data_8YKH
# 
_entry.id   8YKH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YKH         pdb_00008ykh 10.2210/pdb8ykh/pdb 
WWPDB D_1300041959 ?            ?                   
EMDB  EMD-39372    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'EM metadata'     1 0 2025-03-12 ? 
3 FSC               1 0 2025-03-12 ? 
4 'Half map'        1 0 2025-03-12 1 
5 'Half map'        1 0 2025-03-12 2 
6 Image             1 0 2025-03-12 ? 
7 Mask              1 0 2025-03-12 1 
8 'Primary map'     1 0 2025-03-12 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YKH 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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        'Structure of SARS-CoV-2 spike RBD in complex with NT-108 scFv' 
_pdbx_database_related.db_id          EMD-39372 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              maenaka@pharm.hokudai.ac.jp 
_pdbx_contact_author.name_first         Katsumi 
_pdbx_contact_author.name_last          Maenaka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5459-521X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Anraku, Y.'     1  ? 
'Kita, S.'       2  ? 
'Onodera, T.'    3  ? 
'Tadokoro, T.'   4  ? 
'Ito, S.'        5  ? 
'Adachi, Y.'     6  ? 
'Kotaki, R.'     7  ? 
'Suzuki, T.'     8  ? 
'Hashiguchi, T.' 9  ? 
'Takahashi, Y.'  10 ? 
'Maenaka, K.'    11 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural basis for potent neutralization activity of SARS-CoV-2 antibody, NT-108' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Anraku, Y.'  1 ? 
primary 'Maenaka, K.' 2 ? 
# 
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 'NT-108 scFv'                                                                             26820.643  1 ? ? ? ? 
2 polymer  man 'Spike glycoprotein'                                                                      132754.922 1 ? 
'F817P, A892P, A899P, A942P, K986P, V987P, R682G, R683S, R685G' ? ? 
3 branched man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    1 ? ? ? ? 
# 
_entity_name_com.entity_id   2 
_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 
;EIVLTQSPGTLSLSPGERATLSCRASQSVSSTFLAWYQQKPGQAPRLLIYGASYMATGIPDRFSGSGSGTDFTLTISRLE
PEDFAVYYCQQYGSSLTFGGGTKLEIKGGGGSGGGGSGGGGSQVQLQQSGPGLVKPSQTLSLTCSISGDSVSSNSAAWNW
IRQSPSRGLEWLGRTYYRSKWYNDYAGTVKSRIAINPDTSKNQFSLHLNSVTPEDTAVYFCARVISVAGYAFDIWGQGTM
VTVSSHHHHHH
;
;EIVLTQSPGTLSLSPGERATLSCRASQSVSSTFLAWYQQKPGQAPRLLIYGASYMATGIPDRFSGSGSGTDFTLTISRLE
PEDFAVYYCQQYGSSLTFGGGTKLEIKGGGGSGGGGSGGGGSQVQLQQSGPGLVKPSQTLSLTCSISGDSVSSNSAAWNW
IRQSPSRGLEWLGRTYYRSKWYNDYAGTVKSRIAINPDTSKNQFSLHLNSVTPEDTAVYFCARVISVAGYAFDIWGQGTM
VTVSSHHHHHH
;
A ? 
2 'polypeptide(L)' no no 
;SSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVY
FASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYV
SQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTP
GDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPN
ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIAD
TTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLI
GAEHVNNSYECDIPIGAGICASYQTQTNSPGSAGSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSM
TKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSK
PSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAG
PALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTPSALGKLQDVVNQNAQALNTLVKQLSSNFG
AISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMS
FPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIG
IVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI
;
;SSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVY
FASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYV
SQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTP
GDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPN
ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIAD
TTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLI
GAEHVNNSYECDIPIGAGICASYQTQTNSPGSAGSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSM
TKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSK
PSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAG
PALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTPSALGKLQDVVNQNAQALNTLVKQLSSNFG
AISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMS
FPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIG
IVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    GLU n 
1 2    ILE n 
1 3    VAL n 
1 4    LEU n 
1 5    THR n 
1 6    GLN n 
1 7    SER n 
1 8    PRO n 
1 9    GLY n 
1 10   THR n 
1 11   LEU n 
1 12   SER n 
1 13   LEU n 
1 14   SER n 
1 15   PRO n 
1 16   GLY n 
1 17   GLU n 
1 18   ARG n 
1 19   ALA n 
1 20   THR n 
1 21   LEU n 
1 22   SER n 
1 23   CYS n 
1 24   ARG n 
1 25   ALA n 
1 26   SER n 
1 27   GLN n 
1 28   SER n 
1 29   VAL n 
1 30   SER n 
1 31   SER n 
1 32   THR n 
1 33   PHE n 
1 34   LEU n 
1 35   ALA n 
1 36   TRP n 
1 37   TYR n 
1 38   GLN n 
1 39   GLN n 
1 40   LYS n 
1 41   PRO n 
1 42   GLY n 
1 43   GLN n 
1 44   ALA n 
1 45   PRO n 
1 46   ARG n 
1 47   LEU n 
1 48   LEU n 
1 49   ILE n 
1 50   TYR n 
1 51   GLY n 
1 52   ALA n 
1 53   SER n 
1 54   TYR n 
1 55   MET n 
1 56   ALA n 
1 57   THR n 
1 58   GLY n 
1 59   ILE n 
1 60   PRO n 
1 61   ASP n 
1 62   ARG n 
1 63   PHE n 
1 64   SER n 
1 65   GLY n 
1 66   SER n 
1 67   GLY n 
1 68   SER n 
1 69   GLY n 
1 70   THR n 
1 71   ASP n 
1 72   PHE n 
1 73   THR n 
1 74   LEU n 
1 75   THR n 
1 76   ILE n 
1 77   SER n 
1 78   ARG n 
1 79   LEU n 
1 80   GLU n 
1 81   PRO n 
1 82   GLU n 
1 83   ASP n 
1 84   PHE n 
1 85   ALA n 
1 86   VAL n 
1 87   TYR n 
1 88   TYR n 
1 89   CYS n 
1 90   GLN n 
1 91   GLN n 
1 92   TYR n 
1 93   GLY n 
1 94   SER n 
1 95   SER n 
1 96   LEU n 
1 97   THR n 
1 98   PHE n 
1 99   GLY n 
1 100  GLY n 
1 101  GLY n 
1 102  THR n 
1 103  LYS n 
1 104  LEU n 
1 105  GLU n 
1 106  ILE n 
1 107  LYS n 
1 108  GLY n 
1 109  GLY n 
1 110  GLY n 
1 111  GLY n 
1 112  SER n 
1 113  GLY n 
1 114  GLY n 
1 115  GLY n 
1 116  GLY n 
1 117  SER n 
1 118  GLY n 
1 119  GLY n 
1 120  GLY n 
1 121  GLY n 
1 122  SER n 
1 123  GLN n 
1 124  VAL n 
1 125  GLN n 
1 126  LEU n 
1 127  GLN n 
1 128  GLN n 
1 129  SER n 
1 130  GLY n 
1 131  PRO n 
1 132  GLY n 
1 133  LEU n 
1 134  VAL n 
1 135  LYS n 
1 136  PRO n 
1 137  SER n 
1 138  GLN n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  LEU n 
1 143  THR n 
1 144  CYS n 
1 145  SER n 
1 146  ILE n 
1 147  SER n 
1 148  GLY n 
1 149  ASP n 
1 150  SER n 
1 151  VAL n 
1 152  SER n 
1 153  SER n 
1 154  ASN n 
1 155  SER n 
1 156  ALA n 
1 157  ALA n 
1 158  TRP n 
1 159  ASN n 
1 160  TRP n 
1 161  ILE n 
1 162  ARG n 
1 163  GLN n 
1 164  SER n 
1 165  PRO n 
1 166  SER n 
1 167  ARG n 
1 168  GLY n 
1 169  LEU n 
1 170  GLU n 
1 171  TRP n 
1 172  LEU n 
1 173  GLY n 
1 174  ARG n 
1 175  THR n 
1 176  TYR n 
1 177  TYR n 
1 178  ARG n 
1 179  SER n 
1 180  LYS n 
1 181  TRP n 
1 182  TYR n 
1 183  ASN n 
1 184  ASP n 
1 185  TYR n 
1 186  ALA n 
1 187  GLY n 
1 188  THR n 
1 189  VAL n 
1 190  LYS n 
1 191  SER n 
1 192  ARG n 
1 193  ILE n 
1 194  ALA n 
1 195  ILE n 
1 196  ASN n 
1 197  PRO n 
1 198  ASP n 
1 199  THR n 
1 200  SER n 
1 201  LYS n 
1 202  ASN n 
1 203  GLN n 
1 204  PHE n 
1 205  SER n 
1 206  LEU n 
1 207  HIS n 
1 208  LEU n 
1 209  ASN n 
1 210  SER n 
1 211  VAL n 
1 212  THR n 
1 213  PRO n 
1 214  GLU n 
1 215  ASP n 
1 216  THR n 
1 217  ALA n 
1 218  VAL n 
1 219  TYR n 
1 220  PHE n 
1 221  CYS n 
1 222  ALA n 
1 223  ARG n 
1 224  VAL n 
1 225  ILE n 
1 226  SER n 
1 227  VAL n 
1 228  ALA n 
1 229  GLY n 
1 230  TYR n 
1 231  ALA n 
1 232  PHE n 
1 233  ASP n 
1 234  ILE n 
1 235  TRP n 
1 236  GLY n 
1 237  GLN n 
1 238  GLY n 
1 239  THR n 
1 240  MET n 
1 241  VAL n 
1 242  THR n 
1 243  VAL n 
1 244  SER n 
1 245  SER n 
1 246  HIS n 
1 247  HIS n 
1 248  HIS n 
1 249  HIS n 
1 250  HIS n 
1 251  HIS n 
2 1    SER n 
2 2    SER n 
2 3    GLN n 
2 4    CYS n 
2 5    VAL n 
2 6    ASN n 
2 7    LEU n 
2 8    THR n 
2 9    THR n 
2 10   ARG n 
2 11   THR n 
2 12   GLN n 
2 13   LEU n 
2 14   PRO n 
2 15   PRO n 
2 16   ALA n 
2 17   TYR n 
2 18   THR n 
2 19   ASN n 
2 20   SER n 
2 21   PHE n 
2 22   THR n 
2 23   ARG n 
2 24   GLY n 
2 25   VAL n 
2 26   TYR n 
2 27   TYR n 
2 28   PRO n 
2 29   ASP n 
2 30   LYS n 
2 31   VAL n 
2 32   PHE n 
2 33   ARG n 
2 34   SER n 
2 35   SER n 
2 36   VAL n 
2 37   LEU n 
2 38   HIS n 
2 39   SER n 
2 40   THR n 
2 41   GLN n 
2 42   ASP n 
2 43   LEU n 
2 44   PHE n 
2 45   LEU n 
2 46   PRO n 
2 47   PHE n 
2 48   PHE n 
2 49   SER n 
2 50   ASN n 
2 51   VAL n 
2 52   THR n 
2 53   TRP n 
2 54   PHE n 
2 55   HIS n 
2 56   ALA n 
2 57   ILE n 
2 58   HIS n 
2 59   VAL n 
2 60   SER n 
2 61   GLY n 
2 62   THR n 
2 63   ASN n 
2 64   GLY n 
2 65   THR n 
2 66   LYS n 
2 67   ARG n 
2 68   PHE n 
2 69   ASP n 
2 70   ASN n 
2 71   PRO n 
2 72   VAL n 
2 73   LEU n 
2 74   PRO n 
2 75   PHE n 
2 76   ASN n 
2 77   ASP n 
2 78   GLY n 
2 79   VAL n 
2 80   TYR n 
2 81   PHE n 
2 82   ALA n 
2 83   SER n 
2 84   THR n 
2 85   GLU n 
2 86   LYS n 
2 87   SER n 
2 88   ASN n 
2 89   ILE n 
2 90   ILE n 
2 91   ARG n 
2 92   GLY n 
2 93   TRP n 
2 94   ILE n 
2 95   PHE n 
2 96   GLY n 
2 97   THR n 
2 98   THR n 
2 99   LEU n 
2 100  ASP n 
2 101  SER n 
2 102  LYS n 
2 103  THR n 
2 104  GLN n 
2 105  SER n 
2 106  LEU n 
2 107  LEU n 
2 108  ILE n 
2 109  VAL n 
2 110  ASN n 
2 111  ASN n 
2 112  ALA n 
2 113  THR n 
2 114  ASN n 
2 115  VAL n 
2 116  VAL n 
2 117  ILE n 
2 118  LYS n 
2 119  VAL n 
2 120  CYS n 
2 121  GLU n 
2 122  PHE n 
2 123  GLN n 
2 124  PHE n 
2 125  CYS n 
2 126  ASN n 
2 127  ASP n 
2 128  PRO n 
2 129  PHE n 
2 130  LEU n 
2 131  GLY n 
2 132  VAL n 
2 133  TYR n 
2 134  TYR n 
2 135  HIS n 
2 136  LYS n 
2 137  ASN n 
2 138  ASN n 
2 139  LYS n 
2 140  SER n 
2 141  TRP n 
2 142  MET n 
2 143  GLU n 
2 144  SER n 
2 145  GLU n 
2 146  PHE n 
2 147  ARG n 
2 148  VAL n 
2 149  TYR n 
2 150  SER n 
2 151  SER n 
2 152  ALA n 
2 153  ASN n 
2 154  ASN n 
2 155  CYS n 
2 156  THR n 
2 157  PHE n 
2 158  GLU n 
2 159  TYR n 
2 160  VAL n 
2 161  SER n 
2 162  GLN n 
2 163  PRO n 
2 164  PHE n 
2 165  LEU n 
2 166  MET n 
2 167  ASP n 
2 168  LEU n 
2 169  GLU n 
2 170  GLY n 
2 171  LYS n 
2 172  GLN n 
2 173  GLY n 
2 174  ASN n 
2 175  PHE n 
2 176  LYS n 
2 177  ASN n 
2 178  LEU n 
2 179  ARG n 
2 180  GLU n 
2 181  PHE n 
2 182  VAL n 
2 183  PHE n 
2 184  LYS n 
2 185  ASN n 
2 186  ILE n 
2 187  ASP n 
2 188  GLY n 
2 189  TYR n 
2 190  PHE n 
2 191  LYS n 
2 192  ILE n 
2 193  TYR n 
2 194  SER n 
2 195  LYS n 
2 196  HIS n 
2 197  THR n 
2 198  PRO n 
2 199  ILE n 
2 200  ASN n 
2 201  LEU n 
2 202  VAL n 
2 203  ARG n 
2 204  ASP n 
2 205  LEU n 
2 206  PRO n 
2 207  GLN n 
2 208  GLY n 
2 209  PHE n 
2 210  SER n 
2 211  ALA n 
2 212  LEU n 
2 213  GLU n 
2 214  PRO n 
2 215  LEU n 
2 216  VAL n 
2 217  ASP n 
2 218  LEU n 
2 219  PRO n 
2 220  ILE n 
2 221  GLY n 
2 222  ILE n 
2 223  ASN n 
2 224  ILE n 
2 225  THR n 
2 226  ARG n 
2 227  PHE n 
2 228  GLN n 
2 229  THR n 
2 230  LEU n 
2 231  LEU n 
2 232  ALA n 
2 233  LEU n 
2 234  HIS n 
2 235  ARG n 
2 236  SER n 
2 237  TYR n 
2 238  LEU n 
2 239  THR n 
2 240  PRO n 
2 241  GLY n 
2 242  ASP n 
2 243  SER n 
2 244  SER n 
2 245  SER n 
2 246  GLY n 
2 247  TRP n 
2 248  THR n 
2 249  ALA n 
2 250  GLY n 
2 251  ALA n 
2 252  ALA n 
2 253  ALA n 
2 254  TYR n 
2 255  TYR n 
2 256  VAL n 
2 257  GLY n 
2 258  TYR n 
2 259  LEU n 
2 260  GLN n 
2 261  PRO n 
2 262  ARG n 
2 263  THR n 
2 264  PHE n 
2 265  LEU n 
2 266  LEU n 
2 267  LYS n 
2 268  TYR n 
2 269  ASN n 
2 270  GLU n 
2 271  ASN n 
2 272  GLY n 
2 273  THR n 
2 274  ILE n 
2 275  THR n 
2 276  ASP n 
2 277  ALA n 
2 278  VAL n 
2 279  ASP n 
2 280  CYS n 
2 281  ALA n 
2 282  LEU n 
2 283  ASP n 
2 284  PRO n 
2 285  LEU n 
2 286  SER n 
2 287  GLU n 
2 288  THR n 
2 289  LYS n 
2 290  CYS n 
2 291  THR n 
2 292  LEU n 
2 293  LYS n 
2 294  SER n 
2 295  PHE n 
2 296  THR n 
2 297  VAL n 
2 298  GLU n 
2 299  LYS n 
2 300  GLY n 
2 301  ILE n 
2 302  TYR n 
2 303  GLN n 
2 304  THR n 
2 305  SER n 
2 306  ASN n 
2 307  PHE n 
2 308  ARG n 
2 309  VAL n 
2 310  GLN n 
2 311  PRO n 
2 312  THR n 
2 313  GLU n 
2 314  SER n 
2 315  ILE n 
2 316  VAL n 
2 317  ARG n 
2 318  PHE n 
2 319  PRO n 
2 320  ASN n 
2 321  ILE n 
2 322  THR n 
2 323  ASN n 
2 324  LEU n 
2 325  CYS n 
2 326  PRO n 
2 327  PHE n 
2 328  GLY n 
2 329  GLU n 
2 330  VAL n 
2 331  PHE n 
2 332  ASN n 
2 333  ALA n 
2 334  THR n 
2 335  ARG n 
2 336  PHE n 
2 337  ALA n 
2 338  SER n 
2 339  VAL n 
2 340  TYR n 
2 341  ALA n 
2 342  TRP n 
2 343  ASN n 
2 344  ARG n 
2 345  LYS n 
2 346  ARG n 
2 347  ILE n 
2 348  SER n 
2 349  ASN n 
2 350  CYS n 
2 351  VAL n 
2 352  ALA n 
2 353  ASP n 
2 354  TYR n 
2 355  SER n 
2 356  VAL n 
2 357  LEU n 
2 358  TYR n 
2 359  ASN n 
2 360  SER n 
2 361  ALA n 
2 362  SER n 
2 363  PHE n 
2 364  SER n 
2 365  THR n 
2 366  PHE n 
2 367  LYS n 
2 368  CYS n 
2 369  TYR n 
2 370  GLY n 
2 371  VAL n 
2 372  SER n 
2 373  PRO n 
2 374  THR n 
2 375  LYS n 
2 376  LEU n 
2 377  ASN n 
2 378  ASP n 
2 379  LEU n 
2 380  CYS n 
2 381  PHE n 
2 382  THR n 
2 383  ASN n 
2 384  VAL n 
2 385  TYR n 
2 386  ALA n 
2 387  ASP n 
2 388  SER n 
2 389  PHE n 
2 390  VAL n 
2 391  ILE n 
2 392  ARG n 
2 393  GLY n 
2 394  ASP n 
2 395  GLU n 
2 396  VAL n 
2 397  ARG n 
2 398  GLN n 
2 399  ILE n 
2 400  ALA n 
2 401  PRO n 
2 402  GLY n 
2 403  GLN n 
2 404  THR n 
2 405  GLY n 
2 406  LYS n 
2 407  ILE n 
2 408  ALA n 
2 409  ASP n 
2 410  TYR n 
2 411  ASN n 
2 412  TYR n 
2 413  LYS n 
2 414  LEU n 
2 415  PRO n 
2 416  ASP n 
2 417  ASP n 
2 418  PHE n 
2 419  THR n 
2 420  GLY n 
2 421  CYS n 
2 422  VAL n 
2 423  ILE n 
2 424  ALA n 
2 425  TRP n 
2 426  ASN n 
2 427  SER n 
2 428  ASN n 
2 429  ASN n 
2 430  LEU n 
2 431  ASP n 
2 432  SER n 
2 433  LYS n 
2 434  VAL n 
2 435  GLY n 
2 436  GLY n 
2 437  ASN n 
2 438  TYR n 
2 439  ASN n 
2 440  TYR n 
2 441  LEU n 
2 442  TYR n 
2 443  ARG n 
2 444  LEU n 
2 445  PHE n 
2 446  ARG n 
2 447  LYS n 
2 448  SER n 
2 449  ASN n 
2 450  LEU n 
2 451  LYS n 
2 452  PRO n 
2 453  PHE n 
2 454  GLU n 
2 455  ARG n 
2 456  ASP n 
2 457  ILE n 
2 458  SER n 
2 459  THR n 
2 460  GLU n 
2 461  ILE n 
2 462  TYR n 
2 463  GLN n 
2 464  ALA n 
2 465  GLY n 
2 466  SER n 
2 467  THR n 
2 468  PRO n 
2 469  CYS n 
2 470  ASN n 
2 471  GLY n 
2 472  VAL n 
2 473  GLU n 
2 474  GLY n 
2 475  PHE n 
2 476  ASN n 
2 477  CYS n 
2 478  TYR n 
2 479  PHE n 
2 480  PRO n 
2 481  LEU n 
2 482  GLN n 
2 483  SER n 
2 484  TYR n 
2 485  GLY n 
2 486  PHE n 
2 487  GLN n 
2 488  PRO n 
2 489  THR n 
2 490  ASN n 
2 491  GLY n 
2 492  VAL n 
2 493  GLY n 
2 494  TYR n 
2 495  GLN n 
2 496  PRO n 
2 497  TYR n 
2 498  ARG n 
2 499  VAL n 
2 500  VAL n 
2 501  VAL n 
2 502  LEU n 
2 503  SER n 
2 504  PHE n 
2 505  GLU n 
2 506  LEU n 
2 507  LEU n 
2 508  HIS n 
2 509  ALA n 
2 510  PRO n 
2 511  ALA n 
2 512  THR n 
2 513  VAL n 
2 514  CYS n 
2 515  GLY n 
2 516  PRO n 
2 517  LYS n 
2 518  LYS n 
2 519  SER n 
2 520  THR n 
2 521  ASN n 
2 522  LEU n 
2 523  VAL n 
2 524  LYS n 
2 525  ASN n 
2 526  LYS n 
2 527  CYS n 
2 528  VAL n 
2 529  ASN n 
2 530  PHE n 
2 531  ASN n 
2 532  PHE n 
2 533  ASN n 
2 534  GLY n 
2 535  LEU n 
2 536  THR n 
2 537  GLY n 
2 538  THR n 
2 539  GLY n 
2 540  VAL n 
2 541  LEU n 
2 542  THR n 
2 543  GLU n 
2 544  SER n 
2 545  ASN n 
2 546  LYS n 
2 547  LYS n 
2 548  PHE n 
2 549  LEU n 
2 550  PRO n 
2 551  PHE n 
2 552  GLN n 
2 553  GLN n 
2 554  PHE n 
2 555  GLY n 
2 556  ARG n 
2 557  ASP n 
2 558  ILE n 
2 559  ALA n 
2 560  ASP n 
2 561  THR n 
2 562  THR n 
2 563  ASP n 
2 564  ALA n 
2 565  VAL n 
2 566  ARG n 
2 567  ASP n 
2 568  PRO n 
2 569  GLN n 
2 570  THR n 
2 571  LEU n 
2 572  GLU n 
2 573  ILE n 
2 574  LEU n 
2 575  ASP n 
2 576  ILE n 
2 577  THR n 
2 578  PRO n 
2 579  CYS n 
2 580  SER n 
2 581  PHE n 
2 582  GLY n 
2 583  GLY n 
2 584  VAL n 
2 585  SER n 
2 586  VAL n 
2 587  ILE n 
2 588  THR n 
2 589  PRO n 
2 590  GLY n 
2 591  THR n 
2 592  ASN n 
2 593  THR n 
2 594  SER n 
2 595  ASN n 
2 596  GLN n 
2 597  VAL n 
2 598  ALA n 
2 599  VAL n 
2 600  LEU n 
2 601  TYR n 
2 602  GLN n 
2 603  ASP n 
2 604  VAL n 
2 605  ASN n 
2 606  CYS n 
2 607  THR n 
2 608  GLU n 
2 609  VAL n 
2 610  PRO n 
2 611  VAL n 
2 612  ALA n 
2 613  ILE n 
2 614  HIS n 
2 615  ALA n 
2 616  ASP n 
2 617  GLN n 
2 618  LEU n 
2 619  THR n 
2 620  PRO n 
2 621  THR n 
2 622  TRP n 
2 623  ARG n 
2 624  VAL n 
2 625  TYR n 
2 626  SER n 
2 627  THR n 
2 628  GLY n 
2 629  SER n 
2 630  ASN n 
2 631  VAL n 
2 632  PHE n 
2 633  GLN n 
2 634  THR n 
2 635  ARG n 
2 636  ALA n 
2 637  GLY n 
2 638  CYS n 
2 639  LEU n 
2 640  ILE n 
2 641  GLY n 
2 642  ALA n 
2 643  GLU n 
2 644  HIS n 
2 645  VAL n 
2 646  ASN n 
2 647  ASN n 
2 648  SER n 
2 649  TYR n 
2 650  GLU n 
2 651  CYS n 
2 652  ASP n 
2 653  ILE n 
2 654  PRO n 
2 655  ILE n 
2 656  GLY n 
2 657  ALA n 
2 658  GLY n 
2 659  ILE n 
2 660  CYS n 
2 661  ALA n 
2 662  SER n 
2 663  TYR n 
2 664  GLN n 
2 665  THR n 
2 666  GLN n 
2 667  THR n 
2 668  ASN n 
2 669  SER n 
2 670  PRO n 
2 671  GLY n 
2 672  SER n 
2 673  ALA n 
2 674  GLY n 
2 675  SER n 
2 676  VAL n 
2 677  ALA n 
2 678  SER n 
2 679  GLN n 
2 680  SER n 
2 681  ILE n 
2 682  ILE n 
2 683  ALA n 
2 684  TYR n 
2 685  THR n 
2 686  MET n 
2 687  SER n 
2 688  LEU n 
2 689  GLY n 
2 690  ALA n 
2 691  GLU n 
2 692  ASN n 
2 693  SER n 
2 694  VAL n 
2 695  ALA n 
2 696  TYR n 
2 697  SER n 
2 698  ASN n 
2 699  ASN n 
2 700  SER n 
2 701  ILE n 
2 702  ALA n 
2 703  ILE n 
2 704  PRO n 
2 705  THR n 
2 706  ASN n 
2 707  PHE n 
2 708  THR n 
2 709  ILE n 
2 710  SER n 
2 711  VAL n 
2 712  THR n 
2 713  THR n 
2 714  GLU n 
2 715  ILE n 
2 716  LEU n 
2 717  PRO n 
2 718  VAL n 
2 719  SER n 
2 720  MET n 
2 721  THR n 
2 722  LYS n 
2 723  THR n 
2 724  SER n 
2 725  VAL n 
2 726  ASP n 
2 727  CYS n 
2 728  THR n 
2 729  MET n 
2 730  TYR n 
2 731  ILE n 
2 732  CYS n 
2 733  GLY n 
2 734  ASP n 
2 735  SER n 
2 736  THR n 
2 737  GLU n 
2 738  CYS n 
2 739  SER n 
2 740  ASN n 
2 741  LEU n 
2 742  LEU n 
2 743  LEU n 
2 744  GLN n 
2 745  TYR n 
2 746  GLY n 
2 747  SER n 
2 748  PHE n 
2 749  CYS n 
2 750  THR n 
2 751  GLN n 
2 752  LEU n 
2 753  ASN n 
2 754  ARG n 
2 755  ALA n 
2 756  LEU n 
2 757  THR n 
2 758  GLY n 
2 759  ILE n 
2 760  ALA n 
2 761  VAL n 
2 762  GLU n 
2 763  GLN n 
2 764  ASP n 
2 765  LYS n 
2 766  ASN n 
2 767  THR n 
2 768  GLN n 
2 769  GLU n 
2 770  VAL n 
2 771  PHE n 
2 772  ALA n 
2 773  GLN n 
2 774  VAL n 
2 775  LYS n 
2 776  GLN n 
2 777  ILE n 
2 778  TYR n 
2 779  LYS n 
2 780  THR n 
2 781  PRO n 
2 782  PRO n 
2 783  ILE n 
2 784  LYS n 
2 785  ASP n 
2 786  PHE n 
2 787  GLY n 
2 788  GLY n 
2 789  PHE n 
2 790  ASN n 
2 791  PHE n 
2 792  SER n 
2 793  GLN n 
2 794  ILE n 
2 795  LEU n 
2 796  PRO n 
2 797  ASP n 
2 798  PRO n 
2 799  SER n 
2 800  LYS n 
2 801  PRO n 
2 802  SER n 
2 803  LYS n 
2 804  ARG n 
2 805  SER n 
2 806  PRO n 
2 807  ILE n 
2 808  GLU n 
2 809  ASP n 
2 810  LEU n 
2 811  LEU n 
2 812  PHE n 
2 813  ASN n 
2 814  LYS n 
2 815  VAL n 
2 816  THR n 
2 817  LEU n 
2 818  ALA n 
2 819  ASP n 
2 820  ALA n 
2 821  GLY n 
2 822  PHE n 
2 823  ILE n 
2 824  LYS n 
2 825  GLN n 
2 826  TYR n 
2 827  GLY n 
2 828  ASP n 
2 829  CYS n 
2 830  LEU n 
2 831  GLY n 
2 832  ASP n 
2 833  ILE n 
2 834  ALA n 
2 835  ALA n 
2 836  ARG n 
2 837  ASP n 
2 838  LEU n 
2 839  ILE n 
2 840  CYS n 
2 841  ALA n 
2 842  GLN n 
2 843  LYS n 
2 844  PHE n 
2 845  ASN n 
2 846  GLY n 
2 847  LEU n 
2 848  THR n 
2 849  VAL n 
2 850  LEU n 
2 851  PRO n 
2 852  PRO n 
2 853  LEU n 
2 854  LEU n 
2 855  THR n 
2 856  ASP n 
2 857  GLU n 
2 858  MET n 
2 859  ILE n 
2 860  ALA n 
2 861  GLN n 
2 862  TYR n 
2 863  THR n 
2 864  SER n 
2 865  ALA n 
2 866  LEU n 
2 867  LEU n 
2 868  ALA n 
2 869  GLY n 
2 870  THR n 
2 871  ILE n 
2 872  THR n 
2 873  SER n 
2 874  GLY n 
2 875  TRP n 
2 876  THR n 
2 877  PHE n 
2 878  GLY n 
2 879  ALA n 
2 880  GLY n 
2 881  PRO n 
2 882  ALA n 
2 883  LEU n 
2 884  GLN n 
2 885  ILE n 
2 886  PRO n 
2 887  PHE n 
2 888  PRO n 
2 889  MET n 
2 890  GLN n 
2 891  MET n 
2 892  ALA n 
2 893  TYR n 
2 894  ARG n 
2 895  PHE n 
2 896  ASN n 
2 897  GLY n 
2 898  ILE n 
2 899  GLY n 
2 900  VAL n 
2 901  THR n 
2 902  GLN n 
2 903  ASN n 
2 904  VAL n 
2 905  LEU n 
2 906  TYR n 
2 907  GLU n 
2 908  ASN n 
2 909  GLN n 
2 910  LYS n 
2 911  LEU n 
2 912  ILE n 
2 913  ALA n 
2 914  ASN n 
2 915  GLN n 
2 916  PHE n 
2 917  ASN n 
2 918  SER n 
2 919  ALA n 
2 920  ILE n 
2 921  GLY n 
2 922  LYS n 
2 923  ILE n 
2 924  GLN n 
2 925  ASP n 
2 926  SER n 
2 927  LEU n 
2 928  SER n 
2 929  SER n 
2 930  THR n 
2 931  PRO n 
2 932  SER n 
2 933  ALA n 
2 934  LEU n 
2 935  GLY n 
2 936  LYS n 
2 937  LEU n 
2 938  GLN n 
2 939  ASP n 
2 940  VAL n 
2 941  VAL n 
2 942  ASN n 
2 943  GLN n 
2 944  ASN n 
2 945  ALA n 
2 946  GLN n 
2 947  ALA n 
2 948  LEU n 
2 949  ASN n 
2 950  THR n 
2 951  LEU n 
2 952  VAL n 
2 953  LYS n 
2 954  GLN n 
2 955  LEU n 
2 956  SER n 
2 957  SER n 
2 958  ASN n 
2 959  PHE n 
2 960  GLY n 
2 961  ALA n 
2 962  ILE n 
2 963  SER n 
2 964  SER n 
2 965  VAL n 
2 966  LEU n 
2 967  ASN n 
2 968  ASP n 
2 969  ILE n 
2 970  LEU n 
2 971  SER n 
2 972  ARG n 
2 973  LEU n 
2 974  ASP n 
2 975  PRO n 
2 976  PRO n 
2 977  GLU n 
2 978  ALA n 
2 979  GLU n 
2 980  VAL n 
2 981  GLN n 
2 982  ILE n 
2 983  ASP n 
2 984  ARG n 
2 985  LEU n 
2 986  ILE n 
2 987  THR n 
2 988  GLY n 
2 989  ARG n 
2 990  LEU n 
2 991  GLN n 
2 992  SER n 
2 993  LEU n 
2 994  GLN n 
2 995  THR n 
2 996  TYR n 
2 997  VAL n 
2 998  THR n 
2 999  GLN n 
2 1000 GLN n 
2 1001 LEU n 
2 1002 ILE n 
2 1003 ARG n 
2 1004 ALA n 
2 1005 ALA n 
2 1006 GLU n 
2 1007 ILE n 
2 1008 ARG n 
2 1009 ALA n 
2 1010 SER n 
2 1011 ALA n 
2 1012 ASN n 
2 1013 LEU n 
2 1014 ALA n 
2 1015 ALA n 
2 1016 THR n 
2 1017 LYS n 
2 1018 MET n 
2 1019 SER n 
2 1020 GLU n 
2 1021 CYS n 
2 1022 VAL n 
2 1023 LEU n 
2 1024 GLY n 
2 1025 GLN n 
2 1026 SER n 
2 1027 LYS n 
2 1028 ARG n 
2 1029 VAL n 
2 1030 ASP n 
2 1031 PHE n 
2 1032 CYS n 
2 1033 GLY n 
2 1034 LYS n 
2 1035 GLY n 
2 1036 TYR n 
2 1037 HIS n 
2 1038 LEU n 
2 1039 MET n 
2 1040 SER n 
2 1041 PHE n 
2 1042 PRO n 
2 1043 GLN n 
2 1044 SER n 
2 1045 ALA n 
2 1046 PRO n 
2 1047 HIS n 
2 1048 GLY n 
2 1049 VAL n 
2 1050 VAL n 
2 1051 PHE n 
2 1052 LEU n 
2 1053 HIS n 
2 1054 VAL n 
2 1055 THR n 
2 1056 TYR n 
2 1057 VAL n 
2 1058 PRO n 
2 1059 ALA n 
2 1060 GLN n 
2 1061 GLU n 
2 1062 LYS n 
2 1063 ASN n 
2 1064 PHE n 
2 1065 THR n 
2 1066 THR n 
2 1067 ALA n 
2 1068 PRO n 
2 1069 ALA n 
2 1070 ILE n 
2 1071 CYS n 
2 1072 HIS n 
2 1073 ASP n 
2 1074 GLY n 
2 1075 LYS n 
2 1076 ALA n 
2 1077 HIS n 
2 1078 PHE n 
2 1079 PRO n 
2 1080 ARG n 
2 1081 GLU n 
2 1082 GLY n 
2 1083 VAL n 
2 1084 PHE n 
2 1085 VAL n 
2 1086 SER n 
2 1087 ASN n 
2 1088 GLY n 
2 1089 THR n 
2 1090 HIS n 
2 1091 TRP n 
2 1092 PHE n 
2 1093 VAL n 
2 1094 THR n 
2 1095 GLN n 
2 1096 ARG n 
2 1097 ASN n 
2 1098 PHE n 
2 1099 TYR n 
2 1100 GLU n 
2 1101 PRO n 
2 1102 GLN n 
2 1103 ILE n 
2 1104 ILE n 
2 1105 THR n 
2 1106 THR n 
2 1107 ASP n 
2 1108 ASN n 
2 1109 THR n 
2 1110 PHE n 
2 1111 VAL n 
2 1112 SER n 
2 1113 GLY n 
2 1114 ASN n 
2 1115 CYS n 
2 1116 ASP n 
2 1117 VAL n 
2 1118 VAL n 
2 1119 ILE n 
2 1120 GLY n 
2 1121 ILE n 
2 1122 VAL n 
2 1123 ASN n 
2 1124 ASN n 
2 1125 THR n 
2 1126 VAL n 
2 1127 TYR n 
2 1128 ASP n 
2 1129 PRO n 
2 1130 LEU n 
2 1131 GLN n 
2 1132 PRO n 
2 1133 GLU n 
2 1134 LEU n 
2 1135 ASP n 
2 1136 SER n 
2 1137 PHE n 
2 1138 LYS n 
2 1139 GLU n 
2 1140 GLU n 
2 1141 LEU n 
2 1142 ASP n 
2 1143 LYS n 
2 1144 TYR n 
2 1145 PHE n 
2 1146 LYS n 
2 1147 ASN n 
2 1148 HIS n 
2 1149 THR n 
2 1150 SER n 
2 1151 PRO n 
2 1152 ASP n 
2 1153 VAL n 
2 1154 ASP n 
2 1155 LEU n 
2 1156 GLY n 
2 1157 ASP n 
2 1158 ILE n 
2 1159 SER n 
2 1160 GLY n 
2 1161 ILE n 
2 1162 ASN n 
2 1163 ALA n 
2 1164 SER n 
2 1165 VAL n 
2 1166 VAL n 
2 1167 ASN n 
2 1168 ILE n 
2 1169 GLN n 
2 1170 LYS n 
2 1171 GLU n 
2 1172 ILE n 
2 1173 ASP n 
2 1174 ARG n 
2 1175 LEU n 
2 1176 ASN n 
2 1177 GLU n 
2 1178 VAL n 
2 1179 ALA n 
2 1180 LYS n 
2 1181 ASN n 
2 1182 LEU n 
2 1183 ASN n 
2 1184 GLU n 
2 1185 SER n 
2 1186 LEU n 
2 1187 ILE n 
2 1188 ASP n 
2 1189 LEU n 
2 1190 GLN n 
2 1191 GLU n 
2 1192 LEU n 
2 1193 GLY n 
2 1194 LYS n 
2 1195 TYR n 
2 1196 GLU n 
2 1197 GLN n 
2 1198 TYR n 
2 1199 ILE 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' 1 251  ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 1199 ? ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_branch.entity_id   3 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 DGlcpNAcb1-4DGlcpNAcb1-ROH                            'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'       LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  3 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  NAG 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  NAG 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    GLU 1    0    ?   ?   ?   A . n 
A 1 2    ILE 2    1    1   ILE ILE A . n 
A 1 3    VAL 3    2    2   VAL VAL A . n 
A 1 4    LEU 4    3    3   LEU LEU A . n 
A 1 5    THR 5    4    4   THR THR A . n 
A 1 6    GLN 6    5    5   GLN GLN A . n 
A 1 7    SER 7    6    6   SER SER A . n 
A 1 8    PRO 8    7    7   PRO PRO A . n 
A 1 9    GLY 9    8    8   GLY GLY A . n 
A 1 10   THR 10   9    9   THR THR A . n 
A 1 11   LEU 11   10   10  LEU LEU A . n 
A 1 12   SER 12   11   11  SER SER A . n 
A 1 13   LEU 13   12   12  LEU LEU A . n 
A 1 14   SER 14   13   13  SER SER A . n 
A 1 15   PRO 15   14   14  PRO PRO A . n 
A 1 16   GLY 16   15   15  GLY GLY A . n 
A 1 17   GLU 17   16   16  GLU GLU A . n 
A 1 18   ARG 18   17   17  ARG ARG A . n 
A 1 19   ALA 19   18   18  ALA ALA A . n 
A 1 20   THR 20   19   19  THR THR A . n 
A 1 21   LEU 21   20   20  LEU LEU A . n 
A 1 22   SER 22   21   21  SER SER A . n 
A 1 23   CYS 23   22   22  CYS CYS A . n 
A 1 24   ARG 24   23   23  ARG ARG A . n 
A 1 25   ALA 25   24   24  ALA ALA A . n 
A 1 26   SER 26   25   25  SER SER A . n 
A 1 27   GLN 27   26   26  GLN GLN A . n 
A 1 28   SER 28   27   27  SER SER A . n 
A 1 29   VAL 29   28   28  VAL VAL A . n 
A 1 30   SER 30   29   29  SER SER A . n 
A 1 31   SER 31   30   30  SER SER A . n 
A 1 32   THR 32   31   31  THR THR A . n 
A 1 33   PHE 33   32   32  PHE PHE A . n 
A 1 34   LEU 34   33   33  LEU LEU A . n 
A 1 35   ALA 35   34   34  ALA ALA A . n 
A 1 36   TRP 36   35   35  TRP TRP A . n 
A 1 37   TYR 37   36   36  TYR TYR A . n 
A 1 38   GLN 38   37   37  GLN GLN A . n 
A 1 39   GLN 39   38   38  GLN GLN A . n 
A 1 40   LYS 40   39   39  LYS LYS A . n 
A 1 41   PRO 41   40   40  PRO PRO A . n 
A 1 42   GLY 42   41   41  GLY GLY A . n 
A 1 43   GLN 43   42   42  GLN GLN A . n 
A 1 44   ALA 44   43   43  ALA ALA A . n 
A 1 45   PRO 45   44   44  PRO PRO A . n 
A 1 46   ARG 46   45   45  ARG ARG A . n 
A 1 47   LEU 47   46   46  LEU LEU A . n 
A 1 48   LEU 48   47   47  LEU LEU A . n 
A 1 49   ILE 49   48   48  ILE ILE A . n 
A 1 50   TYR 50   49   49  TYR TYR A . n 
A 1 51   GLY 51   50   50  GLY GLY A . n 
A 1 52   ALA 52   51   51  ALA ALA A . n 
A 1 53   SER 53   52   52  SER SER A . n 
A 1 54   TYR 54   53   53  TYR TYR A . n 
A 1 55   MET 55   54   54  MET MET A . n 
A 1 56   ALA 56   55   55  ALA ALA A . n 
A 1 57   THR 57   56   56  THR THR A . n 
A 1 58   GLY 58   57   57  GLY GLY A . n 
A 1 59   ILE 59   58   58  ILE ILE A . n 
A 1 60   PRO 60   59   59  PRO PRO A . n 
A 1 61   ASP 61   60   60  ASP ASP A . n 
A 1 62   ARG 62   61   61  ARG ARG A . n 
A 1 63   PHE 63   62   62  PHE PHE A . n 
A 1 64   SER 64   63   63  SER SER A . n 
A 1 65   GLY 65   64   64  GLY GLY A . n 
A 1 66   SER 66   65   65  SER SER A . n 
A 1 67   GLY 67   66   66  GLY GLY A . n 
A 1 68   SER 68   67   67  SER SER A . n 
A 1 69   GLY 69   68   68  GLY GLY A . n 
A 1 70   THR 70   69   69  THR THR A . n 
A 1 71   ASP 71   70   70  ASP ASP A . n 
A 1 72   PHE 72   71   71  PHE PHE A . n 
A 1 73   THR 73   72   72  THR THR A . n 
A 1 74   LEU 74   73   73  LEU LEU A . n 
A 1 75   THR 75   74   74  THR THR A . n 
A 1 76   ILE 76   75   75  ILE ILE A . n 
A 1 77   SER 77   76   76  SER SER A . n 
A 1 78   ARG 78   77   77  ARG ARG A . n 
A 1 79   LEU 79   78   78  LEU LEU A . n 
A 1 80   GLU 80   79   79  GLU GLU A . n 
A 1 81   PRO 81   80   80  PRO PRO A . n 
A 1 82   GLU 82   81   81  GLU GLU A . n 
A 1 83   ASP 83   82   82  ASP ASP A . n 
A 1 84   PHE 84   83   83  PHE PHE A . n 
A 1 85   ALA 85   84   84  ALA ALA A . n 
A 1 86   VAL 86   85   85  VAL VAL A . n 
A 1 87   TYR 87   86   86  TYR TYR A . n 
A 1 88   TYR 88   87   87  TYR TYR A . n 
A 1 89   CYS 89   88   88  CYS CYS A . n 
A 1 90   GLN 90   89   89  GLN GLN A . n 
A 1 91   GLN 91   90   90  GLN GLN A . n 
A 1 92   TYR 92   91   91  TYR TYR A . n 
A 1 93   GLY 93   92   92  GLY GLY A . n 
A 1 94   SER 94   93   93  SER SER A . n 
A 1 95   SER 95   94   94  SER SER A . n 
A 1 96   LEU 96   95   95  LEU LEU A . n 
A 1 97   THR 97   96   96  THR THR A . n 
A 1 98   PHE 98   97   97  PHE PHE A . n 
A 1 99   GLY 99   98   98  GLY GLY A . n 
A 1 100  GLY 100  99   99  GLY GLY A . n 
A 1 101  GLY 101  100  100 GLY GLY A . n 
A 1 102  THR 102  101  101 THR THR A . n 
A 1 103  LYS 103  102  102 LYS LYS A . n 
A 1 104  LEU 104  103  103 LEU LEU A . n 
A 1 105  GLU 105  104  104 GLU GLU A . n 
A 1 106  ILE 106  105  105 ILE ILE A . n 
A 1 107  LYS 107  106  106 LYS LYS A . n 
A 1 108  GLY 108  107  ?   ?   ?   A . n 
A 1 109  GLY 109  108  ?   ?   ?   A . n 
A 1 110  GLY 110  109  ?   ?   ?   A . n 
A 1 111  GLY 111  110  ?   ?   ?   A . n 
A 1 112  SER 112  111  ?   ?   ?   A . n 
A 1 113  GLY 113  112  ?   ?   ?   A . n 
A 1 114  GLY 114  113  ?   ?   ?   A . n 
A 1 115  GLY 115  114  ?   ?   ?   A . n 
A 1 116  GLY 116  115  ?   ?   ?   A . n 
A 1 117  SER 117  116  ?   ?   ?   A . n 
A 1 118  GLY 118  117  ?   ?   ?   A . n 
A 1 119  GLY 119  118  ?   ?   ?   A . n 
A 1 120  GLY 120  119  ?   ?   ?   A . n 
A 1 121  GLY 121  120  ?   ?   ?   A . n 
A 1 122  SER 122  121  121 SER SER A . n 
A 1 123  GLN 123  122  122 GLN GLN A . n 
A 1 124  VAL 124  123  123 VAL VAL A . n 
A 1 125  GLN 125  124  124 GLN GLN A . n 
A 1 126  LEU 126  125  125 LEU LEU A . n 
A 1 127  GLN 127  126  126 GLN GLN A . n 
A 1 128  GLN 128  127  127 GLN GLN A . n 
A 1 129  SER 129  128  128 SER SER A . n 
A 1 130  GLY 130  129  129 GLY GLY A . n 
A 1 131  PRO 131  130  130 PRO PRO A . n 
A 1 132  GLY 132  131  131 GLY GLY A . n 
A 1 133  LEU 133  132  132 LEU LEU A . n 
A 1 134  VAL 134  133  133 VAL VAL A . n 
A 1 135  LYS 135  134  134 LYS LYS A . n 
A 1 136  PRO 136  135  135 PRO PRO A . n 
A 1 137  SER 137  136  136 SER SER A . n 
A 1 138  GLN 138  137  137 GLN GLN A . n 
A 1 139  THR 139  138  138 THR THR A . n 
A 1 140  LEU 140  139  139 LEU LEU A . n 
A 1 141  SER 141  140  140 SER SER A . n 
A 1 142  LEU 142  141  141 LEU LEU A . n 
A 1 143  THR 143  142  142 THR THR A . n 
A 1 144  CYS 144  143  143 CYS CYS A . n 
A 1 145  SER 145  144  144 SER SER A . n 
A 1 146  ILE 146  145  145 ILE ILE A . n 
A 1 147  SER 147  146  146 SER SER A . n 
A 1 148  GLY 148  147  147 GLY GLY A . n 
A 1 149  ASP 149  148  148 ASP ASP A . n 
A 1 150  SER 150  149  149 SER SER A . n 
A 1 151  VAL 151  150  150 VAL VAL A . n 
A 1 152  SER 152  151  151 SER SER A . n 
A 1 153  SER 153  152  152 SER SER A . n 
A 1 154  ASN 154  153  153 ASN ASN A . n 
A 1 155  SER 155  154  154 SER SER A . n 
A 1 156  ALA 156  155  155 ALA ALA A . n 
A 1 157  ALA 157  156  156 ALA ALA A . n 
A 1 158  TRP 158  157  157 TRP TRP A . n 
A 1 159  ASN 159  158  158 ASN ASN A . n 
A 1 160  TRP 160  159  159 TRP TRP A . n 
A 1 161  ILE 161  160  160 ILE ILE A . n 
A 1 162  ARG 162  161  161 ARG ARG A . n 
A 1 163  GLN 163  162  162 GLN GLN A . n 
A 1 164  SER 164  163  163 SER SER A . n 
A 1 165  PRO 165  164  164 PRO PRO A . n 
A 1 166  SER 166  165  165 SER SER A . n 
A 1 167  ARG 167  166  166 ARG ARG A . n 
A 1 168  GLY 168  167  167 GLY GLY A . n 
A 1 169  LEU 169  168  168 LEU LEU A . n 
A 1 170  GLU 170  169  169 GLU GLU A . n 
A 1 171  TRP 171  170  170 TRP TRP A . n 
A 1 172  LEU 172  171  171 LEU LEU A . n 
A 1 173  GLY 173  172  172 GLY GLY A . n 
A 1 174  ARG 174  173  173 ARG ARG A . n 
A 1 175  THR 175  174  174 THR THR A . n 
A 1 176  TYR 176  175  175 TYR TYR A . n 
A 1 177  TYR 177  176  176 TYR TYR A . n 
A 1 178  ARG 178  177  177 ARG ARG A . n 
A 1 179  SER 179  178  178 SER SER A . n 
A 1 180  LYS 180  179  179 LYS LYS A . n 
A 1 181  TRP 181  180  180 TRP TRP A . n 
A 1 182  TYR 182  181  181 TYR TYR A . n 
A 1 183  ASN 183  182  182 ASN ASN A . n 
A 1 184  ASP 184  183  183 ASP ASP A . n 
A 1 185  TYR 185  184  184 TYR TYR A . n 
A 1 186  ALA 186  185  185 ALA ALA A . n 
A 1 187  GLY 187  186  186 GLY GLY A . n 
A 1 188  THR 188  187  187 THR THR A . n 
A 1 189  VAL 189  188  188 VAL VAL A . n 
A 1 190  LYS 190  189  189 LYS LYS A . n 
A 1 191  SER 191  190  190 SER SER A . n 
A 1 192  ARG 192  191  191 ARG ARG A . n 
A 1 193  ILE 193  192  192 ILE ILE A . n 
A 1 194  ALA 194  193  193 ALA ALA A . n 
A 1 195  ILE 195  194  194 ILE ILE A . n 
A 1 196  ASN 196  195  195 ASN ASN A . n 
A 1 197  PRO 197  196  196 PRO PRO A . n 
A 1 198  ASP 198  197  197 ASP ASP A . n 
A 1 199  THR 199  198  198 THR THR A . n 
A 1 200  SER 200  199  199 SER SER A . n 
A 1 201  LYS 201  200  200 LYS LYS A . n 
A 1 202  ASN 202  201  201 ASN ASN A . n 
A 1 203  GLN 203  202  202 GLN GLN A . n 
A 1 204  PHE 204  203  203 PHE PHE A . n 
A 1 205  SER 205  204  204 SER SER A . n 
A 1 206  LEU 206  205  205 LEU LEU A . n 
A 1 207  HIS 207  206  206 HIS HIS A . n 
A 1 208  LEU 208  207  207 LEU LEU A . n 
A 1 209  ASN 209  208  208 ASN ASN A . n 
A 1 210  SER 210  209  209 SER SER A . n 
A 1 211  VAL 211  210  210 VAL VAL A . n 
A 1 212  THR 212  211  211 THR THR A . n 
A 1 213  PRO 213  212  212 PRO PRO A . n 
A 1 214  GLU 214  213  213 GLU GLU A . n 
A 1 215  ASP 215  214  214 ASP ASP A . n 
A 1 216  THR 216  215  215 THR THR A . n 
A 1 217  ALA 217  216  216 ALA ALA A . n 
A 1 218  VAL 218  217  217 VAL VAL A . n 
A 1 219  TYR 219  218  218 TYR TYR A . n 
A 1 220  PHE 220  219  219 PHE PHE A . n 
A 1 221  CYS 221  220  220 CYS CYS A . n 
A 1 222  ALA 222  221  221 ALA ALA A . n 
A 1 223  ARG 223  222  222 ARG ARG A . n 
A 1 224  VAL 224  223  223 VAL VAL A . n 
A 1 225  ILE 225  224  224 ILE ILE A . n 
A 1 226  SER 226  225  225 SER SER A . n 
A 1 227  VAL 227  226  226 VAL VAL A . n 
A 1 228  ALA 228  227  227 ALA ALA A . n 
A 1 229  GLY 229  228  228 GLY GLY A . n 
A 1 230  TYR 230  229  229 TYR TYR A . n 
A 1 231  ALA 231  230  230 ALA ALA A . n 
A 1 232  PHE 232  231  231 PHE PHE A . n 
A 1 233  ASP 233  232  232 ASP ASP A . n 
A 1 234  ILE 234  233  233 ILE ILE A . n 
A 1 235  TRP 235  234  234 TRP TRP A . n 
A 1 236  GLY 236  235  235 GLY GLY A . n 
A 1 237  GLN 237  236  236 GLN GLN A . n 
A 1 238  GLY 238  237  237 GLY GLY A . n 
A 1 239  THR 239  238  238 THR THR A . n 
A 1 240  MET 240  239  239 MET MET A . n 
A 1 241  VAL 241  240  240 VAL VAL A . n 
A 1 242  THR 242  241  241 THR THR A . n 
A 1 243  VAL 243  242  242 VAL VAL A . n 
A 1 244  SER 244  243  243 SER SER A . n 
A 1 245  SER 245  244  244 SER SER A . n 
A 1 246  HIS 246  245  ?   ?   ?   A . n 
A 1 247  HIS 247  246  ?   ?   ?   A . n 
A 1 248  HIS 248  247  ?   ?   ?   A . n 
A 1 249  HIS 249  248  ?   ?   ?   A . n 
A 1 250  HIS 250  249  ?   ?   ?   A . n 
A 1 251  HIS 251  250  ?   ?   ?   A . n 
B 2 1    SER 1    12   ?   ?   ?   B . n 
B 2 2    SER 2    13   ?   ?   ?   B . n 
B 2 3    GLN 3    14   ?   ?   ?   B . n 
B 2 4    CYS 4    15   ?   ?   ?   B . n 
B 2 5    VAL 5    16   ?   ?   ?   B . n 
B 2 6    ASN 6    17   ?   ?   ?   B . n 
B 2 7    LEU 7    18   ?   ?   ?   B . n 
B 2 8    THR 8    19   ?   ?   ?   B . n 
B 2 9    THR 9    20   ?   ?   ?   B . n 
B 2 10   ARG 10   21   ?   ?   ?   B . n 
B 2 11   THR 11   22   ?   ?   ?   B . n 
B 2 12   GLN 12   23   ?   ?   ?   B . n 
B 2 13   LEU 13   24   ?   ?   ?   B . n 
B 2 14   PRO 14   25   ?   ?   ?   B . n 
B 2 15   PRO 15   26   ?   ?   ?   B . n 
B 2 16   ALA 16   27   ?   ?   ?   B . n 
B 2 17   TYR 17   28   ?   ?   ?   B . n 
B 2 18   THR 18   29   ?   ?   ?   B . n 
B 2 19   ASN 19   30   ?   ?   ?   B . n 
B 2 20   SER 20   31   ?   ?   ?   B . n 
B 2 21   PHE 21   32   ?   ?   ?   B . n 
B 2 22   THR 22   33   ?   ?   ?   B . n 
B 2 23   ARG 23   34   ?   ?   ?   B . n 
B 2 24   GLY 24   35   ?   ?   ?   B . n 
B 2 25   VAL 25   36   ?   ?   ?   B . n 
B 2 26   TYR 26   37   ?   ?   ?   B . n 
B 2 27   TYR 27   38   ?   ?   ?   B . n 
B 2 28   PRO 28   39   ?   ?   ?   B . n 
B 2 29   ASP 29   40   ?   ?   ?   B . n 
B 2 30   LYS 30   41   ?   ?   ?   B . n 
B 2 31   VAL 31   42   ?   ?   ?   B . n 
B 2 32   PHE 32   43   ?   ?   ?   B . n 
B 2 33   ARG 33   44   ?   ?   ?   B . n 
B 2 34   SER 34   45   ?   ?   ?   B . n 
B 2 35   SER 35   46   ?   ?   ?   B . n 
B 2 36   VAL 36   47   ?   ?   ?   B . n 
B 2 37   LEU 37   48   ?   ?   ?   B . n 
B 2 38   HIS 38   49   ?   ?   ?   B . n 
B 2 39   SER 39   50   ?   ?   ?   B . n 
B 2 40   THR 40   51   ?   ?   ?   B . n 
B 2 41   GLN 41   52   ?   ?   ?   B . n 
B 2 42   ASP 42   53   ?   ?   ?   B . n 
B 2 43   LEU 43   54   ?   ?   ?   B . n 
B 2 44   PHE 44   55   ?   ?   ?   B . n 
B 2 45   LEU 45   56   ?   ?   ?   B . n 
B 2 46   PRO 46   57   ?   ?   ?   B . n 
B 2 47   PHE 47   58   ?   ?   ?   B . n 
B 2 48   PHE 48   59   ?   ?   ?   B . n 
B 2 49   SER 49   60   ?   ?   ?   B . n 
B 2 50   ASN 50   61   ?   ?   ?   B . n 
B 2 51   VAL 51   62   ?   ?   ?   B . n 
B 2 52   THR 52   63   ?   ?   ?   B . n 
B 2 53   TRP 53   64   ?   ?   ?   B . n 
B 2 54   PHE 54   65   ?   ?   ?   B . n 
B 2 55   HIS 55   66   ?   ?   ?   B . n 
B 2 56   ALA 56   67   ?   ?   ?   B . n 
B 2 57   ILE 57   68   ?   ?   ?   B . n 
B 2 58   HIS 58   69   ?   ?   ?   B . n 
B 2 59   VAL 59   70   ?   ?   ?   B . n 
B 2 60   SER 60   71   ?   ?   ?   B . n 
B 2 61   GLY 61   72   ?   ?   ?   B . n 
B 2 62   THR 62   73   ?   ?   ?   B . n 
B 2 63   ASN 63   74   ?   ?   ?   B . n 
B 2 64   GLY 64   75   ?   ?   ?   B . n 
B 2 65   THR 65   76   ?   ?   ?   B . n 
B 2 66   LYS 66   77   ?   ?   ?   B . n 
B 2 67   ARG 67   78   ?   ?   ?   B . n 
B 2 68   PHE 68   79   ?   ?   ?   B . n 
B 2 69   ASP 69   80   ?   ?   ?   B . n 
B 2 70   ASN 70   81   ?   ?   ?   B . n 
B 2 71   PRO 71   82   ?   ?   ?   B . n 
B 2 72   VAL 72   83   ?   ?   ?   B . n 
B 2 73   LEU 73   84   ?   ?   ?   B . n 
B 2 74   PRO 74   85   ?   ?   ?   B . n 
B 2 75   PHE 75   86   ?   ?   ?   B . n 
B 2 76   ASN 76   87   ?   ?   ?   B . n 
B 2 77   ASP 77   88   ?   ?   ?   B . n 
B 2 78   GLY 78   89   ?   ?   ?   B . n 
B 2 79   VAL 79   90   ?   ?   ?   B . n 
B 2 80   TYR 80   91   ?   ?   ?   B . n 
B 2 81   PHE 81   92   ?   ?   ?   B . n 
B 2 82   ALA 82   93   ?   ?   ?   B . n 
B 2 83   SER 83   94   ?   ?   ?   B . n 
B 2 84   THR 84   95   ?   ?   ?   B . n 
B 2 85   GLU 85   96   ?   ?   ?   B . n 
B 2 86   LYS 86   97   ?   ?   ?   B . n 
B 2 87   SER 87   98   ?   ?   ?   B . n 
B 2 88   ASN 88   99   ?   ?   ?   B . n 
B 2 89   ILE 89   100  ?   ?   ?   B . n 
B 2 90   ILE 90   101  ?   ?   ?   B . n 
B 2 91   ARG 91   102  ?   ?   ?   B . n 
B 2 92   GLY 92   103  ?   ?   ?   B . n 
B 2 93   TRP 93   104  ?   ?   ?   B . n 
B 2 94   ILE 94   105  ?   ?   ?   B . n 
B 2 95   PHE 95   106  ?   ?   ?   B . n 
B 2 96   GLY 96   107  ?   ?   ?   B . n 
B 2 97   THR 97   108  ?   ?   ?   B . n 
B 2 98   THR 98   109  ?   ?   ?   B . n 
B 2 99   LEU 99   110  ?   ?   ?   B . n 
B 2 100  ASP 100  111  ?   ?   ?   B . n 
B 2 101  SER 101  112  ?   ?   ?   B . n 
B 2 102  LYS 102  113  ?   ?   ?   B . n 
B 2 103  THR 103  114  ?   ?   ?   B . n 
B 2 104  GLN 104  115  ?   ?   ?   B . n 
B 2 105  SER 105  116  ?   ?   ?   B . n 
B 2 106  LEU 106  117  ?   ?   ?   B . n 
B 2 107  LEU 107  118  ?   ?   ?   B . n 
B 2 108  ILE 108  119  ?   ?   ?   B . n 
B 2 109  VAL 109  120  ?   ?   ?   B . n 
B 2 110  ASN 110  121  ?   ?   ?   B . n 
B 2 111  ASN 111  122  ?   ?   ?   B . n 
B 2 112  ALA 112  123  ?   ?   ?   B . n 
B 2 113  THR 113  124  ?   ?   ?   B . n 
B 2 114  ASN 114  125  ?   ?   ?   B . n 
B 2 115  VAL 115  126  ?   ?   ?   B . n 
B 2 116  VAL 116  127  ?   ?   ?   B . n 
B 2 117  ILE 117  128  ?   ?   ?   B . n 
B 2 118  LYS 118  129  ?   ?   ?   B . n 
B 2 119  VAL 119  130  ?   ?   ?   B . n 
B 2 120  CYS 120  131  ?   ?   ?   B . n 
B 2 121  GLU 121  132  ?   ?   ?   B . n 
B 2 122  PHE 122  133  ?   ?   ?   B . n 
B 2 123  GLN 123  134  ?   ?   ?   B . n 
B 2 124  PHE 124  135  ?   ?   ?   B . n 
B 2 125  CYS 125  136  ?   ?   ?   B . n 
B 2 126  ASN 126  137  ?   ?   ?   B . n 
B 2 127  ASP 127  138  ?   ?   ?   B . n 
B 2 128  PRO 128  139  ?   ?   ?   B . n 
B 2 129  PHE 129  140  ?   ?   ?   B . n 
B 2 130  LEU 130  141  ?   ?   ?   B . n 
B 2 131  GLY 131  142  ?   ?   ?   B . n 
B 2 132  VAL 132  143  ?   ?   ?   B . n 
B 2 133  TYR 133  144  ?   ?   ?   B . n 
B 2 134  TYR 134  145  ?   ?   ?   B . n 
B 2 135  HIS 135  146  ?   ?   ?   B . n 
B 2 136  LYS 136  147  ?   ?   ?   B . n 
B 2 137  ASN 137  148  ?   ?   ?   B . n 
B 2 138  ASN 138  149  ?   ?   ?   B . n 
B 2 139  LYS 139  150  ?   ?   ?   B . n 
B 2 140  SER 140  151  ?   ?   ?   B . n 
B 2 141  TRP 141  152  ?   ?   ?   B . n 
B 2 142  MET 142  153  ?   ?   ?   B . n 
B 2 143  GLU 143  154  ?   ?   ?   B . n 
B 2 144  SER 144  155  ?   ?   ?   B . n 
B 2 145  GLU 145  156  ?   ?   ?   B . n 
B 2 146  PHE 146  157  ?   ?   ?   B . n 
B 2 147  ARG 147  158  ?   ?   ?   B . n 
B 2 148  VAL 148  159  ?   ?   ?   B . n 
B 2 149  TYR 149  160  ?   ?   ?   B . n 
B 2 150  SER 150  161  ?   ?   ?   B . n 
B 2 151  SER 151  162  ?   ?   ?   B . n 
B 2 152  ALA 152  163  ?   ?   ?   B . n 
B 2 153  ASN 153  164  ?   ?   ?   B . n 
B 2 154  ASN 154  165  ?   ?   ?   B . n 
B 2 155  CYS 155  166  ?   ?   ?   B . n 
B 2 156  THR 156  167  ?   ?   ?   B . n 
B 2 157  PHE 157  168  ?   ?   ?   B . n 
B 2 158  GLU 158  169  ?   ?   ?   B . n 
B 2 159  TYR 159  170  ?   ?   ?   B . n 
B 2 160  VAL 160  171  ?   ?   ?   B . n 
B 2 161  SER 161  172  ?   ?   ?   B . n 
B 2 162  GLN 162  173  ?   ?   ?   B . n 
B 2 163  PRO 163  174  ?   ?   ?   B . n 
B 2 164  PHE 164  175  ?   ?   ?   B . n 
B 2 165  LEU 165  176  ?   ?   ?   B . n 
B 2 166  MET 166  177  ?   ?   ?   B . n 
B 2 167  ASP 167  178  ?   ?   ?   B . n 
B 2 168  LEU 168  179  ?   ?   ?   B . n 
B 2 169  GLU 169  180  ?   ?   ?   B . n 
B 2 170  GLY 170  181  ?   ?   ?   B . n 
B 2 171  LYS 171  182  ?   ?   ?   B . n 
B 2 172  GLN 172  183  ?   ?   ?   B . n 
B 2 173  GLY 173  184  ?   ?   ?   B . n 
B 2 174  ASN 174  185  ?   ?   ?   B . n 
B 2 175  PHE 175  186  ?   ?   ?   B . n 
B 2 176  LYS 176  187  ?   ?   ?   B . n 
B 2 177  ASN 177  188  ?   ?   ?   B . n 
B 2 178  LEU 178  189  ?   ?   ?   B . n 
B 2 179  ARG 179  190  ?   ?   ?   B . n 
B 2 180  GLU 180  191  ?   ?   ?   B . n 
B 2 181  PHE 181  192  ?   ?   ?   B . n 
B 2 182  VAL 182  193  ?   ?   ?   B . n 
B 2 183  PHE 183  194  ?   ?   ?   B . n 
B 2 184  LYS 184  195  ?   ?   ?   B . n 
B 2 185  ASN 185  196  ?   ?   ?   B . n 
B 2 186  ILE 186  197  ?   ?   ?   B . n 
B 2 187  ASP 187  198  ?   ?   ?   B . n 
B 2 188  GLY 188  199  ?   ?   ?   B . n 
B 2 189  TYR 189  200  ?   ?   ?   B . n 
B 2 190  PHE 190  201  ?   ?   ?   B . n 
B 2 191  LYS 191  202  ?   ?   ?   B . n 
B 2 192  ILE 192  203  ?   ?   ?   B . n 
B 2 193  TYR 193  204  ?   ?   ?   B . n 
B 2 194  SER 194  205  ?   ?   ?   B . n 
B 2 195  LYS 195  206  ?   ?   ?   B . n 
B 2 196  HIS 196  207  ?   ?   ?   B . n 
B 2 197  THR 197  208  ?   ?   ?   B . n 
B 2 198  PRO 198  209  ?   ?   ?   B . n 
B 2 199  ILE 199  210  ?   ?   ?   B . n 
B 2 200  ASN 200  211  ?   ?   ?   B . n 
B 2 201  LEU 201  212  ?   ?   ?   B . n 
B 2 202  VAL 202  213  ?   ?   ?   B . n 
B 2 203  ARG 203  214  ?   ?   ?   B . n 
B 2 204  ASP 204  215  ?   ?   ?   B . n 
B 2 205  LEU 205  216  ?   ?   ?   B . n 
B 2 206  PRO 206  217  ?   ?   ?   B . n 
B 2 207  GLN 207  218  ?   ?   ?   B . n 
B 2 208  GLY 208  219  ?   ?   ?   B . n 
B 2 209  PHE 209  220  ?   ?   ?   B . n 
B 2 210  SER 210  221  ?   ?   ?   B . n 
B 2 211  ALA 211  222  ?   ?   ?   B . n 
B 2 212  LEU 212  223  ?   ?   ?   B . n 
B 2 213  GLU 213  224  ?   ?   ?   B . n 
B 2 214  PRO 214  225  ?   ?   ?   B . n 
B 2 215  LEU 215  226  ?   ?   ?   B . n 
B 2 216  VAL 216  227  ?   ?   ?   B . n 
B 2 217  ASP 217  228  ?   ?   ?   B . n 
B 2 218  LEU 218  229  ?   ?   ?   B . n 
B 2 219  PRO 219  230  ?   ?   ?   B . n 
B 2 220  ILE 220  231  ?   ?   ?   B . n 
B 2 221  GLY 221  232  ?   ?   ?   B . n 
B 2 222  ILE 222  233  ?   ?   ?   B . n 
B 2 223  ASN 223  234  ?   ?   ?   B . n 
B 2 224  ILE 224  235  ?   ?   ?   B . n 
B 2 225  THR 225  236  ?   ?   ?   B . n 
B 2 226  ARG 226  237  ?   ?   ?   B . n 
B 2 227  PHE 227  238  ?   ?   ?   B . n 
B 2 228  GLN 228  239  ?   ?   ?   B . n 
B 2 229  THR 229  240  ?   ?   ?   B . n 
B 2 230  LEU 230  241  ?   ?   ?   B . n 
B 2 231  LEU 231  242  ?   ?   ?   B . n 
B 2 232  ALA 232  243  ?   ?   ?   B . n 
B 2 233  LEU 233  244  ?   ?   ?   B . n 
B 2 234  HIS 234  245  ?   ?   ?   B . n 
B 2 235  ARG 235  246  ?   ?   ?   B . n 
B 2 236  SER 236  247  ?   ?   ?   B . n 
B 2 237  TYR 237  248  ?   ?   ?   B . n 
B 2 238  LEU 238  249  ?   ?   ?   B . n 
B 2 239  THR 239  250  ?   ?   ?   B . n 
B 2 240  PRO 240  251  ?   ?   ?   B . n 
B 2 241  GLY 241  252  ?   ?   ?   B . n 
B 2 242  ASP 242  253  ?   ?   ?   B . n 
B 2 243  SER 243  254  ?   ?   ?   B . n 
B 2 244  SER 244  255  ?   ?   ?   B . n 
B 2 245  SER 245  256  ?   ?   ?   B . n 
B 2 246  GLY 246  257  ?   ?   ?   B . n 
B 2 247  TRP 247  258  ?   ?   ?   B . n 
B 2 248  THR 248  259  ?   ?   ?   B . n 
B 2 249  ALA 249  260  ?   ?   ?   B . n 
B 2 250  GLY 250  261  ?   ?   ?   B . n 
B 2 251  ALA 251  262  ?   ?   ?   B . n 
B 2 252  ALA 252  263  ?   ?   ?   B . n 
B 2 253  ALA 253  264  ?   ?   ?   B . n 
B 2 254  TYR 254  265  ?   ?   ?   B . n 
B 2 255  TYR 255  266  ?   ?   ?   B . n 
B 2 256  VAL 256  267  ?   ?   ?   B . n 
B 2 257  GLY 257  268  ?   ?   ?   B . n 
B 2 258  TYR 258  269  ?   ?   ?   B . n 
B 2 259  LEU 259  270  ?   ?   ?   B . n 
B 2 260  GLN 260  271  ?   ?   ?   B . n 
B 2 261  PRO 261  272  ?   ?   ?   B . n 
B 2 262  ARG 262  273  ?   ?   ?   B . n 
B 2 263  THR 263  274  ?   ?   ?   B . n 
B 2 264  PHE 264  275  ?   ?   ?   B . n 
B 2 265  LEU 265  276  ?   ?   ?   B . n 
B 2 266  LEU 266  277  ?   ?   ?   B . n 
B 2 267  LYS 267  278  ?   ?   ?   B . n 
B 2 268  TYR 268  279  ?   ?   ?   B . n 
B 2 269  ASN 269  280  ?   ?   ?   B . n 
B 2 270  GLU 270  281  ?   ?   ?   B . n 
B 2 271  ASN 271  282  ?   ?   ?   B . n 
B 2 272  GLY 272  283  ?   ?   ?   B . n 
B 2 273  THR 273  284  ?   ?   ?   B . n 
B 2 274  ILE 274  285  ?   ?   ?   B . n 
B 2 275  THR 275  286  ?   ?   ?   B . n 
B 2 276  ASP 276  287  ?   ?   ?   B . n 
B 2 277  ALA 277  288  ?   ?   ?   B . n 
B 2 278  VAL 278  289  ?   ?   ?   B . n 
B 2 279  ASP 279  290  ?   ?   ?   B . n 
B 2 280  CYS 280  291  ?   ?   ?   B . n 
B 2 281  ALA 281  292  ?   ?   ?   B . n 
B 2 282  LEU 282  293  ?   ?   ?   B . n 
B 2 283  ASP 283  294  ?   ?   ?   B . n 
B 2 284  PRO 284  295  ?   ?   ?   B . n 
B 2 285  LEU 285  296  ?   ?   ?   B . n 
B 2 286  SER 286  297  ?   ?   ?   B . n 
B 2 287  GLU 287  298  ?   ?   ?   B . n 
B 2 288  THR 288  299  ?   ?   ?   B . n 
B 2 289  LYS 289  300  ?   ?   ?   B . n 
B 2 290  CYS 290  301  ?   ?   ?   B . n 
B 2 291  THR 291  302  ?   ?   ?   B . n 
B 2 292  LEU 292  303  ?   ?   ?   B . n 
B 2 293  LYS 293  304  ?   ?   ?   B . n 
B 2 294  SER 294  305  ?   ?   ?   B . n 
B 2 295  PHE 295  306  ?   ?   ?   B . n 
B 2 296  THR 296  307  ?   ?   ?   B . n 
B 2 297  VAL 297  308  ?   ?   ?   B . n 
B 2 298  GLU 298  309  ?   ?   ?   B . n 
B 2 299  LYS 299  310  ?   ?   ?   B . n 
B 2 300  GLY 300  311  ?   ?   ?   B . n 
B 2 301  ILE 301  312  ?   ?   ?   B . n 
B 2 302  TYR 302  313  ?   ?   ?   B . n 
B 2 303  GLN 303  314  ?   ?   ?   B . n 
B 2 304  THR 304  315  ?   ?   ?   B . n 
B 2 305  SER 305  316  ?   ?   ?   B . n 
B 2 306  ASN 306  317  ?   ?   ?   B . n 
B 2 307  PHE 307  318  ?   ?   ?   B . n 
B 2 308  ARG 308  319  ?   ?   ?   B . n 
B 2 309  VAL 309  320  ?   ?   ?   B . n 
B 2 310  GLN 310  321  ?   ?   ?   B . n 
B 2 311  PRO 311  322  ?   ?   ?   B . n 
B 2 312  THR 312  323  ?   ?   ?   B . n 
B 2 313  GLU 313  324  ?   ?   ?   B . n 
B 2 314  SER 314  325  ?   ?   ?   B . n 
B 2 315  ILE 315  326  ?   ?   ?   B . n 
B 2 316  VAL 316  327  ?   ?   ?   B . n 
B 2 317  ARG 317  328  ?   ?   ?   B . n 
B 2 318  PHE 318  329  ?   ?   ?   B . n 
B 2 319  PRO 319  330  ?   ?   ?   B . n 
B 2 320  ASN 320  331  331 ASN ASN B . n 
B 2 321  ILE 321  332  332 ILE ILE B . n 
B 2 322  THR 322  333  333 THR THR B . n 
B 2 323  ASN 323  334  334 ASN ASN B . n 
B 2 324  LEU 324  335  335 LEU LEU B . n 
B 2 325  CYS 325  336  336 CYS CYS B . n 
B 2 326  PRO 326  337  337 PRO PRO B . n 
B 2 327  PHE 327  338  338 PHE PHE B . n 
B 2 328  GLY 328  339  339 GLY GLY B . n 
B 2 329  GLU 329  340  340 GLU GLU B . n 
B 2 330  VAL 330  341  341 VAL VAL B . n 
B 2 331  PHE 331  342  342 PHE PHE B . n 
B 2 332  ASN 332  343  343 ASN ASN B . n 
B 2 333  ALA 333  344  344 ALA ALA B . n 
B 2 334  THR 334  345  345 THR THR B . n 
B 2 335  ARG 335  346  346 ARG ARG B . n 
B 2 336  PHE 336  347  347 PHE PHE B . n 
B 2 337  ALA 337  348  348 ALA ALA B . n 
B 2 338  SER 338  349  349 SER SER B . n 
B 2 339  VAL 339  350  350 VAL VAL B . n 
B 2 340  TYR 340  351  351 TYR TYR B . n 
B 2 341  ALA 341  352  352 ALA ALA B . n 
B 2 342  TRP 342  353  353 TRP TRP B . n 
B 2 343  ASN 343  354  354 ASN ASN B . n 
B 2 344  ARG 344  355  355 ARG ARG B . n 
B 2 345  LYS 345  356  356 LYS LYS B . n 
B 2 346  ARG 346  357  357 ARG ARG B . n 
B 2 347  ILE 347  358  358 ILE ILE B . n 
B 2 348  SER 348  359  359 SER SER B . n 
B 2 349  ASN 349  360  360 ASN ASN B . n 
B 2 350  CYS 350  361  361 CYS CYS B . n 
B 2 351  VAL 351  362  362 VAL VAL B . n 
B 2 352  ALA 352  363  363 ALA ALA B . n 
B 2 353  ASP 353  364  364 ASP ASP B . n 
B 2 354  TYR 354  365  365 TYR TYR B . n 
B 2 355  SER 355  366  366 SER SER B . n 
B 2 356  VAL 356  367  367 VAL VAL B . n 
B 2 357  LEU 357  368  368 LEU LEU B . n 
B 2 358  TYR 358  369  369 TYR TYR B . n 
B 2 359  ASN 359  370  370 ASN ASN B . n 
B 2 360  SER 360  371  371 SER SER B . n 
B 2 361  ALA 361  372  372 ALA ALA B . n 
B 2 362  SER 362  373  373 SER SER B . n 
B 2 363  PHE 363  374  374 PHE PHE B . n 
B 2 364  SER 364  375  375 SER SER B . n 
B 2 365  THR 365  376  376 THR THR B . n 
B 2 366  PHE 366  377  377 PHE PHE B . n 
B 2 367  LYS 367  378  378 LYS LYS B . n 
B 2 368  CYS 368  379  379 CYS CYS B . n 
B 2 369  TYR 369  380  380 TYR TYR B . n 
B 2 370  GLY 370  381  381 GLY GLY B . n 
B 2 371  VAL 371  382  382 VAL VAL B . n 
B 2 372  SER 372  383  383 SER SER B . n 
B 2 373  PRO 373  384  384 PRO PRO B . n 
B 2 374  THR 374  385  385 THR THR B . n 
B 2 375  LYS 375  386  386 LYS LYS B . n 
B 2 376  LEU 376  387  387 LEU LEU B . n 
B 2 377  ASN 377  388  388 ASN ASN B . n 
B 2 378  ASP 378  389  389 ASP ASP B . n 
B 2 379  LEU 379  390  390 LEU LEU B . n 
B 2 380  CYS 380  391  391 CYS CYS B . n 
B 2 381  PHE 381  392  392 PHE PHE B . n 
B 2 382  THR 382  393  393 THR THR B . n 
B 2 383  ASN 383  394  394 ASN ASN B . n 
B 2 384  VAL 384  395  395 VAL VAL B . n 
B 2 385  TYR 385  396  396 TYR TYR B . n 
B 2 386  ALA 386  397  397 ALA ALA B . n 
B 2 387  ASP 387  398  398 ASP ASP B . n 
B 2 388  SER 388  399  399 SER SER B . n 
B 2 389  PHE 389  400  400 PHE PHE B . n 
B 2 390  VAL 390  401  401 VAL VAL B . n 
B 2 391  ILE 391  402  402 ILE ILE B . n 
B 2 392  ARG 392  403  403 ARG ARG B . n 
B 2 393  GLY 393  404  404 GLY GLY B . n 
B 2 394  ASP 394  405  405 ASP ASP B . n 
B 2 395  GLU 395  406  406 GLU GLU B . n 
B 2 396  VAL 396  407  407 VAL VAL B . n 
B 2 397  ARG 397  408  408 ARG ARG B . n 
B 2 398  GLN 398  409  409 GLN GLN B . n 
B 2 399  ILE 399  410  410 ILE ILE B . n 
B 2 400  ALA 400  411  411 ALA ALA B . n 
B 2 401  PRO 401  412  412 PRO PRO B . n 
B 2 402  GLY 402  413  413 GLY GLY B . n 
B 2 403  GLN 403  414  414 GLN GLN B . n 
B 2 404  THR 404  415  415 THR THR B . n 
B 2 405  GLY 405  416  416 GLY GLY B . n 
B 2 406  LYS 406  417  417 LYS LYS B . n 
B 2 407  ILE 407  418  418 ILE ILE B . n 
B 2 408  ALA 408  419  419 ALA ALA B . n 
B 2 409  ASP 409  420  420 ASP ASP B . n 
B 2 410  TYR 410  421  421 TYR TYR B . n 
B 2 411  ASN 411  422  422 ASN ASN B . n 
B 2 412  TYR 412  423  423 TYR TYR B . n 
B 2 413  LYS 413  424  424 LYS LYS B . n 
B 2 414  LEU 414  425  425 LEU LEU B . n 
B 2 415  PRO 415  426  426 PRO PRO B . n 
B 2 416  ASP 416  427  427 ASP ASP B . n 
B 2 417  ASP 417  428  428 ASP ASP B . n 
B 2 418  PHE 418  429  429 PHE PHE B . n 
B 2 419  THR 419  430  430 THR THR B . n 
B 2 420  GLY 420  431  431 GLY GLY B . n 
B 2 421  CYS 421  432  432 CYS CYS B . n 
B 2 422  VAL 422  433  433 VAL VAL B . n 
B 2 423  ILE 423  434  434 ILE ILE B . n 
B 2 424  ALA 424  435  435 ALA ALA B . n 
B 2 425  TRP 425  436  436 TRP TRP B . n 
B 2 426  ASN 426  437  437 ASN ASN B . n 
B 2 427  SER 427  438  438 SER SER B . n 
B 2 428  ASN 428  439  439 ASN ASN B . n 
B 2 429  ASN 429  440  440 ASN ASN B . n 
B 2 430  LEU 430  441  441 LEU LEU B . n 
B 2 431  ASP 431  442  442 ASP ASP B . n 
B 2 432  SER 432  443  443 SER SER B . n 
B 2 433  LYS 433  444  444 LYS LYS B . n 
B 2 434  VAL 434  445  445 VAL VAL B . n 
B 2 435  GLY 435  446  446 GLY GLY B . n 
B 2 436  GLY 436  447  447 GLY GLY B . n 
B 2 437  ASN 437  448  448 ASN ASN B . n 
B 2 438  TYR 438  449  449 TYR TYR B . n 
B 2 439  ASN 439  450  450 ASN ASN B . n 
B 2 440  TYR 440  451  451 TYR TYR B . n 
B 2 441  LEU 441  452  452 LEU LEU B . n 
B 2 442  TYR 442  453  453 TYR TYR B . n 
B 2 443  ARG 443  454  454 ARG ARG B . n 
B 2 444  LEU 444  455  455 LEU LEU B . n 
B 2 445  PHE 445  456  456 PHE PHE B . n 
B 2 446  ARG 446  457  457 ARG ARG B . n 
B 2 447  LYS 447  458  458 LYS LYS B . n 
B 2 448  SER 448  459  459 SER SER B . n 
B 2 449  ASN 449  460  460 ASN ASN B . n 
B 2 450  LEU 450  461  461 LEU LEU B . n 
B 2 451  LYS 451  462  462 LYS LYS B . n 
B 2 452  PRO 452  463  463 PRO PRO B . n 
B 2 453  PHE 453  464  464 PHE PHE B . n 
B 2 454  GLU 454  465  465 GLU GLU B . n 
B 2 455  ARG 455  466  466 ARG ARG B . n 
B 2 456  ASP 456  467  467 ASP ASP B . n 
B 2 457  ILE 457  468  468 ILE ILE B . n 
B 2 458  SER 458  469  469 SER SER B . n 
B 2 459  THR 459  470  470 THR THR B . n 
B 2 460  GLU 460  471  471 GLU GLU B . n 
B 2 461  ILE 461  472  472 ILE ILE B . n 
B 2 462  TYR 462  473  473 TYR TYR B . n 
B 2 463  GLN 463  474  474 GLN GLN B . n 
B 2 464  ALA 464  475  475 ALA ALA B . n 
B 2 465  GLY 465  476  476 GLY GLY B . n 
B 2 466  SER 466  477  477 SER SER B . n 
B 2 467  THR 467  478  478 THR THR B . n 
B 2 468  PRO 468  479  479 PRO PRO B . n 
B 2 469  CYS 469  480  480 CYS CYS B . n 
B 2 470  ASN 470  481  481 ASN ASN B . n 
B 2 471  GLY 471  482  482 GLY GLY B . n 
B 2 472  VAL 472  483  483 VAL VAL B . n 
B 2 473  GLU 473  484  484 GLU GLU B . n 
B 2 474  GLY 474  485  485 GLY GLY B . n 
B 2 475  PHE 475  486  486 PHE PHE B . n 
B 2 476  ASN 476  487  487 ASN ASN B . n 
B 2 477  CYS 477  488  488 CYS CYS B . n 
B 2 478  TYR 478  489  489 TYR TYR B . n 
B 2 479  PHE 479  490  490 PHE PHE B . n 
B 2 480  PRO 480  491  491 PRO PRO B . n 
B 2 481  LEU 481  492  492 LEU LEU B . n 
B 2 482  GLN 482  493  493 GLN GLN B . n 
B 2 483  SER 483  494  494 SER SER B . n 
B 2 484  TYR 484  495  495 TYR TYR B . n 
B 2 485  GLY 485  496  496 GLY GLY B . n 
B 2 486  PHE 486  497  497 PHE PHE B . n 
B 2 487  GLN 487  498  498 GLN GLN B . n 
B 2 488  PRO 488  499  499 PRO PRO B . n 
B 2 489  THR 489  500  500 THR THR B . n 
B 2 490  ASN 490  501  501 ASN ASN B . n 
B 2 491  GLY 491  502  502 GLY GLY B . n 
B 2 492  VAL 492  503  503 VAL VAL B . n 
B 2 493  GLY 493  504  504 GLY GLY B . n 
B 2 494  TYR 494  505  505 TYR TYR B . n 
B 2 495  GLN 495  506  506 GLN GLN B . n 
B 2 496  PRO 496  507  507 PRO PRO B . n 
B 2 497  TYR 497  508  508 TYR TYR B . n 
B 2 498  ARG 498  509  509 ARG ARG B . n 
B 2 499  VAL 499  510  510 VAL VAL B . n 
B 2 500  VAL 500  511  511 VAL VAL B . n 
B 2 501  VAL 501  512  512 VAL VAL B . n 
B 2 502  LEU 502  513  513 LEU LEU B . n 
B 2 503  SER 503  514  514 SER SER B . n 
B 2 504  PHE 504  515  515 PHE PHE B . n 
B 2 505  GLU 505  516  516 GLU GLU B . n 
B 2 506  LEU 506  517  517 LEU LEU B . n 
B 2 507  LEU 507  518  ?   ?   ?   B . n 
B 2 508  HIS 508  519  ?   ?   ?   B . n 
B 2 509  ALA 509  520  520 ALA ALA B . n 
B 2 510  PRO 510  521  521 PRO PRO B . n 
B 2 511  ALA 511  522  522 ALA ALA B . n 
B 2 512  THR 512  523  523 THR THR B . n 
B 2 513  VAL 513  524  524 VAL VAL B . n 
B 2 514  CYS 514  525  525 CYS CYS B . n 
B 2 515  GLY 515  526  526 GLY GLY B . n 
B 2 516  PRO 516  527  527 PRO PRO B . n 
B 2 517  LYS 517  528  ?   ?   ?   B . n 
B 2 518  LYS 518  529  ?   ?   ?   B . n 
B 2 519  SER 519  530  ?   ?   ?   B . n 
B 2 520  THR 520  531  ?   ?   ?   B . n 
B 2 521  ASN 521  532  ?   ?   ?   B . n 
B 2 522  LEU 522  533  ?   ?   ?   B . n 
B 2 523  VAL 523  534  ?   ?   ?   B . n 
B 2 524  LYS 524  535  ?   ?   ?   B . n 
B 2 525  ASN 525  536  ?   ?   ?   B . n 
B 2 526  LYS 526  537  ?   ?   ?   B . n 
B 2 527  CYS 527  538  ?   ?   ?   B . n 
B 2 528  VAL 528  539  ?   ?   ?   B . n 
B 2 529  ASN 529  540  ?   ?   ?   B . n 
B 2 530  PHE 530  541  ?   ?   ?   B . n 
B 2 531  ASN 531  542  ?   ?   ?   B . n 
B 2 532  PHE 532  543  ?   ?   ?   B . n 
B 2 533  ASN 533  544  ?   ?   ?   B . n 
B 2 534  GLY 534  545  ?   ?   ?   B . n 
B 2 535  LEU 535  546  ?   ?   ?   B . n 
B 2 536  THR 536  547  ?   ?   ?   B . n 
B 2 537  GLY 537  548  ?   ?   ?   B . n 
B 2 538  THR 538  549  ?   ?   ?   B . n 
B 2 539  GLY 539  550  ?   ?   ?   B . n 
B 2 540  VAL 540  551  ?   ?   ?   B . n 
B 2 541  LEU 541  552  ?   ?   ?   B . n 
B 2 542  THR 542  553  ?   ?   ?   B . n 
B 2 543  GLU 543  554  ?   ?   ?   B . n 
B 2 544  SER 544  555  ?   ?   ?   B . n 
B 2 545  ASN 545  556  ?   ?   ?   B . n 
B 2 546  LYS 546  557  ?   ?   ?   B . n 
B 2 547  LYS 547  558  ?   ?   ?   B . n 
B 2 548  PHE 548  559  ?   ?   ?   B . n 
B 2 549  LEU 549  560  ?   ?   ?   B . n 
B 2 550  PRO 550  561  ?   ?   ?   B . n 
B 2 551  PHE 551  562  ?   ?   ?   B . n 
B 2 552  GLN 552  563  ?   ?   ?   B . n 
B 2 553  GLN 553  564  ?   ?   ?   B . n 
B 2 554  PHE 554  565  ?   ?   ?   B . n 
B 2 555  GLY 555  566  ?   ?   ?   B . n 
B 2 556  ARG 556  567  ?   ?   ?   B . n 
B 2 557  ASP 557  568  ?   ?   ?   B . n 
B 2 558  ILE 558  569  ?   ?   ?   B . n 
B 2 559  ALA 559  570  ?   ?   ?   B . n 
B 2 560  ASP 560  571  ?   ?   ?   B . n 
B 2 561  THR 561  572  ?   ?   ?   B . n 
B 2 562  THR 562  573  ?   ?   ?   B . n 
B 2 563  ASP 563  574  ?   ?   ?   B . n 
B 2 564  ALA 564  575  ?   ?   ?   B . n 
B 2 565  VAL 565  576  ?   ?   ?   B . n 
B 2 566  ARG 566  577  ?   ?   ?   B . n 
B 2 567  ASP 567  578  ?   ?   ?   B . n 
B 2 568  PRO 568  579  ?   ?   ?   B . n 
B 2 569  GLN 569  580  ?   ?   ?   B . n 
B 2 570  THR 570  581  ?   ?   ?   B . n 
B 2 571  LEU 571  582  ?   ?   ?   B . n 
B 2 572  GLU 572  583  ?   ?   ?   B . n 
B 2 573  ILE 573  584  ?   ?   ?   B . n 
B 2 574  LEU 574  585  ?   ?   ?   B . n 
B 2 575  ASP 575  586  ?   ?   ?   B . n 
B 2 576  ILE 576  587  ?   ?   ?   B . n 
B 2 577  THR 577  588  ?   ?   ?   B . n 
B 2 578  PRO 578  589  ?   ?   ?   B . n 
B 2 579  CYS 579  590  ?   ?   ?   B . n 
B 2 580  SER 580  591  ?   ?   ?   B . n 
B 2 581  PHE 581  592  ?   ?   ?   B . n 
B 2 582  GLY 582  593  ?   ?   ?   B . n 
B 2 583  GLY 583  594  ?   ?   ?   B . n 
B 2 584  VAL 584  595  ?   ?   ?   B . n 
B 2 585  SER 585  596  ?   ?   ?   B . n 
B 2 586  VAL 586  597  ?   ?   ?   B . n 
B 2 587  ILE 587  598  ?   ?   ?   B . n 
B 2 588  THR 588  599  ?   ?   ?   B . n 
B 2 589  PRO 589  600  ?   ?   ?   B . n 
B 2 590  GLY 590  601  ?   ?   ?   B . n 
B 2 591  THR 591  602  ?   ?   ?   B . n 
B 2 592  ASN 592  603  ?   ?   ?   B . n 
B 2 593  THR 593  604  ?   ?   ?   B . n 
B 2 594  SER 594  605  ?   ?   ?   B . n 
B 2 595  ASN 595  606  ?   ?   ?   B . n 
B 2 596  GLN 596  607  ?   ?   ?   B . n 
B 2 597  VAL 597  608  ?   ?   ?   B . n 
B 2 598  ALA 598  609  ?   ?   ?   B . n 
B 2 599  VAL 599  610  ?   ?   ?   B . n 
B 2 600  LEU 600  611  ?   ?   ?   B . n 
B 2 601  TYR 601  612  ?   ?   ?   B . n 
B 2 602  GLN 602  613  ?   ?   ?   B . n 
B 2 603  ASP 603  614  ?   ?   ?   B . n 
B 2 604  VAL 604  615  ?   ?   ?   B . n 
B 2 605  ASN 605  616  ?   ?   ?   B . n 
B 2 606  CYS 606  617  ?   ?   ?   B . n 
B 2 607  THR 607  618  ?   ?   ?   B . n 
B 2 608  GLU 608  619  ?   ?   ?   B . n 
B 2 609  VAL 609  620  ?   ?   ?   B . n 
B 2 610  PRO 610  621  ?   ?   ?   B . n 
B 2 611  VAL 611  622  ?   ?   ?   B . n 
B 2 612  ALA 612  623  ?   ?   ?   B . n 
B 2 613  ILE 613  624  ?   ?   ?   B . n 
B 2 614  HIS 614  625  ?   ?   ?   B . n 
B 2 615  ALA 615  626  ?   ?   ?   B . n 
B 2 616  ASP 616  627  ?   ?   ?   B . n 
B 2 617  GLN 617  628  ?   ?   ?   B . n 
B 2 618  LEU 618  629  ?   ?   ?   B . n 
B 2 619  THR 619  630  ?   ?   ?   B . n 
B 2 620  PRO 620  631  ?   ?   ?   B . n 
B 2 621  THR 621  632  ?   ?   ?   B . n 
B 2 622  TRP 622  633  ?   ?   ?   B . n 
B 2 623  ARG 623  634  ?   ?   ?   B . n 
B 2 624  VAL 624  635  ?   ?   ?   B . n 
B 2 625  TYR 625  636  ?   ?   ?   B . n 
B 2 626  SER 626  637  ?   ?   ?   B . n 
B 2 627  THR 627  638  ?   ?   ?   B . n 
B 2 628  GLY 628  639  ?   ?   ?   B . n 
B 2 629  SER 629  640  ?   ?   ?   B . n 
B 2 630  ASN 630  641  ?   ?   ?   B . n 
B 2 631  VAL 631  642  ?   ?   ?   B . n 
B 2 632  PHE 632  643  ?   ?   ?   B . n 
B 2 633  GLN 633  644  ?   ?   ?   B . n 
B 2 634  THR 634  645  ?   ?   ?   B . n 
B 2 635  ARG 635  646  ?   ?   ?   B . n 
B 2 636  ALA 636  647  ?   ?   ?   B . n 
B 2 637  GLY 637  648  ?   ?   ?   B . n 
B 2 638  CYS 638  649  ?   ?   ?   B . n 
B 2 639  LEU 639  650  ?   ?   ?   B . n 
B 2 640  ILE 640  651  ?   ?   ?   B . n 
B 2 641  GLY 641  652  ?   ?   ?   B . n 
B 2 642  ALA 642  653  ?   ?   ?   B . n 
B 2 643  GLU 643  654  ?   ?   ?   B . n 
B 2 644  HIS 644  655  ?   ?   ?   B . n 
B 2 645  VAL 645  656  ?   ?   ?   B . n 
B 2 646  ASN 646  657  ?   ?   ?   B . n 
B 2 647  ASN 647  658  ?   ?   ?   B . n 
B 2 648  SER 648  659  ?   ?   ?   B . n 
B 2 649  TYR 649  660  ?   ?   ?   B . n 
B 2 650  GLU 650  661  ?   ?   ?   B . n 
B 2 651  CYS 651  662  ?   ?   ?   B . n 
B 2 652  ASP 652  663  ?   ?   ?   B . n 
B 2 653  ILE 653  664  ?   ?   ?   B . n 
B 2 654  PRO 654  665  ?   ?   ?   B . n 
B 2 655  ILE 655  666  ?   ?   ?   B . n 
B 2 656  GLY 656  667  ?   ?   ?   B . n 
B 2 657  ALA 657  668  ?   ?   ?   B . n 
B 2 658  GLY 658  669  ?   ?   ?   B . n 
B 2 659  ILE 659  670  ?   ?   ?   B . n 
B 2 660  CYS 660  671  ?   ?   ?   B . n 
B 2 661  ALA 661  672  ?   ?   ?   B . n 
B 2 662  SER 662  673  ?   ?   ?   B . n 
B 2 663  TYR 663  674  ?   ?   ?   B . n 
B 2 664  GLN 664  675  ?   ?   ?   B . n 
B 2 665  THR 665  676  ?   ?   ?   B . n 
B 2 666  GLN 666  677  ?   ?   ?   B . n 
B 2 667  THR 667  678  ?   ?   ?   B . n 
B 2 668  ASN 668  679  ?   ?   ?   B . n 
B 2 669  SER 669  680  ?   ?   ?   B . n 
B 2 670  PRO 670  681  ?   ?   ?   B . n 
B 2 671  GLY 671  682  ?   ?   ?   B . n 
B 2 672  SER 672  683  ?   ?   ?   B . n 
B 2 673  ALA 673  684  ?   ?   ?   B . n 
B 2 674  GLY 674  685  ?   ?   ?   B . n 
B 2 675  SER 675  686  ?   ?   ?   B . n 
B 2 676  VAL 676  687  ?   ?   ?   B . n 
B 2 677  ALA 677  688  ?   ?   ?   B . n 
B 2 678  SER 678  689  ?   ?   ?   B . n 
B 2 679  GLN 679  690  ?   ?   ?   B . n 
B 2 680  SER 680  691  ?   ?   ?   B . n 
B 2 681  ILE 681  692  ?   ?   ?   B . n 
B 2 682  ILE 682  693  ?   ?   ?   B . n 
B 2 683  ALA 683  694  ?   ?   ?   B . n 
B 2 684  TYR 684  695  ?   ?   ?   B . n 
B 2 685  THR 685  696  ?   ?   ?   B . n 
B 2 686  MET 686  697  ?   ?   ?   B . n 
B 2 687  SER 687  698  ?   ?   ?   B . n 
B 2 688  LEU 688  699  ?   ?   ?   B . n 
B 2 689  GLY 689  700  ?   ?   ?   B . n 
B 2 690  ALA 690  701  ?   ?   ?   B . n 
B 2 691  GLU 691  702  ?   ?   ?   B . n 
B 2 692  ASN 692  703  ?   ?   ?   B . n 
B 2 693  SER 693  704  ?   ?   ?   B . n 
B 2 694  VAL 694  705  ?   ?   ?   B . n 
B 2 695  ALA 695  706  ?   ?   ?   B . n 
B 2 696  TYR 696  707  ?   ?   ?   B . n 
B 2 697  SER 697  708  ?   ?   ?   B . n 
B 2 698  ASN 698  709  ?   ?   ?   B . n 
B 2 699  ASN 699  710  ?   ?   ?   B . n 
B 2 700  SER 700  711  ?   ?   ?   B . n 
B 2 701  ILE 701  712  ?   ?   ?   B . n 
B 2 702  ALA 702  713  ?   ?   ?   B . n 
B 2 703  ILE 703  714  ?   ?   ?   B . n 
B 2 704  PRO 704  715  ?   ?   ?   B . n 
B 2 705  THR 705  716  ?   ?   ?   B . n 
B 2 706  ASN 706  717  ?   ?   ?   B . n 
B 2 707  PHE 707  718  ?   ?   ?   B . n 
B 2 708  THR 708  719  ?   ?   ?   B . n 
B 2 709  ILE 709  720  ?   ?   ?   B . n 
B 2 710  SER 710  721  ?   ?   ?   B . n 
B 2 711  VAL 711  722  ?   ?   ?   B . n 
B 2 712  THR 712  723  ?   ?   ?   B . n 
B 2 713  THR 713  724  ?   ?   ?   B . n 
B 2 714  GLU 714  725  ?   ?   ?   B . n 
B 2 715  ILE 715  726  ?   ?   ?   B . n 
B 2 716  LEU 716  727  ?   ?   ?   B . n 
B 2 717  PRO 717  728  ?   ?   ?   B . n 
B 2 718  VAL 718  729  ?   ?   ?   B . n 
B 2 719  SER 719  730  ?   ?   ?   B . n 
B 2 720  MET 720  731  ?   ?   ?   B . n 
B 2 721  THR 721  732  ?   ?   ?   B . n 
B 2 722  LYS 722  733  ?   ?   ?   B . n 
B 2 723  THR 723  734  ?   ?   ?   B . n 
B 2 724  SER 724  735  ?   ?   ?   B . n 
B 2 725  VAL 725  736  ?   ?   ?   B . n 
B 2 726  ASP 726  737  ?   ?   ?   B . n 
B 2 727  CYS 727  738  ?   ?   ?   B . n 
B 2 728  THR 728  739  ?   ?   ?   B . n 
B 2 729  MET 729  740  ?   ?   ?   B . n 
B 2 730  TYR 730  741  ?   ?   ?   B . n 
B 2 731  ILE 731  742  ?   ?   ?   B . n 
B 2 732  CYS 732  743  ?   ?   ?   B . n 
B 2 733  GLY 733  744  ?   ?   ?   B . n 
B 2 734  ASP 734  745  ?   ?   ?   B . n 
B 2 735  SER 735  746  ?   ?   ?   B . n 
B 2 736  THR 736  747  ?   ?   ?   B . n 
B 2 737  GLU 737  748  ?   ?   ?   B . n 
B 2 738  CYS 738  749  ?   ?   ?   B . n 
B 2 739  SER 739  750  ?   ?   ?   B . n 
B 2 740  ASN 740  751  ?   ?   ?   B . n 
B 2 741  LEU 741  752  ?   ?   ?   B . n 
B 2 742  LEU 742  753  ?   ?   ?   B . n 
B 2 743  LEU 743  754  ?   ?   ?   B . n 
B 2 744  GLN 744  755  ?   ?   ?   B . n 
B 2 745  TYR 745  756  ?   ?   ?   B . n 
B 2 746  GLY 746  757  ?   ?   ?   B . n 
B 2 747  SER 747  758  ?   ?   ?   B . n 
B 2 748  PHE 748  759  ?   ?   ?   B . n 
B 2 749  CYS 749  760  ?   ?   ?   B . n 
B 2 750  THR 750  761  ?   ?   ?   B . n 
B 2 751  GLN 751  762  ?   ?   ?   B . n 
B 2 752  LEU 752  763  ?   ?   ?   B . n 
B 2 753  ASN 753  764  ?   ?   ?   B . n 
B 2 754  ARG 754  765  ?   ?   ?   B . n 
B 2 755  ALA 755  766  ?   ?   ?   B . n 
B 2 756  LEU 756  767  ?   ?   ?   B . n 
B 2 757  THR 757  768  ?   ?   ?   B . n 
B 2 758  GLY 758  769  ?   ?   ?   B . n 
B 2 759  ILE 759  770  ?   ?   ?   B . n 
B 2 760  ALA 760  771  ?   ?   ?   B . n 
B 2 761  VAL 761  772  ?   ?   ?   B . n 
B 2 762  GLU 762  773  ?   ?   ?   B . n 
B 2 763  GLN 763  774  ?   ?   ?   B . n 
B 2 764  ASP 764  775  ?   ?   ?   B . n 
B 2 765  LYS 765  776  ?   ?   ?   B . n 
B 2 766  ASN 766  777  ?   ?   ?   B . n 
B 2 767  THR 767  778  ?   ?   ?   B . n 
B 2 768  GLN 768  779  ?   ?   ?   B . n 
B 2 769  GLU 769  780  ?   ?   ?   B . n 
B 2 770  VAL 770  781  ?   ?   ?   B . n 
B 2 771  PHE 771  782  ?   ?   ?   B . n 
B 2 772  ALA 772  783  ?   ?   ?   B . n 
B 2 773  GLN 773  784  ?   ?   ?   B . n 
B 2 774  VAL 774  785  ?   ?   ?   B . n 
B 2 775  LYS 775  786  ?   ?   ?   B . n 
B 2 776  GLN 776  787  ?   ?   ?   B . n 
B 2 777  ILE 777  788  ?   ?   ?   B . n 
B 2 778  TYR 778  789  ?   ?   ?   B . n 
B 2 779  LYS 779  790  ?   ?   ?   B . n 
B 2 780  THR 780  791  ?   ?   ?   B . n 
B 2 781  PRO 781  792  ?   ?   ?   B . n 
B 2 782  PRO 782  793  ?   ?   ?   B . n 
B 2 783  ILE 783  794  ?   ?   ?   B . n 
B 2 784  LYS 784  795  ?   ?   ?   B . n 
B 2 785  ASP 785  796  ?   ?   ?   B . n 
B 2 786  PHE 786  797  ?   ?   ?   B . n 
B 2 787  GLY 787  798  ?   ?   ?   B . n 
B 2 788  GLY 788  799  ?   ?   ?   B . n 
B 2 789  PHE 789  800  ?   ?   ?   B . n 
B 2 790  ASN 790  801  ?   ?   ?   B . n 
B 2 791  PHE 791  802  ?   ?   ?   B . n 
B 2 792  SER 792  803  ?   ?   ?   B . n 
B 2 793  GLN 793  804  ?   ?   ?   B . n 
B 2 794  ILE 794  805  ?   ?   ?   B . n 
B 2 795  LEU 795  806  ?   ?   ?   B . n 
B 2 796  PRO 796  807  ?   ?   ?   B . n 
B 2 797  ASP 797  808  ?   ?   ?   B . n 
B 2 798  PRO 798  809  ?   ?   ?   B . n 
B 2 799  SER 799  810  ?   ?   ?   B . n 
B 2 800  LYS 800  811  ?   ?   ?   B . n 
B 2 801  PRO 801  812  ?   ?   ?   B . n 
B 2 802  SER 802  813  ?   ?   ?   B . n 
B 2 803  LYS 803  814  ?   ?   ?   B . n 
B 2 804  ARG 804  815  ?   ?   ?   B . n 
B 2 805  SER 805  816  ?   ?   ?   B . n 
B 2 806  PRO 806  817  ?   ?   ?   B . n 
B 2 807  ILE 807  818  ?   ?   ?   B . n 
B 2 808  GLU 808  819  ?   ?   ?   B . n 
B 2 809  ASP 809  820  ?   ?   ?   B . n 
B 2 810  LEU 810  821  ?   ?   ?   B . n 
B 2 811  LEU 811  822  ?   ?   ?   B . n 
B 2 812  PHE 812  823  ?   ?   ?   B . n 
B 2 813  ASN 813  824  ?   ?   ?   B . n 
B 2 814  LYS 814  825  ?   ?   ?   B . n 
B 2 815  VAL 815  826  ?   ?   ?   B . n 
B 2 816  THR 816  827  ?   ?   ?   B . n 
B 2 817  LEU 817  828  ?   ?   ?   B . n 
B 2 818  ALA 818  829  ?   ?   ?   B . n 
B 2 819  ASP 819  830  ?   ?   ?   B . n 
B 2 820  ALA 820  831  ?   ?   ?   B . n 
B 2 821  GLY 821  832  ?   ?   ?   B . n 
B 2 822  PHE 822  833  ?   ?   ?   B . n 
B 2 823  ILE 823  834  ?   ?   ?   B . n 
B 2 824  LYS 824  835  ?   ?   ?   B . n 
B 2 825  GLN 825  836  ?   ?   ?   B . n 
B 2 826  TYR 826  837  ?   ?   ?   B . n 
B 2 827  GLY 827  838  ?   ?   ?   B . n 
B 2 828  ASP 828  839  ?   ?   ?   B . n 
B 2 829  CYS 829  840  ?   ?   ?   B . n 
B 2 830  LEU 830  841  ?   ?   ?   B . n 
B 2 831  GLY 831  842  ?   ?   ?   B . n 
B 2 832  ASP 832  843  ?   ?   ?   B . n 
B 2 833  ILE 833  844  ?   ?   ?   B . n 
B 2 834  ALA 834  845  ?   ?   ?   B . n 
B 2 835  ALA 835  846  ?   ?   ?   B . n 
B 2 836  ARG 836  847  ?   ?   ?   B . n 
B 2 837  ASP 837  848  ?   ?   ?   B . n 
B 2 838  LEU 838  849  ?   ?   ?   B . n 
B 2 839  ILE 839  850  ?   ?   ?   B . n 
B 2 840  CYS 840  851  ?   ?   ?   B . n 
B 2 841  ALA 841  852  ?   ?   ?   B . n 
B 2 842  GLN 842  853  ?   ?   ?   B . n 
B 2 843  LYS 843  854  ?   ?   ?   B . n 
B 2 844  PHE 844  855  ?   ?   ?   B . n 
B 2 845  ASN 845  856  ?   ?   ?   B . n 
B 2 846  GLY 846  857  ?   ?   ?   B . n 
B 2 847  LEU 847  858  ?   ?   ?   B . n 
B 2 848  THR 848  859  ?   ?   ?   B . n 
B 2 849  VAL 849  860  ?   ?   ?   B . n 
B 2 850  LEU 850  861  ?   ?   ?   B . n 
B 2 851  PRO 851  862  ?   ?   ?   B . n 
B 2 852  PRO 852  863  ?   ?   ?   B . n 
B 2 853  LEU 853  864  ?   ?   ?   B . n 
B 2 854  LEU 854  865  ?   ?   ?   B . n 
B 2 855  THR 855  866  ?   ?   ?   B . n 
B 2 856  ASP 856  867  ?   ?   ?   B . n 
B 2 857  GLU 857  868  ?   ?   ?   B . n 
B 2 858  MET 858  869  ?   ?   ?   B . n 
B 2 859  ILE 859  870  ?   ?   ?   B . n 
B 2 860  ALA 860  871  ?   ?   ?   B . n 
B 2 861  GLN 861  872  ?   ?   ?   B . n 
B 2 862  TYR 862  873  ?   ?   ?   B . n 
B 2 863  THR 863  874  ?   ?   ?   B . n 
B 2 864  SER 864  875  ?   ?   ?   B . n 
B 2 865  ALA 865  876  ?   ?   ?   B . n 
B 2 866  LEU 866  877  ?   ?   ?   B . n 
B 2 867  LEU 867  878  ?   ?   ?   B . n 
B 2 868  ALA 868  879  ?   ?   ?   B . n 
B 2 869  GLY 869  880  ?   ?   ?   B . n 
B 2 870  THR 870  881  ?   ?   ?   B . n 
B 2 871  ILE 871  882  ?   ?   ?   B . n 
B 2 872  THR 872  883  ?   ?   ?   B . n 
B 2 873  SER 873  884  ?   ?   ?   B . n 
B 2 874  GLY 874  885  ?   ?   ?   B . n 
B 2 875  TRP 875  886  ?   ?   ?   B . n 
B 2 876  THR 876  887  ?   ?   ?   B . n 
B 2 877  PHE 877  888  ?   ?   ?   B . n 
B 2 878  GLY 878  889  ?   ?   ?   B . n 
B 2 879  ALA 879  890  ?   ?   ?   B . n 
B 2 880  GLY 880  891  ?   ?   ?   B . n 
B 2 881  PRO 881  892  ?   ?   ?   B . n 
B 2 882  ALA 882  893  ?   ?   ?   B . n 
B 2 883  LEU 883  894  ?   ?   ?   B . n 
B 2 884  GLN 884  895  ?   ?   ?   B . n 
B 2 885  ILE 885  896  ?   ?   ?   B . n 
B 2 886  PRO 886  897  ?   ?   ?   B . n 
B 2 887  PHE 887  898  ?   ?   ?   B . n 
B 2 888  PRO 888  899  ?   ?   ?   B . n 
B 2 889  MET 889  900  ?   ?   ?   B . n 
B 2 890  GLN 890  901  ?   ?   ?   B . n 
B 2 891  MET 891  902  ?   ?   ?   B . n 
B 2 892  ALA 892  903  ?   ?   ?   B . n 
B 2 893  TYR 893  904  ?   ?   ?   B . n 
B 2 894  ARG 894  905  ?   ?   ?   B . n 
B 2 895  PHE 895  906  ?   ?   ?   B . n 
B 2 896  ASN 896  907  ?   ?   ?   B . n 
B 2 897  GLY 897  908  ?   ?   ?   B . n 
B 2 898  ILE 898  909  ?   ?   ?   B . n 
B 2 899  GLY 899  910  ?   ?   ?   B . n 
B 2 900  VAL 900  911  ?   ?   ?   B . n 
B 2 901  THR 901  912  ?   ?   ?   B . n 
B 2 902  GLN 902  913  ?   ?   ?   B . n 
B 2 903  ASN 903  914  ?   ?   ?   B . n 
B 2 904  VAL 904  915  ?   ?   ?   B . n 
B 2 905  LEU 905  916  ?   ?   ?   B . n 
B 2 906  TYR 906  917  ?   ?   ?   B . n 
B 2 907  GLU 907  918  ?   ?   ?   B . n 
B 2 908  ASN 908  919  ?   ?   ?   B . n 
B 2 909  GLN 909  920  ?   ?   ?   B . n 
B 2 910  LYS 910  921  ?   ?   ?   B . n 
B 2 911  LEU 911  922  ?   ?   ?   B . n 
B 2 912  ILE 912  923  ?   ?   ?   B . n 
B 2 913  ALA 913  924  ?   ?   ?   B . n 
B 2 914  ASN 914  925  ?   ?   ?   B . n 
B 2 915  GLN 915  926  ?   ?   ?   B . n 
B 2 916  PHE 916  927  ?   ?   ?   B . n 
B 2 917  ASN 917  928  ?   ?   ?   B . n 
B 2 918  SER 918  929  ?   ?   ?   B . n 
B 2 919  ALA 919  930  ?   ?   ?   B . n 
B 2 920  ILE 920  931  ?   ?   ?   B . n 
B 2 921  GLY 921  932  ?   ?   ?   B . n 
B 2 922  LYS 922  933  ?   ?   ?   B . n 
B 2 923  ILE 923  934  ?   ?   ?   B . n 
B 2 924  GLN 924  935  ?   ?   ?   B . n 
B 2 925  ASP 925  936  ?   ?   ?   B . n 
B 2 926  SER 926  937  ?   ?   ?   B . n 
B 2 927  LEU 927  938  ?   ?   ?   B . n 
B 2 928  SER 928  939  ?   ?   ?   B . n 
B 2 929  SER 929  940  ?   ?   ?   B . n 
B 2 930  THR 930  941  ?   ?   ?   B . n 
B 2 931  PRO 931  942  ?   ?   ?   B . n 
B 2 932  SER 932  943  ?   ?   ?   B . n 
B 2 933  ALA 933  944  ?   ?   ?   B . n 
B 2 934  LEU 934  945  ?   ?   ?   B . n 
B 2 935  GLY 935  946  ?   ?   ?   B . n 
B 2 936  LYS 936  947  ?   ?   ?   B . n 
B 2 937  LEU 937  948  ?   ?   ?   B . n 
B 2 938  GLN 938  949  ?   ?   ?   B . n 
B 2 939  ASP 939  950  ?   ?   ?   B . n 
B 2 940  VAL 940  951  ?   ?   ?   B . n 
B 2 941  VAL 941  952  ?   ?   ?   B . n 
B 2 942  ASN 942  953  ?   ?   ?   B . n 
B 2 943  GLN 943  954  ?   ?   ?   B . n 
B 2 944  ASN 944  955  ?   ?   ?   B . n 
B 2 945  ALA 945  956  ?   ?   ?   B . n 
B 2 946  GLN 946  957  ?   ?   ?   B . n 
B 2 947  ALA 947  958  ?   ?   ?   B . n 
B 2 948  LEU 948  959  ?   ?   ?   B . n 
B 2 949  ASN 949  960  ?   ?   ?   B . n 
B 2 950  THR 950  961  ?   ?   ?   B . n 
B 2 951  LEU 951  962  ?   ?   ?   B . n 
B 2 952  VAL 952  963  ?   ?   ?   B . n 
B 2 953  LYS 953  964  ?   ?   ?   B . n 
B 2 954  GLN 954  965  ?   ?   ?   B . n 
B 2 955  LEU 955  966  ?   ?   ?   B . n 
B 2 956  SER 956  967  ?   ?   ?   B . n 
B 2 957  SER 957  968  ?   ?   ?   B . n 
B 2 958  ASN 958  969  ?   ?   ?   B . n 
B 2 959  PHE 959  970  ?   ?   ?   B . n 
B 2 960  GLY 960  971  ?   ?   ?   B . n 
B 2 961  ALA 961  972  ?   ?   ?   B . n 
B 2 962  ILE 962  973  ?   ?   ?   B . n 
B 2 963  SER 963  974  ?   ?   ?   B . n 
B 2 964  SER 964  975  ?   ?   ?   B . n 
B 2 965  VAL 965  976  ?   ?   ?   B . n 
B 2 966  LEU 966  977  ?   ?   ?   B . n 
B 2 967  ASN 967  978  ?   ?   ?   B . n 
B 2 968  ASP 968  979  ?   ?   ?   B . n 
B 2 969  ILE 969  980  ?   ?   ?   B . n 
B 2 970  LEU 970  981  ?   ?   ?   B . n 
B 2 971  SER 971  982  ?   ?   ?   B . n 
B 2 972  ARG 972  983  ?   ?   ?   B . n 
B 2 973  LEU 973  984  ?   ?   ?   B . n 
B 2 974  ASP 974  985  ?   ?   ?   B . n 
B 2 975  PRO 975  986  ?   ?   ?   B . n 
B 2 976  PRO 976  987  ?   ?   ?   B . n 
B 2 977  GLU 977  988  ?   ?   ?   B . n 
B 2 978  ALA 978  989  ?   ?   ?   B . n 
B 2 979  GLU 979  990  ?   ?   ?   B . n 
B 2 980  VAL 980  991  ?   ?   ?   B . n 
B 2 981  GLN 981  992  ?   ?   ?   B . n 
B 2 982  ILE 982  993  ?   ?   ?   B . n 
B 2 983  ASP 983  994  ?   ?   ?   B . n 
B 2 984  ARG 984  995  ?   ?   ?   B . n 
B 2 985  LEU 985  996  ?   ?   ?   B . n 
B 2 986  ILE 986  997  ?   ?   ?   B . n 
B 2 987  THR 987  998  ?   ?   ?   B . n 
B 2 988  GLY 988  999  ?   ?   ?   B . n 
B 2 989  ARG 989  1000 ?   ?   ?   B . n 
B 2 990  LEU 990  1001 ?   ?   ?   B . n 
B 2 991  GLN 991  1002 ?   ?   ?   B . n 
B 2 992  SER 992  1003 ?   ?   ?   B . n 
B 2 993  LEU 993  1004 ?   ?   ?   B . n 
B 2 994  GLN 994  1005 ?   ?   ?   B . n 
B 2 995  THR 995  1006 ?   ?   ?   B . n 
B 2 996  TYR 996  1007 ?   ?   ?   B . n 
B 2 997  VAL 997  1008 ?   ?   ?   B . n 
B 2 998  THR 998  1009 ?   ?   ?   B . n 
B 2 999  GLN 999  1010 ?   ?   ?   B . n 
B 2 1000 GLN 1000 1011 ?   ?   ?   B . n 
B 2 1001 LEU 1001 1012 ?   ?   ?   B . n 
B 2 1002 ILE 1002 1013 ?   ?   ?   B . n 
B 2 1003 ARG 1003 1014 ?   ?   ?   B . n 
B 2 1004 ALA 1004 1015 ?   ?   ?   B . n 
B 2 1005 ALA 1005 1016 ?   ?   ?   B . n 
B 2 1006 GLU 1006 1017 ?   ?   ?   B . n 
B 2 1007 ILE 1007 1018 ?   ?   ?   B . n 
B 2 1008 ARG 1008 1019 ?   ?   ?   B . n 
B 2 1009 ALA 1009 1020 ?   ?   ?   B . n 
B 2 1010 SER 1010 1021 ?   ?   ?   B . n 
B 2 1011 ALA 1011 1022 ?   ?   ?   B . n 
B 2 1012 ASN 1012 1023 ?   ?   ?   B . n 
B 2 1013 LEU 1013 1024 ?   ?   ?   B . n 
B 2 1014 ALA 1014 1025 ?   ?   ?   B . n 
B 2 1015 ALA 1015 1026 ?   ?   ?   B . n 
B 2 1016 THR 1016 1027 ?   ?   ?   B . n 
B 2 1017 LYS 1017 1028 ?   ?   ?   B . n 
B 2 1018 MET 1018 1029 ?   ?   ?   B . n 
B 2 1019 SER 1019 1030 ?   ?   ?   B . n 
B 2 1020 GLU 1020 1031 ?   ?   ?   B . n 
B 2 1021 CYS 1021 1032 ?   ?   ?   B . n 
B 2 1022 VAL 1022 1033 ?   ?   ?   B . n 
B 2 1023 LEU 1023 1034 ?   ?   ?   B . n 
B 2 1024 GLY 1024 1035 ?   ?   ?   B . n 
B 2 1025 GLN 1025 1036 ?   ?   ?   B . n 
B 2 1026 SER 1026 1037 ?   ?   ?   B . n 
B 2 1027 LYS 1027 1038 ?   ?   ?   B . n 
B 2 1028 ARG 1028 1039 ?   ?   ?   B . n 
B 2 1029 VAL 1029 1040 ?   ?   ?   B . n 
B 2 1030 ASP 1030 1041 ?   ?   ?   B . n 
B 2 1031 PHE 1031 1042 ?   ?   ?   B . n 
B 2 1032 CYS 1032 1043 ?   ?   ?   B . n 
B 2 1033 GLY 1033 1044 ?   ?   ?   B . n 
B 2 1034 LYS 1034 1045 ?   ?   ?   B . n 
B 2 1035 GLY 1035 1046 ?   ?   ?   B . n 
B 2 1036 TYR 1036 1047 ?   ?   ?   B . n 
B 2 1037 HIS 1037 1048 ?   ?   ?   B . n 
B 2 1038 LEU 1038 1049 ?   ?   ?   B . n 
B 2 1039 MET 1039 1050 ?   ?   ?   B . n 
B 2 1040 SER 1040 1051 ?   ?   ?   B . n 
B 2 1041 PHE 1041 1052 ?   ?   ?   B . n 
B 2 1042 PRO 1042 1053 ?   ?   ?   B . n 
B 2 1043 GLN 1043 1054 ?   ?   ?   B . n 
B 2 1044 SER 1044 1055 ?   ?   ?   B . n 
B 2 1045 ALA 1045 1056 ?   ?   ?   B . n 
B 2 1046 PRO 1046 1057 ?   ?   ?   B . n 
B 2 1047 HIS 1047 1058 ?   ?   ?   B . n 
B 2 1048 GLY 1048 1059 ?   ?   ?   B . n 
B 2 1049 VAL 1049 1060 ?   ?   ?   B . n 
B 2 1050 VAL 1050 1061 ?   ?   ?   B . n 
B 2 1051 PHE 1051 1062 ?   ?   ?   B . n 
B 2 1052 LEU 1052 1063 ?   ?   ?   B . n 
B 2 1053 HIS 1053 1064 ?   ?   ?   B . n 
B 2 1054 VAL 1054 1065 ?   ?   ?   B . n 
B 2 1055 THR 1055 1066 ?   ?   ?   B . n 
B 2 1056 TYR 1056 1067 ?   ?   ?   B . n 
B 2 1057 VAL 1057 1068 ?   ?   ?   B . n 
B 2 1058 PRO 1058 1069 ?   ?   ?   B . n 
B 2 1059 ALA 1059 1070 ?   ?   ?   B . n 
B 2 1060 GLN 1060 1071 ?   ?   ?   B . n 
B 2 1061 GLU 1061 1072 ?   ?   ?   B . n 
B 2 1062 LYS 1062 1073 ?   ?   ?   B . n 
B 2 1063 ASN 1063 1074 ?   ?   ?   B . n 
B 2 1064 PHE 1064 1075 ?   ?   ?   B . n 
B 2 1065 THR 1065 1076 ?   ?   ?   B . n 
B 2 1066 THR 1066 1077 ?   ?   ?   B . n 
B 2 1067 ALA 1067 1078 ?   ?   ?   B . n 
B 2 1068 PRO 1068 1079 ?   ?   ?   B . n 
B 2 1069 ALA 1069 1080 ?   ?   ?   B . n 
B 2 1070 ILE 1070 1081 ?   ?   ?   B . n 
B 2 1071 CYS 1071 1082 ?   ?   ?   B . n 
B 2 1072 HIS 1072 1083 ?   ?   ?   B . n 
B 2 1073 ASP 1073 1084 ?   ?   ?   B . n 
B 2 1074 GLY 1074 1085 ?   ?   ?   B . n 
B 2 1075 LYS 1075 1086 ?   ?   ?   B . n 
B 2 1076 ALA 1076 1087 ?   ?   ?   B . n 
B 2 1077 HIS 1077 1088 ?   ?   ?   B . n 
B 2 1078 PHE 1078 1089 ?   ?   ?   B . n 
B 2 1079 PRO 1079 1090 ?   ?   ?   B . n 
B 2 1080 ARG 1080 1091 ?   ?   ?   B . n 
B 2 1081 GLU 1081 1092 ?   ?   ?   B . n 
B 2 1082 GLY 1082 1093 ?   ?   ?   B . n 
B 2 1083 VAL 1083 1094 ?   ?   ?   B . n 
B 2 1084 PHE 1084 1095 ?   ?   ?   B . n 
B 2 1085 VAL 1085 1096 ?   ?   ?   B . n 
B 2 1086 SER 1086 1097 ?   ?   ?   B . n 
B 2 1087 ASN 1087 1098 ?   ?   ?   B . n 
B 2 1088 GLY 1088 1099 ?   ?   ?   B . n 
B 2 1089 THR 1089 1100 ?   ?   ?   B . n 
B 2 1090 HIS 1090 1101 ?   ?   ?   B . n 
B 2 1091 TRP 1091 1102 ?   ?   ?   B . n 
B 2 1092 PHE 1092 1103 ?   ?   ?   B . n 
B 2 1093 VAL 1093 1104 ?   ?   ?   B . n 
B 2 1094 THR 1094 1105 ?   ?   ?   B . n 
B 2 1095 GLN 1095 1106 ?   ?   ?   B . n 
B 2 1096 ARG 1096 1107 ?   ?   ?   B . n 
B 2 1097 ASN 1097 1108 ?   ?   ?   B . n 
B 2 1098 PHE 1098 1109 ?   ?   ?   B . n 
B 2 1099 TYR 1099 1110 ?   ?   ?   B . n 
B 2 1100 GLU 1100 1111 ?   ?   ?   B . n 
B 2 1101 PRO 1101 1112 ?   ?   ?   B . n 
B 2 1102 GLN 1102 1113 ?   ?   ?   B . n 
B 2 1103 ILE 1103 1114 ?   ?   ?   B . n 
B 2 1104 ILE 1104 1115 ?   ?   ?   B . n 
B 2 1105 THR 1105 1116 ?   ?   ?   B . n 
B 2 1106 THR 1106 1117 ?   ?   ?   B . n 
B 2 1107 ASP 1107 1118 ?   ?   ?   B . n 
B 2 1108 ASN 1108 1119 ?   ?   ?   B . n 
B 2 1109 THR 1109 1120 ?   ?   ?   B . n 
B 2 1110 PHE 1110 1121 ?   ?   ?   B . n 
B 2 1111 VAL 1111 1122 ?   ?   ?   B . n 
B 2 1112 SER 1112 1123 ?   ?   ?   B . n 
B 2 1113 GLY 1113 1124 ?   ?   ?   B . n 
B 2 1114 ASN 1114 1125 ?   ?   ?   B . n 
B 2 1115 CYS 1115 1126 ?   ?   ?   B . n 
B 2 1116 ASP 1116 1127 ?   ?   ?   B . n 
B 2 1117 VAL 1117 1128 ?   ?   ?   B . n 
B 2 1118 VAL 1118 1129 ?   ?   ?   B . n 
B 2 1119 ILE 1119 1130 ?   ?   ?   B . n 
B 2 1120 GLY 1120 1131 ?   ?   ?   B . n 
B 2 1121 ILE 1121 1132 ?   ?   ?   B . n 
B 2 1122 VAL 1122 1133 ?   ?   ?   B . n 
B 2 1123 ASN 1123 1134 ?   ?   ?   B . n 
B 2 1124 ASN 1124 1135 ?   ?   ?   B . n 
B 2 1125 THR 1125 1136 ?   ?   ?   B . n 
B 2 1126 VAL 1126 1137 ?   ?   ?   B . n 
B 2 1127 TYR 1127 1138 ?   ?   ?   B . n 
B 2 1128 ASP 1128 1139 ?   ?   ?   B . n 
B 2 1129 PRO 1129 1140 ?   ?   ?   B . n 
B 2 1130 LEU 1130 1141 ?   ?   ?   B . n 
B 2 1131 GLN 1131 1142 ?   ?   ?   B . n 
B 2 1132 PRO 1132 1143 ?   ?   ?   B . n 
B 2 1133 GLU 1133 1144 ?   ?   ?   B . n 
B 2 1134 LEU 1134 1145 ?   ?   ?   B . n 
B 2 1135 ASP 1135 1146 ?   ?   ?   B . n 
B 2 1136 SER 1136 1147 ?   ?   ?   B . n 
B 2 1137 PHE 1137 1148 ?   ?   ?   B . n 
B 2 1138 LYS 1138 1149 ?   ?   ?   B . n 
B 2 1139 GLU 1139 1150 ?   ?   ?   B . n 
B 2 1140 GLU 1140 1151 ?   ?   ?   B . n 
B 2 1141 LEU 1141 1152 ?   ?   ?   B . n 
B 2 1142 ASP 1142 1153 ?   ?   ?   B . n 
B 2 1143 LYS 1143 1154 ?   ?   ?   B . n 
B 2 1144 TYR 1144 1155 ?   ?   ?   B . n 
B 2 1145 PHE 1145 1156 ?   ?   ?   B . n 
B 2 1146 LYS 1146 1157 ?   ?   ?   B . n 
B 2 1147 ASN 1147 1158 ?   ?   ?   B . n 
B 2 1148 HIS 1148 1159 ?   ?   ?   B . n 
B 2 1149 THR 1149 1160 ?   ?   ?   B . n 
B 2 1150 SER 1150 1161 ?   ?   ?   B . n 
B 2 1151 PRO 1151 1162 ?   ?   ?   B . n 
B 2 1152 ASP 1152 1163 ?   ?   ?   B . n 
B 2 1153 VAL 1153 1164 ?   ?   ?   B . n 
B 2 1154 ASP 1154 1165 ?   ?   ?   B . n 
B 2 1155 LEU 1155 1166 ?   ?   ?   B . n 
B 2 1156 GLY 1156 1167 ?   ?   ?   B . n 
B 2 1157 ASP 1157 1168 ?   ?   ?   B . n 
B 2 1158 ILE 1158 1169 ?   ?   ?   B . n 
B 2 1159 SER 1159 1170 ?   ?   ?   B . n 
B 2 1160 GLY 1160 1171 ?   ?   ?   B . n 
B 2 1161 ILE 1161 1172 ?   ?   ?   B . n 
B 2 1162 ASN 1162 1173 ?   ?   ?   B . n 
B 2 1163 ALA 1163 1174 ?   ?   ?   B . n 
B 2 1164 SER 1164 1175 ?   ?   ?   B . n 
B 2 1165 VAL 1165 1176 ?   ?   ?   B . n 
B 2 1166 VAL 1166 1177 ?   ?   ?   B . n 
B 2 1167 ASN 1167 1178 ?   ?   ?   B . n 
B 2 1168 ILE 1168 1179 ?   ?   ?   B . n 
B 2 1169 GLN 1169 1180 ?   ?   ?   B . n 
B 2 1170 LYS 1170 1181 ?   ?   ?   B . n 
B 2 1171 GLU 1171 1182 ?   ?   ?   B . n 
B 2 1172 ILE 1172 1183 ?   ?   ?   B . n 
B 2 1173 ASP 1173 1184 ?   ?   ?   B . n 
B 2 1174 ARG 1174 1185 ?   ?   ?   B . n 
B 2 1175 LEU 1175 1186 ?   ?   ?   B . n 
B 2 1176 ASN 1176 1187 ?   ?   ?   B . n 
B 2 1177 GLU 1177 1188 ?   ?   ?   B . n 
B 2 1178 VAL 1178 1189 ?   ?   ?   B . n 
B 2 1179 ALA 1179 1190 ?   ?   ?   B . n 
B 2 1180 LYS 1180 1191 ?   ?   ?   B . n 
B 2 1181 ASN 1181 1192 ?   ?   ?   B . n 
B 2 1182 LEU 1182 1193 ?   ?   ?   B . n 
B 2 1183 ASN 1183 1194 ?   ?   ?   B . n 
B 2 1184 GLU 1184 1195 ?   ?   ?   B . n 
B 2 1185 SER 1185 1196 ?   ?   ?   B . n 
B 2 1186 LEU 1186 1197 ?   ?   ?   B . n 
B 2 1187 ILE 1187 1198 ?   ?   ?   B . n 
B 2 1188 ASP 1188 1199 ?   ?   ?   B . n 
B 2 1189 LEU 1189 1200 ?   ?   ?   B . n 
B 2 1190 GLN 1190 1201 ?   ?   ?   B . n 
B 2 1191 GLU 1191 1202 ?   ?   ?   B . n 
B 2 1192 LEU 1192 1203 ?   ?   ?   B . n 
B 2 1193 GLY 1193 1204 ?   ?   ?   B . n 
B 2 1194 LYS 1194 1205 ?   ?   ?   B . n 
B 2 1195 TYR 1195 1206 ?   ?   ?   B . n 
B 2 1196 GLU 1196 1207 ?   ?   ?   B . n 
B 2 1197 GLN 1197 1208 ?   ?   ?   B . n 
B 2 1198 TYR 1198 1209 ?   ?   ?   B . n 
B 2 1199 ILE 1199 1210 ?   ?   ?   B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 3 NAG 1 C NAG 1 C NAG 1 n 
C 3 NAG 2 C NAG 2 C NAG 2 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                     8YKH 
_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                         8YKH 
_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                   8YKH 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8YKH 
_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' ? 0.004 ? 3414 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.592 ? 4644 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.544 ? 480  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.046 ? 508  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 597  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8YKH 
_struct.title                        'Structure of SARS-CoV-2 spike RBD in complex with NT-108 scFv' 
_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        8YKH 
_struct_keywords.text            'Antibody, Complex, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
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 PDB 8YKH        8YKH   ? 1 ? 1  
2 UNP SPIKE_SARS2 P0DTC2 ? 2 
;SSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVY
FASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYV
SQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTP
GDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPN
ITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIA
PGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFP
LQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIAD
TTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLI
GAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSM
TKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSK
PSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAG
AALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFG
AISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMS
FPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIG
IVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYI
;
12 
# 
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 8YKH A 1 ? 251  ? 8YKH   0  ? 250  ? 0  250  
2 2 8YKH B 1 ? 1199 ? P0DTC2 12 ? 1210 ? 12 1210 
# 
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 
2 8YKH GLY B 671 ? UNP P0DTC2 ARG 682 'engineered mutation' 682 1 
2 8YKH SER B 672 ? UNP P0DTC2 ARG 683 'engineered mutation' 683 2 
2 8YKH GLY B 674 ? UNP P0DTC2 ARG 685 'engineered mutation' 685 3 
2 8YKH PRO B 806 ? UNP P0DTC2 PHE 817 'engineered mutation' 817 4 
2 8YKH PRO B 881 ? UNP P0DTC2 ALA 892 'engineered mutation' 892 5 
2 8YKH PRO B 888 ? UNP P0DTC2 ALA 899 'engineered mutation' 899 6 
2 8YKH PRO B 931 ? UNP P0DTC2 ALA 942 'engineered mutation' 942 7 
2 8YKH PRO B 975 ? UNP P0DTC2 LYS 986 'engineered mutation' 986 8 
2 8YKH PRO B 976 ? UNP P0DTC2 VAL 987 'engineered mutation' 987 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 GLY A 187 ? SER A 191 ? GLY A 186 SER A 190 5 ? 5 
HELX_P HELX_P2 AA2 THR A 212 ? THR A 216 ? THR A 211 THR A 215 5 ? 5 
HELX_P HELX_P3 AA3 VAL A 227 ? GLY A 229 ? VAL A 226 GLY A 228 5 ? 3 
HELX_P HELX_P4 AA4 PRO B 326 ? ASN B 332 ? PRO B 337 ASN B 343 1 ? 7 
HELX_P HELX_P5 AA5 SER B 338 ? TRP B 342 ? SER B 349 TRP B 353 5 ? 5 
HELX_P HELX_P6 AA6 TYR B 354 ? ASN B 359 ? TYR B 365 ASN B 370 1 ? 6 
HELX_P HELX_P7 AA7 ASP B 394 ? ILE B 399 ? ASP B 405 ILE B 410 5 ? 6 
HELX_P HELX_P8 AA8 GLY B 405 ? ASN B 411 ? GLY B 416 ASN B 422 1 ? 7 
HELX_P HELX_P9 AA9 GLY B 491 ? TYR B 494 ? GLY B 502 TYR B 505 5 ? 4 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 23  SG  ? ? ? 1_555 A CYS 89  SG ? ? A CYS 22  A CYS 88  1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf2 disulf ?    ? A CYS 144 SG  ? ? ? 1_555 A CYS 221 SG ? ? A CYS 143 A CYS 220 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf3 disulf ?    ? B CYS 325 SG  ? ? ? 1_555 B CYS 350 SG ? ? B CYS 336 B CYS 361 1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf4 disulf ?    ? B CYS 368 SG  ? ? ? 1_555 B CYS 421 SG ? ? B CYS 379 B CYS 432 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf5 disulf ?    ? B CYS 380 SG  ? ? ? 1_555 B CYS 514 SG ? ? B CYS 391 B CYS 525 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf6 disulf ?    ? B CYS 469 SG  ? ? ? 1_555 B CYS 477 SG ? ? B CYS 480 B CYS 488 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
covale1 covale one  ? B ASN 332 ND2 ? ? ? 1_555 C NAG .   C1 ? ? B ASN 343 C NAG 1   1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale2 covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.446 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG C .   ? ASN B 332 ? NAG C 1   ? 1_555 ASN B 343 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 CYS A 23  ? CYS A 89  ? CYS A 22  ? 1_555 CYS A 88  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
3 CYS A 144 ? CYS A 221 ? CYS A 143 ? 1_555 CYS A 220 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS B 325 ? CYS B 350 ? CYS B 336 ? 1_555 CYS B 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS B 368 ? CYS B 421 ? CYS B 379 ? 1_555 CYS B 432 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS B 380 ? CYS B 514 ? CYS B 391 ? 1_555 CYS B 525 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS B 469 ? CYS B 477 ? CYS B 480 ? 1_555 CYS B 488 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 6 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 4   ? GLN A 6   ? LEU A 3   GLN A 5   
AA1 2 CYS A 23  ? ALA A 25  ? CYS A 22  ALA A 24  
AA1 3 ASP A 71  ? ILE A 76  ? ASP A 70  ILE A 75  
AA1 4 ALA A 19  ? THR A 20  ? ALA A 18  THR A 19  
AA2 1 LEU A 4   ? GLN A 6   ? LEU A 3   GLN A 5   
AA2 2 CYS A 23  ? ALA A 25  ? CYS A 22  ALA A 24  
AA2 3 ASP A 71  ? ILE A 76  ? ASP A 70  ILE A 75  
AA2 4 PHE A 63  ? SER A 68  ? PHE A 62  SER A 67  
AA3 1 THR A 10  ? LEU A 13  ? THR A 9   LEU A 12  
AA3 2 THR A 102 ? ILE A 106 ? THR A 101 ILE A 105 
AA3 3 ALA A 85  ? TYR A 87  ? ALA A 84  TYR A 86  
AA3 4 ALA A 35  ? GLN A 39  ? ALA A 34  GLN A 38  
AA3 5 ARG A 46  ? TYR A 50  ? ARG A 45  TYR A 49  
AA3 6 TYR A 54  ? MET A 55  ? TYR A 53  MET A 54  
AA4 1 GLN A 125 ? SER A 129 ? GLN A 124 SER A 128 
AA4 2 LEU A 140 ? SER A 147 ? LEU A 139 SER A 146 
AA4 3 GLN A 203 ? LEU A 208 ? GLN A 202 LEU A 207 
AA4 4 ILE A 193 ? ASP A 198 ? ILE A 192 ASP A 197 
AA5 1 LEU A 133 ? VAL A 134 ? LEU A 132 VAL A 133 
AA5 2 THR A 239 ? VAL A 243 ? THR A 238 VAL A 242 
AA5 3 ALA A 217 ? PHE A 220 ? ALA A 216 PHE A 219 
AA5 4 ALA A 156 ? SER A 164 ? ALA A 155 SER A 163 
AA5 5 GLY A 168 ? TYR A 177 ? GLY A 167 TYR A 176 
AA5 6 TRP A 181 ? TYR A 185 ? TRP A 180 TYR A 184 
AA6 1 LEU A 133 ? VAL A 134 ? LEU A 132 VAL A 133 
AA6 2 THR A 239 ? VAL A 243 ? THR A 238 VAL A 242 
AA6 3 ALA A 217 ? PHE A 220 ? ALA A 216 PHE A 219 
AA6 4 ALA A 156 ? SER A 164 ? ALA A 155 SER A 163 
AA6 5 ARG A 223 ? ILE A 225 ? ARG A 222 ILE A 224 
AA6 6 PHE A 232 ? ILE A 234 ? PHE A 231 ILE A 233 
AA7 1 ASN B 343 ? ILE B 347 ? ASN B 354 ILE B 358 
AA7 2 VAL B 384 ? ARG B 392 ? VAL B 395 ARG B 403 
AA7 3 PRO B 496 ? PHE B 504 ? PRO B 507 PHE B 515 
AA7 4 GLY B 420 ? ASN B 426 ? GLY B 431 ASN B 437 
AA7 5 THR B 365 ? TYR B 369 ? THR B 376 TYR B 380 
AA8 1 LEU B 441 ? ARG B 443 ? LEU B 452 ARG B 454 
AA8 2 LEU B 481 ? SER B 483 ? LEU B 492 SER B 494 
AA9 1 TYR B 462 ? GLN B 463 ? TYR B 473 GLN B 474 
AA9 2 CYS B 477 ? TYR B 478 ? CYS B 488 TYR B 489 
# 
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 5   ? N THR A 4   O ARG A 24  ? O ARG A 23  
AA1 2 3 N CYS A 23  ? N CYS A 22  O PHE A 72  ? O PHE A 71  
AA1 3 4 O ILE A 76  ? O ILE A 75  N ALA A 19  ? N ALA A 18  
AA2 1 2 N THR A 5   ? N THR A 4   O ARG A 24  ? O ARG A 23  
AA2 2 3 N CYS A 23  ? N CYS A 22  O PHE A 72  ? O PHE A 71  
AA2 3 4 O THR A 73  ? O THR A 72  N SER A 66  ? N SER A 65  
AA3 1 2 N LEU A 13  ? N LEU A 12  O GLU A 105 ? O GLU A 104 
AA3 2 3 O LEU A 104 ? O LEU A 103 N ALA A 85  ? N ALA A 84  
AA3 3 4 O VAL A 86  ? O VAL A 85  N GLN A 39  ? N GLN A 38  
AA3 4 5 N GLN A 38  ? N GLN A 37  O ARG A 46  ? O ARG A 45  
AA3 5 6 N TYR A 50  ? N TYR A 49  O TYR A 54  ? O TYR A 53  
AA4 1 2 N GLN A 125 ? N GLN A 124 O SER A 147 ? O SER A 146 
AA4 2 3 N CYS A 144 ? N CYS A 143 O PHE A 204 ? O PHE A 203 
AA4 3 4 O HIS A 207 ? O HIS A 206 N ALA A 194 ? N ALA A 193 
AA5 1 2 N VAL A 134 ? N VAL A 133 O THR A 242 ? O THR A 241 
AA5 2 3 O THR A 239 ? O THR A 238 N TYR A 219 ? N TYR A 218 
AA5 3 4 O PHE A 220 ? O PHE A 219 N ILE A 161 ? N ILE A 160 
AA5 4 5 N ARG A 162 ? N ARG A 161 O GLU A 170 ? O GLU A 169 
AA5 5 6 N TYR A 176 ? N TYR A 175 O TYR A 182 ? O TYR A 181 
AA6 1 2 N VAL A 134 ? N VAL A 133 O THR A 242 ? O THR A 241 
AA6 2 3 O THR A 239 ? O THR A 238 N TYR A 219 ? N TYR A 218 
AA6 3 4 O PHE A 220 ? O PHE A 219 N ILE A 161 ? N ILE A 160 
AA6 4 5 N ALA A 157 ? N ALA A 156 O VAL A 224 ? O VAL A 223 
AA6 5 6 N ARG A 223 ? N ARG A 222 O ILE A 234 ? O ILE A 233 
AA7 1 2 N LYS B 345 ? N LYS B 356 O ALA B 386 ? O ALA B 397 
AA7 2 3 N ILE B 391 ? N ILE B 402 O TYR B 497 ? O TYR B 508 
AA7 3 4 O VAL B 500 ? O VAL B 511 N ILE B 423 ? N ILE B 434 
AA7 4 5 O VAL B 422 ? O VAL B 433 N LYS B 367 ? N LYS B 378 
AA8 1 2 N TYR B 442 ? N TYR B 453 O GLN B 482 ? O GLN B 493 
AA9 1 2 N TYR B 462 ? N TYR B 473 O TYR B 478 ? O TYR B 489 
# 
_pdbx_entry_details.entry_id                   8YKH 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 51  ? ? 73.76   -9.06  
2 1 PHE A 83  ? ? -69.09  95.77  
3 1 SER A 151 ? ? -94.24  31.10  
4 1 PRO B 337 ? ? -78.66  46.68  
5 1 ASN B 370 ? ? -91.12  51.25  
6 1 THR B 385 ? ? 68.35   -4.41  
7 1 LEU B 390 ? ? 70.03   144.39 
8 1 CYS B 525 ? ? -170.88 146.31 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8YKH 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  8YK4 
_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                8YK4 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    8YKH 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'FOURIER SPACE' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.27 
_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               124137 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          2 
_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       PBS 
_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 'SARS-CoV-2 spike glycoprotein in complex with NT-108 scFv' ? ? ? '1, 2' 
2 1 RECOMBINANT        COMPLEX 'SARS-CoV-2 spike glycoprotein'                             ? ? ? 2      
3 1 RECOMBINANT        COMPLEX 'NT-108 scFv'                                               ? ? ? 1      
# 
_em_image_scans.entry_id                8YKH 
_em_image_scans.id                      1 
_em_image_scans.number_digital_images   ? 
_em_image_scans.details                 ? 
_em_image_scans.scanner_model           ? 
_em_image_scans.sampling_size           ? 
_em_image_scans.od_range                ? 
_em_image_scans.quant_bit_size          ? 
_em_image_scans.citation_id             ? 
_em_image_scans.dimension_height        4092 
_em_image_scans.dimension_width         5760 
_em_image_scans.frames_per_image        ? 
_em_image_scans.image_recording_id      1 
_em_image_scans.used_frames_per_image   ? 
# 
_em_imaging.entry_id                        8YKH 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             1800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           130000 
_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             'COMA FREE' 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              8YKH 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   291 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               'blotting time 5 s and blotting force 5.' 
# 
_em_experiment.entry_id                8YKH 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              8YKH 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A GLU 0    ? A GLU 1    
2    1 Y 1 A GLY 107  ? A GLY 108  
3    1 Y 1 A GLY 108  ? A GLY 109  
4    1 Y 1 A GLY 109  ? A GLY 110  
5    1 Y 1 A GLY 110  ? A GLY 111  
6    1 Y 1 A SER 111  ? A SER 112  
7    1 Y 1 A GLY 112  ? A GLY 113  
8    1 Y 1 A GLY 113  ? A GLY 114  
9    1 Y 1 A GLY 114  ? A GLY 115  
10   1 Y 1 A GLY 115  ? A GLY 116  
11   1 Y 1 A SER 116  ? A SER 117  
12   1 Y 1 A GLY 117  ? A GLY 118  
13   1 Y 1 A GLY 118  ? A GLY 119  
14   1 Y 1 A GLY 119  ? A GLY 120  
15   1 Y 1 A GLY 120  ? A GLY 121  
16   1 Y 1 A HIS 245  ? A HIS 246  
17   1 Y 1 A HIS 246  ? A HIS 247  
18   1 Y 1 A HIS 247  ? A HIS 248  
19   1 Y 1 A HIS 248  ? A HIS 249  
20   1 Y 1 A HIS 249  ? A HIS 250  
21   1 Y 1 A HIS 250  ? A HIS 251  
22   1 Y 1 B SER 12   ? B SER 1    
23   1 Y 1 B SER 13   ? B SER 2    
24   1 Y 1 B GLN 14   ? B GLN 3    
25   1 Y 1 B CYS 15   ? B CYS 4    
26   1 Y 1 B VAL 16   ? B VAL 5    
27   1 Y 1 B ASN 17   ? B ASN 6    
28   1 Y 1 B LEU 18   ? B LEU 7    
29   1 Y 1 B THR 19   ? B THR 8    
30   1 Y 1 B THR 20   ? B THR 9    
31   1 Y 1 B ARG 21   ? B ARG 10   
32   1 Y 1 B THR 22   ? B THR 11   
33   1 Y 1 B GLN 23   ? B GLN 12   
34   1 Y 1 B LEU 24   ? B LEU 13   
35   1 Y 1 B PRO 25   ? B PRO 14   
36   1 Y 1 B PRO 26   ? B PRO 15   
37   1 Y 1 B ALA 27   ? B ALA 16   
38   1 Y 1 B TYR 28   ? B TYR 17   
39   1 Y 1 B THR 29   ? B THR 18   
40   1 Y 1 B ASN 30   ? B ASN 19   
41   1 Y 1 B SER 31   ? B SER 20   
42   1 Y 1 B PHE 32   ? B PHE 21   
43   1 Y 1 B THR 33   ? B THR 22   
44   1 Y 1 B ARG 34   ? B ARG 23   
45   1 Y 1 B GLY 35   ? B GLY 24   
46   1 Y 1 B VAL 36   ? B VAL 25   
47   1 Y 1 B TYR 37   ? B TYR 26   
48   1 Y 1 B TYR 38   ? B TYR 27   
49   1 Y 1 B PRO 39   ? B PRO 28   
50   1 Y 1 B ASP 40   ? B ASP 29   
51   1 Y 1 B LYS 41   ? B LYS 30   
52   1 Y 1 B VAL 42   ? B VAL 31   
53   1 Y 1 B PHE 43   ? B PHE 32   
54   1 Y 1 B ARG 44   ? B ARG 33   
55   1 Y 1 B SER 45   ? B SER 34   
56   1 Y 1 B SER 46   ? B SER 35   
57   1 Y 1 B VAL 47   ? B VAL 36   
58   1 Y 1 B LEU 48   ? B LEU 37   
59   1 Y 1 B HIS 49   ? B HIS 38   
60   1 Y 1 B SER 50   ? B SER 39   
61   1 Y 1 B THR 51   ? B THR 40   
62   1 Y 1 B GLN 52   ? B GLN 41   
63   1 Y 1 B ASP 53   ? B ASP 42   
64   1 Y 1 B LEU 54   ? B LEU 43   
65   1 Y 1 B PHE 55   ? B PHE 44   
66   1 Y 1 B LEU 56   ? B LEU 45   
67   1 Y 1 B PRO 57   ? B PRO 46   
68   1 Y 1 B PHE 58   ? B PHE 47   
69   1 Y 1 B PHE 59   ? B PHE 48   
70   1 Y 1 B SER 60   ? B SER 49   
71   1 Y 1 B ASN 61   ? B ASN 50   
72   1 Y 1 B VAL 62   ? B VAL 51   
73   1 Y 1 B THR 63   ? B THR 52   
74   1 Y 1 B TRP 64   ? B TRP 53   
75   1 Y 1 B PHE 65   ? B PHE 54   
76   1 Y 1 B HIS 66   ? B HIS 55   
77   1 Y 1 B ALA 67   ? B ALA 56   
78   1 Y 1 B ILE 68   ? B ILE 57   
79   1 Y 1 B HIS 69   ? B HIS 58   
80   1 Y 1 B VAL 70   ? B VAL 59   
81   1 Y 1 B SER 71   ? B SER 60   
82   1 Y 1 B GLY 72   ? B GLY 61   
83   1 Y 1 B THR 73   ? B THR 62   
84   1 Y 1 B ASN 74   ? B ASN 63   
85   1 Y 1 B GLY 75   ? B GLY 64   
86   1 Y 1 B THR 76   ? B THR 65   
87   1 Y 1 B LYS 77   ? B LYS 66   
88   1 Y 1 B ARG 78   ? B ARG 67   
89   1 Y 1 B PHE 79   ? B PHE 68   
90   1 Y 1 B ASP 80   ? B ASP 69   
91   1 Y 1 B ASN 81   ? B ASN 70   
92   1 Y 1 B PRO 82   ? B PRO 71   
93   1 Y 1 B VAL 83   ? B VAL 72   
94   1 Y 1 B LEU 84   ? B LEU 73   
95   1 Y 1 B PRO 85   ? B PRO 74   
96   1 Y 1 B PHE 86   ? B PHE 75   
97   1 Y 1 B ASN 87   ? B ASN 76   
98   1 Y 1 B ASP 88   ? B ASP 77   
99   1 Y 1 B GLY 89   ? B GLY 78   
100  1 Y 1 B VAL 90   ? B VAL 79   
101  1 Y 1 B TYR 91   ? B TYR 80   
102  1 Y 1 B PHE 92   ? B PHE 81   
103  1 Y 1 B ALA 93   ? B ALA 82   
104  1 Y 1 B SER 94   ? B SER 83   
105  1 Y 1 B THR 95   ? B THR 84   
106  1 Y 1 B GLU 96   ? B GLU 85   
107  1 Y 1 B LYS 97   ? B LYS 86   
108  1 Y 1 B SER 98   ? B SER 87   
109  1 Y 1 B ASN 99   ? B ASN 88   
110  1 Y 1 B ILE 100  ? B ILE 89   
111  1 Y 1 B ILE 101  ? B ILE 90   
112  1 Y 1 B ARG 102  ? B ARG 91   
113  1 Y 1 B GLY 103  ? B GLY 92   
114  1 Y 1 B TRP 104  ? B TRP 93   
115  1 Y 1 B ILE 105  ? B ILE 94   
116  1 Y 1 B PHE 106  ? B PHE 95   
117  1 Y 1 B GLY 107  ? B GLY 96   
118  1 Y 1 B THR 108  ? B THR 97   
119  1 Y 1 B THR 109  ? B THR 98   
120  1 Y 1 B LEU 110  ? B LEU 99   
121  1 Y 1 B ASP 111  ? B ASP 100  
122  1 Y 1 B SER 112  ? B SER 101  
123  1 Y 1 B LYS 113  ? B LYS 102  
124  1 Y 1 B THR 114  ? B THR 103  
125  1 Y 1 B GLN 115  ? B GLN 104  
126  1 Y 1 B SER 116  ? B SER 105  
127  1 Y 1 B LEU 117  ? B LEU 106  
128  1 Y 1 B LEU 118  ? B LEU 107  
129  1 Y 1 B ILE 119  ? B ILE 108  
130  1 Y 1 B VAL 120  ? B VAL 109  
131  1 Y 1 B ASN 121  ? B ASN 110  
132  1 Y 1 B ASN 122  ? B ASN 111  
133  1 Y 1 B ALA 123  ? B ALA 112  
134  1 Y 1 B THR 124  ? B THR 113  
135  1 Y 1 B ASN 125  ? B ASN 114  
136  1 Y 1 B VAL 126  ? B VAL 115  
137  1 Y 1 B VAL 127  ? B VAL 116  
138  1 Y 1 B ILE 128  ? B ILE 117  
139  1 Y 1 B LYS 129  ? B LYS 118  
140  1 Y 1 B VAL 130  ? B VAL 119  
141  1 Y 1 B CYS 131  ? B CYS 120  
142  1 Y 1 B GLU 132  ? B GLU 121  
143  1 Y 1 B PHE 133  ? B PHE 122  
144  1 Y 1 B GLN 134  ? B GLN 123  
145  1 Y 1 B PHE 135  ? B PHE 124  
146  1 Y 1 B CYS 136  ? B CYS 125  
147  1 Y 1 B ASN 137  ? B ASN 126  
148  1 Y 1 B ASP 138  ? B ASP 127  
149  1 Y 1 B PRO 139  ? B PRO 128  
150  1 Y 1 B PHE 140  ? B PHE 129  
151  1 Y 1 B LEU 141  ? B LEU 130  
152  1 Y 1 B GLY 142  ? B GLY 131  
153  1 Y 1 B VAL 143  ? B VAL 132  
154  1 Y 1 B TYR 144  ? B TYR 133  
155  1 Y 1 B TYR 145  ? B TYR 134  
156  1 Y 1 B HIS 146  ? B HIS 135  
157  1 Y 1 B LYS 147  ? B LYS 136  
158  1 Y 1 B ASN 148  ? B ASN 137  
159  1 Y 1 B ASN 149  ? B ASN 138  
160  1 Y 1 B LYS 150  ? B LYS 139  
161  1 Y 1 B SER 151  ? B SER 140  
162  1 Y 1 B TRP 152  ? B TRP 141  
163  1 Y 1 B MET 153  ? B MET 142  
164  1 Y 1 B GLU 154  ? B GLU 143  
165  1 Y 1 B SER 155  ? B SER 144  
166  1 Y 1 B GLU 156  ? B GLU 145  
167  1 Y 1 B PHE 157  ? B PHE 146  
168  1 Y 1 B ARG 158  ? B ARG 147  
169  1 Y 1 B VAL 159  ? B VAL 148  
170  1 Y 1 B TYR 160  ? B TYR 149  
171  1 Y 1 B SER 161  ? B SER 150  
172  1 Y 1 B SER 162  ? B SER 151  
173  1 Y 1 B ALA 163  ? B ALA 152  
174  1 Y 1 B ASN 164  ? B ASN 153  
175  1 Y 1 B ASN 165  ? B ASN 154  
176  1 Y 1 B CYS 166  ? B CYS 155  
177  1 Y 1 B THR 167  ? B THR 156  
178  1 Y 1 B PHE 168  ? B PHE 157  
179  1 Y 1 B GLU 169  ? B GLU 158  
180  1 Y 1 B TYR 170  ? B TYR 159  
181  1 Y 1 B VAL 171  ? B VAL 160  
182  1 Y 1 B SER 172  ? B SER 161  
183  1 Y 1 B GLN 173  ? B GLN 162  
184  1 Y 1 B PRO 174  ? B PRO 163  
185  1 Y 1 B PHE 175  ? B PHE 164  
186  1 Y 1 B LEU 176  ? B LEU 165  
187  1 Y 1 B MET 177  ? B MET 166  
188  1 Y 1 B ASP 178  ? B ASP 167  
189  1 Y 1 B LEU 179  ? B LEU 168  
190  1 Y 1 B GLU 180  ? B GLU 169  
191  1 Y 1 B GLY 181  ? B GLY 170  
192  1 Y 1 B LYS 182  ? B LYS 171  
193  1 Y 1 B GLN 183  ? B GLN 172  
194  1 Y 1 B GLY 184  ? B GLY 173  
195  1 Y 1 B ASN 185  ? B ASN 174  
196  1 Y 1 B PHE 186  ? B PHE 175  
197  1 Y 1 B LYS 187  ? B LYS 176  
198  1 Y 1 B ASN 188  ? B ASN 177  
199  1 Y 1 B LEU 189  ? B LEU 178  
200  1 Y 1 B ARG 190  ? B ARG 179  
201  1 Y 1 B GLU 191  ? B GLU 180  
202  1 Y 1 B PHE 192  ? B PHE 181  
203  1 Y 1 B VAL 193  ? B VAL 182  
204  1 Y 1 B PHE 194  ? B PHE 183  
205  1 Y 1 B LYS 195  ? B LYS 184  
206  1 Y 1 B ASN 196  ? B ASN 185  
207  1 Y 1 B ILE 197  ? B ILE 186  
208  1 Y 1 B ASP 198  ? B ASP 187  
209  1 Y 1 B GLY 199  ? B GLY 188  
210  1 Y 1 B TYR 200  ? B TYR 189  
211  1 Y 1 B PHE 201  ? B PHE 190  
212  1 Y 1 B LYS 202  ? B LYS 191  
213  1 Y 1 B ILE 203  ? B ILE 192  
214  1 Y 1 B TYR 204  ? B TYR 193  
215  1 Y 1 B SER 205  ? B SER 194  
216  1 Y 1 B LYS 206  ? B LYS 195  
217  1 Y 1 B HIS 207  ? B HIS 196  
218  1 Y 1 B THR 208  ? B THR 197  
219  1 Y 1 B PRO 209  ? B PRO 198  
220  1 Y 1 B ILE 210  ? B ILE 199  
221  1 Y 1 B ASN 211  ? B ASN 200  
222  1 Y 1 B LEU 212  ? B LEU 201  
223  1 Y 1 B VAL 213  ? B VAL 202  
224  1 Y 1 B ARG 214  ? B ARG 203  
225  1 Y 1 B ASP 215  ? B ASP 204  
226  1 Y 1 B LEU 216  ? B LEU 205  
227  1 Y 1 B PRO 217  ? B PRO 206  
228  1 Y 1 B GLN 218  ? B GLN 207  
229  1 Y 1 B GLY 219  ? B GLY 208  
230  1 Y 1 B PHE 220  ? B PHE 209  
231  1 Y 1 B SER 221  ? B SER 210  
232  1 Y 1 B ALA 222  ? B ALA 211  
233  1 Y 1 B LEU 223  ? B LEU 212  
234  1 Y 1 B GLU 224  ? B GLU 213  
235  1 Y 1 B PRO 225  ? B PRO 214  
236  1 Y 1 B LEU 226  ? B LEU 215  
237  1 Y 1 B VAL 227  ? B VAL 216  
238  1 Y 1 B ASP 228  ? B ASP 217  
239  1 Y 1 B LEU 229  ? B LEU 218  
240  1 Y 1 B PRO 230  ? B PRO 219  
241  1 Y 1 B ILE 231  ? B ILE 220  
242  1 Y 1 B GLY 232  ? B GLY 221  
243  1 Y 1 B ILE 233  ? B ILE 222  
244  1 Y 1 B ASN 234  ? B ASN 223  
245  1 Y 1 B ILE 235  ? B ILE 224  
246  1 Y 1 B THR 236  ? B THR 225  
247  1 Y 1 B ARG 237  ? B ARG 226  
248  1 Y 1 B PHE 238  ? B PHE 227  
249  1 Y 1 B GLN 239  ? B GLN 228  
250  1 Y 1 B THR 240  ? B THR 229  
251  1 Y 1 B LEU 241  ? B LEU 230  
252  1 Y 1 B LEU 242  ? B LEU 231  
253  1 Y 1 B ALA 243  ? B ALA 232  
254  1 Y 1 B LEU 244  ? B LEU 233  
255  1 Y 1 B HIS 245  ? B HIS 234  
256  1 Y 1 B ARG 246  ? B ARG 235  
257  1 Y 1 B SER 247  ? B SER 236  
258  1 Y 1 B TYR 248  ? B TYR 237  
259  1 Y 1 B LEU 249  ? B LEU 238  
260  1 Y 1 B THR 250  ? B THR 239  
261  1 Y 1 B PRO 251  ? B PRO 240  
262  1 Y 1 B GLY 252  ? B GLY 241  
263  1 Y 1 B ASP 253  ? B ASP 242  
264  1 Y 1 B SER 254  ? B SER 243  
265  1 Y 1 B SER 255  ? B SER 244  
266  1 Y 1 B SER 256  ? B SER 245  
267  1 Y 1 B GLY 257  ? B GLY 246  
268  1 Y 1 B TRP 258  ? B TRP 247  
269  1 Y 1 B THR 259  ? B THR 248  
270  1 Y 1 B ALA 260  ? B ALA 249  
271  1 Y 1 B GLY 261  ? B GLY 250  
272  1 Y 1 B ALA 262  ? B ALA 251  
273  1 Y 1 B ALA 263  ? B ALA 252  
274  1 Y 1 B ALA 264  ? B ALA 253  
275  1 Y 1 B TYR 265  ? B TYR 254  
276  1 Y 1 B TYR 266  ? B TYR 255  
277  1 Y 1 B VAL 267  ? B VAL 256  
278  1 Y 1 B GLY 268  ? B GLY 257  
279  1 Y 1 B TYR 269  ? B TYR 258  
280  1 Y 1 B LEU 270  ? B LEU 259  
281  1 Y 1 B GLN 271  ? B GLN 260  
282  1 Y 1 B PRO 272  ? B PRO 261  
283  1 Y 1 B ARG 273  ? B ARG 262  
284  1 Y 1 B THR 274  ? B THR 263  
285  1 Y 1 B PHE 275  ? B PHE 264  
286  1 Y 1 B LEU 276  ? B LEU 265  
287  1 Y 1 B LEU 277  ? B LEU 266  
288  1 Y 1 B LYS 278  ? B LYS 267  
289  1 Y 1 B TYR 279  ? B TYR 268  
290  1 Y 1 B ASN 280  ? B ASN 269  
291  1 Y 1 B GLU 281  ? B GLU 270  
292  1 Y 1 B ASN 282  ? B ASN 271  
293  1 Y 1 B GLY 283  ? B GLY 272  
294  1 Y 1 B THR 284  ? B THR 273  
295  1 Y 1 B ILE 285  ? B ILE 274  
296  1 Y 1 B THR 286  ? B THR 275  
297  1 Y 1 B ASP 287  ? B ASP 276  
298  1 Y 1 B ALA 288  ? B ALA 277  
299  1 Y 1 B VAL 289  ? B VAL 278  
300  1 Y 1 B ASP 290  ? B ASP 279  
301  1 Y 1 B CYS 291  ? B CYS 280  
302  1 Y 1 B ALA 292  ? B ALA 281  
303  1 Y 1 B LEU 293  ? B LEU 282  
304  1 Y 1 B ASP 294  ? B ASP 283  
305  1 Y 1 B PRO 295  ? B PRO 284  
306  1 Y 1 B LEU 296  ? B LEU 285  
307  1 Y 1 B SER 297  ? B SER 286  
308  1 Y 1 B GLU 298  ? B GLU 287  
309  1 Y 1 B THR 299  ? B THR 288  
310  1 Y 1 B LYS 300  ? B LYS 289  
311  1 Y 1 B CYS 301  ? B CYS 290  
312  1 Y 1 B THR 302  ? B THR 291  
313  1 Y 1 B LEU 303  ? B LEU 292  
314  1 Y 1 B LYS 304  ? B LYS 293  
315  1 Y 1 B SER 305  ? B SER 294  
316  1 Y 1 B PHE 306  ? B PHE 295  
317  1 Y 1 B THR 307  ? B THR 296  
318  1 Y 1 B VAL 308  ? B VAL 297  
319  1 Y 1 B GLU 309  ? B GLU 298  
320  1 Y 1 B LYS 310  ? B LYS 299  
321  1 Y 1 B GLY 311  ? B GLY 300  
322  1 Y 1 B ILE 312  ? B ILE 301  
323  1 Y 1 B TYR 313  ? B TYR 302  
324  1 Y 1 B GLN 314  ? B GLN 303  
325  1 Y 1 B THR 315  ? B THR 304  
326  1 Y 1 B SER 316  ? B SER 305  
327  1 Y 1 B ASN 317  ? B ASN 306  
328  1 Y 1 B PHE 318  ? B PHE 307  
329  1 Y 1 B ARG 319  ? B ARG 308  
330  1 Y 1 B VAL 320  ? B VAL 309  
331  1 Y 1 B GLN 321  ? B GLN 310  
332  1 Y 1 B PRO 322  ? B PRO 311  
333  1 Y 1 B THR 323  ? B THR 312  
334  1 Y 1 B GLU 324  ? B GLU 313  
335  1 Y 1 B SER 325  ? B SER 314  
336  1 Y 1 B ILE 326  ? B ILE 315  
337  1 Y 1 B VAL 327  ? B VAL 316  
338  1 Y 1 B ARG 328  ? B ARG 317  
339  1 Y 1 B PHE 329  ? B PHE 318  
340  1 Y 1 B PRO 330  ? B PRO 319  
341  1 Y 1 B LEU 518  ? B LEU 507  
342  1 Y 1 B HIS 519  ? B HIS 508  
343  1 Y 1 B LYS 528  ? B LYS 517  
344  1 Y 1 B LYS 529  ? B LYS 518  
345  1 Y 1 B SER 530  ? B SER 519  
346  1 Y 1 B THR 531  ? B THR 520  
347  1 Y 1 B ASN 532  ? B ASN 521  
348  1 Y 1 B LEU 533  ? B LEU 522  
349  1 Y 1 B VAL 534  ? B VAL 523  
350  1 Y 1 B LYS 535  ? B LYS 524  
351  1 Y 1 B ASN 536  ? B ASN 525  
352  1 Y 1 B LYS 537  ? B LYS 526  
353  1 Y 1 B CYS 538  ? B CYS 527  
354  1 Y 1 B VAL 539  ? B VAL 528  
355  1 Y 1 B ASN 540  ? B ASN 529  
356  1 Y 1 B PHE 541  ? B PHE 530  
357  1 Y 1 B ASN 542  ? B ASN 531  
358  1 Y 1 B PHE 543  ? B PHE 532  
359  1 Y 1 B ASN 544  ? B ASN 533  
360  1 Y 1 B GLY 545  ? B GLY 534  
361  1 Y 1 B LEU 546  ? B LEU 535  
362  1 Y 1 B THR 547  ? B THR 536  
363  1 Y 1 B GLY 548  ? B GLY 537  
364  1 Y 1 B THR 549  ? B THR 538  
365  1 Y 1 B GLY 550  ? B GLY 539  
366  1 Y 1 B VAL 551  ? B VAL 540  
367  1 Y 1 B LEU 552  ? B LEU 541  
368  1 Y 1 B THR 553  ? B THR 542  
369  1 Y 1 B GLU 554  ? B GLU 543  
370  1 Y 1 B SER 555  ? B SER 544  
371  1 Y 1 B ASN 556  ? B ASN 545  
372  1 Y 1 B LYS 557  ? B LYS 546  
373  1 Y 1 B LYS 558  ? B LYS 547  
374  1 Y 1 B PHE 559  ? B PHE 548  
375  1 Y 1 B LEU 560  ? B LEU 549  
376  1 Y 1 B PRO 561  ? B PRO 550  
377  1 Y 1 B PHE 562  ? B PHE 551  
378  1 Y 1 B GLN 563  ? B GLN 552  
379  1 Y 1 B GLN 564  ? B GLN 553  
380  1 Y 1 B PHE 565  ? B PHE 554  
381  1 Y 1 B GLY 566  ? B GLY 555  
382  1 Y 1 B ARG 567  ? B ARG 556  
383  1 Y 1 B ASP 568  ? B ASP 557  
384  1 Y 1 B ILE 569  ? B ILE 558  
385  1 Y 1 B ALA 570  ? B ALA 559  
386  1 Y 1 B ASP 571  ? B ASP 560  
387  1 Y 1 B THR 572  ? B THR 561  
388  1 Y 1 B THR 573  ? B THR 562  
389  1 Y 1 B ASP 574  ? B ASP 563  
390  1 Y 1 B ALA 575  ? B ALA 564  
391  1 Y 1 B VAL 576  ? B VAL 565  
392  1 Y 1 B ARG 577  ? B ARG 566  
393  1 Y 1 B ASP 578  ? B ASP 567  
394  1 Y 1 B PRO 579  ? B PRO 568  
395  1 Y 1 B GLN 580  ? B GLN 569  
396  1 Y 1 B THR 581  ? B THR 570  
397  1 Y 1 B LEU 582  ? B LEU 571  
398  1 Y 1 B GLU 583  ? B GLU 572  
399  1 Y 1 B ILE 584  ? B ILE 573  
400  1 Y 1 B LEU 585  ? B LEU 574  
401  1 Y 1 B ASP 586  ? B ASP 575  
402  1 Y 1 B ILE 587  ? B ILE 576  
403  1 Y 1 B THR 588  ? B THR 577  
404  1 Y 1 B PRO 589  ? B PRO 578  
405  1 Y 1 B CYS 590  ? B CYS 579  
406  1 Y 1 B SER 591  ? B SER 580  
407  1 Y 1 B PHE 592  ? B PHE 581  
408  1 Y 1 B GLY 593  ? B GLY 582  
409  1 Y 1 B GLY 594  ? B GLY 583  
410  1 Y 1 B VAL 595  ? B VAL 584  
411  1 Y 1 B SER 596  ? B SER 585  
412  1 Y 1 B VAL 597  ? B VAL 586  
413  1 Y 1 B ILE 598  ? B ILE 587  
414  1 Y 1 B THR 599  ? B THR 588  
415  1 Y 1 B PRO 600  ? B PRO 589  
416  1 Y 1 B GLY 601  ? B GLY 590  
417  1 Y 1 B THR 602  ? B THR 591  
418  1 Y 1 B ASN 603  ? B ASN 592  
419  1 Y 1 B THR 604  ? B THR 593  
420  1 Y 1 B SER 605  ? B SER 594  
421  1 Y 1 B ASN 606  ? B ASN 595  
422  1 Y 1 B GLN 607  ? B GLN 596  
423  1 Y 1 B VAL 608  ? B VAL 597  
424  1 Y 1 B ALA 609  ? B ALA 598  
425  1 Y 1 B VAL 610  ? B VAL 599  
426  1 Y 1 B LEU 611  ? B LEU 600  
427  1 Y 1 B TYR 612  ? B TYR 601  
428  1 Y 1 B GLN 613  ? B GLN 602  
429  1 Y 1 B ASP 614  ? B ASP 603  
430  1 Y 1 B VAL 615  ? B VAL 604  
431  1 Y 1 B ASN 616  ? B ASN 605  
432  1 Y 1 B CYS 617  ? B CYS 606  
433  1 Y 1 B THR 618  ? B THR 607  
434  1 Y 1 B GLU 619  ? B GLU 608  
435  1 Y 1 B VAL 620  ? B VAL 609  
436  1 Y 1 B PRO 621  ? B PRO 610  
437  1 Y 1 B VAL 622  ? B VAL 611  
438  1 Y 1 B ALA 623  ? B ALA 612  
439  1 Y 1 B ILE 624  ? B ILE 613  
440  1 Y 1 B HIS 625  ? B HIS 614  
441  1 Y 1 B ALA 626  ? B ALA 615  
442  1 Y 1 B ASP 627  ? B ASP 616  
443  1 Y 1 B GLN 628  ? B GLN 617  
444  1 Y 1 B LEU 629  ? B LEU 618  
445  1 Y 1 B THR 630  ? B THR 619  
446  1 Y 1 B PRO 631  ? B PRO 620  
447  1 Y 1 B THR 632  ? B THR 621  
448  1 Y 1 B TRP 633  ? B TRP 622  
449  1 Y 1 B ARG 634  ? B ARG 623  
450  1 Y 1 B VAL 635  ? B VAL 624  
451  1 Y 1 B TYR 636  ? B TYR 625  
452  1 Y 1 B SER 637  ? B SER 626  
453  1 Y 1 B THR 638  ? B THR 627  
454  1 Y 1 B GLY 639  ? B GLY 628  
455  1 Y 1 B SER 640  ? B SER 629  
456  1 Y 1 B ASN 641  ? B ASN 630  
457  1 Y 1 B VAL 642  ? B VAL 631  
458  1 Y 1 B PHE 643  ? B PHE 632  
459  1 Y 1 B GLN 644  ? B GLN 633  
460  1 Y 1 B THR 645  ? B THR 634  
461  1 Y 1 B ARG 646  ? B ARG 635  
462  1 Y 1 B ALA 647  ? B ALA 636  
463  1 Y 1 B GLY 648  ? B GLY 637  
464  1 Y 1 B CYS 649  ? B CYS 638  
465  1 Y 1 B LEU 650  ? B LEU 639  
466  1 Y 1 B ILE 651  ? B ILE 640  
467  1 Y 1 B GLY 652  ? B GLY 641  
468  1 Y 1 B ALA 653  ? B ALA 642  
469  1 Y 1 B GLU 654  ? B GLU 643  
470  1 Y 1 B HIS 655  ? B HIS 644  
471  1 Y 1 B VAL 656  ? B VAL 645  
472  1 Y 1 B ASN 657  ? B ASN 646  
473  1 Y 1 B ASN 658  ? B ASN 647  
474  1 Y 1 B SER 659  ? B SER 648  
475  1 Y 1 B TYR 660  ? B TYR 649  
476  1 Y 1 B GLU 661  ? B GLU 650  
477  1 Y 1 B CYS 662  ? B CYS 651  
478  1 Y 1 B ASP 663  ? B ASP 652  
479  1 Y 1 B ILE 664  ? B ILE 653  
480  1 Y 1 B PRO 665  ? B PRO 654  
481  1 Y 1 B ILE 666  ? B ILE 655  
482  1 Y 1 B GLY 667  ? B GLY 656  
483  1 Y 1 B ALA 668  ? B ALA 657  
484  1 Y 1 B GLY 669  ? B GLY 658  
485  1 Y 1 B ILE 670  ? B ILE 659  
486  1 Y 1 B CYS 671  ? B CYS 660  
487  1 Y 1 B ALA 672  ? B ALA 661  
488  1 Y 1 B SER 673  ? B SER 662  
489  1 Y 1 B TYR 674  ? B TYR 663  
490  1 Y 1 B GLN 675  ? B GLN 664  
491  1 Y 1 B THR 676  ? B THR 665  
492  1 Y 1 B GLN 677  ? B GLN 666  
493  1 Y 1 B THR 678  ? B THR 667  
494  1 Y 1 B ASN 679  ? B ASN 668  
495  1 Y 1 B SER 680  ? B SER 669  
496  1 Y 1 B PRO 681  ? B PRO 670  
497  1 Y 1 B GLY 682  ? B GLY 671  
498  1 Y 1 B SER 683  ? B SER 672  
499  1 Y 1 B ALA 684  ? B ALA 673  
500  1 Y 1 B GLY 685  ? B GLY 674  
501  1 Y 1 B SER 686  ? B SER 675  
502  1 Y 1 B VAL 687  ? B VAL 676  
503  1 Y 1 B ALA 688  ? B ALA 677  
504  1 Y 1 B SER 689  ? B SER 678  
505  1 Y 1 B GLN 690  ? B GLN 679  
506  1 Y 1 B SER 691  ? B SER 680  
507  1 Y 1 B ILE 692  ? B ILE 681  
508  1 Y 1 B ILE 693  ? B ILE 682  
509  1 Y 1 B ALA 694  ? B ALA 683  
510  1 Y 1 B TYR 695  ? B TYR 684  
511  1 Y 1 B THR 696  ? B THR 685  
512  1 Y 1 B MET 697  ? B MET 686  
513  1 Y 1 B SER 698  ? B SER 687  
514  1 Y 1 B LEU 699  ? B LEU 688  
515  1 Y 1 B GLY 700  ? B GLY 689  
516  1 Y 1 B ALA 701  ? B ALA 690  
517  1 Y 1 B GLU 702  ? B GLU 691  
518  1 Y 1 B ASN 703  ? B ASN 692  
519  1 Y 1 B SER 704  ? B SER 693  
520  1 Y 1 B VAL 705  ? B VAL 694  
521  1 Y 1 B ALA 706  ? B ALA 695  
522  1 Y 1 B TYR 707  ? B TYR 696  
523  1 Y 1 B SER 708  ? B SER 697  
524  1 Y 1 B ASN 709  ? B ASN 698  
525  1 Y 1 B ASN 710  ? B ASN 699  
526  1 Y 1 B SER 711  ? B SER 700  
527  1 Y 1 B ILE 712  ? B ILE 701  
528  1 Y 1 B ALA 713  ? B ALA 702  
529  1 Y 1 B ILE 714  ? B ILE 703  
530  1 Y 1 B PRO 715  ? B PRO 704  
531  1 Y 1 B THR 716  ? B THR 705  
532  1 Y 1 B ASN 717  ? B ASN 706  
533  1 Y 1 B PHE 718  ? B PHE 707  
534  1 Y 1 B THR 719  ? B THR 708  
535  1 Y 1 B ILE 720  ? B ILE 709  
536  1 Y 1 B SER 721  ? B SER 710  
537  1 Y 1 B VAL 722  ? B VAL 711  
538  1 Y 1 B THR 723  ? B THR 712  
539  1 Y 1 B THR 724  ? B THR 713  
540  1 Y 1 B GLU 725  ? B GLU 714  
541  1 Y 1 B ILE 726  ? B ILE 715  
542  1 Y 1 B LEU 727  ? B LEU 716  
543  1 Y 1 B PRO 728  ? B PRO 717  
544  1 Y 1 B VAL 729  ? B VAL 718  
545  1 Y 1 B SER 730  ? B SER 719  
546  1 Y 1 B MET 731  ? B MET 720  
547  1 Y 1 B THR 732  ? B THR 721  
548  1 Y 1 B LYS 733  ? B LYS 722  
549  1 Y 1 B THR 734  ? B THR 723  
550  1 Y 1 B SER 735  ? B SER 724  
551  1 Y 1 B VAL 736  ? B VAL 725  
552  1 Y 1 B ASP 737  ? B ASP 726  
553  1 Y 1 B CYS 738  ? B CYS 727  
554  1 Y 1 B THR 739  ? B THR 728  
555  1 Y 1 B MET 740  ? B MET 729  
556  1 Y 1 B TYR 741  ? B TYR 730  
557  1 Y 1 B ILE 742  ? B ILE 731  
558  1 Y 1 B CYS 743  ? B CYS 732  
559  1 Y 1 B GLY 744  ? B GLY 733  
560  1 Y 1 B ASP 745  ? B ASP 734  
561  1 Y 1 B SER 746  ? B SER 735  
562  1 Y 1 B THR 747  ? B THR 736  
563  1 Y 1 B GLU 748  ? B GLU 737  
564  1 Y 1 B CYS 749  ? B CYS 738  
565  1 Y 1 B SER 750  ? B SER 739  
566  1 Y 1 B ASN 751  ? B ASN 740  
567  1 Y 1 B LEU 752  ? B LEU 741  
568  1 Y 1 B LEU 753  ? B LEU 742  
569  1 Y 1 B LEU 754  ? B LEU 743  
570  1 Y 1 B GLN 755  ? B GLN 744  
571  1 Y 1 B TYR 756  ? B TYR 745  
572  1 Y 1 B GLY 757  ? B GLY 746  
573  1 Y 1 B SER 758  ? B SER 747  
574  1 Y 1 B PHE 759  ? B PHE 748  
575  1 Y 1 B CYS 760  ? B CYS 749  
576  1 Y 1 B THR 761  ? B THR 750  
577  1 Y 1 B GLN 762  ? B GLN 751  
578  1 Y 1 B LEU 763  ? B LEU 752  
579  1 Y 1 B ASN 764  ? B ASN 753  
580  1 Y 1 B ARG 765  ? B ARG 754  
581  1 Y 1 B ALA 766  ? B ALA 755  
582  1 Y 1 B LEU 767  ? B LEU 756  
583  1 Y 1 B THR 768  ? B THR 757  
584  1 Y 1 B GLY 769  ? B GLY 758  
585  1 Y 1 B ILE 770  ? B ILE 759  
586  1 Y 1 B ALA 771  ? B ALA 760  
587  1 Y 1 B VAL 772  ? B VAL 761  
588  1 Y 1 B GLU 773  ? B GLU 762  
589  1 Y 1 B GLN 774  ? B GLN 763  
590  1 Y 1 B ASP 775  ? B ASP 764  
591  1 Y 1 B LYS 776  ? B LYS 765  
592  1 Y 1 B ASN 777  ? B ASN 766  
593  1 Y 1 B THR 778  ? B THR 767  
594  1 Y 1 B GLN 779  ? B GLN 768  
595  1 Y 1 B GLU 780  ? B GLU 769  
596  1 Y 1 B VAL 781  ? B VAL 770  
597  1 Y 1 B PHE 782  ? B PHE 771  
598  1 Y 1 B ALA 783  ? B ALA 772  
599  1 Y 1 B GLN 784  ? B GLN 773  
600  1 Y 1 B VAL 785  ? B VAL 774  
601  1 Y 1 B LYS 786  ? B LYS 775  
602  1 Y 1 B GLN 787  ? B GLN 776  
603  1 Y 1 B ILE 788  ? B ILE 777  
604  1 Y 1 B TYR 789  ? B TYR 778  
605  1 Y 1 B LYS 790  ? B LYS 779  
606  1 Y 1 B THR 791  ? B THR 780  
607  1 Y 1 B PRO 792  ? B PRO 781  
608  1 Y 1 B PRO 793  ? B PRO 782  
609  1 Y 1 B ILE 794  ? B ILE 783  
610  1 Y 1 B LYS 795  ? B LYS 784  
611  1 Y 1 B ASP 796  ? B ASP 785  
612  1 Y 1 B PHE 797  ? B PHE 786  
613  1 Y 1 B GLY 798  ? B GLY 787  
614  1 Y 1 B GLY 799  ? B GLY 788  
615  1 Y 1 B PHE 800  ? B PHE 789  
616  1 Y 1 B ASN 801  ? B ASN 790  
617  1 Y 1 B PHE 802  ? B PHE 791  
618  1 Y 1 B SER 803  ? B SER 792  
619  1 Y 1 B GLN 804  ? B GLN 793  
620  1 Y 1 B ILE 805  ? B ILE 794  
621  1 Y 1 B LEU 806  ? B LEU 795  
622  1 Y 1 B PRO 807  ? B PRO 796  
623  1 Y 1 B ASP 808  ? B ASP 797  
624  1 Y 1 B PRO 809  ? B PRO 798  
625  1 Y 1 B SER 810  ? B SER 799  
626  1 Y 1 B LYS 811  ? B LYS 800  
627  1 Y 1 B PRO 812  ? B PRO 801  
628  1 Y 1 B SER 813  ? B SER 802  
629  1 Y 1 B LYS 814  ? B LYS 803  
630  1 Y 1 B ARG 815  ? B ARG 804  
631  1 Y 1 B SER 816  ? B SER 805  
632  1 Y 1 B PRO 817  ? B PRO 806  
633  1 Y 1 B ILE 818  ? B ILE 807  
634  1 Y 1 B GLU 819  ? B GLU 808  
635  1 Y 1 B ASP 820  ? B ASP 809  
636  1 Y 1 B LEU 821  ? B LEU 810  
637  1 Y 1 B LEU 822  ? B LEU 811  
638  1 Y 1 B PHE 823  ? B PHE 812  
639  1 Y 1 B ASN 824  ? B ASN 813  
640  1 Y 1 B LYS 825  ? B LYS 814  
641  1 Y 1 B VAL 826  ? B VAL 815  
642  1 Y 1 B THR 827  ? B THR 816  
643  1 Y 1 B LEU 828  ? B LEU 817  
644  1 Y 1 B ALA 829  ? B ALA 818  
645  1 Y 1 B ASP 830  ? B ASP 819  
646  1 Y 1 B ALA 831  ? B ALA 820  
647  1 Y 1 B GLY 832  ? B GLY 821  
648  1 Y 1 B PHE 833  ? B PHE 822  
649  1 Y 1 B ILE 834  ? B ILE 823  
650  1 Y 1 B LYS 835  ? B LYS 824  
651  1 Y 1 B GLN 836  ? B GLN 825  
652  1 Y 1 B TYR 837  ? B TYR 826  
653  1 Y 1 B GLY 838  ? B GLY 827  
654  1 Y 1 B ASP 839  ? B ASP 828  
655  1 Y 1 B CYS 840  ? B CYS 829  
656  1 Y 1 B LEU 841  ? B LEU 830  
657  1 Y 1 B GLY 842  ? B GLY 831  
658  1 Y 1 B ASP 843  ? B ASP 832  
659  1 Y 1 B ILE 844  ? B ILE 833  
660  1 Y 1 B ALA 845  ? B ALA 834  
661  1 Y 1 B ALA 846  ? B ALA 835  
662  1 Y 1 B ARG 847  ? B ARG 836  
663  1 Y 1 B ASP 848  ? B ASP 837  
664  1 Y 1 B LEU 849  ? B LEU 838  
665  1 Y 1 B ILE 850  ? B ILE 839  
666  1 Y 1 B CYS 851  ? B CYS 840  
667  1 Y 1 B ALA 852  ? B ALA 841  
668  1 Y 1 B GLN 853  ? B GLN 842  
669  1 Y 1 B LYS 854  ? B LYS 843  
670  1 Y 1 B PHE 855  ? B PHE 844  
671  1 Y 1 B ASN 856  ? B ASN 845  
672  1 Y 1 B GLY 857  ? B GLY 846  
673  1 Y 1 B LEU 858  ? B LEU 847  
674  1 Y 1 B THR 859  ? B THR 848  
675  1 Y 1 B VAL 860  ? B VAL 849  
676  1 Y 1 B LEU 861  ? B LEU 850  
677  1 Y 1 B PRO 862  ? B PRO 851  
678  1 Y 1 B PRO 863  ? B PRO 852  
679  1 Y 1 B LEU 864  ? B LEU 853  
680  1 Y 1 B LEU 865  ? B LEU 854  
681  1 Y 1 B THR 866  ? B THR 855  
682  1 Y 1 B ASP 867  ? B ASP 856  
683  1 Y 1 B GLU 868  ? B GLU 857  
684  1 Y 1 B MET 869  ? B MET 858  
685  1 Y 1 B ILE 870  ? B ILE 859  
686  1 Y 1 B ALA 871  ? B ALA 860  
687  1 Y 1 B GLN 872  ? B GLN 861  
688  1 Y 1 B TYR 873  ? B TYR 862  
689  1 Y 1 B THR 874  ? B THR 863  
690  1 Y 1 B SER 875  ? B SER 864  
691  1 Y 1 B ALA 876  ? B ALA 865  
692  1 Y 1 B LEU 877  ? B LEU 866  
693  1 Y 1 B LEU 878  ? B LEU 867  
694  1 Y 1 B ALA 879  ? B ALA 868  
695  1 Y 1 B GLY 880  ? B GLY 869  
696  1 Y 1 B THR 881  ? B THR 870  
697  1 Y 1 B ILE 882  ? B ILE 871  
698  1 Y 1 B THR 883  ? B THR 872  
699  1 Y 1 B SER 884  ? B SER 873  
700  1 Y 1 B GLY 885  ? B GLY 874  
701  1 Y 1 B TRP 886  ? B TRP 875  
702  1 Y 1 B THR 887  ? B THR 876  
703  1 Y 1 B PHE 888  ? B PHE 877  
704  1 Y 1 B GLY 889  ? B GLY 878  
705  1 Y 1 B ALA 890  ? B ALA 879  
706  1 Y 1 B GLY 891  ? B GLY 880  
707  1 Y 1 B PRO 892  ? B PRO 881  
708  1 Y 1 B ALA 893  ? B ALA 882  
709  1 Y 1 B LEU 894  ? B LEU 883  
710  1 Y 1 B GLN 895  ? B GLN 884  
711  1 Y 1 B ILE 896  ? B ILE 885  
712  1 Y 1 B PRO 897  ? B PRO 886  
713  1 Y 1 B PHE 898  ? B PHE 887  
714  1 Y 1 B PRO 899  ? B PRO 888  
715  1 Y 1 B MET 900  ? B MET 889  
716  1 Y 1 B GLN 901  ? B GLN 890  
717  1 Y 1 B MET 902  ? B MET 891  
718  1 Y 1 B ALA 903  ? B ALA 892  
719  1 Y 1 B TYR 904  ? B TYR 893  
720  1 Y 1 B ARG 905  ? B ARG 894  
721  1 Y 1 B PHE 906  ? B PHE 895  
722  1 Y 1 B ASN 907  ? B ASN 896  
723  1 Y 1 B GLY 908  ? B GLY 897  
724  1 Y 1 B ILE 909  ? B ILE 898  
725  1 Y 1 B GLY 910  ? B GLY 899  
726  1 Y 1 B VAL 911  ? B VAL 900  
727  1 Y 1 B THR 912  ? B THR 901  
728  1 Y 1 B GLN 913  ? B GLN 902  
729  1 Y 1 B ASN 914  ? B ASN 903  
730  1 Y 1 B VAL 915  ? B VAL 904  
731  1 Y 1 B LEU 916  ? B LEU 905  
732  1 Y 1 B TYR 917  ? B TYR 906  
733  1 Y 1 B GLU 918  ? B GLU 907  
734  1 Y 1 B ASN 919  ? B ASN 908  
735  1 Y 1 B GLN 920  ? B GLN 909  
736  1 Y 1 B LYS 921  ? B LYS 910  
737  1 Y 1 B LEU 922  ? B LEU 911  
738  1 Y 1 B ILE 923  ? B ILE 912  
739  1 Y 1 B ALA 924  ? B ALA 913  
740  1 Y 1 B ASN 925  ? B ASN 914  
741  1 Y 1 B GLN 926  ? B GLN 915  
742  1 Y 1 B PHE 927  ? B PHE 916  
743  1 Y 1 B ASN 928  ? B ASN 917  
744  1 Y 1 B SER 929  ? B SER 918  
745  1 Y 1 B ALA 930  ? B ALA 919  
746  1 Y 1 B ILE 931  ? B ILE 920  
747  1 Y 1 B GLY 932  ? B GLY 921  
748  1 Y 1 B LYS 933  ? B LYS 922  
749  1 Y 1 B ILE 934  ? B ILE 923  
750  1 Y 1 B GLN 935  ? B GLN 924  
751  1 Y 1 B ASP 936  ? B ASP 925  
752  1 Y 1 B SER 937  ? B SER 926  
753  1 Y 1 B LEU 938  ? B LEU 927  
754  1 Y 1 B SER 939  ? B SER 928  
755  1 Y 1 B SER 940  ? B SER 929  
756  1 Y 1 B THR 941  ? B THR 930  
757  1 Y 1 B PRO 942  ? B PRO 931  
758  1 Y 1 B SER 943  ? B SER 932  
759  1 Y 1 B ALA 944  ? B ALA 933  
760  1 Y 1 B LEU 945  ? B LEU 934  
761  1 Y 1 B GLY 946  ? B GLY 935  
762  1 Y 1 B LYS 947  ? B LYS 936  
763  1 Y 1 B LEU 948  ? B LEU 937  
764  1 Y 1 B GLN 949  ? B GLN 938  
765  1 Y 1 B ASP 950  ? B ASP 939  
766  1 Y 1 B VAL 951  ? B VAL 940  
767  1 Y 1 B VAL 952  ? B VAL 941  
768  1 Y 1 B ASN 953  ? B ASN 942  
769  1 Y 1 B GLN 954  ? B GLN 943  
770  1 Y 1 B ASN 955  ? B ASN 944  
771  1 Y 1 B ALA 956  ? B ALA 945  
772  1 Y 1 B GLN 957  ? B GLN 946  
773  1 Y 1 B ALA 958  ? B ALA 947  
774  1 Y 1 B LEU 959  ? B LEU 948  
775  1 Y 1 B ASN 960  ? B ASN 949  
776  1 Y 1 B THR 961  ? B THR 950  
777  1 Y 1 B LEU 962  ? B LEU 951  
778  1 Y 1 B VAL 963  ? B VAL 952  
779  1 Y 1 B LYS 964  ? B LYS 953  
780  1 Y 1 B GLN 965  ? B GLN 954  
781  1 Y 1 B LEU 966  ? B LEU 955  
782  1 Y 1 B SER 967  ? B SER 956  
783  1 Y 1 B SER 968  ? B SER 957  
784  1 Y 1 B ASN 969  ? B ASN 958  
785  1 Y 1 B PHE 970  ? B PHE 959  
786  1 Y 1 B GLY 971  ? B GLY 960  
787  1 Y 1 B ALA 972  ? B ALA 961  
788  1 Y 1 B ILE 973  ? B ILE 962  
789  1 Y 1 B SER 974  ? B SER 963  
790  1 Y 1 B SER 975  ? B SER 964  
791  1 Y 1 B VAL 976  ? B VAL 965  
792  1 Y 1 B LEU 977  ? B LEU 966  
793  1 Y 1 B ASN 978  ? B ASN 967  
794  1 Y 1 B ASP 979  ? B ASP 968  
795  1 Y 1 B ILE 980  ? B ILE 969  
796  1 Y 1 B LEU 981  ? B LEU 970  
797  1 Y 1 B SER 982  ? B SER 971  
798  1 Y 1 B ARG 983  ? B ARG 972  
799  1 Y 1 B LEU 984  ? B LEU 973  
800  1 Y 1 B ASP 985  ? B ASP 974  
801  1 Y 1 B PRO 986  ? B PRO 975  
802  1 Y 1 B PRO 987  ? B PRO 976  
803  1 Y 1 B GLU 988  ? B GLU 977  
804  1 Y 1 B ALA 989  ? B ALA 978  
805  1 Y 1 B GLU 990  ? B GLU 979  
806  1 Y 1 B VAL 991  ? B VAL 980  
807  1 Y 1 B GLN 992  ? B GLN 981  
808  1 Y 1 B ILE 993  ? B ILE 982  
809  1 Y 1 B ASP 994  ? B ASP 983  
810  1 Y 1 B ARG 995  ? B ARG 984  
811  1 Y 1 B LEU 996  ? B LEU 985  
812  1 Y 1 B ILE 997  ? B ILE 986  
813  1 Y 1 B THR 998  ? B THR 987  
814  1 Y 1 B GLY 999  ? B GLY 988  
815  1 Y 1 B ARG 1000 ? B ARG 989  
816  1 Y 1 B LEU 1001 ? B LEU 990  
817  1 Y 1 B GLN 1002 ? B GLN 991  
818  1 Y 1 B SER 1003 ? B SER 992  
819  1 Y 1 B LEU 1004 ? B LEU 993  
820  1 Y 1 B GLN 1005 ? B GLN 994  
821  1 Y 1 B THR 1006 ? B THR 995  
822  1 Y 1 B TYR 1007 ? B TYR 996  
823  1 Y 1 B VAL 1008 ? B VAL 997  
824  1 Y 1 B THR 1009 ? B THR 998  
825  1 Y 1 B GLN 1010 ? B GLN 999  
826  1 Y 1 B GLN 1011 ? B GLN 1000 
827  1 Y 1 B LEU 1012 ? B LEU 1001 
828  1 Y 1 B ILE 1013 ? B ILE 1002 
829  1 Y 1 B ARG 1014 ? B ARG 1003 
830  1 Y 1 B ALA 1015 ? B ALA 1004 
831  1 Y 1 B ALA 1016 ? B ALA 1005 
832  1 Y 1 B GLU 1017 ? B GLU 1006 
833  1 Y 1 B ILE 1018 ? B ILE 1007 
834  1 Y 1 B ARG 1019 ? B ARG 1008 
835  1 Y 1 B ALA 1020 ? B ALA 1009 
836  1 Y 1 B SER 1021 ? B SER 1010 
837  1 Y 1 B ALA 1022 ? B ALA 1011 
838  1 Y 1 B ASN 1023 ? B ASN 1012 
839  1 Y 1 B LEU 1024 ? B LEU 1013 
840  1 Y 1 B ALA 1025 ? B ALA 1014 
841  1 Y 1 B ALA 1026 ? B ALA 1015 
842  1 Y 1 B THR 1027 ? B THR 1016 
843  1 Y 1 B LYS 1028 ? B LYS 1017 
844  1 Y 1 B MET 1029 ? B MET 1018 
845  1 Y 1 B SER 1030 ? B SER 1019 
846  1 Y 1 B GLU 1031 ? B GLU 1020 
847  1 Y 1 B CYS 1032 ? B CYS 1021 
848  1 Y 1 B VAL 1033 ? B VAL 1022 
849  1 Y 1 B LEU 1034 ? B LEU 1023 
850  1 Y 1 B GLY 1035 ? B GLY 1024 
851  1 Y 1 B GLN 1036 ? B GLN 1025 
852  1 Y 1 B SER 1037 ? B SER 1026 
853  1 Y 1 B LYS 1038 ? B LYS 1027 
854  1 Y 1 B ARG 1039 ? B ARG 1028 
855  1 Y 1 B VAL 1040 ? B VAL 1029 
856  1 Y 1 B ASP 1041 ? B ASP 1030 
857  1 Y 1 B PHE 1042 ? B PHE 1031 
858  1 Y 1 B CYS 1043 ? B CYS 1032 
859  1 Y 1 B GLY 1044 ? B GLY 1033 
860  1 Y 1 B LYS 1045 ? B LYS 1034 
861  1 Y 1 B GLY 1046 ? B GLY 1035 
862  1 Y 1 B TYR 1047 ? B TYR 1036 
863  1 Y 1 B HIS 1048 ? B HIS 1037 
864  1 Y 1 B LEU 1049 ? B LEU 1038 
865  1 Y 1 B MET 1050 ? B MET 1039 
866  1 Y 1 B SER 1051 ? B SER 1040 
867  1 Y 1 B PHE 1052 ? B PHE 1041 
868  1 Y 1 B PRO 1053 ? B PRO 1042 
869  1 Y 1 B GLN 1054 ? B GLN 1043 
870  1 Y 1 B SER 1055 ? B SER 1044 
871  1 Y 1 B ALA 1056 ? B ALA 1045 
872  1 Y 1 B PRO 1057 ? B PRO 1046 
873  1 Y 1 B HIS 1058 ? B HIS 1047 
874  1 Y 1 B GLY 1059 ? B GLY 1048 
875  1 Y 1 B VAL 1060 ? B VAL 1049 
876  1 Y 1 B VAL 1061 ? B VAL 1050 
877  1 Y 1 B PHE 1062 ? B PHE 1051 
878  1 Y 1 B LEU 1063 ? B LEU 1052 
879  1 Y 1 B HIS 1064 ? B HIS 1053 
880  1 Y 1 B VAL 1065 ? B VAL 1054 
881  1 Y 1 B THR 1066 ? B THR 1055 
882  1 Y 1 B TYR 1067 ? B TYR 1056 
883  1 Y 1 B VAL 1068 ? B VAL 1057 
884  1 Y 1 B PRO 1069 ? B PRO 1058 
885  1 Y 1 B ALA 1070 ? B ALA 1059 
886  1 Y 1 B GLN 1071 ? B GLN 1060 
887  1 Y 1 B GLU 1072 ? B GLU 1061 
888  1 Y 1 B LYS 1073 ? B LYS 1062 
889  1 Y 1 B ASN 1074 ? B ASN 1063 
890  1 Y 1 B PHE 1075 ? B PHE 1064 
891  1 Y 1 B THR 1076 ? B THR 1065 
892  1 Y 1 B THR 1077 ? B THR 1066 
893  1 Y 1 B ALA 1078 ? B ALA 1067 
894  1 Y 1 B PRO 1079 ? B PRO 1068 
895  1 Y 1 B ALA 1080 ? B ALA 1069 
896  1 Y 1 B ILE 1081 ? B ILE 1070 
897  1 Y 1 B CYS 1082 ? B CYS 1071 
898  1 Y 1 B HIS 1083 ? B HIS 1072 
899  1 Y 1 B ASP 1084 ? B ASP 1073 
900  1 Y 1 B GLY 1085 ? B GLY 1074 
901  1 Y 1 B LYS 1086 ? B LYS 1075 
902  1 Y 1 B ALA 1087 ? B ALA 1076 
903  1 Y 1 B HIS 1088 ? B HIS 1077 
904  1 Y 1 B PHE 1089 ? B PHE 1078 
905  1 Y 1 B PRO 1090 ? B PRO 1079 
906  1 Y 1 B ARG 1091 ? B ARG 1080 
907  1 Y 1 B GLU 1092 ? B GLU 1081 
908  1 Y 1 B GLY 1093 ? B GLY 1082 
909  1 Y 1 B VAL 1094 ? B VAL 1083 
910  1 Y 1 B PHE 1095 ? B PHE 1084 
911  1 Y 1 B VAL 1096 ? B VAL 1085 
912  1 Y 1 B SER 1097 ? B SER 1086 
913  1 Y 1 B ASN 1098 ? B ASN 1087 
914  1 Y 1 B GLY 1099 ? B GLY 1088 
915  1 Y 1 B THR 1100 ? B THR 1089 
916  1 Y 1 B HIS 1101 ? B HIS 1090 
917  1 Y 1 B TRP 1102 ? B TRP 1091 
918  1 Y 1 B PHE 1103 ? B PHE 1092 
919  1 Y 1 B VAL 1104 ? B VAL 1093 
920  1 Y 1 B THR 1105 ? B THR 1094 
921  1 Y 1 B GLN 1106 ? B GLN 1095 
922  1 Y 1 B ARG 1107 ? B ARG 1096 
923  1 Y 1 B ASN 1108 ? B ASN 1097 
924  1 Y 1 B PHE 1109 ? B PHE 1098 
925  1 Y 1 B TYR 1110 ? B TYR 1099 
926  1 Y 1 B GLU 1111 ? B GLU 1100 
927  1 Y 1 B PRO 1112 ? B PRO 1101 
928  1 Y 1 B GLN 1113 ? B GLN 1102 
929  1 Y 1 B ILE 1114 ? B ILE 1103 
930  1 Y 1 B ILE 1115 ? B ILE 1104 
931  1 Y 1 B THR 1116 ? B THR 1105 
932  1 Y 1 B THR 1117 ? B THR 1106 
933  1 Y 1 B ASP 1118 ? B ASP 1107 
934  1 Y 1 B ASN 1119 ? B ASN 1108 
935  1 Y 1 B THR 1120 ? B THR 1109 
936  1 Y 1 B PHE 1121 ? B PHE 1110 
937  1 Y 1 B VAL 1122 ? B VAL 1111 
938  1 Y 1 B SER 1123 ? B SER 1112 
939  1 Y 1 B GLY 1124 ? B GLY 1113 
940  1 Y 1 B ASN 1125 ? B ASN 1114 
941  1 Y 1 B CYS 1126 ? B CYS 1115 
942  1 Y 1 B ASP 1127 ? B ASP 1116 
943  1 Y 1 B VAL 1128 ? B VAL 1117 
944  1 Y 1 B VAL 1129 ? B VAL 1118 
945  1 Y 1 B ILE 1130 ? B ILE 1119 
946  1 Y 1 B GLY 1131 ? B GLY 1120 
947  1 Y 1 B ILE 1132 ? B ILE 1121 
948  1 Y 1 B VAL 1133 ? B VAL 1122 
949  1 Y 1 B ASN 1134 ? B ASN 1123 
950  1 Y 1 B ASN 1135 ? B ASN 1124 
951  1 Y 1 B THR 1136 ? B THR 1125 
952  1 Y 1 B VAL 1137 ? B VAL 1126 
953  1 Y 1 B TYR 1138 ? B TYR 1127 
954  1 Y 1 B ASP 1139 ? B ASP 1128 
955  1 Y 1 B PRO 1140 ? B PRO 1129 
956  1 Y 1 B LEU 1141 ? B LEU 1130 
957  1 Y 1 B GLN 1142 ? B GLN 1131 
958  1 Y 1 B PRO 1143 ? B PRO 1132 
959  1 Y 1 B GLU 1144 ? B GLU 1133 
960  1 Y 1 B LEU 1145 ? B LEU 1134 
961  1 Y 1 B ASP 1146 ? B ASP 1135 
962  1 Y 1 B SER 1147 ? B SER 1136 
963  1 Y 1 B PHE 1148 ? B PHE 1137 
964  1 Y 1 B LYS 1149 ? B LYS 1138 
965  1 Y 1 B GLU 1150 ? B GLU 1139 
966  1 Y 1 B GLU 1151 ? B GLU 1140 
967  1 Y 1 B LEU 1152 ? B LEU 1141 
968  1 Y 1 B ASP 1153 ? B ASP 1142 
969  1 Y 1 B LYS 1154 ? B LYS 1143 
970  1 Y 1 B TYR 1155 ? B TYR 1144 
971  1 Y 1 B PHE 1156 ? B PHE 1145 
972  1 Y 1 B LYS 1157 ? B LYS 1146 
973  1 Y 1 B ASN 1158 ? B ASN 1147 
974  1 Y 1 B HIS 1159 ? B HIS 1148 
975  1 Y 1 B THR 1160 ? B THR 1149 
976  1 Y 1 B SER 1161 ? B SER 1150 
977  1 Y 1 B PRO 1162 ? B PRO 1151 
978  1 Y 1 B ASP 1163 ? B ASP 1152 
979  1 Y 1 B VAL 1164 ? B VAL 1153 
980  1 Y 1 B ASP 1165 ? B ASP 1154 
981  1 Y 1 B LEU 1166 ? B LEU 1155 
982  1 Y 1 B GLY 1167 ? B GLY 1156 
983  1 Y 1 B ASP 1168 ? B ASP 1157 
984  1 Y 1 B ILE 1169 ? B ILE 1158 
985  1 Y 1 B SER 1170 ? B SER 1159 
986  1 Y 1 B GLY 1171 ? B GLY 1160 
987  1 Y 1 B ILE 1172 ? B ILE 1161 
988  1 Y 1 B ASN 1173 ? B ASN 1162 
989  1 Y 1 B ALA 1174 ? B ALA 1163 
990  1 Y 1 B SER 1175 ? B SER 1164 
991  1 Y 1 B VAL 1176 ? B VAL 1165 
992  1 Y 1 B VAL 1177 ? B VAL 1166 
993  1 Y 1 B ASN 1178 ? B ASN 1167 
994  1 Y 1 B ILE 1179 ? B ILE 1168 
995  1 Y 1 B GLN 1180 ? B GLN 1169 
996  1 Y 1 B LYS 1181 ? B LYS 1170 
997  1 Y 1 B GLU 1182 ? B GLU 1171 
998  1 Y 1 B ILE 1183 ? B ILE 1172 
999  1 Y 1 B ASP 1184 ? B ASP 1173 
1000 1 Y 1 B ARG 1185 ? B ARG 1174 
1001 1 Y 1 B LEU 1186 ? B LEU 1175 
1002 1 Y 1 B ASN 1187 ? B ASN 1176 
1003 1 Y 1 B GLU 1188 ? B GLU 1177 
1004 1 Y 1 B VAL 1189 ? B VAL 1178 
1005 1 Y 1 B ALA 1190 ? B ALA 1179 
1006 1 Y 1 B LYS 1191 ? B LYS 1180 
1007 1 Y 1 B ASN 1192 ? B ASN 1181 
1008 1 Y 1 B LEU 1193 ? B LEU 1182 
1009 1 Y 1 B ASN 1194 ? B ASN 1183 
1010 1 Y 1 B GLU 1195 ? B GLU 1184 
1011 1 Y 1 B SER 1196 ? B SER 1185 
1012 1 Y 1 B LEU 1197 ? B LEU 1186 
1013 1 Y 1 B ILE 1198 ? B ILE 1187 
1014 1 Y 1 B ASP 1199 ? B ASP 1188 
1015 1 Y 1 B LEU 1200 ? B LEU 1189 
1016 1 Y 1 B GLN 1201 ? B GLN 1190 
1017 1 Y 1 B GLU 1202 ? B GLU 1191 
1018 1 Y 1 B LEU 1203 ? B LEU 1192 
1019 1 Y 1 B GLY 1204 ? B GLY 1193 
1020 1 Y 1 B LYS 1205 ? B LYS 1194 
1021 1 Y 1 B TYR 1206 ? B TYR 1195 
1022 1 Y 1 B GLU 1207 ? B GLU 1196 
1023 1 Y 1 B GLN 1208 ? B GLN 1197 
1024 1 Y 1 B TYR 1209 ? B TYR 1198 
1025 1 Y 1 B ILE 1210 ? B ILE 1199 
# 
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 
NAG C1   C N R 247 
NAG C2   C N R 248 
NAG C3   C N R 249 
NAG C4   C N S 250 
NAG C5   C N R 251 
NAG C6   C N N 252 
NAG C7   C N N 253 
NAG C8   C N N 254 
NAG N2   N N N 255 
NAG O1   O N N 256 
NAG O3   O N N 257 
NAG O4   O N N 258 
NAG O5   O N N 259 
NAG O6   O N N 260 
NAG O7   O N N 261 
NAG H1   H N N 262 
NAG H2   H N N 263 
NAG H3   H N N 264 
NAG H4   H N N 265 
NAG H5   H N N 266 
NAG H61  H N N 267 
NAG H62  H N N 268 
NAG H81  H N N 269 
NAG H82  H N N 270 
NAG H83  H N N 271 
NAG HN2  H N N 272 
NAG HO1  H N N 273 
NAG HO3  H N N 274 
NAG HO4  H N N 275 
NAG HO6  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
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 
NAG C1  C2   sing N N 235 
NAG C1  O1   sing N N 236 
NAG C1  O5   sing N N 237 
NAG C1  H1   sing N N 238 
NAG C2  C3   sing N N 239 
NAG C2  N2   sing N N 240 
NAG C2  H2   sing N N 241 
NAG C3  C4   sing N N 242 
NAG C3  O3   sing N N 243 
NAG C3  H3   sing N N 244 
NAG C4  C5   sing N N 245 
NAG C4  O4   sing N N 246 
NAG C4  H4   sing N N 247 
NAG C5  C6   sing N N 248 
NAG C5  O5   sing N N 249 
NAG C5  H5   sing N N 250 
NAG C6  O6   sing N N 251 
NAG C6  H61  sing N N 252 
NAG C6  H62  sing N N 253 
NAG C7  C8   sing N N 254 
NAG C7  N2   sing N N 255 
NAG C7  O7   doub N N 256 
NAG C8  H81  sing N N 257 
NAG C8  H82  sing N N 258 
NAG C8  H83  sing N N 259 
NAG N2  HN2  sing N N 260 
NAG O1  HO1  sing N N 261 
NAG O3  HO3  sing N N 262 
NAG O4  HO4  sing N N 263 
NAG O6  HO6  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-03-05 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8YKH 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'SARS-CoV-2 spike glycoprotein in complex with NT-108 scFv focused on RBD and NT-108 scFv interface' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 0.14   mol/L NaCl  1 'sodium chloride' 
1 0.0027 mol/L KCl   2 'kalium chloride' 
1 0.010  mol/L H3PO4 3 'phosphoric acid' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
loop_
_em_entity_assembly_molwt.entity_assembly_id 
_em_entity_assembly_molwt.experimental_flag 
_em_entity_assembly_molwt.id 
_em_entity_assembly_molwt.units 
_em_entity_assembly_molwt.value 
1 NO 1 MEGADALTONS 0.47 
1 NO 2 MEGADALTONS 0.42 
1 NO 3 MEGADALTONS 0.02 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
_em_entity_assembly_naturalsource.details 
? ? 1 1 9606    'Homo sapiens'                                    ? ? ? ? ? 
? ? 2 2 2697049 'Severe acute respiratory syndrome coronavirus 2' ? ? ? ? ? 
? ? 3 3 9606    'Homo sapiens'                                    ? ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 1 1 9606 'Homo sapiens' ? ? 
? 2 2 9606 'Homo sapiens' ? ? 
? 3 3 9606 'Homo sapiens' ? ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               1.5 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         53.52 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (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                     2832 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   652138 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? crYOLO    ?      
'IMAGE ACQUISITION'        ? 2  ? ? 1 EPU       ?      
MASKING                    ? 3  ? ? ? ?         ?      
'CTF CORRECTION'           ? 4  1 ? ? RELION    3.1    
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ?      
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ?      
'MODEL FITTING'            ? 7  ? 1 ? ?         ?      
OTHER                      ? 8  ? ? ? ?         ?      
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? RELION    3.1    
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? RELION    3.1    
CLASSIFICATION             ? 11 1 ? ? RELION    3.1    
RECONSTRUCTION             ? 12 1 ? ? cryoSPARC 3.3.1  
'MODEL REFINEMENT'         ? 13 ? 1 ? PHENIX    1.19.2 
# 
_em_specimen.concentration           1.1 
_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 
'Japan Agency for Medical Research and Development (AMED)' Japan JP17am0101093 1 
'Japan Agency for Medical Research and Development (AMED)' Japan JP20ae0101047 2 
'Japan Agency for Medical Research and Development (AMED)' Japan JP21fk0108463 3 
'Japan Agency for Medical Research and Development (AMED)' Japan JP22ama121037 4 
'Japan Society for the Promotion of Science (JSPS)'        Japan JP20H05873    5 
'Japan Agency for Medical Research and Development (AMED)' Japan JP223fa627005 6 
'Japan Agency for Medical Research and Development (AMED)' Japan JP223fa627009 7 
'Japan Agency for Medical Research and Development (AMED)' Japan JP23jf0126002 8 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8YK4 
# 
_atom_sites.entry_id                    8YKH 
_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   . ILE A 1 2   ? 110.349 144.093 200.681 1.00 119.66 ? 1   ILE A N   1 
ATOM   2    C CA  . ILE A 1 2   ? 111.704 143.566 200.746 1.00 119.66 ? 1   ILE A CA  1 
ATOM   3    C C   . ILE A 1 2   ? 111.918 142.919 202.103 1.00 119.66 ? 1   ILE A C   1 
ATOM   4    O O   . ILE A 1 2   ? 111.518 143.470 203.125 1.00 119.66 ? 1   ILE A O   1 
ATOM   5    C CB  . ILE A 1 2   ? 112.755 144.663 200.487 1.00 119.66 ? 1   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 2   ? 112.609 145.239 199.078 1.00 119.66 ? 1   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 2   ? 114.158 144.120 200.681 1.00 119.66 ? 1   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 2   ? 111.653 146.409 198.978 1.00 119.66 ? 1   ILE A CD1 1 
ATOM   9    N N   . VAL A 1 3   ? 112.540 141.742 202.113 1.00 121.42 ? 2   VAL A N   1 
ATOM   10   C CA  . VAL A 1 3   ? 112.816 141.005 203.340 1.00 121.42 ? 2   VAL A CA  1 
ATOM   11   C C   . VAL A 1 3   ? 114.304 140.697 203.396 1.00 121.42 ? 2   VAL A C   1 
ATOM   12   O O   . VAL A 1 3   ? 114.883 140.228 202.410 1.00 121.42 ? 2   VAL A O   1 
ATOM   13   C CB  . VAL A 1 3   ? 111.994 139.707 203.426 1.00 121.42 ? 2   VAL A CB  1 
ATOM   14   C CG1 . VAL A 1 3   ? 112.309 138.969 204.713 1.00 121.42 ? 2   VAL A CG1 1 
ATOM   15   C CG2 . VAL A 1 3   ? 110.512 140.015 203.334 1.00 121.42 ? 2   VAL A CG2 1 
ATOM   16   N N   . LEU A 1 4   ? 114.918 140.957 204.545 1.00 120.87 ? 3   LEU A N   1 
ATOM   17   C CA  . LEU A 1 4   ? 116.335 140.702 204.759 1.00 120.87 ? 3   LEU A CA  1 
ATOM   18   C C   . LEU A 1 4   ? 116.490 139.452 205.613 1.00 120.87 ? 3   LEU A C   1 
ATOM   19   O O   . LEU A 1 4   ? 115.826 139.316 206.645 1.00 120.87 ? 3   LEU A O   1 
ATOM   20   C CB  . LEU A 1 4   ? 117.008 141.894 205.435 1.00 120.87 ? 3   LEU A CB  1 
ATOM   21   C CG  . LEU A 1 4   ? 117.079 143.183 204.624 1.00 120.87 ? 3   LEU A CG  1 
ATOM   22   C CD1 . LEU A 1 4   ? 117.835 144.241 205.396 1.00 120.87 ? 3   LEU A CD1 1 
ATOM   23   C CD2 . LEU A 1 4   ? 117.734 142.925 203.283 1.00 120.87 ? 3   LEU A CD2 1 
ATOM   24   N N   . THR A 1 5   ? 117.363 138.547 205.186 1.00 127.57 ? 4   THR A N   1 
ATOM   25   C CA  . THR A 1 5   ? 117.636 137.314 205.908 1.00 127.57 ? 4   THR A CA  1 
ATOM   26   C C   . THR A 1 5   ? 119.104 137.266 206.304 1.00 127.57 ? 4   THR A C   1 
ATOM   27   O O   . THR A 1 5   ? 119.989 137.456 205.462 1.00 127.57 ? 4   THR A O   1 
ATOM   28   C CB  . THR A 1 5   ? 117.273 136.092 205.062 1.00 127.57 ? 4   THR A CB  1 
ATOM   29   O OG1 . THR A 1 5   ? 117.874 136.208 203.768 1.00 127.57 ? 4   THR A OG1 1 
ATOM   30   C CG2 . THR A 1 5   ? 115.765 135.982 204.907 1.00 127.57 ? 4   THR A CG2 1 
ATOM   31   N N   . GLN A 1 6   ? 119.355 137.023 207.584 1.00 129.21 ? 5   GLN A N   1 
ATOM   32   C CA  . GLN A 1 6   ? 120.714 136.880 208.072 1.00 129.21 ? 5   GLN A CA  1 
ATOM   33   C C   . GLN A 1 6   ? 121.199 135.455 207.826 1.00 129.21 ? 5   GLN A C   1 
ATOM   34   O O   . GLN A 1 6   ? 120.625 134.484 208.324 1.00 129.21 ? 5   GLN A O   1 
ATOM   35   C CB  . GLN A 1 6   ? 120.773 137.207 209.563 1.00 129.21 ? 5   GLN A CB  1 
ATOM   36   C CG  . GLN A 1 6   ? 122.168 137.246 210.146 1.00 129.21 ? 5   GLN A CG  1 
ATOM   37   C CD  . GLN A 1 6   ? 122.961 138.438 209.661 1.00 129.21 ? 5   GLN A CD  1 
ATOM   38   O OE1 . GLN A 1 6   ? 124.139 138.322 209.327 1.00 129.21 ? 5   GLN A OE1 1 
ATOM   39   N NE2 . GLN A 1 6   ? 122.321 139.600 209.639 1.00 129.21 ? 5   GLN A NE2 1 
ATOM   40   N N   . SER A 1 7   ? 122.268 135.329 207.042 1.00 135.49 ? 6   SER A N   1 
ATOM   41   C CA  . SER A 1 7   ? 122.673 134.001 206.596 1.00 135.49 ? 6   SER A CA  1 
ATOM   42   C C   . SER A 1 7   ? 123.350 133.196 207.706 1.00 135.49 ? 6   SER A C   1 
ATOM   43   O O   . SER A 1 7   ? 122.882 132.093 208.017 1.00 135.49 ? 6   SER A O   1 
ATOM   44   C CB  . SER A 1 7   ? 123.574 134.102 205.361 1.00 135.49 ? 6   SER A CB  1 
ATOM   45   O OG  . SER A 1 7   ? 124.049 132.826 204.971 1.00 135.49 ? 6   SER A OG  1 
ATOM   46   N N   . PRO A 1 8   ? 124.431 133.672 208.326 1.00 134.05 ? 7   PRO A N   1 
ATOM   47   C CA  . PRO A 1 8   ? 125.041 132.880 209.400 1.00 134.05 ? 7   PRO A CA  1 
ATOM   48   C C   . PRO A 1 8   ? 124.195 132.949 210.662 1.00 134.05 ? 7   PRO A C   1 
ATOM   49   O O   . PRO A 1 8   ? 123.752 134.022 211.075 1.00 134.05 ? 7   PRO A O   1 
ATOM   50   C CB  . PRO A 1 8   ? 126.410 133.542 209.597 1.00 134.05 ? 7   PRO A CB  1 
ATOM   51   C CG  . PRO A 1 8   ? 126.597 134.430 208.401 1.00 134.05 ? 7   PRO A CG  1 
ATOM   52   C CD  . PRO A 1 8   ? 125.218 134.891 208.085 1.00 134.05 ? 7   PRO A CD  1 
ATOM   53   N N   . GLY A 1 9   ? 123.970 131.789 211.276 1.00 139.46 ? 8   GLY A N   1 
ATOM   54   C CA  . GLY A 1 9   ? 123.138 131.753 212.468 1.00 139.46 ? 8   GLY A CA  1 
ATOM   55   C C   . GLY A 1 9   ? 123.877 132.211 213.709 1.00 139.46 ? 8   GLY A C   1 
ATOM   56   O O   . GLY A 1 9   ? 123.477 133.173 214.368 1.00 139.46 ? 8   GLY A O   1 
ATOM   57   N N   . THR A 1 10  ? 124.966 131.525 214.047 1.00 142.43 ? 9   THR A N   1 
ATOM   58   C CA  . THR A 1 10  ? 125.742 131.843 215.236 1.00 142.43 ? 9   THR A CA  1 
ATOM   59   C C   . THR A 1 10  ? 127.147 131.290 215.058 1.00 142.43 ? 9   THR A C   1 
ATOM   60   O O   . THR A 1 10  ? 127.337 130.176 214.565 1.00 142.43 ? 9   THR A O   1 
ATOM   61   C CB  . THR A 1 10  ? 125.089 131.272 216.502 1.00 142.43 ? 9   THR A CB  1 
ATOM   62   O OG1 . THR A 1 10  ? 123.825 131.911 216.718 1.00 142.43 ? 9   THR A OG1 1 
ATOM   63   C CG2 . THR A 1 10  ? 125.972 131.500 217.717 1.00 142.43 ? 9   THR A CG2 1 
ATOM   64   N N   . LEU A 1 11  ? 128.136 132.084 215.461 1.00 147.98 ? 10  LEU A N   1 
ATOM   65   C CA  . LEU A 1 11  ? 129.532 131.719 215.285 1.00 147.98 ? 10  LEU A CA  1 
ATOM   66   C C   . LEU A 1 11  ? 130.278 131.884 216.599 1.00 147.98 ? 10  LEU A C   1 
ATOM   67   O O   . LEU A 1 11  ? 129.994 132.792 217.384 1.00 147.98 ? 10  LEU A O   1 
ATOM   68   C CB  . LEU A 1 11  ? 130.204 132.567 214.198 1.00 147.98 ? 10  LEU A CB  1 
ATOM   69   C CG  . LEU A 1 11  ? 129.901 132.210 212.743 1.00 147.98 ? 10  LEU A CG  1 
ATOM   70   C CD1 . LEU A 1 11  ? 128.557 132.762 212.317 1.00 147.98 ? 10  LEU A CD1 1 
ATOM   71   C CD2 . LEU A 1 11  ? 131.001 132.731 211.835 1.00 147.98 ? 10  LEU A CD2 1 
ATOM   72   N N   . SER A 1 12  ? 131.243 130.994 216.825 1.00 157.89 ? 11  SER A N   1 
ATOM   73   C CA  . SER A 1 12  ? 132.118 131.055 217.990 1.00 157.89 ? 11  SER A CA  1 
ATOM   74   C C   . SER A 1 12  ? 133.556 131.048 217.503 1.00 157.89 ? 11  SER A C   1 
ATOM   75   O O   . SER A 1 12  ? 133.970 130.115 216.809 1.00 157.89 ? 11  SER A O   1 
ATOM   76   C CB  . SER A 1 12  ? 131.871 129.880 218.939 1.00 157.89 ? 11  SER A CB  1 
ATOM   77   O OG  . SER A 1 12  ? 132.817 129.875 219.994 1.00 157.89 ? 11  SER A OG  1 
ATOM   78   N N   . LEU A 1 13  ? 134.315 132.080 217.860 1.00 160.09 ? 12  LEU A N   1 
ATOM   79   C CA  . LEU A 1 13  ? 135.685 132.231 217.397 1.00 160.09 ? 12  LEU A CA  1 
ATOM   80   C C   . LEU A 1 13  ? 136.609 132.447 218.589 1.00 160.09 ? 12  LEU A C   1 
ATOM   81   O O   . LEU A 1 13  ? 136.201 132.364 219.751 1.00 160.09 ? 12  LEU A O   1 
ATOM   82   C CB  . LEU A 1 13  ? 135.815 133.391 216.401 1.00 160.09 ? 12  LEU A CB  1 
ATOM   83   C CG  . LEU A 1 13  ? 135.500 133.144 214.922 1.00 160.09 ? 12  LEU A CG  1 
ATOM   84   C CD1 . LEU A 1 13  ? 136.453 132.110 214.338 1.00 160.09 ? 12  LEU A CD1 1 
ATOM   85   C CD2 . LEU A 1 13  ? 134.052 132.746 214.687 1.00 160.09 ? 12  LEU A CD2 1 
ATOM   86   N N   . SER A 1 14  ? 137.866 132.729 218.282 1.00 163.47 ? 13  SER A N   1 
ATOM   87   C CA  . SER A 1 14  ? 138.912 133.030 219.244 1.00 163.47 ? 13  SER A CA  1 
ATOM   88   C C   . SER A 1 14  ? 139.558 134.347 218.850 1.00 163.47 ? 13  SER A C   1 
ATOM   89   O O   . SER A 1 14  ? 139.442 134.782 217.701 1.00 163.47 ? 13  SER A O   1 
ATOM   90   C CB  . SER A 1 14  ? 139.971 131.918 219.286 1.00 163.47 ? 13  SER A CB  1 
ATOM   91   O OG  . SER A 1 14  ? 139.465 130.760 219.922 1.00 163.47 ? 13  SER A OG  1 
ATOM   92   N N   . PRO A 1 15  ? 140.212 135.027 219.788 1.00 160.88 ? 14  PRO A N   1 
ATOM   93   C CA  . PRO A 1 15  ? 140.888 136.280 219.434 1.00 160.88 ? 14  PRO A CA  1 
ATOM   94   C C   . PRO A 1 15  ? 141.946 136.063 218.361 1.00 160.88 ? 14  PRO A C   1 
ATOM   95   O O   . PRO A 1 15  ? 142.665 135.063 218.365 1.00 160.88 ? 14  PRO A O   1 
ATOM   96   C CB  . PRO A 1 15  ? 141.511 136.732 220.759 1.00 160.88 ? 14  PRO A CB  1 
ATOM   97   C CG  . PRO A 1 15  ? 140.671 136.088 221.807 1.00 160.88 ? 14  PRO A CG  1 
ATOM   98   C CD  . PRO A 1 15  ? 140.251 134.769 221.238 1.00 160.88 ? 14  PRO A CD  1 
ATOM   99   N N   . GLY A 1 16  ? 142.027 137.010 217.431 1.00 158.90 ? 15  GLY A N   1 
ATOM   100  C CA  . GLY A 1 16  ? 143.110 137.029 216.468 1.00 158.90 ? 15  GLY A CA  1 
ATOM   101  C C   . GLY A 1 16  ? 142.735 136.835 215.012 1.00 158.90 ? 15  GLY A C   1 
ATOM   102  O O   . GLY A 1 16  ? 143.260 137.537 214.143 1.00 158.90 ? 15  GLY A O   1 
ATOM   103  N N   . GLU A 1 17  ? 141.835 135.900 214.721 1.00 157.50 ? 16  GLU A N   1 
ATOM   104  C CA  . GLU A 1 17  ? 141.509 135.569 213.341 1.00 157.50 ? 16  GLU A CA  1 
ATOM   105  C C   . GLU A 1 17  ? 140.367 136.455 212.843 1.00 157.50 ? 16  GLU A C   1 
ATOM   106  O O   . GLU A 1 17  ? 140.045 137.484 213.440 1.00 157.50 ? 16  GLU A O   1 
ATOM   107  C CB  . GLU A 1 17  ? 141.195 134.080 213.208 1.00 157.50 ? 16  GLU A CB  1 
ATOM   108  C CG  . GLU A 1 17  ? 140.012 133.591 214.017 1.00 157.50 ? 16  GLU A CG  1 
ATOM   109  C CD  . GLU A 1 17  ? 140.384 133.250 215.444 1.00 157.50 ? 16  GLU A CD  1 
ATOM   110  O OE1 . GLU A 1 17  ? 139.622 132.501 216.092 1.00 157.50 ? 16  GLU A OE1 1 
ATOM   111  O OE2 . GLU A 1 17  ? 141.431 133.732 215.926 1.00 157.50 ? 16  GLU A OE2 1 
ATOM   112  N N   . ARG A 1 18  ? 139.769 136.079 211.716 1.00 147.61 ? 17  ARG A N   1 
ATOM   113  C CA  . ARG A 1 18  ? 138.758 136.883 211.045 1.00 147.61 ? 17  ARG A CA  1 
ATOM   114  C C   . ARG A 1 18  ? 137.355 136.355 211.326 1.00 147.61 ? 17  ARG A C   1 
ATOM   115  O O   . ARG A 1 18  ? 137.163 135.284 211.904 1.00 147.61 ? 17  ARG A O   1 
ATOM   116  C CB  . ARG A 1 18  ? 139.010 136.904 209.535 1.00 147.61 ? 17  ARG A CB  1 
ATOM   117  C CG  . ARG A 1 18  ? 140.167 137.779 209.101 1.00 147.61 ? 17  ARG A CG  1 
ATOM   118  C CD  . ARG A 1 18  ? 140.563 137.504 207.660 1.00 147.61 ? 17  ARG A CD  1 
ATOM   119  N NE  . ARG A 1 18  ? 139.504 137.847 206.718 1.00 147.61 ? 17  ARG A NE  1 
ATOM   120  C CZ  . ARG A 1 18  ? 138.666 136.972 206.178 1.00 147.61 ? 17  ARG A CZ  1 
ATOM   121  N NH1 . ARG A 1 18  ? 138.726 135.684 206.472 1.00 147.61 ? 17  ARG A NH1 1 
ATOM   122  N NH2 . ARG A 1 18  ? 137.744 137.402 205.321 1.00 147.61 ? 17  ARG A NH2 1 
ATOM   123  N N   . ALA A 1 19  ? 136.362 137.136 210.899 1.00 138.48 ? 18  ALA A N   1 
ATOM   124  C CA  . ALA A 1 19  ? 134.964 136.734 210.952 1.00 138.48 ? 18  ALA A CA  1 
ATOM   125  C C   . ALA A 1 19  ? 134.254 137.237 209.704 1.00 138.48 ? 18  ALA A C   1 
ATOM   126  O O   . ALA A 1 19  ? 134.593 138.294 209.169 1.00 138.48 ? 18  ALA A O   1 
ATOM   127  C CB  . ALA A 1 19  ? 134.265 137.268 212.206 1.00 138.48 ? 18  ALA A CB  1 
ATOM   128  N N   . THR A 1 20  ? 133.252 136.483 209.254 1.00 132.40 ? 19  THR A N   1 
ATOM   129  C CA  . THR A 1 20  ? 132.546 136.799 208.016 1.00 132.40 ? 19  THR A CA  1 
ATOM   130  C C   . THR A 1 20  ? 131.049 136.628 208.222 1.00 132.40 ? 19  THR A C   1 
ATOM   131  O O   . THR A 1 20  ? 130.593 135.543 208.593 1.00 132.40 ? 19  THR A O   1 
ATOM   132  C CB  . THR A 1 20  ? 133.026 135.908 206.869 1.00 132.40 ? 19  THR A CB  1 
ATOM   133  O OG1 . THR A 1 20  ? 134.397 136.202 206.579 1.00 132.40 ? 19  THR A OG1 1 
ATOM   134  C CG2 . THR A 1 20  ? 132.183 136.135 205.626 1.00 132.40 ? 19  THR A CG2 1 
ATOM   135  N N   . LEU A 1 21  ? 130.288 137.687 207.963 1.00 125.22 ? 20  LEU A N   1 
ATOM   136  C CA  . LEU A 1 21  ? 128.838 137.679 208.073 1.00 125.22 ? 20  LEU A CA  1 
ATOM   137  C C   . LEU A 1 21  ? 128.223 137.694 206.681 1.00 125.22 ? 20  LEU A C   1 
ATOM   138  O O   . LEU A 1 21  ? 128.923 137.803 205.672 1.00 125.22 ? 20  LEU A O   1 
ATOM   139  C CB  . LEU A 1 21  ? 128.347 138.880 208.888 1.00 125.22 ? 20  LEU A CB  1 
ATOM   140  C CG  . LEU A 1 21  ? 128.366 138.767 210.413 1.00 125.22 ? 20  LEU A CG  1 
ATOM   141  C CD1 . LEU A 1 21  ? 127.435 137.662 210.860 1.00 125.22 ? 20  LEU A CD1 1 
ATOM   142  C CD2 . LEU A 1 21  ? 129.766 138.556 210.968 1.00 125.22 ? 20  LEU A CD2 1 
ATOM   143  N N   . SER A 1 22  ? 126.897 137.583 206.628 1.00 125.84 ? 21  SER A N   1 
ATOM   144  C CA  . SER A 1 22  ? 126.210 137.611 205.345 1.00 125.84 ? 21  SER A CA  1 
ATOM   145  C C   . SER A 1 22  ? 124.758 138.021 205.534 1.00 125.84 ? 21  SER A C   1 
ATOM   146  O O   . SER A 1 22  ? 124.066 137.544 206.437 1.00 125.84 ? 21  SER A O   1 
ATOM   147  C CB  . SER A 1 22  ? 126.287 136.257 204.637 1.00 125.84 ? 21  SER A CB  1 
ATOM   148  O OG  . SER A 1 22  ? 125.561 136.283 203.423 1.00 125.84 ? 21  SER A OG  1 
ATOM   149  N N   . CYS A 1 23  ? 124.299 138.895 204.640 1.00 128.59 ? 22  CYS A N   1 
ATOM   150  C CA  . CYS A 1 23  ? 122.937 139.406 204.642 1.00 128.59 ? 22  CYS A CA  1 
ATOM   151  C C   . CYS A 1 23  ? 122.385 139.262 203.232 1.00 128.59 ? 22  CYS A C   1 
ATOM   152  O O   . CYS A 1 23  ? 123.045 139.644 202.261 1.00 128.59 ? 22  CYS A O   1 
ATOM   153  C CB  . CYS A 1 23  ? 122.908 140.876 205.104 1.00 128.59 ? 22  CYS A CB  1 
ATOM   154  S SG  . CYS A 1 23  ? 121.295 141.583 205.551 1.00 128.59 ? 22  CYS A SG  1 
ATOM   155  N N   . ARG A 1 24  ? 121.186 138.696 203.115 1.00 130.02 ? 23  ARG A N   1 
ATOM   156  C CA  . ARG A 1 24  ? 120.605 138.392 201.814 1.00 130.02 ? 23  ARG A CA  1 
ATOM   157  C C   . ARG A 1 24  ? 119.285 139.128 201.657 1.00 130.02 ? 23  ARG A C   1 
ATOM   158  O O   . ARG A 1 24  ? 118.466 139.146 202.580 1.00 130.02 ? 23  ARG A O   1 
ATOM   159  C CB  . ARG A 1 24  ? 120.396 136.883 201.649 1.00 130.02 ? 23  ARG A CB  1 
ATOM   160  C CG  . ARG A 1 24  ? 119.319 136.503 200.644 1.00 130.02 ? 23  ARG A CG  1 
ATOM   161  C CD  . ARG A 1 24  ? 119.779 136.754 199.218 1.00 130.02 ? 23  ARG A CD  1 
ATOM   162  N NE  . ARG A 1 24  ? 119.022 135.970 198.251 1.00 130.02 ? 23  ARG A NE  1 
ATOM   163  C CZ  . ARG A 1 24  ? 119.221 134.681 198.014 1.00 130.02 ? 23  ARG A CZ  1 
ATOM   164  N NH1 . ARG A 1 24  ? 120.155 133.997 198.652 1.00 130.02 ? 23  ARG A NH1 1 
ATOM   165  N NH2 . ARG A 1 24  ? 118.463 134.063 197.113 1.00 130.02 ? 23  ARG A NH2 1 
ATOM   166  N N   . ALA A 1 25  ? 119.079 139.727 200.489 1.00 128.66 ? 24  ALA A N   1 
ATOM   167  C CA  . ALA A 1 25  ? 117.858 140.458 200.192 1.00 128.66 ? 24  ALA A CA  1 
ATOM   168  C C   . ALA A 1 25  ? 116.923 139.607 199.346 1.00 128.66 ? 24  ALA A C   1 
ATOM   169  O O   . ALA A 1 25  ? 117.360 138.824 198.500 1.00 128.66 ? 24  ALA A O   1 
ATOM   170  C CB  . ALA A 1 25  ? 118.168 141.766 199.465 1.00 128.66 ? 24  ALA A CB  1 
ATOM   171  N N   . SER A 1 26  ? 115.620 139.765 199.591 1.00 130.35 ? 25  SER A N   1 
ATOM   172  C CA  . SER A 1 26  ? 114.628 139.017 198.827 1.00 130.35 ? 25  SER A CA  1 
ATOM   173  C C   . SER A 1 26  ? 114.647 139.415 197.357 1.00 130.35 ? 25  SER A C   1 
ATOM   174  O O   . SER A 1 26  ? 114.526 138.560 196.474 1.00 130.35 ? 25  SER A O   1 
ATOM   175  C CB  . SER A 1 26  ? 113.239 139.225 199.425 1.00 130.35 ? 25  SER A CB  1 
ATOM   176  O OG  . SER A 1 26  ? 112.894 140.597 199.441 1.00 130.35 ? 25  SER A OG  1 
ATOM   177  N N   . GLN A 1 27  ? 114.794 140.707 197.074 1.00 131.18 ? 26  GLN A N   1 
ATOM   178  C CA  . GLN A 1 27  ? 114.916 141.194 195.709 1.00 131.18 ? 26  GLN A CA  1 
ATOM   179  C C   . GLN A 1 27  ? 115.941 142.320 195.682 1.00 131.18 ? 26  GLN A C   1 
ATOM   180  O O   . GLN A 1 27  ? 116.569 142.639 196.695 1.00 131.18 ? 26  GLN A O   1 
ATOM   181  C CB  . GLN A 1 27  ? 113.561 141.644 195.154 1.00 131.18 ? 26  GLN A CB  1 
ATOM   182  C CG  . GLN A 1 27  ? 112.765 142.512 196.094 1.00 131.18 ? 26  GLN A CG  1 
ATOM   183  C CD  . GLN A 1 27  ? 111.322 142.646 195.662 1.00 131.18 ? 26  GLN A CD  1 
ATOM   184  O OE1 . GLN A 1 27  ? 110.463 141.873 196.081 1.00 131.18 ? 26  GLN A OE1 1 
ATOM   185  N NE2 . GLN A 1 27  ? 111.048 143.628 194.814 1.00 131.18 ? 26  GLN A NE2 1 
ATOM   186  N N   . SER A 1 28  ? 116.114 142.920 194.509 1.00 128.75 ? 27  SER A N   1 
ATOM   187  C CA  . SER A 1 28  ? 117.179 143.894 194.315 1.00 128.75 ? 27  SER A CA  1 
ATOM   188  C C   . SER A 1 28  ? 116.919 145.165 195.112 1.00 128.75 ? 27  SER A C   1 
ATOM   189  O O   . SER A 1 28  ? 115.781 145.627 195.223 1.00 128.75 ? 27  SER A O   1 
ATOM   190  C CB  . SER A 1 28  ? 117.320 144.231 192.833 1.00 128.75 ? 27  SER A CB  1 
ATOM   191  O OG  . SER A 1 28  ? 118.301 145.232 192.634 1.00 128.75 ? 27  SER A OG  1 
ATOM   192  N N   . VAL A 1 29  ? 117.989 145.730 195.670 1.00 119.48 ? 28  VAL A N   1 
ATOM   193  C CA  . VAL A 1 29  ? 117.917 147.011 196.363 1.00 119.48 ? 28  VAL A CA  1 
ATOM   194  C C   . VAL A 1 29  ? 118.590 148.081 195.511 1.00 119.48 ? 28  VAL A C   1 
ATOM   195  O O   . VAL A 1 29  ? 119.807 148.281 195.576 1.00 119.48 ? 28  VAL A O   1 
ATOM   196  C CB  . VAL A 1 29  ? 118.535 146.924 197.771 1.00 119.48 ? 28  VAL A CB  1 
ATOM   197  C CG1 . VAL A 1 29  ? 117.622 146.145 198.685 1.00 119.48 ? 28  VAL A CG1 1 
ATOM   198  C CG2 . VAL A 1 29  ? 119.883 146.236 197.728 1.00 119.48 ? 28  VAL A CG2 1 
ATOM   199  N N   . SER A 1 30  ? 117.795 148.778 194.700 1.00 116.72 ? 29  SER A N   1 
ATOM   200  C CA  . SER A 1 30  ? 118.345 149.798 193.818 1.00 116.72 ? 29  SER A CA  1 
ATOM   201  C C   . SER A 1 30  ? 118.820 151.029 194.576 1.00 116.72 ? 29  SER A C   1 
ATOM   202  O O   . SER A 1 30  ? 119.689 151.750 194.077 1.00 116.72 ? 29  SER A O   1 
ATOM   203  C CB  . SER A 1 30  ? 117.307 150.202 192.773 1.00 116.72 ? 29  SER A CB  1 
ATOM   204  O OG  . SER A 1 30  ? 116.980 149.107 191.936 1.00 116.72 ? 29  SER A OG  1 
ATOM   205  N N   . SER A 1 31  ? 118.270 151.290 195.762 1.00 111.79 ? 30  SER A N   1 
ATOM   206  C CA  . SER A 1 31  ? 118.705 152.451 196.528 1.00 111.79 ? 30  SER A CA  1 
ATOM   207  C C   . SER A 1 31  ? 120.109 152.263 197.086 1.00 111.79 ? 30  SER A C   1 
ATOM   208  O O   . SER A 1 31  ? 120.853 153.240 197.221 1.00 111.79 ? 30  SER A O   1 
ATOM   209  C CB  . SER A 1 31  ? 117.713 152.736 197.655 1.00 111.79 ? 30  SER A CB  1 
ATOM   210  O OG  . SER A 1 31  ? 117.499 151.585 198.450 1.00 111.79 ? 30  SER A OG  1 
ATOM   211  N N   . THR A 1 32  ? 120.489 151.027 197.403 1.00 106.70 ? 31  THR A N   1 
ATOM   212  C CA  . THR A 1 32  ? 121.813 150.694 197.927 1.00 106.70 ? 31  THR A CA  1 
ATOM   213  C C   . THR A 1 32  ? 122.131 151.512 199.175 1.00 106.70 ? 31  THR A C   1 
ATOM   214  O O   . THR A 1 32  ? 123.057 152.320 199.204 1.00 106.70 ? 31  THR A O   1 
ATOM   215  C CB  . THR A 1 32  ? 122.898 150.891 196.868 1.00 106.70 ? 31  THR A CB  1 
ATOM   216  O OG1 . THR A 1 32  ? 122.936 152.265 196.468 1.00 106.70 ? 31  THR A OG1 1 
ATOM   217  C CG2 . THR A 1 32  ? 122.613 150.029 195.655 1.00 106.70 ? 31  THR A CG2 1 
ATOM   218  N N   . PHE A 1 33  ? 121.339 151.287 200.217 1.00 104.66 ? 32  PHE A N   1 
ATOM   219  C CA  . PHE A 1 33  ? 121.486 151.988 201.485 1.00 104.66 ? 32  PHE A CA  1 
ATOM   220  C C   . PHE A 1 33  ? 121.594 151.008 202.646 1.00 104.66 ? 32  PHE A C   1 
ATOM   221  O O   . PHE A 1 33  ? 121.053 151.238 203.727 1.00 104.66 ? 32  PHE A O   1 
ATOM   222  C CB  . PHE A 1 33  ? 120.329 152.957 201.706 1.00 104.66 ? 32  PHE A CB  1 
ATOM   223  C CG  . PHE A 1 33  ? 120.379 154.170 200.826 1.00 104.66 ? 32  PHE A CG  1 
ATOM   224  C CD1 . PHE A 1 33  ? 121.583 154.764 200.511 1.00 104.66 ? 32  PHE A CD1 1 
ATOM   225  C CD2 . PHE A 1 33  ? 119.219 154.715 200.311 1.00 104.66 ? 32  PHE A CD2 1 
ATOM   226  C CE1 . PHE A 1 33  ? 121.627 155.878 199.703 1.00 104.66 ? 32  PHE A CE1 1 
ATOM   227  C CE2 . PHE A 1 33  ? 119.261 155.828 199.503 1.00 104.66 ? 32  PHE A CE2 1 
ATOM   228  C CZ  . PHE A 1 33  ? 120.465 156.408 199.199 1.00 104.66 ? 32  PHE A CZ  1 
ATOM   229  N N   . LEU A 1 34  ? 122.297 149.901 202.434 1.00 104.66 ? 33  LEU A N   1 
ATOM   230  C CA  . LEU A 1 34  ? 122.490 148.924 203.496 1.00 104.66 ? 33  LEU A CA  1 
ATOM   231  C C   . LEU A 1 34  ? 123.402 149.474 204.581 1.00 104.66 ? 33  LEU A C   1 
ATOM   232  O O   . LEU A 1 34  ? 124.412 150.120 204.297 1.00 104.66 ? 33  LEU A O   1 
ATOM   233  C CB  . LEU A 1 34  ? 123.069 147.629 202.934 1.00 104.66 ? 33  LEU A CB  1 
ATOM   234  C CG  . LEU A 1 34  ? 122.084 146.631 202.325 1.00 104.66 ? 33  LEU A CG  1 
ATOM   235  C CD1 . LEU A 1 34  ? 121.146 146.128 203.402 1.00 104.66 ? 33  LEU A CD1 1 
ATOM   236  C CD2 . LEU A 1 34  ? 121.288 147.230 201.178 1.00 104.66 ? 33  LEU A CD2 1 
ATOM   237  N N   . ALA A 1 35  ? 123.041 149.212 205.833 1.00 104.66 ? 34  ALA A N   1 
ATOM   238  C CA  . ALA A 1 35  ? 123.810 149.685 206.970 1.00 104.66 ? 34  ALA A CA  1 
ATOM   239  C C   . ALA A 1 35  ? 123.958 148.563 207.983 1.00 104.66 ? 34  ALA A C   1 
ATOM   240  O O   . ALA A 1 35  ? 123.109 147.672 208.076 1.00 104.66 ? 34  ALA A O   1 
ATOM   241  C CB  . ALA A 1 35  ? 123.155 150.901 207.630 1.00 104.66 ? 34  ALA A CB  1 
ATOM   242  N N   . TRP A 1 36  ? 125.043 148.626 208.749 1.00 104.66 ? 35  TRP A N   1 
ATOM   243  C CA  . TRP A 1 36  ? 125.378 147.597 209.725 1.00 104.66 ? 35  TRP A CA  1 
ATOM   244  C C   . TRP A 1 36  ? 125.477 148.208 211.114 1.00 104.66 ? 35  TRP A C   1 
ATOM   245  O O   . TRP A 1 36  ? 126.189 149.196 211.311 1.00 104.66 ? 35  TRP A O   1 
ATOM   246  C CB  . TRP A 1 36  ? 126.690 146.905 209.356 1.00 104.66 ? 35  TRP A CB  1 
ATOM   247  C CG  . TRP A 1 36  ? 126.625 146.168 208.061 1.00 104.66 ? 35  TRP A CG  1 
ATOM   248  C CD1 . TRP A 1 36  ? 126.849 146.677 206.820 1.00 104.66 ? 35  TRP A CD1 1 
ATOM   249  C CD2 . TRP A 1 36  ? 126.310 144.787 207.876 1.00 104.66 ? 35  TRP A CD2 1 
ATOM   250  N NE1 . TRP A 1 36  ? 126.694 145.700 205.871 1.00 104.66 ? 35  TRP A NE1 1 
ATOM   251  C CE2 . TRP A 1 36  ? 126.362 144.529 206.496 1.00 104.66 ? 35  TRP A CE2 1 
ATOM   252  C CE3 . TRP A 1 36  ? 125.987 143.744 208.745 1.00 104.66 ? 35  TRP A CE3 1 
ATOM   253  C CZ2 . TRP A 1 36  ? 126.103 143.273 205.965 1.00 104.66 ? 35  TRP A CZ2 1 
ATOM   254  C CZ3 . TRP A 1 36  ? 125.730 142.499 208.216 1.00 104.66 ? 35  TRP A CZ3 1 
ATOM   255  C CH2 . TRP A 1 36  ? 125.790 142.273 206.840 1.00 104.66 ? 35  TRP A CH2 1 
ATOM   256  N N   . TYR A 1 37  ? 124.782 147.607 212.075 1.00 104.66 ? 36  TYR A N   1 
ATOM   257  C CA  . TYR A 1 37  ? 124.735 148.095 213.445 1.00 104.66 ? 36  TYR A CA  1 
ATOM   258  C C   . TYR A 1 37  ? 125.255 147.032 214.398 1.00 104.66 ? 36  TYR A C   1 
ATOM   259  O O   . TYR A 1 37  ? 125.014 145.838 214.202 1.00 104.66 ? 36  TYR A O   1 
ATOM   260  C CB  . TYR A 1 37  ? 123.312 148.480 213.856 1.00 104.66 ? 36  TYR A CB  1 
ATOM   261  C CG  . TYR A 1 37  ? 122.677 149.542 212.998 1.00 104.66 ? 36  TYR A CG  1 
ATOM   262  C CD1 . TYR A 1 37  ? 122.061 149.216 211.803 1.00 104.66 ? 36  TYR A CD1 1 
ATOM   263  C CD2 . TYR A 1 37  ? 122.683 150.870 213.388 1.00 104.66 ? 36  TYR A CD2 1 
ATOM   264  C CE1 . TYR A 1 37  ? 121.479 150.179 211.018 1.00 104.66 ? 36  TYR A CE1 1 
ATOM   265  C CE2 . TYR A 1 37  ? 122.101 151.840 212.606 1.00 104.66 ? 36  TYR A CE2 1 
ATOM   266  C CZ  . TYR A 1 37  ? 121.502 151.487 211.423 1.00 104.66 ? 36  TYR A CZ  1 
ATOM   267  O OH  . TYR A 1 37  ? 120.920 152.448 210.635 1.00 104.66 ? 36  TYR A OH  1 
ATOM   268  N N   . GLN A 1 38  ? 125.954 147.475 215.438 1.00 112.32 ? 37  GLN A N   1 
ATOM   269  C CA  . GLN A 1 38  ? 126.452 146.605 216.493 1.00 112.32 ? 37  GLN A CA  1 
ATOM   270  C C   . GLN A 1 38  ? 125.832 147.021 217.816 1.00 112.32 ? 37  GLN A C   1 
ATOM   271  O O   . GLN A 1 38  ? 125.844 148.205 218.164 1.00 112.32 ? 37  GLN A O   1 
ATOM   272  C CB  . GLN A 1 38  ? 127.973 146.669 216.597 1.00 112.32 ? 37  GLN A CB  1 
ATOM   273  C CG  . GLN A 1 38  ? 128.509 146.128 217.907 1.00 112.32 ? 37  GLN A CG  1 
ATOM   274  C CD  . GLN A 1 38  ? 129.962 146.471 218.128 1.00 112.32 ? 37  GLN A CD  1 
ATOM   275  O OE1 . GLN A 1 38  ? 130.302 147.609 218.445 1.00 112.32 ? 37  GLN A OE1 1 
ATOM   276  N NE2 . GLN A 1 38  ? 130.832 145.484 217.965 1.00 112.32 ? 37  GLN A NE2 1 
ATOM   277  N N   . GLN A 1 39  ? 125.304 146.051 218.556 1.00 119.50 ? 38  GLN A N   1 
ATOM   278  C CA  . GLN A 1 39  ? 124.630 146.317 219.819 1.00 119.50 ? 38  GLN A CA  1 
ATOM   279  C C   . GLN A 1 39  ? 125.238 145.454 220.910 1.00 119.50 ? 38  GLN A C   1 
ATOM   280  O O   . GLN A 1 39  ? 125.324 144.229 220.763 1.00 119.50 ? 38  GLN A O   1 
ATOM   281  C CB  . GLN A 1 39  ? 123.127 146.054 219.706 1.00 119.50 ? 38  GLN A CB  1 
ATOM   282  C CG  . GLN A 1 39  ? 122.350 146.392 220.963 1.00 119.50 ? 38  GLN A CG  1 
ATOM   283  C CD  . GLN A 1 39  ? 120.941 145.845 220.938 1.00 119.50 ? 38  GLN A CD  1 
ATOM   284  O OE1 . GLN A 1 39  ? 120.535 145.190 219.981 1.00 119.50 ? 38  GLN A OE1 1 
ATOM   285  N NE2 . GLN A 1 39  ? 120.185 146.113 221.994 1.00 119.50 ? 38  GLN A NE2 1 
ATOM   286  N N   . LYS A 1 40  ? 125.674 146.098 221.986 1.00 131.17 ? 39  LYS A N   1 
ATOM   287  C CA  . LYS A 1 40  ? 126.034 145.421 223.217 1.00 131.17 ? 39  LYS A CA  1 
ATOM   288  C C   . LYS A 1 40  ? 124.793 145.228 224.079 1.00 131.17 ? 39  LYS A C   1 
ATOM   289  O O   . LYS A 1 40  ? 123.814 145.964 223.944 1.00 131.17 ? 39  LYS A O   1 
ATOM   290  C CB  . LYS A 1 40  ? 127.076 146.232 223.980 1.00 131.17 ? 39  LYS A CB  1 
ATOM   291  C CG  . LYS A 1 40  ? 128.502 145.742 223.819 1.00 131.17 ? 39  LYS A CG  1 
ATOM   292  C CD  . LYS A 1 40  ? 129.009 145.970 222.410 1.00 131.17 ? 39  LYS A CD  1 
ATOM   293  C CE  . LYS A 1 40  ? 130.524 146.034 222.383 1.00 131.17 ? 39  LYS A CE  1 
ATOM   294  N NZ  . LYS A 1 40  ? 131.050 146.147 220.997 1.00 131.17 ? 39  LYS A NZ  1 
ATOM   295  N N   . PRO A 1 41  ? 124.800 144.236 224.968 1.00 139.20 ? 40  PRO A N   1 
ATOM   296  C CA  . PRO A 1 41  ? 123.654 144.057 225.867 1.00 139.20 ? 40  PRO A CA  1 
ATOM   297  C C   . PRO A 1 41  ? 123.465 145.263 226.775 1.00 139.20 ? 40  PRO A C   1 
ATOM   298  O O   . PRO A 1 41  ? 124.427 145.832 227.295 1.00 139.20 ? 40  PRO A O   1 
ATOM   299  C CB  . PRO A 1 41  ? 124.022 142.802 226.665 1.00 139.20 ? 40  PRO A CB  1 
ATOM   300  C CG  . PRO A 1 41  ? 125.506 142.696 226.547 1.00 139.20 ? 40  PRO A CG  1 
ATOM   301  C CD  . PRO A 1 41  ? 125.833 143.211 225.184 1.00 139.20 ? 40  PRO A CD  1 
ATOM   302  N N   . GLY A 1 42  ? 122.205 145.648 226.966 1.00 141.32 ? 41  GLY A N   1 
ATOM   303  C CA  . GLY A 1 42  ? 121.879 146.755 227.842 1.00 141.32 ? 41  GLY A CA  1 
ATOM   304  C C   . GLY A 1 42  ? 122.193 148.129 227.298 1.00 141.32 ? 41  GLY A C   1 
ATOM   305  O O   . GLY A 1 42  ? 122.145 149.101 228.056 1.00 141.32 ? 41  GLY A O   1 
ATOM   306  N N   . GLN A 1 43  ? 122.515 148.245 226.013 1.00 134.83 ? 42  GLN A N   1 
ATOM   307  C CA  . GLN A 1 43  ? 122.922 149.509 225.421 1.00 134.83 ? 42  GLN A CA  1 
ATOM   308  C C   . GLN A 1 43  ? 122.227 149.702 224.083 1.00 134.83 ? 42  GLN A C   1 
ATOM   309  O O   . GLN A 1 43  ? 121.759 148.749 223.456 1.00 134.83 ? 42  GLN A O   1 
ATOM   310  C CB  . GLN A 1 43  ? 124.443 149.577 225.228 1.00 134.83 ? 42  GLN A CB  1 
ATOM   311  C CG  . GLN A 1 43  ? 125.246 149.257 226.475 1.00 134.83 ? 42  GLN A CG  1 
ATOM   312  C CD  . GLN A 1 43  ? 126.715 149.058 226.181 1.00 134.83 ? 42  GLN A CD  1 
ATOM   313  O OE1 . GLN A 1 43  ? 127.186 149.355 225.083 1.00 134.83 ? 42  GLN A OE1 1 
ATOM   314  N NE2 . GLN A 1 43  ? 127.450 148.544 227.159 1.00 134.83 ? 42  GLN A NE2 1 
ATOM   315  N N   . ALA A 1 44  ? 122.163 150.958 223.653 1.00 122.02 ? 43  ALA A N   1 
ATOM   316  C CA  . ALA A 1 44  ? 121.581 151.273 222.363 1.00 122.02 ? 43  ALA A CA  1 
ATOM   317  C C   . ALA A 1 44  ? 122.496 150.796 221.237 1.00 122.02 ? 43  ALA A C   1 
ATOM   318  O O   . ALA A 1 44  ? 123.716 150.738 221.402 1.00 122.02 ? 43  ALA A O   1 
ATOM   319  C CB  . ALA A 1 44  ? 121.343 152.773 222.237 1.00 122.02 ? 43  ALA A CB  1 
ATOM   320  N N   . PRO A 1 45  ? 121.930 150.444 220.085 1.00 115.18 ? 44  PRO A N   1 
ATOM   321  C CA  . PRO A 1 45  ? 122.763 150.019 218.958 1.00 115.18 ? 44  PRO A CA  1 
ATOM   322  C C   . PRO A 1 45  ? 123.659 151.146 218.469 1.00 115.18 ? 44  PRO A C   1 
ATOM   323  O O   . PRO A 1 45  ? 123.368 152.329 218.654 1.00 115.18 ? 44  PRO A O   1 
ATOM   324  C CB  . PRO A 1 45  ? 121.740 149.618 217.891 1.00 115.18 ? 44  PRO A CB  1 
ATOM   325  C CG  . PRO A 1 45  ? 120.509 149.307 218.651 1.00 115.18 ? 44  PRO A CG  1 
ATOM   326  C CD  . PRO A 1 45  ? 120.499 150.247 219.814 1.00 115.18 ? 44  PRO A CD  1 
ATOM   327  N N   . ARG A 1 46  ? 124.767 150.760 217.848 1.00 112.80 ? 45  ARG A N   1 
ATOM   328  C CA  . ARG A 1 46  ? 125.757 151.693 217.336 1.00 112.80 ? 45  ARG A CA  1 
ATOM   329  C C   . ARG A 1 46  ? 125.930 151.476 215.841 1.00 112.80 ? 45  ARG A C   1 
ATOM   330  O O   . ARG A 1 46  ? 125.877 150.342 215.361 1.00 112.80 ? 45  ARG A O   1 
ATOM   331  C CB  . ARG A 1 46  ? 127.094 151.512 218.054 1.00 112.80 ? 45  ARG A CB  1 
ATOM   332  C CG  . ARG A 1 46  ? 128.135 152.553 217.713 1.00 112.80 ? 45  ARG A CG  1 
ATOM   333  C CD  . ARG A 1 46  ? 129.081 152.760 218.878 1.00 112.80 ? 45  ARG A CD  1 
ATOM   334  N NE  . ARG A 1 46  ? 129.762 151.525 219.248 1.00 112.80 ? 45  ARG A NE  1 
ATOM   335  C CZ  . ARG A 1 46  ? 130.942 151.151 218.775 1.00 112.80 ? 45  ARG A CZ  1 
ATOM   336  N NH1 . ARG A 1 46  ? 131.608 151.896 217.908 1.00 112.80 ? 45  ARG A NH1 1 
ATOM   337  N NH2 . ARG A 1 46  ? 131.469 150.000 219.183 1.00 112.80 ? 45  ARG A NH2 1 
ATOM   338  N N   . LEU A 1 47  ? 126.129 152.564 215.106 1.00 104.66 ? 46  LEU A N   1 
ATOM   339  C CA  . LEU A 1 47  ? 126.301 152.482 213.664 1.00 104.66 ? 46  LEU A CA  1 
ATOM   340  C C   . LEU A 1 47  ? 127.746 152.156 213.317 1.00 104.66 ? 46  LEU A C   1 
ATOM   341  O O   . LEU A 1 47  ? 128.678 152.688 213.924 1.00 104.66 ? 46  LEU A O   1 
ATOM   342  C CB  . LEU A 1 47  ? 125.888 153.797 213.010 1.00 104.66 ? 46  LEU A CB  1 
ATOM   343  C CG  . LEU A 1 47  ? 126.190 153.948 211.522 1.00 104.66 ? 46  LEU A CG  1 
ATOM   344  C CD1 . LEU A 1 47  ? 125.429 152.917 210.725 1.00 104.66 ? 46  LEU A CD1 1 
ATOM   345  C CD2 . LEU A 1 47  ? 125.844 155.343 211.052 1.00 104.66 ? 46  LEU A CD2 1 
ATOM   346  N N   . LEU A 1 48  ? 127.932 151.270 212.337 1.00 105.84 ? 47  LEU A N   1 
ATOM   347  C CA  . LEU A 1 48  ? 129.261 150.894 211.870 1.00 105.84 ? 47  LEU A CA  1 
ATOM   348  C C   . LEU A 1 48  ? 129.514 151.319 210.430 1.00 105.84 ? 47  LEU A C   1 
ATOM   349  O O   . LEU A 1 48  ? 130.482 152.030 210.157 1.00 105.84 ? 47  LEU A O   1 
ATOM   350  C CB  . LEU A 1 48  ? 129.471 149.381 212.007 1.00 105.84 ? 47  LEU A CB  1 
ATOM   351  C CG  . LEU A 1 48  ? 129.477 148.781 213.410 1.00 105.84 ? 47  LEU A CG  1 
ATOM   352  C CD1 . LEU A 1 48  ? 129.544 147.270 213.326 1.00 105.84 ? 47  LEU A CD1 1 
ATOM   353  C CD2 . LEU A 1 48  ? 130.636 149.321 214.218 1.00 105.84 ? 47  LEU A CD2 1 
ATOM   354  N N   . ILE A 1 49  ? 128.674 150.892 209.493 1.00 104.66 ? 48  ILE A N   1 
ATOM   355  C CA  . ILE A 1 49  ? 128.880 151.151 208.074 1.00 104.66 ? 48  ILE A CA  1 
ATOM   356  C C   . ILE A 1 49  ? 127.560 151.578 207.455 1.00 104.66 ? 48  ILE A C   1 
ATOM   357  O O   . ILE A 1 49  ? 126.521 150.961 207.717 1.00 104.66 ? 48  ILE A O   1 
ATOM   358  C CB  . ILE A 1 49  ? 129.432 149.914 207.344 1.00 104.66 ? 48  ILE A CB  1 
ATOM   359  C CG1 . ILE A 1 49  ? 130.804 149.536 207.887 1.00 104.66 ? 48  ILE A CG1 1 
ATOM   360  C CG2 . ILE A 1 49  ? 129.510 150.161 205.852 1.00 104.66 ? 48  ILE A CG2 1 
ATOM   361  C CD1 . ILE A 1 49  ? 131.282 148.199 207.401 1.00 104.66 ? 48  ILE A CD1 1 
ATOM   362  N N   . TYR A 1 50  ? 127.605 152.628 206.639 1.00 104.66 ? 49  TYR A N   1 
ATOM   363  C CA  . TYR A 1 50  ? 126.487 153.056 205.813 1.00 104.66 ? 49  TYR A CA  1 
ATOM   364  C C   . TYR A 1 50  ? 126.912 153.040 204.353 1.00 104.66 ? 49  TYR A C   1 
ATOM   365  O O   . TYR A 1 50  ? 128.084 153.245 204.032 1.00 104.66 ? 49  TYR A O   1 
ATOM   366  C CB  . TYR A 1 50  ? 126.001 154.455 206.201 1.00 104.66 ? 49  TYR A CB  1 
ATOM   367  C CG  . TYR A 1 50  ? 126.978 155.566 205.900 1.00 104.66 ? 49  TYR A CG  1 
ATOM   368  C CD1 . TYR A 1 50  ? 126.991 156.195 204.665 1.00 104.66 ? 49  TYR A CD1 1 
ATOM   369  C CD2 . TYR A 1 50  ? 127.878 155.998 206.859 1.00 104.66 ? 49  TYR A CD2 1 
ATOM   370  C CE1 . TYR A 1 50  ? 127.881 157.209 204.392 1.00 104.66 ? 49  TYR A CE1 1 
ATOM   371  C CE2 . TYR A 1 50  ? 128.769 157.013 206.594 1.00 104.66 ? 49  TYR A CE2 1 
ATOM   372  C CZ  . TYR A 1 50  ? 128.766 157.614 205.360 1.00 104.66 ? 49  TYR A CZ  1 
ATOM   373  O OH  . TYR A 1 50  ? 129.654 158.626 205.094 1.00 104.66 ? 49  TYR A OH  1 
ATOM   374  N N   . GLY A 1 51  ? 125.954 152.788 203.467 1.00 104.66 ? 50  GLY A N   1 
ATOM   375  C CA  . GLY A 1 51  ? 126.286 152.663 202.064 1.00 104.66 ? 50  GLY A CA  1 
ATOM   376  C C   . GLY A 1 51  ? 126.988 151.376 201.707 1.00 104.66 ? 50  GLY A C   1 
ATOM   377  O O   . GLY A 1 51  ? 127.450 151.235 200.572 1.00 104.66 ? 50  GLY A O   1 
ATOM   378  N N   . ALA A 1 52  ? 127.099 150.452 202.664 1.00 104.66 ? 51  ALA A N   1 
ATOM   379  C CA  . ALA A 1 52  ? 127.688 149.124 202.515 1.00 104.66 ? 51  ALA A CA  1 
ATOM   380  C C   . ALA A 1 52  ? 129.207 149.162 202.417 1.00 104.66 ? 51  ALA A C   1 
ATOM   381  O O   . ALA A 1 52  ? 129.854 148.112 202.460 1.00 104.66 ? 51  ALA A O   1 
ATOM   382  C CB  . ALA A 1 52  ? 127.102 148.399 201.300 1.00 104.66 ? 51  ALA A CB  1 
ATOM   383  N N   . SER A 1 53  ? 129.795 150.348 202.290 1.00 104.66 ? 52  SER A N   1 
ATOM   384  C CA  . SER A 1 53  ? 131.250 150.431 202.201 1.00 104.66 ? 52  SER A CA  1 
ATOM   385  C C   . SER A 1 53  ? 131.887 151.509 203.065 1.00 104.66 ? 52  SER A C   1 
ATOM   386  O O   . SER A 1 53  ? 133.043 151.337 203.462 1.00 104.66 ? 52  SER A O   1 
ATOM   387  C CB  . SER A 1 53  ? 131.677 150.654 200.747 1.00 104.66 ? 52  SER A CB  1 
ATOM   388  O OG  . SER A 1 53  ? 131.501 149.477 199.982 1.00 104.66 ? 52  SER A OG  1 
ATOM   389  N N   . TYR A 1 54  ? 131.199 152.599 203.383 1.00 104.66 ? 53  TYR A N   1 
ATOM   390  C CA  . TYR A 1 54  ? 131.839 153.753 203.994 1.00 104.66 ? 53  TYR A CA  1 
ATOM   391  C C   . TYR A 1 54  ? 131.819 153.644 205.510 1.00 104.66 ? 53  TYR A C   1 
ATOM   392  O O   . TYR A 1 54  ? 130.844 153.174 206.098 1.00 104.66 ? 53  TYR A O   1 
ATOM   393  C CB  . TYR A 1 54  ? 131.152 155.042 203.549 1.00 104.66 ? 53  TYR A CB  1 
ATOM   394  C CG  . TYR A 1 54  ? 131.137 155.228 202.051 1.00 104.66 ? 53  TYR A CG  1 
ATOM   395  C CD1 . TYR A 1 54  ? 130.195 154.591 201.263 1.00 104.66 ? 53  TYR A CD1 1 
ATOM   396  C CD2 . TYR A 1 54  ? 132.069 156.037 201.425 1.00 104.66 ? 53  TYR A CD2 1 
ATOM   397  C CE1 . TYR A 1 54  ? 130.178 154.754 199.900 1.00 104.66 ? 53  TYR A CE1 1 
ATOM   398  C CE2 . TYR A 1 54  ? 132.059 156.205 200.060 1.00 104.66 ? 53  TYR A CE2 1 
ATOM   399  C CZ  . TYR A 1 54  ? 131.110 155.561 199.304 1.00 104.66 ? 53  TYR A CZ  1 
ATOM   400  O OH  . TYR A 1 54  ? 131.092 155.724 197.941 1.00 104.66 ? 53  TYR A OH  1 
ATOM   401  N N   . MET A 1 55  ? 132.904 154.082 206.136 1.00 107.01 ? 54  MET A N   1 
ATOM   402  C CA  . MET A 1 55  ? 133.047 153.948 207.574 1.00 107.01 ? 54  MET A CA  1 
ATOM   403  C C   . MET A 1 55  ? 132.327 155.080 208.298 1.00 107.01 ? 54  MET A C   1 
ATOM   404  O O   . MET A 1 55  ? 132.117 156.167 207.758 1.00 107.01 ? 54  MET A O   1 
ATOM   405  C CB  . MET A 1 55  ? 134.524 153.929 207.962 1.00 107.01 ? 54  MET A CB  1 
ATOM   406  C CG  . MET A 1 55  ? 134.876 152.898 209.014 1.00 107.01 ? 54  MET A CG  1 
ATOM   407  S SD  . MET A 1 55  ? 134.914 151.233 208.330 1.00 107.01 ? 54  MET A SD  1 
ATOM   408  C CE  . MET A 1 55  ? 136.120 151.437 207.025 1.00 107.01 ? 54  MET A CE  1 
ATOM   409  N N   . ALA A 1 56  ? 131.946 154.808 209.541 1.00 110.53 ? 55  ALA A N   1 
ATOM   410  C CA  . ALA A 1 56  ? 131.261 155.784 210.373 1.00 110.53 ? 55  ALA A CA  1 
ATOM   411  C C   . ALA A 1 56  ? 132.281 156.559 211.203 1.00 110.53 ? 55  ALA A C   1 
ATOM   412  O O   . ALA A 1 56  ? 133.492 156.445 211.006 1.00 110.53 ? 55  ALA A O   1 
ATOM   413  C CB  . ALA A 1 56  ? 130.225 155.094 211.253 1.00 110.53 ? 55  ALA A CB  1 
ATOM   414  N N   . THR A 1 57  ? 131.795 157.348 212.156 1.00 116.85 ? 56  THR A N   1 
ATOM   415  C CA  . THR A 1 57  ? 132.661 158.197 212.962 1.00 116.85 ? 56  THR A CA  1 
ATOM   416  C C   . THR A 1 57  ? 133.325 157.392 214.071 1.00 116.85 ? 56  THR A C   1 
ATOM   417  O O   . THR A 1 57  ? 132.654 156.668 214.812 1.00 116.85 ? 56  THR A O   1 
ATOM   418  C CB  . THR A 1 57  ? 131.859 159.347 213.565 1.00 116.85 ? 56  THR A CB  1 
ATOM   419  O OG1 . THR A 1 57  ? 131.279 160.128 212.514 1.00 116.85 ? 56  THR A OG1 1 
ATOM   420  C CG2 . THR A 1 57  ? 132.755 160.231 214.414 1.00 116.85 ? 56  THR A CG2 1 
ATOM   421  N N   . GLY A 1 58  ? 134.641 157.531 214.191 1.00 116.97 ? 57  GLY A N   1 
ATOM   422  C CA  . GLY A 1 58  ? 135.367 156.883 215.273 1.00 116.97 ? 57  GLY A CA  1 
ATOM   423  C C   . GLY A 1 58  ? 135.307 155.373 215.240 1.00 116.97 ? 57  GLY A C   1 
ATOM   424  O O   . GLY A 1 58  ? 135.060 154.741 216.274 1.00 116.97 ? 57  GLY A O   1 
ATOM   425  N N   . ILE A 1 59  ? 135.527 154.778 214.073 1.00 119.00 ? 58  ILE A N   1 
ATOM   426  C CA  . ILE A 1 59  ? 135.444 153.336 213.885 1.00 119.00 ? 58  ILE A CA  1 
ATOM   427  C C   . ILE A 1 59  ? 136.792 152.853 213.370 1.00 119.00 ? 58  ILE A C   1 
ATOM   428  O O   . ILE A 1 59  ? 137.325 153.435 212.424 1.00 119.00 ? 58  ILE A O   1 
ATOM   429  C CB  . ILE A 1 59  ? 134.323 152.939 212.908 1.00 119.00 ? 58  ILE A CB  1 
ATOM   430  C CG1 . ILE A 1 59  ? 132.962 153.274 213.511 1.00 119.00 ? 58  ILE A CG1 1 
ATOM   431  C CG2 . ILE A 1 59  ? 134.399 151.467 212.573 1.00 119.00 ? 58  ILE A CG2 1 
ATOM   432  C CD1 . ILE A 1 59  ? 132.574 152.373 214.654 1.00 119.00 ? 58  ILE A CD1 1 
ATOM   433  N N   . PRO A 1 60  ? 137.378 151.811 213.955 1.00 124.18 ? 59  PRO A N   1 
ATOM   434  C CA  . PRO A 1 60  ? 138.665 151.307 213.462 1.00 124.18 ? 59  PRO A CA  1 
ATOM   435  C C   . PRO A 1 60  ? 138.533 150.707 212.071 1.00 124.18 ? 59  PRO A C   1 
ATOM   436  O O   . PRO A 1 60  ? 137.444 150.561 211.516 1.00 124.18 ? 59  PRO A O   1 
ATOM   437  C CB  . PRO A 1 60  ? 139.054 150.243 214.493 1.00 124.18 ? 59  PRO A CB  1 
ATOM   438  C CG  . PRO A 1 60  ? 138.222 150.548 215.699 1.00 124.18 ? 59  PRO A CG  1 
ATOM   439  C CD  . PRO A 1 60  ? 136.944 151.112 215.174 1.00 124.18 ? 59  PRO A CD  1 
ATOM   440  N N   . ASP A 1 61  ? 139.684 150.351 211.506 1.00 131.89 ? 60  ASP A N   1 
ATOM   441  C CA  . ASP A 1 61  ? 139.753 149.844 210.142 1.00 131.89 ? 60  ASP A CA  1 
ATOM   442  C C   . ASP A 1 61  ? 139.534 148.340 210.036 1.00 131.89 ? 60  ASP A C   1 
ATOM   443  O O   . ASP A 1 61  ? 139.556 147.809 208.920 1.00 131.89 ? 60  ASP A O   1 
ATOM   444  C CB  . ASP A 1 61  ? 141.102 150.217 209.519 1.00 131.89 ? 60  ASP A CB  1 
ATOM   445  C CG  . ASP A 1 61  ? 142.279 149.590 210.247 1.00 131.89 ? 60  ASP A CG  1 
ATOM   446  O OD1 . ASP A 1 61  ? 142.068 148.896 211.265 1.00 131.89 ? 60  ASP A OD1 1 
ATOM   447  O OD2 . ASP A 1 61  ? 143.425 149.794 209.797 1.00 131.89 ? 60  ASP A OD2 1 
ATOM   448  N N   . ARG A 1 62  ? 139.336 147.642 211.156 1.00 131.44 ? 61  ARG A N   1 
ATOM   449  C CA  . ARG A 1 62  ? 139.116 146.200 211.095 1.00 131.44 ? 61  ARG A CA  1 
ATOM   450  C C   . ARG A 1 62  ? 137.849 145.869 210.320 1.00 131.44 ? 61  ARG A C   1 
ATOM   451  O O   . ARG A 1 62  ? 137.836 144.947 209.498 1.00 131.44 ? 61  ARG A O   1 
ATOM   452  C CB  . ARG A 1 62  ? 139.035 145.621 212.504 1.00 131.44 ? 61  ARG A CB  1 
ATOM   453  C CG  . ARG A 1 62  ? 139.913 146.321 213.515 1.00 131.44 ? 61  ARG A CG  1 
ATOM   454  C CD  . ARG A 1 62  ? 140.338 145.356 214.599 1.00 131.44 ? 61  ARG A CD  1 
ATOM   455  N NE  . ARG A 1 62  ? 139.217 144.961 215.442 1.00 131.44 ? 61  ARG A NE  1 
ATOM   456  C CZ  . ARG A 1 62  ? 138.745 145.687 216.445 1.00 131.44 ? 61  ARG A CZ  1 
ATOM   457  N NH1 . ARG A 1 62  ? 139.281 146.853 216.765 1.00 131.44 ? 61  ARG A NH1 1 
ATOM   458  N NH2 . ARG A 1 62  ? 137.713 145.230 217.147 1.00 131.44 ? 61  ARG A NH2 1 
ATOM   459  N N   . PHE A 1 63  ? 136.778 146.613 210.571 1.00 118.67 ? 62  PHE A N   1 
ATOM   460  C CA  . PHE A 1 63  ? 135.501 146.349 209.925 1.00 118.67 ? 62  PHE A CA  1 
ATOM   461  C C   . PHE A 1 63  ? 135.570 146.722 208.451 1.00 118.67 ? 62  PHE A C   1 
ATOM   462  O O   . PHE A 1 63  ? 136.058 147.798 208.097 1.00 118.67 ? 62  PHE A O   1 
ATOM   463  C CB  . PHE A 1 63  ? 134.399 147.146 210.617 1.00 118.67 ? 62  PHE A CB  1 
ATOM   464  C CG  . PHE A 1 63  ? 134.488 147.133 212.117 1.00 118.67 ? 62  PHE A CG  1 
ATOM   465  C CD1 . PHE A 1 63  ? 133.840 146.164 212.852 1.00 118.67 ? 62  PHE A CD1 1 
ATOM   466  C CD2 . PHE A 1 63  ? 135.227 148.087 212.789 1.00 118.67 ? 62  PHE A CD2 1 
ATOM   467  C CE1 . PHE A 1 63  ? 133.921 146.145 214.227 1.00 118.67 ? 62  PHE A CE1 1 
ATOM   468  C CE2 . PHE A 1 63  ? 135.312 148.073 214.165 1.00 118.67 ? 62  PHE A CE2 1 
ATOM   469  C CZ  . PHE A 1 63  ? 134.657 147.100 214.884 1.00 118.67 ? 62  PHE A CZ  1 
ATOM   470  N N   . SER A 1 64  ? 135.083 145.834 207.588 1.00 119.14 ? 63  SER A N   1 
ATOM   471  C CA  . SER A 1 64  ? 134.981 146.150 206.170 1.00 119.14 ? 63  SER A CA  1 
ATOM   472  C C   . SER A 1 64  ? 133.657 145.634 205.637 1.00 119.14 ? 63  SER A C   1 
ATOM   473  O O   . SER A 1 64  ? 133.166 144.596 206.081 1.00 119.14 ? 63  SER A O   1 
ATOM   474  C CB  . SER A 1 64  ? 136.135 145.546 205.367 1.00 119.14 ? 63  SER A CB  1 
ATOM   475  O OG  . SER A 1 64  ? 135.957 144.154 205.195 1.00 119.14 ? 63  SER A OG  1 
ATOM   476  N N   . GLY A 1 65  ? 133.081 146.357 204.686 1.00 113.56 ? 64  GLY A N   1 
ATOM   477  C CA  . GLY A 1 65  ? 131.807 145.987 204.105 1.00 113.56 ? 64  GLY A CA  1 
ATOM   478  C C   . GLY A 1 65  ? 131.923 145.802 202.606 1.00 113.56 ? 64  GLY A C   1 
ATOM   479  O O   . GLY A 1 65  ? 132.732 146.455 201.947 1.00 113.56 ? 64  GLY A O   1 
ATOM   480  N N   . SER A 1 66  ? 131.105 144.902 202.070 1.00 120.49 ? 65  SER A N   1 
ATOM   481  C CA  . SER A 1 66  ? 131.076 144.693 200.629 1.00 120.49 ? 65  SER A CA  1 
ATOM   482  C C   . SER A 1 66  ? 129.733 144.098 200.247 1.00 120.49 ? 65  SER A C   1 
ATOM   483  O O   . SER A 1 66  ? 128.925 143.733 201.101 1.00 120.49 ? 65  SER A O   1 
ATOM   484  C CB  . SER A 1 66  ? 132.219 143.788 200.168 1.00 120.49 ? 65  SER A CB  1 
ATOM   485  O OG  . SER A 1 66  ? 132.134 143.549 198.774 1.00 120.49 ? 65  SER A OG  1 
ATOM   486  N N   . GLY A 1 67  ? 129.509 143.997 198.948 1.00 124.09 ? 66  GLY A N   1 
ATOM   487  C CA  . GLY A 1 67  ? 128.287 143.431 198.417 1.00 124.09 ? 66  GLY A CA  1 
ATOM   488  C C   . GLY A 1 67  ? 127.494 144.446 197.613 1.00 124.09 ? 66  GLY A C   1 
ATOM   489  O O   . GLY A 1 67  ? 127.743 145.651 197.640 1.00 124.09 ? 66  GLY A O   1 
ATOM   490  N N   . SER A 1 68  ? 126.508 143.917 196.894 1.00 128.02 ? 67  SER A N   1 
ATOM   491  C CA  . SER A 1 68  ? 125.686 144.718 195.998 1.00 128.02 ? 67  SER A CA  1 
ATOM   492  C C   . SER A 1 68  ? 124.599 143.830 195.420 1.00 128.02 ? 67  SER A C   1 
ATOM   493  O O   . SER A 1 68  ? 124.762 142.609 195.339 1.00 128.02 ? 67  SER A O   1 
ATOM   494  C CB  . SER A 1 68  ? 126.516 145.337 194.868 1.00 128.02 ? 67  SER A CB  1 
ATOM   495  O OG  . SER A 1 68  ? 127.235 144.338 194.168 1.00 128.02 ? 67  SER A OG  1 
ATOM   496  N N   . GLY A 1 69  ? 123.491 144.450 195.027 1.00 127.52 ? 68  GLY A N   1 
ATOM   497  C CA  . GLY A 1 69  ? 122.433 143.714 194.366 1.00 127.52 ? 68  GLY A CA  1 
ATOM   498  C C   . GLY A 1 69  ? 121.475 143.058 195.335 1.00 127.52 ? 68  GLY A C   1 
ATOM   499  O O   . GLY A 1 69  ? 120.541 143.695 195.828 1.00 127.52 ? 68  GLY A O   1 
ATOM   500  N N   . THR A 1 70  ? 121.690 141.771 195.600 1.00 132.06 ? 69  THR A N   1 
ATOM   501  C CA  . THR A 1 70  ? 120.858 141.018 196.523 1.00 132.06 ? 69  THR A CA  1 
ATOM   502  C C   . THR A 1 70  ? 121.644 140.357 197.647 1.00 132.06 ? 69  THR A C   1 
ATOM   503  O O   . THR A 1 70  ? 121.043 139.664 198.475 1.00 132.06 ? 69  THR A O   1 
ATOM   504  C CB  . THR A 1 70  ? 120.059 139.951 195.765 1.00 132.06 ? 69  THR A CB  1 
ATOM   505  O OG1 . THR A 1 70  ? 120.952 139.155 194.979 1.00 132.06 ? 69  THR A OG1 1 
ATOM   506  C CG2 . THR A 1 70  ? 119.041 140.607 194.850 1.00 132.06 ? 69  THR A CG2 1 
ATOM   507  N N   . ASP A 1 71  ? 122.961 140.542 197.703 1.00 129.44 ? 70  ASP A N   1 
ATOM   508  C CA  . ASP A 1 71  ? 123.783 139.977 198.761 1.00 129.44 ? 70  ASP A CA  1 
ATOM   509  C C   . ASP A 1 71  ? 124.746 141.026 199.303 1.00 129.44 ? 70  ASP A C   1 
ATOM   510  O O   . ASP A 1 71  ? 125.133 141.962 198.595 1.00 129.44 ? 70  ASP A O   1 
ATOM   511  C CB  . ASP A 1 71  ? 124.545 138.737 198.269 1.00 129.44 ? 70  ASP A CB  1 
ATOM   512  C CG  . ASP A 1 71  ? 125.518 139.044 197.144 1.00 129.44 ? 70  ASP A CG  1 
ATOM   513  O OD1 . ASP A 1 71  ? 126.217 138.110 196.704 1.00 129.44 ? 70  ASP A OD1 1 
ATOM   514  O OD2 . ASP A 1 71  ? 125.564 140.195 196.666 1.00 129.44 ? 70  ASP A OD2 1 
ATOM   515  N N   . PHE A 1 72  ? 125.097 140.882 200.582 1.00 121.79 ? 71  PHE A N   1 
ATOM   516  C CA  . PHE A 1 72  ? 126.024 141.794 201.237 1.00 121.79 ? 71  PHE A CA  1 
ATOM   517  C C   . PHE A 1 72  ? 126.769 141.036 202.324 1.00 121.79 ? 71  PHE A C   1 
ATOM   518  O O   . PHE A 1 72  ? 126.276 140.034 202.847 1.00 121.79 ? 71  PHE A O   1 
ATOM   519  C CB  . PHE A 1 72  ? 125.301 143.003 201.838 1.00 121.79 ? 71  PHE A CB  1 
ATOM   520  C CG  . PHE A 1 72  ? 124.494 143.777 200.843 1.00 121.79 ? 71  PHE A CG  1 
ATOM   521  C CD1 . PHE A 1 72  ? 125.087 144.745 200.056 1.00 121.79 ? 71  PHE A CD1 1 
ATOM   522  C CD2 . PHE A 1 72  ? 123.145 143.521 200.678 1.00 121.79 ? 71  PHE A CD2 1 
ATOM   523  C CE1 . PHE A 1 72  ? 124.348 145.450 199.134 1.00 121.79 ? 71  PHE A CE1 1 
ATOM   524  C CE2 . PHE A 1 72  ? 122.404 144.220 199.754 1.00 121.79 ? 71  PHE A CE2 1 
ATOM   525  C CZ  . PHE A 1 72  ? 123.007 145.186 198.981 1.00 121.79 ? 71  PHE A CZ  1 
ATOM   526  N N   . THR A 1 73  ? 127.952 141.533 202.676 1.00 121.33 ? 72  THR A N   1 
ATOM   527  C CA  . THR A 1 73  ? 128.811 140.844 203.625 1.00 121.33 ? 72  THR A CA  1 
ATOM   528  C C   . THR A 1 73  ? 129.626 141.838 204.439 1.00 121.33 ? 72  THR A C   1 
ATOM   529  O O   . THR A 1 73  ? 130.008 142.906 203.948 1.00 121.33 ? 72  THR A O   1 
ATOM   530  C CB  . THR A 1 73  ? 129.747 139.865 202.912 1.00 121.33 ? 72  THR A CB  1 
ATOM   531  O OG1 . THR A 1 73  ? 130.548 139.178 203.879 1.00 121.33 ? 72  THR A OG1 1 
ATOM   532  C CG2 . THR A 1 73  ? 130.647 140.597 201.933 1.00 121.33 ? 72  THR A CG2 1 
ATOM   533  N N   . LEU A 1 74  ? 129.883 141.467 205.691 1.00 119.62 ? 73  LEU A N   1 
ATOM   534  C CA  . LEU A 1 74  ? 130.688 142.245 206.620 1.00 119.62 ? 73  LEU A CA  1 
ATOM   535  C C   . LEU A 1 74  ? 131.836 141.372 207.103 1.00 119.62 ? 73  LEU A C   1 
ATOM   536  O O   . LEU A 1 74  ? 131.639 140.188 207.392 1.00 119.62 ? 73  LEU A O   1 
ATOM   537  C CB  . LEU A 1 74  ? 129.847 142.726 207.803 1.00 119.62 ? 73  LEU A CB  1 
ATOM   538  C CG  . LEU A 1 74  ? 130.584 143.324 209.000 1.00 119.62 ? 73  LEU A CG  1 
ATOM   539  C CD1 . LEU A 1 74  ? 131.252 144.620 208.612 1.00 119.62 ? 73  LEU A CD1 1 
ATOM   540  C CD2 . LEU A 1 74  ? 129.637 143.546 210.165 1.00 119.62 ? 73  LEU A CD2 1 
ATOM   541  N N   . THR A 1 75  ? 133.029 141.949 207.185 1.00 128.76 ? 74  THR A N   1 
ATOM   542  C CA  . THR A 1 75  ? 134.231 141.196 207.503 1.00 128.76 ? 74  THR A CA  1 
ATOM   543  C C   . THR A 1 75  ? 134.973 141.856 208.655 1.00 128.76 ? 74  THR A C   1 
ATOM   544  O O   . THR A 1 75  ? 135.149 143.080 208.677 1.00 128.76 ? 74  THR A O   1 
ATOM   545  C CB  . THR A 1 75  ? 135.142 141.091 206.280 1.00 128.76 ? 74  THR A CB  1 
ATOM   546  O OG1 . THR A 1 75  ? 134.437 140.435 205.220 1.00 128.76 ? 74  THR A OG1 1 
ATOM   547  C CG2 . THR A 1 75  ? 136.388 140.293 206.610 1.00 128.76 ? 74  THR A CG2 1 
ATOM   548  N N   . ILE A 1 76  ? 135.407 141.031 209.605 1.00 138.62 ? 75  ILE A N   1 
ATOM   549  C CA  . ILE A 1 76  ? 136.144 141.467 210.785 1.00 138.62 ? 75  ILE A CA  1 
ATOM   550  C C   . ILE A 1 76  ? 137.558 140.920 210.665 1.00 138.62 ? 75  ILE A C   1 
ATOM   551  O O   . ILE A 1 76  ? 137.757 139.698 210.648 1.00 138.62 ? 75  ILE A O   1 
ATOM   552  C CB  . ILE A 1 76  ? 135.484 140.970 212.078 1.00 138.62 ? 75  ILE A CB  1 
ATOM   553  C CG1 . ILE A 1 76  ? 134.040 141.449 212.151 1.00 138.62 ? 75  ILE A CG1 1 
ATOM   554  C CG2 . ILE A 1 76  ? 136.255 141.468 213.283 1.00 138.62 ? 75  ILE A CG2 1 
ATOM   555  C CD1 . ILE A 1 76  ? 133.905 142.923 212.158 1.00 138.62 ? 75  ILE A CD1 1 
ATOM   556  N N   . SER A 1 77  ? 138.541 141.819 210.595 1.00 145.91 ? 76  SER A N   1 
ATOM   557  C CA  . SER A 1 77  ? 139.911 141.396 210.320 1.00 145.91 ? 76  SER A CA  1 
ATOM   558  C C   . SER A 1 77  ? 140.536 140.697 211.522 1.00 145.91 ? 76  SER A C   1 
ATOM   559  O O   . SER A 1 77  ? 141.189 139.657 211.377 1.00 145.91 ? 76  SER A O   1 
ATOM   560  C CB  . SER A 1 77  ? 140.756 142.600 209.911 1.00 145.91 ? 76  SER A CB  1 
ATOM   561  O OG  . SER A 1 77  ? 140.918 143.490 211.001 1.00 145.91 ? 76  SER A OG  1 
ATOM   562  N N   . ARG A 1 78  ? 140.359 141.255 212.715 1.00 150.94 ? 77  ARG A N   1 
ATOM   563  C CA  . ARG A 1 78  ? 141.038 140.751 213.903 1.00 150.94 ? 77  ARG A CA  1 
ATOM   564  C C   . ARG A 1 78  ? 140.116 140.978 215.088 1.00 150.94 ? 77  ARG A C   1 
ATOM   565  O O   . ARG A 1 78  ? 139.902 142.123 215.496 1.00 150.94 ? 77  ARG A O   1 
ATOM   566  C CB  . ARG A 1 78  ? 142.393 141.458 214.078 1.00 150.94 ? 77  ARG A CB  1 
ATOM   567  C CG  . ARG A 1 78  ? 143.314 140.994 215.219 1.00 150.94 ? 77  ARG A CG  1 
ATOM   568  C CD  . ARG A 1 78  ? 142.832 141.324 216.628 1.00 150.94 ? 77  ARG A CD  1 
ATOM   569  N NE  . ARG A 1 78  ? 142.432 142.717 216.806 1.00 150.94 ? 77  ARG A NE  1 
ATOM   570  C CZ  . ARG A 1 78  ? 143.220 143.770 216.623 1.00 150.94 ? 77  ARG A CZ  1 
ATOM   571  N NH1 . ARG A 1 78  ? 144.490 143.636 216.277 1.00 150.94 ? 77  ARG A NH1 1 
ATOM   572  N NH2 . ARG A 1 78  ? 142.725 144.989 216.812 1.00 150.94 ? 77  ARG A NH2 1 
ATOM   573  N N   . LEU A 1 79  ? 139.586 139.894 215.645 1.00 152.77 ? 78  LEU A N   1 
ATOM   574  C CA  . LEU A 1 79  ? 138.614 140.009 216.720 1.00 152.77 ? 78  LEU A CA  1 
ATOM   575  C C   . LEU A 1 79  ? 139.276 140.417 218.028 1.00 152.77 ? 78  LEU A C   1 
ATOM   576  O O   . LEU A 1 79  ? 140.472 140.212 218.244 1.00 152.77 ? 78  LEU A O   1 
ATOM   577  C CB  . LEU A 1 79  ? 137.850 138.699 216.918 1.00 152.77 ? 78  LEU A CB  1 
ATOM   578  C CG  . LEU A 1 79  ? 136.726 138.360 215.935 1.00 152.77 ? 78  LEU A CG  1 
ATOM   579  C CD1 . LEU A 1 79  ? 137.243 137.985 214.564 1.00 152.77 ? 78  LEU A CD1 1 
ATOM   580  C CD2 . LEU A 1 79  ? 135.858 137.246 216.503 1.00 152.77 ? 78  LEU A CD2 1 
ATOM   581  N N   . GLU A 1 80  ? 138.469 140.995 218.907 1.00 155.48 ? 79  GLU A N   1 
ATOM   582  C CA  . GLU A 1 80  ? 138.872 141.510 220.201 1.00 155.48 ? 79  GLU A CA  1 
ATOM   583  C C   . GLU A 1 80  ? 137.930 140.928 221.245 1.00 155.48 ? 79  GLU A C   1 
ATOM   584  O O   . GLU A 1 80  ? 136.763 140.663 220.943 1.00 155.48 ? 79  GLU A O   1 
ATOM   585  C CB  . GLU A 1 80  ? 138.791 143.047 220.195 1.00 155.48 ? 79  GLU A CB  1 
ATOM   586  C CG  . GLU A 1 80  ? 139.228 143.775 221.450 1.00 155.48 ? 79  GLU A CG  1 
ATOM   587  C CD  . GLU A 1 80  ? 140.706 143.604 221.736 1.00 155.48 ? 79  GLU A CD  1 
ATOM   588  O OE1 . GLU A 1 80  ? 141.469 143.365 220.779 1.00 155.48 ? 79  GLU A OE1 1 
ATOM   589  O OE2 . GLU A 1 80  ? 141.101 143.708 222.915 1.00 155.48 ? 79  GLU A OE2 1 
ATOM   590  N N   . PRO A 1 81  ? 138.402 140.705 222.473 1.00 156.43 ? 80  PRO A N   1 
ATOM   591  C CA  . PRO A 1 81  ? 137.517 140.120 223.494 1.00 156.43 ? 80  PRO A CA  1 
ATOM   592  C C   . PRO A 1 81  ? 136.292 140.958 223.819 1.00 156.43 ? 80  PRO A C   1 
ATOM   593  O O   . PRO A 1 81  ? 135.349 140.432 224.422 1.00 156.43 ? 80  PRO A O   1 
ATOM   594  C CB  . PRO A 1 81  ? 138.439 139.972 224.711 1.00 156.43 ? 80  PRO A CB  1 
ATOM   595  C CG  . PRO A 1 81  ? 139.792 139.839 224.127 1.00 156.43 ? 80  PRO A CG  1 
ATOM   596  C CD  . PRO A 1 81  ? 139.809 140.697 222.905 1.00 156.43 ? 80  PRO A CD  1 
ATOM   597  N N   . GLU A 1 82  ? 136.265 142.235 223.449 1.00 153.98 ? 81  GLU A N   1 
ATOM   598  C CA  . GLU A 1 82  ? 135.100 143.067 223.717 1.00 153.98 ? 81  GLU A CA  1 
ATOM   599  C C   . GLU A 1 82  ? 134.029 142.967 222.636 1.00 153.98 ? 81  GLU A C   1 
ATOM   600  O O   . GLU A 1 82  ? 132.966 143.576 222.788 1.00 153.98 ? 81  GLU A O   1 
ATOM   601  C CB  . GLU A 1 82  ? 135.553 144.520 223.940 1.00 153.98 ? 81  GLU A CB  1 
ATOM   602  C CG  . GLU A 1 82  ? 136.272 145.207 222.775 1.00 153.98 ? 81  GLU A CG  1 
ATOM   603  C CD  . GLU A 1 82  ? 135.371 145.661 221.642 1.00 153.98 ? 81  GLU A CD  1 
ATOM   604  O OE1 . GLU A 1 82  ? 135.910 146.052 220.586 1.00 153.98 ? 81  GLU A OE1 1 
ATOM   605  O OE2 . GLU A 1 82  ? 134.140 145.704 221.819 1.00 153.98 ? 81  GLU A OE2 1 
ATOM   606  N N   . ASP A 1 83  ? 134.253 142.180 221.582 1.00 151.60 ? 82  ASP A N   1 
ATOM   607  C CA  . ASP A 1 83  ? 133.301 142.043 220.483 1.00 151.60 ? 82  ASP A CA  1 
ATOM   608  C C   . ASP A 1 83  ? 132.146 141.092 220.798 1.00 151.60 ? 82  ASP A C   1 
ATOM   609  O O   . ASP A 1 83  ? 131.483 140.614 219.871 1.00 151.60 ? 82  ASP A O   1 
ATOM   610  C CB  . ASP A 1 83  ? 134.019 141.584 219.214 1.00 151.60 ? 82  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 83  ? 134.934 142.647 218.650 1.00 151.60 ? 82  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 83  ? 134.645 143.844 218.845 1.00 151.60 ? 82  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 83  ? 135.939 142.289 218.003 1.00 151.60 ? 82  ASP A OD2 1 
ATOM   614  N N   . PHE A 1 84  ? 131.896 140.808 222.072 1.00 154.04 ? 83  PHE A N   1 
ATOM   615  C CA  . PHE A 1 84  ? 130.712 140.066 222.499 1.00 154.04 ? 83  PHE A CA  1 
ATOM   616  C C   . PHE A 1 84  ? 129.483 140.935 222.277 1.00 154.04 ? 83  PHE A C   1 
ATOM   617  O O   . PHE A 1 84  ? 129.137 141.764 223.120 1.00 154.04 ? 83  PHE A O   1 
ATOM   618  C CB  . PHE A 1 84  ? 130.852 139.673 223.965 1.00 154.04 ? 83  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 84  ? 129.738 138.808 224.475 1.00 154.04 ? 83  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 84  ? 129.128 137.877 223.658 1.00 154.04 ? 83  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 84  ? 129.302 138.931 225.783 1.00 154.04 ? 83  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 84  ? 128.099 137.085 224.135 1.00 154.04 ? 83  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 84  ? 128.277 138.142 226.267 1.00 154.04 ? 83  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 84  ? 127.676 137.217 225.441 1.00 154.04 ? 83  PHE A CZ  1 
ATOM   625  N N   . ALA A 1 85  ? 128.808 140.754 221.145 1.00 136.76 ? 84  ALA A N   1 
ATOM   626  C CA  . ALA A 1 85  ? 127.732 141.670 220.785 1.00 136.76 ? 84  ALA A CA  1 
ATOM   627  C C   . ALA A 1 85  ? 126.788 140.991 219.799 1.00 136.76 ? 84  ALA A C   1 
ATOM   628  O O   . ALA A 1 85  ? 126.853 139.776 219.580 1.00 136.76 ? 84  ALA A O   1 
ATOM   629  C CB  . ALA A 1 85  ? 128.303 142.970 220.212 1.00 136.76 ? 84  ALA A CB  1 
ATOM   630  N N   . VAL A 1 86  ? 125.885 141.784 219.222 1.00 123.71 ? 85  VAL A N   1 
ATOM   631  C CA  . VAL A 1 86  ? 124.965 141.331 218.186 1.00 123.71 ? 85  VAL A CA  1 
ATOM   632  C C   . VAL A 1 86  ? 125.056 142.302 217.019 1.00 123.71 ? 85  VAL A C   1 
ATOM   633  O O   . VAL A 1 86  ? 125.213 143.510 217.218 1.00 123.71 ? 85  VAL A O   1 
ATOM   634  C CB  . VAL A 1 86  ? 123.516 141.235 218.708 1.00 123.71 ? 85  VAL A CB  1 
ATOM   635  C CG1 . VAL A 1 86  ? 122.615 140.599 217.667 1.00 123.71 ? 85  VAL A CG1 1 
ATOM   636  C CG2 . VAL A 1 86  ? 123.467 140.453 220.009 1.00 123.71 ? 85  VAL A CG2 1 
ATOM   637  N N   . TYR A 1 87  ? 124.971 141.780 215.801 1.00 116.89 ? 86  TYR A N   1 
ATOM   638  C CA  . TYR A 1 87  ? 125.162 142.578 214.596 1.00 116.89 ? 86  TYR A CA  1 
ATOM   639  C C   . TYR A 1 87  ? 123.936 142.454 213.704 1.00 116.89 ? 86  TYR A C   1 
ATOM   640  O O   . TYR A 1 87  ? 123.499 141.341 213.396 1.00 116.89 ? 86  TYR A O   1 
ATOM   641  C CB  . TYR A 1 87  ? 126.429 142.143 213.860 1.00 116.89 ? 86  TYR A CB  1 
ATOM   642  C CG  . TYR A 1 87  ? 127.679 142.362 214.678 1.00 116.89 ? 86  TYR A CG  1 
ATOM   643  C CD1 . TYR A 1 87  ? 128.008 141.509 215.719 1.00 116.89 ? 86  TYR A CD1 1 
ATOM   644  C CD2 . TYR A 1 87  ? 128.520 143.431 214.421 1.00 116.89 ? 86  TYR A CD2 1 
ATOM   645  C CE1 . TYR A 1 87  ? 129.138 141.711 216.477 1.00 116.89 ? 86  TYR A CE1 1 
ATOM   646  C CE2 . TYR A 1 87  ? 129.656 143.639 215.174 1.00 116.89 ? 86  TYR A CE2 1 
ATOM   647  C CZ  . TYR A 1 87  ? 129.960 142.775 216.200 1.00 116.89 ? 86  TYR A CZ  1 
ATOM   648  O OH  . TYR A 1 87  ? 131.090 142.974 216.956 1.00 116.89 ? 86  TYR A OH  1 
ATOM   649  N N   . TYR A 1 88  ? 123.389 143.593 213.290 1.00 115.83 ? 87  TYR A N   1 
ATOM   650  C CA  . TYR A 1 88  ? 122.155 143.642 212.523 1.00 115.83 ? 87  TYR A CA  1 
ATOM   651  C C   . TYR A 1 88  ? 122.433 144.074 211.081 1.00 115.83 ? 87  TYR A C   1 
ATOM   652  O O   . TYR A 1 88  ? 123.586 144.221 210.671 1.00 115.83 ? 87  TYR A O   1 
ATOM   653  C CB  . TYR A 1 88  ? 121.156 144.564 213.224 1.00 115.83 ? 87  TYR A CB  1 
ATOM   654  C CG  . TYR A 1 88  ? 120.675 144.034 214.549 1.00 115.83 ? 87  TYR A CG  1 
ATOM   655  C CD1 . TYR A 1 88  ? 121.404 144.246 215.707 1.00 115.83 ? 87  TYR A CD1 1 
ATOM   656  C CD2 . TYR A 1 88  ? 119.498 143.311 214.641 1.00 115.83 ? 87  TYR A CD2 1 
ATOM   657  C CE1 . TYR A 1 88  ? 120.970 143.762 216.920 1.00 115.83 ? 87  TYR A CE1 1 
ATOM   658  C CE2 . TYR A 1 88  ? 119.057 142.822 215.850 1.00 115.83 ? 87  TYR A CE2 1 
ATOM   659  C CZ  . TYR A 1 88  ? 119.798 143.050 216.986 1.00 115.83 ? 87  TYR A CZ  1 
ATOM   660  O OH  . TYR A 1 88  ? 119.364 142.565 218.196 1.00 115.83 ? 87  TYR A OH  1 
ATOM   661  N N   . CYS A 1 89  ? 121.372 144.280 210.309 1.00 113.53 ? 88  CYS A N   1 
ATOM   662  C CA  . CYS A 1 89  ? 121.465 144.576 208.888 1.00 113.53 ? 88  CYS A CA  1 
ATOM   663  C C   . CYS A 1 89  ? 120.206 145.331 208.495 1.00 113.53 ? 88  CYS A C   1 
ATOM   664  O O   . CYS A 1 89  ? 119.109 144.774 208.559 1.00 113.53 ? 88  CYS A O   1 
ATOM   665  C CB  . CYS A 1 89  ? 121.608 143.279 208.076 1.00 113.53 ? 88  CYS A CB  1 
ATOM   666  S SG  . CYS A 1 89  ? 121.731 143.439 206.274 1.00 113.53 ? 88  CYS A SG  1 
ATOM   667  N N   . GLN A 1 90  ? 120.359 146.592 208.093 1.00 106.97 ? 89  GLN A N   1 
ATOM   668  C CA  . GLN A 1 90  ? 119.207 147.450 207.852 1.00 106.97 ? 89  GLN A CA  1 
ATOM   669  C C   . GLN A 1 90  ? 119.238 147.967 206.424 1.00 106.97 ? 89  GLN A C   1 
ATOM   670  O O   . GLN A 1 90  ? 120.310 148.185 205.855 1.00 106.97 ? 89  GLN A O   1 
ATOM   671  C CB  . GLN A 1 90  ? 119.177 148.631 208.828 1.00 106.97 ? 89  GLN A CB  1 
ATOM   672  C CG  . GLN A 1 90  ? 117.925 149.484 208.754 1.00 106.97 ? 89  GLN A CG  1 
ATOM   673  C CD  . GLN A 1 90  ? 118.057 150.626 207.768 1.00 106.97 ? 89  GLN A CD  1 
ATOM   674  O OE1 . GLN A 1 90  ? 119.122 150.849 207.199 1.00 106.97 ? 89  GLN A OE1 1 
ATOM   675  N NE2 . GLN A 1 90  ? 116.972 151.356 207.560 1.00 106.97 ? 89  GLN A NE2 1 
ATOM   676  N N   . GLN A 1 91  ? 118.054 148.176 205.849 1.00 108.67 ? 90  GLN A N   1 
ATOM   677  C CA  . GLN A 1 91  ? 117.953 148.714 204.501 1.00 108.67 ? 90  GLN A CA  1 
ATOM   678  C C   . GLN A 1 91  ? 116.963 149.869 204.469 1.00 108.67 ? 90  GLN A C   1 
ATOM   679  O O   . GLN A 1 91  ? 116.180 150.071 205.397 1.00 108.67 ? 90  GLN A O   1 
ATOM   680  C CB  . GLN A 1 91  ? 117.528 147.643 203.494 1.00 108.67 ? 90  GLN A CB  1 
ATOM   681  C CG  . GLN A 1 91  ? 116.129 147.121 203.721 1.00 108.67 ? 90  GLN A CG  1 
ATOM   682  C CD  . GLN A 1 91  ? 115.089 147.875 202.928 1.00 108.67 ? 90  GLN A CD  1 
ATOM   683  O OE1 . GLN A 1 91  ? 115.407 148.536 201.943 1.00 108.67 ? 90  GLN A OE1 1 
ATOM   684  N NE2 . GLN A 1 91  ? 113.838 147.790 203.361 1.00 108.67 ? 90  GLN A NE2 1 
ATOM   685  N N   . TYR A 1 92  ? 117.013 150.631 203.378 1.00 108.15 ? 91  TYR A N   1 
ATOM   686  C CA  . TYR A 1 92  ? 116.078 151.720 203.140 1.00 108.15 ? 91  TYR A CA  1 
ATOM   687  C C   . TYR A 1 92  ? 115.804 151.827 201.649 1.00 108.15 ? 91  TYR A C   1 
ATOM   688  O O   . TYR A 1 92  ? 116.637 151.454 200.820 1.00 108.15 ? 91  TYR A O   1 
ATOM   689  C CB  . TYR A 1 92  ? 116.604 153.058 203.668 1.00 108.15 ? 91  TYR A CB  1 
ATOM   690  C CG  . TYR A 1 92  ? 115.666 154.219 203.430 1.00 108.15 ? 91  TYR A CG  1 
ATOM   691  C CD1 . TYR A 1 92  ? 114.582 154.441 204.260 1.00 108.15 ? 91  TYR A CD1 1 
ATOM   692  C CD2 . TYR A 1 92  ? 115.864 155.090 202.372 1.00 108.15 ? 91  TYR A CD2 1 
ATOM   693  C CE1 . TYR A 1 92  ? 113.724 155.497 204.046 1.00 108.15 ? 91  TYR A CE1 1 
ATOM   694  C CE2 . TYR A 1 92  ? 115.009 156.148 202.149 1.00 108.15 ? 91  TYR A CE2 1 
ATOM   695  C CZ  . TYR A 1 92  ? 113.942 156.347 202.989 1.00 108.15 ? 91  TYR A CZ  1 
ATOM   696  O OH  . TYR A 1 92  ? 113.088 157.401 202.773 1.00 108.15 ? 91  TYR A OH  1 
ATOM   697  N N   . GLY A 1 93  ? 114.630 152.353 201.318 1.00 115.18 ? 92  GLY A N   1 
ATOM   698  C CA  . GLY A 1 93  ? 114.204 152.468 199.939 1.00 115.18 ? 92  GLY A CA  1 
ATOM   699  C C   . GLY A 1 93  ? 112.698 152.570 199.843 1.00 115.18 ? 92  GLY A C   1 
ATOM   700  O O   . GLY A 1 93  ? 112.085 153.404 200.513 1.00 115.18 ? 92  GLY A O   1 
ATOM   701  N N   . SER A 1 94  ? 112.084 151.721 199.019 1.00 119.79 ? 93  SER A N   1 
ATOM   702  C CA  . SER A 1 94  ? 110.630 151.669 198.971 1.00 119.79 ? 93  SER A CA  1 
ATOM   703  C C   . SER A 1 94  ? 110.023 151.175 200.275 1.00 119.79 ? 93  SER A C   1 
ATOM   704  O O   . SER A 1 94  ? 108.810 151.312 200.464 1.00 119.79 ? 93  SER A O   1 
ATOM   705  C CB  . SER A 1 94  ? 110.178 150.779 197.816 1.00 119.79 ? 93  SER A CB  1 
ATOM   706  O OG  . SER A 1 94  ? 110.724 151.235 196.592 1.00 119.79 ? 93  SER A OG  1 
ATOM   707  N N   . SER A 1 95  ? 110.826 150.602 201.167 1.00 118.32 ? 94  SER A N   1 
ATOM   708  C CA  . SER A 1 95  ? 110.372 150.211 202.492 1.00 118.32 ? 94  SER A CA  1 
ATOM   709  C C   . SER A 1 95  ? 111.576 150.197 203.423 1.00 118.32 ? 94  SER A C   1 
ATOM   710  O O   . SER A 1 95  ? 112.724 150.107 202.984 1.00 118.32 ? 94  SER A O   1 
ATOM   711  C CB  . SER A 1 95  ? 109.672 148.852 202.457 1.00 118.32 ? 94  SER A CB  1 
ATOM   712  O OG  . SER A 1 95  ? 108.501 148.907 201.662 1.00 118.32 ? 94  SER A OG  1 
ATOM   713  N N   . LEU A 1 96  ? 111.305 150.280 204.722 1.00 112.49 ? 95  LEU A N   1 
ATOM   714  C CA  . LEU A 1 96  ? 112.349 150.329 205.741 1.00 112.49 ? 95  LEU A CA  1 
ATOM   715  C C   . LEU A 1 96  ? 112.265 149.054 206.566 1.00 112.49 ? 95  LEU A C   1 
ATOM   716  O O   . LEU A 1 96  ? 111.298 148.857 207.308 1.00 112.49 ? 95  LEU A O   1 
ATOM   717  C CB  . LEU A 1 96  ? 112.191 151.563 206.624 1.00 112.49 ? 95  LEU A CB  1 
ATOM   718  C CG  . LEU A 1 96  ? 113.405 152.011 207.431 1.00 112.49 ? 95  LEU A CG  1 
ATOM   719  C CD1 . LEU A 1 96  ? 113.381 153.515 207.599 1.00 112.49 ? 95  LEU A CD1 1 
ATOM   720  C CD2 . LEU A 1 96  ? 113.435 151.327 208.780 1.00 112.49 ? 95  LEU A CD2 1 
ATOM   721  N N   . THR A 1 97  ? 113.271 148.190 206.443 1.00 112.27 ? 96  THR A N   1 
ATOM   722  C CA  . THR A 1 97  ? 113.265 146.911 207.138 1.00 112.27 ? 96  THR A CA  1 
ATOM   723  C C   . THR A 1 97  ? 114.635 146.599 207.721 1.00 112.27 ? 96  THR A C   1 
ATOM   724  O O   . THR A 1 97  ? 115.672 146.877 207.106 1.00 112.27 ? 96  THR A O   1 
ATOM   725  C CB  . THR A 1 97  ? 112.837 145.764 206.216 1.00 112.27 ? 96  THR A CB  1 
ATOM   726  O OG1 . THR A 1 97  ? 113.751 145.667 205.119 1.00 112.27 ? 96  THR A OG1 1 
ATOM   727  C CG2 . THR A 1 97  ? 111.428 145.978 205.691 1.00 112.27 ? 96  THR A CG2 1 
ATOM   728  N N   . PHE A 1 98  ? 114.615 146.003 208.911 1.00 112.56 ? 97  PHE A N   1 
ATOM   729  C CA  . PHE A 1 98  ? 115.813 145.529 209.588 1.00 112.56 ? 97  PHE A CA  1 
ATOM   730  C C   . PHE A 1 98  ? 116.081 144.074 209.232 1.00 112.56 ? 97  PHE A C   1 
ATOM   731  O O   . PHE A 1 98  ? 115.474 143.534 208.303 1.00 112.56 ? 97  PHE A O   1 
ATOM   732  C CB  . PHE A 1 98  ? 115.666 145.678 211.100 1.00 112.56 ? 97  PHE A CB  1 
ATOM   733  C CG  . PHE A 1 98  ? 116.003 147.045 211.612 1.00 112.56 ? 97  PHE A CG  1 
ATOM   734  C CD1 . PHE A 1 98  ? 115.340 148.160 211.139 1.00 112.56 ? 97  PHE A CD1 1 
ATOM   735  C CD2 . PHE A 1 98  ? 116.983 147.214 212.569 1.00 112.56 ? 97  PHE A CD2 1 
ATOM   736  C CE1 . PHE A 1 98  ? 115.648 149.414 211.613 1.00 112.56 ? 97  PHE A CE1 1 
ATOM   737  C CE2 . PHE A 1 98  ? 117.294 148.465 213.045 1.00 112.56 ? 97  PHE A CE2 1 
ATOM   738  C CZ  . PHE A 1 98  ? 116.627 149.566 212.567 1.00 112.56 ? 97  PHE A CZ  1 
ATOM   739  N N   . GLY A 1 99  ? 116.989 143.434 209.962 1.00 118.25 ? 98  GLY A N   1 
ATOM   740  C CA  . GLY A 1 99  ? 117.285 142.032 209.744 1.00 118.25 ? 98  GLY A CA  1 
ATOM   741  C C   . GLY A 1 99  ? 117.335 141.286 211.055 1.00 118.25 ? 98  GLY A C   1 
ATOM   742  O O   . GLY A 1 99  ? 117.285 141.882 212.135 1.00 118.25 ? 98  GLY A O   1 
ATOM   743  N N   . GLY A 1 100 ? 117.425 139.959 210.950 1.00 124.36 ? 99  GLY A N   1 
ATOM   744  C CA  . GLY A 1 100 ? 117.450 139.134 212.147 1.00 124.36 ? 99  GLY A CA  1 
ATOM   745  C C   . GLY A 1 100 ? 118.678 139.370 213.005 1.00 124.36 ? 99  GLY A C   1 
ATOM   746  O O   . GLY A 1 100 ? 118.575 139.514 214.226 1.00 124.36 ? 99  GLY A O   1 
ATOM   747  N N   . GLY A 1 101 ? 119.854 139.408 212.385 1.00 126.54 ? 100 GLY A N   1 
ATOM   748  C CA  . GLY A 1 101 ? 121.075 139.671 213.119 1.00 126.54 ? 100 GLY A CA  1 
ATOM   749  C C   . GLY A 1 101 ? 121.749 138.432 213.671 1.00 126.54 ? 100 GLY A C   1 
ATOM   750  O O   . GLY A 1 101 ? 121.099 137.407 213.891 1.00 126.54 ? 100 GLY A O   1 
ATOM   751  N N   . THR A 1 102 ? 123.055 138.522 213.906 1.00 131.39 ? 101 THR A N   1 
ATOM   752  C CA  . THR A 1 102 ? 123.858 137.415 214.403 1.00 131.39 ? 101 THR A CA  1 
ATOM   753  C C   . THR A 1 102 ? 124.435 137.769 215.765 1.00 131.39 ? 101 THR A C   1 
ATOM   754  O O   . THR A 1 102 ? 124.918 138.887 215.965 1.00 131.39 ? 101 THR A O   1 
ATOM   755  C CB  . THR A 1 102 ? 124.993 137.089 213.434 1.00 131.39 ? 101 THR A CB  1 
ATOM   756  O OG1 . THR A 1 102 ? 124.451 136.580 212.211 1.00 131.39 ? 101 THR A OG1 1 
ATOM   757  C CG2 . THR A 1 102 ? 125.931 136.058 214.032 1.00 131.39 ? 101 THR A CG2 1 
ATOM   758  N N   . LYS A 1 103 ? 124.383 136.820 216.695 1.00 142.43 ? 102 LYS A N   1 
ATOM   759  C CA  . LYS A 1 103 ? 125.055 136.959 217.977 1.00 142.43 ? 102 LYS A CA  1 
ATOM   760  C C   . LYS A 1 103 ? 126.475 136.425 217.860 1.00 142.43 ? 102 LYS A C   1 
ATOM   761  O O   . LYS A 1 103 ? 126.687 135.288 217.430 1.00 142.43 ? 102 LYS A O   1 
ATOM   762  C CB  . LYS A 1 103 ? 124.293 136.208 219.073 1.00 142.43 ? 102 LYS A CB  1 
ATOM   763  C CG  . LYS A 1 103 ? 124.903 136.302 220.472 1.00 142.43 ? 102 LYS A CG  1 
ATOM   764  C CD  . LYS A 1 103 ? 125.840 135.137 220.787 1.00 142.43 ? 102 LYS A CD  1 
ATOM   765  C CE  . LYS A 1 103 ? 125.081 133.832 220.969 1.00 142.43 ? 102 LYS A CE  1 
ATOM   766  N NZ  . LYS A 1 103 ? 125.997 132.702 221.287 1.00 142.43 ? 102 LYS A NZ  1 
ATOM   767  N N   . LEU A 1 104 ? 127.449 137.250 218.234 1.00 149.29 ? 103 LEU A N   1 
ATOM   768  C CA  . LEU A 1 104 ? 128.851 136.860 218.195 1.00 149.29 ? 103 LEU A CA  1 
ATOM   769  C C   . LEU A 1 104 ? 129.415 136.940 219.605 1.00 149.29 ? 103 LEU A C   1 
ATOM   770  O O   . LEU A 1 104 ? 129.320 137.986 220.261 1.00 149.29 ? 103 LEU A O   1 
ATOM   771  C CB  . LEU A 1 104 ? 129.642 137.745 217.230 1.00 149.29 ? 103 LEU A CB  1 
ATOM   772  C CG  . LEU A 1 104 ? 131.083 137.347 216.903 1.00 149.29 ? 103 LEU A CG  1 
ATOM   773  C CD1 . LEU A 1 104 ? 131.434 137.817 215.504 1.00 149.29 ? 103 LEU A CD1 1 
ATOM   774  C CD2 . LEU A 1 104 ? 132.062 137.929 217.908 1.00 149.29 ? 103 LEU A CD2 1 
ATOM   775  N N   . GLU A 1 105 ? 130.005 135.838 220.060 1.00 157.94 ? 104 GLU A N   1 
ATOM   776  C CA  . GLU A 1 105 ? 130.580 135.724 221.392 1.00 157.94 ? 104 GLU A CA  1 
ATOM   777  C C   . GLU A 1 105 ? 132.023 135.263 221.270 1.00 157.94 ? 104 GLU A C   1 
ATOM   778  O O   . GLU A 1 105 ? 132.377 134.561 220.317 1.00 157.94 ? 104 GLU A O   1 
ATOM   779  C CB  . GLU A 1 105 ? 129.776 134.753 222.263 1.00 157.94 ? 104 GLU A CB  1 
ATOM   780  C CG  . GLU A 1 105 ? 129.902 133.278 221.900 1.00 157.94 ? 104 GLU A CG  1 
ATOM   781  C CD  . GLU A 1 105 ? 129.335 132.945 220.533 1.00 157.94 ? 104 GLU A CD  1 
ATOM   782  O OE1 . GLU A 1 105 ? 129.707 131.893 219.982 1.00 157.94 ? 104 GLU A OE1 1 
ATOM   783  O OE2 . GLU A 1 105 ? 128.524 133.734 220.006 1.00 157.94 ? 104 GLU A OE2 1 
ATOM   784  N N   . ILE A 1 106 ? 132.849 135.658 222.232 1.00 162.89 ? 105 ILE A N   1 
ATOM   785  C CA  . ILE A 1 106 ? 134.274 135.367 222.201 1.00 162.89 ? 105 ILE A CA  1 
ATOM   786  C C   . ILE A 1 106 ? 134.634 134.571 223.447 1.00 162.89 ? 105 ILE A C   1 
ATOM   787  O O   . ILE A 1 106 ? 133.945 134.634 224.471 1.00 162.89 ? 105 ILE A O   1 
ATOM   788  C CB  . ILE A 1 106 ? 135.111 136.661 222.108 1.00 162.89 ? 105 ILE A CB  1 
ATOM   789  C CG1 . ILE A 1 106 ? 136.564 136.343 221.758 1.00 162.89 ? 105 ILE A CG1 1 
ATOM   790  C CG2 . ILE A 1 106 ? 135.038 137.429 223.413 1.00 162.89 ? 105 ILE A CG2 1 
ATOM   791  C CD1 . ILE A 1 106 ? 136.732 135.755 220.380 1.00 162.89 ? 105 ILE A CD1 1 
ATOM   792  N N   . LYS A 1 107 ? 135.716 133.808 223.349 1.00 164.28 ? 106 LYS A N   1 
ATOM   793  C CA  . LYS A 1 107 ? 136.181 132.989 224.459 1.00 164.28 ? 106 LYS A CA  1 
ATOM   794  C C   . LYS A 1 107 ? 137.671 133.201 224.701 1.00 164.28 ? 106 LYS A C   1 
ATOM   795  O O   . LYS A 1 107 ? 138.452 133.308 223.755 1.00 164.28 ? 106 LYS A O   1 
ATOM   796  C CB  . LYS A 1 107 ? 135.896 131.516 224.183 1.00 164.28 ? 106 LYS A CB  1 
ATOM   797  C CG  . LYS A 1 107 ? 136.250 131.092 222.772 1.00 164.28 ? 106 LYS A CG  1 
ATOM   798  C CD  . LYS A 1 107 ? 136.357 129.587 222.662 1.00 164.28 ? 106 LYS A CD  1 
ATOM   799  C CE  . LYS A 1 107 ? 137.192 129.186 221.461 1.00 164.28 ? 106 LYS A CE  1 
ATOM   800  N NZ  . LYS A 1 107 ? 136.643 129.750 220.199 1.00 164.28 ? 106 LYS A NZ  1 
ATOM   801  N N   . SER A 1 122 ? 128.665 162.651 218.992 1.00 144.16 ? 121 SER A N   1 
ATOM   802  C CA  . SER A 1 122 ? 128.882 162.907 220.410 1.00 144.16 ? 121 SER A CA  1 
ATOM   803  C C   . SER A 1 122 ? 128.533 164.348 220.761 1.00 144.16 ? 121 SER A C   1 
ATOM   804  O O   . SER A 1 122 ? 128.413 164.701 221.933 1.00 144.16 ? 121 SER A O   1 
ATOM   805  C CB  . SER A 1 122 ? 130.332 162.611 220.793 1.00 144.16 ? 121 SER A CB  1 
ATOM   806  O OG  . SER A 1 122 ? 131.229 163.371 220.002 1.00 144.16 ? 121 SER A OG  1 
ATOM   807  N N   . GLN A 1 123 ? 128.378 165.182 219.733 1.00 144.89 ? 122 GLN A N   1 
ATOM   808  C CA  . GLN A 1 123 ? 128.062 166.586 219.951 1.00 144.89 ? 122 GLN A CA  1 
ATOM   809  C C   . GLN A 1 123 ? 126.564 166.850 219.996 1.00 144.89 ? 122 GLN A C   1 
ATOM   810  O O   . GLN A 1 123 ? 126.156 167.968 220.328 1.00 144.89 ? 122 GLN A O   1 
ATOM   811  C CB  . GLN A 1 123 ? 128.707 167.439 218.858 1.00 144.89 ? 122 GLN A CB  1 
ATOM   812  C CG  . GLN A 1 123 ? 130.097 166.971 218.447 1.00 144.89 ? 122 GLN A CG  1 
ATOM   813  C CD  . GLN A 1 123 ? 131.041 166.789 219.624 1.00 144.89 ? 122 GLN A CD  1 
ATOM   814  O OE1 . GLN A 1 123 ? 131.861 165.871 219.635 1.00 144.89 ? 122 GLN A OE1 1 
ATOM   815  N NE2 . GLN A 1 123 ? 130.949 167.678 220.607 1.00 144.89 ? 122 GLN A NE2 1 
ATOM   816  N N   . VAL A 1 124 ? 125.743 165.857 219.667 1.00 137.81 ? 123 VAL A N   1 
ATOM   817  C CA  . VAL A 1 124 ? 124.291 165.971 219.713 1.00 137.81 ? 123 VAL A CA  1 
ATOM   818  C C   . VAL A 1 124 ? 123.760 164.832 220.567 1.00 137.81 ? 123 VAL A C   1 
ATOM   819  O O   . VAL A 1 124 ? 124.149 163.675 220.375 1.00 137.81 ? 123 VAL A O   1 
ATOM   820  C CB  . VAL A 1 124 ? 123.673 165.936 218.304 1.00 137.81 ? 123 VAL A CB  1 
ATOM   821  C CG1 . VAL A 1 124 ? 122.163 166.021 218.388 1.00 137.81 ? 123 VAL A CG1 1 
ATOM   822  C CG2 . VAL A 1 124 ? 124.227 167.065 217.455 1.00 137.81 ? 123 VAL A CG2 1 
ATOM   823  N N   . GLN A 1 125 ? 122.881 165.156 221.511 1.00 137.57 ? 124 GLN A N   1 
ATOM   824  C CA  . GLN A 1 125 ? 122.370 164.177 222.459 1.00 137.57 ? 124 GLN A CA  1 
ATOM   825  C C   . GLN A 1 125 ? 120.849 164.143 222.435 1.00 137.57 ? 124 GLN A C   1 
ATOM   826  O O   . GLN A 1 125 ? 120.189 165.175 222.270 1.00 137.57 ? 124 GLN A O   1 
ATOM   827  C CB  . GLN A 1 125 ? 122.864 164.473 223.876 1.00 137.57 ? 124 GLN A CB  1 
ATOM   828  C CG  . GLN A 1 125 ? 124.310 164.082 224.114 1.00 137.57 ? 124 GLN A CG  1 
ATOM   829  C CD  . GLN A 1 125 ? 125.285 165.064 223.502 1.00 137.57 ? 124 GLN A CD  1 
ATOM   830  O OE1 . GLN A 1 125 ? 124.907 166.165 223.106 1.00 137.57 ? 124 GLN A OE1 1 
ATOM   831  N NE2 . GLN A 1 125 ? 126.549 164.668 223.420 1.00 137.57 ? 124 GLN A NE2 1 
ATOM   832  N N   . LEU A 1 126 ? 120.307 162.941 222.595 1.00 132.32 ? 125 LEU A N   1 
ATOM   833  C CA  . LEU A 1 126 ? 118.873 162.703 222.641 1.00 132.32 ? 125 LEU A CA  1 
ATOM   834  C C   . LEU A 1 126 ? 118.536 162.123 224.006 1.00 132.32 ? 125 LEU A C   1 
ATOM   835  O O   . LEU A 1 126 ? 119.174 161.161 224.444 1.00 132.32 ? 125 LEU A O   1 
ATOM   836  C CB  . LEU A 1 126 ? 118.443 161.733 221.538 1.00 132.32 ? 125 LEU A CB  1 
ATOM   837  C CG  . LEU A 1 126 ? 118.225 162.244 220.110 1.00 132.32 ? 125 LEU A CG  1 
ATOM   838  C CD1 . LEU A 1 126 ? 117.101 163.251 220.054 1.00 132.32 ? 125 LEU A CD1 1 
ATOM   839  C CD2 . LEU A 1 126 ? 119.494 162.822 219.512 1.00 132.32 ? 125 LEU A CD2 1 
ATOM   840  N N   . GLN A 1 127 ? 117.547 162.702 224.682 1.00 144.15 ? 126 GLN A N   1 
ATOM   841  C CA  . GLN A 1 127 ? 117.177 162.245 226.016 1.00 144.15 ? 126 GLN A CA  1 
ATOM   842  C C   . GLN A 1 127 ? 115.697 161.901 226.050 1.00 144.15 ? 126 GLN A C   1 
ATOM   843  O O   . GLN A 1 127 ? 114.863 162.702 225.623 1.00 144.15 ? 126 GLN A O   1 
ATOM   844  C CB  . GLN A 1 127 ? 117.498 163.303 227.073 1.00 144.15 ? 126 GLN A CB  1 
ATOM   845  C CG  . GLN A 1 127 ? 117.550 162.756 228.487 1.00 144.15 ? 126 GLN A CG  1 
ATOM   846  C CD  . GLN A 1 127 ? 116.174 162.600 229.094 1.00 144.15 ? 126 GLN A CD  1 
ATOM   847  O OE1 . GLN A 1 127 ? 115.236 163.299 228.716 1.00 144.15 ? 126 GLN A OE1 1 
ATOM   848  N NE2 . GLN A 1 127 ? 116.042 161.671 230.033 1.00 144.15 ? 126 GLN A NE2 1 
ATOM   849  N N   . GLN A 1 128 ? 115.368 160.730 226.584 1.00 141.38 ? 127 GLN A N   1 
ATOM   850  C CA  . GLN A 1 128 ? 113.998 160.239 226.577 1.00 141.38 ? 127 GLN A CA  1 
ATOM   851  C C   . GLN A 1 128 ? 113.328 160.432 227.931 1.00 141.38 ? 127 GLN A C   1 
ATOM   852  O O   . GLN A 1 128 ? 113.976 160.397 228.980 1.00 141.38 ? 127 GLN A O   1 
ATOM   853  C CB  . GLN A 1 128 ? 113.953 158.763 226.190 1.00 141.38 ? 127 GLN A CB  1 
ATOM   854  C CG  . GLN A 1 128 ? 114.565 158.480 224.843 1.00 141.38 ? 127 GLN A CG  1 
ATOM   855  C CD  . GLN A 1 128 ? 114.105 157.165 224.267 1.00 141.38 ? 127 GLN A CD  1 
ATOM   856  O OE1 . GLN A 1 128 ? 114.547 156.760 223.196 1.00 141.38 ? 127 GLN A OE1 1 
ATOM   857  N NE2 . GLN A 1 128 ? 113.212 156.488 224.977 1.00 141.38 ? 127 GLN A NE2 1 
ATOM   858  N N   . SER A 1 129 ? 112.012 160.635 227.892 1.00 152.06 ? 128 SER A N   1 
ATOM   859  C CA  . SER A 1 129 ? 111.220 160.778 229.103 1.00 152.06 ? 128 SER A CA  1 
ATOM   860  C C   . SER A 1 129 ? 109.819 160.241 228.851 1.00 152.06 ? 128 SER A C   1 
ATOM   861  O O   . SER A 1 129 ? 109.346 160.209 227.711 1.00 152.06 ? 128 SER A O   1 
ATOM   862  C CB  . SER A 1 129 ? 111.147 162.237 229.563 1.00 152.06 ? 128 SER A CB  1 
ATOM   863  O OG  . SER A 1 129 ? 110.596 163.058 228.548 1.00 152.06 ? 128 SER A OG  1 
ATOM   864  N N   . GLY A 1 130 ? 109.159 159.826 229.929 1.00 161.54 ? 129 GLY A N   1 
ATOM   865  C CA  . GLY A 1 130 ? 107.817 159.304 229.849 1.00 161.54 ? 129 GLY A CA  1 
ATOM   866  C C   . GLY A 1 130 ? 107.584 158.155 230.808 1.00 161.54 ? 129 GLY A C   1 
ATOM   867  O O   . GLY A 1 130 ? 108.525 157.555 231.337 1.00 161.54 ? 129 GLY A O   1 
ATOM   868  N N   . PRO A 1 131 ? 106.317 157.830 231.057 1.00 167.56 ? 130 PRO A N   1 
ATOM   869  C CA  . PRO A 1 131 ? 106.007 156.712 231.954 1.00 167.56 ? 130 PRO A CA  1 
ATOM   870  C C   . PRO A 1 131 ? 106.439 155.381 231.362 1.00 167.56 ? 130 PRO A C   1 
ATOM   871  O O   . PRO A 1 131 ? 106.427 155.179 230.145 1.00 167.56 ? 130 PRO A O   1 
ATOM   872  C CB  . PRO A 1 131 ? 104.483 156.786 232.097 1.00 167.56 ? 130 PRO A CB  1 
ATOM   873  C CG  . PRO A 1 131 ? 104.026 157.463 230.852 1.00 167.56 ? 130 PRO A CG  1 
ATOM   874  C CD  . PRO A 1 131 ? 105.104 158.444 230.492 1.00 167.56 ? 130 PRO A CD  1 
ATOM   875  N N   . GLY A 1 132 ? 106.821 154.462 232.245 1.00 170.06 ? 131 GLY A N   1 
ATOM   876  C CA  . GLY A 1 132 ? 107.266 153.149 231.821 1.00 170.06 ? 131 GLY A CA  1 
ATOM   877  C C   . GLY A 1 132 ? 106.234 152.058 232.019 1.00 170.06 ? 131 GLY A C   1 
ATOM   878  O O   . GLY A 1 132 ? 106.416 150.930 231.551 1.00 170.06 ? 131 GLY A O   1 
ATOM   879  N N   . LEU A 1 133 ? 105.145 152.381 232.712 1.00 173.44 ? 132 LEU A N   1 
ATOM   880  C CA  . LEU A 1 133 ? 104.069 151.436 232.980 1.00 173.44 ? 132 LEU A CA  1 
ATOM   881  C C   . LEU A 1 133 ? 102.739 152.104 232.676 1.00 173.44 ? 132 LEU A C   1 
ATOM   882  O O   . LEU A 1 133 ? 102.530 153.267 233.035 1.00 173.44 ? 132 LEU A O   1 
ATOM   883  C CB  . LEU A 1 133 ? 104.102 150.953 234.434 1.00 173.44 ? 132 LEU A CB  1 
ATOM   884  C CG  . LEU A 1 133 ? 102.961 150.036 234.880 1.00 173.44 ? 132 LEU A CG  1 
ATOM   885  C CD1 . LEU A 1 133 ? 102.902 148.788 234.016 1.00 173.44 ? 132 LEU A CD1 1 
ATOM   886  C CD2 . LEU A 1 133 ? 103.115 149.669 236.348 1.00 173.44 ? 132 LEU A CD2 1 
ATOM   887  N N   . VAL A 1 134 ? 101.844 151.371 232.015 1.00 176.63 ? 133 VAL A N   1 
ATOM   888  C CA  . VAL A 1 134 ? 100.547 151.904 231.620 1.00 176.63 ? 133 VAL A CA  1 
ATOM   889  C C   . VAL A 1 134 ? 99.488  150.820 231.776 1.00 176.63 ? 133 VAL A C   1 
ATOM   890  O O   . VAL A 1 134 ? 99.749  149.631 231.573 1.00 176.63 ? 133 VAL A O   1 
ATOM   891  C CB  . VAL A 1 134 ? 100.572 152.452 230.173 1.00 176.63 ? 133 VAL A CB  1 
ATOM   892  C CG1 . VAL A 1 134 ? 100.678 151.320 229.162 1.00 176.63 ? 133 VAL A CG1 1 
ATOM   893  C CG2 . VAL A 1 134 ? 99.348  153.312 229.902 1.00 176.63 ? 133 VAL A CG2 1 
ATOM   894  N N   . LYS A 1 135 ? 98.291  151.245 232.171 1.00 179.28 ? 134 LYS A N   1 
ATOM   895  C CA  . LYS A 1 135 ? 97.116  150.393 232.231 1.00 179.28 ? 134 LYS A CA  1 
ATOM   896  C C   . LYS A 1 135 ? 96.684  150.020 230.813 1.00 179.28 ? 134 LYS A C   1 
ATOM   897  O O   . LYS A 1 135 ? 96.642  150.878 229.928 1.00 179.28 ? 134 LYS A O   1 
ATOM   898  C CB  . LYS A 1 135 ? 95.982  151.127 232.951 1.00 179.28 ? 134 LYS A CB  1 
ATOM   899  C CG  . LYS A 1 135 ? 94.658  150.378 233.229 1.00 179.28 ? 134 LYS A CG  1 
ATOM   900  C CD  . LYS A 1 135 ? 94.743  148.932 233.743 1.00 179.28 ? 134 LYS A CD  1 
ATOM   901  C CE  . LYS A 1 135 ? 95.825  148.703 234.795 1.00 179.28 ? 134 LYS A CE  1 
ATOM   902  N NZ  . LYS A 1 135 ? 95.606  147.436 235.543 1.00 179.28 ? 134 LYS A NZ  1 
ATOM   903  N N   . PRO A 1 136 ? 96.383  148.744 230.564 1.00 177.73 ? 135 PRO A N   1 
ATOM   904  C CA  . PRO A 1 136 ? 95.931  148.348 229.225 1.00 177.73 ? 135 PRO A CA  1 
ATOM   905  C C   . PRO A 1 136 ? 94.701  149.125 228.783 1.00 177.73 ? 135 PRO A C   1 
ATOM   906  O O   . PRO A 1 136 ? 93.887  149.565 229.598 1.00 177.73 ? 135 PRO A O   1 
ATOM   907  C CB  . PRO A 1 136 ? 95.623  146.857 229.387 1.00 177.73 ? 135 PRO A CB  1 
ATOM   908  C CG  . PRO A 1 136 ? 96.570  146.412 230.441 1.00 177.73 ? 135 PRO A CG  1 
ATOM   909  C CD  . PRO A 1 136 ? 96.741  147.575 231.386 1.00 177.73 ? 135 PRO A CD  1 
ATOM   910  N N   . SER A 1 137 ? 94.592  149.306 227.464 1.00 173.77 ? 136 SER A N   1 
ATOM   911  C CA  . SER A 1 137 ? 93.525  150.094 226.846 1.00 173.77 ? 136 SER A CA  1 
ATOM   912  C C   . SER A 1 137 ? 93.573  151.552 227.301 1.00 173.77 ? 136 SER A C   1 
ATOM   913  O O   . SER A 1 137 ? 92.550  152.152 227.635 1.00 173.77 ? 136 SER A O   1 
ATOM   914  C CB  . SER A 1 137 ? 92.149  149.481 227.117 1.00 173.77 ? 136 SER A CB  1 
ATOM   915  O OG  . SER A 1 137 ? 92.082  148.153 226.630 1.00 173.77 ? 136 SER A OG  1 
ATOM   916  N N   . GLN A 1 138 ? 94.774  152.126 227.317 1.00 174.55 ? 137 GLN A N   1 
ATOM   917  C CA  . GLN A 1 138 ? 94.978  153.532 227.637 1.00 174.55 ? 137 GLN A CA  1 
ATOM   918  C C   . GLN A 1 138 ? 95.939  154.147 226.627 1.00 174.55 ? 137 GLN A C   1 
ATOM   919  O O   . GLN A 1 138 ? 96.296  153.533 225.617 1.00 174.55 ? 137 GLN A O   1 
ATOM   920  C CB  . GLN A 1 138 ? 95.506  153.715 229.065 1.00 174.55 ? 137 GLN A CB  1 
ATOM   921  C CG  . GLN A 1 138 ? 94.470  153.490 230.148 1.00 174.55 ? 137 GLN A CG  1 
ATOM   922  C CD  . GLN A 1 138 ? 94.928  154.001 231.499 1.00 174.55 ? 137 GLN A CD  1 
ATOM   923  O OE1 . GLN A 1 138 ? 96.110  154.278 231.702 1.00 174.55 ? 137 GLN A OE1 1 
ATOM   924  N NE2 . GLN A 1 138 ? 93.992  154.126 232.432 1.00 174.55 ? 137 GLN A NE2 1 
ATOM   925  N N   . THR A 1 139 ? 96.364  155.374 226.913 1.00 170.02 ? 138 THR A N   1 
ATOM   926  C CA  . THR A 1 139 ? 97.242  156.133 226.033 1.00 170.02 ? 138 THR A CA  1 
ATOM   927  C C   . THR A 1 139 ? 98.672  156.082 226.553 1.00 170.02 ? 138 THR A C   1 
ATOM   928  O O   . THR A 1 139 ? 98.909  156.233 227.756 1.00 170.02 ? 138 THR A O   1 
ATOM   929  C CB  . THR A 1 139 ? 96.784  157.588 225.927 1.00 170.02 ? 138 THR A CB  1 
ATOM   930  O OG1 . THR A 1 139 ? 96.861  158.208 227.216 1.00 170.02 ? 138 THR A OG1 1 
ATOM   931  C CG2 . THR A 1 139 ? 95.354  157.662 225.424 1.00 170.02 ? 138 THR A CG2 1 
ATOM   932  N N   . LEU A 1 140 ? 99.617  155.870 225.643 1.00 158.56 ? 139 LEU A N   1 
ATOM   933  C CA  . LEU A 1 140 ? 101.040 155.874 225.946 1.00 158.56 ? 139 LEU A CA  1 
ATOM   934  C C   . LEU A 1 140 ? 101.675 157.116 225.338 1.00 158.56 ? 139 LEU A C   1 
ATOM   935  O O   . LEU A 1 140 ? 101.459 157.410 224.159 1.00 158.56 ? 139 LEU A O   1 
ATOM   936  C CB  . LEU A 1 140 ? 101.715 154.618 225.397 1.00 158.56 ? 139 LEU A CB  1 
ATOM   937  C CG  . LEU A 1 140 ? 103.200 154.496 225.716 1.00 158.56 ? 139 LEU A CG  1 
ATOM   938  C CD1 . LEU A 1 140 ? 103.405 154.407 227.216 1.00 158.56 ? 139 LEU A CD1 1 
ATOM   939  C CD2 . LEU A 1 140 ? 103.800 153.294 225.011 1.00 158.56 ? 139 LEU A CD2 1 
ATOM   940  N N   . SER A 1 141 ? 102.452 157.841 226.138 1.00 152.32 ? 140 SER A N   1 
ATOM   941  C CA  . SER A 1 141 ? 103.085 159.073 225.688 1.00 152.32 ? 140 SER A CA  1 
ATOM   942  C C   . SER A 1 141 ? 104.563 159.053 226.041 1.00 152.32 ? 140 SER A C   1 
ATOM   943  O O   . SER A 1 141 ? 104.928 158.786 227.190 1.00 152.32 ? 140 SER A O   1 
ATOM   944  C CB  . SER A 1 141 ? 102.410 160.299 226.308 1.00 152.32 ? 140 SER A CB  1 
ATOM   945  O OG  . SER A 1 141 ? 101.040 160.355 225.955 1.00 152.32 ? 140 SER A OG  1 
ATOM   946  N N   . LEU A 1 142 ? 105.406 159.335 225.050 1.00 147.35 ? 141 LEU A N   1 
ATOM   947  C CA  . LEU A 1 142 ? 106.846 159.441 225.245 1.00 147.35 ? 141 LEU A CA  1 
ATOM   948  C C   . LEU A 1 142 ? 107.330 160.746 224.632 1.00 147.35 ? 141 LEU A C   1 
ATOM   949  O O   . LEU A 1 142 ? 106.704 161.291 223.723 1.00 147.35 ? 141 LEU A O   1 
ATOM   950  C CB  . LEU A 1 142 ? 107.605 158.264 224.614 1.00 147.35 ? 141 LEU A CB  1 
ATOM   951  C CG  . LEU A 1 142 ? 107.757 156.947 225.382 1.00 147.35 ? 141 LEU A CG  1 
ATOM   952  C CD1 . LEU A 1 142 ? 108.523 157.166 226.674 1.00 147.35 ? 141 LEU A CD1 1 
ATOM   953  C CD2 . LEU A 1 142 ? 106.426 156.271 225.647 1.00 147.35 ? 141 LEU A CD2 1 
ATOM   954  N N   . THR A 1 143 ? 108.460 161.246 225.130 1.00 145.71 ? 142 THR A N   1 
ATOM   955  C CA  . THR A 1 143 ? 109.028 162.488 224.624 1.00 145.71 ? 142 THR A CA  1 
ATOM   956  C C   . THR A 1 143 ? 110.534 162.333 224.477 1.00 145.71 ? 142 THR A C   1 
ATOM   957  O O   . THR A 1 143 ? 111.178 161.682 225.305 1.00 145.71 ? 142 THR A O   1 
ATOM   958  C CB  . THR A 1 143 ? 108.699 163.658 225.558 1.00 145.71 ? 142 THR A CB  1 
ATOM   959  O OG1 . THR A 1 143 ? 107.277 163.804 225.652 1.00 145.71 ? 142 THR A OG1 1 
ATOM   960  C CG2 . THR A 1 143 ? 109.286 164.951 225.030 1.00 145.71 ? 142 THR A CG2 1 
ATOM   961  N N   . CYS A 1 144 ? 111.096 162.932 223.424 1.00 144.79 ? 143 CYS A N   1 
ATOM   962  C CA  . CYS A 1 144 ? 112.525 162.832 223.129 1.00 144.79 ? 143 CYS A CA  1 
ATOM   963  C C   . CYS A 1 144 ? 113.090 164.240 222.945 1.00 144.79 ? 143 CYS A C   1 
ATOM   964  O O   . CYS A 1 144 ? 112.926 164.851 221.885 1.00 144.79 ? 143 CYS A O   1 
ATOM   965  C CB  . CYS A 1 144 ? 112.759 161.965 221.893 1.00 144.79 ? 143 CYS A CB  1 
ATOM   966  S SG  . CYS A 1 144 ? 114.489 161.566 221.555 1.00 144.79 ? 143 CYS A SG  1 
ATOM   967  N N   . SER A 1 145 ? 113.758 164.746 223.980 1.00 142.79 ? 144 SER A N   1 
ATOM   968  C CA  . SER A 1 145 ? 114.357 166.073 223.948 1.00 142.79 ? 144 SER A CA  1 
ATOM   969  C C   . SER A 1 145 ? 115.698 166.052 223.227 1.00 142.79 ? 144 SER A C   1 
ATOM   970  O O   . SER A 1 145 ? 116.473 165.097 223.348 1.00 142.79 ? 144 SER A O   1 
ATOM   971  C CB  . SER A 1 145 ? 114.547 166.603 225.368 1.00 142.79 ? 144 SER A CB  1 
ATOM   972  O OG  . SER A 1 145 ? 113.316 166.649 226.063 1.00 142.79 ? 144 SER A OG  1 
ATOM   973  N N   . ILE A 1 146 ? 115.976 167.132 222.500 1.00 137.21 ? 145 ILE A N   1 
ATOM   974  C CA  . ILE A 1 146 ? 117.162 167.265 221.662 1.00 137.21 ? 145 ILE A CA  1 
ATOM   975  C C   . ILE A 1 146 ? 118.078 168.310 222.282 1.00 137.21 ? 145 ILE A C   1 
ATOM   976  O O   . ILE A 1 146 ? 117.620 169.392 222.666 1.00 137.21 ? 145 ILE A O   1 
ATOM   977  C CB  . ILE A 1 146 ? 116.786 167.670 220.226 1.00 137.21 ? 145 ILE A CB  1 
ATOM   978  C CG1 . ILE A 1 146 ? 115.935 166.588 219.568 1.00 137.21 ? 145 ILE A CG1 1 
ATOM   979  C CG2 . ILE A 1 146 ? 118.031 167.945 219.401 1.00 137.21 ? 145 ILE A CG2 1 
ATOM   980  C CD1 . ILE A 1 146 ? 115.319 167.024 218.267 1.00 137.21 ? 145 ILE A CD1 1 
ATOM   981  N N   . SER A 1 147 ? 119.368 167.994 222.377 1.00 134.68 ? 146 SER A N   1 
ATOM   982  C CA  . SER A 1 147 ? 120.370 168.964 222.800 1.00 134.68 ? 146 SER A CA  1 
ATOM   983  C C   . SER A 1 147 ? 121.482 168.995 221.765 1.00 134.68 ? 146 SER A C   1 
ATOM   984  O O   . SER A 1 147 ? 122.129 167.972 221.516 1.00 134.68 ? 146 SER A O   1 
ATOM   985  C CB  . SER A 1 147 ? 120.927 168.621 224.183 1.00 134.68 ? 146 SER A CB  1 
ATOM   986  O OG  . SER A 1 147 ? 121.548 167.349 224.178 1.00 134.68 ? 146 SER A OG  1 
ATOM   987  N N   . GLY A 1 148 ? 121.705 170.164 221.169 1.00 136.68 ? 147 GLY A N   1 
ATOM   988  C CA  . GLY A 1 148 ? 122.750 170.347 220.181 1.00 136.68 ? 147 GLY A CA  1 
ATOM   989  C C   . GLY A 1 148 ? 122.274 170.568 218.762 1.00 136.68 ? 147 GLY A C   1 
ATOM   990  O O   . GLY A 1 148 ? 123.116 170.699 217.866 1.00 136.68 ? 147 GLY A O   1 
ATOM   991  N N   . ASP A 1 149 ? 120.967 170.618 218.518 1.00 140.51 ? 148 ASP A N   1 
ATOM   992  C CA  . ASP A 1 149 ? 120.456 170.824 217.168 1.00 140.51 ? 148 ASP A CA  1 
ATOM   993  C C   . ASP A 1 149 ? 119.030 171.350 217.249 1.00 140.51 ? 148 ASP A C   1 
ATOM   994  O O   . ASP A 1 149 ? 118.397 171.334 218.307 1.00 140.51 ? 148 ASP A O   1 
ATOM   995  C CB  . ASP A 1 149 ? 120.513 169.535 216.344 1.00 140.51 ? 148 ASP A CB  1 
ATOM   996  C CG  . ASP A 1 149 ? 120.565 169.801 214.853 1.00 140.51 ? 148 ASP A CG  1 
ATOM   997  O OD1 . ASP A 1 149 ? 119.850 170.711 214.386 1.00 140.51 ? 148 ASP A OD1 1 
ATOM   998  O OD2 . ASP A 1 149 ? 121.319 169.099 214.148 1.00 140.51 ? 148 ASP A OD2 1 
ATOM   999  N N   . SER A 1 150 ? 118.534 171.820 216.107 1.00 136.48 ? 149 SER A N   1 
ATOM   1000 C CA  . SER A 1 150 ? 117.179 172.341 215.984 1.00 136.48 ? 149 SER A CA  1 
ATOM   1001 C C   . SER A 1 150 ? 116.287 171.298 215.327 1.00 136.48 ? 149 SER A C   1 
ATOM   1002 O O   . SER A 1 150 ? 116.642 170.741 214.284 1.00 136.48 ? 149 SER A O   1 
ATOM   1003 C CB  . SER A 1 150 ? 117.164 173.632 215.167 1.00 136.48 ? 149 SER A CB  1 
ATOM   1004 O OG  . SER A 1 150 ? 115.835 174.043 214.902 1.00 136.48 ? 149 SER A OG  1 
ATOM   1005 N N   . VAL A 1 151 ? 115.122 171.051 215.932 1.00 131.50 ? 150 VAL A N   1 
ATOM   1006 C CA  . VAL A 1 151 ? 114.233 169.997 215.461 1.00 131.50 ? 150 VAL A CA  1 
ATOM   1007 C C   . VAL A 1 151 ? 113.709 170.284 214.062 1.00 131.50 ? 150 VAL A C   1 
ATOM   1008 O O   . VAL A 1 151 ? 113.329 169.357 213.340 1.00 131.50 ? 150 VAL A O   1 
ATOM   1009 C CB  . VAL A 1 151 ? 113.073 169.803 216.461 1.00 131.50 ? 150 VAL A CB  1 
ATOM   1010 C CG1 . VAL A 1 151 ? 112.195 171.038 216.501 1.00 131.50 ? 150 VAL A CG1 1 
ATOM   1011 C CG2 . VAL A 1 151 ? 112.262 168.566 216.122 1.00 131.50 ? 150 VAL A CG2 1 
ATOM   1012 N N   . SER A 1 152 ? 113.697 171.550 213.648 1.00 132.24 ? 151 SER A N   1 
ATOM   1013 C CA  . SER A 1 152 ? 113.192 171.941 212.340 1.00 132.24 ? 151 SER A CA  1 
ATOM   1014 C C   . SER A 1 152 ? 114.300 172.029 211.298 1.00 132.24 ? 151 SER A C   1 
ATOM   1015 O O   . SER A 1 152 ? 114.218 172.841 210.370 1.00 132.24 ? 151 SER A O   1 
ATOM   1016 C CB  . SER A 1 152 ? 112.449 173.271 212.438 1.00 132.24 ? 151 SER A CB  1 
ATOM   1017 O OG  . SER A 1 152 ? 113.273 174.266 213.017 1.00 132.24 ? 151 SER A OG  1 
ATOM   1018 N N   . SER A 1 153 ? 115.338 171.208 211.436 1.00 128.33 ? 152 SER A N   1 
ATOM   1019 C CA  . SER A 1 153 ? 116.452 171.249 210.500 1.00 128.33 ? 152 SER A CA  1 
ATOM   1020 C C   . SER A 1 153 ? 116.000 170.836 209.106 1.00 128.33 ? 152 SER A C   1 
ATOM   1021 O O   . SER A 1 153 ? 115.068 170.048 208.936 1.00 128.33 ? 152 SER A O   1 
ATOM   1022 C CB  . SER A 1 153 ? 117.582 170.340 210.974 1.00 128.33 ? 152 SER A CB  1 
ATOM   1023 O OG  . SER A 1 153 ? 118.608 170.267 210.001 1.00 128.33 ? 152 SER A OG  1 
ATOM   1024 N N   . ASN A 1 154 ? 116.677 171.387 208.099 1.00 125.86 ? 153 ASN A N   1 
ATOM   1025 C CA  . ASN A 1 154 ? 116.282 171.145 206.718 1.00 125.86 ? 153 ASN A CA  1 
ATOM   1026 C C   . ASN A 1 154 ? 116.690 169.752 206.253 1.00 125.86 ? 153 ASN A C   1 
ATOM   1027 O O   . ASN A 1 154 ? 115.986 169.141 205.442 1.00 125.86 ? 153 ASN A O   1 
ATOM   1028 C CB  . ASN A 1 154 ? 116.900 172.216 205.818 1.00 125.86 ? 153 ASN A CB  1 
ATOM   1029 C CG  . ASN A 1 154 ? 116.376 172.172 204.395 1.00 125.86 ? 153 ASN A CG  1 
ATOM   1030 O OD1 . ASN A 1 154 ? 115.558 171.328 204.039 1.00 125.86 ? 153 ASN A OD1 1 
ATOM   1031 N ND2 . ASN A 1 154 ? 116.852 173.095 203.570 1.00 125.86 ? 153 ASN A ND2 1 
ATOM   1032 N N   . SER A 1 155 ? 117.800 169.223 206.764 1.00 116.17 ? 154 SER A N   1 
ATOM   1033 C CA  . SER A 1 155 ? 118.359 167.989 206.223 1.00 116.17 ? 154 SER A CA  1 
ATOM   1034 C C   . SER A 1 155 ? 118.415 166.874 207.257 1.00 116.17 ? 154 SER A C   1 
ATOM   1035 O O   . SER A 1 155 ? 119.442 166.205 207.394 1.00 116.17 ? 154 SER A O   1 
ATOM   1036 C CB  . SER A 1 155 ? 119.759 168.247 205.669 1.00 116.17 ? 154 SER A CB  1 
ATOM   1037 O OG  . SER A 1 155 ? 120.622 168.715 206.689 1.00 116.17 ? 154 SER A OG  1 
ATOM   1038 N N   . ALA A 1 156 ? 117.325 166.663 207.990 1.00 110.25 ? 155 ALA A N   1 
ATOM   1039 C CA  . ALA A 1 156 ? 117.282 165.601 208.982 1.00 110.25 ? 155 ALA A CA  1 
ATOM   1040 C C   . ALA A 1 156 ? 115.851 165.114 209.133 1.00 110.25 ? 155 ALA A C   1 
ATOM   1041 O O   . ALA A 1 156 ? 114.898 165.810 208.781 1.00 110.25 ? 155 ALA A O   1 
ATOM   1042 C CB  . ALA A 1 156 ? 117.833 166.070 210.331 1.00 110.25 ? 155 ALA A CB  1 
ATOM   1043 N N   . ALA A 1 157 ? 115.713 163.899 209.657 1.00 107.38 ? 156 ALA A N   1 
ATOM   1044 C CA  . ALA A 1 157 ? 114.408 163.330 209.959 1.00 107.38 ? 156 ALA A CA  1 
ATOM   1045 C C   . ALA A 1 157 ? 114.472 162.641 211.311 1.00 107.38 ? 156 ALA A C   1 
ATOM   1046 O O   . ALA A 1 157 ? 115.519 162.119 211.706 1.00 107.38 ? 156 ALA A O   1 
ATOM   1047 C CB  . ALA A 1 157 ? 113.958 162.340 208.883 1.00 107.38 ? 156 ALA A CB  1 
ATOM   1048 N N   . TRP A 1 158 ? 113.345 162.636 212.021 1.00 112.63 ? 157 TRP A N   1 
ATOM   1049 C CA  . TRP A 1 158 ? 113.282 162.086 213.368 1.00 112.63 ? 157 TRP A CA  1 
ATOM   1050 C C   . TRP A 1 158 ? 112.372 160.869 213.376 1.00 112.63 ? 157 TRP A C   1 
ATOM   1051 O O   . TRP A 1 158 ? 111.218 160.950 212.940 1.00 112.63 ? 157 TRP A O   1 
ATOM   1052 C CB  . TRP A 1 158 ? 112.791 163.143 214.355 1.00 112.63 ? 157 TRP A CB  1 
ATOM   1053 C CG  . TRP A 1 158 ? 113.431 164.469 214.119 1.00 112.63 ? 157 TRP A CG  1 
ATOM   1054 C CD1 . TRP A 1 158 ? 112.937 165.493 213.372 1.00 112.63 ? 157 TRP A CD1 1 
ATOM   1055 C CD2 . TRP A 1 158 ? 114.699 164.910 214.613 1.00 112.63 ? 157 TRP A CD2 1 
ATOM   1056 N NE1 . TRP A 1 158 ? 113.812 166.549 213.377 1.00 112.63 ? 157 TRP A NE1 1 
ATOM   1057 C CE2 . TRP A 1 158 ? 114.903 166.214 214.133 1.00 112.63 ? 157 TRP A CE2 1 
ATOM   1058 C CE3 . TRP A 1 158 ? 115.678 164.329 215.420 1.00 112.63 ? 157 TRP A CE3 1 
ATOM   1059 C CZ2 . TRP A 1 158 ? 116.044 166.947 214.432 1.00 112.63 ? 157 TRP A CZ2 1 
ATOM   1060 C CZ3 . TRP A 1 158 ? 116.810 165.059 215.716 1.00 112.63 ? 157 TRP A CZ3 1 
ATOM   1061 C CH2 . TRP A 1 158 ? 116.984 166.352 215.223 1.00 112.63 ? 157 TRP A CH2 1 
ATOM   1062 N N   . ASN A 1 159 ? 112.886 159.749 213.881 1.00 114.09 ? 158 ASN A N   1 
ATOM   1063 C CA  . ASN A 1 159 ? 112.220 158.461 213.768 1.00 114.09 ? 158 ASN A CA  1 
ATOM   1064 C C   . ASN A 1 159 ? 111.739 157.986 215.133 1.00 114.09 ? 158 ASN A C   1 
ATOM   1065 O O   . ASN A 1 159 ? 111.928 158.648 216.156 1.00 114.09 ? 158 ASN A O   1 
ATOM   1066 C CB  . ASN A 1 159 ? 113.164 157.432 213.155 1.00 114.09 ? 158 ASN A CB  1 
ATOM   1067 C CG  . ASN A 1 159 ? 113.468 157.711 211.709 1.00 114.09 ? 158 ASN A CG  1 
ATOM   1068 O OD1 . ASN A 1 159 ? 112.595 158.072 210.939 1.00 114.09 ? 158 ASN A OD1 1 
ATOM   1069 N ND2 . ASN A 1 159 ? 114.718 157.541 211.333 1.00 114.09 ? 158 ASN A ND2 1 
ATOM   1070 N N   . TRP A 1 160 ? 111.099 156.819 215.138 1.00 126.54 ? 159 TRP A N   1 
ATOM   1071 C CA  . TRP A 1 160 ? 110.808 156.103 216.376 1.00 126.54 ? 159 TRP A CA  1 
ATOM   1072 C C   . TRP A 1 160 ? 110.979 154.613 216.128 1.00 126.54 ? 159 TRP A C   1 
ATOM   1073 O O   . TRP A 1 160 ? 110.364 154.066 215.209 1.00 126.54 ? 159 TRP A O   1 
ATOM   1074 C CB  . TRP A 1 160 ? 109.398 156.408 216.874 1.00 126.54 ? 159 TRP A CB  1 
ATOM   1075 C CG  . TRP A 1 160 ? 109.339 157.585 217.776 1.00 126.54 ? 159 TRP A CG  1 
ATOM   1076 C CD1 . TRP A 1 160 ? 108.986 158.853 217.439 1.00 126.54 ? 159 TRP A CD1 1 
ATOM   1077 C CD2 . TRP A 1 160 ? 109.640 157.610 219.174 1.00 126.54 ? 159 TRP A CD2 1 
ATOM   1078 N NE1 . TRP A 1 160 ? 109.046 159.671 218.539 1.00 126.54 ? 159 TRP A NE1 1 
ATOM   1079 C CE2 . TRP A 1 160 ? 109.447 158.930 219.618 1.00 126.54 ? 159 TRP A CE2 1 
ATOM   1080 C CE3 . TRP A 1 160 ? 110.054 156.646 220.093 1.00 126.54 ? 159 TRP A CE3 1 
ATOM   1081 C CZ2 . TRP A 1 160 ? 109.653 159.309 220.938 1.00 126.54 ? 159 TRP A CZ2 1 
ATOM   1082 C CZ3 . TRP A 1 160 ? 110.256 157.024 221.402 1.00 126.54 ? 159 TRP A CZ3 1 
ATOM   1083 C CH2 . TRP A 1 160 ? 110.057 158.343 221.813 1.00 126.54 ? 159 TRP A CH2 1 
ATOM   1084 N N   . ILE A 1 161 ? 111.808 153.956 216.941 1.00 126.79 ? 160 ILE A N   1 
ATOM   1085 C CA  . ILE A 1 161 ? 112.090 152.534 216.793 1.00 126.79 ? 160 ILE A CA  1 
ATOM   1086 C C   . ILE A 1 161 ? 111.697 151.829 218.081 1.00 126.79 ? 160 ILE A C   1 
ATOM   1087 O O   . ILE A 1 161 ? 111.799 152.396 219.172 1.00 126.79 ? 160 ILE A O   1 
ATOM   1088 C CB  . ILE A 1 161 ? 113.577 152.276 216.471 1.00 126.79 ? 160 ILE A CB  1 
ATOM   1089 C CG1 . ILE A 1 161 ? 114.030 153.128 215.290 1.00 126.79 ? 160 ILE A CG1 1 
ATOM   1090 C CG2 . ILE A 1 161 ? 113.811 150.817 216.145 1.00 126.79 ? 160 ILE A CG2 1 
ATOM   1091 C CD1 . ILE A 1 161 ? 113.179 152.953 214.072 1.00 126.79 ? 160 ILE A CD1 1 
ATOM   1092 N N   . ARG A 1 162 ? 111.236 150.588 217.956 1.00 132.15 ? 161 ARG A N   1 
ATOM   1093 C CA  . ARG A 1 162 ? 110.950 149.775 219.127 1.00 132.15 ? 161 ARG A CA  1 
ATOM   1094 C C   . ARG A 1 162 ? 111.456 148.361 218.898 1.00 132.15 ? 161 ARG A C   1 
ATOM   1095 O O   . ARG A 1 162 ? 111.531 147.885 217.762 1.00 132.15 ? 161 ARG A O   1 
ATOM   1096 C CB  . ARG A 1 162 ? 109.455 149.759 219.467 1.00 132.15 ? 161 ARG A CB  1 
ATOM   1097 C CG  . ARG A 1 162 ? 108.586 148.918 218.554 1.00 132.15 ? 161 ARG A CG  1 
ATOM   1098 C CD  . ARG A 1 162 ? 107.178 148.826 219.117 1.00 132.15 ? 161 ARG A CD  1 
ATOM   1099 N NE  . ARG A 1 162 ? 106.291 148.028 218.280 1.00 132.15 ? 161 ARG A NE  1 
ATOM   1100 C CZ  . ARG A 1 162 ? 105.019 147.785 218.562 1.00 132.15 ? 161 ARG A CZ  1 
ATOM   1101 N NH1 . ARG A 1 162 ? 104.453 148.256 219.660 1.00 132.15 ? 161 ARG A NH1 1 
ATOM   1102 N NH2 . ARG A 1 162 ? 104.297 147.053 217.720 1.00 132.15 ? 161 ARG A NH2 1 
ATOM   1103 N N   . GLN A 1 163 ? 111.811 147.699 219.994 1.00 136.70 ? 162 GLN A N   1 
ATOM   1104 C CA  . GLN A 1 163 ? 112.385 146.364 219.956 1.00 136.70 ? 162 GLN A CA  1 
ATOM   1105 C C   . GLN A 1 163 ? 111.703 145.483 220.987 1.00 136.70 ? 162 GLN A C   1 
ATOM   1106 O O   . GLN A 1 163 ? 111.488 145.905 222.129 1.00 136.70 ? 162 GLN A O   1 
ATOM   1107 C CB  . GLN A 1 163 ? 113.890 146.400 220.221 1.00 136.70 ? 162 GLN A CB  1 
ATOM   1108 C CG  . GLN A 1 163 ? 114.559 145.045 220.119 1.00 136.70 ? 162 GLN A CG  1 
ATOM   1109 C CD  . GLN A 1 163 ? 116.006 145.080 220.554 1.00 136.70 ? 162 GLN A CD  1 
ATOM   1110 O OE1 . GLN A 1 163 ? 116.360 145.763 221.513 1.00 136.70 ? 162 GLN A OE1 1 
ATOM   1111 N NE2 . GLN A 1 163 ? 116.853 144.344 219.849 1.00 136.70 ? 162 GLN A NE2 1 
ATOM   1112 N N   . SER A 1 164 ? 111.365 144.266 220.576 1.00 145.92 ? 163 SER A N   1 
ATOM   1113 C CA  . SER A 1 164 ? 110.857 143.220 221.446 1.00 145.92 ? 163 SER A CA  1 
ATOM   1114 C C   . SER A 1 164 ? 111.506 141.907 221.039 1.00 145.92 ? 163 SER A C   1 
ATOM   1115 O O   . SER A 1 164 ? 111.788 141.694 219.854 1.00 145.92 ? 163 SER A O   1 
ATOM   1116 C CB  . SER A 1 164 ? 109.329 143.091 221.355 1.00 145.92 ? 163 SER A CB  1 
ATOM   1117 O OG  . SER A 1 164 ? 108.939 142.611 220.081 1.00 145.92 ? 163 SER A OG  1 
ATOM   1118 N N   . PRO A 1 165 ? 111.757 141.012 221.996 1.00 149.19 ? 164 PRO A N   1 
ATOM   1119 C CA  . PRO A 1 165 ? 112.414 139.741 221.648 1.00 149.19 ? 164 PRO A CA  1 
ATOM   1120 C C   . PRO A 1 165 ? 111.629 138.898 220.659 1.00 149.19 ? 164 PRO A C   1 
ATOM   1121 O O   . PRO A 1 165 ? 112.236 138.186 219.849 1.00 149.19 ? 164 PRO A O   1 
ATOM   1122 C CB  . PRO A 1 165 ? 112.555 139.037 223.006 1.00 149.19 ? 164 PRO A CB  1 
ATOM   1123 C CG  . PRO A 1 165 ? 111.550 139.700 223.892 1.00 149.19 ? 164 PRO A CG  1 
ATOM   1124 C CD  . PRO A 1 165 ? 111.486 141.120 223.438 1.00 149.19 ? 164 PRO A CD  1 
ATOM   1125 N N   . SER A 1 166 ? 110.298 138.955 220.695 1.00 151.45 ? 165 SER A N   1 
ATOM   1126 C CA  . SER A 1 166 ? 109.498 138.120 219.808 1.00 151.45 ? 165 SER A CA  1 
ATOM   1127 C C   . SER A 1 166 ? 109.507 138.622 218.370 1.00 151.45 ? 165 SER A C   1 
ATOM   1128 O O   . SER A 1 166 ? 109.372 137.819 217.441 1.00 151.45 ? 165 SER A O   1 
ATOM   1129 C CB  . SER A 1 166 ? 108.060 138.040 220.320 1.00 151.45 ? 165 SER A CB  1 
ATOM   1130 O OG  . SER A 1 166 ? 107.591 139.317 220.713 1.00 151.45 ? 165 SER A OG  1 
ATOM   1131 N N   . ARG A 1 167 ? 109.658 139.930 218.162 1.00 149.28 ? 166 ARG A N   1 
ATOM   1132 C CA  . ARG A 1 167 ? 109.591 140.508 216.829 1.00 149.28 ? 166 ARG A CA  1 
ATOM   1133 C C   . ARG A 1 167 ? 110.871 141.196 216.382 1.00 149.28 ? 166 ARG A C   1 
ATOM   1134 O O   . ARG A 1 167 ? 110.961 141.584 215.213 1.00 149.28 ? 166 ARG A O   1 
ATOM   1135 C CB  . ARG A 1 167 ? 108.435 141.516 216.742 1.00 149.28 ? 166 ARG A CB  1 
ATOM   1136 C CG  . ARG A 1 167 ? 107.083 140.943 217.115 1.00 149.28 ? 166 ARG A CG  1 
ATOM   1137 C CD  . ARG A 1 167 ? 106.043 142.041 217.223 1.00 149.28 ? 166 ARG A CD  1 
ATOM   1138 N NE  . ARG A 1 167 ? 105.812 142.431 218.608 1.00 149.28 ? 166 ARG A NE  1 
ATOM   1139 C CZ  . ARG A 1 167 ? 105.818 143.683 219.045 1.00 149.28 ? 166 ARG A CZ  1 
ATOM   1140 N NH1 . ARG A 1 167 ? 106.059 144.698 218.232 1.00 149.28 ? 166 ARG A NH1 1 
ATOM   1141 N NH2 . ARG A 1 167 ? 105.581 143.921 220.332 1.00 149.28 ? 166 ARG A NH2 1 
ATOM   1142 N N   . GLY A 1 168 ? 111.854 141.361 217.261 1.00 141.80 ? 167 GLY A N   1 
ATOM   1143 C CA  . GLY A 1 168 ? 113.088 142.013 216.875 1.00 141.80 ? 167 GLY A CA  1 
ATOM   1144 C C   . GLY A 1 168 ? 112.964 143.521 216.818 1.00 141.80 ? 167 GLY A C   1 
ATOM   1145 O O   . GLY A 1 168 ? 112.248 144.119 217.626 1.00 141.80 ? 167 GLY A O   1 
ATOM   1146 N N   . LEU A 1 169 ? 113.655 144.146 215.870 1.00 125.12 ? 168 LEU A N   1 
ATOM   1147 C CA  . LEU A 1 169 ? 113.636 145.594 215.726 1.00 125.12 ? 168 LEU A CA  1 
ATOM   1148 C C   . LEU A 1 169 ? 112.576 145.997 214.710 1.00 125.12 ? 168 LEU A C   1 
ATOM   1149 O O   . LEU A 1 169 ? 112.541 145.469 213.595 1.00 125.12 ? 168 LEU A O   1 
ATOM   1150 C CB  . LEU A 1 169 ? 115.012 146.105 215.302 1.00 125.12 ? 168 LEU A CB  1 
ATOM   1151 C CG  . LEU A 1 169 ? 116.080 146.038 216.394 1.00 125.12 ? 168 LEU A CG  1 
ATOM   1152 C CD1 . LEU A 1 169 ? 117.469 146.097 215.800 1.00 125.12 ? 168 LEU A CD1 1 
ATOM   1153 C CD2 . LEU A 1 169 ? 115.889 147.166 217.379 1.00 125.12 ? 168 LEU A CD2 1 
ATOM   1154 N N   . GLU A 1 170 ? 111.716 146.934 215.100 1.00 128.79 ? 169 GLU A N   1 
ATOM   1155 C CA  . GLU A 1 170 ? 110.564 147.324 214.303 1.00 128.79 ? 169 GLU A CA  1 
ATOM   1156 C C   . GLU A 1 170 ? 110.532 148.835 214.144 1.00 128.79 ? 169 GLU A C   1 
ATOM   1157 O O   . GLU A 1 170 ? 110.810 149.573 215.093 1.00 128.79 ? 169 GLU A O   1 
ATOM   1158 C CB  . GLU A 1 170 ? 109.268 146.837 214.953 1.00 128.79 ? 169 GLU A CB  1 
ATOM   1159 C CG  . GLU A 1 170 ? 108.014 147.126 214.157 1.00 128.79 ? 169 GLU A CG  1 
ATOM   1160 C CD  . GLU A 1 170 ? 106.768 146.577 214.823 1.00 128.79 ? 169 GLU A CD  1 
ATOM   1161 O OE1 . GLU A 1 170 ? 106.889 145.991 215.918 1.00 128.79 ? 169 GLU A OE1 1 
ATOM   1162 O OE2 . GLU A 1 170 ? 105.668 146.730 214.251 1.00 128.79 ? 169 GLU A OE2 1 
ATOM   1163 N N   . TRP A 1 171 ? 110.187 149.290 212.942 1.00 119.86 ? 170 TRP A N   1 
ATOM   1164 C CA  . TRP A 1 171 ? 110.068 150.712 212.650 1.00 119.86 ? 170 TRP A CA  1 
ATOM   1165 C C   . TRP A 1 171 ? 108.625 151.154 212.856 1.00 119.86 ? 170 TRP A C   1 
ATOM   1166 O O   . TRP A 1 171 ? 107.700 150.526 212.335 1.00 119.86 ? 170 TRP A O   1 
ATOM   1167 C CB  . TRP A 1 171 ? 110.511 151.000 211.216 1.00 119.86 ? 170 TRP A CB  1 
ATOM   1168 C CG  . TRP A 1 171 ? 110.568 152.452 210.880 1.00 119.86 ? 170 TRP A CG  1 
ATOM   1169 C CD1 . TRP A 1 171 ? 111.581 153.314 211.158 1.00 119.86 ? 170 TRP A CD1 1 
ATOM   1170 C CD2 . TRP A 1 171 ? 109.571 153.214 210.195 1.00 119.86 ? 170 TRP A CD2 1 
ATOM   1171 N NE1 . TRP A 1 171 ? 111.279 154.567 210.693 1.00 119.86 ? 170 TRP A NE1 1 
ATOM   1172 C CE2 . TRP A 1 171 ? 110.049 154.531 210.096 1.00 119.86 ? 170 TRP A CE2 1 
ATOM   1173 C CE3 . TRP A 1 171 ? 108.322 152.910 209.656 1.00 119.86 ? 170 TRP A CE3 1 
ATOM   1174 C CZ2 . TRP A 1 171 ? 109.322 155.541 209.484 1.00 119.86 ? 170 TRP A CZ2 1 
ATOM   1175 C CZ3 . TRP A 1 171 ? 107.603 153.914 209.049 1.00 119.86 ? 170 TRP A CZ3 1 
ATOM   1176 C CH2 . TRP A 1 171 ? 108.105 155.214 208.968 1.00 119.86 ? 170 TRP A CH2 1 
ATOM   1177 N N   . LEU A 1 172 ? 108.434 152.234 213.613 1.00 125.11 ? 171 LEU A N   1 
ATOM   1178 C CA  . LEU A 1 172 ? 107.096 152.708 213.952 1.00 125.11 ? 171 LEU A CA  1 
ATOM   1179 C C   . LEU A 1 172 ? 106.653 153.876 213.076 1.00 125.11 ? 171 LEU A C   1 
ATOM   1180 O O   . LEU A 1 172 ? 105.618 153.794 212.412 1.00 125.11 ? 171 LEU A O   1 
ATOM   1181 C CB  . LEU A 1 172 ? 107.039 153.102 215.432 1.00 125.11 ? 171 LEU A CB  1 
ATOM   1182 C CG  . LEU A 1 172 ? 107.288 151.975 216.431 1.00 125.11 ? 171 LEU A CG  1 
ATOM   1183 C CD1 . LEU A 1 172 ? 107.040 152.450 217.848 1.00 125.11 ? 171 LEU A CD1 1 
ATOM   1184 C CD2 . LEU A 1 172 ? 106.410 150.788 216.107 1.00 125.11 ? 171 LEU A CD2 1 
ATOM   1185 N N   . GLY A 1 173 ? 107.415 154.963 213.063 1.00 123.60 ? 172 GLY A N   1 
ATOM   1186 C CA  . GLY A 1 173 ? 107.015 156.130 212.298 1.00 123.60 ? 172 GLY A CA  1 
ATOM   1187 C C   . GLY A 1 173 ? 108.103 157.180 212.304 1.00 123.60 ? 172 GLY A C   1 
ATOM   1188 O O   . GLY A 1 173 ? 109.145 157.027 212.949 1.00 123.60 ? 172 GLY A O   1 
ATOM   1189 N N   . ARG A 1 174 ? 107.844 158.260 211.567 1.00 115.09 ? 173 ARG A N   1 
ATOM   1190 C CA  . ARG A 1 174 ? 108.835 159.315 211.415 1.00 115.09 ? 173 ARG A CA  1 
ATOM   1191 C C   . ARG A 1 174 ? 108.160 160.629 211.066 1.00 115.09 ? 173 ARG A C   1 
ATOM   1192 O O   . ARG A 1 174 ? 107.030 160.662 210.570 1.00 115.09 ? 173 ARG A O   1 
ATOM   1193 C CB  . ARG A 1 174 ? 109.858 158.977 210.335 1.00 115.09 ? 173 ARG A CB  1 
ATOM   1194 C CG  . ARG A 1 174 ? 109.428 159.313 208.927 1.00 115.09 ? 173 ARG A CG  1 
ATOM   1195 C CD  . ARG A 1 174 ? 110.589 159.125 207.975 1.00 115.09 ? 173 ARG A CD  1 
ATOM   1196 N NE  . ARG A 1 174 ? 110.182 159.194 206.579 1.00 115.09 ? 173 ARG A NE  1 
ATOM   1197 C CZ  . ARG A 1 174 ? 110.997 158.981 205.557 1.00 115.09 ? 173 ARG A CZ  1 
ATOM   1198 N NH1 . ARG A 1 174 ? 112.274 158.692 205.742 1.00 115.09 ? 173 ARG A NH1 1 
ATOM   1199 N NH2 . ARG A 1 174 ? 110.520 159.055 204.319 1.00 115.09 ? 173 ARG A NH2 1 
ATOM   1200 N N   . THR A 1 175 ? 108.897 161.712 211.305 1.00 120.54 ? 174 THR A N   1 
ATOM   1201 C CA  . THR A 1 175 ? 108.455 163.052 210.953 1.00 120.54 ? 174 THR A CA  1 
ATOM   1202 C C   . THR A 1 175 ? 109.641 163.883 210.484 1.00 120.54 ? 174 THR A C   1 
ATOM   1203 O O   . THR A 1 175 ? 110.796 163.615 210.842 1.00 120.54 ? 174 THR A O   1 
ATOM   1204 C CB  . THR A 1 175 ? 107.774 163.758 212.128 1.00 120.54 ? 174 THR A CB  1 
ATOM   1205 O OG1 . THR A 1 175 ? 107.452 165.101 211.753 1.00 120.54 ? 174 THR A OG1 1 
ATOM   1206 C CG2 . THR A 1 175 ? 108.695 163.788 213.329 1.00 120.54 ? 174 THR A CG2 1 
ATOM   1207 N N   . TYR A 1 176 ? 109.345 164.895 209.674 1.00 123.59 ? 175 TYR A N   1 
ATOM   1208 C CA  . TYR A 1 176 ? 110.371 165.830 209.230 1.00 123.59 ? 175 TYR A CA  1 
ATOM   1209 C C   . TYR A 1 176 ? 109.699 167.082 208.682 1.00 123.59 ? 175 TYR A C   1 
ATOM   1210 O O   . TYR A 1 176 ? 108.475 167.225 208.719 1.00 123.59 ? 175 TYR A O   1 
ATOM   1211 C CB  . TYR A 1 176 ? 111.303 165.192 208.199 1.00 123.59 ? 175 TYR A CB  1 
ATOM   1212 C CG  . TYR A 1 176 ? 110.618 164.607 206.993 1.00 123.59 ? 175 TYR A CG  1 
ATOM   1213 C CD1 . TYR A 1 176 ? 110.054 163.344 207.037 1.00 123.59 ? 175 TYR A CD1 1 
ATOM   1214 C CD2 . TYR A 1 176 ? 110.568 165.304 205.799 1.00 123.59 ? 175 TYR A CD2 1 
ATOM   1215 C CE1 . TYR A 1 176 ? 109.439 162.799 205.931 1.00 123.59 ? 175 TYR A CE1 1 
ATOM   1216 C CE2 . TYR A 1 176 ? 109.957 164.767 204.687 1.00 123.59 ? 175 TYR A CE2 1 
ATOM   1217 C CZ  . TYR A 1 176 ? 109.394 163.515 204.758 1.00 123.59 ? 175 TYR A CZ  1 
ATOM   1218 O OH  . TYR A 1 176 ? 108.782 162.976 203.652 1.00 123.59 ? 175 TYR A OH  1 
ATOM   1219 N N   . TYR A 1 177 ? 110.522 167.995 208.170 1.00 130.28 ? 176 TYR A N   1 
ATOM   1220 C CA  . TYR A 1 177 ? 110.055 169.308 207.742 1.00 130.28 ? 176 TYR A CA  1 
ATOM   1221 C C   . TYR A 1 177 ? 110.956 169.810 206.627 1.00 130.28 ? 176 TYR A C   1 
ATOM   1222 O O   . TYR A 1 177 ? 112.165 169.952 206.827 1.00 130.28 ? 176 TYR A O   1 
ATOM   1223 C CB  . TYR A 1 177 ? 110.056 170.287 208.917 1.00 130.28 ? 176 TYR A CB  1 
ATOM   1224 C CG  . TYR A 1 177 ? 109.729 171.717 208.555 1.00 130.28 ? 176 TYR A CG  1 
ATOM   1225 C CD1 . TYR A 1 177 ? 110.726 172.605 208.173 1.00 130.28 ? 176 TYR A CD1 1 
ATOM   1226 C CD2 . TYR A 1 177 ? 108.425 172.187 208.617 1.00 130.28 ? 176 TYR A CD2 1 
ATOM   1227 C CE1 . TYR A 1 177 ? 110.431 173.912 207.847 1.00 130.28 ? 176 TYR A CE1 1 
ATOM   1228 C CE2 . TYR A 1 177 ? 108.122 173.493 208.294 1.00 130.28 ? 176 TYR A CE2 1 
ATOM   1229 C CZ  . TYR A 1 177 ? 109.129 174.351 207.909 1.00 130.28 ? 176 TYR A CZ  1 
ATOM   1230 O OH  . TYR A 1 177 ? 108.831 175.653 207.587 1.00 130.28 ? 176 TYR A OH  1 
ATOM   1231 N N   . ARG A 1 178 ? 110.375 170.079 205.460 1.00 127.72 ? 177 ARG A N   1 
ATOM   1232 C CA  . ARG A 1 178 ? 111.093 170.704 204.357 1.00 127.72 ? 177 ARG A CA  1 
ATOM   1233 C C   . ARG A 1 178 ? 110.543 172.091 204.053 1.00 127.72 ? 177 ARG A C   1 
ATOM   1234 O O   . ARG A 1 178 ? 111.278 173.080 204.096 1.00 127.72 ? 177 ARG A O   1 
ATOM   1235 C CB  . ARG A 1 178 ? 111.021 169.813 203.114 1.00 127.72 ? 177 ARG A CB  1 
ATOM   1236 C CG  . ARG A 1 178 ? 111.582 168.428 203.330 1.00 127.72 ? 177 ARG A CG  1 
ATOM   1237 C CD  . ARG A 1 178 ? 113.093 168.436 203.241 1.00 127.72 ? 177 ARG A CD  1 
ATOM   1238 N NE  . ARG A 1 178 ? 113.685 167.265 203.875 1.00 127.72 ? 177 ARG A NE  1 
ATOM   1239 C CZ  . ARG A 1 178 ? 113.827 167.112 205.184 1.00 127.72 ? 177 ARG A CZ  1 
ATOM   1240 N NH1 . ARG A 1 178 ? 113.441 168.047 206.034 1.00 127.72 ? 177 ARG A NH1 1 
ATOM   1241 N NH2 . ARG A 1 178 ? 114.379 165.996 205.650 1.00 127.72 ? 177 ARG A NH2 1 
ATOM   1242 N N   . SER A 1 179 ? 109.257 172.183 203.750 1.00 135.66 ? 178 SER A N   1 
ATOM   1243 C CA  . SER A 1 179 ? 108.529 173.442 203.700 1.00 135.66 ? 178 SER A CA  1 
ATOM   1244 C C   . SER A 1 179 ? 107.422 173.497 204.735 1.00 135.66 ? 178 SER A C   1 
ATOM   1245 O O   . SER A 1 179 ? 107.254 174.518 205.405 1.00 135.66 ? 178 SER A O   1 
ATOM   1246 C CB  . SER A 1 179 ? 107.938 173.663 202.302 1.00 135.66 ? 178 SER A CB  1 
ATOM   1247 O OG  . SER A 1 179 ? 106.966 172.678 202.005 1.00 135.66 ? 178 SER A OG  1 
ATOM   1248 N N   . LYS A 1 180 ? 106.664 172.412 204.878 1.00 135.58 ? 179 LYS A N   1 
ATOM   1249 C CA  . LYS A 1 180 ? 105.767 172.226 206.008 1.00 135.58 ? 179 LYS A CA  1 
ATOM   1250 C C   . LYS A 1 180 ? 106.103 170.896 206.669 1.00 135.58 ? 179 LYS A C   1 
ATOM   1251 O O   . LYS A 1 180 ? 107.116 170.276 206.333 1.00 135.58 ? 179 LYS A O   1 
ATOM   1252 C CB  . LYS A 1 180 ? 104.307 172.271 205.568 1.00 135.58 ? 179 LYS A CB  1 
ATOM   1253 C CG  . LYS A 1 180 ? 103.960 171.297 204.463 1.00 135.58 ? 179 LYS A CG  1 
ATOM   1254 C CD  . LYS A 1 180 ? 102.458 171.220 204.279 1.00 135.58 ? 179 LYS A CD  1 
ATOM   1255 C CE  . LYS A 1 180 ? 101.763 170.987 205.608 1.00 135.58 ? 179 LYS A CE  1 
ATOM   1256 N NZ  . LYS A 1 180 ? 102.236 169.732 206.259 1.00 135.58 ? 179 LYS A NZ  1 
ATOM   1257 N N   . TRP A 1 181 ? 105.279 170.449 207.608 1.00 130.74 ? 180 TRP A N   1 
ATOM   1258 C CA  . TRP A 1 181 ? 105.565 169.231 208.350 1.00 130.74 ? 180 TRP A CA  1 
ATOM   1259 C C   . TRP A 1 181 ? 105.018 168.016 207.615 1.00 130.74 ? 180 TRP A C   1 
ATOM   1260 O O   . TRP A 1 181 ? 103.904 168.043 207.084 1.00 130.74 ? 180 TRP A O   1 
ATOM   1261 C CB  . TRP A 1 181 ? 104.972 169.316 209.754 1.00 130.74 ? 180 TRP A CB  1 
ATOM   1262 C CG  . TRP A 1 181 ? 105.687 170.303 210.610 1.00 130.74 ? 180 TRP A CG  1 
ATOM   1263 C CD1 . TRP A 1 181 ? 105.282 171.567 210.911 1.00 130.74 ? 180 TRP A CD1 1 
ATOM   1264 C CD2 . TRP A 1 181 ? 106.939 170.114 211.273 1.00 130.74 ? 180 TRP A CD2 1 
ATOM   1265 N NE1 . TRP A 1 181 ? 106.204 172.179 211.723 1.00 130.74 ? 180 TRP A NE1 1 
ATOM   1266 C CE2 . TRP A 1 181 ? 107.231 171.306 211.961 1.00 130.74 ? 180 TRP A CE2 1 
ATOM   1267 C CE3 . TRP A 1 181 ? 107.840 169.050 211.355 1.00 130.74 ? 180 TRP A CE3 1 
ATOM   1268 C CZ2 . TRP A 1 181 ? 108.386 171.465 212.719 1.00 130.74 ? 180 TRP A CZ2 1 
ATOM   1269 C CZ3 . TRP A 1 181 ? 108.986 169.211 212.108 1.00 130.74 ? 180 TRP A CZ3 1 
ATOM   1270 C CH2 . TRP A 1 181 ? 109.249 170.408 212.780 1.00 130.74 ? 180 TRP A CH2 1 
ATOM   1271 N N   . TYR A 1 182 ? 105.815 166.951 207.579 1.00 128.47 ? 181 TYR A N   1 
ATOM   1272 C CA  . TYR A 1 182 ? 105.449 165.711 206.914 1.00 128.47 ? 181 TYR A CA  1 
ATOM   1273 C C   . TYR A 1 182 ? 105.644 164.550 207.875 1.00 128.47 ? 181 TYR A C   1 
ATOM   1274 O O   . TYR A 1 182 ? 106.631 164.504 208.617 1.00 128.47 ? 181 TYR A O   1 
ATOM   1275 C CB  . TYR A 1 182 ? 106.285 165.488 205.653 1.00 128.47 ? 181 TYR A CB  1 
ATOM   1276 C CG  . TYR A 1 182 ? 106.031 166.499 204.564 1.00 128.47 ? 181 TYR A CG  1 
ATOM   1277 C CD1 . TYR A 1 182 ? 106.565 167.774 204.639 1.00 128.47 ? 181 TYR A CD1 1 
ATOM   1278 C CD2 . TYR A 1 182 ? 105.271 166.173 203.454 1.00 128.47 ? 181 TYR A CD2 1 
ATOM   1279 C CE1 . TYR A 1 182 ? 106.337 168.701 203.648 1.00 128.47 ? 181 TYR A CE1 1 
ATOM   1280 C CE2 . TYR A 1 182 ? 105.040 167.093 202.455 1.00 128.47 ? 181 TYR A CE2 1 
ATOM   1281 C CZ  . TYR A 1 182 ? 105.576 168.355 202.557 1.00 128.47 ? 181 TYR A CZ  1 
ATOM   1282 O OH  . TYR A 1 182 ? 105.349 169.279 201.565 1.00 128.47 ? 181 TYR A OH  1 
ATOM   1283 N N   . ASN A 1 183 ? 104.696 163.616 207.858 1.00 128.26 ? 182 ASN A N   1 
ATOM   1284 C CA  . ASN A 1 183 ? 104.717 162.455 208.732 1.00 128.26 ? 182 ASN A CA  1 
ATOM   1285 C C   . ASN A 1 183 ? 104.533 161.187 207.914 1.00 128.26 ? 182 ASN A C   1 
ATOM   1286 O O   . ASN A 1 183 ? 103.896 161.198 206.859 1.00 128.26 ? 182 ASN A O   1 
ATOM   1287 C CB  . ASN A 1 183 ? 103.619 162.527 209.797 1.00 128.26 ? 182 ASN A CB  1 
ATOM   1288 C CG  . ASN A 1 183 ? 103.897 163.570 210.855 1.00 128.26 ? 182 ASN A CG  1 
ATOM   1289 O OD1 . ASN A 1 183 ? 104.673 164.499 210.643 1.00 128.26 ? 182 ASN A OD1 1 
ATOM   1290 N ND2 . ASN A 1 183 ? 103.264 163.418 212.011 1.00 128.26 ? 182 ASN A ND2 1 
ATOM   1291 N N   . ASP A 1 184 ? 105.102 160.091 208.414 1.00 128.38 ? 183 ASP A N   1 
ATOM   1292 C CA  . ASP A 1 184 ? 104.881 158.768 207.847 1.00 128.38 ? 183 ASP A CA  1 
ATOM   1293 C C   . ASP A 1 184 ? 104.788 157.759 208.979 1.00 128.38 ? 183 ASP A C   1 
ATOM   1294 O O   . ASP A 1 184 ? 105.405 157.932 210.031 1.00 128.38 ? 183 ASP A O   1 
ATOM   1295 C CB  . ASP A 1 184 ? 105.998 158.360 206.881 1.00 128.38 ? 183 ASP A CB  1 
ATOM   1296 C CG  . ASP A 1 184 ? 105.861 159.011 205.528 1.00 128.38 ? 183 ASP A CG  1 
ATOM   1297 O OD1 . ASP A 1 184 ? 104.716 159.247 205.096 1.00 128.38 ? 183 ASP A OD1 1 
ATOM   1298 O OD2 . ASP A 1 184 ? 106.897 159.287 204.891 1.00 128.38 ? 183 ASP A OD2 1 
ATOM   1299 N N   . TYR A 1 185 ? 104.013 156.701 208.757 1.00 132.55 ? 184 TYR A N   1 
ATOM   1300 C CA  . TYR A 1 185 ? 103.826 155.679 209.775 1.00 132.55 ? 184 TYR A CA  1 
ATOM   1301 C C   . TYR A 1 185 ? 103.794 154.305 209.122 1.00 132.55 ? 184 TYR A C   1 
ATOM   1302 O O   . TYR A 1 185 ? 103.430 154.156 207.954 1.00 132.55 ? 184 TYR A O   1 
ATOM   1303 C CB  . TYR A 1 185 ? 102.544 155.914 210.581 1.00 132.55 ? 184 TYR A CB  1 
ATOM   1304 C CG  . TYR A 1 185 ? 102.330 157.353 210.986 1.00 132.55 ? 184 TYR A CG  1 
ATOM   1305 C CD1 . TYR A 1 185 ? 101.610 158.223 210.181 1.00 132.55 ? 184 TYR A CD1 1 
ATOM   1306 C CD2 . TYR A 1 185 ? 102.859 157.847 212.168 1.00 132.55 ? 184 TYR A CD2 1 
ATOM   1307 C CE1 . TYR A 1 185 ? 101.414 159.538 210.549 1.00 132.55 ? 184 TYR A CE1 1 
ATOM   1308 C CE2 . TYR A 1 185 ? 102.666 159.159 212.545 1.00 132.55 ? 184 TYR A CE2 1 
ATOM   1309 C CZ  . TYR A 1 185 ? 101.946 160.000 211.731 1.00 132.55 ? 184 TYR A CZ  1 
ATOM   1310 O OH  . TYR A 1 185 ? 101.757 161.309 212.105 1.00 132.55 ? 184 TYR A OH  1 
ATOM   1311 N N   . ALA A 1 186 ? 104.186 153.299 209.897 1.00 142.26 ? 185 ALA A N   1 
ATOM   1312 C CA  . ALA A 1 186 ? 104.167 151.928 209.413 1.00 142.26 ? 185 ALA A CA  1 
ATOM   1313 C C   . ALA A 1 186 ? 102.735 151.425 209.291 1.00 142.26 ? 185 ALA A C   1 
ATOM   1314 O O   . ALA A 1 186 ? 101.856 151.792 210.074 1.00 142.26 ? 185 ALA A O   1 
ATOM   1315 C CB  . ALA A 1 186 ? 104.962 151.017 210.346 1.00 142.26 ? 185 ALA A CB  1 
ATOM   1316 N N   . GLY A 1 187 ? 102.513 150.555 208.303 1.00 150.65 ? 186 GLY A N   1 
ATOM   1317 C CA  . GLY A 1 187 ? 101.164 150.105 208.002 1.00 150.65 ? 186 GLY A CA  1 
ATOM   1318 C C   . GLY A 1 187 ? 100.489 149.386 209.152 1.00 150.65 ? 186 GLY A C   1 
ATOM   1319 O O   . GLY A 1 187 ? 99.267  149.463 209.304 1.00 150.65 ? 186 GLY A O   1 
ATOM   1320 N N   . THR A 1 188 ? 101.267 148.680 209.973 1.00 150.78 ? 187 THR A N   1 
ATOM   1321 C CA  . THR A 1 188 ? 100.689 147.933 211.084 1.00 150.78 ? 187 THR A CA  1 
ATOM   1322 C C   . THR A 1 188 ? 100.028 148.859 212.098 1.00 150.78 ? 187 THR A C   1 
ATOM   1323 O O   . THR A 1 188 ? 98.990  148.518 212.676 1.00 150.78 ? 187 THR A O   1 
ATOM   1324 C CB  . THR A 1 188 ? 101.771 147.086 211.754 1.00 150.78 ? 187 THR A CB  1 
ATOM   1325 O OG1 . THR A 1 188 ? 102.254 146.108 210.825 1.00 150.78 ? 187 THR A OG1 1 
ATOM   1326 C CG2 . THR A 1 188 ? 101.224 146.377 212.983 1.00 150.78 ? 187 THR A CG2 1 
ATOM   1327 N N   . VAL A 1 189 ? 100.601 150.041 212.315 1.00 151.43 ? 188 VAL A N   1 
ATOM   1328 C CA  . VAL A 1 189 ? 100.198 150.916 213.408 1.00 151.43 ? 188 VAL A CA  1 
ATOM   1329 C C   . VAL A 1 189 ? 99.546  152.201 212.914 1.00 151.43 ? 188 VAL A C   1 
ATOM   1330 O O   . VAL A 1 189 ? 99.385  153.145 213.701 1.00 151.43 ? 188 VAL A O   1 
ATOM   1331 C CB  . VAL A 1 189 ? 101.404 151.224 214.320 1.00 151.43 ? 188 VAL A CB  1 
ATOM   1332 C CG1 . VAL A 1 189 ? 102.389 152.154 213.623 1.00 151.43 ? 188 VAL A CG1 1 
ATOM   1333 C CG2 . VAL A 1 189 ? 100.979 151.731 215.703 1.00 151.43 ? 188 VAL A CG2 1 
ATOM   1334 N N   . LYS A 1 190 ? 99.132  152.261 211.645 1.00 152.14 ? 189 LYS A N   1 
ATOM   1335 C CA  . LYS A 1 190 ? 98.632  153.516 211.087 1.00 152.14 ? 189 LYS A CA  1 
ATOM   1336 C C   . LYS A 1 190 ? 97.438  154.059 211.857 1.00 152.14 ? 189 LYS A C   1 
ATOM   1337 O O   . LYS A 1 190 ? 97.355  155.268 212.099 1.00 152.14 ? 189 LYS A O   1 
ATOM   1338 C CB  . LYS A 1 190 ? 98.244  153.335 209.621 1.00 152.14 ? 189 LYS A CB  1 
ATOM   1339 C CG  . LYS A 1 190 ? 99.402  153.096 208.687 1.00 152.14 ? 189 LYS A CG  1 
ATOM   1340 C CD  . LYS A 1 190 ? 98.915  152.859 207.274 1.00 152.14 ? 189 LYS A CD  1 
ATOM   1341 C CE  . LYS A 1 190 ? 98.368  154.140 206.676 1.00 152.14 ? 189 LYS A CE  1 
ATOM   1342 N NZ  . LYS A 1 190 ? 99.448  155.141 206.459 1.00 152.14 ? 189 LYS A NZ  1 
ATOM   1343 N N   . SER A 1 191 ? 96.513  153.193 212.255 1.00 155.17 ? 190 SER A N   1 
ATOM   1344 C CA  . SER A 1 191 ? 95.235  153.650 212.779 1.00 155.17 ? 190 SER A CA  1 
ATOM   1345 C C   . SER A 1 191 ? 95.322  154.247 214.177 1.00 155.17 ? 190 SER A C   1 
ATOM   1346 O O   . SER A 1 191 ? 94.378  154.926 214.594 1.00 155.17 ? 190 SER A O   1 
ATOM   1347 C CB  . SER A 1 191 ? 94.235  152.492 212.783 1.00 155.17 ? 190 SER A CB  1 
ATOM   1348 O OG  . SER A 1 191 ? 94.664  151.457 213.648 1.00 155.17 ? 190 SER A OG  1 
ATOM   1349 N N   . ARG A 1 192 ? 96.415  154.029 214.913 1.00 155.94 ? 191 ARG A N   1 
ATOM   1350 C CA  . ARG A 1 192 ? 96.410  154.424 216.316 1.00 155.94 ? 191 ARG A CA  1 
ATOM   1351 C C   . ARG A 1 192 ? 97.710  155.078 216.780 1.00 155.94 ? 191 ARG A C   1 
ATOM   1352 O O   . ARG A 1 192 ? 98.083  154.919 217.947 1.00 155.94 ? 191 ARG A O   1 
ATOM   1353 C CB  . ARG A 1 192 ? 96.109  153.215 217.208 1.00 155.94 ? 191 ARG A CB  1 
ATOM   1354 C CG  . ARG A 1 192 ? 97.120  152.092 217.100 1.00 155.94 ? 191 ARG A CG  1 
ATOM   1355 C CD  . ARG A 1 192 ? 96.895  151.058 218.185 1.00 155.94 ? 191 ARG A CD  1 
ATOM   1356 N NE  . ARG A 1 192 ? 97.891  149.995 218.138 1.00 155.94 ? 191 ARG A NE  1 
ATOM   1357 C CZ  . ARG A 1 192 ? 98.043  149.072 219.077 1.00 155.94 ? 191 ARG A CZ  1 
ATOM   1358 N NH1 . ARG A 1 192 ? 97.285  149.057 220.161 1.00 155.94 ? 191 ARG A NH1 1 
ATOM   1359 N NH2 . ARG A 1 192 ? 98.982  148.143 218.927 1.00 155.94 ? 191 ARG A NH2 1 
ATOM   1360 N N   . ILE A 1 193 ? 98.398  155.825 215.922 1.00 148.20 ? 192 ILE A N   1 
ATOM   1361 C CA  . ILE A 1 193 ? 99.683  156.422 216.266 1.00 148.20 ? 192 ILE A CA  1 
ATOM   1362 C C   . ILE A 1 193 ? 99.655  157.908 215.938 1.00 148.20 ? 192 ILE A C   1 
ATOM   1363 O O   . ILE A 1 193 ? 98.963  158.333 215.007 1.00 148.20 ? 192 ILE A O   1 
ATOM   1364 C CB  . ILE A 1 193 ? 100.839 155.717 215.528 1.00 148.20 ? 192 ILE A CB  1 
ATOM   1365 C CG1 . ILE A 1 193 ? 102.189 156.171 216.081 1.00 148.20 ? 192 ILE A CG1 1 
ATOM   1366 C CG2 . ILE A 1 193 ? 100.749 155.965 214.037 1.00 148.20 ? 192 ILE A CG2 1 
ATOM   1367 C CD1 . ILE A 1 193 ? 103.343 155.308 215.644 1.00 148.20 ? 192 ILE A CD1 1 
ATOM   1368 N N   . ALA A 1 194 ? 100.394 158.701 216.716 1.00 146.08 ? 193 ALA A N   1 
ATOM   1369 C CA  . ALA A 1 194 ? 100.546 160.121 216.431 1.00 146.08 ? 193 ALA A CA  1 
ATOM   1370 C C   . ALA A 1 194 ? 101.919 160.595 216.883 1.00 146.08 ? 193 ALA A C   1 
ATOM   1371 O O   . ALA A 1 194 ? 102.433 160.144 217.909 1.00 146.08 ? 193 ALA A O   1 
ATOM   1372 C CB  . ALA A 1 194 ? 99.456  160.949 217.118 1.00 146.08 ? 193 ALA A CB  1 
ATOM   1373 N N   . ILE A 1 195 ? 102.511 161.504 216.112 1.00 143.04 ? 194 ILE A N   1 
ATOM   1374 C CA  . ILE A 1 195 ? 103.796 162.110 216.446 1.00 143.04 ? 194 ILE A CA  1 
ATOM   1375 C C   . ILE A 1 195 ? 103.631 163.621 216.382 1.00 143.04 ? 194 ILE A C   1 
ATOM   1376 O O   . ILE A 1 195 ? 103.137 164.151 215.380 1.00 143.04 ? 194 ILE A O   1 
ATOM   1377 C CB  . ILE A 1 195 ? 104.919 161.647 215.506 1.00 143.04 ? 194 ILE A CB  1 
ATOM   1378 C CG1 . ILE A 1 195 ? 105.209 160.162 215.709 1.00 143.04 ? 194 ILE A CG1 1 
ATOM   1379 C CG2 . ILE A 1 195 ? 106.175 162.460 215.739 1.00 143.04 ? 194 ILE A CG2 1 
ATOM   1380 C CD1 . ILE A 1 195 ? 106.193 159.596 214.718 1.00 143.04 ? 194 ILE A CD1 1 
ATOM   1381 N N   . ASN A 1 196 ? 104.043 164.312 217.443 1.00 147.52 ? 195 ASN A N   1 
ATOM   1382 C CA  . ASN A 1 196 ? 103.856 165.750 217.537 1.00 147.52 ? 195 ASN A CA  1 
ATOM   1383 C C   . ASN A 1 196 ? 105.174 166.445 217.853 1.00 147.52 ? 195 ASN A C   1 
ATOM   1384 O O   . ASN A 1 196 ? 105.816 166.115 218.859 1.00 147.52 ? 195 ASN A O   1 
ATOM   1385 C CB  . ASN A 1 196 ? 102.821 166.096 218.618 1.00 147.52 ? 195 ASN A CB  1 
ATOM   1386 C CG  . ASN A 1 196 ? 101.397 165.861 218.158 1.00 147.52 ? 195 ASN A CG  1 
ATOM   1387 O OD1 . ASN A 1 196 ? 101.141 165.027 217.291 1.00 147.52 ? 195 ASN A OD1 1 
ATOM   1388 N ND2 . ASN A 1 196 ? 100.460 166.599 218.739 1.00 147.52 ? 195 ASN A ND2 1 
ATOM   1389 N N   . PRO A 1 197 ? 105.610 167.394 217.034 1.00 145.08 ? 196 PRO A N   1 
ATOM   1390 C CA  . PRO A 1 197 ? 106.791 168.191 217.366 1.00 145.08 ? 196 PRO A CA  1 
ATOM   1391 C C   . PRO A 1 197 ? 106.416 169.446 218.148 1.00 145.08 ? 196 PRO A C   1 
ATOM   1392 O O   . PRO A 1 197 ? 105.254 169.850 218.214 1.00 145.08 ? 196 PRO A O   1 
ATOM   1393 C CB  . PRO A 1 197 ? 107.354 168.552 215.989 1.00 145.08 ? 196 PRO A CB  1 
ATOM   1394 C CG  . PRO A 1 197 ? 106.148 168.646 215.127 1.00 145.08 ? 196 PRO A CG  1 
ATOM   1395 C CD  . PRO A 1 197 ? 105.132 167.665 215.668 1.00 145.08 ? 196 PRO A CD  1 
ATOM   1396 N N   . ASP A 1 198 ? 107.437 170.061 218.742 1.00 152.80 ? 197 ASP A N   1 
ATOM   1397 C CA  . ASP A 1 198 ? 107.263 171.295 219.503 1.00 152.80 ? 197 ASP A CA  1 
ATOM   1398 C C   . ASP A 1 198 ? 108.560 172.082 219.401 1.00 152.80 ? 197 ASP A C   1 
ATOM   1399 O O   . ASP A 1 198 ? 109.538 171.765 220.088 1.00 152.80 ? 197 ASP A O   1 
ATOM   1400 C CB  . ASP A 1 198 ? 106.906 171.004 220.959 1.00 152.80 ? 197 ASP A CB  1 
ATOM   1401 C CG  . ASP A 1 198 ? 106.462 172.245 221.712 1.00 152.80 ? 197 ASP A CG  1 
ATOM   1402 O OD1 . ASP A 1 198 ? 106.487 173.346 221.124 1.00 152.80 ? 197 ASP A OD1 1 
ATOM   1403 O OD2 . ASP A 1 198 ? 106.075 172.117 222.892 1.00 152.80 ? 197 ASP A OD2 1 
ATOM   1404 N N   . THR A 1 199 ? 108.566 173.100 218.537 1.00 152.69 ? 198 THR A N   1 
ATOM   1405 C CA  . THR A 1 199 ? 109.765 173.899 218.317 1.00 152.69 ? 198 THR A CA  1 
ATOM   1406 C C   . THR A 1 199 ? 110.030 174.867 219.460 1.00 152.69 ? 198 THR A C   1 
ATOM   1407 O O   . THR A 1 199 ? 111.178 175.277 219.661 1.00 152.69 ? 198 THR A O   1 
ATOM   1408 C CB  . THR A 1 199 ? 109.650 174.673 217.004 1.00 152.69 ? 198 THR A CB  1 
ATOM   1409 O OG1 . THR A 1 199 ? 108.418 175.405 216.989 1.00 152.69 ? 198 THR A OG1 1 
ATOM   1410 C CG2 . THR A 1 199 ? 109.679 173.720 215.821 1.00 152.69 ? 198 THR A CG2 1 
ATOM   1411 N N   . SER A 1 200 ? 108.993 175.247 220.208 1.00 155.59 ? 199 SER A N   1 
ATOM   1412 C CA  . SER A 1 200 ? 109.176 176.195 221.302 1.00 155.59 ? 199 SER A CA  1 
ATOM   1413 C C   . SER A 1 200 ? 110.128 175.637 222.352 1.00 155.59 ? 199 SER A C   1 
ATOM   1414 O O   . SER A 1 200 ? 111.018 176.342 222.839 1.00 155.59 ? 199 SER A O   1 
ATOM   1415 C CB  . SER A 1 200 ? 107.824 176.540 221.925 1.00 155.59 ? 199 SER A CB  1 
ATOM   1416 O OG  . SER A 1 200 ? 107.182 175.378 222.420 1.00 155.59 ? 199 SER A OG  1 
ATOM   1417 N N   . LYS A 1 201 ? 109.954 174.368 222.710 1.00 154.38 ? 200 LYS A N   1 
ATOM   1418 C CA  . LYS A 1 201 ? 110.851 173.678 223.624 1.00 154.38 ? 200 LYS A CA  1 
ATOM   1419 C C   . LYS A 1 201 ? 111.690 172.610 222.933 1.00 154.38 ? 200 LYS A C   1 
ATOM   1420 O O   . LYS A 1 201 ? 112.377 171.841 223.614 1.00 154.38 ? 200 LYS A O   1 
ATOM   1421 C CB  . LYS A 1 201 ? 110.051 173.094 224.791 1.00 154.38 ? 200 LYS A CB  1 
ATOM   1422 C CG  . LYS A 1 201 ? 108.883 172.206 224.393 1.00 154.38 ? 200 LYS A CG  1 
ATOM   1423 C CD  . LYS A 1 201 ? 108.571 171.174 225.463 1.00 154.38 ? 200 LYS A CD  1 
ATOM   1424 C CE  . LYS A 1 201 ? 107.585 170.129 224.963 1.00 154.38 ? 200 LYS A CE  1 
ATOM   1425 N NZ  . LYS A 1 201 ? 108.105 169.332 223.828 1.00 154.38 ? 200 LYS A NZ  1 
ATOM   1426 N N   . ASN A 1 202 ? 111.652 172.554 221.598 1.00 147.52 ? 201 ASN A N   1 
ATOM   1427 C CA  . ASN A 1 202 ? 112.600 171.770 220.801 1.00 147.52 ? 201 ASN A CA  1 
ATOM   1428 C C   . ASN A 1 202 ? 112.561 170.286 221.155 1.00 147.52 ? 201 ASN A C   1 
ATOM   1429 O O   . ASN A 1 202 ? 113.572 169.688 221.527 1.00 147.52 ? 201 ASN A O   1 
ATOM   1430 C CB  . ASN A 1 202 ? 114.018 172.323 220.954 1.00 147.52 ? 201 ASN A CB  1 
ATOM   1431 C CG  . ASN A 1 202 ? 114.910 171.966 219.787 1.00 147.52 ? 201 ASN A CG  1 
ATOM   1432 O OD1 . ASN A 1 202 ? 114.463 171.916 218.643 1.00 147.52 ? 201 ASN A OD1 1 
ATOM   1433 N ND2 . ASN A 1 202 ? 116.180 171.711 220.071 1.00 147.52 ? 201 ASN A ND2 1 
ATOM   1434 N N   . GLN A 1 203 ? 111.380 169.682 221.033 1.00 147.29 ? 202 GLN A N   1 
ATOM   1435 C CA  . GLN A 1 203 ? 111.219 168.265 221.330 1.00 147.29 ? 202 GLN A CA  1 
ATOM   1436 C C   . GLN A 1 203 ? 110.233 167.652 220.349 1.00 147.29 ? 202 GLN A C   1 
ATOM   1437 O O   . GLN A 1 203 ? 109.599 168.347 219.555 1.00 147.29 ? 202 GLN A O   1 
ATOM   1438 C CB  . GLN A 1 203 ? 110.737 168.037 222.767 1.00 147.29 ? 202 GLN A CB  1 
ATOM   1439 C CG  . GLN A 1 203 ? 111.633 168.624 223.840 1.00 147.29 ? 202 GLN A CG  1 
ATOM   1440 C CD  . GLN A 1 203 ? 111.047 168.484 225.228 1.00 147.29 ? 202 GLN A CD  1 
ATOM   1441 O OE1 . GLN A 1 203 ? 109.908 168.051 225.391 1.00 147.29 ? 202 GLN A OE1 1 
ATOM   1442 N NE2 . GLN A 1 203 ? 111.824 168.852 226.238 1.00 147.29 ? 202 GLN A NE2 1 
ATOM   1443 N N   . PHE A 1 204 ? 110.116 166.328 220.402 1.00 138.34 ? 203 PHE A N   1 
ATOM   1444 C CA  . PHE A 1 204 ? 109.073 165.627 219.671 1.00 138.34 ? 203 PHE A CA  1 
ATOM   1445 C C   . PHE A 1 204 ? 108.592 164.451 220.507 1.00 138.34 ? 203 PHE A C   1 
ATOM   1446 O O   . PHE A 1 204 ? 109.373 163.800 221.209 1.00 138.34 ? 203 PHE A O   1 
ATOM   1447 C CB  . PHE A 1 204 ? 109.544 165.163 218.284 1.00 138.34 ? 203 PHE A CB  1 
ATOM   1448 C CG  . PHE A 1 204 ? 110.637 164.141 218.314 1.00 138.34 ? 203 PHE A CG  1 
ATOM   1449 C CD1 . PHE A 1 204 ? 110.343 162.793 218.251 1.00 138.34 ? 203 PHE A CD1 1 
ATOM   1450 C CD2 . PHE A 1 204 ? 111.961 164.529 218.389 1.00 138.34 ? 203 PHE A CD2 1 
ATOM   1451 C CE1 . PHE A 1 204 ? 111.349 161.852 218.271 1.00 138.34 ? 203 PHE A CE1 1 
ATOM   1452 C CE2 . PHE A 1 204 ? 112.971 163.590 218.410 1.00 138.34 ? 203 PHE A CE2 1 
ATOM   1453 C CZ  . PHE A 1 204 ? 112.664 162.251 218.351 1.00 138.34 ? 203 PHE A CZ  1 
ATOM   1454 N N   . SER A 1 205 ? 107.292 164.190 220.426 1.00 145.78 ? 204 SER A N   1 
ATOM   1455 C CA  . SER A 1 205 ? 106.628 163.242 221.300 1.00 145.78 ? 204 SER A CA  1 
ATOM   1456 C C   . SER A 1 205 ? 105.819 162.250 220.477 1.00 145.78 ? 204 SER A C   1 
ATOM   1457 O O   . SER A 1 205 ? 105.354 162.546 219.372 1.00 145.78 ? 204 SER A O   1 
ATOM   1458 C CB  . SER A 1 205 ? 105.721 163.961 222.304 1.00 145.78 ? 204 SER A CB  1 
ATOM   1459 O OG  . SER A 1 205 ? 104.816 164.823 221.638 1.00 145.78 ? 204 SER A OG  1 
ATOM   1460 N N   . LEU A 1 206 ? 105.651 161.065 221.053 1.00 143.38 ? 205 LEU A N   1 
ATOM   1461 C CA  . LEU A 1 206 ? 104.910 159.965 220.457 1.00 143.38 ? 205 LEU A CA  1 
ATOM   1462 C C   . LEU A 1 206 ? 103.715 159.625 221.334 1.00 143.38 ? 205 LEU A C   1 
ATOM   1463 O O   . LEU A 1 206 ? 103.843 159.523 222.560 1.00 143.38 ? 205 LEU A O   1 
ATOM   1464 C CB  . LEU A 1 206 ? 105.798 158.733 220.289 1.00 143.38 ? 205 LEU A CB  1 
ATOM   1465 C CG  . LEU A 1 206 ? 105.121 157.478 219.743 1.00 143.38 ? 205 LEU A CG  1 
ATOM   1466 C CD1 . LEU A 1 206 ? 104.634 157.710 218.330 1.00 143.38 ? 205 LEU A CD1 1 
ATOM   1467 C CD2 . LEU A 1 206 ? 106.068 156.297 219.792 1.00 143.38 ? 205 LEU A CD2 1 
ATOM   1468 N N   . HIS A 1 207 ? 102.557 159.444 220.697 1.00 149.27 ? 206 HIS A N   1 
ATOM   1469 C CA  . HIS A 1 207 ? 101.309 159.164 221.391 1.00 149.27 ? 206 HIS A CA  1 
ATOM   1470 C C   . HIS A 1 207 ? 100.630 157.958 220.761 1.00 149.27 ? 206 HIS A C   1 
ATOM   1471 O O   . HIS A 1 207 ? 100.556 157.849 219.531 1.00 149.27 ? 206 HIS A O   1 
ATOM   1472 C CB  . HIS A 1 207 ? 100.364 160.369 221.344 1.00 149.27 ? 206 HIS A CB  1 
ATOM   1473 C CG  . HIS A 1 207 ? 100.831 161.537 222.153 1.00 149.27 ? 206 HIS A CG  1 
ATOM   1474 N ND1 . HIS A 1 207 ? 100.664 161.610 223.519 1.00 149.27 ? 206 HIS A ND1 1 
ATOM   1475 C CD2 . HIS A 1 207 ? 101.449 162.684 221.788 1.00 149.27 ? 206 HIS A CD2 1 
ATOM   1476 C CE1 . HIS A 1 207 ? 101.165 162.749 223.961 1.00 149.27 ? 206 HIS A CE1 1 
ATOM   1477 N NE2 . HIS A 1 207 ? 101.647 163.420 222.930 1.00 149.27 ? 206 HIS A NE2 1 
ATOM   1478 N N   . LEU A 1 208 ? 100.137 157.063 221.612 1.00 158.31 ? 207 LEU A N   1 
ATOM   1479 C CA  . LEU A 1 208 ? 99.343  155.907 221.206 1.00 158.31 ? 207 LEU A CA  1 
ATOM   1480 C C   . LEU A 1 208 ? 98.043  155.937 221.999 1.00 158.31 ? 207 LEU A C   1 
ATOM   1481 O O   . LEU A 1 208 ? 98.058  155.801 223.227 1.00 158.31 ? 207 LEU A O   1 
ATOM   1482 C CB  . LEU A 1 208 ? 100.102 154.605 221.447 1.00 158.31 ? 207 LEU A CB  1 
ATOM   1483 C CG  . LEU A 1 208 ? 101.350 154.373 220.599 1.00 158.31 ? 207 LEU A CG  1 
ATOM   1484 C CD1 . LEU A 1 208 ? 102.007 153.058 220.975 1.00 158.31 ? 207 LEU A CD1 1 
ATOM   1485 C CD2 . LEU A 1 208 ? 101.008 154.399 219.125 1.00 158.31 ? 207 LEU A CD2 1 
ATOM   1486 N N   . ASN A 1 209 ? 96.921  156.119 221.303 1.00 167.25 ? 208 ASN A N   1 
ATOM   1487 C CA  . ASN A 1 209 ? 95.638  156.236 221.990 1.00 167.25 ? 208 ASN A CA  1 
ATOM   1488 C C   . ASN A 1 209 ? 95.254  154.941 222.698 1.00 167.25 ? 208 ASN A C   1 
ATOM   1489 O O   . ASN A 1 209 ? 94.770  154.971 223.835 1.00 167.25 ? 208 ASN A O   1 
ATOM   1490 C CB  . ASN A 1 209 ? 94.553  156.646 221.000 1.00 167.25 ? 208 ASN A CB  1 
ATOM   1491 C CG  . ASN A 1 209 ? 94.554  155.787 219.761 1.00 167.25 ? 208 ASN A CG  1 
ATOM   1492 O OD1 . ASN A 1 209 ? 95.600  155.563 219.160 1.00 167.25 ? 208 ASN A OD1 1 
ATOM   1493 N ND2 . ASN A 1 209 ? 93.385  155.292 219.377 1.00 167.25 ? 208 ASN A ND2 1 
ATOM   1494 N N   . SER A 1 210 ? 95.453  153.799 222.048 1.00 165.92 ? 209 SER A N   1 
ATOM   1495 C CA  . SER A 1 210 ? 95.064  152.510 222.600 1.00 165.92 ? 209 SER A CA  1 
ATOM   1496 C C   . SER A 1 210 ? 96.270  151.586 222.648 1.00 165.92 ? 209 SER A C   1 
ATOM   1497 O O   . SER A 1 210 ? 97.116  151.606 221.750 1.00 165.92 ? 209 SER A O   1 
ATOM   1498 C CB  . SER A 1 210 ? 93.950  151.866 221.776 1.00 165.92 ? 209 SER A CB  1 
ATOM   1499 O OG  . SER A 1 210 ? 93.621  150.589 222.291 1.00 165.92 ? 209 SER A OG  1 
ATOM   1500 N N   . VAL A 1 211 ? 96.336  150.766 223.697 1.00 169.73 ? 210 VAL A N   1 
ATOM   1501 C CA  . VAL A 1 211 ? 97.477  149.896 223.935 1.00 169.73 ? 210 VAL A CA  1 
ATOM   1502 C C   . VAL A 1 211 ? 96.972  148.475 224.157 1.00 169.73 ? 210 VAL A C   1 
ATOM   1503 O O   . VAL A 1 211 ? 95.835  148.251 224.579 1.00 169.73 ? 210 VAL A O   1 
ATOM   1504 C CB  . VAL A 1 211 ? 98.321  150.381 225.136 1.00 169.73 ? 210 VAL A CB  1 
ATOM   1505 C CG1 . VAL A 1 211 ? 97.525  150.288 226.425 1.00 169.73 ? 210 VAL A CG1 1 
ATOM   1506 C CG2 . VAL A 1 211 ? 99.638  149.629 225.233 1.00 169.73 ? 210 VAL A CG2 1 
ATOM   1507 N N   . THR A 1 212 ? 97.837  147.514 223.864 1.00 169.20 ? 211 THR A N   1 
ATOM   1508 C CA  . THR A 1 212 ? 97.523  146.096 223.919 1.00 169.20 ? 211 THR A CA  1 
ATOM   1509 C C   . THR A 1 212 ? 98.646  145.375 224.648 1.00 169.20 ? 211 THR A C   1 
ATOM   1510 O O   . THR A 1 212 ? 99.763  145.895 224.744 1.00 169.20 ? 211 THR A O   1 
ATOM   1511 C CB  . THR A 1 212 ? 97.343  145.516 222.510 1.00 169.20 ? 211 THR A CB  1 
ATOM   1512 O OG1 . THR A 1 212 ? 98.372  146.020 221.650 1.00 169.20 ? 211 THR A OG1 1 
ATOM   1513 C CG2 . THR A 1 212 ? 95.989  145.906 221.948 1.00 169.20 ? 211 THR A CG2 1 
ATOM   1514 N N   . PRO A 1 213 ? 98.376  144.182 225.190 1.00 166.83 ? 212 PRO A N   1 
ATOM   1515 C CA  . PRO A 1 213 ? 99.407  143.491 225.984 1.00 166.83 ? 212 PRO A CA  1 
ATOM   1516 C C   . PRO A 1 213 ? 100.699 143.222 225.235 1.00 166.83 ? 212 PRO A C   1 
ATOM   1517 O O   . PRO A 1 213 ? 101.775 143.284 225.842 1.00 166.83 ? 212 PRO A O   1 
ATOM   1518 C CB  . PRO A 1 213 ? 98.713  142.185 226.387 1.00 166.83 ? 212 PRO A CB  1 
ATOM   1519 C CG  . PRO A 1 213 ? 97.272  142.521 226.392 1.00 166.83 ? 212 PRO A CG  1 
ATOM   1520 C CD  . PRO A 1 213 ? 97.075  143.497 225.271 1.00 166.83 ? 212 PRO A CD  1 
ATOM   1521 N N   . GLU A 1 214 ? 100.634 142.929 223.936 1.00 167.55 ? 213 GLU A N   1 
ATOM   1522 C CA  . GLU A 1 214 ? 101.842 142.621 223.179 1.00 167.55 ? 213 GLU A CA  1 
ATOM   1523 C C   . GLU A 1 214 ? 102.725 143.840 222.953 1.00 167.55 ? 213 GLU A C   1 
ATOM   1524 O O   . GLU A 1 214 ? 103.851 143.685 222.468 1.00 167.55 ? 213 GLU A O   1 
ATOM   1525 C CB  . GLU A 1 214 ? 101.474 142.002 221.832 1.00 167.55 ? 213 GLU A CB  1 
ATOM   1526 C CG  . GLU A 1 214 ? 100.812 142.973 220.875 1.00 167.55 ? 213 GLU A CG  1 
ATOM   1527 C CD  . GLU A 1 214 ? 99.320  143.083 221.101 1.00 167.55 ? 213 GLU A CD  1 
ATOM   1528 O OE1 . GLU A 1 214 ? 98.844  142.648 222.171 1.00 167.55 ? 213 GLU A OE1 1 
ATOM   1529 O OE2 . GLU A 1 214 ? 98.621  143.613 220.213 1.00 167.55 ? 213 GLU A OE2 1 
ATOM   1530 N N   . ASP A 1 215 ? 102.248 145.039 223.287 1.00 165.07 ? 214 ASP A N   1 
ATOM   1531 C CA  . ASP A 1 215 ? 102.999 146.258 223.023 1.00 165.07 ? 214 ASP A CA  1 
ATOM   1532 C C   . ASP A 1 215 ? 104.221 146.414 223.917 1.00 165.07 ? 214 ASP A C   1 
ATOM   1533 O O   . ASP A 1 215 ? 105.021 147.324 223.678 1.00 165.07 ? 214 ASP A O   1 
ATOM   1534 C CB  . ASP A 1 215 ? 102.083 147.469 223.184 1.00 165.07 ? 214 ASP A CB  1 
ATOM   1535 C CG  . ASP A 1 215 ? 101.032 147.543 222.101 1.00 165.07 ? 214 ASP A CG  1 
ATOM   1536 O OD1 . ASP A 1 215 ? 101.300 147.059 220.982 1.00 165.07 ? 214 ASP A OD1 1 
ATOM   1537 O OD2 . ASP A 1 215 ? 99.935  148.076 222.367 1.00 165.07 ? 214 ASP A OD2 1 
ATOM   1538 N N   . THR A 1 216 ? 104.377 145.567 224.935 1.00 164.61 ? 215 THR A N   1 
ATOM   1539 C CA  . THR A 1 216 ? 105.533 145.620 225.823 1.00 164.61 ? 215 THR A CA  1 
ATOM   1540 C C   . THR A 1 216 ? 106.830 145.539 225.028 1.00 164.61 ? 215 THR A C   1 
ATOM   1541 O O   . THR A 1 216 ? 107.104 144.521 224.386 1.00 164.61 ? 215 THR A O   1 
ATOM   1542 C CB  . THR A 1 216 ? 105.471 144.482 226.844 1.00 164.61 ? 215 THR A CB  1 
ATOM   1543 O OG1 . THR A 1 216 ? 104.391 144.713 227.756 1.00 164.61 ? 215 THR A OG1 1 
ATOM   1544 C CG2 . THR A 1 216 ? 106.776 144.384 227.619 1.00 164.61 ? 215 THR A CG2 1 
ATOM   1545 N N   . ALA A 1 217 ? 107.631 146.601 225.064 1.00 150.58 ? 216 ALA A N   1 
ATOM   1546 C CA  . ALA A 1 217 ? 108.837 146.666 224.246 1.00 150.58 ? 216 ALA A CA  1 
ATOM   1547 C C   . ALA A 1 217 ? 109.689 147.830 224.728 1.00 150.58 ? 216 ALA A C   1 
ATOM   1548 O O   . ALA A 1 217 ? 109.275 148.612 225.586 1.00 150.58 ? 216 ALA A O   1 
ATOM   1549 C CB  . ALA A 1 217 ? 108.500 146.820 222.761 1.00 150.58 ? 216 ALA A CB  1 
ATOM   1550 N N   . VAL A 1 218 ? 110.884 147.945 224.154 1.00 139.86 ? 217 VAL A N   1 
ATOM   1551 C CA  . VAL A 1 218 ? 111.820 149.012 224.491 1.00 139.86 ? 217 VAL A CA  1 
ATOM   1552 C C   . VAL A 1 218 ? 111.899 149.969 223.312 1.00 139.86 ? 217 VAL A C   1 
ATOM   1553 O O   . VAL A 1 218 ? 112.087 149.540 222.169 1.00 139.86 ? 217 VAL A O   1 
ATOM   1554 C CB  . VAL A 1 218 ? 113.207 148.457 224.847 1.00 139.86 ? 217 VAL A CB  1 
ATOM   1555 C CG1 . VAL A 1 218 ? 114.125 149.583 225.275 1.00 139.86 ? 217 VAL A CG1 1 
ATOM   1556 C CG2 . VAL A 1 218 ? 113.088 147.419 225.945 1.00 139.86 ? 217 VAL A CG2 1 
ATOM   1557 N N   . TYR A 1 219 ? 111.766 151.261 223.589 1.00 136.18 ? 218 TYR A N   1 
ATOM   1558 C CA  . TYR A 1 219 ? 111.629 152.280 222.562 1.00 136.18 ? 218 TYR A CA  1 
ATOM   1559 C C   . TYR A 1 219 ? 112.848 153.192 222.540 1.00 136.18 ? 218 TYR A C   1 
ATOM   1560 O O   . TYR A 1 219 ? 113.386 153.558 223.593 1.00 136.18 ? 218 TYR A O   1 
ATOM   1561 C CB  . TYR A 1 219 ? 110.362 153.108 222.790 1.00 136.18 ? 218 TYR A CB  1 
ATOM   1562 C CG  . TYR A 1 219 ? 109.080 152.315 222.659 1.00 136.18 ? 218 TYR A CG  1 
ATOM   1563 C CD1 . TYR A 1 219 ? 108.634 151.501 223.691 1.00 136.18 ? 218 TYR A CD1 1 
ATOM   1564 C CD2 . TYR A 1 219 ? 108.317 152.380 221.504 1.00 136.18 ? 218 TYR A CD2 1 
ATOM   1565 C CE1 . TYR A 1 219 ? 107.469 150.775 223.574 1.00 136.18 ? 218 TYR A CE1 1 
ATOM   1566 C CE2 . TYR A 1 219 ? 107.150 151.658 221.379 1.00 136.18 ? 218 TYR A CE2 1 
ATOM   1567 C CZ  . TYR A 1 219 ? 106.732 150.858 222.415 1.00 136.18 ? 218 TYR A CZ  1 
ATOM   1568 O OH  . TYR A 1 219 ? 105.569 150.138 222.290 1.00 136.18 ? 218 TYR A OH  1 
ATOM   1569 N N   . PHE A 1 220 ? 113.272 153.548 221.325 1.00 128.48 ? 219 PHE A N   1 
ATOM   1570 C CA  . PHE A 1 220 ? 114.354 154.485 221.071 1.00 128.48 ? 219 PHE A CA  1 
ATOM   1571 C C   . PHE A 1 220 ? 113.878 155.552 220.095 1.00 128.48 ? 219 PHE A C   1 
ATOM   1572 O O   . PHE A 1 220 ? 113.011 155.304 219.251 1.00 128.48 ? 219 PHE A O   1 
ATOM   1573 C CB  . PHE A 1 220 ? 115.590 153.799 220.474 1.00 128.48 ? 219 PHE A CB  1 
ATOM   1574 C CG  . PHE A 1 220 ? 116.035 152.577 221.215 1.00 128.48 ? 219 PHE A CG  1 
ATOM   1575 C CD1 . PHE A 1 220 ? 116.785 152.686 222.368 1.00 128.48 ? 219 PHE A CD1 1 
ATOM   1576 C CD2 . PHE A 1 220 ? 115.733 151.318 220.739 1.00 128.48 ? 219 PHE A CD2 1 
ATOM   1577 C CE1 . PHE A 1 220 ? 117.201 151.564 223.045 1.00 128.48 ? 219 PHE A CE1 1 
ATOM   1578 C CE2 . PHE A 1 220 ? 116.150 150.193 221.411 1.00 128.48 ? 219 PHE A CE2 1 
ATOM   1579 C CZ  . PHE A 1 220 ? 116.884 150.316 222.565 1.00 128.48 ? 219 PHE A CZ  1 
ATOM   1580 N N   . CYS A 1 221 ? 114.462 156.742 220.211 1.00 128.75 ? 220 CYS A N   1 
ATOM   1581 C CA  . CYS A 1 221 ? 114.263 157.822 219.255 1.00 128.75 ? 220 CYS A CA  1 
ATOM   1582 C C   . CYS A 1 221 ? 115.587 158.099 218.561 1.00 128.75 ? 220 CYS A C   1 
ATOM   1583 O O   . CYS A 1 221 ? 116.627 158.176 219.220 1.00 128.75 ? 220 CYS A O   1 
ATOM   1584 C CB  . CYS A 1 221 ? 113.734 159.085 219.940 1.00 128.75 ? 220 CYS A CB  1 
ATOM   1585 S SG  . CYS A 1 221 ? 114.577 159.535 221.474 1.00 128.75 ? 220 CYS A SG  1 
ATOM   1586 N N   . ALA A 1 222 ? 115.551 158.245 217.240 1.00 112.79 ? 221 ALA A N   1 
ATOM   1587 C CA  . ALA A 1 222 ? 116.768 158.302 216.445 1.00 112.79 ? 221 ALA A CA  1 
ATOM   1588 C C   . ALA A 1 222 ? 116.703 159.426 215.423 1.00 112.79 ? 221 ALA A C   1 
ATOM   1589 O O   . ALA A 1 222 ? 115.624 159.848 214.991 1.00 112.79 ? 221 ALA A O   1 
ATOM   1590 C CB  . ALA A 1 222 ? 117.020 156.975 215.730 1.00 112.79 ? 221 ALA A CB  1 
ATOM   1591 N N   . ARG A 1 223 ? 117.886 159.896 215.032 1.00 104.66 ? 222 ARG A N   1 
ATOM   1592 C CA  . ARG A 1 223 ? 118.037 160.952 214.039 1.00 104.66 ? 222 ARG A CA  1 
ATOM   1593 C C   . ARG A 1 223 ? 118.657 160.389 212.769 1.00 104.66 ? 222 ARG A C   1 
ATOM   1594 O O   . ARG A 1 223 ? 119.550 159.542 212.833 1.00 104.66 ? 222 ARG A O   1 
ATOM   1595 C CB  . ARG A 1 223 ? 118.913 162.085 214.574 1.00 104.66 ? 222 ARG A CB  1 
ATOM   1596 C CG  . ARG A 1 223 ? 118.986 163.284 213.651 1.00 104.66 ? 222 ARG A CG  1 
ATOM   1597 C CD  . ARG A 1 223 ? 120.121 164.214 214.029 1.00 104.66 ? 222 ARG A CD  1 
ATOM   1598 N NE  . ARG A 1 223 ? 121.394 163.775 213.473 1.00 104.66 ? 222 ARG A NE  1 
ATOM   1599 C CZ  . ARG A 1 223 ? 122.490 164.520 213.435 1.00 104.66 ? 222 ARG A CZ  1 
ATOM   1600 N NH1 . ARG A 1 223 ? 122.504 165.754 213.910 1.00 104.66 ? 222 ARG A NH1 1 
ATOM   1601 N NH2 . ARG A 1 223 ? 123.600 164.014 212.905 1.00 104.66 ? 222 ARG A NH2 1 
ATOM   1602 N N   . VAL A 1 224 ? 118.192 160.861 211.613 1.00 104.66 ? 223 VAL A N   1 
ATOM   1603 C CA  . VAL A 1 224 ? 118.722 160.416 210.329 1.00 104.66 ? 223 VAL A CA  1 
ATOM   1604 C C   . VAL A 1 224 ? 119.099 161.624 209.489 1.00 104.66 ? 223 VAL A C   1 
ATOM   1605 O O   . VAL A 1 224 ? 118.320 162.577 209.378 1.00 104.66 ? 223 VAL A O   1 
ATOM   1606 C CB  . VAL A 1 224 ? 117.721 159.528 209.574 1.00 104.66 ? 223 VAL A CB  1 
ATOM   1607 C CG1 . VAL A 1 224 ? 118.205 159.277 208.164 1.00 104.66 ? 223 VAL A CG1 1 
ATOM   1608 C CG2 . VAL A 1 224 ? 117.577 158.218 210.291 1.00 104.66 ? 223 VAL A CG2 1 
ATOM   1609 N N   . ILE A 1 225 ? 120.288 161.575 208.892 1.00 104.66 ? 224 ILE A N   1 
ATOM   1610 C CA  . ILE A 1 225 ? 120.798 162.621 208.015 1.00 104.66 ? 224 ILE A CA  1 
ATOM   1611 C C   . ILE A 1 225 ? 120.755 162.106 206.585 1.00 104.66 ? 224 ILE A C   1 
ATOM   1612 O O   . ILE A 1 225 ? 121.257 161.014 206.297 1.00 104.66 ? 224 ILE A O   1 
ATOM   1613 C CB  . ILE A 1 225 ? 122.225 163.034 208.405 1.00 104.66 ? 224 ILE A CB  1 
ATOM   1614 C CG1 . ILE A 1 225 ? 122.264 163.474 209.865 1.00 104.66 ? 224 ILE A CG1 1 
ATOM   1615 C CG2 . ILE A 1 225 ? 122.711 164.147 207.508 1.00 104.66 ? 224 ILE A CG2 1 
ATOM   1616 C CD1 . ILE A 1 225 ? 121.463 164.716 210.139 1.00 104.66 ? 224 ILE A CD1 1 
ATOM   1617 N N   . SER A 1 226 ? 120.169 162.899 205.688 1.00 104.66 ? 225 SER A N   1 
ATOM   1618 C CA  . SER A 1 226 ? 119.909 162.425 204.333 1.00 104.66 ? 225 SER A CA  1 
ATOM   1619 C C   . SER A 1 226 ? 121.194 162.239 203.538 1.00 104.66 ? 225 SER A C   1 
ATOM   1620 O O   . SER A 1 226 ? 121.266 161.365 202.668 1.00 104.66 ? 225 SER A O   1 
ATOM   1621 C CB  . SER A 1 226 ? 118.977 163.395 203.615 1.00 104.66 ? 225 SER A CB  1 
ATOM   1622 O OG  . SER A 1 226 ? 119.494 164.711 203.661 1.00 104.66 ? 225 SER A OG  1 
ATOM   1623 N N   . VAL A 1 227 ? 122.214 163.058 203.800 1.00 104.66 ? 226 VAL A N   1 
ATOM   1624 C CA  . VAL A 1 227 ? 123.449 162.963 203.024 1.00 104.66 ? 226 VAL A CA  1 
ATOM   1625 C C   . VAL A 1 227 ? 124.375 161.862 203.507 1.00 104.66 ? 226 VAL A C   1 
ATOM   1626 O O   . VAL A 1 227 ? 125.390 161.593 202.855 1.00 104.66 ? 226 VAL A O   1 
ATOM   1627 C CB  . VAL A 1 227 ? 124.227 164.291 203.035 1.00 104.66 ? 226 VAL A CB  1 
ATOM   1628 C CG1 . VAL A 1 227 ? 123.372 165.404 202.476 1.00 104.66 ? 226 VAL A CG1 1 
ATOM   1629 C CG2 . VAL A 1 227 ? 124.680 164.624 204.438 1.00 104.66 ? 226 VAL A CG2 1 
ATOM   1630 N N   . ALA A 1 228 ? 124.061 161.213 204.624 1.00 104.66 ? 227 ALA A N   1 
ATOM   1631 C CA  . ALA A 1 228 ? 124.904 160.161 205.185 1.00 104.66 ? 227 ALA A CA  1 
ATOM   1632 C C   . ALA A 1 228 ? 124.342 158.775 204.914 1.00 104.66 ? 227 ALA A C   1 
ATOM   1633 O O   . ALA A 1 228 ? 124.437 157.883 205.758 1.00 104.66 ? 227 ALA A O   1 
ATOM   1634 C CB  . ALA A 1 228 ? 125.094 160.377 206.681 1.00 104.66 ? 227 ALA A CB  1 
ATOM   1635 N N   . GLY A 1 229 ? 123.744 158.565 203.746 1.00 104.66 ? 228 GLY A N   1 
ATOM   1636 C CA  . GLY A 1 229 ? 123.244 157.250 203.406 1.00 104.66 ? 228 GLY A CA  1 
ATOM   1637 C C   . GLY A 1 229 ? 121.995 156.828 204.140 1.00 104.66 ? 228 GLY A C   1 
ATOM   1638 O O   . GLY A 1 229 ? 121.719 155.631 204.226 1.00 104.66 ? 228 GLY A O   1 
ATOM   1639 N N   . TYR A 1 230 ? 121.230 157.780 204.672 1.00 104.66 ? 229 TYR A N   1 
ATOM   1640 C CA  . TYR A 1 230 ? 119.975 157.494 205.366 1.00 104.66 ? 229 TYR A CA  1 
ATOM   1641 C C   . TYR A 1 230 ? 120.178 156.500 206.505 1.00 104.66 ? 229 TYR A C   1 
ATOM   1642 O O   . TYR A 1 230 ? 119.355 155.613 206.729 1.00 104.66 ? 229 TYR A O   1 
ATOM   1643 C CB  . TYR A 1 230 ? 118.912 156.981 204.397 1.00 104.66 ? 229 TYR A CB  1 
ATOM   1644 C CG  . TYR A 1 230 ? 118.359 158.022 203.459 1.00 104.66 ? 229 TYR A CG  1 
ATOM   1645 C CD1 . TYR A 1 230 ? 117.453 158.971 203.902 1.00 104.66 ? 229 TYR A CD1 1 
ATOM   1646 C CD2 . TYR A 1 230 ? 118.725 158.042 202.125 1.00 104.66 ? 229 TYR A CD2 1 
ATOM   1647 C CE1 . TYR A 1 230 ? 116.938 159.918 203.045 1.00 104.66 ? 229 TYR A CE1 1 
ATOM   1648 C CE2 . TYR A 1 230 ? 118.215 158.984 201.261 1.00 104.66 ? 229 TYR A CE2 1 
ATOM   1649 C CZ  . TYR A 1 230 ? 117.323 159.919 201.727 1.00 104.66 ? 229 TYR A CZ  1 
ATOM   1650 O OH  . TYR A 1 230 ? 116.814 160.861 200.867 1.00 104.66 ? 229 TYR A OH  1 
ATOM   1651 N N   . ALA A 1 231 ? 121.278 156.645 207.233 1.00 104.66 ? 230 ALA A N   1 
ATOM   1652 C CA  . ALA A 1 231 ? 121.620 155.738 208.316 1.00 104.66 ? 230 ALA A CA  1 
ATOM   1653 C C   . ALA A 1 231 ? 121.310 156.382 209.657 1.00 104.66 ? 230 ALA A C   1 
ATOM   1654 O O   . ALA A 1 231 ? 121.478 157.592 209.828 1.00 104.66 ? 230 ALA A O   1 
ATOM   1655 C CB  . ALA A 1 231 ? 123.095 155.347 208.260 1.00 104.66 ? 230 ALA A CB  1 
ATOM   1656 N N   . PHE A 1 232 ? 120.870 155.567 210.609 1.00 104.66 ? 231 PHE A N   1 
ATOM   1657 C CA  . PHE A 1 232 ? 120.517 156.053 211.940 1.00 104.66 ? 231 PHE A CA  1 
ATOM   1658 C C   . PHE A 1 232 ? 121.790 156.466 212.661 1.00 104.66 ? 231 PHE A C   1 
ATOM   1659 O O   . PHE A 1 232 ? 122.493 155.634 213.234 1.00 104.66 ? 231 PHE A O   1 
ATOM   1660 C CB  . PHE A 1 232 ? 119.772 154.974 212.713 1.00 104.66 ? 231 PHE A CB  1 
ATOM   1661 C CG  . PHE A 1 232 ? 118.403 154.682 212.180 1.00 104.66 ? 231 PHE A CG  1 
ATOM   1662 C CD1 . PHE A 1 232 ? 118.234 153.922 211.041 1.00 104.66 ? 231 PHE A CD1 1 
ATOM   1663 C CD2 . PHE A 1 232 ? 117.284 155.146 212.833 1.00 104.66 ? 231 PHE A CD2 1 
ATOM   1664 C CE1 . PHE A 1 232 ? 116.978 153.651 210.557 1.00 104.66 ? 231 PHE A CE1 1 
ATOM   1665 C CE2 . PHE A 1 232 ? 116.029 154.872 212.356 1.00 104.66 ? 231 PHE A CE2 1 
ATOM   1666 C CZ  . PHE A 1 232 ? 115.875 154.126 211.216 1.00 104.66 ? 231 PHE A CZ  1 
ATOM   1667 N N   . ASP A 1 233 ? 122.080 157.765 212.653 1.00 104.66 ? 232 ASP A N   1 
ATOM   1668 C CA  . ASP A 1 233 ? 123.346 158.252 213.188 1.00 104.66 ? 232 ASP A CA  1 
ATOM   1669 C C   . ASP A 1 233 ? 123.342 158.269 214.709 1.00 104.66 ? 232 ASP A C   1 
ATOM   1670 O O   . ASP A 1 233 ? 124.148 157.588 215.350 1.00 104.66 ? 232 ASP A O   1 
ATOM   1671 C CB  . ASP A 1 233 ? 123.636 159.649 212.642 1.00 104.66 ? 232 ASP A CB  1 
ATOM   1672 C CG  . ASP A 1 233 ? 124.287 159.613 211.280 1.00 104.66 ? 232 ASP A CG  1 
ATOM   1673 O OD1 . ASP A 1 233 ? 125.377 159.020 211.158 1.00 104.66 ? 232 ASP A OD1 1 
ATOM   1674 O OD2 . ASP A 1 233 ? 123.706 160.170 210.326 1.00 104.66 ? 232 ASP A OD2 1 
ATOM   1675 N N   . ILE A 1 234 ? 122.443 159.042 215.304 1.00 108.16 ? 233 ILE A N   1 
ATOM   1676 C CA  . ILE A 1 234 ? 122.416 159.256 216.744 1.00 108.16 ? 233 ILE A CA  1 
ATOM   1677 C C   . ILE A 1 234 ? 121.143 158.648 217.308 1.00 108.16 ? 233 ILE A C   1 
ATOM   1678 O O   . ILE A 1 234 ? 120.037 158.942 216.833 1.00 108.16 ? 233 ILE A O   1 
ATOM   1679 C CB  . ILE A 1 234 ? 122.514 160.750 217.090 1.00 108.16 ? 233 ILE A CB  1 
ATOM   1680 C CG1 . ILE A 1 234 ? 123.626 161.401 216.271 1.00 108.16 ? 233 ILE A CG1 1 
ATOM   1681 C CG2 . ILE A 1 234 ? 122.767 160.932 218.571 1.00 108.16 ? 233 ILE A CG2 1 
ATOM   1682 C CD1 . ILE A 1 234 ? 123.633 162.902 216.342 1.00 108.16 ? 233 ILE A CD1 1 
ATOM   1683 N N   . TRP A 1 235 ? 121.303 157.809 218.323 1.00 110.96 ? 234 TRP A N   1 
ATOM   1684 C CA  . TRP A 1 235 ? 120.199 157.144 218.991 1.00 110.96 ? 234 TRP A CA  1 
ATOM   1685 C C   . TRP A 1 235 ? 119.940 157.780 220.350 1.00 110.96 ? 234 TRP A C   1 
ATOM   1686 O O   . TRP A 1 235 ? 120.684 158.644 220.816 1.00 110.96 ? 234 TRP A O   1 
ATOM   1687 C CB  . TRP A 1 235 ? 120.495 155.654 219.156 1.00 110.96 ? 234 TRP A CB  1 
ATOM   1688 C CG  . TRP A 1 235 ? 120.442 154.897 217.884 1.00 110.96 ? 234 TRP A CG  1 
ATOM   1689 C CD1 . TRP A 1 235 ? 121.222 155.086 216.787 1.00 110.96 ? 234 TRP A CD1 1 
ATOM   1690 C CD2 . TRP A 1 235 ? 119.555 153.824 217.568 1.00 110.96 ? 234 TRP A CD2 1 
ATOM   1691 N NE1 . TRP A 1 235 ? 120.878 154.195 215.804 1.00 110.96 ? 234 TRP A NE1 1 
ATOM   1692 C CE2 . TRP A 1 235 ? 119.854 153.408 216.260 1.00 110.96 ? 234 TRP A CE2 1 
ATOM   1693 C CE3 . TRP A 1 235 ? 118.535 153.175 218.265 1.00 110.96 ? 234 TRP A CE3 1 
ATOM   1694 C CZ2 . TRP A 1 235 ? 119.173 152.373 215.636 1.00 110.96 ? 234 TRP A CZ2 1 
ATOM   1695 C CZ3 . TRP A 1 235 ? 117.861 152.149 217.645 1.00 110.96 ? 234 TRP A CZ3 1 
ATOM   1696 C CH2 . TRP A 1 235 ? 118.182 151.757 216.344 1.00 110.96 ? 234 TRP A CH2 1 
ATOM   1697 N N   . GLY A 1 236 ? 118.860 157.334 220.988 1.00 125.45 ? 235 GLY A N   1 
ATOM   1698 C CA  . GLY A 1 236 ? 118.500 157.797 222.308 1.00 125.45 ? 235 GLY A CA  1 
ATOM   1699 C C   . GLY A 1 236 ? 118.792 156.759 223.380 1.00 125.45 ? 235 GLY A C   1 
ATOM   1700 O O   . GLY A 1 236 ? 119.261 155.655 223.118 1.00 125.45 ? 235 GLY A O   1 
ATOM   1701 N N   . GLN A 1 237 ? 118.503 157.148 224.622 1.00 137.00 ? 236 GLN A N   1 
ATOM   1702 C CA  . GLN A 1 237 ? 118.704 156.239 225.745 1.00 137.00 ? 236 GLN A CA  1 
ATOM   1703 C C   . GLN A 1 237 ? 117.788 155.028 225.643 1.00 137.00 ? 236 GLN A C   1 
ATOM   1704 O O   . GLN A 1 237 ? 118.212 153.893 225.886 1.00 137.00 ? 236 GLN A O   1 
ATOM   1705 C CB  . GLN A 1 237 ? 118.475 156.976 227.063 1.00 137.00 ? 236 GLN A CB  1 
ATOM   1706 C CG  . GLN A 1 237 ? 118.733 156.120 228.285 1.00 137.00 ? 236 GLN A CG  1 
ATOM   1707 C CD  . GLN A 1 237 ? 120.169 155.649 228.365 1.00 137.00 ? 236 GLN A CD  1 
ATOM   1708 O OE1 . GLN A 1 237 ? 120.468 154.488 228.092 1.00 137.00 ? 236 GLN A OE1 1 
ATOM   1709 N NE2 . GLN A 1 237 ? 121.068 156.551 228.740 1.00 137.00 ? 236 GLN A NE2 1 
ATOM   1710 N N   . GLY A 1 238 ? 116.526 155.250 225.290 1.00 139.35 ? 237 GLY A N   1 
ATOM   1711 C CA  . GLY A 1 238 ? 115.578 154.162 225.161 1.00 139.35 ? 237 GLY A CA  1 
ATOM   1712 C C   . GLY A 1 238 ? 115.010 153.719 226.490 1.00 139.35 ? 237 GLY A C   1 
ATOM   1713 O O   . GLY A 1 238 ? 115.743 153.614 227.477 1.00 139.35 ? 237 GLY A O   1 
ATOM   1714 N N   . THR A 1 239 ? 113.707 153.455 226.534 1.00 142.11 ? 238 THR A N   1 
ATOM   1715 C CA  . THR A 1 239 ? 113.058 153.036 227.768 1.00 142.11 ? 238 THR A CA  1 
ATOM   1716 C C   . THR A 1 239 ? 112.091 151.897 227.487 1.00 142.11 ? 238 THR A C   1 
ATOM   1717 O O   . THR A 1 239 ? 111.548 151.780 226.388 1.00 142.11 ? 238 THR A O   1 
ATOM   1718 C CB  . THR A 1 239 ? 112.312 154.193 228.439 1.00 142.11 ? 238 THR A CB  1 
ATOM   1719 O OG1 . THR A 1 239 ? 111.687 153.724 229.640 1.00 142.11 ? 238 THR A OG1 1 
ATOM   1720 C CG2 . THR A 1 239 ? 111.255 154.756 227.508 1.00 142.11 ? 238 THR A CG2 1 
ATOM   1721 N N   . MET A 1 240 ? 111.881 151.056 228.493 1.00 150.85 ? 239 MET A N   1 
ATOM   1722 C CA  . MET A 1 240 ? 111.023 149.889 228.361 1.00 150.85 ? 239 MET A CA  1 
ATOM   1723 C C   . MET A 1 240 ? 109.622 150.207 228.862 1.00 150.85 ? 239 MET A C   1 
ATOM   1724 O O   . MET A 1 240 ? 109.446 150.984 229.806 1.00 150.85 ? 239 MET A O   1 
ATOM   1725 C CB  . MET A 1 240 ? 111.600 148.694 229.124 1.00 150.85 ? 239 MET A CB  1 
ATOM   1726 C CG  . MET A 1 240 ? 111.429 148.760 230.631 1.00 150.85 ? 239 MET A CG  1 
ATOM   1727 S SD  . MET A 1 240 ? 112.548 149.943 231.404 1.00 150.85 ? 239 MET A SD  1 
ATOM   1728 C CE  . MET A 1 240 ? 114.021 148.942 231.587 1.00 150.85 ? 239 MET A CE  1 
ATOM   1729 N N   . VAL A 1 241 ? 108.625 149.622 228.205 1.00 157.90 ? 240 VAL A N   1 
ATOM   1730 C CA  . VAL A 1 241 ? 107.227 149.771 228.581 1.00 157.90 ? 240 VAL A CA  1 
ATOM   1731 C C   . VAL A 1 241 ? 106.604 148.386 228.637 1.00 157.90 ? 240 VAL A C   1 
ATOM   1732 O O   . VAL A 1 241 ? 106.716 147.610 227.680 1.00 157.90 ? 240 VAL A O   1 
ATOM   1733 C CB  . VAL A 1 241 ? 106.456 150.670 227.595 1.00 157.90 ? 240 VAL A CB  1 
ATOM   1734 C CG1 . VAL A 1 241 ? 105.001 150.775 228.008 1.00 157.90 ? 240 VAL A CG1 1 
ATOM   1735 C CG2 . VAL A 1 241 ? 107.089 152.047 227.530 1.00 157.90 ? 240 VAL A CG2 1 
ATOM   1736 N N   . THR A 1 242 ? 105.952 148.081 229.756 1.00 167.74 ? 241 THR A N   1 
ATOM   1737 C CA  . THR A 1 242 ? 105.310 146.795 229.982 1.00 167.74 ? 241 THR A CA  1 
ATOM   1738 C C   . THR A 1 242 ? 103.813 147.006 230.143 1.00 167.74 ? 241 THR A C   1 
ATOM   1739 O O   . THR A 1 242 ? 103.384 147.875 230.908 1.00 167.74 ? 241 THR A O   1 
ATOM   1740 C CB  . THR A 1 242 ? 105.880 146.104 231.223 1.00 167.74 ? 241 THR A CB  1 
ATOM   1741 O OG1 . THR A 1 242 ? 107.291 145.920 231.061 1.00 167.74 ? 241 THR A OG1 1 
ATOM   1742 C CG2 . THR A 1 242 ? 105.219 144.750 231.429 1.00 167.74 ? 241 THR A CG2 1 
ATOM   1743 N N   . VAL A 1 243 ? 103.026 146.212 229.426 1.00 169.70 ? 242 VAL A N   1 
ATOM   1744 C CA  . VAL A 1 243 ? 101.572 146.290 229.474 1.00 169.70 ? 242 VAL A CA  1 
ATOM   1745 C C   . VAL A 1 243 ? 101.080 145.125 230.321 1.00 169.70 ? 242 VAL A C   1 
ATOM   1746 O O   . VAL A 1 243 ? 101.206 143.961 229.925 1.00 169.70 ? 242 VAL A O   1 
ATOM   1747 C CB  . VAL A 1 243 ? 100.959 146.254 228.070 1.00 169.70 ? 242 VAL A CB  1 
ATOM   1748 C CG1 . VAL A 1 243 ? 99.448  146.372 228.152 1.00 169.70 ? 242 VAL A CG1 1 
ATOM   1749 C CG2 . VAL A 1 243 ? 101.552 147.354 227.212 1.00 169.70 ? 242 VAL A CG2 1 
ATOM   1750 N N   . SER A 1 244 ? 100.514 145.433 231.483 1.00 173.18 ? 243 SER A N   1 
ATOM   1751 C CA  . SER A 1 244 ? 100.066 144.403 232.409 1.00 173.18 ? 243 SER A CA  1 
ATOM   1752 C C   . SER A 1 244 ? 99.041  145.010 233.354 1.00 173.18 ? 243 SER A C   1 
ATOM   1753 O O   . SER A 1 244 ? 98.895  146.231 233.446 1.00 173.18 ? 243 SER A O   1 
ATOM   1754 C CB  . SER A 1 244 ? 101.242 143.800 233.183 1.00 173.18 ? 243 SER A CB  1 
ATOM   1755 O OG  . SER A 1 244 ? 100.797 142.835 234.120 1.00 173.18 ? 243 SER A OG  1 
ATOM   1756 N N   . SER A 1 245 ? 98.328  144.135 234.055 1.00 175.75 ? 244 SER A N   1 
ATOM   1757 C CA  . SER A 1 245 ? 97.335  144.559 235.034 1.00 175.75 ? 244 SER A CA  1 
ATOM   1758 C C   . SER A 1 245 ? 97.998  145.241 236.227 1.00 175.75 ? 244 SER A C   1 
ATOM   1759 O O   . SER A 1 245 ? 98.489  144.576 237.139 1.00 175.75 ? 244 SER A O   1 
ATOM   1760 C CB  . SER A 1 245 ? 96.506  143.365 235.506 1.00 175.75 ? 244 SER A CB  1 
ATOM   1761 O OG  . SER A 1 245 ? 97.340  142.347 236.033 1.00 175.75 ? 244 SER A OG  1 
ATOM   1762 N N   . ASN B 2 320 ? 156.968 185.046 172.526 1.00 148.82 ? 331 ASN B N   1 
ATOM   1763 C CA  . ASN B 2 320 ? 158.155 185.792 172.923 1.00 148.82 ? 331 ASN B CA  1 
ATOM   1764 C C   . ASN B 2 320 ? 157.935 186.517 174.248 1.00 148.82 ? 331 ASN B C   1 
ATOM   1765 O O   . ASN B 2 320 ? 158.887 186.964 174.885 1.00 148.82 ? 331 ASN B O   1 
ATOM   1766 C CB  . ASN B 2 320 ? 158.544 186.794 171.836 1.00 148.82 ? 331 ASN B CB  1 
ATOM   1767 C CG  . ASN B 2 320 ? 157.402 187.714 171.458 1.00 148.82 ? 331 ASN B CG  1 
ATOM   1768 O OD1 . ASN B 2 320 ? 157.218 188.772 172.059 1.00 148.82 ? 331 ASN B OD1 1 
ATOM   1769 N ND2 . ASN B 2 320 ? 156.625 187.313 170.459 1.00 148.82 ? 331 ASN B ND2 1 
ATOM   1770 N N   . ILE B 2 321 ? 156.669 186.631 174.652 1.00 145.38 ? 332 ILE B N   1 
ATOM   1771 C CA  . ILE B 2 321 ? 156.339 187.295 175.906 1.00 145.38 ? 332 ILE B CA  1 
ATOM   1772 C C   . ILE B 2 321 ? 156.898 186.498 177.078 1.00 145.38 ? 332 ILE B C   1 
ATOM   1773 O O   . ILE B 2 321 ? 156.989 185.264 177.037 1.00 145.38 ? 332 ILE B O   1 
ATOM   1774 C CB  . ILE B 2 321 ? 154.817 187.480 176.032 1.00 145.38 ? 332 ILE B CB  1 
ATOM   1775 C CG1 . ILE B 2 321 ? 154.106 186.138 175.864 1.00 145.38 ? 332 ILE B CG1 1 
ATOM   1776 C CG2 . ILE B 2 321 ? 154.319 188.479 175.003 1.00 145.38 ? 332 ILE B CG2 1 
ATOM   1777 C CD1 . ILE B 2 321 ? 152.624 186.201 176.129 1.00 145.38 ? 332 ILE B CD1 1 
ATOM   1778 N N   . THR B 2 322 ? 157.283 187.210 178.137 1.00 148.21 ? 333 THR B N   1 
ATOM   1779 C CA  . THR B 2 322 ? 157.970 186.615 179.285 1.00 148.21 ? 333 THR B CA  1 
ATOM   1780 C C   . THR B 2 322 ? 157.200 186.934 180.564 1.00 148.21 ? 333 THR B C   1 
ATOM   1781 O O   . THR B 2 322 ? 157.481 187.927 181.240 1.00 148.21 ? 333 THR B O   1 
ATOM   1782 C CB  . THR B 2 322 ? 159.412 187.108 179.369 1.00 148.21 ? 333 THR B CB  1 
ATOM   1783 O OG1 . THR B 2 322 ? 159.425 188.538 179.471 1.00 148.21 ? 333 THR B OG1 1 
ATOM   1784 C CG2 . THR B 2 322 ? 160.196 186.683 178.136 1.00 148.21 ? 333 THR B CG2 1 
ATOM   1785 N N   . ASN B 2 323 ? 156.230 186.085 180.891 1.00 132.54 ? 334 ASN B N   1 
ATOM   1786 C CA  . ASN B 2 323 ? 155.572 186.113 182.191 1.00 132.54 ? 334 ASN B CA  1 
ATOM   1787 C C   . ASN B 2 323 ? 155.105 184.705 182.530 1.00 132.54 ? 334 ASN B C   1 
ATOM   1788 O O   . ASN B 2 323 ? 154.585 183.991 181.669 1.00 132.54 ? 334 ASN B O   1 
ATOM   1789 C CB  . ASN B 2 323 ? 154.415 187.124 182.222 1.00 132.54 ? 334 ASN B CB  1 
ATOM   1790 C CG  . ASN B 2 323 ? 153.389 186.897 181.126 1.00 132.54 ? 334 ASN B CG  1 
ATOM   1791 O OD1 . ASN B 2 323 ? 153.485 185.956 180.344 1.00 132.54 ? 334 ASN B OD1 1 
ATOM   1792 N ND2 . ASN B 2 323 ? 152.392 187.771 181.070 1.00 132.54 ? 334 ASN B ND2 1 
ATOM   1793 N N   . LEU B 2 324 ? 155.324 184.299 183.775 1.00 122.66 ? 335 LEU B N   1 
ATOM   1794 C CA  . LEU B 2 324 ? 155.093 182.913 184.153 1.00 122.66 ? 335 LEU B CA  1 
ATOM   1795 C C   . LEU B 2 324 ? 153.605 182.619 184.272 1.00 122.66 ? 335 LEU B C   1 
ATOM   1796 O O   . LEU B 2 324 ? 152.828 183.438 184.769 1.00 122.66 ? 335 LEU B O   1 
ATOM   1797 C CB  . LEU B 2 324 ? 155.798 182.595 185.471 1.00 122.66 ? 335 LEU B CB  1 
ATOM   1798 C CG  . LEU B 2 324 ? 157.286 182.236 185.412 1.00 122.66 ? 335 LEU B CG  1 
ATOM   1799 C CD1 . LEU B 2 324 ? 157.492 180.947 184.630 1.00 122.66 ? 335 LEU B CD1 1 
ATOM   1800 C CD2 . LEU B 2 324 ? 158.135 183.362 184.834 1.00 122.66 ? 335 LEU B CD2 1 
ATOM   1801 N N   . CYS B 2 325 ? 153.213 181.434 183.812 1.00 117.33 ? 336 CYS B N   1 
ATOM   1802 C CA  . CYS B 2 325 ? 151.834 181.003 183.937 1.00 117.33 ? 336 CYS B CA  1 
ATOM   1803 C C   . CYS B 2 325 ? 151.483 180.784 185.406 1.00 117.33 ? 336 CYS B C   1 
ATOM   1804 O O   . CYS B 2 325 ? 152.342 180.413 186.210 1.00 117.33 ? 336 CYS B O   1 
ATOM   1805 C CB  . CYS B 2 325 ? 151.603 179.715 183.153 1.00 117.33 ? 336 CYS B CB  1 
ATOM   1806 S SG  . CYS B 2 325 ? 151.734 179.892 181.366 1.00 117.33 ? 336 CYS B SG  1 
ATOM   1807 N N   . PRO B 2 326 ? 150.226 181.004 185.783 1.00 111.20 ? 337 PRO B N   1 
ATOM   1808 C CA  . PRO B 2 326 ? 149.797 180.829 187.176 1.00 111.20 ? 337 PRO B CA  1 
ATOM   1809 C C   . PRO B 2 326 ? 149.568 179.371 187.562 1.00 111.20 ? 337 PRO B C   1 
ATOM   1810 O O   . PRO B 2 326 ? 148.559 179.023 188.175 1.00 111.20 ? 337 PRO B O   1 
ATOM   1811 C CB  . PRO B 2 326 ? 148.498 181.639 187.229 1.00 111.20 ? 337 PRO B CB  1 
ATOM   1812 C CG  . PRO B 2 326 ? 147.946 181.512 185.863 1.00 111.20 ? 337 PRO B CG  1 
ATOM   1813 C CD  . PRO B 2 326 ? 149.127 181.485 184.928 1.00 111.20 ? 337 PRO B CD  1 
ATOM   1814 N N   . PHE B 2 327 ? 150.518 178.509 187.201 1.00 106.24 ? 338 PHE B N   1 
ATOM   1815 C CA  . PHE B 2 327 ? 150.437 177.120 187.630 1.00 106.24 ? 338 PHE B CA  1 
ATOM   1816 C C   . PHE B 2 327 ? 150.595 176.996 189.137 1.00 106.24 ? 338 PHE B C   1 
ATOM   1817 O O   . PHE B 2 327 ? 150.194 175.984 189.720 1.00 106.24 ? 338 PHE B O   1 
ATOM   1818 C CB  . PHE B 2 327 ? 151.499 176.283 186.922 1.00 106.24 ? 338 PHE B CB  1 
ATOM   1819 C CG  . PHE B 2 327 ? 151.088 175.810 185.563 1.00 106.24 ? 338 PHE B CG  1 
ATOM   1820 C CD1 . PHE B 2 327 ? 149.796 175.386 185.327 1.00 106.24 ? 338 PHE B CD1 1 
ATOM   1821 C CD2 . PHE B 2 327 ? 151.995 175.777 184.525 1.00 106.24 ? 338 PHE B CD2 1 
ATOM   1822 C CE1 . PHE B 2 327 ? 149.417 174.948 184.080 1.00 106.24 ? 338 PHE B CE1 1 
ATOM   1823 C CE2 . PHE B 2 327 ? 151.619 175.338 183.277 1.00 106.24 ? 338 PHE B CE2 1 
ATOM   1824 C CZ  . PHE B 2 327 ? 150.330 174.923 183.055 1.00 106.24 ? 338 PHE B CZ  1 
ATOM   1825 N N   . GLY B 2 328 ? 151.177 178.007 189.779 1.00 111.01 ? 339 GLY B N   1 
ATOM   1826 C CA  . GLY B 2 328 ? 151.393 177.932 191.213 1.00 111.01 ? 339 GLY B CA  1 
ATOM   1827 C C   . GLY B 2 328 ? 150.102 177.888 192.004 1.00 111.01 ? 339 GLY B C   1 
ATOM   1828 O O   . GLY B 2 328 ? 149.961 177.093 192.934 1.00 111.01 ? 339 GLY B O   1 
ATOM   1829 N N   . GLU B 2 329 ? 149.140 178.739 191.648 1.00 106.74 ? 340 GLU B N   1 
ATOM   1830 C CA  . GLU B 2 329 ? 147.944 178.855 192.472 1.00 106.74 ? 340 GLU B CA  1 
ATOM   1831 C C   . GLU B 2 329 ? 146.975 177.708 192.212 1.00 106.74 ? 340 GLU B C   1 
ATOM   1832 O O   . GLU B 2 329 ? 146.226 177.311 193.111 1.00 106.74 ? 340 GLU B O   1 
ATOM   1833 C CB  . GLU B 2 329 ? 147.291 180.224 192.251 1.00 106.74 ? 340 GLU B CB  1 
ATOM   1834 C CG  . GLU B 2 329 ? 146.598 180.458 190.915 1.00 106.74 ? 340 GLU B CG  1 
ATOM   1835 C CD  . GLU B 2 329 ? 145.250 179.775 190.811 1.00 106.74 ? 340 GLU B CD  1 
ATOM   1836 O OE1 . GLU B 2 329 ? 144.668 179.434 191.860 1.00 106.74 ? 340 GLU B OE1 1 
ATOM   1837 O OE2 . GLU B 2 329 ? 144.766 179.586 189.681 1.00 106.74 ? 340 GLU B OE2 1 
ATOM   1838 N N   . VAL B 2 330 ? 146.966 177.164 190.995 1.00 104.66 ? 341 VAL B N   1 
ATOM   1839 C CA  . VAL B 2 330 ? 146.064 176.055 190.693 1.00 104.66 ? 341 VAL B CA  1 
ATOM   1840 C C   . VAL B 2 330 ? 146.429 174.834 191.525 1.00 104.66 ? 341 VAL B C   1 
ATOM   1841 O O   . VAL B 2 330 ? 145.577 174.234 192.189 1.00 104.66 ? 341 VAL B O   1 
ATOM   1842 C CB  . VAL B 2 330 ? 146.086 175.727 189.192 1.00 104.66 ? 341 VAL B CB  1 
ATOM   1843 C CG1 . VAL B 2 330 ? 145.536 174.337 188.953 1.00 104.66 ? 341 VAL B CG1 1 
ATOM   1844 C CG2 . VAL B 2 330 ? 145.272 176.740 188.422 1.00 104.66 ? 341 VAL B CG2 1 
ATOM   1845 N N   . PHE B 2 331 ? 147.705 174.457 191.512 1.00 104.66 ? 342 PHE B N   1 
ATOM   1846 C CA  . PHE B 2 331 ? 148.115 173.251 192.218 1.00 104.66 ? 342 PHE B CA  1 
ATOM   1847 C C   . PHE B 2 331 ? 148.194 173.473 193.719 1.00 104.66 ? 342 PHE B C   1 
ATOM   1848 O O   . PHE B 2 331 ? 147.960 172.540 194.493 1.00 104.66 ? 342 PHE B O   1 
ATOM   1849 C CB  . PHE B 2 331 ? 149.460 172.766 191.689 1.00 104.66 ? 342 PHE B CB  1 
ATOM   1850 C CG  . PHE B 2 331 ? 149.382 172.132 190.339 1.00 104.66 ? 342 PHE B CG  1 
ATOM   1851 C CD1 . PHE B 2 331 ? 149.330 172.906 189.202 1.00 104.66 ? 342 PHE B CD1 1 
ATOM   1852 C CD2 . PHE B 2 331 ? 149.367 170.762 190.207 1.00 104.66 ? 342 PHE B CD2 1 
ATOM   1853 C CE1 . PHE B 2 331 ? 149.262 172.326 187.963 1.00 104.66 ? 342 PHE B CE1 1 
ATOM   1854 C CE2 . PHE B 2 331 ? 149.298 170.179 188.969 1.00 104.66 ? 342 PHE B CE2 1 
ATOM   1855 C CZ  . PHE B 2 331 ? 149.246 170.960 187.847 1.00 104.66 ? 342 PHE B CZ  1 
ATOM   1856 N N   . ASN B 2 332 ? 148.526 174.686 194.153 1.00 111.55 ? 343 ASN B N   1 
ATOM   1857 C CA  . ASN B 2 332 ? 148.704 174.981 195.566 1.00 111.55 ? 343 ASN B CA  1 
ATOM   1858 C C   . ASN B 2 332 ? 147.547 175.779 196.150 1.00 111.55 ? 343 ASN B C   1 
ATOM   1859 O O   . ASN B 2 332 ? 147.743 176.530 197.110 1.00 111.55 ? 343 ASN B O   1 
ATOM   1860 C CB  . ASN B 2 332 ? 150.026 175.715 195.785 1.00 111.55 ? 343 ASN B CB  1 
ATOM   1861 C CG  . ASN B 2 332 ? 151.224 174.802 195.639 1.00 111.55 ? 343 ASN B CG  1 
ATOM   1862 O OD1 . ASN B 2 332 ? 151.093 173.581 195.710 1.00 111.55 ? 343 ASN B OD1 1 
ATOM   1863 N ND2 . ASN B 2 332 ? 152.399 175.385 195.425 1.00 111.55 ? 343 ASN B ND2 1 
ATOM   1864 N N   . ALA B 2 333 ? 146.350 175.642 195.588 1.00 110.00 ? 344 ALA B N   1 
ATOM   1865 C CA  . ALA B 2 333 ? 145.179 176.267 196.180 1.00 110.00 ? 344 ALA B CA  1 
ATOM   1866 C C   . ALA B 2 333 ? 144.825 175.580 197.492 1.00 110.00 ? 344 ALA B C   1 
ATOM   1867 O O   . ALA B 2 333 ? 145.061 174.384 197.677 1.00 110.00 ? 344 ALA B O   1 
ATOM   1868 C CB  . ALA B 2 333 ? 143.992 176.209 195.222 1.00 110.00 ? 344 ALA B CB  1 
ATOM   1869 N N   . THR B 2 334 ? 144.256 176.356 198.414 1.00 113.45 ? 345 THR B N   1 
ATOM   1870 C CA  . THR B 2 334 ? 143.933 175.824 199.731 1.00 113.45 ? 345 THR B CA  1 
ATOM   1871 C C   . THR B 2 334 ? 142.710 174.918 199.708 1.00 113.45 ? 345 THR B C   1 
ATOM   1872 O O   . THR B 2 334 ? 142.632 173.973 200.501 1.00 113.45 ? 345 THR B O   1 
ATOM   1873 C CB  . THR B 2 334 ? 143.700 176.965 200.718 1.00 113.45 ? 345 THR B CB  1 
ATOM   1874 O OG1 . THR B 2 334 ? 142.435 177.577 200.444 1.00 113.45 ? 345 THR B OG1 1 
ATOM   1875 C CG2 . THR B 2 334 ? 144.797 178.004 200.591 1.00 113.45 ? 345 THR B CG2 1 
ATOM   1876 N N   . ARG B 2 335 ? 141.754 175.185 198.824 1.00 112.30 ? 346 ARG B N   1 
ATOM   1877 C CA  . ARG B 2 335 ? 140.486 174.470 198.808 1.00 112.30 ? 346 ARG B CA  1 
ATOM   1878 C C   . ARG B 2 335 ? 140.163 174.007 197.397 1.00 112.30 ? 346 ARG B C   1 
ATOM   1879 O O   . ARG B 2 335 ? 140.242 174.795 196.450 1.00 112.30 ? 346 ARG B O   1 
ATOM   1880 C CB  . ARG B 2 335 ? 139.361 175.360 199.329 1.00 112.30 ? 346 ARG B CB  1 
ATOM   1881 C CG  . ARG B 2 335 ? 139.342 175.542 200.834 1.00 112.30 ? 346 ARG B CG  1 
ATOM   1882 C CD  . ARG B 2 335 ? 138.066 176.216 201.385 1.00 112.30 ? 346 ARG B CD  1 
ATOM   1883 N NE  . ARG B 2 335 ? 137.529 177.314 200.582 1.00 112.30 ? 346 ARG B NE  1 
ATOM   1884 C CZ  . ARG B 2 335 ? 136.767 177.181 199.502 1.00 112.30 ? 346 ARG B CZ  1 
ATOM   1885 N NH1 . ARG B 2 335 ? 136.340 175.997 199.095 1.00 112.30 ? 346 ARG B NH1 1 
ATOM   1886 N NH2 . ARG B 2 335 ? 136.407 178.268 198.825 1.00 112.30 ? 346 ARG B NH2 1 
ATOM   1887 N N   . PHE B 2 336 ? 139.789 172.741 197.262 1.00 104.66 ? 347 PHE B N   1 
ATOM   1888 C CA  . PHE B 2 336 ? 139.275 172.204 196.012 1.00 104.66 ? 347 PHE B CA  1 
ATOM   1889 C C   . PHE B 2 336 ? 137.795 171.886 196.156 1.00 104.66 ? 347 PHE B C   1 
ATOM   1890 O O   . PHE B 2 336 ? 137.350 171.411 197.203 1.00 104.66 ? 347 PHE B O   1 
ATOM   1891 C CB  . PHE B 2 336 ? 140.037 170.952 195.577 1.00 104.66 ? 347 PHE B CB  1 
ATOM   1892 C CG  . PHE B 2 336 ? 141.369 171.238 194.952 1.00 104.66 ? 347 PHE B CG  1 
ATOM   1893 C CD1 . PHE B 2 336 ? 141.693 172.511 194.533 1.00 104.66 ? 347 PHE B CD1 1 
ATOM   1894 C CD2 . PHE B 2 336 ? 142.277 170.225 194.739 1.00 104.66 ? 347 PHE B CD2 1 
ATOM   1895 C CE1 . PHE B 2 336 ? 142.910 172.768 193.943 1.00 104.66 ? 347 PHE B CE1 1 
ATOM   1896 C CE2 . PHE B 2 336 ? 143.490 170.480 194.150 1.00 104.66 ? 347 PHE B CE2 1 
ATOM   1897 C CZ  . PHE B 2 336 ? 143.807 171.750 193.753 1.00 104.66 ? 347 PHE B CZ  1 
ATOM   1898 N N   . ALA B 2 337 ? 137.041 172.151 195.095 1.00 104.66 ? 348 ALA B N   1 
ATOM   1899 C CA  . ALA B 2 337 ? 135.599 171.995 195.121 1.00 104.66 ? 348 ALA B CA  1 
ATOM   1900 C C   . ALA B 2 337 ? 135.207 170.529 194.968 1.00 104.66 ? 348 ALA B C   1 
ATOM   1901 O O   . ALA B 2 337 ? 136.021 169.667 194.633 1.00 104.66 ? 348 ALA B O   1 
ATOM   1902 C CB  . ALA B 2 337 ? 134.956 172.834 194.020 1.00 104.66 ? 348 ALA B CB  1 
ATOM   1903 N N   . SER B 2 338 ? 133.929 170.256 195.214 1.00 104.66 ? 349 SER B N   1 
ATOM   1904 C CA  . SER B 2 338 ? 133.401 168.908 195.090 1.00 104.66 ? 349 SER B CA  1 
ATOM   1905 C C   . SER B 2 338 ? 133.464 168.446 193.640 1.00 104.66 ? 349 SER B C   1 
ATOM   1906 O O   . SER B 2 338 ? 133.609 169.243 192.714 1.00 104.66 ? 349 SER B O   1 
ATOM   1907 C CB  . SER B 2 338 ? 131.962 168.851 195.591 1.00 104.66 ? 349 SER B CB  1 
ATOM   1908 O OG  . SER B 2 338 ? 131.898 169.127 196.977 1.00 104.66 ? 349 SER B OG  1 
ATOM   1909 N N   . VAL B 2 339 ? 133.353 167.133 193.449 1.00 104.66 ? 350 VAL B N   1 
ATOM   1910 C CA  . VAL B 2 339 ? 133.489 166.587 192.105 1.00 104.66 ? 350 VAL B CA  1 
ATOM   1911 C C   . VAL B 2 339 ? 132.330 167.017 191.217 1.00 104.66 ? 350 VAL B C   1 
ATOM   1912 O O   . VAL B 2 339 ? 132.501 167.176 190.003 1.00 104.66 ? 350 VAL B O   1 
ATOM   1913 C CB  . VAL B 2 339 ? 133.627 165.057 192.158 1.00 104.66 ? 350 VAL B CB  1 
ATOM   1914 C CG1 . VAL B 2 339 ? 132.394 164.437 192.756 1.00 104.66 ? 350 VAL B CG1 1 
ATOM   1915 C CG2 . VAL B 2 339 ? 133.878 164.502 190.773 1.00 104.66 ? 350 VAL B CG2 1 
ATOM   1916 N N   . TYR B 2 340 ? 131.145 167.227 191.786 1.00 104.66 ? 351 TYR B N   1 
ATOM   1917 C CA  . TYR B 2 340 ? 129.982 167.552 190.972 1.00 104.66 ? 351 TYR B CA  1 
ATOM   1918 C C   . TYR B 2 340 ? 129.884 169.029 190.624 1.00 104.66 ? 351 TYR B C   1 
ATOM   1919 O O   . TYR B 2 340 ? 128.989 169.405 189.861 1.00 104.66 ? 351 TYR B O   1 
ATOM   1920 C CB  . TYR B 2 340 ? 128.702 167.109 191.679 1.00 104.66 ? 351 TYR B CB  1 
ATOM   1921 C CG  . TYR B 2 340 ? 128.176 168.105 192.676 1.00 104.66 ? 351 TYR B CG  1 
ATOM   1922 C CD1 . TYR B 2 340 ? 128.732 168.209 193.937 1.00 104.66 ? 351 TYR B CD1 1 
ATOM   1923 C CD2 . TYR B 2 340 ? 127.116 168.937 192.362 1.00 104.66 ? 351 TYR B CD2 1 
ATOM   1924 C CE1 . TYR B 2 340 ? 128.254 169.116 194.854 1.00 104.66 ? 351 TYR B CE1 1 
ATOM   1925 C CE2 . TYR B 2 340 ? 126.634 169.848 193.272 1.00 104.66 ? 351 TYR B CE2 1 
ATOM   1926 C CZ  . TYR B 2 340 ? 127.206 169.932 194.516 1.00 104.66 ? 351 TYR B CZ  1 
ATOM   1927 O OH  . TYR B 2 340 ? 126.727 170.839 195.428 1.00 104.66 ? 351 TYR B OH  1 
ATOM   1928 N N   . ALA B 2 341 ? 130.767 169.870 191.154 1.00 104.66 ? 352 ALA B N   1 
ATOM   1929 C CA  . ALA B 2 341 ? 130.788 171.302 190.871 1.00 104.66 ? 352 ALA B CA  1 
ATOM   1930 C C   . ALA B 2 341 ? 132.207 171.758 190.573 1.00 104.66 ? 352 ALA B C   1 
ATOM   1931 O O   . ALA B 2 341 ? 132.694 172.756 191.105 1.00 104.66 ? 352 ALA B O   1 
ATOM   1932 C CB  . ALA B 2 341 ? 130.202 172.098 192.029 1.00 104.66 ? 352 ALA B CB  1 
ATOM   1933 N N   . TRP B 2 342 ? 132.888 171.016 189.704 1.00 104.66 ? 353 TRP B N   1 
ATOM   1934 C CA  . TRP B 2 342 ? 134.312 171.224 189.486 1.00 104.66 ? 353 TRP B CA  1 
ATOM   1935 C C   . TRP B 2 342 ? 134.592 172.589 188.876 1.00 104.66 ? 353 TRP B C   1 
ATOM   1936 O O   . TRP B 2 342 ? 133.814 173.101 188.070 1.00 104.66 ? 353 TRP B O   1 
ATOM   1937 C CB  . TRP B 2 342 ? 134.867 170.128 188.584 1.00 104.66 ? 353 TRP B CB  1 
ATOM   1938 C CG  . TRP B 2 342 ? 133.956 169.732 187.477 1.00 104.66 ? 353 TRP B CG  1 
ATOM   1939 C CD1 . TRP B 2 342 ? 132.940 168.835 187.542 1.00 104.66 ? 353 TRP B CD1 1 
ATOM   1940 C CD2 . TRP B 2 342 ? 133.991 170.201 186.128 1.00 104.66 ? 353 TRP B CD2 1 
ATOM   1941 N NE1 . TRP B 2 342 ? 132.331 168.720 186.321 1.00 104.66 ? 353 TRP B NE1 1 
ATOM   1942 C CE2 . TRP B 2 342 ? 132.960 169.549 185.434 1.00 104.66 ? 353 TRP B CE2 1 
ATOM   1943 C CE3 . TRP B 2 342 ? 134.793 171.112 185.441 1.00 104.66 ? 353 TRP B CE3 1 
ATOM   1944 C CZ2 . TRP B 2 342 ? 132.708 169.778 184.091 1.00 104.66 ? 353 TRP B CZ2 1 
ATOM   1945 C CZ3 . TRP B 2 342 ? 134.540 171.337 184.108 1.00 104.66 ? 353 TRP B CZ3 1 
ATOM   1946 C CH2 . TRP B 2 342 ? 133.508 170.675 183.447 1.00 104.66 ? 353 TRP B CH2 1 
ATOM   1947 N N   . ASN B 2 343 ? 135.717 173.176 189.267 1.00 104.66 ? 354 ASN B N   1 
ATOM   1948 C CA  . ASN B 2 343 ? 136.127 174.464 188.739 1.00 104.66 ? 354 ASN B CA  1 
ATOM   1949 C C   . ASN B 2 343 ? 136.740 174.307 187.355 1.00 104.66 ? 354 ASN B C   1 
ATOM   1950 O O   . ASN B 2 343 ? 137.057 173.206 186.904 1.00 104.66 ? 354 ASN B O   1 
ATOM   1951 C CB  . ASN B 2 343 ? 137.133 175.137 189.668 1.00 104.66 ? 354 ASN B CB  1 
ATOM   1952 C CG  . ASN B 2 343 ? 136.540 175.489 191.011 1.00 104.66 ? 354 ASN B CG  1 
ATOM   1953 O OD1 . ASN B 2 343 ? 136.962 174.973 192.044 1.00 104.66 ? 354 ASN B OD1 1 
ATOM   1954 N ND2 . ASN B 2 343 ? 135.552 176.373 191.005 1.00 104.66 ? 354 ASN B ND2 1 
ATOM   1955 N N   . ARG B 2 344 ? 136.897 175.438 186.676 1.00 104.66 ? 355 ARG B N   1 
ATOM   1956 C CA  . ARG B 2 344 ? 137.554 175.501 185.382 1.00 104.66 ? 355 ARG B CA  1 
ATOM   1957 C C   . ARG B 2 344 ? 138.238 176.850 185.258 1.00 104.66 ? 355 ARG B C   1 
ATOM   1958 O O   . ARG B 2 344 ? 137.660 177.876 185.623 1.00 104.66 ? 355 ARG B O   1 
ATOM   1959 C CB  . ARG B 2 344 ? 136.557 175.309 184.242 1.00 104.66 ? 355 ARG B CB  1 
ATOM   1960 C CG  . ARG B 2 344 ? 137.190 175.264 182.877 1.00 104.66 ? 355 ARG B CG  1 
ATOM   1961 C CD  . ARG B 2 344 ? 136.134 175.097 181.813 1.00 104.66 ? 355 ARG B CD  1 
ATOM   1962 N NE  . ARG B 2 344 ? 136.653 174.451 180.616 1.00 104.66 ? 355 ARG B NE  1 
ATOM   1963 C CZ  . ARG B 2 344 ? 136.988 173.171 180.539 1.00 104.66 ? 355 ARG B CZ  1 
ATOM   1964 N NH1 . ARG B 2 344 ? 136.876 172.364 181.579 1.00 104.66 ? 355 ARG B NH1 1 
ATOM   1965 N NH2 . ARG B 2 344 ? 137.443 172.689 179.388 1.00 104.66 ? 355 ARG B NH2 1 
ATOM   1966 N N   . LYS B 2 345 ? 139.465 176.852 184.746 1.00 104.66 ? 356 LYS B N   1 
ATOM   1967 C CA  . LYS B 2 345 ? 140.246 178.075 184.656 1.00 104.66 ? 356 LYS B CA  1 
ATOM   1968 C C   . LYS B 2 345 ? 140.939 178.172 183.306 1.00 104.66 ? 356 LYS B C   1 
ATOM   1969 O O   . LYS B 2 345 ? 141.430 177.175 182.773 1.00 104.66 ? 356 LYS B O   1 
ATOM   1970 C CB  . LYS B 2 345 ? 141.282 178.150 185.777 1.00 104.66 ? 356 LYS B CB  1 
ATOM   1971 C CG  . LYS B 2 345 ? 142.085 179.431 185.772 1.00 104.66 ? 356 LYS B CG  1 
ATOM   1972 C CD  . LYS B 2 345 ? 143.014 179.509 186.960 1.00 104.66 ? 356 LYS B CD  1 
ATOM   1973 C CE  . LYS B 2 345 ? 143.914 180.726 186.859 1.00 104.66 ? 356 LYS B CE  1 
ATOM   1974 N NZ  . LYS B 2 345 ? 143.142 181.993 186.958 1.00 104.66 ? 356 LYS B NZ  1 
ATOM   1975 N N   . ARG B 2 346 ? 140.971 179.383 182.763 1.00 104.66 ? 357 ARG B N   1 
ATOM   1976 C CA  . ARG B 2 346 ? 141.685 179.699 181.535 1.00 104.66 ? 357 ARG B CA  1 
ATOM   1977 C C   . ARG B 2 346 ? 143.107 180.126 181.856 1.00 104.66 ? 357 ARG B C   1 
ATOM   1978 O O   . ARG B 2 346 ? 143.328 180.936 182.760 1.00 104.66 ? 357 ARG B O   1 
ATOM   1979 C CB  . ARG B 2 346 ? 140.977 180.816 180.775 1.00 104.66 ? 357 ARG B CB  1 
ATOM   1980 C CG  . ARG B 2 346 ? 139.736 180.398 180.030 1.00 104.66 ? 357 ARG B CG  1 
ATOM   1981 C CD  . ARG B 2 346 ? 140.124 179.730 178.723 1.00 104.66 ? 357 ARG B CD  1 
ATOM   1982 N NE  . ARG B 2 346 ? 141.091 180.491 177.935 1.00 104.66 ? 357 ARG B NE  1 
ATOM   1983 C CZ  . ARG B 2 346 ? 141.000 181.780 177.621 1.00 104.66 ? 357 ARG B CZ  1 
ATOM   1984 N NH1 . ARG B 2 346 ? 139.929 182.498 177.920 1.00 104.66 ? 357 ARG B NH1 1 
ATOM   1985 N NH2 . ARG B 2 346 ? 142.003 182.359 176.968 1.00 104.66 ? 357 ARG B NH2 1 
ATOM   1986 N N   . ILE B 2 347 ? 144.065 179.587 181.112 1.00 104.66 ? 358 ILE B N   1 
ATOM   1987 C CA  . ILE B 2 347 ? 145.459 179.997 181.201 1.00 104.66 ? 358 ILE B CA  1 
ATOM   1988 C C   . ILE B 2 347 ? 145.877 180.485 179.823 1.00 104.66 ? 358 ILE B C   1 
ATOM   1989 O O   . ILE B 2 347 ? 145.727 179.759 178.834 1.00 104.66 ? 358 ILE B O   1 
ATOM   1990 C CB  . ILE B 2 347 ? 146.362 178.853 181.679 1.00 104.66 ? 358 ILE B CB  1 
ATOM   1991 C CG1 . ILE B 2 347 ? 145.945 178.398 183.072 1.00 104.66 ? 358 ILE B CG1 1 
ATOM   1992 C CG2 . ILE B 2 347 ? 147.806 179.297 181.698 1.00 104.66 ? 358 ILE B CG2 1 
ATOM   1993 C CD1 . ILE B 2 347 ? 146.613 177.121 183.511 1.00 104.66 ? 358 ILE B CD1 1 
ATOM   1994 N N   . SER B 2 348 ? 146.395 181.708 179.754 1.00 104.66 ? 359 SER B N   1 
ATOM   1995 C CA  . SER B 2 348 ? 146.725 182.294 178.463 1.00 104.66 ? 359 SER B CA  1 
ATOM   1996 C C   . SER B 2 348 ? 147.798 183.356 178.634 1.00 104.66 ? 359 SER B C   1 
ATOM   1997 O O   . SER B 2 348 ? 148.039 183.851 179.737 1.00 104.66 ? 359 SER B O   1 
ATOM   1998 C CB  . SER B 2 348 ? 145.489 182.901 177.795 1.00 104.66 ? 359 SER B CB  1 
ATOM   1999 O OG  . SER B 2 348 ? 144.969 183.967 178.565 1.00 104.66 ? 359 SER B OG  1 
ATOM   2000 N N   . ASN B 2 349 ? 148.435 183.696 177.512 1.00 111.08 ? 360 ASN B N   1 
ATOM   2001 C CA  . ASN B 2 349 ? 149.403 184.789 177.437 1.00 111.08 ? 360 ASN B CA  1 
ATOM   2002 C C   . ASN B 2 349 ? 150.526 184.619 178.455 1.00 111.08 ? 360 ASN B C   1 
ATOM   2003 O O   . ASN B 2 349 ? 150.887 185.549 179.179 1.00 111.08 ? 360 ASN B O   1 
ATOM   2004 C CB  . ASN B 2 349 ? 148.710 186.140 177.604 1.00 111.08 ? 360 ASN B CB  1 
ATOM   2005 C CG  . ASN B 2 349 ? 147.638 186.368 176.564 1.00 111.08 ? 360 ASN B CG  1 
ATOM   2006 O OD1 . ASN B 2 349 ? 147.933 186.676 175.410 1.00 111.08 ? 360 ASN B OD1 1 
ATOM   2007 N ND2 . ASN B 2 349 ? 146.384 186.211 176.964 1.00 111.08 ? 360 ASN B ND2 1 
ATOM   2008 N N   . CYS B 2 350 ? 151.086 183.415 178.505 1.00 112.35 ? 361 CYS B N   1 
ATOM   2009 C CA  . CYS B 2 350 ? 152.189 183.140 179.410 1.00 112.35 ? 361 CYS B CA  1 
ATOM   2010 C C   . CYS B 2 350 ? 152.988 181.961 178.882 1.00 112.35 ? 361 CYS B C   1 
ATOM   2011 O O   . CYS B 2 350 ? 152.502 181.171 178.071 1.00 112.35 ? 361 CYS B O   1 
ATOM   2012 C CB  . CYS B 2 350 ? 151.691 182.855 180.828 1.00 112.35 ? 361 CYS B CB  1 
ATOM   2013 S SG  . CYS B 2 350 ? 150.543 181.477 180.941 1.00 112.35 ? 361 CYS B SG  1 
ATOM   2014 N N   . VAL B 2 351 ? 154.221 181.850 179.354 1.00 107.93 ? 362 VAL B N   1 
ATOM   2015 C CA  . VAL B 2 351 ? 155.083 180.733 178.998 1.00 107.93 ? 362 VAL B CA  1 
ATOM   2016 C C   . VAL B 2 351 ? 155.011 179.693 180.106 1.00 107.93 ? 362 VAL B C   1 
ATOM   2017 O O   . VAL B 2 351 ? 155.204 180.008 181.285 1.00 107.93 ? 362 VAL B O   1 
ATOM   2018 C CB  . VAL B 2 351 ? 156.525 181.206 178.751 1.00 107.93 ? 362 VAL B CB  1 
ATOM   2019 C CG1 . VAL B 2 351 ? 156.563 182.121 177.548 1.00 107.93 ? 362 VAL B CG1 1 
ATOM   2020 C CG2 . VAL B 2 351 ? 157.075 181.934 179.961 1.00 107.93 ? 362 VAL B CG2 1 
ATOM   2021 N N   . ALA B 2 352 ? 154.706 178.457 179.734 1.00 104.66 ? 363 ALA B N   1 
ATOM   2022 C CA  . ALA B 2 352 ? 154.453 177.391 180.691 1.00 104.66 ? 363 ALA B CA  1 
ATOM   2023 C C   . ALA B 2 352 ? 155.644 176.449 180.719 1.00 104.66 ? 363 ALA B C   1 
ATOM   2024 O O   . ALA B 2 352 ? 156.005 175.870 179.690 1.00 104.66 ? 363 ALA B O   1 
ATOM   2025 C CB  . ALA B 2 352 ? 153.178 176.631 180.333 1.00 104.66 ? 363 ALA B CB  1 
ATOM   2026 N N   . ASP B 2 353 ? 156.245 176.291 181.892 1.00 104.66 ? 364 ASP B N   1 
ATOM   2027 C CA  . ASP B 2 353 ? 157.369 175.380 182.083 1.00 104.66 ? 364 ASP B CA  1 
ATOM   2028 C C   . ASP B 2 353 ? 156.831 174.112 182.730 1.00 104.66 ? 364 ASP B C   1 
ATOM   2029 O O   . ASP B 2 353 ? 156.571 174.080 183.933 1.00 104.66 ? 364 ASP B O   1 
ATOM   2030 C CB  . ASP B 2 353 ? 158.453 176.026 182.938 1.00 104.66 ? 364 ASP B CB  1 
ATOM   2031 C CG  . ASP B 2 353 ? 159.628 175.104 183.180 1.00 104.66 ? 364 ASP B CG  1 
ATOM   2032 O OD1 . ASP B 2 353 ? 159.516 174.206 184.040 1.00 104.66 ? 364 ASP B OD1 1 
ATOM   2033 O OD2 . ASP B 2 353 ? 160.667 175.278 182.511 1.00 104.66 ? 364 ASP B OD2 1 
ATOM   2034 N N   . TYR B 2 354 ? 156.671 173.065 181.932 1.00 104.66 ? 365 TYR B N   1 
ATOM   2035 C CA  . TYR B 2 354 ? 156.122 171.810 182.420 1.00 104.66 ? 365 TYR B CA  1 
ATOM   2036 C C   . TYR B 2 354 ? 157.175 170.878 182.997 1.00 104.66 ? 365 TYR B C   1 
ATOM   2037 O O   . TYR B 2 354 ? 156.827 169.785 183.450 1.00 104.66 ? 365 TYR B O   1 
ATOM   2038 C CB  . TYR B 2 354 ? 155.377 171.093 181.300 1.00 104.66 ? 365 TYR B CB  1 
ATOM   2039 C CG  . TYR B 2 354 ? 154.211 171.866 180.752 1.00 104.66 ? 365 TYR B CG  1 
ATOM   2040 C CD1 . TYR B 2 354 ? 152.995 171.879 181.409 1.00 104.66 ? 365 TYR B CD1 1 
ATOM   2041 C CD2 . TYR B 2 354 ? 154.321 172.574 179.569 1.00 104.66 ? 365 TYR B CD2 1 
ATOM   2042 C CE1 . TYR B 2 354 ? 151.927 172.580 180.908 1.00 104.66 ? 365 TYR B CE1 1 
ATOM   2043 C CE2 . TYR B 2 354 ? 153.257 173.275 179.059 1.00 104.66 ? 365 TYR B CE2 1 
ATOM   2044 C CZ  . TYR B 2 354 ? 152.063 173.276 179.733 1.00 104.66 ? 365 TYR B CZ  1 
ATOM   2045 O OH  . TYR B 2 354 ? 150.999 173.978 179.228 1.00 104.66 ? 365 TYR B OH  1 
ATOM   2046 N N   . SER B 2 355 ? 158.449 171.265 182.982 1.00 104.66 ? 366 SER B N   1 
ATOM   2047 C CA  . SER B 2 355 ? 159.471 170.395 183.551 1.00 104.66 ? 366 SER B CA  1 
ATOM   2048 C C   . SER B 2 355 ? 159.375 170.347 185.068 1.00 104.66 ? 366 SER B C   1 
ATOM   2049 O O   . SER B 2 355 ? 159.627 169.301 185.676 1.00 104.66 ? 366 SER B O   1 
ATOM   2050 C CB  . SER B 2 355 ? 160.859 170.852 183.116 1.00 104.66 ? 366 SER B CB  1 
ATOM   2051 O OG  . SER B 2 355 ? 161.011 170.727 181.714 1.00 104.66 ? 366 SER B OG  1 
ATOM   2052 N N   . VAL B 2 356 ? 159.006 171.463 185.699 1.00 104.66 ? 367 VAL B N   1 
ATOM   2053 C CA  . VAL B 2 356 ? 158.962 171.500 187.158 1.00 104.66 ? 367 VAL B CA  1 
ATOM   2054 C C   . VAL B 2 356 ? 157.907 170.540 187.689 1.00 104.66 ? 367 VAL B C   1 
ATOM   2055 O O   . VAL B 2 356 ? 158.098 169.900 188.729 1.00 104.66 ? 367 VAL B O   1 
ATOM   2056 C CB  . VAL B 2 356 ? 158.725 172.938 187.652 1.00 104.66 ? 367 VAL B CB  1 
ATOM   2057 C CG1 . VAL B 2 356 ? 159.914 173.809 187.301 1.00 104.66 ? 367 VAL B CG1 1 
ATOM   2058 C CG2 . VAL B 2 356 ? 157.451 173.513 187.060 1.00 104.66 ? 367 VAL B CG2 1 
ATOM   2059 N N   . LEU B 2 357 ? 156.780 170.419 186.988 1.00 104.66 ? 368 LEU B N   1 
ATOM   2060 C CA  . LEU B 2 357 ? 155.735 169.512 187.445 1.00 104.66 ? 368 LEU B CA  1 
ATOM   2061 C C   . LEU B 2 357 ? 156.195 168.064 187.394 1.00 104.66 ? 368 LEU B C   1 
ATOM   2062 O O   . LEU B 2 357 ? 155.997 167.314 188.355 1.00 104.66 ? 368 LEU B O   1 
ATOM   2063 C CB  . LEU B 2 357 ? 154.472 169.687 186.609 1.00 104.66 ? 368 LEU B CB  1 
ATOM   2064 C CG  . LEU B 2 357 ? 154.005 171.112 186.358 1.00 104.66 ? 368 LEU B CG  1 
ATOM   2065 C CD1 . LEU B 2 357 ? 152.714 171.093 185.574 1.00 104.66 ? 368 LEU B CD1 1 
ATOM   2066 C CD2 . LEU B 2 357 ? 153.822 171.830 187.673 1.00 104.66 ? 368 LEU B CD2 1 
ATOM   2067 N N   . TYR B 2 358 ? 156.813 167.652 186.288 1.00 104.66 ? 369 TYR B N   1 
ATOM   2068 C CA  . TYR B 2 358 ? 157.068 166.230 186.088 1.00 104.66 ? 369 TYR B CA  1 
ATOM   2069 C C   . TYR B 2 358 ? 158.098 165.697 187.076 1.00 104.66 ? 369 TYR B C   1 
ATOM   2070 O O   . TYR B 2 358 ? 157.922 164.611 187.639 1.00 104.66 ? 369 TYR B O   1 
ATOM   2071 C CB  . TYR B 2 358 ? 157.512 165.961 184.654 1.00 104.66 ? 369 TYR B CB  1 
ATOM   2072 C CG  . TYR B 2 358 ? 157.710 164.491 184.393 1.00 104.66 ? 369 TYR B CG  1 
ATOM   2073 C CD1 . TYR B 2 358 ? 158.951 163.897 184.559 1.00 104.66 ? 369 TYR B CD1 1 
ATOM   2074 C CD2 . TYR B 2 358 ? 156.645 163.687 184.025 1.00 104.66 ? 369 TYR B CD2 1 
ATOM   2075 C CE1 . TYR B 2 358 ? 159.131 162.548 184.335 1.00 104.66 ? 369 TYR B CE1 1 
ATOM   2076 C CE2 . TYR B 2 358 ? 156.813 162.337 183.800 1.00 104.66 ? 369 TYR B CE2 1 
ATOM   2077 C CZ  . TYR B 2 358 ? 158.058 161.772 183.955 1.00 104.66 ? 369 TYR B CZ  1 
ATOM   2078 O OH  . TYR B 2 358 ? 158.233 160.426 183.731 1.00 104.66 ? 369 TYR B OH  1 
ATOM   2079 N N   . ASN B 2 359 ? 159.183 166.431 187.294 1.00 112.39 ? 370 ASN B N   1 
ATOM   2080 C CA  . ASN B 2 359 ? 160.215 165.961 188.218 1.00 112.39 ? 370 ASN B CA  1 
ATOM   2081 C C   . ASN B 2 359 ? 159.963 166.462 189.636 1.00 112.39 ? 370 ASN B C   1 
ATOM   2082 O O   . ASN B 2 359 ? 160.839 167.025 190.288 1.00 112.39 ? 370 ASN B O   1 
ATOM   2083 C CB  . ASN B 2 359 ? 161.594 166.377 187.723 1.00 112.39 ? 370 ASN B CB  1 
ATOM   2084 C CG  . ASN B 2 359 ? 161.690 167.858 187.434 1.00 112.39 ? 370 ASN B CG  1 
ATOM   2085 O OD1 . ASN B 2 359 ? 160.969 168.668 188.014 1.00 112.39 ? 370 ASN B OD1 1 
ATOM   2086 N ND2 . ASN B 2 359 ? 162.592 168.221 186.532 1.00 112.39 ? 370 ASN B ND2 1 
ATOM   2087 N N   . SER B 2 360 ? 158.744 166.247 190.123 1.00 111.76 ? 371 SER B N   1 
ATOM   2088 C CA  . SER B 2 360 ? 158.367 166.637 191.473 1.00 111.76 ? 371 SER B CA  1 
ATOM   2089 C C   . SER B 2 360 ? 158.267 165.467 192.433 1.00 111.76 ? 371 SER B C   1 
ATOM   2090 O O   . SER B 2 360 ? 158.446 165.659 193.637 1.00 111.76 ? 371 SER B O   1 
ATOM   2091 C CB  . SER B 2 360 ? 157.026 167.378 191.459 1.00 111.76 ? 371 SER B CB  1 
ATOM   2092 O OG  . SER B 2 360 ? 156.599 167.668 192.777 1.00 111.76 ? 371 SER B OG  1 
ATOM   2093 N N   . ALA B 2 361 ? 157.952 164.272 191.931 1.00 110.03 ? 372 ALA B N   1 
ATOM   2094 C CA  . ALA B 2 361 ? 157.903 163.047 192.723 1.00 110.03 ? 372 ALA B CA  1 
ATOM   2095 C C   . ALA B 2 361 ? 156.841 163.108 193.814 1.00 110.03 ? 372 ALA B C   1 
ATOM   2096 O O   . ALA B 2 361 ? 156.713 162.175 194.611 1.00 110.03 ? 372 ALA B O   1 
ATOM   2097 C CB  . ALA B 2 361 ? 159.273 162.745 193.336 1.00 110.03 ? 372 ALA B CB  1 
ATOM   2098 N N   . SER B 2 362 ? 156.078 164.195 193.862 1.00 104.66 ? 373 SER B N   1 
ATOM   2099 C CA  . SER B 2 362 ? 154.986 164.331 194.811 1.00 104.66 ? 373 SER B CA  1 
ATOM   2100 C C   . SER B 2 362 ? 153.637 163.981 194.205 1.00 104.66 ? 373 SER B C   1 
ATOM   2101 O O   . SER B 2 362 ? 152.616 164.121 194.882 1.00 104.66 ? 373 SER B O   1 
ATOM   2102 C CB  . SER B 2 362 ? 154.951 165.753 195.377 1.00 104.66 ? 373 SER B CB  1 
ATOM   2103 O OG  . SER B 2 362 ? 154.680 166.701 194.362 1.00 104.66 ? 373 SER B OG  1 
ATOM   2104 N N   . PHE B 2 363 ? 153.606 163.533 192.954 1.00 104.66 ? 374 PHE B N   1 
ATOM   2105 C CA  . PHE B 2 363 ? 152.375 163.145 192.285 1.00 104.66 ? 374 PHE B CA  1 
ATOM   2106 C C   . PHE B 2 363 ? 152.318 161.631 192.175 1.00 104.66 ? 374 PHE B C   1 
ATOM   2107 O O   . PHE B 2 363 ? 153.272 161.002 191.711 1.00 104.66 ? 374 PHE B O   1 
ATOM   2108 C CB  . PHE B 2 363 ? 152.275 163.778 190.898 1.00 104.66 ? 374 PHE B CB  1 
ATOM   2109 C CG  . PHE B 2 363 ? 152.299 165.272 190.916 1.00 104.66 ? 374 PHE B CG  1 
ATOM   2110 C CD1 . PHE B 2 363 ? 151.584 165.974 191.861 1.00 104.66 ? 374 PHE B CD1 1 
ATOM   2111 C CD2 . PHE B 2 363 ? 153.028 165.975 189.984 1.00 104.66 ? 374 PHE B CD2 1 
ATOM   2112 C CE1 . PHE B 2 363 ? 151.604 167.348 191.882 1.00 104.66 ? 374 PHE B CE1 1 
ATOM   2113 C CE2 . PHE B 2 363 ? 153.048 167.348 190.001 1.00 104.66 ? 374 PHE B CE2 1 
ATOM   2114 C CZ  . PHE B 2 363 ? 152.334 168.034 190.952 1.00 104.66 ? 374 PHE B CZ  1 
ATOM   2115 N N   . SER B 2 364 ? 151.199 161.052 192.606 1.00 104.66 ? 375 SER B N   1 
ATOM   2116 C CA  . SER B 2 364 ? 151.041 159.606 192.526 1.00 104.66 ? 375 SER B CA  1 
ATOM   2117 C C   . SER B 2 364 ? 150.843 159.145 191.089 1.00 104.66 ? 375 SER B C   1 
ATOM   2118 O O   . SER B 2 364 ? 151.399 158.122 190.680 1.00 104.66 ? 375 SER B O   1 
ATOM   2119 C CB  . SER B 2 364 ? 149.866 159.164 193.391 1.00 104.66 ? 375 SER B CB  1 
ATOM   2120 O OG  . SER B 2 364 ? 149.640 157.775 193.257 1.00 104.66 ? 375 SER B OG  1 
ATOM   2121 N N   . THR B 2 365 ? 150.054 159.881 190.312 1.00 104.66 ? 376 THR B N   1 
ATOM   2122 C CA  . THR B 2 365 ? 149.702 159.492 188.953 1.00 104.66 ? 376 THR B CA  1 
ATOM   2123 C C   . THR B 2 365 ? 149.922 160.665 188.015 1.00 104.66 ? 376 THR B C   1 
ATOM   2124 O O   . THR B 2 365 ? 149.457 161.774 188.287 1.00 104.66 ? 376 THR B O   1 
ATOM   2125 C CB  . THR B 2 365 ? 148.246 159.029 188.876 1.00 104.66 ? 376 THR B CB  1 
ATOM   2126 O OG1 . THR B 2 365 ? 148.132 157.714 189.433 1.00 104.66 ? 376 THR B OG1 1 
ATOM   2127 C CG2 . THR B 2 365 ? 147.759 159.015 187.440 1.00 104.66 ? 376 THR B CG2 1 
ATOM   2128 N N   . PHE B 2 366 ? 150.622 160.417 186.910 1.00 104.66 ? 377 PHE B N   1 
ATOM   2129 C CA  . PHE B 2 366 ? 150.854 161.426 185.876 1.00 104.66 ? 377 PHE B CA  1 
ATOM   2130 C C   . PHE B 2 366 ? 150.749 160.709 184.534 1.00 104.66 ? 377 PHE B C   1 
ATOM   2131 O O   . PHE B 2 366 ? 151.738 160.184 184.023 1.00 104.66 ? 377 PHE B O   1 
ATOM   2132 C CB  . PHE B 2 366 ? 152.207 162.094 186.046 1.00 104.66 ? 377 PHE B CB  1 
ATOM   2133 C CG  . PHE B 2 366 ? 152.339 163.382 185.303 1.00 104.66 ? 377 PHE B CG  1 
ATOM   2134 C CD1 . PHE B 2 366 ? 152.224 164.586 185.958 1.00 104.66 ? 377 PHE B CD1 1 
ATOM   2135 C CD2 . PHE B 2 366 ? 152.562 163.388 183.947 1.00 104.66 ? 377 PHE B CD2 1 
ATOM   2136 C CE1 . PHE B 2 366 ? 152.345 165.768 185.276 1.00 104.66 ? 377 PHE B CE1 1 
ATOM   2137 C CE2 . PHE B 2 366 ? 152.680 164.571 183.263 1.00 104.66 ? 377 PHE B CE2 1 
ATOM   2138 C CZ  . PHE B 2 366 ? 152.570 165.761 183.929 1.00 104.66 ? 377 PHE B CZ  1 
ATOM   2139 N N   . LYS B 2 367 ? 149.553 160.704 183.961 1.00 104.66 ? 378 LYS B N   1 
ATOM   2140 C CA  . LYS B 2 367 ? 149.280 159.955 182.746 1.00 104.66 ? 378 LYS B CA  1 
ATOM   2141 C C   . LYS B 2 367 ? 148.841 160.917 181.655 1.00 104.66 ? 378 LYS B C   1 
ATOM   2142 O O   . LYS B 2 367 ? 148.024 161.807 181.902 1.00 104.66 ? 378 LYS B O   1 
ATOM   2143 C CB  . LYS B 2 367 ? 148.215 158.895 183.002 1.00 104.66 ? 378 LYS B CB  1 
ATOM   2144 C CG  . LYS B 2 367 ? 147.940 157.995 181.822 1.00 104.66 ? 378 LYS B CG  1 
ATOM   2145 C CD  . LYS B 2 367 ? 147.014 156.845 182.192 1.00 104.66 ? 378 LYS B CD  1 
ATOM   2146 C CE  . LYS B 2 367 ? 147.295 156.260 183.575 1.00 104.66 ? 378 LYS B CE  1 
ATOM   2147 N NZ  . LYS B 2 367 ? 148.736 155.982 183.838 1.00 104.66 ? 378 LYS B NZ  1 
ATOM   2148 N N   . CYS B 2 368 ? 149.384 160.741 180.455 1.00 104.66 ? 379 CYS B N   1 
ATOM   2149 C CA  . CYS B 2 368 ? 149.163 161.664 179.352 1.00 104.66 ? 379 CYS B CA  1 
ATOM   2150 C C   . CYS B 2 368 ? 148.621 160.914 178.146 1.00 104.66 ? 379 CYS B C   1 
ATOM   2151 O O   . CYS B 2 368 ? 149.178 159.889 177.747 1.00 104.66 ? 379 CYS B O   1 
ATOM   2152 C CB  . CYS B 2 368 ? 150.456 162.385 178.988 1.00 104.66 ? 379 CYS B CB  1 
ATOM   2153 S SG  . CYS B 2 368 ? 150.970 163.633 180.174 1.00 104.66 ? 379 CYS B SG  1 
ATOM   2154 N N   . TYR B 2 369 ? 147.548 161.440 177.561 1.00 104.66 ? 380 TYR B N   1 
ATOM   2155 C CA  . TYR B 2 369 ? 146.864 160.827 176.429 1.00 104.66 ? 380 TYR B CA  1 
ATOM   2156 C C   . TYR B 2 369 ? 147.074 161.682 175.190 1.00 104.66 ? 380 TYR B C   1 
ATOM   2157 O O   . TYR B 2 369 ? 146.839 162.894 175.224 1.00 104.66 ? 380 TYR B O   1 
ATOM   2158 C CB  . TYR B 2 369 ? 145.371 160.674 176.708 1.00 104.66 ? 380 TYR B CB  1 
ATOM   2159 C CG  . TYR B 2 369 ? 145.060 159.962 177.994 1.00 104.66 ? 380 TYR B CG  1 
ATOM   2160 C CD1 . TYR B 2 369 ? 144.917 158.588 178.028 1.00 104.66 ? 380 TYR B CD1 1 
ATOM   2161 C CD2 . TYR B 2 369 ? 144.908 160.664 179.172 1.00 104.66 ? 380 TYR B CD2 1 
ATOM   2162 C CE1 . TYR B 2 369 ? 144.635 157.935 179.198 1.00 104.66 ? 380 TYR B CE1 1 
ATOM   2163 C CE2 . TYR B 2 369 ? 144.627 160.019 180.346 1.00 104.66 ? 380 TYR B CE2 1 
ATOM   2164 C CZ  . TYR B 2 369 ? 144.492 158.654 180.355 1.00 104.66 ? 380 TYR B CZ  1 
ATOM   2165 O OH  . TYR B 2 369 ? 144.205 158.008 181.531 1.00 104.66 ? 380 TYR B OH  1 
ATOM   2166 N N   . GLY B 2 370 ? 147.507 161.053 174.099 1.00 104.66 ? 381 GLY B N   1 
ATOM   2167 C CA  . GLY B 2 370 ? 147.696 161.738 172.839 1.00 104.66 ? 381 GLY B CA  1 
ATOM   2168 C C   . GLY B 2 370 ? 148.912 162.631 172.763 1.00 104.66 ? 381 GLY B C   1 
ATOM   2169 O O   . GLY B 2 370 ? 149.301 163.023 171.657 1.00 104.66 ? 381 GLY B O   1 
ATOM   2170 N N   . VAL B 2 371 ? 149.521 162.974 173.894 1.00 104.66 ? 382 VAL B N   1 
ATOM   2171 C CA  . VAL B 2 371 ? 150.704 163.823 173.938 1.00 104.66 ? 382 VAL B CA  1 
ATOM   2172 C C   . VAL B 2 371 ? 151.658 163.250 174.973 1.00 104.66 ? 382 VAL B C   1 
ATOM   2173 O O   . VAL B 2 371 ? 151.240 162.924 176.087 1.00 104.66 ? 382 VAL B O   1 
ATOM   2174 C CB  . VAL B 2 371 ? 150.344 165.278 174.285 1.00 104.66 ? 382 VAL B CB  1 
ATOM   2175 C CG1 . VAL B 2 371 ? 151.561 166.016 174.746 1.00 104.66 ? 382 VAL B CG1 1 
ATOM   2176 C CG2 . VAL B 2 371 ? 149.744 165.964 173.085 1.00 104.66 ? 382 VAL B CG2 1 
ATOM   2177 N N   . SER B 2 372 ? 152.932 163.133 174.616 1.00 104.66 ? 383 SER B N   1 
ATOM   2178 C CA  . SER B 2 372 ? 153.822 162.513 175.588 1.00 104.66 ? 383 SER B CA  1 
ATOM   2179 C C   . SER B 2 372 ? 154.556 163.563 176.408 1.00 104.66 ? 383 SER B C   1 
ATOM   2180 O O   . SER B 2 372 ? 154.984 164.584 175.863 1.00 104.66 ? 383 SER B O   1 
ATOM   2181 C CB  . SER B 2 372 ? 154.847 161.625 174.884 1.00 104.66 ? 383 SER B CB  1 
ATOM   2182 O OG  . SER B 2 372 ? 155.879 161.243 175.772 1.00 104.66 ? 383 SER B OG  1 
ATOM   2183 N N   . PRO B 2 373 ? 154.731 163.344 177.719 1.00 104.66 ? 384 PRO B N   1 
ATOM   2184 C CA  . PRO B 2 373 ? 155.507 164.292 178.526 1.00 104.66 ? 384 PRO B CA  1 
ATOM   2185 C C   . PRO B 2 373 ? 156.975 164.253 178.153 1.00 104.66 ? 384 PRO B C   1 
ATOM   2186 O O   . PRO B 2 373 ? 157.371 163.458 177.297 1.00 104.66 ? 384 PRO B O   1 
ATOM   2187 C CB  . PRO B 2 373 ? 155.276 163.810 179.960 1.00 104.66 ? 384 PRO B CB  1 
ATOM   2188 C CG  . PRO B 2 373 ? 154.968 162.373 179.818 1.00 104.66 ? 384 PRO B CG  1 
ATOM   2189 C CD  . PRO B 2 373 ? 154.225 162.223 178.525 1.00 104.66 ? 384 PRO B CD  1 
ATOM   2190 N N   . THR B 2 374 ? 157.784 165.102 178.782 1.00 104.66 ? 385 THR B N   1 
ATOM   2191 C CA  . THR B 2 374 ? 159.189 165.343 178.463 1.00 104.66 ? 385 THR B CA  1 
ATOM   2192 C C   . THR B 2 374 ? 159.359 166.040 177.122 1.00 104.66 ? 385 THR B C   1 
ATOM   2193 O O   . THR B 2 374 ? 160.488 166.373 176.752 1.00 104.66 ? 385 THR B O   1 
ATOM   2194 C CB  . THR B 2 374 ? 160.042 164.066 178.459 1.00 104.66 ? 385 THR B CB  1 
ATOM   2195 O OG1 . THR B 2 374 ? 159.785 163.327 177.261 1.00 104.66 ? 385 THR B OG1 1 
ATOM   2196 C CG2 . THR B 2 374 ? 159.723 163.196 179.663 1.00 104.66 ? 385 THR B CG2 1 
ATOM   2197 N N   . LYS B 2 375 ? 158.280 166.261 176.378 1.00 104.66 ? 386 LYS B N   1 
ATOM   2198 C CA  . LYS B 2 375 ? 158.292 167.108 175.199 1.00 104.66 ? 386 LYS B CA  1 
ATOM   2199 C C   . LYS B 2 375 ? 157.327 168.273 175.332 1.00 104.66 ? 386 LYS B C   1 
ATOM   2200 O O   . LYS B 2 375 ? 157.195 169.062 174.391 1.00 104.66 ? 386 LYS B O   1 
ATOM   2201 C CB  . LYS B 2 375 ? 157.947 166.298 173.944 1.00 104.66 ? 386 LYS B CB  1 
ATOM   2202 C CG  . LYS B 2 375 ? 158.988 165.265 173.570 1.00 104.66 ? 386 LYS B CG  1 
ATOM   2203 C CD  . LYS B 2 375 ? 158.664 164.618 172.235 1.00 104.66 ? 386 LYS B CD  1 
ATOM   2204 C CE  . LYS B 2 375 ? 157.501 163.652 172.362 1.00 104.66 ? 386 LYS B CE  1 
ATOM   2205 N NZ  . LYS B 2 375 ? 157.235 162.924 171.091 1.00 104.66 ? 386 LYS B NZ  1 
ATOM   2206 N N   . LEU B 2 376 ? 156.646 168.396 176.470 1.00 104.66 ? 387 LEU B N   1 
ATOM   2207 C CA  . LEU B 2 376 ? 155.684 169.468 176.663 1.00 104.66 ? 387 LEU B CA  1 
ATOM   2208 C C   . LEU B 2 376 ? 156.336 170.838 176.713 1.00 104.66 ? 387 LEU B C   1 
ATOM   2209 O O   . LEU B 2 376 ? 155.651 171.840 176.495 1.00 104.66 ? 387 LEU B O   1 
ATOM   2210 C CB  . LEU B 2 376 ? 154.897 169.227 177.946 1.00 104.66 ? 387 LEU B CB  1 
ATOM   2211 C CG  . LEU B 2 376 ? 153.827 168.154 177.838 1.00 104.66 ? 387 LEU B CG  1 
ATOM   2212 C CD1 . LEU B 2 376 ? 153.072 168.024 179.139 1.00 104.66 ? 387 LEU B CD1 1 
ATOM   2213 C CD2 . LEU B 2 376 ? 152.899 168.551 176.735 1.00 104.66 ? 387 LEU B CD2 1 
ATOM   2214 N N   . ASN B 2 377 ? 157.631 170.914 177.013 1.00 104.66 ? 388 ASN B N   1 
ATOM   2215 C CA  . ASN B 2 377 ? 158.285 172.215 177.037 1.00 104.66 ? 388 ASN B CA  1 
ATOM   2216 C C   . ASN B 2 377 ? 158.380 172.814 175.642 1.00 104.66 ? 388 ASN B C   1 
ATOM   2217 O O   . ASN B 2 377 ? 158.564 174.027 175.503 1.00 104.66 ? 388 ASN B O   1 
ATOM   2218 C CB  . ASN B 2 377 ? 159.663 172.100 177.676 1.00 104.66 ? 388 ASN B CB  1 
ATOM   2219 C CG  . ASN B 2 377 ? 160.472 170.972 177.098 1.00 104.66 ? 388 ASN B CG  1 
ATOM   2220 O OD1 . ASN B 2 377 ? 160.201 170.504 175.994 1.00 104.66 ? 388 ASN B OD1 1 
ATOM   2221 N ND2 . ASN B 2 377 ? 161.472 170.520 177.842 1.00 104.66 ? 388 ASN B ND2 1 
ATOM   2222 N N   . ASP B 2 378 ? 158.272 171.989 174.606 1.00 104.66 ? 389 ASP B N   1 
ATOM   2223 C CA  . ASP B 2 378 ? 158.084 172.466 173.245 1.00 104.66 ? 389 ASP B CA  1 
ATOM   2224 C C   . ASP B 2 378 ? 156.586 172.521 172.951 1.00 104.66 ? 389 ASP B C   1 
ATOM   2225 O O   . ASP B 2 378 ? 155.760 172.450 173.864 1.00 104.66 ? 389 ASP B O   1 
ATOM   2226 C CB  . ASP B 2 378 ? 158.835 171.578 172.261 1.00 104.66 ? 389 ASP B CB  1 
ATOM   2227 C CG  . ASP B 2 378 ? 160.300 171.460 172.598 1.00 104.66 ? 389 ASP B CG  1 
ATOM   2228 O OD1 . ASP B 2 378 ? 160.729 172.097 173.583 1.00 104.66 ? 389 ASP B OD1 1 
ATOM   2229 O OD2 . ASP B 2 378 ? 161.021 170.734 171.884 1.00 104.66 ? 389 ASP B OD2 1 
ATOM   2230 N N   . LEU B 2 379 ? 156.223 172.670 171.674 1.00 104.66 ? 390 LEU B N   1 
ATOM   2231 C CA  . LEU B 2 379 ? 154.831 172.695 171.228 1.00 104.66 ? 390 LEU B CA  1 
ATOM   2232 C C   . LEU B 2 379 ? 154.140 173.970 171.684 1.00 104.66 ? 390 LEU B C   1 
ATOM   2233 O O   . LEU B 2 379 ? 154.406 174.460 172.781 1.00 104.66 ? 390 LEU B O   1 
ATOM   2234 C CB  . LEU B 2 379 ? 154.054 171.482 171.748 1.00 104.66 ? 390 LEU B CB  1 
ATOM   2235 C CG  . LEU B 2 379 ? 154.266 170.097 171.145 1.00 104.66 ? 390 LEU B CG  1 
ATOM   2236 C CD1 . LEU B 2 379 ? 155.597 169.511 171.566 1.00 104.66 ? 390 LEU B CD1 1 
ATOM   2237 C CD2 . LEU B 2 379 ? 153.136 169.189 171.581 1.00 104.66 ? 390 LEU B CD2 1 
ATOM   2238 N N   . CYS B 2 380 ? 153.241 174.510 170.866 1.00 104.66 ? 391 CYS B N   1 
ATOM   2239 C CA  . CYS B 2 380 ? 152.465 175.681 171.246 1.00 104.66 ? 391 CYS B CA  1 
ATOM   2240 C C   . CYS B 2 380 ? 150.984 175.356 171.147 1.00 104.66 ? 391 CYS B C   1 
ATOM   2241 O O   . CYS B 2 380 ? 150.553 174.689 170.202 1.00 104.66 ? 391 CYS B O   1 
ATOM   2242 C CB  . CYS B 2 380 ? 152.812 176.904 170.384 1.00 104.66 ? 391 CYS B CB  1 
ATOM   2243 S SG  . CYS B 2 380 ? 154.482 177.612 170.633 1.00 104.66 ? 391 CYS B SG  1 
ATOM   2244 N N   . PHE B 2 381 ? 150.215 175.824 172.123 1.00 104.66 ? 392 PHE B N   1 
ATOM   2245 C CA  . PHE B 2 381 ? 148.795 175.540 172.227 1.00 104.66 ? 392 PHE B CA  1 
ATOM   2246 C C   . PHE B 2 381 ? 147.987 176.815 172.035 1.00 104.66 ? 392 PHE B C   1 
ATOM   2247 O O   . PHE B 2 381 ? 148.447 177.920 172.327 1.00 104.66 ? 392 PHE B O   1 
ATOM   2248 C CB  . PHE B 2 381 ? 148.460 174.938 173.588 1.00 104.66 ? 392 PHE B CB  1 
ATOM   2249 C CG  . PHE B 2 381 ? 149.306 173.774 173.951 1.00 104.66 ? 392 PHE B CG  1 
ATOM   2250 C CD1 . PHE B 2 381 ? 149.076 172.539 173.397 1.00 104.66 ? 392 PHE B CD1 1 
ATOM   2251 C CD2 . PHE B 2 381 ? 150.336 173.913 174.856 1.00 104.66 ? 392 PHE B CD2 1 
ATOM   2252 C CE1 . PHE B 2 381 ? 149.855 171.464 173.738 1.00 104.66 ? 392 PHE B CE1 1 
ATOM   2253 C CE2 . PHE B 2 381 ? 151.121 172.844 175.201 1.00 104.66 ? 392 PHE B CE2 1 
ATOM   2254 C CZ  . PHE B 2 381 ? 150.880 171.617 174.640 1.00 104.66 ? 392 PHE B CZ  1 
ATOM   2255 N N   . THR B 2 382 ? 146.758 176.646 171.550 1.00 104.66 ? 393 THR B N   1 
ATOM   2256 C CA  . THR B 2 382 ? 145.856 177.785 171.435 1.00 104.66 ? 393 THR B CA  1 
ATOM   2257 C C   . THR B 2 382 ? 145.458 178.289 172.813 1.00 104.66 ? 393 THR B C   1 
ATOM   2258 O O   . THR B 2 382 ? 145.721 179.443 173.165 1.00 104.66 ? 393 THR B O   1 
ATOM   2259 C CB  . THR B 2 382 ? 144.623 177.399 170.622 1.00 104.66 ? 393 THR B CB  1 
ATOM   2260 O OG1 . THR B 2 382 ? 145.009 177.108 169.274 1.00 104.66 ? 393 THR B OG1 1 
ATOM   2261 C CG2 . THR B 2 382 ? 143.615 178.531 170.622 1.00 104.66 ? 393 THR B CG2 1 
ATOM   2262 N N   . ASN B 2 383 ? 144.821 177.433 173.609 1.00 104.66 ? 394 ASN B N   1 
ATOM   2263 C CA  . ASN B 2 383 ? 144.574 177.718 175.015 1.00 104.66 ? 394 ASN B CA  1 
ATOM   2264 C C   . ASN B 2 383 ? 144.415 176.404 175.758 1.00 104.66 ? 394 ASN B C   1 
ATOM   2265 O O   . ASN B 2 383 ? 143.989 175.398 175.190 1.00 104.66 ? 394 ASN B O   1 
ATOM   2266 C CB  . ASN B 2 383 ? 143.340 178.599 175.211 1.00 104.66 ? 394 ASN B CB  1 
ATOM   2267 C CG  . ASN B 2 383 ? 143.695 180.055 175.392 1.00 104.66 ? 394 ASN B CG  1 
ATOM   2268 O OD1 . ASN B 2 383 ? 144.505 180.401 176.248 1.00 104.66 ? 394 ASN B OD1 1 
ATOM   2269 N ND2 . ASN B 2 383 ? 143.094 180.919 174.584 1.00 104.66 ? 394 ASN B ND2 1 
ATOM   2270 N N   . VAL B 2 384 ? 144.753 176.423 177.042 1.00 104.66 ? 395 VAL B N   1 
ATOM   2271 C CA  . VAL B 2 384 ? 144.686 175.230 177.868 1.00 104.66 ? 395 VAL B CA  1 
ATOM   2272 C C   . VAL B 2 384 ? 143.563 175.397 178.878 1.00 104.66 ? 395 VAL B C   1 
ATOM   2273 O O   . VAL B 2 384 ? 142.945 176.456 178.989 1.00 104.66 ? 395 VAL B O   1 
ATOM   2274 C CB  . VAL B 2 384 ? 146.015 174.941 178.583 1.00 104.66 ? 395 VAL B CB  1 
ATOM   2275 C CG1 . VAL B 2 384 ? 147.140 174.906 177.587 1.00 104.66 ? 395 VAL B CG1 1 
ATOM   2276 C CG2 . VAL B 2 384 ? 146.272 175.982 179.626 1.00 104.66 ? 395 VAL B CG2 1 
ATOM   2277 N N   . TYR B 2 385 ? 143.289 174.325 179.609 1.00 104.66 ? 396 TYR B N   1 
ATOM   2278 C CA  . TYR B 2 385 ? 142.248 174.322 180.622 1.00 104.66 ? 396 TYR B CA  1 
ATOM   2279 C C   . TYR B 2 385 ? 142.716 173.536 181.831 1.00 104.66 ? 396 TYR B C   1 
ATOM   2280 O O   . TYR B 2 385 ? 143.426 172.539 181.691 1.00 104.66 ? 396 TYR B O   1 
ATOM   2281 C CB  . TYR B 2 385 ? 140.973 173.721 180.074 1.00 104.66 ? 396 TYR B CB  1 
ATOM   2282 C CG  . TYR B 2 385 ? 140.159 174.703 179.291 1.00 104.66 ? 396 TYR B CG  1 
ATOM   2283 C CD1 . TYR B 2 385 ? 139.602 175.806 179.904 1.00 104.66 ? 396 TYR B CD1 1 
ATOM   2284 C CD2 . TYR B 2 385 ? 139.968 174.542 177.931 1.00 104.66 ? 396 TYR B CD2 1 
ATOM   2285 C CE1 . TYR B 2 385 ? 138.857 176.708 179.195 1.00 104.66 ? 396 TYR B CE1 1 
ATOM   2286 C CE2 . TYR B 2 385 ? 139.230 175.444 177.210 1.00 104.66 ? 396 TYR B CE2 1 
ATOM   2287 C CZ  . TYR B 2 385 ? 138.677 176.528 177.846 1.00 104.66 ? 396 TYR B CZ  1 
ATOM   2288 O OH  . TYR B 2 385 ? 137.936 177.436 177.130 1.00 104.66 ? 396 TYR B OH  1 
ATOM   2289 N N   . ALA B 2 386 ? 142.318 173.981 183.016 1.00 104.66 ? 397 ALA B N   1 
ATOM   2290 C CA  . ALA B 2 386 ? 142.667 173.305 184.259 1.00 104.66 ? 397 ALA B CA  1 
ATOM   2291 C C   . ALA B 2 386 ? 141.387 172.996 185.018 1.00 104.66 ? 397 ALA B C   1 
ATOM   2292 O O   . ALA B 2 386 ? 140.713 173.909 185.505 1.00 104.66 ? 397 ALA B O   1 
ATOM   2293 C CB  . ALA B 2 386 ? 143.613 174.156 185.098 1.00 104.66 ? 397 ALA B CB  1 
ATOM   2294 N N   . ASP B 2 387 ? 141.055 171.716 185.120 1.00 104.66 ? 398 ASP B N   1 
ATOM   2295 C CA  . ASP B 2 387 ? 139.883 171.250 185.845 1.00 104.66 ? 398 ASP B CA  1 
ATOM   2296 C C   . ASP B 2 387 ? 140.345 170.601 187.138 1.00 104.66 ? 398 ASP B C   1 
ATOM   2297 O O   . ASP B 2 387 ? 141.210 169.723 187.112 1.00 104.66 ? 398 ASP B O   1 
ATOM   2298 C CB  . ASP B 2 387 ? 139.098 170.246 185.005 1.00 104.66 ? 398 ASP B CB  1 
ATOM   2299 C CG  . ASP B 2 387 ? 138.509 170.868 183.766 1.00 104.66 ? 398 ASP B CG  1 
ATOM   2300 O OD1 . ASP B 2 387 ? 138.200 172.073 183.801 1.00 104.66 ? 398 ASP B OD1 1 
ATOM   2301 O OD2 . ASP B 2 387 ? 138.363 170.160 182.751 1.00 104.66 ? 398 ASP B OD2 1 
ATOM   2302 N N   . SER B 2 388 ? 139.776 171.020 188.262 1.00 104.66 ? 399 SER B N   1 
ATOM   2303 C CA  . SER B 2 388 ? 140.232 170.547 189.560 1.00 104.66 ? 399 SER B CA  1 
ATOM   2304 C C   . SER B 2 388 ? 139.056 170.140 190.433 1.00 104.66 ? 399 SER B C   1 
ATOM   2305 O O   . SER B 2 388 ? 137.989 170.754 190.378 1.00 104.66 ? 399 SER B O   1 
ATOM   2306 C CB  . SER B 2 388 ? 141.055 171.618 190.264 1.00 104.66 ? 399 SER B CB  1 
ATOM   2307 O OG  . SER B 2 388 ? 140.323 172.822 190.370 1.00 104.66 ? 399 SER B OG  1 
ATOM   2308 N N   . PHE B 2 389 ? 139.265 169.104 191.239 1.00 104.66 ? 400 PHE B N   1 
ATOM   2309 C CA  . PHE B 2 389 ? 138.265 168.602 192.176 1.00 104.66 ? 400 PHE B CA  1 
ATOM   2310 C C   . PHE B 2 389 ? 138.955 167.607 193.102 1.00 104.66 ? 400 PHE B C   1 
ATOM   2311 O O   . PHE B 2 389 ? 140.174 167.430 193.051 1.00 104.66 ? 400 PHE B O   1 
ATOM   2312 C CB  . PHE B 2 389 ? 137.086 167.967 191.446 1.00 104.66 ? 400 PHE B CB  1 
ATOM   2313 C CG  . PHE B 2 389 ? 137.485 167.092 190.304 1.00 104.66 ? 400 PHE B CG  1 
ATOM   2314 C CD1 . PHE B 2 389 ? 137.833 165.777 190.515 1.00 104.66 ? 400 PHE B CD1 1 
ATOM   2315 C CD2 . PHE B 2 389 ? 137.498 167.579 189.017 1.00 104.66 ? 400 PHE B CD2 1 
ATOM   2316 C CE1 . PHE B 2 389 ? 138.189 164.970 189.467 1.00 104.66 ? 400 PHE B CE1 1 
ATOM   2317 C CE2 . PHE B 2 389 ? 137.856 166.774 187.967 1.00 104.66 ? 400 PHE B CE2 1 
ATOM   2318 C CZ  . PHE B 2 389 ? 138.202 165.469 188.193 1.00 104.66 ? 400 PHE B CZ  1 
ATOM   2319 N N   . VAL B 2 390 ? 138.167 166.960 193.957 1.00 104.66 ? 401 VAL B N   1 
ATOM   2320 C CA  . VAL B 2 390 ? 138.678 165.962 194.891 1.00 104.66 ? 401 VAL B CA  1 
ATOM   2321 C C   . VAL B 2 390 ? 137.719 164.779 194.920 1.00 104.66 ? 401 VAL B C   1 
ATOM   2322 O O   . VAL B 2 390 ? 136.500 164.962 194.985 1.00 104.66 ? 401 VAL B O   1 
ATOM   2323 C CB  . VAL B 2 390 ? 138.879 166.551 196.300 1.00 104.66 ? 401 VAL B CB  1 
ATOM   2324 C CG1 . VAL B 2 390 ? 137.580 167.075 196.851 1.00 104.66 ? 401 VAL B CG1 1 
ATOM   2325 C CG2 . VAL B 2 390 ? 139.451 165.511 197.230 1.00 104.66 ? 401 VAL B CG2 1 
ATOM   2326 N N   . ILE B 2 391 ? 138.264 163.567 194.850 1.00 104.66 ? 402 ILE B N   1 
ATOM   2327 C CA  . ILE B 2 391 ? 137.484 162.339 194.809 1.00 104.66 ? 402 ILE B CA  1 
ATOM   2328 C C   . ILE B 2 391 ? 138.135 161.312 195.727 1.00 104.66 ? 402 ILE B C   1 
ATOM   2329 O O   . ILE B 2 391 ? 139.142 161.581 196.382 1.00 104.66 ? 402 ILE B O   1 
ATOM   2330 C CB  . ILE B 2 391 ? 137.356 161.772 193.382 1.00 104.66 ? 402 ILE B CB  1 
ATOM   2331 C CG1 . ILE B 2 391 ? 138.734 161.497 192.797 1.00 104.66 ? 402 ILE B CG1 1 
ATOM   2332 C CG2 . ILE B 2 391 ? 136.602 162.724 192.495 1.00 104.66 ? 402 ILE B CG2 1 
ATOM   2333 C CD1 . ILE B 2 391 ? 138.687 160.850 191.444 1.00 104.66 ? 402 ILE B CD1 1 
ATOM   2334 N N   . ARG B 2 392 ? 137.546 160.123 195.768 1.00 104.66 ? 403 ARG B N   1 
ATOM   2335 C CA  . ARG B 2 392 ? 138.060 159.032 196.578 1.00 104.66 ? 403 ARG B CA  1 
ATOM   2336 C C   . ARG B 2 392 ? 139.242 158.372 195.882 1.00 104.66 ? 403 ARG B C   1 
ATOM   2337 O O   . ARG B 2 392 ? 139.367 158.410 194.658 1.00 104.66 ? 403 ARG B O   1 
ATOM   2338 C CB  . ARG B 2 392 ? 136.962 158.004 196.837 1.00 104.66 ? 403 ARG B CB  1 
ATOM   2339 C CG  . ARG B 2 392 ? 137.106 157.241 198.133 1.00 104.66 ? 403 ARG B CG  1 
ATOM   2340 C CD  . ARG B 2 392 ? 136.051 156.157 198.237 1.00 104.66 ? 403 ARG B CD  1 
ATOM   2341 N NE  . ARG B 2 392 ? 135.863 155.461 196.971 1.00 104.66 ? 403 ARG B NE  1 
ATOM   2342 C CZ  . ARG B 2 392 ? 135.082 154.402 196.809 1.00 104.66 ? 403 ARG B CZ  1 
ATOM   2343 N NH1 . ARG B 2 392 ? 134.380 153.902 197.810 1.00 104.66 ? 403 ARG B NH1 1 
ATOM   2344 N NH2 . ARG B 2 392 ? 134.999 153.835 195.610 1.00 104.66 ? 403 ARG B NH2 1 
ATOM   2345 N N   . GLY B 2 393 ? 140.111 157.753 196.681 1.00 104.66 ? 404 GLY B N   1 
ATOM   2346 C CA  . GLY B 2 393 ? 141.354 157.229 196.139 1.00 104.66 ? 404 GLY B CA  1 
ATOM   2347 C C   . GLY B 2 393 ? 141.149 156.134 195.111 1.00 104.66 ? 404 GLY B C   1 
ATOM   2348 O O   . GLY B 2 393 ? 141.821 156.104 194.080 1.00 104.66 ? 404 GLY B O   1 
ATOM   2349 N N   . ASP B 2 394 ? 140.223 155.216 195.379 1.00 104.66 ? 405 ASP B N   1 
ATOM   2350 C CA  . ASP B 2 394 ? 140.017 154.093 194.474 1.00 104.66 ? 405 ASP B CA  1 
ATOM   2351 C C   . ASP B 2 394 ? 139.465 154.558 193.133 1.00 104.66 ? 405 ASP B C   1 
ATOM   2352 O O   . ASP B 2 394 ? 139.856 154.032 192.086 1.00 104.66 ? 405 ASP B O   1 
ATOM   2353 C CB  . ASP B 2 394 ? 139.094 153.073 195.146 1.00 104.66 ? 405 ASP B CB  1 
ATOM   2354 C CG  . ASP B 2 394 ? 138.774 151.870 194.269 1.00 104.66 ? 405 ASP B CG  1 
ATOM   2355 O OD1 . ASP B 2 394 ? 138.843 150.741 194.796 1.00 104.66 ? 405 ASP B OD1 1 
ATOM   2356 O OD2 . ASP B 2 394 ? 138.405 152.024 193.088 1.00 104.66 ? 405 ASP B OD2 1 
ATOM   2357 N N   . GLU B 2 395 ? 138.586 155.552 193.143 1.00 104.66 ? 406 GLU B N   1 
ATOM   2358 C CA  . GLU B 2 395 ? 137.847 155.987 191.965 1.00 104.66 ? 406 GLU B CA  1 
ATOM   2359 C C   . GLU B 2 395 ? 138.704 156.717 190.938 1.00 104.66 ? 406 GLU B C   1 
ATOM   2360 O O   . GLU B 2 395 ? 138.159 157.202 189.944 1.00 104.66 ? 406 GLU B O   1 
ATOM   2361 C CB  . GLU B 2 395 ? 136.697 156.887 192.410 1.00 104.66 ? 406 GLU B CB  1 
ATOM   2362 C CG  . GLU B 2 395 ? 135.570 156.134 193.085 1.00 104.66 ? 406 GLU B CG  1 
ATOM   2363 C CD  . GLU B 2 395 ? 134.396 157.022 193.431 1.00 104.66 ? 406 GLU B CD  1 
ATOM   2364 O OE1 . GLU B 2 395 ? 133.628 156.666 194.349 1.00 104.66 ? 406 GLU B OE1 1 
ATOM   2365 O OE2 . GLU B 2 395 ? 134.259 158.094 192.816 1.00 104.66 ? 406 GLU B OE2 1 
ATOM   2366 N N   . VAL B 2 396 ? 140.020 156.803 191.144 1.00 104.66 ? 407 VAL B N   1 
ATOM   2367 C CA  . VAL B 2 396 ? 140.873 157.577 190.245 1.00 104.66 ? 407 VAL B CA  1 
ATOM   2368 C C   . VAL B 2 396 ? 140.902 156.971 188.850 1.00 104.66 ? 407 VAL B C   1 
ATOM   2369 O O   . VAL B 2 396 ? 140.956 157.697 187.852 1.00 104.66 ? 407 VAL B O   1 
ATOM   2370 C CB  . VAL B 2 396 ? 142.290 157.702 190.836 1.00 104.66 ? 407 VAL B CB  1 
ATOM   2371 C CG1 . VAL B 2 396 ? 143.288 158.081 189.763 1.00 104.66 ? 407 VAL B CG1 1 
ATOM   2372 C CG2 . VAL B 2 396 ? 142.303 158.734 191.944 1.00 104.66 ? 407 VAL B CG2 1 
ATOM   2373 N N   . ARG B 2 397 ? 140.842 155.645 188.749 1.00 104.66 ? 408 ARG B N   1 
ATOM   2374 C CA  . ARG B 2 397 ? 140.972 155.006 187.446 1.00 104.66 ? 408 ARG B CA  1 
ATOM   2375 C C   . ARG B 2 397 ? 139.815 155.336 186.513 1.00 104.66 ? 408 ARG B C   1 
ATOM   2376 O O   . ARG B 2 397 ? 139.900 155.046 185.317 1.00 104.66 ? 408 ARG B O   1 
ATOM   2377 C CB  . ARG B 2 397 ? 141.101 153.493 187.614 1.00 104.66 ? 408 ARG B CB  1 
ATOM   2378 C CG  . ARG B 2 397 ? 140.142 152.884 188.614 1.00 104.66 ? 408 ARG B CG  1 
ATOM   2379 C CD  . ARG B 2 397 ? 139.817 151.449 188.244 1.00 104.66 ? 408 ARG B CD  1 
ATOM   2380 N NE  . ARG B 2 397 ? 139.005 151.364 187.037 1.00 104.66 ? 408 ARG B NE  1 
ATOM   2381 C CZ  . ARG B 2 397 ? 137.696 151.567 187.000 1.00 104.66 ? 408 ARG B CZ  1 
ATOM   2382 N NH1 . ARG B 2 397 ? 137.010 151.846 188.096 1.00 104.66 ? 408 ARG B NH1 1 
ATOM   2383 N NH2 . ARG B 2 397 ? 137.058 151.483 185.837 1.00 104.66 ? 408 ARG B NH2 1 
ATOM   2384 N N   . GLN B 2 398 ? 138.740 155.930 187.025 1.00 104.66 ? 409 GLN B N   1 
ATOM   2385 C CA  . GLN B 2 398 ? 137.618 156.305 186.178 1.00 104.66 ? 409 GLN B CA  1 
ATOM   2386 C C   . GLN B 2 398 ? 137.845 157.604 185.422 1.00 104.66 ? 409 GLN B C   1 
ATOM   2387 O O   . GLN B 2 398 ? 137.028 157.946 184.563 1.00 104.66 ? 409 GLN B O   1 
ATOM   2388 C CB  . GLN B 2 398 ? 136.344 156.425 187.012 1.00 104.66 ? 409 GLN B CB  1 
ATOM   2389 C CG  . GLN B 2 398 ? 135.694 155.098 187.332 1.00 104.66 ? 409 GLN B CG  1 
ATOM   2390 C CD  . GLN B 2 398 ? 134.387 155.258 188.069 1.00 104.66 ? 409 GLN B CD  1 
ATOM   2391 O OE1 . GLN B 2 398 ? 133.642 156.204 187.831 1.00 104.66 ? 409 GLN B OE1 1 
ATOM   2392 N NE2 . GLN B 2 398 ? 134.098 154.329 188.969 1.00 104.66 ? 409 GLN B NE2 1 
ATOM   2393 N N   . ILE B 2 399 ? 138.913 158.340 185.720 1.00 104.66 ? 410 ILE B N   1 
ATOM   2394 C CA  . ILE B 2 399 ? 139.220 159.586 185.015 1.00 104.66 ? 410 ILE B CA  1 
ATOM   2395 C C   . ILE B 2 399 ? 140.143 159.214 183.858 1.00 104.66 ? 410 ILE B C   1 
ATOM   2396 O O   . ILE B 2 399 ? 141.366 159.277 183.960 1.00 104.66 ? 410 ILE B O   1 
ATOM   2397 C CB  . ILE B 2 399 ? 139.838 160.629 185.937 1.00 104.66 ? 410 ILE B CB  1 
ATOM   2398 C CG1 . ILE B 2 399 ? 138.939 160.866 187.144 1.00 104.66 ? 410 ILE B CG1 1 
ATOM   2399 C CG2 . ILE B 2 399 ? 140.031 161.927 185.202 1.00 104.66 ? 410 ILE B CG2 1 
ATOM   2400 C CD1 . ILE B 2 399 ? 137.547 161.267 186.779 1.00 104.66 ? 410 ILE B CD1 1 
ATOM   2401 N N   . ALA B 2 400 ? 139.539 158.822 182.741 1.00 104.66 ? 411 ALA B N   1 
ATOM   2402 C CA  . ALA B 2 400 ? 140.251 158.415 181.538 1.00 104.66 ? 411 ALA B CA  1 
ATOM   2403 C C   . ALA B 2 400 ? 139.247 158.243 180.409 1.00 104.66 ? 411 ALA B C   1 
ATOM   2404 O O   . ALA B 2 400 ? 138.080 157.930 180.668 1.00 104.66 ? 411 ALA B O   1 
ATOM   2405 C CB  . ALA B 2 400 ? 141.024 157.117 181.773 1.00 104.66 ? 411 ALA B CB  1 
ATOM   2406 N N   . PRO B 2 401 ? 139.643 158.445 179.156 1.00 104.66 ? 412 PRO B N   1 
ATOM   2407 C CA  . PRO B 2 401 ? 138.685 158.298 178.058 1.00 104.66 ? 412 PRO B CA  1 
ATOM   2408 C C   . PRO B 2 401 ? 138.171 156.872 177.956 1.00 104.66 ? 412 PRO B C   1 
ATOM   2409 O O   . PRO B 2 401 ? 138.911 155.910 178.160 1.00 104.66 ? 412 PRO B O   1 
ATOM   2410 C CB  . PRO B 2 401 ? 139.500 158.690 176.823 1.00 104.66 ? 412 PRO B CB  1 
ATOM   2411 C CG  . PRO B 2 401 ? 140.903 158.475 177.217 1.00 104.66 ? 412 PRO B CG  1 
ATOM   2412 C CD  . PRO B 2 401 ? 140.984 158.794 178.669 1.00 104.66 ? 412 PRO B CD  1 
ATOM   2413 N N   . GLY B 2 402 ? 136.888 156.745 177.636 1.00 104.66 ? 413 GLY B N   1 
ATOM   2414 C CA  . GLY B 2 402 ? 136.294 155.447 177.408 1.00 104.66 ? 413 GLY B CA  1 
ATOM   2415 C C   . GLY B 2 402 ? 135.988 154.636 178.645 1.00 104.66 ? 413 GLY B C   1 
ATOM   2416 O O   . GLY B 2 402 ? 135.673 153.449 178.519 1.00 104.66 ? 413 GLY B O   1 
ATOM   2417 N N   . GLN B 2 403 ? 136.069 155.227 179.831 1.00 104.66 ? 414 GLN B N   1 
ATOM   2418 C CA  . GLN B 2 403 ? 135.753 154.528 181.067 1.00 104.66 ? 414 GLN B CA  1 
ATOM   2419 C C   . GLN B 2 403 ? 134.339 154.862 181.520 1.00 104.66 ? 414 GLN B C   1 
ATOM   2420 O O   . GLN B 2 403 ? 133.814 155.940 181.236 1.00 104.66 ? 414 GLN B O   1 
ATOM   2421 C CB  . GLN B 2 403 ? 136.750 154.884 182.168 1.00 104.66 ? 414 GLN B CB  1 
ATOM   2422 C CG  . GLN B 2 403 ? 138.164 154.505 181.826 1.00 104.66 ? 414 GLN B CG  1 
ATOM   2423 C CD  . GLN B 2 403 ? 138.308 153.025 181.589 1.00 104.66 ? 414 GLN B CD  1 
ATOM   2424 O OE1 . GLN B 2 403 ? 137.612 152.217 182.202 1.00 104.66 ? 414 GLN B OE1 1 
ATOM   2425 N NE2 . GLN B 2 403 ? 139.204 152.656 180.684 1.00 104.66 ? 414 GLN B NE2 1 
ATOM   2426 N N   . THR B 2 404 ? 133.720 153.915 182.223 1.00 104.66 ? 415 THR B N   1 
ATOM   2427 C CA  . THR B 2 404 ? 132.339 154.035 182.663 1.00 104.66 ? 415 THR B CA  1 
ATOM   2428 C C   . THR B 2 404 ? 132.243 153.765 184.156 1.00 104.66 ? 415 THR B C   1 
ATOM   2429 O O   . THR B 2 404 ? 133.047 153.023 184.723 1.00 104.66 ? 415 THR B O   1 
ATOM   2430 C CB  . THR B 2 404 ? 131.419 153.064 181.918 1.00 104.66 ? 415 THR B CB  1 
ATOM   2431 O OG1 . THR B 2 404 ? 131.599 151.743 182.443 1.00 104.66 ? 415 THR B OG1 1 
ATOM   2432 C CG2 . THR B 2 404 ? 131.729 153.060 180.429 1.00 104.66 ? 415 THR B CG2 1 
ATOM   2433 N N   . GLY B 2 405 ? 131.243 154.367 184.783 1.00 104.66 ? 416 GLY B N   1 
ATOM   2434 C CA  . GLY B 2 405 ? 131.050 154.219 186.209 1.00 104.66 ? 416 GLY B CA  1 
ATOM   2435 C C   . GLY B 2 405 ? 130.204 155.358 186.743 1.00 104.66 ? 416 GLY B C   1 
ATOM   2436 O O   . GLY B 2 405 ? 129.608 156.120 185.986 1.00 104.66 ? 416 GLY B O   1 
ATOM   2437 N N   . LYS B 2 406 ? 130.166 155.450 188.073 1.00 104.66 ? 417 LYS B N   1 
ATOM   2438 C CA  . LYS B 2 406 ? 129.403 156.518 188.708 1.00 104.66 ? 417 LYS B CA  1 
ATOM   2439 C C   . LYS B 2 406 ? 129.969 157.886 188.358 1.00 104.66 ? 417 LYS B C   1 
ATOM   2440 O O   . LYS B 2 406 ? 129.215 158.816 188.050 1.00 104.66 ? 417 LYS B O   1 
ATOM   2441 C CB  . LYS B 2 406 ? 129.382 156.326 190.221 1.00 104.66 ? 417 LYS B CB  1 
ATOM   2442 C CG  . LYS B 2 406 ? 128.278 155.412 190.710 1.00 104.66 ? 417 LYS B CG  1 
ATOM   2443 C CD  . LYS B 2 406 ? 128.255 155.317 192.229 1.00 104.66 ? 417 LYS B CD  1 
ATOM   2444 C CE  . LYS B 2 406 ? 129.655 155.255 192.823 1.00 104.66 ? 417 LYS B CE  1 
ATOM   2445 N NZ  . LYS B 2 406 ? 130.440 154.098 192.310 1.00 104.66 ? 417 LYS B NZ  1 
ATOM   2446 N N   . ILE B 2 407 ? 131.293 158.033 188.407 1.00 104.66 ? 418 ILE B N   1 
ATOM   2447 C CA  . ILE B 2 407 ? 131.904 159.323 188.108 1.00 104.66 ? 418 ILE B CA  1 
ATOM   2448 C C   . ILE B 2 407 ? 131.802 159.641 186.624 1.00 104.66 ? 418 ILE B C   1 
ATOM   2449 O O   . ILE B 2 407 ? 131.446 160.759 186.239 1.00 104.66 ? 418 ILE B O   1 
ATOM   2450 C CB  . ILE B 2 407 ? 133.363 159.343 188.585 1.00 104.66 ? 418 ILE B CB  1 
ATOM   2451 C CG1 . ILE B 2 407 ? 133.419 159.056 190.074 1.00 104.66 ? 418 ILE B CG1 1 
ATOM   2452 C CG2 . ILE B 2 407 ? 133.989 160.681 188.300 1.00 104.66 ? 418 ILE B CG2 1 
ATOM   2453 C CD1 . ILE B 2 407 ? 132.593 160.002 190.891 1.00 104.66 ? 418 ILE B CD1 1 
ATOM   2454 N N   . ALA B 2 408 ? 132.104 158.670 185.769 1.00 104.66 ? 419 ALA B N   1 
ATOM   2455 C CA  . ALA B 2 408 ? 132.147 158.920 184.338 1.00 104.66 ? 419 ALA B CA  1 
ATOM   2456 C C   . ALA B 2 408 ? 130.770 159.050 183.711 1.00 104.66 ? 419 ALA B C   1 
ATOM   2457 O O   . ALA B 2 408 ? 130.679 159.388 182.528 1.00 104.66 ? 419 ALA B O   1 
ATOM   2458 C CB  . ALA B 2 408 ? 132.921 157.811 183.632 1.00 104.66 ? 419 ALA B CB  1 
ATOM   2459 N N   . ASP B 2 409 ? 129.705 158.781 184.455 1.00 104.66 ? 420 ASP B N   1 
ATOM   2460 C CA  . ASP B 2 409 ? 128.352 158.933 183.939 1.00 104.66 ? 420 ASP B CA  1 
ATOM   2461 C C   . ASP B 2 409 ? 127.618 160.130 184.510 1.00 104.66 ? 420 ASP B C   1 
ATOM   2462 O O   . ASP B 2 409 ? 126.995 160.879 183.758 1.00 104.66 ? 420 ASP B O   1 
ATOM   2463 C CB  . ASP B 2 409 ? 127.530 157.671 184.215 1.00 104.66 ? 420 ASP B CB  1 
ATOM   2464 C CG  . ASP B 2 409 ? 127.996 156.481 183.400 1.00 104.66 ? 420 ASP B CG  1 
ATOM   2465 O OD1 . ASP B 2 409 ? 128.519 156.691 182.287 1.00 104.66 ? 420 ASP B OD1 1 
ATOM   2466 O OD2 . ASP B 2 409 ? 127.837 155.336 183.869 1.00 104.66 ? 420 ASP B OD2 1 
ATOM   2467 N N   . TYR B 2 410 ? 127.683 160.341 185.820 1.00 104.66 ? 421 TYR B N   1 
ATOM   2468 C CA  . TYR B 2 410 ? 126.861 161.344 186.471 1.00 104.66 ? 421 TYR B CA  1 
ATOM   2469 C C   . TYR B 2 410 ? 127.634 162.555 186.967 1.00 104.66 ? 421 TYR B C   1 
ATOM   2470 O O   . TYR B 2 410 ? 127.006 163.557 187.321 1.00 104.66 ? 421 TYR B O   1 
ATOM   2471 C CB  . TYR B 2 410 ? 126.111 160.721 187.654 1.00 104.66 ? 421 TYR B CB  1 
ATOM   2472 C CG  . TYR B 2 410 ? 125.307 159.495 187.301 1.00 104.66 ? 421 TYR B CG  1 
ATOM   2473 C CD1 . TYR B 2 410 ? 124.726 159.358 186.053 1.00 104.66 ? 421 TYR B CD1 1 
ATOM   2474 C CD2 . TYR B 2 410 ? 125.130 158.474 188.219 1.00 104.66 ? 421 TYR B CD2 1 
ATOM   2475 C CE1 . TYR B 2 410 ? 123.992 158.243 185.730 1.00 104.66 ? 421 TYR B CE1 1 
ATOM   2476 C CE2 . TYR B 2 410 ? 124.398 157.355 187.905 1.00 104.66 ? 421 TYR B CE2 1 
ATOM   2477 C CZ  . TYR B 2 410 ? 123.831 157.244 186.659 1.00 104.66 ? 421 TYR B CZ  1 
ATOM   2478 O OH  . TYR B 2 410 ? 123.098 156.128 186.339 1.00 104.66 ? 421 TYR B OH  1 
ATOM   2479 N N   . ASN B 2 411 ? 128.961 162.501 187.013 1.00 104.66 ? 422 ASN B N   1 
ATOM   2480 C CA  . ASN B 2 411 ? 129.727 163.574 187.630 1.00 104.66 ? 422 ASN B CA  1 
ATOM   2481 C C   . ASN B 2 411 ? 130.649 164.299 186.664 1.00 104.66 ? 422 ASN B C   1 
ATOM   2482 O O   . ASN B 2 411 ? 130.561 165.524 186.543 1.00 104.66 ? 422 ASN B O   1 
ATOM   2483 C CB  . ASN B 2 411 ? 130.534 163.015 188.806 1.00 104.66 ? 422 ASN B CB  1 
ATOM   2484 C CG  . ASN B 2 411 ? 129.653 162.473 189.904 1.00 104.66 ? 422 ASN B CG  1 
ATOM   2485 O OD1 . ASN B 2 411 ? 129.437 163.126 190.920 1.00 104.66 ? 422 ASN B OD1 1 
ATOM   2486 N ND2 . ASN B 2 411 ? 129.133 161.274 189.704 1.00 104.66 ? 422 ASN B ND2 1 
ATOM   2487 N N   . TYR B 2 412 ? 131.527 163.586 185.963 1.00 104.66 ? 423 TYR B N   1 
ATOM   2488 C CA  . TYR B 2 412 ? 132.551 164.239 185.149 1.00 104.66 ? 423 TYR B CA  1 
ATOM   2489 C C   . TYR B 2 412 ? 132.980 163.286 184.047 1.00 104.66 ? 423 TYR B C   1 
ATOM   2490 O O   . TYR B 2 412 ? 133.645 162.286 184.325 1.00 104.66 ? 423 TYR B O   1 
ATOM   2491 C CB  . TYR B 2 412 ? 133.743 164.643 186.006 1.00 104.66 ? 423 TYR B CB  1 
ATOM   2492 C CG  . TYR B 2 412 ? 134.814 165.383 185.250 1.00 104.66 ? 423 TYR B CG  1 
ATOM   2493 C CD1 . TYR B 2 412 ? 134.490 166.415 184.390 1.00 104.66 ? 423 TYR B CD1 1 
ATOM   2494 C CD2 . TYR B 2 412 ? 136.149 165.057 185.400 1.00 104.66 ? 423 TYR B CD2 1 
ATOM   2495 C CE1 . TYR B 2 412 ? 135.462 167.095 183.699 1.00 104.66 ? 423 TYR B CE1 1 
ATOM   2496 C CE2 . TYR B 2 412 ? 137.126 165.735 184.713 1.00 104.66 ? 423 TYR B CE2 1 
ATOM   2497 C CZ  . TYR B 2 412 ? 136.774 166.751 183.864 1.00 104.66 ? 423 TYR B CZ  1 
ATOM   2498 O OH  . TYR B 2 412 ? 137.738 167.433 183.172 1.00 104.66 ? 423 TYR B OH  1 
ATOM   2499 N N   . LYS B 2 413 ? 132.628 163.599 182.804 1.00 104.66 ? 424 LYS B N   1 
ATOM   2500 C CA  . LYS B 2 413 ? 132.904 162.721 181.678 1.00 104.66 ? 424 LYS B CA  1 
ATOM   2501 C C   . LYS B 2 413 ? 133.844 163.402 180.699 1.00 104.66 ? 424 LYS B C   1 
ATOM   2502 O O   . LYS B 2 413 ? 133.633 164.561 180.335 1.00 104.66 ? 424 LYS B O   1 
ATOM   2503 C CB  . LYS B 2 413 ? 131.617 162.318 180.966 1.00 104.66 ? 424 LYS B CB  1 
ATOM   2504 C CG  . LYS B 2 413 ? 131.833 161.294 179.875 1.00 104.66 ? 424 LYS B CG  1 
ATOM   2505 C CD  . LYS B 2 413 ? 130.525 160.730 179.376 1.00 104.66 ? 424 LYS B CD  1 
ATOM   2506 C CE  . LYS B 2 413 ? 130.761 159.797 178.212 1.00 104.66 ? 424 LYS B CE  1 
ATOM   2507 N NZ  . LYS B 2 413 ? 131.552 158.611 178.627 1.00 104.66 ? 424 LYS B NZ  1 
ATOM   2508 N N   . LEU B 2 414 ? 134.872 162.673 180.269 1.00 104.66 ? 425 LEU B N   1 
ATOM   2509 C CA  . LEU B 2 414 ? 135.886 163.074 179.304 1.00 104.66 ? 425 LEU B CA  1 
ATOM   2510 C C   . LEU B 2 414 ? 135.534 162.563 177.916 1.00 104.66 ? 425 LEU B C   1 
ATOM   2511 O O   . LEU B 2 414 ? 135.023 161.449 177.777 1.00 104.66 ? 425 LEU B O   1 
ATOM   2512 C CB  . LEU B 2 414 ? 137.259 162.529 179.698 1.00 104.66 ? 425 LEU B CB  1 
ATOM   2513 C CG  . LEU B 2 414 ? 137.943 163.120 180.924 1.00 104.66 ? 425 LEU B CG  1 
ATOM   2514 C CD1 . LEU B 2 414 ? 139.332 162.552 181.049 1.00 104.66 ? 425 LEU B CD1 1 
ATOM   2515 C CD2 . LEU B 2 414 ? 137.992 164.622 180.824 1.00 104.66 ? 425 LEU B CD2 1 
ATOM   2516 N N   . PRO B 2 415 ? 135.802 163.335 176.871 1.00 104.66 ? 426 PRO B N   1 
ATOM   2517 C CA  . PRO B 2 415 ? 135.463 162.890 175.518 1.00 104.66 ? 426 PRO B CA  1 
ATOM   2518 C C   . PRO B 2 415 ? 136.363 161.751 175.077 1.00 104.66 ? 426 PRO B C   1 
ATOM   2519 O O   . PRO B 2 415 ? 137.331 161.386 175.741 1.00 104.66 ? 426 PRO B O   1 
ATOM   2520 C CB  . PRO B 2 415 ? 135.683 164.138 174.667 1.00 104.66 ? 426 PRO B CB  1 
ATOM   2521 C CG  . PRO B 2 415 ? 136.681 164.921 175.419 1.00 104.66 ? 426 PRO B CG  1 
ATOM   2522 C CD  . PRO B 2 415 ? 136.437 164.660 176.872 1.00 104.66 ? 426 PRO B CD  1 
ATOM   2523 N N   . ASP B 2 416 ? 136.012 161.174 173.929 1.00 104.66 ? 427 ASP B N   1 
ATOM   2524 C CA  . ASP B 2 416 ? 136.783 160.071 173.374 1.00 104.66 ? 427 ASP B CA  1 
ATOM   2525 C C   . ASP B 2 416 ? 138.069 160.527 172.701 1.00 104.66 ? 427 ASP B C   1 
ATOM   2526 O O   . ASP B 2 416 ? 138.998 159.726 172.561 1.00 104.66 ? 427 ASP B O   1 
ATOM   2527 C CB  . ASP B 2 416 ? 135.931 159.293 172.372 1.00 104.66 ? 427 ASP B CB  1 
ATOM   2528 C CG  . ASP B 2 416 ? 134.773 158.577 173.030 1.00 104.66 ? 427 ASP B CG  1 
ATOM   2529 O OD1 . ASP B 2 416 ? 134.916 158.166 174.200 1.00 104.66 ? 427 ASP B OD1 1 
ATOM   2530 O OD2 . ASP B 2 416 ? 133.716 158.431 172.382 1.00 104.66 ? 427 ASP B OD2 1 
ATOM   2531 N N   . ASP B 2 417 ? 138.144 161.787 172.283 1.00 104.66 ? 428 ASP B N   1 
ATOM   2532 C CA  . ASP B 2 417 ? 139.316 162.333 171.603 1.00 104.66 ? 428 ASP B CA  1 
ATOM   2533 C C   . ASP B 2 417 ? 140.127 163.239 172.515 1.00 104.66 ? 428 ASP B C   1 
ATOM   2534 O O   . ASP B 2 417 ? 140.618 164.284 172.086 1.00 104.66 ? 428 ASP B O   1 
ATOM   2535 C CB  . ASP B 2 417 ? 138.894 163.080 170.345 1.00 104.66 ? 428 ASP B CB  1 
ATOM   2536 C CG  . ASP B 2 417 ? 138.461 162.147 169.241 1.00 104.66 ? 428 ASP B CG  1 
ATOM   2537 O OD1 . ASP B 2 417 ? 137.972 161.044 169.561 1.00 104.66 ? 428 ASP B OD1 1 
ATOM   2538 O OD2 . ASP B 2 417 ? 138.611 162.511 168.057 1.00 104.66 ? 428 ASP B OD2 1 
ATOM   2539 N N   . PHE B 2 418 ? 140.266 162.869 173.782 1.00 104.66 ? 429 PHE B N   1 
ATOM   2540 C CA  . PHE B 2 418 ? 140.968 163.712 174.736 1.00 104.66 ? 429 PHE B CA  1 
ATOM   2541 C C   . PHE B 2 418 ? 142.434 163.848 174.356 1.00 104.66 ? 429 PHE B C   1 
ATOM   2542 O O   . PHE B 2 418 ? 143.056 162.901 173.872 1.00 104.66 ? 429 PHE B O   1 
ATOM   2543 C CB  . PHE B 2 418 ? 140.845 163.131 176.137 1.00 104.66 ? 429 PHE B CB  1 
ATOM   2544 C CG  . PHE B 2 418 ? 141.405 164.009 177.204 1.00 104.66 ? 429 PHE B CG  1 
ATOM   2545 C CD1 . PHE B 2 418 ? 140.883 165.263 177.423 1.00 104.66 ? 429 PHE B CD1 1 
ATOM   2546 C CD2 . PHE B 2 418 ? 142.444 163.575 177.997 1.00 104.66 ? 429 PHE B CD2 1 
ATOM   2547 C CE1 . PHE B 2 418 ? 141.393 166.069 178.407 1.00 104.66 ? 429 PHE B CE1 1 
ATOM   2548 C CE2 . PHE B 2 418 ? 142.958 164.378 178.980 1.00 104.66 ? 429 PHE B CE2 1 
ATOM   2549 C CZ  . PHE B 2 418 ? 142.432 165.626 179.185 1.00 104.66 ? 429 PHE B CZ  1 
ATOM   2550 N N   . THR B 2 419 ? 142.985 165.042 174.572 1.00 104.66 ? 430 THR B N   1 
ATOM   2551 C CA  . THR B 2 419 ? 144.391 165.343 174.299 1.00 104.66 ? 430 THR B CA  1 
ATOM   2552 C C   . THR B 2 419 ? 144.912 166.172 175.465 1.00 104.66 ? 430 THR B C   1 
ATOM   2553 O O   . THR B 2 419 ? 144.818 167.400 175.447 1.00 104.66 ? 430 THR B O   1 
ATOM   2554 C CB  . THR B 2 419 ? 144.549 166.078 172.983 1.00 104.66 ? 430 THR B CB  1 
ATOM   2555 O OG1 . THR B 2 419 ? 143.956 165.308 171.933 1.00 104.66 ? 430 THR B OG1 1 
ATOM   2556 C CG2 . THR B 2 419 ? 146.013 166.289 172.675 1.00 104.66 ? 430 THR B CG2 1 
ATOM   2557 N N   . GLY B 2 420 ? 145.463 165.508 176.470 1.00 104.66 ? 431 GLY B N   1 
ATOM   2558 C CA  . GLY B 2 420 ? 145.890 166.209 177.661 1.00 104.66 ? 431 GLY B CA  1 
ATOM   2559 C C   . GLY B 2 420 ? 146.590 165.275 178.614 1.00 104.66 ? 431 GLY B C   1 
ATOM   2560 O O   . GLY B 2 420 ? 147.083 164.220 178.215 1.00 104.66 ? 431 GLY B O   1 
ATOM   2561 N N   . CYS B 2 421 ? 146.637 165.674 179.882 1.00 104.66 ? 432 CYS B N   1 
ATOM   2562 C CA  . CYS B 2 421 ? 147.304 164.895 180.912 1.00 104.66 ? 432 CYS B CA  1 
ATOM   2563 C C   . CYS B 2 421 ? 146.492 164.945 182.195 1.00 104.66 ? 432 CYS B C   1 
ATOM   2564 O O   . CYS B 2 421 ? 145.771 165.910 182.451 1.00 104.66 ? 432 CYS B O   1 
ATOM   2565 C CB  . CYS B 2 421 ? 148.720 165.410 181.165 1.00 104.66 ? 432 CYS B CB  1 
ATOM   2566 S SG  . CYS B 2 421 ? 149.818 165.250 179.745 1.00 104.66 ? 432 CYS B SG  1 
ATOM   2567 N N   . VAL B 2 422 ? 146.618 163.897 183.003 1.00 104.66 ? 433 VAL B N   1 
ATOM   2568 C CA  . VAL B 2 422 ? 145.887 163.763 184.257 1.00 104.66 ? 433 VAL B CA  1 
ATOM   2569 C C   . VAL B 2 422 ? 146.892 163.626 185.388 1.00 104.66 ? 433 VAL B C   1 
ATOM   2570 O O   . VAL B 2 422 ? 147.781 162.772 185.330 1.00 104.66 ? 433 VAL B O   1 
ATOM   2571 C CB  . VAL B 2 422 ? 144.939 162.554 184.232 1.00 104.66 ? 433 VAL B CB  1 
ATOM   2572 C CG1 . VAL B 2 422 ? 144.185 162.458 185.534 1.00 104.66 ? 433 VAL B CG1 1 
ATOM   2573 C CG2 . VAL B 2 422 ? 143.989 162.657 183.066 1.00 104.66 ? 433 VAL B CG2 1 
ATOM   2574 N N   . ILE B 2 423 ? 146.745 164.453 186.417 1.00 104.66 ? 434 ILE B N   1 
ATOM   2575 C CA  . ILE B 2 423 ? 147.670 164.488 187.542 1.00 104.66 ? 434 ILE B CA  1 
ATOM   2576 C C   . ILE B 2 423 ? 146.875 164.294 188.821 1.00 104.66 ? 434 ILE B C   1 
ATOM   2577 O O   . ILE B 2 423 ? 145.872 164.980 189.037 1.00 104.66 ? 434 ILE B O   1 
ATOM   2578 C CB  . ILE B 2 423 ? 148.440 165.817 187.600 1.00 104.66 ? 434 ILE B CB  1 
ATOM   2579 C CG1 . ILE B 2 423 ? 149.001 166.171 186.231 1.00 104.66 ? 434 ILE B CG1 1 
ATOM   2580 C CG2 . ILE B 2 423 ? 149.552 165.733 188.611 1.00 104.66 ? 434 ILE B CG2 1 
ATOM   2581 C CD1 . ILE B 2 423 ? 149.424 167.604 186.123 1.00 104.66 ? 434 ILE B CD1 1 
ATOM   2582 N N   . ALA B 2 424 ? 147.322 163.376 189.673 1.00 104.66 ? 435 ALA B N   1 
ATOM   2583 C CA  . ALA B 2 424 ? 146.647 163.124 190.936 1.00 104.66 ? 435 ALA B CA  1 
ATOM   2584 C C   . ALA B 2 424 ? 147.671 162.822 192.015 1.00 104.66 ? 435 ALA B C   1 
ATOM   2585 O O   . ALA B 2 424 ? 148.738 162.272 191.741 1.00 104.66 ? 435 ALA B O   1 
ATOM   2586 C CB  . ALA B 2 424 ? 145.659 161.964 190.824 1.00 104.66 ? 435 ALA B CB  1 
ATOM   2587 N N   . TRP B 2 425 ? 147.336 163.181 193.250 1.00 104.66 ? 436 TRP B N   1 
ATOM   2588 C CA  . TRP B 2 425 ? 148.221 162.906 194.368 1.00 104.66 ? 436 TRP B CA  1 
ATOM   2589 C C   . TRP B 2 425 ? 147.412 162.823 195.652 1.00 104.66 ? 436 TRP B C   1 
ATOM   2590 O O   . TRP B 2 425 ? 146.408 163.518 195.818 1.00 104.66 ? 436 TRP B O   1 
ATOM   2591 C CB  . TRP B 2 425 ? 149.318 163.966 194.490 1.00 104.66 ? 436 TRP B CB  1 
ATOM   2592 C CG  . TRP B 2 425 ? 148.853 165.298 194.963 1.00 104.66 ? 436 TRP B CG  1 
ATOM   2593 C CD1 . TRP B 2 425 ? 148.842 165.750 196.245 1.00 104.66 ? 436 TRP B CD1 1 
ATOM   2594 C CD2 . TRP B 2 425 ? 148.358 166.369 194.156 1.00 104.66 ? 436 TRP B CD2 1 
ATOM   2595 N NE1 . TRP B 2 425 ? 148.360 167.033 196.291 1.00 104.66 ? 436 TRP B NE1 1 
ATOM   2596 C CE2 . TRP B 2 425 ? 148.055 167.435 195.019 1.00 104.66 ? 436 TRP B CE2 1 
ATOM   2597 C CE3 . TRP B 2 425 ? 148.135 166.527 192.789 1.00 104.66 ? 436 TRP B CE3 1 
ATOM   2598 C CZ2 . TRP B 2 425 ? 147.541 168.639 194.560 1.00 104.66 ? 436 TRP B CZ2 1 
ATOM   2599 C CZ3 . TRP B 2 425 ? 147.626 167.722 192.336 1.00 104.66 ? 436 TRP B CZ3 1 
ATOM   2600 C CH2 . TRP B 2 425 ? 147.334 168.762 193.217 1.00 104.66 ? 436 TRP B CH2 1 
ATOM   2601 N N   . ASN B 2 426 ? 147.865 161.964 196.559 1.00 104.66 ? 437 ASN B N   1 
ATOM   2602 C CA  . ASN B 2 426 ? 147.167 161.751 197.817 1.00 104.66 ? 437 ASN B CA  1 
ATOM   2603 C C   . ASN B 2 426 ? 147.203 163.009 198.671 1.00 104.66 ? 437 ASN B C   1 
ATOM   2604 O O   . ASN B 2 426 ? 148.200 163.733 198.695 1.00 104.66 ? 437 ASN B O   1 
ATOM   2605 C CB  . ASN B 2 426 ? 147.799 160.591 198.578 1.00 104.66 ? 437 ASN B CB  1 
ATOM   2606 C CG  . ASN B 2 426 ? 147.007 160.195 199.799 1.00 104.66 ? 437 ASN B CG  1 
ATOM   2607 O OD1 . ASN B 2 426 ? 146.807 160.994 200.712 1.00 104.66 ? 437 ASN B OD1 1 
ATOM   2608 N ND2 . ASN B 2 426 ? 146.562 158.946 199.831 1.00 104.66 ? 437 ASN B ND2 1 
ATOM   2609 N N   . SER B 2 427 ? 146.107 163.264 199.380 1.00 104.66 ? 438 SER B N   1 
ATOM   2610 C CA  . SER B 2 427 ? 145.985 164.449 200.217 1.00 104.66 ? 438 SER B CA  1 
ATOM   2611 C C   . SER B 2 427 ? 145.319 164.107 201.539 1.00 104.66 ? 438 SER B C   1 
ATOM   2612 O O   . SER B 2 427 ? 144.463 164.847 202.032 1.00 104.66 ? 438 SER B O   1 
ATOM   2613 C CB  . SER B 2 427 ? 145.210 165.549 199.499 1.00 104.66 ? 438 SER B CB  1 
ATOM   2614 O OG  . SER B 2 427 ? 144.981 166.647 200.360 1.00 104.66 ? 438 SER B OG  1 
ATOM   2615 N N   . ASN B 2 428 ? 145.713 162.986 202.142 1.00 104.66 ? 439 ASN B N   1 
ATOM   2616 C CA  . ASN B 2 428 ? 145.034 162.504 203.339 1.00 104.66 ? 439 ASN B CA  1 
ATOM   2617 C C   . ASN B 2 428 ? 145.230 163.413 204.545 1.00 104.66 ? 439 ASN B C   1 
ATOM   2618 O O   . ASN B 2 428 ? 144.458 163.315 205.503 1.00 104.66 ? 439 ASN B O   1 
ATOM   2619 C CB  . ASN B 2 428 ? 145.513 161.094 203.680 1.00 104.66 ? 439 ASN B CB  1 
ATOM   2620 C CG  . ASN B 2 428 ? 144.483 160.301 204.454 1.00 104.66 ? 439 ASN B CG  1 
ATOM   2621 O OD1 . ASN B 2 428 ? 143.282 160.445 204.238 1.00 104.66 ? 439 ASN B OD1 1 
ATOM   2622 N ND2 . ASN B 2 428 ? 144.949 159.452 205.359 1.00 104.66 ? 439 ASN B ND2 1 
ATOM   2623 N N   . ASN B 2 429 ? 146.234 164.282 204.531 1.00 104.66 ? 440 ASN B N   1 
ATOM   2624 C CA  . ASN B 2 429 ? 146.540 165.105 205.692 1.00 104.66 ? 440 ASN B CA  1 
ATOM   2625 C C   . ASN B 2 429 ? 145.968 166.512 205.604 1.00 104.66 ? 440 ASN B C   1 
ATOM   2626 O O   . ASN B 2 429 ? 146.276 167.341 206.465 1.00 104.66 ? 440 ASN B O   1 
ATOM   2627 C CB  . ASN B 2 429 ? 148.053 165.185 205.897 1.00 104.66 ? 440 ASN B CB  1 
ATOM   2628 C CG  . ASN B 2 429 ? 148.786 165.599 204.644 1.00 104.66 ? 440 ASN B CG  1 
ATOM   2629 O OD1 . ASN B 2 429 ? 148.550 165.054 203.567 1.00 104.66 ? 440 ASN B OD1 1 
ATOM   2630 N ND2 . ASN B 2 429 ? 149.677 166.573 204.774 1.00 104.66 ? 440 ASN B ND2 1 
ATOM   2631 N N   . LEU B 2 430 ? 145.155 166.806 204.596 1.00 104.66 ? 441 LEU B N   1 
ATOM   2632 C CA  . LEU B 2 430 ? 144.549 168.123 204.454 1.00 104.66 ? 441 LEU B CA  1 
ATOM   2633 C C   . LEU B 2 430 ? 143.037 168.097 204.328 1.00 104.66 ? 441 LEU B C   1 
ATOM   2634 O O   . LEU B 2 430 ? 142.379 169.015 204.820 1.00 104.66 ? 441 LEU B O   1 
ATOM   2635 C CB  . LEU B 2 430 ? 145.118 168.851 203.229 1.00 104.66 ? 441 LEU B CB  1 
ATOM   2636 C CG  . LEU B 2 430 ? 146.620 169.110 203.216 1.00 104.66 ? 441 LEU B CG  1 
ATOM   2637 C CD1 . LEU B 2 430 ? 146.990 169.938 202.003 1.00 104.66 ? 441 LEU B CD1 1 
ATOM   2638 C CD2 . LEU B 2 430 ? 147.043 169.806 204.494 1.00 104.66 ? 441 LEU B CD2 1 
ATOM   2639 N N   . ASP B 2 431 ? 142.470 167.082 203.684 1.00 104.66 ? 442 ASP B N   1 
ATOM   2640 C CA  . ASP B 2 431 ? 141.047 167.042 203.386 1.00 104.66 ? 442 ASP B CA  1 
ATOM   2641 C C   . ASP B 2 431 ? 140.260 166.162 204.346 1.00 104.66 ? 442 ASP B C   1 
ATOM   2642 O O   . ASP B 2 431 ? 139.075 165.917 204.111 1.00 104.66 ? 442 ASP B O   1 
ATOM   2643 C CB  . ASP B 2 431 ? 140.833 166.570 201.949 1.00 104.66 ? 442 ASP B CB  1 
ATOM   2644 C CG  . ASP B 2 431 ? 141.030 167.682 200.940 1.00 104.66 ? 442 ASP B CG  1 
ATOM   2645 O OD1 . ASP B 2 431 ? 140.530 168.799 201.181 1.00 104.66 ? 442 ASP B OD1 1 
ATOM   2646 O OD2 . ASP B 2 431 ? 141.689 167.441 199.908 1.00 104.66 ? 442 ASP B OD2 1 
ATOM   2647 N N   . SER B 2 432 ? 140.878 165.691 205.422 1.00 108.88 ? 443 SER B N   1 
ATOM   2648 C CA  . SER B 2 432 ? 140.205 164.842 206.390 1.00 108.88 ? 443 SER B CA  1 
ATOM   2649 C C   . SER B 2 432 ? 140.133 165.549 207.734 1.00 108.88 ? 443 SER B C   1 
ATOM   2650 O O   . SER B 2 432 ? 141.003 166.352 208.080 1.00 108.88 ? 443 SER B O   1 
ATOM   2651 C CB  . SER B 2 432 ? 140.919 163.499 206.551 1.00 108.88 ? 443 SER B CB  1 
ATOM   2652 O OG  . SER B 2 432 ? 142.172 163.668 207.187 1.00 108.88 ? 443 SER B OG  1 
ATOM   2653 N N   . LYS B 2 433 ? 139.084 165.242 208.488 1.00 116.83 ? 444 LYS B N   1 
ATOM   2654 C CA  . LYS B 2 433 ? 138.857 165.840 209.792 1.00 116.83 ? 444 LYS B CA  1 
ATOM   2655 C C   . LYS B 2 433 ? 138.623 164.745 210.819 1.00 116.83 ? 444 LYS B C   1 
ATOM   2656 O O   . LYS B 2 433 ? 138.264 163.614 210.483 1.00 116.83 ? 444 LYS B O   1 
ATOM   2657 C CB  . LYS B 2 433 ? 137.664 166.799 209.771 1.00 116.83 ? 444 LYS B CB  1 
ATOM   2658 C CG  . LYS B 2 433 ? 137.900 168.056 208.963 1.00 116.83 ? 444 LYS B CG  1 
ATOM   2659 C CD  . LYS B 2 433 ? 136.654 168.918 208.929 1.00 116.83 ? 444 LYS B CD  1 
ATOM   2660 C CE  . LYS B 2 433 ? 136.388 169.541 210.287 1.00 116.83 ? 444 LYS B CE  1 
ATOM   2661 N NZ  . LYS B 2 433 ? 137.427 170.544 210.650 1.00 116.83 ? 444 LYS B NZ  1 
ATOM   2662 N N   . VAL B 2 434 ? 138.841 165.097 212.087 1.00 124.42 ? 445 VAL B N   1 
ATOM   2663 C CA  . VAL B 2 434 ? 138.657 164.135 213.169 1.00 124.42 ? 445 VAL B CA  1 
ATOM   2664 C C   . VAL B 2 434 ? 137.198 163.707 213.262 1.00 124.42 ? 445 VAL B C   1 
ATOM   2665 O O   . VAL B 2 434 ? 136.891 162.517 213.403 1.00 124.42 ? 445 VAL B O   1 
ATOM   2666 C CB  . VAL B 2 434 ? 139.163 164.726 214.496 1.00 124.42 ? 445 VAL B CB  1 
ATOM   2667 C CG1 . VAL B 2 434 ? 138.602 163.951 215.676 1.00 124.42 ? 445 VAL B CG1 1 
ATOM   2668 C CG2 . VAL B 2 434 ? 140.682 164.723 214.525 1.00 124.42 ? 445 VAL B CG2 1 
ATOM   2669 N N   . GLY B 2 435 ? 136.278 164.662 213.175 1.00 121.39 ? 446 GLY B N   1 
ATOM   2670 C CA  . GLY B 2 435 ? 134.866 164.363 213.267 1.00 121.39 ? 446 GLY B CA  1 
ATOM   2671 C C   . GLY B 2 435 ? 134.218 163.864 211.999 1.00 121.39 ? 446 GLY B C   1 
ATOM   2672 O O   . GLY B 2 435 ? 133.010 163.619 211.988 1.00 121.39 ? 446 GLY B O   1 
ATOM   2673 N N   . GLY B 2 436 ? 134.984 163.707 210.924 1.00 114.52 ? 447 GLY B N   1 
ATOM   2674 C CA  . GLY B 2 436 ? 134.424 163.281 209.659 1.00 114.52 ? 447 GLY B CA  1 
ATOM   2675 C C   . GLY B 2 436 ? 134.057 164.456 208.780 1.00 114.52 ? 447 GLY B C   1 
ATOM   2676 O O   . GLY B 2 436 ? 133.216 165.278 209.153 1.00 114.52 ? 447 GLY B O   1 
ATOM   2677 N N   . ASN B 2 437 ? 134.678 164.549 207.610 1.00 106.69 ? 448 ASN B N   1 
ATOM   2678 C CA  . ASN B 2 437 ? 134.473 165.679 206.714 1.00 106.69 ? 448 ASN B CA  1 
ATOM   2679 C C   . ASN B 2 437 ? 133.267 165.392 205.829 1.00 106.69 ? 448 ASN B C   1 
ATOM   2680 O O   . ASN B 2 437 ? 133.291 164.461 205.018 1.00 106.69 ? 448 ASN B O   1 
ATOM   2681 C CB  . ASN B 2 437 ? 135.722 165.934 205.878 1.00 106.69 ? 448 ASN B CB  1 
ATOM   2682 C CG  . ASN B 2 437 ? 135.786 167.347 205.351 1.00 106.69 ? 448 ASN B CG  1 
ATOM   2683 O OD1 . ASN B 2 437 ? 134.869 168.140 205.561 1.00 106.69 ? 448 ASN B OD1 1 
ATOM   2684 N ND2 . ASN B 2 437 ? 136.874 167.675 204.667 1.00 106.69 ? 448 ASN B ND2 1 
ATOM   2685 N N   . TYR B 2 438 ? 132.212 166.190 205.988 1.00 104.91 ? 449 TYR B N   1 
ATOM   2686 C CA  . TYR B 2 438 ? 130.991 166.054 205.204 1.00 104.91 ? 449 TYR B CA  1 
ATOM   2687 C C   . TYR B 2 438 ? 130.808 167.204 204.222 1.00 104.91 ? 449 TYR B C   1 
ATOM   2688 O O   . TYR B 2 438 ? 129.692 167.444 203.754 1.00 104.91 ? 449 TYR B O   1 
ATOM   2689 C CB  . TYR B 2 438 ? 129.778 165.947 206.126 1.00 104.91 ? 449 TYR B CB  1 
ATOM   2690 C CG  . TYR B 2 438 ? 129.593 164.574 206.727 1.00 104.91 ? 449 TYR B CG  1 
ATOM   2691 C CD1 . TYR B 2 438 ? 130.502 163.558 206.475 1.00 104.91 ? 449 TYR B CD1 1 
ATOM   2692 C CD2 . TYR B 2 438 ? 128.516 164.295 207.555 1.00 104.91 ? 449 TYR B CD2 1 
ATOM   2693 C CE1 . TYR B 2 438 ? 130.343 162.305 207.023 1.00 104.91 ? 449 TYR B CE1 1 
ATOM   2694 C CE2 . TYR B 2 438 ? 128.351 163.042 208.109 1.00 104.91 ? 449 TYR B CE2 1 
ATOM   2695 C CZ  . TYR B 2 438 ? 129.269 162.052 207.838 1.00 104.91 ? 449 TYR B CZ  1 
ATOM   2696 O OH  . TYR B 2 438 ? 129.114 160.800 208.383 1.00 104.91 ? 449 TYR B OH  1 
ATOM   2697 N N   . ASN B 2 439 ? 131.879 167.924 203.909 1.00 105.64 ? 450 ASN B N   1 
ATOM   2698 C CA  . ASN B 2 439 ? 131.822 169.038 202.975 1.00 105.64 ? 450 ASN B CA  1 
ATOM   2699 C C   . ASN B 2 439 ? 132.122 168.627 201.543 1.00 105.64 ? 450 ASN B C   1 
ATOM   2700 O O   . ASN B 2 439 ? 132.165 169.491 200.663 1.00 105.64 ? 450 ASN B O   1 
ATOM   2701 C CB  . ASN B 2 439 ? 132.794 170.135 203.409 1.00 105.64 ? 450 ASN B CB  1 
ATOM   2702 C CG  . ASN B 2 439 ? 132.550 170.595 204.827 1.00 105.64 ? 450 ASN B CG  1 
ATOM   2703 O OD1 . ASN B 2 439 ? 133.469 170.642 205.643 1.00 105.64 ? 450 ASN B OD1 1 
ATOM   2704 N ND2 . ASN B 2 439 ? 131.304 170.934 205.131 1.00 105.64 ? 450 ASN B ND2 1 
ATOM   2705 N N   . TYR B 2 440 ? 132.341 167.342 201.289 1.00 104.66 ? 451 TYR B N   1 
ATOM   2706 C CA  . TYR B 2 440 ? 132.568 166.833 199.946 1.00 104.66 ? 451 TYR B CA  1 
ATOM   2707 C C   . TYR B 2 440 ? 131.434 165.892 199.572 1.00 104.66 ? 451 TYR B C   1 
ATOM   2708 O O   . TYR B 2 440 ? 131.140 164.947 200.309 1.00 104.66 ? 451 TYR B O   1 
ATOM   2709 C CB  . TYR B 2 440 ? 133.913 166.117 199.855 1.00 104.66 ? 451 TYR B CB  1 
ATOM   2710 C CG  . TYR B 2 440 ? 135.085 167.029 200.111 1.00 104.66 ? 451 TYR B CG  1 
ATOM   2711 C CD1 . TYR B 2 440 ? 135.316 168.130 199.304 1.00 104.66 ? 451 TYR B CD1 1 
ATOM   2712 C CD2 . TYR B 2 440 ? 135.954 166.796 201.162 1.00 104.66 ? 451 TYR B CD2 1 
ATOM   2713 C CE1 . TYR B 2 440 ? 136.380 168.970 199.533 1.00 104.66 ? 451 TYR B CE1 1 
ATOM   2714 C CE2 . TYR B 2 440 ? 137.021 167.631 201.399 1.00 104.66 ? 451 TYR B CE2 1 
ATOM   2715 C CZ  . TYR B 2 440 ? 137.231 168.716 200.581 1.00 104.66 ? 451 TYR B CZ  1 
ATOM   2716 O OH  . TYR B 2 440 ? 138.297 169.552 200.815 1.00 104.66 ? 451 TYR B OH  1 
ATOM   2717 N N   . LEU B 2 441 ? 130.803 166.152 198.431 1.00 104.66 ? 452 LEU B N   1 
ATOM   2718 C CA  . LEU B 2 441 ? 129.641 165.402 197.987 1.00 104.66 ? 452 LEU B CA  1 
ATOM   2719 C C   . LEU B 2 441 ? 129.861 164.909 196.566 1.00 104.66 ? 452 LEU B C   1 
ATOM   2720 O O   . LEU B 2 441 ? 130.825 165.282 195.897 1.00 104.66 ? 452 LEU B O   1 
ATOM   2721 C CB  . LEU B 2 441 ? 128.369 166.251 198.055 1.00 104.66 ? 452 LEU B CB  1 
ATOM   2722 C CG  . LEU B 2 441 ? 128.113 166.991 199.363 1.00 104.66 ? 452 LEU B CG  1 
ATOM   2723 C CD1 . LEU B 2 441 ? 126.905 167.887 199.232 1.00 104.66 ? 452 LEU B CD1 1 
ATOM   2724 C CD2 . LEU B 2 441 ? 127.912 166.004 200.484 1.00 104.66 ? 452 LEU B CD2 1 
ATOM   2725 N N   . TYR B 2 442 ? 128.951 164.053 196.113 1.00 104.66 ? 453 TYR B N   1 
ATOM   2726 C CA  . TYR B 2 442 ? 128.988 163.548 194.750 1.00 104.66 ? 453 TYR B CA  1 
ATOM   2727 C C   . TYR B 2 442 ? 127.596 163.077 194.366 1.00 104.66 ? 453 TYR B C   1 
ATOM   2728 O O   . TYR B 2 442 ? 126.843 162.581 195.205 1.00 104.66 ? 453 TYR B O   1 
ATOM   2729 C CB  . TYR B 2 442 ? 130.004 162.414 194.597 1.00 104.66 ? 453 TYR B CB  1 
ATOM   2730 C CG  . TYR B 2 442 ? 129.595 161.111 195.236 1.00 104.66 ? 453 TYR B CG  1 
ATOM   2731 C CD1 . TYR B 2 442 ? 129.484 160.996 196.608 1.00 104.66 ? 453 TYR B CD1 1 
ATOM   2732 C CD2 . TYR B 2 442 ? 129.340 159.991 194.466 1.00 104.66 ? 453 TYR B CD2 1 
ATOM   2733 C CE1 . TYR B 2 442 ? 129.118 159.811 197.193 1.00 104.66 ? 453 TYR B CE1 1 
ATOM   2734 C CE2 . TYR B 2 442 ? 128.975 158.802 195.044 1.00 104.66 ? 453 TYR B CE2 1 
ATOM   2735 C CZ  . TYR B 2 442 ? 128.866 158.719 196.407 1.00 104.66 ? 453 TYR B CZ  1 
ATOM   2736 O OH  . TYR B 2 442 ? 128.501 157.533 196.993 1.00 104.66 ? 453 TYR B OH  1 
ATOM   2737 N N   . ARG B 2 443 ? 127.264 163.243 193.091 1.00 104.66 ? 454 ARG B N   1 
ATOM   2738 C CA  . ARG B 2 443 ? 125.946 162.880 192.594 1.00 104.66 ? 454 ARG B CA  1 
ATOM   2739 C C   . ARG B 2 443 ? 125.853 161.377 192.393 1.00 104.66 ? 454 ARG B C   1 
ATOM   2740 O O   . ARG B 2 443 ? 126.808 160.735 191.952 1.00 104.66 ? 454 ARG B O   1 
ATOM   2741 C CB  . ARG B 2 443 ? 125.658 163.606 191.283 1.00 104.66 ? 454 ARG B CB  1 
ATOM   2742 C CG  . ARG B 2 443 ? 124.290 163.343 190.702 1.00 104.66 ? 454 ARG B CG  1 
ATOM   2743 C CD  . ARG B 2 443 ? 124.073 164.184 189.464 1.00 104.66 ? 454 ARG B CD  1 
ATOM   2744 N NE  . ARG B 2 443 ? 124.095 165.606 189.775 1.00 104.66 ? 454 ARG B NE  1 
ATOM   2745 C CZ  . ARG B 2 443 ? 123.045 166.289 190.207 1.00 104.66 ? 454 ARG B CZ  1 
ATOM   2746 N NH1 . ARG B 2 443 ? 121.867 165.713 190.368 1.00 104.66 ? 454 ARG B NH1 1 
ATOM   2747 N NH2 . ARG B 2 443 ? 123.181 167.581 190.481 1.00 104.66 ? 454 ARG B NH2 1 
ATOM   2748 N N   . LEU B 2 444 ? 124.696 160.817 192.716 1.00 104.66 ? 455 LEU B N   1 
ATOM   2749 C CA  . LEU B 2 444 ? 124.495 159.376 192.661 1.00 104.66 ? 455 LEU B CA  1 
ATOM   2750 C C   . LEU B 2 444 ? 123.436 158.945 191.661 1.00 104.66 ? 455 LEU B C   1 
ATOM   2751 O O   . LEU B 2 444 ? 123.615 157.931 190.985 1.00 104.66 ? 455 LEU B O   1 
ATOM   2752 C CB  . LEU B 2 444 ? 124.128 158.854 194.053 1.00 104.66 ? 455 LEU B CB  1 
ATOM   2753 C CG  . LEU B 2 444 ? 123.903 157.352 194.185 1.00 104.66 ? 455 LEU B CG  1 
ATOM   2754 C CD1 . LEU B 2 444 ? 125.081 156.594 193.619 1.00 104.66 ? 455 LEU B CD1 1 
ATOM   2755 C CD2 . LEU B 2 444 ? 123.692 156.991 195.639 1.00 104.66 ? 455 LEU B CD2 1 
ATOM   2756 N N   . PHE B 2 445 ? 122.338 159.685 191.541 1.00 104.66 ? 456 PHE B N   1 
ATOM   2757 C CA  . PHE B 2 445 ? 121.253 159.344 190.633 1.00 104.66 ? 456 PHE B CA  1 
ATOM   2758 C C   . PHE B 2 445 ? 121.092 160.428 189.579 1.00 104.66 ? 456 PHE B C   1 
ATOM   2759 O O   . PHE B 2 445 ? 121.169 161.620 189.886 1.00 104.66 ? 456 PHE B O   1 
ATOM   2760 C CB  . PHE B 2 445 ? 119.932 159.176 191.380 1.00 104.66 ? 456 PHE B CB  1 
ATOM   2761 C CG  . PHE B 2 445 ? 119.996 158.217 192.527 1.00 104.66 ? 456 PHE B CG  1 
ATOM   2762 C CD1 . PHE B 2 445 ? 120.024 156.855 192.306 1.00 104.66 ? 456 PHE B CD1 1 
ATOM   2763 C CD2 . PHE B 2 445 ? 120.011 158.679 193.829 1.00 104.66 ? 456 PHE B CD2 1 
ATOM   2764 C CE1 . PHE B 2 445 ? 120.075 155.974 193.360 1.00 104.66 ? 456 PHE B CE1 1 
ATOM   2765 C CE2 . PHE B 2 445 ? 120.062 157.803 194.886 1.00 104.66 ? 456 PHE B CE2 1 
ATOM   2766 C CZ  . PHE B 2 445 ? 120.094 156.449 194.653 1.00 104.66 ? 456 PHE B CZ  1 
ATOM   2767 N N   . ARG B 2 446 ? 120.859 160.009 188.339 1.00 104.66 ? 457 ARG B N   1 
ATOM   2768 C CA  . ARG B 2 446 ? 120.564 160.944 187.265 1.00 104.66 ? 457 ARG B CA  1 
ATOM   2769 C C   . ARG B 2 446 ? 119.753 160.215 186.207 1.00 104.66 ? 457 ARG B C   1 
ATOM   2770 O O   . ARG B 2 446 ? 119.886 159.002 186.035 1.00 104.66 ? 457 ARG B O   1 
ATOM   2771 C CB  . ARG B 2 446 ? 121.841 161.535 186.662 1.00 104.66 ? 457 ARG B CB  1 
ATOM   2772 C CG  . ARG B 2 446 ? 121.596 162.569 185.579 1.00 104.66 ? 457 ARG B CG  1 
ATOM   2773 C CD  . ARG B 2 446 ? 122.881 163.233 185.143 1.00 104.66 ? 457 ARG B CD  1 
ATOM   2774 N NE  . ARG B 2 446 ? 122.746 163.848 183.830 1.00 104.66 ? 457 ARG B NE  1 
ATOM   2775 C CZ  . ARG B 2 446 ? 122.277 165.068 183.620 1.00 104.66 ? 457 ARG B CZ  1 
ATOM   2776 N NH1 . ARG B 2 446 ? 121.900 165.843 184.622 1.00 104.66 ? 457 ARG B NH1 1 
ATOM   2777 N NH2 . ARG B 2 446 ? 122.187 165.524 182.374 1.00 104.66 ? 457 ARG B NH2 1 
ATOM   2778 N N   . LYS B 2 447 ? 118.902 160.970 185.507 1.00 104.66 ? 458 LYS B N   1 
ATOM   2779 C CA  . LYS B 2 447 ? 118.012 160.364 184.522 1.00 104.66 ? 458 LYS B CA  1 
ATOM   2780 C C   . LYS B 2 447 ? 118.788 159.765 183.355 1.00 104.66 ? 458 LYS B C   1 
ATOM   2781 O O   . LYS B 2 447 ? 118.480 158.656 182.904 1.00 104.66 ? 458 LYS B O   1 
ATOM   2782 C CB  . LYS B 2 447 ? 117.006 161.398 184.023 1.00 104.66 ? 458 LYS B CB  1 
ATOM   2783 C CG  . LYS B 2 447 ? 115.997 160.844 183.036 1.00 104.66 ? 458 LYS B CG  1 
ATOM   2784 C CD  . LYS B 2 447 ? 114.959 161.888 182.665 1.00 104.66 ? 458 LYS B CD  1 
ATOM   2785 C CE  . LYS B 2 447 ? 114.039 161.384 181.567 1.00 104.66 ? 458 LYS B CE  1 
ATOM   2786 N NZ  . LYS B 2 447 ? 113.203 160.242 182.028 1.00 104.66 ? 458 LYS B NZ  1 
ATOM   2787 N N   . SER B 2 448 ? 119.795 160.476 182.853 1.00 104.66 ? 459 SER B N   1 
ATOM   2788 C CA  . SER B 2 448 ? 120.567 159.994 181.717 1.00 104.66 ? 459 SER B CA  1 
ATOM   2789 C C   . SER B 2 448 ? 122.007 160.468 181.847 1.00 104.66 ? 459 SER B C   1 
ATOM   2790 O O   . SER B 2 448 ? 122.301 161.435 182.552 1.00 104.66 ? 459 SER B O   1 
ATOM   2791 C CB  . SER B 2 448 ? 119.964 160.461 180.389 1.00 104.66 ? 459 SER B CB  1 
ATOM   2792 O OG  . SER B 2 448 ? 119.936 161.873 180.312 1.00 104.66 ? 459 SER B OG  1 
ATOM   2793 N N   . ASN B 2 449 ? 122.901 159.777 181.144 1.00 104.66 ? 460 ASN B N   1 
ATOM   2794 C CA  . ASN B 2 449 ? 124.327 160.024 181.278 1.00 104.66 ? 460 ASN B CA  1 
ATOM   2795 C C   . ASN B 2 449 ? 124.689 161.426 180.805 1.00 104.66 ? 460 ASN B C   1 
ATOM   2796 O O   . ASN B 2 449 ? 123.890 162.134 180.189 1.00 104.66 ? 460 ASN B O   1 
ATOM   2797 C CB  . ASN B 2 449 ? 125.125 158.994 180.486 1.00 104.66 ? 460 ASN B CB  1 
ATOM   2798 C CG  . ASN B 2 449 ? 124.913 157.589 180.989 1.00 104.66 ? 460 ASN B CG  1 
ATOM   2799 O OD1 . ASN B 2 449 ? 124.059 157.347 181.838 1.00 104.66 ? 460 ASN B OD1 1 
ATOM   2800 N ND2 . ASN B 2 449 ? 125.691 156.650 180.468 1.00 104.66 ? 460 ASN B ND2 1 
ATOM   2801 N N   . LEU B 2 450 ? 125.920 161.823 181.108 1.00 104.66 ? 461 LEU B N   1 
ATOM   2802 C CA  . LEU B 2 450 ? 126.395 163.157 180.781 1.00 104.66 ? 461 LEU B CA  1 
ATOM   2803 C C   . LEU B 2 450 ? 127.090 163.176 179.427 1.00 104.66 ? 461 LEU B C   1 
ATOM   2804 O O   . LEU B 2 450 ? 127.673 162.183 178.987 1.00 104.66 ? 461 LEU B O   1 
ATOM   2805 C CB  . LEU B 2 450 ? 127.359 163.658 181.854 1.00 104.66 ? 461 LEU B CB  1 
ATOM   2806 C CG  . LEU B 2 450 ? 126.739 164.266 183.106 1.00 104.66 ? 461 LEU B CG  1 
ATOM   2807 C CD1 . LEU B 2 450 ? 127.794 164.972 183.922 1.00 104.66 ? 461 LEU B CD1 1 
ATOM   2808 C CD2 . LEU B 2 450 ? 125.647 165.231 182.720 1.00 104.66 ? 461 LEU B CD2 1 
ATOM   2809 N N   . LYS B 2 451 ? 127.013 164.313 178.768 1.00 104.66 ? 462 LYS B N   1 
ATOM   2810 C CA  . LYS B 2 451 ? 127.828 164.573 177.597 1.00 104.66 ? 462 LYS B CA  1 
ATOM   2811 C C   . LYS B 2 451 ? 129.189 165.097 178.026 1.00 104.66 ? 462 LYS B C   1 
ATOM   2812 O O   . LYS B 2 451 ? 129.330 165.660 179.114 1.00 104.66 ? 462 LYS B O   1 
ATOM   2813 C CB  . LYS B 2 451 ? 127.134 165.582 176.689 1.00 104.66 ? 462 LYS B CB  1 
ATOM   2814 C CG  . LYS B 2 451 ? 125.973 164.998 175.916 1.00 104.66 ? 462 LYS B CG  1 
ATOM   2815 C CD  . LYS B 2 451 ? 125.310 166.042 175.048 1.00 104.66 ? 462 LYS B CD  1 
ATOM   2816 C CE  . LYS B 2 451 ? 124.275 165.410 174.140 1.00 104.66 ? 462 LYS B CE  1 
ATOM   2817 N NZ  . LYS B 2 451 ? 123.635 166.417 173.252 1.00 104.66 ? 462 LYS B NZ  1 
ATOM   2818 N N   . PRO B 2 452 ? 130.219 164.918 177.201 1.00 104.66 ? 463 PRO B N   1 
ATOM   2819 C CA  . PRO B 2 452 ? 131.565 165.328 177.612 1.00 104.66 ? 463 PRO B CA  1 
ATOM   2820 C C   . PRO B 2 452 ? 131.634 166.804 177.976 1.00 104.66 ? 463 PRO B C   1 
ATOM   2821 O O   . PRO B 2 452 ? 131.040 167.656 177.316 1.00 104.66 ? 463 PRO B O   1 
ATOM   2822 C CB  . PRO B 2 452 ? 132.414 165.014 176.380 1.00 104.66 ? 463 PRO B CB  1 
ATOM   2823 C CG  . PRO B 2 452 ? 131.698 163.896 175.726 1.00 104.66 ? 463 PRO B CG  1 
ATOM   2824 C CD  . PRO B 2 452 ? 130.240 164.152 175.945 1.00 104.66 ? 463 PRO B CD  1 
ATOM   2825 N N   . PHE B 2 453 ? 132.363 167.088 179.053 1.00 104.66 ? 464 PHE B N   1 
ATOM   2826 C CA  . PHE B 2 453 ? 132.642 168.441 179.529 1.00 104.66 ? 464 PHE B CA  1 
ATOM   2827 C C   . PHE B 2 453 ? 131.382 169.221 179.876 1.00 104.66 ? 464 PHE B C   1 
ATOM   2828 O O   . PHE B 2 453 ? 131.375 170.452 179.799 1.00 104.66 ? 464 PHE B O   1 
ATOM   2829 C CB  . PHE B 2 453 ? 133.473 169.228 178.511 1.00 104.66 ? 464 PHE B CB  1 
ATOM   2830 C CG  . PHE B 2 453 ? 134.885 168.751 178.390 1.00 104.66 ? 464 PHE B CG  1 
ATOM   2831 C CD1 . PHE B 2 453 ? 135.616 168.426 179.512 1.00 104.66 ? 464 PHE B CD1 1 
ATOM   2832 C CD2 . PHE B 2 453 ? 135.483 168.630 177.151 1.00 104.66 ? 464 PHE B CD2 1 
ATOM   2833 C CE1 . PHE B 2 453 ? 136.912 167.987 179.403 1.00 104.66 ? 464 PHE B CE1 1 
ATOM   2834 C CE2 . PHE B 2 453 ? 136.778 168.192 177.037 1.00 104.66 ? 464 PHE B CE2 1 
ATOM   2835 C CZ  . PHE B 2 453 ? 137.493 167.870 178.163 1.00 104.66 ? 464 PHE B CZ  1 
ATOM   2836 N N   . GLU B 2 454 ? 130.311 168.543 180.271 1.00 104.66 ? 465 GLU B N   1 
ATOM   2837 C CA  . GLU B 2 454 ? 129.076 169.199 180.674 1.00 104.66 ? 465 GLU B CA  1 
ATOM   2838 C C   . GLU B 2 454 ? 128.903 169.057 182.178 1.00 104.66 ? 465 GLU B C   1 
ATOM   2839 O O   . GLU B 2 454 ? 129.095 167.969 182.727 1.00 104.66 ? 465 GLU B O   1 
ATOM   2840 C CB  . GLU B 2 454 ? 127.873 168.607 179.939 1.00 104.66 ? 465 GLU B CB  1 
ATOM   2841 C CG  . GLU B 2 454 ? 126.535 168.940 180.571 1.00 104.66 ? 465 GLU B CG  1 
ATOM   2842 C CD  . GLU B 2 454 ? 125.382 168.211 179.911 1.00 104.66 ? 465 GLU B CD  1 
ATOM   2843 O OE1 . GLU B 2 454 ? 124.478 168.886 179.380 1.00 104.66 ? 465 GLU B OE1 1 
ATOM   2844 O OE2 . GLU B 2 454 ? 125.378 166.963 179.925 1.00 104.66 ? 465 GLU B OE2 1 
ATOM   2845 N N   . ARG B 2 455 ? 128.546 170.152 182.840 1.00 104.66 ? 466 ARG B N   1 
ATOM   2846 C CA  . ARG B 2 455 ? 128.413 170.184 184.287 1.00 104.66 ? 466 ARG B CA  1 
ATOM   2847 C C   . ARG B 2 455 ? 126.956 170.371 184.679 1.00 104.66 ? 466 ARG B C   1 
ATOM   2848 O O   . ARG B 2 455 ? 126.255 171.215 184.114 1.00 104.66 ? 466 ARG B O   1 
ATOM   2849 C CB  . ARG B 2 455 ? 129.257 171.308 184.890 1.00 104.66 ? 466 ARG B CB  1 
ATOM   2850 C CG  . ARG B 2 455 ? 129.164 171.403 186.400 1.00 104.66 ? 466 ARG B CG  1 
ATOM   2851 C CD  . ARG B 2 455 ? 129.329 172.829 186.896 1.00 104.66 ? 466 ARG B CD  1 
ATOM   2852 N NE  . ARG B 2 455 ? 130.661 173.356 186.634 1.00 104.66 ? 466 ARG B NE  1 
ATOM   2853 C CZ  . ARG B 2 455 ? 130.971 174.127 185.603 1.00 104.66 ? 466 ARG B CZ  1 
ATOM   2854 N NH1 . ARG B 2 455 ? 130.063 174.485 184.712 1.00 104.66 ? 466 ARG B NH1 1 
ATOM   2855 N NH2 . ARG B 2 455 ? 132.223 174.549 185.461 1.00 104.66 ? 466 ARG B NH2 1 
ATOM   2856 N N   . ASP B 2 456 ? 126.505 169.580 185.647 1.00 104.66 ? 467 ASP B N   1 
ATOM   2857 C CA  . ASP B 2 456 ? 125.166 169.694 186.204 1.00 104.66 ? 467 ASP B CA  1 
ATOM   2858 C C   . ASP B 2 456 ? 125.277 170.053 187.677 1.00 104.66 ? 467 ASP B C   1 
ATOM   2859 O O   . ASP B 2 456 ? 126.017 169.404 188.421 1.00 104.66 ? 467 ASP B O   1 
ATOM   2860 C CB  . ASP B 2 456 ? 124.382 168.395 186.034 1.00 104.66 ? 467 ASP B CB  1 
ATOM   2861 C CG  . ASP B 2 456 ? 122.898 168.585 186.237 1.00 104.66 ? 467 ASP B CG  1 
ATOM   2862 O OD1 . ASP B 2 456 ? 122.481 169.725 186.531 1.00 104.66 ? 467 ASP B OD1 1 
ATOM   2863 O OD2 . ASP B 2 456 ? 122.146 167.598 186.106 1.00 104.66 ? 467 ASP B OD2 1 
ATOM   2864 N N   . ILE B 2 457 ? 124.537 171.076 188.094 1.00 104.66 ? 468 ILE B N   1 
ATOM   2865 C CA  . ILE B 2 457 ? 124.639 171.589 189.452 1.00 104.66 ? 468 ILE B CA  1 
ATOM   2866 C C   . ILE B 2 457 ? 123.340 171.449 190.238 1.00 104.66 ? 468 ILE B C   1 
ATOM   2867 O O   . ILE B 2 457 ? 123.378 171.460 191.479 1.00 104.66 ? 468 ILE B O   1 
ATOM   2868 C CB  . ILE B 2 457 ? 125.104 173.063 189.432 1.00 104.66 ? 468 ILE B CB  1 
ATOM   2869 C CG1 . ILE B 2 457 ? 125.181 173.662 190.836 1.00 104.66 ? 468 ILE B CG1 1 
ATOM   2870 C CG2 . ILE B 2 457 ? 124.178 173.894 188.570 1.00 104.66 ? 468 ILE B CG2 1 
ATOM   2871 C CD1 . ILE B 2 457 ? 126.210 173.007 191.716 1.00 104.66 ? 468 ILE B CD1 1 
ATOM   2872 N N   . SER B 2 458 ? 122.200 171.251 189.578 1.00 108.63 ? 469 SER B N   1 
ATOM   2873 C CA  . SER B 2 458 ? 120.899 171.231 190.239 1.00 108.63 ? 469 SER B CA  1 
ATOM   2874 C C   . SER B 2 458 ? 120.802 170.167 191.323 1.00 108.63 ? 469 SER B C   1 
ATOM   2875 O O   . SER B 2 458 ? 121.527 169.169 191.295 1.00 108.63 ? 469 SER B O   1 
ATOM   2876 C CB  . SER B 2 458 ? 119.790 171.008 189.212 1.00 108.63 ? 469 SER B CB  1 
ATOM   2877 O OG  . SER B 2 458 ? 118.630 170.489 189.837 1.00 108.63 ? 469 SER B OG  1 
ATOM   2878 N N   . THR B 2 459 ? 119.900 170.378 192.286 1.00 113.11 ? 470 THR B N   1 
ATOM   2879 C CA  . THR B 2 459 ? 119.716 169.450 193.394 1.00 113.11 ? 470 THR B CA  1 
ATOM   2880 C C   . THR B 2 459 ? 118.250 169.079 193.577 1.00 113.11 ? 470 THR B C   1 
ATOM   2881 O O   . THR B 2 459 ? 117.778 168.949 194.711 1.00 113.11 ? 470 THR B O   1 
ATOM   2882 C CB  . THR B 2 459 ? 120.253 170.031 194.702 1.00 113.11 ? 470 THR B CB  1 
ATOM   2883 O OG1 . THR B 2 459 ? 119.535 171.229 195.021 1.00 113.11 ? 470 THR B OG1 1 
ATOM   2884 C CG2 . THR B 2 459 ? 121.731 170.351 194.581 1.00 113.11 ? 470 THR B CG2 1 
ATOM   2885 N N   . GLU B 2 460 ? 117.514 168.913 192.484 1.00 115.51 ? 471 GLU B N   1 
ATOM   2886 C CA  . GLU B 2 460 ? 116.123 168.509 192.589 1.00 115.51 ? 471 GLU B CA  1 
ATOM   2887 C C   . GLU B 2 460 ? 116.025 167.035 192.971 1.00 115.51 ? 471 GLU B C   1 
ATOM   2888 O O   . GLU B 2 460 ? 116.940 166.242 192.738 1.00 115.51 ? 471 GLU B O   1 
ATOM   2889 C CB  . GLU B 2 460 ? 115.391 168.772 191.276 1.00 115.51 ? 471 GLU B CB  1 
ATOM   2890 C CG  . GLU B 2 460 ? 115.275 170.247 190.938 1.00 115.51 ? 471 GLU B CG  1 
ATOM   2891 C CD  . GLU B 2 460 ? 114.391 170.999 191.912 1.00 115.51 ? 471 GLU B CD  1 
ATOM   2892 O OE1 . GLU B 2 460 ? 113.435 170.395 192.440 1.00 115.51 ? 471 GLU B OE1 1 
ATOM   2893 O OE2 . GLU B 2 460 ? 114.655 172.195 192.154 1.00 115.51 ? 471 GLU B OE2 1 
ATOM   2894 N N   . ILE B 2 461 ? 114.894 166.670 193.562 1.00 114.69 ? 472 ILE B N   1 
ATOM   2895 C CA  . ILE B 2 461 ? 114.729 165.332 194.118 1.00 114.69 ? 472 ILE B CA  1 
ATOM   2896 C C   . ILE B 2 461 ? 114.490 164.334 192.995 1.00 114.69 ? 472 ILE B C   1 
ATOM   2897 O O   . ILE B 2 461 ? 113.593 164.510 192.165 1.00 114.69 ? 472 ILE B O   1 
ATOM   2898 C CB  . ILE B 2 461 ? 113.585 165.305 195.139 1.00 114.69 ? 472 ILE B CB  1 
ATOM   2899 C CG1 . ILE B 2 461 ? 113.921 166.214 196.318 1.00 114.69 ? 472 ILE B CG1 1 
ATOM   2900 C CG2 . ILE B 2 461 ? 113.336 163.891 195.616 1.00 114.69 ? 472 ILE B CG2 1 
ATOM   2901 C CD1 . ILE B 2 461 ? 112.765 166.454 197.244 1.00 114.69 ? 472 ILE B CD1 1 
ATOM   2902 N N   . TYR B 2 462 ? 115.296 163.279 192.977 1.00 110.78 ? 473 TYR B N   1 
ATOM   2903 C CA  . TYR B 2 462 ? 115.179 162.237 191.970 1.00 110.78 ? 473 TYR B CA  1 
ATOM   2904 C C   . TYR B 2 462 ? 113.916 161.421 192.199 1.00 110.78 ? 473 TYR B C   1 
ATOM   2905 O O   . TYR B 2 462 ? 113.540 161.137 193.338 1.00 110.78 ? 473 TYR B O   1 
ATOM   2906 C CB  . TYR B 2 462 ? 116.412 161.341 192.022 1.00 110.78 ? 473 TYR B CB  1 
ATOM   2907 C CG  . TYR B 2 462 ? 116.424 160.181 191.063 1.00 110.78 ? 473 TYR B CG  1 
ATOM   2908 C CD1 . TYR B 2 462 ? 116.626 160.378 189.708 1.00 110.78 ? 473 TYR B CD1 1 
ATOM   2909 C CD2 . TYR B 2 462 ? 116.283 158.883 191.521 1.00 110.78 ? 473 TYR B CD2 1 
ATOM   2910 C CE1 . TYR B 2 462 ? 116.660 159.317 188.834 1.00 110.78 ? 473 TYR B CE1 1 
ATOM   2911 C CE2 . TYR B 2 462 ? 116.317 157.817 190.655 1.00 110.78 ? 473 TYR B CE2 1 
ATOM   2912 C CZ  . TYR B 2 462 ? 116.505 158.039 189.314 1.00 110.78 ? 473 TYR B CZ  1 
ATOM   2913 O OH  . TYR B 2 462 ? 116.536 156.974 188.448 1.00 110.78 ? 473 TYR B OH  1 
ATOM   2914 N N   . GLN B 2 463 ? 113.256 161.047 191.108 1.00 123.94 ? 474 GLN B N   1 
ATOM   2915 C CA  . GLN B 2 463 ? 111.998 160.306 191.155 1.00 123.94 ? 474 GLN B CA  1 
ATOM   2916 C C   . GLN B 2 463 ? 112.276 158.886 190.679 1.00 123.94 ? 474 GLN B C   1 
ATOM   2917 O O   . GLN B 2 463 ? 112.355 158.630 189.475 1.00 123.94 ? 474 GLN B O   1 
ATOM   2918 C CB  . GLN B 2 463 ? 110.937 160.987 190.296 1.00 123.94 ? 474 GLN B CB  1 
ATOM   2919 C CG  . GLN B 2 463 ? 110.323 162.220 190.935 1.00 123.94 ? 474 GLN B CG  1 
ATOM   2920 C CD  . GLN B 2 463 ? 108.946 162.539 190.392 1.00 123.94 ? 474 GLN B CD  1 
ATOM   2921 O OE1 . GLN B 2 463 ? 108.235 163.387 190.930 1.00 123.94 ? 474 GLN B OE1 1 
ATOM   2922 N NE2 . GLN B 2 463 ? 108.560 161.855 189.322 1.00 123.94 ? 474 GLN B NE2 1 
ATOM   2923 N N   . ALA B 2 464 ? 112.414 157.962 191.623 1.00 119.84 ? 475 ALA B N   1 
ATOM   2924 C CA  . ALA B 2 464 ? 112.804 156.596 191.309 1.00 119.84 ? 475 ALA B CA  1 
ATOM   2925 C C   . ALA B 2 464 ? 111.622 155.656 191.129 1.00 119.84 ? 475 ALA B C   1 
ATOM   2926 O O   . ALA B 2 464 ? 111.832 154.458 190.923 1.00 119.84 ? 475 ALA B O   1 
ATOM   2927 C CB  . ALA B 2 464 ? 113.725 156.047 192.401 1.00 119.84 ? 475 ALA B CB  1 
ATOM   2928 N N   . GLY B 2 465 ? 110.395 156.159 191.202 1.00 129.22 ? 476 GLY B N   1 
ATOM   2929 C CA  . GLY B 2 465 ? 109.238 155.293 191.105 1.00 129.22 ? 476 GLY B CA  1 
ATOM   2930 C C   . GLY B 2 465 ? 108.115 155.860 190.265 1.00 129.22 ? 476 GLY B C   1 
ATOM   2931 O O   . GLY B 2 465 ? 108.268 156.908 189.631 1.00 129.22 ? 476 GLY B O   1 
ATOM   2932 N N   . SER B 2 466 ? 106.974 155.170 190.254 1.00 136.52 ? 477 SER B N   1 
ATOM   2933 C CA  . SER B 2 466 ? 105.835 155.599 189.456 1.00 136.52 ? 477 SER B CA  1 
ATOM   2934 C C   . SER B 2 466 ? 105.102 156.789 190.057 1.00 136.52 ? 477 SER B C   1 
ATOM   2935 O O   . SER B 2 466 ? 104.487 157.560 189.313 1.00 136.52 ? 477 SER B O   1 
ATOM   2936 C CB  . SER B 2 466 ? 104.856 154.439 189.278 1.00 136.52 ? 477 SER B CB  1 
ATOM   2937 O OG  . SER B 2 466 ? 105.467 153.361 188.594 1.00 136.52 ? 477 SER B OG  1 
ATOM   2938 N N   . THR B 2 467 ? 105.157 156.964 191.373 1.00 139.39 ? 478 THR B N   1 
ATOM   2939 C CA  . THR B 2 467 ? 104.426 158.041 192.022 1.00 139.39 ? 478 THR B CA  1 
ATOM   2940 C C   . THR B 2 467 ? 105.258 159.313 192.001 1.00 139.39 ? 478 THR B C   1 
ATOM   2941 O O   . THR B 2 467 ? 106.364 159.324 192.559 1.00 139.39 ? 478 THR B O   1 
ATOM   2942 C CB  . THR B 2 467 ? 104.086 157.672 193.454 1.00 139.39 ? 478 THR B CB  1 
ATOM   2943 O OG1 . THR B 2 467 ? 103.273 156.493 193.462 1.00 139.39 ? 478 THR B OG1 1 
ATOM   2944 C CG2 . THR B 2 467 ? 103.331 158.806 194.124 1.00 139.39 ? 478 THR B CG2 1 
ATOM   2945 N N   . PRO B 2 468 ? 104.783 160.391 191.378 1.00 141.03 ? 479 PRO B N   1 
ATOM   2946 C CA  . PRO B 2 468 ? 105.551 161.641 191.376 1.00 141.03 ? 479 PRO B CA  1 
ATOM   2947 C C   . PRO B 2 468 ? 105.763 162.169 192.787 1.00 141.03 ? 479 PRO B C   1 
ATOM   2948 O O   . PRO B 2 468 ? 104.899 162.040 193.657 1.00 141.03 ? 479 PRO B O   1 
ATOM   2949 C CB  . PRO B 2 468 ? 104.685 162.591 190.541 1.00 141.03 ? 479 PRO B CB  1 
ATOM   2950 C CG  . PRO B 2 468 ? 103.321 161.980 190.545 1.00 141.03 ? 479 PRO B CG  1 
ATOM   2951 C CD  . PRO B 2 468 ? 103.534 160.504 190.609 1.00 141.03 ? 479 PRO B CD  1 
ATOM   2952 N N   . CYS B 2 469 ? 106.932 162.769 193.007 1.00 140.39 ? 480 CYS B N   1 
ATOM   2953 C CA  . CYS B 2 469 ? 107.314 163.232 194.335 1.00 140.39 ? 480 CYS B CA  1 
ATOM   2954 C C   . CYS B 2 469 ? 106.868 164.657 194.621 1.00 140.39 ? 480 CYS B C   1 
ATOM   2955 O O   . CYS B 2 469 ? 106.727 165.026 195.792 1.00 140.39 ? 480 CYS B O   1 
ATOM   2956 C CB  . CYS B 2 469 ? 108.831 163.129 194.509 1.00 140.39 ? 480 CYS B CB  1 
ATOM   2957 S SG  . CYS B 2 469 ? 109.488 161.464 194.273 1.00 140.39 ? 480 CYS B SG  1 
ATOM   2958 N N   . ASN B 2 470 ? 106.656 165.466 193.582 1.00 139.10 ? 481 ASN B N   1 
ATOM   2959 C CA  . ASN B 2 470 ? 106.190 166.845 193.727 1.00 139.10 ? 481 ASN B CA  1 
ATOM   2960 C C   . ASN B 2 470 ? 107.149 167.690 194.561 1.00 139.10 ? 481 ASN B C   1 
ATOM   2961 O O   . ASN B 2 470 ? 106.730 168.624 195.248 1.00 139.10 ? 481 ASN B O   1 
ATOM   2962 C CB  . ASN B 2 470 ? 104.782 166.898 194.325 1.00 139.10 ? 481 ASN B CB  1 
ATOM   2963 C CG  . ASN B 2 470 ? 103.717 166.472 193.341 1.00 139.10 ? 481 ASN B CG  1 
ATOM   2964 O OD1 . ASN B 2 470 ? 103.135 165.395 193.468 1.00 139.10 ? 481 ASN B OD1 1 
ATOM   2965 N ND2 . ASN B 2 470 ? 103.453 167.317 192.352 1.00 139.10 ? 481 ASN B ND2 1 
ATOM   2966 N N   . GLY B 2 471 ? 108.439 167.371 194.513 1.00 133.39 ? 482 GLY B N   1 
ATOM   2967 C CA  . GLY B 2 471 ? 109.432 168.200 195.166 1.00 133.39 ? 482 GLY B CA  1 
ATOM   2968 C C   . GLY B 2 471 ? 109.614 167.979 196.649 1.00 133.39 ? 482 GLY B C   1 
ATOM   2969 O O   . GLY B 2 471 ? 110.250 168.805 197.308 1.00 133.39 ? 482 GLY B O   1 
ATOM   2970 N N   . VAL B 2 472 ? 109.076 166.896 197.204 1.00 128.16 ? 483 VAL B N   1 
ATOM   2971 C CA  . VAL B 2 472 ? 109.294 166.541 198.600 1.00 128.16 ? 483 VAL B CA  1 
ATOM   2972 C C   . VAL B 2 472 ? 109.845 165.123 198.655 1.00 128.16 ? 483 VAL B C   1 
ATOM   2973 O O   . VAL B 2 472 ? 109.438 164.257 197.873 1.00 128.16 ? 483 VAL B O   1 
ATOM   2974 C CB  . VAL B 2 472 ? 108.006 166.672 199.441 1.00 128.16 ? 483 VAL B CB  1 
ATOM   2975 C CG1 . VAL B 2 472 ? 107.472 168.088 199.364 1.00 128.16 ? 483 VAL B CG1 1 
ATOM   2976 C CG2 . VAL B 2 472 ? 106.952 165.688 198.975 1.00 128.16 ? 483 VAL B CG2 1 
ATOM   2977 N N   . GLU B 2 473 ? 110.796 164.896 199.556 1.00 125.73 ? 484 GLU B N   1 
ATOM   2978 C CA  . GLU B 2 473 ? 111.427 163.590 199.637 1.00 125.73 ? 484 GLU B CA  1 
ATOM   2979 C C   . GLU B 2 473 ? 110.580 162.628 200.463 1.00 125.73 ? 484 GLU B C   1 
ATOM   2980 O O   . GLU B 2 473 ? 109.769 163.026 201.303 1.00 125.73 ? 484 GLU B O   1 
ATOM   2981 C CB  . GLU B 2 473 ? 112.829 163.694 200.235 1.00 125.73 ? 484 GLU B CB  1 
ATOM   2982 C CG  . GLU B 2 473 ? 112.908 164.452 201.545 1.00 125.73 ? 484 GLU B CG  1 
ATOM   2983 C CD  . GLU B 2 473 ? 114.337 164.634 202.019 1.00 125.73 ? 484 GLU B CD  1 
ATOM   2984 O OE1 . GLU B 2 473 ? 114.668 165.727 202.521 1.00 125.73 ? 484 GLU B OE1 1 
ATOM   2985 O OE2 . GLU B 2 473 ? 115.130 163.680 201.892 1.00 125.73 ? 484 GLU B OE2 1 
ATOM   2986 N N   . GLY B 2 474 ? 110.791 161.343 200.212 1.00 123.76 ? 485 GLY B N   1 
ATOM   2987 C CA  . GLY B 2 474 ? 110.038 160.305 200.883 1.00 123.76 ? 485 GLY B CA  1 
ATOM   2988 C C   . GLY B 2 474 ? 110.402 158.954 200.304 1.00 123.76 ? 485 GLY B C   1 
ATOM   2989 O O   . GLY B 2 474 ? 111.444 158.795 199.666 1.00 123.76 ? 485 GLY B O   1 
ATOM   2990 N N   . PHE B 2 475 ? 109.525 157.983 200.542 1.00 120.10 ? 486 PHE B N   1 
ATOM   2991 C CA  . PHE B 2 475 ? 109.721 156.667 199.953 1.00 120.10 ? 486 PHE B CA  1 
ATOM   2992 C C   . PHE B 2 475 ? 109.734 156.778 198.436 1.00 120.10 ? 486 PHE B C   1 
ATOM   2993 O O   . PHE B 2 475 ? 108.860 157.412 197.840 1.00 120.10 ? 486 PHE B O   1 
ATOM   2994 C CB  . PHE B 2 475 ? 108.625 155.705 200.408 1.00 120.10 ? 486 PHE B CB  1 
ATOM   2995 C CG  . PHE B 2 475 ? 108.777 155.240 201.825 1.00 120.10 ? 486 PHE B CG  1 
ATOM   2996 C CD1 . PHE B 2 475 ? 108.613 156.118 202.880 1.00 120.10 ? 486 PHE B CD1 1 
ATOM   2997 C CD2 . PHE B 2 475 ? 109.095 153.925 202.102 1.00 120.10 ? 486 PHE B CD2 1 
ATOM   2998 C CE1 . PHE B 2 475 ? 108.754 155.689 204.181 1.00 120.10 ? 486 PHE B CE1 1 
ATOM   2999 C CE2 . PHE B 2 475 ? 109.239 153.493 203.400 1.00 120.10 ? 486 PHE B CE2 1 
ATOM   3000 C CZ  . PHE B 2 475 ? 109.068 154.376 204.441 1.00 120.10 ? 486 PHE B CZ  1 
ATOM   3001 N N   . ASN B 2 476 ? 110.743 156.167 197.817 1.00 119.24 ? 487 ASN B N   1 
ATOM   3002 C CA  . ASN B 2 476 ? 110.961 156.251 196.375 1.00 119.24 ? 487 ASN B CA  1 
ATOM   3003 C C   . ASN B 2 476 ? 111.149 157.694 195.916 1.00 119.24 ? 487 ASN B C   1 
ATOM   3004 O O   . ASN B 2 476 ? 110.852 158.038 194.771 1.00 119.24 ? 487 ASN B O   1 
ATOM   3005 C CB  . ASN B 2 476 ? 109.823 155.584 195.604 1.00 119.24 ? 487 ASN B CB  1 
ATOM   3006 C CG  . ASN B 2 476 ? 109.823 154.082 195.764 1.00 119.24 ? 487 ASN B CG  1 
ATOM   3007 O OD1 . ASN B 2 476 ? 110.873 153.444 195.735 1.00 119.24 ? 487 ASN B OD1 1 
ATOM   3008 N ND2 . ASN B 2 476 ? 108.641 153.507 195.940 1.00 119.24 ? 487 ASN B ND2 1 
ATOM   3009 N N   . CYS B 2 477 ? 111.649 158.548 196.810 1.00 120.22 ? 488 CYS B N   1 
ATOM   3010 C CA  . CYS B 2 477 ? 111.953 159.949 196.502 1.00 120.22 ? 488 CYS B CA  1 
ATOM   3011 C C   . CYS B 2 477 ? 113.251 160.278 197.235 1.00 120.22 ? 488 CYS B C   1 
ATOM   3012 O O   . CYS B 2 477 ? 113.229 160.705 198.391 1.00 120.22 ? 488 CYS B O   1 
ATOM   3013 C CB  . CYS B 2 477 ? 110.818 160.871 196.923 1.00 120.22 ? 488 CYS B CB  1 
ATOM   3014 S SG  . CYS B 2 477 ? 109.253 160.572 196.080 1.00 120.22 ? 488 CYS B SG  1 
ATOM   3015 N N   . TYR B 2 478 ? 114.374 160.090 196.553 1.00 109.17 ? 489 TYR B N   1 
ATOM   3016 C CA  . TYR B 2 478 ? 115.687 160.173 197.174 1.00 109.17 ? 489 TYR B CA  1 
ATOM   3017 C C   . TYR B 2 478 ? 116.369 161.488 196.838 1.00 109.17 ? 489 TYR B C   1 
ATOM   3018 O O   . TYR B 2 478 ? 116.258 161.989 195.717 1.00 109.17 ? 489 TYR B O   1 
ATOM   3019 C CB  . TYR B 2 478 ? 116.575 159.016 196.722 1.00 109.17 ? 489 TYR B CB  1 
ATOM   3020 C CG  . TYR B 2 478 ? 115.917 157.664 196.798 1.00 109.17 ? 489 TYR B CG  1 
ATOM   3021 C CD1 . TYR B 2 478 ? 115.255 157.258 197.943 1.00 109.17 ? 489 TYR B CD1 1 
ATOM   3022 C CD2 . TYR B 2 478 ? 115.968 156.789 195.727 1.00 109.17 ? 489 TYR B CD2 1 
ATOM   3023 C CE1 . TYR B 2 478 ? 114.659 156.023 198.017 1.00 109.17 ? 489 TYR B CE1 1 
ATOM   3024 C CE2 . TYR B 2 478 ? 115.375 155.551 195.792 1.00 109.17 ? 489 TYR B CE2 1 
ATOM   3025 C CZ  . TYR B 2 478 ? 114.722 155.173 196.939 1.00 109.17 ? 489 TYR B CZ  1 
ATOM   3026 O OH  . TYR B 2 478 ? 114.127 153.936 197.008 1.00 109.17 ? 489 TYR B OH  1 
ATOM   3027 N N   . PHE B 2 479 ? 117.072 162.042 197.816 1.00 104.66 ? 490 PHE B N   1 
ATOM   3028 C CA  . PHE B 2 479 ? 117.942 163.179 197.555 1.00 104.66 ? 490 PHE B CA  1 
ATOM   3029 C C   . PHE B 2 479 ? 119.091 162.726 196.664 1.00 104.66 ? 490 PHE B C   1 
ATOM   3030 O O   . PHE B 2 479 ? 119.647 161.645 196.884 1.00 104.66 ? 490 PHE B O   1 
ATOM   3031 C CB  . PHE B 2 479 ? 118.473 163.752 198.861 1.00 104.66 ? 490 PHE B CB  1 
ATOM   3032 C CG  . PHE B 2 479 ? 119.006 165.144 198.737 1.00 104.66 ? 490 PHE B CG  1 
ATOM   3033 C CD1 . PHE B 2 479 ? 118.147 166.223 198.688 1.00 104.66 ? 490 PHE B CD1 1 
ATOM   3034 C CD2 . PHE B 2 479 ? 120.364 165.374 198.669 1.00 104.66 ? 490 PHE B CD2 1 
ATOM   3035 C CE1 . PHE B 2 479 ? 118.633 167.505 198.575 1.00 104.66 ? 490 PHE B CE1 1 
ATOM   3036 C CE2 . PHE B 2 479 ? 120.856 166.654 198.557 1.00 104.66 ? 490 PHE B CE2 1 
ATOM   3037 C CZ  . PHE B 2 479 ? 119.989 167.720 198.509 1.00 104.66 ? 490 PHE B CZ  1 
ATOM   3038 N N   . PRO B 2 480 ? 119.476 163.507 195.655 1.00 104.66 ? 491 PRO B N   1 
ATOM   3039 C CA  . PRO B 2 480 ? 120.408 163.006 194.639 1.00 104.66 ? 491 PRO B CA  1 
ATOM   3040 C C   . PRO B 2 480 ? 121.880 163.106 195.005 1.00 104.66 ? 491 PRO B C   1 
ATOM   3041 O O   . PRO B 2 480 ? 122.721 162.722 194.187 1.00 104.66 ? 491 PRO B O   1 
ATOM   3042 C CB  . PRO B 2 480 ? 120.088 163.894 193.435 1.00 104.66 ? 491 PRO B CB  1 
ATOM   3043 C CG  . PRO B 2 480 ? 119.686 165.181 194.047 1.00 104.66 ? 491 PRO B CG  1 
ATOM   3044 C CD  . PRO B 2 480 ? 118.968 164.847 195.323 1.00 104.66 ? 491 PRO B CD  1 
ATOM   3045 N N   . LEU B 2 481 ? 122.233 163.601 196.187 1.00 104.66 ? 492 LEU B N   1 
ATOM   3046 C CA  . LEU B 2 481 ? 123.626 163.810 196.553 1.00 104.66 ? 492 LEU B CA  1 
ATOM   3047 C C   . LEU B 2 481 ? 123.969 163.030 197.814 1.00 104.66 ? 492 LEU B C   1 
ATOM   3048 O O   . LEU B 2 481 ? 123.130 162.853 198.699 1.00 104.66 ? 492 LEU B O   1 
ATOM   3049 C CB  . LEU B 2 481 ? 123.918 165.296 196.762 1.00 104.66 ? 492 LEU B CB  1 
ATOM   3050 C CG  . LEU B 2 481 ? 124.393 166.076 195.537 1.00 104.66 ? 492 LEU B CG  1 
ATOM   3051 C CD1 . LEU B 2 481 ? 123.296 166.201 194.513 1.00 104.66 ? 492 LEU B CD1 1 
ATOM   3052 C CD2 . LEU B 2 481 ? 124.874 167.449 195.949 1.00 104.66 ? 492 LEU B CD2 1 
ATOM   3053 N N   . GLN B 2 482 ? 125.213 162.561 197.889 1.00 104.66 ? 493 GLN B N   1 
ATOM   3054 C CA  . GLN B 2 482 ? 125.684 161.788 199.029 1.00 104.66 ? 493 GLN B CA  1 
ATOM   3055 C C   . GLN B 2 482 ? 127.082 162.244 199.415 1.00 104.66 ? 493 GLN B C   1 
ATOM   3056 O O   . GLN B 2 482 ? 127.816 162.809 198.604 1.00 104.66 ? 493 GLN B O   1 
ATOM   3057 C CB  . GLN B 2 482 ? 125.680 160.288 198.733 1.00 104.66 ? 493 GLN B CB  1 
ATOM   3058 C CG  . GLN B 2 482 ? 124.302 159.734 198.468 1.00 104.66 ? 493 GLN B CG  1 
ATOM   3059 C CD  . GLN B 2 482 ? 123.497 159.589 199.736 1.00 104.66 ? 493 GLN B CD  1 
ATOM   3060 O OE1 . GLN B 2 482 ? 123.941 158.964 200.696 1.00 104.66 ? 493 GLN B OE1 1 
ATOM   3061 N NE2 . GLN B 2 482 ? 122.309 160.177 199.752 1.00 104.66 ? 493 GLN B NE2 1 
ATOM   3062 N N   . SER B 2 483 ? 127.448 161.984 200.666 1.00 104.66 ? 494 SER B N   1 
ATOM   3063 C CA  . SER B 2 483 ? 128.690 162.482 201.242 1.00 104.66 ? 494 SER B CA  1 
ATOM   3064 C C   . SER B 2 483 ? 129.757 161.399 201.279 1.00 104.66 ? 494 SER B C   1 
ATOM   3065 O O   . SER B 2 483 ? 129.463 160.229 201.532 1.00 104.66 ? 494 SER B O   1 
ATOM   3066 C CB  . SER B 2 483 ? 128.460 163.007 202.656 1.00 104.66 ? 494 SER B CB  1 
ATOM   3067 O OG  . SER B 2 483 ? 129.691 163.157 203.335 1.00 104.66 ? 494 SER B OG  1 
ATOM   3068 N N   . TYR B 2 484 ? 131.005 161.805 201.038 1.00 104.66 ? 495 TYR B N   1 
ATOM   3069 C CA  . TYR B 2 484 ? 132.112 160.857 201.061 1.00 104.66 ? 495 TYR B CA  1 
ATOM   3070 C C   . TYR B 2 484 ? 132.470 160.456 202.485 1.00 104.66 ? 495 TYR B C   1 
ATOM   3071 O O   . TYR B 2 484 ? 132.747 159.283 202.754 1.00 104.66 ? 495 TYR B O   1 
ATOM   3072 C CB  . TYR B 2 484 ? 133.329 161.454 200.361 1.00 104.66 ? 495 TYR B CB  1 
ATOM   3073 C CG  . TYR B 2 484 ? 133.403 161.158 198.885 1.00 104.66 ? 495 TYR B CG  1 
ATOM   3074 C CD1 . TYR B 2 484 ? 133.467 159.858 198.425 1.00 104.66 ? 495 TYR B CD1 1 
ATOM   3075 C CD2 . TYR B 2 484 ? 133.422 162.182 197.955 1.00 104.66 ? 495 TYR B CD2 1 
ATOM   3076 C CE1 . TYR B 2 484 ? 133.540 159.585 197.082 1.00 104.66 ? 495 TYR B CE1 1 
ATOM   3077 C CE2 . TYR B 2 484 ? 133.494 161.918 196.612 1.00 104.66 ? 495 TYR B CE2 1 
ATOM   3078 C CZ  . TYR B 2 484 ? 133.553 160.617 196.181 1.00 104.66 ? 495 TYR B CZ  1 
ATOM   3079 O OH  . TYR B 2 484 ? 133.626 160.345 194.839 1.00 104.66 ? 495 TYR B OH  1 
ATOM   3080 N N   . GLY B 2 485 ? 132.483 161.414 203.406 1.00 104.66 ? 496 GLY B N   1 
ATOM   3081 C CA  . GLY B 2 485 ? 132.807 161.124 204.788 1.00 104.66 ? 496 GLY B CA  1 
ATOM   3082 C C   . GLY B 2 485 ? 134.241 160.691 205.002 1.00 104.66 ? 496 GLY B C   1 
ATOM   3083 O O   . GLY B 2 485 ? 134.497 159.575 205.459 1.00 104.66 ? 496 GLY B O   1 
ATOM   3084 N N   . PHE B 2 486 ? 135.186 161.566 204.673 1.00 104.66 ? 497 PHE B N   1 
ATOM   3085 C CA  . PHE B 2 486 ? 136.596 161.238 204.826 1.00 104.66 ? 497 PHE B CA  1 
ATOM   3086 C C   . PHE B 2 486 ? 137.002 161.259 206.292 1.00 104.66 ? 497 PHE B C   1 
ATOM   3087 O O   . PHE B 2 486 ? 136.503 162.064 207.081 1.00 104.66 ? 497 PHE B O   1 
ATOM   3088 C CB  . PHE B 2 486 ? 137.455 162.216 204.035 1.00 104.66 ? 497 PHE B CB  1 
ATOM   3089 C CG  . PHE B 2 486 ? 137.229 162.159 202.559 1.00 104.66 ? 497 PHE B CG  1 
ATOM   3090 C CD1 . PHE B 2 486 ? 137.393 160.979 201.870 1.00 104.66 ? 497 PHE B CD1 1 
ATOM   3091 C CD2 . PHE B 2 486 ? 136.861 163.289 201.861 1.00 104.66 ? 497 PHE B CD2 1 
ATOM   3092 C CE1 . PHE B 2 486 ? 137.191 160.927 200.515 1.00 104.66 ? 497 PHE B CE1 1 
ATOM   3093 C CE2 . PHE B 2 486 ? 136.658 163.240 200.507 1.00 104.66 ? 497 PHE B CE2 1 
ATOM   3094 C CZ  . PHE B 2 486 ? 136.822 162.058 199.833 1.00 104.66 ? 497 PHE B CZ  1 
ATOM   3095 N N   . GLN B 2 487 ? 137.915 160.364 206.655 1.00 105.48 ? 498 GLN B N   1 
ATOM   3096 C CA  . GLN B 2 487 ? 138.429 160.267 208.010 1.00 105.48 ? 498 GLN B CA  1 
ATOM   3097 C C   . GLN B 2 487 ? 139.906 159.914 207.963 1.00 105.48 ? 498 GLN B C   1 
ATOM   3098 O O   . GLN B 2 487 ? 140.356 159.239 207.030 1.00 105.48 ? 498 GLN B O   1 
ATOM   3099 C CB  . GLN B 2 487 ? 137.667 159.211 208.822 1.00 105.48 ? 498 GLN B CB  1 
ATOM   3100 C CG  . GLN B 2 487 ? 136.468 159.766 209.555 1.00 105.48 ? 498 GLN B CG  1 
ATOM   3101 C CD  . GLN B 2 487 ? 135.549 158.686 210.071 1.00 105.48 ? 498 GLN B CD  1 
ATOM   3102 O OE1 . GLN B 2 487 ? 134.339 158.881 210.164 1.00 105.48 ? 498 GLN B OE1 1 
ATOM   3103 N NE2 . GLN B 2 487 ? 136.118 157.537 210.411 1.00 105.48 ? 498 GLN B NE2 1 
ATOM   3104 N N   . PRO B 2 488 ? 140.685 160.351 208.957 1.00 108.22 ? 499 PRO B N   1 
ATOM   3105 C CA  . PRO B 2 488 ? 142.127 160.062 208.939 1.00 108.22 ? 499 PRO B CA  1 
ATOM   3106 C C   . PRO B 2 488 ? 142.462 158.590 209.075 1.00 108.22 ? 499 PRO B C   1 
ATOM   3107 O O   . PRO B 2 488 ? 143.578 158.194 208.719 1.00 108.22 ? 499 PRO B O   1 
ATOM   3108 C CB  . PRO B 2 488 ? 142.660 160.862 210.133 1.00 108.22 ? 499 PRO B CB  1 
ATOM   3109 C CG  . PRO B 2 488 ? 141.489 161.006 211.035 1.00 108.22 ? 499 PRO B CG  1 
ATOM   3110 C CD  . PRO B 2 488 ? 140.298 161.139 210.139 1.00 108.22 ? 499 PRO B CD  1 
ATOM   3111 N N   . THR B 2 489 ? 141.548 157.768 209.579 1.00 108.34 ? 500 THR B N   1 
ATOM   3112 C CA  . THR B 2 489 ? 141.826 156.361 209.823 1.00 108.34 ? 500 THR B CA  1 
ATOM   3113 C C   . THR B 2 489 ? 141.345 155.451 208.703 1.00 108.34 ? 500 THR B C   1 
ATOM   3114 O O   . THR B 2 489 ? 141.435 154.229 208.839 1.00 108.34 ? 500 THR B O   1 
ATOM   3115 C CB  . THR B 2 489 ? 141.190 155.923 211.142 1.00 108.34 ? 500 THR B CB  1 
ATOM   3116 O OG1 . THR B 2 489 ? 139.766 156.031 211.042 1.00 108.34 ? 500 THR B OG1 1 
ATOM   3117 C CG2 . THR B 2 489 ? 141.677 156.804 212.277 1.00 108.34 ? 500 THR B CG2 1 
ATOM   3118 N N   . ASN B 2 490 ? 140.839 156.008 207.609 1.00 106.59 ? 501 ASN B N   1 
ATOM   3119 C CA  . ASN B 2 490 ? 140.344 155.183 206.520 1.00 106.59 ? 501 ASN B CA  1 
ATOM   3120 C C   . ASN B 2 490 ? 141.497 154.491 205.799 1.00 106.59 ? 501 ASN B C   1 
ATOM   3121 O O   . ASN B 2 490 ? 142.659 154.891 205.893 1.00 106.59 ? 501 ASN B O   1 
ATOM   3122 C CB  . ASN B 2 490 ? 139.545 156.025 205.527 1.00 106.59 ? 501 ASN B CB  1 
ATOM   3123 C CG  . ASN B 2 490 ? 138.187 156.420 206.062 1.00 106.59 ? 501 ASN B CG  1 
ATOM   3124 O OD1 . ASN B 2 490 ? 137.828 156.079 207.186 1.00 106.59 ? 501 ASN B OD1 1 
ATOM   3125 N ND2 . ASN B 2 490 ? 137.420 157.140 205.254 1.00 106.59 ? 501 ASN B ND2 1 
ATOM   3126 N N   . GLY B 2 491 ? 141.157 153.434 205.071 1.00 104.66 ? 502 GLY B N   1 
ATOM   3127 C CA  . GLY B 2 491 ? 142.143 152.733 204.281 1.00 104.66 ? 502 GLY B CA  1 
ATOM   3128 C C   . GLY B 2 491 ? 142.620 153.564 203.108 1.00 104.66 ? 502 GLY B C   1 
ATOM   3129 O O   . GLY B 2 491 ? 142.007 154.554 202.710 1.00 104.66 ? 502 GLY B O   1 
ATOM   3130 N N   . VAL B 2 492 ? 143.749 153.139 202.538 1.00 104.66 ? 503 VAL B N   1 
ATOM   3131 C CA  . VAL B 2 492 ? 144.356 153.891 201.444 1.00 104.66 ? 503 VAL B CA  1 
ATOM   3132 C C   . VAL B 2 492 ? 143.438 153.930 200.234 1.00 104.66 ? 503 VAL B C   1 
ATOM   3133 O O   . VAL B 2 492 ? 143.522 154.848 199.412 1.00 104.66 ? 503 VAL B O   1 
ATOM   3134 C CB  . VAL B 2 492 ? 145.732 153.301 201.086 1.00 104.66 ? 503 VAL B CB  1 
ATOM   3135 C CG1 . VAL B 2 492 ? 146.692 153.465 202.251 1.00 104.66 ? 503 VAL B CG1 1 
ATOM   3136 C CG2 . VAL B 2 492 ? 145.598 151.839 200.699 1.00 104.66 ? 503 VAL B CG2 1 
ATOM   3137 N N   . GLY B 2 493 ? 142.556 152.946 200.097 1.00 104.66 ? 504 GLY B N   1 
ATOM   3138 C CA  . GLY B 2 493 ? 141.596 152.993 199.016 1.00 104.66 ? 504 GLY B CA  1 
ATOM   3139 C C   . GLY B 2 493 ? 140.467 153.973 199.216 1.00 104.66 ? 504 GLY B C   1 
ATOM   3140 O O   . GLY B 2 493 ? 139.747 154.268 198.260 1.00 104.66 ? 504 GLY B O   1 
ATOM   3141 N N   . TYR B 2 494 ? 140.300 154.490 200.433 1.00 104.66 ? 505 TYR B N   1 
ATOM   3142 C CA  . TYR B 2 494 ? 139.207 155.393 200.770 1.00 104.66 ? 505 TYR B CA  1 
ATOM   3143 C C   . TYR B 2 494 ? 139.722 156.736 201.273 1.00 104.66 ? 505 TYR B C   1 
ATOM   3144 O O   . TYR B 2 494 ? 139.090 157.372 202.116 1.00 104.66 ? 505 TYR B O   1 
ATOM   3145 C CB  . TYR B 2 494 ? 138.290 154.762 201.815 1.00 104.66 ? 505 TYR B CB  1 
ATOM   3146 C CG  . TYR B 2 494 ? 137.321 153.747 201.262 1.00 104.66 ? 505 TYR B CG  1 
ATOM   3147 C CD1 . TYR B 2 494 ? 137.406 153.325 199.948 1.00 104.66 ? 505 TYR B CD1 1 
ATOM   3148 C CD2 . TYR B 2 494 ? 136.322 153.212 202.056 1.00 104.66 ? 505 TYR B CD2 1 
ATOM   3149 C CE1 . TYR B 2 494 ? 136.530 152.399 199.439 1.00 104.66 ? 505 TYR B CE1 1 
ATOM   3150 C CE2 . TYR B 2 494 ? 135.437 152.288 201.553 1.00 104.66 ? 505 TYR B CE2 1 
ATOM   3151 C CZ  . TYR B 2 494 ? 135.546 151.886 200.243 1.00 104.66 ? 505 TYR B CZ  1 
ATOM   3152 O OH  . TYR B 2 494 ? 134.671 150.962 199.730 1.00 104.66 ? 505 TYR B OH  1 
ATOM   3153 N N   . GLN B 2 495 ? 140.856 157.167 200.783 1.00 104.66 ? 506 GLN B N   1 
ATOM   3154 C CA  . GLN B 2 495 ? 141.391 158.440 201.233 1.00 104.66 ? 506 GLN B CA  1 
ATOM   3155 C C   . GLN B 2 495 ? 141.242 159.498 200.147 1.00 104.66 ? 506 GLN B C   1 
ATOM   3156 O O   . GLN B 2 495 ? 141.258 159.179 198.956 1.00 104.66 ? 506 GLN B O   1 
ATOM   3157 C CB  . GLN B 2 495 ? 142.867 158.298 201.608 1.00 104.66 ? 506 GLN B CB  1 
ATOM   3158 C CG  . GLN B 2 495 ? 143.096 157.500 202.870 1.00 104.66 ? 506 GLN B CG  1 
ATOM   3159 C CD  . GLN B 2 495 ? 144.558 157.237 203.131 1.00 104.66 ? 506 GLN B CD  1 
ATOM   3160 O OE1 . GLN B 2 495 ? 145.427 157.913 202.587 1.00 104.66 ? 506 GLN B OE1 1 
ATOM   3161 N NE2 . GLN B 2 495 ? 144.840 156.243 203.962 1.00 104.66 ? 506 GLN B NE2 1 
ATOM   3162 N N   . PRO B 2 496 ? 141.083 160.764 200.528 1.00 104.66 ? 507 PRO B N   1 
ATOM   3163 C CA  . PRO B 2 496 ? 140.877 161.811 199.523 1.00 104.66 ? 507 PRO B CA  1 
ATOM   3164 C C   . PRO B 2 496 ? 142.077 161.966 198.606 1.00 104.66 ? 507 PRO B C   1 
ATOM   3165 O O   . PRO B 2 496 ? 143.227 161.892 199.039 1.00 104.66 ? 507 PRO B O   1 
ATOM   3166 C CB  . PRO B 2 496 ? 140.655 163.070 200.366 1.00 104.66 ? 507 PRO B CB  1 
ATOM   3167 C CG  . PRO B 2 496 ? 141.272 162.766 201.670 1.00 104.66 ? 507 PRO B CG  1 
ATOM   3168 C CD  . PRO B 2 496 ? 141.070 161.306 201.893 1.00 104.66 ? 507 PRO B CD  1 
ATOM   3169 N N   . TYR B 2 497 ? 141.793 162.192 197.328 1.00 104.66 ? 508 TYR B N   1 
ATOM   3170 C CA  . TYR B 2 497 ? 142.808 162.437 196.317 1.00 104.66 ? 508 TYR B CA  1 
ATOM   3171 C C   . TYR B 2 497 ? 142.443 163.691 195.545 1.00 104.66 ? 508 TYR B C   1 
ATOM   3172 O O   . TYR B 2 497 ? 141.276 163.898 195.209 1.00 104.66 ? 508 TYR B O   1 
ATOM   3173 C CB  . TYR B 2 497 ? 142.931 161.264 195.351 1.00 104.66 ? 508 TYR B CB  1 
ATOM   3174 C CG  . TYR B 2 497 ? 143.891 160.193 195.796 1.00 104.66 ? 508 TYR B CG  1 
ATOM   3175 C CD1 . TYR B 2 497 ? 143.702 159.521 196.988 1.00 104.66 ? 508 TYR B CD1 1 
ATOM   3176 C CD2 . TYR B 2 497 ? 144.977 159.840 195.014 1.00 104.66 ? 508 TYR B CD2 1 
ATOM   3177 C CE1 . TYR B 2 497 ? 144.569 158.537 197.395 1.00 104.66 ? 508 TYR B CE1 1 
ATOM   3178 C CE2 . TYR B 2 497 ? 145.851 158.856 195.415 1.00 104.66 ? 508 TYR B CE2 1 
ATOM   3179 C CZ  . TYR B 2 497 ? 145.641 158.210 196.608 1.00 104.66 ? 508 TYR B CZ  1 
ATOM   3180 O OH  . TYR B 2 497 ? 146.506 157.226 197.019 1.00 104.66 ? 508 TYR B OH  1 
ATOM   3181 N N   . ARG B 2 498 ? 143.438 164.519 195.257 1.00 104.66 ? 509 ARG B N   1 
ATOM   3182 C CA  . ARG B 2 498 ? 143.242 165.730 194.476 1.00 104.66 ? 509 ARG B CA  1 
ATOM   3183 C C   . ARG B 2 498 ? 143.646 165.472 193.032 1.00 104.66 ? 509 ARG B C   1 
ATOM   3184 O O   . ARG B 2 498 ? 144.676 164.850 192.772 1.00 104.66 ? 509 ARG B O   1 
ATOM   3185 C CB  . ARG B 2 498 ? 144.057 166.880 195.057 1.00 104.66 ? 509 ARG B CB  1 
ATOM   3186 C CG  . ARG B 2 498 ? 143.650 167.260 196.464 1.00 104.66 ? 509 ARG B CG  1 
ATOM   3187 C CD  . ARG B 2 498 ? 144.292 168.565 196.883 1.00 104.66 ? 509 ARG B CD  1 
ATOM   3188 N NE  . ARG B 2 498 ? 143.754 169.074 198.137 1.00 104.66 ? 509 ARG B NE  1 
ATOM   3189 C CZ  . ARG B 2 498 ? 143.976 170.296 198.599 1.00 104.66 ? 509 ARG B CZ  1 
ATOM   3190 N NH1 . ARG B 2 498 ? 144.701 171.169 197.922 1.00 104.66 ? 509 ARG B NH1 1 
ATOM   3191 N NH2 . ARG B 2 498 ? 143.452 170.653 199.767 1.00 104.66 ? 509 ARG B NH2 1 
ATOM   3192 N N   . VAL B 2 499 ? 142.827 165.937 192.095 1.00 104.66 ? 510 VAL B N   1 
ATOM   3193 C CA  . VAL B 2 499 ? 143.026 165.667 190.677 1.00 104.66 ? 510 VAL B CA  1 
ATOM   3194 C C   . VAL B 2 499 ? 142.973 166.976 189.907 1.00 104.66 ? 510 VAL B C   1 
ATOM   3195 O O   . VAL B 2 499 ? 142.145 167.843 190.201 1.00 104.66 ? 510 VAL B O   1 
ATOM   3196 C CB  . VAL B 2 499 ? 141.970 164.686 190.137 1.00 104.66 ? 510 VAL B CB  1 
ATOM   3197 C CG1 . VAL B 2 499 ? 142.154 164.475 188.656 1.00 104.66 ? 510 VAL B CG1 1 
ATOM   3198 C CG2 . VAL B 2 499 ? 142.058 163.371 190.867 1.00 104.66 ? 510 VAL B CG2 1 
ATOM   3199 N N   . VAL B 2 500 ? 143.867 167.127 188.932 1.00 104.66 ? 511 VAL B N   1 
ATOM   3200 C CA  . VAL B 2 500 ? 143.868 168.270 188.028 1.00 104.66 ? 511 VAL B CA  1 
ATOM   3201 C C   . VAL B 2 500 ? 144.021 167.757 186.605 1.00 104.66 ? 511 VAL B C   1 
ATOM   3202 O O   . VAL B 2 500 ? 144.998 167.071 186.293 1.00 104.66 ? 511 VAL B O   1 
ATOM   3203 C CB  . VAL B 2 500 ? 144.991 169.267 188.361 1.00 104.66 ? 511 VAL B CB  1 
ATOM   3204 C CG1 . VAL B 2 500 ? 145.088 170.308 187.283 1.00 104.66 ? 511 VAL B CG1 1 
ATOM   3205 C CG2 . VAL B 2 500 ? 144.729 169.924 189.691 1.00 104.66 ? 511 VAL B CG2 1 
ATOM   3206 N N   . VAL B 2 501 ? 143.070 168.098 185.743 1.00 104.66 ? 512 VAL B N   1 
ATOM   3207 C CA  . VAL B 2 501 ? 143.050 167.638 184.360 1.00 104.66 ? 512 VAL B CA  1 
ATOM   3208 C C   . VAL B 2 501 ? 143.393 168.810 183.459 1.00 104.66 ? 512 VAL B C   1 
ATOM   3209 O O   . VAL B 2 501 ? 142.736 169.854 183.517 1.00 104.66 ? 512 VAL B O   1 
ATOM   3210 C CB  . VAL B 2 501 ? 141.681 167.056 183.978 1.00 104.66 ? 512 VAL B CB  1 
ATOM   3211 C CG1 . VAL B 2 501 ? 141.652 166.737 182.510 1.00 104.66 ? 512 VAL B CG1 1 
ATOM   3212 C CG2 . VAL B 2 501 ? 141.386 165.822 184.787 1.00 104.66 ? 512 VAL B CG2 1 
ATOM   3213 N N   . LEU B 2 502 ? 144.407 168.636 182.621 1.00 104.66 ? 513 LEU B N   1 
ATOM   3214 C CA  . LEU B 2 502 ? 144.824 169.664 181.679 1.00 104.66 ? 513 LEU B CA  1 
ATOM   3215 C C   . LEU B 2 502 ? 144.347 169.291 180.285 1.00 104.66 ? 513 LEU B C   1 
ATOM   3216 O O   . LEU B 2 502 ? 144.592 168.177 179.820 1.00 104.66 ? 513 LEU B O   1 
ATOM   3217 C CB  . LEU B 2 502 ? 146.342 169.830 181.689 1.00 104.66 ? 513 LEU B CB  1 
ATOM   3218 C CG  . LEU B 2 502 ? 146.958 170.394 182.963 1.00 104.66 ? 513 LEU B CG  1 
ATOM   3219 C CD1 . LEU B 2 502 ? 148.458 170.278 182.909 1.00 104.66 ? 513 LEU B CD1 1 
ATOM   3220 C CD2 . LEU B 2 502 ? 146.553 171.830 183.139 1.00 104.66 ? 513 LEU B CD2 1 
ATOM   3221 N N   . SER B 2 503 ? 143.667 170.220 179.624 1.00 104.66 ? 514 SER B N   1 
ATOM   3222 C CA  . SER B 2 503 ? 143.145 170.000 178.284 1.00 104.66 ? 514 SER B CA  1 
ATOM   3223 C C   . SER B 2 503 ? 143.824 170.965 177.330 1.00 104.66 ? 514 SER B C   1 
ATOM   3224 O O   . SER B 2 503 ? 143.797 172.178 177.552 1.00 104.66 ? 514 SER B O   1 
ATOM   3225 C CB  . SER B 2 503 ? 141.633 170.198 178.244 1.00 104.66 ? 514 SER B CB  1 
ATOM   3226 O OG  . SER B 2 503 ? 140.993 169.344 179.167 1.00 104.66 ? 514 SER B OG  1 
ATOM   3227 N N   . PHE B 2 504 ? 144.423 170.431 176.275 1.00 104.66 ? 515 PHE B N   1 
ATOM   3228 C CA  . PHE B 2 504 ? 145.040 171.235 175.234 1.00 104.66 ? 515 PHE B CA  1 
ATOM   3229 C C   . PHE B 2 504 ? 144.171 171.190 173.991 1.00 104.66 ? 515 PHE B C   1 
ATOM   3230 O O   . PHE B 2 504 ? 143.512 170.184 173.723 1.00 104.66 ? 515 PHE B O   1 
ATOM   3231 C CB  . PHE B 2 504 ? 146.438 170.731 174.883 1.00 104.66 ? 515 PHE B CB  1 
ATOM   3232 C CG  . PHE B 2 504 ? 147.289 170.413 176.068 1.00 104.66 ? 515 PHE B CG  1 
ATOM   3233 C CD1 . PHE B 2 504 ? 147.299 171.232 177.171 1.00 104.66 ? 515 PHE B CD1 1 
ATOM   3234 C CD2 . PHE B 2 504 ? 148.095 169.300 176.068 1.00 104.66 ? 515 PHE B CD2 1 
ATOM   3235 C CE1 . PHE B 2 504 ? 148.087 170.936 178.251 1.00 104.66 ? 515 PHE B CE1 1 
ATOM   3236 C CE2 . PHE B 2 504 ? 148.880 169.004 177.146 1.00 104.66 ? 515 PHE B CE2 1 
ATOM   3237 C CZ  . PHE B 2 504 ? 148.877 169.822 178.238 1.00 104.66 ? 515 PHE B CZ  1 
ATOM   3238 N N   . GLU B 2 505 ? 144.161 172.282 173.240 1.00 104.66 ? 516 GLU B N   1 
ATOM   3239 C CA  . GLU B 2 505 ? 143.501 172.325 171.946 1.00 104.66 ? 516 GLU B CA  1 
ATOM   3240 C C   . GLU B 2 505 ? 144.517 172.694 170.877 1.00 104.66 ? 516 GLU B C   1 
ATOM   3241 O O   . GLU B 2 505 ? 145.150 173.752 170.951 1.00 104.66 ? 516 GLU B O   1 
ATOM   3242 C CB  . GLU B 2 505 ? 142.326 173.304 171.958 1.00 104.66 ? 516 GLU B CB  1 
ATOM   3243 C CG  . GLU B 2 505 ? 142.663 174.725 172.355 1.00 104.66 ? 516 GLU B CG  1 
ATOM   3244 C CD  . GLU B 2 505 ? 141.472 175.449 172.944 1.00 104.66 ? 516 GLU B CD  1 
ATOM   3245 O OE1 . GLU B 2 505 ? 140.329 175.121 172.562 1.00 104.66 ? 516 GLU B OE1 1 
ATOM   3246 O OE2 . GLU B 2 505 ? 141.674 176.343 173.789 1.00 104.66 ? 516 GLU B OE2 1 
ATOM   3247 N N   . LEU B 2 506 ? 144.676 171.818 169.894 1.00 104.66 ? 517 LEU B N   1 
ATOM   3248 C CA  . LEU B 2 506 ? 145.654 172.028 168.838 1.00 104.66 ? 517 LEU B CA  1 
ATOM   3249 C C   . LEU B 2 506 ? 144.973 172.235 167.491 1.00 104.66 ? 517 LEU B C   1 
ATOM   3250 O O   . LEU B 2 506 ? 143.822 172.668 167.428 1.00 104.66 ? 517 LEU B O   1 
ATOM   3251 C CB  . LEU B 2 506 ? 146.620 170.844 168.767 1.00 104.66 ? 517 LEU B CB  1 
ATOM   3252 C CG  . LEU B 2 506 ? 147.605 170.701 169.928 1.00 104.66 ? 517 LEU B CG  1 
ATOM   3253 C CD1 . LEU B 2 506 ? 148.355 169.388 169.847 1.00 104.66 ? 517 LEU B CD1 1 
ATOM   3254 C CD2 . LEU B 2 506 ? 148.580 171.858 169.931 1.00 104.66 ? 517 LEU B CD2 1 
ATOM   3255 N N   . ALA B 2 509 ? 144.683 179.358 164.430 1.00 123.20 ? 520 ALA B N   1 
ATOM   3256 C CA  . ALA B 2 509 ? 144.508 180.348 165.485 1.00 123.20 ? 520 ALA B CA  1 
ATOM   3257 C C   . ALA B 2 509 ? 145.853 180.742 166.083 1.00 123.20 ? 520 ALA B C   1 
ATOM   3258 O O   . ALA B 2 509 ? 146.760 179.915 166.172 1.00 123.20 ? 520 ALA B O   1 
ATOM   3259 C CB  . ALA B 2 509 ? 143.580 179.815 166.564 1.00 123.20 ? 520 ALA B CB  1 
ATOM   3260 N N   . PRO B 2 510 ? 145.987 182.008 166.484 1.00 125.25 ? 521 PRO B N   1 
ATOM   3261 C CA  . PRO B 2 510 ? 147.245 182.456 167.097 1.00 125.25 ? 521 PRO B CA  1 
ATOM   3262 C C   . PRO B 2 510 ? 147.506 181.789 168.436 1.00 125.25 ? 521 PRO B C   1 
ATOM   3263 O O   . PRO B 2 510 ? 146.808 182.057 169.418 1.00 125.25 ? 521 PRO B O   1 
ATOM   3264 C CB  . PRO B 2 510 ? 147.041 183.969 167.258 1.00 125.25 ? 521 PRO B CB  1 
ATOM   3265 C CG  . PRO B 2 510 ? 145.936 184.318 166.318 1.00 125.25 ? 521 PRO B CG  1 
ATOM   3266 C CD  . PRO B 2 510 ? 145.044 183.120 166.283 1.00 125.25 ? 521 PRO B CD  1 
ATOM   3267 N N   . ALA B 2 511 ? 148.511 180.922 168.486 1.00 113.44 ? 522 ALA B N   1 
ATOM   3268 C CA  . ALA B 2 511 ? 148.878 180.284 169.740 1.00 113.44 ? 522 ALA B CA  1 
ATOM   3269 C C   . ALA B 2 511 ? 149.399 181.323 170.720 1.00 113.44 ? 522 ALA B C   1 
ATOM   3270 O O   . ALA B 2 511 ? 150.095 182.266 170.337 1.00 113.44 ? 522 ALA B O   1 
ATOM   3271 C CB  . ALA B 2 511 ? 149.934 179.207 169.503 1.00 113.44 ? 522 ALA B CB  1 
ATOM   3272 N N   . THR B 2 512 ? 149.059 181.153 171.990 1.00 105.37 ? 523 THR B N   1 
ATOM   3273 C CA  . THR B 2 512 ? 149.459 182.111 173.005 1.00 105.37 ? 523 THR B CA  1 
ATOM   3274 C C   . THR B 2 512 ? 150.296 181.519 174.127 1.00 105.37 ? 523 THR B C   1 
ATOM   3275 O O   . THR B 2 512 ? 151.132 182.232 174.683 1.00 105.37 ? 523 THR B O   1 
ATOM   3276 C CB  . THR B 2 512 ? 148.227 182.804 173.609 1.00 105.37 ? 523 THR B CB  1 
ATOM   3277 O OG1 . THR B 2 512 ? 148.648 183.859 174.480 1.00 105.37 ? 523 THR B OG1 1 
ATOM   3278 C CG2 . THR B 2 512 ? 147.379 181.827 174.387 1.00 105.37 ? 523 THR B CG2 1 
ATOM   3279 N N   . VAL B 2 513 ? 150.106 180.251 174.477 1.00 104.66 ? 524 VAL B N   1 
ATOM   3280 C CA  . VAL B 2 513 ? 150.815 179.632 175.592 1.00 104.66 ? 524 VAL B CA  1 
ATOM   3281 C C   . VAL B 2 513 ? 151.724 178.537 175.057 1.00 104.66 ? 524 VAL B C   1 
ATOM   3282 O O   . VAL B 2 513 ? 151.258 177.596 174.404 1.00 104.66 ? 524 VAL B O   1 
ATOM   3283 C CB  . VAL B 2 513 ? 149.842 179.085 176.647 1.00 104.66 ? 524 VAL B CB  1 
ATOM   3284 C CG1 . VAL B 2 513 ? 148.840 178.143 176.025 1.00 104.66 ? 524 VAL B CG1 1 
ATOM   3285 C CG2 . VAL B 2 513 ? 150.610 178.370 177.729 1.00 104.66 ? 524 VAL B CG2 1 
ATOM   3286 N N   . CYS B 2 514 ? 153.023 178.668 175.322 1.00 104.66 ? 525 CYS B N   1 
ATOM   3287 C CA  . CYS B 2 514 ? 153.973 177.592 175.067 1.00 104.66 ? 525 CYS B CA  1 
ATOM   3288 C C   . CYS B 2 514 ? 155.326 177.927 175.663 1.00 104.66 ? 525 CYS B C   1 
ATOM   3289 O O   . CYS B 2 514 ? 155.749 179.086 175.670 1.00 104.66 ? 525 CYS B O   1 
ATOM   3290 C CB  . CYS B 2 514 ? 154.114 177.286 173.579 1.00 104.66 ? 525 CYS B CB  1 
ATOM   3291 S SG  . CYS B 2 514 ? 154.436 178.605 172.414 1.00 104.66 ? 525 CYS B SG  1 
ATOM   3292 N N   . GLY B 2 515 ? 156.013 176.878 176.124 1.00 104.66 ? 526 GLY B N   1 
ATOM   3293 C CA  . GLY B 2 515 ? 157.195 177.030 176.920 1.00 104.66 ? 526 GLY B CA  1 
ATOM   3294 C C   . GLY B 2 515 ? 158.382 177.492 176.106 1.00 104.66 ? 526 GLY B C   1 
ATOM   3295 O O   . GLY B 2 515 ? 158.284 177.748 174.901 1.00 104.66 ? 526 GLY B O   1 
ATOM   3296 N N   . PRO B 2 516 ? 159.534 177.607 176.773 1.00 104.66 ? 527 PRO B N   1 
ATOM   3297 C CA  . PRO B 2 516 ? 160.760 178.148 176.189 1.00 104.66 ? 527 PRO B CA  1 
ATOM   3298 C C   . PRO B 2 516 ? 161.493 177.143 175.311 1.00 104.66 ? 527 PRO B C   1 
ATOM   3299 O O   . PRO B 2 516 ? 162.166 177.561 174.370 1.00 104.66 ? 527 PRO B O   1 
ATOM   3300 C CB  . PRO B 2 516 ? 161.590 178.505 177.417 1.00 104.66 ? 527 PRO B CB  1 
ATOM   3301 C CG  . PRO B 2 516 ? 161.167 177.518 178.435 1.00 104.66 ? 527 PRO B CG  1 
ATOM   3302 C CD  . PRO B 2 516 ? 159.732 177.176 178.164 1.00 104.66 ? 527 PRO B CD  1 
HETATM 3303 C C1  . NAG C 3 .   ? 153.600 174.600 195.279 1.00 130.50 ? 1   NAG C C1  1 
HETATM 3304 C C2  . NAG C 3 .   ? 154.605 175.250 194.332 1.00 130.50 ? 1   NAG C C2  1 
HETATM 3305 C C3  . NAG C 3 .   ? 155.885 174.416 194.247 1.00 130.50 ? 1   NAG C C3  1 
HETATM 3306 C C4  . NAG C 3 .   ? 156.417 174.047 195.627 1.00 130.50 ? 1   NAG C C4  1 
HETATM 3307 C C5  . NAG C 3 .   ? 155.301 173.498 196.514 1.00 130.50 ? 1   NAG C C5  1 
HETATM 3308 C C6  . NAG C 3 .   ? 155.722 173.307 197.952 1.00 130.50 ? 1   NAG C C6  1 
HETATM 3309 C C7  . NAG C 3 .   ? 153.647 174.451 192.198 1.00 130.50 ? 1   NAG C C7  1 
HETATM 3310 C C8  . NAG C 3 .   ? 153.094 174.866 190.871 1.00 130.50 ? 1   NAG C C8  1 
HETATM 3311 N N2  . NAG C 3 .   ? 154.034 175.447 193.007 1.00 130.50 ? 1   NAG C N2  1 
HETATM 3312 O O3  . NAG C 3 .   ? 156.873 175.150 193.534 1.00 130.50 ? 1   NAG C O3  1 
HETATM 3313 O O4  . NAG C 3 .   ? 157.395 173.027 195.448 1.00 130.50 ? 1   NAG C O4  1 
HETATM 3314 O O5  . NAG C 3 .   ? 154.195 174.410 196.538 1.00 130.50 ? 1   NAG C O5  1 
HETATM 3315 O O6  . NAG C 3 .   ? 156.533 174.386 198.397 1.00 130.50 ? 1   NAG C O6  1 
HETATM 3316 O O7  . NAG C 3 .   ? 153.733 173.270 192.522 1.00 130.50 ? 1   NAG C O7  1 
HETATM 3317 C C1  . NAG C 3 .   ? 158.638 173.261 196.148 1.00 141.23 ? 2   NAG C C1  1 
HETATM 3318 C C2  . NAG C 3 .   ? 159.477 171.996 195.987 1.00 141.23 ? 2   NAG C C2  1 
HETATM 3319 C C3  . NAG C 3 .   ? 160.809 172.157 196.708 1.00 141.23 ? 2   NAG C C3  1 
HETATM 3320 C C4  . NAG C 3 .   ? 161.521 173.411 196.219 1.00 141.23 ? 2   NAG C C4  1 
HETATM 3321 C C5  . NAG C 3 .   ? 160.605 174.626 196.345 1.00 141.23 ? 2   NAG C C5  1 
HETATM 3322 C C6  . NAG C 3 .   ? 161.206 175.880 195.756 1.00 141.23 ? 2   NAG C C6  1 
HETATM 3323 C C7  . NAG C 3 .   ? 158.006 170.057 195.688 1.00 141.23 ? 2   NAG C C7  1 
HETATM 3324 C C8  . NAG C 3 .   ? 157.342 168.889 196.354 1.00 141.23 ? 2   NAG C C8  1 
HETATM 3325 N N2  . NAG C 3 .   ? 158.766 170.826 196.475 1.00 141.23 ? 2   NAG C N2  1 
HETATM 3326 O O3  . NAG C 3 .   ? 161.619 171.011 196.472 1.00 141.23 ? 2   NAG C O3  1 
HETATM 3327 O O4  . NAG C 3 .   ? 162.701 173.629 196.984 1.00 141.23 ? 2   NAG C O4  1 
HETATM 3328 O O5  . NAG C 3 .   ? 159.370 174.391 195.649 1.00 141.23 ? 2   NAG C O5  1 
HETATM 3329 O O6  . NAG C 3 .   ? 160.567 177.046 196.258 1.00 141.23 ? 2   NAG C O6  1 
HETATM 3330 O O7  . NAG C 3 .   ? 157.857 170.296 194.493 1.00 141.23 ? 2   NAG C O7  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A N   
2    C CA  . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A CA  
3    C C   . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A C   
4    O O   . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A O   
5    C CB  . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A CB  
6    C CG1 . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A CG1 
7    C CG2 . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A CG2 
8    C CD1 . ILE A 2   ? 1.5156 1.5156 1.5156 0.0000 0.0000 0.0000 1   ILE A CD1 
9    N N   . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A N   
10   C CA  . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A CA  
11   C C   . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A C   
12   O O   . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A O   
13   C CB  . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A CB  
14   C CG1 . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A CG1 
15   C CG2 . VAL A 3   ? 1.5378 1.5378 1.5378 0.0000 0.0000 0.0000 2   VAL A CG2 
16   N N   . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A N   
17   C CA  . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A CA  
18   C C   . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A C   
19   O O   . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A O   
20   C CB  . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A CB  
21   C CG  . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A CG  
22   C CD1 . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A CD1 
23   C CD2 . LEU A 4   ? 1.5308 1.5308 1.5308 0.0000 0.0000 0.0000 3   LEU A CD2 
24   N N   . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A N   
25   C CA  . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A CA  
26   C C   . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A C   
27   O O   . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A O   
28   C CB  . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A CB  
29   O OG1 . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A OG1 
30   C CG2 . THR A 5   ? 1.6157 1.6157 1.6157 0.0000 0.0000 0.0000 4   THR A CG2 
31   N N   . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A N   
32   C CA  . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A CA  
33   C C   . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A C   
34   O O   . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A O   
35   C CB  . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A CB  
36   C CG  . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A CG  
37   C CD  . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A CD  
38   O OE1 . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A OE1 
39   N NE2 . GLN A 6   ? 1.6364 1.6364 1.6364 0.0000 0.0000 0.0000 5   GLN A NE2 
40   N N   . SER A 7   ? 1.7160 1.7160 1.7160 0.0000 0.0000 0.0000 6   SER A N   
41   C CA  . SER A 7   ? 1.7160 1.7160 1.7160 0.0000 0.0000 0.0000 6   SER A CA  
42   C C   . SER A 7   ? 1.7160 1.7160 1.7160 0.0000 0.0000 0.0000 6   SER A C   
43   O O   . SER A 7   ? 1.7160 1.7160 1.7160 0.0000 0.0000 0.0000 6   SER A O   
44   C CB  . SER A 7   ? 1.7160 1.7160 1.7160 0.0000 0.0000 0.0000 6   SER A CB  
45   O OG  . SER A 7   ? 1.7160 1.7160 1.7160 0.0000 0.0000 0.0000 6   SER A OG  
46   N N   . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A N   
47   C CA  . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A CA  
48   C C   . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A C   
49   O O   . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A O   
50   C CB  . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A CB  
51   C CG  . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A CG  
52   C CD  . PRO A 8   ? 1.6977 1.6977 1.6977 0.0000 0.0000 0.0000 7   PRO A CD  
53   N N   . GLY A 9   ? 1.7663 1.7663 1.7663 0.0000 0.0000 0.0000 8   GLY A N   
54   C CA  . GLY A 9   ? 1.7663 1.7663 1.7663 0.0000 0.0000 0.0000 8   GLY A CA  
55   C C   . GLY A 9   ? 1.7663 1.7663 1.7663 0.0000 0.0000 0.0000 8   GLY A C   
56   O O   . GLY A 9   ? 1.7663 1.7663 1.7663 0.0000 0.0000 0.0000 8   GLY A O   
57   N N   . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A N   
58   C CA  . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A CA  
59   C C   . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A C   
60   O O   . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A O   
61   C CB  . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A CB  
62   O OG1 . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A OG1 
63   C CG2 . THR A 10  ? 1.8039 1.8039 1.8039 0.0000 0.0000 0.0000 9   THR A CG2 
64   N N   . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A N   
65   C CA  . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A CA  
66   C C   . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A C   
67   O O   . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A O   
68   C CB  . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A CB  
69   C CG  . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A CG  
70   C CD1 . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A CD1 
71   C CD2 . LEU A 11  ? 1.8742 1.8742 1.8742 0.0000 0.0000 0.0000 10  LEU A CD2 
72   N N   . SER A 12  ? 1.9998 1.9998 1.9998 0.0000 0.0000 0.0000 11  SER A N   
73   C CA  . SER A 12  ? 1.9998 1.9998 1.9998 0.0000 0.0000 0.0000 11  SER A CA  
74   C C   . SER A 12  ? 1.9998 1.9998 1.9998 0.0000 0.0000 0.0000 11  SER A C   
75   O O   . SER A 12  ? 1.9998 1.9998 1.9998 0.0000 0.0000 0.0000 11  SER A O   
76   C CB  . SER A 12  ? 1.9998 1.9998 1.9998 0.0000 0.0000 0.0000 11  SER A CB  
77   O OG  . SER A 12  ? 1.9998 1.9998 1.9998 0.0000 0.0000 0.0000 11  SER A OG  
78   N N   . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A N   
79   C CA  . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A CA  
80   C C   . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A C   
81   O O   . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A O   
82   C CB  . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A CB  
83   C CG  . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A CG  
84   C CD1 . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A CD1 
85   C CD2 . LEU A 13  ? 2.0276 2.0276 2.0276 0.0000 0.0000 0.0000 12  LEU A CD2 
86   N N   . SER A 14  ? 2.0704 2.0704 2.0704 0.0000 0.0000 0.0000 13  SER A N   
87   C CA  . SER A 14  ? 2.0704 2.0704 2.0704 0.0000 0.0000 0.0000 13  SER A CA  
88   C C   . SER A 14  ? 2.0704 2.0704 2.0704 0.0000 0.0000 0.0000 13  SER A C   
89   O O   . SER A 14  ? 2.0704 2.0704 2.0704 0.0000 0.0000 0.0000 13  SER A O   
90   C CB  . SER A 14  ? 2.0704 2.0704 2.0704 0.0000 0.0000 0.0000 13  SER A CB  
91   O OG  . SER A 14  ? 2.0704 2.0704 2.0704 0.0000 0.0000 0.0000 13  SER A OG  
92   N N   . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A N   
93   C CA  . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A CA  
94   C C   . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A C   
95   O O   . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A O   
96   C CB  . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A CB  
97   C CG  . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A CG  
98   C CD  . PRO A 15  ? 2.0376 2.0376 2.0376 0.0000 0.0000 0.0000 14  PRO A CD  
99   N N   . GLY A 16  ? 2.0125 2.0125 2.0125 0.0000 0.0000 0.0000 15  GLY A N   
100  C CA  . GLY A 16  ? 2.0125 2.0125 2.0125 0.0000 0.0000 0.0000 15  GLY A CA  
101  C C   . GLY A 16  ? 2.0125 2.0125 2.0125 0.0000 0.0000 0.0000 15  GLY A C   
102  O O   . GLY A 16  ? 2.0125 2.0125 2.0125 0.0000 0.0000 0.0000 15  GLY A O   
103  N N   . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A N   
104  C CA  . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A CA  
105  C C   . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A C   
106  O O   . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A O   
107  C CB  . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A CB  
108  C CG  . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A CG  
109  C CD  . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A CD  
110  O OE1 . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A OE1 
111  O OE2 . GLU A 17  ? 1.9947 1.9947 1.9947 0.0000 0.0000 0.0000 16  GLU A OE2 
112  N N   . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A N   
113  C CA  . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A CA  
114  C C   . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A C   
115  O O   . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A O   
116  C CB  . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A CB  
117  C CG  . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A CG  
118  C CD  . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A CD  
119  N NE  . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A NE  
120  C CZ  . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A CZ  
121  N NH1 . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A NH1 
122  N NH2 . ARG A 18  ? 1.8695 1.8695 1.8695 0.0000 0.0000 0.0000 17  ARG A NH2 
123  N N   . ALA A 19  ? 1.7539 1.7539 1.7539 0.0000 0.0000 0.0000 18  ALA A N   
124  C CA  . ALA A 19  ? 1.7539 1.7539 1.7539 0.0000 0.0000 0.0000 18  ALA A CA  
125  C C   . ALA A 19  ? 1.7539 1.7539 1.7539 0.0000 0.0000 0.0000 18  ALA A C   
126  O O   . ALA A 19  ? 1.7539 1.7539 1.7539 0.0000 0.0000 0.0000 18  ALA A O   
127  C CB  . ALA A 19  ? 1.7539 1.7539 1.7539 0.0000 0.0000 0.0000 18  ALA A CB  
128  N N   . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A N   
129  C CA  . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A CA  
130  C C   . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A C   
131  O O   . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A O   
132  C CB  . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A CB  
133  O OG1 . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A OG1 
134  C CG2 . THR A 20  ? 1.6769 1.6769 1.6769 0.0000 0.0000 0.0000 19  THR A CG2 
135  N N   . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A N   
136  C CA  . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A CA  
137  C C   . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A C   
138  O O   . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A O   
139  C CB  . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A CB  
140  C CG  . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A CG  
141  C CD1 . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A CD1 
142  C CD2 . LEU A 21  ? 1.5860 1.5860 1.5860 0.0000 0.0000 0.0000 20  LEU A CD2 
143  N N   . SER A 22  ? 1.5938 1.5938 1.5938 0.0000 0.0000 0.0000 21  SER A N   
144  C CA  . SER A 22  ? 1.5938 1.5938 1.5938 0.0000 0.0000 0.0000 21  SER A CA  
145  C C   . SER A 22  ? 1.5938 1.5938 1.5938 0.0000 0.0000 0.0000 21  SER A C   
146  O O   . SER A 22  ? 1.5938 1.5938 1.5938 0.0000 0.0000 0.0000 21  SER A O   
147  C CB  . SER A 22  ? 1.5938 1.5938 1.5938 0.0000 0.0000 0.0000 21  SER A CB  
148  O OG  . SER A 22  ? 1.5938 1.5938 1.5938 0.0000 0.0000 0.0000 21  SER A OG  
149  N N   . CYS A 23  ? 1.6287 1.6287 1.6287 0.0000 0.0000 0.0000 22  CYS A N   
150  C CA  . CYS A 23  ? 1.6287 1.6287 1.6287 0.0000 0.0000 0.0000 22  CYS A CA  
151  C C   . CYS A 23  ? 1.6287 1.6287 1.6287 0.0000 0.0000 0.0000 22  CYS A C   
152  O O   . CYS A 23  ? 1.6287 1.6287 1.6287 0.0000 0.0000 0.0000 22  CYS A O   
153  C CB  . CYS A 23  ? 1.6287 1.6287 1.6287 0.0000 0.0000 0.0000 22  CYS A CB  
154  S SG  . CYS A 23  ? 1.6287 1.6287 1.6287 0.0000 0.0000 0.0000 22  CYS A SG  
155  N N   . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A N   
156  C CA  . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A CA  
157  C C   . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A C   
158  O O   . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A O   
159  C CB  . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A CB  
160  C CG  . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A CG  
161  C CD  . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A CD  
162  N NE  . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A NE  
163  C CZ  . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A CZ  
164  N NH1 . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A NH1 
165  N NH2 . ARG A 24  ? 1.6468 1.6468 1.6468 0.0000 0.0000 0.0000 23  ARG A NH2 
166  N N   . ALA A 25  ? 1.6294 1.6294 1.6294 0.0000 0.0000 0.0000 24  ALA A N   
167  C CA  . ALA A 25  ? 1.6294 1.6294 1.6294 0.0000 0.0000 0.0000 24  ALA A CA  
168  C C   . ALA A 25  ? 1.6294 1.6294 1.6294 0.0000 0.0000 0.0000 24  ALA A C   
169  O O   . ALA A 25  ? 1.6294 1.6294 1.6294 0.0000 0.0000 0.0000 24  ALA A O   
170  C CB  . ALA A 25  ? 1.6294 1.6294 1.6294 0.0000 0.0000 0.0000 24  ALA A CB  
171  N N   . SER A 26  ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 25  SER A N   
172  C CA  . SER A 26  ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 25  SER A CA  
173  C C   . SER A 26  ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 25  SER A C   
174  O O   . SER A 26  ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 25  SER A O   
175  C CB  . SER A 26  ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 25  SER A CB  
176  O OG  . SER A 26  ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 25  SER A OG  
177  N N   . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A N   
178  C CA  . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A CA  
179  C C   . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A C   
180  O O   . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A O   
181  C CB  . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A CB  
182  C CG  . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A CG  
183  C CD  . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A CD  
184  O OE1 . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A OE1 
185  N NE2 . GLN A 27  ? 1.6614 1.6614 1.6614 0.0000 0.0000 0.0000 26  GLN A NE2 
186  N N   . SER A 28  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 27  SER A N   
187  C CA  . SER A 28  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 27  SER A CA  
188  C C   . SER A 28  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 27  SER A C   
189  O O   . SER A 28  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 27  SER A O   
190  C CB  . SER A 28  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 27  SER A CB  
191  O OG  . SER A 28  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 27  SER A OG  
192  N N   . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A N   
193  C CA  . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A CA  
194  C C   . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A C   
195  O O   . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A O   
196  C CB  . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A CB  
197  C CG1 . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A CG1 
198  C CG2 . VAL A 29  ? 1.5132 1.5132 1.5132 0.0000 0.0000 0.0000 28  VAL A CG2 
199  N N   . SER A 30  ? 1.4783 1.4783 1.4783 0.0000 0.0000 0.0000 29  SER A N   
200  C CA  . SER A 30  ? 1.4783 1.4783 1.4783 0.0000 0.0000 0.0000 29  SER A CA  
201  C C   . SER A 30  ? 1.4783 1.4783 1.4783 0.0000 0.0000 0.0000 29  SER A C   
202  O O   . SER A 30  ? 1.4783 1.4783 1.4783 0.0000 0.0000 0.0000 29  SER A O   
203  C CB  . SER A 30  ? 1.4783 1.4783 1.4783 0.0000 0.0000 0.0000 29  SER A CB  
204  O OG  . SER A 30  ? 1.4783 1.4783 1.4783 0.0000 0.0000 0.0000 29  SER A OG  
205  N N   . SER A 31  ? 1.4158 1.4158 1.4158 0.0000 0.0000 0.0000 30  SER A N   
206  C CA  . SER A 31  ? 1.4158 1.4158 1.4158 0.0000 0.0000 0.0000 30  SER A CA  
207  C C   . SER A 31  ? 1.4158 1.4158 1.4158 0.0000 0.0000 0.0000 30  SER A C   
208  O O   . SER A 31  ? 1.4158 1.4158 1.4158 0.0000 0.0000 0.0000 30  SER A O   
209  C CB  . SER A 31  ? 1.4158 1.4158 1.4158 0.0000 0.0000 0.0000 30  SER A CB  
210  O OG  . SER A 31  ? 1.4158 1.4158 1.4158 0.0000 0.0000 0.0000 30  SER A OG  
211  N N   . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A N   
212  C CA  . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A CA  
213  C C   . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A C   
214  O O   . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A O   
215  C CB  . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A CB  
216  O OG1 . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A OG1 
217  C CG2 . THR A 32  ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 31  THR A CG2 
218  N N   . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A N   
219  C CA  . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CA  
220  C C   . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A C   
221  O O   . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A O   
222  C CB  . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CB  
223  C CG  . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CG  
224  C CD1 . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CD1 
225  C CD2 . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CD2 
226  C CE1 . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CE1 
227  C CE2 . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CE2 
228  C CZ  . PHE A 33  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 32  PHE A CZ  
229  N N   . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A N   
230  C CA  . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A CA  
231  C C   . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A C   
232  O O   . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A O   
233  C CB  . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A CB  
234  C CG  . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A CG  
235  C CD1 . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A CD1 
236  C CD2 . LEU A 34  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 33  LEU A CD2 
237  N N   . ALA A 35  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 34  ALA A N   
238  C CA  . ALA A 35  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 34  ALA A CA  
239  C C   . ALA A 35  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 34  ALA A C   
240  O O   . ALA A 35  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 34  ALA A O   
241  C CB  . ALA A 35  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 34  ALA A CB  
242  N N   . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A N   
243  C CA  . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CA  
244  C C   . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A C   
245  O O   . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A O   
246  C CB  . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CB  
247  C CG  . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CG  
248  C CD1 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CD1 
249  C CD2 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CD2 
250  N NE1 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A NE1 
251  C CE2 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CE2 
252  C CE3 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CE3 
253  C CZ2 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CZ2 
254  C CZ3 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CZ3 
255  C CH2 . TRP A 36  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 35  TRP A CH2 
256  N N   . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A N   
257  C CA  . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CA  
258  C C   . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A C   
259  O O   . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A O   
260  C CB  . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CB  
261  C CG  . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CG  
262  C CD1 . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CD1 
263  C CD2 . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CD2 
264  C CE1 . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CE1 
265  C CE2 . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CE2 
266  C CZ  . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A CZ  
267  O OH  . TYR A 37  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 36  TYR A OH  
268  N N   . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A N   
269  C CA  . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A CA  
270  C C   . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A C   
271  O O   . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A O   
272  C CB  . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A CB  
273  C CG  . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A CG  
274  C CD  . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A CD  
275  O OE1 . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A OE1 
276  N NE2 . GLN A 38  ? 1.4226 1.4226 1.4226 0.0000 0.0000 0.0000 37  GLN A NE2 
277  N N   . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A N   
278  C CA  . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A CA  
279  C C   . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A C   
280  O O   . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A O   
281  C CB  . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A CB  
282  C CG  . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A CG  
283  C CD  . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A CD  
284  O OE1 . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A OE1 
285  N NE2 . GLN A 39  ? 1.5134 1.5134 1.5134 0.0000 0.0000 0.0000 38  GLN A NE2 
286  N N   . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A N   
287  C CA  . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A CA  
288  C C   . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A C   
289  O O   . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A O   
290  C CB  . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A CB  
291  C CG  . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A CG  
292  C CD  . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A CD  
293  C CE  . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A CE  
294  N NZ  . LYS A 40  ? 1.6613 1.6613 1.6613 0.0000 0.0000 0.0000 39  LYS A NZ  
295  N N   . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A N   
296  C CA  . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A CA  
297  C C   . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A C   
298  O O   . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A O   
299  C CB  . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A CB  
300  C CG  . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A CG  
301  C CD  . PRO A 41  ? 1.7630 1.7630 1.7630 0.0000 0.0000 0.0000 40  PRO A CD  
302  N N   . GLY A 42  ? 1.7899 1.7899 1.7899 0.0000 0.0000 0.0000 41  GLY A N   
303  C CA  . GLY A 42  ? 1.7899 1.7899 1.7899 0.0000 0.0000 0.0000 41  GLY A CA  
304  C C   . GLY A 42  ? 1.7899 1.7899 1.7899 0.0000 0.0000 0.0000 41  GLY A C   
305  O O   . GLY A 42  ? 1.7899 1.7899 1.7899 0.0000 0.0000 0.0000 41  GLY A O   
306  N N   . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A N   
307  C CA  . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A CA  
308  C C   . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A C   
309  O O   . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A O   
310  C CB  . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A CB  
311  C CG  . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A CG  
312  C CD  . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A CD  
313  O OE1 . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A OE1 
314  N NE2 . GLN A 43  ? 1.7076 1.7076 1.7076 0.0000 0.0000 0.0000 42  GLN A NE2 
315  N N   . ALA A 44  ? 1.5454 1.5454 1.5454 0.0000 0.0000 0.0000 43  ALA A N   
316  C CA  . ALA A 44  ? 1.5454 1.5454 1.5454 0.0000 0.0000 0.0000 43  ALA A CA  
317  C C   . ALA A 44  ? 1.5454 1.5454 1.5454 0.0000 0.0000 0.0000 43  ALA A C   
318  O O   . ALA A 44  ? 1.5454 1.5454 1.5454 0.0000 0.0000 0.0000 43  ALA A O   
319  C CB  . ALA A 44  ? 1.5454 1.5454 1.5454 0.0000 0.0000 0.0000 43  ALA A CB  
320  N N   . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A N   
321  C CA  . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A CA  
322  C C   . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A C   
323  O O   . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A O   
324  C CB  . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A CB  
325  C CG  . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A CG  
326  C CD  . PRO A 45  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 44  PRO A CD  
327  N N   . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A N   
328  C CA  . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A CA  
329  C C   . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A C   
330  O O   . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A O   
331  C CB  . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A CB  
332  C CG  . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A CG  
333  C CD  . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A CD  
334  N NE  . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A NE  
335  C CZ  . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A CZ  
336  N NH1 . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A NH1 
337  N NH2 . ARG A 46  ? 1.4286 1.4286 1.4286 0.0000 0.0000 0.0000 45  ARG A NH2 
338  N N   . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A N   
339  C CA  . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A CA  
340  C C   . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A C   
341  O O   . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A O   
342  C CB  . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A CB  
343  C CG  . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A CG  
344  C CD1 . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A CD1 
345  C CD2 . LEU A 47  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 46  LEU A CD2 
346  N N   . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A N   
347  C CA  . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A CA  
348  C C   . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A C   
349  O O   . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A O   
350  C CB  . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A CB  
351  C CG  . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A CG  
352  C CD1 . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A CD1 
353  C CD2 . LEU A 48  ? 1.3405 1.3405 1.3405 0.0000 0.0000 0.0000 47  LEU A CD2 
354  N N   . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A N   
355  C CA  . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A CA  
356  C C   . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A C   
357  O O   . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A O   
358  C CB  . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A CB  
359  C CG1 . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A CG1 
360  C CG2 . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A CG2 
361  C CD1 . ILE A 49  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 48  ILE A CD1 
362  N N   . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A N   
363  C CA  . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CA  
364  C C   . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A C   
365  O O   . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A O   
366  C CB  . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CB  
367  C CG  . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CG  
368  C CD1 . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CD1 
369  C CD2 . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CD2 
370  C CE1 . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CE1 
371  C CE2 . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CE2 
372  C CZ  . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A CZ  
373  O OH  . TYR A 50  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 49  TYR A OH  
374  N N   . GLY A 51  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 50  GLY A N   
375  C CA  . GLY A 51  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 50  GLY A CA  
376  C C   . GLY A 51  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 50  GLY A C   
377  O O   . GLY A 51  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 50  GLY A O   
378  N N   . ALA A 52  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 51  ALA A N   
379  C CA  . ALA A 52  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 51  ALA A CA  
380  C C   . ALA A 52  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 51  ALA A C   
381  O O   . ALA A 52  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 51  ALA A O   
382  C CB  . ALA A 52  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 51  ALA A CB  
383  N N   . SER A 53  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 52  SER A N   
384  C CA  . SER A 53  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 52  SER A CA  
385  C C   . SER A 53  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 52  SER A C   
386  O O   . SER A 53  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 52  SER A O   
387  C CB  . SER A 53  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 52  SER A CB  
388  O OG  . SER A 53  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 52  SER A OG  
389  N N   . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A N   
390  C CA  . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CA  
391  C C   . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A C   
392  O O   . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A O   
393  C CB  . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CB  
394  C CG  . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CG  
395  C CD1 . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CD1 
396  C CD2 . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CD2 
397  C CE1 . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CE1 
398  C CE2 . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CE2 
399  C CZ  . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A CZ  
400  O OH  . TYR A 54  ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 53  TYR A OH  
401  N N   . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A N   
402  C CA  . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A CA  
403  C C   . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A C   
404  O O   . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A O   
405  C CB  . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A CB  
406  C CG  . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A CG  
407  S SD  . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A SD  
408  C CE  . MET A 55  ? 1.3553 1.3553 1.3553 0.0000 0.0000 0.0000 54  MET A CE  
409  N N   . ALA A 56  ? 1.3999 1.3999 1.3999 0.0000 0.0000 0.0000 55  ALA A N   
410  C CA  . ALA A 56  ? 1.3999 1.3999 1.3999 0.0000 0.0000 0.0000 55  ALA A CA  
411  C C   . ALA A 56  ? 1.3999 1.3999 1.3999 0.0000 0.0000 0.0000 55  ALA A C   
412  O O   . ALA A 56  ? 1.3999 1.3999 1.3999 0.0000 0.0000 0.0000 55  ALA A O   
413  C CB  . ALA A 56  ? 1.3999 1.3999 1.3999 0.0000 0.0000 0.0000 55  ALA A CB  
414  N N   . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A N   
415  C CA  . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A CA  
416  C C   . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A C   
417  O O   . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A O   
418  C CB  . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A CB  
419  O OG1 . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A OG1 
420  C CG2 . THR A 57  ? 1.4800 1.4800 1.4800 0.0000 0.0000 0.0000 56  THR A CG2 
421  N N   . GLY A 58  ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 57  GLY A N   
422  C CA  . GLY A 58  ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 57  GLY A CA  
423  C C   . GLY A 58  ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 57  GLY A C   
424  O O   . GLY A 58  ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 57  GLY A O   
425  N N   . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A N   
426  C CA  . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A CA  
427  C C   . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A C   
428  O O   . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A O   
429  C CB  . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A CB  
430  C CG1 . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A CG1 
431  C CG2 . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A CG2 
432  C CD1 . ILE A 59  ? 1.5072 1.5072 1.5072 0.0000 0.0000 0.0000 58  ILE A CD1 
433  N N   . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A N   
434  C CA  . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A CA  
435  C C   . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A C   
436  O O   . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A O   
437  C CB  . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A CB  
438  C CG  . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A CG  
439  C CD  . PRO A 60  ? 1.5728 1.5728 1.5728 0.0000 0.0000 0.0000 59  PRO A CD  
440  N N   . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A N   
441  C CA  . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A CA  
442  C C   . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A C   
443  O O   . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A O   
444  C CB  . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A CB  
445  C CG  . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A CG  
446  O OD1 . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A OD1 
447  O OD2 . ASP A 61  ? 1.6704 1.6704 1.6704 0.0000 0.0000 0.0000 60  ASP A OD2 
448  N N   . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A N   
449  C CA  . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A CA  
450  C C   . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A C   
451  O O   . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A O   
452  C CB  . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A CB  
453  C CG  . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A CG  
454  C CD  . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A CD  
455  N NE  . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A NE  
456  C CZ  . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A CZ  
457  N NH1 . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A NH1 
458  N NH2 . ARG A 62  ? 1.6648 1.6648 1.6648 0.0000 0.0000 0.0000 61  ARG A NH2 
459  N N   . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A N   
460  C CA  . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CA  
461  C C   . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A C   
462  O O   . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A O   
463  C CB  . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CB  
464  C CG  . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CG  
465  C CD1 . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CD1 
466  C CD2 . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CD2 
467  C CE1 . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CE1 
468  C CE2 . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CE2 
469  C CZ  . PHE A 63  ? 1.5030 1.5030 1.5030 0.0000 0.0000 0.0000 62  PHE A CZ  
470  N N   . SER A 64  ? 1.5090 1.5090 1.5090 0.0000 0.0000 0.0000 63  SER A N   
471  C CA  . SER A 64  ? 1.5090 1.5090 1.5090 0.0000 0.0000 0.0000 63  SER A CA  
472  C C   . SER A 64  ? 1.5090 1.5090 1.5090 0.0000 0.0000 0.0000 63  SER A C   
473  O O   . SER A 64  ? 1.5090 1.5090 1.5090 0.0000 0.0000 0.0000 63  SER A O   
474  C CB  . SER A 64  ? 1.5090 1.5090 1.5090 0.0000 0.0000 0.0000 63  SER A CB  
475  O OG  . SER A 64  ? 1.5090 1.5090 1.5090 0.0000 0.0000 0.0000 63  SER A OG  
476  N N   . GLY A 65  ? 1.4382 1.4382 1.4382 0.0000 0.0000 0.0000 64  GLY A N   
477  C CA  . GLY A 65  ? 1.4382 1.4382 1.4382 0.0000 0.0000 0.0000 64  GLY A CA  
478  C C   . GLY A 65  ? 1.4382 1.4382 1.4382 0.0000 0.0000 0.0000 64  GLY A C   
479  O O   . GLY A 65  ? 1.4382 1.4382 1.4382 0.0000 0.0000 0.0000 64  GLY A O   
480  N N   . SER A 66  ? 1.5260 1.5260 1.5260 0.0000 0.0000 0.0000 65  SER A N   
481  C CA  . SER A 66  ? 1.5260 1.5260 1.5260 0.0000 0.0000 0.0000 65  SER A CA  
482  C C   . SER A 66  ? 1.5260 1.5260 1.5260 0.0000 0.0000 0.0000 65  SER A C   
483  O O   . SER A 66  ? 1.5260 1.5260 1.5260 0.0000 0.0000 0.0000 65  SER A O   
484  C CB  . SER A 66  ? 1.5260 1.5260 1.5260 0.0000 0.0000 0.0000 65  SER A CB  
485  O OG  . SER A 66  ? 1.5260 1.5260 1.5260 0.0000 0.0000 0.0000 65  SER A OG  
486  N N   . GLY A 67  ? 1.5716 1.5716 1.5716 0.0000 0.0000 0.0000 66  GLY A N   
487  C CA  . GLY A 67  ? 1.5716 1.5716 1.5716 0.0000 0.0000 0.0000 66  GLY A CA  
488  C C   . GLY A 67  ? 1.5716 1.5716 1.5716 0.0000 0.0000 0.0000 66  GLY A C   
489  O O   . GLY A 67  ? 1.5716 1.5716 1.5716 0.0000 0.0000 0.0000 66  GLY A O   
490  N N   . SER A 68  ? 1.6213 1.6213 1.6213 0.0000 0.0000 0.0000 67  SER A N   
491  C CA  . SER A 68  ? 1.6213 1.6213 1.6213 0.0000 0.0000 0.0000 67  SER A CA  
492  C C   . SER A 68  ? 1.6213 1.6213 1.6213 0.0000 0.0000 0.0000 67  SER A C   
493  O O   . SER A 68  ? 1.6213 1.6213 1.6213 0.0000 0.0000 0.0000 67  SER A O   
494  C CB  . SER A 68  ? 1.6213 1.6213 1.6213 0.0000 0.0000 0.0000 67  SER A CB  
495  O OG  . SER A 68  ? 1.6213 1.6213 1.6213 0.0000 0.0000 0.0000 67  SER A OG  
496  N N   . GLY A 69  ? 1.6151 1.6151 1.6151 0.0000 0.0000 0.0000 68  GLY A N   
497  C CA  . GLY A 69  ? 1.6151 1.6151 1.6151 0.0000 0.0000 0.0000 68  GLY A CA  
498  C C   . GLY A 69  ? 1.6151 1.6151 1.6151 0.0000 0.0000 0.0000 68  GLY A C   
499  O O   . GLY A 69  ? 1.6151 1.6151 1.6151 0.0000 0.0000 0.0000 68  GLY A O   
500  N N   . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A N   
501  C CA  . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A CA  
502  C C   . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A C   
503  O O   . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A O   
504  C CB  . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A CB  
505  O OG1 . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A OG1 
506  C CG2 . THR A 70  ? 1.6726 1.6726 1.6726 0.0000 0.0000 0.0000 69  THR A CG2 
507  N N   . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A N   
508  C CA  . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A CA  
509  C C   . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A C   
510  O O   . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A O   
511  C CB  . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A CB  
512  C CG  . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A CG  
513  O OD1 . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A OD1 
514  O OD2 . ASP A 71  ? 1.6394 1.6394 1.6394 0.0000 0.0000 0.0000 70  ASP A OD2 
515  N N   . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A N   
516  C CA  . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CA  
517  C C   . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A C   
518  O O   . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A O   
519  C CB  . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CB  
520  C CG  . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CG  
521  C CD1 . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CD1 
522  C CD2 . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CD2 
523  C CE1 . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CE1 
524  C CE2 . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CE2 
525  C CZ  . PHE A 72  ? 1.5425 1.5425 1.5425 0.0000 0.0000 0.0000 71  PHE A CZ  
526  N N   . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A N   
527  C CA  . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A CA  
528  C C   . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A C   
529  O O   . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A O   
530  C CB  . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A CB  
531  O OG1 . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A OG1 
532  C CG2 . THR A 73  ? 1.5367 1.5367 1.5367 0.0000 0.0000 0.0000 72  THR A CG2 
533  N N   . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A N   
534  C CA  . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A CA  
535  C C   . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A C   
536  O O   . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A O   
537  C CB  . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A CB  
538  C CG  . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A CG  
539  C CD1 . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A CD1 
540  C CD2 . LEU A 74  ? 1.5150 1.5150 1.5150 0.0000 0.0000 0.0000 73  LEU A CD2 
541  N N   . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A N   
542  C CA  . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A CA  
543  C C   . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A C   
544  O O   . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A O   
545  C CB  . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A CB  
546  O OG1 . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A OG1 
547  C CG2 . THR A 75  ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 74  THR A CG2 
548  N N   . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A N   
549  C CA  . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A CA  
550  C C   . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A C   
551  O O   . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A O   
552  C CB  . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A CB  
553  C CG1 . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A CG1 
554  C CG2 . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A CG2 
555  C CD1 . ILE A 76  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 75  ILE A CD1 
556  N N   . SER A 77  ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 76  SER A N   
557  C CA  . SER A 77  ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 76  SER A CA  
558  C C   . SER A 77  ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 76  SER A C   
559  O O   . SER A 77  ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 76  SER A O   
560  C CB  . SER A 77  ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 76  SER A CB  
561  O OG  . SER A 77  ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 76  SER A OG  
562  N N   . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A N   
563  C CA  . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A CA  
564  C C   . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A C   
565  O O   . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A O   
566  C CB  . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A CB  
567  C CG  . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A CG  
568  C CD  . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A CD  
569  N NE  . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A NE  
570  C CZ  . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A CZ  
571  N NH1 . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A NH1 
572  N NH2 . ARG A 78  ? 1.9117 1.9117 1.9117 0.0000 0.0000 0.0000 77  ARG A NH2 
573  N N   . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A N   
574  C CA  . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A CA  
575  C C   . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A C   
576  O O   . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A O   
577  C CB  . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A CB  
578  C CG  . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A CG  
579  C CD1 . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A CD1 
580  C CD2 . LEU A 79  ? 1.9349 1.9349 1.9349 0.0000 0.0000 0.0000 78  LEU A CD2 
581  N N   . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A N   
582  C CA  . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A CA  
583  C C   . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A C   
584  O O   . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A O   
585  C CB  . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A CB  
586  C CG  . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A CG  
587  C CD  . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A CD  
588  O OE1 . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A OE1 
589  O OE2 . GLU A 80  ? 1.9692 1.9692 1.9692 0.0000 0.0000 0.0000 79  GLU A OE2 
590  N N   . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A N   
591  C CA  . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A CA  
592  C C   . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A C   
593  O O   . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A O   
594  C CB  . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A CB  
595  C CG  . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A CG  
596  C CD  . PRO A 81  ? 1.9813 1.9813 1.9813 0.0000 0.0000 0.0000 80  PRO A CD  
597  N N   . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A N   
598  C CA  . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A CA  
599  C C   . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A C   
600  O O   . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A O   
601  C CB  . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A CB  
602  C CG  . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A CG  
603  C CD  . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A CD  
604  O OE1 . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A OE1 
605  O OE2 . GLU A 82  ? 1.9502 1.9502 1.9502 0.0000 0.0000 0.0000 81  GLU A OE2 
606  N N   . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A N   
607  C CA  . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A CA  
608  C C   . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A C   
609  O O   . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A O   
610  C CB  . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A CB  
611  C CG  . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A CG  
612  O OD1 . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A OD1 
613  O OD2 . ASP A 83  ? 1.9200 1.9200 1.9200 0.0000 0.0000 0.0000 82  ASP A OD2 
614  N N   . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A N   
615  C CA  . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CA  
616  C C   . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A C   
617  O O   . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A O   
618  C CB  . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CB  
619  C CG  . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CG  
620  C CD1 . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CD1 
621  C CD2 . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CD2 
622  C CE1 . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CE1 
623  C CE2 . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CE2 
624  C CZ  . PHE A 84  ? 1.9510 1.9510 1.9510 0.0000 0.0000 0.0000 83  PHE A CZ  
625  N N   . ALA A 85  ? 1.7321 1.7321 1.7321 0.0000 0.0000 0.0000 84  ALA A N   
626  C CA  . ALA A 85  ? 1.7321 1.7321 1.7321 0.0000 0.0000 0.0000 84  ALA A CA  
627  C C   . ALA A 85  ? 1.7321 1.7321 1.7321 0.0000 0.0000 0.0000 84  ALA A C   
628  O O   . ALA A 85  ? 1.7321 1.7321 1.7321 0.0000 0.0000 0.0000 84  ALA A O   
629  C CB  . ALA A 85  ? 1.7321 1.7321 1.7321 0.0000 0.0000 0.0000 84  ALA A CB  
630  N N   . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A N   
631  C CA  . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A CA  
632  C C   . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A C   
633  O O   . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A O   
634  C CB  . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A CB  
635  C CG1 . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A CG1 
636  C CG2 . VAL A 86  ? 1.5668 1.5668 1.5668 0.0000 0.0000 0.0000 85  VAL A CG2 
637  N N   . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A N   
638  C CA  . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CA  
639  C C   . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A C   
640  O O   . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A O   
641  C CB  . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CB  
642  C CG  . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CG  
643  C CD1 . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CD1 
644  C CD2 . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CD2 
645  C CE1 . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CE1 
646  C CE2 . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CE2 
647  C CZ  . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A CZ  
648  O OH  . TYR A 87  ? 1.4805 1.4805 1.4805 0.0000 0.0000 0.0000 86  TYR A OH  
649  N N   . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A N   
650  C CA  . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CA  
651  C C   . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A C   
652  O O   . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A O   
653  C CB  . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CB  
654  C CG  . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CG  
655  C CD1 . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CD1 
656  C CD2 . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CD2 
657  C CE1 . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CE1 
658  C CE2 . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CE2 
659  C CZ  . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A CZ  
660  O OH  . TYR A 88  ? 1.4671 1.4671 1.4671 0.0000 0.0000 0.0000 87  TYR A OH  
661  N N   . CYS A 89  ? 1.4378 1.4378 1.4378 0.0000 0.0000 0.0000 88  CYS A N   
662  C CA  . CYS A 89  ? 1.4378 1.4378 1.4378 0.0000 0.0000 0.0000 88  CYS A CA  
663  C C   . CYS A 89  ? 1.4378 1.4378 1.4378 0.0000 0.0000 0.0000 88  CYS A C   
664  O O   . CYS A 89  ? 1.4378 1.4378 1.4378 0.0000 0.0000 0.0000 88  CYS A O   
665  C CB  . CYS A 89  ? 1.4378 1.4378 1.4378 0.0000 0.0000 0.0000 88  CYS A CB  
666  S SG  . CYS A 89  ? 1.4378 1.4378 1.4378 0.0000 0.0000 0.0000 88  CYS A SG  
667  N N   . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A N   
668  C CA  . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A CA  
669  C C   . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A C   
670  O O   . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A O   
671  C CB  . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A CB  
672  C CG  . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A CG  
673  C CD  . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A CD  
674  O OE1 . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A OE1 
675  N NE2 . GLN A 90  ? 1.3548 1.3548 1.3548 0.0000 0.0000 0.0000 89  GLN A NE2 
676  N N   . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A N   
677  C CA  . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A CA  
678  C C   . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A C   
679  O O   . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A O   
680  C CB  . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A CB  
681  C CG  . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A CG  
682  C CD  . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A CD  
683  O OE1 . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A OE1 
684  N NE2 . GLN A 91  ? 1.3764 1.3764 1.3764 0.0000 0.0000 0.0000 90  GLN A NE2 
685  N N   . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A N   
686  C CA  . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CA  
687  C C   . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A C   
688  O O   . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A O   
689  C CB  . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CB  
690  C CG  . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CG  
691  C CD1 . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CD1 
692  C CD2 . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CD2 
693  C CE1 . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CE1 
694  C CE2 . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CE2 
695  C CZ  . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A CZ  
696  O OH  . TYR A 92  ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 91  TYR A OH  
697  N N   . GLY A 93  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 92  GLY A N   
698  C CA  . GLY A 93  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 92  GLY A CA  
699  C C   . GLY A 93  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 92  GLY A C   
700  O O   . GLY A 93  ? 1.4588 1.4588 1.4588 0.0000 0.0000 0.0000 92  GLY A O   
701  N N   . SER A 94  ? 1.5172 1.5172 1.5172 0.0000 0.0000 0.0000 93  SER A N   
702  C CA  . SER A 94  ? 1.5172 1.5172 1.5172 0.0000 0.0000 0.0000 93  SER A CA  
703  C C   . SER A 94  ? 1.5172 1.5172 1.5172 0.0000 0.0000 0.0000 93  SER A C   
704  O O   . SER A 94  ? 1.5172 1.5172 1.5172 0.0000 0.0000 0.0000 93  SER A O   
705  C CB  . SER A 94  ? 1.5172 1.5172 1.5172 0.0000 0.0000 0.0000 93  SER A CB  
706  O OG  . SER A 94  ? 1.5172 1.5172 1.5172 0.0000 0.0000 0.0000 93  SER A OG  
707  N N   . SER A 95  ? 1.4986 1.4986 1.4986 0.0000 0.0000 0.0000 94  SER A N   
708  C CA  . SER A 95  ? 1.4986 1.4986 1.4986 0.0000 0.0000 0.0000 94  SER A CA  
709  C C   . SER A 95  ? 1.4986 1.4986 1.4986 0.0000 0.0000 0.0000 94  SER A C   
710  O O   . SER A 95  ? 1.4986 1.4986 1.4986 0.0000 0.0000 0.0000 94  SER A O   
711  C CB  . SER A 95  ? 1.4986 1.4986 1.4986 0.0000 0.0000 0.0000 94  SER A CB  
712  O OG  . SER A 95  ? 1.4986 1.4986 1.4986 0.0000 0.0000 0.0000 94  SER A OG  
713  N N   . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A N   
714  C CA  . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A CA  
715  C C   . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A C   
716  O O   . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A O   
717  C CB  . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A CB  
718  C CG  . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A CG  
719  C CD1 . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A CD1 
720  C CD2 . LEU A 96  ? 1.4246 1.4246 1.4246 0.0000 0.0000 0.0000 95  LEU A CD2 
721  N N   . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A N   
722  C CA  . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A CA  
723  C C   . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A C   
724  O O   . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A O   
725  C CB  . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A CB  
726  O OG1 . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A OG1 
727  C CG2 . THR A 97  ? 1.4219 1.4219 1.4219 0.0000 0.0000 0.0000 96  THR A CG2 
728  N N   . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A N   
729  C CA  . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CA  
730  C C   . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A C   
731  O O   . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A O   
732  C CB  . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CB  
733  C CG  . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CG  
734  C CD1 . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CD1 
735  C CD2 . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CD2 
736  C CE1 . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CE1 
737  C CE2 . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CE2 
738  C CZ  . PHE A 98  ? 1.4256 1.4256 1.4256 0.0000 0.0000 0.0000 97  PHE A CZ  
739  N N   . GLY A 99  ? 1.4977 1.4977 1.4977 0.0000 0.0000 0.0000 98  GLY A N   
740  C CA  . GLY A 99  ? 1.4977 1.4977 1.4977 0.0000 0.0000 0.0000 98  GLY A CA  
741  C C   . GLY A 99  ? 1.4977 1.4977 1.4977 0.0000 0.0000 0.0000 98  GLY A C   
742  O O   . GLY A 99  ? 1.4977 1.4977 1.4977 0.0000 0.0000 0.0000 98  GLY A O   
743  N N   . GLY A 100 ? 1.5750 1.5750 1.5750 0.0000 0.0000 0.0000 99  GLY A N   
744  C CA  . GLY A 100 ? 1.5750 1.5750 1.5750 0.0000 0.0000 0.0000 99  GLY A CA  
745  C C   . GLY A 100 ? 1.5750 1.5750 1.5750 0.0000 0.0000 0.0000 99  GLY A C   
746  O O   . GLY A 100 ? 1.5750 1.5750 1.5750 0.0000 0.0000 0.0000 99  GLY A O   
747  N N   . GLY A 101 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 100 GLY A N   
748  C CA  . GLY A 101 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 100 GLY A CA  
749  C C   . GLY A 101 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 100 GLY A C   
750  O O   . GLY A 101 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 100 GLY A O   
751  N N   . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A N   
752  C CA  . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A CA  
753  C C   . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A C   
754  O O   . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A O   
755  C CB  . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A CB  
756  O OG1 . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A OG1 
757  C CG2 . THR A 102 ? 1.6641 1.6641 1.6641 0.0000 0.0000 0.0000 101 THR A CG2 
758  N N   . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A N   
759  C CA  . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A CA  
760  C C   . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A C   
761  O O   . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A O   
762  C CB  . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A CB  
763  C CG  . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A CG  
764  C CD  . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A CD  
765  C CE  . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A CE  
766  N NZ  . LYS A 103 ? 1.8040 1.8040 1.8040 0.0000 0.0000 0.0000 102 LYS A NZ  
767  N N   . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A N   
768  C CA  . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A CA  
769  C C   . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A C   
770  O O   . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A O   
771  C CB  . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A CB  
772  C CG  . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A CG  
773  C CD1 . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A CD1 
774  C CD2 . LEU A 104 ? 1.8908 1.8908 1.8908 0.0000 0.0000 0.0000 103 LEU A CD2 
775  N N   . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A N   
776  C CA  . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A CA  
777  C C   . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A C   
778  O O   . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A O   
779  C CB  . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A CB  
780  C CG  . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A CG  
781  C CD  . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A CD  
782  O OE1 . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A OE1 
783  O OE2 . GLU A 105 ? 2.0003 2.0003 2.0003 0.0000 0.0000 0.0000 104 GLU A OE2 
784  N N   . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A N   
785  C CA  . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A CA  
786  C C   . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A C   
787  O O   . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A O   
788  C CB  . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A CB  
789  C CG1 . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A CG1 
790  C CG2 . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A CG2 
791  C CD1 . ILE A 106 ? 2.0631 2.0631 2.0631 0.0000 0.0000 0.0000 105 ILE A CD1 
792  N N   . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A N   
793  C CA  . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A CA  
794  C C   . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A C   
795  O O   . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A O   
796  C CB  . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A CB  
797  C CG  . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A CG  
798  C CD  . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A CD  
799  C CE  . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A CE  
800  N NZ  . LYS A 107 ? 2.0807 2.0807 2.0807 0.0000 0.0000 0.0000 106 LYS A NZ  
801  N N   . SER A 122 ? 1.8259 1.8259 1.8259 0.0000 0.0000 0.0000 121 SER A N   
802  C CA  . SER A 122 ? 1.8259 1.8259 1.8259 0.0000 0.0000 0.0000 121 SER A CA  
803  C C   . SER A 122 ? 1.8259 1.8259 1.8259 0.0000 0.0000 0.0000 121 SER A C   
804  O O   . SER A 122 ? 1.8259 1.8259 1.8259 0.0000 0.0000 0.0000 121 SER A O   
805  C CB  . SER A 122 ? 1.8259 1.8259 1.8259 0.0000 0.0000 0.0000 121 SER A CB  
806  O OG  . SER A 122 ? 1.8259 1.8259 1.8259 0.0000 0.0000 0.0000 121 SER A OG  
807  N N   . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A N   
808  C CA  . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A CA  
809  C C   . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A C   
810  O O   . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A O   
811  C CB  . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A CB  
812  C CG  . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A CG  
813  C CD  . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A CD  
814  O OE1 . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A OE1 
815  N NE2 . GLN A 123 ? 1.8351 1.8351 1.8351 0.0000 0.0000 0.0000 122 GLN A NE2 
816  N N   . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A N   
817  C CA  . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A CA  
818  C C   . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A C   
819  O O   . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A O   
820  C CB  . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A CB  
821  C CG1 . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A CG1 
822  C CG2 . VAL A 124 ? 1.7454 1.7454 1.7454 0.0000 0.0000 0.0000 123 VAL A CG2 
823  N N   . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A N   
824  C CA  . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A CA  
825  C C   . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A C   
826  O O   . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A O   
827  C CB  . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A CB  
828  C CG  . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A CG  
829  C CD  . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A CD  
830  O OE1 . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A OE1 
831  N NE2 . GLN A 125 ? 1.7423 1.7423 1.7423 0.0000 0.0000 0.0000 124 GLN A NE2 
832  N N   . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A N   
833  C CA  . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A CA  
834  C C   . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A C   
835  O O   . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A O   
836  C CB  . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A CB  
837  C CG  . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A CG  
838  C CD1 . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A CD1 
839  C CD2 . LEU A 126 ? 1.6759 1.6759 1.6759 0.0000 0.0000 0.0000 125 LEU A CD2 
840  N N   . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A N   
841  C CA  . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A CA  
842  C C   . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A C   
843  O O   . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A O   
844  C CB  . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A CB  
845  C CG  . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A CG  
846  C CD  . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A CD  
847  O OE1 . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A OE1 
848  N NE2 . GLN A 127 ? 1.8257 1.8257 1.8257 0.0000 0.0000 0.0000 126 GLN A NE2 
849  N N   . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A N   
850  C CA  . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A CA  
851  C C   . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A C   
852  O O   . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A O   
853  C CB  . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A CB  
854  C CG  . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A CG  
855  C CD  . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A CD  
856  O OE1 . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A OE1 
857  N NE2 . GLN A 128 ? 1.7906 1.7906 1.7906 0.0000 0.0000 0.0000 127 GLN A NE2 
858  N N   . SER A 129 ? 1.9258 1.9258 1.9258 0.0000 0.0000 0.0000 128 SER A N   
859  C CA  . SER A 129 ? 1.9258 1.9258 1.9258 0.0000 0.0000 0.0000 128 SER A CA  
860  C C   . SER A 129 ? 1.9258 1.9258 1.9258 0.0000 0.0000 0.0000 128 SER A C   
861  O O   . SER A 129 ? 1.9258 1.9258 1.9258 0.0000 0.0000 0.0000 128 SER A O   
862  C CB  . SER A 129 ? 1.9258 1.9258 1.9258 0.0000 0.0000 0.0000 128 SER A CB  
863  O OG  . SER A 129 ? 1.9258 1.9258 1.9258 0.0000 0.0000 0.0000 128 SER A OG  
864  N N   . GLY A 130 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 129 GLY A N   
865  C CA  . GLY A 130 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 129 GLY A CA  
866  C C   . GLY A 130 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 129 GLY A C   
867  O O   . GLY A 130 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 129 GLY A O   
868  N N   . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A N   
869  C CA  . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A CA  
870  C C   . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A C   
871  O O   . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A O   
872  C CB  . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A CB  
873  C CG  . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A CG  
874  C CD  . PRO A 131 ? 2.1222 2.1222 2.1222 0.0000 0.0000 0.0000 130 PRO A CD  
875  N N   . GLY A 132 ? 2.1538 2.1538 2.1538 0.0000 0.0000 0.0000 131 GLY A N   
876  C CA  . GLY A 132 ? 2.1538 2.1538 2.1538 0.0000 0.0000 0.0000 131 GLY A CA  
877  C C   . GLY A 132 ? 2.1538 2.1538 2.1538 0.0000 0.0000 0.0000 131 GLY A C   
878  O O   . GLY A 132 ? 2.1538 2.1538 2.1538 0.0000 0.0000 0.0000 131 GLY A O   
879  N N   . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A N   
880  C CA  . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A CA  
881  C C   . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A C   
882  O O   . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A O   
883  C CB  . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A CB  
884  C CG  . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A CG  
885  C CD1 . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A CD1 
886  C CD2 . LEU A 133 ? 2.1966 2.1966 2.1966 0.0000 0.0000 0.0000 132 LEU A CD2 
887  N N   . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A N   
888  C CA  . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A CA  
889  C C   . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A C   
890  O O   . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A O   
891  C CB  . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A CB  
892  C CG1 . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A CG1 
893  C CG2 . VAL A 134 ? 2.2371 2.2371 2.2371 0.0000 0.0000 0.0000 133 VAL A CG2 
894  N N   . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A N   
895  C CA  . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A CA  
896  C C   . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A C   
897  O O   . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A O   
898  C CB  . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A CB  
899  C CG  . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A CG  
900  C CD  . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A CD  
901  C CE  . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A CE  
902  N NZ  . LYS A 135 ? 2.2706 2.2706 2.2706 0.0000 0.0000 0.0000 134 LYS A NZ  
903  N N   . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A N   
904  C CA  . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A CA  
905  C C   . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A C   
906  O O   . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A O   
907  C CB  . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A CB  
908  C CG  . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A CG  
909  C CD  . PRO A 136 ? 2.2510 2.2510 2.2510 0.0000 0.0000 0.0000 135 PRO A CD  
910  N N   . SER A 137 ? 2.2008 2.2008 2.2008 0.0000 0.0000 0.0000 136 SER A N   
911  C CA  . SER A 137 ? 2.2008 2.2008 2.2008 0.0000 0.0000 0.0000 136 SER A CA  
912  C C   . SER A 137 ? 2.2008 2.2008 2.2008 0.0000 0.0000 0.0000 136 SER A C   
913  O O   . SER A 137 ? 2.2008 2.2008 2.2008 0.0000 0.0000 0.0000 136 SER A O   
914  C CB  . SER A 137 ? 2.2008 2.2008 2.2008 0.0000 0.0000 0.0000 136 SER A CB  
915  O OG  . SER A 137 ? 2.2008 2.2008 2.2008 0.0000 0.0000 0.0000 136 SER A OG  
916  N N   . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A N   
917  C CA  . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A CA  
918  C C   . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A C   
919  O O   . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A O   
920  C CB  . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A CB  
921  C CG  . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A CG  
922  C CD  . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A CD  
923  O OE1 . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A OE1 
924  N NE2 . GLN A 138 ? 2.2107 2.2107 2.2107 0.0000 0.0000 0.0000 137 GLN A NE2 
925  N N   . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A N   
926  C CA  . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A CA  
927  C C   . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A C   
928  O O   . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A O   
929  C CB  . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A CB  
930  O OG1 . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A OG1 
931  C CG2 . THR A 139 ? 2.1533 2.1533 2.1533 0.0000 0.0000 0.0000 138 THR A CG2 
932  N N   . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A N   
933  C CA  . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A CA  
934  C C   . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A C   
935  O O   . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A O   
936  C CB  . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A CB  
937  C CG  . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A CG  
938  C CD1 . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A CD1 
939  C CD2 . LEU A 140 ? 2.0082 2.0082 2.0082 0.0000 0.0000 0.0000 139 LEU A CD2 
940  N N   . SER A 141 ? 1.9292 1.9292 1.9292 0.0000 0.0000 0.0000 140 SER A N   
941  C CA  . SER A 141 ? 1.9292 1.9292 1.9292 0.0000 0.0000 0.0000 140 SER A CA  
942  C C   . SER A 141 ? 1.9292 1.9292 1.9292 0.0000 0.0000 0.0000 140 SER A C   
943  O O   . SER A 141 ? 1.9292 1.9292 1.9292 0.0000 0.0000 0.0000 140 SER A O   
944  C CB  . SER A 141 ? 1.9292 1.9292 1.9292 0.0000 0.0000 0.0000 140 SER A CB  
945  O OG  . SER A 141 ? 1.9292 1.9292 1.9292 0.0000 0.0000 0.0000 140 SER A OG  
946  N N   . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A N   
947  C CA  . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A CA  
948  C C   . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A C   
949  O O   . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A O   
950  C CB  . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A CB  
951  C CG  . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A CG  
952  C CD1 . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A CD1 
953  C CD2 . LEU A 142 ? 1.8662 1.8662 1.8662 0.0000 0.0000 0.0000 141 LEU A CD2 
954  N N   . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A N   
955  C CA  . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A CA  
956  C C   . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A C   
957  O O   . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A O   
958  C CB  . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A CB  
959  O OG1 . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A OG1 
960  C CG2 . THR A 143 ? 1.8455 1.8455 1.8455 0.0000 0.0000 0.0000 142 THR A CG2 
961  N N   . CYS A 144 ? 1.8338 1.8338 1.8338 0.0000 0.0000 0.0000 143 CYS A N   
962  C CA  . CYS A 144 ? 1.8338 1.8338 1.8338 0.0000 0.0000 0.0000 143 CYS A CA  
963  C C   . CYS A 144 ? 1.8338 1.8338 1.8338 0.0000 0.0000 0.0000 143 CYS A C   
964  O O   . CYS A 144 ? 1.8338 1.8338 1.8338 0.0000 0.0000 0.0000 143 CYS A O   
965  C CB  . CYS A 144 ? 1.8338 1.8338 1.8338 0.0000 0.0000 0.0000 143 CYS A CB  
966  S SG  . CYS A 144 ? 1.8338 1.8338 1.8338 0.0000 0.0000 0.0000 143 CYS A SG  
967  N N   . SER A 145 ? 1.8085 1.8085 1.8085 0.0000 0.0000 0.0000 144 SER A N   
968  C CA  . SER A 145 ? 1.8085 1.8085 1.8085 0.0000 0.0000 0.0000 144 SER A CA  
969  C C   . SER A 145 ? 1.8085 1.8085 1.8085 0.0000 0.0000 0.0000 144 SER A C   
970  O O   . SER A 145 ? 1.8085 1.8085 1.8085 0.0000 0.0000 0.0000 144 SER A O   
971  C CB  . SER A 145 ? 1.8085 1.8085 1.8085 0.0000 0.0000 0.0000 144 SER A CB  
972  O OG  . SER A 145 ? 1.8085 1.8085 1.8085 0.0000 0.0000 0.0000 144 SER A OG  
973  N N   . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A N   
974  C CA  . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A CA  
975  C C   . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A C   
976  O O   . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A O   
977  C CB  . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A CB  
978  C CG1 . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A CG1 
979  C CG2 . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A CG2 
980  C CD1 . ILE A 146 ? 1.7378 1.7378 1.7378 0.0000 0.0000 0.0000 145 ILE A CD1 
981  N N   . SER A 147 ? 1.7058 1.7058 1.7058 0.0000 0.0000 0.0000 146 SER A N   
982  C CA  . SER A 147 ? 1.7058 1.7058 1.7058 0.0000 0.0000 0.0000 146 SER A CA  
983  C C   . SER A 147 ? 1.7058 1.7058 1.7058 0.0000 0.0000 0.0000 146 SER A C   
984  O O   . SER A 147 ? 1.7058 1.7058 1.7058 0.0000 0.0000 0.0000 146 SER A O   
985  C CB  . SER A 147 ? 1.7058 1.7058 1.7058 0.0000 0.0000 0.0000 146 SER A CB  
986  O OG  . SER A 147 ? 1.7058 1.7058 1.7058 0.0000 0.0000 0.0000 146 SER A OG  
987  N N   . GLY A 148 ? 1.7311 1.7311 1.7311 0.0000 0.0000 0.0000 147 GLY A N   
988  C CA  . GLY A 148 ? 1.7311 1.7311 1.7311 0.0000 0.0000 0.0000 147 GLY A CA  
989  C C   . GLY A 148 ? 1.7311 1.7311 1.7311 0.0000 0.0000 0.0000 147 GLY A C   
990  O O   . GLY A 148 ? 1.7311 1.7311 1.7311 0.0000 0.0000 0.0000 147 GLY A O   
991  N N   . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A N   
992  C CA  . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A CA  
993  C C   . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A C   
994  O O   . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A O   
995  C CB  . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A CB  
996  C CG  . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A CG  
997  O OD1 . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A OD1 
998  O OD2 . ASP A 149 ? 1.7795 1.7795 1.7795 0.0000 0.0000 0.0000 148 ASP A OD2 
999  N N   . SER A 150 ? 1.7285 1.7285 1.7285 0.0000 0.0000 0.0000 149 SER A N   
1000 C CA  . SER A 150 ? 1.7285 1.7285 1.7285 0.0000 0.0000 0.0000 149 SER A CA  
1001 C C   . SER A 150 ? 1.7285 1.7285 1.7285 0.0000 0.0000 0.0000 149 SER A C   
1002 O O   . SER A 150 ? 1.7285 1.7285 1.7285 0.0000 0.0000 0.0000 149 SER A O   
1003 C CB  . SER A 150 ? 1.7285 1.7285 1.7285 0.0000 0.0000 0.0000 149 SER A CB  
1004 O OG  . SER A 150 ? 1.7285 1.7285 1.7285 0.0000 0.0000 0.0000 149 SER A OG  
1005 N N   . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A N   
1006 C CA  . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A CA  
1007 C C   . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A C   
1008 O O   . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A O   
1009 C CB  . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A CB  
1010 C CG1 . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A CG1 
1011 C CG2 . VAL A 151 ? 1.6654 1.6654 1.6654 0.0000 0.0000 0.0000 150 VAL A CG2 
1012 N N   . SER A 152 ? 1.6749 1.6749 1.6749 0.0000 0.0000 0.0000 151 SER A N   
1013 C CA  . SER A 152 ? 1.6749 1.6749 1.6749 0.0000 0.0000 0.0000 151 SER A CA  
1014 C C   . SER A 152 ? 1.6749 1.6749 1.6749 0.0000 0.0000 0.0000 151 SER A C   
1015 O O   . SER A 152 ? 1.6749 1.6749 1.6749 0.0000 0.0000 0.0000 151 SER A O   
1016 C CB  . SER A 152 ? 1.6749 1.6749 1.6749 0.0000 0.0000 0.0000 151 SER A CB  
1017 O OG  . SER A 152 ? 1.6749 1.6749 1.6749 0.0000 0.0000 0.0000 151 SER A OG  
1018 N N   . SER A 153 ? 1.6253 1.6253 1.6253 0.0000 0.0000 0.0000 152 SER A N   
1019 C CA  . SER A 153 ? 1.6253 1.6253 1.6253 0.0000 0.0000 0.0000 152 SER A CA  
1020 C C   . SER A 153 ? 1.6253 1.6253 1.6253 0.0000 0.0000 0.0000 152 SER A C   
1021 O O   . SER A 153 ? 1.6253 1.6253 1.6253 0.0000 0.0000 0.0000 152 SER A O   
1022 C CB  . SER A 153 ? 1.6253 1.6253 1.6253 0.0000 0.0000 0.0000 152 SER A CB  
1023 O OG  . SER A 153 ? 1.6253 1.6253 1.6253 0.0000 0.0000 0.0000 152 SER A OG  
1024 N N   . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A N   
1025 C CA  . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A CA  
1026 C C   . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A C   
1027 O O   . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A O   
1028 C CB  . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A CB  
1029 C CG  . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A CG  
1030 O OD1 . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A OD1 
1031 N ND2 . ASN A 154 ? 1.5940 1.5940 1.5940 0.0000 0.0000 0.0000 153 ASN A ND2 
1032 N N   . SER A 155 ? 1.4713 1.4713 1.4713 0.0000 0.0000 0.0000 154 SER A N   
1033 C CA  . SER A 155 ? 1.4713 1.4713 1.4713 0.0000 0.0000 0.0000 154 SER A CA  
1034 C C   . SER A 155 ? 1.4713 1.4713 1.4713 0.0000 0.0000 0.0000 154 SER A C   
1035 O O   . SER A 155 ? 1.4713 1.4713 1.4713 0.0000 0.0000 0.0000 154 SER A O   
1036 C CB  . SER A 155 ? 1.4713 1.4713 1.4713 0.0000 0.0000 0.0000 154 SER A CB  
1037 O OG  . SER A 155 ? 1.4713 1.4713 1.4713 0.0000 0.0000 0.0000 154 SER A OG  
1038 N N   . ALA A 156 ? 1.3963 1.3963 1.3963 0.0000 0.0000 0.0000 155 ALA A N   
1039 C CA  . ALA A 156 ? 1.3963 1.3963 1.3963 0.0000 0.0000 0.0000 155 ALA A CA  
1040 C C   . ALA A 156 ? 1.3963 1.3963 1.3963 0.0000 0.0000 0.0000 155 ALA A C   
1041 O O   . ALA A 156 ? 1.3963 1.3963 1.3963 0.0000 0.0000 0.0000 155 ALA A O   
1042 C CB  . ALA A 156 ? 1.3963 1.3963 1.3963 0.0000 0.0000 0.0000 155 ALA A CB  
1043 N N   . ALA A 157 ? 1.3599 1.3599 1.3599 0.0000 0.0000 0.0000 156 ALA A N   
1044 C CA  . ALA A 157 ? 1.3599 1.3599 1.3599 0.0000 0.0000 0.0000 156 ALA A CA  
1045 C C   . ALA A 157 ? 1.3599 1.3599 1.3599 0.0000 0.0000 0.0000 156 ALA A C   
1046 O O   . ALA A 157 ? 1.3599 1.3599 1.3599 0.0000 0.0000 0.0000 156 ALA A O   
1047 C CB  . ALA A 157 ? 1.3599 1.3599 1.3599 0.0000 0.0000 0.0000 156 ALA A CB  
1048 N N   . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A N   
1049 C CA  . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CA  
1050 C C   . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A C   
1051 O O   . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A O   
1052 C CB  . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CB  
1053 C CG  . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CG  
1054 C CD1 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CD1 
1055 C CD2 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CD2 
1056 N NE1 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A NE1 
1057 C CE2 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CE2 
1058 C CE3 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CE3 
1059 C CZ2 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CZ2 
1060 C CZ3 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CZ3 
1061 C CH2 . TRP A 158 ? 1.4265 1.4265 1.4265 0.0000 0.0000 0.0000 157 TRP A CH2 
1062 N N   . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A N   
1063 C CA  . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A CA  
1064 C C   . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A C   
1065 O O   . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A O   
1066 C CB  . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A CB  
1067 C CG  . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A CG  
1068 O OD1 . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A OD1 
1069 N ND2 . ASN A 159 ? 1.4450 1.4450 1.4450 0.0000 0.0000 0.0000 158 ASN A ND2 
1070 N N   . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A N   
1071 C CA  . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CA  
1072 C C   . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A C   
1073 O O   . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A O   
1074 C CB  . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CB  
1075 C CG  . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CG  
1076 C CD1 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CD1 
1077 C CD2 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CD2 
1078 N NE1 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A NE1 
1079 C CE2 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CE2 
1080 C CE3 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CE3 
1081 C CZ2 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CZ2 
1082 C CZ3 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CZ3 
1083 C CH2 . TRP A 160 ? 1.6027 1.6027 1.6027 0.0000 0.0000 0.0000 159 TRP A CH2 
1084 N N   . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A N   
1085 C CA  . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A CA  
1086 C C   . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A C   
1087 O O   . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A O   
1088 C CB  . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A CB  
1089 C CG1 . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A CG1 
1090 C CG2 . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A CG2 
1091 C CD1 . ILE A 161 ? 1.6059 1.6059 1.6059 0.0000 0.0000 0.0000 160 ILE A CD1 
1092 N N   . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A N   
1093 C CA  . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A CA  
1094 C C   . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A C   
1095 O O   . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A O   
1096 C CB  . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A CB  
1097 C CG  . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A CG  
1098 C CD  . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A CD  
1099 N NE  . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A NE  
1100 C CZ  . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A CZ  
1101 N NH1 . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A NH1 
1102 N NH2 . ARG A 162 ? 1.6736 1.6736 1.6736 0.0000 0.0000 0.0000 161 ARG A NH2 
1103 N N   . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A N   
1104 C CA  . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A CA  
1105 C C   . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A C   
1106 O O   . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A O   
1107 C CB  . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A CB  
1108 C CG  . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A CG  
1109 C CD  . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A CD  
1110 O OE1 . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A OE1 
1111 N NE2 . GLN A 163 ? 1.7314 1.7314 1.7314 0.0000 0.0000 0.0000 162 GLN A NE2 
1112 N N   . SER A 164 ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 163 SER A N   
1113 C CA  . SER A 164 ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 163 SER A CA  
1114 C C   . SER A 164 ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 163 SER A C   
1115 O O   . SER A 164 ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 163 SER A O   
1116 C CB  . SER A 164 ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 163 SER A CB  
1117 O OG  . SER A 164 ? 1.8480 1.8480 1.8480 0.0000 0.0000 0.0000 163 SER A OG  
1118 N N   . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A N   
1119 C CA  . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A CA  
1120 C C   . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A C   
1121 O O   . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A O   
1122 C CB  . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A CB  
1123 C CG  . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A CG  
1124 C CD  . PRO A 165 ? 1.8895 1.8895 1.8895 0.0000 0.0000 0.0000 164 PRO A CD  
1125 N N   . SER A 166 ? 1.9182 1.9182 1.9182 0.0000 0.0000 0.0000 165 SER A N   
1126 C CA  . SER A 166 ? 1.9182 1.9182 1.9182 0.0000 0.0000 0.0000 165 SER A CA  
1127 C C   . SER A 166 ? 1.9182 1.9182 1.9182 0.0000 0.0000 0.0000 165 SER A C   
1128 O O   . SER A 166 ? 1.9182 1.9182 1.9182 0.0000 0.0000 0.0000 165 SER A O   
1129 C CB  . SER A 166 ? 1.9182 1.9182 1.9182 0.0000 0.0000 0.0000 165 SER A CB  
1130 O OG  . SER A 166 ? 1.9182 1.9182 1.9182 0.0000 0.0000 0.0000 165 SER A OG  
1131 N N   . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A N   
1132 C CA  . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A CA  
1133 C C   . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A C   
1134 O O   . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A O   
1135 C CB  . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A CB  
1136 C CG  . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A CG  
1137 C CD  . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A CD  
1138 N NE  . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A NE  
1139 C CZ  . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A CZ  
1140 N NH1 . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A NH1 
1141 N NH2 . ARG A 167 ? 1.8907 1.8907 1.8907 0.0000 0.0000 0.0000 166 ARG A NH2 
1142 N N   . GLY A 168 ? 1.7959 1.7959 1.7959 0.0000 0.0000 0.0000 167 GLY A N   
1143 C CA  . GLY A 168 ? 1.7959 1.7959 1.7959 0.0000 0.0000 0.0000 167 GLY A CA  
1144 C C   . GLY A 168 ? 1.7959 1.7959 1.7959 0.0000 0.0000 0.0000 167 GLY A C   
1145 O O   . GLY A 168 ? 1.7959 1.7959 1.7959 0.0000 0.0000 0.0000 167 GLY A O   
1146 N N   . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A N   
1147 C CA  . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A CA  
1148 C C   . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A C   
1149 O O   . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A O   
1150 C CB  . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A CB  
1151 C CG  . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A CG  
1152 C CD1 . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A CD1 
1153 C CD2 . LEU A 169 ? 1.5847 1.5847 1.5847 0.0000 0.0000 0.0000 168 LEU A CD2 
1154 N N   . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A N   
1155 C CA  . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A CA  
1156 C C   . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A C   
1157 O O   . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A O   
1158 C CB  . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A CB  
1159 C CG  . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A CG  
1160 C CD  . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A CD  
1161 O OE1 . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A OE1 
1162 O OE2 . GLU A 170 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 169 GLU A OE2 
1163 N N   . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A N   
1164 C CA  . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CA  
1165 C C   . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A C   
1166 O O   . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A O   
1167 C CB  . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CB  
1168 C CG  . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CG  
1169 C CD1 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CD1 
1170 C CD2 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CD2 
1171 N NE1 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A NE1 
1172 C CE2 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CE2 
1173 C CE3 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CE3 
1174 C CZ2 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CZ2 
1175 C CZ3 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CZ3 
1176 C CH2 . TRP A 171 ? 1.5180 1.5180 1.5180 0.0000 0.0000 0.0000 170 TRP A CH2 
1177 N N   . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A N   
1178 C CA  . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A CA  
1179 C C   . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A C   
1180 O O   . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A O   
1181 C CB  . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A CB  
1182 C CG  . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A CG  
1183 C CD1 . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A CD1 
1184 C CD2 . LEU A 172 ? 1.5845 1.5845 1.5845 0.0000 0.0000 0.0000 171 LEU A CD2 
1185 N N   . GLY A 173 ? 1.5654 1.5654 1.5654 0.0000 0.0000 0.0000 172 GLY A N   
1186 C CA  . GLY A 173 ? 1.5654 1.5654 1.5654 0.0000 0.0000 0.0000 172 GLY A CA  
1187 C C   . GLY A 173 ? 1.5654 1.5654 1.5654 0.0000 0.0000 0.0000 172 GLY A C   
1188 O O   . GLY A 173 ? 1.5654 1.5654 1.5654 0.0000 0.0000 0.0000 172 GLY A O   
1189 N N   . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A N   
1190 C CA  . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A CA  
1191 C C   . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A C   
1192 O O   . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A O   
1193 C CB  . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A CB  
1194 C CG  . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A CG  
1195 C CD  . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A CD  
1196 N NE  . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A NE  
1197 C CZ  . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A CZ  
1198 N NH1 . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A NH1 
1199 N NH2 . ARG A 174 ? 1.4577 1.4577 1.4577 0.0000 0.0000 0.0000 173 ARG A NH2 
1200 N N   . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A N   
1201 C CA  . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A CA  
1202 C C   . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A C   
1203 O O   . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A O   
1204 C CB  . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A CB  
1205 O OG1 . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A OG1 
1206 C CG2 . THR A 175 ? 1.5267 1.5267 1.5267 0.0000 0.0000 0.0000 174 THR A CG2 
1207 N N   . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A N   
1208 C CA  . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CA  
1209 C C   . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A C   
1210 O O   . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A O   
1211 C CB  . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CB  
1212 C CG  . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CG  
1213 C CD1 . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CD1 
1214 C CD2 . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CD2 
1215 C CE1 . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CE1 
1216 C CE2 . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CE2 
1217 C CZ  . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A CZ  
1218 O OH  . TYR A 176 ? 1.5652 1.5652 1.5652 0.0000 0.0000 0.0000 175 TYR A OH  
1219 N N   . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A N   
1220 C CA  . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CA  
1221 C C   . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A C   
1222 O O   . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A O   
1223 C CB  . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CB  
1224 C CG  . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CG  
1225 C CD1 . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CD1 
1226 C CD2 . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CD2 
1227 C CE1 . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CE1 
1228 C CE2 . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CE2 
1229 C CZ  . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A CZ  
1230 O OH  . TYR A 177 ? 1.6500 1.6500 1.6500 0.0000 0.0000 0.0000 176 TYR A OH  
1231 N N   . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A N   
1232 C CA  . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A CA  
1233 C C   . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A C   
1234 O O   . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A O   
1235 C CB  . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A CB  
1236 C CG  . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A CG  
1237 C CD  . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A CD  
1238 N NE  . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A NE  
1239 C CZ  . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A CZ  
1240 N NH1 . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A NH1 
1241 N NH2 . ARG A 178 ? 1.6176 1.6176 1.6176 0.0000 0.0000 0.0000 177 ARG A NH2 
1242 N N   . SER A 179 ? 1.7182 1.7182 1.7182 0.0000 0.0000 0.0000 178 SER A N   
1243 C CA  . SER A 179 ? 1.7182 1.7182 1.7182 0.0000 0.0000 0.0000 178 SER A CA  
1244 C C   . SER A 179 ? 1.7182 1.7182 1.7182 0.0000 0.0000 0.0000 178 SER A C   
1245 O O   . SER A 179 ? 1.7182 1.7182 1.7182 0.0000 0.0000 0.0000 178 SER A O   
1246 C CB  . SER A 179 ? 1.7182 1.7182 1.7182 0.0000 0.0000 0.0000 178 SER A CB  
1247 O OG  . SER A 179 ? 1.7182 1.7182 1.7182 0.0000 0.0000 0.0000 178 SER A OG  
1248 N N   . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A N   
1249 C CA  . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A CA  
1250 C C   . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A C   
1251 O O   . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A O   
1252 C CB  . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A CB  
1253 C CG  . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A CG  
1254 C CD  . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A CD  
1255 C CE  . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A CE  
1256 N NZ  . LYS A 180 ? 1.7172 1.7172 1.7172 0.0000 0.0000 0.0000 179 LYS A NZ  
1257 N N   . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A N   
1258 C CA  . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CA  
1259 C C   . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A C   
1260 O O   . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A O   
1261 C CB  . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CB  
1262 C CG  . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CG  
1263 C CD1 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CD1 
1264 C CD2 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CD2 
1265 N NE1 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A NE1 
1266 C CE2 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CE2 
1267 C CE3 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CE3 
1268 C CZ2 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CZ2 
1269 C CZ3 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CZ3 
1270 C CH2 . TRP A 181 ? 1.6558 1.6558 1.6558 0.0000 0.0000 0.0000 180 TRP A CH2 
1271 N N   . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A N   
1272 C CA  . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CA  
1273 C C   . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A C   
1274 O O   . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A O   
1275 C CB  . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CB  
1276 C CG  . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CG  
1277 C CD1 . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CD1 
1278 C CD2 . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CD2 
1279 C CE1 . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CE1 
1280 C CE2 . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CE2 
1281 C CZ  . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A CZ  
1282 O OH  . TYR A 182 ? 1.6271 1.6271 1.6271 0.0000 0.0000 0.0000 181 TYR A OH  
1283 N N   . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A N   
1284 C CA  . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A CA  
1285 C C   . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A C   
1286 O O   . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A O   
1287 C CB  . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A CB  
1288 C CG  . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A CG  
1289 O OD1 . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A OD1 
1290 N ND2 . ASN A 183 ? 1.6245 1.6245 1.6245 0.0000 0.0000 0.0000 182 ASN A ND2 
1291 N N   . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A N   
1292 C CA  . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A CA  
1293 C C   . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A C   
1294 O O   . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A O   
1295 C CB  . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A CB  
1296 C CG  . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A CG  
1297 O OD1 . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A OD1 
1298 O OD2 . ASP A 184 ? 1.6259 1.6259 1.6259 0.0000 0.0000 0.0000 183 ASP A OD2 
1299 N N   . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A N   
1300 C CA  . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CA  
1301 C C   . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A C   
1302 O O   . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A O   
1303 C CB  . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CB  
1304 C CG  . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CG  
1305 C CD1 . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CD1 
1306 C CD2 . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CD2 
1307 C CE1 . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CE1 
1308 C CE2 . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CE2 
1309 C CZ  . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A CZ  
1310 O OH  . TYR A 185 ? 1.6787 1.6787 1.6787 0.0000 0.0000 0.0000 184 TYR A OH  
1311 N N   . ALA A 186 ? 1.8018 1.8018 1.8018 0.0000 0.0000 0.0000 185 ALA A N   
1312 C CA  . ALA A 186 ? 1.8018 1.8018 1.8018 0.0000 0.0000 0.0000 185 ALA A CA  
1313 C C   . ALA A 186 ? 1.8018 1.8018 1.8018 0.0000 0.0000 0.0000 185 ALA A C   
1314 O O   . ALA A 186 ? 1.8018 1.8018 1.8018 0.0000 0.0000 0.0000 185 ALA A O   
1315 C CB  . ALA A 186 ? 1.8018 1.8018 1.8018 0.0000 0.0000 0.0000 185 ALA A CB  
1316 N N   . GLY A 187 ? 1.9080 1.9080 1.9080 0.0000 0.0000 0.0000 186 GLY A N   
1317 C CA  . GLY A 187 ? 1.9080 1.9080 1.9080 0.0000 0.0000 0.0000 186 GLY A CA  
1318 C C   . GLY A 187 ? 1.9080 1.9080 1.9080 0.0000 0.0000 0.0000 186 GLY A C   
1319 O O   . GLY A 187 ? 1.9080 1.9080 1.9080 0.0000 0.0000 0.0000 186 GLY A O   
1320 N N   . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A N   
1321 C CA  . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A CA  
1322 C C   . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A C   
1323 O O   . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A O   
1324 C CB  . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A CB  
1325 O OG1 . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A OG1 
1326 C CG2 . THR A 188 ? 1.9096 1.9096 1.9096 0.0000 0.0000 0.0000 187 THR A CG2 
1327 N N   . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A N   
1328 C CA  . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A CA  
1329 C C   . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A C   
1330 O O   . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A O   
1331 C CB  . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A CB  
1332 C CG1 . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A CG1 
1333 C CG2 . VAL A 189 ? 1.9179 1.9179 1.9179 0.0000 0.0000 0.0000 188 VAL A CG2 
1334 N N   . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A N   
1335 C CA  . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A CA  
1336 C C   . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A C   
1337 O O   . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A O   
1338 C CB  . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A CB  
1339 C CG  . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A CG  
1340 C CD  . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A CD  
1341 C CE  . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A CE  
1342 N NZ  . LYS A 190 ? 1.9268 1.9268 1.9268 0.0000 0.0000 0.0000 189 LYS A NZ  
1343 N N   . SER A 191 ? 1.9653 1.9653 1.9653 0.0000 0.0000 0.0000 190 SER A N   
1344 C CA  . SER A 191 ? 1.9653 1.9653 1.9653 0.0000 0.0000 0.0000 190 SER A CA  
1345 C C   . SER A 191 ? 1.9653 1.9653 1.9653 0.0000 0.0000 0.0000 190 SER A C   
1346 O O   . SER A 191 ? 1.9653 1.9653 1.9653 0.0000 0.0000 0.0000 190 SER A O   
1347 C CB  . SER A 191 ? 1.9653 1.9653 1.9653 0.0000 0.0000 0.0000 190 SER A CB  
1348 O OG  . SER A 191 ? 1.9653 1.9653 1.9653 0.0000 0.0000 0.0000 190 SER A OG  
1349 N N   . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A N   
1350 C CA  . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A CA  
1351 C C   . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A C   
1352 O O   . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A O   
1353 C CB  . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A CB  
1354 C CG  . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A CG  
1355 C CD  . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A CD  
1356 N NE  . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A NE  
1357 C CZ  . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A CZ  
1358 N NH1 . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A NH1 
1359 N NH2 . ARG A 192 ? 1.9750 1.9750 1.9750 0.0000 0.0000 0.0000 191 ARG A NH2 
1360 N N   . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A N   
1361 C CA  . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A CA  
1362 C C   . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A C   
1363 O O   . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A O   
1364 C CB  . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A CB  
1365 C CG1 . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A CG1 
1366 C CG2 . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A CG2 
1367 C CD1 . ILE A 193 ? 1.8770 1.8770 1.8770 0.0000 0.0000 0.0000 192 ILE A CD1 
1368 N N   . ALA A 194 ? 1.8502 1.8502 1.8502 0.0000 0.0000 0.0000 193 ALA A N   
1369 C CA  . ALA A 194 ? 1.8502 1.8502 1.8502 0.0000 0.0000 0.0000 193 ALA A CA  
1370 C C   . ALA A 194 ? 1.8502 1.8502 1.8502 0.0000 0.0000 0.0000 193 ALA A C   
1371 O O   . ALA A 194 ? 1.8502 1.8502 1.8502 0.0000 0.0000 0.0000 193 ALA A O   
1372 C CB  . ALA A 194 ? 1.8502 1.8502 1.8502 0.0000 0.0000 0.0000 193 ALA A CB  
1373 N N   . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A N   
1374 C CA  . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A CA  
1375 C C   . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A C   
1376 O O   . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A O   
1377 C CB  . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A CB  
1378 C CG1 . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A CG1 
1379 C CG2 . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A CG2 
1380 C CD1 . ILE A 195 ? 1.8116 1.8116 1.8116 0.0000 0.0000 0.0000 194 ILE A CD1 
1381 N N   . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A N   
1382 C CA  . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A CA  
1383 C C   . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A C   
1384 O O   . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A O   
1385 C CB  . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A CB  
1386 C CG  . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A CG  
1387 O OD1 . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A OD1 
1388 N ND2 . ASN A 196 ? 1.8684 1.8684 1.8684 0.0000 0.0000 0.0000 195 ASN A ND2 
1389 N N   . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A N   
1390 C CA  . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A CA  
1391 C C   . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A C   
1392 O O   . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A O   
1393 C CB  . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A CB  
1394 C CG  . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A CG  
1395 C CD  . PRO A 197 ? 1.8375 1.8375 1.8375 0.0000 0.0000 0.0000 196 PRO A CD  
1396 N N   . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A N   
1397 C CA  . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A CA  
1398 C C   . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A C   
1399 O O   . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A O   
1400 C CB  . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A CB  
1401 C CG  . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A CG  
1402 O OD1 . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A OD1 
1403 O OD2 . ASP A 198 ? 1.9353 1.9353 1.9353 0.0000 0.0000 0.0000 197 ASP A OD2 
1404 N N   . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A N   
1405 C CA  . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A CA  
1406 C C   . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A C   
1407 O O   . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A O   
1408 C CB  . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A CB  
1409 O OG1 . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A OG1 
1410 C CG2 . THR A 199 ? 1.9338 1.9338 1.9338 0.0000 0.0000 0.0000 198 THR A CG2 
1411 N N   . SER A 200 ? 1.9706 1.9706 1.9706 0.0000 0.0000 0.0000 199 SER A N   
1412 C CA  . SER A 200 ? 1.9706 1.9706 1.9706 0.0000 0.0000 0.0000 199 SER A CA  
1413 C C   . SER A 200 ? 1.9706 1.9706 1.9706 0.0000 0.0000 0.0000 199 SER A C   
1414 O O   . SER A 200 ? 1.9706 1.9706 1.9706 0.0000 0.0000 0.0000 199 SER A O   
1415 C CB  . SER A 200 ? 1.9706 1.9706 1.9706 0.0000 0.0000 0.0000 199 SER A CB  
1416 O OG  . SER A 200 ? 1.9706 1.9706 1.9706 0.0000 0.0000 0.0000 199 SER A OG  
1417 N N   . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A N   
1418 C CA  . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A CA  
1419 C C   . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A C   
1420 O O   . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A O   
1421 C CB  . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A CB  
1422 C CG  . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A CG  
1423 C CD  . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A CD  
1424 C CE  . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A CE  
1425 N NZ  . LYS A 201 ? 1.9552 1.9552 1.9552 0.0000 0.0000 0.0000 200 LYS A NZ  
1426 N N   . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A N   
1427 C CA  . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A CA  
1428 C C   . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A C   
1429 O O   . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A O   
1430 C CB  . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A CB  
1431 C CG  . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A CG  
1432 O OD1 . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A OD1 
1433 N ND2 . ASN A 202 ? 1.8683 1.8683 1.8683 0.0000 0.0000 0.0000 201 ASN A ND2 
1434 N N   . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A N   
1435 C CA  . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A CA  
1436 C C   . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A C   
1437 O O   . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A O   
1438 C CB  . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A CB  
1439 C CG  . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A CG  
1440 C CD  . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A CD  
1441 O OE1 . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A OE1 
1442 N NE2 . GLN A 203 ? 1.8655 1.8655 1.8655 0.0000 0.0000 0.0000 202 GLN A NE2 
1443 N N   . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A N   
1444 C CA  . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CA  
1445 C C   . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A C   
1446 O O   . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A O   
1447 C CB  . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CB  
1448 C CG  . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CG  
1449 C CD1 . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CD1 
1450 C CD2 . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CD2 
1451 C CE1 . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CE1 
1452 C CE2 . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CE2 
1453 C CZ  . PHE A 204 ? 1.7521 1.7521 1.7521 0.0000 0.0000 0.0000 203 PHE A CZ  
1454 N N   . SER A 205 ? 1.8464 1.8464 1.8464 0.0000 0.0000 0.0000 204 SER A N   
1455 C CA  . SER A 205 ? 1.8464 1.8464 1.8464 0.0000 0.0000 0.0000 204 SER A CA  
1456 C C   . SER A 205 ? 1.8464 1.8464 1.8464 0.0000 0.0000 0.0000 204 SER A C   
1457 O O   . SER A 205 ? 1.8464 1.8464 1.8464 0.0000 0.0000 0.0000 204 SER A O   
1458 C CB  . SER A 205 ? 1.8464 1.8464 1.8464 0.0000 0.0000 0.0000 204 SER A CB  
1459 O OG  . SER A 205 ? 1.8464 1.8464 1.8464 0.0000 0.0000 0.0000 204 SER A OG  
1460 N N   . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A N   
1461 C CA  . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A CA  
1462 C C   . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A C   
1463 O O   . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A O   
1464 C CB  . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A CB  
1465 C CG  . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A CG  
1466 C CD1 . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A CD1 
1467 C CD2 . LEU A 206 ? 1.8160 1.8160 1.8160 0.0000 0.0000 0.0000 205 LEU A CD2 
1468 N N   . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A N   
1469 C CA  . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A CA  
1470 C C   . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A C   
1471 O O   . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A O   
1472 C CB  . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A CB  
1473 C CG  . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A CG  
1474 N ND1 . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A ND1 
1475 C CD2 . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A CD2 
1476 C CE1 . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A CE1 
1477 N NE2 . HIS A 207 ? 1.8906 1.8906 1.8906 0.0000 0.0000 0.0000 206 HIS A NE2 
1478 N N   . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A N   
1479 C CA  . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A CA  
1480 C C   . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A C   
1481 O O   . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A O   
1482 C CB  . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A CB  
1483 C CG  . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A CG  
1484 C CD1 . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A CD1 
1485 C CD2 . LEU A 208 ? 2.0050 2.0050 2.0050 0.0000 0.0000 0.0000 207 LEU A CD2 
1486 N N   . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A N   
1487 C CA  . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A CA  
1488 C C   . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A C   
1489 O O   . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A O   
1490 C CB  . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A CB  
1491 C CG  . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A CG  
1492 O OD1 . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A OD1 
1493 N ND2 . ASN A 209 ? 2.1183 2.1183 2.1183 0.0000 0.0000 0.0000 208 ASN A ND2 
1494 N N   . SER A 210 ? 2.1013 2.1013 2.1013 0.0000 0.0000 0.0000 209 SER A N   
1495 C CA  . SER A 210 ? 2.1013 2.1013 2.1013 0.0000 0.0000 0.0000 209 SER A CA  
1496 C C   . SER A 210 ? 2.1013 2.1013 2.1013 0.0000 0.0000 0.0000 209 SER A C   
1497 O O   . SER A 210 ? 2.1013 2.1013 2.1013 0.0000 0.0000 0.0000 209 SER A O   
1498 C CB  . SER A 210 ? 2.1013 2.1013 2.1013 0.0000 0.0000 0.0000 209 SER A CB  
1499 O OG  . SER A 210 ? 2.1013 2.1013 2.1013 0.0000 0.0000 0.0000 209 SER A OG  
1500 N N   . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A N   
1501 C CA  . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A CA  
1502 C C   . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A C   
1503 O O   . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A O   
1504 C CB  . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A CB  
1505 C CG1 . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A CG1 
1506 C CG2 . VAL A 211 ? 2.1496 2.1496 2.1496 0.0000 0.0000 0.0000 210 VAL A CG2 
1507 N N   . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A N   
1508 C CA  . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A CA  
1509 C C   . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A C   
1510 O O   . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A O   
1511 C CB  . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A CB  
1512 O OG1 . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A OG1 
1513 C CG2 . THR A 212 ? 2.1430 2.1430 2.1430 0.0000 0.0000 0.0000 211 THR A CG2 
1514 N N   . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A N   
1515 C CA  . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A CA  
1516 C C   . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A C   
1517 O O   . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A O   
1518 C CB  . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A CB  
1519 C CG  . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A CG  
1520 C CD  . PRO A 213 ? 2.1129 2.1129 2.1129 0.0000 0.0000 0.0000 212 PRO A CD  
1521 N N   . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A N   
1522 C CA  . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A CA  
1523 C C   . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A C   
1524 O O   . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A O   
1525 C CB  . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A CB  
1526 C CG  . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A CG  
1527 C CD  . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A CD  
1528 O OE1 . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A OE1 
1529 O OE2 . GLU A 214 ? 2.1220 2.1220 2.1220 0.0000 0.0000 0.0000 213 GLU A OE2 
1530 N N   . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A N   
1531 C CA  . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A CA  
1532 C C   . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A C   
1533 O O   . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A O   
1534 C CB  . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A CB  
1535 C CG  . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A CG  
1536 O OD1 . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A OD1 
1537 O OD2 . ASP A 215 ? 2.0907 2.0907 2.0907 0.0000 0.0000 0.0000 214 ASP A OD2 
1538 N N   . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A N   
1539 C CA  . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A CA  
1540 C C   . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A C   
1541 O O   . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A O   
1542 C CB  . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A CB  
1543 O OG1 . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A OG1 
1544 C CG2 . THR A 216 ? 2.0848 2.0848 2.0848 0.0000 0.0000 0.0000 215 THR A CG2 
1545 N N   . ALA A 217 ? 1.9071 1.9071 1.9071 0.0000 0.0000 0.0000 216 ALA A N   
1546 C CA  . ALA A 217 ? 1.9071 1.9071 1.9071 0.0000 0.0000 0.0000 216 ALA A CA  
1547 C C   . ALA A 217 ? 1.9071 1.9071 1.9071 0.0000 0.0000 0.0000 216 ALA A C   
1548 O O   . ALA A 217 ? 1.9071 1.9071 1.9071 0.0000 0.0000 0.0000 216 ALA A O   
1549 C CB  . ALA A 217 ? 1.9071 1.9071 1.9071 0.0000 0.0000 0.0000 216 ALA A CB  
1550 N N   . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A N   
1551 C CA  . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A CA  
1552 C C   . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A C   
1553 O O   . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A O   
1554 C CB  . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A CB  
1555 C CG1 . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A CG1 
1556 C CG2 . VAL A 218 ? 1.7713 1.7713 1.7713 0.0000 0.0000 0.0000 217 VAL A CG2 
1557 N N   . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A N   
1558 C CA  . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CA  
1559 C C   . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A C   
1560 O O   . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A O   
1561 C CB  . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CB  
1562 C CG  . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CG  
1563 C CD1 . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CD1 
1564 C CD2 . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CD2 
1565 C CE1 . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CE1 
1566 C CE2 . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CE2 
1567 C CZ  . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A CZ  
1568 O OH  . TYR A 219 ? 1.7247 1.7247 1.7247 0.0000 0.0000 0.0000 218 TYR A OH  
1569 N N   . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A N   
1570 C CA  . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CA  
1571 C C   . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A C   
1572 O O   . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A O   
1573 C CB  . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CB  
1574 C CG  . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CG  
1575 C CD1 . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CD1 
1576 C CD2 . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CD2 
1577 C CE1 . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CE1 
1578 C CE2 . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CE2 
1579 C CZ  . PHE A 220 ? 1.6273 1.6273 1.6273 0.0000 0.0000 0.0000 219 PHE A CZ  
1580 N N   . CYS A 221 ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 220 CYS A N   
1581 C CA  . CYS A 221 ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 220 CYS A CA  
1582 C C   . CYS A 221 ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 220 CYS A C   
1583 O O   . CYS A 221 ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 220 CYS A O   
1584 C CB  . CYS A 221 ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 220 CYS A CB  
1585 S SG  . CYS A 221 ? 1.6307 1.6307 1.6307 0.0000 0.0000 0.0000 220 CYS A SG  
1586 N N   . ALA A 222 ? 1.4285 1.4285 1.4285 0.0000 0.0000 0.0000 221 ALA A N   
1587 C CA  . ALA A 222 ? 1.4285 1.4285 1.4285 0.0000 0.0000 0.0000 221 ALA A CA  
1588 C C   . ALA A 222 ? 1.4285 1.4285 1.4285 0.0000 0.0000 0.0000 221 ALA A C   
1589 O O   . ALA A 222 ? 1.4285 1.4285 1.4285 0.0000 0.0000 0.0000 221 ALA A O   
1590 C CB  . ALA A 222 ? 1.4285 1.4285 1.4285 0.0000 0.0000 0.0000 221 ALA A CB  
1591 N N   . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A N   
1592 C CA  . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A CA  
1593 C C   . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A C   
1594 O O   . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A O   
1595 C CB  . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A CB  
1596 C CG  . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A CG  
1597 C CD  . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A CD  
1598 N NE  . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A NE  
1599 C CZ  . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A CZ  
1600 N NH1 . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A NH1 
1601 N NH2 . ARG A 223 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 222 ARG A NH2 
1602 N N   . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A N   
1603 C CA  . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A CA  
1604 C C   . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A C   
1605 O O   . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A O   
1606 C CB  . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A CB  
1607 C CG1 . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A CG1 
1608 C CG2 . VAL A 224 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 223 VAL A CG2 
1609 N N   . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A N   
1610 C CA  . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A CA  
1611 C C   . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A C   
1612 O O   . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A O   
1613 C CB  . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A CB  
1614 C CG1 . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A CG1 
1615 C CG2 . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A CG2 
1616 C CD1 . ILE A 225 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 224 ILE A CD1 
1617 N N   . SER A 226 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 225 SER A N   
1618 C CA  . SER A 226 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 225 SER A CA  
1619 C C   . SER A 226 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 225 SER A C   
1620 O O   . SER A 226 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 225 SER A O   
1621 C CB  . SER A 226 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 225 SER A CB  
1622 O OG  . SER A 226 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 225 SER A OG  
1623 N N   . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A N   
1624 C CA  . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A CA  
1625 C C   . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A C   
1626 O O   . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A O   
1627 C CB  . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A CB  
1628 C CG1 . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A CG1 
1629 C CG2 . VAL A 227 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 226 VAL A CG2 
1630 N N   . ALA A 228 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 227 ALA A N   
1631 C CA  . ALA A 228 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 227 ALA A CA  
1632 C C   . ALA A 228 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 227 ALA A C   
1633 O O   . ALA A 228 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 227 ALA A O   
1634 C CB  . ALA A 228 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 227 ALA A CB  
1635 N N   . GLY A 229 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 228 GLY A N   
1636 C CA  . GLY A 229 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 228 GLY A CA  
1637 C C   . GLY A 229 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 228 GLY A C   
1638 O O   . GLY A 229 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 228 GLY A O   
1639 N N   . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A N   
1640 C CA  . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CA  
1641 C C   . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A C   
1642 O O   . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A O   
1643 C CB  . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CB  
1644 C CG  . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CG  
1645 C CD1 . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CD1 
1646 C CD2 . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CD2 
1647 C CE1 . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CE1 
1648 C CE2 . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CE2 
1649 C CZ  . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A CZ  
1650 O OH  . TYR A 230 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 229 TYR A OH  
1651 N N   . ALA A 231 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 230 ALA A N   
1652 C CA  . ALA A 231 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 230 ALA A CA  
1653 C C   . ALA A 231 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 230 ALA A C   
1654 O O   . ALA A 231 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 230 ALA A O   
1655 C CB  . ALA A 231 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 230 ALA A CB  
1656 N N   . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A N   
1657 C CA  . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CA  
1658 C C   . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A C   
1659 O O   . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A O   
1660 C CB  . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CB  
1661 C CG  . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CG  
1662 C CD1 . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CD1 
1663 C CD2 . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CD2 
1664 C CE1 . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CE1 
1665 C CE2 . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CE2 
1666 C CZ  . PHE A 232 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 231 PHE A CZ  
1667 N N   . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A N   
1668 C CA  . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A CA  
1669 C C   . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A C   
1670 O O   . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A O   
1671 C CB  . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A CB  
1672 C CG  . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A CG  
1673 O OD1 . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A OD1 
1674 O OD2 . ASP A 233 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 232 ASP A OD2 
1675 N N   . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A N   
1676 C CA  . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A CA  
1677 C C   . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A C   
1678 O O   . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A O   
1679 C CB  . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A CB  
1680 C CG1 . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A CG1 
1681 C CG2 . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A CG2 
1682 C CD1 . ILE A 234 ? 1.3698 1.3698 1.3698 0.0000 0.0000 0.0000 233 ILE A CD1 
1683 N N   . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A N   
1684 C CA  . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CA  
1685 C C   . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A C   
1686 O O   . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A O   
1687 C CB  . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CB  
1688 C CG  . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CG  
1689 C CD1 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CD1 
1690 C CD2 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CD2 
1691 N NE1 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A NE1 
1692 C CE2 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CE2 
1693 C CE3 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CE3 
1694 C CZ2 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CZ2 
1695 C CZ3 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CZ3 
1696 C CH2 . TRP A 235 ? 1.4054 1.4054 1.4054 0.0000 0.0000 0.0000 234 TRP A CH2 
1697 N N   . GLY A 236 ? 1.5889 1.5889 1.5889 0.0000 0.0000 0.0000 235 GLY A N   
1698 C CA  . GLY A 236 ? 1.5889 1.5889 1.5889 0.0000 0.0000 0.0000 235 GLY A CA  
1699 C C   . GLY A 236 ? 1.5889 1.5889 1.5889 0.0000 0.0000 0.0000 235 GLY A C   
1700 O O   . GLY A 236 ? 1.5889 1.5889 1.5889 0.0000 0.0000 0.0000 235 GLY A O   
1701 N N   . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A N   
1702 C CA  . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A CA  
1703 C C   . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A C   
1704 O O   . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A O   
1705 C CB  . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A CB  
1706 C CG  . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A CG  
1707 C CD  . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A CD  
1708 O OE1 . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A OE1 
1709 N NE2 . GLN A 237 ? 1.7351 1.7351 1.7351 0.0000 0.0000 0.0000 236 GLN A NE2 
1710 N N   . GLY A 238 ? 1.7649 1.7649 1.7649 0.0000 0.0000 0.0000 237 GLY A N   
1711 C CA  . GLY A 238 ? 1.7649 1.7649 1.7649 0.0000 0.0000 0.0000 237 GLY A CA  
1712 C C   . GLY A 238 ? 1.7649 1.7649 1.7649 0.0000 0.0000 0.0000 237 GLY A C   
1713 O O   . GLY A 238 ? 1.7649 1.7649 1.7649 0.0000 0.0000 0.0000 237 GLY A O   
1714 N N   . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A N   
1715 C CA  . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A CA  
1716 C C   . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A C   
1717 O O   . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A O   
1718 C CB  . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A CB  
1719 O OG1 . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A OG1 
1720 C CG2 . THR A 239 ? 1.7999 1.7999 1.7999 0.0000 0.0000 0.0000 238 THR A CG2 
1721 N N   . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A N   
1722 C CA  . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A CA  
1723 C C   . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A C   
1724 O O   . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A O   
1725 C CB  . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A CB  
1726 C CG  . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A CG  
1727 S SD  . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A SD  
1728 C CE  . MET A 240 ? 1.9106 1.9106 1.9106 0.0000 0.0000 0.0000 239 MET A CE  
1729 N N   . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A N   
1730 C CA  . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A CA  
1731 C C   . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A C   
1732 O O   . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A O   
1733 C CB  . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A CB  
1734 C CG1 . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A CG1 
1735 C CG2 . VAL A 241 ? 1.9999 1.9999 1.9999 0.0000 0.0000 0.0000 240 VAL A CG2 
1736 N N   . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A N   
1737 C CA  . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A CA  
1738 C C   . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A C   
1739 O O   . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A O   
1740 C CB  . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A CB  
1741 O OG1 . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A OG1 
1742 C CG2 . THR A 242 ? 2.1244 2.1244 2.1244 0.0000 0.0000 0.0000 241 THR A CG2 
1743 N N   . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A N   
1744 C CA  . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A CA  
1745 C C   . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A C   
1746 O O   . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A O   
1747 C CB  . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A CB  
1748 C CG1 . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A CG1 
1749 C CG2 . VAL A 243 ? 2.1493 2.1493 2.1493 0.0000 0.0000 0.0000 242 VAL A CG2 
1750 N N   . SER A 244 ? 2.1934 2.1934 2.1934 0.0000 0.0000 0.0000 243 SER A N   
1751 C CA  . SER A 244 ? 2.1934 2.1934 2.1934 0.0000 0.0000 0.0000 243 SER A CA  
1752 C C   . SER A 244 ? 2.1934 2.1934 2.1934 0.0000 0.0000 0.0000 243 SER A C   
1753 O O   . SER A 244 ? 2.1934 2.1934 2.1934 0.0000 0.0000 0.0000 243 SER A O   
1754 C CB  . SER A 244 ? 2.1934 2.1934 2.1934 0.0000 0.0000 0.0000 243 SER A CB  
1755 O OG  . SER A 244 ? 2.1934 2.1934 2.1934 0.0000 0.0000 0.0000 243 SER A OG  
1756 N N   . SER A 245 ? 2.2258 2.2258 2.2258 0.0000 0.0000 0.0000 244 SER A N   
1757 C CA  . SER A 245 ? 2.2258 2.2258 2.2258 0.0000 0.0000 0.0000 244 SER A CA  
1758 C C   . SER A 245 ? 2.2258 2.2258 2.2258 0.0000 0.0000 0.0000 244 SER A C   
1759 O O   . SER A 245 ? 2.2258 2.2258 2.2258 0.0000 0.0000 0.0000 244 SER A O   
1760 C CB  . SER A 245 ? 2.2258 2.2258 2.2258 0.0000 0.0000 0.0000 244 SER A CB  
1761 O OG  . SER A 245 ? 2.2258 2.2258 2.2258 0.0000 0.0000 0.0000 244 SER A OG  
1762 N N   . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B N   
1763 C CA  . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B CA  
1764 C C   . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B C   
1765 O O   . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B O   
1766 C CB  . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B CB  
1767 C CG  . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B CG  
1768 O OD1 . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B OD1 
1769 N ND2 . ASN B 320 ? 1.8848 1.8848 1.8848 0.0000 0.0000 0.0000 331 ASN B ND2 
1770 N N   . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B N   
1771 C CA  . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B CA  
1772 C C   . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B C   
1773 O O   . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B O   
1774 C CB  . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B CB  
1775 C CG1 . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B CG1 
1776 C CG2 . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B CG2 
1777 C CD1 . ILE B 321 ? 1.8412 1.8412 1.8412 0.0000 0.0000 0.0000 332 ILE B CD1 
1778 N N   . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B N   
1779 C CA  . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B CA  
1780 C C   . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B C   
1781 O O   . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B O   
1782 C CB  . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B CB  
1783 O OG1 . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B OG1 
1784 C CG2 . THR B 322 ? 1.8771 1.8771 1.8771 0.0000 0.0000 0.0000 333 THR B CG2 
1785 N N   . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B N   
1786 C CA  . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B CA  
1787 C C   . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B C   
1788 O O   . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B O   
1789 C CB  . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B CB  
1790 C CG  . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B CG  
1791 O OD1 . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B OD1 
1792 N ND2 . ASN B 323 ? 1.6786 1.6786 1.6786 0.0000 0.0000 0.0000 334 ASN B ND2 
1793 N N   . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B N   
1794 C CA  . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B CA  
1795 C C   . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B C   
1796 O O   . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B O   
1797 C CB  . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B CB  
1798 C CG  . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B CG  
1799 C CD1 . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B CD1 
1800 C CD2 . LEU B 324 ? 1.5536 1.5536 1.5536 0.0000 0.0000 0.0000 335 LEU B CD2 
1801 N N   . CYS B 325 ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 336 CYS B N   
1802 C CA  . CYS B 325 ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 336 CYS B CA  
1803 C C   . CYS B 325 ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 336 CYS B C   
1804 O O   . CYS B 325 ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 336 CYS B O   
1805 C CB  . CYS B 325 ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 336 CYS B CB  
1806 S SG  . CYS B 325 ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 336 CYS B SG  
1807 N N   . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B N   
1808 C CA  . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B CA  
1809 C C   . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B C   
1810 O O   . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B O   
1811 C CB  . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B CB  
1812 C CG  . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B CG  
1813 C CD  . PRO B 326 ? 1.4083 1.4083 1.4083 0.0000 0.0000 0.0000 337 PRO B CD  
1814 N N   . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B N   
1815 C CA  . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CA  
1816 C C   . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B C   
1817 O O   . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B O   
1818 C CB  . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CB  
1819 C CG  . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CG  
1820 C CD1 . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CD1 
1821 C CD2 . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CD2 
1822 C CE1 . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CE1 
1823 C CE2 . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CE2 
1824 C CZ  . PHE B 327 ? 1.3456 1.3456 1.3456 0.0000 0.0000 0.0000 338 PHE B CZ  
1825 N N   . GLY B 328 ? 1.4059 1.4059 1.4059 0.0000 0.0000 0.0000 339 GLY B N   
1826 C CA  . GLY B 328 ? 1.4059 1.4059 1.4059 0.0000 0.0000 0.0000 339 GLY B CA  
1827 C C   . GLY B 328 ? 1.4059 1.4059 1.4059 0.0000 0.0000 0.0000 339 GLY B C   
1828 O O   . GLY B 328 ? 1.4059 1.4059 1.4059 0.0000 0.0000 0.0000 339 GLY B O   
1829 N N   . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B N   
1830 C CA  . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B CA  
1831 C C   . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B C   
1832 O O   . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B O   
1833 C CB  . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B CB  
1834 C CG  . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B CG  
1835 C CD  . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B CD  
1836 O OE1 . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B OE1 
1837 O OE2 . GLU B 329 ? 1.3519 1.3519 1.3519 0.0000 0.0000 0.0000 340 GLU B OE2 
1838 N N   . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B N   
1839 C CA  . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B CA  
1840 C C   . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B C   
1841 O O   . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B O   
1842 C CB  . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B CB  
1843 C CG1 . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B CG1 
1844 C CG2 . VAL B 330 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 341 VAL B CG2 
1845 N N   . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B N   
1846 C CA  . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CA  
1847 C C   . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B C   
1848 O O   . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B O   
1849 C CB  . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CB  
1850 C CG  . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CG  
1851 C CD1 . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CD1 
1852 C CD2 . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CD2 
1853 C CE1 . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CE1 
1854 C CE2 . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CE2 
1855 C CZ  . PHE B 331 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 342 PHE B CZ  
1856 N N   . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B N   
1857 C CA  . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B CA  
1858 C C   . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B C   
1859 O O   . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B O   
1860 C CB  . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B CB  
1861 C CG  . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B CG  
1862 O OD1 . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B OD1 
1863 N ND2 . ASN B 332 ? 1.4128 1.4128 1.4128 0.0000 0.0000 0.0000 343 ASN B ND2 
1864 N N   . ALA B 333 ? 1.3931 1.3931 1.3931 0.0000 0.0000 0.0000 344 ALA B N   
1865 C CA  . ALA B 333 ? 1.3931 1.3931 1.3931 0.0000 0.0000 0.0000 344 ALA B CA  
1866 C C   . ALA B 333 ? 1.3931 1.3931 1.3931 0.0000 0.0000 0.0000 344 ALA B C   
1867 O O   . ALA B 333 ? 1.3931 1.3931 1.3931 0.0000 0.0000 0.0000 344 ALA B O   
1868 C CB  . ALA B 333 ? 1.3931 1.3931 1.3931 0.0000 0.0000 0.0000 344 ALA B CB  
1869 N N   . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B N   
1870 C CA  . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B CA  
1871 C C   . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B C   
1872 O O   . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B O   
1873 C CB  . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B CB  
1874 O OG1 . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B OG1 
1875 C CG2 . THR B 334 ? 1.4368 1.4368 1.4368 0.0000 0.0000 0.0000 345 THR B CG2 
1876 N N   . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B N   
1877 C CA  . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B CA  
1878 C C   . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B C   
1879 O O   . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B O   
1880 C CB  . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B CB  
1881 C CG  . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B CG  
1882 C CD  . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B CD  
1883 N NE  . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B NE  
1884 C CZ  . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B CZ  
1885 N NH1 . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B NH1 
1886 N NH2 . ARG B 335 ? 1.4223 1.4223 1.4223 0.0000 0.0000 0.0000 346 ARG B NH2 
1887 N N   . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B N   
1888 C CA  . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CA  
1889 C C   . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B C   
1890 O O   . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B O   
1891 C CB  . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CB  
1892 C CG  . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CG  
1893 C CD1 . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CD1 
1894 C CD2 . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CD2 
1895 C CE1 . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CE1 
1896 C CE2 . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CE2 
1897 C CZ  . PHE B 336 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 347 PHE B CZ  
1898 N N   . ALA B 337 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 348 ALA B N   
1899 C CA  . ALA B 337 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 348 ALA B CA  
1900 C C   . ALA B 337 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 348 ALA B C   
1901 O O   . ALA B 337 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 348 ALA B O   
1902 C CB  . ALA B 337 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 348 ALA B CB  
1903 N N   . SER B 338 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 349 SER B N   
1904 C CA  . SER B 338 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 349 SER B CA  
1905 C C   . SER B 338 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 349 SER B C   
1906 O O   . SER B 338 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 349 SER B O   
1907 C CB  . SER B 338 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 349 SER B CB  
1908 O OG  . SER B 338 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 349 SER B OG  
1909 N N   . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B N   
1910 C CA  . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B CA  
1911 C C   . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B C   
1912 O O   . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B O   
1913 C CB  . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B CB  
1914 C CG1 . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B CG1 
1915 C CG2 . VAL B 339 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 350 VAL B CG2 
1916 N N   . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B N   
1917 C CA  . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CA  
1918 C C   . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B C   
1919 O O   . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B O   
1920 C CB  . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CB  
1921 C CG  . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CG  
1922 C CD1 . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CD1 
1923 C CD2 . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CD2 
1924 C CE1 . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CE1 
1925 C CE2 . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CE2 
1926 C CZ  . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B CZ  
1927 O OH  . TYR B 340 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 351 TYR B OH  
1928 N N   . ALA B 341 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 352 ALA B N   
1929 C CA  . ALA B 341 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 352 ALA B CA  
1930 C C   . ALA B 341 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 352 ALA B C   
1931 O O   . ALA B 341 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 352 ALA B O   
1932 C CB  . ALA B 341 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 352 ALA B CB  
1933 N N   . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B N   
1934 C CA  . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CA  
1935 C C   . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B C   
1936 O O   . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B O   
1937 C CB  . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CB  
1938 C CG  . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CG  
1939 C CD1 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CD1 
1940 C CD2 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CD2 
1941 N NE1 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B NE1 
1942 C CE2 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CE2 
1943 C CE3 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CE3 
1944 C CZ2 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CZ2 
1945 C CZ3 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CZ3 
1946 C CH2 . TRP B 342 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 353 TRP B CH2 
1947 N N   . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B N   
1948 C CA  . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B CA  
1949 C C   . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B C   
1950 O O   . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B O   
1951 C CB  . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B CB  
1952 C CG  . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B CG  
1953 O OD1 . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B OD1 
1954 N ND2 . ASN B 343 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 354 ASN B ND2 
1955 N N   . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B N   
1956 C CA  . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B CA  
1957 C C   . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B C   
1958 O O   . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B O   
1959 C CB  . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B CB  
1960 C CG  . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B CG  
1961 C CD  . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B CD  
1962 N NE  . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B NE  
1963 C CZ  . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B CZ  
1964 N NH1 . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B NH1 
1965 N NH2 . ARG B 344 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 355 ARG B NH2 
1966 N N   . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B N   
1967 C CA  . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B CA  
1968 C C   . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B C   
1969 O O   . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B O   
1970 C CB  . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B CB  
1971 C CG  . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B CG  
1972 C CD  . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B CD  
1973 C CE  . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B CE  
1974 N NZ  . LYS B 345 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 356 LYS B NZ  
1975 N N   . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B N   
1976 C CA  . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B CA  
1977 C C   . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B C   
1978 O O   . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B O   
1979 C CB  . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B CB  
1980 C CG  . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B CG  
1981 C CD  . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B CD  
1982 N NE  . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B NE  
1983 C CZ  . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B CZ  
1984 N NH1 . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B NH1 
1985 N NH2 . ARG B 346 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 357 ARG B NH2 
1986 N N   . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B N   
1987 C CA  . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B CA  
1988 C C   . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B C   
1989 O O   . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B O   
1990 C CB  . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B CB  
1991 C CG1 . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B CG1 
1992 C CG2 . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B CG2 
1993 C CD1 . ILE B 347 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 358 ILE B CD1 
1994 N N   . SER B 348 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 359 SER B N   
1995 C CA  . SER B 348 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 359 SER B CA  
1996 C C   . SER B 348 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 359 SER B C   
1997 O O   . SER B 348 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 359 SER B O   
1998 C CB  . SER B 348 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 359 SER B CB  
1999 O OG  . SER B 348 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 359 SER B OG  
2000 N N   . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B N   
2001 C CA  . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B CA  
2002 C C   . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B C   
2003 O O   . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B O   
2004 C CB  . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B CB  
2005 C CG  . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B CG  
2006 O OD1 . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B OD1 
2007 N ND2 . ASN B 349 ? 1.4069 1.4069 1.4069 0.0000 0.0000 0.0000 360 ASN B ND2 
2008 N N   . CYS B 350 ? 1.4229 1.4229 1.4229 0.0000 0.0000 0.0000 361 CYS B N   
2009 C CA  . CYS B 350 ? 1.4229 1.4229 1.4229 0.0000 0.0000 0.0000 361 CYS B CA  
2010 C C   . CYS B 350 ? 1.4229 1.4229 1.4229 0.0000 0.0000 0.0000 361 CYS B C   
2011 O O   . CYS B 350 ? 1.4229 1.4229 1.4229 0.0000 0.0000 0.0000 361 CYS B O   
2012 C CB  . CYS B 350 ? 1.4229 1.4229 1.4229 0.0000 0.0000 0.0000 361 CYS B CB  
2013 S SG  . CYS B 350 ? 1.4229 1.4229 1.4229 0.0000 0.0000 0.0000 361 CYS B SG  
2014 N N   . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B N   
2015 C CA  . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B CA  
2016 C C   . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B C   
2017 O O   . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B O   
2018 C CB  . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B CB  
2019 C CG1 . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B CG1 
2020 C CG2 . VAL B 351 ? 1.3670 1.3670 1.3670 0.0000 0.0000 0.0000 362 VAL B CG2 
2021 N N   . ALA B 352 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 363 ALA B N   
2022 C CA  . ALA B 352 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 363 ALA B CA  
2023 C C   . ALA B 352 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 363 ALA B C   
2024 O O   . ALA B 352 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 363 ALA B O   
2025 C CB  . ALA B 352 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 363 ALA B CB  
2026 N N   . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B N   
2027 C CA  . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B CA  
2028 C C   . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B C   
2029 O O   . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B O   
2030 C CB  . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B CB  
2031 C CG  . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B CG  
2032 O OD1 . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B OD1 
2033 O OD2 . ASP B 353 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 364 ASP B OD2 
2034 N N   . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B N   
2035 C CA  . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CA  
2036 C C   . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B C   
2037 O O   . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B O   
2038 C CB  . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CB  
2039 C CG  . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CG  
2040 C CD1 . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CD1 
2041 C CD2 . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CD2 
2042 C CE1 . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CE1 
2043 C CE2 . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CE2 
2044 C CZ  . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B CZ  
2045 O OH  . TYR B 354 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 365 TYR B OH  
2046 N N   . SER B 355 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 366 SER B N   
2047 C CA  . SER B 355 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 366 SER B CA  
2048 C C   . SER B 355 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 366 SER B C   
2049 O O   . SER B 355 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 366 SER B O   
2050 C CB  . SER B 355 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 366 SER B CB  
2051 O OG  . SER B 355 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 366 SER B OG  
2052 N N   . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B N   
2053 C CA  . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B CA  
2054 C C   . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B C   
2055 O O   . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B O   
2056 C CB  . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B CB  
2057 C CG1 . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B CG1 
2058 C CG2 . VAL B 356 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 367 VAL B CG2 
2059 N N   . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B N   
2060 C CA  . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B CA  
2061 C C   . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B C   
2062 O O   . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B O   
2063 C CB  . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B CB  
2064 C CG  . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B CG  
2065 C CD1 . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B CD1 
2066 C CD2 . LEU B 357 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 368 LEU B CD2 
2067 N N   . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B N   
2068 C CA  . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CA  
2069 C C   . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B C   
2070 O O   . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B O   
2071 C CB  . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CB  
2072 C CG  . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CG  
2073 C CD1 . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CD1 
2074 C CD2 . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CD2 
2075 C CE1 . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CE1 
2076 C CE2 . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CE2 
2077 C CZ  . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B CZ  
2078 O OH  . TYR B 358 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 369 TYR B OH  
2079 N N   . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B N   
2080 C CA  . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B CA  
2081 C C   . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B C   
2082 O O   . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B O   
2083 C CB  . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B CB  
2084 C CG  . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B CG  
2085 O OD1 . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B OD1 
2086 N ND2 . ASN B 359 ? 1.4234 1.4234 1.4234 0.0000 0.0000 0.0000 370 ASN B ND2 
2087 N N   . SER B 360 ? 1.4155 1.4155 1.4155 0.0000 0.0000 0.0000 371 SER B N   
2088 C CA  . SER B 360 ? 1.4155 1.4155 1.4155 0.0000 0.0000 0.0000 371 SER B CA  
2089 C C   . SER B 360 ? 1.4155 1.4155 1.4155 0.0000 0.0000 0.0000 371 SER B C   
2090 O O   . SER B 360 ? 1.4155 1.4155 1.4155 0.0000 0.0000 0.0000 371 SER B O   
2091 C CB  . SER B 360 ? 1.4155 1.4155 1.4155 0.0000 0.0000 0.0000 371 SER B CB  
2092 O OG  . SER B 360 ? 1.4155 1.4155 1.4155 0.0000 0.0000 0.0000 371 SER B OG  
2093 N N   . ALA B 361 ? 1.3936 1.3936 1.3936 0.0000 0.0000 0.0000 372 ALA B N   
2094 C CA  . ALA B 361 ? 1.3936 1.3936 1.3936 0.0000 0.0000 0.0000 372 ALA B CA  
2095 C C   . ALA B 361 ? 1.3936 1.3936 1.3936 0.0000 0.0000 0.0000 372 ALA B C   
2096 O O   . ALA B 361 ? 1.3936 1.3936 1.3936 0.0000 0.0000 0.0000 372 ALA B O   
2097 C CB  . ALA B 361 ? 1.3936 1.3936 1.3936 0.0000 0.0000 0.0000 372 ALA B CB  
2098 N N   . SER B 362 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 373 SER B N   
2099 C CA  . SER B 362 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 373 SER B CA  
2100 C C   . SER B 362 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 373 SER B C   
2101 O O   . SER B 362 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 373 SER B O   
2102 C CB  . SER B 362 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 373 SER B CB  
2103 O OG  . SER B 362 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 373 SER B OG  
2104 N N   . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B N   
2105 C CA  . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CA  
2106 C C   . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B C   
2107 O O   . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B O   
2108 C CB  . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CB  
2109 C CG  . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CG  
2110 C CD1 . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CD1 
2111 C CD2 . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CD2 
2112 C CE1 . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CE1 
2113 C CE2 . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CE2 
2114 C CZ  . PHE B 363 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 374 PHE B CZ  
2115 N N   . SER B 364 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 375 SER B N   
2116 C CA  . SER B 364 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 375 SER B CA  
2117 C C   . SER B 364 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 375 SER B C   
2118 O O   . SER B 364 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 375 SER B O   
2119 C CB  . SER B 364 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 375 SER B CB  
2120 O OG  . SER B 364 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 375 SER B OG  
2121 N N   . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B N   
2122 C CA  . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B CA  
2123 C C   . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B C   
2124 O O   . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B O   
2125 C CB  . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B CB  
2126 O OG1 . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B OG1 
2127 C CG2 . THR B 365 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 376 THR B CG2 
2128 N N   . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B N   
2129 C CA  . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CA  
2130 C C   . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B C   
2131 O O   . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B O   
2132 C CB  . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CB  
2133 C CG  . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CG  
2134 C CD1 . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CD1 
2135 C CD2 . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CD2 
2136 C CE1 . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CE1 
2137 C CE2 . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CE2 
2138 C CZ  . PHE B 366 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 377 PHE B CZ  
2139 N N   . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B N   
2140 C CA  . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B CA  
2141 C C   . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B C   
2142 O O   . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B O   
2143 C CB  . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B CB  
2144 C CG  . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B CG  
2145 C CD  . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B CD  
2146 C CE  . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B CE  
2147 N NZ  . LYS B 367 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 378 LYS B NZ  
2148 N N   . CYS B 368 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 379 CYS B N   
2149 C CA  . CYS B 368 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 379 CYS B CA  
2150 C C   . CYS B 368 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 379 CYS B C   
2151 O O   . CYS B 368 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 379 CYS B O   
2152 C CB  . CYS B 368 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 379 CYS B CB  
2153 S SG  . CYS B 368 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 379 CYS B SG  
2154 N N   . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B N   
2155 C CA  . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CA  
2156 C C   . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B C   
2157 O O   . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B O   
2158 C CB  . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CB  
2159 C CG  . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CG  
2160 C CD1 . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CD1 
2161 C CD2 . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CD2 
2162 C CE1 . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CE1 
2163 C CE2 . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CE2 
2164 C CZ  . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B CZ  
2165 O OH  . TYR B 369 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 380 TYR B OH  
2166 N N   . GLY B 370 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 381 GLY B N   
2167 C CA  . GLY B 370 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 381 GLY B CA  
2168 C C   . GLY B 370 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 381 GLY B C   
2169 O O   . GLY B 370 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 381 GLY B O   
2170 N N   . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B N   
2171 C CA  . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B CA  
2172 C C   . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B C   
2173 O O   . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B O   
2174 C CB  . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B CB  
2175 C CG1 . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B CG1 
2176 C CG2 . VAL B 371 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 382 VAL B CG2 
2177 N N   . SER B 372 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 383 SER B N   
2178 C CA  . SER B 372 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 383 SER B CA  
2179 C C   . SER B 372 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 383 SER B C   
2180 O O   . SER B 372 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 383 SER B O   
2181 C CB  . SER B 372 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 383 SER B CB  
2182 O OG  . SER B 372 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 383 SER B OG  
2183 N N   . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B N   
2184 C CA  . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B CA  
2185 C C   . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B C   
2186 O O   . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B O   
2187 C CB  . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B CB  
2188 C CG  . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B CG  
2189 C CD  . PRO B 373 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 384 PRO B CD  
2190 N N   . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B N   
2191 C CA  . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B CA  
2192 C C   . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B C   
2193 O O   . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B O   
2194 C CB  . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B CB  
2195 O OG1 . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B OG1 
2196 C CG2 . THR B 374 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 385 THR B CG2 
2197 N N   . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B N   
2198 C CA  . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B CA  
2199 C C   . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B C   
2200 O O   . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B O   
2201 C CB  . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B CB  
2202 C CG  . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B CG  
2203 C CD  . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B CD  
2204 C CE  . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B CE  
2205 N NZ  . LYS B 375 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 386 LYS B NZ  
2206 N N   . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B N   
2207 C CA  . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B CA  
2208 C C   . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B C   
2209 O O   . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B O   
2210 C CB  . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B CB  
2211 C CG  . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B CG  
2212 C CD1 . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B CD1 
2213 C CD2 . LEU B 376 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 387 LEU B CD2 
2214 N N   . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B N   
2215 C CA  . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B CA  
2216 C C   . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B C   
2217 O O   . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B O   
2218 C CB  . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B CB  
2219 C CG  . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B CG  
2220 O OD1 . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B OD1 
2221 N ND2 . ASN B 377 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 388 ASN B ND2 
2222 N N   . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B N   
2223 C CA  . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B CA  
2224 C C   . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B C   
2225 O O   . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B O   
2226 C CB  . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B CB  
2227 C CG  . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B CG  
2228 O OD1 . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B OD1 
2229 O OD2 . ASP B 378 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 389 ASP B OD2 
2230 N N   . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B N   
2231 C CA  . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B CA  
2232 C C   . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B C   
2233 O O   . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B O   
2234 C CB  . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B CB  
2235 C CG  . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B CG  
2236 C CD1 . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B CD1 
2237 C CD2 . LEU B 379 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 390 LEU B CD2 
2238 N N   . CYS B 380 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 391 CYS B N   
2239 C CA  . CYS B 380 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 391 CYS B CA  
2240 C C   . CYS B 380 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 391 CYS B C   
2241 O O   . CYS B 380 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 391 CYS B O   
2242 C CB  . CYS B 380 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 391 CYS B CB  
2243 S SG  . CYS B 380 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 391 CYS B SG  
2244 N N   . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B N   
2245 C CA  . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CA  
2246 C C   . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B C   
2247 O O   . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B O   
2248 C CB  . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CB  
2249 C CG  . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CG  
2250 C CD1 . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CD1 
2251 C CD2 . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CD2 
2252 C CE1 . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CE1 
2253 C CE2 . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CE2 
2254 C CZ  . PHE B 381 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 392 PHE B CZ  
2255 N N   . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B N   
2256 C CA  . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B CA  
2257 C C   . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B C   
2258 O O   . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B O   
2259 C CB  . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B CB  
2260 O OG1 . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B OG1 
2261 C CG2 . THR B 382 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 393 THR B CG2 
2262 N N   . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B N   
2263 C CA  . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B CA  
2264 C C   . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B C   
2265 O O   . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B O   
2266 C CB  . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B CB  
2267 C CG  . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B CG  
2268 O OD1 . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B OD1 
2269 N ND2 . ASN B 383 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 394 ASN B ND2 
2270 N N   . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B N   
2271 C CA  . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B CA  
2272 C C   . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B C   
2273 O O   . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B O   
2274 C CB  . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B CB  
2275 C CG1 . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B CG1 
2276 C CG2 . VAL B 384 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 395 VAL B CG2 
2277 N N   . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B N   
2278 C CA  . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CA  
2279 C C   . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B C   
2280 O O   . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B O   
2281 C CB  . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CB  
2282 C CG  . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CG  
2283 C CD1 . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CD1 
2284 C CD2 . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CD2 
2285 C CE1 . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CE1 
2286 C CE2 . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CE2 
2287 C CZ  . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B CZ  
2288 O OH  . TYR B 385 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 396 TYR B OH  
2289 N N   . ALA B 386 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 397 ALA B N   
2290 C CA  . ALA B 386 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 397 ALA B CA  
2291 C C   . ALA B 386 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 397 ALA B C   
2292 O O   . ALA B 386 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 397 ALA B O   
2293 C CB  . ALA B 386 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 397 ALA B CB  
2294 N N   . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B N   
2295 C CA  . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B CA  
2296 C C   . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B C   
2297 O O   . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B O   
2298 C CB  . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B CB  
2299 C CG  . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B CG  
2300 O OD1 . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B OD1 
2301 O OD2 . ASP B 387 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 398 ASP B OD2 
2302 N N   . SER B 388 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 399 SER B N   
2303 C CA  . SER B 388 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 399 SER B CA  
2304 C C   . SER B 388 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 399 SER B C   
2305 O O   . SER B 388 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 399 SER B O   
2306 C CB  . SER B 388 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 399 SER B CB  
2307 O OG  . SER B 388 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 399 SER B OG  
2308 N N   . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B N   
2309 C CA  . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CA  
2310 C C   . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B C   
2311 O O   . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B O   
2312 C CB  . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CB  
2313 C CG  . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CG  
2314 C CD1 . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CD1 
2315 C CD2 . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CD2 
2316 C CE1 . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CE1 
2317 C CE2 . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CE2 
2318 C CZ  . PHE B 389 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 400 PHE B CZ  
2319 N N   . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B N   
2320 C CA  . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B CA  
2321 C C   . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B C   
2322 O O   . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B O   
2323 C CB  . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B CB  
2324 C CG1 . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B CG1 
2325 C CG2 . VAL B 390 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 401 VAL B CG2 
2326 N N   . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B N   
2327 C CA  . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B CA  
2328 C C   . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B C   
2329 O O   . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B O   
2330 C CB  . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B CB  
2331 C CG1 . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B CG1 
2332 C CG2 . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B CG2 
2333 C CD1 . ILE B 391 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 402 ILE B CD1 
2334 N N   . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B N   
2335 C CA  . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B CA  
2336 C C   . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B C   
2337 O O   . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B O   
2338 C CB  . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B CB  
2339 C CG  . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B CG  
2340 C CD  . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B CD  
2341 N NE  . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B NE  
2342 C CZ  . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B CZ  
2343 N NH1 . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B NH1 
2344 N NH2 . ARG B 392 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 403 ARG B NH2 
2345 N N   . GLY B 393 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 404 GLY B N   
2346 C CA  . GLY B 393 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 404 GLY B CA  
2347 C C   . GLY B 393 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 404 GLY B C   
2348 O O   . GLY B 393 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 404 GLY B O   
2349 N N   . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B N   
2350 C CA  . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B CA  
2351 C C   . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B C   
2352 O O   . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B O   
2353 C CB  . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B CB  
2354 C CG  . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B CG  
2355 O OD1 . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B OD1 
2356 O OD2 . ASP B 394 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 405 ASP B OD2 
2357 N N   . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B N   
2358 C CA  . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B CA  
2359 C C   . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B C   
2360 O O   . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B O   
2361 C CB  . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B CB  
2362 C CG  . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B CG  
2363 C CD  . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B CD  
2364 O OE1 . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B OE1 
2365 O OE2 . GLU B 395 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 406 GLU B OE2 
2366 N N   . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B N   
2367 C CA  . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B CA  
2368 C C   . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B C   
2369 O O   . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B O   
2370 C CB  . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B CB  
2371 C CG1 . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B CG1 
2372 C CG2 . VAL B 396 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 407 VAL B CG2 
2373 N N   . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B N   
2374 C CA  . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B CA  
2375 C C   . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B C   
2376 O O   . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B O   
2377 C CB  . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B CB  
2378 C CG  . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B CG  
2379 C CD  . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B CD  
2380 N NE  . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B NE  
2381 C CZ  . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B CZ  
2382 N NH1 . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B NH1 
2383 N NH2 . ARG B 397 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 408 ARG B NH2 
2384 N N   . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B N   
2385 C CA  . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B CA  
2386 C C   . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B C   
2387 O O   . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B O   
2388 C CB  . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B CB  
2389 C CG  . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B CG  
2390 C CD  . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B CD  
2391 O OE1 . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B OE1 
2392 N NE2 . GLN B 398 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 409 GLN B NE2 
2393 N N   . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B N   
2394 C CA  . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B CA  
2395 C C   . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B C   
2396 O O   . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B O   
2397 C CB  . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B CB  
2398 C CG1 . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B CG1 
2399 C CG2 . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B CG2 
2400 C CD1 . ILE B 399 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 410 ILE B CD1 
2401 N N   . ALA B 400 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 411 ALA B N   
2402 C CA  . ALA B 400 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 411 ALA B CA  
2403 C C   . ALA B 400 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 411 ALA B C   
2404 O O   . ALA B 400 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 411 ALA B O   
2405 C CB  . ALA B 400 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 411 ALA B CB  
2406 N N   . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B N   
2407 C CA  . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B CA  
2408 C C   . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B C   
2409 O O   . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B O   
2410 C CB  . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B CB  
2411 C CG  . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B CG  
2412 C CD  . PRO B 401 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 412 PRO B CD  
2413 N N   . GLY B 402 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 413 GLY B N   
2414 C CA  . GLY B 402 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 413 GLY B CA  
2415 C C   . GLY B 402 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 413 GLY B C   
2416 O O   . GLY B 402 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 413 GLY B O   
2417 N N   . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B N   
2418 C CA  . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B CA  
2419 C C   . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B C   
2420 O O   . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B O   
2421 C CB  . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B CB  
2422 C CG  . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B CG  
2423 C CD  . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B CD  
2424 O OE1 . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B OE1 
2425 N NE2 . GLN B 403 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 414 GLN B NE2 
2426 N N   . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B N   
2427 C CA  . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B CA  
2428 C C   . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B C   
2429 O O   . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B O   
2430 C CB  . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B CB  
2431 O OG1 . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B OG1 
2432 C CG2 . THR B 404 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 415 THR B CG2 
2433 N N   . GLY B 405 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 416 GLY B N   
2434 C CA  . GLY B 405 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 416 GLY B CA  
2435 C C   . GLY B 405 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 416 GLY B C   
2436 O O   . GLY B 405 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 416 GLY B O   
2437 N N   . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B N   
2438 C CA  . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B CA  
2439 C C   . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B C   
2440 O O   . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B O   
2441 C CB  . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B CB  
2442 C CG  . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B CG  
2443 C CD  . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B CD  
2444 C CE  . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B CE  
2445 N NZ  . LYS B 406 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 417 LYS B NZ  
2446 N N   . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B N   
2447 C CA  . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B CA  
2448 C C   . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B C   
2449 O O   . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B O   
2450 C CB  . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B CB  
2451 C CG1 . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B CG1 
2452 C CG2 . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B CG2 
2453 C CD1 . ILE B 407 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 418 ILE B CD1 
2454 N N   . ALA B 408 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 419 ALA B N   
2455 C CA  . ALA B 408 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 419 ALA B CA  
2456 C C   . ALA B 408 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 419 ALA B C   
2457 O O   . ALA B 408 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 419 ALA B O   
2458 C CB  . ALA B 408 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 419 ALA B CB  
2459 N N   . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B N   
2460 C CA  . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B CA  
2461 C C   . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B C   
2462 O O   . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B O   
2463 C CB  . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B CB  
2464 C CG  . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B CG  
2465 O OD1 . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B OD1 
2466 O OD2 . ASP B 409 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 420 ASP B OD2 
2467 N N   . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B N   
2468 C CA  . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CA  
2469 C C   . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B C   
2470 O O   . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B O   
2471 C CB  . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CB  
2472 C CG  . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CG  
2473 C CD1 . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CD1 
2474 C CD2 . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CD2 
2475 C CE1 . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CE1 
2476 C CE2 . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CE2 
2477 C CZ  . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B CZ  
2478 O OH  . TYR B 410 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 421 TYR B OH  
2479 N N   . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B N   
2480 C CA  . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B CA  
2481 C C   . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B C   
2482 O O   . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B O   
2483 C CB  . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B CB  
2484 C CG  . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B CG  
2485 O OD1 . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B OD1 
2486 N ND2 . ASN B 411 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 422 ASN B ND2 
2487 N N   . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B N   
2488 C CA  . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CA  
2489 C C   . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B C   
2490 O O   . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B O   
2491 C CB  . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CB  
2492 C CG  . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CG  
2493 C CD1 . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CD1 
2494 C CD2 . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CD2 
2495 C CE1 . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CE1 
2496 C CE2 . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CE2 
2497 C CZ  . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B CZ  
2498 O OH  . TYR B 412 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 423 TYR B OH  
2499 N N   . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B N   
2500 C CA  . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B CA  
2501 C C   . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B C   
2502 O O   . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B O   
2503 C CB  . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B CB  
2504 C CG  . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B CG  
2505 C CD  . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B CD  
2506 C CE  . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B CE  
2507 N NZ  . LYS B 413 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 424 LYS B NZ  
2508 N N   . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B N   
2509 C CA  . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B CA  
2510 C C   . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B C   
2511 O O   . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B O   
2512 C CB  . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B CB  
2513 C CG  . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B CG  
2514 C CD1 . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B CD1 
2515 C CD2 . LEU B 414 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 425 LEU B CD2 
2516 N N   . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B N   
2517 C CA  . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B CA  
2518 C C   . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B C   
2519 O O   . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B O   
2520 C CB  . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B CB  
2521 C CG  . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B CG  
2522 C CD  . PRO B 415 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 426 PRO B CD  
2523 N N   . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B N   
2524 C CA  . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B CA  
2525 C C   . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B C   
2526 O O   . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B O   
2527 C CB  . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B CB  
2528 C CG  . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B CG  
2529 O OD1 . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B OD1 
2530 O OD2 . ASP B 416 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 427 ASP B OD2 
2531 N N   . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B N   
2532 C CA  . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B CA  
2533 C C   . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B C   
2534 O O   . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B O   
2535 C CB  . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B CB  
2536 C CG  . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B CG  
2537 O OD1 . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B OD1 
2538 O OD2 . ASP B 417 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 428 ASP B OD2 
2539 N N   . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B N   
2540 C CA  . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CA  
2541 C C   . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B C   
2542 O O   . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B O   
2543 C CB  . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CB  
2544 C CG  . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CG  
2545 C CD1 . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CD1 
2546 C CD2 . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CD2 
2547 C CE1 . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CE1 
2548 C CE2 . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CE2 
2549 C CZ  . PHE B 418 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 429 PHE B CZ  
2550 N N   . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B N   
2551 C CA  . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B CA  
2552 C C   . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B C   
2553 O O   . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B O   
2554 C CB  . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B CB  
2555 O OG1 . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B OG1 
2556 C CG2 . THR B 419 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 430 THR B CG2 
2557 N N   . GLY B 420 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 431 GLY B N   
2558 C CA  . GLY B 420 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 431 GLY B CA  
2559 C C   . GLY B 420 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 431 GLY B C   
2560 O O   . GLY B 420 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 431 GLY B O   
2561 N N   . CYS B 421 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 432 CYS B N   
2562 C CA  . CYS B 421 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 432 CYS B CA  
2563 C C   . CYS B 421 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 432 CYS B C   
2564 O O   . CYS B 421 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 432 CYS B O   
2565 C CB  . CYS B 421 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 432 CYS B CB  
2566 S SG  . CYS B 421 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 432 CYS B SG  
2567 N N   . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B N   
2568 C CA  . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B CA  
2569 C C   . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B C   
2570 O O   . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B O   
2571 C CB  . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B CB  
2572 C CG1 . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B CG1 
2573 C CG2 . VAL B 422 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 433 VAL B CG2 
2574 N N   . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B N   
2575 C CA  . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B CA  
2576 C C   . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B C   
2577 O O   . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B O   
2578 C CB  . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B CB  
2579 C CG1 . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B CG1 
2580 C CG2 . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B CG2 
2581 C CD1 . ILE B 423 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 434 ILE B CD1 
2582 N N   . ALA B 424 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 435 ALA B N   
2583 C CA  . ALA B 424 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 435 ALA B CA  
2584 C C   . ALA B 424 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 435 ALA B C   
2585 O O   . ALA B 424 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 435 ALA B O   
2586 C CB  . ALA B 424 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 435 ALA B CB  
2587 N N   . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B N   
2588 C CA  . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CA  
2589 C C   . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B C   
2590 O O   . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B O   
2591 C CB  . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CB  
2592 C CG  . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CG  
2593 C CD1 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CD1 
2594 C CD2 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CD2 
2595 N NE1 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B NE1 
2596 C CE2 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CE2 
2597 C CE3 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CE3 
2598 C CZ2 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CZ2 
2599 C CZ3 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CZ3 
2600 C CH2 . TRP B 425 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 436 TRP B CH2 
2601 N N   . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B N   
2602 C CA  . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B CA  
2603 C C   . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B C   
2604 O O   . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B O   
2605 C CB  . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B CB  
2606 C CG  . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B CG  
2607 O OD1 . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B OD1 
2608 N ND2 . ASN B 426 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 437 ASN B ND2 
2609 N N   . SER B 427 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 438 SER B N   
2610 C CA  . SER B 427 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 438 SER B CA  
2611 C C   . SER B 427 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 438 SER B C   
2612 O O   . SER B 427 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 438 SER B O   
2613 C CB  . SER B 427 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 438 SER B CB  
2614 O OG  . SER B 427 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 438 SER B OG  
2615 N N   . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B N   
2616 C CA  . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B CA  
2617 C C   . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B C   
2618 O O   . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B O   
2619 C CB  . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B CB  
2620 C CG  . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B CG  
2621 O OD1 . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B OD1 
2622 N ND2 . ASN B 428 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 439 ASN B ND2 
2623 N N   . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B N   
2624 C CA  . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B CA  
2625 C C   . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B C   
2626 O O   . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B O   
2627 C CB  . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B CB  
2628 C CG  . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B CG  
2629 O OD1 . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B OD1 
2630 N ND2 . ASN B 429 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 440 ASN B ND2 
2631 N N   . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B N   
2632 C CA  . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B CA  
2633 C C   . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B C   
2634 O O   . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B O   
2635 C CB  . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B CB  
2636 C CG  . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B CG  
2637 C CD1 . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B CD1 
2638 C CD2 . LEU B 430 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 441 LEU B CD2 
2639 N N   . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B N   
2640 C CA  . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B CA  
2641 C C   . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B C   
2642 O O   . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B O   
2643 C CB  . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B CB  
2644 C CG  . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B CG  
2645 O OD1 . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B OD1 
2646 O OD2 . ASP B 431 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 442 ASP B OD2 
2647 N N   . SER B 432 ? 1.3790 1.3790 1.3790 0.0000 0.0000 0.0000 443 SER B N   
2648 C CA  . SER B 432 ? 1.3790 1.3790 1.3790 0.0000 0.0000 0.0000 443 SER B CA  
2649 C C   . SER B 432 ? 1.3790 1.3790 1.3790 0.0000 0.0000 0.0000 443 SER B C   
2650 O O   . SER B 432 ? 1.3790 1.3790 1.3790 0.0000 0.0000 0.0000 443 SER B O   
2651 C CB  . SER B 432 ? 1.3790 1.3790 1.3790 0.0000 0.0000 0.0000 443 SER B CB  
2652 O OG  . SER B 432 ? 1.3790 1.3790 1.3790 0.0000 0.0000 0.0000 443 SER B OG  
2653 N N   . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B N   
2654 C CA  . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B CA  
2655 C C   . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B C   
2656 O O   . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B O   
2657 C CB  . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B CB  
2658 C CG  . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B CG  
2659 C CD  . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B CD  
2660 C CE  . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B CE  
2661 N NZ  . LYS B 433 ? 1.4797 1.4797 1.4797 0.0000 0.0000 0.0000 444 LYS B NZ  
2662 N N   . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B N   
2663 C CA  . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B CA  
2664 C C   . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B C   
2665 O O   . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B O   
2666 C CB  . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B CB  
2667 C CG1 . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B CG1 
2668 C CG2 . VAL B 434 ? 1.5758 1.5758 1.5758 0.0000 0.0000 0.0000 445 VAL B CG2 
2669 N N   . GLY B 435 ? 1.5374 1.5374 1.5374 0.0000 0.0000 0.0000 446 GLY B N   
2670 C CA  . GLY B 435 ? 1.5374 1.5374 1.5374 0.0000 0.0000 0.0000 446 GLY B CA  
2671 C C   . GLY B 435 ? 1.5374 1.5374 1.5374 0.0000 0.0000 0.0000 446 GLY B C   
2672 O O   . GLY B 435 ? 1.5374 1.5374 1.5374 0.0000 0.0000 0.0000 446 GLY B O   
2673 N N   . GLY B 436 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 447 GLY B N   
2674 C CA  . GLY B 436 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 447 GLY B CA  
2675 C C   . GLY B 436 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 447 GLY B C   
2676 O O   . GLY B 436 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 447 GLY B O   
2677 N N   . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B N   
2678 C CA  . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B CA  
2679 C C   . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B C   
2680 O O   . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B O   
2681 C CB  . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B CB  
2682 C CG  . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B CG  
2683 O OD1 . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B OD1 
2684 N ND2 . ASN B 437 ? 1.3513 1.3513 1.3513 0.0000 0.0000 0.0000 448 ASN B ND2 
2685 N N   . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B N   
2686 C CA  . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CA  
2687 C C   . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B C   
2688 O O   . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B O   
2689 C CB  . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CB  
2690 C CG  . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CG  
2691 C CD1 . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CD1 
2692 C CD2 . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CD2 
2693 C CE1 . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CE1 
2694 C CE2 . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CE2 
2695 C CZ  . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B CZ  
2696 O OH  . TYR B 438 ? 1.3287 1.3287 1.3287 0.0000 0.0000 0.0000 449 TYR B OH  
2697 N N   . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B N   
2698 C CA  . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B CA  
2699 C C   . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B C   
2700 O O   . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B O   
2701 C CB  . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B CB  
2702 C CG  . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B CG  
2703 O OD1 . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B OD1 
2704 N ND2 . ASN B 439 ? 1.3380 1.3380 1.3380 0.0000 0.0000 0.0000 450 ASN B ND2 
2705 N N   . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B N   
2706 C CA  . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CA  
2707 C C   . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B C   
2708 O O   . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B O   
2709 C CB  . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CB  
2710 C CG  . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CG  
2711 C CD1 . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CD1 
2712 C CD2 . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CD2 
2713 C CE1 . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CE1 
2714 C CE2 . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CE2 
2715 C CZ  . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B CZ  
2716 O OH  . TYR B 440 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 451 TYR B OH  
2717 N N   . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B N   
2718 C CA  . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B CA  
2719 C C   . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B C   
2720 O O   . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B O   
2721 C CB  . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B CB  
2722 C CG  . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B CG  
2723 C CD1 . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B CD1 
2724 C CD2 . LEU B 441 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 452 LEU B CD2 
2725 N N   . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B N   
2726 C CA  . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CA  
2727 C C   . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B C   
2728 O O   . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B O   
2729 C CB  . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CB  
2730 C CG  . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CG  
2731 C CD1 . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CD1 
2732 C CD2 . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CD2 
2733 C CE1 . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CE1 
2734 C CE2 . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CE2 
2735 C CZ  . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B CZ  
2736 O OH  . TYR B 442 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 453 TYR B OH  
2737 N N   . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B N   
2738 C CA  . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B CA  
2739 C C   . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B C   
2740 O O   . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B O   
2741 C CB  . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B CB  
2742 C CG  . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B CG  
2743 C CD  . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B CD  
2744 N NE  . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B NE  
2745 C CZ  . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B CZ  
2746 N NH1 . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B NH1 
2747 N NH2 . ARG B 443 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 454 ARG B NH2 
2748 N N   . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B N   
2749 C CA  . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B CA  
2750 C C   . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B C   
2751 O O   . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B O   
2752 C CB  . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B CB  
2753 C CG  . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B CG  
2754 C CD1 . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B CD1 
2755 C CD2 . LEU B 444 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 455 LEU B CD2 
2756 N N   . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B N   
2757 C CA  . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CA  
2758 C C   . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B C   
2759 O O   . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B O   
2760 C CB  . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CB  
2761 C CG  . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CG  
2762 C CD1 . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CD1 
2763 C CD2 . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CD2 
2764 C CE1 . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CE1 
2765 C CE2 . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CE2 
2766 C CZ  . PHE B 445 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 456 PHE B CZ  
2767 N N   . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B N   
2768 C CA  . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B CA  
2769 C C   . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B C   
2770 O O   . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B O   
2771 C CB  . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B CB  
2772 C CG  . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B CG  
2773 C CD  . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B CD  
2774 N NE  . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B NE  
2775 C CZ  . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B CZ  
2776 N NH1 . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B NH1 
2777 N NH2 . ARG B 446 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 457 ARG B NH2 
2778 N N   . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B N   
2779 C CA  . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B CA  
2780 C C   . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B C   
2781 O O   . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B O   
2782 C CB  . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B CB  
2783 C CG  . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B CG  
2784 C CD  . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B CD  
2785 C CE  . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B CE  
2786 N NZ  . LYS B 447 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 458 LYS B NZ  
2787 N N   . SER B 448 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 459 SER B N   
2788 C CA  . SER B 448 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 459 SER B CA  
2789 C C   . SER B 448 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 459 SER B C   
2790 O O   . SER B 448 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 459 SER B O   
2791 C CB  . SER B 448 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 459 SER B CB  
2792 O OG  . SER B 448 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 459 SER B OG  
2793 N N   . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B N   
2794 C CA  . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B CA  
2795 C C   . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B C   
2796 O O   . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B O   
2797 C CB  . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B CB  
2798 C CG  . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B CG  
2799 O OD1 . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B OD1 
2800 N ND2 . ASN B 449 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 460 ASN B ND2 
2801 N N   . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B N   
2802 C CA  . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B CA  
2803 C C   . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B C   
2804 O O   . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B O   
2805 C CB  . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B CB  
2806 C CG  . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B CG  
2807 C CD1 . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B CD1 
2808 C CD2 . LEU B 450 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 461 LEU B CD2 
2809 N N   . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B N   
2810 C CA  . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B CA  
2811 C C   . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B C   
2812 O O   . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B O   
2813 C CB  . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B CB  
2814 C CG  . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B CG  
2815 C CD  . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B CD  
2816 C CE  . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B CE  
2817 N NZ  . LYS B 451 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 462 LYS B NZ  
2818 N N   . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B N   
2819 C CA  . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B CA  
2820 C C   . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B C   
2821 O O   . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B O   
2822 C CB  . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B CB  
2823 C CG  . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B CG  
2824 C CD  . PRO B 452 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 463 PRO B CD  
2825 N N   . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B N   
2826 C CA  . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CA  
2827 C C   . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B C   
2828 O O   . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B O   
2829 C CB  . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CB  
2830 C CG  . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CG  
2831 C CD1 . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CD1 
2832 C CD2 . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CD2 
2833 C CE1 . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CE1 
2834 C CE2 . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CE2 
2835 C CZ  . PHE B 453 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 464 PHE B CZ  
2836 N N   . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B N   
2837 C CA  . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B CA  
2838 C C   . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B C   
2839 O O   . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B O   
2840 C CB  . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B CB  
2841 C CG  . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B CG  
2842 C CD  . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B CD  
2843 O OE1 . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B OE1 
2844 O OE2 . GLU B 454 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 465 GLU B OE2 
2845 N N   . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B N   
2846 C CA  . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B CA  
2847 C C   . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B C   
2848 O O   . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B O   
2849 C CB  . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B CB  
2850 C CG  . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B CG  
2851 C CD  . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B CD  
2852 N NE  . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B NE  
2853 C CZ  . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B CZ  
2854 N NH1 . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B NH1 
2855 N NH2 . ARG B 455 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 466 ARG B NH2 
2856 N N   . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B N   
2857 C CA  . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B CA  
2858 C C   . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B C   
2859 O O   . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B O   
2860 C CB  . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B CB  
2861 C CG  . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B CG  
2862 O OD1 . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B OD1 
2863 O OD2 . ASP B 456 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 467 ASP B OD2 
2864 N N   . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B N   
2865 C CA  . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B CA  
2866 C C   . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B C   
2867 O O   . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B O   
2868 C CB  . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B CB  
2869 C CG1 . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B CG1 
2870 C CG2 . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B CG2 
2871 C CD1 . ILE B 457 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 468 ILE B CD1 
2872 N N   . SER B 458 ? 1.3758 1.3758 1.3758 0.0000 0.0000 0.0000 469 SER B N   
2873 C CA  . SER B 458 ? 1.3758 1.3758 1.3758 0.0000 0.0000 0.0000 469 SER B CA  
2874 C C   . SER B 458 ? 1.3758 1.3758 1.3758 0.0000 0.0000 0.0000 469 SER B C   
2875 O O   . SER B 458 ? 1.3758 1.3758 1.3758 0.0000 0.0000 0.0000 469 SER B O   
2876 C CB  . SER B 458 ? 1.3758 1.3758 1.3758 0.0000 0.0000 0.0000 469 SER B CB  
2877 O OG  . SER B 458 ? 1.3758 1.3758 1.3758 0.0000 0.0000 0.0000 469 SER B OG  
2878 N N   . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B N   
2879 C CA  . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B CA  
2880 C C   . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B C   
2881 O O   . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B O   
2882 C CB  . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B CB  
2883 O OG1 . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B OG1 
2884 C CG2 . THR B 459 ? 1.4325 1.4325 1.4325 0.0000 0.0000 0.0000 470 THR B CG2 
2885 N N   . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B N   
2886 C CA  . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B CA  
2887 C C   . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B C   
2888 O O   . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B O   
2889 C CB  . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B CB  
2890 C CG  . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B CG  
2891 C CD  . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B CD  
2892 O OE1 . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B OE1 
2893 O OE2 . GLU B 460 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 471 GLU B OE2 
2894 N N   . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B N   
2895 C CA  . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B CA  
2896 C C   . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B C   
2897 O O   . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B O   
2898 C CB  . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B CB  
2899 C CG1 . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B CG1 
2900 C CG2 . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B CG2 
2901 C CD1 . ILE B 461 ? 1.4525 1.4525 1.4525 0.0000 0.0000 0.0000 472 ILE B CD1 
2902 N N   . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B N   
2903 C CA  . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CA  
2904 C C   . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B C   
2905 O O   . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B O   
2906 C CB  . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CB  
2907 C CG  . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CG  
2908 C CD1 . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CD1 
2909 C CD2 . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CD2 
2910 C CE1 . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CE1 
2911 C CE2 . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CE2 
2912 C CZ  . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B CZ  
2913 O OH  . TYR B 462 ? 1.4030 1.4030 1.4030 0.0000 0.0000 0.0000 473 TYR B OH  
2914 N N   . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B N   
2915 C CA  . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B CA  
2916 C C   . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B C   
2917 O O   . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B O   
2918 C CB  . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B CB  
2919 C CG  . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B CG  
2920 C CD  . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B CD  
2921 O OE1 . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B OE1 
2922 N NE2 . GLN B 463 ? 1.5697 1.5697 1.5697 0.0000 0.0000 0.0000 474 GLN B NE2 
2923 N N   . ALA B 464 ? 1.5178 1.5178 1.5178 0.0000 0.0000 0.0000 475 ALA B N   
2924 C CA  . ALA B 464 ? 1.5178 1.5178 1.5178 0.0000 0.0000 0.0000 475 ALA B CA  
2925 C C   . ALA B 464 ? 1.5178 1.5178 1.5178 0.0000 0.0000 0.0000 475 ALA B C   
2926 O O   . ALA B 464 ? 1.5178 1.5178 1.5178 0.0000 0.0000 0.0000 475 ALA B O   
2927 C CB  . ALA B 464 ? 1.5178 1.5178 1.5178 0.0000 0.0000 0.0000 475 ALA B CB  
2928 N N   . GLY B 465 ? 1.6366 1.6366 1.6366 0.0000 0.0000 0.0000 476 GLY B N   
2929 C CA  . GLY B 465 ? 1.6366 1.6366 1.6366 0.0000 0.0000 0.0000 476 GLY B CA  
2930 C C   . GLY B 465 ? 1.6366 1.6366 1.6366 0.0000 0.0000 0.0000 476 GLY B C   
2931 O O   . GLY B 465 ? 1.6366 1.6366 1.6366 0.0000 0.0000 0.0000 476 GLY B O   
2932 N N   . SER B 466 ? 1.7290 1.7290 1.7290 0.0000 0.0000 0.0000 477 SER B N   
2933 C CA  . SER B 466 ? 1.7290 1.7290 1.7290 0.0000 0.0000 0.0000 477 SER B CA  
2934 C C   . SER B 466 ? 1.7290 1.7290 1.7290 0.0000 0.0000 0.0000 477 SER B C   
2935 O O   . SER B 466 ? 1.7290 1.7290 1.7290 0.0000 0.0000 0.0000 477 SER B O   
2936 C CB  . SER B 466 ? 1.7290 1.7290 1.7290 0.0000 0.0000 0.0000 477 SER B CB  
2937 O OG  . SER B 466 ? 1.7290 1.7290 1.7290 0.0000 0.0000 0.0000 477 SER B OG  
2938 N N   . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B N   
2939 C CA  . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B CA  
2940 C C   . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B C   
2941 O O   . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B O   
2942 C CB  . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B CB  
2943 O OG1 . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B OG1 
2944 C CG2 . THR B 467 ? 1.7654 1.7654 1.7654 0.0000 0.0000 0.0000 478 THR B CG2 
2945 N N   . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B N   
2946 C CA  . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B CA  
2947 C C   . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B C   
2948 O O   . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B O   
2949 C CB  . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B CB  
2950 C CG  . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B CG  
2951 C CD  . PRO B 468 ? 1.7862 1.7862 1.7862 0.0000 0.0000 0.0000 479 PRO B CD  
2952 N N   . CYS B 469 ? 1.7781 1.7781 1.7781 0.0000 0.0000 0.0000 480 CYS B N   
2953 C CA  . CYS B 469 ? 1.7781 1.7781 1.7781 0.0000 0.0000 0.0000 480 CYS B CA  
2954 C C   . CYS B 469 ? 1.7781 1.7781 1.7781 0.0000 0.0000 0.0000 480 CYS B C   
2955 O O   . CYS B 469 ? 1.7781 1.7781 1.7781 0.0000 0.0000 0.0000 480 CYS B O   
2956 C CB  . CYS B 469 ? 1.7781 1.7781 1.7781 0.0000 0.0000 0.0000 480 CYS B CB  
2957 S SG  . CYS B 469 ? 1.7781 1.7781 1.7781 0.0000 0.0000 0.0000 480 CYS B SG  
2958 N N   . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B N   
2959 C CA  . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B CA  
2960 C C   . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B C   
2961 O O   . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B O   
2962 C CB  . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B CB  
2963 C CG  . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B CG  
2964 O OD1 . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B OD1 
2965 N ND2 . ASN B 470 ? 1.7617 1.7617 1.7617 0.0000 0.0000 0.0000 481 ASN B ND2 
2966 N N   . GLY B 471 ? 1.6895 1.6895 1.6895 0.0000 0.0000 0.0000 482 GLY B N   
2967 C CA  . GLY B 471 ? 1.6895 1.6895 1.6895 0.0000 0.0000 0.0000 482 GLY B CA  
2968 C C   . GLY B 471 ? 1.6895 1.6895 1.6895 0.0000 0.0000 0.0000 482 GLY B C   
2969 O O   . GLY B 471 ? 1.6895 1.6895 1.6895 0.0000 0.0000 0.0000 482 GLY B O   
2970 N N   . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B N   
2971 C CA  . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B CA  
2972 C C   . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B C   
2973 O O   . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B O   
2974 C CB  . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B CB  
2975 C CG1 . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B CG1 
2976 C CG2 . VAL B 472 ? 1.6231 1.6231 1.6231 0.0000 0.0000 0.0000 483 VAL B CG2 
2977 N N   . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B N   
2978 C CA  . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B CA  
2979 C C   . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B C   
2980 O O   . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B O   
2981 C CB  . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B CB  
2982 C CG  . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B CG  
2983 C CD  . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B CD  
2984 O OE1 . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B OE1 
2985 O OE2 . GLU B 473 ? 1.5923 1.5923 1.5923 0.0000 0.0000 0.0000 484 GLU B OE2 
2986 N N   . GLY B 474 ? 1.5674 1.5674 1.5674 0.0000 0.0000 0.0000 485 GLY B N   
2987 C CA  . GLY B 474 ? 1.5674 1.5674 1.5674 0.0000 0.0000 0.0000 485 GLY B CA  
2988 C C   . GLY B 474 ? 1.5674 1.5674 1.5674 0.0000 0.0000 0.0000 485 GLY B C   
2989 O O   . GLY B 474 ? 1.5674 1.5674 1.5674 0.0000 0.0000 0.0000 485 GLY B O   
2990 N N   . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B N   
2991 C CA  . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CA  
2992 C C   . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B C   
2993 O O   . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B O   
2994 C CB  . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CB  
2995 C CG  . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CG  
2996 C CD1 . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CD1 
2997 C CD2 . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CD2 
2998 C CE1 . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CE1 
2999 C CE2 . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CE2 
3000 C CZ  . PHE B 475 ? 1.5211 1.5211 1.5211 0.0000 0.0000 0.0000 486 PHE B CZ  
3001 N N   . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B N   
3002 C CA  . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B CA  
3003 C C   . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B C   
3004 O O   . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B O   
3005 C CB  . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B CB  
3006 C CG  . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B CG  
3007 O OD1 . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B OD1 
3008 N ND2 . ASN B 476 ? 1.5101 1.5101 1.5101 0.0000 0.0000 0.0000 487 ASN B ND2 
3009 N N   . CYS B 477 ? 1.5226 1.5226 1.5226 0.0000 0.0000 0.0000 488 CYS B N   
3010 C CA  . CYS B 477 ? 1.5226 1.5226 1.5226 0.0000 0.0000 0.0000 488 CYS B CA  
3011 C C   . CYS B 477 ? 1.5226 1.5226 1.5226 0.0000 0.0000 0.0000 488 CYS B C   
3012 O O   . CYS B 477 ? 1.5226 1.5226 1.5226 0.0000 0.0000 0.0000 488 CYS B O   
3013 C CB  . CYS B 477 ? 1.5226 1.5226 1.5226 0.0000 0.0000 0.0000 488 CYS B CB  
3014 S SG  . CYS B 477 ? 1.5226 1.5226 1.5226 0.0000 0.0000 0.0000 488 CYS B SG  
3015 N N   . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B N   
3016 C CA  . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CA  
3017 C C   . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B C   
3018 O O   . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B O   
3019 C CB  . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CB  
3020 C CG  . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CG  
3021 C CD1 . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CD1 
3022 C CD2 . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CD2 
3023 C CE1 . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CE1 
3024 C CE2 . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CE2 
3025 C CZ  . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B CZ  
3026 O OH  . TYR B 478 ? 1.3827 1.3827 1.3827 0.0000 0.0000 0.0000 489 TYR B OH  
3027 N N   . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B N   
3028 C CA  . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CA  
3029 C C   . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B C   
3030 O O   . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B O   
3031 C CB  . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CB  
3032 C CG  . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CG  
3033 C CD1 . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CD1 
3034 C CD2 . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CD2 
3035 C CE1 . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CE1 
3036 C CE2 . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CE2 
3037 C CZ  . PHE B 479 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 490 PHE B CZ  
3038 N N   . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B N   
3039 C CA  . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B CA  
3040 C C   . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B C   
3041 O O   . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B O   
3042 C CB  . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B CB  
3043 C CG  . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B CG  
3044 C CD  . PRO B 480 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 491 PRO B CD  
3045 N N   . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B N   
3046 C CA  . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B CA  
3047 C C   . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B C   
3048 O O   . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B O   
3049 C CB  . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B CB  
3050 C CG  . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B CG  
3051 C CD1 . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B CD1 
3052 C CD2 . LEU B 481 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 492 LEU B CD2 
3053 N N   . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B N   
3054 C CA  . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B CA  
3055 C C   . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B C   
3056 O O   . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B O   
3057 C CB  . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B CB  
3058 C CG  . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B CG  
3059 C CD  . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B CD  
3060 O OE1 . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B OE1 
3061 N NE2 . GLN B 482 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 493 GLN B NE2 
3062 N N   . SER B 483 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 494 SER B N   
3063 C CA  . SER B 483 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 494 SER B CA  
3064 C C   . SER B 483 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 494 SER B C   
3065 O O   . SER B 483 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 494 SER B O   
3066 C CB  . SER B 483 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 494 SER B CB  
3067 O OG  . SER B 483 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 494 SER B OG  
3068 N N   . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B N   
3069 C CA  . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CA  
3070 C C   . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B C   
3071 O O   . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B O   
3072 C CB  . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CB  
3073 C CG  . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CG  
3074 C CD1 . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CD1 
3075 C CD2 . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CD2 
3076 C CE1 . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CE1 
3077 C CE2 . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CE2 
3078 C CZ  . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B CZ  
3079 O OH  . TYR B 484 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 495 TYR B OH  
3080 N N   . GLY B 485 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 496 GLY B N   
3081 C CA  . GLY B 485 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 496 GLY B CA  
3082 C C   . GLY B 485 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 496 GLY B C   
3083 O O   . GLY B 485 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 496 GLY B O   
3084 N N   . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B N   
3085 C CA  . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CA  
3086 C C   . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B C   
3087 O O   . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B O   
3088 C CB  . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CB  
3089 C CG  . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CG  
3090 C CD1 . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CD1 
3091 C CD2 . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CD2 
3092 C CE1 . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CE1 
3093 C CE2 . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CE2 
3094 C CZ  . PHE B 486 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 497 PHE B CZ  
3095 N N   . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B N   
3096 C CA  . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B CA  
3097 C C   . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B C   
3098 O O   . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B O   
3099 C CB  . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B CB  
3100 C CG  . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B CG  
3101 C CD  . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B CD  
3102 O OE1 . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B OE1 
3103 N NE2 . GLN B 487 ? 1.3360 1.3360 1.3360 0.0000 0.0000 0.0000 498 GLN B NE2 
3104 N N   . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B N   
3105 C CA  . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B CA  
3106 C C   . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B C   
3107 O O   . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B O   
3108 C CB  . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B CB  
3109 C CG  . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B CG  
3110 C CD  . PRO B 488 ? 1.3706 1.3706 1.3706 0.0000 0.0000 0.0000 499 PRO B CD  
3111 N N   . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B N   
3112 C CA  . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B CA  
3113 C C   . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B C   
3114 O O   . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B O   
3115 C CB  . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B CB  
3116 O OG1 . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B OG1 
3117 C CG2 . THR B 489 ? 1.3722 1.3722 1.3722 0.0000 0.0000 0.0000 500 THR B CG2 
3118 N N   . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B N   
3119 C CA  . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B CA  
3120 C C   . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B C   
3121 O O   . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B O   
3122 C CB  . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B CB  
3123 C CG  . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B CG  
3124 O OD1 . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B OD1 
3125 N ND2 . ASN B 490 ? 1.3500 1.3500 1.3500 0.0000 0.0000 0.0000 501 ASN B ND2 
3126 N N   . GLY B 491 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 502 GLY B N   
3127 C CA  . GLY B 491 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 502 GLY B CA  
3128 C C   . GLY B 491 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 502 GLY B C   
3129 O O   . GLY B 491 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 502 GLY B O   
3130 N N   . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B N   
3131 C CA  . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B CA  
3132 C C   . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B C   
3133 O O   . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B O   
3134 C CB  . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B CB  
3135 C CG1 . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B CG1 
3136 C CG2 . VAL B 492 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 503 VAL B CG2 
3137 N N   . GLY B 493 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 504 GLY B N   
3138 C CA  . GLY B 493 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 504 GLY B CA  
3139 C C   . GLY B 493 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 504 GLY B C   
3140 O O   . GLY B 493 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 504 GLY B O   
3141 N N   . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B N   
3142 C CA  . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CA  
3143 C C   . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B C   
3144 O O   . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B O   
3145 C CB  . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CB  
3146 C CG  . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CG  
3147 C CD1 . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CD1 
3148 C CD2 . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CD2 
3149 C CE1 . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CE1 
3150 C CE2 . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CE2 
3151 C CZ  . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B CZ  
3152 O OH  . TYR B 494 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 505 TYR B OH  
3153 N N   . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B N   
3154 C CA  . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B CA  
3155 C C   . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B C   
3156 O O   . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B O   
3157 C CB  . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B CB  
3158 C CG  . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B CG  
3159 C CD  . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B CD  
3160 O OE1 . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B OE1 
3161 N NE2 . GLN B 495 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 506 GLN B NE2 
3162 N N   . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B N   
3163 C CA  . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B CA  
3164 C C   . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B C   
3165 O O   . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B O   
3166 C CB  . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B CB  
3167 C CG  . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B CG  
3168 C CD  . PRO B 496 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 507 PRO B CD  
3169 N N   . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B N   
3170 C CA  . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CA  
3171 C C   . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B C   
3172 O O   . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B O   
3173 C CB  . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CB  
3174 C CG  . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CG  
3175 C CD1 . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CD1 
3176 C CD2 . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CD2 
3177 C CE1 . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CE1 
3178 C CE2 . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CE2 
3179 C CZ  . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B CZ  
3180 O OH  . TYR B 497 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 508 TYR B OH  
3181 N N   . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B N   
3182 C CA  . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B CA  
3183 C C   . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B C   
3184 O O   . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B O   
3185 C CB  . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B CB  
3186 C CG  . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B CG  
3187 C CD  . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B CD  
3188 N NE  . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B NE  
3189 C CZ  . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B CZ  
3190 N NH1 . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B NH1 
3191 N NH2 . ARG B 498 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 509 ARG B NH2 
3192 N N   . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B N   
3193 C CA  . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B CA  
3194 C C   . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B C   
3195 O O   . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B O   
3196 C CB  . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B CB  
3197 C CG1 . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B CG1 
3198 C CG2 . VAL B 499 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 510 VAL B CG2 
3199 N N   . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B N   
3200 C CA  . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B CA  
3201 C C   . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B C   
3202 O O   . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B O   
3203 C CB  . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B CB  
3204 C CG1 . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B CG1 
3205 C CG2 . VAL B 500 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 511 VAL B CG2 
3206 N N   . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B N   
3207 C CA  . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B CA  
3208 C C   . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B C   
3209 O O   . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B O   
3210 C CB  . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B CB  
3211 C CG1 . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B CG1 
3212 C CG2 . VAL B 501 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 512 VAL B CG2 
3213 N N   . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B N   
3214 C CA  . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B CA  
3215 C C   . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B C   
3216 O O   . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B O   
3217 C CB  . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B CB  
3218 C CG  . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B CG  
3219 C CD1 . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B CD1 
3220 C CD2 . LEU B 502 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 513 LEU B CD2 
3221 N N   . SER B 503 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 514 SER B N   
3222 C CA  . SER B 503 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 514 SER B CA  
3223 C C   . SER B 503 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 514 SER B C   
3224 O O   . SER B 503 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 514 SER B O   
3225 C CB  . SER B 503 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 514 SER B CB  
3226 O OG  . SER B 503 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 514 SER B OG  
3227 N N   . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B N   
3228 C CA  . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CA  
3229 C C   . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B C   
3230 O O   . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B O   
3231 C CB  . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CB  
3232 C CG  . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CG  
3233 C CD1 . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CD1 
3234 C CD2 . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CD2 
3235 C CE1 . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CE1 
3236 C CE2 . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CE2 
3237 C CZ  . PHE B 504 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 515 PHE B CZ  
3238 N N   . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B N   
3239 C CA  . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B CA  
3240 C C   . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B C   
3241 O O   . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B O   
3242 C CB  . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B CB  
3243 C CG  . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B CG  
3244 C CD  . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B CD  
3245 O OE1 . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B OE1 
3246 O OE2 . GLU B 505 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 516 GLU B OE2 
3247 N N   . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B N   
3248 C CA  . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B CA  
3249 C C   . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B C   
3250 O O   . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B O   
3251 C CB  . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B CB  
3252 C CG  . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B CG  
3253 C CD1 . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B CD1 
3254 C CD2 . LEU B 506 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 517 LEU B CD2 
3255 N N   . ALA B 509 ? 1.5603 1.5603 1.5603 0.0000 0.0000 0.0000 520 ALA B N   
3256 C CA  . ALA B 509 ? 1.5603 1.5603 1.5603 0.0000 0.0000 0.0000 520 ALA B CA  
3257 C C   . ALA B 509 ? 1.5603 1.5603 1.5603 0.0000 0.0000 0.0000 520 ALA B C   
3258 O O   . ALA B 509 ? 1.5603 1.5603 1.5603 0.0000 0.0000 0.0000 520 ALA B O   
3259 C CB  . ALA B 509 ? 1.5603 1.5603 1.5603 0.0000 0.0000 0.0000 520 ALA B CB  
3260 N N   . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B N   
3261 C CA  . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B CA  
3262 C C   . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B C   
3263 O O   . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B O   
3264 C CB  . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B CB  
3265 C CG  . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B CG  
3266 C CD  . PRO B 510 ? 1.5863 1.5863 1.5863 0.0000 0.0000 0.0000 521 PRO B CD  
3267 N N   . ALA B 511 ? 1.4367 1.4367 1.4367 0.0000 0.0000 0.0000 522 ALA B N   
3268 C CA  . ALA B 511 ? 1.4367 1.4367 1.4367 0.0000 0.0000 0.0000 522 ALA B CA  
3269 C C   . ALA B 511 ? 1.4367 1.4367 1.4367 0.0000 0.0000 0.0000 522 ALA B C   
3270 O O   . ALA B 511 ? 1.4367 1.4367 1.4367 0.0000 0.0000 0.0000 522 ALA B O   
3271 C CB  . ALA B 511 ? 1.4367 1.4367 1.4367 0.0000 0.0000 0.0000 522 ALA B CB  
3272 N N   . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B N   
3273 C CA  . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B CA  
3274 C C   . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B C   
3275 O O   . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B O   
3276 C CB  . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B CB  
3277 O OG1 . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B OG1 
3278 C CG2 . THR B 512 ? 1.3345 1.3345 1.3345 0.0000 0.0000 0.0000 523 THR B CG2 
3279 N N   . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B N   
3280 C CA  . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B CA  
3281 C C   . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B C   
3282 O O   . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B O   
3283 C CB  . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B CB  
3284 C CG1 . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B CG1 
3285 C CG2 . VAL B 513 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 524 VAL B CG2 
3286 N N   . CYS B 514 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 525 CYS B N   
3287 C CA  . CYS B 514 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 525 CYS B CA  
3288 C C   . CYS B 514 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 525 CYS B C   
3289 O O   . CYS B 514 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 525 CYS B O   
3290 C CB  . CYS B 514 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 525 CYS B CB  
3291 S SG  . CYS B 514 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 525 CYS B SG  
3292 N N   . GLY B 515 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 526 GLY B N   
3293 C CA  . GLY B 515 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 526 GLY B CA  
3294 C C   . GLY B 515 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 526 GLY B C   
3295 O O   . GLY B 515 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 526 GLY B O   
3296 N N   . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B N   
3297 C CA  . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B CA  
3298 C C   . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B C   
3299 O O   . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B O   
3300 C CB  . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B CB  
3301 C CG  . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B CG  
3302 C CD  . PRO B 516 ? 1.3256 1.3256 1.3256 0.0000 0.0000 0.0000 527 PRO B CD  
# 
