data_9CO9
# 
_entry.id   9CO9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CO9         pdb_00009co9 10.2210/pdb9co9/pdb 
WWPDB D_1000285397 ?            ?                   
EMDB  EMD-45774    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2024-12-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 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                        9CO9 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'local refinement of JN.1 spike/Nanosota-9 complex' 
_pdbx_database_related.db_id          EMD-45774 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              lifang@umn.edu 
_pdbx_contact_author.name_first         Fang 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1958-366X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ye, G.'  1 ? 
'Bu, F.'  2 ? 
'Liu, B.' 3 ? 
'Li, F.'  4 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Plos Pathog.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1553-7374 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                e1012726 
_citation.page_last                 e1012726 
_citation.title                     'Discovery of Nanosota-9 as anti-Omicron nanobody therapeutic candidate.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1371/journal.ppat.1012726 
_citation.pdbx_database_id_PubMed   39591462 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ye, G.'             1  ?                   
primary 'Bu, F.'             2  ?                   
primary 'Saxena, D.'         3  ?                   
primary 'Turner-Hubbard, H.' 4  ?                   
primary 'Herbst, M.'         5  ?                   
primary 'Spiller, B.'        6  ?                   
primary 'Wadzinski, B.E.'    7  ?                   
primary 'Du, L.'             8  ?                   
primary 'Liu, B.'            9  ?                   
primary 'Zheng, J.'          10 ?                   
primary 'Li, F.'             11 0000-0002-1958-366X 
# 
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' 138330.781 2 ? ? ? 'JN.1 spike' 
2 polymer man Nanosota-9           16311.601  2 ? ? ? ?            
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'S glycoprotein,E2,Peplomer protein' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MFVFLVLLPLVSSQCVMPLFNLITTTQSYTNSFTRGVYYPDKVFRSSVLHLTQDLFLPFFSNVTWFHAISGTNGTKRFDN
PVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVFIKVCEFQFCNDPFLDVYHKNNKSWMESESGVYSS
ANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPIIGRDFPQGFSALEPLVDLPIGINITRFQTLLA
LNRSYLTPGDSSSGWTAGAADYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPT
ESIVRFPNVTNLCPFHEVFNATRFASVYAWNRTRISNCVADYSVLYNFAPFFAFKCYGVSPTKLNDLCFTNVYADSFVIK
GNEVSQIAPGQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKHSGNYDYWYRSFRKSKLKPFERDISTEIYQAGNKPCKGK
GPNCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTKSNKKFLPFQQ
FGRDIVDTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVSVAIHADQLTPTWRVYSTGSNVFQ
TRAGCLIGAEYVNNSYECDIPIGAGICASYQTQTKSRAGARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTT
EILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLKRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKYFGGFNFSQ
ILPDPSKPSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITS
GWTFGAGPALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLFSTPSALGKLQDVVNHNAQALNTLVK
QLSSKFGAISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCG
KGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSG
NCDVVIGIVNNTVYDPLQLELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG
KYEQYIKGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGHHHHHH
;
;MFVFLVLLPLVSSQCVMPLFNLITTTQSYTNSFTRGVYYPDKVFRSSVLHLTQDLFLPFFSNVTWFHAISGTNGTKRFDN
PVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVFIKVCEFQFCNDPFLDVYHKNNKSWMESESGVYSS
ANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPIIGRDFPQGFSALEPLVDLPIGINITRFQTLLA
LNRSYLTPGDSSSGWTAGAADYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPT
ESIVRFPNVTNLCPFHEVFNATRFASVYAWNRTRISNCVADYSVLYNFAPFFAFKCYGVSPTKLNDLCFTNVYADSFVIK
GNEVSQIAPGQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKHSGNYDYWYRSFRKSKLKPFERDISTEIYQAGNKPCKGK
GPNCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTKSNKKFLPFQQ
FGRDIVDTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVSVAIHADQLTPTWRVYSTGSNVFQ
TRAGCLIGAEYVNNSYECDIPIGAGICASYQTQTKSRAGARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTT
EILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLKRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKYFGGFNFSQ
ILPDPSKPSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITS
GWTFGAGPALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLFSTPSALGKLQDVVNHNAQALNTLVK
QLSSKFGAISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCG
KGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSG
NCDVVIGIVNNTVYDPLQLELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG
KYEQYIKGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGHHHHHH
;
B,A ? 
2 'polypeptide(L)' no no 
;QVQLQESGGGLVQPGGSLRLSCTASGIALHTHATGWFRQAPGKEREGVSCISSGDGTTYYEDSVEGRFTISRDNAKNTVY
LQMNSLKLEDTAVYYCAADPGAVCHSGSYYYTDDDFYYRGQGTQVTVSSGGQHHHHHHGAYPYDVPDYAS
;
;QVQLQESGGGLVQPGGSLRLSCTASGIALHTHATGWFRQAPGKEREGVSCISSGDGTTYYEDSVEGRFTISRDNAKNTVY
LQMNSLKLEDTAVYYCAADPGAVCHSGSYYYTDDDFYYRGQGTQVTVSSGGQHHHHHHGAYPYDVPDYAS
;
D,E ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    PHE n 
1 3    VAL n 
1 4    PHE n 
1 5    LEU n 
1 6    VAL n 
1 7    LEU n 
1 8    LEU n 
1 9    PRO n 
1 10   LEU n 
1 11   VAL n 
1 12   SER n 
1 13   SER n 
1 14   GLN n 
1 15   CYS n 
1 16   VAL n 
1 17   MET n 
1 18   PRO n 
1 19   LEU n 
1 20   PHE n 
1 21   ASN n 
1 22   LEU n 
1 23   ILE n 
1 24   THR n 
1 25   THR n 
1 26   THR n 
1 27   GLN n 
1 28   SER n 
1 29   TYR n 
1 30   THR n 
1 31   ASN n 
1 32   SER n 
1 33   PHE n 
1 34   THR n 
1 35   ARG n 
1 36   GLY n 
1 37   VAL n 
1 38   TYR n 
1 39   TYR n 
1 40   PRO n 
1 41   ASP n 
1 42   LYS n 
1 43   VAL n 
1 44   PHE n 
1 45   ARG n 
1 46   SER n 
1 47   SER n 
1 48   VAL n 
1 49   LEU n 
1 50   HIS n 
1 51   LEU n 
1 52   THR n 
1 53   GLN n 
1 54   ASP n 
1 55   LEU n 
1 56   PHE n 
1 57   LEU n 
1 58   PRO n 
1 59   PHE n 
1 60   PHE n 
1 61   SER n 
1 62   ASN n 
1 63   VAL n 
1 64   THR n 
1 65   TRP n 
1 66   PHE n 
1 67   HIS n 
1 68   ALA n 
1 69   ILE n 
1 70   SER n 
1 71   GLY n 
1 72   THR n 
1 73   ASN n 
1 74   GLY n 
1 75   THR n 
1 76   LYS n 
1 77   ARG n 
1 78   PHE n 
1 79   ASP n 
1 80   ASN n 
1 81   PRO n 
1 82   VAL n 
1 83   LEU n 
1 84   PRO n 
1 85   PHE n 
1 86   ASN n 
1 87   ASP n 
1 88   GLY n 
1 89   VAL n 
1 90   TYR n 
1 91   PHE n 
1 92   ALA n 
1 93   SER n 
1 94   THR n 
1 95   GLU n 
1 96   LYS n 
1 97   SER n 
1 98   ASN n 
1 99   ILE n 
1 100  ILE n 
1 101  ARG n 
1 102  GLY n 
1 103  TRP n 
1 104  ILE n 
1 105  PHE n 
1 106  GLY n 
1 107  THR n 
1 108  THR n 
1 109  LEU n 
1 110  ASP n 
1 111  SER n 
1 112  LYS n 
1 113  THR n 
1 114  GLN n 
1 115  SER n 
1 116  LEU n 
1 117  LEU n 
1 118  ILE n 
1 119  VAL n 
1 120  ASN n 
1 121  ASN n 
1 122  ALA n 
1 123  THR n 
1 124  ASN n 
1 125  VAL n 
1 126  PHE n 
1 127  ILE n 
1 128  LYS n 
1 129  VAL n 
1 130  CYS n 
1 131  GLU n 
1 132  PHE n 
1 133  GLN n 
1 134  PHE n 
1 135  CYS n 
1 136  ASN n 
1 137  ASP n 
1 138  PRO n 
1 139  PHE n 
1 140  LEU n 
1 141  ASP n 
1 142  VAL n 
1 143  TYR n 
1 144  HIS n 
1 145  LYS n 
1 146  ASN n 
1 147  ASN n 
1 148  LYS n 
1 149  SER n 
1 150  TRP n 
1 151  MET n 
1 152  GLU n 
1 153  SER n 
1 154  GLU n 
1 155  SER n 
1 156  GLY n 
1 157  VAL n 
1 158  TYR n 
1 159  SER n 
1 160  SER n 
1 161  ALA n 
1 162  ASN n 
1 163  ASN n 
1 164  CYS n 
1 165  THR n 
1 166  PHE n 
1 167  GLU n 
1 168  TYR n 
1 169  VAL n 
1 170  SER n 
1 171  GLN n 
1 172  PRO n 
1 173  PHE n 
1 174  LEU n 
1 175  MET n 
1 176  ASP n 
1 177  LEU n 
1 178  GLU n 
1 179  GLY n 
1 180  LYS n 
1 181  GLN n 
1 182  GLY n 
1 183  ASN n 
1 184  PHE n 
1 185  LYS n 
1 186  ASN n 
1 187  LEU n 
1 188  ARG n 
1 189  GLU n 
1 190  PHE n 
1 191  VAL n 
1 192  PHE n 
1 193  LYS n 
1 194  ASN n 
1 195  ILE n 
1 196  ASP n 
1 197  GLY n 
1 198  TYR n 
1 199  PHE n 
1 200  LYS n 
1 201  ILE n 
1 202  TYR n 
1 203  SER n 
1 204  LYS n 
1 205  HIS n 
1 206  THR n 
1 207  PRO n 
1 208  ILE n 
1 209  ILE n 
1 210  GLY n 
1 211  ARG n 
1 212  ASP n 
1 213  PHE n 
1 214  PRO n 
1 215  GLN n 
1 216  GLY n 
1 217  PHE n 
1 218  SER n 
1 219  ALA n 
1 220  LEU n 
1 221  GLU n 
1 222  PRO n 
1 223  LEU n 
1 224  VAL n 
1 225  ASP n 
1 226  LEU n 
1 227  PRO n 
1 228  ILE n 
1 229  GLY n 
1 230  ILE n 
1 231  ASN n 
1 232  ILE n 
1 233  THR n 
1 234  ARG n 
1 235  PHE n 
1 236  GLN n 
1 237  THR n 
1 238  LEU n 
1 239  LEU n 
1 240  ALA n 
1 241  LEU n 
1 242  ASN n 
1 243  ARG n 
1 244  SER n 
1 245  TYR n 
1 246  LEU n 
1 247  THR n 
1 248  PRO n 
1 249  GLY n 
1 250  ASP n 
1 251  SER n 
1 252  SER n 
1 253  SER n 
1 254  GLY n 
1 255  TRP n 
1 256  THR n 
1 257  ALA n 
1 258  GLY n 
1 259  ALA n 
1 260  ALA n 
1 261  ASP n 
1 262  TYR n 
1 263  TYR n 
1 264  VAL n 
1 265  GLY n 
1 266  TYR n 
1 267  LEU n 
1 268  GLN n 
1 269  PRO n 
1 270  ARG n 
1 271  THR n 
1 272  PHE n 
1 273  LEU n 
1 274  LEU n 
1 275  LYS n 
1 276  TYR n 
1 277  ASN n 
1 278  GLU n 
1 279  ASN n 
1 280  GLY n 
1 281  THR n 
1 282  ILE n 
1 283  THR n 
1 284  ASP n 
1 285  ALA n 
1 286  VAL n 
1 287  ASP n 
1 288  CYS n 
1 289  ALA n 
1 290  LEU n 
1 291  ASP n 
1 292  PRO n 
1 293  LEU n 
1 294  SER n 
1 295  GLU n 
1 296  THR n 
1 297  LYS n 
1 298  CYS n 
1 299  THR n 
1 300  LEU n 
1 301  LYS n 
1 302  SER n 
1 303  PHE n 
1 304  THR n 
1 305  VAL n 
1 306  GLU n 
1 307  LYS n 
1 308  GLY n 
1 309  ILE n 
1 310  TYR n 
1 311  GLN n 
1 312  THR n 
1 313  SER n 
1 314  ASN n 
1 315  PHE n 
1 316  ARG n 
1 317  VAL n 
1 318  GLN n 
1 319  PRO n 
1 320  THR n 
1 321  GLU n 
1 322  SER n 
1 323  ILE n 
1 324  VAL n 
1 325  ARG n 
1 326  PHE n 
1 327  PRO n 
1 328  ASN n 
1 329  VAL n 
1 330  THR n 
1 331  ASN n 
1 332  LEU n 
1 333  CYS n 
1 334  PRO n 
1 335  PHE n 
1 336  HIS n 
1 337  GLU n 
1 338  VAL n 
1 339  PHE n 
1 340  ASN n 
1 341  ALA n 
1 342  THR n 
1 343  ARG n 
1 344  PHE n 
1 345  ALA n 
1 346  SER n 
1 347  VAL n 
1 348  TYR n 
1 349  ALA n 
1 350  TRP n 
1 351  ASN n 
1 352  ARG n 
1 353  THR n 
1 354  ARG n 
1 355  ILE n 
1 356  SER n 
1 357  ASN n 
1 358  CYS n 
1 359  VAL n 
1 360  ALA n 
1 361  ASP n 
1 362  TYR n 
1 363  SER n 
1 364  VAL n 
1 365  LEU n 
1 366  TYR n 
1 367  ASN n 
1 368  PHE n 
1 369  ALA n 
1 370  PRO n 
1 371  PHE n 
1 372  PHE n 
1 373  ALA n 
1 374  PHE n 
1 375  LYS n 
1 376  CYS n 
1 377  TYR n 
1 378  GLY n 
1 379  VAL n 
1 380  SER n 
1 381  PRO n 
1 382  THR n 
1 383  LYS n 
1 384  LEU n 
1 385  ASN n 
1 386  ASP n 
1 387  LEU n 
1 388  CYS n 
1 389  PHE n 
1 390  THR n 
1 391  ASN n 
1 392  VAL n 
1 393  TYR n 
1 394  ALA n 
1 395  ASP n 
1 396  SER n 
1 397  PHE n 
1 398  VAL n 
1 399  ILE n 
1 400  LYS n 
1 401  GLY n 
1 402  ASN n 
1 403  GLU n 
1 404  VAL n 
1 405  SER n 
1 406  GLN n 
1 407  ILE n 
1 408  ALA n 
1 409  PRO n 
1 410  GLY n 
1 411  GLN n 
1 412  THR n 
1 413  GLY n 
1 414  ASN n 
1 415  ILE n 
1 416  ALA n 
1 417  ASP n 
1 418  TYR n 
1 419  ASN n 
1 420  TYR n 
1 421  LYS n 
1 422  LEU n 
1 423  PRO n 
1 424  ASP n 
1 425  ASP n 
1 426  PHE n 
1 427  THR n 
1 428  GLY n 
1 429  CYS n 
1 430  VAL n 
1 431  ILE n 
1 432  ALA n 
1 433  TRP n 
1 434  ASN n 
1 435  SER n 
1 436  ASN n 
1 437  LYS n 
1 438  LEU n 
1 439  ASP n 
1 440  SER n 
1 441  LYS n 
1 442  HIS n 
1 443  SER n 
1 444  GLY n 
1 445  ASN n 
1 446  TYR n 
1 447  ASP n 
1 448  TYR n 
1 449  TRP n 
1 450  TYR n 
1 451  ARG n 
1 452  SER n 
1 453  PHE n 
1 454  ARG n 
1 455  LYS n 
1 456  SER n 
1 457  LYS n 
1 458  LEU n 
1 459  LYS n 
1 460  PRO n 
1 461  PHE n 
1 462  GLU n 
1 463  ARG n 
1 464  ASP n 
1 465  ILE n 
1 466  SER n 
1 467  THR n 
1 468  GLU n 
1 469  ILE n 
1 470  TYR n 
1 471  GLN n 
1 472  ALA n 
1 473  GLY n 
1 474  ASN n 
1 475  LYS n 
1 476  PRO n 
1 477  CYS n 
1 478  LYS n 
1 479  GLY n 
1 480  LYS n 
1 481  GLY n 
1 482  PRO n 
1 483  ASN n 
1 484  CYS n 
1 485  TYR n 
1 486  PHE n 
1 487  PRO n 
1 488  LEU n 
1 489  GLN n 
1 490  SER n 
1 491  TYR n 
1 492  GLY n 
1 493  PHE n 
1 494  ARG n 
1 495  PRO n 
1 496  THR n 
1 497  TYR n 
1 498  GLY n 
1 499  VAL n 
1 500  GLY n 
1 501  HIS n 
1 502  GLN n 
1 503  PRO n 
1 504  TYR n 
1 505  ARG n 
1 506  VAL n 
1 507  VAL n 
1 508  VAL n 
1 509  LEU n 
1 510  SER n 
1 511  PHE n 
1 512  GLU n 
1 513  LEU n 
1 514  LEU n 
1 515  HIS n 
1 516  ALA n 
1 517  PRO n 
1 518  ALA n 
1 519  THR n 
1 520  VAL n 
1 521  CYS n 
1 522  GLY n 
1 523  PRO n 
1 524  LYS n 
1 525  LYS n 
1 526  SER n 
1 527  THR n 
1 528  ASN n 
1 529  LEU n 
1 530  VAL n 
1 531  LYS n 
1 532  ASN n 
1 533  LYS n 
1 534  CYS n 
1 535  VAL n 
1 536  ASN n 
1 537  PHE n 
1 538  ASN n 
1 539  PHE n 
1 540  ASN n 
1 541  GLY n 
1 542  LEU n 
1 543  THR n 
1 544  GLY n 
1 545  THR n 
1 546  GLY n 
1 547  VAL n 
1 548  LEU n 
1 549  THR n 
1 550  LYS n 
1 551  SER n 
1 552  ASN n 
1 553  LYS n 
1 554  LYS n 
1 555  PHE n 
1 556  LEU n 
1 557  PRO n 
1 558  PHE n 
1 559  GLN n 
1 560  GLN n 
1 561  PHE n 
1 562  GLY n 
1 563  ARG n 
1 564  ASP n 
1 565  ILE n 
1 566  VAL n 
1 567  ASP n 
1 568  THR n 
1 569  THR n 
1 570  ASP n 
1 571  ALA n 
1 572  VAL n 
1 573  ARG n 
1 574  ASP n 
1 575  PRO n 
1 576  GLN n 
1 577  THR n 
1 578  LEU n 
1 579  GLU n 
1 580  ILE n 
1 581  LEU n 
1 582  ASP n 
1 583  ILE n 
1 584  THR n 
1 585  PRO n 
1 586  CYS n 
1 587  SER n 
1 588  PHE n 
1 589  GLY n 
1 590  GLY n 
1 591  VAL n 
1 592  SER n 
1 593  VAL n 
1 594  ILE n 
1 595  THR n 
1 596  PRO n 
1 597  GLY n 
1 598  THR n 
1 599  ASN n 
1 600  THR n 
1 601  SER n 
1 602  ASN n 
1 603  GLN n 
1 604  VAL n 
1 605  ALA n 
1 606  VAL n 
1 607  LEU n 
1 608  TYR n 
1 609  GLN n 
1 610  GLY n 
1 611  VAL n 
1 612  ASN n 
1 613  CYS n 
1 614  THR n 
1 615  GLU n 
1 616  VAL n 
1 617  SER n 
1 618  VAL n 
1 619  ALA n 
1 620  ILE n 
1 621  HIS n 
1 622  ALA n 
1 623  ASP n 
1 624  GLN n 
1 625  LEU n 
1 626  THR n 
1 627  PRO n 
1 628  THR n 
1 629  TRP n 
1 630  ARG n 
1 631  VAL n 
1 632  TYR n 
1 633  SER n 
1 634  THR n 
1 635  GLY n 
1 636  SER n 
1 637  ASN n 
1 638  VAL n 
1 639  PHE n 
1 640  GLN n 
1 641  THR n 
1 642  ARG n 
1 643  ALA n 
1 644  GLY n 
1 645  CYS n 
1 646  LEU n 
1 647  ILE n 
1 648  GLY n 
1 649  ALA n 
1 650  GLU n 
1 651  TYR n 
1 652  VAL n 
1 653  ASN n 
1 654  ASN n 
1 655  SER n 
1 656  TYR n 
1 657  GLU n 
1 658  CYS n 
1 659  ASP n 
1 660  ILE n 
1 661  PRO n 
1 662  ILE n 
1 663  GLY n 
1 664  ALA n 
1 665  GLY n 
1 666  ILE n 
1 667  CYS n 
1 668  ALA n 
1 669  SER n 
1 670  TYR n 
1 671  GLN n 
1 672  THR n 
1 673  GLN n 
1 674  THR n 
1 675  LYS n 
1 676  SER n 
1 677  ARG n 
1 678  ALA n 
1 679  GLY n 
1 680  ALA n 
1 681  ARG n 
1 682  SER n 
1 683  VAL n 
1 684  ALA n 
1 685  SER n 
1 686  GLN n 
1 687  SER n 
1 688  ILE n 
1 689  ILE n 
1 690  ALA n 
1 691  TYR n 
1 692  THR n 
1 693  MET n 
1 694  SER n 
1 695  LEU n 
1 696  GLY n 
1 697  ALA n 
1 698  GLU n 
1 699  ASN n 
1 700  SER n 
1 701  VAL n 
1 702  ALA n 
1 703  TYR n 
1 704  SER n 
1 705  ASN n 
1 706  ASN n 
1 707  SER n 
1 708  ILE n 
1 709  ALA n 
1 710  ILE n 
1 711  PRO n 
1 712  THR n 
1 713  ASN n 
1 714  PHE n 
1 715  THR n 
1 716  ILE n 
1 717  SER n 
1 718  VAL n 
1 719  THR n 
1 720  THR n 
1 721  GLU n 
1 722  ILE n 
1 723  LEU n 
1 724  PRO n 
1 725  VAL n 
1 726  SER n 
1 727  MET n 
1 728  THR n 
1 729  LYS n 
1 730  THR n 
1 731  SER n 
1 732  VAL n 
1 733  ASP n 
1 734  CYS n 
1 735  THR n 
1 736  MET n 
1 737  TYR n 
1 738  ILE n 
1 739  CYS n 
1 740  GLY n 
1 741  ASP n 
1 742  SER n 
1 743  THR n 
1 744  GLU n 
1 745  CYS n 
1 746  SER n 
1 747  ASN n 
1 748  LEU n 
1 749  LEU n 
1 750  LEU n 
1 751  GLN n 
1 752  TYR n 
1 753  GLY n 
1 754  SER n 
1 755  PHE n 
1 756  CYS n 
1 757  THR n 
1 758  GLN n 
1 759  LEU n 
1 760  LYS n 
1 761  ARG n 
1 762  ALA n 
1 763  LEU n 
1 764  THR n 
1 765  GLY n 
1 766  ILE n 
1 767  ALA n 
1 768  VAL n 
1 769  GLU n 
1 770  GLN n 
1 771  ASP n 
1 772  LYS n 
1 773  ASN n 
1 774  THR n 
1 775  GLN n 
1 776  GLU n 
1 777  VAL n 
1 778  PHE n 
1 779  ALA n 
1 780  GLN n 
1 781  VAL n 
1 782  LYS n 
1 783  GLN n 
1 784  ILE n 
1 785  TYR n 
1 786  LYS n 
1 787  THR n 
1 788  PRO n 
1 789  PRO n 
1 790  ILE n 
1 791  LYS n 
1 792  TYR n 
1 793  PHE n 
1 794  GLY n 
1 795  GLY n 
1 796  PHE n 
1 797  ASN n 
1 798  PHE n 
1 799  SER n 
1 800  GLN n 
1 801  ILE n 
1 802  LEU n 
1 803  PRO n 
1 804  ASP n 
1 805  PRO n 
1 806  SER n 
1 807  LYS n 
1 808  PRO n 
1 809  SER n 
1 810  LYS n 
1 811  ARG n 
1 812  SER n 
1 813  PRO n 
1 814  ILE n 
1 815  GLU n 
1 816  ASP n 
1 817  LEU n 
1 818  LEU n 
1 819  PHE n 
1 820  ASN n 
1 821  LYS n 
1 822  VAL n 
1 823  THR n 
1 824  LEU n 
1 825  ALA n 
1 826  ASP n 
1 827  ALA n 
1 828  GLY n 
1 829  PHE n 
1 830  ILE n 
1 831  LYS n 
1 832  GLN n 
1 833  TYR n 
1 834  GLY n 
1 835  ASP n 
1 836  CYS n 
1 837  LEU n 
1 838  GLY n 
1 839  ASP n 
1 840  ILE n 
1 841  ALA n 
1 842  ALA n 
1 843  ARG n 
1 844  ASP n 
1 845  LEU n 
1 846  ILE n 
1 847  CYS n 
1 848  ALA n 
1 849  GLN n 
1 850  LYS n 
1 851  PHE n 
1 852  ASN n 
1 853  GLY n 
1 854  LEU n 
1 855  THR n 
1 856  VAL n 
1 857  LEU n 
1 858  PRO n 
1 859  PRO n 
1 860  LEU n 
1 861  LEU n 
1 862  THR n 
1 863  ASP n 
1 864  GLU n 
1 865  MET n 
1 866  ILE n 
1 867  ALA n 
1 868  GLN n 
1 869  TYR n 
1 870  THR n 
1 871  SER n 
1 872  ALA n 
1 873  LEU n 
1 874  LEU n 
1 875  ALA n 
1 876  GLY n 
1 877  THR n 
1 878  ILE n 
1 879  THR n 
1 880  SER n 
1 881  GLY n 
1 882  TRP n 
1 883  THR n 
1 884  PHE n 
1 885  GLY n 
1 886  ALA n 
1 887  GLY n 
1 888  PRO n 
1 889  ALA n 
1 890  LEU n 
1 891  GLN n 
1 892  ILE n 
1 893  PRO n 
1 894  PHE n 
1 895  PRO n 
1 896  MET n 
1 897  GLN n 
1 898  MET n 
1 899  ALA n 
1 900  TYR n 
1 901  ARG n 
1 902  PHE n 
1 903  ASN n 
1 904  GLY n 
1 905  ILE n 
1 906  GLY n 
1 907  VAL n 
1 908  THR n 
1 909  GLN n 
1 910  ASN n 
1 911  VAL n 
1 912  LEU n 
1 913  TYR n 
1 914  GLU n 
1 915  ASN n 
1 916  GLN n 
1 917  LYS n 
1 918  LEU n 
1 919  ILE n 
1 920  ALA n 
1 921  ASN n 
1 922  GLN n 
1 923  PHE n 
1 924  ASN n 
1 925  SER n 
1 926  ALA n 
1 927  ILE n 
1 928  GLY n 
1 929  LYS n 
1 930  ILE n 
1 931  GLN n 
1 932  ASP n 
1 933  SER n 
1 934  LEU n 
1 935  PHE n 
1 936  SER n 
1 937  THR n 
1 938  PRO n 
1 939  SER n 
1 940  ALA n 
1 941  LEU n 
1 942  GLY n 
1 943  LYS n 
1 944  LEU n 
1 945  GLN n 
1 946  ASP n 
1 947  VAL n 
1 948  VAL n 
1 949  ASN n 
1 950  HIS n 
1 951  ASN n 
1 952  ALA n 
1 953  GLN n 
1 954  ALA n 
1 955  LEU n 
1 956  ASN n 
1 957  THR n 
1 958  LEU n 
1 959  VAL n 
1 960  LYS n 
1 961  GLN n 
1 962  LEU n 
1 963  SER n 
1 964  SER n 
1 965  LYS n 
1 966  PHE n 
1 967  GLY n 
1 968  ALA n 
1 969  ILE n 
1 970  SER n 
1 971  SER n 
1 972  VAL n 
1 973  LEU n 
1 974  ASN n 
1 975  ASP n 
1 976  ILE n 
1 977  LEU n 
1 978  SER n 
1 979  ARG n 
1 980  LEU n 
1 981  ASP n 
1 982  PRO n 
1 983  PRO n 
1 984  GLU n 
1 985  ALA n 
1 986  GLU n 
1 987  VAL n 
1 988  GLN n 
1 989  ILE n 
1 990  ASP n 
1 991  ARG n 
1 992  LEU n 
1 993  ILE n 
1 994  THR n 
1 995  GLY n 
1 996  ARG n 
1 997  LEU n 
1 998  GLN n 
1 999  SER n 
1 1000 LEU n 
1 1001 GLN n 
1 1002 THR n 
1 1003 TYR n 
1 1004 VAL n 
1 1005 THR n 
1 1006 GLN n 
1 1007 GLN n 
1 1008 LEU n 
1 1009 ILE n 
1 1010 ARG n 
1 1011 ALA n 
1 1012 ALA n 
1 1013 GLU n 
1 1014 ILE n 
1 1015 ARG n 
1 1016 ALA n 
1 1017 SER n 
1 1018 ALA n 
1 1019 ASN n 
1 1020 LEU n 
1 1021 ALA n 
1 1022 ALA n 
1 1023 THR n 
1 1024 LYS n 
1 1025 MET n 
1 1026 SER n 
1 1027 GLU n 
1 1028 CYS n 
1 1029 VAL n 
1 1030 LEU n 
1 1031 GLY n 
1 1032 GLN n 
1 1033 SER n 
1 1034 LYS n 
1 1035 ARG n 
1 1036 VAL n 
1 1037 ASP n 
1 1038 PHE n 
1 1039 CYS n 
1 1040 GLY n 
1 1041 LYS n 
1 1042 GLY n 
1 1043 TYR n 
1 1044 HIS n 
1 1045 LEU n 
1 1046 MET n 
1 1047 SER n 
1 1048 PHE n 
1 1049 PRO n 
1 1050 GLN n 
1 1051 SER n 
1 1052 ALA n 
1 1053 PRO n 
1 1054 HIS n 
1 1055 GLY n 
1 1056 VAL n 
1 1057 VAL n 
1 1058 PHE n 
1 1059 LEU n 
1 1060 HIS n 
1 1061 VAL n 
1 1062 THR n 
1 1063 TYR n 
1 1064 VAL n 
1 1065 PRO n 
1 1066 ALA n 
1 1067 GLN n 
1 1068 GLU n 
1 1069 LYS n 
1 1070 ASN n 
1 1071 PHE n 
1 1072 THR n 
1 1073 THR n 
1 1074 ALA n 
1 1075 PRO n 
1 1076 ALA n 
1 1077 ILE n 
1 1078 CYS n 
1 1079 HIS n 
1 1080 ASP n 
1 1081 GLY n 
1 1082 LYS n 
1 1083 ALA n 
1 1084 HIS n 
1 1085 PHE n 
1 1086 PRO n 
1 1087 ARG n 
1 1088 GLU n 
1 1089 GLY n 
1 1090 VAL n 
1 1091 PHE n 
1 1092 VAL n 
1 1093 SER n 
1 1094 ASN n 
1 1095 GLY n 
1 1096 THR n 
1 1097 HIS n 
1 1098 TRP n 
1 1099 PHE n 
1 1100 VAL n 
1 1101 THR n 
1 1102 GLN n 
1 1103 ARG n 
1 1104 ASN n 
1 1105 PHE n 
1 1106 TYR n 
1 1107 GLU n 
1 1108 PRO n 
1 1109 GLN n 
1 1110 ILE n 
1 1111 ILE n 
1 1112 THR n 
1 1113 THR n 
1 1114 ASP n 
1 1115 ASN n 
1 1116 THR n 
1 1117 PHE n 
1 1118 VAL n 
1 1119 SER n 
1 1120 GLY n 
1 1121 ASN n 
1 1122 CYS n 
1 1123 ASP n 
1 1124 VAL n 
1 1125 VAL n 
1 1126 ILE n 
1 1127 GLY n 
1 1128 ILE n 
1 1129 VAL n 
1 1130 ASN n 
1 1131 ASN n 
1 1132 THR n 
1 1133 VAL n 
1 1134 TYR n 
1 1135 ASP n 
1 1136 PRO n 
1 1137 LEU n 
1 1138 GLN n 
1 1139 LEU n 
1 1140 GLU n 
1 1141 LEU n 
1 1142 ASP n 
1 1143 SER n 
1 1144 PHE n 
1 1145 LYS n 
1 1146 GLU n 
1 1147 GLU n 
1 1148 LEU n 
1 1149 ASP n 
1 1150 LYS n 
1 1151 TYR n 
1 1152 PHE n 
1 1153 LYS n 
1 1154 ASN n 
1 1155 HIS n 
1 1156 THR n 
1 1157 SER n 
1 1158 PRO n 
1 1159 ASP n 
1 1160 VAL n 
1 1161 ASP n 
1 1162 LEU n 
1 1163 GLY n 
1 1164 ASP n 
1 1165 ILE n 
1 1166 SER n 
1 1167 GLY n 
1 1168 ILE n 
1 1169 ASN n 
1 1170 ALA n 
1 1171 SER n 
1 1172 VAL n 
1 1173 VAL n 
1 1174 ASN n 
1 1175 ILE n 
1 1176 GLN n 
1 1177 LYS n 
1 1178 GLU n 
1 1179 ILE n 
1 1180 ASP n 
1 1181 ARG n 
1 1182 LEU n 
1 1183 ASN n 
1 1184 GLU n 
1 1185 VAL n 
1 1186 ALA n 
1 1187 LYS n 
1 1188 ASN n 
1 1189 LEU n 
1 1190 ASN n 
1 1191 GLU n 
1 1192 SER n 
1 1193 LEU n 
1 1194 ILE n 
1 1195 ASP n 
1 1196 LEU n 
1 1197 GLN n 
1 1198 GLU n 
1 1199 LEU n 
1 1200 GLY n 
1 1201 LYS n 
1 1202 TYR n 
1 1203 GLU n 
1 1204 GLN n 
1 1205 TYR n 
1 1206 ILE n 
1 1207 LYS n 
1 1208 GLY n 
1 1209 SER n 
1 1210 GLY n 
1 1211 TYR n 
1 1212 ILE n 
1 1213 PRO n 
1 1214 GLU n 
1 1215 ALA n 
1 1216 PRO n 
1 1217 ARG n 
1 1218 ASP n 
1 1219 GLY n 
1 1220 GLN n 
1 1221 ALA n 
1 1222 TYR n 
1 1223 VAL n 
1 1224 ARG n 
1 1225 LYS n 
1 1226 ASP n 
1 1227 GLY n 
1 1228 GLU n 
1 1229 TRP n 
1 1230 VAL n 
1 1231 LEU n 
1 1232 LEU n 
1 1233 SER n 
1 1234 THR n 
1 1235 PHE n 
1 1236 LEU n 
1 1237 GLY n 
1 1238 HIS n 
1 1239 HIS n 
1 1240 HIS n 
1 1241 HIS n 
1 1242 HIS n 
1 1243 HIS n 
2 1    GLN n 
2 2    VAL n 
2 3    GLN n 
2 4    LEU n 
2 5    GLN n 
2 6    GLU n 
2 7    SER n 
2 8    GLY n 
2 9    GLY n 
2 10   GLY n 
2 11   LEU n 
2 12   VAL n 
2 13   GLN n 
2 14   PRO n 
2 15   GLY n 
2 16   GLY n 
2 17   SER n 
2 18   LEU n 
2 19   ARG n 
2 20   LEU n 
2 21   SER n 
2 22   CYS n 
2 23   THR n 
2 24   ALA n 
2 25   SER n 
2 26   GLY n 
2 27   ILE n 
2 28   ALA n 
2 29   LEU n 
2 30   HIS n 
2 31   THR n 
2 32   HIS n 
2 33   ALA n 
2 34   THR n 
2 35   GLY n 
2 36   TRP n 
2 37   PHE n 
2 38   ARG n 
2 39   GLN n 
2 40   ALA n 
2 41   PRO n 
2 42   GLY n 
2 43   LYS n 
2 44   GLU n 
2 45   ARG n 
2 46   GLU n 
2 47   GLY n 
2 48   VAL n 
2 49   SER n 
2 50   CYS n 
2 51   ILE n 
2 52   SER n 
2 53   SER n 
2 54   GLY n 
2 55   ASP n 
2 56   GLY n 
2 57   THR n 
2 58   THR n 
2 59   TYR n 
2 60   TYR n 
2 61   GLU n 
2 62   ASP n 
2 63   SER n 
2 64   VAL n 
2 65   GLU n 
2 66   GLY n 
2 67   ARG n 
2 68   PHE n 
2 69   THR n 
2 70   ILE n 
2 71   SER n 
2 72   ARG n 
2 73   ASP n 
2 74   ASN n 
2 75   ALA n 
2 76   LYS n 
2 77   ASN n 
2 78   THR n 
2 79   VAL n 
2 80   TYR n 
2 81   LEU n 
2 82   GLN n 
2 83   MET n 
2 84   ASN n 
2 85   SER n 
2 86   LEU n 
2 87   LYS n 
2 88   LEU n 
2 89   GLU n 
2 90   ASP n 
2 91   THR n 
2 92   ALA n 
2 93   VAL n 
2 94   TYR n 
2 95   TYR n 
2 96   CYS n 
2 97   ALA n 
2 98   ALA n 
2 99   ASP n 
2 100  PRO n 
2 101  GLY n 
2 102  ALA n 
2 103  VAL n 
2 104  CYS n 
2 105  HIS n 
2 106  SER n 
2 107  GLY n 
2 108  SER n 
2 109  TYR n 
2 110  TYR n 
2 111  TYR n 
2 112  THR n 
2 113  ASP n 
2 114  ASP n 
2 115  ASP n 
2 116  PHE n 
2 117  TYR n 
2 118  TYR n 
2 119  ARG n 
2 120  GLY n 
2 121  GLN n 
2 122  GLY n 
2 123  THR n 
2 124  GLN n 
2 125  VAL n 
2 126  THR n 
2 127  VAL n 
2 128  SER n 
2 129  SER n 
2 130  GLY n 
2 131  GLY n 
2 132  GLN n 
2 133  HIS n 
2 134  HIS n 
2 135  HIS n 
2 136  HIS n 
2 137  HIS n 
2 138  HIS n 
2 139  GLY n 
2 140  ALA n 
2 141  TYR n 
2 142  PRO n 
2 143  TYR n 
2 144  ASP n 
2 145  VAL n 
2 146  PRO n 
2 147  ASP n 
2 148  TYR n 
2 149  ALA n 
2 150  SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 1243 ? ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? 
? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 150  ? ? ?      ? ? ? ? ? ? 'Vicugna pacos'                                   30538   ? ? ? ? ? 
? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?   ?   ?   B . n 
A 1 2    PHE 2    2    ?   ?   ?   B . n 
A 1 3    VAL 3    3    ?   ?   ?   B . n 
A 1 4    PHE 4    4    ?   ?   ?   B . n 
A 1 5    LEU 5    5    ?   ?   ?   B . n 
A 1 6    VAL 6    6    ?   ?   ?   B . n 
A 1 7    LEU 7    7    ?   ?   ?   B . n 
A 1 8    LEU 8    8    ?   ?   ?   B . n 
A 1 9    PRO 9    9    ?   ?   ?   B . n 
A 1 10   LEU 10   10   ?   ?   ?   B . n 
A 1 11   VAL 11   11   ?   ?   ?   B . n 
A 1 12   SER 12   12   ?   ?   ?   B . n 
A 1 13   SER 13   13   ?   ?   ?   B . n 
A 1 14   GLN 14   14   ?   ?   ?   B . n 
A 1 15   CYS 15   15   ?   ?   ?   B . n 
A 1 16   VAL 16   16   ?   ?   ?   B . n 
A 1 17   MET 17   17   ?   ?   ?   B . n 
A 1 18   PRO 18   18   ?   ?   ?   B . n 
A 1 19   LEU 19   19   ?   ?   ?   B . n 
A 1 20   PHE 20   20   ?   ?   ?   B . n 
A 1 21   ASN 21   21   ?   ?   ?   B . n 
A 1 22   LEU 22   22   ?   ?   ?   B . n 
A 1 23   ILE 23   23   ?   ?   ?   B . n 
A 1 24   THR 24   24   ?   ?   ?   B . n 
A 1 25   THR 25   25   ?   ?   ?   B . n 
A 1 26   THR 26   26   ?   ?   ?   B . n 
A 1 27   GLN 27   27   ?   ?   ?   B . n 
A 1 28   SER 28   28   ?   ?   ?   B . n 
A 1 29   TYR 29   29   ?   ?   ?   B . n 
A 1 30   THR 30   30   ?   ?   ?   B . n 
A 1 31   ASN 31   31   ?   ?   ?   B . n 
A 1 32   SER 32   32   ?   ?   ?   B . n 
A 1 33   PHE 33   33   ?   ?   ?   B . n 
A 1 34   THR 34   34   ?   ?   ?   B . n 
A 1 35   ARG 35   35   ?   ?   ?   B . n 
A 1 36   GLY 36   36   ?   ?   ?   B . n 
A 1 37   VAL 37   37   ?   ?   ?   B . n 
A 1 38   TYR 38   38   ?   ?   ?   B . n 
A 1 39   TYR 39   39   ?   ?   ?   B . n 
A 1 40   PRO 40   40   ?   ?   ?   B . n 
A 1 41   ASP 41   41   ?   ?   ?   B . n 
A 1 42   LYS 42   42   ?   ?   ?   B . n 
A 1 43   VAL 43   43   ?   ?   ?   B . n 
A 1 44   PHE 44   44   ?   ?   ?   B . n 
A 1 45   ARG 45   45   ?   ?   ?   B . n 
A 1 46   SER 46   46   ?   ?   ?   B . n 
A 1 47   SER 47   47   ?   ?   ?   B . n 
A 1 48   VAL 48   48   ?   ?   ?   B . n 
A 1 49   LEU 49   49   ?   ?   ?   B . n 
A 1 50   HIS 50   50   ?   ?   ?   B . n 
A 1 51   LEU 51   51   ?   ?   ?   B . n 
A 1 52   THR 52   52   ?   ?   ?   B . n 
A 1 53   GLN 53   53   ?   ?   ?   B . n 
A 1 54   ASP 54   54   ?   ?   ?   B . n 
A 1 55   LEU 55   55   ?   ?   ?   B . n 
A 1 56   PHE 56   56   ?   ?   ?   B . n 
A 1 57   LEU 57   57   ?   ?   ?   B . n 
A 1 58   PRO 58   58   ?   ?   ?   B . n 
A 1 59   PHE 59   59   ?   ?   ?   B . n 
A 1 60   PHE 60   60   ?   ?   ?   B . n 
A 1 61   SER 61   61   ?   ?   ?   B . n 
A 1 62   ASN 62   62   ?   ?   ?   B . n 
A 1 63   VAL 63   63   ?   ?   ?   B . n 
A 1 64   THR 64   64   ?   ?   ?   B . n 
A 1 65   TRP 65   65   ?   ?   ?   B . n 
A 1 66   PHE 66   66   ?   ?   ?   B . n 
A 1 67   HIS 67   67   ?   ?   ?   B . n 
A 1 68   ALA 68   68   ?   ?   ?   B . n 
A 1 69   ILE 69   69   ?   ?   ?   B . n 
A 1 70   SER 70   70   ?   ?   ?   B . n 
A 1 71   GLY 71   71   ?   ?   ?   B . n 
A 1 72   THR 72   72   ?   ?   ?   B . n 
A 1 73   ASN 73   73   ?   ?   ?   B . n 
A 1 74   GLY 74   74   ?   ?   ?   B . n 
A 1 75   THR 75   75   ?   ?   ?   B . n 
A 1 76   LYS 76   76   ?   ?   ?   B . n 
A 1 77   ARG 77   77   ?   ?   ?   B . n 
A 1 78   PHE 78   78   ?   ?   ?   B . n 
A 1 79   ASP 79   79   ?   ?   ?   B . n 
A 1 80   ASN 80   80   ?   ?   ?   B . n 
A 1 81   PRO 81   81   ?   ?   ?   B . n 
A 1 82   VAL 82   82   ?   ?   ?   B . n 
A 1 83   LEU 83   83   ?   ?   ?   B . n 
A 1 84   PRO 84   84   ?   ?   ?   B . n 
A 1 85   PHE 85   85   ?   ?   ?   B . n 
A 1 86   ASN 86   86   ?   ?   ?   B . n 
A 1 87   ASP 87   87   ?   ?   ?   B . n 
A 1 88   GLY 88   88   ?   ?   ?   B . n 
A 1 89   VAL 89   89   ?   ?   ?   B . n 
A 1 90   TYR 90   90   ?   ?   ?   B . n 
A 1 91   PHE 91   91   ?   ?   ?   B . n 
A 1 92   ALA 92   92   ?   ?   ?   B . n 
A 1 93   SER 93   93   ?   ?   ?   B . n 
A 1 94   THR 94   94   ?   ?   ?   B . n 
A 1 95   GLU 95   95   ?   ?   ?   B . n 
A 1 96   LYS 96   96   ?   ?   ?   B . n 
A 1 97   SER 97   97   ?   ?   ?   B . n 
A 1 98   ASN 98   98   ?   ?   ?   B . n 
A 1 99   ILE 99   99   ?   ?   ?   B . n 
A 1 100  ILE 100  100  ?   ?   ?   B . n 
A 1 101  ARG 101  101  ?   ?   ?   B . n 
A 1 102  GLY 102  102  ?   ?   ?   B . n 
A 1 103  TRP 103  103  ?   ?   ?   B . n 
A 1 104  ILE 104  104  ?   ?   ?   B . n 
A 1 105  PHE 105  105  ?   ?   ?   B . n 
A 1 106  GLY 106  106  ?   ?   ?   B . n 
A 1 107  THR 107  107  ?   ?   ?   B . n 
A 1 108  THR 108  108  ?   ?   ?   B . n 
A 1 109  LEU 109  109  ?   ?   ?   B . n 
A 1 110  ASP 110  110  ?   ?   ?   B . n 
A 1 111  SER 111  111  ?   ?   ?   B . n 
A 1 112  LYS 112  112  ?   ?   ?   B . n 
A 1 113  THR 113  113  ?   ?   ?   B . n 
A 1 114  GLN 114  114  ?   ?   ?   B . n 
A 1 115  SER 115  115  ?   ?   ?   B . n 
A 1 116  LEU 116  116  ?   ?   ?   B . n 
A 1 117  LEU 117  117  ?   ?   ?   B . n 
A 1 118  ILE 118  118  ?   ?   ?   B . n 
A 1 119  VAL 119  119  ?   ?   ?   B . n 
A 1 120  ASN 120  120  ?   ?   ?   B . n 
A 1 121  ASN 121  121  ?   ?   ?   B . n 
A 1 122  ALA 122  122  ?   ?   ?   B . n 
A 1 123  THR 123  123  ?   ?   ?   B . n 
A 1 124  ASN 124  124  ?   ?   ?   B . n 
A 1 125  VAL 125  125  ?   ?   ?   B . n 
A 1 126  PHE 126  126  ?   ?   ?   B . n 
A 1 127  ILE 127  127  ?   ?   ?   B . n 
A 1 128  LYS 128  128  ?   ?   ?   B . n 
A 1 129  VAL 129  129  ?   ?   ?   B . n 
A 1 130  CYS 130  130  ?   ?   ?   B . n 
A 1 131  GLU 131  131  ?   ?   ?   B . n 
A 1 132  PHE 132  132  ?   ?   ?   B . n 
A 1 133  GLN 133  133  ?   ?   ?   B . n 
A 1 134  PHE 134  134  ?   ?   ?   B . n 
A 1 135  CYS 135  135  ?   ?   ?   B . n 
A 1 136  ASN 136  136  ?   ?   ?   B . n 
A 1 137  ASP 137  137  ?   ?   ?   B . n 
A 1 138  PRO 138  138  ?   ?   ?   B . n 
A 1 139  PHE 139  139  ?   ?   ?   B . n 
A 1 140  LEU 140  140  ?   ?   ?   B . n 
A 1 141  ASP 141  141  ?   ?   ?   B . n 
A 1 142  VAL 142  142  ?   ?   ?   B . n 
A 1 143  TYR 143  143  ?   ?   ?   B . n 
A 1 144  HIS 144  144  ?   ?   ?   B . n 
A 1 145  LYS 145  145  ?   ?   ?   B . n 
A 1 146  ASN 146  146  ?   ?   ?   B . n 
A 1 147  ASN 147  147  ?   ?   ?   B . n 
A 1 148  LYS 148  148  ?   ?   ?   B . n 
A 1 149  SER 149  149  ?   ?   ?   B . n 
A 1 150  TRP 150  150  ?   ?   ?   B . n 
A 1 151  MET 151  151  ?   ?   ?   B . n 
A 1 152  GLU 152  152  ?   ?   ?   B . n 
A 1 153  SER 153  153  ?   ?   ?   B . n 
A 1 154  GLU 154  154  ?   ?   ?   B . n 
A 1 155  SER 155  155  ?   ?   ?   B . n 
A 1 156  GLY 156  156  ?   ?   ?   B . n 
A 1 157  VAL 157  157  ?   ?   ?   B . n 
A 1 158  TYR 158  158  ?   ?   ?   B . n 
A 1 159  SER 159  159  ?   ?   ?   B . n 
A 1 160  SER 160  160  ?   ?   ?   B . n 
A 1 161  ALA 161  161  ?   ?   ?   B . n 
A 1 162  ASN 162  162  ?   ?   ?   B . n 
A 1 163  ASN 163  163  ?   ?   ?   B . n 
A 1 164  CYS 164  164  ?   ?   ?   B . n 
A 1 165  THR 165  165  ?   ?   ?   B . n 
A 1 166  PHE 166  166  ?   ?   ?   B . n 
A 1 167  GLU 167  167  ?   ?   ?   B . n 
A 1 168  TYR 168  168  ?   ?   ?   B . n 
A 1 169  VAL 169  169  ?   ?   ?   B . n 
A 1 170  SER 170  170  ?   ?   ?   B . n 
A 1 171  GLN 171  171  ?   ?   ?   B . n 
A 1 172  PRO 172  172  ?   ?   ?   B . n 
A 1 173  PHE 173  173  ?   ?   ?   B . n 
A 1 174  LEU 174  174  ?   ?   ?   B . n 
A 1 175  MET 175  175  ?   ?   ?   B . n 
A 1 176  ASP 176  176  ?   ?   ?   B . n 
A 1 177  LEU 177  177  ?   ?   ?   B . n 
A 1 178  GLU 178  178  ?   ?   ?   B . n 
A 1 179  GLY 179  179  ?   ?   ?   B . n 
A 1 180  LYS 180  180  ?   ?   ?   B . n 
A 1 181  GLN 181  181  ?   ?   ?   B . n 
A 1 182  GLY 182  182  ?   ?   ?   B . n 
A 1 183  ASN 183  183  ?   ?   ?   B . n 
A 1 184  PHE 184  184  ?   ?   ?   B . n 
A 1 185  LYS 185  185  ?   ?   ?   B . n 
A 1 186  ASN 186  186  ?   ?   ?   B . n 
A 1 187  LEU 187  187  ?   ?   ?   B . n 
A 1 188  ARG 188  188  ?   ?   ?   B . n 
A 1 189  GLU 189  189  ?   ?   ?   B . n 
A 1 190  PHE 190  190  ?   ?   ?   B . n 
A 1 191  VAL 191  191  ?   ?   ?   B . n 
A 1 192  PHE 192  192  ?   ?   ?   B . n 
A 1 193  LYS 193  193  ?   ?   ?   B . n 
A 1 194  ASN 194  194  ?   ?   ?   B . n 
A 1 195  ILE 195  195  ?   ?   ?   B . n 
A 1 196  ASP 196  196  ?   ?   ?   B . n 
A 1 197  GLY 197  197  ?   ?   ?   B . n 
A 1 198  TYR 198  198  ?   ?   ?   B . n 
A 1 199  PHE 199  199  ?   ?   ?   B . n 
A 1 200  LYS 200  200  ?   ?   ?   B . n 
A 1 201  ILE 201  201  ?   ?   ?   B . n 
A 1 202  TYR 202  202  ?   ?   ?   B . n 
A 1 203  SER 203  203  ?   ?   ?   B . n 
A 1 204  LYS 204  204  ?   ?   ?   B . n 
A 1 205  HIS 205  205  ?   ?   ?   B . n 
A 1 206  THR 206  206  ?   ?   ?   B . n 
A 1 207  PRO 207  207  ?   ?   ?   B . n 
A 1 208  ILE 208  208  ?   ?   ?   B . n 
A 1 209  ILE 209  209  ?   ?   ?   B . n 
A 1 210  GLY 210  210  ?   ?   ?   B . n 
A 1 211  ARG 211  211  ?   ?   ?   B . n 
A 1 212  ASP 212  212  ?   ?   ?   B . n 
A 1 213  PHE 213  213  ?   ?   ?   B . n 
A 1 214  PRO 214  214  ?   ?   ?   B . n 
A 1 215  GLN 215  215  ?   ?   ?   B . n 
A 1 216  GLY 216  216  ?   ?   ?   B . n 
A 1 217  PHE 217  217  ?   ?   ?   B . n 
A 1 218  SER 218  218  ?   ?   ?   B . n 
A 1 219  ALA 219  219  ?   ?   ?   B . n 
A 1 220  LEU 220  220  ?   ?   ?   B . n 
A 1 221  GLU 221  221  ?   ?   ?   B . n 
A 1 222  PRO 222  222  ?   ?   ?   B . n 
A 1 223  LEU 223  223  ?   ?   ?   B . n 
A 1 224  VAL 224  224  ?   ?   ?   B . n 
A 1 225  ASP 225  225  ?   ?   ?   B . n 
A 1 226  LEU 226  226  ?   ?   ?   B . n 
A 1 227  PRO 227  227  ?   ?   ?   B . n 
A 1 228  ILE 228  228  ?   ?   ?   B . n 
A 1 229  GLY 229  229  ?   ?   ?   B . n 
A 1 230  ILE 230  230  ?   ?   ?   B . n 
A 1 231  ASN 231  231  ?   ?   ?   B . n 
A 1 232  ILE 232  232  ?   ?   ?   B . n 
A 1 233  THR 233  233  ?   ?   ?   B . n 
A 1 234  ARG 234  234  ?   ?   ?   B . n 
A 1 235  PHE 235  235  ?   ?   ?   B . n 
A 1 236  GLN 236  236  ?   ?   ?   B . n 
A 1 237  THR 237  237  ?   ?   ?   B . n 
A 1 238  LEU 238  238  ?   ?   ?   B . n 
A 1 239  LEU 239  239  ?   ?   ?   B . n 
A 1 240  ALA 240  240  ?   ?   ?   B . n 
A 1 241  LEU 241  241  ?   ?   ?   B . n 
A 1 242  ASN 242  242  ?   ?   ?   B . n 
A 1 243  ARG 243  243  ?   ?   ?   B . n 
A 1 244  SER 244  244  ?   ?   ?   B . n 
A 1 245  TYR 245  245  ?   ?   ?   B . n 
A 1 246  LEU 246  246  ?   ?   ?   B . n 
A 1 247  THR 247  247  ?   ?   ?   B . n 
A 1 248  PRO 248  248  ?   ?   ?   B . n 
A 1 249  GLY 249  249  ?   ?   ?   B . n 
A 1 250  ASP 250  250  ?   ?   ?   B . n 
A 1 251  SER 251  251  ?   ?   ?   B . n 
A 1 252  SER 252  252  ?   ?   ?   B . n 
A 1 253  SER 253  253  ?   ?   ?   B . n 
A 1 254  GLY 254  254  ?   ?   ?   B . n 
A 1 255  TRP 255  255  ?   ?   ?   B . n 
A 1 256  THR 256  256  ?   ?   ?   B . n 
A 1 257  ALA 257  257  ?   ?   ?   B . n 
A 1 258  GLY 258  258  ?   ?   ?   B . n 
A 1 259  ALA 259  259  ?   ?   ?   B . n 
A 1 260  ALA 260  260  ?   ?   ?   B . n 
A 1 261  ASP 261  261  ?   ?   ?   B . n 
A 1 262  TYR 262  262  ?   ?   ?   B . n 
A 1 263  TYR 263  263  ?   ?   ?   B . n 
A 1 264  VAL 264  264  ?   ?   ?   B . n 
A 1 265  GLY 265  265  ?   ?   ?   B . n 
A 1 266  TYR 266  266  ?   ?   ?   B . n 
A 1 267  LEU 267  267  ?   ?   ?   B . n 
A 1 268  GLN 268  268  ?   ?   ?   B . n 
A 1 269  PRO 269  269  ?   ?   ?   B . n 
A 1 270  ARG 270  270  ?   ?   ?   B . n 
A 1 271  THR 271  271  ?   ?   ?   B . n 
A 1 272  PHE 272  272  ?   ?   ?   B . n 
A 1 273  LEU 273  273  ?   ?   ?   B . n 
A 1 274  LEU 274  274  ?   ?   ?   B . n 
A 1 275  LYS 275  275  ?   ?   ?   B . n 
A 1 276  TYR 276  276  ?   ?   ?   B . n 
A 1 277  ASN 277  277  ?   ?   ?   B . n 
A 1 278  GLU 278  278  ?   ?   ?   B . n 
A 1 279  ASN 279  279  ?   ?   ?   B . n 
A 1 280  GLY 280  280  ?   ?   ?   B . n 
A 1 281  THR 281  281  ?   ?   ?   B . n 
A 1 282  ILE 282  282  ?   ?   ?   B . n 
A 1 283  THR 283  283  ?   ?   ?   B . n 
A 1 284  ASP 284  284  ?   ?   ?   B . n 
A 1 285  ALA 285  285  ?   ?   ?   B . n 
A 1 286  VAL 286  286  ?   ?   ?   B . n 
A 1 287  ASP 287  287  ?   ?   ?   B . n 
A 1 288  CYS 288  288  ?   ?   ?   B . n 
A 1 289  ALA 289  289  ?   ?   ?   B . n 
A 1 290  LEU 290  290  ?   ?   ?   B . n 
A 1 291  ASP 291  291  ?   ?   ?   B . n 
A 1 292  PRO 292  292  ?   ?   ?   B . n 
A 1 293  LEU 293  293  ?   ?   ?   B . n 
A 1 294  SER 294  294  ?   ?   ?   B . n 
A 1 295  GLU 295  295  ?   ?   ?   B . n 
A 1 296  THR 296  296  ?   ?   ?   B . n 
A 1 297  LYS 297  297  ?   ?   ?   B . n 
A 1 298  CYS 298  298  ?   ?   ?   B . n 
A 1 299  THR 299  299  ?   ?   ?   B . n 
A 1 300  LEU 300  300  ?   ?   ?   B . n 
A 1 301  LYS 301  301  ?   ?   ?   B . n 
A 1 302  SER 302  302  ?   ?   ?   B . n 
A 1 303  PHE 303  303  ?   ?   ?   B . n 
A 1 304  THR 304  304  ?   ?   ?   B . n 
A 1 305  VAL 305  305  ?   ?   ?   B . n 
A 1 306  GLU 306  306  ?   ?   ?   B . n 
A 1 307  LYS 307  307  ?   ?   ?   B . n 
A 1 308  GLY 308  308  ?   ?   ?   B . n 
A 1 309  ILE 309  309  ?   ?   ?   B . n 
A 1 310  TYR 310  310  ?   ?   ?   B . n 
A 1 311  GLN 311  311  ?   ?   ?   B . n 
A 1 312  THR 312  312  ?   ?   ?   B . n 
A 1 313  SER 313  313  ?   ?   ?   B . n 
A 1 314  ASN 314  314  ?   ?   ?   B . n 
A 1 315  PHE 315  315  ?   ?   ?   B . n 
A 1 316  ARG 316  316  ?   ?   ?   B . n 
A 1 317  VAL 317  317  ?   ?   ?   B . n 
A 1 318  GLN 318  318  ?   ?   ?   B . n 
A 1 319  PRO 319  319  ?   ?   ?   B . n 
A 1 320  THR 320  320  ?   ?   ?   B . n 
A 1 321  GLU 321  321  ?   ?   ?   B . n 
A 1 322  SER 322  322  ?   ?   ?   B . n 
A 1 323  ILE 323  323  ?   ?   ?   B . n 
A 1 324  VAL 324  324  ?   ?   ?   B . n 
A 1 325  ARG 325  325  ?   ?   ?   B . n 
A 1 326  PHE 326  326  326 PHE PHE B . n 
A 1 327  PRO 327  327  327 PRO PRO B . n 
A 1 328  ASN 328  328  328 ASN ASN B . n 
A 1 329  VAL 329  329  329 VAL VAL B . n 
A 1 330  THR 330  330  330 THR THR B . n 
A 1 331  ASN 331  331  331 ASN ASN B . n 
A 1 332  LEU 332  332  332 LEU LEU B . n 
A 1 333  CYS 333  333  333 CYS CYS B . n 
A 1 334  PRO 334  334  334 PRO PRO B . n 
A 1 335  PHE 335  335  335 PHE PHE B . n 
A 1 336  HIS 336  336  336 HIS HIS B . n 
A 1 337  GLU 337  337  337 GLU GLU B . n 
A 1 338  VAL 338  338  338 VAL VAL B . n 
A 1 339  PHE 339  339  339 PHE PHE B . n 
A 1 340  ASN 340  340  340 ASN ASN B . n 
A 1 341  ALA 341  341  341 ALA ALA B . n 
A 1 342  THR 342  342  342 THR THR B . n 
A 1 343  ARG 343  343  343 ARG ARG B . n 
A 1 344  PHE 344  344  344 PHE PHE B . n 
A 1 345  ALA 345  345  345 ALA ALA B . n 
A 1 346  SER 346  346  346 SER SER B . n 
A 1 347  VAL 347  347  347 VAL VAL B . n 
A 1 348  TYR 348  348  348 TYR TYR B . n 
A 1 349  ALA 349  349  349 ALA ALA B . n 
A 1 350  TRP 350  350  350 TRP TRP B . n 
A 1 351  ASN 351  351  351 ASN ASN B . n 
A 1 352  ARG 352  352  352 ARG ARG B . n 
A 1 353  THR 353  353  353 THR THR B . n 
A 1 354  ARG 354  354  354 ARG ARG B . n 
A 1 355  ILE 355  355  355 ILE ILE B . n 
A 1 356  SER 356  356  356 SER SER B . n 
A 1 357  ASN 357  357  357 ASN ASN B . n 
A 1 358  CYS 358  358  358 CYS CYS B . n 
A 1 359  VAL 359  359  359 VAL VAL B . n 
A 1 360  ALA 360  360  360 ALA ALA B . n 
A 1 361  ASP 361  361  361 ASP ASP B . n 
A 1 362  TYR 362  362  362 TYR TYR B . n 
A 1 363  SER 363  363  363 SER SER B . n 
A 1 364  VAL 364  364  364 VAL VAL B . n 
A 1 365  LEU 365  365  365 LEU LEU B . n 
A 1 366  TYR 366  366  366 TYR TYR B . n 
A 1 367  ASN 367  367  367 ASN ASN B . n 
A 1 368  PHE 368  368  368 PHE PHE B . n 
A 1 369  ALA 369  369  369 ALA ALA B . n 
A 1 370  PRO 370  370  370 PRO PRO B . n 
A 1 371  PHE 371  371  371 PHE PHE B . n 
A 1 372  PHE 372  372  372 PHE PHE B . n 
A 1 373  ALA 373  373  373 ALA ALA B . n 
A 1 374  PHE 374  374  374 PHE PHE B . n 
A 1 375  LYS 375  375  375 LYS LYS B . n 
A 1 376  CYS 376  376  376 CYS CYS B . n 
A 1 377  TYR 377  377  377 TYR TYR B . n 
A 1 378  GLY 378  378  378 GLY GLY B . n 
A 1 379  VAL 379  379  379 VAL VAL B . n 
A 1 380  SER 380  380  380 SER SER B . n 
A 1 381  PRO 381  381  381 PRO PRO B . n 
A 1 382  THR 382  382  382 THR THR B . n 
A 1 383  LYS 383  383  383 LYS LYS B . n 
A 1 384  LEU 384  384  384 LEU LEU B . n 
A 1 385  ASN 385  385  385 ASN ASN B . n 
A 1 386  ASP 386  386  386 ASP ASP B . n 
A 1 387  LEU 387  387  387 LEU LEU B . n 
A 1 388  CYS 388  388  388 CYS CYS B . n 
A 1 389  PHE 389  389  389 PHE PHE B . n 
A 1 390  THR 390  390  390 THR THR B . n 
A 1 391  ASN 391  391  391 ASN ASN B . n 
A 1 392  VAL 392  392  392 VAL VAL B . n 
A 1 393  TYR 393  393  393 TYR TYR B . n 
A 1 394  ALA 394  394  394 ALA ALA B . n 
A 1 395  ASP 395  395  395 ASP ASP B . n 
A 1 396  SER 396  396  396 SER SER B . n 
A 1 397  PHE 397  397  397 PHE PHE B . n 
A 1 398  VAL 398  398  398 VAL VAL B . n 
A 1 399  ILE 399  399  399 ILE ILE B . n 
A 1 400  LYS 400  400  400 LYS LYS B . n 
A 1 401  GLY 401  401  401 GLY GLY B . n 
A 1 402  ASN 402  402  402 ASN ASN B . n 
A 1 403  GLU 403  403  403 GLU GLU B . n 
A 1 404  VAL 404  404  404 VAL VAL B . n 
A 1 405  SER 405  405  405 SER SER B . n 
A 1 406  GLN 406  406  406 GLN GLN B . n 
A 1 407  ILE 407  407  407 ILE ILE B . n 
A 1 408  ALA 408  408  408 ALA ALA B . n 
A 1 409  PRO 409  409  409 PRO PRO B . n 
A 1 410  GLY 410  410  410 GLY GLY B . n 
A 1 411  GLN 411  411  411 GLN GLN B . n 
A 1 412  THR 412  412  412 THR THR B . n 
A 1 413  GLY 413  413  413 GLY GLY B . n 
A 1 414  ASN 414  414  414 ASN ASN B . n 
A 1 415  ILE 415  415  415 ILE ILE B . n 
A 1 416  ALA 416  416  416 ALA ALA B . n 
A 1 417  ASP 417  417  417 ASP ASP B . n 
A 1 418  TYR 418  418  418 TYR TYR B . n 
A 1 419  ASN 419  419  419 ASN ASN B . n 
A 1 420  TYR 420  420  420 TYR TYR B . n 
A 1 421  LYS 421  421  421 LYS LYS B . n 
A 1 422  LEU 422  422  422 LEU LEU B . n 
A 1 423  PRO 423  423  423 PRO PRO B . n 
A 1 424  ASP 424  424  424 ASP ASP B . n 
A 1 425  ASP 425  425  425 ASP ASP B . n 
A 1 426  PHE 426  426  426 PHE PHE B . n 
A 1 427  THR 427  427  427 THR THR B . n 
A 1 428  GLY 428  428  428 GLY GLY B . n 
A 1 429  CYS 429  429  429 CYS CYS B . n 
A 1 430  VAL 430  430  430 VAL VAL B . n 
A 1 431  ILE 431  431  431 ILE ILE B . n 
A 1 432  ALA 432  432  432 ALA ALA B . n 
A 1 433  TRP 433  433  433 TRP TRP B . n 
A 1 434  ASN 434  434  434 ASN ASN B . n 
A 1 435  SER 435  435  435 SER SER B . n 
A 1 436  ASN 436  436  436 ASN ASN B . n 
A 1 437  LYS 437  437  437 LYS LYS B . n 
A 1 438  LEU 438  438  438 LEU LEU B . n 
A 1 439  ASP 439  439  439 ASP ASP B . n 
A 1 440  SER 440  440  440 SER SER B . n 
A 1 441  LYS 441  441  441 LYS LYS B . n 
A 1 442  HIS 442  442  442 HIS HIS B . n 
A 1 443  SER 443  443  443 SER SER B . n 
A 1 444  GLY 444  444  444 GLY GLY B . n 
A 1 445  ASN 445  445  445 ASN ASN B . n 
A 1 446  TYR 446  446  446 TYR TYR B . n 
A 1 447  ASP 447  447  447 ASP ASP B . n 
A 1 448  TYR 448  448  448 TYR TYR B . n 
A 1 449  TRP 449  449  449 TRP TRP B . n 
A 1 450  TYR 450  450  450 TYR TYR B . n 
A 1 451  ARG 451  451  451 ARG ARG B . n 
A 1 452  SER 452  452  452 SER SER B . n 
A 1 453  PHE 453  453  453 PHE PHE B . n 
A 1 454  ARG 454  454  454 ARG ARG B . n 
A 1 455  LYS 455  455  455 LYS LYS B . n 
A 1 456  SER 456  456  456 SER SER B . n 
A 1 457  LYS 457  457  457 LYS LYS B . n 
A 1 458  LEU 458  458  458 LEU LEU B . n 
A 1 459  LYS 459  459  459 LYS LYS B . n 
A 1 460  PRO 460  460  460 PRO PRO B . n 
A 1 461  PHE 461  461  461 PHE PHE B . n 
A 1 462  GLU 462  462  462 GLU GLU B . n 
A 1 463  ARG 463  463  463 ARG ARG B . n 
A 1 464  ASP 464  464  464 ASP ASP B . n 
A 1 465  ILE 465  465  465 ILE ILE B . n 
A 1 466  SER 466  466  466 SER SER B . n 
A 1 467  THR 467  467  467 THR THR B . n 
A 1 468  GLU 468  468  468 GLU GLU B . n 
A 1 469  ILE 469  469  469 ILE ILE B . n 
A 1 470  TYR 470  470  470 TYR TYR B . n 
A 1 471  GLN 471  471  471 GLN GLN B . n 
A 1 472  ALA 472  472  472 ALA ALA B . n 
A 1 473  GLY 473  473  473 GLY GLY B . n 
A 1 474  ASN 474  474  474 ASN ASN B . n 
A 1 475  LYS 475  475  475 LYS LYS B . n 
A 1 476  PRO 476  476  476 PRO PRO B . n 
A 1 477  CYS 477  477  477 CYS CYS B . n 
A 1 478  LYS 478  478  478 LYS LYS B . n 
A 1 479  GLY 479  479  479 GLY GLY B . n 
A 1 480  LYS 480  480  480 LYS LYS B . n 
A 1 481  GLY 481  481  481 GLY GLY B . n 
A 1 482  PRO 482  482  482 PRO PRO B . n 
A 1 483  ASN 483  483  483 ASN ASN B . n 
A 1 484  CYS 484  484  484 CYS CYS B . n 
A 1 485  TYR 485  485  485 TYR TYR B . n 
A 1 486  PHE 486  486  486 PHE PHE B . n 
A 1 487  PRO 487  487  487 PRO PRO B . n 
A 1 488  LEU 488  488  488 LEU LEU B . n 
A 1 489  GLN 489  489  489 GLN GLN B . n 
A 1 490  SER 490  490  490 SER SER B . n 
A 1 491  TYR 491  491  491 TYR TYR B . n 
A 1 492  GLY 492  492  492 GLY GLY B . n 
A 1 493  PHE 493  493  493 PHE PHE B . n 
A 1 494  ARG 494  494  494 ARG ARG B . n 
A 1 495  PRO 495  495  495 PRO PRO B . n 
A 1 496  THR 496  496  496 THR THR B . n 
A 1 497  TYR 497  497  497 TYR TYR B . n 
A 1 498  GLY 498  498  498 GLY GLY B . n 
A 1 499  VAL 499  499  499 VAL VAL B . n 
A 1 500  GLY 500  500  500 GLY GLY B . n 
A 1 501  HIS 501  501  501 HIS HIS B . n 
A 1 502  GLN 502  502  502 GLN GLN B . n 
A 1 503  PRO 503  503  503 PRO PRO B . n 
A 1 504  TYR 504  504  504 TYR TYR B . n 
A 1 505  ARG 505  505  505 ARG ARG B . n 
A 1 506  VAL 506  506  506 VAL VAL B . n 
A 1 507  VAL 507  507  507 VAL VAL B . n 
A 1 508  VAL 508  508  508 VAL VAL B . n 
A 1 509  LEU 509  509  509 LEU LEU B . n 
A 1 510  SER 510  510  510 SER SER B . n 
A 1 511  PHE 511  511  511 PHE PHE B . n 
A 1 512  GLU 512  512  512 GLU GLU B . n 
A 1 513  LEU 513  513  513 LEU LEU B . n 
A 1 514  LEU 514  514  514 LEU LEU B . n 
A 1 515  HIS 515  515  515 HIS HIS B . n 
A 1 516  ALA 516  516  516 ALA ALA B . n 
A 1 517  PRO 517  517  517 PRO PRO B . n 
A 1 518  ALA 518  518  518 ALA ALA B . n 
A 1 519  THR 519  519  519 THR THR B . n 
A 1 520  VAL 520  520  520 VAL VAL B . n 
A 1 521  CYS 521  521  521 CYS CYS B . n 
A 1 522  GLY 522  522  522 GLY GLY B . n 
A 1 523  PRO 523  523  523 PRO PRO B . n 
A 1 524  LYS 524  524  524 LYS LYS B . n 
A 1 525  LYS 525  525  525 LYS LYS B . n 
A 1 526  SER 526  526  ?   ?   ?   B . n 
A 1 527  THR 527  527  ?   ?   ?   B . n 
A 1 528  ASN 528  528  ?   ?   ?   B . n 
A 1 529  LEU 529  529  ?   ?   ?   B . n 
A 1 530  VAL 530  530  ?   ?   ?   B . n 
A 1 531  LYS 531  531  ?   ?   ?   B . n 
A 1 532  ASN 532  532  ?   ?   ?   B . n 
A 1 533  LYS 533  533  ?   ?   ?   B . n 
A 1 534  CYS 534  534  ?   ?   ?   B . n 
A 1 535  VAL 535  535  ?   ?   ?   B . n 
A 1 536  ASN 536  536  ?   ?   ?   B . n 
A 1 537  PHE 537  537  ?   ?   ?   B . n 
A 1 538  ASN 538  538  ?   ?   ?   B . n 
A 1 539  PHE 539  539  ?   ?   ?   B . n 
A 1 540  ASN 540  540  ?   ?   ?   B . n 
A 1 541  GLY 541  541  ?   ?   ?   B . n 
A 1 542  LEU 542  542  ?   ?   ?   B . n 
A 1 543  THR 543  543  ?   ?   ?   B . n 
A 1 544  GLY 544  544  ?   ?   ?   B . n 
A 1 545  THR 545  545  ?   ?   ?   B . n 
A 1 546  GLY 546  546  ?   ?   ?   B . n 
A 1 547  VAL 547  547  ?   ?   ?   B . n 
A 1 548  LEU 548  548  ?   ?   ?   B . n 
A 1 549  THR 549  549  ?   ?   ?   B . n 
A 1 550  LYS 550  550  ?   ?   ?   B . n 
A 1 551  SER 551  551  ?   ?   ?   B . n 
A 1 552  ASN 552  552  ?   ?   ?   B . n 
A 1 553  LYS 553  553  ?   ?   ?   B . n 
A 1 554  LYS 554  554  ?   ?   ?   B . n 
A 1 555  PHE 555  555  ?   ?   ?   B . n 
A 1 556  LEU 556  556  ?   ?   ?   B . n 
A 1 557  PRO 557  557  ?   ?   ?   B . n 
A 1 558  PHE 558  558  ?   ?   ?   B . n 
A 1 559  GLN 559  559  ?   ?   ?   B . n 
A 1 560  GLN 560  560  ?   ?   ?   B . n 
A 1 561  PHE 561  561  ?   ?   ?   B . n 
A 1 562  GLY 562  562  ?   ?   ?   B . n 
A 1 563  ARG 563  563  ?   ?   ?   B . n 
A 1 564  ASP 564  564  ?   ?   ?   B . n 
A 1 565  ILE 565  565  ?   ?   ?   B . n 
A 1 566  VAL 566  566  ?   ?   ?   B . n 
A 1 567  ASP 567  567  ?   ?   ?   B . n 
A 1 568  THR 568  568  ?   ?   ?   B . n 
A 1 569  THR 569  569  ?   ?   ?   B . n 
A 1 570  ASP 570  570  ?   ?   ?   B . n 
A 1 571  ALA 571  571  ?   ?   ?   B . n 
A 1 572  VAL 572  572  ?   ?   ?   B . n 
A 1 573  ARG 573  573  ?   ?   ?   B . n 
A 1 574  ASP 574  574  ?   ?   ?   B . n 
A 1 575  PRO 575  575  ?   ?   ?   B . n 
A 1 576  GLN 576  576  ?   ?   ?   B . n 
A 1 577  THR 577  577  ?   ?   ?   B . n 
A 1 578  LEU 578  578  ?   ?   ?   B . n 
A 1 579  GLU 579  579  ?   ?   ?   B . n 
A 1 580  ILE 580  580  ?   ?   ?   B . n 
A 1 581  LEU 581  581  ?   ?   ?   B . n 
A 1 582  ASP 582  582  ?   ?   ?   B . n 
A 1 583  ILE 583  583  ?   ?   ?   B . n 
A 1 584  THR 584  584  ?   ?   ?   B . n 
A 1 585  PRO 585  585  ?   ?   ?   B . n 
A 1 586  CYS 586  586  ?   ?   ?   B . n 
A 1 587  SER 587  587  ?   ?   ?   B . n 
A 1 588  PHE 588  588  ?   ?   ?   B . n 
A 1 589  GLY 589  589  ?   ?   ?   B . n 
A 1 590  GLY 590  590  ?   ?   ?   B . n 
A 1 591  VAL 591  591  ?   ?   ?   B . n 
A 1 592  SER 592  592  ?   ?   ?   B . n 
A 1 593  VAL 593  593  ?   ?   ?   B . n 
A 1 594  ILE 594  594  ?   ?   ?   B . n 
A 1 595  THR 595  595  ?   ?   ?   B . n 
A 1 596  PRO 596  596  ?   ?   ?   B . n 
A 1 597  GLY 597  597  ?   ?   ?   B . n 
A 1 598  THR 598  598  ?   ?   ?   B . n 
A 1 599  ASN 599  599  ?   ?   ?   B . n 
A 1 600  THR 600  600  ?   ?   ?   B . n 
A 1 601  SER 601  601  ?   ?   ?   B . n 
A 1 602  ASN 602  602  ?   ?   ?   B . n 
A 1 603  GLN 603  603  ?   ?   ?   B . n 
A 1 604  VAL 604  604  ?   ?   ?   B . n 
A 1 605  ALA 605  605  ?   ?   ?   B . n 
A 1 606  VAL 606  606  ?   ?   ?   B . n 
A 1 607  LEU 607  607  ?   ?   ?   B . n 
A 1 608  TYR 608  608  ?   ?   ?   B . n 
A 1 609  GLN 609  609  ?   ?   ?   B . n 
A 1 610  GLY 610  610  ?   ?   ?   B . n 
A 1 611  VAL 611  611  ?   ?   ?   B . n 
A 1 612  ASN 612  612  ?   ?   ?   B . n 
A 1 613  CYS 613  613  ?   ?   ?   B . n 
A 1 614  THR 614  614  ?   ?   ?   B . n 
A 1 615  GLU 615  615  ?   ?   ?   B . n 
A 1 616  VAL 616  616  ?   ?   ?   B . n 
A 1 617  SER 617  617  ?   ?   ?   B . n 
A 1 618  VAL 618  618  ?   ?   ?   B . n 
A 1 619  ALA 619  619  ?   ?   ?   B . n 
A 1 620  ILE 620  620  ?   ?   ?   B . n 
A 1 621  HIS 621  621  ?   ?   ?   B . n 
A 1 622  ALA 622  622  ?   ?   ?   B . n 
A 1 623  ASP 623  623  ?   ?   ?   B . n 
A 1 624  GLN 624  624  ?   ?   ?   B . n 
A 1 625  LEU 625  625  ?   ?   ?   B . n 
A 1 626  THR 626  626  ?   ?   ?   B . n 
A 1 627  PRO 627  627  ?   ?   ?   B . n 
A 1 628  THR 628  628  ?   ?   ?   B . n 
A 1 629  TRP 629  629  ?   ?   ?   B . n 
A 1 630  ARG 630  630  ?   ?   ?   B . n 
A 1 631  VAL 631  631  ?   ?   ?   B . n 
A 1 632  TYR 632  632  ?   ?   ?   B . n 
A 1 633  SER 633  633  ?   ?   ?   B . n 
A 1 634  THR 634  634  ?   ?   ?   B . n 
A 1 635  GLY 635  635  ?   ?   ?   B . n 
A 1 636  SER 636  636  ?   ?   ?   B . n 
A 1 637  ASN 637  637  ?   ?   ?   B . n 
A 1 638  VAL 638  638  ?   ?   ?   B . n 
A 1 639  PHE 639  639  ?   ?   ?   B . n 
A 1 640  GLN 640  640  ?   ?   ?   B . n 
A 1 641  THR 641  641  ?   ?   ?   B . n 
A 1 642  ARG 642  642  ?   ?   ?   B . n 
A 1 643  ALA 643  643  ?   ?   ?   B . n 
A 1 644  GLY 644  644  ?   ?   ?   B . n 
A 1 645  CYS 645  645  ?   ?   ?   B . n 
A 1 646  LEU 646  646  ?   ?   ?   B . n 
A 1 647  ILE 647  647  ?   ?   ?   B . n 
A 1 648  GLY 648  648  ?   ?   ?   B . n 
A 1 649  ALA 649  649  ?   ?   ?   B . n 
A 1 650  GLU 650  650  ?   ?   ?   B . n 
A 1 651  TYR 651  651  ?   ?   ?   B . n 
A 1 652  VAL 652  652  ?   ?   ?   B . n 
A 1 653  ASN 653  653  ?   ?   ?   B . n 
A 1 654  ASN 654  654  ?   ?   ?   B . n 
A 1 655  SER 655  655  ?   ?   ?   B . n 
A 1 656  TYR 656  656  ?   ?   ?   B . n 
A 1 657  GLU 657  657  ?   ?   ?   B . n 
A 1 658  CYS 658  658  ?   ?   ?   B . n 
A 1 659  ASP 659  659  ?   ?   ?   B . n 
A 1 660  ILE 660  660  ?   ?   ?   B . n 
A 1 661  PRO 661  661  ?   ?   ?   B . n 
A 1 662  ILE 662  662  ?   ?   ?   B . n 
A 1 663  GLY 663  663  ?   ?   ?   B . n 
A 1 664  ALA 664  664  ?   ?   ?   B . n 
A 1 665  GLY 665  665  ?   ?   ?   B . n 
A 1 666  ILE 666  666  ?   ?   ?   B . n 
A 1 667  CYS 667  667  ?   ?   ?   B . n 
A 1 668  ALA 668  668  ?   ?   ?   B . n 
A 1 669  SER 669  669  ?   ?   ?   B . n 
A 1 670  TYR 670  670  ?   ?   ?   B . n 
A 1 671  GLN 671  671  ?   ?   ?   B . n 
A 1 672  THR 672  672  ?   ?   ?   B . n 
A 1 673  GLN 673  673  ?   ?   ?   B . n 
A 1 674  THR 674  674  ?   ?   ?   B . n 
A 1 675  LYS 675  675  ?   ?   ?   B . n 
A 1 676  SER 676  676  ?   ?   ?   B . n 
A 1 677  ARG 677  677  ?   ?   ?   B . n 
A 1 678  ALA 678  678  ?   ?   ?   B . n 
A 1 679  GLY 679  679  ?   ?   ?   B . n 
A 1 680  ALA 680  680  ?   ?   ?   B . n 
A 1 681  ARG 681  681  ?   ?   ?   B . n 
A 1 682  SER 682  682  ?   ?   ?   B . n 
A 1 683  VAL 683  683  ?   ?   ?   B . n 
A 1 684  ALA 684  684  ?   ?   ?   B . n 
A 1 685  SER 685  685  ?   ?   ?   B . n 
A 1 686  GLN 686  686  ?   ?   ?   B . n 
A 1 687  SER 687  687  ?   ?   ?   B . n 
A 1 688  ILE 688  688  ?   ?   ?   B . n 
A 1 689  ILE 689  689  ?   ?   ?   B . n 
A 1 690  ALA 690  690  ?   ?   ?   B . n 
A 1 691  TYR 691  691  ?   ?   ?   B . n 
A 1 692  THR 692  692  ?   ?   ?   B . n 
A 1 693  MET 693  693  ?   ?   ?   B . n 
A 1 694  SER 694  694  ?   ?   ?   B . n 
A 1 695  LEU 695  695  ?   ?   ?   B . n 
A 1 696  GLY 696  696  ?   ?   ?   B . n 
A 1 697  ALA 697  697  ?   ?   ?   B . n 
A 1 698  GLU 698  698  ?   ?   ?   B . n 
A 1 699  ASN 699  699  ?   ?   ?   B . n 
A 1 700  SER 700  700  ?   ?   ?   B . n 
A 1 701  VAL 701  701  ?   ?   ?   B . n 
A 1 702  ALA 702  702  ?   ?   ?   B . n 
A 1 703  TYR 703  703  ?   ?   ?   B . n 
A 1 704  SER 704  704  ?   ?   ?   B . n 
A 1 705  ASN 705  705  ?   ?   ?   B . n 
A 1 706  ASN 706  706  ?   ?   ?   B . n 
A 1 707  SER 707  707  ?   ?   ?   B . n 
A 1 708  ILE 708  708  ?   ?   ?   B . n 
A 1 709  ALA 709  709  ?   ?   ?   B . n 
A 1 710  ILE 710  710  ?   ?   ?   B . n 
A 1 711  PRO 711  711  ?   ?   ?   B . n 
A 1 712  THR 712  712  ?   ?   ?   B . n 
A 1 713  ASN 713  713  ?   ?   ?   B . n 
A 1 714  PHE 714  714  ?   ?   ?   B . n 
A 1 715  THR 715  715  ?   ?   ?   B . n 
A 1 716  ILE 716  716  ?   ?   ?   B . n 
A 1 717  SER 717  717  ?   ?   ?   B . n 
A 1 718  VAL 718  718  ?   ?   ?   B . n 
A 1 719  THR 719  719  ?   ?   ?   B . n 
A 1 720  THR 720  720  ?   ?   ?   B . n 
A 1 721  GLU 721  721  ?   ?   ?   B . n 
A 1 722  ILE 722  722  ?   ?   ?   B . n 
A 1 723  LEU 723  723  ?   ?   ?   B . n 
A 1 724  PRO 724  724  ?   ?   ?   B . n 
A 1 725  VAL 725  725  ?   ?   ?   B . n 
A 1 726  SER 726  726  ?   ?   ?   B . n 
A 1 727  MET 727  727  ?   ?   ?   B . n 
A 1 728  THR 728  728  ?   ?   ?   B . n 
A 1 729  LYS 729  729  ?   ?   ?   B . n 
A 1 730  THR 730  730  ?   ?   ?   B . n 
A 1 731  SER 731  731  ?   ?   ?   B . n 
A 1 732  VAL 732  732  ?   ?   ?   B . n 
A 1 733  ASP 733  733  ?   ?   ?   B . n 
A 1 734  CYS 734  734  ?   ?   ?   B . n 
A 1 735  THR 735  735  ?   ?   ?   B . n 
A 1 736  MET 736  736  ?   ?   ?   B . n 
A 1 737  TYR 737  737  ?   ?   ?   B . n 
A 1 738  ILE 738  738  ?   ?   ?   B . n 
A 1 739  CYS 739  739  ?   ?   ?   B . n 
A 1 740  GLY 740  740  ?   ?   ?   B . n 
A 1 741  ASP 741  741  ?   ?   ?   B . n 
A 1 742  SER 742  742  ?   ?   ?   B . n 
A 1 743  THR 743  743  ?   ?   ?   B . n 
A 1 744  GLU 744  744  ?   ?   ?   B . n 
A 1 745  CYS 745  745  ?   ?   ?   B . n 
A 1 746  SER 746  746  ?   ?   ?   B . n 
A 1 747  ASN 747  747  ?   ?   ?   B . n 
A 1 748  LEU 748  748  ?   ?   ?   B . n 
A 1 749  LEU 749  749  ?   ?   ?   B . n 
A 1 750  LEU 750  750  ?   ?   ?   B . n 
A 1 751  GLN 751  751  ?   ?   ?   B . n 
A 1 752  TYR 752  752  ?   ?   ?   B . n 
A 1 753  GLY 753  753  ?   ?   ?   B . n 
A 1 754  SER 754  754  ?   ?   ?   B . n 
A 1 755  PHE 755  755  ?   ?   ?   B . n 
A 1 756  CYS 756  756  ?   ?   ?   B . n 
A 1 757  THR 757  757  ?   ?   ?   B . n 
A 1 758  GLN 758  758  ?   ?   ?   B . n 
A 1 759  LEU 759  759  ?   ?   ?   B . n 
A 1 760  LYS 760  760  ?   ?   ?   B . n 
A 1 761  ARG 761  761  ?   ?   ?   B . n 
A 1 762  ALA 762  762  ?   ?   ?   B . n 
A 1 763  LEU 763  763  ?   ?   ?   B . n 
A 1 764  THR 764  764  ?   ?   ?   B . n 
A 1 765  GLY 765  765  ?   ?   ?   B . n 
A 1 766  ILE 766  766  ?   ?   ?   B . n 
A 1 767  ALA 767  767  ?   ?   ?   B . n 
A 1 768  VAL 768  768  ?   ?   ?   B . n 
A 1 769  GLU 769  769  ?   ?   ?   B . n 
A 1 770  GLN 770  770  ?   ?   ?   B . n 
A 1 771  ASP 771  771  ?   ?   ?   B . n 
A 1 772  LYS 772  772  ?   ?   ?   B . n 
A 1 773  ASN 773  773  ?   ?   ?   B . n 
A 1 774  THR 774  774  ?   ?   ?   B . n 
A 1 775  GLN 775  775  ?   ?   ?   B . n 
A 1 776  GLU 776  776  ?   ?   ?   B . n 
A 1 777  VAL 777  777  ?   ?   ?   B . n 
A 1 778  PHE 778  778  ?   ?   ?   B . n 
A 1 779  ALA 779  779  ?   ?   ?   B . n 
A 1 780  GLN 780  780  ?   ?   ?   B . n 
A 1 781  VAL 781  781  ?   ?   ?   B . n 
A 1 782  LYS 782  782  ?   ?   ?   B . n 
A 1 783  GLN 783  783  ?   ?   ?   B . n 
A 1 784  ILE 784  784  ?   ?   ?   B . n 
A 1 785  TYR 785  785  ?   ?   ?   B . n 
A 1 786  LYS 786  786  ?   ?   ?   B . n 
A 1 787  THR 787  787  ?   ?   ?   B . n 
A 1 788  PRO 788  788  ?   ?   ?   B . n 
A 1 789  PRO 789  789  ?   ?   ?   B . n 
A 1 790  ILE 790  790  ?   ?   ?   B . n 
A 1 791  LYS 791  791  ?   ?   ?   B . n 
A 1 792  TYR 792  792  ?   ?   ?   B . n 
A 1 793  PHE 793  793  ?   ?   ?   B . n 
A 1 794  GLY 794  794  ?   ?   ?   B . n 
A 1 795  GLY 795  795  ?   ?   ?   B . n 
A 1 796  PHE 796  796  ?   ?   ?   B . n 
A 1 797  ASN 797  797  ?   ?   ?   B . n 
A 1 798  PHE 798  798  ?   ?   ?   B . n 
A 1 799  SER 799  799  ?   ?   ?   B . n 
A 1 800  GLN 800  800  ?   ?   ?   B . n 
A 1 801  ILE 801  801  ?   ?   ?   B . n 
A 1 802  LEU 802  802  ?   ?   ?   B . n 
A 1 803  PRO 803  803  ?   ?   ?   B . n 
A 1 804  ASP 804  804  ?   ?   ?   B . n 
A 1 805  PRO 805  805  ?   ?   ?   B . n 
A 1 806  SER 806  806  ?   ?   ?   B . n 
A 1 807  LYS 807  807  ?   ?   ?   B . n 
A 1 808  PRO 808  808  ?   ?   ?   B . n 
A 1 809  SER 809  809  ?   ?   ?   B . n 
A 1 810  LYS 810  810  ?   ?   ?   B . n 
A 1 811  ARG 811  811  ?   ?   ?   B . n 
A 1 812  SER 812  812  ?   ?   ?   B . n 
A 1 813  PRO 813  813  ?   ?   ?   B . n 
A 1 814  ILE 814  814  ?   ?   ?   B . n 
A 1 815  GLU 815  815  ?   ?   ?   B . n 
A 1 816  ASP 816  816  ?   ?   ?   B . n 
A 1 817  LEU 817  817  ?   ?   ?   B . n 
A 1 818  LEU 818  818  ?   ?   ?   B . n 
A 1 819  PHE 819  819  ?   ?   ?   B . n 
A 1 820  ASN 820  820  ?   ?   ?   B . n 
A 1 821  LYS 821  821  ?   ?   ?   B . n 
A 1 822  VAL 822  822  ?   ?   ?   B . n 
A 1 823  THR 823  823  ?   ?   ?   B . n 
A 1 824  LEU 824  824  ?   ?   ?   B . n 
A 1 825  ALA 825  825  ?   ?   ?   B . n 
A 1 826  ASP 826  826  ?   ?   ?   B . n 
A 1 827  ALA 827  827  ?   ?   ?   B . n 
A 1 828  GLY 828  828  ?   ?   ?   B . n 
A 1 829  PHE 829  829  ?   ?   ?   B . n 
A 1 830  ILE 830  830  ?   ?   ?   B . n 
A 1 831  LYS 831  831  ?   ?   ?   B . n 
A 1 832  GLN 832  832  ?   ?   ?   B . n 
A 1 833  TYR 833  833  ?   ?   ?   B . n 
A 1 834  GLY 834  834  ?   ?   ?   B . n 
A 1 835  ASP 835  835  ?   ?   ?   B . n 
A 1 836  CYS 836  836  ?   ?   ?   B . n 
A 1 837  LEU 837  837  ?   ?   ?   B . n 
A 1 838  GLY 838  838  ?   ?   ?   B . n 
A 1 839  ASP 839  839  ?   ?   ?   B . n 
A 1 840  ILE 840  840  ?   ?   ?   B . n 
A 1 841  ALA 841  841  ?   ?   ?   B . n 
A 1 842  ALA 842  842  ?   ?   ?   B . n 
A 1 843  ARG 843  843  ?   ?   ?   B . n 
A 1 844  ASP 844  844  ?   ?   ?   B . n 
A 1 845  LEU 845  845  ?   ?   ?   B . n 
A 1 846  ILE 846  846  ?   ?   ?   B . n 
A 1 847  CYS 847  847  ?   ?   ?   B . n 
A 1 848  ALA 848  848  ?   ?   ?   B . n 
A 1 849  GLN 849  849  ?   ?   ?   B . n 
A 1 850  LYS 850  850  ?   ?   ?   B . n 
A 1 851  PHE 851  851  ?   ?   ?   B . n 
A 1 852  ASN 852  852  ?   ?   ?   B . n 
A 1 853  GLY 853  853  ?   ?   ?   B . n 
A 1 854  LEU 854  854  ?   ?   ?   B . n 
A 1 855  THR 855  855  ?   ?   ?   B . n 
A 1 856  VAL 856  856  ?   ?   ?   B . n 
A 1 857  LEU 857  857  ?   ?   ?   B . n 
A 1 858  PRO 858  858  ?   ?   ?   B . n 
A 1 859  PRO 859  859  ?   ?   ?   B . n 
A 1 860  LEU 860  860  ?   ?   ?   B . n 
A 1 861  LEU 861  861  ?   ?   ?   B . n 
A 1 862  THR 862  862  ?   ?   ?   B . n 
A 1 863  ASP 863  863  ?   ?   ?   B . n 
A 1 864  GLU 864  864  ?   ?   ?   B . n 
A 1 865  MET 865  865  ?   ?   ?   B . n 
A 1 866  ILE 866  866  ?   ?   ?   B . n 
A 1 867  ALA 867  867  ?   ?   ?   B . n 
A 1 868  GLN 868  868  ?   ?   ?   B . n 
A 1 869  TYR 869  869  ?   ?   ?   B . n 
A 1 870  THR 870  870  ?   ?   ?   B . n 
A 1 871  SER 871  871  ?   ?   ?   B . n 
A 1 872  ALA 872  872  ?   ?   ?   B . n 
A 1 873  LEU 873  873  ?   ?   ?   B . n 
A 1 874  LEU 874  874  ?   ?   ?   B . n 
A 1 875  ALA 875  875  ?   ?   ?   B . n 
A 1 876  GLY 876  876  ?   ?   ?   B . n 
A 1 877  THR 877  877  ?   ?   ?   B . n 
A 1 878  ILE 878  878  ?   ?   ?   B . n 
A 1 879  THR 879  879  ?   ?   ?   B . n 
A 1 880  SER 880  880  ?   ?   ?   B . n 
A 1 881  GLY 881  881  ?   ?   ?   B . n 
A 1 882  TRP 882  882  ?   ?   ?   B . n 
A 1 883  THR 883  883  ?   ?   ?   B . n 
A 1 884  PHE 884  884  ?   ?   ?   B . n 
A 1 885  GLY 885  885  ?   ?   ?   B . n 
A 1 886  ALA 886  886  ?   ?   ?   B . n 
A 1 887  GLY 887  887  ?   ?   ?   B . n 
A 1 888  PRO 888  888  ?   ?   ?   B . n 
A 1 889  ALA 889  889  ?   ?   ?   B . n 
A 1 890  LEU 890  890  ?   ?   ?   B . n 
A 1 891  GLN 891  891  ?   ?   ?   B . n 
A 1 892  ILE 892  892  ?   ?   ?   B . n 
A 1 893  PRO 893  893  ?   ?   ?   B . n 
A 1 894  PHE 894  894  ?   ?   ?   B . n 
A 1 895  PRO 895  895  ?   ?   ?   B . n 
A 1 896  MET 896  896  ?   ?   ?   B . n 
A 1 897  GLN 897  897  ?   ?   ?   B . n 
A 1 898  MET 898  898  ?   ?   ?   B . n 
A 1 899  ALA 899  899  ?   ?   ?   B . n 
A 1 900  TYR 900  900  ?   ?   ?   B . n 
A 1 901  ARG 901  901  ?   ?   ?   B . n 
A 1 902  PHE 902  902  ?   ?   ?   B . n 
A 1 903  ASN 903  903  ?   ?   ?   B . n 
A 1 904  GLY 904  904  ?   ?   ?   B . n 
A 1 905  ILE 905  905  ?   ?   ?   B . n 
A 1 906  GLY 906  906  ?   ?   ?   B . n 
A 1 907  VAL 907  907  ?   ?   ?   B . n 
A 1 908  THR 908  908  ?   ?   ?   B . n 
A 1 909  GLN 909  909  ?   ?   ?   B . n 
A 1 910  ASN 910  910  ?   ?   ?   B . n 
A 1 911  VAL 911  911  ?   ?   ?   B . n 
A 1 912  LEU 912  912  ?   ?   ?   B . n 
A 1 913  TYR 913  913  ?   ?   ?   B . n 
A 1 914  GLU 914  914  ?   ?   ?   B . n 
A 1 915  ASN 915  915  ?   ?   ?   B . n 
A 1 916  GLN 916  916  ?   ?   ?   B . n 
A 1 917  LYS 917  917  ?   ?   ?   B . n 
A 1 918  LEU 918  918  ?   ?   ?   B . n 
A 1 919  ILE 919  919  ?   ?   ?   B . n 
A 1 920  ALA 920  920  ?   ?   ?   B . n 
A 1 921  ASN 921  921  ?   ?   ?   B . n 
A 1 922  GLN 922  922  ?   ?   ?   B . n 
A 1 923  PHE 923  923  ?   ?   ?   B . n 
A 1 924  ASN 924  924  ?   ?   ?   B . n 
A 1 925  SER 925  925  ?   ?   ?   B . n 
A 1 926  ALA 926  926  ?   ?   ?   B . n 
A 1 927  ILE 927  927  ?   ?   ?   B . n 
A 1 928  GLY 928  928  ?   ?   ?   B . n 
A 1 929  LYS 929  929  ?   ?   ?   B . n 
A 1 930  ILE 930  930  ?   ?   ?   B . n 
A 1 931  GLN 931  931  ?   ?   ?   B . n 
A 1 932  ASP 932  932  ?   ?   ?   B . n 
A 1 933  SER 933  933  ?   ?   ?   B . n 
A 1 934  LEU 934  934  ?   ?   ?   B . n 
A 1 935  PHE 935  935  ?   ?   ?   B . n 
A 1 936  SER 936  936  ?   ?   ?   B . n 
A 1 937  THR 937  937  ?   ?   ?   B . n 
A 1 938  PRO 938  938  ?   ?   ?   B . n 
A 1 939  SER 939  939  ?   ?   ?   B . n 
A 1 940  ALA 940  940  ?   ?   ?   B . n 
A 1 941  LEU 941  941  ?   ?   ?   B . n 
A 1 942  GLY 942  942  ?   ?   ?   B . n 
A 1 943  LYS 943  943  ?   ?   ?   B . n 
A 1 944  LEU 944  944  ?   ?   ?   B . n 
A 1 945  GLN 945  945  ?   ?   ?   B . n 
A 1 946  ASP 946  946  ?   ?   ?   B . n 
A 1 947  VAL 947  947  ?   ?   ?   B . n 
A 1 948  VAL 948  948  ?   ?   ?   B . n 
A 1 949  ASN 949  949  ?   ?   ?   B . n 
A 1 950  HIS 950  950  ?   ?   ?   B . n 
A 1 951  ASN 951  951  ?   ?   ?   B . n 
A 1 952  ALA 952  952  ?   ?   ?   B . n 
A 1 953  GLN 953  953  ?   ?   ?   B . n 
A 1 954  ALA 954  954  ?   ?   ?   B . n 
A 1 955  LEU 955  955  ?   ?   ?   B . n 
A 1 956  ASN 956  956  ?   ?   ?   B . n 
A 1 957  THR 957  957  ?   ?   ?   B . n 
A 1 958  LEU 958  958  ?   ?   ?   B . n 
A 1 959  VAL 959  959  ?   ?   ?   B . n 
A 1 960  LYS 960  960  ?   ?   ?   B . n 
A 1 961  GLN 961  961  ?   ?   ?   B . n 
A 1 962  LEU 962  962  ?   ?   ?   B . n 
A 1 963  SER 963  963  ?   ?   ?   B . n 
A 1 964  SER 964  964  ?   ?   ?   B . n 
A 1 965  LYS 965  965  ?   ?   ?   B . n 
A 1 966  PHE 966  966  ?   ?   ?   B . n 
A 1 967  GLY 967  967  ?   ?   ?   B . n 
A 1 968  ALA 968  968  ?   ?   ?   B . n 
A 1 969  ILE 969  969  ?   ?   ?   B . n 
A 1 970  SER 970  970  ?   ?   ?   B . n 
A 1 971  SER 971  971  ?   ?   ?   B . n 
A 1 972  VAL 972  972  ?   ?   ?   B . n 
A 1 973  LEU 973  973  ?   ?   ?   B . n 
A 1 974  ASN 974  974  ?   ?   ?   B . n 
A 1 975  ASP 975  975  ?   ?   ?   B . n 
A 1 976  ILE 976  976  ?   ?   ?   B . n 
A 1 977  LEU 977  977  ?   ?   ?   B . n 
A 1 978  SER 978  978  ?   ?   ?   B . n 
A 1 979  ARG 979  979  ?   ?   ?   B . n 
A 1 980  LEU 980  980  ?   ?   ?   B . n 
A 1 981  ASP 981  981  ?   ?   ?   B . n 
A 1 982  PRO 982  982  ?   ?   ?   B . n 
A 1 983  PRO 983  983  ?   ?   ?   B . n 
A 1 984  GLU 984  984  ?   ?   ?   B . n 
A 1 985  ALA 985  985  ?   ?   ?   B . n 
A 1 986  GLU 986  986  ?   ?   ?   B . n 
A 1 987  VAL 987  987  ?   ?   ?   B . n 
A 1 988  GLN 988  988  ?   ?   ?   B . n 
A 1 989  ILE 989  989  ?   ?   ?   B . n 
A 1 990  ASP 990  990  ?   ?   ?   B . n 
A 1 991  ARG 991  991  ?   ?   ?   B . n 
A 1 992  LEU 992  992  ?   ?   ?   B . n 
A 1 993  ILE 993  993  ?   ?   ?   B . n 
A 1 994  THR 994  994  ?   ?   ?   B . n 
A 1 995  GLY 995  995  ?   ?   ?   B . n 
A 1 996  ARG 996  996  ?   ?   ?   B . n 
A 1 997  LEU 997  997  ?   ?   ?   B . n 
A 1 998  GLN 998  998  ?   ?   ?   B . n 
A 1 999  SER 999  999  ?   ?   ?   B . n 
A 1 1000 LEU 1000 1000 ?   ?   ?   B . n 
A 1 1001 GLN 1001 1001 ?   ?   ?   B . n 
A 1 1002 THR 1002 1002 ?   ?   ?   B . n 
A 1 1003 TYR 1003 1003 ?   ?   ?   B . n 
A 1 1004 VAL 1004 1004 ?   ?   ?   B . n 
A 1 1005 THR 1005 1005 ?   ?   ?   B . n 
A 1 1006 GLN 1006 1006 ?   ?   ?   B . n 
A 1 1007 GLN 1007 1007 ?   ?   ?   B . n 
A 1 1008 LEU 1008 1008 ?   ?   ?   B . n 
A 1 1009 ILE 1009 1009 ?   ?   ?   B . n 
A 1 1010 ARG 1010 1010 ?   ?   ?   B . n 
A 1 1011 ALA 1011 1011 ?   ?   ?   B . n 
A 1 1012 ALA 1012 1012 ?   ?   ?   B . n 
A 1 1013 GLU 1013 1013 ?   ?   ?   B . n 
A 1 1014 ILE 1014 1014 ?   ?   ?   B . n 
A 1 1015 ARG 1015 1015 ?   ?   ?   B . n 
A 1 1016 ALA 1016 1016 ?   ?   ?   B . n 
A 1 1017 SER 1017 1017 ?   ?   ?   B . n 
A 1 1018 ALA 1018 1018 ?   ?   ?   B . n 
A 1 1019 ASN 1019 1019 ?   ?   ?   B . n 
A 1 1020 LEU 1020 1020 ?   ?   ?   B . n 
A 1 1021 ALA 1021 1021 ?   ?   ?   B . n 
A 1 1022 ALA 1022 1022 ?   ?   ?   B . n 
A 1 1023 THR 1023 1023 ?   ?   ?   B . n 
A 1 1024 LYS 1024 1024 ?   ?   ?   B . n 
A 1 1025 MET 1025 1025 ?   ?   ?   B . n 
A 1 1026 SER 1026 1026 ?   ?   ?   B . n 
A 1 1027 GLU 1027 1027 ?   ?   ?   B . n 
A 1 1028 CYS 1028 1028 ?   ?   ?   B . n 
A 1 1029 VAL 1029 1029 ?   ?   ?   B . n 
A 1 1030 LEU 1030 1030 ?   ?   ?   B . n 
A 1 1031 GLY 1031 1031 ?   ?   ?   B . n 
A 1 1032 GLN 1032 1032 ?   ?   ?   B . n 
A 1 1033 SER 1033 1033 ?   ?   ?   B . n 
A 1 1034 LYS 1034 1034 ?   ?   ?   B . n 
A 1 1035 ARG 1035 1035 ?   ?   ?   B . n 
A 1 1036 VAL 1036 1036 ?   ?   ?   B . n 
A 1 1037 ASP 1037 1037 ?   ?   ?   B . n 
A 1 1038 PHE 1038 1038 ?   ?   ?   B . n 
A 1 1039 CYS 1039 1039 ?   ?   ?   B . n 
A 1 1040 GLY 1040 1040 ?   ?   ?   B . n 
A 1 1041 LYS 1041 1041 ?   ?   ?   B . n 
A 1 1042 GLY 1042 1042 ?   ?   ?   B . n 
A 1 1043 TYR 1043 1043 ?   ?   ?   B . n 
A 1 1044 HIS 1044 1044 ?   ?   ?   B . n 
A 1 1045 LEU 1045 1045 ?   ?   ?   B . n 
A 1 1046 MET 1046 1046 ?   ?   ?   B . n 
A 1 1047 SER 1047 1047 ?   ?   ?   B . n 
A 1 1048 PHE 1048 1048 ?   ?   ?   B . n 
A 1 1049 PRO 1049 1049 ?   ?   ?   B . n 
A 1 1050 GLN 1050 1050 ?   ?   ?   B . n 
A 1 1051 SER 1051 1051 ?   ?   ?   B . n 
A 1 1052 ALA 1052 1052 ?   ?   ?   B . n 
A 1 1053 PRO 1053 1053 ?   ?   ?   B . n 
A 1 1054 HIS 1054 1054 ?   ?   ?   B . n 
A 1 1055 GLY 1055 1055 ?   ?   ?   B . n 
A 1 1056 VAL 1056 1056 ?   ?   ?   B . n 
A 1 1057 VAL 1057 1057 ?   ?   ?   B . n 
A 1 1058 PHE 1058 1058 ?   ?   ?   B . n 
A 1 1059 LEU 1059 1059 ?   ?   ?   B . n 
A 1 1060 HIS 1060 1060 ?   ?   ?   B . n 
A 1 1061 VAL 1061 1061 ?   ?   ?   B . n 
A 1 1062 THR 1062 1062 ?   ?   ?   B . n 
A 1 1063 TYR 1063 1063 ?   ?   ?   B . n 
A 1 1064 VAL 1064 1064 ?   ?   ?   B . n 
A 1 1065 PRO 1065 1065 ?   ?   ?   B . n 
A 1 1066 ALA 1066 1066 ?   ?   ?   B . n 
A 1 1067 GLN 1067 1067 ?   ?   ?   B . n 
A 1 1068 GLU 1068 1068 ?   ?   ?   B . n 
A 1 1069 LYS 1069 1069 ?   ?   ?   B . n 
A 1 1070 ASN 1070 1070 ?   ?   ?   B . n 
A 1 1071 PHE 1071 1071 ?   ?   ?   B . n 
A 1 1072 THR 1072 1072 ?   ?   ?   B . n 
A 1 1073 THR 1073 1073 ?   ?   ?   B . n 
A 1 1074 ALA 1074 1074 ?   ?   ?   B . n 
A 1 1075 PRO 1075 1075 ?   ?   ?   B . n 
A 1 1076 ALA 1076 1076 ?   ?   ?   B . n 
A 1 1077 ILE 1077 1077 ?   ?   ?   B . n 
A 1 1078 CYS 1078 1078 ?   ?   ?   B . n 
A 1 1079 HIS 1079 1079 ?   ?   ?   B . n 
A 1 1080 ASP 1080 1080 ?   ?   ?   B . n 
A 1 1081 GLY 1081 1081 ?   ?   ?   B . n 
A 1 1082 LYS 1082 1082 ?   ?   ?   B . n 
A 1 1083 ALA 1083 1083 ?   ?   ?   B . n 
A 1 1084 HIS 1084 1084 ?   ?   ?   B . n 
A 1 1085 PHE 1085 1085 ?   ?   ?   B . n 
A 1 1086 PRO 1086 1086 ?   ?   ?   B . n 
A 1 1087 ARG 1087 1087 ?   ?   ?   B . n 
A 1 1088 GLU 1088 1088 ?   ?   ?   B . n 
A 1 1089 GLY 1089 1089 ?   ?   ?   B . n 
A 1 1090 VAL 1090 1090 ?   ?   ?   B . n 
A 1 1091 PHE 1091 1091 ?   ?   ?   B . n 
A 1 1092 VAL 1092 1092 ?   ?   ?   B . n 
A 1 1093 SER 1093 1093 ?   ?   ?   B . n 
A 1 1094 ASN 1094 1094 ?   ?   ?   B . n 
A 1 1095 GLY 1095 1095 ?   ?   ?   B . n 
A 1 1096 THR 1096 1096 ?   ?   ?   B . n 
A 1 1097 HIS 1097 1097 ?   ?   ?   B . n 
A 1 1098 TRP 1098 1098 ?   ?   ?   B . n 
A 1 1099 PHE 1099 1099 ?   ?   ?   B . n 
A 1 1100 VAL 1100 1100 ?   ?   ?   B . n 
A 1 1101 THR 1101 1101 ?   ?   ?   B . n 
A 1 1102 GLN 1102 1102 ?   ?   ?   B . n 
A 1 1103 ARG 1103 1103 ?   ?   ?   B . n 
A 1 1104 ASN 1104 1104 ?   ?   ?   B . n 
A 1 1105 PHE 1105 1105 ?   ?   ?   B . n 
A 1 1106 TYR 1106 1106 ?   ?   ?   B . n 
A 1 1107 GLU 1107 1107 ?   ?   ?   B . n 
A 1 1108 PRO 1108 1108 ?   ?   ?   B . n 
A 1 1109 GLN 1109 1109 ?   ?   ?   B . n 
A 1 1110 ILE 1110 1110 ?   ?   ?   B . n 
A 1 1111 ILE 1111 1111 ?   ?   ?   B . n 
A 1 1112 THR 1112 1112 ?   ?   ?   B . n 
A 1 1113 THR 1113 1113 ?   ?   ?   B . n 
A 1 1114 ASP 1114 1114 ?   ?   ?   B . n 
A 1 1115 ASN 1115 1115 ?   ?   ?   B . n 
A 1 1116 THR 1116 1116 ?   ?   ?   B . n 
A 1 1117 PHE 1117 1117 ?   ?   ?   B . n 
A 1 1118 VAL 1118 1118 ?   ?   ?   B . n 
A 1 1119 SER 1119 1119 ?   ?   ?   B . n 
A 1 1120 GLY 1120 1120 ?   ?   ?   B . n 
A 1 1121 ASN 1121 1121 ?   ?   ?   B . n 
A 1 1122 CYS 1122 1122 ?   ?   ?   B . n 
A 1 1123 ASP 1123 1123 ?   ?   ?   B . n 
A 1 1124 VAL 1124 1124 ?   ?   ?   B . n 
A 1 1125 VAL 1125 1125 ?   ?   ?   B . n 
A 1 1126 ILE 1126 1126 ?   ?   ?   B . n 
A 1 1127 GLY 1127 1127 ?   ?   ?   B . n 
A 1 1128 ILE 1128 1128 ?   ?   ?   B . n 
A 1 1129 VAL 1129 1129 ?   ?   ?   B . n 
A 1 1130 ASN 1130 1130 ?   ?   ?   B . n 
A 1 1131 ASN 1131 1131 ?   ?   ?   B . n 
A 1 1132 THR 1132 1132 ?   ?   ?   B . n 
A 1 1133 VAL 1133 1133 ?   ?   ?   B . n 
A 1 1134 TYR 1134 1134 ?   ?   ?   B . n 
A 1 1135 ASP 1135 1135 ?   ?   ?   B . n 
A 1 1136 PRO 1136 1136 ?   ?   ?   B . n 
A 1 1137 LEU 1137 1137 ?   ?   ?   B . n 
A 1 1138 GLN 1138 1138 ?   ?   ?   B . n 
A 1 1139 LEU 1139 1139 ?   ?   ?   B . n 
A 1 1140 GLU 1140 1140 ?   ?   ?   B . n 
A 1 1141 LEU 1141 1141 ?   ?   ?   B . n 
A 1 1142 ASP 1142 1142 ?   ?   ?   B . n 
A 1 1143 SER 1143 1143 ?   ?   ?   B . n 
A 1 1144 PHE 1144 1144 ?   ?   ?   B . n 
A 1 1145 LYS 1145 1145 ?   ?   ?   B . n 
A 1 1146 GLU 1146 1146 ?   ?   ?   B . n 
A 1 1147 GLU 1147 1147 ?   ?   ?   B . n 
A 1 1148 LEU 1148 1148 ?   ?   ?   B . n 
A 1 1149 ASP 1149 1149 ?   ?   ?   B . n 
A 1 1150 LYS 1150 1150 ?   ?   ?   B . n 
A 1 1151 TYR 1151 1151 ?   ?   ?   B . n 
A 1 1152 PHE 1152 1152 ?   ?   ?   B . n 
A 1 1153 LYS 1153 1153 ?   ?   ?   B . n 
A 1 1154 ASN 1154 1154 ?   ?   ?   B . n 
A 1 1155 HIS 1155 1155 ?   ?   ?   B . n 
A 1 1156 THR 1156 1156 ?   ?   ?   B . n 
A 1 1157 SER 1157 1157 ?   ?   ?   B . n 
A 1 1158 PRO 1158 1158 ?   ?   ?   B . n 
A 1 1159 ASP 1159 1159 ?   ?   ?   B . n 
A 1 1160 VAL 1160 1160 ?   ?   ?   B . n 
A 1 1161 ASP 1161 1161 ?   ?   ?   B . n 
A 1 1162 LEU 1162 1162 ?   ?   ?   B . n 
A 1 1163 GLY 1163 1163 ?   ?   ?   B . n 
A 1 1164 ASP 1164 1164 ?   ?   ?   B . n 
A 1 1165 ILE 1165 1165 ?   ?   ?   B . n 
A 1 1166 SER 1166 1166 ?   ?   ?   B . n 
A 1 1167 GLY 1167 1167 ?   ?   ?   B . n 
A 1 1168 ILE 1168 1168 ?   ?   ?   B . n 
A 1 1169 ASN 1169 1169 ?   ?   ?   B . n 
A 1 1170 ALA 1170 1170 ?   ?   ?   B . n 
A 1 1171 SER 1171 1171 ?   ?   ?   B . n 
A 1 1172 VAL 1172 1172 ?   ?   ?   B . n 
A 1 1173 VAL 1173 1173 ?   ?   ?   B . n 
A 1 1174 ASN 1174 1174 ?   ?   ?   B . n 
A 1 1175 ILE 1175 1175 ?   ?   ?   B . n 
A 1 1176 GLN 1176 1176 ?   ?   ?   B . n 
A 1 1177 LYS 1177 1177 ?   ?   ?   B . n 
A 1 1178 GLU 1178 1178 ?   ?   ?   B . n 
A 1 1179 ILE 1179 1179 ?   ?   ?   B . n 
A 1 1180 ASP 1180 1180 ?   ?   ?   B . n 
A 1 1181 ARG 1181 1181 ?   ?   ?   B . n 
A 1 1182 LEU 1182 1182 ?   ?   ?   B . n 
A 1 1183 ASN 1183 1183 ?   ?   ?   B . n 
A 1 1184 GLU 1184 1184 ?   ?   ?   B . n 
A 1 1185 VAL 1185 1185 ?   ?   ?   B . n 
A 1 1186 ALA 1186 1186 ?   ?   ?   B . n 
A 1 1187 LYS 1187 1187 ?   ?   ?   B . n 
A 1 1188 ASN 1188 1188 ?   ?   ?   B . n 
A 1 1189 LEU 1189 1189 ?   ?   ?   B . n 
A 1 1190 ASN 1190 1190 ?   ?   ?   B . n 
A 1 1191 GLU 1191 1191 ?   ?   ?   B . n 
A 1 1192 SER 1192 1192 ?   ?   ?   B . n 
A 1 1193 LEU 1193 1193 ?   ?   ?   B . n 
A 1 1194 ILE 1194 1194 ?   ?   ?   B . n 
A 1 1195 ASP 1195 1195 ?   ?   ?   B . n 
A 1 1196 LEU 1196 1196 ?   ?   ?   B . n 
A 1 1197 GLN 1197 1197 ?   ?   ?   B . n 
A 1 1198 GLU 1198 1198 ?   ?   ?   B . n 
A 1 1199 LEU 1199 1199 ?   ?   ?   B . n 
A 1 1200 GLY 1200 1200 ?   ?   ?   B . n 
A 1 1201 LYS 1201 1201 ?   ?   ?   B . n 
A 1 1202 TYR 1202 1202 ?   ?   ?   B . n 
A 1 1203 GLU 1203 1203 ?   ?   ?   B . n 
A 1 1204 GLN 1204 1204 ?   ?   ?   B . n 
A 1 1205 TYR 1205 1205 ?   ?   ?   B . n 
A 1 1206 ILE 1206 1206 ?   ?   ?   B . n 
A 1 1207 LYS 1207 1207 ?   ?   ?   B . n 
A 1 1208 GLY 1208 1208 ?   ?   ?   B . n 
A 1 1209 SER 1209 1209 ?   ?   ?   B . n 
A 1 1210 GLY 1210 1210 ?   ?   ?   B . n 
A 1 1211 TYR 1211 1211 ?   ?   ?   B . n 
A 1 1212 ILE 1212 1212 ?   ?   ?   B . n 
A 1 1213 PRO 1213 1213 ?   ?   ?   B . n 
A 1 1214 GLU 1214 1214 ?   ?   ?   B . n 
A 1 1215 ALA 1215 1215 ?   ?   ?   B . n 
A 1 1216 PRO 1216 1216 ?   ?   ?   B . n 
A 1 1217 ARG 1217 1217 ?   ?   ?   B . n 
A 1 1218 ASP 1218 1218 ?   ?   ?   B . n 
A 1 1219 GLY 1219 1219 ?   ?   ?   B . n 
A 1 1220 GLN 1220 1220 ?   ?   ?   B . n 
A 1 1221 ALA 1221 1221 ?   ?   ?   B . n 
A 1 1222 TYR 1222 1222 ?   ?   ?   B . n 
A 1 1223 VAL 1223 1223 ?   ?   ?   B . n 
A 1 1224 ARG 1224 1224 ?   ?   ?   B . n 
A 1 1225 LYS 1225 1225 ?   ?   ?   B . n 
A 1 1226 ASP 1226 1226 ?   ?   ?   B . n 
A 1 1227 GLY 1227 1227 ?   ?   ?   B . n 
A 1 1228 GLU 1228 1228 ?   ?   ?   B . n 
A 1 1229 TRP 1229 1229 ?   ?   ?   B . n 
A 1 1230 VAL 1230 1230 ?   ?   ?   B . n 
A 1 1231 LEU 1231 1231 ?   ?   ?   B . n 
A 1 1232 LEU 1232 1232 ?   ?   ?   B . n 
A 1 1233 SER 1233 1233 ?   ?   ?   B . n 
A 1 1234 THR 1234 1234 ?   ?   ?   B . n 
A 1 1235 PHE 1235 1235 ?   ?   ?   B . n 
A 1 1236 LEU 1236 1236 ?   ?   ?   B . n 
A 1 1237 GLY 1237 1237 ?   ?   ?   B . n 
A 1 1238 HIS 1238 1238 ?   ?   ?   B . n 
A 1 1239 HIS 1239 1239 ?   ?   ?   B . n 
A 1 1240 HIS 1240 1240 ?   ?   ?   B . n 
A 1 1241 HIS 1241 1241 ?   ?   ?   B . n 
A 1 1242 HIS 1242 1242 ?   ?   ?   B . n 
A 1 1243 HIS 1243 1243 ?   ?   ?   B . n 
B 1 1    MET 1    1    ?   ?   ?   A . n 
B 1 2    PHE 2    2    ?   ?   ?   A . n 
B 1 3    VAL 3    3    ?   ?   ?   A . n 
B 1 4    PHE 4    4    ?   ?   ?   A . n 
B 1 5    LEU 5    5    ?   ?   ?   A . n 
B 1 6    VAL 6    6    ?   ?   ?   A . n 
B 1 7    LEU 7    7    ?   ?   ?   A . n 
B 1 8    LEU 8    8    ?   ?   ?   A . n 
B 1 9    PRO 9    9    ?   ?   ?   A . n 
B 1 10   LEU 10   10   ?   ?   ?   A . n 
B 1 11   VAL 11   11   ?   ?   ?   A . n 
B 1 12   SER 12   12   ?   ?   ?   A . n 
B 1 13   SER 13   13   ?   ?   ?   A . n 
B 1 14   GLN 14   14   ?   ?   ?   A . n 
B 1 15   CYS 15   15   ?   ?   ?   A . n 
B 1 16   VAL 16   16   ?   ?   ?   A . n 
B 1 17   MET 17   17   ?   ?   ?   A . n 
B 1 18   PRO 18   18   ?   ?   ?   A . n 
B 1 19   LEU 19   19   ?   ?   ?   A . n 
B 1 20   PHE 20   20   ?   ?   ?   A . n 
B 1 21   ASN 21   21   ?   ?   ?   A . n 
B 1 22   LEU 22   22   ?   ?   ?   A . n 
B 1 23   ILE 23   23   ?   ?   ?   A . n 
B 1 24   THR 24   24   ?   ?   ?   A . n 
B 1 25   THR 25   25   ?   ?   ?   A . n 
B 1 26   THR 26   26   ?   ?   ?   A . n 
B 1 27   GLN 27   27   ?   ?   ?   A . n 
B 1 28   SER 28   28   ?   ?   ?   A . n 
B 1 29   TYR 29   29   ?   ?   ?   A . n 
B 1 30   THR 30   30   ?   ?   ?   A . n 
B 1 31   ASN 31   31   ?   ?   ?   A . n 
B 1 32   SER 32   32   ?   ?   ?   A . n 
B 1 33   PHE 33   33   ?   ?   ?   A . n 
B 1 34   THR 34   34   ?   ?   ?   A . n 
B 1 35   ARG 35   35   ?   ?   ?   A . n 
B 1 36   GLY 36   36   ?   ?   ?   A . n 
B 1 37   VAL 37   37   ?   ?   ?   A . n 
B 1 38   TYR 38   38   ?   ?   ?   A . n 
B 1 39   TYR 39   39   ?   ?   ?   A . n 
B 1 40   PRO 40   40   ?   ?   ?   A . n 
B 1 41   ASP 41   41   ?   ?   ?   A . n 
B 1 42   LYS 42   42   ?   ?   ?   A . n 
B 1 43   VAL 43   43   ?   ?   ?   A . n 
B 1 44   PHE 44   44   ?   ?   ?   A . n 
B 1 45   ARG 45   45   ?   ?   ?   A . n 
B 1 46   SER 46   46   ?   ?   ?   A . n 
B 1 47   SER 47   47   ?   ?   ?   A . n 
B 1 48   VAL 48   48   ?   ?   ?   A . n 
B 1 49   LEU 49   49   ?   ?   ?   A . n 
B 1 50   HIS 50   50   ?   ?   ?   A . n 
B 1 51   LEU 51   51   ?   ?   ?   A . n 
B 1 52   THR 52   52   ?   ?   ?   A . n 
B 1 53   GLN 53   53   ?   ?   ?   A . n 
B 1 54   ASP 54   54   ?   ?   ?   A . n 
B 1 55   LEU 55   55   ?   ?   ?   A . n 
B 1 56   PHE 56   56   ?   ?   ?   A . n 
B 1 57   LEU 57   57   ?   ?   ?   A . n 
B 1 58   PRO 58   58   ?   ?   ?   A . n 
B 1 59   PHE 59   59   ?   ?   ?   A . n 
B 1 60   PHE 60   60   ?   ?   ?   A . n 
B 1 61   SER 61   61   ?   ?   ?   A . n 
B 1 62   ASN 62   62   ?   ?   ?   A . n 
B 1 63   VAL 63   63   ?   ?   ?   A . n 
B 1 64   THR 64   64   ?   ?   ?   A . n 
B 1 65   TRP 65   65   ?   ?   ?   A . n 
B 1 66   PHE 66   66   ?   ?   ?   A . n 
B 1 67   HIS 67   67   ?   ?   ?   A . n 
B 1 68   ALA 68   68   ?   ?   ?   A . n 
B 1 69   ILE 69   69   ?   ?   ?   A . n 
B 1 70   SER 70   70   ?   ?   ?   A . n 
B 1 71   GLY 71   71   ?   ?   ?   A . n 
B 1 72   THR 72   72   ?   ?   ?   A . n 
B 1 73   ASN 73   73   ?   ?   ?   A . n 
B 1 74   GLY 74   74   ?   ?   ?   A . n 
B 1 75   THR 75   75   ?   ?   ?   A . n 
B 1 76   LYS 76   76   ?   ?   ?   A . n 
B 1 77   ARG 77   77   ?   ?   ?   A . n 
B 1 78   PHE 78   78   ?   ?   ?   A . n 
B 1 79   ASP 79   79   ?   ?   ?   A . n 
B 1 80   ASN 80   80   ?   ?   ?   A . n 
B 1 81   PRO 81   81   ?   ?   ?   A . n 
B 1 82   VAL 82   82   ?   ?   ?   A . n 
B 1 83   LEU 83   83   ?   ?   ?   A . n 
B 1 84   PRO 84   84   ?   ?   ?   A . n 
B 1 85   PHE 85   85   ?   ?   ?   A . n 
B 1 86   ASN 86   86   ?   ?   ?   A . n 
B 1 87   ASP 87   87   ?   ?   ?   A . n 
B 1 88   GLY 88   88   ?   ?   ?   A . n 
B 1 89   VAL 89   89   ?   ?   ?   A . n 
B 1 90   TYR 90   90   ?   ?   ?   A . n 
B 1 91   PHE 91   91   ?   ?   ?   A . n 
B 1 92   ALA 92   92   ?   ?   ?   A . n 
B 1 93   SER 93   93   ?   ?   ?   A . n 
B 1 94   THR 94   94   ?   ?   ?   A . n 
B 1 95   GLU 95   95   ?   ?   ?   A . n 
B 1 96   LYS 96   96   ?   ?   ?   A . n 
B 1 97   SER 97   97   ?   ?   ?   A . n 
B 1 98   ASN 98   98   ?   ?   ?   A . n 
B 1 99   ILE 99   99   ?   ?   ?   A . n 
B 1 100  ILE 100  100  ?   ?   ?   A . n 
B 1 101  ARG 101  101  ?   ?   ?   A . n 
B 1 102  GLY 102  102  ?   ?   ?   A . n 
B 1 103  TRP 103  103  ?   ?   ?   A . n 
B 1 104  ILE 104  104  ?   ?   ?   A . n 
B 1 105  PHE 105  105  ?   ?   ?   A . n 
B 1 106  GLY 106  106  ?   ?   ?   A . n 
B 1 107  THR 107  107  ?   ?   ?   A . n 
B 1 108  THR 108  108  ?   ?   ?   A . n 
B 1 109  LEU 109  109  ?   ?   ?   A . n 
B 1 110  ASP 110  110  ?   ?   ?   A . n 
B 1 111  SER 111  111  ?   ?   ?   A . n 
B 1 112  LYS 112  112  ?   ?   ?   A . n 
B 1 113  THR 113  113  ?   ?   ?   A . n 
B 1 114  GLN 114  114  ?   ?   ?   A . n 
B 1 115  SER 115  115  ?   ?   ?   A . n 
B 1 116  LEU 116  116  ?   ?   ?   A . n 
B 1 117  LEU 117  117  ?   ?   ?   A . n 
B 1 118  ILE 118  118  ?   ?   ?   A . n 
B 1 119  VAL 119  119  ?   ?   ?   A . n 
B 1 120  ASN 120  120  ?   ?   ?   A . n 
B 1 121  ASN 121  121  ?   ?   ?   A . n 
B 1 122  ALA 122  122  ?   ?   ?   A . n 
B 1 123  THR 123  123  ?   ?   ?   A . n 
B 1 124  ASN 124  124  ?   ?   ?   A . n 
B 1 125  VAL 125  125  ?   ?   ?   A . n 
B 1 126  PHE 126  126  ?   ?   ?   A . n 
B 1 127  ILE 127  127  ?   ?   ?   A . n 
B 1 128  LYS 128  128  ?   ?   ?   A . n 
B 1 129  VAL 129  129  ?   ?   ?   A . n 
B 1 130  CYS 130  130  ?   ?   ?   A . n 
B 1 131  GLU 131  131  ?   ?   ?   A . n 
B 1 132  PHE 132  132  ?   ?   ?   A . n 
B 1 133  GLN 133  133  ?   ?   ?   A . n 
B 1 134  PHE 134  134  ?   ?   ?   A . n 
B 1 135  CYS 135  135  ?   ?   ?   A . n 
B 1 136  ASN 136  136  ?   ?   ?   A . n 
B 1 137  ASP 137  137  ?   ?   ?   A . n 
B 1 138  PRO 138  138  ?   ?   ?   A . n 
B 1 139  PHE 139  139  ?   ?   ?   A . n 
B 1 140  LEU 140  140  ?   ?   ?   A . n 
B 1 141  ASP 141  141  ?   ?   ?   A . n 
B 1 142  VAL 142  142  ?   ?   ?   A . n 
B 1 143  TYR 143  143  ?   ?   ?   A . n 
B 1 144  HIS 144  144  ?   ?   ?   A . n 
B 1 145  LYS 145  145  ?   ?   ?   A . n 
B 1 146  ASN 146  146  ?   ?   ?   A . n 
B 1 147  ASN 147  147  ?   ?   ?   A . n 
B 1 148  LYS 148  148  ?   ?   ?   A . n 
B 1 149  SER 149  149  ?   ?   ?   A . n 
B 1 150  TRP 150  150  ?   ?   ?   A . n 
B 1 151  MET 151  151  ?   ?   ?   A . n 
B 1 152  GLU 152  152  ?   ?   ?   A . n 
B 1 153  SER 153  153  ?   ?   ?   A . n 
B 1 154  GLU 154  154  ?   ?   ?   A . n 
B 1 155  SER 155  155  ?   ?   ?   A . n 
B 1 156  GLY 156  156  ?   ?   ?   A . n 
B 1 157  VAL 157  157  ?   ?   ?   A . n 
B 1 158  TYR 158  158  ?   ?   ?   A . n 
B 1 159  SER 159  159  ?   ?   ?   A . n 
B 1 160  SER 160  160  ?   ?   ?   A . n 
B 1 161  ALA 161  161  ?   ?   ?   A . n 
B 1 162  ASN 162  162  ?   ?   ?   A . n 
B 1 163  ASN 163  163  ?   ?   ?   A . n 
B 1 164  CYS 164  164  ?   ?   ?   A . n 
B 1 165  THR 165  165  ?   ?   ?   A . n 
B 1 166  PHE 166  166  ?   ?   ?   A . n 
B 1 167  GLU 167  167  ?   ?   ?   A . n 
B 1 168  TYR 168  168  ?   ?   ?   A . n 
B 1 169  VAL 169  169  ?   ?   ?   A . n 
B 1 170  SER 170  170  ?   ?   ?   A . n 
B 1 171  GLN 171  171  ?   ?   ?   A . n 
B 1 172  PRO 172  172  ?   ?   ?   A . n 
B 1 173  PHE 173  173  ?   ?   ?   A . n 
B 1 174  LEU 174  174  ?   ?   ?   A . n 
B 1 175  MET 175  175  ?   ?   ?   A . n 
B 1 176  ASP 176  176  ?   ?   ?   A . n 
B 1 177  LEU 177  177  ?   ?   ?   A . n 
B 1 178  GLU 178  178  ?   ?   ?   A . n 
B 1 179  GLY 179  179  ?   ?   ?   A . n 
B 1 180  LYS 180  180  ?   ?   ?   A . n 
B 1 181  GLN 181  181  ?   ?   ?   A . n 
B 1 182  GLY 182  182  ?   ?   ?   A . n 
B 1 183  ASN 183  183  ?   ?   ?   A . n 
B 1 184  PHE 184  184  ?   ?   ?   A . n 
B 1 185  LYS 185  185  ?   ?   ?   A . n 
B 1 186  ASN 186  186  ?   ?   ?   A . n 
B 1 187  LEU 187  187  ?   ?   ?   A . n 
B 1 188  ARG 188  188  ?   ?   ?   A . n 
B 1 189  GLU 189  189  ?   ?   ?   A . n 
B 1 190  PHE 190  190  ?   ?   ?   A . n 
B 1 191  VAL 191  191  ?   ?   ?   A . n 
B 1 192  PHE 192  192  ?   ?   ?   A . n 
B 1 193  LYS 193  193  ?   ?   ?   A . n 
B 1 194  ASN 194  194  ?   ?   ?   A . n 
B 1 195  ILE 195  195  ?   ?   ?   A . n 
B 1 196  ASP 196  196  ?   ?   ?   A . n 
B 1 197  GLY 197  197  ?   ?   ?   A . n 
B 1 198  TYR 198  198  ?   ?   ?   A . n 
B 1 199  PHE 199  199  ?   ?   ?   A . n 
B 1 200  LYS 200  200  ?   ?   ?   A . n 
B 1 201  ILE 201  201  ?   ?   ?   A . n 
B 1 202  TYR 202  202  ?   ?   ?   A . n 
B 1 203  SER 203  203  ?   ?   ?   A . n 
B 1 204  LYS 204  204  ?   ?   ?   A . n 
B 1 205  HIS 205  205  ?   ?   ?   A . n 
B 1 206  THR 206  206  ?   ?   ?   A . n 
B 1 207  PRO 207  207  ?   ?   ?   A . n 
B 1 208  ILE 208  208  ?   ?   ?   A . n 
B 1 209  ILE 209  209  ?   ?   ?   A . n 
B 1 210  GLY 210  210  ?   ?   ?   A . n 
B 1 211  ARG 211  211  ?   ?   ?   A . n 
B 1 212  ASP 212  212  ?   ?   ?   A . n 
B 1 213  PHE 213  213  ?   ?   ?   A . n 
B 1 214  PRO 214  214  ?   ?   ?   A . n 
B 1 215  GLN 215  215  ?   ?   ?   A . n 
B 1 216  GLY 216  216  ?   ?   ?   A . n 
B 1 217  PHE 217  217  ?   ?   ?   A . n 
B 1 218  SER 218  218  ?   ?   ?   A . n 
B 1 219  ALA 219  219  ?   ?   ?   A . n 
B 1 220  LEU 220  220  ?   ?   ?   A . n 
B 1 221  GLU 221  221  ?   ?   ?   A . n 
B 1 222  PRO 222  222  ?   ?   ?   A . n 
B 1 223  LEU 223  223  ?   ?   ?   A . n 
B 1 224  VAL 224  224  ?   ?   ?   A . n 
B 1 225  ASP 225  225  ?   ?   ?   A . n 
B 1 226  LEU 226  226  ?   ?   ?   A . n 
B 1 227  PRO 227  227  ?   ?   ?   A . n 
B 1 228  ILE 228  228  ?   ?   ?   A . n 
B 1 229  GLY 229  229  ?   ?   ?   A . n 
B 1 230  ILE 230  230  ?   ?   ?   A . n 
B 1 231  ASN 231  231  ?   ?   ?   A . n 
B 1 232  ILE 232  232  ?   ?   ?   A . n 
B 1 233  THR 233  233  ?   ?   ?   A . n 
B 1 234  ARG 234  234  ?   ?   ?   A . n 
B 1 235  PHE 235  235  ?   ?   ?   A . n 
B 1 236  GLN 236  236  ?   ?   ?   A . n 
B 1 237  THR 237  237  ?   ?   ?   A . n 
B 1 238  LEU 238  238  ?   ?   ?   A . n 
B 1 239  LEU 239  239  ?   ?   ?   A . n 
B 1 240  ALA 240  240  ?   ?   ?   A . n 
B 1 241  LEU 241  241  ?   ?   ?   A . n 
B 1 242  ASN 242  242  ?   ?   ?   A . n 
B 1 243  ARG 243  243  ?   ?   ?   A . n 
B 1 244  SER 244  244  ?   ?   ?   A . n 
B 1 245  TYR 245  245  ?   ?   ?   A . n 
B 1 246  LEU 246  246  ?   ?   ?   A . n 
B 1 247  THR 247  247  ?   ?   ?   A . n 
B 1 248  PRO 248  248  ?   ?   ?   A . n 
B 1 249  GLY 249  249  ?   ?   ?   A . n 
B 1 250  ASP 250  250  ?   ?   ?   A . n 
B 1 251  SER 251  251  ?   ?   ?   A . n 
B 1 252  SER 252  252  ?   ?   ?   A . n 
B 1 253  SER 253  253  ?   ?   ?   A . n 
B 1 254  GLY 254  254  ?   ?   ?   A . n 
B 1 255  TRP 255  255  ?   ?   ?   A . n 
B 1 256  THR 256  256  ?   ?   ?   A . n 
B 1 257  ALA 257  257  ?   ?   ?   A . n 
B 1 258  GLY 258  258  ?   ?   ?   A . n 
B 1 259  ALA 259  259  ?   ?   ?   A . n 
B 1 260  ALA 260  260  ?   ?   ?   A . n 
B 1 261  ASP 261  261  ?   ?   ?   A . n 
B 1 262  TYR 262  262  ?   ?   ?   A . n 
B 1 263  TYR 263  263  ?   ?   ?   A . n 
B 1 264  VAL 264  264  ?   ?   ?   A . n 
B 1 265  GLY 265  265  ?   ?   ?   A . n 
B 1 266  TYR 266  266  ?   ?   ?   A . n 
B 1 267  LEU 267  267  ?   ?   ?   A . n 
B 1 268  GLN 268  268  ?   ?   ?   A . n 
B 1 269  PRO 269  269  ?   ?   ?   A . n 
B 1 270  ARG 270  270  ?   ?   ?   A . n 
B 1 271  THR 271  271  ?   ?   ?   A . n 
B 1 272  PHE 272  272  ?   ?   ?   A . n 
B 1 273  LEU 273  273  ?   ?   ?   A . n 
B 1 274  LEU 274  274  ?   ?   ?   A . n 
B 1 275  LYS 275  275  ?   ?   ?   A . n 
B 1 276  TYR 276  276  ?   ?   ?   A . n 
B 1 277  ASN 277  277  ?   ?   ?   A . n 
B 1 278  GLU 278  278  ?   ?   ?   A . n 
B 1 279  ASN 279  279  ?   ?   ?   A . n 
B 1 280  GLY 280  280  ?   ?   ?   A . n 
B 1 281  THR 281  281  ?   ?   ?   A . n 
B 1 282  ILE 282  282  ?   ?   ?   A . n 
B 1 283  THR 283  283  ?   ?   ?   A . n 
B 1 284  ASP 284  284  ?   ?   ?   A . n 
B 1 285  ALA 285  285  ?   ?   ?   A . n 
B 1 286  VAL 286  286  ?   ?   ?   A . n 
B 1 287  ASP 287  287  ?   ?   ?   A . n 
B 1 288  CYS 288  288  ?   ?   ?   A . n 
B 1 289  ALA 289  289  ?   ?   ?   A . n 
B 1 290  LEU 290  290  ?   ?   ?   A . n 
B 1 291  ASP 291  291  ?   ?   ?   A . n 
B 1 292  PRO 292  292  ?   ?   ?   A . n 
B 1 293  LEU 293  293  ?   ?   ?   A . n 
B 1 294  SER 294  294  ?   ?   ?   A . n 
B 1 295  GLU 295  295  ?   ?   ?   A . n 
B 1 296  THR 296  296  ?   ?   ?   A . n 
B 1 297  LYS 297  297  ?   ?   ?   A . n 
B 1 298  CYS 298  298  ?   ?   ?   A . n 
B 1 299  THR 299  299  ?   ?   ?   A . n 
B 1 300  LEU 300  300  ?   ?   ?   A . n 
B 1 301  LYS 301  301  ?   ?   ?   A . n 
B 1 302  SER 302  302  ?   ?   ?   A . n 
B 1 303  PHE 303  303  ?   ?   ?   A . n 
B 1 304  THR 304  304  ?   ?   ?   A . n 
B 1 305  VAL 305  305  ?   ?   ?   A . n 
B 1 306  GLU 306  306  ?   ?   ?   A . n 
B 1 307  LYS 307  307  ?   ?   ?   A . n 
B 1 308  GLY 308  308  ?   ?   ?   A . n 
B 1 309  ILE 309  309  ?   ?   ?   A . n 
B 1 310  TYR 310  310  ?   ?   ?   A . n 
B 1 311  GLN 311  311  ?   ?   ?   A . n 
B 1 312  THR 312  312  ?   ?   ?   A . n 
B 1 313  SER 313  313  ?   ?   ?   A . n 
B 1 314  ASN 314  314  ?   ?   ?   A . n 
B 1 315  PHE 315  315  ?   ?   ?   A . n 
B 1 316  ARG 316  316  ?   ?   ?   A . n 
B 1 317  VAL 317  317  ?   ?   ?   A . n 
B 1 318  GLN 318  318  ?   ?   ?   A . n 
B 1 319  PRO 319  319  ?   ?   ?   A . n 
B 1 320  THR 320  320  ?   ?   ?   A . n 
B 1 321  GLU 321  321  ?   ?   ?   A . n 
B 1 322  SER 322  322  ?   ?   ?   A . n 
B 1 323  ILE 323  323  323 ILE ILE A . n 
B 1 324  VAL 324  324  324 VAL VAL A . n 
B 1 325  ARG 325  325  325 ARG ARG A . n 
B 1 326  PHE 326  326  326 PHE PHE A . n 
B 1 327  PRO 327  327  327 PRO PRO A . n 
B 1 328  ASN 328  328  328 ASN ASN A . n 
B 1 329  VAL 329  329  329 VAL VAL A . n 
B 1 330  THR 330  330  330 THR THR A . n 
B 1 331  ASN 331  331  331 ASN ASN A . n 
B 1 332  LEU 332  332  332 LEU LEU A . n 
B 1 333  CYS 333  333  333 CYS CYS A . n 
B 1 334  PRO 334  334  334 PRO PRO A . n 
B 1 335  PHE 335  335  335 PHE PHE A . n 
B 1 336  HIS 336  336  336 HIS HIS A . n 
B 1 337  GLU 337  337  337 GLU GLU A . n 
B 1 338  VAL 338  338  338 VAL VAL A . n 
B 1 339  PHE 339  339  339 PHE PHE A . n 
B 1 340  ASN 340  340  340 ASN ASN A . n 
B 1 341  ALA 341  341  341 ALA ALA A . n 
B 1 342  THR 342  342  342 THR THR A . n 
B 1 343  ARG 343  343  343 ARG ARG A . n 
B 1 344  PHE 344  344  344 PHE PHE A . n 
B 1 345  ALA 345  345  345 ALA ALA A . n 
B 1 346  SER 346  346  346 SER SER A . n 
B 1 347  VAL 347  347  347 VAL VAL A . n 
B 1 348  TYR 348  348  348 TYR TYR A . n 
B 1 349  ALA 349  349  349 ALA ALA A . n 
B 1 350  TRP 350  350  350 TRP TRP A . n 
B 1 351  ASN 351  351  351 ASN ASN A . n 
B 1 352  ARG 352  352  352 ARG ARG A . n 
B 1 353  THR 353  353  353 THR THR A . n 
B 1 354  ARG 354  354  354 ARG ARG A . n 
B 1 355  ILE 355  355  355 ILE ILE A . n 
B 1 356  SER 356  356  356 SER SER A . n 
B 1 357  ASN 357  357  357 ASN ASN A . n 
B 1 358  CYS 358  358  358 CYS CYS A . n 
B 1 359  VAL 359  359  359 VAL VAL A . n 
B 1 360  ALA 360  360  360 ALA ALA A . n 
B 1 361  ASP 361  361  361 ASP ASP A . n 
B 1 362  TYR 362  362  362 TYR TYR A . n 
B 1 363  SER 363  363  363 SER SER A . n 
B 1 364  VAL 364  364  364 VAL VAL A . n 
B 1 365  LEU 365  365  365 LEU LEU A . n 
B 1 366  TYR 366  366  366 TYR TYR A . n 
B 1 367  ASN 367  367  367 ASN ASN A . n 
B 1 368  PHE 368  368  368 PHE PHE A . n 
B 1 369  ALA 369  369  369 ALA ALA A . n 
B 1 370  PRO 370  370  370 PRO PRO A . n 
B 1 371  PHE 371  371  371 PHE PHE A . n 
B 1 372  PHE 372  372  372 PHE PHE A . n 
B 1 373  ALA 373  373  373 ALA ALA A . n 
B 1 374  PHE 374  374  374 PHE PHE A . n 
B 1 375  LYS 375  375  375 LYS LYS A . n 
B 1 376  CYS 376  376  376 CYS CYS A . n 
B 1 377  TYR 377  377  377 TYR TYR A . n 
B 1 378  GLY 378  378  378 GLY GLY A . n 
B 1 379  VAL 379  379  379 VAL VAL A . n 
B 1 380  SER 380  380  380 SER SER A . n 
B 1 381  PRO 381  381  381 PRO PRO A . n 
B 1 382  THR 382  382  382 THR THR A . n 
B 1 383  LYS 383  383  383 LYS LYS A . n 
B 1 384  LEU 384  384  384 LEU LEU A . n 
B 1 385  ASN 385  385  385 ASN ASN A . n 
B 1 386  ASP 386  386  386 ASP ASP A . n 
B 1 387  LEU 387  387  387 LEU LEU A . n 
B 1 388  CYS 388  388  388 CYS CYS A . n 
B 1 389  PHE 389  389  389 PHE PHE A . n 
B 1 390  THR 390  390  390 THR THR A . n 
B 1 391  ASN 391  391  391 ASN ASN A . n 
B 1 392  VAL 392  392  392 VAL VAL A . n 
B 1 393  TYR 393  393  393 TYR TYR A . n 
B 1 394  ALA 394  394  394 ALA ALA A . n 
B 1 395  ASP 395  395  395 ASP ASP A . n 
B 1 396  SER 396  396  396 SER SER A . n 
B 1 397  PHE 397  397  397 PHE PHE A . n 
B 1 398  VAL 398  398  398 VAL VAL A . n 
B 1 399  ILE 399  399  399 ILE ILE A . n 
B 1 400  LYS 400  400  400 LYS LYS A . n 
B 1 401  GLY 401  401  401 GLY GLY A . n 
B 1 402  ASN 402  402  402 ASN ASN A . n 
B 1 403  GLU 403  403  403 GLU GLU A . n 
B 1 404  VAL 404  404  404 VAL VAL A . n 
B 1 405  SER 405  405  405 SER SER A . n 
B 1 406  GLN 406  406  406 GLN GLN A . n 
B 1 407  ILE 407  407  407 ILE ILE A . n 
B 1 408  ALA 408  408  408 ALA ALA A . n 
B 1 409  PRO 409  409  409 PRO PRO A . n 
B 1 410  GLY 410  410  410 GLY GLY A . n 
B 1 411  GLN 411  411  411 GLN GLN A . n 
B 1 412  THR 412  412  412 THR THR A . n 
B 1 413  GLY 413  413  413 GLY GLY A . n 
B 1 414  ASN 414  414  414 ASN ASN A . n 
B 1 415  ILE 415  415  415 ILE ILE A . n 
B 1 416  ALA 416  416  416 ALA ALA A . n 
B 1 417  ASP 417  417  417 ASP ASP A . n 
B 1 418  TYR 418  418  418 TYR TYR A . n 
B 1 419  ASN 419  419  419 ASN ASN A . n 
B 1 420  TYR 420  420  420 TYR TYR A . n 
B 1 421  LYS 421  421  421 LYS LYS A . n 
B 1 422  LEU 422  422  422 LEU LEU A . n 
B 1 423  PRO 423  423  423 PRO PRO A . n 
B 1 424  ASP 424  424  424 ASP ASP A . n 
B 1 425  ASP 425  425  425 ASP ASP A . n 
B 1 426  PHE 426  426  426 PHE PHE A . n 
B 1 427  THR 427  427  427 THR THR A . n 
B 1 428  GLY 428  428  428 GLY GLY A . n 
B 1 429  CYS 429  429  429 CYS CYS A . n 
B 1 430  VAL 430  430  430 VAL VAL A . n 
B 1 431  ILE 431  431  431 ILE ILE A . n 
B 1 432  ALA 432  432  432 ALA ALA A . n 
B 1 433  TRP 433  433  433 TRP TRP A . n 
B 1 434  ASN 434  434  434 ASN ASN A . n 
B 1 435  SER 435  435  435 SER SER A . n 
B 1 436  ASN 436  436  436 ASN ASN A . n 
B 1 437  LYS 437  437  437 LYS LYS A . n 
B 1 438  LEU 438  438  438 LEU LEU A . n 
B 1 439  ASP 439  439  439 ASP ASP A . n 
B 1 440  SER 440  440  440 SER SER A . n 
B 1 441  LYS 441  441  441 LYS LYS A . n 
B 1 442  HIS 442  442  442 HIS HIS A . n 
B 1 443  SER 443  443  443 SER SER A . n 
B 1 444  GLY 444  444  444 GLY GLY A . n 
B 1 445  ASN 445  445  445 ASN ASN A . n 
B 1 446  TYR 446  446  446 TYR TYR A . n 
B 1 447  ASP 447  447  447 ASP ASP A . n 
B 1 448  TYR 448  448  448 TYR TYR A . n 
B 1 449  TRP 449  449  449 TRP TRP A . n 
B 1 450  TYR 450  450  450 TYR TYR A . n 
B 1 451  ARG 451  451  451 ARG ARG A . n 
B 1 452  SER 452  452  452 SER SER A . n 
B 1 453  PHE 453  453  453 PHE PHE A . n 
B 1 454  ARG 454  454  454 ARG ARG A . n 
B 1 455  LYS 455  455  455 LYS LYS A . n 
B 1 456  SER 456  456  456 SER SER A . n 
B 1 457  LYS 457  457  457 LYS LYS A . n 
B 1 458  LEU 458  458  458 LEU LEU A . n 
B 1 459  LYS 459  459  459 LYS LYS A . n 
B 1 460  PRO 460  460  460 PRO PRO A . n 
B 1 461  PHE 461  461  461 PHE PHE A . n 
B 1 462  GLU 462  462  462 GLU GLU A . n 
B 1 463  ARG 463  463  463 ARG ARG A . n 
B 1 464  ASP 464  464  464 ASP ASP A . n 
B 1 465  ILE 465  465  465 ILE ILE A . n 
B 1 466  SER 466  466  466 SER SER A . n 
B 1 467  THR 467  467  467 THR THR A . n 
B 1 468  GLU 468  468  468 GLU GLU A . n 
B 1 469  ILE 469  469  469 ILE ILE A . n 
B 1 470  TYR 470  470  470 TYR TYR A . n 
B 1 471  GLN 471  471  471 GLN GLN A . n 
B 1 472  ALA 472  472  472 ALA ALA A . n 
B 1 473  GLY 473  473  473 GLY GLY A . n 
B 1 474  ASN 474  474  474 ASN ASN A . n 
B 1 475  LYS 475  475  475 LYS LYS A . n 
B 1 476  PRO 476  476  476 PRO PRO A . n 
B 1 477  CYS 477  477  477 CYS CYS A . n 
B 1 478  LYS 478  478  478 LYS LYS A . n 
B 1 479  GLY 479  479  479 GLY GLY A . n 
B 1 480  LYS 480  480  480 LYS LYS A . n 
B 1 481  GLY 481  481  481 GLY GLY A . n 
B 1 482  PRO 482  482  482 PRO PRO A . n 
B 1 483  ASN 483  483  483 ASN ASN A . n 
B 1 484  CYS 484  484  484 CYS CYS A . n 
B 1 485  TYR 485  485  485 TYR TYR A . n 
B 1 486  PHE 486  486  486 PHE PHE A . n 
B 1 487  PRO 487  487  487 PRO PRO A . n 
B 1 488  LEU 488  488  488 LEU LEU A . n 
B 1 489  GLN 489  489  489 GLN GLN A . n 
B 1 490  SER 490  490  490 SER SER A . n 
B 1 491  TYR 491  491  491 TYR TYR A . n 
B 1 492  GLY 492  492  492 GLY GLY A . n 
B 1 493  PHE 493  493  493 PHE PHE A . n 
B 1 494  ARG 494  494  494 ARG ARG A . n 
B 1 495  PRO 495  495  495 PRO PRO A . n 
B 1 496  THR 496  496  496 THR THR A . n 
B 1 497  TYR 497  497  497 TYR TYR A . n 
B 1 498  GLY 498  498  498 GLY GLY A . n 
B 1 499  VAL 499  499  499 VAL VAL A . n 
B 1 500  GLY 500  500  500 GLY GLY A . n 
B 1 501  HIS 501  501  501 HIS HIS A . n 
B 1 502  GLN 502  502  502 GLN GLN A . n 
B 1 503  PRO 503  503  503 PRO PRO A . n 
B 1 504  TYR 504  504  504 TYR TYR A . n 
B 1 505  ARG 505  505  505 ARG ARG A . n 
B 1 506  VAL 506  506  506 VAL VAL A . n 
B 1 507  VAL 507  507  507 VAL VAL A . n 
B 1 508  VAL 508  508  508 VAL VAL A . n 
B 1 509  LEU 509  509  509 LEU LEU A . n 
B 1 510  SER 510  510  510 SER SER A . n 
B 1 511  PHE 511  511  511 PHE PHE A . n 
B 1 512  GLU 512  512  512 GLU GLU A . n 
B 1 513  LEU 513  513  513 LEU LEU A . n 
B 1 514  LEU 514  514  514 LEU LEU A . n 
B 1 515  HIS 515  515  515 HIS HIS A . n 
B 1 516  ALA 516  516  516 ALA ALA A . n 
B 1 517  PRO 517  517  517 PRO PRO A . n 
B 1 518  ALA 518  518  518 ALA ALA A . n 
B 1 519  THR 519  519  519 THR THR A . n 
B 1 520  VAL 520  520  520 VAL VAL A . n 
B 1 521  CYS 521  521  521 CYS CYS A . n 
B 1 522  GLY 522  522  522 GLY GLY A . n 
B 1 523  PRO 523  523  523 PRO PRO A . n 
B 1 524  LYS 524  524  524 LYS LYS A . n 
B 1 525  LYS 525  525  525 LYS LYS A . n 
B 1 526  SER 526  526  ?   ?   ?   A . n 
B 1 527  THR 527  527  ?   ?   ?   A . n 
B 1 528  ASN 528  528  ?   ?   ?   A . n 
B 1 529  LEU 529  529  ?   ?   ?   A . n 
B 1 530  VAL 530  530  ?   ?   ?   A . n 
B 1 531  LYS 531  531  ?   ?   ?   A . n 
B 1 532  ASN 532  532  ?   ?   ?   A . n 
B 1 533  LYS 533  533  ?   ?   ?   A . n 
B 1 534  CYS 534  534  ?   ?   ?   A . n 
B 1 535  VAL 535  535  ?   ?   ?   A . n 
B 1 536  ASN 536  536  ?   ?   ?   A . n 
B 1 537  PHE 537  537  ?   ?   ?   A . n 
B 1 538  ASN 538  538  ?   ?   ?   A . n 
B 1 539  PHE 539  539  ?   ?   ?   A . n 
B 1 540  ASN 540  540  ?   ?   ?   A . n 
B 1 541  GLY 541  541  ?   ?   ?   A . n 
B 1 542  LEU 542  542  ?   ?   ?   A . n 
B 1 543  THR 543  543  ?   ?   ?   A . n 
B 1 544  GLY 544  544  ?   ?   ?   A . n 
B 1 545  THR 545  545  ?   ?   ?   A . n 
B 1 546  GLY 546  546  ?   ?   ?   A . n 
B 1 547  VAL 547  547  ?   ?   ?   A . n 
B 1 548  LEU 548  548  ?   ?   ?   A . n 
B 1 549  THR 549  549  ?   ?   ?   A . n 
B 1 550  LYS 550  550  ?   ?   ?   A . n 
B 1 551  SER 551  551  ?   ?   ?   A . n 
B 1 552  ASN 552  552  ?   ?   ?   A . n 
B 1 553  LYS 553  553  ?   ?   ?   A . n 
B 1 554  LYS 554  554  ?   ?   ?   A . n 
B 1 555  PHE 555  555  ?   ?   ?   A . n 
B 1 556  LEU 556  556  ?   ?   ?   A . n 
B 1 557  PRO 557  557  ?   ?   ?   A . n 
B 1 558  PHE 558  558  ?   ?   ?   A . n 
B 1 559  GLN 559  559  ?   ?   ?   A . n 
B 1 560  GLN 560  560  ?   ?   ?   A . n 
B 1 561  PHE 561  561  ?   ?   ?   A . n 
B 1 562  GLY 562  562  ?   ?   ?   A . n 
B 1 563  ARG 563  563  ?   ?   ?   A . n 
B 1 564  ASP 564  564  ?   ?   ?   A . n 
B 1 565  ILE 565  565  ?   ?   ?   A . n 
B 1 566  VAL 566  566  ?   ?   ?   A . n 
B 1 567  ASP 567  567  ?   ?   ?   A . n 
B 1 568  THR 568  568  ?   ?   ?   A . n 
B 1 569  THR 569  569  ?   ?   ?   A . n 
B 1 570  ASP 570  570  ?   ?   ?   A . n 
B 1 571  ALA 571  571  ?   ?   ?   A . n 
B 1 572  VAL 572  572  ?   ?   ?   A . n 
B 1 573  ARG 573  573  ?   ?   ?   A . n 
B 1 574  ASP 574  574  ?   ?   ?   A . n 
B 1 575  PRO 575  575  ?   ?   ?   A . n 
B 1 576  GLN 576  576  ?   ?   ?   A . n 
B 1 577  THR 577  577  ?   ?   ?   A . n 
B 1 578  LEU 578  578  ?   ?   ?   A . n 
B 1 579  GLU 579  579  ?   ?   ?   A . n 
B 1 580  ILE 580  580  ?   ?   ?   A . n 
B 1 581  LEU 581  581  ?   ?   ?   A . n 
B 1 582  ASP 582  582  ?   ?   ?   A . n 
B 1 583  ILE 583  583  ?   ?   ?   A . n 
B 1 584  THR 584  584  ?   ?   ?   A . n 
B 1 585  PRO 585  585  ?   ?   ?   A . n 
B 1 586  CYS 586  586  ?   ?   ?   A . n 
B 1 587  SER 587  587  ?   ?   ?   A . n 
B 1 588  PHE 588  588  ?   ?   ?   A . n 
B 1 589  GLY 589  589  ?   ?   ?   A . n 
B 1 590  GLY 590  590  ?   ?   ?   A . n 
B 1 591  VAL 591  591  ?   ?   ?   A . n 
B 1 592  SER 592  592  ?   ?   ?   A . n 
B 1 593  VAL 593  593  ?   ?   ?   A . n 
B 1 594  ILE 594  594  ?   ?   ?   A . n 
B 1 595  THR 595  595  ?   ?   ?   A . n 
B 1 596  PRO 596  596  ?   ?   ?   A . n 
B 1 597  GLY 597  597  ?   ?   ?   A . n 
B 1 598  THR 598  598  ?   ?   ?   A . n 
B 1 599  ASN 599  599  ?   ?   ?   A . n 
B 1 600  THR 600  600  ?   ?   ?   A . n 
B 1 601  SER 601  601  ?   ?   ?   A . n 
B 1 602  ASN 602  602  ?   ?   ?   A . n 
B 1 603  GLN 603  603  ?   ?   ?   A . n 
B 1 604  VAL 604  604  ?   ?   ?   A . n 
B 1 605  ALA 605  605  ?   ?   ?   A . n 
B 1 606  VAL 606  606  ?   ?   ?   A . n 
B 1 607  LEU 607  607  ?   ?   ?   A . n 
B 1 608  TYR 608  608  ?   ?   ?   A . n 
B 1 609  GLN 609  609  ?   ?   ?   A . n 
B 1 610  GLY 610  610  ?   ?   ?   A . n 
B 1 611  VAL 611  611  ?   ?   ?   A . n 
B 1 612  ASN 612  612  ?   ?   ?   A . n 
B 1 613  CYS 613  613  ?   ?   ?   A . n 
B 1 614  THR 614  614  ?   ?   ?   A . n 
B 1 615  GLU 615  615  ?   ?   ?   A . n 
B 1 616  VAL 616  616  ?   ?   ?   A . n 
B 1 617  SER 617  617  ?   ?   ?   A . n 
B 1 618  VAL 618  618  ?   ?   ?   A . n 
B 1 619  ALA 619  619  ?   ?   ?   A . n 
B 1 620  ILE 620  620  ?   ?   ?   A . n 
B 1 621  HIS 621  621  ?   ?   ?   A . n 
B 1 622  ALA 622  622  ?   ?   ?   A . n 
B 1 623  ASP 623  623  ?   ?   ?   A . n 
B 1 624  GLN 624  624  ?   ?   ?   A . n 
B 1 625  LEU 625  625  ?   ?   ?   A . n 
B 1 626  THR 626  626  ?   ?   ?   A . n 
B 1 627  PRO 627  627  ?   ?   ?   A . n 
B 1 628  THR 628  628  ?   ?   ?   A . n 
B 1 629  TRP 629  629  ?   ?   ?   A . n 
B 1 630  ARG 630  630  ?   ?   ?   A . n 
B 1 631  VAL 631  631  ?   ?   ?   A . n 
B 1 632  TYR 632  632  ?   ?   ?   A . n 
B 1 633  SER 633  633  ?   ?   ?   A . n 
B 1 634  THR 634  634  ?   ?   ?   A . n 
B 1 635  GLY 635  635  ?   ?   ?   A . n 
B 1 636  SER 636  636  ?   ?   ?   A . n 
B 1 637  ASN 637  637  ?   ?   ?   A . n 
B 1 638  VAL 638  638  ?   ?   ?   A . n 
B 1 639  PHE 639  639  ?   ?   ?   A . n 
B 1 640  GLN 640  640  ?   ?   ?   A . n 
B 1 641  THR 641  641  ?   ?   ?   A . n 
B 1 642  ARG 642  642  ?   ?   ?   A . n 
B 1 643  ALA 643  643  ?   ?   ?   A . n 
B 1 644  GLY 644  644  ?   ?   ?   A . n 
B 1 645  CYS 645  645  ?   ?   ?   A . n 
B 1 646  LEU 646  646  ?   ?   ?   A . n 
B 1 647  ILE 647  647  ?   ?   ?   A . n 
B 1 648  GLY 648  648  ?   ?   ?   A . n 
B 1 649  ALA 649  649  ?   ?   ?   A . n 
B 1 650  GLU 650  650  ?   ?   ?   A . n 
B 1 651  TYR 651  651  ?   ?   ?   A . n 
B 1 652  VAL 652  652  ?   ?   ?   A . n 
B 1 653  ASN 653  653  ?   ?   ?   A . n 
B 1 654  ASN 654  654  ?   ?   ?   A . n 
B 1 655  SER 655  655  ?   ?   ?   A . n 
B 1 656  TYR 656  656  ?   ?   ?   A . n 
B 1 657  GLU 657  657  ?   ?   ?   A . n 
B 1 658  CYS 658  658  ?   ?   ?   A . n 
B 1 659  ASP 659  659  ?   ?   ?   A . n 
B 1 660  ILE 660  660  ?   ?   ?   A . n 
B 1 661  PRO 661  661  ?   ?   ?   A . n 
B 1 662  ILE 662  662  ?   ?   ?   A . n 
B 1 663  GLY 663  663  ?   ?   ?   A . n 
B 1 664  ALA 664  664  ?   ?   ?   A . n 
B 1 665  GLY 665  665  ?   ?   ?   A . n 
B 1 666  ILE 666  666  ?   ?   ?   A . n 
B 1 667  CYS 667  667  ?   ?   ?   A . n 
B 1 668  ALA 668  668  ?   ?   ?   A . n 
B 1 669  SER 669  669  ?   ?   ?   A . n 
B 1 670  TYR 670  670  ?   ?   ?   A . n 
B 1 671  GLN 671  671  ?   ?   ?   A . n 
B 1 672  THR 672  672  ?   ?   ?   A . n 
B 1 673  GLN 673  673  ?   ?   ?   A . n 
B 1 674  THR 674  674  ?   ?   ?   A . n 
B 1 675  LYS 675  675  ?   ?   ?   A . n 
B 1 676  SER 676  676  ?   ?   ?   A . n 
B 1 677  ARG 677  677  ?   ?   ?   A . n 
B 1 678  ALA 678  678  ?   ?   ?   A . n 
B 1 679  GLY 679  679  ?   ?   ?   A . n 
B 1 680  ALA 680  680  ?   ?   ?   A . n 
B 1 681  ARG 681  681  ?   ?   ?   A . n 
B 1 682  SER 682  682  ?   ?   ?   A . n 
B 1 683  VAL 683  683  ?   ?   ?   A . n 
B 1 684  ALA 684  684  ?   ?   ?   A . n 
B 1 685  SER 685  685  ?   ?   ?   A . n 
B 1 686  GLN 686  686  ?   ?   ?   A . n 
B 1 687  SER 687  687  ?   ?   ?   A . n 
B 1 688  ILE 688  688  ?   ?   ?   A . n 
B 1 689  ILE 689  689  ?   ?   ?   A . n 
B 1 690  ALA 690  690  ?   ?   ?   A . n 
B 1 691  TYR 691  691  ?   ?   ?   A . n 
B 1 692  THR 692  692  ?   ?   ?   A . n 
B 1 693  MET 693  693  ?   ?   ?   A . n 
B 1 694  SER 694  694  ?   ?   ?   A . n 
B 1 695  LEU 695  695  ?   ?   ?   A . n 
B 1 696  GLY 696  696  ?   ?   ?   A . n 
B 1 697  ALA 697  697  ?   ?   ?   A . n 
B 1 698  GLU 698  698  ?   ?   ?   A . n 
B 1 699  ASN 699  699  ?   ?   ?   A . n 
B 1 700  SER 700  700  ?   ?   ?   A . n 
B 1 701  VAL 701  701  ?   ?   ?   A . n 
B 1 702  ALA 702  702  ?   ?   ?   A . n 
B 1 703  TYR 703  703  ?   ?   ?   A . n 
B 1 704  SER 704  704  ?   ?   ?   A . n 
B 1 705  ASN 705  705  ?   ?   ?   A . n 
B 1 706  ASN 706  706  ?   ?   ?   A . n 
B 1 707  SER 707  707  ?   ?   ?   A . n 
B 1 708  ILE 708  708  ?   ?   ?   A . n 
B 1 709  ALA 709  709  ?   ?   ?   A . n 
B 1 710  ILE 710  710  ?   ?   ?   A . n 
B 1 711  PRO 711  711  ?   ?   ?   A . n 
B 1 712  THR 712  712  ?   ?   ?   A . n 
B 1 713  ASN 713  713  ?   ?   ?   A . n 
B 1 714  PHE 714  714  ?   ?   ?   A . n 
B 1 715  THR 715  715  ?   ?   ?   A . n 
B 1 716  ILE 716  716  ?   ?   ?   A . n 
B 1 717  SER 717  717  ?   ?   ?   A . n 
B 1 718  VAL 718  718  ?   ?   ?   A . n 
B 1 719  THR 719  719  ?   ?   ?   A . n 
B 1 720  THR 720  720  ?   ?   ?   A . n 
B 1 721  GLU 721  721  ?   ?   ?   A . n 
B 1 722  ILE 722  722  ?   ?   ?   A . n 
B 1 723  LEU 723  723  ?   ?   ?   A . n 
B 1 724  PRO 724  724  ?   ?   ?   A . n 
B 1 725  VAL 725  725  ?   ?   ?   A . n 
B 1 726  SER 726  726  ?   ?   ?   A . n 
B 1 727  MET 727  727  ?   ?   ?   A . n 
B 1 728  THR 728  728  ?   ?   ?   A . n 
B 1 729  LYS 729  729  ?   ?   ?   A . n 
B 1 730  THR 730  730  ?   ?   ?   A . n 
B 1 731  SER 731  731  ?   ?   ?   A . n 
B 1 732  VAL 732  732  ?   ?   ?   A . n 
B 1 733  ASP 733  733  ?   ?   ?   A . n 
B 1 734  CYS 734  734  ?   ?   ?   A . n 
B 1 735  THR 735  735  ?   ?   ?   A . n 
B 1 736  MET 736  736  ?   ?   ?   A . n 
B 1 737  TYR 737  737  ?   ?   ?   A . n 
B 1 738  ILE 738  738  ?   ?   ?   A . n 
B 1 739  CYS 739  739  ?   ?   ?   A . n 
B 1 740  GLY 740  740  ?   ?   ?   A . n 
B 1 741  ASP 741  741  ?   ?   ?   A . n 
B 1 742  SER 742  742  ?   ?   ?   A . n 
B 1 743  THR 743  743  ?   ?   ?   A . n 
B 1 744  GLU 744  744  ?   ?   ?   A . n 
B 1 745  CYS 745  745  ?   ?   ?   A . n 
B 1 746  SER 746  746  ?   ?   ?   A . n 
B 1 747  ASN 747  747  ?   ?   ?   A . n 
B 1 748  LEU 748  748  ?   ?   ?   A . n 
B 1 749  LEU 749  749  ?   ?   ?   A . n 
B 1 750  LEU 750  750  ?   ?   ?   A . n 
B 1 751  GLN 751  751  ?   ?   ?   A . n 
B 1 752  TYR 752  752  ?   ?   ?   A . n 
B 1 753  GLY 753  753  ?   ?   ?   A . n 
B 1 754  SER 754  754  ?   ?   ?   A . n 
B 1 755  PHE 755  755  ?   ?   ?   A . n 
B 1 756  CYS 756  756  ?   ?   ?   A . n 
B 1 757  THR 757  757  ?   ?   ?   A . n 
B 1 758  GLN 758  758  ?   ?   ?   A . n 
B 1 759  LEU 759  759  ?   ?   ?   A . n 
B 1 760  LYS 760  760  ?   ?   ?   A . n 
B 1 761  ARG 761  761  ?   ?   ?   A . n 
B 1 762  ALA 762  762  ?   ?   ?   A . n 
B 1 763  LEU 763  763  ?   ?   ?   A . n 
B 1 764  THR 764  764  ?   ?   ?   A . n 
B 1 765  GLY 765  765  ?   ?   ?   A . n 
B 1 766  ILE 766  766  ?   ?   ?   A . n 
B 1 767  ALA 767  767  ?   ?   ?   A . n 
B 1 768  VAL 768  768  ?   ?   ?   A . n 
B 1 769  GLU 769  769  ?   ?   ?   A . n 
B 1 770  GLN 770  770  ?   ?   ?   A . n 
B 1 771  ASP 771  771  ?   ?   ?   A . n 
B 1 772  LYS 772  772  ?   ?   ?   A . n 
B 1 773  ASN 773  773  ?   ?   ?   A . n 
B 1 774  THR 774  774  ?   ?   ?   A . n 
B 1 775  GLN 775  775  ?   ?   ?   A . n 
B 1 776  GLU 776  776  ?   ?   ?   A . n 
B 1 777  VAL 777  777  ?   ?   ?   A . n 
B 1 778  PHE 778  778  ?   ?   ?   A . n 
B 1 779  ALA 779  779  ?   ?   ?   A . n 
B 1 780  GLN 780  780  ?   ?   ?   A . n 
B 1 781  VAL 781  781  ?   ?   ?   A . n 
B 1 782  LYS 782  782  ?   ?   ?   A . n 
B 1 783  GLN 783  783  ?   ?   ?   A . n 
B 1 784  ILE 784  784  ?   ?   ?   A . n 
B 1 785  TYR 785  785  ?   ?   ?   A . n 
B 1 786  LYS 786  786  ?   ?   ?   A . n 
B 1 787  THR 787  787  ?   ?   ?   A . n 
B 1 788  PRO 788  788  ?   ?   ?   A . n 
B 1 789  PRO 789  789  ?   ?   ?   A . n 
B 1 790  ILE 790  790  ?   ?   ?   A . n 
B 1 791  LYS 791  791  ?   ?   ?   A . n 
B 1 792  TYR 792  792  ?   ?   ?   A . n 
B 1 793  PHE 793  793  ?   ?   ?   A . n 
B 1 794  GLY 794  794  ?   ?   ?   A . n 
B 1 795  GLY 795  795  ?   ?   ?   A . n 
B 1 796  PHE 796  796  ?   ?   ?   A . n 
B 1 797  ASN 797  797  ?   ?   ?   A . n 
B 1 798  PHE 798  798  ?   ?   ?   A . n 
B 1 799  SER 799  799  ?   ?   ?   A . n 
B 1 800  GLN 800  800  ?   ?   ?   A . n 
B 1 801  ILE 801  801  ?   ?   ?   A . n 
B 1 802  LEU 802  802  ?   ?   ?   A . n 
B 1 803  PRO 803  803  ?   ?   ?   A . n 
B 1 804  ASP 804  804  ?   ?   ?   A . n 
B 1 805  PRO 805  805  ?   ?   ?   A . n 
B 1 806  SER 806  806  ?   ?   ?   A . n 
B 1 807  LYS 807  807  ?   ?   ?   A . n 
B 1 808  PRO 808  808  ?   ?   ?   A . n 
B 1 809  SER 809  809  ?   ?   ?   A . n 
B 1 810  LYS 810  810  ?   ?   ?   A . n 
B 1 811  ARG 811  811  ?   ?   ?   A . n 
B 1 812  SER 812  812  ?   ?   ?   A . n 
B 1 813  PRO 813  813  ?   ?   ?   A . n 
B 1 814  ILE 814  814  ?   ?   ?   A . n 
B 1 815  GLU 815  815  ?   ?   ?   A . n 
B 1 816  ASP 816  816  ?   ?   ?   A . n 
B 1 817  LEU 817  817  ?   ?   ?   A . n 
B 1 818  LEU 818  818  ?   ?   ?   A . n 
B 1 819  PHE 819  819  ?   ?   ?   A . n 
B 1 820  ASN 820  820  ?   ?   ?   A . n 
B 1 821  LYS 821  821  ?   ?   ?   A . n 
B 1 822  VAL 822  822  ?   ?   ?   A . n 
B 1 823  THR 823  823  ?   ?   ?   A . n 
B 1 824  LEU 824  824  ?   ?   ?   A . n 
B 1 825  ALA 825  825  ?   ?   ?   A . n 
B 1 826  ASP 826  826  ?   ?   ?   A . n 
B 1 827  ALA 827  827  ?   ?   ?   A . n 
B 1 828  GLY 828  828  ?   ?   ?   A . n 
B 1 829  PHE 829  829  ?   ?   ?   A . n 
B 1 830  ILE 830  830  ?   ?   ?   A . n 
B 1 831  LYS 831  831  ?   ?   ?   A . n 
B 1 832  GLN 832  832  ?   ?   ?   A . n 
B 1 833  TYR 833  833  ?   ?   ?   A . n 
B 1 834  GLY 834  834  ?   ?   ?   A . n 
B 1 835  ASP 835  835  ?   ?   ?   A . n 
B 1 836  CYS 836  836  ?   ?   ?   A . n 
B 1 837  LEU 837  837  ?   ?   ?   A . n 
B 1 838  GLY 838  838  ?   ?   ?   A . n 
B 1 839  ASP 839  839  ?   ?   ?   A . n 
B 1 840  ILE 840  840  ?   ?   ?   A . n 
B 1 841  ALA 841  841  ?   ?   ?   A . n 
B 1 842  ALA 842  842  ?   ?   ?   A . n 
B 1 843  ARG 843  843  ?   ?   ?   A . n 
B 1 844  ASP 844  844  ?   ?   ?   A . n 
B 1 845  LEU 845  845  ?   ?   ?   A . n 
B 1 846  ILE 846  846  ?   ?   ?   A . n 
B 1 847  CYS 847  847  ?   ?   ?   A . n 
B 1 848  ALA 848  848  ?   ?   ?   A . n 
B 1 849  GLN 849  849  ?   ?   ?   A . n 
B 1 850  LYS 850  850  ?   ?   ?   A . n 
B 1 851  PHE 851  851  ?   ?   ?   A . n 
B 1 852  ASN 852  852  ?   ?   ?   A . n 
B 1 853  GLY 853  853  ?   ?   ?   A . n 
B 1 854  LEU 854  854  ?   ?   ?   A . n 
B 1 855  THR 855  855  ?   ?   ?   A . n 
B 1 856  VAL 856  856  ?   ?   ?   A . n 
B 1 857  LEU 857  857  ?   ?   ?   A . n 
B 1 858  PRO 858  858  ?   ?   ?   A . n 
B 1 859  PRO 859  859  ?   ?   ?   A . n 
B 1 860  LEU 860  860  ?   ?   ?   A . n 
B 1 861  LEU 861  861  ?   ?   ?   A . n 
B 1 862  THR 862  862  ?   ?   ?   A . n 
B 1 863  ASP 863  863  ?   ?   ?   A . n 
B 1 864  GLU 864  864  ?   ?   ?   A . n 
B 1 865  MET 865  865  ?   ?   ?   A . n 
B 1 866  ILE 866  866  ?   ?   ?   A . n 
B 1 867  ALA 867  867  ?   ?   ?   A . n 
B 1 868  GLN 868  868  ?   ?   ?   A . n 
B 1 869  TYR 869  869  ?   ?   ?   A . n 
B 1 870  THR 870  870  ?   ?   ?   A . n 
B 1 871  SER 871  871  ?   ?   ?   A . n 
B 1 872  ALA 872  872  ?   ?   ?   A . n 
B 1 873  LEU 873  873  ?   ?   ?   A . n 
B 1 874  LEU 874  874  ?   ?   ?   A . n 
B 1 875  ALA 875  875  ?   ?   ?   A . n 
B 1 876  GLY 876  876  ?   ?   ?   A . n 
B 1 877  THR 877  877  ?   ?   ?   A . n 
B 1 878  ILE 878  878  ?   ?   ?   A . n 
B 1 879  THR 879  879  ?   ?   ?   A . n 
B 1 880  SER 880  880  ?   ?   ?   A . n 
B 1 881  GLY 881  881  ?   ?   ?   A . n 
B 1 882  TRP 882  882  ?   ?   ?   A . n 
B 1 883  THR 883  883  ?   ?   ?   A . n 
B 1 884  PHE 884  884  ?   ?   ?   A . n 
B 1 885  GLY 885  885  ?   ?   ?   A . n 
B 1 886  ALA 886  886  ?   ?   ?   A . n 
B 1 887  GLY 887  887  ?   ?   ?   A . n 
B 1 888  PRO 888  888  ?   ?   ?   A . n 
B 1 889  ALA 889  889  ?   ?   ?   A . n 
B 1 890  LEU 890  890  ?   ?   ?   A . n 
B 1 891  GLN 891  891  ?   ?   ?   A . n 
B 1 892  ILE 892  892  ?   ?   ?   A . n 
B 1 893  PRO 893  893  ?   ?   ?   A . n 
B 1 894  PHE 894  894  ?   ?   ?   A . n 
B 1 895  PRO 895  895  ?   ?   ?   A . n 
B 1 896  MET 896  896  ?   ?   ?   A . n 
B 1 897  GLN 897  897  ?   ?   ?   A . n 
B 1 898  MET 898  898  ?   ?   ?   A . n 
B 1 899  ALA 899  899  ?   ?   ?   A . n 
B 1 900  TYR 900  900  ?   ?   ?   A . n 
B 1 901  ARG 901  901  ?   ?   ?   A . n 
B 1 902  PHE 902  902  ?   ?   ?   A . n 
B 1 903  ASN 903  903  ?   ?   ?   A . n 
B 1 904  GLY 904  904  ?   ?   ?   A . n 
B 1 905  ILE 905  905  ?   ?   ?   A . n 
B 1 906  GLY 906  906  ?   ?   ?   A . n 
B 1 907  VAL 907  907  ?   ?   ?   A . n 
B 1 908  THR 908  908  ?   ?   ?   A . n 
B 1 909  GLN 909  909  ?   ?   ?   A . n 
B 1 910  ASN 910  910  ?   ?   ?   A . n 
B 1 911  VAL 911  911  ?   ?   ?   A . n 
B 1 912  LEU 912  912  ?   ?   ?   A . n 
B 1 913  TYR 913  913  ?   ?   ?   A . n 
B 1 914  GLU 914  914  ?   ?   ?   A . n 
B 1 915  ASN 915  915  ?   ?   ?   A . n 
B 1 916  GLN 916  916  ?   ?   ?   A . n 
B 1 917  LYS 917  917  ?   ?   ?   A . n 
B 1 918  LEU 918  918  ?   ?   ?   A . n 
B 1 919  ILE 919  919  ?   ?   ?   A . n 
B 1 920  ALA 920  920  ?   ?   ?   A . n 
B 1 921  ASN 921  921  ?   ?   ?   A . n 
B 1 922  GLN 922  922  ?   ?   ?   A . n 
B 1 923  PHE 923  923  ?   ?   ?   A . n 
B 1 924  ASN 924  924  ?   ?   ?   A . n 
B 1 925  SER 925  925  ?   ?   ?   A . n 
B 1 926  ALA 926  926  ?   ?   ?   A . n 
B 1 927  ILE 927  927  ?   ?   ?   A . n 
B 1 928  GLY 928  928  ?   ?   ?   A . n 
B 1 929  LYS 929  929  ?   ?   ?   A . n 
B 1 930  ILE 930  930  ?   ?   ?   A . n 
B 1 931  GLN 931  931  ?   ?   ?   A . n 
B 1 932  ASP 932  932  ?   ?   ?   A . n 
B 1 933  SER 933  933  ?   ?   ?   A . n 
B 1 934  LEU 934  934  ?   ?   ?   A . n 
B 1 935  PHE 935  935  ?   ?   ?   A . n 
B 1 936  SER 936  936  ?   ?   ?   A . n 
B 1 937  THR 937  937  ?   ?   ?   A . n 
B 1 938  PRO 938  938  ?   ?   ?   A . n 
B 1 939  SER 939  939  ?   ?   ?   A . n 
B 1 940  ALA 940  940  ?   ?   ?   A . n 
B 1 941  LEU 941  941  ?   ?   ?   A . n 
B 1 942  GLY 942  942  ?   ?   ?   A . n 
B 1 943  LYS 943  943  ?   ?   ?   A . n 
B 1 944  LEU 944  944  ?   ?   ?   A . n 
B 1 945  GLN 945  945  ?   ?   ?   A . n 
B 1 946  ASP 946  946  ?   ?   ?   A . n 
B 1 947  VAL 947  947  ?   ?   ?   A . n 
B 1 948  VAL 948  948  ?   ?   ?   A . n 
B 1 949  ASN 949  949  ?   ?   ?   A . n 
B 1 950  HIS 950  950  ?   ?   ?   A . n 
B 1 951  ASN 951  951  ?   ?   ?   A . n 
B 1 952  ALA 952  952  ?   ?   ?   A . n 
B 1 953  GLN 953  953  ?   ?   ?   A . n 
B 1 954  ALA 954  954  ?   ?   ?   A . n 
B 1 955  LEU 955  955  ?   ?   ?   A . n 
B 1 956  ASN 956  956  ?   ?   ?   A . n 
B 1 957  THR 957  957  ?   ?   ?   A . n 
B 1 958  LEU 958  958  ?   ?   ?   A . n 
B 1 959  VAL 959  959  ?   ?   ?   A . n 
B 1 960  LYS 960  960  ?   ?   ?   A . n 
B 1 961  GLN 961  961  ?   ?   ?   A . n 
B 1 962  LEU 962  962  ?   ?   ?   A . n 
B 1 963  SER 963  963  ?   ?   ?   A . n 
B 1 964  SER 964  964  ?   ?   ?   A . n 
B 1 965  LYS 965  965  ?   ?   ?   A . n 
B 1 966  PHE 966  966  ?   ?   ?   A . n 
B 1 967  GLY 967  967  ?   ?   ?   A . n 
B 1 968  ALA 968  968  ?   ?   ?   A . n 
B 1 969  ILE 969  969  ?   ?   ?   A . n 
B 1 970  SER 970  970  ?   ?   ?   A . n 
B 1 971  SER 971  971  ?   ?   ?   A . n 
B 1 972  VAL 972  972  ?   ?   ?   A . n 
B 1 973  LEU 973  973  ?   ?   ?   A . n 
B 1 974  ASN 974  974  ?   ?   ?   A . n 
B 1 975  ASP 975  975  ?   ?   ?   A . n 
B 1 976  ILE 976  976  ?   ?   ?   A . n 
B 1 977  LEU 977  977  ?   ?   ?   A . n 
B 1 978  SER 978  978  ?   ?   ?   A . n 
B 1 979  ARG 979  979  ?   ?   ?   A . n 
B 1 980  LEU 980  980  ?   ?   ?   A . n 
B 1 981  ASP 981  981  ?   ?   ?   A . n 
B 1 982  PRO 982  982  ?   ?   ?   A . n 
B 1 983  PRO 983  983  ?   ?   ?   A . n 
B 1 984  GLU 984  984  ?   ?   ?   A . n 
B 1 985  ALA 985  985  ?   ?   ?   A . n 
B 1 986  GLU 986  986  ?   ?   ?   A . n 
B 1 987  VAL 987  987  ?   ?   ?   A . n 
B 1 988  GLN 988  988  ?   ?   ?   A . n 
B 1 989  ILE 989  989  ?   ?   ?   A . n 
B 1 990  ASP 990  990  ?   ?   ?   A . n 
B 1 991  ARG 991  991  ?   ?   ?   A . n 
B 1 992  LEU 992  992  ?   ?   ?   A . n 
B 1 993  ILE 993  993  ?   ?   ?   A . n 
B 1 994  THR 994  994  ?   ?   ?   A . n 
B 1 995  GLY 995  995  ?   ?   ?   A . n 
B 1 996  ARG 996  996  ?   ?   ?   A . n 
B 1 997  LEU 997  997  ?   ?   ?   A . n 
B 1 998  GLN 998  998  ?   ?   ?   A . n 
B 1 999  SER 999  999  ?   ?   ?   A . n 
B 1 1000 LEU 1000 1000 ?   ?   ?   A . n 
B 1 1001 GLN 1001 1001 ?   ?   ?   A . n 
B 1 1002 THR 1002 1002 ?   ?   ?   A . n 
B 1 1003 TYR 1003 1003 ?   ?   ?   A . n 
B 1 1004 VAL 1004 1004 ?   ?   ?   A . n 
B 1 1005 THR 1005 1005 ?   ?   ?   A . n 
B 1 1006 GLN 1006 1006 ?   ?   ?   A . n 
B 1 1007 GLN 1007 1007 ?   ?   ?   A . n 
B 1 1008 LEU 1008 1008 ?   ?   ?   A . n 
B 1 1009 ILE 1009 1009 ?   ?   ?   A . n 
B 1 1010 ARG 1010 1010 ?   ?   ?   A . n 
B 1 1011 ALA 1011 1011 ?   ?   ?   A . n 
B 1 1012 ALA 1012 1012 ?   ?   ?   A . n 
B 1 1013 GLU 1013 1013 ?   ?   ?   A . n 
B 1 1014 ILE 1014 1014 ?   ?   ?   A . n 
B 1 1015 ARG 1015 1015 ?   ?   ?   A . n 
B 1 1016 ALA 1016 1016 ?   ?   ?   A . n 
B 1 1017 SER 1017 1017 ?   ?   ?   A . n 
B 1 1018 ALA 1018 1018 ?   ?   ?   A . n 
B 1 1019 ASN 1019 1019 ?   ?   ?   A . n 
B 1 1020 LEU 1020 1020 ?   ?   ?   A . n 
B 1 1021 ALA 1021 1021 ?   ?   ?   A . n 
B 1 1022 ALA 1022 1022 ?   ?   ?   A . n 
B 1 1023 THR 1023 1023 ?   ?   ?   A . n 
B 1 1024 LYS 1024 1024 ?   ?   ?   A . n 
B 1 1025 MET 1025 1025 ?   ?   ?   A . n 
B 1 1026 SER 1026 1026 ?   ?   ?   A . n 
B 1 1027 GLU 1027 1027 ?   ?   ?   A . n 
B 1 1028 CYS 1028 1028 ?   ?   ?   A . n 
B 1 1029 VAL 1029 1029 ?   ?   ?   A . n 
B 1 1030 LEU 1030 1030 ?   ?   ?   A . n 
B 1 1031 GLY 1031 1031 ?   ?   ?   A . n 
B 1 1032 GLN 1032 1032 ?   ?   ?   A . n 
B 1 1033 SER 1033 1033 ?   ?   ?   A . n 
B 1 1034 LYS 1034 1034 ?   ?   ?   A . n 
B 1 1035 ARG 1035 1035 ?   ?   ?   A . n 
B 1 1036 VAL 1036 1036 ?   ?   ?   A . n 
B 1 1037 ASP 1037 1037 ?   ?   ?   A . n 
B 1 1038 PHE 1038 1038 ?   ?   ?   A . n 
B 1 1039 CYS 1039 1039 ?   ?   ?   A . n 
B 1 1040 GLY 1040 1040 ?   ?   ?   A . n 
B 1 1041 LYS 1041 1041 ?   ?   ?   A . n 
B 1 1042 GLY 1042 1042 ?   ?   ?   A . n 
B 1 1043 TYR 1043 1043 ?   ?   ?   A . n 
B 1 1044 HIS 1044 1044 ?   ?   ?   A . n 
B 1 1045 LEU 1045 1045 ?   ?   ?   A . n 
B 1 1046 MET 1046 1046 ?   ?   ?   A . n 
B 1 1047 SER 1047 1047 ?   ?   ?   A . n 
B 1 1048 PHE 1048 1048 ?   ?   ?   A . n 
B 1 1049 PRO 1049 1049 ?   ?   ?   A . n 
B 1 1050 GLN 1050 1050 ?   ?   ?   A . n 
B 1 1051 SER 1051 1051 ?   ?   ?   A . n 
B 1 1052 ALA 1052 1052 ?   ?   ?   A . n 
B 1 1053 PRO 1053 1053 ?   ?   ?   A . n 
B 1 1054 HIS 1054 1054 ?   ?   ?   A . n 
B 1 1055 GLY 1055 1055 ?   ?   ?   A . n 
B 1 1056 VAL 1056 1056 ?   ?   ?   A . n 
B 1 1057 VAL 1057 1057 ?   ?   ?   A . n 
B 1 1058 PHE 1058 1058 ?   ?   ?   A . n 
B 1 1059 LEU 1059 1059 ?   ?   ?   A . n 
B 1 1060 HIS 1060 1060 ?   ?   ?   A . n 
B 1 1061 VAL 1061 1061 ?   ?   ?   A . n 
B 1 1062 THR 1062 1062 ?   ?   ?   A . n 
B 1 1063 TYR 1063 1063 ?   ?   ?   A . n 
B 1 1064 VAL 1064 1064 ?   ?   ?   A . n 
B 1 1065 PRO 1065 1065 ?   ?   ?   A . n 
B 1 1066 ALA 1066 1066 ?   ?   ?   A . n 
B 1 1067 GLN 1067 1067 ?   ?   ?   A . n 
B 1 1068 GLU 1068 1068 ?   ?   ?   A . n 
B 1 1069 LYS 1069 1069 ?   ?   ?   A . n 
B 1 1070 ASN 1070 1070 ?   ?   ?   A . n 
B 1 1071 PHE 1071 1071 ?   ?   ?   A . n 
B 1 1072 THR 1072 1072 ?   ?   ?   A . n 
B 1 1073 THR 1073 1073 ?   ?   ?   A . n 
B 1 1074 ALA 1074 1074 ?   ?   ?   A . n 
B 1 1075 PRO 1075 1075 ?   ?   ?   A . n 
B 1 1076 ALA 1076 1076 ?   ?   ?   A . n 
B 1 1077 ILE 1077 1077 ?   ?   ?   A . n 
B 1 1078 CYS 1078 1078 ?   ?   ?   A . n 
B 1 1079 HIS 1079 1079 ?   ?   ?   A . n 
B 1 1080 ASP 1080 1080 ?   ?   ?   A . n 
B 1 1081 GLY 1081 1081 ?   ?   ?   A . n 
B 1 1082 LYS 1082 1082 ?   ?   ?   A . n 
B 1 1083 ALA 1083 1083 ?   ?   ?   A . n 
B 1 1084 HIS 1084 1084 ?   ?   ?   A . n 
B 1 1085 PHE 1085 1085 ?   ?   ?   A . n 
B 1 1086 PRO 1086 1086 ?   ?   ?   A . n 
B 1 1087 ARG 1087 1087 ?   ?   ?   A . n 
B 1 1088 GLU 1088 1088 ?   ?   ?   A . n 
B 1 1089 GLY 1089 1089 ?   ?   ?   A . n 
B 1 1090 VAL 1090 1090 ?   ?   ?   A . n 
B 1 1091 PHE 1091 1091 ?   ?   ?   A . n 
B 1 1092 VAL 1092 1092 ?   ?   ?   A . n 
B 1 1093 SER 1093 1093 ?   ?   ?   A . n 
B 1 1094 ASN 1094 1094 ?   ?   ?   A . n 
B 1 1095 GLY 1095 1095 ?   ?   ?   A . n 
B 1 1096 THR 1096 1096 ?   ?   ?   A . n 
B 1 1097 HIS 1097 1097 ?   ?   ?   A . n 
B 1 1098 TRP 1098 1098 ?   ?   ?   A . n 
B 1 1099 PHE 1099 1099 ?   ?   ?   A . n 
B 1 1100 VAL 1100 1100 ?   ?   ?   A . n 
B 1 1101 THR 1101 1101 ?   ?   ?   A . n 
B 1 1102 GLN 1102 1102 ?   ?   ?   A . n 
B 1 1103 ARG 1103 1103 ?   ?   ?   A . n 
B 1 1104 ASN 1104 1104 ?   ?   ?   A . n 
B 1 1105 PHE 1105 1105 ?   ?   ?   A . n 
B 1 1106 TYR 1106 1106 ?   ?   ?   A . n 
B 1 1107 GLU 1107 1107 ?   ?   ?   A . n 
B 1 1108 PRO 1108 1108 ?   ?   ?   A . n 
B 1 1109 GLN 1109 1109 ?   ?   ?   A . n 
B 1 1110 ILE 1110 1110 ?   ?   ?   A . n 
B 1 1111 ILE 1111 1111 ?   ?   ?   A . n 
B 1 1112 THR 1112 1112 ?   ?   ?   A . n 
B 1 1113 THR 1113 1113 ?   ?   ?   A . n 
B 1 1114 ASP 1114 1114 ?   ?   ?   A . n 
B 1 1115 ASN 1115 1115 ?   ?   ?   A . n 
B 1 1116 THR 1116 1116 ?   ?   ?   A . n 
B 1 1117 PHE 1117 1117 ?   ?   ?   A . n 
B 1 1118 VAL 1118 1118 ?   ?   ?   A . n 
B 1 1119 SER 1119 1119 ?   ?   ?   A . n 
B 1 1120 GLY 1120 1120 ?   ?   ?   A . n 
B 1 1121 ASN 1121 1121 ?   ?   ?   A . n 
B 1 1122 CYS 1122 1122 ?   ?   ?   A . n 
B 1 1123 ASP 1123 1123 ?   ?   ?   A . n 
B 1 1124 VAL 1124 1124 ?   ?   ?   A . n 
B 1 1125 VAL 1125 1125 ?   ?   ?   A . n 
B 1 1126 ILE 1126 1126 ?   ?   ?   A . n 
B 1 1127 GLY 1127 1127 ?   ?   ?   A . n 
B 1 1128 ILE 1128 1128 ?   ?   ?   A . n 
B 1 1129 VAL 1129 1129 ?   ?   ?   A . n 
B 1 1130 ASN 1130 1130 ?   ?   ?   A . n 
B 1 1131 ASN 1131 1131 ?   ?   ?   A . n 
B 1 1132 THR 1132 1132 ?   ?   ?   A . n 
B 1 1133 VAL 1133 1133 ?   ?   ?   A . n 
B 1 1134 TYR 1134 1134 ?   ?   ?   A . n 
B 1 1135 ASP 1135 1135 ?   ?   ?   A . n 
B 1 1136 PRO 1136 1136 ?   ?   ?   A . n 
B 1 1137 LEU 1137 1137 ?   ?   ?   A . n 
B 1 1138 GLN 1138 1138 ?   ?   ?   A . n 
B 1 1139 LEU 1139 1139 ?   ?   ?   A . n 
B 1 1140 GLU 1140 1140 ?   ?   ?   A . n 
B 1 1141 LEU 1141 1141 ?   ?   ?   A . n 
B 1 1142 ASP 1142 1142 ?   ?   ?   A . n 
B 1 1143 SER 1143 1143 ?   ?   ?   A . n 
B 1 1144 PHE 1144 1144 ?   ?   ?   A . n 
B 1 1145 LYS 1145 1145 ?   ?   ?   A . n 
B 1 1146 GLU 1146 1146 ?   ?   ?   A . n 
B 1 1147 GLU 1147 1147 ?   ?   ?   A . n 
B 1 1148 LEU 1148 1148 ?   ?   ?   A . n 
B 1 1149 ASP 1149 1149 ?   ?   ?   A . n 
B 1 1150 LYS 1150 1150 ?   ?   ?   A . n 
B 1 1151 TYR 1151 1151 ?   ?   ?   A . n 
B 1 1152 PHE 1152 1152 ?   ?   ?   A . n 
B 1 1153 LYS 1153 1153 ?   ?   ?   A . n 
B 1 1154 ASN 1154 1154 ?   ?   ?   A . n 
B 1 1155 HIS 1155 1155 ?   ?   ?   A . n 
B 1 1156 THR 1156 1156 ?   ?   ?   A . n 
B 1 1157 SER 1157 1157 ?   ?   ?   A . n 
B 1 1158 PRO 1158 1158 ?   ?   ?   A . n 
B 1 1159 ASP 1159 1159 ?   ?   ?   A . n 
B 1 1160 VAL 1160 1160 ?   ?   ?   A . n 
B 1 1161 ASP 1161 1161 ?   ?   ?   A . n 
B 1 1162 LEU 1162 1162 ?   ?   ?   A . n 
B 1 1163 GLY 1163 1163 ?   ?   ?   A . n 
B 1 1164 ASP 1164 1164 ?   ?   ?   A . n 
B 1 1165 ILE 1165 1165 ?   ?   ?   A . n 
B 1 1166 SER 1166 1166 ?   ?   ?   A . n 
B 1 1167 GLY 1167 1167 ?   ?   ?   A . n 
B 1 1168 ILE 1168 1168 ?   ?   ?   A . n 
B 1 1169 ASN 1169 1169 ?   ?   ?   A . n 
B 1 1170 ALA 1170 1170 ?   ?   ?   A . n 
B 1 1171 SER 1171 1171 ?   ?   ?   A . n 
B 1 1172 VAL 1172 1172 ?   ?   ?   A . n 
B 1 1173 VAL 1173 1173 ?   ?   ?   A . n 
B 1 1174 ASN 1174 1174 ?   ?   ?   A . n 
B 1 1175 ILE 1175 1175 ?   ?   ?   A . n 
B 1 1176 GLN 1176 1176 ?   ?   ?   A . n 
B 1 1177 LYS 1177 1177 ?   ?   ?   A . n 
B 1 1178 GLU 1178 1178 ?   ?   ?   A . n 
B 1 1179 ILE 1179 1179 ?   ?   ?   A . n 
B 1 1180 ASP 1180 1180 ?   ?   ?   A . n 
B 1 1181 ARG 1181 1181 ?   ?   ?   A . n 
B 1 1182 LEU 1182 1182 ?   ?   ?   A . n 
B 1 1183 ASN 1183 1183 ?   ?   ?   A . n 
B 1 1184 GLU 1184 1184 ?   ?   ?   A . n 
B 1 1185 VAL 1185 1185 ?   ?   ?   A . n 
B 1 1186 ALA 1186 1186 ?   ?   ?   A . n 
B 1 1187 LYS 1187 1187 ?   ?   ?   A . n 
B 1 1188 ASN 1188 1188 ?   ?   ?   A . n 
B 1 1189 LEU 1189 1189 ?   ?   ?   A . n 
B 1 1190 ASN 1190 1190 ?   ?   ?   A . n 
B 1 1191 GLU 1191 1191 ?   ?   ?   A . n 
B 1 1192 SER 1192 1192 ?   ?   ?   A . n 
B 1 1193 LEU 1193 1193 ?   ?   ?   A . n 
B 1 1194 ILE 1194 1194 ?   ?   ?   A . n 
B 1 1195 ASP 1195 1195 ?   ?   ?   A . n 
B 1 1196 LEU 1196 1196 ?   ?   ?   A . n 
B 1 1197 GLN 1197 1197 ?   ?   ?   A . n 
B 1 1198 GLU 1198 1198 ?   ?   ?   A . n 
B 1 1199 LEU 1199 1199 ?   ?   ?   A . n 
B 1 1200 GLY 1200 1200 ?   ?   ?   A . n 
B 1 1201 LYS 1201 1201 ?   ?   ?   A . n 
B 1 1202 TYR 1202 1202 ?   ?   ?   A . n 
B 1 1203 GLU 1203 1203 ?   ?   ?   A . n 
B 1 1204 GLN 1204 1204 ?   ?   ?   A . n 
B 1 1205 TYR 1205 1205 ?   ?   ?   A . n 
B 1 1206 ILE 1206 1206 ?   ?   ?   A . n 
B 1 1207 LYS 1207 1207 ?   ?   ?   A . n 
B 1 1208 GLY 1208 1208 ?   ?   ?   A . n 
B 1 1209 SER 1209 1209 ?   ?   ?   A . n 
B 1 1210 GLY 1210 1210 ?   ?   ?   A . n 
B 1 1211 TYR 1211 1211 ?   ?   ?   A . n 
B 1 1212 ILE 1212 1212 ?   ?   ?   A . n 
B 1 1213 PRO 1213 1213 ?   ?   ?   A . n 
B 1 1214 GLU 1214 1214 ?   ?   ?   A . n 
B 1 1215 ALA 1215 1215 ?   ?   ?   A . n 
B 1 1216 PRO 1216 1216 ?   ?   ?   A . n 
B 1 1217 ARG 1217 1217 ?   ?   ?   A . n 
B 1 1218 ASP 1218 1218 ?   ?   ?   A . n 
B 1 1219 GLY 1219 1219 ?   ?   ?   A . n 
B 1 1220 GLN 1220 1220 ?   ?   ?   A . n 
B 1 1221 ALA 1221 1221 ?   ?   ?   A . n 
B 1 1222 TYR 1222 1222 ?   ?   ?   A . n 
B 1 1223 VAL 1223 1223 ?   ?   ?   A . n 
B 1 1224 ARG 1224 1224 ?   ?   ?   A . n 
B 1 1225 LYS 1225 1225 ?   ?   ?   A . n 
B 1 1226 ASP 1226 1226 ?   ?   ?   A . n 
B 1 1227 GLY 1227 1227 ?   ?   ?   A . n 
B 1 1228 GLU 1228 1228 ?   ?   ?   A . n 
B 1 1229 TRP 1229 1229 ?   ?   ?   A . n 
B 1 1230 VAL 1230 1230 ?   ?   ?   A . n 
B 1 1231 LEU 1231 1231 ?   ?   ?   A . n 
B 1 1232 LEU 1232 1232 ?   ?   ?   A . n 
B 1 1233 SER 1233 1233 ?   ?   ?   A . n 
B 1 1234 THR 1234 1234 ?   ?   ?   A . n 
B 1 1235 PHE 1235 1235 ?   ?   ?   A . n 
B 1 1236 LEU 1236 1236 ?   ?   ?   A . n 
B 1 1237 GLY 1237 1237 ?   ?   ?   A . n 
B 1 1238 HIS 1238 1238 ?   ?   ?   A . n 
B 1 1239 HIS 1239 1239 ?   ?   ?   A . n 
B 1 1240 HIS 1240 1240 ?   ?   ?   A . n 
B 1 1241 HIS 1241 1241 ?   ?   ?   A . n 
B 1 1242 HIS 1242 1242 ?   ?   ?   A . n 
B 1 1243 HIS 1243 1243 ?   ?   ?   A . n 
C 2 1    GLN 1    1    1   GLN GLN D . n 
C 2 2    VAL 2    2    2   VAL VAL D . n 
C 2 3    GLN 3    3    3   GLN GLN D . n 
C 2 4    LEU 4    4    4   LEU LEU D . n 
C 2 5    GLN 5    5    5   GLN GLN D . n 
C 2 6    GLU 6    6    6   GLU GLU D . n 
C 2 7    SER 7    7    7   SER SER D . n 
C 2 8    GLY 8    8    8   GLY GLY D . n 
C 2 9    GLY 9    9    9   GLY GLY D . n 
C 2 10   GLY 10   10   10  GLY GLY D . n 
C 2 11   LEU 11   11   11  LEU LEU D . n 
C 2 12   VAL 12   12   12  VAL VAL D . n 
C 2 13   GLN 13   13   13  GLN GLN D . n 
C 2 14   PRO 14   14   14  PRO PRO D . n 
C 2 15   GLY 15   15   15  GLY GLY D . n 
C 2 16   GLY 16   16   16  GLY GLY D . n 
C 2 17   SER 17   17   17  SER SER D . n 
C 2 18   LEU 18   18   18  LEU LEU D . n 
C 2 19   ARG 19   19   19  ARG ARG D . n 
C 2 20   LEU 20   20   20  LEU LEU D . n 
C 2 21   SER 21   21   21  SER SER D . n 
C 2 22   CYS 22   22   22  CYS CYS D . n 
C 2 23   THR 23   23   23  THR THR D . n 
C 2 24   ALA 24   24   24  ALA ALA D . n 
C 2 25   SER 25   25   25  SER SER D . n 
C 2 26   GLY 26   26   26  GLY GLY D . n 
C 2 27   ILE 27   27   27  ILE ILE D . n 
C 2 28   ALA 28   28   28  ALA ALA D . n 
C 2 29   LEU 29   29   29  LEU LEU D . n 
C 2 30   HIS 30   30   30  HIS HIS D . n 
C 2 31   THR 31   31   31  THR THR D . n 
C 2 32   HIS 32   32   32  HIS HIS D . n 
C 2 33   ALA 33   33   33  ALA ALA D . n 
C 2 34   THR 34   34   34  THR THR D . n 
C 2 35   GLY 35   35   35  GLY GLY D . n 
C 2 36   TRP 36   36   36  TRP TRP D . n 
C 2 37   PHE 37   37   37  PHE PHE D . n 
C 2 38   ARG 38   38   38  ARG ARG D . n 
C 2 39   GLN 39   39   39  GLN GLN D . n 
C 2 40   ALA 40   40   40  ALA ALA D . n 
C 2 41   PRO 41   41   41  PRO PRO D . n 
C 2 42   GLY 42   42   42  GLY GLY D . n 
C 2 43   LYS 43   43   43  LYS LYS D . n 
C 2 44   GLU 44   44   44  GLU GLU D . n 
C 2 45   ARG 45   45   45  ARG ARG D . n 
C 2 46   GLU 46   46   46  GLU GLU D . n 
C 2 47   GLY 47   47   47  GLY GLY D . n 
C 2 48   VAL 48   48   48  VAL VAL D . n 
C 2 49   SER 49   49   49  SER SER D . n 
C 2 50   CYS 50   50   50  CYS CYS D . n 
C 2 51   ILE 51   51   51  ILE ILE D . n 
C 2 52   SER 52   52   52  SER SER D . n 
C 2 53   SER 53   53   53  SER SER D . n 
C 2 54   GLY 54   54   54  GLY GLY D . n 
C 2 55   ASP 55   55   55  ASP ASP D . n 
C 2 56   GLY 56   56   56  GLY GLY D . n 
C 2 57   THR 57   57   57  THR THR D . n 
C 2 58   THR 58   58   58  THR THR D . n 
C 2 59   TYR 59   59   59  TYR TYR D . n 
C 2 60   TYR 60   60   60  TYR TYR D . n 
C 2 61   GLU 61   61   61  GLU GLU D . n 
C 2 62   ASP 62   62   62  ASP ASP D . n 
C 2 63   SER 63   63   63  SER SER D . n 
C 2 64   VAL 64   64   64  VAL VAL D . n 
C 2 65   GLU 65   65   65  GLU GLU D . n 
C 2 66   GLY 66   66   66  GLY GLY D . n 
C 2 67   ARG 67   67   67  ARG ARG D . n 
C 2 68   PHE 68   68   68  PHE PHE D . n 
C 2 69   THR 69   69   69  THR THR D . n 
C 2 70   ILE 70   70   70  ILE ILE D . n 
C 2 71   SER 71   71   71  SER SER D . n 
C 2 72   ARG 72   72   72  ARG ARG D . n 
C 2 73   ASP 73   73   73  ASP ASP D . n 
C 2 74   ASN 74   74   74  ASN ASN D . n 
C 2 75   ALA 75   75   75  ALA ALA D . n 
C 2 76   LYS 76   76   76  LYS LYS D . n 
C 2 77   ASN 77   77   77  ASN ASN D . n 
C 2 78   THR 78   78   78  THR THR D . n 
C 2 79   VAL 79   79   79  VAL VAL D . n 
C 2 80   TYR 80   80   80  TYR TYR D . n 
C 2 81   LEU 81   81   81  LEU LEU D . n 
C 2 82   GLN 82   82   82  GLN GLN D . n 
C 2 83   MET 83   83   83  MET MET D . n 
C 2 84   ASN 84   84   84  ASN ASN D . n 
C 2 85   SER 85   85   85  SER SER D . n 
C 2 86   LEU 86   86   86  LEU LEU D . n 
C 2 87   LYS 87   87   87  LYS LYS D . n 
C 2 88   LEU 88   88   88  LEU LEU D . n 
C 2 89   GLU 89   89   89  GLU GLU D . n 
C 2 90   ASP 90   90   90  ASP ASP D . n 
C 2 91   THR 91   91   91  THR THR D . n 
C 2 92   ALA 92   92   92  ALA ALA D . n 
C 2 93   VAL 93   93   93  VAL VAL D . n 
C 2 94   TYR 94   94   94  TYR TYR D . n 
C 2 95   TYR 95   95   95  TYR TYR D . n 
C 2 96   CYS 96   96   96  CYS CYS D . n 
C 2 97   ALA 97   97   97  ALA ALA D . n 
C 2 98   ALA 98   98   98  ALA ALA D . n 
C 2 99   ASP 99   99   99  ASP ASP D . n 
C 2 100  PRO 100  100  100 PRO PRO D . n 
C 2 101  GLY 101  101  101 GLY GLY D . n 
C 2 102  ALA 102  102  102 ALA ALA D . n 
C 2 103  VAL 103  103  103 VAL VAL D . n 
C 2 104  CYS 104  104  104 CYS CYS D . n 
C 2 105  HIS 105  105  105 HIS HIS D . n 
C 2 106  SER 106  106  106 SER SER D . n 
C 2 107  GLY 107  107  107 GLY GLY D . n 
C 2 108  SER 108  108  108 SER SER D . n 
C 2 109  TYR 109  109  109 TYR TYR D . n 
C 2 110  TYR 110  110  110 TYR TYR D . n 
C 2 111  TYR 111  111  111 TYR TYR D . n 
C 2 112  THR 112  112  112 THR THR D . n 
C 2 113  ASP 113  113  113 ASP ASP D . n 
C 2 114  ASP 114  114  114 ASP ASP D . n 
C 2 115  ASP 115  115  115 ASP ASP D . n 
C 2 116  PHE 116  116  116 PHE PHE D . n 
C 2 117  TYR 117  117  117 TYR TYR D . n 
C 2 118  TYR 118  118  118 TYR TYR D . n 
C 2 119  ARG 119  119  119 ARG ARG D . n 
C 2 120  GLY 120  120  120 GLY GLY D . n 
C 2 121  GLN 121  121  121 GLN GLN D . n 
C 2 122  GLY 122  122  122 GLY GLY D . n 
C 2 123  THR 123  123  123 THR THR D . n 
C 2 124  GLN 124  124  124 GLN GLN D . n 
C 2 125  VAL 125  125  125 VAL VAL D . n 
C 2 126  THR 126  126  126 THR THR D . n 
C 2 127  VAL 127  127  127 VAL VAL D . n 
C 2 128  SER 128  128  128 SER SER D . n 
C 2 129  SER 129  129  129 SER SER D . n 
C 2 130  GLY 130  130  ?   ?   ?   D . n 
C 2 131  GLY 131  131  ?   ?   ?   D . n 
C 2 132  GLN 132  132  ?   ?   ?   D . n 
C 2 133  HIS 133  133  ?   ?   ?   D . n 
C 2 134  HIS 134  134  ?   ?   ?   D . n 
C 2 135  HIS 135  135  ?   ?   ?   D . n 
C 2 136  HIS 136  136  ?   ?   ?   D . n 
C 2 137  HIS 137  137  ?   ?   ?   D . n 
C 2 138  HIS 138  138  ?   ?   ?   D . n 
C 2 139  GLY 139  139  ?   ?   ?   D . n 
C 2 140  ALA 140  140  ?   ?   ?   D . n 
C 2 141  TYR 141  141  ?   ?   ?   D . n 
C 2 142  PRO 142  142  ?   ?   ?   D . n 
C 2 143  TYR 143  143  ?   ?   ?   D . n 
C 2 144  ASP 144  144  ?   ?   ?   D . n 
C 2 145  VAL 145  145  ?   ?   ?   D . n 
C 2 146  PRO 146  146  ?   ?   ?   D . n 
C 2 147  ASP 147  147  ?   ?   ?   D . n 
C 2 148  TYR 148  148  ?   ?   ?   D . n 
C 2 149  ALA 149  149  ?   ?   ?   D . n 
C 2 150  SER 150  150  ?   ?   ?   D . n 
D 2 1    GLN 1    1    1   GLN GLN E . n 
D 2 2    VAL 2    2    2   VAL VAL E . n 
D 2 3    GLN 3    3    3   GLN GLN E . n 
D 2 4    LEU 4    4    4   LEU LEU E . n 
D 2 5    GLN 5    5    5   GLN GLN E . n 
D 2 6    GLU 6    6    6   GLU GLU E . n 
D 2 7    SER 7    7    7   SER SER E . n 
D 2 8    GLY 8    8    8   GLY GLY E . n 
D 2 9    GLY 9    9    9   GLY GLY E . n 
D 2 10   GLY 10   10   10  GLY GLY E . n 
D 2 11   LEU 11   11   11  LEU LEU E . n 
D 2 12   VAL 12   12   12  VAL VAL E . n 
D 2 13   GLN 13   13   13  GLN GLN E . n 
D 2 14   PRO 14   14   14  PRO PRO E . n 
D 2 15   GLY 15   15   15  GLY GLY E . n 
D 2 16   GLY 16   16   16  GLY GLY E . n 
D 2 17   SER 17   17   17  SER SER E . n 
D 2 18   LEU 18   18   18  LEU LEU E . n 
D 2 19   ARG 19   19   19  ARG ARG E . n 
D 2 20   LEU 20   20   20  LEU LEU E . n 
D 2 21   SER 21   21   21  SER SER E . n 
D 2 22   CYS 22   22   22  CYS CYS E . n 
D 2 23   THR 23   23   23  THR THR E . n 
D 2 24   ALA 24   24   24  ALA ALA E . n 
D 2 25   SER 25   25   25  SER SER E . n 
D 2 26   GLY 26   26   26  GLY GLY E . n 
D 2 27   ILE 27   27   27  ILE ILE E . n 
D 2 28   ALA 28   28   28  ALA ALA E . n 
D 2 29   LEU 29   29   29  LEU LEU E . n 
D 2 30   HIS 30   30   30  HIS HIS E . n 
D 2 31   THR 31   31   31  THR THR E . n 
D 2 32   HIS 32   32   32  HIS HIS E . n 
D 2 33   ALA 33   33   33  ALA ALA E . n 
D 2 34   THR 34   34   34  THR THR E . n 
D 2 35   GLY 35   35   35  GLY GLY E . n 
D 2 36   TRP 36   36   36  TRP TRP E . n 
D 2 37   PHE 37   37   37  PHE PHE E . n 
D 2 38   ARG 38   38   38  ARG ARG E . n 
D 2 39   GLN 39   39   39  GLN GLN E . n 
D 2 40   ALA 40   40   40  ALA ALA E . n 
D 2 41   PRO 41   41   41  PRO PRO E . n 
D 2 42   GLY 42   42   42  GLY GLY E . n 
D 2 43   LYS 43   43   43  LYS LYS E . n 
D 2 44   GLU 44   44   44  GLU GLU E . n 
D 2 45   ARG 45   45   45  ARG ARG E . n 
D 2 46   GLU 46   46   46  GLU GLU E . n 
D 2 47   GLY 47   47   47  GLY GLY E . n 
D 2 48   VAL 48   48   48  VAL VAL E . n 
D 2 49   SER 49   49   49  SER SER E . n 
D 2 50   CYS 50   50   50  CYS CYS E . n 
D 2 51   ILE 51   51   51  ILE ILE E . n 
D 2 52   SER 52   52   52  SER SER E . n 
D 2 53   SER 53   53   53  SER SER E . n 
D 2 54   GLY 54   54   54  GLY GLY E . n 
D 2 55   ASP 55   55   55  ASP ASP E . n 
D 2 56   GLY 56   56   56  GLY GLY E . n 
D 2 57   THR 57   57   57  THR THR E . n 
D 2 58   THR 58   58   58  THR THR E . n 
D 2 59   TYR 59   59   59  TYR TYR E . n 
D 2 60   TYR 60   60   60  TYR TYR E . n 
D 2 61   GLU 61   61   61  GLU GLU E . n 
D 2 62   ASP 62   62   62  ASP ASP E . n 
D 2 63   SER 63   63   63  SER SER E . n 
D 2 64   VAL 64   64   64  VAL VAL E . n 
D 2 65   GLU 65   65   65  GLU GLU E . n 
D 2 66   GLY 66   66   66  GLY GLY E . n 
D 2 67   ARG 67   67   67  ARG ARG E . n 
D 2 68   PHE 68   68   68  PHE PHE E . n 
D 2 69   THR 69   69   69  THR THR E . n 
D 2 70   ILE 70   70   70  ILE ILE E . n 
D 2 71   SER 71   71   71  SER SER E . n 
D 2 72   ARG 72   72   72  ARG ARG E . n 
D 2 73   ASP 73   73   73  ASP ASP E . n 
D 2 74   ASN 74   74   74  ASN ASN E . n 
D 2 75   ALA 75   75   75  ALA ALA E . n 
D 2 76   LYS 76   76   76  LYS LYS E . n 
D 2 77   ASN 77   77   77  ASN ASN E . n 
D 2 78   THR 78   78   78  THR THR E . n 
D 2 79   VAL 79   79   79  VAL VAL E . n 
D 2 80   TYR 80   80   80  TYR TYR E . n 
D 2 81   LEU 81   81   81  LEU LEU E . n 
D 2 82   GLN 82   82   82  GLN GLN E . n 
D 2 83   MET 83   83   83  MET MET E . n 
D 2 84   ASN 84   84   84  ASN ASN E . n 
D 2 85   SER 85   85   85  SER SER E . n 
D 2 86   LEU 86   86   86  LEU LEU E . n 
D 2 87   LYS 87   87   87  LYS LYS E . n 
D 2 88   LEU 88   88   88  LEU LEU E . n 
D 2 89   GLU 89   89   89  GLU GLU E . n 
D 2 90   ASP 90   90   90  ASP ASP E . n 
D 2 91   THR 91   91   91  THR THR E . n 
D 2 92   ALA 92   92   92  ALA ALA E . n 
D 2 93   VAL 93   93   93  VAL VAL E . n 
D 2 94   TYR 94   94   94  TYR TYR E . n 
D 2 95   TYR 95   95   95  TYR TYR E . n 
D 2 96   CYS 96   96   96  CYS CYS E . n 
D 2 97   ALA 97   97   97  ALA ALA E . n 
D 2 98   ALA 98   98   98  ALA ALA E . n 
D 2 99   ASP 99   99   99  ASP ASP E . n 
D 2 100  PRO 100  100  100 PRO PRO E . n 
D 2 101  GLY 101  101  101 GLY GLY E . n 
D 2 102  ALA 102  102  102 ALA ALA E . n 
D 2 103  VAL 103  103  103 VAL VAL E . n 
D 2 104  CYS 104  104  104 CYS CYS E . n 
D 2 105  HIS 105  105  105 HIS HIS E . n 
D 2 106  SER 106  106  106 SER SER E . n 
D 2 107  GLY 107  107  107 GLY GLY E . n 
D 2 108  SER 108  108  108 SER SER E . n 
D 2 109  TYR 109  109  109 TYR TYR E . n 
D 2 110  TYR 110  110  110 TYR TYR E . n 
D 2 111  TYR 111  111  111 TYR TYR E . n 
D 2 112  THR 112  112  112 THR THR E . n 
D 2 113  ASP 113  113  113 ASP ASP E . n 
D 2 114  ASP 114  114  114 ASP ASP E . n 
D 2 115  ASP 115  115  115 ASP ASP E . n 
D 2 116  PHE 116  116  116 PHE PHE E . n 
D 2 117  TYR 117  117  117 TYR TYR E . n 
D 2 118  TYR 118  118  118 TYR TYR E . n 
D 2 119  ARG 119  119  119 ARG ARG E . n 
D 2 120  GLY 120  120  120 GLY GLY E . n 
D 2 121  GLN 121  121  121 GLN GLN E . n 
D 2 122  GLY 122  122  122 GLY GLY E . n 
D 2 123  THR 123  123  123 THR THR E . n 
D 2 124  GLN 124  124  124 GLN GLN E . n 
D 2 125  VAL 125  125  125 VAL VAL E . n 
D 2 126  THR 126  126  126 THR THR E . n 
D 2 127  VAL 127  127  127 VAL VAL E . n 
D 2 128  SER 128  128  128 SER SER E . n 
D 2 129  SER 129  129  129 SER SER E . n 
D 2 130  GLY 130  130  ?   ?   ?   E . n 
D 2 131  GLY 131  131  ?   ?   ?   E . n 
D 2 132  GLN 132  132  ?   ?   ?   E . n 
D 2 133  HIS 133  133  ?   ?   ?   E . n 
D 2 134  HIS 134  134  ?   ?   ?   E . n 
D 2 135  HIS 135  135  ?   ?   ?   E . n 
D 2 136  HIS 136  136  ?   ?   ?   E . n 
D 2 137  HIS 137  137  ?   ?   ?   E . n 
D 2 138  HIS 138  138  ?   ?   ?   E . n 
D 2 139  GLY 139  139  ?   ?   ?   E . n 
D 2 140  ALA 140  140  ?   ?   ?   E . n 
D 2 141  TYR 141  141  ?   ?   ?   E . n 
D 2 142  PRO 142  142  ?   ?   ?   E . n 
D 2 143  TYR 143  143  ?   ?   ?   E . n 
D 2 144  ASP 144  144  ?   ?   ?   E . n 
D 2 145  VAL 145  145  ?   ?   ?   E . n 
D 2 146  PRO 146  146  ?   ?   ?   E . n 
D 2 147  ASP 147  147  ?   ?   ?   E . n 
D 2 148  TYR 148  148  ?   ?   ?   E . n 
D 2 149  ALA 149  149  ?   ?   ?   E . n 
D 2 150  SER 150  150  ?   ?   ?   E . n 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CO9 
_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                         9CO9 
_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                   9CO9 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9CO9 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.006  ? 5348 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 1.021  ? 7267 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 13.001 ? 1895 ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.059  ? 753  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.008  ? 952  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9CO9 
_struct.title                        'Local refinement of JN.1 spike/Nanosota-9 complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CO9 
_struct_keywords.text            'spike, nanobody, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SPIKE_SARS2 P0DTC2 ? 1 
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFD
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRV
QPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSF
VIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPC
NGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFL
PFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGS
NVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTI
SVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGF
NFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAG
TITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALN
TLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRV
DFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNT
FVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDL
QELGKYEQYIKWPWYI
;
1 
2 PDB 9CO9        9CO9   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CO9 B 1 ? 1212 ? P0DTC2 1 ? 1216 ? 1 1212 
2 1 9CO9 A 1 ? 1212 ? P0DTC2 1 ? 1216 ? 1 1212 
3 2 9CO9 D 1 ? 150  ? 9CO9   1 ? 150  ? 1 150  
4 2 9CO9 E 1 ? 150  ? 9CO9   1 ? 150  ? 1 150  
# 
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 9CO9 MET B 17   ? UNP P0DTC2 ?   ?    insertion        17   1   
1 9CO9 PRO B 18   ? UNP P0DTC2 ASN 17   conflict         18   2   
1 9CO9 PHE B 20   ? UNP P0DTC2 THR 19   conflict         20   3   
1 9CO9 ASN B 21   ? UNP P0DTC2 THR 20   conflict         21   4   
1 9CO9 LEU B 22   ? UNP P0DTC2 ARG 21   conflict         22   5   
1 9CO9 ILE B 23   ? UNP P0DTC2 THR 22   conflict         23   6   
1 9CO9 THR B 24   ? UNP P0DTC2 GLN 23   conflict         24   7   
1 9CO9 THR B 25   ? UNP P0DTC2 LEU 24   conflict         25   8   
1 9CO9 THR B 26   ? UNP P0DTC2 PRO 25   conflict         26   9   
1 9CO9 GLN B 27   ? UNP P0DTC2 PRO 26   conflict         27   10  
1 9CO9 SER B 28   ? UNP P0DTC2 ALA 27   conflict         28   11  
1 9CO9 LEU B 51   ? UNP P0DTC2 SER 50   conflict         51   12  
1 9CO9 ?   B ?    ? UNP P0DTC2 HIS 69   deletion         ?    13  
1 9CO9 ?   B ?    ? UNP P0DTC2 VAL 70   deletion         ?    14  
1 9CO9 PHE B 126  ? UNP P0DTC2 VAL 127  conflict         126  15  
1 9CO9 ASP B 141  ? UNP P0DTC2 GLY 142  conflict         141  16  
1 9CO9 ?   B ?    ? UNP P0DTC2 TYR 144  deletion         ?    17  
1 9CO9 SER B 155  ? UNP P0DTC2 PHE 157  conflict         155  18  
1 9CO9 GLY B 156  ? UNP P0DTC2 ARG 158  conflict         156  19  
1 9CO9 ?   B ?    ? UNP P0DTC2 ASN 211  deletion         ?    20  
1 9CO9 ILE B 209  ? UNP P0DTC2 LEU 212  conflict         209  21  
1 9CO9 GLY B 210  ? UNP P0DTC2 VAL 213  conflict         210  22  
1 9CO9 PHE B 213  ? UNP P0DTC2 LEU 216  conflict         213  23  
1 9CO9 ASN B 242  ? UNP P0DTC2 HIS 245  conflict         242  24  
1 9CO9 ASP B 261  ? UNP P0DTC2 ALA 264  conflict         261  25  
1 9CO9 VAL B 329  ? UNP P0DTC2 ILE 332  conflict         329  26  
1 9CO9 HIS B 336  ? UNP P0DTC2 GLY 339  conflict         336  27  
1 9CO9 THR B 353  ? UNP P0DTC2 LYS 356  conflict         353  28  
1 9CO9 PHE B 368  ? UNP P0DTC2 SER 371  conflict         368  29  
1 9CO9 PRO B 370  ? UNP P0DTC2 SER 373  conflict         370  30  
1 9CO9 PHE B 372  ? UNP P0DTC2 SER 375  conflict         372  31  
1 9CO9 ALA B 373  ? UNP P0DTC2 THR 376  conflict         373  32  
1 9CO9 LYS B 400  ? UNP P0DTC2 ARG 403  conflict         400  33  
1 9CO9 ASN B 402  ? UNP P0DTC2 ASP 405  conflict         402  34  
1 9CO9 SER B 405  ? UNP P0DTC2 ARG 408  conflict         405  35  
1 9CO9 ASN B 414  ? UNP P0DTC2 LYS 417  conflict         414  36  
1 9CO9 LYS B 437  ? UNP P0DTC2 ASN 440  conflict         437  37  
1 9CO9 HIS B 442  ? UNP P0DTC2 VAL 445  conflict         442  38  
1 9CO9 SER B 443  ? UNP P0DTC2 GLY 446  conflict         443  39  
1 9CO9 ASP B 447  ? UNP P0DTC2 ASN 450  conflict         447  40  
1 9CO9 TRP B 449  ? UNP P0DTC2 LEU 452  conflict         449  41  
1 9CO9 SER B 452  ? UNP P0DTC2 LEU 455  conflict         452  42  
1 9CO9 LYS B 457  ? UNP P0DTC2 ASN 460  conflict         457  43  
1 9CO9 ASN B 474  ? UNP P0DTC2 SER 477  conflict         474  44  
1 9CO9 LYS B 475  ? UNP P0DTC2 THR 478  conflict         475  45  
1 9CO9 LYS B 478  ? UNP P0DTC2 ASN 481  conflict         478  46  
1 9CO9 ?   B ?    ? UNP P0DTC2 VAL 483  deletion         ?    47  
1 9CO9 LYS B 480  ? UNP P0DTC2 GLU 484  conflict         480  48  
1 9CO9 PRO B 482  ? UNP P0DTC2 PHE 486  conflict         482  49  
1 9CO9 ARG B 494  ? UNP P0DTC2 GLN 498  conflict         494  50  
1 9CO9 TYR B 497  ? UNP P0DTC2 ASN 501  conflict         497  51  
1 9CO9 HIS B 501  ? UNP P0DTC2 TYR 505  conflict         501  52  
1 9CO9 LYS B 550  ? UNP P0DTC2 GLU 554  conflict         550  53  
1 9CO9 VAL B 566  ? UNP P0DTC2 ALA 570  conflict         566  54  
1 9CO9 GLY B 610  ? UNP P0DTC2 ASP 614  conflict         610  55  
1 9CO9 SER B 617  ? UNP P0DTC2 PRO 621  conflict         617  56  
1 9CO9 TYR B 651  ? UNP P0DTC2 HIS 655  conflict         651  57  
1 9CO9 LYS B 675  ? UNP P0DTC2 ASN 679  conflict         675  58  
1 9CO9 ARG B 677  ? UNP P0DTC2 PRO 681  conflict         677  59  
1 9CO9 ALA B 678  ? UNP P0DTC2 ARG 682  conflict         678  60  
1 9CO9 GLY B 679  ? UNP P0DTC2 ARG 683  conflict         679  61  
1 9CO9 LYS B 760  ? UNP P0DTC2 ASN 764  conflict         760  62  
1 9CO9 TYR B 792  ? UNP P0DTC2 ASP 796  conflict         792  63  
1 9CO9 PRO B 813  ? UNP P0DTC2 PHE 817  conflict         813  64  
1 9CO9 PRO B 888  ? UNP P0DTC2 ALA 892  conflict         888  65  
1 9CO9 PRO B 895  ? UNP P0DTC2 ALA 899  conflict         895  66  
1 9CO9 PHE B 935  ? UNP P0DTC2 SER 939  conflict         935  67  
1 9CO9 PRO B 938  ? UNP P0DTC2 ALA 942  conflict         938  68  
1 9CO9 HIS B 950  ? UNP P0DTC2 GLN 954  conflict         950  69  
1 9CO9 LYS B 965  ? UNP P0DTC2 ASN 969  conflict         965  70  
1 9CO9 PRO B 982  ? UNP P0DTC2 LYS 986  conflict         982  71  
1 9CO9 PRO B 983  ? UNP P0DTC2 VAL 987  conflict         983  72  
1 9CO9 LEU B 1139 ? UNP P0DTC2 PRO 1143 conflict         1139 73  
1 9CO9 GLY B 1208 ? UNP P0DTC2 TRP 1212 conflict         1208 74  
1 9CO9 SER B 1209 ? UNP P0DTC2 PRO 1213 conflict         1209 75  
1 9CO9 GLY B 1210 ? UNP P0DTC2 TRP 1214 conflict         1210 76  
1 9CO9 PRO B 1213 ? UNP P0DTC2 ?   ?    'expression tag' 1213 77  
1 9CO9 GLU B 1214 ? UNP P0DTC2 ?   ?    'expression tag' 1214 78  
1 9CO9 ALA B 1215 ? UNP P0DTC2 ?   ?    'expression tag' 1215 79  
1 9CO9 PRO B 1216 ? UNP P0DTC2 ?   ?    'expression tag' 1216 80  
1 9CO9 ARG B 1217 ? UNP P0DTC2 ?   ?    'expression tag' 1217 81  
1 9CO9 ASP B 1218 ? UNP P0DTC2 ?   ?    'expression tag' 1218 82  
1 9CO9 GLY B 1219 ? UNP P0DTC2 ?   ?    'expression tag' 1219 83  
1 9CO9 GLN B 1220 ? UNP P0DTC2 ?   ?    'expression tag' 1220 84  
1 9CO9 ALA B 1221 ? UNP P0DTC2 ?   ?    'expression tag' 1221 85  
1 9CO9 TYR B 1222 ? UNP P0DTC2 ?   ?    'expression tag' 1222 86  
1 9CO9 VAL B 1223 ? UNP P0DTC2 ?   ?    'expression tag' 1223 87  
1 9CO9 ARG B 1224 ? UNP P0DTC2 ?   ?    'expression tag' 1224 88  
1 9CO9 LYS B 1225 ? UNP P0DTC2 ?   ?    'expression tag' 1225 89  
1 9CO9 ASP B 1226 ? UNP P0DTC2 ?   ?    'expression tag' 1226 90  
1 9CO9 GLY B 1227 ? UNP P0DTC2 ?   ?    'expression tag' 1227 91  
1 9CO9 GLU B 1228 ? UNP P0DTC2 ?   ?    'expression tag' 1228 92  
1 9CO9 TRP B 1229 ? UNP P0DTC2 ?   ?    'expression tag' 1229 93  
1 9CO9 VAL B 1230 ? UNP P0DTC2 ?   ?    'expression tag' 1230 94  
1 9CO9 LEU B 1231 ? UNP P0DTC2 ?   ?    'expression tag' 1231 95  
1 9CO9 LEU B 1232 ? UNP P0DTC2 ?   ?    'expression tag' 1232 96  
1 9CO9 SER B 1233 ? UNP P0DTC2 ?   ?    'expression tag' 1233 97  
1 9CO9 THR B 1234 ? UNP P0DTC2 ?   ?    'expression tag' 1234 98  
1 9CO9 PHE B 1235 ? UNP P0DTC2 ?   ?    'expression tag' 1235 99  
1 9CO9 LEU B 1236 ? UNP P0DTC2 ?   ?    'expression tag' 1236 100 
1 9CO9 GLY B 1237 ? UNP P0DTC2 ?   ?    'expression tag' 1237 101 
1 9CO9 HIS B 1238 ? UNP P0DTC2 ?   ?    'expression tag' 1238 102 
1 9CO9 HIS B 1239 ? UNP P0DTC2 ?   ?    'expression tag' 1239 103 
1 9CO9 HIS B 1240 ? UNP P0DTC2 ?   ?    'expression tag' 1240 104 
1 9CO9 HIS B 1241 ? UNP P0DTC2 ?   ?    'expression tag' 1241 105 
1 9CO9 HIS B 1242 ? UNP P0DTC2 ?   ?    'expression tag' 1242 106 
1 9CO9 HIS B 1243 ? UNP P0DTC2 ?   ?    'expression tag' 1243 107 
2 9CO9 MET A 17   ? UNP P0DTC2 ?   ?    insertion        17   108 
2 9CO9 PRO A 18   ? UNP P0DTC2 ASN 17   conflict         18   109 
2 9CO9 PHE A 20   ? UNP P0DTC2 THR 19   conflict         20   110 
2 9CO9 ASN A 21   ? UNP P0DTC2 THR 20   conflict         21   111 
2 9CO9 LEU A 22   ? UNP P0DTC2 ARG 21   conflict         22   112 
2 9CO9 ILE A 23   ? UNP P0DTC2 THR 22   conflict         23   113 
2 9CO9 THR A 24   ? UNP P0DTC2 GLN 23   conflict         24   114 
2 9CO9 THR A 25   ? UNP P0DTC2 LEU 24   conflict         25   115 
2 9CO9 THR A 26   ? UNP P0DTC2 PRO 25   conflict         26   116 
2 9CO9 GLN A 27   ? UNP P0DTC2 PRO 26   conflict         27   117 
2 9CO9 SER A 28   ? UNP P0DTC2 ALA 27   conflict         28   118 
2 9CO9 LEU A 51   ? UNP P0DTC2 SER 50   conflict         51   119 
2 9CO9 ?   A ?    ? UNP P0DTC2 HIS 69   deletion         ?    120 
2 9CO9 ?   A ?    ? UNP P0DTC2 VAL 70   deletion         ?    121 
2 9CO9 PHE A 126  ? UNP P0DTC2 VAL 127  conflict         126  122 
2 9CO9 ASP A 141  ? UNP P0DTC2 GLY 142  conflict         141  123 
2 9CO9 ?   A ?    ? UNP P0DTC2 TYR 144  deletion         ?    124 
2 9CO9 SER A 155  ? UNP P0DTC2 PHE 157  conflict         155  125 
2 9CO9 GLY A 156  ? UNP P0DTC2 ARG 158  conflict         156  126 
2 9CO9 ?   A ?    ? UNP P0DTC2 ASN 211  deletion         ?    127 
2 9CO9 ILE A 209  ? UNP P0DTC2 LEU 212  conflict         209  128 
2 9CO9 GLY A 210  ? UNP P0DTC2 VAL 213  conflict         210  129 
2 9CO9 PHE A 213  ? UNP P0DTC2 LEU 216  conflict         213  130 
2 9CO9 ASN A 242  ? UNP P0DTC2 HIS 245  conflict         242  131 
2 9CO9 ASP A 261  ? UNP P0DTC2 ALA 264  conflict         261  132 
2 9CO9 VAL A 329  ? UNP P0DTC2 ILE 332  conflict         329  133 
2 9CO9 HIS A 336  ? UNP P0DTC2 GLY 339  conflict         336  134 
2 9CO9 THR A 353  ? UNP P0DTC2 LYS 356  conflict         353  135 
2 9CO9 PHE A 368  ? UNP P0DTC2 SER 371  conflict         368  136 
2 9CO9 PRO A 370  ? UNP P0DTC2 SER 373  conflict         370  137 
2 9CO9 PHE A 372  ? UNP P0DTC2 SER 375  conflict         372  138 
2 9CO9 ALA A 373  ? UNP P0DTC2 THR 376  conflict         373  139 
2 9CO9 LYS A 400  ? UNP P0DTC2 ARG 403  conflict         400  140 
2 9CO9 ASN A 402  ? UNP P0DTC2 ASP 405  conflict         402  141 
2 9CO9 SER A 405  ? UNP P0DTC2 ARG 408  conflict         405  142 
2 9CO9 ASN A 414  ? UNP P0DTC2 LYS 417  conflict         414  143 
2 9CO9 LYS A 437  ? UNP P0DTC2 ASN 440  conflict         437  144 
2 9CO9 HIS A 442  ? UNP P0DTC2 VAL 445  conflict         442  145 
2 9CO9 SER A 443  ? UNP P0DTC2 GLY 446  conflict         443  146 
2 9CO9 ASP A 447  ? UNP P0DTC2 ASN 450  conflict         447  147 
2 9CO9 TRP A 449  ? UNP P0DTC2 LEU 452  conflict         449  148 
2 9CO9 SER A 452  ? UNP P0DTC2 LEU 455  conflict         452  149 
2 9CO9 LYS A 457  ? UNP P0DTC2 ASN 460  conflict         457  150 
2 9CO9 ASN A 474  ? UNP P0DTC2 SER 477  conflict         474  151 
2 9CO9 LYS A 475  ? UNP P0DTC2 THR 478  conflict         475  152 
2 9CO9 LYS A 478  ? UNP P0DTC2 ASN 481  conflict         478  153 
2 9CO9 ?   A ?    ? UNP P0DTC2 VAL 483  deletion         ?    154 
2 9CO9 LYS A 480  ? UNP P0DTC2 GLU 484  conflict         480  155 
2 9CO9 PRO A 482  ? UNP P0DTC2 PHE 486  conflict         482  156 
2 9CO9 ARG A 494  ? UNP P0DTC2 GLN 498  conflict         494  157 
2 9CO9 TYR A 497  ? UNP P0DTC2 ASN 501  conflict         497  158 
2 9CO9 HIS A 501  ? UNP P0DTC2 TYR 505  conflict         501  159 
2 9CO9 LYS A 550  ? UNP P0DTC2 GLU 554  conflict         550  160 
2 9CO9 VAL A 566  ? UNP P0DTC2 ALA 570  conflict         566  161 
2 9CO9 GLY A 610  ? UNP P0DTC2 ASP 614  conflict         610  162 
2 9CO9 SER A 617  ? UNP P0DTC2 PRO 621  conflict         617  163 
2 9CO9 TYR A 651  ? UNP P0DTC2 HIS 655  conflict         651  164 
2 9CO9 LYS A 675  ? UNP P0DTC2 ASN 679  conflict         675  165 
2 9CO9 ARG A 677  ? UNP P0DTC2 PRO 681  conflict         677  166 
2 9CO9 ALA A 678  ? UNP P0DTC2 ARG 682  conflict         678  167 
2 9CO9 GLY A 679  ? UNP P0DTC2 ARG 683  conflict         679  168 
2 9CO9 LYS A 760  ? UNP P0DTC2 ASN 764  conflict         760  169 
2 9CO9 TYR A 792  ? UNP P0DTC2 ASP 796  conflict         792  170 
2 9CO9 PRO A 813  ? UNP P0DTC2 PHE 817  conflict         813  171 
2 9CO9 PRO A 888  ? UNP P0DTC2 ALA 892  conflict         888  172 
2 9CO9 PRO A 895  ? UNP P0DTC2 ALA 899  conflict         895  173 
2 9CO9 PHE A 935  ? UNP P0DTC2 SER 939  conflict         935  174 
2 9CO9 PRO A 938  ? UNP P0DTC2 ALA 942  conflict         938  175 
2 9CO9 HIS A 950  ? UNP P0DTC2 GLN 954  conflict         950  176 
2 9CO9 LYS A 965  ? UNP P0DTC2 ASN 969  conflict         965  177 
2 9CO9 PRO A 982  ? UNP P0DTC2 LYS 986  conflict         982  178 
2 9CO9 PRO A 983  ? UNP P0DTC2 VAL 987  conflict         983  179 
2 9CO9 LEU A 1139 ? UNP P0DTC2 PRO 1143 conflict         1139 180 
2 9CO9 GLY A 1208 ? UNP P0DTC2 TRP 1212 conflict         1208 181 
2 9CO9 SER A 1209 ? UNP P0DTC2 PRO 1213 conflict         1209 182 
2 9CO9 GLY A 1210 ? UNP P0DTC2 TRP 1214 conflict         1210 183 
2 9CO9 PRO A 1213 ? UNP P0DTC2 ?   ?    'expression tag' 1213 184 
2 9CO9 GLU A 1214 ? UNP P0DTC2 ?   ?    'expression tag' 1214 185 
2 9CO9 ALA A 1215 ? UNP P0DTC2 ?   ?    'expression tag' 1215 186 
2 9CO9 PRO A 1216 ? UNP P0DTC2 ?   ?    'expression tag' 1216 187 
2 9CO9 ARG A 1217 ? UNP P0DTC2 ?   ?    'expression tag' 1217 188 
2 9CO9 ASP A 1218 ? UNP P0DTC2 ?   ?    'expression tag' 1218 189 
2 9CO9 GLY A 1219 ? UNP P0DTC2 ?   ?    'expression tag' 1219 190 
2 9CO9 GLN A 1220 ? UNP P0DTC2 ?   ?    'expression tag' 1220 191 
2 9CO9 ALA A 1221 ? UNP P0DTC2 ?   ?    'expression tag' 1221 192 
2 9CO9 TYR A 1222 ? UNP P0DTC2 ?   ?    'expression tag' 1222 193 
2 9CO9 VAL A 1223 ? UNP P0DTC2 ?   ?    'expression tag' 1223 194 
2 9CO9 ARG A 1224 ? UNP P0DTC2 ?   ?    'expression tag' 1224 195 
2 9CO9 LYS A 1225 ? UNP P0DTC2 ?   ?    'expression tag' 1225 196 
2 9CO9 ASP A 1226 ? UNP P0DTC2 ?   ?    'expression tag' 1226 197 
2 9CO9 GLY A 1227 ? UNP P0DTC2 ?   ?    'expression tag' 1227 198 
2 9CO9 GLU A 1228 ? UNP P0DTC2 ?   ?    'expression tag' 1228 199 
2 9CO9 TRP A 1229 ? UNP P0DTC2 ?   ?    'expression tag' 1229 200 
2 9CO9 VAL A 1230 ? UNP P0DTC2 ?   ?    'expression tag' 1230 201 
2 9CO9 LEU A 1231 ? UNP P0DTC2 ?   ?    'expression tag' 1231 202 
2 9CO9 LEU A 1232 ? UNP P0DTC2 ?   ?    'expression tag' 1232 203 
2 9CO9 SER A 1233 ? UNP P0DTC2 ?   ?    'expression tag' 1233 204 
2 9CO9 THR A 1234 ? UNP P0DTC2 ?   ?    'expression tag' 1234 205 
2 9CO9 PHE A 1235 ? UNP P0DTC2 ?   ?    'expression tag' 1235 206 
2 9CO9 LEU A 1236 ? UNP P0DTC2 ?   ?    'expression tag' 1236 207 
2 9CO9 GLY A 1237 ? UNP P0DTC2 ?   ?    'expression tag' 1237 208 
2 9CO9 HIS A 1238 ? UNP P0DTC2 ?   ?    'expression tag' 1238 209 
2 9CO9 HIS A 1239 ? UNP P0DTC2 ?   ?    'expression tag' 1239 210 
2 9CO9 HIS A 1240 ? UNP P0DTC2 ?   ?    'expression tag' 1240 211 
2 9CO9 HIS A 1241 ? UNP P0DTC2 ?   ?    'expression tag' 1241 212 
2 9CO9 HIS A 1242 ? UNP P0DTC2 ?   ?    'expression tag' 1242 213 
2 9CO9 HIS A 1243 ? UNP P0DTC2 ?   ?    'expression tag' 1243 214 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 334 ? ASN A 340 ? PRO B 334 ASN B 340 1 ? 7 
HELX_P HELX_P2  AA2 LYS A 400 ? ILE A 407 ? LYS B 400 ILE B 407 5 ? 8 
HELX_P HELX_P3  AA3 GLY A 413 ? ASN A 419 ? GLY B 413 ASN B 419 1 ? 7 
HELX_P HELX_P4  AA4 GLY A 498 ? GLN A 502 ? GLY B 498 GLN B 502 5 ? 5 
HELX_P HELX_P5  AA5 PRO B 334 ? ASN B 340 ? PRO A 334 ASN A 340 1 ? 7 
HELX_P HELX_P6  AA6 SER B 380 ? LEU B 384 ? SER A 380 LEU A 384 5 ? 5 
HELX_P HELX_P7  AA7 LYS B 400 ? ILE B 407 ? LYS A 400 ILE A 407 5 ? 8 
HELX_P HELX_P8  AA8 GLY B 413 ? ASN B 419 ? GLY A 413 ASN A 419 1 ? 7 
HELX_P HELX_P9  AA9 GLY B 498 ? GLN B 502 ? GLY A 498 GLN A 502 5 ? 5 
HELX_P HELX_P10 AB1 LYS C 87  ? THR C 91  ? LYS D 87  THR D 91  5 ? 5 
HELX_P HELX_P11 AB2 LYS D 87  ? THR D 91  ? LYS E 87  THR E 91  5 ? 5 
# 
_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 333 SG ? ? ? 1_555 A CYS 358 SG ? ? B CYS 333 B CYS 358 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2  disulf ? ? A CYS 376 SG ? ? ? 1_555 A CYS 429 SG ? ? B CYS 376 B CYS 429 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf3  disulf ? ? A CYS 388 SG ? ? ? 1_555 A CYS 521 SG ? ? B CYS 388 B CYS 521 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf4  disulf ? ? A CYS 477 SG ? ? ? 1_555 A CYS 484 SG ? ? B CYS 477 B CYS 484 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf5  disulf ? ? B CYS 333 SG ? ? ? 1_555 B CYS 358 SG ? ? A CYS 333 A CYS 358 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf6  disulf ? ? B CYS 376 SG ? ? ? 1_555 B CYS 429 SG ? ? A CYS 376 A CYS 429 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf7  disulf ? ? B CYS 388 SG ? ? ? 1_555 B CYS 521 SG ? ? A CYS 388 A CYS 521 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf8  disulf ? ? B CYS 477 SG ? ? ? 1_555 B CYS 484 SG ? ? A CYS 477 A CYS 484 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf9  disulf ? ? C CYS 22  SG ? ? ? 1_555 C CYS 96  SG ? ? D CYS 22  D CYS 96  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf10 disulf ? ? C CYS 50  SG ? ? ? 1_555 C CYS 104 SG ? ? D CYS 50  D CYS 104 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf11 disulf ? ? D CYS 22  SG ? ? ? 1_555 D CYS 96  SG ? ? E CYS 22  E CYS 96  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf12 disulf ? ? D CYS 50  SG ? ? ? 1_555 D CYS 104 SG ? ? E CYS 50  E CYS 104 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  CYS A 333 ? CYS A 358 ? CYS B 333 ? 1_555 CYS B 358 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 376 ? CYS A 429 ? CYS B 376 ? 1_555 CYS B 429 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 388 ? CYS A 521 ? CYS B 388 ? 1_555 CYS B 521 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 477 ? CYS A 484 ? CYS B 477 ? 1_555 CYS B 484 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS B 333 ? CYS B 358 ? CYS A 333 ? 1_555 CYS A 358 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS B 376 ? CYS B 429 ? CYS A 376 ? 1_555 CYS A 429 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS B 388 ? CYS B 521 ? CYS A 388 ? 1_555 CYS A 521 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS B 477 ? CYS B 484 ? CYS A 477 ? 1_555 CYS A 484 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS C 22  ? CYS C 96  ? CYS D 22  ? 1_555 CYS D 96  ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS C 50  ? CYS C 104 ? CYS D 50  ? 1_555 CYS D 104 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS D 22  ? CYS D 96  ? CYS E 22  ? 1_555 CYS E 96  ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS D 50  ? CYS D 104 ? CYS E 50  ? 1_555 CYS E 104 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
AA8 ? 5 ? 
AA9 ? 4 ? 
AB1 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? 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 ASN A 351 ? ILE A 355 ? ASN B 351 ILE B 355 
AA1 2 VAL A 392 ? ILE A 399 ? VAL B 392 ILE B 399 
AA1 3 TYR A 504 ? LEU A 509 ? TYR B 504 LEU B 509 
AA1 4 GLY A 428 ? ASN A 434 ? GLY B 428 ASN B 434 
AA1 5 ALA A 373 ? TYR A 377 ? ALA B 373 TYR B 377 
AA2 1 TRP A 449 ? ARG A 451 ? TRP B 449 ARG B 451 
AA2 2 LEU A 488 ? SER A 490 ? LEU B 488 SER B 490 
AA3 1 TYR A 470 ? GLN A 471 ? TYR B 470 GLN B 471 
AA3 2 CYS A 484 ? TYR A 485 ? CYS B 484 TYR B 485 
AA4 1 ASN B 351 ? ILE B 355 ? ASN A 351 ILE A 355 
AA4 2 THR B 390 ? ILE B 399 ? THR A 390 ILE A 399 
AA4 3 TYR B 504 ? GLU B 512 ? TYR A 504 GLU A 512 
AA4 4 GLY B 428 ? ASN B 434 ? GLY A 428 ASN A 434 
AA4 5 ALA B 373 ? TYR B 377 ? ALA A 373 TYR A 377 
AA5 1 TRP B 449 ? ARG B 451 ? TRP A 449 ARG A 451 
AA5 2 LEU B 488 ? SER B 490 ? LEU A 488 SER A 490 
AA6 1 TYR B 470 ? GLN B 471 ? TYR A 470 GLN A 471 
AA6 2 CYS B 484 ? TYR B 485 ? CYS A 484 TYR A 485 
AA7 1 LEU C 4   ? SER C 7   ? LEU D 4   SER D 7   
AA7 2 SER C 17  ? ALA C 24  ? SER D 17  ALA D 24  
AA7 3 THR C 78  ? ASN C 84  ? THR D 78  ASN D 84  
AA7 4 PHE C 68  ? ASP C 73  ? PHE D 68  ASP D 73  
AA8 1 GLY C 10  ? VAL C 12  ? GLY D 10  VAL D 12  
AA8 2 THR C 123 ? VAL C 127 ? THR D 123 VAL D 127 
AA8 3 ALA C 92  ? PRO C 100 ? ALA D 92  PRO D 100 
AA8 4 HIS C 32  ? GLN C 39  ? HIS D 32  GLN D 39  
AA8 5 GLU C 46  ? CYS C 50  ? GLU D 46  CYS D 50  
AA9 1 GLN D 5   ? SER D 7   ? GLN E 5   SER E 7   
AA9 2 SER D 17  ? THR D 23  ? SER E 17  THR E 23  
AA9 3 THR D 78  ? ASN D 84  ? THR E 78  ASN E 84  
AA9 4 PHE D 68  ? ASP D 73  ? PHE E 68  ASP E 73  
AB1 1 GLY D 10  ? VAL D 12  ? GLY E 10  VAL E 12  
AB1 2 THR D 123 ? VAL D 127 ? THR E 123 VAL E 127 
AB1 3 ALA D 92  ? PRO D 100 ? ALA E 92  PRO E 100 
AB1 4 HIS D 32  ? GLN D 39  ? HIS E 32  GLN E 39  
AB1 5 GLU D 46  ? ILE D 51  ? GLU E 46  ILE E 51  
AB1 6 TYR D 59  ? TYR D 60  ? TYR E 59  TYR E 60  
# 
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 THR A 353 ? N THR B 353 O ALA A 394 ? O ALA B 394 
AA1 2 3 N PHE A 397 ? N PHE B 397 O VAL A 506 ? O VAL B 506 
AA1 3 4 O LEU A 509 ? O LEU B 509 N CYS A 429 ? N CYS B 429 
AA1 4 5 O ALA A 432 ? O ALA B 432 N ALA A 373 ? N ALA B 373 
AA2 1 2 N TYR A 450 ? N TYR B 450 O GLN A 489 ? O GLN B 489 
AA3 1 2 N TYR A 470 ? N TYR B 470 O TYR A 485 ? O TYR B 485 
AA4 1 2 N THR B 353 ? N THR A 353 O ALA B 394 ? O ALA A 394 
AA4 2 3 N TYR B 393 ? N TYR A 393 O SER B 510 ? O SER A 510 
AA4 3 4 O VAL B 507 ? O VAL A 507 N ILE B 431 ? N ILE A 431 
AA4 4 5 O GLY B 428 ? O GLY A 428 N TYR B 377 ? N TYR A 377 
AA5 1 2 N TYR B 450 ? N TYR A 450 O GLN B 489 ? O GLN A 489 
AA6 1 2 N TYR B 470 ? N TYR A 470 O TYR B 485 ? O TYR A 485 
AA7 1 2 N GLN C 5   ? N GLN D 5   O THR C 23  ? O THR D 23  
AA7 2 3 N LEU C 18  ? N LEU D 18  O MET C 83  ? O MET D 83  
AA7 3 4 O TYR C 80  ? O TYR D 80  N SER C 71  ? N SER D 71  
AA8 1 2 N VAL C 12  ? N VAL D 12  O THR C 126 ? O THR D 126 
AA8 2 3 O THR C 123 ? O THR D 123 N TYR C 94  ? N TYR D 94  
AA8 3 4 O TYR C 95  ? O TYR D 95  N PHE C 37  ? N PHE D 37  
AA8 4 5 N TRP C 36  ? N TRP D 36  O VAL C 48  ? O VAL D 48  
AA9 1 2 N GLN D 5   ? N GLN E 5   O THR D 23  ? O THR E 23  
AA9 2 3 N LEU D 18  ? N LEU E 18  O MET D 83  ? O MET E 83  
AA9 3 4 O TYR D 80  ? O TYR E 80  N SER D 71  ? N SER E 71  
AB1 1 2 N GLY D 10  ? N GLY E 10  O THR D 126 ? O THR E 126 
AB1 2 3 O VAL D 125 ? O VAL E 125 N ALA D 92  ? N ALA E 92  
AB1 3 4 O TYR D 95  ? O TYR E 95  N PHE D 37  ? N PHE E 37  
AB1 4 5 N TRP D 36  ? N TRP E 36  O VAL D 48  ? O VAL E 48  
AB1 5 6 N CYS D 50  ? N CYS E 50  O TYR D 59  ? O TYR E 59  
# 
_pdbx_entry_details.entry_id                   9CO9 
_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     ? 
_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 CA B CYS 376 ? ? CB B CYS 376 ? ? SG B CYS 376 ? ? 121.33 114.20 7.13 1.10 N 
2 1 CA A CYS 388 ? ? CB A CYS 388 ? ? SG A CYS 388 ? ? 123.07 114.20 8.87 1.10 N 
3 1 CA D CYS 22  ? ? CB D CYS 22  ? ? SG D CYS 22  ? ? 121.89 114.20 7.69 1.10 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 CYS B 333 ? ? 68.06   145.46  
2  1 TYR B 362 ? ? -91.64  50.94   
3  1 ASN B 367 ? ? -92.07  51.96   
4  1 ASP B 439 ? ? -97.26  30.05   
5  1 CYS A 333 ? ? 67.59   140.95  
6  1 PRO A 334 ? ? -82.12  48.80   
7  1 TYR A 362 ? ? -89.65  49.45   
8  1 ASN A 367 ? ? -91.10  50.24   
9  1 ASN A 391 ? ? 33.81   55.63   
10 1 ASP A 439 ? ? -93.62  52.74   
11 1 TYR A 446 ? ? -95.09  58.17   
12 1 LEU D 29  ? ? -98.02  58.08   
13 1 HIS D 30  ? ? -143.88 -7.07   
14 1 VAL D 48  ? ? -122.53 -51.91  
15 1 SER D 53  ? ? 52.25   -119.61 
16 1 ASP D 113 ? ? -55.61  106.05  
17 1 ASP D 115 ? ? -47.23  91.53   
18 1 TYR D 117 ? ? -80.07  -154.85 
19 1 TYR D 118 ? ? 10.14   82.67   
20 1 VAL E 48  ? ? -124.74 -55.45  
21 1 SER E 52  ? ? -78.37  -168.95 
22 1 ASP E 55  ? ? 56.38   -74.62  
23 1 SER E 108 ? ? -90.83  51.37   
24 1 SER E 128 ? ? -171.81 -179.27 
# 
_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     494 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.083 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CO9 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  8IOS 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                8IOS 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9CO9 
_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                  3.44 
_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               248315 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX 'JN.1 spike/Nanosota-9 complex' ?                           ? ? '1, 2' 
2 1 RECOMBINANT        COMPLEX 'JN.1 spike'                    'Recombinant spike protein' ? ? 1      
3 1 RECOMBINANT        COMPLEX Nanosota-9                      ?                           ? ? 2      
# 
_em_imaging.entry_id                        9CO9 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1100 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9CO9 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9CO9 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 B MET 1    ? A MET 1    
2    1 Y 1 B PHE 2    ? A PHE 2    
3    1 Y 1 B VAL 3    ? A VAL 3    
4    1 Y 1 B PHE 4    ? A PHE 4    
5    1 Y 1 B LEU 5    ? A LEU 5    
6    1 Y 1 B VAL 6    ? A VAL 6    
7    1 Y 1 B LEU 7    ? A LEU 7    
8    1 Y 1 B LEU 8    ? A LEU 8    
9    1 Y 1 B PRO 9    ? A PRO 9    
10   1 Y 1 B LEU 10   ? A LEU 10   
11   1 Y 1 B VAL 11   ? A VAL 11   
12   1 Y 1 B SER 12   ? A SER 12   
13   1 Y 1 B SER 13   ? A SER 13   
14   1 Y 1 B GLN 14   ? A GLN 14   
15   1 Y 1 B CYS 15   ? A CYS 15   
16   1 Y 1 B VAL 16   ? A VAL 16   
17   1 Y 1 B MET 17   ? A MET 17   
18   1 Y 1 B PRO 18   ? A PRO 18   
19   1 Y 1 B LEU 19   ? A LEU 19   
20   1 Y 1 B PHE 20   ? A PHE 20   
21   1 Y 1 B ASN 21   ? A ASN 21   
22   1 Y 1 B LEU 22   ? A LEU 22   
23   1 Y 1 B ILE 23   ? A ILE 23   
24   1 Y 1 B THR 24   ? A THR 24   
25   1 Y 1 B THR 25   ? A THR 25   
26   1 Y 1 B THR 26   ? A THR 26   
27   1 Y 1 B GLN 27   ? A GLN 27   
28   1 Y 1 B SER 28   ? A SER 28   
29   1 Y 1 B TYR 29   ? A TYR 29   
30   1 Y 1 B THR 30   ? A THR 30   
31   1 Y 1 B ASN 31   ? A ASN 31   
32   1 Y 1 B SER 32   ? A SER 32   
33   1 Y 1 B PHE 33   ? A PHE 33   
34   1 Y 1 B THR 34   ? A THR 34   
35   1 Y 1 B ARG 35   ? A ARG 35   
36   1 Y 1 B GLY 36   ? A GLY 36   
37   1 Y 1 B VAL 37   ? A VAL 37   
38   1 Y 1 B TYR 38   ? A TYR 38   
39   1 Y 1 B TYR 39   ? A TYR 39   
40   1 Y 1 B PRO 40   ? A PRO 40   
41   1 Y 1 B ASP 41   ? A ASP 41   
42   1 Y 1 B LYS 42   ? A LYS 42   
43   1 Y 1 B VAL 43   ? A VAL 43   
44   1 Y 1 B PHE 44   ? A PHE 44   
45   1 Y 1 B ARG 45   ? A ARG 45   
46   1 Y 1 B SER 46   ? A SER 46   
47   1 Y 1 B SER 47   ? A SER 47   
48   1 Y 1 B VAL 48   ? A VAL 48   
49   1 Y 1 B LEU 49   ? A LEU 49   
50   1 Y 1 B HIS 50   ? A HIS 50   
51   1 Y 1 B LEU 51   ? A LEU 51   
52   1 Y 1 B THR 52   ? A THR 52   
53   1 Y 1 B GLN 53   ? A GLN 53   
54   1 Y 1 B ASP 54   ? A ASP 54   
55   1 Y 1 B LEU 55   ? A LEU 55   
56   1 Y 1 B PHE 56   ? A PHE 56   
57   1 Y 1 B LEU 57   ? A LEU 57   
58   1 Y 1 B PRO 58   ? A PRO 58   
59   1 Y 1 B PHE 59   ? A PHE 59   
60   1 Y 1 B PHE 60   ? A PHE 60   
61   1 Y 1 B SER 61   ? A SER 61   
62   1 Y 1 B ASN 62   ? A ASN 62   
63   1 Y 1 B VAL 63   ? A VAL 63   
64   1 Y 1 B THR 64   ? A THR 64   
65   1 Y 1 B TRP 65   ? A TRP 65   
66   1 Y 1 B PHE 66   ? A PHE 66   
67   1 Y 1 B HIS 67   ? A HIS 67   
68   1 Y 1 B ALA 68   ? A ALA 68   
69   1 Y 1 B ILE 69   ? A ILE 69   
70   1 Y 1 B SER 70   ? A SER 70   
71   1 Y 1 B GLY 71   ? A GLY 71   
72   1 Y 1 B THR 72   ? A THR 72   
73   1 Y 1 B ASN 73   ? A ASN 73   
74   1 Y 1 B GLY 74   ? A GLY 74   
75   1 Y 1 B THR 75   ? A THR 75   
76   1 Y 1 B LYS 76   ? A LYS 76   
77   1 Y 1 B ARG 77   ? A ARG 77   
78   1 Y 1 B PHE 78   ? A PHE 78   
79   1 Y 1 B ASP 79   ? A ASP 79   
80   1 Y 1 B ASN 80   ? A ASN 80   
81   1 Y 1 B PRO 81   ? A PRO 81   
82   1 Y 1 B VAL 82   ? A VAL 82   
83   1 Y 1 B LEU 83   ? A LEU 83   
84   1 Y 1 B PRO 84   ? A PRO 84   
85   1 Y 1 B PHE 85   ? A PHE 85   
86   1 Y 1 B ASN 86   ? A ASN 86   
87   1 Y 1 B ASP 87   ? A ASP 87   
88   1 Y 1 B GLY 88   ? A GLY 88   
89   1 Y 1 B VAL 89   ? A VAL 89   
90   1 Y 1 B TYR 90   ? A TYR 90   
91   1 Y 1 B PHE 91   ? A PHE 91   
92   1 Y 1 B ALA 92   ? A ALA 92   
93   1 Y 1 B SER 93   ? A SER 93   
94   1 Y 1 B THR 94   ? A THR 94   
95   1 Y 1 B GLU 95   ? A GLU 95   
96   1 Y 1 B LYS 96   ? A LYS 96   
97   1 Y 1 B SER 97   ? A SER 97   
98   1 Y 1 B ASN 98   ? A ASN 98   
99   1 Y 1 B ILE 99   ? A ILE 99   
100  1 Y 1 B ILE 100  ? A ILE 100  
101  1 Y 1 B ARG 101  ? A ARG 101  
102  1 Y 1 B GLY 102  ? A GLY 102  
103  1 Y 1 B TRP 103  ? A TRP 103  
104  1 Y 1 B ILE 104  ? A ILE 104  
105  1 Y 1 B PHE 105  ? A PHE 105  
106  1 Y 1 B GLY 106  ? A GLY 106  
107  1 Y 1 B THR 107  ? A THR 107  
108  1 Y 1 B THR 108  ? A THR 108  
109  1 Y 1 B LEU 109  ? A LEU 109  
110  1 Y 1 B ASP 110  ? A ASP 110  
111  1 Y 1 B SER 111  ? A SER 111  
112  1 Y 1 B LYS 112  ? A LYS 112  
113  1 Y 1 B THR 113  ? A THR 113  
114  1 Y 1 B GLN 114  ? A GLN 114  
115  1 Y 1 B SER 115  ? A SER 115  
116  1 Y 1 B LEU 116  ? A LEU 116  
117  1 Y 1 B LEU 117  ? A LEU 117  
118  1 Y 1 B ILE 118  ? A ILE 118  
119  1 Y 1 B VAL 119  ? A VAL 119  
120  1 Y 1 B ASN 120  ? A ASN 120  
121  1 Y 1 B ASN 121  ? A ASN 121  
122  1 Y 1 B ALA 122  ? A ALA 122  
123  1 Y 1 B THR 123  ? A THR 123  
124  1 Y 1 B ASN 124  ? A ASN 124  
125  1 Y 1 B VAL 125  ? A VAL 125  
126  1 Y 1 B PHE 126  ? A PHE 126  
127  1 Y 1 B ILE 127  ? A ILE 127  
128  1 Y 1 B LYS 128  ? A LYS 128  
129  1 Y 1 B VAL 129  ? A VAL 129  
130  1 Y 1 B CYS 130  ? A CYS 130  
131  1 Y 1 B GLU 131  ? A GLU 131  
132  1 Y 1 B PHE 132  ? A PHE 132  
133  1 Y 1 B GLN 133  ? A GLN 133  
134  1 Y 1 B PHE 134  ? A PHE 134  
135  1 Y 1 B CYS 135  ? A CYS 135  
136  1 Y 1 B ASN 136  ? A ASN 136  
137  1 Y 1 B ASP 137  ? A ASP 137  
138  1 Y 1 B PRO 138  ? A PRO 138  
139  1 Y 1 B PHE 139  ? A PHE 139  
140  1 Y 1 B LEU 140  ? A LEU 140  
141  1 Y 1 B ASP 141  ? A ASP 141  
142  1 Y 1 B VAL 142  ? A VAL 142  
143  1 Y 1 B TYR 143  ? A TYR 143  
144  1 Y 1 B HIS 144  ? A HIS 144  
145  1 Y 1 B LYS 145  ? A LYS 145  
146  1 Y 1 B ASN 146  ? A ASN 146  
147  1 Y 1 B ASN 147  ? A ASN 147  
148  1 Y 1 B LYS 148  ? A LYS 148  
149  1 Y 1 B SER 149  ? A SER 149  
150  1 Y 1 B TRP 150  ? A TRP 150  
151  1 Y 1 B MET 151  ? A MET 151  
152  1 Y 1 B GLU 152  ? A GLU 152  
153  1 Y 1 B SER 153  ? A SER 153  
154  1 Y 1 B GLU 154  ? A GLU 154  
155  1 Y 1 B SER 155  ? A SER 155  
156  1 Y 1 B GLY 156  ? A GLY 156  
157  1 Y 1 B VAL 157  ? A VAL 157  
158  1 Y 1 B TYR 158  ? A TYR 158  
159  1 Y 1 B SER 159  ? A SER 159  
160  1 Y 1 B SER 160  ? A SER 160  
161  1 Y 1 B ALA 161  ? A ALA 161  
162  1 Y 1 B ASN 162  ? A ASN 162  
163  1 Y 1 B ASN 163  ? A ASN 163  
164  1 Y 1 B CYS 164  ? A CYS 164  
165  1 Y 1 B THR 165  ? A THR 165  
166  1 Y 1 B PHE 166  ? A PHE 166  
167  1 Y 1 B GLU 167  ? A GLU 167  
168  1 Y 1 B TYR 168  ? A TYR 168  
169  1 Y 1 B VAL 169  ? A VAL 169  
170  1 Y 1 B SER 170  ? A SER 170  
171  1 Y 1 B GLN 171  ? A GLN 171  
172  1 Y 1 B PRO 172  ? A PRO 172  
173  1 Y 1 B PHE 173  ? A PHE 173  
174  1 Y 1 B LEU 174  ? A LEU 174  
175  1 Y 1 B MET 175  ? A MET 175  
176  1 Y 1 B ASP 176  ? A ASP 176  
177  1 Y 1 B LEU 177  ? A LEU 177  
178  1 Y 1 B GLU 178  ? A GLU 178  
179  1 Y 1 B GLY 179  ? A GLY 179  
180  1 Y 1 B LYS 180  ? A LYS 180  
181  1 Y 1 B GLN 181  ? A GLN 181  
182  1 Y 1 B GLY 182  ? A GLY 182  
183  1 Y 1 B ASN 183  ? A ASN 183  
184  1 Y 1 B PHE 184  ? A PHE 184  
185  1 Y 1 B LYS 185  ? A LYS 185  
186  1 Y 1 B ASN 186  ? A ASN 186  
187  1 Y 1 B LEU 187  ? A LEU 187  
188  1 Y 1 B ARG 188  ? A ARG 188  
189  1 Y 1 B GLU 189  ? A GLU 189  
190  1 Y 1 B PHE 190  ? A PHE 190  
191  1 Y 1 B VAL 191  ? A VAL 191  
192  1 Y 1 B PHE 192  ? A PHE 192  
193  1 Y 1 B LYS 193  ? A LYS 193  
194  1 Y 1 B ASN 194  ? A ASN 194  
195  1 Y 1 B ILE 195  ? A ILE 195  
196  1 Y 1 B ASP 196  ? A ASP 196  
197  1 Y 1 B GLY 197  ? A GLY 197  
198  1 Y 1 B TYR 198  ? A TYR 198  
199  1 Y 1 B PHE 199  ? A PHE 199  
200  1 Y 1 B LYS 200  ? A LYS 200  
201  1 Y 1 B ILE 201  ? A ILE 201  
202  1 Y 1 B TYR 202  ? A TYR 202  
203  1 Y 1 B SER 203  ? A SER 203  
204  1 Y 1 B LYS 204  ? A LYS 204  
205  1 Y 1 B HIS 205  ? A HIS 205  
206  1 Y 1 B THR 206  ? A THR 206  
207  1 Y 1 B PRO 207  ? A PRO 207  
208  1 Y 1 B ILE 208  ? A ILE 208  
209  1 Y 1 B ILE 209  ? A ILE 209  
210  1 Y 1 B GLY 210  ? A GLY 210  
211  1 Y 1 B ARG 211  ? A ARG 211  
212  1 Y 1 B ASP 212  ? A ASP 212  
213  1 Y 1 B PHE 213  ? A PHE 213  
214  1 Y 1 B PRO 214  ? A PRO 214  
215  1 Y 1 B GLN 215  ? A GLN 215  
216  1 Y 1 B GLY 216  ? A GLY 216  
217  1 Y 1 B PHE 217  ? A PHE 217  
218  1 Y 1 B SER 218  ? A SER 218  
219  1 Y 1 B ALA 219  ? A ALA 219  
220  1 Y 1 B LEU 220  ? A LEU 220  
221  1 Y 1 B GLU 221  ? A GLU 221  
222  1 Y 1 B PRO 222  ? A PRO 222  
223  1 Y 1 B LEU 223  ? A LEU 223  
224  1 Y 1 B VAL 224  ? A VAL 224  
225  1 Y 1 B ASP 225  ? A ASP 225  
226  1 Y 1 B LEU 226  ? A LEU 226  
227  1 Y 1 B PRO 227  ? A PRO 227  
228  1 Y 1 B ILE 228  ? A ILE 228  
229  1 Y 1 B GLY 229  ? A GLY 229  
230  1 Y 1 B ILE 230  ? A ILE 230  
231  1 Y 1 B ASN 231  ? A ASN 231  
232  1 Y 1 B ILE 232  ? A ILE 232  
233  1 Y 1 B THR 233  ? A THR 233  
234  1 Y 1 B ARG 234  ? A ARG 234  
235  1 Y 1 B PHE 235  ? A PHE 235  
236  1 Y 1 B GLN 236  ? A GLN 236  
237  1 Y 1 B THR 237  ? A THR 237  
238  1 Y 1 B LEU 238  ? A LEU 238  
239  1 Y 1 B LEU 239  ? A LEU 239  
240  1 Y 1 B ALA 240  ? A ALA 240  
241  1 Y 1 B LEU 241  ? A LEU 241  
242  1 Y 1 B ASN 242  ? A ASN 242  
243  1 Y 1 B ARG 243  ? A ARG 243  
244  1 Y 1 B SER 244  ? A SER 244  
245  1 Y 1 B TYR 245  ? A TYR 245  
246  1 Y 1 B LEU 246  ? A LEU 246  
247  1 Y 1 B THR 247  ? A THR 247  
248  1 Y 1 B PRO 248  ? A PRO 248  
249  1 Y 1 B GLY 249  ? A GLY 249  
250  1 Y 1 B ASP 250  ? A ASP 250  
251  1 Y 1 B SER 251  ? A SER 251  
252  1 Y 1 B SER 252  ? A SER 252  
253  1 Y 1 B SER 253  ? A SER 253  
254  1 Y 1 B GLY 254  ? A GLY 254  
255  1 Y 1 B TRP 255  ? A TRP 255  
256  1 Y 1 B THR 256  ? A THR 256  
257  1 Y 1 B ALA 257  ? A ALA 257  
258  1 Y 1 B GLY 258  ? A GLY 258  
259  1 Y 1 B ALA 259  ? A ALA 259  
260  1 Y 1 B ALA 260  ? A ALA 260  
261  1 Y 1 B ASP 261  ? A ASP 261  
262  1 Y 1 B TYR 262  ? A TYR 262  
263  1 Y 1 B TYR 263  ? A TYR 263  
264  1 Y 1 B VAL 264  ? A VAL 264  
265  1 Y 1 B GLY 265  ? A GLY 265  
266  1 Y 1 B TYR 266  ? A TYR 266  
267  1 Y 1 B LEU 267  ? A LEU 267  
268  1 Y 1 B GLN 268  ? A GLN 268  
269  1 Y 1 B PRO 269  ? A PRO 269  
270  1 Y 1 B ARG 270  ? A ARG 270  
271  1 Y 1 B THR 271  ? A THR 271  
272  1 Y 1 B PHE 272  ? A PHE 272  
273  1 Y 1 B LEU 273  ? A LEU 273  
274  1 Y 1 B LEU 274  ? A LEU 274  
275  1 Y 1 B LYS 275  ? A LYS 275  
276  1 Y 1 B TYR 276  ? A TYR 276  
277  1 Y 1 B ASN 277  ? A ASN 277  
278  1 Y 1 B GLU 278  ? A GLU 278  
279  1 Y 1 B ASN 279  ? A ASN 279  
280  1 Y 1 B GLY 280  ? A GLY 280  
281  1 Y 1 B THR 281  ? A THR 281  
282  1 Y 1 B ILE 282  ? A ILE 282  
283  1 Y 1 B THR 283  ? A THR 283  
284  1 Y 1 B ASP 284  ? A ASP 284  
285  1 Y 1 B ALA 285  ? A ALA 285  
286  1 Y 1 B VAL 286  ? A VAL 286  
287  1 Y 1 B ASP 287  ? A ASP 287  
288  1 Y 1 B CYS 288  ? A CYS 288  
289  1 Y 1 B ALA 289  ? A ALA 289  
290  1 Y 1 B LEU 290  ? A LEU 290  
291  1 Y 1 B ASP 291  ? A ASP 291  
292  1 Y 1 B PRO 292  ? A PRO 292  
293  1 Y 1 B LEU 293  ? A LEU 293  
294  1 Y 1 B SER 294  ? A SER 294  
295  1 Y 1 B GLU 295  ? A GLU 295  
296  1 Y 1 B THR 296  ? A THR 296  
297  1 Y 1 B LYS 297  ? A LYS 297  
298  1 Y 1 B CYS 298  ? A CYS 298  
299  1 Y 1 B THR 299  ? A THR 299  
300  1 Y 1 B LEU 300  ? A LEU 300  
301  1 Y 1 B LYS 301  ? A LYS 301  
302  1 Y 1 B SER 302  ? A SER 302  
303  1 Y 1 B PHE 303  ? A PHE 303  
304  1 Y 1 B THR 304  ? A THR 304  
305  1 Y 1 B VAL 305  ? A VAL 305  
306  1 Y 1 B GLU 306  ? A GLU 306  
307  1 Y 1 B LYS 307  ? A LYS 307  
308  1 Y 1 B GLY 308  ? A GLY 308  
309  1 Y 1 B ILE 309  ? A ILE 309  
310  1 Y 1 B TYR 310  ? A TYR 310  
311  1 Y 1 B GLN 311  ? A GLN 311  
312  1 Y 1 B THR 312  ? A THR 312  
313  1 Y 1 B SER 313  ? A SER 313  
314  1 Y 1 B ASN 314  ? A ASN 314  
315  1 Y 1 B PHE 315  ? A PHE 315  
316  1 Y 1 B ARG 316  ? A ARG 316  
317  1 Y 1 B VAL 317  ? A VAL 317  
318  1 Y 1 B GLN 318  ? A GLN 318  
319  1 Y 1 B PRO 319  ? A PRO 319  
320  1 Y 1 B THR 320  ? A THR 320  
321  1 Y 1 B GLU 321  ? A GLU 321  
322  1 Y 1 B SER 322  ? A SER 322  
323  1 Y 1 B ILE 323  ? A ILE 323  
324  1 Y 1 B VAL 324  ? A VAL 324  
325  1 Y 1 B ARG 325  ? A ARG 325  
326  1 Y 1 B SER 526  ? A SER 526  
327  1 Y 1 B THR 527  ? A THR 527  
328  1 Y 1 B ASN 528  ? A ASN 528  
329  1 Y 1 B LEU 529  ? A LEU 529  
330  1 Y 1 B VAL 530  ? A VAL 530  
331  1 Y 1 B LYS 531  ? A LYS 531  
332  1 Y 1 B ASN 532  ? A ASN 532  
333  1 Y 1 B LYS 533  ? A LYS 533  
334  1 Y 1 B CYS 534  ? A CYS 534  
335  1 Y 1 B VAL 535  ? A VAL 535  
336  1 Y 1 B ASN 536  ? A ASN 536  
337  1 Y 1 B PHE 537  ? A PHE 537  
338  1 Y 1 B ASN 538  ? A ASN 538  
339  1 Y 1 B PHE 539  ? A PHE 539  
340  1 Y 1 B ASN 540  ? A ASN 540  
341  1 Y 1 B GLY 541  ? A GLY 541  
342  1 Y 1 B LEU 542  ? A LEU 542  
343  1 Y 1 B THR 543  ? A THR 543  
344  1 Y 1 B GLY 544  ? A GLY 544  
345  1 Y 1 B THR 545  ? A THR 545  
346  1 Y 1 B GLY 546  ? A GLY 546  
347  1 Y 1 B VAL 547  ? A VAL 547  
348  1 Y 1 B LEU 548  ? A LEU 548  
349  1 Y 1 B THR 549  ? A THR 549  
350  1 Y 1 B LYS 550  ? A LYS 550  
351  1 Y 1 B SER 551  ? A SER 551  
352  1 Y 1 B ASN 552  ? A ASN 552  
353  1 Y 1 B LYS 553  ? A LYS 553  
354  1 Y 1 B LYS 554  ? A LYS 554  
355  1 Y 1 B PHE 555  ? A PHE 555  
356  1 Y 1 B LEU 556  ? A LEU 556  
357  1 Y 1 B PRO 557  ? A PRO 557  
358  1 Y 1 B PHE 558  ? A PHE 558  
359  1 Y 1 B GLN 559  ? A GLN 559  
360  1 Y 1 B GLN 560  ? A GLN 560  
361  1 Y 1 B PHE 561  ? A PHE 561  
362  1 Y 1 B GLY 562  ? A GLY 562  
363  1 Y 1 B ARG 563  ? A ARG 563  
364  1 Y 1 B ASP 564  ? A ASP 564  
365  1 Y 1 B ILE 565  ? A ILE 565  
366  1 Y 1 B VAL 566  ? A VAL 566  
367  1 Y 1 B ASP 567  ? A ASP 567  
368  1 Y 1 B THR 568  ? A THR 568  
369  1 Y 1 B THR 569  ? A THR 569  
370  1 Y 1 B ASP 570  ? A ASP 570  
371  1 Y 1 B ALA 571  ? A ALA 571  
372  1 Y 1 B VAL 572  ? A VAL 572  
373  1 Y 1 B ARG 573  ? A ARG 573  
374  1 Y 1 B ASP 574  ? A ASP 574  
375  1 Y 1 B PRO 575  ? A PRO 575  
376  1 Y 1 B GLN 576  ? A GLN 576  
377  1 Y 1 B THR 577  ? A THR 577  
378  1 Y 1 B LEU 578  ? A LEU 578  
379  1 Y 1 B GLU 579  ? A GLU 579  
380  1 Y 1 B ILE 580  ? A ILE 580  
381  1 Y 1 B LEU 581  ? A LEU 581  
382  1 Y 1 B ASP 582  ? A ASP 582  
383  1 Y 1 B ILE 583  ? A ILE 583  
384  1 Y 1 B THR 584  ? A THR 584  
385  1 Y 1 B PRO 585  ? A PRO 585  
386  1 Y 1 B CYS 586  ? A CYS 586  
387  1 Y 1 B SER 587  ? A SER 587  
388  1 Y 1 B PHE 588  ? A PHE 588  
389  1 Y 1 B GLY 589  ? A GLY 589  
390  1 Y 1 B GLY 590  ? A GLY 590  
391  1 Y 1 B VAL 591  ? A VAL 591  
392  1 Y 1 B SER 592  ? A SER 592  
393  1 Y 1 B VAL 593  ? A VAL 593  
394  1 Y 1 B ILE 594  ? A ILE 594  
395  1 Y 1 B THR 595  ? A THR 595  
396  1 Y 1 B PRO 596  ? A PRO 596  
397  1 Y 1 B GLY 597  ? A GLY 597  
398  1 Y 1 B THR 598  ? A THR 598  
399  1 Y 1 B ASN 599  ? A ASN 599  
400  1 Y 1 B THR 600  ? A THR 600  
401  1 Y 1 B SER 601  ? A SER 601  
402  1 Y 1 B ASN 602  ? A ASN 602  
403  1 Y 1 B GLN 603  ? A GLN 603  
404  1 Y 1 B VAL 604  ? A VAL 604  
405  1 Y 1 B ALA 605  ? A ALA 605  
406  1 Y 1 B VAL 606  ? A VAL 606  
407  1 Y 1 B LEU 607  ? A LEU 607  
408  1 Y 1 B TYR 608  ? A TYR 608  
409  1 Y 1 B GLN 609  ? A GLN 609  
410  1 Y 1 B GLY 610  ? A GLY 610  
411  1 Y 1 B VAL 611  ? A VAL 611  
412  1 Y 1 B ASN 612  ? A ASN 612  
413  1 Y 1 B CYS 613  ? A CYS 613  
414  1 Y 1 B THR 614  ? A THR 614  
415  1 Y 1 B GLU 615  ? A GLU 615  
416  1 Y 1 B VAL 616  ? A VAL 616  
417  1 Y 1 B SER 617  ? A SER 617  
418  1 Y 1 B VAL 618  ? A VAL 618  
419  1 Y 1 B ALA 619  ? A ALA 619  
420  1 Y 1 B ILE 620  ? A ILE 620  
421  1 Y 1 B HIS 621  ? A HIS 621  
422  1 Y 1 B ALA 622  ? A ALA 622  
423  1 Y 1 B ASP 623  ? A ASP 623  
424  1 Y 1 B GLN 624  ? A GLN 624  
425  1 Y 1 B LEU 625  ? A LEU 625  
426  1 Y 1 B THR 626  ? A THR 626  
427  1 Y 1 B PRO 627  ? A PRO 627  
428  1 Y 1 B THR 628  ? A THR 628  
429  1 Y 1 B TRP 629  ? A TRP 629  
430  1 Y 1 B ARG 630  ? A ARG 630  
431  1 Y 1 B VAL 631  ? A VAL 631  
432  1 Y 1 B TYR 632  ? A TYR 632  
433  1 Y 1 B SER 633  ? A SER 633  
434  1 Y 1 B THR 634  ? A THR 634  
435  1 Y 1 B GLY 635  ? A GLY 635  
436  1 Y 1 B SER 636  ? A SER 636  
437  1 Y 1 B ASN 637  ? A ASN 637  
438  1 Y 1 B VAL 638  ? A VAL 638  
439  1 Y 1 B PHE 639  ? A PHE 639  
440  1 Y 1 B GLN 640  ? A GLN 640  
441  1 Y 1 B THR 641  ? A THR 641  
442  1 Y 1 B ARG 642  ? A ARG 642  
443  1 Y 1 B ALA 643  ? A ALA 643  
444  1 Y 1 B GLY 644  ? A GLY 644  
445  1 Y 1 B CYS 645  ? A CYS 645  
446  1 Y 1 B LEU 646  ? A LEU 646  
447  1 Y 1 B ILE 647  ? A ILE 647  
448  1 Y 1 B GLY 648  ? A GLY 648  
449  1 Y 1 B ALA 649  ? A ALA 649  
450  1 Y 1 B GLU 650  ? A GLU 650  
451  1 Y 1 B TYR 651  ? A TYR 651  
452  1 Y 1 B VAL 652  ? A VAL 652  
453  1 Y 1 B ASN 653  ? A ASN 653  
454  1 Y 1 B ASN 654  ? A ASN 654  
455  1 Y 1 B SER 655  ? A SER 655  
456  1 Y 1 B TYR 656  ? A TYR 656  
457  1 Y 1 B GLU 657  ? A GLU 657  
458  1 Y 1 B CYS 658  ? A CYS 658  
459  1 Y 1 B ASP 659  ? A ASP 659  
460  1 Y 1 B ILE 660  ? A ILE 660  
461  1 Y 1 B PRO 661  ? A PRO 661  
462  1 Y 1 B ILE 662  ? A ILE 662  
463  1 Y 1 B GLY 663  ? A GLY 663  
464  1 Y 1 B ALA 664  ? A ALA 664  
465  1 Y 1 B GLY 665  ? A GLY 665  
466  1 Y 1 B ILE 666  ? A ILE 666  
467  1 Y 1 B CYS 667  ? A CYS 667  
468  1 Y 1 B ALA 668  ? A ALA 668  
469  1 Y 1 B SER 669  ? A SER 669  
470  1 Y 1 B TYR 670  ? A TYR 670  
471  1 Y 1 B GLN 671  ? A GLN 671  
472  1 Y 1 B THR 672  ? A THR 672  
473  1 Y 1 B GLN 673  ? A GLN 673  
474  1 Y 1 B THR 674  ? A THR 674  
475  1 Y 1 B LYS 675  ? A LYS 675  
476  1 Y 1 B SER 676  ? A SER 676  
477  1 Y 1 B ARG 677  ? A ARG 677  
478  1 Y 1 B ALA 678  ? A ALA 678  
479  1 Y 1 B GLY 679  ? A GLY 679  
480  1 Y 1 B ALA 680  ? A ALA 680  
481  1 Y 1 B ARG 681  ? A ARG 681  
482  1 Y 1 B SER 682  ? A SER 682  
483  1 Y 1 B VAL 683  ? A VAL 683  
484  1 Y 1 B ALA 684  ? A ALA 684  
485  1 Y 1 B SER 685  ? A SER 685  
486  1 Y 1 B GLN 686  ? A GLN 686  
487  1 Y 1 B SER 687  ? A SER 687  
488  1 Y 1 B ILE 688  ? A ILE 688  
489  1 Y 1 B ILE 689  ? A ILE 689  
490  1 Y 1 B ALA 690  ? A ALA 690  
491  1 Y 1 B TYR 691  ? A TYR 691  
492  1 Y 1 B THR 692  ? A THR 692  
493  1 Y 1 B MET 693  ? A MET 693  
494  1 Y 1 B SER 694  ? A SER 694  
495  1 Y 1 B LEU 695  ? A LEU 695  
496  1 Y 1 B GLY 696  ? A GLY 696  
497  1 Y 1 B ALA 697  ? A ALA 697  
498  1 Y 1 B GLU 698  ? A GLU 698  
499  1 Y 1 B ASN 699  ? A ASN 699  
500  1 Y 1 B SER 700  ? A SER 700  
501  1 Y 1 B VAL 701  ? A VAL 701  
502  1 Y 1 B ALA 702  ? A ALA 702  
503  1 Y 1 B TYR 703  ? A TYR 703  
504  1 Y 1 B SER 704  ? A SER 704  
505  1 Y 1 B ASN 705  ? A ASN 705  
506  1 Y 1 B ASN 706  ? A ASN 706  
507  1 Y 1 B SER 707  ? A SER 707  
508  1 Y 1 B ILE 708  ? A ILE 708  
509  1 Y 1 B ALA 709  ? A ALA 709  
510  1 Y 1 B ILE 710  ? A ILE 710  
511  1 Y 1 B PRO 711  ? A PRO 711  
512  1 Y 1 B THR 712  ? A THR 712  
513  1 Y 1 B ASN 713  ? A ASN 713  
514  1 Y 1 B PHE 714  ? A PHE 714  
515  1 Y 1 B THR 715  ? A THR 715  
516  1 Y 1 B ILE 716  ? A ILE 716  
517  1 Y 1 B SER 717  ? A SER 717  
518  1 Y 1 B VAL 718  ? A VAL 718  
519  1 Y 1 B THR 719  ? A THR 719  
520  1 Y 1 B THR 720  ? A THR 720  
521  1 Y 1 B GLU 721  ? A GLU 721  
522  1 Y 1 B ILE 722  ? A ILE 722  
523  1 Y 1 B LEU 723  ? A LEU 723  
524  1 Y 1 B PRO 724  ? A PRO 724  
525  1 Y 1 B VAL 725  ? A VAL 725  
526  1 Y 1 B SER 726  ? A SER 726  
527  1 Y 1 B MET 727  ? A MET 727  
528  1 Y 1 B THR 728  ? A THR 728  
529  1 Y 1 B LYS 729  ? A LYS 729  
530  1 Y 1 B THR 730  ? A THR 730  
531  1 Y 1 B SER 731  ? A SER 731  
532  1 Y 1 B VAL 732  ? A VAL 732  
533  1 Y 1 B ASP 733  ? A ASP 733  
534  1 Y 1 B CYS 734  ? A CYS 734  
535  1 Y 1 B THR 735  ? A THR 735  
536  1 Y 1 B MET 736  ? A MET 736  
537  1 Y 1 B TYR 737  ? A TYR 737  
538  1 Y 1 B ILE 738  ? A ILE 738  
539  1 Y 1 B CYS 739  ? A CYS 739  
540  1 Y 1 B GLY 740  ? A GLY 740  
541  1 Y 1 B ASP 741  ? A ASP 741  
542  1 Y 1 B SER 742  ? A SER 742  
543  1 Y 1 B THR 743  ? A THR 743  
544  1 Y 1 B GLU 744  ? A GLU 744  
545  1 Y 1 B CYS 745  ? A CYS 745  
546  1 Y 1 B SER 746  ? A SER 746  
547  1 Y 1 B ASN 747  ? A ASN 747  
548  1 Y 1 B LEU 748  ? A LEU 748  
549  1 Y 1 B LEU 749  ? A LEU 749  
550  1 Y 1 B LEU 750  ? A LEU 750  
551  1 Y 1 B GLN 751  ? A GLN 751  
552  1 Y 1 B TYR 752  ? A TYR 752  
553  1 Y 1 B GLY 753  ? A GLY 753  
554  1 Y 1 B SER 754  ? A SER 754  
555  1 Y 1 B PHE 755  ? A PHE 755  
556  1 Y 1 B CYS 756  ? A CYS 756  
557  1 Y 1 B THR 757  ? A THR 757  
558  1 Y 1 B GLN 758  ? A GLN 758  
559  1 Y 1 B LEU 759  ? A LEU 759  
560  1 Y 1 B LYS 760  ? A LYS 760  
561  1 Y 1 B ARG 761  ? A ARG 761  
562  1 Y 1 B ALA 762  ? A ALA 762  
563  1 Y 1 B LEU 763  ? A LEU 763  
564  1 Y 1 B THR 764  ? A THR 764  
565  1 Y 1 B GLY 765  ? A GLY 765  
566  1 Y 1 B ILE 766  ? A ILE 766  
567  1 Y 1 B ALA 767  ? A ALA 767  
568  1 Y 1 B VAL 768  ? A VAL 768  
569  1 Y 1 B GLU 769  ? A GLU 769  
570  1 Y 1 B GLN 770  ? A GLN 770  
571  1 Y 1 B ASP 771  ? A ASP 771  
572  1 Y 1 B LYS 772  ? A LYS 772  
573  1 Y 1 B ASN 773  ? A ASN 773  
574  1 Y 1 B THR 774  ? A THR 774  
575  1 Y 1 B GLN 775  ? A GLN 775  
576  1 Y 1 B GLU 776  ? A GLU 776  
577  1 Y 1 B VAL 777  ? A VAL 777  
578  1 Y 1 B PHE 778  ? A PHE 778  
579  1 Y 1 B ALA 779  ? A ALA 779  
580  1 Y 1 B GLN 780  ? A GLN 780  
581  1 Y 1 B VAL 781  ? A VAL 781  
582  1 Y 1 B LYS 782  ? A LYS 782  
583  1 Y 1 B GLN 783  ? A GLN 783  
584  1 Y 1 B ILE 784  ? A ILE 784  
585  1 Y 1 B TYR 785  ? A TYR 785  
586  1 Y 1 B LYS 786  ? A LYS 786  
587  1 Y 1 B THR 787  ? A THR 787  
588  1 Y 1 B PRO 788  ? A PRO 788  
589  1 Y 1 B PRO 789  ? A PRO 789  
590  1 Y 1 B ILE 790  ? A ILE 790  
591  1 Y 1 B LYS 791  ? A LYS 791  
592  1 Y 1 B TYR 792  ? A TYR 792  
593  1 Y 1 B PHE 793  ? A PHE 793  
594  1 Y 1 B GLY 794  ? A GLY 794  
595  1 Y 1 B GLY 795  ? A GLY 795  
596  1 Y 1 B PHE 796  ? A PHE 796  
597  1 Y 1 B ASN 797  ? A ASN 797  
598  1 Y 1 B PHE 798  ? A PHE 798  
599  1 Y 1 B SER 799  ? A SER 799  
600  1 Y 1 B GLN 800  ? A GLN 800  
601  1 Y 1 B ILE 801  ? A ILE 801  
602  1 Y 1 B LEU 802  ? A LEU 802  
603  1 Y 1 B PRO 803  ? A PRO 803  
604  1 Y 1 B ASP 804  ? A ASP 804  
605  1 Y 1 B PRO 805  ? A PRO 805  
606  1 Y 1 B SER 806  ? A SER 806  
607  1 Y 1 B LYS 807  ? A LYS 807  
608  1 Y 1 B PRO 808  ? A PRO 808  
609  1 Y 1 B SER 809  ? A SER 809  
610  1 Y 1 B LYS 810  ? A LYS 810  
611  1 Y 1 B ARG 811  ? A ARG 811  
612  1 Y 1 B SER 812  ? A SER 812  
613  1 Y 1 B PRO 813  ? A PRO 813  
614  1 Y 1 B ILE 814  ? A ILE 814  
615  1 Y 1 B GLU 815  ? A GLU 815  
616  1 Y 1 B ASP 816  ? A ASP 816  
617  1 Y 1 B LEU 817  ? A LEU 817  
618  1 Y 1 B LEU 818  ? A LEU 818  
619  1 Y 1 B PHE 819  ? A PHE 819  
620  1 Y 1 B ASN 820  ? A ASN 820  
621  1 Y 1 B LYS 821  ? A LYS 821  
622  1 Y 1 B VAL 822  ? A VAL 822  
623  1 Y 1 B THR 823  ? A THR 823  
624  1 Y 1 B LEU 824  ? A LEU 824  
625  1 Y 1 B ALA 825  ? A ALA 825  
626  1 Y 1 B ASP 826  ? A ASP 826  
627  1 Y 1 B ALA 827  ? A ALA 827  
628  1 Y 1 B GLY 828  ? A GLY 828  
629  1 Y 1 B PHE 829  ? A PHE 829  
630  1 Y 1 B ILE 830  ? A ILE 830  
631  1 Y 1 B LYS 831  ? A LYS 831  
632  1 Y 1 B GLN 832  ? A GLN 832  
633  1 Y 1 B TYR 833  ? A TYR 833  
634  1 Y 1 B GLY 834  ? A GLY 834  
635  1 Y 1 B ASP 835  ? A ASP 835  
636  1 Y 1 B CYS 836  ? A CYS 836  
637  1 Y 1 B LEU 837  ? A LEU 837  
638  1 Y 1 B GLY 838  ? A GLY 838  
639  1 Y 1 B ASP 839  ? A ASP 839  
640  1 Y 1 B ILE 840  ? A ILE 840  
641  1 Y 1 B ALA 841  ? A ALA 841  
642  1 Y 1 B ALA 842  ? A ALA 842  
643  1 Y 1 B ARG 843  ? A ARG 843  
644  1 Y 1 B ASP 844  ? A ASP 844  
645  1 Y 1 B LEU 845  ? A LEU 845  
646  1 Y 1 B ILE 846  ? A ILE 846  
647  1 Y 1 B CYS 847  ? A CYS 847  
648  1 Y 1 B ALA 848  ? A ALA 848  
649  1 Y 1 B GLN 849  ? A GLN 849  
650  1 Y 1 B LYS 850  ? A LYS 850  
651  1 Y 1 B PHE 851  ? A PHE 851  
652  1 Y 1 B ASN 852  ? A ASN 852  
653  1 Y 1 B GLY 853  ? A GLY 853  
654  1 Y 1 B LEU 854  ? A LEU 854  
655  1 Y 1 B THR 855  ? A THR 855  
656  1 Y 1 B VAL 856  ? A VAL 856  
657  1 Y 1 B LEU 857  ? A LEU 857  
658  1 Y 1 B PRO 858  ? A PRO 858  
659  1 Y 1 B PRO 859  ? A PRO 859  
660  1 Y 1 B LEU 860  ? A LEU 860  
661  1 Y 1 B LEU 861  ? A LEU 861  
662  1 Y 1 B THR 862  ? A THR 862  
663  1 Y 1 B ASP 863  ? A ASP 863  
664  1 Y 1 B GLU 864  ? A GLU 864  
665  1 Y 1 B MET 865  ? A MET 865  
666  1 Y 1 B ILE 866  ? A ILE 866  
667  1 Y 1 B ALA 867  ? A ALA 867  
668  1 Y 1 B GLN 868  ? A GLN 868  
669  1 Y 1 B TYR 869  ? A TYR 869  
670  1 Y 1 B THR 870  ? A THR 870  
671  1 Y 1 B SER 871  ? A SER 871  
672  1 Y 1 B ALA 872  ? A ALA 872  
673  1 Y 1 B LEU 873  ? A LEU 873  
674  1 Y 1 B LEU 874  ? A LEU 874  
675  1 Y 1 B ALA 875  ? A ALA 875  
676  1 Y 1 B GLY 876  ? A GLY 876  
677  1 Y 1 B THR 877  ? A THR 877  
678  1 Y 1 B ILE 878  ? A ILE 878  
679  1 Y 1 B THR 879  ? A THR 879  
680  1 Y 1 B SER 880  ? A SER 880  
681  1 Y 1 B GLY 881  ? A GLY 881  
682  1 Y 1 B TRP 882  ? A TRP 882  
683  1 Y 1 B THR 883  ? A THR 883  
684  1 Y 1 B PHE 884  ? A PHE 884  
685  1 Y 1 B GLY 885  ? A GLY 885  
686  1 Y 1 B ALA 886  ? A ALA 886  
687  1 Y 1 B GLY 887  ? A GLY 887  
688  1 Y 1 B PRO 888  ? A PRO 888  
689  1 Y 1 B ALA 889  ? A ALA 889  
690  1 Y 1 B LEU 890  ? A LEU 890  
691  1 Y 1 B GLN 891  ? A GLN 891  
692  1 Y 1 B ILE 892  ? A ILE 892  
693  1 Y 1 B PRO 893  ? A PRO 893  
694  1 Y 1 B PHE 894  ? A PHE 894  
695  1 Y 1 B PRO 895  ? A PRO 895  
696  1 Y 1 B MET 896  ? A MET 896  
697  1 Y 1 B GLN 897  ? A GLN 897  
698  1 Y 1 B MET 898  ? A MET 898  
699  1 Y 1 B ALA 899  ? A ALA 899  
700  1 Y 1 B TYR 900  ? A TYR 900  
701  1 Y 1 B ARG 901  ? A ARG 901  
702  1 Y 1 B PHE 902  ? A PHE 902  
703  1 Y 1 B ASN 903  ? A ASN 903  
704  1 Y 1 B GLY 904  ? A GLY 904  
705  1 Y 1 B ILE 905  ? A ILE 905  
706  1 Y 1 B GLY 906  ? A GLY 906  
707  1 Y 1 B VAL 907  ? A VAL 907  
708  1 Y 1 B THR 908  ? A THR 908  
709  1 Y 1 B GLN 909  ? A GLN 909  
710  1 Y 1 B ASN 910  ? A ASN 910  
711  1 Y 1 B VAL 911  ? A VAL 911  
712  1 Y 1 B LEU 912  ? A LEU 912  
713  1 Y 1 B TYR 913  ? A TYR 913  
714  1 Y 1 B GLU 914  ? A GLU 914  
715  1 Y 1 B ASN 915  ? A ASN 915  
716  1 Y 1 B GLN 916  ? A GLN 916  
717  1 Y 1 B LYS 917  ? A LYS 917  
718  1 Y 1 B LEU 918  ? A LEU 918  
719  1 Y 1 B ILE 919  ? A ILE 919  
720  1 Y 1 B ALA 920  ? A ALA 920  
721  1 Y 1 B ASN 921  ? A ASN 921  
722  1 Y 1 B GLN 922  ? A GLN 922  
723  1 Y 1 B PHE 923  ? A PHE 923  
724  1 Y 1 B ASN 924  ? A ASN 924  
725  1 Y 1 B SER 925  ? A SER 925  
726  1 Y 1 B ALA 926  ? A ALA 926  
727  1 Y 1 B ILE 927  ? A ILE 927  
728  1 Y 1 B GLY 928  ? A GLY 928  
729  1 Y 1 B LYS 929  ? A LYS 929  
730  1 Y 1 B ILE 930  ? A ILE 930  
731  1 Y 1 B GLN 931  ? A GLN 931  
732  1 Y 1 B ASP 932  ? A ASP 932  
733  1 Y 1 B SER 933  ? A SER 933  
734  1 Y 1 B LEU 934  ? A LEU 934  
735  1 Y 1 B PHE 935  ? A PHE 935  
736  1 Y 1 B SER 936  ? A SER 936  
737  1 Y 1 B THR 937  ? A THR 937  
738  1 Y 1 B PRO 938  ? A PRO 938  
739  1 Y 1 B SER 939  ? A SER 939  
740  1 Y 1 B ALA 940  ? A ALA 940  
741  1 Y 1 B LEU 941  ? A LEU 941  
742  1 Y 1 B GLY 942  ? A GLY 942  
743  1 Y 1 B LYS 943  ? A LYS 943  
744  1 Y 1 B LEU 944  ? A LEU 944  
745  1 Y 1 B GLN 945  ? A GLN 945  
746  1 Y 1 B ASP 946  ? A ASP 946  
747  1 Y 1 B VAL 947  ? A VAL 947  
748  1 Y 1 B VAL 948  ? A VAL 948  
749  1 Y 1 B ASN 949  ? A ASN 949  
750  1 Y 1 B HIS 950  ? A HIS 950  
751  1 Y 1 B ASN 951  ? A ASN 951  
752  1 Y 1 B ALA 952  ? A ALA 952  
753  1 Y 1 B GLN 953  ? A GLN 953  
754  1 Y 1 B ALA 954  ? A ALA 954  
755  1 Y 1 B LEU 955  ? A LEU 955  
756  1 Y 1 B ASN 956  ? A ASN 956  
757  1 Y 1 B THR 957  ? A THR 957  
758  1 Y 1 B LEU 958  ? A LEU 958  
759  1 Y 1 B VAL 959  ? A VAL 959  
760  1 Y 1 B LYS 960  ? A LYS 960  
761  1 Y 1 B GLN 961  ? A GLN 961  
762  1 Y 1 B LEU 962  ? A LEU 962  
763  1 Y 1 B SER 963  ? A SER 963  
764  1 Y 1 B SER 964  ? A SER 964  
765  1 Y 1 B LYS 965  ? A LYS 965  
766  1 Y 1 B PHE 966  ? A PHE 966  
767  1 Y 1 B GLY 967  ? A GLY 967  
768  1 Y 1 B ALA 968  ? A ALA 968  
769  1 Y 1 B ILE 969  ? A ILE 969  
770  1 Y 1 B SER 970  ? A SER 970  
771  1 Y 1 B SER 971  ? A SER 971  
772  1 Y 1 B VAL 972  ? A VAL 972  
773  1 Y 1 B LEU 973  ? A LEU 973  
774  1 Y 1 B ASN 974  ? A ASN 974  
775  1 Y 1 B ASP 975  ? A ASP 975  
776  1 Y 1 B ILE 976  ? A ILE 976  
777  1 Y 1 B LEU 977  ? A LEU 977  
778  1 Y 1 B SER 978  ? A SER 978  
779  1 Y 1 B ARG 979  ? A ARG 979  
780  1 Y 1 B LEU 980  ? A LEU 980  
781  1 Y 1 B ASP 981  ? A ASP 981  
782  1 Y 1 B PRO 982  ? A PRO 982  
783  1 Y 1 B PRO 983  ? A PRO 983  
784  1 Y 1 B GLU 984  ? A GLU 984  
785  1 Y 1 B ALA 985  ? A ALA 985  
786  1 Y 1 B GLU 986  ? A GLU 986  
787  1 Y 1 B VAL 987  ? A VAL 987  
788  1 Y 1 B GLN 988  ? A GLN 988  
789  1 Y 1 B ILE 989  ? A ILE 989  
790  1 Y 1 B ASP 990  ? A ASP 990  
791  1 Y 1 B ARG 991  ? A ARG 991  
792  1 Y 1 B LEU 992  ? A LEU 992  
793  1 Y 1 B ILE 993  ? A ILE 993  
794  1 Y 1 B THR 994  ? A THR 994  
795  1 Y 1 B GLY 995  ? A GLY 995  
796  1 Y 1 B ARG 996  ? A ARG 996  
797  1 Y 1 B LEU 997  ? A LEU 997  
798  1 Y 1 B GLN 998  ? A GLN 998  
799  1 Y 1 B SER 999  ? A SER 999  
800  1 Y 1 B LEU 1000 ? A LEU 1000 
801  1 Y 1 B GLN 1001 ? A GLN 1001 
802  1 Y 1 B THR 1002 ? A THR 1002 
803  1 Y 1 B TYR 1003 ? A TYR 1003 
804  1 Y 1 B VAL 1004 ? A VAL 1004 
805  1 Y 1 B THR 1005 ? A THR 1005 
806  1 Y 1 B GLN 1006 ? A GLN 1006 
807  1 Y 1 B GLN 1007 ? A GLN 1007 
808  1 Y 1 B LEU 1008 ? A LEU 1008 
809  1 Y 1 B ILE 1009 ? A ILE 1009 
810  1 Y 1 B ARG 1010 ? A ARG 1010 
811  1 Y 1 B ALA 1011 ? A ALA 1011 
812  1 Y 1 B ALA 1012 ? A ALA 1012 
813  1 Y 1 B GLU 1013 ? A GLU 1013 
814  1 Y 1 B ILE 1014 ? A ILE 1014 
815  1 Y 1 B ARG 1015 ? A ARG 1015 
816  1 Y 1 B ALA 1016 ? A ALA 1016 
817  1 Y 1 B SER 1017 ? A SER 1017 
818  1 Y 1 B ALA 1018 ? A ALA 1018 
819  1 Y 1 B ASN 1019 ? A ASN 1019 
820  1 Y 1 B LEU 1020 ? A LEU 1020 
821  1 Y 1 B ALA 1021 ? A ALA 1021 
822  1 Y 1 B ALA 1022 ? A ALA 1022 
823  1 Y 1 B THR 1023 ? A THR 1023 
824  1 Y 1 B LYS 1024 ? A LYS 1024 
825  1 Y 1 B MET 1025 ? A MET 1025 
826  1 Y 1 B SER 1026 ? A SER 1026 
827  1 Y 1 B GLU 1027 ? A GLU 1027 
828  1 Y 1 B CYS 1028 ? A CYS 1028 
829  1 Y 1 B VAL 1029 ? A VAL 1029 
830  1 Y 1 B LEU 1030 ? A LEU 1030 
831  1 Y 1 B GLY 1031 ? A GLY 1031 
832  1 Y 1 B GLN 1032 ? A GLN 1032 
833  1 Y 1 B SER 1033 ? A SER 1033 
834  1 Y 1 B LYS 1034 ? A LYS 1034 
835  1 Y 1 B ARG 1035 ? A ARG 1035 
836  1 Y 1 B VAL 1036 ? A VAL 1036 
837  1 Y 1 B ASP 1037 ? A ASP 1037 
838  1 Y 1 B PHE 1038 ? A PHE 1038 
839  1 Y 1 B CYS 1039 ? A CYS 1039 
840  1 Y 1 B GLY 1040 ? A GLY 1040 
841  1 Y 1 B LYS 1041 ? A LYS 1041 
842  1 Y 1 B GLY 1042 ? A GLY 1042 
843  1 Y 1 B TYR 1043 ? A TYR 1043 
844  1 Y 1 B HIS 1044 ? A HIS 1044 
845  1 Y 1 B LEU 1045 ? A LEU 1045 
846  1 Y 1 B MET 1046 ? A MET 1046 
847  1 Y 1 B SER 1047 ? A SER 1047 
848  1 Y 1 B PHE 1048 ? A PHE 1048 
849  1 Y 1 B PRO 1049 ? A PRO 1049 
850  1 Y 1 B GLN 1050 ? A GLN 1050 
851  1 Y 1 B SER 1051 ? A SER 1051 
852  1 Y 1 B ALA 1052 ? A ALA 1052 
853  1 Y 1 B PRO 1053 ? A PRO 1053 
854  1 Y 1 B HIS 1054 ? A HIS 1054 
855  1 Y 1 B GLY 1055 ? A GLY 1055 
856  1 Y 1 B VAL 1056 ? A VAL 1056 
857  1 Y 1 B VAL 1057 ? A VAL 1057 
858  1 Y 1 B PHE 1058 ? A PHE 1058 
859  1 Y 1 B LEU 1059 ? A LEU 1059 
860  1 Y 1 B HIS 1060 ? A HIS 1060 
861  1 Y 1 B VAL 1061 ? A VAL 1061 
862  1 Y 1 B THR 1062 ? A THR 1062 
863  1 Y 1 B TYR 1063 ? A TYR 1063 
864  1 Y 1 B VAL 1064 ? A VAL 1064 
865  1 Y 1 B PRO 1065 ? A PRO 1065 
866  1 Y 1 B ALA 1066 ? A ALA 1066 
867  1 Y 1 B GLN 1067 ? A GLN 1067 
868  1 Y 1 B GLU 1068 ? A GLU 1068 
869  1 Y 1 B LYS 1069 ? A LYS 1069 
870  1 Y 1 B ASN 1070 ? A ASN 1070 
871  1 Y 1 B PHE 1071 ? A PHE 1071 
872  1 Y 1 B THR 1072 ? A THR 1072 
873  1 Y 1 B THR 1073 ? A THR 1073 
874  1 Y 1 B ALA 1074 ? A ALA 1074 
875  1 Y 1 B PRO 1075 ? A PRO 1075 
876  1 Y 1 B ALA 1076 ? A ALA 1076 
877  1 Y 1 B ILE 1077 ? A ILE 1077 
878  1 Y 1 B CYS 1078 ? A CYS 1078 
879  1 Y 1 B HIS 1079 ? A HIS 1079 
880  1 Y 1 B ASP 1080 ? A ASP 1080 
881  1 Y 1 B GLY 1081 ? A GLY 1081 
882  1 Y 1 B LYS 1082 ? A LYS 1082 
883  1 Y 1 B ALA 1083 ? A ALA 1083 
884  1 Y 1 B HIS 1084 ? A HIS 1084 
885  1 Y 1 B PHE 1085 ? A PHE 1085 
886  1 Y 1 B PRO 1086 ? A PRO 1086 
887  1 Y 1 B ARG 1087 ? A ARG 1087 
888  1 Y 1 B GLU 1088 ? A GLU 1088 
889  1 Y 1 B GLY 1089 ? A GLY 1089 
890  1 Y 1 B VAL 1090 ? A VAL 1090 
891  1 Y 1 B PHE 1091 ? A PHE 1091 
892  1 Y 1 B VAL 1092 ? A VAL 1092 
893  1 Y 1 B SER 1093 ? A SER 1093 
894  1 Y 1 B ASN 1094 ? A ASN 1094 
895  1 Y 1 B GLY 1095 ? A GLY 1095 
896  1 Y 1 B THR 1096 ? A THR 1096 
897  1 Y 1 B HIS 1097 ? A HIS 1097 
898  1 Y 1 B TRP 1098 ? A TRP 1098 
899  1 Y 1 B PHE 1099 ? A PHE 1099 
900  1 Y 1 B VAL 1100 ? A VAL 1100 
901  1 Y 1 B THR 1101 ? A THR 1101 
902  1 Y 1 B GLN 1102 ? A GLN 1102 
903  1 Y 1 B ARG 1103 ? A ARG 1103 
904  1 Y 1 B ASN 1104 ? A ASN 1104 
905  1 Y 1 B PHE 1105 ? A PHE 1105 
906  1 Y 1 B TYR 1106 ? A TYR 1106 
907  1 Y 1 B GLU 1107 ? A GLU 1107 
908  1 Y 1 B PRO 1108 ? A PRO 1108 
909  1 Y 1 B GLN 1109 ? A GLN 1109 
910  1 Y 1 B ILE 1110 ? A ILE 1110 
911  1 Y 1 B ILE 1111 ? A ILE 1111 
912  1 Y 1 B THR 1112 ? A THR 1112 
913  1 Y 1 B THR 1113 ? A THR 1113 
914  1 Y 1 B ASP 1114 ? A ASP 1114 
915  1 Y 1 B ASN 1115 ? A ASN 1115 
916  1 Y 1 B THR 1116 ? A THR 1116 
917  1 Y 1 B PHE 1117 ? A PHE 1117 
918  1 Y 1 B VAL 1118 ? A VAL 1118 
919  1 Y 1 B SER 1119 ? A SER 1119 
920  1 Y 1 B GLY 1120 ? A GLY 1120 
921  1 Y 1 B ASN 1121 ? A ASN 1121 
922  1 Y 1 B CYS 1122 ? A CYS 1122 
923  1 Y 1 B ASP 1123 ? A ASP 1123 
924  1 Y 1 B VAL 1124 ? A VAL 1124 
925  1 Y 1 B VAL 1125 ? A VAL 1125 
926  1 Y 1 B ILE 1126 ? A ILE 1126 
927  1 Y 1 B GLY 1127 ? A GLY 1127 
928  1 Y 1 B ILE 1128 ? A ILE 1128 
929  1 Y 1 B VAL 1129 ? A VAL 1129 
930  1 Y 1 B ASN 1130 ? A ASN 1130 
931  1 Y 1 B ASN 1131 ? A ASN 1131 
932  1 Y 1 B THR 1132 ? A THR 1132 
933  1 Y 1 B VAL 1133 ? A VAL 1133 
934  1 Y 1 B TYR 1134 ? A TYR 1134 
935  1 Y 1 B ASP 1135 ? A ASP 1135 
936  1 Y 1 B PRO 1136 ? A PRO 1136 
937  1 Y 1 B LEU 1137 ? A LEU 1137 
938  1 Y 1 B GLN 1138 ? A GLN 1138 
939  1 Y 1 B LEU 1139 ? A LEU 1139 
940  1 Y 1 B GLU 1140 ? A GLU 1140 
941  1 Y 1 B LEU 1141 ? A LEU 1141 
942  1 Y 1 B ASP 1142 ? A ASP 1142 
943  1 Y 1 B SER 1143 ? A SER 1143 
944  1 Y 1 B PHE 1144 ? A PHE 1144 
945  1 Y 1 B LYS 1145 ? A LYS 1145 
946  1 Y 1 B GLU 1146 ? A GLU 1146 
947  1 Y 1 B GLU 1147 ? A GLU 1147 
948  1 Y 1 B LEU 1148 ? A LEU 1148 
949  1 Y 1 B ASP 1149 ? A ASP 1149 
950  1 Y 1 B LYS 1150 ? A LYS 1150 
951  1 Y 1 B TYR 1151 ? A TYR 1151 
952  1 Y 1 B PHE 1152 ? A PHE 1152 
953  1 Y 1 B LYS 1153 ? A LYS 1153 
954  1 Y 1 B ASN 1154 ? A ASN 1154 
955  1 Y 1 B HIS 1155 ? A HIS 1155 
956  1 Y 1 B THR 1156 ? A THR 1156 
957  1 Y 1 B SER 1157 ? A SER 1157 
958  1 Y 1 B PRO 1158 ? A PRO 1158 
959  1 Y 1 B ASP 1159 ? A ASP 1159 
960  1 Y 1 B VAL 1160 ? A VAL 1160 
961  1 Y 1 B ASP 1161 ? A ASP 1161 
962  1 Y 1 B LEU 1162 ? A LEU 1162 
963  1 Y 1 B GLY 1163 ? A GLY 1163 
964  1 Y 1 B ASP 1164 ? A ASP 1164 
965  1 Y 1 B ILE 1165 ? A ILE 1165 
966  1 Y 1 B SER 1166 ? A SER 1166 
967  1 Y 1 B GLY 1167 ? A GLY 1167 
968  1 Y 1 B ILE 1168 ? A ILE 1168 
969  1 Y 1 B ASN 1169 ? A ASN 1169 
970  1 Y 1 B ALA 1170 ? A ALA 1170 
971  1 Y 1 B SER 1171 ? A SER 1171 
972  1 Y 1 B VAL 1172 ? A VAL 1172 
973  1 Y 1 B VAL 1173 ? A VAL 1173 
974  1 Y 1 B ASN 1174 ? A ASN 1174 
975  1 Y 1 B ILE 1175 ? A ILE 1175 
976  1 Y 1 B GLN 1176 ? A GLN 1176 
977  1 Y 1 B LYS 1177 ? A LYS 1177 
978  1 Y 1 B GLU 1178 ? A GLU 1178 
979  1 Y 1 B ILE 1179 ? A ILE 1179 
980  1 Y 1 B ASP 1180 ? A ASP 1180 
981  1 Y 1 B ARG 1181 ? A ARG 1181 
982  1 Y 1 B LEU 1182 ? A LEU 1182 
983  1 Y 1 B ASN 1183 ? A ASN 1183 
984  1 Y 1 B GLU 1184 ? A GLU 1184 
985  1 Y 1 B VAL 1185 ? A VAL 1185 
986  1 Y 1 B ALA 1186 ? A ALA 1186 
987  1 Y 1 B LYS 1187 ? A LYS 1187 
988  1 Y 1 B ASN 1188 ? A ASN 1188 
989  1 Y 1 B LEU 1189 ? A LEU 1189 
990  1 Y 1 B ASN 1190 ? A ASN 1190 
991  1 Y 1 B GLU 1191 ? A GLU 1191 
992  1 Y 1 B SER 1192 ? A SER 1192 
993  1 Y 1 B LEU 1193 ? A LEU 1193 
994  1 Y 1 B ILE 1194 ? A ILE 1194 
995  1 Y 1 B ASP 1195 ? A ASP 1195 
996  1 Y 1 B LEU 1196 ? A LEU 1196 
997  1 Y 1 B GLN 1197 ? A GLN 1197 
998  1 Y 1 B GLU 1198 ? A GLU 1198 
999  1 Y 1 B LEU 1199 ? A LEU 1199 
1000 1 Y 1 B GLY 1200 ? A GLY 1200 
1001 1 Y 1 B LYS 1201 ? A LYS 1201 
1002 1 Y 1 B TYR 1202 ? A TYR 1202 
1003 1 Y 1 B GLU 1203 ? A GLU 1203 
1004 1 Y 1 B GLN 1204 ? A GLN 1204 
1005 1 Y 1 B TYR 1205 ? A TYR 1205 
1006 1 Y 1 B ILE 1206 ? A ILE 1206 
1007 1 Y 1 B LYS 1207 ? A LYS 1207 
1008 1 Y 1 B GLY 1208 ? A GLY 1208 
1009 1 Y 1 B SER 1209 ? A SER 1209 
1010 1 Y 1 B GLY 1210 ? A GLY 1210 
1011 1 Y 1 B TYR 1211 ? A TYR 1211 
1012 1 Y 1 B ILE 1212 ? A ILE 1212 
1013 1 Y 1 B PRO 1213 ? A PRO 1213 
1014 1 Y 1 B GLU 1214 ? A GLU 1214 
1015 1 Y 1 B ALA 1215 ? A ALA 1215 
1016 1 Y 1 B PRO 1216 ? A PRO 1216 
1017 1 Y 1 B ARG 1217 ? A ARG 1217 
1018 1 Y 1 B ASP 1218 ? A ASP 1218 
1019 1 Y 1 B GLY 1219 ? A GLY 1219 
1020 1 Y 1 B GLN 1220 ? A GLN 1220 
1021 1 Y 1 B ALA 1221 ? A ALA 1221 
1022 1 Y 1 B TYR 1222 ? A TYR 1222 
1023 1 Y 1 B VAL 1223 ? A VAL 1223 
1024 1 Y 1 B ARG 1224 ? A ARG 1224 
1025 1 Y 1 B LYS 1225 ? A LYS 1225 
1026 1 Y 1 B ASP 1226 ? A ASP 1226 
1027 1 Y 1 B GLY 1227 ? A GLY 1227 
1028 1 Y 1 B GLU 1228 ? A GLU 1228 
1029 1 Y 1 B TRP 1229 ? A TRP 1229 
1030 1 Y 1 B VAL 1230 ? A VAL 1230 
1031 1 Y 1 B LEU 1231 ? A LEU 1231 
1032 1 Y 1 B LEU 1232 ? A LEU 1232 
1033 1 Y 1 B SER 1233 ? A SER 1233 
1034 1 Y 1 B THR 1234 ? A THR 1234 
1035 1 Y 1 B PHE 1235 ? A PHE 1235 
1036 1 Y 1 B LEU 1236 ? A LEU 1236 
1037 1 Y 1 B GLY 1237 ? A GLY 1237 
1038 1 Y 1 B HIS 1238 ? A HIS 1238 
1039 1 Y 1 B HIS 1239 ? A HIS 1239 
1040 1 Y 1 B HIS 1240 ? A HIS 1240 
1041 1 Y 1 B HIS 1241 ? A HIS 1241 
1042 1 Y 1 B HIS 1242 ? A HIS 1242 
1043 1 Y 1 B HIS 1243 ? A HIS 1243 
1044 1 Y 1 A MET 1    ? B MET 1    
1045 1 Y 1 A PHE 2    ? B PHE 2    
1046 1 Y 1 A VAL 3    ? B VAL 3    
1047 1 Y 1 A PHE 4    ? B PHE 4    
1048 1 Y 1 A LEU 5    ? B LEU 5    
1049 1 Y 1 A VAL 6    ? B VAL 6    
1050 1 Y 1 A LEU 7    ? B LEU 7    
1051 1 Y 1 A LEU 8    ? B LEU 8    
1052 1 Y 1 A PRO 9    ? B PRO 9    
1053 1 Y 1 A LEU 10   ? B LEU 10   
1054 1 Y 1 A VAL 11   ? B VAL 11   
1055 1 Y 1 A SER 12   ? B SER 12   
1056 1 Y 1 A SER 13   ? B SER 13   
1057 1 Y 1 A GLN 14   ? B GLN 14   
1058 1 Y 1 A CYS 15   ? B CYS 15   
1059 1 Y 1 A VAL 16   ? B VAL 16   
1060 1 Y 1 A MET 17   ? B MET 17   
1061 1 Y 1 A PRO 18   ? B PRO 18   
1062 1 Y 1 A LEU 19   ? B LEU 19   
1063 1 Y 1 A PHE 20   ? B PHE 20   
1064 1 Y 1 A ASN 21   ? B ASN 21   
1065 1 Y 1 A LEU 22   ? B LEU 22   
1066 1 Y 1 A ILE 23   ? B ILE 23   
1067 1 Y 1 A THR 24   ? B THR 24   
1068 1 Y 1 A THR 25   ? B THR 25   
1069 1 Y 1 A THR 26   ? B THR 26   
1070 1 Y 1 A GLN 27   ? B GLN 27   
1071 1 Y 1 A SER 28   ? B SER 28   
1072 1 Y 1 A TYR 29   ? B TYR 29   
1073 1 Y 1 A THR 30   ? B THR 30   
1074 1 Y 1 A ASN 31   ? B ASN 31   
1075 1 Y 1 A SER 32   ? B SER 32   
1076 1 Y 1 A PHE 33   ? B PHE 33   
1077 1 Y 1 A THR 34   ? B THR 34   
1078 1 Y 1 A ARG 35   ? B ARG 35   
1079 1 Y 1 A GLY 36   ? B GLY 36   
1080 1 Y 1 A VAL 37   ? B VAL 37   
1081 1 Y 1 A TYR 38   ? B TYR 38   
1082 1 Y 1 A TYR 39   ? B TYR 39   
1083 1 Y 1 A PRO 40   ? B PRO 40   
1084 1 Y 1 A ASP 41   ? B ASP 41   
1085 1 Y 1 A LYS 42   ? B LYS 42   
1086 1 Y 1 A VAL 43   ? B VAL 43   
1087 1 Y 1 A PHE 44   ? B PHE 44   
1088 1 Y 1 A ARG 45   ? B ARG 45   
1089 1 Y 1 A SER 46   ? B SER 46   
1090 1 Y 1 A SER 47   ? B SER 47   
1091 1 Y 1 A VAL 48   ? B VAL 48   
1092 1 Y 1 A LEU 49   ? B LEU 49   
1093 1 Y 1 A HIS 50   ? B HIS 50   
1094 1 Y 1 A LEU 51   ? B LEU 51   
1095 1 Y 1 A THR 52   ? B THR 52   
1096 1 Y 1 A GLN 53   ? B GLN 53   
1097 1 Y 1 A ASP 54   ? B ASP 54   
1098 1 Y 1 A LEU 55   ? B LEU 55   
1099 1 Y 1 A PHE 56   ? B PHE 56   
1100 1 Y 1 A LEU 57   ? B LEU 57   
1101 1 Y 1 A PRO 58   ? B PRO 58   
1102 1 Y 1 A PHE 59   ? B PHE 59   
1103 1 Y 1 A PHE 60   ? B PHE 60   
1104 1 Y 1 A SER 61   ? B SER 61   
1105 1 Y 1 A ASN 62   ? B ASN 62   
1106 1 Y 1 A VAL 63   ? B VAL 63   
1107 1 Y 1 A THR 64   ? B THR 64   
1108 1 Y 1 A TRP 65   ? B TRP 65   
1109 1 Y 1 A PHE 66   ? B PHE 66   
1110 1 Y 1 A HIS 67   ? B HIS 67   
1111 1 Y 1 A ALA 68   ? B ALA 68   
1112 1 Y 1 A ILE 69   ? B ILE 69   
1113 1 Y 1 A SER 70   ? B SER 70   
1114 1 Y 1 A GLY 71   ? B GLY 71   
1115 1 Y 1 A THR 72   ? B THR 72   
1116 1 Y 1 A ASN 73   ? B ASN 73   
1117 1 Y 1 A GLY 74   ? B GLY 74   
1118 1 Y 1 A THR 75   ? B THR 75   
1119 1 Y 1 A LYS 76   ? B LYS 76   
1120 1 Y 1 A ARG 77   ? B ARG 77   
1121 1 Y 1 A PHE 78   ? B PHE 78   
1122 1 Y 1 A ASP 79   ? B ASP 79   
1123 1 Y 1 A ASN 80   ? B ASN 80   
1124 1 Y 1 A PRO 81   ? B PRO 81   
1125 1 Y 1 A VAL 82   ? B VAL 82   
1126 1 Y 1 A LEU 83   ? B LEU 83   
1127 1 Y 1 A PRO 84   ? B PRO 84   
1128 1 Y 1 A PHE 85   ? B PHE 85   
1129 1 Y 1 A ASN 86   ? B ASN 86   
1130 1 Y 1 A ASP 87   ? B ASP 87   
1131 1 Y 1 A GLY 88   ? B GLY 88   
1132 1 Y 1 A VAL 89   ? B VAL 89   
1133 1 Y 1 A TYR 90   ? B TYR 90   
1134 1 Y 1 A PHE 91   ? B PHE 91   
1135 1 Y 1 A ALA 92   ? B ALA 92   
1136 1 Y 1 A SER 93   ? B SER 93   
1137 1 Y 1 A THR 94   ? B THR 94   
1138 1 Y 1 A GLU 95   ? B GLU 95   
1139 1 Y 1 A LYS 96   ? B LYS 96   
1140 1 Y 1 A SER 97   ? B SER 97   
1141 1 Y 1 A ASN 98   ? B ASN 98   
1142 1 Y 1 A ILE 99   ? B ILE 99   
1143 1 Y 1 A ILE 100  ? B ILE 100  
1144 1 Y 1 A ARG 101  ? B ARG 101  
1145 1 Y 1 A GLY 102  ? B GLY 102  
1146 1 Y 1 A TRP 103  ? B TRP 103  
1147 1 Y 1 A ILE 104  ? B ILE 104  
1148 1 Y 1 A PHE 105  ? B PHE 105  
1149 1 Y 1 A GLY 106  ? B GLY 106  
1150 1 Y 1 A THR 107  ? B THR 107  
1151 1 Y 1 A THR 108  ? B THR 108  
1152 1 Y 1 A LEU 109  ? B LEU 109  
1153 1 Y 1 A ASP 110  ? B ASP 110  
1154 1 Y 1 A SER 111  ? B SER 111  
1155 1 Y 1 A LYS 112  ? B LYS 112  
1156 1 Y 1 A THR 113  ? B THR 113  
1157 1 Y 1 A GLN 114  ? B GLN 114  
1158 1 Y 1 A SER 115  ? B SER 115  
1159 1 Y 1 A LEU 116  ? B LEU 116  
1160 1 Y 1 A LEU 117  ? B LEU 117  
1161 1 Y 1 A ILE 118  ? B ILE 118  
1162 1 Y 1 A VAL 119  ? B VAL 119  
1163 1 Y 1 A ASN 120  ? B ASN 120  
1164 1 Y 1 A ASN 121  ? B ASN 121  
1165 1 Y 1 A ALA 122  ? B ALA 122  
1166 1 Y 1 A THR 123  ? B THR 123  
1167 1 Y 1 A ASN 124  ? B ASN 124  
1168 1 Y 1 A VAL 125  ? B VAL 125  
1169 1 Y 1 A PHE 126  ? B PHE 126  
1170 1 Y 1 A ILE 127  ? B ILE 127  
1171 1 Y 1 A LYS 128  ? B LYS 128  
1172 1 Y 1 A VAL 129  ? B VAL 129  
1173 1 Y 1 A CYS 130  ? B CYS 130  
1174 1 Y 1 A GLU 131  ? B GLU 131  
1175 1 Y 1 A PHE 132  ? B PHE 132  
1176 1 Y 1 A GLN 133  ? B GLN 133  
1177 1 Y 1 A PHE 134  ? B PHE 134  
1178 1 Y 1 A CYS 135  ? B CYS 135  
1179 1 Y 1 A ASN 136  ? B ASN 136  
1180 1 Y 1 A ASP 137  ? B ASP 137  
1181 1 Y 1 A PRO 138  ? B PRO 138  
1182 1 Y 1 A PHE 139  ? B PHE 139  
1183 1 Y 1 A LEU 140  ? B LEU 140  
1184 1 Y 1 A ASP 141  ? B ASP 141  
1185 1 Y 1 A VAL 142  ? B VAL 142  
1186 1 Y 1 A TYR 143  ? B TYR 143  
1187 1 Y 1 A HIS 144  ? B HIS 144  
1188 1 Y 1 A LYS 145  ? B LYS 145  
1189 1 Y 1 A ASN 146  ? B ASN 146  
1190 1 Y 1 A ASN 147  ? B ASN 147  
1191 1 Y 1 A LYS 148  ? B LYS 148  
1192 1 Y 1 A SER 149  ? B SER 149  
1193 1 Y 1 A TRP 150  ? B TRP 150  
1194 1 Y 1 A MET 151  ? B MET 151  
1195 1 Y 1 A GLU 152  ? B GLU 152  
1196 1 Y 1 A SER 153  ? B SER 153  
1197 1 Y 1 A GLU 154  ? B GLU 154  
1198 1 Y 1 A SER 155  ? B SER 155  
1199 1 Y 1 A GLY 156  ? B GLY 156  
1200 1 Y 1 A VAL 157  ? B VAL 157  
1201 1 Y 1 A TYR 158  ? B TYR 158  
1202 1 Y 1 A SER 159  ? B SER 159  
1203 1 Y 1 A SER 160  ? B SER 160  
1204 1 Y 1 A ALA 161  ? B ALA 161  
1205 1 Y 1 A ASN 162  ? B ASN 162  
1206 1 Y 1 A ASN 163  ? B ASN 163  
1207 1 Y 1 A CYS 164  ? B CYS 164  
1208 1 Y 1 A THR 165  ? B THR 165  
1209 1 Y 1 A PHE 166  ? B PHE 166  
1210 1 Y 1 A GLU 167  ? B GLU 167  
1211 1 Y 1 A TYR 168  ? B TYR 168  
1212 1 Y 1 A VAL 169  ? B VAL 169  
1213 1 Y 1 A SER 170  ? B SER 170  
1214 1 Y 1 A GLN 171  ? B GLN 171  
1215 1 Y 1 A PRO 172  ? B PRO 172  
1216 1 Y 1 A PHE 173  ? B PHE 173  
1217 1 Y 1 A LEU 174  ? B LEU 174  
1218 1 Y 1 A MET 175  ? B MET 175  
1219 1 Y 1 A ASP 176  ? B ASP 176  
1220 1 Y 1 A LEU 177  ? B LEU 177  
1221 1 Y 1 A GLU 178  ? B GLU 178  
1222 1 Y 1 A GLY 179  ? B GLY 179  
1223 1 Y 1 A LYS 180  ? B LYS 180  
1224 1 Y 1 A GLN 181  ? B GLN 181  
1225 1 Y 1 A GLY 182  ? B GLY 182  
1226 1 Y 1 A ASN 183  ? B ASN 183  
1227 1 Y 1 A PHE 184  ? B PHE 184  
1228 1 Y 1 A LYS 185  ? B LYS 185  
1229 1 Y 1 A ASN 186  ? B ASN 186  
1230 1 Y 1 A LEU 187  ? B LEU 187  
1231 1 Y 1 A ARG 188  ? B ARG 188  
1232 1 Y 1 A GLU 189  ? B GLU 189  
1233 1 Y 1 A PHE 190  ? B PHE 190  
1234 1 Y 1 A VAL 191  ? B VAL 191  
1235 1 Y 1 A PHE 192  ? B PHE 192  
1236 1 Y 1 A LYS 193  ? B LYS 193  
1237 1 Y 1 A ASN 194  ? B ASN 194  
1238 1 Y 1 A ILE 195  ? B ILE 195  
1239 1 Y 1 A ASP 196  ? B ASP 196  
1240 1 Y 1 A GLY 197  ? B GLY 197  
1241 1 Y 1 A TYR 198  ? B TYR 198  
1242 1 Y 1 A PHE 199  ? B PHE 199  
1243 1 Y 1 A LYS 200  ? B LYS 200  
1244 1 Y 1 A ILE 201  ? B ILE 201  
1245 1 Y 1 A TYR 202  ? B TYR 202  
1246 1 Y 1 A SER 203  ? B SER 203  
1247 1 Y 1 A LYS 204  ? B LYS 204  
1248 1 Y 1 A HIS 205  ? B HIS 205  
1249 1 Y 1 A THR 206  ? B THR 206  
1250 1 Y 1 A PRO 207  ? B PRO 207  
1251 1 Y 1 A ILE 208  ? B ILE 208  
1252 1 Y 1 A ILE 209  ? B ILE 209  
1253 1 Y 1 A GLY 210  ? B GLY 210  
1254 1 Y 1 A ARG 211  ? B ARG 211  
1255 1 Y 1 A ASP 212  ? B ASP 212  
1256 1 Y 1 A PHE 213  ? B PHE 213  
1257 1 Y 1 A PRO 214  ? B PRO 214  
1258 1 Y 1 A GLN 215  ? B GLN 215  
1259 1 Y 1 A GLY 216  ? B GLY 216  
1260 1 Y 1 A PHE 217  ? B PHE 217  
1261 1 Y 1 A SER 218  ? B SER 218  
1262 1 Y 1 A ALA 219  ? B ALA 219  
1263 1 Y 1 A LEU 220  ? B LEU 220  
1264 1 Y 1 A GLU 221  ? B GLU 221  
1265 1 Y 1 A PRO 222  ? B PRO 222  
1266 1 Y 1 A LEU 223  ? B LEU 223  
1267 1 Y 1 A VAL 224  ? B VAL 224  
1268 1 Y 1 A ASP 225  ? B ASP 225  
1269 1 Y 1 A LEU 226  ? B LEU 226  
1270 1 Y 1 A PRO 227  ? B PRO 227  
1271 1 Y 1 A ILE 228  ? B ILE 228  
1272 1 Y 1 A GLY 229  ? B GLY 229  
1273 1 Y 1 A ILE 230  ? B ILE 230  
1274 1 Y 1 A ASN 231  ? B ASN 231  
1275 1 Y 1 A ILE 232  ? B ILE 232  
1276 1 Y 1 A THR 233  ? B THR 233  
1277 1 Y 1 A ARG 234  ? B ARG 234  
1278 1 Y 1 A PHE 235  ? B PHE 235  
1279 1 Y 1 A GLN 236  ? B GLN 236  
1280 1 Y 1 A THR 237  ? B THR 237  
1281 1 Y 1 A LEU 238  ? B LEU 238  
1282 1 Y 1 A LEU 239  ? B LEU 239  
1283 1 Y 1 A ALA 240  ? B ALA 240  
1284 1 Y 1 A LEU 241  ? B LEU 241  
1285 1 Y 1 A ASN 242  ? B ASN 242  
1286 1 Y 1 A ARG 243  ? B ARG 243  
1287 1 Y 1 A SER 244  ? B SER 244  
1288 1 Y 1 A TYR 245  ? B TYR 245  
1289 1 Y 1 A LEU 246  ? B LEU 246  
1290 1 Y 1 A THR 247  ? B THR 247  
1291 1 Y 1 A PRO 248  ? B PRO 248  
1292 1 Y 1 A GLY 249  ? B GLY 249  
1293 1 Y 1 A ASP 250  ? B ASP 250  
1294 1 Y 1 A SER 251  ? B SER 251  
1295 1 Y 1 A SER 252  ? B SER 252  
1296 1 Y 1 A SER 253  ? B SER 253  
1297 1 Y 1 A GLY 254  ? B GLY 254  
1298 1 Y 1 A TRP 255  ? B TRP 255  
1299 1 Y 1 A THR 256  ? B THR 256  
1300 1 Y 1 A ALA 257  ? B ALA 257  
1301 1 Y 1 A GLY 258  ? B GLY 258  
1302 1 Y 1 A ALA 259  ? B ALA 259  
1303 1 Y 1 A ALA 260  ? B ALA 260  
1304 1 Y 1 A ASP 261  ? B ASP 261  
1305 1 Y 1 A TYR 262  ? B TYR 262  
1306 1 Y 1 A TYR 263  ? B TYR 263  
1307 1 Y 1 A VAL 264  ? B VAL 264  
1308 1 Y 1 A GLY 265  ? B GLY 265  
1309 1 Y 1 A TYR 266  ? B TYR 266  
1310 1 Y 1 A LEU 267  ? B LEU 267  
1311 1 Y 1 A GLN 268  ? B GLN 268  
1312 1 Y 1 A PRO 269  ? B PRO 269  
1313 1 Y 1 A ARG 270  ? B ARG 270  
1314 1 Y 1 A THR 271  ? B THR 271  
1315 1 Y 1 A PHE 272  ? B PHE 272  
1316 1 Y 1 A LEU 273  ? B LEU 273  
1317 1 Y 1 A LEU 274  ? B LEU 274  
1318 1 Y 1 A LYS 275  ? B LYS 275  
1319 1 Y 1 A TYR 276  ? B TYR 276  
1320 1 Y 1 A ASN 277  ? B ASN 277  
1321 1 Y 1 A GLU 278  ? B GLU 278  
1322 1 Y 1 A ASN 279  ? B ASN 279  
1323 1 Y 1 A GLY 280  ? B GLY 280  
1324 1 Y 1 A THR 281  ? B THR 281  
1325 1 Y 1 A ILE 282  ? B ILE 282  
1326 1 Y 1 A THR 283  ? B THR 283  
1327 1 Y 1 A ASP 284  ? B ASP 284  
1328 1 Y 1 A ALA 285  ? B ALA 285  
1329 1 Y 1 A VAL 286  ? B VAL 286  
1330 1 Y 1 A ASP 287  ? B ASP 287  
1331 1 Y 1 A CYS 288  ? B CYS 288  
1332 1 Y 1 A ALA 289  ? B ALA 289  
1333 1 Y 1 A LEU 290  ? B LEU 290  
1334 1 Y 1 A ASP 291  ? B ASP 291  
1335 1 Y 1 A PRO 292  ? B PRO 292  
1336 1 Y 1 A LEU 293  ? B LEU 293  
1337 1 Y 1 A SER 294  ? B SER 294  
1338 1 Y 1 A GLU 295  ? B GLU 295  
1339 1 Y 1 A THR 296  ? B THR 296  
1340 1 Y 1 A LYS 297  ? B LYS 297  
1341 1 Y 1 A CYS 298  ? B CYS 298  
1342 1 Y 1 A THR 299  ? B THR 299  
1343 1 Y 1 A LEU 300  ? B LEU 300  
1344 1 Y 1 A LYS 301  ? B LYS 301  
1345 1 Y 1 A SER 302  ? B SER 302  
1346 1 Y 1 A PHE 303  ? B PHE 303  
1347 1 Y 1 A THR 304  ? B THR 304  
1348 1 Y 1 A VAL 305  ? B VAL 305  
1349 1 Y 1 A GLU 306  ? B GLU 306  
1350 1 Y 1 A LYS 307  ? B LYS 307  
1351 1 Y 1 A GLY 308  ? B GLY 308  
1352 1 Y 1 A ILE 309  ? B ILE 309  
1353 1 Y 1 A TYR 310  ? B TYR 310  
1354 1 Y 1 A GLN 311  ? B GLN 311  
1355 1 Y 1 A THR 312  ? B THR 312  
1356 1 Y 1 A SER 313  ? B SER 313  
1357 1 Y 1 A ASN 314  ? B ASN 314  
1358 1 Y 1 A PHE 315  ? B PHE 315  
1359 1 Y 1 A ARG 316  ? B ARG 316  
1360 1 Y 1 A VAL 317  ? B VAL 317  
1361 1 Y 1 A GLN 318  ? B GLN 318  
1362 1 Y 1 A PRO 319  ? B PRO 319  
1363 1 Y 1 A THR 320  ? B THR 320  
1364 1 Y 1 A GLU 321  ? B GLU 321  
1365 1 Y 1 A SER 322  ? B SER 322  
1366 1 Y 1 A SER 526  ? B SER 526  
1367 1 Y 1 A THR 527  ? B THR 527  
1368 1 Y 1 A ASN 528  ? B ASN 528  
1369 1 Y 1 A LEU 529  ? B LEU 529  
1370 1 Y 1 A VAL 530  ? B VAL 530  
1371 1 Y 1 A LYS 531  ? B LYS 531  
1372 1 Y 1 A ASN 532  ? B ASN 532  
1373 1 Y 1 A LYS 533  ? B LYS 533  
1374 1 Y 1 A CYS 534  ? B CYS 534  
1375 1 Y 1 A VAL 535  ? B VAL 535  
1376 1 Y 1 A ASN 536  ? B ASN 536  
1377 1 Y 1 A PHE 537  ? B PHE 537  
1378 1 Y 1 A ASN 538  ? B ASN 538  
1379 1 Y 1 A PHE 539  ? B PHE 539  
1380 1 Y 1 A ASN 540  ? B ASN 540  
1381 1 Y 1 A GLY 541  ? B GLY 541  
1382 1 Y 1 A LEU 542  ? B LEU 542  
1383 1 Y 1 A THR 543  ? B THR 543  
1384 1 Y 1 A GLY 544  ? B GLY 544  
1385 1 Y 1 A THR 545  ? B THR 545  
1386 1 Y 1 A GLY 546  ? B GLY 546  
1387 1 Y 1 A VAL 547  ? B VAL 547  
1388 1 Y 1 A LEU 548  ? B LEU 548  
1389 1 Y 1 A THR 549  ? B THR 549  
1390 1 Y 1 A LYS 550  ? B LYS 550  
1391 1 Y 1 A SER 551  ? B SER 551  
1392 1 Y 1 A ASN 552  ? B ASN 552  
1393 1 Y 1 A LYS 553  ? B LYS 553  
1394 1 Y 1 A LYS 554  ? B LYS 554  
1395 1 Y 1 A PHE 555  ? B PHE 555  
1396 1 Y 1 A LEU 556  ? B LEU 556  
1397 1 Y 1 A PRO 557  ? B PRO 557  
1398 1 Y 1 A PHE 558  ? B PHE 558  
1399 1 Y 1 A GLN 559  ? B GLN 559  
1400 1 Y 1 A GLN 560  ? B GLN 560  
1401 1 Y 1 A PHE 561  ? B PHE 561  
1402 1 Y 1 A GLY 562  ? B GLY 562  
1403 1 Y 1 A ARG 563  ? B ARG 563  
1404 1 Y 1 A ASP 564  ? B ASP 564  
1405 1 Y 1 A ILE 565  ? B ILE 565  
1406 1 Y 1 A VAL 566  ? B VAL 566  
1407 1 Y 1 A ASP 567  ? B ASP 567  
1408 1 Y 1 A THR 568  ? B THR 568  
1409 1 Y 1 A THR 569  ? B THR 569  
1410 1 Y 1 A ASP 570  ? B ASP 570  
1411 1 Y 1 A ALA 571  ? B ALA 571  
1412 1 Y 1 A VAL 572  ? B VAL 572  
1413 1 Y 1 A ARG 573  ? B ARG 573  
1414 1 Y 1 A ASP 574  ? B ASP 574  
1415 1 Y 1 A PRO 575  ? B PRO 575  
1416 1 Y 1 A GLN 576  ? B GLN 576  
1417 1 Y 1 A THR 577  ? B THR 577  
1418 1 Y 1 A LEU 578  ? B LEU 578  
1419 1 Y 1 A GLU 579  ? B GLU 579  
1420 1 Y 1 A ILE 580  ? B ILE 580  
1421 1 Y 1 A LEU 581  ? B LEU 581  
1422 1 Y 1 A ASP 582  ? B ASP 582  
1423 1 Y 1 A ILE 583  ? B ILE 583  
1424 1 Y 1 A THR 584  ? B THR 584  
1425 1 Y 1 A PRO 585  ? B PRO 585  
1426 1 Y 1 A CYS 586  ? B CYS 586  
1427 1 Y 1 A SER 587  ? B SER 587  
1428 1 Y 1 A PHE 588  ? B PHE 588  
1429 1 Y 1 A GLY 589  ? B GLY 589  
1430 1 Y 1 A GLY 590  ? B GLY 590  
1431 1 Y 1 A VAL 591  ? B VAL 591  
1432 1 Y 1 A SER 592  ? B SER 592  
1433 1 Y 1 A VAL 593  ? B VAL 593  
1434 1 Y 1 A ILE 594  ? B ILE 594  
1435 1 Y 1 A THR 595  ? B THR 595  
1436 1 Y 1 A PRO 596  ? B PRO 596  
1437 1 Y 1 A GLY 597  ? B GLY 597  
1438 1 Y 1 A THR 598  ? B THR 598  
1439 1 Y 1 A ASN 599  ? B ASN 599  
1440 1 Y 1 A THR 600  ? B THR 600  
1441 1 Y 1 A SER 601  ? B SER 601  
1442 1 Y 1 A ASN 602  ? B ASN 602  
1443 1 Y 1 A GLN 603  ? B GLN 603  
1444 1 Y 1 A VAL 604  ? B VAL 604  
1445 1 Y 1 A ALA 605  ? B ALA 605  
1446 1 Y 1 A VAL 606  ? B VAL 606  
1447 1 Y 1 A LEU 607  ? B LEU 607  
1448 1 Y 1 A TYR 608  ? B TYR 608  
1449 1 Y 1 A GLN 609  ? B GLN 609  
1450 1 Y 1 A GLY 610  ? B GLY 610  
1451 1 Y 1 A VAL 611  ? B VAL 611  
1452 1 Y 1 A ASN 612  ? B ASN 612  
1453 1 Y 1 A CYS 613  ? B CYS 613  
1454 1 Y 1 A THR 614  ? B THR 614  
1455 1 Y 1 A GLU 615  ? B GLU 615  
1456 1 Y 1 A VAL 616  ? B VAL 616  
1457 1 Y 1 A SER 617  ? B SER 617  
1458 1 Y 1 A VAL 618  ? B VAL 618  
1459 1 Y 1 A ALA 619  ? B ALA 619  
1460 1 Y 1 A ILE 620  ? B ILE 620  
1461 1 Y 1 A HIS 621  ? B HIS 621  
1462 1 Y 1 A ALA 622  ? B ALA 622  
1463 1 Y 1 A ASP 623  ? B ASP 623  
1464 1 Y 1 A GLN 624  ? B GLN 624  
1465 1 Y 1 A LEU 625  ? B LEU 625  
1466 1 Y 1 A THR 626  ? B THR 626  
1467 1 Y 1 A PRO 627  ? B PRO 627  
1468 1 Y 1 A THR 628  ? B THR 628  
1469 1 Y 1 A TRP 629  ? B TRP 629  
1470 1 Y 1 A ARG 630  ? B ARG 630  
1471 1 Y 1 A VAL 631  ? B VAL 631  
1472 1 Y 1 A TYR 632  ? B TYR 632  
1473 1 Y 1 A SER 633  ? B SER 633  
1474 1 Y 1 A THR 634  ? B THR 634  
1475 1 Y 1 A GLY 635  ? B GLY 635  
1476 1 Y 1 A SER 636  ? B SER 636  
1477 1 Y 1 A ASN 637  ? B ASN 637  
1478 1 Y 1 A VAL 638  ? B VAL 638  
1479 1 Y 1 A PHE 639  ? B PHE 639  
1480 1 Y 1 A GLN 640  ? B GLN 640  
1481 1 Y 1 A THR 641  ? B THR 641  
1482 1 Y 1 A ARG 642  ? B ARG 642  
1483 1 Y 1 A ALA 643  ? B ALA 643  
1484 1 Y 1 A GLY 644  ? B GLY 644  
1485 1 Y 1 A CYS 645  ? B CYS 645  
1486 1 Y 1 A LEU 646  ? B LEU 646  
1487 1 Y 1 A ILE 647  ? B ILE 647  
1488 1 Y 1 A GLY 648  ? B GLY 648  
1489 1 Y 1 A ALA 649  ? B ALA 649  
1490 1 Y 1 A GLU 650  ? B GLU 650  
1491 1 Y 1 A TYR 651  ? B TYR 651  
1492 1 Y 1 A VAL 652  ? B VAL 652  
1493 1 Y 1 A ASN 653  ? B ASN 653  
1494 1 Y 1 A ASN 654  ? B ASN 654  
1495 1 Y 1 A SER 655  ? B SER 655  
1496 1 Y 1 A TYR 656  ? B TYR 656  
1497 1 Y 1 A GLU 657  ? B GLU 657  
1498 1 Y 1 A CYS 658  ? B CYS 658  
1499 1 Y 1 A ASP 659  ? B ASP 659  
1500 1 Y 1 A ILE 660  ? B ILE 660  
1501 1 Y 1 A PRO 661  ? B PRO 661  
1502 1 Y 1 A ILE 662  ? B ILE 662  
1503 1 Y 1 A GLY 663  ? B GLY 663  
1504 1 Y 1 A ALA 664  ? B ALA 664  
1505 1 Y 1 A GLY 665  ? B GLY 665  
1506 1 Y 1 A ILE 666  ? B ILE 666  
1507 1 Y 1 A CYS 667  ? B CYS 667  
1508 1 Y 1 A ALA 668  ? B ALA 668  
1509 1 Y 1 A SER 669  ? B SER 669  
1510 1 Y 1 A TYR 670  ? B TYR 670  
1511 1 Y 1 A GLN 671  ? B GLN 671  
1512 1 Y 1 A THR 672  ? B THR 672  
1513 1 Y 1 A GLN 673  ? B GLN 673  
1514 1 Y 1 A THR 674  ? B THR 674  
1515 1 Y 1 A LYS 675  ? B LYS 675  
1516 1 Y 1 A SER 676  ? B SER 676  
1517 1 Y 1 A ARG 677  ? B ARG 677  
1518 1 Y 1 A ALA 678  ? B ALA 678  
1519 1 Y 1 A GLY 679  ? B GLY 679  
1520 1 Y 1 A ALA 680  ? B ALA 680  
1521 1 Y 1 A ARG 681  ? B ARG 681  
1522 1 Y 1 A SER 682  ? B SER 682  
1523 1 Y 1 A VAL 683  ? B VAL 683  
1524 1 Y 1 A ALA 684  ? B ALA 684  
1525 1 Y 1 A SER 685  ? B SER 685  
1526 1 Y 1 A GLN 686  ? B GLN 686  
1527 1 Y 1 A SER 687  ? B SER 687  
1528 1 Y 1 A ILE 688  ? B ILE 688  
1529 1 Y 1 A ILE 689  ? B ILE 689  
1530 1 Y 1 A ALA 690  ? B ALA 690  
1531 1 Y 1 A TYR 691  ? B TYR 691  
1532 1 Y 1 A THR 692  ? B THR 692  
1533 1 Y 1 A MET 693  ? B MET 693  
1534 1 Y 1 A SER 694  ? B SER 694  
1535 1 Y 1 A LEU 695  ? B LEU 695  
1536 1 Y 1 A GLY 696  ? B GLY 696  
1537 1 Y 1 A ALA 697  ? B ALA 697  
1538 1 Y 1 A GLU 698  ? B GLU 698  
1539 1 Y 1 A ASN 699  ? B ASN 699  
1540 1 Y 1 A SER 700  ? B SER 700  
1541 1 Y 1 A VAL 701  ? B VAL 701  
1542 1 Y 1 A ALA 702  ? B ALA 702  
1543 1 Y 1 A TYR 703  ? B TYR 703  
1544 1 Y 1 A SER 704  ? B SER 704  
1545 1 Y 1 A ASN 705  ? B ASN 705  
1546 1 Y 1 A ASN 706  ? B ASN 706  
1547 1 Y 1 A SER 707  ? B SER 707  
1548 1 Y 1 A ILE 708  ? B ILE 708  
1549 1 Y 1 A ALA 709  ? B ALA 709  
1550 1 Y 1 A ILE 710  ? B ILE 710  
1551 1 Y 1 A PRO 711  ? B PRO 711  
1552 1 Y 1 A THR 712  ? B THR 712  
1553 1 Y 1 A ASN 713  ? B ASN 713  
1554 1 Y 1 A PHE 714  ? B PHE 714  
1555 1 Y 1 A THR 715  ? B THR 715  
1556 1 Y 1 A ILE 716  ? B ILE 716  
1557 1 Y 1 A SER 717  ? B SER 717  
1558 1 Y 1 A VAL 718  ? B VAL 718  
1559 1 Y 1 A THR 719  ? B THR 719  
1560 1 Y 1 A THR 720  ? B THR 720  
1561 1 Y 1 A GLU 721  ? B GLU 721  
1562 1 Y 1 A ILE 722  ? B ILE 722  
1563 1 Y 1 A LEU 723  ? B LEU 723  
1564 1 Y 1 A PRO 724  ? B PRO 724  
1565 1 Y 1 A VAL 725  ? B VAL 725  
1566 1 Y 1 A SER 726  ? B SER 726  
1567 1 Y 1 A MET 727  ? B MET 727  
1568 1 Y 1 A THR 728  ? B THR 728  
1569 1 Y 1 A LYS 729  ? B LYS 729  
1570 1 Y 1 A THR 730  ? B THR 730  
1571 1 Y 1 A SER 731  ? B SER 731  
1572 1 Y 1 A VAL 732  ? B VAL 732  
1573 1 Y 1 A ASP 733  ? B ASP 733  
1574 1 Y 1 A CYS 734  ? B CYS 734  
1575 1 Y 1 A THR 735  ? B THR 735  
1576 1 Y 1 A MET 736  ? B MET 736  
1577 1 Y 1 A TYR 737  ? B TYR 737  
1578 1 Y 1 A ILE 738  ? B ILE 738  
1579 1 Y 1 A CYS 739  ? B CYS 739  
1580 1 Y 1 A GLY 740  ? B GLY 740  
1581 1 Y 1 A ASP 741  ? B ASP 741  
1582 1 Y 1 A SER 742  ? B SER 742  
1583 1 Y 1 A THR 743  ? B THR 743  
1584 1 Y 1 A GLU 744  ? B GLU 744  
1585 1 Y 1 A CYS 745  ? B CYS 745  
1586 1 Y 1 A SER 746  ? B SER 746  
1587 1 Y 1 A ASN 747  ? B ASN 747  
1588 1 Y 1 A LEU 748  ? B LEU 748  
1589 1 Y 1 A LEU 749  ? B LEU 749  
1590 1 Y 1 A LEU 750  ? B LEU 750  
1591 1 Y 1 A GLN 751  ? B GLN 751  
1592 1 Y 1 A TYR 752  ? B TYR 752  
1593 1 Y 1 A GLY 753  ? B GLY 753  
1594 1 Y 1 A SER 754  ? B SER 754  
1595 1 Y 1 A PHE 755  ? B PHE 755  
1596 1 Y 1 A CYS 756  ? B CYS 756  
1597 1 Y 1 A THR 757  ? B THR 757  
1598 1 Y 1 A GLN 758  ? B GLN 758  
1599 1 Y 1 A LEU 759  ? B LEU 759  
1600 1 Y 1 A LYS 760  ? B LYS 760  
1601 1 Y 1 A ARG 761  ? B ARG 761  
1602 1 Y 1 A ALA 762  ? B ALA 762  
1603 1 Y 1 A LEU 763  ? B LEU 763  
1604 1 Y 1 A THR 764  ? B THR 764  
1605 1 Y 1 A GLY 765  ? B GLY 765  
1606 1 Y 1 A ILE 766  ? B ILE 766  
1607 1 Y 1 A ALA 767  ? B ALA 767  
1608 1 Y 1 A VAL 768  ? B VAL 768  
1609 1 Y 1 A GLU 769  ? B GLU 769  
1610 1 Y 1 A GLN 770  ? B GLN 770  
1611 1 Y 1 A ASP 771  ? B ASP 771  
1612 1 Y 1 A LYS 772  ? B LYS 772  
1613 1 Y 1 A ASN 773  ? B ASN 773  
1614 1 Y 1 A THR 774  ? B THR 774  
1615 1 Y 1 A GLN 775  ? B GLN 775  
1616 1 Y 1 A GLU 776  ? B GLU 776  
1617 1 Y 1 A VAL 777  ? B VAL 777  
1618 1 Y 1 A PHE 778  ? B PHE 778  
1619 1 Y 1 A ALA 779  ? B ALA 779  
1620 1 Y 1 A GLN 780  ? B GLN 780  
1621 1 Y 1 A VAL 781  ? B VAL 781  
1622 1 Y 1 A LYS 782  ? B LYS 782  
1623 1 Y 1 A GLN 783  ? B GLN 783  
1624 1 Y 1 A ILE 784  ? B ILE 784  
1625 1 Y 1 A TYR 785  ? B TYR 785  
1626 1 Y 1 A LYS 786  ? B LYS 786  
1627 1 Y 1 A THR 787  ? B THR 787  
1628 1 Y 1 A PRO 788  ? B PRO 788  
1629 1 Y 1 A PRO 789  ? B PRO 789  
1630 1 Y 1 A ILE 790  ? B ILE 790  
1631 1 Y 1 A LYS 791  ? B LYS 791  
1632 1 Y 1 A TYR 792  ? B TYR 792  
1633 1 Y 1 A PHE 793  ? B PHE 793  
1634 1 Y 1 A GLY 794  ? B GLY 794  
1635 1 Y 1 A GLY 795  ? B GLY 795  
1636 1 Y 1 A PHE 796  ? B PHE 796  
1637 1 Y 1 A ASN 797  ? B ASN 797  
1638 1 Y 1 A PHE 798  ? B PHE 798  
1639 1 Y 1 A SER 799  ? B SER 799  
1640 1 Y 1 A GLN 800  ? B GLN 800  
1641 1 Y 1 A ILE 801  ? B ILE 801  
1642 1 Y 1 A LEU 802  ? B LEU 802  
1643 1 Y 1 A PRO 803  ? B PRO 803  
1644 1 Y 1 A ASP 804  ? B ASP 804  
1645 1 Y 1 A PRO 805  ? B PRO 805  
1646 1 Y 1 A SER 806  ? B SER 806  
1647 1 Y 1 A LYS 807  ? B LYS 807  
1648 1 Y 1 A PRO 808  ? B PRO 808  
1649 1 Y 1 A SER 809  ? B SER 809  
1650 1 Y 1 A LYS 810  ? B LYS 810  
1651 1 Y 1 A ARG 811  ? B ARG 811  
1652 1 Y 1 A SER 812  ? B SER 812  
1653 1 Y 1 A PRO 813  ? B PRO 813  
1654 1 Y 1 A ILE 814  ? B ILE 814  
1655 1 Y 1 A GLU 815  ? B GLU 815  
1656 1 Y 1 A ASP 816  ? B ASP 816  
1657 1 Y 1 A LEU 817  ? B LEU 817  
1658 1 Y 1 A LEU 818  ? B LEU 818  
1659 1 Y 1 A PHE 819  ? B PHE 819  
1660 1 Y 1 A ASN 820  ? B ASN 820  
1661 1 Y 1 A LYS 821  ? B LYS 821  
1662 1 Y 1 A VAL 822  ? B VAL 822  
1663 1 Y 1 A THR 823  ? B THR 823  
1664 1 Y 1 A LEU 824  ? B LEU 824  
1665 1 Y 1 A ALA 825  ? B ALA 825  
1666 1 Y 1 A ASP 826  ? B ASP 826  
1667 1 Y 1 A ALA 827  ? B ALA 827  
1668 1 Y 1 A GLY 828  ? B GLY 828  
1669 1 Y 1 A PHE 829  ? B PHE 829  
1670 1 Y 1 A ILE 830  ? B ILE 830  
1671 1 Y 1 A LYS 831  ? B LYS 831  
1672 1 Y 1 A GLN 832  ? B GLN 832  
1673 1 Y 1 A TYR 833  ? B TYR 833  
1674 1 Y 1 A GLY 834  ? B GLY 834  
1675 1 Y 1 A ASP 835  ? B ASP 835  
1676 1 Y 1 A CYS 836  ? B CYS 836  
1677 1 Y 1 A LEU 837  ? B LEU 837  
1678 1 Y 1 A GLY 838  ? B GLY 838  
1679 1 Y 1 A ASP 839  ? B ASP 839  
1680 1 Y 1 A ILE 840  ? B ILE 840  
1681 1 Y 1 A ALA 841  ? B ALA 841  
1682 1 Y 1 A ALA 842  ? B ALA 842  
1683 1 Y 1 A ARG 843  ? B ARG 843  
1684 1 Y 1 A ASP 844  ? B ASP 844  
1685 1 Y 1 A LEU 845  ? B LEU 845  
1686 1 Y 1 A ILE 846  ? B ILE 846  
1687 1 Y 1 A CYS 847  ? B CYS 847  
1688 1 Y 1 A ALA 848  ? B ALA 848  
1689 1 Y 1 A GLN 849  ? B GLN 849  
1690 1 Y 1 A LYS 850  ? B LYS 850  
1691 1 Y 1 A PHE 851  ? B PHE 851  
1692 1 Y 1 A ASN 852  ? B ASN 852  
1693 1 Y 1 A GLY 853  ? B GLY 853  
1694 1 Y 1 A LEU 854  ? B LEU 854  
1695 1 Y 1 A THR 855  ? B THR 855  
1696 1 Y 1 A VAL 856  ? B VAL 856  
1697 1 Y 1 A LEU 857  ? B LEU 857  
1698 1 Y 1 A PRO 858  ? B PRO 858  
1699 1 Y 1 A PRO 859  ? B PRO 859  
1700 1 Y 1 A LEU 860  ? B LEU 860  
1701 1 Y 1 A LEU 861  ? B LEU 861  
1702 1 Y 1 A THR 862  ? B THR 862  
1703 1 Y 1 A ASP 863  ? B ASP 863  
1704 1 Y 1 A GLU 864  ? B GLU 864  
1705 1 Y 1 A MET 865  ? B MET 865  
1706 1 Y 1 A ILE 866  ? B ILE 866  
1707 1 Y 1 A ALA 867  ? B ALA 867  
1708 1 Y 1 A GLN 868  ? B GLN 868  
1709 1 Y 1 A TYR 869  ? B TYR 869  
1710 1 Y 1 A THR 870  ? B THR 870  
1711 1 Y 1 A SER 871  ? B SER 871  
1712 1 Y 1 A ALA 872  ? B ALA 872  
1713 1 Y 1 A LEU 873  ? B LEU 873  
1714 1 Y 1 A LEU 874  ? B LEU 874  
1715 1 Y 1 A ALA 875  ? B ALA 875  
1716 1 Y 1 A GLY 876  ? B GLY 876  
1717 1 Y 1 A THR 877  ? B THR 877  
1718 1 Y 1 A ILE 878  ? B ILE 878  
1719 1 Y 1 A THR 879  ? B THR 879  
1720 1 Y 1 A SER 880  ? B SER 880  
1721 1 Y 1 A GLY 881  ? B GLY 881  
1722 1 Y 1 A TRP 882  ? B TRP 882  
1723 1 Y 1 A THR 883  ? B THR 883  
1724 1 Y 1 A PHE 884  ? B PHE 884  
1725 1 Y 1 A GLY 885  ? B GLY 885  
1726 1 Y 1 A ALA 886  ? B ALA 886  
1727 1 Y 1 A GLY 887  ? B GLY 887  
1728 1 Y 1 A PRO 888  ? B PRO 888  
1729 1 Y 1 A ALA 889  ? B ALA 889  
1730 1 Y 1 A LEU 890  ? B LEU 890  
1731 1 Y 1 A GLN 891  ? B GLN 891  
1732 1 Y 1 A ILE 892  ? B ILE 892  
1733 1 Y 1 A PRO 893  ? B PRO 893  
1734 1 Y 1 A PHE 894  ? B PHE 894  
1735 1 Y 1 A PRO 895  ? B PRO 895  
1736 1 Y 1 A MET 896  ? B MET 896  
1737 1 Y 1 A GLN 897  ? B GLN 897  
1738 1 Y 1 A MET 898  ? B MET 898  
1739 1 Y 1 A ALA 899  ? B ALA 899  
1740 1 Y 1 A TYR 900  ? B TYR 900  
1741 1 Y 1 A ARG 901  ? B ARG 901  
1742 1 Y 1 A PHE 902  ? B PHE 902  
1743 1 Y 1 A ASN 903  ? B ASN 903  
1744 1 Y 1 A GLY 904  ? B GLY 904  
1745 1 Y 1 A ILE 905  ? B ILE 905  
1746 1 Y 1 A GLY 906  ? B GLY 906  
1747 1 Y 1 A VAL 907  ? B VAL 907  
1748 1 Y 1 A THR 908  ? B THR 908  
1749 1 Y 1 A GLN 909  ? B GLN 909  
1750 1 Y 1 A ASN 910  ? B ASN 910  
1751 1 Y 1 A VAL 911  ? B VAL 911  
1752 1 Y 1 A LEU 912  ? B LEU 912  
1753 1 Y 1 A TYR 913  ? B TYR 913  
1754 1 Y 1 A GLU 914  ? B GLU 914  
1755 1 Y 1 A ASN 915  ? B ASN 915  
1756 1 Y 1 A GLN 916  ? B GLN 916  
1757 1 Y 1 A LYS 917  ? B LYS 917  
1758 1 Y 1 A LEU 918  ? B LEU 918  
1759 1 Y 1 A ILE 919  ? B ILE 919  
1760 1 Y 1 A ALA 920  ? B ALA 920  
1761 1 Y 1 A ASN 921  ? B ASN 921  
1762 1 Y 1 A GLN 922  ? B GLN 922  
1763 1 Y 1 A PHE 923  ? B PHE 923  
1764 1 Y 1 A ASN 924  ? B ASN 924  
1765 1 Y 1 A SER 925  ? B SER 925  
1766 1 Y 1 A ALA 926  ? B ALA 926  
1767 1 Y 1 A ILE 927  ? B ILE 927  
1768 1 Y 1 A GLY 928  ? B GLY 928  
1769 1 Y 1 A LYS 929  ? B LYS 929  
1770 1 Y 1 A ILE 930  ? B ILE 930  
1771 1 Y 1 A GLN 931  ? B GLN 931  
1772 1 Y 1 A ASP 932  ? B ASP 932  
1773 1 Y 1 A SER 933  ? B SER 933  
1774 1 Y 1 A LEU 934  ? B LEU 934  
1775 1 Y 1 A PHE 935  ? B PHE 935  
1776 1 Y 1 A SER 936  ? B SER 936  
1777 1 Y 1 A THR 937  ? B THR 937  
1778 1 Y 1 A PRO 938  ? B PRO 938  
1779 1 Y 1 A SER 939  ? B SER 939  
1780 1 Y 1 A ALA 940  ? B ALA 940  
1781 1 Y 1 A LEU 941  ? B LEU 941  
1782 1 Y 1 A GLY 942  ? B GLY 942  
1783 1 Y 1 A LYS 943  ? B LYS 943  
1784 1 Y 1 A LEU 944  ? B LEU 944  
1785 1 Y 1 A GLN 945  ? B GLN 945  
1786 1 Y 1 A ASP 946  ? B ASP 946  
1787 1 Y 1 A VAL 947  ? B VAL 947  
1788 1 Y 1 A VAL 948  ? B VAL 948  
1789 1 Y 1 A ASN 949  ? B ASN 949  
1790 1 Y 1 A HIS 950  ? B HIS 950  
1791 1 Y 1 A ASN 951  ? B ASN 951  
1792 1 Y 1 A ALA 952  ? B ALA 952  
1793 1 Y 1 A GLN 953  ? B GLN 953  
1794 1 Y 1 A ALA 954  ? B ALA 954  
1795 1 Y 1 A LEU 955  ? B LEU 955  
1796 1 Y 1 A ASN 956  ? B ASN 956  
1797 1 Y 1 A THR 957  ? B THR 957  
1798 1 Y 1 A LEU 958  ? B LEU 958  
1799 1 Y 1 A VAL 959  ? B VAL 959  
1800 1 Y 1 A LYS 960  ? B LYS 960  
1801 1 Y 1 A GLN 961  ? B GLN 961  
1802 1 Y 1 A LEU 962  ? B LEU 962  
1803 1 Y 1 A SER 963  ? B SER 963  
1804 1 Y 1 A SER 964  ? B SER 964  
1805 1 Y 1 A LYS 965  ? B LYS 965  
1806 1 Y 1 A PHE 966  ? B PHE 966  
1807 1 Y 1 A GLY 967  ? B GLY 967  
1808 1 Y 1 A ALA 968  ? B ALA 968  
1809 1 Y 1 A ILE 969  ? B ILE 969  
1810 1 Y 1 A SER 970  ? B SER 970  
1811 1 Y 1 A SER 971  ? B SER 971  
1812 1 Y 1 A VAL 972  ? B VAL 972  
1813 1 Y 1 A LEU 973  ? B LEU 973  
1814 1 Y 1 A ASN 974  ? B ASN 974  
1815 1 Y 1 A ASP 975  ? B ASP 975  
1816 1 Y 1 A ILE 976  ? B ILE 976  
1817 1 Y 1 A LEU 977  ? B LEU 977  
1818 1 Y 1 A SER 978  ? B SER 978  
1819 1 Y 1 A ARG 979  ? B ARG 979  
1820 1 Y 1 A LEU 980  ? B LEU 980  
1821 1 Y 1 A ASP 981  ? B ASP 981  
1822 1 Y 1 A PRO 982  ? B PRO 982  
1823 1 Y 1 A PRO 983  ? B PRO 983  
1824 1 Y 1 A GLU 984  ? B GLU 984  
1825 1 Y 1 A ALA 985  ? B ALA 985  
1826 1 Y 1 A GLU 986  ? B GLU 986  
1827 1 Y 1 A VAL 987  ? B VAL 987  
1828 1 Y 1 A GLN 988  ? B GLN 988  
1829 1 Y 1 A ILE 989  ? B ILE 989  
1830 1 Y 1 A ASP 990  ? B ASP 990  
1831 1 Y 1 A ARG 991  ? B ARG 991  
1832 1 Y 1 A LEU 992  ? B LEU 992  
1833 1 Y 1 A ILE 993  ? B ILE 993  
1834 1 Y 1 A THR 994  ? B THR 994  
1835 1 Y 1 A GLY 995  ? B GLY 995  
1836 1 Y 1 A ARG 996  ? B ARG 996  
1837 1 Y 1 A LEU 997  ? B LEU 997  
1838 1 Y 1 A GLN 998  ? B GLN 998  
1839 1 Y 1 A SER 999  ? B SER 999  
1840 1 Y 1 A LEU 1000 ? B LEU 1000 
1841 1 Y 1 A GLN 1001 ? B GLN 1001 
1842 1 Y 1 A THR 1002 ? B THR 1002 
1843 1 Y 1 A TYR 1003 ? B TYR 1003 
1844 1 Y 1 A VAL 1004 ? B VAL 1004 
1845 1 Y 1 A THR 1005 ? B THR 1005 
1846 1 Y 1 A GLN 1006 ? B GLN 1006 
1847 1 Y 1 A GLN 1007 ? B GLN 1007 
1848 1 Y 1 A LEU 1008 ? B LEU 1008 
1849 1 Y 1 A ILE 1009 ? B ILE 1009 
1850 1 Y 1 A ARG 1010 ? B ARG 1010 
1851 1 Y 1 A ALA 1011 ? B ALA 1011 
1852 1 Y 1 A ALA 1012 ? B ALA 1012 
1853 1 Y 1 A GLU 1013 ? B GLU 1013 
1854 1 Y 1 A ILE 1014 ? B ILE 1014 
1855 1 Y 1 A ARG 1015 ? B ARG 1015 
1856 1 Y 1 A ALA 1016 ? B ALA 1016 
1857 1 Y 1 A SER 1017 ? B SER 1017 
1858 1 Y 1 A ALA 1018 ? B ALA 1018 
1859 1 Y 1 A ASN 1019 ? B ASN 1019 
1860 1 Y 1 A LEU 1020 ? B LEU 1020 
1861 1 Y 1 A ALA 1021 ? B ALA 1021 
1862 1 Y 1 A ALA 1022 ? B ALA 1022 
1863 1 Y 1 A THR 1023 ? B THR 1023 
1864 1 Y 1 A LYS 1024 ? B LYS 1024 
1865 1 Y 1 A MET 1025 ? B MET 1025 
1866 1 Y 1 A SER 1026 ? B SER 1026 
1867 1 Y 1 A GLU 1027 ? B GLU 1027 
1868 1 Y 1 A CYS 1028 ? B CYS 1028 
1869 1 Y 1 A VAL 1029 ? B VAL 1029 
1870 1 Y 1 A LEU 1030 ? B LEU 1030 
1871 1 Y 1 A GLY 1031 ? B GLY 1031 
1872 1 Y 1 A GLN 1032 ? B GLN 1032 
1873 1 Y 1 A SER 1033 ? B SER 1033 
1874 1 Y 1 A LYS 1034 ? B LYS 1034 
1875 1 Y 1 A ARG 1035 ? B ARG 1035 
1876 1 Y 1 A VAL 1036 ? B VAL 1036 
1877 1 Y 1 A ASP 1037 ? B ASP 1037 
1878 1 Y 1 A PHE 1038 ? B PHE 1038 
1879 1 Y 1 A CYS 1039 ? B CYS 1039 
1880 1 Y 1 A GLY 1040 ? B GLY 1040 
1881 1 Y 1 A LYS 1041 ? B LYS 1041 
1882 1 Y 1 A GLY 1042 ? B GLY 1042 
1883 1 Y 1 A TYR 1043 ? B TYR 1043 
1884 1 Y 1 A HIS 1044 ? B HIS 1044 
1885 1 Y 1 A LEU 1045 ? B LEU 1045 
1886 1 Y 1 A MET 1046 ? B MET 1046 
1887 1 Y 1 A SER 1047 ? B SER 1047 
1888 1 Y 1 A PHE 1048 ? B PHE 1048 
1889 1 Y 1 A PRO 1049 ? B PRO 1049 
1890 1 Y 1 A GLN 1050 ? B GLN 1050 
1891 1 Y 1 A SER 1051 ? B SER 1051 
1892 1 Y 1 A ALA 1052 ? B ALA 1052 
1893 1 Y 1 A PRO 1053 ? B PRO 1053 
1894 1 Y 1 A HIS 1054 ? B HIS 1054 
1895 1 Y 1 A GLY 1055 ? B GLY 1055 
1896 1 Y 1 A VAL 1056 ? B VAL 1056 
1897 1 Y 1 A VAL 1057 ? B VAL 1057 
1898 1 Y 1 A PHE 1058 ? B PHE 1058 
1899 1 Y 1 A LEU 1059 ? B LEU 1059 
1900 1 Y 1 A HIS 1060 ? B HIS 1060 
1901 1 Y 1 A VAL 1061 ? B VAL 1061 
1902 1 Y 1 A THR 1062 ? B THR 1062 
1903 1 Y 1 A TYR 1063 ? B TYR 1063 
1904 1 Y 1 A VAL 1064 ? B VAL 1064 
1905 1 Y 1 A PRO 1065 ? B PRO 1065 
1906 1 Y 1 A ALA 1066 ? B ALA 1066 
1907 1 Y 1 A GLN 1067 ? B GLN 1067 
1908 1 Y 1 A GLU 1068 ? B GLU 1068 
1909 1 Y 1 A LYS 1069 ? B LYS 1069 
1910 1 Y 1 A ASN 1070 ? B ASN 1070 
1911 1 Y 1 A PHE 1071 ? B PHE 1071 
1912 1 Y 1 A THR 1072 ? B THR 1072 
1913 1 Y 1 A THR 1073 ? B THR 1073 
1914 1 Y 1 A ALA 1074 ? B ALA 1074 
1915 1 Y 1 A PRO 1075 ? B PRO 1075 
1916 1 Y 1 A ALA 1076 ? B ALA 1076 
1917 1 Y 1 A ILE 1077 ? B ILE 1077 
1918 1 Y 1 A CYS 1078 ? B CYS 1078 
1919 1 Y 1 A HIS 1079 ? B HIS 1079 
1920 1 Y 1 A ASP 1080 ? B ASP 1080 
1921 1 Y 1 A GLY 1081 ? B GLY 1081 
1922 1 Y 1 A LYS 1082 ? B LYS 1082 
1923 1 Y 1 A ALA 1083 ? B ALA 1083 
1924 1 Y 1 A HIS 1084 ? B HIS 1084 
1925 1 Y 1 A PHE 1085 ? B PHE 1085 
1926 1 Y 1 A PRO 1086 ? B PRO 1086 
1927 1 Y 1 A ARG 1087 ? B ARG 1087 
1928 1 Y 1 A GLU 1088 ? B GLU 1088 
1929 1 Y 1 A GLY 1089 ? B GLY 1089 
1930 1 Y 1 A VAL 1090 ? B VAL 1090 
1931 1 Y 1 A PHE 1091 ? B PHE 1091 
1932 1 Y 1 A VAL 1092 ? B VAL 1092 
1933 1 Y 1 A SER 1093 ? B SER 1093 
1934 1 Y 1 A ASN 1094 ? B ASN 1094 
1935 1 Y 1 A GLY 1095 ? B GLY 1095 
1936 1 Y 1 A THR 1096 ? B THR 1096 
1937 1 Y 1 A HIS 1097 ? B HIS 1097 
1938 1 Y 1 A TRP 1098 ? B TRP 1098 
1939 1 Y 1 A PHE 1099 ? B PHE 1099 
1940 1 Y 1 A VAL 1100 ? B VAL 1100 
1941 1 Y 1 A THR 1101 ? B THR 1101 
1942 1 Y 1 A GLN 1102 ? B GLN 1102 
1943 1 Y 1 A ARG 1103 ? B ARG 1103 
1944 1 Y 1 A ASN 1104 ? B ASN 1104 
1945 1 Y 1 A PHE 1105 ? B PHE 1105 
1946 1 Y 1 A TYR 1106 ? B TYR 1106 
1947 1 Y 1 A GLU 1107 ? B GLU 1107 
1948 1 Y 1 A PRO 1108 ? B PRO 1108 
1949 1 Y 1 A GLN 1109 ? B GLN 1109 
1950 1 Y 1 A ILE 1110 ? B ILE 1110 
1951 1 Y 1 A ILE 1111 ? B ILE 1111 
1952 1 Y 1 A THR 1112 ? B THR 1112 
1953 1 Y 1 A THR 1113 ? B THR 1113 
1954 1 Y 1 A ASP 1114 ? B ASP 1114 
1955 1 Y 1 A ASN 1115 ? B ASN 1115 
1956 1 Y 1 A THR 1116 ? B THR 1116 
1957 1 Y 1 A PHE 1117 ? B PHE 1117 
1958 1 Y 1 A VAL 1118 ? B VAL 1118 
1959 1 Y 1 A SER 1119 ? B SER 1119 
1960 1 Y 1 A GLY 1120 ? B GLY 1120 
1961 1 Y 1 A ASN 1121 ? B ASN 1121 
1962 1 Y 1 A CYS 1122 ? B CYS 1122 
1963 1 Y 1 A ASP 1123 ? B ASP 1123 
1964 1 Y 1 A VAL 1124 ? B VAL 1124 
1965 1 Y 1 A VAL 1125 ? B VAL 1125 
1966 1 Y 1 A ILE 1126 ? B ILE 1126 
1967 1 Y 1 A GLY 1127 ? B GLY 1127 
1968 1 Y 1 A ILE 1128 ? B ILE 1128 
1969 1 Y 1 A VAL 1129 ? B VAL 1129 
1970 1 Y 1 A ASN 1130 ? B ASN 1130 
1971 1 Y 1 A ASN 1131 ? B ASN 1131 
1972 1 Y 1 A THR 1132 ? B THR 1132 
1973 1 Y 1 A VAL 1133 ? B VAL 1133 
1974 1 Y 1 A TYR 1134 ? B TYR 1134 
1975 1 Y 1 A ASP 1135 ? B ASP 1135 
1976 1 Y 1 A PRO 1136 ? B PRO 1136 
1977 1 Y 1 A LEU 1137 ? B LEU 1137 
1978 1 Y 1 A GLN 1138 ? B GLN 1138 
1979 1 Y 1 A LEU 1139 ? B LEU 1139 
1980 1 Y 1 A GLU 1140 ? B GLU 1140 
1981 1 Y 1 A LEU 1141 ? B LEU 1141 
1982 1 Y 1 A ASP 1142 ? B ASP 1142 
1983 1 Y 1 A SER 1143 ? B SER 1143 
1984 1 Y 1 A PHE 1144 ? B PHE 1144 
1985 1 Y 1 A LYS 1145 ? B LYS 1145 
1986 1 Y 1 A GLU 1146 ? B GLU 1146 
1987 1 Y 1 A GLU 1147 ? B GLU 1147 
1988 1 Y 1 A LEU 1148 ? B LEU 1148 
1989 1 Y 1 A ASP 1149 ? B ASP 1149 
1990 1 Y 1 A LYS 1150 ? B LYS 1150 
1991 1 Y 1 A TYR 1151 ? B TYR 1151 
1992 1 Y 1 A PHE 1152 ? B PHE 1152 
1993 1 Y 1 A LYS 1153 ? B LYS 1153 
1994 1 Y 1 A ASN 1154 ? B ASN 1154 
1995 1 Y 1 A HIS 1155 ? B HIS 1155 
1996 1 Y 1 A THR 1156 ? B THR 1156 
1997 1 Y 1 A SER 1157 ? B SER 1157 
1998 1 Y 1 A PRO 1158 ? B PRO 1158 
1999 1 Y 1 A ASP 1159 ? B ASP 1159 
2000 1 Y 1 A VAL 1160 ? B VAL 1160 
2001 1 Y 1 A ASP 1161 ? B ASP 1161 
2002 1 Y 1 A LEU 1162 ? B LEU 1162 
2003 1 Y 1 A GLY 1163 ? B GLY 1163 
2004 1 Y 1 A ASP 1164 ? B ASP 1164 
2005 1 Y 1 A ILE 1165 ? B ILE 1165 
2006 1 Y 1 A SER 1166 ? B SER 1166 
2007 1 Y 1 A GLY 1167 ? B GLY 1167 
2008 1 Y 1 A ILE 1168 ? B ILE 1168 
2009 1 Y 1 A ASN 1169 ? B ASN 1169 
2010 1 Y 1 A ALA 1170 ? B ALA 1170 
2011 1 Y 1 A SER 1171 ? B SER 1171 
2012 1 Y 1 A VAL 1172 ? B VAL 1172 
2013 1 Y 1 A VAL 1173 ? B VAL 1173 
2014 1 Y 1 A ASN 1174 ? B ASN 1174 
2015 1 Y 1 A ILE 1175 ? B ILE 1175 
2016 1 Y 1 A GLN 1176 ? B GLN 1176 
2017 1 Y 1 A LYS 1177 ? B LYS 1177 
2018 1 Y 1 A GLU 1178 ? B GLU 1178 
2019 1 Y 1 A ILE 1179 ? B ILE 1179 
2020 1 Y 1 A ASP 1180 ? B ASP 1180 
2021 1 Y 1 A ARG 1181 ? B ARG 1181 
2022 1 Y 1 A LEU 1182 ? B LEU 1182 
2023 1 Y 1 A ASN 1183 ? B ASN 1183 
2024 1 Y 1 A GLU 1184 ? B GLU 1184 
2025 1 Y 1 A VAL 1185 ? B VAL 1185 
2026 1 Y 1 A ALA 1186 ? B ALA 1186 
2027 1 Y 1 A LYS 1187 ? B LYS 1187 
2028 1 Y 1 A ASN 1188 ? B ASN 1188 
2029 1 Y 1 A LEU 1189 ? B LEU 1189 
2030 1 Y 1 A ASN 1190 ? B ASN 1190 
2031 1 Y 1 A GLU 1191 ? B GLU 1191 
2032 1 Y 1 A SER 1192 ? B SER 1192 
2033 1 Y 1 A LEU 1193 ? B LEU 1193 
2034 1 Y 1 A ILE 1194 ? B ILE 1194 
2035 1 Y 1 A ASP 1195 ? B ASP 1195 
2036 1 Y 1 A LEU 1196 ? B LEU 1196 
2037 1 Y 1 A GLN 1197 ? B GLN 1197 
2038 1 Y 1 A GLU 1198 ? B GLU 1198 
2039 1 Y 1 A LEU 1199 ? B LEU 1199 
2040 1 Y 1 A GLY 1200 ? B GLY 1200 
2041 1 Y 1 A LYS 1201 ? B LYS 1201 
2042 1 Y 1 A TYR 1202 ? B TYR 1202 
2043 1 Y 1 A GLU 1203 ? B GLU 1203 
2044 1 Y 1 A GLN 1204 ? B GLN 1204 
2045 1 Y 1 A TYR 1205 ? B TYR 1205 
2046 1 Y 1 A ILE 1206 ? B ILE 1206 
2047 1 Y 1 A LYS 1207 ? B LYS 1207 
2048 1 Y 1 A GLY 1208 ? B GLY 1208 
2049 1 Y 1 A SER 1209 ? B SER 1209 
2050 1 Y 1 A GLY 1210 ? B GLY 1210 
2051 1 Y 1 A TYR 1211 ? B TYR 1211 
2052 1 Y 1 A ILE 1212 ? B ILE 1212 
2053 1 Y 1 A PRO 1213 ? B PRO 1213 
2054 1 Y 1 A GLU 1214 ? B GLU 1214 
2055 1 Y 1 A ALA 1215 ? B ALA 1215 
2056 1 Y 1 A PRO 1216 ? B PRO 1216 
2057 1 Y 1 A ARG 1217 ? B ARG 1217 
2058 1 Y 1 A ASP 1218 ? B ASP 1218 
2059 1 Y 1 A GLY 1219 ? B GLY 1219 
2060 1 Y 1 A GLN 1220 ? B GLN 1220 
2061 1 Y 1 A ALA 1221 ? B ALA 1221 
2062 1 Y 1 A TYR 1222 ? B TYR 1222 
2063 1 Y 1 A VAL 1223 ? B VAL 1223 
2064 1 Y 1 A ARG 1224 ? B ARG 1224 
2065 1 Y 1 A LYS 1225 ? B LYS 1225 
2066 1 Y 1 A ASP 1226 ? B ASP 1226 
2067 1 Y 1 A GLY 1227 ? B GLY 1227 
2068 1 Y 1 A GLU 1228 ? B GLU 1228 
2069 1 Y 1 A TRP 1229 ? B TRP 1229 
2070 1 Y 1 A VAL 1230 ? B VAL 1230 
2071 1 Y 1 A LEU 1231 ? B LEU 1231 
2072 1 Y 1 A LEU 1232 ? B LEU 1232 
2073 1 Y 1 A SER 1233 ? B SER 1233 
2074 1 Y 1 A THR 1234 ? B THR 1234 
2075 1 Y 1 A PHE 1235 ? B PHE 1235 
2076 1 Y 1 A LEU 1236 ? B LEU 1236 
2077 1 Y 1 A GLY 1237 ? B GLY 1237 
2078 1 Y 1 A HIS 1238 ? B HIS 1238 
2079 1 Y 1 A HIS 1239 ? B HIS 1239 
2080 1 Y 1 A HIS 1240 ? B HIS 1240 
2081 1 Y 1 A HIS 1241 ? B HIS 1241 
2082 1 Y 1 A HIS 1242 ? B HIS 1242 
2083 1 Y 1 A HIS 1243 ? B HIS 1243 
2084 1 Y 1 D GLY 130  ? C GLY 130  
2085 1 Y 1 D GLY 131  ? C GLY 131  
2086 1 Y 1 D GLN 132  ? C GLN 132  
2087 1 Y 1 D HIS 133  ? C HIS 133  
2088 1 Y 1 D HIS 134  ? C HIS 134  
2089 1 Y 1 D HIS 135  ? C HIS 135  
2090 1 Y 1 D HIS 136  ? C HIS 136  
2091 1 Y 1 D HIS 137  ? C HIS 137  
2092 1 Y 1 D HIS 138  ? C HIS 138  
2093 1 Y 1 D GLY 139  ? C GLY 139  
2094 1 Y 1 D ALA 140  ? C ALA 140  
2095 1 Y 1 D TYR 141  ? C TYR 141  
2096 1 Y 1 D PRO 142  ? C PRO 142  
2097 1 Y 1 D TYR 143  ? C TYR 143  
2098 1 Y 1 D ASP 144  ? C ASP 144  
2099 1 Y 1 D VAL 145  ? C VAL 145  
2100 1 Y 1 D PRO 146  ? C PRO 146  
2101 1 Y 1 D ASP 147  ? C ASP 147  
2102 1 Y 1 D TYR 148  ? C TYR 148  
2103 1 Y 1 D ALA 149  ? C ALA 149  
2104 1 Y 1 D SER 150  ? C SER 150  
2105 1 Y 1 E GLY 130  ? D GLY 130  
2106 1 Y 1 E GLY 131  ? D GLY 131  
2107 1 Y 1 E GLN 132  ? D GLN 132  
2108 1 Y 1 E HIS 133  ? D HIS 133  
2109 1 Y 1 E HIS 134  ? D HIS 134  
2110 1 Y 1 E HIS 135  ? D HIS 135  
2111 1 Y 1 E HIS 136  ? D HIS 136  
2112 1 Y 1 E HIS 137  ? D HIS 137  
2113 1 Y 1 E HIS 138  ? D HIS 138  
2114 1 Y 1 E GLY 139  ? D GLY 139  
2115 1 Y 1 E ALA 140  ? D ALA 140  
2116 1 Y 1 E TYR 141  ? D TYR 141  
2117 1 Y 1 E PRO 142  ? D PRO 142  
2118 1 Y 1 E TYR 143  ? D TYR 143  
2119 1 Y 1 E ASP 144  ? D ASP 144  
2120 1 Y 1 E VAL 145  ? D VAL 145  
2121 1 Y 1 E PRO 146  ? D PRO 146  
2122 1 Y 1 E ASP 147  ? D ASP 147  
2123 1 Y 1 E TYR 148  ? D TYR 148  
2124 1 Y 1 E ALA 149  ? D ALA 149  
2125 1 Y 1 E SER 150  ? D SER 150  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-16 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CO9 
_em_admin.last_update        2024-12-11 
_em_admin.map_release_date   2024-11-20 
_em_admin.title              'Local refinement of JN.1 spike/Nanosota-9 complex' 
# 
_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                ? 
_em_entity_assembly_molwt.value                ? 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
_em_entity_assembly_naturalsource.details 
? ? 2 2 2697049 'Severe acute respiratory syndrome coronavirus 2' ? ? ? ? ? 
? ? 3 3 30538   'Vicugna pacos'                                   ? ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 2 2 9606 'Homo sapiens'     ? ? 
? 3 3 562  'Escherichia coli' ? ? 
# 
_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         54.8 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k 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 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.21.1_5286: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' AI089728 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' AI110700 2 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' AI171954 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8IOS 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CO9 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . PHE A 1 326 ? 178.174 206.857 190.185 1.00 34.95  ? 326 PHE B N   1 
ATOM 2    C CA  . PHE A 1 326 ? 177.719 208.140 189.650 1.00 36.53  ? 326 PHE B CA  1 
ATOM 3    C C   . PHE A 1 326 ? 176.984 209.036 190.665 1.00 42.89  ? 326 PHE B C   1 
ATOM 4    O O   . PHE A 1 326 ? 177.151 210.254 190.602 1.00 36.96  ? 326 PHE B O   1 
ATOM 5    C CB  . PHE A 1 326 ? 176.838 207.927 188.406 1.00 51.42  ? 326 PHE B CB  1 
ATOM 6    C CG  . PHE A 1 326 ? 177.580 207.395 187.207 1.00 70.37  ? 326 PHE B CG  1 
ATOM 7    C CD1 . PHE A 1 326 ? 178.966 207.416 187.153 1.00 72.99  ? 326 PHE B CD1 1 
ATOM 8    C CD2 . PHE A 1 326 ? 176.881 206.874 186.129 1.00 74.44  ? 326 PHE B CD2 1 
ATOM 9    C CE1 . PHE A 1 326 ? 179.639 206.928 186.049 1.00 72.99  ? 326 PHE B CE1 1 
ATOM 10   C CE2 . PHE A 1 326 ? 177.548 206.384 185.022 1.00 75.78  ? 326 PHE B CE2 1 
ATOM 11   C CZ  . PHE A 1 326 ? 178.928 206.411 184.982 1.00 75.03  ? 326 PHE B CZ  1 
ATOM 12   N N   . PRO A 1 327 ? 176.156 208.471 191.605 1.00 56.90  ? 327 PRO B N   1 
ATOM 13   C CA  . PRO A 1 327 ? 175.666 209.323 192.700 1.00 56.66  ? 327 PRO B CA  1 
ATOM 14   C C   . PRO A 1 327 ? 176.676 209.462 193.828 1.00 52.68  ? 327 PRO B C   1 
ATOM 15   O O   . PRO A 1 327 ? 177.353 208.495 194.192 1.00 50.23  ? 327 PRO B O   1 
ATOM 16   C CB  . PRO A 1 327 ? 174.404 208.595 193.183 1.00 46.26  ? 327 PRO B CB  1 
ATOM 17   C CG  . PRO A 1 327 ? 174.626 207.200 192.823 1.00 46.95  ? 327 PRO B CG  1 
ATOM 18   C CD  . PRO A 1 327 ? 175.332 207.248 191.513 1.00 51.29  ? 327 PRO B CD  1 
ATOM 19   N N   . ASN A 1 328 ? 176.784 210.659 194.391 1.00 45.72  ? 328 ASN B N   1 
ATOM 20   C CA  . ASN A 1 328 ? 177.617 210.903 195.558 1.00 49.49  ? 328 ASN B CA  1 
ATOM 21   C C   . ASN A 1 328 ? 176.763 210.806 196.813 1.00 59.10  ? 328 ASN B C   1 
ATOM 22   O O   . ASN A 1 328 ? 175.583 211.168 196.802 1.00 63.31  ? 328 ASN B O   1 
ATOM 23   C CB  . ASN A 1 328 ? 178.292 212.274 195.480 1.00 51.07  ? 328 ASN B CB  1 
ATOM 24   C CG  . ASN A 1 328 ? 179.222 212.400 194.289 1.00 48.10  ? 328 ASN B CG  1 
ATOM 25   O OD1 . ASN A 1 328 ? 179.364 211.467 193.500 1.00 52.92  ? 328 ASN B OD1 1 
ATOM 26   N ND2 . ASN A 1 328 ? 179.868 213.554 194.158 1.00 35.15  ? 328 ASN B ND2 1 
ATOM 27   N N   . VAL A 1 329 ? 177.362 210.305 197.893 1.00 62.13  ? 329 VAL B N   1 
ATOM 28   C CA  . VAL A 1 329 ? 176.600 210.052 199.109 1.00 65.76  ? 329 VAL B CA  1 
ATOM 29   C C   . VAL A 1 329 ? 176.296 211.370 199.811 1.00 69.38  ? 329 VAL B C   1 
ATOM 30   O O   . VAL A 1 329 ? 177.192 212.180 200.082 1.00 69.85  ? 329 VAL B O   1 
ATOM 31   C CB  . VAL A 1 329 ? 177.340 209.059 200.016 1.00 68.14  ? 329 VAL B CB  1 
ATOM 32   C CG1 . VAL A 1 329 ? 177.230 207.658 199.445 1.00 69.87  ? 329 VAL B CG1 1 
ATOM 33   C CG2 . VAL A 1 329 ? 178.812 209.432 200.155 1.00 66.93  ? 329 VAL B CG2 1 
ATOM 34   N N   . THR A 1 330 ? 175.013 211.604 200.076 1.00 73.12  ? 330 THR B N   1 
ATOM 35   C CA  . THR A 1 330 ? 174.543 212.739 200.855 1.00 76.31  ? 330 THR B CA  1 
ATOM 36   C C   . THR A 1 330 ? 173.470 212.230 201.804 1.00 80.95  ? 330 THR B C   1 
ATOM 37   O O   . THR A 1 330 ? 173.120 211.045 201.780 1.00 83.34  ? 330 THR B O   1 
ATOM 38   C CB  . THR A 1 330 ? 174.007 213.858 199.956 1.00 75.44  ? 330 THR B CB  1 
ATOM 39   O OG1 . THR A 1 330 ? 173.451 214.899 200.769 1.00 79.39  ? 330 THR B OG1 1 
ATOM 40   C CG2 . THR A 1 330 ? 172.931 213.321 199.026 1.00 74.09  ? 330 THR B CG2 1 
ATOM 41   N N   . ASN A 1 331 ? 172.939 213.137 202.633 1.00 81.35  ? 331 ASN B N   1 
ATOM 42   C CA  . ASN A 1 331 ? 171.927 212.829 203.649 1.00 84.56  ? 331 ASN B CA  1 
ATOM 43   C C   . ASN A 1 331 ? 172.443 211.759 204.617 1.00 86.38  ? 331 ASN B C   1 
ATOM 44   O O   . ASN A 1 331 ? 172.014 210.606 204.616 1.00 87.16  ? 331 ASN B O   1 
ATOM 45   C CB  . ASN A 1 331 ? 170.593 212.415 203.009 1.00 85.51  ? 331 ASN B CB  1 
ATOM 46   C CG  . ASN A 1 331 ? 169.967 213.527 202.194 1.00 83.05  ? 331 ASN B CG  1 
ATOM 47   O OD1 . ASN A 1 331 ? 169.840 213.421 200.975 1.00 79.85  ? 331 ASN B OD1 1 
ATOM 48   N ND2 . ASN A 1 331 ? 169.571 214.602 202.865 1.00 85.73  ? 331 ASN B ND2 1 
ATOM 49   N N   . LEU A 1 332 ? 173.428 212.167 205.414 1.00 85.96  ? 332 LEU B N   1 
ATOM 50   C CA  . LEU A 1 332 ? 174.143 211.263 206.307 1.00 88.42  ? 332 LEU B CA  1 
ATOM 51   C C   . LEU A 1 332 ? 173.397 210.969 207.610 1.00 92.66  ? 332 LEU B C   1 
ATOM 52   O O   . LEU A 1 332 ? 174.011 210.434 208.540 1.00 93.34  ? 332 LEU B O   1 
ATOM 53   C CB  . LEU A 1 332 ? 175.533 211.826 206.633 1.00 90.21  ? 332 LEU B CB  1 
ATOM 54   C CG  . LEU A 1 332 ? 176.715 211.614 205.674 1.00 92.59  ? 332 LEU B CG  1 
ATOM 55   C CD1 . LEU A 1 332 ? 177.066 210.133 205.572 1.00 91.78  ? 332 LEU B CD1 1 
ATOM 56   C CD2 . LEU A 1 332 ? 176.513 212.226 204.286 1.00 87.77  ? 332 LEU B CD2 1 
ATOM 57   N N   . CYS A 1 333 ? 172.098 211.322 207.698 1.00 94.66  ? 333 CYS B N   1 
ATOM 58   C CA  . CYS A 1 333 ? 171.149 211.092 208.794 1.00 91.70  ? 333 CYS B CA  1 
ATOM 59   C C   . CYS A 1 333 ? 171.493 211.896 210.047 1.00 87.62  ? 333 CYS B C   1 
ATOM 60   O O   . CYS A 1 333 ? 172.672 212.113 210.354 1.00 90.13  ? 333 CYS B O   1 
ATOM 61   C CB  . CYS A 1 333 ? 171.049 209.605 209.148 1.00 90.76  ? 333 CYS B CB  1 
ATOM 62   S SG  . CYS A 1 333 ? 170.351 208.551 207.859 1.00 102.86 ? 333 CYS B SG  1 
ATOM 63   N N   . PRO A 1 334 ? 170.489 212.357 210.799 1.00 84.12  ? 334 PRO B N   1 
ATOM 64   C CA  . PRO A 1 334 ? 170.753 213.152 212.013 1.00 84.21  ? 334 PRO B CA  1 
ATOM 65   C C   . PRO A 1 334 ? 170.994 212.293 213.252 1.00 78.02  ? 334 PRO B C   1 
ATOM 66   O O   . PRO A 1 334 ? 170.265 212.366 214.245 1.00 76.45  ? 334 PRO B O   1 
ATOM 67   C CB  . PRO A 1 334 ? 169.477 214.002 212.133 1.00 83.82  ? 334 PRO B CB  1 
ATOM 68   C CG  . PRO A 1 334 ? 168.714 213.809 210.843 1.00 80.67  ? 334 PRO B CG  1 
ATOM 69   C CD  . PRO A 1 334 ? 169.080 212.445 210.390 1.00 81.42  ? 334 PRO B CD  1 
ATOM 70   N N   . PHE A 1 335 ? 172.036 211.460 213.203 1.00 72.23  ? 335 PHE B N   1 
ATOM 71   C CA  . PHE A 1 335 ? 172.446 210.738 214.404 1.00 71.25  ? 335 PHE B CA  1 
ATOM 72   C C   . PHE A 1 335 ? 173.190 211.635 215.384 1.00 70.98  ? 335 PHE B C   1 
ATOM 73   O O   . PHE A 1 335 ? 173.161 211.378 216.593 1.00 73.53  ? 335 PHE B O   1 
ATOM 74   C CB  . PHE A 1 335 ? 173.319 209.531 214.052 1.00 77.65  ? 335 PHE B CB  1 
ATOM 75   C CG  . PHE A 1 335 ? 172.586 208.418 213.353 1.00 81.14  ? 335 PHE B CG  1 
ATOM 76   C CD1 . PHE A 1 335 ? 171.200 208.372 213.337 1.00 81.49  ? 335 PHE B CD1 1 
ATOM 77   C CD2 . PHE A 1 335 ? 173.291 207.403 212.727 1.00 85.12  ? 335 PHE B CD2 1 
ATOM 78   C CE1 . PHE A 1 335 ? 170.534 207.343 212.700 1.00 83.87  ? 335 PHE B CE1 1 
ATOM 79   C CE2 . PHE A 1 335 ? 172.630 206.372 212.088 1.00 87.52  ? 335 PHE B CE2 1 
ATOM 80   C CZ  . PHE A 1 335 ? 171.251 206.342 212.074 1.00 84.97  ? 335 PHE B CZ  1 
ATOM 81   N N   . HIS A 1 336 ? 173.859 212.678 214.892 1.00 70.77  ? 336 HIS B N   1 
ATOM 82   C CA  . HIS A 1 336 ? 174.610 213.557 215.780 1.00 75.44  ? 336 HIS B CA  1 
ATOM 83   C C   . HIS A 1 336 ? 173.701 214.490 216.567 1.00 77.38  ? 336 HIS B C   1 
ATOM 84   O O   . HIS A 1 336 ? 174.042 214.875 217.691 1.00 80.15  ? 336 HIS B O   1 
ATOM 85   C CB  . HIS A 1 336 ? 175.628 214.369 214.981 1.00 78.25  ? 336 HIS B CB  1 
ATOM 86   C CG  . HIS A 1 336 ? 176.668 215.031 215.830 1.00 80.87  ? 336 HIS B CG  1 
ATOM 87   N ND1 . HIS A 1 336 ? 177.872 214.433 216.133 1.00 81.20  ? 336 HIS B ND1 1 
ATOM 88   C CD2 . HIS A 1 336 ? 176.684 216.239 216.440 1.00 81.58  ? 336 HIS B CD2 1 
ATOM 89   C CE1 . HIS A 1 336 ? 178.585 215.244 216.894 1.00 82.14  ? 336 HIS B CE1 1 
ATOM 90   N NE2 . HIS A 1 336 ? 177.887 216.347 217.095 1.00 83.81  ? 336 HIS B NE2 1 
ATOM 91   N N   . GLU A 1 337 ? 172.552 214.864 216.001 1.00 75.54  ? 337 GLU B N   1 
ATOM 92   C CA  . GLU A 1 337 ? 171.611 215.714 216.720 1.00 75.55  ? 337 GLU B CA  1 
ATOM 93   C C   . GLU A 1 337 ? 170.891 214.964 217.831 1.00 75.88  ? 337 GLU B C   1 
ATOM 94   O O   . GLU A 1 337 ? 170.392 215.596 218.768 1.00 73.50  ? 337 GLU B O   1 
ATOM 95   C CB  . GLU A 1 337 ? 170.593 216.309 215.746 1.00 76.47  ? 337 GLU B CB  1 
ATOM 96   C CG  . GLU A 1 337 ? 171.160 217.391 214.841 1.00 83.62  ? 337 GLU B CG  1 
ATOM 97   C CD  . GLU A 1 337 ? 170.128 217.941 213.877 1.00 91.71  ? 337 GLU B CD  1 
ATOM 98   O OE1 . GLU A 1 337 ? 168.979 217.453 213.893 1.00 93.13  ? 337 GLU B OE1 1 
ATOM 99   O OE2 . GLU A 1 337 ? 170.466 218.862 213.103 1.00 93.31  ? 337 GLU B OE2 1 
ATOM 100  N N   . VAL A 1 338 ? 170.824 213.636 217.745 1.00 75.03  ? 338 VAL B N   1 
ATOM 101  C CA  . VAL A 1 338 ? 170.185 212.844 218.790 1.00 67.47  ? 338 VAL B CA  1 
ATOM 102  C C   . VAL A 1 338 ? 171.171 212.530 219.906 1.00 65.54  ? 338 VAL B C   1 
ATOM 103  O O   . VAL A 1 338 ? 170.851 212.668 221.092 1.00 66.98  ? 338 VAL B O   1 
ATOM 104  C CB  . VAL A 1 338 ? 169.591 211.562 218.182 1.00 63.84  ? 338 VAL B CB  1 
ATOM 105  C CG1 . VAL A 1 338 ? 169.013 210.667 219.265 1.00 60.50  ? 338 VAL B CG1 1 
ATOM 106  C CG2 . VAL A 1 338 ? 168.542 211.914 217.145 1.00 68.67  ? 338 VAL B CG2 1 
ATOM 107  N N   . PHE A 1 339 ? 172.387 212.117 219.547 1.00 63.48  ? 339 PHE B N   1 
ATOM 108  C CA  . PHE A 1 339 ? 173.351 211.659 220.540 1.00 67.21  ? 339 PHE B CA  1 
ATOM 109  C C   . PHE A 1 339 ? 173.948 212.816 221.332 1.00 68.69  ? 339 PHE B C   1 
ATOM 110  O O   . PHE A 1 339 ? 174.151 212.700 222.546 1.00 71.82  ? 339 PHE B O   1 
ATOM 111  C CB  . PHE A 1 339 ? 174.457 210.859 219.854 1.00 68.15  ? 339 PHE B CB  1 
ATOM 112  C CG  . PHE A 1 339 ? 174.176 209.388 219.770 1.00 65.93  ? 339 PHE B CG  1 
ATOM 113  C CD1 . PHE A 1 339 ? 173.211 208.907 218.902 1.00 65.61  ? 339 PHE B CD1 1 
ATOM 114  C CD2 . PHE A 1 339 ? 174.876 208.487 220.551 1.00 63.79  ? 339 PHE B CD2 1 
ATOM 115  C CE1 . PHE A 1 339 ? 172.947 207.556 218.815 1.00 63.45  ? 339 PHE B CE1 1 
ATOM 116  C CE2 . PHE A 1 339 ? 174.615 207.135 220.468 1.00 60.94  ? 339 PHE B CE2 1 
ATOM 117  C CZ  . PHE A 1 339 ? 173.650 206.672 219.598 1.00 61.81  ? 339 PHE B CZ  1 
ATOM 118  N N   . ASN A 1 340 ? 174.231 213.935 220.673 1.00 65.16  ? 340 ASN B N   1 
ATOM 119  C CA  . ASN A 1 340 ? 174.874 215.083 221.303 1.00 65.38  ? 340 ASN B CA  1 
ATOM 120  C C   . ASN A 1 340 ? 173.758 216.111 221.466 1.00 66.66  ? 340 ASN B C   1 
ATOM 121  O O   . ASN A 1 340 ? 173.430 216.842 220.527 1.00 68.89  ? 340 ASN B O   1 
ATOM 122  C CB  . ASN A 1 340 ? 176.043 215.579 220.442 1.00 71.86  ? 340 ASN B CB  1 
ATOM 123  C CG  . ASN A 1 340 ? 176.701 216.882 220.948 1.00 77.21  ? 340 ASN B CG  1 
ATOM 124  O OD1 . ASN A 1 340 ? 176.192 217.604 221.806 1.00 77.54  ? 340 ASN B OD1 1 
ATOM 125  N ND2 . ASN A 1 340 ? 177.869 217.171 220.388 1.00 76.67  ? 340 ASN B ND2 1 
ATOM 126  N N   . ALA A 1 341 ? 173.176 216.160 222.661 1.00 67.86  ? 341 ALA B N   1 
ATOM 127  C CA  . ALA A 1 341 ? 172.164 217.143 223.007 1.00 66.89  ? 341 ALA B CA  1 
ATOM 128  C C   . ALA A 1 341 ? 172.474 217.704 224.386 1.00 66.39  ? 341 ALA B C   1 
ATOM 129  O O   . ALA A 1 341 ? 173.186 217.089 225.184 1.00 67.96  ? 341 ALA B O   1 
ATOM 130  C CB  . ALA A 1 341 ? 170.751 216.545 222.981 1.00 61.86  ? 341 ALA B CB  1 
ATOM 131  N N   . THR A 1 342 ? 171.938 218.896 224.654 1.00 64.92  ? 342 THR B N   1 
ATOM 132  C CA  . THR A 1 342 ? 172.179 219.539 225.941 1.00 69.26  ? 342 THR B CA  1 
ATOM 133  C C   . THR A 1 342 ? 171.473 218.800 227.071 1.00 72.17  ? 342 THR B C   1 
ATOM 134  O O   . THR A 1 342 ? 171.993 218.724 228.191 1.00 71.88  ? 342 THR B O   1 
ATOM 135  C CB  . THR A 1 342 ? 171.731 220.999 225.894 1.00 70.95  ? 342 THR B CB  1 
ATOM 136  O OG1 . THR A 1 342 ? 170.324 221.061 225.626 1.00 73.09  ? 342 THR B OG1 1 
ATOM 137  C CG2 . THR A 1 342 ? 172.482 221.749 224.806 1.00 68.31  ? 342 THR B CG2 1 
ATOM 138  N N   . ARG A 1 343 ? 170.294 218.246 226.798 1.00 68.37  ? 343 ARG B N   1 
ATOM 139  C CA  . ARG A 1 343 ? 169.537 217.526 227.811 1.00 65.70  ? 343 ARG B CA  1 
ATOM 140  C C   . ARG A 1 343 ? 168.604 216.538 227.127 1.00 61.72  ? 343 ARG B C   1 
ATOM 141  O O   . ARG A 1 343 ? 168.157 216.765 226.000 1.00 61.86  ? 343 ARG B O   1 
ATOM 142  C CB  . ARG A 1 343 ? 168.746 218.493 228.702 1.00 71.01  ? 343 ARG B CB  1 
ATOM 143  C CG  . ARG A 1 343 ? 167.765 219.375 227.944 1.00 70.77  ? 343 ARG B CG  1 
ATOM 144  C CD  . ARG A 1 343 ? 166.939 220.234 228.888 1.00 77.08  ? 343 ARG B CD  1 
ATOM 145  N NE  . ARG A 1 343 ? 165.989 219.446 229.664 1.00 82.88  ? 343 ARG B NE  1 
ATOM 146  C CZ  . ARG A 1 343 ? 165.874 219.500 230.984 1.00 87.92  ? 343 ARG B CZ  1 
ATOM 147  N NH1 . ARG A 1 343 ? 166.637 220.298 231.712 1.00 88.43  ? 343 ARG B NH1 1 
ATOM 148  N NH2 . ARG A 1 343 ? 164.969 218.735 231.588 1.00 83.63  ? 343 ARG B NH2 1 
ATOM 149  N N   . PHE A 1 344 ? 168.327 215.434 227.817 1.00 54.64  ? 344 PHE B N   1 
ATOM 150  C CA  . PHE A 1 344 ? 167.364 214.448 227.354 1.00 50.59  ? 344 PHE B CA  1 
ATOM 151  C C   . PHE A 1 344 ? 166.069 214.565 228.153 1.00 54.95  ? 344 PHE B C   1 
ATOM 152  O O   . PHE A 1 344 ? 165.938 215.378 229.071 1.00 61.16  ? 344 PHE B O   1 
ATOM 153  C CB  . PHE A 1 344 ? 167.927 213.028 227.450 1.00 49.44  ? 344 PHE B CB  1 
ATOM 154  C CG  . PHE A 1 344 ? 169.031 212.732 226.473 1.00 52.67  ? 344 PHE B CG  1 
ATOM 155  C CD1 . PHE A 1 344 ? 169.273 213.565 225.391 1.00 61.33  ? 344 PHE B CD1 1 
ATOM 156  C CD2 . PHE A 1 344 ? 169.807 211.596 226.621 1.00 49.87  ? 344 PHE B CD2 1 
ATOM 157  C CE1 . PHE A 1 344 ? 170.282 213.279 224.491 1.00 61.61  ? 344 PHE B CE1 1 
ATOM 158  C CE2 . PHE A 1 344 ? 170.814 211.305 225.723 1.00 51.44  ? 344 PHE B CE2 1 
ATOM 159  C CZ  . PHE A 1 344 ? 171.053 212.147 224.659 1.00 54.85  ? 344 PHE B CZ  1 
ATOM 160  N N   . ALA A 1 345 ? 165.101 213.733 227.792 1.00 55.05  ? 345 ALA B N   1 
ATOM 161  C CA  . ALA A 1 345 ? 163.805 213.698 228.447 1.00 56.15  ? 345 ALA B CA  1 
ATOM 162  C C   . ALA A 1 345 ? 163.753 212.565 229.465 1.00 55.09  ? 345 ALA B C   1 
ATOM 163  O O   . ALA A 1 345 ? 164.575 211.646 229.454 1.00 56.44  ? 345 ALA B O   1 
ATOM 164  C CB  . ALA A 1 345 ? 162.681 213.535 227.421 1.00 56.85  ? 345 ALA B CB  1 
ATOM 165  N N   . SER A 1 346 ? 162.766 212.647 230.353 1.00 53.13  ? 346 SER B N   1 
ATOM 166  C CA  . SER A 1 346 ? 162.607 211.659 231.406 1.00 54.19  ? 346 SER B CA  1 
ATOM 167  C C   . SER A 1 346 ? 162.088 210.339 230.836 1.00 55.37  ? 346 SER B C   1 
ATOM 168  O O   . SER A 1 346 ? 161.734 210.228 229.658 1.00 59.48  ? 346 SER B O   1 
ATOM 169  C CB  . SER A 1 346 ? 161.665 212.181 232.488 1.00 56.71  ? 346 SER B CB  1 
ATOM 170  O OG  . SER A 1 346 ? 162.212 213.319 233.131 1.00 58.12  ? 346 SER B OG  1 
ATOM 171  N N   . VAL A 1 347 ? 162.057 209.322 231.700 1.00 48.68  ? 347 VAL B N   1 
ATOM 172  C CA  . VAL A 1 347 ? 161.681 207.980 231.267 1.00 47.32  ? 347 VAL B CA  1 
ATOM 173  C C   . VAL A 1 347 ? 160.196 207.919 230.934 1.00 53.92  ? 347 VAL B C   1 
ATOM 174  O O   . VAL A 1 347 ? 159.794 207.306 229.939 1.00 58.42  ? 347 VAL B O   1 
ATOM 175  C CB  . VAL A 1 347 ? 162.061 206.954 232.348 1.00 47.64  ? 347 VAL B CB  1 
ATOM 176  C CG1 . VAL A 1 347 ? 161.611 205.564 231.957 1.00 49.42  ? 347 VAL B CG1 1 
ATOM 177  C CG2 . VAL A 1 347 ? 163.537 206.985 232.593 1.00 49.96  ? 347 VAL B CG2 1 
ATOM 178  N N   . TYR A 1 348 ? 159.358 208.553 231.756 1.00 50.55  ? 348 TYR B N   1 
ATOM 179  C CA  . TYR A 1 348 ? 157.919 208.537 231.524 1.00 48.62  ? 348 TYR B CA  1 
ATOM 180  C C   . TYR A 1 348 ? 157.512 209.323 230.285 1.00 52.30  ? 348 TYR B C   1 
ATOM 181  O O   . TYR A 1 348 ? 156.416 209.103 229.761 1.00 58.93  ? 348 TYR B O   1 
ATOM 182  C CB  . TYR A 1 348 ? 157.188 209.079 232.753 1.00 50.51  ? 348 TYR B CB  1 
ATOM 183  C CG  . TYR A 1 348 ? 157.059 210.583 232.784 1.00 52.34  ? 348 TYR B CG  1 
ATOM 184  C CD1 . TYR A 1 348 ? 158.176 211.391 232.939 1.00 55.41  ? 348 TYR B CD1 1 
ATOM 185  C CD2 . TYR A 1 348 ? 155.819 211.195 232.662 1.00 57.05  ? 348 TYR B CD2 1 
ATOM 186  C CE1 . TYR A 1 348 ? 158.065 212.767 232.969 1.00 57.65  ? 348 TYR B CE1 1 
ATOM 187  C CE2 . TYR A 1 348 ? 155.697 212.572 232.689 1.00 59.08  ? 348 TYR B CE2 1 
ATOM 188  C CZ  . TYR A 1 348 ? 156.824 213.352 232.843 1.00 59.64  ? 348 TYR B CZ  1 
ATOM 189  O OH  . TYR A 1 348 ? 156.710 214.721 232.872 1.00 61.72  ? 348 TYR B OH  1 
ATOM 190  N N   . ALA A 1 349 ? 158.362 210.228 229.809 1.00 54.74  ? 349 ALA B N   1 
ATOM 191  C CA  . ALA A 1 349 ? 158.077 211.090 228.667 1.00 58.81  ? 349 ALA B CA  1 
ATOM 192  C C   . ALA A 1 349 ? 159.194 210.991 227.638 1.00 60.46  ? 349 ALA B C   1 
ATOM 193  O O   . ALA A 1 349 ? 159.745 211.997 227.187 1.00 62.58  ? 349 ALA B O   1 
ATOM 194  C CB  . ALA A 1 349 ? 157.876 212.535 229.111 1.00 56.69  ? 349 ALA B CB  1 
ATOM 195  N N   . TRP A 1 350 ? 159.556 209.761 227.269 1.00 58.43  ? 350 TRP B N   1 
ATOM 196  C CA  . TRP A 1 350 ? 160.719 209.529 226.419 1.00 55.43  ? 350 TRP B CA  1 
ATOM 197  C C   . TRP A 1 350 ? 160.467 210.049 225.008 1.00 57.55  ? 350 TRP B C   1 
ATOM 198  O O   . TRP A 1 350 ? 159.493 209.659 224.357 1.00 59.69  ? 350 TRP B O   1 
ATOM 199  C CB  . TRP A 1 350 ? 161.068 208.043 226.384 1.00 51.76  ? 350 TRP B CB  1 
ATOM 200  C CG  . TRP A 1 350 ? 159.918 207.098 226.154 1.00 51.39  ? 350 TRP B CG  1 
ATOM 201  C CD1 . TRP A 1 350 ? 159.066 206.599 227.092 1.00 54.09  ? 350 TRP B CD1 1 
ATOM 202  C CD2 . TRP A 1 350 ? 159.537 206.496 224.911 1.00 52.63  ? 350 TRP B CD2 1 
ATOM 203  N NE1 . TRP A 1 350 ? 158.163 205.747 226.510 1.00 55.45  ? 350 TRP B NE1 1 
ATOM 204  C CE2 . TRP A 1 350 ? 158.432 205.664 225.170 1.00 53.62  ? 350 TRP B CE2 1 
ATOM 205  C CE3 . TRP A 1 350 ? 160.016 206.590 223.601 1.00 58.52  ? 350 TRP B CE3 1 
ATOM 206  C CZ2 . TRP A 1 350 ? 157.798 204.933 224.171 1.00 57.28  ? 350 TRP B CZ2 1 
ATOM 207  C CZ3 . TRP A 1 350 ? 159.386 205.862 222.611 1.00 64.11  ? 350 TRP B CZ3 1 
ATOM 208  C CH2 . TRP A 1 350 ? 158.289 205.045 222.900 1.00 62.87  ? 350 TRP B CH2 1 
ATOM 209  N N   . ASN A 1 351 ? 161.345 210.933 224.542 1.00 56.41  ? 351 ASN B N   1 
ATOM 210  C CA  . ASN A 1 351 ? 161.215 211.508 223.212 1.00 59.72  ? 351 ASN B CA  1 
ATOM 211  C C   . ASN A 1 351 ? 161.721 210.531 222.161 1.00 59.79  ? 351 ASN B C   1 
ATOM 212  O O   . ASN A 1 351 ? 162.777 209.916 222.323 1.00 59.68  ? 351 ASN B O   1 
ATOM 213  C CB  . ASN A 1 351 ? 161.991 212.823 223.119 1.00 63.09  ? 351 ASN B CB  1 
ATOM 214  C CG  . ASN A 1 351 ? 161.436 213.892 224.038 1.00 66.87  ? 351 ASN B CG  1 
ATOM 215  O OD1 . ASN A 1 351 ? 160.494 213.650 224.792 1.00 66.40  ? 351 ASN B OD1 1 
ATOM 216  N ND2 . ASN A 1 351 ? 162.020 215.083 223.980 1.00 67.78  ? 351 ASN B ND2 1 
ATOM 217  N N   . ARG A 1 352 ? 160.963 210.399 221.076 1.00 61.03  ? 352 ARG B N   1 
ATOM 218  C CA  . ARG A 1 352 ? 161.281 209.463 220.007 1.00 61.60  ? 352 ARG B CA  1 
ATOM 219  C C   . ARG A 1 352 ? 161.335 210.215 218.688 1.00 64.08  ? 352 ARG B C   1 
ATOM 220  O O   . ARG A 1 352 ? 160.433 211.000 218.378 1.00 64.68  ? 352 ARG B O   1 
ATOM 221  C CB  . ARG A 1 352 ? 160.248 208.330 219.947 1.00 63.22  ? 352 ARG B CB  1 
ATOM 222  C CG  . ARG A 1 352 ? 160.018 207.738 218.568 1.00 65.73  ? 352 ARG B CG  1 
ATOM 223  C CD  . ARG A 1 352 ? 159.237 206.441 218.663 1.00 69.25  ? 352 ARG B CD  1 
ATOM 224  N NE  . ARG A 1 352 ? 160.097 205.304 218.967 1.00 70.46  ? 352 ARG B NE  1 
ATOM 225  C CZ  . ARG A 1 352 ? 159.769 204.039 218.741 1.00 75.19  ? 352 ARG B CZ  1 
ATOM 226  N NH1 . ARG A 1 352 ? 158.594 203.712 218.230 1.00 76.81  ? 352 ARG B NH1 1 
ATOM 227  N NH2 . ARG A 1 352 ? 160.639 203.080 219.041 1.00 74.47  ? 352 ARG B NH2 1 
ATOM 228  N N   . THR A 1 353 ? 162.396 209.983 217.920 1.00 65.43  ? 353 THR B N   1 
ATOM 229  C CA  . THR A 1 353 ? 162.580 210.606 216.620 1.00 66.37  ? 353 THR B CA  1 
ATOM 230  C C   . THR A 1 353 ? 162.667 209.532 215.543 1.00 70.80  ? 353 THR B C   1 
ATOM 231  O O   . THR A 1 353 ? 162.986 208.370 215.814 1.00 71.17  ? 353 THR B O   1 
ATOM 232  C CB  . THR A 1 353 ? 163.832 211.497 216.598 1.00 64.67  ? 353 THR B CB  1 
ATOM 233  O OG1 . THR A 1 353 ? 163.848 212.275 215.395 1.00 72.13  ? 353 THR B OG1 1 
ATOM 234  C CG2 . THR A 1 353 ? 165.097 210.663 216.681 1.00 60.83  ? 353 THR B CG2 1 
ATOM 235  N N   . ARG A 1 354 ? 162.343 209.926 214.315 1.00 74.56  ? 354 ARG B N   1 
ATOM 236  C CA  . ARG A 1 354 ? 162.340 209.022 213.174 1.00 71.90  ? 354 ARG B CA  1 
ATOM 237  C C   . ARG A 1 354 ? 163.468 209.398 212.225 1.00 71.59  ? 354 ARG B C   1 
ATOM 238  O O   . ARG A 1 354 ? 163.639 210.575 211.890 1.00 74.80  ? 354 ARG B O   1 
ATOM 239  C CB  . ARG A 1 354 ? 160.998 209.059 212.440 1.00 72.82  ? 354 ARG B CB  1 
ATOM 240  C CG  . ARG A 1 354 ? 160.885 208.031 211.328 1.00 74.54  ? 354 ARG B CG  1 
ATOM 241  C CD  . ARG A 1 354 ? 159.450 207.849 210.868 1.00 81.79  ? 354 ARG B CD  1 
ATOM 242  N NE  . ARG A 1 354 ? 158.995 208.952 210.031 1.00 87.75  ? 354 ARG B NE  1 
ATOM 243  C CZ  . ARG A 1 354 ? 158.084 209.842 210.397 1.00 92.30  ? 354 ARG B CZ  1 
ATOM 244  N NH1 . ARG A 1 354 ? 157.505 209.790 211.585 1.00 94.94  ? 354 ARG B NH1 1 
ATOM 245  N NH2 . ARG A 1 354 ? 157.744 210.809 209.549 1.00 89.91  ? 354 ARG B NH2 1 
ATOM 246  N N   . ILE A 1 355 ? 164.231 208.399 211.800 1.00 70.14  ? 355 ILE B N   1 
ATOM 247  C CA  . ILE A 1 355 ? 165.352 208.577 210.886 1.00 70.74  ? 355 ILE B CA  1 
ATOM 248  C C   . ILE A 1 355 ? 164.999 207.844 209.599 1.00 82.49  ? 355 ILE B C   1 
ATOM 249  O O   . ILE A 1 355 ? 164.905 206.610 209.582 1.00 85.23  ? 355 ILE B O   1 
ATOM 250  C CB  . ILE A 1 355 ? 166.672 208.065 211.481 1.00 70.97  ? 355 ILE B CB  1 
ATOM 251  C CG1 . ILE A 1 355 ? 167.084 208.853 212.735 1.00 72.79  ? 355 ILE B CG1 1 
ATOM 252  C CG2 . ILE A 1 355 ? 167.776 208.100 210.450 1.00 80.33  ? 355 ILE B CG2 1 
ATOM 253  C CD1 . ILE A 1 355 ? 166.560 208.312 214.054 1.00 72.76  ? 355 ILE B CD1 1 
ATOM 254  N N   . SER A 1 356 ? 164.801 208.597 208.519 1.00 89.40  ? 356 SER B N   1 
ATOM 255  C CA  . SER A 1 356 ? 164.377 208.016 207.252 1.00 90.85  ? 356 SER B CA  1 
ATOM 256  C C   . SER A 1 356 ? 164.795 208.935 206.115 1.00 91.40  ? 356 SER B C   1 
ATOM 257  O O   . SER A 1 356 ? 165.113 210.109 206.328 1.00 93.45  ? 356 SER B O   1 
ATOM 258  C CB  . SER A 1 356 ? 162.864 207.776 207.223 1.00 87.96  ? 356 SER B CB  1 
ATOM 259  O OG  . SER A 1 356 ? 162.153 208.990 207.392 1.00 86.85  ? 356 SER B OG  1 
ATOM 260  N N   . ASN A 1 357 ? 164.777 208.373 204.898 1.00 88.11  ? 357 ASN B N   1 
ATOM 261  C CA  . ASN A 1 357 ? 165.145 209.068 203.658 1.00 90.86  ? 357 ASN B CA  1 
ATOM 262  C C   . ASN A 1 357 ? 166.552 209.659 203.739 1.00 92.67  ? 357 ASN B C   1 
ATOM 263  O O   . ASN A 1 357 ? 166.803 210.797 203.334 1.00 91.87  ? 357 ASN B O   1 
ATOM 264  C CB  . ASN A 1 357 ? 164.115 210.142 203.294 1.00 90.37  ? 357 ASN B CB  1 
ATOM 265  C CG  . ASN A 1 357 ? 162.748 209.559 202.998 1.00 89.37  ? 357 ASN B CG  1 
ATOM 266  O OD1 . ASN A 1 357 ? 161.785 209.807 203.722 1.00 91.80  ? 357 ASN B OD1 1 
ATOM 267  N ND2 . ASN A 1 357 ? 162.658 208.779 201.929 1.00 88.11  ? 357 ASN B ND2 1 
ATOM 268  N N   . CYS A 1 358 ? 167.476 208.863 204.268 1.00 90.73  ? 358 CYS B N   1 
ATOM 269  C CA  . CYS A 1 358 ? 168.867 209.262 204.427 1.00 88.50  ? 358 CYS B CA  1 
ATOM 270  C C   . CYS A 1 358 ? 169.708 207.999 204.553 1.00 89.59  ? 358 CYS B C   1 
ATOM 271  O O   . CYS A 1 358 ? 169.201 206.930 204.896 1.00 92.62  ? 358 CYS B O   1 
ATOM 272  C CB  . CYS A 1 358 ? 169.030 210.198 205.633 1.00 92.90  ? 358 CYS B CB  1 
ATOM 273  S SG  . CYS A 1 358 ? 168.653 209.485 207.253 1.00 102.00 ? 358 CYS B SG  1 
ATOM 274  N N   . VAL A 1 359 ? 171.004 208.125 204.271 1.00 90.29  ? 359 VAL B N   1 
ATOM 275  C CA  . VAL A 1 359 ? 171.928 207.000 204.383 1.00 94.96  ? 359 VAL B CA  1 
ATOM 276  C C   . VAL A 1 359 ? 172.595 207.052 205.752 1.00 96.14  ? 359 VAL B C   1 
ATOM 277  O O   . VAL A 1 359 ? 173.046 208.114 206.203 1.00 96.85  ? 359 VAL B O   1 
ATOM 278  C CB  . VAL A 1 359 ? 172.953 206.976 203.230 1.00 94.70  ? 359 VAL B CB  1 
ATOM 279  C CG1 . VAL A 1 359 ? 172.234 206.812 201.898 1.00 93.48  ? 359 VAL B CG1 1 
ATOM 280  C CG2 . VAL A 1 359 ? 173.829 208.220 203.190 1.00 87.73  ? 359 VAL B CG2 1 
ATOM 281  N N   . ALA A 1 360 ? 172.597 205.919 206.445 1.00 95.30  ? 360 ALA B N   1 
ATOM 282  C CA  . ALA A 1 360 ? 173.019 205.854 207.838 1.00 94.07  ? 360 ALA B CA  1 
ATOM 283  C C   . ALA A 1 360 ? 174.441 205.315 207.904 1.00 96.22  ? 360 ALA B C   1 
ATOM 284  O O   . ALA A 1 360 ? 174.682 204.140 207.609 1.00 98.95  ? 360 ALA B O   1 
ATOM 285  C CB  . ALA A 1 360 ? 172.062 204.986 208.652 1.00 94.37  ? 360 ALA B CB  1 
ATOM 286  N N   . ASP A 1 361 ? 175.379 206.174 208.288 1.00 97.47  ? 361 ASP B N   1 
ATOM 287  C CA  . ASP A 1 361 ? 176.762 205.770 208.508 1.00 99.90  ? 361 ASP B CA  1 
ATOM 288  C C   . ASP A 1 361 ? 176.918 205.386 209.975 1.00 99.02  ? 361 ASP B C   1 
ATOM 289  O O   . ASP A 1 361 ? 176.811 206.236 210.864 1.00 100.18 ? 361 ASP B O   1 
ATOM 290  C CB  . ASP A 1 361 ? 177.722 206.890 208.113 1.00 102.69 ? 361 ASP B CB  1 
ATOM 291  C CG  . ASP A 1 361 ? 177.279 208.250 208.623 1.00 103.44 ? 361 ASP B CG  1 
ATOM 292  O OD1 . ASP A 1 361 ? 176.079 208.409 208.927 1.00 101.01 ? 361 ASP B OD1 1 
ATOM 293  O OD2 . ASP A 1 361 ? 178.131 209.158 208.720 1.00 103.70 ? 361 ASP B OD2 1 
ATOM 294  N N   . TYR A 1 362 ? 177.156 204.104 210.231 1.00 96.81  ? 362 TYR B N   1 
ATOM 295  C CA  . TYR A 1 362 ? 177.320 203.621 211.601 1.00 91.65  ? 362 TYR B CA  1 
ATOM 296  C C   . TYR A 1 362 ? 178.785 203.644 212.023 1.00 92.21  ? 362 TYR B C   1 
ATOM 297  O O   . TYR A 1 362 ? 179.339 202.664 212.519 1.00 92.20  ? 362 TYR B O   1 
ATOM 298  C CB  . TYR A 1 362 ? 176.729 202.224 211.727 1.00 89.96  ? 362 TYR B CB  1 
ATOM 299  C CG  . TYR A 1 362 ? 175.279 202.164 211.319 1.00 91.83  ? 362 TYR B CG  1 
ATOM 300  C CD1 . TYR A 1 362 ? 174.320 202.918 211.982 1.00 89.39  ? 362 TYR B CD1 1 
ATOM 301  C CD2 . TYR A 1 362 ? 174.872 201.376 210.251 1.00 96.79  ? 362 TYR B CD2 1 
ATOM 302  C CE1 . TYR A 1 362 ? 172.991 202.873 211.604 1.00 86.92  ? 362 TYR B CE1 1 
ATOM 303  C CE2 . TYR A 1 362 ? 173.548 201.324 209.866 1.00 93.96  ? 362 TYR B CE2 1 
ATOM 304  C CZ  . TYR A 1 362 ? 172.613 202.073 210.547 1.00 86.14  ? 362 TYR B CZ  1 
ATOM 305  O OH  . TYR A 1 362 ? 171.297 202.026 210.159 1.00 79.45  ? 362 TYR B OH  1 
ATOM 306  N N   . SER A 1 363 ? 179.420 204.798 211.820 1.00 92.99  ? 363 SER B N   1 
ATOM 307  C CA  . SER A 1 363 ? 180.780 205.043 212.265 1.00 94.37  ? 363 SER B CA  1 
ATOM 308  C C   . SER A 1 363 ? 180.905 206.255 213.170 1.00 98.19  ? 363 SER B C   1 
ATOM 309  O O   . SER A 1 363 ? 181.892 206.351 213.905 1.00 100.43 ? 363 SER B O   1 
ATOM 310  C CB  . SER A 1 363 ? 181.719 205.223 211.062 1.00 99.86  ? 363 SER B CB  1 
ATOM 311  O OG  . SER A 1 363 ? 181.396 206.396 210.335 1.00 102.53 ? 363 SER B OG  1 
ATOM 312  N N   . VAL A 1 364 ? 179.939 207.176 213.139 1.00 99.95  ? 364 VAL B N   1 
ATOM 313  C CA  . VAL A 1 364 ? 179.955 208.316 214.048 1.00 103.24 ? 364 VAL B CA  1 
ATOM 314  C C   . VAL A 1 364 ? 179.545 207.923 215.460 1.00 102.78 ? 364 VAL B C   1 
ATOM 315  O O   . VAL A 1 364 ? 179.773 208.694 216.401 1.00 102.11 ? 364 VAL B O   1 
ATOM 316  C CB  . VAL A 1 364 ? 179.043 209.439 213.528 1.00 102.41 ? 364 VAL B CB  1 
ATOM 317  C CG1 . VAL A 1 364 ? 179.540 209.945 212.183 1.00 101.63 ? 364 VAL B CG1 1 
ATOM 318  C CG2 . VAL A 1 364 ? 177.606 208.951 213.419 1.00 100.64 ? 364 VAL B CG2 1 
ATOM 319  N N   . LEU A 1 365 ? 178.942 206.745 215.635 1.00 100.52 ? 365 LEU B N   1 
ATOM 320  C CA  . LEU A 1 365 ? 178.555 206.292 216.965 1.00 101.40 ? 365 LEU B CA  1 
ATOM 321  C C   . LEU A 1 365 ? 179.753 205.832 217.784 1.00 102.33 ? 365 LEU B C   1 
ATOM 322  O O   . LEU A 1 365 ? 179.730 205.932 219.015 1.00 100.42 ? 365 LEU B O   1 
ATOM 323  C CB  . LEU A 1 365 ? 177.532 205.159 216.857 1.00 99.31  ? 365 LEU B CB  1 
ATOM 324  C CG  . LEU A 1 365 ? 176.327 205.360 215.935 1.00 100.18 ? 365 LEU B CG  1 
ATOM 325  C CD1 . LEU A 1 365 ? 175.348 204.207 216.085 1.00 97.06  ? 365 LEU B CD1 1 
ATOM 326  C CD2 . LEU A 1 365 ? 175.631 206.685 216.220 1.00 94.98  ? 365 LEU B CD2 1 
ATOM 327  N N   . TYR A 1 366 ? 180.801 205.331 217.128 1.00 104.69 ? 366 TYR B N   1 
ATOM 328  C CA  . TYR A 1 366 ? 181.941 204.781 217.853 1.00 104.05 ? 366 TYR B CA  1 
ATOM 329  C C   . TYR A 1 366 ? 182.844 205.863 218.433 1.00 103.04 ? 366 TYR B C   1 
ATOM 330  O O   . TYR A 1 366 ? 183.415 205.667 219.512 1.00 101.66 ? 366 TYR B O   1 
ATOM 331  C CB  . TYR A 1 366 ? 182.745 203.855 216.941 1.00 99.82  ? 366 TYR B CB  1 
ATOM 332  C CG  . TYR A 1 366 ? 182.097 202.506 216.736 1.00 101.04 ? 366 TYR B CG  1 
ATOM 333  C CD1 . TYR A 1 366 ? 181.971 201.609 217.789 1.00 100.78 ? 366 TYR B CD1 1 
ATOM 334  C CD2 . TYR A 1 366 ? 181.607 202.130 215.491 1.00 103.31 ? 366 TYR B CD2 1 
ATOM 335  C CE1 . TYR A 1 366 ? 181.376 200.373 217.608 1.00 104.33 ? 366 TYR B CE1 1 
ATOM 336  C CE2 . TYR A 1 366 ? 181.011 200.896 215.300 1.00 107.06 ? 366 TYR B CE2 1 
ATOM 337  C CZ  . TYR A 1 366 ? 180.899 200.022 216.362 1.00 108.99 ? 366 TYR B CZ  1 
ATOM 338  O OH  . TYR A 1 366 ? 180.307 198.794 216.178 1.00 108.54 ? 366 TYR B OH  1 
ATOM 339  N N   . ASN A 1 367 ? 182.992 206.994 217.750 1.00 103.74 ? 367 ASN B N   1 
ATOM 340  C CA  . ASN A 1 367 ? 183.855 208.073 218.236 1.00 103.19 ? 367 ASN B CA  1 
ATOM 341  C C   . ASN A 1 367 ? 183.080 209.084 219.080 1.00 103.61 ? 367 ASN B C   1 
ATOM 342  O O   . ASN A 1 367 ? 183.146 210.295 218.869 1.00 103.95 ? 367 ASN B O   1 
ATOM 343  C CB  . ASN A 1 367 ? 184.557 208.748 217.061 1.00 105.89 ? 367 ASN B CB  1 
ATOM 344  C CG  . ASN A 1 367 ? 183.587 209.329 216.048 1.00 106.79 ? 367 ASN B CG  1 
ATOM 345  O OD1 . ASN A 1 367 ? 183.074 208.621 215.185 1.00 102.91 ? 367 ASN B OD1 1 
ATOM 346  N ND2 . ASN A 1 367 ? 183.332 210.628 216.152 1.00 109.39 ? 367 ASN B ND2 1 
ATOM 347  N N   . PHE A 1 368 ? 182.355 208.585 220.078 1.00 102.21 ? 368 PHE B N   1 
ATOM 348  C CA  . PHE A 1 368 ? 181.537 209.425 220.942 1.00 98.60  ? 368 PHE B CA  1 
ATOM 349  C C   . PHE A 1 368 ? 182.012 209.448 222.387 1.00 100.40 ? 368 PHE B C   1 
ATOM 350  O O   . PHE A 1 368 ? 182.253 210.525 222.940 1.00 103.98 ? 368 PHE B O   1 
ATOM 351  C CB  . PHE A 1 368 ? 180.074 208.960 220.888 1.00 93.04  ? 368 PHE B CB  1 
ATOM 352  C CG  . PHE A 1 368 ? 179.087 210.021 221.279 1.00 89.34  ? 368 PHE B CG  1 
ATOM 353  C CD1 . PHE A 1 368 ? 178.702 210.997 220.374 1.00 87.57  ? 368 PHE B CD1 1 
ATOM 354  C CD2 . PHE A 1 368 ? 178.545 210.042 222.554 1.00 85.84  ? 368 PHE B CD2 1 
ATOM 355  C CE1 . PHE A 1 368 ? 177.793 211.976 220.734 1.00 82.54  ? 368 PHE B CE1 1 
ATOM 356  C CE2 . PHE A 1 368 ? 177.635 211.017 222.921 1.00 80.90  ? 368 PHE B CE2 1 
ATOM 357  C CZ  . PHE A 1 368 ? 177.260 211.985 222.010 1.00 80.64  ? 368 PHE B CZ  1 
ATOM 358  N N   . ALA A 1 369 ? 182.160 208.285 223.012 1.00 97.06  ? 369 ALA B N   1 
ATOM 359  C CA  . ALA A 1 369 ? 182.391 208.200 224.447 1.00 93.72  ? 369 ALA B CA  1 
ATOM 360  C C   . ALA A 1 369 ? 182.974 206.826 224.757 1.00 92.28  ? 369 ALA B C   1 
ATOM 361  O O   . ALA A 1 369 ? 182.893 205.915 223.924 1.00 90.33  ? 369 ALA B O   1 
ATOM 362  C CB  . ALA A 1 369 ? 181.082 208.433 225.226 1.00 86.31  ? 369 ALA B CB  1 
ATOM 363  N N   . PRO A 1 370 ? 183.595 206.645 225.941 1.00 95.37  ? 370 PRO B N   1 
ATOM 364  C CA  . PRO A 1 370 ? 183.883 205.277 226.395 1.00 91.47  ? 370 PRO B CA  1 
ATOM 365  C C   . PRO A 1 370 ? 182.615 204.594 226.880 1.00 87.33  ? 370 PRO B C   1 
ATOM 366  O O   . PRO A 1 370 ? 182.278 204.645 228.067 1.00 87.95  ? 370 PRO B O   1 
ATOM 367  C CB  . PRO A 1 370 ? 184.914 205.460 227.517 1.00 93.57  ? 370 PRO B CB  1 
ATOM 368  C CG  . PRO A 1 370 ? 185.034 206.916 227.763 1.00 94.89  ? 370 PRO B CG  1 
ATOM 369  C CD  . PRO A 1 370 ? 184.093 207.664 226.886 1.00 96.16  ? 370 PRO B CD  1 
ATOM 370  N N   . PHE A 1 371 ? 181.906 203.977 225.932 1.00 84.12  ? 371 PHE B N   1 
ATOM 371  C CA  . PHE A 1 371 ? 180.556 203.462 226.140 1.00 78.09  ? 371 PHE B CA  1 
ATOM 372  C C   . PHE A 1 371 ? 180.514 202.398 227.232 1.00 72.38  ? 371 PHE B C   1 
ATOM 373  O O   . PHE A 1 371 ? 181.437 201.596 227.391 1.00 73.08  ? 371 PHE B O   1 
ATOM 374  C CB  . PHE A 1 371 ? 180.013 202.872 224.834 1.00 78.96  ? 371 PHE B CB  1 
ATOM 375  C CG  . PHE A 1 371 ? 179.503 203.895 223.846 1.00 81.11  ? 371 PHE B CG  1 
ATOM 376  C CD1 . PHE A 1 371 ? 179.806 205.242 223.974 1.00 84.71  ? 371 PHE B CD1 1 
ATOM 377  C CD2 . PHE A 1 371 ? 178.756 203.490 222.753 1.00 83.95  ? 371 PHE B CD2 1 
ATOM 378  C CE1 . PHE A 1 371 ? 179.342 206.165 223.055 1.00 85.86  ? 371 PHE B CE1 1 
ATOM 379  C CE2 . PHE A 1 371 ? 178.297 204.410 221.826 1.00 83.95  ? 371 PHE B CE2 1 
ATOM 380  C CZ  . PHE A 1 371 ? 178.588 205.748 221.981 1.00 85.29  ? 371 PHE B CZ  1 
ATOM 381  N N   . PHE A 1 372 ? 179.418 202.404 227.989 1.00 66.34  ? 372 PHE B N   1 
ATOM 382  C CA  . PHE A 1 372 ? 179.194 201.445 229.063 1.00 62.83  ? 372 PHE B CA  1 
ATOM 383  C C   . PHE A 1 372 ? 178.626 200.128 228.557 1.00 61.82  ? 372 PHE B C   1 
ATOM 384  O O   . PHE A 1 372 ? 179.152 199.060 228.888 1.00 64.87  ? 372 PHE B O   1 
ATOM 385  C CB  . PHE A 1 372 ? 178.249 202.042 230.108 1.00 63.48  ? 372 PHE B CB  1 
ATOM 386  C CG  . PHE A 1 372 ? 177.888 201.092 231.215 1.00 62.04  ? 372 PHE B CG  1 
ATOM 387  C CD1 . PHE A 1 372 ? 178.819 200.739 232.178 1.00 60.59  ? 372 PHE B CD1 1 
ATOM 388  C CD2 . PHE A 1 372 ? 176.613 200.555 231.293 1.00 60.47  ? 372 PHE B CD2 1 
ATOM 389  C CE1 . PHE A 1 372 ? 178.485 199.867 233.198 1.00 60.08  ? 372 PHE B CE1 1 
ATOM 390  C CE2 . PHE A 1 372 ? 176.274 199.684 232.310 1.00 60.53  ? 372 PHE B CE2 1 
ATOM 391  C CZ  . PHE A 1 372 ? 177.211 199.339 233.263 1.00 60.03  ? 372 PHE B CZ  1 
ATOM 392  N N   . ALA A 1 373 ? 177.560 200.179 227.762 1.00 62.64  ? 373 ALA B N   1 
ATOM 393  C CA  . ALA A 1 373 ? 176.897 198.970 227.295 1.00 66.40  ? 373 ALA B CA  1 
ATOM 394  C C   . ALA A 1 373 ? 176.522 199.120 225.831 1.00 70.18  ? 373 ALA B C   1 
ATOM 395  O O   . ALA A 1 373 ? 175.959 200.142 225.430 1.00 67.84  ? 373 ALA B O   1 
ATOM 396  C CB  . ALA A 1 373 ? 175.646 198.668 228.127 1.00 62.28  ? 373 ALA B CB  1 
ATOM 397  N N   . PHE A 1 374 ? 176.841 198.097 225.038 1.00 76.28  ? 374 PHE B N   1 
ATOM 398  C CA  . PHE A 1 374 ? 176.368 197.980 223.657 1.00 76.89  ? 374 PHE B CA  1 
ATOM 399  C C   . PHE A 1 374 ? 175.985 196.512 223.479 1.00 80.26  ? 374 PHE B C   1 
ATOM 400  O O   . PHE A 1 374 ? 176.803 195.689 223.062 1.00 83.84  ? 374 PHE B O   1 
ATOM 401  C CB  . PHE A 1 374 ? 177.430 198.427 222.661 1.00 77.47  ? 374 PHE B CB  1 
ATOM 402  C CG  . PHE A 1 374 ? 176.980 198.382 221.230 1.00 80.60  ? 374 PHE B CG  1 
ATOM 403  C CD1 . PHE A 1 374 ? 176.130 199.354 220.728 1.00 80.67  ? 374 PHE B CD1 1 
ATOM 404  C CD2 . PHE A 1 374 ? 177.411 197.373 220.385 1.00 85.92  ? 374 PHE B CD2 1 
ATOM 405  C CE1 . PHE A 1 374 ? 175.713 199.318 219.411 1.00 87.26  ? 374 PHE B CE1 1 
ATOM 406  C CE2 . PHE A 1 374 ? 176.999 197.331 219.067 1.00 91.20  ? 374 PHE B CE2 1 
ATOM 407  C CZ  . PHE A 1 374 ? 176.149 198.305 218.579 1.00 92.62  ? 374 PHE B CZ  1 
ATOM 408  N N   . LYS A 1 375 ? 174.734 196.194 223.803 1.00 78.90  ? 375 LYS B N   1 
ATOM 409  C CA  . LYS A 1 375 ? 174.238 194.824 223.815 1.00 84.55  ? 375 LYS B CA  1 
ATOM 410  C C   . LYS A 1 375 ? 172.953 194.755 223.011 1.00 88.07  ? 375 LYS B C   1 
ATOM 411  O O   . LYS A 1 375 ? 172.015 195.511 223.283 1.00 85.49  ? 375 LYS B O   1 
ATOM 412  C CB  . LYS A 1 375 ? 173.977 194.346 225.247 1.00 89.59  ? 375 LYS B CB  1 
ATOM 413  C CG  . LYS A 1 375 ? 175.220 194.156 226.093 1.00 92.52  ? 375 LYS B CG  1 
ATOM 414  C CD  . LYS A 1 375 ? 174.842 193.756 227.510 1.00 99.46  ? 375 LYS B CD  1 
ATOM 415  C CE  . LYS A 1 375 ? 174.285 192.343 227.557 1.00 104.96 ? 375 LYS B CE  1 
ATOM 416  N NZ  . LYS A 1 375 ? 175.321 191.324 227.237 1.00 109.73 ? 375 LYS B NZ  1 
ATOM 417  N N   . CYS A 1 376 ? 172.900 193.841 222.043 1.00 92.89  ? 376 CYS B N   1 
ATOM 418  C CA  . CYS A 1 376 ? 171.702 193.717 221.224 1.00 94.32  ? 376 CYS B CA  1 
ATOM 419  C C   . CYS A 1 376 ? 171.617 192.361 220.546 1.00 97.81  ? 376 CYS B C   1 
ATOM 420  O O   . CYS A 1 376 ? 172.593 191.610 220.470 1.00 99.32  ? 376 CYS B O   1 
ATOM 421  C CB  . CYS A 1 376 ? 171.611 194.844 220.200 1.00 90.07  ? 376 CYS B CB  1 
ATOM 422  S SG  . CYS A 1 376 ? 172.865 195.051 218.918 1.00 94.89  ? 376 CYS B SG  1 
ATOM 423  N N   . TYR A 1 377 ? 170.414 192.072 220.051 1.00 98.38  ? 377 TYR B N   1 
ATOM 424  C CA  . TYR A 1 377 ? 170.032 190.764 219.547 1.00 104.22 ? 377 TYR B CA  1 
ATOM 425  C C   . TYR A 1 377 ? 169.461 190.916 218.146 1.00 103.78 ? 377 TYR B C   1 
ATOM 426  O O   . TYR A 1 377 ? 168.779 191.902 217.851 1.00 97.97  ? 377 TYR B O   1 
ATOM 427  C CB  . TYR A 1 377 ? 168.980 190.120 220.456 1.00 108.59 ? 377 TYR B CB  1 
ATOM 428  C CG  . TYR A 1 377 ? 169.477 189.792 221.844 1.00 113.45 ? 377 TYR B CG  1 
ATOM 429  C CD1 . TYR A 1 377 ? 170.222 188.647 222.091 1.00 114.20 ? 377 TYR B CD1 1 
ATOM 430  C CD2 . TYR A 1 377 ? 169.200 190.639 222.911 1.00 113.44 ? 377 TYR B CD2 1 
ATOM 431  C CE1 . TYR A 1 377 ? 170.675 188.352 223.365 1.00 117.21 ? 377 TYR B CE1 1 
ATOM 432  C CE2 . TYR A 1 377 ? 169.648 190.355 224.186 1.00 118.10 ? 377 TYR B CE2 1 
ATOM 433  C CZ  . TYR A 1 377 ? 170.385 189.211 224.408 1.00 123.69 ? 377 TYR B CZ  1 
ATOM 434  O OH  . TYR A 1 377 ? 170.832 188.925 225.677 1.00 125.41 ? 377 TYR B OH  1 
ATOM 435  N N   . GLY A 1 378 ? 169.736 189.938 217.286 1.00 106.57 ? 378 GLY B N   1 
ATOM 436  C CA  . GLY A 1 378 ? 169.134 189.882 215.972 1.00 106.34 ? 378 GLY B CA  1 
ATOM 437  C C   . GLY A 1 378 ? 169.944 190.494 214.850 1.00 104.05 ? 378 GLY B C   1 
ATOM 438  O O   . GLY A 1 378 ? 169.640 190.231 213.679 1.00 105.23 ? 378 GLY B O   1 
ATOM 439  N N   . VAL A 1 379 ? 170.958 191.300 215.158 1.00 101.40 ? 379 VAL B N   1 
ATOM 440  C CA  . VAL A 1 379 ? 171.816 191.879 214.132 1.00 101.85 ? 379 VAL B CA  1 
ATOM 441  C C   . VAL A 1 379 ? 173.213 192.048 214.716 1.00 102.77 ? 379 VAL B C   1 
ATOM 442  O O   . VAL A 1 379 ? 173.382 192.280 215.917 1.00 101.39 ? 379 VAL B O   1 
ATOM 443  C CB  . VAL A 1 379 ? 171.228 193.210 213.589 1.00 104.97 ? 379 VAL B CB  1 
ATOM 444  C CG1 . VAL A 1 379 ? 171.285 194.326 214.631 1.00 101.61 ? 379 VAL B CG1 1 
ATOM 445  C CG2 . VAL A 1 379 ? 171.899 193.619 212.280 1.00 108.52 ? 379 VAL B CG2 1 
ATOM 446  N N   . SER A 1 380 ? 174.223 191.877 213.863 1.00 103.51 ? 380 SER B N   1 
ATOM 447  C CA  . SER A 1 380 ? 175.610 191.992 214.283 1.00 105.95 ? 380 SER B CA  1 
ATOM 448  C C   . SER A 1 380 ? 176.048 193.456 214.303 1.00 105.86 ? 380 SER B C   1 
ATOM 449  O O   . SER A 1 380 ? 175.557 194.269 213.515 1.00 105.62 ? 380 SER B O   1 
ATOM 450  C CB  . SER A 1 380 ? 176.510 191.189 213.347 1.00 109.82 ? 380 SER B CB  1 
ATOM 451  O OG  . SER A 1 380 ? 177.872 191.550 213.497 1.00 111.67 ? 380 SER B OG  1 
ATOM 452  N N   . PRO A 1 381 ? 176.966 193.820 215.211 1.00 105.95 ? 381 PRO B N   1 
ATOM 453  C CA  . PRO A 1 381 ? 177.456 195.206 215.261 1.00 107.42 ? 381 PRO B CA  1 
ATOM 454  C C   . PRO A 1 381 ? 178.253 195.617 214.032 1.00 109.34 ? 381 PRO B C   1 
ATOM 455  O O   . PRO A 1 381 ? 177.985 196.663 213.432 1.00 108.75 ? 381 PRO B O   1 
ATOM 456  C CB  . PRO A 1 381 ? 178.340 195.215 216.514 1.00 107.96 ? 381 PRO B CB  1 
ATOM 457  C CG  . PRO A 1 381 ? 177.800 194.116 217.359 1.00 106.86 ? 381 PRO B CG  1 
ATOM 458  C CD  . PRO A 1 381 ? 177.399 193.047 216.388 1.00 106.13 ? 381 PRO B CD  1 
ATOM 459  N N   . THR A 1 382 ? 179.240 194.806 213.652 1.00 110.54 ? 382 THR B N   1 
ATOM 460  C CA  . THR A 1 382 ? 180.092 195.136 212.517 1.00 108.74 ? 382 THR B CA  1 
ATOM 461  C C   . THR A 1 382 ? 179.416 194.902 211.173 1.00 106.61 ? 382 THR B C   1 
ATOM 462  O O   . THR A 1 382 ? 179.937 195.359 210.150 1.00 105.68 ? 382 THR B O   1 
ATOM 463  C CB  . THR A 1 382 ? 181.398 194.335 212.584 1.00 108.03 ? 382 THR B CB  1 
ATOM 464  O OG1 . THR A 1 382 ? 182.357 194.902 211.682 1.00 107.27 ? 382 THR B OG1 1 
ATOM 465  C CG2 . THR A 1 382 ? 181.162 192.875 212.219 1.00 107.56 ? 382 THR B CG2 1 
ATOM 466  N N   . LYS A 1 383 ? 178.277 194.214 211.146 1.00 107.19 ? 383 LYS B N   1 
ATOM 467  C CA  . LYS A 1 383 ? 177.574 193.922 209.906 1.00 109.73 ? 383 LYS B CA  1 
ATOM 468  C C   . LYS A 1 383 ? 176.498 194.945 209.578 1.00 110.07 ? 383 LYS B C   1 
ATOM 469  O O   . LYS A 1 383 ? 175.790 194.772 208.584 1.00 111.89 ? 383 LYS B O   1 
ATOM 470  C CB  . LYS A 1 383 ? 176.948 192.526 209.966 1.00 112.61 ? 383 LYS B CB  1 
ATOM 471  C CG  . LYS A 1 383 ? 177.896 191.393 209.610 1.00 115.28 ? 383 LYS B CG  1 
ATOM 472  C CD  . LYS A 1 383 ? 177.195 190.043 209.683 1.00 117.36 ? 383 LYS B CD  1 
ATOM 473  C CE  . LYS A 1 383 ? 175.920 190.030 208.851 1.00 117.30 ? 383 LYS B CE  1 
ATOM 474  N NZ  . LYS A 1 383 ? 174.868 189.166 209.454 1.00 118.09 ? 383 LYS B NZ  1 
ATOM 475  N N   . LEU A 1 384 ? 176.360 196.004 210.383 1.00 110.07 ? 384 LEU B N   1 
ATOM 476  C CA  . LEU A 1 384 ? 175.311 196.998 210.166 1.00 109.79 ? 384 LEU B CA  1 
ATOM 477  C C   . LEU A 1 384 ? 175.484 197.777 208.868 1.00 110.20 ? 384 LEU B C   1 
ATOM 478  O O   . LEU A 1 384 ? 174.513 198.368 208.384 1.00 109.33 ? 384 LEU B O   1 
ATOM 479  C CB  . LEU A 1 384 ? 175.261 197.980 211.338 1.00 107.46 ? 384 LEU B CB  1 
ATOM 480  C CG  . LEU A 1 384 ? 174.837 197.463 212.712 1.00 107.53 ? 384 LEU B CG  1 
ATOM 481  C CD1 . LEU A 1 384 ? 174.998 198.554 213.757 1.00 103.39 ? 384 LEU B CD1 1 
ATOM 482  C CD2 . LEU A 1 384 ? 173.399 196.985 212.667 1.00 104.79 ? 384 LEU B CD2 1 
ATOM 483  N N   . ASN A 1 385 ? 176.691 197.798 208.300 1.00 111.46 ? 385 ASN B N   1 
ATOM 484  C CA  . ASN A 1 385 ? 176.931 198.608 207.111 1.00 114.76 ? 385 ASN B CA  1 
ATOM 485  C C   . ASN A 1 385 ? 176.322 197.978 205.862 1.00 114.77 ? 385 ASN B C   1 
ATOM 486  O O   . ASN A 1 385 ? 175.770 198.688 205.014 1.00 110.25 ? 385 ASN B O   1 
ATOM 487  C CB  . ASN A 1 385 ? 178.433 198.826 206.922 1.00 114.78 ? 385 ASN B CB  1 
ATOM 488  C CG  . ASN A 1 385 ? 179.001 199.843 207.893 1.00 112.28 ? 385 ASN B CG  1 
ATOM 489  O OD1 . ASN A 1 385 ? 178.575 200.997 207.922 1.00 107.66 ? 385 ASN B OD1 1 
ATOM 490  N ND2 . ASN A 1 385 ? 179.971 199.418 208.694 1.00 110.26 ? 385 ASN B ND2 1 
ATOM 491  N N   . ASP A 1 386 ? 176.404 196.653 205.727 1.00 116.50 ? 386 ASP B N   1 
ATOM 492  C CA  . ASP A 1 386 ? 176.094 195.995 204.464 1.00 118.58 ? 386 ASP B CA  1 
ATOM 493  C C   . ASP A 1 386 ? 174.747 195.267 204.457 1.00 116.26 ? 386 ASP B C   1 
ATOM 494  O O   . ASP A 1 386 ? 174.620 194.227 203.801 1.00 117.05 ? 386 ASP B O   1 
ATOM 495  C CB  . ASP A 1 386 ? 177.235 195.052 204.061 1.00 120.92 ? 386 ASP B CB  1 
ATOM 496  C CG  . ASP A 1 386 ? 177.473 193.920 205.057 1.00 123.60 ? 386 ASP B CG  1 
ATOM 497  O OD1 . ASP A 1 386 ? 176.800 193.855 206.105 1.00 121.95 ? 386 ASP B OD1 1 
ATOM 498  O OD2 . ASP A 1 386 ? 178.354 193.080 204.781 1.00 124.66 ? 386 ASP B OD2 1 
ATOM 499  N N   . LEU A 1 387 ? 173.743 195.783 205.164 1.00 112.00 ? 387 LEU B N   1 
ATOM 500  C CA  . LEU A 1 387 ? 172.361 195.396 204.913 1.00 108.43 ? 387 LEU B CA  1 
ATOM 501  C C   . LEU A 1 387 ? 171.512 196.659 204.883 1.00 106.66 ? 387 LEU B C   1 
ATOM 502  O O   . LEU A 1 387 ? 172.023 197.778 204.991 1.00 105.01 ? 387 LEU B O   1 
ATOM 503  C CB  . LEU A 1 387 ? 171.809 194.406 205.955 1.00 104.88 ? 387 LEU B CB  1 
ATOM 504  C CG  . LEU A 1 387 ? 171.443 194.797 207.390 1.00 102.73 ? 387 LEU B CG  1 
ATOM 505  C CD1 . LEU A 1 387 ? 170.595 193.690 208.004 1.00 98.10  ? 387 LEU B CD1 1 
ATOM 506  C CD2 . LEU A 1 387 ? 172.635 195.091 208.262 1.00 106.17 ? 387 LEU B CD2 1 
ATOM 507  N N   . CYS A 1 388 ? 170.202 196.481 204.735 1.00 105.40 ? 388 CYS B N   1 
ATOM 508  C CA  . CYS A 1 388 ? 169.297 197.608 204.582 1.00 103.73 ? 388 CYS B CA  1 
ATOM 509  C C   . CYS A 1 388 ? 168.045 197.397 205.424 1.00 98.87  ? 388 CYS B C   1 
ATOM 510  O O   . CYS A 1 388 ? 167.598 196.268 205.645 1.00 99.90  ? 388 CYS B O   1 
ATOM 511  C CB  . CYS A 1 388 ? 168.914 197.806 203.107 1.00 107.79 ? 388 CYS B CB  1 
ATOM 512  S SG  . CYS A 1 388 ? 170.235 198.514 202.083 1.00 119.75 ? 388 CYS B SG  1 
ATOM 513  N N   . PHE A 1 389 ? 167.488 198.509 205.897 1.00 95.09  ? 389 PHE B N   1 
ATOM 514  C CA  . PHE A 1 389 ? 166.184 198.542 206.551 1.00 90.28  ? 389 PHE B CA  1 
ATOM 515  C C   . PHE A 1 389 ? 165.375 199.653 205.891 1.00 93.23  ? 389 PHE B C   1 
ATOM 516  O O   . PHE A 1 389 ? 165.827 200.283 204.929 1.00 97.41  ? 389 PHE B O   1 
ATOM 517  C CB  . PHE A 1 389 ? 166.317 198.743 208.068 1.00 86.08  ? 389 PHE B CB  1 
ATOM 518  C CG  . PHE A 1 389 ? 167.047 197.634 208.775 1.00 87.92  ? 389 PHE B CG  1 
ATOM 519  C CD1 . PHE A 1 389 ? 168.425 197.668 208.918 1.00 93.22  ? 389 PHE B CD1 1 
ATOM 520  C CD2 . PHE A 1 389 ? 166.349 196.564 209.311 1.00 87.61  ? 389 PHE B CD2 1 
ATOM 521  C CE1 . PHE A 1 389 ? 169.093 196.652 209.574 1.00 96.84  ? 389 PHE B CE1 1 
ATOM 522  C CE2 . PHE A 1 389 ? 167.011 195.543 209.969 1.00 89.98  ? 389 PHE B CE2 1 
ATOM 523  C CZ  . PHE A 1 389 ? 168.385 195.589 210.102 1.00 96.16  ? 389 PHE B CZ  1 
ATOM 524  N N   . THR A 1 390 ? 164.165 199.905 206.398 1.00 88.62  ? 390 THR B N   1 
ATOM 525  C CA  . THR A 1 390 ? 163.301 200.925 205.805 1.00 87.86  ? 390 THR B CA  1 
ATOM 526  C C   . THR A 1 390 ? 162.937 202.030 206.792 1.00 87.29  ? 390 THR B C   1 
ATOM 527  O O   . THR A 1 390 ? 162.923 203.197 206.395 1.00 88.85  ? 390 THR B O   1 
ATOM 528  C CB  . THR A 1 390 ? 162.069 200.275 205.159 1.00 89.20  ? 390 THR B CB  1 
ATOM 529  O OG1 . THR A 1 390 ? 161.314 201.265 204.445 1.00 91.82  ? 390 THR B OG1 1 
ATOM 530  C CG2 . THR A 1 390 ? 161.184 199.545 206.155 1.00 89.01  ? 390 THR B CG2 1 
ATOM 531  N N   . ASN A 1 391 ? 162.644 201.726 208.059 1.00 87.68  ? 391 ASN B N   1 
ATOM 532  C CA  . ASN A 1 391 ? 162.300 202.758 209.038 1.00 86.31  ? 391 ASN B CA  1 
ATOM 533  C C   . ASN A 1 391 ? 162.922 202.413 210.391 1.00 83.51  ? 391 ASN B C   1 
ATOM 534  O O   . ASN A 1 391 ? 162.468 201.498 211.084 1.00 84.76  ? 391 ASN B O   1 
ATOM 535  C CB  . ASN A 1 391 ? 160.784 202.937 209.141 1.00 87.09  ? 391 ASN B CB  1 
ATOM 536  C CG  . ASN A 1 391 ? 160.029 201.619 209.202 1.00 88.45  ? 391 ASN B CG  1 
ATOM 537  O OD1 . ASN A 1 391 ? 160.622 200.543 209.166 1.00 90.66  ? 391 ASN B OD1 1 
ATOM 538  N ND2 . ASN A 1 391 ? 158.706 201.703 209.286 1.00 87.37  ? 391 ASN B ND2 1 
ATOM 539  N N   . VAL A 1 392 ? 163.962 203.148 210.762 1.00 75.04  ? 392 VAL B N   1 
ATOM 540  C CA  . VAL A 1 392 ? 164.578 203.016 212.076 1.00 70.62  ? 392 VAL B CA  1 
ATOM 541  C C   . VAL A 1 392 ? 164.049 204.119 212.987 1.00 71.75  ? 392 VAL B C   1 
ATOM 542  O O   . VAL A 1 392 ? 163.792 205.250 212.558 1.00 75.82  ? 392 VAL B O   1 
ATOM 543  C CB  . VAL A 1 392 ? 166.122 203.022 211.968 1.00 70.00  ? 392 VAL B CB  1 
ATOM 544  C CG1 . VAL A 1 392 ? 166.647 204.356 211.465 1.00 68.55  ? 392 VAL B CG1 1 
ATOM 545  C CG2 . VAL A 1 392 ? 166.765 202.666 213.303 1.00 71.92  ? 392 VAL B CG2 1 
ATOM 546  N N   . TYR A 1 393 ? 163.832 203.771 214.252 1.00 71.06  ? 393 TYR B N   1 
ATOM 547  C CA  . TYR A 1 393 ? 163.420 204.714 215.276 1.00 69.42  ? 393 TYR B CA  1 
ATOM 548  C C   . TYR A 1 393 ? 164.550 204.884 216.283 1.00 65.85  ? 393 TYR B C   1 
ATOM 549  O O   . TYR A 1 393 ? 165.402 204.006 216.444 1.00 65.51  ? 393 TYR B O   1 
ATOM 550  C CB  . TYR A 1 393 ? 162.157 204.240 216.005 1.00 68.84  ? 393 TYR B CB  1 
ATOM 551  C CG  . TYR A 1 393 ? 160.874 204.365 215.218 1.00 70.76  ? 393 TYR B CG  1 
ATOM 552  C CD1 . TYR A 1 393 ? 160.608 205.491 214.451 1.00 77.08  ? 393 TYR B CD1 1 
ATOM 553  C CD2 . TYR A 1 393 ? 159.927 203.351 215.245 1.00 71.02  ? 393 TYR B CD2 1 
ATOM 554  C CE1 . TYR A 1 393 ? 159.430 205.603 213.733 1.00 80.72  ? 393 TYR B CE1 1 
ATOM 555  C CE2 . TYR A 1 393 ? 158.748 203.452 214.532 1.00 76.14  ? 393 TYR B CE2 1 
ATOM 556  C CZ  . TYR A 1 393 ? 158.505 204.580 213.777 1.00 81.57  ? 393 TYR B CZ  1 
ATOM 557  O OH  . TYR A 1 393 ? 157.332 204.684 213.065 1.00 86.23  ? 393 TYR B OH  1 
ATOM 558  N N   . ALA A 1 394 ? 164.552 206.028 216.960 1.00 62.22  ? 394 ALA B N   1 
ATOM 559  C CA  . ALA A 1 394 ? 165.502 206.278 218.033 1.00 58.95  ? 394 ALA B CA  1 
ATOM 560  C C   . ALA A 1 394 ? 164.804 207.019 219.161 1.00 60.86  ? 394 ALA B C   1 
ATOM 561  O O   . ALA A 1 394 ? 164.074 207.984 218.921 1.00 63.75  ? 394 ALA B O   1 
ATOM 562  C CB  . ALA A 1 394 ? 166.707 207.086 217.543 1.00 56.22  ? 394 ALA B CB  1 
ATOM 563  N N   . ASP A 1 395 ? 165.034 206.563 220.389 1.00 58.36  ? 395 ASP B N   1 
ATOM 564  C CA  . ASP A 1 395 ? 164.505 207.223 221.572 1.00 56.19  ? 395 ASP B CA  1 
ATOM 565  C C   . ASP A 1 395 ? 165.599 207.341 222.623 1.00 50.28  ? 395 ASP B C   1 
ATOM 566  O O   . ASP A 1 395 ? 166.541 206.547 222.649 1.00 53.68  ? 395 ASP B O   1 
ATOM 567  C CB  . ASP A 1 395 ? 163.267 206.490 222.123 1.00 60.79  ? 395 ASP B CB  1 
ATOM 568  C CG  . ASP A 1 395 ? 163.461 204.984 222.234 1.00 62.94  ? 395 ASP B CG  1 
ATOM 569  O OD1 . ASP A 1 395 ? 164.611 204.505 222.234 1.00 62.64  ? 395 ASP B OD1 1 
ATOM 570  O OD2 . ASP A 1 395 ? 162.440 204.270 222.323 1.00 66.56  ? 395 ASP B OD2 1 
ATOM 571  N N   . SER A 1 396 ? 165.476 208.351 223.482 1.00 46.09  ? 396 SER B N   1 
ATOM 572  C CA  . SER A 1 396 ? 166.519 208.664 224.446 1.00 48.59  ? 396 SER B CA  1 
ATOM 573  C C   . SER A 1 396 ? 165.907 209.040 225.786 1.00 51.11  ? 396 SER B C   1 
ATOM 574  O O   . SER A 1 396 ? 164.925 209.784 225.843 1.00 54.41  ? 396 SER B O   1 
ATOM 575  C CB  . SER A 1 396 ? 167.411 209.806 223.944 1.00 50.88  ? 396 SER B CB  1 
ATOM 576  O OG  . SER A 1 396 ? 166.686 211.019 223.854 1.00 52.85  ? 396 SER B OG  1 
ATOM 577  N N   . PHE A 1 397 ? 166.508 208.527 226.857 1.00 48.49  ? 397 PHE B N   1 
ATOM 578  C CA  . PHE A 1 397 ? 166.102 208.797 228.231 1.00 45.09  ? 397 PHE B CA  1 
ATOM 579  C C   . PHE A 1 397 ? 167.236 208.355 229.145 1.00 49.20  ? 397 PHE B C   1 
ATOM 580  O O   . PHE A 1 397 ? 168.135 207.618 228.734 1.00 52.78  ? 397 PHE B O   1 
ATOM 581  C CB  . PHE A 1 397 ? 164.787 208.094 228.589 1.00 47.77  ? 397 PHE B CB  1 
ATOM 582  C CG  . PHE A 1 397 ? 164.707 206.665 228.125 1.00 49.85  ? 397 PHE B CG  1 
ATOM 583  C CD1 . PHE A 1 397 ? 165.222 205.636 228.891 1.00 49.17  ? 397 PHE B CD1 1 
ATOM 584  C CD2 . PHE A 1 397 ? 164.105 206.353 226.918 1.00 57.13  ? 397 PHE B CD2 1 
ATOM 585  C CE1 . PHE A 1 397 ? 165.137 204.328 228.457 1.00 52.94  ? 397 PHE B CE1 1 
ATOM 586  C CE2 . PHE A 1 397 ? 164.021 205.048 226.483 1.00 58.16  ? 397 PHE B CE2 1 
ATOM 587  C CZ  . PHE A 1 397 ? 164.538 204.035 227.255 1.00 57.39  ? 397 PHE B CZ  1 
ATOM 588  N N   . VAL A 1 398 ? 167.186 208.814 230.394 1.00 50.04  ? 398 VAL B N   1 
ATOM 589  C CA  . VAL A 1 398 ? 168.225 208.529 231.377 1.00 51.05  ? 398 VAL B CA  1 
ATOM 590  C C   . VAL A 1 398 ? 167.603 207.816 232.575 1.00 49.41  ? 398 VAL B C   1 
ATOM 591  O O   . VAL A 1 398 ? 166.496 208.148 233.010 1.00 51.93  ? 398 VAL B O   1 
ATOM 592  C CB  . VAL A 1 398 ? 168.978 209.818 231.782 1.00 47.25  ? 398 VAL B CB  1 
ATOM 593  C CG1 . VAL A 1 398 ? 168.087 210.791 232.492 1.00 44.40  ? 398 VAL B CG1 1 
ATOM 594  C CG2 . VAL A 1 398 ? 170.173 209.499 232.639 1.00 47.70  ? 398 VAL B CG2 1 
ATOM 595  N N   . ILE A 1 399 ? 168.305 206.800 233.077 1.00 46.32  ? 399 ILE B N   1 
ATOM 596  C CA  . ILE A 1 399 ? 167.808 205.916 234.122 1.00 43.74  ? 399 ILE B CA  1 
ATOM 597  C C   . ILE A 1 399 ? 168.868 205.869 235.218 1.00 46.03  ? 399 ILE B C   1 
ATOM 598  O O   . ILE A 1 399 ? 170.046 206.144 234.967 1.00 48.05  ? 399 ILE B O   1 
ATOM 599  C CB  . ILE A 1 399 ? 167.497 204.511 233.528 1.00 44.64  ? 399 ILE B CB  1 
ATOM 600  C CG1 . ILE A 1 399 ? 166.265 204.577 232.645 1.00 47.55  ? 399 ILE B CG1 1 
ATOM 601  C CG2 . ILE A 1 399 ? 167.169 203.437 234.562 1.00 50.91  ? 399 ILE B CG2 1 
ATOM 602  C CD1 . ILE A 1 399 ? 166.189 203.444 231.689 1.00 54.71  ? 399 ILE B CD1 1 
ATOM 603  N N   . LYS A 1 400 ? 168.429 205.591 236.453 1.00 45.80  ? 400 LYS B N   1 
ATOM 604  C CA  . LYS A 1 400 ? 169.320 205.196 237.539 1.00 42.77  ? 400 LYS B CA  1 
ATOM 605  C C   . LYS A 1 400 ? 170.283 204.101 237.091 1.00 45.37  ? 400 LYS B C   1 
ATOM 606  O O   . LYS A 1 400 ? 169.946 203.241 236.271 1.00 46.24  ? 400 LYS B O   1 
ATOM 607  C CB  . LYS A 1 400 ? 168.495 204.699 238.729 1.00 43.45  ? 400 LYS B CB  1 
ATOM 608  C CG  . LYS A 1 400 ? 169.173 204.836 240.075 1.00 44.23  ? 400 LYS B CG  1 
ATOM 609  C CD  . LYS A 1 400 ? 168.148 205.027 241.179 1.00 46.44  ? 400 LYS B CD  1 
ATOM 610  C CE  . LYS A 1 400 ? 167.334 203.760 241.392 1.00 46.98  ? 400 LYS B CE  1 
ATOM 611  N NZ  . LYS A 1 400 ? 166.935 203.584 242.814 1.00 45.89  ? 400 LYS B NZ  1 
ATOM 612  N N   . GLY A 1 401 ? 171.493 204.133 237.655 1.00 44.19  ? 401 GLY B N   1 
ATOM 613  C CA  . GLY A 1 401 ? 172.557 203.261 237.178 1.00 40.79  ? 401 GLY B CA  1 
ATOM 614  C C   . GLY A 1 401 ? 172.294 201.786 237.418 1.00 38.58  ? 401 GLY B C   1 
ATOM 615  O O   . GLY A 1 401 ? 172.667 200.941 236.600 1.00 39.40  ? 401 GLY B O   1 
ATOM 616  N N   . ASN A 1 402 ? 171.649 201.455 238.534 1.00 41.10  ? 402 ASN B N   1 
ATOM 617  C CA  . ASN A 1 402 ? 171.383 200.066 238.892 1.00 43.83  ? 402 ASN B CA  1 
ATOM 618  C C   . ASN A 1 402 ? 170.192 199.450 238.163 1.00 41.78  ? 402 ASN B C   1 
ATOM 619  O O   . ASN A 1 402 ? 169.747 198.364 238.548 1.00 41.20  ? 402 ASN B O   1 
ATOM 620  C CB  . ASN A 1 402 ? 171.264 199.943 240.430 1.00 49.02  ? 402 ASN B CB  1 
ATOM 621  C CG  . ASN A 1 402 ? 169.857 200.291 241.021 1.00 49.12  ? 402 ASN B CG  1 
ATOM 622  O OD1 . ASN A 1 402 ? 168.910 200.699 240.346 1.00 48.26  ? 402 ASN B OD1 1 
ATOM 623  N ND2 . ASN A 1 402 ? 169.752 200.104 242.331 1.00 50.58  ? 402 ASN B ND2 1 
ATOM 624  N N   . GLU A 1 403 ? 169.669 200.104 237.129 1.00 44.42  ? 403 GLU B N   1 
ATOM 625  C CA  . GLU A 1 403 ? 168.434 199.627 236.523 1.00 49.91  ? 403 GLU B CA  1 
ATOM 626  C C   . GLU A 1 403 ? 168.534 199.736 234.996 1.00 53.53  ? 403 GLU B C   1 
ATOM 627  O O   . GLU A 1 403 ? 167.519 199.669 234.292 1.00 55.51  ? 403 GLU B O   1 
ATOM 628  C CB  . GLU A 1 403 ? 167.280 200.408 237.197 1.00 56.19  ? 403 GLU B CB  1 
ATOM 629  C CG  . GLU A 1 403 ? 165.842 200.081 236.840 1.00 67.78  ? 403 GLU B CG  1 
ATOM 630  C CD  . GLU A 1 403 ? 164.865 200.915 237.643 1.00 76.30  ? 403 GLU B CD  1 
ATOM 631  O OE1 . GLU A 1 403 ? 165.326 201.750 238.449 1.00 73.63  ? 403 GLU B OE1 1 
ATOM 632  O OE2 . GLU A 1 403 ? 163.644 200.696 237.526 1.00 82.39  ? 403 GLU B OE2 1 
ATOM 633  N N   . VAL A 1 404 ? 169.758 199.868 234.474 1.00 52.24  ? 404 VAL B N   1 
ATOM 634  C CA  . VAL A 1 404 ? 170.008 199.823 233.035 1.00 50.52  ? 404 VAL B CA  1 
ATOM 635  C C   . VAL A 1 404 ? 169.675 198.447 232.472 1.00 51.57  ? 404 VAL B C   1 
ATOM 636  O O   . VAL A 1 404 ? 169.224 198.325 231.325 1.00 54.86  ? 404 VAL B O   1 
ATOM 637  C CB  . VAL A 1 404 ? 171.475 200.218 232.759 1.00 50.37  ? 404 VAL B CB  1 
ATOM 638  C CG1 . VAL A 1 404 ? 171.799 200.192 231.270 1.00 50.28  ? 404 VAL B CG1 1 
ATOM 639  C CG2 . VAL A 1 404 ? 171.777 201.586 233.354 1.00 53.31  ? 404 VAL B CG2 1 
ATOM 640  N N   . SER A 1 405 ? 169.859 197.394 233.277 1.00 49.94  ? 405 SER B N   1 
ATOM 641  C CA  . SER A 1 405 ? 169.636 196.021 232.831 1.00 53.32  ? 405 SER B CA  1 
ATOM 642  C C   . SER A 1 405 ? 168.184 195.735 232.460 1.00 57.82  ? 405 SER B C   1 
ATOM 643  O O   . SER A 1 405 ? 167.922 194.746 231.767 1.00 65.14  ? 405 SER B O   1 
ATOM 644  C CB  . SER A 1 405 ? 170.088 195.044 233.918 1.00 54.51  ? 405 SER B CB  1 
ATOM 645  O OG  . SER A 1 405 ? 169.843 193.701 233.537 1.00 56.17  ? 405 SER B OG  1 
ATOM 646  N N   . GLN A 1 406 ? 167.238 196.563 232.903 1.00 56.09  ? 406 GLN B N   1 
ATOM 647  C CA  . GLN A 1 406 ? 165.838 196.366 232.548 1.00 60.42  ? 406 GLN B CA  1 
ATOM 648  C C   . GLN A 1 406 ? 165.507 196.795 231.124 1.00 63.23  ? 406 GLN B C   1 
ATOM 649  O O   . GLN A 1 406 ? 164.419 196.466 230.639 1.00 68.94  ? 406 GLN B O   1 
ATOM 650  C CB  . GLN A 1 406 ? 164.932 197.114 233.529 1.00 63.18  ? 406 GLN B CB  1 
ATOM 651  C CG  . GLN A 1 406 ? 164.796 196.438 234.880 1.00 68.97  ? 406 GLN B CG  1 
ATOM 652  C CD  . GLN A 1 406 ? 163.842 197.166 235.803 1.00 76.16  ? 406 GLN B CD  1 
ATOM 653  O OE1 . GLN A 1 406 ? 162.807 197.672 235.372 1.00 77.07  ? 406 GLN B OE1 1 
ATOM 654  N NE2 . GLN A 1 406 ? 164.174 197.198 237.088 1.00 76.64  ? 406 GLN B NE2 1 
ATOM 655  N N   . ILE A 1 407 ? 166.397 197.510 230.443 1.00 58.84  ? 407 ILE B N   1 
ATOM 656  C CA  . ILE A 1 407 ? 166.140 197.932 229.053 1.00 58.69  ? 407 ILE B CA  1 
ATOM 657  C C   . ILE A 1 407 ? 166.652 196.801 228.170 1.00 64.81  ? 407 ILE B C   1 
ATOM 658  O O   . ILE A 1 407 ? 167.762 196.825 227.630 1.00 66.48  ? 407 ILE B O   1 
ATOM 659  C CB  . ILE A 1 407 ? 166.771 199.288 228.726 1.00 59.39  ? 407 ILE B CB  1 
ATOM 660  C CG1 . ILE A 1 407 ? 166.354 200.349 229.746 1.00 59.94  ? 407 ILE B CG1 1 
ATOM 661  C CG2 . ILE A 1 407 ? 166.350 199.747 227.342 1.00 59.00  ? 407 ILE B CG2 1 
ATOM 662  C CD1 . ILE A 1 407 ? 164.859 200.379 230.062 1.00 60.59  ? 407 ILE B CD1 1 
ATOM 663  N N   . ALA A 1 408 ? 165.805 195.794 228.007 1.00 69.65  ? 408 ALA B N   1 
ATOM 664  C CA  . ALA A 1 408 ? 166.087 194.572 227.266 1.00 73.13  ? 408 ALA B CA  1 
ATOM 665  C C   . ALA A 1 408 ? 164.773 193.805 227.132 1.00 75.68  ? 408 ALA B C   1 
ATOM 666  O O   . ALA A 1 408 ? 163.852 194.024 227.923 1.00 75.51  ? 408 ALA B O   1 
ATOM 667  C CB  . ALA A 1 408 ? 167.151 193.716 227.980 1.00 71.68  ? 408 ALA B CB  1 
ATOM 668  N N   . PRO A 1 409 ? 164.645 192.929 226.133 1.00 76.83  ? 409 PRO B N   1 
ATOM 669  C CA  . PRO A 1 409 ? 163.403 192.153 226.017 1.00 75.07  ? 409 PRO B CA  1 
ATOM 670  C C   . PRO A 1 409 ? 163.326 191.046 227.060 1.00 75.70  ? 409 PRO B C   1 
ATOM 671  O O   . PRO A 1 409 ? 164.271 190.275 227.243 1.00 80.17  ? 409 PRO B O   1 
ATOM 672  C CB  . PRO A 1 409 ? 163.468 191.592 224.593 1.00 79.87  ? 409 PRO B CB  1 
ATOM 673  C CG  . PRO A 1 409 ? 164.913 191.513 224.288 1.00 80.41  ? 409 PRO B CG  1 
ATOM 674  C CD  . PRO A 1 409 ? 165.543 192.689 224.985 1.00 79.11  ? 409 PRO B CD  1 
ATOM 675  N N   . GLY A 1 410 ? 162.190 190.979 227.751 1.00 73.41  ? 410 GLY B N   1 
ATOM 676  C CA  . GLY A 1 410 ? 161.868 189.854 228.602 1.00 77.03  ? 410 GLY B CA  1 
ATOM 677  C C   . GLY A 1 410 ? 162.099 190.019 230.089 1.00 79.99  ? 410 GLY B C   1 
ATOM 678  O O   . GLY A 1 410 ? 162.106 189.010 230.804 1.00 86.29  ? 410 GLY B O   1 
ATOM 679  N N   . GLN A 1 411 ? 162.282 191.240 230.583 1.00 77.25  ? 411 GLN B N   1 
ATOM 680  C CA  . GLN A 1 411 ? 162.522 191.467 232.001 1.00 80.29  ? 411 GLN B CA  1 
ATOM 681  C C   . GLN A 1 411 ? 161.416 192.312 232.615 1.00 80.26  ? 411 GLN B C   1 
ATOM 682  O O   . GLN A 1 411 ? 160.635 192.967 231.919 1.00 79.13  ? 411 GLN B O   1 
ATOM 683  C CB  . GLN A 1 411 ? 163.883 192.133 232.250 1.00 78.34  ? 411 GLN B CB  1 
ATOM 684  C CG  . GLN A 1 411 ? 165.088 191.260 231.933 1.00 79.22  ? 411 GLN B CG  1 
ATOM 685  C CD  . GLN A 1 411 ? 165.422 191.242 230.465 1.00 80.57  ? 411 GLN B CD  1 
ATOM 686  O OE1 . GLN A 1 411 ? 164.972 192.099 229.714 1.00 80.63  ? 411 GLN B OE1 1 
ATOM 687  N NE2 . GLN A 1 411 ? 166.219 190.266 230.046 1.00 81.78  ? 411 GLN B NE2 1 
ATOM 688  N N   . THR A 1 412 ? 161.360 192.276 233.943 1.00 82.82  ? 412 THR B N   1 
ATOM 689  C CA  . THR A 1 412 ? 160.367 192.975 234.741 1.00 83.02  ? 412 THR B CA  1 
ATOM 690  C C   . THR A 1 412 ? 161.059 193.952 235.684 1.00 85.85  ? 412 THR B C   1 
ATOM 691  O O   . THR A 1 412 ? 162.282 193.934 235.852 1.00 85.75  ? 412 THR B O   1 
ATOM 692  C CB  . THR A 1 412 ? 159.505 191.984 235.535 1.00 89.43  ? 412 THR B CB  1 
ATOM 693  O OG1 . THR A 1 412 ? 158.341 192.649 236.040 1.00 88.68  ? 412 THR B OG1 1 
ATOM 694  C CG2 . THR A 1 412 ? 160.293 191.394 236.698 1.00 94.07  ? 412 THR B CG2 1 
ATOM 695  N N   . GLY A 1 413 ? 160.263 194.811 236.298 1.00 85.66  ? 413 GLY B N   1 
ATOM 696  C CA  . GLY A 1 413 ? 160.778 195.809 237.211 1.00 82.22  ? 413 GLY B CA  1 
ATOM 697  C C   . GLY A 1 413 ? 159.877 197.027 237.218 1.00 79.67  ? 413 GLY B C   1 
ATOM 698  O O   . GLY A 1 413 ? 158.765 197.002 236.700 1.00 80.29  ? 413 GLY B O   1 
ATOM 699  N N   . ASN A 1 414 ? 160.382 198.098 237.832 1.00 76.33  ? 414 ASN B N   1 
ATOM 700  C CA  . ASN A 1 414 ? 159.614 199.338 237.893 1.00 73.00  ? 414 ASN B CA  1 
ATOM 701  C C   . ASN A 1 414 ? 159.558 200.012 236.527 1.00 69.42  ? 414 ASN B C   1 
ATOM 702  O O   . ASN A 1 414 ? 158.490 200.444 236.081 1.00 71.12  ? 414 ASN B O   1 
ATOM 703  C CB  . ASN A 1 414 ? 160.216 200.275 238.942 1.00 74.87  ? 414 ASN B CB  1 
ATOM 704  C CG  . ASN A 1 414 ? 159.225 201.314 239.441 1.00 74.88  ? 414 ASN B CG  1 
ATOM 705  O OD1 . ASN A 1 414 ? 158.230 201.615 238.782 1.00 73.47  ? 414 ASN B OD1 1 
ATOM 706  N ND2 . ASN A 1 414 ? 159.495 201.863 240.620 1.00 75.40  ? 414 ASN B ND2 1 
ATOM 707  N N   . ILE A 1 415 ? 160.704 200.120 235.850 1.00 66.95  ? 415 ILE B N   1 
ATOM 708  C CA  . ILE A 1 415 ? 160.714 200.673 234.499 1.00 67.85  ? 415 ILE B CA  1 
ATOM 709  C C   . ILE A 1 415 ? 160.084 199.696 233.514 1.00 71.53  ? 415 ILE B C   1 
ATOM 710  O O   . ILE A 1 415 ? 159.255 200.081 232.680 1.00 72.20  ? 415 ILE B O   1 
ATOM 711  C CB  . ILE A 1 415 ? 162.150 201.048 234.083 1.00 63.01  ? 415 ILE B CB  1 
ATOM 712  C CG1 . ILE A 1 415 ? 162.672 202.217 234.918 1.00 65.01  ? 415 ILE B CG1 1 
ATOM 713  C CG2 . ILE A 1 415 ? 162.217 201.397 232.604 1.00 63.26  ? 415 ILE B CG2 1 
ATOM 714  C CD1 . ILE A 1 415 ? 161.730 203.385 235.015 1.00 67.59  ? 415 ILE B CD1 1 
ATOM 715  N N   . ALA A 1 416 ? 160.445 198.415 233.613 1.00 71.78  ? 416 ALA B N   1 
ATOM 716  C CA  . ALA A 1 416 ? 160.079 197.429 232.604 1.00 73.27  ? 416 ALA B CA  1 
ATOM 717  C C   . ALA A 1 416 ? 158.600 197.067 232.614 1.00 74.40  ? 416 ALA B C   1 
ATOM 718  O O   . ALA A 1 416 ? 158.131 196.442 231.658 1.00 77.46  ? 416 ALA B O   1 
ATOM 719  C CB  . ALA A 1 416 ? 160.918 196.164 232.788 1.00 75.08  ? 416 ALA B CB  1 
ATOM 720  N N   . ASP A 1 417 ? 157.856 197.435 233.658 1.00 71.40  ? 417 ASP B N   1 
ATOM 721  C CA  . ASP A 1 417 ? 156.428 197.169 233.710 1.00 73.29  ? 417 ASP B CA  1 
ATOM 722  C C   . ASP A 1 417 ? 155.562 198.416 233.700 1.00 71.64  ? 417 ASP B C   1 
ATOM 723  O O   . ASP A 1 417 ? 154.398 198.330 233.295 1.00 75.26  ? 417 ASP B O   1 
ATOM 724  C CB  . ASP A 1 417 ? 156.074 196.347 234.959 1.00 78.46  ? 417 ASP B CB  1 
ATOM 725  C CG  . ASP A 1 417 ? 156.598 194.930 234.892 1.00 82.90  ? 417 ASP B CG  1 
ATOM 726  O OD1 . ASP A 1 417 ? 156.975 194.485 233.788 1.00 86.27  ? 417 ASP B OD1 1 
ATOM 727  O OD2 . ASP A 1 417 ? 156.631 194.258 235.944 1.00 82.67  ? 417 ASP B OD2 1 
ATOM 728  N N   . TYR A 1 418 ? 156.084 199.565 234.129 1.00 69.62  ? 418 TYR B N   1 
ATOM 729  C CA  . TYR A 1 418 ? 155.275 200.766 234.271 1.00 68.97  ? 418 TYR B CA  1 
ATOM 730  C C   . TYR A 1 418 ? 155.662 201.887 233.319 1.00 66.05  ? 418 TYR B C   1 
ATOM 731  O O   . TYR A 1 418 ? 154.818 202.740 233.028 1.00 67.59  ? 418 TYR B O   1 
ATOM 732  C CB  . TYR A 1 418 ? 155.360 201.302 235.709 1.00 68.90  ? 418 TYR B CB  1 
ATOM 733  C CG  . TYR A 1 418 ? 154.710 200.431 236.766 1.00 72.57  ? 418 TYR B CG  1 
ATOM 734  C CD1 . TYR A 1 418 ? 153.834 199.409 236.422 1.00 74.46  ? 418 TYR B CD1 1 
ATOM 735  C CD2 . TYR A 1 418 ? 154.984 200.631 238.114 1.00 74.45  ? 418 TYR B CD2 1 
ATOM 736  C CE1 . TYR A 1 418 ? 153.248 198.614 237.388 1.00 80.97  ? 418 TYR B CE1 1 
ATOM 737  C CE2 . TYR A 1 418 ? 154.402 199.842 239.087 1.00 79.16  ? 418 TYR B CE2 1 
ATOM 738  C CZ  . TYR A 1 418 ? 153.535 198.835 238.719 1.00 85.93  ? 418 TYR B CZ  1 
ATOM 739  O OH  . TYR A 1 418 ? 152.952 198.048 239.685 1.00 91.80  ? 418 TYR B OH  1 
ATOM 740  N N   . ASN A 1 419 ? 156.901 201.915 232.831 1.00 62.24  ? 419 ASN B N   1 
ATOM 741  C CA  . ASN A 1 419 ? 157.387 203.053 232.061 1.00 58.55  ? 419 ASN B CA  1 
ATOM 742  C C   . ASN A 1 419 ? 157.752 202.706 230.627 1.00 62.31  ? 419 ASN B C   1 
ATOM 743  O O   . ASN A 1 419 ? 157.248 203.344 229.695 1.00 65.04  ? 419 ASN B O   1 
ATOM 744  C CB  . ASN A 1 419 ? 158.599 203.676 232.763 1.00 57.47  ? 419 ASN B CB  1 
ATOM 745  C CG  . ASN A 1 419 ? 158.202 204.544 233.924 1.00 63.33  ? 419 ASN B CG  1 
ATOM 746  O OD1 . ASN A 1 419 ? 157.071 204.475 234.391 1.00 67.75  ? 419 ASN B OD1 1 
ATOM 747  N ND2 . ASN A 1 419 ? 159.117 205.388 234.382 1.00 64.32  ? 419 ASN B ND2 1 
ATOM 748  N N   . TYR A 1 420 ? 158.618 201.718 230.419 1.00 62.38  ? 420 TYR B N   1 
ATOM 749  C CA  . TYR A 1 420 ? 159.124 201.403 229.088 1.00 63.88  ? 420 TYR B CA  1 
ATOM 750  C C   . TYR A 1 420 ? 159.310 199.898 228.994 1.00 67.83  ? 420 TYR B C   1 
ATOM 751  O O   . TYR A 1 420 ? 160.078 199.317 229.766 1.00 71.51  ? 420 TYR B O   1 
ATOM 752  C CB  . TYR A 1 420 ? 160.436 202.157 228.822 1.00 63.75  ? 420 TYR B CB  1 
ATOM 753  C CG  . TYR A 1 420 ? 160.996 202.074 227.411 1.00 63.20  ? 420 TYR B CG  1 
ATOM 754  C CD1 . TYR A 1 420 ? 161.618 200.923 226.940 1.00 65.69  ? 420 TYR B CD1 1 
ATOM 755  C CD2 . TYR A 1 420 ? 160.895 203.157 226.548 1.00 61.09  ? 420 TYR B CD2 1 
ATOM 756  C CE1 . TYR A 1 420 ? 162.125 200.858 225.663 1.00 64.42  ? 420 TYR B CE1 1 
ATOM 757  C CE2 . TYR A 1 420 ? 161.396 203.097 225.264 1.00 60.18  ? 420 TYR B CE2 1 
ATOM 758  C CZ  . TYR A 1 420 ? 162.011 201.945 224.827 1.00 62.47  ? 420 TYR B CZ  1 
ATOM 759  O OH  . TYR A 1 420 ? 162.514 201.880 223.549 1.00 66.71  ? 420 TYR B OH  1 
ATOM 760  N N   . LYS A 1 421 ? 158.613 199.274 228.047 1.00 64.96  ? 421 LYS B N   1 
ATOM 761  C CA  . LYS A 1 421 ? 158.703 197.840 227.818 1.00 67.23  ? 421 LYS B CA  1 
ATOM 762  C C   . LYS A 1 421 ? 158.976 197.582 226.345 1.00 67.72  ? 421 LYS B C   1 
ATOM 763  O O   . LYS A 1 421 ? 158.304 198.147 225.477 1.00 68.02  ? 421 LYS B O   1 
ATOM 764  C CB  . LYS A 1 421 ? 157.418 197.126 228.253 1.00 70.00  ? 421 LYS B CB  1 
ATOM 765  C CG  . LYS A 1 421 ? 157.466 195.613 228.091 1.00 73.59  ? 421 LYS B CG  1 
ATOM 766  C CD  . LYS A 1 421 ? 156.215 194.952 228.644 1.00 73.47  ? 421 LYS B CD  1 
ATOM 767  C CE  . LYS A 1 421 ? 156.202 193.463 228.339 1.00 72.08  ? 421 LYS B CE  1 
ATOM 768  N NZ  . LYS A 1 421 ? 157.292 192.739 229.048 1.00 71.26  ? 421 LYS B NZ  1 
ATOM 769  N N   . LEU A 1 422 ? 159.958 196.742 226.071 1.00 68.71  ? 422 LEU B N   1 
ATOM 770  C CA  . LEU A 1 422 ? 160.329 196.286 224.742 1.00 72.86  ? 422 LEU B CA  1 
ATOM 771  C C   . LEU A 1 422 ? 159.563 195.020 224.369 1.00 79.46  ? 422 LEU B C   1 
ATOM 772  O O   . LEU A 1 422 ? 159.206 194.224 225.244 1.00 79.59  ? 422 LEU B O   1 
ATOM 773  C CB  . LEU A 1 422 ? 161.830 196.013 224.674 1.00 73.17  ? 422 LEU B CB  1 
ATOM 774  C CG  . LEU A 1 422 ? 162.756 197.217 224.516 1.00 73.47  ? 422 LEU B CG  1 
ATOM 775  C CD1 . LEU A 1 422 ? 164.167 196.752 224.209 1.00 75.43  ? 422 LEU B CD1 1 
ATOM 776  C CD2 . LEU A 1 422 ? 162.248 198.109 223.397 1.00 74.08  ? 422 LEU B CD2 1 
ATOM 777  N N   . PRO A 1 423 ? 159.285 194.818 223.082 1.00 81.67  ? 423 PRO B N   1 
ATOM 778  C CA  . PRO A 1 423 ? 158.655 193.565 222.654 1.00 82.23  ? 423 PRO B CA  1 
ATOM 779  C C   . PRO A 1 423 ? 159.602 192.386 222.813 1.00 85.48  ? 423 PRO B C   1 
ATOM 780  O O   . PRO A 1 423 ? 160.826 192.531 222.826 1.00 87.16  ? 423 PRO B O   1 
ATOM 781  C CB  . PRO A 1 423 ? 158.323 193.813 221.177 1.00 82.15  ? 423 PRO B CB  1 
ATOM 782  C CG  . PRO A 1 423 ? 158.400 195.295 220.998 1.00 78.77  ? 423 PRO B CG  1 
ATOM 783  C CD  . PRO A 1 423 ? 159.433 195.765 221.965 1.00 78.19  ? 423 PRO B CD  1 
ATOM 784  N N   . ASP A 1 424 ? 159.005 191.199 222.952 1.00 85.37  ? 424 ASP B N   1 
ATOM 785  C CA  . ASP A 1 424 ? 159.797 189.982 223.101 1.00 91.50  ? 424 ASP B CA  1 
ATOM 786  C C   . ASP A 1 424 ? 160.574 189.659 221.831 1.00 94.26  ? 424 ASP B C   1 
ATOM 787  O O   . ASP A 1 424 ? 161.684 189.119 221.905 1.00 94.23  ? 424 ASP B O   1 
ATOM 788  C CB  . ASP A 1 424 ? 158.892 188.811 223.484 1.00 92.39  ? 424 ASP B CB  1 
ATOM 789  C CG  . ASP A 1 424 ? 159.578 187.823 224.408 1.00 97.02  ? 424 ASP B CG  1 
ATOM 790  O OD1 . ASP A 1 424 ? 160.738 187.454 224.132 1.00 95.07  ? 424 ASP B OD1 1 
ATOM 791  O OD2 . ASP A 1 424 ? 158.956 187.417 225.412 1.00 100.50 ? 424 ASP B OD2 1 
ATOM 792  N N   . ASP A 1 425 ? 160.015 189.976 220.668 1.00 93.39  ? 425 ASP B N   1 
ATOM 793  C CA  . ASP A 1 425 ? 160.698 189.833 219.385 1.00 95.76  ? 425 ASP B CA  1 
ATOM 794  C C   . ASP A 1 425 ? 161.110 191.236 218.946 1.00 94.43  ? 425 ASP B C   1 
ATOM 795  O O   . ASP A 1 425 ? 160.374 191.922 218.236 1.00 94.28  ? 425 ASP B O   1 
ATOM 796  C CB  . ASP A 1 425 ? 159.801 189.154 218.352 1.00 99.85  ? 425 ASP B CB  1 
ATOM 797  C CG  . ASP A 1 425 ? 160.587 188.544 217.206 1.00 103.13 ? 425 ASP B CG  1 
ATOM 798  O OD1 . ASP A 1 425 ? 161.827 188.693 217.185 1.00 103.24 ? 425 ASP B OD1 1 
ATOM 799  O OD2 . ASP A 1 425 ? 159.963 187.915 216.326 1.00 101.88 ? 425 ASP B OD2 1 
ATOM 800  N N   . PHE A 1 426 ? 162.296 191.657 219.377 1.00 89.76  ? 426 PHE B N   1 
ATOM 801  C CA  . PHE A 1 426 ? 162.786 193.009 219.148 1.00 86.77  ? 426 PHE B CA  1 
ATOM 802  C C   . PHE A 1 426 ? 164.088 192.961 218.364 1.00 87.05  ? 426 PHE B C   1 
ATOM 803  O O   . PHE A 1 426 ? 165.019 192.243 218.743 1.00 90.06  ? 426 PHE B O   1 
ATOM 804  C CB  . PHE A 1 426 ? 162.994 193.743 220.474 1.00 83.46  ? 426 PHE B CB  1 
ATOM 805  C CG  . PHE A 1 426 ? 163.461 195.157 220.317 1.00 81.06  ? 426 PHE B CG  1 
ATOM 806  C CD1 . PHE A 1 426 ? 162.578 196.149 219.925 1.00 80.13  ? 426 PHE B CD1 1 
ATOM 807  C CD2 . PHE A 1 426 ? 164.776 195.500 220.578 1.00 77.84  ? 426 PHE B CD2 1 
ATOM 808  C CE1 . PHE A 1 426 ? 163.002 197.453 219.783 1.00 78.03  ? 426 PHE B CE1 1 
ATOM 809  C CE2 . PHE A 1 426 ? 165.206 196.802 220.440 1.00 73.48  ? 426 PHE B CE2 1 
ATOM 810  C CZ  . PHE A 1 426 ? 164.316 197.781 220.043 1.00 76.71  ? 426 PHE B CZ  1 
ATOM 811  N N   . THR A 1 427 ? 164.153 193.735 217.282 1.00 84.82  ? 427 THR B N   1 
ATOM 812  C CA  . THR A 1 427 ? 165.358 193.873 216.469 1.00 85.17  ? 427 THR B CA  1 
ATOM 813  C C   . THR A 1 427 ? 165.802 195.330 216.524 1.00 81.42  ? 427 THR B C   1 
ATOM 814  O O   . THR A 1 427 ? 165.029 196.235 216.193 1.00 82.29  ? 427 THR B O   1 
ATOM 815  C CB  . THR A 1 427 ? 165.113 193.426 215.028 1.00 87.99  ? 427 THR B CB  1 
ATOM 816  O OG1 . THR A 1 427 ? 163.967 194.105 214.500 1.00 87.44  ? 427 THR B OG1 1 
ATOM 817  C CG2 . THR A 1 427 ? 164.875 191.924 214.973 1.00 87.52  ? 427 THR B CG2 1 
ATOM 818  N N   . GLY A 1 428 ? 167.040 195.547 216.936 1.00 79.40  ? 428 GLY B N   1 
ATOM 819  C CA  . GLY A 1 428 ? 167.556 196.879 217.176 1.00 75.44  ? 428 GLY B CA  1 
ATOM 820  C C   . GLY A 1 428 ? 168.544 196.841 218.314 1.00 73.87  ? 428 GLY B C   1 
ATOM 821  O O   . GLY A 1 428 ? 168.663 195.847 219.030 1.00 80.32  ? 428 GLY B O   1 
ATOM 822  N N   . CYS A 1 429 ? 169.264 197.948 218.489 1.00 67.95  ? 429 CYS B N   1 
ATOM 823  C CA  . CYS A 1 429 ? 170.372 197.934 219.429 1.00 67.33  ? 429 CYS B CA  1 
ATOM 824  C C   . CYS A 1 429 ? 170.253 199.011 220.499 1.00 65.75  ? 429 CYS B C   1 
ATOM 825  O O   . CYS A 1 429 ? 169.693 200.088 220.276 1.00 67.59  ? 429 CYS B O   1 
ATOM 826  C CB  . CYS A 1 429 ? 171.725 198.021 218.696 1.00 75.35  ? 429 CYS B CB  1 
ATOM 827  S SG  . CYS A 1 429 ? 172.131 196.517 217.689 1.00 109.60 ? 429 CYS B SG  1 
ATOM 828  N N   . VAL A 1 430 ? 170.796 198.683 221.673 1.00 61.67  ? 430 VAL B N   1 
ATOM 829  C CA  . VAL A 1 430 ? 170.604 199.432 222.910 1.00 54.14  ? 430 VAL B CA  1 
ATOM 830  C C   . VAL A 1 430 ? 171.962 199.946 223.367 1.00 54.23  ? 430 VAL B C   1 
ATOM 831  O O   . VAL A 1 430 ? 172.915 199.168 223.494 1.00 61.57  ? 430 VAL B O   1 
ATOM 832  C CB  . VAL A 1 430 ? 169.955 198.562 223.998 1.00 53.21  ? 430 VAL B CB  1 
ATOM 833  C CG1 . VAL A 1 430 ? 169.951 199.281 225.337 1.00 55.66  ? 430 VAL B CG1 1 
ATOM 834  C CG2 . VAL A 1 430 ? 168.546 198.160 223.592 1.00 56.68  ? 430 VAL B CG2 1 
ATOM 835  N N   . ILE A 1 431 ? 172.049 201.253 223.612 1.00 52.02  ? 431 ILE B N   1 
ATOM 836  C CA  . ILE A 1 431 ? 173.297 201.926 223.954 1.00 52.81  ? 431 ILE B CA  1 
ATOM 837  C C   . ILE A 1 431 ? 173.108 202.694 225.256 1.00 52.46  ? 431 ILE B C   1 
ATOM 838  O O   . ILE A 1 431 ? 172.061 203.313 225.473 1.00 55.02  ? 431 ILE B O   1 
ATOM 839  C CB  . ILE A 1 431 ? 173.754 202.880 222.827 1.00 53.04  ? 431 ILE B CB  1 
ATOM 840  C CG1 . ILE A 1 431 ? 173.631 202.214 221.454 1.00 52.35  ? 431 ILE B CG1 1 
ATOM 841  C CG2 . ILE A 1 431 ? 175.169 203.339 223.058 1.00 59.96  ? 431 ILE B CG2 1 
ATOM 842  C CD1 . ILE A 1 431 ? 173.799 203.162 220.297 1.00 60.24  ? 431 ILE B CD1 1 
ATOM 843  N N   . ALA A 1 432 ? 174.121 202.653 226.123 1.00 49.32  ? 432 ALA B N   1 
ATOM 844  C CA  . ALA A 1 432 ? 174.105 203.403 227.370 1.00 45.32  ? 432 ALA B CA  1 
ATOM 845  C C   . ALA A 1 432 ? 175.498 203.936 227.676 1.00 48.09  ? 432 ALA B C   1 
ATOM 846  O O   . ALA A 1 432 ? 176.505 203.291 227.373 1.00 57.26  ? 432 ALA B O   1 
ATOM 847  C CB  . ALA A 1 432 ? 173.608 202.542 228.536 1.00 46.83  ? 432 ALA B CB  1 
ATOM 848  N N   . TRP A 1 433 ? 175.548 205.122 228.284 1.00 45.29  ? 433 TRP B N   1 
ATOM 849  C CA  . TRP A 1 433 ? 176.806 205.692 228.751 1.00 46.68  ? 433 TRP B CA  1 
ATOM 850  C C   . TRP A 1 433 ? 176.531 206.626 229.922 1.00 49.81  ? 433 TRP B C   1 
ATOM 851  O O   . TRP A 1 433 ? 175.396 207.051 230.151 1.00 51.52  ? 433 TRP B O   1 
ATOM 852  C CB  . TRP A 1 433 ? 177.560 206.440 227.642 1.00 50.22  ? 433 TRP B CB  1 
ATOM 853  C CG  . TRP A 1 433 ? 176.844 207.629 227.076 1.00 49.22  ? 433 TRP B CG  1 
ATOM 854  C CD1 . TRP A 1 433 ? 177.067 208.938 227.384 1.00 47.46  ? 433 TRP B CD1 1 
ATOM 855  C CD2 . TRP A 1 433 ? 175.823 207.623 226.072 1.00 47.41  ? 433 TRP B CD2 1 
ATOM 856  N NE1 . TRP A 1 433 ? 176.233 209.746 226.654 1.00 44.35  ? 433 TRP B NE1 1 
ATOM 857  C CE2 . TRP A 1 433 ? 175.460 208.963 225.839 1.00 45.11  ? 433 TRP B CE2 1 
ATOM 858  C CE3 . TRP A 1 433 ? 175.173 206.614 225.356 1.00 51.39  ? 433 TRP B CE3 1 
ATOM 859  C CZ2 . TRP A 1 433 ? 174.479 209.320 224.922 1.00 51.57  ? 433 TRP B CZ2 1 
ATOM 860  C CZ3 . TRP A 1 433 ? 174.199 206.972 224.446 1.00 51.71  ? 433 TRP B CZ3 1 
ATOM 861  C CH2 . TRP A 1 433 ? 173.862 208.313 224.237 1.00 53.55  ? 433 TRP B CH2 1 
ATOM 862  N N   . ASN A 1 434 ? 177.592 206.944 230.660 1.00 48.19  ? 434 ASN B N   1 
ATOM 863  C CA  . ASN A 1 434 ? 177.472 207.714 231.890 1.00 44.29  ? 434 ASN B CA  1 
ATOM 864  C C   . ASN A 1 434 ? 177.335 209.203 231.589 1.00 46.23  ? 434 ASN B C   1 
ATOM 865  O O   . ASN A 1 434 ? 177.881 209.716 230.608 1.00 50.78  ? 434 ASN B O   1 
ATOM 866  C CB  . ASN A 1 434 ? 178.689 207.464 232.784 1.00 44.54  ? 434 ASN B CB  1 
ATOM 867  C CG  . ASN A 1 434 ? 178.460 207.876 234.229 1.00 49.72  ? 434 ASN B CG  1 
ATOM 868  O OD1 . ASN A 1 434 ? 177.948 208.955 234.516 1.00 51.45  ? 434 ASN B OD1 1 
ATOM 869  N ND2 . ASN A 1 434 ? 178.849 207.005 235.152 1.00 50.03  ? 434 ASN B ND2 1 
ATOM 870  N N   . SER A 1 435 ? 176.591 209.894 232.449 1.00 42.62  ? 435 SER B N   1 
ATOM 871  C CA  . SER A 1 435 ? 176.408 211.340 232.354 1.00 45.39  ? 435 SER B CA  1 
ATOM 872  C C   . SER A 1 435 ? 176.449 211.979 233.740 1.00 47.70  ? 435 SER B C   1 
ATOM 873  O O   . SER A 1 435 ? 175.621 212.823 234.082 1.00 50.71  ? 435 SER B O   1 
ATOM 874  C CB  . SER A 1 435 ? 175.103 211.680 231.643 1.00 49.57  ? 435 SER B CB  1 
ATOM 875  O OG  . SER A 1 435 ? 174.004 211.608 232.534 1.00 50.81  ? 435 SER B OG  1 
ATOM 876  N N   . ASN A 1 436 ? 177.411 211.562 234.566 1.00 46.65  ? 436 ASN B N   1 
ATOM 877  C CA  . ASN A 1 436 ? 177.520 212.126 235.910 1.00 47.06  ? 436 ASN B CA  1 
ATOM 878  C C   . ASN A 1 436 ? 177.980 213.578 235.864 1.00 51.34  ? 436 ASN B C   1 
ATOM 879  O O   . ASN A 1 436 ? 177.485 214.418 236.624 1.00 53.98  ? 436 ASN B O   1 
ATOM 880  C CB  . ASN A 1 436 ? 178.481 211.288 236.752 1.00 47.66  ? 436 ASN B CB  1 
ATOM 881  C CG  . ASN A 1 436 ? 178.476 211.682 238.219 1.00 51.97  ? 436 ASN B CG  1 
ATOM 882  O OD1 . ASN A 1 436 ? 177.597 212.408 238.680 1.00 53.76  ? 436 ASN B OD1 1 
ATOM 883  N ND2 . ASN A 1 436 ? 179.464 211.198 238.961 1.00 51.71  ? 436 ASN B ND2 1 
ATOM 884  N N   . LYS A 1 437 ? 178.918 213.894 234.972 1.00 51.74  ? 437 LYS B N   1 
ATOM 885  C CA  . LYS A 1 437 ? 179.456 215.243 234.871 1.00 52.73  ? 437 LYS B CA  1 
ATOM 886  C C   . LYS A 1 437 ? 178.502 216.219 234.196 1.00 55.84  ? 437 LYS B C   1 
ATOM 887  O O   . LYS A 1 437 ? 178.765 217.427 234.216 1.00 59.87  ? 437 LYS B O   1 
ATOM 888  C CB  . LYS A 1 437 ? 180.781 215.219 234.108 1.00 52.95  ? 437 LYS B CB  1 
ATOM 889  C CG  . LYS A 1 437 ? 180.644 214.781 232.658 1.00 59.48  ? 437 LYS B CG  1 
ATOM 890  C CD  . LYS A 1 437 ? 181.992 214.720 231.962 1.00 63.22  ? 437 LYS B CD  1 
ATOM 891  C CE  . LYS A 1 437 ? 181.839 214.308 230.506 1.00 64.53  ? 437 LYS B CE  1 
ATOM 892  N NZ  . LYS A 1 437 ? 181.366 212.902 230.375 1.00 61.49  ? 437 LYS B NZ  1 
ATOM 893  N N   . LEU A 1 438 ? 177.413 215.737 233.603 1.00 52.76  ? 438 LEU B N   1 
ATOM 894  C CA  . LEU A 1 438 ? 176.502 216.570 232.832 1.00 51.36  ? 438 LEU B CA  1 
ATOM 895  C C   . LEU A 1 438 ? 175.118 216.678 233.452 1.00 53.14  ? 438 LEU B C   1 
ATOM 896  O O   . LEU A 1 438 ? 174.586 217.784 233.586 1.00 54.83  ? 438 LEU B O   1 
ATOM 897  C CB  . LEU A 1 438 ? 176.391 216.025 231.400 1.00 52.70  ? 438 LEU B CB  1 
ATOM 898  C CG  . LEU A 1 438 ? 176.168 217.049 230.287 1.00 62.68  ? 438 LEU B CG  1 
ATOM 899  C CD1 . LEU A 1 438 ? 177.236 218.131 230.328 1.00 62.32  ? 438 LEU B CD1 1 
ATOM 900  C CD2 . LEU A 1 438 ? 176.147 216.364 228.929 1.00 60.39  ? 438 LEU B CD2 1 
ATOM 901  N N   . ASP A 1 439 ? 174.515 215.553 233.839 1.00 54.16  ? 439 ASP B N   1 
ATOM 902  C CA  . ASP A 1 439 ? 173.155 215.529 234.364 1.00 56.98  ? 439 ASP B CA  1 
ATOM 903  C C   . ASP A 1 439 ? 173.114 215.522 235.889 1.00 55.85  ? 439 ASP B C   1 
ATOM 904  O O   . ASP A 1 439 ? 172.181 214.968 236.480 1.00 55.70  ? 439 ASP B O   1 
ATOM 905  C CB  . ASP A 1 439 ? 172.397 214.322 233.812 1.00 56.78  ? 439 ASP B CB  1 
ATOM 906  C CG  . ASP A 1 439 ? 172.174 214.408 232.317 1.00 58.59  ? 439 ASP B CG  1 
ATOM 907  O OD1 . ASP A 1 439 ? 171.953 215.529 231.811 1.00 60.34  ? 439 ASP B OD1 1 
ATOM 908  O OD2 . ASP A 1 439 ? 172.218 213.356 231.646 1.00 58.48  ? 439 ASP B OD2 1 
ATOM 909  N N   . SER A 1 440 ? 174.105 216.124 236.541 1.00 56.67  ? 440 SER B N   1 
ATOM 910  C CA  . SER A 1 440 ? 174.136 216.156 237.995 1.00 60.08  ? 440 SER B CA  1 
ATOM 911  C C   . SER A 1 440 ? 174.831 217.428 238.456 1.00 63.86  ? 440 SER B C   1 
ATOM 912  O O   . SER A 1 440 ? 175.628 218.026 237.727 1.00 67.24  ? 440 SER B O   1 
ATOM 913  C CB  . SER A 1 440 ? 174.838 214.921 238.568 1.00 58.83  ? 440 SER B CB  1 
ATOM 914  O OG  . SER A 1 440 ? 175.064 215.066 239.957 1.00 57.93  ? 440 SER B OG  1 
ATOM 915  N N   . LYS A 1 441 ? 174.520 217.834 239.684 1.00 64.54  ? 441 LYS B N   1 
ATOM 916  C CA  . LYS A 1 441 ? 175.095 219.035 240.275 1.00 65.81  ? 441 LYS B CA  1 
ATOM 917  C C   . LYS A 1 441 ? 175.045 218.898 241.791 1.00 63.81  ? 441 LYS B C   1 
ATOM 918  O O   . LYS A 1 441 ? 174.521 217.920 242.330 1.00 62.73  ? 441 LYS B O   1 
ATOM 919  C CB  . LYS A 1 441 ? 174.360 220.296 239.812 1.00 67.21  ? 441 LYS B CB  1 
ATOM 920  C CG  . LYS A 1 441 ? 172.917 220.383 240.282 1.00 66.86  ? 441 LYS B CG  1 
ATOM 921  C CD  . LYS A 1 441 ? 172.269 221.683 239.829 1.00 73.52  ? 441 LYS B CD  1 
ATOM 922  C CE  . LYS A 1 441 ? 172.001 221.687 238.333 1.00 78.08  ? 441 LYS B CE  1 
ATOM 923  N NZ  . LYS A 1 441 ? 170.976 220.682 237.945 1.00 75.04  ? 441 LYS B NZ  1 
ATOM 924  N N   . HIS A 1 442 ? 175.605 219.893 242.475 1.00 64.66  ? 442 HIS B N   1 
ATOM 925  C CA  . HIS A 1 442 ? 175.583 219.924 243.929 1.00 64.14  ? 442 HIS B CA  1 
ATOM 926  C C   . HIS A 1 442 ? 174.162 220.126 244.443 1.00 64.41  ? 442 HIS B C   1 
ATOM 927  O O   . HIS A 1 442 ? 173.311 220.710 243.765 1.00 68.48  ? 442 HIS B O   1 
ATOM 928  C CB  . HIS A 1 442 ? 176.491 221.036 244.452 1.00 65.96  ? 442 HIS B CB  1 
ATOM 929  C CG  . HIS A 1 442 ? 176.779 220.944 245.918 1.00 67.42  ? 442 HIS B CG  1 
ATOM 930  N ND1 . HIS A 1 442 ? 177.246 219.792 246.514 1.00 70.07  ? 442 HIS B ND1 1 
ATOM 931  C CD2 . HIS A 1 442 ? 176.660 221.858 246.909 1.00 68.98  ? 442 HIS B CD2 1 
ATOM 932  C CE1 . HIS A 1 442 ? 177.406 220.002 247.808 1.00 71.71  ? 442 HIS B CE1 1 
ATOM 933  N NE2 . HIS A 1 442 ? 177.057 221.248 248.074 1.00 73.18  ? 442 HIS B NE2 1 
ATOM 934  N N   . SER A 1 443 ? 173.908 219.597 245.642 1.00 59.79  ? 443 SER B N   1 
ATOM 935  C CA  . SER A 1 443 ? 172.648 219.688 246.379 1.00 60.80  ? 443 SER B CA  1 
ATOM 936  C C   . SER A 1 443 ? 171.479 219.020 245.662 1.00 59.31  ? 443 SER B C   1 
ATOM 937  O O   . SER A 1 443 ? 170.322 219.249 246.033 1.00 62.55  ? 443 SER B O   1 
ATOM 938  C CB  . SER A 1 443 ? 172.285 221.142 246.716 1.00 65.43  ? 443 SER B CB  1 
ATOM 939  O OG  . SER A 1 443 ? 173.254 221.726 247.568 1.00 70.59  ? 443 SER B OG  1 
ATOM 940  N N   . GLY A 1 444 ? 171.740 218.204 244.656 1.00 56.68  ? 444 GLY B N   1 
ATOM 941  C CA  . GLY A 1 444 ? 170.681 217.440 244.022 1.00 57.27  ? 444 GLY B CA  1 
ATOM 942  C C   . GLY A 1 444 ? 170.217 218.050 242.713 1.00 57.89  ? 444 GLY B C   1 
ATOM 943  O O   . GLY A 1 444 ? 170.176 219.276 242.549 1.00 59.92  ? 444 GLY B O   1 
ATOM 944  N N   . ASN A 1 445 ? 169.861 217.182 241.771 1.00 56.92  ? 445 ASN B N   1 
ATOM 945  C CA  . ASN A 1 445 ? 169.252 217.569 240.504 1.00 56.51  ? 445 ASN B CA  1 
ATOM 946  C C   . ASN A 1 445 ? 167.862 216.952 240.469 1.00 57.35  ? 445 ASN B C   1 
ATOM 947  O O   . ASN A 1 445 ? 167.724 215.733 240.320 1.00 59.92  ? 445 ASN B O   1 
ATOM 948  C CB  . ASN A 1 445 ? 170.094 217.099 239.320 1.00 57.80  ? 445 ASN B CB  1 
ATOM 949  C CG  . ASN A 1 445 ? 169.695 217.764 238.025 1.00 63.33  ? 445 ASN B CG  1 
ATOM 950  O OD1 . ASN A 1 445 ? 169.010 218.786 238.028 1.00 66.45  ? 445 ASN B OD1 1 
ATOM 951  N ND2 . ASN A 1 445 ? 170.115 217.186 236.905 1.00 62.90  ? 445 ASN B ND2 1 
ATOM 952  N N   . TYR A 1 446 ? 166.836 217.785 240.604 1.00 56.16  ? 446 TYR B N   1 
ATOM 953  C CA  . TYR A 1 446 ? 165.461 217.323 240.751 1.00 52.52  ? 446 TYR B CA  1 
ATOM 954  C C   . TYR A 1 446 ? 164.626 217.626 239.512 1.00 52.65  ? 446 TYR B C   1 
ATOM 955  O O   . TYR A 1 446 ? 163.457 218.001 239.613 1.00 55.67  ? 446 TYR B O   1 
ATOM 956  C CB  . TYR A 1 446 ? 164.790 217.932 241.985 1.00 52.03  ? 446 TYR B CB  1 
ATOM 957  C CG  . TYR A 1 446 ? 165.508 217.759 243.314 1.00 53.75  ? 446 TYR B CG  1 
ATOM 958  C CD1 . TYR A 1 446 ? 166.660 218.479 243.621 1.00 54.87  ? 446 TYR B CD1 1 
ATOM 959  C CD2 . TYR A 1 446 ? 164.980 216.931 244.294 1.00 54.62  ? 446 TYR B CD2 1 
ATOM 960  C CE1 . TYR A 1 446 ? 167.292 218.331 244.838 1.00 54.96  ? 446 TYR B CE1 1 
ATOM 961  C CE2 . TYR A 1 446 ? 165.606 216.778 245.513 1.00 58.16  ? 446 TYR B CE2 1 
ATOM 962  C CZ  . TYR A 1 446 ? 166.760 217.483 245.781 1.00 57.54  ? 446 TYR B CZ  1 
ATOM 963  O OH  . TYR A 1 446 ? 167.387 217.340 246.995 1.00 59.13  ? 446 TYR B OH  1 
ATOM 964  N N   . ASP A 1 447 ? 165.209 217.472 238.325 1.00 54.27  ? 447 ASP B N   1 
ATOM 965  C CA  . ASP A 1 447 ? 164.484 217.730 237.089 1.00 57.53  ? 447 ASP B CA  1 
ATOM 966  C C   . ASP A 1 447 ? 164.358 216.520 236.169 1.00 59.87  ? 447 ASP B C   1 
ATOM 967  O O   . ASP A 1 447 ? 163.984 216.690 235.004 1.00 57.61  ? 447 ASP B O   1 
ATOM 968  C CB  . ASP A 1 447 ? 165.105 218.925 236.343 1.00 61.90  ? 447 ASP B CB  1 
ATOM 969  C CG  . ASP A 1 447 ? 166.548 218.693 235.913 1.00 69.60  ? 447 ASP B CG  1 
ATOM 970  O OD1 . ASP A 1 447 ? 167.123 217.631 236.213 1.00 69.98  ? 447 ASP B OD1 1 
ATOM 971  O OD2 . ASP A 1 447 ? 167.115 219.594 235.260 1.00 70.47  ? 447 ASP B OD2 1 
ATOM 972  N N   . TYR A 1 448 ? 164.647 215.310 236.647 1.00 59.96  ? 448 TYR B N   1 
ATOM 973  C CA  . TYR A 1 448 ? 164.271 214.095 235.936 1.00 55.55  ? 448 TYR B CA  1 
ATOM 974  C C   . TYR A 1 448 ? 163.394 213.243 236.841 1.00 55.87  ? 448 TYR B C   1 
ATOM 975  O O   . TYR A 1 448 ? 163.611 213.186 238.055 1.00 57.36  ? 448 TYR B O   1 
ATOM 976  C CB  . TYR A 1 448 ? 165.475 213.273 235.466 1.00 51.11  ? 448 TYR B CB  1 
ATOM 977  C CG  . TYR A 1 448 ? 166.389 213.985 234.495 1.00 54.20  ? 448 TYR B CG  1 
ATOM 978  C CD1 . TYR A 1 448 ? 167.374 214.846 234.946 1.00 56.05  ? 448 TYR B CD1 1 
ATOM 979  C CD2 . TYR A 1 448 ? 166.340 213.707 233.140 1.00 57.10  ? 448 TYR B CD2 1 
ATOM 980  C CE1 . TYR A 1 448 ? 168.233 215.476 234.069 1.00 58.68  ? 448 TYR B CE1 1 
ATOM 981  C CE2 . TYR A 1 448 ? 167.193 214.330 232.250 1.00 60.08  ? 448 TYR B CE2 1 
ATOM 982  C CZ  . TYR A 1 448 ? 168.141 215.212 232.721 1.00 62.40  ? 448 TYR B CZ  1 
ATOM 983  O OH  . TYR A 1 448 ? 168.998 215.833 231.841 1.00 66.13  ? 448 TYR B OH  1 
ATOM 984  N N   . TRP A 1 449 ? 162.408 212.576 236.244 1.00 54.00  ? 449 TRP B N   1 
ATOM 985  C CA  . TRP A 1 449 ? 161.330 211.935 236.982 1.00 52.50  ? 449 TRP B CA  1 
ATOM 986  C C   . TRP A 1 449 ? 161.078 210.533 236.446 1.00 54.67  ? 449 TRP B C   1 
ATOM 987  O O   . TRP A 1 449 ? 161.468 210.192 235.326 1.00 57.79  ? 449 TRP B O   1 
ATOM 988  C CB  . TRP A 1 449 ? 160.038 212.762 236.896 1.00 55.37  ? 449 TRP B CB  1 
ATOM 989  C CG  . TRP A 1 449 ? 160.179 214.169 237.393 1.00 56.74  ? 449 TRP B CG  1 
ATOM 990  C CD1 . TRP A 1 449 ? 160.721 215.226 236.720 1.00 57.91  ? 449 TRP B CD1 1 
ATOM 991  C CD2 . TRP A 1 449 ? 159.728 214.685 238.650 1.00 55.37  ? 449 TRP B CD2 1 
ATOM 992  N NE1 . TRP A 1 449 ? 160.664 216.359 237.492 1.00 56.83  ? 449 TRP B NE1 1 
ATOM 993  C CE2 . TRP A 1 449 ? 160.054 216.055 238.680 1.00 55.20  ? 449 TRP B CE2 1 
ATOM 994  C CE3 . TRP A 1 449 ? 159.087 214.121 239.756 1.00 57.84  ? 449 TRP B CE3 1 
ATOM 995  C CZ2 . TRP A 1 449 ? 159.763 216.867 239.772 1.00 57.45  ? 449 TRP B CZ2 1 
ATOM 996  C CZ3 . TRP A 1 449 ? 158.802 214.929 240.840 1.00 59.76  ? 449 TRP B CZ3 1 
ATOM 997  C CH2 . TRP A 1 449 ? 159.139 216.286 240.840 1.00 58.63  ? 449 TRP B CH2 1 
ATOM 998  N N   . TYR A 1 450 ? 160.416 209.716 237.266 1.00 54.45  ? 450 TYR B N   1 
ATOM 999  C CA  . TYR A 1 450 ? 159.962 208.404 236.830 1.00 54.58  ? 450 TYR B CA  1 
ATOM 1000 C C   . TYR A 1 450 ? 158.652 208.084 237.532 1.00 58.09  ? 450 TYR B C   1 
ATOM 1001 O O   . TYR A 1 450 ? 158.367 208.607 238.612 1.00 60.35  ? 450 TYR B O   1 
ATOM 1002 C CB  . TYR A 1 450 ? 160.994 207.306 237.115 1.00 56.16  ? 450 TYR B CB  1 
ATOM 1003 C CG  . TYR A 1 450 ? 161.226 206.995 238.578 1.00 58.14  ? 450 TYR B CG  1 
ATOM 1004 C CD1 . TYR A 1 450 ? 161.965 207.845 239.390 1.00 57.70  ? 450 TYR B CD1 1 
ATOM 1005 C CD2 . TYR A 1 450 ? 160.740 205.818 239.135 1.00 61.40  ? 450 TYR B CD2 1 
ATOM 1006 C CE1 . TYR A 1 450 ? 162.186 207.546 240.723 1.00 58.62  ? 450 TYR B CE1 1 
ATOM 1007 C CE2 . TYR A 1 450 ? 160.958 205.511 240.461 1.00 60.95  ? 450 TYR B CE2 1 
ATOM 1008 C CZ  . TYR A 1 450 ? 161.682 206.376 241.250 1.00 59.66  ? 450 TYR B CZ  1 
ATOM 1009 O OH  . TYR A 1 450 ? 161.900 206.068 242.572 1.00 59.02  ? 450 TYR B OH  1 
ATOM 1010 N N   . ARG A 1 451 ? 157.857 207.219 236.908 1.00 62.15  ? 451 ARG B N   1 
ATOM 1011 C CA  . ARG A 1 451 ? 156.552 206.842 237.435 1.00 67.88  ? 451 ARG B CA  1 
ATOM 1012 C C   . ARG A 1 451 ? 156.698 205.623 238.337 1.00 67.58  ? 451 ARG B C   1 
ATOM 1013 O O   . ARG A 1 451 ? 157.372 204.653 237.976 1.00 66.60  ? 451 ARG B O   1 
ATOM 1014 C CB  . ARG A 1 451 ? 155.577 206.550 236.296 1.00 66.88  ? 451 ARG B CB  1 
ATOM 1015 C CG  . ARG A 1 451 ? 154.174 206.170 236.731 1.00 68.84  ? 451 ARG B CG  1 
ATOM 1016 C CD  . ARG A 1 451 ? 153.283 205.952 235.518 1.00 73.27  ? 451 ARG B CD  1 
ATOM 1017 N NE  . ARG A 1 451 ? 153.137 207.159 234.715 1.00 76.63  ? 451 ARG B NE  1 
ATOM 1018 C CZ  . ARG A 1 451 ? 152.283 208.139 234.977 1.00 78.94  ? 451 ARG B CZ  1 
ATOM 1019 N NH1 . ARG A 1 451 ? 151.469 208.087 236.018 1.00 80.01  ? 451 ARG B NH1 1 
ATOM 1020 N NH2 . ARG A 1 451 ? 152.241 209.195 234.170 1.00 75.30  ? 451 ARG B NH2 1 
ATOM 1021 N N   . SER A 1 452 ? 156.063 205.675 239.509 1.00 65.28  ? 452 SER B N   1 
ATOM 1022 C CA  . SER A 1 452 ? 156.250 204.652 240.527 1.00 67.75  ? 452 SER B CA  1 
ATOM 1023 C C   . SER A 1 452 ? 155.042 203.756 240.748 1.00 70.80  ? 452 SER B C   1 
ATOM 1024 O O   . SER A 1 452 ? 155.215 202.628 241.220 1.00 77.58  ? 452 SER B O   1 
ATOM 1025 C CB  . SER A 1 452 ? 156.628 205.302 241.866 1.00 69.55  ? 452 SER B CB  1 
ATOM 1026 O OG  . SER A 1 452 ? 157.172 204.348 242.761 1.00 77.28  ? 452 SER B OG  1 
ATOM 1027 N N   . PHE A 1 453 ? 153.835 204.215 240.426 1.00 65.58  ? 453 PHE B N   1 
ATOM 1028 C CA  . PHE A 1 453 ? 152.628 203.443 240.684 1.00 69.64  ? 453 PHE B CA  1 
ATOM 1029 C C   . PHE A 1 453 ? 151.695 203.513 239.485 1.00 74.85  ? 453 PHE B C   1 
ATOM 1030 O O   . PHE A 1 453 ? 151.539 204.575 238.876 1.00 78.98  ? 453 PHE B O   1 
ATOM 1031 C CB  . PHE A 1 453 ? 151.895 203.957 241.929 1.00 72.09  ? 453 PHE B CB  1 
ATOM 1032 C CG  . PHE A 1 453 ? 152.767 204.069 243.144 1.00 73.62  ? 453 PHE B CG  1 
ATOM 1033 C CD1 . PHE A 1 453 ? 153.200 202.934 243.811 1.00 78.49  ? 453 PHE B CD1 1 
ATOM 1034 C CD2 . PHE A 1 453 ? 153.156 205.309 243.618 1.00 71.44  ? 453 PHE B CD2 1 
ATOM 1035 C CE1 . PHE A 1 453 ? 154.005 203.036 244.930 1.00 78.18  ? 453 PHE B CE1 1 
ATOM 1036 C CE2 . PHE A 1 453 ? 153.960 205.420 244.736 1.00 77.71  ? 453 PHE B CE2 1 
ATOM 1037 C CZ  . PHE A 1 453 ? 154.386 204.281 245.393 1.00 80.20  ? 453 PHE B CZ  1 
ATOM 1038 N N   . ARG A 1 454 ? 151.075 202.381 239.154 1.00 77.16  ? 454 ARG B N   1 
ATOM 1039 C CA  . ARG A 1 454 ? 150.001 202.355 238.170 1.00 80.52  ? 454 ARG B CA  1 
ATOM 1040 C C   . ARG A 1 454 ? 149.142 201.123 238.449 1.00 82.23  ? 454 ARG B C   1 
ATOM 1041 O O   . ARG A 1 454 ? 149.549 200.216 239.179 1.00 85.16  ? 454 ARG B O   1 
ATOM 1042 C CB  . ARG A 1 454 ? 150.539 202.344 236.728 1.00 80.18  ? 454 ARG B CB  1 
ATOM 1043 C CG  . ARG A 1 454 ? 149.516 202.792 235.679 1.00 80.41  ? 454 ARG B CG  1 
ATOM 1044 C CD  . ARG A 1 454 ? 150.157 203.432 234.466 1.00 75.65  ? 454 ARG B CD  1 
ATOM 1045 N NE  . ARG A 1 454 ? 150.721 202.408 233.597 1.00 72.05  ? 454 ARG B NE  1 
ATOM 1046 C CZ  . ARG A 1 454 ? 150.006 201.626 232.799 1.00 68.13  ? 454 ARG B CZ  1 
ATOM 1047 N NH1 . ARG A 1 454 ? 148.698 201.778 232.666 1.00 64.58  ? 454 ARG B NH1 1 
ATOM 1048 N NH2 . ARG A 1 454 ? 150.619 200.667 232.116 1.00 68.40  ? 454 ARG B NH2 1 
ATOM 1049 N N   . LYS A 1 455 ? 147.936 201.113 237.872 1.00 81.38  ? 455 LYS B N   1 
ATOM 1050 C CA  . LYS A 1 455 ? 146.980 200.034 238.111 1.00 84.04  ? 455 LYS B CA  1 
ATOM 1051 C C   . LYS A 1 455 ? 147.469 198.704 237.543 1.00 81.94  ? 455 LYS B C   1 
ATOM 1052 O O   . LYS A 1 455 ? 147.476 197.685 238.242 1.00 84.55  ? 455 LYS B O   1 
ATOM 1053 C CB  . LYS A 1 455 ? 145.625 200.402 237.504 1.00 88.10  ? 455 LYS B CB  1 
ATOM 1054 C CG  . LYS A 1 455 ? 144.987 201.648 238.095 1.00 90.80  ? 455 LYS B CG  1 
ATOM 1055 C CD  . LYS A 1 455 ? 144.698 201.475 239.575 1.00 90.90  ? 455 LYS B CD  1 
ATOM 1056 C CE  . LYS A 1 455 ? 143.621 200.427 239.799 1.00 94.80  ? 455 LYS B CE  1 
ATOM 1057 N NZ  . LYS A 1 455 ? 142.311 200.852 239.230 1.00 95.76  ? 455 LYS B NZ  1 
ATOM 1058 N N   . SER A 1 456 ? 147.882 198.692 236.277 1.00 77.38  ? 456 SER B N   1 
ATOM 1059 C CA  . SER A 1 456 ? 148.189 197.443 235.588 1.00 75.02  ? 456 SER B CA  1 
ATOM 1060 C C   . SER A 1 456 ? 149.493 197.608 234.815 1.00 75.24  ? 456 SER B C   1 
ATOM 1061 O O   . SER A 1 456 ? 150.219 198.593 234.978 1.00 78.22  ? 456 SER B O   1 
ATOM 1062 C CB  . SER A 1 456 ? 147.028 197.034 234.673 1.00 72.52  ? 456 SER B CB  1 
ATOM 1063 O OG  . SER A 1 456 ? 146.834 197.987 233.643 1.00 73.34  ? 456 SER B OG  1 
ATOM 1064 N N   . LYS A 1 457 ? 149.788 196.627 233.963 1.00 73.40  ? 457 LYS B N   1 
ATOM 1065 C CA  . LYS A 1 457 ? 151.028 196.602 233.203 1.00 71.62  ? 457 LYS B CA  1 
ATOM 1066 C C   . LYS A 1 457 ? 150.933 197.532 231.993 1.00 76.01  ? 457 LYS B C   1 
ATOM 1067 O O   . LYS A 1 457 ? 149.920 198.196 231.759 1.00 78.07  ? 457 LYS B O   1 
ATOM 1068 C CB  . LYS A 1 457 ? 151.352 195.175 232.766 1.00 70.04  ? 457 LYS B CB  1 
ATOM 1069 C CG  . LYS A 1 457 ? 151.736 194.230 233.898 1.00 77.96  ? 457 LYS B CG  1 
ATOM 1070 C CD  . LYS A 1 457 ? 152.695 194.880 234.883 1.00 81.53  ? 457 LYS B CD  1 
ATOM 1071 C CE  . LYS A 1 457 ? 153.242 193.869 235.880 1.00 80.51  ? 457 LYS B CE  1 
ATOM 1072 N NZ  . LYS A 1 457 ? 152.312 192.724 236.083 1.00 76.62  ? 457 LYS B NZ  1 
ATOM 1073 N N   . LEU A 1 458 ? 152.008 197.572 231.207 1.00 74.77  ? 458 LEU B N   1 
ATOM 1074 C CA  . LEU A 1 458 ? 152.099 198.417 230.022 1.00 67.31  ? 458 LEU B CA  1 
ATOM 1075 C C   . LEU A 1 458 ? 152.419 197.566 228.805 1.00 66.22  ? 458 LEU B C   1 
ATOM 1076 O O   . LEU A 1 458 ? 153.342 196.746 228.842 1.00 71.24  ? 458 LEU B O   1 
ATOM 1077 C CB  . LEU A 1 458 ? 153.166 199.503 230.189 1.00 65.79  ? 458 LEU B CB  1 
ATOM 1078 C CG  . LEU A 1 458 ? 153.202 200.639 229.162 1.00 68.84  ? 458 LEU B CG  1 
ATOM 1079 C CD1 . LEU A 1 458 ? 151.933 201.476 229.169 1.00 71.18  ? 458 LEU B CD1 1 
ATOM 1080 C CD2 . LEU A 1 458 ? 154.420 201.513 229.413 1.00 66.77  ? 458 LEU B CD2 1 
ATOM 1081 N N   . LYS A 1 459 ? 151.656 197.765 227.734 1.00 63.13  ? 459 LYS B N   1 
ATOM 1082 C CA  . LYS A 1 459 ? 151.963 197.145 226.461 1.00 66.30  ? 459 LYS B CA  1 
ATOM 1083 C C   . LYS A 1 459 ? 153.238 197.762 225.886 1.00 68.91  ? 459 LYS B C   1 
ATOM 1084 O O   . LYS A 1 459 ? 153.610 198.881 226.250 1.00 72.97  ? 459 LYS B O   1 
ATOM 1085 C CB  . LYS A 1 459 ? 150.791 197.317 225.495 1.00 72.22  ? 459 LYS B CB  1 
ATOM 1086 C CG  . LYS A 1 459 ? 150.532 198.752 225.057 1.00 75.94  ? 459 LYS B CG  1 
ATOM 1087 C CD  . LYS A 1 459 ? 149.418 198.838 224.016 1.00 77.45  ? 459 LYS B CD  1 
ATOM 1088 C CE  . LYS A 1 459 ? 148.132 198.162 224.479 1.00 83.28  ? 459 LYS B CE  1 
ATOM 1089 N NZ  . LYS A 1 459 ? 147.748 198.543 225.870 1.00 84.42  ? 459 LYS B NZ  1 
ATOM 1090 N N   . PRO A 1 460 ? 153.951 197.028 225.026 1.00 65.36  ? 460 PRO B N   1 
ATOM 1091 C CA  . PRO A 1 460 ? 155.192 197.564 224.451 1.00 64.84  ? 460 PRO B CA  1 
ATOM 1092 C C   . PRO A 1 460 ? 154.968 198.831 223.635 1.00 62.73  ? 460 PRO B C   1 
ATOM 1093 O O   . PRO A 1 460 ? 153.949 198.985 222.959 1.00 63.49  ? 460 PRO B O   1 
ATOM 1094 C CB  . PRO A 1 460 ? 155.694 196.415 223.572 1.00 65.34  ? 460 PRO B CB  1 
ATOM 1095 C CG  . PRO A 1 460 ? 155.173 195.196 224.240 1.00 64.49  ? 460 PRO B CG  1 
ATOM 1096 C CD  . PRO A 1 460 ? 153.829 195.576 224.798 1.00 63.00  ? 460 PRO B CD  1 
ATOM 1097 N N   . PHE A 1 461 ? 155.942 199.742 223.732 1.00 61.06  ? 461 PHE B N   1 
ATOM 1098 C CA  . PHE A 1 461 ? 155.998 200.998 222.979 1.00 63.93  ? 461 PHE B CA  1 
ATOM 1099 C C   . PHE A 1 461 ? 154.777 201.881 223.253 1.00 66.90  ? 461 PHE B C   1 
ATOM 1100 O O   . PHE A 1 461 ? 153.969 202.169 222.368 1.00 72.87  ? 461 PHE B O   1 
ATOM 1101 C CB  . PHE A 1 461 ? 156.164 200.731 221.478 1.00 63.59  ? 461 PHE B CB  1 
ATOM 1102 C CG  . PHE A 1 461 ? 157.523 200.220 221.101 1.00 64.14  ? 461 PHE B CG  1 
ATOM 1103 C CD1 . PHE A 1 461 ? 158.663 200.784 221.644 1.00 66.54  ? 461 PHE B CD1 1 
ATOM 1104 C CD2 . PHE A 1 461 ? 157.660 199.179 220.197 1.00 67.05  ? 461 PHE B CD2 1 
ATOM 1105 C CE1 . PHE A 1 461 ? 159.915 200.317 221.299 1.00 66.82  ? 461 PHE B CE1 1 
ATOM 1106 C CE2 . PHE A 1 461 ? 158.910 198.708 219.846 1.00 70.39  ? 461 PHE B CE2 1 
ATOM 1107 C CZ  . PHE A 1 461 ? 160.039 199.277 220.398 1.00 68.16  ? 461 PHE B CZ  1 
ATOM 1108 N N   . GLU A 1 462 ? 154.655 202.307 224.509 1.00 62.32  ? 462 GLU B N   1 
ATOM 1109 C CA  . GLU A 1 462 ? 153.610 203.239 224.905 1.00 62.75  ? 462 GLU B CA  1 
ATOM 1110 C C   . GLU A 1 462 ? 154.188 204.277 225.857 1.00 61.23  ? 462 GLU B C   1 
ATOM 1111 O O   . GLU A 1 462 ? 155.075 203.980 226.661 1.00 66.40  ? 462 GLU B O   1 
ATOM 1112 C CB  . GLU A 1 462 ? 152.425 202.520 225.568 1.00 68.76  ? 462 GLU B CB  1 
ATOM 1113 C CG  . GLU A 1 462 ? 151.152 203.357 225.624 1.00 76.50  ? 462 GLU B CG  1 
ATOM 1114 C CD  . GLU A 1 462 ? 149.895 202.519 225.743 1.00 82.84  ? 462 GLU B CD  1 
ATOM 1115 O OE1 . GLU A 1 462 ? 149.878 201.580 226.565 1.00 84.04  ? 462 GLU B OE1 1 
ATOM 1116 O OE2 . GLU A 1 462 ? 148.921 202.799 225.013 1.00 82.74  ? 462 GLU B OE2 1 
ATOM 1117 N N   . ARG A 1 463 ? 153.675 205.500 225.753 1.00 57.48  ? 463 ARG B N   1 
ATOM 1118 C CA  . ARG A 1 463 ? 154.056 206.604 226.623 1.00 60.47  ? 463 ARG B CA  1 
ATOM 1119 C C   . ARG A 1 463 ? 152.839 207.043 227.424 1.00 69.06  ? 463 ARG B C   1 
ATOM 1120 O O   . ARG A 1 463 ? 151.777 207.304 226.850 1.00 73.48  ? 463 ARG B O   1 
ATOM 1121 C CB  . ARG A 1 463 ? 154.613 207.776 225.811 1.00 58.17  ? 463 ARG B CB  1 
ATOM 1122 C CG  . ARG A 1 463 ? 155.623 208.627 226.557 1.00 60.41  ? 463 ARG B CG  1 
ATOM 1123 C CD  . ARG A 1 463 ? 155.816 209.977 225.885 1.00 58.34  ? 463 ARG B CD  1 
ATOM 1124 N NE  . ARG A 1 463 ? 156.619 209.877 224.673 1.00 60.14  ? 463 ARG B NE  1 
ATOM 1125 C CZ  . ARG A 1 463 ? 156.158 210.089 223.449 1.00 64.39  ? 463 ARG B CZ  1 
ATOM 1126 N NH1 . ARG A 1 463 ? 154.895 210.417 223.234 1.00 67.06  ? 463 ARG B NH1 1 
ATOM 1127 N NH2 . ARG A 1 463 ? 156.985 209.968 222.415 1.00 64.27  ? 463 ARG B NH2 1 
ATOM 1128 N N   . ASP A 1 464 ? 152.994 207.126 228.743 1.00 67.67  ? 464 ASP B N   1 
ATOM 1129 C CA  . ASP A 1 464 ? 151.910 207.490 229.654 1.00 67.08  ? 464 ASP B CA  1 
ATOM 1130 C C   . ASP A 1 464 ? 152.244 208.858 230.248 1.00 66.82  ? 464 ASP B C   1 
ATOM 1131 O O   . ASP A 1 464 ? 152.973 208.964 231.235 1.00 66.47  ? 464 ASP B O   1 
ATOM 1132 C CB  . ASP A 1 464 ? 151.724 206.428 230.736 1.00 69.93  ? 464 ASP B CB  1 
ATOM 1133 C CG  . ASP A 1 464 ? 150.346 206.472 231.371 1.00 77.62  ? 464 ASP B CG  1 
ATOM 1134 O OD1 . ASP A 1 464 ? 149.921 207.558 231.818 1.00 79.77  ? 464 ASP B OD1 1 
ATOM 1135 O OD2 . ASP A 1 464 ? 149.683 205.415 231.422 1.00 81.06  ? 464 ASP B OD2 1 
ATOM 1136 N N   . ILE A 1 465 ? 151.688 209.905 229.640 1.00 65.29  ? 465 ILE B N   1 
ATOM 1137 C CA  . ILE A 1 465 ? 152.014 211.273 230.032 1.00 65.69  ? 465 ILE B CA  1 
ATOM 1138 C C   . ILE A 1 465 ? 151.171 211.700 231.235 1.00 68.21  ? 465 ILE B C   1 
ATOM 1139 O O   . ILE A 1 465 ? 151.618 212.514 232.055 1.00 68.98  ? 465 ILE B O   1 
ATOM 1140 C CB  . ILE A 1 465 ? 151.838 212.229 228.826 1.00 69.96  ? 465 ILE B CB  1 
ATOM 1141 C CG1 . ILE A 1 465 ? 152.795 211.894 227.669 1.00 70.88  ? 465 ILE B CG1 1 
ATOM 1142 C CG2 . ILE A 1 465 ? 152.071 213.692 229.199 1.00 72.94  ? 465 ILE B CG2 1 
ATOM 1143 C CD1 . ILE A 1 465 ? 152.277 210.892 226.633 1.00 70.57  ? 465 ILE B CD1 1 
ATOM 1144 N N   . SER A 1 466 ? 149.987 211.106 231.398 1.00 70.55  ? 466 SER B N   1 
ATOM 1145 C CA  . SER A 1 466 ? 148.976 211.607 232.323 1.00 73.56  ? 466 SER B CA  1 
ATOM 1146 C C   . SER A 1 466 ? 149.430 211.529 233.778 1.00 72.46  ? 466 SER B C   1 
ATOM 1147 O O   . SER A 1 466 ? 150.117 210.590 234.187 1.00 72.24  ? 466 SER B O   1 
ATOM 1148 C CB  . SER A 1 466 ? 147.675 210.826 232.147 1.00 75.97  ? 466 SER B CB  1 
ATOM 1149 O OG  . SER A 1 466 ? 146.622 211.413 232.890 1.00 80.47  ? 466 SER B OG  1 
ATOM 1150 N N   . THR A 1 467 ? 149.039 212.539 234.554 1.00 73.89  ? 467 THR B N   1 
ATOM 1151 C CA  . THR A 1 467 ? 149.442 212.709 235.949 1.00 76.69  ? 467 THR B CA  1 
ATOM 1152 C C   . THR A 1 467 ? 148.175 212.741 236.802 1.00 79.44  ? 467 THR B C   1 
ATOM 1153 O O   . THR A 1 467 ? 147.605 213.808 237.038 1.00 80.83  ? 467 THR B O   1 
ATOM 1154 C CB  . THR A 1 467 ? 150.258 213.993 236.131 1.00 77.59  ? 467 THR B CB  1 
ATOM 1155 O OG1 . THR A 1 467 ? 149.453 215.122 235.772 1.00 78.32  ? 467 THR B OG1 1 
ATOM 1156 C CG2 . THR A 1 467 ? 151.488 213.978 235.238 1.00 76.09  ? 467 THR B CG2 1 
ATOM 1157 N N   . GLU A 1 468 ? 147.737 211.574 237.269 1.00 79.30  ? 468 GLU B N   1 
ATOM 1158 C CA  . GLU A 1 468 ? 146.539 211.470 238.089 1.00 79.94  ? 468 GLU B CA  1 
ATOM 1159 C C   . GLU A 1 468 ? 146.854 210.687 239.355 1.00 80.21  ? 468 GLU B C   1 
ATOM 1160 O O   . GLU A 1 468 ? 147.803 209.903 239.405 1.00 83.17  ? 468 GLU B O   1 
ATOM 1161 C CB  . GLU A 1 468 ? 145.383 210.797 237.329 1.00 79.11  ? 468 GLU B CB  1 
ATOM 1162 C CG  . GLU A 1 468 ? 145.577 209.311 237.043 1.00 82.67  ? 468 GLU B CG  1 
ATOM 1163 C CD  . GLU A 1 468 ? 146.374 209.034 235.779 1.00 86.33  ? 468 GLU B CD  1 
ATOM 1164 O OE1 . GLU A 1 468 ? 147.040 209.956 235.264 1.00 84.27  ? 468 GLU B OE1 1 
ATOM 1165 O OE2 . GLU A 1 468 ? 146.333 207.883 235.297 1.00 91.21  ? 468 GLU B OE2 1 
ATOM 1166 N N   . ILE A 1 469 ? 146.038 210.915 240.387 1.00 74.87  ? 469 ILE B N   1 
ATOM 1167 C CA  . ILE A 1 469 ? 146.264 210.259 241.670 1.00 76.86  ? 469 ILE B CA  1 
ATOM 1168 C C   . ILE A 1 469 ? 145.965 208.764 241.556 1.00 79.59  ? 469 ILE B C   1 
ATOM 1169 O O   . ILE A 1 469 ? 145.229 208.306 240.672 1.00 82.74  ? 469 ILE B O   1 
ATOM 1170 C CB  . ILE A 1 469 ? 145.427 210.928 242.775 1.00 81.55  ? 469 ILE B CB  1 
ATOM 1171 C CG1 . ILE A 1 469 ? 146.112 210.788 244.136 1.00 86.99  ? 469 ILE B CG1 1 
ATOM 1172 C CG2 . ILE A 1 469 ? 144.007 210.372 242.821 1.00 82.57  ? 469 ILE B CG2 1 
ATOM 1173 C CD1 . ILE A 1 469 ? 147.287 211.716 244.319 1.00 88.05  ? 469 ILE B CD1 1 
ATOM 1174 N N   . TYR A 1 470 ? 146.578 207.988 242.447 1.00 80.04  ? 470 TYR B N   1 
ATOM 1175 C CA  . TYR A 1 470 ? 146.508 206.534 242.401 1.00 81.50  ? 470 TYR B CA  1 
ATOM 1176 C C   . TYR A 1 470 ? 146.029 206.017 243.748 1.00 83.76  ? 470 TYR B C   1 
ATOM 1177 O O   . TYR A 1 470 ? 146.558 206.412 244.791 1.00 84.66  ? 470 TYR B O   1 
ATOM 1178 C CB  . TYR A 1 470 ? 147.875 205.936 242.030 1.00 81.87  ? 470 TYR B CB  1 
ATOM 1179 C CG  . TYR A 1 470 ? 148.035 204.450 242.286 1.00 80.25  ? 470 TYR B CG  1 
ATOM 1180 C CD1 . TYR A 1 470 ? 147.651 203.520 241.329 1.00 81.60  ? 470 TYR B CD1 1 
ATOM 1181 C CD2 . TYR A 1 470 ? 148.623 203.979 243.457 1.00 81.32  ? 470 TYR B CD2 1 
ATOM 1182 C CE1 . TYR A 1 470 ? 147.806 202.164 241.547 1.00 84.54  ? 470 TYR B CE1 1 
ATOM 1183 C CE2 . TYR A 1 470 ? 148.782 202.627 243.683 1.00 84.77  ? 470 TYR B CE2 1 
ATOM 1184 C CZ  . TYR A 1 470 ? 148.374 201.723 242.724 1.00 87.29  ? 470 TYR B CZ  1 
ATOM 1185 O OH  . TYR A 1 470 ? 148.534 200.375 242.944 1.00 88.80  ? 470 TYR B OH  1 
ATOM 1186 N N   . GLN A 1 471 ? 145.039 205.130 243.723 1.00 85.60  ? 471 GLN B N   1 
ATOM 1187 C CA  . GLN A 1 471 ? 144.456 204.562 244.931 1.00 88.18  ? 471 GLN B CA  1 
ATOM 1188 C C   . GLN A 1 471 ? 145.023 203.166 245.150 1.00 87.65  ? 471 GLN B C   1 
ATOM 1189 O O   . GLN A 1 471 ? 144.895 202.297 244.281 1.00 86.16  ? 471 GLN B O   1 
ATOM 1190 C CB  . GLN A 1 471 ? 142.932 204.510 244.827 1.00 91.53  ? 471 GLN B CB  1 
ATOM 1191 C CG  . GLN A 1 471 ? 142.262 203.731 245.945 1.00 93.09  ? 471 GLN B CG  1 
ATOM 1192 C CD  . GLN A 1 471 ? 140.795 203.464 245.673 1.00 93.92  ? 471 GLN B CD  1 
ATOM 1193 O OE1 . GLN A 1 471 ? 140.076 204.329 245.173 1.00 95.06  ? 471 GLN B OE1 1 
ATOM 1194 N NE2 . GLN A 1 471 ? 140.341 202.263 246.010 1.00 92.68  ? 471 GLN B NE2 1 
ATOM 1195 N N   . ALA A 1 472 ? 145.645 202.953 246.310 1.00 89.88  ? 472 ALA B N   1 
ATOM 1196 C CA  . ALA A 1 472 ? 146.213 201.656 246.649 1.00 91.92  ? 472 ALA B CA  1 
ATOM 1197 C C   . ALA A 1 472 ? 145.405 200.897 247.692 1.00 96.04  ? 472 ALA B C   1 
ATOM 1198 O O   . ALA A 1 472 ? 145.609 199.689 247.849 1.00 97.82  ? 472 ALA B O   1 
ATOM 1199 C CB  . ALA A 1 472 ? 147.651 201.821 247.154 1.00 90.85  ? 472 ALA B CB  1 
ATOM 1200 N N   . GLY A 1 473 ? 144.500 201.570 248.403 1.00 96.87  ? 473 GLY B N   1 
ATOM 1201 C CA  . GLY A 1 473 ? 143.683 200.946 249.415 1.00 97.31  ? 473 GLY B CA  1 
ATOM 1202 C C   . GLY A 1 473 ? 142.228 200.822 249.004 1.00 96.33  ? 473 GLY B C   1 
ATOM 1203 O O   . GLY A 1 473 ? 141.844 201.074 247.860 1.00 96.36  ? 473 GLY B O   1 
ATOM 1204 N N   . ASN A 1 474 ? 141.409 200.414 249.974 1.00 94.72  ? 474 ASN B N   1 
ATOM 1205 C CA  . ASN A 1 474 ? 139.979 200.272 249.729 1.00 99.35  ? 474 ASN B CA  1 
ATOM 1206 C C   . ASN A 1 474 ? 139.260 201.615 249.713 1.00 100.12 ? 474 ASN B C   1 
ATOM 1207 O O   . ASN A 1 474 ? 138.292 201.785 248.963 1.00 98.10  ? 474 ASN B O   1 
ATOM 1208 C CB  . ASN A 1 474 ? 139.355 199.357 250.783 1.00 103.80 ? 474 ASN B CB  1 
ATOM 1209 C CG  . ASN A 1 474 ? 139.266 197.915 250.323 1.00 105.83 ? 474 ASN B CG  1 
ATOM 1210 O OD1 . ASN A 1 474 ? 138.953 197.638 249.165 1.00 106.85 ? 474 ASN B OD1 1 
ATOM 1211 N ND2 . ASN A 1 474 ? 139.542 196.986 251.232 1.00 103.31 ? 474 ASN B ND2 1 
ATOM 1212 N N   . LYS A 1 475 ? 139.708 202.567 250.522 1.00 100.76 ? 475 LYS B N   1 
ATOM 1213 C CA  . LYS A 1 475 ? 139.049 203.866 250.610 1.00 101.83 ? 475 LYS B CA  1 
ATOM 1214 C C   . LYS A 1 475 ? 139.410 204.724 249.402 1.00 104.17 ? 475 LYS B C   1 
ATOM 1215 O O   . LYS A 1 475 ? 140.597 204.899 249.109 1.00 104.96 ? 475 LYS B O   1 
ATOM 1216 C CB  . LYS A 1 475 ? 139.449 204.583 251.895 1.00 101.75 ? 475 LYS B CB  1 
ATOM 1217 C CG  . LYS A 1 475 ? 138.593 205.795 252.223 1.00 104.81 ? 475 LYS B CG  1 
ATOM 1218 C CD  . LYS A 1 475 ? 138.795 206.239 253.662 1.00 108.87 ? 475 LYS B CD  1 
ATOM 1219 C CE  . LYS A 1 475 ? 137.865 207.386 254.022 1.00 111.47 ? 475 LYS B CE  1 
ATOM 1220 N NZ  . LYS A 1 475 ? 137.978 207.764 255.458 1.00 114.19 ? 475 LYS B NZ  1 
ATOM 1221 N N   . PRO A 1 476 ? 138.427 205.255 248.674 1.00 105.79 ? 476 PRO B N   1 
ATOM 1222 C CA  . PRO A 1 476 ? 138.738 206.174 247.571 1.00 104.25 ? 476 PRO B CA  1 
ATOM 1223 C C   . PRO A 1 476 ? 139.291 207.491 248.099 1.00 105.17 ? 476 PRO B C   1 
ATOM 1224 O O   . PRO A 1 476 ? 138.720 208.100 249.006 1.00 105.34 ? 476 PRO B O   1 
ATOM 1225 C CB  . PRO A 1 476 ? 137.383 206.373 246.882 1.00 105.04 ? 476 PRO B CB  1 
ATOM 1226 C CG  . PRO A 1 476 ? 136.599 205.154 247.236 1.00 104.69 ? 476 PRO B CG  1 
ATOM 1227 C CD  . PRO A 1 476 ? 137.024 204.810 248.637 1.00 105.38 ? 476 PRO B CD  1 
ATOM 1228 N N   . CYS A 1 477 ? 140.409 207.927 247.525 1.00 107.47 ? 477 CYS B N   1 
ATOM 1229 C CA  . CYS A 1 477 ? 141.034 209.188 247.898 1.00 112.69 ? 477 CYS B CA  1 
ATOM 1230 C C   . CYS A 1 477 ? 140.707 210.231 246.836 1.00 113.32 ? 477 CYS B C   1 
ATOM 1231 O O   . CYS A 1 477 ? 141.091 210.079 245.672 1.00 114.78 ? 477 CYS B O   1 
ATOM 1232 C CB  . CYS A 1 477 ? 142.549 209.039 248.052 1.00 111.61 ? 477 CYS B CB  1 
ATOM 1233 S SG  . CYS A 1 477 ? 143.378 210.570 248.568 1.00 114.23 ? 477 CYS B SG  1 
ATOM 1234 N N   . LYS A 1 478 ? 140.001 211.282 247.239 1.00 110.47 ? 478 LYS B N   1 
ATOM 1235 C CA  . LYS A 1 478 ? 139.676 212.398 246.366 1.00 111.90 ? 478 LYS B CA  1 
ATOM 1236 C C   . LYS A 1 478 ? 140.482 213.618 246.785 1.00 110.55 ? 478 LYS B C   1 
ATOM 1237 O O   . LYS A 1 478 ? 140.634 213.894 247.979 1.00 108.97 ? 478 LYS B O   1 
ATOM 1238 C CB  . LYS A 1 478 ? 138.176 212.716 246.405 1.00 116.24 ? 478 LYS B CB  1 
ATOM 1239 C CG  . LYS A 1 478 ? 137.213 211.593 245.961 1.00 117.23 ? 478 LYS B CG  1 
ATOM 1240 C CD  . LYS A 1 478 ? 137.223 211.296 244.449 1.00 120.64 ? 478 LYS B CD  1 
ATOM 1241 C CE  . LYS A 1 478 ? 138.156 210.153 244.045 1.00 120.21 ? 478 LYS B CE  1 
ATOM 1242 N NZ  . LYS A 1 478 ? 138.049 209.836 242.594 1.00 126.86 ? 478 LYS B NZ  1 
ATOM 1243 N N   . GLY A 1 479 ? 141.000 214.344 245.799 1.00 111.30 ? 479 GLY B N   1 
ATOM 1244 C CA  . GLY A 1 479 ? 141.858 215.476 246.079 1.00 113.46 ? 479 GLY B CA  1 
ATOM 1245 C C   . GLY A 1 479 ? 143.290 215.050 246.322 1.00 113.90 ? 479 GLY B C   1 
ATOM 1246 O O   . GLY A 1 479 ? 143.980 214.624 245.391 1.00 110.10 ? 479 GLY B O   1 
ATOM 1247 N N   . LYS A 1 480 ? 143.746 215.151 247.568 1.00 114.29 ? 480 LYS B N   1 
ATOM 1248 C CA  . LYS A 1 480 ? 145.101 214.745 247.910 1.00 107.89 ? 480 LYS B CA  1 
ATOM 1249 C C   . LYS A 1 480 ? 145.144 214.426 249.398 1.00 105.29 ? 480 LYS B C   1 
ATOM 1250 O O   . LYS A 1 480 ? 144.555 215.148 250.206 1.00 108.19 ? 480 LYS B O   1 
ATOM 1251 C CB  . LYS A 1 480 ? 146.112 215.846 247.565 1.00 103.17 ? 480 LYS B CB  1 
ATOM 1252 C CG  . LYS A 1 480 ? 147.556 215.460 247.804 1.00 100.23 ? 480 LYS B CG  1 
ATOM 1253 C CD  . LYS A 1 480 ? 147.957 214.372 246.822 1.00 97.07  ? 480 LYS B CD  1 
ATOM 1254 C CE  . LYS A 1 480 ? 149.390 213.923 247.016 1.00 88.26  ? 480 LYS B CE  1 
ATOM 1255 N NZ  . LYS A 1 480 ? 150.367 214.999 246.697 1.00 81.84  ? 480 LYS B NZ  1 
ATOM 1256 N N   . GLY A 1 481 ? 145.841 213.348 249.751 1.00 99.89  ? 481 GLY B N   1 
ATOM 1257 C CA  . GLY A 1 481 ? 145.952 212.938 251.131 1.00 101.66 ? 481 GLY B CA  1 
ATOM 1258 C C   . GLY A 1 481 ? 146.699 211.630 251.291 1.00 97.21  ? 481 GLY B C   1 
ATOM 1259 O O   . GLY A 1 481 ? 147.309 211.120 250.347 1.00 94.43  ? 481 GLY B O   1 
ATOM 1260 N N   . PRO A 1 482 ? 146.684 211.074 252.502 1.00 92.64  ? 482 PRO B N   1 
ATOM 1261 C CA  . PRO A 1 482 ? 147.315 209.769 252.728 1.00 87.40  ? 482 PRO B CA  1 
ATOM 1262 C C   . PRO A 1 482 ? 146.599 208.656 251.975 1.00 90.40  ? 482 PRO B C   1 
ATOM 1263 O O   . PRO A 1 482 ? 145.425 208.764 251.612 1.00 92.61  ? 482 PRO B O   1 
ATOM 1264 C CB  . PRO A 1 482 ? 147.195 209.573 254.242 1.00 88.01  ? 482 PRO B CB  1 
ATOM 1265 C CG  . PRO A 1 482 ? 147.100 210.951 254.792 1.00 90.53  ? 482 PRO B CG  1 
ATOM 1266 C CD  . PRO A 1 482 ? 146.342 211.747 253.767 1.00 91.96  ? 482 PRO B CD  1 
ATOM 1267 N N   . ASN A 1 483 ? 147.357 207.587 251.715 1.00 89.02  ? 483 ASN B N   1 
ATOM 1268 C CA  . ASN A 1 483 ? 146.985 206.370 250.990 1.00 87.27  ? 483 ASN B CA  1 
ATOM 1269 C C   . ASN A 1 483 ? 146.696 206.608 249.510 1.00 87.05  ? 483 ASN B C   1 
ATOM 1270 O O   . ASN A 1 483 ? 146.346 205.655 248.805 1.00 90.02  ? 483 ASN B O   1 
ATOM 1271 C CB  . ASN A 1 483 ? 145.788 205.642 251.621 1.00 89.27  ? 483 ASN B CB  1 
ATOM 1272 C CG  . ASN A 1 483 ? 146.085 205.137 253.018 1.00 89.10  ? 483 ASN B CG  1 
ATOM 1273 O OD1 . ASN A 1 483 ? 145.490 205.592 253.995 1.00 87.78  ? 483 ASN B OD1 1 
ATOM 1274 N ND2 . ASN A 1 483 ? 147.010 204.190 253.121 1.00 87.48  ? 483 ASN B ND2 1 
ATOM 1275 N N   . CYS A 1 484 ? 146.829 207.836 249.014 1.00 87.14  ? 484 CYS B N   1 
ATOM 1276 C CA  . CYS A 1 484 ? 146.784 208.126 247.588 1.00 90.37  ? 484 CYS B CA  1 
ATOM 1277 C C   . CYS A 1 484 ? 148.001 208.975 247.249 1.00 87.70  ? 484 CYS B C   1 
ATOM 1278 O O   . CYS A 1 484 ? 148.297 209.951 247.945 1.00 88.76  ? 484 CYS B O   1 
ATOM 1279 C CB  . CYS A 1 484 ? 145.460 208.808 247.193 1.00 95.55  ? 484 CYS B CB  1 
ATOM 1280 S SG  . CYS A 1 484 ? 145.219 210.527 247.706 1.00 104.30 ? 484 CYS B SG  1 
ATOM 1281 N N   . TYR A 1 485 ? 148.730 208.580 246.209 1.00 83.82  ? 485 TYR B N   1 
ATOM 1282 C CA  . TYR A 1 485 ? 150.090 209.055 245.993 1.00 78.94  ? 485 TYR B CA  1 
ATOM 1283 C C   . TYR A 1 485 ? 150.229 209.724 244.633 1.00 77.45  ? 485 TYR B C   1 
ATOM 1284 O O   . TYR A 1 485 ? 149.604 209.304 243.654 1.00 82.61  ? 485 TYR B O   1 
ATOM 1285 C CB  . TYR A 1 485 ? 151.088 207.896 246.100 1.00 82.23  ? 485 TYR B CB  1 
ATOM 1286 C CG  . TYR A 1 485 ? 150.960 207.088 247.374 1.00 86.69  ? 485 TYR B CG  1 
ATOM 1287 C CD1 . TYR A 1 485 ? 150.824 207.713 248.609 1.00 86.55  ? 485 TYR B CD1 1 
ATOM 1288 C CD2 . TYR A 1 485 ? 150.963 205.699 247.340 1.00 85.05  ? 485 TYR B CD2 1 
ATOM 1289 C CE1 . TYR A 1 485 ? 150.700 206.976 249.773 1.00 85.64  ? 485 TYR B CE1 1 
ATOM 1290 C CE2 . TYR A 1 485 ? 150.840 204.955 248.498 1.00 84.38  ? 485 TYR B CE2 1 
ATOM 1291 C CZ  . TYR A 1 485 ? 150.711 205.598 249.711 1.00 86.27  ? 485 TYR B CZ  1 
ATOM 1292 O OH  . TYR A 1 485 ? 150.590 204.861 250.866 1.00 91.17  ? 485 TYR B OH  1 
ATOM 1293 N N   . PHE A 1 486 ? 151.047 210.767 244.586 1.00 73.94  ? 486 PHE B N   1 
ATOM 1294 C CA  . PHE A 1 486 ? 151.416 211.398 243.326 1.00 70.22  ? 486 PHE B CA  1 
ATOM 1295 C C   . PHE A 1 486 ? 152.313 210.437 242.558 1.00 68.65  ? 486 PHE B C   1 
ATOM 1296 O O   . PHE A 1 486 ? 153.349 210.017 243.091 1.00 72.69  ? 486 PHE B O   1 
ATOM 1297 C CB  . PHE A 1 486 ? 152.138 212.716 243.596 1.00 72.64  ? 486 PHE B CB  1 
ATOM 1298 C CG  . PHE A 1 486 ? 152.239 213.620 242.400 1.00 76.22  ? 486 PHE B CG  1 
ATOM 1299 C CD1 . PHE A 1 486 ? 151.127 213.885 241.616 1.00 76.80  ? 486 PHE B CD1 1 
ATOM 1300 C CD2 . PHE A 1 486 ? 153.445 214.215 242.065 1.00 76.61  ? 486 PHE B CD2 1 
ATOM 1301 C CE1 . PHE A 1 486 ? 151.217 214.720 240.516 1.00 78.75  ? 486 PHE B CE1 1 
ATOM 1302 C CE2 . PHE A 1 486 ? 153.543 215.051 240.967 1.00 74.36  ? 486 PHE B CE2 1 
ATOM 1303 C CZ  . PHE A 1 486 ? 152.428 215.303 240.192 1.00 78.01  ? 486 PHE B CZ  1 
ATOM 1304 N N   . PRO A 1 487 ? 151.967 210.056 241.324 1.00 66.74  ? 487 PRO B N   1 
ATOM 1305 C CA  . PRO A 1 487 ? 152.693 208.959 240.662 1.00 68.59  ? 487 PRO B CA  1 
ATOM 1306 C C   . PRO A 1 487 ? 154.080 209.327 240.165 1.00 65.00  ? 487 PRO B C   1 
ATOM 1307 O O   . PRO A 1 487 ? 154.810 208.427 239.733 1.00 66.01  ? 487 PRO B O   1 
ATOM 1308 C CB  . PRO A 1 487 ? 151.776 208.590 239.492 1.00 69.64  ? 487 PRO B CB  1 
ATOM 1309 C CG  . PRO A 1 487 ? 151.046 209.843 239.188 1.00 74.60  ? 487 PRO B CG  1 
ATOM 1310 C CD  . PRO A 1 487 ? 150.853 210.554 240.501 1.00 72.59  ? 487 PRO B CD  1 
ATOM 1311 N N   . LEU A 1 488 ? 154.476 210.593 240.214 1.00 63.85  ? 488 LEU B N   1 
ATOM 1312 C CA  . LEU A 1 488 ? 155.763 211.020 239.682 1.00 64.24  ? 488 LEU B CA  1 
ATOM 1313 C C   . LEU A 1 488 ? 156.745 211.254 240.820 1.00 61.50  ? 488 LEU B C   1 
ATOM 1314 O O   . LEU A 1 488 ? 156.426 211.943 241.795 1.00 61.78  ? 488 LEU B O   1 
ATOM 1315 C CB  . LEU A 1 488 ? 155.630 212.284 238.828 1.00 65.42  ? 488 LEU B CB  1 
ATOM 1316 C CG  . LEU A 1 488 ? 155.099 212.163 237.393 1.00 68.80  ? 488 LEU B CG  1 
ATOM 1317 C CD1 . LEU A 1 488 ? 153.611 211.847 237.325 1.00 73.06  ? 488 LEU B CD1 1 
ATOM 1318 C CD2 . LEU A 1 488 ? 155.412 213.430 236.606 1.00 70.66  ? 488 LEU B CD2 1 
ATOM 1319 N N   . GLN A 1 489 ? 157.933 210.676 240.688 1.00 55.91  ? 489 GLN B N   1 
ATOM 1320 C CA  . GLN A 1 489 ? 158.983 210.761 241.690 1.00 51.65  ? 489 GLN B CA  1 
ATOM 1321 C C   . GLN A 1 489 ? 160.276 211.159 241.001 1.00 54.73  ? 489 GLN B C   1 
ATOM 1322 O O   . GLN A 1 489 ? 160.595 210.645 239.926 1.00 59.47  ? 489 GLN B O   1 
ATOM 1323 C CB  . GLN A 1 489 ? 159.155 209.426 242.404 1.00 55.83  ? 489 GLN B CB  1 
ATOM 1324 C CG  . GLN A 1 489 ? 160.162 209.425 243.531 1.00 63.29  ? 489 GLN B CG  1 
ATOM 1325 C CD  . GLN A 1 489 ? 160.224 208.079 244.208 1.00 71.03  ? 489 GLN B CD  1 
ATOM 1326 O OE1 . GLN A 1 489 ? 159.538 207.147 243.798 1.00 74.03  ? 489 GLN B OE1 1 
ATOM 1327 N NE2 . GLN A 1 489 ? 161.040 207.966 245.248 1.00 68.23  ? 489 GLN B NE2 1 
ATOM 1328 N N   . SER A 1 490 ? 161.020 212.069 241.618 1.00 52.54  ? 490 SER B N   1 
ATOM 1329 C CA  . SER A 1 490 ? 162.213 212.639 241.009 1.00 54.34  ? 490 SER B CA  1 
ATOM 1330 C C   . SER A 1 490 ? 163.451 211.933 241.542 1.00 51.53  ? 490 SER B C   1 
ATOM 1331 O O   . SER A 1 490 ? 163.660 211.882 242.758 1.00 52.68  ? 490 SER B O   1 
ATOM 1332 C CB  . SER A 1 490 ? 162.303 214.138 241.286 1.00 54.74  ? 490 SER B CB  1 
ATOM 1333 O OG  . SER A 1 490 ? 163.572 214.643 240.913 1.00 56.28  ? 490 SER B OG  1 
ATOM 1334 N N   . TYR A 1 491 ? 164.257 211.378 240.636 1.00 49.73  ? 491 TYR B N   1 
ATOM 1335 C CA  . TYR A 1 491 ? 165.592 210.933 241.011 1.00 46.21  ? 491 TYR B CA  1 
ATOM 1336 C C   . TYR A 1 491 ? 166.400 212.104 241.549 1.00 47.08  ? 491 TYR B C   1 
ATOM 1337 O O   . TYR A 1 491 ? 166.486 213.159 240.914 1.00 53.40  ? 491 TYR B O   1 
ATOM 1338 C CB  . TYR A 1 491 ? 166.336 210.329 239.818 1.00 47.08  ? 491 TYR B CB  1 
ATOM 1339 C CG  . TYR A 1 491 ? 165.767 209.086 239.178 1.00 49.14  ? 491 TYR B CG  1 
ATOM 1340 C CD1 . TYR A 1 491 ? 165.744 207.877 239.862 1.00 54.38  ? 491 TYR B CD1 1 
ATOM 1341 C CD2 . TYR A 1 491 ? 165.310 209.106 237.867 1.00 47.47  ? 491 TYR B CD2 1 
ATOM 1342 C CE1 . TYR A 1 491 ? 165.251 206.729 239.267 1.00 57.87  ? 491 TYR B CE1 1 
ATOM 1343 C CE2 . TYR A 1 491 ? 164.811 207.966 237.266 1.00 47.69  ? 491 TYR B CE2 1 
ATOM 1344 C CZ  . TYR A 1 491 ? 164.787 206.781 237.968 1.00 56.44  ? 491 TYR B CZ  1 
ATOM 1345 O OH  . TYR A 1 491 ? 164.288 205.646 237.373 1.00 60.91  ? 491 TYR B OH  1 
ATOM 1346 N N   . GLY A 1 492 ? 166.994 211.918 242.724 1.00 45.14  ? 492 GLY B N   1 
ATOM 1347 C CA  . GLY A 1 492 ? 167.980 212.864 243.206 1.00 44.29  ? 492 GLY B CA  1 
ATOM 1348 C C   . GLY A 1 492 ? 169.331 212.508 242.623 1.00 47.36  ? 492 GLY B C   1 
ATOM 1349 O O   . GLY A 1 492 ? 169.848 211.410 242.849 1.00 55.50  ? 492 GLY B O   1 
ATOM 1350 N N   . PHE A 1 493 ? 169.901 213.429 241.854 1.00 46.49  ? 493 PHE B N   1 
ATOM 1351 C CA  . PHE A 1 493 ? 171.194 213.218 241.215 1.00 48.54  ? 493 PHE B CA  1 
ATOM 1352 C C   . PHE A 1 493 ? 172.221 214.132 241.866 1.00 51.45  ? 493 PHE B C   1 
ATOM 1353 O O   . PHE A 1 493 ? 172.158 215.357 241.713 1.00 58.74  ? 493 PHE B O   1 
ATOM 1354 C CB  . PHE A 1 493 ? 171.121 213.471 239.711 1.00 50.19  ? 493 PHE B CB  1 
ATOM 1355 C CG  . PHE A 1 493 ? 170.357 212.426 238.951 1.00 48.14  ? 493 PHE B CG  1 
ATOM 1356 C CD1 . PHE A 1 493 ? 170.432 211.094 239.314 1.00 45.49  ? 493 PHE B CD1 1 
ATOM 1357 C CD2 . PHE A 1 493 ? 169.590 212.774 237.851 1.00 51.66  ? 493 PHE B CD2 1 
ATOM 1358 C CE1 . PHE A 1 493 ? 169.744 210.129 238.607 1.00 45.26  ? 493 PHE B CE1 1 
ATOM 1359 C CE2 . PHE A 1 493 ? 168.897 211.813 237.138 1.00 50.64  ? 493 PHE B CE2 1 
ATOM 1360 C CZ  . PHE A 1 493 ? 168.978 210.488 237.515 1.00 46.92  ? 493 PHE B CZ  1 
ATOM 1361 N N   . ARG A 1 494 ? 173.162 213.536 242.590 1.00 46.38  ? 494 ARG B N   1 
ATOM 1362 C CA  . ARG A 1 494 ? 174.323 214.223 243.127 1.00 51.08  ? 494 ARG B CA  1 
ATOM 1363 C C   . ARG A 1 494 ? 175.574 213.477 242.688 1.00 56.97  ? 494 ARG B C   1 
ATOM 1364 O O   . ARG A 1 494 ? 175.545 212.250 242.546 1.00 60.44  ? 494 ARG B O   1 
ATOM 1365 C CB  . ARG A 1 494 ? 174.262 214.311 244.662 1.00 49.38  ? 494 ARG B CB  1 
ATOM 1366 C CG  . ARG A 1 494 ? 172.950 214.865 245.192 1.00 52.23  ? 494 ARG B CG  1 
ATOM 1367 C CD  . ARG A 1 494 ? 172.670 214.436 246.618 1.00 54.83  ? 494 ARG B CD  1 
ATOM 1368 N NE  . ARG A 1 494 ? 171.852 215.404 247.338 1.00 53.66  ? 494 ARG B NE  1 
ATOM 1369 C CZ  . ARG A 1 494 ? 170.596 215.191 247.704 1.00 52.53  ? 494 ARG B CZ  1 
ATOM 1370 N NH1 . ARG A 1 494 ? 169.980 214.052 247.431 1.00 49.63  ? 494 ARG B NH1 1 
ATOM 1371 N NH2 . ARG A 1 494 ? 169.939 216.145 248.358 1.00 56.67  ? 494 ARG B NH2 1 
ATOM 1372 N N   . PRO A 1 495 ? 176.684 214.187 242.450 1.00 55.55  ? 495 PRO B N   1 
ATOM 1373 C CA  . PRO A 1 495 ? 177.878 213.519 241.904 1.00 56.85  ? 495 PRO B CA  1 
ATOM 1374 C C   . PRO A 1 495 ? 178.584 212.603 242.890 1.00 56.83  ? 495 PRO B C   1 
ATOM 1375 O O   . PRO A 1 495 ? 179.474 211.850 242.475 1.00 56.27  ? 495 PRO B O   1 
ATOM 1376 C CB  . PRO A 1 495 ? 178.779 214.692 241.500 1.00 57.49  ? 495 PRO B CB  1 
ATOM 1377 C CG  . PRO A 1 495 ? 178.374 215.795 242.402 1.00 58.26  ? 495 PRO B CG  1 
ATOM 1378 C CD  . PRO A 1 495 ? 176.898 215.635 242.620 1.00 54.95  ? 495 PRO B CD  1 
ATOM 1379 N N   . THR A 1 496 ? 178.222 212.639 244.168 1.00 56.02  ? 496 THR B N   1 
ATOM 1380 C CA  . THR A 1 496 ? 178.839 211.808 245.189 1.00 56.42  ? 496 THR B CA  1 
ATOM 1381 C C   . THR A 1 496 ? 178.126 210.474 245.384 1.00 53.63  ? 496 THR B C   1 
ATOM 1382 O O   . THR A 1 496 ? 178.517 209.700 246.262 1.00 59.69  ? 496 THR B O   1 
ATOM 1383 C CB  . THR A 1 496 ? 178.897 212.574 246.512 1.00 62.70  ? 496 THR B CB  1 
ATOM 1384 O OG1 . THR A 1 496 ? 177.585 213.032 246.855 1.00 64.77  ? 496 THR B OG1 1 
ATOM 1385 C CG2 . THR A 1 496 ? 179.832 213.769 246.394 1.00 62.31  ? 496 THR B CG2 1 
ATOM 1386 N N   . TYR A 1 497 ? 177.093 210.192 244.594 1.00 47.32  ? 497 TYR B N   1 
ATOM 1387 C CA  . TYR A 1 497 ? 176.449 208.887 244.629 1.00 43.36  ? 497 TYR B CA  1 
ATOM 1388 C C   . TYR A 1 497 ? 177.340 207.810 244.020 1.00 43.17  ? 497 TYR B C   1 
ATOM 1389 O O   . TYR A 1 497 ? 178.284 208.084 243.275 1.00 47.73  ? 497 TYR B O   1 
ATOM 1390 C CB  . TYR A 1 497 ? 175.105 208.908 243.893 1.00 42.84  ? 497 TYR B CB  1 
ATOM 1391 C CG  . TYR A 1 497 ? 173.948 209.547 244.634 1.00 44.30  ? 497 TYR B CG  1 
ATOM 1392 C CD1 . TYR A 1 497 ? 174.153 210.426 245.687 1.00 48.06  ? 497 TYR B CD1 1 
ATOM 1393 C CD2 . TYR A 1 497 ? 172.641 209.251 244.278 1.00 41.80  ? 497 TYR B CD2 1 
ATOM 1394 C CE1 . TYR A 1 497 ? 173.091 210.985 246.362 1.00 50.82  ? 497 TYR B CE1 1 
ATOM 1395 C CE2 . TYR A 1 497 ? 171.574 209.808 244.944 1.00 42.98  ? 497 TYR B CE2 1 
ATOM 1396 C CZ  . TYR A 1 497 ? 171.803 210.678 245.983 1.00 48.65  ? 497 TYR B CZ  1 
ATOM 1397 O OH  . TYR A 1 497 ? 170.737 211.238 246.645 1.00 50.89  ? 497 TYR B OH  1 
ATOM 1398 N N   . GLY A 1 498 ? 177.018 206.564 244.354 1.00 39.11  ? 498 GLY B N   1 
ATOM 1399 C CA  . GLY A 1 498 ? 177.689 205.431 243.759 1.00 39.31  ? 498 GLY B CA  1 
ATOM 1400 C C   . GLY A 1 498 ? 177.245 205.201 242.329 1.00 39.34  ? 498 GLY B C   1 
ATOM 1401 O O   . GLY A 1 498 ? 176.344 205.858 241.809 1.00 40.92  ? 498 GLY B O   1 
ATOM 1402 N N   . VAL A 1 499 ? 177.896 204.222 241.694 1.00 36.53  ? 499 VAL B N   1 
ATOM 1403 C CA  . VAL A 1 499 ? 177.729 203.979 240.262 1.00 35.73  ? 499 VAL B CA  1 
ATOM 1404 C C   . VAL A 1 499 ? 176.302 203.557 239.932 1.00 39.36  ? 499 VAL B C   1 
ATOM 1405 O O   . VAL A 1 499 ? 175.749 203.960 238.900 1.00 41.17  ? 499 VAL B O   1 
ATOM 1406 C CB  . VAL A 1 499 ? 178.764 202.931 239.801 1.00 35.90  ? 499 VAL B CB  1 
ATOM 1407 C CG1 . VAL A 1 499 ? 178.571 202.560 238.340 1.00 38.82  ? 499 VAL B CG1 1 
ATOM 1408 C CG2 . VAL A 1 499 ? 180.174 203.447 240.041 1.00 38.29  ? 499 VAL B CG2 1 
ATOM 1409 N N   . GLY A 1 500 ? 175.666 202.789 240.814 1.00 40.96  ? 500 GLY B N   1 
ATOM 1410 C CA  . GLY A 1 500 ? 174.310 202.337 240.570 1.00 41.44  ? 500 GLY B CA  1 
ATOM 1411 C C   . GLY A 1 500 ? 173.231 203.383 240.745 1.00 39.92  ? 500 GLY B C   1 
ATOM 1412 O O   . GLY A 1 500 ? 172.071 203.111 240.426 1.00 41.90  ? 500 GLY B O   1 
ATOM 1413 N N   . HIS A 1 501 ? 173.577 204.568 241.247 1.00 37.98  ? 501 HIS B N   1 
ATOM 1414 C CA  . HIS A 1 501 ? 172.606 205.631 241.475 1.00 39.84  ? 501 HIS B CA  1 
ATOM 1415 C C   . HIS A 1 501 ? 172.922 206.900 240.693 1.00 38.36  ? 501 HIS B C   1 
ATOM 1416 O O   . HIS A 1 501 ? 172.285 207.933 240.927 1.00 38.53  ? 501 HIS B O   1 
ATOM 1417 C CB  . HIS A 1 501 ? 172.517 205.941 242.970 1.00 40.48  ? 501 HIS B CB  1 
ATOM 1418 C CG  . HIS A 1 501 ? 171.978 204.810 243.789 1.00 39.38  ? 501 HIS B CG  1 
ATOM 1419 N ND1 . HIS A 1 501 ? 170.641 204.483 243.819 1.00 39.61  ? 501 HIS B ND1 1 
ATOM 1420 C CD2 . HIS A 1 501 ? 172.603 203.911 244.584 1.00 38.40  ? 501 HIS B CD2 1 
ATOM 1421 C CE1 . HIS A 1 501 ? 170.462 203.444 244.615 1.00 39.21  ? 501 HIS B CE1 1 
ATOM 1422 N NE2 . HIS A 1 501 ? 171.637 203.078 245.092 1.00 38.97  ? 501 HIS B NE2 1 
ATOM 1423 N N   . GLN A 1 502 ? 173.883 206.852 239.775 1.00 34.95  ? 502 GLN B N   1 
ATOM 1424 C CA  . GLN A 1 502 ? 174.317 207.911 238.881 1.00 36.33  ? 502 GLN B CA  1 
ATOM 1425 C C   . GLN A 1 502 ? 173.562 207.840 237.557 1.00 39.33  ? 502 GLN B C   1 
ATOM 1426 O O   . GLN A 1 502 ? 173.110 206.765 237.153 1.00 42.11  ? 502 GLN B O   1 
ATOM 1427 C CB  . GLN A 1 502 ? 175.827 207.808 238.630 1.00 40.47  ? 502 GLN B CB  1 
ATOM 1428 C CG  . GLN A 1 502 ? 176.672 208.316 239.786 1.00 41.32  ? 502 GLN B CG  1 
ATOM 1429 C CD  . GLN A 1 502 ? 178.160 208.227 239.513 1.00 41.27  ? 502 GLN B CD  1 
ATOM 1430 O OE1 . GLN A 1 502 ? 178.618 208.506 238.409 1.00 42.96  ? 502 GLN B OE1 1 
ATOM 1431 N NE2 . GLN A 1 502 ? 178.923 207.840 240.527 1.00 41.31  ? 502 GLN B NE2 1 
ATOM 1432 N N   . PRO A 1 503 ? 173.390 208.970 236.868 1.00 39.43  ? 503 PRO B N   1 
ATOM 1433 C CA  . PRO A 1 503 ? 172.628 208.957 235.613 1.00 39.23  ? 503 PRO B CA  1 
ATOM 1434 C C   . PRO A 1 503 ? 173.360 208.230 234.494 1.00 42.04  ? 503 PRO B C   1 
ATOM 1435 O O   . PRO A 1 503 ? 174.557 208.429 234.275 1.00 46.37  ? 503 PRO B O   1 
ATOM 1436 C CB  . PRO A 1 503 ? 172.464 210.446 235.285 1.00 44.21  ? 503 PRO B CB  1 
ATOM 1437 C CG  . PRO A 1 503 ? 172.675 211.152 236.563 1.00 47.13  ? 503 PRO B CG  1 
ATOM 1438 C CD  . PRO A 1 503 ? 173.676 210.344 237.315 1.00 44.08  ? 503 PRO B CD  1 
ATOM 1439 N N   . TYR A 1 504 ? 172.616 207.389 233.773 1.00 42.20  ? 504 TYR B N   1 
ATOM 1440 C CA  . TYR A 1 504 ? 173.115 206.681 232.596 1.00 45.33  ? 504 TYR B CA  1 
ATOM 1441 C C   . TYR A 1 504 ? 172.162 206.953 231.439 1.00 46.70  ? 504 TYR B C   1 
ATOM 1442 O O   . TYR A 1 504 ? 171.020 206.485 231.453 1.00 47.88  ? 504 TYR B O   1 
ATOM 1443 C CB  . TYR A 1 504 ? 173.230 205.176 232.850 1.00 42.91  ? 504 TYR B CB  1 
ATOM 1444 C CG  . TYR A 1 504 ? 174.532 204.723 233.475 1.00 43.52  ? 504 TYR B CG  1 
ATOM 1445 C CD1 . TYR A 1 504 ? 175.007 205.299 234.644 1.00 42.67  ? 504 TYR B CD1 1 
ATOM 1446 C CD2 . TYR A 1 504 ? 175.284 203.714 232.892 1.00 46.65  ? 504 TYR B CD2 1 
ATOM 1447 C CE1 . TYR A 1 504 ? 176.193 204.885 235.214 1.00 41.89  ? 504 TYR B CE1 1 
ATOM 1448 C CE2 . TYR A 1 504 ? 176.470 203.295 233.455 1.00 46.96  ? 504 TYR B CE2 1 
ATOM 1449 C CZ  . TYR A 1 504 ? 176.919 203.883 234.615 1.00 45.60  ? 504 TYR B CZ  1 
ATOM 1450 O OH  . TYR A 1 504 ? 178.103 203.466 235.175 1.00 50.91  ? 504 TYR B OH  1 
ATOM 1451 N N   . ARG A 1 505 ? 172.627 207.700 230.440 1.00 45.47  ? 505 ARG B N   1 
ATOM 1452 C CA  . ARG A 1 505 ? 171.801 208.041 229.288 1.00 43.76  ? 505 ARG B CA  1 
ATOM 1453 C C   . ARG A 1 505 ? 171.626 206.811 228.406 1.00 46.25  ? 505 ARG B C   1 
ATOM 1454 O O   . ARG A 1 505 ? 172.614 206.205 227.983 1.00 52.25  ? 505 ARG B O   1 
ATOM 1455 C CB  . ARG A 1 505 ? 172.440 209.180 228.499 1.00 47.32  ? 505 ARG B CB  1 
ATOM 1456 C CG  . ARG A 1 505 ? 172.621 210.459 229.291 1.00 51.86  ? 505 ARG B CG  1 
ATOM 1457 C CD  . ARG A 1 505 ? 173.125 211.584 228.404 1.00 55.52  ? 505 ARG B CD  1 
ATOM 1458 N NE  . ARG A 1 505 ? 173.034 212.886 229.051 1.00 57.71  ? 505 ARG B NE  1 
ATOM 1459 C CZ  . ARG A 1 505 ? 172.837 214.027 228.406 1.00 56.79  ? 505 ARG B CZ  1 
ATOM 1460 N NH1 . ARG A 1 505 ? 172.697 214.061 227.091 1.00 53.67  ? 505 ARG B NH1 1 
ATOM 1461 N NH2 . ARG A 1 505 ? 172.778 215.161 229.097 1.00 60.68  ? 505 ARG B NH2 1 
ATOM 1462 N N   . VAL A 1 506 ? 170.379 206.452 228.116 1.00 42.84  ? 506 VAL B N   1 
ATOM 1463 C CA  . VAL A 1 506 ? 170.057 205.230 227.386 1.00 45.66  ? 506 VAL B CA  1 
ATOM 1464 C C   . VAL A 1 506 ? 169.411 205.618 226.062 1.00 45.99  ? 506 VAL B C   1 
ATOM 1465 O O   . VAL A 1 506 ? 168.429 206.371 226.038 1.00 49.10  ? 506 VAL B O   1 
ATOM 1466 C CB  . VAL A 1 506 ? 169.138 204.310 228.208 1.00 47.66  ? 506 VAL B CB  1 
ATOM 1467 C CG1 . VAL A 1 506 ? 168.401 203.324 227.309 1.00 50.13  ? 506 VAL B CG1 1 
ATOM 1468 C CG2 . VAL A 1 506 ? 169.939 203.577 229.273 1.00 48.60  ? 506 VAL B CG2 1 
ATOM 1469 N N   . VAL A 1 507 ? 169.972 205.119 224.961 1.00 46.49  ? 507 VAL B N   1 
ATOM 1470 C CA  . VAL A 1 507 ? 169.430 205.319 223.620 1.00 46.71  ? 507 VAL B CA  1 
ATOM 1471 C C   . VAL A 1 507 ? 169.222 203.953 222.981 1.00 47.66  ? 507 VAL B C   1 
ATOM 1472 O O   . VAL A 1 507 ? 170.133 203.118 222.978 1.00 52.45  ? 507 VAL B O   1 
ATOM 1473 C CB  . VAL A 1 507 ? 170.352 206.199 222.757 1.00 51.18  ? 507 VAL B CB  1 
ATOM 1474 C CG1 . VAL A 1 507 ? 169.819 206.302 221.339 1.00 53.57  ? 507 VAL B CG1 1 
ATOM 1475 C CG2 . VAL A 1 507 ? 170.473 207.585 223.362 1.00 52.82  ? 507 VAL B CG2 1 
ATOM 1476 N N   . VAL A 1 508 ? 168.023 203.727 222.445 1.00 48.76  ? 508 VAL B N   1 
ATOM 1477 C CA  . VAL A 1 508 ? 167.624 202.442 221.885 1.00 53.93  ? 508 VAL B CA  1 
ATOM 1478 C C   . VAL A 1 508 ? 167.188 202.653 220.441 1.00 60.12  ? 508 VAL B C   1 
ATOM 1479 O O   . VAL A 1 508 ? 166.377 203.541 220.155 1.00 63.12  ? 508 VAL B O   1 
ATOM 1480 C CB  . VAL A 1 508 ? 166.491 201.797 222.707 1.00 55.89  ? 508 VAL B CB  1 
ATOM 1481 C CG1 . VAL A 1 508 ? 166.011 200.510 222.054 1.00 60.00  ? 508 VAL B CG1 1 
ATOM 1482 C CG2 . VAL A 1 508 ? 166.946 201.538 224.133 1.00 57.10  ? 508 VAL B CG2 1 
ATOM 1483 N N   . LEU A 1 509 ? 167.729 201.842 219.536 1.00 61.37  ? 509 LEU B N   1 
ATOM 1484 C CA  . LEU A 1 509 ? 167.311 201.817 218.144 1.00 59.84  ? 509 LEU B CA  1 
ATOM 1485 C C   . LEU A 1 509 ? 166.399 200.619 217.906 1.00 64.33  ? 509 LEU B C   1 
ATOM 1486 O O   . LEU A 1 509 ? 166.510 199.593 218.581 1.00 71.62  ? 509 LEU B O   1 
ATOM 1487 C CB  . LEU A 1 509 ? 168.523 201.758 217.214 1.00 60.27  ? 509 LEU B CB  1 
ATOM 1488 C CG  . LEU A 1 509 ? 169.440 202.981 217.269 1.00 56.50  ? 509 LEU B CG  1 
ATOM 1489 C CD1 . LEU A 1 509 ? 170.830 202.642 216.762 1.00 54.43  ? 509 LEU B CD1 1 
ATOM 1490 C CD2 . LEU A 1 509 ? 168.843 204.133 216.476 1.00 65.51  ? 509 LEU B CD2 1 
ATOM 1491 N N   . SER A 1 510 ? 165.474 200.765 216.954 1.00 64.98  ? 510 SER B N   1 
ATOM 1492 C CA  . SER A 1 510 ? 164.411 199.781 216.728 1.00 72.64  ? 510 SER B CA  1 
ATOM 1493 C C   . SER A 1 510 ? 164.255 199.497 215.230 1.00 75.97  ? 510 SER B C   1 
ATOM 1494 O O   . SER A 1 510 ? 163.180 199.692 214.664 1.00 78.77  ? 510 SER B O   1 
ATOM 1495 C CB  . SER A 1 510 ? 163.082 200.231 217.329 1.00 75.64  ? 510 SER B CB  1 
ATOM 1496 O OG  . SER A 1 510 ? 162.384 201.076 216.438 1.00 80.77  ? 510 SER B OG  1 
ATOM 1497 N N   . PHE A 1 511 ? 165.365 199.124 214.584 1.00 74.43  ? 511 PHE B N   1 
ATOM 1498 C CA  . PHE A 1 511 ? 165.444 198.718 213.179 1.00 77.12  ? 511 PHE B CA  1 
ATOM 1499 C C   . PHE A 1 511 ? 164.297 197.801 212.763 1.00 83.08  ? 511 PHE B C   1 
ATOM 1500 O O   . PHE A 1 511 ? 164.037 196.781 213.409 1.00 85.05  ? 511 PHE B O   1 
ATOM 1501 C CB  . PHE A 1 511 ? 166.776 198.003 212.943 1.00 78.26  ? 511 PHE B CB  1 
ATOM 1502 C CG  . PHE A 1 511 ? 167.978 198.882 213.105 1.00 74.53  ? 511 PHE B CG  1 
ATOM 1503 C CD1 . PHE A 1 511 ? 168.378 199.725 212.086 1.00 74.81  ? 511 PHE B CD1 1 
ATOM 1504 C CD2 . PHE A 1 511 ? 168.706 198.865 214.282 1.00 71.34  ? 511 PHE B CD2 1 
ATOM 1505 C CE1 . PHE A 1 511 ? 169.485 200.533 212.238 1.00 75.13  ? 511 PHE B CE1 1 
ATOM 1506 C CE2 . PHE A 1 511 ? 169.811 199.671 214.440 1.00 71.11  ? 511 PHE B CE2 1 
ATOM 1507 C CZ  . PHE A 1 511 ? 170.202 200.507 213.416 1.00 74.85  ? 511 PHE B CZ  1 
ATOM 1508 N N   . GLU A 1 512 ? 163.609 198.164 211.679 1.00 84.47  ? 512 GLU B N   1 
ATOM 1509 C CA  . GLU A 1 512 ? 162.434 197.441 211.206 1.00 85.78  ? 512 GLU B CA  1 
ATOM 1510 C C   . GLU A 1 512 ? 162.488 197.279 209.689 1.00 90.27  ? 512 GLU B C   1 
ATOM 1511 O O   . GLU A 1 512 ? 163.268 197.938 208.994 1.00 90.95  ? 512 GLU B O   1 
ATOM 1512 C CB  . GLU A 1 512 ? 161.139 198.159 211.612 1.00 87.32  ? 512 GLU B CB  1 
ATOM 1513 C CG  . GLU A 1 512 ? 160.803 198.076 213.089 1.00 90.62  ? 512 GLU B CG  1 
ATOM 1514 C CD  . GLU A 1 512 ? 159.978 199.257 213.562 1.00 92.46  ? 512 GLU B CD  1 
ATOM 1515 O OE1 . GLU A 1 512 ? 159.661 200.133 212.729 1.00 93.90  ? 512 GLU B OE1 1 
ATOM 1516 O OE2 . GLU A 1 512 ? 159.647 199.311 214.765 1.00 89.26  ? 512 GLU B OE2 1 
ATOM 1517 N N   . LEU A 1 513 ? 161.635 196.390 209.178 1.00 92.63  ? 513 LEU B N   1 
ATOM 1518 C CA  . LEU A 1 513 ? 161.451 196.197 207.743 1.00 90.18  ? 513 LEU B CA  1 
ATOM 1519 C C   . LEU A 1 513 ? 160.002 195.786 207.511 1.00 86.06  ? 513 LEU B C   1 
ATOM 1520 O O   . LEU A 1 513 ? 159.493 194.897 208.200 1.00 85.88  ? 513 LEU B O   1 
ATOM 1521 C CB  . LEU A 1 513 ? 162.438 195.157 207.176 1.00 90.03  ? 513 LEU B CB  1 
ATOM 1522 C CG  . LEU A 1 513 ? 162.347 193.645 207.424 1.00 90.34  ? 513 LEU B CG  1 
ATOM 1523 C CD1 . LEU A 1 513 ? 163.224 192.899 206.430 1.00 86.05  ? 513 LEU B CD1 1 
ATOM 1524 C CD2 . LEU A 1 513 ? 162.739 193.274 208.849 1.00 87.94  ? 513 LEU B CD2 1 
ATOM 1525 N N   . LEU A 1 514 ? 159.333 196.452 206.576 1.00 86.13  ? 514 LEU B N   1 
ATOM 1526 C CA  . LEU A 1 514 ? 157.875 196.358 206.464 1.00 89.91  ? 514 LEU B CA  1 
ATOM 1527 C C   . LEU A 1 514 ? 157.466 196.481 204.997 1.00 86.69  ? 514 LEU B C   1 
ATOM 1528 O O   . LEU A 1 514 ? 158.274 196.254 204.090 1.00 84.14  ? 514 LEU B O   1 
ATOM 1529 C CB  . LEU A 1 514 ? 157.181 197.420 207.338 1.00 93.32  ? 514 LEU B CB  1 
ATOM 1530 C CG  . LEU A 1 514 ? 157.272 197.379 208.865 1.00 93.59  ? 514 LEU B CG  1 
ATOM 1531 C CD1 . LEU A 1 514 ? 156.622 198.612 209.472 1.00 90.47  ? 514 LEU B CD1 1 
ATOM 1532 C CD2 . LEU A 1 514 ? 156.624 196.112 209.402 1.00 90.70  ? 514 LEU B CD2 1 
ATOM 1533 N N   . HIS A 1 515 ? 156.188 196.816 204.782 1.00 85.54  ? 515 HIS B N   1 
ATOM 1534 C CA  . HIS A 1 515 ? 155.594 196.890 203.448 1.00 84.13  ? 515 HIS B CA  1 
ATOM 1535 C C   . HIS A 1 515 ? 156.276 197.937 202.575 1.00 83.23  ? 515 HIS B C   1 
ATOM 1536 O O   . HIS A 1 515 ? 156.459 197.731 201.369 1.00 83.41  ? 515 HIS B O   1 
ATOM 1537 C CB  . HIS A 1 515 ? 154.098 197.190 203.581 1.00 86.40  ? 515 HIS B CB  1 
ATOM 1538 C CG  . HIS A 1 515 ? 153.368 197.266 202.275 1.00 83.84  ? 515 HIS B CG  1 
ATOM 1539 N ND1 . HIS A 1 515 ? 153.064 196.152 201.523 1.00 85.19  ? 515 HIS B ND1 1 
ATOM 1540 C CD2 . HIS A 1 515 ? 152.860 198.325 201.600 1.00 75.56  ? 515 HIS B CD2 1 
ATOM 1541 C CE1 . HIS A 1 515 ? 152.412 196.522 200.436 1.00 77.84  ? 515 HIS B CE1 1 
ATOM 1542 N NE2 . HIS A 1 515 ? 152.274 197.835 200.458 1.00 70.15  ? 515 HIS B NE2 1 
ATOM 1543 N N   . ALA A 1 516 ? 156.623 199.079 203.161 1.00 84.68  ? 516 ALA B N   1 
ATOM 1544 C CA  . ALA A 1 516 ? 157.371 200.094 202.434 1.00 85.61  ? 516 ALA B CA  1 
ATOM 1545 C C   . ALA A 1 516 ? 158.746 199.547 202.054 1.00 85.83  ? 516 ALA B C   1 
ATOM 1546 O O   . ALA A 1 516 ? 159.349 198.797 202.832 1.00 88.18  ? 516 ALA B O   1 
ATOM 1547 C CB  . ALA A 1 516 ? 157.516 201.359 203.282 1.00 86.82  ? 516 ALA B CB  1 
ATOM 1548 N N   . PRO A 1 517 ? 159.256 199.870 200.863 1.00 77.64  ? 517 PRO B N   1 
ATOM 1549 C CA  . PRO A 1 517 ? 160.524 199.278 200.420 1.00 77.61  ? 517 PRO B CA  1 
ATOM 1550 C C   . PRO A 1 517 ? 161.701 199.767 201.252 1.00 82.57  ? 517 PRO B C   1 
ATOM 1551 O O   . PRO A 1 517 ? 161.675 200.864 201.814 1.00 87.20  ? 517 PRO B O   1 
ATOM 1552 C CB  . PRO A 1 517 ? 160.634 199.734 198.962 1.00 76.69  ? 517 PRO B CB  1 
ATOM 1553 C CG  . PRO A 1 517 ? 159.862 201.001 198.913 1.00 73.88  ? 517 PRO B CG  1 
ATOM 1554 C CD  . PRO A 1 517 ? 158.724 200.833 199.882 1.00 71.25  ? 517 PRO B CD  1 
ATOM 1555 N N   . ALA A 1 518 ? 162.731 198.923 201.340 1.00 82.71  ? 518 ALA B N   1 
ATOM 1556 C CA  . ALA A 1 518 ? 163.936 199.237 202.100 1.00 89.24  ? 518 ALA B CA  1 
ATOM 1557 C C   . ALA A 1 518 ? 164.664 200.428 201.492 1.00 91.28  ? 518 ALA B C   1 
ATOM 1558 O O   . ALA A 1 518 ? 165.239 200.325 200.404 1.00 90.91  ? 518 ALA B O   1 
ATOM 1559 C CB  . ALA A 1 518 ? 164.861 198.020 202.164 1.00 89.68  ? 518 ALA B CB  1 
ATOM 1560 N N   . THR A 1 519 ? 164.646 201.561 202.193 1.00 93.19  ? 519 THR B N   1 
ATOM 1561 C CA  . THR A 1 519 ? 165.173 202.814 201.669 1.00 97.29  ? 519 THR B CA  1 
ATOM 1562 C C   . THR A 1 519 ? 166.492 203.205 202.321 1.00 102.03 ? 519 THR B C   1 
ATOM 1563 O O   . THR A 1 519 ? 167.468 203.489 201.620 1.00 107.53 ? 519 THR B O   1 
ATOM 1564 C CB  . THR A 1 519 ? 164.139 203.933 201.851 1.00 97.25  ? 519 THR B CB  1 
ATOM 1565 O OG1 . THR A 1 519 ? 162.835 203.440 201.522 1.00 95.24  ? 519 THR B OG1 1 
ATOM 1566 C CG2 . THR A 1 519 ? 164.471 205.113 200.950 1.00 97.82  ? 519 THR B CG2 1 
ATOM 1567 N N   . VAL A 1 520 ? 166.550 203.231 203.652 1.00 98.68  ? 520 VAL B N   1 
ATOM 1568 C CA  . VAL A 1 520 ? 167.762 203.665 204.337 1.00 97.95  ? 520 VAL B CA  1 
ATOM 1569 C C   . VAL A 1 520 ? 168.808 202.555 204.284 1.00 99.66  ? 520 VAL B C   1 
ATOM 1570 O O   . VAL A 1 520 ? 168.526 201.386 204.580 1.00 100.88 ? 520 VAL B O   1 
ATOM 1571 C CB  . VAL A 1 520 ? 167.437 204.119 205.771 1.00 94.31  ? 520 VAL B CB  1 
ATOM 1572 C CG1 . VAL A 1 520 ? 166.505 205.315 205.729 1.00 92.00  ? 520 VAL B CG1 1 
ATOM 1573 C CG2 . VAL A 1 520 ? 166.765 203.019 206.586 1.00 92.50  ? 520 VAL B CG2 1 
ATOM 1574 N N   . CYS A 1 521 ? 170.015 202.908 203.845 1.00 98.27  ? 521 CYS B N   1 
ATOM 1575 C CA  . CYS A 1 521 ? 171.098 201.947 203.669 1.00 100.73 ? 521 CYS B CA  1 
ATOM 1576 C C   . CYS A 1 521 ? 172.411 202.621 204.059 1.00 104.07 ? 521 CYS B C   1 
ATOM 1577 O O   . CYS A 1 521 ? 172.425 203.717 204.628 1.00 102.16 ? 521 CYS B O   1 
ATOM 1578 C CB  . CYS A 1 521 ? 171.129 201.408 202.232 1.00 104.18 ? 521 CYS B CB  1 
ATOM 1579 S SG  . CYS A 1 521 ? 169.679 200.436 201.733 1.00 114.59 ? 521 CYS B SG  1 
ATOM 1580 N N   . GLY A 1 522 ? 173.524 201.957 203.751 1.00 107.25 ? 522 GLY B N   1 
ATOM 1581 C CA  . GLY A 1 522 ? 174.833 202.443 204.117 1.00 104.66 ? 522 GLY B CA  1 
ATOM 1582 C C   . GLY A 1 522 ? 175.708 202.748 202.917 1.00 105.03 ? 522 GLY B C   1 
ATOM 1583 O O   . GLY A 1 522 ? 175.488 202.241 201.813 1.00 107.09 ? 522 GLY B O   1 
ATOM 1584 N N   . PRO A 1 523 ? 176.722 203.588 203.113 1.00 104.86 ? 523 PRO B N   1 
ATOM 1585 C CA  . PRO A 1 523 ? 177.595 203.967 202.000 1.00 107.48 ? 523 PRO B CA  1 
ATOM 1586 C C   . PRO A 1 523 ? 178.554 202.855 201.608 1.00 109.28 ? 523 PRO B C   1 
ATOM 1587 O O   . PRO A 1 523 ? 178.889 201.971 202.400 1.00 107.63 ? 523 PRO B O   1 
ATOM 1588 C CB  . PRO A 1 523 ? 178.351 205.178 202.557 1.00 104.37 ? 523 PRO B CB  1 
ATOM 1589 C CG  . PRO A 1 523 ? 178.467 204.874 204.011 1.00 105.19 ? 523 PRO B CG  1 
ATOM 1590 C CD  . PRO A 1 523 ? 177.177 204.172 204.388 1.00 102.38 ? 523 PRO B CD  1 
ATOM 1591 N N   . LYS A 1 524 ? 178.995 202.914 200.353 1.00 109.45 ? 524 LYS B N   1 
ATOM 1592 C CA  . LYS A 1 524 ? 179.924 201.951 199.781 1.00 106.86 ? 524 LYS B CA  1 
ATOM 1593 C C   . LYS A 1 524 ? 180.996 202.721 199.014 1.00 105.82 ? 524 LYS B C   1 
ATOM 1594 O O   . LYS A 1 524 ? 180.984 203.955 198.964 1.00 106.80 ? 524 LYS B O   1 
ATOM 1595 C CB  . LYS A 1 524 ? 179.179 200.949 198.885 1.00 106.38 ? 524 LYS B CB  1 
ATOM 1596 C CG  . LYS A 1 524 ? 179.813 199.563 198.778 1.00 107.40 ? 524 LYS B CG  1 
ATOM 1597 C CD  . LYS A 1 524 ? 180.012 198.936 200.149 1.00 108.30 ? 524 LYS B CD  1 
ATOM 1598 C CE  . LYS A 1 524 ? 180.660 197.565 200.038 1.00 104.92 ? 524 LYS B CE  1 
ATOM 1599 N NZ  . LYS A 1 524 ? 180.873 196.938 201.372 1.00 104.70 ? 524 LYS B NZ  1 
ATOM 1600 N N   . LYS A 1 525 ? 181.937 201.992 198.420 1.00 101.95 ? 525 LYS B N   1 
ATOM 1601 C CA  . LYS A 1 525 ? 183.006 202.603 197.637 1.00 96.54  ? 525 LYS B CA  1 
ATOM 1602 C C   . LYS A 1 525 ? 182.468 203.196 196.338 1.00 86.48  ? 525 LYS B C   1 
ATOM 1603 O O   . LYS A 1 525 ? 182.379 204.414 196.191 1.00 80.08  ? 525 LYS B O   1 
ATOM 1604 C CB  . LYS A 1 525 ? 184.098 201.577 197.330 1.00 100.36 ? 525 LYS B CB  1 
ATOM 1605 C CG  . LYS A 1 525 ? 184.410 200.639 198.482 1.00 103.80 ? 525 LYS B CG  1 
ATOM 1606 C CD  . LYS A 1 525 ? 185.439 199.597 198.079 1.00 104.83 ? 525 LYS B CD  1 
ATOM 1607 C CE  . LYS A 1 525 ? 185.744 198.648 199.226 1.00 111.51 ? 525 LYS B CE  1 
ATOM 1608 N NZ  . LYS A 1 525 ? 184.517 197.963 199.718 1.00 112.85 ? 525 LYS B NZ  1 
ATOM 1609 N N   . ILE B 1 323 ? 182.254 133.112 182.999 1.00 89.60  ? 323 ILE A N   1 
ATOM 1610 C CA  . ILE B 1 323 ? 183.153 132.634 184.041 1.00 89.12  ? 323 ILE A CA  1 
ATOM 1611 C C   . ILE B 1 323 ? 183.766 133.809 184.799 1.00 83.17  ? 323 ILE A C   1 
ATOM 1612 O O   . ILE B 1 323 ? 183.938 134.898 184.248 1.00 85.53  ? 323 ILE A O   1 
ATOM 1613 C CB  . ILE B 1 323 ? 184.245 131.716 183.453 1.00 89.66  ? 323 ILE A CB  1 
ATOM 1614 C CG1 . ILE B 1 323 ? 185.111 132.477 182.445 1.00 83.93  ? 323 ILE A CG1 1 
ATOM 1615 C CG2 . ILE B 1 323 ? 183.618 130.491 182.804 1.00 81.28  ? 323 ILE A CG2 1 
ATOM 1616 C CD1 . ILE B 1 323 ? 186.340 131.717 181.998 1.00 73.89  ? 323 ILE A CD1 1 
ATOM 1617 N N   . VAL B 1 324 ? 184.074 133.589 186.076 1.00 70.29  ? 324 VAL A N   1 
ATOM 1618 C CA  . VAL B 1 324 ? 184.654 134.608 186.943 1.00 58.44  ? 324 VAL A CA  1 
ATOM 1619 C C   . VAL B 1 324 ? 185.943 134.048 187.529 1.00 48.35  ? 324 VAL A C   1 
ATOM 1620 O O   . VAL B 1 324 ? 185.933 132.970 188.135 1.00 48.51  ? 324 VAL A O   1 
ATOM 1621 C CB  . VAL B 1 324 ? 183.688 135.028 188.064 1.00 58.69  ? 324 VAL A CB  1 
ATOM 1622 C CG1 . VAL B 1 324 ? 184.357 136.023 189.000 1.00 61.85  ? 324 VAL A CG1 1 
ATOM 1623 C CG2 . VAL B 1 324 ? 182.409 135.613 187.483 1.00 49.62  ? 324 VAL A CG2 1 
ATOM 1624 N N   . ARG B 1 325 ? 187.048 134.770 187.346 1.00 42.63  ? 325 ARG A N   1 
ATOM 1625 C CA  . ARG B 1 325 ? 188.342 134.380 187.894 1.00 45.85  ? 325 ARG A CA  1 
ATOM 1626 C C   . ARG B 1 325 ? 188.897 135.516 188.741 1.00 56.79  ? 325 ARG A C   1 
ATOM 1627 O O   . ARG B 1 325 ? 189.144 136.614 188.230 1.00 65.18  ? 325 ARG A O   1 
ATOM 1628 C CB  . ARG B 1 325 ? 189.333 134.008 186.789 1.00 39.97  ? 325 ARG A CB  1 
ATOM 1629 C CG  . ARG B 1 325 ? 188.810 133.001 185.783 1.00 41.56  ? 325 ARG A CG  1 
ATOM 1630 C CD  . ARG B 1 325 ? 188.787 131.607 186.379 1.00 35.97  ? 325 ARG A CD  1 
ATOM 1631 N NE  . ARG B 1 325 ? 190.110 130.999 186.424 1.00 23.06  ? 325 ARG A NE  1 
ATOM 1632 C CZ  . ARG B 1 325 ? 190.347 129.753 186.806 1.00 18.83  ? 325 ARG A CZ  1 
ATOM 1633 N NH1 . ARG B 1 325 ? 189.369 128.951 187.191 1.00 12.81  ? 325 ARG A NH1 1 
ATOM 1634 N NH2 . ARG B 1 325 ? 191.597 129.300 186.804 1.00 23.54  ? 325 ARG A NH2 1 
ATOM 1635 N N   . PHE B 1 326 ? 189.117 135.235 190.021 1.00 61.40  ? 326 PHE A N   1 
ATOM 1636 C CA  . PHE B 1 326 ? 189.665 136.115 191.040 1.00 57.32  ? 326 PHE A CA  1 
ATOM 1637 C C   . PHE B 1 326 ? 190.885 135.438 191.651 1.00 63.17  ? 326 PHE A C   1 
ATOM 1638 O O   . PHE B 1 326 ? 190.929 134.205 191.721 1.00 74.22  ? 326 PHE A O   1 
ATOM 1639 C CB  . PHE B 1 326 ? 188.606 136.405 192.120 1.00 53.50  ? 326 PHE A CB  1 
ATOM 1640 C CG  . PHE B 1 326 ? 187.658 137.529 191.776 1.00 56.88  ? 326 PHE A CG  1 
ATOM 1641 C CD1 . PHE B 1 326 ? 187.697 138.146 190.540 1.00 61.67  ? 326 PHE A CD1 1 
ATOM 1642 C CD2 . PHE B 1 326 ? 186.723 137.964 192.701 1.00 62.04  ? 326 PHE A CD2 1 
ATOM 1643 C CE1 . PHE B 1 326 ? 186.825 139.175 190.231 1.00 64.09  ? 326 PHE A CE1 1 
ATOM 1644 C CE2 . PHE B 1 326 ? 185.848 138.993 192.400 1.00 61.79  ? 326 PHE A CE2 1 
ATOM 1645 C CZ  . PHE B 1 326 ? 185.900 139.598 191.164 1.00 61.73  ? 326 PHE A CZ  1 
ATOM 1646 N N   . PRO B 1 327 ? 191.887 136.195 192.101 1.00 58.86  ? 327 PRO A N   1 
ATOM 1647 C CA  . PRO B 1 327 ? 193.179 135.587 192.437 1.00 69.18  ? 327 PRO A CA  1 
ATOM 1648 C C   . PRO B 1 327 ? 193.170 134.943 193.822 1.00 69.30  ? 327 PRO A C   1 
ATOM 1649 O O   . PRO B 1 327 ? 192.171 134.944 194.537 1.00 67.05  ? 327 PRO A O   1 
ATOM 1650 C CB  . PRO B 1 327 ? 194.153 136.769 192.372 1.00 66.90  ? 327 PRO A CB  1 
ATOM 1651 C CG  . PRO B 1 327 ? 193.301 138.017 192.378 1.00 62.26  ? 327 PRO A CG  1 
ATOM 1652 C CD  . PRO B 1 327 ? 191.868 137.613 192.497 1.00 54.21  ? 327 PRO A CD  1 
ATOM 1653 N N   . ASN B 1 328 ? 194.320 134.370 194.178 1.00 70.93  ? 328 ASN A N   1 
ATOM 1654 C CA  . ASN B 1 328 ? 194.483 133.724 195.473 1.00 71.41  ? 328 ASN A CA  1 
ATOM 1655 C C   . ASN B 1 328 ? 194.503 134.758 196.593 1.00 78.57  ? 328 ASN A C   1 
ATOM 1656 O O   . ASN B 1 328 ? 195.089 135.835 196.457 1.00 79.30  ? 328 ASN A O   1 
ATOM 1657 C CB  . ASN B 1 328 ? 195.773 132.904 195.499 1.00 68.70  ? 328 ASN A CB  1 
ATOM 1658 C CG  . ASN B 1 328 ? 195.895 131.972 194.312 1.00 69.02  ? 328 ASN A CG  1 
ATOM 1659 O OD1 . ASN B 1 328 ? 196.086 132.411 193.179 1.00 67.76  ? 328 ASN A OD1 1 
ATOM 1660 N ND2 . ASN B 1 328 ? 195.789 130.673 194.568 1.00 72.11  ? 328 ASN A ND2 1 
ATOM 1661 N N   . VAL B 1 329 ? 193.852 134.421 197.708 1.00 76.35  ? 329 VAL A N   1 
ATOM 1662 C CA  . VAL B 1 329 ? 193.692 135.326 198.838 1.00 75.68  ? 329 VAL A CA  1 
ATOM 1663 C C   . VAL B 1 329 ? 193.901 134.557 200.135 1.00 83.46  ? 329 VAL A C   1 
ATOM 1664 O O   . VAL B 1 329 ? 193.763 133.334 200.189 1.00 79.20  ? 329 VAL A O   1 
ATOM 1665 C CB  . VAL B 1 329 ? 192.307 136.000 198.839 1.00 74.12  ? 329 VAL A CB  1 
ATOM 1666 C CG1 . VAL B 1 329 ? 192.241 137.090 197.779 1.00 72.03  ? 329 VAL A CG1 1 
ATOM 1667 C CG2 . VAL B 1 329 ? 191.232 134.953 198.597 1.00 72.12  ? 329 VAL A CG2 1 
ATOM 1668 N N   . THR B 1 330 ? 194.239 135.297 201.194 1.00 92.75  ? 330 THR A N   1 
ATOM 1669 C CA  . THR B 1 330 ? 194.569 134.701 202.484 1.00 94.69  ? 330 THR A CA  1 
ATOM 1670 C C   . THR B 1 330 ? 193.603 135.092 203.597 1.00 81.57  ? 330 THR A C   1 
ATOM 1671 O O   . THR B 1 330 ? 192.984 134.216 204.207 1.00 79.18  ? 330 THR A O   1 
ATOM 1672 C CB  . THR B 1 330 ? 196.005 135.078 202.879 1.00 96.45  ? 330 THR A CB  1 
ATOM 1673 O OG1 . THR B 1 330 ? 196.111 136.502 203.002 1.00 91.92  ? 330 THR A OG1 1 
ATOM 1674 C CG2 . THR B 1 330 ? 196.998 134.584 201.835 1.00 86.56  ? 330 THR A CG2 1 
ATOM 1675 N N   . ASN B 1 331 ? 193.445 136.382 203.879 1.00 74.47  ? 331 ASN A N   1 
ATOM 1676 C CA  . ASN B 1 331 ? 192.793 136.834 205.104 1.00 77.14  ? 331 ASN A CA  1 
ATOM 1677 C C   . ASN B 1 331 ? 191.548 137.663 204.793 1.00 75.65  ? 331 ASN A C   1 
ATOM 1678 O O   . ASN B 1 331 ? 191.207 137.909 203.636 1.00 74.88  ? 331 ASN A O   1 
ATOM 1679 C CB  . ASN B 1 331 ? 193.779 137.611 205.982 1.00 81.10  ? 331 ASN A CB  1 
ATOM 1680 C CG  . ASN B 1 331 ? 194.223 138.912 205.352 1.00 80.98  ? 331 ASN A CG  1 
ATOM 1681 O OD1 . ASN B 1 331 ? 194.773 138.921 204.250 1.00 82.79  ? 331 ASN A OD1 1 
ATOM 1682 N ND2 . ASN B 1 331 ? 193.989 140.021 206.045 1.00 74.98  ? 331 ASN A ND2 1 
ATOM 1683 N N   . LEU B 1 332 ? 190.881 138.107 205.863 1.00 75.77  ? 332 LEU A N   1 
ATOM 1684 C CA  . LEU B 1 332 ? 189.514 138.615 205.815 1.00 72.81  ? 332 LEU A CA  1 
ATOM 1685 C C   . LEU B 1 332 ? 189.421 140.116 206.086 1.00 70.42  ? 332 LEU A C   1 
ATOM 1686 O O   . LEU B 1 332 ? 188.328 140.608 206.388 1.00 68.31  ? 332 LEU A O   1 
ATOM 1687 C CB  . LEU B 1 332 ? 188.636 137.858 206.817 1.00 69.48  ? 332 LEU A CB  1 
ATOM 1688 C CG  . LEU B 1 332 ? 187.990 136.502 206.497 1.00 69.50  ? 332 LEU A CG  1 
ATOM 1689 C CD1 . LEU B 1 332 ? 186.981 136.623 205.368 1.00 70.23  ? 332 LEU A CD1 1 
ATOM 1690 C CD2 . LEU B 1 332 ? 189.018 135.412 206.194 1.00 68.87  ? 332 LEU A CD2 1 
ATOM 1691 N N   . CYS B 1 333 ? 190.553 140.842 206.008 1.00 70.53  ? 333 CYS A N   1 
ATOM 1692 C CA  . CYS B 1 333 ? 190.739 142.287 206.200 1.00 66.97  ? 333 CYS A CA  1 
ATOM 1693 C C   . CYS B 1 333 ? 190.500 142.720 207.646 1.00 59.76  ? 333 CYS A C   1 
ATOM 1694 O O   . CYS B 1 333 ? 189.563 142.244 208.297 1.00 58.77  ? 333 CYS A O   1 
ATOM 1695 C CB  . CYS B 1 333 ? 189.838 143.094 205.260 1.00 64.76  ? 333 CYS A CB  1 
ATOM 1696 S SG  . CYS B 1 333 ? 190.215 142.916 203.502 1.00 78.51  ? 333 CYS A SG  1 
ATOM 1697 N N   . PRO B 1 334 ? 191.311 143.665 208.180 1.00 59.28  ? 334 PRO A N   1 
ATOM 1698 C CA  . PRO B 1 334 ? 191.238 144.038 209.601 1.00 63.29  ? 334 PRO A CA  1 
ATOM 1699 C C   . PRO B 1 334 ? 190.131 145.044 209.930 1.00 64.04  ? 334 PRO A C   1 
ATOM 1700 O O   . PRO B 1 334 ? 190.356 146.046 210.609 1.00 69.42  ? 334 PRO A O   1 
ATOM 1701 C CB  . PRO B 1 334 ? 192.627 144.633 209.864 1.00 67.34  ? 334 PRO A CB  1 
ATOM 1702 C CG  . PRO B 1 334 ? 193.439 144.398 208.583 1.00 61.05  ? 334 PRO A CG  1 
ATOM 1703 C CD  . PRO B 1 334 ? 192.421 144.358 207.508 1.00 60.79  ? 334 PRO A CD  1 
ATOM 1704 N N   . PHE B 1 335 ? 188.921 144.769 209.449 1.00 58.46  ? 335 PHE A N   1 
ATOM 1705 C CA  . PHE B 1 335 ? 187.796 145.666 209.680 1.00 54.08  ? 335 PHE A CA  1 
ATOM 1706 C C   . PHE B 1 335 ? 187.230 145.535 211.085 1.00 57.79  ? 335 PHE A C   1 
ATOM 1707 O O   . PHE B 1 335 ? 186.759 146.528 211.651 1.00 59.21  ? 335 PHE A O   1 
ATOM 1708 C CB  . PHE B 1 335 ? 186.731 145.403 208.627 1.00 56.99  ? 335 PHE A CB  1 
ATOM 1709 C CG  . PHE B 1 335 ? 187.003 146.103 207.335 1.00 59.95  ? 335 PHE A CG  1 
ATOM 1710 C CD1 . PHE B 1 335 ? 187.959 147.090 207.251 1.00 64.79  ? 335 PHE A CD1 1 
ATOM 1711 C CD2 . PHE B 1 335 ? 186.385 145.691 206.175 1.00 58.60  ? 335 PHE A CD2 1 
ATOM 1712 C CE1 . PHE B 1 335 ? 188.224 147.722 206.050 1.00 68.92  ? 335 PHE A CE1 1 
ATOM 1713 C CE2 . PHE B 1 335 ? 186.672 146.300 204.974 1.00 64.05  ? 335 PHE A CE2 1 
ATOM 1714 C CZ  . PHE B 1 335 ? 187.587 147.321 204.921 1.00 69.34  ? 335 PHE A CZ  1 
ATOM 1715 N N   . HIS B 1 336 ? 187.232 144.324 211.644 1.00 59.63  ? 336 HIS A N   1 
ATOM 1716 C CA  . HIS B 1 336 ? 186.862 144.154 213.043 1.00 58.53  ? 336 HIS A CA  1 
ATOM 1717 C C   . HIS B 1 336 ? 187.862 144.859 213.952 1.00 53.75  ? 336 HIS A C   1 
ATOM 1718 O O   . HIS B 1 336 ? 187.470 145.524 214.915 1.00 56.75  ? 336 HIS A O   1 
ATOM 1719 C CB  . HIS B 1 336 ? 186.770 142.661 213.369 1.00 63.97  ? 336 HIS A CB  1 
ATOM 1720 C CG  . HIS B 1 336 ? 185.888 142.335 214.537 1.00 71.66  ? 336 HIS A CG  1 
ATOM 1721 N ND1 . HIS B 1 336 ? 184.700 142.990 214.784 1.00 75.43  ? 336 HIS A ND1 1 
ATOM 1722 C CD2 . HIS B 1 336 ? 185.998 141.385 215.497 1.00 73.08  ? 336 HIS A CD2 1 
ATOM 1723 C CE1 . HIS B 1 336 ? 184.132 142.477 215.861 1.00 78.56  ? 336 HIS A CE1 1 
ATOM 1724 N NE2 . HIS B 1 336 ? 184.899 141.501 216.312 1.00 80.37  ? 336 HIS A NE2 1 
ATOM 1725 N N   . GLU B 1 337 ? 189.157 144.769 213.622 1.00 51.00  ? 337 GLU A N   1 
ATOM 1726 C CA  . GLU B 1 337 ? 190.215 145.347 214.448 1.00 57.27  ? 337 GLU A CA  1 
ATOM 1727 C C   . GLU B 1 337 ? 190.174 146.869 214.497 1.00 59.53  ? 337 GLU A C   1 
ATOM 1728 O O   . GLU B 1 337 ? 190.716 147.458 215.438 1.00 65.07  ? 337 GLU A O   1 
ATOM 1729 C CB  . GLU B 1 337 ? 191.585 144.897 213.936 1.00 66.22  ? 337 GLU A CB  1 
ATOM 1730 C CG  . GLU B 1 337 ? 191.940 143.458 214.277 1.00 79.54  ? 337 GLU A CG  1 
ATOM 1731 C CD  . GLU B 1 337 ? 193.293 143.049 213.728 1.00 89.65  ? 337 GLU A CD  1 
ATOM 1732 O OE1 . GLU B 1 337 ? 193.927 143.876 213.040 1.00 87.74  ? 337 GLU A OE1 1 
ATOM 1733 O OE2 . GLU B 1 337 ? 193.720 141.902 213.980 1.00 96.22  ? 337 GLU A OE2 1 
ATOM 1734 N N   . VAL B 1 338 ? 189.554 147.516 213.515 1.00 56.52  ? 338 VAL A N   1 
ATOM 1735 C CA  . VAL B 1 338 ? 189.403 148.967 213.537 1.00 49.42  ? 338 VAL A CA  1 
ATOM 1736 C C   . VAL B 1 338 ? 188.131 149.377 214.271 1.00 47.64  ? 338 VAL A C   1 
ATOM 1737 O O   . VAL B 1 338 ? 188.131 150.348 215.032 1.00 51.57  ? 338 VAL A O   1 
ATOM 1738 C CB  . VAL B 1 338 ? 189.432 149.509 212.091 1.00 45.50  ? 338 VAL A CB  1 
ATOM 1739 C CG1 . VAL B 1 338 ? 189.122 150.996 212.050 1.00 40.76  ? 338 VAL A CG1 1 
ATOM 1740 C CG2 . VAL B 1 338 ? 190.782 149.228 211.448 1.00 47.20  ? 338 VAL A CG2 1 
ATOM 1741 N N   . PHE B 1 339 ? 187.028 148.716 213.954 1.00 45.81  ? 339 PHE A N   1 
ATOM 1742 C CA  . PHE B 1 339 ? 185.709 149.203 214.434 1.00 45.37  ? 339 PHE A CA  1 
ATOM 1743 C C   . PHE B 1 339 ? 185.529 148.934 215.903 1.00 50.65  ? 339 PHE A C   1 
ATOM 1744 O O   . PHE B 1 339 ? 184.725 149.646 216.520 1.00 52.73  ? 339 PHE A O   1 
ATOM 1745 C CB  . PHE B 1 339 ? 184.588 148.645 213.546 1.00 47.06  ? 339 PHE A CB  1 
ATOM 1746 C CG  . PHE B 1 339 ? 184.332 149.247 212.173 1.00 44.44  ? 339 PHE A CG  1 
ATOM 1747 C CD1 . PHE B 1 339 ? 185.157 148.953 211.098 1.00 43.67  ? 339 PHE A CD1 1 
ATOM 1748 C CD2 . PHE B 1 339 ? 183.219 150.040 211.944 1.00 44.49  ? 339 PHE A CD2 1 
ATOM 1749 C CE1 . PHE B 1 339 ? 184.911 149.488 209.847 1.00 41.54  ? 339 PHE A CE1 1 
ATOM 1750 C CE2 . PHE B 1 339 ? 182.974 150.571 210.693 1.00 44.87  ? 339 PHE A CE2 1 
ATOM 1751 C CZ  . PHE B 1 339 ? 183.816 150.291 209.646 1.00 42.13  ? 339 PHE A CZ  1 
ATOM 1752 N N   . ASN B 1 340 ? 186.272 147.994 216.464 1.00 51.38  ? 340 ASN A N   1 
ATOM 1753 C CA  . ASN B 1 340 ? 186.113 147.636 217.886 1.00 51.88  ? 340 ASN A CA  1 
ATOM 1754 C C   . ASN B 1 340 ? 187.480 147.709 218.568 1.00 50.29  ? 340 ASN A C   1 
ATOM 1755 O O   . ASN B 1 340 ? 188.029 146.638 218.853 1.00 51.75  ? 340 ASN A O   1 
ATOM 1756 C CB  . ASN B 1 340 ? 185.404 146.292 217.984 1.00 57.58  ? 340 ASN A CB  1 
ATOM 1757 C CG  . ASN B 1 340 ? 185.340 145.753 219.392 1.00 65.86  ? 340 ASN A CG  1 
ATOM 1758 O OD1 . ASN B 1 340 ? 184.792 146.405 220.287 1.00 68.43  ? 340 ASN A OD1 1 
ATOM 1759 N ND2 . ASN B 1 340 ? 185.894 144.568 219.605 1.00 68.68  ? 340 ASN A ND2 1 
ATOM 1760 N N   . ALA B 1 341 ? 188.003 148.916 218.804 1.00 48.74  ? 341 ALA A N   1 
ATOM 1761 C CA  . ALA B 1 341 ? 189.289 149.104 219.523 1.00 48.71  ? 341 ALA A CA  1 
ATOM 1762 C C   . ALA B 1 341 ? 189.074 149.748 220.895 1.00 51.68  ? 341 ALA A C   1 
ATOM 1763 O O   . ALA B 1 341 ? 187.965 150.247 221.126 1.00 55.01  ? 341 ALA A O   1 
ATOM 1764 C CB  . ALA B 1 341 ? 190.215 149.928 218.680 1.00 46.01  ? 341 ALA A CB  1 
ATOM 1765 N N   . THR B 1 342 ? 190.091 149.777 221.761 1.00 46.36  ? 342 THR A N   1 
ATOM 1766 C CA  . THR B 1 342 ? 189.938 150.274 223.124 1.00 46.02  ? 342 THR A CA  1 
ATOM 1767 C C   . THR B 1 342 ? 189.666 151.773 223.141 1.00 47.97  ? 342 THR A C   1 
ATOM 1768 O O   . THR B 1 342 ? 188.825 152.247 223.913 1.00 50.35  ? 342 THR A O   1 
ATOM 1769 C CB  . THR B 1 342 ? 191.183 149.946 223.946 1.00 53.52  ? 342 THR A CB  1 
ATOM 1770 O OG1 . THR B 1 342 ? 192.324 150.592 223.368 1.00 59.05  ? 342 THR A OG1 1 
ATOM 1771 C CG2 . THR B 1 342 ? 191.418 148.444 223.977 1.00 52.74  ? 342 THR A CG2 1 
ATOM 1772 N N   . ARG B 1 343 ? 190.358 152.531 222.294 1.00 47.54  ? 343 ARG A N   1 
ATOM 1773 C CA  . ARG B 1 343 ? 190.164 153.970 222.215 1.00 45.44  ? 343 ARG A CA  1 
ATOM 1774 C C   . ARG B 1 343 ? 190.577 154.457 220.834 1.00 43.49  ? 343 ARG A C   1 
ATOM 1775 O O   . ARG B 1 343 ? 191.598 154.026 220.291 1.00 42.62  ? 343 ARG A O   1 
ATOM 1776 C CB  . ARG B 1 343 ? 190.942 154.693 223.327 1.00 50.65  ? 343 ARG A CB  1 
ATOM 1777 C CG  . ARG B 1 343 ? 192.446 154.447 223.334 1.00 55.01  ? 343 ARG A CG  1 
ATOM 1778 C CD  . ARG B 1 343 ? 193.146 155.261 224.412 1.00 65.25  ? 343 ARG A CD  1 
ATOM 1779 N NE  . ARG B 1 343 ? 193.153 156.688 224.116 1.00 73.90  ? 343 ARG A NE  1 
ATOM 1780 C CZ  . ARG B 1 343 ? 192.797 157.632 224.976 1.00 77.23  ? 343 ARG A CZ  1 
ATOM 1781 N NH1 . ARG B 1 343 ? 192.395 157.336 226.201 1.00 77.39  ? 343 ARG A NH1 1 
ATOM 1782 N NH2 . ARG B 1 343 ? 192.846 158.906 224.598 1.00 71.80  ? 343 ARG A NH2 1 
ATOM 1783 N N   . PHE B 1 344 ? 189.757 155.331 220.257 1.00 40.91  ? 344 PHE A N   1 
ATOM 1784 C CA  . PHE B 1 344 ? 190.045 155.907 218.953 1.00 37.80  ? 344 PHE A CA  1 
ATOM 1785 C C   . PHE B 1 344 ? 190.887 157.169 219.112 1.00 40.58  ? 344 PHE A C   1 
ATOM 1786 O O   . PHE B 1 344 ? 191.206 157.605 220.220 1.00 46.04  ? 344 PHE A O   1 
ATOM 1787 C CB  . PHE B 1 344 ? 188.761 156.203 218.169 1.00 36.23  ? 344 PHE A CB  1 
ATOM 1788 C CG  . PHE B 1 344 ? 187.963 154.977 217.751 1.00 40.98  ? 344 PHE A CG  1 
ATOM 1789 C CD1 . PHE B 1 344 ? 188.370 153.686 218.062 1.00 46.09  ? 344 PHE A CD1 1 
ATOM 1790 C CD2 . PHE B 1 344 ? 186.803 155.137 217.013 1.00 35.70  ? 344 PHE A CD2 1 
ATOM 1791 C CE1 . PHE B 1 344 ? 187.629 152.591 217.658 1.00 46.25  ? 344 PHE A CE1 1 
ATOM 1792 C CE2 . PHE B 1 344 ? 186.063 154.049 216.606 1.00 35.14  ? 344 PHE A CE2 1 
ATOM 1793 C CZ  . PHE B 1 344 ? 186.474 152.775 216.931 1.00 42.20  ? 344 PHE A CZ  1 
ATOM 1794 N N   . ALA B 1 345 ? 191.255 157.764 217.985 1.00 38.26  ? 345 ALA A N   1 
ATOM 1795 C CA  . ALA B 1 345 ? 192.101 158.946 217.966 1.00 36.26  ? 345 ALA A CA  1 
ATOM 1796 C C   . ALA B 1 345 ? 191.256 160.212 218.004 1.00 30.04  ? 345 ALA A C   1 
ATOM 1797 O O   . ALA B 1 345 ? 190.055 160.200 217.725 1.00 31.69  ? 345 ALA A O   1 
ATOM 1798 C CB  . ALA B 1 345 ? 192.997 158.953 216.725 1.00 37.82  ? 345 ALA A CB  1 
ATOM 1799 N N   . SER B 1 346 ? 191.907 161.313 218.365 1.00 27.31  ? 346 SER A N   1 
ATOM 1800 C CA  . SER B 1 346 ? 191.248 162.605 218.376 1.00 31.93  ? 346 SER A CA  1 
ATOM 1801 C C   . SER B 1 346 ? 191.018 163.092 216.947 1.00 37.14  ? 346 SER A C   1 
ATOM 1802 O O   . SER B 1 346 ? 191.569 162.561 215.979 1.00 43.03  ? 346 SER A O   1 
ATOM 1803 C CB  . SER B 1 346 ? 192.074 163.617 219.167 1.00 39.21  ? 346 SER A CB  1 
ATOM 1804 O OG  . SER B 1 346 ? 192.167 163.238 220.528 1.00 48.80  ? 346 SER A OG  1 
ATOM 1805 N N   . VAL B 1 347 ? 190.179 164.123 216.825 1.00 33.32  ? 347 VAL A N   1 
ATOM 1806 C CA  . VAL B 1 347 ? 189.746 164.575 215.507 1.00 31.65  ? 347 VAL A CA  1 
ATOM 1807 C C   . VAL B 1 347 ? 190.874 165.288 214.768 1.00 35.49  ? 347 VAL A C   1 
ATOM 1808 O O   . VAL B 1 347 ? 191.012 165.140 213.548 1.00 39.95  ? 347 VAL A O   1 
ATOM 1809 C CB  . VAL B 1 347 ? 188.494 165.461 215.652 1.00 35.36  ? 347 VAL A CB  1 
ATOM 1810 C CG1 . VAL B 1 347 ? 188.053 166.011 214.321 1.00 34.21  ? 347 VAL A CG1 1 
ATOM 1811 C CG2 . VAL B 1 347 ? 187.380 164.677 216.273 1.00 37.28  ? 347 VAL A CG2 1 
ATOM 1812 N N   . TYR B 1 348 ? 191.715 166.049 215.477 1.00 33.95  ? 348 TYR A N   1 
ATOM 1813 C CA  . TYR B 1 348 ? 192.758 166.809 214.794 1.00 34.57  ? 348 TYR A CA  1 
ATOM 1814 C C   . TYR B 1 348 ? 193.867 165.903 214.276 1.00 41.27  ? 348 TYR A C   1 
ATOM 1815 O O   . TYR B 1 348 ? 194.625 166.312 213.390 1.00 51.30  ? 348 TYR A O   1 
ATOM 1816 C CB  . TYR B 1 348 ? 193.361 167.867 215.725 1.00 38.20  ? 348 TYR A CB  1 
ATOM 1817 C CG  . TYR B 1 348 ? 194.133 167.321 216.909 1.00 40.80  ? 348 TYR A CG  1 
ATOM 1818 C CD1 . TYR B 1 348 ? 193.504 167.026 218.105 1.00 43.97  ? 348 TYR A CD1 1 
ATOM 1819 C CD2 . TYR B 1 348 ? 195.515 167.166 216.844 1.00 44.91  ? 348 TYR A CD2 1 
ATOM 1820 C CE1 . TYR B 1 348 ? 194.221 166.534 219.180 1.00 47.07  ? 348 TYR A CE1 1 
ATOM 1821 C CE2 . TYR B 1 348 ? 196.236 166.683 217.915 1.00 46.04  ? 348 TYR A CE2 1 
ATOM 1822 C CZ  . TYR B 1 348 ? 195.584 166.372 219.082 1.00 50.10  ? 348 TYR A CZ  1 
ATOM 1823 O OH  . TYR B 1 348 ? 196.298 165.892 220.155 1.00 55.38  ? 348 TYR A OH  1 
ATOM 1824 N N   . ALA B 1 349 ? 193.973 164.691 214.811 1.00 36.75  ? 349 ALA A N   1 
ATOM 1825 C CA  . ALA B 1 349 ? 195.026 163.731 214.505 1.00 39.50  ? 349 ALA A CA  1 
ATOM 1826 C C   . ALA B 1 349 ? 194.419 162.363 214.234 1.00 44.62  ? 349 ALA A C   1 
ATOM 1827 O O   . ALA B 1 349 ? 194.807 161.356 214.831 1.00 48.85  ? 349 ALA A O   1 
ATOM 1828 C CB  . ALA B 1 349 ? 196.045 163.656 215.636 1.00 37.91  ? 349 ALA A CB  1 
ATOM 1829 N N   . TRP B 1 350 ? 193.417 162.332 213.351 1.00 45.08  ? 350 TRP A N   1 
ATOM 1830 C CA  . TRP B 1 350 ? 192.631 161.127 213.109 1.00 41.31  ? 350 TRP A CA  1 
ATOM 1831 C C   . TRP B 1 350 ? 193.496 160.000 212.557 1.00 41.85  ? 350 TRP A C   1 
ATOM 1832 O O   . TRP B 1 350 ? 194.317 160.211 211.659 1.00 47.99  ? 350 TRP A O   1 
ATOM 1833 C CB  . TRP B 1 350 ? 191.483 161.428 212.144 1.00 37.17  ? 350 TRP A CB  1 
ATOM 1834 C CG  . TRP B 1 350 ? 191.832 162.342 211.002 1.00 43.08  ? 350 TRP A CG  1 
ATOM 1835 C CD1 . TRP B 1 350 ? 191.734 163.699 210.982 1.00 44.44  ? 350 TRP A CD1 1 
ATOM 1836 C CD2 . TRP B 1 350 ? 192.287 161.958 209.697 1.00 46.58  ? 350 TRP A CD2 1 
ATOM 1837 N NE1 . TRP B 1 350 ? 192.121 164.189 209.762 1.00 47.05  ? 350 TRP A NE1 1 
ATOM 1838 C CE2 . TRP B 1 350 ? 192.463 163.140 208.953 1.00 47.78  ? 350 TRP A CE2 1 
ATOM 1839 C CE3 . TRP B 1 350 ? 192.570 160.732 209.089 1.00 49.12  ? 350 TRP A CE3 1 
ATOM 1840 C CZ2 . TRP B 1 350 ? 192.912 163.132 207.636 1.00 48.07  ? 350 TRP A CZ2 1 
ATOM 1841 C CZ3 . TRP B 1 350 ? 193.016 160.728 207.782 1.00 51.89  ? 350 TRP A CZ3 1 
ATOM 1842 C CH2 . TRP B 1 350 ? 193.182 161.919 207.070 1.00 49.74  ? 350 TRP A CH2 1 
ATOM 1843 N N   . ASN B 1 351 ? 193.322 158.808 213.118 1.00 36.48  ? 351 ASN A N   1 
ATOM 1844 C CA  . ASN B 1 351 ? 194.079 157.647 212.677 1.00 38.53  ? 351 ASN A CA  1 
ATOM 1845 C C   . ASN B 1 351 ? 193.550 157.184 211.328 1.00 41.47  ? 351 ASN A C   1 
ATOM 1846 O O   . ASN B 1 351 ? 192.341 157.073 211.128 1.00 44.24  ? 351 ASN A O   1 
ATOM 1847 C CB  . ASN B 1 351 ? 193.967 156.523 213.711 1.00 38.90  ? 351 ASN A CB  1 
ATOM 1848 C CG  . ASN B 1 351 ? 194.993 155.413 213.508 1.00 40.46  ? 351 ASN A CG  1 
ATOM 1849 O OD1 . ASN B 1 351 ? 195.503 155.196 212.409 1.00 44.54  ? 351 ASN A OD1 1 
ATOM 1850 N ND2 . ASN B 1 351 ? 195.297 154.701 214.586 1.00 34.77  ? 351 ASN A ND2 1 
ATOM 1851 N N   . ARG B 1 352 ? 194.465 156.911 210.403 1.00 45.71  ? 352 ARG A N   1 
ATOM 1852 C CA  . ARG B 1 352 ? 194.126 156.437 209.069 1.00 46.98  ? 352 ARG A CA  1 
ATOM 1853 C C   . ARG B 1 352 ? 194.847 155.120 208.833 1.00 47.01  ? 352 ARG A C   1 
ATOM 1854 O O   . ARG B 1 352 ? 196.042 155.004 209.125 1.00 51.51  ? 352 ARG A O   1 
ATOM 1855 C CB  . ARG B 1 352 ? 194.515 157.468 208.001 1.00 51.00  ? 352 ARG A CB  1 
ATOM 1856 C CG  . ARG B 1 352 ? 194.938 156.883 206.662 1.00 56.74  ? 352 ARG A CG  1 
ATOM 1857 C CD  . ARG B 1 352 ? 194.865 157.920 205.552 1.00 60.15  ? 352 ARG A CD  1 
ATOM 1858 N NE  . ARG B 1 352 ? 193.507 158.107 205.059 1.00 60.37  ? 352 ARG A NE  1 
ATOM 1859 C CZ  . ARG B 1 352 ? 193.207 158.651 203.888 1.00 61.38  ? 352 ARG A CZ  1 
ATOM 1860 N NH1 . ARG B 1 352 ? 194.148 159.075 203.062 1.00 58.72  ? 352 ARG A NH1 1 
ATOM 1861 N NH2 . ARG B 1 352 ? 191.930 158.771 203.537 1.00 65.66  ? 352 ARG A NH2 1 
ATOM 1862 N N   . THR B 1 353 ? 194.125 154.129 208.319 1.00 41.51  ? 353 THR A N   1 
ATOM 1863 C CA  . THR B 1 353 ? 194.695 152.818 208.061 1.00 45.09  ? 353 THR A CA  1 
ATOM 1864 C C   . THR B 1 353 ? 194.434 152.411 206.618 1.00 53.40  ? 353 THR A C   1 
ATOM 1865 O O   . THR B 1 353 ? 193.499 152.895 205.973 1.00 57.62  ? 353 THR A O   1 
ATOM 1866 C CB  . THR B 1 353 ? 194.140 151.760 209.037 1.00 48.05  ? 353 THR A CB  1 
ATOM 1867 O OG1 . THR B 1 353 ? 194.935 150.570 208.962 1.00 57.44  ? 353 THR A OG1 1 
ATOM 1868 C CG2 . THR B 1 353 ? 192.688 151.432 208.741 1.00 46.89  ? 353 THR A CG2 1 
ATOM 1869 N N   . ARG B 1 354 ? 195.302 151.545 206.106 1.00 56.33  ? 354 ARG A N   1 
ATOM 1870 C CA  . ARG B 1 354 ? 195.196 151.022 204.753 1.00 53.01  ? 354 ARG A CA  1 
ATOM 1871 C C   . ARG B 1 354 ? 194.809 149.554 204.796 1.00 55.79  ? 354 ARG A C   1 
ATOM 1872 O O   . ARG B 1 354 ? 195.332 148.785 205.607 1.00 58.78  ? 354 ARG A O   1 
ATOM 1873 C CB  . ARG B 1 354 ? 196.505 151.177 203.982 1.00 52.69  ? 354 ARG A CB  1 
ATOM 1874 C CG  . ARG B 1 354 ? 196.692 152.536 203.366 1.00 62.69  ? 354 ARG A CG  1 
ATOM 1875 C CD  . ARG B 1 354 ? 198.052 152.661 202.717 1.00 77.71  ? 354 ARG A CD  1 
ATOM 1876 N NE  . ARG B 1 354 ? 198.471 154.051 202.602 1.00 85.37  ? 354 ARG A NE  1 
ATOM 1877 C CZ  . ARG B 1 354 ? 199.521 154.458 201.903 1.00 89.54  ? 354 ARG A CZ  1 
ATOM 1878 N NH1 . ARG B 1 354 ? 200.283 153.604 201.240 1.00 93.35  ? 354 ARG A NH1 1 
ATOM 1879 N NH2 . ARG B 1 354 ? 199.814 155.755 201.868 1.00 89.20  ? 354 ARG A NH2 1 
ATOM 1880 N N   . ILE B 1 355 ? 193.887 149.174 203.920 1.00 51.73  ? 355 ILE A N   1 
ATOM 1881 C CA  . ILE B 1 355 ? 193.412 147.803 203.822 1.00 53.27  ? 355 ILE A CA  1 
ATOM 1882 C C   . ILE B 1 355 ? 193.694 147.313 202.413 1.00 55.56  ? 355 ILE A C   1 
ATOM 1883 O O   . ILE B 1 355 ? 193.187 147.879 201.437 1.00 60.62  ? 355 ILE A O   1 
ATOM 1884 C CB  . ILE B 1 355 ? 191.921 147.674 204.177 1.00 59.69  ? 355 ILE A CB  1 
ATOM 1885 C CG1 . ILE B 1 355 ? 191.656 148.078 205.635 1.00 66.24  ? 355 ILE A CG1 1 
ATOM 1886 C CG2 . ILE B 1 355 ? 191.425 146.277 203.902 1.00 66.89  ? 355 ILE A CG2 1 
ATOM 1887 C CD1 . ILE B 1 355 ? 191.365 149.544 205.871 1.00 62.66  ? 355 ILE A CD1 1 
ATOM 1888 N N   . SER B 1 356 ? 194.508 146.268 202.308 1.00 56.83  ? 356 SER A N   1 
ATOM 1889 C CA  . SER B 1 356 ? 194.941 145.765 201.018 1.00 61.84  ? 356 SER A CA  1 
ATOM 1890 C C   . SER B 1 356 ? 195.309 144.298 201.157 1.00 63.19  ? 356 SER A C   1 
ATOM 1891 O O   . SER B 1 356 ? 195.655 143.833 202.247 1.00 66.97  ? 356 SER A O   1 
ATOM 1892 C CB  . SER B 1 356 ? 196.128 146.570 200.476 1.00 65.92  ? 356 SER A CB  1 
ATOM 1893 O OG  . SER B 1 356 ? 197.276 146.393 201.288 1.00 73.16  ? 356 SER A OG  1 
ATOM 1894 N N   . ASN B 1 357 ? 195.223 143.583 200.031 1.00 59.79  ? 357 ASN A N   1 
ATOM 1895 C CA  . ASN B 1 357 ? 195.598 142.171 199.917 1.00 66.61  ? 357 ASN A CA  1 
ATOM 1896 C C   . ASN B 1 357 ? 194.812 141.288 200.888 1.00 71.51  ? 357 ASN A C   1 
ATOM 1897 O O   . ASN B 1 357 ? 195.377 140.478 201.626 1.00 79.36  ? 357 ASN A O   1 
ATOM 1898 C CB  . ASN B 1 357 ? 197.107 141.991 200.103 1.00 71.01  ? 357 ASN A CB  1 
ATOM 1899 C CG  . ASN B 1 357 ? 197.910 142.682 199.022 1.00 74.34  ? 357 ASN A CG  1 
ATOM 1900 O OD1 . ASN B 1 357 ? 198.647 143.631 199.292 1.00 78.39  ? 357 ASN A OD1 1 
ATOM 1901 N ND2 . ASN B 1 357 ? 197.763 142.219 197.788 1.00 76.62  ? 357 ASN A ND2 1 
ATOM 1902 N N   . CYS B 1 358 ? 193.491 141.452 200.882 1.00 65.34  ? 358 CYS A N   1 
ATOM 1903 C CA  . CYS B 1 358 ? 192.593 140.572 201.619 1.00 65.60  ? 358 CYS A CA  1 
ATOM 1904 C C   . CYS B 1 358 ? 191.230 140.598 200.941 1.00 69.28  ? 358 CYS A C   1 
ATOM 1905 O O   . CYS B 1 358 ? 191.048 141.222 199.893 1.00 73.12  ? 358 CYS A O   1 
ATOM 1906 C CB  . CYS B 1 358 ? 192.492 140.971 203.095 1.00 68.48  ? 358 CYS A CB  1 
ATOM 1907 S SG  . CYS B 1 358 ? 192.233 142.725 203.422 1.00 81.05  ? 358 CYS A SG  1 
ATOM 1908 N N   . VAL B 1 359 ? 190.267 139.902 201.539 1.00 70.06  ? 359 VAL A N   1 
ATOM 1909 C CA  . VAL B 1 359 ? 188.891 139.898 201.059 1.00 67.80  ? 359 VAL A CA  1 
ATOM 1910 C C   . VAL B 1 359 ? 188.039 140.715 202.023 1.00 70.51  ? 359 VAL A C   1 
ATOM 1911 O O   . VAL B 1 359 ? 188.097 140.524 203.246 1.00 79.41  ? 359 VAL A O   1 
ATOM 1912 C CB  . VAL B 1 359 ? 188.361 138.465 200.849 1.00 65.12  ? 359 VAL A CB  1 
ATOM 1913 C CG1 . VAL B 1 359 ? 189.215 137.768 199.830 1.00 66.30  ? 359 VAL A CG1 1 
ATOM 1914 C CG2 . VAL B 1 359 ? 188.361 137.640 202.119 1.00 67.99  ? 359 VAL A CG2 1 
ATOM 1915 N N   . ALA B 1 360 ? 187.300 141.675 201.476 1.00 63.87  ? 360 ALA A N   1 
ATOM 1916 C CA  . ALA B 1 360 ? 186.585 142.665 202.276 1.00 63.54  ? 360 ALA A CA  1 
ATOM 1917 C C   . ALA B 1 360 ? 185.104 142.306 202.278 1.00 65.29  ? 360 ALA A C   1 
ATOM 1918 O O   . ALA B 1 360 ? 184.346 142.699 201.390 1.00 71.94  ? 360 ALA A O   1 
ATOM 1919 C CB  . ALA B 1 360 ? 186.823 144.071 201.737 1.00 62.04  ? 360 ALA A CB  1 
ATOM 1920 N N   . ASP B 1 361 ? 184.693 141.555 203.293 1.00 63.56  ? 361 ASP A N   1 
ATOM 1921 C CA  . ASP B 1 361 ? 183.288 141.229 203.499 1.00 71.60  ? 361 ASP A CA  1 
ATOM 1922 C C   . ASP B 1 361 ? 182.610 142.291 204.369 1.00 72.60  ? 361 ASP A C   1 
ATOM 1923 O O   . ASP B 1 361 ? 182.951 142.481 205.538 1.00 77.19  ? 361 ASP A O   1 
ATOM 1924 C CB  . ASP B 1 361 ? 183.137 139.798 204.026 1.00 77.51  ? 361 ASP A CB  1 
ATOM 1925 C CG  . ASP B 1 361 ? 183.870 139.530 205.351 1.00 86.23  ? 361 ASP A CG  1 
ATOM 1926 O OD1 . ASP B 1 361 ? 184.586 140.400 205.886 1.00 83.70  ? 361 ASP A OD1 1 
ATOM 1927 O OD2 . ASP B 1 361 ? 183.726 138.399 205.862 1.00 91.37  ? 361 ASP A OD2 1 
ATOM 1928 N N   . TYR B 1 362 ? 181.655 143.007 203.785 1.00 66.48  ? 362 TYR A N   1 
ATOM 1929 C CA  . TYR B 1 362 ? 180.931 144.039 204.523 1.00 62.95  ? 362 TYR A CA  1 
ATOM 1930 C C   . TYR B 1 362 ? 179.697 143.455 205.205 1.00 69.89  ? 362 TYR A C   1 
ATOM 1931 O O   . TYR B 1 362 ? 178.587 143.972 205.079 1.00 73.42  ? 362 TYR A O   1 
ATOM 1932 C CB  . TYR B 1 362 ? 180.547 145.194 203.605 1.00 62.80  ? 362 TYR A CB  1 
ATOM 1933 C CG  . TYR B 1 362 ? 181.700 146.032 203.085 1.00 61.90  ? 362 TYR A CG  1 
ATOM 1934 C CD1 . TYR B 1 362 ? 182.960 145.957 203.644 1.00 61.69  ? 362 TYR A CD1 1 
ATOM 1935 C CD2 . TYR B 1 362 ? 181.492 146.952 202.068 1.00 66.51  ? 362 TYR A CD2 1 
ATOM 1936 C CE1 . TYR B 1 362 ? 183.977 146.735 203.154 1.00 68.41  ? 362 TYR A CE1 1 
ATOM 1937 C CE2 . TYR B 1 362 ? 182.513 147.735 201.586 1.00 70.30  ? 362 TYR A CE2 1 
ATOM 1938 C CZ  . TYR B 1 362 ? 183.759 147.625 202.135 1.00 74.29  ? 362 TYR A CZ  1 
ATOM 1939 O OH  . TYR B 1 362 ? 184.786 148.406 201.663 1.00 80.49  ? 362 TYR A OH  1 
ATOM 1940 N N   . SER B 1 363 ? 179.880 142.344 205.924 1.00 69.71  ? 363 SER A N   1 
ATOM 1941 C CA  . SER B 1 363 ? 178.834 141.812 206.781 1.00 68.06  ? 363 SER A CA  1 
ATOM 1942 C C   . SER B 1 363 ? 179.177 141.913 208.253 1.00 65.83  ? 363 SER A C   1 
ATOM 1943 O O   . SER B 1 363 ? 178.262 141.959 209.078 1.00 69.55  ? 363 SER A O   1 
ATOM 1944 C CB  . SER B 1 363 ? 178.545 140.343 206.438 1.00 68.99  ? 363 SER A CB  1 
ATOM 1945 O OG  . SER B 1 363 ? 179.655 139.514 206.740 1.00 71.75  ? 363 SER A OG  1 
ATOM 1946 N N   . VAL B 1 364 ? 180.468 141.956 208.593 1.00 63.27  ? 364 VAL A N   1 
ATOM 1947 C CA  . VAL B 1 364 ? 180.884 142.101 209.981 1.00 71.28  ? 364 VAL A CA  1 
ATOM 1948 C C   . VAL B 1 364 ? 180.589 143.496 210.512 1.00 73.22  ? 364 VAL A C   1 
ATOM 1949 O O   . VAL B 1 364 ? 180.553 143.696 211.731 1.00 77.05  ? 364 VAL A O   1 
ATOM 1950 C CB  . VAL B 1 364 ? 182.378 141.766 210.124 1.00 73.65  ? 364 VAL A CB  1 
ATOM 1951 C CG1 . VAL B 1 364 ? 182.638 140.322 209.729 1.00 70.84  ? 364 VAL A CG1 1 
ATOM 1952 C CG2 . VAL B 1 364 ? 183.224 142.709 209.282 1.00 71.53  ? 364 VAL A CG2 1 
ATOM 1953 N N   . LEU B 1 365 ? 180.381 144.475 209.629 1.00 67.29  ? 365 LEU A N   1 
ATOM 1954 C CA  . LEU B 1 365 ? 179.997 145.806 210.080 1.00 63.56  ? 365 LEU A CA  1 
ATOM 1955 C C   . LEU B 1 365 ? 178.536 145.858 210.501 1.00 69.43  ? 365 LEU A C   1 
ATOM 1956 O O   . LEU B 1 365 ? 178.174 146.664 211.364 1.00 71.99  ? 365 LEU A O   1 
ATOM 1957 C CB  . LEU B 1 365 ? 180.258 146.842 208.983 1.00 61.95  ? 365 LEU A CB  1 
ATOM 1958 C CG  . LEU B 1 365 ? 181.594 146.831 208.235 1.00 67.79  ? 365 LEU A CG  1 
ATOM 1959 C CD1 . LEU B 1 365 ? 181.717 148.079 207.377 1.00 59.97  ? 365 LEU A CD1 1 
ATOM 1960 C CD2 . LEU B 1 365 ? 182.770 146.733 209.197 1.00 67.55  ? 365 LEU A CD2 1 
ATOM 1961 N N   . TYR B 1 366 ? 177.690 145.012 209.912 1.00 74.36  ? 366 TYR A N   1 
ATOM 1962 C CA  . TYR B 1 366 ? 176.262 145.054 210.205 1.00 75.60  ? 366 TYR A CA  1 
ATOM 1963 C C   . TYR B 1 366 ? 175.927 144.479 211.575 1.00 76.95  ? 366 TYR A C   1 
ATOM 1964 O O   . TYR B 1 366 ? 175.019 144.986 212.243 1.00 77.26  ? 366 TYR A O   1 
ATOM 1965 C CB  . TYR B 1 366 ? 175.479 144.318 209.118 1.00 77.32  ? 366 TYR A CB  1 
ATOM 1966 C CG  . TYR B 1 366 ? 175.295 145.129 207.857 1.00 82.08  ? 366 TYR A CG  1 
ATOM 1967 C CD1 . TYR B 1 366 ? 174.531 146.289 207.864 1.00 79.96  ? 366 TYR A CD1 1 
ATOM 1968 C CD2 . TYR B 1 366 ? 175.886 144.740 206.663 1.00 80.34  ? 366 TYR A CD2 1 
ATOM 1969 C CE1 . TYR B 1 366 ? 174.357 147.037 206.716 1.00 81.35  ? 366 TYR A CE1 1 
ATOM 1970 C CE2 . TYR B 1 366 ? 175.719 145.483 205.508 1.00 80.36  ? 366 TYR A CE2 1 
ATOM 1971 C CZ  . TYR B 1 366 ? 174.954 146.631 205.542 1.00 82.78  ? 366 TYR A CZ  1 
ATOM 1972 O OH  . TYR B 1 366 ? 174.783 147.375 204.397 1.00 78.59  ? 366 TYR A OH  1 
ATOM 1973 N N   . ASN B 1 367 ? 176.627 143.436 212.012 1.00 81.21  ? 367 ASN A N   1 
ATOM 1974 C CA  . ASN B 1 367 ? 176.391 142.877 213.344 1.00 84.75  ? 367 ASN A CA  1 
ATOM 1975 C C   . ASN B 1 367 ? 177.296 143.528 214.388 1.00 76.18  ? 367 ASN A C   1 
ATOM 1976 O O   . ASN B 1 367 ? 177.957 142.867 215.189 1.00 76.63  ? 367 ASN A O   1 
ATOM 1977 C CB  . ASN B 1 367 ? 176.565 141.361 213.320 1.00 89.88  ? 367 ASN A CB  1 
ATOM 1978 C CG  . ASN B 1 367 ? 177.952 140.930 212.874 1.00 90.42  ? 367 ASN A CG  1 
ATOM 1979 O OD1 . ASN B 1 367 ? 178.233 140.837 211.682 1.00 86.22  ? 367 ASN A OD1 1 
ATOM 1980 N ND2 . ASN B 1 367 ? 178.826 140.663 213.838 1.00 87.86  ? 367 ASN A ND2 1 
ATOM 1981 N N   . PHE B 1 368 ? 177.306 144.859 214.394 1.00 69.13  ? 368 PHE A N   1 
ATOM 1982 C CA  . PHE B 1 368 ? 178.132 145.629 215.313 1.00 68.18  ? 368 PHE A CA  1 
ATOM 1983 C C   . PHE B 1 368 ? 177.318 146.493 216.259 1.00 70.25  ? 368 PHE A C   1 
ATOM 1984 O O   . PHE B 1 368 ? 177.492 146.397 217.480 1.00 74.12  ? 368 PHE A O   1 
ATOM 1985 C CB  . PHE B 1 368 ? 179.116 146.507 214.525 1.00 67.23  ? 368 PHE A CB  1 
ATOM 1986 C CG  . PHE B 1 368 ? 180.318 146.923 215.316 1.00 64.15  ? 368 PHE A CG  1 
ATOM 1987 C CD1 . PHE B 1 368 ? 181.423 146.095 215.415 1.00 67.00  ? 368 PHE A CD1 1 
ATOM 1988 C CD2 . PHE B 1 368 ? 180.339 148.147 215.963 1.00 59.03  ? 368 PHE A CD2 1 
ATOM 1989 C CE1 . PHE B 1 368 ? 182.525 146.478 216.148 1.00 65.26  ? 368 PHE A CE1 1 
ATOM 1990 C CE2 . PHE B 1 368 ? 181.440 148.538 216.696 1.00 61.17  ? 368 PHE A CE2 1 
ATOM 1991 C CZ  . PHE B 1 368 ? 182.532 147.704 216.789 1.00 65.53  ? 368 PHE A CZ  1 
ATOM 1992 N N   . ALA B 1 369 ? 176.428 147.334 215.736 1.00 69.18  ? 369 ALA A N   1 
ATOM 1993 C CA  . ALA B 1 369 ? 175.744 148.316 216.563 1.00 67.58  ? 369 ALA A CA  1 
ATOM 1994 C C   . ALA B 1 369 ? 174.469 148.751 215.859 1.00 63.06  ? 369 ALA A C   1 
ATOM 1995 O O   . ALA B 1 369 ? 174.377 148.638 214.632 1.00 61.57  ? 369 ALA A O   1 
ATOM 1996 C CB  . ALA B 1 369 ? 176.651 149.529 216.829 1.00 59.45  ? 369 ALA A CB  1 
ATOM 1997 N N   . PRO B 1 370 ? 173.467 149.244 216.600 1.00 62.08  ? 370 PRO A N   1 
ATOM 1998 C CA  . PRO B 1 370 ? 172.359 149.960 215.952 1.00 61.55  ? 370 PRO A CA  1 
ATOM 1999 C C   . PRO B 1 370 ? 172.796 151.357 215.547 1.00 61.95  ? 370 PRO A C   1 
ATOM 2000 O O   . PRO B 1 370 ? 172.639 152.311 216.317 1.00 63.02  ? 370 PRO A O   1 
ATOM 2001 C CB  . PRO B 1 370 ? 171.256 149.985 217.019 1.00 62.25  ? 370 PRO A CB  1 
ATOM 2002 C CG  . PRO B 1 370 ? 171.857 149.456 218.276 1.00 64.55  ? 370 PRO A CG  1 
ATOM 2003 C CD  . PRO B 1 370 ? 173.298 149.145 218.061 1.00 62.37  ? 370 PRO A CD  1 
ATOM 2004 N N   . PHE B 1 371 ? 173.367 151.463 214.346 1.00 60.19  ? 371 PHE A N   1 
ATOM 2005 C CA  . PHE B 1 371 ? 174.101 152.648 213.916 1.00 48.06  ? 371 PHE A CA  1 
ATOM 2006 C C   . PHE B 1 371 ? 173.211 153.885 213.866 1.00 44.52  ? 371 PHE A C   1 
ATOM 2007 O O   . PHE B 1 371 ? 171.998 153.805 213.656 1.00 48.89  ? 371 PHE A O   1 
ATOM 2008 C CB  . PHE B 1 371 ? 174.714 152.412 212.535 1.00 43.05  ? 371 PHE A CB  1 
ATOM 2009 C CG  . PHE B 1 371 ? 175.872 151.463 212.538 1.00 44.53  ? 371 PHE A CG  1 
ATOM 2010 C CD1 . PHE B 1 371 ? 176.821 151.506 213.546 1.00 49.47  ? 371 PHE A CD1 1 
ATOM 2011 C CD2 . PHE B 1 371 ? 176.016 150.530 211.528 1.00 44.73  ? 371 PHE A CD2 1 
ATOM 2012 C CE1 . PHE B 1 371 ? 177.890 150.631 213.545 1.00 53.52  ? 371 PHE A CE1 1 
ATOM 2013 C CE2 . PHE B 1 371 ? 177.079 149.655 211.522 1.00 48.57  ? 371 PHE A CE2 1 
ATOM 2014 C CZ  . PHE B 1 371 ? 178.017 149.704 212.531 1.00 52.52  ? 371 PHE A CZ  1 
ATOM 2015 N N   . PHE B 1 372 ? 173.839 155.043 214.067 1.00 40.79  ? 372 PHE A N   1 
ATOM 2016 C CA  . PHE B 1 372 ? 173.145 156.322 214.053 1.00 43.38  ? 372 PHE A CA  1 
ATOM 2017 C C   . PHE B 1 372 ? 173.134 156.967 212.675 1.00 41.98  ? 372 PHE A C   1 
ATOM 2018 O O   . PHE B 1 372 ? 172.181 157.679 212.340 1.00 46.64  ? 372 PHE A O   1 
ATOM 2019 C CB  . PHE B 1 372 ? 173.791 157.274 215.065 1.00 49.95  ? 372 PHE A CB  1 
ATOM 2020 C CG  . PHE B 1 372 ? 173.171 158.642 215.102 1.00 52.77  ? 372 PHE A CG  1 
ATOM 2021 C CD1 . PHE B 1 372 ? 171.862 158.813 215.520 1.00 56.31  ? 372 PHE A CD1 1 
ATOM 2022 C CD2 . PHE B 1 372 ? 173.902 159.756 214.726 1.00 50.40  ? 372 PHE A CD2 1 
ATOM 2023 C CE1 . PHE B 1 372 ? 171.291 160.072 215.556 1.00 57.51  ? 372 PHE A CE1 1 
ATOM 2024 C CE2 . PHE B 1 372 ? 173.338 161.016 214.760 1.00 54.68  ? 372 PHE A CE2 1 
ATOM 2025 C CZ  . PHE B 1 372 ? 172.031 161.174 215.176 1.00 58.86  ? 372 PHE A CZ  1 
ATOM 2026 N N   . ALA B 1 373 ? 174.162 156.725 211.866 1.00 42.89  ? 373 ALA A N   1 
ATOM 2027 C CA  . ALA B 1 373 ? 174.230 157.291 210.523 1.00 50.70  ? 373 ALA A CA  1 
ATOM 2028 C C   . ALA B 1 373 ? 175.067 156.371 209.651 1.00 50.47  ? 373 ALA A C   1 
ATOM 2029 O O   . ALA B 1 373 ? 176.263 156.201 209.901 1.00 50.97  ? 373 ALA A O   1 
ATOM 2030 C CB  . ALA B 1 373 ? 174.826 158.700 210.546 1.00 50.61  ? 373 ALA A CB  1 
ATOM 2031 N N   . PHE B 1 374 ? 174.439 155.781 208.635 1.00 48.40  ? 374 PHE A N   1 
ATOM 2032 C CA  . PHE B 1 374 ? 175.108 154.890 207.686 1.00 45.93  ? 374 PHE A CA  1 
ATOM 2033 C C   . PHE B 1 374 ? 174.737 155.401 206.297 1.00 47.90  ? 374 PHE A C   1 
ATOM 2034 O O   . PHE B 1 374 ? 173.771 154.933 205.689 1.00 53.25  ? 374 PHE A O   1 
ATOM 2035 C CB  . PHE B 1 374 ? 174.686 153.436 207.908 1.00 41.93  ? 374 PHE A CB  1 
ATOM 2036 C CG  . PHE B 1 374 ? 175.555 152.420 207.209 1.00 46.14  ? 374 PHE A CG  1 
ATOM 2037 C CD1 . PHE B 1 374 ? 176.752 152.782 206.612 1.00 47.28  ? 374 PHE A CD1 1 
ATOM 2038 C CD2 . PHE B 1 374 ? 175.177 151.089 207.176 1.00 53.40  ? 374 PHE A CD2 1 
ATOM 2039 C CE1 . PHE B 1 374 ? 177.541 151.838 205.980 1.00 51.70  ? 374 PHE A CE1 1 
ATOM 2040 C CE2 . PHE B 1 374 ? 175.965 150.144 206.550 1.00 55.46  ? 374 PHE A CE2 1 
ATOM 2041 C CZ  . PHE B 1 374 ? 177.147 150.519 205.953 1.00 54.04  ? 374 PHE A CZ  1 
ATOM 2042 N N   . LYS B 1 375 ? 175.512 156.359 205.797 1.00 47.38  ? 375 LYS A N   1 
ATOM 2043 C CA  . LYS B 1 375 ? 175.264 156.995 204.512 1.00 50.83  ? 375 LYS A CA  1 
ATOM 2044 C C   . LYS B 1 375 ? 176.406 156.673 203.564 1.00 50.15  ? 375 LYS A C   1 
ATOM 2045 O O   . LYS B 1 375 ? 177.577 156.858 203.912 1.00 52.74  ? 375 LYS A O   1 
ATOM 2046 C CB  . LYS B 1 375 ? 175.117 158.510 204.670 1.00 58.46  ? 375 LYS A CB  1 
ATOM 2047 C CG  . LYS B 1 375 ? 173.860 158.938 205.410 1.00 65.31  ? 375 LYS A CG  1 
ATOM 2048 C CD  . LYS B 1 375 ? 173.816 160.446 205.597 1.00 73.12  ? 375 LYS A CD  1 
ATOM 2049 C CE  . LYS B 1 375 ? 173.570 161.159 204.279 1.00 71.84  ? 375 LYS A CE  1 
ATOM 2050 N NZ  . LYS B 1 375 ? 172.203 160.896 203.750 1.00 71.65  ? 375 LYS A NZ  1 
ATOM 2051 N N   . CYS B 1 376 ? 176.066 156.197 202.370 1.00 52.66  ? 376 CYS A N   1 
ATOM 2052 C CA  . CYS B 1 376 ? 177.046 155.818 201.364 1.00 55.71  ? 376 CYS A CA  1 
ATOM 2053 C C   . CYS B 1 376 ? 176.849 156.660 200.112 1.00 58.93  ? 376 CYS A C   1 
ATOM 2054 O O   . CYS B 1 376 ? 175.721 156.844 199.647 1.00 61.16  ? 376 CYS A O   1 
ATOM 2055 C CB  . CYS B 1 376 ? 176.934 154.330 201.023 1.00 56.84  ? 376 CYS A CB  1 
ATOM 2056 S SG  . CYS B 1 376 ? 177.499 153.230 202.339 1.00 84.96  ? 376 CYS A SG  1 
ATOM 2057 N N   . TYR B 1 377 ? 177.953 157.170 199.573 1.00 61.20  ? 377 TYR A N   1 
ATOM 2058 C CA  . TYR B 1 377 ? 177.939 158.019 198.390 1.00 59.46  ? 377 TYR A CA  1 
ATOM 2059 C C   . TYR B 1 377 ? 178.594 157.292 197.225 1.00 59.69  ? 377 TYR A C   1 
ATOM 2060 O O   . TYR B 1 377 ? 179.735 156.830 197.336 1.00 65.34  ? 377 TYR A O   1 
ATOM 2061 C CB  . TYR B 1 377 ? 178.661 159.340 198.659 1.00 55.35  ? 377 TYR A CB  1 
ATOM 2062 C CG  . TYR B 1 377 ? 178.100 160.110 199.831 1.00 58.57  ? 377 TYR A CG  1 
ATOM 2063 C CD1 . TYR B 1 377 ? 176.845 160.704 199.760 1.00 65.14  ? 377 TYR A CD1 1 
ATOM 2064 C CD2 . TYR B 1 377 ? 178.822 160.241 201.007 1.00 55.17  ? 377 TYR A CD2 1 
ATOM 2065 C CE1 . TYR B 1 377 ? 176.329 161.410 200.831 1.00 63.64  ? 377 TYR A CE1 1 
ATOM 2066 C CE2 . TYR B 1 377 ? 178.314 160.942 202.082 1.00 55.37  ? 377 TYR A CE2 1 
ATOM 2067 C CZ  . TYR B 1 377 ? 177.069 161.525 201.989 1.00 59.71  ? 377 TYR A CZ  1 
ATOM 2068 O OH  . TYR B 1 377 ? 176.561 162.224 203.058 1.00 62.31  ? 377 TYR A OH  1 
ATOM 2069 N N   . GLY B 1 378 ? 177.870 157.194 196.111 1.00 54.58  ? 378 GLY A N   1 
ATOM 2070 C CA  . GLY B 1 378 ? 178.379 156.568 194.913 1.00 53.87  ? 378 GLY A CA  1 
ATOM 2071 C C   . GLY B 1 378 ? 178.155 155.075 194.818 1.00 56.02  ? 378 GLY A C   1 
ATOM 2072 O O   . GLY B 1 378 ? 178.435 154.493 193.762 1.00 60.07  ? 378 GLY A O   1 
ATOM 2073 N N   . VAL B 1 379 ? 177.659 154.436 195.874 1.00 53.57  ? 379 VAL A N   1 
ATOM 2074 C CA  . VAL B 1 379 ? 177.469 152.991 195.875 1.00 48.64  ? 379 VAL A CA  1 
ATOM 2075 C C   . VAL B 1 379 ? 176.377 152.655 196.884 1.00 47.44  ? 379 VAL A C   1 
ATOM 2076 O O   . VAL B 1 379 ? 176.247 153.309 197.923 1.00 53.18  ? 379 VAL A O   1 
ATOM 2077 C CB  . VAL B 1 379 ? 178.806 152.259 196.161 1.00 55.66  ? 379 VAL A CB  1 
ATOM 2078 C CG1 . VAL B 1 379 ? 179.326 152.555 197.567 1.00 58.43  ? 379 VAL A CG1 1 
ATOM 2079 C CG2 . VAL B 1 379 ? 178.685 150.764 195.906 1.00 57.76  ? 379 VAL A CG2 1 
ATOM 2080 N N   . SER B 1 380 ? 175.555 151.662 196.544 1.00 45.56  ? 380 SER A N   1 
ATOM 2081 C CA  . SER B 1 380 ? 174.475 151.234 197.417 1.00 51.94  ? 380 SER A CA  1 
ATOM 2082 C C   . SER B 1 380 ? 175.013 150.357 198.545 1.00 53.60  ? 380 SER A C   1 
ATOM 2083 O O   . SER B 1 380 ? 175.981 149.617 198.354 1.00 57.19  ? 380 SER A O   1 
ATOM 2084 C CB  . SER B 1 380 ? 173.423 150.465 196.624 1.00 61.25  ? 380 SER A CB  1 
ATOM 2085 O OG  . SER B 1 380 ? 172.539 149.768 197.485 1.00 60.79  ? 380 SER A OG  1 
ATOM 2086 N N   . PRO B 1 381 ? 174.415 150.445 199.739 1.00 51.13  ? 381 PRO A N   1 
ATOM 2087 C CA  . PRO B 1 381 ? 174.882 149.608 200.857 1.00 53.12  ? 381 PRO A CA  1 
ATOM 2088 C C   . PRO B 1 381 ? 174.714 148.113 200.632 1.00 54.00  ? 381 PRO A C   1 
ATOM 2089 O O   . PRO B 1 381 ? 175.501 147.330 201.176 1.00 56.85  ? 381 PRO A O   1 
ATOM 2090 C CB  . PRO B 1 381 ? 174.028 150.099 202.032 1.00 54.18  ? 381 PRO A CB  1 
ATOM 2091 C CG  . PRO B 1 381 ? 173.716 151.513 201.683 1.00 50.29  ? 381 PRO A CG  1 
ATOM 2092 C CD  . PRO B 1 381 ? 173.486 151.492 200.196 1.00 50.89  ? 381 PRO A CD  1 
ATOM 2093 N N   . THR B 1 382 ? 173.709 147.687 199.869 1.00 52.59  ? 382 THR A N   1 
ATOM 2094 C CA  . THR B 1 382 ? 173.502 146.268 199.609 1.00 53.02  ? 382 THR A CA  1 
ATOM 2095 C C   . THR B 1 382 ? 174.300 145.747 198.420 1.00 55.28  ? 382 THR A C   1 
ATOM 2096 O O   . THR B 1 382 ? 174.423 144.528 198.266 1.00 57.46  ? 382 THR A O   1 
ATOM 2097 C CB  . THR B 1 382 ? 172.015 145.979 199.383 1.00 58.75  ? 382 THR A CB  1 
ATOM 2098 O OG1 . THR B 1 382 ? 171.811 144.564 199.300 1.00 63.82  ? 382 THR A OG1 1 
ATOM 2099 C CG2 . THR B 1 382 ? 171.530 146.627 198.097 1.00 57.62  ? 382 THR A CG2 1 
ATOM 2100 N N   . LYS B 1 383 ? 174.851 146.629 197.591 1.00 56.37  ? 383 LYS A N   1 
ATOM 2101 C CA  . LYS B 1 383 ? 175.639 146.241 196.429 1.00 58.90  ? 383 LYS A CA  1 
ATOM 2102 C C   . LYS B 1 383 ? 177.114 146.097 196.757 1.00 59.69  ? 383 LYS A C   1 
ATOM 2103 O O   . LYS B 1 383 ? 177.925 145.901 195.848 1.00 69.31  ? 383 LYS A O   1 
ATOM 2104 C CB  . LYS B 1 383 ? 175.473 147.269 195.307 1.00 63.82  ? 383 LYS A CB  1 
ATOM 2105 C CG  . LYS B 1 383 ? 174.271 147.065 194.402 1.00 64.92  ? 383 LYS A CG  1 
ATOM 2106 C CD  . LYS B 1 383 ? 174.211 148.151 193.330 1.00 67.35  ? 383 LYS A CD  1 
ATOM 2107 C CE  . LYS B 1 383 ? 175.509 148.227 192.527 1.00 55.81  ? 383 LYS A CE  1 
ATOM 2108 N NZ  . LYS B 1 383 ? 175.844 149.618 192.104 1.00 23.96  ? 383 LYS A NZ  1 
ATOM 2109 N N   . LEU B 1 384 ? 177.478 146.212 198.032 1.00 51.48  ? 384 LEU A N   1 
ATOM 2110 C CA  . LEU B 1 384 ? 178.876 146.321 198.421 1.00 54.88  ? 384 LEU A CA  1 
ATOM 2111 C C   . LEU B 1 384 ? 179.640 145.004 198.334 1.00 55.61  ? 384 LEU A C   1 
ATOM 2112 O O   . LEU B 1 384 ? 180.875 145.024 198.319 1.00 58.44  ? 384 LEU A O   1 
ATOM 2113 C CB  . LEU B 1 384 ? 178.960 146.888 199.833 1.00 55.92  ? 384 LEU A CB  1 
ATOM 2114 C CG  . LEU B 1 384 ? 178.485 148.325 200.050 1.00 58.10  ? 384 LEU A CG  1 
ATOM 2115 C CD1 . LEU B 1 384 ? 178.484 148.738 201.518 1.00 54.41  ? 384 LEU A CD1 1 
ATOM 2116 C CD2 . LEU B 1 384 ? 179.362 149.265 199.251 1.00 57.16  ? 384 LEU A CD2 1 
ATOM 2117 N N   . ASN B 1 385 ? 178.951 143.866 198.290 1.00 57.68  ? 385 ASN A N   1 
ATOM 2118 C CA  . ASN B 1 385 ? 179.666 142.595 198.270 1.00 61.78  ? 385 ASN A CA  1 
ATOM 2119 C C   . ASN B 1 385 ? 179.993 142.131 196.856 1.00 66.45  ? 385 ASN A C   1 
ATOM 2120 O O   . ASN B 1 385 ? 181.042 141.512 196.645 1.00 67.73  ? 385 ASN A O   1 
ATOM 2121 C CB  . ASN B 1 385 ? 178.856 141.523 199.000 1.00 59.32  ? 385 ASN A CB  1 
ATOM 2122 C CG  . ASN B 1 385 ? 178.941 141.657 200.507 1.00 59.53  ? 385 ASN A CG  1 
ATOM 2123 O OD1 . ASN B 1 385 ? 180.029 141.672 201.081 1.00 63.01  ? 385 ASN A OD1 1 
ATOM 2124 N ND2 . ASN B 1 385 ? 177.788 141.751 201.158 1.00 60.69  ? 385 ASN A ND2 1 
ATOM 2125 N N   . ASP B 1 386 ? 179.131 142.419 195.879 1.00 70.30  ? 386 ASP A N   1 
ATOM 2126 C CA  . ASP B 1 386 ? 179.263 141.852 194.543 1.00 76.33  ? 386 ASP A CA  1 
ATOM 2127 C C   . ASP B 1 386 ? 179.962 142.775 193.545 1.00 75.61  ? 386 ASP A C   1 
ATOM 2128 O O   . ASP B 1 386 ? 180.018 142.449 192.355 1.00 82.00  ? 386 ASP A O   1 
ATOM 2129 C CB  . ASP B 1 386 ? 177.887 141.416 194.015 1.00 81.44  ? 386 ASP A CB  1 
ATOM 2130 C CG  . ASP B 1 386 ? 176.894 142.566 193.873 1.00 84.96  ? 386 ASP A CG  1 
ATOM 2131 O OD1 . ASP B 1 386 ? 177.216 143.720 194.218 1.00 81.55  ? 386 ASP A OD1 1 
ATOM 2132 O OD2 . ASP B 1 386 ? 175.765 142.304 193.410 1.00 84.89  ? 386 ASP A OD2 1 
ATOM 2133 N N   . LEU B 1 387 ? 180.493 143.908 193.994 1.00 66.86  ? 387 LEU A N   1 
ATOM 2134 C CA  . LEU B 1 387 ? 181.351 144.751 193.175 1.00 68.59  ? 387 LEU A CA  1 
ATOM 2135 C C   . LEU B 1 387 ? 182.678 144.927 193.896 1.00 68.70  ? 387 LEU A C   1 
ATOM 2136 O O   . LEU B 1 387 ? 182.778 144.693 195.104 1.00 69.34  ? 387 LEU A O   1 
ATOM 2137 C CB  . LEU B 1 387 ? 180.699 146.116 192.875 1.00 70.49  ? 387 LEU A CB  1 
ATOM 2138 C CG  . LEU B 1 387 ? 180.309 147.130 193.962 1.00 68.07  ? 387 LEU A CG  1 
ATOM 2139 C CD1 . LEU B 1 387 ? 181.450 148.041 194.431 1.00 65.11  ? 387 LEU A CD1 1 
ATOM 2140 C CD2 . LEU B 1 387 ? 179.132 147.964 193.480 1.00 67.61  ? 387 LEU A CD2 1 
ATOM 2141 N N   . CYS B 1 388 ? 183.707 145.342 193.162 1.00 66.54  ? 388 CYS A N   1 
ATOM 2142 C CA  . CYS B 1 388 ? 184.991 145.514 193.816 1.00 65.64  ? 388 CYS A CA  1 
ATOM 2143 C C   . CYS B 1 388 ? 185.764 146.660 193.179 1.00 75.40  ? 388 CYS A C   1 
ATOM 2144 O O   . CYS B 1 388 ? 185.322 147.283 192.210 1.00 80.55  ? 388 CYS A O   1 
ATOM 2145 C CB  . CYS B 1 388 ? 185.776 144.207 193.827 1.00 68.09  ? 388 CYS A CB  1 
ATOM 2146 S SG  . CYS B 1 388 ? 186.782 143.656 192.444 1.00 97.41  ? 388 CYS A SG  1 
ATOM 2147 N N   . PHE B 1 389 ? 186.932 146.922 193.746 1.00 77.53  ? 389 PHE A N   1 
ATOM 2148 C CA  . PHE B 1 389 ? 187.561 148.239 193.740 1.00 73.50  ? 389 PHE A CA  1 
ATOM 2149 C C   . PHE B 1 389 ? 189.004 148.092 194.217 1.00 69.04  ? 389 PHE A C   1 
ATOM 2150 O O   . PHE B 1 389 ? 189.517 146.976 194.365 1.00 72.61  ? 389 PHE A O   1 
ATOM 2151 C CB  . PHE B 1 389 ? 186.734 149.207 194.589 1.00 67.18  ? 389 PHE A CB  1 
ATOM 2152 C CG  . PHE B 1 389 ? 186.612 148.797 196.034 1.00 62.05  ? 389 PHE A CG  1 
ATOM 2153 C CD1 . PHE B 1 389 ? 187.533 149.204 196.980 1.00 66.95  ? 389 PHE A CD1 1 
ATOM 2154 C CD2 . PHE B 1 389 ? 185.543 148.015 196.444 1.00 60.48  ? 389 PHE A CD2 1 
ATOM 2155 C CE1 . PHE B 1 389 ? 187.401 148.818 198.299 1.00 68.98  ? 389 PHE A CE1 1 
ATOM 2156 C CE2 . PHE B 1 389 ? 185.406 147.630 197.759 1.00 54.92  ? 389 PHE A CE2 1 
ATOM 2157 C CZ  . PHE B 1 389 ? 186.336 148.032 198.690 1.00 61.46  ? 389 PHE A CZ  1 
ATOM 2158 N N   . THR B 1 390 ? 189.660 149.227 194.458 1.00 67.42  ? 390 THR A N   1 
ATOM 2159 C CA  . THR B 1 390 ? 191.050 149.267 194.888 1.00 71.13  ? 390 THR A CA  1 
ATOM 2160 C C   . THR B 1 390 ? 191.202 150.298 196.000 1.00 74.98  ? 390 THR A C   1 
ATOM 2161 O O   . THR B 1 390 ? 190.228 150.938 196.412 1.00 76.42  ? 390 THR A O   1 
ATOM 2162 C CB  . THR B 1 390 ? 191.984 149.603 193.722 1.00 75.50  ? 390 THR A CB  1 
ATOM 2163 O OG1 . THR B 1 390 ? 193.342 149.591 194.177 1.00 76.81  ? 390 THR A OG1 1 
ATOM 2164 C CG2 . THR B 1 390 ? 191.654 150.978 193.173 1.00 74.98  ? 390 THR A CG2 1 
ATOM 2165 N N   . ASN B 1 391 ? 192.439 150.396 196.514 1.00 73.64  ? 391 ASN A N   1 
ATOM 2166 C CA  . ASN B 1 391 ? 193.005 151.403 197.424 1.00 63.10  ? 391 ASN A CA  1 
ATOM 2167 C C   . ASN B 1 391 ? 192.042 151.985 198.460 1.00 60.12  ? 391 ASN A C   1 
ATOM 2168 O O   . ASN B 1 391 ? 191.893 153.206 198.571 1.00 62.22  ? 391 ASN A O   1 
ATOM 2169 C CB  . ASN B 1 391 ? 193.719 152.520 196.622 1.00 60.92  ? 391 ASN A CB  1 
ATOM 2170 C CG  . ASN B 1 391 ? 192.799 153.362 195.722 1.00 69.10  ? 391 ASN A CG  1 
ATOM 2171 O OD1 . ASN B 1 391 ? 191.578 153.258 195.742 1.00 73.31  ? 391 ASN A OD1 1 
ATOM 2172 N ND2 . ASN B 1 391 ? 193.420 154.221 194.922 1.00 69.86  ? 391 ASN A ND2 1 
ATOM 2173 N N   . VAL B 1 392 ? 191.421 151.122 199.255 1.00 56.27  ? 392 VAL A N   1 
ATOM 2174 C CA  . VAL B 1 392 ? 190.450 151.575 200.244 1.00 61.31  ? 392 VAL A CA  1 
ATOM 2175 C C   . VAL B 1 392 ? 191.174 152.175 201.445 1.00 62.01  ? 392 VAL A C   1 
ATOM 2176 O O   . VAL B 1 392 ? 192.228 151.689 201.876 1.00 62.57  ? 392 VAL A O   1 
ATOM 2177 C CB  . VAL B 1 392 ? 189.497 150.426 200.635 1.00 62.21  ? 392 VAL A CB  1 
ATOM 2178 C CG1 . VAL B 1 392 ? 190.218 149.296 201.338 1.00 62.25  ? 392 VAL A CG1 1 
ATOM 2179 C CG2 . VAL B 1 392 ? 188.338 150.939 201.484 1.00 63.32  ? 392 VAL A CG2 1 
ATOM 2180 N N   . TYR B 1 393 ? 190.631 153.279 201.952 1.00 57.83  ? 393 TYR A N   1 
ATOM 2181 C CA  . TYR B 1 393 ? 191.176 153.996 203.095 1.00 51.06  ? 393 TYR A CA  1 
ATOM 2182 C C   . TYR B 1 393 ? 190.124 154.013 204.193 1.00 51.56  ? 393 TYR A C   1 
ATOM 2183 O O   . TYR B 1 393 ? 188.968 154.365 203.937 1.00 56.80  ? 393 TYR A O   1 
ATOM 2184 C CB  . TYR B 1 393 ? 191.540 155.436 202.723 1.00 56.55  ? 393 TYR A CB  1 
ATOM 2185 C CG  . TYR B 1 393 ? 192.815 155.605 201.929 1.00 59.79  ? 393 TYR A CG  1 
ATOM 2186 C CD1 . TYR B 1 393 ? 193.873 154.720 202.065 1.00 60.28  ? 393 TYR A CD1 1 
ATOM 2187 C CD2 . TYR B 1 393 ? 192.956 156.664 201.040 1.00 62.04  ? 393 TYR A CD2 1 
ATOM 2188 C CE1 . TYR B 1 393 ? 195.037 154.885 201.332 1.00 63.93  ? 393 TYR A CE1 1 
ATOM 2189 C CE2 . TYR B 1 393 ? 194.113 156.836 200.308 1.00 63.88  ? 393 TYR A CE2 1 
ATOM 2190 C CZ  . TYR B 1 393 ? 195.150 155.944 200.458 1.00 68.40  ? 393 TYR A CZ  1 
ATOM 2191 O OH  . TYR B 1 393 ? 196.306 156.110 199.730 1.00 71.71  ? 393 TYR A OH  1 
ATOM 2192 N N   . ALA B 1 394 ? 190.515 153.637 205.406 1.00 47.30  ? 394 ALA A N   1 
ATOM 2193 C CA  . ALA B 1 394 ? 189.636 153.718 206.565 1.00 45.06  ? 394 ALA A CA  1 
ATOM 2194 C C   . ALA B 1 394 ? 190.257 154.641 207.601 1.00 43.21  ? 394 ALA A C   1 
ATOM 2195 O O   . ALA B 1 394 ? 191.433 154.489 207.946 1.00 49.27  ? 394 ALA A O   1 
ATOM 2196 C CB  . ALA B 1 394 ? 189.384 152.341 207.177 1.00 43.73  ? 394 ALA A CB  1 
ATOM 2197 N N   . ASP B 1 395 ? 189.469 155.593 208.093 1.00 37.79  ? 395 ASP A N   1 
ATOM 2198 C CA  . ASP B 1 395 ? 189.933 156.498 209.132 1.00 37.49  ? 395 ASP A CA  1 
ATOM 2199 C C   . ASP B 1 395 ? 188.850 156.706 210.185 1.00 34.14  ? 395 ASP A C   1 
ATOM 2200 O O   . ASP B 1 395 ? 187.654 156.624 209.897 1.00 39.13  ? 395 ASP A O   1 
ATOM 2201 C CB  . ASP B 1 395 ? 190.459 157.818 208.521 1.00 43.35  ? 395 ASP A CB  1 
ATOM 2202 C CG  . ASP B 1 395 ? 189.401 158.617 207.773 1.00 51.69  ? 395 ASP A CG  1 
ATOM 2203 O OD1 . ASP B 1 395 ? 188.241 158.182 207.654 1.00 53.73  ? 395 ASP A OD1 1 
ATOM 2204 O OD2 . ASP B 1 395 ? 189.754 159.704 207.273 1.00 53.82  ? 395 ASP A OD2 1 
ATOM 2205 N N   . SER B 1 396 ? 189.288 156.941 211.423 1.00 30.13  ? 396 SER A N   1 
ATOM 2206 C CA  . SER B 1 396 ? 188.394 156.932 212.572 1.00 30.06  ? 396 SER A CA  1 
ATOM 2207 C C   . SER B 1 396 ? 188.685 158.108 213.494 1.00 33.87  ? 396 SER A C   1 
ATOM 2208 O O   . SER B 1 396 ? 189.834 158.534 213.640 1.00 40.16  ? 396 SER A O   1 
ATOM 2209 C CB  . SER B 1 396 ? 188.515 155.621 213.358 1.00 33.29  ? 396 SER A CB  1 
ATOM 2210 O OG  . SER B 1 396 ? 189.796 155.500 213.948 1.00 39.91  ? 396 SER A OG  1 
ATOM 2211 N N   . PHE B 1 397 ? 187.626 158.614 214.127 1.00 32.22  ? 397 PHE A N   1 
ATOM 2212 C CA  . PHE B 1 397 ? 187.700 159.722 215.072 1.00 31.60  ? 397 PHE A CA  1 
ATOM 2213 C C   . PHE B 1 397 ? 186.413 159.755 215.891 1.00 32.00  ? 397 PHE A C   1 
ATOM 2214 O O   . PHE B 1 397 ? 185.453 159.039 215.599 1.00 36.54  ? 397 PHE A O   1 
ATOM 2215 C CB  . PHE B 1 397 ? 187.952 161.058 214.359 1.00 32.54  ? 397 PHE A CB  1 
ATOM 2216 C CG  . PHE B 1 397 ? 187.127 161.261 213.118 1.00 32.42  ? 397 PHE A CG  1 
ATOM 2217 C CD1 . PHE B 1 397 ? 185.883 161.851 213.189 1.00 33.08  ? 397 PHE A CD1 1 
ATOM 2218 C CD2 . PHE B 1 397 ? 187.621 160.909 211.873 1.00 36.22  ? 397 PHE A CD2 1 
ATOM 2219 C CE1 . PHE B 1 397 ? 185.130 162.052 212.054 1.00 34.56  ? 397 PHE A CE1 1 
ATOM 2220 C CE2 . PHE B 1 397 ? 186.871 161.107 210.733 1.00 38.01  ? 397 PHE A CE2 1 
ATOM 2221 C CZ  . PHE B 1 397 ? 185.624 161.681 210.825 1.00 36.97  ? 397 PHE A CZ  1 
ATOM 2222 N N   . VAL B 1 398 ? 186.406 160.595 216.928 1.00 29.72  ? 398 VAL A N   1 
ATOM 2223 C CA  . VAL B 1 398 ? 185.297 160.677 217.879 1.00 30.57  ? 398 VAL A CA  1 
ATOM 2224 C C   . VAL B 1 398 ? 184.858 162.134 217.979 1.00 34.31  ? 398 VAL A C   1 
ATOM 2225 O O   . VAL B 1 398 ? 185.656 162.998 218.360 1.00 40.92  ? 398 VAL A O   1 
ATOM 2226 C CB  . VAL B 1 398 ? 185.694 160.134 219.264 1.00 33.25  ? 398 VAL A CB  1 
ATOM 2227 C CG1 . VAL B 1 398 ? 184.757 160.646 220.351 1.00 29.57  ? 398 VAL A CG1 1 
ATOM 2228 C CG2 . VAL B 1 398 ? 185.750 158.622 219.250 1.00 36.91  ? 398 VAL A CG2 1 
ATOM 2229 N N   . ILE B 1 399 ? 183.591 162.406 217.661 1.00 32.18  ? 399 ILE A N   1 
ATOM 2230 C CA  . ILE B 1 399 ? 183.086 163.769 217.544 1.00 33.35  ? 399 ILE A CA  1 
ATOM 2231 C C   . ILE B 1 399 ? 181.883 163.972 218.460 1.00 36.30  ? 399 ILE A C   1 
ATOM 2232 O O   . ILE B 1 399 ? 181.349 163.036 219.055 1.00 38.78  ? 399 ILE A O   1 
ATOM 2233 C CB  . ILE B 1 399 ? 182.715 164.137 216.094 1.00 33.24  ? 399 ILE A CB  1 
ATOM 2234 C CG1 . ILE B 1 399 ? 181.502 163.330 215.629 1.00 37.32  ? 399 ILE A CG1 1 
ATOM 2235 C CG2 . ILE B 1 399 ? 183.895 163.971 215.167 1.00 35.11  ? 399 ILE A CG2 1 
ATOM 2236 C CD1 . ILE B 1 399 ? 181.143 163.561 214.182 1.00 42.16  ? 399 ILE A CD1 1 
ATOM 2237 N N   . LYS B 1 400 ? 181.470 165.234 218.561 1.00 40.08  ? 400 LYS A N   1 
ATOM 2238 C CA  . LYS B 1 400 ? 180.298 165.643 219.319 1.00 39.45  ? 400 LYS A CA  1 
ATOM 2239 C C   . LYS B 1 400 ? 179.027 165.232 218.567 1.00 41.51  ? 400 LYS A C   1 
ATOM 2240 O O   . LYS B 1 400 ? 179.045 164.982 217.358 1.00 43.55  ? 400 LYS A O   1 
ATOM 2241 C CB  . LYS B 1 400 ? 180.352 167.161 219.561 1.00 40.74  ? 400 LYS A CB  1 
ATOM 2242 C CG  . LYS B 1 400 ? 179.280 167.765 220.468 1.00 41.57  ? 400 LYS A CG  1 
ATOM 2243 C CD  . LYS B 1 400 ? 179.395 169.279 220.566 1.00 50.98  ? 400 LYS A CD  1 
ATOM 2244 C CE  . LYS B 1 400 ? 180.574 169.704 221.422 1.00 51.06  ? 400 LYS A CE  1 
ATOM 2245 N NZ  . LYS B 1 400 ? 180.614 171.182 221.610 1.00 49.36  ? 400 LYS A NZ  1 
ATOM 2246 N N   . GLY B 1 401 ? 177.917 165.144 219.309 1.00 42.47  ? 401 GLY A N   1 
ATOM 2247 C CA  . GLY B 1 401 ? 176.677 164.644 218.736 1.00 36.71  ? 401 GLY A CA  1 
ATOM 2248 C C   . GLY B 1 401 ? 176.084 165.521 217.650 1.00 35.19  ? 401 GLY A C   1 
ATOM 2249 O O   . GLY B 1 401 ? 175.629 165.019 216.620 1.00 36.34  ? 401 GLY A O   1 
ATOM 2250 N N   . ASN B 1 402 ? 176.078 166.834 217.856 1.00 36.23  ? 402 ASN A N   1 
ATOM 2251 C CA  . ASN B 1 402 ? 175.482 167.736 216.879 1.00 40.66  ? 402 ASN A CA  1 
ATOM 2252 C C   . ASN B 1 402 ? 176.401 168.032 215.698 1.00 44.92  ? 402 ASN A C   1 
ATOM 2253 O O   . ASN B 1 402 ? 176.040 168.847 214.843 1.00 48.20  ? 402 ASN A O   1 
ATOM 2254 C CB  . ASN B 1 402 ? 175.015 169.025 217.585 1.00 42.52  ? 402 ASN A CB  1 
ATOM 2255 C CG  . ASN B 1 402 ? 176.158 169.957 217.993 1.00 49.12  ? 402 ASN A CG  1 
ATOM 2256 O OD1 . ASN B 1 402 ? 176.861 170.533 217.161 1.00 53.08  ? 402 ASN A OD1 1 
ATOM 2257 N ND2 . ASN B 1 402 ? 176.335 170.113 219.299 1.00 45.66  ? 402 ASN A ND2 1 
ATOM 2258 N N   . GLU B 1 403 ? 177.571 167.398 215.631 1.00 42.46  ? 403 GLU A N   1 
ATOM 2259 C CA  . GLU B 1 403 ? 178.528 167.613 214.556 1.00 43.12  ? 403 GLU A CA  1 
ATOM 2260 C C   . GLU B 1 403 ? 178.606 166.435 213.592 1.00 48.47  ? 403 GLU A C   1 
ATOM 2261 O O   . GLU B 1 403 ? 179.478 166.422 212.717 1.00 54.91  ? 403 GLU A O   1 
ATOM 2262 C CB  . GLU B 1 403 ? 179.910 167.902 215.143 1.00 44.36  ? 403 GLU A CB  1 
ATOM 2263 C CG  . GLU B 1 403 ? 180.061 169.305 215.699 1.00 56.19  ? 403 GLU A CG  1 
ATOM 2264 C CD  . GLU B 1 403 ? 181.245 169.433 216.634 1.00 61.53  ? 403 GLU A CD  1 
ATOM 2265 O OE1 . GLU B 1 403 ? 181.954 168.426 216.836 1.00 60.05  ? 403 GLU A OE1 1 
ATOM 2266 O OE2 . GLU B 1 403 ? 181.462 170.539 217.172 1.00 59.45  ? 403 GLU A OE2 1 
ATOM 2267 N N   . VAL B 1 404 ? 177.725 165.442 213.740 1.00 47.26  ? 404 VAL A N   1 
ATOM 2268 C CA  . VAL B 1 404 ? 177.757 164.268 212.872 1.00 42.03  ? 404 VAL A CA  1 
ATOM 2269 C C   . VAL B 1 404 ? 177.337 164.629 211.452 1.00 44.59  ? 404 VAL A C   1 
ATOM 2270 O O   . VAL B 1 404 ? 177.905 164.117 210.478 1.00 47.14  ? 404 VAL A O   1 
ATOM 2271 C CB  . VAL B 1 404 ? 176.879 163.152 213.471 1.00 42.34  ? 404 VAL A CB  1 
ATOM 2272 C CG1 . VAL B 1 404 ? 176.825 161.936 212.556 1.00 46.04  ? 404 VAL A CG1 1 
ATOM 2273 C CG2 . VAL B 1 404 ? 177.396 162.759 214.842 1.00 43.16  ? 404 VAL A CG2 1 
ATOM 2274 N N   . SER B 1 405 ? 176.372 165.539 211.305 1.00 47.38  ? 405 SER A N   1 
ATOM 2275 C CA  . SER B 1 405 ? 175.888 165.945 209.990 1.00 50.54  ? 405 SER A CA  1 
ATOM 2276 C C   . SER B 1 405 ? 176.918 166.730 209.187 1.00 51.38  ? 405 SER A C   1 
ATOM 2277 O O   . SER B 1 405 ? 176.722 166.919 207.982 1.00 55.17  ? 405 SER A O   1 
ATOM 2278 C CB  . SER B 1 405 ? 174.614 166.776 210.140 1.00 50.58  ? 405 SER A CB  1 
ATOM 2279 O OG  . SER B 1 405 ? 173.566 166.005 210.700 1.00 53.85  ? 405 SER A OG  1 
ATOM 2280 N N   . GLN B 1 406 ? 178.001 167.190 209.814 1.00 47.75  ? 406 GLN A N   1 
ATOM 2281 C CA  . GLN B 1 406 ? 179.062 167.882 209.097 1.00 51.28  ? 406 GLN A CA  1 
ATOM 2282 C C   . GLN B 1 406 ? 180.000 166.938 208.361 1.00 54.91  ? 406 GLN A C   1 
ATOM 2283 O O   . GLN B 1 406 ? 180.760 167.397 207.502 1.00 62.69  ? 406 GLN A O   1 
ATOM 2284 C CB  . GLN B 1 406 ? 179.873 168.748 210.062 1.00 52.70  ? 406 GLN A CB  1 
ATOM 2285 C CG  . GLN B 1 406 ? 179.183 170.032 210.470 1.00 62.36  ? 406 GLN A CG  1 
ATOM 2286 C CD  . GLN B 1 406 ? 180.048 170.890 211.366 1.00 64.43  ? 406 GLN A CD  1 
ATOM 2287 O OE1 . GLN B 1 406 ? 181.254 171.006 211.156 1.00 64.90  ? 406 GLN A OE1 1 
ATOM 2288 N NE2 . GLN B 1 406 ? 179.435 171.501 212.373 1.00 68.03  ? 406 GLN A NE2 1 
ATOM 2289 N N   . ILE B 1 407 ? 179.972 165.644 208.665 1.00 54.16  ? 407 ILE A N   1 
ATOM 2290 C CA  . ILE B 1 407 ? 180.823 164.673 207.957 1.00 55.82  ? 407 ILE A CA  1 
ATOM 2291 C C   . ILE B 1 407 ? 180.026 164.254 206.728 1.00 64.61  ? 407 ILE A C   1 
ATOM 2292 O O   . ILE B 1 407 ? 179.309 163.248 206.704 1.00 63.82  ? 407 ILE A O   1 
ATOM 2293 C CB  . ILE B 1 407 ? 181.229 163.495 208.851 1.00 50.74  ? 407 ILE A CB  1 
ATOM 2294 C CG1 . ILE B 1 407 ? 182.053 163.994 210.037 1.00 46.26  ? 407 ILE A CG1 1 
ATOM 2295 C CG2 . ILE B 1 407 ? 182.085 162.497 208.080 1.00 45.78  ? 407 ILE A CG2 1 
ATOM 2296 C CD1 . ILE B 1 407 ? 183.325 164.708 209.644 1.00 47.85  ? 407 ILE A CD1 1 
ATOM 2297 N N   . ALA B 1 408 ? 180.138 165.070 205.678 1.00 67.78  ? 408 ALA A N   1 
ATOM 2298 C CA  . ALA B 1 408 ? 179.425 164.926 204.416 1.00 64.31  ? 408 ALA A CA  1 
ATOM 2299 C C   . ALA B 1 408 ? 180.044 165.872 203.395 1.00 66.59  ? 408 ALA A C   1 
ATOM 2300 O O   . ALA B 1 408 ? 180.615 166.903 203.777 1.00 71.41  ? 408 ALA A O   1 
ATOM 2301 C CB  . ALA B 1 408 ? 177.932 165.223 204.587 1.00 60.79  ? 408 ALA A CB  1 
ATOM 2302 N N   . PRO B 1 409 ? 179.974 165.558 202.101 1.00 62.84  ? 409 PRO A N   1 
ATOM 2303 C CA  . PRO B 1 409 ? 180.514 166.471 201.081 1.00 64.92  ? 409 PRO A CA  1 
ATOM 2304 C C   . PRO B 1 409 ? 179.690 167.747 200.979 1.00 69.20  ? 409 PRO A C   1 
ATOM 2305 O O   . PRO B 1 409 ? 178.479 167.701 200.752 1.00 71.07  ? 409 PRO A O   1 
ATOM 2306 C CB  . PRO B 1 409 ? 180.429 165.645 199.793 1.00 67.42  ? 409 PRO A CB  1 
ATOM 2307 C CG  . PRO B 1 409 ? 180.465 164.236 200.254 1.00 64.45  ? 409 PRO A CG  1 
ATOM 2308 C CD  . PRO B 1 409 ? 179.709 164.220 201.547 1.00 60.76  ? 409 PRO A CD  1 
ATOM 2309 N N   . GLY B 1 410 ? 180.355 168.887 201.138 1.00 68.17  ? 410 GLY A N   1 
ATOM 2310 C CA  . GLY B 1 410 ? 179.728 170.171 200.894 1.00 69.81  ? 410 GLY A CA  1 
ATOM 2311 C C   . GLY B 1 410 ? 179.155 170.885 202.096 1.00 76.59  ? 410 GLY A C   1 
ATOM 2312 O O   . GLY B 1 410 ? 178.407 171.852 201.918 1.00 81.64  ? 410 GLY A O   1 
ATOM 2313 N N   . GLN B 1 411 ? 179.476 170.453 203.310 1.00 77.21  ? 411 GLN A N   1 
ATOM 2314 C CA  . GLN B 1 411 ? 179.013 171.126 204.515 1.00 75.10  ? 411 GLN A CA  1 
ATOM 2315 C C   . GLN B 1 411 ? 180.114 172.006 205.097 1.00 75.10  ? 411 GLN A C   1 
ATOM 2316 O O   . GLN B 1 411 ? 181.283 171.929 204.711 1.00 77.24  ? 411 GLN A O   1 
ATOM 2317 C CB  . GLN B 1 411 ? 178.533 170.109 205.557 1.00 68.83  ? 411 GLN A CB  1 
ATOM 2318 C CG  . GLN B 1 411 ? 177.086 169.645 205.393 1.00 71.47  ? 411 GLN A CG  1 
ATOM 2319 C CD  . GLN B 1 411 ? 176.874 168.654 204.257 1.00 75.62  ? 411 GLN A CD  1 
ATOM 2320 O OE1 . GLN B 1 411 ? 177.786 168.353 203.488 1.00 77.59  ? 411 GLN A OE1 1 
ATOM 2321 N NE2 . GLN B 1 411 ? 175.654 168.141 204.152 1.00 75.78  ? 411 GLN A NE2 1 
ATOM 2322 N N   . THR B 1 412 ? 179.719 172.856 206.041 1.00 74.72  ? 412 THR A N   1 
ATOM 2323 C CA  . THR B 1 412 ? 180.633 173.767 206.710 1.00 76.01  ? 412 THR A CA  1 
ATOM 2324 C C   . THR B 1 412 ? 180.389 173.722 208.213 1.00 75.39  ? 412 THR A C   1 
ATOM 2325 O O   . THR B 1 412 ? 179.363 173.226 208.685 1.00 78.94  ? 412 THR A O   1 
ATOM 2326 C CB  . THR B 1 412 ? 180.487 175.206 206.188 1.00 74.83  ? 412 THR A CB  1 
ATOM 2327 O OG1 . THR B 1 412 ? 181.633 175.976 206.571 1.00 76.61  ? 412 THR A OG1 1 
ATOM 2328 C CG2 . THR B 1 412 ? 179.229 175.864 206.740 1.00 71.82  ? 412 THR A CG2 1 
ATOM 2329 N N   . GLY B 1 413 ? 181.355 174.231 208.958 1.00 69.56  ? 413 GLY A N   1 
ATOM 2330 C CA  . GLY B 1 413 ? 181.293 174.224 210.403 1.00 66.15  ? 413 GLY A CA  1 
ATOM 2331 C C   . GLY B 1 413 ? 182.694 174.236 210.981 1.00 71.26  ? 413 GLY A C   1 
ATOM 2332 O O   . GLY B 1 413 ? 183.669 174.487 210.282 1.00 75.55  ? 413 GLY A O   1 
ATOM 2333 N N   . ASN B 1 414 ? 182.771 173.965 212.285 1.00 69.56  ? 414 ASN A N   1 
ATOM 2334 C CA  . ASN B 1 414 ? 184.071 173.935 212.947 1.00 65.74  ? 414 ASN A CA  1 
ATOM 2335 C C   . ASN B 1 414 ? 184.855 172.686 212.559 1.00 61.03  ? 414 ASN A C   1 
ATOM 2336 O O   . ASN B 1 414 ? 186.059 172.761 212.287 1.00 62.55  ? 414 ASN A O   1 
ATOM 2337 C CB  . ASN B 1 414 ? 183.887 174.012 214.463 1.00 66.18  ? 414 ASN A CB  1 
ATOM 2338 C CG  . ASN B 1 414 ? 185.130 174.508 215.184 1.00 67.86  ? 414 ASN A CG  1 
ATOM 2339 O OD1 . ASN B 1 414 ? 186.245 174.420 214.670 1.00 65.99  ? 414 ASN A OD1 1 
ATOM 2340 N ND2 . ASN B 1 414 ? 184.938 175.035 216.388 1.00 66.40  ? 414 ASN A ND2 1 
ATOM 2341 N N   . ILE B 1 415 ? 184.189 171.531 212.534 1.00 61.24  ? 415 ILE A N   1 
ATOM 2342 C CA  . ILE B 1 415 ? 184.857 170.286 212.168 1.00 56.33  ? 415 ILE A CA  1 
ATOM 2343 C C   . ILE B 1 415 ? 185.166 170.264 210.676 1.00 58.42  ? 415 ILE A C   1 
ATOM 2344 O O   . ILE B 1 415 ? 186.283 169.937 210.258 1.00 57.55  ? 415 ILE A O   1 
ATOM 2345 C CB  . ILE B 1 415 ? 183.992 169.080 212.580 1.00 52.46  ? 415 ILE A CB  1 
ATOM 2346 C CG1 . ILE B 1 415 ? 183.850 169.003 214.101 1.00 52.91  ? 415 ILE A CG1 1 
ATOM 2347 C CG2 . ILE B 1 415 ? 184.574 167.785 212.036 1.00 56.14  ? 415 ILE A CG2 1 
ATOM 2348 C CD1 . ILE B 1 415 ? 185.151 169.085 214.857 1.00 53.62  ? 415 ILE A CD1 1 
ATOM 2349 N N   . ALA B 1 416 ? 184.184 170.633 209.851 1.00 63.82  ? 416 ALA A N   1 
ATOM 2350 C CA  . ALA B 1 416 ? 184.287 170.475 208.406 1.00 62.50  ? 416 ALA A CA  1 
ATOM 2351 C C   . ALA B 1 416 ? 185.220 171.482 207.747 1.00 64.71  ? 416 ALA A C   1 
ATOM 2352 O O   . ALA B 1 416 ? 185.535 171.317 206.565 1.00 70.99  ? 416 ALA A O   1 
ATOM 2353 C CB  . ALA B 1 416 ? 182.900 170.575 207.771 1.00 62.94  ? 416 ALA A CB  1 
ATOM 2354 N N   . ASP B 1 417 ? 185.669 172.510 208.462 1.00 64.12  ? 417 ASP A N   1 
ATOM 2355 C CA  . ASP B 1 417 ? 186.552 173.513 207.883 1.00 67.07  ? 417 ASP A CA  1 
ATOM 2356 C C   . ASP B 1 417 ? 187.946 173.522 208.485 1.00 67.88  ? 417 ASP A C   1 
ATOM 2357 O O   . ASP B 1 417 ? 188.883 173.984 207.830 1.00 73.63  ? 417 ASP A O   1 
ATOM 2358 C CB  . ASP B 1 417 ? 185.945 174.913 208.036 1.00 71.02  ? 417 ASP A CB  1 
ATOM 2359 C CG  . ASP B 1 417 ? 184.648 175.075 207.269 1.00 78.17  ? 417 ASP A CG  1 
ATOM 2360 O OD1 . ASP B 1 417 ? 184.342 174.210 206.422 1.00 81.30  ? 417 ASP A OD1 1 
ATOM 2361 O OD2 . ASP B 1 417 ? 183.934 176.070 207.513 1.00 76.70  ? 417 ASP A OD2 1 
ATOM 2362 N N   . TYR B 1 418 ? 188.108 173.022 209.707 1.00 66.40  ? 418 TYR A N   1 
ATOM 2363 C CA  . TYR B 1 418 ? 189.379 173.090 210.409 1.00 64.21  ? 418 TYR A CA  1 
ATOM 2364 C C   . TYR B 1 418 ? 189.925 171.728 210.805 1.00 58.41  ? 418 TYR A C   1 
ATOM 2365 O O   . TYR B 1 418 ? 191.111 171.632 211.137 1.00 58.18  ? 418 TYR A O   1 
ATOM 2366 C CB  . TYR B 1 418 ? 189.253 173.951 211.680 1.00 65.44  ? 418 TYR A CB  1 
ATOM 2367 C CG  . TYR B 1 418 ? 188.920 175.417 211.459 1.00 72.11  ? 418 TYR A CG  1 
ATOM 2368 C CD1 . TYR B 1 418 ? 187.654 175.822 211.050 1.00 75.11  ? 418 TYR A CD1 1 
ATOM 2369 C CD2 . TYR B 1 418 ? 189.874 176.396 211.678 1.00 71.27  ? 418 TYR A CD2 1 
ATOM 2370 C CE1 . TYR B 1 418 ? 187.360 177.157 210.851 1.00 78.13  ? 418 TYR A CE1 1 
ATOM 2371 C CE2 . TYR B 1 418 ? 189.591 177.733 211.482 1.00 71.93  ? 418 TYR A CE2 1 
ATOM 2372 C CZ  . TYR B 1 418 ? 188.332 178.108 211.070 1.00 81.04  ? 418 TYR A CZ  1 
ATOM 2373 O OH  . TYR B 1 418 ? 188.045 179.439 210.877 1.00 89.53  ? 418 TYR A OH  1 
ATOM 2374 N N   . ASN B 1 419 ? 189.104 170.681 210.786 1.00 53.89  ? 419 ASN A N   1 
ATOM 2375 C CA  . ASN B 1 419 ? 189.501 169.393 211.336 1.00 52.42  ? 419 ASN A CA  1 
ATOM 2376 C C   . ASN B 1 419 ? 189.468 168.266 210.309 1.00 53.91  ? 419 ASN A C   1 
ATOM 2377 O O   . ASN B 1 419 ? 190.426 167.496 210.197 1.00 52.35  ? 419 ASN A O   1 
ATOM 2378 C CB  . ASN B 1 419 ? 188.602 169.058 212.522 1.00 51.93  ? 419 ASN A CB  1 
ATOM 2379 C CG  . ASN B 1 419 ? 188.758 170.039 213.662 1.00 56.17  ? 419 ASN A CG  1 
ATOM 2380 O OD1 . ASN B 1 419 ? 187.831 170.774 213.998 1.00 58.72  ? 419 ASN A OD1 1 
ATOM 2381 N ND2 . ASN B 1 419 ? 189.932 170.045 214.276 1.00 56.46  ? 419 ASN A ND2 1 
ATOM 2382 N N   . TYR B 1 420 ? 188.373 168.153 209.562 1.00 54.23  ? 420 TYR A N   1 
ATOM 2383 C CA  . TYR B 1 420 ? 188.203 167.048 208.625 1.00 54.66  ? 420 TYR A CA  1 
ATOM 2384 C C   . TYR B 1 420 ? 187.317 167.495 207.475 1.00 63.55  ? 420 TYR A C   1 
ATOM 2385 O O   . TYR B 1 420 ? 186.151 167.838 207.690 1.00 65.06  ? 420 TYR A O   1 
ATOM 2386 C CB  . TYR B 1 420 ? 187.600 165.830 209.324 1.00 51.15  ? 420 TYR A CB  1 
ATOM 2387 C CG  . TYR B 1 420 ? 187.701 164.550 208.530 1.00 53.11  ? 420 TYR A CG  1 
ATOM 2388 C CD1 . TYR B 1 420 ? 188.931 163.958 208.283 1.00 51.78  ? 420 TYR A CD1 1 
ATOM 2389 C CD2 . TYR B 1 420 ? 186.563 163.928 208.037 1.00 51.50  ? 420 TYR A CD2 1 
ATOM 2390 C CE1 . TYR B 1 420 ? 189.024 162.788 207.561 1.00 47.40  ? 420 TYR A CE1 1 
ATOM 2391 C CE2 . TYR B 1 420 ? 186.646 162.759 207.316 1.00 48.26  ? 420 TYR A CE2 1 
ATOM 2392 C CZ  . TYR B 1 420 ? 187.879 162.193 207.081 1.00 46.97  ? 420 TYR A CZ  1 
ATOM 2393 O OH  . TYR B 1 420 ? 187.964 161.026 206.360 1.00 51.69  ? 420 TYR A OH  1 
ATOM 2394 N N   . LYS B 1 421 ? 187.864 167.478 206.263 1.00 62.42  ? 421 LYS A N   1 
ATOM 2395 C CA  . LYS B 1 421 ? 187.139 167.848 205.055 1.00 60.57  ? 421 LYS A CA  1 
ATOM 2396 C C   . LYS B 1 421 ? 187.061 166.657 204.113 1.00 65.50  ? 421 LYS A C   1 
ATOM 2397 O O   . LYS B 1 421 ? 188.069 165.990 203.863 1.00 64.84  ? 421 LYS A O   1 
ATOM 2398 C CB  . LYS B 1 421 ? 187.807 169.028 204.346 1.00 63.62  ? 421 LYS A CB  1 
ATOM 2399 C CG  . LYS B 1 421 ? 187.046 169.525 203.123 1.00 70.62  ? 421 LYS A CG  1 
ATOM 2400 C CD  . LYS B 1 421 ? 186.082 170.644 203.459 1.00 72.40  ? 421 LYS A CD  1 
ATOM 2401 C CE  . LYS B 1 421 ? 184.999 170.769 202.403 1.00 69.20  ? 421 LYS A CE  1 
ATOM 2402 N NZ  . LYS B 1 421 ? 183.949 171.746 202.798 1.00 70.46  ? 421 LYS A NZ  1 
ATOM 2403 N N   . LEU B 1 422 ? 185.864 166.396 203.597 1.00 66.57  ? 422 LEU A N   1 
ATOM 2404 C CA  . LEU B 1 422 ? 185.642 165.436 202.527 1.00 64.75  ? 422 LEU A CA  1 
ATOM 2405 C C   . LEU B 1 422 ? 185.466 166.163 201.201 1.00 66.92  ? 422 LEU A C   1 
ATOM 2406 O O   . LEU B 1 422 ? 184.879 167.250 201.166 1.00 70.56  ? 422 LEU A O   1 
ATOM 2407 C CB  . LEU B 1 422 ? 184.404 164.583 202.805 1.00 58.58  ? 422 LEU A CB  1 
ATOM 2408 C CG  . LEU B 1 422 ? 184.505 163.528 203.906 1.00 52.40  ? 422 LEU A CG  1 
ATOM 2409 C CD1 . LEU B 1 422 ? 183.306 162.601 203.855 1.00 54.37  ? 422 LEU A CD1 1 
ATOM 2410 C CD2 . LEU B 1 422 ? 185.796 162.737 203.772 1.00 56.68  ? 422 LEU A CD2 1 
ATOM 2411 N N   . PRO B 1 423 ? 185.970 165.605 200.103 1.00 61.72  ? 423 PRO A N   1 
ATOM 2412 C CA  . PRO B 1 423 ? 185.804 166.258 198.802 1.00 65.38  ? 423 PRO A CA  1 
ATOM 2413 C C   . PRO B 1 423 ? 184.356 166.216 198.339 1.00 74.69  ? 423 PRO A C   1 
ATOM 2414 O O   . PRO B 1 423 ? 183.543 165.423 198.820 1.00 79.76  ? 423 PRO A O   1 
ATOM 2415 C CB  . PRO B 1 423 ? 186.707 165.441 197.870 1.00 68.11  ? 423 PRO A CB  1 
ATOM 2416 C CG  . PRO B 1 423 ? 187.610 164.663 198.778 1.00 64.11  ? 423 PRO A CG  1 
ATOM 2417 C CD  . PRO B 1 423 ? 186.813 164.404 200.009 1.00 61.20  ? 423 PRO A CD  1 
ATOM 2418 N N   . ASP B 1 424 ? 184.042 167.112 197.399 1.00 74.42  ? 424 ASP A N   1 
ATOM 2419 C CA  . ASP B 1 424 ? 182.690 167.188 196.852 1.00 78.94  ? 424 ASP A CA  1 
ATOM 2420 C C   . ASP B 1 424 ? 182.331 165.899 196.119 1.00 81.47  ? 424 ASP A C   1 
ATOM 2421 O O   . ASP B 1 424 ? 181.222 165.374 196.273 1.00 81.83  ? 424 ASP A O   1 
ATOM 2422 C CB  . ASP B 1 424 ? 182.585 168.402 195.922 1.00 87.27  ? 424 ASP A CB  1 
ATOM 2423 C CG  . ASP B 1 424 ? 181.153 168.714 195.487 1.00 99.60  ? 424 ASP A CG  1 
ATOM 2424 O OD1 . ASP B 1 424 ? 180.206 167.995 195.867 1.00 102.65 ? 424 ASP A OD1 1 
ATOM 2425 O OD2 . ASP B 1 424 ? 180.977 169.704 194.746 1.00 105.31 ? 424 ASP A OD2 1 
ATOM 2426 N N   . ASP B 1 425 ? 183.264 165.362 195.337 1.00 81.61  ? 425 ASP A N   1 
ATOM 2427 C CA  . ASP B 1 425 ? 183.066 164.100 194.626 1.00 83.12  ? 425 ASP A CA  1 
ATOM 2428 C C   . ASP B 1 425 ? 183.670 162.996 195.487 1.00 81.30  ? 425 ASP A C   1 
ATOM 2429 O O   . ASP B 1 425 ? 184.819 162.593 195.301 1.00 79.33  ? 425 ASP A O   1 
ATOM 2430 C CB  . ASP B 1 425 ? 183.694 164.150 193.239 1.00 86.04  ? 425 ASP A CB  1 
ATOM 2431 C CG  . ASP B 1 425 ? 183.149 163.081 192.311 1.00 93.46  ? 425 ASP A CG  1 
ATOM 2432 O OD1 . ASP B 1 425 ? 182.313 162.268 192.759 1.00 93.24  ? 425 ASP A OD1 1 
ATOM 2433 O OD2 . ASP B 1 425 ? 183.554 163.056 191.130 1.00 95.85  ? 425 ASP A OD2 1 
ATOM 2434 N N   . PHE B 1 426 ? 182.882 162.504 196.438 1.00 79.73  ? 426 PHE A N   1 
ATOM 2435 C CA  . PHE B 1 426 ? 183.320 161.499 197.396 1.00 74.75  ? 426 PHE A CA  1 
ATOM 2436 C C   . PHE B 1 426 ? 182.647 160.170 197.089 1.00 74.01  ? 426 PHE A C   1 
ATOM 2437 O O   . PHE B 1 426 ? 181.425 160.114 196.916 1.00 74.94  ? 426 PHE A O   1 
ATOM 2438 C CB  . PHE B 1 426 ? 182.997 161.938 198.826 1.00 65.25  ? 426 PHE A CB  1 
ATOM 2439 C CG  . PHE B 1 426 ? 183.409 160.949 199.874 1.00 59.76  ? 426 PHE A CG  1 
ATOM 2440 C CD1 . PHE B 1 426 ? 184.729 160.557 199.996 1.00 56.41  ? 426 PHE A CD1 1 
ATOM 2441 C CD2 . PHE B 1 426 ? 182.472 160.410 200.742 1.00 62.44  ? 426 PHE A CD2 1 
ATOM 2442 C CE1 . PHE B 1 426 ? 185.109 159.648 200.963 1.00 55.72  ? 426 PHE A CE1 1 
ATOM 2443 C CE2 . PHE B 1 426 ? 182.845 159.500 201.708 1.00 56.24  ? 426 PHE A CE2 1 
ATOM 2444 C CZ  . PHE B 1 426 ? 184.165 159.118 201.819 1.00 54.01  ? 426 PHE A CZ  1 
ATOM 2445 N N   . THR B 1 427 ? 183.444 159.108 197.021 1.00 66.41  ? 427 THR A N   1 
ATOM 2446 C CA  . THR B 1 427 ? 182.952 157.752 196.786 1.00 64.36  ? 427 THR A CA  1 
ATOM 2447 C C   . THR B 1 427 ? 183.301 156.910 198.010 1.00 57.54  ? 427 THR A C   1 
ATOM 2448 O O   . THR B 1 427 ? 184.439 156.453 198.151 1.00 62.54  ? 427 THR A O   1 
ATOM 2449 C CB  . THR B 1 427 ? 183.553 157.156 195.515 1.00 69.49  ? 427 THR A CB  1 
ATOM 2450 O OG1 . THR B 1 427 ? 184.978 157.078 195.649 1.00 74.02  ? 427 THR A OG1 1 
ATOM 2451 C CG2 . THR B 1 427 ? 183.207 158.012 194.307 1.00 67.62  ? 427 THR A CG2 1 
ATOM 2452 N N   . GLY B 1 428 ? 182.327 156.705 198.890 1.00 54.24  ? 428 GLY A N   1 
ATOM 2453 C CA  . GLY B 1 428 ? 182.573 155.925 200.088 1.00 53.84  ? 428 GLY A CA  1 
ATOM 2454 C C   . GLY B 1 428 ? 181.366 155.930 201.005 1.00 55.03  ? 428 GLY A C   1 
ATOM 2455 O O   . GLY B 1 428 ? 180.251 156.236 200.581 1.00 63.77  ? 428 GLY A O   1 
ATOM 2456 N N   . CYS B 1 429 ? 181.612 155.587 202.269 1.00 47.35  ? 429 CYS A N   1 
ATOM 2457 C CA  . CYS B 1 429 ? 180.555 155.443 203.259 1.00 46.01  ? 429 CYS A CA  1 
ATOM 2458 C C   . CYS B 1 429 ? 180.983 156.093 204.567 1.00 43.84  ? 429 CYS A C   1 
ATOM 2459 O O   . CYS B 1 429 ? 182.176 156.227 204.850 1.00 46.59  ? 429 CYS A O   1 
ATOM 2460 C CB  . CYS B 1 429 ? 180.213 153.967 203.497 1.00 48.11  ? 429 CYS A CB  1 
ATOM 2461 S SG  . CYS B 1 429 ? 179.508 153.119 202.065 1.00 78.87  ? 429 CYS A SG  1 
ATOM 2462 N N   . VAL B 1 430 ? 179.994 156.496 205.365 1.00 42.65  ? 430 VAL A N   1 
ATOM 2463 C CA  . VAL B 1 430 ? 180.216 157.107 206.672 1.00 35.64  ? 430 VAL A CA  1 
ATOM 2464 C C   . VAL B 1 430 ? 179.365 156.359 207.691 1.00 37.99  ? 430 VAL A C   1 
ATOM 2465 O O   . VAL B 1 430 ? 178.142 156.268 207.532 1.00 49.68  ? 430 VAL A O   1 
ATOM 2466 C CB  . VAL B 1 430 ? 179.871 158.606 206.672 1.00 38.53  ? 430 VAL A CB  1 
ATOM 2467 C CG1 . VAL B 1 430 ? 179.754 159.135 208.094 1.00 39.48  ? 430 VAL A CG1 1 
ATOM 2468 C CG2 . VAL B 1 430 ? 180.915 159.391 205.894 1.00 45.19  ? 430 VAL A CG2 1 
ATOM 2469 N N   . ILE B 1 431 ? 180.006 155.823 208.729 1.00 33.42  ? 431 ILE A N   1 
ATOM 2470 C CA  . ILE B 1 431 ? 179.338 155.048 209.770 1.00 31.22  ? 431 ILE A CA  1 
ATOM 2471 C C   . ILE B 1 431 ? 179.588 155.720 211.112 1.00 34.77  ? 431 ILE A C   1 
ATOM 2472 O O   . ILE B 1 431 ? 180.732 156.050 211.441 1.00 40.88  ? 431 ILE A O   1 
ATOM 2473 C CB  . ILE B 1 431 ? 179.827 153.588 209.796 1.00 33.33  ? 431 ILE A CB  1 
ATOM 2474 C CG1 . ILE B 1 431 ? 179.888 153.019 208.381 1.00 38.75  ? 431 ILE A CG1 1 
ATOM 2475 C CG2 . ILE B 1 431 ? 178.926 152.740 210.675 1.00 39.51  ? 431 ILE A CG2 1 
ATOM 2476 C CD1 . ILE B 1 431 ? 180.703 151.760 208.255 1.00 46.83  ? 431 ILE A CD1 1 
ATOM 2477 N N   . ALA B 1 432 ? 178.520 155.919 211.885 1.00 32.50  ? 432 ALA A N   1 
ATOM 2478 C CA  . ALA B 1 432 ? 178.606 156.555 213.192 1.00 29.23  ? 432 ALA A CA  1 
ATOM 2479 C C   . ALA B 1 432 ? 177.703 155.833 214.180 1.00 33.11  ? 432 ALA A C   1 
ATOM 2480 O O   . ALA B 1 432 ? 176.602 155.407 213.823 1.00 44.70  ? 432 ALA A O   1 
ATOM 2481 C CB  . ALA B 1 432 ? 178.215 158.034 213.119 1.00 29.78  ? 432 ALA A CB  1 
ATOM 2482 N N   . TRP B 1 433 ? 178.166 155.705 215.423 1.00 26.50  ? 433 TRP A N   1 
ATOM 2483 C CA  . TRP B 1 433 ? 177.370 155.075 216.466 1.00 28.76  ? 433 TRP A CA  1 
ATOM 2484 C C   . TRP B 1 433 ? 177.692 155.711 217.810 1.00 31.63  ? 433 TRP A C   1 
ATOM 2485 O O   . TRP B 1 433 ? 178.703 156.398 217.968 1.00 37.40  ? 433 TRP A O   1 
ATOM 2486 C CB  . TRP B 1 433 ? 177.596 153.561 216.540 1.00 34.39  ? 433 TRP A CB  1 
ATOM 2487 C CG  . TRP B 1 433 ? 179.009 153.142 216.813 1.00 32.10  ? 433 TRP A CG  1 
ATOM 2488 C CD1 . TRP B 1 433 ? 179.519 152.729 218.005 1.00 31.15  ? 433 TRP A CD1 1 
ATOM 2489 C CD2 . TRP B 1 433 ? 180.076 153.035 215.863 1.00 32.13  ? 433 TRP A CD2 1 
ATOM 2490 N NE1 . TRP B 1 433 ? 180.843 152.400 217.867 1.00 30.97  ? 433 TRP A NE1 1 
ATOM 2491 C CE2 . TRP B 1 433 ? 181.208 152.576 216.559 1.00 31.31  ? 433 TRP A CE2 1 
ATOM 2492 C CE3 . TRP B 1 433 ? 180.186 153.292 214.494 1.00 33.55  ? 433 TRP A CE3 1 
ATOM 2493 C CZ2 . TRP B 1 433 ? 182.434 152.373 215.937 1.00 33.71  ? 433 TRP A CZ2 1 
ATOM 2494 C CZ3 . TRP B 1 433 ? 181.405 153.090 213.878 1.00 34.84  ? 433 TRP A CZ3 1 
ATOM 2495 C CH2 . TRP B 1 433 ? 182.512 152.635 214.599 1.00 35.25  ? 433 TRP A CH2 1 
ATOM 2496 N N   . ASN B 1 434 ? 176.816 155.466 218.781 1.00 32.79  ? 434 ASN A N   1 
ATOM 2497 C CA  . ASN B 1 434 ? 176.937 156.085 220.093 1.00 28.33  ? 434 ASN A CA  1 
ATOM 2498 C C   . ASN B 1 434 ? 177.929 155.326 220.963 1.00 32.34  ? 434 ASN A C   1 
ATOM 2499 O O   . ASN B 1 434 ? 177.942 154.092 220.989 1.00 42.56  ? 434 ASN A O   1 
ATOM 2500 C CB  . ASN B 1 434 ? 175.570 156.150 220.774 1.00 28.90  ? 434 ASN A CB  1 
ATOM 2501 C CG  . ASN B 1 434 ? 175.480 157.264 221.796 1.00 33.89  ? 434 ASN A CG  1 
ATOM 2502 O OD1 . ASN B 1 434 ? 176.395 157.471 222.592 1.00 38.84  ? 434 ASN A OD1 1 
ATOM 2503 N ND2 . ASN B 1 434 ? 174.374 157.997 221.772 1.00 34.96  ? 434 ASN A ND2 1 
ATOM 2504 N N   . SER B 1 435 ? 178.761 156.077 221.680 1.00 28.80  ? 435 SER A N   1 
ATOM 2505 C CA  . SER B 1 435 ? 179.834 155.513 222.489 1.00 33.19  ? 435 SER A CA  1 
ATOM 2506 C C   . SER B 1 435 ? 179.892 156.190 223.851 1.00 37.63  ? 435 SER A C   1 
ATOM 2507 O O   . SER B 1 435 ? 180.968 156.546 224.342 1.00 43.21  ? 435 SER A O   1 
ATOM 2508 C CB  . SER B 1 435 ? 181.178 155.634 221.776 1.00 38.69  ? 435 SER A CB  1 
ATOM 2509 O OG  . SER B 1 435 ? 181.558 156.992 221.636 1.00 41.09  ? 435 SER A OG  1 
ATOM 2510 N N   . ASN B 1 436 ? 178.732 156.380 224.480 1.00 34.09  ? 436 ASN A N   1 
ATOM 2511 C CA  . ASN B 1 436 ? 178.696 157.051 225.774 1.00 34.39  ? 436 ASN A CA  1 
ATOM 2512 C C   . ASN B 1 436 ? 179.188 156.151 226.894 1.00 40.64  ? 436 ASN A C   1 
ATOM 2513 O O   . ASN B 1 436 ? 179.859 156.623 227.818 1.00 46.06  ? 436 ASN A O   1 
ATOM 2514 C CB  . ASN B 1 436 ? 177.279 157.511 226.084 1.00 33.47  ? 436 ASN A CB  1 
ATOM 2515 C CG  . ASN B 1 436 ? 177.216 158.474 227.250 1.00 37.47  ? 436 ASN A CG  1 
ATOM 2516 O OD1 . ASN B 1 436 ? 178.223 159.057 227.644 1.00 39.10  ? 436 ASN A OD1 1 
ATOM 2517 N ND2 . ASN B 1 436 ? 176.025 158.647 227.809 1.00 38.01  ? 436 ASN A ND2 1 
ATOM 2518 N N   . LYS B 1 437 ? 178.864 154.861 226.833 1.00 38.95  ? 437 LYS A N   1 
ATOM 2519 C CA  . LYS B 1 437 ? 179.208 153.930 227.897 1.00 42.51  ? 437 LYS A CA  1 
ATOM 2520 C C   . LYS B 1 437 ? 180.701 153.651 227.992 1.00 44.69  ? 437 LYS A C   1 
ATOM 2521 O O   . LYS B 1 437 ? 181.140 153.067 228.989 1.00 51.89  ? 437 LYS A O   1 
ATOM 2522 C CB  . LYS B 1 437 ? 178.446 152.618 227.697 1.00 52.67  ? 437 LYS A CB  1 
ATOM 2523 C CG  . LYS B 1 437 ? 178.822 151.872 226.428 1.00 61.48  ? 437 LYS A CG  1 
ATOM 2524 C CD  . LYS B 1 437 ? 177.988 150.613 226.258 1.00 67.52  ? 437 LYS A CD  1 
ATOM 2525 C CE  . LYS B 1 437 ? 178.382 149.853 225.001 1.00 75.82  ? 437 LYS A CE  1 
ATOM 2526 N NZ  . LYS B 1 437 ? 178.036 150.609 223.765 1.00 70.42  ? 437 LYS A NZ  1 
ATOM 2527 N N   . LEU B 1 438 ? 181.486 154.047 226.998 1.00 40.39  ? 438 LEU A N   1 
ATOM 2528 C CA  . LEU B 1 438 ? 182.924 153.831 227.026 1.00 42.43  ? 438 LEU A CA  1 
ATOM 2529 C C   . LEU B 1 438 ? 183.731 155.118 226.955 1.00 45.43  ? 438 LEU A C   1 
ATOM 2530 O O   . LEU B 1 438 ? 184.676 155.285 227.729 1.00 50.63  ? 438 LEU A O   1 
ATOM 2531 C CB  . LEU B 1 438 ? 183.330 152.891 225.881 1.00 43.82  ? 438 LEU A CB  1 
ATOM 2532 C CG  . LEU B 1 438 ? 184.804 152.498 225.800 1.00 52.24  ? 438 LEU A CG  1 
ATOM 2533 C CD1 . LEU B 1 438 ? 185.209 151.736 227.048 1.00 51.39  ? 438 LEU A CD1 1 
ATOM 2534 C CD2 . LEU B 1 438 ? 185.043 151.644 224.568 1.00 46.92  ? 438 LEU A CD2 1 
ATOM 2535 N N   . ASP B 1 439 ? 183.388 156.036 226.057 1.00 42.83  ? 439 ASP A N   1 
ATOM 2536 C CA  . ASP B 1 439 ? 184.131 157.289 225.905 1.00 44.71  ? 439 ASP A CA  1 
ATOM 2537 C C   . ASP B 1 439 ? 183.521 158.417 226.732 1.00 50.82  ? 439 ASP A C   1 
ATOM 2538 O O   . ASP B 1 439 ? 183.250 159.500 226.215 1.00 52.22  ? 439 ASP A O   1 
ATOM 2539 C CB  . ASP B 1 439 ? 184.209 157.679 224.434 1.00 45.00  ? 439 ASP A CB  1 
ATOM 2540 C CG  . ASP B 1 439 ? 184.630 156.528 223.546 1.00 51.26  ? 439 ASP A CG  1 
ATOM 2541 O OD1 . ASP B 1 439 ? 185.295 155.600 224.050 1.00 53.53  ? 439 ASP A OD1 1 
ATOM 2542 O OD2 . ASP B 1 439 ? 184.307 156.557 222.340 1.00 51.10  ? 439 ASP A OD2 1 
ATOM 2543 N N   . SER B 1 440 ? 183.320 158.180 228.027 1.00 52.90  ? 440 SER A N   1 
ATOM 2544 C CA  . SER B 1 440 ? 182.806 159.197 228.935 1.00 47.33  ? 440 SER A CA  1 
ATOM 2545 C C   . SER B 1 440 ? 183.086 158.767 230.367 1.00 50.11  ? 440 SER A C   1 
ATOM 2546 O O   . SER B 1 440 ? 182.897 157.599 230.715 1.00 54.28  ? 440 SER A O   1 
ATOM 2547 C CB  . SER B 1 440 ? 181.302 159.424 228.747 1.00 40.53  ? 440 SER A CB  1 
ATOM 2548 O OG  . SER B 1 440 ? 180.800 160.330 229.712 1.00 41.49  ? 440 SER A OG  1 
ATOM 2549 N N   . LYS B 1 441 ? 183.531 159.714 231.188 1.00 46.71  ? 441 LYS A N   1 
ATOM 2550 C CA  . LYS B 1 441 ? 183.737 159.479 232.608 1.00 47.61  ? 441 LYS A CA  1 
ATOM 2551 C C   . LYS B 1 441 ? 183.085 160.595 233.411 1.00 51.46  ? 441 LYS A C   1 
ATOM 2552 O O   . LYS B 1 441 ? 182.851 161.697 232.908 1.00 50.00  ? 441 LYS A O   1 
ATOM 2553 C CB  . LYS B 1 441 ? 185.225 159.374 232.972 1.00 46.39  ? 441 LYS A CB  1 
ATOM 2554 C CG  . LYS B 1 441 ? 185.946 158.186 232.353 1.00 52.52  ? 441 LYS A CG  1 
ATOM 2555 C CD  . LYS B 1 441 ? 187.389 158.105 232.831 1.00 59.11  ? 441 LYS A CD  1 
ATOM 2556 C CE  . LYS B 1 441 ? 188.242 159.220 232.255 1.00 58.71  ? 441 LYS A CE  1 
ATOM 2557 N NZ  . LYS B 1 441 ? 188.396 159.087 230.783 1.00 62.89  ? 441 LYS A NZ  1 
ATOM 2558 N N   . HIS B 1 442 ? 182.781 160.281 234.668 1.00 57.52  ? 442 HIS A N   1 
ATOM 2559 C CA  . HIS B 1 442 ? 182.166 161.248 235.566 1.00 55.10  ? 442 HIS A CA  1 
ATOM 2560 C C   . HIS B 1 442 ? 183.147 162.371 235.881 1.00 54.55  ? 442 HIS A C   1 
ATOM 2561 O O   . HIS B 1 442 ? 184.352 162.139 236.018 1.00 56.65  ? 442 HIS A O   1 
ATOM 2562 C CB  . HIS B 1 442 ? 181.712 160.549 236.850 1.00 54.82  ? 442 HIS A CB  1 
ATOM 2563 C CG  . HIS B 1 442 ? 181.275 161.482 237.936 1.00 65.48  ? 442 HIS A CG  1 
ATOM 2564 N ND1 . HIS B 1 442 ? 180.402 162.526 237.716 1.00 73.50  ? 442 HIS A ND1 1 
ATOM 2565 C CD2 . HIS B 1 442 ? 181.586 161.523 239.253 1.00 67.30  ? 442 HIS A CD2 1 
ATOM 2566 C CE1 . HIS B 1 442 ? 180.198 163.173 238.850 1.00 73.97  ? 442 HIS A CE1 1 
ATOM 2567 N NE2 . HIS B 1 442 ? 180.904 162.584 239.798 1.00 71.51  ? 442 HIS A NE2 1 
ATOM 2568 N N   . SER B 1 443 ? 182.615 163.595 235.974 1.00 50.34  ? 443 SER A N   1 
ATOM 2569 C CA  . SER B 1 443 ? 183.384 164.823 236.204 1.00 50.44  ? 443 SER A CA  1 
ATOM 2570 C C   . SER B 1 443 ? 184.435 165.057 235.121 1.00 48.33  ? 443 SER A C   1 
ATOM 2571 O O   . SER B 1 443 ? 185.542 165.520 235.403 1.00 53.60  ? 443 SER A O   1 
ATOM 2572 C CB  . SER B 1 443 ? 184.033 164.840 237.594 1.00 54.38  ? 443 SER A CB  1 
ATOM 2573 O OG  . SER B 1 443 ? 183.067 164.643 238.611 1.00 61.05  ? 443 SER A OG  1 
ATOM 2574 N N   . GLY B 1 444 ? 184.096 164.740 233.874 1.00 41.99  ? 444 GLY A N   1 
ATOM 2575 C CA  . GLY B 1 444 ? 184.946 165.086 232.753 1.00 41.37  ? 444 GLY A CA  1 
ATOM 2576 C C   . GLY B 1 444 ? 185.781 163.950 232.202 1.00 49.32  ? 444 GLY A C   1 
ATOM 2577 O O   . GLY B 1 444 ? 186.323 163.139 232.958 1.00 57.43  ? 444 GLY A O   1 
ATOM 2578 N N   . ASN B 1 445 ? 185.889 163.884 230.875 1.00 46.49  ? 445 ASN A N   1 
ATOM 2579 C CA  . ASN B 1 445 ? 186.754 162.931 230.183 1.00 44.01  ? 445 ASN A CA  1 
ATOM 2580 C C   . ASN B 1 445 ? 187.558 163.782 229.203 1.00 44.66  ? 445 ASN A C   1 
ATOM 2581 O O   . ASN B 1 445 ? 187.183 163.925 228.037 1.00 45.42  ? 445 ASN A O   1 
ATOM 2582 C CB  . ASN B 1 445 ? 185.938 161.844 229.480 1.00 49.40  ? 445 ASN A CB  1 
ATOM 2583 C CG  . ASN B 1 445 ? 186.800 160.865 228.699 1.00 55.89  ? 445 ASN A CG  1 
ATOM 2584 O OD1 . ASN B 1 445 ? 188.021 160.836 228.841 1.00 58.13  ? 445 ASN A OD1 1 
ATOM 2585 N ND2 . ASN B 1 445 ? 186.159 160.054 227.865 1.00 53.29  ? 445 ASN A ND2 1 
ATOM 2586 N N   . TYR B 1 446 ? 188.662 164.344 229.680 1.00 47.70  ? 446 TYR A N   1 
ATOM 2587 C CA  . TYR B 1 446 ? 189.439 165.312 228.906 1.00 46.71  ? 446 TYR A CA  1 
ATOM 2588 C C   . TYR B 1 446 ? 190.586 164.624 228.167 1.00 50.75  ? 446 TYR A C   1 
ATOM 2589 O O   . TYR B 1 446 ? 191.761 164.949 228.337 1.00 53.53  ? 446 TYR A O   1 
ATOM 2590 C CB  . TYR B 1 446 ? 189.953 166.419 229.820 1.00 48.61  ? 446 TYR A CB  1 
ATOM 2591 C CG  . TYR B 1 446 ? 188.860 167.286 230.397 1.00 50.99  ? 446 TYR A CG  1 
ATOM 2592 C CD1 . TYR B 1 446 ? 188.005 168.002 229.571 1.00 50.87  ? 446 TYR A CD1 1 
ATOM 2593 C CD2 . TYR B 1 446 ? 188.682 167.388 231.771 1.00 50.96  ? 446 TYR A CD2 1 
ATOM 2594 C CE1 . TYR B 1 446 ? 187.004 168.797 230.096 1.00 53.06  ? 446 TYR A CE1 1 
ATOM 2595 C CE2 . TYR B 1 446 ? 187.684 168.179 232.304 1.00 51.17  ? 446 TYR A CE2 1 
ATOM 2596 C CZ  . TYR B 1 446 ? 186.850 168.880 231.462 1.00 54.66  ? 446 TYR A CZ  1 
ATOM 2597 O OH  . TYR B 1 446 ? 185.855 169.668 231.992 1.00 58.94  ? 446 TYR A OH  1 
ATOM 2598 N N   . ASP B 1 447 ? 190.226 163.654 227.327 1.00 51.66  ? 447 ASP A N   1 
ATOM 2599 C CA  . ASP B 1 447 ? 191.195 162.978 226.480 1.00 51.29  ? 447 ASP A CA  1 
ATOM 2600 C C   . ASP B 1 447 ? 190.896 163.120 224.996 1.00 48.17  ? 447 ASP A C   1 
ATOM 2601 O O   . ASP B 1 447 ? 191.679 162.634 224.174 1.00 46.36  ? 447 ASP A O   1 
ATOM 2602 C CB  . ASP B 1 447 ? 191.284 161.485 226.842 1.00 58.03  ? 447 ASP A CB  1 
ATOM 2603 C CG  . ASP B 1 447 ? 190.155 160.659 226.242 1.00 63.71  ? 447 ASP A CG  1 
ATOM 2604 O OD1 . ASP B 1 447 ? 188.999 161.131 226.213 1.00 62.43  ? 447 ASP A OD1 1 
ATOM 2605 O OD2 . ASP B 1 447 ? 190.429 159.527 225.791 1.00 65.27  ? 447 ASP A OD2 1 
ATOM 2606 N N   . TYR B 1 448 ? 189.794 163.769 224.630 1.00 44.18  ? 448 TYR A N   1 
ATOM 2607 C CA  . TYR B 1 448 ? 189.381 163.913 223.240 1.00 35.84  ? 448 TYR A CA  1 
ATOM 2608 C C   . TYR B 1 448 ? 189.385 165.397 222.899 1.00 40.11  ? 448 TYR A C   1 
ATOM 2609 O O   . TYR B 1 448 ? 188.544 166.159 223.389 1.00 46.08  ? 448 TYR A O   1 
ATOM 2610 C CB  . TYR B 1 448 ? 188.014 163.275 223.012 1.00 34.61  ? 448 TYR A CB  1 
ATOM 2611 C CG  . TYR B 1 448 ? 188.098 161.785 222.761 1.00 37.44  ? 448 TYR A CG  1 
ATOM 2612 C CD1 . TYR B 1 448 ? 188.960 161.275 221.801 1.00 39.54  ? 448 TYR A CD1 1 
ATOM 2613 C CD2 . TYR B 1 448 ? 187.331 160.890 223.494 1.00 41.26  ? 448 TYR A CD2 1 
ATOM 2614 C CE1 . TYR B 1 448 ? 189.049 159.917 221.570 1.00 42.59  ? 448 TYR A CE1 1 
ATOM 2615 C CE2 . TYR B 1 448 ? 187.415 159.529 223.271 1.00 40.66  ? 448 TYR A CE2 1 
ATOM 2616 C CZ  . TYR B 1 448 ? 188.275 159.050 222.307 1.00 41.57  ? 448 TYR A CZ  1 
ATOM 2617 O OH  . TYR B 1 448 ? 188.364 157.697 222.078 1.00 45.74  ? 448 TYR A OH  1 
ATOM 2618 N N   . TRP B 1 449 ? 190.332 165.793 222.058 1.00 37.67  ? 449 TRP A N   1 
ATOM 2619 C CA  . TRP B 1 449 ? 190.644 167.175 221.738 1.00 35.98  ? 449 TRP A CA  1 
ATOM 2620 C C   . TRP B 1 449 ? 190.162 167.489 220.325 1.00 35.18  ? 449 TRP A C   1 
ATOM 2621 O O   . TRP B 1 449 ? 190.009 166.593 219.491 1.00 38.66  ? 449 TRP A O   1 
ATOM 2622 C CB  . TRP B 1 449 ? 192.158 167.384 221.829 1.00 39.43  ? 449 TRP A CB  1 
ATOM 2623 C CG  . TRP B 1 449 ? 192.760 167.335 223.209 1.00 40.29  ? 449 TRP A CG  1 
ATOM 2624 C CD1 . TRP B 1 449 ? 193.530 166.332 223.716 1.00 42.98  ? 449 TRP A CD1 1 
ATOM 2625 C CD2 . TRP B 1 449 ? 192.782 168.382 224.190 1.00 39.68  ? 449 TRP A CD2 1 
ATOM 2626 N NE1 . TRP B 1 449 ? 193.954 166.648 224.981 1.00 44.89  ? 449 TRP A NE1 1 
ATOM 2627 C CE2 . TRP B 1 449 ? 193.516 167.907 225.291 1.00 40.38  ? 449 TRP A CE2 1 
ATOM 2628 C CE3 . TRP B 1 449 ? 192.228 169.660 224.254 1.00 43.08  ? 449 TRP A CE3 1 
ATOM 2629 C CZ2 . TRP B 1 449 ? 193.705 168.664 226.445 1.00 44.12  ? 449 TRP A CZ2 1 
ATOM 2630 C CZ3 . TRP B 1 449 ? 192.410 170.408 225.402 1.00 42.89  ? 449 TRP A CZ3 1 
ATOM 2631 C CH2 . TRP B 1 449 ? 193.145 169.909 226.479 1.00 43.46  ? 449 TRP A CH2 1 
ATOM 2632 N N   . TYR B 1 450 ? 189.927 168.771 220.050 1.00 37.17  ? 450 TYR A N   1 
ATOM 2633 C CA  . TYR B 1 450 ? 189.709 169.215 218.679 1.00 39.05  ? 450 TYR A CA  1 
ATOM 2634 C C   . TYR B 1 450 ? 190.301 170.604 218.492 1.00 49.07  ? 450 TYR A C   1 
ATOM 2635 O O   . TYR B 1 450 ? 190.418 171.382 219.443 1.00 53.77  ? 450 TYR A O   1 
ATOM 2636 C CB  . TYR B 1 450 ? 188.224 169.242 218.262 1.00 40.40  ? 450 TYR A CB  1 
ATOM 2637 C CG  . TYR B 1 450 ? 187.331 170.224 218.997 1.00 41.03  ? 450 TYR A CG  1 
ATOM 2638 C CD1 . TYR B 1 450 ? 187.012 170.051 220.335 1.00 41.50  ? 450 TYR A CD1 1 
ATOM 2639 C CD2 . TYR B 1 450 ? 186.818 171.336 218.344 1.00 41.75  ? 450 TYR A CD2 1 
ATOM 2640 C CE1 . TYR B 1 450 ? 186.202 170.952 221.001 1.00 39.81  ? 450 TYR A CE1 1 
ATOM 2641 C CE2 . TYR B 1 450 ? 186.006 172.241 219.000 1.00 40.76  ? 450 TYR A CE2 1 
ATOM 2642 C CZ  . TYR B 1 450 ? 185.702 172.045 220.327 1.00 39.86  ? 450 TYR A CZ  1 
ATOM 2643 O OH  . TYR B 1 450 ? 184.895 172.944 220.983 1.00 43.62  ? 450 TYR A OH  1 
ATOM 2644 N N   . ARG B 1 451 ? 190.673 170.905 217.250 1.00 48.79  ? 451 ARG A N   1 
ATOM 2645 C CA  . ARG B 1 451 ? 191.219 172.204 216.884 1.00 51.10  ? 451 ARG A CA  1 
ATOM 2646 C C   . ARG B 1 451 ? 190.094 173.156 216.502 1.00 51.02  ? 451 ARG A C   1 
ATOM 2647 O O   . ARG B 1 451 ? 189.146 172.770 215.813 1.00 55.59  ? 451 ARG A O   1 
ATOM 2648 C CB  . ARG B 1 451 ? 192.203 172.063 215.719 1.00 56.57  ? 451 ARG A CB  1 
ATOM 2649 C CG  . ARG B 1 451 ? 192.871 173.358 215.283 1.00 57.69  ? 451 ARG A CG  1 
ATOM 2650 C CD  . ARG B 1 451 ? 193.811 173.129 214.112 1.00 51.41  ? 451 ARG A CD  1 
ATOM 2651 N NE  . ARG B 1 451 ? 194.833 172.133 214.405 1.00 48.87  ? 451 ARG A NE  1 
ATOM 2652 C CZ  . ARG B 1 451 ? 195.957 172.387 215.059 1.00 50.12  ? 451 ARG A CZ  1 
ATOM 2653 N NH1 . ARG B 1 451 ? 196.242 173.600 215.502 1.00 51.75  ? 451 ARG A NH1 1 
ATOM 2654 N NH2 . ARG B 1 451 ? 196.823 171.400 215.266 1.00 55.50  ? 451 ARG A NH2 1 
ATOM 2655 N N   . SER B 1 452 ? 190.172 174.390 217.007 1.00 50.66  ? 452 SER A N   1 
ATOM 2656 C CA  . SER B 1 452 ? 189.075 175.361 216.766 1.00 58.35  ? 452 SER A CA  1 
ATOM 2657 C C   . SER B 1 452 ? 189.594 176.597 216.022 1.00 64.87  ? 452 SER A C   1 
ATOM 2658 O O   . SER B 1 452 ? 188.787 177.242 215.323 1.00 67.35  ? 452 SER A O   1 
ATOM 2659 C CB  . SER B 1 452 ? 188.432 175.762 218.056 1.00 53.87  ? 452 SER A CB  1 
ATOM 2660 O OG  . SER B 1 452 ? 187.423 176.736 217.829 1.00 56.62  ? 452 SER A OG  1 
ATOM 2661 N N   . PHE B 1 453 ? 190.878 176.921 216.181 1.00 64.47  ? 453 PHE A N   1 
ATOM 2662 C CA  . PHE B 1 453 ? 191.437 178.142 215.542 1.00 62.84  ? 453 PHE A CA  1 
ATOM 2663 C C   . PHE B 1 453 ? 192.494 177.750 214.518 1.00 68.90  ? 453 PHE A C   1 
ATOM 2664 O O   . PHE B 1 453 ? 193.460 177.051 214.888 1.00 72.41  ? 453 PHE A O   1 
ATOM 2665 C CB  . PHE B 1 453 ? 192.034 179.041 216.625 1.00 64.20  ? 453 PHE A CB  1 
ATOM 2666 C CG  . PHE B 1 453 ? 191.031 179.619 217.613 1.00 68.22  ? 453 PHE A CG  1 
ATOM 2667 C CD1 . PHE B 1 453 ? 189.731 179.913 217.220 1.00 70.82  ? 453 PHE A CD1 1 
ATOM 2668 C CD2 . PHE B 1 453 ? 191.391 179.865 218.932 1.00 64.25  ? 453 PHE A CD2 1 
ATOM 2669 C CE1 . PHE B 1 453 ? 188.821 180.439 218.122 1.00 70.67  ? 453 PHE A CE1 1 
ATOM 2670 C CE2 . PHE B 1 453 ? 190.477 180.391 219.829 1.00 62.27  ? 453 PHE A CE2 1 
ATOM 2671 C CZ  . PHE B 1 453 ? 189.195 180.677 219.423 1.00 66.45  ? 453 PHE A CZ  1 
ATOM 2672 N N   . ARG B 1 454 ? 192.324 178.183 213.265 1.00 69.09  ? 454 ARG A N   1 
ATOM 2673 C CA  . ARG B 1 454 ? 193.339 177.911 212.213 1.00 67.51  ? 454 ARG A CA  1 
ATOM 2674 C C   . ARG B 1 454 ? 193.407 179.125 211.279 1.00 72.67  ? 454 ARG A C   1 
ATOM 2675 O O   . ARG B 1 454 ? 192.368 179.796 211.107 1.00 77.35  ? 454 ARG A O   1 
ATOM 2676 C CB  . ARG B 1 454 ? 193.011 176.644 211.417 1.00 68.28  ? 454 ARG A CB  1 
ATOM 2677 C CG  . ARG B 1 454 ? 194.075 175.559 211.486 1.00 71.03  ? 454 ARG A CG  1 
ATOM 2678 C CD  . ARG B 1 454 ? 195.137 175.751 210.421 1.00 72.93  ? 454 ARG A CD  1 
ATOM 2679 N NE  . ARG B 1 454 ? 194.542 175.714 209.081 1.00 78.72  ? 454 ARG A NE  1 
ATOM 2680 C CZ  . ARG B 1 454 ? 194.837 174.809 208.158 1.00 75.53  ? 454 ARG A CZ  1 
ATOM 2681 N NH1 . ARG B 1 454 ? 195.678 173.831 208.440 1.00 71.43  ? 454 ARG A NH1 1 
ATOM 2682 N NH2 . ARG B 1 454 ? 194.288 174.884 206.960 1.00 71.91  ? 454 ARG A NH2 1 
ATOM 2683 N N   . LYS B 1 455 ? 194.578 179.385 210.693 1.00 73.29  ? 455 LYS A N   1 
ATOM 2684 C CA  . LYS B 1 455 ? 194.753 180.579 209.827 1.00 75.18  ? 455 LYS A CA  1 
ATOM 2685 C C   . LYS B 1 455 ? 193.771 180.518 208.648 1.00 77.12  ? 455 LYS A C   1 
ATOM 2686 O O   . LYS B 1 455 ? 193.188 181.571 208.316 1.00 79.26  ? 455 LYS A O   1 
ATOM 2687 C CB  . LYS B 1 455 ? 196.198 180.643 209.325 1.00 71.63  ? 455 LYS A CB  1 
ATOM 2688 C CG  . LYS B 1 455 ? 197.252 180.660 210.420 1.00 71.14  ? 455 LYS A CG  1 
ATOM 2689 C CD  . LYS B 1 455 ? 197.137 181.871 211.337 1.00 72.93  ? 455 LYS A CD  1 
ATOM 2690 C CE  . LYS B 1 455 ? 197.309 183.158 210.596 1.00 75.06  ? 455 LYS A CE  1 
ATOM 2691 N NZ  . LYS B 1 455 ? 198.600 183.211 209.906 1.00 75.55  ? 455 LYS A NZ  1 
ATOM 2692 N N   . SER B 1 456 ? 193.595 179.339 208.046 1.00 76.17  ? 456 SER A N   1 
ATOM 2693 C CA  . SER B 1 456 ? 192.720 179.218 206.850 1.00 75.68  ? 456 SER A CA  1 
ATOM 2694 C C   . SER B 1 456 ? 191.958 177.888 206.881 1.00 73.96  ? 456 SER A C   1 
ATOM 2695 O O   . SER B 1 456 ? 192.171 177.105 207.829 1.00 74.50  ? 456 SER A O   1 
ATOM 2696 C CB  . SER B 1 456 ? 193.527 179.333 205.592 1.00 81.12  ? 456 SER A CB  1 
ATOM 2697 O OG  . SER B 1 456 ? 194.473 178.276 205.510 1.00 83.89  ? 456 SER A OG  1 
ATOM 2698 N N   . LYS B 1 457 ? 191.118 177.644 205.872 1.00 73.79  ? 457 LYS A N   1 
ATOM 2699 C CA  . LYS B 1 457 ? 190.323 176.389 205.814 1.00 72.36  ? 457 LYS A CA  1 
ATOM 2700 C C   . LYS B 1 457 ? 191.254 175.208 205.503 1.00 71.62  ? 457 LYS A C   1 
ATOM 2701 O O   . LYS B 1 457 ? 192.438 175.451 205.192 1.00 72.02  ? 457 LYS A O   1 
ATOM 2702 C CB  . LYS B 1 457 ? 189.208 176.502 204.770 1.00 72.14  ? 457 LYS A CB  1 
ATOM 2703 C CG  . LYS B 1 457 ? 187.801 176.546 205.342 1.00 69.96  ? 457 LYS A CG  1 
ATOM 2704 C CD  . LYS B 1 457 ? 187.585 177.692 206.324 1.00 71.09  ? 457 LYS A CD  1 
ATOM 2705 C CE  . LYS B 1 457 ? 187.724 179.031 205.675 1.00 70.04  ? 457 LYS A CE  1 
ATOM 2706 N NZ  . LYS B 1 457 ? 187.516 180.115 206.637 1.00 65.79  ? 457 LYS A NZ  1 
ATOM 2707 N N   . LEU B 1 458 ? 190.734 173.982 205.584 1.00 69.11  ? 458 LEU A N   1 
ATOM 2708 C CA  . LEU B 1 458 ? 191.577 172.780 205.369 1.00 69.86  ? 458 LEU A CA  1 
ATOM 2709 C C   . LEU B 1 458 ? 191.264 172.171 203.997 1.00 74.36  ? 458 LEU A C   1 
ATOM 2710 O O   . LEU B 1 458 ? 190.065 171.999 203.691 1.00 75.44  ? 458 LEU A O   1 
ATOM 2711 C CB  . LEU B 1 458 ? 191.254 171.809 206.500 1.00 70.09  ? 458 LEU A CB  1 
ATOM 2712 C CG  . LEU B 1 458 ? 192.105 170.540 206.575 1.00 70.98  ? 458 LEU A CG  1 
ATOM 2713 C CD1 . LEU B 1 458 ? 193.360 170.804 207.386 1.00 71.24  ? 458 LEU A CD1 1 
ATOM 2714 C CD2 . LEU B 1 458 ? 191.285 169.427 207.198 1.00 63.55  ? 458 LEU A CD2 1 
ATOM 2715 N N   . LYS B 1 459 ? 192.295 171.856 203.206 1.00 76.26  ? 459 LYS A N   1 
ATOM 2716 C CA  . LYS B 1 459 ? 192.076 171.201 201.889 1.00 74.73  ? 459 LYS A CA  1 
ATOM 2717 C C   . LYS B 1 459 ? 191.595 169.764 202.132 1.00 73.83  ? 459 LYS A C   1 
ATOM 2718 O O   . LYS B 1 459 ? 192.010 169.165 203.145 1.00 76.62  ? 459 LYS A O   1 
ATOM 2719 C CB  . LYS B 1 459 ? 193.356 171.218 201.047 1.00 72.26  ? 459 LYS A CB  1 
ATOM 2720 C CG  . LYS B 1 459 ? 194.500 170.368 201.573 1.00 75.10  ? 459 LYS A CG  1 
ATOM 2721 C CD  . LYS B 1 459 ? 195.780 170.547 200.768 1.00 76.12  ? 459 LYS A CD  1 
ATOM 2722 C CE  . LYS B 1 459 ? 196.202 171.980 200.711 1.00 81.43  ? 459 LYS A CE  1 
ATOM 2723 N NZ  . LYS B 1 459 ? 196.402 172.539 202.051 1.00 83.35  ? 459 LYS A NZ  1 
ATOM 2724 N N   . PRO B 1 460 ? 190.745 169.180 201.263 1.00 67.31  ? 460 PRO A N   1 
ATOM 2725 C CA  . PRO B 1 460 ? 190.211 167.852 201.525 1.00 65.48  ? 460 PRO A CA  1 
ATOM 2726 C C   . PRO B 1 460 ? 191.274 166.850 201.937 1.00 66.89  ? 460 PRO A C   1 
ATOM 2727 O O   . PRO B 1 460 ? 192.358 166.847 201.325 1.00 70.99  ? 460 PRO A O   1 
ATOM 2728 C CB  . PRO B 1 460 ? 189.597 167.505 200.169 1.00 64.10  ? 460 PRO A CB  1 
ATOM 2729 C CG  . PRO B 1 460 ? 189.133 168.838 199.639 1.00 65.43  ? 460 PRO A CG  1 
ATOM 2730 C CD  . PRO B 1 460 ? 190.251 169.783 200.038 1.00 63.78  ? 460 PRO A CD  1 
ATOM 2731 N N   . PHE B 1 461 ? 190.982 166.033 202.952 1.00 65.39  ? 461 PHE A N   1 
ATOM 2732 C CA  . PHE B 1 461 ? 191.923 164.962 203.386 1.00 65.19  ? 461 PHE A CA  1 
ATOM 2733 C C   . PHE B 1 461 ? 193.290 165.550 203.729 1.00 63.08  ? 461 PHE A C   1 
ATOM 2734 O O   . PHE B 1 461 ? 194.271 165.243 203.022 1.00 67.27  ? 461 PHE A O   1 
ATOM 2735 C CB  . PHE B 1 461 ? 192.033 163.894 202.294 1.00 64.31  ? 461 PHE A CB  1 
ATOM 2736 C CG  . PHE B 1 461 ? 190.844 162.951 202.182 1.00 62.39  ? 461 PHE A CG  1 
ATOM 2737 C CD1 . PHE B 1 461 ? 190.121 162.577 203.307 1.00 57.98  ? 461 PHE A CD1 1 
ATOM 2738 C CD2 . PHE B 1 461 ? 190.453 162.441 200.950 1.00 61.88  ? 461 PHE A CD2 1 
ATOM 2739 C CE1 . PHE B 1 461 ? 189.043 161.714 203.200 1.00 51.43  ? 461 PHE A CE1 1 
ATOM 2740 C CE2 . PHE B 1 461 ? 189.372 161.581 200.849 1.00 57.21  ? 461 PHE A CE2 1 
ATOM 2741 C CZ  . PHE B 1 461 ? 188.670 161.221 201.973 1.00 51.78  ? 461 PHE A CZ  1 
ATOM 2742 N N   . GLU B 1 462 ? 193.363 166.359 204.787 1.00 59.51  ? 462 GLU A N   1 
ATOM 2743 C CA  . GLU B 1 462 ? 194.665 166.913 205.243 1.00 60.81  ? 462 GLU A CA  1 
ATOM 2744 C C   . GLU B 1 462 ? 194.680 166.934 206.779 1.00 60.48  ? 462 GLU A C   1 
ATOM 2745 O O   . GLU B 1 462 ? 193.687 167.402 207.367 1.00 63.15  ? 462 GLU A O   1 
ATOM 2746 C CB  . GLU B 1 462 ? 194.861 168.306 204.650 1.00 65.31  ? 462 GLU A CB  1 
ATOM 2747 C CG  . GLU B 1 462 ? 196.013 169.084 205.277 1.00 70.74  ? 462 GLU A CG  1 
ATOM 2748 C CD  . GLU B 1 462 ? 196.204 170.460 204.666 1.00 80.45  ? 462 GLU A CD  1 
ATOM 2749 O OE1 . GLU B 1 462 ? 195.244 171.259 204.690 1.00 78.91  ? 462 GLU A OE1 1 
ATOM 2750 O OE2 . GLU B 1 462 ? 197.314 170.734 204.165 1.00 87.09  ? 462 GLU A OE2 1 
ATOM 2751 N N   . ARG B 1 463 ? 195.753 166.443 207.405 1.00 56.10  ? 463 ARG A N   1 
ATOM 2752 C CA  . ARG B 1 463 ? 195.793 166.364 208.889 1.00 52.85  ? 463 ARG A CA  1 
ATOM 2753 C C   . ARG B 1 463 ? 196.727 167.455 209.431 1.00 63.92  ? 463 ARG A C   1 
ATOM 2754 O O   . ARG B 1 463 ? 197.870 167.545 208.938 1.00 71.39  ? 463 ARG A O   1 
ATOM 2755 C CB  . ARG B 1 463 ? 196.267 164.983 209.349 1.00 47.75  ? 463 ARG A CB  1 
ATOM 2756 C CG  . ARG B 1 463 ? 196.158 164.794 210.855 1.00 48.00  ? 463 ARG A CG  1 
ATOM 2757 C CD  . ARG B 1 463 ? 196.670 163.434 211.286 1.00 46.37  ? 463 ARG A CD  1 
ATOM 2758 N NE  . ARG B 1 463 ? 196.022 162.362 210.526 1.00 53.68  ? 463 ARG A NE  1 
ATOM 2759 C CZ  . ARG B 1 463 ? 196.682 161.528 209.739 1.00 72.03  ? 463 ARG A CZ  1 
ATOM 2760 N NH1 . ARG B 1 463 ? 197.992 161.638 209.621 1.00 74.84  ? 463 ARG A NH1 1 
ATOM 2761 N NH2 . ARG B 1 463 ? 196.034 160.591 209.073 1.00 69.75  ? 463 ARG A NH2 1 
ATOM 2762 N N   . ASP B 1 464 ? 196.258 168.244 210.403 1.00 65.18  ? 464 ASP A N   1 
ATOM 2763 C CA  . ASP B 1 464 ? 197.095 169.318 211.007 1.00 63.49  ? 464 ASP A CA  1 
ATOM 2764 C C   . ASP B 1 464 ? 197.325 169.007 212.488 1.00 58.74  ? 464 ASP A C   1 
ATOM 2765 O O   . ASP B 1 464 ? 196.423 169.295 213.299 1.00 53.56  ? 464 ASP A O   1 
ATOM 2766 C CB  . ASP B 1 464 ? 196.463 170.685 210.813 1.00 61.81  ? 464 ASP A CB  1 
ATOM 2767 C CG  . ASP B 1 464 ? 197.313 171.874 211.237 1.00 71.04  ? 464 ASP A CG  1 
ATOM 2768 O OD1 . ASP B 1 464 ? 197.668 171.950 212.432 1.00 74.77  ? 464 ASP A OD1 1 
ATOM 2769 O OD2 . ASP B 1 464 ? 197.611 172.719 210.367 1.00 73.85  ? 464 ASP A OD2 1 
ATOM 2770 N N   . ILE B 1 465 ? 198.494 168.461 212.824 1.00 56.28  ? 465 ILE A N   1 
ATOM 2771 C CA  . ILE B 1 465 ? 198.805 168.104 214.238 1.00 54.21  ? 465 ILE A CA  1 
ATOM 2772 C C   . ILE B 1 465 ? 199.686 169.214 214.825 1.00 59.27  ? 465 ILE A C   1 
ATOM 2773 O O   . ILE B 1 465 ? 200.334 168.971 215.862 1.00 64.51  ? 465 ILE A O   1 
ATOM 2774 C CB  . ILE B 1 465 ? 199.504 166.738 214.302 1.00 55.91  ? 465 ILE A CB  1 
ATOM 2775 C CG1 . ILE B 1 465 ? 199.147 165.872 213.098 1.00 60.28  ? 465 ILE A CG1 1 
ATOM 2776 C CG2 . ILE B 1 465 ? 199.200 166.026 215.620 1.00 58.76  ? 465 ILE A CG2 1 
ATOM 2777 C CD1 . ILE B 1 465 ? 199.818 164.511 213.098 1.00 63.44  ? 465 ILE A CD1 1 
ATOM 2778 N N   . SER B 1 466 ? 199.706 170.382 214.183 1.00 60.30  ? 466 SER A N   1 
ATOM 2779 C CA  . SER B 1 466 ? 200.598 171.479 214.641 1.00 69.23  ? 466 SER A CA  1 
ATOM 2780 C C   . SER B 1 466 ? 199.993 172.200 215.851 1.00 68.54  ? 466 SER A C   1 
ATOM 2781 O O   . SER B 1 466 ? 198.880 172.743 215.719 1.00 62.68  ? 466 SER A O   1 
ATOM 2782 C CB  . SER B 1 466 ? 200.872 172.450 213.527 1.00 75.74  ? 466 SER A CB  1 
ATOM 2783 O OG  . SER B 1 466 ? 201.613 173.564 214.003 1.00 82.26  ? 466 SER A OG  1 
ATOM 2784 N N   . THR B 1 467 ? 200.713 172.220 216.973 1.00 71.79  ? 467 THR A N   1 
ATOM 2785 C CA  . THR B 1 467 ? 200.238 172.962 218.157 1.00 70.80  ? 467 THR A CA  1 
ATOM 2786 C C   . THR B 1 467 ? 201.101 174.191 218.323 1.00 73.02  ? 467 THR A C   1 
ATOM 2787 O O   . THR B 1 467 ? 202.244 174.051 218.806 1.00 74.03  ? 467 THR A O   1 
ATOM 2788 C CB  . THR B 1 467 ? 200.302 172.057 219.384 1.00 71.68  ? 467 THR A CB  1 
ATOM 2789 O OG1 . THR B 1 467 ? 201.679 171.737 219.549 1.00 75.89  ? 467 THR A OG1 1 
ATOM 2790 C CG2 . THR B 1 467 ? 199.502 170.780 219.203 1.00 69.14  ? 467 THR A CG2 1 
ATOM 2791 N N   . GLU B 1 468 ? 200.587 175.356 217.928 1.00 71.57  ? 468 GLU A N   1 
ATOM 2792 C CA  . GLU B 1 468 ? 201.346 176.624 218.076 1.00 67.81  ? 468 GLU A CA  1 
ATOM 2793 C C   . GLU B 1 468 ? 200.364 177.727 218.489 1.00 69.88  ? 468 GLU A C   1 
ATOM 2794 O O   . GLU B 1 468 ? 199.200 177.680 218.047 1.00 72.21  ? 468 GLU A O   1 
ATOM 2795 C CB  . GLU B 1 468 ? 202.065 176.969 216.773 1.00 74.22  ? 468 GLU A CB  1 
ATOM 2796 C CG  . GLU B 1 468 ? 201.163 177.602 215.717 1.00 80.81  ? 468 GLU A CG  1 
ATOM 2797 C CD  . GLU B 1 468 ? 200.117 176.701 215.083 1.00 85.91  ? 468 GLU A CD  1 
ATOM 2798 O OE1 . GLU B 1 468 ? 200.085 175.494 215.400 1.00 84.87  ? 468 GLU A OE1 1 
ATOM 2799 O OE2 . GLU B 1 468 ? 199.321 177.218 214.272 1.00 89.91  ? 468 GLU A OE2 1 
ATOM 2800 N N   . ILE B 1 469 ? 200.814 178.679 219.306 1.00 67.39  ? 469 ILE A N   1 
ATOM 2801 C CA  . ILE B 1 469 ? 199.875 179.724 219.809 1.00 67.18  ? 469 ILE A CA  1 
ATOM 2802 C C   . ILE B 1 469 ? 199.237 180.423 218.598 1.00 65.93  ? 469 ILE A C   1 
ATOM 2803 O O   . ILE B 1 469 ? 199.969 180.761 217.647 1.00 72.31  ? 469 ILE A O   1 
ATOM 2804 C CB  . ILE B 1 469 ? 200.595 180.706 220.751 1.00 68.58  ? 469 ILE A CB  1 
ATOM 2805 C CG1 . ILE B 1 469 ? 199.600 181.585 221.502 1.00 74.89  ? 469 ILE A CG1 1 
ATOM 2806 C CG2 . ILE B 1 469 ? 201.644 181.537 220.011 1.00 72.01  ? 469 ILE A CG2 1 
ATOM 2807 C CD1 . ILE B 1 469 ? 198.720 180.818 222.472 1.00 73.95  ? 469 ILE A CD1 1 
ATOM 2808 N N   . TYR B 1 470 ? 197.917 180.591 218.621 1.00 58.68  ? 470 TYR A N   1 
ATOM 2809 C CA  . TYR B 1 470 ? 197.218 181.283 217.508 1.00 60.51  ? 470 TYR A CA  1 
ATOM 2810 C C   . TYR B 1 470 ? 197.007 182.725 217.918 1.00 72.68  ? 470 TYR A C   1 
ATOM 2811 O O   . TYR B 1 470 ? 196.486 182.966 219.025 1.00 78.22  ? 470 TYR A O   1 
ATOM 2812 C CB  . TYR B 1 470 ? 195.896 180.575 217.208 1.00 56.80  ? 470 TYR A CB  1 
ATOM 2813 C CG  . TYR B 1 470 ? 194.910 181.353 216.349 1.00 64.02  ? 470 TYR A CG  1 
ATOM 2814 C CD1 . TYR B 1 470 ? 194.939 181.264 214.964 1.00 64.98  ? 470 TYR A CD1 1 
ATOM 2815 C CD2 . TYR B 1 470 ? 193.938 182.160 216.927 1.00 69.33  ? 470 TYR A CD2 1 
ATOM 2816 C CE1 . TYR B 1 470 ? 194.040 181.963 214.177 1.00 63.38  ? 470 TYR A CE1 1 
ATOM 2817 C CE2 . TYR B 1 470 ? 193.034 182.864 216.152 1.00 69.71  ? 470 TYR A CE2 1 
ATOM 2818 C CZ  . TYR B 1 470 ? 193.085 182.766 214.774 1.00 65.47  ? 470 TYR A CZ  1 
ATOM 2819 O OH  . TYR B 1 470 ? 192.194 183.459 214.007 1.00 67.22  ? 470 TYR A OH  1 
ATOM 2820 N N   . GLN B 1 471 ? 197.408 183.662 217.059 1.00 77.14  ? 471 GLN A N   1 
ATOM 2821 C CA  . GLN B 1 471 ? 197.286 185.105 217.389 1.00 79.48  ? 471 GLN A CA  1 
ATOM 2822 C C   . GLN B 1 471 ? 196.018 185.666 216.732 1.00 79.55  ? 471 GLN A C   1 
ATOM 2823 O O   . GLN B 1 471 ? 195.943 185.661 215.486 1.00 79.56  ? 471 GLN A O   1 
ATOM 2824 C CB  . GLN B 1 471 ? 198.546 185.831 216.921 1.00 85.00  ? 471 GLN A CB  1 
ATOM 2825 C CG  . GLN B 1 471 ? 198.394 187.344 216.826 1.00 93.20  ? 471 GLN A CG  1 
ATOM 2826 C CD  . GLN B 1 471 ? 199.595 188.023 216.207 1.00 93.33  ? 471 GLN A CD  1 
ATOM 2827 O OE1 . GLN B 1 471 ? 200.621 187.393 215.930 1.00 92.69  ? 471 GLN A OE1 1 
ATOM 2828 N NE2 . GLN B 1 471 ? 199.482 189.326 215.994 1.00 91.08  ? 471 GLN A NE2 1 
ATOM 2829 N N   . ALA B 1 472 ? 195.060 186.119 217.543 1.00 81.19  ? 472 ALA A N   1 
ATOM 2830 C CA  . ALA B 1 472 ? 193.796 186.671 217.002 1.00 81.22  ? 472 ALA A CA  1 
ATOM 2831 C C   . ALA B 1 472 ? 193.791 188.190 217.164 1.00 90.71  ? 472 ALA A C   1 
ATOM 2832 O O   . ALA B 1 472 ? 192.724 188.811 216.968 1.00 86.55  ? 472 ALA A O   1 
ATOM 2833 C CB  . ALA B 1 472 ? 192.620 186.045 217.710 1.00 74.55  ? 472 ALA A CB  1 
ATOM 2834 N N   . GLY B 1 473 ? 194.943 188.769 217.513 1.00 95.76  ? 473 GLY A N   1 
ATOM 2835 C CA  . GLY B 1 473 ? 195.027 190.225 217.736 1.00 94.60  ? 473 GLY A CA  1 
ATOM 2836 C C   . GLY B 1 473 ? 196.178 190.833 216.962 1.00 95.76  ? 473 GLY A C   1 
ATOM 2837 O O   . GLY B 1 473 ? 197.030 190.069 216.470 1.00 98.01  ? 473 GLY A O   1 
ATOM 2838 N N   . ASN B 1 474 ? 196.203 192.162 216.849 1.00 92.99  ? 474 ASN A N   1 
ATOM 2839 C CA  . ASN B 1 474 ? 197.266 192.845 216.066 1.00 91.82  ? 474 ASN A CA  1 
ATOM 2840 C C   . ASN B 1 474 ? 198.626 192.550 216.703 1.00 95.29  ? 474 ASN A C   1 
ATOM 2841 O O   . ASN B 1 474 ? 199.574 192.227 215.957 1.00 98.43  ? 474 ASN A O   1 
ATOM 2842 C CB  . ASN B 1 474 ? 196.999 194.341 215.971 1.00 91.29  ? 474 ASN A CB  1 
ATOM 2843 C CG  . ASN B 1 474 ? 195.597 194.630 215.495 1.00 94.58  ? 474 ASN A CG  1 
ATOM 2844 O OD1 . ASN B 1 474 ? 195.217 194.217 214.394 1.00 96.59  ? 474 ASN A OD1 1 
ATOM 2845 N ND2 . ASN B 1 474 ? 194.814 195.325 216.306 1.00 94.35  ? 474 ASN A ND2 1 
ATOM 2846 N N   . LYS B 1 475 ? 198.711 192.643 218.032 1.00 94.32  ? 475 LYS A N   1 
ATOM 2847 C CA  . LYS B 1 475 ? 200.010 192.444 218.724 1.00 95.81  ? 475 LYS A CA  1 
ATOM 2848 C C   . LYS B 1 475 ? 200.534 191.031 218.435 1.00 101.28 ? 475 LYS A C   1 
ATOM 2849 O O   . LYS B 1 475 ? 199.758 190.064 218.584 1.00 102.52 ? 475 LYS A O   1 
ATOM 2850 C CB  . LYS B 1 475 ? 199.840 192.697 220.225 1.00 96.80  ? 475 LYS A CB  1 
ATOM 2851 C CG  . LYS B 1 475 ? 198.651 192.006 220.881 1.00 101.09 ? 475 LYS A CG  1 
ATOM 2852 C CD  . LYS B 1 475 ? 198.266 192.650 222.208 1.00 98.83  ? 475 LYS A CD  1 
ATOM 2853 C CE  . LYS B 1 475 ? 197.136 191.961 222.907 1.00 97.40  ? 475 LYS A CE  1 
ATOM 2854 N NZ  . LYS B 1 475 ? 197.555 190.691 223.504 1.00 96.91  ? 475 LYS A NZ  1 
ATOM 2855 N N   . PRO B 1 476 ? 201.811 190.870 218.027 1.00 104.08 ? 476 PRO A N   1 
ATOM 2856 C CA  . PRO B 1 476 ? 202.372 189.545 217.809 1.00 105.88 ? 476 PRO A CA  1 
ATOM 2857 C C   . PRO B 1 476 ? 202.344 188.767 219.112 1.00 109.44 ? 476 PRO A C   1 
ATOM 2858 O O   . PRO B 1 476 ? 202.635 189.351 220.175 1.00 109.01 ? 476 PRO A O   1 
ATOM 2859 C CB  . PRO B 1 476 ? 203.799 189.818 217.316 1.00 104.46 ? 476 PRO A CB  1 
ATOM 2860 C CG  . PRO B 1 476 ? 204.082 191.240 217.750 1.00 102.36 ? 476 PRO A CG  1 
ATOM 2861 C CD  . PRO B 1 476 ? 202.740 191.950 217.756 1.00 100.63 ? 476 PRO A CD  1 
ATOM 2862 N N   . CYS B 1 477 ? 202.006 187.477 219.042 1.00 109.57 ? 477 CYS A N   1 
ATOM 2863 C CA  . CYS B 1 477 ? 201.871 186.665 220.280 1.00 109.31 ? 477 CYS A CA  1 
ATOM 2864 C C   . CYS B 1 477 ? 203.212 186.019 220.655 1.00 108.58 ? 477 CYS A C   1 
ATOM 2865 O O   . CYS B 1 477 ? 203.835 185.397 219.770 1.00 105.05 ? 477 CYS A O   1 
ATOM 2866 C CB  . CYS B 1 477 ? 200.815 185.583 220.103 1.00 108.11 ? 477 CYS A CB  1 
ATOM 2867 S SG  . CYS B 1 477 ? 199.168 186.106 220.643 1.00 118.71 ? 477 CYS A SG  1 
ATOM 2868 N N   . LYS B 1 478 ? 203.630 186.163 221.916 1.00 111.38 ? 478 LYS A N   1 
ATOM 2869 C CA  . LYS B 1 478 ? 204.879 185.510 222.386 1.00 111.49 ? 478 LYS A CA  1 
ATOM 2870 C C   . LYS B 1 478 ? 204.498 184.356 223.323 1.00 107.10 ? 478 LYS A C   1 
ATOM 2871 O O   . LYS B 1 478 ? 205.208 183.328 223.318 1.00 105.65 ? 478 LYS A O   1 
ATOM 2872 C CB  . LYS B 1 478 ? 205.773 186.512 223.122 1.00 112.36 ? 478 LYS A CB  1 
ATOM 2873 C CG  . LYS B 1 478 ? 206.008 187.819 222.382 1.00 113.09 ? 478 LYS A CG  1 
ATOM 2874 C CD  . LYS B 1 478 ? 206.534 187.627 220.965 1.00 109.15 ? 478 LYS A CD  1 
ATOM 2875 C CE  . LYS B 1 478 ? 206.621 188.930 220.241 1.00 107.66 ? 478 LYS A CE  1 
ATOM 2876 N NZ  . LYS B 1 478 ? 205.364 189.671 220.366 1.00 109.57 ? 478 LYS A NZ  1 
ATOM 2877 N N   . GLY B 1 479 ? 203.422 184.529 224.093 1.00 105.32 ? 479 GLY A N   1 
ATOM 2878 C CA  . GLY B 1 479 ? 202.949 183.475 225.013 1.00 103.53 ? 479 GLY A CA  1 
ATOM 2879 C C   . GLY B 1 479 ? 201.474 183.668 225.301 1.00 101.69 ? 479 GLY A C   1 
ATOM 2880 O O   . GLY B 1 479 ? 200.921 184.695 224.858 1.00 98.90  ? 479 GLY A O   1 
ATOM 2881 N N   . LYS B 1 480 ? 200.852 182.726 226.012 1.00 100.40 ? 480 LYS A N   1 
ATOM 2882 C CA  . LYS B 1 480 ? 199.394 182.820 226.270 1.00 89.00  ? 480 LYS A CA  1 
ATOM 2883 C C   . LYS B 1 480 ? 199.070 184.244 226.741 1.00 89.83  ? 480 LYS A C   1 
ATOM 2884 O O   . LYS B 1 480 ? 199.655 184.677 227.755 1.00 96.25  ? 480 LYS A O   1 
ATOM 2885 C CB  . LYS B 1 480 ? 198.972 181.788 227.319 1.00 84.40  ? 480 LYS A CB  1 
ATOM 2886 C CG  . LYS B 1 480 ? 199.187 180.338 226.916 1.00 88.91  ? 480 LYS A CG  1 
ATOM 2887 C CD  . LYS B 1 480 ? 198.747 179.346 227.985 1.00 89.23  ? 480 LYS A CD  1 
ATOM 2888 C CE  . LYS B 1 480 ? 198.978 177.929 227.570 1.00 86.28  ? 480 LYS A CE  1 
ATOM 2889 N NZ  . LYS B 1 480 ? 198.556 176.986 228.608 1.00 81.15  ? 480 LYS A NZ  1 
ATOM 2890 N N   . GLY B 1 481 ? 198.165 184.933 226.041 1.00 86.86  ? 481 GLY A N   1 
ATOM 2891 C CA  . GLY B 1 481 ? 197.795 186.315 226.404 1.00 81.55  ? 481 GLY A CA  1 
ATOM 2892 C C   . GLY B 1 481 ? 196.343 186.583 226.072 1.00 79.92  ? 481 GLY A C   1 
ATOM 2893 O O   . GLY B 1 481 ? 195.705 185.705 225.461 1.00 83.84  ? 481 GLY A O   1 
ATOM 2894 N N   . PRO B 1 482 ? 195.781 187.759 226.418 1.00 78.27  ? 482 PRO A N   1 
ATOM 2895 C CA  . PRO B 1 482 ? 194.364 188.013 226.193 1.00 80.05  ? 482 PRO A CA  1 
ATOM 2896 C C   . PRO B 1 482 ? 193.943 187.769 224.750 1.00 76.67  ? 482 PRO A C   1 
ATOM 2897 O O   . PRO B 1 482 ? 192.739 187.579 224.499 1.00 75.00  ? 482 PRO A O   1 
ATOM 2898 C CB  . PRO B 1 482 ? 194.221 189.486 226.593 1.00 84.46  ? 482 PRO A CB  1 
ATOM 2899 C CG  . PRO B 1 482 ? 195.337 189.700 227.588 1.00 88.83  ? 482 PRO A CG  1 
ATOM 2900 C CD  . PRO B 1 482 ? 196.482 188.864 227.045 1.00 81.64  ? 482 PRO A CD  1 
ATOM 2901 N N   . ASN B 1 483 ? 194.900 187.794 223.820 1.00 78.99  ? 483 ASN A N   1 
ATOM 2902 C CA  . ASN B 1 483 ? 194.585 187.507 222.395 1.00 82.86  ? 483 ASN A CA  1 
ATOM 2903 C C   . ASN B 1 483 ? 195.207 186.167 221.994 1.00 83.40  ? 483 ASN A C   1 
ATOM 2904 O O   . ASN B 1 483 ? 194.732 185.568 221.008 1.00 84.11  ? 483 ASN A O   1 
ATOM 2905 C CB  . ASN B 1 483 ? 195.084 188.617 221.482 1.00 90.81  ? 483 ASN A CB  1 
ATOM 2906 C CG  . ASN B 1 483 ? 196.568 188.504 221.231 1.00 97.59  ? 483 ASN A CG  1 
ATOM 2907 O OD1 . ASN B 1 483 ? 197.360 188.492 222.181 1.00 94.86  ? 483 ASN A OD1 1 
ATOM 2908 N ND2 . ASN B 1 483 ? 196.965 188.395 219.972 1.00 98.74  ? 483 ASN A ND2 1 
ATOM 2909 N N   . CYS B 1 484 ? 196.231 185.719 222.724 1.00 80.13  ? 484 CYS A N   1 
ATOM 2910 C CA  . CYS B 1 484 ? 196.929 184.455 222.374 1.00 77.52  ? 484 CYS A CA  1 
ATOM 2911 C C   . CYS B 1 484 ? 196.108 183.262 222.878 1.00 73.98  ? 484 CYS A C   1 
ATOM 2912 O O   . CYS B 1 484 ? 195.941 183.144 224.108 1.00 76.57  ? 484 CYS A O   1 
ATOM 2913 C CB  . CYS B 1 484 ? 198.318 184.426 222.992 1.00 86.86  ? 484 CYS A CB  1 
ATOM 2914 S SG  . CYS B 1 484 ? 199.265 185.934 222.662 1.00 112.62 ? 484 CYS A SG  1 
ATOM 2915 N N   . TYR B 1 485 ? 195.635 182.407 221.969 1.00 71.83  ? 485 TYR A N   1 
ATOM 2916 C CA  . TYR B 1 485 ? 194.763 181.273 222.370 1.00 65.06  ? 485 TYR A CA  1 
ATOM 2917 C C   . TYR B 1 485 ? 195.353 179.959 221.882 1.00 64.86  ? 485 TYR A C   1 
ATOM 2918 O O   . TYR B 1 485 ? 195.725 179.880 220.696 1.00 70.26  ? 485 TYR A O   1 
ATOM 2919 C CB  . TYR B 1 485 ? 193.393 181.505 221.731 1.00 63.25  ? 485 TYR A CB  1 
ATOM 2920 C CG  . TYR B 1 485 ? 192.685 182.785 222.153 1.00 65.89  ? 485 TYR A CG  1 
ATOM 2921 C CD1 . TYR B 1 485 ? 192.799 183.278 223.446 1.00 68.66  ? 485 TYR A CD1 1 
ATOM 2922 C CD2 . TYR B 1 485 ? 191.911 183.502 221.250 1.00 67.94  ? 485 TYR A CD2 1 
ATOM 2923 C CE1 . TYR B 1 485 ? 192.159 184.444 223.830 1.00 71.40  ? 485 TYR A CE1 1 
ATOM 2924 C CE2 . TYR B 1 485 ? 191.266 184.669 221.622 1.00 69.83  ? 485 TYR A CE2 1 
ATOM 2925 C CZ  . TYR B 1 485 ? 191.390 185.140 222.916 1.00 71.69  ? 485 TYR A CZ  1 
ATOM 2926 O OH  . TYR B 1 485 ? 190.757 186.290 223.286 1.00 74.18  ? 485 TYR A OH  1 
ATOM 2927 N N   . PHE B 1 486 ? 195.446 178.954 222.757 1.00 61.30  ? 486 PHE A N   1 
ATOM 2928 C CA  . PHE B 1 486 ? 195.909 177.612 222.314 1.00 62.63  ? 486 PHE A CA  1 
ATOM 2929 C C   . PHE B 1 486 ? 194.846 177.058 221.382 1.00 63.43  ? 486 PHE A C   1 
ATOM 2930 O O   . PHE B 1 486 ? 193.658 177.088 221.754 1.00 68.15  ? 486 PHE A O   1 
ATOM 2931 C CB  . PHE B 1 486 ? 196.095 176.703 223.528 1.00 61.44  ? 486 PHE A CB  1 
ATOM 2932 C CG  . PHE B 1 486 ? 196.698 175.338 223.228 1.00 63.16  ? 486 PHE A CG  1 
ATOM 2933 C CD1 . PHE B 1 486 ? 197.776 175.208 222.362 1.00 60.65  ? 486 PHE A CD1 1 
ATOM 2934 C CD2 . PHE B 1 486 ? 196.167 174.186 223.794 1.00 68.10  ? 486 PHE A CD2 1 
ATOM 2935 C CE1 . PHE B 1 486 ? 198.316 173.963 222.085 1.00 65.82  ? 486 PHE A CE1 1 
ATOM 2936 C CE2 . PHE B 1 486 ? 196.711 172.943 223.513 1.00 70.57  ? 486 PHE A CE2 1 
ATOM 2937 C CZ  . PHE B 1 486 ? 197.783 172.835 222.660 1.00 69.67  ? 486 PHE A CZ  1 
ATOM 2938 N N   . PRO B 1 487 ? 195.188 176.561 220.175 1.00 56.24  ? 487 PRO A N   1 
ATOM 2939 C CA  . PRO B 1 487 ? 194.167 176.125 219.230 1.00 56.71  ? 487 PRO A CA  1 
ATOM 2940 C C   . PRO B 1 487 ? 193.365 174.870 219.578 1.00 59.95  ? 487 PRO A C   1 
ATOM 2941 O O   . PRO B 1 487 ? 192.275 174.698 218.998 1.00 59.57  ? 487 PRO A O   1 
ATOM 2942 C CB  . PRO B 1 487 ? 194.994 175.922 217.950 1.00 58.93  ? 487 PRO A CB  1 
ATOM 2943 C CG  . PRO B 1 487 ? 196.253 176.712 218.189 1.00 58.42  ? 487 PRO A CG  1 
ATOM 2944 C CD  . PRO B 1 487 ? 196.534 176.471 219.656 1.00 57.18  ? 487 PRO A CD  1 
ATOM 2945 N N   . LEU B 1 488 ? 193.865 174.015 220.475 1.00 58.44  ? 488 LEU A N   1 
ATOM 2946 C CA  . LEU B 1 488 ? 193.161 172.732 220.751 1.00 52.60  ? 488 LEU A CA  1 
ATOM 2947 C C   . LEU B 1 488 ? 192.269 172.847 221.998 1.00 52.71  ? 488 LEU A C   1 
ATOM 2948 O O   . LEU B 1 488 ? 192.812 173.161 223.074 1.00 58.37  ? 488 LEU A O   1 
ATOM 2949 C CB  . LEU B 1 488 ? 194.190 171.618 220.916 1.00 47.57  ? 488 LEU A CB  1 
ATOM 2950 C CG  . LEU B 1 488 ? 195.062 171.312 219.696 1.00 52.99  ? 488 LEU A CG  1 
ATOM 2951 C CD1 . LEU B 1 488 ? 195.980 170.150 220.021 1.00 61.73  ? 488 LEU A CD1 1 
ATOM 2952 C CD2 . LEU B 1 488 ? 194.182 170.968 218.513 1.00 58.21  ? 488 LEU A CD2 1 
ATOM 2953 N N   . GLN B 1 489 ? 190.965 172.589 221.862 1.00 47.26  ? 489 GLN A N   1 
ATOM 2954 C CA  . GLN B 1 489 ? 190.028 172.593 223.018 1.00 44.27  ? 489 GLN A CA  1 
ATOM 2955 C C   . GLN B 1 489 ? 189.554 171.148 223.217 1.00 43.98  ? 489 GLN A C   1 
ATOM 2956 O O   . GLN B 1 489 ? 189.640 170.378 222.241 1.00 49.34  ? 489 GLN A O   1 
ATOM 2957 C CB  . GLN B 1 489 ? 188.870 173.544 222.729 1.00 42.28  ? 489 GLN A CB  1 
ATOM 2958 C CG  . GLN B 1 489 ? 187.913 173.760 223.896 1.00 45.11  ? 489 GLN A CG  1 
ATOM 2959 C CD  . GLN B 1 489 ? 186.751 174.660 223.539 1.00 53.86  ? 489 GLN A CD  1 
ATOM 2960 O OE1 . GLN B 1 489 ? 186.625 175.127 222.402 1.00 58.41  ? 489 GLN A OE1 1 
ATOM 2961 N NE2 . GLN B 1 489 ? 185.885 174.911 224.508 1.00 53.48  ? 489 GLN A NE2 1 
ATOM 2962 N N   . SER B 1 490 ? 189.082 170.778 224.409 1.00 39.62  ? 490 SER A N   1 
ATOM 2963 C CA  . SER B 1 490 ? 188.736 169.352 224.652 1.00 38.61  ? 490 SER A CA  1 
ATOM 2964 C C   . SER B 1 490 ? 187.240 169.158 224.905 1.00 41.43  ? 490 SER A C   1 
ATOM 2965 O O   . SER B 1 490 ? 186.756 169.644 225.937 1.00 46.15  ? 490 SER A O   1 
ATOM 2966 C CB  . SER B 1 490 ? 189.508 168.817 225.816 1.00 39.07  ? 490 SER A CB  1 
ATOM 2967 O OG  . SER B 1 490 ? 189.265 169.595 226.978 1.00 39.84  ? 490 SER A OG  1 
ATOM 2968 N N   . TYR B 1 491 ? 186.547 168.425 224.033 1.00 40.02  ? 491 TYR A N   1 
ATOM 2969 C CA  . TYR B 1 491 ? 185.128 168.122 224.338 1.00 33.80  ? 491 TYR A CA  1 
ATOM 2970 C C   . TYR B 1 491 ? 185.128 167.534 225.737 1.00 36.70  ? 491 TYR A C   1 
ATOM 2971 O O   . TYR B 1 491 ? 185.960 166.651 226.019 1.00 45.33  ? 491 TYR A O   1 
ATOM 2972 C CB  . TYR B 1 491 ? 184.492 167.075 223.423 1.00 33.62  ? 491 TYR A CB  1 
ATOM 2973 C CG  . TYR B 1 491 ? 184.690 167.200 221.920 1.00 33.65  ? 491 TYR A CG  1 
ATOM 2974 C CD1 . TYR B 1 491 ? 185.756 166.578 221.284 1.00 39.32  ? 491 TYR A CD1 1 
ATOM 2975 C CD2 . TYR B 1 491 ? 183.783 167.898 221.134 1.00 36.80  ? 491 TYR A CD2 1 
ATOM 2976 C CE1 . TYR B 1 491 ? 185.930 166.671 219.914 1.00 44.38  ? 491 TYR A CE1 1 
ATOM 2977 C CE2 . TYR B 1 491 ? 183.946 167.999 219.764 1.00 39.53  ? 491 TYR A CE2 1 
ATOM 2978 C CZ  . TYR B 1 491 ? 185.022 167.384 219.153 1.00 45.29  ? 491 TYR A CZ  1 
ATOM 2979 O OH  . TYR B 1 491 ? 185.185 167.483 217.802 1.00 50.86  ? 491 TYR A OH  1 
ATOM 2980 N N   . GLY B 1 492 ? 184.242 168.017 226.604 1.00 33.90  ? 492 GLY A N   1 
ATOM 2981 C CA  . GLY B 1 492 ? 184.164 167.484 227.975 1.00 38.87  ? 492 GLY A CA  1 
ATOM 2982 C C   . GLY B 1 492 ? 183.086 166.431 228.080 1.00 42.59  ? 492 GLY A C   1 
ATOM 2983 O O   . GLY B 1 492 ? 182.033 166.725 228.678 1.00 50.02  ? 492 GLY A O   1 
ATOM 2984 N N   . PHE B 1 493 ? 183.336 165.215 227.617 1.00 35.10  ? 493 PHE A N   1 
ATOM 2985 C CA  . PHE B 1 493 ? 182.237 164.220 227.614 1.00 34.05  ? 493 PHE A CA  1 
ATOM 2986 C C   . PHE B 1 493 ? 181.878 163.921 229.055 1.00 38.72  ? 493 PHE A C   1 
ATOM 2987 O O   . PHE B 1 493 ? 182.808 163.742 229.848 1.00 46.16  ? 493 PHE A O   1 
ATOM 2988 C CB  . PHE B 1 493 ? 182.755 163.058 226.778 1.00 38.93  ? 493 PHE A CB  1 
ATOM 2989 C CG  . PHE B 1 493 ? 182.960 163.354 225.300 1.00 41.37  ? 493 PHE A CG  1 
ATOM 2990 C CD1 . PHE B 1 493 ? 182.034 164.098 224.586 1.00 37.46  ? 493 PHE A CD1 1 
ATOM 2991 C CD2 . PHE B 1 493 ? 184.089 162.899 224.634 1.00 43.72  ? 493 PHE A CD2 1 
ATOM 2992 C CE1 . PHE B 1 493 ? 182.225 164.358 223.243 1.00 35.97  ? 493 PHE A CE1 1 
ATOM 2993 C CE2 . PHE B 1 493 ? 184.274 163.168 223.292 1.00 39.81  ? 493 PHE A CE2 1 
ATOM 2994 C CZ  . PHE B 1 493 ? 183.343 163.895 222.602 1.00 33.67  ? 493 PHE A CZ  1 
ATOM 2995 N N   . ARG B 1 494 ? 180.590 163.949 229.407 1.00 36.01  ? 494 ARG A N   1 
ATOM 2996 C CA  . ARG B 1 494 ? 180.103 163.649 230.784 1.00 38.26  ? 494 ARG A CA  1 
ATOM 2997 C C   . ARG B 1 494 ? 178.846 162.798 230.612 1.00 39.52  ? 494 ARG A C   1 
ATOM 2998 O O   . ARG B 1 494 ? 178.095 163.060 229.658 1.00 42.88  ? 494 ARG A O   1 
ATOM 2999 C CB  . ARG B 1 494 ? 179.796 164.906 231.600 1.00 36.95  ? 494 ARG A CB  1 
ATOM 3000 C CG  . ARG B 1 494 ? 181.013 165.643 232.131 1.00 39.63  ? 494 ARG A CG  1 
ATOM 3001 C CD  . ARG B 1 494 ? 180.629 166.988 232.706 1.00 34.34  ? 494 ARG A CD  1 
ATOM 3002 N NE  . ARG B 1 494 ? 181.799 167.652 233.283 1.00 35.35  ? 494 ARG A NE  1 
ATOM 3003 C CZ  . ARG B 1 494 ? 182.336 168.750 232.787 1.00 40.02  ? 494 ARG A CZ  1 
ATOM 3004 N NH1 . ARG B 1 494 ? 182.056 169.121 231.554 1.00 34.22  ? 494 ARG A NH1 1 
ATOM 3005 N NH2 . ARG B 1 494 ? 183.164 169.469 233.518 1.00 46.07  ? 494 ARG A NH2 1 
ATOM 3006 N N   . PRO B 1 495 ? 178.552 161.816 231.479 1.00 33.25  ? 495 PRO A N   1 
ATOM 3007 C CA  . PRO B 1 495 ? 177.453 160.909 231.195 1.00 29.99  ? 495 PRO A CA  1 
ATOM 3008 C C   . PRO B 1 495 ? 176.042 161.451 231.251 1.00 33.18  ? 495 PRO A C   1 
ATOM 3009 O O   . PRO B 1 495 ? 175.167 160.775 230.703 1.00 40.22  ? 495 PRO A O   1 
ATOM 3010 C CB  . PRO B 1 495 ? 177.694 159.850 232.255 1.00 31.07  ? 495 PRO A CB  1 
ATOM 3011 C CG  . PRO B 1 495 ? 179.112 160.062 232.714 1.00 38.29  ? 495 PRO A CG  1 
ATOM 3012 C CD  . PRO B 1 495 ? 179.248 161.561 232.714 1.00 35.73  ? 495 PRO A CD  1 
ATOM 3013 N N   . THR B 1 496 ? 175.801 162.604 231.879 1.00 33.54  ? 496 THR A N   1 
ATOM 3014 C CA  . THR B 1 496 ? 174.411 163.092 232.055 1.00 36.49  ? 496 THR A CA  1 
ATOM 3015 C C   . THR B 1 496 ? 173.985 164.010 230.929 1.00 34.44  ? 496 THR A C   1 
ATOM 3016 O O   . THR B 1 496 ? 172.845 164.513 230.993 1.00 42.16  ? 496 THR A O   1 
ATOM 3017 C CB  . THR B 1 496 ? 174.295 163.785 233.409 1.00 43.49  ? 496 THR A CB  1 
ATOM 3018 O OG1 . THR B 1 496 ? 175.390 164.694 233.444 1.00 46.15  ? 496 THR A OG1 1 
ATOM 3019 C CG2 . THR B 1 496 ? 174.401 162.813 234.569 1.00 41.14  ? 496 THR A CG2 1 
ATOM 3020 N N   . TYR B 1 497 ? 174.842 164.233 229.934 1.00 29.33  ? 497 TYR A N   1 
ATOM 3021 C CA  . TYR B 1 497 ? 174.520 165.145 228.846 1.00 30.91  ? 497 TYR A CA  1 
ATOM 3022 C C   . TYR B 1 497 ? 173.371 164.610 227.999 1.00 36.27  ? 497 TYR A C   1 
ATOM 3023 O O   . TYR B 1 497 ? 173.042 163.421 228.017 1.00 38.19  ? 497 TYR A O   1 
ATOM 3024 C CB  . TYR B 1 497 ? 175.728 165.386 227.938 1.00 30.53  ? 497 TYR A CB  1 
ATOM 3025 C CG  . TYR B 1 497 ? 176.822 166.286 228.477 1.00 33.89  ? 497 TYR A CG  1 
ATOM 3026 C CD1 . TYR B 1 497 ? 176.983 166.510 229.835 1.00 34.81  ? 497 TYR A CD1 1 
ATOM 3027 C CD2 . TYR B 1 497 ? 177.703 166.910 227.606 1.00 31.98  ? 497 TYR A CD2 1 
ATOM 3028 C CE1 . TYR B 1 497 ? 177.981 167.334 230.304 1.00 33.47  ? 497 TYR A CE1 1 
ATOM 3029 C CE2 . TYR B 1 497 ? 178.701 167.731 228.066 1.00 26.23  ? 497 TYR A CE2 1 
ATOM 3030 C CZ  . TYR B 1 497 ? 178.841 167.937 229.413 1.00 30.09  ? 497 TYR A CZ  1 
ATOM 3031 O OH  . TYR B 1 497 ? 179.844 168.755 229.869 1.00 35.81  ? 497 TYR A OH  1 
ATOM 3032 N N   . GLY B 1 498 ? 172.759 165.520 227.246 1.00 35.48  ? 498 GLY A N   1 
ATOM 3033 C CA  . GLY B 1 498 ? 171.796 165.131 226.243 1.00 34.72  ? 498 GLY A CA  1 
ATOM 3034 C C   . GLY B 1 498 ? 172.477 164.570 225.016 1.00 37.77  ? 498 GLY A C   1 
ATOM 3035 O O   . GLY B 1 498 ? 173.689 164.697 224.851 1.00 40.53  ? 498 GLY A O   1 
ATOM 3036 N N   . VAL B 1 499 ? 171.656 163.978 224.143 1.00 38.02  ? 499 VAL A N   1 
ATOM 3037 C CA  . VAL B 1 499 ? 172.133 163.201 222.999 1.00 35.39  ? 499 VAL A CA  1 
ATOM 3038 C C   . VAL B 1 499 ? 172.982 164.048 222.054 1.00 33.44  ? 499 VAL A C   1 
ATOM 3039 O O   . VAL B 1 499 ? 173.975 163.563 221.495 1.00 31.99  ? 499 VAL A O   1 
ATOM 3040 C CB  . VAL B 1 499 ? 170.914 162.568 222.292 1.00 38.87  ? 499 VAL A CB  1 
ATOM 3041 C CG1 . VAL B 1 499 ? 171.263 162.033 220.912 1.00 37.52  ? 499 VAL A CG1 1 
ATOM 3042 C CG2 . VAL B 1 499 ? 170.320 161.467 223.161 1.00 39.06  ? 499 VAL A CG2 1 
ATOM 3043 N N   . GLY B 1 500 ? 172.654 165.330 221.908 1.00 34.21  ? 500 GLY A N   1 
ATOM 3044 C CA  . GLY B 1 500 ? 173.365 166.189 220.976 1.00 32.80  ? 500 GLY A CA  1 
ATOM 3045 C C   . GLY B 1 500 ? 174.777 166.564 221.390 1.00 34.62  ? 500 GLY A C   1 
ATOM 3046 O O   . GLY B 1 500 ? 175.512 167.116 220.564 1.00 39.40  ? 500 GLY A O   1 
ATOM 3047 N N   . HIS B 1 501 ? 175.168 166.296 222.635 1.00 32.43  ? 501 HIS A N   1 
ATOM 3048 C CA  . HIS B 1 501 ? 176.537 166.518 223.083 1.00 33.29  ? 501 HIS A CA  1 
ATOM 3049 C C   . HIS B 1 501 ? 177.242 165.223 223.457 1.00 31.25  ? 501 HIS A C   1 
ATOM 3050 O O   . HIS B 1 501 ? 178.373 165.265 223.953 1.00 32.37  ? 501 HIS A O   1 
ATOM 3051 C CB  . HIS B 1 501 ? 176.569 167.484 224.276 1.00 34.25  ? 501 HIS A CB  1 
ATOM 3052 C CG  . HIS B 1 501 ? 176.039 168.852 223.972 1.00 37.98  ? 501 HIS A CG  1 
ATOM 3053 N ND1 . HIS B 1 501 ? 174.733 169.083 223.597 1.00 39.07  ? 501 HIS A ND1 1 
ATOM 3054 C CD2 . HIS B 1 501 ? 176.644 170.064 223.985 1.00 38.14  ? 501 HIS A CD2 1 
ATOM 3055 C CE1 . HIS B 1 501 ? 174.556 170.376 223.394 1.00 38.28  ? 501 HIS A CE1 1 
ATOM 3056 N NE2 . HIS B 1 501 ? 175.701 170.993 223.622 1.00 39.96  ? 501 HIS A NE2 1 
ATOM 3057 N N   . GLN B 1 502 ? 176.601 164.082 223.236 1.00 30.12  ? 502 GLN A N   1 
ATOM 3058 C CA  . GLN B 1 502 ? 177.146 162.784 223.583 1.00 30.88  ? 502 GLN A CA  1 
ATOM 3059 C C   . GLN B 1 502 ? 178.216 162.367 222.573 1.00 32.05  ? 502 GLN A C   1 
ATOM 3060 O O   . GLN B 1 502 ? 178.209 162.823 221.428 1.00 35.70  ? 502 GLN A O   1 
ATOM 3061 C CB  . GLN B 1 502 ? 175.998 161.780 223.628 1.00 35.79  ? 502 GLN A CB  1 
ATOM 3062 C CG  . GLN B 1 502 ? 175.169 161.903 224.896 1.00 34.92  ? 502 GLN A CG  1 
ATOM 3063 C CD  . GLN B 1 502 ? 174.653 160.588 225.402 1.00 35.58  ? 502 GLN A CD  1 
ATOM 3064 O OE1 . GLN B 1 502 ? 175.168 159.540 225.052 1.00 35.95  ? 502 GLN A OE1 1 
ATOM 3065 N NE2 . GLN B 1 502 ? 173.631 160.637 226.247 1.00 35.55  ? 502 GLN A NE2 1 
ATOM 3066 N N   . PRO B 1 503 ? 179.166 161.523 222.980 1.00 27.32  ? 503 PRO A N   1 
ATOM 3067 C CA  . PRO B 1 503 ? 180.201 161.075 222.039 1.00 26.45  ? 503 PRO A CA  1 
ATOM 3068 C C   . PRO B 1 503 ? 179.664 160.139 220.963 1.00 30.28  ? 503 PRO A C   1 
ATOM 3069 O O   . PRO B 1 503 ? 178.711 159.385 221.172 1.00 37.01  ? 503 PRO A O   1 
ATOM 3070 C CB  . PRO B 1 503 ? 181.211 160.357 222.941 1.00 30.07  ? 503 PRO A CB  1 
ATOM 3071 C CG  . PRO B 1 503 ? 180.434 159.973 224.144 1.00 32.83  ? 503 PRO A CG  1 
ATOM 3072 C CD  . PRO B 1 503 ? 179.470 161.096 224.355 1.00 31.68  ? 503 PRO A CD  1 
ATOM 3073 N N   . TYR B 1 504 ? 180.306 160.201 219.796 1.00 28.79  ? 504 TYR A N   1 
ATOM 3074 C CA  . TYR B 1 504 ? 180.030 159.341 218.649 1.00 25.36  ? 504 TYR A CA  1 
ATOM 3075 C C   . TYR B 1 504 ? 181.312 158.990 217.915 1.00 27.52  ? 504 TYR A C   1 
ATOM 3076 O O   . TYR B 1 504 ? 182.114 159.871 217.597 1.00 37.74  ? 504 TYR A O   1 
ATOM 3077 C CB  . TYR B 1 504 ? 179.028 159.987 217.684 1.00 25.07  ? 504 TYR A CB  1 
ATOM 3078 C CG  . TYR B 1 504 ? 177.631 160.093 218.232 1.00 31.13  ? 504 TYR A CG  1 
ATOM 3079 C CD1 . TYR B 1 504 ? 176.778 159.006 218.165 1.00 33.49  ? 504 TYR A CD1 1 
ATOM 3080 C CD2 . TYR B 1 504 ? 177.188 161.225 218.883 1.00 32.84  ? 504 TYR A CD2 1 
ATOM 3081 C CE1 . TYR B 1 504 ? 175.501 159.063 218.670 1.00 33.84  ? 504 TYR A CE1 1 
ATOM 3082 C CE2 . TYR B 1 504 ? 175.908 161.289 219.406 1.00 32.40  ? 504 TYR A CE2 1 
ATOM 3083 C CZ  . TYR B 1 504 ? 175.072 160.204 219.295 1.00 35.52  ? 504 TYR A CZ  1 
ATOM 3084 O OH  . TYR B 1 504 ? 173.801 160.259 219.809 1.00 41.58  ? 504 TYR A OH  1 
ATOM 3085 N N   . ARG B 1 505 ? 181.484 157.700 217.642 1.00 24.24  ? 505 ARG A N   1 
ATOM 3086 C CA  . ARG B 1 505 ? 182.638 157.184 216.921 1.00 26.49  ? 505 ARG A CA  1 
ATOM 3087 C C   . ARG B 1 505 ? 182.301 157.112 215.438 1.00 27.87  ? 505 ARG A C   1 
ATOM 3088 O O   . ARG B 1 505 ? 181.296 156.504 215.058 1.00 34.18  ? 505 ARG A O   1 
ATOM 3089 C CB  . ARG B 1 505 ? 183.019 155.805 217.455 1.00 31.45  ? 505 ARG A CB  1 
ATOM 3090 C CG  . ARG B 1 505 ? 183.456 155.814 218.902 1.00 36.65  ? 505 ARG A CG  1 
ATOM 3091 C CD  . ARG B 1 505 ? 183.855 154.438 219.396 1.00 40.07  ? 505 ARG A CD  1 
ATOM 3092 N NE  . ARG B 1 505 ? 184.549 154.525 220.674 1.00 40.12  ? 505 ARG A NE  1 
ATOM 3093 C CZ  . ARG B 1 505 ? 185.452 153.652 221.098 1.00 40.67  ? 505 ARG A CZ  1 
ATOM 3094 N NH1 . ARG B 1 505 ? 185.770 152.585 220.385 1.00 38.84  ? 505 ARG A NH1 1 
ATOM 3095 N NH2 . ARG B 1 505 ? 186.056 153.859 222.263 1.00 44.95  ? 505 ARG A NH2 1 
ATOM 3096 N N   . VAL B 1 506 ? 183.139 157.717 214.602 1.00 24.93  ? 506 VAL A N   1 
ATOM 3097 C CA  . VAL B 1 506 ? 182.875 157.833 213.173 1.00 27.47  ? 506 VAL A CA  1 
ATOM 3098 C C   . VAL B 1 506 ? 183.999 157.142 212.414 1.00 29.73  ? 506 VAL A C   1 
ATOM 3099 O O   . VAL B 1 506 ? 185.175 157.472 212.603 1.00 34.25  ? 506 VAL A O   1 
ATOM 3100 C CB  . VAL B 1 506 ? 182.739 159.301 212.739 1.00 30.55  ? 506 VAL A CB  1 
ATOM 3101 C CG1 . VAL B 1 506 ? 182.714 159.415 211.225 1.00 35.26  ? 506 VAL A CG1 1 
ATOM 3102 C CG2 . VAL B 1 506 ? 181.488 159.912 213.338 1.00 27.86  ? 506 VAL A CG2 1 
ATOM 3103 N N   . VAL B 1 507 ? 183.636 156.192 211.555 1.00 29.59  ? 507 VAL A N   1 
ATOM 3104 C CA  . VAL B 1 507 ? 184.568 155.529 210.649 1.00 31.43  ? 507 VAL A CA  1 
ATOM 3105 C C   . VAL B 1 507 ? 184.146 155.860 209.225 1.00 33.56  ? 507 VAL A C   1 
ATOM 3106 O O   . VAL B 1 507 ? 183.020 155.547 208.817 1.00 39.31  ? 507 VAL A O   1 
ATOM 3107 C CB  . VAL B 1 507 ? 184.603 154.010 210.868 1.00 31.52  ? 507 VAL A CB  1 
ATOM 3108 C CG1 . VAL B 1 507 ? 185.495 153.352 209.839 1.00 33.31  ? 507 VAL A CG1 1 
ATOM 3109 C CG2 . VAL B 1 507 ? 185.091 153.692 212.269 1.00 34.37  ? 507 VAL A CG2 1 
ATOM 3110 N N   . VAL B 1 508 ? 185.045 156.485 208.471 1.00 31.91  ? 508 VAL A N   1 
ATOM 3111 C CA  . VAL B 1 508 ? 184.782 156.895 207.098 1.00 32.60  ? 508 VAL A CA  1 
ATOM 3112 C C   . VAL B 1 508 ? 185.635 156.037 206.177 1.00 38.43  ? 508 VAL A C   1 
ATOM 3113 O O   . VAL B 1 508 ? 186.865 156.009 206.302 1.00 44.39  ? 508 VAL A O   1 
ATOM 3114 C CB  . VAL B 1 508 ? 185.068 158.388 206.884 1.00 35.61  ? 508 VAL A CB  1 
ATOM 3115 C CG1 . VAL B 1 508 ? 184.859 158.763 205.427 1.00 42.90  ? 508 VAL A CG1 1 
ATOM 3116 C CG2 . VAL B 1 508 ? 184.185 159.230 207.785 1.00 41.29  ? 508 VAL A CG2 1 
ATOM 3117 N N   . LEU B 1 509 ? 184.983 155.336 205.258 1.00 42.87  ? 509 LEU A N   1 
ATOM 3118 C CA  . LEU B 1 509 ? 185.657 154.499 204.277 1.00 43.20  ? 509 LEU A CA  1 
ATOM 3119 C C   . LEU B 1 509 ? 185.686 155.235 202.946 1.00 48.42  ? 509 LEU A C   1 
ATOM 3120 O O   . LEU B 1 509 ? 184.670 155.795 202.523 1.00 57.68  ? 509 LEU A O   1 
ATOM 3121 C CB  . LEU B 1 509 ? 184.942 153.156 204.127 1.00 44.13  ? 509 LEU A CB  1 
ATOM 3122 C CG  . LEU B 1 509 ? 184.942 152.229 205.342 1.00 43.69  ? 509 LEU A CG  1 
ATOM 3123 C CD1 . LEU B 1 509 ? 183.757 151.284 205.286 1.00 44.99  ? 509 LEU A CD1 1 
ATOM 3124 C CD2 . LEU B 1 509 ? 186.240 151.446 205.411 1.00 49.99  ? 509 LEU A CD2 1 
ATOM 3125 N N   . SER B 1 510 ? 186.849 155.257 202.303 1.00 46.60  ? 510 SER A N   1 
ATOM 3126 C CA  . SER B 1 510 ? 187.009 155.911 201.013 1.00 52.20  ? 510 SER A CA  1 
ATOM 3127 C C   . SER B 1 510 ? 187.719 154.967 200.057 1.00 59.75  ? 510 SER A C   1 
ATOM 3128 O O   . SER B 1 510 ? 188.713 154.336 200.424 1.00 63.50  ? 510 SER A O   1 
ATOM 3129 C CB  . SER B 1 510 ? 187.799 157.215 201.140 1.00 52.00  ? 510 SER A CB  1 
ATOM 3130 O OG  . SER B 1 510 ? 189.189 156.981 201.011 1.00 58.28  ? 510 SER A OG  1 
ATOM 3131 N N   . PHE B 1 511 ? 187.212 154.885 198.829 1.00 61.56  ? 511 PHE A N   1 
ATOM 3132 C CA  . PHE B 1 511 ? 187.743 153.948 197.850 1.00 61.43  ? 511 PHE A CA  1 
ATOM 3133 C C   . PHE B 1 511 ? 187.401 154.416 196.442 1.00 66.92  ? 511 PHE A C   1 
ATOM 3134 O O   . PHE B 1 511 ? 186.462 155.189 196.235 1.00 67.90  ? 511 PHE A O   1 
ATOM 3135 C CB  . PHE B 1 511 ? 187.230 152.528 198.123 1.00 60.07  ? 511 PHE A CB  1 
ATOM 3136 C CG  . PHE B 1 511 ? 185.767 152.455 198.485 1.00 55.82  ? 511 PHE A CG  1 
ATOM 3137 C CD1 . PHE B 1 511 ? 184.780 152.701 197.548 1.00 60.34  ? 511 PHE A CD1 1 
ATOM 3138 C CD2 . PHE B 1 511 ? 185.385 152.128 199.775 1.00 55.89  ? 511 PHE A CD2 1 
ATOM 3139 C CE1 . PHE B 1 511 ? 183.443 152.631 197.891 1.00 64.76  ? 511 PHE A CE1 1 
ATOM 3140 C CE2 . PHE B 1 511 ? 184.051 152.053 200.123 1.00 60.34  ? 511 PHE A CE2 1 
ATOM 3141 C CZ  . PHE B 1 511 ? 183.079 152.306 199.180 1.00 64.36  ? 511 PHE A CZ  1 
ATOM 3142 N N   . GLU B 1 512 ? 188.181 153.932 195.478 1.00 73.16  ? 512 GLU A N   1 
ATOM 3143 C CA  . GLU B 1 512 ? 188.062 154.315 194.076 1.00 80.98  ? 512 GLU A CA  1 
ATOM 3144 C C   . GLU B 1 512 ? 187.463 153.163 193.282 1.00 83.83  ? 512 GLU A C   1 
ATOM 3145 O O   . GLU B 1 512 ? 187.905 152.018 193.419 1.00 79.19  ? 512 GLU A O   1 
ATOM 3146 C CB  . GLU B 1 512 ? 189.428 154.696 193.500 1.00 82.26  ? 512 GLU A CB  1 
ATOM 3147 C CG  . GLU B 1 512 ? 189.869 156.120 193.808 1.00 91.36  ? 512 GLU A CG  1 
ATOM 3148 C CD  . GLU B 1 512 ? 189.281 157.143 192.853 1.00 103.56 ? 512 GLU A CD  1 
ATOM 3149 O OE1 . GLU B 1 512 ? 188.588 156.742 191.894 1.00 107.03 ? 512 GLU A OE1 1 
ATOM 3150 O OE2 . GLU B 1 512 ? 189.515 158.352 193.061 1.00 109.79 ? 512 GLU A OE2 1 
ATOM 3151 N N   . LEU B 1 513 ? 186.472 153.466 192.444 1.00 90.44  ? 513 LEU A N   1 
ATOM 3152 C CA  . LEU B 1 513 ? 185.716 152.448 191.720 1.00 90.28  ? 513 LEU A CA  1 
ATOM 3153 C C   . LEU B 1 513 ? 186.153 152.419 190.259 1.00 94.71  ? 513 LEU A C   1 
ATOM 3154 O O   . LEU B 1 513 ? 185.977 153.403 189.534 1.00 97.14  ? 513 LEU A O   1 
ATOM 3155 C CB  . LEU B 1 513 ? 184.211 152.699 191.814 1.00 92.16  ? 513 LEU A CB  1 
ATOM 3156 C CG  . LEU B 1 513 ? 183.410 152.346 193.073 1.00 88.76  ? 513 LEU A CG  1 
ATOM 3157 C CD1 . LEU B 1 513 ? 183.699 153.292 194.224 1.00 80.81  ? 513 LEU A CD1 1 
ATOM 3158 C CD2 . LEU B 1 513 ? 181.920 152.324 192.761 1.00 80.26  ? 513 LEU A CD2 1 
ATOM 3159 N N   . LEU B 1 514 ? 186.726 151.284 189.842 1.00 96.39  ? 514 LEU A N   1 
ATOM 3160 C CA  . LEU B 1 514 ? 186.936 150.929 188.432 1.00 102.79 ? 514 LEU A CA  1 
ATOM 3161 C C   . LEU B 1 514 ? 187.826 151.923 187.688 1.00 103.38 ? 514 LEU A C   1 
ATOM 3162 O O   . LEU B 1 514 ? 187.704 152.086 186.472 1.00 104.69 ? 514 LEU A O   1 
ATOM 3163 C CB  . LEU B 1 514 ? 185.600 150.765 187.699 1.00 105.28 ? 514 LEU A CB  1 
ATOM 3164 C CG  . LEU B 1 514 ? 184.595 149.799 188.331 1.00 104.09 ? 514 LEU A CG  1 
ATOM 3165 C CD1 . LEU B 1 514 ? 183.185 150.090 187.842 1.00 94.52  ? 514 LEU A CD1 1 
ATOM 3166 C CD2 . LEU B 1 514 ? 184.979 148.354 188.044 1.00 104.63 ? 514 LEU A CD2 1 
ATOM 3167 N N   . HIS B 1 515 ? 188.730 152.595 188.399 1.00 103.49 ? 515 HIS A N   1 
ATOM 3168 C CA  . HIS B 1 515 ? 189.688 153.498 187.774 1.00 112.55 ? 515 HIS A CA  1 
ATOM 3169 C C   . HIS B 1 515 ? 191.128 153.025 187.936 1.00 117.39 ? 515 HIS A C   1 
ATOM 3170 O O   . HIS B 1 515 ? 192.057 153.765 187.595 1.00 120.63 ? 515 HIS A O   1 
ATOM 3171 C CB  . HIS B 1 515 ? 189.530 154.913 188.335 1.00 115.37 ? 515 HIS A CB  1 
ATOM 3172 C CG  . HIS B 1 515 ? 188.214 155.549 188.008 1.00 116.12 ? 515 HIS A CG  1 
ATOM 3173 N ND1 . HIS B 1 515 ? 187.203 155.692 188.934 1.00 113.27 ? 515 HIS A ND1 1 
ATOM 3174 C CD2 . HIS B 1 515 ? 187.743 156.079 186.854 1.00 117.17 ? 515 HIS A CD2 1 
ATOM 3175 C CE1 . HIS B 1 515 ? 186.168 156.285 188.366 1.00 114.92 ? 515 HIS A CE1 1 
ATOM 3176 N NE2 . HIS B 1 515 ? 186.470 156.529 187.103 1.00 119.45 ? 515 HIS A NE2 1 
ATOM 3177 N N   . ALA B 1 516 ? 191.332 151.811 188.438 1.00 114.16 ? 516 ALA A N   1 
ATOM 3178 C CA  . ALA B 1 516 ? 192.659 151.257 188.665 1.00 116.92 ? 516 ALA A CA  1 
ATOM 3179 C C   . ALA B 1 516 ? 192.531 149.741 188.736 1.00 119.84 ? 516 ALA A C   1 
ATOM 3180 O O   . ALA B 1 516 ? 191.423 149.223 188.925 1.00 113.86 ? 516 ALA A O   1 
ATOM 3181 C CB  . ALA B 1 516 ? 193.280 151.817 189.957 1.00 107.65 ? 516 ALA A CB  1 
ATOM 3182 N N   . PRO B 1 517 ? 193.629 149.002 188.539 1.00 123.97 ? 517 PRO A N   1 
ATOM 3183 C CA  . PRO B 1 517 ? 193.590 147.556 188.796 1.00 114.19 ? 517 PRO A CA  1 
ATOM 3184 C C   . PRO B 1 517 ? 193.238 147.253 190.246 1.00 107.55 ? 517 PRO A C   1 
ATOM 3185 O O   . PRO B 1 517 ? 193.722 147.905 191.174 1.00 105.15 ? 517 PRO A O   1 
ATOM 3186 C CB  . PRO B 1 517 ? 195.011 147.095 188.453 1.00 104.96 ? 517 PRO A CB  1 
ATOM 3187 C CG  . PRO B 1 517 ? 195.492 148.089 187.464 1.00 110.74 ? 517 PRO A CG  1 
ATOM 3188 C CD  . PRO B 1 517 ? 194.872 149.401 187.851 1.00 118.99 ? 517 PRO A CD  1 
ATOM 3189 N N   . ALA B 1 518 ? 192.383 146.252 190.430 1.00 97.53  ? 518 ALA A N   1 
ATOM 3190 C CA  . ALA B 1 518 ? 191.854 145.934 191.746 1.00 86.02  ? 518 ALA A CA  1 
ATOM 3191 C C   . ALA B 1 518 ? 192.872 145.166 192.579 1.00 79.72  ? 518 ALA A C   1 
ATOM 3192 O O   . ALA B 1 518 ? 193.694 144.407 192.057 1.00 83.36  ? 518 ALA A O   1 
ATOM 3193 C CB  . ALA B 1 518 ? 190.565 145.122 191.623 1.00 79.52  ? 518 ALA A CB  1 
ATOM 3194 N N   . THR B 1 519 ? 192.807 145.373 193.890 1.00 73.73  ? 519 THR A N   1 
ATOM 3195 C CA  . THR B 1 519 ? 193.631 144.655 194.854 1.00 75.49  ? 519 THR A CA  1 
ATOM 3196 C C   . THR B 1 519 ? 192.816 143.860 195.860 1.00 71.45  ? 519 THR A C   1 
ATOM 3197 O O   . THR B 1 519 ? 193.247 142.783 196.279 1.00 73.64  ? 519 THR A O   1 
ATOM 3198 C CB  . THR B 1 519 ? 194.549 145.632 195.607 1.00 83.65  ? 519 THR A CB  1 
ATOM 3199 O OG1 . THR B 1 519 ? 193.753 146.579 196.331 1.00 87.16  ? 519 THR A OG1 1 
ATOM 3200 C CG2 . THR B 1 519 ? 195.462 146.373 194.639 1.00 80.54  ? 519 THR A CG2 1 
ATOM 3201 N N   . VAL B 1 520 ? 191.652 144.362 196.265 1.00 66.74  ? 520 VAL A N   1 
ATOM 3202 C CA  . VAL B 1 520 ? 190.770 143.679 197.206 1.00 68.15  ? 520 VAL A CA  1 
ATOM 3203 C C   . VAL B 1 520 ? 189.396 143.530 196.562 1.00 71.90  ? 520 VAL A C   1 
ATOM 3204 O O   . VAL B 1 520 ? 188.879 144.482 195.964 1.00 75.19  ? 520 VAL A O   1 
ATOM 3205 C CB  . VAL B 1 520 ? 190.683 144.427 198.552 1.00 61.60  ? 520 VAL A CB  1 
ATOM 3206 C CG1 . VAL B 1 520 ? 191.988 144.297 199.303 1.00 66.56  ? 520 VAL A CG1 1 
ATOM 3207 C CG2 . VAL B 1 520 ? 190.375 145.905 198.350 1.00 54.34  ? 520 VAL A CG2 1 
ATOM 3208 N N   . CYS B 1 521 ? 188.829 142.325 196.628 1.00 66.66  ? 521 CYS A N   1 
ATOM 3209 C CA  . CYS B 1 521 ? 187.462 142.282 196.124 1.00 59.11  ? 521 CYS A CA  1 
ATOM 3210 C C   . CYS B 1 521 ? 186.446 141.629 197.051 1.00 55.84  ? 521 CYS A C   1 
ATOM 3211 O O   . CYS B 1 521 ? 185.313 142.111 197.128 1.00 57.50  ? 521 CYS A O   1 
ATOM 3212 C CB  . CYS B 1 521 ? 187.393 141.623 194.719 1.00 69.16  ? 521 CYS A CB  1 
ATOM 3213 S SG  . CYS B 1 521 ? 188.233 142.540 193.361 1.00 96.14  ? 521 CYS A SG  1 
ATOM 3214 N N   . GLY B 1 522 ? 186.800 140.560 197.751 1.00 59.23  ? 522 GLY A N   1 
ATOM 3215 C CA  . GLY B 1 522 ? 185.870 139.977 198.690 1.00 64.21  ? 522 GLY A CA  1 
ATOM 3216 C C   . GLY B 1 522 ? 185.507 138.531 198.413 1.00 62.93  ? 522 GLY A C   1 
ATOM 3217 O O   . GLY B 1 522 ? 186.374 137.662 198.284 1.00 68.41  ? 522 GLY A O   1 
ATOM 3218 N N   . PRO B 1 523 ? 184.199 138.246 198.316 1.00 50.88  ? 523 PRO A N   1 
ATOM 3219 C CA  . PRO B 1 523 ? 183.744 136.848 198.236 1.00 52.05  ? 523 PRO A CA  1 
ATOM 3220 C C   . PRO B 1 523 ? 184.099 136.171 196.919 1.00 62.89  ? 523 PRO A C   1 
ATOM 3221 O O   . PRO B 1 523 ? 183.537 136.488 195.866 1.00 60.46  ? 523 PRO A O   1 
ATOM 3222 C CB  . PRO B 1 523 ? 182.223 136.960 198.411 1.00 47.80  ? 523 PRO A CB  1 
ATOM 3223 C CG  . PRO B 1 523 ? 181.971 138.353 198.904 1.00 50.85  ? 523 PRO A CG  1 
ATOM 3224 C CD  . PRO B 1 523 ? 183.076 139.192 198.369 1.00 46.60  ? 523 PRO A CD  1 
ATOM 3225 N N   . LYS B 1 524 ? 185.033 135.226 196.984 1.00 68.08  ? 524 LYS A N   1 
ATOM 3226 C CA  . LYS B 1 524 ? 185.574 134.575 195.802 1.00 65.27  ? 524 LYS A CA  1 
ATOM 3227 C C   . LYS B 1 524 ? 184.656 133.457 195.318 1.00 58.57  ? 524 LYS A C   1 
ATOM 3228 O O   . LYS B 1 524 ? 183.830 132.925 196.065 1.00 61.36  ? 524 LYS A O   1 
ATOM 3229 C CB  . LYS B 1 524 ? 186.962 133.996 196.095 1.00 68.24  ? 524 LYS A CB  1 
ATOM 3230 C CG  . LYS B 1 524 ? 188.076 135.010 196.376 1.00 70.95  ? 524 LYS A CG  1 
ATOM 3231 C CD  . LYS B 1 524 ? 187.865 136.344 195.681 1.00 71.81  ? 524 LYS A CD  1 
ATOM 3232 C CE  . LYS B 1 524 ? 189.109 137.211 195.765 1.00 73.82  ? 524 LYS A CE  1 
ATOM 3233 N NZ  . LYS B 1 524 ? 188.840 138.612 195.342 1.00 74.12  ? 524 LYS A NZ  1 
ATOM 3234 N N   . LYS B 1 525 ? 184.825 133.099 194.048 1.00 53.20  ? 525 LYS A N   1 
ATOM 3235 C CA  . LYS B 1 525 ? 184.192 131.922 193.455 1.00 52.84  ? 525 LYS A CA  1 
ATOM 3236 C C   . LYS B 1 525 ? 184.917 131.520 192.176 1.00 52.36  ? 525 LYS A C   1 
ATOM 3237 O O   . LYS B 1 525 ? 186.130 131.697 192.056 1.00 49.22  ? 525 LYS A O   1 
ATOM 3238 C CB  . LYS B 1 525 ? 182.708 132.171 193.160 1.00 58.01  ? 525 LYS A CB  1 
ATOM 3239 C CG  . LYS B 1 525 ? 181.906 130.901 192.866 1.00 61.62  ? 525 LYS A CG  1 
ATOM 3240 C CD  . LYS B 1 525 ? 182.054 129.824 193.944 1.00 58.96  ? 525 LYS A CD  1 
ATOM 3241 C CE  . LYS B 1 525 ? 181.546 130.282 195.309 1.00 57.08  ? 525 LYS A CE  1 
ATOM 3242 N NZ  . LYS B 1 525 ? 180.060 130.347 195.350 1.00 54.66  ? 525 LYS A NZ  1 
ATOM 3243 N N   . GLN C 2 1   ? 151.589 221.012 248.682 1.00 110.37 ? 1   GLN D N   1 
ATOM 3244 C CA  . GLN C 2 1   ? 151.150 219.820 247.968 1.00 114.69 ? 1   GLN D CA  1 
ATOM 3245 C C   . GLN C 2 1   ? 151.460 218.570 248.784 1.00 114.66 ? 1   GLN D C   1 
ATOM 3246 O O   . GLN C 2 1   ? 150.585 217.739 249.027 1.00 118.51 ? 1   GLN D O   1 
ATOM 3247 C CB  . GLN C 2 1   ? 151.820 219.739 246.590 1.00 117.97 ? 1   GLN D CB  1 
ATOM 3248 C CG  . GLN C 2 1   ? 151.720 218.395 245.835 1.00 123.56 ? 1   GLN D CG  1 
ATOM 3249 C CD  . GLN C 2 1   ? 150.299 217.962 245.460 1.00 129.97 ? 1   GLN D CD  1 
ATOM 3250 O OE1 . GLN C 2 1   ? 149.431 217.762 246.311 1.00 132.42 ? 1   GLN D OE1 1 
ATOM 3251 N NE2 . GLN C 2 1   ? 150.066 217.816 244.160 1.00 136.64 ? 1   GLN D NE2 1 
ATOM 3252 N N   . VAL C 2 2   ? 152.716 218.448 249.208 1.00 108.70 ? 2   VAL D N   1 
ATOM 3253 C CA  . VAL C 2 2   ? 153.177 217.342 250.039 1.00 98.01  ? 2   VAL D CA  1 
ATOM 3254 C C   . VAL C 2 2   ? 153.574 217.905 251.395 1.00 97.01  ? 2   VAL D C   1 
ATOM 3255 O O   . VAL C 2 2   ? 154.378 218.842 251.473 1.00 97.53  ? 2   VAL D O   1 
ATOM 3256 C CB  . VAL C 2 2   ? 154.354 216.598 249.385 1.00 89.94  ? 2   VAL D CB  1 
ATOM 3257 C CG1 . VAL C 2 2   ? 154.886 215.524 250.319 1.00 83.62  ? 2   VAL D CG1 1 
ATOM 3258 C CG2 . VAL C 2 2   ? 153.928 215.996 248.054 1.00 88.25  ? 2   VAL D CG2 1 
ATOM 3259 N N   . GLN C 2 3   ? 153.014 217.336 252.461 1.00 94.81  ? 3   GLN D N   1 
ATOM 3260 C CA  . GLN C 2 3   ? 153.250 217.822 253.811 1.00 100.15 ? 3   GLN D CA  1 
ATOM 3261 C C   . GLN C 2 3   ? 153.659 216.675 254.722 1.00 94.26  ? 3   GLN D C   1 
ATOM 3262 O O   . GLN C 2 3   ? 153.126 215.566 254.620 1.00 90.18  ? 3   GLN D O   1 
ATOM 3263 C CB  . GLN C 2 3   ? 152.004 218.517 254.374 1.00 105.65 ? 3   GLN D CB  1 
ATOM 3264 C CG  . GLN C 2 3   ? 151.739 219.888 253.772 1.00 108.84 ? 3   GLN D CG  1 
ATOM 3265 C CD  . GLN C 2 3   ? 150.269 220.256 253.780 1.00 114.10 ? 3   GLN D CD  1 
ATOM 3266 O OE1 . GLN C 2 3   ? 149.480 219.690 254.537 1.00 120.61 ? 3   GLN D OE1 1 
ATOM 3267 N NE2 . GLN C 2 3   ? 149.893 221.209 252.936 1.00 107.73 ? 3   GLN D NE2 1 
ATOM 3268 N N   . LEU C 2 4   ? 154.611 216.953 255.608 1.00 91.99  ? 4   LEU D N   1 
ATOM 3269 C CA  . LEU C 2 4   ? 155.049 216.020 256.640 1.00 90.14  ? 4   LEU D CA  1 
ATOM 3270 C C   . LEU C 2 4   ? 154.668 216.610 257.991 1.00 96.30  ? 4   LEU D C   1 
ATOM 3271 O O   . LEU C 2 4   ? 155.125 217.702 258.344 1.00 100.29 ? 4   LEU D O   1 
ATOM 3272 C CB  . LEU C 2 4   ? 156.558 215.777 256.565 1.00 89.27  ? 4   LEU D CB  1 
ATOM 3273 C CG  . LEU C 2 4   ? 157.168 214.759 255.591 1.00 85.95  ? 4   LEU D CG  1 
ATOM 3274 C CD1 . LEU C 2 4   ? 156.709 213.349 255.926 1.00 85.58  ? 4   LEU D CD1 1 
ATOM 3275 C CD2 . LEU C 2 4   ? 156.898 215.090 254.123 1.00 84.28  ? 4   LEU D CD2 1 
ATOM 3276 N N   . GLN C 2 5   ? 153.840 215.891 258.745 1.00 98.51  ? 5   GLN D N   1 
ATOM 3277 C CA  . GLN C 2 5   ? 153.287 216.394 259.995 1.00 104.04 ? 5   GLN D CA  1 
ATOM 3278 C C   . GLN C 2 5   ? 153.727 215.505 261.147 1.00 103.83 ? 5   GLN D C   1 
ATOM 3279 O O   . GLN C 2 5   ? 153.453 214.302 261.145 1.00 103.64 ? 5   GLN D O   1 
ATOM 3280 C CB  . GLN C 2 5   ? 151.756 216.455 259.933 1.00 107.16 ? 5   GLN D CB  1 
ATOM 3281 C CG  . GLN C 2 5   ? 151.076 216.818 261.251 1.00 107.48 ? 5   GLN D CG  1 
ATOM 3282 C CD  . GLN C 2 5   ? 151.630 218.079 261.895 1.00 111.08 ? 5   GLN D CD  1 
ATOM 3283 O OE1 . GLN C 2 5   ? 151.943 219.058 261.215 1.00 113.91 ? 5   GLN D OE1 1 
ATOM 3284 N NE2 . GLN C 2 5   ? 151.757 218.057 263.217 1.00 108.92 ? 5   GLN D NE2 1 
ATOM 3285 N N   . GLU C 2 6   ? 154.365 216.111 262.144 1.00 103.25 ? 6   GLU D N   1 
ATOM 3286 C CA  . GLU C 2 6   ? 154.940 215.410 263.281 1.00 100.65 ? 6   GLU D CA  1 
ATOM 3287 C C   . GLU C 2 6   ? 153.954 215.362 264.441 1.00 103.04 ? 6   GLU D C   1 
ATOM 3288 O O   . GLU C 2 6   ? 153.002 216.144 264.514 1.00 107.94 ? 6   GLU D O   1 
ATOM 3289 C CB  . GLU C 2 6   ? 156.238 216.089 263.735 1.00 100.33 ? 6   GLU D CB  1 
ATOM 3290 C CG  . GLU C 2 6   ? 157.301 216.188 262.661 1.00 101.86 ? 6   GLU D CG  1 
ATOM 3291 C CD  . GLU C 2 6   ? 157.302 217.524 261.964 1.00 95.99  ? 6   GLU D CD  1 
ATOM 3292 O OE1 . GLU C 2 6   ? 156.330 218.288 262.141 1.00 92.83  ? 6   GLU D OE1 1 
ATOM 3293 O OE2 . GLU C 2 6   ? 158.275 217.815 261.237 1.00 93.77  ? 6   GLU D OE2 1 
ATOM 3294 N N   . SER C 2 7   ? 154.199 214.423 265.353 1.00 100.71 ? 7   SER D N   1 
ATOM 3295 C CA  . SER C 2 7   ? 153.386 214.281 266.552 1.00 104.32 ? 7   SER D CA  1 
ATOM 3296 C C   . SER C 2 7   ? 154.264 213.775 267.687 1.00 106.95 ? 7   SER D C   1 
ATOM 3297 O O   . SER C 2 7   ? 155.308 213.156 267.464 1.00 107.39 ? 7   SER D O   1 
ATOM 3298 C CB  . SER C 2 7   ? 152.202 213.334 266.322 1.00 105.81 ? 7   SER D CB  1 
ATOM 3299 O OG  . SER C 2 7   ? 151.569 213.002 267.545 1.00 107.60 ? 7   SER D OG  1 
ATOM 3300 N N   . GLY C 2 8   ? 153.824 214.044 268.914 1.00 111.12 ? 8   GLY D N   1 
ATOM 3301 C CA  . GLY C 2 8   ? 154.561 213.624 270.090 1.00 114.05 ? 8   GLY D CA  1 
ATOM 3302 C C   . GLY C 2 8   ? 154.834 214.753 271.063 1.00 117.98 ? 8   GLY D C   1 
ATOM 3303 O O   . GLY C 2 8   ? 153.950 215.568 271.340 1.00 122.08 ? 8   GLY D O   1 
ATOM 3304 N N   . GLY C 2 9   ? 156.055 214.810 271.589 1.00 114.47 ? 9   GLY D N   1 
ATOM 3305 C CA  . GLY C 2 9   ? 156.422 215.846 272.530 1.00 113.56 ? 9   GLY D CA  1 
ATOM 3306 C C   . GLY C 2 9   ? 155.868 215.593 273.920 1.00 121.93 ? 9   GLY D C   1 
ATOM 3307 O O   . GLY C 2 9   ? 155.284 214.547 274.220 1.00 126.20 ? 9   GLY D O   1 
ATOM 3308 N N   . GLY C 2 10  ? 156.066 216.587 274.786 1.00 122.45 ? 10  GLY D N   1 
ATOM 3309 C CA  . GLY C 2 10  ? 155.550 216.552 276.135 1.00 127.28 ? 10  GLY D CA  1 
ATOM 3310 C C   . GLY C 2 10  ? 156.637 216.862 277.140 1.00 127.89 ? 10  GLY D C   1 
ATOM 3311 O O   . GLY C 2 10  ? 157.687 217.419 276.801 1.00 124.23 ? 10  GLY D O   1 
ATOM 3312 N N   . LEU C 2 11  ? 156.374 216.493 278.391 1.00 132.11 ? 11  LEU D N   1 
ATOM 3313 C CA  . LEU C 2 11  ? 157.282 216.720 279.514 1.00 136.15 ? 11  LEU D CA  1 
ATOM 3314 C C   . LEU C 2 11  ? 157.705 215.354 280.043 1.00 142.80 ? 11  LEU D C   1 
ATOM 3315 O O   . LEU C 2 11  ? 157.059 214.791 280.930 1.00 145.08 ? 11  LEU D O   1 
ATOM 3316 C CB  . LEU C 2 11  ? 156.623 217.571 280.616 1.00 140.01 ? 11  LEU D CB  1 
ATOM 3317 C CG  . LEU C 2 11  ? 156.595 219.103 280.521 1.00 139.79 ? 11  LEU D CG  1 
ATOM 3318 C CD1 . LEU C 2 11  ? 158.010 219.667 280.559 1.00 137.32 ? 11  LEU D CD1 1 
ATOM 3319 C CD2 . LEU C 2 11  ? 155.831 219.623 279.305 1.00 135.35 ? 11  LEU D CD2 1 
ATOM 3320 N N   . VAL C 2 12  ? 158.791 214.823 279.496 1.00 145.01 ? 12  VAL D N   1 
ATOM 3321 C CA  . VAL C 2 12  ? 159.286 213.515 279.896 1.00 150.56 ? 12  VAL D CA  1 
ATOM 3322 C C   . VAL C 2 12  ? 160.418 213.685 280.902 1.00 147.82 ? 12  VAL D C   1 
ATOM 3323 O O   . VAL C 2 12  ? 160.998 214.763 281.055 1.00 142.42 ? 12  VAL D O   1 
ATOM 3324 C CB  . VAL C 2 12  ? 159.742 212.686 278.679 1.00 148.70 ? 12  VAL D CB  1 
ATOM 3325 C CG1 . VAL C 2 12  ? 158.570 212.427 277.747 1.00 144.99 ? 12  VAL D CG1 1 
ATOM 3326 C CG2 . VAL C 2 12  ? 160.859 213.400 277.943 1.00 143.65 ? 12  VAL D CG2 1 
ATOM 3327 N N   . GLN C 2 13  ? 160.724 212.601 281.604 1.00 151.45 ? 13  GLN D N   1 
ATOM 3328 C CA  . GLN C 2 13  ? 161.787 212.533 282.592 1.00 150.70 ? 13  GLN D CA  1 
ATOM 3329 C C   . GLN C 2 13  ? 162.936 211.676 282.074 1.00 148.23 ? 13  GLN D C   1 
ATOM 3330 O O   . GLN C 2 13  ? 162.760 210.902 281.126 1.00 147.07 ? 13  GLN D O   1 
ATOM 3331 C CB  . GLN C 2 13  ? 161.255 211.953 283.911 1.00 154.12 ? 13  GLN D CB  1 
ATOM 3332 C CG  . GLN C 2 13  ? 160.242 212.846 284.610 1.00 152.12 ? 13  GLN D CG  1 
ATOM 3333 C CD  . GLN C 2 13  ? 159.718 212.242 285.897 1.00 153.32 ? 13  GLN D CD  1 
ATOM 3334 O OE1 . GLN C 2 13  ? 160.059 211.113 286.251 1.00 157.29 ? 13  GLN D OE1 1 
ATOM 3335 N NE2 . GLN C 2 13  ? 158.885 212.994 286.607 1.00 151.25 ? 13  GLN D NE2 1 
ATOM 3336 N N   . PRO C 2 14  ? 164.143 211.836 282.628 1.00 145.71 ? 14  PRO D N   1 
ATOM 3337 C CA  . PRO C 2 14  ? 165.252 210.945 282.254 1.00 141.12 ? 14  PRO D CA  1 
ATOM 3338 C C   . PRO C 2 14  ? 164.924 209.485 282.536 1.00 144.41 ? 14  PRO D C   1 
ATOM 3339 O O   . PRO C 2 14  ? 164.363 209.144 283.580 1.00 145.74 ? 14  PRO D O   1 
ATOM 3340 C CB  . PRO C 2 14  ? 166.415 211.428 283.128 1.00 138.84 ? 14  PRO D CB  1 
ATOM 3341 C CG  . PRO C 2 14  ? 166.035 212.778 283.629 1.00 136.52 ? 14  PRO D CG  1 
ATOM 3342 C CD  . PRO C 2 14  ? 164.619 213.078 283.263 1.00 141.64 ? 14  PRO D CD  1 
ATOM 3343 N N   . GLY C 2 15  ? 165.287 208.622 281.590 1.00 141.97 ? 15  GLY D N   1 
ATOM 3344 C CA  . GLY C 2 15  ? 164.953 207.217 281.673 1.00 142.57 ? 15  GLY D CA  1 
ATOM 3345 C C   . GLY C 2 15  ? 163.557 206.863 281.210 1.00 143.08 ? 15  GLY D C   1 
ATOM 3346 O O   . GLY C 2 15  ? 163.183 205.685 281.276 1.00 141.95 ? 15  GLY D O   1 
ATOM 3347 N N   . GLY C 2 16  ? 162.778 207.835 280.745 1.00 145.64 ? 16  GLY D N   1 
ATOM 3348 C CA  . GLY C 2 16  ? 161.428 207.588 280.290 1.00 145.30 ? 16  GLY D CA  1 
ATOM 3349 C C   . GLY C 2 16  ? 161.388 207.087 278.859 1.00 141.62 ? 16  GLY D C   1 
ATOM 3350 O O   . GLY C 2 16  ? 162.407 206.798 278.231 1.00 135.95 ? 16  GLY D O   1 
ATOM 3351 N N   . SER C 2 17  ? 160.168 206.989 278.336 1.00 142.07 ? 17  SER D N   1 
ATOM 3352 C CA  . SER C 2 17  ? 159.937 206.476 276.996 1.00 134.37 ? 17  SER D CA  1 
ATOM 3353 C C   . SER C 2 17  ? 159.031 207.422 276.221 1.00 132.87 ? 17  SER D C   1 
ATOM 3354 O O   . SER C 2 17  ? 158.154 208.078 276.791 1.00 136.77 ? 17  SER D O   1 
ATOM 3355 C CB  . SER C 2 17  ? 159.317 205.072 277.031 1.00 131.53 ? 17  SER D CB  1 
ATOM 3356 O OG  . SER C 2 17  ? 158.013 205.104 277.585 1.00 130.89 ? 17  SER D OG  1 
ATOM 3357 N N   . LEU C 2 18  ? 159.256 207.482 274.911 1.00 126.85 ? 18  LEU D N   1 
ATOM 3358 C CA  . LEU C 2 18  ? 158.450 208.299 274.018 1.00 121.61 ? 18  LEU D CA  1 
ATOM 3359 C C   . LEU C 2 18  ? 158.479 207.674 272.632 1.00 114.11 ? 18  LEU D C   1 
ATOM 3360 O O   . LEU C 2 18  ? 159.378 206.896 272.299 1.00 111.69 ? 18  LEU D O   1 
ATOM 3361 C CB  . LEU C 2 18  ? 158.951 209.748 273.968 1.00 118.61 ? 18  LEU D CB  1 
ATOM 3362 C CG  . LEU C 2 18  ? 157.914 210.841 273.694 1.00 121.05 ? 18  LEU D CG  1 
ATOM 3363 C CD1 . LEU C 2 18  ? 156.647 210.616 274.510 1.00 127.46 ? 18  LEU D CD1 1 
ATOM 3364 C CD2 . LEU C 2 18  ? 158.498 212.218 273.969 1.00 123.42 ? 18  LEU D CD2 1 
ATOM 3365 N N   . ARG C 2 19  ? 157.478 208.020 271.822 1.00 109.02 ? 19  ARG D N   1 
ATOM 3366 C CA  . ARG C 2 19  ? 157.374 207.511 270.452 1.00 103.89 ? 19  ARG D CA  1 
ATOM 3367 C C   . ARG C 2 19  ? 156.974 208.676 269.549 1.00 98.84  ? 19  ARG D C   1 
ATOM 3368 O O   . ARG C 2 19  ? 155.786 208.941 269.345 1.00 97.10  ? 19  ARG D O   1 
ATOM 3369 C CB  . ARG C 2 19  ? 156.379 206.361 270.366 1.00 99.25  ? 19  ARG D CB  1 
ATOM 3370 C CG  . ARG C 2 19  ? 156.645 205.399 269.222 1.00 93.74  ? 19  ARG D CG  1 
ATOM 3371 C CD  . ARG C 2 19  ? 156.027 204.037 269.490 1.00 95.71  ? 19  ARG D CD  1 
ATOM 3372 N NE  . ARG C 2 19  ? 154.608 204.000 269.157 1.00 96.77  ? 19  ARG D NE  1 
ATOM 3373 C CZ  . ARG C 2 19  ? 154.087 203.261 268.188 1.00 100.81 ? 19  ARG D CZ  1 
ATOM 3374 N NH1 . ARG C 2 19  ? 154.841 202.482 267.430 1.00 101.93 ? 19  ARG D NH1 1 
ATOM 3375 N NH2 . ARG C 2 19  ? 152.774 203.301 267.976 1.00 103.17 ? 19  ARG D NH2 1 
ATOM 3376 N N   . LEU C 2 20  ? 157.975 209.369 269.015 1.00 95.11  ? 20  LEU D N   1 
ATOM 3377 C CA  . LEU C 2 20  ? 157.724 210.405 268.026 1.00 93.42  ? 20  LEU D CA  1 
ATOM 3378 C C   . LEU C 2 20  ? 157.292 209.779 266.706 1.00 94.05  ? 20  LEU D C   1 
ATOM 3379 O O   . LEU C 2 20  ? 157.755 208.703 266.318 1.00 96.02  ? 20  LEU D O   1 
ATOM 3380 C CB  . LEU C 2 20  ? 158.971 211.264 267.819 1.00 93.41  ? 20  LEU D CB  1 
ATOM 3381 C CG  . LEU C 2 20  ? 159.438 212.140 268.983 1.00 100.13 ? 20  LEU D CG  1 
ATOM 3382 C CD1 . LEU C 2 20  ? 160.320 213.264 268.468 1.00 101.26 ? 20  LEU D CD1 1 
ATOM 3383 C CD2 . LEU C 2 20  ? 158.258 212.704 269.764 1.00 108.37 ? 20  LEU D CD2 1 
ATOM 3384 N N   . SER C 2 21  ? 156.387 210.465 266.013 1.00 92.98  ? 21  SER D N   1 
ATOM 3385 C CA  . SER C 2 21  ? 155.813 209.951 264.776 1.00 93.93  ? 21  SER D CA  1 
ATOM 3386 C C   . SER C 2 21  ? 155.496 211.115 263.855 1.00 98.08  ? 21  SER D C   1 
ATOM 3387 O O   . SER C 2 21  ? 154.701 211.988 264.216 1.00 102.54 ? 21  SER D O   1 
ATOM 3388 C CB  . SER C 2 21  ? 154.547 209.140 265.060 1.00 92.91  ? 21  SER D CB  1 
ATOM 3389 O OG  . SER C 2 21  ? 153.569 209.936 265.706 1.00 96.15  ? 21  SER D OG  1 
ATOM 3390 N N   . CYS C 2 22  ? 156.106 211.135 262.673 1.00 91.60  ? 22  CYS D N   1 
ATOM 3391 C CA  . CYS C 2 22  ? 155.726 212.096 261.648 1.00 91.28  ? 22  CYS D CA  1 
ATOM 3392 C C   . CYS C 2 22  ? 155.109 211.357 260.469 1.00 91.67  ? 22  CYS D C   1 
ATOM 3393 O O   . CYS C 2 22  ? 155.686 210.390 259.959 1.00 87.68  ? 22  CYS D O   1 
ATOM 3394 C CB  . CYS C 2 22  ? 156.896 212.976 261.209 1.00 94.60  ? 22  CYS D CB  1 
ATOM 3395 S SG  . CYS C 2 22  ? 158.331 212.298 260.384 1.00 93.96  ? 22  CYS D SG  1 
ATOM 3396 N N   . THR C 2 23  ? 153.934 211.818 260.050 1.00 97.43  ? 23  THR D N   1 
ATOM 3397 C CA  . THR C 2 23  ? 153.084 211.130 259.088 1.00 93.65  ? 23  THR D CA  1 
ATOM 3398 C C   . THR C 2 23  ? 153.208 211.800 257.728 1.00 89.84  ? 23  THR D C   1 
ATOM 3399 O O   . THR C 2 23  ? 153.080 213.025 257.621 1.00 89.73  ? 23  THR D O   1 
ATOM 3400 C CB  . THR C 2 23  ? 151.624 211.147 259.559 1.00 88.49  ? 23  THR D CB  1 
ATOM 3401 O OG1 . THR C 2 23  ? 151.465 210.255 260.668 1.00 90.21  ? 23  THR D OG1 1 
ATOM 3402 C CG2 . THR C 2 23  ? 150.675 210.725 258.443 1.00 82.04  ? 23  THR D CG2 1 
ATOM 3403 N N   . ALA C 2 24  ? 153.458 211.000 256.695 1.00 88.18  ? 24  ALA D N   1 
ATOM 3404 C CA  . ALA C 2 24  ? 153.531 211.485 255.325 1.00 85.87  ? 24  ALA D CA  1 
ATOM 3405 C C   . ALA C 2 24  ? 152.149 211.431 254.693 1.00 84.35  ? 24  ALA D C   1 
ATOM 3406 O O   . ALA C 2 24  ? 151.506 210.376 254.684 1.00 85.58  ? 24  ALA D O   1 
ATOM 3407 C CB  . ALA C 2 24  ? 154.516 210.657 254.501 1.00 86.42  ? 24  ALA D CB  1 
ATOM 3408 N N   . SER C 2 25  ? 151.698 212.568 254.166 1.00 82.86  ? 25  SER D N   1 
ATOM 3409 C CA  . SER C 2 25  ? 150.408 212.639 253.487 1.00 81.79  ? 25  SER D CA  1 
ATOM 3410 C C   . SER C 2 25  ? 150.559 212.426 251.984 1.00 81.74  ? 25  SER D C   1 
ATOM 3411 O O   . SER C 2 25  ? 149.988 211.486 251.422 1.00 87.41  ? 25  SER D O   1 
ATOM 3412 C CB  . SER C 2 25  ? 149.737 213.986 253.774 1.00 82.33  ? 25  SER D CB  1 
ATOM 3413 O OG  . SER C 2 25  ? 148.553 214.134 253.009 1.00 84.80  ? 25  SER D OG  1 
ATOM 3414 N N   . GLY C 2 26  ? 151.331 213.286 251.326 1.00 78.12  ? 26  GLY D N   1 
ATOM 3415 C CA  . GLY C 2 26  ? 151.481 213.226 249.886 1.00 75.31  ? 26  GLY D CA  1 
ATOM 3416 C C   . GLY C 2 26  ? 152.284 212.049 249.375 1.00 71.45  ? 26  GLY D C   1 
ATOM 3417 O O   . GLY C 2 26  ? 151.748 211.165 248.700 1.00 63.49  ? 26  GLY D O   1 
ATOM 3418 N N   . ILE C 2 27  ? 153.578 212.031 249.688 1.00 72.72  ? 27  ILE D N   1 
ATOM 3419 C CA  . ILE C 2 27  ? 154.473 210.980 249.220 1.00 65.85  ? 27  ILE D CA  1 
ATOM 3420 C C   . ILE C 2 27  ? 154.220 209.698 249.997 1.00 68.50  ? 27  ILE D C   1 
ATOM 3421 O O   . ILE C 2 27  ? 153.546 209.703 251.033 1.00 76.24  ? 27  ILE D O   1 
ATOM 3422 C CB  . ILE C 2 27  ? 155.947 211.404 249.344 1.00 64.43  ? 27  ILE D CB  1 
ATOM 3423 C CG1 . ILE C 2 27  ? 156.300 211.663 250.811 1.00 66.54  ? 27  ILE D CG1 1 
ATOM 3424 C CG2 . ILE C 2 27  ? 156.230 212.617 248.475 1.00 70.58  ? 27  ILE D CG2 1 
ATOM 3425 C CD1 . ILE C 2 27  ? 157.777 211.858 251.062 1.00 64.84  ? 27  ILE D CD1 1 
ATOM 3426 N N   . ALA C 2 28  ? 154.763 208.594 249.500 1.00 65.51  ? 28  ALA D N   1 
ATOM 3427 C CA  . ALA C 2 28  ? 154.678 207.305 250.160 1.00 63.80  ? 28  ALA D CA  1 
ATOM 3428 C C   . ALA C 2 28  ? 156.048 206.898 250.681 1.00 65.66  ? 28  ALA D C   1 
ATOM 3429 O O   . ALA C 2 28  ? 157.077 207.196 250.068 1.00 66.25  ? 28  ALA D O   1 
ATOM 3430 C CB  . ALA C 2 28  ? 154.155 206.229 249.205 1.00 57.56  ? 28  ALA D CB  1 
ATOM 3431 N N   . LEU C 2 29  ? 156.079 206.374 251.909 1.00 66.71  ? 29  LEU D N   1 
ATOM 3432 C CA  . LEU C 2 29  ? 157.397 206.107 252.543 1.00 63.99  ? 29  LEU D CA  1 
ATOM 3433 C C   . LEU C 2 29  ? 157.800 204.638 252.387 1.00 65.70  ? 29  LEU D C   1 
ATOM 3434 O O   . LEU C 2 29  ? 157.980 203.966 253.416 1.00 71.91  ? 29  LEU D O   1 
ATOM 3435 C CB  . LEU C 2 29  ? 157.380 206.542 254.007 1.00 70.57  ? 29  LEU D CB  1 
ATOM 3436 C CG  . LEU C 2 29  ? 157.210 208.046 254.236 1.00 72.30  ? 29  LEU D CG  1 
ATOM 3437 C CD1 . LEU C 2 29  ? 157.063 208.305 255.723 1.00 69.56  ? 29  LEU D CD1 1 
ATOM 3438 C CD2 . LEU C 2 29  ? 158.408 208.796 253.687 1.00 61.45  ? 29  LEU D CD2 1 
ATOM 3439 N N   . HIS C 2 30  ? 157.890 204.159 251.153 1.00 63.47  ? 30  HIS D N   1 
ATOM 3440 C CA  . HIS C 2 30  ? 158.416 202.794 250.897 1.00 64.80  ? 30  HIS D CA  1 
ATOM 3441 C C   . HIS C 2 30  ? 159.187 202.963 249.592 1.00 62.54  ? 30  HIS D C   1 
ATOM 3442 O O   . HIS C 2 30  ? 159.880 202.028 249.144 1.00 65.38  ? 30  HIS D O   1 
ATOM 3443 C CB  . HIS C 2 30  ? 157.295 201.751 250.878 1.00 68.41  ? 30  HIS D CB  1 
ATOM 3444 C CG  . HIS C 2 30  ? 156.272 201.969 249.817 1.00 73.74  ? 30  HIS D CG  1 
ATOM 3445 N ND1 . HIS C 2 30  ? 155.132 202.717 250.019 1.00 79.32  ? 30  HIS D ND1 1 
ATOM 3446 C CD2 . HIS C 2 30  ? 156.211 201.532 248.554 1.00 77.17  ? 30  HIS D CD2 1 
ATOM 3447 C CE1 . HIS C 2 30  ? 154.415 202.727 248.905 1.00 82.41  ? 30  HIS D CE1 1 
ATOM 3448 N NE2 . HIS C 2 30  ? 155.052 202.014 248.002 1.00 84.76  ? 30  HIS D NE2 1 
ATOM 3449 N N   . THR C 2 31  ? 159.056 204.155 249.003 1.00 61.55  ? 31  THR D N   1 
ATOM 3450 C CA  . THR C 2 31  ? 159.782 204.473 247.762 1.00 61.80  ? 31  THR D CA  1 
ATOM 3451 C C   . THR C 2 31  ? 160.605 205.710 248.024 1.00 58.80  ? 31  THR D C   1 
ATOM 3452 O O   . THR C 2 31  ? 161.485 206.019 247.197 1.00 56.44  ? 31  THR D O   1 
ATOM 3453 C CB  . THR C 2 31  ? 158.777 204.693 246.637 1.00 65.71  ? 31  THR D CB  1 
ATOM 3454 O OG1 . THR C 2 31  ? 159.546 205.198 245.550 1.00 75.98  ? 31  THR D OG1 1 
ATOM 3455 C CG2 . THR C 2 31  ? 157.697 205.690 247.011 1.00 62.43  ? 31  THR D CG2 1 
ATOM 3456 N N   . HIS C 2 32  ? 160.332 206.402 249.133 1.00 57.67  ? 32  HIS D N   1 
ATOM 3457 C CA  . HIS C 2 32  ? 161.142 207.590 249.514 1.00 55.38  ? 32  HIS D CA  1 
ATOM 3458 C C   . HIS C 2 32  ? 162.006 207.218 250.722 1.00 55.69  ? 32  HIS D C   1 
ATOM 3459 O O   . HIS C 2 32  ? 161.659 206.254 251.435 1.00 60.37  ? 32  HIS D O   1 
ATOM 3460 C CB  . HIS C 2 32  ? 160.237 208.788 249.815 1.00 61.09  ? 32  HIS D CB  1 
ATOM 3461 C CG  . HIS C 2 32  ? 159.552 209.349 248.616 1.00 63.29  ? 32  HIS D CG  1 
ATOM 3462 N ND1 . HIS C 2 32  ? 158.343 208.878 248.155 1.00 67.08  ? 32  HIS D ND1 1 
ATOM 3463 C CD2 . HIS C 2 32  ? 159.909 210.333 247.785 1.00 59.64  ? 32  HIS D CD2 1 
ATOM 3464 C CE1 . HIS C 2 32  ? 157.990 209.565 247.078 1.00 64.03  ? 32  HIS D CE1 1 
ATOM 3465 N NE2 . HIS C 2 32  ? 158.927 210.456 246.838 1.00 60.89  ? 32  HIS D NE2 1 
ATOM 3466 N N   . ALA C 2 33  ? 163.100 207.952 250.941 1.00 49.97  ? 33  ALA D N   1 
ATOM 3467 C CA  . ALA C 2 33  ? 163.994 207.666 252.088 1.00 48.39  ? 33  ALA D CA  1 
ATOM 3468 C C   . ALA C 2 33  ? 163.922 208.812 253.093 1.00 46.70  ? 33  ALA D C   1 
ATOM 3469 O O   . ALA C 2 33  ? 164.261 209.951 252.716 1.00 51.53  ? 33  ALA D O   1 
ATOM 3470 C CB  . ALA C 2 33  ? 165.403 207.460 251.600 1.00 51.47  ? 33  ALA D CB  1 
ATOM 3471 N N   . THR C 2 34  ? 163.524 208.517 254.333 1.00 43.40  ? 34  THR D N   1 
ATOM 3472 C CA  . THR C 2 34  ? 163.342 209.595 255.328 1.00 45.44  ? 34  THR D CA  1 
ATOM 3473 C C   . THR C 2 34  ? 164.365 209.487 256.431 1.00 48.56  ? 34  THR D C   1 
ATOM 3474 O O   . THR C 2 34  ? 165.185 208.548 256.392 1.00 55.21  ? 34  THR D O   1 
ATOM 3475 C CB  . THR C 2 34  ? 161.927 209.534 255.897 1.00 47.86  ? 34  THR D CB  1 
ATOM 3476 O OG1 . THR C 2 34  ? 161.793 210.722 256.669 1.00 56.64  ? 34  THR D OG1 1 
ATOM 3477 C CG2 . THR C 2 34  ? 161.700 208.318 256.776 1.00 50.63  ? 34  THR D CG2 1 
ATOM 3478 N N   . GLY C 2 35  ? 164.327 210.421 257.380 1.00 49.95  ? 35  GLY D N   1 
ATOM 3479 C CA  . GLY C 2 35  ? 165.221 210.414 258.519 1.00 59.18  ? 35  GLY D CA  1 
ATOM 3480 C C   . GLY C 2 35  ? 164.793 211.487 259.495 1.00 68.40  ? 35  GLY D C   1 
ATOM 3481 O O   . GLY C 2 35  ? 163.838 212.227 259.256 1.00 70.45  ? 35  GLY D O   1 
ATOM 3482 N N   . TRP C 2 36  ? 165.518 211.569 260.606 1.00 72.22  ? 36  TRP D N   1 
ATOM 3483 C CA  . TRP C 2 36  ? 165.220 212.525 261.663 1.00 73.32  ? 36  TRP D CA  1 
ATOM 3484 C C   . TRP C 2 36  ? 166.405 213.451 261.889 1.00 80.80  ? 36  TRP D C   1 
ATOM 3485 O O   . TRP C 2 36  ? 167.561 213.018 261.858 1.00 88.23  ? 36  TRP D O   1 
ATOM 3486 C CB  . TRP C 2 36  ? 164.862 211.815 262.970 1.00 73.74  ? 36  TRP D CB  1 
ATOM 3487 C CG  . TRP C 2 36  ? 163.491 211.224 262.970 1.00 80.40  ? 36  TRP D CG  1 
ATOM 3488 C CD1 . TRP C 2 36  ? 163.109 210.044 262.410 1.00 85.99  ? 36  TRP D CD1 1 
ATOM 3489 C CD2 . TRP C 2 36  ? 162.316 211.786 263.565 1.00 80.58  ? 36  TRP D CD2 1 
ATOM 3490 N NE1 . TRP C 2 36  ? 161.767 209.834 262.615 1.00 84.90  ? 36  TRP D NE1 1 
ATOM 3491 C CE2 . TRP C 2 36  ? 161.257 210.890 263.323 1.00 84.17  ? 36  TRP D CE2 1 
ATOM 3492 C CE3 . TRP C 2 36  ? 162.056 212.960 264.276 1.00 87.83  ? 36  TRP D CE3 1 
ATOM 3493 C CZ2 . TRP C 2 36  ? 159.960 211.131 263.767 1.00 90.38  ? 36  TRP D CZ2 1 
ATOM 3494 C CZ3 . TRP C 2 36  ? 160.767 213.197 264.716 1.00 88.95  ? 36  TRP D CZ3 1 
ATOM 3495 C CH2 . TRP C 2 36  ? 159.736 212.288 264.459 1.00 89.80  ? 36  TRP D CH2 1 
ATOM 3496 N N   . PHE C 2 37  ? 166.107 214.731 262.100 1.00 79.55  ? 37  PHE D N   1 
ATOM 3497 C CA  . PHE C 2 37  ? 167.106 215.736 262.425 1.00 82.82  ? 37  PHE D CA  1 
ATOM 3498 C C   . PHE C 2 37  ? 166.590 216.590 263.573 1.00 90.60  ? 37  PHE D C   1 
ATOM 3499 O O   . PHE C 2 37  ? 165.380 216.761 263.745 1.00 90.66  ? 37  PHE D O   1 
ATOM 3500 C CB  . PHE C 2 37  ? 167.433 216.628 261.222 1.00 78.83  ? 37  PHE D CB  1 
ATOM 3501 C CG  . PHE C 2 37  ? 167.445 215.898 259.913 1.00 77.89  ? 37  PHE D CG  1 
ATOM 3502 C CD1 . PHE C 2 37  ? 168.487 215.045 259.588 1.00 76.78  ? 37  PHE D CD1 1 
ATOM 3503 C CD2 . PHE C 2 37  ? 166.404 216.053 259.014 1.00 79.67  ? 37  PHE D CD2 1 
ATOM 3504 C CE1 . PHE C 2 37  ? 168.494 214.367 258.384 1.00 70.77  ? 37  PHE D CE1 1 
ATOM 3505 C CE2 . PHE C 2 37  ? 166.405 215.378 257.809 1.00 79.52  ? 37  PHE D CE2 1 
ATOM 3506 C CZ  . PHE C 2 37  ? 167.451 214.533 257.495 1.00 71.39  ? 37  PHE D CZ  1 
ATOM 3507 N N   . ARG C 2 38  ? 167.518 217.126 264.360 1.00 99.28  ? 38  ARG D N   1 
ATOM 3508 C CA  . ARG C 2 38  ? 167.169 217.934 265.518 1.00 105.31 ? 38  ARG D CA  1 
ATOM 3509 C C   . ARG C 2 38  ? 168.131 219.107 265.623 1.00 113.61 ? 38  ARG D C   1 
ATOM 3510 O O   . ARG C 2 38  ? 169.237 219.080 265.077 1.00 113.30 ? 38  ARG D O   1 
ATOM 3511 C CB  . ARG C 2 38  ? 167.181 217.098 266.806 1.00 106.20 ? 38  ARG D CB  1 
ATOM 3512 C CG  . ARG C 2 38  ? 168.539 216.989 267.480 1.00 109.23 ? 38  ARG D CG  1 
ATOM 3513 C CD  . ARG C 2 38  ? 168.417 216.372 268.861 1.00 112.97 ? 38  ARG D CD  1 
ATOM 3514 N NE  . ARG C 2 38  ? 169.659 215.733 269.280 1.00 121.07 ? 38  ARG D NE  1 
ATOM 3515 C CZ  . ARG C 2 38  ? 169.781 214.971 270.359 1.00 123.10 ? 38  ARG D CZ  1 
ATOM 3516 N NH1 . ARG C 2 38  ? 168.749 214.721 271.148 1.00 122.20 ? 38  ARG D NH1 1 
ATOM 3517 N NH2 . ARG C 2 38  ? 170.966 214.444 270.650 1.00 125.23 ? 38  ARG D NH2 1 
ATOM 3518 N N   . GLN C 2 39  ? 167.691 220.149 266.326 1.00 118.61 ? 39  GLN D N   1 
ATOM 3519 C CA  . GLN C 2 39  ? 168.505 221.344 266.536 1.00 122.43 ? 39  GLN D CA  1 
ATOM 3520 C C   . GLN C 2 39  ? 168.334 221.801 267.977 1.00 127.82 ? 39  GLN D C   1 
ATOM 3521 O O   . GLN C 2 39  ? 167.257 222.271 268.357 1.00 127.38 ? 39  GLN D O   1 
ATOM 3522 C CB  . GLN C 2 39  ? 168.119 222.462 265.569 1.00 118.32 ? 39  GLN D CB  1 
ATOM 3523 C CG  . GLN C 2 39  ? 169.001 223.698 265.685 1.00 119.68 ? 39  GLN D CG  1 
ATOM 3524 C CD  . GLN C 2 39  ? 168.643 224.771 264.679 1.00 114.52 ? 39  GLN D CD  1 
ATOM 3525 O OE1 . GLN C 2 39  ? 167.703 224.620 263.899 1.00 115.20 ? 39  GLN D OE1 1 
ATOM 3526 N NE2 . GLN C 2 39  ? 169.397 225.864 264.688 1.00 112.99 ? 39  GLN D NE2 1 
ATOM 3527 N N   . ALA C 2 40  ? 169.390 221.661 268.773 1.00 131.67 ? 40  ALA D N   1 
ATOM 3528 C CA  . ALA C 2 40  ? 169.383 222.210 270.115 1.00 135.00 ? 40  ALA D CA  1 
ATOM 3529 C C   . ALA C 2 40  ? 169.484 223.734 270.052 1.00 139.46 ? 40  ALA D C   1 
ATOM 3530 O O   . ALA C 2 40  ? 170.049 224.284 269.102 1.00 135.12 ? 40  ALA D O   1 
ATOM 3531 C CB  . ALA C 2 40  ? 170.541 221.641 270.932 1.00 131.44 ? 40  ALA D CB  1 
ATOM 3532 N N   . PRO C 2 41  ? 168.913 224.439 271.031 1.00 145.27 ? 41  PRO D N   1 
ATOM 3533 C CA  . PRO C 2 41  ? 169.075 225.898 271.073 1.00 143.04 ? 41  PRO D CA  1 
ATOM 3534 C C   . PRO C 2 41  ? 170.528 226.290 271.297 1.00 141.87 ? 41  PRO D C   1 
ATOM 3535 O O   . PRO C 2 41  ? 171.229 225.707 272.127 1.00 144.38 ? 41  PRO D O   1 
ATOM 3536 C CB  . PRO C 2 41  ? 168.193 226.320 272.253 1.00 146.29 ? 41  PRO D CB  1 
ATOM 3537 C CG  . PRO C 2 41  ? 167.192 225.221 272.387 1.00 150.30 ? 41  PRO D CG  1 
ATOM 3538 C CD  . PRO C 2 41  ? 167.930 223.968 272.022 1.00 145.38 ? 41  PRO D CD  1 
ATOM 3539 N N   . GLY C 2 42  ? 170.975 227.289 270.540 1.00 140.59 ? 42  GLY D N   1 
ATOM 3540 C CA  . GLY C 2 42  ? 172.351 227.733 270.605 1.00 142.33 ? 42  GLY D CA  1 
ATOM 3541 C C   . GLY C 2 42  ? 173.346 226.855 269.880 1.00 142.12 ? 42  GLY D C   1 
ATOM 3542 O O   . GLY C 2 42  ? 174.553 227.097 269.990 1.00 141.49 ? 42  GLY D O   1 
ATOM 3543 N N   . LYS C 2 43  ? 172.884 225.848 269.143 1.00 140.72 ? 43  LYS D N   1 
ATOM 3544 C CA  . LYS C 2 43  ? 173.748 224.925 268.420 1.00 137.28 ? 43  LYS D CA  1 
ATOM 3545 C C   . LYS C 2 43  ? 173.276 224.819 266.975 1.00 132.74 ? 43  LYS D C   1 
ATOM 3546 O O   . LYS C 2 43  ? 172.218 225.333 266.602 1.00 128.72 ? 43  LYS D O   1 
ATOM 3547 C CB  . LYS C 2 43  ? 173.765 223.542 269.085 1.00 135.24 ? 43  LYS D CB  1 
ATOM 3548 C CG  . LYS C 2 43  ? 174.372 223.515 270.478 1.00 137.39 ? 43  LYS D CG  1 
ATOM 3549 C CD  . LYS C 2 43  ? 174.288 222.123 271.087 1.00 137.41 ? 43  LYS D CD  1 
ATOM 3550 C CE  . LYS C 2 43  ? 174.959 221.084 270.201 1.00 142.09 ? 43  LYS D CE  1 
ATOM 3551 N NZ  . LYS C 2 43  ? 176.425 221.319 270.081 1.00 146.21 ? 43  LYS D NZ  1 
ATOM 3552 N N   . GLU C 2 44  ? 174.072 224.137 266.157 1.00 130.08 ? 44  GLU D N   1 
ATOM 3553 C CA  . GLU C 2 44  ? 173.737 223.867 264.769 1.00 125.41 ? 44  GLU D CA  1 
ATOM 3554 C C   . GLU C 2 44  ? 173.133 222.472 264.658 1.00 125.54 ? 44  GLU D C   1 
ATOM 3555 O O   . GLU C 2 44  ? 173.472 221.568 265.428 1.00 128.05 ? 44  GLU D O   1 
ATOM 3556 C CB  . GLU C 2 44  ? 174.974 224.022 263.868 1.00 127.72 ? 44  GLU D CB  1 
ATOM 3557 C CG  . GLU C 2 44  ? 176.154 223.092 264.167 1.00 130.65 ? 44  GLU D CG  1 
ATOM 3558 C CD  . GLU C 2 44  ? 176.060 221.749 263.466 1.00 127.15 ? 44  GLU D CD  1 
ATOM 3559 O OE1 . GLU C 2 44  ? 175.318 221.653 262.466 1.00 127.43 ? 44  GLU D OE1 1 
ATOM 3560 O OE2 . GLU C 2 44  ? 176.731 220.794 263.910 1.00 124.00 ? 44  GLU D OE2 1 
ATOM 3561 N N   . ARG C 2 45  ? 172.227 222.309 263.697 1.00 119.66 ? 45  ARG D N   1 
ATOM 3562 C CA  . ARG C 2 45  ? 171.388 221.119 263.635 1.00 115.74 ? 45  ARG D CA  1 
ATOM 3563 C C   . ARG C 2 45  ? 172.159 219.900 263.137 1.00 111.51 ? 45  ARG D C   1 
ATOM 3564 O O   . ARG C 2 45  ? 172.989 219.993 262.229 1.00 116.52 ? 45  ARG D O   1 
ATOM 3565 C CB  . ARG C 2 45  ? 170.163 221.385 262.760 1.00 109.35 ? 45  ARG D CB  1 
ATOM 3566 C CG  . ARG C 2 45  ? 170.428 221.697 261.312 1.00 99.59  ? 45  ARG D CG  1 
ATOM 3567 C CD  . ARG C 2 45  ? 169.099 221.956 260.643 1.00 94.40  ? 45  ARG D CD  1 
ATOM 3568 N NE  . ARG C 2 45  ? 168.268 220.760 260.572 1.00 94.30  ? 45  ARG D NE  1 
ATOM 3569 C CZ  . ARG C 2 45  ? 166.969 220.774 260.302 1.00 89.65  ? 45  ARG D CZ  1 
ATOM 3570 N NH1 . ARG C 2 45  ? 166.310 221.910 260.135 1.00 87.91  ? 45  ARG D NH1 1 
ATOM 3571 N NH2 . ARG C 2 45  ? 166.314 219.622 260.193 1.00 89.70  ? 45  ARG D NH2 1 
ATOM 3572 N N   . GLU C 2 46  ? 171.876 218.752 263.752 1.00 102.07 ? 46  GLU D N   1 
ATOM 3573 C CA  . GLU C 2 46  ? 172.590 217.509 263.497 1.00 99.07  ? 46  GLU D CA  1 
ATOM 3574 C C   . GLU C 2 46  ? 171.575 216.383 263.346 1.00 94.99  ? 46  GLU D C   1 
ATOM 3575 O O   . GLU C 2 46  ? 170.535 216.377 264.009 1.00 96.00  ? 46  GLU D O   1 
ATOM 3576 C CB  . GLU C 2 46  ? 173.594 217.222 264.637 1.00 102.36 ? 46  GLU D CB  1 
ATOM 3577 C CG  . GLU C 2 46  ? 174.197 215.816 264.694 1.00 102.99 ? 46  GLU D CG  1 
ATOM 3578 C CD  . GLU C 2 46  ? 175.245 215.568 263.623 1.00 106.12 ? 46  GLU D CD  1 
ATOM 3579 O OE1 . GLU C 2 46  ? 175.682 216.538 262.967 1.00 111.06 ? 46  GLU D OE1 1 
ATOM 3580 O OE2 . GLU C 2 46  ? 175.635 214.396 263.441 1.00 101.73 ? 46  GLU D OE2 1 
ATOM 3581 N N   . GLY C 2 47  ? 171.882 215.432 262.462 1.00 91.98  ? 47  GLY D N   1 
ATOM 3582 C CA  . GLY C 2 47  ? 170.955 214.355 262.182 1.00 87.11  ? 47  GLY D CA  1 
ATOM 3583 C C   . GLY C 2 47  ? 170.813 213.375 263.331 1.00 86.31  ? 47  GLY D C   1 
ATOM 3584 O O   . GLY C 2 47  ? 171.580 213.370 264.294 1.00 92.67  ? 47  GLY D O   1 
ATOM 3585 N N   . VAL C 2 48  ? 169.790 212.523 263.216 1.00 82.52  ? 48  VAL D N   1 
ATOM 3586 C CA  . VAL C 2 48  ? 169.453 211.547 264.242 1.00 82.02  ? 48  VAL D CA  1 
ATOM 3587 C C   . VAL C 2 48  ? 169.461 210.122 263.702 1.00 74.66  ? 48  VAL D C   1 
ATOM 3588 O O   . VAL C 2 48  ? 170.130 209.246 264.265 1.00 75.75  ? 48  VAL D O   1 
ATOM 3589 C CB  . VAL C 2 48  ? 168.087 211.879 264.887 1.00 87.50  ? 48  VAL D CB  1 
ATOM 3590 C CG1 . VAL C 2 48  ? 167.532 210.691 265.651 1.00 89.70  ? 48  VAL D CG1 1 
ATOM 3591 C CG2 . VAL C 2 48  ? 168.213 213.092 265.801 1.00 90.36  ? 48  VAL D CG2 1 
ATOM 3592 N N   . SER C 2 49  ? 168.751 209.868 262.605 1.00 72.47  ? 49  SER D N   1 
ATOM 3593 C CA  . SER C 2 49  ? 168.623 208.515 262.073 1.00 72.59  ? 49  SER D CA  1 
ATOM 3594 C C   . SER C 2 49  ? 168.244 208.593 260.601 1.00 70.15  ? 49  SER D C   1 
ATOM 3595 O O   . SER C 2 49  ? 168.049 209.681 260.048 1.00 71.89  ? 49  SER D O   1 
ATOM 3596 C CB  . SER C 2 49  ? 167.587 207.701 262.855 1.00 73.38  ? 49  SER D CB  1 
ATOM 3597 O OG  . SER C 2 49  ? 166.265 208.049 262.472 1.00 72.69  ? 49  SER D OG  1 
ATOM 3598 N N   . CYS C 2 50  ? 168.152 207.418 259.973 1.00 62.78  ? 50  CYS D N   1 
ATOM 3599 C CA  . CYS C 2 50  ? 167.647 207.306 258.612 1.00 58.82  ? 50  CYS D CA  1 
ATOM 3600 C C   . CYS C 2 50  ? 167.101 205.905 258.394 1.00 53.46  ? 50  CYS D C   1 
ATOM 3601 O O   . CYS C 2 50  ? 167.503 204.949 259.061 1.00 59.20  ? 50  CYS D O   1 
ATOM 3602 C CB  . CYS C 2 50  ? 168.717 207.591 257.553 1.00 66.18  ? 50  CYS D CB  1 
ATOM 3603 S SG  . CYS C 2 50  ? 168.073 207.516 255.849 1.00 88.54  ? 50  CYS D SG  1 
ATOM 3604 N N   . ILE C 2 51  ? 166.177 205.806 257.447 1.00 48.72  ? 51  ILE D N   1 
ATOM 3605 C CA  . ILE C 2 51  ? 165.771 204.545 256.840 1.00 46.25  ? 51  ILE D CA  1 
ATOM 3606 C C   . ILE C 2 51  ? 165.857 204.719 255.330 1.00 51.89  ? 51  ILE D C   1 
ATOM 3607 O O   . ILE C 2 51  ? 165.572 205.801 254.802 1.00 62.87  ? 51  ILE D O   1 
ATOM 3608 C CB  . ILE C 2 51  ? 164.357 204.102 257.285 1.00 48.56  ? 51  ILE D CB  1 
ATOM 3609 C CG1 . ILE C 2 51  ? 163.296 205.118 256.857 1.00 61.90  ? 51  ILE D CG1 1 
ATOM 3610 C CG2 . ILE C 2 51  ? 164.308 203.855 258.789 1.00 51.98  ? 51  ILE D CG2 1 
ATOM 3611 C CD1 . ILE C 2 51  ? 161.891 204.644 257.051 1.00 72.31  ? 51  ILE D CD1 1 
ATOM 3612 N N   . SER C 2 52  ? 166.288 203.671 254.637 1.00 49.34  ? 52  SER D N   1 
ATOM 3613 C CA  . SER C 2 52  ? 166.583 203.752 253.214 1.00 47.52  ? 52  SER D CA  1 
ATOM 3614 C C   . SER C 2 52  ? 165.660 202.823 252.442 1.00 51.10  ? 52  SER D C   1 
ATOM 3615 O O   . SER C 2 52  ? 165.573 201.631 252.759 1.00 61.60  ? 52  SER D O   1 
ATOM 3616 C CB  . SER C 2 52  ? 168.046 203.394 252.938 1.00 57.25  ? 52  SER D CB  1 
ATOM 3617 O OG  . SER C 2 52  ? 168.916 204.133 253.777 1.00 63.60  ? 52  SER D OG  1 
ATOM 3618 N N   . SER C 2 53  ? 165.002 203.377 251.418 1.00 48.80  ? 53  SER D N   1 
ATOM 3619 C CA  . SER C 2 53  ? 164.075 202.674 250.535 1.00 53.69  ? 53  SER D CA  1 
ATOM 3620 C C   . SER C 2 53  ? 163.003 201.927 251.318 1.00 57.61  ? 53  SER D C   1 
ATOM 3621 O O   . SER C 2 53  ? 162.241 202.537 252.073 1.00 61.11  ? 53  SER D O   1 
ATOM 3622 C CB  . SER C 2 53  ? 164.836 201.713 249.617 1.00 54.18  ? 53  SER D CB  1 
ATOM 3623 O OG  . SER C 2 53  ? 163.946 201.002 248.776 1.00 57.52  ? 53  SER D OG  1 
ATOM 3624 N N   . GLY C 2 54  ? 162.949 200.609 251.155 1.00 53.67  ? 54  GLY D N   1 
ATOM 3625 C CA  . GLY C 2 54  ? 161.994 199.798 251.882 1.00 58.49  ? 54  GLY D CA  1 
ATOM 3626 C C   . GLY C 2 54  ? 162.648 198.697 252.689 1.00 63.42  ? 54  GLY D C   1 
ATOM 3627 O O   . GLY C 2 54  ? 161.994 198.051 253.513 1.00 64.60  ? 54  GLY D O   1 
ATOM 3628 N N   . ASP C 2 55  ? 163.942 198.467 252.452 1.00 64.75  ? 55  ASP D N   1 
ATOM 3629 C CA  . ASP C 2 55  ? 164.642 197.384 253.136 1.00 66.79  ? 55  ASP D CA  1 
ATOM 3630 C C   . ASP C 2 55  ? 164.886 197.716 254.604 1.00 68.82  ? 55  ASP D C   1 
ATOM 3631 O O   . ASP C 2 55  ? 164.640 196.886 255.487 1.00 74.96  ? 55  ASP D O   1 
ATOM 3632 C CB  . ASP C 2 55  ? 165.961 197.086 252.424 1.00 68.96  ? 55  ASP D CB  1 
ATOM 3633 C CG  . ASP C 2 55  ? 166.735 195.959 253.079 1.00 79.93  ? 55  ASP D CG  1 
ATOM 3634 O OD1 . ASP C 2 55  ? 166.148 194.877 253.290 1.00 83.39  ? 55  ASP D OD1 1 
ATOM 3635 O OD2 . ASP C 2 55  ? 167.931 196.154 253.381 1.00 87.00  ? 55  ASP D OD2 1 
ATOM 3636 N N   . GLY C 2 56  ? 165.366 198.924 254.886 1.00 62.32  ? 56  GLY D N   1 
ATOM 3637 C CA  . GLY C 2 56  ? 165.689 199.306 256.247 1.00 60.76  ? 56  GLY D CA  1 
ATOM 3638 C C   . GLY C 2 56  ? 167.165 199.156 256.554 1.00 63.77  ? 56  GLY D C   1 
ATOM 3639 O O   . GLY C 2 56  ? 167.657 198.043 256.765 1.00 69.76  ? 56  GLY D O   1 
ATOM 3640 N N   . THR C 2 57  ? 167.880 200.279 256.580 1.00 60.16  ? 57  THR D N   1 
ATOM 3641 C CA  . THR C 2 57  ? 169.332 200.301 256.715 1.00 64.04  ? 57  THR D CA  1 
ATOM 3642 C C   . THR C 2 57  ? 169.663 201.400 257.734 1.00 65.44  ? 57  THR D C   1 
ATOM 3643 O O   . THR C 2 57  ? 170.270 202.421 257.418 1.00 65.30  ? 57  THR D O   1 
ATOM 3644 C CB  . THR C 2 57  ? 170.001 200.479 255.350 1.00 67.52  ? 57  THR D CB  1 
ATOM 3645 O OG1 . THR C 2 57  ? 169.585 199.410 254.495 1.00 70.95  ? 57  THR D OG1 1 
ATOM 3646 C CG2 . THR C 2 57  ? 171.521 200.347 255.462 1.00 71.32  ? 57  THR D CG2 1 
ATOM 3647 N N   . THR C 2 58  ? 169.106 201.242 258.940 1.00 63.80  ? 58  THR D N   1 
ATOM 3648 C CA  . THR C 2 58  ? 169.191 202.229 260.019 1.00 65.20  ? 58  THR D CA  1 
ATOM 3649 C C   . THR C 2 58  ? 170.617 202.711 260.270 1.00 63.85  ? 58  THR D C   1 
ATOM 3650 O O   . THR C 2 58  ? 171.548 201.911 260.388 1.00 67.26  ? 58  THR D O   1 
ATOM 3651 C CB  . THR C 2 58  ? 168.623 201.625 261.304 1.00 69.46  ? 58  THR D CB  1 
ATOM 3652 O OG1 . THR C 2 58  ? 169.620 200.809 261.930 1.00 73.75  ? 58  THR D OG1 1 
ATOM 3653 C CG2 . THR C 2 58  ? 167.402 200.769 260.997 1.00 65.81  ? 58  THR D CG2 1 
ATOM 3654 N N   . TYR C 2 59  ? 170.773 204.033 260.354 1.00 59.81  ? 59  TYR D N   1 
ATOM 3655 C CA  . TYR C 2 59  ? 172.077 204.684 260.386 1.00 64.47  ? 59  TYR D CA  1 
ATOM 3656 C C   . TYR C 2 59  ? 172.091 205.705 261.513 1.00 73.64  ? 59  TYR D C   1 
ATOM 3657 O O   . TYR C 2 59  ? 171.270 206.627 261.523 1.00 77.62  ? 59  TYR D O   1 
ATOM 3658 C CB  . TYR C 2 59  ? 172.371 205.370 259.050 1.00 67.43  ? 59  TYR D CB  1 
ATOM 3659 C CG  . TYR C 2 59  ? 172.954 204.455 258.003 1.00 66.72  ? 59  TYR D CG  1 
ATOM 3660 C CD1 . TYR C 2 59  ? 173.931 203.528 258.330 1.00 68.08  ? 59  TYR D CD1 1 
ATOM 3661 C CD2 . TYR C 2 59  ? 172.521 204.516 256.685 1.00 66.55  ? 59  TYR D CD2 1 
ATOM 3662 C CE1 . TYR C 2 59  ? 174.463 202.687 257.373 1.00 71.33  ? 59  TYR D CE1 1 
ATOM 3663 C CE2 . TYR C 2 59  ? 173.044 203.679 255.723 1.00 67.52  ? 59  TYR D CE2 1 
ATOM 3664 C CZ  . TYR C 2 59  ? 174.018 202.769 256.070 1.00 73.20  ? 59  TYR D CZ  1 
ATOM 3665 O OH  . TYR C 2 59  ? 174.545 201.932 255.114 1.00 80.63  ? 59  TYR D OH  1 
ATOM 3666 N N   . TYR C 2 60  ? 173.025 205.552 262.450 1.00 80.24  ? 60  TYR D N   1 
ATOM 3667 C CA  . TYR C 2 60  ? 173.106 206.395 263.635 1.00 85.51  ? 60  TYR D CA  1 
ATOM 3668 C C   . TYR C 2 60  ? 174.459 207.096 263.687 1.00 93.98  ? 60  TYR D C   1 
ATOM 3669 O O   . TYR C 2 60  ? 175.405 206.717 262.991 1.00 98.70  ? 60  TYR D O   1 
ATOM 3670 C CB  . TYR C 2 60  ? 172.906 205.571 264.918 1.00 86.40  ? 60  TYR D CB  1 
ATOM 3671 C CG  . TYR C 2 60  ? 171.513 205.006 265.114 1.00 78.21  ? 60  TYR D CG  1 
ATOM 3672 C CD1 . TYR C 2 60  ? 170.436 205.472 264.375 1.00 71.74  ? 60  TYR D CD1 1 
ATOM 3673 C CD2 . TYR C 2 60  ? 171.286 203.977 266.019 1.00 82.64  ? 60  TYR D CD2 1 
ATOM 3674 C CE1 . TYR C 2 60  ? 169.174 204.949 264.541 1.00 72.87  ? 60  TYR D CE1 1 
ATOM 3675 C CE2 . TYR C 2 60  ? 170.022 203.446 266.192 1.00 80.44  ? 60  TYR D CE2 1 
ATOM 3676 C CZ  . TYR C 2 60  ? 168.972 203.939 265.449 1.00 73.38  ? 60  TYR D CZ  1 
ATOM 3677 O OH  . TYR C 2 60  ? 167.711 203.422 265.608 1.00 70.66  ? 60  TYR D OH  1 
ATOM 3678 N N   . GLU C 2 61  ? 174.542 208.128 264.522 1.00 93.93  ? 61  GLU D N   1 
ATOM 3679 C CA  . GLU C 2 61  ? 175.783 208.848 264.778 1.00 102.63 ? 61  GLU D CA  1 
ATOM 3680 C C   . GLU C 2 61  ? 176.288 208.561 266.186 1.00 109.11 ? 61  GLU D C   1 
ATOM 3681 O O   . GLU C 2 61  ? 175.554 208.078 267.050 1.00 109.91 ? 61  GLU D O   1 
ATOM 3682 C CB  . GLU C 2 61  ? 175.608 210.358 264.577 1.00 102.76 ? 61  GLU D CB  1 
ATOM 3683 C CG  . GLU C 2 61  ? 175.342 210.780 263.146 1.00 98.34  ? 61  GLU D CG  1 
ATOM 3684 C CD  . GLU C 2 61  ? 173.894 210.647 262.740 1.00 93.69  ? 61  GLU D CD  1 
ATOM 3685 O OE1 . GLU C 2 61  ? 173.054 210.280 263.586 1.00 92.09  ? 61  GLU D OE1 1 
ATOM 3686 O OE2 . GLU C 2 61  ? 173.601 210.906 261.561 1.00 91.62  ? 61  GLU D OE2 1 
ATOM 3687 N N   . ASP C 2 62  ? 177.566 208.890 266.402 1.00 113.26 ? 62  ASP D N   1 
ATOM 3688 C CA  . ASP C 2 62  ? 178.251 208.521 267.640 1.00 116.93 ? 62  ASP D CA  1 
ATOM 3689 C C   . ASP C 2 62  ? 177.654 209.212 268.864 1.00 116.96 ? 62  ASP D C   1 
ATOM 3690 O O   . ASP C 2 62  ? 177.562 208.607 269.939 1.00 120.53 ? 62  ASP D O   1 
ATOM 3691 C CB  . ASP C 2 62  ? 179.753 208.806 267.506 1.00 119.27 ? 62  ASP D CB  1 
ATOM 3692 C CG  . ASP C 2 62  ? 180.074 210.284 267.269 1.00 122.92 ? 62  ASP D CG  1 
ATOM 3693 O OD1 . ASP C 2 62  ? 179.152 211.119 267.149 1.00 121.74 ? 62  ASP D OD1 1 
ATOM 3694 O OD2 . ASP C 2 62  ? 181.277 210.612 267.201 1.00 125.34 ? 62  ASP D OD2 1 
ATOM 3695 N N   . SER C 2 63  ? 177.243 210.472 268.725 1.00 110.14 ? 63  SER D N   1 
ATOM 3696 C CA  . SER C 2 63  ? 176.667 211.190 269.854 1.00 111.47 ? 63  SER D CA  1 
ATOM 3697 C C   . SER C 2 63  ? 175.217 210.810 270.119 1.00 111.43 ? 63  SER D C   1 
ATOM 3698 O O   . SER C 2 63  ? 174.687 211.156 271.180 1.00 113.51 ? 63  SER D O   1 
ATOM 3699 C CB  . SER C 2 63  ? 176.765 212.700 269.626 1.00 116.48 ? 63  SER D CB  1 
ATOM 3700 O OG  . SER C 2 63  ? 176.346 213.047 268.318 1.00 115.94 ? 63  SER D OG  1 
ATOM 3701 N N   . VAL C 2 64  ? 174.566 210.114 269.190 1.00 110.39 ? 64  VAL D N   1 
ATOM 3702 C CA  . VAL C 2 64  ? 173.140 209.825 269.300 1.00 112.23 ? 64  VAL D CA  1 
ATOM 3703 C C   . VAL C 2 64  ? 172.826 208.337 269.338 1.00 108.54 ? 64  VAL D C   1 
ATOM 3704 O O   . VAL C 2 64  ? 171.673 207.976 269.620 1.00 106.31 ? 64  VAL D O   1 
ATOM 3705 C CB  . VAL C 2 64  ? 172.339 210.497 268.163 1.00 113.46 ? 64  VAL D CB  1 
ATOM 3706 C CG1 . VAL C 2 64  ? 172.589 212.000 268.136 1.00 109.34 ? 64  VAL D CG1 1 
ATOM 3707 C CG2 . VAL C 2 64  ? 172.680 209.863 266.830 1.00 107.59 ? 64  VAL D CG2 1 
ATOM 3708 N N   . GLU C 2 65  ? 173.789 207.461 269.064 1.00 107.30 ? 65  GLU D N   1 
ATOM 3709 C CA  . GLU C 2 65  ? 173.503 206.034 269.028 1.00 103.22 ? 65  GLU D CA  1 
ATOM 3710 C C   . GLU C 2 65  ? 173.389 205.463 270.437 1.00 103.52 ? 65  GLU D C   1 
ATOM 3711 O O   . GLU C 2 65  ? 173.817 206.069 271.424 1.00 106.11 ? 65  GLU D O   1 
ATOM 3712 C CB  . GLU C 2 65  ? 174.582 205.278 268.252 1.00 106.23 ? 65  GLU D CB  1 
ATOM 3713 C CG  . GLU C 2 65  ? 175.956 205.312 268.901 1.00 114.12 ? 65  GLU D CG  1 
ATOM 3714 C CD  . GLU C 2 65  ? 177.010 204.609 268.069 1.00 117.35 ? 65  GLU D CD  1 
ATOM 3715 O OE1 . GLU C 2 65  ? 176.671 204.115 266.972 1.00 118.22 ? 65  GLU D OE1 1 
ATOM 3716 O OE2 . GLU C 2 65  ? 178.177 204.551 268.510 1.00 118.96 ? 65  GLU D OE2 1 
ATOM 3717 N N   . GLY C 2 66  ? 172.796 204.274 270.518 1.00 100.03 ? 66  GLY D N   1 
ATOM 3718 C CA  . GLY C 2 66  ? 172.646 203.562 271.766 1.00 101.01 ? 66  GLY D CA  1 
ATOM 3719 C C   . GLY C 2 66  ? 171.381 203.868 272.535 1.00 105.63 ? 66  GLY D C   1 
ATOM 3720 O O   . GLY C 2 66  ? 171.079 203.159 273.504 1.00 108.83 ? 66  GLY D O   1 
ATOM 3721 N N   . ARG C 2 67  ? 170.628 204.897 272.140 1.00 104.65 ? 67  ARG D N   1 
ATOM 3722 C CA  . ARG C 2 67  ? 169.386 205.245 272.814 1.00 102.37 ? 67  ARG D CA  1 
ATOM 3723 C C   . ARG C 2 67  ? 168.191 205.374 271.882 1.00 97.92  ? 67  ARG D C   1 
ATOM 3724 O O   . ARG C 2 67  ? 167.061 205.468 272.374 1.00 99.77  ? 67  ARG D O   1 
ATOM 3725 C CB  . ARG C 2 67  ? 169.541 206.560 273.596 1.00 106.04 ? 67  ARG D CB  1 
ATOM 3726 C CG  . ARG C 2 67  ? 170.674 206.563 274.612 1.00 110.09 ? 67  ARG D CG  1 
ATOM 3727 C CD  . ARG C 2 67  ? 170.911 207.965 275.195 1.00 113.74 ? 67  ARG D CD  1 
ATOM 3728 N NE  . ARG C 2 67  ? 171.476 208.981 274.302 1.00 112.66 ? 67  ARG D NE  1 
ATOM 3729 C CZ  . ARG C 2 67  ? 172.551 208.870 273.525 1.00 110.68 ? 67  ARG D CZ  1 
ATOM 3730 N NH1 . ARG C 2 67  ? 173.369 207.831 273.594 1.00 107.50 ? 67  ARG D NH1 1 
ATOM 3731 N NH2 . ARG C 2 67  ? 172.846 209.862 272.690 1.00 110.74 ? 67  ARG D NH2 1 
ATOM 3732 N N   . PHE C 2 68  ? 168.392 205.378 270.569 1.00 97.33  ? 68  PHE D N   1 
ATOM 3733 C CA  . PHE C 2 68  ? 167.318 205.580 269.609 1.00 96.52  ? 68  PHE D CA  1 
ATOM 3734 C C   . PHE C 2 68  ? 167.027 204.284 268.864 1.00 90.49  ? 68  PHE D C   1 
ATOM 3735 O O   . PHE C 2 68  ? 167.926 203.478 268.609 1.00 91.09  ? 68  PHE D O   1 
ATOM 3736 C CB  . PHE C 2 68  ? 167.666 206.686 268.603 1.00 101.11 ? 68  PHE D CB  1 
ATOM 3737 C CG  . PHE C 2 68  ? 167.925 208.040 269.224 1.00 104.28 ? 68  PHE D CG  1 
ATOM 3738 C CD1 . PHE C 2 68  ? 167.443 208.366 270.485 1.00 110.06 ? 68  PHE D CD1 1 
ATOM 3739 C CD2 . PHE C 2 68  ? 168.665 208.987 268.539 1.00 105.05 ? 68  PHE D CD2 1 
ATOM 3740 C CE1 . PHE C 2 68  ? 167.692 209.607 271.040 1.00 117.58 ? 68  PHE D CE1 1 
ATOM 3741 C CE2 . PHE C 2 68  ? 168.909 210.232 269.088 1.00 112.60 ? 68  PHE D CE2 1 
ATOM 3742 C CZ  . PHE C 2 68  ? 168.425 210.540 270.340 1.00 117.63 ? 68  PHE D CZ  1 
ATOM 3743 N N   . THR C 2 69  ? 165.754 204.089 268.522 1.00 91.94  ? 69  THR D N   1 
ATOM 3744 C CA  . THR C 2 69  ? 165.309 202.913 267.772 1.00 90.91  ? 69  THR D CA  1 
ATOM 3745 C C   . THR C 2 69  ? 164.341 203.390 266.694 1.00 86.29  ? 69  THR D C   1 
ATOM 3746 O O   . THR C 2 69  ? 163.145 203.548 266.953 1.00 90.48  ? 69  THR D O   1 
ATOM 3747 C CB  . THR C 2 69  ? 164.657 201.877 268.681 1.00 95.34  ? 69  THR D CB  1 
ATOM 3748 O OG1 . THR C 2 69  ? 163.795 202.533 269.619 1.00 104.90 ? 69  THR D OG1 1 
ATOM 3749 C CG2 . THR C 2 69  ? 165.711 201.073 269.434 1.00 89.21  ? 69  THR D CG2 1 
ATOM 3750 N N   . ILE C 2 70  ? 164.861 203.616 265.491 1.00 74.11  ? 70  ILE D N   1 
ATOM 3751 C CA  . ILE C 2 70  ? 164.030 204.032 264.368 1.00 71.47  ? 70  ILE D CA  1 
ATOM 3752 C C   . ILE C 2 70  ? 163.267 202.827 263.831 1.00 70.19  ? 70  ILE D C   1 
ATOM 3753 O O   . ILE C 2 70  ? 163.766 201.694 263.836 1.00 74.46  ? 70  ILE D O   1 
ATOM 3754 C CB  . ILE C 2 70  ? 164.890 204.721 263.286 1.00 71.80  ? 70  ILE D CB  1 
ATOM 3755 C CG1 . ILE C 2 70  ? 164.012 205.424 262.248 1.00 73.30  ? 70  ILE D CG1 1 
ATOM 3756 C CG2 . ILE C 2 70  ? 165.871 203.757 262.636 1.00 67.04  ? 70  ILE D CG2 1 
ATOM 3757 C CD1 . ILE C 2 70  ? 163.225 206.579 262.802 1.00 76.78  ? 70  ILE D CD1 1 
ATOM 3758 N N   . SER C 2 71  ? 162.025 203.062 263.414 1.00 68.18  ? 71  SER D N   1 
ATOM 3759 C CA  . SER C 2 71  ? 161.169 202.004 262.898 1.00 69.31  ? 71  SER D CA  1 
ATOM 3760 C C   . SER C 2 71  ? 160.142 202.631 261.971 1.00 68.88  ? 71  SER D C   1 
ATOM 3761 O O   . SER C 2 71  ? 159.931 203.845 261.981 1.00 76.66  ? 71  SER D O   1 
ATOM 3762 C CB  . SER C 2 71  ? 160.483 201.229 264.029 1.00 77.18  ? 71  SER D CB  1 
ATOM 3763 O OG  . SER C 2 71  ? 159.313 201.896 264.468 1.00 86.19  ? 71  SER D OG  1 
ATOM 3764 N N   . ARG C 2 72  ? 159.497 201.785 261.173 1.00 68.73  ? 72  ARG D N   1 
ATOM 3765 C CA  . ARG C 2 72  ? 158.569 202.268 260.164 1.00 70.21  ? 72  ARG D CA  1 
ATOM 3766 C C   . ARG C 2 72  ? 157.552 201.179 259.864 1.00 73.17  ? 72  ARG D C   1 
ATOM 3767 O O   . ARG C 2 72  ? 157.874 199.988 259.862 1.00 76.83  ? 72  ARG D O   1 
ATOM 3768 C CB  . ARG C 2 72  ? 159.339 202.712 258.908 1.00 74.43  ? 72  ARG D CB  1 
ATOM 3769 C CG  . ARG C 2 72  ? 158.548 203.380 257.771 1.00 77.80  ? 72  ARG D CG  1 
ATOM 3770 C CD  . ARG C 2 72  ? 157.961 202.392 256.765 1.00 79.16  ? 72  ARG D CD  1 
ATOM 3771 N NE  . ARG C 2 72  ? 158.998 201.530 256.207 1.00 80.44  ? 72  ARG D NE  1 
ATOM 3772 C CZ  . ARG C 2 72  ? 159.811 201.872 255.217 1.00 80.06  ? 72  ARG D CZ  1 
ATOM 3773 N NH1 . ARG C 2 72  ? 159.758 203.070 254.660 1.00 77.72  ? 72  ARG D NH1 1 
ATOM 3774 N NH2 . ARG C 2 72  ? 160.709 200.992 254.784 1.00 75.73  ? 72  ARG D NH2 1 
ATOM 3775 N N   . ASP C 2 73  ? 156.319 201.607 259.610 1.00 73.54  ? 73  ASP D N   1 
ATOM 3776 C CA  . ASP C 2 73  ? 155.232 200.722 259.221 1.00 82.84  ? 73  ASP D CA  1 
ATOM 3777 C C   . ASP C 2 73  ? 154.734 201.141 257.847 1.00 84.53  ? 73  ASP D C   1 
ATOM 3778 O O   . ASP C 2 73  ? 154.431 202.318 257.625 1.00 85.34  ? 73  ASP D O   1 
ATOM 3779 C CB  . ASP C 2 73  ? 154.092 200.768 260.243 1.00 87.71  ? 73  ASP D CB  1 
ATOM 3780 C CG  . ASP C 2 73  ? 152.982 199.777 259.932 1.00 92.28  ? 73  ASP D CG  1 
ATOM 3781 O OD1 . ASP C 2 73  ? 153.226 198.814 259.175 1.00 93.53  ? 73  ASP D OD1 1 
ATOM 3782 O OD2 . ASP C 2 73  ? 151.860 199.965 260.447 1.00 91.13  ? 73  ASP D OD2 1 
ATOM 3783 N N   . ASN C 2 74  ? 154.648 200.180 256.931 1.00 84.45  ? 74  ASN D N   1 
ATOM 3784 C CA  . ASN C 2 74  ? 154.142 200.444 255.591 1.00 85.20  ? 74  ASN D CA  1 
ATOM 3785 C C   . ASN C 2 74  ? 152.621 200.454 255.524 1.00 83.73  ? 74  ASN D C   1 
ATOM 3786 O O   . ASN C 2 74  ? 152.066 200.744 254.458 1.00 86.21  ? 74  ASN D O   1 
ATOM 3787 C CB  . ASN C 2 74  ? 154.705 199.417 254.603 1.00 87.38  ? 74  ASN D CB  1 
ATOM 3788 C CG  . ASN C 2 74  ? 154.660 197.996 255.139 1.00 91.15  ? 74  ASN D CG  1 
ATOM 3789 O OD1 . ASN C 2 74  ? 153.731 197.612 255.850 1.00 93.62  ? 74  ASN D OD1 1 
ATOM 3790 N ND2 . ASN C 2 74  ? 155.672 197.207 254.798 1.00 91.99  ? 74  ASN D ND2 1 
ATOM 3791 N N   . ALA C 2 75  ? 151.938 200.148 256.627 1.00 81.03  ? 75  ALA D N   1 
ATOM 3792 C CA  . ALA C 2 75  ? 150.479 200.160 256.635 1.00 82.85  ? 75  ALA D CA  1 
ATOM 3793 C C   . ALA C 2 75  ? 149.937 201.571 256.833 1.00 83.72  ? 75  ALA D C   1 
ATOM 3794 O O   . ALA C 2 75  ? 149.196 202.088 255.991 1.00 83.27  ? 75  ALA D O   1 
ATOM 3795 C CB  . ALA C 2 75  ? 149.954 199.222 257.725 1.00 83.39  ? 75  ALA D CB  1 
ATOM 3796 N N   . LYS C 2 76  ? 150.299 202.210 257.943 1.00 85.13  ? 76  LYS D N   1 
ATOM 3797 C CA  . LYS C 2 76  ? 149.794 203.534 258.278 1.00 85.17  ? 76  LYS D CA  1 
ATOM 3798 C C   . LYS C 2 76  ? 150.613 204.663 257.666 1.00 83.36  ? 76  LYS D C   1 
ATOM 3799 O O   . LYS C 2 76  ? 150.243 205.830 257.841 1.00 84.08  ? 76  LYS D O   1 
ATOM 3800 C CB  . LYS C 2 76  ? 149.737 203.710 259.798 1.00 88.23  ? 76  LYS D CB  1 
ATOM 3801 C CG  . LYS C 2 76  ? 149.561 202.414 260.569 1.00 94.29  ? 76  LYS D CG  1 
ATOM 3802 C CD  . LYS C 2 76  ? 149.649 202.647 262.067 1.00 100.32 ? 76  LYS D CD  1 
ATOM 3803 C CE  . LYS C 2 76  ? 149.251 201.403 262.842 1.00 103.18 ? 76  LYS D CE  1 
ATOM 3804 N NZ  . LYS C 2 76  ? 149.488 201.561 264.303 1.00 101.34 ? 76  LYS D NZ  1 
ATOM 3805 N N   . ASN C 2 77  ? 151.707 204.337 256.965 1.00 84.62  ? 77  ASN D N   1 
ATOM 3806 C CA  . ASN C 2 77  ? 152.579 205.311 256.293 1.00 86.47  ? 77  ASN D CA  1 
ATOM 3807 C C   . ASN C 2 77  ? 153.132 206.349 257.269 1.00 83.61  ? 77  ASN D C   1 
ATOM 3808 O O   . ASN C 2 77  ? 153.265 207.530 256.941 1.00 86.55  ? 77  ASN D O   1 
ATOM 3809 C CB  . ASN C 2 77  ? 151.861 205.989 255.122 1.00 88.08  ? 77  ASN D CB  1 
ATOM 3810 C CG  . ASN C 2 77  ? 152.815 206.447 254.038 1.00 82.18  ? 77  ASN D CG  1 
ATOM 3811 O OD1 . ASN C 2 77  ? 153.807 205.780 253.745 1.00 79.06  ? 77  ASN D OD1 1 
ATOM 3812 N ND2 . ASN C 2 77  ? 152.518 207.592 253.436 1.00 79.22  ? 77  ASN D ND2 1 
ATOM 3813 N N   . THR C 2 78  ? 153.453 205.905 258.482 1.00 81.16  ? 78  THR D N   1 
ATOM 3814 C CA  . THR C 2 78  ? 153.992 206.775 259.518 1.00 83.20  ? 78  THR D CA  1 
ATOM 3815 C C   . THR C 2 78  ? 155.277 206.172 260.061 1.00 76.66  ? 78  THR D C   1 
ATOM 3816 O O   . THR C 2 78  ? 155.288 205.018 260.501 1.00 81.54  ? 78  THR D O   1 
ATOM 3817 C CB  . THR C 2 78  ? 152.981 206.977 260.653 1.00 90.20  ? 78  THR D CB  1 
ATOM 3818 O OG1 . THR C 2 78  ? 151.775 207.542 260.126 1.00 95.07  ? 78  THR D OG1 1 
ATOM 3819 C CG2 . THR C 2 78  ? 153.551 207.903 261.713 1.00 90.44  ? 78  THR D CG2 1 
ATOM 3820 N N   . VAL C 2 79  ? 156.354 206.951 260.030 1.00 72.87  ? 79  VAL D N   1 
ATOM 3821 C CA  . VAL C 2 79  ? 157.629 206.516 260.587 1.00 77.33  ? 79  VAL D CA  1 
ATOM 3822 C C   . VAL C 2 79  ? 157.628 206.786 262.088 1.00 83.67  ? 79  VAL D C   1 
ATOM 3823 O O   . VAL C 2 79  ? 157.054 207.776 262.562 1.00 86.97  ? 79  VAL D O   1 
ATOM 3824 C CB  . VAL C 2 79  ? 158.799 207.207 259.854 1.00 74.75  ? 79  VAL D CB  1 
ATOM 3825 C CG1 . VAL C 2 79  ? 158.795 208.708 260.072 1.00 79.81  ? 79  VAL D CG1 1 
ATOM 3826 C CG2 . VAL C 2 79  ? 160.138 206.609 260.251 1.00 72.77  ? 79  VAL D CG2 1 
ATOM 3827 N N   . TYR C 2 80  ? 158.222 205.873 262.854 1.00 86.76  ? 80  TYR D N   1 
ATOM 3828 C CA  . TYR C 2 80  ? 158.218 205.935 264.309 1.00 85.69  ? 80  TYR D CA  1 
ATOM 3829 C C   . TYR C 2 80  ? 159.640 206.055 264.836 1.00 85.82  ? 80  TYR D C   1 
ATOM 3830 O O   . TYR C 2 80  ? 160.545 205.351 264.378 1.00 88.72  ? 80  TYR D O   1 
ATOM 3831 C CB  . TYR C 2 80  ? 157.555 204.693 264.915 1.00 86.34  ? 80  TYR D CB  1 
ATOM 3832 C CG  . TYR C 2 80  ? 156.076 204.569 264.633 1.00 92.77  ? 80  TYR D CG  1 
ATOM 3833 C CD1 . TYR C 2 80  ? 155.234 205.665 264.751 1.00 95.24  ? 80  TYR D CD1 1 
ATOM 3834 C CD2 . TYR C 2 80  ? 155.519 203.352 264.258 1.00 92.56  ? 80  TYR D CD2 1 
ATOM 3835 C CE1 . TYR C 2 80  ? 153.879 205.557 264.498 1.00 95.94  ? 80  TYR D CE1 1 
ATOM 3836 C CE2 . TYR C 2 80  ? 154.164 203.234 264.002 1.00 97.02  ? 80  TYR D CE2 1 
ATOM 3837 C CZ  . TYR C 2 80  ? 153.350 204.340 264.124 1.00 99.75  ? 80  TYR D CZ  1 
ATOM 3838 O OH  . TYR C 2 80  ? 152.002 204.228 263.871 1.00 101.52 ? 80  TYR D OH  1 
ATOM 3839 N N   . LEU C 2 81  ? 159.832 206.945 265.806 1.00 85.45  ? 81  LEU D N   1 
ATOM 3840 C CA  . LEU C 2 81  ? 161.111 207.119 266.492 1.00 86.71  ? 81  LEU D CA  1 
ATOM 3841 C C   . LEU C 2 81  ? 160.876 206.840 267.974 1.00 96.37  ? 81  LEU D C   1 
ATOM 3842 O O   . LEU C 2 81  ? 160.490 207.730 268.735 1.00 104.15 ? 81  LEU D O   1 
ATOM 3843 C CB  . LEU C 2 81  ? 161.683 208.512 266.262 1.00 87.35  ? 81  LEU D CB  1 
ATOM 3844 C CG  . LEU C 2 81  ? 163.054 208.781 266.885 1.00 89.49  ? 81  LEU D CG  1 
ATOM 3845 C CD1 . LEU C 2 81  ? 164.108 207.865 266.285 1.00 84.06  ? 81  LEU D CD1 1 
ATOM 3846 C CD2 . LEU C 2 81  ? 163.446 210.241 266.712 1.00 97.30  ? 81  LEU D CD2 1 
ATOM 3847 N N   . GLN C 2 82  ? 161.101 205.592 268.376 1.00 95.89  ? 82  GLN D N   1 
ATOM 3848 C CA  . GLN C 2 82  ? 160.900 205.201 269.765 1.00 99.86  ? 82  GLN D CA  1 
ATOM 3849 C C   . GLN C 2 82  ? 162.074 205.669 270.617 1.00 101.85 ? 82  GLN D C   1 
ATOM 3850 O O   . GLN C 2 82  ? 163.237 205.504 270.236 1.00 99.67  ? 82  GLN D O   1 
ATOM 3851 C CB  . GLN C 2 82  ? 160.727 203.684 269.859 1.00 102.81 ? 82  GLN D CB  1 
ATOM 3852 C CG  . GLN C 2 82  ? 160.771 203.117 271.268 1.00 111.98 ? 82  GLN D CG  1 
ATOM 3853 C CD  . GLN C 2 82  ? 159.509 203.412 272.055 1.00 116.63 ? 82  GLN D CD  1 
ATOM 3854 O OE1 . GLN C 2 82  ? 158.421 202.960 271.698 1.00 119.06 ? 82  GLN D OE1 1 
ATOM 3855 N NE2 . GLN C 2 82  ? 159.650 204.171 273.136 1.00 118.03 ? 82  GLN D NE2 1 
ATOM 3856 N N   . MET C 2 83  ? 161.767 206.258 271.770 1.00 107.24 ? 83  MET D N   1 
ATOM 3857 C CA  . MET C 2 83  ? 162.766 206.797 272.685 1.00 112.09 ? 83  MET D CA  1 
ATOM 3858 C C   . MET C 2 83  ? 162.947 205.839 273.855 1.00 114.06 ? 83  MET D C   1 
ATOM 3859 O O   . MET C 2 83  ? 161.991 205.565 274.587 1.00 116.37 ? 83  MET D O   1 
ATOM 3860 C CB  . MET C 2 83  ? 162.346 208.177 273.189 1.00 118.03 ? 83  MET D CB  1 
ATOM 3861 C CG  . MET C 2 83  ? 163.383 208.868 274.053 1.00 126.98 ? 83  MET D CG  1 
ATOM 3862 S SD  . MET C 2 83  ? 164.899 209.229 273.154 1.00 136.50 ? 83  MET D SD  1 
ATOM 3863 C CE  . MET C 2 83  ? 164.348 210.570 272.100 1.00 119.24 ? 83  MET D CE  1 
ATOM 3864 N N   . ASN C 2 84  ? 164.167 205.335 274.028 1.00 112.79 ? 84  ASN D N   1 
ATOM 3865 C CA  . ASN C 2 84  ? 164.518 204.472 275.150 1.00 118.12 ? 84  ASN D CA  1 
ATOM 3866 C C   . ASN C 2 84  ? 165.709 205.062 275.889 1.00 119.25 ? 84  ASN D C   1 
ATOM 3867 O O   . ASN C 2 84  ? 166.747 205.330 275.274 1.00 118.60 ? 84  ASN D O   1 
ATOM 3868 C CB  . ASN C 2 84  ? 164.854 203.044 274.692 1.00 123.48 ? 84  ASN D CB  1 
ATOM 3869 C CG  . ASN C 2 84  ? 163.709 202.367 273.959 1.00 121.69 ? 84  ASN D CG  1 
ATOM 3870 O OD1 . ASN C 2 84  ? 162.564 202.808 274.021 1.00 119.67 ? 84  ASN D OD1 1 
ATOM 3871 N ND2 . ASN C 2 84  ? 164.020 201.283 273.258 1.00 119.15 ? 84  ASN D ND2 1 
ATOM 3872 N N   . SER C 2 85  ? 165.563 205.213 277.209 1.00 123.86 ? 85  SER D N   1 
ATOM 3873 C CA  . SER C 2 85  ? 166.599 205.685 278.143 1.00 127.83 ? 85  SER D CA  1 
ATOM 3874 C C   . SER C 2 85  ? 167.274 206.970 277.655 1.00 126.38 ? 85  SER D C   1 
ATOM 3875 O O   . SER C 2 85  ? 168.476 207.016 277.388 1.00 123.38 ? 85  SER D O   1 
ATOM 3876 C CB  . SER C 2 85  ? 167.642 204.595 278.433 1.00 127.47 ? 85  SER D CB  1 
ATOM 3877 O OG  . SER C 2 85  ? 168.065 203.893 277.277 1.00 127.29 ? 85  SER D OG  1 
ATOM 3878 N N   . LEU C 2 86  ? 166.472 208.023 277.544 1.00 127.23 ? 86  LEU D N   1 
ATOM 3879 C CA  . LEU C 2 86  ? 166.977 209.310 277.093 1.00 128.44 ? 86  LEU D CA  1 
ATOM 3880 C C   . LEU C 2 86  ? 167.717 210.026 278.217 1.00 127.27 ? 86  LEU D C   1 
ATOM 3881 O O   . LEU C 2 86  ? 167.464 209.798 279.404 1.00 128.09 ? 86  LEU D O   1 
ATOM 3882 C CB  . LEU C 2 86  ? 165.843 210.200 276.575 1.00 132.09 ? 86  LEU D CB  1 
ATOM 3883 C CG  . LEU C 2 86  ? 164.840 210.861 277.529 1.00 132.92 ? 86  LEU D CG  1 
ATOM 3884 C CD1 . LEU C 2 86  ? 164.106 211.963 276.786 1.00 132.72 ? 86  LEU D CD1 1 
ATOM 3885 C CD2 . LEU C 2 86  ? 163.834 209.879 278.115 1.00 133.68 ? 86  LEU D CD2 1 
ATOM 3886 N N   . LYS C 2 87  ? 168.640 210.900 277.829 1.00 123.47 ? 87  LYS D N   1 
ATOM 3887 C CA  . LYS C 2 87  ? 169.444 211.679 278.759 1.00 121.99 ? 87  LYS D CA  1 
ATOM 3888 C C   . LYS C 2 87  ? 168.944 213.121 278.800 1.00 122.76 ? 87  LYS D C   1 
ATOM 3889 O O   . LYS C 2 87  ? 168.004 213.503 278.097 1.00 121.92 ? 87  LYS D O   1 
ATOM 3890 C CB  . LYS C 2 87  ? 170.924 211.613 278.377 1.00 121.62 ? 87  LYS D CB  1 
ATOM 3891 C CG  . LYS C 2 87  ? 171.452 210.203 278.148 1.00 122.82 ? 87  LYS D CG  1 
ATOM 3892 C CD  . LYS C 2 87  ? 171.196 209.311 279.355 1.00 121.40 ? 87  LYS D CD  1 
ATOM 3893 C CE  . LYS C 2 87  ? 171.680 207.891 279.112 1.00 113.55 ? 87  LYS D CE  1 
ATOM 3894 N NZ  . LYS C 2 87  ? 171.333 206.986 280.243 1.00 111.86 ? 87  LYS D NZ  1 
ATOM 3895 N N   . LEU C 2 88  ? 169.592 213.929 279.643 1.00 125.92 ? 88  LEU D N   1 
ATOM 3896 C CA  . LEU C 2 88  ? 169.123 215.283 279.913 1.00 127.49 ? 88  LEU D CA  1 
ATOM 3897 C C   . LEU C 2 88  ? 169.537 216.292 278.848 1.00 124.82 ? 88  LEU D C   1 
ATOM 3898 O O   . LEU C 2 88  ? 168.982 217.396 278.815 1.00 121.40 ? 88  LEU D O   1 
ATOM 3899 C CB  . LEU C 2 88  ? 169.607 215.726 281.303 1.00 129.12 ? 88  LEU D CB  1 
ATOM 3900 C CG  . LEU C 2 88  ? 171.095 215.834 281.682 1.00 131.16 ? 88  LEU D CG  1 
ATOM 3901 C CD1 . LEU C 2 88  ? 171.758 217.155 281.277 1.00 130.20 ? 88  LEU D CD1 1 
ATOM 3902 C CD2 . LEU C 2 88  ? 171.272 215.586 283.176 1.00 131.24 ? 88  LEU D CD2 1 
ATOM 3903 N N   . GLU C 2 89  ? 170.489 215.952 277.984 1.00 125.51 ? 89  GLU D N   1 
ATOM 3904 C CA  . GLU C 2 89  ? 170.938 216.862 276.939 1.00 124.07 ? 89  GLU D CA  1 
ATOM 3905 C C   . GLU C 2 89  ? 170.149 216.714 275.644 1.00 122.20 ? 89  GLU D C   1 
ATOM 3906 O O   . GLU C 2 89  ? 170.469 217.387 274.658 1.00 123.19 ? 89  GLU D O   1 
ATOM 3907 C CB  . GLU C 2 89  ? 172.437 216.663 276.668 1.00 130.15 ? 89  GLU D CB  1 
ATOM 3908 C CG  . GLU C 2 89  ? 172.789 215.452 275.811 1.00 133.06 ? 89  GLU D CG  1 
ATOM 3909 C CD  . GLU C 2 89  ? 172.785 214.157 276.596 1.00 130.40 ? 89  GLU D CD  1 
ATOM 3910 O OE1 . GLU C 2 89  ? 172.861 214.218 277.841 1.00 131.91 ? 89  GLU D OE1 1 
ATOM 3911 O OE2 . GLU C 2 89  ? 172.710 213.080 275.968 1.00 125.89 ? 89  GLU D OE2 1 
ATOM 3912 N N   . ASP C 2 90  ? 169.116 215.876 275.629 1.00 121.59 ? 90  ASP D N   1 
ATOM 3913 C CA  . ASP C 2 90  ? 168.357 215.580 274.424 1.00 123.97 ? 90  ASP D CA  1 
ATOM 3914 C C   . ASP C 2 90  ? 167.216 216.561 274.173 1.00 126.29 ? 90  ASP D C   1 
ATOM 3915 O O   . ASP C 2 90  ? 166.431 216.348 273.244 1.00 127.43 ? 90  ASP D O   1 
ATOM 3916 C CB  . ASP C 2 90  ? 167.805 214.153 274.490 1.00 125.67 ? 90  ASP D CB  1 
ATOM 3917 C CG  . ASP C 2 90  ? 168.871 213.103 274.239 1.00 127.82 ? 90  ASP D CG  1 
ATOM 3918 O OD1 . ASP C 2 90  ? 169.586 213.212 273.221 1.00 128.12 ? 90  ASP D OD1 1 
ATOM 3919 O OD2 . ASP C 2 90  ? 168.994 212.170 275.061 1.00 126.95 ? 90  ASP D OD2 1 
ATOM 3920 N N   . THR C 2 91  ? 167.099 217.619 274.976 1.00 127.49 ? 91  THR D N   1 
ATOM 3921 C CA  . THR C 2 91  ? 166.038 218.599 274.775 1.00 122.85 ? 91  THR D CA  1 
ATOM 3922 C C   . THR C 2 91  ? 166.348 219.444 273.544 1.00 119.70 ? 91  THR D C   1 
ATOM 3923 O O   . THR C 2 91  ? 167.348 220.172 273.515 1.00 119.97 ? 91  THR D O   1 
ATOM 3924 C CB  . THR C 2 91  ? 165.881 219.483 276.013 1.00 119.07 ? 91  THR D CB  1 
ATOM 3925 O OG1 . THR C 2 91  ? 165.229 218.742 277.050 1.00 117.41 ? 91  THR D OG1 1 
ATOM 3926 C CG2 . THR C 2 91  ? 165.035 220.712 275.698 1.00 117.86 ? 91  THR D CG2 1 
ATOM 3927 N N   . ALA C 2 92  ? 165.493 219.336 272.531 1.00 116.53 ? 92  ALA D N   1 
ATOM 3928 C CA  . ALA C 2 92  ? 165.637 220.043 271.261 1.00 115.87 ? 92  ALA D CA  1 
ATOM 3929 C C   . ALA C 2 92  ? 164.322 219.903 270.505 1.00 114.11 ? 92  ALA D C   1 
ATOM 3930 O O   . ALA C 2 92  ? 163.410 219.190 270.935 1.00 113.23 ? 92  ALA D O   1 
ATOM 3931 C CB  . ALA C 2 92  ? 166.804 219.500 270.431 1.00 118.90 ? 92  ALA D CB  1 
ATOM 3932 N N   . VAL C 2 93  ? 164.236 220.575 269.364 1.00 115.10 ? 93  VAL D N   1 
ATOM 3933 C CA  . VAL C 2 93  ? 163.099 220.439 268.460 1.00 113.46 ? 93  VAL D CA  1 
ATOM 3934 C C   . VAL C 2 93  ? 163.505 219.521 267.313 1.00 111.33 ? 93  VAL D C   1 
ATOM 3935 O O   . VAL C 2 93  ? 164.617 219.620 266.777 1.00 113.03 ? 93  VAL D O   1 
ATOM 3936 C CB  . VAL C 2 93  ? 162.598 221.818 267.971 1.00 109.75 ? 93  VAL D CB  1 
ATOM 3937 C CG1 . VAL C 2 93  ? 163.681 222.598 267.224 1.00 109.02 ? 93  VAL D CG1 1 
ATOM 3938 C CG2 . VAL C 2 93  ? 161.346 221.667 267.113 1.00 105.42 ? 93  VAL D CG2 1 
ATOM 3939 N N   . TYR C 2 94  ? 162.626 218.580 266.976 1.00 107.31 ? 94  TYR D N   1 
ATOM 3940 C CA  . TYR C 2 94  ? 162.930 217.528 266.018 1.00 101.86 ? 94  TYR D CA  1 
ATOM 3941 C C   . TYR C 2 94  ? 162.202 217.767 264.702 1.00 92.97  ? 94  TYR D C   1 
ATOM 3942 O O   . TYR C 2 94  ? 161.036 218.173 264.687 1.00 94.85  ? 94  TYR D O   1 
ATOM 3943 C CB  . TYR C 2 94  ? 162.558 216.151 266.577 1.00 105.20 ? 94  TYR D CB  1 
ATOM 3944 C CG  . TYR C 2 94  ? 163.532 215.624 267.608 1.00 109.97 ? 94  TYR D CG  1 
ATOM 3945 C CD1 . TYR C 2 94  ? 163.480 216.054 268.929 1.00 110.45 ? 94  TYR D CD1 1 
ATOM 3946 C CD2 . TYR C 2 94  ? 164.505 214.696 267.258 1.00 109.96 ? 94  TYR D CD2 1 
ATOM 3947 C CE1 . TYR C 2 94  ? 164.371 215.573 269.873 1.00 109.81 ? 94  TYR D CE1 1 
ATOM 3948 C CE2 . TYR C 2 94  ? 165.400 214.210 268.195 1.00 114.39 ? 94  TYR D CE2 1 
ATOM 3949 C CZ  . TYR C 2 94  ? 165.328 214.652 269.500 1.00 113.96 ? 94  TYR D CZ  1 
ATOM 3950 O OH  . TYR C 2 94  ? 166.216 214.170 270.433 1.00 117.52 ? 94  TYR D OH  1 
ATOM 3951 N N   . TYR C 2 95  ? 162.904 217.508 263.602 1.00 87.14  ? 95  TYR D N   1 
ATOM 3952 C CA  . TYR C 2 95  ? 162.370 217.639 262.257 1.00 84.41  ? 95  TYR D CA  1 
ATOM 3953 C C   . TYR C 2 95  ? 162.589 216.322 261.526 1.00 81.94  ? 95  TYR D C   1 
ATOM 3954 O O   . TYR C 2 95  ? 163.525 215.580 261.836 1.00 89.49  ? 95  TYR D O   1 
ATOM 3955 C CB  . TYR C 2 95  ? 163.063 218.772 261.477 1.00 91.24  ? 95  TYR D CB  1 
ATOM 3956 C CG  . TYR C 2 95  ? 163.065 220.123 262.166 1.00 97.40  ? 95  TYR D CG  1 
ATOM 3957 C CD1 . TYR C 2 95  ? 164.062 220.455 263.080 1.00 101.72 ? 95  TYR D CD1 1 
ATOM 3958 C CD2 . TYR C 2 95  ? 162.084 221.068 261.898 1.00 96.15  ? 95  TYR D CD2 1 
ATOM 3959 C CE1 . TYR C 2 95  ? 164.076 221.685 263.711 1.00 103.72 ? 95  TYR D CE1 1 
ATOM 3960 C CE2 . TYR C 2 95  ? 162.093 222.303 262.525 1.00 101.36 ? 95  TYR D CE2 1 
ATOM 3961 C CZ  . TYR C 2 95  ? 163.088 222.605 263.430 1.00 105.92 ? 95  TYR D CZ  1 
ATOM 3962 O OH  . TYR C 2 95  ? 163.095 223.832 264.053 1.00 107.27 ? 95  TYR D OH  1 
ATOM 3963 N N   . CYS C 2 96  ? 161.729 216.026 260.555 1.00 74.91  ? 96  CYS D N   1 
ATOM 3964 C CA  . CYS C 2 96  ? 161.947 214.890 259.668 1.00 76.53  ? 96  CYS D CA  1 
ATOM 3965 C C   . CYS C 2 96  ? 161.786 215.341 258.224 1.00 70.08  ? 96  CYS D C   1 
ATOM 3966 O O   . CYS C 2 96  ? 160.861 216.094 257.900 1.00 73.80  ? 96  CYS D O   1 
ATOM 3967 C CB  . CYS C 2 96  ? 160.999 213.718 259.975 1.00 85.19  ? 96  CYS D CB  1 
ATOM 3968 S SG  . CYS C 2 96  ? 159.237 214.000 259.726 1.00 101.13 ? 96  CYS D SG  1 
ATOM 3969 N N   . ALA C 2 97  ? 162.698 214.890 257.366 1.00 62.07  ? 97  ALA D N   1 
ATOM 3970 C CA  . ALA C 2 97  ? 162.662 215.194 255.945 1.00 58.41  ? 97  ALA D CA  1 
ATOM 3971 C C   . ALA C 2 97  ? 162.958 213.926 255.160 1.00 52.89  ? 97  ALA D C   1 
ATOM 3972 O O   . ALA C 2 97  ? 163.715 213.063 255.611 1.00 56.66  ? 97  ALA D O   1 
ATOM 3973 C CB  . ALA C 2 97  ? 163.664 216.295 255.574 1.00 64.20  ? 97  ALA D CB  1 
ATOM 3974 N N   . ALA C 2 98  ? 162.359 213.823 253.977 1.00 50.59  ? 98  ALA D N   1 
ATOM 3975 C CA  . ALA C 2 98  ? 162.452 212.624 253.158 1.00 49.95  ? 98  ALA D CA  1 
ATOM 3976 C C   . ALA C 2 98  ? 162.909 212.987 251.755 1.00 49.49  ? 98  ALA D C   1 
ATOM 3977 O O   . ALA C 2 98  ? 162.448 213.975 251.179 1.00 59.68  ? 98  ALA D O   1 
ATOM 3978 C CB  . ALA C 2 98  ? 161.107 211.892 253.090 1.00 52.15  ? 98  ALA D CB  1 
ATOM 3979 N N   . ASP C 2 99  ? 163.807 212.177 251.204 1.00 46.70  ? 99  ASP D N   1 
ATOM 3980 C CA  . ASP C 2 99  ? 164.336 212.404 249.872 1.00 45.65  ? 99  ASP D CA  1 
ATOM 3981 C C   . ASP C 2 99  ? 164.123 211.148 249.038 1.00 49.32  ? 99  ASP D C   1 
ATOM 3982 O O   . ASP C 2 99  ? 164.294 210.032 249.545 1.00 55.35  ? 99  ASP D O   1 
ATOM 3983 C CB  . ASP C 2 99  ? 165.832 212.748 249.928 1.00 47.54  ? 99  ASP D CB  1 
ATOM 3984 C CG  . ASP C 2 99  ? 166.283 213.598 248.758 1.00 47.60  ? 99  ASP D CG  1 
ATOM 3985 O OD1 . ASP C 2 99  ? 165.521 214.494 248.342 1.00 45.87  ? 99  ASP D OD1 1 
ATOM 3986 O OD2 . ASP C 2 99  ? 167.401 213.369 248.253 1.00 47.01  ? 99  ASP D OD2 1 
ATOM 3987 N N   . PRO C 2 100 ? 163.727 211.292 247.774 1.00 42.77  ? 100 PRO D N   1 
ATOM 3988 C CA  . PRO C 2 100 ? 163.506 210.110 246.932 1.00 44.11  ? 100 PRO D CA  1 
ATOM 3989 C C   . PRO C 2 100 ? 164.795 209.358 246.637 1.00 47.19  ? 100 PRO D C   1 
ATOM 3990 O O   . PRO C 2 100 ? 165.880 209.938 246.542 1.00 45.54  ? 100 PRO D O   1 
ATOM 3991 C CB  . PRO C 2 100 ? 162.900 210.696 245.654 1.00 40.69  ? 100 PRO D CB  1 
ATOM 3992 C CG  . PRO C 2 100 ? 162.348 212.016 246.062 1.00 46.81  ? 100 PRO D CG  1 
ATOM 3993 C CD  . PRO C 2 100 ? 163.270 212.525 247.116 1.00 43.07  ? 100 PRO D CD  1 
ATOM 3994 N N   . GLY C 2 101 ? 164.657 208.045 246.493 1.00 51.28  ? 101 GLY D N   1 
ATOM 3995 C CA  . GLY C 2 101 ? 165.790 207.162 246.322 1.00 45.91  ? 101 GLY D CA  1 
ATOM 3996 C C   . GLY C 2 101 ? 166.404 206.753 247.650 1.00 46.36  ? 101 GLY D C   1 
ATOM 3997 O O   . GLY C 2 101 ? 166.180 207.367 248.690 1.00 46.95  ? 101 GLY D O   1 
ATOM 3998 N N   . ALA C 2 102 ? 167.208 205.691 247.601 1.00 49.38  ? 102 ALA D N   1 
ATOM 3999 C CA  . ALA C 2 102 ? 167.935 205.219 248.780 1.00 48.05  ? 102 ALA D CA  1 
ATOM 4000 C C   . ALA C 2 102 ? 169.074 206.201 249.038 1.00 45.94  ? 102 ALA D C   1 
ATOM 4001 O O   . ALA C 2 102 ? 170.224 206.000 248.641 1.00 48.98  ? 102 ALA D O   1 
ATOM 4002 C CB  . ALA C 2 102 ? 168.443 203.797 248.575 1.00 50.15  ? 102 ALA D CB  1 
ATOM 4003 N N   . VAL C 2 103 ? 168.737 207.286 249.727 1.00 46.66  ? 103 VAL D N   1 
ATOM 4004 C CA  . VAL C 2 103 ? 169.573 208.481 249.711 1.00 58.13  ? 103 VAL D CA  1 
ATOM 4005 C C   . VAL C 2 103 ? 170.674 208.431 250.767 1.00 62.89  ? 103 VAL D C   1 
ATOM 4006 O O   . VAL C 2 103 ? 171.788 208.903 250.524 1.00 69.91  ? 103 VAL D O   1 
ATOM 4007 C CB  . VAL C 2 103 ? 168.678 209.738 249.851 1.00 61.96  ? 103 VAL D CB  1 
ATOM 4008 C CG1 . VAL C 2 103 ? 167.879 209.726 251.153 1.00 61.93  ? 103 VAL D CG1 1 
ATOM 4009 C CG2 . VAL C 2 103 ? 169.493 211.021 249.716 1.00 60.31  ? 103 VAL D CG2 1 
ATOM 4010 N N   . CYS C 2 104 ? 170.436 207.836 251.933 1.00 59.87  ? 104 CYS D N   1 
ATOM 4011 C CA  . CYS C 2 104 ? 171.366 207.984 253.045 1.00 63.98  ? 104 CYS D CA  1 
ATOM 4012 C C   . CYS C 2 104 ? 172.479 206.943 252.962 1.00 63.84  ? 104 CYS D C   1 
ATOM 4013 O O   . CYS C 2 104 ? 172.224 205.733 253.027 1.00 65.33  ? 104 CYS D O   1 
ATOM 4014 C CB  . CYS C 2 104 ? 170.648 207.918 254.393 1.00 70.30  ? 104 CYS D CB  1 
ATOM 4015 S SG  . CYS C 2 104 ? 169.517 206.569 254.746 1.00 81.20  ? 104 CYS D SG  1 
ATOM 4016 N N   . HIS C 2 105 ? 173.712 207.437 252.816 1.00 68.91  ? 105 HIS D N   1 
ATOM 4017 C CA  . HIS C 2 105 ? 174.959 206.667 252.824 1.00 64.77  ? 105 HIS D CA  1 
ATOM 4018 C C   . HIS C 2 105 ? 174.946 205.602 251.721 1.00 62.22  ? 105 HIS D C   1 
ATOM 4019 O O   . HIS C 2 105 ? 174.922 204.394 251.960 1.00 62.37  ? 105 HIS D O   1 
ATOM 4020 C CB  . HIS C 2 105 ? 175.220 206.074 254.215 1.00 65.33  ? 105 HIS D CB  1 
ATOM 4021 C CG  . HIS C 2 105 ? 176.522 205.348 254.333 1.00 69.55  ? 105 HIS D CG  1 
ATOM 4022 N ND1 . HIS C 2 105 ? 177.731 206.007 254.388 1.00 71.05  ? 105 HIS D ND1 1 
ATOM 4023 C CD2 . HIS C 2 105 ? 176.807 204.029 254.429 1.00 73.64  ? 105 HIS D CD2 1 
ATOM 4024 C CE1 . HIS C 2 105 ? 178.706 205.123 254.500 1.00 71.61  ? 105 HIS D CE1 1 
ATOM 4025 N NE2 . HIS C 2 105 ? 178.172 203.916 254.529 1.00 72.50  ? 105 HIS D NE2 1 
ATOM 4026 N N   . SER C 2 106 ? 174.925 206.104 250.491 1.00 66.61  ? 106 SER D N   1 
ATOM 4027 C CA  . SER C 2 106 ? 174.900 205.286 249.284 1.00 65.40  ? 106 SER D CA  1 
ATOM 4028 C C   . SER C 2 106 ? 176.047 205.671 248.360 1.00 58.10  ? 106 SER D C   1 
ATOM 4029 O O   . SER C 2 106 ? 175.875 205.894 247.160 1.00 53.58  ? 106 SER D O   1 
ATOM 4030 C CB  . SER C 2 106 ? 173.562 205.418 248.569 1.00 71.06  ? 106 SER D CB  1 
ATOM 4031 O OG  . SER C 2 106 ? 173.599 204.747 247.327 1.00 75.59  ? 106 SER D OG  1 
ATOM 4032 N N   . GLY C 2 107 ? 177.246 205.756 248.927 1.00 57.80  ? 107 GLY D N   1 
ATOM 4033 C CA  . GLY C 2 107 ? 178.425 206.137 248.178 1.00 56.38  ? 107 GLY D CA  1 
ATOM 4034 C C   . GLY C 2 107 ? 179.397 206.901 249.048 1.00 61.23  ? 107 GLY D C   1 
ATOM 4035 O O   . GLY C 2 107 ? 179.785 206.428 250.121 1.00 62.66  ? 107 GLY D O   1 
ATOM 4036 N N   . SER C 2 108 ? 179.804 208.083 248.595 1.00 62.81  ? 108 SER D N   1 
ATOM 4037 C CA  . SER C 2 108 ? 180.566 209.012 249.415 1.00 62.45  ? 108 SER D CA  1 
ATOM 4038 C C   . SER C 2 108 ? 179.679 210.068 250.058 1.00 63.36  ? 108 SER D C   1 
ATOM 4039 O O   . SER C 2 108 ? 180.195 211.047 250.607 1.00 66.73  ? 108 SER D O   1 
ATOM 4040 C CB  . SER C 2 108 ? 181.660 209.681 248.581 1.00 61.04  ? 108 SER D CB  1 
ATOM 4041 O OG  . SER C 2 108 ? 181.131 210.216 247.381 1.00 61.46  ? 108 SER D OG  1 
ATOM 4042 N N   . TYR C 2 109 ? 178.360 209.889 250.005 1.00 63.65  ? 109 TYR D N   1 
ATOM 4043 C CA  . TYR C 2 109 ? 177.398 210.884 250.466 1.00 72.21  ? 109 TYR D CA  1 
ATOM 4044 C C   . TYR C 2 109 ? 176.603 210.335 251.644 1.00 75.16  ? 109 TYR D C   1 
ATOM 4045 O O   . TYR C 2 109 ? 175.682 209.534 251.456 1.00 72.55  ? 109 TYR D O   1 
ATOM 4046 C CB  . TYR C 2 109 ? 176.458 211.289 249.334 1.00 76.77  ? 109 TYR D CB  1 
ATOM 4047 C CG  . TYR C 2 109 ? 175.456 212.350 249.728 1.00 84.52  ? 109 TYR D CG  1 
ATOM 4048 C CD1 . TYR C 2 109 ? 175.837 213.680 249.861 1.00 90.88  ? 109 TYR D CD1 1 
ATOM 4049 C CD2 . TYR C 2 109 ? 174.127 212.021 249.967 1.00 84.02  ? 109 TYR D CD2 1 
ATOM 4050 C CE1 . TYR C 2 109 ? 174.922 214.653 250.223 1.00 93.99  ? 109 TYR D CE1 1 
ATOM 4051 C CE2 . TYR C 2 109 ? 173.205 212.986 250.329 1.00 88.86  ? 109 TYR D CE2 1 
ATOM 4052 C CZ  . TYR C 2 109 ? 173.608 214.300 250.455 1.00 94.74  ? 109 TYR D CZ  1 
ATOM 4053 O OH  . TYR C 2 109 ? 172.694 215.263 250.814 1.00 100.00 ? 109 TYR D OH  1 
ATOM 4054 N N   . TYR C 2 110 ? 176.697 210.907 252.848 1.00 78.24  ? 110 TYR D N   1 
ATOM 4055 C CA  . TYR C 2 110 ? 175.781 210.493 253.954 1.00 74.37  ? 110 TYR D CA  1 
ATOM 4056 C C   . TYR C 2 110 ? 174.776 211.635 254.090 1.00 80.99  ? 110 TYR D C   1 
ATOM 4057 O O   . TYR C 2 110 ? 174.879 212.598 253.313 1.00 89.00  ? 110 TYR D O   1 
ATOM 4058 C CB  . TYR C 2 110 ? 176.551 210.110 255.221 1.00 70.47  ? 110 TYR D CB  1 
ATOM 4059 C CG  . TYR C 2 110 ? 175.877 209.677 256.514 1.00 70.13  ? 110 TYR D CG  1 
ATOM 4060 C CD1 . TYR C 2 110 ? 175.528 208.353 256.728 1.00 69.48  ? 110 TYR D CD1 1 
ATOM 4061 C CD2 . TYR C 2 110 ? 175.694 210.570 257.560 1.00 75.40  ? 110 TYR D CD2 1 
ATOM 4062 C CE1 . TYR C 2 110 ? 174.956 207.938 257.919 1.00 72.18  ? 110 TYR D CE1 1 
ATOM 4063 C CE2 . TYR C 2 110 ? 175.121 210.172 258.756 1.00 79.85  ? 110 TYR D CE2 1 
ATOM 4064 C CZ  . TYR C 2 110 ? 174.755 208.851 258.938 1.00 80.60  ? 110 TYR D CZ  1 
ATOM 4065 O OH  . TYR C 2 110 ? 174.191 208.448 260.114 1.00 87.06  ? 110 TYR D OH  1 
ATOM 4066 N N   . TYR C 2 111 ? 173.838 211.560 255.027 1.00 78.25  ? 111 TYR D N   1 
ATOM 4067 C CA  . TYR C 2 111 ? 172.776 212.601 255.104 1.00 79.27  ? 111 TYR D CA  1 
ATOM 4068 C C   . TYR C 2 111 ? 173.271 213.828 255.889 1.00 84.13  ? 111 TYR D C   1 
ATOM 4069 O O   . TYR C 2 111 ? 172.489 214.761 256.080 1.00 83.71  ? 111 TYR D O   1 
ATOM 4070 C CB  . TYR C 2 111 ? 171.503 211.931 255.625 1.00 73.94  ? 111 TYR D CB  1 
ATOM 4071 C CG  . TYR C 2 111 ? 171.557 211.165 256.938 1.00 73.75  ? 111 TYR D CG  1 
ATOM 4072 C CD1 . TYR C 2 111 ? 171.451 211.821 258.157 1.00 74.73  ? 111 TYR D CD1 1 
ATOM 4073 C CD2 . TYR C 2 111 ? 171.643 209.781 256.956 1.00 72.58  ? 111 TYR D CD2 1 
ATOM 4074 C CE1 . TYR C 2 111 ? 171.475 211.128 259.354 1.00 73.16  ? 111 TYR D CE1 1 
ATOM 4075 C CE2 . TYR C 2 111 ? 171.666 209.076 258.146 1.00 73.45  ? 111 TYR D CE2 1 
ATOM 4076 C CZ  . TYR C 2 111 ? 171.581 209.751 259.348 1.00 73.94  ? 111 TYR D CZ  1 
ATOM 4077 O OH  . TYR C 2 111 ? 171.608 209.062 260.524 1.00 78.27  ? 111 TYR D OH  1 
ATOM 4078 N N   . THR C 2 112 ? 174.525 213.826 256.337 1.00 88.17  ? 112 THR D N   1 
ATOM 4079 C CA  . THR C 2 112 ? 175.094 215.022 256.980 1.00 89.81  ? 112 THR D CA  1 
ATOM 4080 C C   . THR C 2 112 ? 174.853 216.191 256.064 1.00 94.38  ? 112 THR D C   1 
ATOM 4081 O O   . THR C 2 112 ? 174.318 217.211 256.550 1.00 96.47  ? 112 THR D O   1 
ATOM 4082 C CB  . THR C 2 112 ? 176.588 214.844 257.195 1.00 93.26  ? 112 THR D CB  1 
ATOM 4083 O OG1 . THR C 2 112 ? 177.104 214.530 255.905 1.00 96.88  ? 112 THR D OG1 1 
ATOM 4084 C CG2 . THR C 2 112 ? 176.907 213.725 258.170 1.00 92.04  ? 112 THR D CG2 1 
ATOM 4085 N N   . ASP C 2 113 ? 175.227 216.075 254.784 1.00 96.67  ? 113 ASP D N   1 
ATOM 4086 C CA  . ASP C 2 113 ? 174.865 217.177 253.851 1.00 102.24 ? 113 ASP D CA  1 
ATOM 4087 C C   . ASP C 2 113 ? 173.348 217.338 253.953 1.00 101.06 ? 113 ASP D C   1 
ATOM 4088 O O   . ASP C 2 113 ? 172.631 216.479 253.402 1.00 102.40 ? 113 ASP D O   1 
ATOM 4089 C CB  . ASP C 2 113 ? 175.408 216.927 252.456 1.00 102.16 ? 113 ASP D CB  1 
ATOM 4090 C CG  . ASP C 2 113 ? 176.923 216.822 252.365 1.00 105.63 ? 113 ASP D CG  1 
ATOM 4091 O OD1 . ASP C 2 113 ? 177.600 217.814 252.707 1.00 108.92 ? 113 ASP D OD1 1 
ATOM 4092 O OD2 . ASP C 2 113 ? 177.414 215.746 251.965 1.00 105.86 ? 113 ASP D OD2 1 
ATOM 4093 N N   . ASP C 2 114 ? 172.874 218.401 254.614 1.00 98.93  ? 114 ASP D N   1 
ATOM 4094 C CA  . ASP C 2 114 ? 171.413 218.547 254.886 1.00 97.82  ? 114 ASP D CA  1 
ATOM 4095 C C   . ASP C 2 114 ? 170.621 218.870 253.616 1.00 94.60  ? 114 ASP D C   1 
ATOM 4096 O O   . ASP C 2 114 ? 169.407 219.097 253.742 1.00 97.17  ? 114 ASP D O   1 
ATOM 4097 C CB  . ASP C 2 114 ? 171.143 219.588 255.962 1.00 101.13 ? 114 ASP D CB  1 
ATOM 4098 C CG  . ASP C 2 114 ? 169.917 219.327 256.826 1.00 95.53  ? 114 ASP D CG  1 
ATOM 4099 O OD1 . ASP C 2 114 ? 169.269 218.278 256.623 1.00 89.06  ? 114 ASP D OD1 1 
ATOM 4100 O OD2 . ASP C 2 114 ? 169.617 220.175 257.692 1.00 95.35  ? 114 ASP D OD2 1 
ATOM 4101 N N   . ASP C 2 115 ? 171.259 218.893 252.451 1.00 91.07  ? 115 ASP D N   1 
ATOM 4102 C CA  . ASP C 2 115 ? 170.435 219.138 251.243 1.00 96.72  ? 115 ASP D CA  1 
ATOM 4103 C C   . ASP C 2 115 ? 169.201 218.231 251.305 1.00 86.27  ? 115 ASP D C   1 
ATOM 4104 O O   . ASP C 2 115 ? 169.304 217.100 250.802 1.00 88.70  ? 115 ASP D O   1 
ATOM 4105 C CB  . ASP C 2 115 ? 171.235 218.907 249.971 1.00 106.09 ? 115 ASP D CB  1 
ATOM 4106 C CG  . ASP C 2 115 ? 172.675 219.398 250.009 1.00 108.57 ? 115 ASP D CG  1 
ATOM 4107 O OD1 . ASP C 2 115 ? 172.874 220.614 250.210 1.00 108.73 ? 115 ASP D OD1 1 
ATOM 4108 O OD2 . ASP C 2 115 ? 173.584 218.560 249.836 1.00 110.31 ? 115 ASP D OD2 1 
ATOM 4109 N N   . PHE C 2 116 ? 168.084 218.685 251.869 1.00 76.78  ? 116 PHE D N   1 
ATOM 4110 C CA  . PHE C 2 116 ? 166.946 217.734 251.951 1.00 74.17  ? 116 PHE D CA  1 
ATOM 4111 C C   . PHE C 2 116 ? 165.675 218.362 251.427 1.00 79.71  ? 116 PHE D C   1 
ATOM 4112 O O   . PHE C 2 116 ? 165.391 219.522 251.776 1.00 88.19  ? 116 PHE D O   1 
ATOM 4113 C CB  . PHE C 2 116 ? 166.767 217.198 253.372 1.00 74.91  ? 116 PHE D CB  1 
ATOM 4114 C CG  . PHE C 2 116 ? 167.319 215.789 253.542 1.00 80.43  ? 116 PHE D CG  1 
ATOM 4115 C CD1 . PHE C 2 116 ? 166.586 214.682 253.131 1.00 65.91  ? 116 PHE D CD1 1 
ATOM 4116 C CD2 . PHE C 2 116 ? 168.566 215.577 254.116 1.00 86.25  ? 116 PHE D CD2 1 
ATOM 4117 C CE1 . PHE C 2 116 ? 167.089 213.404 253.287 1.00 62.20  ? 116 PHE D CE1 1 
ATOM 4118 C CE2 . PHE C 2 116 ? 169.062 214.294 254.269 1.00 81.83  ? 116 PHE D CE2 1 
ATOM 4119 C CZ  . PHE C 2 116 ? 168.322 213.212 253.857 1.00 71.90  ? 116 PHE D CZ  1 
ATOM 4120 N N   . TYR C 2 117 ? 164.921 217.624 250.616 1.00 75.35  ? 117 TYR D N   1 
ATOM 4121 C CA  . TYR C 2 117 ? 163.618 218.122 250.115 1.00 70.58  ? 117 TYR D CA  1 
ATOM 4122 C C   . TYR C 2 117 ? 162.580 217.928 251.192 1.00 59.26  ? 117 TYR D C   1 
ATOM 4123 O O   . TYR C 2 117 ? 162.922 217.875 252.379 1.00 58.32  ? 117 TYR D O   1 
ATOM 4124 C CB  . TYR C 2 117 ? 163.072 217.378 248.898 1.00 74.15  ? 117 TYR D CB  1 
ATOM 4125 C CG  . TYR C 2 117 ? 162.455 218.214 247.784 1.00 77.03  ? 117 TYR D CG  1 
ATOM 4126 C CD1 . TYR C 2 117 ? 161.957 219.488 248.022 1.00 85.16  ? 117 TYR D CD1 1 
ATOM 4127 C CD2 . TYR C 2 117 ? 162.344 217.707 246.497 1.00 71.21  ? 117 TYR D CD2 1 
ATOM 4128 C CE1 . TYR C 2 117 ? 161.392 220.239 247.005 1.00 86.77  ? 117 TYR D CE1 1 
ATOM 4129 C CE2 . TYR C 2 117 ? 161.782 218.447 245.472 1.00 75.59  ? 117 TYR D CE2 1 
ATOM 4130 C CZ  . TYR C 2 117 ? 161.302 219.716 245.728 1.00 83.93  ? 117 TYR D CZ  1 
ATOM 4131 O OH  . TYR C 2 117 ? 160.746 220.447 244.723 1.00 92.74  ? 117 TYR D OH  1 
ATOM 4132 N N   . TYR C 2 118 ? 161.325 217.823 250.776 1.00 62.24  ? 118 TYR D N   1 
ATOM 4133 C CA  . TYR C 2 118 ? 160.206 217.711 251.740 1.00 62.84  ? 118 TYR D CA  1 
ATOM 4134 C C   . TYR C 2 118 ? 160.649 217.980 253.177 1.00 62.64  ? 118 TYR D C   1 
ATOM 4135 O O   . TYR C 2 118 ? 160.846 217.008 253.933 1.00 67.02  ? 118 TYR D O   1 
ATOM 4136 C CB  . TYR C 2 118 ? 159.639 216.311 251.521 1.00 62.63  ? 118 TYR D CB  1 
ATOM 4137 C CG  . TYR C 2 118 ? 159.522 215.865 250.070 1.00 60.55  ? 118 TYR D CG  1 
ATOM 4138 C CD1 . TYR C 2 118 ? 159.204 216.760 249.058 1.00 59.14  ? 118 TYR D CD1 1 
ATOM 4139 C CD2 . TYR C 2 118 ? 159.742 214.540 249.718 1.00 64.50  ? 118 TYR D CD2 1 
ATOM 4140 C CE1 . TYR C 2 118 ? 159.106 216.349 247.741 1.00 61.13  ? 118 TYR D CE1 1 
ATOM 4141 C CE2 . TYR C 2 118 ? 159.647 214.116 248.404 1.00 63.99  ? 118 TYR D CE2 1 
ATOM 4142 C CZ  . TYR C 2 118 ? 159.325 215.025 247.414 1.00 63.04  ? 118 TYR D CZ  1 
ATOM 4143 O OH  . TYR C 2 118 ? 159.229 214.613 246.117 1.00 68.11  ? 118 TYR D OH  1 
ATOM 4144 N N   . ARG C 2 119 ? 160.737 219.248 253.579 1.00 63.36  ? 119 ARG D N   1 
ATOM 4145 C CA  . ARG C 2 119 ? 161.054 219.590 254.959 1.00 61.82  ? 119 ARG D CA  1 
ATOM 4146 C C   . ARG C 2 119 ? 159.776 219.714 255.786 1.00 65.17  ? 119 ARG D C   1 
ATOM 4147 O O   . ARG C 2 119 ? 158.776 220.270 255.326 1.00 69.07  ? 119 ARG D O   1 
ATOM 4148 C CB  . ARG C 2 119 ? 161.853 220.893 254.997 1.00 63.94  ? 119 ARG D CB  1 
ATOM 4149 C CG  . ARG C 2 119 ? 161.933 221.576 256.348 1.00 66.64  ? 119 ARG D CG  1 
ATOM 4150 C CD  . ARG C 2 119 ? 163.001 220.939 257.217 1.00 71.53  ? 119 ARG D CD  1 
ATOM 4151 N NE  . ARG C 2 119 ? 164.292 221.592 257.038 1.00 77.67  ? 119 ARG D NE  1 
ATOM 4152 C CZ  . ARG C 2 119 ? 164.649 222.728 257.622 1.00 83.06  ? 119 ARG D CZ  1 
ATOM 4153 N NH1 . ARG C 2 119 ? 163.835 223.368 258.445 1.00 88.31  ? 119 ARG D NH1 1 
ATOM 4154 N NH2 . ARG C 2 119 ? 165.854 223.234 257.374 1.00 81.27  ? 119 ARG D NH2 1 
ATOM 4155 N N   . GLY C 2 120 ? 159.813 219.189 257.015 1.00 66.12  ? 120 GLY D N   1 
ATOM 4156 C CA  . GLY C 2 120 ? 158.668 219.217 257.898 1.00 79.72  ? 120 GLY D CA  1 
ATOM 4157 C C   . GLY C 2 120 ? 158.640 220.445 258.803 1.00 84.74  ? 120 GLY D C   1 
ATOM 4158 O O   . GLY C 2 120 ? 159.554 221.264 258.822 1.00 83.35  ? 120 GLY D O   1 
ATOM 4159 N N   . GLN C 2 121 ? 157.550 220.552 259.569 1.00 90.70  ? 121 GLN D N   1 
ATOM 4160 C CA  . GLN C 2 121 ? 157.348 221.708 260.441 1.00 91.74  ? 121 GLN D CA  1 
ATOM 4161 C C   . GLN C 2 121 ? 158.115 221.567 261.753 1.00 89.16  ? 121 GLN D C   1 
ATOM 4162 O O   . GLN C 2 121 ? 158.989 222.383 262.062 1.00 86.10  ? 121 GLN D O   1 
ATOM 4163 C CB  . GLN C 2 121 ? 155.853 221.922 260.717 1.00 95.72  ? 121 GLN D CB  1 
ATOM 4164 C CG  . GLN C 2 121 ? 155.024 222.476 259.551 1.00 97.71  ? 121 GLN D CG  1 
ATOM 4165 C CD  . GLN C 2 121 ? 154.843 221.498 258.406 1.00 98.73  ? 121 GLN D CD  1 
ATOM 4166 O OE1 . GLN C 2 121 ? 155.253 221.764 257.276 1.00 100.40 ? 121 GLN D OE1 1 
ATOM 4167 N NE2 . GLN C 2 121 ? 154.222 220.359 258.693 1.00 96.81  ? 121 GLN D NE2 1 
ATOM 4168 N N   . GLY C 2 122 ? 157.791 220.546 262.544 1.00 92.26  ? 122 GLY D N   1 
ATOM 4169 C CA  . GLY C 2 122 ? 158.520 220.281 263.772 1.00 96.79  ? 122 GLY D CA  1 
ATOM 4170 C C   . GLY C 2 122 ? 157.667 220.112 265.014 1.00 103.13 ? 122 GLY D C   1 
ATOM 4171 O O   . GLY C 2 122 ? 156.527 220.584 265.068 1.00 105.91 ? 122 GLY D O   1 
ATOM 4172 N N   . THR C 2 123 ? 158.214 219.428 266.020 1.00 103.15 ? 123 THR D N   1 
ATOM 4173 C CA  . THR C 2 123 ? 157.576 219.261 267.319 1.00 106.18 ? 123 THR D CA  1 
ATOM 4174 C C   . THR C 2 123 ? 158.631 219.374 268.412 1.00 107.56 ? 123 THR D C   1 
ATOM 4175 O O   . THR C 2 123 ? 159.702 218.767 268.329 1.00 105.92 ? 123 THR D O   1 
ATOM 4176 C CB  . THR C 2 123 ? 156.839 217.908 267.417 1.00 103.97 ? 123 THR D CB  1 
ATOM 4177 O OG1 . THR C 2 123 ? 155.828 217.843 266.406 1.00 103.00 ? 123 THR D OG1 1 
ATOM 4178 C CG2 . THR C 2 123 ? 156.182 217.730 268.779 1.00 105.60 ? 123 THR D CG2 1 
ATOM 4179 N N   . GLN C 2 124 ? 158.315 220.156 269.441 1.00 109.95 ? 124 GLN D N   1 
ATOM 4180 C CA  . GLN C 2 124 ? 159.237 220.452 270.531 1.00 112.06 ? 124 GLN D CA  1 
ATOM 4181 C C   . GLN C 2 124 ? 159.185 219.319 271.550 1.00 113.73 ? 124 GLN D C   1 
ATOM 4182 O O   . GLN C 2 124 ? 158.112 218.996 272.070 1.00 111.92 ? 124 GLN D O   1 
ATOM 4183 C CB  . GLN C 2 124 ? 158.873 221.786 271.185 1.00 114.59 ? 124 GLN D CB  1 
ATOM 4184 C CG  . GLN C 2 124 ? 159.792 222.282 272.307 1.00 118.95 ? 124 GLN D CG  1 
ATOM 4185 C CD  . GLN C 2 124 ? 161.256 221.918 272.119 1.00 117.81 ? 124 GLN D CD  1 
ATOM 4186 O OE1 . GLN C 2 124 ? 161.715 220.868 272.568 1.00 115.96 ? 124 GLN D OE1 1 
ATOM 4187 N NE2 . GLN C 2 124 ? 161.996 222.790 271.445 1.00 115.14 ? 124 GLN D NE2 1 
ATOM 4188 N N   . VAL C 2 125 ? 160.340 218.719 271.830 1.00 113.48 ? 125 VAL D N   1 
ATOM 4189 C CA  . VAL C 2 125 ? 160.462 217.633 272.798 1.00 111.95 ? 125 VAL D CA  1 
ATOM 4190 C C   . VAL C 2 125 ? 161.479 218.052 273.848 1.00 114.03 ? 125 VAL D C   1 
ATOM 4191 O O   . VAL C 2 125 ? 162.652 218.280 273.526 1.00 111.31 ? 125 VAL D O   1 
ATOM 4192 C CB  . VAL C 2 125 ? 160.883 216.313 272.132 1.00 112.81 ? 125 VAL D CB  1 
ATOM 4193 C CG1 . VAL C 2 125 ? 161.098 215.233 273.182 1.00 115.75 ? 125 VAL D CG1 1 
ATOM 4194 C CG2 . VAL C 2 125 ? 159.848 215.875 271.110 1.00 116.31 ? 125 VAL D CG2 1 
ATOM 4195 N N   . THR C 2 126 ? 161.041 218.138 275.101 1.00 121.87 ? 126 THR D N   1 
ATOM 4196 C CA  . THR C 2 126 ? 161.897 218.564 276.196 1.00 126.31 ? 126 THR D CA  1 
ATOM 4197 C C   . THR C 2 126 ? 161.916 217.510 277.295 1.00 128.96 ? 126 THR D C   1 
ATOM 4198 O O   . THR C 2 126 ? 160.983 216.713 277.436 1.00 130.96 ? 126 THR D O   1 
ATOM 4199 C CB  . THR C 2 126 ? 161.445 219.921 276.767 1.00 129.33 ? 126 THR D CB  1 
ATOM 4200 O OG1 . THR C 2 126 ? 162.401 220.381 277.731 1.00 131.50 ? 126 THR D OG1 1 
ATOM 4201 C CG2 . THR C 2 126 ? 160.071 219.819 277.416 1.00 130.27 ? 126 THR D CG2 1 
ATOM 4202 N N   . VAL C 2 127 ? 163.006 217.498 278.057 1.00 128.00 ? 127 VAL D N   1 
ATOM 4203 C CA  . VAL C 2 127 ? 163.183 216.566 279.163 1.00 132.54 ? 127 VAL D CA  1 
ATOM 4204 C C   . VAL C 2 127 ? 163.812 217.319 280.331 1.00 131.48 ? 127 VAL D C   1 
ATOM 4205 O O   . VAL C 2 127 ? 164.688 218.171 280.139 1.00 127.45 ? 127 VAL D O   1 
ATOM 4206 C CB  . VAL C 2 127 ? 164.013 215.328 278.732 1.00 136.81 ? 127 VAL D CB  1 
ATOM 4207 C CG1 . VAL C 2 127 ? 165.431 215.702 278.300 1.00 131.40 ? 127 VAL D CG1 1 
ATOM 4208 C CG2 . VAL C 2 127 ? 164.040 214.273 279.827 1.00 141.51 ? 127 VAL D CG2 1 
ATOM 4209 N N   . SER C 2 128 ? 163.323 217.042 281.537 1.00 134.70 ? 128 SER D N   1 
ATOM 4210 C CA  . SER C 2 128 ? 163.809 217.690 282.749 1.00 142.65 ? 128 SER D CA  1 
ATOM 4211 C C   . SER C 2 128 ? 163.403 216.836 283.943 1.00 147.00 ? 128 SER D C   1 
ATOM 4212 O O   . SER C 2 128 ? 162.777 215.783 283.795 1.00 143.45 ? 128 SER D O   1 
ATOM 4213 C CB  . SER C 2 128 ? 163.266 219.117 282.878 1.00 145.01 ? 128 SER D CB  1 
ATOM 4214 O OG  . SER C 2 128 ? 161.938 219.115 283.371 1.00 146.93 ? 128 SER D OG  1 
ATOM 4215 N N   . SER C 2 129 ? 163.763 217.304 285.134 1.00 154.42 ? 129 SER D N   1 
ATOM 4216 C CA  . SER C 2 129 ? 163.402 216.620 286.370 1.00 153.65 ? 129 SER D CA  1 
ATOM 4217 C C   . SER C 2 129 ? 162.521 217.510 287.241 1.00 151.14 ? 129 SER D C   1 
ATOM 4218 O O   . SER C 2 129 ? 161.766 217.026 288.084 1.00 150.41 ? 129 SER D O   1 
ATOM 4219 C CB  . SER C 2 129 ? 164.656 216.201 287.141 1.00 152.70 ? 129 SER D CB  1 
ATOM 4220 O OG  . SER C 2 129 ? 164.339 215.852 288.477 1.00 155.45 ? 129 SER D OG  1 
ATOM 4221 N N   . GLN D 2 1   ? 200.319 177.485 231.455 1.00 77.82  ? 1   GLN E N   1 
ATOM 4222 C CA  . GLN D 2 1   ? 199.070 177.085 232.093 1.00 76.40  ? 1   GLN E CA  1 
ATOM 4223 C C   . GLN D 2 1   ? 198.045 178.212 232.005 1.00 76.42  ? 1   GLN E C   1 
ATOM 4224 O O   . GLN D 2 1   ? 198.350 179.364 232.311 1.00 79.39  ? 1   GLN E O   1 
ATOM 4225 C CB  . GLN D 2 1   ? 199.317 176.693 233.553 1.00 78.02  ? 1   GLN E CB  1 
ATOM 4226 C CG  . GLN D 2 1   ? 198.073 176.689 234.428 1.00 83.88  ? 1   GLN E CG  1 
ATOM 4227 C CD  . GLN D 2 1   ? 197.076 175.622 234.017 1.00 88.12  ? 1   GLN E CD  1 
ATOM 4228 O OE1 . GLN D 2 1   ? 197.450 174.487 233.723 1.00 86.94  ? 1   GLN E OE1 1 
ATOM 4229 N NE2 . GLN D 2 1   ? 195.799 175.985 233.991 1.00 86.29  ? 1   GLN E NE2 1 
ATOM 4230 N N   . VAL D 2 2   ? 196.830 177.870 231.575 1.00 73.50  ? 2   VAL E N   1 
ATOM 4231 C CA  . VAL D 2 2   ? 195.770 178.862 231.444 1.00 69.97  ? 2   VAL E CA  1 
ATOM 4232 C C   . VAL D 2 2   ? 195.286 179.268 232.829 1.00 71.89  ? 2   VAL E C   1 
ATOM 4233 O O   . VAL D 2 2   ? 194.926 178.418 233.654 1.00 72.69  ? 2   VAL E O   1 
ATOM 4234 C CB  . VAL D 2 2   ? 194.621 178.308 230.591 1.00 67.56  ? 2   VAL E CB  1 
ATOM 4235 C CG1 . VAL D 2 2   ? 193.473 179.298 230.539 1.00 61.94  ? 2   VAL E CG1 1 
ATOM 4236 C CG2 . VAL D 2 2   ? 195.113 177.978 229.190 1.00 63.93  ? 2   VAL E CG2 1 
ATOM 4237 N N   . GLN D 2 3   ? 195.275 180.573 233.090 1.00 68.15  ? 3   GLN E N   1 
ATOM 4238 C CA  . GLN D 2 3   ? 194.904 181.113 234.387 1.00 64.61  ? 3   GLN E CA  1 
ATOM 4239 C C   . GLN D 2 3   ? 193.769 182.114 234.232 1.00 61.68  ? 3   GLN E C   1 
ATOM 4240 O O   . GLN D 2 3   ? 193.681 182.827 233.228 1.00 62.58  ? 3   GLN E O   1 
ATOM 4241 C CB  . GLN D 2 3   ? 196.097 181.789 235.069 1.00 65.17  ? 3   GLN E CB  1 
ATOM 4242 C CG  . GLN D 2 3   ? 197.194 180.832 235.498 1.00 76.57  ? 3   GLN E CG  1 
ATOM 4243 C CD  . GLN D 2 3   ? 198.561 181.486 235.503 1.00 87.84  ? 3   GLN E CD  1 
ATOM 4244 O OE1 . GLN D 2 3   ? 198.675 182.711 235.488 1.00 93.91  ? 3   GLN E OE1 1 
ATOM 4245 N NE2 . GLN D 2 3   ? 199.608 180.669 235.522 1.00 83.98  ? 3   GLN E NE2 1 
ATOM 4246 N N   . LEU D 2 4   ? 192.899 182.158 235.237 1.00 58.43  ? 4   LEU E N   1 
ATOM 4247 C CA  . LEU D 2 4   ? 191.767 183.072 235.272 1.00 55.56  ? 4   LEU E CA  1 
ATOM 4248 C C   . LEU D 2 4   ? 191.929 183.987 236.478 1.00 60.99  ? 4   LEU E C   1 
ATOM 4249 O O   . LEU D 2 4   ? 192.130 183.509 237.599 1.00 64.57  ? 4   LEU E O   1 
ATOM 4250 C CB  . LEU D 2 4   ? 190.432 182.317 235.352 1.00 51.57  ? 4   LEU E CB  1 
ATOM 4251 C CG  . LEU D 2 4   ? 189.757 181.687 234.120 1.00 51.06  ? 4   LEU E CG  1 
ATOM 4252 C CD1 . LEU D 2 4   ? 189.201 182.753 233.190 1.00 51.22  ? 4   LEU E CD1 1 
ATOM 4253 C CD2 . LEU D 2 4   ? 190.636 180.705 233.350 1.00 57.32  ? 4   LEU E CD2 1 
ATOM 4254 N N   . GLN D 2 5   ? 191.840 185.295 236.250 1.00 61.61  ? 5   GLN E N   1 
ATOM 4255 C CA  . GLN D 2 5   ? 192.091 186.293 237.282 1.00 63.88  ? 5   GLN E CA  1 
ATOM 4256 C C   . GLN D 2 5   ? 190.849 187.145 237.490 1.00 64.33  ? 5   GLN E C   1 
ATOM 4257 O O   . GLN D 2 5   ? 190.268 187.648 236.523 1.00 64.45  ? 5   GLN E O   1 
ATOM 4258 C CB  . GLN D 2 5   ? 193.286 187.178 236.905 1.00 63.84  ? 5   GLN E CB  1 
ATOM 4259 C CG  . GLN D 2 5   ? 193.573 188.324 237.871 1.00 70.89  ? 5   GLN E CG  1 
ATOM 4260 C CD  . GLN D 2 5   ? 193.706 187.883 239.320 1.00 78.05  ? 5   GLN E CD  1 
ATOM 4261 O OE1 . GLN D 2 5   ? 194.268 186.827 239.617 1.00 73.70  ? 5   GLN E OE1 1 
ATOM 4262 N NE2 . GLN D 2 5   ? 193.184 188.695 240.232 1.00 82.97  ? 5   GLN E NE2 1 
ATOM 4263 N N   . GLU D 2 6   ? 190.451 187.310 238.747 1.00 64.98  ? 6   GLU E N   1 
ATOM 4264 C CA  . GLU D 2 6   ? 189.302 188.128 239.104 1.00 63.36  ? 6   GLU E CA  1 
ATOM 4265 C C   . GLU D 2 6   ? 189.735 189.522 239.546 1.00 63.38  ? 6   GLU E C   1 
ATOM 4266 O O   . GLU D 2 6   ? 190.896 189.765 239.886 1.00 68.27  ? 6   GLU E O   1 
ATOM 4267 C CB  . GLU D 2 6   ? 188.479 187.472 240.215 1.00 61.83  ? 6   GLU E CB  1 
ATOM 4268 C CG  . GLU D 2 6   ? 188.014 186.068 239.917 1.00 64.96  ? 6   GLU E CG  1 
ATOM 4269 C CD  . GLU D 2 6   ? 188.748 185.023 240.727 1.00 67.73  ? 6   GLU E CD  1 
ATOM 4270 O OE1 . GLU D 2 6   ? 189.822 185.342 241.278 1.00 64.78  ? 6   GLU E OE1 1 
ATOM 4271 O OE2 . GLU D 2 6   ? 188.250 183.882 240.817 1.00 66.34  ? 6   GLU E OE2 1 
ATOM 4272 N N   . SER D 2 7   ? 188.770 190.440 239.539 1.00 58.44  ? 7   SER E N   1 
ATOM 4273 C CA  . SER D 2 7   ? 188.980 191.800 240.008 1.00 61.93  ? 7   SER E CA  1 
ATOM 4274 C C   . SER D 2 7   ? 187.643 192.380 240.444 1.00 63.98  ? 7   SER E C   1 
ATOM 4275 O O   . SER D 2 7   ? 186.593 192.034 239.896 1.00 63.40  ? 7   SER E O   1 
ATOM 4276 C CB  . SER D 2 7   ? 189.616 192.683 238.928 1.00 64.86  ? 7   SER E CB  1 
ATOM 4277 O OG  . SER D 2 7   ? 189.529 194.054 239.276 1.00 66.59  ? 7   SER E OG  1 
ATOM 4278 N N   . GLY D 2 8   ? 187.691 193.268 241.433 1.00 63.12  ? 8   GLY E N   1 
ATOM 4279 C CA  . GLY D 2 8   ? 186.484 193.885 241.947 1.00 58.80  ? 8   GLY E CA  1 
ATOM 4280 C C   . GLY D 2 8   ? 186.409 193.881 243.459 1.00 64.10  ? 8   GLY E C   1 
ATOM 4281 O O   . GLY D 2 8   ? 187.434 193.983 244.139 1.00 70.80  ? 8   GLY E O   1 
ATOM 4282 N N   . GLY D 2 9   ? 185.200 193.764 243.999 1.00 64.52  ? 9   GLY E N   1 
ATOM 4283 C CA  . GLY D 2 9   ? 185.017 193.749 245.433 1.00 67.16  ? 9   GLY E CA  1 
ATOM 4284 C C   . GLY D 2 9   ? 185.124 195.134 246.041 1.00 71.05  ? 9   GLY E C   1 
ATOM 4285 O O   . GLY D 2 9   ? 185.204 196.155 245.351 1.00 72.79  ? 9   GLY E O   1 
ATOM 4286 N N   . GLY D 2 10  ? 185.122 195.161 247.371 1.00 72.18  ? 10  GLY E N   1 
ATOM 4287 C CA  . GLY D 2 10  ? 185.269 196.413 248.084 1.00 74.29  ? 10  GLY E CA  1 
ATOM 4288 C C   . GLY D 2 10  ? 184.445 196.514 249.350 1.00 70.79  ? 10  GLY E C   1 
ATOM 4289 O O   . GLY D 2 10  ? 184.248 195.524 250.060 1.00 70.99  ? 10  GLY E O   1 
ATOM 4290 N N   . LEU D 2 11  ? 183.955 197.719 249.636 1.00 66.75  ? 11  LEU E N   1 
ATOM 4291 C CA  . LEU D 2 11  ? 183.208 197.996 250.857 1.00 66.57  ? 11  LEU E CA  1 
ATOM 4292 C C   . LEU D 2 11  ? 181.840 198.565 250.510 1.00 69.39  ? 11  LEU E C   1 
ATOM 4293 O O   . LEU D 2 11  ? 181.459 199.630 251.010 1.00 72.42  ? 11  LEU E O   1 
ATOM 4294 C CB  . LEU D 2 11  ? 183.968 198.966 251.770 1.00 72.61  ? 11  LEU E CB  1 
ATOM 4295 C CG  . LEU D 2 11  ? 185.061 198.470 252.730 1.00 76.57  ? 11  LEU E CG  1 
ATOM 4296 C CD1 . LEU D 2 11  ? 184.466 197.530 253.774 1.00 72.66  ? 11  LEU E CD1 1 
ATOM 4297 C CD2 . LEU D 2 11  ? 186.262 197.833 252.034 1.00 74.78  ? 11  LEU E CD2 1 
ATOM 4298 N N   . VAL D 2 12  ? 181.119 197.873 249.624 1.00 63.63  ? 12  VAL E N   1 
ATOM 4299 C CA  . VAL D 2 12  ? 179.804 198.318 249.177 1.00 54.30  ? 12  VAL E CA  1 
ATOM 4300 C C   . VAL D 2 12  ? 178.833 198.332 250.355 1.00 55.80  ? 12  VAL E C   1 
ATOM 4301 O O   . VAL D 2 12  ? 178.993 197.596 251.339 1.00 63.47  ? 12  VAL E O   1 
ATOM 4302 C CB  . VAL D 2 12  ? 179.313 197.401 248.037 1.00 53.46  ? 12  VAL E CB  1 
ATOM 4303 C CG1 . VAL D 2 12  ? 179.077 195.985 248.545 1.00 56.42  ? 12  VAL E CG1 1 
ATOM 4304 C CG2 . VAL D 2 12  ? 178.087 197.968 247.312 1.00 51.78  ? 12  VAL E CG2 1 
ATOM 4305 N N   . GLN D 2 13  ? 177.845 199.213 250.282 1.00 54.98  ? 13  GLN E N   1 
ATOM 4306 C CA  . GLN D 2 13  ? 176.811 199.368 251.287 1.00 51.79  ? 13  GLN E CA  1 
ATOM 4307 C C   . GLN D 2 13  ? 175.508 198.748 250.795 1.00 51.83  ? 13  GLN E C   1 
ATOM 4308 O O   . GLN D 2 13  ? 175.330 198.554 249.587 1.00 60.36  ? 13  GLN E O   1 
ATOM 4309 C CB  . GLN D 2 13  ? 176.618 200.857 251.602 1.00 46.11  ? 13  GLN E CB  1 
ATOM 4310 C CG  . GLN D 2 13  ? 177.846 201.478 252.227 1.00 56.37  ? 13  GLN E CG  1 
ATOM 4311 C CD  . GLN D 2 13  ? 178.202 200.842 253.557 1.00 67.66  ? 13  GLN E CD  1 
ATOM 4312 O OE1 . GLN D 2 13  ? 177.502 201.021 254.553 1.00 72.98  ? 13  GLN E OE1 1 
ATOM 4313 N NE2 . GLN D 2 13  ? 179.298 200.092 253.578 1.00 65.59  ? 13  GLN E NE2 1 
ATOM 4314 N N   . PRO D 2 14  ? 174.599 198.365 251.701 1.00 42.40  ? 14  PRO E N   1 
ATOM 4315 C CA  . PRO D 2 14  ? 173.334 197.747 251.266 1.00 43.66  ? 14  PRO E CA  1 
ATOM 4316 C C   . PRO D 2 14  ? 172.506 198.684 250.401 1.00 50.29  ? 14  PRO E C   1 
ATOM 4317 O O   . PRO D 2 14  ? 172.234 199.829 250.770 1.00 52.90  ? 14  PRO E O   1 
ATOM 4318 C CB  . PRO D 2 14  ? 172.630 197.421 252.588 1.00 43.13  ? 14  PRO E CB  1 
ATOM 4319 C CG  . PRO D 2 14  ? 173.725 197.301 253.570 1.00 45.32  ? 14  PRO E CG  1 
ATOM 4320 C CD  . PRO D 2 14  ? 174.741 198.314 253.167 1.00 44.98  ? 14  PRO E CD  1 
ATOM 4321 N N   . GLY D 2 15  ? 172.104 198.180 249.237 1.00 56.00  ? 15  GLY E N   1 
ATOM 4322 C CA  . GLY D 2 15  ? 171.507 198.991 248.199 1.00 58.87  ? 15  GLY E CA  1 
ATOM 4323 C C   . GLY D 2 15  ? 172.470 199.434 247.121 1.00 58.63  ? 15  GLY E C   1 
ATOM 4324 O O   . GLY D 2 15  ? 172.037 200.064 246.149 1.00 66.33  ? 15  GLY E O   1 
ATOM 4325 N N   . GLY D 2 16  ? 173.758 199.124 247.261 1.00 48.64  ? 16  GLY E N   1 
ATOM 4326 C CA  . GLY D 2 16  ? 174.761 199.514 246.294 1.00 43.96  ? 16  GLY E CA  1 
ATOM 4327 C C   . GLY D 2 16  ? 174.899 198.514 245.163 1.00 46.57  ? 16  GLY E C   1 
ATOM 4328 O O   . GLY D 2 16  ? 174.039 197.663 244.928 1.00 51.50  ? 16  GLY E O   1 
ATOM 4329 N N   . SER D 2 17  ? 176.017 198.628 244.447 1.00 47.59  ? 17  SER E N   1 
ATOM 4330 C CA  . SER D 2 17  ? 176.263 197.788 243.286 1.00 48.40  ? 17  SER E CA  1 
ATOM 4331 C C   . SER D 2 17  ? 177.759 197.601 243.084 1.00 48.66  ? 17  SER E C   1 
ATOM 4332 O O   . SER D 2 17  ? 178.561 198.462 243.454 1.00 52.75  ? 17  SER E O   1 
ATOM 4333 C CB  . SER D 2 17  ? 175.636 198.392 242.024 1.00 50.18  ? 17  SER E CB  1 
ATOM 4334 O OG  . SER D 2 17  ? 176.188 199.666 241.742 1.00 52.05  ? 17  SER E OG  1 
ATOM 4335 N N   . LEU D 2 18  ? 178.124 196.464 242.490 1.00 46.72  ? 18  LEU E N   1 
ATOM 4336 C CA  . LEU D 2 18  ? 179.495 196.206 242.070 1.00 46.68  ? 18  LEU E CA  1 
ATOM 4337 C C   . LEU D 2 18  ? 179.493 195.456 240.747 1.00 46.68  ? 18  LEU E C   1 
ATOM 4338 O O   . LEU D 2 18  ? 178.509 194.817 240.369 1.00 49.51  ? 18  LEU E O   1 
ATOM 4339 C CB  . LEU D 2 18  ? 180.294 195.392 243.093 1.00 46.45  ? 18  LEU E CB  1 
ATOM 4340 C CG  . LEU D 2 18  ? 180.599 195.962 244.472 1.00 52.77  ? 18  LEU E CG  1 
ATOM 4341 C CD1 . LEU D 2 18  ? 180.624 194.825 245.460 1.00 55.01  ? 18  LEU E CD1 1 
ATOM 4342 C CD2 . LEU D 2 18  ? 181.924 196.704 244.467 1.00 52.35  ? 18  LEU E CD2 1 
ATOM 4343 N N   . ARG D 2 19  ? 180.624 195.535 240.051 1.00 44.44  ? 19  ARG E N   1 
ATOM 4344 C CA  . ARG D 2 19  ? 180.850 194.820 238.800 1.00 44.64  ? 19  ARG E CA  1 
ATOM 4345 C C   . ARG D 2 19  ? 182.103 193.969 238.954 1.00 47.50  ? 19  ARG E C   1 
ATOM 4346 O O   . ARG D 2 19  ? 183.219 194.499 238.969 1.00 49.49  ? 19  ARG E O   1 
ATOM 4347 C CB  . ARG D 2 19  ? 180.989 195.793 237.632 1.00 50.23  ? 19  ARG E CB  1 
ATOM 4348 C CG  . ARG D 2 19  ? 180.434 195.277 236.316 1.00 53.47  ? 19  ARG E CG  1 
ATOM 4349 C CD  . ARG D 2 19  ? 180.181 196.421 235.351 1.00 59.54  ? 19  ARG E CD  1 
ATOM 4350 N NE  . ARG D 2 19  ? 181.405 197.150 235.043 1.00 66.59  ? 19  ARG E NE  1 
ATOM 4351 C CZ  . ARG D 2 19  ? 182.115 196.990 233.936 1.00 63.16  ? 19  ARG E CZ  1 
ATOM 4352 N NH1 . ARG D 2 19  ? 181.748 196.133 232.998 1.00 61.46  ? 19  ARG E NH1 1 
ATOM 4353 N NH2 . ARG D 2 19  ? 183.222 197.707 233.765 1.00 60.15  ? 19  ARG E NH2 1 
ATOM 4354 N N   . LEU D 2 20  ? 181.921 192.658 239.070 1.00 48.97  ? 20  LEU E N   1 
ATOM 4355 C CA  . LEU D 2 20  ? 183.039 191.730 239.142 1.00 48.14  ? 20  LEU E CA  1 
ATOM 4356 C C   . LEU D 2 20  ? 183.483 191.346 237.738 1.00 52.23  ? 20  LEU E C   1 
ATOM 4357 O O   . LEU D 2 20  ? 182.655 191.156 236.843 1.00 53.17  ? 20  LEU E O   1 
ATOM 4358 C CB  . LEU D 2 20  ? 182.655 190.477 239.931 1.00 45.32  ? 20  LEU E CB  1 
ATOM 4359 C CG  . LEU D 2 20  ? 182.413 190.627 241.434 1.00 52.98  ? 20  LEU E CG  1 
ATOM 4360 C CD1 . LEU D 2 20  ? 182.487 189.275 242.115 1.00 56.16  ? 20  LEU E CD1 1 
ATOM 4361 C CD2 . LEU D 2 20  ? 183.409 191.593 242.056 1.00 56.34  ? 20  LEU E CD2 1 
ATOM 4362 N N   . SER D 2 21  ? 184.795 191.232 237.550 1.00 49.75  ? 21  SER E N   1 
ATOM 4363 C CA  . SER D 2 21  ? 185.376 190.917 236.253 1.00 50.38  ? 21  SER E CA  1 
ATOM 4364 C C   . SER D 2 21  ? 186.291 189.710 236.385 1.00 54.90  ? 21  SER E C   1 
ATOM 4365 O O   . SER D 2 21  ? 186.958 189.541 237.408 1.00 58.38  ? 21  SER E O   1 
ATOM 4366 C CB  . SER D 2 21  ? 186.161 192.107 235.694 1.00 51.45  ? 21  SER E CB  1 
ATOM 4367 O OG  . SER D 2 21  ? 187.156 192.532 236.608 1.00 56.81  ? 21  SER E OG  1 
ATOM 4368 N N   . CYS D 2 22  ? 186.315 188.872 235.350 1.00 53.00  ? 22  CYS E N   1 
ATOM 4369 C CA  . CYS D 2 22  ? 187.173 187.693 235.302 1.00 51.40  ? 22  CYS E CA  1 
ATOM 4370 C C   . CYS D 2 22  ? 187.823 187.624 233.927 1.00 54.73  ? 22  CYS E C   1 
ATOM 4371 O O   . CYS D 2 22  ? 187.131 187.436 232.921 1.00 58.34  ? 22  CYS E O   1 
ATOM 4372 C CB  . CYS D 2 22  ? 186.373 186.420 235.600 1.00 51.78  ? 22  CYS E CB  1 
ATOM 4373 S SG  . CYS D 2 22  ? 187.278 184.871 235.384 1.00 75.54  ? 22  CYS E SG  1 
ATOM 4374 N N   . THR D 2 23  ? 189.147 187.766 233.886 1.00 57.88  ? 23  THR E N   1 
ATOM 4375 C CA  . THR D 2 23  ? 189.904 187.893 232.645 1.00 60.50  ? 23  THR E CA  1 
ATOM 4376 C C   . THR D 2 23  ? 190.794 186.669 232.467 1.00 61.82  ? 23  THR E C   1 
ATOM 4377 O O   . THR D 2 23  ? 191.450 186.234 233.420 1.00 65.32  ? 23  THR E O   1 
ATOM 4378 C CB  . THR D 2 23  ? 190.751 189.174 232.657 1.00 68.10  ? 23  THR E CB  1 
ATOM 4379 O OG1 . THR D 2 23  ? 189.897 190.312 232.814 1.00 75.50  ? 23  THR E OG1 1 
ATOM 4380 C CG2 . THR D 2 23  ? 191.536 189.330 231.361 1.00 64.94  ? 23  THR E CG2 1 
ATOM 4381 N N   . ALA D 2 24  ? 190.817 186.118 231.253 1.00 57.06  ? 24  ALA E N   1 
ATOM 4382 C CA  . ALA D 2 24  ? 191.576 184.914 230.952 1.00 52.10  ? 24  ALA E CA  1 
ATOM 4383 C C   . ALA D 2 24  ? 192.919 185.261 230.315 1.00 53.93  ? 24  ALA E C   1 
ATOM 4384 O O   . ALA D 2 24  ? 193.233 186.421 230.042 1.00 64.69  ? 24  ALA E O   1 
ATOM 4385 C CB  . ALA D 2 24  ? 190.777 183.990 230.037 1.00 50.51  ? 24  ALA E CB  1 
ATOM 4386 N N   . SER D 2 25  ? 193.721 184.223 230.073 1.00 53.90  ? 25  SER E N   1 
ATOM 4387 C CA  . SER D 2 25  ? 195.068 184.402 229.547 1.00 62.49  ? 25  SER E CA  1 
ATOM 4388 C C   . SER D 2 25  ? 195.357 183.483 228.366 1.00 65.69  ? 25  SER E C   1 
ATOM 4389 O O   . SER D 2 25  ? 196.233 183.781 227.549 1.00 69.00  ? 25  SER E O   1 
ATOM 4390 C CB  . SER D 2 25  ? 196.099 184.167 230.653 1.00 68.95  ? 25  SER E CB  1 
ATOM 4391 O OG  . SER D 2 25  ? 195.974 185.133 231.682 1.00 67.34  ? 25  SER E OG  1 
ATOM 4392 N N   . GLY D 2 26  ? 194.652 182.359 228.271 1.00 60.99  ? 26  GLY E N   1 
ATOM 4393 C CA  . GLY D 2 26  ? 194.964 181.395 227.234 1.00 52.75  ? 26  GLY E CA  1 
ATOM 4394 C C   . GLY D 2 26  ? 193.781 180.837 226.470 1.00 46.65  ? 26  GLY E C   1 
ATOM 4395 O O   . GLY D 2 26  ? 193.965 180.155 225.458 1.00 50.23  ? 26  GLY E O   1 
ATOM 4396 N N   . ILE D 2 27  ? 192.566 181.114 226.931 1.00 42.03  ? 27  ILE E N   1 
ATOM 4397 C CA  . ILE D 2 27  ? 191.366 180.551 226.329 1.00 36.86  ? 27  ILE E CA  1 
ATOM 4398 C C   . ILE D 2 27  ? 190.437 181.681 225.915 1.00 47.48  ? 27  ILE E C   1 
ATOM 4399 O O   . ILE D 2 27  ? 190.483 182.786 226.465 1.00 59.24  ? 27  ILE E O   1 
ATOM 4400 C CB  . ILE D 2 27  ? 190.642 179.582 227.288 1.00 38.74  ? 27  ILE E CB  1 
ATOM 4401 C CG1 . ILE D 2 27  ? 190.432 180.238 228.651 1.00 46.32  ? 27  ILE E CG1 1 
ATOM 4402 C CG2 . ILE D 2 27  ? 191.430 178.296 227.441 1.00 44.45  ? 27  ILE E CG2 1 
ATOM 4403 C CD1 . ILE D 2 27  ? 189.515 179.460 229.567 1.00 49.24  ? 27  ILE E CD1 1 
ATOM 4404 N N   . ALA D 2 28  ? 189.576 181.395 224.942 1.00 46.76  ? 28  ALA E N   1 
ATOM 4405 C CA  . ALA D 2 28  ? 188.578 182.405 224.529 1.00 49.03  ? 28  ALA E CA  1 
ATOM 4406 C C   . ALA D 2 28  ? 187.265 182.084 225.235 1.00 48.01  ? 28  ALA E C   1 
ATOM 4407 O O   . ALA D 2 28  ? 186.720 180.989 225.012 1.00 53.48  ? 28  ALA E O   1 
ATOM 4408 C CB  . ALA D 2 28  ? 188.419 182.373 223.035 1.00 51.33  ? 28  ALA E CB  1 
ATOM 4409 N N   . LEU D 2 29  ? 186.786 182.991 226.083 1.00 42.41  ? 29  LEU E N   1 
ATOM 4410 C CA  . LEU D 2 29  ? 185.568 182.672 226.870 1.00 46.13  ? 29  LEU E CA  1 
ATOM 4411 C C   . LEU D 2 29  ? 184.342 182.686 225.945 1.00 51.98  ? 29  LEU E C   1 
ATOM 4412 O O   . LEU D 2 29  ? 183.214 182.591 226.468 1.00 56.31  ? 29  LEU E O   1 
ATOM 4413 C CB  . LEU D 2 29  ? 185.401 183.641 228.038 1.00 47.01  ? 29  LEU E CB  1 
ATOM 4414 C CG  . LEU D 2 29  ? 186.376 183.474 229.206 1.00 38.27  ? 29  LEU E CG  1 
ATOM 4415 C CD1 . LEU D 2 29  ? 186.713 182.015 229.443 1.00 42.42  ? 29  LEU E CD1 1 
ATOM 4416 C CD2 . LEU D 2 29  ? 187.626 184.294 228.984 1.00 34.43  ? 29  LEU E CD2 1 
ATOM 4417 N N   . HIS D 2 30  ? 184.547 182.789 224.630 1.00 51.01  ? 30  HIS E N   1 
ATOM 4418 C CA  . HIS D 2 30  ? 183.386 182.715 223.701 1.00 54.20  ? 30  HIS E CA  1 
ATOM 4419 C C   . HIS D 2 30  ? 183.286 181.301 223.123 1.00 54.42  ? 30  HIS E C   1 
ATOM 4420 O O   . HIS D 2 30  ? 182.352 181.037 222.341 1.00 58.93  ? 30  HIS E O   1 
ATOM 4421 C CB  . HIS D 2 30  ? 183.472 183.786 222.608 1.00 58.51  ? 30  HIS E CB  1 
ATOM 4422 C CG  . HIS D 2 30  ? 184.664 183.688 221.719 1.00 66.96  ? 30  HIS E CG  1 
ATOM 4423 N ND1 . HIS D 2 30  ? 184.693 182.898 220.591 1.00 69.58  ? 30  HIS E ND1 1 
ATOM 4424 C CD2 . HIS D 2 30  ? 185.860 184.284 221.785 1.00 64.73  ? 30  HIS E CD2 1 
ATOM 4425 C CE1 . HIS D 2 30  ? 185.874 183.017 220.004 1.00 67.41  ? 30  HIS E CE1 1 
ATOM 4426 N NE2 . HIS D 2 30  ? 186.598 183.857 220.711 1.00 68.95  ? 30  HIS E NE2 1 
ATOM 4427 N N   . THR D 2 31  ? 184.224 180.425 223.486 1.00 50.80  ? 31  THR E N   1 
ATOM 4428 C CA  . THR D 2 31  ? 184.155 179.021 223.029 1.00 49.09  ? 31  THR E CA  1 
ATOM 4429 C C   . THR D 2 31  ? 184.088 178.129 224.245 1.00 46.78  ? 31  THR E C   1 
ATOM 4430 O O   . THR D 2 31  ? 183.820 176.925 224.077 1.00 48.09  ? 31  THR E O   1 
ATOM 4431 C CB  . THR D 2 31  ? 185.354 178.688 222.146 1.00 51.68  ? 31  THR E CB  1 
ATOM 4432 O OG1 . THR D 2 31  ? 185.125 177.348 221.725 1.00 49.72  ? 31  THR E OG1 1 
ATOM 4433 C CG2 . THR D 2 31  ? 186.676 178.765 222.887 1.00 55.73  ? 31  THR E CG2 1 
ATOM 4434 N N   . HIS D 2 32  ? 184.326 178.694 225.428 1.00 45.16  ? 32  HIS E N   1 
ATOM 4435 C CA  . HIS D 2 32  ? 184.211 177.912 226.685 1.00 42.39  ? 32  HIS E CA  1 
ATOM 4436 C C   . HIS D 2 32  ? 182.916 178.329 227.386 1.00 47.07  ? 32  HIS E C   1 
ATOM 4437 O O   . HIS D 2 32  ? 182.216 179.217 226.861 1.00 51.70  ? 32  HIS E O   1 
ATOM 4438 C CB  . HIS D 2 32  ? 185.449 178.129 227.559 1.00 38.70  ? 32  HIS E CB  1 
ATOM 4439 C CG  . HIS D 2 32  ? 186.651 177.368 227.120 1.00 38.30  ? 32  HIS E CG  1 
ATOM 4440 N ND1 . HIS D 2 32  ? 187.526 177.837 226.166 1.00 44.18  ? 32  HIS E ND1 1 
ATOM 4441 C CD2 . HIS D 2 32  ? 187.118 176.173 227.496 1.00 40.53  ? 32  HIS E CD2 1 
ATOM 4442 C CE1 . HIS D 2 32  ? 188.488 176.946 225.982 1.00 47.76  ? 32  HIS E CE1 1 
ATOM 4443 N NE2 . HIS D 2 32  ? 188.261 175.928 226.782 1.00 43.04  ? 32  HIS E NE2 1 
ATOM 4444 N N   . ALA D 2 33  ? 182.601 177.710 228.526 1.00 40.69  ? 33  ALA E N   1 
ATOM 4445 C CA  . ALA D 2 33  ? 181.398 178.094 229.298 1.00 39.47  ? 33  ALA E CA  1 
ATOM 4446 C C   . ALA D 2 33  ? 181.835 178.643 230.652 1.00 39.89  ? 33  ALA E C   1 
ATOM 4447 O O   . ALA D 2 33  ? 182.518 177.905 231.386 1.00 45.90  ? 33  ALA E O   1 
ATOM 4448 C CB  . ALA D 2 33  ? 180.505 176.899 229.463 1.00 42.70  ? 33  ALA E CB  1 
ATOM 4449 N N   . THR D 2 34  ? 181.453 179.879 230.980 1.00 34.81  ? 34  THR E N   1 
ATOM 4450 C CA  . THR D 2 34  ? 181.942 180.503 232.229 1.00 33.74  ? 34  THR E CA  1 
ATOM 4451 C C   . THR D 2 34  ? 180.873 180.474 233.294 1.00 36.58  ? 34  THR E C   1 
ATOM 4452 O O   . THR D 2 34  ? 179.695 180.261 232.945 1.00 43.49  ? 34  THR E O   1 
ATOM 4453 C CB  . THR D 2 34  ? 182.386 181.930 231.927 1.00 40.11  ? 34  THR E CB  1 
ATOM 4454 O OG1 . THR D 2 34  ? 182.641 182.513 233.200 1.00 44.91  ? 34  THR E OG1 1 
ATOM 4455 C CG2 . THR D 2 34  ? 181.318 182.725 231.199 1.00 47.39  ? 34  THR E CG2 1 
ATOM 4456 N N   . GLY D 2 35  ? 181.263 180.686 234.553 1.00 35.91  ? 35  GLY E N   1 
ATOM 4457 C CA  . GLY D 2 35  ? 180.316 180.702 235.652 1.00 39.62  ? 35  GLY E CA  1 
ATOM 4458 C C   . GLY D 2 35  ? 180.897 181.375 236.874 1.00 43.18  ? 35  GLY E C   1 
ATOM 4459 O O   . GLY D 2 35  ? 182.076 181.733 236.917 1.00 45.54  ? 35  GLY E O   1 
ATOM 4460 N N   . TRP D 2 36  ? 180.039 181.547 237.879 1.00 41.94  ? 36  TRP E N   1 
ATOM 4461 C CA  . TRP D 2 36  ? 180.424 182.137 239.153 1.00 38.92  ? 36  TRP E CA  1 
ATOM 4462 C C   . TRP D 2 36  ? 179.900 181.286 240.300 1.00 44.08  ? 36  TRP E C   1 
ATOM 4463 O O   . TRP D 2 36  ? 178.794 180.743 240.230 1.00 51.85  ? 36  TRP E O   1 
ATOM 4464 C CB  . TRP D 2 36  ? 179.902 183.567 239.285 1.00 36.80  ? 36  TRP E CB  1 
ATOM 4465 C CG  . TRP D 2 36  ? 180.607 184.548 238.407 1.00 36.55  ? 36  TRP E CG  1 
ATOM 4466 C CD1 . TRP D 2 36  ? 180.282 184.880 237.132 1.00 37.41  ? 36  TRP E CD1 1 
ATOM 4467 C CD2 . TRP D 2 36  ? 181.748 185.342 238.750 1.00 35.99  ? 36  TRP E CD2 1 
ATOM 4468 N NE1 . TRP D 2 36  ? 181.150 185.826 236.650 1.00 36.35  ? 36  TRP E NE1 1 
ATOM 4469 C CE2 . TRP D 2 36  ? 182.061 186.126 237.626 1.00 33.42  ? 36  TRP E CE2 1 
ATOM 4470 C CE3 . TRP D 2 36  ? 182.536 185.462 239.896 1.00 41.90  ? 36  TRP E CE3 1 
ATOM 4471 C CZ2 . TRP D 2 36  ? 183.129 187.016 237.612 1.00 38.33  ? 36  TRP E CZ2 1 
ATOM 4472 C CZ3 . TRP D 2 36  ? 183.594 186.347 239.882 1.00 46.72  ? 36  TRP E CZ3 1 
ATOM 4473 C CH2 . TRP D 2 36  ? 183.882 187.112 238.748 1.00 47.46  ? 36  TRP E CH2 1 
ATOM 4474 N N   . PHE D 2 37  ? 180.705 181.174 241.356 1.00 44.31  ? 37  PHE E N   1 
ATOM 4475 C CA  . PHE D 2 37  ? 180.364 180.397 242.538 1.00 48.51  ? 37  PHE E CA  1 
ATOM 4476 C C   . PHE D 2 37  ? 180.810 181.191 243.758 1.00 52.90  ? 37  PHE E C   1 
ATOM 4477 O O   . PHE D 2 37  ? 181.712 182.026 243.661 1.00 57.59  ? 37  PHE E O   1 
ATOM 4478 C CB  . PHE D 2 37  ? 181.037 179.013 242.526 1.00 49.56  ? 37  PHE E CB  1 
ATOM 4479 C CG  . PHE D 2 37  ? 180.841 178.248 241.242 1.00 46.21  ? 37  PHE E CG  1 
ATOM 4480 C CD1 . PHE D 2 37  ? 179.745 177.425 241.064 1.00 44.51  ? 37  PHE E CD1 1 
ATOM 4481 C CD2 . PHE D 2 37  ? 181.749 178.376 240.203 1.00 47.05  ? 37  PHE E CD2 1 
ATOM 4482 C CE1 . PHE D 2 37  ? 179.564 176.740 239.878 1.00 45.11  ? 37  PHE E CE1 1 
ATOM 4483 C CE2 . PHE D 2 37  ? 181.575 177.688 239.022 1.00 46.25  ? 37  PHE E CE2 1 
ATOM 4484 C CZ  . PHE D 2 37  ? 180.482 176.869 238.860 1.00 43.67  ? 37  PHE E CZ  1 
ATOM 4485 N N   . ARG D 2 38  ? 180.185 180.939 244.910 1.00 46.66  ? 38  ARG E N   1 
ATOM 4486 C CA  . ARG D 2 38  ? 180.487 181.759 246.075 1.00 44.28  ? 38  ARG E CA  1 
ATOM 4487 C C   . ARG D 2 38  ? 180.614 180.930 247.348 1.00 50.05  ? 38  ARG E C   1 
ATOM 4488 O O   . ARG D 2 38  ? 180.055 179.838 247.467 1.00 57.38  ? 38  ARG E O   1 
ATOM 4489 C CB  . ARG D 2 38  ? 179.446 182.875 246.264 1.00 44.35  ? 38  ARG E CB  1 
ATOM 4490 C CG  . ARG D 2 38  ? 178.178 182.502 247.001 1.00 47.50  ? 38  ARG E CG  1 
ATOM 4491 C CD  . ARG D 2 38  ? 177.376 183.764 247.290 1.00 51.68  ? 38  ARG E CD  1 
ATOM 4492 N NE  . ARG D 2 38  ? 175.938 183.532 247.347 1.00 52.67  ? 38  ARG E NE  1 
ATOM 4493 C CZ  . ARG D 2 38  ? 175.026 184.433 247.008 1.00 50.49  ? 38  ARG E CZ  1 
ATOM 4494 N NH1 . ARG D 2 38  ? 175.370 185.638 246.585 1.00 52.74  ? 38  ARG E NH1 1 
ATOM 4495 N NH2 . ARG D 2 38  ? 173.738 184.119 247.100 1.00 46.87  ? 38  ARG E NH2 1 
ATOM 4496 N N   . GLN D 2 39  ? 181.375 181.483 248.296 1.00 48.90  ? 39  GLN E N   1 
ATOM 4497 C CA  . GLN D 2 39  ? 181.679 180.879 249.597 1.00 48.12  ? 39  GLN E CA  1 
ATOM 4498 C C   . GLN D 2 39  ? 181.403 181.869 250.722 1.00 49.07  ? 39  GLN E C   1 
ATOM 4499 O O   . GLN D 2 39  ? 182.232 182.736 251.008 1.00 51.43  ? 39  GLN E O   1 
ATOM 4500 C CB  . GLN D 2 39  ? 183.132 180.412 249.665 1.00 49.52  ? 39  GLN E CB  1 
ATOM 4501 C CG  . GLN D 2 39  ? 183.432 179.335 250.713 1.00 52.98  ? 39  GLN E CG  1 
ATOM 4502 C CD  . GLN D 2 39  ? 183.144 177.923 250.271 1.00 57.13  ? 39  GLN E CD  1 
ATOM 4503 O OE1 . GLN D 2 39  ? 182.256 177.683 249.467 1.00 54.59  ? 39  GLN E OE1 1 
ATOM 4504 N NE2 . GLN D 2 39  ? 183.900 176.973 250.806 1.00 59.75  ? 39  GLN E NE2 1 
ATOM 4505 N N   . ALA D 2 40  ? 180.255 181.735 251.359 1.00 51.51  ? 40  ALA E N   1 
ATOM 4506 C CA  . ALA D 2 40  ? 180.093 182.364 252.656 1.00 54.86  ? 40  ALA E CA  1 
ATOM 4507 C C   . ALA D 2 40  ? 180.809 181.526 253.713 1.00 62.36  ? 40  ALA E C   1 
ATOM 4508 O O   . ALA D 2 40  ? 180.945 180.310 253.554 1.00 65.88  ? 40  ALA E O   1 
ATOM 4509 C CB  . ALA D 2 40  ? 178.615 182.501 253.005 1.00 55.73  ? 40  ALA E CB  1 
ATOM 4510 N N   . PRO D 2 41  ? 181.310 182.153 254.780 1.00 64.60  ? 41  PRO E N   1 
ATOM 4511 C CA  . PRO D 2 41  ? 181.987 181.381 255.832 1.00 64.59  ? 41  PRO E CA  1 
ATOM 4512 C C   . PRO D 2 41  ? 181.036 180.431 256.545 1.00 63.06  ? 41  PRO E C   1 
ATOM 4513 O O   . PRO D 2 41  ? 179.902 180.785 256.874 1.00 67.54  ? 41  PRO E O   1 
ATOM 4514 C CB  . PRO D 2 41  ? 182.512 182.462 256.783 1.00 62.80  ? 41  PRO E CB  1 
ATOM 4515 C CG  . PRO D 2 41  ? 182.638 183.677 255.932 1.00 62.96  ? 41  PRO E CG  1 
ATOM 4516 C CD  . PRO D 2 41  ? 181.496 183.602 254.962 1.00 62.53  ? 41  PRO E CD  1 
ATOM 4517 N N   . GLY D 2 42  ? 181.516 179.212 256.781 1.00 57.15  ? 42  GLY E N   1 
ATOM 4518 C CA  . GLY D 2 42  ? 180.716 178.200 257.438 1.00 56.93  ? 42  GLY E CA  1 
ATOM 4519 C C   . GLY D 2 42  ? 179.698 177.510 256.561 1.00 66.15  ? 42  GLY E C   1 
ATOM 4520 O O   . GLY D 2 42  ? 178.792 176.855 257.085 1.00 70.71  ? 42  GLY E O   1 
ATOM 4521 N N   . LYS D 2 43  ? 179.811 177.635 255.238 1.00 67.33  ? 43  LYS E N   1 
ATOM 4522 C CA  . LYS D 2 43  ? 178.852 177.017 254.330 1.00 66.38  ? 43  LYS E CA  1 
ATOM 4523 C C   . LYS D 2 43  ? 179.548 176.211 253.240 1.00 67.55  ? 43  LYS E C   1 
ATOM 4524 O O   . LYS D 2 43  ? 180.765 176.007 253.287 1.00 66.96  ? 43  LYS E O   1 
ATOM 4525 C CB  . LYS D 2 43  ? 177.950 178.080 253.697 1.00 61.66  ? 43  LYS E CB  1 
ATOM 4526 C CG  . LYS D 2 43  ? 177.056 178.816 254.683 1.00 60.19  ? 43  LYS E CG  1 
ATOM 4527 C CD  . LYS D 2 43  ? 176.190 179.852 253.986 1.00 60.66  ? 43  LYS E CD  1 
ATOM 4528 C CE  . LYS D 2 43  ? 175.340 179.225 252.893 1.00 61.65  ? 43  LYS E CE  1 
ATOM 4529 N NZ  . LYS D 2 43  ? 174.360 178.248 253.439 1.00 61.63  ? 43  LYS E NZ  1 
ATOM 4530 N N   . GLU D 2 44  ? 178.778 175.746 252.260 1.00 67.60  ? 44  GLU E N   1 
ATOM 4531 C CA  . GLU D 2 44  ? 179.290 175.018 251.109 1.00 67.54  ? 44  GLU E CA  1 
ATOM 4532 C C   . GLU D 2 44  ? 178.981 175.803 249.839 1.00 69.97  ? 44  GLU E C   1 
ATOM 4533 O O   . GLU D 2 44  ? 178.009 176.561 249.776 1.00 72.49  ? 44  GLU E O   1 
ATOM 4534 C CB  . GLU D 2 44  ? 178.707 173.592 251.062 1.00 67.29  ? 44  GLU E CB  1 
ATOM 4535 C CG  . GLU D 2 44  ? 177.183 173.488 250.942 1.00 76.15  ? 44  GLU E CG  1 
ATOM 4536 C CD  . GLU D 2 44  ? 176.683 173.528 249.511 1.00 80.59  ? 44  GLU E CD  1 
ATOM 4537 O OE1 . GLU D 2 44  ? 177.487 173.257 248.595 1.00 82.52  ? 44  GLU E OE1 1 
ATOM 4538 O OE2 . GLU D 2 44  ? 175.489 173.830 249.303 1.00 78.27  ? 44  GLU E OE2 1 
ATOM 4539 N N   . ARG D 2 45  ? 179.826 175.621 248.824 1.00 63.00  ? 45  ARG E N   1 
ATOM 4540 C CA  . ARG D 2 45  ? 179.805 176.493 247.655 1.00 59.32  ? 45  ARG E CA  1 
ATOM 4541 C C   . ARG D 2 45  ? 178.587 176.245 246.773 1.00 66.34  ? 45  ARG E C   1 
ATOM 4542 O O   . ARG D 2 45  ? 178.186 175.103 246.532 1.00 72.86  ? 45  ARG E O   1 
ATOM 4543 C CB  . ARG D 2 45  ? 181.101 176.346 246.850 1.00 58.21  ? 45  ARG E CB  1 
ATOM 4544 C CG  . ARG D 2 45  ? 181.387 174.994 246.233 1.00 68.48  ? 45  ARG E CG  1 
ATOM 4545 C CD  . ARG D 2 45  ? 182.223 175.173 244.975 1.00 72.69  ? 45  ARG E CD  1 
ATOM 4546 N NE  . ARG D 2 45  ? 183.384 176.022 245.212 1.00 74.05  ? 45  ARG E NE  1 
ATOM 4547 C CZ  . ARG D 2 45  ? 184.270 176.358 244.285 1.00 64.10  ? 45  ARG E CZ  1 
ATOM 4548 N NH1 . ARG D 2 45  ? 184.158 175.936 243.036 1.00 59.42  ? 45  ARG E NH1 1 
ATOM 4549 N NH2 . ARG D 2 45  ? 185.292 177.141 244.618 1.00 61.29  ? 45  ARG E NH2 1 
ATOM 4550 N N   . GLU D 2 46  ? 177.994 177.341 246.305 1.00 58.67  ? 46  GLU E N   1 
ATOM 4551 C CA  . GLU D 2 46  ? 176.771 177.317 245.522 1.00 55.17  ? 46  GLU E CA  1 
ATOM 4552 C C   . GLU D 2 46  ? 176.937 178.274 244.350 1.00 53.32  ? 46  GLU E C   1 
ATOM 4553 O O   . GLU D 2 46  ? 177.571 179.325 244.478 1.00 53.34  ? 46  GLU E O   1 
ATOM 4554 C CB  . GLU D 2 46  ? 175.559 177.698 246.400 1.00 58.54  ? 46  GLU E CB  1 
ATOM 4555 C CG  . GLU D 2 46  ? 174.257 178.030 245.671 1.00 64.81  ? 46  GLU E CG  1 
ATOM 4556 C CD  . GLU D 2 46  ? 173.577 176.813 245.064 1.00 71.73  ? 46  GLU E CD  1 
ATOM 4557 O OE1 . GLU D 2 46  ? 173.961 175.671 245.398 1.00 72.99  ? 46  GLU E OE1 1 
ATOM 4558 O OE2 . GLU D 2 46  ? 172.650 177.000 244.248 1.00 72.43  ? 46  GLU E OE2 1 
ATOM 4559 N N   . GLY D 2 47  ? 176.372 177.899 243.205 1.00 54.08  ? 47  GLY E N   1 
ATOM 4560 C CA  . GLY D 2 47  ? 176.545 178.672 241.993 1.00 49.72  ? 47  GLY E CA  1 
ATOM 4561 C C   . GLY D 2 47  ? 175.832 180.011 242.031 1.00 44.19  ? 47  GLY E C   1 
ATOM 4562 O O   . GLY D 2 47  ? 175.013 180.304 242.902 1.00 48.92  ? 47  GLY E O   1 
ATOM 4563 N N   . VAL D 2 48  ? 176.178 180.852 241.058 1.00 37.86  ? 48  VAL E N   1 
ATOM 4564 C CA  . VAL D 2 48  ? 175.594 182.183 240.941 1.00 38.45  ? 48  VAL E CA  1 
ATOM 4565 C C   . VAL D 2 48  ? 174.986 182.361 239.556 1.00 42.08  ? 48  VAL E C   1 
ATOM 4566 O O   . VAL D 2 48  ? 173.797 182.674 239.429 1.00 46.02  ? 48  VAL E O   1 
ATOM 4567 C CB  . VAL D 2 48  ? 176.638 183.278 241.230 1.00 42.70  ? 48  VAL E CB  1 
ATOM 4568 C CG1 . VAL D 2 48  ? 176.078 184.650 240.889 1.00 46.24  ? 48  VAL E CG1 1 
ATOM 4569 C CG2 . VAL D 2 48  ? 177.071 183.230 242.683 1.00 43.20  ? 48  VAL E CG2 1 
ATOM 4570 N N   . SER D 2 49  ? 175.784 182.153 238.510 1.00 41.23  ? 49  SER E N   1 
ATOM 4571 C CA  . SER D 2 49  ? 175.324 182.385 237.146 1.00 43.01  ? 49  SER E CA  1 
ATOM 4572 C C   . SER D 2 49  ? 176.181 181.581 236.176 1.00 44.83  ? 49  SER E C   1 
ATOM 4573 O O   . SER D 2 49  ? 177.194 180.989 236.554 1.00 49.08  ? 49  SER E O   1 
ATOM 4574 C CB  . SER D 2 49  ? 175.358 183.876 236.796 1.00 44.74  ? 49  SER E CB  1 
ATOM 4575 O OG  . SER D 2 49  ? 176.560 184.476 237.246 1.00 45.74  ? 49  SER E OG  1 
ATOM 4576 N N   . CYS D 2 50  ? 175.749 181.562 234.913 1.00 40.74  ? 50  CYS E N   1 
ATOM 4577 C CA  . CYS D 2 50  ? 176.472 180.897 233.836 1.00 38.44  ? 50  CYS E CA  1 
ATOM 4578 C C   . CYS D 2 50  ? 176.170 181.565 232.503 1.00 46.72  ? 50  CYS E C   1 
ATOM 4579 O O   . CYS D 2 50  ? 175.139 182.220 232.329 1.00 58.33  ? 50  CYS E O   1 
ATOM 4580 C CB  . CYS D 2 50  ? 176.129 179.406 233.730 1.00 43.95  ? 50  CYS E CB  1 
ATOM 4581 S SG  . CYS D 2 50  ? 177.053 178.574 232.402 1.00 68.74  ? 50  CYS E SG  1 
ATOM 4582 N N   . ILE D 2 51  ? 177.098 181.391 231.563 1.00 42.95  ? 51  ILE E N   1 
ATOM 4583 C CA  . ILE D 2 51  ? 176.888 181.685 230.150 1.00 40.95  ? 51  ILE E CA  1 
ATOM 4584 C C   . ILE D 2 51  ? 177.364 180.472 229.361 1.00 49.45  ? 51  ILE E C   1 
ATOM 4585 O O   . ILE D 2 51  ? 178.415 179.901 229.670 1.00 57.48  ? 51  ILE E O   1 
ATOM 4586 C CB  . ILE D 2 51  ? 177.641 182.954 229.687 1.00 37.98  ? 51  ILE E CB  1 
ATOM 4587 C CG1 . ILE D 2 51  ? 177.157 184.202 230.411 1.00 46.34  ? 51  ILE E CG1 1 
ATOM 4588 C CG2 . ILE D 2 51  ? 177.427 183.209 228.209 1.00 47.64  ? 51  ILE E CG2 1 
ATOM 4589 C CD1 . ILE D 2 51  ? 178.046 185.399 230.144 1.00 42.77  ? 51  ILE E CD1 1 
ATOM 4590 N N   . SER D 2 52  ? 176.596 180.074 228.348 1.00 51.03  ? 52  SER E N   1 
ATOM 4591 C CA  . SER D 2 52  ? 176.988 178.971 227.479 1.00 50.55  ? 52  SER E CA  1 
ATOM 4592 C C   . SER D 2 52  ? 178.031 179.453 226.466 1.00 50.36  ? 52  SER E C   1 
ATOM 4593 O O   . SER D 2 52  ? 178.578 180.554 226.570 1.00 53.61  ? 52  SER E O   1 
ATOM 4594 C CB  . SER D 2 52  ? 175.761 178.371 226.800 1.00 58.10  ? 52  SER E CB  1 
ATOM 4595 O OG  . SER D 2 52  ? 174.914 179.382 226.284 1.00 65.52  ? 52  SER E OG  1 
ATOM 4596 N N   . SER D 2 53  ? 178.320 178.624 225.461 1.00 49.75  ? 53  SER E N   1 
ATOM 4597 C CA  . SER D 2 53  ? 179.453 178.893 224.574 1.00 55.76  ? 53  SER E CA  1 
ATOM 4598 C C   . SER D 2 53  ? 179.123 179.953 223.527 1.00 58.32  ? 53  SER E C   1 
ATOM 4599 O O   . SER D 2 53  ? 179.705 181.042 223.525 1.00 58.04  ? 53  SER E O   1 
ATOM 4600 C CB  . SER D 2 53  ? 179.900 177.590 223.904 1.00 57.35  ? 53  SER E CB  1 
ATOM 4601 O OG  . SER D 2 53  ? 180.976 177.816 223.012 1.00 62.58  ? 53  SER E OG  1 
ATOM 4602 N N   . GLY D 2 54  ? 178.177 179.659 222.642 1.00 65.09  ? 54  GLY E N   1 
ATOM 4603 C CA  . GLY D 2 54  ? 177.803 180.573 221.574 1.00 72.19  ? 54  GLY E CA  1 
ATOM 4604 C C   . GLY D 2 54  ? 176.584 181.383 221.977 1.00 80.88  ? 54  GLY E C   1 
ATOM 4605 O O   . GLY D 2 54  ? 175.669 180.862 222.618 1.00 84.43  ? 54  GLY E O   1 
ATOM 4606 N N   . ASP D 2 55  ? 176.593 182.668 221.597 1.00 78.18  ? 55  ASP E N   1 
ATOM 4607 C CA  . ASP D 2 55  ? 175.580 183.654 221.977 1.00 82.65  ? 55  ASP E CA  1 
ATOM 4608 C C   . ASP D 2 55  ? 175.462 183.741 223.494 1.00 82.80  ? 55  ASP E C   1 
ATOM 4609 O O   . ASP D 2 55  ? 175.931 184.706 224.108 1.00 85.08  ? 55  ASP E O   1 
ATOM 4610 C CB  . ASP D 2 55  ? 174.221 183.338 221.341 1.00 80.77  ? 55  ASP E CB  1 
ATOM 4611 C CG  . ASP D 2 55  ? 174.222 183.535 219.838 1.00 89.63  ? 55  ASP E CG  1 
ATOM 4612 O OD1 . ASP D 2 55  ? 174.993 184.388 219.350 1.00 93.31  ? 55  ASP E OD1 1 
ATOM 4613 O OD2 . ASP D 2 55  ? 173.451 182.839 219.144 1.00 92.20  ? 55  ASP E OD2 1 
ATOM 4614 N N   . GLY D 2 56  ? 174.838 182.738 224.103 1.00 77.64  ? 56  GLY E N   1 
ATOM 4615 C CA  . GLY D 2 56  ? 174.852 182.600 225.542 1.00 66.42  ? 56  GLY E CA  1 
ATOM 4616 C C   . GLY D 2 56  ? 173.487 182.633 226.190 1.00 62.61  ? 56  GLY E C   1 
ATOM 4617 O O   . GLY D 2 56  ? 172.867 183.694 226.310 1.00 58.98  ? 56  GLY E O   1 
ATOM 4618 N N   . THR D 2 57  ? 173.013 181.467 226.614 1.00 60.67  ? 57  THR E N   1 
ATOM 4619 C CA  . THR D 2 57  ? 171.825 181.388 227.450 1.00 60.55  ? 57  THR E CA  1 
ATOM 4620 C C   . THR D 2 57  ? 172.252 181.585 228.896 1.00 58.16  ? 57  THR E C   1 
ATOM 4621 O O   . THR D 2 57  ? 173.027 180.789 229.434 1.00 57.68  ? 57  THR E O   1 
ATOM 4622 C CB  . THR D 2 57  ? 171.118 180.048 227.269 1.00 62.53  ? 57  THR E CB  1 
ATOM 4623 O OG1 . THR D 2 57  ? 170.724 179.893 225.900 1.00 64.26  ? 57  THR E OG1 1 
ATOM 4624 C CG2 . THR D 2 57  ? 169.882 179.978 228.153 1.00 60.04  ? 57  THR E CG2 1 
ATOM 4625 N N   . THR D 2 58  ? 171.772 182.656 229.515 1.00 56.80  ? 58  THR E N   1 
ATOM 4626 C CA  . THR D 2 58  ? 172.150 182.986 230.879 1.00 52.79  ? 58  THR E CA  1 
ATOM 4627 C C   . THR D 2 58  ? 171.243 182.253 231.857 1.00 51.46  ? 58  THR E C   1 
ATOM 4628 O O   . THR D 2 58  ? 170.016 182.359 231.774 1.00 55.93  ? 58  THR E O   1 
ATOM 4629 C CB  . THR D 2 58  ? 172.068 184.495 231.108 1.00 53.93  ? 58  THR E CB  1 
ATOM 4630 O OG1 . THR D 2 58  ? 170.702 184.875 231.319 1.00 59.34  ? 58  THR E OG1 1 
ATOM 4631 C CG2 . THR D 2 58  ? 172.618 185.247 229.907 1.00 52.11  ? 58  THR E CG2 1 
ATOM 4632 N N   . TYR D 2 59  ? 171.848 181.512 232.780 1.00 44.37  ? 59  TYR E N   1 
ATOM 4633 C CA  . TYR D 2 59  ? 171.119 180.831 233.838 1.00 49.15  ? 59  TYR E CA  1 
ATOM 4634 C C   . TYR D 2 59  ? 171.441 181.490 235.170 1.00 50.07  ? 59  TYR E C   1 
ATOM 4635 O O   . TYR D 2 59  ? 172.568 181.942 235.392 1.00 52.60  ? 59  TYR E O   1 
ATOM 4636 C CB  . TYR D 2 59  ? 171.447 179.332 233.911 1.00 53.33  ? 59  TYR E CB  1 
ATOM 4637 C CG  . TYR D 2 59  ? 171.215 178.547 232.635 1.00 50.56  ? 59  TYR E CG  1 
ATOM 4638 C CD1 . TYR D 2 59  ? 172.080 178.652 231.554 1.00 48.51  ? 59  TYR E CD1 1 
ATOM 4639 C CD2 . TYR D 2 59  ? 170.176 177.633 232.551 1.00 53.90  ? 59  TYR E CD2 1 
ATOM 4640 C CE1 . TYR D 2 59  ? 171.877 177.924 230.403 1.00 53.61  ? 59  TYR E CE1 1 
ATOM 4641 C CE2 . TYR D 2 59  ? 169.959 176.906 231.400 1.00 56.67  ? 59  TYR E CE2 1 
ATOM 4642 C CZ  . TYR D 2 59  ? 170.819 177.049 230.332 1.00 56.85  ? 59  TYR E CZ  1 
ATOM 4643 O OH  . TYR D 2 59  ? 170.617 176.316 229.185 1.00 58.93  ? 59  TYR E OH  1 
ATOM 4644 N N   . TYR D 2 60  ? 170.446 181.550 236.049 1.00 46.21  ? 60  TYR E N   1 
ATOM 4645 C CA  . TYR D 2 60  ? 170.583 182.233 237.323 1.00 42.79  ? 60  TYR E CA  1 
ATOM 4646 C C   . TYR D 2 60  ? 170.022 181.343 238.420 1.00 46.03  ? 60  TYR E C   1 
ATOM 4647 O O   . TYR D 2 60  ? 169.107 180.549 238.186 1.00 53.28  ? 60  TYR E O   1 
ATOM 4648 C CB  . TYR D 2 60  ? 169.840 183.566 237.320 1.00 41.96  ? 60  TYR E CB  1 
ATOM 4649 C CG  . TYR D 2 60  ? 170.518 184.639 236.510 1.00 38.45  ? 60  TYR E CG  1 
ATOM 4650 C CD1 . TYR D 2 60  ? 170.237 184.776 235.159 1.00 43.55  ? 60  TYR E CD1 1 
ATOM 4651 C CD2 . TYR D 2 60  ? 171.445 185.498 237.078 1.00 36.55  ? 60  TYR E CD2 1 
ATOM 4652 C CE1 . TYR D 2 60  ? 170.842 185.744 234.399 1.00 45.87  ? 60  TYR E CE1 1 
ATOM 4653 C CE2 . TYR D 2 60  ? 172.063 186.473 236.319 1.00 39.80  ? 60  TYR E CE2 1 
ATOM 4654 C CZ  . TYR D 2 60  ? 171.754 186.589 234.979 1.00 44.17  ? 60  TYR E CZ  1 
ATOM 4655 O OH  . TYR D 2 60  ? 172.349 187.549 234.199 1.00 49.56  ? 60  TYR E OH  1 
ATOM 4656 N N   . GLU D 2 61  ? 170.576 181.476 239.619 1.00 45.57  ? 61  GLU E N   1 
ATOM 4657 C CA  . GLU D 2 61  ? 170.049 180.721 240.741 1.00 51.20  ? 61  GLU E CA  1 
ATOM 4658 C C   . GLU D 2 61  ? 168.852 181.443 241.353 1.00 54.38  ? 61  GLU E C   1 
ATOM 4659 O O   . GLU D 2 61  ? 168.550 182.595 241.030 1.00 57.91  ? 61  GLU E O   1 
ATOM 4660 C CB  . GLU D 2 61  ? 171.133 180.480 241.789 1.00 51.91  ? 61  GLU E CB  1 
ATOM 4661 C CG  . GLU D 2 61  ? 172.253 179.573 241.313 1.00 54.11  ? 61  GLU E CG  1 
ATOM 4662 C CD  . GLU D 2 61  ? 171.794 178.147 241.069 1.00 59.14  ? 61  GLU E CD  1 
ATOM 4663 O OE1 . GLU D 2 61  ? 170.872 177.684 241.771 1.00 58.46  ? 61  GLU E OE1 1 
ATOM 4664 O OE2 . GLU D 2 61  ? 172.359 177.487 240.171 1.00 62.17  ? 61  GLU E OE2 1 
ATOM 4665 N N   . ASP D 2 62  ? 168.160 180.738 242.251 1.00 57.16  ? 62  ASP E N   1 
ATOM 4666 C CA  . ASP D 2 62  ? 166.927 181.266 242.822 1.00 58.90  ? 62  ASP E CA  1 
ATOM 4667 C C   . ASP D 2 62  ? 167.188 182.421 243.779 1.00 55.22  ? 62  ASP E C   1 
ATOM 4668 O O   . ASP D 2 62  ? 166.346 183.317 243.907 1.00 55.70  ? 62  ASP E O   1 
ATOM 4669 C CB  . ASP D 2 62  ? 166.163 180.152 243.537 1.00 63.68  ? 62  ASP E CB  1 
ATOM 4670 C CG  . ASP D 2 62  ? 165.961 178.931 242.663 1.00 69.64  ? 62  ASP E CG  1 
ATOM 4671 O OD1 . ASP D 2 62  ? 166.295 178.997 241.461 1.00 68.34  ? 62  ASP E OD1 1 
ATOM 4672 O OD2 . ASP D 2 62  ? 165.468 177.905 243.177 1.00 76.22  ? 62  ASP E OD2 1 
ATOM 4673 N N   . SER D 2 63  ? 168.338 182.421 244.454 1.00 48.24  ? 63  SER E N   1 
ATOM 4674 C CA  . SER D 2 63  ? 168.616 183.448 245.449 1.00 46.53  ? 63  SER E CA  1 
ATOM 4675 C C   . SER D 2 63  ? 168.921 184.802 244.826 1.00 50.31  ? 63  SER E C   1 
ATOM 4676 O O   . SER D 2 63  ? 168.707 185.831 245.476 1.00 53.59  ? 63  SER E O   1 
ATOM 4677 C CB  . SER D 2 63  ? 169.787 183.016 246.331 1.00 47.08  ? 63  SER E CB  1 
ATOM 4678 O OG  . SER D 2 63  ? 169.460 181.856 247.075 1.00 49.59  ? 63  SER E OG  1 
ATOM 4679 N N   . VAL D 2 64  ? 169.406 184.827 243.588 1.00 52.41  ? 64  VAL E N   1 
ATOM 4680 C CA  . VAL D 2 64  ? 169.942 186.034 242.977 1.00 50.02  ? 64  VAL E CA  1 
ATOM 4681 C C   . VAL D 2 64  ? 169.209 186.390 241.684 1.00 52.97  ? 64  VAL E C   1 
ATOM 4682 O O   . VAL D 2 64  ? 169.737 187.124 240.858 1.00 55.36  ? 64  VAL E O   1 
ATOM 4683 C CB  . VAL D 2 64  ? 171.456 185.892 242.734 1.00 50.41  ? 64  VAL E CB  1 
ATOM 4684 C CG1 . VAL D 2 64  ? 172.185 185.701 244.053 1.00 52.46  ? 64  VAL E CG1 1 
ATOM 4685 C CG2 . VAL D 2 64  ? 171.732 184.716 241.801 1.00 52.91  ? 64  VAL E CG2 1 
ATOM 4686 N N   . GLU D 2 65  ? 167.995 185.880 241.501 1.00 54.10  ? 65  GLU E N   1 
ATOM 4687 C CA  . GLU D 2 65  ? 167.266 186.127 240.264 1.00 55.64  ? 65  GLU E CA  1 
ATOM 4688 C C   . GLU D 2 65  ? 166.752 187.563 240.210 1.00 58.16  ? 65  GLU E C   1 
ATOM 4689 O O   . GLU D 2 65  ? 166.315 188.129 241.216 1.00 56.72  ? 65  GLU E O   1 
ATOM 4690 C CB  . GLU D 2 65  ? 166.117 185.126 240.116 1.00 59.62  ? 65  GLU E CB  1 
ATOM 4691 C CG  . GLU D 2 65  ? 165.017 185.233 241.162 1.00 73.20  ? 65  GLU E CG  1 
ATOM 4692 C CD  . GLU D 2 65  ? 163.946 184.179 240.988 1.00 85.33  ? 65  GLU E CD  1 
ATOM 4693 O OE1 . GLU D 2 65  ? 164.076 183.345 240.067 1.00 87.99  ? 65  GLU E OE1 1 
ATOM 4694 O OE2 . GLU D 2 65  ? 162.975 184.183 241.773 1.00 88.26  ? 65  GLU E OE2 1 
ATOM 4695 N N   . GLY D 2 66  ? 166.853 188.172 239.027 1.00 58.12  ? 66  GLY E N   1 
ATOM 4696 C CA  . GLY D 2 66  ? 166.417 189.535 238.814 1.00 54.70  ? 66  GLY E CA  1 
ATOM 4697 C C   . GLY D 2 66  ? 167.375 190.611 239.276 1.00 56.36  ? 66  GLY E C   1 
ATOM 4698 O O   . GLY D 2 66  ? 167.324 191.731 238.753 1.00 60.15  ? 66  GLY E O   1 
ATOM 4699 N N   . ARG D 2 67  ? 168.251 190.317 240.234 1.00 52.09  ? 67  ARG E N   1 
ATOM 4700 C CA  . ARG D 2 67  ? 169.167 191.304 240.790 1.00 47.68  ? 67  ARG E CA  1 
ATOM 4701 C C   . ARG D 2 67  ? 170.505 191.347 240.071 1.00 51.29  ? 67  ARG E C   1 
ATOM 4702 O O   . ARG D 2 67  ? 171.050 192.433 239.853 1.00 54.42  ? 67  ARG E O   1 
ATOM 4703 C CB  . ARG D 2 67  ? 169.410 191.020 242.276 1.00 49.01  ? 67  ARG E CB  1 
ATOM 4704 C CG  . ARG D 2 67  ? 168.174 191.117 243.152 1.00 58.65  ? 67  ARG E CG  1 
ATOM 4705 C CD  . ARG D 2 67  ? 168.557 191.252 244.617 1.00 56.79  ? 67  ARG E CD  1 
ATOM 4706 N NE  . ARG D 2 67  ? 168.913 189.973 245.218 1.00 60.31  ? 67  ARG E NE  1 
ATOM 4707 C CZ  . ARG D 2 67  ? 169.971 189.781 245.994 1.00 58.07  ? 67  ARG E CZ  1 
ATOM 4708 N NH1 . ARG D 2 67  ? 170.810 190.763 246.274 1.00 56.71  ? 67  ARG E NH1 1 
ATOM 4709 N NH2 . ARG D 2 67  ? 170.192 188.571 246.500 1.00 54.67  ? 67  ARG E NH2 1 
ATOM 4710 N N   . PHE D 2 68  ? 171.045 190.195 239.694 1.00 53.13  ? 68  PHE E N   1 
ATOM 4711 C CA  . PHE D 2 68  ? 172.383 190.109 239.127 1.00 53.13  ? 68  PHE E CA  1 
ATOM 4712 C C   . PHE D 2 68  ? 172.287 189.953 237.614 1.00 51.39  ? 68  PHE E C   1 
ATOM 4713 O O   . PHE D 2 68  ? 171.289 189.459 237.084 1.00 53.93  ? 68  PHE E O   1 
ATOM 4714 C CB  . PHE D 2 68  ? 173.190 188.941 239.720 1.00 47.39  ? 68  PHE E CB  1 
ATOM 4715 C CG  . PHE D 2 68  ? 173.505 189.053 241.209 1.00 52.56  ? 68  PHE E CG  1 
ATOM 4716 C CD1 . PHE D 2 68  ? 173.038 190.102 241.995 1.00 60.12  ? 68  PHE E CD1 1 
ATOM 4717 C CD2 . PHE D 2 68  ? 174.286 188.079 241.816 1.00 48.61  ? 68  PHE E CD2 1 
ATOM 4718 C CE1 . PHE D 2 68  ? 173.336 190.168 243.338 1.00 60.54  ? 68  PHE E CE1 1 
ATOM 4719 C CE2 . PHE D 2 68  ? 174.592 188.144 243.157 1.00 50.02  ? 68  PHE E CE2 1 
ATOM 4720 C CZ  . PHE D 2 68  ? 174.116 189.185 243.920 1.00 58.22  ? 68  PHE E CZ  1 
ATOM 4721 N N   . THR D 2 69  ? 173.331 190.400 236.921 1.00 51.11  ? 69  THR E N   1 
ATOM 4722 C CA  . THR D 2 69  ? 173.383 190.345 235.467 1.00 48.81  ? 69  THR E CA  1 
ATOM 4723 C C   . THR D 2 69  ? 174.746 189.828 235.033 1.00 47.39  ? 69  THR E C   1 
ATOM 4724 O O   . THR D 2 69  ? 175.775 190.356 235.464 1.00 52.57  ? 69  THR E O   1 
ATOM 4725 C CB  . THR D 2 69  ? 173.113 191.725 234.855 1.00 49.53  ? 69  THR E CB  1 
ATOM 4726 O OG1 . THR D 2 69  ? 171.812 192.174 235.250 1.00 52.27  ? 69  THR E OG1 1 
ATOM 4727 C CG2 . THR D 2 69  ? 173.189 191.673 233.340 1.00 45.37  ? 69  THR E CG2 1 
ATOM 4728 N N   . ILE D 2 70  ? 174.752 188.804 234.182 1.00 42.93  ? 70  ILE E N   1 
ATOM 4729 C CA  . ILE D 2 70  ? 175.977 188.212 233.660 1.00 43.87  ? 70  ILE E CA  1 
ATOM 4730 C C   . ILE D 2 70  ? 176.103 188.588 232.187 1.00 48.03  ? 70  ILE E C   1 
ATOM 4731 O O   . ILE D 2 70  ? 175.106 188.630 231.455 1.00 53.26  ? 70  ILE E O   1 
ATOM 4732 C CB  . ILE D 2 70  ? 176.008 186.681 233.889 1.00 45.89  ? 70  ILE E CB  1 
ATOM 4733 C CG1 . ILE D 2 70  ? 177.394 186.103 233.616 1.00 41.86  ? 70  ILE E CG1 1 
ATOM 4734 C CG2 . ILE D 2 70  ? 174.948 185.938 233.078 1.00 46.07  ? 70  ILE E CG2 1 
ATOM 4735 C CD1 . ILE D 2 70  ? 178.411 186.420 234.661 1.00 42.46  ? 70  ILE E CD1 1 
ATOM 4736 N N   . SER D 2 71  ? 177.320 188.937 231.772 1.00 46.29  ? 71  SER E N   1 
ATOM 4737 C CA  . SER D 2 71  ? 177.563 189.382 230.406 1.00 48.06  ? 71  SER E CA  1 
ATOM 4738 C C   . SER D 2 71  ? 179.037 189.201 230.075 1.00 49.53  ? 71  SER E C   1 
ATOM 4739 O O   . SER D 2 71  ? 179.888 189.186 230.967 1.00 54.80  ? 71  SER E O   1 
ATOM 4740 C CB  . SER D 2 71  ? 177.153 190.846 230.206 1.00 50.34  ? 71  SER E CB  1 
ATOM 4741 O OG  . SER D 2 71  ? 177.424 191.275 228.883 1.00 57.67  ? 71  SER E OG  1 
ATOM 4742 N N   . ARG D 2 72  ? 179.327 189.074 228.782 1.00 47.98  ? 72  ARG E N   1 
ATOM 4743 C CA  . ARG D 2 72  ? 180.681 188.855 228.293 1.00 52.75  ? 72  ARG E CA  1 
ATOM 4744 C C   . ARG D 2 72  ? 181.024 189.875 227.217 1.00 62.60  ? 72  ARG E C   1 
ATOM 4745 O O   . ARG D 2 72  ? 180.191 190.194 226.363 1.00 66.43  ? 72  ARG E O   1 
ATOM 4746 C CB  . ARG D 2 72  ? 180.844 187.441 227.720 1.00 55.20  ? 72  ARG E CB  1 
ATOM 4747 C CG  . ARG D 2 72  ? 182.269 187.107 227.299 1.00 57.75  ? 72  ARG E CG  1 
ATOM 4748 C CD  . ARG D 2 72  ? 182.404 185.689 226.792 1.00 57.58  ? 72  ARG E CD  1 
ATOM 4749 N NE  . ARG D 2 72  ? 181.638 185.479 225.571 1.00 59.55  ? 72  ARG E NE  1 
ATOM 4750 C CZ  . ARG D 2 72  ? 180.587 184.678 225.477 1.00 57.24  ? 72  ARG E CZ  1 
ATOM 4751 N NH1 . ARG D 2 72  ? 180.178 183.956 226.505 1.00 52.82  ? 72  ARG E NH1 1 
ATOM 4752 N NH2 . ARG D 2 72  ? 179.938 184.591 224.320 1.00 60.23  ? 72  ARG E NH2 1 
ATOM 4753 N N   . ASP D 2 73  ? 182.253 190.385 227.262 1.00 67.43  ? 73  ASP E N   1 
ATOM 4754 C CA  . ASP D 2 73  ? 182.815 191.200 226.193 1.00 73.18  ? 73  ASP E CA  1 
ATOM 4755 C C   . ASP D 2 73  ? 183.894 190.382 225.497 1.00 76.17  ? 73  ASP E C   1 
ATOM 4756 O O   . ASP D 2 73  ? 184.854 189.943 226.139 1.00 72.33  ? 73  ASP E O   1 
ATOM 4757 C CB  . ASP D 2 73  ? 183.389 192.507 226.739 1.00 78.77  ? 73  ASP E CB  1 
ATOM 4758 C CG  . ASP D 2 73  ? 183.880 193.434 225.642 1.00 84.62  ? 73  ASP E CG  1 
ATOM 4759 O OD1 . ASP D 2 73  ? 183.444 193.276 224.482 1.00 82.85  ? 73  ASP E OD1 1 
ATOM 4760 O OD2 . ASP D 2 73  ? 184.706 194.322 225.941 1.00 86.04  ? 73  ASP E OD2 1 
ATOM 4761 N N   . ASN D 2 74  ? 183.738 190.182 224.191 1.00 79.44  ? 74  ASN E N   1 
ATOM 4762 C CA  . ASN D 2 74  ? 184.639 189.328 223.428 1.00 77.25  ? 74  ASN E CA  1 
ATOM 4763 C C   . ASN D 2 74  ? 185.883 190.050 222.919 1.00 74.57  ? 74  ASN E C   1 
ATOM 4764 O O   . ASN D 2 74  ? 186.761 189.402 222.339 1.00 75.85  ? 74  ASN E O   1 
ATOM 4765 C CB  . ASN D 2 74  ? 183.876 188.661 222.268 1.00 77.27  ? 74  ASN E CB  1 
ATOM 4766 C CG  . ASN D 2 74  ? 183.308 189.657 221.253 1.00 83.47  ? 74  ASN E CG  1 
ATOM 4767 O OD1 . ASN D 2 74  ? 183.551 190.863 221.311 1.00 89.29  ? 74  ASN E OD1 1 
ATOM 4768 N ND2 . ASN D 2 74  ? 182.538 189.133 220.305 1.00 75.26  ? 74  ASN E ND2 1 
ATOM 4769 N N   . ALA D 2 75  ? 185.980 191.363 223.119 1.00 75.64  ? 75  ALA E N   1 
ATOM 4770 C CA  . ALA D 2 75  ? 187.176 192.089 222.708 1.00 76.56  ? 75  ALA E CA  1 
ATOM 4771 C C   . ALA D 2 75  ? 188.278 191.974 223.754 1.00 76.29  ? 75  ALA E C   1 
ATOM 4772 O O   . ALA D 2 75  ? 189.431 191.680 223.424 1.00 74.66  ? 75  ALA E O   1 
ATOM 4773 C CB  . ALA D 2 75  ? 186.835 193.556 222.442 1.00 70.01  ? 75  ALA E CB  1 
ATOM 4774 N N   . LYS D 2 76  ? 187.939 192.204 225.019 1.00 74.01  ? 76  LYS E N   1 
ATOM 4775 C CA  . LYS D 2 76  ? 188.891 192.088 226.114 1.00 72.86  ? 76  LYS E CA  1 
ATOM 4776 C C   . LYS D 2 76  ? 188.919 190.694 226.727 1.00 74.97  ? 76  LYS E C   1 
ATOM 4777 O O   . LYS D 2 76  ? 189.711 190.463 227.648 1.00 77.91  ? 76  LYS E O   1 
ATOM 4778 C CB  . LYS D 2 76  ? 188.575 193.126 227.195 1.00 72.74  ? 76  LYS E CB  1 
ATOM 4779 C CG  . LYS D 2 76  ? 188.797 194.562 226.748 1.00 79.28  ? 76  LYS E CG  1 
ATOM 4780 C CD  . LYS D 2 76  ? 188.626 195.539 227.899 1.00 84.21  ? 76  LYS E CD  1 
ATOM 4781 C CE  . LYS D 2 76  ? 187.162 195.706 228.270 1.00 84.74  ? 76  LYS E CE  1 
ATOM 4782 N NZ  . LYS D 2 76  ? 186.973 196.743 229.321 1.00 77.24  ? 76  LYS E NZ  1 
ATOM 4783 N N   . ASN D 2 77  ? 188.078 189.776 226.230 1.00 71.40  ? 77  ASN E N   1 
ATOM 4784 C CA  . ASN D 2 77  ? 188.014 188.378 226.678 1.00 65.66  ? 77  ASN E CA  1 
ATOM 4785 C C   . ASN D 2 77  ? 187.747 188.281 228.181 1.00 67.68  ? 77  ASN E C   1 
ATOM 4786 O O   . ASN D 2 77  ? 188.379 187.507 228.903 1.00 68.64  ? 77  ASN E O   1 
ATOM 4787 C CB  . ASN D 2 77  ? 189.286 187.618 226.291 1.00 60.85  ? 77  ASN E CB  1 
ATOM 4788 C CG  . ASN D 2 77  ? 189.070 186.123 226.209 1.00 57.46  ? 77  ASN E CG  1 
ATOM 4789 O OD1 . ASN D 2 77  ? 188.027 185.659 225.751 1.00 59.31  ? 77  ASN E OD1 1 
ATOM 4790 N ND2 . ASN D 2 77  ? 190.059 185.359 226.655 1.00 56.86  ? 77  ASN E ND2 1 
ATOM 4791 N N   . THR D 2 78  ? 186.797 189.085 228.653 1.00 62.08  ? 78  THR E N   1 
ATOM 4792 C CA  . THR D 2 78  ? 186.495 189.190 230.073 1.00 55.31  ? 78  THR E CA  1 
ATOM 4793 C C   . THR D 2 78  ? 184.993 189.074 230.278 1.00 52.92  ? 78  THR E C   1 
ATOM 4794 O O   . THR D 2 78  ? 184.216 189.715 229.562 1.00 59.17  ? 78  THR E O   1 
ATOM 4795 C CB  . THR D 2 78  ? 187.016 190.516 230.641 1.00 61.21  ? 78  THR E CB  1 
ATOM 4796 O OG1 . THR D 2 78  ? 188.436 190.586 230.463 1.00 66.96  ? 78  THR E OG1 1 
ATOM 4797 C CG2 . THR D 2 78  ? 186.701 190.637 232.123 1.00 58.76  ? 78  THR E CG2 1 
ATOM 4798 N N   . VAL D 2 79  ? 184.586 188.255 231.246 1.00 47.30  ? 79  VAL E N   1 
ATOM 4799 C CA  . VAL D 2 79  ? 183.187 188.121 231.634 1.00 46.21  ? 79  VAL E CA  1 
ATOM 4800 C C   . VAL D 2 79  ? 182.922 189.045 232.818 1.00 48.38  ? 79  VAL E C   1 
ATOM 4801 O O   . VAL D 2 79  ? 183.798 189.259 233.667 1.00 53.36  ? 79  VAL E O   1 
ATOM 4802 C CB  . VAL D 2 79  ? 182.836 186.648 231.945 1.00 45.40  ? 79  VAL E CB  1 
ATOM 4803 C CG1 . VAL D 2 79  ? 183.592 186.126 233.160 1.00 45.74  ? 79  VAL E CG1 1 
ATOM 4804 C CG2 . VAL D 2 79  ? 181.334 186.463 232.120 1.00 48.82  ? 79  VAL E CG2 1 
ATOM 4805 N N   . TYR D 2 80  ? 181.731 189.639 232.849 1.00 45.82  ? 80  TYR E N   1 
ATOM 4806 C CA  . TYR D 2 80  ? 181.347 190.598 233.875 1.00 44.26  ? 80  TYR E CA  1 
ATOM 4807 C C   . TYR D 2 80  ? 180.127 190.106 234.639 1.00 45.30  ? 80  TYR E C   1 
ATOM 4808 O O   . TYR D 2 80  ? 179.204 189.536 234.052 1.00 50.65  ? 80  TYR E O   1 
ATOM 4809 C CB  . TYR D 2 80  ? 181.034 191.967 233.266 1.00 47.97  ? 80  TYR E CB  1 
ATOM 4810 C CG  . TYR D 2 80  ? 182.211 192.670 232.637 1.00 49.25  ? 80  TYR E CG  1 
ATOM 4811 C CD1 . TYR D 2 80  ? 183.434 192.735 233.289 1.00 52.22  ? 80  TYR E CD1 1 
ATOM 4812 C CD2 . TYR D 2 80  ? 182.097 193.275 231.393 1.00 46.01  ? 80  TYR E CD2 1 
ATOM 4813 C CE1 . TYR D 2 80  ? 184.509 193.386 232.720 1.00 56.21  ? 80  TYR E CE1 1 
ATOM 4814 C CE2 . TYR D 2 80  ? 183.167 193.923 230.815 1.00 48.77  ? 80  TYR E CE2 1 
ATOM 4815 C CZ  . TYR D 2 80  ? 184.371 193.974 231.481 1.00 57.40  ? 80  TYR E CZ  1 
ATOM 4816 O OH  . TYR D 2 80  ? 185.441 194.620 230.909 1.00 62.98  ? 80  TYR E OH  1 
ATOM 4817 N N   . LEU D 2 81  ? 180.124 190.346 235.949 1.00 42.15  ? 81  LEU E N   1 
ATOM 4818 C CA  . LEU D 2 81  ? 178.968 190.106 236.811 1.00 43.33  ? 81  LEU E CA  1 
ATOM 4819 C C   . LEU D 2 81  ? 178.555 191.441 237.422 1.00 49.84  ? 81  LEU E C   1 
ATOM 4820 O O   . LEU D 2 81  ? 179.196 191.925 238.360 1.00 57.21  ? 81  LEU E O   1 
ATOM 4821 C CB  . LEU D 2 81  ? 179.285 189.078 237.893 1.00 41.84  ? 81  LEU E CB  1 
ATOM 4822 C CG  . LEU D 2 81  ? 178.095 188.567 238.710 1.00 41.49  ? 81  LEU E CG  1 
ATOM 4823 C CD1 . LEU D 2 81  ? 177.129 187.768 237.857 1.00 41.24  ? 81  LEU E CD1 1 
ATOM 4824 C CD2 . LEU D 2 81  ? 178.574 187.746 239.896 1.00 45.97  ? 81  LEU E CD2 1 
ATOM 4825 N N   . GLN D 2 82  ? 177.486 192.033 236.895 1.00 46.57  ? 82  GLN E N   1 
ATOM 4826 C CA  . GLN D 2 82  ? 176.950 193.280 237.425 1.00 45.30  ? 82  GLN E CA  1 
ATOM 4827 C C   . GLN D 2 82  ? 175.939 192.931 238.509 1.00 48.91  ? 82  GLN E C   1 
ATOM 4828 O O   . GLN D 2 82  ? 174.867 192.386 238.224 1.00 56.36  ? 82  GLN E O   1 
ATOM 4829 C CB  . GLN D 2 82  ? 176.329 194.128 236.316 1.00 50.00  ? 82  GLN E CB  1 
ATOM 4830 C CG  . GLN D 2 82  ? 175.426 195.248 236.818 1.00 53.19  ? 82  GLN E CG  1 
ATOM 4831 C CD  . GLN D 2 82  ? 176.165 196.555 237.016 1.00 55.51  ? 82  GLN E CD  1 
ATOM 4832 O OE1 . GLN D 2 82  ? 177.387 196.577 237.161 1.00 61.35  ? 82  GLN E OE1 1 
ATOM 4833 N NE2 . GLN D 2 82  ? 175.423 197.654 237.034 1.00 53.91  ? 82  GLN E NE2 1 
ATOM 4834 N N   . MET D 2 83  ? 176.298 193.217 239.753 1.00 47.64  ? 83  MET E N   1 
ATOM 4835 C CA  . MET D 2 83  ? 175.469 192.893 240.903 1.00 47.47  ? 83  MET E CA  1 
ATOM 4836 C C   . MET D 2 83  ? 174.717 194.144 241.336 1.00 53.38  ? 83  MET E C   1 
ATOM 4837 O O   . MET D 2 83  ? 175.333 195.185 241.579 1.00 60.92  ? 83  MET E O   1 
ATOM 4838 C CB  . MET D 2 83  ? 176.336 192.369 242.049 1.00 50.06  ? 83  MET E CB  1 
ATOM 4839 C CG  . MET D 2 83  ? 176.565 190.878 242.031 1.00 55.07  ? 83  MET E CG  1 
ATOM 4840 S SD  . MET D 2 83  ? 177.704 190.355 243.333 1.00 57.81  ? 83  MET E SD  1 
ATOM 4841 C CE  . MET D 2 83  ? 179.090 191.447 243.039 1.00 55.28  ? 83  MET E CE  1 
ATOM 4842 N N   . ASN D 2 84  ? 173.394 194.051 241.427 1.00 48.89  ? 84  ASN E N   1 
ATOM 4843 C CA  . ASN D 2 84  ? 172.565 195.189 241.802 1.00 50.37  ? 84  ASN E CA  1 
ATOM 4844 C C   . ASN D 2 84  ? 171.775 194.877 243.065 1.00 52.61  ? 84  ASN E C   1 
ATOM 4845 O O   . ASN D 2 84  ? 171.287 193.756 243.240 1.00 59.86  ? 84  ASN E O   1 
ATOM 4846 C CB  . ASN D 2 84  ? 171.607 195.572 240.672 1.00 53.39  ? 84  ASN E CB  1 
ATOM 4847 C CG  . ASN D 2 84  ? 172.328 195.972 239.403 1.00 58.75  ? 84  ASN E CG  1 
ATOM 4848 O OD1 . ASN D 2 84  ? 173.530 196.227 239.410 1.00 58.34  ? 84  ASN E OD1 1 
ATOM 4849 N ND2 . ASN D 2 84  ? 171.589 196.041 238.304 1.00 63.69  ? 84  ASN E ND2 1 
ATOM 4850 N N   . SER D 2 85  ? 171.652 195.887 243.932 1.00 47.74  ? 85  SER E N   1 
ATOM 4851 C CA  . SER D 2 85  ? 170.854 195.830 245.162 1.00 47.71  ? 85  SER E CA  1 
ATOM 4852 C C   . SER D 2 85  ? 171.304 194.682 246.070 1.00 53.77  ? 85  SER E C   1 
ATOM 4853 O O   . SER D 2 85  ? 170.565 193.734 246.343 1.00 60.20  ? 85  SER E O   1 
ATOM 4854 C CB  . SER D 2 85  ? 169.356 195.739 244.848 1.00 50.54  ? 85  SER E CB  1 
ATOM 4855 O OG  . SER D 2 85  ? 169.004 194.475 244.315 1.00 56.37  ? 85  SER E OG  1 
ATOM 4856 N N   . LEU D 2 86  ? 172.548 194.785 246.526 1.00 51.60  ? 86  LEU E N   1 
ATOM 4857 C CA  . LEU D 2 86  ? 173.148 193.752 247.358 1.00 52.10  ? 86  LEU E CA  1 
ATOM 4858 C C   . LEU D 2 86  ? 172.579 193.800 248.770 1.00 50.78  ? 86  LEU E C   1 
ATOM 4859 O O   . LEU D 2 86  ? 172.511 194.867 249.387 1.00 53.11  ? 86  LEU E O   1 
ATOM 4860 C CB  . LEU D 2 86  ? 174.665 193.926 247.392 1.00 52.37  ? 86  LEU E CB  1 
ATOM 4861 C CG  . LEU D 2 86  ? 175.368 193.787 246.044 1.00 57.74  ? 86  LEU E CG  1 
ATOM 4862 C CD1 . LEU D 2 86  ? 176.748 194.413 246.089 1.00 56.83  ? 86  LEU E CD1 1 
ATOM 4863 C CD2 . LEU D 2 86  ? 175.456 192.321 245.658 1.00 57.32  ? 86  LEU E CD2 1 
ATOM 4864 N N   . LYS D 2 87  ? 172.171 192.642 249.274 1.00 49.74  ? 87  LYS E N   1 
ATOM 4865 C CA  . LYS D 2 87  ? 171.687 192.492 250.636 1.00 50.28  ? 87  LYS E CA  1 
ATOM 4866 C C   . LYS D 2 87  ? 172.820 192.029 251.543 1.00 52.06  ? 87  LYS E C   1 
ATOM 4867 O O   . LYS D 2 87  ? 173.857 191.551 251.080 1.00 56.99  ? 87  LYS E O   1 
ATOM 4868 C CB  . LYS D 2 87  ? 170.524 191.500 250.693 1.00 54.50  ? 87  LYS E CB  1 
ATOM 4869 C CG  . LYS D 2 87  ? 169.412 191.779 249.695 1.00 57.89  ? 87  LYS E CG  1 
ATOM 4870 C CD  . LYS D 2 87  ? 168.848 193.180 249.869 1.00 60.61  ? 87  LYS E CD  1 
ATOM 4871 C CE  . LYS D 2 87  ? 167.722 193.448 248.884 1.00 58.35  ? 87  LYS E CE  1 
ATOM 4872 N NZ  . LYS D 2 87  ? 167.210 194.842 248.987 1.00 54.72  ? 87  LYS E NZ  1 
ATOM 4873 N N   . LEU D 2 88  ? 172.597 192.158 252.855 1.00 54.93  ? 88  LEU E N   1 
ATOM 4874 C CA  . LEU D 2 88  ? 173.666 191.949 253.828 1.00 58.23  ? 88  LEU E CA  1 
ATOM 4875 C C   . LEU D 2 88  ? 174.097 190.491 253.943 1.00 61.78  ? 88  LEU E C   1 
ATOM 4876 O O   . LEU D 2 88  ? 175.201 190.225 254.429 1.00 62.77  ? 88  LEU E O   1 
ATOM 4877 C CB  . LEU D 2 88  ? 173.239 192.501 255.196 1.00 60.36  ? 88  LEU E CB  1 
ATOM 4878 C CG  . LEU D 2 88  ? 172.020 191.981 255.978 1.00 67.08  ? 88  LEU E CG  1 
ATOM 4879 C CD1 . LEU D 2 88  ? 172.296 190.729 256.818 1.00 63.86  ? 88  LEU E CD1 1 
ATOM 4880 C CD2 . LEU D 2 88  ? 171.449 193.092 256.853 1.00 65.52  ? 88  LEU E CD2 1 
ATOM 4881 N N   . GLU D 2 89  ? 173.265 189.546 253.515 1.00 62.01  ? 89  GLU E N   1 
ATOM 4882 C CA  . GLU D 2 89  ? 173.627 188.136 253.554 1.00 59.03  ? 89  GLU E CA  1 
ATOM 4883 C C   . GLU D 2 89  ? 174.397 187.689 252.318 1.00 57.41  ? 89  GLU E C   1 
ATOM 4884 O O   . GLU D 2 89  ? 174.782 186.518 252.234 1.00 57.51  ? 89  GLU E O   1 
ATOM 4885 C CB  . GLU D 2 89  ? 172.373 187.270 253.737 1.00 62.22  ? 89  GLU E CB  1 
ATOM 4886 C CG  . GLU D 2 89  ? 171.587 186.993 252.463 1.00 67.65  ? 89  GLU E CG  1 
ATOM 4887 C CD  . GLU D 2 89  ? 170.718 188.161 252.046 1.00 72.78  ? 89  GLU E CD  1 
ATOM 4888 O OE1 . GLU D 2 89  ? 170.450 189.038 252.894 1.00 71.98  ? 89  GLU E OE1 1 
ATOM 4889 O OE2 . GLU D 2 89  ? 170.300 188.200 250.870 1.00 71.91  ? 89  GLU E OE2 1 
ATOM 4890 N N   . ASP D 2 90  ? 174.651 188.592 251.374 1.00 57.62  ? 90  ASP E N   1 
ATOM 4891 C CA  . ASP D 2 90  ? 175.361 188.270 250.145 1.00 55.73  ? 90  ASP E CA  1 
ATOM 4892 C C   . ASP D 2 90  ? 176.873 188.366 250.290 1.00 57.43  ? 90  ASP E C   1 
ATOM 4893 O O   . ASP D 2 90  ? 177.585 188.203 249.294 1.00 61.84  ? 90  ASP E O   1 
ATOM 4894 C CB  . ASP D 2 90  ? 174.899 189.185 249.009 1.00 55.63  ? 90  ASP E CB  1 
ATOM 4895 C CG  . ASP D 2 90  ? 173.575 188.755 248.415 1.00 63.97  ? 90  ASP E CG  1 
ATOM 4896 O OD1 . ASP D 2 90  ? 173.435 187.561 248.078 1.00 67.64  ? 90  ASP E OD1 1 
ATOM 4897 O OD2 . ASP D 2 90  ? 172.677 189.612 248.278 1.00 65.18  ? 90  ASP E OD2 1 
ATOM 4898 N N   . THR D 2 91  ? 177.377 188.636 251.491 1.00 57.61  ? 91  THR E N   1 
ATOM 4899 C CA  . THR D 2 91  ? 178.819 188.685 251.693 1.00 59.68  ? 91  THR E CA  1 
ATOM 4900 C C   . THR D 2 91  ? 179.422 187.284 251.594 1.00 59.10  ? 91  THR E C   1 
ATOM 4901 O O   . THR D 2 91  ? 178.936 186.329 252.212 1.00 63.24  ? 91  THR E O   1 
ATOM 4902 C CB  . THR D 2 91  ? 179.151 189.374 253.028 1.00 61.12  ? 91  THR E CB  1 
ATOM 4903 O OG1 . THR D 2 91  ? 180.567 189.567 253.143 1.00 63.49  ? 91  THR E OG1 1 
ATOM 4904 C CG2 . THR D 2 91  ? 178.590 188.647 254.260 1.00 59.45  ? 91  THR E CG2 1 
ATOM 4905 N N   . ALA D 2 92  ? 180.449 187.159 250.763 1.00 56.03  ? 92  ALA E N   1 
ATOM 4906 C CA  . ALA D 2 92  ? 181.085 185.887 250.426 1.00 57.08  ? 92  ALA E CA  1 
ATOM 4907 C C   . ALA D 2 92  ? 182.370 186.198 249.668 1.00 57.16  ? 92  ALA E C   1 
ATOM 4908 O O   . ALA D 2 92  ? 182.772 187.361 249.541 1.00 59.86  ? 92  ALA E O   1 
ATOM 4909 C CB  . ALA D 2 92  ? 180.159 184.993 249.597 1.00 58.03  ? 92  ALA E CB  1 
ATOM 4910 N N   . VAL D 2 93  ? 183.015 185.151 249.163 1.00 52.98  ? 93  VAL E N   1 
ATOM 4911 C CA  . VAL D 2 93  ? 184.100 185.266 248.200 1.00 51.73  ? 93  VAL E CA  1 
ATOM 4912 C C   . VAL D 2 93  ? 183.656 184.575 246.914 1.00 49.00  ? 93  VAL E C   1 
ATOM 4913 O O   . VAL D 2 93  ? 183.014 183.521 246.952 1.00 51.13  ? 93  VAL E O   1 
ATOM 4914 C CB  . VAL D 2 93  ? 185.430 184.704 248.764 1.00 54.20  ? 93  VAL E CB  1 
ATOM 4915 C CG1 . VAL D 2 93  ? 185.439 183.185 248.874 1.00 54.20  ? 93  VAL E CG1 1 
ATOM 4916 C CG2 . VAL D 2 93  ? 186.603 185.162 247.919 1.00 58.83  ? 93  VAL E CG2 1 
ATOM 4917 N N   . TYR D 2 94  ? 183.920 185.215 245.779 1.00 49.98  ? 94  TYR E N   1 
ATOM 4918 C CA  . TYR D 2 94  ? 183.397 184.776 244.492 1.00 50.13  ? 94  TYR E CA  1 
ATOM 4919 C C   . TYR D 2 94  ? 184.513 184.229 243.611 1.00 55.03  ? 94  TYR E C   1 
ATOM 4920 O O   . TYR D 2 94  ? 185.585 184.831 243.506 1.00 61.13  ? 94  TYR E O   1 
ATOM 4921 C CB  . TYR D 2 94  ? 182.684 185.921 243.765 1.00 51.25  ? 94  TYR E CB  1 
ATOM 4922 C CG  . TYR D 2 94  ? 181.318 186.260 244.316 1.00 46.89  ? 94  TYR E CG  1 
ATOM 4923 C CD1 . TYR D 2 94  ? 181.168 187.183 245.341 1.00 48.27  ? 94  TYR E CD1 1 
ATOM 4924 C CD2 . TYR D 2 94  ? 180.176 185.660 243.804 1.00 47.96  ? 94  TYR E CD2 1 
ATOM 4925 C CE1 . TYR D 2 94  ? 179.919 187.496 245.844 1.00 47.52  ? 94  TYR E CE1 1 
ATOM 4926 C CE2 . TYR D 2 94  ? 178.922 185.965 244.301 1.00 52.88  ? 94  TYR E CE2 1 
ATOM 4927 C CZ  . TYR D 2 94  ? 178.801 186.883 245.322 1.00 50.22  ? 94  TYR E CZ  1 
ATOM 4928 O OH  . TYR D 2 94  ? 177.557 187.191 245.819 1.00 54.77  ? 94  TYR E OH  1 
ATOM 4929 N N   . TYR D 2 95  ? 184.245 183.096 242.965 1.00 49.33  ? 95  TYR E N   1 
ATOM 4930 C CA  . TYR D 2 95  ? 185.197 182.440 242.080 1.00 49.11  ? 95  TYR E CA  1 
ATOM 4931 C C   . TYR D 2 95  ? 184.618 182.364 240.676 1.00 50.86  ? 95  TYR E C   1 
ATOM 4932 O O   . TYR D 2 95  ? 183.415 182.146 240.506 1.00 52.91  ? 95  TYR E O   1 
ATOM 4933 C CB  . TYR D 2 95  ? 185.524 181.023 242.564 1.00 51.38  ? 95  TYR E CB  1 
ATOM 4934 C CG  . TYR D 2 95  ? 186.030 180.937 243.983 1.00 58.23  ? 95  TYR E CG  1 
ATOM 4935 C CD1 . TYR D 2 95  ? 187.382 181.067 244.269 1.00 60.72  ? 95  TYR E CD1 1 
ATOM 4936 C CD2 . TYR D 2 95  ? 185.157 180.698 245.036 1.00 57.78  ? 95  TYR E CD2 1 
ATOM 4937 C CE1 . TYR D 2 95  ? 187.848 180.980 245.566 1.00 60.97  ? 95  TYR E CE1 1 
ATOM 4938 C CE2 . TYR D 2 95  ? 185.615 180.609 246.337 1.00 63.46  ? 95  TYR E CE2 1 
ATOM 4939 C CZ  . TYR D 2 95  ? 186.962 180.752 246.595 1.00 64.99  ? 95  TYR E CZ  1 
ATOM 4940 O OH  . TYR D 2 95  ? 187.426 180.664 247.887 1.00 68.65  ? 95  TYR E OH  1 
ATOM 4941 N N   . CYS D 2 96  ? 185.470 182.534 239.668 1.00 47.56  ? 96  CYS E N   1 
ATOM 4942 C CA  . CYS D 2 96  ? 185.075 182.336 238.281 1.00 41.26  ? 96  CYS E CA  1 
ATOM 4943 C C   . CYS D 2 96  ? 185.736 181.075 237.741 1.00 42.30  ? 96  CYS E C   1 
ATOM 4944 O O   . CYS D 2 96  ? 186.926 180.837 237.969 1.00 48.69  ? 96  CYS E O   1 
ATOM 4945 C CB  . CYS D 2 96  ? 185.427 183.550 237.407 1.00 40.87  ? 96  CYS E CB  1 
ATOM 4946 S SG  . CYS D 2 96  ? 187.179 183.919 237.179 1.00 56.73  ? 96  CYS E SG  1 
ATOM 4947 N N   . ALA D 2 97  ? 184.950 180.257 237.047 1.00 38.89  ? 97  ALA E N   1 
ATOM 4948 C CA  . ALA D 2 97  ? 185.408 178.979 236.530 1.00 34.98  ? 97  ALA E CA  1 
ATOM 4949 C C   . ALA D 2 97  ? 184.958 178.817 235.086 1.00 35.11  ? 97  ALA E C   1 
ATOM 4950 O O   . ALA D 2 97  ? 183.941 179.377 234.671 1.00 41.56  ? 97  ALA E O   1 
ATOM 4951 C CB  . ALA D 2 97  ? 184.881 177.820 237.380 1.00 35.80  ? 97  ALA E CB  1 
ATOM 4952 N N   . ALA D 2 98  ? 185.722 178.037 234.325 1.00 33.42  ? 98  ALA E N   1 
ATOM 4953 C CA  . ALA D 2 98  ? 185.447 177.822 232.913 1.00 37.34  ? 98  ALA E CA  1 
ATOM 4954 C C   . ALA D 2 98  ? 185.580 176.342 232.589 1.00 41.64  ? 98  ALA E C   1 
ATOM 4955 O O   . ALA D 2 98  ? 186.295 175.604 233.271 1.00 46.46  ? 98  ALA E O   1 
ATOM 4956 C CB  . ALA D 2 98  ? 186.388 178.640 232.020 1.00 37.01  ? 98  ALA E CB  1 
ATOM 4957 N N   . ASP D 2 99  ? 184.882 175.916 231.534 1.00 37.00  ? 99  ASP E N   1 
ATOM 4958 C CA  . ASP D 2 99  ? 184.863 174.520 231.131 1.00 37.34  ? 99  ASP E CA  1 
ATOM 4959 C C   . ASP D 2 99  ? 184.641 174.445 229.629 1.00 37.40  ? 99  ASP E C   1 
ATOM 4960 O O   . ASP D 2 99  ? 183.866 175.246 229.088 1.00 42.46  ? 99  ASP E O   1 
ATOM 4961 C CB  . ASP D 2 99  ? 183.763 173.742 231.859 1.00 42.33  ? 99  ASP E CB  1 
ATOM 4962 C CG  . ASP D 2 99  ? 184.117 172.286 232.068 1.00 48.98  ? 99  ASP E CG  1 
ATOM 4963 O OD1 . ASP D 2 99  ? 185.284 171.998 232.404 1.00 49.75  ? 99  ASP E OD1 1 
ATOM 4964 O OD2 . ASP D 2 99  ? 183.228 171.427 231.894 1.00 50.64  ? 99  ASP E OD2 1 
ATOM 4965 N N   . PRO D 2 100 ? 185.301 173.519 228.934 1.00 31.29  ? 100 PRO E N   1 
ATOM 4966 C CA  . PRO D 2 100 ? 185.075 173.382 227.491 1.00 29.93  ? 100 PRO E CA  1 
ATOM 4967 C C   . PRO D 2 100 ? 183.692 172.830 227.180 1.00 33.03  ? 100 PRO E C   1 
ATOM 4968 O O   . PRO D 2 100 ? 183.186 171.940 227.866 1.00 32.45  ? 100 PRO E O   1 
ATOM 4969 C CB  . PRO D 2 100 ? 186.176 172.410 227.051 1.00 26.73  ? 100 PRO E CB  1 
ATOM 4970 C CG  . PRO D 2 100 ? 187.184 172.443 228.151 1.00 29.25  ? 100 PRO E CG  1 
ATOM 4971 C CD  . PRO D 2 100 ? 186.409 172.670 229.397 1.00 32.18  ? 100 PRO E CD  1 
ATOM 4972 N N   . GLY D 2 101 ? 183.084 173.372 226.131 1.00 40.03  ? 101 GLY E N   1 
ATOM 4973 C CA  . GLY D 2 101 ? 181.758 172.969 225.716 1.00 37.58  ? 101 GLY E CA  1 
ATOM 4974 C C   . GLY D 2 101 ? 180.664 173.775 226.395 1.00 41.33  ? 101 GLY E C   1 
ATOM 4975 O O   . GLY D 2 101 ? 180.867 174.423 227.421 1.00 42.11  ? 101 GLY E O   1 
ATOM 4976 N N   . ALA D 2 102 ? 179.472 173.724 225.799 1.00 46.57  ? 102 ALA E N   1 
ATOM 4977 C CA  . ALA D 2 102 ? 178.286 174.360 226.376 1.00 46.90  ? 102 ALA E CA  1 
ATOM 4978 C C   . ALA D 2 102 ? 177.816 173.491 227.538 1.00 46.05  ? 102 ALA E C   1 
ATOM 4979 O O   . ALA D 2 102 ? 176.859 172.718 227.447 1.00 41.81  ? 102 ALA E O   1 
ATOM 4980 C CB  . ALA D 2 102 ? 177.201 174.542 225.322 1.00 48.53  ? 102 ALA E CB  1 
ATOM 4981 N N   . VAL D 2 103 ? 178.512 173.638 228.664 1.00 52.18  ? 103 VAL E N   1 
ATOM 4982 C CA  . VAL D 2 103 ? 178.396 172.684 229.758 1.00 58.35  ? 103 VAL E CA  1 
ATOM 4983 C C   . VAL D 2 103 ? 177.173 172.946 230.636 1.00 61.46  ? 103 VAL E C   1 
ATOM 4984 O O   . VAL D 2 103 ? 176.669 172.012 231.277 1.00 64.69  ? 103 VAL E O   1 
ATOM 4985 C CB  . VAL D 2 103 ? 179.714 172.702 230.563 1.00 56.96  ? 103 VAL E CB  1 
ATOM 4986 C CG1 . VAL D 2 103 ? 179.925 174.039 231.244 1.00 53.34  ? 103 VAL E CG1 1 
ATOM 4987 C CG2 . VAL D 2 103 ? 179.813 171.552 231.551 1.00 56.61  ? 103 VAL E CG2 1 
ATOM 4988 N N   . CYS D 2 104 ? 176.648 174.168 230.645 1.00 53.91  ? 104 CYS E N   1 
ATOM 4989 C CA  . CYS D 2 104 ? 175.518 174.501 231.504 1.00 47.54  ? 104 CYS E CA  1 
ATOM 4990 C C   . CYS D 2 104 ? 174.217 174.026 230.869 1.00 50.24  ? 104 CYS E C   1 
ATOM 4991 O O   . CYS D 2 104 ? 173.842 174.487 229.784 1.00 57.43  ? 104 CYS E O   1 
ATOM 4992 C CB  . CYS D 2 104 ? 175.485 176.003 231.783 1.00 47.96  ? 104 CYS E CB  1 
ATOM 4993 S SG  . CYS D 2 104 ? 176.896 176.583 232.768 1.00 78.96  ? 104 CYS E SG  1 
ATOM 4994 N N   . HIS D 2 105 ? 173.541 173.100 231.555 1.00 48.02  ? 105 HIS E N   1 
ATOM 4995 C CA  . HIS D 2 105 ? 172.234 172.547 231.185 1.00 50.64  ? 105 HIS E CA  1 
ATOM 4996 C C   . HIS D 2 105 ? 172.266 171.876 229.807 1.00 57.02  ? 105 HIS E C   1 
ATOM 4997 O O   . HIS D 2 105 ? 171.666 172.334 228.833 1.00 61.28  ? 105 HIS E O   1 
ATOM 4998 C CB  . HIS D 2 105 ? 171.128 173.603 231.253 1.00 53.33  ? 105 HIS E CB  1 
ATOM 4999 C CG  . HIS D 2 105 ? 169.751 173.033 231.107 1.00 59.06  ? 105 HIS E CG  1 
ATOM 5000 N ND1 . HIS D 2 105 ? 169.258 172.060 231.949 1.00 58.35  ? 105 HIS E ND1 1 
ATOM 5001 C CD2 . HIS D 2 105 ? 168.772 173.284 230.207 1.00 61.03  ? 105 HIS E CD2 1 
ATOM 5002 C CE1 . HIS D 2 105 ? 168.030 171.744 231.581 1.00 60.44  ? 105 HIS E CE1 1 
ATOM 5003 N NE2 . HIS D 2 105 ? 167.711 172.471 230.526 1.00 65.69  ? 105 HIS E NE2 1 
ATOM 5004 N N   . SER D 2 106 ? 173.011 170.778 229.752 1.00 54.10  ? 106 SER E N   1 
ATOM 5005 C CA  . SER D 2 106 ? 172.931 169.829 228.648 1.00 47.96  ? 106 SER E CA  1 
ATOM 5006 C C   . SER D 2 106 ? 172.343 168.534 229.197 1.00 46.64  ? 106 SER E C   1 
ATOM 5007 O O   . SER D 2 106 ? 172.990 167.843 229.991 1.00 50.09  ? 106 SER E O   1 
ATOM 5008 C CB  . SER D 2 106 ? 174.301 169.594 228.017 1.00 52.69  ? 106 SER E CB  1 
ATOM 5009 O OG  . SER D 2 106 ? 174.188 168.819 226.836 1.00 59.69  ? 106 SER E OG  1 
ATOM 5010 N N   . GLY D 2 107 ? 171.119 168.214 228.781 1.00 46.85  ? 107 GLY E N   1 
ATOM 5011 C CA  . GLY D 2 107 ? 170.484 166.985 229.233 1.00 45.72  ? 107 GLY E CA  1 
ATOM 5012 C C   . GLY D 2 107 ? 170.069 167.067 230.689 1.00 45.43  ? 107 GLY E C   1 
ATOM 5013 O O   . GLY D 2 107 ? 169.575 168.094 231.166 1.00 52.38  ? 107 GLY E O   1 
ATOM 5014 N N   . SER D 2 108 ? 170.268 165.967 231.410 1.00 46.59  ? 108 SER E N   1 
ATOM 5015 C CA  . SER D 2 108 ? 170.010 165.928 232.849 1.00 49.36  ? 108 SER E CA  1 
ATOM 5016 C C   . SER D 2 108 ? 171.260 166.301 233.639 1.00 44.84  ? 108 SER E C   1 
ATOM 5017 O O   . SER D 2 108 ? 171.686 165.601 234.556 1.00 44.04  ? 108 SER E O   1 
ATOM 5018 C CB  . SER D 2 108 ? 169.500 164.550 233.251 1.00 54.83  ? 108 SER E CB  1 
ATOM 5019 O OG  . SER D 2 108 ? 170.501 163.564 233.070 1.00 58.76  ? 108 SER E OG  1 
ATOM 5020 N N   . TYR D 2 109 ? 171.851 167.435 233.273 1.00 42.72  ? 109 TYR E N   1 
ATOM 5021 C CA  . TYR D 2 109 ? 173.050 167.949 233.911 1.00 45.46  ? 109 TYR E CA  1 
ATOM 5022 C C   . TYR D 2 109 ? 172.870 169.445 234.107 1.00 52.21  ? 109 TYR E C   1 
ATOM 5023 O O   . TYR D 2 109 ? 172.184 170.103 233.323 1.00 61.22  ? 109 TYR E O   1 
ATOM 5024 C CB  . TYR D 2 109 ? 174.294 167.663 233.064 1.00 46.51  ? 109 TYR E CB  1 
ATOM 5025 C CG  . TYR D 2 109 ? 175.570 168.253 233.609 1.00 50.47  ? 109 TYR E CG  1 
ATOM 5026 C CD1 . TYR D 2 109 ? 176.081 167.839 234.831 1.00 56.30  ? 109 TYR E CD1 1 
ATOM 5027 C CD2 . TYR D 2 109 ? 176.260 169.225 232.906 1.00 46.35  ? 109 TYR E CD2 1 
ATOM 5028 C CE1 . TYR D 2 109 ? 177.250 168.376 235.334 1.00 57.45  ? 109 TYR E CE1 1 
ATOM 5029 C CE2 . TYR D 2 109 ? 177.423 169.767 233.402 1.00 47.40  ? 109 TYR E CE2 1 
ATOM 5030 C CZ  . TYR D 2 109 ? 177.917 169.341 234.612 1.00 54.46  ? 109 TYR E CZ  1 
ATOM 5031 O OH  . TYR D 2 109 ? 179.080 169.886 235.102 1.00 52.30  ? 109 TYR E OH  1 
ATOM 5032 N N   . TYR D 2 110 ? 173.476 169.980 235.164 1.00 49.35  ? 110 TYR E N   1 
ATOM 5033 C CA  . TYR D 2 110 ? 173.342 171.400 235.445 1.00 47.26  ? 110 TYR E CA  1 
ATOM 5034 C C   . TYR D 2 110 ? 174.578 171.833 236.222 1.00 47.12  ? 110 TYR E C   1 
ATOM 5035 O O   . TYR D 2 110 ? 175.232 171.020 236.881 1.00 50.04  ? 110 TYR E O   1 
ATOM 5036 C CB  . TYR D 2 110 ? 172.034 171.673 236.204 1.00 48.51  ? 110 TYR E CB  1 
ATOM 5037 C CG  . TYR D 2 110 ? 171.728 173.121 236.504 1.00 51.89  ? 110 TYR E CG  1 
ATOM 5038 C CD1 . TYR D 2 110 ? 171.269 173.968 235.502 1.00 52.24  ? 110 TYR E CD1 1 
ATOM 5039 C CD2 . TYR D 2 110 ? 171.845 173.630 237.788 1.00 56.17  ? 110 TYR E CD2 1 
ATOM 5040 C CE1 . TYR D 2 110 ? 170.966 175.289 235.764 1.00 57.12  ? 110 TYR E CE1 1 
ATOM 5041 C CE2 . TYR D 2 110 ? 171.542 174.954 238.059 1.00 60.90  ? 110 TYR E CE2 1 
ATOM 5042 C CZ  . TYR D 2 110 ? 171.104 175.777 237.044 1.00 64.55  ? 110 TYR E CZ  1 
ATOM 5043 O OH  . TYR D 2 110 ? 170.803 177.093 237.311 1.00 67.11  ? 110 TYR E OH  1 
ATOM 5044 N N   . TYR D 2 111 ? 174.898 173.124 236.140 1.00 47.39  ? 111 TYR E N   1 
ATOM 5045 C CA  . TYR D 2 111 ? 176.204 173.612 236.573 1.00 47.04  ? 111 TYR E CA  1 
ATOM 5046 C C   . TYR D 2 111 ? 176.366 173.680 238.088 1.00 49.39  ? 111 TYR E C   1 
ATOM 5047 O O   . TYR D 2 111 ? 177.460 174.021 238.552 1.00 47.29  ? 111 TYR E O   1 
ATOM 5048 C CB  . TYR D 2 111 ? 176.485 174.986 235.952 1.00 48.21  ? 111 TYR E CB  1 
ATOM 5049 C CG  . TYR D 2 111 ? 175.894 176.173 236.682 1.00 46.88  ? 111 TYR E CG  1 
ATOM 5050 C CD1 . TYR D 2 111 ? 174.560 176.517 236.521 1.00 45.02  ? 111 TYR E CD1 1 
ATOM 5051 C CD2 . TYR D 2 111 ? 176.675 176.956 237.523 1.00 47.50  ? 111 TYR E CD2 1 
ATOM 5052 C CE1 . TYR D 2 111 ? 174.019 177.599 237.182 1.00 43.79  ? 111 TYR E CE1 1 
ATOM 5053 C CE2 . TYR D 2 111 ? 176.141 178.040 238.188 1.00 46.85  ? 111 TYR E CE2 1 
ATOM 5054 C CZ  . TYR D 2 111 ? 174.813 178.357 238.013 1.00 48.87  ? 111 TYR E CZ  1 
ATOM 5055 O OH  . TYR D 2 111 ? 174.276 179.436 238.672 1.00 55.96  ? 111 TYR E OH  1 
ATOM 5056 N N   . THR D 2 112 ? 175.317 173.387 238.863 1.00 51.16  ? 112 THR E N   1 
ATOM 5057 C CA  . THR D 2 112 ? 175.450 173.321 240.317 1.00 48.89  ? 112 THR E CA  1 
ATOM 5058 C C   . THR D 2 112 ? 176.414 172.213 240.735 1.00 54.72  ? 112 THR E C   1 
ATOM 5059 O O   . THR D 2 112 ? 177.113 172.347 241.748 1.00 59.15  ? 112 THR E O   1 
ATOM 5060 C CB  . THR D 2 112 ? 174.065 173.136 240.950 1.00 48.69  ? 112 THR E CB  1 
ATOM 5061 O OG1 . THR D 2 112 ? 173.236 174.246 240.593 1.00 53.22  ? 112 THR E OG1 1 
ATOM 5062 C CG2 . THR D 2 112 ? 174.135 173.073 242.472 1.00 50.35  ? 112 THR E CG2 1 
ATOM 5063 N N   . ASP D 2 113 ? 176.496 171.136 239.954 1.00 51.81  ? 113 ASP E N   1 
ATOM 5064 C CA  . ASP D 2 113 ? 177.554 170.146 240.133 1.00 53.28  ? 113 ASP E CA  1 
ATOM 5065 C C   . ASP D 2 113 ? 178.888 170.819 239.837 1.00 58.67  ? 113 ASP E C   1 
ATOM 5066 O O   . ASP D 2 113 ? 179.202 171.119 238.681 1.00 62.80  ? 113 ASP E O   1 
ATOM 5067 C CB  . ASP D 2 113 ? 177.321 168.947 239.218 1.00 60.51  ? 113 ASP E CB  1 
ATOM 5068 C CG  . ASP D 2 113 ? 178.530 168.029 239.130 1.00 69.60  ? 113 ASP E CG  1 
ATOM 5069 O OD1 . ASP D 2 113 ? 179.189 167.796 240.167 1.00 71.57  ? 113 ASP E OD1 1 
ATOM 5070 O OD2 . ASP D 2 113 ? 178.824 167.538 238.020 1.00 67.18  ? 113 ASP E OD2 1 
ATOM 5071 N N   . ASP D 2 114 ? 179.671 171.062 240.885 1.00 59.77  ? 114 ASP E N   1 
ATOM 5072 C CA  . ASP D 2 114 ? 180.826 171.956 240.823 1.00 61.80  ? 114 ASP E CA  1 
ATOM 5073 C C   . ASP D 2 114 ? 182.037 171.154 240.364 1.00 60.73  ? 114 ASP E C   1 
ATOM 5074 O O   . ASP D 2 114 ? 182.824 170.657 241.169 1.00 65.22  ? 114 ASP E O   1 
ATOM 5075 C CB  . ASP D 2 114 ? 181.048 172.602 242.183 1.00 65.73  ? 114 ASP E CB  1 
ATOM 5076 C CG  . ASP D 2 114 ? 179.943 173.573 242.544 1.00 68.42  ? 114 ASP E CG  1 
ATOM 5077 O OD1 . ASP D 2 114 ? 179.349 174.162 241.620 1.00 68.71  ? 114 ASP E OD1 1 
ATOM 5078 O OD2 . ASP D 2 114 ? 179.634 173.715 243.744 1.00 71.27  ? 114 ASP E OD2 1 
ATOM 5079 N N   . ASP D 2 115 ? 182.190 171.030 239.043 1.00 55.03  ? 115 ASP E N   1 
ATOM 5080 C CA  . ASP D 2 115 ? 183.242 170.195 238.477 1.00 53.92  ? 115 ASP E CA  1 
ATOM 5081 C C   . ASP D 2 115 ? 183.908 170.846 237.268 1.00 51.67  ? 115 ASP E C   1 
ATOM 5082 O O   . ASP D 2 115 ? 184.359 170.146 236.355 1.00 52.09  ? 115 ASP E O   1 
ATOM 5083 C CB  . ASP D 2 115 ? 182.695 168.809 238.112 1.00 59.80  ? 115 ASP E CB  1 
ATOM 5084 C CG  . ASP D 2 115 ? 181.626 168.858 237.029 1.00 66.53  ? 115 ASP E CG  1 
ATOM 5085 O OD1 . ASP D 2 115 ? 181.058 169.942 236.778 1.00 67.14  ? 115 ASP E OD1 1 
ATOM 5086 O OD2 . ASP D 2 115 ? 181.352 167.799 236.426 1.00 67.10  ? 115 ASP E OD2 1 
ATOM 5087 N N   . PHE D 2 116 ? 183.974 172.174 237.241 1.00 44.93  ? 116 PHE E N   1 
ATOM 5088 C CA  . PHE D 2 116 ? 184.617 172.868 236.134 1.00 42.35  ? 116 PHE E CA  1 
ATOM 5089 C C   . PHE D 2 116 ? 186.124 172.634 236.157 1.00 49.26  ? 116 PHE E C   1 
ATOM 5090 O O   . PHE D 2 116 ? 186.725 172.400 237.208 1.00 54.96  ? 116 PHE E O   1 
ATOM 5091 C CB  . PHE D 2 116 ? 184.324 174.368 236.189 1.00 38.99  ? 116 PHE E CB  1 
ATOM 5092 C CG  . PHE D 2 116 ? 183.014 174.769 235.559 1.00 38.69  ? 116 PHE E CG  1 
ATOM 5093 C CD1 . PHE D 2 116 ? 181.913 173.929 235.587 1.00 42.25  ? 116 PHE E CD1 1 
ATOM 5094 C CD2 . PHE D 2 116 ? 182.887 176.002 234.942 1.00 40.78  ? 116 PHE E CD2 1 
ATOM 5095 C CE1 . PHE D 2 116 ? 180.718 174.308 235.010 1.00 42.21  ? 116 PHE E CE1 1 
ATOM 5096 C CE2 . PHE D 2 116 ? 181.693 176.385 234.364 1.00 39.18  ? 116 PHE E CE2 1 
ATOM 5097 C CZ  . PHE D 2 116 ? 180.609 175.538 234.401 1.00 35.10  ? 116 PHE E CZ  1 
ATOM 5098 N N   . TYR D 2 117 ? 186.735 172.696 234.973 1.00 46.59  ? 117 TYR E N   1 
ATOM 5099 C CA  . TYR D 2 117 ? 188.154 172.381 234.849 1.00 44.31  ? 117 TYR E CA  1 
ATOM 5100 C C   . TYR D 2 117 ? 189.017 173.561 235.284 1.00 44.29  ? 117 TYR E C   1 
ATOM 5101 O O   . TYR D 2 117 ? 189.817 173.449 236.218 1.00 50.78  ? 117 TYR E O   1 
ATOM 5102 C CB  . TYR D 2 117 ? 188.469 171.969 233.409 1.00 45.07  ? 117 TYR E CB  1 
ATOM 5103 C CG  . TYR D 2 117 ? 189.904 171.562 233.170 1.00 46.76  ? 117 TYR E CG  1 
ATOM 5104 C CD1 . TYR D 2 117 ? 190.371 170.324 233.593 1.00 48.94  ? 117 TYR E CD1 1 
ATOM 5105 C CD2 . TYR D 2 117 ? 190.787 172.404 232.511 1.00 51.37  ? 117 TYR E CD2 1 
ATOM 5106 C CE1 . TYR D 2 117 ? 191.680 169.939 233.374 1.00 52.39  ? 117 TYR E CE1 1 
ATOM 5107 C CE2 . TYR D 2 117 ? 192.101 172.028 232.288 1.00 56.70  ? 117 TYR E CE2 1 
ATOM 5108 C CZ  . TYR D 2 117 ? 192.540 170.795 232.721 1.00 59.52  ? 117 TYR E CZ  1 
ATOM 5109 O OH  . TYR D 2 117 ? 193.844 170.416 232.502 1.00 65.28  ? 117 TYR E OH  1 
ATOM 5110 N N   . TYR D 2 118 ? 188.867 174.701 234.617 1.00 40.86  ? 118 TYR E N   1 
ATOM 5111 C CA  . TYR D 2 118 ? 189.599 175.901 234.991 1.00 44.97  ? 118 TYR E CA  1 
ATOM 5112 C C   . TYR D 2 118 ? 188.938 176.579 236.185 1.00 47.06  ? 118 TYR E C   1 
ATOM 5113 O O   . TYR D 2 118 ? 187.723 176.489 236.378 1.00 48.67  ? 118 TYR E O   1 
ATOM 5114 C CB  . TYR D 2 118 ? 189.671 176.876 233.816 1.00 45.94  ? 118 TYR E CB  1 
ATOM 5115 C CG  . TYR D 2 118 ? 190.272 176.293 232.557 1.00 50.19  ? 118 TYR E CG  1 
ATOM 5116 C CD1 . TYR D 2 118 ? 191.611 175.930 232.506 1.00 52.53  ? 118 TYR E CD1 1 
ATOM 5117 C CD2 . TYR D 2 118 ? 189.501 176.112 231.418 1.00 49.10  ? 118 TYR E CD2 1 
ATOM 5118 C CE1 . TYR D 2 118 ? 192.165 175.401 231.355 1.00 48.23  ? 118 TYR E CE1 1 
ATOM 5119 C CE2 . TYR D 2 118 ? 190.045 175.582 230.264 1.00 46.33  ? 118 TYR E CE2 1 
ATOM 5120 C CZ  . TYR D 2 118 ? 191.377 175.228 230.239 1.00 47.28  ? 118 TYR E CZ  1 
ATOM 5121 O OH  . TYR D 2 118 ? 191.923 174.701 229.093 1.00 55.61  ? 118 TYR E OH  1 
ATOM 5122 N N   . ARG D 2 119 ? 189.750 177.265 236.985 1.00 48.73  ? 119 ARG E N   1 
ATOM 5123 C CA  . ARG D 2 119 ? 189.259 177.983 238.157 1.00 46.22  ? 119 ARG E CA  1 
ATOM 5124 C C   . ARG D 2 119 ? 190.279 179.051 238.537 1.00 51.07  ? 119 ARG E C   1 
ATOM 5125 O O   . ARG D 2 119 ? 191.322 179.199 237.895 1.00 56.04  ? 119 ARG E O   1 
ATOM 5126 C CB  . ARG D 2 119 ? 188.977 177.022 239.313 1.00 45.92  ? 119 ARG E CB  1 
ATOM 5127 C CG  . ARG D 2 119 ? 190.142 176.129 239.690 1.00 49.85  ? 119 ARG E CG  1 
ATOM 5128 C CD  . ARG D 2 119 ? 189.684 175.044 240.645 1.00 49.40  ? 119 ARG E CD  1 
ATOM 5129 N NE  . ARG D 2 119 ? 188.506 174.356 240.133 1.00 50.11  ? 119 ARG E NE  1 
ATOM 5130 C CZ  . ARG D 2 119 ? 187.394 174.153 240.826 1.00 54.44  ? 119 ARG E CZ  1 
ATOM 5131 N NH1 . ARG D 2 119 ? 187.270 174.577 242.073 1.00 57.75  ? 119 ARG E NH1 1 
ATOM 5132 N NH2 . ARG D 2 119 ? 186.380 173.512 240.252 1.00 53.80  ? 119 ARG E NH2 1 
ATOM 5133 N N   . GLY D 2 120 ? 189.968 179.799 239.595 1.00 49.72  ? 120 GLY E N   1 
ATOM 5134 C CA  . GLY D 2 120 ? 190.794 180.927 239.984 1.00 57.24  ? 120 GLY E CA  1 
ATOM 5135 C C   . GLY D 2 120 ? 191.005 181.088 241.476 1.00 61.34  ? 120 GLY E C   1 
ATOM 5136 O O   . GLY D 2 120 ? 190.810 180.142 242.245 1.00 63.02  ? 120 GLY E O   1 
ATOM 5137 N N   . GLN D 2 121 ? 191.407 182.289 241.897 1.00 62.07  ? 121 GLN E N   1 
ATOM 5138 C CA  . GLN D 2 121 ? 191.776 182.567 243.282 1.00 62.06  ? 121 GLN E CA  1 
ATOM 5139 C C   . GLN D 2 121 ? 190.630 183.125 244.116 1.00 65.23  ? 121 GLN E C   1 
ATOM 5140 O O   . GLN D 2 121 ? 190.471 182.731 245.275 1.00 69.45  ? 121 GLN E O   1 
ATOM 5141 C CB  . GLN D 2 121 ? 192.951 183.550 243.330 1.00 66.25  ? 121 GLN E CB  1 
ATOM 5142 C CG  . GLN D 2 121 ? 194.162 183.180 242.475 1.00 71.03  ? 121 GLN E CG  1 
ATOM 5143 C CD  . GLN D 2 121 ? 194.504 181.701 242.520 1.00 72.19  ? 121 GLN E CD  1 
ATOM 5144 O OE1 . GLN D 2 121 ? 194.114 180.931 241.642 1.00 68.14  ? 121 GLN E OE1 1 
ATOM 5145 N NE2 . GLN D 2 121 ? 195.238 181.297 243.550 1.00 76.13  ? 121 GLN E NE2 1 
ATOM 5146 N N   . GLY D 2 122 ? 189.843 184.038 243.571 1.00 62.83  ? 122 GLY E N   1 
ATOM 5147 C CA  . GLY D 2 122 ? 188.711 184.584 244.292 1.00 62.09  ? 122 GLY E CA  1 
ATOM 5148 C C   . GLY D 2 122 ? 188.957 185.997 244.792 1.00 61.71  ? 122 GLY E C   1 
ATOM 5149 O O   . GLY D 2 122 ? 190.089 186.401 245.081 1.00 65.04  ? 122 GLY E O   1 
ATOM 5150 N N   . THR D 2 123 ? 187.873 186.767 244.897 1.00 55.82  ? 123 THR E N   1 
ATOM 5151 C CA  . THR D 2 123 ? 187.910 188.133 245.404 1.00 59.59  ? 123 THR E CA  1 
ATOM 5152 C C   . THR D 2 123 ? 186.835 188.309 246.465 1.00 60.25  ? 123 THR E C   1 
ATOM 5153 O O   . THR D 2 123 ? 185.687 187.902 246.263 1.00 62.14  ? 123 THR E O   1 
ATOM 5154 C CB  . THR D 2 123 ? 187.704 189.159 244.284 1.00 64.15  ? 123 THR E CB  1 
ATOM 5155 O OG1 . THR D 2 123 ? 186.559 188.797 243.503 1.00 62.93  ? 123 THR E OG1 1 
ATOM 5156 C CG2 . THR D 2 123 ? 188.935 189.246 243.395 1.00 62.68  ? 123 THR E CG2 1 
ATOM 5157 N N   . GLN D 2 124 ? 187.208 188.922 247.585 1.00 59.72  ? 124 GLN E N   1 
ATOM 5158 C CA  . GLN D 2 124 ? 186.292 189.100 248.703 1.00 56.62  ? 124 GLN E CA  1 
ATOM 5159 C C   . GLN D 2 124 ? 185.330 190.250 248.435 1.00 62.15  ? 124 GLN E C   1 
ATOM 5160 O O   . GLN D 2 124 ? 185.740 191.330 248.000 1.00 68.88  ? 124 GLN E O   1 
ATOM 5161 C CB  . GLN D 2 124 ? 187.073 189.358 249.991 1.00 55.01  ? 124 GLN E CB  1 
ATOM 5162 C CG  . GLN D 2 124 ? 186.206 189.486 251.233 1.00 53.65  ? 124 GLN E CG  1 
ATOM 5163 C CD  . GLN D 2 124 ? 185.506 188.194 251.594 1.00 62.49  ? 124 GLN E CD  1 
ATOM 5164 O OE1 . GLN D 2 124 ? 186.091 187.114 251.517 1.00 68.28  ? 124 GLN E OE1 1 
ATOM 5165 N NE2 . GLN D 2 124 ? 184.243 188.298 251.991 1.00 64.18  ? 124 GLN E NE2 1 
ATOM 5166 N N   . VAL D 2 125 ? 184.048 190.010 248.696 1.00 57.43  ? 125 VAL E N   1 
ATOM 5167 C CA  . VAL D 2 125 ? 183.008 191.028 248.621 1.00 58.32  ? 125 VAL E CA  1 
ATOM 5168 C C   . VAL D 2 125 ? 182.311 191.072 249.972 1.00 60.62  ? 125 VAL E C   1 
ATOM 5169 O O   . VAL D 2 125 ? 181.761 190.061 250.425 1.00 64.00  ? 125 VAL E O   1 
ATOM 5170 C CB  . VAL D 2 125 ? 182.001 190.738 247.498 1.00 58.39  ? 125 VAL E CB  1 
ATOM 5171 C CG1 . VAL D 2 125 ? 180.879 191.758 247.522 1.00 56.29  ? 125 VAL E CG1 1 
ATOM 5172 C CG2 . VAL D 2 125 ? 182.693 190.736 246.145 1.00 60.75  ? 125 VAL E CG2 1 
ATOM 5173 N N   . THR D 2 126 ? 182.331 192.236 250.614 1.00 61.10  ? 126 THR E N   1 
ATOM 5174 C CA  . THR D 2 126 ? 181.657 192.427 251.888 1.00 59.90  ? 126 THR E CA  1 
ATOM 5175 C C   . THR D 2 126 ? 180.668 193.580 251.782 1.00 60.96  ? 126 THR E C   1 
ATOM 5176 O O   . THR D 2 126 ? 180.869 194.522 251.009 1.00 61.68  ? 126 THR E O   1 
ATOM 5177 C CB  . THR D 2 126 ? 182.661 192.668 253.034 1.00 63.95  ? 126 THR E CB  1 
ATOM 5178 O OG1 . THR D 2 126 ? 181.966 192.681 254.287 1.00 57.72  ? 126 THR E OG1 1 
ATOM 5179 C CG2 . THR D 2 126 ? 183.422 193.976 252.859 1.00 66.54  ? 126 THR E CG2 1 
ATOM 5180 N N   . VAL D 2 127 ? 179.574 193.466 252.530 1.00 58.07  ? 127 VAL E N   1 
ATOM 5181 C CA  . VAL D 2 127 ? 178.537 194.488 252.584 1.00 49.03  ? 127 VAL E CA  1 
ATOM 5182 C C   . VAL D 2 127 ? 177.937 194.498 253.991 1.00 53.49  ? 127 VAL E C   1 
ATOM 5183 O O   . VAL D 2 127 ? 177.444 193.472 254.477 1.00 59.37  ? 127 VAL E O   1 
ATOM 5184 C CB  . VAL D 2 127 ? 177.482 194.305 251.466 1.00 45.24  ? 127 VAL E CB  1 
ATOM 5185 C CG1 . VAL D 2 127 ? 176.710 192.993 251.554 1.00 51.79  ? 127 VAL E CG1 1 
ATOM 5186 C CG2 . VAL D 2 127 ? 176.505 195.460 251.473 1.00 53.40  ? 127 VAL E CG2 1 
ATOM 5187 N N   . SER D 2 128 ? 178.054 195.635 254.670 1.00 54.75  ? 128 SER E N   1 
ATOM 5188 C CA  . SER D 2 128 ? 177.709 195.768 256.084 1.00 58.91  ? 128 SER E CA  1 
ATOM 5189 C C   . SER D 2 128 ? 177.779 197.245 256.451 1.00 58.20  ? 128 SER E C   1 
ATOM 5190 O O   . SER D 2 128 ? 178.072 198.100 255.608 1.00 58.33  ? 128 SER E O   1 
ATOM 5191 C CB  . SER D 2 128 ? 178.643 194.951 256.981 1.00 58.80  ? 128 SER E CB  1 
ATOM 5192 O OG  . SER D 2 128 ? 179.948 195.501 256.988 1.00 55.56  ? 128 SER E OG  1 
ATOM 5193 N N   . SER D 2 129 ? 177.502 197.527 257.725 1.00 58.12  ? 129 SER E N   1 
ATOM 5194 C CA  . SER D 2 129 ? 177.657 198.846 258.347 1.00 59.67  ? 129 SER E CA  1 
ATOM 5195 C C   . SER D 2 129 ? 176.866 199.947 257.646 1.00 65.25  ? 129 SER E C   1 
ATOM 5196 O O   . SER D 2 129 ? 175.902 199.684 256.928 1.00 62.21  ? 129 SER E O   1 
ATOM 5197 C CB  . SER D 2 129 ? 179.141 199.231 258.412 1.00 56.52  ? 129 SER E CB  1 
ATOM 5198 O OG  . SER D 2 129 ? 179.305 200.632 258.544 1.00 52.14  ? 129 SER E OG  1 
# 
