASP   A 1 84  ? 188.773 146.200 117.035 1.00 135.48 ? 97   ASP   A C    1 
ATOM   1291 O O    . ASP   A 1 84  ? 188.936 146.404 118.235 1.00 131.58 ? 97   ASP   A O    1 
ATOM   1292 C CB   . ASP   A 1 84  ? 188.648 143.717 116.736 1.00 142.69 ? 97   ASP   A CB   1 
ATOM   1293 C CG   . ASP   A 1 84  ? 189.367 142.418 116.359 1.00 149.81 ? 97   ASP   A CG   1 
ATOM   1294 O OD1  . ASP   A 1 84  ? 190.399 142.094 116.991 1.00 151.10 ? 97   ASP   A OD1  1 
ATOM   1295 O OD2  . ASP   A 1 84  ? 188.881 141.702 115.454 1.00 149.76 ? 97   ASP   A OD2  1 
ATOM   1296 H H    . ASP   A 1 84  ? 191.126 144.054 117.213 1.00 139.82 ? 97   ASP   A H    1 
ATOM   1297 H HA   . ASP   A 1 84  ? 189.348 145.108 115.276 1.00 140.05 ? 97   ASP   A HA   1 
ATOM   1298 H HB2  . ASP   A 1 84  ? 188.486 143.712 117.814 1.00 140.71 ? 97   ASP   A HB2  1 
ATOM   1299 H HB3  . ASP   A 1 84  ? 187.669 143.753 116.259 1.00 140.59 ? 97   ASP   A HB3  1 
ATOM   1300 N N    . PHE   A 1 85  ? 188.012 147.001 116.293 1.00 122.51 ? 98   PHE   A N    1 
ATOM   1301 C CA   . PHE   A 1 85  ? 187.430 148.238 116.818 1.00 121.35 ? 98   PHE   A CA   1 
ATOM   1302 C C    . PHE   A 1 85  ? 186.103 148.036 117.562 1.00 128.89 ? 98   PHE   A C    1 
ATOM   1303 O O    . PHE   A 1 85  ? 185.813 148.783 118.490 1.00 130.58 ? 98   PHE   A O    1 
ATOM   1304 C CB   . PHE   A 1 85  ? 187.289 149.227 115.664 1.00 117.05 ? 98   PHE   A CB   1 
ATOM   1305 C CG   . PHE   A 1 85  ? 186.864 150.618 116.069 1.00 117.87 ? 98   PHE   A CG   1 
ATOM   1306 C CD1  . PHE   A 1 85  ? 187.781 151.486 116.677 1.00 117.42 ? 98   PHE   A CD1  1 
ATOM   1307 C CD2  . PHE   A 1 85  ? 185.568 151.069 115.785 1.00 121.40 ? 98   PHE   A CD2  1 
ATOM   1308 C CE1  . PHE   A 1 85  ? 187.407 152.800 116.990 1.00 120.04 ? 98   PHE   A CE1  1 
ATOM   1309 C CE2  . PHE   A 1 85  ? 185.192 152.382 116.101 1.00 123.01 ? 98   PHE   A CE2  1 
ATOM   1310 C CZ   . PHE   A 1 85  ? 186.111 153.249 116.704 1.00 122.42 ? 98   PHE   A CZ   1 
ATOM   1311 H H    . PHE   A 1 85  ? 187.908 146.784 115.312 1.00 123.51 ? 98   PHE   A H    1 
ATOM   1312 H HA   . PHE   A 1 85  ? 188.123 148.673 117.539 1.00 122.67 ? 98   PHE   A HA   1 
ATOM   1313 H HB2  . PHE   A 1 85  ? 188.249 149.310 115.154 1.00 122.34 ? 98   PHE   A HB2  1 
ATOM   1314 H HB3  . PHE   A 1 85  ? 186.574 148.829 114.944 1.00 121.75 ? 98   PHE   A HB3  1 
ATOM   1315 H HD1  . PHE   A 1 85  ? 188.785 151.153 116.896 1.00 122.55 ? 98   PHE   A HD1  1 
ATOM   1316 H HD2  . PHE   A 1 85  ? 184.860 150.406 115.308 1.00 122.34 ? 98   PHE   A HD2  1 
ATOM   1317 H HE1  . PHE   A 1 85  ? 188.120 153.468 117.449 1.00 122.76 ? 98   PHE   A HE1  1 
ATOM   1318 H HE2  . PHE   A 1 85  ? 184.195 152.730 115.873 1.00 122.57 ? 98   PHE   A HE2  1 
ATOM   1319 H HZ   . PHE   A 1 85  ? 185.821 154.259 116.951 1.00 122.89 ? 98   PHE   A HZ   1 
ATOM   1320 N N    . ASN   A 1 86  ? 185.301 147.028 117.205 1.00 133.71 ? 99   ASN   A N    1 
ATOM   1321 C CA   . ASN   A 1 86  ? 184.004 146.731 117.830 1.00 127.76 ? 99   ASN   A CA   1 
ATOM   1322 C C    . ASN   A 1 86  ? 183.117 147.986 117.964 1.00 129.46 ? 99   ASN   A C    1 
ATOM   1323 O O    . ASN   A 1 86  ? 182.846 148.648 116.964 1.00 134.85 ? 99   ASN   A O    1 
ATOM   1324 C CB   . ASN   A 1 86  ? 184.224 145.943 119.135 1.00 126.33 ? 99   ASN   A CB   1 
ATOM   1325 C CG   . ASN   A 1 86  ? 184.940 144.625 118.913 1.00 133.44 ? 99   ASN   A CG   1 
ATOM   1326 O OD1  . ASN   A 1 86  ? 184.767 143.955 117.907 1.00 136.78 ? 99   ASN   A OD1  1 
ATOM   1327 N ND2  . ASN   A 1 86  ? 185.752 144.199 119.849 1.00 134.89 ? 99   ASN   A ND2  1 
ATOM   1328 H H    . ASN   A 1 86  ? 185.604 146.430 116.448 1.00 131.23 ? 99   ASN   A H    1 
ATOM   1329 H HA   . ASN   A 1 86  ? 183.455 146.074 117.154 1.00 130.46 ? 99   ASN   A HA   1 
ATOM   1330 H HB2  . ASN   A 1 86  ? 184.804 146.549 119.832 1.00 130.00 ? 99   ASN   A HB2  1 
ATOM   1331 H HB3  . ASN   A 1 86  ? 183.263 145.709 119.593 1.00 130.55 ? 99   ASN   A HB3  1 
ATOM   1332 H HD21 . ASN   A 1 86  ? 185.896 144.741 120.688 1.00 131.46 ? 99   ASN   A HD21 1 
ATOM   1333 H HD22 . ASN   A 1 86  ? 186.222 143.316 119.707 1.00 131.87 ? 99   ASN   A HD22 1 
ATOM   1334 N N    . ASN   A 1 87  ? 182.645 148.335 119.164 1.00 128.13 ? 100  ASN   A N    1 
ATOM   1335 C CA   . ASN   A 1 87  ? 181.893 149.572 119.383 1.00 128.58 ? 100  ASN   A CA   1 
ATOM   1336 C C    . ASN   A 1 87  ? 182.776 150.820 119.407 1.00 133.85 ? 100  ASN   A C    1 
ATOM   1337 O O    . ASN   A 1 87  ? 182.324 151.887 119.001 1.00 140.77 ? 100  ASN   A O    1 
ATOM   1338 C CB   . ASN   A 1 87  ? 181.122 149.475 120.702 1.00 133.12 ? 100  ASN   A CB   1 
ATOM   1339 C CG   . ASN   A 1 87  ? 180.077 148.384 120.686 1.00 143.18 ? 100  ASN   A CG   1 
ATOM   1340 O OD1  . ASN   A 1 87  ? 180.166 147.398 121.399 1.00 144.31 ? 100  ASN   A OD1  1 
ATOM   1341 N ND2  . ASN   A 1 87  ? 179.062 148.514 119.866 1.00 140.94 ? 100  ASN   A ND2  1 
ATOM   1342 H H    . ASN   A 1 87  ? 182.858 147.750 119.959 1.00 133.20 ? 100  ASN   A H    1 
ATOM   1343 H HA   . ASN   A 1 87  ? 181.179 149.706 118.571 1.00 133.72 ? 100  ASN   A HA   1 
ATOM   1344 H HB2  . ASN   A 1 87  ? 181.813 149.292 121.525 1.00 133.71 ? 100  ASN   A HB2  1 
ATOM   1345 H HB3  . ASN   A 1 87  ? 180.615 150.422 120.887 1.00 133.73 ? 100  ASN   A HB3  1 
ATOM   1346 H HD21 . ASN   A 1 87  ? 178.974 149.331 119.279 1.00 133.94 ? 100  ASN   A HD21 1 
ATOM   1347 H HD22 . ASN   A 1 87  ? 178.372 147.777 119.843 1.00 135.52 ? 100  ASN   A HD22 1 
ATOM   1348 N N    . GLY   A 1 88  ? 184.009 150.718 119.892 1.00 123.87 ? 101  GLY   A N    1 
ATOM   1349 C CA   . GLY   A 1 88  ? 184.919 151.850 120.017 1.00 125.60 ? 101  GLY   A CA   1 
ATOM   1350 C C    . GLY   A 1 88  ? 186.060 151.598 120.994 1.00 123.91 ? 101  GLY   A C    1 
ATOM   1351 O O    . GLY   A 1 88  ? 186.177 150.517 121.567 1.00 128.24 ? 101  GLY   A O    1 
ATOM   1352 H H    . GLY   A 1 88  ? 184.367 149.806 120.138 1.00 124.37 ? 101  GLY   A H    1 
ATOM   1353 H HA2  . GLY   A 1 88  ? 185.344 152.084 119.040 1.00 124.63 ? 101  GLY   A HA2  1 
ATOM   1354 H HA3  . GLY   A 1 88  ? 184.363 152.718 120.370 1.00 125.50 ? 101  GLY   A HA3  1 
ATOM   1355 N N    . ILE   A 1 89  ? 186.871 152.621 121.238 1.00 114.53 ? 102  ILE   A N    1 
ATOM   1356 C CA   . ILE   A 1 89  ? 188.003 152.601 122.162 1.00 115.52 ? 102  ILE   A CA   1 
ATOM   1357 C C    . ILE   A 1 89  ? 188.111 153.904 122.946 1.00 114.39 ? 102  ILE   A C    1 
ATOM   1358 O O    . ILE   A 1 89  ? 187.743 154.972 122.464 1.00 121.95 ? 102  ILE   A O    1 
ATOM   1359 C CB   . ILE   A 1 89  ? 189.324 152.325 121.430 1.00 112.74 ? 102  ILE   A CB   1 
ATOM   1360 C CG1  . ILE   A 1 89  ? 189.644 153.416 120.391 1.00 115.63 ? 102  ILE   A CG1  1 
ATOM   1361 C CG2  . ILE   A 1 89  ? 189.303 150.923 120.821 1.00 116.09 ? 102  ILE   A CG2  1 
ATOM   1362 C CD1  . ILE   A 1 89  ? 190.944 153.181 119.627 1.00 119.95 ? 102  ILE   A CD1  1 
ATOM   1363 H H    . ILE   A 1 89  ? 186.671 153.495 120.773 1.00 116.70 ? 102  ILE   A H    1 
ATOM   1364 H HA   . ILE   A 1 89  ? 187.850 151.802 122.888 1.00 117.06 ? 102  ILE   A HA   1 
ATOM   1365 H HB   . ILE   A 1 89  ? 190.120 152.335 122.175 1.00 115.73 ? 102  ILE   A HB   1 
ATOM   1366 H HG12 . ILE   A 1 89  ? 188.830 153.485 119.669 1.00 116.38 ? 102  ILE   A HG12 1 
ATOM   1367 H HG13 . ILE   A 1 89  ? 189.736 154.378 120.895 1.00 116.45 ? 102  ILE   A HG13 1 
ATOM   1368 H HG21 . ILE   A 1 89  ? 190.311 150.639 120.520 1.00 116.58 ? 102  ILE   A HG21 1 
ATOM   1369 H HG22 . ILE   A 1 89  ? 188.955 150.200 121.559 1.00 116.43 ? 102  ILE   A HG22 1 
ATOM   1370 H HG23 . ILE   A 1 89  ? 188.648 150.893 119.950 1.00 116.96 ? 102  ILE   A HG23 1 
ATOM   1371 H HD11 . ILE   A 1 89  ? 191.133 154.042 118.986 1.00 116.46 ? 102  ILE   A HD11 1 
ATOM   1372 H HD12 . ILE   A 1 89  ? 190.861 152.296 118.996 1.00 117.06 ? 102  ILE   A HD12 1 
ATOM   1373 H HD13 . ILE   A 1 89  ? 191.772 153.062 120.325 1.00 116.74 ? 102  ILE   A HD13 1 
ATOM   1374 N N    . PHE   A 1 90  ? 188.660 153.811 124.150 1.00 109.46 ? 103  PHE   A N    1 
ATOM   1375 C CA   . PHE   A 1 90  ? 189.114 154.945 124.938 1.00 102.11 ? 103  PHE   A CA   1 
ATOM   1376 C C    . PHE   A 1 90  ? 190.635 154.958 124.935 1.00 110.67 ? 103  PHE   A C    1 
ATOM   1377 O O    . PHE   A 1 90  ? 191.240 153.921 125.201 1.00 119.74 ? 103  PHE   A O    1 
ATOM   1378 C CB   . PHE   A 1 90  ? 188.564 154.831 126.358 1.00 104.54 ? 103  PHE   A CB   1 
ATOM   1379 C CG   . PHE   A 1 90  ? 188.983 155.954 127.274 1.00 99.48  ? 103  PHE   A CG   1 
ATOM   1380 C CD1  . PHE   A 1 90  ? 188.531 157.255 127.020 1.00 104.67 ? 103  PHE   A CD1  1 
ATOM   1381 C CD2  . PHE   A 1 90  ? 189.809 155.709 128.380 1.00 104.43 ? 103  PHE   A CD2  1 
ATOM   1382 C CE1  . PHE   A 1 90  ? 188.921 158.313 127.853 1.00 114.15 ? 103  PHE   A CE1  1 
ATOM   1383 C CE2  . PHE   A 1 90  ? 190.195 156.767 129.216 1.00 113.13 ? 103  PHE   A CE2  1 
ATOM   1384 C CZ   . PHE   A 1 90  ? 189.753 158.070 128.951 1.00 116.12 ? 103  PHE   A CZ   1 
ATOM   1385 H H    . PHE   A 1 90  ? 188.918 152.894 124.483 1.00 112.74 ? 103  PHE   A H    1 
ATOM   1386 H HA   . PHE   A 1 90  ? 188.749 155.873 124.498 1.00 109.96 ? 103  PHE   A HA   1 
ATOM   1387 H HB2  . PHE   A 1 90  ? 187.475 154.826 126.311 1.00 111.10 ? 103  PHE   A HB2  1 
ATOM   1388 H HB3  . PHE   A 1 90  ? 188.880 153.879 126.785 1.00 111.16 ? 103  PHE   A HB3  1 
ATOM   1389 H HD1  . PHE   A 1 90  ? 187.887 157.447 126.175 1.00 110.91 ? 103  PHE   A HD1  1 
ATOM   1390 H HD2  . PHE   A 1 90  ? 190.146 154.705 128.592 1.00 110.36 ? 103  PHE   A HD2  1 
ATOM   1391 H HE1  . PHE   A 1 90  ? 188.584 159.317 127.640 1.00 112.77 ? 103  PHE   A HE1  1 
ATOM   1392 H HE2  . PHE   A 1 90  ? 190.837 156.584 130.065 1.00 111.83 ? 103  PHE   A HE2  1 
ATOM   1393 H HZ   . PHE   A 1 90  ? 190.054 158.887 129.590 1.00 112.23 ? 103  PHE   A HZ   1 
ATOM   1394 N N    . SER   A 1 91  ? 191.249 156.099 124.645 1.00 111.22 ? 104  SER   A N    1 
ATOM   1395 C CA   . SER   A 1 91  ? 192.701 156.284 124.650 1.00 108.26 ? 104  SER   A CA   1 
ATOM   1396 C C    . SER   A 1 91  ? 193.142 157.206 125.772 1.00 110.30 ? 104  SER   A C    1 
ATOM   1397 O O    . SER   A 1 91  ? 192.597 158.296 125.910 1.00 128.38 ? 104  SER   A O    1 
ATOM   1398 C CB   . SER   A 1 91  ? 193.202 156.910 123.354 1.00 111.72 ? 104  SER   A CB   1 
ATOM   1399 O OG   . SER   A 1 91  ? 192.817 156.171 122.220 1.00 120.85 ? 104  SER   A OG   1 
ATOM   1400 H H    . SER   A 1 91  ? 190.674 156.904 124.442 1.00 115.30 ? 104  SER   A H    1 
ATOM   1401 H HA   . SER   A 1 91  ? 193.189 155.316 124.760 1.00 115.55 ? 104  SER   A HA   1 
ATOM   1402 H HB2  . SER   A 1 91  ? 192.814 157.925 123.268 1.00 116.07 ? 104  SER   A HB2  1 
ATOM   1403 H HB3  . SER   A 1 91  ? 194.291 156.960 123.387 1.00 115.83 ? 104  SER   A HB3  1 
ATOM   1404 H HG   . SER   A 1 91  ? 193.287 156.535 121.466 1.00 117.47 ? 104  SER   A HG   1 
ATOM   1405 N N    . ARG   A 1 92  ? 194.183 156.831 126.510 1.00 101.70 ? 105  ARG   A N    1 
ATOM   1406 C CA   . ARG   A 1 92  ? 194.931 157.687 127.438 1.00 101.92 ? 105  ARG   A CA   1 
ATOM   1407 C C    . ARG   A 1 92  ? 196.336 157.831 126.879 1.00 116.87 ? 105  ARG   A C    1 
ATOM   1408 O O    . ARG   A 1 92  ? 197.048 156.843 126.741 1.00 131.26 ? 105  ARG   A O    1 
ATOM   1409 C CB   . ARG   A 1 92  ? 194.879 157.037 128.831 1.00 115.78 ? 105  ARG   A CB   1 
ATOM   1410 C CG   . ARG   A 1 92  ? 195.969 157.489 129.812 1.00 116.89 ? 105  ARG   A CG   1 
ATOM   1411 C CD   . ARG   A 1 92  ? 195.775 156.781 131.158 1.00 120.63 ? 105  ARG   A CD   1 
ATOM   1412 N NE   . ARG   A 1 92  ? 197.037 156.666 131.900 1.00 123.57 ? 105  ARG   A NE   1 
ATOM   1413 C CZ   . ARG   A 1 92  ? 197.621 157.583 132.642 1.00 129.93 ? 105  ARG   A CZ   1 
ATOM   1414 N NH1  . ARG   A 1 92  ? 198.736 157.302 133.245 1.00 130.15 ? 105  ARG   A NH1  1 
ATOM   1415 N NH2  . ARG   A 1 92  ? 197.124 158.773 132.818 1.00 123.84 ? 105  ARG   A NH2  1 
ATOM   1416 H H    . ARG   A 1 92  ? 194.573 155.920 126.315 1.00 119.17 ? 105  ARG   A H    1 
ATOM   1417 H HA   . ARG   A 1 92  ? 194.483 158.679 127.496 1.00 118.07 ? 105  ARG   A HA   1 
ATOM   1418 H HB2  . ARG   A 1 92  ? 193.900 157.238 129.265 1.00 119.98 ? 105  ARG   A HB2  1 
ATOM   1419 H HB3  . ARG   A 1 92  ? 194.962 155.956 128.717 1.00 120.16 ? 105  ARG   A HB3  1 
ATOM   1420 H HG2  . ARG   A 1 92  ? 196.945 157.216 129.412 1.00 119.38 ? 105  ARG   A HG2  1 
ATOM   1421 H HG3  . ARG   A 1 92  ? 195.933 158.570 129.949 1.00 119.07 ? 105  ARG   A HG3  1 
ATOM   1422 H HD2  . ARG   A 1 92  ? 195.023 157.303 131.750 1.00 119.69 ? 105  ARG   A HD2  1 
ATOM   1423 H HD3  . ARG   A 1 92  ? 195.405 155.772 130.975 1.00 119.47 ? 105  ARG   A HD3  1 
ATOM   1424 H HE   . ARG   A 1 92  ? 197.514 155.777 131.847 1.00 119.24 ? 105  ARG   A HE   1 
ATOM   1425 H HH11 . ARG   A 1 92  ? 199.155 156.389 133.142 1.00 120.42 ? 105  ARG   A HH11 1 
ATOM   1426 H HH12 . ARG   A 1 92  ? 199.212 158.012 133.782 1.00 120.94 ? 105  ARG   A HH12 1 
ATOM   1427 H HH21 . ARG   A 1 92  ? 196.249 159.029 132.383 1.00 119.33 ? 105  ARG   A HH21 1 
ATOM   1428 H HH22 . ARG   A 1 92  ? 197.625 159.446 133.380 1.00 119.94 ? 105  ARG   A HH22 1 
ATOM   1429 N N    . VAL   A 1 93  ? 196.736 159.042 126.525 1.00 119.75 ? 106  VAL   A N    1 
ATOM   1430 C CA   . VAL   A 1 93  ? 197.912 159.293 125.686 1.00 118.11 ? 106  VAL   A CA   1 
ATOM   1431 C C    . VAL   A 1 93  ? 198.902 160.180 126.409 1.00 119.23 ? 106  VAL   A C    1 
ATOM   1432 O O    . VAL   A 1 93  ? 198.532 161.269 126.833 1.00 124.24 ? 106  VAL   A O    1 
ATOM   1433 C CB   . VAL   A 1 93  ? 197.483 159.954 124.372 1.00 115.14 ? 106  VAL   A CB   1 
ATOM   1434 C CG1  . VAL   A 1 93  ? 198.677 160.121 123.438 1.00 119.39 ? 106  VAL   A CG1  1 
ATOM   1435 C CG2  . VAL   A 1 93  ? 196.416 159.124 123.661 1.00 120.47 ? 106  VAL   A CG2  1 
ATOM   1436 H H    . VAL   A 1 93  ? 196.101 159.814 126.670 1.00 120.21 ? 106  VAL   A H    1 
ATOM   1437 H HA   . VAL   A 1 93  ? 198.409 158.355 125.442 1.00 120.10 ? 106  VAL   A HA   1 
ATOM   1438 H HB   . VAL   A 1 93  ? 197.063 160.939 124.575 1.00 119.31 ? 106  VAL   A HB   1 
ATOM   1439 H HG11 . VAL   A 1 93  ? 199.378 160.847 123.847 1.00 119.66 ? 106  VAL   A HG11 1 
ATOM   1440 H HG12 . VAL   A 1 93  ? 198.336 160.491 122.471 1.00 120.83 ? 106  VAL   A HG12 1 
ATOM   1441 H HG13 . VAL   A 1 93  ? 199.184 159.165 123.304 1.00 120.12 ? 106  VAL   A HG13 1 
ATOM   1442 H HG21 . VAL   A 1 93  ? 195.492 159.128 124.239 1.00 120.75 ? 106  VAL   A HG21 1 
ATOM   1443 H HG22 . VAL   A 1 93  ? 196.764 158.098 123.539 1.00 119.62 ? 106  VAL   A HG22 1 
ATOM   1444 H HG23 . VAL   A 1 93  ? 196.202 159.556 122.684 1.00 120.63 ? 106  VAL   A HG23 1 
ATOM   1445 N N    . LYS   A 1 94  ? 200.157 159.755 126.549 1.00 123.33 ? 107  LYS   A N    1 
ATOM   1446 C CA   . LYS   A 1 94  ? 201.203 160.615 127.106 1.00 123.94 ? 107  LYS   A CA   1 
ATOM   1447 C C    . LYS   A 1 94  ? 201.609 161.646 126.065 1.00 119.67 ? 107  LYS   A C    1 
ATOM   1448 O O    . LYS   A 1 94  ? 201.975 161.278 124.958 1.00 124.33 ? 107  LYS   A O    1 
ATOM   1449 C CB   . LYS   A 1 94  ? 202.399 159.767 127.556 1.00 124.28 ? 107  LYS   A CB   1 
ATOM   1450 C CG   . LYS   A 1 94  ? 203.544 160.635 128.089 1.00 124.91 ? 107  LYS   A CG   1 
ATOM   1451 C CD   . LYS   A 1 94  ? 204.709 159.786 128.603 1.00 129.18 ? 107  LYS   A CD   1 
ATOM   1452 C CE   . LYS   A 1 94  ? 205.904 160.713 128.837 1.00 130.18 ? 107  LYS   A CE   1 
ATOM   1453 N NZ   . LYS   A 1 94  ? 207.117 159.977 129.269 1.00 132.50 ? 107  LYS   A NZ   1 
ATOM   1454 H H    . LYS   A 1 94  ? 200.427 158.881 126.121 1.00 126.48 ? 107  LYS   A H    1 
ATOM   1455 H HA   . LYS   A 1 94  ? 200.813 161.143 127.976 1.00 127.04 ? 107  LYS   A HA   1 
ATOM   1456 H HB2  . LYS   A 1 94  ? 202.076 159.089 128.346 1.00 125.53 ? 107  LYS   A HB2  1 
ATOM   1457 H HB3  . LYS   A 1 94  ? 202.763 159.178 126.713 1.00 126.96 ? 107  LYS   A HB3  1 
ATOM   1458 H HG2  . LYS   A 1 94  ? 203.911 161.272 127.284 1.00 125.67 ? 107  LYS   A HG2  1 
ATOM   1459 H HG3  . LYS   A 1 94  ? 203.176 161.267 128.897 1.00 126.41 ? 107  LYS   A HG3  1 
ATOM   1460 H HD2  . LYS   A 1 94  ? 204.423 159.291 129.531 1.00 126.39 ? 107  LYS   A HD2  1 
ATOM   1461 H HD3  . LYS   A 1 94  ? 204.970 159.038 127.855 1.00 127.18 ? 107  LYS   A HD3  1 
ATOM   1462 H HE2  . LYS   A 1 94  ? 206.113 161.231 127.902 1.00 126.84 ? 107  LYS   A HE2  1 
ATOM   1463 H HE3  . LYS   A 1 94  ? 205.634 161.466 129.577 1.00 126.39 ? 107  LYS   A HE3  1 
ATOM   1464 H HZ1  . LYS   A 1 94  ? 207.933 160.551 129.113 1.00 127.73 ? 107  LYS   A HZ1  1 
ATOM   1465 H HZ2  . LYS   A 1 94  ? 207.073 159.737 130.249 1.00 127.27 ? 107  LYS   A HZ2  1 
ATOM   1466 H HZ3  . LYS   A 1 94  ? 207.253 159.131 128.734 1.00 127.02 ? 107  LYS   A HZ3  1 
ATOM   1467 N N    . ASN   A 1 95  ? 201.609 162.924 126.410 1.00 124.32 ? 108  ASN   A N    1 
ATOM   1468 C CA   . ASN   A 1 95  ? 202.203 163.949 125.566 1.00 127.90 ? 108  ASN   A CA   1 
ATOM   1469 C C    . ASN   A 1 95  ? 203.723 163.943 125.767 1.00 131.51 ? 108  ASN   A C    1 
ATOM   1470 O O    . ASN   A 1 95  ? 204.210 164.425 126.787 1.00 135.40 ? 108  ASN   A O    1 
ATOM   1471 C CB   . ASN   A 1 95  ? 201.568 165.285 125.947 1.00 131.15 ? 108  ASN   A CB   1 
ATOM   1472 C CG   . ASN   A 1 95  ? 202.188 166.459 125.229 1.00 132.67 ? 108  ASN   A CG   1 
ATOM   1473 O OD1  . ASN   A 1 95  ? 202.834 166.334 124.203 1.00 133.96 ? 108  ASN   A OD1  1 
ATOM   1474 N ND2  . ASN   A 1 95  ? 202.016 167.638 125.756 1.00 139.22 ? 108  ASN   A ND2  1 
ATOM   1475 H H    . ASN   A 1 95  ? 201.319 163.175 127.345 1.00 131.69 ? 108  ASN   A H    1 
ATOM   1476 H HA   . ASN   A 1 95  ? 201.990 163.749 124.515 1.00 131.84 ? 108  ASN   A HA   1 
ATOM   1477 H HB2  . ASN   A 1 95  ? 200.502 165.268 125.720 1.00 131.92 ? 108  ASN   A HB2  1 
ATOM   1478 H HB3  . ASN   A 1 95  ? 201.690 165.437 127.020 1.00 132.58 ? 108  ASN   A HB3  1 
ATOM   1479 H HD21 . ASN   A 1 95  ? 201.510 167.704 126.627 1.00 133.49 ? 108  ASN   A HD21 1 
ATOM   1480 H HD22 . ASN   A 1 95  ? 202.474 168.453 125.373 1.00 132.92 ? 108  ASN   A HD22 1 
ATOM   1481 N N    . THR   A 1 96  ? 204.494 163.378 124.840 1.00 135.84 ? 109  THR   A N    1 
ATOM   1482 C CA   . THR   A 1 96  ? 205.950 163.285 124.989 1.00 131.23 ? 109  THR   A CA   1 
ATOM   1483 C C    . THR   A 1 96  ? 206.595 164.625 124.676 1.00 134.65 ? 109  THR   A C    1 
ATOM   1484 O O    . THR   A 1 96  ? 206.907 164.938 123.530 1.00 144.27 ? 109  THR   A O    1 
ATOM   1485 C CB   . THR   A 1 96  ? 206.525 162.163 124.127 1.00 139.08 ? 109  THR   A CB   1 
ATOM   1486 O OG1  . THR   A 1 96  ? 205.913 160.953 124.496 1.00 142.45 ? 109  THR   A OG1  1 
ATOM   1487 C CG2  . THR   A 1 96  ? 208.025 161.971 124.323 1.00 141.10 ? 109  THR   A CG2  1 
ATOM   1488 H H    . THR   A 1 96  ? 204.080 163.004 123.999 1.00 139.05 ? 109  THR   A H    1 
ATOM   1489 H HA   . THR   A 1 96  ? 206.183 163.037 126.024 1.00 137.05 ? 109  THR   A HA   1 
ATOM   1490 H HB   . THR   A 1 96  ? 206.323 162.358 123.074 1.00 139.41 ? 109  THR   A HB   1 
ATOM   1491 H HG1  . THR   A 1 96  ? 206.492 160.478 125.097 1.00 139.48 ? 109  THR   A HG1  1 
ATOM   1492 H HG21 . THR   A 1 96  ? 208.359 161.095 123.767 1.00 139.28 ? 109  THR   A HG21 1 
ATOM   1493 H HG22 . THR   A 1 96  ? 208.561 162.840 123.943 1.00 138.90 ? 109  THR   A HG22 1 
ATOM   1494 H HG23 . THR   A 1 96  ? 208.257 161.839 125.380 1.00 138.97 ? 109  THR   A HG23 1 
ATOM   1495 N N    . LYS   A 1 97  ? 206.766 165.447 125.708 1.00 128.36 ? 110  LYS   A N    1 
ATOM   1496 C CA   . LYS   A 1 97  ? 207.385 166.770 125.624 1.00 134.10 ? 110  LYS   A CA   1 
ATOM   1497 C C    . LYS   A 1 97  ? 208.898 166.636 125.437 1.00 135.43 ? 110  LYS   A C    1 
ATOM   1498 O O    . LYS   A 1 97  ? 209.590 166.171 126.337 1.00 137.28 ? 110  LYS   A O    1 
ATOM   1499 C CB   . LYS   A 1 97  ? 206.996 167.558 126.887 1.00 130.49 ? 110  LYS   A CB   1 
ATOM   1500 C CG   . LYS   A 1 97  ? 205.519 167.995 126.822 1.00 128.76 ? 110  LYS   A CG   1 
ATOM   1501 C CD   . LYS   A 1 97  ? 204.773 167.991 128.164 1.00 127.19 ? 110  LYS   A CD   1 
ATOM   1502 C CE   . LYS   A 1 97  ? 205.463 168.816 129.252 1.00 130.83 ? 110  LYS   A CE   1 
ATOM   1503 N NZ   . LYS   A 1 97  ? 204.607 168.944 130.460 1.00 140.04 ? 110  LYS   A NZ   1 
ATOM   1504 H H    . LYS   A 1 97  ? 206.403 165.149 126.602 1.00 133.01 ? 110  LYS   A H    1 
ATOM   1505 H HA   . LYS   A 1 97  ? 206.994 167.299 124.755 1.00 133.87 ? 110  LYS   A HA   1 
ATOM   1506 H HB2  . LYS   A 1 97  ? 207.168 166.935 127.764 1.00 133.03 ? 110  LYS   A HB2  1 
ATOM   1507 H HB3  . LYS   A 1 97  ? 207.619 168.448 126.972 1.00 132.70 ? 110  LYS   A HB3  1 
ATOM   1508 H HG2  . LYS   A 1 97  ? 205.471 168.993 126.388 1.00 133.03 ? 110  LYS   A HG2  1 
ATOM   1509 H HG3  . LYS   A 1 97  ? 204.971 167.331 126.153 1.00 133.12 ? 110  LYS   A HG3  1 
ATOM   1510 H HD2  . LYS   A 1 97  ? 203.773 168.389 127.991 1.00 132.92 ? 110  LYS   A HD2  1 
ATOM   1511 H HD3  . LYS   A 1 97  ? 204.674 166.961 128.506 1.00 132.86 ? 110  LYS   A HD3  1 
ATOM   1512 H HE2  . LYS   A 1 97  ? 206.405 168.331 129.510 1.00 133.13 ? 110  LYS   A HE2  1 
ATOM   1513 H HE3  . LYS   A 1 97  ? 205.694 169.804 128.853 1.00 133.00 ? 110  LYS   A HE3  1 
ATOM   1514 H HZ1  . LYS   A 1 97  ? 204.302 168.051 130.821 1.00 134.83 ? 110  LYS   A HZ1  1 
ATOM   1515 H HZ2  . LYS   A 1 97  ? 205.099 169.414 131.206 1.00 134.82 ? 110  LYS   A HZ2  1 
ATOM   1516 H HZ3  . LYS   A 1 97  ? 203.769 169.472 130.264 1.00 134.62 ? 110  LYS   A HZ3  1 
ATOM   1517 N N    . LEU   A 1 98  ? 209.408 167.034 124.276 1.00 147.53 ? 111  LEU   A N    1 
ATOM   1518 C CA   . LEU   A 1 98  ? 210.836 167.108 123.946 1.00 144.60 ? 111  LEU   A CA   1 
ATOM   1519 C C    . LEU   A 1 98  ? 211.337 168.551 123.946 1.00 147.33 ? 111  LEU   A C    1 
ATOM   1520 O O    . LEU   A 1 98  ? 210.543 169.487 123.890 1.00 151.57 ? 111  LEU   A O    1 
ATOM   1521 C CB   . LEU   A 1 98  ? 211.088 166.466 122.571 1.00 144.48 ? 111  LEU   A CB   1 
ATOM   1522 C CG   . LEU   A 1 98  ? 210.640 165.004 122.462 1.00 148.96 ? 111  LEU   A CG   1 
ATOM   1523 C CD1  . LEU   A 1 98  ? 211.051 164.459 121.098 1.00 147.34 ? 111  LEU   A CD1  1 
ATOM   1524 C CD2  . LEU   A 1 98  ? 211.282 164.141 123.543 1.00 149.64 ? 111  LEU   A CD2  1 
ATOM   1525 H H    . LEU   A 1 98  ? 208.761 167.423 123.605 1.00 147.04 ? 111  LEU   A H    1 
ATOM   1526 H HA   . LEU   A 1 98  ? 211.418 166.576 124.698 1.00 146.80 ? 111  LEU   A HA   1 
ATOM   1527 H HB2  . LEU   A 1 98  ? 210.562 167.045 121.813 1.00 147.05 ? 111  LEU   A HB2  1 
ATOM   1528 H HB3  . LEU   A 1 98  ? 212.154 166.515 122.352 1.00 146.35 ? 111  LEU   A HB3  1 
ATOM   1529 H HG   . LEU   A 1 98  ? 209.556 164.941 122.549 1.00 147.58 ? 111  LEU   A HG   1 
ATOM   1530 H HD11 . LEU   A 1 98  ? 210.627 165.081 120.309 1.00 147.24 ? 111  LEU   A HD11 1 
ATOM   1531 H HD12 . LEU   A 1 98  ? 212.138 164.446 121.011 1.00 147.00 ? 111  LEU   A HD12 1 
ATOM   1532 H HD13 . LEU   A 1 98  ? 210.671 163.444 120.983 1.00 147.32 ? 111  LEU   A HD13 1 
ATOM   1533 H HD21 . LEU   A 1 98  ? 210.959 164.467 124.531 1.00 147.48 ? 111  LEU   A HD21 1 
ATOM   1534 H HD22 . LEU   A 1 98  ? 210.957 163.107 123.423 1.00 147.44 ? 111  LEU   A HD22 1 
ATOM   1535 H HD23 . LEU   A 1 98  ? 212.369 164.190 123.476 1.00 147.36 ? 111  LEU   A HD23 1 
ATOM   1536 N N    . TYR   A 1 99  ? 212.656 168.737 123.943 1.00 142.59 ? 112  TYR   A N    1 
ATOM   1537 C CA   . TYR   A 1 99  ? 213.276 170.060 123.886 1.00 146.53 ? 112  TYR   A CA   1 
ATOM   1538 C C    . TYR   A 1 99  ? 214.382 170.147 122.838 1.00 144.89 ? 112  TYR   A C    1 
ATOM   1539 O O    . TYR   A 1 99  ? 215.213 169.246 122.726 1.00 144.74 ? 112  TYR   A O    1 
ATOM   1540 C CB   . TYR   A 1 99  ? 213.813 170.459 125.263 1.00 146.26 ? 112  TYR   A CB   1 
ATOM   1541 C CG   . TYR   A 1 99  ? 212.748 170.546 126.333 1.00 147.97 ? 112  TYR   A CG   1 
ATOM   1542 C CD1  . TYR   A 1 99  ? 211.997 171.725 126.477 1.00 145.63 ? 112  TYR   A CD1  1 
ATOM   1543 C CD2  . TYR   A 1 99  ? 212.504 169.447 127.175 1.00 144.34 ? 112  TYR   A CD2  1 
ATOM   1544 C CE1  . TYR   A 1 99  ? 211.002 171.808 127.466 1.00 144.10 ? 112  TYR   A CE1  1 
ATOM   1545 C CE2  . TYR   A 1 99  ? 211.505 169.523 128.160 1.00 143.60 ? 112  TYR   A CE2  1 
ATOM   1546 C CZ   . TYR   A 1 99  ? 210.753 170.706 128.307 1.00 146.67 ? 112  TYR   A CZ   1 
ATOM   1547 O OH   . TYR   A 1 99  ? 209.801 170.792 129.269 1.00 151.44 ? 112  TYR   A OH   1 
ATOM   1548 H H    . TYR   A 1 99  ? 213.264 167.930 123.974 1.00 144.29 ? 112  TYR   A H    1 
ATOM   1549 H HA   . TYR   A 1 99  ? 212.512 170.789 123.614 1.00 145.57 ? 112  TYR   A HA   1 
ATOM   1550 H HB2  . TYR   A 1 99  ? 214.573 169.741 125.572 1.00 145.01 ? 112  TYR   A HB2  1 
ATOM   1551 H HB3  . TYR   A 1 99  ? 214.297 171.432 125.182 1.00 144.80 ? 112  TYR   A HB3  1 
ATOM   1552 H HD1  . TYR   A 1 99  ? 212.183 172.568 125.828 1.00 144.97 ? 112  TYR   A HD1  1 
ATOM   1553 H HD2  . TYR   A 1 99  ? 213.081 168.540 127.063 1.00 144.88 ? 112  TYR   A HD2  1 
ATOM   1554 H HE1  . TYR   A 1 99  ? 210.428 172.713 127.593 1.00 145.01 ? 112  TYR   A HE1  1 
ATOM   1555 H HE2  . TYR   A 1 99  ? 211.316 168.677 128.805 1.00 144.83 ? 112  TYR   A HE2  1 
ATOM   1556 H HH   . TYR   A 1 99  ? 209.801 170.013 129.830 1.00 146.09 ? 112  TYR   A HH   1 
ATOM   1557 N N    . VAL   A 1 100 ? 214.428 171.261 122.107 1.00 154.29 ? 113  VAL   A N    1 
ATOM   1558 C CA   . VAL   A 1 100 ? 215.545 171.632 121.223 1.00 158.22 ? 113  VAL   A CA   1 
ATOM   1559 C C    . VAL   A 1 100 ? 215.922 173.083 121.510 1.00 160.31 ? 113  VAL   A C    1 
ATOM   1560 O O    . VAL   A 1 100 ? 215.056 173.952 121.474 1.00 159.85 ? 113  VAL   A O    1 
ATOM   1561 C CB   . VAL   A 1 100 ? 215.182 171.432 119.738 1.00 156.80 ? 113  VAL   A CB   1 
ATOM   1562 C CG1  . VAL   A 1 100 ? 216.354 171.804 118.825 1.00 155.52 ? 113  VAL   A CG1  1 
ATOM   1563 C CG2  . VAL   A 1 100 ? 214.796 169.980 119.434 1.00 156.03 ? 113  VAL   A CG2  1 
ATOM   1564 H H    . VAL   A 1 100 ? 213.699 171.945 122.248 1.00 155.45 ? 113  VAL   A H    1 
ATOM   1565 H HA   . VAL   A 1 100 ? 216.410 171.008 121.444 1.00 156.17 ? 113  VAL   A HA   1 
ATOM   1566 H HB   . VAL   A 1 100 ? 214.337 172.071 119.483 1.00 155.95 ? 113  VAL   A HB   1 
ATOM   1567 H HG11 . VAL   A 1 100 ? 216.591 172.863 118.923 1.00 156.07 ? 113  VAL   A HG11 1 
ATOM   1568 H HG12 . VAL   A 1 100 ? 216.083 171.615 117.786 1.00 156.19 ? 113  VAL   A HG12 1 
ATOM   1569 H HG13 . VAL   A 1 100 ? 217.232 171.209 119.078 1.00 156.11 ? 113  VAL   A HG13 1 
ATOM   1570 H HG21 . VAL   A 1 100 ? 213.902 169.704 119.994 1.00 156.17 ? 113  VAL   A HG21 1 
ATOM   1571 H HG22 . VAL   A 1 100 ? 215.617 169.315 119.700 1.00 156.33 ? 113  VAL   A HG22 1 
ATOM   1572 H HG23 . VAL   A 1 100 ? 214.576 169.872 118.372 1.00 155.83 ? 113  VAL   A HG23 1 
ATOM   1573 N N    . ASN   A 1 101 ? 217.191 173.360 121.824 1.00 168.20 ? 114  ASN   A N    1 
ATOM   1574 C CA   . ASN   A 1 101 ? 217.671 174.695 122.223 1.00 168.56 ? 114  ASN   A CA   1 
ATOM   1575 C C    . ASN   A 1 101 ? 216.742 175.383 123.254 1.00 167.90 ? 114  ASN   A C    1 
ATOM   1576 O O    . ASN   A 1 101 ? 216.331 176.532 123.082 1.00 166.64 ? 114  ASN   A O    1 
ATOM   1577 C CB   . ASN   A 1 101 ? 217.974 175.551 120.975 1.00 167.73 ? 114  ASN   A CB   1 
ATOM   1578 C CG   . ASN   A 1 101 ? 219.073 174.985 120.094 1.00 167.98 ? 114  ASN   A CG   1 
ATOM   1579 O OD1  . ASN   A 1 101 ? 219.932 174.229 120.524 1.00 167.73 ? 114  ASN   A OD1  1 
ATOM   1580 N ND2  . ASN   A 1 101 ? 219.093 175.339 118.830 1.00 164.22 ? 114  ASN   A ND2  1 
ATOM   1581 H H    . ASN   A 1 101 ? 217.863 172.607 121.810 1.00 165.06 ? 114  ASN   A H    1 
ATOM   1582 H HA   . ASN   A 1 101 ? 218.616 174.554 122.749 1.00 165.46 ? 114  ASN   A HA   1 
ATOM   1583 H HB2  . ASN   A 1 101 ? 217.063 175.659 120.386 1.00 165.51 ? 114  ASN   A HB2  1 
ATOM   1584 H HB3  . ASN   A 1 101 ? 218.291 176.546 121.287 1.00 165.41 ? 114  ASN   A HB3  1 
ATOM   1585 H HD21 . ASN   A 1 101 ? 218.396 175.974 118.468 1.00 164.98 ? 114  ASN   A HD21 1 
ATOM   1586 H HD22 . ASN   A 1 101 ? 219.825 174.972 118.239 1.00 164.85 ? 114  ASN   A HD22 1 
ATOM   1587 N N    . LYS   A 1 102 ? 216.348 174.639 124.298 1.00 162.12 ? 115  LYS   A N    1 
ATOM   1588 C CA   . LYS   A 1 102 ? 215.370 175.008 125.348 1.00 160.53 ? 115  LYS   A CA   1 
ATOM   1589 C C    . LYS   A 1 102 ? 213.934 175.314 124.884 1.00 160.73 ? 115  LYS   A C    1 
ATOM   1590 O O    . LYS   A 1 102 ? 213.073 175.552 125.728 1.00 160.11 ? 115  LYS   A O    1 
ATOM   1591 C CB   . LYS   A 1 102 ? 215.916 176.139 126.243 1.00 159.91 ? 115  LYS   A CB   1 
ATOM   1592 C CG   . LYS   A 1 102 ? 217.220 175.770 126.963 1.00 160.64 ? 115  LYS   A CG   1 
ATOM   1593 C CD   . LYS   A 1 102 ? 217.680 176.930 127.851 1.00 161.09 ? 115  LYS   A CD   1 
ATOM   1594 C CE   . LYS   A 1 102 ? 218.996 176.566 128.542 1.00 163.52 ? 115  LYS   A CE   1 
ATOM   1595 N NZ   . LYS   A 1 102 ? 219.469 177.665 129.417 1.00 163.36 ? 115  LYS   A NZ   1 
ATOM   1596 H H    . LYS   A 1 102 ? 216.750 173.714 124.355 1.00 159.98 ? 115  LYS   A H    1 
ATOM   1597 H HA   . LYS   A 1 102 ? 215.255 174.137 125.993 1.00 159.59 ? 115  LYS   A HA   1 
ATOM   1598 H HB2  . LYS   A 1 102 ? 216.076 177.036 125.645 1.00 160.14 ? 115  LYS   A HB2  1 
ATOM   1599 H HB3  . LYS   A 1 102 ? 215.174 176.376 127.005 1.00 160.04 ? 115  LYS   A HB3  1 
ATOM   1600 H HG2  . LYS   A 1 102 ? 217.055 174.885 127.578 1.00 160.27 ? 115  LYS   A HG2  1 
ATOM   1601 H HG3  . LYS   A 1 102 ? 217.997 175.555 126.229 1.00 160.28 ? 115  LYS   A HG3  1 
ATOM   1602 H HD2  . LYS   A 1 102 ? 217.825 177.818 127.236 1.00 160.18 ? 115  LYS   A HD2  1 
ATOM   1603 H HD3  . LYS   A 1 102 ? 216.916 177.135 128.601 1.00 160.17 ? 115  LYS   A HD3  1 
ATOM   1604 H HE2  . LYS   A 1 102 ? 218.843 175.661 129.130 1.00 160.71 ? 115  LYS   A HE2  1 
ATOM   1605 H HE3  . LYS   A 1 102 ? 219.743 176.349 127.779 1.00 160.61 ? 115  LYS   A HE3  1 
ATOM   1606 H HZ1  . LYS   A 1 102 ? 220.337 177.419 129.871 1.00 160.44 ? 115  LYS   A HZ1  1 
ATOM   1607 H HZ2  . LYS   A 1 102 ? 219.627 178.510 128.887 1.00 160.54 ? 115  LYS   A HZ2  1 
ATOM   1608 H HZ3  . LYS   A 1 102 ? 218.792 177.872 130.139 1.00 160.65 ? 115  LYS   A HZ3  1 
ATOM   1609 N N    . THR   A 1 103 ? 213.629 175.275 123.589 1.00 154.19 ? 116  THR   A N    1 
ATOM   1610 C CA   . THR   A 1 103 ? 212.249 175.361 123.081 1.00 153.71 ? 116  THR   A CA   1 
ATOM   1611 C C    . THR   A 1 103 ? 211.542 174.016 123.216 1.00 151.52 ? 116  THR   A C    1 
ATOM   1612 O O    . THR   A 1 103 ? 212.126 172.984 122.894 1.00 150.05 ? 116  THR   A O    1 
ATOM   1613 C CB   . THR   A 1 103 ? 212.238 175.822 121.620 1.00 153.72 ? 116  THR   A CB   1 
ATOM   1614 O OG1  . THR   A 1 103 ? 212.790 177.117 121.552 1.00 154.58 ? 116  THR   A OG1  1 
ATOM   1615 C CG2  . THR   A 1 103 ? 210.837 175.909 121.020 1.00 151.23 ? 116  THR   A CG2  1 
ATOM   1616 H H    . THR   A 1 103 ? 214.356 175.018 122.937 1.00 152.73 ? 116  THR   A H    1 
ATOM   1617 H HA   . THR   A 1 103 ? 211.695 176.097 123.663 1.00 152.28 ? 116  THR   A HA   1 
ATOM   1618 H HB   . THR   A 1 103 ? 212.835 175.143 121.011 1.00 152.33 ? 116  THR   A HB   1 
ATOM   1619 H HG1  . THR   A 1 103 ? 213.701 177.052 121.847 1.00 152.34 ? 116  THR   A HG1  1 
ATOM   1620 H HG21 . THR   A 1 103 ? 210.893 176.359 120.029 1.00 152.00 ? 116  THR   A HG21 1 
ATOM   1621 H HG22 . THR   A 1 103 ? 210.192 176.516 121.656 1.00 151.92 ? 116  THR   A HG22 1 
ATOM   1622 H HG23 . THR   A 1 103 ? 210.411 174.911 120.914 1.00 151.62 ? 116  THR   A HG23 1 
ATOM   1623 N N    . LEU   A 1 104 ? 210.295 174.014 123.685 1.00 139.74 ? 117  LEU   A N    1 
ATOM   1624 C CA   . LEU   A 1 104 ? 209.479 172.809 123.840 1.00 139.86 ? 117  LEU   A CA   1 
ATOM   1625 C C    . LEU   A 1 104 ? 208.851 172.357 122.517 1.00 143.80 ? 117  LEU   A C    1 
ATOM   1626 O O    . LEU   A 1 104 ? 208.376 173.186 121.744 1.00 142.63 ? 117  LEU   A O    1 
ATOM   1627 C CB   . LEU   A 1 104 ? 208.411 173.093 124.907 1.00 140.36 ? 117  LEU   A CB   1 
ATOM   1628 C CG   . LEU   A 1 104 ? 207.487 171.899 125.216 1.00 142.99 ? 117  LEU   A CG   1 
ATOM   1629 C CD1  . LEU   A 1 104 ? 207.118 171.898 126.696 1.00 144.89 ? 117  LEU   A CD1  1 
ATOM   1630 C CD2  . LEU   A 1 104 ? 206.171 171.965 124.440 1.00 140.97 ? 117  LEU   A CD2  1 
ATOM   1631 H H    . LEU   A 1 104 ? 209.867 174.899 123.915 1.00 141.64 ? 117  LEU   A H    1 
ATOM   1632 H HA   . LEU   A 1 104 ? 210.114 172.002 124.206 1.00 141.85 ? 117  LEU   A HA   1 
ATOM   1633 H HB2  . LEU   A 1 104 ? 208.937 173.375 125.819 1.00 141.64 ? 117  LEU   A HB2  1 
ATOM   1634 H HB3  . LEU   A 1 104 ? 207.806 173.947 124.604 1.00 141.41 ? 117  LEU   A HB3  1 
ATOM   1635 H HG   . LEU   A 1 104 ? 207.999 170.963 124.993 1.00 141.75 ? 117  LEU   A HG   1 
ATOM   1636 H HD11 . LEU   A 1 104 ? 208.019 171.773 127.297 1.00 142.16 ? 117  LEU   A HD11 1 
ATOM   1637 H HD12 . LEU   A 1 104 ? 206.440 171.072 126.909 1.00 141.62 ? 117  LEU   A HD12 1 
ATOM   1638 H HD13 . LEU   A 1 104 ? 206.635 172.839 126.962 1.00 142.30 ? 117  LEU   A HD13 1 
ATOM   1639 H HD21 . LEU   A 1 104 ? 206.352 171.980 123.365 1.00 141.51 ? 117  LEU   A HD21 1 
ATOM   1640 H HD22 . LEU   A 1 104 ? 205.561 171.093 124.675 1.00 141.45 ? 117  LEU   A HD22 1 
ATOM   1641 H HD23 . LEU   A 1 104 ? 205.621 172.865 124.714 1.00 141.83 ? 117  LEU   A HD23 1 
ATOM   1642 N N    . TYR   A 1 105 ? 208.758 171.044 122.307 1.00 149.66 ? 118  TYR   A N    1 
ATOM   1643 C CA   . TYR   A 1 105 ? 207.994 170.414 121.230 1.00 144.87 ? 118  TYR   A CA   1 
ATOM   1644 C C    . TYR   A 1 105 ? 207.174 169.233 121.749 1.00 142.26 ? 118  TYR   A C    1 
ATOM   1645 O O    . TYR   A 1 105 ? 207.628 168.487 122.609 1.00 144.21 ? 118  TYR   A O    1 
ATOM   1646 C CB   . TYR   A 1 105 ? 208.924 169.922 120.125 1.00 144.69 ? 118  TYR   A CB   1 
ATOM   1647 C CG   . TYR   A 1 105 ? 209.648 171.010 119.364 1.00 147.59 ? 118  TYR   A CG   1 
ATOM   1648 C CD1  . TYR   A 1 105 ? 210.829 171.570 119.881 1.00 149.82 ? 118  TYR   A CD1  1 
ATOM   1649 C CD2  . TYR   A 1 105 ? 209.132 171.468 118.139 1.00 144.59 ? 118  TYR   A CD2  1 
ATOM   1650 C CE1  . TYR   A 1 105 ? 211.477 172.606 119.188 1.00 151.54 ? 118  TYR   A CE1  1 
ATOM   1651 C CE2  . TYR   A 1 105 ? 209.786 172.495 117.436 1.00 146.31 ? 118  TYR   A CE2  1 
ATOM   1652 C CZ   . TYR   A 1 105 ? 210.958 173.071 117.965 1.00 150.60 ? 118  TYR   A CZ   1 
ATOM   1653 O OH   . TYR   A 1 105 ? 211.585 174.078 117.305 1.00 151.10 ? 118  TYR   A OH   1 
ATOM   1654 H H    . TYR   A 1 105 ? 209.201 170.429 122.974 1.00 147.07 ? 118  TYR   A H    1 
ATOM   1655 H HA   . TYR   A 1 105 ? 207.306 171.141 120.799 1.00 146.48 ? 118  TYR   A HA   1 
ATOM   1656 H HB2  . TYR   A 1 105 ? 209.656 169.235 120.548 1.00 146.43 ? 118  TYR   A HB2  1 
ATOM   1657 H HB3  . TYR   A 1 105 ? 208.311 169.359 119.422 1.00 146.85 ? 118  TYR   A HB3  1 
ATOM   1658 H HD1  . TYR   A 1 105 ? 211.225 171.224 120.824 1.00 147.12 ? 118  TYR   A HD1  1 
ATOM   1659 H HD2  . TYR   A 1 105 ? 208.232 171.028 117.735 1.00 146.39 ? 118  TYR   A HD2  1 
ATOM   1660 H HE1  . TYR   A 1 105 ? 212.364 173.068 119.597 1.00 147.72 ? 118  TYR   A HE1  1 
ATOM   1661 H HE2  . TYR   A 1 105 ? 209.386 172.846 116.496 1.00 146.88 ? 118  TYR   A HE2  1 
ATOM   1662 H HH   . TYR   A 1 105 ? 211.128 174.301 116.491 1.00 147.27 ? 118  TYR   A HH   1 
ATOM   1663 N N    . SER   A 1 106 ? 205.979 169.031 121.209 1.00 137.70 ? 119  SER   A N    1 
ATOM   1664 C CA   . SER   A 1 106 ? 205.058 167.959 121.591 1.00 142.30 ? 119  SER   A CA   1 
ATOM   1665 C C    . SER   A 1 106 ? 204.988 166.875 120.516 1.00 140.53 ? 119  SER   A C    1 
ATOM   1666 O O    . SER   A 1 106 ? 204.689 167.173 119.364 1.00 145.59 ? 119  SER   A O    1 
ATOM   1667 C CB   . SER   A 1 106 ? 203.683 168.586 121.824 1.00 145.85 ? 119  SER   A CB   1 
ATOM   1668 O OG   . SER   A 1 106 ? 202.663 167.613 121.909 1.00 150.21 ? 119  SER   A OG   1 
ATOM   1669 H H    . SER   A 1 106 ? 205.669 169.683 120.503 1.00 143.23 ? 119  SER   A H    1 
ATOM   1670 H HA   . SER   A 1 106 ? 205.382 167.499 122.525 1.00 143.44 ? 119  SER   A HA   1 
ATOM   1671 H HB2  . SER   A 1 106 ? 203.705 169.175 122.741 1.00 143.09 ? 119  SER   A HB2  1 
ATOM   1672 H HB3  . SER   A 1 106 ? 203.450 169.250 120.992 1.00 143.95 ? 119  SER   A HB3  1 
ATOM   1673 H HG   . SER   A 1 106 ? 202.779 167.124 122.727 1.00 144.17 ? 119  SER   A HG   1 
ATOM   1674 N N    . GLU   A 1 107 ? 205.220 165.616 120.881 1.00 140.22 ? 120  GLU   A N    1 
ATOM   1675 C CA   . GLU   A 1 107 ? 205.073 164.445 120.006 1.00 137.50 ? 120  GLU   A CA   1 
ATOM   1676 C C    . GLU   A 1 107 ? 204.147 163.408 120.662 1.00 141.19 ? 120  GLU   A C    1 
ATOM   1677 O O    . GLU   A 1 107 ? 204.202 163.232 121.875 1.00 152.71 ? 120  GLU   A O    1 
ATOM   1678 C CB   . GLU   A 1 107 ? 206.444 163.786 119.753 1.00 141.81 ? 120  GLU   A CB   1 
ATOM   1679 C CG   . GLU   A 1 107 ? 207.577 164.674 119.202 1.00 149.16 ? 120  GLU   A CG   1 
ATOM   1680 C CD   . GLU   A 1 107 ? 207.438 165.088 117.722 1.00 157.59 ? 120  GLU   A CD   1 
ATOM   1681 O OE1  . GLU   A 1 107 ? 206.390 164.804 117.101 1.00 156.15 ? 120  GLU   A OE1  1 
ATOM   1682 O OE2  . GLU   A 1 107 ? 208.401 165.689 117.175 1.00 160.02 ? 120  GLU   A OE2  1 
ATOM   1683 H H    . GLU   A 1 107 ? 205.493 165.430 121.835 1.00 147.11 ? 120  GLU   A H    1 
ATOM   1684 H HA   . GLU   A 1 107 ? 204.638 164.736 119.050 1.00 146.24 ? 120  GLU   A HA   1 
ATOM   1685 H HB2  . GLU   A 1 107 ? 206.797 163.384 120.703 1.00 146.84 ? 120  GLU   A HB2  1 
ATOM   1686 H HB3  . GLU   A 1 107 ? 206.311 162.934 119.085 1.00 146.63 ? 120  GLU   A HB3  1 
ATOM   1687 H HG2  . GLU   A 1 107 ? 207.680 165.564 119.824 1.00 147.36 ? 120  GLU   A HG2  1 
ATOM   1688 H HG3  . GLU   A 1 107 ? 208.503 164.108 119.307 1.00 147.35 ? 120  GLU   A HG3  1 
ATOM   1689 N N    . PHE   A 1 108 ? 203.344 162.670 119.894 1.00 120.02 ? 121  PHE   A N    1 
ATOM   1690 C CA   . PHE   A 1 108 ? 202.747 161.395 120.322 1.00 121.04 ? 121  PHE   A CA   1 
ATOM   1691 C C    . PHE   A 1 108 ? 202.269 160.570 119.120 1.00 121.96 ? 121  PHE   A C    1 
ATOM   1692 O O    . PHE   A 1 108 ? 202.190 161.076 118.003 1.00 126.11 ? 121  PHE   A O    1 
ATOM   1693 C CB   . PHE   A 1 108 ? 201.623 161.592 121.347 1.00 120.47 ? 121  PHE   A CB   1 
ATOM   1694 C CG   . PHE   A 1 108 ? 200.458 162.458 120.937 1.00 120.06 ? 121  PHE   A CG   1 
ATOM   1695 C CD1  . PHE   A 1 108 ? 199.354 161.890 120.284 1.00 120.52 ? 121  PHE   A CD1  1 
ATOM   1696 C CD2  . PHE   A 1 108 ? 200.439 163.814 121.291 1.00 121.06 ? 121  PHE   A CD2  1 
ATOM   1697 C CE1  . PHE   A 1 108 ? 198.224 162.671 120.002 1.00 122.04 ? 121  PHE   A CE1  1 
ATOM   1698 C CE2  . PHE   A 1 108 ? 199.304 164.591 121.021 1.00 122.25 ? 121  PHE   A CE2  1 
ATOM   1699 C CZ   . PHE   A 1 108 ? 198.194 164.019 120.385 1.00 122.12 ? 121  PHE   A CZ   1 
ATOM   1700 H H    . PHE   A 1 108 ? 203.301 162.871 118.905 1.00 123.80 ? 121  PHE   A H    1 
ATOM   1701 H HA   . PHE   A 1 108 ? 203.527 160.810 120.810 1.00 123.62 ? 121  PHE   A HA   1 
ATOM   1702 H HB2  . PHE   A 1 108 ? 201.234 160.612 121.626 1.00 122.70 ? 121  PHE   A HB2  1 
ATOM   1703 H HB3  . PHE   A 1 108 ? 202.047 162.007 122.261 1.00 124.68 ? 121  PHE   A HB3  1 
ATOM   1704 H HD1  . PHE   A 1 108 ? 199.359 160.843 120.019 1.00 122.55 ? 121  PHE   A HD1  1 
ATOM   1705 H HD2  . PHE   A 1 108 ? 201.285 164.253 121.799 1.00 123.54 ? 121  PHE   A HD2  1 
ATOM   1706 H HE1  . PHE   A 1 108 ? 197.369 162.232 119.509 1.00 123.31 ? 121  PHE   A HE1  1 
ATOM   1707 H HE2  . PHE   A 1 108 ? 199.277 165.630 121.315 1.00 123.02 ? 121  PHE   A HE2  1 
ATOM   1708 H HZ   . PHE   A 1 108 ? 197.318 164.619 120.187 1.00 122.95 ? 121  PHE   A HZ   1 
ATOM   1709 N N    . SER   A 1 109 ? 201.987 159.282 119.313 1.00 120.86 ? 122  SER   A N    1 
ATOM   1710 C CA   . SER   A 1 109 ? 201.642 158.371 118.217 1.00 126.16 ? 122  SER   A CA   1 
ATOM   1711 C C    . SER   A 1 109 ? 200.373 158.776 117.463 1.00 126.30 ? 122  SER   A C    1 
ATOM   1712 O O    . SER   A 1 109 ? 199.356 159.103 118.065 1.00 123.97 ? 122  SER   A O    1 
ATOM   1713 C CB   . SER   A 1 109 ? 201.451 156.949 118.744 1.00 125.75 ? 122  SER   A CB   1 
ATOM   1714 O OG   . SER   A 1 109 ? 202.618 156.499 119.405 1.00 127.32 ? 122  SER   A OG   1 
ATOM   1715 H H    . SER   A 1 109 ? 202.092 158.888 120.237 1.00 124.16 ? 122  SER   A H    1 
ATOM   1716 H HA   . SER   A 1 109 ? 202.471 158.361 117.509 1.00 125.22 ? 122  SER   A HA   1 
ATOM   1717 H HB2  . SER   A 1 109 ? 200.615 156.932 119.444 1.00 125.14 ? 122  SER   A HB2  1 
ATOM   1718 H HB3  . SER   A 1 109 ? 201.224 156.283 117.912 1.00 125.62 ? 122  SER   A HB3  1 
ATOM   1719 H HG   . SER   A 1 109 ? 203.291 156.334 118.740 1.00 124.97 ? 122  SER   A HG   1 
ATOM   1720 N N    . THR   A 1 110 ? 200.403 158.681 116.135 1.00 123.47 ? 123  THR   A N    1 
ATOM   1721 C CA   . THR   A 1 110 ? 199.197 158.755 115.294 1.00 122.34 ? 123  THR   A CA   1 
ATOM   1722 C C    . THR   A 1 110 ? 198.366 157.492 115.444 1.00 120.65 ? 123  THR   A C    1 
ATOM   1723 O O    . THR   A 1 110 ? 198.932 156.406 115.499 1.00 124.42 ? 123  THR   A O    1 
ATOM   1724 C CB   . THR   A 1 110 ? 199.604 158.914 113.829 1.00 126.23 ? 123  THR   A CB   1 
ATOM   1725 O OG1  . THR   A 1 110 ? 200.133 160.200 113.668 1.00 129.21 ? 123  THR   A OG1  1 
ATOM   1726 C CG2  . THR   A 1 110 ? 198.490 158.779 112.798 1.00 133.20 ? 123  THR   A CG2  1 
ATOM   1727 H H    . THR   A 1 110 ? 201.260 158.358 115.710 1.00 124.78 ? 123  THR   A H    1 
ATOM   1728 H HA   . THR   A 1 110 ? 198.588 159.610 115.587 1.00 125.36 ? 123  THR   A HA   1 
ATOM   1729 H HB   . THR   A 1 110 ? 200.373 158.179 113.592 1.00 124.57 ? 123  THR   A HB   1 
ATOM   1730 H HG1  . THR   A 1 110 ? 200.849 160.309 114.298 1.00 125.08 ? 123  THR   A HG1  1 
ATOM   1731 H HG21 . THR   A 1 110 ? 197.680 159.475 113.017 1.00 126.06 ? 123  THR   A HG21 1 
ATOM   1732 H HG22 . THR   A 1 110 ? 198.886 159.009 111.809 1.00 127.18 ? 123  THR   A HG22 1 
ATOM   1733 H HG23 . THR   A 1 110 ? 198.103 157.760 112.782 1.00 125.59 ? 123  THR   A HG23 1 
ATOM   1734 N N    . ILE   A 1 111 ? 197.042 157.589 115.424 1.00 113.31 ? 124  ILE   A N    1 
ATOM   1735 C CA   . ILE   A 1 111 ? 196.158 156.423 115.331 1.00 109.62 ? 124  ILE   A CA   1 
ATOM   1736 C C    . ILE   A 1 111 ? 195.383 156.460 114.020 1.00 114.70 ? 124  ILE   A C    1 
ATOM   1737 O O    . ILE   A 1 111 ? 194.942 157.524 113.591 1.00 127.94 ? 124  ILE   A O    1 
ATOM   1738 C CB   . ILE   A 1 111 ? 195.254 156.303 116.568 1.00 111.07 ? 124  ILE   A CB   1 
ATOM   1739 C CG1  . ILE   A 1 111 ? 194.411 155.020 116.497 1.00 116.52 ? 124  ILE   A CG1  1 
ATOM   1740 C CG2  . ILE   A 1 111 ? 194.351 157.527 116.745 1.00 111.17 ? 124  ILE   A CG2  1 
ATOM   1741 C CD1  . ILE   A 1 111 ? 193.706 154.672 117.808 1.00 118.07 ? 124  ILE   A CD1  1 
ATOM   1742 H H    . ILE   A 1 111 ? 196.627 158.503 115.320 1.00 117.57 ? 124  ILE   A H    1 
ATOM   1743 H HA   . ILE   A 1 111 ? 196.763 155.517 115.304 1.00 116.88 ? 124  ILE   A HA   1 
ATOM   1744 H HB   . ILE   A 1 111 ? 195.903 156.232 117.441 1.00 117.25 ? 124  ILE   A HB   1 
ATOM   1745 H HG12 . ILE   A 1 111 ? 193.659 155.110 115.713 1.00 116.83 ? 124  ILE   A HG12 1 
ATOM   1746 H HG13 . ILE   A 1 111 ? 195.068 154.185 116.251 1.00 117.65 ? 124  ILE   A HG13 1 
ATOM   1747 H HG21 . ILE   A 1 111 ? 194.957 158.432 116.802 1.00 116.54 ? 124  ILE   A HG21 1 
ATOM   1748 H HG22 . ILE   A 1 111 ? 193.649 157.608 115.915 1.00 115.69 ? 124  ILE   A HG22 1 
ATOM   1749 H HG23 . ILE   A 1 111 ? 193.786 157.450 117.674 1.00 116.94 ? 124  ILE   A HG23 1 
ATOM   1750 H HD11 . ILE   A 1 111 ? 193.216 153.704 117.703 1.00 116.42 ? 124  ILE   A HD11 1 
ATOM   1751 H HD12 . ILE   A 1 111 ? 192.947 155.418 118.044 1.00 117.33 ? 124  ILE   A HD12 1 
ATOM   1752 H HD13 . ILE   A 1 111 ? 194.431 154.617 118.620 1.00 116.87 ? 124  ILE   A HD13 1 
ATOM   1753 N N    . VAL   A 1 112 ? 195.213 155.302 113.385 1.00 118.13 ? 125  VAL   A N    1 
ATOM   1754 C CA   . VAL   A 1 112 ? 194.364 155.132 112.204 1.00 110.87 ? 125  VAL   A CA   1 
ATOM   1755 C C    . VAL   A 1 112 ? 193.241 154.171 112.525 1.00 114.92 ? 125  VAL   A C    1 
ATOM   1756 O O    . VAL   A 1 112 ? 193.437 153.198 113.249 1.00 127.12 ? 125  VAL   A O    1 
ATOM   1757 C CB   . VAL   A 1 112 ? 195.141 154.688 110.960 1.00 111.78 ? 125  VAL   A CB   1 
ATOM   1758 C CG1  . VAL   A 1 112 ? 196.310 155.632 110.697 1.00 118.22 ? 125  VAL   A CG1  1 
ATOM   1759 C CG2  . VAL   A 1 112 ? 195.698 153.269 111.039 1.00 119.79 ? 125  VAL   A CG2  1 
ATOM   1760 H H    . VAL   A 1 112 ? 195.607 154.466 113.791 1.00 120.51 ? 125  VAL   A H    1 
ATOM   1761 H HA   . VAL   A 1 112 ? 193.910 156.093 111.963 1.00 119.38 ? 125  VAL   A HA   1 
ATOM   1762 H HB   . VAL   A 1 112 ? 194.464 154.738 110.107 1.00 118.95 ? 125  VAL   A HB   1 
ATOM   1763 H HG11 . VAL   A 1 112 ? 195.962 156.664 110.745 1.00 119.74 ? 125  VAL   A HG11 1 
ATOM   1764 H HG12 . VAL   A 1 112 ? 196.726 155.440 109.708 1.00 119.91 ? 125  VAL   A HG12 1 
ATOM   1765 H HG13 . VAL   A 1 112 ? 197.086 155.493 111.450 1.00 119.27 ? 125  VAL   A HG13 1 
ATOM   1766 H HG21 . VAL   A 1 112 ? 194.888 152.545 111.132 1.00 120.18 ? 125  VAL   A HG21 1 
ATOM   1767 H HG22 . VAL   A 1 112 ? 196.252 153.042 110.128 1.00 120.35 ? 125  VAL   A HG22 1 
ATOM   1768 H HG23 . VAL   A 1 112 ? 196.367 153.176 111.895 1.00 118.85 ? 125  VAL   A HG23 1 
ATOM   1769 N N    . ILE   A 1 113 ? 192.054 154.439 112.002 1.00 119.94 ? 126  ILE   A N    1 
ATOM   1770 C CA   . ILE   A 1 113 ? 190.846 153.650 112.246 1.00 117.77 ? 126  ILE   A CA   1 
ATOM   1771 C C    . ILE   A 1 113 ? 190.189 153.389 110.893 1.00 127.81 ? 126  ILE   A C    1 
ATOM   1772 O O    . ILE   A 1 113 ? 190.110 154.293 110.065 1.00 139.95 ? 126  ILE   A O    1 
ATOM   1773 C CB   . ILE   A 1 113 ? 189.903 154.379 113.226 1.00 119.71 ? 126  ILE   A CB   1 
ATOM   1774 C CG1  . ILE   A 1 113 ? 190.610 154.815 114.527 1.00 125.93 ? 126  ILE   A CG1  1 
ATOM   1775 C CG2  . ILE   A 1 113 ? 188.708 153.474 113.545 1.00 124.23 ? 126  ILE   A CG2  1 
ATOM   1776 C CD1  . ILE   A 1 113 ? 189.752 155.684 115.446 1.00 128.66 ? 126  ILE   A CD1  1 
ATOM   1777 H H    . ILE   A 1 113 ? 191.969 155.254 111.412 1.00 125.13 ? 126  ILE   A H    1 
ATOM   1778 H HA   . ILE   A 1 113 ? 191.115 152.688 112.683 1.00 123.91 ? 126  ILE   A HA   1 
ATOM   1779 H HB   . ILE   A 1 113 ? 189.527 155.276 112.735 1.00 124.58 ? 126  ILE   A HB   1 
ATOM   1780 H HG12 . ILE   A 1 113 ? 190.940 153.934 115.077 1.00 125.92 ? 126  ILE   A HG12 1 
ATOM   1781 H HG13 . ILE   A 1 113 ? 191.490 155.411 114.282 1.00 124.95 ? 126  ILE   A HG13 1 
ATOM   1782 H HG21 . ILE   A 1 113 ? 187.992 153.995 114.182 1.00 125.51 ? 126  ILE   A HG21 1 
ATOM   1783 H HG22 . ILE   A 1 113 ? 188.183 153.194 112.633 1.00 124.42 ? 126  ILE   A HG22 1 
ATOM   1784 H HG23 . ILE   A 1 113 ? 189.045 152.571 114.054 1.00 125.78 ? 126  ILE   A HG23 1 
ATOM   1785 H HD11 . ILE   A 1 113 ? 190.367 156.052 116.267 1.00 125.99 ? 126  ILE   A HD11 1 
ATOM   1786 H HD12 . ILE   A 1 113 ? 188.928 155.106 115.865 1.00 125.56 ? 126  ILE   A HD12 1 
ATOM   1787 H HD13 . ILE   A 1 113 ? 189.359 156.535 114.889 1.00 125.78 ? 126  ILE   A HD13 1 
ATOM   1788 N N    . GLY   A 1 114 ? 189.735 152.172 110.625 1.00 133.74 ? 127  GLY   A N    1 
ATOM   1789 C CA   . GLY   A 1 114 ? 189.269 151.806 109.292 1.00 136.03 ? 127  GLY   A CA   1 
ATOM   1790 C C    . GLY   A 1 114 ? 188.629 150.427 109.223 1.00 137.51 ? 127  GLY   A C    1 
ATOM   1791 O O    . GLY   A 1 114 ? 188.060 149.934 110.198 1.00 143.87 ? 127  GLY   A O    1 
ATOM   1792 H H    . GLY   A 1 114 ? 189.795 151.451 111.331 1.00 134.48 ? 127  GLY   A H    1 
ATOM   1793 H HA2  . GLY   A 1 114 ? 188.540 152.535 108.937 1.00 135.32 ? 127  GLY   A HA2  1 
ATOM   1794 H HA3  . GLY   A 1 114 ? 190.122 151.828 108.613 1.00 134.16 ? 127  GLY   A HA3  1 
ATOM   1795 N N    . SER   A 1 115 ? 188.715 149.796 108.056 1.00 121.12 ? 128  SER   A N    1 
ATOM   1796 C CA   . SER   A 1 115 ? 188.150 148.467 107.820 1.00 123.12 ? 128  SER   A CA   1 
ATOM   1797 C C    . SER   A 1 115 ? 189.077 147.566 107.011 1.00 124.40 ? 128  SER   A C    1 
ATOM   1798 O O    . SER   A 1 115 ? 189.505 146.531 107.511 1.00 125.93 ? 128  SER   A O    1 
ATOM   1799 C CB   . SER   A 1 115 ? 186.771 148.595 107.176 1.00 123.29 ? 128  SER   A CB   1 
ATOM   1800 O OG   . SER   A 1 115 ? 186.857 149.308 105.955 1.00 128.59 ? 128  SER   A OG   1 
ATOM   1801 H H    . SER   A 1 115 ? 189.132 150.285 107.277 1.00 124.71 ? 128  SER   A H    1 
ATOM   1802 H HA   . SER   A 1 115 ? 188.011 147.968 108.780 1.00 125.90 ? 128  SER   A HA   1 
ATOM   1803 H HB2  . SER   A 1 115 ? 186.362 147.601 106.995 1.00 125.44 ? 128  SER   A HB2  1 
ATOM   1804 H HB3  . SER   A 1 115 ? 186.109 149.126 107.859 1.00 124.96 ? 128  SER   A HB3  1 
ATOM   1805 H HG   . SER   A 1 115 ? 185.964 149.463 105.640 1.00 126.60 ? 128  SER   A HG   1 
ATOM   1806 N N    . VAL   A 1 116 ? 189.440 147.959 105.792 1.00 122.35 ? 129  VAL   A N    1 
ATOM   1807 C CA   . VAL   A 1 116 ? 190.407 147.221 104.957 1.00 126.07 ? 129  VAL   A CA   1 
ATOM   1808 C C    . VAL   A 1 116 ? 191.684 148.006 104.671 1.00 126.69 ? 129  VAL   A C    1 
ATOM   1809 O O    . VAL   A 1 116 ? 192.643 147.427 104.178 1.00 128.98 ? 129  VAL   A O    1 
ATOM   1810 C CB   . VAL   A 1 116 ? 189.769 146.712 103.652 1.00 131.44 ? 129  VAL   A CB   1 
ATOM   1811 C CG1  . VAL   A 1 116 ? 188.651 145.707 103.928 1.00 128.28 ? 129  VAL   A CG1  1 
ATOM   1812 C CG2  . VAL   A 1 116 ? 189.197 147.830 102.780 1.00 131.13 ? 129  VAL   A CG2  1 
ATOM   1813 H H    . VAL   A 1 116 ? 188.931 148.733 105.390 1.00 126.56 ? 129  VAL   A H    1 
ATOM   1814 H HA   . VAL   A 1 116 ? 190.740 146.334 105.495 1.00 126.78 ? 129  VAL   A HA   1 
ATOM   1815 H HB   . VAL   A 1 116 ? 190.534 146.192 103.074 1.00 128.24 ? 129  VAL   A HB   1 
ATOM   1816 H HG11 . VAL   A 1 116 ? 189.037 144.892 104.541 1.00 127.36 ? 129  VAL   A HG11 1 
ATOM   1817 H HG12 . VAL   A 1 116 ? 187.825 146.189 104.450 1.00 126.91 ? 129  VAL   A HG12 1 
ATOM   1818 H HG13 . VAL   A 1 116 ? 188.287 145.296 102.987 1.00 127.94 ? 129  VAL   A HG13 1 
ATOM   1819 H HG21 . VAL   A 1 116 ? 189.968 148.569 102.562 1.00 127.81 ? 129  VAL   A HG21 1 
ATOM   1820 H HG22 . VAL   A 1 116 ? 188.359 148.315 103.279 1.00 127.51 ? 129  VAL   A HG22 1 
ATOM   1821 H HG23 . VAL   A 1 116 ? 188.846 147.410 101.837 1.00 127.89 ? 129  VAL   A HG23 1 
ATOM   1822 N N    . PHE   A 1 117 ? 191.728 149.306 104.977 1.00 121.24 ? 130  PHE   A N    1 
ATOM   1823 C CA   . PHE   A 1 117 ? 192.866 150.187 104.692 1.00 121.04 ? 130  PHE   A CA   1 
ATOM   1824 C C    . PHE   A 1 117 ? 193.280 150.201 103.207 1.00 124.01 ? 130  PHE   A C    1 
ATOM   1825 O O    . PHE   A 1 117 ? 194.458 150.296 102.877 1.00 124.19 ? 130  PHE   A O    1 
ATOM   1826 C CB   . PHE   A 1 117 ? 194.033 149.896 105.649 1.00 123.34 ? 130  PHE   A CB   1 
ATOM   1827 C CG   . PHE   A 1 117 ? 193.673 149.951 107.119 1.00 121.96 ? 130  PHE   A CG   1 
ATOM   1828 C CD1  . PHE   A 1 117 ? 193.405 151.186 107.730 1.00 119.85 ? 130  PHE   A CD1  1 
ATOM   1829 C CD2  . PHE   A 1 117 ? 193.595 148.770 107.873 1.00 120.30 ? 130  PHE   A CD2  1 
ATOM   1830 C CE1  . PHE   A 1 117 ? 193.039 151.237 109.084 1.00 115.87 ? 130  PHE   A CE1  1 
ATOM   1831 C CE2  . PHE   A 1 117 ? 193.234 148.822 109.227 1.00 115.34 ? 130  PHE   A CE2  1 
ATOM   1832 C CZ   . PHE   A 1 117 ? 192.949 150.055 109.831 1.00 116.64 ? 130  PHE   A CZ   1 
ATOM   1833 H H    . PHE   A 1 117 ? 190.927 149.711 105.440 1.00 122.18 ? 130  PHE   A H    1 
ATOM   1834 H HA   . PHE   A 1 117 ? 192.540 151.205 104.905 1.00 121.69 ? 130  PHE   A HA   1 
ATOM   1835 H HB2  . PHE   A 1 117 ? 194.446 148.914 105.419 1.00 123.06 ? 130  PHE   A HB2  1 
ATOM   1836 H HB3  . PHE   A 1 117 ? 194.826 150.622 105.473 1.00 122.58 ? 130  PHE   A HB3  1 
ATOM   1837 H HD1  . PHE   A 1 117 ? 193.469 152.098 107.156 1.00 122.40 ? 130  PHE   A HD1  1 
ATOM   1838 H HD2  . PHE   A 1 117 ? 193.808 147.817 107.410 1.00 123.11 ? 130  PHE   A HD2  1 
ATOM   1839 H HE1  . PHE   A 1 117 ? 192.827 152.188 109.550 1.00 122.00 ? 130  PHE   A HE1  1 
ATOM   1840 H HE2  . PHE   A 1 117 ? 193.174 147.910 109.803 1.00 121.85 ? 130  PHE   A HE2  1 
ATOM   1841 H HZ   . PHE   A 1 117 ? 192.667 150.095 110.873 1.00 122.81 ? 130  PHE   A HZ   1 
ATOM   1842 N N    . ILE   A 1 118 ? 192.304 150.135 102.300 1.00 130.05 ? 131  ILE   A N    1 
ATOM   1843 C CA   . ILE   A 1 118 ? 192.484 150.219 100.842 1.00 127.94 ? 131  ILE   A CA   1 
ATOM   1844 C C    . ILE   A 1 118 ? 191.790 151.480 100.332 1.00 129.56 ? 131  ILE   A C    1 
ATOM   1845 O O    . ILE   A 1 118 ? 190.732 151.846 100.842 1.00 135.66 ? 131  ILE   A O    1 
ATOM   1846 C CB   . ILE   A 1 118 ? 191.906 148.971 100.143 1.00 130.51 ? 131  ILE   A CB   1 
ATOM   1847 C CG1  . ILE   A 1 118 ? 192.491 147.645 100.657 1.00 132.34 ? 131  ILE   A CG1  1 
ATOM   1848 C CG2  . ILE   A 1 118 ? 192.080 149.040 98.619  1.00 130.84 ? 131  ILE   A CG2  1 
ATOM   1849 C CD1  . ILE   A 1 118 ? 194.009 147.504 100.509 1.00 133.62 ? 131  ILE   A CD1  1 
ATOM   1850 H H    . ILE   A 1 118 ? 191.356 150.101 102.646 1.00 130.78 ? 131  ILE   A H    1 
ATOM   1851 H HA   . ILE   A 1 118 ? 193.545 150.294 100.601 1.00 130.03 ? 131  ILE   A HA   1 
ATOM   1852 H HB   . ILE   A 1 118 ? 190.835 148.939 100.345 1.00 130.83 ? 131  ILE   A HB   1 
ATOM   1853 H HG12 . ILE   A 1 118 ? 192.230 147.525 101.708 1.00 131.22 ? 131  ILE   A HG12 1 
ATOM   1854 H HG13 . ILE   A 1 118 ? 192.017 146.822 100.122 1.00 130.74 ? 131  ILE   A HG13 1 
ATOM   1855 H HG21 . ILE   A 1 118 ? 191.454 149.823 98.190  1.00 130.79 ? 131  ILE   A HG21 1 
ATOM   1856 H HG22 . ILE   A 1 118 ? 193.122 149.226 98.357  1.00 130.84 ? 131  ILE   A HG22 1 
ATOM   1857 H HG23 . ILE   A 1 118 ? 191.770 148.096 98.169  1.00 131.01 ? 131  ILE   A HG23 1 
ATOM   1858 H HD11 . ILE   A 1 118 ? 194.317 146.535 100.904 1.00 131.73 ? 131  ILE   A HD11 1 
ATOM   1859 H HD12 . ILE   A 1 118 ? 194.290 147.556 99.457  1.00 131.68 ? 131  ILE   A HD12 1 
ATOM   1860 H HD13 . ILE   A 1 118 ? 194.525 148.286 101.066 1.00 131.27 ? 131  ILE   A HD13 1 
ATOM   1861 N N    . ASN   A 1 119 ? 192.333 152.129 99.303  1.00 128.23 ? 132  ASN   A N    1 
ATOM   1862 C CA   . ASN   A 1 119 ? 191.810 153.376 98.728  1.00 131.01 ? 132  ASN   A CA   1 
ATOM   1863 C C    . ASN   A 1 119 ? 190.428 153.290 98.042  1.00 132.31 ? 132  ASN   A C    1 
ATOM   1864 O O    . ASN   A 1 119 ? 190.017 154.233 97.375  1.00 135.86 ? 132  ASN   A O    1 
ATOM   1865 C CB   . ASN   A 1 119 ? 192.877 153.969 97.802  1.00 131.34 ? 132  ASN   A CB   1 
ATOM   1866 C CG   . ASN   A 1 119 ? 193.155 153.133 96.571  1.00 132.84 ? 132  ASN   A CG   1 
ATOM   1867 O OD1  . ASN   A 1 119 ? 192.348 152.302 96.170  1.00 134.84 ? 132  ASN   A OD1  1 
ATOM   1868 N ND2  . ASN   A 1 119 ? 194.335 153.307 96.007  1.00 136.20 ? 132  ASN   A ND2  1 
ATOM   1869 H H    . ASN   A 1 119 ? 193.178 151.749 98.902  1.00 132.23 ? 132  ASN   A H    1 
ATOM   1870 H HA   . ASN   A 1 119 ? 191.681 154.074 99.555  1.00 133.36 ? 132  ASN   A HA   1 
ATOM   1871 H HB2  . ASN   A 1 119 ? 192.567 154.961 97.473  1.00 133.33 ? 132  ASN   A HB2  1 
ATOM   1872 H HB3  . ASN   A 1 119 ? 193.798 154.089 98.373  1.00 132.81 ? 132  ASN   A HB3  1 
ATOM   1873 H HD21 . ASN   A 1 119 ? 194.964 153.990 96.405  1.00 133.88 ? 132  ASN   A HD21 1 
ATOM   1874 N N    . ASN   A 1 120 ? 189.674 152.213 98.241  1.00 131.78 ? 133  ASN   A N    1 
ATOM   1875 C CA   . ASN   A 1 120 ? 188.244 152.128 97.945  1.00 132.19 ? 133  ASN   A CA   1 
ATOM   1876 C C    . ASN   A 1 120 ? 187.388 152.126 99.229  1.00 134.38 ? 133  ASN   A C    1 
ATOM   1877 O O    . ASN   A 1 120 ? 186.222 151.736 99.203  1.00 134.62 ? 133  ASN   A O    1 
ATOM   1878 C CB   . ASN   A 1 120 ? 187.991 150.920 97.033  1.00 132.39 ? 133  ASN   A CB   1 
ATOM   1879 C CG   . ASN   A 1 120 ? 188.320 149.589 97.675  1.00 140.07 ? 133  ASN   A CG   1 
ATOM   1880 O OD1  . ASN   A 1 120 ? 188.649 149.489 98.846  1.00 138.20 ? 133  ASN   A OD1  1 
ATOM   1881 N ND2  . ASN   A 1 120 ? 188.261 148.524 96.915  1.00 142.57 ? 133  ASN   A ND2  1 
ATOM   1882 H H    . ASN   A 1 120 ? 190.063 151.466 98.799  1.00 134.11 ? 133  ASN   A H    1 
ATOM   1883 H HA   . ASN   A 1 120 ? 187.940 153.017 97.393  1.00 134.35 ? 133  ASN   A HA   1 
ATOM   1884 H HB2  . ASN   A 1 120 ? 186.943 150.907 96.736  1.00 133.80 ? 133  ASN   A HB2  1 
ATOM   1885 H HB3  . ASN   A 1 120 ? 188.591 151.027 96.129  1.00 134.17 ? 133  ASN   A HB3  1 
ATOM   1886 H HD21 . ASN   A 1 120 ? 187.996 148.605 95.944  1.00 134.57 ? 133  ASN   A HD21 1 
ATOM   1887 H HD22 . ASN   A 1 120 ? 188.482 147.629 97.327  1.00 135.22 ? 133  ASN   A HD22 1 
ATOM   1888 N N    . SER   A 1 121 ? 187.968 152.536 100.359 1.00 137.29 ? 134  SER   A N    1 
ATOM   1889 C CA   . SER   A 1 121 ? 187.329 152.623 101.674 1.00 137.49 ? 134  SER   A CA   1 
ATOM   1890 C C    . SER   A 1 121 ? 187.882 153.817 102.448 1.00 135.68 ? 134  SER   A C    1 
ATOM   1891 O O    . SER   A 1 121 ? 189.032 154.201 102.250 1.00 140.79 ? 134  SER   A O    1 
ATOM   1892 C CB   . SER   A 1 121 ? 187.579 151.330 102.453 1.00 137.91 ? 134  SER   A CB   1 
ATOM   1893 O OG   . SER   A 1 121 ? 188.947 151.208 102.800 1.00 139.55 ? 134  SER   A OG   1 
ATOM   1894 H H    . SER   A 1 121 ? 188.942 152.802 100.319 1.00 136.98 ? 134  SER   A H    1 
ATOM   1895 H HA   . SER   A 1 121 ? 186.254 152.756 101.551 1.00 137.37 ? 134  SER   A HA   1 
ATOM   1896 H HB2  . SER   A 1 121 ? 186.980 151.335 103.363 1.00 136.79 ? 134  SER   A HB2  1 
ATOM   1897 H HB3  . SER   A 1 121 ? 187.279 150.477 101.844 1.00 137.23 ? 134  SER   A HB3  1 
ATOM   1898 H HG   . SER   A 1 121 ? 189.470 151.451 102.033 1.00 137.69 ? 134  SER   A HG   1 
ATOM   1899 N N    . TYR   A 1 122 ? 187.096 154.418 103.335 1.00 129.87 ? 135  TYR   A N    1 
ATOM   1900 C CA   . TYR   A 1 122 ? 187.564 155.552 104.129 1.00 129.83 ? 135  TYR   A CA   1 
ATOM   1901 C C    . TYR   A 1 122 ? 188.358 155.097 105.352 1.00 127.59 ? 135  TYR   A C    1 
ATOM   1902 O O    . TYR   A 1 122 ? 187.887 154.279 106.135 1.00 128.36 ? 135  TYR   A O    1 
ATOM   1903 C CB   . TYR   A 1 122 ? 186.383 156.440 104.511 1.00 127.96 ? 135  TYR   A CB   1 
ATOM   1904 C CG   . TYR   A 1 122 ? 185.786 157.115 103.299 1.00 131.06 ? 135  TYR   A CG   1 
ATOM   1905 C CD1  . TYR   A 1 122 ? 186.429 158.238 102.754 1.00 134.28 ? 135  TYR   A CD1  1 
ATOM   1906 C CD2  . TYR   A 1 122 ? 184.635 156.595 102.685 1.00 131.12 ? 135  TYR   A CD2  1 
ATOM   1907 C CE1  . TYR   A 1 122 ? 185.936 158.834 101.581 1.00 135.17 ? 135  TYR   A CE1  1 
ATOM   1908 C CE2  . TYR   A 1 122 ? 184.128 157.199 101.520 1.00 135.30 ? 135  TYR   A CE2  1 
ATOM   1909 C CZ   . TYR   A 1 122 ? 184.781 158.318 100.965 1.00 137.14 ? 135  TYR   A CZ   1 
ATOM   1910 O OH   . TYR   A 1 122 ? 184.299 158.905 99.841  1.00 138.35 ? 135  TYR   A OH   1 
ATOM   1911 H H    . TYR   A 1 122 ? 186.156 154.080 103.483 1.00 132.88 ? 135  TYR   A H    1 
ATOM   1912 H HA   . TYR   A 1 122 ? 188.227 156.157 103.512 1.00 133.17 ? 135  TYR   A HA   1 
ATOM   1913 H HB2  . TYR   A 1 122 ? 185.623 155.847 105.020 1.00 132.60 ? 135  TYR   A HB2  1 
ATOM   1914 H HB3  . TYR   A 1 122 ? 186.725 157.210 105.202 1.00 132.70 ? 135  TYR   A HB3  1 
ATOM   1915 H HD1  . TYR   A 1 122 ? 187.304 158.642 103.241 1.00 133.20 ? 135  TYR   A HD1  1 
ATOM   1916 H HD2  . TYR   A 1 122 ? 184.140 155.731 103.104 1.00 132.79 ? 135  TYR   A HD2  1 
ATOM   1917 H HE1  . TYR   A 1 122 ? 186.426 159.696 101.153 1.00 133.03 ? 135  TYR   A HE1  1 
ATOM   1918 H HE2  . TYR   A 1 122 ? 183.241 156.801 101.049 1.00 133.50 ? 135  TYR   A HE2  1 
ATOM   1919 H HH   . TYR   A 1 122 ? 183.508 158.463 99.525  1.00 133.82 ? 135  TYR   A HH   1 
ATOM   1920 N N    . THR   A 1 123 ? 189.546 155.663 105.544 1.00 126.45 ? 136  THR   A N    1 
ATOM   1921 C CA   . THR   A 1 123 ? 190.356 155.520 106.759 1.00 125.61 ? 136  THR   A CA   1 
ATOM   1922 C C    . THR   A 1 123 ? 190.357 156.841 107.505 1.00 129.61 ? 136  THR   A C    1 
ATOM   1923 O O    . THR   A 1 123 ? 190.648 157.874 106.906 1.00 135.35 ? 136  THR   A O    1 
ATOM   1924 C CB   . THR   A 1 123 ? 191.789 155.124 106.406 1.00 127.85 ? 136  THR   A CB   1 
ATOM   1925 O OG1  . THR   A 1 123 ? 191.767 153.870 105.775 1.00 128.48 ? 136  THR   A OG1  1 
ATOM   1926 C CG2  . THR   A 1 123 ? 192.703 154.995 107.615 1.00 130.15 ? 136  THR   A CG2  1 
ATOM   1927 H H    . THR   A 1 123 ? 189.863 156.335 104.859 1.00 129.94 ? 136  THR   A H    1 
ATOM   1928 H HA   . THR   A 1 123 ? 189.941 154.751 107.411 1.00 129.01 ? 136  THR   A HA   1 
ATOM   1929 H HB   . THR   A 1 123 ? 192.213 155.859 105.722 1.00 129.54 ? 136  THR   A HB   1 
ATOM   1930 H HG1  . THR   A 1 123 ? 191.231 153.964 104.984 1.00 129.43 ? 136  THR   A HG1  1 
ATOM   1931 H HG21 . THR   A 1 123 ? 193.676 154.619 107.298 1.00 129.40 ? 136  THR   A HG21 1 
ATOM   1932 H HG22 . THR   A 1 123 ? 192.266 154.309 108.341 1.00 130.03 ? 136  THR   A HG22 1 
ATOM   1933 H HG23 . THR   A 1 123 ? 192.849 155.970 108.080 1.00 129.30 ? 136  THR   A HG23 1 
ATOM   1934 N N    . ILE   A 1 124 ? 190.034 156.827 108.794 1.00 119.03 ? 137  ILE   A N    1 
ATOM   1935 C CA   . ILE   A 1 124 ? 190.181 157.982 109.679 1.00 117.74 ? 137  ILE   A CA   1 
ATOM   1936 C C    . ILE   A 1 124 ? 191.606 158.006 110.212 1.00 120.58 ? 137  ILE   A C    1 
ATOM   1937 O O    . ILE   A 1 124 ? 192.126 156.966 110.610 1.00 124.65 ? 137  ILE   A O    1 
ATOM   1938 C CB   . ILE   A 1 124 ? 189.162 157.907 110.825 1.00 113.33 ? 137  ILE   A CB   1 
ATOM   1939 C CG1  . ILE   A 1 124 ? 187.741 158.146 110.291 1.00 117.12 ? 137  ILE   A CG1  1 
ATOM   1940 C CG2  . ILE   A 1 124 ? 189.464 158.921 111.940 1.00 117.64 ? 137  ILE   A CG2  1 
ATOM   1941 C CD1  . ILE   A 1 124 ? 186.679 157.495 111.172 1.00 125.24 ? 137  ILE   A CD1  1 
ATOM   1942 H H    . ILE   A 1 124 ? 189.874 155.931 109.232 1.00 122.15 ? 137  ILE   A H    1 
ATOM   1943 H HA   . ILE   A 1 124 ? 190.001 158.900 109.120 1.00 122.28 ? 137  ILE   A HA   1 
ATOM   1944 H HB   . ILE   A 1 124 ? 189.214 156.906 111.252 1.00 120.69 ? 137  ILE   A HB   1 
ATOM   1945 H HG12 . ILE   A 1 124 ? 187.548 159.217 110.231 1.00 121.54 ? 137  ILE   A HG12 1 
ATOM   1946 H HG13 . ILE   A 1 124 ? 187.636 157.726 109.291 1.00 121.53 ? 137  ILE   A HG13 1 
ATOM   1947 H HG21 . ILE   A 1 124 ? 190.397 158.668 112.444 1.00 121.02 ? 137  ILE   A HG21 1 
ATOM   1948 H HG22 . ILE   A 1 124 ? 189.537 159.925 111.522 1.00 121.55 ? 137  ILE   A HG22 1 
ATOM   1949 H HG23 . ILE   A 1 124 ? 188.675 158.908 112.691 1.00 121.49 ? 137  ILE   A HG23 1 
ATOM   1950 H HD11 . ILE   A 1 124 ? 185.692 157.764 110.797 1.00 122.43 ? 137  ILE   A HD11 1 
ATOM   1951 H HD12 . ILE   A 1 124 ? 186.766 157.846 112.201 1.00 122.26 ? 137  ILE   A HD12 1 
ATOM   1952 H HD13 . ILE   A 1 124 ? 186.794 156.411 111.150 1.00 122.15 ? 137  ILE   A HD13 1 
ATOM   1953 N N    . VAL   A 1 125 ? 192.227 159.180 110.265 1.00 122.82 ? 138  VAL   A N    1 
ATOM   1954 C CA   . VAL   A 1 125 ? 193.582 159.367 110.790 1.00 119.99 ? 138  VAL   A CA   1 
ATOM   1955 C C    . VAL   A 1 125 ? 193.600 160.550 111.737 1.00 122.83 ? 138  VAL   A C    1 
ATOM   1956 O O    . VAL   A 1 125 ? 193.094 161.616 111.397 1.00 131.58 ? 138  VAL   A O    1 
ATOM   1957 C CB   . VAL   A 1 125 ? 194.588 159.589 109.656 1.00 121.97 ? 138  VAL   A CB   1 
ATOM   1958 C CG1  . VAL   A 1 125 ? 196.011 159.737 110.198 1.00 122.45 ? 138  VAL   A CG1  1 
ATOM   1959 C CG2  . VAL   A 1 125 ? 194.544 158.430 108.659 1.00 132.34 ? 138  VAL   A CG2  1 
ATOM   1960 H H    . VAL   A 1 125 ? 191.735 159.994 109.925 1.00 125.55 ? 138  VAL   A H    1 
ATOM   1961 H HA   . VAL   A 1 125 ? 193.887 158.480 111.345 1.00 125.66 ? 138  VAL   A HA   1 
ATOM   1962 H HB   . VAL   A 1 125 ? 194.335 160.504 109.119 1.00 124.88 ? 138  VAL   A HB   1 
ATOM   1963 H HG11 . VAL   A 1 125 ? 196.103 160.660 110.771 1.00 124.56 ? 138  VAL   A HG11 1 
ATOM   1964 H HG12 . VAL   A 1 125 ? 196.262 158.890 110.836 1.00 125.77 ? 138  VAL   A HG12 1 
ATOM   1965 H HG13 . VAL   A 1 125 ? 196.718 159.784 109.370 1.00 125.12 ? 138  VAL   A HG13 1 
ATOM   1966 H HG21 . VAL   A 1 125 ? 193.610 158.457 108.098 1.00 126.46 ? 138  VAL   A HG21 1 
ATOM   1967 H HG22 . VAL   A 1 125 ? 194.618 157.476 109.180 1.00 126.41 ? 138  VAL   A HG22 1 
ATOM   1968 H HG23 . VAL   A 1 125 ? 195.366 158.518 107.949 1.00 126.25 ? 138  VAL   A HG23 1 
ATOM   1969 N N    . VAL   A 1 126 ? 194.206 160.376 112.909 1.00 113.84 ? 139  VAL   A N    1 
ATOM   1970 C CA   . VAL   A 1 126 ? 194.365 161.424 113.923 1.00 110.88 ? 139  VAL   A CA   1 
ATOM   1971 C C    . VAL   A 1 126 ? 195.846 161.601 114.212 1.00 107.89 ? 139  VAL   A C    1 
ATOM   1972 O O    . VAL   A 1 126 ? 196.464 160.705 114.783 1.00 115.38 ? 139  VAL   A O    1 
ATOM   1973 C CB   . VAL   A 1 126 ? 193.598 161.038 115.195 1.00 104.44 ? 139  VAL   A CB   1 
ATOM   1974 C CG1  . VAL   A 1 126 ? 193.810 162.049 116.319 1.00 111.38 ? 139  VAL   A CG1  1 
ATOM   1975 C CG2  . VAL   A 1 126 ? 192.097 160.920 114.934 1.00 109.14 ? 139  VAL   A CG2  1 
ATOM   1976 H H    . VAL   A 1 126 ? 194.576 159.461 113.122 1.00 115.47 ? 139  VAL   A H    1 
ATOM   1977 H HA   . VAL   A 1 126 ? 193.968 162.371 113.559 1.00 114.71 ? 139  VAL   A HA   1 
ATOM   1978 H HB   . VAL   A 1 126 ? 193.952 160.067 115.542 1.00 113.65 ? 139  VAL   A HB   1 
ATOM   1979 H HG11 . VAL   A 1 126 ? 194.853 162.041 116.636 1.00 114.66 ? 139  VAL   A HG11 1 
ATOM   1980 H HG12 . VAL   A 1 126 ? 193.538 163.049 115.983 1.00 114.25 ? 139  VAL   A HG12 1 
ATOM   1981 H HG13 . VAL   A 1 126 ? 193.197 161.781 117.180 1.00 114.60 ? 139  VAL   A HG13 1 
ATOM   1982 H HG21 . VAL   A 1 126 ? 191.900 160.137 114.202 1.00 113.92 ? 139  VAL   A HG21 1 
ATOM   1983 H HG22 . VAL   A 1 126 ? 191.581 160.658 115.858 1.00 114.28 ? 139  VAL   A HG22 1 
ATOM   1984 H HG23 . VAL   A 1 126 ? 191.708 161.868 114.562 1.00 113.63 ? 139  VAL   A HG23 1 
ATOM   1985 N N    . GLN   A 1 127 ? 196.426 162.738 113.834 1.00 116.69 ? 140  GLN   A N    1 
ATOM   1986 C CA   . GLN   A 1 127 ? 197.870 162.963 113.893 1.00 116.67 ? 140  GLN   A CA   1 
ATOM   1987 C C    . GLN   A 1 127 ? 198.204 164.312 114.543 1.00 122.19 ? 140  GLN   A C    1 
ATOM   1988 O O    . GLN   A 1 127 ? 197.689 165.341 114.111 1.00 133.32 ? 140  GLN   A O    1 
ATOM   1989 C CB   . GLN   A 1 127 ? 198.444 162.873 112.470 1.00 122.32 ? 140  GLN   A CB   1 
ATOM   1990 C CG   . GLN   A 1 127 ? 199.939 163.226 112.417 1.00 125.87 ? 140  GLN   A CG   1 
ATOM   1991 C CD   . GLN   A 1 127 ? 200.605 162.884 111.089 1.00 127.13 ? 140  GLN   A CD   1 
ATOM   1992 O OE1  . GLN   A 1 127 ? 199.984 162.792 110.043 1.00 124.83 ? 140  GLN   A OE1  1 
ATOM   1993 N NE2  . GLN   A 1 127 ? 201.913 162.730 111.078 1.00 127.30 ? 140  GLN   A NE2  1 
ATOM   1994 H H    . GLN   A 1 127 ? 195.859 163.454 113.404 1.00 124.61 ? 140  GLN   A H    1 
ATOM   1995 H HA   . GLN   A 1 127 ? 198.330 162.161 114.470 1.00 123.17 ? 140  GLN   A HA   1 
ATOM   1996 H HB2  . GLN   A 1 127 ? 198.305 161.856 112.105 1.00 124.33 ? 140  GLN   A HB2  1 
ATOM   1997 H HB3  . GLN   A 1 127 ? 197.901 163.554 111.815 1.00 124.19 ? 140  GLN   A HB3  1 
ATOM   1998 H HG2  . GLN   A 1 127 ? 200.065 164.295 112.591 1.00 124.94 ? 140  GLN   A HG2  1 
ATOM   1999 H HG3  . GLN   A 1 127 ? 200.460 162.699 113.216 1.00 124.67 ? 140  GLN   A HG3  1 
ATOM   2000 H HE21 . GLN   A 1 127 ? 202.428 162.773 111.946 1.00 125.32 ? 140  GLN   A HE21 1 
ATOM   2001 H HE22 . GLN   A 1 127 ? 202.371 162.527 110.201 1.00 125.04 ? 140  GLN   A HE22 1 
ATOM   2002 N N    . PRO   A 1 128 ? 199.098 164.363 115.538 1.00 117.99 ? 141  PRO   A N    1 
ATOM   2003 C CA   . PRO   A 1 128 ? 199.569 165.612 116.110 1.00 123.75 ? 141  PRO   A CA   1 
ATOM   2004 C C    . PRO   A 1 128 ? 200.693 166.238 115.284 1.00 125.46 ? 141  PRO   A C    1 
ATOM   2005 O O    . PRO   A 1 128 ? 201.584 165.545 114.800 1.00 129.13 ? 141  PRO   A O    1 
ATOM   2006 C CB   . PRO   A 1 128 ? 200.064 165.237 117.499 1.00 128.24 ? 141  PRO   A CB   1 
ATOM   2007 C CG   . PRO   A 1 128 ? 200.603 163.826 117.293 1.00 132.67 ? 141  PRO   A CG   1 
ATOM   2008 C CD   . PRO   A 1 128 ? 199.643 163.237 116.269 1.00 125.49 ? 141  PRO   A CD   1 
ATOM   2009 H HA   . PRO   A 1 128 ? 198.749 166.324 116.206 1.00 127.03 ? 141  PRO   A HA   1 
ATOM   2010 H HB2  . PRO   A 1 128 ? 200.832 165.917 117.868 1.00 128.01 ? 141  PRO   A HB2  1 
ATOM   2011 H HB3  . PRO   A 1 128 ? 199.216 165.212 118.183 1.00 127.02 ? 141  PRO   A HB3  1 
ATOM   2012 H HG2  . PRO   A 1 128 ? 201.610 163.868 116.877 1.00 128.00 ? 141  PRO   A HG2  1 
ATOM   2013 H HG3  . PRO   A 1 128 ? 200.599 163.259 118.223 1.00 128.36 ? 141  PRO   A HG3  1 
ATOM   2014 H HD2  . PRO   A 1 128 ? 200.177 162.554 115.608 1.00 127.07 ? 141  PRO   A HD2  1 
ATOM   2015 H HD3  . PRO   A 1 128 ? 198.835 162.716 116.782 1.00 127.25 ? 141  PRO   A HD3  1 
ATOM   2016 N N    . HIS   A 1 129 ? 200.704 167.565 115.207 1.00 131.39 ? 142  HIS   A N    1 
ATOM   2017 C CA   . HIS   A 1 129 ? 201.751 168.385 114.596 1.00 131.91 ? 142  HIS   A CA   1 
ATOM   2018 C C    . HIS   A 1 129 ? 202.148 169.524 115.540 1.00 133.87 ? 142  HIS   A C    1 
ATOM   2019 O O    . HIS   A 1 129 ? 201.944 170.697 115.241 1.00 137.43 ? 142  HIS   A O    1 
ATOM   2020 C CB   . HIS   A 1 129 ? 201.275 168.924 113.243 1.00 135.54 ? 142  HIS   A CB   1 
ATOM   2021 C CG   . HIS   A 1 129 ? 200.914 167.882 112.226 1.00 139.03 ? 142  HIS   A CG   1 
ATOM   2022 N ND1  . HIS   A 1 129 ? 201.812 167.166 111.431 1.00 138.85 ? 142  HIS   A ND1  1 
ATOM   2023 C CD2  . HIS   A 1 129 ? 199.644 167.602 111.828 1.00 139.80 ? 142  HIS   A CD2  1 
ATOM   2024 C CE1  . HIS   A 1 129 ? 201.051 166.473 110.568 1.00 141.48 ? 142  HIS   A CE1  1 
ATOM   2025 N NE2  . HIS   A 1 129 ? 199.751 166.722 110.780 1.00 143.52 ? 142  HIS   A NE2  1 
ATOM   2026 H H    . HIS   A 1 129 ? 199.885 168.049 115.545 1.00 136.77 ? 142  HIS   A H    1 
ATOM   2027 H HA   . HIS   A 1 129 ? 202.643 167.783 114.423 1.00 137.12 ? 142  HIS   A HA   1 
ATOM   2028 H HB2  . HIS   A 1 129 ? 200.404 169.560 113.402 1.00 137.46 ? 142  HIS   A HB2  1 
ATOM   2029 H HB3  . HIS   A 1 129 ? 202.064 169.542 112.816 1.00 137.58 ? 142  HIS   A HB3  1 
ATOM   2030 H HD2  . HIS   A 1 129 ? 198.741 168.041 112.226 1.00 137.50 ? 142  HIS   A HD2  1 
ATOM   2031 H HE1  . HIS   A 1 129 ? 201.427 165.838 109.779 1.00 137.39 ? 142  HIS   A HE1  1 
ATOM   2032 H HE2  . HIS   A 1 129 ? 198.996 166.410 110.187 1.00 137.97 ? 142  HIS   A HE2  1 
ATOM   2033 N N    . ASN   A 1 130 ? 202.668 169.182 116.718 1.00 138.66 ? 143  ASN   A N    1 
ATOM   2034 C CA   . ASN   A 1 130 ? 203.136 170.133 117.730 1.00 141.78 ? 143  ASN   A CA   1 
ATOM   2035 C C    . ASN   A 1 130 ? 202.093 171.205 118.109 1.00 140.59 ? 143  ASN   A C    1 
ATOM   2036 O O    . ASN   A 1 130 ? 202.286 172.397 117.875 1.00 141.77 ? 143  ASN   A O    1 
ATOM   2037 C CB   . ASN   A 1 130 ? 204.483 170.715 117.273 1.00 144.13 ? 143  ASN   A CB   1 
ATOM   2038 C CG   . ASN   A 1 130 ? 205.131 171.535 118.368 1.00 148.03 ? 143  ASN   A CG   1 
ATOM   2039 O OD1  . ASN   A 1 130 ? 205.096 171.175 119.533 1.00 149.87 ? 143  ASN   A OD1  1 
ATOM   2040 N ND2  . ASN   A 1 130 ? 205.752 172.639 118.037 1.00 146.33 ? 143  ASN   A ND2  1 
ATOM   2041 H H    . ASN   A 1 130 ? 202.807 168.198 116.900 1.00 142.70 ? 143  ASN   A H    1 
ATOM   2042 H HA   . ASN   A 1 130 ? 203.323 169.558 118.637 1.00 143.49 ? 143  ASN   A HA   1 
ATOM   2043 H HB2  . ASN   A 1 130 ? 205.166 169.908 117.009 1.00 143.40 ? 143  ASN   A HB2  1 
ATOM   2044 H HB3  . ASN   A 1 130 ? 204.333 171.340 116.393 1.00 142.94 ? 143  ASN   A HB3  1 
ATOM   2045 H HD21 . ASN   A 1 130 ? 205.766 172.949 117.076 1.00 143.28 ? 143  ASN   A HD21 1 
ATOM   2046 H HD22 . ASN   A 1 130 ? 206.180 173.185 118.771 1.00 143.60 ? 143  ASN   A HD22 1 
ATOM   2047 N N    . GLY   A 1 131 ? 200.971 170.781 118.690 1.00 132.66 ? 144  GLY   A N    1 
ATOM   2048 C CA   . GLY   A 1 131 ? 199.908 171.667 119.188 1.00 133.85 ? 144  GLY   A CA   1 
ATOM   2049 C C    . GLY   A 1 131 ? 198.696 171.801 118.272 1.00 135.83 ? 144  GLY   A C    1 
ATOM   2050 O O    . GLY   A 1 131 ? 197.638 172.248 118.712 1.00 137.92 ? 144  GLY   A O    1 
ATOM   2051 H H    . GLY   A 1 131 ? 200.878 169.792 118.876 1.00 135.43 ? 144  GLY   A H    1 
ATOM   2052 H HA2  . GLY   A 1 131 ? 199.553 171.290 120.147 1.00 135.40 ? 144  GLY   A HA2  1 
ATOM   2053 H HA3  . GLY   A 1 131 ? 200.308 172.668 119.351 1.00 134.94 ? 144  GLY   A HA3  1 
ATOM   2054 N N    . VAL   A 1 132 ? 198.809 171.350 117.025 1.00 134.34 ? 145  VAL   A N    1 
ATOM   2055 C CA   . VAL   A 1 132 ? 197.674 171.163 116.117 1.00 130.43 ? 145  VAL   A CA   1 
ATOM   2056 C C    . VAL   A 1 132 ? 197.407 169.676 115.977 1.00 128.60 ? 145  VAL   A C    1 
ATOM   2057 O O    . VAL   A 1 132 ? 198.289 168.924 115.580 1.00 134.49 ? 145  VAL   A O    1 
ATOM   2058 C CB   . VAL   A 1 132 ? 197.962 171.787 114.746 1.00 136.27 ? 145  VAL   A CB   1 
ATOM   2059 C CG1  . VAL   A 1 132 ? 196.836 171.483 113.759 1.00 136.68 ? 145  VAL   A CG1  1 
ATOM   2060 C CG2  . VAL   A 1 132 ? 198.093 173.307 114.858 1.00 135.25 ? 145  VAL   A CG2  1 
ATOM   2061 H H    . VAL   A 1 132 ? 199.718 171.034 116.717 1.00 134.85 ? 145  VAL   A H    1 
ATOM   2062 H HA   . VAL   A 1 132 ? 196.780 171.638 116.521 1.00 134.07 ? 145  VAL   A HA   1 
ATOM   2063 H HB   . VAL   A 1 132 ? 198.894 171.386 114.347 1.00 135.32 ? 145  VAL   A HB   1 
ATOM   2064 H HG11 . VAL   A 1 132 ? 196.810 170.419 113.523 1.00 135.53 ? 145  VAL   A HG11 1 
ATOM   2065 H HG12 . VAL   A 1 132 ? 197.004 172.028 112.830 1.00 135.01 ? 145  VAL   A HG12 1 
ATOM   2066 H HG13 . VAL   A 1 132 ? 195.883 171.787 114.193 1.00 134.69 ? 145  VAL   A HG13 1 
ATOM   2067 H HG21 . VAL   A 1 132 ? 198.925 173.564 115.514 1.00 135.23 ? 145  VAL   A HG21 1 
ATOM   2068 H HG22 . VAL   A 1 132 ? 198.288 173.734 113.875 1.00 134.57 ? 145  VAL   A HG22 1 
ATOM   2069 H HG23 . VAL   A 1 132 ? 197.174 173.734 115.261 1.00 134.89 ? 145  VAL   A HG23 1 
ATOM   2070 N N    . LEU   A 1 133 ? 196.198 169.242 116.292 1.00 123.19 ? 146  LEU   A N    1 
ATOM   2071 C CA   . LEU   A 1 133 ? 195.716 167.894 116.053 1.00 128.52 ? 146  LEU   A CA   1 
ATOM   2072 C C    . LEU   A 1 133 ? 194.997 167.869 114.706 1.00 129.34 ? 146  LEU   A C    1 
ATOM   2073 O O    . LEU   A 1 133 ? 193.865 168.336 114.595 1.00 133.48 ? 146  LEU   A O    1 
ATOM   2074 C CB   . LEU   A 1 133 ? 194.796 167.513 117.218 1.00 128.49 ? 146  LEU   A CB   1 
ATOM   2075 C CG   . LEU   A 1 133 ? 194.358 166.050 117.175 1.00 128.78 ? 146  LEU   A CG   1 
ATOM   2076 C CD1  . LEU   A 1 133 ? 195.509 165.142 117.595 1.00 130.16 ? 146  LEU   A CD1  1 
ATOM   2077 C CD2  . LEU   A 1 133 ? 193.207 165.835 118.144 1.00 125.53 ? 146  LEU   A CD2  1 
ATOM   2078 H H    . LEU   A 1 133 ? 195.517 169.913 116.618 1.00 128.23 ? 146  LEU   A H    1 
ATOM   2079 H HA   . LEU   A 1 133 ? 196.558 167.202 116.019 1.00 128.70 ? 146  LEU   A HA   1 
ATOM   2080 H HB2  . LEU   A 1 133 ? 195.305 167.697 118.164 1.00 128.45 ? 146  LEU   A HB2  1 
ATOM   2081 H HB3  . LEU   A 1 133 ? 193.910 168.148 117.190 1.00 128.63 ? 146  LEU   A HB3  1 
ATOM   2082 H HG   . LEU   A 1 133 ? 194.024 165.781 116.173 1.00 129.10 ? 146  LEU   A HG   1 
ATOM   2083 H HD11 . LEU   A 1 133 ? 196.299 165.162 116.844 1.00 128.74 ? 146  LEU   A HD11 1 
ATOM   2084 H HD12 . LEU   A 1 133 ? 195.912 165.473 118.553 1.00 127.84 ? 146  LEU   A HD12 1 
ATOM   2085 H HD13 . LEU   A 1 133 ? 195.154 164.117 117.701 1.00 129.54 ? 146  LEU   A HD13 1 
ATOM   2086 H HD21 . LEU   A 1 133 ? 192.375 166.486 117.879 1.00 128.49 ? 146  LEU   A HD21 1 
ATOM   2087 H HD22 . LEU   A 1 133 ? 193.527 166.055 119.163 1.00 128.04 ? 146  LEU   A HD22 1 
ATOM   2088 H HD23 . LEU   A 1 133 ? 192.873 164.799 118.078 1.00 128.47 ? 146  LEU   A HD23 1 
ATOM   2089 N N    . GLU   A 1 134 ? 195.659 167.376 113.667 1.00 140.65 ? 147  GLU   A N    1 
ATOM   2090 C CA   . GLU   A 1 134 ? 195.039 167.195 112.357 1.00 139.56 ? 147  GLU   A CA   1 
ATOM   2091 C C    . GLU   A 1 134 ? 194.203 165.921 112.355 1.00 136.72 ? 147  GLU   A C    1 
ATOM   2092 O O    . GLU   A 1 134 ? 194.697 164.849 112.704 1.00 141.35 ? 147  GLU   A O    1 
ATOM   2093 C CB   . GLU   A 1 134 ? 196.109 167.160 111.260 1.00 143.30 ? 147  GLU   A CB   1 
ATOM   2094 C CG   . GLU   A 1 134 ? 195.507 166.899 109.871 1.00 149.31 ? 147  GLU   A CG   1 
ATOM   2095 C CD   . GLU   A 1 134 ? 196.556 166.933 108.750 1.00 155.03 ? 147  GLU   A CD   1 
ATOM   2096 O OE1  . GLU   A 1 134 ? 197.692 166.454 108.960 1.00 154.51 ? 147  GLU   A OE1  1 
ATOM   2097 O OE2  . GLU   A 1 134 ? 196.236 167.405 107.636 1.00 153.91 ? 147  GLU   A OE2  1 
ATOM   2098 H H    . GLU   A 1 134 ? 196.548 166.924 113.827 1.00 142.89 ? 147  GLU   A H    1 
ATOM   2099 H HA   . GLU   A 1 134 ? 194.376 168.035 112.151 1.00 143.64 ? 147  GLU   A HA   1 
ATOM   2100 H HB2  . GLU   A 1 134 ? 196.626 168.119 111.242 1.00 143.64 ? 147  GLU   A HB2  1 
ATOM   2101 H HB3  . GLU   A 1 134 ? 196.827 166.373 111.491 1.00 142.87 ? 147  GLU   A HB3  1 
ATOM   2102 H HG2  . GLU   A 1 134 ? 195.033 165.918 109.865 1.00 144.08 ? 147  GLU   A HG2  1 
ATOM   2103 H HG3  . GLU   A 1 134 ? 194.733 167.642 109.679 1.00 144.72 ? 147  GLU   A HG3  1 
ATOM   2104 N N    . ILE   A 1 135 ? 192.949 166.022 111.926 1.00 120.19 ? 148  ILE   A N    1 
ATOM   2105 C CA   . ILE   A 1 135 ? 192.053 164.880 111.787 1.00 119.12 ? 148  ILE   A CA   1 
ATOM   2106 C C    . ILE   A 1 135 ? 191.488 164.854 110.377 1.00 122.92 ? 148  ILE   A C    1 
ATOM   2107 O O    . ILE   A 1 135 ? 190.959 165.851 109.886 1.00 130.57 ? 148  ILE   A O    1 
ATOM   2108 C CB   . ILE   A 1 135 ? 190.937 164.906 112.842 1.00 115.12 ? 148  ILE   A CB   1 
ATOM   2109 C CG1  . ILE   A 1 135 ? 191.547 164.934 114.257 1.00 122.31 ? 148  ILE   A CG1  1 
ATOM   2110 C CG2  . ILE   A 1 135 ? 190.026 163.688 112.630 1.00 114.47 ? 148  ILE   A CG2  1 
ATOM   2111 C CD1  . ILE   A 1 135 ? 190.545 164.757 115.400 1.00 129.01 ? 148  ILE   A CD1  1 
ATOM   2112 H H    . ILE   A 1 135 ? 192.595 166.926 111.646 1.00 125.22 ? 148  ILE   A H    1 
ATOM   2113 H HA   . ILE   A 1 135 ? 192.619 163.960 111.932 1.00 124.68 ? 148  ILE   A HA   1 
ATOM   2114 H HB   . ILE   A 1 135 ? 190.338 165.807 112.709 1.00 123.74 ? 148  ILE   A HB   1 
ATOM   2115 H HG12 . ILE   A 1 135 ? 192.302 164.152 114.335 1.00 124.26 ? 148  ILE   A HG12 1 
ATOM   2116 H HG13 . ILE   A 1 135 ? 192.042 165.894 114.404 1.00 124.77 ? 148  ILE   A HG13 1 
ATOM   2117 H HG21 . ILE   A 1 135 ? 189.238 163.666 113.383 1.00 123.23 ? 148  ILE   A HG21 1 
ATOM   2118 H HG22 . ILE   A 1 135 ? 190.606 162.767 112.688 1.00 123.28 ? 148  ILE   A HG22 1 
ATOM   2119 H HG23 . ILE   A 1 135 ? 189.527 163.739 111.662 1.00 123.48 ? 148  ILE   A HG23 1 
ATOM   2120 H HD11 . ILE   A 1 135 ? 191.033 164.992 116.346 1.00 125.37 ? 148  ILE   A HD11 1 
ATOM   2121 H HD12 . ILE   A 1 135 ? 189.695 165.426 115.264 1.00 125.27 ? 148  ILE   A HD12 1 
ATOM   2122 H HD13 . ILE   A 1 135 ? 190.201 163.724 115.443 1.00 124.89 ? 148  ILE   A HD13 1 
ATOM   2123 N N    . THR   A 1 136 ? 191.540 163.694 109.735 1.00 131.40 ? 149  THR   A N    1 
ATOM   2124 C CA   . THR   A 1 136 ? 191.007 163.494 108.386 1.00 134.83 ? 149  THR   A CA   1 
ATOM   2125 C C    . THR   A 1 136 ? 190.317 162.148 108.261 1.00 134.14 ? 149  THR   A C    1 
ATOM   2126 O O    . THR   A 1 136 ? 190.551 161.239 109.053 1.00 139.91 ? 149  THR   A O    1 
ATOM   2127 C CB   . THR   A 1 136 ? 192.099 163.591 107.320 1.00 133.40 ? 149  THR   A CB   1 
ATOM   2128 O OG1  . THR   A 1 136 ? 193.055 162.589 107.511 1.00 133.76 ? 149  THR   A OG1  1 
ATOM   2129 C CG2  . THR   A 1 136 ? 192.833 164.924 107.318 1.00 131.96 ? 149  THR   A CG2  1 
ATOM   2130 H H    . THR   A 1 136 ? 191.989 162.908 110.183 1.00 133.38 ? 149  THR   A H    1 
ATOM   2131 H HA   . THR   A 1 136 ? 190.263 164.261 108.173 1.00 134.16 ? 149  THR   A HA   1 
ATOM   2132 H HB   . THR   A 1 136 ? 191.640 163.453 106.341 1.00 133.80 ? 149  THR   A HB   1 
ATOM   2133 H HG1  . THR   A 1 136 ? 193.573 162.539 106.705 1.00 134.00 ? 149  THR   A HG1  1 
ATOM   2134 H HG21 . THR   A 1 136 ? 193.499 164.977 106.457 1.00 133.59 ? 149  THR   A HG21 1 
ATOM   2135 H HG22 . THR   A 1 136 ? 193.416 165.041 108.231 1.00 133.95 ? 149  THR   A HG22 1 
ATOM   2136 H HG23 . THR   A 1 136 ? 192.102 165.731 107.254 1.00 133.30 ? 149  THR   A HG23 1 
ATOM   2137 N N    . ALA   A 1 137 ? 189.459 162.014 107.254 1.00 129.93 ? 150  ALA   A N    1 
ATOM   2138 C CA   . ALA   A 1 137 ? 188.829 160.757 106.888 1.00 130.24 ? 150  ALA   A CA   1 
ATOM   2139 C C    . ALA   A 1 137 ? 188.747 160.666 105.368 1.00 131.50 ? 150  ALA   A C    1 
ATOM   2140 O O    . ALA   A 1 137 ? 187.923 161.339 104.748 1.00 139.72 ? 150  ALA   A O    1 
ATOM   2141 C CB   . ALA   A 1 137 ? 187.455 160.674 107.549 1.00 132.76 ? 150  ALA   A CB   1 
ATOM   2142 H H    . ALA   A 1 137 ? 189.257 162.822 106.683 1.00 134.04 ? 150  ALA   A H    1 
ATOM   2143 H HA   . ALA   A 1 137 ? 189.434 159.927 107.253 1.00 133.57 ? 150  ALA   A HA   1 
ATOM   2144 H HB1  . ALA   A 1 137 ? 187.026 159.687 107.378 1.00 134.14 ? 150  ALA   A HB1  1 
ATOM   2145 H HB2  . ALA   A 1 137 ? 187.548 160.844 108.622 1.00 133.59 ? 150  ALA   A HB2  1 
ATOM   2146 H HB3  . ALA   A 1 137 ? 186.790 161.426 107.125 1.00 133.62 ? 150  ALA   A HB3  1 
ATOM   2147 N N    . CYS   A 1 138 ? 189.624 159.877 104.758 1.00 142.90 ? 151  CYS   A N    1 
ATOM   2148 C CA   . CYS   A 1 138 ? 189.843 159.891 103.315 1.00 147.39 ? 151  CYS   A CA   1 
ATOM   2149 C C    . CYS   A 1 138 ? 190.087 158.494 102.763 1.00 148.25 ? 151  CYS   A C    1 
ATOM   2150 O O    . CYS   A 1 138 ? 190.414 157.564 103.499 1.00 152.92 ? 151  CYS   A O    1 
ATOM   2151 C CB   . CYS   A 1 138 ? 191.032 160.791 102.973 1.00 151.56 ? 151  CYS   A CB   1 
ATOM   2152 S SG   . CYS   A 1 138 ? 191.003 162.446 103.695 1.00 177.65 ? 151  CYS   A SG   1 
ATOM   2153 H H    . CYS   A 1 138 ? 190.237 159.305 105.322 1.00 148.85 ? 151  CYS   A H    1 
ATOM   2154 H HA   . CYS   A 1 138 ? 188.955 160.283 102.819 1.00 149.92 ? 151  CYS   A HA   1 
ATOM   2155 H HB2  . CYS   A 1 138 ? 191.942 160.297 103.311 1.00 150.28 ? 151  CYS   A HB2  1 
ATOM   2156 H HB3  . CYS   A 1 138 ? 191.105 160.894 101.890 1.00 150.83 ? 151  CYS   A HB3  1 
ATOM   2157 N N    . GLN   A 1 139 ? 189.956 158.340 101.452 1.00 142.83 ? 152  GLN   A N    1 
ATOM   2158 C CA   . GLN   A 1 139 ? 190.309 157.112 100.752 1.00 145.59 ? 152  GLN   A CA   1 
ATOM   2159 C C    . GLN   A 1 139 ? 191.830 156.976 100.584 1.00 144.86 ? 152  GLN   A C    1 
ATOM   2160 O O    . GLN   A 1 139 ? 192.339 156.909 99.470  1.00 146.08 ? 152  GLN   A O    1 
ATOM   2161 C CB   . GLN   A 1 139 ? 189.560 157.045 99.417  1.00 148.79 ? 152  GLN   A CB   1 
ATOM   2162 C CG   . GLN   A 1 139 ? 188.037 157.039 99.594  1.00 149.65 ? 152  GLN   A CG   1 
ATOM   2163 C CD   . GLN   A 1 139 ? 187.313 156.356 98.440  1.00 150.66 ? 152  GLN   A CD   1 
ATOM   2164 O OE1  . GLN   A 1 139 ? 186.516 155.449 98.626  1.00 150.12 ? 152  GLN   A OE1  1 
ATOM   2165 N NE2  . GLN   A 1 139 ? 187.570 156.732 97.207  1.00 148.78 ? 152  GLN   A NE2  1 
ATOM   2166 H H    . GLN   A 1 139 ? 189.658 159.136 100.906 1.00 145.95 ? 152  GLN   A H    1 
ATOM   2167 H HA   . GLN   A 1 139 ? 189.986 156.264 101.356 1.00 145.98 ? 152  GLN   A HA   1 
ATOM   2168 H HB2  . GLN   A 1 139 ? 189.852 157.881 98.780  1.00 146.48 ? 152  GLN   A HB2  1 
ATOM   2169 H HB3  . GLN   A 1 139 ? 189.854 156.115 98.931  1.00 146.15 ? 152  GLN   A HB3  1 
ATOM   2170 H HG2  . GLN   A 1 139 ? 187.780 156.516 100.515 1.00 145.70 ? 152  GLN   A HG2  1 
ATOM   2171 H HG3  . GLN   A 1 139 ? 187.690 158.070 99.666  1.00 146.37 ? 152  GLN   A HG3  1 
ATOM   2172 H HE21 . GLN   A 1 139 ? 188.265 157.439 97.017  1.00 146.22 ? 152  GLN   A HE21 1 
ATOM   2173 H HE22 . GLN   A 1 139 ? 187.100 156.247 96.457  1.00 146.44 ? 152  GLN   A HE22 1 
ATOM   2174 N N    . TYR   A 1 140 ? 192.576 156.978 101.685 1.00 134.30 ? 153  TYR   A N    1 
ATOM   2175 C CA   . TYR   A 1 140 ? 194.034 156.906 101.659 1.00 135.99 ? 153  TYR   A CA   1 
ATOM   2176 C C    . TYR   A 1 140 ? 194.552 155.586 101.093 1.00 136.28 ? 153  TYR   A C    1 
ATOM   2177 O O    . TYR   A 1 140 ? 194.112 154.509 101.489 1.00 137.48 ? 153  TYR   A O    1 
ATOM   2178 C CB   . TYR   A 1 140 ? 194.594 157.087 103.070 1.00 136.09 ? 153  TYR   A CB   1 
ATOM   2179 C CG   . TYR   A 1 140 ? 194.488 158.496 103.603 1.00 134.97 ? 153  TYR   A CG   1 
ATOM   2180 C CD1  . TYR   A 1 140 ? 195.192 159.521 102.955 1.00 134.70 ? 153  TYR   A CD1  1 
ATOM   2181 C CD2  . TYR   A 1 140 ? 193.731 158.778 104.751 1.00 133.76 ? 153  TYR   A CD2  1 
ATOM   2182 C CE1  . TYR   A 1 140 ? 195.145 160.832 103.451 1.00 137.15 ? 153  TYR   A CE1  1 
ATOM   2183 C CE2  . TYR   A 1 140 ? 193.685 160.088 105.255 1.00 134.33 ? 153  TYR   A CE2  1 
ATOM   2184 C CZ   . TYR   A 1 140 ? 194.391 161.117 104.604 1.00 139.22 ? 153  TYR   A CZ   1 
ATOM   2185 O OH   . TYR   A 1 140 ? 194.356 162.385 105.088 1.00 143.08 ? 153  TYR   A OH   1 
ATOM   2186 H H    . TYR   A 1 140 ? 192.111 157.042 102.579 1.00 137.07 ? 153  TYR   A H    1 
ATOM   2187 H HA   . TYR   A 1 140 ? 194.407 157.713 101.029 1.00 137.07 ? 153  TYR   A HA   1 
ATOM   2188 H HB2  . TYR   A 1 140 ? 194.097 156.394 103.749 1.00 136.76 ? 153  TYR   A HB2  1 
ATOM   2189 H HB3  . TYR   A 1 140 ? 195.652 156.824 103.061 1.00 136.75 ? 153  TYR   A HB3  1 
ATOM   2190 H HD1  . TYR   A 1 140 ? 195.777 159.300 102.075 1.00 136.70 ? 153  TYR   A HD1  1 
ATOM   2191 H HD2  . TYR   A 1 140 ? 193.196 157.990 105.259 1.00 136.72 ? 153  TYR   A HD2  1 
ATOM   2192 H HE1  . TYR   A 1 140 ? 195.694 161.616 102.951 1.00 136.99 ? 153  TYR   A HE1  1 
ATOM   2193 H HE2  . TYR   A 1 140 ? 193.114 160.306 106.146 1.00 136.49 ? 153  TYR   A HE2  1 
ATOM   2194 H HH   . TYR   A 1 140 ? 194.877 162.973 104.536 1.00 137.59 ? 153  TYR   A HH   1 
ATOM   2195 N N    . THR   A 1 141 ? 195.562 155.653 100.234 1.00 135.51 ? 154  THR   A N    1 
ATOM   2196 C CA   . THR   A 1 141 ? 196.373 154.502 99.833  1.00 133.59 ? 154  THR   A CA   1 
ATOM   2197 C C    . THR   A 1 141 ? 197.378 154.201 100.938 1.00 136.89 ? 154  THR   A C    1 
ATOM   2198 O O    . THR   A 1 141 ? 198.523 154.641 100.882 1.00 142.23 ? 154  THR   A O    1 
ATOM   2199 C CB   . THR   A 1 141 ? 197.072 154.772 98.494  1.00 137.97 ? 154  THR   A CB   1 
ATOM   2200 O OG1  . THR   A 1 141 ? 196.113 155.068 97.509  1.00 145.54 ? 154  THR   A OG1  1 
ATOM   2201 C CG2  . THR   A 1 141 ? 197.849 153.562 97.987  1.00 138.67 ? 154  THR   A CG2  1 
ATOM   2202 H H    . THR   A 1 141 ? 195.854 156.568 99.923  1.00 138.79 ? 154  THR   A H    1 
ATOM   2203 H HA   . THR   A 1 141 ? 195.736 153.627 99.709  1.00 138.12 ? 154  THR   A HA   1 
ATOM   2204 H HB   . THR   A 1 141 ? 197.747 155.622 98.592  1.00 138.77 ? 154  THR   A HB   1 
ATOM   2205 H HG1  . THR   A 1 141 ? 196.059 156.026 97.509  1.00 139.70 ? 154  THR   A HG1  1 
ATOM   2206 H HG21 . THR   A 1 141 ? 198.229 153.768 96.987  1.00 139.17 ? 154  THR   A HG21 1 
ATOM   2207 H HG22 . THR   A 1 141 ? 198.703 153.373 98.638  1.00 138.31 ? 154  THR   A HG22 1 
ATOM   2208 H HG23 . THR   A 1 141 ? 197.206 152.682 97.960  1.00 139.05 ? 154  THR   A HG23 1 
ATOM   2209 N N    . MET   A 1 142 ? 196.942 153.509 101.990 1.00 134.67 ? 155  MET   A N    1 
ATOM   2210 C CA   . MET   A 1 142 ? 197.787 153.177 103.141 1.00 132.32 ? 155  MET   A CA   1 
ATOM   2211 C C    . MET   A 1 142 ? 198.943 152.249 102.757 1.00 133.01 ? 155  MET   A C    1 
ATOM   2212 O O    . MET   A 1 142 ? 198.777 151.327 101.960 1.00 137.10 ? 155  MET   A O    1 
ATOM   2213 C CB   . MET   A 1 142 ? 196.960 152.504 104.240 1.00 133.76 ? 155  MET   A CB   1 
ATOM   2214 C CG   . MET   A 1 142 ? 195.870 153.403 104.830 1.00 137.73 ? 155  MET   A CG   1 
ATOM   2215 S SD   . MET   A 1 142 ? 196.458 154.875 105.689 1.00 140.83 ? 155  MET   A SD   1 
ATOM   2216 C CE   . MET   A 1 142 ? 197.419 154.133 107.029 1.00 138.65 ? 155  MET   A CE   1 
ATOM   2217 H H    . MET   A 1 142 ? 195.974 153.224 102.007 1.00 135.77 ? 155  MET   A H    1 
ATOM   2218 H HA   . MET   A 1 142 ? 198.206 154.099 103.544 1.00 135.56 ? 155  MET   A HA   1 
ATOM   2219 H HB2  . MET   A 1 142 ? 196.485 151.614 103.825 1.00 135.50 ? 155  MET   A HB2  1 
ATOM   2220 H HB3  . MET   A 1 142 ? 197.622 152.175 105.041 1.00 135.41 ? 155  MET   A HB3  1 
ATOM   2221 H HG2  . MET   A 1 142 ? 195.196 153.716 104.033 1.00 136.20 ? 155  MET   A HG2  1 
ATOM   2222 H HG3  . MET   A 1 142 ? 195.288 152.817 105.541 1.00 135.51 ? 155  MET   A HG3  1 
ATOM   2223 H HE1  . MET   A 1 142 ? 197.778 154.921 107.691 1.00 136.38 ? 155  MET   A HE1  1 
ATOM   2224 H HE2  . MET   A 1 142 ? 198.280 153.603 106.621 1.00 136.33 ? 155  MET   A HE2  1 
ATOM   2225 H HE3  . MET   A 1 142 ? 196.793 153.442 107.593 1.00 135.87 ? 155  MET   A HE3  1 
ATOM   2226 N N    . CYS   A 1 143 ? 200.109 152.451 103.360 1.00 144.08 ? 156  CYS   A N    1 
ATOM   2227 C CA   . CYS   A 1 143 ? 201.267 151.586 103.154 1.00 146.56 ? 156  CYS   A CA   1 
ATOM   2228 C C    . CYS   A 1 143 ? 201.102 150.193 103.778 1.00 144.74 ? 156  CYS   A C    1 
ATOM   2229 O O    . CYS   A 1 143 ? 200.320 149.997 104.705 1.00 147.38 ? 156  CYS   A O    1 
ATOM   2230 C CB   . CYS   A 1 143 ? 202.500 152.262 103.751 1.00 151.01 ? 156  CYS   A CB   1 
ATOM   2231 S SG   . CYS   A 1 143 ? 202.913 153.850 103.005 1.00 169.13 ? 156  CYS   A SG   1 
ATOM   2232 H H    . CYS   A 1 143 ? 200.194 153.230 103.999 1.00 148.65 ? 156  CYS   A H    1 
ATOM   2233 H HA   . CYS   A 1 143 ? 201.426 151.461 102.082 1.00 149.27 ? 156  CYS   A HA   1 
ATOM   2234 H HB2  . CYS   A 1 143 ? 202.333 152.414 104.818 1.00 149.55 ? 156  CYS   A HB2  1 
ATOM   2235 H HB3  . CYS   A 1 143 ? 203.361 151.605 103.633 1.00 149.57 ? 156  CYS   A HB3  1 
ATOM   2236 N N    . GLU   A 1 144 ? 201.917 149.229 103.349 1.00 141.45 ? 157  GLU   A N    1 
ATOM   2237 C CA   . GLU   A 1 144 ? 202.062 147.946 104.049 1.00 142.32 ? 157  GLU   A CA   1 
ATOM   2238 C C    . GLU   A 1 144 ? 202.582 148.123 105.478 1.00 146.06 ? 157  GLU   A C    1 
ATOM   2239 O O    . GLU   A 1 144 ? 202.046 147.511 106.402 1.00 153.00 ? 157  GLU   A O    1 
ATOM   2240 C CB   . GLU   A 1 144 ? 203.032 147.032 103.288 1.00 144.96 ? 157  GLU   A CB   1 
ATOM   2241 C CG   . GLU   A 1 144 ? 202.375 146.414 102.053 1.00 150.59 ? 157  GLU   A CG   1 
ATOM   2242 C CD   . GLU   A 1 144 ? 203.312 145.431 101.337 1.00 153.20 ? 157  GLU   A CD   1 
ATOM   2243 O OE1  . GLU   A 1 144 ? 204.487 145.775 101.088 1.00 150.93 ? 157  GLU   A OE1  1 
ATOM   2244 O OE2  . GLU   A 1 144 ? 202.872 144.304 101.016 1.00 154.03 ? 157  GLU   A OE2  1 
ATOM   2245 H H    . GLU   A 1 144 ? 202.443 149.382 102.501 1.00 146.98 ? 157  GLU   A H    1 
ATOM   2246 H HA   . GLU   A 1 144 ? 201.090 147.457 104.116 1.00 146.07 ? 157  GLU   A HA   1 
ATOM   2247 H HB2  . GLU   A 1 144 ? 203.918 147.598 103.002 1.00 146.39 ? 157  GLU   A HB2  1 
ATOM   2248 H HB3  . GLU   A 1 144 ? 203.340 146.220 103.947 1.00 146.63 ? 157  GLU   A HB3  1 
ATOM   2249 H HG2  . GLU   A 1 144 ? 201.473 145.892 102.373 1.00 147.64 ? 157  GLU   A HG2  1 
ATOM   2250 H HG3  . GLU   A 1 144 ? 202.082 147.206 101.365 1.00 147.08 ? 157  GLU   A HG3  1 
ATOM   2251 N N    . TYR   A 1 145 ? 203.587 148.983 105.653 1.00 129.83 ? 158  TYR   A N    1 
ATOM   2252 C CA   . TYR   A 1 145 ? 204.286 149.240 106.911 1.00 131.47 ? 158  TYR   A CA   1 
ATOM   2253 C C    . TYR   A 1 145 ? 204.271 150.744 107.234 1.00 127.84 ? 158  TYR   A C    1 
ATOM   2254 O O    . TYR   A 1 145 ? 205.281 151.426 107.071 1.00 126.27 ? 158  TYR   A O    1 
ATOM   2255 C CB   . TYR   A 1 145 ? 205.721 148.701 106.799 1.00 129.58 ? 158  TYR   A CB   1 
ATOM   2256 C CG   . TYR   A 1 145 ? 205.866 147.257 106.369 1.00 131.52 ? 158  TYR   A CG   1 
ATOM   2257 C CD1  . TYR   A 1 145 ? 205.078 146.249 106.949 1.00 132.35 ? 158  TYR   A CD1  1 
ATOM   2258 C CD2  . TYR   A 1 145 ? 206.817 146.923 105.389 1.00 130.55 ? 158  TYR   A CD2  1 
ATOM   2259 C CE1  . TYR   A 1 145 ? 205.240 144.909 106.556 1.00 128.46 ? 158  TYR   A CE1  1 
ATOM   2260 C CE2  . TYR   A 1 145 ? 206.968 145.588 104.979 1.00 131.74 ? 158  TYR   A CE2  1 
ATOM   2261 C CZ   . TYR   A 1 145 ? 206.178 144.580 105.559 1.00 132.57 ? 158  TYR   A CZ   1 
ATOM   2262 O OH   . TYR   A 1 145 ? 206.331 143.294 105.156 1.00 140.40 ? 158  TYR   A OH   1 
ATOM   2263 H H    . TYR   A 1 145 ? 203.967 149.415 104.822 1.00 131.40 ? 158  TYR   A H    1 
ATOM   2264 H HA   . TYR   A 1 145 ? 203.790 148.714 107.727 1.00 132.26 ? 158  TYR   A HA   1 
ATOM   2265 H HB2  . TYR   A 1 145 ? 206.266 149.317 106.083 1.00 131.08 ? 158  TYR   A HB2  1 
ATOM   2266 H HB3  . TYR   A 1 145 ? 206.213 148.817 107.766 1.00 131.45 ? 158  TYR   A HB3  1 
ATOM   2267 H HD1  . TYR   A 1 145 ? 204.347 146.504 107.702 1.00 132.32 ? 158  TYR   A HD1  1 
ATOM   2268 H HD2  . TYR   A 1 145 ? 207.432 147.690 104.943 1.00 132.14 ? 158  TYR   A HD2  1 
ATOM   2269 H HE1  . TYR   A 1 145 ? 204.648 144.134 107.019 1.00 131.30 ? 158  TYR   A HE1  1 
ATOM   2270 H HE2  . TYR   A 1 145 ? 207.690 145.327 104.219 1.00 132.10 ? 158  TYR   A HE2  1 
ATOM   2271 H HH   . TYR   A 1 145 ? 205.644 142.722 105.506 1.00 132.69 ? 158  TYR   A HH   1 
ATOM   2272 N N    . PRO   A 1 146 ? 203.125 151.320 107.622 1.00 123.48 ? 159  PRO   A N    1 
ATOM   2273 C CA   . PRO   A 1 146 ? 203.009 152.750 107.865 1.00 124.69 ? 159  PRO   A CA   1 
ATOM   2274 C C    . PRO   A 1 146 ? 203.771 153.174 109.118 1.00 128.06 ? 159  PRO   A C    1 
ATOM   2275 O O    . PRO   A 1 146 ? 203.844 152.416 110.080 1.00 136.49 ? 159  PRO   A O    1 
ATOM   2276 C CB   . PRO   A 1 146 ? 201.511 153.007 108.015 1.00 124.06 ? 159  PRO   A CB   1 
ATOM   2277 C CG   . PRO   A 1 146 ? 200.976 151.685 108.545 1.00 123.52 ? 159  PRO   A CG   1 
ATOM   2278 C CD   . PRO   A 1 146 ? 201.858 150.658 107.846 1.00 127.54 ? 159  PRO   A CD   1 
ATOM   2279 H HA   . PRO   A 1 146 ? 203.396 153.305 107.011 1.00 128.69 ? 159  PRO   A HA   1 
ATOM   2280 H HB2  . PRO   A 1 146 ? 201.295 153.830 108.696 1.00 128.04 ? 159  PRO   A HB2  1 
ATOM   2281 H HB3  . PRO   A 1 146 ? 201.072 153.198 107.035 1.00 129.64 ? 159  PRO   A HB3  1 
ATOM   2282 H HG2  . PRO   A 1 146 ? 201.137 151.625 109.621 1.00 128.54 ? 159  PRO   A HG2  1 
ATOM   2283 H HG3  . PRO   A 1 146 ? 199.922 151.553 108.304 1.00 128.53 ? 159  PRO   A HG3  1 
ATOM   2284 H HD2  . PRO   A 1 146 ? 201.970 149.769 108.466 1.00 129.57 ? 159  PRO   A HD2  1 
ATOM   2285 H HD3  . PRO   A 1 146 ? 201.416 150.391 106.886 1.00 130.19 ? 159  PRO   A HD3  1 
ATOM   2286 N N    . HIS   A 1 147 ? 204.299 154.393 109.159 1.00 127.21 ? 160  HIS   A N    1 
ATOM   2287 C CA   . HIS   A 1 147 ? 204.872 154.978 110.372 1.00 126.13 ? 160  HIS   A CA   1 
ATOM   2288 C C    . HIS   A 1 147 ? 204.971 156.502 110.265 1.00 128.04 ? 160  HIS   A C    1 
ATOM   2289 O O    . HIS   A 1 147 ? 204.846 157.070 109.185 1.00 138.74 ? 160  HIS   A O    1 
ATOM   2290 C CB   . HIS   A 1 147 ? 206.252 154.376 110.640 1.00 128.82 ? 160  HIS   A CB   1 
ATOM   2291 C CG   . HIS   A 1 147 ? 207.286 154.898 109.702 1.00 123.19 ? 160  HIS   A CG   1 
ATOM   2292 N ND1  . HIS   A 1 147 ? 207.958 156.082 109.844 1.00 125.75 ? 160  HIS   A ND1  1 
ATOM   2293 C CD2  . HIS   A 1 147 ? 207.609 154.380 108.483 1.00 123.14 ? 160  HIS   A CD2  1 
ATOM   2294 C CE1  . HIS   A 1 147 ? 208.697 156.265 108.744 1.00 128.49 ? 160  HIS   A CE1  1 
ATOM   2295 N NE2  . HIS   A 1 147 ? 208.527 155.245 107.889 1.00 126.68 ? 160  HIS   A NE2  1 
ATOM   2296 H H    . HIS   A 1 147 ? 204.289 154.965 108.327 1.00 129.71 ? 160  HIS   A H    1 
ATOM   2297 H HA   . HIS   A 1 147 ? 204.225 154.740 111.217 1.00 129.53 ? 160  HIS   A HA   1 
ATOM   2298 H HB2  . HIS   A 1 147 ? 206.560 154.624 111.656 1.00 130.30 ? 160  HIS   A HB2  1 
ATOM   2299 H HB3  . HIS   A 1 147 ? 206.219 153.288 110.570 1.00 130.85 ? 160  HIS   A HB3  1 
ATOM   2300 H HD1  . HIS   A 1 147 ? 207.850 156.738 110.604 1.00 129.88 ? 160  HIS   A HD1  1 
ATOM   2301 H HD2  . HIS   A 1 147 ? 207.200 153.480 108.048 1.00 129.03 ? 160  HIS   A HD2  1 
ATOM   2302 H HE1  . HIS   A 1 147 ? 209.346 157.111 108.576 1.00 129.93 ? 160  HIS   A HE1  1 
ATOM   2303 N N    . THR   A 1 148 ? 205.244 157.174 111.379 1.00 129.65 ? 161  THR   A N    1 
ATOM   2304 C CA   . THR   A 1 148 ? 205.484 158.629 111.435 1.00 131.06 ? 161  THR   A CA   1 
ATOM   2305 C C    . THR   A 1 148 ? 206.901 158.950 111.914 1.00 131.45 ? 161  THR   A C    1 
ATOM   2306 O O    . THR   A 1 148 ? 207.688 158.029 112.169 1.00 138.36 ? 161  THR   A O    1 
ATOM   2307 C CB   . THR   A 1 148 ? 204.428 159.313 112.305 1.00 132.58 ? 161  THR   A CB   1 
ATOM   2308 O OG1  . THR   A 1 148 ? 204.481 158.812 113.618 1.00 141.37 ? 161  THR   A OG1  1 
ATOM   2309 C CG2  . THR   A 1 148 ? 203.023 159.077 111.768 1.00 129.13 ? 161  THR   A CG2  1 
ATOM   2310 H H    . THR   A 1 148 ? 205.360 156.639 112.228 1.00 133.19 ? 161  THR   A H    1 
ATOM   2311 H HA   . THR   A 1 148 ? 205.394 159.057 110.437 1.00 133.16 ? 161  THR   A HA   1 
ATOM   2312 H HB   . THR   A 1 148 ? 204.616 160.387 112.329 1.00 133.12 ? 161  THR   A HB   1 
ATOM   2313 H HG1  . THR   A 1 148 ? 204.218 157.889 113.594 1.00 134.12 ? 161  THR   A HG1  1 
ATOM   2314 H HG21 . THR   A 1 148 ? 202.316 159.687 112.331 1.00 132.09 ? 161  THR   A HG21 1 
ATOM   2315 H HG22 . THR   A 1 148 ? 202.745 158.026 111.847 1.00 132.03 ? 161  THR   A HG22 1 
ATOM   2316 H HG23 . THR   A 1 148 ? 202.979 159.381 110.722 1.00 132.82 ? 161  THR   A HG23 1 
ATOM   2317 N N    . ILE   A 1 149 ? 207.266 160.229 112.008 1.00 140.93 ? 162  ILE   A N    1 
ATOM   2318 C CA   . ILE   A 1 149 ? 208.584 160.678 112.483 1.00 145.25 ? 162  ILE   A CA   1 
ATOM   2319 C C    . ILE   A 1 149 ? 208.500 161.762 113.561 1.00 148.52 ? 162  ILE   A C    1 
ATOM   2320 O O    . ILE   A 1 149 ? 207.568 162.560 113.584 1.00 147.63 ? 162  ILE   A O    1 
ATOM   2321 C CB   . ILE   A 1 149 ? 209.490 161.143 111.322 1.00 146.26 ? 162  ILE   A CB   1 
ATOM   2322 C CG1  . ILE   A 1 149 ? 209.081 162.510 110.738 1.00 149.34 ? 162  ILE   A CG1  1 
ATOM   2323 C CG2  . ILE   A 1 149 ? 209.568 160.065 110.238 1.00 146.73 ? 162  ILE   A CG2  1 
ATOM   2324 C CD1  . ILE   A 1 149 ? 210.001 163.018 109.622 1.00 147.99 ? 162  ILE   A CD1  1 
ATOM   2325 H H    . ILE   A 1 149 ? 206.621 160.928 111.668 1.00 146.78 ? 162  ILE   A H    1 
ATOM   2326 H HA   . ILE   A 1 149 ? 209.082 159.826 112.946 1.00 147.60 ? 162  ILE   A HA   1 
ATOM   2327 H HB   . ILE   A 1 149 ? 210.494 161.260 111.729 1.00 147.56 ? 162  ILE   A HB   1 
ATOM   2328 H HG12 . ILE   A 1 149 ? 208.062 162.455 110.355 1.00 147.79 ? 162  ILE   A HG12 1 
ATOM   2329 H HG13 . ILE   A 1 149 ? 209.107 163.263 111.526 1.00 148.05 ? 162  ILE   A HG13 1 
ATOM   2330 H HG21 . ILE   A 1 149 ? 210.350 160.311 109.519 1.00 147.67 ? 162  ILE   A HG21 1 
ATOM   2331 H HG22 . ILE   A 1 149 ? 209.817 159.104 110.690 1.00 147.28 ? 162  ILE   A HG22 1 
ATOM   2332 H HG23 . ILE   A 1 149 ? 208.614 159.986 109.717 1.00 147.41 ? 162  ILE   A HG23 1 
ATOM   2333 H HD11 . ILE   A 1 149 ? 209.723 164.040 109.366 1.00 147.41 ? 162  ILE   A HD11 1 
ATOM   2334 H HD12 . ILE   A 1 149 ? 211.037 163.007 109.960 1.00 147.94 ? 162  ILE   A HD12 1 
ATOM   2335 H HD13 . ILE   A 1 149 ? 209.898 162.400 108.730 1.00 147.63 ? 162  ILE   A HD13 1 
ATOM   2336 N N    . CYS   A 1 150 ? 209.532 161.860 114.398 1.00 169.62 ? 163  CYS   A N    1 
ATOM   2337 C CA   . CYS   A 1 150 ? 209.820 163.076 115.161 1.00 168.14 ? 163  CYS   A CA   1 
ATOM   2338 C C    . CYS   A 1 150 ? 210.181 164.232 114.219 1.00 171.21 ? 163  CYS   A C    1 
ATOM   2339 O O    . CYS   A 1 150 ? 211.339 164.353 113.815 1.00 172.94 ? 163  CYS   A O    1 
ATOM   2340 C CB   . CYS   A 1 150 ? 211.026 162.825 116.073 1.00 171.84 ? 163  CYS   A CB   1 
ATOM   2341 S SG   . CYS   A 1 150 ? 210.702 161.970 117.615 1.00 188.90 ? 163  CYS   A SG   1 
ATOM   2342 H H    . CYS   A 1 150 ? 210.232 161.132 114.385 1.00 170.82 ? 163  CYS   A H    1 
ATOM   2343 H HA   . CYS   A 1 150 ? 208.959 163.359 115.767 1.00 169.90 ? 163  CYS   A HA   1 
ATOM   2344 H HB2  . CYS   A 1 150 ? 211.782 162.272 115.517 1.00 171.34 ? 163  CYS   A HB2  1 
ATOM   2345 H HB3  . CYS   A 1 150 ? 211.468 163.784 116.346 1.00 171.00 ? 163  CYS   A HB3  1 
ATOM   2346 N N    . LYS   A 1 151 ? 209.245 165.124 113.890 1.00 166.08 ? 164  LYS   A N    1 
ATOM   2347 C CA   . LYS   A 1 151 ? 209.579 166.322 113.094 1.00 167.02 ? 164  LYS   A CA   1 
ATOM   2348 C C    . LYS   A 1 151 ? 210.476 167.294 113.869 1.00 166.76 ? 164  LYS   A C    1 
ATOM   2349 O O    . LYS   A 1 151 ? 211.209 168.070 113.262 1.00 163.57 ? 164  LYS   A O    1 
ATOM   2350 C CB   . LYS   A 1 151 ? 208.303 167.004 112.576 1.00 165.05 ? 164  LYS   A CB   1 
ATOM   2351 C CG   . LYS   A 1 151 ? 207.577 166.100 111.570 1.00 167.74 ? 164  LYS   A CG   1 
ATOM   2352 C CD   . LYS   A 1 151 ? 206.347 166.789 110.963 1.00 169.58 ? 164  LYS   A CD   1 
ATOM   2353 C CE   . LYS   A 1 151 ? 205.678 165.919 109.887 1.00 168.86 ? 164  LYS   A CE   1 
ATOM   2354 N NZ   . LYS   A 1 151 ? 204.932 164.766 110.460 1.00 169.28 ? 164  LYS   A NZ   1 
ATOM   2355 H H    . LYS   A 1 151 ? 208.303 164.993 114.229 1.00 164.76 ? 164  LYS   A H    1 
ATOM   2356 H HA   . LYS   A 1 151 ? 210.166 166.016 112.227 1.00 165.48 ? 164  LYS   A HA   1 
ATOM   2357 H HB2  . LYS   A 1 151 ? 207.641 167.240 113.409 1.00 164.62 ? 164  LYS   A HB2  1 
ATOM   2358 H HB3  . LYS   A 1 151 ? 208.576 167.933 112.076 1.00 165.32 ? 164  LYS   A HB3  1 
ATOM   2359 H HG2  . LYS   A 1 151 ? 208.268 165.844 110.766 1.00 165.24 ? 164  LYS   A HG2  1 
ATOM   2360 H HG3  . LYS   A 1 151 ? 207.266 165.183 112.070 1.00 165.37 ? 164  LYS   A HG3  1 
ATOM   2361 H HD2  . LYS   A 1 151 ? 205.631 167.036 111.747 1.00 165.44 ? 164  LYS   A HD2  1 
ATOM   2362 H HD3  . LYS   A 1 151 ? 206.671 167.719 110.495 1.00 165.35 ? 164  LYS   A HD3  1 
ATOM   2363 H HE2  . LYS   A 1 151 ? 204.994 166.549 109.317 1.00 165.01 ? 164  LYS   A HE2  1 
ATOM   2364 H HE3  . LYS   A 1 151 ? 206.447 165.572 109.197 1.00 165.65 ? 164  LYS   A HE3  1 
ATOM   2365 H HZ1  . LYS   A 1 151 ? 204.572 164.162 109.735 1.00 165.42 ? 164  LYS   A HZ1  1 
ATOM   2366 H HZ2  . LYS   A 1 151 ? 205.530 164.185 111.031 1.00 165.44 ? 164  LYS   A HZ2  1 
ATOM   2367 H HZ3  . LYS   A 1 151 ? 204.158 165.086 111.024 1.00 165.03 ? 164  LYS   A HZ3  1 
ATOM   2368 N N    . SER   A 1 152 ? 210.462 167.219 115.200 1.00 159.17 ? 165  SER   A N    1 
ATOM   2369 C CA   . SER   A 1 152 ? 211.261 168.073 116.089 1.00 155.12 ? 165  SER   A CA   1 
ATOM   2370 C C    . SER   A 1 152 ? 212.744 167.684 116.089 1.00 153.76 ? 165  SER   A C    1 
ATOM   2371 O O    . SER   A 1 152 ? 213.599 168.463 115.675 1.00 152.00 ? 165  SER   A O    1 
ATOM   2372 C CB   . SER   A 1 152 ? 210.688 168.024 117.513 1.00 156.98 ? 165  SER   A CB   1 
ATOM   2373 O OG   . SER   A 1 152 ? 209.278 168.113 117.474 1.00 163.26 ? 165  SER   A OG   1 
ATOM   2374 H H    . SER   A 1 152 ? 209.769 166.617 115.621 1.00 157.16 ? 165  SER   A H    1 
ATOM   2375 H HA   . SER   A 1 152 ? 211.189 169.104 115.742 1.00 156.18 ? 165  SER   A HA   1 
ATOM   2376 H HB2  . SER   A 1 152 ? 210.959 167.091 118.007 1.00 156.28 ? 165  SER   A HB2  1 
ATOM   2377 H HB3  . SER   A 1 152 ? 211.093 168.856 118.088 1.00 156.21 ? 165  SER   A HB3  1 
ATOM   2378 H HG   . SER   A 1 152 ? 208.925 167.227 117.361 1.00 157.38 ? 165  SER   A HG   1 
ATOM   2379 N N    . LYS   A 1 153 ? 213.054 166.462 116.538 1.00 161.82 ? 166  LYS   A N    1 
ATOM   2380 C CA   . LYS   A 1 153 ? 214.423 165.930 116.674 1.00 165.65 ? 166  LYS   A CA   1 
ATOM   2381 C C    . LYS   A 1 153 ? 214.995 165.297 115.401 1.00 164.84 ? 166  LYS   A C    1 
ATOM   2382 O O    . LYS   A 1 153 ? 216.200 165.069 115.330 1.00 162.43 ? 166  LYS   A O    1 
ATOM   2383 C CB   . LYS   A 1 153 ? 214.439 164.916 117.830 1.00 162.88 ? 166  LYS   A CB   1 
ATOM   2384 C CG   . LYS   A 1 153 ? 214.467 165.594 119.209 1.00 163.10 ? 166  LYS   A CG   1 
ATOM   2385 C CD   . LYS   A 1 153 ? 215.880 166.072 119.578 1.00 163.47 ? 166  LYS   A CD   1 
ATOM   2386 C CE   . LYS   A 1 153 ? 215.906 166.541 121.036 1.00 162.55 ? 166  LYS   A CE   1 
ATOM   2387 N NZ   . LYS   A 1 153 ? 217.286 166.859 121.481 1.00 163.00 ? 166  LYS   A NZ   1 
ATOM   2388 H H    . LYS   A 1 153 ? 212.295 165.892 116.883 1.00 161.88 ? 166  LYS   A H    1 
ATOM   2389 H HA   . LYS   A 1 153 ? 215.103 166.748 116.913 1.00 162.53 ? 166  LYS   A HA   1 
ATOM   2390 H HB2  . LYS   A 1 153 ? 213.559 164.276 117.765 1.00 162.17 ? 166  LYS   A HB2  1 
ATOM   2391 H HB3  . LYS   A 1 153 ? 215.311 164.268 117.746 1.00 161.95 ? 166  LYS   A HB3  1 
ATOM   2392 H HG2  . LYS   A 1 153 ? 213.772 166.433 119.232 1.00 162.12 ? 166  LYS   A HG2  1 
ATOM   2393 H HG3  . LYS   A 1 153 ? 214.144 164.868 119.954 1.00 161.82 ? 166  LYS   A HG3  1 
ATOM   2394 H HD2  . LYS   A 1 153 ? 216.581 165.246 119.457 1.00 162.06 ? 166  LYS   A HD2  1 
ATOM   2395 H HD3  . LYS   A 1 153 ? 216.179 166.888 118.921 1.00 162.36 ? 166  LYS   A HD3  1 
ATOM   2396 H HE2  . LYS   A 1 153 ? 215.265 167.417 121.134 1.00 161.90 ? 166  LYS   A HE2  1 
ATOM   2397 H HE3  . LYS   A 1 153 ? 215.492 165.753 121.664 1.00 161.96 ? 166  LYS   A HE3  1 
ATOM   2398 H HZ1  . LYS   A 1 153 ? 217.284 167.218 122.425 1.00 162.21 ? 166  LYS   A HZ1  1 
ATOM   2399 H HZ2  . LYS   A 1 153 ? 217.716 167.554 120.887 1.00 162.20 ? 166  LYS   A HZ2  1 
ATOM   2400 H HZ3  . LYS   A 1 153 ? 217.872 166.037 121.467 1.00 162.36 ? 166  LYS   A HZ3  1 
ATOM   2401 N N    . GLY   A 1 154 ? 214.160 165.008 114.407 1.00 161.09 ? 167  GLY   A N    1 
ATOM   2402 C CA   . GLY   A 1 154 ? 214.549 164.287 113.195 1.00 156.69 ? 167  GLY   A CA   1 
ATOM   2403 C C    . GLY   A 1 154 ? 214.554 162.766 113.359 1.00 158.65 ? 167  GLY   A C    1 
ATOM   2404 O O    . GLY   A 1 154 ? 214.415 162.222 114.459 1.00 159.83 ? 167  GLY   A O    1 
ATOM   2405 H H    . GLY   A 1 154 ? 213.177 165.208 114.529 1.00 160.09 ? 167  GLY   A H    1 
ATOM   2406 H HA2  . GLY   A 1 154 ? 213.849 164.539 112.398 1.00 159.24 ? 167  GLY   A HA2  1 
ATOM   2407 H HA3  . GLY   A 1 154 ? 215.541 164.602 112.873 1.00 159.18 ? 167  GLY   A HA3  1 
ATOM   2408 N N    . SER   A 1 155 ? 214.700 162.065 112.237 1.00 162.19 ? 168  SER   A N    1 
ATOM   2409 C CA   . SER   A 1 155 ? 214.682 160.603 112.161 1.00 167.42 ? 168  SER   A CA   1 
ATOM   2410 C C    . SER   A 1 155 ? 215.626 160.085 111.075 1.00 164.57 ? 168  SER   A C    1 
ATOM   2411 O O    . SER   A 1 155 ? 215.967 160.800 110.135 1.00 159.20 ? 168  SER   A O    1 
ATOM   2412 C CB   . SER   A 1 155 ? 213.252 160.108 111.927 1.00 165.44 ? 168  SER   A CB   1 
ATOM   2413 O OG   . SER   A 1 155 ? 213.226 158.692 111.910 1.00 168.55 ? 168  SER   A OG   1 
ATOM   2414 H H    . SER   A 1 155 ? 214.847 162.571 111.375 1.00 162.68 ? 168  SER   A H    1 
ATOM   2415 H HA   . SER   A 1 155 ? 215.023 160.194 113.113 1.00 163.78 ? 168  SER   A HA   1 
ATOM   2416 H HB2  . SER   A 1 155 ? 212.613 160.474 112.730 1.00 163.01 ? 168  SER   A HB2  1 
ATOM   2417 H HB3  . SER   A 1 155 ? 212.883 160.495 110.977 1.00 162.79 ? 168  SER   A HB3  1 
ATOM   2418 H HG   . SER   A 1 155 ? 212.320 158.384 111.831 1.00 163.41 ? 168  SER   A HG   1 
ATOM   2419 N N    . SER   A 1 156 ? 216.035 158.824 111.193 1.00 163.74 ? 169  SER   A N    1 
ATOM   2420 C CA   . SER   A 1 156 ? 216.893 158.129 110.225 1.00 158.70 ? 169  SER   A CA   1 
ATOM   2421 C C    . SER   A 1 156 ? 216.146 157.639 108.977 1.00 155.18 ? 169  SER   A C    1 
ATOM   2422 O O    . SER   A 1 156 ? 216.758 157.041 108.094 1.00 154.98 ? 169  SER   A O    1 
ATOM   2423 C CB   . SER   A 1 156 ? 217.618 156.982 110.934 1.00 161.94 ? 169  SER   A CB   1 
ATOM   2424 O OG   . SER   A 1 156 ? 218.469 157.516 111.940 1.00 166.73 ? 169  SER   A OG   1 
ATOM   2425 H H    . SER   A 1 156 ? 215.664 158.290 111.965 1.00 160.90 ? 169  SER   A H    1 
ATOM   2426 H HA   . SER   A 1 156 ? 217.652 158.826 109.872 1.00 159.63 ? 169  SER   A HA   1 
ATOM   2427 H HB2  . SER   A 1 156 ? 216.893 156.300 111.379 1.00 159.86 ? 169  SER   A HB2  1 
ATOM   2428 H HB3  . SER   A 1 156 ? 218.225 156.433 110.215 1.00 159.76 ? 169  SER   A HB3  1 
ATOM   2429 H HG   . SER   A 1 156 ? 217.937 157.946 112.613 1.00 160.42 ? 169  SER   A HG   1 
ATOM   2430 N N    . ARG   A 1 157 ? 214.838 157.901 108.873 1.00 146.65 ? 170  ARG   A N    1 
ATOM   2431 C CA   . ARG   A 1 157 ? 214.006 157.629 107.690 1.00 153.95 ? 170  ARG   A CA   1 
ATOM   2432 C C    . ARG   A 1 157 ? 212.936 158.706 107.494 1.00 156.48 ? 170  ARG   A C    1 
ATOM   2433 O O    . ARG   A 1 157 ? 212.564 159.373 108.455 1.00 154.64 ? 170  ARG   A O    1 
ATOM   2434 C CB   . ARG   A 1 157 ? 213.397 156.220 107.777 1.00 152.13 ? 170  ARG   A CB   1 
ATOM   2435 C CG   . ARG   A 1 157 ? 212.519 155.987 109.019 1.00 151.33 ? 170  ARG   A CG   1 
ATOM   2436 C CD   . ARG   A 1 157 ? 211.580 154.801 108.793 1.00 153.01 ? 170  ARG   A CD   1 
ATOM   2437 N NE   . ARG   A 1 157 ? 212.291 153.517 108.704 1.00 158.08 ? 170  ARG   A NE   1 
ATOM   2438 C CZ   . ARG   A 1 157 ? 212.146 152.595 107.775 1.00 153.92 ? 170  ARG   A CZ   1 
ATOM   2439 N NH1  . ARG   A 1 157 ? 212.849 151.512 107.862 1.00 155.11 ? 170  ARG   A NH1  1 
ATOM   2440 N NH2  . ARG   A 1 157 ? 211.332 152.713 106.770 1.00 148.11 ? 170  ARG   A NH2  1 
ATOM   2441 H H    . ARG   A 1 157 ? 214.403 158.398 109.637 1.00 152.11 ? 170  ARG   A H    1 
ATOM   2442 H HA   . ARG   A 1 157 ? 214.643 157.662 106.806 1.00 153.06 ? 170  ARG   A HA   1 
ATOM   2443 H HB2  . ARG   A 1 157 ? 212.802 156.055 106.879 1.00 152.37 ? 170  ARG   A HB2  1 
ATOM   2444 H HB3  . ARG   A 1 157 ? 214.200 155.483 107.776 1.00 152.47 ? 170  ARG   A HB3  1 
ATOM   2445 H HG2  . ARG   A 1 157 ? 213.144 155.811 109.895 1.00 152.83 ? 170  ARG   A HG2  1 
ATOM   2446 H HG3  . ARG   A 1 157 ? 211.902 156.867 109.204 1.00 151.82 ? 170  ARG   A HG3  1 
ATOM   2447 H HD2  . ARG   A 1 157 ? 210.865 154.753 109.615 1.00 151.92 ? 170  ARG   A HD2  1 
ATOM   2448 H HD3  . ARG   A 1 157 ? 211.026 154.992 107.873 1.00 151.62 ? 170  ARG   A HD3  1 
ATOM   2449 H HE   . ARG   A 1 157 ? 212.951 153.296 109.435 1.00 153.40 ? 170  ARG   A HE   1 
ATOM   2450 H HH11 . ARG   A 1 157 ? 213.458 151.393 108.659 1.00 153.06 ? 170  ARG   A HH11 1 
ATOM   2451 H HH12 . ARG   A 1 157 ? 212.839 150.831 107.117 1.00 152.66 ? 170  ARG   A HH12 1 
ATOM   2452 H HH21 . ARG   A 1 157 ? 210.732 153.524 106.714 1.00 151.60 ? 170  ARG   A HH21 1 
ATOM   2453 H HH22 . ARG   A 1 157 ? 211.256 151.970 106.090 1.00 151.61 ? 170  ARG   A HH22 1 
ATOM   2454 N N    . ASN   A 1 158 ? 212.438 158.876 106.269 1.00 154.32 ? 171  ASN   A N    1 
ATOM   2455 C CA   . ASN   A 1 158 ? 211.362 159.825 105.954 1.00 150.84 ? 171  ASN   A CA   1 
ATOM   2456 C C    . ASN   A 1 158 ? 209.995 159.305 106.414 1.00 150.96 ? 171  ASN   A C    1 
ATOM   2457 O O    . ASN   A 1 158 ? 209.783 158.100 106.485 1.00 150.87 ? 171  ASN   A O    1 
ATOM   2458 C CB   . ASN   A 1 158 ? 211.339 160.074 104.441 1.00 148.96 ? 171  ASN   A CB   1 
ATOM   2459 C CG   . ASN   A 1 158 ? 212.628 160.687 103.926 1.00 151.08 ? 171  ASN   A CG   1 
ATOM   2460 O OD1  . ASN   A 1 158 ? 213.168 161.612 104.526 1.00 149.66 ? 171  ASN   A OD1  1 
ATOM   2461 N ND2  . ASN   A 1 158 ? 213.123 160.160 102.820 1.00 155.55 ? 171  ASN   A ND2  1 
ATOM   2462 H H    . ASN   A 1 158 ? 212.755 158.257 105.537 1.00 151.59 ? 171  ASN   A H    1 
ATOM   2463 H HA   . ASN   A 1 158 ? 211.550 160.769 106.465 1.00 151.45 ? 171  ASN   A HA   1 
ATOM   2464 H HB2  . ASN   A 1 158 ? 211.143 159.133 103.927 1.00 150.97 ? 171  ASN   A HB2  1 
ATOM   2465 H HB3  . ASN   A 1 158 ? 210.529 160.760 104.193 1.00 151.37 ? 171  ASN   A HB3  1 
ATOM   2466 H HD21 . ASN   A 1 158 ? 212.662 159.353 102.426 1.00 151.91 ? 171  ASN   A HD21 1 
ATOM   2467 N N    . GLU   A 1 159 ? 209.014 160.188 106.583 1.00 145.53 ? 172  GLU   A N    1 
ATOM   2468 C CA   . GLU   A 1 159 ? 207.644 159.806 106.938 1.00 144.31 ? 172  GLU   A CA   1 
ATOM   2469 C C    . GLU   A 1 159 ? 206.906 159.147 105.769 1.00 146.48 ? 172  GLU   A C    1 
ATOM   2470 O O    . GLU   A 1 159 ? 206.886 159.693 104.667 1.00 147.72 ? 172  GLU   A O    1 
ATOM   2471 C CB   . GLU   A 1 159 ? 206.896 161.053 107.435 1.00 146.29 ? 172  GLU   A CB   1 
ATOM   2472 C CG   . GLU   A 1 159 ? 205.455 160.774 107.888 1.00 151.77 ? 172  GLU   A CG   1 
ATOM   2473 C CD   . GLU   A 1 159 ? 205.029 161.723 109.021 1.00 157.68 ? 172  GLU   A CD   1 
ATOM   2474 O OE1  . GLU   A 1 159 ? 205.539 161.569 110.155 1.00 157.28 ? 172  GLU   A OE1  1 
ATOM   2475 O OE2  . GLU   A 1 159 ? 204.197 162.633 108.794 1.00 155.31 ? 172  GLU   A OE2  1 
ATOM   2476 H H    . GLU   A 1 159 ? 209.206 161.166 106.415 1.00 148.18 ? 172  GLU   A H    1 
ATOM   2477 H HA   . GLU   A 1 159 ? 207.680 159.086 107.756 1.00 148.17 ? 172  GLU   A HA   1 
ATOM   2478 H HB2  . GLU   A 1 159 ? 207.460 161.463 108.272 1.00 149.05 ? 172  GLU   A HB2  1 
ATOM   2479 H HB3  . GLU   A 1 159 ? 206.877 161.809 106.650 1.00 147.85 ? 172  GLU   A HB3  1 
ATOM   2480 H HG2  . GLU   A 1 159 ? 204.785 160.858 107.032 1.00 148.33 ? 172  GLU   A HG2  1 
ATOM   2481 H HG3  . GLU   A 1 159 ? 205.395 159.749 108.255 1.00 148.89 ? 172  GLU   A HG3  1 
ATOM   2482 N N    . SER   A 1 160 ? 206.245 158.012 106.003 1.00 144.54 ? 173  SER   A N    1 
ATOM   2483 C CA   . SER   A 1 160 ? 205.315 157.420 105.037 1.00 143.46 ? 173  SER   A CA   1 
ATOM   2484 C C    . SER   A 1 160 ? 204.297 156.528 105.734 1.00 138.80 ? 173  SER   A C    1 
ATOM   2485 O O    . SER   A 1 160 ? 204.638 155.479 106.279 1.00 140.54 ? 173  SER   A O    1 
ATOM   2486 C CB   . SER   A 1 160 ? 206.047 156.614 103.954 1.00 145.89 ? 173  SER   A CB   1 
ATOM   2487 O OG   . SER   A 1 160 ? 206.752 155.513 104.496 1.00 146.12 ? 173  SER   A OG   1 
ATOM   2488 H H    . SER   A 1 160 ? 206.319 157.572 106.909 1.00 142.43 ? 173  SER   A H    1 
ATOM   2489 H HA   . SER   A 1 160 ? 204.776 158.222 104.534 1.00 142.11 ? 173  SER   A HA   1 
ATOM   2490 H HB2  . SER   A 1 160 ? 205.314 156.243 103.238 1.00 142.89 ? 173  SER   A HB2  1 
ATOM   2491 H HB3  . SER   A 1 160 ? 206.744 157.262 103.424 1.00 142.74 ? 173  SER   A HB3  1 
ATOM   2492 H HG   . SER   A 1 160 ? 206.189 155.122 105.168 1.00 142.77 ? 173  SER   A HG   1 
ATOM   2493 N N    . TRP   A 1 161 ? 203.029 156.909 105.673 1.00 123.29 ? 174  TRP   A N    1 
ATOM   2494 C CA   . TRP   A 1 161 ? 201.914 156.056 106.079 1.00 129.35 ? 174  TRP   A CA   1 
ATOM   2495 C C    . TRP   A 1 161 ? 200.854 155.918 104.988 1.00 131.10 ? 174  TRP   A C    1 
ATOM   2496 O O    . TRP   A 1 161 ? 200.120 154.932 104.981 1.00 135.43 ? 174  TRP   A O    1 
ATOM   2497 C CB   . TRP   A 1 161 ? 201.358 156.554 107.411 1.00 133.98 ? 174  TRP   A CB   1 
ATOM   2498 C CG   . TRP   A 1 161 ? 200.949 157.986 107.446 1.00 129.88 ? 174  TRP   A CG   1 
ATOM   2499 C CD1  . TRP   A 1 161 ? 201.742 159.016 107.805 1.00 129.32 ? 174  TRP   A CD1  1 
ATOM   2500 C CD2  . TRP   A 1 161 ? 199.678 158.576 107.058 1.00 125.64 ? 174  TRP   A CD2  1 
ATOM   2501 N NE1  . TRP   A 1 161 ? 201.041 160.197 107.695 1.00 126.41 ? 174  TRP   A NE1  1 
ATOM   2502 C CE2  . TRP   A 1 161 ? 199.760 159.983 107.249 1.00 126.83 ? 174  TRP   A CE2  1 
ATOM   2503 C CE3  . TRP   A 1 161 ? 198.466 158.064 106.559 1.00 128.16 ? 174  TRP   A CE3  1 
ATOM   2504 C CZ2  . TRP   A 1 161 ? 198.689 160.840 106.986 1.00 129.89 ? 174  TRP   A CZ2  1 
ATOM   2505 C CZ3  . TRP   A 1 161 ? 197.393 158.920 106.259 1.00 135.17 ? 174  TRP   A CZ3  1 
ATOM   2506 C CH2  . TRP   A 1 161 ? 197.495 160.302 106.484 1.00 133.58 ? 174  TRP   A CH2  1 
ATOM   2507 H H    . TRP   A 1 161 ? 202.820 157.830 105.316 1.00 130.22 ? 174  TRP   A H    1 
ATOM   2508 H HA   . TRP   A 1 161 ? 202.280 155.042 106.237 1.00 131.08 ? 174  TRP   A HA   1 
ATOM   2509 H HB2  . TRP   A 1 161 ? 200.494 155.945 107.679 1.00 131.62 ? 174  TRP   A HB2  1 
ATOM   2510 H HB3  . TRP   A 1 161 ? 202.118 156.400 108.177 1.00 131.55 ? 174  TRP   A HB3  1 
ATOM   2511 H HD1  . TRP   A 1 161 ? 202.766 158.919 108.134 1.00 130.96 ? 174  TRP   A HD1  1 
ATOM   2512 H HE1  . TRP   A 1 161 ? 201.426 161.102 107.925 1.00 130.41 ? 174  TRP   A HE1  1 
ATOM   2513 H HE3  . TRP   A 1 161 ? 198.370 157.002 106.389 1.00 130.24 ? 174  TRP   A HE3  1 
ATOM   2514 H HZ2  . TRP   A 1 161 ? 198.786 161.902 107.156 1.00 130.53 ? 174  TRP   A HZ2  1 
ATOM   2515 H HZ3  . TRP   A 1 161 ? 196.478 158.511 105.855 1.00 131.37 ? 174  TRP   A HZ3  1 
ATOM   2516 H HH2  . TRP   A 1 161 ? 196.659 160.949 106.264 1.00 130.94 ? 174  TRP   A HH2  1 
ATOM   2517 N N    . HIS   A 1 162 ? 200.858 156.803 103.994 1.00 131.98 ? 175  HIS   A N    1 
ATOM   2518 C CA   . HIS   A 1 162 ? 200.091 156.677 102.761 1.00 134.10 ? 175  HIS   A CA   1 
ATOM   2519 C C    . HIS   A 1 162 ? 200.934 157.082 101.555 1.00 135.54 ? 175  HIS   A C    1 
ATOM   2520 O O    . HIS   A 1 162 ? 201.937 157.782 101.690 1.00 133.94 ? 175  HIS   A O    1 
ATOM   2521 C CB   . HIS   A 1 162 ? 198.821 157.527 102.848 1.00 133.06 ? 175  HIS   A CB   1 
ATOM   2522 C CG   . HIS   A 1 162 ? 199.076 159.010 102.754 1.00 134.52 ? 175  HIS   A CG   1 
ATOM   2523 N ND1  . HIS   A 1 162 ? 199.917 159.749 103.586 1.00 138.04 ? 175  HIS   A ND1  1 
ATOM   2524 C CD2  . HIS   A 1 162 ? 198.534 159.849 101.829 1.00 134.68 ? 175  HIS   A CD2  1 
ATOM   2525 C CE1  . HIS   A 1 162 ? 199.845 161.017 103.156 1.00 137.73 ? 175  HIS   A CE1  1 
ATOM   2526 N NE2  . HIS   A 1 162 ? 199.023 161.104 102.101 1.00 134.85 ? 175  HIS   A NE2  1 
ATOM   2527 H H    . HIS   A 1 162 ? 201.463 157.610 104.059 1.00 134.86 ? 175  HIS   A H    1 
ATOM   2528 H HA   . HIS   A 1 162 ? 199.805 155.633 102.631 1.00 136.23 ? 175  HIS   A HA   1 
ATOM   2529 H HB2  . HIS   A 1 162 ? 198.159 157.242 102.030 1.00 135.75 ? 175  HIS   A HB2  1 
ATOM   2530 H HB3  . HIS   A 1 162 ? 198.298 157.310 103.780 1.00 135.07 ? 175  HIS   A HB3  1 
ATOM   2531 H HD2  . HIS   A 1 162 ? 197.846 159.573 101.043 1.00 135.72 ? 175  HIS   A HD2  1 
ATOM   2532 H HE1  . HIS   A 1 162 ? 200.375 161.850 103.594 1.00 135.81 ? 175  HIS   A HE1  1 
ATOM   2533 H HE2  . HIS   A 1 162 ? 198.808 161.956 101.601 1.00 135.62 ? 175  HIS   A HE2  1 
ATOM   2534 N N    . PHE   A 1 163 ? 200.516 156.662 100.366 1.00 146.05 ? 176  PHE   A N    1 
ATOM   2535 C CA   . PHE   A 1 163 ? 201.127 157.059 99.102  1.00 143.45 ? 176  PHE   A CA   1 
ATOM   2536 C C    . PHE   A 1 163 ? 200.056 157.480 98.095  1.00 142.41 ? 176  PHE   A C    1 
ATOM   2537 O O    . PHE   A 1 163 ? 199.708 156.742 97.179  1.00 146.29 ? 176  PHE   A O    1 
ATOM   2538 C CB   . PHE   A 1 163 ? 202.045 155.948 98.580  1.00 138.92 ? 176  PHE   A CB   1 
ATOM   2539 C CG   . PHE   A 1 163 ? 202.795 156.363 97.332  1.00 141.41 ? 176  PHE   A CG   1 
ATOM   2540 C CD1  . PHE   A 1 163 ? 203.886 157.242 97.435  1.00 145.71 ? 176  PHE   A CD1  1 
ATOM   2541 C CD2  . PHE   A 1 163 ? 202.382 155.916 96.067  1.00 143.90 ? 176  PHE   A CD2  1 
ATOM   2542 C CE1  . PHE   A 1 163 ? 204.559 157.671 96.280  1.00 147.08 ? 176  PHE   A CE1  1 
ATOM   2543 C CE2  . PHE   A 1 163 ? 203.053 156.345 94.910  1.00 142.41 ? 176  PHE   A CE2  1 
ATOM   2544 C CZ   . PHE   A 1 163 ? 204.143 157.223 95.016  1.00 142.14 ? 176  PHE   A CZ   1 
ATOM   2545 H H    . PHE   A 1 163 ? 199.720 156.041 100.337 1.00 143.42 ? 176  PHE   A H    1 
ATOM   2546 H HA   . PHE   A 1 163 ? 201.752 157.936 99.268  1.00 142.86 ? 176  PHE   A HA   1 
ATOM   2547 H HB2  . PHE   A 1 163 ? 202.774 155.702 99.352  1.00 142.75 ? 176  PHE   A HB2  1 
ATOM   2548 H HB3  . PHE   A 1 163 ? 201.459 155.052 98.378  1.00 142.63 ? 176  PHE   A HB3  1 
ATOM   2549 H HD1  . PHE   A 1 163 ? 204.204 157.595 98.405  1.00 143.26 ? 176  PHE   A HD1  1 
ATOM   2550 H HD2  . PHE   A 1 163 ? 201.537 155.249 95.980  1.00 143.57 ? 176  PHE   A HD2  1 
ATOM   2551 H HE1  . PHE   A 1 163 ? 205.397 158.348 96.363  1.00 143.68 ? 176  PHE   A HE1  1 
ATOM   2552 H HE2  . PHE   A 1 163 ? 202.729 155.999 93.940  1.00 143.08 ? 176  PHE   A HE2  1 
ATOM   2553 H HZ   . PHE   A 1 163 ? 204.660 157.553 94.127  1.00 142.72 ? 176  PHE   A HZ   1 
ATOM   2554 N N    . ASP   A 1 164 ? 199.515 158.682 98.271  1.00 144.74 ? 177  ASP   A N    1 
ATOM   2555 C CA   . ASP   A 1 164 ? 198.643 159.321 97.287  1.00 148.50 ? 177  ASP   A CA   1 
ATOM   2556 C C    . ASP   A 1 164 ? 199.373 160.522 96.676  1.00 151.01 ? 177  ASP   A C    1 
ATOM   2557 O O    . ASP   A 1 164 ? 199.701 161.487 97.366  1.00 150.60 ? 177  ASP   A O    1 
ATOM   2558 C CB   . ASP   A 1 164 ? 197.303 159.696 97.932  1.00 149.10 ? 177  ASP   A CB   1 
ATOM   2559 C CG   . ASP   A 1 164 ? 196.529 158.450 98.365  1.00 154.14 ? 177  ASP   A CG   1 
ATOM   2560 O OD1  . ASP   A 1 164 ? 196.117 157.666 97.481  1.00 155.91 ? 177  ASP   A OD1  1 
ATOM   2561 O OD2  . ASP   A 1 164 ? 196.347 158.246 99.583  1.00 156.43 ? 177  ASP   A OD2  1 
ATOM   2562 H H    . ASP   A 1 164 ? 199.829 159.243 99.050  1.00 148.65 ? 177  ASP   A H    1 
ATOM   2563 H HA   . ASP   A 1 164 ? 198.422 158.628 96.476  1.00 149.97 ? 177  ASP   A HA   1 
ATOM   2564 H HB2  . ASP   A 1 164 ? 197.477 160.353 98.784  1.00 149.38 ? 177  ASP   A HB2  1 
ATOM   2565 H HB3  . ASP   A 1 164 ? 196.704 160.241 97.203  1.00 149.65 ? 177  ASP   A HB3  1 
ATOM   2566 N N    . LYS   A 1 165 ? 199.651 160.454 95.370  1.00 161.27 ? 178  LYS   A N    1 
ATOM   2567 C CA   . LYS   A 1 165 ? 200.396 161.490 94.631  1.00 160.39 ? 178  LYS   A CA   1 
ATOM   2568 C C    . LYS   A 1 165 ? 199.543 162.724 94.327  1.00 160.13 ? 178  LYS   A C    1 
ATOM   2569 O O    . LYS   A 1 165 ? 200.065 163.831 94.201  1.00 156.89 ? 178  LYS   A O    1 
ATOM   2570 C CB   . LYS   A 1 165 ? 200.955 160.848 93.354  1.00 159.40 ? 178  LYS   A CB   1 
ATOM   2571 C CG   . LYS   A 1 165 ? 201.965 161.753 92.638  1.00 158.88 ? 178  LYS   A CG   1 
ATOM   2572 C CD   . LYS   A 1 165 ? 202.628 161.000 91.480  1.00 159.72 ? 178  LYS   A CD   1 
ATOM   2573 C CE   . LYS   A 1 165 ? 203.658 161.902 90.796  1.00 159.71 ? 178  LYS   A CE   1 
ATOM   2574 N NZ   . LYS   A 1 165 ? 204.350 161.192 89.693  1.00 160.40 ? 178  LYS   A NZ   1 
ATOM   2575 H H    . LYS   A 1 165 ? 199.385 159.615 94.875  1.00 158.02 ? 178  LYS   A H    1 
ATOM   2576 H HA   . LYS   A 1 165 ? 201.231 161.827 95.245  1.00 158.30 ? 178  LYS   A HA   1 
ATOM   2577 H HB2  . LYS   A 1 165 ? 201.460 159.922 93.626  1.00 158.18 ? 178  LYS   A HB2  1 
ATOM   2578 H HB3  . LYS   A 1 165 ? 200.138 160.607 92.674  1.00 158.05 ? 178  LYS   A HB3  1 
ATOM   2579 H HG2  . LYS   A 1 165 ? 201.458 162.635 92.246  1.00 157.89 ? 178  LYS   A HG2  1 
ATOM   2580 H HG3  . LYS   A 1 165 ? 202.732 162.066 93.347  1.00 158.28 ? 178  LYS   A HG3  1 
ATOM   2581 H HD2  . LYS   A 1 165 ? 203.125 160.111 91.868  1.00 158.12 ? 178  LYS   A HD2  1 
ATOM   2582 H HD3  . LYS   A 1 165 ? 201.866 160.700 90.761  1.00 158.41 ? 178  LYS   A HD3  1 
ATOM   2583 H HE2  . LYS   A 1 165 ? 203.149 162.785 90.411  1.00 158.38 ? 178  LYS   A HE2  1 
ATOM   2584 H HE3  . LYS   A 1 165 ? 204.384 162.230 91.540  1.00 158.33 ? 178  LYS   A HE3  1 
ATOM   2585 H HZ1  . LYS   A 1 165 ? 205.026 161.793 89.245  1.00 158.50 ? 178  LYS   A HZ1  1 
ATOM   2586 H HZ2  . LYS   A 1 165 ? 204.839 160.378 90.036  1.00 158.49 ? 178  LYS   A HZ2  1 
ATOM   2587 H HZ3  . LYS   A 1 165 ? 203.692 160.888 88.989  1.00 158.51 ? 178  LYS   A HZ3  1 
ATOM   2588 N N    . SER   A 1 166 ? 198.233 162.528 94.244  1.00 169.80 ? 179  SER   A N    1 
ATOM   2589 C CA   . SER   A 1 166 ? 197.189 163.547 94.122  1.00 169.17 ? 179  SER   A CA   1 
ATOM   2590 C C    . SER   A 1 166 ? 196.194 163.388 95.271  1.00 166.91 ? 179  SER   A C    1 
ATOM   2591 O O    . SER   A 1 166 ? 196.030 162.298 95.814  1.00 166.58 ? 179  SER   A O    1 
ATOM   2592 C CB   . SER   A 1 166 ? 196.493 163.430 92.764  1.00 167.10 ? 179  SER   A CB   1 
ATOM   2593 O OG   . SER   A 1 166 ? 195.923 162.143 92.590  1.00 166.53 ? 179  SER   A OG   1 
ATOM   2594 H H    . SER   A 1 166 ? 197.908 161.580 94.364  1.00 166.06 ? 179  SER   A H    1 
ATOM   2595 H HA   . SER   A 1 166 ? 197.632 164.541 94.193  1.00 166.39 ? 179  SER   A HA   1 
ATOM   2596 H HB2  . SER   A 1 166 ? 195.711 164.187 92.696  1.00 166.12 ? 179  SER   A HB2  1 
ATOM   2597 H HB3  . SER   A 1 166 ? 197.221 163.612 91.974  1.00 166.04 ? 179  SER   A HB3  1 
ATOM   2598 H HG   . SER   A 1 166 ? 195.468 162.129 91.745  1.00 166.07 ? 179  SER   A HG   1 
ATOM   2599 N N    . GLU   A 1 167 ? 195.553 164.471 95.702  1.00 161.61 ? 180  GLU   A N    1 
ATOM   2600 C CA   . GLU   A 1 167 ? 194.759 164.453 96.933  1.00 163.71 ? 180  GLU   A CA   1 
ATOM   2601 C C    . GLU   A 1 167 ? 193.556 163.488 96.839  1.00 160.19 ? 180  GLU   A C    1 
ATOM   2602 O O    . GLU   A 1 167 ? 192.738 163.630 95.924  1.00 156.56 ? 180  GLU   A O    1 
ATOM   2603 C CB   . GLU   A 1 167 ? 194.309 165.887 97.250  1.00 163.24 ? 180  GLU   A CB   1 
ATOM   2604 C CG   . GLU   A 1 167 ? 193.674 166.040 98.639  1.00 164.03 ? 180  GLU   A CG   1 
ATOM   2605 C CD   . GLU   A 1 167 ? 194.654 165.847 99.811  1.00 165.05 ? 180  GLU   A CD   1 
ATOM   2606 O OE1  . GLU   A 1 167 ? 195.869 165.637 99.593  1.00 165.05 ? 180  GLU   A OE1  1 
ATOM   2607 O OE2  . GLU   A 1 167 ? 194.199 165.937 100.974 1.00 162.16 ? 180  GLU   A OE2  1 
ATOM   2608 H H    . GLU   A 1 167 ? 195.700 165.354 95.235  1.00 161.23 ? 180  GLU   A H    1 
ATOM   2609 H HA   . GLU   A 1 167 ? 195.425 164.125 97.730  1.00 161.77 ? 180  GLU   A HA   1 
ATOM   2610 H HB2  . GLU   A 1 167 ? 195.162 166.562 97.178  1.00 161.37 ? 180  GLU   A HB2  1 
ATOM   2611 H HB3  . GLU   A 1 167 ? 193.582 166.201 96.502  1.00 160.78 ? 180  GLU   A HB3  1 
ATOM   2612 H HG2  . GLU   A 1 167 ? 193.254 167.044 98.699  1.00 160.92 ? 180  GLU   A HG2  1 
ATOM   2613 H HG3  . GLU   A 1 167 ? 192.847 165.336 98.731  1.00 161.48 ? 180  GLU   A HG3  1 
ATOM   2614 N N    . PRO   A 1 168 ? 193.411 162.511 97.752  1.00 145.25 ? 181  PRO   A N    1 
ATOM   2615 C CA   . PRO   A 1 168 ? 192.323 161.540 97.711  1.00 141.29 ? 181  PRO   A CA   1 
ATOM   2616 C C    . PRO   A 1 168 ? 190.981 162.159 98.115  1.00 143.88 ? 181  PRO   A C    1 
ATOM   2617 O O    . PRO   A 1 168 ? 190.929 163.227 98.723  1.00 147.56 ? 181  PRO   A O    1 
ATOM   2618 C CB   . PRO   A 1 168 ? 192.748 160.422 98.665  1.00 143.21 ? 181  PRO   A CB   1 
ATOM   2619 C CG   . PRO   A 1 168 ? 193.615 161.145 99.689  1.00 145.04 ? 181  PRO   A CG   1 
ATOM   2620 C CD   . PRO   A 1 168 ? 194.304 162.223 98.860  1.00 146.63 ? 181  PRO   A CD   1 
ATOM   2621 H HA   . PRO   A 1 168 ? 192.227 161.129 96.706  1.00 144.89 ? 181  PRO   A HA   1 
ATOM   2622 H HB2  . PRO   A 1 168 ? 191.899 159.925 99.135  1.00 145.05 ? 181  PRO   A HB2  1 
ATOM   2623 H HB3  . PRO   A 1 168 ? 193.357 159.698 98.124  1.00 144.90 ? 181  PRO   A HB3  1 
ATOM   2624 H HG2  . PRO   A 1 168 ? 192.980 161.615 100.440 1.00 144.98 ? 181  PRO   A HG2  1 
ATOM   2625 H HG3  . PRO   A 1 168 ? 194.335 160.475 100.158 1.00 145.12 ? 181  PRO   A HG3  1 
ATOM   2626 H HD2  . PRO   A 1 168 ? 194.475 163.106 99.476  1.00 146.00 ? 181  PRO   A HD2  1 
ATOM   2627 H HD3  . PRO   A 1 168 ? 195.249 161.841 98.474  1.00 145.99 ? 181  PRO   A HD3  1 
ATOM   2628 N N    . LEU   A 1 169 ? 189.876 161.473 97.816  1.00 144.87 ? 182  LEU   A N    1 
ATOM   2629 C CA   . LEU   A 1 169 ? 188.545 161.878 98.276  1.00 147.00 ? 182  LEU   A CA   1 
ATOM   2630 C C    . LEU   A 1 169 ? 188.484 161.839 99.805  1.00 151.01 ? 182  LEU   A C    1 
ATOM   2631 O O    . LEU   A 1 169 ? 188.895 160.849 100.413 1.00 152.22 ? 182  LEU   A O    1 
ATOM   2632 C CB   . LEU   A 1 169 ? 187.458 160.957 97.695  1.00 144.77 ? 182  LEU   A CB   1 
ATOM   2633 C CG   . LEU   A 1 169 ? 187.016 161.302 96.265  1.00 148.94 ? 182  LEU   A CG   1 
ATOM   2634 C CD1  . LEU   A 1 169 ? 188.114 161.094 95.223  1.00 147.36 ? 182  LEU   A CD1  1 
ATOM   2635 C CD2  . LEU   A 1 169 ? 185.832 160.416 95.882  1.00 148.07 ? 182  LEU   A CD2  1 
ATOM   2636 H H    . LEU   A 1 169 ? 189.967 160.610 97.301  1.00 146.65 ? 182  LEU   A H    1 
ATOM   2637 H HA   . LEU   A 1 169 ? 188.348 162.901 97.954  1.00 147.25 ? 182  LEU   A HA   1 
ATOM   2638 H HB2  . LEU   A 1 169 ? 187.789 159.919 97.741  1.00 146.45 ? 182  LEU   A HB2  1 
ATOM   2639 H HB3  . LEU   A 1 169 ? 186.576 161.044 98.330  1.00 146.71 ? 182  LEU   A HB3  1 
ATOM   2640 H HG   . LEU   A 1 169 ? 186.692 162.342 96.233  1.00 147.25 ? 182  LEU   A HG   1 
ATOM   2641 H HD11 . LEU   A 1 169 ? 188.915 161.816 95.379  1.00 146.91 ? 182  LEU   A HD11 1 
ATOM   2642 H HD12 . LEU   A 1 169 ? 187.706 161.257 94.225  1.00 147.14 ? 182  LEU   A HD12 1 
ATOM   2643 H HD13 . LEU   A 1 169 ? 188.508 160.080 95.287  1.00 147.18 ? 182  LEU   A HD13 1 
ATOM   2644 H HD21 . LEU   A 1 169 ? 185.016 160.567 96.588  1.00 146.93 ? 182  LEU   A HD21 1 
ATOM   2645 H HD22 . LEU   A 1 169 ? 186.129 159.367 95.895  1.00 147.04 ? 182  LEU   A HD22 1 
ATOM   2646 H HD23 . LEU   A 1 169 ? 185.483 160.679 94.884  1.00 147.31 ? 182  LEU   A HD23 1 
ATOM   2647 N N    . CYS   A 1 170 ? 187.921 162.877 100.420 1.00 152.67 ? 183  CYS   A N    1 
ATOM   2648 C CA   . CYS   A 1 170 ? 187.776 162.984 101.869 1.00 151.46 ? 183  CYS   A CA   1 
ATOM   2649 C C    . CYS   A 1 170 ? 186.341 163.314 102.271 1.00 145.12 ? 183  CYS   A C    1 
ATOM   2650 O O    . CYS   A 1 170 ? 185.743 164.249 101.742 1.00 144.02 ? 183  CYS   A O    1 
ATOM   2651 C CB   . CYS   A 1 170 ? 188.727 164.052 102.410 1.00 153.77 ? 183  CYS   A CB   1 
ATOM   2652 S SG   . CYS   A 1 170 ? 190.486 163.710 102.181 1.00 173.72 ? 183  CYS   A SG   1 
ATOM   2653 H H    . CYS   A 1 170 ? 187.591 163.649 99.859  1.00 151.66 ? 183  CYS   A H    1 
ATOM   2654 H HA   . CYS   A 1 170 ? 188.041 162.036 102.337 1.00 152.03 ? 183  CYS   A HA   1 
ATOM   2655 H HB2  . CYS   A 1 170 ? 188.498 164.996 101.915 1.00 151.45 ? 183  CYS   A HB2  1 
ATOM   2656 H HB3  . CYS   A 1 170 ? 188.546 164.185 103.476 1.00 152.11 ? 183  CYS   A HB3  1 
ATOM   2657 N N    . LEU   A 1 171 ? 185.811 162.597 103.260 1.00 133.01 ? 184  LEU   A N    1 
ATOM   2658 C CA   . LEU   A 1 171 ? 184.553 162.955 103.912 1.00 139.65 ? 184  LEU   A CA   1 
ATOM   2659 C C    . LEU   A 1 171 ? 184.758 164.069 104.939 1.00 139.46 ? 184  LEU   A C    1 
ATOM   2660 O O    . LEU   A 1 171 ? 183.843 164.847 105.197 1.00 140.81 ? 184  LEU   A O    1 
ATOM   2661 C CB   . LEU   A 1 171 ? 183.962 161.729 104.619 1.00 139.19 ? 184  LEU   A CB   1 
ATOM   2662 C CG   . LEU   A 1 171 ? 183.634 160.550 103.699 1.00 136.52 ? 184  LEU   A CG   1 
ATOM   2663 C CD1  . LEU   A 1 171 ? 183.212 159.353 104.542 1.00 135.11 ? 184  LEU   A CD1  1 
ATOM   2664 C CD2  . LEU   A 1 171 ? 182.513 160.879 102.716 1.00 138.47 ? 184  LEU   A CD2  1 
ATOM   2665 H H    . LEU   A 1 171 ? 186.370 161.863 103.670 1.00 137.04 ? 184  LEU   A H    1 
ATOM   2666 H HA   . LEU   A 1 171 ? 183.841 163.319 103.172 1.00 137.82 ? 184  LEU   A HA   1 
ATOM   2667 H HB2  . LEU   A 1 171 ? 184.666 161.393 105.380 1.00 136.85 ? 184  LEU   A HB2  1 
ATOM   2668 H HB3  . LEU   A 1 171 ? 183.041 162.034 105.115 1.00 137.11 ? 184  LEU   A HB3  1 
ATOM   2669 H HG   . LEU   A 1 171 ? 184.528 160.279 103.138 1.00 136.01 ? 184  LEU   A HG   1 
ATOM   2670 H HD11 . LEU   A 1 171 ? 184.036 159.053 105.188 1.00 136.10 ? 184  LEU   A HD11 1 
ATOM   2671 H HD12 . LEU   A 1 171 ? 182.956 158.516 103.892 1.00 136.41 ? 184  LEU   A HD12 1 
ATOM   2672 H HD13 . LEU   A 1 171 ? 182.345 159.611 105.151 1.00 137.22 ? 184  LEU   A HD13 1 
ATOM   2673 H HD21 . LEU   A 1 171 ? 182.829 161.677 102.045 1.00 137.28 ? 184  LEU   A HD21 1 
ATOM   2674 H HD22 . LEU   A 1 171 ? 181.619 161.187 103.257 1.00 136.94 ? 184  LEU   A HD22 1 
ATOM   2675 H HD23 . LEU   A 1 171 ? 182.286 159.997 102.116 1.00 136.92 ? 184  LEU   A HD23 1 
ATOM   2676 N N    . PHE   A 1 172 ? 185.946 164.141 105.540 1.00 139.68 ? 185  PHE   A N    1 
ATOM   2677 C CA   . PHE   A 1 172 ? 186.243 165.054 106.636 1.00 139.06 ? 185  PHE   A CA   1 
ATOM   2678 C C    . PHE   A 1 172 ? 187.706 165.485 106.624 1.00 139.83 ? 185  PHE   A C    1 
ATOM   2679 O O    . PHE   A 1 172 ? 188.593 164.678 106.344 1.00 146.10 ? 185  PHE   A O    1 
ATOM   2680 C CB   . PHE   A 1 172 ? 185.903 164.337 107.943 1.00 138.08 ? 185  PHE   A CB   1 
ATOM   2681 C CG   . PHE   A 1 172 ? 185.950 165.205 109.174 1.00 132.19 ? 185  PHE   A CG   1 
ATOM   2682 C CD1  . PHE   A 1 172 ? 184.816 165.937 109.556 1.00 132.37 ? 185  PHE   A CD1  1 
ATOM   2683 C CD2  . PHE   A 1 172 ? 187.117 165.264 109.949 1.00 134.83 ? 185  PHE   A CD2  1 
ATOM   2684 C CE1  . PHE   A 1 172 ? 184.841 166.712 110.725 1.00 134.92 ? 185  PHE   A CE1  1 
ATOM   2685 C CE2  . PHE   A 1 172 ? 187.142 166.039 111.116 1.00 136.57 ? 185  PHE   A CE2  1 
ATOM   2686 C CZ   . PHE   A 1 172 ? 186.003 166.756 111.508 1.00 134.99 ? 185  PHE   A CZ   1 
ATOM   2687 H H    . PHE   A 1 172 ? 186.660 163.477 105.277 1.00 137.34 ? 185  PHE   A H    1 
ATOM   2688 H HA   . PHE   A 1 172 ? 185.620 165.944 106.552 1.00 136.28 ? 185  PHE   A HA   1 
ATOM   2689 H HB2  . PHE   A 1 172 ? 184.897 163.922 107.863 1.00 136.99 ? 185  PHE   A HB2  1 
ATOM   2690 H HB3  . PHE   A 1 172 ? 186.589 163.501 108.081 1.00 137.05 ? 185  PHE   A HB3  1 
ATOM   2691 H HD1  . PHE   A 1 172 ? 183.916 165.892 108.960 1.00 136.18 ? 185  PHE   A HD1  1 
ATOM   2692 H HD2  . PHE   A 1 172 ? 187.993 164.700 109.662 1.00 136.28 ? 185  PHE   A HD2  1 
ATOM   2693 H HE1  . PHE   A 1 172 ? 183.963 167.264 111.028 1.00 136.63 ? 185  PHE   A HE1  1 
ATOM   2694 H HE2  . PHE   A 1 172 ? 188.035 166.070 111.724 1.00 136.60 ? 185  PHE   A HE2  1 
ATOM   2695 H HZ   . PHE   A 1 172 ? 186.018 167.334 112.420 1.00 136.48 ? 185  PHE   A HZ   1 
ATOM   2696 N N    . LYS   A 1 173 ? 187.963 166.737 106.993 1.00 138.67 ? 186  LYS   A N    1 
ATOM   2697 C CA   . LYS   A 1 173 ? 189.297 167.312 107.186 1.00 141.14 ? 186  LYS   A CA   1 
ATOM   2698 C C    . LYS   A 1 173 ? 189.165 168.549 108.065 1.00 142.51 ? 186  LYS   A C    1 
ATOM   2699 O O    . LYS   A 1 173 ? 188.594 169.547 107.628 1.00 141.94 ? 186  LYS   A O    1 
ATOM   2700 C CB   . LYS   A 1 173 ? 189.910 167.643 105.814 1.00 136.40 ? 186  LYS   A CB   1 
ATOM   2701 C CG   . LYS   A 1 173 ? 191.241 168.403 105.927 1.00 141.09 ? 186  LYS   A CG   1 
ATOM   2702 C CD   . LYS   A 1 173 ? 191.873 168.709 104.568 1.00 146.11 ? 186  LYS   A CD   1 
ATOM   2703 C CE   . LYS   A 1 173 ? 192.354 167.442 103.855 1.00 145.45 ? 186  LYS   A CE   1 
ATOM   2704 N NZ   . LYS   A 1 173 ? 193.104 167.795 102.628 1.00 148.07 ? 186  LYS   A NZ   1 
ATOM   2705 H H    . LYS   A 1 173 ? 187.169 167.329 107.190 1.00 140.39 ? 186  LYS   A H    1 
ATOM   2706 H HA   . LYS   A 1 173 ? 189.940 166.592 107.693 1.00 141.52 ? 186  LYS   A HA   1 
ATOM   2707 H HB2  . LYS   A 1 173 ? 190.073 166.711 105.272 1.00 140.47 ? 186  LYS   A HB2  1 
ATOM   2708 H HB3  . LYS   A 1 173 ? 189.209 168.251 105.242 1.00 140.49 ? 186  LYS   A HB3  1 
ATOM   2709 H HG2  . LYS   A 1 173 ? 191.068 169.356 106.427 1.00 141.44 ? 186  LYS   A HG2  1 
ATOM   2710 H HG3  . LYS   A 1 173 ? 191.946 167.831 106.530 1.00 140.78 ? 186  LYS   A HG3  1 
ATOM   2711 H HD2  . LYS   A 1 173 ? 191.152 169.235 103.944 1.00 141.82 ? 186  LYS   A HD2  1 
ATOM   2712 H HD3  . LYS   A 1 173 ? 192.726 169.366 104.738 1.00 142.06 ? 186  LYS   A HD3  1 
ATOM   2713 H HE2  . LYS   A 1 173 ? 192.996 166.879 104.533 1.00 141.61 ? 186  LYS   A HE2  1 
ATOM   2714 H HE3  . LYS   A 1 173 ? 191.494 166.821 103.606 1.00 141.53 ? 186  LYS   A HE3  1 
ATOM   2715 H HZ1  . LYS   A 1 173 ? 193.442 166.974 102.148 1.00 142.37 ? 186  LYS   A HZ1  1 
ATOM   2716 H HZ2  . LYS   A 1 173 ? 192.526 168.309 101.979 1.00 142.55 ? 186  LYS   A HZ2  1 
ATOM   2717 H HZ3  . LYS   A 1 173 ? 193.913 168.360 102.845 1.00 142.60 ? 186  LYS   A HZ3  1 
ATOM   2718 N N    . LYS   A 1 174 ? 189.688 168.496 109.287 1.00 141.09 ? 187  LYS   A N    1 
ATOM   2719 C CA   . LYS   A 1 174 ? 189.720 169.623 110.230 1.00 139.27 ? 187  LYS   A CA   1 
ATOM   2720 C C    . LYS   A 1 174 ? 190.977 169.584 111.079 1.00 141.70 ? 187  LYS   A C    1 
ATOM   2721 O O    . LYS   A 1 174 ? 191.574 168.531 111.277 1.00 147.81 ? 187  LYS   A O    1 
ATOM   2722 C CB   . LYS   A 1 174 ? 188.476 169.638 111.134 1.00 139.24 ? 187  LYS   A CB   1 
ATOM   2723 C CG   . LYS   A 1 174 ? 187.216 170.110 110.395 1.00 138.43 ? 187  LYS   A CG   1 
ATOM   2724 C CD   . LYS   A 1 174 ? 186.079 170.528 111.337 1.00 142.86 ? 187  LYS   A CD   1 
ATOM   2725 C CE   . LYS   A 1 174 ? 186.426 171.805 112.118 1.00 144.39 ? 187  LYS   A CE   1 
ATOM   2726 N NZ   . LYS   A 1 174 ? 185.266 172.309 112.893 1.00 145.87 ? 187  LYS   A NZ   1 
ATOM   2727 H H    . LYS   A 1 174 ? 190.150 167.642 109.566 1.00 141.45 ? 187  LYS   A H    1 
ATOM   2728 H HA   . LYS   A 1 174 ? 189.754 170.556 109.669 1.00 141.37 ? 187  LYS   A HA   1 
ATOM   2729 H HB2  . LYS   A 1 174 ? 188.308 168.647 111.556 1.00 141.24 ? 187  LYS   A HB2  1 
ATOM   2730 H HB3  . LYS   A 1 174 ? 188.666 170.319 111.964 1.00 141.36 ? 187  LYS   A HB3  1 
ATOM   2731 H HG2  . LYS   A 1 174 ? 187.463 170.962 109.762 1.00 140.95 ? 187  LYS   A HG2  1 
ATOM   2732 H HG3  . LYS   A 1 174 ? 186.859 169.300 109.759 1.00 140.67 ? 187  LYS   A HG3  1 
ATOM   2733 H HD2  . LYS   A 1 174 ? 185.192 170.713 110.731 1.00 141.65 ? 187  LYS   A HD2  1 
ATOM   2734 H HD3  . LYS   A 1 174 ? 185.861 169.716 112.031 1.00 141.64 ? 187  LYS   A HD3  1 
ATOM   2735 H HE2  . LYS   A 1 174 ? 187.258 171.597 112.791 1.00 141.53 ? 187  LYS   A HE2  1 
ATOM   2736 H HE3  . LYS   A 1 174 ? 186.752 172.567 111.409 1.00 141.65 ? 187  LYS   A HE3  1 
ATOM   2737 H HZ1  . LYS   A 1 174 ? 185.510 173.143 113.407 1.00 142.22 ? 187  LYS   A HZ1  1 
ATOM   2738 H HZ2  . LYS   A 1 174 ? 184.498 172.545 112.282 1.00 142.46 ? 187  LYS   A HZ2  1 
ATOM   2739 H HZ3  . LYS   A 1 174 ? 184.936 171.622 113.555 1.00 141.63 ? 187  LYS   A HZ3  1 
ATOM   2740 N N    . ASN   A 1 175 ? 191.318 170.739 111.633 1.00 137.83 ? 188  ASN   A N    1 
ATOM   2741 C CA   . ASN   A 1 175 ? 192.338 170.884 112.654 1.00 136.37 ? 188  ASN   A CA   1 
ATOM   2742 C C    . ASN   A 1 175 ? 191.692 171.329 113.959 1.00 136.40 ? 188  ASN   A C    1 
ATOM   2743 O O    . ASN   A 1 175 ? 190.894 172.265 113.972 1.00 139.43 ? 188  ASN   A O    1 
ATOM   2744 C CB   . ASN   A 1 175 ? 193.374 171.903 112.171 1.00 135.86 ? 188  ASN   A CB   1 
ATOM   2745 C CG   . ASN   A 1 175 ? 194.263 171.347 111.081 1.00 141.81 ? 188  ASN   A CG   1 
ATOM   2746 O OD1  . ASN   A 1 175 ? 194.293 170.148 110.844 1.00 144.10 ? 188  ASN   A OD1  1 
ATOM   2747 N ND2  . ASN   A 1 175 ? 194.998 172.220 110.419 1.00 144.97 ? 188  ASN   A ND2  1 
ATOM   2748 H H    . ASN   A 1 175 ? 190.747 171.547 111.430 1.00 139.44 ? 188  ASN   A H    1 
ATOM   2749 H HA   . ASN   A 1 175 ? 192.833 169.930 112.839 1.00 139.62 ? 188  ASN   A HA   1 
ATOM   2750 H HB2  . ASN   A 1 175 ? 192.867 172.796 111.804 1.00 139.06 ? 188  ASN   A HB2  1 
ATOM   2751 H HB3  . ASN   A 1 175 ? 194.009 172.200 113.005 1.00 138.74 ? 188  ASN   A HB3  1 
ATOM   2752 H HD21 . ASN   A 1 175 ? 194.928 173.199 110.654 1.00 139.70 ? 188  ASN   A HD21 1 
ATOM   2753 N N    . PHE   A 1 176 ? 192.185 170.796 115.067 1.00 134.00 ? 189  PHE   A N    1 
ATOM   2754 C CA   . PHE   A 1 176 ? 191.810 171.211 116.409 1.00 136.38 ? 189  PHE   A CA   1 
ATOM   2755 C C    . PHE   A 1 176 ? 193.075 171.535 117.192 1.00 140.44 ? 189  PHE   A C    1 
ATOM   2756 O O    . PHE   A 1 176 ? 194.074 170.834 117.065 1.00 141.35 ? 189  PHE   A O    1 
ATOM   2757 C CB   . PHE   A 1 176 ? 191.011 170.090 117.069 1.00 134.56 ? 189  PHE   A CB   1 
ATOM   2758 C CG   . PHE   A 1 176 ? 189.784 169.671 116.290 1.00 135.64 ? 189  PHE   A CG   1 
ATOM   2759 C CD1  . PHE   A 1 176 ? 188.592 170.402 116.419 1.00 137.22 ? 189  PHE   A CD1  1 
ATOM   2760 C CD2  . PHE   A 1 176 ? 189.824 168.544 115.454 1.00 134.45 ? 189  PHE   A CD2  1 
ATOM   2761 C CE1  . PHE   A 1 176 ? 187.437 169.992 115.736 1.00 137.22 ? 189  PHE   A CE1  1 
ATOM   2762 C CE2  . PHE   A 1 176 ? 188.670 168.140 114.765 1.00 137.48 ? 189  PHE   A CE2  1 
ATOM   2763 C CZ   . PHE   A 1 176 ? 187.475 168.858 114.913 1.00 138.88 ? 189  PHE   A CZ   1 
ATOM   2764 H H    . PHE   A 1 176 ? 192.858 170.047 114.987 1.00 136.84 ? 189  PHE   A H    1 
ATOM   2765 H HA   . PHE   A 1 176 ? 191.189 172.106 116.376 1.00 136.92 ? 189  PHE   A HA   1 
ATOM   2766 H HB2  . PHE   A 1 176 ? 191.657 169.221 117.199 1.00 136.06 ? 189  PHE   A HB2  1 
ATOM   2767 H HB3  . PHE   A 1 176 ? 190.702 170.416 118.062 1.00 136.83 ? 189  PHE   A HB3  1 
ATOM   2768 H HD1  . PHE   A 1 176 ? 188.557 171.268 117.063 1.00 137.05 ? 189  PHE   A HD1  1 
ATOM   2769 H HD2  . PHE   A 1 176 ? 190.740 167.982 115.348 1.00 136.29 ? 189  PHE   A HD2  1 
ATOM   2770 H HE1  . PHE   A 1 176 ? 186.515 170.541 115.859 1.00 137.03 ? 189  PHE   A HE1  1 
ATOM   2771 H HE2  . PHE   A 1 176 ? 188.699 167.269 114.127 1.00 136.83 ? 189  PHE   A HE2  1 
ATOM   2772 H HZ   . PHE   A 1 176 ? 186.583 168.535 114.397 1.00 137.28 ? 189  PHE   A HZ   1 
ATOM   2773 N N    . THR   A 1 177 ? 193.087 172.589 117.993 1.00 148.01 ? 190  THR   A N    1 
ATOM   2774 C CA   . THR   A 1 177 ? 194.250 172.887 118.838 1.00 147.56 ? 190  THR   A CA   1 
ATOM   2775 C C    . THR   A 1 177 ? 194.248 172.030 120.098 1.00 144.81 ? 190  THR   A C    1 
ATOM   2776 O O    . THR   A 1 177 ? 193.193 171.648 120.604 1.00 145.80 ? 190  THR   A O    1 
ATOM   2777 C CB   . THR   A 1 177 ? 194.312 174.371 119.203 1.00 146.28 ? 190  THR   A CB   1 
ATOM   2778 O OG1  . THR   A 1 177 ? 193.083 174.814 119.736 1.00 150.28 ? 190  THR   A OG1  1 
ATOM   2779 C CG2  . THR   A 1 177 ? 194.624 175.225 117.978 1.00 141.47 ? 190  THR   A CG2  1 
ATOM   2780 H H    . THR   A 1 177 ? 192.261 173.163 118.090 1.00 144.37 ? 190  THR   A H    1 
ATOM   2781 H HA   . THR   A 1 177 ? 195.161 172.656 118.287 1.00 144.39 ? 190  THR   A HA   1 
ATOM   2782 H HB   . THR   A 1 177 ? 195.101 174.527 119.939 1.00 144.37 ? 190  THR   A HB   1 
ATOM   2783 H HG1  . THR   A 1 177 ? 192.919 174.332 120.550 1.00 145.17 ? 190  THR   A HG1  1 
ATOM   2784 H HG21 . THR   A 1 177 ? 194.701 176.271 118.275 1.00 144.02 ? 190  THR   A HG21 1 
ATOM   2785 H HG22 . THR   A 1 177 ? 193.838 175.121 117.230 1.00 143.54 ? 190  THR   A HG22 1 
ATOM   2786 H HG23 . THR   A 1 177 ? 195.575 174.912 117.547 1.00 143.61 ? 190  THR   A HG23 1 
ATOM   2787 N N    . TYR   A 1 178 ? 195.425 171.775 120.657 1.00 128.67 ? 191  TYR   A N    1 
ATOM   2788 C CA   . TYR   A 1 178 ? 195.573 171.217 121.998 1.00 125.22 ? 191  TYR   A CA   1 
ATOM   2789 C C    . TYR   A 1 178 ? 196.728 171.902 122.721 1.00 127.19 ? 191  TYR   A C    1 
ATOM   2790 O O    . TYR   A 1 178 ? 197.692 172.349 122.102 1.00 134.44 ? 191  TYR   A O    1 
ATOM   2791 C CB   . TYR   A 1 178 ? 195.746 169.696 121.941 1.00 121.24 ? 191  TYR   A CB   1 
ATOM   2792 C CG   . TYR   A 1 178 ? 197.085 169.220 121.423 1.00 119.31 ? 191  TYR   A CG   1 
ATOM   2793 C CD1  . TYR   A 1 178 ? 197.282 169.045 120.045 1.00 123.58 ? 191  TYR   A CD1  1 
ATOM   2794 C CD2  . TYR   A 1 178 ? 198.132 168.957 122.320 1.00 124.44 ? 191  TYR   A CD2  1 
ATOM   2795 C CE1  . TYR   A 1 178 ? 198.528 168.617 119.562 1.00 128.77 ? 191  TYR   A CE1  1 
ATOM   2796 C CE2  . TYR   A 1 178 ? 199.384 168.541 121.839 1.00 125.24 ? 191  TYR   A CE2  1 
ATOM   2797 C CZ   . TYR   A 1 178 ? 199.585 168.379 120.458 1.00 127.02 ? 191  TYR   A CZ   1 
ATOM   2798 O OH   . TYR   A 1 178 ? 200.805 168.039 119.974 1.00 131.03 ? 191  TYR   A OH   1 
ATOM   2799 H H    . TYR   A 1 178 ? 196.268 172.064 120.183 1.00 129.41 ? 191  TYR   A H    1 
ATOM   2800 H HA   . TYR   A 1 178 ? 194.667 171.423 122.567 1.00 128.41 ? 191  TYR   A HA   1 
ATOM   2801 H HB2  . TYR   A 1 178 ? 195.612 169.301 122.948 1.00 127.75 ? 191  TYR   A HB2  1 
ATOM   2802 H HB3  . TYR   A 1 178 ? 194.956 169.270 121.323 1.00 128.30 ? 191  TYR   A HB3  1 
ATOM   2803 H HD1  . TYR   A 1 178 ? 196.475 169.253 119.357 1.00 128.55 ? 191  TYR   A HD1  1 
ATOM   2804 H HD2  . TYR   A 1 178 ? 197.981 169.083 123.382 1.00 128.85 ? 191  TYR   A HD2  1 
ATOM   2805 H HE1  . TYR   A 1 178 ? 198.683 168.478 118.502 1.00 129.49 ? 191  TYR   A HE1  1 
ATOM   2806 H HE2  . TYR   A 1 178 ? 200.191 168.352 122.532 1.00 128.25 ? 191  TYR   A HE2  1 
ATOM   2807 H HH   . TYR   A 1 178 ? 201.417 167.807 120.677 1.00 129.24 ? 191  TYR   A HH   1 
ATOM   2808 N N    . ASN   A 1 179 ? 196.633 172.020 124.037 1.00 131.13 ? 192  ASN   A N    1 
ATOM   2809 C CA   . ASN   A 1 179 ? 197.654 172.644 124.860 1.00 129.61 ? 192  ASN   A CA   1 
ATOM   2810 C C    . ASN   A 1 179 ? 198.919 171.776 124.922 1.00 131.94 ? 192  ASN   A C    1 
ATOM   2811 O O    . ASN   A 1 179 ? 198.977 170.811 125.679 1.00 138.61 ? 192  ASN   A O    1 
ATOM   2812 C CB   . ASN   A 1 179 ? 197.034 172.906 126.235 1.00 136.42 ? 192  ASN   A CB   1 
ATOM   2813 C CG   . ASN   A 1 179 ? 197.989 173.580 127.200 1.00 142.01 ? 192  ASN   A CG   1 
ATOM   2814 O OD1  . ASN   A 1 179 ? 199.175 173.748 126.934 1.00 141.35 ? 192  ASN   A OD1  1 
ATOM   2815 N ND2  . ASN   A 1 179 ? 197.444 173.934 128.348 1.00 143.23 ? 192  ASN   A ND2  1 
ATOM   2816 H H    . ASN   A 1 179 ? 195.797 171.680 124.490 1.00 137.39 ? 192  ASN   A H    1 
ATOM   2817 H HA   . ASN   A 1 179 ? 197.923 173.606 124.422 1.00 136.55 ? 192  ASN   A HA   1 
ATOM   2818 H HB2  . ASN   A 1 179 ? 196.161 173.547 126.112 1.00 137.67 ? 192  ASN   A HB2  1 
ATOM   2819 H HB3  . ASN   A 1 179 ? 196.703 171.964 126.674 1.00 137.65 ? 192  ASN   A HB3  1 
ATOM   2820 H HD21 . ASN   A 1 179 ? 196.436 173.962 128.403 1.00 137.82 ? 192  ASN   A HD21 1 
ATOM   2821 N N    . VAL   A 1 180 ? 199.979 172.177 124.218 1.00 133.38 ? 193  VAL   A N    1 
ATOM   2822 C CA   . VAL   A 1 180 ? 201.261 171.452 124.184 1.00 137.95 ? 193  VAL   A CA   1 
ATOM   2823 C C    . VAL   A 1 180 ? 201.913 171.243 125.549 1.00 141.66 ? 193  VAL   A C    1 
ATOM   2824 O O    . VAL   A 1 180 ? 202.787 170.388 125.661 1.00 144.81 ? 193  VAL   A O    1 
ATOM   2825 C CB   . VAL   A 1 180 ? 202.283 172.151 123.274 1.00 137.15 ? 193  VAL   A CB   1 
ATOM   2826 C CG1  . VAL   A 1 180 ? 201.812 172.141 121.827 1.00 141.03 ? 193  VAL   A CG1  1 
ATOM   2827 C CG2  . VAL   A 1 180 ? 202.583 173.595 123.682 1.00 136.73 ? 193  VAL   A CG2  1 
ATOM   2828 H H    . VAL   A 1 180 ? 199.869 172.975 123.609 1.00 137.62 ? 193  VAL   A H    1 
ATOM   2829 H HA   . VAL   A 1 180 ? 201.075 170.459 123.776 1.00 137.88 ? 193  VAL   A HA   1 
ATOM   2830 H HB   . VAL   A 1 180 ? 203.218 171.591 123.310 1.00 137.92 ? 193  VAL   A HB   1 
ATOM   2831 H HG11 . VAL   A 1 180 ? 201.594 171.116 121.526 1.00 139.05 ? 193  VAL   A HG11 1 
ATOM   2832 H HG12 . VAL   A 1 180 ? 200.918 172.754 121.715 1.00 138.79 ? 193  VAL   A HG12 1 
ATOM   2833 H HG13 . VAL   A 1 180 ? 202.597 172.537 121.183 1.00 138.71 ? 193  VAL   A HG13 1 
ATOM   2834 H HG21 . VAL   A 1 180 ? 202.972 173.627 124.700 1.00 138.51 ? 193  VAL   A HG21 1 
ATOM   2835 H HG22 . VAL   A 1 180 ? 203.339 174.010 123.016 1.00 137.65 ? 193  VAL   A HG22 1 
ATOM   2836 H HG23 . VAL   A 1 180 ? 201.685 174.210 123.620 1.00 137.99 ? 193  VAL   A HG23 1 
ATOM   2837 N N    . SER   A 1 181 ? 201.526 171.987 126.585 1.00 138.18 ? 194  SER   A N    1 
ATOM   2838 C CA   . SER   A 1 181 ? 202.136 171.878 127.909 1.00 136.13 ? 194  SER   A CA   1 
ATOM   2839 C C    . SER   A 1 181 ? 201.555 170.769 128.787 1.00 137.68 ? 194  SER   A C    1 
ATOM   2840 O O    . SER   A 1 181 ? 202.224 170.378 129.743 1.00 140.92 ? 194  SER   A O    1 
ATOM   2841 C CB   . SER   A 1 181 ? 202.028 173.210 128.650 1.00 136.33 ? 194  SER   A CB   1 
ATOM   2842 O OG   . SER   A 1 181 ? 202.719 174.215 127.930 1.00 136.65 ? 194  SER   A OG   1 
ATOM   2843 H H    . SER   A 1 181 ? 200.806 172.682 126.448 1.00 138.22 ? 194  SER   A H    1 
ATOM   2844 H HA   . SER   A 1 181 ? 203.198 171.664 127.788 1.00 138.19 ? 194  SER   A HA   1 
ATOM   2845 H HB2  . SER   A 1 181 ? 200.980 173.485 128.764 1.00 138.46 ? 194  SER   A HB2  1 
ATOM   2846 H HB3  . SER   A 1 181 ? 202.476 173.110 129.639 1.00 138.24 ? 194  SER   A HB3  1 
ATOM   2847 H HG   . SER   A 1 181 ? 202.647 175.043 128.410 1.00 138.94 ? 194  SER   A HG   1 
ATOM   2848 N N    . THR   A 1 182 ? 200.347 170.257 128.535 1.00 137.62 ? 195  THR   A N    1 
ATOM   2849 C CA   . THR   A 1 182 ? 199.721 169.274 129.444 1.00 138.20 ? 195  THR   A CA   1 
ATOM   2850 C C    . THR   A 1 182 ? 200.345 167.895 129.318 1.00 135.08 ? 195  THR   A C    1 
ATOM   2851 O O    . THR   A 1 182 ? 200.906 167.557 128.284 1.00 138.49 ? 195  THR   A O    1 
ATOM   2852 C CB   . THR   A 1 182 ? 198.212 169.144 129.253 1.00 138.34 ? 195  THR   A CB   1 
ATOM   2853 O OG1  . THR   A 1 182 ? 197.893 168.562 128.021 1.00 130.89 ? 195  THR   A OG1  1 
ATOM   2854 C CG2  . THR   A 1 182 ? 197.531 170.504 129.373 1.00 144.59 ? 195  THR   A CG2  1 
ATOM   2855 H H    . THR   A 1 182 ? 199.848 170.528 127.699 1.00 137.99 ? 195  THR   A H    1 
ATOM   2856 H HA   . THR   A 1 182 ? 199.880 169.611 130.469 1.00 138.48 ? 195  THR   A HA   1 
ATOM   2857 H HB   . THR   A 1 182 ? 197.818 168.498 130.038 1.00 137.97 ? 195  THR   A HB   1 
ATOM   2858 H HG1  . THR   A 1 182 ? 196.945 168.415 128.061 1.00 138.25 ? 195  THR   A HG1  1 
ATOM   2859 H HG21 . THR   A 1 182 ? 196.447 170.402 129.322 1.00 138.77 ? 195  THR   A HG21 1 
ATOM   2860 H HG22 . THR   A 1 182 ? 197.784 170.952 130.334 1.00 139.06 ? 195  THR   A HG22 1 
ATOM   2861 H HG23 . THR   A 1 182 ? 197.866 171.161 128.571 1.00 139.11 ? 195  THR   A HG23 1 
ATOM   2862 N N    . ASP   A 1 183 ? 200.289 167.082 130.371 1.00 129.63 ? 196  ASP   A N    1 
ATOM   2863 C CA   . ASP   A 1 183 ? 200.988 165.793 130.385 1.00 127.06 ? 196  ASP   A CA   1 
ATOM   2864 C C    . ASP   A 1 183 ? 200.226 164.659 129.694 1.00 127.81 ? 196  ASP   A C    1 
ATOM   2865 O O    . ASP   A 1 183 ? 200.851 163.737 129.172 1.00 134.58 ? 196  ASP   A O    1 
ATOM   2866 C CB   . ASP   A 1 183 ? 201.317 165.417 131.830 1.00 131.08 ? 196  ASP   A CB   1 
ATOM   2867 C CG   . ASP   A 1 183 ? 202.305 166.386 132.484 1.00 140.11 ? 196  ASP   A CG   1 
ATOM   2868 O OD1  . ASP   A 1 183 ? 203.161 166.969 131.778 1.00 146.58 ? 196  ASP   A OD1  1 
ATOM   2869 O OD2  . ASP   A 1 183 ? 202.233 166.549 133.722 1.00 136.75 ? 196  ASP   A OD2  1 
ATOM   2870 H H    . ASP   A 1 183 ? 199.836 167.393 131.218 1.00 132.60 ? 196  ASP   A H    1 
ATOM   2871 H HA   . ASP   A 1 183 ? 201.933 165.893 129.850 1.00 132.03 ? 196  ASP   A HA   1 
ATOM   2872 H HB2  . ASP   A 1 183 ? 200.393 165.383 132.407 1.00 132.08 ? 196  ASP   A HB2  1 
ATOM   2873 H HB3  . ASP   A 1 183 ? 201.757 164.420 131.841 1.00 132.63 ? 196  ASP   A HB3  1 
ATOM   2874 N N    . TRP   A 1 184 ? 198.897 164.725 129.645 1.00 116.77 ? 197  TRP   A N    1 
ATOM   2875 C CA   . TRP   A 1 184 ? 198.049 163.667 129.096 1.00 117.36 ? 197  TRP   A CA   1 
ATOM   2876 C C    . TRP   A 1 184 ? 196.978 164.216 128.166 1.00 119.47 ? 197  TRP   A C    1 
ATOM   2877 O O    . TRP   A 1 184 ? 196.441 165.292 128.407 1.00 128.19 ? 197  TRP   A O    1 
ATOM   2878 C CB   . TRP   A 1 184 ? 197.393 162.883 130.233 1.00 113.98 ? 197  TRP   A CB   1 
ATOM   2879 C CG   . TRP   A 1 184 ? 198.360 162.241 131.166 1.00 113.48 ? 197  TRP   A CG   1 
ATOM   2880 C CD1  . TRP   A 1 184 ? 198.820 162.786 132.311 1.00 120.27 ? 197  TRP   A CD1  1 
ATOM   2881 C CD2  . TRP   A 1 184 ? 199.083 160.992 131.002 1.00 109.11 ? 197  TRP   A CD2  1 
ATOM   2882 N NE1  . TRP   A 1 184 ? 199.793 161.974 132.851 1.00 120.48 ? 197  TRP   A NE1  1 
ATOM   2883 C CE2  . TRP   A 1 184 ? 200.023 160.875 132.061 1.00 114.62 ? 197  TRP   A CE2  1 
ATOM   2884 C CE3  . TRP   A 1 184 ? 199.055 159.956 130.053 1.00 113.29 ? 197  TRP   A CE3  1 
ATOM   2885 C CZ2  . TRP   A 1 184 ? 200.928 159.815 132.150 1.00 116.40 ? 197  TRP   A CZ2  1 
ATOM   2886 C CZ3  . TRP   A 1 184 ? 199.947 158.876 130.138 1.00 120.93 ? 197  TRP   A CZ3  1 
ATOM   2887 C CH2  . TRP   A 1 184 ? 200.893 158.813 131.172 1.00 119.96 ? 197  TRP   A CH2  1 
ATOM   2888 H H    . TRP   A 1 184 ? 198.441 165.538 130.035 1.00 118.68 ? 197  TRP   A H    1 
ATOM   2889 H HA   . TRP   A 1 184 ? 198.664 162.972 128.524 1.00 119.29 ? 197  TRP   A HA   1 
ATOM   2890 H HB2  . TRP   A 1 184 ? 196.744 163.551 130.800 1.00 118.64 ? 197  TRP   A HB2  1 
ATOM   2891 H HB3  . TRP   A 1 184 ? 196.768 162.101 129.802 1.00 118.19 ? 197  TRP   A HB3  1 
ATOM   2892 H HD1  . TRP   A 1 184 ? 198.508 163.740 132.711 1.00 119.27 ? 197  TRP   A HD1  1 
ATOM   2893 H HE1  . TRP   A 1 184 ? 200.306 162.204 133.690 1.00 119.55 ? 197  TRP   A HE1  1 
ATOM   2894 H HE3  . TRP   A 1 184 ? 198.347 160.012 129.239 1.00 118.53 ? 197  TRP   A HE3  1 
ATOM   2895 H HZ2  . TRP   A 1 184 ? 201.643 159.773 132.958 1.00 118.57 ? 197  TRP   A HZ2  1 
ATOM   2896 H HZ3  . TRP   A 1 184 ? 199.922 158.096 129.391 1.00 118.84 ? 197  TRP   A HZ3  1 
ATOM   2897 H HH2  . TRP   A 1 184 ? 201.587 157.986 131.221 1.00 118.89 ? 197  TRP   A HH2  1 
ATOM   2898 N N    . LEU   A 1 185 ? 196.609 163.441 127.152 1.00 114.12 ? 198  LEU   A N    1 
ATOM   2899 C CA   . LEU   A 1 185 ? 195.392 163.639 126.378 1.00 119.94 ? 198  LEU   A CA   1 
ATOM   2900 C C    . LEU   A 1 185 ? 194.514 162.403 126.494 1.00 123.94 ? 198  LEU   A C    1 
ATOM   2901 O O    . LEU   A 1 185 ? 195.015 161.284 126.558 1.00 128.71 ? 198  LEU   A O    1 
ATOM   2902 C CB   . LEU   A 1 185 ? 195.688 163.932 124.905 1.00 115.92 ? 198  LEU   A CB   1 
ATOM   2903 C CG   . LEU   A 1 185 ? 196.366 165.285 124.669 1.00 119.15 ? 198  LEU   A CG   1 
ATOM   2904 C CD1  . LEU   A 1 185 ? 197.878 165.138 124.564 1.00 126.00 ? 198  LEU   A CD1  1 
ATOM   2905 C CD2  . LEU   A 1 185 ? 195.871 165.892 123.362 1.00 122.38 ? 198  LEU   A CD2  1 
ATOM   2906 H H    . LEU   A 1 185 ? 197.113 162.577 127.009 1.00 121.42 ? 198  LEU   A H    1 
ATOM   2907 H HA   . LEU   A 1 185 ? 194.829 164.479 126.785 1.00 123.43 ? 198  LEU   A HA   1 
ATOM   2908 H HB2  . LEU   A 1 185 ? 196.288 163.131 124.473 1.00 121.28 ? 198  LEU   A HB2  1 
ATOM   2909 H HB3  . LEU   A 1 185 ? 194.730 163.933 124.385 1.00 122.38 ? 198  LEU   A HB3  1 
ATOM   2910 H HG   . LEU   A 1 185 ? 196.123 165.972 125.480 1.00 121.85 ? 198  LEU   A HG   1 
ATOM   2911 H HD11 . LEU   A 1 185 ? 198.271 164.706 125.484 1.00 122.92 ? 198  LEU   A HD11 1 
ATOM   2912 H HD12 . LEU   A 1 185 ? 198.135 164.490 123.725 1.00 122.97 ? 198  LEU   A HD12 1 
ATOM   2913 H HD13 . LEU   A 1 185 ? 198.331 166.118 124.412 1.00 123.30 ? 198  LEU   A HD13 1 
ATOM   2914 H HD21 . LEU   A 1 185 ? 194.798 166.072 123.421 1.00 121.63 ? 198  LEU   A HD21 1 
ATOM   2915 H HD22 . LEU   A 1 185 ? 196.374 166.843 123.185 1.00 122.46 ? 198  LEU   A HD22 1 
ATOM   2916 H HD23 . LEU   A 1 185 ? 196.082 165.217 122.533 1.00 123.29 ? 198  LEU   A HD23 1 
ATOM   2917 N N    . TYR   A 1 186 ? 193.204 162.599 126.482 1.00 115.64 ? 199  TYR   A N    1 
ATOM   2918 C CA   . TYR   A 1 186 ? 192.219 161.531 126.553 1.00 105.85 ? 199  TYR   A CA   1 
ATOM   2919 C C    . TYR   A 1 186 ? 191.301 161.591 125.345 1.00 106.07 ? 199  TYR   A C    1 
ATOM   2920 O O    . TYR   A 1 186 ? 190.882 162.682 124.979 1.00 120.58 ? 199  TYR   A O    1 
ATOM   2921 C CB   . TYR   A 1 186 ? 191.425 161.674 127.846 1.00 109.29 ? 199  TYR   A CB   1 
ATOM   2922 C CG   . TYR   A 1 186 ? 192.278 161.494 129.078 1.00 111.77 ? 199  TYR   A CG   1 
ATOM   2923 C CD1  . TYR   A 1 186 ? 192.608 160.197 129.496 1.00 116.44 ? 199  TYR   A CD1  1 
ATOM   2924 C CD2  . TYR   A 1 186 ? 192.781 162.606 129.771 1.00 115.17 ? 199  TYR   A CD2  1 
ATOM   2925 C CE1  . TYR   A 1 186 ? 193.432 160.008 130.613 1.00 120.15 ? 199  TYR   A CE1  1 
ATOM   2926 C CE2  . TYR   A 1 186 ? 193.632 162.422 130.873 1.00 119.02 ? 199  TYR   A CE2  1 
ATOM   2927 C CZ   . TYR   A 1 186 ? 193.965 161.118 131.289 1.00 122.89 ? 199  TYR   A CZ   1 
ATOM   2928 O OH   . TYR   A 1 186 ? 194.814 160.920 132.327 1.00 122.38 ? 199  TYR   A OH   1 
ATOM   2929 H H    . TYR   A 1 186 ? 192.865 163.549 126.432 1.00 117.65 ? 199  TYR   A H    1 
ATOM   2930 H HA   . TYR   A 1 186 ? 192.719 160.562 126.564 1.00 117.12 ? 199  TYR   A HA   1 
ATOM   2931 H HB2  . TYR   A 1 186 ? 190.954 162.656 127.874 1.00 116.54 ? 199  TYR   A HB2  1 
ATOM   2932 H HB3  . TYR   A 1 186 ? 190.634 160.924 127.857 1.00 116.39 ? 199  TYR   A HB3  1 
ATOM   2933 H HD1  . TYR   A 1 186 ? 192.240 159.344 128.946 1.00 117.23 ? 199  TYR   A HD1  1 
ATOM   2934 H HD2  . TYR   A 1 186 ? 192.532 163.606 129.446 1.00 117.36 ? 199  TYR   A HD2  1 
ATOM   2935 H HE1  . TYR   A 1 186 ? 193.672 159.011 130.952 1.00 117.07 ? 199  TYR   A HE1  1 
ATOM   2936 H HE2  . TYR   A 1 186 ? 194.031 163.280 131.393 1.00 117.47 ? 199  TYR   A HE2  1 
ATOM   2937 H HH   . TYR   A 1 186 ? 195.106 161.755 132.700 1.00 118.11 ? 199  TYR   A HH   1 
ATOM   2938 N N    . PHE   A 1 187 ? 190.953 160.452 124.748 1.00 96.47  ? 200  PHE   A N    1 
ATOM   2939 C CA   . PHE   A 1 187 ? 190.057 160.382 123.593 1.00 101.17 ? 200  PHE   A CA   1 
ATOM   2940 C C    . PHE   A 1 187 ? 189.026 159.270 123.726 1.00 106.60 ? 200  PHE   A C    1 
ATOM   2941 O O    . PHE   A 1 187 ? 189.389 158.155 124.082 1.00 111.03 ? 200  PHE   A O    1 
ATOM   2942 C CB   . PHE   A 1 187 ? 190.834 160.120 122.303 1.00 105.14 ? 200  PHE   A CB   1 
ATOM   2943 C CG   . PHE   A 1 187 ? 191.889 161.132 121.943 1.00 106.05 ? 200  PHE   A CG   1 
ATOM   2944 C CD1  . PHE   A 1 187 ? 193.205 160.984 122.405 1.00 106.52 ? 200  PHE   A CD1  1 
ATOM   2945 C CD2  . PHE   A 1 187 ? 191.560 162.207 121.107 1.00 104.33 ? 200  PHE   A CD2  1 
ATOM   2946 C CE1  . PHE   A 1 187 ? 194.192 161.906 122.027 1.00 105.38 ? 200  PHE   A CE1  1 
ATOM   2947 C CE2  . PHE   A 1 187 ? 192.543 163.136 120.742 1.00 109.25 ? 200  PHE   A CE2  1 
ATOM   2948 C CZ   . PHE   A 1 187 ? 193.861 162.984 121.194 1.00 109.93 ? 200  PHE   A CZ   1 
ATOM   2949 H H    . PHE   A 1 187 ? 191.329 159.588 125.112 1.00 109.85 ? 200  PHE   A H    1 
ATOM   2950 H HA   . PHE   A 1 187 ? 189.529 161.330 123.488 1.00 109.53 ? 200  PHE   A HA   1 
ATOM   2951 H HB2  . PHE   A 1 187 ? 191.300 159.136 122.358 1.00 109.20 ? 200  PHE   A HB2  1 
ATOM   2952 H HB3  . PHE   A 1 187 ? 190.115 160.077 121.486 1.00 109.37 ? 200  PHE   A HB3  1 
ATOM   2953 H HD1  . PHE   A 1 187 ? 193.462 160.158 123.051 1.00 110.26 ? 200  PHE   A HD1  1 
ATOM   2954 H HD2  . PHE   A 1 187 ? 190.549 162.323 120.747 1.00 108.78 ? 200  PHE   A HD2  1 
ATOM   2955 H HE1  . PHE   A 1 187 ? 195.206 161.793 122.381 1.00 109.32 ? 200  PHE   A HE1  1 
ATOM   2956 H HE2  . PHE   A 1 187 ? 192.280 163.973 120.112 1.00 109.91 ? 200  PHE   A HE2  1 
ATOM   2957 H HZ   . PHE   A 1 187 ? 194.618 163.699 120.906 1.00 110.23 ? 200  PHE   A HZ   1 
ATOM   2958 N N    . HIS   A 1 188 ? 187.781 159.512 123.327 1.00 107.89 ? 201  HIS   A N    1 
ATOM   2959 C CA   . HIS   A 1 188 ? 186.836 158.445 122.992 1.00 108.97 ? 201  HIS   A CA   1 
ATOM   2960 C C    . HIS   A 1 188 ? 186.642 158.427 121.490 1.00 112.02 ? 201  HIS   A C    1 
ATOM   2961 O O    . HIS   A 1 188 ? 186.276 159.451 120.921 1.00 126.22 ? 201  HIS   A O    1 
ATOM   2962 C CB   . HIS   A 1 188 ? 185.463 158.652 123.633 1.00 104.97 ? 201  HIS   A CB   1 
ATOM   2963 C CG   . HIS   A 1 188 ? 185.445 158.650 125.129 1.00 109.35 ? 201  HIS   A CG   1 
ATOM   2964 N ND1  . HIS   A 1 188 ? 186.043 159.608 125.940 1.00 117.19 ? 201  HIS   A ND1  1 
ATOM   2965 C CD2  . HIS   A 1 188 ? 184.778 157.755 125.906 1.00 111.96 ? 201  HIS   A CD2  1 
ATOM   2966 C CE1  . HIS   A 1 188 ? 185.738 159.256 127.196 1.00 119.89 ? 201  HIS   A CE1  1 
ATOM   2967 N NE2  . HIS   A 1 188 ? 184.992 158.144 127.203 1.00 116.70 ? 201  HIS   A NE2  1 
ATOM   2968 H H    . HIS   A 1 188 ? 187.564 160.445 123.007 1.00 113.22 ? 201  HIS   A H    1 
ATOM   2969 H HA   . HIS   A 1 188 ? 187.219 157.475 123.308 1.00 113.92 ? 201  HIS   A HA   1 
ATOM   2970 H HB2  . HIS   A 1 188 ? 185.038 159.595 123.288 1.00 111.81 ? 201  HIS   A HB2  1 
ATOM   2971 H HB3  . HIS   A 1 188 ? 184.802 157.858 123.287 1.00 113.31 ? 201  HIS   A HB3  1 
ATOM   2972 H HD2  . HIS   A 1 188 ? 184.185 156.920 125.564 1.00 113.60 ? 201  HIS   A HD2  1 
ATOM   2973 H HE1  . HIS   A 1 188 ? 186.051 159.792 128.080 1.00 115.00 ? 201  HIS   A HE1  1 
ATOM   2974 H HE2  . HIS   A 1 188 ? 184.656 157.683 128.036 1.00 114.15 ? 201  HIS   A HE2  1 
ATOM   2975 N N    . PHE   A 1 189 ? 186.819 157.274 120.859 1.00 104.10 ? 202  PHE   A N    1 
ATOM   2976 C CA   . PHE   A 1 189 ? 186.411 157.040 119.482 1.00 104.41 ? 202  PHE   A CA   1 
ATOM   2977 C C    . PHE   A 1 189 ? 185.398 155.904 119.467 1.00 113.78 ? 202  PHE   A C    1 
ATOM   2978 O O    . PHE   A 1 189 ? 185.723 154.802 119.895 1.00 124.07 ? 202  PHE   A O    1 
ATOM   2979 C CB   . PHE   A 1 189 ? 187.644 156.694 118.646 1.00 107.91 ? 202  PHE   A CB   1 
ATOM   2980 C CG   . PHE   A 1 189 ? 188.741 157.732 118.673 1.00 106.44 ? 202  PHE   A CG   1 
ATOM   2981 C CD1  . PHE   A 1 189 ? 188.463 159.057 118.304 1.00 110.53 ? 202  PHE   A CD1  1 
ATOM   2982 C CD2  . PHE   A 1 189 ? 190.041 157.373 119.058 1.00 106.61 ? 202  PHE   A CD2  1 
ATOM   2983 C CE1  . PHE   A 1 189 ? 189.482 160.020 118.318 1.00 114.45 ? 202  PHE   A CE1  1 
ATOM   2984 C CE2  . PHE   A 1 189 ? 191.059 158.336 119.074 1.00 113.04 ? 202  PHE   A CE2  1 
ATOM   2985 C CZ   . PHE   A 1 189 ? 190.780 159.660 118.704 1.00 115.46 ? 202  PHE   A CZ   1 
ATOM   2986 H H    . PHE   A 1 189 ? 187.136 156.474 121.388 1.00 113.14 ? 202  PHE   A H    1 
ATOM   2987 H HA   . PHE   A 1 189 ? 185.942 157.928 119.061 1.00 111.88 ? 202  PHE   A HA   1 
ATOM   2988 H HB2  . PHE   A 1 189 ? 188.050 155.745 118.996 1.00 112.80 ? 202  PHE   A HB2  1 
ATOM   2989 H HB3  . PHE   A 1 189 ? 187.331 156.550 117.612 1.00 113.21 ? 202  PHE   A HB3  1 
ATOM   2990 H HD1  . PHE   A 1 189 ? 187.464 159.338 118.006 1.00 112.19 ? 202  PHE   A HD1  1 
ATOM   2991 H HD2  . PHE   A 1 189 ? 190.263 156.356 119.343 1.00 111.70 ? 202  PHE   A HD2  1 
ATOM   2992 H HE1  . PHE   A 1 189 ? 189.269 161.039 118.030 1.00 113.17 ? 202  PHE   A HE1  1 
ATOM   2993 H HE2  . PHE   A 1 189 ? 192.059 158.059 119.374 1.00 113.08 ? 202  PHE   A HE2  1 
ATOM   2994 H HZ   . PHE   A 1 189 ? 191.566 160.401 118.718 1.00 113.25 ? 202  PHE   A HZ   1 
ATOM   2995 N N    . TYR   A 1 190 ? 184.182 156.125 118.984 1.00 113.09 ? 203  TYR   A N    1 
ATOM   2996 C CA   . TYR   A 1 190 ? 183.169 155.071 118.915 1.00 113.62 ? 203  TYR   A CA   1 
ATOM   2997 C C    . TYR   A 1 190 ? 182.270 155.236 117.705 1.00 118.90 ? 203  TYR   A C    1 
ATOM   2998 O O    . TYR   A 1 190 ? 182.235 156.299 117.093 1.00 129.89 ? 203  TYR   A O    1 
ATOM   2999 C CB   . TYR   A 1 190 ? 182.364 154.989 120.216 1.00 115.54 ? 203  TYR   A CB   1 
ATOM   3000 C CG   . TYR   A 1 190 ? 181.418 156.132 120.503 1.00 112.53 ? 203  TYR   A CG   1 
ATOM   3001 C CD1  . TYR   A 1 190 ? 180.145 156.162 119.911 1.00 114.96 ? 203  TYR   A CD1  1 
ATOM   3002 C CD2  . TYR   A 1 190 ? 181.780 157.124 121.426 1.00 117.21 ? 203  TYR   A CD2  1 
ATOM   3003 C CE1  . TYR   A 1 190 ? 179.248 157.199 120.212 1.00 118.30 ? 203  TYR   A CE1  1 
ATOM   3004 C CE2  . TYR   A 1 190 ? 180.878 158.149 121.751 1.00 121.06 ? 203  TYR   A CE2  1 
ATOM   3005 C CZ   . TYR   A 1 190 ? 179.615 158.198 121.132 1.00 121.32 ? 203  TYR   A CZ   1 
ATOM   3006 O OH   . TYR   A 1 190 ? 178.749 159.201 121.425 1.00 125.43 ? 203  TYR   A OH   1 
ATOM   3007 H H    . TYR   A 1 190 ? 183.948 157.038 118.622 1.00 118.74 ? 203  TYR   A H    1 
ATOM   3008 H HA   . TYR   A 1 190 ? 183.675 154.115 118.783 1.00 119.12 ? 203  TYR   A HA   1 
ATOM   3009 H HB2  . TYR   A 1 190 ? 181.770 154.075 120.200 1.00 119.20 ? 203  TYR   A HB2  1 
ATOM   3010 H HB3  . TYR   A 1 190 ? 183.059 154.889 121.050 1.00 119.72 ? 203  TYR   A HB3  1 
ATOM   3011 H HD1  . TYR   A 1 190 ? 179.843 155.379 119.231 1.00 119.17 ? 203  TYR   A HD1  1 
ATOM   3012 H HD2  . TYR   A 1 190 ? 182.748 157.088 121.905 1.00 119.06 ? 203  TYR   A HD2  1 
ATOM   3013 H HE1  . TYR   A 1 190 ? 178.276 157.224 119.743 1.00 119.21 ? 203  TYR   A HE1  1 
ATOM   3014 H HE2  . TYR   A 1 190 ? 181.147 158.895 122.484 1.00 119.64 ? 203  TYR   A HE2  1 
ATOM   3015 H HH   . TYR   A 1 190 ? 177.926 159.097 120.941 1.00 120.11 ? 203  TYR   A HH   1 
ATOM   3016 N N    . GLN   A 1 191 ? 181.541 154.187 117.346 1.00 118.28 ? 204  GLN   A N    1 
ATOM   3017 C CA   . GLN   A 1 191 ? 180.603 154.219 116.233 1.00 116.48 ? 204  GLN   A CA   1 
ATOM   3018 C C    . GLN   A 1 191 ? 179.214 153.768 116.658 1.00 114.71 ? 204  GLN   A C    1 
ATOM   3019 O O    . GLN   A 1 191 ? 179.057 152.807 117.403 1.00 121.16 ? 204  GLN   A O    1 
ATOM   3020 C CB   . GLN   A 1 191 ? 181.141 153.399 115.058 1.00 113.92 ? 204  GLN   A CB   1 
ATOM   3021 C CG   . GLN   A 1 191 ? 181.282 151.900 115.361 1.00 116.21 ? 204  GLN   A CG   1 
ATOM   3022 C CD   . GLN   A 1 191 ? 181.827 151.114 114.181 1.00 118.31 ? 204  GLN   A CD   1 
ATOM   3023 O OE1  . GLN   A 1 191 ? 181.766 151.526 113.032 1.00 122.02 ? 204  GLN   A OE1  1 
ATOM   3024 N NE2  . GLN   A 1 191 ? 182.365 149.942 114.416 1.00 120.95 ? 204  GLN   A NE2  1 
ATOM   3025 H H    . GLN   A 1 191 ? 181.611 153.340 117.891 1.00 120.39 ? 204  GLN   A H    1 
ATOM   3026 H HA   . GLN   A 1 191 ? 180.508 155.247 115.883 1.00 120.30 ? 204  GLN   A HA   1 
ATOM   3027 H HB2  . GLN   A 1 191 ? 180.461 153.528 114.216 1.00 119.73 ? 204  GLN   A HB2  1 
ATOM   3028 H HB3  . GLN   A 1 191 ? 182.114 153.797 114.770 1.00 119.41 ? 204  GLN   A HB3  1 
ATOM   3029 H HG2  . GLN   A 1 191 ? 181.950 151.763 116.212 1.00 120.15 ? 204  GLN   A HG2  1 
ATOM   3030 H HG3  . GLN   A 1 191 ? 180.311 151.475 115.614 1.00 120.13 ? 204  GLN   A HG3  1 
ATOM   3031 H HE21 . GLN   A 1 191 ? 182.426 149.573 115.354 1.00 120.79 ? 204  GLN   A HE21 1 
ATOM   3032 H HE22 . GLN   A 1 191 ? 182.786 149.443 113.645 1.00 120.84 ? 204  GLN   A HE22 1 
ATOM   3033 N N    . GLU   A 1 192 ? 178.189 154.440 116.159 1.00 130.85 ? 205  GLU   A N    1 
ATOM   3034 C CA   . GLU   A 1 192 ? 176.799 154.036 116.330 1.00 134.81 ? 205  GLU   A CA   1 
ATOM   3035 C C    . GLU   A 1 192 ? 176.037 154.299 115.030 1.00 137.15 ? 205  GLU   A C    1 
ATOM   3036 O O    . GLU   A 1 192 ? 176.182 155.372 114.446 1.00 139.07 ? 205  GLU   A O    1 
ATOM   3037 C CB   . GLU   A 1 192 ? 176.207 154.776 117.538 1.00 139.99 ? 205  GLU   A CB   1 
ATOM   3038 C CG   . GLU   A 1 192 ? 174.745 154.406 117.790 1.00 144.84 ? 205  GLU   A CG   1 
ATOM   3039 C CD   . GLU   A 1 192 ? 174.210 155.035 119.080 1.00 148.23 ? 205  GLU   A CD   1 
ATOM   3040 O OE1  . GLU   A 1 192 ? 174.478 154.480 120.170 1.00 151.26 ? 205  GLU   A OE1  1 
ATOM   3041 O OE2  . GLU   A 1 192 ? 173.495 156.058 118.997 1.00 144.17 ? 205  GLU   A OE2  1 
ATOM   3042 H H    . GLU   A 1 192 ? 178.377 155.223 115.549 1.00 138.11 ? 205  GLU   A H    1 
ATOM   3043 H HA   . GLU   A 1 192 ? 176.750 152.966 116.533 1.00 137.95 ? 205  GLU   A HA   1 
ATOM   3044 H HB2  . GLU   A 1 192 ? 176.791 154.523 118.423 1.00 138.85 ? 205  GLU   A HB2  1 
ATOM   3045 H HB3  . GLU   A 1 192 ? 176.276 155.852 117.379 1.00 138.59 ? 205  GLU   A HB3  1 
ATOM   3046 H HG2  . GLU   A 1 192 ? 174.145 154.745 116.946 1.00 139.28 ? 205  GLU   A HG2  1 
ATOM   3047 H HG3  . GLU   A 1 192 ? 174.660 153.321 117.849 1.00 139.59 ? 205  GLU   A HG3  1 
ATOM   3048 N N    . ARG   A 1 193 ? 175.237 153.338 114.553 1.00 131.62 ? 206  ARG   A N    1 
ATOM   3049 C CA   . ARG   A 1 193 ? 174.408 153.475 113.339 1.00 133.61 ? 206  ARG   A CA   1 
ATOM   3050 C C    . ARG   A 1 193 ? 175.173 154.055 112.141 1.00 137.58 ? 206  ARG   A C    1 
ATOM   3051 O O    . ARG   A 1 193 ? 174.720 154.990 111.487 1.00 142.08 ? 206  ARG   A O    1 
ATOM   3052 C CB   . ARG   A 1 193 ? 173.137 154.275 113.669 1.00 141.83 ? 206  ARG   A CB   1 
ATOM   3053 C CG   . ARG   A 1 193 ? 172.240 153.576 114.694 1.00 143.05 ? 206  ARG   A CG   1 
ATOM   3054 C CD   . ARG   A 1 193 ? 171.005 154.437 114.958 1.00 141.80 ? 206  ARG   A CD   1 
ATOM   3055 N NE   . ARG   A 1 193 ? 170.086 153.776 115.897 1.00 140.39 ? 206  ARG   A NE   1 
ATOM   3056 C CZ   . ARG   A 1 193 ? 170.004 153.966 117.199 1.00 142.42 ? 206  ARG   A CZ   1 
ATOM   3057 N NH1  . ARG   A 1 193 ? 169.125 153.310 117.897 1.00 146.50 ? 206  ARG   A NH1  1 
ATOM   3058 N NH2  . ARG   A 1 193 ? 170.774 154.799 117.838 1.00 142.84 ? 206  ARG   A NH2  1 
ATOM   3059 H H    . ARG   A 1 193 ? 175.173 152.475 115.074 1.00 138.56 ? 206  ARG   A H    1 
ATOM   3060 H HA   . ARG   A 1 193 ? 174.098 152.480 113.022 1.00 138.60 ? 206  ARG   A HA   1 
ATOM   3061 H HB2  . ARG   A 1 193 ? 173.414 155.260 114.043 1.00 139.46 ? 206  ARG   A HB2  1 
ATOM   3062 H HB3  . ARG   A 1 193 ? 172.556 154.408 112.756 1.00 140.50 ? 206  ARG   A HB3  1 
ATOM   3063 H HG2  . ARG   A 1 193 ? 171.930 152.608 114.299 1.00 140.43 ? 206  ARG   A HG2  1 
ATOM   3064 H HG3  . ARG   A 1 193 ? 172.779 153.420 115.629 1.00 139.36 ? 206  ARG   A HG3  1 
ATOM   3065 H HD2  . ARG   A 1 193 ? 171.314 155.412 115.336 1.00 139.22 ? 206  ARG   A HD2  1 
ATOM   3066 H HD3  . ARG   A 1 193 ? 170.484 154.600 114.014 1.00 140.55 ? 206  ARG   A HD3  1 
ATOM   3067 H HE   . ARG   A 1 193 ? 169.435 153.111 115.505 1.00 139.89 ? 206  ARG   A HE   1 
ATOM   3068 H HH11 . ARG   A 1 193 ? 168.501 152.660 117.441 1.00 140.41 ? 206  ARG   A HH11 1 
ATOM   3069 H HH12 . ARG   A 1 193 ? 169.056 153.461 118.893 1.00 140.60 ? 206  ARG   A HH12 1 
ATOM   3070 H HH21 . ARG   A 1 193 ? 171.464 155.337 117.334 1.00 139.31 ? 206  ARG   A HH21 1 
ATOM   3071 H HH22 . ARG   A 1 193 ? 170.674 154.927 118.835 1.00 140.77 ? 206  ARG   A HH22 1 
ATOM   3072 N N    . GLY   A 1 194 ? 176.375 153.548 111.876 1.00 142.24 ? 207  GLY   A N    1 
ATOM   3073 C CA   . GLY   A 1 194 ? 177.203 153.985 110.744 1.00 145.43 ? 207  GLY   A CA   1 
ATOM   3074 C C    . GLY   A 1 194 ? 177.766 155.405 110.855 1.00 141.47 ? 207  GLY   A C    1 
ATOM   3075 O O    . GLY   A 1 194 ? 178.320 155.920 109.885 1.00 142.13 ? 207  GLY   A O    1 
ATOM   3076 H H    . GLY   A 1 194 ? 176.701 152.786 112.453 1.00 141.07 ? 207  GLY   A H    1 
ATOM   3077 H HA2  . GLY   A 1 194 ? 178.047 153.303 110.648 1.00 141.46 ? 207  GLY   A HA2  1 
ATOM   3078 H HA3  . GLY   A 1 194 ? 176.615 153.928 109.828 1.00 141.86 ? 207  GLY   A HA3  1 
ATOM   3079 N N    . THR   A 1 195 ? 177.638 156.048 112.014 1.00 126.09 ? 208  THR   A N    1 
ATOM   3080 C CA   . THR   A 1 195 ? 178.245 157.345 112.320 1.00 124.74 ? 208  THR   A CA   1 
ATOM   3081 C C    . THR   A 1 195 ? 179.367 157.163 113.325 1.00 121.25 ? 208  THR   A C    1 
ATOM   3082 O O    . THR   A 1 195 ? 179.172 156.553 114.371 1.00 125.03 ? 208  THR   A O    1 
ATOM   3083 C CB   . THR   A 1 195 ? 177.199 158.310 112.872 1.00 125.22 ? 208  THR   A CB   1 
ATOM   3084 O OG1  . THR   A 1 195 ? 176.198 158.497 111.903 1.00 130.39 ? 208  THR   A OG1  1 
ATOM   3085 C CG2  . THR   A 1 195 ? 177.757 159.691 113.190 1.00 126.75 ? 208  THR   A CG2  1 
ATOM   3086 H H    . THR   A 1 195 ? 177.156 155.583 112.770 1.00 127.60 ? 208  THR   A H    1 
ATOM   3087 H HA   . THR   A 1 195 ? 178.663 157.786 111.415 1.00 127.29 ? 208  THR   A HA   1 
ATOM   3088 H HB   . THR   A 1 195 ? 176.750 157.894 113.774 1.00 126.80 ? 208  THR   A HB   1 
ATOM   3089 H HG1  . THR   A 1 195 ? 175.752 157.653 111.803 1.00 127.71 ? 208  THR   A HG1  1 
ATOM   3090 H HG21 . THR   A 1 195 ? 176.947 160.342 113.517 1.00 126.94 ? 208  THR   A HG21 1 
ATOM   3091 H HG22 . THR   A 1 195 ? 178.224 160.119 112.303 1.00 127.10 ? 208  THR   A HG22 1 
ATOM   3092 H HG23 . THR   A 1 195 ? 178.488 159.625 113.995 1.00 126.91 ? 208  THR   A HG23 1 
ATOM   3093 N N    . PHE   A 1 196 ? 180.543 157.688 113.017 1.00 112.41 ? 209  PHE   A N    1 
ATOM   3094 C CA   . PHE   A 1 196 ? 181.674 157.761 113.929 1.00 109.80 ? 209  PHE   A CA   1 
ATOM   3095 C C    . PHE   A 1 196 ? 181.575 159.005 114.807 1.00 118.67 ? 209  PHE   A C    1 
ATOM   3096 O O    . PHE   A 1 196 ? 181.138 160.051 114.336 1.00 127.34 ? 209  PHE   A O    1 
ATOM   3097 C CB   . PHE   A 1 196 ? 182.941 157.782 113.083 1.00 112.78 ? 209  PHE   A CB   1 
ATOM   3098 C CG   . PHE   A 1 196 ? 184.219 157.904 113.870 1.00 114.99 ? 209  PHE   A CG   1 
ATOM   3099 C CD1  . PHE   A 1 196 ? 184.822 156.755 114.397 1.00 117.02 ? 209  PHE   A CD1  1 
ATOM   3100 C CD2  . PHE   A 1 196 ? 184.830 159.155 114.037 1.00 118.57 ? 209  PHE   A CD2  1 
ATOM   3101 C CE1  . PHE   A 1 196 ? 186.057 156.847 115.051 1.00 119.17 ? 209  PHE   A CE1  1 
ATOM   3102 C CE2  . PHE   A 1 196 ? 186.059 159.248 114.705 1.00 118.32 ? 209  PHE   A CE2  1 
ATOM   3103 C CZ   . PHE   A 1 196 ? 186.678 158.094 115.204 1.00 117.15 ? 209  PHE   A CZ   1 
ATOM   3104 H H    . PHE   A 1 196 ? 180.618 158.212 112.157 1.00 119.38 ? 209  PHE   A H    1 
ATOM   3105 H HA   . PHE   A 1 196 ? 181.696 156.879 114.569 1.00 118.54 ? 209  PHE   A HA   1 
ATOM   3106 H HB2  . PHE   A 1 196 ? 182.984 156.864 112.496 1.00 118.84 ? 209  PHE   A HB2  1 
ATOM   3107 H HB3  . PHE   A 1 196 ? 182.885 158.613 112.380 1.00 118.61 ? 209  PHE   A HB3  1 
ATOM   3108 H HD1  . PHE   A 1 196 ? 184.345 155.792 114.284 1.00 118.92 ? 209  PHE   A HD1  1 
ATOM   3109 H HD2  . PHE   A 1 196 ? 184.367 160.045 113.637 1.00 118.78 ? 209  PHE   A HD2  1 
ATOM   3110 H HE1  . PHE   A 1 196 ? 186.537 155.954 115.424 1.00 119.42 ? 209  PHE   A HE1  1 
ATOM   3111 H HE2  . PHE   A 1 196 ? 186.539 160.207 114.827 1.00 118.74 ? 209  PHE   A HE2  1 
ATOM   3112 H HZ   . PHE   A 1 196 ? 187.635 158.167 115.698 1.00 118.54 ? 209  PHE   A HZ   1 
ATOM   3113 N N    . TYR   A 1 197 ? 182.012 158.920 116.058 1.00 118.02 ? 210  TYR   A N    1 
ATOM   3114 C CA   . TYR   A 1 197 ? 181.996 160.005 117.035 1.00 113.86 ? 210  TYR   A CA   1 
ATOM   3115 C C    . TYR   A 1 197 ? 183.351 160.121 117.717 1.00 117.42 ? 210  TYR   A C    1 
ATOM   3116 O O    . TYR   A 1 197 ? 183.932 159.107 118.099 1.00 123.58 ? 210  TYR   A O    1 
ATOM   3117 C CB   . TYR   A 1 197 ? 180.941 159.727 118.103 1.00 116.92 ? 210  TYR   A CB   1 
ATOM   3118 C CG   . TYR   A 1 197 ? 179.513 159.724 117.616 1.00 115.78 ? 210  TYR   A CG   1 
ATOM   3119 C CD1  . TYR   A 1 197 ? 178.967 158.569 117.037 1.00 120.23 ? 210  TYR   A CD1  1 
ATOM   3120 C CD2  . TYR   A 1 197 ? 178.723 160.872 117.771 1.00 115.96 ? 210  TYR   A CD2  1 
ATOM   3121 C CE1  . TYR   A 1 197 ? 177.633 158.563 116.596 1.00 121.78 ? 210  TYR   A CE1  1 
ATOM   3122 C CE2  . TYR   A 1 197 ? 177.391 160.874 117.328 1.00 117.07 ? 210  TYR   A CE2  1 
ATOM   3123 C CZ   . TYR   A 1 197 ? 176.845 159.719 116.739 1.00 122.97 ? 210  TYR   A CZ   1 
ATOM   3124 O OH   . TYR   A 1 197 ? 175.554 159.724 116.325 1.00 132.60 ? 210  TYR   A OH   1 
ATOM   3125 H H    . TYR   A 1 197 ? 182.346 158.024 116.383 1.00 121.18 ? 210  TYR   A H    1 
ATOM   3126 H HA   . TYR   A 1 197 ? 181.765 160.953 116.550 1.00 120.77 ? 210  TYR   A HA   1 
ATOM   3127 H HB2  . TYR   A 1 197 ? 181.153 158.762 118.564 1.00 121.01 ? 210  TYR   A HB2  1 
ATOM   3128 H HB3  . TYR   A 1 197 ? 181.036 160.482 118.883 1.00 120.85 ? 210  TYR   A HB3  1 
ATOM   3129 H HD1  . TYR   A 1 197 ? 179.574 157.683 116.930 1.00 121.95 ? 210  TYR   A HD1  1 
ATOM   3130 H HD2  . TYR   A 1 197 ? 179.137 161.752 118.241 1.00 120.88 ? 210  TYR   A HD2  1 
ATOM   3131 H HE1  . TYR   A 1 197 ? 177.219 157.673 116.146 1.00 122.09 ? 210  TYR   A HE1  1 
ATOM   3132 H HE2  . TYR   A 1 197 ? 176.775 161.754 117.447 1.00 120.88 ? 210  TYR   A HE2  1 
ATOM   3133 H HH   . TYR   A 1 197 ? 175.269 158.853 116.039 1.00 122.72 ? 210  TYR   A HH   1 
ATOM   3134 N N    . ALA   A 1 198 ? 183.825 161.345 117.933 1.00 126.32 ? 211  ALA   A N    1 
ATOM   3135 C CA   . ALA   A 1 198 ? 185.073 161.602 118.631 1.00 128.30 ? 211  ALA   A CA   1 
ATOM   3136 C C    . ALA   A 1 198 ? 184.903 162.632 119.742 1.00 127.31 ? 211  ALA   A C    1 
ATOM   3137 O O    . ALA   A 1 198 ? 184.395 163.729 119.521 1.00 133.71 ? 211  ALA   A O    1 
ATOM   3138 C CB   . ALA   A 1 198 ? 186.121 162.066 117.627 1.00 127.27 ? 211  ALA   A CB   1 
ATOM   3139 H H    . ALA   A 1 198 ? 183.316 162.141 117.578 1.00 127.49 ? 211  ALA   A H    1 
ATOM   3140 H HA   . ALA   A 1 198 ? 185.438 160.677 119.078 1.00 127.14 ? 211  ALA   A HA   1 
ATOM   3141 H HB1  . ALA   A 1 198 ? 187.066 162.247 118.139 1.00 126.62 ? 211  ALA   A HB1  1 
ATOM   3142 H HB2  . ALA   A 1 198 ? 186.268 161.302 116.863 1.00 126.96 ? 211  ALA   A HB2  1 
ATOM   3143 H HB3  . ALA   A 1 198 ? 185.787 162.991 117.156 1.00 127.15 ? 211  ALA   A HB3  1 
ATOM   3144 N N    . TYR   A 1 199 ? 185.415 162.310 120.922 1.00 109.06 ? 212  TYR   A N    1 
ATOM   3145 C CA   . TYR   A 1 199 ? 185.525 163.217 122.057 1.00 110.30 ? 212  TYR   A CA   1 
ATOM   3146 C C    . TYR   A 1 199 ? 186.983 163.283 122.470 1.00 112.33 ? 212  TYR   A C    1 
ATOM   3147 O O    . TYR   A 1 199 ? 187.682 162.280 122.361 1.00 120.39 ? 212  TYR   A O    1 
ATOM   3148 C CB   . TYR   A 1 199 ? 184.696 162.738 123.251 1.00 112.63 ? 212  TYR   A CB   1 
ATOM   3149 C CG   . TYR   A 1 199 ? 183.203 162.639 123.043 1.00 112.59 ? 212  TYR   A CG   1 
ATOM   3150 C CD1  . TYR   A 1 199 ? 182.668 161.667 122.185 1.00 112.67 ? 212  TYR   A CD1  1 
ATOM   3151 C CD2  . TYR   A 1 199 ? 182.340 163.489 123.752 1.00 118.11 ? 212  TYR   A CD2  1 
ATOM   3152 C CE1  . TYR   A 1 199 ? 181.282 161.591 121.985 1.00 117.12 ? 212  TYR   A CE1  1 
ATOM   3153 C CE2  . TYR   A 1 199 ? 180.951 163.404 123.570 1.00 121.75 ? 212  TYR   A CE2  1 
ATOM   3154 C CZ   . TYR   A 1 199 ? 180.421 162.458 122.678 1.00 123.42 ? 212  TYR   A CZ   1 
ATOM   3155 O OH   . TYR   A 1 199 ? 179.082 162.371 122.489 1.00 129.21 ? 212  TYR   A OH   1 
ATOM   3156 H H    . TYR   A 1 199 ? 185.849 161.403 121.013 1.00 117.36 ? 212  TYR   A H    1 
ATOM   3157 H HA   . TYR   A 1 199 ? 185.196 164.216 121.771 1.00 117.77 ? 212  TYR   A HA   1 
ATOM   3158 H HB2  . TYR   A 1 199 ? 185.069 161.767 123.575 1.00 116.51 ? 212  TYR   A HB2  1 
ATOM   3159 H HB3  . TYR   A 1 199 ? 184.879 163.432 124.072 1.00 117.83 ? 212  TYR   A HB3  1 
ATOM   3160 H HD1  . TYR   A 1 199 ? 183.316 160.974 121.670 1.00 117.02 ? 212  TYR   A HD1  1 
ATOM   3161 H HD2  . TYR   A 1 199 ? 182.740 164.200 124.460 1.00 117.93 ? 212  TYR   A HD2  1 
ATOM   3162 H HE1  . TYR   A 1 199 ? 180.874 160.870 121.292 1.00 117.72 ? 212  TYR   A HE1  1 
ATOM   3163 H HE2  . TYR   A 1 199 ? 180.284 164.055 124.116 1.00 118.13 ? 212  TYR   A HE2  1 
ATOM   3164 H HH   . TYR   A 1 199 ? 178.854 161.553 122.041 1.00 119.27 ? 212  TYR   A HH   1 
ATOM   3165 N N    . TYR   A 1 200 ? 187.444 164.411 122.993 1.00 115.25 ? 213  TYR   A N    1 
ATOM   3166 C CA   . TYR   A 1 200 ? 188.773 164.496 123.580 1.00 117.95 ? 213  TYR   A CA   1 
ATOM   3167 C C    . TYR   A 1 200 ? 188.823 165.382 124.817 1.00 120.35 ? 213  TYR   A C    1 
ATOM   3168 O O    . TYR   A 1 200 ? 187.895 166.136 125.085 1.00 126.83 ? 213  TYR   A O    1 
ATOM   3169 C CB   . TYR   A 1 200 ? 189.816 164.898 122.531 1.00 116.99 ? 213  TYR   A CB   1 
ATOM   3170 C CG   . TYR   A 1 200 ? 190.158 166.370 122.430 1.00 121.75 ? 213  TYR   A CG   1 
ATOM   3171 C CD1  . TYR   A 1 200 ? 189.153 167.349 122.489 1.00 125.79 ? 213  TYR   A CD1  1 
ATOM   3172 C CD2  . TYR   A 1 200 ? 191.500 166.759 122.270 1.00 121.54 ? 213  TYR   A CD2  1 
ATOM   3173 C CE1  . TYR   A 1 200 ? 189.488 168.710 122.402 1.00 129.13 ? 213  TYR   A CE1  1 
ATOM   3174 C CE2  . TYR   A 1 200 ? 191.837 168.119 122.159 1.00 129.14 ? 213  TYR   A CE2  1 
ATOM   3175 C CZ   . TYR   A 1 200 ? 190.827 169.099 122.221 1.00 132.66 ? 213  TYR   A CZ   1 
ATOM   3176 O OH   . TYR   A 1 200 ? 191.121 170.419 122.104 1.00 129.27 ? 213  TYR   A OH   1 
ATOM   3177 H H    . TYR   A 1 200 ? 186.813 165.189 123.116 1.00 122.85 ? 213  TYR   A H    1 
ATOM   3178 H HA   . TYR   A 1 200 ? 189.025 163.490 123.918 1.00 123.57 ? 213  TYR   A HA   1 
ATOM   3179 H HB2  . TYR   A 1 200 ? 190.733 164.368 122.786 1.00 122.62 ? 213  TYR   A HB2  1 
ATOM   3180 H HB3  . TYR   A 1 200 ? 189.507 164.538 121.550 1.00 122.74 ? 213  TYR   A HB3  1 
ATOM   3181 H HD1  . TYR   A 1 200 ? 188.117 167.067 122.604 1.00 123.08 ? 213  TYR   A HD1  1 
ATOM   3182 H HD2  . TYR   A 1 200 ? 192.278 166.011 122.219 1.00 122.26 ? 213  TYR   A HD2  1 
ATOM   3183 H HE1  . TYR   A 1 200 ? 188.717 169.466 122.449 1.00 123.47 ? 213  TYR   A HE1  1 
ATOM   3184 H HE2  . TYR   A 1 200 ? 192.867 168.414 122.027 1.00 124.21 ? 213  TYR   A HE2  1 
ATOM   3185 H HH   . TYR   A 1 200 ? 191.951 170.590 121.653 1.00 124.68 ? 213  TYR   A HH   1 
ATOM   3186 N N    . ALA   A 1 201 ? 189.901 165.297 125.580 1.00 117.68 ? 214  ALA   A N    1 
ATOM   3187 C CA   . ALA   A 1 201 ? 190.308 166.347 126.496 1.00 118.45 ? 214  ALA   A CA   1 
ATOM   3188 C C    . ALA   A 1 201 ? 191.824 166.423 126.549 1.00 119.15 ? 214  ALA   A C    1 
ATOM   3189 O O    . ALA   A 1 201 ? 192.489 165.400 126.675 1.00 127.46 ? 214  ALA   A O    1 
ATOM   3190 C CB   . ALA   A 1 201 ? 189.740 166.088 127.888 1.00 121.45 ? 214  ALA   A CB   1 
ATOM   3191 H H    . ALA   A 1 201 ? 190.576 164.577 125.365 1.00 121.75 ? 214  ALA   A H    1 
ATOM   3192 H HA   . ALA   A 1 201 ? 189.933 167.306 126.140 1.00 121.59 ? 214  ALA   A HA   1 
ATOM   3193 H HB1  . ALA   A 1 201 ? 190.232 166.738 128.611 1.00 121.97 ? 214  ALA   A HB1  1 
ATOM   3194 H HB2  . ALA   A 1 201 ? 188.677 166.330 127.894 1.00 122.25 ? 214  ALA   A HB2  1 
ATOM   3195 H HB3  . ALA   A 1 201 ? 189.897 165.050 128.180 1.00 122.33 ? 214  ALA   A HB3  1 
ATOM   3196 N N    . ASP   A 1 202 ? 192.371 167.629 126.493 1.00 135.19 ? 215  ASP   A N    1 
ATOM   3197 C CA   . ASP   A 1 202 ? 193.788 167.893 126.732 1.00 142.32 ? 215  ASP   A CA   1 
ATOM   3198 C C    . ASP   A 1 202 ? 194.058 168.387 128.159 1.00 145.27 ? 215  ASP   A C    1 
ATOM   3199 O O    . ASP   A 1 202 ? 195.212 168.420 128.575 1.00 147.21 ? 215  ASP   A O    1 
ATOM   3200 C CB   . ASP   A 1 202 ? 194.312 168.902 125.705 1.00 147.16 ? 215  ASP   A CB   1 
ATOM   3201 C CG   . ASP   A 1 202 ? 193.638 170.278 125.759 1.00 150.70 ? 215  ASP   A CG   1 
ATOM   3202 O OD1  . ASP   A 1 202 ? 192.560 170.413 126.379 1.00 150.45 ? 215  ASP   A OD1  1 
ATOM   3203 O OD2  . ASP   A 1 202 ? 194.203 171.225 125.171 1.00 151.22 ? 215  ASP   A OD2  1 
ATOM   3204 H H    . ASP   A 1 202 ? 191.783 168.437 126.347 1.00 141.06 ? 215  ASP   A H    1 
ATOM   3205 H HA   . ASP   A 1 202 ? 194.355 166.971 126.604 1.00 141.99 ? 215  ASP   A HA   1 
ATOM   3206 H HB2  . ASP   A 1 202 ? 195.385 169.020 125.855 1.00 143.43 ? 215  ASP   A HB2  1 
ATOM   3207 H HB3  . ASP   A 1 202 ? 194.165 168.480 124.711 1.00 142.01 ? 215  ASP   A HB3  1 
ATOM   3208 N N    . SER   A 1 203 ? 193.017 168.761 128.907 1.00 138.84 ? 216  SER   A N    1 
ATOM   3209 C CA   . SER   A 1 203 ? 193.074 169.220 130.297 1.00 136.00 ? 216  SER   A CA   1 
ATOM   3210 C C    . SER   A 1 203 ? 191.957 168.576 131.119 1.00 133.55 ? 216  SER   A C    1 
ATOM   3211 O O    . SER   A 1 203 ? 190.821 168.477 130.655 1.00 134.49 ? 216  SER   A O    1 
ATOM   3212 C CB   . SER   A 1 203 ? 192.969 170.744 130.341 1.00 131.83 ? 216  SER   A CB   1 
ATOM   3213 O OG   . SER   A 1 203 ? 192.963 171.199 131.681 1.00 139.02 ? 216  SER   A OG   1 
ATOM   3214 H H    . SER   A 1 203 ? 192.104 168.723 128.477 1.00 134.89 ? 216  SER   A H    1 
ATOM   3215 H HA   . SER   A 1 203 ? 194.030 168.933 130.736 1.00 135.21 ? 216  SER   A HA   1 
ATOM   3216 H HB2  . SER   A 1 203 ? 193.818 171.178 129.812 1.00 134.23 ? 216  SER   A HB2  1 
ATOM   3217 H HB3  . SER   A 1 203 ? 192.048 171.057 129.850 1.00 134.29 ? 216  SER   A HB3  1 
ATOM   3218 H HG   . SER   A 1 203 ? 192.891 172.156 131.667 1.00 135.89 ? 216  SER   A HG   1 
ATOM   3219 N N    . GLY   A 1 204 ? 192.264 168.128 132.336 1.00 127.56 ? 217  GLY   A N    1 
ATOM   3220 C CA   . GLY   A 1 204 ? 191.372 167.262 133.110 1.00 128.05 ? 217  GLY   A CA   1 
ATOM   3221 C C    . GLY   A 1 204 ? 191.226 165.871 132.489 1.00 130.53 ? 217  GLY   A C    1 
ATOM   3222 O O    . GLY   A 1 204 ? 191.961 165.508 131.573 1.00 134.19 ? 217  GLY   A O    1 
ATOM   3223 H H    . GLY   A 1 204 ? 193.204 168.273 132.676 1.00 129.69 ? 217  GLY   A H    1 
ATOM   3224 H HA2  . GLY   A 1 204 ? 191.761 167.148 134.122 1.00 129.46 ? 217  GLY   A HA2  1 
ATOM   3225 H HA3  . GLY   A 1 204 ? 190.385 167.721 133.176 1.00 129.61 ? 217  GLY   A HA3  1 
ATOM   3226 N N    . MET   A 1 205 ? 190.289 165.074 132.999 1.00 124.50 ? 218  MET   A N    1 
ATOM   3227 C CA   . MET   A 1 205 ? 190.039 163.701 132.540 1.00 125.54 ? 218  MET   A CA   1 
ATOM   3228 C C    . MET   A 1 205 ? 188.741 163.499 131.748 1.00 122.11 ? 218  MET   A C    1 
ATOM   3229 O O    . MET   A 1 205 ? 188.780 162.772 130.759 1.00 122.21 ? 218  MET   A O    1 
ATOM   3230 C CB   . MET   A 1 205 ? 190.086 162.736 133.726 1.00 127.86 ? 218  MET   A CB   1 
ATOM   3231 C CG   . MET   A 1 205 ? 191.519 162.437 134.151 1.00 132.55 ? 218  MET   A CG   1 
ATOM   3232 S SD   . MET   A 1 205 ? 191.601 161.453 135.658 1.00 140.80 ? 218  MET   A SD   1 
ATOM   3233 C CE   . MET   A 1 205 ? 193.359 161.037 135.645 1.00 130.29 ? 218  MET   A CE   1 
ATOM   3234 H H    . MET   A 1 205 ? 189.739 165.427 133.769 1.00 126.28 ? 218  MET   A H    1 
ATOM   3235 H HA   . MET   A 1 205 ? 190.836 163.400 131.859 1.00 126.69 ? 218  MET   A HA   1 
ATOM   3236 H HB2  . MET   A 1 205 ? 189.539 163.149 134.573 1.00 125.93 ? 218  MET   A HB2  1 
ATOM   3237 H HB3  . MET   A 1 205 ? 189.617 161.794 133.442 1.00 126.81 ? 218  MET   A HB3  1 
ATOM   3238 H HG2  . MET   A 1 205 ? 192.016 161.895 133.347 1.00 127.26 ? 218  MET   A HG2  1 
ATOM   3239 H HG3  . MET   A 1 205 ? 192.050 163.374 134.320 1.00 127.50 ? 218  MET   A HG3  1 
ATOM   3240 H HE1  . MET   A 1 205 ? 193.600 160.451 136.533 1.00 127.54 ? 218  MET   A HE1  1 
ATOM   3241 H HE2  . MET   A 1 205 ? 193.954 161.950 135.645 1.00 127.30 ? 218  MET   A HE2  1 
ATOM   3242 H HE3  . MET   A 1 205 ? 193.589 160.449 134.757 1.00 126.13 ? 218  MET   A HE3  1 
ATOM   3243 N N    . PRO   A 1 206 ? 187.584 164.068 132.124 1.00 116.37 ? 219  PRO   A N    1 
ATOM   3244 C CA   . PRO   A 1 206 ? 186.362 163.888 131.355 1.00 119.75 ? 219  PRO   A CA   1 
ATOM   3245 C C    . PRO   A 1 206 ? 186.500 164.513 129.971 1.00 119.04 ? 219  PRO   A C    1 
ATOM   3246 O O    . PRO   A 1 206 ? 186.892 165.672 129.858 1.00 120.71 ? 219  PRO   A O    1 
ATOM   3247 C CB   . PRO   A 1 206 ? 185.254 164.565 132.155 1.00 124.47 ? 219  PRO   A CB   1 
ATOM   3248 C CG   . PRO   A 1 206 ? 185.827 164.662 133.561 1.00 125.45 ? 219  PRO   A CG   1 
ATOM   3249 C CD   . PRO   A 1 206 ? 187.314 164.845 133.313 1.00 117.85 ? 219  PRO   A CD   1 
ATOM   3250 H HA   . PRO   A 1 206 ? 186.148 162.822 131.273 1.00 119.53 ? 219  PRO   A HA   1 
ATOM   3251 H HB2  . PRO   A 1 206 ? 185.068 165.571 131.779 1.00 118.92 ? 219  PRO   A HB2  1 
ATOM   3252 H HB3  . PRO   A 1 206 ? 184.335 163.979 132.136 1.00 120.77 ? 219  PRO   A HB3  1 
ATOM   3253 H HG2  . PRO   A 1 206 ? 185.411 165.506 134.110 1.00 120.43 ? 219  PRO   A HG2  1 
ATOM   3254 H HG3  . PRO   A 1 206 ? 185.658 163.725 134.093 1.00 120.49 ? 219  PRO   A HG3  1 
ATOM   3255 H HD2  . PRO   A 1 206 ? 187.526 165.896 133.115 1.00 119.14 ? 219  PRO   A HD2  1 
ATOM   3256 H HD3  . PRO   A 1 206 ? 187.874 164.494 134.179 1.00 119.19 ? 219  PRO   A HD3  1 
ATOM   3257 N N    . THR   A 1 207 ? 186.192 163.778 128.909 1.00 116.00 ? 220  THR   A N    1 
ATOM   3258 C CA   . THR   A 1 207 ? 186.324 164.289 127.540 1.00 114.79 ? 220  THR   A CA   1 
ATOM   3259 C C    . THR   A 1 207 ? 185.108 165.097 127.101 1.00 119.65 ? 220  THR   A C    1 
ATOM   3260 O O    . THR   A 1 207 ? 184.038 165.037 127.704 1.00 124.61 ? 220  THR   A O    1 
ATOM   3261 C CB   . THR   A 1 207 ? 186.618 163.174 126.544 1.00 118.03 ? 220  THR   A CB   1 
ATOM   3262 O OG1  . THR   A 1 207 ? 185.526 162.319 126.479 1.00 122.92 ? 220  THR   A OG1  1 
ATOM   3263 C CG2  . THR   A 1 207 ? 187.843 162.351 126.915 1.00 119.23 ? 220  THR   A CG2  1 
ATOM   3264 H H    . THR   A 1 207 ? 185.829 162.844 129.041 1.00 118.41 ? 220  THR   A H    1 
ATOM   3265 H HA   . THR   A 1 207 ? 187.179 164.964 127.497 1.00 118.12 ? 220  THR   A HA   1 
ATOM   3266 H HB   . THR   A 1 207 ? 186.780 163.609 125.558 1.00 119.06 ? 220  THR   A HB   1 
ATOM   3267 H HG1  . THR   A 1 207 ? 185.822 161.457 126.178 1.00 119.00 ? 220  THR   A HG1  1 
ATOM   3268 H HG21 . THR   A 1 207 ? 188.067 161.649 126.112 1.00 119.12 ? 220  THR   A HG21 1 
ATOM   3269 H HG22 . THR   A 1 207 ? 187.674 161.803 127.842 1.00 118.70 ? 220  THR   A HG22 1 
ATOM   3270 H HG23 . THR   A 1 207 ? 188.695 163.018 127.044 1.00 118.21 ? 220  THR   A HG23 1 
ATOM   3271 N N    . THR   A 1 208 ? 185.267 165.880 126.039 1.00 123.69 ? 221  THR   A N    1 
ATOM   3272 C CA   . THR   A 1 208 ? 184.228 166.709 125.425 1.00 118.90 ? 221  THR   A CA   1 
ATOM   3273 C C    . THR   A 1 208 ? 184.201 166.501 123.915 1.00 119.31 ? 221  THR   A C    1 
ATOM   3274 O O    . THR   A 1 208 ? 185.192 166.081 123.324 1.00 129.05 ? 221  THR   A O    1 
ATOM   3275 C CB   . THR   A 1 208 ? 184.418 168.179 125.801 1.00 122.52 ? 221  THR   A CB   1 
ATOM   3276 O OG1  . THR   A 1 208 ? 183.348 168.921 125.278 1.00 127.73 ? 221  THR   A OG1  1 
ATOM   3277 C CG2  . THR   A 1 208 ? 185.704 168.804 125.268 1.00 122.13 ? 221  THR   A CG2  1 
ATOM   3278 H H    . THR   A 1 208 ? 186.176 165.908 125.600 1.00 122.57 ? 221  THR   A H    1 
ATOM   3279 H HA   . THR   A 1 208 ? 183.256 166.403 125.811 1.00 121.88 ? 221  THR   A HA   1 
ATOM   3280 H HB   . THR   A 1 208 ? 184.410 168.270 126.887 1.00 122.53 ? 221  THR   A HB   1 
ATOM   3281 H HG1  . THR   A 1 208 ? 183.456 169.827 125.578 1.00 122.77 ? 221  THR   A HG1  1 
ATOM   3282 H HG21 . THR   A 1 208 ? 185.747 169.855 125.553 1.00 123.24 ? 221  THR   A HG21 1 
ATOM   3283 H HG22 . THR   A 1 208 ? 185.751 168.726 124.182 1.00 121.14 ? 221  THR   A HG22 1 
ATOM   3284 H HG23 . THR   A 1 208 ? 186.566 168.299 125.705 1.00 122.12 ? 221  THR   A HG23 1 
ATOM   3285 N N    . PHE   A 1 209 ? 183.058 166.724 123.280 1.00 113.92 ? 222  PHE   A N    1 
ATOM   3286 C CA   . PHE   A 1 209 ? 182.817 166.382 121.880 1.00 121.59 ? 222  PHE   A CA   1 
ATOM   3287 C C    . PHE   A 1 209 ? 183.681 167.199 120.909 1.00 125.66 ? 222  PHE   A C    1 
ATOM   3288 O O    . PHE   A 1 209 ? 183.655 168.428 120.949 1.00 129.13 ? 222  PHE   A O    1 
ATOM   3289 C CB   . PHE   A 1 209 ? 181.330 166.618 121.624 1.00 120.93 ? 222  PHE   A CB   1 
ATOM   3290 C CG   . PHE   A 1 209 ? 180.883 166.388 120.204 1.00 118.43 ? 222  PHE   A CG   1 
ATOM   3291 C CD1  . PHE   A 1 209 ? 180.469 165.111 119.798 1.00 118.20 ? 222  PHE   A CD1  1 
ATOM   3292 C CD2  . PHE   A 1 209 ? 180.824 167.463 119.304 1.00 116.86 ? 222  PHE   A CD2  1 
ATOM   3293 C CE1  . PHE   A 1 209 ? 179.982 164.916 118.498 1.00 120.06 ? 222  PHE   A CE1  1 
ATOM   3294 C CE2  . PHE   A 1 209 ? 180.336 167.266 118.004 1.00 122.68 ? 222  PHE   A CE2  1 
ATOM   3295 C CZ   . PHE   A 1 209 ? 179.907 165.993 117.603 1.00 122.14 ? 222  PHE   A CZ   1 
ATOM   3296 H H    . PHE   A 1 209 ? 182.303 167.150 123.799 1.00 120.09 ? 222  PHE   A H    1 
ATOM   3297 H HA   . PHE   A 1 209 ? 183.028 165.324 121.723 1.00 120.98 ? 222  PHE   A HA   1 
ATOM   3298 H HB2  . PHE   A 1 209 ? 180.752 165.966 122.279 1.00 121.21 ? 222  PHE   A HB2  1 
ATOM   3299 H HB3  . PHE   A 1 209 ? 181.085 167.645 121.896 1.00 121.15 ? 222  PHE   A HB3  1 
ATOM   3300 H HD1  . PHE   A 1 209 ? 180.510 164.282 120.490 1.00 120.36 ? 222  PHE   A HD1  1 
ATOM   3301 H HD2  . PHE   A 1 209 ? 181.136 168.449 119.617 1.00 119.80 ? 222  PHE   A HD2  1 
ATOM   3302 H HE1  . PHE   A 1 209 ? 179.652 163.934 118.190 1.00 120.90 ? 222  PHE   A HE1  1 
ATOM   3303 H HE2  . PHE   A 1 209 ? 180.279 168.097 117.317 1.00 121.31 ? 222  PHE   A HE2  1 
ATOM   3304 H HZ   . PHE   A 1 209 ? 179.515 165.843 116.608 1.00 120.99 ? 222  PHE   A HZ   1 
ATOM   3305 N N    . LEU   A 1 210 ? 184.411 166.538 120.004 1.00 129.07 ? 223  LEU   A N    1 
ATOM   3306 C CA   . LEU   A 1 210 ? 185.085 167.184 118.876 1.00 126.79 ? 223  LEU   A CA   1 
ATOM   3307 C C    . LEU   A 1 210 ? 184.175 167.249 117.652 1.00 129.80 ? 223  LEU   A C    1 
ATOM   3308 O O    . LEU   A 1 210 ? 183.876 168.332 117.156 1.00 132.19 ? 223  LEU   A O    1 
ATOM   3309 C CB   . LEU   A 1 210 ? 186.362 166.427 118.479 1.00 124.03 ? 223  LEU   A CB   1 
ATOM   3310 C CG   . LEU   A 1 210 ? 187.581 166.635 119.373 1.00 132.28 ? 223  LEU   A CG   1 
ATOM   3311 C CD1  . LEU   A 1 210 ? 188.720 165.767 118.849 1.00 133.21 ? 223  LEU   A CD1  1 
ATOM   3312 C CD2  . LEU   A 1 210 ? 188.045 168.086 119.325 1.00 129.69 ? 223  LEU   A CD2  1 
ATOM   3313 H H    . LEU   A 1 210 ? 184.374 165.528 120.007 1.00 128.07 ? 223  LEU   A H    1 
ATOM   3314 H HA   . LEU   A 1 210 ? 185.344 168.211 119.133 1.00 128.21 ? 223  LEU   A HA   1 
ATOM   3315 H HB2  . LEU   A 1 210 ? 186.145 165.361 118.416 1.00 127.48 ? 223  LEU   A HB2  1 
ATOM   3316 H HB3  . LEU   A 1 210 ? 186.649 166.769 117.485 1.00 127.25 ? 223  LEU   A HB3  1 
ATOM   3317 H HG   . LEU   A 1 210 ? 187.348 166.346 120.398 1.00 129.09 ? 223  LEU   A HG   1 
ATOM   3318 H HD11 . LEU   A 1 210 ? 188.431 164.716 118.882 1.00 128.59 ? 223  LEU   A HD11 1 
ATOM   3319 H HD12 . LEU   A 1 210 ? 189.605 165.907 119.469 1.00 129.71 ? 223  LEU   A HD12 1 
ATOM   3320 H HD13 . LEU   A 1 210 ? 188.961 166.044 117.823 1.00 128.49 ? 223  LEU   A HD13 1 
ATOM   3321 H HD21 . LEU   A 1 210 ? 187.348 168.723 119.870 1.00 128.70 ? 223  LEU   A HD21 1 
ATOM   3322 H HD22 . LEU   A 1 210 ? 189.031 168.177 119.782 1.00 128.67 ? 223  LEU   A HD22 1 
ATOM   3323 H HD23 . LEU   A 1 210 ? 188.115 168.420 118.290 1.00 128.19 ? 223  LEU   A HD23 1 
ATOM   3324 N N    . PHE   A 1 211 ? 183.772 166.088 117.138 1.00 127.64 ? 224  PHE   A N    1 
ATOM   3325 C CA   . PHE   A 1 211 ? 183.026 165.960 115.891 1.00 126.50 ? 224  PHE   A CA   1 
ATOM   3326 C C    . PHE   A 1 211 ? 182.327 164.605 115.800 1.00 127.11 ? 224  PHE   A C    1 
ATOM   3327 O O    . PHE   A 1 211 ? 182.649 163.663 116.522 1.00 133.72 ? 224  PHE   A O    1 
ATOM   3328 C CB   . PHE   A 1 211 ? 183.959 166.147 114.683 1.00 125.09 ? 224  PHE   A CB   1 
ATOM   3329 C CG   . PHE   A 1 211 ? 184.848 164.962 114.358 1.00 124.93 ? 224  PHE   A CG   1 
ATOM   3330 C CD1  . PHE   A 1 211 ? 186.074 164.802 115.016 1.00 127.25 ? 224  PHE   A CD1  1 
ATOM   3331 C CD2  . PHE   A 1 211 ? 184.463 164.024 113.385 1.00 127.39 ? 224  PHE   A CD2  1 
ATOM   3332 C CE1  . PHE   A 1 211 ? 186.900 163.707 114.724 1.00 128.10 ? 224  PHE   A CE1  1 
ATOM   3333 C CE2  . PHE   A 1 211 ? 185.296 162.935 113.080 1.00 130.42 ? 224  PHE   A CE2  1 
ATOM   3334 C CZ   . PHE   A 1 211 ? 186.515 162.776 113.751 1.00 127.52 ? 224  PHE   A CZ   1 
ATOM   3335 H H    . PHE   A 1 211 ? 184.006 165.235 117.625 1.00 127.29 ? 224  PHE   A H    1 
ATOM   3336 H HA   . PHE   A 1 211 ? 182.262 166.736 115.859 1.00 127.41 ? 224  PHE   A HA   1 
ATOM   3337 H HB2  . PHE   A 1 211 ? 183.343 166.355 113.809 1.00 127.83 ? 224  PHE   A HB2  1 
ATOM   3338 H HB3  . PHE   A 1 211 ? 184.584 167.027 114.836 1.00 127.36 ? 224  PHE   A HB3  1 
ATOM   3339 H HD1  . PHE   A 1 211 ? 186.392 165.527 115.750 1.00 127.56 ? 224  PHE   A HD1  1 
ATOM   3340 H HD2  . PHE   A 1 211 ? 183.533 164.151 112.849 1.00 127.85 ? 224  PHE   A HD2  1 
ATOM   3341 H HE1  . PHE   A 1 211 ? 187.835 163.583 115.250 1.00 128.04 ? 224  PHE   A HE1  1 
ATOM   3342 H HE2  . PHE   A 1 211 ? 185.006 162.224 112.321 1.00 128.18 ? 224  PHE   A HE2  1 
ATOM   3343 H HZ   . PHE   A 1 211 ? 187.165 161.948 113.506 1.00 127.49 ? 224  PHE   A HZ   1 
ATOM   3344 N N    . SER   A 1 212 ? 181.407 164.493 114.851 1.00 124.54 ? 225  SER   A N    1 
ATOM   3345 C CA   . SER   A 1 212 ? 180.855 163.223 114.397 1.00 126.00 ? 225  SER   A CA   1 
ATOM   3346 C C    . SER   A 1 212 ? 180.817 163.195 112.878 1.00 126.23 ? 225  SER   A C    1 
ATOM   3347 O O    . SER   A 1 212 ? 180.874 164.236 112.220 1.00 128.63 ? 225  SER   A O    1 
ATOM   3348 C CB   . SER   A 1 212 ? 179.465 162.983 114.981 1.00 126.82 ? 225  SER   A CB   1 
ATOM   3349 O OG   . SER   A 1 212 ? 178.549 163.951 114.502 1.00 124.35 ? 225  SER   A OG   1 
ATOM   3350 H H    . SER   A 1 212 ? 181.187 165.304 114.290 1.00 126.10 ? 225  SER   A H    1 
ATOM   3351 H HA   . SER   A 1 212 ? 181.508 162.416 114.727 1.00 126.16 ? 225  SER   A HA   1 
ATOM   3352 H HB2  . SER   A 1 212 ? 179.123 161.988 114.695 1.00 125.98 ? 225  SER   A HB2  1 
ATOM   3353 H HB3  . SER   A 1 212 ? 179.520 163.033 116.068 1.00 125.84 ? 225  SER   A HB3  1 
ATOM   3354 H HG   . SER   A 1 212 ? 177.689 163.775 114.889 1.00 125.56 ? 225  SER   A HG   1 
ATOM   3355 N N    . LEU   A 1 213 ? 180.769 162.001 112.306 1.00 127.57 ? 226  LEU   A N    1 
ATOM   3356 C CA   . LEU   A 1 213 ? 181.020 161.789 110.891 1.00 125.20 ? 226  LEU   A CA   1 
ATOM   3357 C C    . LEU   A 1 213 ? 180.235 160.587 110.386 1.00 125.35 ? 226  LEU   A C    1 
ATOM   3358 O O    . LEU   A 1 213 ? 180.477 159.463 110.814 1.00 129.99 ? 226  LEU   A O    1 
ATOM   3359 C CB   . LEU   A 1 213 ? 182.533 161.598 110.740 1.00 121.57 ? 226  LEU   A CB   1 
ATOM   3360 C CG   . LEU   A 1 213 ? 182.973 161.155 109.347 1.00 123.82 ? 226  LEU   A CG   1 
ATOM   3361 C CD1  . LEU   A 1 213 ? 182.558 162.175 108.296 1.00 126.96 ? 226  LEU   A CD1  1 
ATOM   3362 C CD2  . LEU   A 1 213 ? 184.487 161.012 109.331 1.00 122.50 ? 226  LEU   A CD2  1 
ATOM   3363 H H    . LEU   A 1 213 ? 180.757 161.190 112.907 1.00 125.94 ? 226  LEU   A H    1 
ATOM   3364 H HA   . LEU   A 1 213 ? 180.713 162.666 110.321 1.00 124.92 ? 226  LEU   A HA   1 
ATOM   3365 H HB2  . LEU   A 1 213 ? 183.028 162.538 110.982 1.00 125.07 ? 226  LEU   A HB2  1 
ATOM   3366 H HB3  . LEU   A 1 213 ? 182.867 160.845 111.454 1.00 124.53 ? 226  LEU   A HB3  1 
ATOM   3367 H HG   . LEU   A 1 213 ? 182.535 160.187 109.101 1.00 125.71 ? 226  LEU   A HG   1 
ATOM   3368 H HD11 . LEU   A 1 213 ? 181.478 162.150 108.151 1.00 125.88 ? 226  LEU   A HD11 1 
ATOM   3369 H HD12 . LEU   A 1 213 ? 182.860 163.176 108.603 1.00 125.46 ? 226  LEU   A HD12 1 
ATOM   3370 H HD13 . LEU   A 1 213 ? 183.034 161.927 107.348 1.00 126.63 ? 226  LEU   A HD13 1 
ATOM   3371 H HD21 . LEU   A 1 213 ? 184.799 160.662 108.347 1.00 125.49 ? 226  LEU   A HD21 1 
ATOM   3372 H HD22 . LEU   A 1 213 ? 184.961 161.970 109.549 1.00 125.47 ? 226  LEU   A HD22 1 
ATOM   3373 H HD23 . LEU   A 1 213 ? 184.796 160.279 110.076 1.00 125.11 ? 226  LEU   A HD23 1 
ATOM   3374 N N    . TYR   A 1 214 ? 179.297 160.801 109.471 1.00 123.65 ? 227  TYR   A N    1 
ATOM   3375 C CA   . TYR   A 1 214 ? 178.618 159.694 108.816 1.00 122.16 ? 227  TYR   A CA   1 
ATOM   3376 C C    . TYR   A 1 214 ? 179.560 158.980 107.852 1.00 126.92 ? 227  TYR   A C    1 
ATOM   3377 O O    . TYR   A 1 214 ? 180.076 159.598 106.925 1.00 133.98 ? 227  TYR   A O    1 
ATOM   3378 C CB   . TYR   A 1 214 ? 177.383 160.195 108.080 1.00 128.98 ? 227  TYR   A CB   1 
ATOM   3379 C CG   . TYR   A 1 214 ? 176.689 159.083 107.332 1.00 128.08 ? 227  TYR   A CG   1 
ATOM   3380 C CD1  . TYR   A 1 214 ? 175.928 158.139 108.039 1.00 125.96 ? 227  TYR   A CD1  1 
ATOM   3381 C CD2  . TYR   A 1 214 ? 176.845 158.964 105.941 1.00 128.83 ? 227  TYR   A CD2  1 
ATOM   3382 C CE1  . TYR   A 1 214 ? 175.298 157.088 107.353 1.00 128.55 ? 227  TYR   A CE1  1 
ATOM   3383 C CE2  . TYR   A 1 214 ? 176.214 157.916 105.250 1.00 129.66 ? 227  TYR   A CE2  1 
ATOM   3384 C CZ   . TYR   A 1 214 ? 175.430 156.984 105.956 1.00 133.95 ? 227  TYR   A CZ   1 
ATOM   3385 O OH   . TYR   A 1 214 ? 174.803 155.981 105.294 1.00 140.56 ? 227  TYR   A OH   1 
ATOM   3386 H H    . TYR   A 1 214 ? 179.115 161.742 109.151 1.00 128.69 ? 227  TYR   A H    1 
ATOM   3387 H HA   . TYR   A 1 214 ? 178.285 158.981 109.570 1.00 128.27 ? 227  TYR   A HA   1 
ATOM   3388 H HB2  . TYR   A 1 214 ? 176.687 160.625 108.801 1.00 129.85 ? 227  TYR   A HB2  1 
ATOM   3389 H HB3  . TYR   A 1 214 ? 177.669 160.979 107.379 1.00 129.41 ? 227  TYR   A HB3  1 
ATOM   3390 H HD1  . TYR   A 1 214 ? 175.819 158.226 109.109 1.00 128.96 ? 227  TYR   A HD1  1 
ATOM   3391 H HD2  . TYR   A 1 214 ? 177.448 159.679 105.401 1.00 129.34 ? 227  TYR   A HD2  1 
ATOM   3392 H HE1  . TYR   A 1 214 ? 174.700 156.365 107.887 1.00 129.20 ? 227  TYR   A HE1  1 
ATOM   3393 H HE2  . TYR   A 1 214 ? 176.327 157.829 104.179 1.00 129.39 ? 227  TYR   A HE2  1 
ATOM   3394 H HH   . TYR   A 1 214 ? 174.889 156.080 104.343 1.00 130.04 ? 227  TYR   A HH   1 
ATOM   3395 N N    . LEU   A 1 215 ? 179.757 157.678 108.043 1.00 127.83 ? 228  LEU   A N    1 
ATOM   3396 C CA   . LEU   A 1 215 ? 180.511 156.825 107.127 1.00 128.34 ? 228  LEU   A CA   1 
ATOM   3397 C C    . LEU   A 1 215 ? 179.599 155.917 106.305 1.00 130.64 ? 228  LEU   A C    1 
ATOM   3398 O O    . LEU   A 1 215 ? 179.926 155.568 105.175 1.00 131.00 ? 228  LEU   A O    1 
ATOM   3399 C CB   . LEU   A 1 215 ? 181.485 155.961 107.933 1.00 123.32 ? 228  LEU   A CB   1 
ATOM   3400 C CG   . LEU   A 1 215 ? 182.520 156.753 108.738 1.00 125.00 ? 228  LEU   A CG   1 
ATOM   3401 C CD1  . LEU   A 1 215 ? 183.374 155.761 109.510 1.00 123.78 ? 228  LEU   A CD1  1 
ATOM   3402 C CD2  . LEU   A 1 215 ? 183.444 157.579 107.851 1.00 124.30 ? 228  LEU   A CD2  1 
ATOM   3403 H H    . LEU   A 1 215 ? 179.317 157.241 108.840 1.00 127.69 ? 228  LEU   A H    1 
ATOM   3404 H HA   . LEU   A 1 215 ? 181.079 157.430 106.420 1.00 127.76 ? 228  LEU   A HA   1 
ATOM   3405 H HB2  . LEU   A 1 215 ? 180.912 155.339 108.621 1.00 126.84 ? 228  LEU   A HB2  1 
ATOM   3406 H HB3  . LEU   A 1 215 ? 182.012 155.302 107.244 1.00 127.22 ? 228  LEU   A HB3  1 
ATOM   3407 H HG   . LEU   A 1 215 ? 182.024 157.410 109.452 1.00 127.56 ? 228  LEU   A HG   1 
ATOM   3408 H HD11 . LEU   A 1 215 ? 184.114 156.302 110.100 1.00 127.25 ? 228  LEU   A HD11 1 
ATOM   3409 H HD12 . LEU   A 1 215 ? 182.744 155.180 110.183 1.00 126.61 ? 228  LEU   A HD12 1 
ATOM   3410 H HD13 . LEU   A 1 215 ? 183.883 155.089 108.818 1.00 127.44 ? 228  LEU   A HD13 1 
ATOM   3411 H HD21 . LEU   A 1 215 ? 182.875 158.371 107.365 1.00 127.01 ? 228  LEU   A HD21 1 
ATOM   3412 H HD22 . LEU   A 1 215 ? 184.223 158.040 108.459 1.00 127.00 ? 228  LEU   A HD22 1 
ATOM   3413 H HD23 . LEU   A 1 215 ? 183.906 156.945 107.094 1.00 127.85 ? 228  LEU   A HD23 1 
ATOM   3414 N N    . GLY   A 1 216 ? 178.471 155.493 106.877 1.00 139.61 ? 229  GLY   A N    1 
ATOM   3415 C CA   . GLY   A 1 216 ? 177.557 154.532 106.256 1.00 142.29 ? 229  GLY   A CA   1 
ATOM   3416 C C    . GLY   A 1 216 ? 178.070 153.091 106.225 1.00 143.10 ? 229  GLY   A C    1 
ATOM   3417 O O    . GLY   A 1 216 ? 177.360 152.198 105.768 1.00 144.17 ? 229  GLY   A O    1 
ATOM   3418 H H    . GLY   A 1 216 ? 178.258 155.819 107.808 1.00 139.40 ? 229  GLY   A H    1 
ATOM   3419 H HA2  . GLY   A 1 216 ? 176.616 154.535 106.807 1.00 140.09 ? 229  GLY   A HA2  1 
ATOM   3420 H HA3  . GLY   A 1 216 ? 177.356 154.840 105.230 1.00 140.39 ? 229  GLY   A HA3  1 
ATOM   3421 N N    . THR   A 1 217 ? 179.275 152.842 106.730 1.00 139.77 ? 230  THR   A N    1 
ATOM   3422 C CA   . THR   A 1 217 ? 179.922 151.525 106.764 1.00 143.26 ? 230  THR   A CA   1 
ATOM   3423 C C    . THR   A 1 217 ? 180.507 151.249 108.137 1.00 138.33 ? 230  THR   A C    1 
ATOM   3424 O O    . THR   A 1 217 ? 181.072 152.139 108.767 1.00 136.89 ? 230  THR   A O    1 
ATOM   3425 C CB   . THR   A 1 217 ? 181.045 151.412 105.728 1.00 145.45 ? 230  THR   A CB   1 
ATOM   3426 O OG1  . THR   A 1 217 ? 182.029 152.403 105.936 1.00 145.98 ? 230  THR   A OG1  1 
ATOM   3427 C CG2  . THR   A 1 217 ? 180.531 151.551 104.299 1.00 142.50 ? 230  THR   A CG2  1 
ATOM   3428 H H    . THR   A 1 217 ? 179.806 153.623 107.087 1.00 139.21 ? 230  THR   A H    1 
ATOM   3429 H HA   . THR   A 1 217 ? 179.189 150.748 106.550 1.00 141.00 ? 230  THR   A HA   1 
ATOM   3430 H HB   . THR   A 1 217 ? 181.511 150.432 105.828 1.00 140.94 ? 230  THR   A HB   1 
ATOM   3431 H HG1  . THR   A 1 217 ? 182.291 152.370 106.859 1.00 140.78 ? 230  THR   A HG1  1 
ATOM   3432 H HG21 . THR   A 1 217 ? 181.348 151.370 103.600 1.00 140.21 ? 230  THR   A HG21 1 
ATOM   3433 H HG22 . THR   A 1 217 ? 179.745 150.818 104.119 1.00 140.28 ? 230  THR   A HG22 1 
ATOM   3434 H HG23 . THR   A 1 217 ? 180.136 152.554 104.132 1.00 140.45 ? 230  THR   A HG23 1 
ATOM   3435 N N    . LEU   A 1 218 ? 180.425 150.005 108.588 1.00 125.13 ? 231  LEU   A N    1 
ATOM   3436 C CA   . LEU   A 1 218 ? 180.972 149.572 109.865 1.00 124.22 ? 231  LEU   A CA   1 
ATOM   3437 C C    . LEU   A 1 218 ? 182.509 149.624 109.856 1.00 128.54 ? 231  LEU   A C    1 
ATOM   3438 O O    . LEU   A 1 218 ? 183.144 148.914 109.079 1.00 125.16 ? 231  LEU   A O    1 
ATOM   3439 C CB   . LEU   A 1 218 ? 180.431 148.152 110.099 1.00 125.34 ? 231  LEU   A CB   1 
ATOM   3440 C CG   . LEU   A 1 218 ? 180.756 147.563 111.473 1.00 130.06 ? 231  LEU   A CG   1 
ATOM   3441 C CD1  . LEU   A 1 218 ? 179.915 148.222 112.562 1.00 130.06 ? 231  LEU   A CD1  1 
ATOM   3442 C CD2  . LEU   A 1 218 ? 180.452 146.068 111.481 1.00 130.86 ? 231  LEU   A CD2  1 
ATOM   3443 H H    . LEU   A 1 218 ? 179.963 149.313 108.016 1.00 127.97 ? 231  LEU   A H    1 
ATOM   3444 H HA   . LEU   A 1 218 ? 180.602 150.233 110.648 1.00 126.92 ? 231  LEU   A HA   1 
ATOM   3445 H HB2  . LEU   A 1 218 ? 179.348 148.153 109.974 1.00 127.42 ? 231  LEU   A HB2  1 
ATOM   3446 H HB3  . LEU   A 1 218 ? 180.849 147.497 109.334 1.00 127.30 ? 231  LEU   A HB3  1 
ATOM   3447 H HG   . LEU   A 1 218 ? 181.815 147.699 111.694 1.00 128.07 ? 231  LEU   A HG   1 
ATOM   3448 H HD11 . LEU   A 1 218 ? 180.118 149.293 112.598 1.00 127.48 ? 231  LEU   A HD11 1 
ATOM   3449 H HD12 . LEU   A 1 218 ? 178.854 148.066 112.363 1.00 127.76 ? 231  LEU   A HD12 1 
ATOM   3450 H HD13 . LEU   A 1 218 ? 180.166 147.789 113.530 1.00 127.95 ? 231  LEU   A HD13 1 
ATOM   3451 H HD21 . LEU   A 1 218 ? 181.066 145.565 110.734 1.00 127.55 ? 231  LEU   A HD21 1 
ATOM   3452 H HD22 . LEU   A 1 218 ? 180.684 145.651 112.461 1.00 128.25 ? 231  LEU   A HD22 1 
ATOM   3453 H HD23 . LEU   A 1 218 ? 179.399 145.897 111.256 1.00 128.30 ? 231  LEU   A HD23 1 
ATOM   3454 N N    . LEU   A 1 219 ? 183.121 150.429 110.726 1.00 129.21 ? 232  LEU   A N    1 
ATOM   3455 C CA   . LEU   A 1 219 ? 184.557 150.354 111.010 1.00 122.21 ? 232  LEU   A CA   1 
ATOM   3456 C C    . LEU   A 1 219 ? 184.851 149.055 111.754 1.00 123.47 ? 232  LEU   A C    1 
ATOM   3457 O O    . LEU   A 1 219 ? 184.031 148.614 112.554 1.00 132.07 ? 232  LEU   A O    1 
ATOM   3458 C CB   . LEU   A 1 219 ? 184.991 151.534 111.884 1.00 118.89 ? 232  LEU   A CB   1 
ATOM   3459 C CG   . LEU   A 1 219 ? 184.836 152.906 111.219 1.00 119.69 ? 232  LEU   A CG   1 
ATOM   3460 C CD1  . LEU   A 1 219 ? 184.937 153.983 112.287 1.00 125.94 ? 232  LEU   A CD1  1 
ATOM   3461 C CD2  . LEU   A 1 219 ? 185.934 153.129 110.185 1.00 116.01 ? 232  LEU   A CD2  1 
ATOM   3462 H H    . LEU   A 1 219 ? 182.550 150.972 111.357 1.00 124.66 ? 232  LEU   A H    1 
ATOM   3463 H HA   . LEU   A 1 219 ? 185.124 150.359 110.079 1.00 123.38 ? 232  LEU   A HA   1 
ATOM   3464 H HB2  . LEU   A 1 219 ? 184.401 151.516 112.800 1.00 123.54 ? 232  LEU   A HB2  1 
ATOM   3465 H HB3  . LEU   A 1 219 ? 186.033 151.400 112.172 1.00 122.72 ? 232  LEU   A HB3  1 
ATOM   3466 H HG   . LEU   A 1 219 ? 183.862 152.988 110.737 1.00 123.18 ? 232  LEU   A HG   1 
ATOM   3467 H HD11 . LEU   A 1 219 ? 184.875 154.971 111.831 1.00 123.74 ? 232  LEU   A HD11 1 
ATOM   3468 H HD12 . LEU   A 1 219 ? 184.110 153.867 112.988 1.00 124.32 ? 232  LEU   A HD12 1 
ATOM   3469 H HD13 . LEU   A 1 219 ? 185.881 153.897 112.825 1.00 123.92 ? 232  LEU   A HD13 1 
ATOM   3470 H HD21 . LEU   A 1 219 ? 185.837 152.405 109.376 1.00 123.08 ? 232  LEU   A HD21 1 
ATOM   3471 H HD22 . LEU   A 1 219 ? 185.849 154.132 109.767 1.00 123.64 ? 232  LEU   A HD22 1 
ATOM   3472 H HD23 . LEU   A 1 219 ? 186.913 153.026 110.653 1.00 122.86 ? 232  LEU   A HD23 1 
ATOM   3473 N N    . SER   A 1 220 ? 186.011 148.445 111.542 1.00 127.38 ? 233  SER   A N    1 
ATOM   3474 C CA   . SER   A 1 220 ? 186.302 147.129 112.119 1.00 129.81 ? 233  SER   A CA   1 
ATOM   3475 C C    . SER   A 1 220 ? 187.715 146.965 112.653 1.00 126.72 ? 233  SER   A C    1 
ATOM   3476 O O    . SER   A 1 220 ? 187.924 146.084 113.480 1.00 130.48 ? 233  SER   A O    1 
ATOM   3477 C CB   . SER   A 1 220 ? 185.976 146.025 111.118 1.00 133.51 ? 233  SER   A CB   1 
ATOM   3478 O OG   . SER   A 1 220 ? 186.802 146.123 109.977 1.00 137.07 ? 233  SER   A OG   1 
ATOM   3479 H H    . SER   A 1 220 ? 186.667 148.852 110.891 1.00 129.74 ? 233  SER   A H    1 
ATOM   3480 H HA   . SER   A 1 220 ? 185.653 146.964 112.980 1.00 129.78 ? 233  SER   A HA   1 
ATOM   3481 H HB2  . SER   A 1 220 ? 186.128 145.056 111.594 1.00 130.14 ? 233  SER   A HB2  1 
ATOM   3482 H HB3  . SER   A 1 220 ? 184.930 146.106 110.822 1.00 130.40 ? 233  SER   A HB3  1 
ATOM   3483 H HG   . SER   A 1 220 ? 186.595 145.382 109.403 1.00 130.53 ? 233  SER   A HG   1 
ATOM   3484 N N    . HIS   A 1 221 ? 188.664 147.833 112.311 1.00 124.12 ? 234  HIS   A N    1 
ATOM   3485 C CA   . HIS   A 1 221 ? 190.023 147.763 112.845 1.00 123.78 ? 234  HIS   A CA   1 
ATOM   3486 C C    . HIS   A 1 221 ? 190.575 149.134 113.183 1.00 129.02 ? 234  HIS   A C    1 
ATOM   3487 O O    . HIS   A 1 221 ? 190.216 150.134 112.569 1.00 135.76 ? 234  HIS   A O    1 
ATOM   3488 C CB   . HIS   A 1 221 ? 190.948 147.080 111.841 1.00 122.60 ? 234  HIS   A CB   1 
ATOM   3489 C CG   . HIS   A 1 221 ? 190.657 145.622 111.658 1.00 124.69 ? 234  HIS   A CG   1 
ATOM   3490 N ND1  . HIS   A 1 221 ? 191.091 144.603 112.500 1.00 126.58 ? 234  HIS   A ND1  1 
ATOM   3491 C CD2  . HIS   A 1 221 ? 189.923 145.082 110.651 1.00 127.90 ? 234  HIS   A CD2  1 
ATOM   3492 C CE1  . HIS   A 1 221 ? 190.601 143.467 111.985 1.00 130.16 ? 234  HIS   A CE1  1 
ATOM   3493 N NE2  . HIS   A 1 221 ? 189.902 143.726 110.870 1.00 134.98 ? 234  HIS   A NE2  1 
ATOM   3494 H H    . HIS   A 1 221 ? 188.448 148.576 111.663 1.00 128.54 ? 234  HIS   A H    1 
ATOM   3495 H HA   . HIS   A 1 221 ? 190.033 147.175 113.762 1.00 127.88 ? 234  HIS   A HA   1 
ATOM   3496 H HB2  . HIS   A 1 221 ? 190.875 147.587 110.879 1.00 127.83 ? 234  HIS   A HB2  1 
ATOM   3497 H HB3  . HIS   A 1 221 ? 191.977 147.171 112.189 1.00 127.23 ? 234  HIS   A HB3  1 
ATOM   3498 H HD2  . HIS   A 1 221 ? 189.446 145.623 109.846 1.00 127.89 ? 234  HIS   A HD2  1 
ATOM   3499 H HE1  . HIS   A 1 221 ? 190.748 142.483 112.404 1.00 128.16 ? 234  HIS   A HE1  1 
ATOM   3500 H HE2  . HIS   A 1 221 ? 189.439 143.032 110.300 1.00 129.42 ? 234  HIS   A HE2  1 
ATOM   3501 N N    . TYR   A 1 222 ? 191.518 149.170 114.109 1.00 115.10 ? 235  TYR   A N    1 
ATOM   3502 C CA   . TYR   A 1 222 ? 192.340 150.334 114.378 1.00 110.03 ? 235  TYR   A CA   1 
ATOM   3503 C C    . TYR   A 1 222 ? 193.778 149.914 114.619 1.00 114.66 ? 235  TYR   A C    1 
ATOM   3504 O O    . TYR   A 1 222 ? 194.065 148.758 114.934 1.00 130.26 ? 235  TYR   A O    1 
ATOM   3505 C CB   . TYR   A 1 222 ? 191.794 151.122 115.565 1.00 109.84 ? 235  TYR   A CB   1 
ATOM   3506 C CG   . TYR   A 1 222 ? 192.011 150.448 116.898 1.00 110.15 ? 235  TYR   A CG   1 
ATOM   3507 C CD1  . TYR   A 1 222 ? 191.082 149.515 117.377 1.00 119.42 ? 235  TYR   A CD1  1 
ATOM   3508 C CD2  . TYR   A 1 222 ? 193.157 150.745 117.649 1.00 114.39 ? 235  TYR   A CD2  1 
ATOM   3509 C CE1  . TYR   A 1 222 ? 191.286 148.890 118.616 1.00 116.77 ? 235  TYR   A CE1  1 
ATOM   3510 C CE2  . TYR   A 1 222 ? 193.375 150.111 118.881 1.00 120.63 ? 235  TYR   A CE2  1 
ATOM   3511 C CZ   . TYR   A 1 222 ? 192.436 149.183 119.368 1.00 115.59 ? 235  TYR   A CZ   1 
ATOM   3512 O OH   . TYR   A 1 222 ? 192.652 148.532 120.536 1.00 118.85 ? 235  TYR   A OH   1 
ATOM   3513 H H    . TYR   A 1 222 ? 191.753 148.317 114.597 1.00 119.51 ? 235  TYR   A H    1 
ATOM   3514 H HA   . TYR   A 1 222 ? 192.330 150.984 113.504 1.00 118.64 ? 235  TYR   A HA   1 
ATOM   3515 H HB2  . TYR   A 1 222 ? 192.291 152.092 115.589 1.00 118.06 ? 235  TYR   A HB2  1 
ATOM   3516 H HB3  . TYR   A 1 222 ? 190.730 151.307 115.417 1.00 118.98 ? 235  TYR   A HB3  1 
ATOM   3517 H HD1  . TYR   A 1 222 ? 190.216 149.263 116.782 1.00 119.69 ? 235  TYR   A HD1  1 
ATOM   3518 H HD2  . TYR   A 1 222 ? 193.881 151.454 117.276 1.00 117.44 ? 235  TYR   A HD2  1 
ATOM   3519 H HE1  . TYR   A 1 222 ? 190.574 148.171 118.993 1.00 118.96 ? 235  TYR   A HE1  1 
ATOM   3520 H HE2  . TYR   A 1 222 ? 194.271 150.337 119.441 1.00 119.64 ? 235  TYR   A HE2  1 
ATOM   3521 H HH   . TYR   A 1 222 ? 193.463 148.833 120.953 1.00 119.16 ? 235  TYR   A HH   1 
ATOM   3522 N N    . TYR   A 1 223 ? 194.694 150.856 114.462 1.00 115.97 ? 236  TYR   A N    1 
ATOM   3523 C CA   . TYR   A 1 223 ? 196.110 150.608 114.643 1.00 114.86 ? 236  TYR   A CA   1 
ATOM   3524 C C    . TYR   A 1 223 ? 196.832 151.888 115.049 1.00 120.15 ? 236  TYR   A C    1 
ATOM   3525 O O    . TYR   A 1 223 ? 196.554 152.956 114.512 1.00 134.74 ? 236  TYR   A O    1 
ATOM   3526 C CB   . TYR   A 1 223 ? 196.644 150.032 113.335 1.00 113.27 ? 236  TYR   A CB   1 
ATOM   3527 C CG   . TYR   A 1 223 ? 198.111 149.726 113.381 1.00 108.43 ? 236  TYR   A CG   1 
ATOM   3528 C CD1  . TYR   A 1 223 ? 198.585 148.762 114.280 1.00 112.33 ? 236  TYR   A CD1  1 
ATOM   3529 C CD2  . TYR   A 1 223 ? 198.995 150.418 112.546 1.00 115.05 ? 236  TYR   A CD2  1 
ATOM   3530 C CE1  . TYR   A 1 223 ? 199.956 148.483 114.336 1.00 118.15 ? 236  TYR   A CE1  1 
ATOM   3531 C CE2  . TYR   A 1 223 ? 200.370 150.161 112.622 1.00 120.87 ? 236  TYR   A CE2  1 
ATOM   3532 C CZ   . TYR   A 1 223 ? 200.848 149.187 113.514 1.00 120.58 ? 236  TYR   A CZ   1 
ATOM   3533 O OH   . TYR   A 1 223 ? 202.166 148.901 113.567 1.00 130.50 ? 236  TYR   A OH   1 
ATOM   3534 H H    . TYR   A 1 223 ? 194.403 151.775 114.163 1.00 120.98 ? 236  TYR   A H    1 
ATOM   3535 H HA   . TYR   A 1 223 ? 196.249 149.875 115.436 1.00 120.48 ? 236  TYR   A HA   1 
ATOM   3536 H HB2  . TYR   A 1 223 ? 196.115 149.107 113.105 1.00 120.42 ? 236  TYR   A HB2  1 
ATOM   3537 H HB3  . TYR   A 1 223 ? 196.444 150.735 112.527 1.00 120.39 ? 236  TYR   A HB3  1 
ATOM   3538 H HD1  . TYR   A 1 223 ? 197.898 148.228 114.921 1.00 119.97 ? 236  TYR   A HD1  1 
ATOM   3539 H HD2  . TYR   A 1 223 ? 198.612 151.137 111.837 1.00 120.64 ? 236  TYR   A HD2  1 
ATOM   3540 H HE1  . TYR   A 1 223 ? 200.336 147.730 115.011 1.00 121.26 ? 236  TYR   A HE1  1 
ATOM   3541 H HE2  . TYR   A 1 223 ? 201.064 150.693 111.987 1.00 122.10 ? 236  TYR   A HE2  1 
ATOM   3542 H HH   . TYR   A 1 223 ? 202.305 148.021 113.922 1.00 122.91 ? 236  TYR   A HH   1 
ATOM   3543 N N    . VAL   A 1 224 ? 197.763 151.803 115.993 1.00 106.73 ? 237  VAL   A N    1 
ATOM   3544 C CA   . VAL   A 1 224 ? 198.537 152.954 116.472 1.00 107.41 ? 237  VAL   A CA   1 
ATOM   3545 C C    . VAL   A 1 224 ? 199.883 152.935 115.770 1.00 114.42 ? 237  VAL   A C    1 
ATOM   3546 O O    . VAL   A 1 224 ? 200.659 152.002 115.948 1.00 115.73 ? 237  VAL   A O    1 
ATOM   3547 C CB   . VAL   A 1 224 ? 198.679 152.902 117.998 1.00 105.18 ? 237  VAL   A CB   1 
ATOM   3548 C CG1  . VAL   A 1 224 ? 199.572 154.020 118.533 1.00 116.76 ? 237  VAL   A CG1  1 
ATOM   3549 C CG2  . VAL   A 1 224 ? 197.303 153.061 118.643 1.00 108.67 ? 237  VAL   A CG2  1 
ATOM   3550 H H    . VAL   A 1 224 ? 197.993 150.892 116.364 1.00 112.76 ? 237  VAL   A H    1 
ATOM   3551 H HA   . VAL   A 1 224 ? 198.030 153.885 116.218 1.00 112.95 ? 237  VAL   A HA   1 
ATOM   3552 H HB   . VAL   A 1 224 ? 199.099 151.941 118.295 1.00 112.40 ? 237  VAL   A HB   1 
ATOM   3553 H HG11 . VAL   A 1 224 ? 200.589 153.898 118.162 1.00 114.37 ? 237  VAL   A HG11 1 
ATOM   3554 H HG12 . VAL   A 1 224 ? 199.598 153.978 119.622 1.00 113.83 ? 237  VAL   A HG12 1 
ATOM   3555 H HG13 . VAL   A 1 224 ? 199.177 154.987 118.222 1.00 114.13 ? 237  VAL   A HG13 1 
ATOM   3556 H HG21 . VAL   A 1 224 ? 196.639 152.255 118.330 1.00 112.63 ? 237  VAL   A HG21 1 
ATOM   3557 H HG22 . VAL   A 1 224 ? 197.399 153.021 119.728 1.00 114.14 ? 237  VAL   A HG22 1 
ATOM   3558 H HG23 . VAL   A 1 224 ? 196.866 154.019 118.361 1.00 112.06 ? 237  VAL   A HG23 1 
ATOM   3559 N N    . LEU   A 1 225 ? 200.163 153.934 114.939 1.00 116.44 ? 238  LEU   A N    1 
ATOM   3560 C CA   . LEU   A 1 225 ? 201.323 153.910 114.056 1.00 114.89 ? 238  LEU   A CA   1 
ATOM   3561 C C    . LEU   A 1 225 ? 202.631 153.995 114.847 1.00 114.01 ? 238  LEU   A C    1 
ATOM   3562 O O    . LEU   A 1 225 ? 202.758 154.867 115.708 1.00 108.32 ? 238  LEU   A O    1 
ATOM   3563 C CB   . LEU   A 1 225 ? 201.279 155.069 113.047 1.00 119.37 ? 238  LEU   A CB   1 
ATOM   3564 C CG   . LEU   A 1 225 ? 200.030 155.171 112.164 1.00 120.43 ? 238  LEU   A CG   1 
ATOM   3565 C CD1  . LEU   A 1 225 ? 200.283 156.166 111.039 1.00 120.97 ? 238  LEU   A CD1  1 
ATOM   3566 C CD2  . LEU   A 1 225 ? 199.683 153.839 111.522 1.00 121.38 ? 238  LEU   A CD2  1 
ATOM   3567 H H    . LEU   A 1 225 ? 199.545 154.732 114.913 1.00 119.10 ? 238  LEU   A H    1 
ATOM   3568 H HA   . LEU   A 1 225 ? 201.299 152.973 113.501 1.00 118.88 ? 238  LEU   A HA   1 
ATOM   3569 H HB2  . LEU   A 1 225 ? 201.384 156.009 113.589 1.00 119.62 ? 238  LEU   A HB2  1 
ATOM   3570 H HB3  . LEU   A 1 225 ? 202.148 154.965 112.398 1.00 119.34 ? 238  LEU   A HB3  1 
ATOM   3571 H HG   . LEU   A 1 225 ? 199.184 155.511 112.762 1.00 119.11 ? 238  LEU   A HG   1 
ATOM   3572 H HD11 . LEU   A 1 225 ? 200.539 157.142 111.453 1.00 120.11 ? 238  LEU   A HD11 1 
ATOM   3573 H HD12 . LEU   A 1 225 ? 201.099 155.821 110.405 1.00 119.52 ? 238  LEU   A HD12 1 
ATOM   3574 H HD13 . LEU   A 1 225 ? 199.383 156.277 110.434 1.00 120.17 ? 238  LEU   A HD13 1 
ATOM   3575 H HD21 . LEU   A 1 225 ? 199.319 153.167 112.299 1.00 119.43 ? 238  LEU   A HD21 1 
ATOM   3576 H HD22 . LEU   A 1 225 ? 198.893 153.969 110.782 1.00 119.28 ? 238  LEU   A HD22 1 
ATOM   3577 H HD23 . LEU   A 1 225 ? 200.566 153.414 111.044 1.00 119.74 ? 238  LEU   A HD23 1 
ATOM   3578 N N    . PRO   A 1 226 ? 203.645 153.183 114.524 1.00 118.82 ? 239  PRO   A N    1 
ATOM   3579 C CA   . PRO   A 1 226 ? 204.996 153.402 114.994 1.00 121.95 ? 239  PRO   A CA   1 
ATOM   3580 C C    . PRO   A 1 226 ? 205.483 154.818 114.714 1.00 126.65 ? 239  PRO   A C    1 
ATOM   3581 O O    . PRO   A 1 226 ? 205.082 155.457 113.739 1.00 136.65 ? 239  PRO   A O    1 
ATOM   3582 C CB   . PRO   A 1 226 ? 205.855 152.359 114.282 1.00 116.84 ? 239  PRO   A CB   1 
ATOM   3583 C CG   . PRO   A 1 226 ? 204.868 151.225 114.059 1.00 118.66 ? 239  PRO   A CG   1 
ATOM   3584 C CD   . PRO   A 1 226 ? 203.577 151.969 113.747 1.00 118.94 ? 239  PRO   A CD   1 
ATOM   3585 H HA   . PRO   A 1 226 ? 205.013 153.217 116.068 1.00 125.26 ? 239  PRO   A HA   1 
ATOM   3586 H HB2  . PRO   A 1 226 ? 206.194 152.737 113.318 1.00 123.38 ? 239  PRO   A HB2  1 
ATOM   3587 H HB3  . PRO   A 1 226 ? 206.702 152.044 114.892 1.00 125.52 ? 239  PRO   A HB3  1 
ATOM   3588 H HG2  . PRO   A 1 226 ? 205.173 150.569 113.244 1.00 124.94 ? 239  PRO   A HG2  1 
ATOM   3589 H HG3  . PRO   A 1 226 ? 204.750 150.656 114.981 1.00 125.27 ? 239  PRO   A HG3  1 
ATOM   3590 H HD2  . PRO   A 1 226 ? 203.535 152.214 112.686 1.00 124.33 ? 239  PRO   A HD2  1 
ATOM   3591 H HD3  . PRO   A 1 226 ? 202.717 151.366 114.039 1.00 124.93 ? 239  PRO   A HD3  1 
ATOM   3592 N N    . LEU   A 1 227 ? 206.381 155.314 115.551 1.00 130.26 ? 240  LEU   A N    1 
ATOM   3593 C CA   . LEU   A 1 227 ? 207.005 156.620 115.399 1.00 125.69 ? 240  LEU   A CA   1 
ATOM   3594 C C    . LEU   A 1 227 ? 208.513 156.421 115.415 1.00 129.38 ? 240  LEU   A C    1 
ATOM   3595 O O    . LEU   A 1 227 ? 209.038 155.787 116.322 1.00 137.98 ? 240  LEU   A O    1 
ATOM   3596 C CB   . LEU   A 1 227 ? 206.456 157.517 116.514 1.00 127.21 ? 240  LEU   A CB   1 
ATOM   3597 C CG   . LEU   A 1 227 ? 206.867 158.994 116.456 1.00 132.45 ? 240  LEU   A CG   1 
ATOM   3598 C CD1  . LEU   A 1 227 ? 205.908 159.808 117.319 1.00 130.04 ? 240  LEU   A CD1  1 
ATOM   3599 C CD2  . LEU   A 1 227 ? 208.271 159.249 116.993 1.00 137.49 ? 240  LEU   A CD2  1 
ATOM   3600 H H    . LEU   A 1 227 ? 206.690 154.729 116.315 1.00 133.93 ? 240  LEU   A H    1 
ATOM   3601 H HA   . LEU   A 1 227 ? 206.730 157.061 114.441 1.00 133.12 ? 240  LEU   A HA   1 
ATOM   3602 H HB2  . LEU   A 1 227 ? 205.369 157.473 116.448 1.00 132.53 ? 240  LEU   A HB2  1 
ATOM   3603 H HB3  . LEU   A 1 227 ? 206.741 157.100 117.480 1.00 133.61 ? 240  LEU   A HB3  1 
ATOM   3604 H HG   . LEU   A 1 227 ? 206.804 159.351 115.428 1.00 134.20 ? 240  LEU   A HG   1 
ATOM   3605 H HD11 . LEU   A 1 227 ? 204.892 159.712 116.935 1.00 133.02 ? 240  LEU   A HD11 1 
ATOM   3606 H HD12 . LEU   A 1 227 ? 205.942 159.460 118.351 1.00 133.53 ? 240  LEU   A HD12 1 
ATOM   3607 H HD13 . LEU   A 1 227 ? 206.185 160.861 117.285 1.00 133.45 ? 240  LEU   A HD13 1 
ATOM   3608 H HD21 . LEU   A 1 227 ? 209.024 158.808 116.340 1.00 134.60 ? 240  LEU   A HD21 1 
ATOM   3609 H HD22 . LEU   A 1 227 ? 208.448 160.324 117.029 1.00 135.06 ? 240  LEU   A HD22 1 
ATOM   3610 H HD23 . LEU   A 1 227 ? 208.371 158.842 117.999 1.00 134.35 ? 240  LEU   A HD23 1 
ATOM   3611 N N    . THR   A 1 228 ? 209.229 156.933 114.421 1.00 149.80 ? 241  THR   A N    1 
ATOM   3612 C CA   . THR   A 1 228 ? 210.691 156.778 114.350 1.00 153.55 ? 241  THR   A CA   1 
ATOM   3613 C C    . THR   A 1 228 ? 211.389 158.076 114.702 1.00 151.48 ? 241  THR   A C    1 
ATOM   3614 O O    . THR   A 1 228 ? 210.969 159.153 114.281 1.00 155.39 ? 241  THR   A O    1 
ATOM   3615 C CB   . THR   A 1 228 ? 211.178 156.226 113.014 1.00 155.00 ? 241  THR   A CB   1 
ATOM   3616 O OG1  . THR   A 1 228 ? 210.836 157.089 111.958 1.00 159.31 ? 241  THR   A OG1  1 
ATOM   3617 C CG2  . THR   A 1 228 ? 210.577 154.855 112.731 1.00 152.81 ? 241  THR   A CG2  1 
ATOM   3618 H H    . THR   A 1 228 ? 208.755 157.482 113.719 1.00 152.08 ? 241  THR   A H    1 
ATOM   3619 H HA   . THR   A 1 228 ? 211.002 156.047 115.097 1.00 152.46 ? 241  THR   A HA   1 
ATOM   3620 H HB   . THR   A 1 228 ? 212.263 156.127 113.050 1.00 152.72 ? 241  THR   A HB   1 
ATOM   3621 H HG1  . THR   A 1 228 ? 209.877 157.140 111.941 1.00 153.08 ? 241  THR   A HG1  1 
ATOM   3622 H HG21 . THR   A 1 228 ? 211.039 154.438 111.836 1.00 152.86 ? 241  THR   A HG21 1 
ATOM   3623 H HG22 . THR   A 1 228 ? 210.782 154.184 113.565 1.00 152.39 ? 241  THR   A HG22 1 
ATOM   3624 H HG23 . THR   A 1 228 ? 209.499 154.923 112.585 1.00 152.28 ? 241  THR   A HG23 1 
ATOM   3625 N N    . CYS   A 1 229 ? 212.418 157.992 115.536 1.00 161.62 ? 242  CYS   A N    1 
ATOM   3626 C CA   . CYS   A 1 229 ? 213.045 159.168 116.117 1.00 163.94 ? 242  CYS   A CA   1 
ATOM   3627 C C    . CYS   A 1 229 ? 214.513 158.912 116.449 1.00 166.43 ? 242  CYS   A C    1 
ATOM   3628 O O    . CYS   A 1 229 ? 214.844 157.835 116.945 1.00 170.76 ? 242  CYS   A O    1 
ATOM   3629 C CB   . CYS   A 1 229 ? 212.272 159.485 117.395 1.00 170.99 ? 242  CYS   A CB   1 
ATOM   3630 S SG   . CYS   A 1 229 ? 212.503 161.141 118.040 1.00 191.38 ? 242  CYS   A SG   1 
ATOM   3631 H H    . CYS   A 1 229 ? 212.721 157.086 115.862 1.00 167.22 ? 242  CYS   A H    1 
ATOM   3632 H HA   . CYS   A 1 229 ? 212.974 160.011 115.429 1.00 167.53 ? 242  CYS   A HA   1 
ATOM   3633 H HB2  . CYS   A 1 229 ? 211.206 159.355 117.212 1.00 168.38 ? 242  CYS   A HB2  1 
ATOM   3634 H HB3  . CYS   A 1 229 ? 212.558 158.775 118.172 1.00 168.54 ? 242  CYS   A HB3  1 
ATOM   3635 N N    . ASN   A 1 230 ? 215.378 159.911 116.283 1.00 158.50 ? 243  ASN   A N    1 
ATOM   3636 C CA   . ASN   A 1 230 ? 216.750 159.835 116.797 1.00 158.71 ? 243  ASN   A CA   1 
ATOM   3637 C C    . ASN   A 1 230 ? 216.838 160.144 118.306 1.00 160.49 ? 243  ASN   A C    1 
ATOM   3638 O O    . ASN   A 1 230 ? 217.875 159.910 118.920 1.00 160.89 ? 243  ASN   A O    1 
ATOM   3639 C CB   . ASN   A 1 230 ? 217.650 160.757 115.963 1.00 158.63 ? 243  ASN   A CB   1 
ATOM   3640 C CG   . ASN   A 1 230 ? 217.868 160.283 114.535 1.00 162.22 ? 243  ASN   A CG   1 
ATOM   3641 O OD1  . ASN   A 1 230 ? 217.398 159.244 114.088 1.00 163.83 ? 243  ASN   A OD1  1 
ATOM   3642 N ND2  . ASN   A 1 230 ? 218.614 161.037 113.765 1.00 161.50 ? 243  ASN   A ND2  1 
ATOM   3643 H H    . ASN   A 1 230 ? 215.074 160.760 115.829 1.00 160.04 ? 243  ASN   A H    1 
ATOM   3644 H HA   . ASN   A 1 230 ? 217.119 158.817 116.676 1.00 160.04 ? 243  ASN   A HA   1 
ATOM   3645 H HB2  . ASN   A 1 230 ? 217.233 161.764 115.944 1.00 159.95 ? 243  ASN   A HB2  1 
ATOM   3646 H HB3  . ASN   A 1 230 ? 218.631 160.812 116.436 1.00 159.81 ? 243  ASN   A HB3  1 
ATOM   3647 H HD21 . ASN   A 1 230 ? 219.021 161.887 114.128 1.00 160.36 ? 243  ASN   A HD21 1 
ATOM   3648 H HD22 . ASN   A 1 230 ? 218.814 160.723 112.826 1.00 160.29 ? 243  ASN   A HD22 1 
ATOM   3649 N N    . ALA   A 1 231 ? 215.760 160.656 118.903 1.00 161.94 ? 244  ALA   A N    1 
ATOM   3650 C CA   . ALA   A 1 231 ? 215.588 160.877 120.340 1.00 161.61 ? 244  ALA   A CA   1 
ATOM   3651 C C    . ALA   A 1 231 ? 214.621 159.837 120.946 1.00 157.09 ? 244  ALA   A C    1 
ATOM   3652 O O    . ALA   A 1 231 ? 214.355 158.815 120.318 1.00 157.38 ? 244  ALA   A O    1 
ATOM   3653 C CB   . ALA   A 1 231 ? 215.104 162.320 120.504 1.00 159.43 ? 244  ALA   A CB   1 
ATOM   3654 H H    . ALA   A 1 231 ? 214.948 160.820 118.324 1.00 159.14 ? 244  ALA   A H    1 
ATOM   3655 H HA   . ALA   A 1 231 ? 216.547 160.786 120.851 1.00 158.84 ? 244  ALA   A HA   1 
ATOM   3656 H HB1  . ALA   A 1 231 ? 215.082 162.597 121.558 1.00 158.21 ? 244  ALA   A HB1  1 
ATOM   3657 H HB2  . ALA   A 1 231 ? 215.795 162.990 119.993 1.00 158.67 ? 244  ALA   A HB2  1 
ATOM   3658 H HB3  . ALA   A 1 231 ? 214.104 162.435 120.085 1.00 158.80 ? 244  ALA   A HB3  1 
ATOM   3659 N N    . ILE   A 1 232 ? 214.060 160.090 122.131 1.00 139.35 ? 245  ILE   A N    1 
ATOM   3660 C CA   . ILE   A 1 232 ? 213.091 159.224 122.818 1.00 140.82 ? 245  ILE   A CA   1 
ATOM   3661 C C    . ILE   A 1 232 ? 213.669 157.829 123.102 1.00 142.97 ? 245  ILE   A C    1 
ATOM   3662 O O    . ILE   A 1 232 ? 213.166 156.820 122.608 1.00 144.43 ? 245  ILE   A O    1 
ATOM   3663 C CB   . ILE   A 1 232 ? 211.713 159.178 122.109 1.00 140.13 ? 245  ILE   A CB   1 
ATOM   3664 C CG1  . ILE   A 1 232 ? 211.217 160.555 121.634 1.00 139.74 ? 245  ILE   A CG1  1 
ATOM   3665 C CG2  . ILE   A 1 232 ? 210.665 158.576 123.063 1.00 142.62 ? 245  ILE   A CG2  1 
ATOM   3666 C CD1  . ILE   A 1 232 ? 209.868 160.511 120.905 1.00 141.42 ? 245  ILE   A CD1  1 
ATOM   3667 H H    . ILE   A 1 232 ? 214.346 160.919 122.632 1.00 143.24 ? 245  ILE   A H    1 
ATOM   3668 H HA   . ILE   A 1 232 ? 212.920 159.682 123.792 1.00 143.47 ? 245  ILE   A HA   1 
ATOM   3669 H HB   . ILE   A 1 232 ? 211.795 158.541 121.229 1.00 143.41 ? 245  ILE   A HB   1 
ATOM   3670 H HG12 . ILE   A 1 232 ? 211.129 161.210 122.501 1.00 142.91 ? 245  ILE   A HG12 1 
ATOM   3671 H HG13 . ILE   A 1 232 ? 211.944 160.989 120.947 1.00 143.97 ? 245  ILE   A HG13 1 
ATOM   3672 H HG21 . ILE   A 1 232 ? 211.016 157.641 123.500 1.00 143.45 ? 245  ILE   A HG21 1 
ATOM   3673 H HG22 . ILE   A 1 232 ? 209.746 158.357 122.521 1.00 143.66 ? 245  ILE   A HG22 1 
ATOM   3674 H HG23 . ILE   A 1 232 ? 210.453 159.278 123.870 1.00 143.05 ? 245  ILE   A HG23 1 
ATOM   3675 H HD11 . ILE   A 1 232 ? 209.656 161.485 120.464 1.00 143.54 ? 245  ILE   A HD11 1 
ATOM   3676 H HD12 . ILE   A 1 232 ? 209.898 159.766 120.111 1.00 143.89 ? 245  ILE   A HD12 1 
ATOM   3677 H HD13 . ILE   A 1 232 ? 209.062 160.276 121.601 1.00 143.00 ? 245  ILE   A HD13 1 
ATOM   3678 N N    . SER   A 1 233 ? 214.759 157.749 123.865 1.00 159.94 ? 246  SER   A N    1 
ATOM   3679 C CA   . SER   A 1 233 ? 215.263 156.469 124.384 1.00 157.25 ? 246  SER   A CA   1 
ATOM   3680 C C    . SER   A 1 233 ? 216.238 156.644 125.554 1.00 158.51 ? 246  SER   A C    1 
ATOM   3681 O O    . SER   A 1 233 ? 216.812 157.711 125.795 1.00 161.16 ? 246  SER   A O    1 
ATOM   3682 C CB   . SER   A 1 233 ? 215.913 155.625 123.275 1.00 161.09 ? 246  SER   A CB   1 
ATOM   3683 O OG   . SER   A 1 233 ? 217.094 156.223 122.800 1.00 165.22 ? 246  SER   A OG   1 
ATOM   3684 H H    . SER   A 1 233 ? 215.102 158.601 124.285 1.00 160.54 ? 246  SER   A H    1 
ATOM   3685 H HA   . SER   A 1 233 ? 214.411 155.905 124.763 1.00 159.15 ? 246  SER   A HA   1 
ATOM   3686 H HB2  . SER   A 1 233 ? 216.152 154.636 123.665 1.00 160.09 ? 246  SER   A HB2  1 
ATOM   3687 H HB3  . SER   A 1 233 ? 215.222 155.495 122.442 1.00 160.33 ? 246  SER   A HB3  1 
ATOM   3688 H HG   . SER   A 1 233 ? 217.003 156.327 121.850 1.00 160.98 ? 246  SER   A HG   1 
ATOM   3689 N N    . SER   A 1 234 ? 216.457 155.566 126.304 1.00 162.62 ? 247  SER   A N    1 
ATOM   3690 C CA   . SER   A 1 234 ? 217.262 155.585 127.529 1.00 166.20 ? 247  SER   A CA   1 
ATOM   3691 C C    . SER   A 1 234 ? 218.730 155.960 127.312 1.00 165.96 ? 247  SER   A C    1 
ATOM   3692 O O    . SER   A 1 234 ? 219.359 156.497 128.223 1.00 166.75 ? 247  SER   A O    1 
ATOM   3693 C CB   . SER   A 1 234 ? 217.172 154.223 128.216 1.00 163.83 ? 247  SER   A CB   1 
ATOM   3694 O OG   . SER   A 1 234 ? 217.658 153.212 127.350 1.00 161.83 ? 247  SER   A OG   1 
ATOM   3695 H H    . SER   A 1 234 ? 215.996 154.699 126.065 1.00 163.45 ? 247  SER   A H    1 
ATOM   3696 H HA   . SER   A 1 234 ? 216.839 156.328 128.206 1.00 164.27 ? 247  SER   A HA   1 
ATOM   3697 H HB2  . SER   A 1 234 ? 217.761 154.238 129.133 1.00 163.69 ? 247  SER   A HB2  1 
ATOM   3698 H HB3  . SER   A 1 234 ? 216.133 154.017 128.471 1.00 163.73 ? 247  SER   A HB3  1 
ATOM   3699 H HG   . SER   A 1 234 ? 217.590 152.370 127.806 1.00 163.71 ? 247  SER   A HG   1 
ATOM   3700 N N    . ASN   A 1 235 ? 219.285 155.747 126.116 1.00 169.73 ? 248  ASN   A N    1 
ATOM   3701 C CA   . ASN   A 1 235 ? 220.664 156.137 125.822 1.00 169.86 ? 248  ASN   A CA   1 
ATOM   3702 C C    . ASN   A 1 235 ? 220.829 157.624 125.451 1.00 168.00 ? 248  ASN   A C    1 
ATOM   3703 O O    . ASN   A 1 235 ? 221.963 158.066 125.263 1.00 168.00 ? 248  ASN   A O    1 
ATOM   3704 C CB   . ASN   A 1 235 ? 221.280 155.171 124.790 1.00 170.27 ? 248  ASN   A CB   1 
ATOM   3705 C CG   . ASN   A 1 235 ? 221.008 155.513 123.336 1.00 174.57 ? 248  ASN   A CG   1 
ATOM   3706 O OD1  . ASN   A 1 235 ? 220.172 154.913 122.676 1.00 176.15 ? 248  ASN   A OD1  1 
ATOM   3707 N ND2  . ASN   A 1 235 ? 221.722 156.466 122.785 1.00 172.77 ? 248  ASN   A ND2  1 
ATOM   3708 H H    . ASN   A 1 235 ? 218.742 155.276 125.406 1.00 169.05 ? 248  ASN   A H    1 
ATOM   3709 H HA   . ASN   A 1 235 ? 221.240 156.002 126.738 1.00 169.17 ? 248  ASN   A HA   1 
ATOM   3710 H HB2  . ASN   A 1 235 ? 222.362 155.174 124.928 1.00 169.34 ? 248  ASN   A HB2  1 
ATOM   3711 H HB3  . ASN   A 1 235 ? 220.938 154.154 124.985 1.00 168.93 ? 248  ASN   A HB3  1 
ATOM   3712 H HD21 . ASN   A 1 235 ? 222.397 156.970 123.343 1.00 169.76 ? 248  ASN   A HD21 1 
ATOM   3713 H HD22 . ASN   A 1 235 ? 221.606 156.658 121.800 1.00 169.55 ? 248  ASN   A HD22 1 
ATOM   3714 N N    . THR   A 1 236 ? 219.742 158.396 125.311 1.00 159.27 ? 249  THR   A N    1 
ATOM   3715 C CA   . THR   A 1 236 ? 219.804 159.777 124.789 1.00 163.60 ? 249  THR   A CA   1 
ATOM   3716 C C    . THR   A 1 236 ? 219.026 160.810 125.606 1.00 164.22 ? 249  THR   A C    1 
ATOM   3717 O O    . THR   A 1 236 ? 219.520 161.922 125.783 1.00 160.35 ? 249  THR   A O    1 
ATOM   3718 C CB   . THR   A 1 236 ? 219.413 159.804 123.301 1.00 160.72 ? 249  THR   A CB   1 
ATOM   3719 O OG1  . THR   A 1 236 ? 219.656 161.072 122.735 1.00 160.68 ? 249  THR   A OG1  1 
ATOM   3720 C CG2  . THR   A 1 236 ? 217.941 159.507 123.037 1.00 159.95 ? 249  THR   A CG2  1 
ATOM   3721 H H    . THR   A 1 236 ? 218.836 157.982 125.478 1.00 161.44 ? 249  THR   A H    1 
ATOM   3722 H HA   . THR   A 1 236 ? 220.841 160.112 124.834 1.00 162.14 ? 249  THR   A HA   1 
ATOM   3723 H HB   . THR   A 1 236 ? 220.014 159.065 122.772 1.00 161.36 ? 249  THR   A HB   1 
ATOM   3724 H HG1  . THR   A 1 236 ? 220.606 161.206 122.706 1.00 161.91 ? 249  THR   A HG1  1 
ATOM   3725 H HG21 . THR   A 1 236 ? 217.800 159.332 121.970 1.00 161.12 ? 249  THR   A HG21 1 
ATOM   3726 H HG22 . THR   A 1 236 ? 217.640 158.605 123.572 1.00 161.59 ? 249  THR   A HG22 1 
ATOM   3727 H HG23 . THR   A 1 236 ? 217.315 160.341 123.354 1.00 161.45 ? 249  THR   A HG23 1 
ATOM   3728 N N    . ASP   A 1 237 ? 217.857 160.477 126.161 1.00 169.86 ? 250  ASP   A N    1 
ATOM   3729 C CA   . ASP   A 1 237 ? 217.044 161.454 126.909 1.00 167.00 ? 250  ASP   A CA   1 
ATOM   3730 C C    . ASP   A 1 237 ? 216.130 160.862 127.997 1.00 164.70 ? 250  ASP   A C    1 
ATOM   3731 O O    . ASP   A 1 237 ? 215.503 161.622 128.733 1.00 163.06 ? 250  ASP   A O    1 
ATOM   3732 C CB   . ASP   A 1 237 ? 216.225 162.302 125.920 1.00 166.63 ? 250  ASP   A CB   1 
ATOM   3733 C CG   . ASP   A 1 237 ? 215.261 161.502 125.037 1.00 170.45 ? 250  ASP   A CG   1 
ATOM   3734 O OD1  . ASP   A 1 237 ? 214.959 160.330 125.361 1.00 176.46 ? 250  ASP   A OD1  1 
ATOM   3735 O OD2  . ASP   A 1 237 ? 214.825 162.066 124.009 1.00 165.06 ? 250  ASP   A OD2  1 
ATOM   3736 H H    . ASP   A 1 237 ? 217.439 159.590 125.923 1.00 166.78 ? 250  ASP   A H    1 
ATOM   3737 H HA   . ASP   A 1 237 ? 217.716 162.131 127.436 1.00 165.89 ? 250  ASP   A HA   1 
ATOM   3738 H HB2  . ASP   A 1 237 ? 215.657 163.047 126.477 1.00 166.16 ? 250  ASP   A HB2  1 
ATOM   3739 H HB3  . ASP   A 1 237 ? 216.919 162.846 125.279 1.00 165.64 ? 250  ASP   A HB3  1 
ATOM   3740 N N    . ASN   A 1 238 ? 216.062 159.533 128.134 1.00 160.56 ? 251  ASN   A N    1 
ATOM   3741 C CA   . ASN   A 1 238 ? 215.143 158.835 129.042 1.00 160.41 ? 251  ASN   A CA   1 
ATOM   3742 C C    . ASN   A 1 238 ? 213.654 159.195 128.859 1.00 158.99 ? 251  ASN   A C    1 
ATOM   3743 O O    . ASN   A 1 238 ? 212.837 158.819 129.699 1.00 158.86 ? 251  ASN   A O    1 
ATOM   3744 C CB   . ASN   A 1 238 ? 215.630 158.965 130.506 1.00 160.58 ? 251  ASN   A CB   1 
ATOM   3745 C CG   . ASN   A 1 238 ? 216.618 157.892 130.922 1.00 164.67 ? 251  ASN   A CG   1 
ATOM   3746 O OD1  . ASN   A 1 238 ? 216.417 156.719 130.623 1.00 165.36 ? 251  ASN   A OD1  1 
ATOM   3747 N ND2  . ASN   A 1 238 ? 217.662 158.267 131.643 1.00 166.58 ? 251  ASN   A ND2  1 
ATOM   3748 H H    . ASN   A 1 238 ? 216.550 158.973 127.450 1.00 162.18 ? 251  ASN   A H    1 
ATOM   3749 H HA   . ASN   A 1 238 ? 215.176 157.778 128.774 1.00 162.01 ? 251  ASN   A HA   1 
ATOM   3750 H HB2  . ASN   A 1 238 ? 216.061 159.953 130.672 1.00 161.77 ? 251  ASN   A HB2  1 
ATOM   3751 H HB3  . ASN   A 1 238 ? 214.788 158.874 131.193 1.00 161.76 ? 251  ASN   A HB3  1 
ATOM   3752 H HD21 . ASN   A 1 238 ? 217.815 159.255 131.788 1.00 162.19 ? 251  ASN   A HD21 1 
ATOM   3753 N N    . GLU   A 1 239 ? 213.246 159.809 127.748 1.00 150.49 ? 252  GLU   A N    1 
ATOM   3754 C CA   . GLU   A 1 239 ? 211.822 159.967 127.445 1.00 150.50 ? 252  GLU   A CA   1 
ATOM   3755 C C    . GLU   A 1 239 ? 211.190 158.700 126.864 1.00 148.64 ? 252  GLU   A C    1 
ATOM   3756 O O    . GLU   A 1 239 ? 211.876 157.770 126.445 1.00 150.33 ? 252  GLU   A O    1 
ATOM   3757 C CB   . GLU   A 1 239 ? 211.577 161.183 126.537 1.00 153.12 ? 252  GLU   A CB   1 
ATOM   3758 C CG   . GLU   A 1 239 ? 211.237 162.434 127.355 1.00 152.47 ? 252  GLU   A CG   1 
ATOM   3759 C CD   . GLU   A 1 239 ? 209.969 162.286 128.222 1.00 157.63 ? 252  GLU   A CD   1 
ATOM   3760 O OE1  . GLU   A 1 239 ? 209.237 161.273 128.099 1.00 160.53 ? 252  GLU   A OE1  1 
ATOM   3761 O OE2  . GLU   A 1 239 ? 209.715 163.177 129.061 1.00 160.41 ? 252  GLU   A OE2  1 
ATOM   3762 H H    . GLU   A 1 239 ? 213.917 160.024 127.024 1.00 153.34 ? 252  GLU   A H    1 
ATOM   3763 H HA   . GLU   A 1 239 ? 211.306 160.131 128.391 1.00 152.46 ? 252  GLU   A HA   1 
ATOM   3764 H HB2  . GLU   A 1 239 ? 212.458 161.380 125.925 1.00 152.92 ? 252  GLU   A HB2  1 
ATOM   3765 H HB3  . GLU   A 1 239 ? 210.749 160.989 125.856 1.00 152.90 ? 252  GLU   A HB3  1 
ATOM   3766 H HG2  . GLU   A 1 239 ? 212.088 162.669 127.994 1.00 152.46 ? 252  GLU   A HG2  1 
ATOM   3767 H HG3  . GLU   A 1 239 ? 211.101 163.267 126.665 1.00 152.19 ? 252  GLU   A HG3  1 
ATOM   3768 N N    . THR   A 1 240 ? 209.859 158.664 126.836 1.00 132.21 ? 253  THR   A N    1 
ATOM   3769 C CA   . THR   A 1 240 ? 209.073 157.525 126.336 1.00 133.02 ? 253  THR   A CA   1 
ATOM   3770 C C    . THR   A 1 240 ? 207.802 157.978 125.632 1.00 138.53 ? 253  THR   A C    1 
ATOM   3771 O O    . THR   A 1 240 ? 207.206 158.993 125.996 1.00 144.89 ? 253  THR   A O    1 
ATOM   3772 C CB   . THR   A 1 240 ? 208.679 156.560 127.466 1.00 133.22 ? 253  THR   A CB   1 
ATOM   3773 O OG1  . THR   A 1 240 ? 207.941 157.222 128.472 1.00 132.02 ? 253  THR   A OG1  1 
ATOM   3774 C CG2  . THR   A 1 240 ? 209.878 155.912 128.151 1.00 134.66 ? 253  THR   A CG2  1 
ATOM   3775 H H    . THR   A 1 240 ? 209.363 159.477 127.172 1.00 136.91 ? 253  THR   A H    1 
ATOM   3776 H HA   . THR   A 1 240 ? 209.669 156.967 125.614 1.00 135.86 ? 253  THR   A HA   1 
ATOM   3777 H HB   . THR   A 1 240 ? 208.065 155.764 127.045 1.00 135.75 ? 253  THR   A HB   1 
ATOM   3778 H HG1  . THR   A 1 240 ? 207.896 156.608 129.209 1.00 135.95 ? 253  THR   A HG1  1 
ATOM   3779 H HG21 . THR   A 1 240 ? 209.537 155.143 128.844 1.00 135.80 ? 253  THR   A HG21 1 
ATOM   3780 H HG22 . THR   A 1 240 ? 210.516 155.443 127.401 1.00 136.48 ? 253  THR   A HG22 1 
ATOM   3781 H HG23 . THR   A 1 240 ? 210.456 156.658 128.697 1.00 136.16 ? 253  THR   A HG23 1 
ATOM   3782 N N    . LEU   A 1 241 ? 207.347 157.203 124.648 1.00 130.72 ? 254  LEU   A N    1 
ATOM   3783 C CA   . LEU   A 1 241 ? 205.959 157.249 124.189 1.00 124.84 ? 254  LEU   A CA   1 
ATOM   3784 C C    . LEU   A 1 241 ? 205.106 156.368 125.102 1.00 128.18 ? 254  LEU   A C    1 
ATOM   3785 O O    . LEU   A 1 241 ? 205.593 155.357 125.600 1.00 129.41 ? 254  LEU   A O    1 
ATOM   3786 C CB   . LEU   A 1 241 ? 205.839 156.732 122.747 1.00 122.69 ? 254  LEU   A CB   1 
ATOM   3787 C CG   . LEU   A 1 241 ? 206.715 157.439 121.709 1.00 130.36 ? 254  LEU   A CG   1 
ATOM   3788 C CD1  . LEU   A 1 241 ? 206.551 156.763 120.356 1.00 136.26 ? 254  LEU   A CD1  1 
ATOM   3789 C CD2  . LEU   A 1 241 ? 206.340 158.904 121.534 1.00 129.18 ? 254  LEU   A CD2  1 
ATOM   3790 H H    . LEU   A 1 241 ? 207.882 156.383 124.401 1.00 130.27 ? 254  LEU   A H    1 
ATOM   3791 H HA   . LEU   A 1 241 ? 205.581 158.270 124.232 1.00 130.03 ? 254  LEU   A HA   1 
ATOM   3792 H HB2  . LEU   A 1 241 ? 206.101 155.674 122.743 1.00 130.00 ? 254  LEU   A HB2  1 
ATOM   3793 H HB3  . LEU   A 1 241 ? 204.799 156.819 122.433 1.00 129.34 ? 254  LEU   A HB3  1 
ATOM   3794 H HG   . LEU   A 1 241 ? 207.763 157.363 122.001 1.00 130.78 ? 254  LEU   A HG   1 
ATOM   3795 H HD11 . LEU   A 1 241 ? 206.724 155.691 120.449 1.00 131.31 ? 254  LEU   A HD11 1 
ATOM   3796 H HD12 . LEU   A 1 241 ? 205.544 156.932 119.974 1.00 131.51 ? 254  LEU   A HD12 1 
ATOM   3797 H HD13 . LEU   A 1 241 ? 207.284 157.179 119.666 1.00 131.31 ? 254  LEU   A HD13 1 
ATOM   3798 H HD21 . LEU   A 1 241 ? 206.555 159.448 122.454 1.00 130.75 ? 254  LEU   A HD21 1 
ATOM   3799 H HD22 . LEU   A 1 241 ? 206.929 159.344 120.729 1.00 130.42 ? 254  LEU   A HD22 1 
ATOM   3800 H HD23 . LEU   A 1 241 ? 205.280 158.995 121.299 1.00 129.97 ? 254  LEU   A HD23 1 
ATOM   3801 N N    . GLN   A 1 242 ? 203.833 156.711 125.279 1.00 122.57 ? 255  GLN   A N    1 
ATOM   3802 C CA   . GLN   A 1 242 ? 202.813 155.781 125.763 1.00 120.34 ? 255  GLN   A CA   1 
ATOM   3803 C C    . GLN   A 1 242 ? 201.497 156.088 125.062 1.00 117.40 ? 255  GLN   A C    1 
ATOM   3804 O O    . GLN   A 1 242 ? 201.110 157.250 124.967 1.00 122.76 ? 255  GLN   A O    1 
ATOM   3805 C CB   . GLN   A 1 242 ? 202.615 155.881 127.279 1.00 117.20 ? 255  GLN   A CB   1 
ATOM   3806 C CG   . GLN   A 1 242 ? 203.864 155.551 128.104 1.00 119.66 ? 255  GLN   A CG   1 
ATOM   3807 C CD   . GLN   A 1 242 ? 203.594 155.518 129.601 1.00 125.47 ? 255  GLN   A CD   1 
ATOM   3808 O OE1  . GLN   A 1 242 ? 202.537 155.883 130.090 1.00 126.65 ? 255  GLN   A OE1  1 
ATOM   3809 N NE2  . GLN   A 1 242 ? 204.543 155.079 130.395 1.00 124.79 ? 255  GLN   A NE2  1 
ATOM   3810 H H    . GLN   A 1 242 ? 203.503 157.570 124.863 1.00 122.61 ? 255  GLN   A H    1 
ATOM   3811 H HA   . GLN   A 1 242 ? 203.101 154.758 125.523 1.00 122.28 ? 255  GLN   A HA   1 
ATOM   3812 H HB2  . GLN   A 1 242 ? 202.273 156.884 127.533 1.00 121.12 ? 255  GLN   A HB2  1 
ATOM   3813 H HB3  . GLN   A 1 242 ? 201.829 155.176 127.550 1.00 121.70 ? 255  GLN   A HB3  1 
ATOM   3814 H HG2  . GLN   A 1 242 ? 204.238 154.573 127.802 1.00 121.48 ? 255  GLN   A HG2  1 
ATOM   3815 H HG3  . GLN   A 1 242 ? 204.636 156.298 127.918 1.00 121.82 ? 255  GLN   A HG3  1 
ATOM   3816 H HE21 . GLN   A 1 242 ? 205.412 154.734 130.014 1.00 122.12 ? 255  GLN   A HE21 1 
ATOM   3817 H HE22 . GLN   A 1 242 ? 204.361 155.054 131.388 1.00 122.47 ? 255  GLN   A HE22 1 
ATOM   3818 N N    . TYR   A 1 243 ? 200.773 155.070 124.620 1.00 107.73 ? 256  TYR   A N    1 
ATOM   3819 C CA   . TYR   A 1 243 ? 199.457 155.241 124.018 1.00 104.66 ? 256  TYR   A CA   1 
ATOM   3820 C C    . TYR   A 1 243 ? 198.563 154.113 124.516 1.00 111.39 ? 256  TYR   A C    1 
ATOM   3821 O O    . TYR   A 1 243 ? 198.475 153.047 123.911 1.00 119.42 ? 256  TYR   A O    1 
ATOM   3822 C CB   . TYR   A 1 243 ? 199.587 155.322 122.490 1.00 112.15 ? 256  TYR   A CB   1 
ATOM   3823 C CG   . TYR   A 1 243 ? 198.361 155.884 121.809 1.00 112.98 ? 256  TYR   A CG   1 
ATOM   3824 C CD1  . TYR   A 1 243 ? 197.200 155.110 121.689 1.00 111.84 ? 256  TYR   A CD1  1 
ATOM   3825 C CD2  . TYR   A 1 243 ? 198.370 157.199 121.320 1.00 119.04 ? 256  TYR   A CD2  1 
ATOM   3826 C CE1  . TYR   A 1 243 ? 196.032 155.666 121.146 1.00 113.52 ? 256  TYR   A CE1  1 
ATOM   3827 C CE2  . TYR   A 1 243 ? 197.207 157.757 120.764 1.00 114.18 ? 256  TYR   A CE2  1 
ATOM   3828 C CZ   . TYR   A 1 243 ? 196.026 156.998 120.708 1.00 112.16 ? 256  TYR   A CZ   1 
ATOM   3829 O OH   . TYR   A 1 243 ? 194.875 157.543 120.245 1.00 117.09 ? 256  TYR   A OH   1 
ATOM   3830 H H    . TYR   A 1 243 ? 201.142 154.134 124.711 1.00 116.61 ? 256  TYR   A H    1 
ATOM   3831 H HA   . TYR   A 1 243 ? 199.018 156.178 124.359 1.00 113.94 ? 256  TYR   A HA   1 
ATOM   3832 H HB2  . TYR   A 1 243 ? 200.429 155.970 122.248 1.00 115.87 ? 256  TYR   A HB2  1 
ATOM   3833 H HB3  . TYR   A 1 243 ? 199.808 154.335 122.082 1.00 114.95 ? 256  TYR   A HB3  1 
ATOM   3834 H HD1  . TYR   A 1 243 ? 197.200 154.084 122.025 1.00 115.84 ? 256  TYR   A HD1  1 
ATOM   3835 H HD2  . TYR   A 1 243 ? 199.268 157.795 121.385 1.00 117.01 ? 256  TYR   A HD2  1 
ATOM   3836 H HE1  . TYR   A 1 243 ? 195.131 155.076 121.060 1.00 116.32 ? 256  TYR   A HE1  1 
ATOM   3837 H HE2  . TYR   A 1 243 ? 197.218 158.776 120.405 1.00 115.51 ? 256  TYR   A HE2  1 
ATOM   3838 H HH   . TYR   A 1 243 ? 195.037 158.400 119.844 1.00 114.61 ? 256  TYR   A HH   1 
ATOM   3839 N N    . TRP   A 1 244 ? 197.969 154.307 125.686 1.00 112.02 ? 257  TRP   A N    1 
ATOM   3840 C CA   . TRP   A 1 244 ? 197.143 153.307 126.339 1.00 113.63 ? 257  TRP   A CA   1 
ATOM   3841 C C    . TRP   A 1 244 ? 195.758 153.273 125.713 1.00 112.87 ? 257  TRP   A C    1 
ATOM   3842 O O    . TRP   A 1 244 ? 195.097 154.302 125.688 1.00 121.90 ? 257  TRP   A O    1 
ATOM   3843 C CB   . TRP   A 1 244 ? 197.032 153.663 127.816 1.00 114.69 ? 257  TRP   A CB   1 
ATOM   3844 C CG   . TRP   A 1 244 ? 198.316 153.699 128.563 1.00 110.06 ? 257  TRP   A CG   1 
ATOM   3845 C CD1  . TRP   A 1 244 ? 198.999 154.814 128.885 1.00 112.04 ? 257  TRP   A CD1  1 
ATOM   3846 C CD2  . TRP   A 1 244 ? 199.095 152.588 129.077 1.00 106.93 ? 257  TRP   A CD2  1 
ATOM   3847 N NE1  . TRP   A 1 244 ? 200.146 154.467 129.560 1.00 114.38 ? 257  TRP   A NE1  1 
ATOM   3848 C CE2  . TRP   A 1 244 ? 200.259 153.108 129.700 1.00 110.99 ? 257  TRP   A CE2  1 
ATOM   3849 C CE3  . TRP   A 1 244 ? 198.940 151.193 129.071 1.00 113.06 ? 257  TRP   A CE3  1 
ATOM   3850 C CZ2  . TRP   A 1 244 ? 201.227 152.293 130.289 1.00 115.08 ? 257  TRP   A CZ2  1 
ATOM   3851 C CZ3  . TRP   A 1 244 ? 199.902 150.362 129.663 1.00 120.25 ? 257  TRP   A CZ3  1 
ATOM   3852 C CH2  . TRP   A 1 244 ? 201.044 150.905 130.270 1.00 117.22 ? 257  TRP   A CH2  1 
ATOM   3853 H H    . TRP   A 1 244 ? 198.017 155.217 126.120 1.00 116.70 ? 257  TRP   A H    1 
ATOM   3854 H HA   . TRP   A 1 244 ? 197.611 152.327 126.251 1.00 116.90 ? 257  TRP   A HA   1 
ATOM   3855 H HB2  . TRP   A 1 244 ? 196.553 154.637 127.914 1.00 117.03 ? 257  TRP   A HB2  1 
ATOM   3856 H HB3  . TRP   A 1 244 ? 196.378 152.942 128.305 1.00 116.34 ? 257  TRP   A HB3  1 
ATOM   3857 H HD1  . TRP   A 1 244 ? 198.697 155.819 128.633 1.00 116.39 ? 257  TRP   A HD1  1 
ATOM   3858 H HE1  . TRP   A 1 244 ? 200.843 155.131 129.867 1.00 117.07 ? 257  TRP   A HE1  1 
ATOM   3859 H HE3  . TRP   A 1 244 ? 198.075 150.756 128.594 1.00 116.38 ? 257  TRP   A HE3  1 
ATOM   3860 H HZ2  . TRP   A 1 244 ? 202.100 152.728 130.752 1.00 116.81 ? 257  TRP   A HZ2  1 
ATOM   3861 H HZ3  . TRP   A 1 244 ? 199.770 149.290 129.638 1.00 118.80 ? 257  TRP   A HZ3  1 
ATOM   3862 H HH2  . TRP   A 1 244 ? 201.778 150.252 130.720 1.00 117.36 ? 257  TRP   A HH2  1 
ATOM   3863 N N    . VAL   A 1 245 ? 195.268 152.118 125.271 1.00 107.02 ? 258  VAL   A N    1 
ATOM   3864 C CA   . VAL   A 1 245 ? 193.889 151.971 124.770 1.00 104.50 ? 258  VAL   A CA   1 
ATOM   3865 C C    . VAL   A 1 245 ? 193.130 150.882 125.500 1.00 111.72 ? 258  VAL   A C    1 
ATOM   3866 O O    . VAL   A 1 245 ? 193.724 149.904 125.946 1.00 118.53 ? 258  VAL   A O    1 
ATOM   3867 C CB   . VAL   A 1 245 ? 193.808 151.724 123.261 1.00 104.66 ? 258  VAL   A CB   1 
ATOM   3868 C CG1  . VAL   A 1 245 ? 194.601 152.751 122.474 1.00 114.93 ? 258  VAL   A CG1  1 
ATOM   3869 C CG2  . VAL   A 1 245 ? 194.310 150.344 122.854 1.00 114.09 ? 258  VAL   A CG2  1 
ATOM   3870 H H    . VAL   A 1 245 ? 195.869 151.307 125.279 1.00 114.34 ? 258  VAL   A H    1 
ATOM   3871 H HA   . VAL   A 1 245 ? 193.355 152.904 124.954 1.00 113.31 ? 258  VAL   A HA   1 
ATOM   3872 H HB   . VAL   A 1 245 ? 192.764 151.806 122.959 1.00 112.54 ? 258  VAL   A HB   1 
ATOM   3873 H HG11 . VAL   A 1 245 ? 194.313 153.750 122.803 1.00 114.49 ? 258  VAL   A HG11 1 
ATOM   3874 H HG12 . VAL   A 1 245 ? 194.388 152.650 121.410 1.00 114.41 ? 258  VAL   A HG12 1 
ATOM   3875 H HG13 . VAL   A 1 245 ? 195.667 152.605 122.645 1.00 114.18 ? 258  VAL   A HG13 1 
ATOM   3876 H HG21 . VAL   A 1 245 ? 195.324 150.193 123.225 1.00 114.49 ? 258  VAL   A HG21 1 
ATOM   3877 H HG22 . VAL   A 1 245 ? 194.311 150.278 121.767 1.00 114.13 ? 258  VAL   A HG22 1 
ATOM   3878 H HG23 . VAL   A 1 245 ? 193.658 149.569 123.256 1.00 114.22 ? 258  VAL   A HG23 1 
ATOM   3879 N N    . THR   A 1 246 ? 191.813 151.021 125.610 1.00 113.51 ? 259  THR   A N    1 
ATOM   3880 C CA   . THR   A 1 246 ? 190.929 149.966 126.119 1.00 117.56 ? 259  THR   A CA   1 
ATOM   3881 C C    . THR   A 1 246 ? 189.572 150.002 125.409 1.00 113.29 ? 259  THR   A C    1 
ATOM   3882 O O    . THR   A 1 246 ? 189.148 151.085 125.001 1.00 120.55 ? 259  THR   A O    1 
ATOM   3883 C CB   . THR   A 1 246 ? 190.784 150.093 127.638 1.00 125.73 ? 259  THR   A CB   1 
ATOM   3884 O OG1  . THR   A 1 246 ? 190.216 148.927 128.176 1.00 125.72 ? 259  THR   A OG1  1 
ATOM   3885 C CG2  . THR   A 1 246 ? 189.928 151.283 128.060 1.00 120.83 ? 259  THR   A CG2  1 
ATOM   3886 H H    . THR   A 1 246 ? 191.389 151.879 125.288 1.00 117.54 ? 259  THR   A H    1 
ATOM   3887 H HA   . THR   A 1 246 ? 191.408 149.009 125.913 1.00 118.87 ? 259  THR   A HA   1 
ATOM   3888 H HB   . THR   A 1 246 ? 191.775 150.213 128.076 1.00 119.79 ? 259  THR   A HB   1 
ATOM   3889 H HG1  . THR   A 1 246 ? 190.940 148.346 128.421 1.00 119.74 ? 259  THR   A HG1  1 
ATOM   3890 H HG21 . THR   A 1 246 ? 189.969 151.396 129.143 1.00 118.91 ? 259  THR   A HG21 1 
ATOM   3891 H HG22 . THR   A 1 246 ? 190.321 152.194 127.607 1.00 117.63 ? 259  THR   A HG22 1 
ATOM   3892 H HG23 . THR   A 1 246 ? 188.891 151.140 127.757 1.00 118.17 ? 259  THR   A HG23 1 
ATOM   3893 N N    . PRO   A 1 247 ? 188.880 148.872 125.199 1.00 103.95 ? 260  PRO   A N    1 
ATOM   3894 C CA   . PRO   A 1 247 ? 187.604 148.847 124.493 1.00 106.31 ? 260  PRO   A CA   1 
ATOM   3895 C C    . PRO   A 1 247 ? 186.509 149.649 125.188 1.00 108.89 ? 260  PRO   A C    1 
ATOM   3896 O O    . PRO   A 1 247 ? 186.382 149.598 126.407 1.00 111.55 ? 260  PRO   A O    1 
ATOM   3897 C CB   . PRO   A 1 247 ? 187.194 147.378 124.421 1.00 106.00 ? 260  PRO   A CB   1 
ATOM   3898 C CG   . PRO   A 1 247 ? 188.513 146.633 124.548 1.00 109.45 ? 260  PRO   A CG   1 
ATOM   3899 C CD   . PRO   A 1 247 ? 189.316 147.519 125.486 1.00 106.30 ? 260  PRO   A CD   1 
ATOM   3900 H HA   . PRO   A 1 247 ? 187.754 149.225 123.482 1.00 108.33 ? 260  PRO   A HA   1 
ATOM   3901 H HB2  . PRO   A 1 247 ? 186.559 147.115 125.267 1.00 107.64 ? 260  PRO   A HB2  1 
ATOM   3902 H HB3  . PRO   A 1 247 ? 186.691 147.147 123.483 1.00 108.41 ? 260  PRO   A HB3  1 
ATOM   3903 H HG2  . PRO   A 1 247 ? 188.377 145.631 124.955 1.00 108.86 ? 260  PRO   A HG2  1 
ATOM   3904 H HG3  . PRO   A 1 247 ? 189.003 146.592 123.575 1.00 108.62 ? 260  PRO   A HG3  1 
ATOM   3905 H HD2  . PRO   A 1 247 ? 189.071 147.268 126.518 1.00 108.12 ? 260  PRO   A HD2  1 
ATOM   3906 H HD3  . PRO   A 1 247 ? 190.379 147.371 125.296 1.00 108.67 ? 260  PRO   A HD3  1 
ATOM   3907 N N    . LEU   A 1 248 ? 185.660 150.326 124.420 1.00 117.48 ? 261  LEU   A N    1 
ATOM   3908 C CA   . LEU   A 1 248 ? 184.392 150.873 124.904 1.00 110.93 ? 261  LEU   A CA   1 
ATOM   3909 C C    . LEU   A 1 248 ? 183.263 149.852 124.789 1.00 111.40 ? 261  LEU   A C    1 
ATOM   3910 O O    . LEU   A 1 248 ? 183.302 148.947 123.961 1.00 116.17 ? 261  LEU   A O    1 
ATOM   3911 C CB   . LEU   A 1 248 ? 184.023 152.135 124.116 1.00 109.76 ? 261  LEU   A CB   1 
ATOM   3912 C CG   . LEU   A 1 248 ? 184.954 153.316 124.388 1.00 110.79 ? 261  LEU   A CG   1 
ATOM   3913 C CD1  . LEU   A 1 248 ? 184.598 154.477 123.473 1.00 113.21 ? 261  LEU   A CD1  1 
ATOM   3914 C CD2  . LEU   A 1 248 ? 184.838 153.798 125.825 1.00 118.03 ? 261  LEU   A CD2  1 
ATOM   3915 H H    . LEU   A 1 248 ? 185.807 150.300 123.421 1.00 115.30 ? 261  LEU   A H    1 
ATOM   3916 H HA   . LEU   A 1 248 ? 184.485 151.128 125.959 1.00 113.00 ? 261  LEU   A HA   1 
ATOM   3917 H HB2  . LEU   A 1 248 ? 184.040 151.902 123.051 1.00 114.13 ? 261  LEU   A HB2  1 
ATOM   3918 H HB3  . LEU   A 1 248 ? 183.006 152.434 124.371 1.00 113.46 ? 261  LEU   A HB3  1 
ATOM   3919 H HG   . LEU   A 1 248 ? 185.985 153.019 124.196 1.00 114.35 ? 261  LEU   A HG   1 
ATOM   3920 H HD11 . LEU   A 1 248 ? 184.716 154.167 122.434 1.00 114.71 ? 261  LEU   A HD11 1 
ATOM   3921 H HD12 . LEU   A 1 248 ? 183.571 154.799 123.648 1.00 113.52 ? 261  LEU   A HD12 1 
ATOM   3922 H HD13 . LEU   A 1 248 ? 185.275 155.311 123.656 1.00 115.11 ? 261  LEU   A HD13 1 
ATOM   3923 H HD21 . LEU   A 1 248 ? 185.325 153.084 126.490 1.00 114.29 ? 261  LEU   A HD21 1 
ATOM   3924 H HD22 . LEU   A 1 248 ? 183.786 153.911 126.086 1.00 114.25 ? 261  LEU   A HD22 1 
ATOM   3925 H HD23 . LEU   A 1 248 ? 185.326 154.766 125.936 1.00 114.98 ? 261  LEU   A HD23 1 
ATOM   3926 N N    . SER   A 1 249 ? 182.216 150.030 125.584 1.00 121.78 ? 262  SER   A N    1 
ATOM   3927 C CA   . SER   A 1 249 ? 180.957 149.292 125.464 1.00 123.15 ? 262  SER   A CA   1 
ATOM   3928 C C    . SER   A 1 249 ? 179.807 150.130 126.017 1.00 126.36 ? 262  SER   A C    1 
ATOM   3929 O O    . SER   A 1 249 ? 180.038 151.098 126.741 1.00 134.27 ? 262  SER   A O    1 
ATOM   3930 C CB   . SER   A 1 249 ? 181.076 147.941 126.175 1.00 126.84 ? 262  SER   A CB   1 
ATOM   3931 O OG   . SER   A 1 249 ? 181.432 148.109 127.534 1.00 121.24 ? 262  SER   A OG   1 
ATOM   3932 H H    . SER   A 1 249 ? 182.253 150.760 126.281 1.00 122.91 ? 262  SER   A H    1 
ATOM   3933 H HA   . SER   A 1 249 ? 180.749 149.101 124.411 1.00 122.36 ? 262  SER   A HA   1 
ATOM   3934 H HB2  . SER   A 1 249 ? 180.125 147.411 126.112 1.00 123.72 ? 262  SER   A HB2  1 
ATOM   3935 H HB3  . SER   A 1 249 ? 181.836 147.339 125.678 1.00 124.16 ? 262  SER   A HB3  1 
ATOM   3936 H HG   . SER   A 1 249 ? 182.240 148.627 127.554 1.00 123.14 ? 262  SER   A HG   1 
ATOM   3937 N N    . LYS   A 1 250 ? 178.563 149.810 125.660 1.00 117.57 ? 263  LYS   A N    1 
ATOM   3938 C CA   . LYS   A 1 250 ? 177.383 150.522 126.165 1.00 117.62 ? 263  LYS   A CA   1 
ATOM   3939 C C    . LYS   A 1 250 ? 177.153 150.127 127.626 1.00 116.57 ? 263  LYS   A C    1 
ATOM   3940 O O    . LYS   A 1 250 ? 176.785 148.986 127.900 1.00 114.00 ? 263  LYS   A O    1 
ATOM   3941 C CB   . LYS   A 1 250 ? 176.188 150.200 125.253 1.00 116.88 ? 263  LYS   A CB   1 
ATOM   3942 C CG   . LYS   A 1 250 ? 175.041 151.217 125.321 1.00 119.37 ? 263  LYS   A CG   1 
ATOM   3943 C CD   . LYS   A 1 250 ? 175.413 152.552 124.661 1.00 122.85 ? 263  LYS   A CD   1 
ATOM   3944 C CE   . LYS   A 1 250 ? 174.215 153.501 124.529 1.00 122.52 ? 263  LYS   A CE   1 
ATOM   3945 N NZ   . LYS   A 1 250 ? 173.290 153.101 123.437 1.00 118.76 ? 263  LYS   A NZ   1 
ATOM   3946 H H    . LYS   A 1 250 ? 178.421 149.009 125.062 1.00 117.91 ? 263  LYS   A H    1 
ATOM   3947 H HA   . LYS   A 1 250 ? 177.587 151.592 126.125 1.00 118.26 ? 263  LYS   A HA   1 
ATOM   3948 H HB2  . LYS   A 1 250 ? 176.528 150.155 124.218 1.00 117.71 ? 263  LYS   A HB2  1 
ATOM   3949 H HB3  . LYS   A 1 250 ? 175.797 149.214 125.502 1.00 118.44 ? 263  LYS   A HB3  1 
ATOM   3950 H HG2  . LYS   A 1 250 ? 174.187 150.787 124.798 1.00 118.99 ? 263  LYS   A HG2  1 
ATOM   3951 H HG3  . LYS   A 1 250 ? 174.761 151.382 126.361 1.00 117.41 ? 263  LYS   A HG3  1 
ATOM   3952 H HD2  . LYS   A 1 250 ? 176.172 153.047 125.268 1.00 118.77 ? 263  LYS   A HD2  1 
ATOM   3953 H HD3  . LYS   A 1 250 ? 175.838 152.367 123.674 1.00 118.29 ? 263  LYS   A HD3  1 
ATOM   3954 H HE2  . LYS   A 1 250 ? 173.684 153.532 125.480 1.00 118.24 ? 263  LYS   A HE2  1 
ATOM   3955 H HE3  . LYS   A 1 250 ? 174.592 154.504 124.330 1.00 118.89 ? 263  LYS   A HE3  1 
ATOM   3956 H HZ1  . LYS   A 1 250 ? 173.742 153.142 122.535 1.00 118.20 ? 263  LYS   A HZ1  1 
ATOM   3957 H HZ2  . LYS   A 1 250 ? 172.495 153.723 123.400 1.00 118.49 ? 263  LYS   A HZ2  1 
ATOM   3958 H HZ3  . LYS   A 1 250 ? 172.937 152.165 123.577 1.00 118.84 ? 263  LYS   A HZ3  1 
ATOM   3959 N N    . ARG   A 1 251 ? 177.399 151.039 128.566 1.00 117.69 ? 264  ARG   A N    1 
ATOM   3960 C CA   . ARG   A 1 251 ? 177.405 150.781 130.018 1.00 115.53 ? 264  ARG   A CA   1 
ATOM   3961 C C    . ARG   A 1 251 ? 176.669 151.859 130.780 1.00 119.60 ? 264  ARG   A C    1 
ATOM   3962 O O    . ARG   A 1 251 ? 176.601 152.992 130.319 1.00 122.08 ? 264  ARG   A O    1 
ATOM   3963 C CB   . ARG   A 1 251 ? 178.849 150.703 130.530 1.00 111.44 ? 264  ARG   A CB   1 
ATOM   3964 C CG   . ARG   A 1 251 ? 179.455 149.351 130.192 1.00 111.35 ? 264  ARG   A CG   1 
ATOM   3965 C CD   . ARG   A 1 251 ? 180.852 149.182 130.785 1.00 114.08 ? 264  ARG   A CD   1 
ATOM   3966 N NE   . ARG   A 1 251 ? 181.173 147.750 130.818 1.00 119.52 ? 264  ARG   A NE   1 
ATOM   3967 C CZ   . ARG   A 1 251 ? 180.870 146.927 131.805 1.00 124.94 ? 264  ARG   A CZ   1 
ATOM   3968 N NH1  . ARG   A 1 251 ? 180.831 145.647 131.585 1.00 127.59 ? 264  ARG   A NH1  1 
ATOM   3969 N NH2  . ARG   A 1 251 ? 180.574 147.322 133.007 1.00 120.45 ? 264  ARG   A NH2  1 
ATOM   3970 H H    . ARG   A 1 251 ? 177.691 151.954 128.253 1.00 117.62 ? 264  ARG   A H    1 
ATOM   3971 H HA   . ARG   A 1 251 ? 176.894 149.843 130.233 1.00 117.17 ? 264  ARG   A HA   1 
ATOM   3972 H HB2  . ARG   A 1 251 ? 179.448 151.501 130.091 1.00 117.73 ? 264  ARG   A HB2  1 
ATOM   3973 H HB3  . ARG   A 1 251 ? 178.858 150.816 131.614 1.00 116.18 ? 264  ARG   A HB3  1 
ATOM   3974 H HG2  . ARG   A 1 251 ? 178.801 148.580 130.599 1.00 117.08 ? 264  ARG   A HG2  1 
ATOM   3975 H HG3  . ARG   A 1 251 ? 179.506 149.226 129.110 1.00 116.72 ? 264  ARG   A HG3  1 
ATOM   3976 H HD2  . ARG   A 1 251 ? 181.572 149.718 130.167 1.00 116.84 ? 264  ARG   A HD2  1 
ATOM   3977 H HD3  . ARG   A 1 251 ? 180.883 149.603 131.789 1.00 117.43 ? 264  ARG   A HD3  1 
ATOM   3978 H HE   . ARG   A 1 251 ? 181.408 147.328 129.932 1.00 117.74 ? 264  ARG   A HE   1 
ATOM   3979 H HH11 . ARG   A 1 251 ? 180.910 145.297 130.641 1.00 119.04 ? 264  ARG   A HH11 1 
ATOM   3980 H HH12 . ARG   A 1 251 ? 180.542 145.026 132.327 1.00 118.64 ? 264  ARG   A HH12 1 
ATOM   3981 H HH21 . ARG   A 1 251 ? 180.686 148.289 133.277 1.00 118.01 ? 264  ARG   A HH21 1 
ATOM   3982 H HH22 . ARG   A 1 251 ? 180.349 146.648 133.725 1.00 117.91 ? 264  ARG   A HH22 1 
ATOM   3983 N N    . GLN   A 1 252 ? 176.178 151.525 131.968 1.00 112.30 ? 265  GLN   A N    1 
ATOM   3984 C CA   . GLN   A 1 252 ? 175.562 152.482 132.879 1.00 114.88 ? 265  GLN   A CA   1 
ATOM   3985 C C    . GLN   A 1 252 ? 176.567 152.880 133.955 1.00 110.49 ? 265  GLN   A C    1 
ATOM   3986 O O    . GLN   A 1 252 ? 177.065 152.030 134.688 1.00 107.83 ? 265  GLN   A O    1 
ATOM   3987 C CB   . GLN   A 1 252 ? 174.302 151.869 133.494 1.00 117.53 ? 265  GLN   A CB   1 
ATOM   3988 C CG   . GLN   A 1 252 ? 173.572 152.844 134.427 1.00 116.93 ? 265  GLN   A CG   1 
ATOM   3989 C CD   . GLN   A 1 252 ? 172.323 152.206 135.010 1.00 121.98 ? 265  GLN   A CD   1 
ATOM   3990 O OE1  . GLN   A 1 252 ? 172.363 151.155 135.630 1.00 127.39 ? 265  GLN   A OE1  1 
ATOM   3991 N NE2  . GLN   A 1 252 ? 171.165 152.800 134.841 1.00 119.91 ? 265  GLN   A NE2  1 
ATOM   3992 H H    . GLN   A 1 252 ? 176.301 150.577 132.291 1.00 114.66 ? 265  GLN   A H    1 
ATOM   3993 H HA   . GLN   A 1 252 ? 175.260 153.373 132.329 1.00 115.30 ? 265  GLN   A HA   1 
ATOM   3994 H HB2  . GLN   A 1 252 ? 173.624 151.581 132.691 1.00 115.50 ? 265  GLN   A HB2  1 
ATOM   3995 H HB3  . GLN   A 1 252 ? 174.575 150.973 134.051 1.00 115.44 ? 265  GLN   A HB3  1 
ATOM   3996 H HG2  . GLN   A 1 252 ? 174.221 153.135 135.253 1.00 114.98 ? 265  GLN   A HG2  1 
ATOM   3997 H HG3  . GLN   A 1 252 ? 173.304 153.740 133.867 1.00 114.71 ? 265  GLN   A HG3  1 
ATOM   3998 H HE21 . GLN   A 1 252 ? 171.096 153.658 134.313 1.00 115.27 ? 265  GLN   A HE21 1 
ATOM   3999 H HE22 . GLN   A 1 252 ? 170.345 152.357 135.230 1.00 116.33 ? 265  GLN   A HE22 1 
ATOM   4000 N N    . TYR   A 1 253 ? 176.849 154.169 134.067 1.00 112.02 ? 266  TYR   A N    1 
ATOM   4001 C CA   . TYR   A 1 253 ? 177.752 154.741 135.056 1.00 112.83 ? 266  TYR   A CA   1 
ATOM   4002 C C    . TYR   A 1 253 ? 176.978 155.652 135.998 1.00 121.64 ? 266  TYR   A C    1 
ATOM   4003 O O    . TYR   A 1 253 ? 176.099 156.394 135.568 1.00 125.49 ? 266  TYR   A O    1 
ATOM   4004 C CB   . TYR   A 1 253 ? 178.838 155.578 134.372 1.00 116.89 ? 266  TYR   A CB   1 
ATOM   4005 C CG   . TYR   A 1 253 ? 180.106 154.865 133.961 1.00 117.45 ? 266  TYR   A CG   1 
ATOM   4006 C CD1  . TYR   A 1 253 ? 180.101 153.539 133.500 1.00 117.55 ? 266  TYR   A CD1  1 
ATOM   4007 C CD2  . TYR   A 1 253 ? 181.320 155.565 134.049 1.00 115.78 ? 266  TYR   A CD2  1 
ATOM   4008 C CE1  . TYR   A 1 253 ? 181.305 152.912 133.142 1.00 116.01 ? 266  TYR   A CE1  1 
ATOM   4009 C CE2  . TYR   A 1 253 ? 182.526 154.939 133.710 1.00 114.66 ? 266  TYR   A CE2  1 
ATOM   4010 C CZ   . TYR   A 1 253 ? 182.516 153.611 133.257 1.00 112.71 ? 266  TYR   A CZ   1 
ATOM   4011 O OH   . TYR   A 1 253 ? 183.676 153.024 132.893 1.00 120.26 ? 266  TYR   A OH   1 
ATOM   4012 H H    . TYR   A 1 253 ? 176.367 154.817 133.460 1.00 115.79 ? 266  TYR   A H    1 
ATOM   4013 H HA   . TYR   A 1 253 ? 178.225 153.953 135.642 1.00 115.32 ? 266  TYR   A HA   1 
ATOM   4014 H HB2  . TYR   A 1 253 ? 178.415 156.076 133.499 1.00 116.45 ? 266  TYR   A HB2  1 
ATOM   4015 H HB3  . TYR   A 1 253 ? 179.133 156.366 135.064 1.00 116.03 ? 266  TYR   A HB3  1 
ATOM   4016 H HD1  . TYR   A 1 253 ? 179.176 152.989 133.411 1.00 115.87 ? 266  TYR   A HD1  1 
ATOM   4017 H HD2  . TYR   A 1 253 ? 181.325 156.591 134.387 1.00 115.78 ? 266  TYR   A HD2  1 
ATOM   4018 H HE1  . TYR   A 1 253 ? 181.305 151.894 132.782 1.00 116.36 ? 266  TYR   A HE1  1 
ATOM   4019 H HE2  . TYR   A 1 253 ? 183.461 155.475 133.781 1.00 116.38 ? 266  TYR   A HE2  1 
ATOM   4020 H HH   . TYR   A 1 253 ? 183.546 152.248 132.343 1.00 116.45 ? 266  TYR   A HH   1 
ATOM   4021 N N    . LEU   A 1 254 ? 177.348 155.660 137.272 1.00 121.55 ? 267  LEU   A N    1 
ATOM   4022 C CA   . LEU   A 1 254 ? 177.077 156.795 138.138 1.00 108.14 ? 267  LEU   A CA   1 
ATOM   4023 C C    . LEU   A 1 254 ? 178.111 157.873 137.831 1.00 107.82 ? 267  LEU   A C    1 
ATOM   4024 O O    . LEU   A 1 254 ? 179.299 157.575 137.855 1.00 120.79 ? 267  LEU   A O    1 
ATOM   4025 C CB   . LEU   A 1 254 ? 177.181 156.338 139.594 1.00 102.35 ? 267  LEU   A CB   1 
ATOM   4026 C CG   . LEU   A 1 254 ? 176.704 157.404 140.580 1.00 111.02 ? 267  LEU   A CG   1 
ATOM   4027 C CD1  . LEU   A 1 254 ? 175.183 157.408 140.662 1.00 123.88 ? 267  LEU   A CD1  1 
ATOM   4028 C CD2  . LEU   A 1 254 ? 177.260 157.119 141.966 1.00 114.38 ? 267  LEU   A CD2  1 
ATOM   4029 H H    . LEU   A 1 254 ? 178.095 155.035 137.542 1.00 115.16 ? 267  LEU   A H    1 
ATOM   4030 H HA   . LEU   A 1 254 ? 176.076 157.179 137.943 1.00 113.03 ? 267  LEU   A HA   1 
ATOM   4031 H HB2  . LEU   A 1 254 ? 176.603 155.425 139.740 1.00 112.53 ? 267  LEU   A HB2  1 
ATOM   4032 H HB3  . LEU   A 1 254 ? 178.227 156.114 139.802 1.00 112.04 ? 267  LEU   A HB3  1 
ATOM   4033 H HG   . LEU   A 1 254 ? 177.052 158.390 140.271 1.00 112.60 ? 267  LEU   A HG   1 
ATOM   4034 H HD11 . LEU   A 1 254 ? 174.757 157.682 139.697 1.00 114.24 ? 267  LEU   A HD11 1 
ATOM   4035 H HD12 . LEU   A 1 254 ? 174.821 156.421 140.948 1.00 115.59 ? 267  LEU   A HD12 1 
ATOM   4036 H HD13 . LEU   A 1 254 ? 174.855 158.131 141.409 1.00 114.71 ? 267  LEU   A HD13 1 
ATOM   4037 H HD21 . LEU   A 1 254 ? 178.350 157.146 141.937 1.00 113.54 ? 267  LEU   A HD21 1 
ATOM   4038 H HD22 . LEU   A 1 254 ? 176.910 157.877 142.666 1.00 113.38 ? 267  LEU   A HD22 1 
ATOM   4039 H HD23 . LEU   A 1 254 ? 176.933 156.135 142.304 1.00 114.78 ? 267  LEU   A HD23 1 
ATOM   4040 N N    . LEU   A 1 255 ? 177.703 159.107 137.575 1.00 95.44  ? 268  LEU   A N    1 
ATOM   4041 C CA   . LEU   A 1 255 ? 178.591 160.257 137.392 1.00 91.94  ? 268  LEU   A CA   1 
ATOM   4042 C C    . LEU   A 1 255 ? 178.345 161.265 138.505 1.00 101.87 ? 268  LEU   A C    1 
ATOM   4043 O O    . LEU   A 1 255 ? 177.189 161.595 138.749 1.00 119.24 ? 268  LEU   A O    1 
ATOM   4044 C CB   . LEU   A 1 255 ? 178.301 160.913 136.036 1.00 98.55  ? 268  LEU   A CB   1 
ATOM   4045 C CG   . LEU   A 1 255 ? 178.511 160.011 134.818 1.00 103.99 ? 268  LEU   A CG   1 
ATOM   4046 C CD1  . LEU   A 1 255 ? 178.038 160.738 133.569 1.00 103.67 ? 268  LEU   A CD1  1 
ATOM   4047 C CD2  . LEU   A 1 255 ? 179.977 159.654 134.632 1.00 107.89 ? 268  LEU   A CD2  1 
ATOM   4048 H H    . LEU   A 1 255 ? 176.708 159.274 137.532 1.00 107.26 ? 268  LEU   A H    1 
ATOM   4049 H HA   . LEU   A 1 255 ? 179.637 159.951 137.431 1.00 105.48 ? 268  LEU   A HA   1 
ATOM   4050 H HB2  . LEU   A 1 255 ? 177.263 161.244 136.035 1.00 105.67 ? 268  LEU   A HB2  1 
ATOM   4051 H HB3  . LEU   A 1 255 ? 178.931 161.797 135.931 1.00 105.83 ? 268  LEU   A HB3  1 
ATOM   4052 H HG   . LEU   A 1 255 ? 177.929 159.095 134.920 1.00 106.79 ? 268  LEU   A HG   1 
ATOM   4053 H HD11 . LEU   A 1 255 ? 176.980 160.980 133.671 1.00 106.25 ? 268  LEU   A HD11 1 
ATOM   4054 H HD12 . LEU   A 1 255 ? 178.167 160.098 132.697 1.00 106.42 ? 268  LEU   A HD12 1 
ATOM   4055 H HD13 . LEU   A 1 255 ? 178.607 161.658 133.430 1.00 105.65 ? 268  LEU   A HD13 1 
ATOM   4056 H HD21 . LEU   A 1 255 ? 180.317 159.057 135.478 1.00 107.30 ? 268  LEU   A HD21 1 
ATOM   4057 H HD22 . LEU   A 1 255 ? 180.575 160.562 134.556 1.00 106.90 ? 268  LEU   A HD22 1 
ATOM   4058 H HD23 . LEU   A 1 255 ? 180.095 159.063 133.724 1.00 106.60 ? 268  LEU   A HD23 1 
ATOM   4059 N N    . LYS   A 1 256 ? 179.379 161.794 139.160 1.00 108.11 ? 269  LYS   A N    1 
ATOM   4060 C CA   . LYS   A 1 256 ? 179.239 162.882 140.139 1.00 107.34 ? 269  LYS   A CA   1 
ATOM   4061 C C    . LYS   A 1 256 ? 179.753 164.198 139.579 1.00 114.03 ? 269  LYS   A C    1 
ATOM   4062 O O    . LYS   A 1 256 ? 180.915 164.290 139.199 1.00 128.79 ? 269  LYS   A O    1 
ATOM   4063 C CB   . LYS   A 1 256 ? 179.970 162.527 141.435 1.00 102.29 ? 269  LYS   A CB   1 
ATOM   4064 C CG   . LYS   A 1 256 ? 179.703 163.607 142.488 1.00 104.34 ? 269  LYS   A CG   1 
ATOM   4065 C CD   . LYS   A 1 256 ? 180.286 163.246 143.850 1.00 118.51 ? 269  LYS   A CD   1 
ATOM   4066 C CE   . LYS   A 1 256 ? 180.012 164.407 144.809 1.00 119.00 ? 269  LYS   A CE   1 
ATOM   4067 N NZ   . LYS   A 1 256 ? 180.546 164.129 146.163 1.00 128.46 ? 269  LYS   A NZ   1 
ATOM   4068 H H    . LYS   A 1 256 ? 180.309 161.468 138.937 1.00 114.06 ? 269  LYS   A H    1 
ATOM   4069 H HA   . LYS   A 1 256 ? 178.185 163.020 140.380 1.00 113.67 ? 269  LYS   A HA   1 
ATOM   4070 H HB2  . LYS   A 1 256 ? 179.614 161.564 141.801 1.00 113.74 ? 269  LYS   A HB2  1 
ATOM   4071 H HB3  . LYS   A 1 256 ? 181.042 162.457 141.248 1.00 113.61 ? 269  LYS   A HB3  1 
ATOM   4072 H HG2  . LYS   A 1 256 ? 180.150 164.546 142.164 1.00 113.08 ? 269  LYS   A HG2  1 
ATOM   4073 H HG3  . LYS   A 1 256 ? 178.628 163.752 142.592 1.00 113.40 ? 269  LYS   A HG3  1 
ATOM   4074 H HD2  . LYS   A 1 256 ? 179.812 162.337 144.219 1.00 115.73 ? 269  LYS   A HD2  1 
ATOM   4075 H HD3  . LYS   A 1 256 ? 181.360 163.088 143.757 1.00 115.11 ? 269  LYS   A HD3  1 
ATOM   4076 H HE2  . LYS   A 1 256 ? 180.471 165.310 144.406 1.00 114.40 ? 269  LYS   A HE2  1 
ATOM   4077 H HE3  . LYS   A 1 256 ? 178.936 164.573 144.860 1.00 114.39 ? 269  LYS   A HE3  1 
ATOM   4078 H HZ1  . LYS   A 1 256 ? 180.361 164.899 146.789 1.00 116.05 ? 269  LYS   A HZ1  1 
ATOM   4079 H HZ2  . LYS   A 1 256 ? 180.122 163.302 146.559 1.00 115.71 ? 269  LYS   A HZ2  1 
ATOM   4080 H HZ3  . LYS   A 1 256 ? 181.545 163.986 146.139 1.00 116.88 ? 269  LYS   A HZ3  1 
ATOM   4081 N N    . PHE   A 1 257 ? 178.918 165.226 139.597 1.00 99.55  ? 270  PHE   A N    1 
ATOM   4082 C CA   . PHE   A 1 257 ? 179.247 166.573 139.152 1.00 97.57  ? 270  PHE   A CA   1 
ATOM   4083 C C    . PHE   A 1 257 ? 179.427 167.495 140.352 1.00 104.98 ? 270  PHE   A C    1 
ATOM   4084 O O    . PHE   A 1 257 ? 178.568 167.515 141.229 1.00 113.56 ? 270  PHE   A O    1 
ATOM   4085 C CB   . PHE   A 1 257 ? 178.117 167.091 138.270 1.00 100.22 ? 270  PHE   A CB   1 
ATOM   4086 C CG   . PHE   A 1 257 ? 177.910 166.313 136.994 1.00 95.17  ? 270  PHE   A CG   1 
ATOM   4087 C CD1  . PHE   A 1 257 ? 177.156 165.132 136.997 1.00 100.93 ? 270  PHE   A CD1  1 
ATOM   4088 C CD2  . PHE   A 1 257 ? 178.450 166.792 135.793 1.00 101.72 ? 270  PHE   A CD2  1 
ATOM   4089 C CE1  . PHE   A 1 257 ? 176.952 164.428 135.803 1.00 108.25 ? 270  PHE   A CE1  1 
ATOM   4090 C CE2  . PHE   A 1 257 ? 178.233 166.097 134.596 1.00 108.06 ? 270  PHE   A CE2  1 
ATOM   4091 C CZ   . PHE   A 1 257 ? 177.495 164.906 134.605 1.00 109.73 ? 270  PHE   A CZ   1 
ATOM   4092 H H    . PHE   A 1 257 ? 177.991 165.077 139.969 1.00 108.77 ? 270  PHE   A H    1 
ATOM   4093 H HA   . PHE   A 1 257 ? 180.166 166.565 138.566 1.00 107.22 ? 270  PHE   A HA   1 
ATOM   4094 H HB2  . PHE   A 1 257 ? 177.186 167.084 138.836 1.00 108.38 ? 270  PHE   A HB2  1 
ATOM   4095 H HB3  . PHE   A 1 257 ? 178.331 168.129 138.014 1.00 107.76 ? 270  PHE   A HB3  1 
ATOM   4096 H HD1  . PHE   A 1 257 ? 176.722 164.765 137.916 1.00 108.12 ? 270  PHE   A HD1  1 
ATOM   4097 H HD2  . PHE   A 1 257 ? 179.023 167.707 135.782 1.00 107.27 ? 270  PHE   A HD2  1 
ATOM   4098 H HE1  . PHE   A 1 257 ? 176.371 163.517 135.805 1.00 108.08 ? 270  PHE   A HE1  1 
ATOM   4099 H HE2  . PHE   A 1 257 ? 178.646 166.471 133.671 1.00 108.17 ? 270  PHE   A HE2  1 
ATOM   4100 H HZ   . PHE   A 1 257 ? 177.340 164.360 133.686 1.00 108.97 ? 270  PHE   A HZ   1 
ATOM   4101 N N    . ASP   A 1 258 ? 180.510 168.263 140.420 1.00 124.10 ? 271  ASP   A N    1 
ATOM   4102 C CA   . ASP   A 1 258 ? 180.715 169.222 141.510 1.00 127.48 ? 271  ASP   A CA   1 
ATOM   4103 C C    . ASP   A 1 258 ? 179.862 170.491 141.358 1.00 129.50 ? 271  ASP   A C    1 
ATOM   4104 O O    . ASP   A 1 258 ? 179.064 170.640 140.434 1.00 137.66 ? 271  ASP   A O    1 
ATOM   4105 C CB   . ASP   A 1 258 ? 182.204 169.545 141.686 1.00 126.53 ? 271  ASP   A CB   1 
ATOM   4106 C CG   . ASP   A 1 258 ? 182.803 170.508 140.654 1.00 134.91 ? 271  ASP   A CG   1 
ATOM   4107 O OD1  . ASP   A 1 258 ? 182.095 170.896 139.698 1.00 139.02 ? 271  ASP   A OD1  1 
ATOM   4108 O OD2  . ASP   A 1 258 ? 183.961 170.939 140.870 1.00 136.28 ? 271  ASP   A OD2  1 
ATOM   4109 H H    . ASP   A 1 258 ? 181.173 168.245 139.659 1.00 128.81 ? 271  ASP   A H    1 
ATOM   4110 H HA   . ASP   A 1 258 ? 180.398 168.746 142.437 1.00 129.70 ? 271  ASP   A HA   1 
ATOM   4111 H HB2  . ASP   A 1 258 ? 182.333 169.983 142.676 1.00 128.80 ? 271  ASP   A HB2  1 
ATOM   4112 H HB3  . ASP   A 1 258 ? 182.763 168.609 141.684 1.00 128.69 ? 271  ASP   A HB3  1 
ATOM   4113 N N    . ASN   A 1 259 ? 180.009 171.440 142.277 1.00 128.48 ? 272  ASN   A N    1 
ATOM   4114 C CA   . ASN   A 1 259 ? 179.264 172.696 142.263 1.00 131.35 ? 272  ASN   A CA   1 
ATOM   4115 C C    . ASN   A 1 259 ? 179.695 173.682 141.163 1.00 125.53 ? 272  ASN   A C    1 
ATOM   4116 O O    . ASN   A 1 259 ? 179.188 174.803 141.147 1.00 125.73 ? 272  ASN   A O    1 
ATOM   4117 C CB   . ASN   A 1 259 ? 179.305 173.318 143.666 1.00 131.31 ? 272  ASN   A CB   1 
ATOM   4118 C CG   . ASN   A 1 259 ? 180.715 173.673 144.088 1.00 135.19 ? 272  ASN   A CG   1 
ATOM   4119 O OD1  . ASN   A 1 259 ? 181.522 172.809 144.394 1.00 136.05 ? 272  ASN   A OD1  1 
ATOM   4120 N ND2  . ASN   A 1 259 ? 181.067 174.935 144.097 1.00 136.57 ? 272  ASN   A ND2  1 
ATOM   4121 H H    . ASN   A 1 259 ? 180.677 171.303 143.022 1.00 130.18 ? 272  ASN   A H    1 
ATOM   4122 H HA   . ASN   A 1 259 ? 178.222 172.463 142.042 1.00 130.97 ? 272  ASN   A HA   1 
ATOM   4123 H HB2  . ASN   A 1 259 ? 178.679 174.210 143.690 1.00 130.67 ? 272  ASN   A HB2  1 
ATOM   4124 H HB3  . ASN   A 1 259 ? 178.901 172.612 144.391 1.00 130.30 ? 272  ASN   A HB3  1 
ATOM   4125 H HD21 . ASN   A 1 259 ? 180.410 175.651 143.822 1.00 131.48 ? 272  ASN   A HD21 1 
ATOM   4126 H HD22 . ASN   A 1 259 ? 182.009 175.167 144.380 1.00 131.55 ? 272  ASN   A HD22 1 
ATOM   4127 N N    . ARG   A 1 260 ? 180.579 173.298 140.232 1.00 126.90 ? 273  ARG   A N    1 
ATOM   4128 C CA   . ARG   A 1 260 ? 180.900 174.077 139.024 1.00 129.64 ? 273  ARG   A CA   1 
ATOM   4129 C C    . ARG   A 1 260 ? 180.776 173.266 137.732 1.00 130.26 ? 273  ARG   A C    1 
ATOM   4130 O O    . ARG   A 1 260 ? 181.222 173.710 136.678 1.00 130.46 ? 273  ARG   A O    1 
ATOM   4131 C CB   . ARG   A 1 260 ? 182.227 174.829 139.203 1.00 130.76 ? 273  ARG   A CB   1 
ATOM   4132 C CG   . ARG   A 1 260 ? 183.488 174.022 138.869 1.00 137.52 ? 273  ARG   A CG   1 
ATOM   4133 C CD   . ARG   A 1 260 ? 184.698 174.614 139.598 1.00 139.01 ? 273  ARG   A CD   1 
ATOM   4134 N NE   . ARG   A 1 260 ? 185.978 174.221 138.983 1.00 147.86 ? 273  ARG   A NE   1 
ATOM   4135 C CZ   . ARG   A 1 260 ? 186.680 173.118 139.180 1.00 147.14 ? 273  ARG   A CZ   1 
ATOM   4136 N NH1  . ARG   A 1 260 ? 187.867 173.021 138.659 1.00 142.55 ? 273  ARG   A NH1  1 
ATOM   4137 N NH2  . ARG   A 1 260 ? 186.266 172.096 139.872 1.00 147.86 ? 273  ARG   A NH2  1 
ATOM   4138 H H    . ARG   A 1 260 ? 180.984 172.375 140.304 1.00 134.50 ? 273  ARG   A H    1 
ATOM   4139 H HA   . ARG   A 1 260 ? 180.134 174.845 138.918 1.00 134.67 ? 273  ARG   A HA   1 
ATOM   4140 H HB2  . ARG   A 1 260 ? 182.217 175.710 138.561 1.00 134.43 ? 273  ARG   A HB2  1 
ATOM   4141 H HB3  . ARG   A 1 260 ? 182.284 175.183 140.232 1.00 134.58 ? 273  ARG   A HB3  1 
ATOM   4142 H HG2  . ARG   A 1 260 ? 183.370 172.982 139.174 1.00 136.16 ? 273  ARG   A HG2  1 
ATOM   4143 H HG3  . ARG   A 1 260 ? 183.656 174.060 137.793 1.00 135.69 ? 273  ARG   A HG3  1 
ATOM   4144 H HD2  . ARG   A 1 260 ? 184.627 175.701 139.561 1.00 134.86 ? 273  ARG   A HD2  1 
ATOM   4145 H HD3  . ARG   A 1 260 ? 184.671 174.314 140.646 1.00 135.50 ? 273  ARG   A HD3  1 
ATOM   4146 H HE   . ARG   A 1 260 ? 186.419 174.913 138.394 1.00 136.60 ? 273  ARG   A HE   1 
ATOM   4147 H HH11 . ARG   A 1 260 ? 188.246 173.783 138.116 1.00 136.07 ? 273  ARG   A HH11 1 
ATOM   4148 H HH12 . ARG   A 1 260 ? 188.418 172.187 138.807 1.00 136.46 ? 273  ARG   A HH12 1 
ATOM   4149 H HH21 . ARG   A 1 260 ? 185.316 172.024 140.208 1.00 136.88 ? 273  ARG   A HH21 1 
ATOM   4150 H HH22 . ARG   A 1 260 ? 186.872 171.299 140.004 1.00 136.83 ? 273  ARG   A HH22 1 
ATOM   4151 N N    . GLY   A 1 261 ? 180.125 172.108 137.795 1.00 117.47 ? 274  GLY   A N    1 
ATOM   4152 C CA   . GLY   A 1 261 ? 179.746 171.300 136.640 1.00 115.84 ? 274  GLY   A CA   1 
ATOM   4153 C C    . GLY   A 1 261 ? 180.834 170.377 136.104 1.00 116.66 ? 274  GLY   A C    1 
ATOM   4154 O O    . GLY   A 1 261 ? 180.651 169.788 135.043 1.00 119.07 ? 274  GLY   A O    1 
ATOM   4155 H H    . GLY   A 1 261 ? 179.846 171.776 138.707 1.00 120.23 ? 274  GLY   A H    1 
ATOM   4156 H HA2  . GLY   A 1 261 ? 178.910 170.667 136.935 1.00 118.78 ? 274  GLY   A HA2  1 
ATOM   4157 H HA3  . GLY   A 1 261 ? 179.415 171.952 135.831 1.00 118.69 ? 274  GLY   A HA3  1 
ATOM   4158 N N    . VAL   A 1 262 ? 181.959 170.229 136.797 1.00 116.70 ? 275  VAL   A N    1 
ATOM   4159 C CA   . VAL   A 1 262 ? 183.015 169.286 136.416 1.00 112.31 ? 275  VAL   A CA   1 
ATOM   4160 C C    . VAL   A 1 262 ? 182.653 167.890 136.908 1.00 119.29 ? 275  VAL   A C    1 
ATOM   4161 O O    . VAL   A 1 262 ? 182.246 167.740 138.056 1.00 126.99 ? 275  VAL   A O    1 
ATOM   4162 C CB   . VAL   A 1 262 ? 184.355 169.738 137.006 1.00 114.20 ? 275  VAL   A CB   1 
ATOM   4163 C CG1  . VAL   A 1 262 ? 185.476 168.736 136.727 1.00 119.24 ? 275  VAL   A CG1  1 
ATOM   4164 C CG2  . VAL   A 1 262 ? 184.779 171.079 136.401 1.00 117.92 ? 275  VAL   A CG2  1 
ATOM   4165 H H    . VAL   A 1 262 ? 182.019 170.657 137.710 1.00 119.65 ? 275  VAL   A H    1 
ATOM   4166 H HA   . VAL   A 1 262 ? 183.111 169.260 135.330 1.00 117.66 ? 275  VAL   A HA   1 
ATOM   4167 H HB   . VAL   A 1 262 ? 184.261 169.853 138.086 1.00 118.96 ? 275  VAL   A HB   1 
ATOM   4168 H HG11 . VAL   A 1 262 ? 185.292 167.804 137.261 1.00 119.39 ? 275  VAL   A HG11 1 
ATOM   4169 H HG12 . VAL   A 1 262 ? 186.426 169.138 137.079 1.00 119.31 ? 275  VAL   A HG12 1 
ATOM   4170 H HG13 . VAL   A 1 262 ? 185.547 168.538 135.657 1.00 118.76 ? 275  VAL   A HG13 1 
ATOM   4171 H HG21 . VAL   A 1 262 ? 184.047 171.849 136.644 1.00 119.38 ? 275  VAL   A HG21 1 
ATOM   4172 H HG22 . VAL   A 1 262 ? 184.859 170.990 135.318 1.00 119.28 ? 275  VAL   A HG22 1 
ATOM   4173 H HG23 . VAL   A 1 262 ? 185.743 171.382 136.809 1.00 118.99 ? 275  VAL   A HG23 1 
ATOM   4174 N N    . ILE   A 1 263 ? 182.823 166.846 136.094 1.00 114.97 ? 276  ILE   A N    1 
ATOM   4175 C CA   . ILE   A 1 263 ? 182.671 165.463 136.571 1.00 113.60 ? 276  ILE   A CA   1 
ATOM   4176 C C    . ILE   A 1 263 ? 183.886 165.119 137.426 1.00 106.21 ? 276  ILE   A C    1 
ATOM   4177 O O    . ILE   A 1 263 ? 184.991 165.032 136.899 1.00 117.53 ? 276  ILE   A O    1 
ATOM   4178 C CB   . ILE   A 1 263 ? 182.508 164.469 135.406 1.00 106.07 ? 276  ILE   A CB   1 
ATOM   4179 C CG1  . ILE   A 1 263 ? 181.203 164.739 134.644 1.00 109.92 ? 276  ILE   A CG1  1 
ATOM   4180 C CG2  . ILE   A 1 263 ? 182.518 163.023 135.922 1.00 107.00 ? 276  ILE   A CG2  1 
ATOM   4181 C CD1  . ILE   A 1 263 ? 181.113 164.008 133.304 1.00 112.40 ? 276  ILE   A CD1  1 
ATOM   4182 H H    . ILE   A 1 263 ? 183.184 167.004 135.163 1.00 112.56 ? 276  ILE   A H    1 
ATOM   4183 H HA   . ILE   A 1 263 ? 181.777 165.396 137.192 1.00 113.76 ? 276  ILE   A HA   1 
ATOM   4184 H HB   . ILE   A 1 263 ? 183.342 164.597 134.716 1.00 112.33 ? 276  ILE   A HB   1 
ATOM   4185 H HG12 . ILE   A 1 263 ? 180.358 164.448 135.268 1.00 112.83 ? 276  ILE   A HG12 1 
ATOM   4186 H HG13 . ILE   A 1 263 ? 181.121 165.805 134.432 1.00 112.76 ? 276  ILE   A HG13 1 
ATOM   4187 H HG21 . ILE   A 1 263 ? 183.470 162.785 136.396 1.00 111.51 ? 276  ILE   A HG21 1 
ATOM   4188 H HG22 . ILE   A 1 263 ? 182.394 162.324 135.095 1.00 111.85 ? 276  ILE   A HG22 1 
ATOM   4189 H HG23 . ILE   A 1 263 ? 181.711 162.875 136.639 1.00 113.45 ? 276  ILE   A HG23 1 
ATOM   4190 H HD11 . ILE   A 1 263 ? 180.210 164.327 132.784 1.00 113.49 ? 276  ILE   A HD11 1 
ATOM   4191 H HD12 . ILE   A 1 263 ? 181.062 162.929 133.451 1.00 111.59 ? 276  ILE   A HD12 1 
ATOM   4192 H HD13 . ILE   A 1 263 ? 181.977 164.255 132.687 1.00 113.23 ? 276  ILE   A HD13 1 
ATOM   4193 N N    . THR   A 1 264 ? 183.728 164.927 138.732 1.00 97.30  ? 277  THR   A N    1 
ATOM   4194 C CA   . THR   A 1 264 ? 184.870 164.635 139.615 1.00 106.41 ? 277  THR   A CA   1 
ATOM   4195 C C    . THR   A 1 264 ? 185.055 163.156 139.902 1.00 112.43 ? 277  THR   A C    1 
ATOM   4196 O O    . THR   A 1 264 ? 186.175 162.742 140.175 1.00 118.52 ? 277  THR   A O    1 
ATOM   4197 C CB   . THR   A 1 264 ? 184.791 165.380 140.946 1.00 110.86 ? 277  THR   A CB   1 
ATOM   4198 O OG1  . THR   A 1 264 ? 183.659 165.001 141.686 1.00 112.29 ? 277  THR   A OG1  1 
ATOM   4199 C CG2  . THR   A 1 264 ? 184.757 166.885 140.741 1.00 114.15 ? 277  THR   A CG2  1 
ATOM   4200 H H    . THR   A 1 264 ? 182.805 165.014 139.131 1.00 111.23 ? 277  THR   A H    1 
ATOM   4201 H HA   . THR   A 1 264 ? 185.791 164.969 139.138 1.00 111.18 ? 277  THR   A HA   1 
ATOM   4202 H HB   . THR   A 1 264 ? 185.679 165.142 141.532 1.00 111.03 ? 277  THR   A HB   1 
ATOM   4203 H HG1  . THR   A 1 264 ? 183.886 164.195 142.156 1.00 111.78 ? 277  THR   A HG1  1 
ATOM   4204 H HG21 . THR   A 1 264 ? 184.795 167.382 141.710 1.00 111.61 ? 277  THR   A HG21 1 
ATOM   4205 H HG22 . THR   A 1 264 ? 185.623 167.194 140.154 1.00 112.49 ? 277  THR   A HG22 1 
ATOM   4206 H HG23 . THR   A 1 264 ? 183.846 167.175 140.217 1.00 112.05 ? 277  THR   A HG23 1 
ATOM   4207 N N    . ASN   A 1 265 ? 183.999 162.342 139.857 1.00 108.66 ? 278  ASN   A N    1 
ATOM   4208 C CA   . ASN   A 1 265 ? 184.054 160.920 140.200 1.00 105.09 ? 278  ASN   A CA   1 
ATOM   4209 C C    . ASN   A 1 265 ? 183.045 160.116 139.391 1.00 102.04 ? 278  ASN   A C    1 
ATOM   4210 O O    . ASN   A 1 265 ? 182.039 160.662 138.945 1.00 109.83 ? 278  ASN   A O    1 
ATOM   4211 C CB   . ASN   A 1 265 ? 183.787 160.719 141.697 1.00 102.79 ? 278  ASN   A CB   1 
ATOM   4212 C CG   . ASN   A 1 265 ? 184.717 161.515 142.582 1.00 114.45 ? 278  ASN   A CG   1 
ATOM   4213 O OD1  . ASN   A 1 265 ? 184.442 162.653 142.936 1.00 122.85 ? 278  ASN   A OD1  1 
ATOM   4214 N ND2  . ASN   A 1 265 ? 185.839 160.953 142.953 1.00 118.41 ? 278  ASN   A ND2  1 
ATOM   4215 H H    . ASN   A 1 265 ? 183.104 162.727 139.589 1.00 110.88 ? 278  ASN   A H    1 
ATOM   4216 H HA   . ASN   A 1 265 ? 185.046 160.534 139.966 1.00 111.45 ? 278  ASN   A HA   1 
ATOM   4217 H HB2  . ASN   A 1 265 ? 182.763 161.014 141.929 1.00 110.07 ? 278  ASN   A HB2  1 
ATOM   4218 H HB3  . ASN   A 1 265 ? 183.888 159.663 141.946 1.00 110.22 ? 278  ASN   A HB3  1 
ATOM   4219 H HD21 . ASN   A 1 265 ? 186.103 160.063 142.556 1.00 112.49 ? 278  ASN   A HD21 1 
ATOM   4220 H HD22 . ASN   A 1 265 ? 186.474 161.479 143.537 1.00 112.41 ? 278  ASN   A HD22 1 
ATOM   4221 N N    . ALA   A 1 266 ? 183.273 158.816 139.240 1.00 89.20  ? 279  ALA   A N    1 
ATOM   4222 C CA   . ALA   A 1 266 ? 182.341 157.925 138.567 1.00 94.47  ? 279  ALA   A CA   1 
ATOM   4223 C C    . ALA   A 1 266 ? 182.405 156.493 139.100 1.00 100.75 ? 279  ALA   A C    1 
ATOM   4224 O O    . ALA   A 1 266 ? 183.389 156.099 139.719 1.00 112.60 ? 279  ALA   A O    1 
ATOM   4225 C CB   . ALA   A 1 266 ? 182.615 157.968 137.070 1.00 99.06  ? 279  ALA   A CB   1 
ATOM   4226 H H    . ALA   A 1 266 ? 184.096 158.399 139.653 1.00 103.86 ? 279  ALA   A H    1 
ATOM   4227 H HA   . ALA   A 1 266 ? 181.332 158.295 138.749 1.00 104.83 ? 279  ALA   A HA   1 
ATOM   4228 H HB1  . ALA   A 1 266 ? 181.888 157.346 136.546 1.00 104.01 ? 279  ALA   A HB1  1 
ATOM   4229 H HB2  . ALA   A 1 266 ? 182.519 158.996 136.720 1.00 104.55 ? 279  ALA   A HB2  1 
ATOM   4230 H HB3  . ALA   A 1 266 ? 183.619 157.601 136.859 1.00 104.88 ? 279  ALA   A HB3  1 
ATOM   4231 N N    . VAL   A 1 267 ? 181.357 155.707 138.867 1.00 101.66 ? 280  VAL   A N    1 
ATOM   4232 C CA   . VAL   A 1 267 ? 181.283 154.292 139.253 1.00 98.46  ? 280  VAL   A CA   1 
ATOM   4233 C C    . VAL   A 1 267 ? 180.660 153.489 138.122 1.00 108.47 ? 280  VAL   A C    1 
ATOM   4234 O O    . VAL   A 1 267 ? 179.669 153.919 137.547 1.00 120.35 ? 280  VAL   A O    1 
ATOM   4235 C CB   . VAL   A 1 267 ? 180.475 154.108 140.544 1.00 103.59 ? 280  VAL   A CB   1 
ATOM   4236 C CG1  . VAL   A 1 267 ? 180.513 152.652 141.008 1.00 117.40 ? 280  VAL   A CG1  1 
ATOM   4237 C CG2  . VAL   A 1 267 ? 181.007 154.966 141.692 1.00 102.24 ? 280  VAL   A CG2  1 
ATOM   4238 H H    . VAL   A 1 267 ? 180.577 156.102 138.361 1.00 109.00 ? 280  VAL   A H    1 
ATOM   4239 H HA   . VAL   A 1 267 ? 182.290 153.910 139.424 1.00 107.34 ? 280  VAL   A HA   1 
ATOM   4240 H HB   . VAL   A 1 267 ? 179.434 154.377 140.367 1.00 108.23 ? 280  VAL   A HB   1 
ATOM   4241 H HG11 . VAL   A 1 267 ? 180.022 152.006 140.281 1.00 110.46 ? 280  VAL   A HG11 1 
ATOM   4242 H HG12 . VAL   A 1 267 ? 179.980 152.553 141.954 1.00 110.44 ? 280  VAL   A HG12 1 
ATOM   4243 H HG13 . VAL   A 1 267 ? 181.544 152.328 141.147 1.00 109.76 ? 280  VAL   A HG13 1 
ATOM   4244 H HG21 . VAL   A 1 267 ? 180.879 156.024 141.462 1.00 108.67 ? 280  VAL   A HG21 1 
ATOM   4245 H HG22 . VAL   A 1 267 ? 180.450 154.752 142.604 1.00 108.09 ? 280  VAL   A HG22 1 
ATOM   4246 H HG23 . VAL   A 1 267 ? 182.063 154.754 141.858 1.00 107.90 ? 280  VAL   A HG23 1 
ATOM   4247 N N    . ASP   A 1 268 ? 181.200 152.321 137.795 1.00 111.02 ? 281  ASP   A N    1 
ATOM   4248 C CA   . ASP   A 1 268 ? 180.761 151.531 136.642 1.00 113.80 ? 281  ASP   A CA   1 
ATOM   4249 C C    . ASP   A 1 268 ? 179.396 150.849 136.842 1.00 110.90 ? 281  ASP   A C    1 
ATOM   4250 O O    . ASP   A 1 268 ? 179.218 149.977 137.702 1.00 90.12  ? 281  ASP   A O    1 
ATOM   4251 C CB   . ASP   A 1 268 ? 181.885 150.556 136.289 1.00 116.97 ? 281  ASP   A CB   1 
ATOM   4252 C CG   . ASP   A 1 268 ? 181.666 149.752 135.004 1.00 128.57 ? 281  ASP   A CG   1 
ATOM   4253 O OD1  . ASP   A 1 268 ? 180.561 149.772 134.422 1.00 132.04 ? 281  ASP   A OD1  1 
ATOM   4254 O OD2  . ASP   A 1 268 ? 182.620 149.070 134.580 1.00 129.30 ? 281  ASP   A OD2  1 
ATOM   4255 H H    . ASP   A 1 268 ? 181.987 151.983 138.330 1.00 115.15 ? 281  ASP   A H    1 
ATOM   4256 H HA   . ASP   A 1 268 ? 180.645 152.208 135.795 1.00 115.48 ? 281  ASP   A HA   1 
ATOM   4257 H HB2  . ASP   A 1 268 ? 182.800 151.137 136.174 1.00 115.70 ? 281  ASP   A HB2  1 
ATOM   4258 H HB3  . ASP   A 1 268 ? 182.027 149.865 137.119 1.00 115.82 ? 281  ASP   A HB3  1 
HETATM 4259 C C1   . NAG   B 2 .   ? 208.707 146.776 97.035  1.00 183.99 ? 1    NAG   B C1   1 
HETATM 4260 C C2   . NAG   B 2 .   ? 209.136 145.574 96.169  1.00 182.45 ? 1    NAG   B C2   1 
HETATM 4261 C C3   . NAG   B 2 .   ? 210.671 145.474 96.142  1.00 182.64 ? 1    NAG   B C3   1 
HETATM 4262 C C4   . NAG   B 2 .   ? 211.262 146.796 95.635  1.00 184.60 ? 1    NAG   B C4   1 
HETATM 4263 C C5   . NAG   B 2 .   ? 210.782 147.977 96.484  1.00 185.70 ? 1    NAG   B C5   1 
HETATM 4264 C C6   . NAG   B 2 .   ? 211.298 149.323 95.962  1.00 187.34 ? 1    NAG   B C6   1 
HETATM 4265 C C7   . NAG   B 2 .   ? 208.605 143.772 97.771  1.00 180.26 ? 1    NAG   B C7   1 
HETATM 4266 C C8   . NAG   B 2 .   ? 207.797 142.490 98.005  1.00 177.94 ? 1    NAG   B C8   1 
HETATM 4267 N N2   . NAG   B 2 .   ? 208.482 144.330 96.573  1.00 181.47 ? 1    NAG   B N2   1 
HETATM 4268 O O3   . NAG   B 2 .   ? 211.095 144.393 95.273  1.00 183.37 ? 1    NAG   B O3   1 
HETATM 4269 O O4   . NAG   B 2 .   ? 212.729 146.715 95.733  1.00 185.66 ? 1    NAG   B O4   1 
HETATM 4270 O O5   . NAG   B 2 .   ? 209.303 147.986 96.472  1.00 185.78 ? 1    NAG   B O5   1 
HETATM 4271 O O6   . NAG   B 2 .   ? 210.862 150.379 96.839  1.00 190.17 ? 1    NAG   B O6   1 
HETATM 4272 O O7   . NAG   B 2 .   ? 209.320 144.262 98.640  1.00 182.32 ? 1    NAG   B O7   1 
HETATM 4273 H H1   . NAG   B 2 .   ? 209.043 146.659 98.065  1.00 182.73 ? 1    NAG   B H1   1 
HETATM 4274 H H2   . NAG   B 2 .   ? 208.801 145.767 95.150  1.00 182.92 ? 1    NAG   B H2   1 
HETATM 4275 H H3   . NAG   B 2 .   ? 211.058 145.286 97.143  1.00 182.91 ? 1    NAG   B H3   1 
HETATM 4276 H H4   . NAG   B 2 .   ? 210.966 146.957 94.598  1.00 183.22 ? 1    NAG   B H4   1 
HETATM 4277 H H5   . NAG   B 2 .   ? 211.125 147.841 97.510  1.00 182.93 ? 1    NAG   B H5   1 
HETATM 4278 H H61  . NAG   B 2 .   ? 212.387 149.322 95.929  1.00 183.73 ? 1    NAG   B H61  1 
HETATM 4279 H H62  . NAG   B 2 .   ? 210.920 149.507 94.956  1.00 183.11 ? 1    NAG   B H62  1 
HETATM 4280 H H81  . NAG   B 2 .   ? 207.978 142.114 99.012  1.00 182.45 ? 1    NAG   B H81  1 
HETATM 4281 H H82  . NAG   B 2 .   ? 206.734 142.700 97.888  1.00 182.39 ? 1    NAG   B H82  1 
HETATM 4282 H H83  . NAG   B 2 .   ? 208.096 141.730 97.283  1.00 182.23 ? 1    NAG   B H83  1 
HETATM 4283 H HN2  . NAG   B 2 .   ? 207.923 143.857 95.877  1.00 182.95 ? 1    NAG   B HN2  1 
HETATM 4284 H HO3  . NAG   B 2 .   ? 211.993 144.565 94.982  1.00 183.19 ? 1    NAG   B HO3  1 
HETATM 4285 H HO6  . NAG   B 2 .   ? 211.087 151.224 96.442  1.00 183.89 ? 1    NAG   B HO6  1 
HETATM 4286 C C1   . NAG   B 2 .   ? 213.431 146.671 94.447  1.00 198.86 ? 2    NAG   B C1   1 
HETATM 4287 C C2   . NAG   B 2 .   ? 214.948 146.889 94.663  1.00 198.99 ? 2    NAG   B C2   1 
HETATM 4288 C C3   . NAG   B 2 .   ? 215.712 146.754 93.331  1.00 200.01 ? 2    NAG   B C3   1 
HETATM 4289 C C4   . NAG   B 2 .   ? 215.383 145.417 92.648  1.00 200.75 ? 2    NAG   B C4   1 
HETATM 4290 C C5   . NAG   B 2 .   ? 213.865 145.217 92.490  1.00 199.92 ? 2    NAG   B C5   1 
HETATM 4291 C C6   . NAG   B 2 .   ? 213.475 143.839 91.941  1.00 196.60 ? 2    NAG   B C6   1 
HETATM 4292 C C7   . NAG   B 2 .   ? 214.918 149.354 94.875  1.00 197.57 ? 2    NAG   B C7   1 
HETATM 4293 C C8   . NAG   B 2 .   ? 215.372 150.557 95.717  1.00 194.53 ? 2    NAG   B C8   1 
HETATM 4294 N N2   . NAG   B 2 .   ? 215.245 148.154 95.345  1.00 198.06 ? 2    NAG   B N2   1 
HETATM 4295 O O3   . NAG   B 2 .   ? 217.148 146.824 93.549  1.00 197.45 ? 2    NAG   B O3   1 
HETATM 4296 O O4   . NAG   B 2 .   ? 216.002 145.437 91.340  1.00 197.47 ? 2    NAG   B O4   1 
HETATM 4297 O O5   . NAG   B 2 .   ? 213.227 145.362 93.819  1.00 199.51 ? 2    NAG   B O5   1 
HETATM 4298 O O6   . NAG   B 2 .   ? 213.981 143.693 90.600  1.00 197.10 ? 2    NAG   B O6   1 
HETATM 4299 O O7   . NAG   B 2 .   ? 214.273 149.491 93.838  1.00 196.39 ? 2    NAG   B O7   1 
HETATM 4300 H H1   . NAG   B 2 .   ? 213.023 147.443 93.796  1.00 196.44 ? 2    NAG   B H1   1 
HETATM 4301 H H2   . NAG   B 2 .   ? 215.292 146.098 95.329  1.00 196.41 ? 2    NAG   B H2   1 
HETATM 4302 H H3   . NAG   B 2 .   ? 215.425 147.565 92.662  1.00 196.81 ? 2    NAG   B H3   1 
HETATM 4303 H H4   . NAG   B 2 .   ? 215.796 144.591 93.228  1.00 196.65 ? 2    NAG   B H4   1 
HETATM 4304 H H5   . NAG   B 2 .   ? 213.463 145.987 91.831  1.00 196.78 ? 2    NAG   B H5   1 
HETATM 4305 H H61  . NAG   B 2 .   ? 213.881 143.049 92.573  1.00 196.19 ? 2    NAG   B H61  1 
HETATM 4306 H H62  . NAG   B 2 .   ? 212.389 143.743 91.925  1.00 195.90 ? 2    NAG   B H62  1 
HETATM 4307 H H81  . NAG   B 2 .   ? 215.030 151.483 95.256  1.00 196.03 ? 2    NAG   B H81  1 
HETATM 4308 H H82  . NAG   B 2 .   ? 214.954 150.482 96.720  1.00 196.05 ? 2    NAG   B H82  1 
HETATM 4309 H H83  . NAG   B 2 .   ? 216.460 150.571 95.780  1.00 196.03 ? 2    NAG   B H83  1 
HETATM 4310 H HN2  . NAG   B 2 .   ? 215.818 148.100 96.176  1.00 196.33 ? 2    NAG   B HN2  1 
HETATM 4311 H HO3  . NAG   B 2 .   ? 217.577 146.631 92.712  1.00 196.42 ? 2    NAG   B HO3  1 
HETATM 4312 H HO4  . NAG   B 2 .   ? 215.551 144.780 90.805  1.00 196.44 ? 2    NAG   B HO4  1 
HETATM 4313 H HO6  . NAG   B 2 .   ? 213.634 142.876 90.234  1.00 196.44 ? 2    NAG   B HO6  1 
HETATM 4314 C C1   . NAG   C 2 .   ? 176.142 170.693 147.449 1.00 163.01 ? 1    NAG   C C1   1 
HETATM 4315 C C2   . NAG   C 2 .   ? 175.729 171.924 148.280 1.00 163.38 ? 1    NAG   C C2   1 
HETATM 4316 C C3   . NAG   C 2 .   ? 176.053 171.657 149.762 1.00 167.68 ? 1    NAG   C C3   1 
HETATM 4317 C C4   . NAG   C 2 .   ? 175.470 170.325 150.266 1.00 169.37 ? 1    NAG   C C4   1 
HETATM 4318 C C5   . NAG   C 2 .   ? 175.814 169.164 149.321 1.00 164.78 ? 1    NAG   C C5   1 
HETATM 4319 C C6   . NAG   C 2 .   ? 175.156 167.834 149.708 1.00 162.22 ? 1    NAG   C C6   1 
HETATM 4320 C C7   . NAG   C 2 .   ? 175.987 173.858 146.793 1.00 162.08 ? 1    NAG   C C7   1 
HETATM 4321 C C8   . NAG   C 2 .   ? 176.822 175.096 146.435 1.00 159.76 ? 1    NAG   C C8   1 
HETATM 4322 N N2   . NAG   C 2 .   ? 176.432 173.119 147.802 1.00 162.41 ? 1    NAG   C N2   1 
HETATM 4323 O O3   . NAG   C 2 .   ? 175.549 172.742 150.585 1.00 168.63 ? 1    NAG   C O3   1 
HETATM 4324 O O4   . NAG   C 2 .   ? 176.098 170.017 151.565 1.00 171.67 ? 1    NAG   C O4   1 
HETATM 4325 O O5   . NAG   C 2 .   ? 175.426 169.521 147.942 1.00 163.89 ? 1    NAG   C O5   1 
HETATM 4326 O O6   . NAG   C 2 .   ? 173.724 167.978 149.748 1.00 165.33 ? 1    NAG   C O6   1 
HETATM 4327 O O7   . NAG   C 2 .   ? 174.977 173.542 146.164 1.00 161.26 ? 1    NAG   C O7   1 
HETATM 4328 H H1   . NAG   C 2 .   ? 177.215 170.520 147.533 1.00 162.15 ? 1    NAG   C H1   1 
HETATM 4329 H H2   . NAG   C 2 .   ? 174.655 172.078 148.174 1.00 162.41 ? 1    NAG   C H2   1 
HETATM 4330 H H3   . NAG   C 2 .   ? 177.136 171.617 149.877 1.00 163.37 ? 1    NAG   C H3   1 
HETATM 4331 H H4   . NAG   C 2 .   ? 174.389 170.413 150.377 1.00 163.46 ? 1    NAG   C H4   1 
HETATM 4332 H H5   . NAG   C 2 .   ? 176.893 169.015 149.338 1.00 162.63 ? 1    NAG   C H5   1 
HETATM 4333 H H61  . NAG   C 2 .   ? 175.419 167.068 148.979 1.00 162.40 ? 1    NAG   C H61  1 
HETATM 4334 H H62  . NAG   C 2 .   ? 175.511 167.507 150.686 1.00 162.78 ? 1    NAG   C H62  1 
HETATM 4335 H H81  . NAG   C 2 .   ? 176.440 175.549 145.521 1.00 162.07 ? 1    NAG   C H81  1 
HETATM 4336 H H82  . NAG   C 2 .   ? 177.862 174.806 146.282 1.00 161.86 ? 1    NAG   C H82  1 
HETATM 4337 H H83  . NAG   C 2 .   ? 176.766 175.822 147.246 1.00 162.76 ? 1    NAG   C H83  1 
HETATM 4338 H HN2  . NAG   C 2 .   ? 177.269 173.404 148.292 1.00 162.74 ? 1    NAG   C HN2  1 
HETATM 4339 H HO3  . NAG   C 2 .   ? 175.491 172.445 151.496 1.00 163.76 ? 1    NAG   C HO3  1 
HETATM 4340 H HO6  . NAG   C 2 .   ? 173.330 167.108 149.839 1.00 163.30 ? 1    NAG   C HO6  1 
HETATM 4341 C C1   . NAG   C 2 .   ? 175.262 170.170 152.759 1.00 186.58 ? 2    NAG   C C1   1 
HETATM 4342 C C2   . NAG   C 2 .   ? 175.943 169.456 153.948 1.00 186.93 ? 2    NAG   C C2   1 
HETATM 4343 C C3   . NAG   C 2 .   ? 175.153 169.696 155.243 1.00 185.41 ? 2    NAG   C C3   1 
HETATM 4344 C C4   . NAG   C 2 .   ? 175.011 171.202 155.497 1.00 185.40 ? 2    NAG   C C4   1 
HETATM 4345 C C5   . NAG   C 2 .   ? 174.325 171.889 154.305 1.00 186.98 ? 2    NAG   C C5   1 
HETATM 4346 C C6   . NAG   C 2 .   ? 174.229 173.409 154.486 1.00 185.17 ? 2    NAG   C C6   1 
HETATM 4347 C C7   . NAG   C 2 .   ? 177.207 167.438 153.344 1.00 185.04 ? 2    NAG   C C7   1 
HETATM 4348 C C8   . NAG   C 2 .   ? 177.136 165.935 153.037 1.00 182.30 ? 2    NAG   C C8   1 
HETATM 4349 N N2   . NAG   C 2 .   ? 176.059 168.017 153.692 1.00 186.53 ? 2    NAG   C N2   1 
HETATM 4350 O O3   . NAG   C 2 .   ? 175.826 169.087 156.382 1.00 181.40 ? 2    NAG   C O3   1 
HETATM 4351 O O4   . NAG   C 2 .   ? 174.207 171.372 156.685 1.00 178.49 ? 2    NAG   C O4   1 
HETATM 4352 O O5   . NAG   C 2 .   ? 175.105 171.597 153.073 1.00 189.06 ? 2    NAG   C O5   1 
HETATM 4353 O O6   . NAG   C 2 .   ? 173.555 173.981 153.348 1.00 186.15 ? 2    NAG   C O6   1 
HETATM 4354 O O7   . NAG   C 2 .   ? 178.262 168.065 153.276 1.00 184.22 ? 2    NAG   C O7   1 
HETATM 4355 H H1   . NAG   C 2 .   ? 174.284 169.726 152.572 1.00 183.14 ? 2    NAG   C H1   1 
HETATM 4356 H H2   . NAG   C 2 .   ? 176.937 169.887 154.075 1.00 183.66 ? 2    NAG   C H2   1 
HETATM 4357 H H3   . NAG   C 2 .   ? 174.163 169.249 155.145 1.00 183.44 ? 2    NAG   C H3   1 
HETATM 4358 H H4   . NAG   C 2 .   ? 175.993 171.644 155.664 1.00 183.58 ? 2    NAG   C H4   1 
HETATM 4359 H H5   . NAG   C 2 .   ? 173.321 171.482 154.185 1.00 183.66 ? 2    NAG   C H5   1 
HETATM 4360 H H61  . NAG   C 2 .   ? 173.668 173.652 155.388 1.00 183.25 ? 2    NAG   C H61  1 
HETATM 4361 H H62  . NAG   C 2 .   ? 175.225 173.842 154.570 1.00 183.62 ? 2    NAG   C H62  1 
HETATM 4362 H H81  . NAG   C 2 .   ? 178.114 165.575 152.718 1.00 183.09 ? 2    NAG   C H81  1 
HETATM 4363 H H82  . NAG   C 2 .   ? 176.413 165.756 152.241 1.00 182.92 ? 2    NAG   C H82  1 
HETATM 4364 H H83  . NAG   C 2 .   ? 176.829 165.393 153.931 1.00 183.44 ? 2    NAG   C H83  1 
HETATM 4365 H HN2  . NAG   C 2 .   ? 175.217 167.460 153.702 1.00 183.38 ? 2    NAG   C HN2  1 
HETATM 4366 H HO3  . NAG   C 2 .   ? 175.975 168.157 156.198 1.00 183.12 ? 2    NAG   C HO3  1 
HETATM 4367 H HO4  . NAG   C 2 .   ? 174.568 170.778 157.347 1.00 182.60 ? 2    NAG   C HO4  1 
HETATM 4368 H HO6  . NAG   C 2 .   ? 173.512 174.933 153.467 1.00 183.81 ? 2    NAG   C HO6  1 
HETATM 4369 C C1   . NAG   D 3 .   ? 194.819 152.406 94.985  1.00 138.58 ? 1    NAG   D C1   1 
HETATM 4370 C C2   . NAG   D 3 .   ? 195.736 153.095 93.960  1.00 136.97 ? 1    NAG   D C2   1 
HETATM 4371 C C3   . NAG   D 3 .   ? 196.395 152.037 93.059  1.00 139.55 ? 1    NAG   D C3   1 
HETATM 4372 C C4   . NAG   D 3 .   ? 197.071 150.935 93.883  1.00 140.20 ? 1    NAG   D C4   1 
HETATM 4373 C C5   . NAG   D 3 .   ? 196.092 150.316 94.879  1.00 137.74 ? 1    NAG   D C5   1 
HETATM 4374 C C6   . NAG   D 3 .   ? 196.741 149.275 95.795  1.00 140.81 ? 1    NAG   D C6   1 
HETATM 4375 C C7   . NAG   D 3 .   ? 195.263 155.307 93.015  1.00 139.39 ? 1    NAG   D C7   1 
HETATM 4376 C C8   . NAG   D 3 .   ? 194.262 156.160 92.226  1.00 137.75 ? 1    NAG   D C8   1 
HETATM 4377 N N2   . NAG   D 3 .   ? 194.942 154.028 93.163  1.00 135.68 ? 1    NAG   D N2   1 
HETATM 4378 O O3   . NAG   D 3 .   ? 197.385 152.655 92.197  1.00 140.32 ? 1    NAG   D O3   1 
HETATM 4379 O O4   . NAG   D 3 .   ? 197.507 149.875 92.962  1.00 143.72 ? 1    NAG   D O4   1 
HETATM 4380 O O5   . NAG   D 3 .   ? 195.565 151.399 95.720  1.00 137.24 ? 1    NAG   D O5   1 
HETATM 4381 O O6   . NAG   D 3 .   ? 195.736 148.700 96.641  1.00 142.20 ? 1    NAG   D O6   1 
HETATM 4382 O O7   . NAG   D 3 .   ? 196.291 155.780 93.491  1.00 139.53 ? 1    NAG   D O7   1 
HETATM 4383 H H1   . NAG   D 3 .   ? 193.979 151.931 94.478  1.00 138.80 ? 1    NAG   D H1   1 
HETATM 4384 H H2   . NAG   D 3 .   ? 196.518 153.628 94.502  1.00 138.84 ? 1    NAG   D H2   1 
HETATM 4385 H H3   . NAG   D 3 .   ? 195.631 151.578 92.433  1.00 138.95 ? 1    NAG   D H3   1 
HETATM 4386 H H4   . NAG   D 3 .   ? 197.928 151.343 94.420  1.00 139.15 ? 1    NAG   D H4   1 
HETATM 4387 H H5   . NAG   D 3 .   ? 195.269 149.853 94.334  1.00 138.73 ? 1    NAG   D H5   1 
HETATM 4388 H H61  . NAG   D 3 .   ? 197.209 148.483 95.210  1.00 139.33 ? 1    NAG   D H61  1 
HETATM 4389 H H62  . NAG   D 3 .   ? 197.505 149.744 96.416  1.00 139.64 ? 1    NAG   D H62  1 
HETATM 4390 H H81  . NAG   D 3 .   ? 194.623 157.186 92.154  1.00 139.00 ? 1    NAG   D H81  1 
HETATM 4391 H H82  . NAG   D 3 .   ? 194.144 155.752 91.222  1.00 139.21 ? 1    NAG   D H82  1 
HETATM 4392 H H83  . NAG   D 3 .   ? 193.297 156.156 92.733  1.00 138.30 ? 1    NAG   D H83  1 
HETATM 4393 H HN2  . NAG   D 3 .   ? 194.101 153.684 92.723  1.00 138.39 ? 1    NAG   D HN2  1 
HETATM 4394 H HO3  . NAG   D 3 .   ? 197.974 151.977 91.858  1.00 139.37 ? 1    NAG   D HO3  1 
HETATM 4395 H HO6  . NAG   D 3 .   ? 196.180 148.292 97.388  1.00 140.08 ? 1    NAG   D HO6  1 
HETATM 4396 C C1   . NAG   D 3 .   ? 198.952 149.727 92.789  1.00 163.22 ? 2    NAG   D C1   1 
HETATM 4397 C C2   . NAG   D 3 .   ? 199.258 148.374 92.126  1.00 161.71 ? 2    NAG   D C2   1 
HETATM 4398 C C3   . NAG   D 3 .   ? 200.768 148.231 91.872  1.00 162.68 ? 2    NAG   D C3   1 
HETATM 4399 C C4   . NAG   D 3 .   ? 201.257 149.387 90.973  1.00 164.89 ? 2    NAG   D C4   1 
HETATM 4400 C C5   . NAG   D 3 .   ? 200.919 150.719 91.664  1.00 164.57 ? 2    NAG   D C5   1 
HETATM 4401 C C6   . NAG   D 3 .   ? 201.349 151.967 90.884  1.00 161.77 ? 2    NAG   D C6   1 
HETATM 4402 C C7   . NAG   D 3 .   ? 197.605 146.687 92.755  1.00 162.64 ? 2    NAG   D C7   1 
HETATM 4403 C C8   . NAG   D 3 .   ? 197.180 145.641 93.790  1.00 161.22 ? 2    NAG   D C8   1 
HETATM 4404 N N2   . NAG   D 3 .   ? 198.777 147.280 92.971  1.00 162.23 ? 2    NAG   D N2   1 
HETATM 4405 O O3   . NAG   D 3 .   ? 201.022 146.938 91.262  1.00 161.75 ? 2    NAG   D O3   1 
HETATM 4406 O O4   . NAG   D 3 .   ? 202.729 149.398 90.789  1.00 166.33 ? 2    NAG   D O4   1 
HETATM 4407 O O5   . NAG   D 3 .   ? 199.465 150.799 91.940  1.00 165.32 ? 2    NAG   D O5   1 
HETATM 4408 O O6   . NAG   D 3 .   ? 200.637 152.035 89.637  1.00 165.50 ? 2    NAG   D O6   1 
HETATM 4409 O O7   . NAG   D 3 .   ? 196.907 146.958 91.780  1.00 160.17 ? 2    NAG   D O7   1 
HETATM 4410 H H1   . NAG   D 3 .   ? 199.432 149.772 93.766  1.00 161.19 ? 2    NAG   D H1   1 
HETATM 4411 H H2   . NAG   D 3 .   ? 198.750 148.343 91.162  1.00 161.29 ? 2    NAG   D H2   1 
HETATM 4412 H H3   . NAG   D 3 .   ? 201.297 148.271 92.824  1.00 162.00 ? 2    NAG   D H3   1 
HETATM 4413 H H4   . NAG   D 3 .   ? 200.770 149.332 89.999  1.00 162.06 ? 2    NAG   D H4   1 
HETATM 4414 H H5   . NAG   D 3 .   ? 201.442 150.742 92.620  1.00 161.92 ? 2    NAG   D H5   1 
HETATM 4415 H H61  . NAG   D 3 .   ? 201.124 152.858 91.470  1.00 161.33 ? 2    NAG   D H61  1 
HETATM 4416 H H62  . NAG   D 3 .   ? 202.422 151.953 90.690  1.00 161.83 ? 2    NAG   D H62  1 
HETATM 4417 H H81  . NAG   D 3 .   ? 196.159 145.316 93.592  1.00 161.47 ? 2    NAG   D H81  1 
HETATM 4418 H H82  . NAG   D 3 .   ? 197.229 146.071 94.791  1.00 161.19 ? 2    NAG   D H82  1 
HETATM 4419 H H83  . NAG   D 3 .   ? 197.847 144.780 93.734  1.00 161.94 ? 2    NAG   D H83  1 
HETATM 4420 H HN2  . NAG   D 3 .   ? 199.289 147.047 93.810  1.00 161.59 ? 2    NAG   D HN2  1 
HETATM 4421 H HO3  . NAG   D 3 .   ? 200.604 146.254 91.791  1.00 162.03 ? 2    NAG   D HO3  1 
HETATM 4422 H HO6  . NAG   D 3 .   ? 200.900 152.835 89.177  1.00 162.39 ? 2    NAG   D HO6  1 
HETATM 4423 C C1   . BMA   D 3 .   ? 203.473 148.253 90.245  1.00 200.86 ? 3    BMA   D C1   1 
HETATM 4424 C C2   . BMA   D 3 .   ? 202.922 147.712 88.902  1.00 199.74 ? 3    BMA   D C2   1 
HETATM 4425 C C3   . BMA   D 3 .   ? 203.800 146.512 88.517  1.00 201.75 ? 3    BMA   D C3   1 
HETATM 4426 C C4   . BMA   D 3 .   ? 205.258 146.947 88.323  1.00 202.25 ? 3    BMA   D C4   1 
HETATM 4427 C C5   . BMA   D 3 .   ? 205.777 147.554 89.627  1.00 203.81 ? 3    BMA   D C5   1 
HETATM 4428 C C6   . BMA   D 3 .   ? 207.192 148.098 89.459  1.00 202.67 ? 3    BMA   D C6   1 
HETATM 4429 O O2   . BMA   D 3 .   ? 202.991 148.720 87.863  1.00 196.73 ? 3    BMA   D O2   1 
HETATM 4430 O O3   . BMA   D 3 .   ? 203.307 145.854 87.287  1.00 203.02 ? 3    BMA   D O3   1 
HETATM 4431 O O4   . BMA   D 3 .   ? 206.068 145.793 88.001  1.00 200.11 ? 3    BMA   D O4   1 
HETATM 4432 O O5   . BMA   D 3 .   ? 204.873 148.652 90.041  1.00 201.75 ? 3    BMA   D O5   1 
HETATM 4433 O O6   . BMA   D 3 .   ? 207.532 148.864 90.659  1.00 205.61 ? 3    BMA   D O6   1 
HETATM 4434 H H1   . BMA   D 3 .   ? 203.461 147.462 90.994  1.00 200.22 ? 3    BMA   D H1   1 
HETATM 4435 H H2   . BMA   D 3 .   ? 201.886 147.388 89.003  1.00 199.83 ? 3    BMA   D H2   1 
HETATM 4436 H H3   . BMA   D 3 .   ? 203.770 145.799 89.341  1.00 200.63 ? 3    BMA   D H3   1 
HETATM 4437 H H4   . BMA   D 3 .   ? 205.338 147.671 87.514  1.00 200.66 ? 3    BMA   D H4   1 
HETATM 4438 H H5   . BMA   D 3 .   ? 205.782 146.798 90.411  1.00 201.17 ? 3    BMA   D H5   1 
HETATM 4439 H H61  . BMA   D 3 .   ? 207.901 147.280 89.334  1.00 200.90 ? 3    BMA   D H61  1 
HETATM 4440 H H62  . BMA   D 3 .   ? 207.243 148.744 88.583  1.00 200.62 ? 3    BMA   D H62  1 
HETATM 4441 H HO2  . BMA   D 3 .   ? 202.591 148.378 87.060  1.00 200.06 ? 3    BMA   D HO2  1 
HETATM 4442 H HO4  . BMA   D 3 .   ? 205.956 145.590 87.070  1.00 200.70 ? 3    BMA   D HO4  1 
HETATM 4443 C C1   . MAN   D 3 .   ? 202.339 144.768 87.506  1.00 209.29 ? 4    MAN   D C1   1 
HETATM 4444 C C2   . MAN   D 3 .   ? 203.006 143.507 88.117  1.00 206.81 ? 4    MAN   D C2   1 
HETATM 4445 C C3   . MAN   D 3 .   ? 203.947 142.866 87.085  1.00 207.98 ? 4    MAN   D C3   1 
HETATM 4446 C C4   . MAN   D 3 .   ? 203.190 142.484 85.803  1.00 212.09 ? 4    MAN   D C4   1 
HETATM 4447 C C5   . MAN   D 3 .   ? 202.546 143.751 85.204  1.00 212.55 ? 4    MAN   D C5   1 
HETATM 4448 C C6   . MAN   D 3 .   ? 201.682 143.445 83.969  1.00 207.56 ? 4    MAN   D C6   1 
HETATM 4449 O O2   . MAN   D 3 .   ? 201.970 142.557 88.499  1.00 203.61 ? 4    MAN   D O2   1 
HETATM 4450 O O3   . MAN   D 3 .   ? 204.596 141.697 87.650  1.00 201.21 ? 4    MAN   D O3   1 
HETATM 4451 O O4   . MAN   D 3 .   ? 204.152 141.915 84.871  1.00 208.86 ? 4    MAN   D O4   1 
HETATM 4452 O O5   . MAN   D 3 .   ? 201.694 144.418 86.229  1.00 212.30 ? 4    MAN   D O5   1 
HETATM 4453 O O6   . MAN   D 3 .   ? 201.221 144.675 83.370  1.00 204.73 ? 4    MAN   D O6   1 
HETATM 4454 H H1   . MAN   D 3 .   ? 201.565 145.131 88.183  1.00 206.72 ? 4    MAN   D H1   1 
HETATM 4455 H H2   . MAN   D 3 .   ? 203.576 143.765 89.010  1.00 206.43 ? 4    MAN   D H2   1 
HETATM 4456 H H3   . MAN   D 3 .   ? 204.725 143.584 86.828  1.00 206.97 ? 4    MAN   D H3   1 
HETATM 4457 H H4   . MAN   D 3 .   ? 202.424 141.739 86.021  1.00 207.55 ? 4    MAN   D H4   1 
HETATM 4458 H H5   . MAN   D 3 .   ? 203.338 144.441 84.913  1.00 207.56 ? 4    MAN   D H5   1 
HETATM 4459 H H61  . MAN   D 3 .   ? 202.260 142.893 83.228  1.00 206.79 ? 4    MAN   D H61  1 
HETATM 4460 H H62  . MAN   D 3 .   ? 200.821 142.839 84.253  1.00 206.99 ? 4    MAN   D H62  1 
HETATM 4461 H HO2  . MAN   D 3 .   ? 201.541 142.847 89.308  1.00 206.39 ? 4    MAN   D HO2  1 
HETATM 4462 H HO3  . MAN   D 3 .   ? 205.046 141.249 86.930  1.00 206.48 ? 4    MAN   D HO3  1 
HETATM 4463 H HO4  . MAN   D 3 .   ? 203.691 141.405 84.201  1.00 206.84 ? 4    MAN   D HO4  1 
HETATM 4464 H HO6  . MAN   D 3 .   ? 200.639 144.461 82.637  1.00 206.70 ? 4    MAN   D HO6  1 
HETATM 4465 C C1   . MAN   D 3 .   ? 208.914 149.323 90.689  1.00 219.41 ? 5    MAN   D C1   1 
HETATM 4466 C C2   . MAN   D 3 .   ? 209.104 150.165 91.967  1.00 219.25 ? 5    MAN   D C2   1 
HETATM 4467 C C3   . MAN   D 3 .   ? 208.239 151.439 91.864  1.00 221.06 ? 5    MAN   D C3   1 
HETATM 4468 C C4   . MAN   D 3 .   ? 208.550 152.245 90.593  1.00 221.60 ? 5    MAN   D C4   1 
HETATM 4469 C C5   . MAN   D 3 .   ? 208.406 151.367 89.340  1.00 220.16 ? 5    MAN   D C5   1 
HETATM 4470 C C6   . MAN   D 3 .   ? 208.848 152.083 88.056  1.00 215.71 ? 5    MAN   D C6   1 
HETATM 4471 O O2   . MAN   D 3 .   ? 210.508 150.515 92.127  1.00 217.37 ? 5    MAN   D O2   1 
HETATM 4472 O O3   . MAN   D 3 .   ? 208.423 152.294 93.027  1.00 218.81 ? 5    MAN   D O3   1 
HETATM 4473 O O4   . MAN   D 3 .   ? 207.601 153.337 90.524  1.00 218.82 ? 5    MAN   D O4   1 
HETATM 4474 O O5   . MAN   D 3 .   ? 209.219 150.133 89.500  1.00 219.52 ? 5    MAN   D O5   1 
HETATM 4475 O O6   . MAN   D 3 .   ? 208.578 151.244 86.912  1.00 212.86 ? 5    MAN   D O6   1 
HETATM 4476 H H1   . MAN   D 3 .   ? 209.574 148.456 90.717  1.00 217.25 ? 5    MAN   D H1   1 
HETATM 4477 H H2   . MAN   D 3 .   ? 208.791 149.579 92.831  1.00 216.95 ? 5    MAN   D H2   1 
HETATM 4478 H H3   . MAN   D 3 .   ? 207.191 151.139 91.838  1.00 217.51 ? 5    MAN   D H3   1 
HETATM 4479 H H4   . MAN   D 3 .   ? 209.560 152.652 90.646  1.00 217.91 ? 5    MAN   D H4   1 
HETATM 4480 H H5   . MAN   D 3 .   ? 207.360 151.082 89.234  1.00 217.40 ? 5    MAN   D H5   1 
HETATM 4481 H H61  . MAN   D 3 .   ? 208.306 153.022 87.938  1.00 216.87 ? 5    MAN   D H61  1 
HETATM 4482 H H62  . MAN   D 3 .   ? 209.914 152.305 88.097  1.00 216.94 ? 5    MAN   D H62  1 
HETATM 4483 H HO2  . MAN   D 3 .   ? 211.064 149.745 91.992  1.00 216.71 ? 5    MAN   D HO2  1 
HETATM 4484 H HO3  . MAN   D 3 .   ? 208.276 151.782 93.826  1.00 217.18 ? 5    MAN   D HO3  1 
HETATM 4485 H HO4  . MAN   D 3 .   ? 207.593 153.742 91.394  1.00 217.37 ? 5    MAN   D HO4  1 
HETATM 4486 H HO6  . MAN   D 3 .   ? 208.914 151.681 86.127  1.00 216.67 ? 5    MAN   D HO6  1 
HETATM 4487 C C1   . NAG   E 4 .   ? 195.897 171.790 109.369 1.00 162.11 ? 1    NAG   E C1   1 
HETATM 4488 C C2   . NAG   E 4 .   ? 195.987 172.793 108.204 1.00 163.61 ? 1    NAG   E C2   1 
HETATM 4489 C C3   . NAG   E 4 .   ? 197.035 172.306 107.189 1.00 163.43 ? 1    NAG   E C3   1 
HETATM 4490 C C4   . NAG   E 4 .   ? 198.374 172.015 107.885 1.00 162.90 ? 1    NAG   E C4   1 
HETATM 4491 C C5   . NAG   E 4 .   ? 198.221 171.110 109.112 1.00 160.44 ? 1    NAG   E C5   1 
HETATM 4492 C C6   . NAG   E 4 .   ? 199.521 170.940 109.902 1.00 160.73 ? 1    NAG   E C6   1 
HETATM 4493 C C7   . NAG   E 4 .   ? 193.867 172.147 107.095 1.00 162.26 ? 1    NAG   E C7   1 
HETATM 4494 C C8   . NAG   E 4 .   ? 192.499 172.644 106.609 1.00 159.43 ? 1    NAG   E C8   1 
HETATM 4495 N N2   . NAG   E 4 .   ? 194.678 173.071 107.598 1.00 163.47 ? 1    NAG   E N2   1 
HETATM 4496 O O3   . NAG   E 4 .   ? 197.243 173.318 106.168 1.00 164.74 ? 1    NAG   E O3   1 
HETATM 4497 O O4   . NAG   E 4 .   ? 199.244 171.317 106.922 1.00 163.01 ? 1    NAG   E O4   1 
HETATM 4498 O O5   . NAG   E 4 .   ? 197.199 171.682 110.005 1.00 161.48 ? 1    NAG   E O5   1 
HETATM 4499 O O6   . NAG   E 4 .   ? 200.009 172.230 110.317 1.00 163.33 ? 1    NAG   E O6   1 
HETATM 4500 O O7   . NAG   E 4 .   ? 194.183 170.964 107.037 1.00 160.04 ? 1    NAG   E O7   1 
HETATM 4501 H H1   . NAG   E 4 .   ? 195.602 170.805 109.007 1.00 160.18 ? 1    NAG   E H1   1 
HETATM 4502 H H2   . NAG   E 4 .   ? 196.337 173.740 108.614 1.00 160.87 ? 1    NAG   E H2   1 
HETATM 4503 H H3   . NAG   E 4 .   ? 196.690 171.391 106.708 1.00 160.87 ? 1    NAG   E H3   1 
HETATM 4504 H H4   . NAG   E 4 .   ? 198.825 172.961 108.184 1.00 161.38 ? 1    NAG   E H4   1 
HETATM 4505 H H5   . NAG   E 4 .   ? 197.882 170.126 108.789 1.00 160.29 ? 1    NAG   E H5   1 
HETATM 4506 H H61  . NAG   E 4 .   ? 199.341 170.324 110.783 1.00 159.96 ? 1    NAG   E H61  1 
HETATM 4507 H H62  . NAG   E 4 .   ? 200.274 170.446 109.288 1.00 160.88 ? 1    NAG   E H62  1 
HETATM 4508 H H81  . NAG   E 4 .   ? 191.964 171.835 106.111 1.00 160.42 ? 1    NAG   E H81  1 
HETATM 4509 H H82  . NAG   E 4 .   ? 192.633 173.467 105.907 1.00 161.00 ? 1    NAG   E H82  1 
HETATM 4510 H H83  . NAG   E 4 .   ? 191.912 172.989 107.461 1.00 160.28 ? 1    NAG   E H83  1 
HETATM 4511 H HN2  . NAG   E 4 .   ? 194.400 174.041 107.544 1.00 160.83 ? 1    NAG   E HN2  1 
HETATM 4512 H HO3  . NAG   E 4 .   ? 198.098 173.168 105.757 1.00 161.47 ? 1    NAG   E HO3  1 
HETATM 4513 H HO6  . NAG   E 4 .   ? 200.817 172.111 110.821 1.00 160.93 ? 1    NAG   E HO6  1 
HETATM 4514 C C1   . NAG   E 4 .   ? 200.403 172.099 106.489 1.00 191.87 ? 2    NAG   E C1   1 
HETATM 4515 C C2   . NAG   E 4 .   ? 201.371 171.212 105.672 1.00 193.03 ? 2    NAG   E C2   1 
HETATM 4516 C C3   . NAG   E 4 .   ? 202.553 172.051 105.149 1.00 195.62 ? 2    NAG   E C3   1 
HETATM 4517 C C4   . NAG   E 4 .   ? 202.030 173.227 104.317 1.00 197.05 ? 2    NAG   E C4   1 
HETATM 4518 C C5   . NAG   E 4 .   ? 201.023 174.071 105.111 1.00 192.42 ? 2    NAG   E C5   1 
HETATM 4519 C C6   . NAG   E 4 .   ? 200.384 175.184 104.272 1.00 191.38 ? 2    NAG   E C6   1 
HETATM 4520 C C7   . NAG   E 4 .   ? 202.493 170.052 107.542 1.00 192.26 ? 2    NAG   E C7   1 
HETATM 4521 C C8   . NAG   E 4 .   ? 202.887 168.691 108.133 1.00 188.73 ? 2    NAG   E C8   1 
HETATM 4522 N N2   . NAG   E 4 .   ? 201.813 170.020 106.402 1.00 192.65 ? 2    NAG   E N2   1 
HETATM 4523 O O3   . NAG   E 4 .   ? 203.437 171.235 104.334 1.00 193.94 ? 2    NAG   E O3   1 
HETATM 4524 O O4   . NAG   E 4 .   ? 203.172 174.095 103.964 1.00 199.48 ? 2    NAG   E O4   1 
HETATM 4525 O O5   . NAG   E 4 .   ? 199.947 173.200 105.637 1.00 192.98 ? 2    NAG   E O5   1 
HETATM 4526 O O6   . NAG   E 4 .   ? 199.678 174.605 103.157 1.00 193.60 ? 2    NAG   E O6   1 
HETATM 4527 O O7   . NAG   E 4 .   ? 202.778 171.111 108.096 1.00 191.87 ? 2    NAG   E O7   1 
HETATM 4528 H H1   . NAG   E 4 .   ? 200.905 172.508 107.366 1.00 190.77 ? 2    NAG   E H1   1 
HETATM 4529 H H2   . NAG   E 4 .   ? 200.818 170.844 104.808 1.00 191.38 ? 2    NAG   E H2   1 
HETATM 4530 H H3   . NAG   E 4 .   ? 203.128 172.451 105.984 1.00 191.86 ? 2    NAG   E H3   1 
HETATM 4531 H H4   . NAG   E 4 .   ? 201.556 172.843 103.413 1.00 192.18 ? 2    NAG   E H4   1 
HETATM 4532 H H5   . NAG   E 4 .   ? 201.537 174.529 105.957 1.00 191.28 ? 2    NAG   E H5   1 
HETATM 4533 H H61  . NAG   E 4 .   ? 199.684 175.751 104.884 1.00 191.18 ? 2    NAG   E H61  1 
HETATM 4534 H H62  . NAG   E 4 .   ? 201.147 175.869 103.901 1.00 191.55 ? 2    NAG   E H62  1 
HETATM 4535 H H81  . NAG   E 4 .   ? 203.288 168.823 109.137 1.00 190.00 ? 2    NAG   E H81  1 
HETATM 4536 H H82  . NAG   E 4 .   ? 202.011 168.043 108.181 1.00 190.25 ? 2    NAG   E H82  1 
HETATM 4537 H H83  . NAG   E 4 .   ? 203.645 168.225 107.504 1.00 190.97 ? 2    NAG   E H83  1 
HETATM 4538 H HN2  . NAG   E 4 .   ? 201.615 169.125 105.977 1.00 191.47 ? 2    NAG   E HN2  1 
HETATM 4539 H HO3  . NAG   E 4 .   ? 203.950 171.809 103.760 1.00 191.96 ? 2    NAG   E HO3  1 
HETATM 4540 H HO6  . NAG   E 4 .   ? 199.197 175.301 102.704 1.00 191.84 ? 2    NAG   E HO6  1 
HETATM 4541 C C1   . BMA   E 4 .   ? 203.513 174.095 102.539 1.00 217.22 ? 3    BMA   E C1   1 
HETATM 4542 C C2   . BMA   E 4 .   ? 204.442 175.289 102.259 1.00 215.15 ? 3    BMA   E C2   1 
HETATM 4543 C C3   . BMA   E 4 .   ? 204.902 175.233 100.794 1.00 215.16 ? 3    BMA   E C3   1 
HETATM 4544 C C4   . BMA   E 4 .   ? 205.621 173.910 100.478 1.00 216.60 ? 3    BMA   E C4   1 
HETATM 4545 C C5   . BMA   E 4 .   ? 204.696 172.723 100.810 1.00 216.09 ? 3    BMA   E C5   1 
HETATM 4546 C C6   . BMA   E 4 .   ? 205.357 171.347 100.654 1.00 212.60 ? 3    BMA   E C6   1 
HETATM 4547 O O2   . BMA   E 4 .   ? 205.577 175.213 103.160 1.00 213.58 ? 3    BMA   E O2   1 
HETATM 4548 O O3   . BMA   E 4 .   ? 205.762 176.362 100.486 1.00 211.44 ? 3    BMA   E O3   1 
HETATM 4549 O O4   . BMA   E 4 .   ? 205.927 173.905 99.058  1.00 214.08 ? 3    BMA   E O4   1 
HETATM 4550 O O5   . BMA   E 4 .   ? 204.203 172.844 102.203 1.00 219.33 ? 3    BMA   E O5   1 
HETATM 4551 O O6   . BMA   E 4 .   ? 206.481 171.232 101.548 1.00 211.35 ? 3    BMA   E O6   1 
HETATM 4552 H H1   . BMA   E 4 .   ? 202.603 174.187 101.947 1.00 212.98 ? 3    BMA   E H1   1 
HETATM 4553 H H2   . BMA   E 4 .   ? 203.903 176.218 102.445 1.00 212.80 ? 3    BMA   E H2   1 
HETATM 4554 H H3   . BMA   E 4 .   ? 204.019 175.307 100.159 1.00 213.09 ? 3    BMA   E H3   1 
HETATM 4555 H H4   . BMA   E 4 .   ? 206.549 173.845 101.047 1.00 213.44 ? 3    BMA   E H4   1 
HETATM 4556 H H5   . BMA   E 4 .   ? 203.832 172.760 100.146 1.00 213.06 ? 3    BMA   E H5   1 
HETATM 4557 H H61  . BMA   E 4 .   ? 204.634 170.566 100.891 1.00 212.56 ? 3    BMA   E H61  1 
HETATM 4558 H H62  . BMA   E 4 .   ? 205.693 171.197 99.628  1.00 212.85 ? 3    BMA   E H62  1 
HETATM 4559 H HO2  . BMA   E 4 .   ? 205.233 175.029 104.038 1.00 212.88 ? 3    BMA   E HO2  1 
HETATM 4560 H HO3  . BMA   E 4 .   ? 206.125 176.206 99.611  1.00 212.76 ? 3    BMA   E HO3  1 
HETATM 4561 H HO4  . BMA   E 4 .   ? 206.595 173.237 98.888  1.00 213.10 ? 3    BMA   E HO4  1 
HETATM 4562 H HO6  . BMA   E 4 .   ? 206.805 170.329 101.519 1.00 212.51 ? 3    BMA   E HO6  1 
HETATM 4563 C C1   . NAG   F 2 .   ? 198.184 174.584 129.407 1.00 165.58 ? 1    NAG   F C1   1 
HETATM 4564 C C2   . NAG   F 2 .   ? 197.317 175.601 130.177 1.00 164.40 ? 1    NAG   F C2   1 
HETATM 4565 C C3   . NAG   F 2 .   ? 198.091 176.115 131.400 1.00 168.08 ? 1    NAG   F C3   1 
HETATM 4566 C C4   . NAG   F 2 .   ? 198.527 174.941 132.290 1.00 171.97 ? 1    NAG   F C4   1 
HETATM 4567 C C5   . NAG   F 2 .   ? 199.356 173.931 131.490 1.00 167.91 ? 1    NAG   F C5   1 
HETATM 4568 C C6   . NAG   F 2 .   ? 199.764 172.691 132.297 1.00 165.94 ? 1    NAG   F C6   1 
HETATM 4569 C C7   . NAG   F 2 .   ? 195.867 176.646 128.505 1.00 167.34 ? 1    NAG   F C7   1 
HETATM 4570 C C8   . NAG   F 2 .   ? 195.592 177.883 127.642 1.00 165.19 ? 1    NAG   F C8   1 
HETATM 4571 N N2   . NAG   F 2 .   ? 196.930 176.706 129.300 1.00 164.65 ? 1    NAG   F N2   1 
HETATM 4572 O O3   . NAG   F 2 .   ? 197.262 177.035 132.158 1.00 168.59 ? 1    NAG   F O3   1 
HETATM 4573 O O4   . NAG   F 2 .   ? 199.394 175.458 133.366 1.00 177.27 ? 1    NAG   F O4   1 
HETATM 4574 O O5   . NAG   F 2 .   ? 198.600 173.503 130.297 1.00 165.29 ? 1    NAG   F O5   1 
HETATM 4575 O O6   . NAG   F 2 .   ? 198.596 171.997 132.774 1.00 165.88 ? 1    NAG   F O6   1 
HETATM 4576 O O7   . NAG   F 2 .   ? 195.162 175.638 128.451 1.00 167.24 ? 1    NAG   F O7   1 
HETATM 4577 H H1   . NAG   F 2 .   ? 199.069 175.069 128.994 1.00 165.28 ? 1    NAG   F H1   1 
HETATM 4578 H H2   . NAG   F 2 .   ? 196.416 175.096 130.527 1.00 165.41 ? 1    NAG   F H2   1 
HETATM 4579 H H3   . NAG   F 2 .   ? 198.979 176.650 131.065 1.00 166.11 ? 1    NAG   F H3   1 
HETATM 4580 H H4   . NAG   F 2 .   ? 197.649 174.452 132.713 1.00 166.56 ? 1    NAG   F H4   1 
HETATM 4581 H H5   . NAG   F 2 .   ? 200.267 174.425 131.151 1.00 165.94 ? 1    NAG   F H5   1 
HETATM 4582 H H61  . NAG   F 2 .   ? 200.346 172.020 131.665 1.00 165.02 ? 1    NAG   F H61  1 
HETATM 4583 H H62  . NAG   F 2 .   ? 200.383 172.981 133.146 1.00 166.16 ? 1    NAG   F H62  1 
HETATM 4584 H H81  . NAG   F 2 .   ? 194.700 177.722 127.036 1.00 166.10 ? 1    NAG   F H81  1 
HETATM 4585 H H82  . NAG   F 2 .   ? 195.435 178.751 128.283 1.00 165.98 ? 1    NAG   F H82  1 
HETATM 4586 H H83  . NAG   F 2 .   ? 196.441 178.068 126.984 1.00 165.65 ? 1    NAG   F H83  1 
HETATM 4587 H HN2  . NAG   F 2 .   ? 197.488 177.548 129.316 1.00 165.48 ? 1    NAG   F HN2  1 
HETATM 4588 H HO3  . NAG   F 2 .   ? 197.545 177.040 133.075 1.00 166.63 ? 1    NAG   F HO3  1 
HETATM 4589 H HO6  . NAG   F 2 .   ? 198.870 171.220 133.266 1.00 165.75 ? 1    NAG   F HO6  1 
HETATM 4590 C C1   . NAG   F 2 .   ? 198.795 175.492 134.704 1.00 205.98 ? 2    NAG   F C1   1 
HETATM 4591 C C2   . NAG   F 2 .   ? 199.906 175.617 135.768 1.00 205.55 ? 2    NAG   F C2   1 
HETATM 4592 C C3   . NAG   F 2 .   ? 199.277 175.743 137.165 1.00 205.03 ? 2    NAG   F C3   1 
HETATM 4593 C C4   . NAG   F 2 .   ? 198.310 176.934 137.211 1.00 204.92 ? 2    NAG   F C4   1 
HETATM 4594 C C5   . NAG   F 2 .   ? 197.229 176.821 136.124 1.00 204.43 ? 2    NAG   F C5   1 
HETATM 4595 C C6   . NAG   F 2 .   ? 196.337 178.069 136.068 1.00 200.66 ? 2    NAG   F C6   1 
HETATM 4596 C C7   . NAG   F 2 .   ? 202.023 174.509 135.202 1.00 200.23 ? 2    NAG   F C7   1 
HETATM 4597 C C8   . NAG   F 2 .   ? 202.820 173.196 135.220 1.00 199.05 ? 2    NAG   F C8   1 
HETATM 4598 N N2   . NAG   F 2 .   ? 200.802 174.455 135.727 1.00 203.19 ? 2    NAG   F N2   1 
HETATM 4599 O O3   . NAG   F 2 .   ? 200.306 175.936 138.178 1.00 202.81 ? 2    NAG   F O3   1 
HETATM 4600 O O4   . NAG   F 2 .   ? 197.683 176.934 138.512 1.00 200.91 ? 2    NAG   F O4   1 
HETATM 4601 O O5   . NAG   F 2 .   ? 197.891 176.645 134.806 1.00 206.13 ? 2    NAG   F O5   1 
HETATM 4602 O O6   . NAG   F 2 .   ? 195.352 177.907 135.029 1.00 200.14 ? 2    NAG   F O6   1 
HETATM 4603 O O7   . NAG   F 2 .   ? 202.488 175.546 134.735 1.00 198.32 ? 2    NAG   F O7   1 
HETATM 4604 H H1   . NAG   F 2 .   ? 198.234 174.572 134.868 1.00 200.77 ? 2    NAG   F H1   1 
HETATM 4605 H H2   . NAG   F 2 .   ? 200.472 176.526 135.565 1.00 201.08 ? 2    NAG   F H2   1 
HETATM 4606 H H3   . NAG   F 2 .   ? 198.733 174.826 137.393 1.00 201.02 ? 2    NAG   F H3   1 
HETATM 4607 H H4   . NAG   F 2 .   ? 198.865 177.863 137.081 1.00 201.27 ? 2    NAG   F H4   1 
HETATM 4608 H H5   . NAG   F 2 .   ? 196.609 175.946 136.320 1.00 201.13 ? 2    NAG   F H5   1 
HETATM 4609 H H61  . NAG   F 2 .   ? 195.828 178.218 137.020 1.00 200.72 ? 2    NAG   F H61  1 
HETATM 4610 H H62  . NAG   F 2 .   ? 196.939 178.953 135.857 1.00 200.51 ? 2    NAG   F H62  1 
HETATM 4611 H H81  . NAG   F 2 .   ? 203.770 173.332 134.704 1.00 200.52 ? 2    NAG   F H81  1 
HETATM 4612 H H82  . NAG   F 2 .   ? 202.251 172.413 134.719 1.00 200.30 ? 2    NAG   F H82  1 
HETATM 4613 H H83  . NAG   F 2 .   ? 203.012 172.899 136.251 1.00 200.65 ? 2    NAG   F H83  1 
HETATM 4614 H HN2  . NAG   F 2 .   ? 200.456 173.569 136.068 1.00 200.75 ? 2    NAG   F HN2  1 
HETATM 4615 H HO3  . NAG   F 2 .   ? 200.948 175.226 138.116 1.00 200.87 ? 2    NAG   F HO3  1 
HETATM 4616 H HO4  . NAG   F 2 .   ? 198.388 176.835 139.156 1.00 200.59 ? 2    NAG   F HO4  1 
HETATM 4617 H HO6  . NAG   F 2 .   ? 194.815 178.702 134.993 1.00 200.65 ? 2    NAG   F HO6  1 
HETATM 4618 C C1   . NAG   G 5 .   ? 214.366 160.598 102.218 1.00 177.87 ? 1401 NAG   A C1   1 
HETATM 4619 C C2   . NAG   G 5 .   ? 215.134 159.432 101.551 1.00 179.82 ? 1401 NAG   A C2   1 
HETATM 4620 C C3   . NAG   G 5 .   ? 216.326 159.982 100.752 1.00 179.22 ? 1401 NAG   A C3   1 
HETATM 4621 C C4   . NAG   G 5 .   ? 215.854 161.027 99.730  1.00 177.32 ? 1401 NAG   A C4   1 
HETATM 4622 C C5   . NAG   G 5 .   ? 215.080 162.163 100.417 1.00 177.69 ? 1401 NAG   A C5   1 
HETATM 4623 C C6   . NAG   G 5 .   ? 214.510 163.200 99.438  1.00 177.10 ? 1401 NAG   A C6   1 
HETATM 4624 C C7   . NAG   G 5 .   ? 214.872 157.416 102.928 1.00 175.88 ? 1401 NAG   A C7   1 
HETATM 4625 C C8   . NAG   G 5 .   ? 215.524 156.444 103.925 1.00 172.44 ? 1401 NAG   A C8   1 
HETATM 4626 N N2   . NAG   G 5 .   ? 215.602 158.464 102.554 1.00 177.90 ? 1401 NAG   A N2   1 
HETATM 4627 O O3   . NAG   G 5 .   ? 217.009 158.909 100.043 1.00 178.91 ? 1401 NAG   A O3   1 
HETATM 4628 O O4   . NAG   G 5 .   ? 217.034 161.568 99.094  1.00 174.67 ? 1401 NAG   A O4   1 
HETATM 4629 O O5   . NAG   G 5 .   ? 213.968 161.585 101.211 1.00 175.79 ? 1401 NAG   A O5   1 
HETATM 4630 O O6   . NAG   G 5 .   ? 213.543 162.588 98.560  1.00 177.48 ? 1401 NAG   A O6   1 
HETATM 4631 O O7   . NAG   G 5 .   ? 213.734 157.240 102.497 1.00 177.66 ? 1401 NAG   A O7   1 
HETATM 4632 H H1   . NAG   G 5 .   ? 214.989 161.083 102.969 1.00 175.07 ? 1401 NAG   A H1   1 
HETATM 4633 H H2   . NAG   G 5 .   ? 214.465 158.925 100.855 1.00 175.44 ? 1401 NAG   A H2   1 
HETATM 4634 H H3   . NAG   G 5 .   ? 217.030 160.446 101.443 1.00 175.71 ? 1401 NAG   A H3   1 
HETATM 4635 H H4   . NAG   G 5 .   ? 215.230 160.546 98.977  1.00 175.12 ? 1401 NAG   A H4   1 
HETATM 4636 H H5   . NAG   G 5 .   ? 215.752 162.679 101.103 1.00 175.24 ? 1401 NAG   A H5   1 
HETATM 4637 H H61  . NAG   G 5 .   ? 214.022 163.999 99.997  1.00 175.14 ? 1401 NAG   A H61  1 
HETATM 4638 H H62  . NAG   G 5 .   ? 215.308 163.644 98.843  1.00 175.18 ? 1401 NAG   A H62  1 
HETATM 4639 H H81  . NAG   G 5 .   ? 214.754 155.848 104.415 1.00 174.13 ? 1401 NAG   A H81  1 
HETATM 4640 H H82  . NAG   G 5 .   ? 216.206 155.780 103.395 1.00 174.15 ? 1401 NAG   A H82  1 
HETATM 4641 H H83  . NAG   G 5 .   ? 216.077 157.000 104.682 1.00 174.38 ? 1401 NAG   A H83  1 
HETATM 4642 H HN2  . NAG   G 5 .   ? 216.480 158.641 103.021 1.00 175.07 ? 1401 NAG   A HN2  1 
HETATM 4643 H HO3  . NAG   G 5 .   ? 217.260 158.224 100.667 1.00 175.75 ? 1401 NAG   A HO3  1 
HETATM 4644 H HO4  . NAG   G 5 .   ? 217.569 160.816 98.830  1.00 174.87 ? 1401 NAG   A HO4  1 
HETATM 4645 H HO6  . NAG   G 5 .   ? 213.166 163.272 98.002  1.00 175.15 ? 1401 NAG   A HO6  1 
HETATM 4646 C C1   . NAG   H 5 .   ? 218.694 157.344 132.081 1.00 178.61 ? 1402 NAG   A C1   1 
HETATM 4647 C C2   . NAG   H 5 .   ? 220.091 158.001 132.131 1.00 177.78 ? 1402 NAG   A C2   1 
HETATM 4648 C C3   . NAG   H 5 .   ? 221.097 156.978 132.674 1.00 177.50 ? 1402 NAG   A C3   1 
HETATM 4649 C C4   . NAG   H 5 .   ? 220.669 156.533 134.080 1.00 177.16 ? 1402 NAG   A C4   1 
HETATM 4650 C C5   . NAG   H 5 .   ? 219.234 155.974 134.094 1.00 176.80 ? 1402 NAG   A C5   1 
HETATM 4651 C C6   . NAG   H 5 .   ? 218.719 155.682 135.511 1.00 172.32 ? 1402 NAG   A C6   1 
HETATM 4652 C C7   . NAG   H 5 .   ? 220.203 159.708 130.385 1.00 176.82 ? 1402 NAG   A C7   1 
HETATM 4653 C C8   . NAG   H 5 .   ? 220.634 160.059 128.954 1.00 174.74 ? 1402 NAG   A C8   1 
HETATM 4654 N N2   . NAG   H 5 .   ? 220.495 158.480 130.805 1.00 178.54 ? 1402 NAG   A N2   1 
HETATM 4655 O O3   . NAG   H 5 .   ? 222.432 157.552 132.750 1.00 176.05 ? 1402 NAG   A O3   1 
HETATM 4656 O O4   . NAG   H 5 .   ? 221.588 155.498 134.500 1.00 173.93 ? 1402 NAG   A O4   1 
HETATM 4657 O O5   . NAG   H 5 .   ? 218.304 156.928 133.431 1.00 176.12 ? 1402 NAG   A O5   1 
HETATM 4658 O O6   . NAG   H 5 .   ? 218.677 156.895 136.291 1.00 169.13 ? 1402 NAG   A O6   1 
HETATM 4659 O O7   . NAG   H 5 .   ? 219.613 160.511 131.106 1.00 175.08 ? 1402 NAG   A O7   1 
HETATM 4660 H H1   . NAG   H 5 .   ? 218.707 156.474 131.425 1.00 174.97 ? 1402 NAG   A H1   1 
HETATM 4661 H H2   . NAG   H 5 .   ? 220.059 158.847 132.818 1.00 174.61 ? 1402 NAG   A H2   1 
HETATM 4662 H H3   . NAG   H 5 .   ? 221.125 156.115 132.008 1.00 174.72 ? 1402 NAG   A H3   1 
HETATM 4663 H H4   . NAG   H 5 .   ? 220.749 157.378 134.764 1.00 174.59 ? 1402 NAG   A H4   1 
HETATM 4664 H H5   . NAG   H 5 .   ? 219.217 155.043 133.527 1.00 174.86 ? 1402 NAG   A H5   1 
HETATM 4665 H H61  . NAG   H 5 .   ? 217.715 155.260 135.457 1.00 173.97 ? 1402 NAG   A H61  1 
HETATM 4666 H H62  . NAG   H 5 .   ? 219.364 154.956 136.008 1.00 174.09 ? 1402 NAG   A H62  1 
HETATM 4667 H H81  . NAG   H 5 .   ? 220.340 161.082 128.718 1.00 174.23 ? 1402 NAG   A H81  1 
HETATM 4668 H H82  . NAG   H 5 .   ? 221.716 159.968 128.863 1.00 174.46 ? 1402 NAG   A H82  1 
HETATM 4669 H H83  . NAG   H 5 .   ? 220.154 159.380 128.249 1.00 174.13 ? 1402 NAG   A H83  1 
HETATM 4670 H HN2  . NAG   H 5 .   ? 220.836 157.807 130.134 1.00 174.81 ? 1402 NAG   A HN2  1 
HETATM 4671 H HO3  . NAG   H 5 .   ? 222.659 157.934 131.898 1.00 174.51 ? 1402 NAG   A HO3  1 
HETATM 4672 H HO4  . NAG   H 5 .   ? 222.471 155.832 134.324 1.00 174.25 ? 1402 NAG   A HO4  1 
HETATM 4673 H HO6  . NAG   H 5 .   ? 218.295 156.690 137.148 1.00 173.78 ? 1402 NAG   A HO6  1 
HETATM 4674 C C21  . A1AR1 I 6 .   ? 221.057 151.310 118.752 1.00 166.82 ? 1403 A1AR1 A C21  1 
HETATM 4675 C C6   . A1AR1 I 6 .   ? 213.490 149.939 120.134 1.00 163.85 ? 1403 A1AR1 A C6   1 
HETATM 4676 C C7   . A1AR1 I 6 .   ? 213.402 148.658 119.289 1.00 164.87 ? 1403 A1AR1 A C7   1 
HETATM 4677 C C8   . A1AR1 I 6 .   ? 214.558 148.569 118.250 1.00 163.17 ? 1403 A1AR1 A C8   1 
HETATM 4678 C C11  . A1AR1 I 6 .   ? 209.034 148.892 119.943 1.00 160.38 ? 1403 A1AR1 A C11  1 
HETATM 4679 C C10  . A1AR1 I 6 .   ? 210.388 148.780 120.596 1.00 162.90 ? 1403 A1AR1 A C10  1 
HETATM 4680 C C9   . A1AR1 I 6 .   ? 214.194 147.435 117.259 1.00 161.90 ? 1403 A1AR1 A C9   1 
HETATM 4681 C C5   . A1AR1 I 6 .   ? 212.429 150.076 121.240 1.00 162.07 ? 1403 A1AR1 A C5   1 
HETATM 4682 C C4   . A1AR1 I 6 .   ? 212.631 151.463 121.878 1.00 161.72 ? 1403 A1AR1 A C4   1 
HETATM 4683 C C3   . A1AR1 I 6 .   ? 214.076 151.632 122.378 1.00 164.48 ? 1403 A1AR1 A C3   1 
HETATM 4684 C C2   . A1AR1 I 6 .   ? 215.130 151.284 121.290 1.00 167.62 ? 1403 A1AR1 A C2   1 
HETATM 4685 O O6   . A1AR1 I 6 .   ? 214.783 149.982 120.770 1.00 166.31 ? 1403 A1AR1 A O6   1 
HETATM 4686 C C1   . A1AR1 I 6 .   ? 215.280 152.377 120.131 1.00 169.73 ? 1403 A1AR1 A C1   1 
HETATM 4687 C C12  . A1AR1 I 6 .   ? 220.214 150.552 117.616 1.00 167.37 ? 1403 A1AR1 A C12  1 
HETATM 4688 C C31  . A1AR1 I 6 .   ? 221.560 152.714 118.318 1.00 164.60 ? 1403 A1AR1 A C31  1 
HETATM 4689 C C41  . A1AR1 I 6 .   ? 220.389 153.709 118.152 1.00 164.10 ? 1403 A1AR1 A C41  1 
HETATM 4690 C C51  . A1AR1 I 6 .   ? 219.534 153.767 119.449 1.00 164.31 ? 1403 A1AR1 A C51  1 
HETATM 4691 C C61  . A1AR1 I 6 .   ? 219.112 152.330 119.820 1.00 163.48 ? 1403 A1AR1 A C61  1 
HETATM 4692 C C71  . A1AR1 I 6 .   ? 218.300 152.256 121.132 1.00 164.06 ? 1403 A1AR1 A C71  1 
HETATM 4693 C C81  . A1AR1 I 6 .   ? 217.543 150.903 121.215 1.00 167.22 ? 1403 A1AR1 A C81  1 
HETATM 4694 C C91  . A1AR1 I 6 .   ? 218.332 149.737 121.833 1.00 164.88 ? 1403 A1AR1 A C91  1 
HETATM 4695 C CA9  . A1AR1 I 6 .   ? 214.992 146.421 115.178 1.00 166.60 ? 1403 A1AR1 A CA9  1 
HETATM 4696 C CM9  . A1AR1 I 6 .   ? 213.535 146.069 114.884 1.00 163.55 ? 1403 A1AR1 A CM9  1 
HETATM 4697 N N5   . A1AR1 I 6 .   ? 211.066 149.960 120.707 1.00 161.24 ? 1403 A1AR1 A N5   1 
HETATM 4698 N N51  . A1AR1 I 6 .   ? 218.339 154.633 119.308 1.00 166.28 ? 1403 A1AR1 A N51  1 
HETATM 4699 O O10  . A1AR1 I 6 .   ? 210.862 147.723 120.971 1.00 165.96 ? 1403 A1AR1 A O10  1 
HETATM 4700 O O1A  . A1AR1 I 6 .   ? 215.043 153.541 120.405 1.00 172.14 ? 1403 A1AR1 A O1A  1 
HETATM 4701 O O1B  . A1AR1 I 6 .   ? 215.449 152.002 118.971 1.00 168.79 ? 1403 A1AR1 A O1B  1 
HETATM 4702 O O3   . A1AR1 I 6 .   ? 222.186 150.535 119.161 1.00 161.00 ? 1403 A1AR1 A O3   1 
HETATM 4703 O O4   . A1AR1 I 6 .   ? 211.726 151.634 122.962 1.00 159.67 ? 1403 A1AR1 A O4   1 
HETATM 4704 O O41  . A1AR1 I 6 .   ? 220.914 154.995 117.826 1.00 167.69 ? 1403 A1AR1 A O41  1 
HETATM 4705 O O61  . A1AR1 I 6 .   ? 220.296 151.509 119.963 1.00 167.93 ? 1403 A1AR1 A O61  1 
HETATM 4706 O O7   . A1AR1 I 6 .   ? 213.386 147.492 120.116 1.00 163.86 ? 1403 A1AR1 A O7   1 
HETATM 4707 O O71  . A1AR1 I 6 .   ? 219.103 152.482 122.297 1.00 166.58 ? 1403 A1AR1 A O71  1 
HETATM 4708 O O8   . A1AR1 I 6 .   ? 214.722 149.820 117.553 1.00 163.48 ? 1403 A1AR1 A O8   1 
HETATM 4709 O O81  . A1AR1 I 6 .   ? 216.362 151.089 122.021 1.00 166.32 ? 1403 A1AR1 A O81  1 
HETATM 4710 O O9   . A1AR1 I 6 .   ? 215.199 147.268 116.238 1.00 163.70 ? 1403 A1AR1 A O9   1 
HETATM 4711 O O91  . A1AR1 I 6 .   ? 217.445 148.624 121.947 1.00 163.97 ? 1403 A1AR1 A O91  1 
HETATM 4712 O OA9  . A1AR1 I 6 .   ? 215.902 146.003 114.488 1.00 170.49 ? 1403 A1AR1 A OA9  1 
HETATM 4713 C C101 . A1AR1 I 6 .   ? 218.210 155.905 119.797 1.00 167.48 ? 1403 A1AR1 A C101 1 
HETATM 4714 C C111 . A1AR1 I 6 .   ? 219.445 156.791 119.878 1.00 163.86 ? 1403 A1AR1 A C111 1 
HETATM 4715 O O101 . A1AR1 I 6 .   ? 217.110 156.320 120.111 1.00 169.29 ? 1403 A1AR1 A O101 1 
HETATM 4716 O O1A1 . A1AR1 I 6 .   ? 219.291 149.827 117.960 1.00 166.15 ? 1403 A1AR1 A O1A1 1 
HETATM 4717 O O1B1 . A1AR1 I 6 .   ? 220.381 150.877 116.449 1.00 167.38 ? 1403 A1AR1 A O1B1 1 
HETATM 4718 H H1   . A1AR1 I 6 .   ? 213.356 150.784 119.448 1.00 163.80 ? 1403 A1AR1 A H1   1 
HETATM 4719 H H2   . A1AR1 I 6 .   ? 212.459 148.707 118.729 1.00 163.96 ? 1403 A1AR1 A H2   1 
HETATM 4720 H H3   . A1AR1 I 6 .   ? 215.486 148.303 118.770 1.00 163.56 ? 1403 A1AR1 A H3   1 
HETATM 4721 H H4   . A1AR1 I 6 .   ? 208.371 149.492 120.578 1.00 162.41 ? 1403 A1AR1 A H4   1 
HETATM 4722 H H5   . A1AR1 I 6 .   ? 208.598 147.894 119.807 1.00 162.63 ? 1403 A1AR1 A H5   1 
HETATM 4723 H H6   . A1AR1 I 6 .   ? 209.126 149.379 118.965 1.00 162.10 ? 1403 A1AR1 A H6   1 
HETATM 4724 H H7   . A1AR1 I 6 .   ? 214.095 146.495 117.817 1.00 163.48 ? 1403 A1AR1 A H7   1 
HETATM 4725 H H8   . A1AR1 I 6 .   ? 213.223 147.691 116.817 1.00 163.30 ? 1403 A1AR1 A H8   1 
HETATM 4726 H H9   . A1AR1 I 6 .   ? 212.601 149.304 122.000 1.00 163.76 ? 1403 A1AR1 A H9   1 
HETATM 4727 H H10  . A1AR1 I 6 .   ? 212.443 152.226 121.112 1.00 163.10 ? 1403 A1AR1 A H10  1 
HETATM 4728 H H11  . A1AR1 I 6 .   ? 214.229 152.660 122.729 1.00 163.95 ? 1403 A1AR1 A H11  1 
HETATM 4729 H H12  . A1AR1 I 6 .   ? 214.232 150.977 123.245 1.00 163.56 ? 1403 A1AR1 A H12  1 
HETATM 4730 H H13  . A1AR1 I 6 .   ? 222.251 153.099 119.078 1.00 163.67 ? 1403 A1AR1 A H13  1 
HETATM 4731 H H14  . A1AR1 I 6 .   ? 222.126 152.635 117.381 1.00 163.76 ? 1403 A1AR1 A H14  1 
HETATM 4732 H H15  . A1AR1 I 6 .   ? 219.750 153.352 117.335 1.00 163.29 ? 1403 A1AR1 A H15  1 
HETATM 4733 H H16  . A1AR1 I 6 .   ? 220.165 154.137 120.267 1.00 164.15 ? 1403 A1AR1 A H16  1 
HETATM 4734 H H17  . A1AR1 I 6 .   ? 218.472 151.951 119.013 1.00 163.27 ? 1403 A1AR1 A H17  1 
HETATM 4735 H H18  . A1AR1 I 6 .   ? 217.541 153.047 121.087 1.00 163.52 ? 1403 A1AR1 A H18  1 
HETATM 4736 H H19  . A1AR1 I 6 .   ? 217.265 150.585 120.202 1.00 164.20 ? 1403 A1AR1 A H19  1 
HETATM 4737 H H20  . A1AR1 I 6 .   ? 218.710 150.022 122.823 1.00 163.95 ? 1403 A1AR1 A H20  1 
HETATM 4738 H H21  . A1AR1 I 6 .   ? 219.189 149.485 121.196 1.00 163.38 ? 1403 A1AR1 A H21  1 
HETATM 4739 H H22  . A1AR1 I 6 .   ? 213.474 145.516 113.938 1.00 163.20 ? 1403 A1AR1 A H22  1 
HETATM 4740 H H23  . A1AR1 I 6 .   ? 212.931 146.978 114.779 1.00 162.58 ? 1403 A1AR1 A H23  1 
HETATM 4741 H H24  . A1AR1 I 6 .   ? 213.126 145.432 115.679 1.00 163.01 ? 1403 A1AR1 A H24  1 
HETATM 4742 H H25  . A1AR1 I 6 .   ? 210.650 150.768 120.260 1.00 162.54 ? 1403 A1AR1 A H25  1 
HETATM 4743 H H26  . A1AR1 I 6 .   ? 217.446 154.205 119.097 1.00 163.83 ? 1403 A1AR1 A H26  1 
HETATM 4744 H H28  . A1AR1 I 6 .   ? 221.895 150.144 120.003 1.00 162.95 ? 1403 A1AR1 A H28  1 
HETATM 4745 H H29  . A1AR1 I 6 .   ? 211.011 150.985 122.839 1.00 163.48 ? 1403 A1AR1 A H29  1 
HETATM 4746 H H30  . A1AR1 I 6 .   ? 221.602 154.867 117.150 1.00 164.16 ? 1403 A1AR1 A H30  1 
HETATM 4747 H H31  . A1AR1 I 6 .   ? 212.515 147.486 120.548 1.00 163.98 ? 1403 A1AR1 A H31  1 
HETATM 4748 H H32  . A1AR1 I 6 .   ? 219.430 153.399 122.281 1.00 164.22 ? 1403 A1AR1 A H32  1 
HETATM 4749 H H33  . A1AR1 I 6 .   ? 215.069 150.485 118.174 1.00 163.72 ? 1403 A1AR1 A H33  1 
HETATM 4750 H H34  . A1AR1 I 6 .   ? 216.562 149.032 121.919 1.00 163.99 ? 1403 A1AR1 A H34  1 
HETATM 4751 H H35  . A1AR1 I 6 .   ? 219.243 157.650 120.530 1.00 163.46 ? 1403 A1AR1 A H35  1 
HETATM 4752 H H36  . A1AR1 I 6 .   ? 220.313 156.250 120.275 1.00 164.01 ? 1403 A1AR1 A H36  1 
HETATM 4753 H H37  . A1AR1 I 6 .   ? 219.692 157.164 118.877 1.00 163.57 ? 1403 A1AR1 A H37  1 
# 
