data_7SOF
# 
_entry.id   7SOF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.353 
_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   7SOF         pdb_00007sof 10.2210/pdb7sof/pdb 
WWPDB D_1000260126 ?            ?                   
EMDB  EMD-25269    ?            ?                   
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'SARS-CoV-2 S NTD B.1.617.1 kappa variant S2X303 Local Refinement' 
_pdbx_database_related.db_id          EMD-25269 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7SOF 
_pdbx_database_status.recvd_initial_deposition_date   2021-10-29 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McCallum, M.'                                                       1 0000-0001-8398-8330 
'Veesler, D.'                                                        2 0000-0002-6019-8675 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 3 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Science 
_citation.journal_id_ASTM           SCIEAS 
_citation.journal_id_CSD            0038 
_citation.journal_id_ISSN           1095-9203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            374 
_citation.language                  ? 
_citation.page_first                1621 
_citation.page_last                 1626 
_citation.title                     'Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/science.abl8506 
_citation.pdbx_database_id_PubMed   34751595 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McCallum, M.'      1  ? 
primary 'Walls, A.C.'       2  ? 
primary 'Sprouse, K.R.'     3  ? 
primary 'Bowen, J.E.'       4  ? 
primary 'Rosen, L.E.'       5  ? 
primary 'Dang, H.V.'        6  ? 
primary 'De Marco, A.'      7  ? 
primary 'Franko, N.'        8  ? 
primary 'Tilles, S.W.'      9  ? 
primary 'Logue, J.'         10 ? 
primary 'Miranda, M.C.'     11 ? 
primary 'Ahlrichs, M.'      12 ? 
primary 'Carter, L.'        13 ? 
primary 'Snell, G.'         14 ? 
primary 'Pizzuto, M.S.'     15 ? 
primary 'Chu, H.Y.'         16 ? 
primary 'Van Voorhis, W.C.' 17 ? 
primary 'Corti, D.'         18 ? 
primary 'Veesler, D.'       19 ? 
# 
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 'S2X303 Fab light chain' 11270.294  1 ? ? ? ? 
2 polymer     man 'S2X303 Fab heavy chain' 13737.725  1 ? ? ? ? 
3 polymer     man 'Spike glycoprotein' 141867.312 1 ? ? ? ? 
4 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542    1 
? ? ? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    6 ? ? ? ? 
# 
_entity_name_com.entity_id   3 
_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 
;SYELTQPPSVSVSPGQTASITCSGDKLGETYASWYQQKPGQSPILVIYQDNKRPSGIPERFSGSNSENTATLTISGTQTM
DEADYYCQAWDKTIAGFGGGTKLTV
;
;SYELTQPPSVSVSPGQTASITCSGDKLGETYASWYQQKPGQSPILVIYQDNKRPSGIPERFSGSNSENTATLTISGTQTM
DEADYYCQAWDKTIAGFGGGTKLTV
;
L ? 
2 'polypeptide(L)' no no 
;QITLKESGPTLVKPTQTLTLTCKLSGFSVNTGGVGVGWIRQPPGKALEWLALIYWNDDKLYSPSLKSRLTVTKDTSKNQV
VLTMTNMDPVDTATYYCAHVLVWFGEVLPDAFDVWGQGTMVTVSS
;
;QITLKESGPTLVKPTQTLTLTCKLSGFSVNTGGVGVGWIRQPPGKALEWLALIYWNDDKLYSPSLKSRLTVTKDTSKNQV
VLTMTNMDPVDTATYYCAHVLVWFGEVLPDAFDVWGQGTMVTVSS
;
H ? 
3 'polypeptide(L)' no no 
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFD
NPVLPFNDGVYFASIEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLDVYYHKNNKSWMKSEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRV
QPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVCPTKLNDLCFTNVYADSF
VIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYRYRLFRKSNLKPFERDISTEIYQAGSTPC
NGVQGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFL
PFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVPVAIHADQLTPTWRVYSTGS
NVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSRRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTI
SVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGF
NFSQILPDPSKPSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAG
TITSGWTFGAGPALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTPSALGKLQDVVNQNAQALN
TLVKQLSSNFGAISSVLNDILSRLCPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRV
DFCGKGYHLMSFPQSAPHGVVFLHVTYVPAHEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNT
FVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDL
QELGKYEQGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGRSLEVLFQGPGSGGLNDIFEAQKIEWHEGSGHHHHHHHH
;
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFD
NPVLPFNDGVYFASIEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLDVYYHKNNKSWMKSEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRV
QPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVCPTKLNDLCFTNVYADSF
VIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYRYRLFRKSNLKPFERDISTEIYQAGSTPC
NGVQGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFL
PFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVPVAIHADQLTPTWRVYSTGS
NVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSRRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTI
SVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGF
NFSQILPDPSKPSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAG
TITSGWTFGAGPALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTPSALGKLQDVVNQNAQALN
TLVKQLSSNFGAISSVLNDILSRLCPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRV
DFCGKGYHLMSFPQSAPHGVVFLHVTYVPAHEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNT
FVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDL
QELGKYEQGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGRSLEVLFQGPGSGGLNDIFEAQKIEWHEGSGHHHHHHHH
;
A ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    SER n 
1 2    TYR n 
1 3    GLU n 
1 4    LEU n 
1 5    THR n 
1 6    GLN n 
1 7    PRO n 
1 8    PRO n 
1 9    SER n 
1 10   VAL n 
1 11   SER n 
1 12   VAL n 
1 13   SER n 
1 14   PRO n 
1 15   GLY n 
1 16   GLN n 
1 17   THR n 
1 18   ALA n 
1 19   SER n 
1 20   ILE n 
1 21   THR n 
1 22   CYS n 
1 23   SER n 
1 24   GLY n 
1 25   ASP n 
1 26   LYS n 
1 27   LEU n 
1 28   GLY n 
1 29   GLU n 
1 30   THR n 
1 31   TYR n 
1 32   ALA n 
1 33   SER n 
1 34   TRP n 
1 35   TYR n 
1 36   GLN n 
1 37   GLN n 
1 38   LYS n 
1 39   PRO n 
1 40   GLY n 
1 41   GLN n 
1 42   SER n 
1 43   PRO n 
1 44   ILE n 
1 45   LEU n 
1 46   VAL n 
1 47   ILE n 
1 48   TYR n 
1 49   GLN n 
1 50   ASP n 
1 51   ASN n 
1 52   LYS n 
1 53   ARG n 
1 54   PRO n 
1 55   SER n 
1 56   GLY n 
1 57   ILE n 
1 58   PRO n 
1 59   GLU n 
1 60   ARG n 
1 61   PHE n 
1 62   SER n 
1 63   GLY n 
1 64   SER n 
1 65   ASN n 
1 66   SER n 
1 67   GLU n 
1 68   ASN n 
1 69   THR n 
1 70   ALA n 
1 71   THR n 
1 72   LEU n 
1 73   THR n 
1 74   ILE n 
1 75   SER n 
1 76   GLY n 
1 77   THR n 
1 78   GLN n 
1 79   THR n 
1 80   MET n 
1 81   ASP n 
1 82   GLU n 
1 83   ALA n 
1 84   ASP n 
1 85   TYR n 
1 86   TYR n 
1 87   CYS n 
1 88   GLN n 
1 89   ALA n 
1 90   TRP n 
1 91   ASP n 
1 92   LYS n 
1 93   THR n 
1 94   ILE n 
1 95   ALA n 
1 96   GLY n 
1 97   PHE n 
1 98   GLY n 
1 99   GLY n 
1 100  GLY n 
1 101  THR n 
1 102  LYS n 
1 103  LEU n 
1 104  THR n 
1 105  VAL n 
2 1    GLN n 
2 2    ILE n 
2 3    THR n 
2 4    LEU n 
2 5    LYS n 
2 6    GLU n 
2 7    SER n 
2 8    GLY n 
2 9    PRO n 
2 10   THR n 
2 11   LEU n 
2 12   VAL n 
2 13   LYS n 
2 14   PRO n 
2 15   THR n 
2 16   GLN n 
2 17   THR n 
2 18   LEU n 
2 19   THR n 
2 20   LEU n 
2 21   THR n 
2 22   CYS n 
2 23   LYS n 
2 24   LEU n 
2 25   SER n 
2 26   GLY n 
2 27   PHE n 
2 28   SER n 
2 29   VAL n 
2 30   ASN n 
2 31   THR n 
2 32   GLY n 
2 33   GLY n 
2 34   VAL n 
2 35   GLY n 
2 36   VAL n 
2 37   GLY n 
2 38   TRP n 
2 39   ILE n 
2 40   ARG n 
2 41   GLN n 
2 42   PRO n 
2 43   PRO n 
2 44   GLY n 
2 45   LYS n 
2 46   ALA n 
2 47   LEU n 
2 48   GLU n 
2 49   TRP n 
2 50   LEU n 
2 51   ALA n 
2 52   LEU n 
2 53   ILE n 
2 54   TYR n 
2 55   TRP n 
2 56   ASN n 
2 57   ASP n 
2 58   ASP n 
2 59   LYS n 
2 60   LEU n 
2 61   TYR n 
2 62   SER n 
2 63   PRO n 
2 64   SER n 
2 65   LEU n 
2 66   LYS n 
2 67   SER n 
2 68   ARG n 
2 69   LEU n 
2 70   THR n 
2 71   VAL n 
2 72   THR n 
2 73   LYS n 
2 74   ASP n 
2 75   THR n 
2 76   SER n 
2 77   LYS n 
2 78   ASN n 
2 79   GLN n 
2 80   VAL n 
2 81   VAL n 
2 82   LEU n 
2 83   THR n 
2 84   MET n 
2 85   THR n 
2 86   ASN n 
2 87   MET n 
2 88   ASP n 
2 89   PRO n 
2 90   VAL n 
2 91   ASP n 
2 92   THR n 
2 93   ALA n 
2 94   THR n 
2 95   TYR n 
2 96   TYR n 
2 97   CYS n 
2 98   ALA n 
2 99   HIS n 
2 100  VAL n 
2 101  LEU n 
2 102  VAL n 
2 103  TRP n 
2 104  PHE n 
2 105  GLY n 
2 106  GLU n 
2 107  VAL n 
2 108  LEU n 
2 109  PRO n 
2 110  ASP n 
2 111  ALA n 
2 112  PHE n 
2 113  ASP n 
2 114  VAL n 
2 115  TRP n 
2 116  GLY n 
2 117  GLN n 
2 118  GLY n 
2 119  THR n 
2 120  MET n 
2 121  VAL n 
2 122  THR n 
2 123  VAL n 
2 124  SER n 
2 125  SER n 
3 1    MET n 
3 2    PHE n 
3 3    VAL n 
3 4    PHE n 
3 5    LEU n 
3 6    VAL n 
3 7    LEU n 
3 8    LEU n 
3 9    PRO n 
3 10   LEU n 
3 11   VAL n 
3 12   SER n 
3 13   SER n 
3 14   GLN n 
3 15   CYS n 
3 16   VAL n 
3 17   ASN n 
3 18   LEU n 
3 19   THR n 
3 20   THR n 
3 21   ARG n 
3 22   THR n 
3 23   GLN n 
3 24   LEU n 
3 25   PRO n 
3 26   PRO n 
3 27   ALA n 
3 28   TYR n 
3 29   THR n 
3 30   ASN n 
3 31   SER n 
3 32   PHE n 
3 33   THR n 
3 34   ARG n 
3 35   GLY n 
3 36   VAL n 
3 37   TYR n 
3 38   TYR n 
3 39   PRO n 
3 40   ASP n 
3 41   LYS n 
3 42   VAL n 
3 43   PHE n 
3 44   ARG n 
3 45   SER n 
3 46   SER n 
3 47   VAL n 
3 48   LEU n 
3 49   HIS n 
3 50   SER n 
3 51   THR n 
3 52   GLN n 
3 53   ASP n 
3 54   LEU n 
3 55   PHE n 
3 56   LEU n 
3 57   PRO n 
3 58   PHE n 
3 59   PHE n 
3 60   SER n 
3 61   ASN n 
3 62   VAL n 
3 63   THR n 
3 64   TRP n 
3 65   PHE n 
3 66   HIS n 
3 67   ALA n 
3 68   ILE n 
3 69   HIS n 
3 70   VAL n 
3 71   SER n 
3 72   GLY n 
3 73   THR n 
3 74   ASN n 
3 75   GLY n 
3 76   THR n 
3 77   LYS n 
3 78   ARG n 
3 79   PHE n 
3 80   ASP n 
3 81   ASN n 
3 82   PRO n 
3 83   VAL n 
3 84   LEU n 
3 85   PRO n 
3 86   PHE n 
3 87   ASN n 
3 88   ASP n 
3 89   GLY n 
3 90   VAL n 
3 91   TYR n 
3 92   PHE n 
3 93   ALA n 
3 94   SER n 
3 95   ILE n 
3 96   GLU n 
3 97   LYS n 
3 98   SER n 
3 99   ASN n 
3 100  ILE n 
3 101  ILE n 
3 102  ARG n 
3 103  GLY n 
3 104  TRP n 
3 105  ILE n 
3 106  PHE n 
3 107  GLY n 
3 108  THR n 
3 109  THR n 
3 110  LEU n 
3 111  ASP n 
3 112  SER n 
3 113  LYS n 
3 114  THR n 
3 115  GLN n 
3 116  SER n 
3 117  LEU n 
3 118  LEU n 
3 119  ILE n 
3 120  VAL n 
3 121  ASN n 
3 122  ASN n 
3 123  ALA n 
3 124  THR n 
3 125  ASN n 
3 126  VAL n 
3 127  VAL n 
3 128  ILE n 
3 129  LYS n 
3 130  VAL n 
3 131  CYS n 
3 132  GLU n 
3 133  PHE n 
3 134  GLN n 
3 135  PHE n 
3 136  CYS n 
3 137  ASN n 
3 138  ASP n 
3 139  PRO n 
3 140  PHE n 
3 141  LEU n 
3 142  ASP n 
3 143  VAL n 
3 144  TYR n 
3 145  TYR n 
3 146  HIS n 
3 147  LYS n 
3 148  ASN n 
3 149  ASN n 
3 150  LYS n 
3 151  SER n 
3 152  TRP n 
3 153  MET n 
3 154  LYS n 
3 155  SER n 
3 156  GLU n 
3 157  PHE n 
3 158  ARG n 
3 159  VAL n 
3 160  TYR n 
3 161  SER n 
3 162  SER n 
3 163  ALA n 
3 164  ASN n 
3 165  ASN n 
3 166  CYS n 
3 167  THR n 
3 168  PHE n 
3 169  GLU n 
3 170  TYR n 
3 171  VAL n 
3 172  SER n 
3 173  GLN n 
3 174  PRO n 
3 175  PHE n 
3 176  LEU n 
3 177  MET n 
3 178  ASP n 
3 179  LEU n 
3 180  GLU n 
3 181  GLY n 
3 182  LYS n 
3 183  GLN n 
3 184  GLY n 
3 185  ASN n 
3 186  PHE n 
3 187  LYS n 
3 188  ASN n 
3 189  LEU n 
3 190  ARG n 
3 191  GLU n 
3 192  PHE n 
3 193  VAL n 
3 194  PHE n 
3 195  LYS n 
3 196  ASN n 
3 197  ILE n 
3 198  ASP n 
3 199  GLY n 
3 200  TYR n 
3 201  PHE n 
3 202  LYS n 
3 203  ILE n 
3 204  TYR n 
3 205  SER n 
3 206  LYS n 
3 207  HIS n 
3 208  THR n 
3 209  PRO n 
3 210  ILE n 
3 211  ASN n 
3 212  LEU n 
3 213  VAL n 
3 214  ARG n 
3 215  ASP n 
3 216  LEU n 
3 217  PRO n 
3 218  GLN n 
3 219  GLY n 
3 220  PHE n 
3 221  SER n 
3 222  ALA n 
3 223  LEU n 
3 224  GLU n 
3 225  PRO n 
3 226  LEU n 
3 227  VAL n 
3 228  ASP n 
3 229  LEU n 
3 230  PRO n 
3 231  ILE n 
3 232  GLY n 
3 233  ILE n 
3 234  ASN n 
3 235  ILE n 
3 236  THR n 
3 237  ARG n 
3 238  PHE n 
3 239  GLN n 
3 240  THR n 
3 241  LEU n 
3 242  LEU n 
3 243  ALA n 
3 244  LEU n 
3 245  HIS n 
3 246  ARG n 
3 247  SER n 
3 248  TYR n 
3 249  LEU n 
3 250  THR n 
3 251  PRO n 
3 252  GLY n 
3 253  ASP n 
3 254  SER n 
3 255  SER n 
3 256  SER n 
3 257  GLY n 
3 258  TRP n 
3 259  THR n 
3 260  ALA n 
3 261  GLY n 
3 262  ALA n 
3 263  ALA n 
3 264  ALA n 
3 265  TYR n 
3 266  TYR n 
3 267  VAL n 
3 268  GLY n 
3 269  TYR n 
3 270  LEU n 
3 271  GLN n 
3 272  PRO n 
3 273  ARG n 
3 274  THR n 
3 275  PHE n 
3 276  LEU n 
3 277  LEU n 
3 278  LYS n 
3 279  TYR n 
3 280  ASN n 
3 281  GLU n 
3 282  ASN n 
3 283  GLY n 
3 284  THR n 
3 285  ILE n 
3 286  THR n 
3 287  ASP n 
3 288  ALA n 
3 289  VAL n 
3 290  ASP n 
3 291  CYS n 
3 292  ALA n 
3 293  LEU n 
3 294  ASP n 
3 295  PRO n 
3 296  LEU n 
3 297  SER n 
3 298  GLU n 
3 299  THR n 
3 300  LYS n 
3 301  CYS n 
3 302  THR n 
3 303  LEU n 
3 304  LYS n 
3 305  SER n 
3 306  PHE n 
3 307  THR n 
3 308  VAL n 
3 309  GLU n 
3 310  LYS n 
3 311  GLY n 
3 312  ILE n 
3 313  TYR n 
3 314  GLN n 
3 315  THR n 
3 316  SER n 
3 317  ASN n 
3 318  PHE n 
3 319  ARG n 
3 320  VAL n 
3 321  GLN n 
3 322  PRO n 
3 323  THR n 
3 324  GLU n 
3 325  SER n 
3 326  ILE n 
3 327  VAL n 
3 328  ARG n 
3 329  PHE n 
3 330  PRO n 
3 331  ASN n 
3 332  ILE n 
3 333  THR n 
3 334  ASN n 
3 335  LEU n 
3 336  CYS n 
3 337  PRO n 
3 338  PHE n 
3 339  GLY n 
3 340  GLU n 
3 341  VAL n 
3 342  PHE n 
3 343  ASN n 
3 344  ALA n 
3 345  THR n 
3 346  ARG n 
3 347  PHE n 
3 348  ALA n 
3 349  SER n 
3 350  VAL n 
3 351  TYR n 
3 352  ALA n 
3 353  TRP n 
3 354  ASN n 
3 355  ARG n 
3 356  LYS n 
3 357  ARG n 
3 358  ILE n 
3 359  SER n 
3 360  ASN n 
3 361  CYS n 
3 362  VAL n 
3 363  ALA n 
3 364  ASP n 
3 365  TYR n 
3 366  SER n 
3 367  VAL n 
3 368  LEU n 
3 369  TYR n 
3 370  ASN n 
3 371  SER n 
3 372  ALA n 
3 373  SER n 
3 374  PHE n 
3 375  SER n 
3 376  THR n 
3 377  PHE n 
3 378  LYS n 
3 379  CYS n 
3 380  TYR n 
3 381  GLY n 
3 382  VAL n 
3 383  CYS n 
3 384  PRO n 
3 385  THR n 
3 386  LYS n 
3 387  LEU n 
3 388  ASN n 
3 389  ASP n 
3 390  LEU n 
3 391  CYS n 
3 392  PHE n 
3 393  THR n 
3 394  ASN n 
3 395  VAL n 
3 396  TYR n 
3 397  ALA n 
3 398  ASP n 
3 399  SER n 
3 400  PHE n 
3 401  VAL n 
3 402  ILE n 
3 403  ARG n 
3 404  GLY n 
3 405  ASP n 
3 406  GLU n 
3 407  VAL n 
3 408  ARG n 
3 409  GLN n 
3 410  ILE n 
3 411  ALA n 
3 412  PRO n 
3 413  GLY n 
3 414  GLN n 
3 415  THR n 
3 416  GLY n 
3 417  LYS n 
3 418  ILE n 
3 419  ALA n 
3 420  ASP n 
3 421  TYR n 
3 422  ASN n 
3 423  TYR n 
3 424  LYS n 
3 425  LEU n 
3 426  PRO n 
3 427  ASP n 
3 428  ASP n 
3 429  PHE n 
3 430  THR n 
3 431  GLY n 
3 432  CYS n 
3 433  VAL n 
3 434  ILE n 
3 435  ALA n 
3 436  TRP n 
3 437  ASN n 
3 438  SER n 
3 439  ASN n 
3 440  ASN n 
3 441  LEU n 
3 442  ASP n 
3 443  SER n 
3 444  LYS n 
3 445  VAL n 
3 446  GLY n 
3 447  GLY n 
3 448  ASN n 
3 449  TYR n 
3 450  ASN n 
3 451  TYR n 
3 452  ARG n 
3 453  TYR n 
3 454  ARG n 
3 455  LEU n 
3 456  PHE n 
3 457  ARG n 
3 458  LYS n 
3 459  SER n 
3 460  ASN n 
3 461  LEU n 
3 462  LYS n 
3 463  PRO n 
3 464  PHE n 
3 465  GLU n 
3 466  ARG n 
3 467  ASP n 
3 468  ILE n 
3 469  SER n 
3 470  THR n 
3 471  GLU n 
3 472  ILE n 
3 473  TYR n 
3 474  GLN n 
3 475  ALA n 
3 476  GLY n 
3 477  SER n 
3 478  THR n 
3 479  PRO n 
3 480  CYS n 
3 481  ASN n 
3 482  GLY n 
3 483  VAL n 
3 484  GLN n 
3 485  GLY n 
3 486  PHE n 
3 487  ASN n 
3 488  CYS n 
3 489  TYR n 
3 490  PHE n 
3 491  PRO n 
3 492  LEU n 
3 493  GLN n 
3 494  SER n 
3 495  TYR n 
3 496  GLY n 
3 497  PHE n 
3 498  GLN n 
3 499  PRO n 
3 500  THR n 
3 501  ASN n 
3 502  GLY n 
3 503  VAL n 
3 504  GLY n 
3 505  TYR n 
3 506  GLN n 
3 507  PRO n 
3 508  TYR n 
3 509  ARG n 
3 510  VAL n 
3 511  VAL n 
3 512  VAL n 
3 513  LEU n 
3 514  SER n 
3 515  PHE n 
3 516  GLU n 
3 517  LEU n 
3 518  LEU n 
3 519  HIS n 
3 520  ALA n 
3 521  PRO n 
3 522  ALA n 
3 523  THR n 
3 524  VAL n 
3 525  CYS n 
3 526  GLY n 
3 527  PRO n 
3 528  LYS n 
3 529  LYS n 
3 530  SER n 
3 531  THR n 
3 532  ASN n 
3 533  LEU n 
3 534  VAL n 
3 535  LYS n 
3 536  ASN n 
3 537  LYS n 
3 538  CYS n 
3 539  VAL n 
3 540  ASN n 
3 541  PHE n 
3 542  ASN n 
3 543  PHE n 
3 544  ASN n 
3 545  GLY n 
3 546  LEU n 
3 547  THR n 
3 548  GLY n 
3 549  THR n 
3 550  GLY n 
3 551  VAL n 
3 552  LEU n 
3 553  THR n 
3 554  GLU n 
3 555  SER n 
3 556  ASN n 
3 557  LYS n 
3 558  LYS n 
3 559  PHE n 
3 560  LEU n 
3 561  PRO n 
3 562  PHE n 
3 563  GLN n 
3 564  GLN n 
3 565  PHE n 
3 566  GLY n 
3 567  ARG n 
3 568  ASP n 
3 569  ILE n 
3 570  ALA n 
3 571  ASP n 
3 572  THR n 
3 573  THR n 
3 574  ASP n 
3 575  ALA n 
3 576  VAL n 
3 577  ARG n 
3 578  ASP n 
3 579  PRO n 
3 580  GLN n 
3 581  THR n 
3 582  LEU n 
3 583  GLU n 
3 584  ILE n 
3 585  LEU n 
3 586  ASP n 
3 587  ILE n 
3 588  THR n 
3 589  PRO n 
3 590  CYS n 
3 591  SER n 
3 592  PHE n 
3 593  GLY n 
3 594  GLY n 
3 595  VAL n 
3 596  SER n 
3 597  VAL n 
3 598  ILE n 
3 599  THR n 
3 600  PRO n 
3 601  GLY n 
3 602  THR n 
3 603  ASN n 
3 604  THR n 
3 605  SER n 
3 606  ASN n 
3 607  GLN n 
3 608  VAL n 
3 609  ALA n 
3 610  VAL n 
3 611  LEU n 
3 612  TYR n 
3 613  GLN n 
3 614  GLY n 
3 615  VAL n 
3 616  ASN n 
3 617  CYS n 
3 618  THR n 
3 619  GLU n 
3 620  VAL n 
3 621  PRO n 
3 622  VAL n 
3 623  ALA n 
3 624  ILE n 
3 625  HIS n 
3 626  ALA n 
3 627  ASP n 
3 628  GLN n 
3 629  LEU n 
3 630  THR n 
3 631  PRO n 
3 632  THR n 
3 633  TRP n 
3 634  ARG n 
3 635  VAL n 
3 636  TYR n 
3 637  SER n 
3 638  THR n 
3 639  GLY n 
3 640  SER n 
3 641  ASN n 
3 642  VAL n 
3 643  PHE n 
3 644  GLN n 
3 645  THR n 
3 646  ARG n 
3 647  ALA n 
3 648  GLY n 
3 649  CYS n 
3 650  LEU n 
3 651  ILE n 
3 652  GLY n 
3 653  ALA n 
3 654  GLU n 
3 655  HIS n 
3 656  VAL n 
3 657  ASN n 
3 658  ASN n 
3 659  SER n 
3 660  TYR n 
3 661  GLU n 
3 662  CYS n 
3 663  ASP n 
3 664  ILE n 
3 665  PRO n 
3 666  ILE n 
3 667  GLY n 
3 668  ALA n 
3 669  GLY n 
3 670  ILE n 
3 671  CYS n 
3 672  ALA n 
3 673  SER n 
3 674  TYR n 
3 675  GLN n 
3 676  THR n 
3 677  GLN n 
3 678  THR n 
3 679  ASN n 
3 680  SER n 
3 681  ARG n 
3 682  ARG n 
3 683  ARG n 
3 684  ALA n 
3 685  ARG n 
3 686  SER n 
3 687  VAL n 
3 688  ALA n 
3 689  SER n 
3 690  GLN n 
3 691  SER n 
3 692  ILE n 
3 693  ILE n 
3 694  ALA n 
3 695  TYR n 
3 696  THR n 
3 697  MET n 
3 698  SER n 
3 699  LEU n 
3 700  GLY n 
3 701  ALA n 
3 702  GLU n 
3 703  ASN n 
3 704  SER n 
3 705  VAL n 
3 706  ALA n 
3 707  TYR n 
3 708  SER n 
3 709  ASN n 
3 710  ASN n 
3 711  SER n 
3 712  ILE n 
3 713  ALA n 
3 714  ILE n 
3 715  PRO n 
3 716  THR n 
3 717  ASN n 
3 718  PHE n 
3 719  THR n 
3 720  ILE n 
3 721  SER n 
3 722  VAL n 
3 723  THR n 
3 724  THR n 
3 725  GLU n 
3 726  ILE n 
3 727  LEU n 
3 728  PRO n 
3 729  VAL n 
3 730  SER n 
3 731  MET n 
3 732  THR n 
3 733  LYS n 
3 734  THR n 
3 735  SER n 
3 736  VAL n 
3 737  ASP n 
3 738  CYS n 
3 739  THR n 
3 740  MET n 
3 741  TYR n 
3 742  ILE n 
3 743  CYS n 
3 744  GLY n 
3 745  ASP n 
3 746  SER n 
3 747  THR n 
3 748  GLU n 
3 749  CYS n 
3 750  SER n 
3 751  ASN n 
3 752  LEU n 
3 753  LEU n 
3 754  LEU n 
3 755  GLN n 
3 756  TYR n 
3 757  GLY n 
3 758  SER n 
3 759  PHE n 
3 760  CYS n 
3 761  THR n 
3 762  GLN n 
3 763  LEU n 
3 764  ASN n 
3 765  ARG n 
3 766  ALA n 
3 767  LEU n 
3 768  THR n 
3 769  GLY n 
3 770  ILE n 
3 771  ALA n 
3 772  VAL n 
3 773  GLU n 
3 774  GLN n 
3 775  ASP n 
3 776  LYS n 
3 777  ASN n 
3 778  THR n 
3 779  GLN n 
3 780  GLU n 
3 781  VAL n 
3 782  PHE n 
3 783  ALA n 
3 784  GLN n 
3 785  VAL n 
3 786  LYS n 
3 787  GLN n 
3 788  ILE n 
3 789  TYR n 
3 790  LYS n 
3 791  THR n 
3 792  PRO n 
3 793  PRO n 
3 794  ILE n 
3 795  LYS n 
3 796  ASP n 
3 797  PHE n 
3 798  GLY n 
3 799  GLY n 
3 800  PHE n 
3 801  ASN n 
3 802  PHE n 
3 803  SER n 
3 804  GLN n 
3 805  ILE n 
3 806  LEU n 
3 807  PRO n 
3 808  ASP n 
3 809  PRO n 
3 810  SER n 
3 811  LYS n 
3 812  PRO n 
3 813  SER n 
3 814  LYS n 
3 815  ARG n 
3 816  SER n 
3 817  PRO n 
3 818  ILE n 
3 819  GLU n 
3 820  ASP n 
3 821  LEU n 
3 822  LEU n 
3 823  PHE n 
3 824  ASN n 
3 825  LYS n 
3 826  VAL n 
3 827  THR n 
3 828  LEU n 
3 829  ALA n 
3 830  ASP n 
3 831  ALA n 
3 832  GLY n 
3 833  PHE n 
3 834  ILE n 
3 835  LYS n 
3 836  GLN n 
3 837  TYR n 
3 838  GLY n 
3 839  ASP n 
3 840  CYS n 
3 841  LEU n 
3 842  GLY n 
3 843  ASP n 
3 844  ILE n 
3 845  ALA n 
3 846  ALA n 
3 847  ARG n 
3 848  ASP n 
3 849  LEU n 
3 850  ILE n 
3 851  CYS n 
3 852  ALA n 
3 853  GLN n 
3 854  LYS n 
3 855  PHE n 
3 856  ASN n 
3 857  GLY n 
3 858  LEU n 
3 859  THR n 
3 860  VAL n 
3 861  LEU n 
3 862  PRO n 
3 863  PRO n 
3 864  LEU n 
3 865  LEU n 
3 866  THR n 
3 867  ASP n 
3 868  GLU n 
3 869  MET n 
3 870  ILE n 
3 871  ALA n 
3 872  GLN n 
3 873  TYR n 
3 874  THR n 
3 875  SER n 
3 876  ALA n 
3 877  LEU n 
3 878  LEU n 
3 879  ALA n 
3 880  GLY n 
3 881  THR n 
3 882  ILE n 
3 883  THR n 
3 884  SER n 
3 885  GLY n 
3 886  TRP n 
3 887  THR n 
3 888  PHE n 
3 889  GLY n 
3 890  ALA n 
3 891  GLY n 
3 892  PRO n 
3 893  ALA n 
3 894  LEU n 
3 895  GLN n 
3 896  ILE n 
3 897  PRO n 
3 898  PHE n 
3 899  PRO n 
3 900  MET n 
3 901  GLN n 
3 902  MET n 
3 903  ALA n 
3 904  TYR n 
3 905  ARG n 
3 906  PHE n 
3 907  ASN n 
3 908  GLY n 
3 909  ILE n 
3 910  GLY n 
3 911  VAL n 
3 912  THR n 
3 913  GLN n 
3 914  ASN n 
3 915  VAL n 
3 916  LEU n 
3 917  TYR n 
3 918  GLU n 
3 919  ASN n 
3 920  GLN n 
3 921  LYS n 
3 922  LEU n 
3 923  ILE n 
3 924  ALA n 
3 925  ASN n 
3 926  GLN n 
3 927  PHE n 
3 928  ASN n 
3 929  SER n 
3 930  ALA n 
3 931  ILE n 
3 932  GLY n 
3 933  LYS n 
3 934  ILE n 
3 935  GLN n 
3 936  ASP n 
3 937  SER n 
3 938  LEU n 
3 939  SER n 
3 940  SER n 
3 941  THR n 
3 942  PRO n 
3 943  SER n 
3 944  ALA n 
3 945  LEU n 
3 946  GLY n 
3 947  LYS n 
3 948  LEU n 
3 949  GLN n 
3 950  ASP n 
3 951  VAL n 
3 952  VAL n 
3 953  ASN n 
3 954  GLN n 
3 955  ASN n 
3 956  ALA n 
3 957  GLN n 
3 958  ALA n 
3 959  LEU n 
3 960  ASN n 
3 961  THR n 
3 962  LEU n 
3 963  VAL n 
3 964  LYS n 
3 965  GLN n 
3 966  LEU n 
3 967  SER n 
3 968  SER n 
3 969  ASN n 
3 970  PHE n 
3 971  GLY n 
3 972  ALA n 
3 973  ILE n 
3 974  SER n 
3 975  SER n 
3 976  VAL n 
3 977  LEU n 
3 978  ASN n 
3 979  ASP n 
3 980  ILE n 
3 981  LEU n 
3 982  SER n 
3 983  ARG n 
3 984  LEU n 
3 985  CYS n 
3 986  PRO n 
3 987  PRO n 
3 988  GLU n 
3 989  ALA n 
3 990  GLU n 
3 991  VAL n 
3 992  GLN n 
3 993  ILE n 
3 994  ASP n 
3 995  ARG n 
3 996  LEU n 
3 997  ILE n 
3 998  THR n 
3 999  GLY n 
3 1000 ARG n 
3 1001 LEU n 
3 1002 GLN n 
3 1003 SER n 
3 1004 LEU n 
3 1005 GLN n 
3 1006 THR n 
3 1007 TYR n 
3 1008 VAL n 
3 1009 THR n 
3 1010 GLN n 
3 1011 GLN n 
3 1012 LEU n 
3 1013 ILE n 
3 1014 ARG n 
3 1015 ALA n 
3 1016 ALA n 
3 1017 GLU n 
3 1018 ILE n 
3 1019 ARG n 
3 1020 ALA n 
3 1021 SER n 
3 1022 ALA n 
3 1023 ASN n 
3 1024 LEU n 
3 1025 ALA n 
3 1026 ALA n 
3 1027 THR n 
3 1028 LYS n 
3 1029 MET n 
3 1030 SER n 
3 1031 GLU n 
3 1032 CYS n 
3 1033 VAL n 
3 1034 LEU n 
3 1035 GLY n 
3 1036 GLN n 
3 1037 SER n 
3 1038 LYS n 
3 1039 ARG n 
3 1040 VAL n 
3 1041 ASP n 
3 1042 PHE n 
3 1043 CYS n 
3 1044 GLY n 
3 1045 LYS n 
3 1046 GLY n 
3 1047 TYR n 
3 1048 HIS n 
3 1049 LEU n 
3 1050 MET n 
3 1051 SER n 
3 1052 PHE n 
3 1053 PRO n 
3 1054 GLN n 
3 1055 SER n 
3 1056 ALA n 
3 1057 PRO n 
3 1058 HIS n 
3 1059 GLY n 
3 1060 VAL n 
3 1061 VAL n 
3 1062 PHE n 
3 1063 LEU n 
3 1064 HIS n 
3 1065 VAL n 
3 1066 THR n 
3 1067 TYR n 
3 1068 VAL n 
3 1069 PRO n 
3 1070 ALA n 
3 1071 HIS n 
3 1072 GLU n 
3 1073 LYS n 
3 1074 ASN n 
3 1075 PHE n 
3 1076 THR n 
3 1077 THR n 
3 1078 ALA n 
3 1079 PRO n 
3 1080 ALA n 
3 1081 ILE n 
3 1082 CYS n 
3 1083 HIS n 
3 1084 ASP n 
3 1085 GLY n 
3 1086 LYS n 
3 1087 ALA n 
3 1088 HIS n 
3 1089 PHE n 
3 1090 PRO n 
3 1091 ARG n 
3 1092 GLU n 
3 1093 GLY n 
3 1094 VAL n 
3 1095 PHE n 
3 1096 VAL n 
3 1097 SER n 
3 1098 ASN n 
3 1099 GLY n 
3 1100 THR n 
3 1101 HIS n 
3 1102 TRP n 
3 1103 PHE n 
3 1104 VAL n 
3 1105 THR n 
3 1106 GLN n 
3 1107 ARG n 
3 1108 ASN n 
3 1109 PHE n 
3 1110 TYR n 
3 1111 GLU n 
3 1112 PRO n 
3 1113 GLN n 
3 1114 ILE n 
3 1115 ILE n 
3 1116 THR n 
3 1117 THR n 
3 1118 ASP n 
3 1119 ASN n 
3 1120 THR n 
3 1121 PHE n 
3 1122 VAL n 
3 1123 SER n 
3 1124 GLY n 
3 1125 ASN n 
3 1126 CYS n 
3 1127 ASP n 
3 1128 VAL n 
3 1129 VAL n 
3 1130 ILE n 
3 1131 GLY n 
3 1132 ILE n 
3 1133 VAL n 
3 1134 ASN n 
3 1135 ASN n 
3 1136 THR n 
3 1137 VAL n 
3 1138 TYR n 
3 1139 ASP n 
3 1140 PRO n 
3 1141 LEU n 
3 1142 GLN n 
3 1143 PRO n 
3 1144 GLU n 
3 1145 LEU n 
3 1146 ASP n 
3 1147 SER n 
3 1148 PHE n 
3 1149 LYS n 
3 1150 GLU n 
3 1151 GLU n 
3 1152 LEU n 
3 1153 ASP n 
3 1154 LYS n 
3 1155 TYR n 
3 1156 PHE n 
3 1157 LYS n 
3 1158 ASN n 
3 1159 HIS n 
3 1160 THR n 
3 1161 SER n 
3 1162 PRO n 
3 1163 ASP n 
3 1164 VAL n 
3 1165 ASP n 
3 1166 LEU n 
3 1167 GLY n 
3 1168 ASP n 
3 1169 ILE n 
3 1170 SER n 
3 1171 GLY n 
3 1172 ILE n 
3 1173 ASN n 
3 1174 ALA n 
3 1175 SER n 
3 1176 VAL n 
3 1177 VAL n 
3 1178 ASN n 
3 1179 ILE n 
3 1180 GLN n 
3 1181 LYS n 
3 1182 GLU n 
3 1183 ILE n 
3 1184 ASP n 
3 1185 ARG n 
3 1186 LEU n 
3 1187 ASN n 
3 1188 GLU n 
3 1189 VAL n 
3 1190 ALA n 
3 1191 LYS n 
3 1192 ASN n 
3 1193 LEU n 
3 1194 ASN n 
3 1195 GLU n 
3 1196 SER n 
3 1197 LEU n 
3 1198 ILE n 
3 1199 ASP n 
3 1200 LEU n 
3 1201 GLN n 
3 1202 GLU n 
3 1203 LEU n 
3 1204 GLY n 
3 1205 LYS n 
3 1206 TYR n 
3 1207 GLU n 
3 1208 GLN n 
3 1209 GLY n 
3 1210 SER n 
3 1211 GLY n 
3 1212 TYR n 
3 1213 ILE n 
3 1214 PRO n 
3 1215 GLU n 
3 1216 ALA n 
3 1217 PRO n 
3 1218 ARG n 
3 1219 ASP n 
3 1220 GLY n 
3 1221 GLN n 
3 1222 ALA n 
3 1223 TYR n 
3 1224 VAL n 
3 1225 ARG n 
3 1226 LYS n 
3 1227 ASP n 
3 1228 GLY n 
3 1229 GLU n 
3 1230 TRP n 
3 1231 VAL n 
3 1232 LEU n 
3 1233 LEU n 
3 1234 SER n 
3 1235 THR n 
3 1236 PHE n 
3 1237 LEU n 
3 1238 GLY n 
3 1239 ARG n 
3 1240 SER n 
3 1241 LEU n 
3 1242 GLU n 
3 1243 VAL n 
3 1244 LEU n 
3 1245 PHE n 
3 1246 GLN n 
3 1247 GLY n 
3 1248 PRO n 
3 1249 GLY n 
3 1250 SER n 
3 1251 GLY n 
3 1252 GLY n 
3 1253 LEU n 
3 1254 ASN n 
3 1255 ASP n 
3 1256 ILE n 
3 1257 PHE n 
3 1258 GLU n 
3 1259 ALA n 
3 1260 GLN n 
3 1261 LYS n 
3 1262 ILE n 
3 1263 GLU n 
3 1264 TRP n 
3 1265 HIS n 
3 1266 GLU n 
3 1267 GLY n 
3 1268 SER n 
3 1269 GLY n 
3 1270 HIS n 
3 1271 HIS n 
3 1272 HIS n 
3 1273 HIS n 
3 1274 HIS n 
3 1275 HIS n 
3 1276 HIS n 
3 1277 HIS 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' 1 105  ?                       ? ?      ? ? ? ? ? ? 'Homo sapiens' 9606    ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 125  ?                       ? ?      ? ? ? ? ? ? 'Homo sapiens' 9606    ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 1277 '2019-nCoV, SARS-CoV-2' ? 'S, 2' ? ? ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
? ? ? 
# 
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 7SOF        7SOF   ? 1 ? 1 
2 PDB 7SOF        7SOF   ? 2 ? 1 
3 UNP SPIKE_SARS2 P0DTC2 ? 3 
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFD
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRV
QPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSF
VIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPC
NGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFL
PFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGS
NVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTI
SVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGF
NFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAG
TITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALN
TLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRV
DFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNT
FVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDL
QELGKYEQ
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7SOF L 1 ? 105  ? 7SOF   1 ? 105  ? 1 105  
2 2 7SOF H 1 ? 125  ? 7SOF   1 ? 125  ? 1 125  
3 3 7SOF A 1 ? 1208 ? P0DTC2 1 ? 1208 ? 1 1208 
# 
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 
3 7SOF ILE A 95   ? UNP P0DTC2 THR 95   variant          95   1  
3 7SOF ASP A 142  ? UNP P0DTC2 GLY 142  variant          142  2  
3 7SOF LYS A 154  ? UNP P0DTC2 GLU 154  variant          154  3  
3 7SOF CYS A 383  ? UNP P0DTC2 SER 383  variant          383  4  
3 7SOF ARG A 452  ? UNP P0DTC2 LEU 452  variant          452  5  
3 7SOF GLN A 484  ? UNP P0DTC2 GLU 484  variant          484  6  
3 7SOF GLY A 614  ? UNP P0DTC2 ASP 614  variant          614  7  
3 7SOF ARG A 681  ? UNP P0DTC2 PRO 681  variant          681  8  
3 7SOF PRO A 817  ? UNP P0DTC2 PHE 817  variant          817  9  
3 7SOF PRO A 892  ? UNP P0DTC2 ALA 892  variant          892  10 
3 7SOF PRO A 899  ? UNP P0DTC2 ALA 899  variant          899  11 
3 7SOF PRO A 942  ? UNP P0DTC2 ALA 942  variant          942  12 
3 7SOF CYS A 985  ? UNP P0DTC2 ASP 985  variant          985  13 
3 7SOF PRO A 986  ? UNP P0DTC2 LYS 986  variant          986  14 
3 7SOF PRO A 987  ? UNP P0DTC2 VAL 987  variant          987  15 
3 7SOF HIS A 1071 ? UNP P0DTC2 GLN 1071 variant          1071 16 
3 7SOF GLY A 1209 ? UNP P0DTC2 ?   ?    'expression tag' 1209 17 
3 7SOF SER A 1210 ? UNP P0DTC2 ?   ?    'expression tag' 1210 18 
3 7SOF GLY A 1211 ? UNP P0DTC2 ?   ?    'expression tag' 1211 19 
3 7SOF TYR A 1212 ? UNP P0DTC2 ?   ?    'expression tag' 1212 20 
3 7SOF ILE A 1213 ? UNP P0DTC2 ?   ?    'expression tag' 1213 21 
3 7SOF PRO A 1214 ? UNP P0DTC2 ?   ?    'expression tag' 1214 22 
3 7SOF GLU A 1215 ? UNP P0DTC2 ?   ?    'expression tag' 1215 23 
3 7SOF ALA A 1216 ? UNP P0DTC2 ?   ?    'expression tag' 1216 24 
3 7SOF PRO A 1217 ? UNP P0DTC2 ?   ?    'expression tag' 1217 25 
3 7SOF ARG A 1218 ? UNP P0DTC2 ?   ?    'expression tag' 1218 26 
3 7SOF ASP A 1219 ? UNP P0DTC2 ?   ?    'expression tag' 1219 27 
3 7SOF GLY A 1220 ? UNP P0DTC2 ?   ?    'expression tag' 1220 28 
3 7SOF GLN A 1221 ? UNP P0DTC2 ?   ?    'expression tag' 1221 29 
3 7SOF ALA A 1222 ? UNP P0DTC2 ?   ?    'expression tag' 1222 30 
3 7SOF TYR A 1223 ? UNP P0DTC2 ?   ?    'expression tag' 1223 31 
3 7SOF VAL A 1224 ? UNP P0DTC2 ?   ?    'expression tag' 1224 32 
3 7SOF ARG A 1225 ? UNP P0DTC2 ?   ?    'expression tag' 1225 33 
3 7SOF LYS A 1226 ? UNP P0DTC2 ?   ?    'expression tag' 1226 34 
3 7SOF ASP A 1227 ? UNP P0DTC2 ?   ?    'expression tag' 1227 35 
3 7SOF GLY A 1228 ? UNP P0DTC2 ?   ?    'expression tag' 1228 36 
3 7SOF GLU A 1229 ? UNP P0DTC2 ?   ?    'expression tag' 1229 37 
3 7SOF TRP A 1230 ? UNP P0DTC2 ?   ?    'expression tag' 1230 38 
3 7SOF VAL A 1231 ? UNP P0DTC2 ?   ?    'expression tag' 1231 39 
3 7SOF LEU A 1232 ? UNP P0DTC2 ?   ?    'expression tag' 1232 40 
3 7SOF LEU A 1233 ? UNP P0DTC2 ?   ?    'expression tag' 1233 41 
3 7SOF SER A 1234 ? UNP P0DTC2 ?   ?    'expression tag' 1234 42 
3 7SOF THR A 1235 ? UNP P0DTC2 ?   ?    'expression tag' 1235 43 
3 7SOF PHE A 1236 ? UNP P0DTC2 ?   ?    'expression tag' 1236 44 
3 7SOF LEU A 1237 ? UNP P0DTC2 ?   ?    'expression tag' 1237 45 
3 7SOF GLY A 1238 ? UNP P0DTC2 ?   ?    'expression tag' 1238 46 
3 7SOF ARG A 1239 ? UNP P0DTC2 ?   ?    'expression tag' 1239 47 
3 7SOF SER A 1240 ? UNP P0DTC2 ?   ?    'expression tag' 1240 48 
3 7SOF LEU A 1241 ? UNP P0DTC2 ?   ?    'expression tag' 1241 49 
3 7SOF GLU A 1242 ? UNP P0DTC2 ?   ?    'expression tag' 1242 50 
3 7SOF VAL A 1243 ? UNP P0DTC2 ?   ?    'expression tag' 1243 51 
3 7SOF LEU A 1244 ? UNP P0DTC2 ?   ?    'expression tag' 1244 52 
3 7SOF PHE A 1245 ? UNP P0DTC2 ?   ?    'expression tag' 1245 53 
3 7SOF GLN A 1246 ? UNP P0DTC2 ?   ?    'expression tag' 1246 54 
3 7SOF GLY A 1247 ? UNP P0DTC2 ?   ?    'expression tag' 1247 55 
3 7SOF PRO A 1248 ? UNP P0DTC2 ?   ?    'expression tag' 1248 56 
3 7SOF GLY A 1249 ? UNP P0DTC2 ?   ?    'expression tag' 1249 57 
3 7SOF SER A 1250 ? UNP P0DTC2 ?   ?    'expression tag' 1250 58 
3 7SOF GLY A 1251 ? UNP P0DTC2 ?   ?    'expression tag' 1251 59 
3 7SOF GLY A 1252 ? UNP P0DTC2 ?   ?    'expression tag' 1252 60 
3 7SOF LEU A 1253 ? UNP P0DTC2 ?   ?    'expression tag' 1253 61 
3 7SOF ASN A 1254 ? UNP P0DTC2 ?   ?    'expression tag' 1254 62 
3 7SOF ASP A 1255 ? UNP P0DTC2 ?   ?    'expression tag' 1255 63 
3 7SOF ILE A 1256 ? UNP P0DTC2 ?   ?    'expression tag' 1256 64 
3 7SOF PHE A 1257 ? UNP P0DTC2 ?   ?    'expression tag' 1257 65 
3 7SOF GLU A 1258 ? UNP P0DTC2 ?   ?    'expression tag' 1258 66 
3 7SOF ALA A 1259 ? UNP P0DTC2 ?   ?    'expression tag' 1259 67 
3 7SOF GLN A 1260 ? UNP P0DTC2 ?   ?    'expression tag' 1260 68 
3 7SOF LYS A 1261 ? UNP P0DTC2 ?   ?    'expression tag' 1261 69 
3 7SOF ILE A 1262 ? UNP P0DTC2 ?   ?    'expression tag' 1262 70 
3 7SOF GLU A 1263 ? UNP P0DTC2 ?   ?    'expression tag' 1263 71 
3 7SOF TRP A 1264 ? UNP P0DTC2 ?   ?    'expression tag' 1264 72 
3 7SOF HIS A 1265 ? UNP P0DTC2 ?   ?    'expression tag' 1265 73 
3 7SOF GLU A 1266 ? UNP P0DTC2 ?   ?    'expression tag' 1266 74 
3 7SOF GLY A 1267 ? UNP P0DTC2 ?   ?    'expression tag' 1267 75 
3 7SOF SER A 1268 ? UNP P0DTC2 ?   ?    'expression tag' 1268 76 
3 7SOF GLY A 1269 ? UNP P0DTC2 ?   ?    'expression tag' 1269 77 
3 7SOF HIS A 1270 ? UNP P0DTC2 ?   ?    'expression tag' 1270 78 
3 7SOF HIS A 1271 ? UNP P0DTC2 ?   ?    'expression tag' 1271 79 
3 7SOF HIS A 1272 ? UNP P0DTC2 ?   ?    'expression tag' 1272 80 
3 7SOF HIS A 1273 ? UNP P0DTC2 ?   ?    'expression tag' 1273 81 
3 7SOF HIS A 1274 ? UNP P0DTC2 ?   ?    'expression tag' 1274 82 
3 7SOF HIS A 1275 ? UNP P0DTC2 ?   ?    'expression tag' 1275 83 
3 7SOF HIS A 1276 ? UNP P0DTC2 ?   ?    'expression tag' 1276 84 
3 7SOF HIS A 1277 ? UNP P0DTC2 ?   ?    'expression tag' 1277 85 
# 
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 
BMA 'D-saccharide, beta linking' . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
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 
# 
_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                   7SOF 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     7SOF 
_struct.title                        'SARS-CoV-2 S NTD B.1.617.1 kappa variant S2X303 Local Refinement' 
_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        7SOF 
_struct_keywords.text            
;kappa, spike, antibody, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, VIRAL PROTEIN-IMMUNE SYSTEM complex
;
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
# 
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 GLN A 78  ? GLU A 82  ? GLN L 78  GLU L 82  5 ? 5  
HELX_P HELX_P2 AA2 LEU B 65  ? SER B 67  ? LEU H 65  SER H 67  5 ? 3  
HELX_P HELX_P3 AA3 ASP B 88  ? THR B 92  ? ASP H 88  THR H 92  5 ? 5  
HELX_P HELX_P4 AA4 ASP C 294 ? LEU C 303 ? ASP A 294 LEU A 303 1 ? 10 
# 
_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 22  SG  ? ? ? 1_555 A CYS 87  SG ? ? L CYS 22  L CYS 87   1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf2 disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 97  SG ? ? H CYS 22  H CYS 97   1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf3 disulf ?    ? C CYS 15  SG  ? ? ? 1_555 C CYS 136 SG ? ? A CYS 15  A CYS 136  1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf4 disulf ?    ? C CYS 131 SG  ? ? ? 1_555 C CYS 166 SG ? ? A CYS 131 A CYS 166  1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf5 disulf ?    ? C CYS 291 SG  ? ? ? 1_555 C CYS 301 SG ? ? A CYS 291 A CYS 301  1_555 ? ? ? ? ? ? ? 2.021 ? ?               
covale1 covale one  ? C ASN 17  ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 17  A NAG 1306 1_555 ? ? ? ? ? ? ? 1.494 ? N-Glycosylation 
covale2 covale one  ? C ASN 61  ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 61  A NAG 1301 1_555 ? ? ? ? ? ? ? 1.494 ? N-Glycosylation 
covale3 covale one  ? C ASN 122 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 122 B NAG 1    1_555 ? ? ? ? ? ? ? 1.501 ? N-Glycosylation 
covale4 covale one  ? C ASN 149 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 149 A NAG 1305 1_555 ? ? ? ? ? ? ? 1.496 ? N-Glycosylation 
covale5 covale one  ? C ASN 165 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 165 A NAG 1303 1_555 ? ? ? ? ? ? ? 1.479 ? N-Glycosylation 
covale6 covale one  ? C ASN 234 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 234 A NAG 1304 1_555 ? ? ? ? ? ? ? 1.497 ? N-Glycosylation 
covale7 covale one  ? C ASN 282 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 282 A NAG 1302 1_555 ? ? ? ? ? ? ? 1.495 ? N-Glycosylation 
covale8 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? B NAG 1   B NAG 2    1_555 ? ? ? ? ? ? ? 1.490 ? ?               
covale9 covale both ? D NAG .   O4  ? ? ? 1_555 D BMA .   C1 ? ? B NAG 2   B BMA 3    1_555 ? ? ? ? ? ? ? 1.501 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5  ? 
AA2 ? 3  ? 
AA3 ? 4  ? 
AA4 ? 13 ? 
AA5 ? 7  ? 
AA6 ? 3  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? parallel      
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA4 1  7  ? parallel      
AA4 2  3  ? anti-parallel 
AA4 2  5  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA4 5  6  ? anti-parallel 
AA4 5  7  ? anti-parallel 
AA4 5  12 ? anti-parallel 
AA4 8  13 ? anti-parallel 
AA4 9  10 ? anti-parallel 
AA4 9  13 ? anti-parallel 
AA4 10 11 ? anti-parallel 
AA4 11 12 ? anti-parallel 
AA4 11 13 ? parallel      
AA5 1  2  ? anti-parallel 
AA5 2  3  ? anti-parallel 
AA5 3  4  ? anti-parallel 
AA5 4  5  ? anti-parallel 
AA5 5  6  ? anti-parallel 
AA5 6  7  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA6 2  3  ? 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  SER A 9   ? SER A 11  ? SER L 9   SER L 11  
AA1 2  THR A 101 ? THR A 104 ? THR L 101 THR L 104 
AA1 3  ALA A 83  ? ALA A 89  ? ALA L 83  ALA L 89  
AA1 4  ALA A 32  ? GLN A 37  ? ALA L 32  GLN L 37  
AA1 5  ILE A 44  ? ILE A 47  ? ILE L 44  ILE L 47  
AA2 1  ALA A 18  ? SER A 23  ? ALA L 18  SER L 23  
AA2 2  THR A 69  ? ILE A 74  ? THR L 69  ILE L 74  
AA2 3  PHE A 61  ? SER A 66  ? PHE L 61  SER L 66  
AA3 1  THR B 3   ? SER B 7   ? THR H 3   SER H 7   
AA3 2  LEU B 18  ? SER B 25  ? LEU H 18  SER H 25  
AA3 3  GLN B 79  ? MET B 84  ? GLN H 79  MET H 84  
AA3 4  LEU B 69  ? ASP B 74  ? LEU H 69  ASP H 74  
AA4 1  LEU B 11  ? VAL B 12  ? LEU H 11  VAL H 12  
AA4 2  GLY B 35  ? GLN B 41  ? GLY H 35  GLN H 41  
AA4 3  GLU B 48  ? TYR B 54  ? GLU H 48  TYR H 54  
AA4 4  LYS B 59  ? TYR B 61  ? LYS H 59  TYR H 61  
AA4 5  ALA B 93  ? GLY B 105 ? ALA H 93  GLY H 105 
AA4 6  LEU B 108 ? TRP B 115 ? LEU H 108 TRP H 115 
AA4 7  THR B 119 ? VAL B 123 ? THR H 119 VAL H 123 
AA4 8  VAL C 83  ? PRO C 85  ? VAL A 83  PRO A 85  
AA4 9  ILE C 101 ? GLY C 107 ? ILE A 101 GLY A 107 
AA4 10 SER C 116 ? ASN C 121 ? SER A 116 ASN A 121 
AA4 11 VAL C 126 ? TYR C 145 ? VAL A 126 TYR A 145 
AA4 12 SER C 151 ? SER C 172 ? SER A 151 SER A 172 
AA4 13 ARG C 237 ? LEU C 244 ? ARG A 237 LEU A 244 
AA5 1  ALA C 27  ? SER C 31  ? ALA A 27  SER A 31  
AA5 2  SER C 60  ? ALA C 67  ? SER A 60  ALA A 67  
AA5 3  ALA C 263 ? TYR C 269 ? ALA A 263 TYR A 269 
AA5 4  VAL C 90  ? GLU C 96  ? VAL A 90  GLU A 96  
AA5 5  LYS C 187 ? ILE C 197 ? LYS A 187 ILE A 197 
AA5 6  TYR C 200 ? ILE C 210 ? TYR A 200 ILE A 210 
AA5 7  GLU C 224 ? PRO C 230 ? GLU A 224 PRO A 230 
AA6 1  VAL C 47  ? PHE C 55  ? VAL A 47  PHE A 55  
AA6 2  GLN C 271 ? TYR C 279 ? GLN A 271 TYR A 279 
AA6 3  ILE C 285 ? ASP C 290 ? ILE A 285 ASP A 290 
# 
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 VAL A 10  ? N VAL L 10  O THR A 104 ? O THR L 104 
AA1 2  3  O THR A 101 ? O THR L 101 N TYR A 85  ? N TYR L 85  
AA1 3  4  O TYR A 86  ? O TYR L 86  N TYR A 35  ? N TYR L 35  
AA1 4  5  N TRP A 34  ? N TRP L 34  O VAL A 46  ? O VAL L 46  
AA2 1  2  N CYS A 22  ? N CYS L 22  O ALA A 70  ? O ALA L 70  
AA2 2  3  O THR A 73  ? O THR L 73  N SER A 62  ? N SER L 62  
AA3 1  2  N LYS B 5   ? N LYS H 5   O LYS B 23  ? O LYS H 23  
AA3 2  3  N CYS B 22  ? N CYS H 22  O VAL B 80  ? O VAL H 80  
AA3 3  4  O GLN B 79  ? O GLN H 79  N ASP B 74  ? N ASP H 74  
AA4 1  7  N VAL B 12  ? N VAL H 12  O THR B 122 ? O THR H 122 
AA4 2  3  N TRP B 38  ? N TRP H 38  O ALA B 51  ? O ALA H 51  
AA4 2  5  N ILE B 39  ? N ILE H 39  O TYR B 96  ? O TYR H 96  
AA4 3  4  N LEU B 52  ? N LEU H 52  O LEU B 60  ? O LEU H 60  
AA4 5  6  N TRP B 103 ? N TRP H 103 O LEU B 108 ? O LEU H 108 
AA4 5  7  N TYR B 95  ? N TYR H 95  O THR B 119 ? O THR H 119 
AA4 5  12 N PHE B 104 ? N PHE H 104 O TRP C 152 ? O TRP A 152 
AA4 8  13 N LEU C 84  ? N LEU A 84  O PHE C 238 ? O PHE A 238 
AA4 9  10 N PHE C 106 ? N PHE A 106 O LEU C 117 ? O LEU A 117 
AA4 9  13 N GLY C 103 ? N GLY A 103 O LEU C 241 ? O LEU A 241 
AA4 10 11 N LEU C 118 ? N LEU A 118 O LYS C 129 ? O LYS A 129 
AA4 11 12 N GLU C 132 ? N GLU A 132 O ASN C 164 ? O ASN A 164 
AA4 11 13 N VAL C 143 ? N VAL A 143 O LEU C 244 ? O LEU A 244 
AA5 1  2  N ALA C 27  ? N ALA A 27  O TRP C 64  ? O TRP A 64  
AA5 2  3  N ALA C 67  ? N ALA A 67  O ALA C 263 ? O ALA A 263 
AA5 3  4  O TYR C 266 ? O TYR A 266 N ALA C 93  ? N ALA A 93  
AA5 4  5  N PHE C 92  ? N PHE A 92  O PHE C 192 ? O PHE A 192 
AA5 5  6  N LEU C 189 ? N LEU A 189 O THR C 208 ? O THR A 208 
AA5 6  7  N ILE C 203 ? N ILE A 203 O LEU C 226 ? O LEU A 226 
AA6 1  2  N HIS C 49  ? N HIS A 49  O LEU C 277 ? O LEU A 277 
AA6 2  3  N LYS C 278 ? N LYS A 278 O ASP C 287 ? O ASP A 287 
# 
_atom_sites.entry_id                    7SOF 
_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.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   . SER A 1 1   ? 223.586 129.002 233.796 1.00 31.29 ? 1    SER L N   1 
ATOM   2    C CA  . SER A 1 1   ? 224.538 129.561 234.747 1.00 31.23 ? 1    SER L CA  1 
ATOM   3    C C   . SER A 1 1   ? 225.972 129.236 234.320 1.00 30.93 ? 1    SER L C   1 
ATOM   4    O O   . SER A 1 1   ? 226.189 128.416 233.424 1.00 31.14 ? 1    SER L O   1 
ATOM   5    C CB  . SER A 1 1   ? 224.251 129.032 236.150 1.00 31.60 ? 1    SER L CB  1 
ATOM   6    N N   . TYR A 1 2   ? 226.946 129.891 234.962 1.00 31.01 ? 2    TYR L N   1 
ATOM   7    C CA  . TYR A 1 2   ? 228.366 129.690 234.679 1.00 31.48 ? 2    TYR L CA  1 
ATOM   8    C C   . TYR A 1 2   ? 228.886 128.443 235.385 1.00 31.56 ? 2    TYR L C   1 
ATOM   9    O O   . TYR A 1 2   ? 228.673 128.266 236.585 1.00 31.57 ? 2    TYR L O   1 
ATOM   10   C CB  . TYR A 1 2   ? 229.157 130.933 235.097 1.00 31.39 ? 2    TYR L CB  1 
ATOM   11   C CG  . TYR A 1 2   ? 230.646 130.841 234.881 1.00 31.62 ? 2    TYR L CG  1 
ATOM   12   C CD1 . TYR A 1 2   ? 231.164 130.809 233.597 1.00 31.52 ? 2    TYR L CD1 1 
ATOM   13   C CD2 . TYR A 1 2   ? 231.496 130.812 235.969 1.00 31.55 ? 2    TYR L CD2 1 
ATOM   14   C CE1 . TYR A 1 2   ? 232.531 130.745 233.407 1.00 31.83 ? 2    TYR L CE1 1 
ATOM   15   C CE2 . TYR A 1 2   ? 232.856 130.752 235.775 1.00 31.91 ? 2    TYR L CE2 1 
ATOM   16   C CZ  . TYR A 1 2   ? 233.374 130.717 234.506 1.00 32.34 ? 2    TYR L CZ  1 
ATOM   17   O OH  . TYR A 1 2   ? 234.735 130.662 234.330 1.00 33.06 ? 2    TYR L OH  1 
ATOM   18   N N   . GLU A 1 3   ? 229.546 127.568 234.632 1.00 31.54 ? 3    GLU L N   1 
ATOM   19   C CA  . GLU A 1 3   ? 230.066 126.323 235.185 1.00 31.22 ? 3    GLU L CA  1 
ATOM   20   C C   . GLU A 1 3   ? 231.260 126.591 236.086 1.00 31.31 ? 3    GLU L C   1 
ATOM   21   O O   . GLU A 1 3   ? 232.206 127.270 235.687 1.00 31.61 ? 3    GLU L O   1 
ATOM   22   C CB  . GLU A 1 3   ? 230.467 125.367 234.060 1.00 30.76 ? 3    GLU L CB  1 
ATOM   23   N N   . LEU A 1 4   ? 231.217 126.061 237.303 1.00 30.85 ? 4    LEU L N   1 
ATOM   24   C CA  . LEU A 1 4   ? 232.290 126.312 238.249 1.00 30.57 ? 4    LEU L CA  1 
ATOM   25   C C   . LEU A 1 4   ? 232.433 125.133 239.217 1.00 30.46 ? 4    LEU L C   1 
ATOM   26   O O   . LEU A 1 4   ? 231.482 124.765 239.907 1.00 30.58 ? 4    LEU L O   1 
ATOM   27   C CB  . LEU A 1 4   ? 231.983 127.624 238.985 1.00 30.77 ? 4    LEU L CB  1 
ATOM   28   C CG  . LEU A 1 4   ? 233.094 128.243 239.803 1.00 29.93 ? 4    LEU L CG  1 
ATOM   29   C CD1 . LEU A 1 4   ? 234.235 128.650 238.873 1.00 31.51 ? 4    LEU L CD1 1 
ATOM   30   C CD2 . LEU A 1 4   ? 232.548 129.463 240.525 1.00 29.97 ? 4    LEU L CD2 1 
ATOM   31   N N   . THR A 1 5   ? 233.607 124.504 239.221 1.00 30.33 ? 5    THR L N   1 
ATOM   32   C CA  . THR A 1 5   ? 233.814 123.261 239.966 1.00 29.54 ? 5    THR L CA  1 
ATOM   33   C C   . THR A 1 5   ? 234.725 123.397 241.183 1.00 29.99 ? 5    THR L C   1 
ATOM   34   O O   . THR A 1 5   ? 235.830 123.928 241.095 1.00 30.59 ? 5    THR L O   1 
ATOM   35   C CB  . THR A 1 5   ? 234.387 122.169 239.041 1.00 30.18 ? 5    THR L CB  1 
ATOM   36   O OG1 . THR A 1 5   ? 233.448 121.884 237.999 1.00 31.42 ? 5    THR L OG1 1 
ATOM   37   C CG2 . THR A 1 5   ? 234.672 120.893 239.824 1.00 29.52 ? 5    THR L CG2 1 
ATOM   38   N N   . GLN A 1 6   ? 234.270 122.846 242.306 1.00 29.66 ? 6    GLN L N   1 
ATOM   39   C CA  . GLN A 1 6   ? 235.066 122.761 243.530 1.00 29.83 ? 6    GLN L CA  1 
ATOM   40   C C   . GLN A 1 6   ? 235.172 121.305 243.989 1.00 30.04 ? 6    GLN L C   1 
ATOM   41   O O   . GLN A 1 6   ? 234.284 120.508 243.692 1.00 30.50 ? 6    GLN L O   1 
ATOM   42   C CB  . GLN A 1 6   ? 234.434 123.589 244.650 1.00 29.85 ? 6    GLN L CB  1 
ATOM   43   C CG  . GLN A 1 6   ? 234.478 125.072 244.439 1.00 29.68 ? 6    GLN L CG  1 
ATOM   44   C CD  . GLN A 1 6   ? 233.834 125.830 245.588 1.00 29.89 ? 6    GLN L CD  1 
ATOM   45   O OE1 . GLN A 1 6   ? 232.852 126.558 245.401 1.00 29.55 ? 6    GLN L OE1 1 
ATOM   46   N NE2 . GLN A 1 6   ? 234.370 125.647 246.790 1.00 30.44 ? 6    GLN L NE2 1 
ATOM   47   N N   . PRO A 1 7   ? 236.245 120.939 244.701 1.00 29.93 ? 7    PRO L N   1 
ATOM   48   C CA  . PRO A 1 7   ? 236.386 119.715 245.469 1.00 30.31 ? 7    PRO L CA  1 
ATOM   49   C C   . PRO A 1 7   ? 235.290 119.660 246.525 1.00 30.52 ? 7    PRO L C   1 
ATOM   50   O O   . PRO A 1 7   ? 234.929 120.695 247.077 1.00 30.59 ? 7    PRO L O   1 
ATOM   51   C CB  . PRO A 1 7   ? 237.773 119.877 246.106 1.00 30.36 ? 7    PRO L CB  1 
ATOM   52   C CG  . PRO A 1 7   ? 238.507 120.831 245.190 1.00 29.88 ? 7    PRO L CG  1 
ATOM   53   C CD  . PRO A 1 7   ? 237.440 121.777 244.670 1.00 29.94 ? 7    PRO L CD  1 
ATOM   54   N N   . PRO A 1 8   ? 234.755 118.477 246.828 1.00 30.44 ? 8    PRO L N   1 
ATOM   55   C CA  . PRO A 1 8   ? 233.704 118.254 247.803 1.00 29.92 ? 8    PRO L CA  1 
ATOM   56   C C   . PRO A 1 8   ? 234.165 118.499 249.238 1.00 31.06 ? 8    PRO L C   1 
ATOM   57   O O   . PRO A 1 8   ? 233.364 118.894 250.088 1.00 31.27 ? 8    PRO L O   1 
ATOM   58   C CB  . PRO A 1 8   ? 233.350 116.779 247.566 1.00 30.81 ? 8    PRO L CB  1 
ATOM   59   C CG  . PRO A 1 8   ? 234.598 116.170 246.940 1.00 30.36 ? 8    PRO L CG  1 
ATOM   60   C CD  . PRO A 1 8   ? 235.223 117.286 246.131 1.00 30.05 ? 8    PRO L CD  1 
ATOM   61   N N   . SER A 1 9   ? 235.455 118.302 249.507 1.00 31.30 ? 9    SER L N   1 
ATOM   62   C CA  . SER A 1 9   ? 235.965 118.511 250.857 1.00 32.05 ? 9    SER L CA  1 
ATOM   63   C C   . SER A 1 9   ? 237.484 118.612 250.916 1.00 32.81 ? 9    SER L C   1 
ATOM   64   O O   . SER A 1 9   ? 238.196 118.079 250.062 1.00 32.67 ? 9    SER L O   1 
ATOM   65   C CB  . SER A 1 9   ? 235.508 117.389 251.769 1.00 32.56 ? 9    SER L CB  1 
ATOM   66   N N   . VAL A 1 10  ? 237.961 119.262 251.972 1.00 33.22 ? 10   VAL L N   1 
ATOM   67   C CA  . VAL A 1 10  ? 239.374 119.334 252.322 1.00 34.14 ? 10   VAL L CA  1 
ATOM   68   C C   . VAL A 1 10  ? 239.549 119.048 253.808 1.00 35.07 ? 10   VAL L C   1 
ATOM   69   O O   . VAL A 1 10  ? 238.782 119.544 254.631 1.00 35.45 ? 10   VAL L O   1 
ATOM   70   C CB  . VAL A 1 10  ? 239.951 120.721 251.967 1.00 34.24 ? 10   VAL L CB  1 
ATOM   71   C CG1 . VAL A 1 10  ? 241.381 120.862 252.481 1.00 35.73 ? 10   VAL L CG1 1 
ATOM   72   C CG2 . VAL A 1 10  ? 239.935 120.895 250.459 1.00 32.21 ? 10   VAL L CG2 1 
ATOM   73   N N   . SER A 1 11  ? 240.553 118.253 254.156 1.00 35.58 ? 11   SER L N   1 
ATOM   74   C CA  . SER A 1 11  ? 240.789 117.931 255.559 1.00 36.42 ? 11   SER L CA  1 
ATOM   75   C C   . SER A 1 11  ? 242.249 118.105 255.936 1.00 36.83 ? 11   SER L C   1 
ATOM   76   O O   . SER A 1 11  ? 243.133 117.482 255.348 1.00 37.42 ? 11   SER L O   1 
ATOM   77   C CB  . SER A 1 11  ? 240.348 116.512 255.852 1.00 36.07 ? 11   SER L CB  1 
ATOM   78   N N   . VAL A 1 12  ? 242.497 118.977 256.907 1.00 37.26 ? 12   VAL L N   1 
ATOM   79   C CA  . VAL A 1 12  ? 243.855 119.255 257.354 1.00 37.93 ? 12   VAL L CA  1 
ATOM   80   C C   . VAL A 1 12  ? 243.969 119.167 258.868 1.00 38.96 ? 12   VAL L C   1 
ATOM   81   O O   . VAL A 1 12  ? 242.974 119.271 259.581 1.00 38.95 ? 12   VAL L O   1 
ATOM   82   C CB  . VAL A 1 12  ? 244.294 120.660 256.899 1.00 38.77 ? 12   VAL L CB  1 
ATOM   83   N N   . SER A 1 13  ? 245.191 119.026 259.359 1.00 39.68 ? 13   SER L N   1 
ATOM   84   C CA  . SER A 1 13  ? 245.443 119.117 260.788 1.00 40.14 ? 13   SER L CA  1 
ATOM   85   C C   . SER A 1 13  ? 245.581 120.587 261.162 1.00 39.80 ? 13   SER L C   1 
ATOM   86   O O   . SER A 1 13  ? 245.970 121.401 260.324 1.00 40.01 ? 13   SER L O   1 
ATOM   87   C CB  . SER A 1 13  ? 246.708 118.352 261.143 1.00 40.39 ? 13   SER L CB  1 
ATOM   88   N N   . PRO A 1 14  ? 245.263 120.964 262.397 1.00 40.09 ? 14   PRO L N   1 
ATOM   89   C CA  . PRO A 1 14  ? 245.412 122.307 262.908 1.00 40.19 ? 14   PRO L CA  1 
ATOM   90   C C   . PRO A 1 14  ? 246.868 122.722 262.809 1.00 40.42 ? 14   PRO L C   1 
ATOM   91   O O   . PRO A 1 14  ? 247.765 121.961 263.171 1.00 40.77 ? 14   PRO L O   1 
ATOM   92   C CB  . PRO A 1 14  ? 244.924 122.177 264.359 1.00 40.78 ? 14   PRO L CB  1 
ATOM   93   C CG  . PRO A 1 14  ? 244.987 120.684 264.671 1.00 40.67 ? 14   PRO L CG  1 
ATOM   94   C CD  . PRO A 1 14  ? 244.735 119.992 263.349 1.00 39.86 ? 14   PRO L CD  1 
ATOM   95   N N   . GLY A 1 15  ? 247.098 123.925 262.299 1.00 39.81 ? 15   GLY L N   1 
ATOM   96   C CA  . GLY A 1 15  ? 248.447 124.439 262.117 1.00 39.98 ? 15   GLY L CA  1 
ATOM   97   C C   . GLY A 1 15  ? 248.947 124.241 260.687 1.00 39.58 ? 15   GLY L C   1 
ATOM   98   O O   . GLY A 1 15  ? 249.947 124.839 260.288 1.00 39.84 ? 15   GLY L O   1 
ATOM   99   N N   . GLN A 1 16  ? 248.247 123.416 259.910 1.00 39.54 ? 16   GLN L N   1 
ATOM   100  C CA  . GLN A 1 16  ? 248.645 123.167 258.528 1.00 39.33 ? 16   GLN L CA  1 
ATOM   101  C C   . GLN A 1 16  ? 247.998 124.158 257.576 1.00 38.56 ? 16   GLN L C   1 
ATOM   102  O O   . GLN A 1 16  ? 247.167 124.975 257.977 1.00 38.83 ? 16   GLN L O   1 
ATOM   103  C CB  . GLN A 1 16  ? 248.296 121.742 258.093 1.00 39.82 ? 16   GLN L CB  1 
ATOM   104  N N   . THR A 1 17  ? 248.378 124.079 256.307 1.00 37.90 ? 17   THR L N   1 
ATOM   105  C CA  . THR A 1 17  ? 247.816 124.969 255.304 1.00 37.53 ? 17   THR L CA  1 
ATOM   106  C C   . THR A 1 17  ? 246.757 124.262 254.468 1.00 37.50 ? 17   THR L C   1 
ATOM   107  O O   . THR A 1 17  ? 247.015 123.213 253.877 1.00 37.59 ? 17   THR L O   1 
ATOM   108  C CB  . THR A 1 17  ? 248.920 125.526 254.386 1.00 37.09 ? 17   THR L CB  1 
ATOM   109  O OG1 . THR A 1 17  ? 249.865 126.264 255.174 1.00 37.37 ? 17   THR L OG1 1 
ATOM   110  C CG2 . THR A 1 17  ? 248.321 126.445 253.339 1.00 36.40 ? 17   THR L CG2 1 
ATOM   111  N N   . ALA A 1 18  ? 245.565 124.847 254.418 1.00 37.00 ? 18   ALA L N   1 
ATOM   112  C CA  . ALA A 1 18  ? 244.477 124.297 253.619 1.00 36.00 ? 18   ALA L CA  1 
ATOM   113  C C   . ALA A 1 18  ? 244.486 124.924 252.236 1.00 35.37 ? 18   ALA L C   1 
ATOM   114  O O   . ALA A 1 18  ? 244.761 126.115 252.093 1.00 34.83 ? 18   ALA L O   1 
ATOM   115  C CB  . ALA A 1 18  ? 243.138 124.532 254.301 1.00 36.79 ? 18   ALA L CB  1 
ATOM   116  N N   . SER A 1 19  ? 244.160 124.132 251.220 1.00 34.27 ? 19   SER L N   1 
ATOM   117  C CA  . SER A 1 19  ? 244.103 124.646 249.857 1.00 33.32 ? 19   SER L CA  1 
ATOM   118  C C   . SER A 1 19  ? 242.856 124.173 249.126 1.00 33.28 ? 19   SER L C   1 
ATOM   119  O O   . SER A 1 19  ? 242.691 122.983 248.853 1.00 33.67 ? 19   SER L O   1 
ATOM   120  C CB  . SER A 1 19  ? 245.339 124.225 249.089 1.00 33.48 ? 19   SER L CB  1 
ATOM   121  O OG  . SER A 1 19  ? 245.273 124.655 247.757 1.00 32.64 ? 19   SER L OG  1 
ATOM   122  N N   . ILE A 1 20  ? 241.973 125.115 248.821 1.00 32.34 ? 20   ILE L N   1 
ATOM   123  C CA  . ILE A 1 20  ? 240.717 124.811 248.154 1.00 31.55 ? 20   ILE L CA  1 
ATOM   124  C C   . ILE A 1 20  ? 240.707 125.378 246.740 1.00 31.22 ? 20   ILE L C   1 
ATOM   125  O O   . ILE A 1 20  ? 240.812 126.589 246.547 1.00 31.34 ? 20   ILE L O   1 
ATOM   126  C CB  . ILE A 1 20  ? 239.531 125.379 248.953 1.00 31.30 ? 20   ILE L CB  1 
ATOM   127  C CG1 . ILE A 1 20  ? 239.532 124.779 250.373 1.00 31.50 ? 20   ILE L CG1 1 
ATOM   128  C CG2 . ILE A 1 20  ? 238.228 125.072 248.227 1.00 31.53 ? 20   ILE L CG2 1 
ATOM   129  C CD1 . ILE A 1 20  ? 238.588 125.455 251.339 1.00 34.06 ? 20   ILE L CD1 1 
ATOM   130  N N   . THR A 1 21  ? 240.596 124.500 245.751 1.00 30.74 ? 21   THR L N   1 
ATOM   131  C CA  . THR A 1 21  ? 240.654 124.923 244.356 1.00 30.04 ? 21   THR L CA  1 
ATOM   132  C C   . THR A 1 21  ? 239.268 125.247 243.804 1.00 30.47 ? 21   THR L C   1 
ATOM   133  O O   . THR A 1 21  ? 238.250 124.878 244.394 1.00 30.36 ? 21   THR L O   1 
ATOM   134  C CB  . THR A 1 21  ? 241.325 123.840 243.489 1.00 30.21 ? 21   THR L CB  1 
ATOM   135  N N   . CYS A 1 22  ? 239.243 125.944 242.662 1.00 30.54 ? 22   CYS L N   1 
ATOM   136  C CA  . CYS A 1 22  ? 238.021 126.317 241.959 1.00 30.61 ? 22   CYS L CA  1 
ATOM   137  C C   . CYS A 1 22  ? 238.288 126.454 240.462 1.00 31.42 ? 22   CYS L C   1 
ATOM   138  O O   . CYS A 1 22  ? 239.017 127.345 240.025 1.00 31.86 ? 22   CYS L O   1 
ATOM   139  C CB  . CYS A 1 22  ? 237.468 127.635 242.518 1.00 31.60 ? 22   CYS L CB  1 
ATOM   140  S SG  . CYS A 1 22  ? 235.931 128.186 241.762 1.00 31.65 ? 22   CYS L SG  1 
ATOM   141  N N   . SER A 1 23  ? 237.743 125.532 239.679 1.00 31.07 ? 23   SER L N   1 
ATOM   142  C CA  . SER A 1 23  ? 238.041 125.474 238.251 1.00 31.62 ? 23   SER L CA  1 
ATOM   143  C C   . SER A 1 23  ? 236.874 125.931 237.388 1.00 31.59 ? 23   SER L C   1 
ATOM   144  O O   . SER A 1 23  ? 235.731 125.520 237.596 1.00 31.53 ? 23   SER L O   1 
ATOM   145  C CB  . SER A 1 23  ? 238.438 124.066 237.863 1.00 32.08 ? 23   SER L CB  1 
ATOM   146  N N   . GLY A 1 24  ? 237.164 126.783 236.413 1.00 31.52 ? 24   GLY L N   1 
ATOM   147  C CA  . GLY A 1 24  ? 236.139 127.248 235.486 1.00 32.25 ? 24   GLY L CA  1 
ATOM   148  C C   . GLY A 1 24  ? 236.681 127.270 234.066 1.00 33.04 ? 24   GLY L C   1 
ATOM   149  O O   . GLY A 1 24  ? 237.771 126.764 233.802 1.00 33.41 ? 24   GLY L O   1 
ATOM   150  N N   . ASP A 1 25  ? 235.922 127.858 233.147 1.00 32.69 ? 25   ASP L N   1 
ATOM   151  C CA  . ASP A 1 25  ? 236.358 127.935 231.758 1.00 32.98 ? 25   ASP L CA  1 
ATOM   152  C C   . ASP A 1 25  ? 237.082 129.241 231.470 1.00 33.67 ? 25   ASP L C   1 
ATOM   153  O O   . ASP A 1 25  ? 237.975 129.291 230.624 1.00 33.73 ? 25   ASP L O   1 
ATOM   154  C CB  . ASP A 1 25  ? 235.166 127.806 230.806 1.00 32.99 ? 25   ASP L CB  1 
ATOM   155  N N   . LYS A 1 26  ? 236.664 130.307 232.147 1.00 33.44 ? 26   LYS L N   1 
ATOM   156  C CA  . LYS A 1 26  ? 237.166 131.644 231.857 1.00 33.32 ? 26   LYS L CA  1 
ATOM   157  C C   . LYS A 1 26  ? 237.620 132.395 233.105 1.00 33.36 ? 26   LYS L C   1 
ATOM   158  O O   . LYS A 1 26  ? 237.541 133.624 233.149 1.00 32.63 ? 26   LYS L O   1 
ATOM   159  C CB  . LYS A 1 26  ? 236.086 132.462 231.139 1.00 33.47 ? 26   LYS L CB  1 
ATOM   160  N N   . LEU A 1 27  ? 238.107 131.678 234.115 1.00 32.57 ? 27   LEU L N   1 
ATOM   161  C CA  . LEU A 1 27  ? 238.538 132.351 235.338 1.00 33.31 ? 27   LEU L CA  1 
ATOM   162  C C   . LEU A 1 27  ? 239.820 133.138 235.112 1.00 32.85 ? 27   LEU L C   1 
ATOM   163  O O   . LEU A 1 27  ? 240.189 133.983 235.924 1.00 32.25 ? 27   LEU L O   1 
ATOM   164  C CB  . LEU A 1 27  ? 238.752 131.356 236.485 1.00 32.53 ? 27   LEU L CB  1 
ATOM   165  C CG  . LEU A 1 27  ? 237.516 130.620 237.004 1.00 33.09 ? 27   LEU L CG  1 
ATOM   166  C CD1 . LEU A 1 27  ? 237.950 129.644 238.087 1.00 33.25 ? 27   LEU L CD1 1 
ATOM   167  C CD2 . LEU A 1 27  ? 236.510 131.609 237.552 1.00 31.98 ? 27   LEU L CD2 1 
ATOM   168  N N   . GLY A 1 28  ? 240.500 132.871 234.003 1.00 32.78 ? 28   GLY L N   1 
ATOM   169  C CA  . GLY A 1 28  ? 241.709 133.608 233.670 1.00 33.07 ? 28   GLY L CA  1 
ATOM   170  C C   . GLY A 1 28  ? 241.375 134.962 233.045 1.00 32.82 ? 28   GLY L C   1 
ATOM   171  O O   . GLY A 1 28  ? 242.260 135.794 232.844 1.00 32.34 ? 28   GLY L O   1 
ATOM   172  N N   . GLU A 1 29  ? 240.099 135.174 232.728 1.00 32.64 ? 29   GLU L N   1 
ATOM   173  C CA  . GLU A 1 29  ? 239.660 136.419 232.110 1.00 32.14 ? 29   GLU L CA  1 
ATOM   174  C C   . GLU A 1 29  ? 238.862 137.287 233.079 1.00 31.78 ? 29   GLU L C   1 
ATOM   175  O O   . GLU A 1 29  ? 238.903 138.514 232.996 1.00 31.23 ? 29   GLU L O   1 
ATOM   176  C CB  . GLU A 1 29  ? 238.820 136.127 230.867 1.00 32.75 ? 29   GLU L CB  1 
ATOM   177  N N   . THR A 1 30  ? 238.130 136.648 233.988 1.00 31.73 ? 30   THR L N   1 
ATOM   178  C CA  . THR A 1 30  ? 237.292 137.372 234.939 1.00 31.43 ? 30   THR L CA  1 
ATOM   179  C C   . THR A 1 30  ? 237.819 137.257 236.360 1.00 31.25 ? 30   THR L C   1 
ATOM   180  O O   . THR A 1 30  ? 238.852 136.636 236.603 1.00 31.33 ? 30   THR L O   1 
ATOM   181  C CB  . THR A 1 30  ? 235.837 136.878 234.901 1.00 31.19 ? 30   THR L CB  1 
ATOM   182  O OG1 . THR A 1 30  ? 235.016 137.782 235.650 1.00 32.29 ? 30   THR L OG1 1 
ATOM   183  C CG2 . THR A 1 30  ? 235.721 135.475 235.501 1.00 31.42 ? 30   THR L CG2 1 
ATOM   184  N N   . TYR A 1 31  ? 237.112 137.873 237.299 1.00 30.65 ? 31   TYR L N   1 
ATOM   185  C CA  . TYR A 1 31  ? 237.519 137.839 238.698 1.00 30.45 ? 31   TYR L CA  1 
ATOM   186  C C   . TYR A 1 31  ? 236.784 136.764 239.478 1.00 30.68 ? 31   TYR L C   1 
ATOM   187  O O   . TYR A 1 31  ? 235.591 136.541 239.277 1.00 31.18 ? 31   TYR L O   1 
ATOM   188  C CB  . TYR A 1 31  ? 237.284 139.190 239.365 1.00 29.43 ? 31   TYR L CB  1 
ATOM   189  C CG  . TYR A 1 31  ? 238.275 140.251 238.986 1.00 29.39 ? 31   TYR L CG  1 
ATOM   190  C CD1 . TYR A 1 31  ? 237.949 141.203 238.045 1.00 29.20 ? 31   TYR L CD1 1 
ATOM   191  C CD2 . TYR A 1 31  ? 239.514 140.276 239.594 1.00 29.64 ? 31   TYR L CD2 1 
ATOM   192  C CE1 . TYR A 1 31  ? 238.859 142.180 237.716 1.00 29.60 ? 31   TYR L CE1 1 
ATOM   193  C CE2 . TYR A 1 31  ? 240.422 141.251 239.269 1.00 29.85 ? 31   TYR L CE2 1 
ATOM   194  C CZ  . TYR A 1 31  ? 240.098 142.202 238.334 1.00 29.88 ? 31   TYR L CZ  1 
ATOM   195  O OH  . TYR A 1 31  ? 241.005 143.178 238.009 1.00 31.37 ? 31   TYR L OH  1 
ATOM   196  N N   . ALA A 1 32  ? 237.494 136.133 240.404 1.00 30.16 ? 32   ALA L N   1 
ATOM   197  C CA  . ALA A 1 32  ? 236.892 135.153 241.297 1.00 29.09 ? 32   ALA L CA  1 
ATOM   198  C C   . ALA A 1 32  ? 236.757 135.722 242.706 1.00 29.48 ? 32   ALA L C   1 
ATOM   199  O O   . ALA A 1 32  ? 237.518 136.603 243.108 1.00 29.81 ? 32   ALA L O   1 
ATOM   200  C CB  . ALA A 1 32  ? 237.722 133.880 241.318 1.00 30.21 ? 32   ALA L CB  1 
ATOM   201  N N   . SER A 1 33  ? 235.810 135.190 243.467 1.00 28.97 ? 33   SER L N   1 
ATOM   202  C CA  . SER A 1 33  ? 235.643 135.572 244.867 1.00 29.14 ? 33   SER L CA  1 
ATOM   203  C C   . SER A 1 33  ? 235.312 134.357 245.721 1.00 28.49 ? 33   SER L C   1 
ATOM   204  O O   . SER A 1 33  ? 234.871 133.329 245.207 1.00 30.35 ? 33   SER L O   1 
ATOM   205  C CB  . SER A 1 33  ? 234.550 136.611 245.002 1.00 29.01 ? 33   SER L CB  1 
ATOM   206  O OG  . SER A 1 33  ? 233.317 136.094 244.598 1.00 29.43 ? 33   SER L OG  1 
ATOM   207  N N   . TRP A 1 34  ? 235.543 134.471 247.026 1.00 29.27 ? 34   TRP L N   1 
ATOM   208  C CA  . TRP A 1 34  ? 235.288 133.368 247.945 1.00 29.64 ? 34   TRP L CA  1 
ATOM   209  C C   . TRP A 1 34  ? 234.466 133.786 249.153 1.00 28.85 ? 34   TRP L C   1 
ATOM   210  O O   . TRP A 1 34  ? 234.689 134.854 249.730 1.00 30.78 ? 34   TRP L O   1 
ATOM   211  C CB  . TRP A 1 34  ? 236.604 132.782 248.431 1.00 29.63 ? 34   TRP L CB  1 
ATOM   212  C CG  . TRP A 1 34  ? 237.391 132.115 247.362 1.00 29.92 ? 34   TRP L CG  1 
ATOM   213  C CD1 . TRP A 1 34  ? 238.220 132.709 246.463 1.00 30.43 ? 34   TRP L CD1 1 
ATOM   214  C CD2 . TRP A 1 34  ? 237.444 130.703 247.085 1.00 30.09 ? 34   TRP L CD2 1 
ATOM   215  N NE1 . TRP A 1 34  ? 238.778 131.768 245.644 1.00 30.56 ? 34   TRP L NE1 1 
ATOM   216  C CE2 . TRP A 1 34  ? 238.317 130.532 246.013 1.00 30.56 ? 34   TRP L CE2 1 
ATOM   217  C CE3 . TRP A 1 34  ? 236.834 129.585 247.658 1.00 30.47 ? 34   TRP L CE3 1 
ATOM   218  C CZ2 . TRP A 1 34  ? 238.601 129.286 245.497 1.00 30.90 ? 34   TRP L CZ2 1 
ATOM   219  C CZ3 . TRP A 1 34  ? 237.121 128.335 247.143 1.00 30.78 ? 34   TRP L CZ3 1 
ATOM   220  C CH2 . TRP A 1 34  ? 237.983 128.190 246.091 1.00 30.81 ? 34   TRP L CH2 1 
ATOM   221  N N   . TYR A 1 35  ? 233.573 132.895 249.579 1.00 29.60 ? 35   TYR L N   1 
ATOM   222  C CA  . TYR A 1 35  ? 232.736 133.118 250.750 1.00 29.71 ? 35   TYR L CA  1 
ATOM   223  C C   . TYR A 1 35  ? 232.873 131.978 251.750 1.00 31.00 ? 35   TYR L C   1 
ATOM   224  O O   . TYR A 1 35  ? 232.984 130.813 251.368 1.00 30.84 ? 35   TYR L O   1 
ATOM   225  C CB  . TYR A 1 35  ? 231.275 133.236 250.329 1.00 29.04 ? 35   TYR L CB  1 
ATOM   226  C CG  . TYR A 1 35  ? 231.042 134.263 249.275 1.00 28.77 ? 35   TYR L CG  1 
ATOM   227  C CD1 . TYR A 1 35  ? 230.752 135.558 249.624 1.00 28.60 ? 35   TYR L CD1 1 
ATOM   228  C CD2 . TYR A 1 35  ? 231.123 133.904 247.944 1.00 29.15 ? 35   TYR L CD2 1 
ATOM   229  C CE1 . TYR A 1 35  ? 230.545 136.499 248.645 1.00 28.07 ? 35   TYR L CE1 1 
ATOM   230  C CE2 . TYR A 1 35  ? 230.916 134.845 246.967 1.00 28.64 ? 35   TYR L CE2 1 
ATOM   231  C CZ  . TYR A 1 35  ? 230.629 136.140 247.312 1.00 28.12 ? 35   TYR L CZ  1 
ATOM   232  O OH  . TYR A 1 35  ? 230.418 137.082 246.331 1.00 28.23 ? 35   TYR L OH  1 
ATOM   233  N N   . GLN A 1 36  ? 232.824 132.311 253.032 1.00 30.92 ? 36   GLN L N   1 
ATOM   234  C CA  . GLN A 1 36  ? 232.897 131.312 254.090 1.00 31.48 ? 36   GLN L CA  1 
ATOM   235  C C   . GLN A 1 36  ? 231.583 131.208 254.844 1.00 31.55 ? 36   GLN L C   1 
ATOM   236  O O   . GLN A 1 36  ? 231.129 132.182 255.444 1.00 31.44 ? 36   GLN L O   1 
ATOM   237  C CB  . GLN A 1 36  ? 234.017 131.665 255.062 1.00 32.18 ? 36   GLN L CB  1 
ATOM   238  C CG  . GLN A 1 36  ? 234.174 130.712 256.208 1.00 32.63 ? 36   GLN L CG  1 
ATOM   239  C CD  . GLN A 1 36  ? 235.257 131.152 257.156 1.00 32.85 ? 36   GLN L CD  1 
ATOM   240  O OE1 . GLN A 1 36  ? 235.971 132.122 256.893 1.00 32.60 ? 36   GLN L OE1 1 
ATOM   241  N NE2 . GLN A 1 36  ? 235.387 130.452 258.271 1.00 34.91 ? 36   GLN L NE2 1 
ATOM   242  N N   . GLN A 1 37  ? 230.965 130.033 254.808 1.00 31.77 ? 37   GLN L N   1 
ATOM   243  C CA  . GLN A 1 37  ? 229.680 129.845 255.466 1.00 31.85 ? 37   GLN L CA  1 
ATOM   244  C C   . GLN A 1 37  ? 229.736 128.849 256.612 1.00 32.40 ? 37   GLN L C   1 
ATOM   245  O O   . GLN A 1 37  ? 230.035 127.670 256.418 1.00 32.55 ? 37   GLN L O   1 
ATOM   246  C CB  . GLN A 1 37  ? 228.629 129.378 254.462 1.00 31.57 ? 37   GLN L CB  1 
ATOM   247  C CG  . GLN A 1 37  ? 227.257 129.201 255.068 1.00 31.50 ? 37   GLN L CG  1 
ATOM   248  C CD  . GLN A 1 37  ? 226.204 128.851 254.054 1.00 30.71 ? 37   GLN L CD  1 
ATOM   249  O OE1 . GLN A 1 37  ? 226.451 128.110 253.097 1.00 29.41 ? 37   GLN L OE1 1 
ATOM   250  N NE2 . GLN A 1 37  ? 225.010 129.385 254.260 1.00 30.53 ? 37   GLN L NE2 1 
ATOM   251  N N   . LYS A 1 38  ? 229.393 129.315 257.804 1.00 33.05 ? 38   LYS L N   1 
ATOM   252  C CA  . LYS A 1 38  ? 229.293 128.437 258.956 1.00 33.22 ? 38   LYS L CA  1 
ATOM   253  C C   . LYS A 1 38  ? 227.865 127.904 259.031 1.00 33.16 ? 38   LYS L C   1 
ATOM   254  O O   . LYS A 1 38  ? 226.953 128.541 258.505 1.00 32.91 ? 38   LYS L O   1 
ATOM   255  C CB  . LYS A 1 38  ? 229.672 129.181 260.234 1.00 33.34 ? 38   LYS L CB  1 
ATOM   256  C CG  . LYS A 1 38  ? 231.134 129.583 260.300 1.00 34.02 ? 38   LYS L CG  1 
ATOM   257  C CD  . LYS A 1 38  ? 231.457 130.282 261.606 1.00 35.21 ? 38   LYS L CD  1 
ATOM   258  C CE  . LYS A 1 38  ? 232.930 130.656 261.682 1.00 35.38 ? 38   LYS L CE  1 
ATOM   259  N NZ  . LYS A 1 38  ? 233.251 131.386 262.938 1.00 36.07 ? 38   LYS L NZ  1 
ATOM   260  N N   . PRO A 1 39  ? 227.648 126.730 259.624 1.00 33.17 ? 39   PRO L N   1 
ATOM   261  C CA  . PRO A 1 39  ? 226.348 126.128 259.841 1.00 33.53 ? 39   PRO L CA  1 
ATOM   262  C C   . PRO A 1 39  ? 225.407 127.081 260.563 1.00 33.56 ? 39   PRO L C   1 
ATOM   263  O O   . PRO A 1 39  ? 225.739 127.608 261.624 1.00 33.63 ? 39   PRO L O   1 
ATOM   264  C CB  . PRO A 1 39  ? 226.698 124.919 260.715 1.00 33.12 ? 39   PRO L CB  1 
ATOM   265  C CG  . PRO A 1 39  ? 228.115 124.568 260.321 1.00 33.45 ? 39   PRO L CG  1 
ATOM   266  C CD  . PRO A 1 39  ? 228.783 125.902 260.055 1.00 33.35 ? 39   PRO L CD  1 
ATOM   267  N N   . GLY A 1 40  ? 224.223 127.279 259.992 1.00 33.18 ? 40   GLY L N   1 
ATOM   268  C CA  . GLY A 1 40  ? 223.199 128.118 260.604 1.00 33.01 ? 40   GLY L CA  1 
ATOM   269  C C   . GLY A 1 40  ? 223.427 129.612 260.382 1.00 33.15 ? 40   GLY L C   1 
ATOM   270  O O   . GLY A 1 40  ? 222.704 130.438 260.940 1.00 32.98 ? 40   GLY L O   1 
ATOM   271  N N   . GLN A 1 41  ? 224.431 129.968 259.584 1.00 32.39 ? 41   GLN L N   1 
ATOM   272  C CA  . GLN A 1 41  ? 224.748 131.378 259.378 1.00 32.17 ? 41   GLN L CA  1 
ATOM   273  C C   . GLN A 1 41  ? 224.848 131.756 257.903 1.00 31.29 ? 41   GLN L C   1 
ATOM   274  O O   . GLN A 1 41  ? 225.138 130.917 257.049 1.00 31.49 ? 41   GLN L O   1 
ATOM   275  C CB  . GLN A 1 41  ? 226.051 131.736 260.094 1.00 32.72 ? 41   GLN L CB  1 
ATOM   276  C CG  . GLN A 1 41  ? 226.007 131.521 261.597 1.00 32.87 ? 41   GLN L CG  1 
ATOM   277  C CD  . GLN A 1 41  ? 227.252 132.026 262.300 1.00 33.90 ? 41   GLN L CD  1 
ATOM   278  O OE1 . GLN A 1 41  ? 228.260 132.346 261.663 1.00 33.92 ? 41   GLN L OE1 1 
ATOM   279  N NE2 . GLN A 1 41  ? 227.187 132.104 263.623 1.00 34.28 ? 41   GLN L NE2 1 
ATOM   280  N N   . SER A 1 42  ? 224.624 133.037 257.619 1.00 30.54 ? 42   SER L N   1 
ATOM   281  C CA  . SER A 1 42  ? 224.839 133.590 256.288 1.00 30.36 ? 42   SER L CA  1 
ATOM   282  C C   . SER A 1 42  ? 226.332 133.590 255.977 1.00 30.19 ? 42   SER L C   1 
ATOM   283  O O   . SER A 1 42  ? 227.143 133.722 256.892 1.00 30.93 ? 42   SER L O   1 
ATOM   284  C CB  . SER A 1 42  ? 224.294 135.005 256.224 1.00 30.78 ? 42   SER L CB  1 
ATOM   285  N N   . PRO A 1 43  ? 226.714 133.440 254.706 1.00 30.04 ? 43   PRO L N   1 
ATOM   286  C CA  . PRO A 1 43  ? 228.077 133.448 254.208 1.00 29.89 ? 43   PRO L CA  1 
ATOM   287  C C   . PRO A 1 43  ? 228.731 134.815 254.358 1.00 29.50 ? 43   PRO L C   1 
ATOM   288  O O   . PRO A 1 43  ? 228.079 135.848 254.208 1.00 29.93 ? 43   PRO L O   1 
ATOM   289  C CB  . PRO A 1 43  ? 227.891 133.066 252.735 1.00 29.73 ? 43   PRO L CB  1 
ATOM   290  C CG  . PRO A 1 43  ? 226.473 133.460 252.411 1.00 30.22 ? 43   PRO L CG  1 
ATOM   291  C CD  . PRO A 1 43  ? 225.695 133.241 253.682 1.00 30.42 ? 43   PRO L CD  1 
ATOM   292  N N   . ILE A 1 44  ? 230.032 134.808 254.620 1.00 29.53 ? 44   ILE L N   1 
ATOM   293  C CA  . ILE A 1 44  ? 230.819 136.026 254.756 1.00 28.82 ? 44   ILE L CA  1 
ATOM   294  C C   . ILE A 1 44  ? 231.873 136.127 253.663 1.00 29.48 ? 44   ILE L C   1 
ATOM   295  O O   . ILE A 1 44  ? 232.593 135.166 253.397 1.00 29.71 ? 44   ILE L O   1 
ATOM   296  C CB  . ILE A 1 44  ? 231.502 136.071 256.137 1.00 28.95 ? 44   ILE L CB  1 
ATOM   297  C CG1 . ILE A 1 44  ? 230.430 136.100 257.240 1.00 29.06 ? 44   ILE L CG1 1 
ATOM   298  C CG2 . ILE A 1 44  ? 232.435 137.276 256.236 1.00 28.87 ? 44   ILE L CG2 1 
ATOM   299  C CD1 . ILE A 1 44  ? 230.970 135.860 258.635 1.00 27.67 ? 44   ILE L CD1 1 
ATOM   300  N N   . LEU A 1 45  ? 231.965 137.287 253.021 1.00 28.86 ? 45   LEU L N   1 
ATOM   301  C CA  . LEU A 1 45  ? 232.967 137.482 251.980 1.00 29.03 ? 45   LEU L CA  1 
ATOM   302  C C   . LEU A 1 45  ? 234.363 137.446 252.578 1.00 30.01 ? 45   LEU L C   1 
ATOM   303  O O   . LEU A 1 45  ? 234.665 138.192 253.508 1.00 30.75 ? 45   LEU L O   1 
ATOM   304  C CB  . LEU A 1 45  ? 232.742 138.826 251.271 1.00 28.31 ? 45   LEU L CB  1 
ATOM   305  C CG  . LEU A 1 45  ? 233.735 139.186 250.137 1.00 28.94 ? 45   LEU L CG  1 
ATOM   306  C CD1 . LEU A 1 45  ? 233.565 138.225 248.968 1.00 29.04 ? 45   LEU L CD1 1 
ATOM   307  C CD2 . LEU A 1 45  ? 233.477 140.620 249.692 1.00 28.68 ? 45   LEU L CD2 1 
ATOM   308  N N   . VAL A 1 46  ? 235.218 136.590 252.029 1.00 30.22 ? 46   VAL L N   1 
ATOM   309  C CA  . VAL A 1 46  ? 236.577 136.447 252.531 1.00 30.41 ? 46   VAL L CA  1 
ATOM   310  C C   . VAL A 1 46  ? 237.576 137.034 251.543 1.00 30.60 ? 46   VAL L C   1 
ATOM   311  O O   . VAL A 1 46  ? 238.502 137.743 251.930 1.00 31.52 ? 46   VAL L O   1 
ATOM   312  C CB  . VAL A 1 46  ? 236.900 134.965 252.785 1.00 30.46 ? 46   VAL L CB  1 
ATOM   313  C CG1 . VAL A 1 46  ? 238.307 134.807 253.317 1.00 32.80 ? 46   VAL L CG1 1 
ATOM   314  C CG2 . VAL A 1 46  ? 235.916 134.394 253.770 1.00 31.30 ? 46   VAL L CG2 1 
ATOM   315  N N   . ILE A 1 47  ? 237.405 136.699 250.267 1.00 29.92 ? 47   ILE L N   1 
ATOM   316  C CA  . ILE A 1 47  ? 238.278 137.212 249.214 1.00 29.67 ? 47   ILE L CA  1 
ATOM   317  C C   . ILE A 1 47  ? 237.469 137.725 248.031 1.00 29.69 ? 47   ILE L C   1 
ATOM   318  O O   . ILE A 1 47  ? 236.566 137.045 247.545 1.00 29.40 ? 47   ILE L O   1 
ATOM   319  C CB  . ILE A 1 47  ? 239.271 136.139 248.721 1.00 29.56 ? 47   ILE L CB  1 
ATOM   320  C CG1 . ILE A 1 47  ? 240.133 135.656 249.885 1.00 30.75 ? 47   ILE L CG1 1 
ATOM   321  C CG2 . ILE A 1 47  ? 240.139 136.699 247.599 1.00 30.22 ? 47   ILE L CG2 1 
ATOM   322  C CD1 . ILE A 1 47  ? 241.043 134.494 249.556 1.00 33.03 ? 47   ILE L CD1 1 
ATOM   323  N N   . TYR A 1 48  ? 237.821 138.901 247.532 1.00 29.66 ? 48   TYR L N   1 
ATOM   324  C CA  . TYR A 1 48  ? 237.189 139.423 246.329 1.00 29.50 ? 48   TYR L CA  1 
ATOM   325  C C   . TYR A 1 48  ? 238.240 139.868 245.330 1.00 28.82 ? 48   TYR L C   1 
ATOM   326  O O   . TYR A 1 48  ? 239.384 140.139 245.694 1.00 30.57 ? 48   TYR L O   1 
ATOM   327  C CB  . TYR A 1 48  ? 236.230 140.564 246.662 1.00 29.58 ? 48   TYR L CB  1 
ATOM   328  C CG  . TYR A 1 48  ? 236.887 141.804 247.211 1.00 29.73 ? 48   TYR L CG  1 
ATOM   329  C CD1 . TYR A 1 48  ? 237.235 142.834 246.363 1.00 29.54 ? 48   TYR L CD1 1 
ATOM   330  C CD2 . TYR A 1 48  ? 237.133 141.913 248.563 1.00 30.06 ? 48   TYR L CD2 1 
ATOM   331  C CE1 . TYR A 1 48  ? 237.827 143.972 246.861 1.00 29.30 ? 48   TYR L CE1 1 
ATOM   332  C CE2 . TYR A 1 48  ? 237.726 143.051 249.065 1.00 30.50 ? 48   TYR L CE2 1 
ATOM   333  C CZ  . TYR A 1 48  ? 238.072 144.078 248.218 1.00 29.68 ? 48   TYR L CZ  1 
ATOM   334  O OH  . TYR A 1 48  ? 238.660 145.218 248.717 1.00 28.64 ? 48   TYR L OH  1 
ATOM   335  N N   . GLN A 1 49  ? 237.865 139.909 244.058 1.00 29.13 ? 49   GLN L N   1 
ATOM   336  C CA  . GLN A 1 49  ? 238.803 140.295 243.014 1.00 29.00 ? 49   GLN L CA  1 
ATOM   337  C C   . GLN A 1 49  ? 240.100 139.502 243.110 1.00 29.22 ? 49   GLN L C   1 
ATOM   338  O O   . GLN A 1 49  ? 241.191 140.071 243.112 1.00 29.25 ? 49   GLN L O   1 
ATOM   339  C CB  . GLN A 1 49  ? 239.078 141.797 243.049 1.00 28.87 ? 49   GLN L CB  1 
ATOM   340  C CG  . GLN A 1 49  ? 237.885 142.647 242.642 1.00 28.58 ? 49   GLN L CG  1 
ATOM   341  C CD  . GLN A 1 49  ? 238.149 144.127 242.797 1.00 27.88 ? 49   GLN L CD  1 
ATOM   342  O OE1 . GLN A 1 49  ? 239.304 144.573 242.761 1.00 28.37 ? 49   GLN L OE1 1 
ATOM   343  N NE2 . GLN A 1 49  ? 237.084 144.898 242.969 1.00 27.96 ? 49   GLN L NE2 1 
ATOM   344  N N   . ASP A 1 50  ? 239.962 138.181 243.184 1.00 29.34 ? 50   ASP L N   1 
ATOM   345  C CA  . ASP A 1 50  ? 241.070 137.229 243.201 1.00 29.43 ? 50   ASP L CA  1 
ATOM   346  C C   . ASP A 1 50  ? 241.849 137.181 244.514 1.00 29.66 ? 50   ASP L C   1 
ATOM   347  O O   . ASP A 1 50  ? 241.984 136.112 245.107 1.00 30.40 ? 50   ASP L O   1 
ATOM   348  C CB  . ASP A 1 50  ? 242.043 137.491 242.047 1.00 29.44 ? 50   ASP L CB  1 
ATOM   349  C CG  . ASP A 1 50  ? 241.438 137.198 240.680 1.00 30.59 ? 50   ASP L CG  1 
ATOM   350  O OD1 . ASP A 1 50  ? 240.398 136.575 240.616 1.00 30.61 ? 50   ASP L OD1 1 
ATOM   351  O OD2 . ASP A 1 50  ? 242.029 137.592 239.704 1.00 30.99 ? 50   ASP L OD2 1 
ATOM   352  N N   . ASN A 1 51  ? 242.412 138.306 244.946 1.00 29.05 ? 51   ASN L N   1 
ATOM   353  C CA  . ASN A 1 51  ? 243.285 138.269 246.116 1.00 29.04 ? 51   ASN L CA  1 
ATOM   354  C C   . ASN A 1 51  ? 243.140 139.435 247.096 1.00 28.95 ? 51   ASN L C   1 
ATOM   355  O O   . ASN A 1 51  ? 244.088 139.747 247.817 1.00 29.92 ? 51   ASN L O   1 
ATOM   356  C CB  . ASN A 1 51  ? 244.728 138.152 245.669 1.00 28.44 ? 51   ASN L CB  1 
ATOM   357  C CG  . ASN A 1 51  ? 245.170 139.330 244.857 1.00 28.87 ? 51   ASN L CG  1 
ATOM   358  O OD1 . ASN A 1 51  ? 244.351 140.160 244.448 1.00 28.98 ? 51   ASN L OD1 1 
ATOM   359  N ND2 . ASN A 1 51  ? 246.452 139.421 244.610 1.00 27.98 ? 51   ASN L ND2 1 
ATOM   360  N N   . LYS A 1 52  ? 241.974 140.071 247.155 1.00 29.02 ? 52   LYS L N   1 
ATOM   361  C CA  . LYS A 1 52  ? 241.798 141.175 248.098 1.00 29.36 ? 52   LYS L CA  1 
ATOM   362  C C   . LYS A 1 52  ? 240.920 140.781 249.277 1.00 29.63 ? 52   LYS L C   1 
ATOM   363  O O   . LYS A 1 52  ? 239.849 140.203 249.102 1.00 31.97 ? 52   LYS L O   1 
ATOM   364  C CB  . LYS A 1 52  ? 241.196 142.388 247.395 1.00 29.37 ? 52   LYS L CB  1 
ATOM   365  C CG  . LYS A 1 52  ? 242.075 142.985 246.317 1.00 29.13 ? 52   LYS L CG  1 
ATOM   366  C CD  . LYS A 1 52  ? 241.421 144.200 245.690 1.00 28.15 ? 52   LYS L CD  1 
ATOM   367  C CE  . LYS A 1 52  ? 242.268 144.765 244.565 1.00 27.34 ? 52   LYS L CE  1 
ATOM   368  N NZ  . LYS A 1 52  ? 241.588 145.891 243.882 1.00 27.32 ? 52   LYS L NZ  1 
ATOM   369  N N   . ARG A 1 53  ? 241.356 141.131 250.482 1.00 31.04 ? 53   ARG L N   1 
ATOM   370  C CA  . ARG A 1 53  ? 240.556 140.870 251.675 1.00 31.84 ? 53   ARG L CA  1 
ATOM   371  C C   . ARG A 1 53  ? 239.720 142.093 252.056 1.00 31.93 ? 53   ARG L C   1 
ATOM   372  O O   . ARG A 1 53  ? 240.197 143.222 251.949 1.00 32.68 ? 53   ARG L O   1 
ATOM   373  C CB  . ARG A 1 53  ? 241.435 140.516 252.863 1.00 33.15 ? 53   ARG L CB  1 
ATOM   374  C CG  . ARG A 1 53  ? 242.113 139.164 252.807 1.00 33.90 ? 53   ARG L CG  1 
ATOM   375  C CD  . ARG A 1 53  ? 242.779 138.854 254.104 1.00 35.03 ? 53   ARG L CD  1 
ATOM   376  N NE  . ARG A 1 53  ? 243.867 139.775 254.386 1.00 35.16 ? 53   ARG L NE  1 
ATOM   377  C CZ  . ARG A 1 53  ? 245.142 139.620 253.972 1.00 35.88 ? 53   ARG L CZ  1 
ATOM   378  N NH1 . ARG A 1 53  ? 245.492 138.567 253.263 1.00 34.87 ? 53   ARG L NH1 1 
ATOM   379  N NH2 . ARG A 1 53  ? 246.045 140.535 254.281 1.00 35.53 ? 53   ARG L NH2 1 
ATOM   380  N N   . PRO A 1 54  ? 238.474 141.888 252.482 1.00 31.90 ? 54   PRO L N   1 
ATOM   381  C CA  . PRO A 1 54  ? 237.640 142.823 253.210 1.00 32.14 ? 54   PRO L CA  1 
ATOM   382  C C   . PRO A 1 54  ? 238.224 143.089 254.584 1.00 34.13 ? 54   PRO L C   1 
ATOM   383  O O   . PRO A 1 54  ? 238.861 142.214 255.172 1.00 34.21 ? 54   PRO L O   1 
ATOM   384  C CB  . PRO A 1 54  ? 236.305 142.078 253.321 1.00 32.55 ? 54   PRO L CB  1 
ATOM   385  C CG  . PRO A 1 54  ? 236.347 141.036 252.235 1.00 31.77 ? 54   PRO L CG  1 
ATOM   386  C CD  . PRO A 1 54  ? 237.802 140.661 252.102 1.00 31.65 ? 54   PRO L CD  1 
ATOM   387  N N   . SER A 1 55  ? 237.966 144.271 255.122 1.00 34.83 ? 55   SER L N   1 
ATOM   388  C CA  . SER A 1 55  ? 238.400 144.572 256.474 1.00 35.23 ? 55   SER L CA  1 
ATOM   389  C C   . SER A 1 55  ? 237.753 143.598 257.448 1.00 35.28 ? 55   SER L C   1 
ATOM   390  O O   . SER A 1 55  ? 236.570 143.282 257.327 1.00 35.23 ? 55   SER L O   1 
ATOM   391  C CB  . SER A 1 55  ? 238.024 145.996 256.840 1.00 34.98 ? 55   SER L CB  1 
ATOM   392  N N   . GLY A 1 56  ? 238.528 143.128 258.419 1.00 35.03 ? 56   GLY L N   1 
ATOM   393  C CA  . GLY A 1 56  ? 238.014 142.204 259.424 1.00 35.28 ? 56   GLY L CA  1 
ATOM   394  C C   . GLY A 1 56  ? 238.390 140.753 259.129 1.00 35.47 ? 56   GLY L C   1 
ATOM   395  O O   . GLY A 1 56  ? 238.264 139.890 259.997 1.00 35.53 ? 56   GLY L O   1 
ATOM   396  N N   . ILE A 1 57  ? 238.864 140.486 257.915 1.00 35.18 ? 57   ILE L N   1 
ATOM   397  C CA  . ILE A 1 57  ? 239.277 139.136 257.543 1.00 35.30 ? 57   ILE L CA  1 
ATOM   398  C C   . ILE A 1 57  ? 240.746 138.895 257.909 1.00 35.70 ? 57   ILE L C   1 
ATOM   399  O O   . ILE A 1 57  ? 241.617 139.650 257.480 1.00 35.78 ? 57   ILE L O   1 
ATOM   400  C CB  . ILE A 1 57  ? 239.069 138.892 256.038 1.00 34.50 ? 57   ILE L CB  1 
ATOM   401  C CG1 . ILE A 1 57  ? 237.582 139.096 255.659 1.00 33.90 ? 57   ILE L CG1 1 
ATOM   402  C CG2 . ILE A 1 57  ? 239.550 137.499 255.644 1.00 34.67 ? 57   ILE L CG2 1 
ATOM   403  C CD1 . ILE A 1 57  ? 236.597 138.192 256.387 1.00 32.97 ? 57   ILE L CD1 1 
ATOM   404  N N   . PRO A 1 58  ? 241.041 137.850 258.696 1.00 35.95 ? 58   PRO L N   1 
ATOM   405  C CA  . PRO A 1 58  ? 242.363 137.451 259.146 1.00 36.15 ? 58   PRO L CA  1 
ATOM   406  C C   . PRO A 1 58  ? 243.336 137.261 257.993 1.00 36.25 ? 58   PRO L C   1 
ATOM   407  O O   . PRO A 1 58  ? 242.964 136.783 256.921 1.00 36.12 ? 58   PRO L O   1 
ATOM   408  C CB  . PRO A 1 58  ? 242.081 136.114 259.846 1.00 36.93 ? 58   PRO L CB  1 
ATOM   409  C CG  . PRO A 1 58  ? 240.656 136.226 260.321 1.00 37.08 ? 58   PRO L CG  1 
ATOM   410  C CD  . PRO A 1 58  ? 239.948 137.035 259.258 1.00 36.02 ? 58   PRO L CD  1 
ATOM   411  N N   . GLU A 1 59  ? 244.597 137.599 258.246 1.00 36.58 ? 59   GLU L N   1 
ATOM   412  C CA  . GLU A 1 59  ? 245.671 137.511 257.261 1.00 36.74 ? 59   GLU L CA  1 
ATOM   413  C C   . GLU A 1 59  ? 245.961 136.071 256.856 1.00 36.95 ? 59   GLU L C   1 
ATOM   414  O O   . GLU A 1 59  ? 246.732 135.820 255.931 1.00 37.05 ? 59   GLU L O   1 
ATOM   415  C CB  . GLU A 1 59  ? 246.947 138.166 257.803 1.00 36.08 ? 59   GLU L CB  1 
ATOM   416  N N   . ARG A 1 60  ? 245.340 135.128 257.555 1.00 37.19 ? 60   ARG L N   1 
ATOM   417  C CA  . ARG A 1 60  ? 245.483 133.714 257.246 1.00 37.02 ? 60   ARG L CA  1 
ATOM   418  C C   . ARG A 1 60  ? 244.934 133.418 255.858 1.00 36.60 ? 60   ARG L C   1 
ATOM   419  O O   . ARG A 1 60  ? 245.352 132.460 255.207 1.00 36.22 ? 60   ARG L O   1 
ATOM   420  C CB  . ARG A 1 60  ? 244.742 132.852 258.265 1.00 37.25 ? 60   ARG L CB  1 
ATOM   421  C CG  . ARG A 1 60  ? 245.318 132.883 259.669 1.00 37.73 ? 60   ARG L CG  1 
ATOM   422  C CD  . ARG A 1 60  ? 244.801 131.767 260.537 1.00 38.33 ? 60   ARG L CD  1 
ATOM   423  N NE  . ARG A 1 60  ? 243.345 131.798 260.715 1.00 38.12 ? 60   ARG L NE  1 
ATOM   424  C CZ  . ARG A 1 60  ? 242.687 132.596 261.584 1.00 38.07 ? 60   ARG L CZ  1 
ATOM   425  N NH1 . ARG A 1 60  ? 243.350 133.458 262.328 1.00 37.12 ? 60   ARG L NH1 1 
ATOM   426  N NH2 . ARG A 1 60  ? 241.370 132.509 261.689 1.00 37.23 ? 60   ARG L NH2 1 
ATOM   427  N N   . PHE A 1 61  ? 243.963 134.221 255.426 1.00 35.97 ? 61   PHE L N   1 
ATOM   428  C CA  . PHE A 1 61  ? 243.274 133.985 254.166 1.00 35.31 ? 61   PHE L CA  1 
ATOM   429  C C   . PHE A 1 61  ? 243.928 134.710 252.997 1.00 34.89 ? 61   PHE L C   1 
ATOM   430  O O   . PHE A 1 61  ? 244.053 135.936 252.997 1.00 36.30 ? 61   PHE L O   1 
ATOM   431  C CB  . PHE A 1 61  ? 241.818 134.432 254.278 1.00 34.46 ? 61   PHE L CB  1 
ATOM   432  C CG  . PHE A 1 61  ? 241.024 133.629 255.256 1.00 34.46 ? 61   PHE L CG  1 
ATOM   433  C CD1 . PHE A 1 61  ? 240.871 134.066 256.561 1.00 35.70 ? 61   PHE L CD1 1 
ATOM   434  C CD2 . PHE A 1 61  ? 240.433 132.438 254.881 1.00 34.18 ? 61   PHE L CD2 1 
ATOM   435  C CE1 . PHE A 1 61  ? 240.144 133.327 257.470 1.00 35.80 ? 61   PHE L CE1 1 
ATOM   436  C CE2 . PHE A 1 61  ? 239.704 131.699 255.788 1.00 35.09 ? 61   PHE L CE2 1 
ATOM   437  C CZ  . PHE A 1 61  ? 239.561 132.144 257.083 1.00 35.65 ? 61   PHE L CZ  1 
ATOM   438  N N   . SER A 1 62  ? 244.298 133.944 251.980 1.00 33.99 ? 62   SER L N   1 
ATOM   439  C CA  . SER A 1 62  ? 244.890 134.482 250.763 1.00 32.96 ? 62   SER L CA  1 
ATOM   440  C C   . SER A 1 62  ? 244.409 133.668 249.576 1.00 32.68 ? 62   SER L C   1 
ATOM   441  O O   . SER A 1 62  ? 243.685 132.688 249.751 1.00 33.21 ? 62   SER L O   1 
ATOM   442  C CB  . SER A 1 62  ? 246.402 134.447 250.846 1.00 32.91 ? 62   SER L CB  1 
ATOM   443  O OG  . SER A 1 62  ? 246.875 133.131 250.812 1.00 33.70 ? 62   SER L OG  1 
ATOM   444  N N   . GLY A 1 63  ? 244.780 134.073 248.369 1.00 32.52 ? 63   GLY L N   1 
ATOM   445  C CA  . GLY A 1 63  ? 244.339 133.346 247.187 1.00 32.51 ? 63   GLY L CA  1 
ATOM   446  C C   . GLY A 1 63  ? 244.955 133.893 245.911 1.00 31.71 ? 63   GLY L C   1 
ATOM   447  O O   . GLY A 1 63  ? 245.722 134.858 245.937 1.00 32.10 ? 63   GLY L O   1 
ATOM   448  N N   . SER A 1 64  ? 244.628 133.250 244.799 1.00 30.58 ? 64   SER L N   1 
ATOM   449  C CA  . SER A 1 64  ? 245.160 133.631 243.498 1.00 30.17 ? 64   SER L CA  1 
ATOM   450  C C   . SER A 1 64  ? 244.269 133.118 242.378 1.00 31.07 ? 64   SER L C   1 
ATOM   451  O O   . SER A 1 64  ? 243.336 132.349 242.615 1.00 31.39 ? 64   SER L O   1 
ATOM   452  C CB  . SER A 1 64  ? 246.568 133.100 243.324 1.00 31.35 ? 64   SER L CB  1 
ATOM   453  N N   . ASN A 1 65  ? 244.551 133.561 241.156 1.00 31.07 ? 65   ASN L N   1 
ATOM   454  C CA  . ASN A 1 65  ? 243.770 133.154 239.995 1.00 31.63 ? 65   ASN L CA  1 
ATOM   455  C C   . ASN A 1 65  ? 244.602 133.175 238.716 1.00 31.93 ? 65   ASN L C   1 
ATOM   456  O O   . ASN A 1 65  ? 244.992 134.242 238.238 1.00 32.67 ? 65   ASN L O   1 
ATOM   457  C CB  . ASN A 1 65  ? 242.547 134.038 239.857 1.00 31.54 ? 65   ASN L CB  1 
ATOM   458  C CG  . ASN A 1 65  ? 241.629 133.609 238.760 1.00 32.02 ? 65   ASN L CG  1 
ATOM   459  O OD1 . ASN A 1 65  ? 241.891 132.621 238.062 1.00 32.10 ? 65   ASN L OD1 1 
ATOM   460  N ND2 . ASN A 1 65  ? 240.558 134.342 238.583 1.00 31.93 ? 65   ASN L ND2 1 
ATOM   461  N N   . SER A 1 66  ? 244.894 131.994 238.179 1.00 32.13 ? 66   SER L N   1 
ATOM   462  C CA  . SER A 1 66  ? 245.691 131.878 236.960 1.00 32.70 ? 66   SER L CA  1 
ATOM   463  C C   . SER A 1 66  ? 245.343 130.606 236.196 1.00 32.74 ? 66   SER L C   1 
ATOM   464  O O   . SER A 1 66  ? 244.904 129.619 236.782 1.00 32.88 ? 66   SER L O   1 
ATOM   465  C CB  . SER A 1 66  ? 247.170 131.888 237.294 1.00 33.20 ? 66   SER L CB  1 
ATOM   466  N N   . GLU A 1 67  ? 245.547 130.626 234.882 1.00 32.75 ? 67   GLU L N   1 
ATOM   467  C CA  . GLU A 1 67  ? 245.309 129.451 234.043 1.00 33.05 ? 67   GLU L CA  1 
ATOM   468  C C   . GLU A 1 67  ? 243.915 128.866 234.270 1.00 32.62 ? 67   GLU L C   1 
ATOM   469  O O   . GLU A 1 67  ? 243.739 127.649 234.314 1.00 32.96 ? 67   GLU L O   1 
ATOM   470  C CB  . GLU A 1 67  ? 246.374 128.380 234.301 1.00 33.81 ? 67   GLU L CB  1 
ATOM   471  N N   . ASN A 1 68  ? 242.931 129.749 234.407 1.00 32.69 ? 68   ASN L N   1 
ATOM   472  C CA  . ASN A 1 68  ? 241.531 129.378 234.594 1.00 33.15 ? 68   ASN L CA  1 
ATOM   473  C C   . ASN A 1 68  ? 241.260 128.599 235.883 1.00 32.70 ? 68   ASN L C   1 
ATOM   474  O O   . ASN A 1 68  ? 240.191 128.004 236.034 1.00 32.62 ? 68   ASN L O   1 
ATOM   475  C CB  . ASN A 1 68  ? 241.017 128.609 233.392 1.00 32.87 ? 68   ASN L CB  1 
ATOM   476  C CG  . ASN A 1 68  ? 240.991 129.446 232.148 1.00 33.73 ? 68   ASN L CG  1 
ATOM   477  O OD1 . ASN A 1 68  ? 240.611 130.628 232.177 1.00 34.00 ? 68   ASN L OD1 1 
ATOM   478  N ND2 . ASN A 1 68  ? 241.392 128.860 231.049 1.00 33.73 ? 68   ASN L ND2 1 
ATOM   479  N N   . THR A 1 69  ? 242.190 128.655 236.833 1.00 32.48 ? 69   THR L N   1 
ATOM   480  C CA  . THR A 1 69  ? 241.986 128.041 238.141 1.00 32.29 ? 69   THR L CA  1 
ATOM   481  C C   . THR A 1 69  ? 242.200 129.046 239.265 1.00 32.06 ? 69   THR L C   1 
ATOM   482  O O   . THR A 1 69  ? 243.224 129.727 239.324 1.00 32.03 ? 69   THR L O   1 
ATOM   483  C CB  . THR A 1 69  ? 242.927 126.839 238.351 1.00 32.41 ? 69   THR L CB  1 
ATOM   484  O OG1 . THR A 1 69  ? 242.685 125.858 237.335 1.00 32.67 ? 69   THR L OG1 1 
ATOM   485  C CG2 . THR A 1 69  ? 242.684 126.209 239.726 1.00 32.15 ? 69   THR L CG2 1 
ATOM   486  N N   . ALA A 1 70  ? 241.238 129.119 240.173 1.00 31.57 ? 70   ALA L N   1 
ATOM   487  C CA  . ALA A 1 70  ? 241.340 130.001 241.323 1.00 31.46 ? 70   ALA L CA  1 
ATOM   488  C C   . ALA A 1 70  ? 241.496 129.174 242.585 1.00 31.08 ? 70   ALA L C   1 
ATOM   489  O O   . ALA A 1 70  ? 240.975 128.061 242.675 1.00 30.91 ? 70   ALA L O   1 
ATOM   490  C CB  . ALA A 1 70  ? 240.120 130.901 241.412 1.00 31.80 ? 70   ALA L CB  1 
ATOM   491  N N   . THR A 1 71  ? 242.225 129.702 243.559 1.00 30.72 ? 71   THR L N   1 
ATOM   492  C CA  . THR A 1 71  ? 242.401 128.981 244.811 1.00 31.06 ? 71   THR L CA  1 
ATOM   493  C C   . THR A 1 71  ? 242.237 129.875 246.030 1.00 31.70 ? 71   THR L C   1 
ATOM   494  O O   . THR A 1 71  ? 242.562 131.064 246.000 1.00 31.82 ? 71   THR L O   1 
ATOM   495  C CB  . THR A 1 71  ? 243.789 128.311 244.875 1.00 30.99 ? 71   THR L CB  1 
ATOM   496  O OG1 . THR A 1 71  ? 244.805 129.320 244.925 1.00 31.99 ? 71   THR L OG1 1 
ATOM   497  C CG2 . THR A 1 71  ? 244.016 127.443 243.650 1.00 32.57 ? 71   THR L CG2 1 
ATOM   498  N N   . LEU A 1 72  ? 241.814 129.261 247.130 1.00 32.07 ? 72   LEU L N   1 
ATOM   499  C CA  . LEU A 1 72  ? 241.818 129.890 248.443 1.00 32.09 ? 72   LEU L CA  1 
ATOM   500  C C   . LEU A 1 72  ? 242.753 129.124 249.359 1.00 32.67 ? 72   LEU L C   1 
ATOM   501  O O   . LEU A 1 72  ? 242.680 127.898 249.459 1.00 32.85 ? 72   LEU L O   1 
ATOM   502  C CB  . LEU A 1 72  ? 240.400 129.932 249.031 1.00 31.22 ? 72   LEU L CB  1 
ATOM   503  C CG  . LEU A 1 72  ? 240.251 130.544 250.448 1.00 31.64 ? 72   LEU L CG  1 
ATOM   504  C CD1 . LEU A 1 72  ? 238.938 131.301 250.537 1.00 31.31 ? 72   LEU L CD1 1 
ATOM   505  C CD2 . LEU A 1 72  ? 240.266 129.430 251.488 1.00 33.39 ? 72   LEU L CD2 1 
ATOM   506  N N   . THR A 1 73  ? 243.641 129.846 250.022 1.00 33.33 ? 73   THR L N   1 
ATOM   507  C CA  . THR A 1 73  ? 244.622 129.228 250.897 1.00 33.38 ? 73   THR L CA  1 
ATOM   508  C C   . THR A 1 73  ? 244.498 129.755 252.315 1.00 34.33 ? 73   THR L C   1 
ATOM   509  O O   . THR A 1 73  ? 244.380 130.961 252.535 1.00 34.49 ? 73   THR L O   1 
ATOM   510  C CB  . THR A 1 73  ? 246.051 129.473 250.379 1.00 33.26 ? 73   THR L CB  1 
ATOM   511  O OG1 . THR A 1 73  ? 246.185 128.913 249.069 1.00 34.04 ? 73   THR L OG1 1 
ATOM   512  C CG2 . THR A 1 73  ? 247.066 128.826 251.300 1.00 35.41 ? 73   THR L CG2 1 
ATOM   513  N N   . ILE A 1 74  ? 244.521 128.848 253.283 1.00 35.28 ? 74   ILE L N   1 
ATOM   514  C CA  . ILE A 1 74  ? 244.488 129.247 254.681 1.00 36.11 ? 74   ILE L CA  1 
ATOM   515  C C   . ILE A 1 74  ? 245.769 128.827 255.378 1.00 36.87 ? 74   ILE L C   1 
ATOM   516  O O   . ILE A 1 74  ? 246.012 127.637 255.577 1.00 37.06 ? 74   ILE L O   1 
ATOM   517  C CB  . ILE A 1 74  ? 243.287 128.631 255.413 1.00 35.95 ? 74   ILE L CB  1 
ATOM   518  C CG1 . ILE A 1 74  ? 241.998 129.019 254.699 1.00 35.50 ? 74   ILE L CG1 1 
ATOM   519  C CG2 . ILE A 1 74  ? 243.269 129.120 256.863 1.00 37.13 ? 74   ILE L CG2 1 
ATOM   520  C CD1 . ILE A 1 74  ? 240.782 128.260 255.164 1.00 35.74 ? 74   ILE L CD1 1 
ATOM   521  N N   . SER A 1 75  ? 246.595 129.803 255.733 1.00 37.25 ? 75   SER L N   1 
ATOM   522  C CA  . SER A 1 75  ? 247.876 129.521 256.368 1.00 37.64 ? 75   SER L CA  1 
ATOM   523  C C   . SER A 1 75  ? 247.727 129.461 257.880 1.00 38.15 ? 75   SER L C   1 
ATOM   524  O O   . SER A 1 75  ? 247.169 130.372 258.491 1.00 38.43 ? 75   SER L O   1 
ATOM   525  C CB  . SER A 1 75  ? 248.893 130.577 255.990 1.00 37.79 ? 75   SER L CB  1 
ATOM   526  N N   . GLY A 1 76  ? 248.203 128.378 258.487 1.00 38.74 ? 76   GLY L N   1 
ATOM   527  C CA  . GLY A 1 76  ? 248.064 128.221 259.928 1.00 38.97 ? 76   GLY L CA  1 
ATOM   528  C C   . GLY A 1 76  ? 246.607 127.977 260.286 1.00 38.98 ? 76   GLY L C   1 
ATOM   529  O O   . GLY A 1 76  ? 246.064 128.618 261.187 1.00 38.54 ? 76   GLY L O   1 
ATOM   530  N N   . THR A 1 77  ? 245.964 127.081 259.544 1.00 38.89 ? 77   THR L N   1 
ATOM   531  C CA  . THR A 1 77  ? 244.537 126.833 259.695 1.00 38.96 ? 77   THR L CA  1 
ATOM   532  C C   . THR A 1 77  ? 244.173 126.552 261.143 1.00 39.23 ? 77   THR L C   1 
ATOM   533  O O   . THR A 1 77  ? 244.789 125.716 261.808 1.00 39.35 ? 77   THR L O   1 
ATOM   534  C CB  . THR A 1 77  ? 244.085 125.648 258.817 1.00 38.82 ? 77   THR L CB  1 
ATOM   535  N N   . GLN A 1 78  ? 243.160 127.258 261.625 1.00 38.97 ? 78   GLN L N   1 
ATOM   536  C CA  . GLN A 1 78  ? 242.687 127.104 262.992 1.00 39.09 ? 78   GLN L CA  1 
ATOM   537  C C   . GLN A 1 78  ? 241.446 126.235 263.031 1.00 39.40 ? 78   GLN L C   1 
ATOM   538  O O   . GLN A 1 78  ? 240.774 126.054 262.018 1.00 39.28 ? 78   GLN L O   1 
ATOM   539  C CB  . GLN A 1 78  ? 242.396 128.472 263.611 1.00 38.90 ? 78   GLN L CB  1 
ATOM   540  N N   . THR A 1 79  ? 241.119 125.713 264.203 1.00 39.30 ? 79   THR L N   1 
ATOM   541  C CA  . THR A 1 79  ? 239.931 124.883 264.344 1.00 38.91 ? 79   THR L CA  1 
ATOM   542  C C   . THR A 1 79  ? 238.668 125.723 264.218 1.00 38.56 ? 79   THR L C   1 
ATOM   543  O O   . THR A 1 79  ? 237.568 125.196 264.066 1.00 38.58 ? 79   THR L O   1 
ATOM   544  C CB  . THR A 1 79  ? 239.939 124.131 265.685 1.00 40.67 ? 79   THR L CB  1 
ATOM   545  N N   . MET A 1 80  ? 238.837 127.039 264.262 1.00 38.59 ? 80   MET L N   1 
ATOM   546  C CA  . MET A 1 80  ? 237.724 127.967 264.125 1.00 38.75 ? 80   MET L CA  1 
ATOM   547  C C   . MET A 1 80  ? 237.469 128.314 262.662 1.00 38.25 ? 80   MET L C   1 
ATOM   548  O O   . MET A 1 80  ? 236.554 129.076 262.349 1.00 37.77 ? 80   MET L O   1 
ATOM   549  C CB  . MET A 1 80  ? 237.996 129.235 264.931 1.00 39.54 ? 80   MET L CB  1 
ATOM   550  N N   . ASP A 1 81  ? 238.278 127.751 261.766 1.00 38.23 ? 81   ASP L N   1 
ATOM   551  C CA  . ASP A 1 81  ? 238.139 128.009 260.338 1.00 37.89 ? 81   ASP L CA  1 
ATOM   552  C C   . ASP A 1 81  ? 237.291 126.937 259.660 1.00 37.25 ? 81   ASP L C   1 
ATOM   553  O O   . ASP A 1 81  ? 237.127 126.942 258.439 1.00 36.06 ? 81   ASP L O   1 
ATOM   554  C CB  . ASP A 1 81  ? 239.515 128.086 259.663 1.00 38.18 ? 81   ASP L CB  1 
ATOM   555  C CG  . ASP A 1 81  ? 240.335 129.324 260.069 1.00 38.38 ? 81   ASP L CG  1 
ATOM   556  O OD1 . ASP A 1 81  ? 239.752 130.355 260.320 1.00 38.28 ? 81   ASP L OD1 1 
ATOM   557  O OD2 . ASP A 1 81  ? 241.543 129.218 260.131 1.00 39.06 ? 81   ASP L OD2 1 
ATOM   558  N N   . GLU A 1 82  ? 236.737 126.022 260.454 1.00 37.07 ? 82   GLU L N   1 
ATOM   559  C CA  . GLU A 1 82  ? 235.867 124.990 259.904 1.00 36.27 ? 82   GLU L CA  1 
ATOM   560  C C   . GLU A 1 82  ? 234.614 125.627 259.323 1.00 35.67 ? 82   GLU L C   1 
ATOM   561  O O   . GLU A 1 82  ? 233.901 126.357 260.011 1.00 36.26 ? 82   GLU L O   1 
ATOM   562  C CB  . GLU A 1 82  ? 235.484 123.970 260.981 1.00 36.48 ? 82   GLU L CB  1 
ATOM   563  C CG  . GLU A 1 82  ? 234.575 122.847 260.482 1.00 36.57 ? 82   GLU L CG  1 
ATOM   564  C CD  . GLU A 1 82  ? 234.266 121.808 261.524 1.00 36.44 ? 82   GLU L CD  1 
ATOM   565  O OE1 . GLU A 1 82  ? 234.799 121.890 262.603 1.00 37.14 ? 82   GLU L OE1 1 
ATOM   566  O OE2 . GLU A 1 82  ? 233.496 120.924 261.234 1.00 36.21 ? 82   GLU L OE2 1 
ATOM   567  N N   . ALA A 1 83  ? 234.368 125.374 258.043 1.00 34.63 ? 83   ALA L N   1 
ATOM   568  C CA  . ALA A 1 83  ? 233.248 125.996 257.344 1.00 34.00 ? 83   ALA L CA  1 
ATOM   569  C C   . ALA A 1 83  ? 233.103 125.435 255.938 1.00 33.02 ? 83   ALA L C   1 
ATOM   570  O O   . ALA A 1 83  ? 234.014 124.786 255.423 1.00 33.24 ? 83   ALA L O   1 
ATOM   571  C CB  . ALA A 1 83  ? 233.431 127.504 257.282 1.00 33.69 ? 83   ALA L CB  1 
ATOM   572  N N   . ASP A 1 84  ? 231.980 125.740 255.300 1.00 31.65 ? 84   ASP L N   1 
ATOM   573  C CA  . ASP A 1 84  ? 231.801 125.435 253.888 1.00 31.98 ? 84   ASP L CA  1 
ATOM   574  C C   . ASP A 1 84  ? 232.223 126.626 253.039 1.00 30.81 ? 84   ASP L C   1 
ATOM   575  O O   . ASP A 1 84  ? 231.662 127.715 253.160 1.00 32.08 ? 84   ASP L O   1 
ATOM   576  C CB  . ASP A 1 84  ? 230.349 125.062 253.588 1.00 31.17 ? 84   ASP L CB  1 
ATOM   577  C CG  . ASP A 1 84  ? 229.952 123.715 254.177 1.00 31.91 ? 84   ASP L CG  1 
ATOM   578  O OD1 . ASP A 1 84  ? 230.827 122.993 254.590 1.00 32.66 ? 84   ASP L OD1 1 
ATOM   579  O OD2 . ASP A 1 84  ? 228.782 123.420 254.207 1.00 30.61 ? 84   ASP L OD2 1 
ATOM   580  N N   . TYR A 1 85  ? 233.240 126.433 252.212 1.00 31.80 ? 85   TYR L N   1 
ATOM   581  C CA  . TYR A 1 85  ? 233.769 127.524 251.406 1.00 31.51 ? 85   TYR L CA  1 
ATOM   582  C C   . TYR A 1 85  ? 233.239 127.457 249.983 1.00 30.65 ? 85   TYR L C   1 
ATOM   583  O O   . TYR A 1 85  ? 233.236 126.397 249.358 1.00 30.82 ? 85   TYR L O   1 
ATOM   584  C CB  . TYR A 1 85  ? 235.297 127.493 251.414 1.00 31.51 ? 85   TYR L CB  1 
ATOM   585  C CG  . TYR A 1 85  ? 235.899 127.855 252.751 1.00 31.71 ? 85   TYR L CG  1 
ATOM   586  C CD1 . TYR A 1 85  ? 235.936 126.918 253.766 1.00 32.95 ? 85   TYR L CD1 1 
ATOM   587  C CD2 . TYR A 1 85  ? 236.416 129.120 252.962 1.00 32.16 ? 85   TYR L CD2 1 
ATOM   588  C CE1 . TYR A 1 85  ? 236.479 127.245 254.986 1.00 33.91 ? 85   TYR L CE1 1 
ATOM   589  C CE2 . TYR A 1 85  ? 236.966 129.444 254.184 1.00 32.84 ? 85   TYR L CE2 1 
ATOM   590  C CZ  . TYR A 1 85  ? 236.996 128.508 255.196 1.00 33.85 ? 85   TYR L CZ  1 
ATOM   591  O OH  . TYR A 1 85  ? 237.543 128.825 256.421 1.00 35.19 ? 85   TYR L OH  1 
ATOM   592  N N   . TYR A 1 86  ? 232.793 128.594 249.473 1.00 30.71 ? 86   TYR L N   1 
ATOM   593  C CA  . TYR A 1 86  ? 232.253 128.660 248.124 1.00 29.97 ? 86   TYR L CA  1 
ATOM   594  C C   . TYR A 1 86  ? 233.034 129.651 247.281 1.00 29.75 ? 86   TYR L C   1 
ATOM   595  O O   . TYR A 1 86  ? 233.420 130.711 247.771 1.00 29.53 ? 86   TYR L O   1 
ATOM   596  C CB  . TYR A 1 86  ? 230.784 129.086 248.159 1.00 29.79 ? 86   TYR L CB  1 
ATOM   597  C CG  . TYR A 1 86  ? 229.883 128.138 248.891 1.00 30.22 ? 86   TYR L CG  1 
ATOM   598  C CD1 . TYR A 1 86  ? 229.239 127.127 248.204 1.00 29.68 ? 86   TYR L CD1 1 
ATOM   599  C CD2 . TYR A 1 86  ? 229.695 128.283 250.251 1.00 30.82 ? 86   TYR L CD2 1 
ATOM   600  C CE1 . TYR A 1 86  ? 228.411 126.262 248.880 1.00 29.73 ? 86   TYR L CE1 1 
ATOM   601  C CE2 . TYR A 1 86  ? 228.866 127.418 250.924 1.00 30.66 ? 86   TYR L CE2 1 
ATOM   602  C CZ  . TYR A 1 86  ? 228.226 126.412 250.246 1.00 29.92 ? 86   TYR L CZ  1 
ATOM   603  O OH  . TYR A 1 86  ? 227.398 125.550 250.921 1.00 29.88 ? 86   TYR L OH  1 
ATOM   604  N N   . CYS A 1 87  ? 233.209 129.334 245.997 1.00 29.17 ? 87   CYS L N   1 
ATOM   605  C CA  . CYS A 1 87  ? 233.798 130.264 245.038 1.00 29.33 ? 87   CYS L CA  1 
ATOM   606  C C   . CYS A 1 87  ? 232.735 130.776 244.079 1.00 28.50 ? 87   CYS L C   1 
ATOM   607  O O   . CYS A 1 87  ? 231.767 130.079 243.766 1.00 28.90 ? 87   CYS L O   1 
ATOM   608  C CB  . CYS A 1 87  ? 234.957 129.618 244.258 1.00 30.21 ? 87   CYS L CB  1 
ATOM   609  S SG  . CYS A 1 87  ? 234.514 128.211 243.211 1.00 30.94 ? 87   CYS L SG  1 
ATOM   610  N N   . GLN A 1 88  ? 232.937 131.992 243.599 1.00 28.27 ? 88   GLN L N   1 
ATOM   611  C CA  . GLN A 1 88  ? 232.042 132.603 242.631 1.00 28.78 ? 88   GLN L CA  1 
ATOM   612  C C   . GLN A 1 88  ? 232.811 133.307 241.532 1.00 29.22 ? 88   GLN L C   1 
ATOM   613  O O   . GLN A 1 88  ? 233.878 133.873 241.769 1.00 29.49 ? 88   GLN L O   1 
ATOM   614  C CB  . GLN A 1 88  ? 231.105 133.602 243.306 1.00 28.53 ? 88   GLN L CB  1 
ATOM   615  C CG  . GLN A 1 88  ? 230.178 134.316 242.341 1.00 28.84 ? 88   GLN L CG  1 
ATOM   616  C CD  . GLN A 1 88  ? 229.137 135.134 243.030 1.00 29.07 ? 88   GLN L CD  1 
ATOM   617  O OE1 . GLN A 1 88  ? 229.385 135.761 244.063 1.00 28.88 ? 88   GLN L OE1 1 
ATOM   618  N NE2 . GLN A 1 88  ? 227.944 135.139 242.457 1.00 29.43 ? 88   GLN L NE2 1 
ATOM   619  N N   . ALA A 1 89  ? 232.250 133.298 240.333 1.00 29.10 ? 89   ALA L N   1 
ATOM   620  C CA  . ALA A 1 89  ? 232.822 134.063 239.236 1.00 29.43 ? 89   ALA L CA  1 
ATOM   621  C C   . ALA A 1 89  ? 231.728 134.555 238.310 1.00 29.74 ? 89   ALA L C   1 
ATOM   622  O O   . ALA A 1 89  ? 230.731 133.869 238.096 1.00 30.32 ? 89   ALA L O   1 
ATOM   623  C CB  . ALA A 1 89  ? 233.822 133.219 238.474 1.00 31.29 ? 89   ALA L CB  1 
ATOM   624  N N   . TRP A 1 90  ? 231.921 135.744 237.756 1.00 29.83 ? 90   TRP L N   1 
ATOM   625  C CA  . TRP A 1 90  ? 230.955 136.313 236.827 1.00 29.86 ? 90   TRP L CA  1 
ATOM   626  C C   . TRP A 1 90  ? 231.469 136.287 235.398 1.00 30.65 ? 90   TRP L C   1 
ATOM   627  O O   . TRP A 1 90  ? 232.507 136.873 235.092 1.00 32.20 ? 90   TRP L O   1 
ATOM   628  C CB  . TRP A 1 90  ? 230.643 137.756 237.208 1.00 29.72 ? 90   TRP L CB  1 
ATOM   629  C CG  . TRP A 1 90  ? 229.880 137.899 238.472 1.00 28.88 ? 90   TRP L CG  1 
ATOM   630  C CD1 . TRP A 1 90  ? 230.393 138.007 239.724 1.00 28.90 ? 90   TRP L CD1 1 
ATOM   631  C CD2 . TRP A 1 90  ? 228.450 137.976 238.618 1.00 28.89 ? 90   TRP L CD2 1 
ATOM   632  N NE1 . TRP A 1 90  ? 229.385 138.147 240.633 1.00 28.45 ? 90   TRP L NE1 1 
ATOM   633  C CE2 . TRP A 1 90  ? 228.189 138.136 239.973 1.00 28.32 ? 90   TRP L CE2 1 
ATOM   634  C CE3 . TRP A 1 90  ? 227.390 137.934 237.719 1.00 29.08 ? 90   TRP L CE3 1 
ATOM   635  C CZ2 . TRP A 1 90  ? 226.907 138.260 240.458 1.00 28.29 ? 90   TRP L CZ2 1 
ATOM   636  C CZ3 . TRP A 1 90  ? 226.103 138.063 238.203 1.00 29.63 ? 90   TRP L CZ3 1 
ATOM   637  C CH2 . TRP A 1 90  ? 225.870 138.223 239.539 1.00 29.25 ? 90   TRP L CH2 1 
ATOM   638  N N   . ASP A 1 91  ? 230.724 135.619 234.518 1.00 30.72 ? 91   ASP L N   1 
ATOM   639  C CA  . ASP A 1 91  ? 231.102 135.628 233.083 1.00 30.50 ? 91   ASP L CA  1 
ATOM   640  C C   . ASP A 1 91  ? 230.202 136.634 232.365 1.00 30.91 ? 91   ASP L C   1 
ATOM   641  O O   . ASP A 1 91  ? 229.109 136.232 231.937 1.00 30.94 ? 91   ASP L O   1 
ATOM   642  C CB  . ASP A 1 91  ? 231.014 134.233 232.464 1.00 30.61 ? 91   ASP L CB  1 
ATOM   643  N N   . LYS A 1 92  ? 230.630 137.898 232.284 1.00 30.88 ? 92   LYS L N   1 
ATOM   644  C CA  . LYS A 1 92  ? 229.845 138.938 231.565 1.00 30.65 ? 92   LYS L CA  1 
ATOM   645  C C   . LYS A 1 92  ? 228.412 138.988 232.101 1.00 30.40 ? 92   LYS L C   1 
ATOM   646  O O   . LYS A 1 92  ? 227.491 138.885 231.266 1.00 31.09 ? 92   LYS L O   1 
ATOM   647  C CB  . LYS A 1 92  ? 229.908 138.728 230.049 1.00 32.31 ? 92   LYS L CB  1 
ATOM   648  C CG  . LYS A 1 92  ? 231.306 138.764 229.447 1.00 31.59 ? 92   LYS L CG  1 
ATOM   649  C CD  . LYS A 1 92  ? 231.305 138.708 227.936 1.00 31.29 ? 92   LYS L CD  1 
ATOM   650  C CE  . LYS A 1 92  ? 230.479 139.811 227.310 1.00 31.11 ? 92   LYS L CE  1 
ATOM   651  N NZ  . LYS A 1 92  ? 230.902 141.149 227.786 1.00 31.75 ? 92   LYS L NZ  1 
ATOM   652  N N   . THR A 1 93  ? 228.240 139.062 233.427 1.00 30.21 ? 93   THR L N   1 
ATOM   653  C CA  . THR A 1 93  ? 226.897 139.177 234.068 1.00 29.89 ? 93   THR L CA  1 
ATOM   654  C C   . THR A 1 93  ? 226.229 137.809 234.240 1.00 30.31 ? 93   THR L C   1 
ATOM   655  O O   . THR A 1 93  ? 225.088 137.783 234.737 1.00 30.34 ? 93   THR L O   1 
ATOM   656  C CB  . THR A 1 93  ? 226.022 140.264 233.432 1.00 29.78 ? 93   THR L CB  1 
ATOM   657  N N   . ILE A 1 94  ? 226.911 136.718 233.879 1.00 30.37 ? 94   ILE L N   1 
ATOM   658  C CA  . ILE A 1 94  ? 226.346 135.360 234.141 1.00 30.61 ? 94   ILE L CA  1 
ATOM   659  C C   . ILE A 1 94  ? 226.959 134.847 235.444 1.00 30.34 ? 94   ILE L C   1 
ATOM   660  O O   . ILE A 1 94  ? 228.177 134.596 235.456 1.00 30.83 ? 94   ILE L O   1 
ATOM   661  C CB  . ILE A 1 94  ? 226.583 134.399 232.961 1.00 30.60 ? 94   ILE L CB  1 
ATOM   662  C CG1 . ILE A 1 94  ? 225.998 134.951 231.659 1.00 30.81 ? 94   ILE L CG1 1 
ATOM   663  C CG2 . ILE A 1 94  ? 226.037 133.016 233.276 1.00 31.25 ? 94   ILE L CG2 1 
ATOM   664  C CD1 . ILE A 1 94  ? 224.533 135.304 231.750 1.00 30.16 ? 94   ILE L CD1 1 
ATOM   665  N N   . ALA A 1 95  ? 226.154 134.712 236.499 1.00 31.00 ? 95   ALA L N   1 
ATOM   666  C CA  . ALA A 1 95  ? 226.623 134.271 237.807 1.00 30.21 ? 95   ALA L CA  1 
ATOM   667  C C   . ALA A 1 95  ? 226.894 132.780 237.831 1.00 30.41 ? 95   ALA L C   1 
ATOM   668  O O   . ALA A 1 95  ? 226.415 132.036 236.973 1.00 31.78 ? 95   ALA L O   1 
ATOM   669  C CB  . ALA A 1 95  ? 225.604 134.594 238.877 1.00 30.46 ? 95   ALA L CB  1 
ATOM   670  N N   . GLY A 1 96  ? 227.610 132.346 238.859 1.00 29.68 ? 96   GLY L N   1 
ATOM   671  C CA  . GLY A 1 96  ? 227.837 130.931 239.095 1.00 30.61 ? 96   GLY L CA  1 
ATOM   672  C C   . GLY A 1 96  ? 228.630 130.704 240.375 1.00 30.21 ? 96   GLY L C   1 
ATOM   673  O O   . GLY A 1 96  ? 229.685 131.305 240.588 1.00 29.78 ? 96   GLY L O   1 
ATOM   674  N N   . PHE A 1 97  ? 228.114 129.815 241.215 1.00 30.01 ? 97   PHE L N   1 
ATOM   675  C CA  . PHE A 1 97  ? 228.791 129.387 242.433 1.00 28.83 ? 97   PHE L CA  1 
ATOM   676  C C   . PHE A 1 97  ? 229.238 127.945 242.277 1.00 29.22 ? 97   PHE L C   1 
ATOM   677  O O   . PHE A 1 97  ? 228.593 127.164 241.578 1.00 31.01 ? 97   PHE L O   1 
ATOM   678  C CB  . PHE A 1 97  ? 227.867 129.471 243.652 1.00 29.23 ? 97   PHE L CB  1 
ATOM   679  C CG  . PHE A 1 97  ? 227.538 130.854 244.145 1.00 29.26 ? 97   PHE L CG  1 
ATOM   680  C CD1 . PHE A 1 97  ? 228.350 131.478 245.075 1.00 28.83 ? 97   PHE L CD1 1 
ATOM   681  C CD2 . PHE A 1 97  ? 226.404 131.517 243.708 1.00 29.45 ? 97   PHE L CD2 1 
ATOM   682  C CE1 . PHE A 1 97  ? 228.041 132.733 245.555 1.00 28.22 ? 97   PHE L CE1 1 
ATOM   683  C CE2 . PHE A 1 97  ? 226.095 132.773 244.188 1.00 29.28 ? 97   PHE L CE2 1 
ATOM   684  C CZ  . PHE A 1 97  ? 226.918 133.379 245.113 1.00 28.34 ? 97   PHE L CZ  1 
ATOM   685  N N   . GLY A 1 98  ? 230.314 127.581 242.954 1.00 28.92 ? 98   GLY L N   1 
ATOM   686  C CA  . GLY A 1 98  ? 230.756 126.194 242.948 1.00 29.12 ? 98   GLY L CA  1 
ATOM   687  C C   . GLY A 1 98  ? 229.899 125.363 243.895 1.00 28.61 ? 98   GLY L C   1 
ATOM   688  O O   . GLY A 1 98  ? 229.062 125.902 244.617 1.00 28.78 ? 98   GLY L O   1 
ATOM   689  N N   . GLY A 1 99  ? 230.115 124.050 243.899 1.00 29.23 ? 99   GLY L N   1 
ATOM   690  C CA  . GLY A 1 99  ? 229.327 123.142 244.728 1.00 29.43 ? 99   GLY L CA  1 
ATOM   691  C C   . GLY A 1 99  ? 229.564 123.357 246.219 1.00 29.54 ? 99   GLY L C   1 
ATOM   692  O O   . GLY A 1 99  ? 228.730 122.991 247.047 1.00 29.49 ? 99   GLY L O   1 
ATOM   693  N N   . GLY A 1 100 ? 230.712 123.927 246.556 1.00 29.47 ? 100  GLY L N   1 
ATOM   694  C CA  . GLY A 1 100 ? 231.058 124.184 247.946 1.00 29.85 ? 100  GLY L CA  1 
ATOM   695  C C   . GLY A 1 100 ? 232.011 123.129 248.479 1.00 30.18 ? 100  GLY L C   1 
ATOM   696  O O   . GLY A 1 100 ? 231.825 121.935 248.244 1.00 30.53 ? 100  GLY L O   1 
ATOM   697  N N   . THR A 1 101 ? 233.026 123.573 249.208 1.00 30.40 ? 101  THR L N   1 
ATOM   698  C CA  . THR A 1 101 ? 234.018 122.666 249.759 1.00 30.96 ? 101  THR L CA  1 
ATOM   699  C C   . THR A 1 101 ? 233.921 122.635 251.271 1.00 31.37 ? 101  THR L C   1 
ATOM   700  O O   . THR A 1 101 ? 234.075 123.665 251.928 1.00 32.14 ? 101  THR L O   1 
ATOM   701  C CB  . THR A 1 101 ? 235.441 123.111 249.379 1.00 31.36 ? 101  THR L CB  1 
ATOM   702  O OG1 . THR A 1 101 ? 235.567 123.173 247.955 1.00 30.81 ? 101  THR L OG1 1 
ATOM   703  C CG2 . THR A 1 101 ? 236.465 122.133 249.930 1.00 31.94 ? 101  THR L CG2 1 
ATOM   704  N N   . LYS A 1 102 ? 233.676 121.456 251.836 1.00 31.91 ? 102  LYS L N   1 
ATOM   705  C CA  . LYS A 1 102 ? 233.618 121.355 253.314 1.00 32.27 ? 102  LYS L CA  1 
ATOM   706  C C   . LYS A 1 102 ? 235.029 121.228 253.870 1.00 33.12 ? 102  LYS L C   1 
ATOM   707  O O   . LYS A 1 102 ? 235.668 120.201 253.611 1.00 33.31 ? 102  LYS L O   1 
ATOM   708  C CB  . LYS A 1 102 ? 232.717 120.214 253.786 1.00 32.68 ? 102  LYS L CB  1 
ATOM   709  C CG  . LYS A 1 102 ? 232.713 120.009 255.294 1.00 33.97 ? 102  LYS L CG  1 
ATOM   710  C CD  . LYS A 1 102 ? 231.371 119.598 255.855 1.00 33.87 ? 102  LYS L CD  1 
ATOM   711  C CE  . LYS A 1 102 ? 231.302 119.753 257.359 1.00 34.66 ? 102  LYS L CE  1 
ATOM   712  N NZ  . LYS A 1 102 ? 229.941 119.485 257.877 1.00 35.59 ? 102  LYS L NZ  1 
ATOM   713  N N   . LEU A 1 103 ? 235.485 122.234 254.610 1.00 33.98 ? 103  LEU L N   1 
ATOM   714  C CA  . LEU A 1 103 ? 236.814 122.215 255.205 1.00 34.62 ? 103  LEU L CA  1 
ATOM   715  C C   . LEU A 1 103 ? 236.753 121.840 256.668 1.00 35.34 ? 103  LEU L C   1 
ATOM   716  O O   . LEU A 1 103 ? 236.150 122.552 257.472 1.00 35.59 ? 103  LEU L O   1 
ATOM   717  C CB  . LEU A 1 103 ? 237.493 123.581 255.087 1.00 34.60 ? 103  LEU L CB  1 
ATOM   718  C CG  . LEU A 1 103 ? 238.853 123.718 255.829 1.00 35.37 ? 103  LEU L CG  1 
ATOM   719  C CD1 . LEU A 1 103 ? 239.888 122.807 255.190 1.00 36.42 ? 103  LEU L CD1 1 
ATOM   720  C CD2 . LEU A 1 103 ? 239.305 125.158 255.786 1.00 36.78 ? 103  LEU L CD2 1 
ATOM   721  N N   . THR A 1 104 ? 237.419 120.749 257.018 1.00 36.18 ? 104  THR L N   1 
ATOM   722  C CA  . THR A 1 104 ? 237.483 120.307 258.401 1.00 36.41 ? 104  THR L CA  1 
ATOM   723  C C   . THR A 1 104 ? 238.915 120.436 258.903 1.00 37.12 ? 104  THR L C   1 
ATOM   724  O O   . THR A 1 104 ? 239.851 120.481 258.101 1.00 37.14 ? 104  THR L O   1 
ATOM   725  C CB  . THR A 1 104 ? 236.996 118.853 258.540 1.00 36.72 ? 104  THR L CB  1 
ATOM   726  N N   . VAL A 1 105 ? 239.080 120.514 260.229 1.00 37.41 ? 105  VAL L N   1 
ATOM   727  C CA  . VAL A 1 105 ? 240.390 120.731 260.845 1.00 37.92 ? 105  VAL L CA  1 
ATOM   728  C C   . VAL A 1 105 ? 240.568 119.786 262.031 1.00 38.56 ? 105  VAL L C   1 
ATOM   729  O O   . VAL A 1 105 ? 239.660 119.617 262.848 1.00 37.43 ? 105  VAL L O   1 
ATOM   730  C CB  . VAL A 1 105 ? 240.544 122.219 261.307 1.00 39.00 ? 105  VAL L CB  1 
ATOM   731  N N   . GLN B 2 1   ? 226.353 151.659 259.535 1.00 37.93 ? 1    GLN H N   1 
ATOM   732  C CA  . GLN B 2 1   ? 226.820 150.505 258.776 1.00 37.31 ? 1    GLN H CA  1 
ATOM   733  C C   . GLN B 2 1   ? 225.761 150.082 257.755 1.00 36.12 ? 1    GLN H C   1 
ATOM   734  O O   . GLN B 2 1   ? 224.690 150.688 257.682 1.00 35.39 ? 1    GLN H O   1 
ATOM   735  C CB  . GLN B 2 1   ? 227.166 149.332 259.727 1.00 37.40 ? 1    GLN H CB  1 
ATOM   736  N N   . ILE B 2 2   ? 226.068 149.041 256.971 1.00 35.22 ? 2    ILE H N   1 
ATOM   737  C CA  . ILE B 2 2   ? 225.166 148.511 255.947 1.00 34.12 ? 2    ILE H CA  1 
ATOM   738  C C   . ILE B 2 2   ? 224.539 147.202 256.396 1.00 33.38 ? 2    ILE H C   1 
ATOM   739  O O   . ILE B 2 2   ? 225.238 146.280 256.816 1.00 33.40 ? 2    ILE H O   1 
ATOM   740  C CB  . ILE B 2 2   ? 225.906 148.300 254.615 1.00 33.44 ? 2    ILE H CB  1 
ATOM   741  C CG1 . ILE B 2 2   ? 226.422 149.648 254.091 1.00 34.41 ? 2    ILE H CG1 1 
ATOM   742  C CG2 . ILE B 2 2   ? 224.980 147.639 253.602 1.00 32.17 ? 2    ILE H CG2 1 
ATOM   743  C CD1 . ILE B 2 2   ? 227.371 149.531 252.916 1.00 34.16 ? 2    ILE H CD1 1 
ATOM   744  N N   . THR B 2 3   ? 223.217 147.129 256.307 1.00 33.11 ? 3    THR H N   1 
ATOM   745  C CA  . THR B 2 3   ? 222.489 145.928 256.691 1.00 32.79 ? 3    THR H CA  1 
ATOM   746  C C   . THR B 2 3   ? 221.294 145.686 255.780 1.00 32.68 ? 3    THR H C   1 
ATOM   747  O O   . THR B 2 3   ? 220.702 146.625 255.245 1.00 32.67 ? 3    THR H O   1 
ATOM   748  C CB  . THR B 2 3   ? 222.018 146.016 258.153 1.00 32.84 ? 3    THR H CB  1 
ATOM   749  O OG1 . THR B 2 3   ? 221.388 144.785 258.524 1.00 32.29 ? 3    THR H OG1 1 
ATOM   750  C CG2 . THR B 2 3   ? 221.032 147.163 258.323 1.00 33.15 ? 3    THR H CG2 1 
ATOM   751  N N   . LEU B 2 4   ? 220.942 144.417 255.609 1.00 32.42 ? 4    LEU H N   1 
ATOM   752  C CA  . LEU B 2 4   ? 219.786 144.032 254.809 1.00 32.32 ? 4    LEU H CA  1 
ATOM   753  C C   . LEU B 2 4   ? 218.896 143.021 255.527 1.00 32.61 ? 4    LEU H C   1 
ATOM   754  O O   . LEU B 2 4   ? 219.395 142.097 256.171 1.00 32.54 ? 4    LEU H O   1 
ATOM   755  C CB  . LEU B 2 4   ? 220.242 143.493 253.444 1.00 31.56 ? 4    LEU H CB  1 
ATOM   756  C CG  . LEU B 2 4   ? 221.063 144.466 252.558 1.00 31.34 ? 4    LEU H CG  1 
ATOM   757  C CD1 . LEU B 2 4   ? 222.553 144.225 252.772 1.00 30.58 ? 4    LEU H CD1 1 
ATOM   758  C CD2 . LEU B 2 4   ? 220.696 144.252 251.098 1.00 31.48 ? 4    LEU H CD2 1 
ATOM   759  N N   . LYS B 2 5   ? 217.572 143.185 255.398 1.00 32.72 ? 5    LYS H N   1 
ATOM   760  C CA  . LYS B 2 5   ? 216.620 142.304 256.131 1.00 32.44 ? 5    LYS H CA  1 
ATOM   761  C C   . LYS B 2 5   ? 215.571 141.694 255.201 1.00 32.72 ? 5    LYS H C   1 
ATOM   762  O O   . LYS B 2 5   ? 214.773 142.467 254.654 1.00 32.82 ? 5    LYS H O   1 
ATOM   763  C CB  . LYS B 2 5   ? 215.888 143.090 257.221 1.00 33.08 ? 5    LYS H CB  1 
ATOM   764  C CG  . LYS B 2 5   ? 216.775 143.923 258.135 1.00 33.91 ? 5    LYS H CG  1 
ATOM   765  C CD  . LYS B 2 5   ? 216.118 144.263 259.453 1.00 34.19 ? 5    LYS H CD  1 
ATOM   766  C CE  . LYS B 2 5   ? 215.738 143.032 260.248 1.00 34.66 ? 5    LYS H CE  1 
ATOM   767  N NZ  . LYS B 2 5   ? 216.894 142.124 260.438 1.00 35.38 ? 5    LYS H NZ  1 
ATOM   768  N N   . GLU B 2 6   ? 215.549 140.367 255.055 1.00 32.11 ? 6    GLU H N   1 
ATOM   769  C CA  . GLU B 2 6   ? 214.576 139.646 254.247 1.00 31.97 ? 6    GLU H CA  1 
ATOM   770  C C   . GLU B 2 6   ? 213.274 139.452 255.011 1.00 32.35 ? 6    GLU H C   1 
ATOM   771  O O   . GLU B 2 6   ? 213.286 139.080 256.186 1.00 32.84 ? 6    GLU H O   1 
ATOM   772  C CB  . GLU B 2 6   ? 215.088 138.283 253.778 1.00 31.72 ? 6    GLU H CB  1 
ATOM   773  C CG  . GLU B 2 6   ? 216.356 138.337 252.952 1.00 31.64 ? 6    GLU H CG  1 
ATOM   774  C CD  . GLU B 2 6   ? 217.615 138.451 253.791 1.00 32.04 ? 6    GLU H CD  1 
ATOM   775  O OE1 . GLU B 2 6   ? 217.509 138.610 254.987 1.00 31.77 ? 6    GLU H OE1 1 
ATOM   776  O OE2 . GLU B 2 6   ? 218.681 138.345 253.234 1.00 31.17 ? 6    GLU H OE2 1 
ATOM   777  N N   . SER B 2 7   ? 212.153 139.611 254.316 1.00 31.98 ? 7    SER H N   1 
ATOM   778  C CA  . SER B 2 7   ? 210.853 139.283 254.886 1.00 32.56 ? 7    SER H CA  1 
ATOM   779  C C   . SER B 2 7   ? 209.882 138.800 253.815 1.00 33.18 ? 7    SER H C   1 
ATOM   780  O O   . SER B 2 7   ? 210.052 139.077 252.627 1.00 33.01 ? 7    SER H O   1 
ATOM   781  C CB  . SER B 2 7   ? 210.270 140.485 255.602 1.00 32.79 ? 7    SER H CB  1 
ATOM   782  O OG  . SER B 2 7   ? 209.958 141.510 254.700 1.00 33.35 ? 7    SER H OG  1 
ATOM   783  N N   . GLY B 2 8   ? 208.856 138.077 254.245 1.00 34.14 ? 8    GLY H N   1 
ATOM   784  C CA  . GLY B 2 8   ? 207.838 137.566 253.335 1.00 33.35 ? 8    GLY H CA  1 
ATOM   785  C C   . GLY B 2 8   ? 207.378 136.188 253.790 1.00 33.72 ? 8    GLY H C   1 
ATOM   786  O O   . GLY B 2 8   ? 207.847 135.689 254.813 1.00 33.59 ? 8    GLY H O   1 
ATOM   787  N N   . PRO B 2 9   ? 206.473 135.561 253.039 1.00 33.79 ? 9    PRO H N   1 
ATOM   788  C CA  . PRO B 2 9   ? 205.864 134.269 253.301 1.00 33.98 ? 9    PRO H CA  1 
ATOM   789  C C   . PRO B 2 9   ? 206.922 133.190 253.443 1.00 34.08 ? 9    PRO H C   1 
ATOM   790  O O   . PRO B 2 9   ? 207.877 133.147 252.670 1.00 34.06 ? 9    PRO H O   1 
ATOM   791  C CB  . PRO B 2 9   ? 205.014 134.044 252.041 1.00 34.57 ? 9    PRO H CB  1 
ATOM   792  C CG  . PRO B 2 9   ? 204.742 135.436 251.513 1.00 33.27 ? 9    PRO H CG  1 
ATOM   793  C CD  . PRO B 2 9   ? 206.008 136.211 251.814 1.00 33.76 ? 9    PRO H CD  1 
ATOM   794  N N   . THR B 2 10  ? 206.730 132.304 254.412 1.00 34.04 ? 10   THR H N   1 
ATOM   795  C CA  . THR B 2 10  ? 207.658 131.204 254.641 1.00 34.00 ? 10   THR H CA  1 
ATOM   796  C C   . THR B 2 10  ? 207.054 129.894 254.162 1.00 34.87 ? 10   THR H C   1 
ATOM   797  O O   . THR B 2 10  ? 207.649 128.825 254.306 1.00 34.87 ? 10   THR H O   1 
ATOM   798  C CB  . THR B 2 10  ? 208.028 131.101 256.128 1.00 34.40 ? 10   THR H CB  1 
ATOM   799  O OG1 . THR B 2 10  ? 206.843 130.868 256.902 1.00 34.08 ? 10   THR H OG1 1 
ATOM   800  C CG2 . THR B 2 10  ? 208.686 132.391 256.585 1.00 34.60 ? 10   THR H CG2 1 
ATOM   801  N N   . LEU B 2 11  ? 205.857 129.984 253.601 1.00 34.89 ? 11   LEU H N   1 
ATOM   802  C CA  . LEU B 2 11  ? 205.177 128.823 253.053 1.00 35.51 ? 11   LEU H CA  1 
ATOM   803  C C   . LEU B 2 11  ? 204.253 129.212 251.916 1.00 35.80 ? 11   LEU H C   1 
ATOM   804  O O   . LEU B 2 11  ? 203.359 130.042 252.082 1.00 36.71 ? 11   LEU H O   1 
ATOM   805  C CB  . LEU B 2 11  ? 204.370 128.103 254.141 1.00 35.84 ? 11   LEU H CB  1 
ATOM   806  C CG  . LEU B 2 11  ? 203.492 126.916 253.662 1.00 36.14 ? 11   LEU H CG  1 
ATOM   807  C CD1 . LEU B 2 11  ? 204.374 125.798 253.107 1.00 36.31 ? 11   LEU H CD1 1 
ATOM   808  C CD2 . LEU B 2 11  ? 202.660 126.414 254.829 1.00 35.87 ? 11   LEU H CD2 1 
ATOM   809  N N   . VAL B 2 12  ? 204.460 128.586 250.770 1.00 35.36 ? 12   VAL H N   1 
ATOM   810  C CA  . VAL B 2 12  ? 203.582 128.768 249.626 1.00 35.72 ? 12   VAL H CA  1 
ATOM   811  C C   . VAL B 2 12  ? 203.222 127.410 249.053 1.00 36.49 ? 12   VAL H C   1 
ATOM   812  O O   . VAL B 2 12  ? 203.963 126.443 249.228 1.00 36.13 ? 12   VAL H O   1 
ATOM   813  C CB  . VAL B 2 12  ? 204.251 129.645 248.549 1.00 36.22 ? 12   VAL H CB  1 
ATOM   814  C CG1 . VAL B 2 12  ? 204.555 131.026 249.112 1.00 36.65 ? 12   VAL H CG1 1 
ATOM   815  C CG2 . VAL B 2 12  ? 205.523 128.979 248.061 1.00 36.30 ? 12   VAL H CG2 1 
ATOM   816  N N   . LYS B 2 13  ? 202.109 127.340 248.344 1.00 37.40 ? 13   LYS H N   1 
ATOM   817  C CA  . LYS B 2 13  ? 201.719 126.095 247.706 1.00 37.61 ? 13   LYS H CA  1 
ATOM   818  C C   . LYS B 2 13  ? 202.270 126.042 246.287 1.00 37.23 ? 13   LYS H C   1 
ATOM   819  O O   . LYS B 2 13  ? 202.642 127.075 245.731 1.00 37.18 ? 13   LYS H O   1 
ATOM   820  C CB  . LYS B 2 13  ? 200.195 125.950 247.717 1.00 37.83 ? 13   LYS H CB  1 
ATOM   821  N N   . PRO B 2 14  ? 202.363 124.855 245.695 1.00 36.93 ? 14   PRO H N   1 
ATOM   822  C CA  . PRO B 2 14  ? 202.722 124.633 244.315 1.00 37.02 ? 14   PRO H CA  1 
ATOM   823  C C   . PRO B 2 14  ? 201.851 125.476 243.402 1.00 36.80 ? 14   PRO H C   1 
ATOM   824  O O   . PRO B 2 14  ? 200.654 125.617 243.642 1.00 37.00 ? 14   PRO H O   1 
ATOM   825  C CB  . PRO B 2 14  ? 202.446 123.135 244.153 1.00 38.69 ? 14   PRO H CB  1 
ATOM   826  C CG  . PRO B 2 14  ? 202.685 122.564 245.537 1.00 38.10 ? 14   PRO H CG  1 
ATOM   827  C CD  . PRO B 2 14  ? 202.183 123.630 246.484 1.00 37.28 ? 14   PRO H CD  1 
ATOM   828  N N   . THR B 2 15  ? 202.483 126.040 242.373 1.00 36.57 ? 15   THR H N   1 
ATOM   829  C CA  . THR B 2 15  ? 201.880 126.896 241.342 1.00 36.95 ? 15   THR H CA  1 
ATOM   830  C C   . THR B 2 15  ? 201.521 128.294 241.851 1.00 36.95 ? 15   THR H C   1 
ATOM   831  O O   . THR B 2 15  ? 201.056 129.133 241.080 1.00 36.59 ? 15   THR H O   1 
ATOM   832  C CB  . THR B 2 15  ? 200.639 126.263 240.662 1.00 37.57 ? 15   THR H CB  1 
ATOM   833  O OG1 . THR B 2 15  ? 199.476 126.430 241.480 1.00 37.67 ? 15   THR H OG1 1 
ATOM   834  C CG2 . THR B 2 15  ? 200.860 124.777 240.383 1.00 38.25 ? 15   THR H CG2 1 
ATOM   835  N N   . GLN B 2 16  ? 201.756 128.564 243.133 1.00 36.74 ? 16   GLN H N   1 
ATOM   836  C CA  . GLN B 2 16  ? 201.509 129.901 243.660 1.00 36.37 ? 16   GLN H CA  1 
ATOM   837  C C   . GLN B 2 16  ? 202.716 130.800 243.440 1.00 35.80 ? 16   GLN H C   1 
ATOM   838  O O   . GLN B 2 16  ? 203.820 130.326 243.164 1.00 36.00 ? 16   GLN H O   1 
ATOM   839  C CB  . GLN B 2 16  ? 201.144 129.875 245.148 1.00 37.25 ? 16   GLN H CB  1 
ATOM   840  N N   . THR B 2 17  ? 202.494 132.106 243.541 1.00 35.18 ? 17   THR H N   1 
ATOM   841  C CA  . THR B 2 17  ? 203.561 133.079 243.353 1.00 35.11 ? 17   THR H CA  1 
ATOM   842  C C   . THR B 2 17  ? 204.081 133.601 244.688 1.00 34.84 ? 17   THR H C   1 
ATOM   843  O O   . THR B 2 17  ? 203.307 133.992 245.563 1.00 35.51 ? 17   THR H O   1 
ATOM   844  C CB  . THR B 2 17  ? 203.085 134.255 242.480 1.00 34.85 ? 17   THR H CB  1 
ATOM   845  O OG1 . THR B 2 17  ? 202.672 133.758 241.198 1.00 34.99 ? 17   THR H OG1 1 
ATOM   846  C CG2 . THR B 2 17  ? 204.208 135.263 242.286 1.00 34.56 ? 17   THR H CG2 1 
ATOM   847  N N   . LEU B 2 18  ? 205.399 133.598 244.834 1.00 34.16 ? 18   LEU H N   1 
ATOM   848  C CA  . LEU B 2 18  ? 206.061 134.065 246.042 1.00 34.10 ? 18   LEU H CA  1 
ATOM   849  C C   . LEU B 2 18  ? 206.595 135.476 245.880 1.00 33.73 ? 18   LEU H C   1 
ATOM   850  O O   . LEU B 2 18  ? 207.280 135.783 244.904 1.00 33.81 ? 18   LEU H O   1 
ATOM   851  C CB  . LEU B 2 18  ? 207.235 133.145 246.378 1.00 34.62 ? 18   LEU H CB  1 
ATOM   852  C CG  . LEU B 2 18  ? 208.147 133.592 247.532 1.00 34.37 ? 18   LEU H CG  1 
ATOM   853  C CD1 . LEU B 2 18  ? 207.407 133.465 248.861 1.00 34.45 ? 18   LEU H CD1 1 
ATOM   854  C CD2 . LEU B 2 18  ? 209.407 132.749 247.507 1.00 34.69 ? 18   LEU H CD2 1 
ATOM   855  N N   . THR B 2 19  ? 206.328 136.323 246.863 1.00 33.66 ? 19   THR H N   1 
ATOM   856  C CA  . THR B 2 19  ? 206.903 137.660 246.866 1.00 33.04 ? 19   THR H CA  1 
ATOM   857  C C   . THR B 2 19  ? 207.796 137.859 248.081 1.00 33.36 ? 19   THR H C   1 
ATOM   858  O O   . THR B 2 19  ? 207.349 137.717 249.220 1.00 33.56 ? 19   THR H O   1 
ATOM   859  C CB  . THR B 2 19  ? 205.808 138.741 246.848 1.00 32.98 ? 19   THR H CB  1 
ATOM   860  O OG1 . THR B 2 19  ? 205.003 138.589 245.673 1.00 33.59 ? 19   THR H OG1 1 
ATOM   861  C CG2 . THR B 2 19  ? 206.440 140.120 246.840 1.00 33.35 ? 19   THR H CG2 1 
ATOM   862  N N   . LEU B 2 20  ? 209.055 138.206 247.837 1.00 33.05 ? 20   LEU H N   1 
ATOM   863  C CA  . LEU B 2 20  ? 210.001 138.467 248.915 1.00 32.76 ? 20   LEU H CA  1 
ATOM   864  C C   . LEU B 2 20  ? 210.455 139.917 248.902 1.00 32.75 ? 20   LEU H C   1 
ATOM   865  O O   . LEU B 2 20  ? 210.771 140.474 247.850 1.00 32.66 ? 20   LEU H O   1 
ATOM   866  C CB  . LEU B 2 20  ? 211.227 137.553 248.797 1.00 32.18 ? 20   LEU H CB  1 
ATOM   867  C CG  . LEU B 2 20  ? 210.964 136.045 248.855 1.00 32.03 ? 20   LEU H CG  1 
ATOM   868  C CD1 . LEU B 2 20  ? 212.266 135.305 248.602 1.00 32.73 ? 20   LEU H CD1 1 
ATOM   869  C CD2 . LEU B 2 20  ? 210.392 135.676 250.220 1.00 34.47 ? 20   LEU H CD2 1 
ATOM   870  N N   . THR B 2 21  ? 210.500 140.527 250.079 1.00 33.07 ? 21   THR H N   1 
ATOM   871  C CA  . THR B 2 21  ? 210.921 141.917 250.195 1.00 32.67 ? 21   THR H CA  1 
ATOM   872  C C   . THR B 2 21  ? 212.209 142.042 251.001 1.00 32.62 ? 21   THR H C   1 
ATOM   873  O O   . THR B 2 21  ? 212.314 141.505 252.105 1.00 32.45 ? 21   THR H O   1 
ATOM   874  C CB  . THR B 2 21  ? 209.821 142.770 250.857 1.00 33.02 ? 21   THR H CB  1 
ATOM   875  O OG1 . THR B 2 21  ? 208.634 142.726 250.054 1.00 32.86 ? 21   THR H OG1 1 
ATOM   876  C CG2 . THR B 2 21  ? 210.280 144.215 250.997 1.00 34.04 ? 21   THR H CG2 1 
ATOM   877  N N   . CYS B 2 22  ? 213.188 142.766 250.449 1.00 32.31 ? 22   CYS H N   1 
ATOM   878  C CA  . CYS B 2 22  ? 214.447 143.053 251.126 1.00 32.60 ? 22   CYS H CA  1 
ATOM   879  C C   . CYS B 2 22  ? 214.475 144.496 251.616 1.00 32.86 ? 22   CYS H C   1 
ATOM   880  O O   . CYS B 2 22  ? 214.528 145.436 250.819 1.00 32.68 ? 22   CYS H O   1 
ATOM   881  C CB  . CYS B 2 22  ? 215.635 142.803 250.192 1.00 32.28 ? 22   CYS H CB  1 
ATOM   882  S SG  . CYS B 2 22  ? 217.262 143.086 250.946 1.00 33.68 ? 22   CYS H SG  1 
ATOM   883  N N   . LYS B 2 23  ? 214.426 144.664 252.928 1.00 33.13 ? 23   LYS H N   1 
ATOM   884  C CA  . LYS B 2 23  ? 214.462 145.985 253.535 1.00 33.20 ? 23   LYS H CA  1 
ATOM   885  C C   . LYS B 2 23  ? 215.897 146.329 253.883 1.00 33.37 ? 23   LYS H C   1 
ATOM   886  O O   . LYS B 2 23  ? 216.557 145.593 254.617 1.00 33.13 ? 23   LYS H O   1 
ATOM   887  C CB  . LYS B 2 23  ? 213.579 146.033 254.782 1.00 33.11 ? 23   LYS H CB  1 
ATOM   888  N N   . LEU B 2 24  ? 216.402 147.412 253.323 1.00 33.07 ? 24   LEU H N   1 
ATOM   889  C CA  . LEU B 2 24  ? 217.805 147.740 253.513 1.00 33.22 ? 24   LEU H CA  1 
ATOM   890  C C   . LEU B 2 24  ? 218.020 149.068 254.212 1.00 33.66 ? 24   LEU H C   1 
ATOM   891  O O   . LEU B 2 24  ? 217.179 149.966 254.151 1.00 34.14 ? 24   LEU H O   1 
ATOM   892  C CB  . LEU B 2 24  ? 218.519 147.704 252.163 1.00 33.03 ? 24   LEU H CB  1 
ATOM   893  C CG  . LEU B 2 24  ? 217.892 148.549 251.062 1.00 33.13 ? 24   LEU H CG  1 
ATOM   894  C CD1 . LEU B 2 24  ? 218.566 149.918 250.993 1.00 33.40 ? 24   LEU H CD1 1 
ATOM   895  C CD2 . LEU B 2 24  ? 218.005 147.793 249.757 1.00 32.98 ? 24   LEU H CD2 1 
ATOM   896  N N   . SER B 2 25  ? 219.165 149.183 254.873 1.00 33.40 ? 25   SER H N   1 
ATOM   897  C CA  . SER B 2 25  ? 219.549 150.403 255.565 1.00 33.21 ? 25   SER H CA  1 
ATOM   898  C C   . SER B 2 25  ? 221.051 150.628 255.480 1.00 33.08 ? 25   SER H C   1 
ATOM   899  O O   . SER B 2 25  ? 221.827 149.685 255.316 1.00 33.27 ? 25   SER H O   1 
ATOM   900  C CB  . SER B 2 25  ? 219.116 150.352 257.014 1.00 33.54 ? 25   SER H CB  1 
ATOM   901  N N   . GLY B 2 26  ? 221.453 151.891 255.556 1.00 32.77 ? 26   GLY H N   1 
ATOM   902  C CA  . GLY B 2 26  ? 222.858 152.270 255.455 1.00 33.63 ? 26   GLY H CA  1 
ATOM   903  C C   . GLY B 2 26  ? 223.168 152.804 254.063 1.00 33.50 ? 26   GLY H C   1 
ATOM   904  O O   . GLY B 2 26  ? 224.203 153.433 253.840 1.00 33.55 ? 26   GLY H O   1 
ATOM   905  N N   . PHE B 2 27  ? 222.258 152.553 253.132 1.00 32.58 ? 27   PHE H N   1 
ATOM   906  C CA  . PHE B 2 27  ? 222.390 153.029 251.765 1.00 32.85 ? 27   PHE H CA  1 
ATOM   907  C C   . PHE B 2 27  ? 221.016 153.137 251.128 1.00 32.90 ? 27   PHE H C   1 
ATOM   908  O O   . PHE B 2 27  ? 220.052 152.553 251.620 1.00 32.84 ? 27   PHE H O   1 
ATOM   909  C CB  . PHE B 2 27  ? 223.291 152.098 250.949 1.00 32.77 ? 27   PHE H CB  1 
ATOM   910  C CG  . PHE B 2 27  ? 222.726 150.730 250.697 1.00 32.26 ? 27   PHE H CG  1 
ATOM   911  C CD1 . PHE B 2 27  ? 222.777 149.753 251.667 1.00 32.68 ? 27   PHE H CD1 1 
ATOM   912  C CD2 . PHE B 2 27  ? 222.173 150.414 249.473 1.00 32.10 ? 27   PHE H CD2 1 
ATOM   913  C CE1 . PHE B 2 27  ? 222.281 148.485 251.422 1.00 32.20 ? 27   PHE H CE1 1 
ATOM   914  C CE2 . PHE B 2 27  ? 221.680 149.150 249.223 1.00 31.69 ? 27   PHE H CE2 1 
ATOM   915  C CZ  . PHE B 2 27  ? 221.736 148.185 250.199 1.00 31.34 ? 27   PHE H CZ  1 
ATOM   916  N N   . SER B 2 28  ? 220.925 153.877 250.035 1.00 32.17 ? 28   SER H N   1 
ATOM   917  C CA  . SER B 2 28  ? 219.663 154.002 249.324 1.00 32.21 ? 28   SER H CA  1 
ATOM   918  C C   . SER B 2 28  ? 219.703 153.302 247.980 1.00 31.90 ? 28   SER H C   1 
ATOM   919  O O   . SER B 2 28  ? 220.746 153.230 247.331 1.00 31.47 ? 28   SER H O   1 
ATOM   920  C CB  . SER B 2 28  ? 219.299 155.457 249.128 1.00 32.53 ? 28   SER H CB  1 
ATOM   921  N N   . VAL B 2 29  ? 218.549 152.812 247.551 1.00 32.44 ? 29   VAL H N   1 
ATOM   922  C CA  . VAL B 2 29  ? 218.440 152.120 246.272 1.00 31.47 ? 29   VAL H CA  1 
ATOM   923  C C   . VAL B 2 29  ? 218.596 153.081 245.100 1.00 31.62 ? 29   VAL H C   1 
ATOM   924  O O   . VAL B 2 29  ? 218.740 152.655 243.955 1.00 31.40 ? 29   VAL H O   1 
ATOM   925  C CB  . VAL B 2 29  ? 217.086 151.394 246.161 1.00 31.83 ? 29   VAL H CB  1 
ATOM   926  C CG1 . VAL B 2 29  ? 216.946 150.393 247.283 1.00 32.76 ? 29   VAL H CG1 1 
ATOM   927  C CG2 . VAL B 2 29  ? 215.942 152.405 246.192 1.00 32.43 ? 29   VAL H CG2 1 
ATOM   928  N N   . ASN B 2 30  ? 218.546 154.377 245.390 1.00 31.89 ? 30   ASN H N   1 
ATOM   929  C CA  . ASN B 2 30  ? 218.630 155.405 244.364 1.00 31.46 ? 30   ASN H CA  1 
ATOM   930  C C   . ASN B 2 30  ? 220.051 155.946 244.221 1.00 31.34 ? 30   ASN H C   1 
ATOM   931  O O   . ASN B 2 30  ? 220.290 156.881 243.458 1.00 31.50 ? 30   ASN H O   1 
ATOM   932  C CB  . ASN B 2 30  ? 217.689 156.541 244.706 1.00 31.75 ? 30   ASN H CB  1 
ATOM   933  C CG  . ASN B 2 30  ? 216.266 156.095 244.837 1.00 32.08 ? 30   ASN H CG  1 
ATOM   934  O OD1 . ASN B 2 30  ? 215.762 155.297 244.040 1.00 31.66 ? 30   ASN H OD1 1 
ATOM   935  N ND2 . ASN B 2 30  ? 215.607 156.593 245.855 1.00 32.29 ? 30   ASN H ND2 1 
ATOM   936  N N   . THR B 2 31  ? 220.985 155.378 244.977 1.00 30.94 ? 31   THR H N   1 
ATOM   937  C CA  . THR B 2 31  ? 222.363 155.858 244.982 1.00 30.19 ? 31   THR H CA  1 
ATOM   938  C C   . THR B 2 31  ? 223.214 155.167 243.924 1.00 29.79 ? 31   THR H C   1 
ATOM   939  O O   . THR B 2 31  ? 223.193 153.944 243.787 1.00 29.94 ? 31   THR H O   1 
ATOM   940  C CB  . THR B 2 31  ? 222.996 155.677 246.373 1.00 29.73 ? 31   THR H CB  1 
ATOM   941  O OG1 . THR B 2 31  ? 222.300 156.496 247.319 1.00 30.57 ? 31   THR H OG1 1 
ATOM   942  C CG2 . THR B 2 31  ? 224.465 156.061 246.361 1.00 29.52 ? 31   THR H CG2 1 
ATOM   943  N N   . GLY B 2 32  ? 223.972 155.958 243.176 1.00 29.29 ? 32   GLY H N   1 
ATOM   944  C CA  . GLY B 2 32  ? 224.806 155.418 242.113 1.00 28.58 ? 32   GLY H CA  1 
ATOM   945  C C   . GLY B 2 32  ? 225.807 154.407 242.654 1.00 28.44 ? 32   GLY H C   1 
ATOM   946  O O   . GLY B 2 32  ? 226.396 154.604 243.716 1.00 28.47 ? 32   GLY H O   1 
ATOM   947  N N   . GLY B 2 33  ? 225.989 153.316 241.919 1.00 28.70 ? 33   GLY H N   1 
ATOM   948  C CA  . GLY B 2 33  ? 226.922 152.267 242.309 1.00 28.30 ? 33   GLY H CA  1 
ATOM   949  C C   . GLY B 2 33  ? 226.257 151.178 243.143 1.00 28.80 ? 33   GLY H C   1 
ATOM   950  O O   . GLY B 2 33  ? 226.868 150.148 243.425 1.00 28.77 ? 33   GLY H O   1 
ATOM   951  N N   . VAL B 2 34  ? 225.012 151.410 243.545 1.00 28.90 ? 34   VAL H N   1 
ATOM   952  C CA  . VAL B 2 34  ? 224.285 150.448 244.362 1.00 28.54 ? 34   VAL H CA  1 
ATOM   953  C C   . VAL B 2 34  ? 223.550 149.400 243.545 1.00 29.04 ? 34   VAL H C   1 
ATOM   954  O O   . VAL B 2 34  ? 222.871 149.713 242.567 1.00 29.23 ? 34   VAL H O   1 
ATOM   955  C CB  . VAL B 2 34  ? 223.275 151.170 245.271 1.00 29.28 ? 34   VAL H CB  1 
ATOM   956  C CG1 . VAL B 2 34  ? 222.376 150.166 245.976 1.00 30.11 ? 34   VAL H CG1 1 
ATOM   957  C CG2 . VAL B 2 34  ? 224.033 151.993 246.294 1.00 29.94 ? 34   VAL H CG2 1 
ATOM   958  N N   . GLY B 2 35  ? 223.649 148.157 243.994 1.00 28.54 ? 35   GLY H N   1 
ATOM   959  C CA  . GLY B 2 35  ? 222.890 147.062 243.414 1.00 28.39 ? 35   GLY H CA  1 
ATOM   960  C C   . GLY B 2 35  ? 222.512 146.074 244.506 1.00 28.67 ? 35   GLY H C   1 
ATOM   961  O O   . GLY B 2 35  ? 223.219 145.942 245.506 1.00 28.54 ? 35   GLY H O   1 
ATOM   962  N N   . VAL B 2 36  ? 221.385 145.397 244.328 1.00 28.96 ? 36   VAL H N   1 
ATOM   963  C CA  . VAL B 2 36  ? 220.947 144.391 245.289 1.00 28.89 ? 36   VAL H CA  1 
ATOM   964  C C   . VAL B 2 36  ? 220.570 143.097 244.588 1.00 29.45 ? 36   VAL H C   1 
ATOM   965  O O   . VAL B 2 36  ? 219.731 143.092 243.685 1.00 29.88 ? 36   VAL H O   1 
ATOM   966  C CB  . VAL B 2 36  ? 219.752 144.905 246.111 1.00 29.29 ? 36   VAL H CB  1 
ATOM   967  C CG1 . VAL B 2 36  ? 219.289 143.835 247.104 1.00 30.07 ? 36   VAL H CG1 1 
ATOM   968  C CG2 . VAL B 2 36  ? 220.153 146.177 246.851 1.00 30.14 ? 36   VAL H CG2 1 
ATOM   969  N N   . GLY B 2 37  ? 221.190 142.000 245.005 1.00 28.98 ? 37   GLY H N   1 
ATOM   970  C CA  . GLY B 2 37  ? 220.936 140.713 244.374 1.00 29.15 ? 37   GLY H CA  1 
ATOM   971  C C   . GLY B 2 37  ? 220.219 139.743 245.293 1.00 29.82 ? 37   GLY H C   1 
ATOM   972  O O   . GLY B 2 37  ? 220.297 139.852 246.517 1.00 29.87 ? 37   GLY H O   1 
ATOM   973  N N   . TRP B 2 38  ? 219.550 138.770 244.684 1.00 29.58 ? 38   TRP H N   1 
ATOM   974  C CA  . TRP B 2 38  ? 218.895 137.689 245.400 1.00 29.89 ? 38   TRP H CA  1 
ATOM   975  C C   . TRP B 2 38  ? 219.553 136.356 245.094 1.00 29.68 ? 38   TRP H C   1 
ATOM   976  O O   . TRP B 2 38  ? 219.821 136.035 243.933 1.00 30.68 ? 38   TRP H O   1 
ATOM   977  C CB  . TRP B 2 38  ? 217.422 137.613 245.023 1.00 30.72 ? 38   TRP H CB  1 
ATOM   978  C CG  . TRP B 2 38  ? 216.596 138.700 245.599 1.00 31.05 ? 38   TRP H CG  1 
ATOM   979  C CD1 . TRP B 2 38  ? 216.333 139.910 245.044 1.00 31.23 ? 38   TRP H CD1 1 
ATOM   980  C CD2 . TRP B 2 38  ? 215.900 138.676 246.863 1.00 30.92 ? 38   TRP H CD2 1 
ATOM   981  N NE1 . TRP B 2 38  ? 215.521 140.637 245.870 1.00 31.28 ? 38   TRP H NE1 1 
ATOM   982  C CE2 . TRP B 2 38  ? 215.244 139.894 246.986 1.00 31.34 ? 38   TRP H CE2 1 
ATOM   983  C CE3 . TRP B 2 38  ? 215.780 137.725 247.884 1.00 31.17 ? 38   TRP H CE3 1 
ATOM   984  C CZ2 . TRP B 2 38  ? 214.471 140.197 248.085 1.00 32.12 ? 38   TRP H CZ2 1 
ATOM   985  C CZ3 . TRP B 2 38  ? 215.008 138.030 248.992 1.00 30.82 ? 38   TRP H CZ3 1 
ATOM   986  C CH2 . TRP B 2 38  ? 214.369 139.235 249.089 1.00 31.96 ? 38   TRP H CH2 1 
ATOM   987  N N   . ILE B 2 39  ? 219.797 135.588 246.149 1.00 30.23 ? 39   ILE H N   1 
ATOM   988  C CA  . ILE B 2 39  ? 220.428 134.275 246.070 1.00 30.28 ? 39   ILE H CA  1 
ATOM   989  C C   . ILE B 2 39  ? 219.642 133.261 246.891 1.00 30.64 ? 39   ILE H C   1 
ATOM   990  O O   . ILE B 2 39  ? 219.161 133.581 247.975 1.00 30.78 ? 39   ILE H O   1 
ATOM   991  C CB  . ILE B 2 39  ? 221.881 134.353 246.580 1.00 29.53 ? 39   ILE H CB  1 
ATOM   992  C CG1 . ILE B 2 39  ? 222.682 135.331 245.705 1.00 29.47 ? 39   ILE H CG1 1 
ATOM   993  C CG2 . ILE B 2 39  ? 222.529 132.970 246.581 1.00 30.14 ? 39   ILE H CG2 1 
ATOM   994  C CD1 . ILE B 2 39  ? 224.018 135.702 246.262 1.00 29.58 ? 39   ILE H CD1 1 
ATOM   995  N N   . ARG B 2 40  ? 219.517 132.038 246.393 1.00 30.56 ? 40   ARG H N   1 
ATOM   996  C CA  . ARG B 2 40  ? 218.829 131.010 247.163 1.00 31.19 ? 40   ARG H CA  1 
ATOM   997  C C   . ARG B 2 40  ? 219.747 129.839 247.470 1.00 30.88 ? 40   ARG H C   1 
ATOM   998  O O   . ARG B 2 40  ? 220.667 129.539 246.711 1.00 30.47 ? 40   ARG H O   1 
ATOM   999  C CB  . ARG B 2 40  ? 217.601 130.496 246.432 1.00 31.48 ? 40   ARG H CB  1 
ATOM   1000 C CG  . ARG B 2 40  ? 217.883 129.673 245.194 1.00 31.03 ? 40   ARG H CG  1 
ATOM   1001 C CD  . ARG B 2 40  ? 216.637 129.114 244.620 1.00 31.05 ? 40   ARG H CD  1 
ATOM   1002 N NE  . ARG B 2 40  ? 216.905 128.270 243.468 1.00 30.41 ? 40   ARG H NE  1 
ATOM   1003 C CZ  . ARG B 2 40  ? 215.973 127.587 242.781 1.00 31.45 ? 40   ARG H CZ  1 
ATOM   1004 N NH1 . ARG B 2 40  ? 214.711 127.650 243.135 1.00 32.29 ? 40   ARG H NH1 1 
ATOM   1005 N NH2 . ARG B 2 40  ? 216.337 126.848 241.751 1.00 31.33 ? 40   ARG H NH2 1 
ATOM   1006 N N   . GLN B 2 41  ? 219.484 129.170 248.582 1.00 31.24 ? 41   GLN H N   1 
ATOM   1007 C CA  . GLN B 2 41  ? 220.260 128.005 248.980 1.00 30.89 ? 41   GLN H CA  1 
ATOM   1008 C C   . GLN B 2 41  ? 219.381 126.898 249.548 1.00 31.51 ? 41   GLN H C   1 
ATOM   1009 O O   . GLN B 2 41  ? 218.971 126.976 250.706 1.00 31.62 ? 41   GLN H O   1 
ATOM   1010 C CB  . GLN B 2 41  ? 221.292 128.400 250.030 1.00 30.68 ? 41   GLN H CB  1 
ATOM   1011 C CG  . GLN B 2 41  ? 222.149 127.259 250.493 1.00 30.62 ? 41   GLN H CG  1 
ATOM   1012 C CD  . GLN B 2 41  ? 223.197 127.694 251.469 1.00 30.54 ? 41   GLN H CD  1 
ATOM   1013 O OE1 . GLN B 2 41  ? 223.010 128.650 252.237 1.00 31.20 ? 41   GLN H OE1 1 
ATOM   1014 N NE2 . GLN B 2 41  ? 224.323 126.996 251.452 1.00 30.85 ? 41   GLN H NE2 1 
ATOM   1015 N N   . PRO B 2 42  ? 219.062 125.876 248.752 1.00 31.68 ? 42   PRO H N   1 
ATOM   1016 C CA  . PRO B 2 42  ? 218.327 124.692 249.147 1.00 31.97 ? 42   PRO H CA  1 
ATOM   1017 C C   . PRO B 2 42  ? 219.108 124.009 250.266 1.00 31.92 ? 42   PRO H C   1 
ATOM   1018 O O   . PRO B 2 42  ? 220.331 124.139 250.315 1.00 31.61 ? 42   PRO H O   1 
ATOM   1019 C CB  . PRO B 2 42  ? 218.298 123.865 247.857 1.00 31.95 ? 42   PRO H CB  1 
ATOM   1020 C CG  . PRO B 2 42  ? 218.503 124.880 246.745 1.00 32.05 ? 42   PRO H CG  1 
ATOM   1021 C CD  . PRO B 2 42  ? 219.419 125.932 247.341 1.00 31.72 ? 42   PRO H CD  1 
ATOM   1022 N N   . PRO B 2 43  ? 218.441 123.317 251.190 1.00 31.83 ? 43   PRO H N   1 
ATOM   1023 C CA  . PRO B 2 43  ? 219.043 122.616 252.307 1.00 31.37 ? 43   PRO H CA  1 
ATOM   1024 C C   . PRO B 2 43  ? 220.128 121.653 251.846 1.00 32.07 ? 43   PRO H C   1 
ATOM   1025 O O   . PRO B 2 43  ? 219.866 120.739 251.065 1.00 32.44 ? 43   PRO H O   1 
ATOM   1026 C CB  . PRO B 2 43  ? 217.844 121.858 252.891 1.00 31.81 ? 43   PRO H CB  1 
ATOM   1027 C CG  . PRO B 2 43  ? 216.646 122.703 252.520 1.00 31.69 ? 43   PRO H CG  1 
ATOM   1028 C CD  . PRO B 2 43  ? 216.975 123.261 251.150 1.00 32.21 ? 43   PRO H CD  1 
ATOM   1029 N N   . GLY B 2 44  ? 221.341 121.842 252.358 1.00 31.62 ? 44   GLY H N   1 
ATOM   1030 C CA  . GLY B 2 44  ? 222.455 120.946 252.061 1.00 31.69 ? 44   GLY H CA  1 
ATOM   1031 C C   . GLY B 2 44  ? 223.074 121.188 250.685 1.00 31.27 ? 44   GLY H C   1 
ATOM   1032 O O   . GLY B 2 44  ? 223.939 120.427 250.251 1.00 31.69 ? 44   GLY H O   1 
ATOM   1033 N N   . LYS B 2 45  ? 222.655 122.261 250.029 1.00 30.71 ? 45   LYS H N   1 
ATOM   1034 C CA  . LYS B 2 45  ? 223.148 122.455 248.656 1.00 31.26 ? 45   LYS H CA  1 
ATOM   1035 C C   . LYS B 2 45  ? 223.933 123.753 248.532 1.00 31.02 ? 45   LYS H C   1 
ATOM   1036 O O   . LYS B 2 45  ? 224.054 124.478 249.535 1.00 31.01 ? 45   LYS H O   1 
ATOM   1037 C CB  . LYS B 2 45  ? 221.977 122.362 247.678 1.00 31.88 ? 45   LYS H CB  1 
ATOM   1038 C CG  . LYS B 2 45  ? 221.457 120.956 247.417 1.00 32.11 ? 45   LYS H CG  1 
ATOM   1039 C CD  . LYS B 2 45  ? 222.443 120.101 246.653 1.00 32.65 ? 45   LYS H CD  1 
ATOM   1040 C CE  . LYS B 2 45  ? 221.864 118.774 246.212 1.00 32.96 ? 45   LYS H CE  1 
ATOM   1041 N NZ  . LYS B 2 45  ? 222.829 118.002 245.394 1.00 35.85 ? 45   LYS H NZ  1 
ATOM   1042 N N   . ALA B 2 46  ? 224.454 124.012 247.343 1.00 30.07 ? 46   ALA H N   1 
ATOM   1043 C CA  . ALA B 2 46  ? 225.227 125.208 247.038 1.00 30.17 ? 46   ALA H CA  1 
ATOM   1044 C C   . ALA B 2 46  ? 224.326 126.393 246.733 1.00 30.40 ? 46   ALA H C   1 
ATOM   1045 O O   . ALA B 2 46  ? 223.138 126.230 246.456 1.00 30.84 ? 46   ALA H O   1 
ATOM   1046 C CB  . ALA B 2 46  ? 226.149 124.949 245.862 1.00 30.84 ? 46   ALA H CB  1 
ATOM   1047 N N   . LEU B 2 47  ? 224.908 127.583 246.777 1.00 29.89 ? 47   LEU H N   1 
ATOM   1048 C CA  . LEU B 2 47  ? 224.190 128.819 246.506 1.00 29.59 ? 47   LEU H CA  1 
ATOM   1049 C C   . LEU B 2 47  ? 223.876 128.967 245.025 1.00 29.76 ? 47   LEU H C   1 
ATOM   1050 O O   . LEU B 2 47  ? 224.708 128.657 244.173 1.00 30.27 ? 47   LEU H O   1 
ATOM   1051 C CB  . LEU B 2 47  ? 225.043 130.014 246.940 1.00 29.16 ? 47   LEU H CB  1 
ATOM   1052 C CG  . LEU B 2 47  ? 224.987 130.403 248.418 1.00 29.48 ? 47   LEU H CG  1 
ATOM   1053 C CD1 . LEU B 2 47  ? 225.527 129.270 249.280 1.00 30.50 ? 47   LEU H CD1 1 
ATOM   1054 C CD2 . LEU B 2 47  ? 225.813 131.653 248.614 1.00 29.99 ? 47   LEU H CD2 1 
ATOM   1055 N N   . GLU B 2 48  ? 222.692 129.482 244.722 1.00 29.47 ? 48   GLU H N   1 
ATOM   1056 C CA  . GLU B 2 48  ? 222.314 129.779 243.347 1.00 29.77 ? 48   GLU H CA  1 
ATOM   1057 C C   . GLU B 2 48  ? 221.854 131.221 243.202 1.00 29.92 ? 48   GLU H C   1 
ATOM   1058 O O   . GLU B 2 48  ? 220.939 131.665 243.895 1.00 29.91 ? 48   GLU H O   1 
ATOM   1059 C CB  . GLU B 2 48  ? 221.201 128.838 242.886 1.00 30.35 ? 48   GLU H CB  1 
ATOM   1060 C CG  . GLU B 2 48  ? 220.760 129.046 241.448 1.00 29.67 ? 48   GLU H CG  1 
ATOM   1061 C CD  . GLU B 2 48  ? 219.702 128.081 241.022 1.00 29.55 ? 48   GLU H CD  1 
ATOM   1062 O OE1 . GLU B 2 48  ? 219.218 127.351 241.853 1.00 29.21 ? 48   GLU H OE1 1 
ATOM   1063 O OE2 . GLU B 2 48  ? 219.376 128.066 239.862 1.00 29.59 ? 48   GLU H OE2 1 
ATOM   1064 N N   . TRP B 2 49  ? 222.485 131.956 242.295 1.00 29.14 ? 49   TRP H N   1 
ATOM   1065 C CA  . TRP B 2 49  ? 222.105 133.342 242.061 1.00 29.37 ? 49   TRP H CA  1 
ATOM   1066 C C   . TRP B 2 49  ? 220.854 133.425 241.205 1.00 29.60 ? 49   TRP H C   1 
ATOM   1067 O O   . TRP B 2 49  ? 220.726 132.710 240.211 1.00 30.23 ? 49   TRP H O   1 
ATOM   1068 C CB  . TRP B 2 49  ? 223.247 134.094 241.396 1.00 28.89 ? 49   TRP H CB  1 
ATOM   1069 C CG  . TRP B 2 49  ? 222.909 135.491 241.027 1.00 29.26 ? 49   TRP H CG  1 
ATOM   1070 C CD1 . TRP B 2 49  ? 222.912 136.572 241.847 1.00 29.55 ? 49   TRP H CD1 1 
ATOM   1071 C CD2 . TRP B 2 49  ? 222.536 135.979 239.723 1.00 29.79 ? 49   TRP H CD2 1 
ATOM   1072 N NE1 . TRP B 2 49  ? 222.566 137.692 241.148 1.00 29.77 ? 49   TRP H NE1 1 
ATOM   1073 C CE2 . TRP B 2 49  ? 222.339 137.348 239.844 1.00 29.64 ? 49   TRP H CE2 1 
ATOM   1074 C CE3 . TRP B 2 49  ? 222.364 135.372 238.480 1.00 30.45 ? 49   TRP H CE3 1 
ATOM   1075 C CZ2 . TRP B 2 49  ? 221.983 138.129 238.767 1.00 30.45 ? 49   TRP H CZ2 1 
ATOM   1076 C CZ3 . TRP B 2 49  ? 222.011 136.155 237.401 1.00 30.88 ? 49   TRP H CZ3 1 
ATOM   1077 C CH2 . TRP B 2 49  ? 221.827 137.496 237.541 1.00 30.72 ? 49   TRP H CH2 1 
ATOM   1078 N N   . LEU B 2 50  ? 219.930 134.300 241.590 1.00 29.74 ? 50   LEU H N   1 
ATOM   1079 C CA  . LEU B 2 50  ? 218.676 134.444 240.869 1.00 30.04 ? 50   LEU H CA  1 
ATOM   1080 C C   . LEU B 2 50  ? 218.656 135.689 239.996 1.00 29.60 ? 50   LEU H C   1 
ATOM   1081 O O   . LEU B 2 50  ? 218.444 135.604 238.785 1.00 31.51 ? 50   LEU H O   1 
ATOM   1082 C CB  . LEU B 2 50  ? 217.519 134.522 241.868 1.00 29.41 ? 50   LEU H CB  1 
ATOM   1083 C CG  . LEU B 2 50  ? 217.369 133.330 242.814 1.00 30.32 ? 50   LEU H CG  1 
ATOM   1084 C CD1 . LEU B 2 50  ? 216.265 133.622 243.803 1.00 31.39 ? 50   LEU H CD1 1 
ATOM   1085 C CD2 . LEU B 2 50  ? 217.058 132.084 242.021 1.00 30.57 ? 50   LEU H CD2 1 
ATOM   1086 N N   . ALA B 2 51  ? 218.823 136.850 240.623 1.00 30.23 ? 51   ALA H N   1 
ATOM   1087 C CA  . ALA B 2 51  ? 218.713 138.115 239.905 1.00 30.35 ? 51   ALA H CA  1 
ATOM   1088 C C   . ALA B 2 51  ? 219.267 139.271 240.725 1.00 30.14 ? 51   ALA H C   1 
ATOM   1089 O O   . ALA B 2 51  ? 219.324 139.195 241.951 1.00 30.10 ? 51   ALA H O   1 
ATOM   1090 C CB  . ALA B 2 51  ? 217.260 138.383 239.552 1.00 30.91 ? 51   ALA H CB  1 
ATOM   1091 N N   . LEU B 2 52  ? 219.625 140.366 240.058 1.00 30.19 ? 52   LEU H N   1 
ATOM   1092 C CA  . LEU B 2 52  ? 219.958 141.597 240.775 1.00 29.76 ? 52   LEU H CA  1 
ATOM   1093 C C   . LEU B 2 52  ? 219.476 142.834 240.033 1.00 30.01 ? 52   LEU H C   1 
ATOM   1094 O O   . LEU B 2 52  ? 219.396 142.850 238.803 1.00 30.01 ? 52   LEU H O   1 
ATOM   1095 C CB  . LEU B 2 52  ? 221.468 141.696 241.066 1.00 29.52 ? 52   LEU H CB  1 
ATOM   1096 C CG  . LEU B 2 52  ? 222.409 141.947 239.891 1.00 29.22 ? 52   LEU H CG  1 
ATOM   1097 C CD1 . LEU B 2 52  ? 222.685 143.446 239.756 1.00 29.27 ? 52   LEU H CD1 1 
ATOM   1098 C CD2 . LEU B 2 52  ? 223.708 141.188 240.132 1.00 29.72 ? 52   LEU H CD2 1 
ATOM   1099 N N   . ILE B 2 53  ? 219.159 143.874 240.798 1.00 29.95 ? 53   ILE H N   1 
ATOM   1100 C CA  . ILE B 2 53  ? 218.714 145.143 240.235 1.00 29.90 ? 53   ILE H CA  1 
ATOM   1101 C C   . ILE B 2 53  ? 219.692 146.270 240.543 1.00 29.78 ? 53   ILE H C   1 
ATOM   1102 O O   . ILE B 2 53  ? 220.212 146.374 241.655 1.00 29.56 ? 53   ILE H O   1 
ATOM   1103 C CB  . ILE B 2 53  ? 217.308 145.502 240.753 1.00 30.05 ? 53   ILE H CB  1 
ATOM   1104 C CG1 . ILE B 2 53  ? 216.791 146.771 240.060 1.00 30.53 ? 53   ILE H CG1 1 
ATOM   1105 C CG2 . ILE B 2 53  ? 217.332 145.685 242.272 1.00 31.25 ? 53   ILE H CG2 1 
ATOM   1106 C CD1 . ILE B 2 53  ? 215.292 146.966 240.187 1.00 31.31 ? 53   ILE H CD1 1 
ATOM   1107 N N   . TYR B 2 54  ? 219.939 147.108 239.544 1.00 29.70 ? 54   TYR H N   1 
ATOM   1108 C CA  . TYR B 2 54  ? 220.828 148.255 239.679 1.00 29.52 ? 54   TYR H CA  1 
ATOM   1109 C C   . TYR B 2 54  ? 220.058 149.515 240.051 1.00 28.84 ? 54   TYR H C   1 
ATOM   1110 O O   . TYR B 2 54  ? 218.863 149.630 239.785 1.00 30.49 ? 54   TYR H O   1 
ATOM   1111 C CB  . TYR B 2 54  ? 221.592 148.504 238.381 1.00 29.41 ? 54   TYR H CB  1 
ATOM   1112 C CG  . TYR B 2 54  ? 222.636 147.477 238.034 1.00 29.57 ? 54   TYR H CG  1 
ATOM   1113 C CD1 . TYR B 2 54  ? 222.370 146.523 237.070 1.00 29.20 ? 54   TYR H CD1 1 
ATOM   1114 C CD2 . TYR B 2 54  ? 223.866 147.500 238.662 1.00 29.23 ? 54   TYR H CD2 1 
ATOM   1115 C CE1 . TYR B 2 54  ? 223.331 145.603 236.728 1.00 29.24 ? 54   TYR H CE1 1 
ATOM   1116 C CE2 . TYR B 2 54  ? 224.825 146.574 238.321 1.00 28.71 ? 54   TYR H CE2 1 
ATOM   1117 C CZ  . TYR B 2 54  ? 224.562 145.634 237.359 1.00 29.21 ? 54   TYR H CZ  1 
ATOM   1118 O OH  . TYR B 2 54  ? 225.522 144.719 237.018 1.00 30.43 ? 54   TYR H OH  1 
ATOM   1119 N N   . TRP B 2 55  ? 220.768 150.486 240.614 1.00 29.93 ? 55   TRP H N   1 
ATOM   1120 C CA  . TRP B 2 55  ? 220.203 151.791 240.956 1.00 29.85 ? 55   TRP H CA  1 
ATOM   1121 C C   . TRP B 2 55  ? 219.496 152.453 239.774 1.00 29.80 ? 55   TRP H C   1 
ATOM   1122 O O   . TRP B 2 55  ? 218.628 153.307 239.958 1.00 29.95 ? 55   TRP H O   1 
ATOM   1123 C CB  . TRP B 2 55  ? 221.316 152.730 241.423 1.00 30.06 ? 55   TRP H CB  1 
ATOM   1124 C CG  . TRP B 2 55  ? 222.186 153.229 240.293 1.00 29.39 ? 55   TRP H CG  1 
ATOM   1125 C CD1 . TRP B 2 55  ? 222.006 154.378 239.581 1.00 29.63 ? 55   TRP H CD1 1 
ATOM   1126 C CD2 . TRP B 2 55  ? 223.356 152.590 239.727 1.00 29.37 ? 55   TRP H CD2 1 
ATOM   1127 N NE1 . TRP B 2 55  ? 222.983 154.499 238.623 1.00 28.89 ? 55   TRP H NE1 1 
ATOM   1128 C CE2 . TRP B 2 55  ? 223.813 153.413 238.696 1.00 28.69 ? 55   TRP H CE2 1 
ATOM   1129 C CE3 . TRP B 2 55  ? 224.038 151.408 240.004 1.00 29.23 ? 55   TRP H CE3 1 
ATOM   1130 C CZ2 . TRP B 2 55  ? 224.925 153.086 237.939 1.00 27.86 ? 55   TRP H CZ2 1 
ATOM   1131 C CZ3 . TRP B 2 55  ? 225.148 151.083 239.249 1.00 28.86 ? 55   TRP H CZ3 1 
ATOM   1132 C CH2 . TRP B 2 55  ? 225.582 151.898 238.243 1.00 28.12 ? 55   TRP H CH2 1 
ATOM   1133 N N   . ASN B 2 56  ? 219.888 152.077 238.558 1.00 29.74 ? 56   ASN H N   1 
ATOM   1134 C CA  . ASN B 2 56  ? 219.345 152.679 237.346 1.00 29.67 ? 56   ASN H CA  1 
ATOM   1135 C C   . ASN B 2 56  ? 218.264 151.819 236.702 1.00 29.89 ? 56   ASN H C   1 
ATOM   1136 O O   . ASN B 2 56  ? 217.928 152.007 235.533 1.00 30.21 ? 56   ASN H O   1 
ATOM   1137 C CB  . ASN B 2 56  ? 220.459 152.964 236.361 1.00 29.14 ? 56   ASN H CB  1 
ATOM   1138 C CG  . ASN B 2 56  ? 221.151 151.721 235.899 1.00 29.89 ? 56   ASN H CG  1 
ATOM   1139 O OD1 . ASN B 2 56  ? 220.744 150.599 236.230 1.00 29.66 ? 56   ASN H OD1 1 
ATOM   1140 N ND2 . ASN B 2 56  ? 222.205 151.895 235.141 1.00 29.21 ? 56   ASN H ND2 1 
ATOM   1141 N N   . ASP B 2 57  ? 217.722 150.882 237.475 1.00 29.73 ? 57   ASP H N   1 
ATOM   1142 C CA  . ASP B 2 57  ? 216.630 150.008 237.052 1.00 29.87 ? 57   ASP H CA  1 
ATOM   1143 C C   . ASP B 2 57  ? 217.026 149.012 235.969 1.00 29.72 ? 57   ASP H C   1 
ATOM   1144 O O   . ASP B 2 57  ? 216.176 148.284 235.450 1.00 29.81 ? 57   ASP H O   1 
ATOM   1145 C CB  . ASP B 2 57  ? 215.418 150.830 236.594 1.00 29.89 ? 57   ASP H CB  1 
ATOM   1146 C CG  . ASP B 2 57  ? 214.650 151.449 237.756 1.00 30.11 ? 57   ASP H CG  1 
ATOM   1147 O OD1 . ASP B 2 57  ? 214.133 150.707 238.559 1.00 30.07 ? 57   ASP H OD1 1 
ATOM   1148 O OD2 . ASP B 2 57  ? 214.604 152.652 237.848 1.00 29.58 ? 57   ASP H OD2 1 
ATOM   1149 N N   . ASP B 2 58  ? 218.320 148.909 235.683 1.00 29.40 ? 58   ASP H N   1 
ATOM   1150 C CA  . ASP B 2 58  ? 218.780 147.826 234.828 1.00 29.23 ? 58   ASP H CA  1 
ATOM   1151 C C   . ASP B 2 58  ? 218.735 146.543 235.641 1.00 28.95 ? 58   ASP H C   1 
ATOM   1152 O O   . ASP B 2 58  ? 218.825 146.584 236.869 1.00 31.38 ? 58   ASP H O   1 
ATOM   1153 C CB  . ASP B 2 58  ? 220.187 148.088 234.293 1.00 29.58 ? 58   ASP H CB  1 
ATOM   1154 N N   . LYS B 2 59  ? 218.542 145.412 234.976 1.00 29.07 ? 59   LYS H N   1 
ATOM   1155 C CA  . LYS B 2 59  ? 218.348 144.164 235.708 1.00 29.66 ? 59   LYS H CA  1 
ATOM   1156 C C   . LYS B 2 59  ? 219.025 142.968 235.059 1.00 30.53 ? 59   LYS H C   1 
ATOM   1157 O O   . LYS B 2 59  ? 219.036 142.830 233.836 1.00 32.44 ? 59   LYS H O   1 
ATOM   1158 C CB  . LYS B 2 59  ? 216.854 143.889 235.869 1.00 30.20 ? 59   LYS H CB  1 
ATOM   1159 C CG  . LYS B 2 59  ? 216.112 144.954 236.676 1.00 30.80 ? 59   LYS H CG  1 
ATOM   1160 C CD  . LYS B 2 59  ? 214.622 144.697 236.738 1.00 31.25 ? 59   LYS H CD  1 
ATOM   1161 C CE  . LYS B 2 59  ? 213.900 145.179 235.479 1.00 29.98 ? 59   LYS H CE  1 
ATOM   1162 N NZ  . LYS B 2 59  ? 213.748 146.665 235.454 1.00 30.31 ? 59   LYS H NZ  1 
ATOM   1163 N N   . LEU B 2 60  ? 219.544 142.080 235.899 1.00 30.01 ? 60   LEU H N   1 
ATOM   1164 C CA  . LEU B 2 60  ? 220.150 140.839 235.443 1.00 30.41 ? 60   LEU H CA  1 
ATOM   1165 C C   . LEU B 2 60  ? 219.411 139.642 236.020 1.00 30.49 ? 60   LEU H C   1 
ATOM   1166 O O   . LEU B 2 60  ? 219.072 139.628 237.203 1.00 31.71 ? 60   LEU H O   1 
ATOM   1167 C CB  . LEU B 2 60  ? 221.617 140.781 235.878 1.00 29.90 ? 60   LEU H CB  1 
ATOM   1168 C CG  . LEU B 2 60  ? 222.503 141.953 235.452 1.00 29.68 ? 60   LEU H CG  1 
ATOM   1169 C CD1 . LEU B 2 60  ? 223.859 141.808 236.121 1.00 29.92 ? 60   LEU H CD1 1 
ATOM   1170 C CD2 . LEU B 2 60  ? 222.645 141.970 233.941 1.00 30.38 ? 60   LEU H CD2 1 
ATOM   1171 N N   . TYR B 2 61  ? 219.191 138.624 235.193 1.00 31.21 ? 61   TYR H N   1 
ATOM   1172 C CA  . TYR B 2 61  ? 218.533 137.399 235.637 1.00 31.19 ? 61   TYR H CA  1 
ATOM   1173 C C   . TYR B 2 61  ? 219.305 136.164 235.207 1.00 31.65 ? 61   TYR H C   1 
ATOM   1174 O O   . TYR B 2 61  ? 219.921 136.152 234.142 1.00 32.71 ? 61   TYR H O   1 
ATOM   1175 C CB  . TYR B 2 61  ? 217.120 137.312 235.068 1.00 31.51 ? 61   TYR H CB  1 
ATOM   1176 C CG  . TYR B 2 61  ? 216.200 138.404 235.509 1.00 31.33 ? 61   TYR H CG  1 
ATOM   1177 C CD1 . TYR B 2 61  ? 216.150 139.596 234.812 1.00 31.71 ? 61   TYR H CD1 1 
ATOM   1178 C CD2 . TYR B 2 61  ? 215.390 138.208 236.604 1.00 31.71 ? 61   TYR H CD2 1 
ATOM   1179 C CE1 . TYR B 2 61  ? 215.287 140.588 235.215 1.00 31.67 ? 61   TYR H CE1 1 
ATOM   1180 C CE2 . TYR B 2 61  ? 214.530 139.195 237.008 1.00 31.88 ? 61   TYR H CE2 1 
ATOM   1181 C CZ  . TYR B 2 61  ? 214.475 140.381 236.319 1.00 31.67 ? 61   TYR H CZ  1 
ATOM   1182 O OH  . TYR B 2 61  ? 213.610 141.363 236.723 1.00 31.97 ? 61   TYR H OH  1 
ATOM   1183 N N   . SER B 2 62  ? 219.218 135.103 236.004 1.00 31.40 ? 62   SER H N   1 
ATOM   1184 C CA  . SER B 2 62  ? 219.761 133.810 235.611 1.00 31.71 ? 62   SER H CA  1 
ATOM   1185 C C   . SER B 2 62  ? 218.927 133.232 234.464 1.00 31.63 ? 62   SER H C   1 
ATOM   1186 O O   . SER B 2 62  ? 217.724 133.029 234.633 1.00 32.58 ? 62   SER H O   1 
ATOM   1187 C CB  . SER B 2 62  ? 219.741 132.855 236.787 1.00 31.57 ? 62   SER H CB  1 
ATOM   1188 O OG  . SER B 2 62  ? 220.166 131.580 236.395 1.00 32.40 ? 62   SER H OG  1 
ATOM   1189 N N   . PRO B 2 63  ? 219.533 132.949 233.303 1.00 31.85 ? 63   PRO H N   1 
ATOM   1190 C CA  . PRO B 2 63  ? 218.901 132.463 232.086 1.00 32.10 ? 63   PRO H CA  1 
ATOM   1191 C C   . PRO B 2 63  ? 217.964 131.278 232.309 1.00 32.63 ? 63   PRO H C   1 
ATOM   1192 O O   . PRO B 2 63  ? 216.927 131.176 231.655 1.00 33.15 ? 63   PRO H O   1 
ATOM   1193 C CB  . PRO B 2 63  ? 220.114 132.041 231.251 1.00 33.08 ? 63   PRO H CB  1 
ATOM   1194 C CG  . PRO B 2 63  ? 221.210 132.974 231.690 1.00 32.62 ? 63   PRO H CG  1 
ATOM   1195 C CD  . PRO B 2 63  ? 220.984 133.169 233.175 1.00 31.36 ? 63   PRO H CD  1 
ATOM   1196 N N   . SER B 2 64  ? 218.320 130.388 233.232 1.00 32.38 ? 64   SER H N   1 
ATOM   1197 C CA  . SER B 2 64  ? 217.517 129.195 233.479 1.00 32.67 ? 64   SER H CA  1 
ATOM   1198 C C   . SER B 2 64  ? 216.257 129.478 234.293 1.00 32.80 ? 64   SER H C   1 
ATOM   1199 O O   . SER B 2 64  ? 215.332 128.666 234.317 1.00 33.38 ? 64   SER H O   1 
ATOM   1200 C CB  . SER B 2 64  ? 218.353 128.152 234.192 1.00 31.86 ? 64   SER H CB  1 
ATOM   1201 N N   . LEU B 2 65  ? 216.231 130.614 234.981 1.00 32.59 ? 65   LEU H N   1 
ATOM   1202 C CA  . LEU B 2 65  ? 215.100 130.963 235.830 1.00 32.56 ? 65   LEU H CA  1 
ATOM   1203 C C   . LEU B 2 65  ? 214.420 132.247 235.382 1.00 33.04 ? 65   LEU H C   1 
ATOM   1204 O O   . LEU B 2 65  ? 213.368 132.609 235.904 1.00 32.99 ? 65   LEU H O   1 
ATOM   1205 C CB  . LEU B 2 65  ? 215.558 131.108 237.284 1.00 32.03 ? 65   LEU H CB  1 
ATOM   1206 C CG  . LEU B 2 65  ? 216.155 129.851 237.933 1.00 32.23 ? 65   LEU H CG  1 
ATOM   1207 C CD1 . LEU B 2 65  ? 216.710 130.214 239.287 1.00 32.27 ? 65   LEU H CD1 1 
ATOM   1208 C CD2 . LEU B 2 65  ? 215.082 128.789 238.079 1.00 32.45 ? 65   LEU H CD2 1 
ATOM   1209 N N   . LYS B 2 66  ? 215.027 132.938 234.425 1.00 32.23 ? 66   LYS H N   1 
ATOM   1210 C CA  . LYS B 2 66  ? 214.560 134.252 233.998 1.00 33.14 ? 66   LYS H CA  1 
ATOM   1211 C C   . LYS B 2 66  ? 213.058 134.299 233.742 1.00 33.50 ? 66   LYS H C   1 
ATOM   1212 O O   . LYS B 2 66  ? 212.397 135.278 234.085 1.00 33.51 ? 66   LYS H O   1 
ATOM   1213 C CB  . LYS B 2 66  ? 215.310 134.690 232.739 1.00 32.65 ? 66   LYS H CB  1 
ATOM   1214 C CG  . LYS B 2 66  ? 214.916 136.063 232.211 1.00 33.30 ? 66   LYS H CG  1 
ATOM   1215 C CD  . LYS B 2 66  ? 215.775 136.462 231.020 1.00 33.85 ? 66   LYS H CD  1 
ATOM   1216 C CE  . LYS B 2 66  ? 215.360 137.817 230.466 1.00 34.72 ? 66   LYS H CE  1 
ATOM   1217 N NZ  . LYS B 2 66  ? 216.182 138.212 229.289 1.00 36.19 ? 66   LYS H NZ  1 
ATOM   1218 N N   . SER B 2 67  ? 212.516 133.250 233.136 1.00 33.69 ? 67   SER H N   1 
ATOM   1219 C CA  . SER B 2 67  ? 211.111 133.234 232.738 1.00 33.91 ? 67   SER H CA  1 
ATOM   1220 C C   . SER B 2 67  ? 210.146 133.294 233.922 1.00 33.25 ? 67   SER H C   1 
ATOM   1221 O O   . SER B 2 67  ? 208.958 133.564 233.743 1.00 33.32 ? 67   SER H O   1 
ATOM   1222 C CB  . SER B 2 67  ? 210.823 131.993 231.919 1.00 33.05 ? 67   SER H CB  1 
ATOM   1223 N N   . ARG B 2 68  ? 210.644 133.022 235.124 1.00 33.53 ? 68   ARG H N   1 
ATOM   1224 C CA  . ARG B 2 68  ? 209.794 133.013 236.308 1.00 34.10 ? 68   ARG H CA  1 
ATOM   1225 C C   . ARG B 2 68  ? 210.137 134.134 237.287 1.00 34.60 ? 68   ARG H C   1 
ATOM   1226 O O   . ARG B 2 68  ? 209.554 134.210 238.371 1.00 34.49 ? 68   ARG H O   1 
ATOM   1227 C CB  . ARG B 2 68  ? 209.911 131.680 237.038 1.00 34.58 ? 68   ARG H CB  1 
ATOM   1228 C CG  . ARG B 2 68  ? 209.424 130.467 236.257 1.00 34.68 ? 68   ARG H CG  1 
ATOM   1229 C CD  . ARG B 2 68  ? 209.301 129.256 237.126 1.00 35.42 ? 68   ARG H CD  1 
ATOM   1230 N NE  . ARG B 2 68  ? 210.590 128.811 237.637 1.00 34.41 ? 68   ARG H NE  1 
ATOM   1231 C CZ  . ARG B 2 68  ? 210.762 127.997 238.705 1.00 34.60 ? 68   ARG H CZ  1 
ATOM   1232 N NH1 . ARG B 2 68  ? 209.728 127.532 239.372 1.00 35.60 ? 68   ARG H NH1 1 
ATOM   1233 N NH2 . ARG B 2 68  ? 211.982 127.660 239.088 1.00 33.28 ? 68   ARG H NH2 1 
ATOM   1234 N N   . LEU B 2 69  ? 211.104 134.983 236.935 1.00 34.36 ? 69   LEU H N   1 
ATOM   1235 C CA  . LEU B 2 69  ? 211.595 135.982 237.886 1.00 33.42 ? 69   LEU H CA  1 
ATOM   1236 C C   . LEU B 2 69  ? 211.343 137.422 237.449 1.00 32.94 ? 69   LEU H C   1 
ATOM   1237 O O   . LEU B 2 69  ? 211.684 137.816 236.334 1.00 33.12 ? 69   LEU H O   1 
ATOM   1238 C CB  . LEU B 2 69  ? 213.104 135.804 238.098 1.00 32.51 ? 69   LEU H CB  1 
ATOM   1239 C CG  . LEU B 2 69  ? 213.578 134.436 238.615 1.00 33.02 ? 69   LEU H CG  1 
ATOM   1240 C CD1 . LEU B 2 69  ? 215.098 134.415 238.609 1.00 32.46 ? 69   LEU H CD1 1 
ATOM   1241 C CD2 . LEU B 2 69  ? 213.044 134.187 240.013 1.00 34.28 ? 69   LEU H CD2 1 
ATOM   1242 N N   . THR B 2 70  ? 210.805 138.219 238.368 1.00 32.72 ? 70   THR H N   1 
ATOM   1243 C CA  . THR B 2 70  ? 210.652 139.659 238.171 1.00 31.94 ? 70   THR H CA  1 
ATOM   1244 C C   . THR B 2 70  ? 211.196 140.428 239.374 1.00 32.23 ? 70   THR H C   1 
ATOM   1245 O O   . THR B 2 70  ? 210.888 140.101 240.520 1.00 32.39 ? 70   THR H O   1 
ATOM   1246 C CB  . THR B 2 70  ? 209.178 140.038 237.930 1.00 32.39 ? 70   THR H CB  1 
ATOM   1247 N N   . VAL B 2 71  ? 212.009 141.448 239.117 1.00 31.81 ? 71   VAL H N   1 
ATOM   1248 C CA  . VAL B 2 71  ? 212.575 142.253 240.197 1.00 31.92 ? 71   VAL H CA  1 
ATOM   1249 C C   . VAL B 2 71  ? 212.283 143.737 240.019 1.00 32.45 ? 71   VAL H C   1 
ATOM   1250 O O   . VAL B 2 71  ? 212.505 144.299 238.947 1.00 32.66 ? 71   VAL H O   1 
ATOM   1251 C CB  . VAL B 2 71  ? 214.099 142.041 240.298 1.00 31.38 ? 71   VAL H CB  1 
ATOM   1252 C CG1 . VAL B 2 71  ? 214.686 142.922 241.395 1.00 31.45 ? 71   VAL H CG1 1 
ATOM   1253 C CG2 . VAL B 2 71  ? 214.386 140.593 240.602 1.00 32.41 ? 71   VAL H CG2 1 
ATOM   1254 N N   . THR B 2 72  ? 211.790 144.365 241.079 1.00 31.70 ? 72   THR H N   1 
ATOM   1255 C CA  . THR B 2 72  ? 211.523 145.799 241.080 1.00 31.28 ? 72   THR H CA  1 
ATOM   1256 C C   . THR B 2 72  ? 212.054 146.428 242.360 1.00 32.13 ? 72   THR H C   1 
ATOM   1257 O O   . THR B 2 72  ? 212.363 145.721 243.319 1.00 32.03 ? 72   THR H O   1 
ATOM   1258 C CB  . THR B 2 72  ? 210.015 146.086 240.948 1.00 32.87 ? 72   THR H CB  1 
ATOM   1259 N N   . LYS B 2 73  ? 212.134 147.755 242.395 1.00 32.12 ? 73   LYS H N   1 
ATOM   1260 C CA  . LYS B 2 73  ? 212.552 148.434 243.617 1.00 32.46 ? 73   LYS H CA  1 
ATOM   1261 C C   . LYS B 2 73  ? 211.634 149.594 243.974 1.00 33.06 ? 73   LYS H C   1 
ATOM   1262 O O   . LYS B 2 73  ? 211.170 150.331 243.104 1.00 33.96 ? 73   LYS H O   1 
ATOM   1263 C CB  . LYS B 2 73  ? 213.999 148.922 243.507 1.00 32.22 ? 73   LYS H CB  1 
ATOM   1264 C CG  . LYS B 2 73  ? 214.269 149.907 242.371 1.00 31.69 ? 73   LYS H CG  1 
ATOM   1265 C CD  . LYS B 2 73  ? 215.737 150.331 242.355 1.00 31.05 ? 73   LYS H CD  1 
ATOM   1266 C CE  . LYS B 2 73  ? 216.131 150.990 241.032 1.00 30.65 ? 73   LYS H CE  1 
ATOM   1267 N NZ  . LYS B 2 73  ? 215.431 152.286 240.812 1.00 30.21 ? 73   LYS H NZ  1 
ATOM   1268 N N   . ASP B 2 74  ? 211.400 149.756 245.271 1.00 33.23 ? 74   ASP H N   1 
ATOM   1269 C CA  . ASP B 2 74  ? 210.625 150.866 245.803 1.00 33.39 ? 74   ASP H CA  1 
ATOM   1270 C C   . ASP B 2 74  ? 211.554 152.008 246.186 1.00 33.31 ? 74   ASP H C   1 
ATOM   1271 O O   . ASP B 2 74  ? 212.348 151.895 247.124 1.00 33.60 ? 74   ASP H O   1 
ATOM   1272 C CB  . ASP B 2 74  ? 209.789 150.423 247.006 1.00 33.74 ? 74   ASP H CB  1 
ATOM   1273 C CG  . ASP B 2 74  ? 208.866 151.520 247.517 1.00 34.04 ? 74   ASP H CG  1 
ATOM   1274 O OD1 . ASP B 2 74  ? 209.279 152.660 247.536 1.00 33.89 ? 74   ASP H OD1 1 
ATOM   1275 O OD2 . ASP B 2 74  ? 207.754 151.214 247.883 1.00 34.29 ? 74   ASP H OD2 1 
ATOM   1276 N N   . THR B 2 75  ? 211.482 153.091 245.425 1.00 33.55 ? 75   THR H N   1 
ATOM   1277 C CA  . THR B 2 75  ? 212.417 154.202 245.549 1.00 33.33 ? 75   THR H CA  1 
ATOM   1278 C C   . THR B 2 75  ? 212.133 155.085 246.757 1.00 33.34 ? 75   THR H C   1 
ATOM   1279 O O   . THR B 2 75  ? 212.930 155.965 247.086 1.00 33.13 ? 75   THR H O   1 
ATOM   1280 C CB  . THR B 2 75  ? 212.395 155.057 244.272 1.00 33.08 ? 75   THR H CB  1 
ATOM   1281 N N   . SER B 2 76  ? 210.987 154.875 247.398 1.00 33.79 ? 76   SER H N   1 
ATOM   1282 C CA  . SER B 2 76  ? 210.606 155.678 248.555 1.00 33.86 ? 76   SER H CA  1 
ATOM   1283 C C   . SER B 2 76  ? 210.892 154.946 249.860 1.00 33.49 ? 76   SER H C   1 
ATOM   1284 O O   . SER B 2 76  ? 211.294 155.555 250.852 1.00 33.50 ? 76   SER H O   1 
ATOM   1285 C CB  . SER B 2 76  ? 209.132 156.030 248.485 1.00 33.94 ? 76   SER H CB  1 
ATOM   1286 N N   . LYS B 2 77  ? 210.682 153.634 249.855 1.00 33.75 ? 77   LYS H N   1 
ATOM   1287 C CA  . LYS B 2 77  ? 210.844 152.825 251.059 1.00 33.67 ? 77   LYS H CA  1 
ATOM   1288 C C   . LYS B 2 77  ? 212.227 152.192 251.164 1.00 33.41 ? 77   LYS H C   1 
ATOM   1289 O O   . LYS B 2 77  ? 212.541 151.550 252.166 1.00 33.78 ? 77   LYS H O   1 
ATOM   1290 C CB  . LYS B 2 77  ? 209.790 151.722 251.104 1.00 33.65 ? 77   LYS H CB  1 
ATOM   1291 C CG  . LYS B 2 77  ? 208.360 152.208 251.200 1.00 33.36 ? 77   LYS H CG  1 
ATOM   1292 C CD  . LYS B 2 77  ? 207.396 151.034 251.216 1.00 33.69 ? 77   LYS H CD  1 
ATOM   1293 C CE  . LYS B 2 77  ? 205.952 151.496 251.221 1.00 34.14 ? 77   LYS H CE  1 
ATOM   1294 N NZ  . LYS B 2 77  ? 205.010 150.352 251.105 1.00 34.74 ? 77   LYS H NZ  1 
ATOM   1295 N N   . ASN B 2 78  ? 213.037 152.337 250.119 1.00 33.50 ? 78   ASN H N   1 
ATOM   1296 C CA  . ASN B 2 78  ? 214.330 151.662 250.065 1.00 33.60 ? 78   ASN H CA  1 
ATOM   1297 C C   . ASN B 2 78  ? 214.163 150.163 250.247 1.00 33.41 ? 78   ASN H C   1 
ATOM   1298 O O   . ASN B 2 78  ? 214.714 149.567 251.175 1.00 33.46 ? 78   ASN H O   1 
ATOM   1299 C CB  . ASN B 2 78  ? 215.304 152.235 251.077 1.00 33.10 ? 78   ASN H CB  1 
ATOM   1300 C CG  . ASN B 2 78  ? 215.835 153.573 250.662 1.00 33.54 ? 78   ASN H CG  1 
ATOM   1301 O OD1 . ASN B 2 78  ? 216.379 153.725 249.554 1.00 33.54 ? 78   ASN H OD1 1 
ATOM   1302 N ND2 . ASN B 2 78  ? 215.693 154.548 251.521 1.00 32.24 ? 78   ASN H ND2 1 
ATOM   1303 N N   . GLN B 2 79  ? 213.341 149.573 249.388 1.00 33.38 ? 79   GLN H N   1 
ATOM   1304 C CA  . GLN B 2 79  ? 213.085 148.141 249.429 1.00 32.97 ? 79   GLN H CA  1 
ATOM   1305 C C   . GLN B 2 79  ? 213.228 147.519 248.049 1.00 33.01 ? 79   GLN H C   1 
ATOM   1306 O O   . GLN B 2 79  ? 212.846 148.116 247.043 1.00 33.00 ? 79   GLN H O   1 
ATOM   1307 C CB  . GLN B 2 79  ? 211.683 147.858 249.974 1.00 33.09 ? 79   GLN H CB  1 
ATOM   1308 C CG  . GLN B 2 79  ? 211.469 148.305 251.399 1.00 33.28 ? 79   GLN H CG  1 
ATOM   1309 C CD  . GLN B 2 79  ? 210.082 147.992 251.897 1.00 33.80 ? 79   GLN H CD  1 
ATOM   1310 O OE1 . GLN B 2 79  ? 209.280 147.376 251.191 1.00 33.86 ? 79   GLN H OE1 1 
ATOM   1311 N NE2 . GLN B 2 79  ? 209.781 148.422 253.115 1.00 33.72 ? 79   GLN H NE2 1 
ATOM   1312 N N   . VAL B 2 80  ? 213.736 146.298 248.007 1.00 32.47 ? 80   VAL H N   1 
ATOM   1313 C CA  . VAL B 2 80  ? 213.833 145.561 246.754 1.00 31.83 ? 80   VAL H CA  1 
ATOM   1314 C C   . VAL B 2 80  ? 212.937 144.335 246.798 1.00 31.88 ? 80   VAL H C   1 
ATOM   1315 O O   . VAL B 2 80  ? 212.962 143.568 247.758 1.00 32.87 ? 80   VAL H O   1 
ATOM   1316 C CB  . VAL B 2 80  ? 215.291 145.166 246.470 1.00 31.87 ? 80   VAL H CB  1 
ATOM   1317 C CG1 . VAL B 2 80  ? 215.380 144.352 245.187 1.00 32.11 ? 80   VAL H CG1 1 
ATOM   1318 C CG2 . VAL B 2 80  ? 216.130 146.430 246.359 1.00 32.23 ? 80   VAL H CG2 1 
ATOM   1319 N N   . VAL B 2 81  ? 212.102 144.179 245.781 1.00 32.10 ? 81   VAL H N   1 
ATOM   1320 C CA  . VAL B 2 81  ? 211.122 143.105 245.784 1.00 32.01 ? 81   VAL H CA  1 
ATOM   1321 C C   . VAL B 2 81  ? 211.345 142.093 244.671 1.00 32.35 ? 81   VAL H C   1 
ATOM   1322 O O   . VAL B 2 81  ? 211.435 142.444 243.493 1.00 32.33 ? 81   VAL H O   1 
ATOM   1323 C CB  . VAL B 2 81  ? 209.703 143.688 245.675 1.00 31.91 ? 81   VAL H CB  1 
ATOM   1324 C CG1 . VAL B 2 81  ? 208.675 142.568 245.638 1.00 32.75 ? 81   VAL H CG1 1 
ATOM   1325 C CG2 . VAL B 2 81  ? 209.449 144.607 246.861 1.00 33.59 ? 81   VAL H CG2 1 
ATOM   1326 N N   . LEU B 2 82  ? 211.413 140.826 245.060 1.00 32.52 ? 82   LEU H N   1 
ATOM   1327 C CA  . LEU B 2 82  ? 211.554 139.724 244.120 1.00 32.69 ? 82   LEU H CA  1 
ATOM   1328 C C   . LEU B 2 82  ? 210.265 138.933 244.011 1.00 32.77 ? 82   LEU H C   1 
ATOM   1329 O O   . LEU B 2 82  ? 209.737 138.443 245.010 1.00 33.07 ? 82   LEU H O   1 
ATOM   1330 C CB  . LEU B 2 82  ? 212.676 138.774 244.559 1.00 32.74 ? 82   LEU H CB  1 
ATOM   1331 C CG  . LEU B 2 82  ? 212.780 137.442 243.772 1.00 32.38 ? 82   LEU H CG  1 
ATOM   1332 C CD1 . LEU B 2 82  ? 213.203 137.718 242.337 1.00 32.87 ? 82   LEU H CD1 1 
ATOM   1333 C CD2 . LEU B 2 82  ? 213.772 136.529 244.461 1.00 32.46 ? 82   LEU H CD2 1 
ATOM   1334 N N   . THR B 2 83  ? 209.785 138.768 242.789 1.00 32.74 ? 83   THR H N   1 
ATOM   1335 C CA  . THR B 2 83  ? 208.614 137.944 242.549 1.00 32.85 ? 83   THR H CA  1 
ATOM   1336 C C   . THR B 2 83  ? 209.008 136.693 241.779 1.00 33.23 ? 83   THR H C   1 
ATOM   1337 O O   . THR B 2 83  ? 209.572 136.773 240.687 1.00 33.37 ? 83   THR H O   1 
ATOM   1338 C CB  . THR B 2 83  ? 207.536 138.716 241.766 1.00 33.04 ? 83   THR H CB  1 
ATOM   1339 O OG1 . THR B 2 83  ? 207.135 139.872 242.511 1.00 32.56 ? 83   THR H OG1 1 
ATOM   1340 C CG2 . THR B 2 83  ? 206.327 137.832 241.535 1.00 34.17 ? 83   THR H CG2 1 
ATOM   1341 N N   . MET B 2 84  ? 208.713 135.536 242.354 1.00 33.47 ? 84   MET H N   1 
ATOM   1342 C CA  . MET B 2 84  ? 209.017 134.266 241.711 1.00 34.01 ? 84   MET H CA  1 
ATOM   1343 C C   . MET B 2 84  ? 207.747 133.452 241.549 1.00 34.50 ? 84   MET H C   1 
ATOM   1344 O O   . MET B 2 84  ? 207.106 133.082 242.534 1.00 34.66 ? 84   MET H O   1 
ATOM   1345 C CB  . MET B 2 84  ? 210.063 133.498 242.513 1.00 33.84 ? 84   MET H CB  1 
ATOM   1346 C CG  . MET B 2 84  ? 210.466 132.176 241.897 1.00 34.72 ? 84   MET H CG  1 
ATOM   1347 S SD  . MET B 2 84  ? 211.830 131.393 242.770 1.00 33.14 ? 84   MET H SD  1 
ATOM   1348 C CE  . MET B 2 84  ? 212.109 129.970 241.723 1.00 33.02 ? 84   MET H CE  1 
ATOM   1349 N N   . THR B 2 85  ? 207.357 133.204 240.307 1.00 35.18 ? 85   THR H N   1 
ATOM   1350 C CA  . THR B 2 85  ? 206.070 132.572 240.051 1.00 35.59 ? 85   THR H CA  1 
ATOM   1351 C C   . THR B 2 85  ? 206.195 131.093 239.739 1.00 35.60 ? 85   THR H C   1 
ATOM   1352 O O   . THR B 2 85  ? 207.295 130.579 239.543 1.00 35.57 ? 85   THR H O   1 
ATOM   1353 C CB  . THR B 2 85  ? 205.342 133.268 238.891 1.00 35.90 ? 85   THR H CB  1 
ATOM   1354 O OG1 . THR B 2 85  ? 204.001 132.775 238.809 1.00 36.49 ? 85   THR H OG1 1 
ATOM   1355 C CG2 . THR B 2 85  ? 206.063 132.997 237.578 1.00 36.01 ? 85   THR H CG2 1 
ATOM   1356 N N   . ASN B 2 86  ? 205.050 130.417 239.678 1.00 36.01 ? 86   ASN H N   1 
ATOM   1357 C CA  . ASN B 2 86  ? 204.984 129.015 239.289 1.00 35.98 ? 86   ASN H CA  1 
ATOM   1358 C C   . ASN B 2 86  ? 205.995 128.158 240.035 1.00 36.24 ? 86   ASN H C   1 
ATOM   1359 O O   . ASN B 2 86  ? 206.751 127.412 239.411 1.00 36.47 ? 86   ASN H O   1 
ATOM   1360 C CB  . ASN B 2 86  ? 205.165 128.872 237.791 1.00 35.31 ? 86   ASN H CB  1 
ATOM   1361 C CG  . ASN B 2 86  ? 204.037 129.492 237.021 1.00 35.99 ? 86   ASN H CG  1 
ATOM   1362 O OD1 . ASN B 2 86  ? 202.869 129.383 237.415 1.00 35.03 ? 86   ASN H OD1 1 
ATOM   1363 N ND2 . ASN B 2 86  ? 204.357 130.140 235.929 1.00 33.95 ? 86   ASN H ND2 1 
ATOM   1364 N N   . MET B 2 87  ? 206.023 128.270 241.361 1.00 36.52 ? 87   MET H N   1 
ATOM   1365 C CA  . MET B 2 87  ? 206.985 127.505 242.147 1.00 36.41 ? 87   MET H CA  1 
ATOM   1366 C C   . MET B 2 87  ? 206.571 126.050 242.338 1.00 36.20 ? 87   MET H C   1 
ATOM   1367 O O   . MET B 2 87  ? 205.392 125.736 242.505 1.00 36.28 ? 87   MET H O   1 
ATOM   1368 C CB  . MET B 2 87  ? 207.219 128.164 243.499 1.00 37.01 ? 87   MET H CB  1 
ATOM   1369 C CG  . MET B 2 87  ? 207.951 129.488 243.420 1.00 36.49 ? 87   MET H CG  1 
ATOM   1370 S SD  . MET B 2 87  ? 208.278 130.201 245.033 1.00 36.11 ? 87   MET H SD  1 
ATOM   1371 C CE  . MET B 2 87  ? 209.766 129.340 245.520 1.00 35.15 ? 87   MET H CE  1 
ATOM   1372 N N   . ASP B 2 88  ? 207.570 125.173 242.337 1.00 36.09 ? 88   ASP H N   1 
ATOM   1373 C CA  . ASP B 2 88  ? 207.410 123.747 242.599 1.00 35.80 ? 88   ASP H CA  1 
ATOM   1374 C C   . ASP B 2 88  ? 208.093 123.396 243.922 1.00 35.72 ? 88   ASP H C   1 
ATOM   1375 O O   . ASP B 2 88  ? 208.934 124.158 244.391 1.00 35.37 ? 88   ASP H O   1 
ATOM   1376 C CB  . ASP B 2 88  ? 208.019 122.933 241.450 1.00 35.95 ? 88   ASP H CB  1 
ATOM   1377 N N   . PRO B 2 89  ? 207.775 122.250 244.531 1.00 35.48 ? 89   PRO H N   1 
ATOM   1378 C CA  . PRO B 2 89  ? 208.385 121.722 245.743 1.00 35.72 ? 89   PRO H CA  1 
ATOM   1379 C C   . PRO B 2 89  ? 209.915 121.740 245.688 1.00 35.23 ? 89   PRO H C   1 
ATOM   1380 O O   . PRO B 2 89  ? 210.581 121.895 246.713 1.00 35.45 ? 89   PRO H O   1 
ATOM   1381 C CB  . PRO B 2 89  ? 207.831 120.295 245.777 1.00 35.27 ? 89   PRO H CB  1 
ATOM   1382 C CG  . PRO B 2 89  ? 206.476 120.409 245.106 1.00 35.69 ? 89   PRO H CG  1 
ATOM   1383 C CD  . PRO B 2 89  ? 206.671 121.430 244.003 1.00 35.22 ? 89   PRO H CD  1 
ATOM   1384 N N   . VAL B 2 90  ? 210.469 121.611 244.488 1.00 35.08 ? 90   VAL H N   1 
ATOM   1385 C CA  . VAL B 2 90  ? 211.916 121.585 244.300 1.00 34.78 ? 90   VAL H CA  1 
ATOM   1386 C C   . VAL B 2 90  ? 212.561 122.953 244.513 1.00 34.80 ? 90   VAL H C   1 
ATOM   1387 O O   . VAL B 2 90  ? 213.785 123.065 244.570 1.00 34.67 ? 90   VAL H O   1 
ATOM   1388 C CB  . VAL B 2 90  ? 212.259 121.078 242.889 1.00 36.08 ? 90   VAL H CB  1 
ATOM   1389 N N   . ASP B 2 91  ? 211.738 123.992 244.615 1.00 34.97 ? 91   ASP H N   1 
ATOM   1390 C CA  . ASP B 2 91  ? 212.225 125.357 244.768 1.00 34.78 ? 91   ASP H CA  1 
ATOM   1391 C C   . ASP B 2 91  ? 212.362 125.748 246.237 1.00 34.69 ? 91   ASP H C   1 
ATOM   1392 O O   . ASP B 2 91  ? 212.635 126.907 246.553 1.00 34.34 ? 91   ASP H O   1 
ATOM   1393 C CB  . ASP B 2 91  ? 211.290 126.346 244.061 1.00 35.14 ? 91   ASP H CB  1 
ATOM   1394 C CG  . ASP B 2 91  ? 211.296 126.231 242.523 1.00 35.29 ? 91   ASP H CG  1 
ATOM   1395 O OD1 . ASP B 2 91  ? 212.356 126.269 241.935 1.00 34.82 ? 91   ASP H OD1 1 
ATOM   1396 O OD2 . ASP B 2 91  ? 210.231 126.121 241.954 1.00 35.83 ? 91   ASP H OD2 1 
ATOM   1397 N N   . THR B 2 92  ? 212.187 124.780 247.134 1.00 34.40 ? 92   THR H N   1 
ATOM   1398 C CA  . THR B 2 92  ? 212.377 125.029 248.559 1.00 34.07 ? 92   THR H CA  1 
ATOM   1399 C C   . THR B 2 92  ? 213.817 125.441 248.830 1.00 33.65 ? 92   THR H C   1 
ATOM   1400 O O   . THR B 2 92  ? 214.754 124.761 248.408 1.00 33.75 ? 92   THR H O   1 
ATOM   1401 C CB  . THR B 2 92  ? 212.026 123.778 249.390 1.00 34.16 ? 92   THR H CB  1 
ATOM   1402 O OG1 . THR B 2 92  ? 210.629 123.474 249.240 1.00 35.57 ? 92   THR H OG1 1 
ATOM   1403 C CG2 . THR B 2 92  ? 212.356 123.992 250.855 1.00 34.20 ? 92   THR H CG2 1 
ATOM   1404 N N   . ALA B 2 93  ? 213.996 126.563 249.521 1.00 33.43 ? 93   ALA H N   1 
ATOM   1405 C CA  . ALA B 2 93  ? 215.340 127.074 249.773 1.00 32.68 ? 93   ALA H CA  1 
ATOM   1406 C C   . ALA B 2 93  ? 215.348 128.204 250.784 1.00 31.63 ? 93   ALA H C   1 
ATOM   1407 O O   . ALA B 2 93  ? 214.314 128.812 251.064 1.00 33.40 ? 93   ALA H O   1 
ATOM   1408 C CB  . ALA B 2 93  ? 215.965 127.553 248.471 1.00 32.35 ? 93   ALA H CB  1 
ATOM   1409 N N   . THR B 2 94  ? 216.535 128.519 251.291 1.00 31.84 ? 94   THR H N   1 
ATOM   1410 C CA  . THR B 2 94  ? 216.725 129.735 252.067 1.00 31.85 ? 94   THR H CA  1 
ATOM   1411 C C   . THR B 2 94  ? 217.073 130.872 251.124 1.00 31.22 ? 94   THR H C   1 
ATOM   1412 O O   . THR B 2 94  ? 217.977 130.749 250.299 1.00 32.88 ? 94   THR H O   1 
ATOM   1413 C CB  . THR B 2 94  ? 217.839 129.579 253.119 1.00 31.08 ? 94   THR H CB  1 
ATOM   1414 O OG1 . THR B 2 94  ? 217.490 128.543 254.041 1.00 30.81 ? 94   THR H OG1 1 
ATOM   1415 C CG2 . THR B 2 94  ? 218.028 130.887 253.884 1.00 31.60 ? 94   THR H CG2 1 
ATOM   1416 N N   . TYR B 2 95  ? 216.339 131.968 251.218 1.00 31.48 ? 95   TYR H N   1 
ATOM   1417 C CA  . TYR B 2 95  ? 216.561 133.093 250.324 1.00 31.50 ? 95   TYR H CA  1 
ATOM   1418 C C   . TYR B 2 95  ? 217.292 134.224 251.026 1.00 31.42 ? 95   TYR H C   1 
ATOM   1419 O O   . TYR B 2 95  ? 216.973 134.576 252.160 1.00 31.16 ? 95   TYR H O   1 
ATOM   1420 C CB  . TYR B 2 95  ? 215.230 133.570 249.744 1.00 31.76 ? 95   TYR H CB  1 
ATOM   1421 C CG  . TYR B 2 95  ? 214.630 132.592 248.749 1.00 31.94 ? 95   TYR H CG  1 
ATOM   1422 C CD1 . TYR B 2 95  ? 213.970 131.462 249.201 1.00 32.43 ? 95   TYR H CD1 1 
ATOM   1423 C CD2 . TYR B 2 95  ? 214.738 132.829 247.388 1.00 31.64 ? 95   TYR H CD2 1 
ATOM   1424 C CE1 . TYR B 2 95  ? 213.431 130.570 248.297 1.00 33.01 ? 95   TYR H CE1 1 
ATOM   1425 C CE2 . TYR B 2 95  ? 214.192 131.935 246.487 1.00 31.15 ? 95   TYR H CE2 1 
ATOM   1426 C CZ  . TYR B 2 95  ? 213.546 130.810 246.939 1.00 32.16 ? 95   TYR H CZ  1 
ATOM   1427 O OH  . TYR B 2 95  ? 213.008 129.918 246.043 1.00 32.80 ? 95   TYR H OH  1 
ATOM   1428 N N   . TYR B 2 96  ? 218.271 134.793 250.335 1.00 30.90 ? 96   TYR H N   1 
ATOM   1429 C CA  . TYR B 2 96  ? 219.064 135.896 250.854 1.00 30.60 ? 96   TYR H CA  1 
ATOM   1430 C C   . TYR B 2 96  ? 219.014 137.076 249.893 1.00 30.63 ? 96   TYR H C   1 
ATOM   1431 O O   . TYR B 2 96  ? 218.972 136.881 248.676 1.00 30.13 ? 96   TYR H O   1 
ATOM   1432 C CB  . TYR B 2 96  ? 220.541 135.497 250.986 1.00 30.25 ? 96   TYR H CB  1 
ATOM   1433 C CG  . TYR B 2 96  ? 220.846 134.247 251.768 1.00 30.80 ? 96   TYR H CG  1 
ATOM   1434 C CD1 . TYR B 2 96  ? 221.130 134.311 253.122 1.00 31.20 ? 96   TYR H CD1 1 
ATOM   1435 C CD2 . TYR B 2 96  ? 220.890 133.033 251.109 1.00 31.06 ? 96   TYR H CD2 1 
ATOM   1436 C CE1 . TYR B 2 96  ? 221.458 133.158 253.808 1.00 31.29 ? 96   TYR H CE1 1 
ATOM   1437 C CE2 . TYR B 2 96  ? 221.216 131.888 251.791 1.00 31.34 ? 96   TYR H CE2 1 
ATOM   1438 C CZ  . TYR B 2 96  ? 221.503 131.943 253.132 1.00 31.08 ? 96   TYR H CZ  1 
ATOM   1439 O OH  . TYR B 2 96  ? 221.849 130.794 253.806 1.00 31.66 ? 96   TYR H OH  1 
ATOM   1440 N N   . CYS B 2 97  ? 219.137 138.291 250.431 1.00 30.07 ? 97   CYS H N   1 
ATOM   1441 C CA  . CYS B 2 97  ? 219.447 139.473 249.631 1.00 30.21 ? 97   CYS H CA  1 
ATOM   1442 C C   . CYS B 2 97  ? 220.793 140.026 250.091 1.00 29.83 ? 97   CYS H C   1 
ATOM   1443 O O   . CYS B 2 97  ? 221.159 139.902 251.264 1.00 30.21 ? 97   CYS H O   1 
ATOM   1444 C CB  . CYS B 2 97  ? 218.336 140.539 249.716 1.00 31.01 ? 97   CYS H CB  1 
ATOM   1445 S SG  . CYS B 2 97  ? 218.034 141.252 251.358 1.00 32.57 ? 97   CYS H SG  1 
ATOM   1446 N N   . ALA B 2 98  ? 221.544 140.609 249.167 1.00 28.74 ? 98   ALA H N   1 
ATOM   1447 C CA  . ALA B 2 98  ? 222.866 141.119 249.512 1.00 28.64 ? 98   ALA H CA  1 
ATOM   1448 C C   . ALA B 2 98  ? 223.271 142.293 248.633 1.00 29.22 ? 98   ALA H C   1 
ATOM   1449 O O   . ALA B 2 98  ? 222.795 142.442 247.506 1.00 29.12 ? 98   ALA H O   1 
ATOM   1450 C CB  . ALA B 2 98  ? 223.892 140.000 249.403 1.00 28.76 ? 98   ALA H CB  1 
ATOM   1451 N N   . HIS B 2 99  ? 224.164 143.122 249.163 1.00 28.58 ? 99   HIS H N   1 
ATOM   1452 C CA  . HIS B 2 99  ? 224.693 144.275 248.444 1.00 28.26 ? 99   HIS H CA  1 
ATOM   1453 C C   . HIS B 2 99  ? 225.665 143.836 247.357 1.00 28.30 ? 99   HIS H C   1 
ATOM   1454 O O   . HIS B 2 99  ? 226.454 142.914 247.555 1.00 28.40 ? 99   HIS H O   1 
ATOM   1455 C CB  . HIS B 2 99  ? 225.379 145.237 249.420 1.00 28.15 ? 99   HIS H CB  1 
ATOM   1456 C CG  . HIS B 2 99  ? 225.875 146.496 248.790 1.00 27.64 ? 99   HIS H CG  1 
ATOM   1457 N ND1 . HIS B 2 99  ? 227.084 146.570 248.138 1.00 27.26 ? 99   HIS H ND1 1 
ATOM   1458 C CD2 . HIS B 2 99  ? 225.330 147.731 248.713 1.00 29.55 ? 99   HIS H CD2 1 
ATOM   1459 C CE1 . HIS B 2 99  ? 227.262 147.797 247.684 1.00 27.51 ? 99   HIS H CE1 1 
ATOM   1460 N NE2 . HIS B 2 99  ? 226.213 148.521 248.021 1.00 28.74 ? 99   HIS H NE2 1 
ATOM   1461 N N   . VAL B 2 100 ? 225.603 144.495 246.205 1.00 28.44 ? 100  VAL H N   1 
ATOM   1462 C CA  . VAL B 2 100 ? 226.456 144.150 245.073 1.00 28.09 ? 100  VAL H CA  1 
ATOM   1463 C C   . VAL B 2 100 ? 227.452 145.253 244.737 1.00 27.85 ? 100  VAL H C   1 
ATOM   1464 O O   . VAL B 2 100 ? 227.067 146.393 244.482 1.00 27.93 ? 100  VAL H O   1 
ATOM   1465 C CB  . VAL B 2 100 ? 225.585 143.881 243.829 1.00 28.58 ? 100  VAL H CB  1 
ATOM   1466 C CG1 . VAL B 2 100 ? 226.453 143.518 242.633 1.00 28.26 ? 100  VAL H CG1 1 
ATOM   1467 C CG2 . VAL B 2 100 ? 224.614 142.777 244.132 1.00 29.05 ? 100  VAL H CG2 1 
ATOM   1468 N N   . LEU B 2 101 ? 228.731 144.895 244.687 1.00 27.31 ? 101  LEU H N   1 
ATOM   1469 C CA  . LEU B 2 101 ? 229.764 145.821 244.236 1.00 26.81 ? 101  LEU H CA  1 
ATOM   1470 C C   . LEU B 2 101 ? 229.735 145.884 242.711 1.00 27.22 ? 101  LEU H C   1 
ATOM   1471 O O   . LEU B 2 101 ? 229.630 144.853 242.045 1.00 27.39 ? 101  LEU H O   1 
ATOM   1472 C CB  . LEU B 2 101 ? 231.140 145.362 244.734 1.00 26.66 ? 101  LEU H CB  1 
ATOM   1473 C CG  . LEU B 2 101 ? 231.334 145.325 246.260 1.00 27.13 ? 101  LEU H CG  1 
ATOM   1474 C CD1 . LEU B 2 101 ? 232.664 144.653 246.575 1.00 27.53 ? 101  LEU H CD1 1 
ATOM   1475 C CD2 . LEU B 2 101 ? 231.301 146.740 246.820 1.00 26.35 ? 101  LEU H CD2 1 
ATOM   1476 N N   . VAL B 2 102 ? 229.796 147.092 242.156 1.00 27.33 ? 102  VAL H N   1 
ATOM   1477 C CA  . VAL B 2 102 ? 229.595 147.265 240.719 1.00 27.19 ? 102  VAL H CA  1 
ATOM   1478 C C   . VAL B 2 102 ? 230.738 147.975 239.995 1.00 27.77 ? 102  VAL H C   1 
ATOM   1479 O O   . VAL B 2 102 ? 231.211 149.022 240.433 1.00 28.16 ? 102  VAL H O   1 
ATOM   1480 C CB  . VAL B 2 102 ? 228.289 148.047 240.479 1.00 27.30 ? 102  VAL H CB  1 
ATOM   1481 C CG1 . VAL B 2 102 ? 228.076 148.271 238.996 1.00 28.27 ? 102  VAL H CG1 1 
ATOM   1482 C CG2 . VAL B 2 102 ? 227.122 147.279 241.082 1.00 28.11 ? 102  VAL H CG2 1 
ATOM   1483 N N   . TRP B 2 103 ? 231.142 147.403 238.860 1.00 28.19 ? 103  TRP H N   1 
ATOM   1484 C CA  . TRP B 2 103 ? 232.126 147.996 237.952 1.00 28.44 ? 103  TRP H CA  1 
ATOM   1485 C C   . TRP B 2 103 ? 231.437 149.016 237.047 1.00 27.87 ? 103  TRP H C   1 
ATOM   1486 O O   . TRP B 2 103 ? 230.287 148.818 236.660 1.00 28.00 ? 103  TRP H O   1 
ATOM   1487 C CB  . TRP B 2 103 ? 232.773 146.916 237.080 1.00 28.36 ? 103  TRP H CB  1 
ATOM   1488 C CG  . TRP B 2 103 ? 233.737 146.014 237.798 1.00 28.30 ? 103  TRP H CG  1 
ATOM   1489 C CD1 . TRP B 2 103 ? 233.453 144.828 238.393 1.00 28.63 ? 103  TRP H CD1 1 
ATOM   1490 C CD2 . TRP B 2 103 ? 235.160 146.214 237.971 1.00 28.43 ? 103  TRP H CD2 1 
ATOM   1491 N NE1 . TRP B 2 103 ? 234.595 144.286 238.933 1.00 28.31 ? 103  TRP H NE1 1 
ATOM   1492 C CE2 . TRP B 2 103 ? 235.642 145.119 238.684 1.00 28.13 ? 103  TRP H CE2 1 
ATOM   1493 C CE3 . TRP B 2 103 ? 236.043 147.212 237.584 1.00 28.96 ? 103  TRP H CE3 1 
ATOM   1494 C CZ2 . TRP B 2 103 ? 236.975 144.997 239.023 1.00 28.77 ? 103  TRP H CZ2 1 
ATOM   1495 C CZ3 . TRP B 2 103 ? 237.382 147.091 237.923 1.00 29.00 ? 103  TRP H CZ3 1 
ATOM   1496 C CH2 . TRP B 2 103 ? 237.834 146.011 238.623 1.00 28.89 ? 103  TRP H CH2 1 
ATOM   1497 N N   . PHE B 2 104 ? 232.137 150.093 236.701 1.00 28.15 ? 104  PHE H N   1 
ATOM   1498 C CA  . PHE B 2 104 ? 231.557 151.163 235.893 1.00 27.97 ? 104  PHE H CA  1 
ATOM   1499 C C   . PHE B 2 104 ? 232.131 151.234 234.483 1.00 27.33 ? 104  PHE H C   1 
ATOM   1500 O O   . PHE B 2 104 ? 233.151 150.614 234.180 1.00 30.19 ? 104  PHE H O   1 
ATOM   1501 C CB  . PHE B 2 104 ? 231.754 152.499 236.588 1.00 27.74 ? 104  PHE H CB  1 
ATOM   1502 C CG  . PHE B 2 104 ? 231.136 152.539 237.931 1.00 27.39 ? 104  PHE H CG  1 
ATOM   1503 C CD1 . PHE B 2 104 ? 231.929 152.539 239.060 1.00 27.78 ? 104  PHE H CD1 1 
ATOM   1504 C CD2 . PHE B 2 104 ? 229.759 152.565 238.080 1.00 27.23 ? 104  PHE H CD2 1 
ATOM   1505 C CE1 . PHE B 2 104 ? 231.366 152.574 240.313 1.00 27.08 ? 104  PHE H CE1 1 
ATOM   1506 C CE2 . PHE B 2 104 ? 229.192 152.601 239.332 1.00 27.79 ? 104  PHE H CE2 1 
ATOM   1507 C CZ  . PHE B 2 104 ? 229.999 152.607 240.450 1.00 27.16 ? 104  PHE H CZ  1 
ATOM   1508 N N   . GLY B 2 105 ? 231.458 151.993 233.620 1.00 27.61 ? 105  GLY H N   1 
ATOM   1509 C CA  . GLY B 2 105 ? 231.822 152.103 232.209 1.00 28.11 ? 105  GLY H CA  1 
ATOM   1510 C C   . GLY B 2 105 ? 231.060 151.043 231.433 1.00 28.26 ? 105  GLY H C   1 
ATOM   1511 O O   . GLY B 2 105 ? 229.909 151.252 231.050 1.00 28.21 ? 105  GLY H O   1 
ATOM   1512 N N   . GLU B 2 106 ? 231.638 149.855 231.345 1.00 28.01 ? 106  GLU H N   1 
ATOM   1513 C CA  . GLU B 2 106 ? 230.849 148.678 231.033 1.00 27.96 ? 106  GLU H CA  1 
ATOM   1514 C C   . GLU B 2 106 ? 230.395 148.094 232.357 1.00 27.96 ? 106  GLU H C   1 
ATOM   1515 O O   . GLU B 2 106 ? 231.209 147.591 233.132 1.00 28.34 ? 106  GLU H O   1 
ATOM   1516 C CB  . GLU B 2 106 ? 231.649 147.653 230.229 1.00 28.43 ? 106  GLU H CB  1 
ATOM   1517 N N   . VAL B 2 107 ? 229.110 148.235 232.654 1.00 27.74 ? 107  VAL H N   1 
ATOM   1518 C CA  . VAL B 2 107 ? 228.632 147.915 233.988 1.00 28.00 ? 107  VAL H CA  1 
ATOM   1519 C C   . VAL B 2 107 ? 228.518 146.422 234.214 1.00 28.31 ? 107  VAL H C   1 
ATOM   1520 O O   . VAL B 2 107 ? 227.818 145.717 233.487 1.00 28.31 ? 107  VAL H O   1 
ATOM   1521 C CB  . VAL B 2 107 ? 227.280 148.600 234.248 1.00 27.30 ? 107  VAL H CB  1 
ATOM   1522 C CG1 . VAL B 2 107 ? 226.729 148.186 235.605 1.00 28.92 ? 107  VAL H CG1 1 
ATOM   1523 C CG2 . VAL B 2 107 ? 227.477 150.108 234.196 1.00 28.13 ? 107  VAL H CG2 1 
ATOM   1524 N N   . LEU B 2 108 ? 229.228 145.954 235.232 1.00 28.46 ? 108  LEU H N   1 
ATOM   1525 C CA  . LEU B 2 108 ? 229.273 144.542 235.574 1.00 28.58 ? 108  LEU H CA  1 
ATOM   1526 C C   . LEU B 2 108 ? 229.194 144.366 237.088 1.00 27.87 ? 108  LEU H C   1 
ATOM   1527 O O   . LEU B 2 108 ? 229.678 145.217 237.832 1.00 28.95 ? 108  LEU H O   1 
ATOM   1528 C CB  . LEU B 2 108 ? 230.582 143.924 235.057 1.00 28.72 ? 108  LEU H CB  1 
ATOM   1529 C CG  . LEU B 2 108 ? 230.828 144.008 233.539 1.00 28.23 ? 108  LEU H CG  1 
ATOM   1530 C CD1 . LEU B 2 108 ? 232.265 143.610 233.247 1.00 28.42 ? 108  LEU H CD1 1 
ATOM   1531 C CD2 . LEU B 2 108 ? 229.854 143.101 232.807 1.00 28.45 ? 108  LEU H CD2 1 
ATOM   1532 N N   . PRO B 2 109 ? 228.599 143.276 237.562 1.00 27.35 ? 109  PRO H N   1 
ATOM   1533 C CA  . PRO B 2 109 ? 228.581 142.842 238.945 1.00 27.19 ? 109  PRO H CA  1 
ATOM   1534 C C   . PRO B 2 109 ? 229.962 142.344 239.349 1.00 27.88 ? 109  PRO H C   1 
ATOM   1535 O O   . PRO B 2 109 ? 230.692 141.805 238.518 1.00 28.25 ? 109  PRO H O   1 
ATOM   1536 C CB  . PRO B 2 109 ? 227.543 141.723 238.918 1.00 28.80 ? 109  PRO H CB  1 
ATOM   1537 C CG  . PRO B 2 109 ? 227.587 141.201 237.493 1.00 29.06 ? 109  PRO H CG  1 
ATOM   1538 C CD  . PRO B 2 109 ? 227.899 142.397 236.635 1.00 28.62 ? 109  PRO H CD  1 
ATOM   1539 N N   . ASP B 2 110 ? 230.313 142.512 240.620 1.00 27.64 ? 110  ASP H N   1 
ATOM   1540 C CA  . ASP B 2 110 ? 231.621 142.087 241.107 1.00 27.47 ? 110  ASP H CA  1 
ATOM   1541 C C   . ASP B 2 110 ? 231.515 141.040 242.220 1.00 27.51 ? 110  ASP H C   1 
ATOM   1542 O O   . ASP B 2 110 ? 231.808 139.864 242.006 1.00 28.38 ? 110  ASP H O   1 
ATOM   1543 C CB  . ASP B 2 110 ? 232.407 143.307 241.599 1.00 27.14 ? 110  ASP H CB  1 
ATOM   1544 C CG  . ASP B 2 110 ? 233.883 143.037 241.840 1.00 28.20 ? 110  ASP H CG  1 
ATOM   1545 O OD1 . ASP B 2 110 ? 234.395 143.490 242.839 1.00 28.92 ? 110  ASP H OD1 1 
ATOM   1546 O OD2 . ASP B 2 110 ? 234.495 142.410 241.008 1.00 27.84 ? 110  ASP H OD2 1 
ATOM   1547 N N   . ALA B 2 111 ? 231.121 141.468 243.418 1.00 26.96 ? 111  ALA H N   1 
ATOM   1548 C CA  . ALA B 2 111 ? 231.062 140.563 244.566 1.00 25.98 ? 111  ALA H CA  1 
ATOM   1549 C C   . ALA B 2 111 ? 230.025 141.019 245.585 1.00 26.68 ? 111  ALA H C   1 
ATOM   1550 O O   . ALA B 2 111 ? 229.607 142.178 245.589 1.00 27.28 ? 111  ALA H O   1 
ATOM   1551 C CB  . ALA B 2 111 ? 232.429 140.461 245.228 1.00 27.04 ? 111  ALA H CB  1 
ATOM   1552 N N   . PHE B 2 112 ? 229.615 140.097 246.453 1.00 26.39 ? 112  PHE H N   1 
ATOM   1553 C CA  . PHE B 2 112 ? 228.634 140.393 247.493 1.00 27.04 ? 112  PHE H CA  1 
ATOM   1554 C C   . PHE B 2 112 ? 229.304 140.560 248.853 1.00 27.36 ? 112  PHE H C   1 
ATOM   1555 O O   . PHE B 2 112 ? 229.761 139.584 249.445 1.00 27.65 ? 112  PHE H O   1 
ATOM   1556 C CB  . PHE B 2 112 ? 227.616 139.257 247.591 1.00 27.24 ? 112  PHE H CB  1 
ATOM   1557 C CG  . PHE B 2 112 ? 226.806 139.027 246.354 1.00 27.71 ? 112  PHE H CG  1 
ATOM   1558 C CD1 . PHE B 2 112 ? 227.240 138.149 245.381 1.00 26.73 ? 112  PHE H CD1 1 
ATOM   1559 C CD2 . PHE B 2 112 ? 225.604 139.672 246.167 1.00 29.22 ? 112  PHE H CD2 1 
ATOM   1560 C CE1 . PHE B 2 112 ? 226.491 137.928 244.249 1.00 26.14 ? 112  PHE H CE1 1 
ATOM   1561 C CE2 . PHE B 2 112 ? 224.850 139.446 245.038 1.00 29.38 ? 112  PHE H CE2 1 
ATOM   1562 C CZ  . PHE B 2 112 ? 225.295 138.575 244.076 1.00 27.55 ? 112  PHE H CZ  1 
ATOM   1563 N N   . ASP B 2 113 ? 229.388 141.793 249.342 1.00 27.38 ? 113  ASP H N   1 
ATOM   1564 C CA  . ASP B 2 113 ? 230.079 142.045 250.604 1.00 27.21 ? 113  ASP H CA  1 
ATOM   1565 C C   . ASP B 2 113 ? 229.166 141.901 251.820 1.00 28.08 ? 113  ASP H C   1 
ATOM   1566 O O   . ASP B 2 113 ? 229.478 141.163 252.755 1.00 28.88 ? 113  ASP H O   1 
ATOM   1567 C CB  . ASP B 2 113 ? 230.751 143.423 250.585 1.00 26.68 ? 113  ASP H CB  1 
ATOM   1568 C CG  . ASP B 2 113 ? 229.815 144.548 250.195 1.00 27.79 ? 113  ASP H CG  1 
ATOM   1569 O OD1 . ASP B 2 113 ? 228.679 144.271 249.890 1.00 27.83 ? 113  ASP H OD1 1 
ATOM   1570 O OD2 . ASP B 2 113 ? 230.241 145.677 250.204 1.00 26.55 ? 113  ASP H OD2 1 
ATOM   1571 N N   . VAL B 2 114 ? 228.040 142.600 251.811 1.00 28.10 ? 114  VAL H N   1 
ATOM   1572 C CA  . VAL B 2 114 ? 227.128 142.559 252.948 1.00 28.31 ? 114  VAL H CA  1 
ATOM   1573 C C   . VAL B 2 114 ? 225.889 141.730 252.652 1.00 28.69 ? 114  VAL H C   1 
ATOM   1574 O O   . VAL B 2 114 ? 225.128 142.030 251.732 1.00 28.94 ? 114  VAL H O   1 
ATOM   1575 C CB  . VAL B 2 114 ? 226.699 143.976 253.356 1.00 28.85 ? 114  VAL H CB  1 
ATOM   1576 C CG1 . VAL B 2 114 ? 225.749 143.902 254.542 1.00 31.33 ? 114  VAL H CG1 1 
ATOM   1577 C CG2 . VAL B 2 114 ? 227.926 144.798 253.698 1.00 29.10 ? 114  VAL H CG2 1 
ATOM   1578 N N   . TRP B 2 115 ? 225.689 140.688 253.449 1.00 28.57 ? 115  TRP H N   1 
ATOM   1579 C CA  . TRP B 2 115 ? 224.569 139.773 253.275 1.00 29.08 ? 115  TRP H CA  1 
ATOM   1580 C C   . TRP B 2 115 ? 223.544 139.952 254.382 1.00 29.83 ? 115  TRP H C   1 
ATOM   1581 O O   . TRP B 2 115 ? 223.898 140.274 255.515 1.00 31.12 ? 115  TRP H O   1 
ATOM   1582 C CB  . TRP B 2 115 ? 225.068 138.330 253.293 1.00 29.36 ? 115  TRP H CB  1 
ATOM   1583 C CG  . TRP B 2 115 ? 225.948 137.979 252.145 1.00 28.87 ? 115  TRP H CG  1 
ATOM   1584 C CD1 . TRP B 2 115 ? 227.167 138.513 251.861 1.00 28.44 ? 115  TRP H CD1 1 
ATOM   1585 C CD2 . TRP B 2 115 ? 225.701 136.986 251.131 1.00 27.85 ? 115  TRP H CD2 1 
ATOM   1586 N NE1 . TRP B 2 115 ? 227.686 137.932 250.743 1.00 28.28 ? 115  TRP H NE1 1 
ATOM   1587 C CE2 . TRP B 2 115 ? 226.807 136.988 250.285 1.00 27.94 ? 115  TRP H CE2 1 
ATOM   1588 C CE3 . TRP B 2 115 ? 224.647 136.103 250.880 1.00 28.96 ? 115  TRP H CE3 1 
ATOM   1589 C CZ2 . TRP B 2 115 ? 226.898 136.141 249.204 1.00 28.43 ? 115  TRP H CZ2 1 
ATOM   1590 C CZ3 . TRP B 2 115 ? 224.743 135.251 249.796 1.00 29.15 ? 115  TRP H CZ3 1 
ATOM   1591 C CH2 . TRP B 2 115 ? 225.844 135.272 248.982 1.00 28.51 ? 115  TRP H CH2 1 
ATOM   1592 N N   . GLY B 2 116 ? 222.280 139.689 254.070 1.00 30.04 ? 116  GLY H N   1 
ATOM   1593 C CA  . GLY B 2 116 ? 221.237 139.696 255.088 1.00 30.74 ? 116  GLY H CA  1 
ATOM   1594 C C   . GLY B 2 116 ? 221.227 138.375 255.850 1.00 31.38 ? 116  GLY H C   1 
ATOM   1595 O O   . GLY B 2 116 ? 222.083 137.517 255.628 1.00 31.62 ? 116  GLY H O   1 
ATOM   1596 N N   . GLN B 2 117 ? 220.267 138.225 256.759 1.00 31.53 ? 117  GLN H N   1 
ATOM   1597 C CA  . GLN B 2 117 ? 220.159 137.022 257.578 1.00 31.38 ? 117  GLN H CA  1 
ATOM   1598 C C   . GLN B 2 117 ? 219.584 135.855 256.787 1.00 30.99 ? 117  GLN H C   1 
ATOM   1599 O O   . GLN B 2 117 ? 219.939 134.699 257.016 1.00 31.42 ? 117  GLN H O   1 
ATOM   1600 C CB  . GLN B 2 117 ? 219.282 137.295 258.802 1.00 32.17 ? 117  GLN H CB  1 
ATOM   1601 N N   . GLY B 2 118 ? 218.681 136.166 255.867 1.00 31.21 ? 118  GLY H N   1 
ATOM   1602 C CA  . GLY B 2 118 ? 218.043 135.158 255.035 1.00 31.25 ? 118  GLY H CA  1 
ATOM   1603 C C   . GLY B 2 118 ? 216.724 134.692 255.637 1.00 31.48 ? 118  GLY H C   1 
ATOM   1604 O O   . GLY B 2 118 ? 216.526 134.755 256.852 1.00 31.86 ? 118  GLY H O   1 
ATOM   1605 N N   . THR B 2 119 ? 215.830 134.207 254.784 1.00 31.26 ? 119  THR H N   1 
ATOM   1606 C CA  . THR B 2 119 ? 214.550 133.675 255.237 1.00 31.17 ? 119  THR H CA  1 
ATOM   1607 C C   . THR B 2 119 ? 214.245 132.352 254.547 1.00 31.82 ? 119  THR H C   1 
ATOM   1608 O O   . THR B 2 119 ? 214.501 132.189 253.355 1.00 32.11 ? 119  THR H O   1 
ATOM   1609 C CB  . THR B 2 119 ? 213.407 134.679 254.995 1.00 31.24 ? 119  THR H CB  1 
ATOM   1610 N N   . MET B 2 120 ? 213.715 131.397 255.301 1.00 31.91 ? 120  MET H N   1 
ATOM   1611 C CA  . MET B 2 120 ? 213.435 130.078 254.747 1.00 31.94 ? 120  MET H CA  1 
ATOM   1612 C C   . MET B 2 120 ? 212.046 130.013 254.141 1.00 32.63 ? 120  MET H C   1 
ATOM   1613 O O   . MET B 2 120 ? 211.062 130.348 254.797 1.00 33.31 ? 120  MET H O   1 
ATOM   1614 C CB  . MET B 2 120 ? 213.579 129.014 255.833 1.00 31.57 ? 120  MET H CB  1 
ATOM   1615 N N   . VAL B 2 121 ? 211.962 129.544 252.899 1.00 32.78 ? 121  VAL H N   1 
ATOM   1616 C CA  . VAL B 2 121 ? 210.671 129.388 252.246 1.00 33.68 ? 121  VAL H CA  1 
ATOM   1617 C C   . VAL B 2 121 ? 210.440 127.953 251.797 1.00 34.22 ? 121  VAL H C   1 
ATOM   1618 O O   . VAL B 2 121 ? 211.226 127.392 251.031 1.00 34.23 ? 121  VAL H O   1 
ATOM   1619 C CB  . VAL B 2 121 ? 210.560 130.316 251.028 1.00 33.65 ? 121  VAL H CB  1 
ATOM   1620 C CG1 . VAL B 2 121 ? 209.186 130.152 250.380 1.00 34.86 ? 121  VAL H CG1 1 
ATOM   1621 C CG2 . VAL B 2 121 ? 210.794 131.753 251.459 1.00 33.84 ? 121  VAL H CG2 1 
ATOM   1622 N N   . THR B 2 122 ? 209.338 127.373 252.254 1.00 35.19 ? 122  THR H N   1 
ATOM   1623 C CA  . THR B 2 122 ? 208.975 126.009 251.891 1.00 35.51 ? 122  THR H CA  1 
ATOM   1624 C C   . THR B 2 122 ? 207.862 125.992 250.857 1.00 35.46 ? 122  THR H C   1 
ATOM   1625 O O   . THR B 2 122 ? 206.900 126.754 250.960 1.00 36.03 ? 122  THR H O   1 
ATOM   1626 C CB  . THR B 2 122 ? 208.541 125.205 253.132 1.00 35.52 ? 122  THR H CB  1 
ATOM   1627 O OG1 . THR B 2 122 ? 209.638 125.119 254.051 1.00 33.93 ? 122  THR H OG1 1 
ATOM   1628 C CG2 . THR B 2 122 ? 208.103 123.799 252.739 1.00 35.96 ? 122  THR H CG2 1 
ATOM   1629 N N   . VAL B 2 123 ? 207.990 125.119 249.865 1.00 35.78 ? 123  VAL H N   1 
ATOM   1630 C CA  . VAL B 2 123 ? 206.920 124.939 248.894 1.00 36.06 ? 123  VAL H CA  1 
ATOM   1631 C C   . VAL B 2 123 ? 206.288 123.565 249.080 1.00 36.41 ? 123  VAL H C   1 
ATOM   1632 O O   . VAL B 2 123 ? 206.950 122.541 248.911 1.00 36.76 ? 123  VAL H O   1 
ATOM   1633 C CB  . VAL B 2 123 ? 207.450 125.082 247.456 1.00 35.51 ? 123  VAL H CB  1 
ATOM   1634 C CG1 . VAL B 2 123 ? 206.301 124.931 246.459 1.00 36.31 ? 123  VAL H CG1 1 
ATOM   1635 C CG2 . VAL B 2 123 ? 208.132 126.417 247.292 1.00 36.22 ? 123  VAL H CG2 1 
ATOM   1636 N N   . SER B 2 124 ? 205.023 123.549 249.485 1.00 36.88 ? 124  SER H N   1 
ATOM   1637 C CA  . SER B 2 124 ? 204.340 122.295 249.794 1.00 36.77 ? 124  SER H CA  1 
ATOM   1638 C C   . SER B 2 124 ? 202.826 122.482 249.825 1.00 36.98 ? 124  SER H C   1 
ATOM   1639 O O   . SER B 2 124 ? 202.337 123.610 249.871 1.00 37.24 ? 124  SER H O   1 
ATOM   1640 C CB  . SER B 2 124 ? 204.824 121.751 251.129 1.00 36.81 ? 124  SER H CB  1 
ATOM   1641 O OG  . SER B 2 124 ? 204.371 122.543 252.190 1.00 36.78 ? 124  SER H OG  1 
ATOM   1642 N N   . SER B 2 125 ? 202.086 121.368 249.813 1.00 37.70 ? 125  SER H N   1 
ATOM   1643 C CA  . SER B 2 125 ? 200.625 121.381 249.897 1.00 38.53 ? 125  SER H CA  1 
ATOM   1644 C C   . SER B 2 125 ? 200.168 121.219 251.346 1.00 38.48 ? 125  SER H C   1 
ATOM   1645 O O   . SER B 2 125 ? 200.598 120.301 252.049 1.00 39.94 ? 125  SER H O   1 
ATOM   1646 C CB  . SER B 2 125 ? 200.037 120.277 249.028 1.00 37.17 ? 125  SER H CB  1 
ATOM   1647 N N   . GLN C 3 14  ? 245.805 162.258 251.665 1.00 32.95 ? 14   GLN A N   1 
ATOM   1648 C CA  . GLN C 3 14  ? 245.503 161.428 250.468 1.00 33.13 ? 14   GLN A CA  1 
ATOM   1649 C C   . GLN C 3 14  ? 246.277 161.976 249.267 1.00 33.02 ? 14   GLN A C   1 
ATOM   1650 O O   . GLN C 3 14  ? 246.141 161.400 248.179 1.00 33.41 ? 14   GLN A O   1 
ATOM   1651 C CB  . GLN C 3 14  ? 243.999 161.441 250.188 1.00 31.10 ? 14   GLN A CB  1 
ATOM   1652 N N   . CYS C 3 15  ? 247.085 163.021 249.463 1.00 32.33 ? 15   CYS A N   1 
ATOM   1653 C CA  . CYS C 3 15  ? 247.789 163.652 248.354 1.00 32.75 ? 15   CYS A CA  1 
ATOM   1654 C C   . CYS C 3 15  ? 249.059 162.885 247.992 1.00 34.20 ? 15   CYS A C   1 
ATOM   1655 O O   . CYS C 3 15  ? 249.855 162.530 248.865 1.00 34.65 ? 15   CYS A O   1 
ATOM   1656 C CB  . CYS C 3 15  ? 248.150 165.102 248.702 1.00 32.01 ? 15   CYS A CB  1 
ATOM   1657 S SG  . CYS C 3 15  ? 246.717 166.182 249.003 1.00 29.30 ? 15   CYS A SG  1 
ATOM   1658 N N   . VAL C 3 16  ? 249.252 162.653 246.700 1.00 34.83 ? 16   VAL A N   1 
ATOM   1659 C CA  . VAL C 3 16  ? 250.433 161.951 246.207 1.00 36.01 ? 16   VAL A CA  1 
ATOM   1660 C C   . VAL C 3 16  ? 251.376 162.896 245.470 1.00 36.90 ? 16   VAL A C   1 
ATOM   1661 O O   . VAL C 3 16  ? 251.026 163.437 244.421 1.00 36.16 ? 16   VAL A O   1 
ATOM   1662 C CB  . VAL C 3 16  ? 250.009 160.812 245.261 1.00 35.44 ? 16   VAL A CB  1 
ATOM   1663 C CG1 . VAL C 3 16  ? 251.228 160.125 244.672 1.00 35.45 ? 16   VAL A CG1 1 
ATOM   1664 C CG2 . VAL C 3 16  ? 249.165 159.813 246.029 1.00 34.17 ? 16   VAL A CG2 1 
ATOM   1665 N N   . ASN C 3 17  ? 252.590 163.063 246.003 1.00 37.09 ? 17   ASN A N   1 
ATOM   1666 C CA  . ASN C 3 17  ? 253.583 163.961 245.415 1.00 37.94 ? 17   ASN A CA  1 
ATOM   1667 C C   . ASN C 3 17  ? 254.399 163.237 244.342 1.00 38.63 ? 17   ASN A C   1 
ATOM   1668 O O   . ASN C 3 17  ? 255.591 162.974 244.517 1.00 39.45 ? 17   ASN A O   1 
ATOM   1669 C CB  . ASN C 3 17  ? 254.479 164.560 246.503 1.00 39.10 ? 17   ASN A CB  1 
ATOM   1670 C CG  . ASN C 3 17  ? 254.293 166.066 246.683 1.00 39.11 ? 17   ASN A CG  1 
ATOM   1671 O OD1 . ASN C 3 17  ? 253.784 166.759 245.789 1.00 38.53 ? 17   ASN A OD1 1 
ATOM   1672 N ND2 . ASN C 3 17  ? 254.703 166.567 247.831 1.00 39.45 ? 17   ASN A ND2 1 
ATOM   1673 N N   . LEU C 3 18  ? 253.739 162.918 243.227 1.00 38.55 ? 18   LEU A N   1 
ATOM   1674 C CA  . LEU C 3 18  ? 254.367 162.251 242.086 1.00 38.76 ? 18   LEU A CA  1 
ATOM   1675 C C   . LEU C 3 18  ? 254.680 163.254 240.987 1.00 38.97 ? 18   LEU A C   1 
ATOM   1676 O O   . LEU C 3 18  ? 253.817 163.586 240.176 1.00 38.09 ? 18   LEU A O   1 
ATOM   1677 C CB  . LEU C 3 18  ? 253.439 161.159 241.538 1.00 38.16 ? 18   LEU A CB  1 
ATOM   1678 C CG  . LEU C 3 18  ? 253.938 160.394 240.296 1.00 37.80 ? 18   LEU A CG  1 
ATOM   1679 C CD1 . LEU C 3 18  ? 255.224 159.643 240.629 1.00 38.35 ? 18   LEU A CD1 1 
ATOM   1680 C CD2 . LEU C 3 18  ? 252.851 159.429 239.844 1.00 35.55 ? 18   LEU A CD2 1 
ATOM   1681 N N   . THR C 3 19  ? 255.914 163.745 240.972 1.00 39.73 ? 19   THR A N   1 
ATOM   1682 C CA  . THR C 3 19  ? 256.306 164.782 240.027 1.00 40.65 ? 19   THR A CA  1 
ATOM   1683 C C   . THR C 3 19  ? 257.601 164.406 239.314 1.00 41.43 ? 19   THR A C   1 
ATOM   1684 O O   . THR C 3 19  ? 258.339 163.536 239.781 1.00 41.31 ? 19   THR A O   1 
ATOM   1685 C CB  . THR C 3 19  ? 256.481 166.138 240.744 1.00 40.89 ? 19   THR A CB  1 
ATOM   1686 N N   . THR C 3 20  ? 257.882 165.086 238.195 1.00 41.29 ? 20   THR A N   1 
ATOM   1687 C CA  . THR C 3 20  ? 259.104 164.882 237.415 1.00 42.02 ? 20   THR A CA  1 
ATOM   1688 C C   . THR C 3 20  ? 259.748 166.224 237.085 1.00 42.59 ? 20   THR A C   1 
ATOM   1689 O O   . THR C 3 20  ? 260.924 166.451 237.374 1.00 42.56 ? 20   THR A O   1 
ATOM   1690 C CB  . THR C 3 20  ? 258.821 164.102 236.102 1.00 43.07 ? 20   THR A CB  1 
ATOM   1691 N N   . PRO C 3 26  ? 254.925 173.151 225.456 1.00 30.78 ? 26   PRO A N   1 
ATOM   1692 C CA  . PRO C 3 26  ? 253.846 172.371 224.866 1.00 30.87 ? 26   PRO A CA  1 
ATOM   1693 C C   . PRO C 3 26  ? 253.858 172.466 223.338 1.00 31.80 ? 26   PRO A C   1 
ATOM   1694 O O   . PRO C 3 26  ? 254.664 173.196 222.755 1.00 31.02 ? 26   PRO A O   1 
ATOM   1695 C CB  . PRO C 3 26  ? 252.601 173.023 225.487 1.00 30.56 ? 26   PRO A CB  1 
ATOM   1696 C CG  . PRO C 3 26  ? 252.976 174.477 225.600 1.00 30.71 ? 26   PRO A CG  1 
ATOM   1697 C CD  . PRO C 3 26  ? 254.451 174.456 225.974 1.00 31.52 ? 26   PRO A CD  1 
ATOM   1698 N N   . ALA C 3 27  ? 252.958 171.715 222.697 1.00 32.26 ? 27   ALA A N   1 
ATOM   1699 C CA  . ALA C 3 27  ? 252.793 171.722 221.245 1.00 32.86 ? 27   ALA A CA  1 
ATOM   1700 C C   . ALA C 3 27  ? 251.671 172.677 220.875 1.00 33.03 ? 27   ALA A C   1 
ATOM   1701 O O   . ALA C 3 27  ? 250.900 173.089 221.739 1.00 33.76 ? 27   ALA A O   1 
ATOM   1702 C CB  . ALA C 3 27  ? 252.503 170.317 220.740 1.00 32.84 ? 27   ALA A CB  1 
ATOM   1703 N N   . TYR C 3 28  ? 251.584 173.052 219.607 1.00 33.64 ? 28   TYR A N   1 
ATOM   1704 C CA  . TYR C 3 28  ? 250.486 173.903 219.165 1.00 34.30 ? 28   TYR A CA  1 
ATOM   1705 C C   . TYR C 3 28  ? 249.823 173.360 217.912 1.00 35.49 ? 28   TYR A C   1 
ATOM   1706 O O   . TYR C 3 28  ? 250.479 172.762 217.058 1.00 35.77 ? 28   TYR A O   1 
ATOM   1707 C CB  . TYR C 3 28  ? 250.969 175.335 218.942 1.00 35.21 ? 28   TYR A CB  1 
ATOM   1708 C CG  . TYR C 3 28  ? 251.360 176.027 220.220 1.00 34.44 ? 28   TYR A CG  1 
ATOM   1709 C CD1 . TYR C 3 28  ? 252.635 175.868 220.740 1.00 33.26 ? 28   TYR A CD1 1 
ATOM   1710 C CD2 . TYR C 3 28  ? 250.435 176.815 220.880 1.00 34.91 ? 28   TYR A CD2 1 
ATOM   1711 C CE1 . TYR C 3 28  ? 252.981 176.495 221.919 1.00 33.02 ? 28   TYR A CE1 1 
ATOM   1712 C CE2 . TYR C 3 28  ? 250.780 177.443 222.056 1.00 34.57 ? 28   TYR A CE2 1 
ATOM   1713 C CZ  . TYR C 3 28  ? 252.046 177.285 222.576 1.00 33.58 ? 28   TYR A CZ  1 
ATOM   1714 O OH  . TYR C 3 28  ? 252.388 177.912 223.752 1.00 33.03 ? 28   TYR A OH  1 
ATOM   1715 N N   . THR C 3 29  ? 248.520 173.590 217.795 1.00 36.23 ? 29   THR A N   1 
ATOM   1716 C CA  . THR C 3 29  ? 247.792 173.193 216.599 1.00 37.87 ? 29   THR A CA  1 
ATOM   1717 C C   . THR C 3 29  ? 246.977 174.338 216.020 1.00 39.19 ? 29   THR A C   1 
ATOM   1718 O O   . THR C 3 29  ? 246.832 175.393 216.639 1.00 39.08 ? 29   THR A O   1 
ATOM   1719 C CB  . THR C 3 29  ? 246.868 171.997 216.869 1.00 37.46 ? 29   THR A CB  1 
ATOM   1720 O OG1 . THR C 3 29  ? 246.355 171.525 215.618 1.00 38.30 ? 29   THR A OG1 1 
ATOM   1721 C CG2 . THR C 3 29  ? 245.710 172.400 217.781 1.00 36.68 ? 29   THR A CG2 1 
ATOM   1722 N N   . ASN C 3 30  ? 246.438 174.111 214.828 1.00 40.53 ? 30   ASN A N   1 
ATOM   1723 C CA  . ASN C 3 30  ? 245.654 175.113 214.117 1.00 42.05 ? 30   ASN A CA  1 
ATOM   1724 C C   . ASN C 3 30  ? 244.160 174.865 214.259 1.00 42.87 ? 30   ASN A C   1 
ATOM   1725 O O   . ASN C 3 30  ? 243.621 173.925 213.673 1.00 43.07 ? 30   ASN A O   1 
ATOM   1726 C CB  . ASN C 3 30  ? 246.052 175.141 212.649 1.00 43.36 ? 30   ASN A CB  1 
ATOM   1727 N N   . SER C 3 31  ? 243.494 175.701 215.046 1.00 43.39 ? 31   SER A N   1 
ATOM   1728 C CA  . SER C 3 31  ? 242.050 175.589 215.200 1.00 43.18 ? 31   SER A CA  1 
ATOM   1729 C C   . SER C 3 31  ? 241.388 176.442 214.138 1.00 44.92 ? 31   SER A C   1 
ATOM   1730 O O   . SER C 3 31  ? 241.364 177.671 214.236 1.00 45.72 ? 31   SER A O   1 
ATOM   1731 C CB  . SER C 3 31  ? 241.616 176.028 216.578 1.00 41.98 ? 31   SER A CB  1 
ATOM   1732 O OG  . SER C 3 31  ? 240.222 175.978 216.702 1.00 42.40 ? 31   SER A OG  1 
ATOM   1733 N N   . PHE C 3 32  ? 240.907 175.788 213.092 1.00 45.03 ? 32   PHE A N   1 
ATOM   1734 C CA  . PHE C 3 32  ? 240.498 176.487 211.887 1.00 44.19 ? 32   PHE A CA  1 
ATOM   1735 C C   . PHE C 3 32  ? 239.261 177.344 212.103 1.00 47.10 ? 32   PHE A C   1 
ATOM   1736 O O   . PHE C 3 32  ? 239.349 178.569 212.148 1.00 46.73 ? 32   PHE A O   1 
ATOM   1737 C CB  . PHE C 3 32  ? 240.231 175.468 210.782 1.00 45.31 ? 32   PHE A CB  1 
ATOM   1738 N N   . THR C 3 33  ? 238.113 176.703 212.279 1.00 45.48 ? 33   THR A N   1 
ATOM   1739 C CA  . THR C 3 33  ? 236.861 177.434 212.440 1.00 46.05 ? 33   THR A CA  1 
ATOM   1740 C C   . THR C 3 33  ? 236.022 176.866 213.575 1.00 45.56 ? 33   THR A C   1 
ATOM   1741 O O   . THR C 3 33  ? 234.917 176.374 213.348 1.00 45.18 ? 33   THR A O   1 
ATOM   1742 C CB  . THR C 3 33  ? 236.035 177.394 211.142 1.00 46.54 ? 33   THR A CB  1 
ATOM   1743 N N   . ARG C 3 34  ? 236.558 176.893 214.790 1.00 44.72 ? 34   ARG A N   1 
ATOM   1744 C CA  . ARG C 3 34  ? 235.885 176.256 215.916 1.00 42.80 ? 34   ARG A CA  1 
ATOM   1745 C C   . ARG C 3 34  ? 235.822 177.174 217.126 1.00 42.24 ? 34   ARG A C   1 
ATOM   1746 O O   . ARG C 3 34  ? 236.490 178.204 217.169 1.00 43.27 ? 34   ARG A O   1 
ATOM   1747 C CB  . ARG C 3 34  ? 236.580 174.960 216.294 1.00 40.45 ? 34   ARG A CB  1 
ATOM   1748 C CG  . ARG C 3 34  ? 236.682 173.963 215.160 1.00 41.81 ? 34   ARG A CG  1 
ATOM   1749 C CD  . ARG C 3 34  ? 237.062 172.613 215.630 1.00 39.35 ? 34   ARG A CD  1 
ATOM   1750 N NE  . ARG C 3 34  ? 235.931 171.912 216.212 1.00 38.37 ? 34   ARG A NE  1 
ATOM   1751 C CZ  . ARG C 3 34  ? 234.996 171.253 215.499 1.00 38.88 ? 34   ARG A CZ  1 
ATOM   1752 N NH1 . ARG C 3 34  ? 235.065 171.228 214.184 1.00 40.83 ? 34   ARG A NH1 1 
ATOM   1753 N NH2 . ARG C 3 34  ? 234.011 170.632 216.120 1.00 37.57 ? 34   ARG A NH2 1 
ATOM   1754 N N   . GLY C 3 35  ? 235.012 176.793 218.108 1.00 39.89 ? 35   GLY A N   1 
ATOM   1755 C CA  . GLY C 3 35  ? 234.895 177.550 219.351 1.00 39.24 ? 35   GLY A CA  1 
ATOM   1756 C C   . GLY C 3 35  ? 233.695 178.488 219.331 1.00 40.39 ? 35   GLY A C   1 
ATOM   1757 O O   . GLY C 3 35  ? 233.529 179.319 220.226 1.00 40.86 ? 35   GLY A O   1 
ATOM   1758 N N   . VAL C 3 36  ? 232.862 178.348 218.306 1.00 39.74 ? 36   VAL A N   1 
ATOM   1759 C CA  . VAL C 3 36  ? 231.647 179.141 218.178 1.00 40.48 ? 36   VAL A CA  1 
ATOM   1760 C C   . VAL C 3 36  ? 230.494 178.477 218.909 1.00 39.41 ? 36   VAL A C   1 
ATOM   1761 O O   . VAL C 3 36  ? 230.275 177.275 218.782 1.00 38.98 ? 36   VAL A O   1 
ATOM   1762 C CB  . VAL C 3 36  ? 231.282 179.355 216.698 1.00 42.07 ? 36   VAL A CB  1 
ATOM   1763 C CG1 . VAL C 3 36  ? 229.930 180.061 216.575 1.00 43.06 ? 36   VAL A CG1 1 
ATOM   1764 C CG2 . VAL C 3 36  ? 232.368 180.186 216.039 1.00 44.40 ? 36   VAL A CG2 1 
ATOM   1765 N N   . TYR C 3 37  ? 229.765 179.271 219.669 1.00 40.22 ? 37   TYR A N   1 
ATOM   1766 C CA  . TYR C 3 37  ? 228.627 178.806 220.444 1.00 39.74 ? 37   TYR A CA  1 
ATOM   1767 C C   . TYR C 3 37  ? 227.447 179.735 220.234 1.00 41.43 ? 37   TYR A C   1 
ATOM   1768 O O   . TYR C 3 37  ? 227.620 180.880 219.818 1.00 42.58 ? 37   TYR A O   1 
ATOM   1769 C CB  . TYR C 3 37  ? 229.001 178.742 221.921 1.00 38.25 ? 37   TYR A CB  1 
ATOM   1770 C CG  . TYR C 3 37  ? 229.432 180.070 222.451 1.00 38.62 ? 37   TYR A CG  1 
ATOM   1771 C CD1 . TYR C 3 37  ? 228.509 180.933 223.002 1.00 39.04 ? 37   TYR A CD1 1 
ATOM   1772 C CD2 . TYR C 3 37  ? 230.761 180.436 222.361 1.00 38.88 ? 37   TYR A CD2 1 
ATOM   1773 C CE1 . TYR C 3 37  ? 228.912 182.163 223.460 1.00 40.07 ? 37   TYR A CE1 1 
ATOM   1774 C CE2 . TYR C 3 37  ? 231.165 181.662 222.818 1.00 40.14 ? 37   TYR A CE2 1 
ATOM   1775 C CZ  . TYR C 3 37  ? 230.246 182.527 223.364 1.00 39.93 ? 37   TYR A CZ  1 
ATOM   1776 O OH  . TYR C 3 37  ? 230.645 183.759 223.811 1.00 41.38 ? 37   TYR A OH  1 
ATOM   1777 N N   . TYR C 3 38  ? 226.250 179.251 220.532 1.00 41.60 ? 38   TYR A N   1 
ATOM   1778 C CA  . TYR C 3 38  ? 225.063 180.087 220.427 1.00 44.12 ? 38   TYR A CA  1 
ATOM   1779 C C   . TYR C 3 38  ? 225.130 181.192 221.485 1.00 44.53 ? 38   TYR A C   1 
ATOM   1780 O O   . TYR C 3 38  ? 225.043 180.903 222.677 1.00 42.71 ? 38   TYR A O   1 
ATOM   1781 C CB  . TYR C 3 38  ? 223.802 179.242 220.620 1.00 43.24 ? 38   TYR A CB  1 
ATOM   1782 C CG  . TYR C 3 38  ? 223.541 178.275 219.489 1.00 44.73 ? 38   TYR A CG  1 
ATOM   1783 C CD1 . TYR C 3 38  ? 224.140 177.032 219.498 1.00 41.70 ? 38   TYR A CD1 1 
ATOM   1784 C CD2 . TYR C 3 38  ? 222.703 178.628 218.450 1.00 48.52 ? 38   TYR A CD2 1 
ATOM   1785 C CE1 . TYR C 3 38  ? 223.917 176.145 218.475 1.00 41.97 ? 38   TYR A CE1 1 
ATOM   1786 C CE2 . TYR C 3 38  ? 222.472 177.736 217.422 1.00 51.36 ? 38   TYR A CE2 1 
ATOM   1787 C CZ  . TYR C 3 38  ? 223.082 176.500 217.433 1.00 48.83 ? 38   TYR A CZ  1 
ATOM   1788 O OH  . TYR C 3 38  ? 222.860 175.614 216.410 1.00 51.71 ? 38   TYR A OH  1 
ATOM   1789 N N   . PRO C 3 39  ? 225.275 182.460 221.069 1.00 45.50 ? 39   PRO A N   1 
ATOM   1790 C CA  . PRO C 3 39  ? 225.583 183.610 221.905 1.00 46.72 ? 39   PRO A CA  1 
ATOM   1791 C C   . PRO C 3 39  ? 224.481 183.914 222.913 1.00 47.88 ? 39   PRO A C   1 
ATOM   1792 O O   . PRO C 3 39  ? 224.734 184.508 223.962 1.00 47.51 ? 39   PRO A O   1 
ATOM   1793 C CB  . PRO C 3 39  ? 225.731 184.738 220.874 1.00 47.98 ? 39   PRO A CB  1 
ATOM   1794 C CG  . PRO C 3 39  ? 224.920 184.282 219.673 1.00 49.41 ? 39   PRO A CG  1 
ATOM   1795 C CD  . PRO C 3 39  ? 225.053 182.775 219.655 1.00 47.17 ? 39   PRO A CD  1 
ATOM   1796 N N   . ASP C 3 40  ? 223.261 183.489 222.606 1.00 49.06 ? 40   ASP A N   1 
ATOM   1797 C CA  . ASP C 3 40  ? 222.132 183.706 223.499 1.00 50.68 ? 40   ASP A CA  1 
ATOM   1798 C C   . ASP C 3 40  ? 221.097 182.600 223.335 1.00 51.67 ? 40   ASP A C   1 
ATOM   1799 O O   . ASP C 3 40  ? 221.377 181.557 222.742 1.00 50.59 ? 40   ASP A O   1 
ATOM   1800 C CB  . ASP C 3 40  ? 221.512 185.091 223.274 1.00 52.04 ? 40   ASP A CB  1 
ATOM   1801 N N   . LYS C 3 41  ? 219.918 182.807 223.909 1.00 53.26 ? 41   LYS A N   1 
ATOM   1802 C CA  . LYS C 3 41  ? 218.880 181.786 223.918 1.00 54.57 ? 41   LYS A CA  1 
ATOM   1803 C C   . LYS C 3 41  ? 217.706 182.166 223.023 1.00 55.83 ? 41   LYS A C   1 
ATOM   1804 O O   . LYS C 3 41  ? 216.590 181.676 223.205 1.00 56.22 ? 41   LYS A O   1 
ATOM   1805 C CB  . LYS C 3 41  ? 218.416 181.541 225.353 1.00 52.82 ? 41   LYS A CB  1 
ATOM   1806 N N   . VAL C 3 42  ? 217.958 183.057 222.068 1.00 55.86 ? 42   VAL A N   1 
ATOM   1807 C CA  . VAL C 3 42  ? 216.929 183.498 221.136 1.00 57.10 ? 42   VAL A CA  1 
ATOM   1808 C C   . VAL C 3 42  ? 216.942 182.647 219.873 1.00 58.40 ? 42   VAL A C   1 
ATOM   1809 O O   . VAL C 3 42  ? 217.988 182.455 219.254 1.00 58.20 ? 42   VAL A O   1 
ATOM   1810 C CB  . VAL C 3 42  ? 217.147 184.977 220.769 1.00 57.59 ? 42   VAL A CB  1 
ATOM   1811 N N   . PHE C 3 43  ? 215.780 182.132 219.491 1.00 58.76 ? 43   PHE A N   1 
ATOM   1812 C CA  . PHE C 3 43  ? 215.695 181.315 218.289 1.00 60.32 ? 43   PHE A CA  1 
ATOM   1813 C C   . PHE C 3 43  ? 215.782 182.162 217.031 1.00 60.26 ? 43   PHE A C   1 
ATOM   1814 O O   . PHE C 3 43  ? 215.082 183.165 216.894 1.00 60.57 ? 43   PHE A O   1 
ATOM   1815 C CB  . PHE C 3 43  ? 214.397 180.514 218.254 1.00 61.18 ? 43   PHE A CB  1 
ATOM   1816 C CG  . PHE C 3 43  ? 214.294 179.637 217.039 1.00 61.49 ? 43   PHE A CG  1 
ATOM   1817 C CD1 . PHE C 3 43  ? 213.540 180.029 215.944 1.00 61.30 ? 43   PHE A CD1 1 
ATOM   1818 C CD2 . PHE C 3 43  ? 214.959 178.424 216.985 1.00 61.99 ? 43   PHE A CD2 1 
ATOM   1819 C CE1 . PHE C 3 43  ? 213.455 179.227 214.824 1.00 61.74 ? 43   PHE A CE1 1 
ATOM   1820 C CE2 . PHE C 3 43  ? 214.874 177.621 215.868 1.00 61.68 ? 43   PHE A CE2 1 
ATOM   1821 C CZ  . PHE C 3 43  ? 214.122 178.023 214.787 1.00 61.58 ? 43   PHE A CZ  1 
ATOM   1822 N N   . ARG C 3 44  ? 216.625 181.732 216.103 1.00 60.36 ? 44   ARG A N   1 
ATOM   1823 C CA  . ARG C 3 44  ? 216.761 182.381 214.808 1.00 61.15 ? 44   ARG A CA  1 
ATOM   1824 C C   . ARG C 3 44  ? 216.847 181.320 213.730 1.00 60.00 ? 44   ARG A C   1 
ATOM   1825 O O   . ARG C 3 44  ? 217.386 180.244 213.973 1.00 59.17 ? 44   ARG A O   1 
ATOM   1826 C CB  . ARG C 3 44  ? 218.012 183.242 214.765 1.00 59.64 ? 44   ARG A CB  1 
ATOM   1827 N N   . SER C 3 45  ? 216.340 181.620 212.540 1.00 60.60 ? 45   SER A N   1 
ATOM   1828 C CA  . SER C 3 45  ? 216.440 180.682 211.427 1.00 61.27 ? 45   SER A CA  1 
ATOM   1829 C C   . SER C 3 45  ? 216.486 181.399 210.088 1.00 62.46 ? 45   SER A C   1 
ATOM   1830 O O   . SER C 3 45  ? 215.993 182.520 209.955 1.00 61.60 ? 45   SER A O   1 
ATOM   1831 C CB  . SER C 3 45  ? 215.276 179.712 211.454 1.00 61.27 ? 45   SER A CB  1 
ATOM   1832 N N   . SER C 3 46  ? 217.080 180.739 209.097 1.00 61.06 ? 46   SER A N   1 
ATOM   1833 C CA  . SER C 3 46  ? 217.155 181.267 207.737 1.00 61.70 ? 46   SER A CA  1 
ATOM   1834 C C   . SER C 3 46  ? 217.626 182.716 207.731 1.00 62.14 ? 46   SER A C   1 
ATOM   1835 O O   . SER C 3 46  ? 216.993 183.581 207.124 1.00 62.28 ? 46   SER A O   1 
ATOM   1836 C CB  . SER C 3 46  ? 215.801 181.164 207.060 1.00 62.38 ? 46   SER A CB  1 
ATOM   1837 N N   . VAL C 3 47  ? 218.715 182.988 208.443 1.00 60.47 ? 47   VAL A N   1 
ATOM   1838 C CA  . VAL C 3 47  ? 219.183 184.361 208.592 1.00 61.55 ? 47   VAL A CA  1 
ATOM   1839 C C   . VAL C 3 47  ? 220.684 184.454 208.830 1.00 61.61 ? 47   VAL A C   1 
ATOM   1840 O O   . VAL C 3 47  ? 221.276 183.607 209.501 1.00 59.11 ? 47   VAL A O   1 
ATOM   1841 C CB  . VAL C 3 47  ? 218.424 185.041 209.756 1.00 61.69 ? 47   VAL A CB  1 
ATOM   1842 C CG1 . VAL C 3 47  ? 218.742 184.345 211.073 1.00 60.95 ? 47   VAL A CG1 1 
ATOM   1843 C CG2 . VAL C 3 47  ? 218.788 186.523 209.841 1.00 61.21 ? 47   VAL A CG2 1 
ATOM   1844 N N   . LEU C 3 48  ? 221.283 185.530 208.330 1.00 61.02 ? 48   LEU A N   1 
ATOM   1845 C CA  . LEU C 3 48  ? 222.665 185.857 208.649 1.00 60.45 ? 48   LEU A CA  1 
ATOM   1846 C C   . LEU C 3 48  ? 222.683 186.923 209.737 1.00 60.53 ? 48   LEU A C   1 
ATOM   1847 O O   . LEU C 3 48  ? 222.256 188.057 209.515 1.00 60.82 ? 48   LEU A O   1 
ATOM   1848 C CB  . LEU C 3 48  ? 223.400 186.362 207.402 1.00 61.02 ? 48   LEU A CB  1 
ATOM   1849 N N   . HIS C 3 49  ? 223.129 186.541 210.926 1.00 60.09 ? 49   HIS A N   1 
ATOM   1850 C CA  . HIS C 3 49  ? 223.062 187.420 212.088 1.00 59.25 ? 49   HIS A CA  1 
ATOM   1851 C C   . HIS C 3 49  ? 224.438 187.859 212.565 1.00 59.44 ? 49   HIS A C   1 
ATOM   1852 O O   . HIS C 3 49  ? 225.322 187.033 212.789 1.00 59.07 ? 49   HIS A O   1 
ATOM   1853 C CB  . HIS C 3 49  ? 222.327 186.726 213.237 1.00 59.82 ? 49   HIS A CB  1 
ATOM   1854 C CG  . HIS C 3 49  ? 222.280 187.535 214.490 1.00 59.36 ? 49   HIS A CG  1 
ATOM   1855 N ND1 . HIS C 3 49  ? 221.475 188.643 214.629 1.00 59.49 ? 49   HIS A ND1 1 
ATOM   1856 C CD2 . HIS C 3 49  ? 222.944 187.401 215.661 1.00 58.90 ? 49   HIS A CD2 1 
ATOM   1857 C CE1 . HIS C 3 49  ? 221.648 189.159 215.834 1.00 59.27 ? 49   HIS A CE1 1 
ATOM   1858 N NE2 . HIS C 3 49  ? 222.532 188.423 216.479 1.00 59.06 ? 49   HIS A NE2 1 
ATOM   1859 N N   . SER C 3 50  ? 224.613 189.165 212.724 1.00 58.76 ? 50   SER A N   1 
ATOM   1860 C CA  . SER C 3 50  ? 225.876 189.715 213.202 1.00 58.74 ? 50   SER A CA  1 
ATOM   1861 C C   . SER C 3 50  ? 225.853 189.899 214.712 1.00 58.39 ? 50   SER A C   1 
ATOM   1862 O O   . SER C 3 50  ? 224.958 190.549 215.255 1.00 57.91 ? 50   SER A O   1 
ATOM   1863 C CB  . SER C 3 50  ? 226.166 191.037 212.525 1.00 60.04 ? 50   SER A CB  1 
ATOM   1864 N N   . THR C 3 51  ? 226.841 189.323 215.388 1.00 57.37 ? 51   THR A N   1 
ATOM   1865 C CA  . THR C 3 51  ? 226.916 189.394 216.842 1.00 57.01 ? 51   THR A CA  1 
ATOM   1866 C C   . THR C 3 51  ? 228.328 189.720 217.317 1.00 55.45 ? 51   THR A C   1 
ATOM   1867 O O   . THR C 3 51  ? 229.309 189.455 216.621 1.00 55.44 ? 51   THR A O   1 
ATOM   1868 C CB  . THR C 3 51  ? 226.457 188.068 217.478 1.00 56.96 ? 51   THR A CB  1 
ATOM   1869 N N   . GLN C 3 52  ? 228.424 190.280 218.518 1.00 54.16 ? 52   GLN A N   1 
ATOM   1870 C CA  . GLN C 3 52  ? 229.716 190.582 219.124 1.00 53.49 ? 52   GLN A CA  1 
ATOM   1871 C C   . GLN C 3 52  ? 229.820 189.941 220.499 1.00 51.59 ? 52   GLN A C   1 
ATOM   1872 O O   . GLN C 3 52  ? 229.009 190.219 221.383 1.00 50.60 ? 52   GLN A O   1 
ATOM   1873 C CB  . GLN C 3 52  ? 229.913 192.095 219.233 1.00 54.16 ? 52   GLN A CB  1 
ATOM   1874 N N   . ASP C 3 53  ? 230.797 189.056 220.663 1.00 50.14 ? 53   ASP A N   1 
ATOM   1875 C CA  . ASP C 3 53  ? 230.960 188.330 221.919 1.00 47.81 ? 53   ASP A CA  1 
ATOM   1876 C C   . ASP C 3 53  ? 232.347 187.708 222.011 1.00 46.89 ? 53   ASP A C   1 
ATOM   1877 O O   . ASP C 3 53  ? 233.164 187.851 221.100 1.00 47.40 ? 53   ASP A O   1 
ATOM   1878 C CB  . ASP C 3 53  ? 229.879 187.250 222.067 1.00 46.98 ? 53   ASP A CB  1 
ATOM   1879 N N   . LEU C 3 54  ? 232.606 187.008 223.106 1.00 45.39 ? 54   LEU A N   1 
ATOM   1880 C CA  . LEU C 3 54  ? 233.885 186.340 223.295 1.00 44.39 ? 54   LEU A CA  1 
ATOM   1881 C C   . LEU C 3 54  ? 233.907 184.987 222.599 1.00 43.37 ? 54   LEU A C   1 
ATOM   1882 O O   . LEU C 3 54  ? 233.241 184.046 223.023 1.00 42.86 ? 54   LEU A O   1 
ATOM   1883 C CB  . LEU C 3 54  ? 234.154 186.139 224.792 1.00 42.84 ? 54   LEU A CB  1 
ATOM   1884 C CG  . LEU C 3 54  ? 234.209 187.405 225.655 1.00 43.94 ? 54   LEU A CG  1 
ATOM   1885 C CD1 . LEU C 3 54  ? 234.323 186.997 227.119 1.00 40.65 ? 54   LEU A CD1 1 
ATOM   1886 C CD2 . LEU C 3 54  ? 235.402 188.255 225.237 1.00 44.43 ? 54   LEU A CD2 1 
ATOM   1887 N N   . PHE C 3 55  ? 234.676 184.899 221.522 1.00 43.36 ? 55   PHE A N   1 
ATOM   1888 C CA  . PHE C 3 55  ? 234.764 183.680 220.727 1.00 43.63 ? 55   PHE A CA  1 
ATOM   1889 C C   . PHE C 3 55  ? 236.215 183.303 220.504 1.00 43.27 ? 55   PHE A C   1 
ATOM   1890 O O   . PHE C 3 55  ? 237.094 184.163 220.537 1.00 43.07 ? 55   PHE A O   1 
ATOM   1891 C CB  . PHE C 3 55  ? 234.103 183.852 219.362 1.00 45.82 ? 55   PHE A CB  1 
ATOM   1892 C CG  . PHE C 3 55  ? 232.625 184.119 219.371 1.00 45.79 ? 55   PHE A CG  1 
ATOM   1893 C CD1 . PHE C 3 55  ? 232.140 185.403 219.199 1.00 47.18 ? 55   PHE A CD1 1 
ATOM   1894 C CD2 . PHE C 3 55  ? 231.718 183.085 219.528 1.00 43.79 ? 55   PHE A CD2 1 
ATOM   1895 C CE1 . PHE C 3 55  ? 230.784 185.650 219.177 1.00 47.70 ? 55   PHE A CE1 1 
ATOM   1896 C CE2 . PHE C 3 55  ? 230.357 183.328 219.513 1.00 43.48 ? 55   PHE A CE2 1 
ATOM   1897 C CZ  . PHE C 3 55  ? 229.891 184.612 219.334 1.00 46.44 ? 55   PHE A CZ  1 
ATOM   1898 N N   . LEU C 3 56  ? 236.469 182.028 220.250 1.00 42.43 ? 56   LEU A N   1 
ATOM   1899 C CA  . LEU C 3 56  ? 237.806 181.609 219.861 1.00 42.60 ? 56   LEU A CA  1 
ATOM   1900 C C   . LEU C 3 56  ? 238.097 182.160 218.461 1.00 43.91 ? 56   LEU A C   1 
ATOM   1901 O O   . LEU C 3 56  ? 237.307 181.931 217.546 1.00 45.08 ? 56   LEU A O   1 
ATOM   1902 C CB  . LEU C 3 56  ? 237.895 180.076 219.832 1.00 41.19 ? 56   LEU A CB  1 
ATOM   1903 C CG  . LEU C 3 56  ? 239.299 179.465 219.621 1.00 40.34 ? 56   LEU A CG  1 
ATOM   1904 C CD1 . LEU C 3 56  ? 240.151 179.696 220.863 1.00 37.09 ? 56   LEU A CD1 1 
ATOM   1905 C CD2 . LEU C 3 56  ? 239.163 177.978 219.328 1.00 38.77 ? 56   LEU A CD2 1 
ATOM   1906 N N   . PRO C 3 57  ? 239.194 182.903 218.271 1.00 44.44 ? 57   PRO A N   1 
ATOM   1907 C CA  . PRO C 3 57  ? 239.656 183.420 216.996 1.00 46.30 ? 57   PRO A CA  1 
ATOM   1908 C C   . PRO C 3 57  ? 239.846 182.282 216.010 1.00 46.31 ? 57   PRO A C   1 
ATOM   1909 O O   . PRO C 3 57  ? 240.291 181.201 216.392 1.00 45.73 ? 57   PRO A O   1 
ATOM   1910 C CB  . PRO C 3 57  ? 240.993 184.072 217.370 1.00 46.60 ? 57   PRO A CB  1 
ATOM   1911 C CG  . PRO C 3 57  ? 240.844 184.434 218.825 1.00 45.75 ? 57   PRO A CG  1 
ATOM   1912 C CD  . PRO C 3 57  ? 240.003 183.325 219.420 1.00 43.80 ? 57   PRO A CD  1 
ATOM   1913 N N   . PHE C 3 58  ? 239.509 182.517 214.747 1.00 47.80 ? 58   PHE A N   1 
ATOM   1914 C CA  . PHE C 3 58  ? 239.673 181.480 213.733 1.00 48.23 ? 58   PHE A CA  1 
ATOM   1915 C C   . PHE C 3 58  ? 241.125 181.352 213.289 1.00 47.77 ? 58   PHE A C   1 
ATOM   1916 O O   . PHE C 3 58  ? 241.855 182.342 213.216 1.00 48.41 ? 58   PHE A O   1 
ATOM   1917 C CB  . PHE C 3 58  ? 238.766 181.750 212.532 1.00 49.14 ? 58   PHE A CB  1 
ATOM   1918 C CG  . PHE C 3 58  ? 237.314 181.376 212.745 1.00 49.06 ? 58   PHE A CG  1 
ATOM   1919 C CD1 . PHE C 3 58  ? 236.830 180.977 213.992 1.00 48.17 ? 58   PHE A CD1 1 
ATOM   1920 C CD2 . PHE C 3 58  ? 236.429 181.402 211.681 1.00 49.50 ? 58   PHE A CD2 1 
ATOM   1921 C CE1 . PHE C 3 58  ? 235.512 180.615 214.152 1.00 48.37 ? 58   PHE A CE1 1 
ATOM   1922 C CE2 . PHE C 3 58  ? 235.109 181.042 211.846 1.00 50.52 ? 58   PHE A CE2 1 
ATOM   1923 C CZ  . PHE C 3 58  ? 234.651 180.646 213.080 1.00 49.88 ? 58   PHE A CZ  1 
ATOM   1924 N N   . PHE C 3 59  ? 241.535 180.120 212.996 1.00 47.17 ? 59   PHE A N   1 
ATOM   1925 C CA  . PHE C 3 59  ? 242.892 179.812 212.560 1.00 46.83 ? 59   PHE A CA  1 
ATOM   1926 C C   . PHE C 3 59  ? 243.919 180.263 213.588 1.00 46.70 ? 59   PHE A C   1 
ATOM   1927 O O   . PHE C 3 59  ? 244.945 180.850 213.243 1.00 46.83 ? 59   PHE A O   1 
ATOM   1928 C CB  . PHE C 3 59  ? 243.170 180.450 211.200 1.00 47.99 ? 59   PHE A CB  1 
ATOM   1929 C CG  . PHE C 3 59  ? 242.229 179.974 210.129 1.00 47.92 ? 59   PHE A CG  1 
ATOM   1930 C CD1 . PHE C 3 59  ? 241.096 180.697 209.815 1.00 48.76 ? 59   PHE A CD1 1 
ATOM   1931 C CD2 . PHE C 3 59  ? 242.474 178.800 209.438 1.00 46.81 ? 59   PHE A CD2 1 
ATOM   1932 C CE1 . PHE C 3 59  ? 240.221 180.259 208.841 1.00 48.76 ? 59   PHE A CE1 1 
ATOM   1933 C CE2 . PHE C 3 59  ? 241.604 178.360 208.459 1.00 46.80 ? 59   PHE A CE2 1 
ATOM   1934 C CZ  . PHE C 3 59  ? 240.475 179.091 208.164 1.00 47.18 ? 59   PHE A CZ  1 
ATOM   1935 N N   . SER C 3 60  ? 243.626 179.989 214.855 1.00 46.06 ? 60   SER A N   1 
ATOM   1936 C CA  . SER C 3 60  ? 244.490 180.380 215.963 1.00 45.69 ? 60   SER A CA  1 
ATOM   1937 C C   . SER C 3 60  ? 245.410 179.244 216.412 1.00 43.10 ? 60   SER A C   1 
ATOM   1938 O O   . SER C 3 60  ? 245.171 178.076 216.093 1.00 42.62 ? 60   SER A O   1 
ATOM   1939 C CB  . SER C 3 60  ? 243.638 180.840 217.127 1.00 44.91 ? 60   SER A CB  1 
ATOM   1940 N N   . ASN C 3 61  ? 246.442 179.599 217.196 1.00 42.57 ? 61   ASN A N   1 
ATOM   1941 C CA  . ASN C 3 61  ? 247.368 178.634 217.793 1.00 40.74 ? 61   ASN A CA  1 
ATOM   1942 C C   . ASN C 3 61  ? 246.859 178.166 219.154 1.00 39.12 ? 61   ASN A C   1 
ATOM   1943 O O   . ASN C 3 61  ? 246.930 178.902 220.143 1.00 38.39 ? 61   ASN A O   1 
ATOM   1944 C CB  . ASN C 3 61  ? 248.767 179.231 217.919 1.00 41.60 ? 61   ASN A CB  1 
ATOM   1945 C CG  . ASN C 3 61  ? 249.618 179.039 216.671 1.00 43.23 ? 61   ASN A CG  1 
ATOM   1946 O OD1 . ASN C 3 61  ? 249.681 177.934 216.113 1.00 42.02 ? 61   ASN A OD1 1 
ATOM   1947 N ND2 . ASN C 3 61  ? 250.271 180.096 216.239 1.00 46.00 ? 61   ASN A ND2 1 
ATOM   1948 N N   . VAL C 3 62  ? 246.333 176.942 219.193 1.00 37.80 ? 62   VAL A N   1 
ATOM   1949 C CA  . VAL C 3 62  ? 245.757 176.340 220.395 1.00 35.88 ? 62   VAL A CA  1 
ATOM   1950 C C   . VAL C 3 62  ? 246.767 175.410 221.055 1.00 34.63 ? 62   VAL A C   1 
ATOM   1951 O O   . VAL C 3 62  ? 247.419 174.613 220.380 1.00 34.98 ? 62   VAL A O   1 
ATOM   1952 C CB  . VAL C 3 62  ? 244.463 175.588 220.040 1.00 35.16 ? 62   VAL A CB  1 
ATOM   1953 C CG1 . VAL C 3 62  ? 243.920 174.879 221.244 1.00 33.63 ? 62   VAL A CG1 1 
ATOM   1954 C CG2 . VAL C 3 62  ? 243.437 176.585 219.529 1.00 37.87 ? 62   VAL A CG2 1 
ATOM   1955 N N   . THR C 3 63  ? 246.941 175.557 222.365 1.00 33.27 ? 63   THR A N   1 
ATOM   1956 C CA  . THR C 3 63  ? 247.967 174.805 223.075 1.00 32.82 ? 63   THR A CA  1 
ATOM   1957 C C   . THR C 3 63  ? 247.570 173.344 223.216 1.00 31.28 ? 63   THR A C   1 
ATOM   1958 O O   . THR C 3 63  ? 246.463 173.027 223.646 1.00 30.78 ? 63   THR A O   1 
ATOM   1959 C CB  . THR C 3 63  ? 248.241 175.407 224.462 1.00 31.86 ? 63   THR A CB  1 
ATOM   1960 O OG1 . THR C 3 63  ? 248.552 176.799 224.329 1.00 33.15 ? 63   THR A OG1 1 
ATOM   1961 C CG2 . THR C 3 63  ? 249.429 174.709 225.085 1.00 32.43 ? 63   THR A CG2 1 
ATOM   1962 N N   . TRP C 3 64  ? 248.477 172.459 222.834 1.00 31.34 ? 64   TRP A N   1 
ATOM   1963 C CA  . TRP C 3 64  ? 248.236 171.024 222.813 1.00 30.24 ? 64   TRP A CA  1 
ATOM   1964 C C   . TRP C 3 64  ? 249.026 170.277 223.888 1.00 30.48 ? 64   TRP A C   1 
ATOM   1965 O O   . TRP C 3 64  ? 250.260 170.253 223.877 1.00 31.95 ? 64   TRP A O   1 
ATOM   1966 C CB  . TRP C 3 64  ? 248.577 170.492 221.421 1.00 31.81 ? 64   TRP A CB  1 
ATOM   1967 C CG  . TRP C 3 64  ? 248.493 169.012 221.255 1.00 31.10 ? 64   TRP A CG  1 
ATOM   1968 C CD1 . TRP C 3 64  ? 247.812 168.117 222.019 1.00 31.41 ? 64   TRP A CD1 1 
ATOM   1969 C CD2 . TRP C 3 64  ? 249.127 168.244 220.212 1.00 31.93 ? 64   TRP A CD2 1 
ATOM   1970 N NE1 . TRP C 3 64  ? 247.986 166.851 221.527 1.00 30.63 ? 64   TRP A NE1 1 
ATOM   1971 C CE2 . TRP C 3 64  ? 248.785 166.911 220.423 1.00 31.36 ? 64   TRP A CE2 1 
ATOM   1972 C CE3 . TRP C 3 64  ? 249.944 168.579 219.129 1.00 32.47 ? 64   TRP A CE3 1 
ATOM   1973 C CZ2 . TRP C 3 64  ? 249.232 165.900 219.591 1.00 31.68 ? 64   TRP A CZ2 1 
ATOM   1974 C CZ3 . TRP C 3 64  ? 250.394 167.567 218.294 1.00 30.81 ? 64   TRP A CZ3 1 
ATOM   1975 C CH2 . TRP C 3 64  ? 250.047 166.261 218.520 1.00 32.36 ? 64   TRP A CH2 1 
ATOM   1976 N N   . PHE C 3 65  ? 248.298 169.666 224.819 1.00 29.87 ? 65   PHE A N   1 
ATOM   1977 C CA  . PHE C 3 65  ? 248.891 168.906 225.912 1.00 29.24 ? 65   PHE A CA  1 
ATOM   1978 C C   . PHE C 3 65  ? 248.568 167.426 225.778 1.00 29.05 ? 65   PHE A C   1 
ATOM   1979 O O   . PHE C 3 65  ? 247.491 167.060 225.309 1.00 29.08 ? 65   PHE A O   1 
ATOM   1980 C CB  . PHE C 3 65  ? 248.353 169.384 227.256 1.00 28.41 ? 65   PHE A CB  1 
ATOM   1981 C CG  . PHE C 3 65  ? 248.695 170.783 227.602 1.00 28.81 ? 65   PHE A CG  1 
ATOM   1982 C CD1 . PHE C 3 65  ? 249.909 171.089 228.183 1.00 29.25 ? 65   PHE A CD1 1 
ATOM   1983 C CD2 . PHE C 3 65  ? 247.797 171.800 227.363 1.00 29.31 ? 65   PHE A CD2 1 
ATOM   1984 C CE1 . PHE C 3 65  ? 250.220 172.388 228.513 1.00 28.43 ? 65   PHE A CE1 1 
ATOM   1985 C CE2 . PHE C 3 65  ? 248.101 173.095 227.692 1.00 29.47 ? 65   PHE A CE2 1 
ATOM   1986 C CZ  . PHE C 3 65  ? 249.316 173.390 228.267 1.00 27.87 ? 65   PHE A CZ  1 
ATOM   1987 N N   . HIS C 3 66  ? 249.469 166.574 226.245 1.00 29.22 ? 66   HIS A N   1 
ATOM   1988 C CA  . HIS C 3 66  ? 249.211 165.139 226.257 1.00 28.60 ? 66   HIS A CA  1 
ATOM   1989 C C   . HIS C 3 66  ? 248.897 164.655 227.669 1.00 28.70 ? 66   HIS A C   1 
ATOM   1990 O O   . HIS C 3 66  ? 249.371 165.236 228.645 1.00 28.42 ? 66   HIS A O   1 
ATOM   1991 C CB  . HIS C 3 66  ? 250.415 164.376 225.703 1.00 28.24 ? 66   HIS A CB  1 
ATOM   1992 C CG  . HIS C 3 66  ? 250.684 164.657 224.266 1.00 29.61 ? 66   HIS A CG  1 
ATOM   1993 N ND1 . HIS C 3 66  ? 251.304 165.813 223.837 1.00 31.14 ? 66   HIS A ND1 1 
ATOM   1994 C CD2 . HIS C 3 66  ? 250.424 163.935 223.153 1.00 28.57 ? 66   HIS A CD2 1 
ATOM   1995 C CE1 . HIS C 3 66  ? 251.412 165.788 222.522 1.00 30.70 ? 66   HIS A CE1 1 
ATOM   1996 N NE2 . HIS C 3 66  ? 250.888 164.659 222.084 1.00 28.63 ? 66   HIS A NE2 1 
ATOM   1997 N N   . ALA C 3 67  ? 248.109 163.580 227.771 1.00 29.29 ? 67   ALA A N   1 
ATOM   1998 C CA  . ALA C 3 67  ? 247.764 162.950 229.046 1.00 28.62 ? 67   ALA A CA  1 
ATOM   1999 C C   . ALA C 3 67  ? 248.158 161.476 229.017 1.00 29.10 ? 67   ALA A C   1 
ATOM   2000 O O   . ALA C 3 67  ? 248.659 160.975 228.008 1.00 28.56 ? 67   ALA A O   1 
ATOM   2001 C CB  . ALA C 3 67  ? 246.270 163.104 229.336 1.00 27.78 ? 67   ALA A CB  1 
ATOM   2002 N N   . ARG C 3 78  ? 253.135 158.915 231.922 1.00 32.31 ? 78   ARG A N   1 
ATOM   2003 C CA  . ARG C 3 78  ? 253.376 160.242 231.371 1.00 32.27 ? 78   ARG A CA  1 
ATOM   2004 C C   . ARG C 3 78  ? 252.059 160.990 231.153 1.00 30.97 ? 78   ARG A C   1 
ATOM   2005 O O   . ARG C 3 78  ? 251.190 160.525 230.411 1.00 29.96 ? 78   ARG A O   1 
ATOM   2006 C CB  . ARG C 3 78  ? 254.138 160.145 230.041 1.00 34.39 ? 78   ARG A CB  1 
ATOM   2007 C CG  . ARG C 3 78  ? 254.451 161.508 229.338 1.00 36.47 ? 78   ARG A CG  1 
ATOM   2008 C CD  . ARG C 3 78  ? 255.112 161.330 227.994 1.00 39.64 ? 78   ARG A CD  1 
ATOM   2009 N NE  . ARG C 3 78  ? 255.274 162.620 227.286 1.00 42.18 ? 78   ARG A NE  1 
ATOM   2010 C CZ  . ARG C 3 78  ? 255.717 162.785 226.003 1.00 42.41 ? 78   ARG A CZ  1 
ATOM   2011 N NH1 . ARG C 3 78  ? 256.055 161.752 225.255 1.00 43.01 ? 78   ARG A NH1 1 
ATOM   2012 N NH2 . ARG C 3 78  ? 255.808 164.000 225.497 1.00 43.65 ? 78   ARG A NH2 1 
ATOM   2013 N N   . PHE C 3 79  ? 251.932 162.163 231.780 1.00 30.14 ? 79   PHE A N   1 
ATOM   2014 C CA  . PHE C 3 79  ? 250.790 163.052 231.580 1.00 29.35 ? 79   PHE A CA  1 
ATOM   2015 C C   . PHE C 3 79  ? 251.153 164.486 231.937 1.00 28.48 ? 79   PHE A C   1 
ATOM   2016 O O   . PHE C 3 79  ? 251.919 164.728 232.869 1.00 28.53 ? 79   PHE A O   1 
ATOM   2017 C CB  . PHE C 3 79  ? 249.597 162.599 232.427 1.00 28.71 ? 79   PHE A CB  1 
ATOM   2018 C CG  . PHE C 3 79  ? 249.918 162.450 233.887 1.00 29.03 ? 79   PHE A CG  1 
ATOM   2019 C CD1 . PHE C 3 79  ? 249.782 163.521 234.760 1.00 27.90 ? 79   PHE A CD1 1 
ATOM   2020 C CD2 . PHE C 3 79  ? 250.359 161.234 234.391 1.00 29.84 ? 79   PHE A CD2 1 
ATOM   2021 C CE1 . PHE C 3 79  ? 250.083 163.380 236.100 1.00 28.23 ? 79   PHE A CE1 1 
ATOM   2022 C CE2 . PHE C 3 79  ? 250.659 161.092 235.731 1.00 30.05 ? 79   PHE A CE2 1 
ATOM   2023 C CZ  . PHE C 3 79  ? 250.522 162.166 236.585 1.00 28.91 ? 79   PHE A CZ  1 
ATOM   2024 N N   . ASP C 3 80  ? 250.553 165.434 231.226 1.00 28.14 ? 80   ASP A N   1 
ATOM   2025 C CA  . ASP C 3 80  ? 250.724 166.849 231.522 1.00 26.88 ? 80   ASP A CA  1 
ATOM   2026 C C   . ASP C 3 80  ? 249.438 167.450 232.065 1.00 26.57 ? 80   ASP A C   1 
ATOM   2027 O O   . ASP C 3 80  ? 248.424 167.492 231.371 1.00 26.63 ? 80   ASP A O   1 
ATOM   2028 C CB  . ASP C 3 80  ? 251.155 167.617 230.269 1.00 27.56 ? 80   ASP A CB  1 
ATOM   2029 C CG  . ASP C 3 80  ? 252.577 167.295 229.812 1.00 28.18 ? 80   ASP A CG  1 
ATOM   2030 O OD1 . ASP C 3 80  ? 253.425 167.096 230.649 1.00 27.26 ? 80   ASP A OD1 1 
ATOM   2031 O OD2 . ASP C 3 80  ? 252.801 167.269 228.624 1.00 28.19 ? 80   ASP A OD2 1 
ATOM   2032 N N   . ASN C 3 81  ? 249.479 167.910 233.307 1.00 25.97 ? 81   ASN A N   1 
ATOM   2033 C CA  . ASN C 3 81  ? 248.311 168.519 233.926 1.00 25.68 ? 81   ASN A CA  1 
ATOM   2034 C C   . ASN C 3 81  ? 248.659 169.786 234.715 1.00 25.27 ? 81   ASN A C   1 
ATOM   2035 O O   . ASN C 3 81  ? 248.359 169.867 235.906 1.00 25.78 ? 81   ASN A O   1 
ATOM   2036 C CB  . ASN C 3 81  ? 247.613 167.507 234.812 1.00 24.82 ? 81   ASN A CB  1 
ATOM   2037 C CG  . ASN C 3 81  ? 248.488 167.024 235.925 1.00 26.10 ? 81   ASN A CG  1 
ATOM   2038 O OD1 . ASN C 3 81  ? 249.718 167.180 235.880 1.00 26.45 ? 81   ASN A OD1 1 
ATOM   2039 N ND2 . ASN C 3 81  ? 247.883 166.446 236.930 1.00 25.71 ? 81   ASN A ND2 1 
ATOM   2040 N N   . PRO C 3 82  ? 249.294 170.776 234.072 1.00 24.49 ? 82   PRO A N   1 
ATOM   2041 C CA  . PRO C 3 82  ? 249.759 172.031 234.634 1.00 24.25 ? 82   PRO A CA  1 
ATOM   2042 C C   . PRO C 3 82  ? 248.605 172.973 234.923 1.00 24.71 ? 82   PRO A C   1 
ATOM   2043 O O   . PRO C 3 82  ? 247.497 172.782 234.421 1.00 24.52 ? 82   PRO A O   1 
ATOM   2044 C CB  . PRO C 3 82  ? 250.638 172.583 233.510 1.00 24.43 ? 82   PRO A CB  1 
ATOM   2045 C CG  . PRO C 3 82  ? 250.018 172.025 232.255 1.00 25.71 ? 82   PRO A CG  1 
ATOM   2046 C CD  . PRO C 3 82  ? 249.569 170.637 232.637 1.00 25.23 ? 82   PRO A CD  1 
ATOM   2047 N N   . VAL C 3 83  ? 248.873 174.006 235.710 1.00 24.29 ? 83   VAL A N   1 
ATOM   2048 C CA  . VAL C 3 83  ? 247.885 175.048 235.931 1.00 23.71 ? 83   VAL A CA  1 
ATOM   2049 C C   . VAL C 3 83  ? 247.997 176.103 234.842 1.00 24.08 ? 83   VAL A C   1 
ATOM   2050 O O   . VAL C 3 83  ? 249.075 176.640 234.593 1.00 25.59 ? 83   VAL A O   1 
ATOM   2051 C CB  . VAL C 3 83  ? 248.073 175.695 237.311 1.00 23.68 ? 83   VAL A CB  1 
ATOM   2052 C CG1 . VAL C 3 83  ? 247.062 176.812 237.498 1.00 25.07 ? 83   VAL A CG1 1 
ATOM   2053 C CG2 . VAL C 3 83  ? 247.910 174.641 238.389 1.00 24.19 ? 83   VAL A CG2 1 
ATOM   2054 N N   . LEU C 3 84  ? 246.884 176.368 234.177 1.00 24.28 ? 84   LEU A N   1 
ATOM   2055 C CA  . LEU C 3 84  ? 246.841 177.292 233.056 1.00 24.69 ? 84   LEU A CA  1 
ATOM   2056 C C   . LEU C 3 84  ? 246.033 178.528 233.428 1.00 24.67 ? 84   LEU A C   1 
ATOM   2057 O O   . LEU C 3 84  ? 245.161 178.452 234.290 1.00 25.13 ? 84   LEU A O   1 
ATOM   2058 C CB  . LEU C 3 84  ? 246.207 176.575 231.858 1.00 24.35 ? 84   LEU A CB  1 
ATOM   2059 C CG  . LEU C 3 84  ? 246.881 175.259 231.456 1.00 24.30 ? 84   LEU A CG  1 
ATOM   2060 C CD1 . LEU C 3 84  ? 246.077 174.603 230.358 1.00 26.34 ? 84   LEU A CD1 1 
ATOM   2061 C CD2 . LEU C 3 84  ? 248.302 175.529 230.999 1.00 25.86 ? 84   LEU A CD2 1 
ATOM   2062 N N   . PRO C 3 85  ? 246.301 179.673 232.804 1.00 24.82 ? 85   PRO A N   1 
ATOM   2063 C CA  . PRO C 3 85  ? 245.564 180.908 232.955 1.00 24.96 ? 85   PRO A CA  1 
ATOM   2064 C C   . PRO C 3 85  ? 244.164 180.768 232.384 1.00 25.61 ? 85   PRO A C   1 
ATOM   2065 O O   . PRO C 3 85  ? 243.947 180.017 231.436 1.00 25.94 ? 85   PRO A O   1 
ATOM   2066 C CB  . PRO C 3 85  ? 246.418 181.908 232.168 1.00 25.84 ? 85   PRO A CB  1 
ATOM   2067 C CG  . PRO C 3 85  ? 247.211 181.066 231.188 1.00 25.85 ? 85   PRO A CG  1 
ATOM   2068 C CD  . PRO C 3 85  ? 247.441 179.744 231.894 1.00 25.15 ? 85   PRO A CD  1 
ATOM   2069 N N   . PHE C 3 86  ? 243.221 181.500 232.959 1.00 25.96 ? 86   PHE A N   1 
ATOM   2070 C CA  . PHE C 3 86  ? 241.842 181.509 232.488 1.00 26.21 ? 86   PHE A CA  1 
ATOM   2071 C C   . PHE C 3 86  ? 241.596 182.691 231.554 1.00 26.85 ? 86   PHE A C   1 
ATOM   2072 O O   . PHE C 3 86  ? 240.758 182.627 230.654 1.00 27.44 ? 86   PHE A O   1 
ATOM   2073 C CB  . PHE C 3 86  ? 240.884 181.580 233.677 1.00 26.38 ? 86   PHE A CB  1 
ATOM   2074 C CG  . PHE C 3 86  ? 239.440 181.381 233.332 1.00 26.62 ? 86   PHE A CG  1 
ATOM   2075 C CD1 . PHE C 3 86  ? 238.603 182.467 233.146 1.00 27.48 ? 86   PHE A CD1 1 
ATOM   2076 C CD2 . PHE C 3 86  ? 238.909 180.110 233.215 1.00 25.33 ? 86   PHE A CD2 1 
ATOM   2077 C CE1 . PHE C 3 86  ? 237.271 182.287 232.843 1.00 27.52 ? 86   PHE A CE1 1 
ATOM   2078 C CE2 . PHE C 3 86  ? 237.577 179.928 232.912 1.00 26.52 ? 86   PHE A CE2 1 
ATOM   2079 C CZ  . PHE C 3 86  ? 236.759 181.018 232.725 1.00 27.24 ? 86   PHE A CZ  1 
ATOM   2080 N N   . ASN C 3 87  ? 242.323 183.778 231.793 1.00 26.52 ? 87   ASN A N   1 
ATOM   2081 C CA  . ASN C 3 87  ? 242.171 185.015 231.037 1.00 26.83 ? 87   ASN A CA  1 
ATOM   2082 C C   . ASN C 3 87  ? 240.721 185.496 231.013 1.00 27.08 ? 87   ASN A C   1 
ATOM   2083 O O   . ASN C 3 87  ? 240.113 185.689 232.065 1.00 27.27 ? 87   ASN A O   1 
ATOM   2084 C CB  . ASN C 3 87  ? 242.729 184.857 229.633 1.00 27.14 ? 87   ASN A CB  1 
ATOM   2085 C CG  . ASN C 3 87  ? 244.213 184.578 229.632 1.00 26.85 ? 87   ASN A CG  1 
ATOM   2086 O OD1 . ASN C 3 87  ? 244.918 184.906 230.595 1.00 26.02 ? 87   ASN A OD1 1 
ATOM   2087 N ND2 . ASN C 3 87  ? 244.699 183.992 228.570 1.00 26.94 ? 87   ASN A ND2 1 
ATOM   2088 N N   . ASP C 3 88  ? 240.176 185.706 229.816 1.00 27.52 ? 88   ASP A N   1 
ATOM   2089 C CA  . ASP C 3 88  ? 238.824 186.239 229.675 1.00 27.58 ? 88   ASP A CA  1 
ATOM   2090 C C   . ASP C 3 88  ? 237.813 185.153 229.340 1.00 28.79 ? 88   ASP A C   1 
ATOM   2091 O O   . ASP C 3 88  ? 236.660 185.443 229.025 1.00 30.65 ? 88   ASP A O   1 
ATOM   2092 C CB  . ASP C 3 88  ? 238.786 187.315 228.588 1.00 28.61 ? 88   ASP A CB  1 
ATOM   2093 N N   . GLY C 3 89  ? 238.252 183.905 229.394 1.00 28.39 ? 89   GLY A N   1 
ATOM   2094 C CA  . GLY C 3 89  ? 237.409 182.775 229.035 1.00 29.23 ? 89   GLY A CA  1 
ATOM   2095 C C   . GLY C 3 89  ? 238.244 181.700 228.361 1.00 29.38 ? 89   GLY A C   1 
ATOM   2096 O O   . GLY C 3 89  ? 239.246 181.994 227.706 1.00 30.29 ? 89   GLY A O   1 
ATOM   2097 N N   . VAL C 3 90  ? 237.833 180.450 228.530 1.00 28.39 ? 90   VAL A N   1 
ATOM   2098 C CA  . VAL C 3 90  ? 238.632 179.331 228.053 1.00 27.99 ? 90   VAL A CA  1 
ATOM   2099 C C   . VAL C 3 90  ? 237.912 178.407 227.090 1.00 27.78 ? 90   VAL A C   1 
ATOM   2100 O O   . VAL C 3 90  ? 236.817 177.920 227.368 1.00 27.83 ? 90   VAL A O   1 
ATOM   2101 C CB  . VAL C 3 90  ? 239.125 178.501 229.252 1.00 27.78 ? 90   VAL A CB  1 
ATOM   2102 C CG1 . VAL C 3 90  ? 239.877 177.272 228.778 1.00 28.48 ? 90   VAL A CG1 1 
ATOM   2103 C CG2 . VAL C 3 90  ? 240.020 179.356 230.114 1.00 27.52 ? 90   VAL A CG2 1 
ATOM   2104 N N   . TYR C 3 91  ? 238.575 178.112 225.983 1.00 28.60 ? 91   TYR A N   1 
ATOM   2105 C CA  . TYR C 3 91  ? 238.126 177.064 225.083 1.00 28.69 ? 91   TYR A CA  1 
ATOM   2106 C C   . TYR C 3 91  ? 238.878 175.787 225.402 1.00 28.97 ? 91   TYR A C   1 
ATOM   2107 O O   . TYR C 3 91  ? 240.105 175.746 225.326 1.00 29.33 ? 91   TYR A O   1 
ATOM   2108 C CB  . TYR C 3 91  ? 238.353 177.445 223.627 1.00 30.71 ? 91   TYR A CB  1 
ATOM   2109 C CG  . TYR C 3 91  ? 238.203 176.273 222.682 1.00 31.12 ? 91   TYR A CG  1 
ATOM   2110 C CD1 . TYR C 3 91  ? 239.339 175.653 222.196 1.00 31.87 ? 91   TYR A CD1 1 
ATOM   2111 C CD2 . TYR C 3 91  ? 236.951 175.813 222.308 1.00 30.45 ? 91   TYR A CD2 1 
ATOM   2112 C CE1 . TYR C 3 91  ? 239.232 174.584 221.344 1.00 32.09 ? 91   TYR A CE1 1 
ATOM   2113 C CE2 . TYR C 3 91  ? 236.845 174.734 221.447 1.00 29.56 ? 91   TYR A CE2 1 
ATOM   2114 C CZ  . TYR C 3 91  ? 237.986 174.124 220.968 1.00 29.64 ? 91   TYR A CZ  1 
ATOM   2115 O OH  . TYR C 3 91  ? 237.901 173.051 220.115 1.00 30.96 ? 91   TYR A OH  1 
ATOM   2116 N N   . PHE C 3 92  ? 238.152 174.747 225.768 1.00 28.29 ? 92   PHE A N   1 
ATOM   2117 C CA  . PHE C 3 92  ? 238.778 173.493 226.154 1.00 27.87 ? 92   PHE A CA  1 
ATOM   2118 C C   . PHE C 3 92  ? 238.255 172.354 225.306 1.00 27.91 ? 92   PHE A C   1 
ATOM   2119 O O   . PHE C 3 92  ? 237.052 172.224 225.103 1.00 27.45 ? 92   PHE A O   1 
ATOM   2120 C CB  . PHE C 3 92  ? 238.501 173.190 227.625 1.00 26.02 ? 92   PHE A CB  1 
ATOM   2121 C CG  . PHE C 3 92  ? 239.161 171.941 228.124 1.00 25.25 ? 92   PHE A CG  1 
ATOM   2122 C CD1 . PHE C 3 92  ? 240.396 171.998 228.742 1.00 24.55 ? 92   PHE A CD1 1 
ATOM   2123 C CD2 . PHE C 3 92  ? 238.554 170.707 227.971 1.00 25.85 ? 92   PHE A CD2 1 
ATOM   2124 C CE1 . PHE C 3 92  ? 241.009 170.852 229.198 1.00 24.51 ? 92   PHE A CE1 1 
ATOM   2125 C CE2 . PHE C 3 92  ? 239.166 169.558 228.424 1.00 25.54 ? 92   PHE A CE2 1 
ATOM   2126 C CZ  . PHE C 3 92  ? 240.396 169.632 229.038 1.00 24.38 ? 92   PHE A CZ  1 
ATOM   2127 N N   . ALA C 3 93  ? 239.149 171.510 224.827 1.00 27.48 ? 93   ALA A N   1 
ATOM   2128 C CA  . ALA C 3 93  ? 238.719 170.365 224.047 1.00 27.29 ? 93   ALA A CA  1 
ATOM   2129 C C   . ALA C 3 93  ? 239.541 169.148 224.396 1.00 27.84 ? 93   ALA A C   1 
ATOM   2130 O O   . ALA C 3 93  ? 240.724 169.256 224.704 1.00 27.45 ? 93   ALA A O   1 
ATOM   2131 C CB  . ALA C 3 93  ? 238.829 170.665 222.563 1.00 28.98 ? 93   ALA A CB  1 
ATOM   2132 N N   . SER C 3 94  ? 238.935 167.977 224.307 1.00 27.83 ? 94   SER A N   1 
ATOM   2133 C CA  . SER C 3 94  ? 239.677 166.755 224.558 1.00 27.85 ? 94   SER A CA  1 
ATOM   2134 C C   . SER C 3 94  ? 239.323 165.648 223.586 1.00 28.75 ? 94   SER A C   1 
ATOM   2135 O O   . SER C 3 94  ? 238.181 165.524 223.142 1.00 28.73 ? 94   SER A O   1 
ATOM   2136 C CB  . SER C 3 94  ? 239.439 166.283 225.974 1.00 26.44 ? 94   SER A CB  1 
ATOM   2137 O OG  . SER C 3 94  ? 238.085 166.001 226.195 1.00 26.86 ? 94   SER A OG  1 
ATOM   2138 N N   . ILE C 3 95  ? 240.320 164.828 223.276 1.00 28.29 ? 95   ILE A N   1 
ATOM   2139 C CA  . ILE C 3 95  ? 240.131 163.646 222.455 1.00 27.89 ? 95   ILE A CA  1 
ATOM   2140 C C   . ILE C 3 95  ? 240.620 162.419 223.205 1.00 28.67 ? 95   ILE A C   1 
ATOM   2141 O O   . ILE C 3 95  ? 241.794 162.329 223.569 1.00 29.38 ? 95   ILE A O   1 
ATOM   2142 C CB  . ILE C 3 95  ? 240.878 163.771 221.117 1.00 28.06 ? 95   ILE A CB  1 
ATOM   2143 C CG1 . ILE C 3 95  ? 240.373 164.997 220.353 1.00 29.33 ? 95   ILE A CG1 1 
ATOM   2144 C CG2 . ILE C 3 95  ? 240.674 162.503 220.299 1.00 30.28 ? 95   ILE A CG2 1 
ATOM   2145 C CD1 . ILE C 3 95  ? 241.200 165.359 219.141 1.00 31.76 ? 95   ILE A CD1 1 
ATOM   2146 N N   . GLU C 3 96  ? 239.716 161.483 223.456 1.00 29.33 ? 96   GLU A N   1 
ATOM   2147 C CA  . GLU C 3 96  ? 240.065 160.298 224.226 1.00 28.96 ? 96   GLU A CA  1 
ATOM   2148 C C   . GLU C 3 96  ? 239.123 159.136 223.958 1.00 29.65 ? 96   GLU A C   1 
ATOM   2149 O O   . GLU C 3 96  ? 238.011 159.322 223.467 1.00 29.94 ? 96   GLU A O   1 
ATOM   2150 C CB  . GLU C 3 96  ? 240.067 160.629 225.713 1.00 27.66 ? 96   GLU A CB  1 
ATOM   2151 C CG  . GLU C 3 96  ? 238.739 161.112 226.232 1.00 28.18 ? 96   GLU A CG  1 
ATOM   2152 C CD  . GLU C 3 96  ? 238.768 161.418 227.682 1.00 26.96 ? 96   GLU A CD  1 
ATOM   2153 O OE1 . GLU C 3 96  ? 239.791 161.227 228.294 1.00 26.69 ? 96   GLU A OE1 1 
ATOM   2154 O OE2 . GLU C 3 96  ? 237.764 161.838 228.193 1.00 26.36 ? 96   GLU A OE2 1 
ATOM   2155 N N   . LYS C 3 97  ? 239.563 157.936 224.311 1.00 29.28 ? 97   LYS A N   1 
ATOM   2156 C CA  . LYS C 3 97  ? 238.726 156.751 224.183 1.00 29.04 ? 97   LYS A CA  1 
ATOM   2157 C C   . LYS C 3 97  ? 238.339 156.166 225.539 1.00 28.83 ? 97   LYS A C   1 
ATOM   2158 O O   . LYS C 3 97  ? 237.295 155.530 225.670 1.00 29.01 ? 97   LYS A O   1 
ATOM   2159 C CB  . LYS C 3 97  ? 239.437 155.692 223.341 1.00 31.21 ? 97   LYS A CB  1 
ATOM   2160 C CG  . LYS C 3 97  ? 238.612 154.439 223.069 1.00 31.89 ? 97   LYS A CG  1 
ATOM   2161 C CD  . LYS C 3 97  ? 239.330 153.506 222.100 1.00 32.60 ? 97   LYS A CD  1 
ATOM   2162 C CE  . LYS C 3 97  ? 238.518 152.246 221.837 1.00 35.26 ? 97   LYS A CE  1 
ATOM   2163 N NZ  . LYS C 3 97  ? 239.211 151.328 220.890 1.00 37.81 ? 97   LYS A NZ  1 
ATOM   2164 N N   . SER C 3 98  ? 239.207 156.338 226.535 1.00 28.32 ? 98   SER A N   1 
ATOM   2165 C CA  . SER C 3 98  ? 239.045 155.657 227.816 1.00 27.84 ? 98   SER A CA  1 
ATOM   2166 C C   . SER C 3 98  ? 238.541 156.558 228.945 1.00 27.46 ? 98   SER A C   1 
ATOM   2167 O O   . SER C 3 98  ? 238.536 156.150 230.106 1.00 28.00 ? 98   SER A O   1 
ATOM   2168 C CB  . SER C 3 98  ? 240.358 155.023 228.225 1.00 27.68 ? 98   SER A CB  1 
ATOM   2169 O OG  . SER C 3 98  ? 241.347 155.994 228.401 1.00 27.53 ? 98   SER A OG  1 
ATOM   2170 N N   . ASN C 3 99  ? 238.103 157.768 228.611 1.00 27.08 ? 99   ASN A N   1 
ATOM   2171 C CA  . ASN C 3 99  ? 237.556 158.686 229.612 1.00 26.38 ? 99   ASN A CA  1 
ATOM   2172 C C   . ASN C 3 99  ? 238.537 158.973 230.748 1.00 25.80 ? 99   ASN A C   1 
ATOM   2173 O O   . ASN C 3 99  ? 238.261 158.675 231.912 1.00 25.66 ? 99   ASN A O   1 
ATOM   2174 C CB  . ASN C 3 99  ? 236.252 158.147 230.165 1.00 25.19 ? 99   ASN A CB  1 
ATOM   2175 C CG  . ASN C 3 99  ? 235.222 157.948 229.096 1.00 26.33 ? 99   ASN A CG  1 
ATOM   2176 O OD1 . ASN C 3 99  ? 234.976 158.834 228.269 1.00 25.46 ? 99   ASN A OD1 1 
ATOM   2177 N ND2 . ASN C 3 99  ? 234.608 156.793 229.094 1.00 26.33 ? 99   ASN A ND2 1 
ATOM   2178 N N   . ILE C 3 100 ? 239.687 159.545 230.404 1.00 25.96 ? 100  ILE A N   1 
ATOM   2179 C CA  . ILE C 3 100 ? 240.716 159.869 231.382 1.00 25.58 ? 100  ILE A CA  1 
ATOM   2180 C C   . ILE C 3 100 ? 240.472 161.242 231.984 1.00 24.76 ? 100  ILE A C   1 
ATOM   2181 O O   . ILE C 3 100 ? 240.700 161.456 233.173 1.00 25.25 ? 100  ILE A O   1 
ATOM   2182 C CB  . ILE C 3 100 ? 242.120 159.811 230.758 1.00 25.01 ? 100  ILE A CB  1 
ATOM   2183 C CG1 . ILE C 3 100 ? 242.427 158.370 230.353 1.00 27.01 ? 100  ILE A CG1 1 
ATOM   2184 C CG2 . ILE C 3 100 ? 243.163 160.335 231.751 1.00 26.17 ? 100  ILE A CG2 1 
ATOM   2185 C CD1 . ILE C 3 100 ? 243.649 158.215 229.481 1.00 27.84 ? 100  ILE A CD1 1 
ATOM   2186 N N   . ILE C 3 101 ? 240.034 162.185 231.161 1.00 24.61 ? 101  ILE A N   1 
ATOM   2187 C CA  . ILE C 3 101 ? 239.764 163.529 231.658 1.00 24.08 ? 101  ILE A CA  1 
ATOM   2188 C C   . ILE C 3 101 ? 238.382 163.588 232.293 1.00 23.83 ? 101  ILE A C   1 
ATOM   2189 O O   . ILE C 3 101 ? 237.367 163.350 231.636 1.00 24.02 ? 101  ILE A O   1 
ATOM   2190 C CB  . ILE C 3 101 ? 239.889 164.566 230.532 1.00 23.36 ? 101  ILE A CB  1 
ATOM   2191 C CG1 . ILE C 3 101 ? 241.334 164.570 230.016 1.00 24.25 ? 101  ILE A CG1 1 
ATOM   2192 C CG2 . ILE C 3 101 ? 239.486 165.947 231.047 1.00 22.98 ? 101  ILE A CG2 1 
ATOM   2193 C CD1 . ILE C 3 101 ? 241.520 165.260 228.703 1.00 25.58 ? 101  ILE A CD1 1 
ATOM   2194 N N   . ARG C 3 102 ? 238.351 163.877 233.591 1.00 23.54 ? 102  ARG A N   1 
ATOM   2195 C CA  . ARG C 3 102 ? 237.110 163.799 234.348 1.00 22.86 ? 102  ARG A CA  1 
ATOM   2196 C C   . ARG C 3 102 ? 236.554 165.158 234.729 1.00 22.90 ? 102  ARG A C   1 
ATOM   2197 O O   . ARG C 3 102 ? 235.346 165.303 234.919 1.00 23.32 ? 102  ARG A O   1 
ATOM   2198 C CB  . ARG C 3 102 ? 237.311 162.986 235.613 1.00 22.78 ? 102  ARG A CB  1 
ATOM   2199 C CG  . ARG C 3 102 ? 237.771 161.562 235.393 1.00 24.27 ? 102  ARG A CG  1 
ATOM   2200 C CD  . ARG C 3 102 ? 236.761 160.742 234.667 1.00 23.76 ? 102  ARG A CD  1 
ATOM   2201 N NE  . ARG C 3 102 ? 237.172 159.353 234.581 1.00 23.84 ? 102  ARG A NE  1 
ATOM   2202 C CZ  . ARG C 3 102 ? 236.981 158.440 235.552 1.00 24.82 ? 102  ARG A CZ  1 
ATOM   2203 N NH1 . ARG C 3 102 ? 236.374 158.784 236.668 1.00 24.76 ? 102  ARG A NH1 1 
ATOM   2204 N NH2 . ARG C 3 102 ? 237.407 157.200 235.385 1.00 27.74 ? 102  ARG A NH2 1 
ATOM   2205 N N   . GLY C 3 103 ? 237.416 166.150 234.881 1.00 22.86 ? 103  GLY A N   1 
ATOM   2206 C CA  . GLY C 3 103 ? 236.917 167.427 235.366 1.00 22.62 ? 103  GLY A CA  1 
ATOM   2207 C C   . GLY C 3 103 ? 237.959 168.525 235.402 1.00 22.70 ? 103  GLY A C   1 
ATOM   2208 O O   . GLY C 3 103 ? 239.053 168.386 234.855 1.00 22.87 ? 103  GLY A O   1 
ATOM   2209 N N   . TRP C 3 104 ? 237.583 169.641 236.014 1.00 22.37 ? 104  TRP A N   1 
ATOM   2210 C CA  . TRP C 3 104 ? 238.429 170.819 236.071 1.00 22.34 ? 104  TRP A CA  1 
ATOM   2211 C C   . TRP C 3 104 ? 238.347 171.508 237.423 1.00 22.52 ? 104  TRP A C   1 
ATOM   2212 O O   . TRP C 3 104 ? 237.323 171.455 238.105 1.00 22.78 ? 104  TRP A O   1 
ATOM   2213 C CB  . TRP C 3 104 ? 238.011 171.828 235.008 1.00 22.71 ? 104  TRP A CB  1 
ATOM   2214 C CG  . TRP C 3 104 ? 237.916 171.274 233.642 1.00 21.54 ? 104  TRP A CG  1 
ATOM   2215 C CD1 . TRP C 3 104 ? 238.885 171.256 232.695 1.00 22.73 ? 104  TRP A CD1 1 
ATOM   2216 C CD2 . TRP C 3 104 ? 236.760 170.660 233.045 1.00 21.39 ? 104  TRP A CD2 1 
ATOM   2217 N NE1 . TRP C 3 104 ? 238.415 170.670 231.556 1.00 23.35 ? 104  TRP A NE1 1 
ATOM   2218 C CE2 . TRP C 3 104 ? 237.115 170.299 231.753 1.00 22.63 ? 104  TRP A CE2 1 
ATOM   2219 C CE3 . TRP C 3 104 ? 235.467 170.394 233.500 1.00 22.59 ? 104  TRP A CE3 1 
ATOM   2220 C CZ2 . TRP C 3 104 ? 236.226 169.678 230.897 1.00 23.48 ? 104  TRP A CZ2 1 
ATOM   2221 C CZ3 . TRP C 3 104 ? 234.575 169.773 232.646 1.00 21.88 ? 104  TRP A CZ3 1 
ATOM   2222 C CH2 . TRP C 3 104 ? 234.944 169.423 231.378 1.00 22.38 ? 104  TRP A CH2 1 
ATOM   2223 N N   . ILE C 3 105 ? 239.405 172.222 237.764 1.00 22.48 ? 105  ILE A N   1 
ATOM   2224 C CA  . ILE C 3 105 ? 239.399 173.107 238.917 1.00 22.65 ? 105  ILE A CA  1 
ATOM   2225 C C   . ILE C 3 105 ? 239.560 174.548 238.464 1.00 23.49 ? 105  ILE A C   1 
ATOM   2226 O O   . ILE C 3 105 ? 240.497 174.864 237.737 1.00 24.14 ? 105  ILE A O   1 
ATOM   2227 C CB  . ILE C 3 105 ? 240.539 172.765 239.886 1.00 23.33 ? 105  ILE A CB  1 
ATOM   2228 C CG1 . ILE C 3 105 ? 240.376 171.346 240.420 1.00 24.01 ? 105  ILE A CG1 1 
ATOM   2229 C CG2 . ILE C 3 105 ? 240.551 173.768 241.016 1.00 25.75 ? 105  ILE A CG2 1 
ATOM   2230 C CD1 . ILE C 3 105 ? 241.590 170.828 241.159 1.00 24.09 ? 105  ILE A CD1 1 
ATOM   2231 N N   . PHE C 3 106 ? 238.660 175.422 238.898 1.00 23.80 ? 106  PHE A N   1 
ATOM   2232 C CA  . PHE C 3 106 ? 238.754 176.836 238.548 1.00 24.21 ? 106  PHE A CA  1 
ATOM   2233 C C   . PHE C 3 106 ? 238.888 177.694 239.799 1.00 24.74 ? 106  PHE A C   1 
ATOM   2234 O O   . PHE C 3 106 ? 238.189 177.476 240.788 1.00 25.28 ? 106  PHE A O   1 
ATOM   2235 C CB  . PHE C 3 106 ? 237.518 177.279 237.768 1.00 23.96 ? 106  PHE A CB  1 
ATOM   2236 C CG  . PHE C 3 106 ? 237.326 176.592 236.458 1.00 23.62 ? 106  PHE A CG  1 
ATOM   2237 C CD1 . PHE C 3 106 ? 236.537 175.464 236.362 1.00 22.69 ? 106  PHE A CD1 1 
ATOM   2238 C CD2 . PHE C 3 106 ? 237.927 177.075 235.318 1.00 24.74 ? 106  PHE A CD2 1 
ATOM   2239 C CE1 . PHE C 3 106 ? 236.358 174.836 235.152 1.00 23.13 ? 106  PHE A CE1 1 
ATOM   2240 C CE2 . PHE C 3 106 ? 237.754 176.443 234.106 1.00 25.11 ? 106  PHE A CE2 1 
ATOM   2241 C CZ  . PHE C 3 106 ? 236.969 175.322 234.026 1.00 24.60 ? 106  PHE A CZ  1 
ATOM   2242 N N   . GLY C 3 107 ? 239.758 178.696 239.750 1.00 25.33 ? 107  GLY A N   1 
ATOM   2243 C CA  . GLY C 3 107 ? 239.926 179.590 240.893 1.00 25.98 ? 107  GLY A CA  1 
ATOM   2244 C C   . GLY C 3 107 ? 241.134 180.504 240.734 1.00 26.22 ? 107  GLY A C   1 
ATOM   2245 O O   . GLY C 3 107 ? 241.558 180.803 239.618 1.00 26.31 ? 107  GLY A O   1 
ATOM   2246 N N   . THR C 3 108 ? 241.667 180.969 241.859 1.00 26.30 ? 108  THR A N   1 
ATOM   2247 C CA  . THR C 3 108 ? 242.803 181.881 241.857 1.00 26.37 ? 108  THR A CA  1 
ATOM   2248 C C   . THR C 3 108 ? 244.024 181.232 242.494 1.00 26.59 ? 108  THR A C   1 
ATOM   2249 O O   . THR C 3 108 ? 244.914 180.747 241.795 1.00 26.52 ? 108  THR A O   1 
ATOM   2250 C CB  . THR C 3 108 ? 242.465 183.189 242.593 1.00 27.11 ? 108  THR A CB  1 
ATOM   2251 O OG1 . THR C 3 108 ? 242.036 182.893 243.929 1.00 27.42 ? 108  THR A OG1 1 
ATOM   2252 C CG2 . THR C 3 108 ? 241.358 183.914 241.864 1.00 27.60 ? 108  THR A CG2 1 
ATOM   2253 N N   . THR C 3 109 ? 244.064 181.226 243.821 1.00 26.31 ? 109  THR A N   1 
ATOM   2254 C CA  . THR C 3 109 ? 245.184 180.647 244.552 1.00 26.72 ? 109  THR A CA  1 
ATOM   2255 C C   . THR C 3 109 ? 245.052 179.132 244.661 1.00 27.21 ? 109  THR A C   1 
ATOM   2256 O O   . THR C 3 109 ? 246.032 178.433 244.914 1.00 27.74 ? 109  THR A O   1 
ATOM   2257 C CB  . THR C 3 109 ? 245.304 181.283 245.949 1.00 27.28 ? 109  THR A CB  1 
ATOM   2258 O OG1 . THR C 3 109 ? 244.107 181.042 246.697 1.00 27.34 ? 109  THR A OG1 1 
ATOM   2259 C CG2 . THR C 3 109 ? 245.511 182.782 245.815 1.00 26.42 ? 109  THR A CG2 1 
ATOM   2260 N N   . LEU C 3 110 ? 243.844 178.627 244.423 1.00 26.98 ? 110  LEU A N   1 
ATOM   2261 C CA  . LEU C 3 110 ? 243.576 177.192 244.410 1.00 27.08 ? 110  LEU A CA  1 
ATOM   2262 C C   . LEU C 3 110 ? 244.001 176.514 245.707 1.00 27.55 ? 110  LEU A C   1 
ATOM   2263 O O   . LEU C 3 110 ? 244.581 175.428 245.690 1.00 28.18 ? 110  LEU A O   1 
ATOM   2264 C CB  . LEU C 3 110 ? 244.291 176.535 243.219 1.00 26.35 ? 110  LEU A CB  1 
ATOM   2265 C CG  . LEU C 3 110 ? 243.986 177.139 241.825 1.00 26.31 ? 110  LEU A CG  1 
ATOM   2266 C CD1 . LEU C 3 110 ? 244.801 176.407 240.769 1.00 25.97 ? 110  LEU A CD1 1 
ATOM   2267 C CD2 . LEU C 3 110 ? 242.503 177.027 241.529 1.00 26.48 ? 110  LEU A CD2 1 
ATOM   2268 N N   . ASP C 3 111 ? 243.705 177.158 246.829 1.00 27.52 ? 111  ASP A N   1 
ATOM   2269 C CA  . ASP C 3 111 ? 243.995 176.608 248.146 1.00 27.62 ? 111  ASP A CA  1 
ATOM   2270 C C   . ASP C 3 111 ? 242.921 177.035 249.141 1.00 27.21 ? 111  ASP A C   1 
ATOM   2271 O O   . ASP C 3 111 ? 241.913 177.632 248.759 1.00 27.94 ? 111  ASP A O   1 
ATOM   2272 C CB  . ASP C 3 111 ? 245.377 177.052 248.628 1.00 27.80 ? 111  ASP A CB  1 
ATOM   2273 C CG  . ASP C 3 111 ? 245.477 178.545 248.800 1.00 27.77 ? 111  ASP A CG  1 
ATOM   2274 O OD1 . ASP C 3 111 ? 244.461 179.192 248.717 1.00 27.63 ? 111  ASP A OD1 1 
ATOM   2275 O OD2 . ASP C 3 111 ? 246.560 179.036 249.028 1.00 27.82 ? 111  ASP A OD2 1 
ATOM   2276 N N   . SER C 3 112 ? 243.143 176.731 250.416 1.00 27.63 ? 112  SER A N   1 
ATOM   2277 C CA  . SER C 3 112 ? 242.154 176.966 251.465 1.00 27.77 ? 112  SER A CA  1 
ATOM   2278 C C   . SER C 3 112 ? 241.888 178.441 251.746 1.00 27.73 ? 112  SER A C   1 
ATOM   2279 O O   . SER C 3 112 ? 241.031 178.765 252.567 1.00 27.66 ? 112  SER A O   1 
ATOM   2280 C CB  . SER C 3 112 ? 242.597 176.304 252.752 1.00 27.86 ? 112  SER A CB  1 
ATOM   2281 O OG  . SER C 3 112 ? 243.731 176.938 253.279 1.00 28.13 ? 112  SER A OG  1 
ATOM   2282 N N   . LYS C 3 113 ? 242.658 179.335 251.130 1.00 27.68 ? 113  LYS A N   1 
ATOM   2283 C CA  . LYS C 3 113 ? 242.515 180.758 251.408 1.00 27.80 ? 113  LYS A CA  1 
ATOM   2284 C C   . LYS C 3 113 ? 241.305 181.383 250.716 1.00 27.83 ? 113  LYS A C   1 
ATOM   2285 O O   . LYS C 3 113 ? 240.789 182.402 251.176 1.00 27.84 ? 113  LYS A O   1 
ATOM   2286 C CB  . LYS C 3 113 ? 243.779 181.519 251.003 1.00 27.71 ? 113  LYS A CB  1 
ATOM   2287 N N   . THR C 3 114 ? 240.883 180.815 249.588 1.00 27.44 ? 114  THR A N   1 
ATOM   2288 C CA  . THR C 3 114 ? 239.792 181.412 248.821 1.00 27.19 ? 114  THR A CA  1 
ATOM   2289 C C   . THR C 3 114 ? 238.786 180.366 248.368 1.00 27.20 ? 114  THR A C   1 
ATOM   2290 O O   . THR C 3 114 ? 239.058 179.169 248.411 1.00 27.08 ? 114  THR A O   1 
ATOM   2291 C CB  . THR C 3 114 ? 240.323 182.156 247.580 1.00 27.30 ? 114  THR A CB  1 
ATOM   2292 O OG1 . THR C 3 114 ? 240.806 181.204 246.624 1.00 27.03 ? 114  THR A OG1 1 
ATOM   2293 C CG2 . THR C 3 114 ? 241.459 183.094 247.964 1.00 27.00 ? 114  THR A CG2 1 
ATOM   2294 N N   . GLN C 3 115 ? 237.636 180.823 247.885 1.00 26.64 ? 115  GLN A N   1 
ATOM   2295 C CA  . GLN C 3 115 ? 236.654 179.914 247.310 1.00 26.28 ? 115  GLN A CA  1 
ATOM   2296 C C   . GLN C 3 115 ? 237.092 179.478 245.922 1.00 26.22 ? 115  GLN A C   1 
ATOM   2297 O O   . GLN C 3 115 ? 237.644 180.273 245.160 1.00 26.76 ? 115  GLN A O   1 
ATOM   2298 C CB  . GLN C 3 115 ? 235.278 180.575 247.228 1.00 25.67 ? 115  GLN A CB  1 
ATOM   2299 C CG  . GLN C 3 115 ? 234.641 180.864 248.565 1.00 25.66 ? 115  GLN A CG  1 
ATOM   2300 C CD  . GLN C 3 115 ? 233.288 181.525 248.414 1.00 25.67 ? 115  GLN A CD  1 
ATOM   2301 O OE1 . GLN C 3 115 ? 232.483 181.136 247.563 1.00 25.44 ? 115  GLN A OE1 1 
ATOM   2302 N NE2 . GLN C 3 115 ? 233.028 182.533 249.237 1.00 24.89 ? 115  GLN A NE2 1 
ATOM   2303 N N   . SER C 3 116 ? 236.816 178.227 245.579 1.00 25.50 ? 116  SER A N   1 
ATOM   2304 C CA  . SER C 3 116 ? 237.145 177.716 244.258 1.00 24.68 ? 116  SER A CA  1 
ATOM   2305 C C   . SER C 3 116 ? 236.082 176.756 243.750 1.00 24.28 ? 116  SER A C   1 
ATOM   2306 O O   . SER C 3 116 ? 235.315 176.184 244.525 1.00 24.64 ? 116  SER A O   1 
ATOM   2307 C CB  . SER C 3 116 ? 238.497 177.036 244.291 1.00 25.21 ? 116  SER A CB  1 
ATOM   2308 O OG  . SER C 3 116 ? 239.510 177.956 244.572 1.00 26.72 ? 116  SER A OG  1 
ATOM   2309 N N   . LEU C 3 117 ? 236.028 176.609 242.433 1.00 23.75 ? 117  LEU A N   1 
ATOM   2310 C CA  . LEU C 3 117 ? 235.023 175.794 241.768 1.00 23.69 ? 117  LEU A CA  1 
ATOM   2311 C C   . LEU C 3 117 ? 235.566 174.451 241.310 1.00 23.43 ? 117  LEU A C   1 
ATOM   2312 O O   . LEU C 3 117 ? 236.516 174.379 240.530 1.00 23.44 ? 117  LEU A O   1 
ATOM   2313 C CB  . LEU C 3 117 ? 234.458 176.577 240.578 1.00 24.03 ? 117  LEU A CB  1 
ATOM   2314 C CG  . LEU C 3 117 ? 233.571 175.820 239.594 1.00 22.84 ? 117  LEU A CG  1 
ATOM   2315 C CD1 . LEU C 3 117 ? 232.320 175.340 240.286 1.00 24.06 ? 117  LEU A CD1 1 
ATOM   2316 C CD2 . LEU C 3 117 ? 233.222 176.750 238.444 1.00 23.75 ? 117  LEU A CD2 1 
ATOM   2317 N N   . LEU C 3 118 ? 234.952 173.384 241.801 1.00 23.35 ? 118  LEU A N   1 
ATOM   2318 C CA  . LEU C 3 118 ? 235.358 172.030 241.460 1.00 22.82 ? 118  LEU A CA  1 
ATOM   2319 C C   . LEU C 3 118 ? 234.288 171.326 240.635 1.00 23.29 ? 118  LEU A C   1 
ATOM   2320 O O   . LEU C 3 118 ? 233.178 171.093 241.115 1.00 23.20 ? 118  LEU A O   1 
ATOM   2321 C CB  . LEU C 3 118 ? 235.627 171.241 242.751 1.00 23.25 ? 118  LEU A CB  1 
ATOM   2322 C CG  . LEU C 3 118 ? 235.998 169.761 242.593 1.00 22.70 ? 118  LEU A CG  1 
ATOM   2323 C CD1 . LEU C 3 118 ? 237.321 169.636 241.856 1.00 24.51 ? 118  LEU A CD1 1 
ATOM   2324 C CD2 . LEU C 3 118 ? 236.092 169.126 243.970 1.00 24.58 ? 118  LEU A CD2 1 
ATOM   2325 N N   . ILE C 3 119 ? 234.622 170.988 239.391 1.00 23.09 ? 119  ILE A N   1 
ATOM   2326 C CA  . ILE C 3 119 ? 233.700 170.274 238.511 1.00 22.25 ? 119  ILE A CA  1 
ATOM   2327 C C   . ILE C 3 119 ? 234.241 168.895 238.185 1.00 22.97 ? 119  ILE A C   1 
ATOM   2328 O O   . ILE C 3 119 ? 235.228 168.773 237.463 1.00 22.88 ? 119  ILE A O   1 
ATOM   2329 C CB  . ILE C 3 119 ? 233.473 171.040 237.191 1.00 21.28 ? 119  ILE A CB  1 
ATOM   2330 C CG1 . ILE C 3 119 ? 232.867 172.419 237.479 1.00 22.89 ? 119  ILE A CG1 1 
ATOM   2331 C CG2 . ILE C 3 119 ? 232.583 170.219 236.248 1.00 22.19 ? 119  ILE A CG2 1 
ATOM   2332 C CD1 . ILE C 3 119 ? 232.774 173.322 236.271 1.00 22.65 ? 119  ILE A CD1 1 
ATOM   2333 N N   . VAL C 3 120 ? 233.611 167.855 238.721 1.00 22.64 ? 120  VAL A N   1 
ATOM   2334 C CA  . VAL C 3 120 ? 234.099 166.498 238.499 1.00 21.56 ? 120  VAL A CA  1 
ATOM   2335 C C   . VAL C 3 120 ? 233.009 165.534 238.058 1.00 22.93 ? 120  VAL A C   1 
ATOM   2336 O O   . VAL C 3 120 ? 231.960 165.429 238.693 1.00 23.27 ? 120  VAL A O   1 
ATOM   2337 C CB  . VAL C 3 120 ? 234.767 165.954 239.773 1.00 21.42 ? 120  VAL A CB  1 
ATOM   2338 C CG1 . VAL C 3 120 ? 235.216 164.515 239.559 1.00 23.42 ? 120  VAL A CG1 1 
ATOM   2339 C CG2 . VAL C 3 120 ? 235.953 166.823 240.123 1.00 22.62 ? 120  VAL A CG2 1 
ATOM   2340 N N   . ASN C 3 121 ? 233.290 164.786 236.998 1.00 22.76 ? 121  ASN A N   1 
ATOM   2341 C CA  . ASN C 3 121 ? 232.396 163.731 236.544 1.00 23.05 ? 121  ASN A CA  1 
ATOM   2342 C C   . ASN C 3 121 ? 232.792 162.386 237.151 1.00 23.67 ? 121  ASN A C   1 
ATOM   2343 O O   . ASN C 3 121 ? 233.837 161.833 236.802 1.00 24.06 ? 121  ASN A O   1 
ATOM   2344 C CB  . ASN C 3 121 ? 232.410 163.632 235.030 1.00 21.31 ? 121  ASN A CB  1 
ATOM   2345 C CG  . ASN C 3 121 ? 231.755 164.792 234.357 1.00 23.28 ? 121  ASN A CG  1 
ATOM   2346 O OD1 . ASN C 3 121 ? 230.525 164.827 234.223 1.00 23.78 ? 121  ASN A OD1 1 
ATOM   2347 N ND2 . ASN C 3 121 ? 232.542 165.745 233.933 1.00 23.02 ? 121  ASN A ND2 1 
ATOM   2348 N N   . ASN C 3 122 ? 231.963 161.867 238.066 1.00 23.95 ? 122  ASN A N   1 
ATOM   2349 C CA  . ASN C 3 122 ? 232.200 160.560 238.675 1.00 24.12 ? 122  ASN A CA  1 
ATOM   2350 C C   . ASN C 3 122 ? 231.461 159.483 237.878 1.00 25.11 ? 122  ASN A C   1 
ATOM   2351 O O   . ASN C 3 122 ? 231.026 159.726 236.754 1.00 25.47 ? 122  ASN A O   1 
ATOM   2352 C CB  . ASN C 3 122 ? 231.839 160.564 240.170 1.00 24.02 ? 122  ASN A CB  1 
ATOM   2353 C CG  . ASN C 3 122 ? 230.338 160.442 240.497 1.00 24.87 ? 122  ASN A CG  1 
ATOM   2354 O OD1 . ASN C 3 122 ? 229.495 160.290 239.609 1.00 25.10 ? 122  ASN A OD1 1 
ATOM   2355 N ND2 . ASN C 3 122 ? 230.019 160.512 241.779 1.00 25.44 ? 122  ASN A ND2 1 
ATOM   2356 N N   . ALA C 3 123 ? 231.361 158.279 238.436 1.00 25.08 ? 123  ALA A N   1 
ATOM   2357 C CA  . ALA C 3 123 ? 230.802 157.127 237.734 1.00 25.47 ? 123  ALA A CA  1 
ATOM   2358 C C   . ALA C 3 123 ? 229.358 157.319 237.255 1.00 24.66 ? 123  ALA A C   1 
ATOM   2359 O O   . ALA C 3 123 ? 228.952 156.700 236.270 1.00 25.10 ? 123  ALA A O   1 
ATOM   2360 C CB  . ALA C 3 123 ? 230.862 155.917 238.635 1.00 26.46 ? 123  ALA A CB  1 
ATOM   2361 N N   . THR C 3 124 ? 228.559 158.103 237.980 1.00 25.01 ? 124  THR A N   1 
ATOM   2362 C CA  . THR C 3 124 ? 227.134 158.190 237.658 1.00 24.81 ? 124  THR A CA  1 
ATOM   2363 C C   . THR C 3 124 ? 226.600 159.614 237.484 1.00 24.95 ? 124  THR A C   1 
ATOM   2364 O O   . THR C 3 124 ? 225.550 159.811 236.871 1.00 24.99 ? 124  THR A O   1 
ATOM   2365 C CB  . THR C 3 124 ? 226.302 157.473 238.737 1.00 24.95 ? 124  THR A CB  1 
ATOM   2366 O OG1 . THR C 3 124 ? 226.464 158.142 239.999 1.00 25.36 ? 124  THR A OG1 1 
ATOM   2367 C CG2 . THR C 3 124 ? 226.762 156.025 238.871 1.00 26.38 ? 124  THR A CG2 1 
ATOM   2368 N N   . ASN C 3 125 ? 227.284 160.597 238.060 1.00 24.67 ? 125  ASN A N   1 
ATOM   2369 C CA  . ASN C 3 125 ? 226.788 161.972 238.095 1.00 24.18 ? 125  ASN A CA  1 
ATOM   2370 C C   . ASN C 3 125 ? 227.910 162.998 238.017 1.00 23.79 ? 125  ASN A C   1 
ATOM   2371 O O   . ASN C 3 125 ? 229.058 162.706 238.355 1.00 24.42 ? 125  ASN A O   1 
ATOM   2372 C CB  . ASN C 3 125 ? 225.974 162.211 239.350 1.00 24.06 ? 125  ASN A CB  1 
ATOM   2373 C CG  . ASN C 3 125 ? 224.718 161.414 239.386 1.00 24.78 ? 125  ASN A CG  1 
ATOM   2374 O OD1 . ASN C 3 125 ? 224.652 160.359 240.028 1.00 26.33 ? 125  ASN A OD1 1 
ATOM   2375 N ND2 . ASN C 3 125 ? 223.710 161.892 238.706 1.00 24.89 ? 125  ASN A ND2 1 
ATOM   2376 N N   . VAL C 3 126 ? 227.558 164.223 237.642 1.00 23.88 ? 126  VAL A N   1 
ATOM   2377 C CA  . VAL C 3 126 ? 228.520 165.316 237.696 1.00 23.79 ? 126  VAL A CA  1 
ATOM   2378 C C   . VAL C 3 126 ? 228.310 166.119 238.962 1.00 23.81 ? 126  VAL A C   1 
ATOM   2379 O O   . VAL C 3 126 ? 227.191 166.524 239.280 1.00 23.54 ? 126  VAL A O   1 
ATOM   2380 C CB  . VAL C 3 126 ? 228.404 166.243 236.469 1.00 23.75 ? 126  VAL A CB  1 
ATOM   2381 C CG1 . VAL C 3 126 ? 227.041 166.913 236.415 1.00 23.93 ? 126  VAL A CG1 1 
ATOM   2382 C CG2 . VAL C 3 126 ? 229.513 167.288 236.520 1.00 24.01 ? 126  VAL A CG2 1 
ATOM   2383 N N   . VAL C 3 127 ? 229.390 166.333 239.693 1.00 23.43 ? 127  VAL A N   1 
ATOM   2384 C CA  . VAL C 3 127 ? 229.324 167.059 240.946 1.00 22.85 ? 127  VAL A CA  1 
ATOM   2385 C C   . VAL C 3 127 ? 230.014 168.403 240.841 1.00 23.46 ? 127  VAL A C   1 
ATOM   2386 O O   . VAL C 3 127 ? 231.215 168.480 240.582 1.00 23.37 ? 127  VAL A O   1 
ATOM   2387 C CB  . VAL C 3 127 ? 229.978 166.236 242.063 1.00 22.82 ? 127  VAL A CB  1 
ATOM   2388 C CG1 . VAL C 3 127 ? 229.934 167.000 243.375 1.00 23.00 ? 127  VAL A CG1 1 
ATOM   2389 C CG2 . VAL C 3 127 ? 229.256 164.916 242.185 1.00 25.41 ? 127  VAL A CG2 1 
ATOM   2390 N N   . ILE C 3 128 ? 229.248 169.464 241.041 1.00 22.76 ? 128  ILE A N   1 
ATOM   2391 C CA  . ILE C 3 128 ? 229.784 170.809 240.966 1.00 22.24 ? 128  ILE A CA  1 
ATOM   2392 C C   . ILE C 3 128 ? 229.668 171.509 242.309 1.00 22.76 ? 128  ILE A C   1 
ATOM   2393 O O   . ILE C 3 128 ? 228.568 171.725 242.817 1.00 22.83 ? 128  ILE A O   1 
ATOM   2394 C CB  . ILE C 3 128 ? 229.062 171.615 239.877 1.00 22.08 ? 128  ILE A CB  1 
ATOM   2395 C CG1 . ILE C 3 128 ? 229.246 170.904 238.522 1.00 23.20 ? 128  ILE A CG1 1 
ATOM   2396 C CG2 . ILE C 3 128 ? 229.591 173.024 239.843 1.00 23.64 ? 128  ILE A CG2 1 
ATOM   2397 C CD1 . ILE C 3 128 ? 228.542 171.557 237.351 1.00 22.91 ? 128  ILE A CD1 1 
ATOM   2398 N N   . LYS C 3 129 ? 230.807 171.850 242.895 1.00 22.98 ? 129  LYS A N   1 
ATOM   2399 C CA  . LYS C 3 129 ? 230.812 172.466 244.215 1.00 22.86 ? 129  LYS A CA  1 
ATOM   2400 C C   . LYS C 3 129 ? 231.701 173.692 244.277 1.00 23.68 ? 129  LYS A C   1 
ATOM   2401 O O   . LYS C 3 129 ? 232.740 173.756 243.619 1.00 23.74 ? 129  LYS A O   1 
ATOM   2402 C CB  . LYS C 3 129 ? 231.269 171.463 245.272 1.00 22.86 ? 129  LYS A CB  1 
ATOM   2403 C CG  . LYS C 3 129 ? 230.280 170.350 245.555 1.00 22.31 ? 129  LYS A CG  1 
ATOM   2404 C CD  . LYS C 3 129 ? 230.868 169.306 246.494 1.00 21.69 ? 129  LYS A CD  1 
ATOM   2405 C CE  . LYS C 3 129 ? 230.915 169.805 247.934 1.00 20.97 ? 129  LYS A CE  1 
ATOM   2406 N NZ  . LYS C 3 129 ? 231.293 168.721 248.877 1.00 20.89 ? 129  LYS A NZ  1 
ATOM   2407 N N   . VAL C 3 130 ? 231.314 174.646 245.111 1.00 24.13 ? 130  VAL A N   1 
ATOM   2408 C CA  . VAL C 3 130 ? 232.159 175.797 245.386 1.00 24.15 ? 130  VAL A CA  1 
ATOM   2409 C C   . VAL C 3 130 ? 232.422 175.900 246.880 1.00 24.92 ? 130  VAL A C   1 
ATOM   2410 O O   . VAL C 3 130 ? 231.492 176.101 247.668 1.00 25.02 ? 130  VAL A O   1 
ATOM   2411 C CB  . VAL C 3 130 ? 231.503 177.083 244.876 1.00 23.98 ? 130  VAL A CB  1 
ATOM   2412 C CG1 . VAL C 3 130 ? 232.405 178.283 245.138 1.00 24.59 ? 130  VAL A CG1 1 
ATOM   2413 C CG2 . VAL C 3 130 ? 231.218 176.923 243.401 1.00 24.67 ? 130  VAL A CG2 1 
ATOM   2414 N N   . CYS C 3 131 ? 233.690 175.728 247.262 1.00 25.24 ? 131  CYS A N   1 
ATOM   2415 C CA  . CYS C 3 131 ? 234.113 175.663 248.657 1.00 26.32 ? 131  CYS A CA  1 
ATOM   2416 C C   . CYS C 3 131 ? 235.528 176.201 248.804 1.00 26.08 ? 131  CYS A C   1 
ATOM   2417 O O   . CYS C 3 131 ? 236.228 176.417 247.816 1.00 27.57 ? 131  CYS A O   1 
ATOM   2418 C CB  . CYS C 3 131 ? 234.084 174.217 249.183 1.00 26.72 ? 131  CYS A CB  1 
ATOM   2419 S SG  . CYS C 3 131 ? 232.536 173.313 248.878 1.00 26.07 ? 131  CYS A SG  1 
ATOM   2420 N N   . GLU C 3 132 ? 235.963 176.382 250.040 1.00 27.33 ? 132  GLU A N   1 
ATOM   2421 C CA  . GLU C 3 132 ? 237.347 176.736 250.287 1.00 27.32 ? 132  GLU A CA  1 
ATOM   2422 C C   . GLU C 3 132 ? 238.160 175.453 250.335 1.00 27.18 ? 132  GLU A C   1 
ATOM   2423 O O   . GLU C 3 132 ? 238.476 174.931 251.407 1.00 27.64 ? 132  GLU A O   1 
ATOM   2424 C CB  . GLU C 3 132 ? 237.485 177.542 251.579 1.00 28.05 ? 132  GLU A CB  1 
ATOM   2425 N N   . PHE C 3 133 ? 238.428 174.917 249.150 1.00 27.24 ? 133  PHE A N   1 
ATOM   2426 C CA  . PHE C 3 133 ? 239.095 173.635 248.999 1.00 27.25 ? 133  PHE A CA  1 
ATOM   2427 C C   . PHE C 3 133 ? 240.583 173.763 249.233 1.00 27.69 ? 133  PHE A C   1 
ATOM   2428 O O   . PHE C 3 133 ? 241.212 174.711 248.768 1.00 27.71 ? 133  PHE A O   1 
ATOM   2429 C CB  . PHE C 3 133 ? 238.901 173.084 247.584 1.00 27.15 ? 133  PHE A CB  1 
ATOM   2430 C CG  . PHE C 3 133 ? 237.531 172.582 247.259 1.00 26.58 ? 133  PHE A CG  1 
ATOM   2431 C CD1 . PHE C 3 133 ? 236.683 173.317 246.452 1.00 25.95 ? 133  PHE A CD1 1 
ATOM   2432 C CD2 . PHE C 3 133 ? 237.097 171.367 247.734 1.00 26.70 ? 133  PHE A CD2 1 
ATOM   2433 C CE1 . PHE C 3 133 ? 235.430 172.846 246.131 1.00 25.39 ? 133  PHE A CE1 1 
ATOM   2434 C CE2 . PHE C 3 133 ? 235.844 170.893 247.417 1.00 26.71 ? 133  PHE A CE2 1 
ATOM   2435 C CZ  . PHE C 3 133 ? 235.011 171.634 246.616 1.00 25.56 ? 133  PHE A CZ  1 
ATOM   2436 N N   . GLN C 3 134 ? 241.161 172.767 249.882 1.00 27.83 ? 134  GLN A N   1 
ATOM   2437 C CA  . GLN C 3 134 ? 242.609 172.683 249.949 1.00 27.95 ? 134  GLN A CA  1 
ATOM   2438 C C   . GLN C 3 134 ? 243.081 171.597 249.006 1.00 27.53 ? 134  GLN A C   1 
ATOM   2439 O O   . GLN C 3 134 ? 243.086 170.415 249.352 1.00 27.99 ? 134  GLN A O   1 
ATOM   2440 C CB  . GLN C 3 134 ? 243.101 172.406 251.367 1.00 27.90 ? 134  GLN A CB  1 
ATOM   2441 C CG  . GLN C 3 134 ? 244.616 172.311 251.477 1.00 28.14 ? 134  GLN A CG  1 
ATOM   2442 C CD  . GLN C 3 134 ? 245.319 173.566 250.962 1.00 28.50 ? 134  GLN A CD  1 
ATOM   2443 O OE1 . GLN C 3 134 ? 245.029 174.689 251.390 1.00 28.07 ? 134  GLN A OE1 1 
ATOM   2444 N NE2 . GLN C 3 134 ? 246.250 173.375 250.033 1.00 27.17 ? 134  GLN A NE2 1 
ATOM   2445 N N   . PHE C 3 135 ? 243.446 172.002 247.801 1.00 27.97 ? 135  PHE A N   1 
ATOM   2446 C CA  . PHE C 3 135 ? 243.783 171.056 246.754 1.00 28.12 ? 135  PHE A CA  1 
ATOM   2447 C C   . PHE C 3 135 ? 245.185 170.500 246.949 1.00 28.64 ? 135  PHE A C   1 
ATOM   2448 O O   . PHE C 3 135 ? 246.056 171.176 247.502 1.00 29.11 ? 135  PHE A O   1 
ATOM   2449 C CB  . PHE C 3 135 ? 243.667 171.717 245.381 1.00 27.23 ? 135  PHE A CB  1 
ATOM   2450 C CG  . PHE C 3 135 ? 242.254 172.021 244.976 1.00 27.13 ? 135  PHE A CG  1 
ATOM   2451 C CD1 . PHE C 3 135 ? 241.861 173.314 244.706 1.00 27.49 ? 135  PHE A CD1 1 
ATOM   2452 C CD2 . PHE C 3 135 ? 241.317 171.014 244.874 1.00 26.97 ? 135  PHE A CD2 1 
ATOM   2453 C CE1 . PHE C 3 135 ? 240.563 173.591 244.337 1.00 26.44 ? 135  PHE A CE1 1 
ATOM   2454 C CE2 . PHE C 3 135 ? 240.016 171.286 244.511 1.00 26.17 ? 135  PHE A CE2 1 
ATOM   2455 C CZ  . PHE C 3 135 ? 239.639 172.576 244.240 1.00 25.04 ? 135  PHE A CZ  1 
ATOM   2456 N N   . CYS C 3 136 ? 245.395 169.273 246.471 1.00 28.79 ? 136  CYS A N   1 
ATOM   2457 C CA  . CYS C 3 136 ? 246.694 168.610 246.497 1.00 29.47 ? 136  CYS A CA  1 
ATOM   2458 C C   . CYS C 3 136 ? 247.669 169.273 245.527 1.00 29.92 ? 136  CYS A C   1 
ATOM   2459 O O   . CYS C 3 136 ? 247.265 169.954 244.584 1.00 30.13 ? 136  CYS A O   1 
ATOM   2460 C CB  . CYS C 3 136 ? 246.551 167.123 246.128 1.00 30.18 ? 136  CYS A CB  1 
ATOM   2461 S SG  . CYS C 3 136 ? 245.590 166.137 247.308 1.00 32.27 ? 136  CYS A SG  1 
ATOM   2462 N N   . ASN C 3 137 ? 248.963 169.055 245.751 1.00 30.44 ? 137  ASN A N   1 
ATOM   2463 C CA  . ASN C 3 137 ? 249.986 169.600 244.866 1.00 31.07 ? 137  ASN A CA  1 
ATOM   2464 C C   . ASN C 3 137 ? 249.808 169.066 243.449 1.00 31.47 ? 137  ASN A C   1 
ATOM   2465 O O   . ASN C 3 137 ? 250.104 169.751 242.471 1.00 31.63 ? 137  ASN A O   1 
ATOM   2466 C CB  . ASN C 3 137 ? 251.370 169.292 245.407 1.00 32.84 ? 137  ASN A CB  1 
ATOM   2467 N N   . ASP C 3 138 ? 249.289 167.848 243.347 1.00 30.92 ? 138  ASP A N   1 
ATOM   2468 C CA  . ASP C 3 138 ? 248.967 167.236 242.066 1.00 30.07 ? 138  ASP A CA  1 
ATOM   2469 C C   . ASP C 3 138 ? 247.708 166.385 242.215 1.00 29.95 ? 138  ASP A C   1 
ATOM   2470 O O   . ASP C 3 138 ? 247.804 165.189 242.487 1.00 30.05 ? 138  ASP A O   1 
ATOM   2471 C CB  . ASP C 3 138 ? 250.120 166.362 241.567 1.00 30.47 ? 138  ASP A CB  1 
ATOM   2472 C CG  . ASP C 3 138 ? 249.872 165.831 240.158 1.00 29.63 ? 138  ASP A CG  1 
ATOM   2473 O OD1 . ASP C 3 138 ? 248.858 166.167 239.600 1.00 29.54 ? 138  ASP A OD1 1 
ATOM   2474 O OD2 . ASP C 3 138 ? 250.692 165.106 239.652 1.00 29.29 ? 138  ASP A OD2 1 
ATOM   2475 N N   . PRO C 3 139 ? 246.525 166.999 242.112 1.00 29.54 ? 139  PRO A N   1 
ATOM   2476 C CA  . PRO C 3 139 ? 245.223 166.420 242.375 1.00 28.59 ? 139  PRO A CA  1 
ATOM   2477 C C   . PRO C 3 139 ? 244.797 165.477 241.262 1.00 28.72 ? 139  PRO A C   1 
ATOM   2478 O O   . PRO C 3 139 ? 244.998 165.777 240.085 1.00 27.86 ? 139  PRO A O   1 
ATOM   2479 C CB  . PRO C 3 139 ? 244.330 167.661 242.436 1.00 28.03 ? 139  PRO A CB  1 
ATOM   2480 C CG  . PRO C 3 139 ? 245.001 168.661 241.517 1.00 27.66 ? 139  PRO A CG  1 
ATOM   2481 C CD  . PRO C 3 139 ? 246.490 168.382 241.633 1.00 28.86 ? 139  PRO A CD  1 
ATOM   2482 N N   . PHE C 3 140 ? 244.161 164.370 241.627 1.00 28.35 ? 140  PHE A N   1 
ATOM   2483 C CA  . PHE C 3 140 ? 243.622 163.446 240.636 1.00 28.06 ? 140  PHE A CA  1 
ATOM   2484 C C   . PHE C 3 140 ? 242.649 162.447 241.246 1.00 28.20 ? 140  PHE A C   1 
ATOM   2485 O O   . PHE C 3 140 ? 242.529 162.338 242.466 1.00 27.91 ? 140  PHE A O   1 
ATOM   2486 C CB  . PHE C 3 140 ? 244.745 162.704 239.902 1.00 28.54 ? 140  PHE A CB  1 
ATOM   2487 C CG  . PHE C 3 140 ? 245.639 161.856 240.762 1.00 28.98 ? 140  PHE A CG  1 
ATOM   2488 C CD1 . PHE C 3 140 ? 245.349 160.523 240.987 1.00 28.87 ? 140  PHE A CD1 1 
ATOM   2489 C CD2 . PHE C 3 140 ? 246.788 162.379 241.316 1.00 29.64 ? 140  PHE A CD2 1 
ATOM   2490 C CE1 . PHE C 3 140 ? 246.182 159.734 241.748 1.00 29.20 ? 140  PHE A CE1 1 
ATOM   2491 C CE2 . PHE C 3 140 ? 247.628 161.595 242.079 1.00 30.29 ? 140  PHE A CE2 1 
ATOM   2492 C CZ  . PHE C 3 140 ? 247.324 160.267 242.295 1.00 30.35 ? 140  PHE A CZ  1 
ATOM   2493 N N   . LEU C 3 141 ? 241.974 161.696 240.384 1.00 27.49 ? 141  LEU A N   1 
ATOM   2494 C CA  . LEU C 3 141 ? 241.106 160.618 240.832 1.00 27.56 ? 141  LEU A CA  1 
ATOM   2495 C C   . LEU C 3 141 ? 241.867 159.307 240.753 1.00 27.88 ? 141  LEU A C   1 
ATOM   2496 O O   . LEU C 3 141 ? 242.573 159.056 239.777 1.00 30.20 ? 141  LEU A O   1 
ATOM   2497 C CB  . LEU C 3 141 ? 239.848 160.537 239.960 1.00 27.05 ? 141  LEU A CB  1 
ATOM   2498 C CG  . LEU C 3 141 ? 238.722 161.522 240.298 1.00 26.42 ? 141  LEU A CG  1 
ATOM   2499 C CD1 . LEU C 3 141 ? 239.080 162.925 239.797 1.00 26.61 ? 141  LEU A CD1 1 
ATOM   2500 C CD2 . LEU C 3 141 ? 237.433 161.031 239.660 1.00 25.36 ? 141  LEU A CD2 1 
ATOM   2501 N N   . ASP C 3 142 ? 241.764 158.489 241.793 1.00 28.59 ? 142  ASP A N   1 
ATOM   2502 C CA  . ASP C 3 142 ? 242.506 157.236 241.828 1.00 28.47 ? 142  ASP A CA  1 
ATOM   2503 C C   . ASP C 3 142 ? 241.597 156.067 241.491 1.00 29.06 ? 142  ASP A C   1 
ATOM   2504 O O   . ASP C 3 142 ? 240.707 155.712 242.270 1.00 28.50 ? 142  ASP A O   1 
ATOM   2505 C CB  . ASP C 3 142 ? 243.165 157.035 243.194 1.00 29.05 ? 142  ASP A CB  1 
ATOM   2506 C CG  . ASP C 3 142 ? 244.107 155.836 243.226 1.00 29.83 ? 142  ASP A CG  1 
ATOM   2507 O OD1 . ASP C 3 142 ? 243.977 154.983 242.387 1.00 30.46 ? 142  ASP A OD1 1 
ATOM   2508 O OD2 . ASP C 3 142 ? 244.971 155.799 244.072 1.00 29.91 ? 142  ASP A OD2 1 
ATOM   2509 N N   . VAL C 3 143 ? 241.792 155.503 240.306 1.00 29.11 ? 143  VAL A N   1 
ATOM   2510 C CA  . VAL C 3 143 ? 240.941 154.431 239.816 1.00 28.34 ? 143  VAL A CA  1 
ATOM   2511 C C   . VAL C 3 143 ? 241.772 153.232 239.404 1.00 28.72 ? 143  VAL A C   1 
ATOM   2512 O O   . VAL C 3 143 ? 242.971 153.347 239.162 1.00 29.28 ? 143  VAL A O   1 
ATOM   2513 C CB  . VAL C 3 143 ? 240.114 154.909 238.605 1.00 27.61 ? 143  VAL A CB  1 
ATOM   2514 C CG1 . VAL C 3 143 ? 239.252 156.104 238.994 1.00 28.94 ? 143  VAL A CG1 1 
ATOM   2515 C CG2 . VAL C 3 143 ? 241.045 155.275 237.457 1.00 29.07 ? 143  VAL A CG2 1 
ATOM   2516 N N   . TYR C 3 144 ? 241.123 152.087 239.281 1.00 28.49 ? 144  TYR A N   1 
ATOM   2517 C CA  . TYR C 3 144 ? 241.778 150.906 238.750 1.00 28.84 ? 144  TYR A CA  1 
ATOM   2518 C C   . TYR C 3 144 ? 240.881 150.227 237.739 1.00 28.66 ? 144  TYR A C   1 
ATOM   2519 O O   . TYR C 3 144 ? 239.671 150.453 237.715 1.00 29.88 ? 144  TYR A O   1 
ATOM   2520 C CB  . TYR C 3 144 ? 242.201 149.956 239.869 1.00 29.21 ? 144  TYR A CB  1 
ATOM   2521 C CG  . TYR C 3 144 ? 241.083 149.449 240.734 1.00 28.38 ? 144  TYR A CG  1 
ATOM   2522 C CD1 . TYR C 3 144 ? 240.452 148.255 240.445 1.00 28.98 ? 144  TYR A CD1 1 
ATOM   2523 C CD2 . TYR C 3 144 ? 240.709 150.179 241.836 1.00 28.14 ? 144  TYR A CD2 1 
ATOM   2524 C CE1 . TYR C 3 144 ? 239.451 147.797 241.275 1.00 28.73 ? 144  TYR A CE1 1 
ATOM   2525 C CE2 . TYR C 3 144 ? 239.711 149.726 242.663 1.00 27.72 ? 144  TYR A CE2 1 
ATOM   2526 C CZ  . TYR C 3 144 ? 239.087 148.538 242.389 1.00 27.73 ? 144  TYR A CZ  1 
ATOM   2527 O OH  . TYR C 3 144 ? 238.102 148.074 243.222 1.00 27.50 ? 144  TYR A OH  1 
ATOM   2528 N N   . TYR C 3 145 ? 241.482 149.444 236.863 1.00 28.58 ? 145  TYR A N   1 
ATOM   2529 C CA  . TYR C 3 145 ? 240.746 148.859 235.761 1.00 29.14 ? 145  TYR A CA  1 
ATOM   2530 C C   . TYR C 3 145 ? 240.560 147.364 235.911 1.00 30.02 ? 145  TYR A C   1 
ATOM   2531 O O   . TYR C 3 145 ? 241.311 146.694 236.621 1.00 30.29 ? 145  TYR A O   1 
ATOM   2532 C CB  . TYR C 3 145 ? 241.437 149.195 234.445 1.00 29.47 ? 145  TYR A CB  1 
ATOM   2533 C CG  . TYR C 3 145 ? 241.374 150.667 234.114 1.00 29.17 ? 145  TYR A CG  1 
ATOM   2534 C CD1 . TYR C 3 145 ? 242.314 151.539 234.638 1.00 29.47 ? 145  TYR A CD1 1 
ATOM   2535 C CD2 . TYR C 3 145 ? 240.371 151.147 233.291 1.00 29.89 ? 145  TYR A CD2 1 
ATOM   2536 C CE1 . TYR C 3 145 ? 242.248 152.884 234.339 1.00 29.38 ? 145  TYR A CE1 1 
ATOM   2537 C CE2 . TYR C 3 145 ? 240.308 152.493 232.992 1.00 29.44 ? 145  TYR A CE2 1 
ATOM   2538 C CZ  . TYR C 3 145 ? 241.243 153.358 233.514 1.00 29.42 ? 145  TYR A CZ  1 
ATOM   2539 O OH  . TYR C 3 145 ? 241.183 154.699 233.217 1.00 28.91 ? 145  TYR A OH  1 
ATOM   2540 N N   . HIS C 3 146 ? 239.539 146.858 235.236 1.00 30.25 ? 146  HIS A N   1 
ATOM   2541 C CA  . HIS C 3 146 ? 239.228 145.439 235.194 1.00 30.49 ? 146  HIS A CA  1 
ATOM   2542 C C   . HIS C 3 146 ? 240.307 144.712 234.403 1.00 31.32 ? 146  HIS A C   1 
ATOM   2543 O O   . HIS C 3 146 ? 241.255 145.338 233.929 1.00 31.40 ? 146  HIS A O   1 
ATOM   2544 C CB  . HIS C 3 146 ? 237.852 145.247 234.544 1.00 30.40 ? 146  HIS A CB  1 
ATOM   2545 C CG  . HIS C 3 146 ? 237.278 143.872 234.629 1.00 30.48 ? 146  HIS A CG  1 
ATOM   2546 N ND1 . HIS C 3 146 ? 237.722 142.831 233.847 1.00 31.34 ? 146  HIS A ND1 1 
ATOM   2547 C CD2 . HIS C 3 146 ? 236.277 143.372 235.389 1.00 30.10 ? 146  HIS A CD2 1 
ATOM   2548 C CE1 . HIS C 3 146 ? 237.022 141.744 234.129 1.00 31.57 ? 146  HIS A CE1 1 
ATOM   2549 N NE2 . HIS C 3 146 ? 236.141 142.048 235.061 1.00 30.60 ? 146  HIS A NE2 1 
ATOM   2550 N N   . LYS C 3 147 ? 240.185 143.396 234.273 1.00 31.35 ? 147  LYS A N   1 
ATOM   2551 C CA  . LYS C 3 147 ? 241.139 142.650 233.463 1.00 31.19 ? 147  LYS A CA  1 
ATOM   2552 C C   . LYS C 3 147 ? 240.961 143.034 232.003 1.00 31.65 ? 147  LYS A C   1 
ATOM   2553 O O   . LYS C 3 147 ? 241.922 143.055 231.232 1.00 32.38 ? 147  LYS A O   1 
ATOM   2554 C CB  . LYS C 3 147 ? 240.987 141.147 233.677 1.00 31.15 ? 147  LYS A CB  1 
ATOM   2555 C CG  . LYS C 3 147 ? 241.441 140.700 235.054 1.00 31.15 ? 147  LYS A CG  1 
ATOM   2556 C CD  . LYS C 3 147 ? 241.343 139.200 235.244 1.00 31.44 ? 147  LYS A CD  1 
ATOM   2557 C CE  . LYS C 3 147 ? 241.678 138.834 236.678 1.00 30.92 ? 147  LYS A CE  1 
ATOM   2558 N NZ  . LYS C 3 147 ? 241.587 137.383 236.931 1.00 31.62 ? 147  LYS A NZ  1 
ATOM   2559 N N   . ASN C 3 148 ? 239.732 143.394 231.647 1.00 31.71 ? 148  ASN A N   1 
ATOM   2560 C CA  . ASN C 3 148 ? 239.456 143.949 230.333 1.00 31.94 ? 148  ASN A CA  1 
ATOM   2561 C C   . ASN C 3 148 ? 239.805 145.434 230.370 1.00 31.89 ? 148  ASN A C   1 
ATOM   2562 O O   . ASN C 3 148 ? 240.266 145.929 231.397 1.00 31.63 ? 148  ASN A O   1 
ATOM   2563 C CB  . ASN C 3 148 ? 238.008 143.695 229.929 1.00 31.60 ? 148  ASN A CB  1 
ATOM   2564 C CG  . ASN C 3 148 ? 237.004 144.478 230.743 1.00 31.13 ? 148  ASN A CG  1 
ATOM   2565 O OD1 . ASN C 3 148 ? 237.195 145.669 231.027 1.00 30.97 ? 148  ASN A OD1 1 
ATOM   2566 N ND2 . ASN C 3 148 ? 235.935 143.825 231.123 1.00 30.69 ? 148  ASN A ND2 1 
ATOM   2567 N N   . ASN C 3 149 ? 239.629 146.135 229.248 1.00 31.86 ? 149  ASN A N   1 
ATOM   2568 C CA  . ASN C 3 149 ? 240.013 147.542 229.149 1.00 31.73 ? 149  ASN A CA  1 
ATOM   2569 C C   . ASN C 3 149 ? 238.800 148.454 228.912 1.00 31.90 ? 149  ASN A C   1 
ATOM   2570 O O   . ASN C 3 149 ? 238.929 149.527 228.327 1.00 32.46 ? 149  ASN A O   1 
ATOM   2571 C CB  . ASN C 3 149 ? 241.066 147.724 228.060 1.00 33.26 ? 149  ASN A CB  1 
ATOM   2572 C CG  . ASN C 3 149 ? 242.384 147.026 228.400 1.00 33.60 ? 149  ASN A CG  1 
ATOM   2573 O OD1 . ASN C 3 149 ? 243.265 147.630 229.027 1.00 33.27 ? 149  ASN A OD1 1 
ATOM   2574 N ND2 . ASN C 3 149 ? 242.521 145.775 227.998 1.00 33.94 ? 149  ASN A ND2 1 
ATOM   2575 N N   . LYS C 3 150 ? 237.623 148.021 229.387 1.00 31.18 ? 150  LYS A N   1 
ATOM   2576 C CA  . LYS C 3 150 ? 236.379 148.784 229.260 1.00 30.68 ? 150  LYS A CA  1 
ATOM   2577 C C   . LYS C 3 150 ? 235.809 149.176 230.620 1.00 30.35 ? 150  LYS A C   1 
ATOM   2578 O O   . LYS C 3 150 ? 235.239 150.257 230.772 1.00 30.52 ? 150  LYS A O   1 
ATOM   2579 C CB  . LYS C 3 150 ? 235.345 147.975 228.479 1.00 30.95 ? 150  LYS A CB  1 
ATOM   2580 C CG  . LYS C 3 150 ? 235.724 147.718 227.033 1.00 31.50 ? 150  LYS A CG  1 
ATOM   2581 C CD  . LYS C 3 150 ? 234.652 146.925 226.311 1.00 32.01 ? 150  LYS A CD  1 
ATOM   2582 C CE  . LYS C 3 150 ? 235.057 146.642 224.873 1.00 31.88 ? 150  LYS A CE  1 
ATOM   2583 N NZ  . LYS C 3 150 ? 234.053 145.804 224.165 1.00 32.01 ? 150  LYS A NZ  1 
ATOM   2584 N N   . SER C 3 151 ? 235.942 148.287 231.600 1.00 30.10 ? 151  SER A N   1 
ATOM   2585 C CA  . SER C 3 151 ? 235.363 148.510 232.920 1.00 29.30 ? 151  SER A CA  1 
ATOM   2586 C C   . SER C 3 151 ? 236.382 149.103 233.884 1.00 29.47 ? 151  SER A C   1 
ATOM   2587 O O   . SER C 3 151 ? 237.579 148.823 233.789 1.00 29.25 ? 151  SER A O   1 
ATOM   2588 C CB  . SER C 3 151 ? 234.835 147.205 233.479 1.00 29.31 ? 151  SER A CB  1 
ATOM   2589 O OG  . SER C 3 151 ? 233.791 146.699 232.696 1.00 29.18 ? 151  SER A OG  1 
ATOM   2590 N N   . TRP C 3 152 ? 235.898 149.900 234.832 1.00 28.87 ? 152  TRP A N   1 
ATOM   2591 C CA  . TRP C 3 152 ? 236.761 150.483 235.855 1.00 28.35 ? 152  TRP A CA  1 
ATOM   2592 C C   . TRP C 3 152 ? 236.038 150.661 237.180 1.00 26.98 ? 152  TRP A C   1 
ATOM   2593 O O   . TRP C 3 152 ? 234.811 150.681 237.237 1.00 30.15 ? 152  TRP A O   1 
ATOM   2594 C CB  . TRP C 3 152 ? 237.310 151.830 235.390 1.00 28.51 ? 152  TRP A CB  1 
ATOM   2595 C CG  . TRP C 3 152 ? 236.261 152.865 235.157 1.00 28.11 ? 152  TRP A CG  1 
ATOM   2596 C CD1 . TRP C 3 152 ? 235.594 153.096 233.996 1.00 28.48 ? 152  TRP A CD1 1 
ATOM   2597 C CD2 . TRP C 3 152 ? 235.750 153.827 236.107 1.00 27.53 ? 152  TRP A CD2 1 
ATOM   2598 N NE1 . TRP C 3 152 ? 234.708 154.129 234.157 1.00 28.34 ? 152  TRP A NE1 1 
ATOM   2599 C CE2 . TRP C 3 152 ? 234.788 154.585 235.443 1.00 26.94 ? 152  TRP A CE2 1 
ATOM   2600 C CE3 . TRP C 3 152 ? 236.029 154.101 237.447 1.00 27.81 ? 152  TRP A CE3 1 
ATOM   2601 C CZ2 . TRP C 3 152 ? 234.095 155.601 236.071 1.00 26.22 ? 152  TRP A CZ2 1 
ATOM   2602 C CZ3 . TRP C 3 152 ? 235.333 155.119 238.078 1.00 27.65 ? 152  TRP A CZ3 1 
ATOM   2603 C CH2 . TRP C 3 152 ? 234.391 155.849 237.408 1.00 26.25 ? 152  TRP A CH2 1 
ATOM   2604 N N   . MET C 3 153 ? 236.804 150.783 238.254 1.00 28.67 ? 153  MET A N   1 
ATOM   2605 C CA  . MET C 3 153 ? 236.228 150.996 239.574 1.00 28.22 ? 153  MET A CA  1 
ATOM   2606 C C   . MET C 3 153 ? 237.071 151.991 240.360 1.00 27.50 ? 153  MET A C   1 
ATOM   2607 O O   . MET C 3 153 ? 238.288 152.059 240.190 1.00 29.38 ? 153  MET A O   1 
ATOM   2608 C CB  . MET C 3 153 ? 236.101 149.661 240.306 1.00 28.53 ? 153  MET A CB  1 
ATOM   2609 C CG  . MET C 3 153 ? 235.393 149.723 241.654 1.00 29.31 ? 153  MET A CG  1 
ATOM   2610 S SD  . MET C 3 153 ? 235.225 148.094 242.429 1.00 27.58 ? 153  MET A SD  1 
ATOM   2611 C CE  . MET C 3 153 ? 233.940 147.335 241.449 1.00 28.53 ? 153  MET A CE  1 
ATOM   2612 N N   . LYS C 3 154 ? 236.419 152.793 241.189 1.00 27.47 ? 154  LYS A N   1 
ATOM   2613 C CA  . LYS C 3 154 ? 237.117 153.805 241.972 1.00 27.55 ? 154  LYS A CA  1 
ATOM   2614 C C   . LYS C 3 154 ? 237.838 153.199 243.167 1.00 27.77 ? 154  LYS A C   1 
ATOM   2615 O O   . LYS C 3 154 ? 237.307 152.313 243.836 1.00 28.45 ? 154  LYS A O   1 
ATOM   2616 C CB  . LYS C 3 154 ? 236.133 154.876 242.446 1.00 28.06 ? 154  LYS A CB  1 
ATOM   2617 C CG  . LYS C 3 154 ? 236.776 156.046 243.195 1.00 28.19 ? 154  LYS A CG  1 
ATOM   2618 C CD  . LYS C 3 154 ? 235.775 157.175 243.436 1.00 26.68 ? 154  LYS A CD  1 
ATOM   2619 C CE  . LYS C 3 154 ? 234.762 156.805 244.519 1.00 26.34 ? 154  LYS A CE  1 
ATOM   2620 N NZ  . LYS C 3 154 ? 233.865 157.944 244.857 1.00 25.47 ? 154  LYS A NZ  1 
ATOM   2621 N N   . SER C 3 155 ? 239.028 153.717 243.457 1.00 27.90 ? 155  SER A N   1 
ATOM   2622 C CA  . SER C 3 155 ? 239.766 153.350 244.659 1.00 27.74 ? 155  SER A CA  1 
ATOM   2623 C C   . SER C 3 155 ? 239.618 154.435 245.711 1.00 28.10 ? 155  SER A C   1 
ATOM   2624 O O   . SER C 3 155 ? 239.199 154.172 246.840 1.00 28.25 ? 155  SER A O   1 
ATOM   2625 C CB  . SER C 3 155 ? 241.237 153.157 244.350 1.00 28.23 ? 155  SER A CB  1 
ATOM   2626 O OG  . SER C 3 155 ? 241.955 152.835 245.507 1.00 28.38 ? 155  SER A OG  1 
ATOM   2627 N N   . GLU C 3 156 ? 239.972 155.660 245.333 1.00 28.18 ? 156  GLU A N   1 
ATOM   2628 C CA  . GLU C 3 156 ? 239.920 156.788 246.251 1.00 28.16 ? 156  GLU A CA  1 
ATOM   2629 C C   . GLU C 3 156 ? 239.813 158.104 245.482 1.00 28.31 ? 156  GLU A C   1 
ATOM   2630 O O   . GLU C 3 156 ? 239.837 158.124 244.250 1.00 28.46 ? 156  GLU A O   1 
ATOM   2631 C CB  . GLU C 3 156 ? 241.170 156.766 247.152 1.00 28.19 ? 156  GLU A CB  1 
ATOM   2632 C CG  . GLU C 3 156 ? 241.173 157.748 248.331 1.00 28.48 ? 156  GLU A CG  1 
ATOM   2633 C CD  . GLU C 3 156 ? 242.247 157.441 249.337 1.00 29.98 ? 156  GLU A CD  1 
ATOM   2634 O OE1 . GLU C 3 156 ? 242.946 156.472 249.158 1.00 28.27 ? 156  GLU A OE1 1 
ATOM   2635 O OE2 . GLU C 3 156 ? 242.361 158.172 250.294 1.00 29.45 ? 156  GLU A OE2 1 
ATOM   2636 N N   . PHE C 3 157 ? 239.708 159.203 246.214 1.00 28.08 ? 157  PHE A N   1 
ATOM   2637 C CA  . PHE C 3 157 ? 239.610 160.527 245.623 1.00 27.83 ? 157  PHE A CA  1 
ATOM   2638 C C   . PHE C 3 157 ? 240.739 161.389 246.171 1.00 28.45 ? 157  PHE A C   1 
ATOM   2639 O O   . PHE C 3 157 ? 240.797 161.642 247.373 1.00 29.13 ? 157  PHE A O   1 
ATOM   2640 C CB  . PHE C 3 157 ? 238.249 161.131 245.968 1.00 27.49 ? 157  PHE A CB  1 
ATOM   2641 C CG  . PHE C 3 157 ? 237.841 162.295 245.136 1.00 26.76 ? 157  PHE A CG  1 
ATOM   2642 C CD1 . PHE C 3 157 ? 237.391 162.095 243.847 1.00 26.85 ? 157  PHE A CD1 1 
ATOM   2643 C CD2 . PHE C 3 157 ? 237.874 163.581 245.635 1.00 27.05 ? 157  PHE A CD2 1 
ATOM   2644 C CE1 . PHE C 3 157 ? 236.985 163.153 243.071 1.00 25.71 ? 157  PHE A CE1 1 
ATOM   2645 C CE2 . PHE C 3 157 ? 237.465 164.643 244.857 1.00 26.78 ? 157  PHE A CE2 1 
ATOM   2646 C CZ  . PHE C 3 157 ? 237.021 164.428 243.574 1.00 25.51 ? 157  PHE A CZ  1 
ATOM   2647 N N   . ARG C 3 158 ? 241.671 161.788 245.312 1.00 28.14 ? 158  ARG A N   1 
ATOM   2648 C CA  . ARG C 3 158 ? 242.877 162.463 245.777 1.00 28.94 ? 158  ARG A CA  1 
ATOM   2649 C C   . ARG C 3 158 ? 242.989 163.858 245.187 1.00 28.92 ? 158  ARG A C   1 
ATOM   2650 O O   . ARG C 3 158 ? 244.003 164.213 244.587 1.00 29.06 ? 158  ARG A O   1 
ATOM   2651 C CB  . ARG C 3 158 ? 244.109 161.663 245.389 1.00 29.32 ? 158  ARG A CB  1 
ATOM   2652 C CG  . ARG C 3 158 ? 244.155 160.253 245.940 1.00 29.47 ? 158  ARG A CG  1 
ATOM   2653 C CD  . ARG C 3 158 ? 245.418 159.580 245.572 1.00 30.01 ? 158  ARG A CD  1 
ATOM   2654 N NE  . ARG C 3 158 ? 245.389 158.155 245.852 1.00 30.06 ? 158  ARG A NE  1 
ATOM   2655 C CZ  . ARG C 3 158 ? 245.612 157.588 247.048 1.00 30.68 ? 158  ARG A CZ  1 
ATOM   2656 N NH1 . ARG C 3 158 ? 245.883 158.322 248.106 1.00 31.58 ? 158  ARG A NH1 1 
ATOM   2657 N NH2 . ARG C 3 158 ? 245.554 156.276 247.144 1.00 30.16 ? 158  ARG A NH2 1 
ATOM   2658 N N   . VAL C 3 159 ? 241.928 164.636 245.331 1.00 28.44 ? 159  VAL A N   1 
ATOM   2659 C CA  . VAL C 3 159 ? 241.885 165.971 244.757 1.00 28.25 ? 159  VAL A CA  1 
ATOM   2660 C C   . VAL C 3 159 ? 242.126 167.033 245.817 1.00 27.88 ? 159  VAL A C   1 
ATOM   2661 O O   . VAL C 3 159 ? 242.877 167.981 245.592 1.00 28.93 ? 159  VAL A O   1 
ATOM   2662 C CB  . VAL C 3 159 ? 240.538 166.197 244.051 1.00 27.06 ? 159  VAL A CB  1 
ATOM   2663 C CG1 . VAL C 3 159 ? 240.429 167.619 243.551 1.00 26.34 ? 159  VAL A CG1 1 
ATOM   2664 C CG2 . VAL C 3 159 ? 240.419 165.218 242.889 1.00 26.90 ? 159  VAL A CG2 1 
ATOM   2665 N N   . TYR C 3 160 ? 241.481 166.876 246.966 1.00 28.11 ? 160  TYR A N   1 
ATOM   2666 C CA  . TYR C 3 160 ? 241.609 167.833 248.055 1.00 27.77 ? 160  TYR A CA  1 
ATOM   2667 C C   . TYR C 3 160 ? 241.607 167.135 249.405 1.00 28.08 ? 160  TYR A C   1 
ATOM   2668 O O   . TYR C 3 160 ? 241.081 166.031 249.542 1.00 27.90 ? 160  TYR A O   1 
ATOM   2669 C CB  . TYR C 3 160 ? 240.483 168.868 247.995 1.00 27.60 ? 160  TYR A CB  1 
ATOM   2670 C CG  . TYR C 3 160 ? 239.097 168.279 248.127 1.00 27.25 ? 160  TYR A CG  1 
ATOM   2671 C CD1 . TYR C 3 160 ? 238.572 168.026 249.376 1.00 27.36 ? 160  TYR A CD1 1 
ATOM   2672 C CD2 . TYR C 3 160 ? 238.344 168.010 246.998 1.00 26.93 ? 160  TYR A CD2 1 
ATOM   2673 C CE1 . TYR C 3 160 ? 237.311 167.501 249.507 1.00 27.38 ? 160  TYR A CE1 1 
ATOM   2674 C CE2 . TYR C 3 160 ? 237.075 167.487 247.130 1.00 26.37 ? 160  TYR A CE2 1 
ATOM   2675 C CZ  . TYR C 3 160 ? 236.562 167.231 248.380 1.00 26.77 ? 160  TYR A CZ  1 
ATOM   2676 O OH  . TYR C 3 160 ? 235.298 166.708 248.516 1.00 26.52 ? 160  TYR A OH  1 
ATOM   2677 N N   . SER C 3 161 ? 242.184 167.798 250.405 1.00 28.09 ? 161  SER A N   1 
ATOM   2678 C CA  . SER C 3 161 ? 242.204 167.281 251.768 1.00 27.70 ? 161  SER A CA  1 
ATOM   2679 C C   . SER C 3 161 ? 241.084 167.874 252.621 1.00 27.80 ? 161  SER A C   1 
ATOM   2680 O O   . SER C 3 161 ? 240.737 167.330 253.670 1.00 27.61 ? 161  SER A O   1 
ATOM   2681 C CB  . SER C 3 161 ? 243.543 167.573 252.412 1.00 27.08 ? 161  SER A CB  1 
ATOM   2682 O OG  . SER C 3 161 ? 243.743 168.952 252.550 1.00 27.65 ? 161  SER A OG  1 
ATOM   2683 N N   . SER C 3 162 ? 240.521 168.991 252.170 1.00 27.79 ? 162  SER A N   1 
ATOM   2684 C CA  . SER C 3 162 ? 239.445 169.658 252.897 1.00 27.32 ? 162  SER A CA  1 
ATOM   2685 C C   . SER C 3 162 ? 238.548 170.458 251.958 1.00 27.22 ? 162  SER A C   1 
ATOM   2686 O O   . SER C 3 162 ? 238.951 170.820 250.851 1.00 28.64 ? 162  SER A O   1 
ATOM   2687 C CB  . SER C 3 162 ? 240.017 170.567 253.967 1.00 27.92 ? 162  SER A CB  1 
ATOM   2688 O OG  . SER C 3 162 ? 240.728 171.629 253.399 1.00 28.41 ? 162  SER A OG  1 
ATOM   2689 N N   . ALA C 3 163 ? 237.329 170.740 252.413 1.00 27.35 ? 163  ALA A N   1 
ATOM   2690 C CA  . ALA C 3 163 ? 236.364 171.524 251.646 1.00 27.54 ? 163  ALA A CA  1 
ATOM   2691 C C   . ALA C 3 163 ? 235.476 172.327 252.583 1.00 27.46 ? 163  ALA A C   1 
ATOM   2692 O O   . ALA C 3 163 ? 234.359 171.916 252.895 1.00 27.25 ? 163  ALA A O   1 
ATOM   2693 C CB  . ALA C 3 163 ? 235.514 170.616 250.776 1.00 27.07 ? 163  ALA A CB  1 
ATOM   2694 N N   . ASN C 3 164 ? 236.004 173.432 253.091 1.00 27.80 ? 164  ASN A N   1 
ATOM   2695 C CA  . ASN C 3 164 ? 235.325 174.181 254.141 1.00 28.42 ? 164  ASN A CA  1 
ATOM   2696 C C   . ASN C 3 164 ? 234.476 175.313 253.569 1.00 28.75 ? 164  ASN A C   1 
ATOM   2697 O O   . ASN C 3 164 ? 234.734 175.787 252.463 1.00 28.09 ? 164  ASN A O   1 
ATOM   2698 C CB  . ASN C 3 164 ? 236.342 174.719 255.127 1.00 29.51 ? 164  ASN A CB  1 
ATOM   2699 C CG  . ASN C 3 164 ? 237.135 173.627 255.781 1.00 29.69 ? 164  ASN A CG  1 
ATOM   2700 O OD1 . ASN C 3 164 ? 236.617 172.538 256.056 1.00 28.79 ? 164  ASN A OD1 1 
ATOM   2701 N ND2 . ASN C 3 164 ? 238.388 173.896 256.038 1.00 28.67 ? 164  ASN A ND2 1 
ATOM   2702 N N   . ASN C 3 165 ? 233.560 175.847 254.388 1.00 29.04 ? 165  ASN A N   1 
ATOM   2703 C CA  . ASN C 3 165 ? 232.724 177.013 253.980 1.00 28.71 ? 165  ASN A CA  1 
ATOM   2704 C C   . ASN C 3 165 ? 232.166 176.825 252.564 1.00 27.71 ? 165  ASN A C   1 
ATOM   2705 O O   . ASN C 3 165 ? 232.398 177.721 251.729 1.00 27.58 ? 165  ASN A O   1 
ATOM   2706 C CB  . ASN C 3 165 ? 233.468 178.354 254.066 1.00 30.20 ? 165  ASN A CB  1 
ATOM   2707 C CG  . ASN C 3 165 ? 234.064 178.721 255.414 1.00 31.38 ? 165  ASN A CG  1 
ATOM   2708 O OD1 . ASN C 3 165 ? 235.283 178.835 255.525 1.00 31.17 ? 165  ASN A OD1 1 
ATOM   2709 N ND2 . ASN C 3 165 ? 233.232 178.930 256.431 1.00 32.84 ? 165  ASN A ND2 1 
ATOM   2710 N N   . CYS C 3 166 ? 231.443 175.731 252.298 1.00 26.99 ? 166  CYS A N   1 
ATOM   2711 C CA  . CYS C 3 166 ? 230.805 175.521 250.995 1.00 26.11 ? 166  CYS A CA  1 
ATOM   2712 C C   . CYS C 3 166 ? 229.597 176.437 250.804 1.00 25.43 ? 166  CYS A C   1 
ATOM   2713 O O   . CYS C 3 166 ? 228.744 176.557 251.686 1.00 25.57 ? 166  CYS A O   1 
ATOM   2714 C CB  . CYS C 3 166 ? 230.376 174.056 250.827 1.00 25.11 ? 166  CYS A CB  1 
ATOM   2715 S SG  . CYS C 3 166 ? 231.760 172.891 250.703 1.00 28.33 ? 166  CYS A SG  1 
ATOM   2716 N N   . THR C 3 167 ? 229.536 177.085 249.643 1.00 25.01 ? 167  THR A N   1 
ATOM   2717 C CA  . THR C 3 167 ? 228.470 178.034 249.348 1.00 24.09 ? 167  THR A CA  1 
ATOM   2718 C C   . THR C 3 167 ? 227.542 177.554 248.239 1.00 24.21 ? 167  THR A C   1 
ATOM   2719 O O   . THR C 3 167 ? 226.404 178.011 248.135 1.00 24.64 ? 167  THR A O   1 
ATOM   2720 C CB  . THR C 3 167 ? 229.057 179.396 248.939 1.00 24.60 ? 167  THR A CB  1 
ATOM   2721 O OG1 . THR C 3 167 ? 229.846 179.232 247.754 1.00 25.24 ? 167  THR A OG1 1 
ATOM   2722 C CG2 . THR C 3 167 ? 229.935 179.946 250.050 1.00 25.03 ? 167  THR A CG2 1 
ATOM   2723 N N   . PHE C 3 168 ? 228.026 176.642 247.403 1.00 23.88 ? 168  PHE A N   1 
ATOM   2724 C CA  . PHE C 3 168 ? 227.237 176.182 246.264 1.00 23.69 ? 168  PHE A CA  1 
ATOM   2725 C C   . PHE C 3 168 ? 227.427 174.698 246.002 1.00 23.48 ? 168  PHE A C   1 
ATOM   2726 O O   . PHE C 3 168 ? 228.549 174.191 246.015 1.00 23.59 ? 168  PHE A O   1 
ATOM   2727 C CB  . PHE C 3 168 ? 227.610 176.971 245.009 1.00 23.84 ? 168  PHE A CB  1 
ATOM   2728 C CG  . PHE C 3 168 ? 226.879 176.559 243.777 1.00 23.03 ? 168  PHE A CG  1 
ATOM   2729 C CD1 . PHE C 3 168 ? 227.416 175.607 242.928 1.00 23.80 ? 168  PHE A CD1 1 
ATOM   2730 C CD2 . PHE C 3 168 ? 225.667 177.130 243.450 1.00 23.79 ? 168  PHE A CD2 1 
ATOM   2731 C CE1 . PHE C 3 168 ? 226.754 175.233 241.783 1.00 23.46 ? 168  PHE A CE1 1 
ATOM   2732 C CE2 . PHE C 3 168 ? 225.001 176.758 242.305 1.00 24.21 ? 168  PHE A CE2 1 
ATOM   2733 C CZ  . PHE C 3 168 ? 225.545 175.810 241.471 1.00 23.29 ? 168  PHE A CZ  1 
ATOM   2734 N N   . GLU C 3 169 ? 226.326 174.008 245.726 1.00 22.99 ? 169  GLU A N   1 
ATOM   2735 C CA  . GLU C 3 169 ? 226.384 172.605 245.344 1.00 22.42 ? 169  GLU A CA  1 
ATOM   2736 C C   . GLU C 3 169 ? 225.325 172.275 244.304 1.00 22.83 ? 169  GLU A C   1 
ATOM   2737 O O   . GLU C 3 169 ? 224.151 172.609 244.466 1.00 24.02 ? 169  GLU A O   1 
ATOM   2738 C CB  . GLU C 3 169 ? 226.216 171.702 246.566 1.00 21.48 ? 169  GLU A CB  1 
ATOM   2739 C CG  . GLU C 3 169 ? 226.294 170.213 246.253 1.00 21.61 ? 169  GLU A CG  1 
ATOM   2740 C CD  . GLU C 3 169 ? 226.278 169.352 247.478 1.00 20.25 ? 169  GLU A CD  1 
ATOM   2741 O OE1 . GLU C 3 169 ? 226.227 169.886 248.559 1.00 19.70 ? 169  GLU A OE1 1 
ATOM   2742 O OE2 . GLU C 3 169 ? 226.322 168.153 247.335 1.00 19.57 ? 169  GLU A OE2 1 
ATOM   2743 N N   . TYR C 3 170 ? 225.748 171.597 243.247 1.00 22.49 ? 170  TYR A N   1 
ATOM   2744 C CA  . TYR C 3 170 ? 224.865 171.204 242.161 1.00 22.31 ? 170  TYR A CA  1 
ATOM   2745 C C   . TYR C 3 170 ? 225.205 169.808 241.662 1.00 22.60 ? 170  TYR A C   1 
ATOM   2746 O O   . TYR C 3 170 ? 226.373 169.480 241.454 1.00 22.65 ? 170  TYR A O   1 
ATOM   2747 C CB  . TYR C 3 170 ? 224.985 172.225 241.032 1.00 22.70 ? 170  TYR A CB  1 
ATOM   2748 C CG  . TYR C 3 170 ? 224.259 171.885 239.766 1.00 22.30 ? 170  TYR A CG  1 
ATOM   2749 C CD1 . TYR C 3 170 ? 224.919 171.207 238.763 1.00 22.61 ? 170  TYR A CD1 1 
ATOM   2750 C CD2 . TYR C 3 170 ? 222.951 172.281 239.589 1.00 23.17 ? 170  TYR A CD2 1 
ATOM   2751 C CE1 . TYR C 3 170 ? 224.275 170.922 237.583 1.00 22.58 ? 170  TYR A CE1 1 
ATOM   2752 C CE2 . TYR C 3 170 ? 222.301 171.996 238.408 1.00 22.37 ? 170  TYR A CE2 1 
ATOM   2753 C CZ  . TYR C 3 170 ? 222.960 171.321 237.407 1.00 22.31 ? 170  TYR A CZ  1 
ATOM   2754 O OH  . TYR C 3 170 ? 222.315 171.040 236.225 1.00 22.39 ? 170  TYR A OH  1 
ATOM   2755 N N   . VAL C 3 171 ? 224.185 168.978 241.481 1.00 23.31 ? 171  VAL A N   1 
ATOM   2756 C CA  . VAL C 3 171 ? 224.390 167.636 240.954 1.00 23.05 ? 171  VAL A CA  1 
ATOM   2757 C C   . VAL C 3 171 ? 223.433 167.350 239.811 1.00 22.92 ? 171  VAL A C   1 
ATOM   2758 O O   . VAL C 3 171 ? 222.228 167.570 239.927 1.00 23.87 ? 171  VAL A O   1 
ATOM   2759 C CB  . VAL C 3 171 ? 224.214 166.574 242.059 1.00 23.80 ? 171  VAL A CB  1 
ATOM   2760 C CG1 . VAL C 3 171 ? 224.415 165.172 241.477 1.00 23.97 ? 171  VAL A CG1 1 
ATOM   2761 C CG2 . VAL C 3 171 ? 225.218 166.830 243.177 1.00 23.51 ? 171  VAL A CG2 1 
ATOM   2762 N N   . SER C 3 172 ? 223.971 166.850 238.709 1.00 22.99 ? 172  SER A N   1 
ATOM   2763 C CA  . SER C 3 172 ? 223.152 166.504 237.555 1.00 23.43 ? 172  SER A CA  1 
ATOM   2764 C C   . SER C 3 172 ? 223.742 165.331 236.796 1.00 23.10 ? 172  SER A C   1 
ATOM   2765 O O   . SER C 3 172 ? 224.563 164.583 237.327 1.00 23.65 ? 172  SER A O   1 
ATOM   2766 C CB  . SER C 3 172 ? 223.007 167.694 236.633 1.00 24.34 ? 172  SER A CB  1 
ATOM   2767 O OG  . SER C 3 172 ? 222.023 167.458 235.662 1.00 23.02 ? 172  SER A OG  1 
ATOM   2768 N N   . GLN C 3 173 ? 223.313 165.161 235.555 1.00 21.80 ? 173  GLN A N   1 
ATOM   2769 C CA  . GLN C 3 173 ? 223.799 164.060 234.742 1.00 23.38 ? 173  GLN A CA  1 
ATOM   2770 C C   . GLN C 3 173 ? 225.206 164.372 234.239 1.00 23.87 ? 173  GLN A C   1 
ATOM   2771 O O   . GLN C 3 173 ? 225.541 165.541 234.058 1.00 24.21 ? 173  GLN A O   1 
ATOM   2772 C CB  . GLN C 3 173 ? 222.850 163.810 233.569 1.00 24.24 ? 173  GLN A CB  1 
ATOM   2773 C CG  . GLN C 3 173 ? 221.480 163.334 233.991 1.00 23.26 ? 173  GLN A CG  1 
ATOM   2774 C CD  . GLN C 3 173 ? 221.554 162.036 234.756 1.00 23.34 ? 173  GLN A CD  1 
ATOM   2775 O OE1 . GLN C 3 173 ? 222.145 161.060 234.286 1.00 23.37 ? 173  GLN A OE1 1 
ATOM   2776 N NE2 . GLN C 3 173 ? 220.962 162.014 235.943 1.00 22.92 ? 173  GLN A NE2 1 
ATOM   2777 N N   . PRO C 3 174 ? 226.036 163.354 233.986 1.00 23.83 ? 174  PRO A N   1 
ATOM   2778 C CA  . PRO C 3 174 ? 227.403 163.464 233.518 1.00 23.46 ? 174  PRO A CA  1 
ATOM   2779 C C   . PRO C 3 174 ? 227.491 164.296 232.252 1.00 24.19 ? 174  PRO A C   1 
ATOM   2780 O O   . PRO C 3 174 ? 226.608 164.231 231.398 1.00 25.52 ? 174  PRO A O   1 
ATOM   2781 C CB  . PRO C 3 174 ? 227.771 162.005 233.231 1.00 23.76 ? 174  PRO A CB  1 
ATOM   2782 C CG  . PRO C 3 174 ? 226.886 161.202 234.140 1.00 24.54 ? 174  PRO A CG  1 
ATOM   2783 C CD  . PRO C 3 174 ? 225.586 161.968 234.199 1.00 24.01 ? 174  PRO A CD  1 
ATOM   2784 N N   . PHE C 3 175 ? 228.579 165.046 232.115 1.00 23.82 ? 175  PHE A N   1 
ATOM   2785 C CA  . PHE C 3 175 ? 228.815 165.835 230.909 1.00 23.00 ? 175  PHE A CA  1 
ATOM   2786 C C   . PHE C 3 175 ? 229.063 164.938 229.688 1.00 23.36 ? 175  PHE A C   1 
ATOM   2787 O O   . PHE C 3 175 ? 228.701 165.298 228.567 1.00 23.70 ? 175  PHE A O   1 
ATOM   2788 C CB  . PHE C 3 175 ? 230.002 166.780 231.108 1.00 22.69 ? 175  PHE A CB  1 
ATOM   2789 C CG  . PHE C 3 175 ? 229.724 167.991 231.985 1.00 22.77 ? 175  PHE A CG  1 
ATOM   2790 C CD1 . PHE C 3 175 ? 228.507 168.166 232.643 1.00 22.82 ? 175  PHE A CD1 1 
ATOM   2791 C CD2 . PHE C 3 175 ? 230.692 168.971 232.134 1.00 22.64 ? 175  PHE A CD2 1 
ATOM   2792 C CE1 . PHE C 3 175 ? 228.282 169.288 233.416 1.00 22.90 ? 175  PHE A CE1 1 
ATOM   2793 C CE2 . PHE C 3 175 ? 230.463 170.087 232.906 1.00 22.50 ? 175  PHE A CE2 1 
ATOM   2794 C CZ  . PHE C 3 175 ? 229.258 170.246 233.545 1.00 23.21 ? 175  PHE A CZ  1 
ATOM   2795 N N   . LEU C 3 176 ? 229.666 163.762 229.916 1.00 23.67 ? 176  LEU A N   1 
ATOM   2796 C CA  . LEU C 3 176 ? 229.914 162.759 228.880 1.00 23.72 ? 176  LEU A CA  1 
ATOM   2797 C C   . LEU C 3 176 ? 228.589 162.210 228.346 1.00 24.21 ? 176  LEU A C   1 
ATOM   2798 O O   . LEU C 3 176 ? 228.552 161.466 227.365 1.00 24.29 ? 176  LEU A O   1 
ATOM   2799 C CB  . LEU C 3 176 ? 230.783 161.615 229.463 1.00 24.19 ? 176  LEU A CB  1 
ATOM   2800 N N   . PHE C 3 186 ? 236.725 154.600 217.109 1.00 32.87 ? 186  PHE A N   1 
ATOM   2801 C CA  . PHE C 3 186 ? 236.360 156.040 217.054 1.00 34.01 ? 186  PHE A CA  1 
ATOM   2802 C C   . PHE C 3 186 ? 236.623 156.679 218.420 1.00 33.53 ? 186  PHE A C   1 
ATOM   2803 O O   . PHE C 3 186 ? 236.136 156.145 219.434 1.00 33.64 ? 186  PHE A O   1 
ATOM   2804 C CB  . PHE C 3 186 ? 234.880 156.202 216.699 1.00 33.60 ? 186  PHE A CB  1 
ATOM   2805 C CG  . PHE C 3 186 ? 233.952 156.174 217.887 1.00 33.35 ? 186  PHE A CG  1 
ATOM   2806 C CD1 . PHE C 3 186 ? 233.483 154.974 218.396 1.00 32.57 ? 186  PHE A CD1 1 
ATOM   2807 C CD2 . PHE C 3 186 ? 233.561 157.349 218.509 1.00 32.74 ? 186  PHE A CD2 1 
ATOM   2808 C CE1 . PHE C 3 186 ? 232.636 154.950 219.492 1.00 32.92 ? 186  PHE A CE1 1 
ATOM   2809 C CE2 . PHE C 3 186 ? 232.714 157.325 219.605 1.00 32.66 ? 186  PHE A CE2 1 
ATOM   2810 C CZ  . PHE C 3 186 ? 232.253 156.126 220.095 1.00 33.33 ? 186  PHE A CZ  1 
ATOM   2811 N N   . LYS C 3 187 ? 237.357 157.795 218.444 1.00 32.69 ? 187  LYS A N   1 
ATOM   2812 C CA  . LYS C 3 187 ? 237.603 158.502 219.702 1.00 32.28 ? 187  LYS A CA  1 
ATOM   2813 C C   . LYS C 3 187 ? 236.502 159.520 219.960 1.00 31.87 ? 187  LYS A C   1 
ATOM   2814 O O   . LYS C 3 187 ? 235.811 159.950 219.036 1.00 31.78 ? 187  LYS A O   1 
ATOM   2815 C CB  . LYS C 3 187 ? 238.972 159.179 219.679 1.00 32.16 ? 187  LYS A CB  1 
ATOM   2816 C CG  . LYS C 3 187 ? 240.138 158.209 219.577 1.00 32.71 ? 187  LYS A CG  1 
ATOM   2817 C CD  . LYS C 3 187 ? 241.477 158.929 219.660 1.00 33.78 ? 187  LYS A CD  1 
ATOM   2818 C CE  . LYS C 3 187 ? 242.639 157.950 219.547 1.00 34.63 ? 187  LYS A CE  1 
ATOM   2819 N NZ  . LYS C 3 187 ? 243.961 158.622 219.718 1.00 36.82 ? 187  LYS A NZ  1 
ATOM   2820 N N   . ASN C 3 188 ? 236.333 159.899 221.218 1.00 30.92 ? 188  ASN A N   1 
ATOM   2821 C CA  . ASN C 3 188 ? 235.326 160.881 221.584 1.00 30.03 ? 188  ASN A CA  1 
ATOM   2822 C C   . ASN C 3 188 ? 235.909 162.280 221.647 1.00 30.15 ? 188  ASN A C   1 
ATOM   2823 O O   . ASN C 3 188 ? 236.872 162.527 222.373 1.00 29.87 ? 188  ASN A O   1 
ATOM   2824 C CB  . ASN C 3 188 ? 234.696 160.519 222.914 1.00 29.55 ? 188  ASN A CB  1 
ATOM   2825 C CG  . ASN C 3 188 ? 233.826 159.308 222.826 1.00 30.60 ? 188  ASN A CG  1 
ATOM   2826 O OD1 . ASN C 3 188 ? 232.694 159.388 222.336 1.00 29.80 ? 188  ASN A OD1 1 
ATOM   2827 N ND2 . ASN C 3 188 ? 234.324 158.189 223.287 1.00 30.10 ? 188  ASN A ND2 1 
ATOM   2828 N N   . LEU C 3 189 ? 235.321 163.197 220.888 1.00 29.85 ? 189  LEU A N   1 
ATOM   2829 C CA  . LEU C 3 189 ? 235.726 164.593 220.929 1.00 29.22 ? 189  LEU A CA  1 
ATOM   2830 C C   . LEU C 3 189 ? 234.744 165.401 221.754 1.00 28.70 ? 189  LEU A C   1 
ATOM   2831 O O   . LEU C 3 189 ? 233.553 165.462 221.444 1.00 28.57 ? 189  LEU A O   1 
ATOM   2832 C CB  . LEU C 3 189 ? 235.800 165.187 219.518 1.00 30.20 ? 189  LEU A CB  1 
ATOM   2833 C CG  . LEU C 3 189 ? 236.043 166.715 219.441 1.00 28.55 ? 189  LEU A CG  1 
ATOM   2834 C CD1 . LEU C 3 189 ? 237.433 167.053 219.958 1.00 29.55 ? 189  LEU A CD1 1 
ATOM   2835 C CD2 . LEU C 3 189 ? 235.879 167.170 218.013 1.00 30.77 ? 189  LEU A CD2 1 
ATOM   2836 N N   . ARG C 3 190 ? 235.244 166.036 222.798 1.00 28.11 ? 190  ARG A N   1 
ATOM   2837 C CA  . ARG C 3 190 ? 234.396 166.860 223.638 1.00 27.55 ? 190  ARG A CA  1 
ATOM   2838 C C   . ARG C 3 190 ? 234.926 168.275 223.699 1.00 27.44 ? 190  ARG A C   1 
ATOM   2839 O O   . ARG C 3 190 ? 236.106 168.498 223.961 1.00 27.65 ? 190  ARG A O   1 
ATOM   2840 C CB  . ARG C 3 190 ? 234.292 166.285 225.039 1.00 26.44 ? 190  ARG A CB  1 
ATOM   2841 C CG  . ARG C 3 190 ? 233.562 164.961 225.129 1.00 26.44 ? 190  ARG A CG  1 
ATOM   2842 C CD  . ARG C 3 190 ? 233.543 164.442 226.516 1.00 24.66 ? 190  ARG A CD  1 
ATOM   2843 N NE  . ARG C 3 190 ? 232.824 163.181 226.618 1.00 24.19 ? 190  ARG A NE  1 
ATOM   2844 C CZ  . ARG C 3 190 ? 233.349 161.965 226.347 1.00 24.04 ? 190  ARG A CZ  1 
ATOM   2845 N NH1 . ARG C 3 190 ? 234.596 161.857 225.944 1.00 23.67 ? 190  ARG A NH1 1 
ATOM   2846 N NH2 . ARG C 3 190 ? 232.604 160.882 226.490 1.00 23.79 ? 190  ARG A NH2 1 
ATOM   2847 N N   . GLU C 3 191 ? 234.050 169.232 223.438 1.00 26.64 ? 191  GLU A N   1 
ATOM   2848 C CA  . GLU C 3 191 ? 234.435 170.631 223.441 1.00 27.21 ? 191  GLU A CA  1 
ATOM   2849 C C   . GLU C 3 191 ? 233.617 171.412 224.448 1.00 27.31 ? 191  GLU A C   1 
ATOM   2850 O O   . GLU C 3 191 ? 232.404 171.229 224.551 1.00 27.46 ? 191  GLU A O   1 
ATOM   2851 C CB  . GLU C 3 191 ? 234.264 171.224 222.044 1.00 27.79 ? 191  GLU A CB  1 
ATOM   2852 C CG  . GLU C 3 191 ? 235.186 170.618 221.001 1.00 29.27 ? 191  GLU A CG  1 
ATOM   2853 C CD  . GLU C 3 191 ? 234.899 171.091 219.612 1.00 30.79 ? 191  GLU A CD  1 
ATOM   2854 O OE1 . GLU C 3 191 ? 235.573 171.977 219.150 1.00 33.04 ? 191  GLU A OE1 1 
ATOM   2855 O OE2 . GLU C 3 191 ? 234.010 170.553 219.000 1.00 30.90 ? 191  GLU A OE2 1 
ATOM   2856 N N   . PHE C 3 192 ? 234.289 172.285 225.184 1.00 27.08 ? 192  PHE A N   1 
ATOM   2857 C CA  . PHE C 3 192 ? 233.649 173.127 226.180 1.00 27.05 ? 192  PHE A CA  1 
ATOM   2858 C C   . PHE C 3 192 ? 234.103 174.572 226.062 1.00 27.59 ? 192  PHE A C   1 
ATOM   2859 O O   . PHE C 3 192 ? 235.266 174.851 225.774 1.00 27.86 ? 192  PHE A O   1 
ATOM   2860 C CB  . PHE C 3 192 ? 233.975 172.632 227.587 1.00 25.88 ? 192  PHE A CB  1 
ATOM   2861 C CG  . PHE C 3 192 ? 233.501 171.254 227.879 1.00 25.29 ? 192  PHE A CG  1 
ATOM   2862 C CD1 . PHE C 3 192 ? 234.297 170.163 227.593 1.00 25.81 ? 192  PHE A CD1 1 
ATOM   2863 C CD2 . PHE C 3 192 ? 232.263 171.043 228.449 1.00 24.46 ? 192  PHE A CD2 1 
ATOM   2864 C CE1 . PHE C 3 192 ? 233.863 168.887 227.868 1.00 25.09 ? 192  PHE A CE1 1 
ATOM   2865 C CE2 . PHE C 3 192 ? 231.822 169.770 228.725 1.00 23.45 ? 192  PHE A CE2 1 
ATOM   2866 C CZ  . PHE C 3 192 ? 232.624 168.689 228.433 1.00 24.12 ? 192  PHE A CZ  1 
ATOM   2867 N N   . VAL C 3 193 ? 233.201 175.491 226.359 1.00 27.47 ? 193  VAL A N   1 
ATOM   2868 C CA  . VAL C 3 193 ? 233.564 176.893 226.490 1.00 26.06 ? 193  VAL A CA  1 
ATOM   2869 C C   . VAL C 3 193 ? 233.185 177.411 227.860 1.00 27.00 ? 193  VAL A C   1 
ATOM   2870 O O   . VAL C 3 193 ? 232.029 177.320 228.272 1.00 27.59 ? 193  VAL A O   1 
ATOM   2871 C CB  . VAL C 3 193 ? 232.906 177.738 225.392 1.00 28.08 ? 193  VAL A CB  1 
ATOM   2872 C CG1 . VAL C 3 193 ? 233.170 179.202 225.625 1.00 31.39 ? 193  VAL A CG1 1 
ATOM   2873 C CG2 . VAL C 3 193 ? 233.477 177.330 224.057 1.00 31.72 ? 193  VAL A CG2 1 
ATOM   2874 N N   . PHE C 3 194 ? 234.170 177.941 228.570 1.00 26.74 ? 194  PHE A N   1 
ATOM   2875 C CA  . PHE C 3 194 ? 233.967 178.410 229.930 1.00 26.70 ? 194  PHE A CA  1 
ATOM   2876 C C   . PHE C 3 194 ? 234.040 179.928 230.029 1.00 27.53 ? 194  PHE A C   1 
ATOM   2877 O O   . PHE C 3 194 ? 235.089 180.529 229.788 1.00 28.49 ? 194  PHE A O   1 
ATOM   2878 C CB  . PHE C 3 194 ? 235.020 177.800 230.850 1.00 26.32 ? 194  PHE A CB  1 
ATOM   2879 C CG  . PHE C 3 194 ? 234.983 176.302 230.913 1.00 25.63 ? 194  PHE A CG  1 
ATOM   2880 C CD1 . PHE C 3 194 ? 235.892 175.541 230.203 1.00 25.24 ? 194  PHE A CD1 1 
ATOM   2881 C CD2 . PHE C 3 194 ? 234.041 175.656 231.675 1.00 25.51 ? 194  PHE A CD2 1 
ATOM   2882 C CE1 . PHE C 3 194 ? 235.854 174.164 230.267 1.00 24.34 ? 194  PHE A CE1 1 
ATOM   2883 C CE2 . PHE C 3 194 ? 233.997 174.281 231.740 1.00 24.31 ? 194  PHE A CE2 1 
ATOM   2884 C CZ  . PHE C 3 194 ? 234.907 173.536 231.034 1.00 23.52 ? 194  PHE A CZ  1 
ATOM   2885 N N   . LYS C 3 195 ? 232.927 180.543 230.410 1.00 27.33 ? 195  LYS A N   1 
ATOM   2886 C CA  . LYS C 3 195 ? 232.857 181.992 230.576 1.00 26.83 ? 195  LYS A CA  1 
ATOM   2887 C C   . LYS C 3 195 ? 232.435 182.341 231.996 1.00 26.81 ? 195  LYS A C   1 
ATOM   2888 O O   . LYS C 3 195 ? 231.736 181.569 232.644 1.00 26.88 ? 195  LYS A O   1 
ATOM   2889 C CB  . LYS C 3 195 ? 231.869 182.596 229.581 1.00 28.38 ? 195  LYS A CB  1 
ATOM   2890 C CG  . LYS C 3 195 ? 232.295 182.498 228.123 1.00 30.54 ? 195  LYS A CG  1 
ATOM   2891 C CD  . LYS C 3 195 ? 231.112 182.717 227.185 1.00 33.33 ? 195  LYS A CD  1 
ATOM   2892 C CE  . LYS C 3 195 ? 230.560 184.132 227.296 1.00 35.74 ? 195  LYS A CE  1 
ATOM   2893 N NZ  . LYS C 3 195 ? 229.465 184.383 226.321 1.00 36.87 ? 195  LYS A NZ  1 
ATOM   2894 N N   . ASN C 3 196 ? 232.836 183.513 232.475 1.00 26.82 ? 196  ASN A N   1 
ATOM   2895 C CA  . ASN C 3 196 ? 232.445 183.946 233.815 1.00 26.74 ? 196  ASN A CA  1 
ATOM   2896 C C   . ASN C 3 196 ? 231.995 185.400 233.799 1.00 27.58 ? 196  ASN A C   1 
ATOM   2897 O O   . ASN C 3 196 ? 232.817 186.316 233.854 1.00 28.40 ? 196  ASN A O   1 
ATOM   2898 C CB  . ASN C 3 196 ? 233.587 183.742 234.794 1.00 26.36 ? 196  ASN A CB  1 
ATOM   2899 C CG  . ASN C 3 196 ? 233.196 184.001 236.233 1.00 26.51 ? 196  ASN A CG  1 
ATOM   2900 O OD1 . ASN C 3 196 ? 232.016 184.148 236.566 1.00 27.24 ? 196  ASN A OD1 1 
ATOM   2901 N ND2 . ASN C 3 196 ? 234.184 184.058 237.093 1.00 26.67 ? 196  ASN A ND2 1 
ATOM   2902 N N   . ILE C 3 197 ? 230.689 185.609 233.665 1.00 27.25 ? 197  ILE A N   1 
ATOM   2903 C CA  . ILE C 3 197 ? 230.148 186.952 233.503 1.00 27.29 ? 197  ILE A CA  1 
ATOM   2904 C C   . ILE C 3 197 ? 229.153 187.308 234.596 1.00 27.26 ? 197  ILE A C   1 
ATOM   2905 O O   . ILE C 3 197 ? 228.136 186.639 234.772 1.00 27.12 ? 197  ILE A O   1 
ATOM   2906 C CB  . ILE C 3 197 ? 229.483 187.109 232.125 1.00 26.99 ? 197  ILE A CB  1 
ATOM   2907 N N   . ASP C 3 198 ? 229.440 188.390 235.309 1.00 27.26 ? 198  ASP A N   1 
ATOM   2908 C CA  . ASP C 3 198 ? 228.569 188.887 236.367 1.00 27.07 ? 198  ASP A CA  1 
ATOM   2909 C C   . ASP C 3 198 ? 228.246 187.809 237.395 1.00 26.97 ? 198  ASP A C   1 
ATOM   2910 O O   . ASP C 3 198 ? 227.130 187.742 237.911 1.00 26.58 ? 198  ASP A O   1 
ATOM   2911 C CB  . ASP C 3 198 ? 227.276 189.449 235.774 1.00 26.80 ? 198  ASP A CB  1 
ATOM   2912 N N   . GLY C 3 199 ? 229.233 186.978 237.706 1.00 27.04 ? 199  GLY A N   1 
ATOM   2913 C CA  . GLY C 3 199 ? 229.078 185.950 238.727 1.00 27.17 ? 199  GLY A CA  1 
ATOM   2914 C C   . GLY C 3 199 ? 228.574 184.622 238.171 1.00 26.56 ? 199  GLY A C   1 
ATOM   2915 O O   . GLY C 3 199 ? 228.566 183.613 238.883 1.00 26.21 ? 199  GLY A O   1 
ATOM   2916 N N   . TYR C 3 200 ? 228.160 184.611 236.908 1.00 27.00 ? 200  TYR A N   1 
ATOM   2917 C CA  . TYR C 3 200 ? 227.648 183.388 236.309 1.00 26.72 ? 200  TYR A CA  1 
ATOM   2918 C C   . TYR C 3 200 ? 228.716 182.649 235.531 1.00 26.74 ? 200  TYR A C   1 
ATOM   2919 O O   . TYR C 3 200 ? 229.265 183.167 234.557 1.00 27.12 ? 200  TYR A O   1 
ATOM   2920 C CB  . TYR C 3 200 ? 226.466 183.690 235.395 1.00 26.44 ? 200  TYR A CB  1 
ATOM   2921 C CG  . TYR C 3 200 ? 225.203 183.993 236.127 1.00 25.73 ? 200  TYR A CG  1 
ATOM   2922 C CD1 . TYR C 3 200 ? 224.956 185.272 236.589 1.00 26.12 ? 200  TYR A CD1 1 
ATOM   2923 C CD2 . TYR C 3 200 ? 224.280 182.986 236.334 1.00 26.02 ? 200  TYR A CD2 1 
ATOM   2924 C CE1 . TYR C 3 200 ? 223.783 185.543 237.261 1.00 26.16 ? 200  TYR A CE1 1 
ATOM   2925 C CE2 . TYR C 3 200 ? 223.109 183.254 237.001 1.00 26.28 ? 200  TYR A CE2 1 
ATOM   2926 C CZ  . TYR C 3 200 ? 222.858 184.526 237.466 1.00 25.54 ? 200  TYR A CZ  1 
ATOM   2927 O OH  . TYR C 3 200 ? 221.687 184.794 238.135 1.00 25.63 ? 200  TYR A OH  1 
ATOM   2928 N N   . PHE C 3 201 ? 228.982 181.418 235.944 1.00 26.57 ? 201  PHE A N   1 
ATOM   2929 C CA  . PHE C 3 201 ? 229.929 180.580 235.239 1.00 26.38 ? 201  PHE A CA  1 
ATOM   2930 C C   . PHE C 3 201 ? 229.150 179.781 234.214 1.00 26.49 ? 201  PHE A C   1 
ATOM   2931 O O   . PHE C 3 201 ? 228.359 178.903 234.563 1.00 26.32 ? 201  PHE A O   1 
ATOM   2932 C CB  . PHE C 3 201 ? 230.675 179.661 236.204 1.00 25.58 ? 201  PHE A CB  1 
ATOM   2933 C CG  . PHE C 3 201 ? 231.878 179.001 235.610 1.00 24.31 ? 201  PHE A CG  1 
ATOM   2934 C CD1 . PHE C 3 201 ? 233.043 179.717 235.423 1.00 25.54 ? 201  PHE A CD1 1 
ATOM   2935 C CD2 . PHE C 3 201 ? 231.859 177.672 235.253 1.00 24.93 ? 201  PHE A CD2 1 
ATOM   2936 C CE1 . PHE C 3 201 ? 234.160 179.120 234.890 1.00 25.24 ? 201  PHE A CE1 1 
ATOM   2937 C CE2 . PHE C 3 201 ? 232.976 177.072 234.724 1.00 25.32 ? 201  PHE A CE2 1 
ATOM   2938 C CZ  . PHE C 3 201 ? 234.126 177.798 234.543 1.00 25.00 ? 201  PHE A CZ  1 
ATOM   2939 N N   . LYS C 3 202 ? 229.296 180.161 232.956 1.00 26.77 ? 202  LYS A N   1 
ATOM   2940 C CA  . LYS C 3 202 ? 228.479 179.604 231.895 1.00 26.85 ? 202  LYS A CA  1 
ATOM   2941 C C   . LYS C 3 202 ? 229.251 178.588 231.084 1.00 27.00 ? 202  LYS A C   1 
ATOM   2942 O O   . LYS C 3 202 ? 230.354 178.862 230.609 1.00 27.40 ? 202  LYS A O   1 
ATOM   2943 C CB  . LYS C 3 202 ? 227.950 180.718 230.997 1.00 27.91 ? 202  LYS A CB  1 
ATOM   2944 C CG  . LYS C 3 202 ? 227.013 181.682 231.707 1.00 28.05 ? 202  LYS A CG  1 
ATOM   2945 C CD  . LYS C 3 202 ? 226.435 182.708 230.752 1.00 26.88 ? 202  LYS A CD  1 
ATOM   2946 C CE  . LYS C 3 202 ? 225.490 183.657 231.475 1.00 26.58 ? 202  LYS A CE  1 
ATOM   2947 N NZ  . LYS C 3 202 ? 224.848 184.621 230.540 1.00 26.17 ? 202  LYS A NZ  1 
ATOM   2948 N N   . ILE C 3 203 ? 228.672 177.407 230.934 1.00 26.88 ? 203  ILE A N   1 
ATOM   2949 C CA  . ILE C 3 203 ? 229.323 176.345 230.190 1.00 26.57 ? 203  ILE A CA  1 
ATOM   2950 C C   . ILE C 3 203 ? 228.538 175.991 228.942 1.00 27.59 ? 203  ILE A C   1 
ATOM   2951 O O   . ILE C 3 203 ? 227.338 175.719 229.007 1.00 27.58 ? 203  ILE A O   1 
ATOM   2952 C CB  . ILE C 3 203 ? 229.495 175.085 231.057 1.00 25.87 ? 203  ILE A CB  1 
ATOM   2953 C CG1 . ILE C 3 203 ? 230.303 175.427 232.313 1.00 26.45 ? 203  ILE A CG1 1 
ATOM   2954 C CG2 . ILE C 3 203 ? 230.197 173.995 230.247 1.00 26.44 ? 203  ILE A CG2 1 
ATOM   2955 C CD1 . ILE C 3 203 ? 230.351 174.320 233.349 1.00 24.43 ? 203  ILE A CD1 1 
ATOM   2956 N N   . TYR C 3 204 ? 229.235 175.968 227.814 1.00 27.85 ? 204  TYR A N   1 
ATOM   2957 C CA  . TYR C 3 204 ? 228.676 175.514 226.546 1.00 28.55 ? 204  TYR A CA  1 
ATOM   2958 C C   . TYR C 3 204 ? 229.407 174.245 226.154 1.00 28.54 ? 204  TYR A C   1 
ATOM   2959 O O   . TYR C 3 204 ? 230.573 174.081 226.509 1.00 27.99 ? 204  TYR A O   1 
ATOM   2960 C CB  . TYR C 3 204 ? 228.849 176.576 225.462 1.00 30.24 ? 204  TYR A CB  1 
ATOM   2961 C CG  . TYR C 3 204 ? 228.167 177.880 225.759 1.00 31.42 ? 204  TYR A CG  1 
ATOM   2962 C CD1 . TYR C 3 204 ? 228.725 178.764 226.665 1.00 31.05 ? 204  TYR A CD1 1 
ATOM   2963 C CD2 . TYR C 3 204 ? 226.993 178.202 225.114 1.00 32.62 ? 204  TYR A CD2 1 
ATOM   2964 C CE1 . TYR C 3 204 ? 228.099 179.959 226.934 1.00 31.54 ? 204  TYR A CE1 1 
ATOM   2965 C CE2 . TYR C 3 204 ? 226.370 179.399 225.379 1.00 34.56 ? 204  TYR A CE2 1 
ATOM   2966 C CZ  . TYR C 3 204 ? 226.916 180.273 226.286 1.00 33.02 ? 204  TYR A CZ  1 
ATOM   2967 O OH  . TYR C 3 204 ? 226.287 181.467 226.550 1.00 33.93 ? 204  TYR A OH  1 
ATOM   2968 N N   . SER C 3 205 ? 228.749 173.342 225.434 1.00 28.78 ? 205  SER A N   1 
ATOM   2969 C CA  . SER C 3 205 ? 229.427 172.105 225.071 1.00 28.04 ? 205  SER A CA  1 
ATOM   2970 C C   . SER C 3 205 ? 228.910 171.440 223.803 1.00 28.82 ? 205  SER A C   1 
ATOM   2971 O O   . SER C 3 205 ? 227.802 171.707 223.333 1.00 29.99 ? 205  SER A O   1 
ATOM   2972 C CB  . SER C 3 205 ? 229.334 171.112 226.210 1.00 27.36 ? 205  SER A CB  1 
ATOM   2973 O OG  . SER C 3 205 ? 228.015 170.687 226.401 1.00 26.32 ? 205  SER A OG  1 
ATOM   2974 N N   . LYS C 3 206 ? 229.737 170.546 223.268 1.00 27.93 ? 206  LYS A N   1 
ATOM   2975 C CA  . LYS C 3 206 ? 229.386 169.702 222.134 1.00 27.07 ? 206  LYS A CA  1 
ATOM   2976 C C   . LYS C 3 206 ? 230.117 168.365 222.232 1.00 28.35 ? 206  LYS A C   1 
ATOM   2977 O O   . LYS C 3 206 ? 231.293 168.319 222.595 1.00 28.17 ? 206  LYS A O   1 
ATOM   2978 C CB  . LYS C 3 206 ? 229.729 170.402 220.817 1.00 29.17 ? 206  LYS A CB  1 
ATOM   2979 C CG  . LYS C 3 206 ? 229.313 169.653 219.561 1.00 29.53 ? 206  LYS A CG  1 
ATOM   2980 C CD  . LYS C 3 206 ? 227.833 169.840 219.257 1.00 29.59 ? 206  LYS A CD  1 
ATOM   2981 C CE  . LYS C 3 206 ? 227.413 169.032 218.036 1.00 29.31 ? 206  LYS A CE  1 
ATOM   2982 N NZ  . LYS C 3 206 ? 225.980 169.242 217.695 1.00 28.09 ? 206  LYS A NZ  1 
ATOM   2983 N N   . HIS C 3 207 ? 229.426 167.277 221.908 1.00 28.59 ? 207  HIS A N   1 
ATOM   2984 C CA  . HIS C 3 207 ? 230.042 165.952 221.911 1.00 27.98 ? 207  HIS A CA  1 
ATOM   2985 C C   . HIS C 3 207 ? 229.827 165.231 220.586 1.00 28.31 ? 207  HIS A C   1 
ATOM   2986 O O   . HIS C 3 207 ? 228.694 164.937 220.204 1.00 29.41 ? 207  HIS A O   1 
ATOM   2987 C CB  . HIS C 3 207 ? 229.488 165.105 223.062 1.00 27.09 ? 207  HIS A CB  1 
ATOM   2988 C CG  . HIS C 3 207 ? 230.026 163.695 223.122 1.00 27.64 ? 207  HIS A CG  1 
ATOM   2989 N ND1 . HIS C 3 207 ? 229.398 162.700 223.841 1.00 26.40 ? 207  HIS A ND1 1 
ATOM   2990 C CD2 . HIS C 3 207 ? 231.116 163.114 222.556 1.00 28.03 ? 207  HIS A CD2 1 
ATOM   2991 C CE1 . HIS C 3 207 ? 230.073 161.572 223.711 1.00 26.58 ? 207  HIS A CE1 1 
ATOM   2992 N NE2 . HIS C 3 207 ? 231.114 161.795 222.936 1.00 27.81 ? 207  HIS A NE2 1 
ATOM   2993 N N   . THR C 3 208 ? 230.922 164.967 219.881 1.00 28.51 ? 208  THR A N   1 
ATOM   2994 C CA  . THR C 3 208 ? 230.875 164.275 218.599 1.00 28.66 ? 208  THR A CA  1 
ATOM   2995 C C   . THR C 3 208 ? 231.948 163.190 218.564 1.00 29.33 ? 208  THR A C   1 
ATOM   2996 O O   . THR C 3 208 ? 232.915 163.262 219.319 1.00 29.41 ? 208  THR A O   1 
ATOM   2997 C CB  . THR C 3 208 ? 231.105 165.264 217.436 1.00 28.55 ? 208  THR A CB  1 
ATOM   2998 O OG1 . THR C 3 208 ? 232.429 165.802 217.523 1.00 29.47 ? 208  THR A OG1 1 
ATOM   2999 C CG2 . THR C 3 208 ? 230.105 166.396 217.506 1.00 28.34 ? 208  THR A CG2 1 
ATOM   3000 N N   . PRO C 3 209 ? 231.789 162.168 217.722 1.00 29.52 ? 209  PRO A N   1 
ATOM   3001 C CA  . PRO C 3 209 ? 232.802 161.192 217.369 1.00 30.56 ? 209  PRO A CA  1 
ATOM   3002 C C   . PRO C 3 209 ? 233.858 161.824 216.474 1.00 31.50 ? 209  PRO A C   1 
ATOM   3003 O O   . PRO C 3 209 ? 233.545 162.690 215.657 1.00 31.69 ? 209  PRO A O   1 
ATOM   3004 C CB  . PRO C 3 209 ? 231.987 160.118 216.640 1.00 31.41 ? 209  PRO A CB  1 
ATOM   3005 C CG  . PRO C 3 209 ? 230.782 160.858 216.089 1.00 29.92 ? 209  PRO A CG  1 
ATOM   3006 C CD  . PRO C 3 209 ? 230.479 161.941 217.110 1.00 29.42 ? 209  PRO A CD  1 
ATOM   3007 N N   . ILE C 3 210 ? 235.097 161.371 216.611 1.00 32.45 ? 210  ILE A N   1 
ATOM   3008 C CA  . ILE C 3 210 ? 236.178 161.831 215.752 1.00 33.48 ? 210  ILE A CA  1 
ATOM   3009 C C   . ILE C 3 210 ? 237.028 160.661 215.257 1.00 34.21 ? 210  ILE A C   1 
ATOM   3010 O O   . ILE C 3 210 ? 237.304 159.717 216.000 1.00 33.88 ? 210  ILE A O   1 
ATOM   3011 C CB  . ILE C 3 210 ? 237.035 162.884 216.481 1.00 33.52 ? 210  ILE A CB  1 
ATOM   3012 C CG1 . ILE C 3 210 ? 238.095 163.445 215.545 1.00 35.20 ? 210  ILE A CG1 1 
ATOM   3013 C CG2 . ILE C 3 210 ? 237.672 162.291 217.725 1.00 32.97 ? 210  ILE A CG2 1 
ATOM   3014 C CD1 . ILE C 3 210 ? 238.697 164.728 216.026 1.00 35.13 ? 210  ILE A CD1 1 
ATOM   3015 N N   . ASN C 3 211 ? 237.434 160.722 213.989 1.00 34.95 ? 211  ASN A N   1 
ATOM   3016 C CA  . ASN C 3 211 ? 238.212 159.645 213.381 1.00 35.19 ? 211  ASN A CA  1 
ATOM   3017 C C   . ASN C 3 211 ? 239.665 160.034 213.119 1.00 35.61 ? 211  ASN A C   1 
ATOM   3018 O O   . ASN C 3 211 ? 240.354 159.390 212.327 1.00 35.27 ? 211  ASN A O   1 
ATOM   3019 C CB  . ASN C 3 211 ? 237.548 159.179 212.100 1.00 35.05 ? 211  ASN A CB  1 
ATOM   3020 N N   . LEU C 3 212 ? 240.131 161.078 213.789 1.00 35.81 ? 212  LEU A N   1 
ATOM   3021 C CA  . LEU C 3 212 ? 241.522 161.499 213.669 1.00 36.30 ? 212  LEU A CA  1 
ATOM   3022 C C   . LEU C 3 212 ? 242.346 160.880 214.783 1.00 36.53 ? 212  LEU A C   1 
ATOM   3023 O O   . LEU C 3 212 ? 241.814 160.520 215.833 1.00 35.76 ? 212  LEU A O   1 
ATOM   3024 C CB  . LEU C 3 212 ? 241.654 163.027 213.718 1.00 36.26 ? 212  LEU A CB  1 
ATOM   3025 C CG  . LEU C 3 212 ? 240.886 163.819 212.646 1.00 36.56 ? 212  LEU A CG  1 
ATOM   3026 C CD1 . LEU C 3 212 ? 241.188 165.303 212.819 1.00 37.08 ? 212  LEU A CD1 1 
ATOM   3027 C CD2 . LEU C 3 212 ? 241.288 163.342 211.256 1.00 37.58 ? 212  LEU A CD2 1 
ATOM   3028 N N   . VAL C 3 213 ? 243.643 160.742 214.548 1.00 37.05 ? 213  VAL A N   1 
ATOM   3029 C CA  . VAL C 3 213 ? 244.521 160.109 215.521 1.00 37.72 ? 213  VAL A CA  1 
ATOM   3030 C C   . VAL C 3 213 ? 244.879 161.028 216.685 1.00 37.24 ? 213  VAL A C   1 
ATOM   3031 O O   . VAL C 3 213 ? 244.796 160.626 217.847 1.00 36.99 ? 213  VAL A O   1 
ATOM   3032 C CB  . VAL C 3 213 ? 245.812 159.628 214.829 1.00 38.51 ? 213  VAL A CB  1 
ATOM   3033 N N   . ARG C 3 214 ? 245.317 162.247 216.380 1.00 37.02 ? 214  ARG A N   1 
ATOM   3034 C CA  . ARG C 3 214 ? 245.789 163.137 217.434 1.00 36.99 ? 214  ARG A CA  1 
ATOM   3035 C C   . ARG C 3 214 ? 245.673 164.618 217.089 1.00 36.18 ? 214  ARG A C   1 
ATOM   3036 O O   . ARG C 3 214 ? 246.606 165.383 217.329 1.00 35.32 ? 214  ARG A O   1 
ATOM   3037 C CB  . ARG C 3 214 ? 247.239 162.818 217.772 1.00 37.13 ? 214  ARG A CB  1 
ATOM   3038 N N   . ASP C 3 215 ? 244.539 165.033 216.536 1.00 36.06 ? 215  ASP A N   1 
ATOM   3039 C CA  . ASP C 3 215 ? 244.364 166.447 216.226 1.00 35.41 ? 215  ASP A CA  1 
ATOM   3040 C C   . ASP C 3 215 ? 242.896 166.851 216.199 1.00 35.40 ? 215  ASP A C   1 
ATOM   3041 O O   . ASP C 3 215 ? 242.005 166.009 216.303 1.00 35.52 ? 215  ASP A O   1 
ATOM   3042 C CB  . ASP C 3 215 ? 245.016 166.775 214.877 1.00 36.12 ? 215  ASP A CB  1 
ATOM   3043 N N   . LEU C 3 216 ? 242.657 168.143 216.011 1.00 35.00 ? 216  LEU A N   1 
ATOM   3044 C CA  . LEU C 3 216 ? 241.310 168.682 215.916 1.00 35.65 ? 216  LEU A CA  1 
ATOM   3045 C C   . LEU C 3 216 ? 240.811 168.586 214.478 1.00 36.75 ? 216  LEU A C   1 
ATOM   3046 O O   . LEU C 3 216 ? 241.608 168.659 213.543 1.00 37.45 ? 216  LEU A O   1 
ATOM   3047 C CB  . LEU C 3 216 ? 241.304 170.143 216.398 1.00 35.15 ? 216  LEU A CB  1 
ATOM   3048 C CG  . LEU C 3 216 ? 241.685 170.367 217.884 1.00 34.48 ? 216  LEU A CG  1 
ATOM   3049 C CD1 . LEU C 3 216 ? 241.791 171.862 218.159 1.00 34.14 ? 216  LEU A CD1 1 
ATOM   3050 C CD2 . LEU C 3 216 ? 240.629 169.731 218.790 1.00 33.67 ? 216  LEU A CD2 1 
ATOM   3051 N N   . PRO C 3 217 ? 239.503 168.408 214.283 1.00 37.08 ? 217  PRO A N   1 
ATOM   3052 C CA  . PRO C 3 217 ? 238.825 168.297 213.008 1.00 38.52 ? 217  PRO A CA  1 
ATOM   3053 C C   . PRO C 3 217 ? 238.745 169.635 212.296 1.00 40.43 ? 217  PRO A C   1 
ATOM   3054 O O   . PRO C 3 217 ? 238.713 170.687 212.936 1.00 40.47 ? 217  PRO A O   1 
ATOM   3055 C CB  . PRO C 3 217 ? 237.444 167.789 213.420 1.00 38.43 ? 217  PRO A CB  1 
ATOM   3056 C CG  . PRO C 3 217 ? 237.245 168.329 214.815 1.00 37.98 ? 217  PRO A CG  1 
ATOM   3057 C CD  . PRO C 3 217 ? 238.621 168.328 215.446 1.00 36.64 ? 217  PRO A CD  1 
ATOM   3058 N N   . GLN C 3 218 ? 238.670 169.586 210.971 1.00 41.44 ? 218  GLN A N   1 
ATOM   3059 C CA  . GLN C 3 218 ? 238.497 170.788 210.171 1.00 42.68 ? 218  GLN A CA  1 
ATOM   3060 C C   . GLN C 3 218 ? 237.081 170.867 209.623 1.00 42.54 ? 218  GLN A C   1 
ATOM   3061 O O   . GLN C 3 218 ? 236.690 170.084 208.757 1.00 42.19 ? 218  GLN A O   1 
ATOM   3062 C CB  . GLN C 3 218 ? 239.517 170.825 209.033 1.00 42.89 ? 218  GLN A CB  1 
ATOM   3063 N N   . GLY C 3 219 ? 236.311 171.805 210.154 1.00 42.38 ? 219  GLY A N   1 
ATOM   3064 C CA  . GLY C 3 219 ? 234.906 171.961 209.808 1.00 42.76 ? 219  GLY A CA  1 
ATOM   3065 C C   . GLY C 3 219 ? 234.232 172.837 210.848 1.00 43.61 ? 219  GLY A C   1 
ATOM   3066 O O   . GLY C 3 219 ? 234.892 173.351 211.749 1.00 43.77 ? 219  GLY A O   1 
ATOM   3067 N N   . PHE C 3 220 ? 232.925 173.028 210.725 1.00 44.24 ? 220  PHE A N   1 
ATOM   3068 C CA  . PHE C 3 220 ? 232.229 173.895 211.666 1.00 44.67 ? 220  PHE A CA  1 
ATOM   3069 C C   . PHE C 3 220 ? 231.195 173.150 212.496 1.00 44.13 ? 220  PHE A C   1 
ATOM   3070 O O   . PHE C 3 220 ? 230.408 172.363 211.971 1.00 44.30 ? 220  PHE A O   1 
ATOM   3071 C CB  . PHE C 3 220 ? 231.541 175.045 210.939 1.00 46.47 ? 220  PHE A CB  1 
ATOM   3072 C CG  . PHE C 3 220 ? 230.832 175.951 211.878 1.00 47.31 ? 220  PHE A CG  1 
ATOM   3073 C CD1 . PHE C 3 220 ? 231.494 177.012 212.468 1.00 47.55 ? 220  PHE A CD1 1 
ATOM   3074 C CD2 . PHE C 3 220 ? 229.511 175.725 212.205 1.00 48.14 ? 220  PHE A CD2 1 
ATOM   3075 C CE1 . PHE C 3 220 ? 230.845 177.829 213.360 1.00 47.76 ? 220  PHE A CE1 1 
ATOM   3076 C CE2 . PHE C 3 220 ? 228.863 176.534 213.097 1.00 48.89 ? 220  PHE A CE2 1 
ATOM   3077 C CZ  . PHE C 3 220 ? 229.528 177.591 213.677 1.00 48.37 ? 220  PHE A CZ  1 
ATOM   3078 N N   . SER C 3 221 ? 231.184 173.435 213.794 1.00 43.31 ? 221  SER A N   1 
ATOM   3079 C CA  . SER C 3 221 ? 230.183 172.897 214.704 1.00 42.13 ? 221  SER A CA  1 
ATOM   3080 C C   . SER C 3 221 ? 229.957 173.854 215.867 1.00 41.44 ? 221  SER A C   1 
ATOM   3081 O O   . SER C 3 221 ? 230.902 174.226 216.564 1.00 40.76 ? 221  SER A O   1 
ATOM   3082 C CB  . SER C 3 221 ? 230.617 171.544 215.220 1.00 39.31 ? 221  SER A CB  1 
ATOM   3083 O OG  . SER C 3 221 ? 229.675 171.019 216.110 1.00 37.11 ? 221  SER A OG  1 
ATOM   3084 N N   . ALA C 3 222 ? 228.710 174.271 216.063 1.00 41.31 ? 222  ALA A N   1 
ATOM   3085 C CA  . ALA C 3 222 ? 228.386 175.219 217.125 1.00 39.24 ? 222  ALA A CA  1 
ATOM   3086 C C   . ALA C 3 222 ? 228.106 174.498 218.437 1.00 37.32 ? 222  ALA A C   1 
ATOM   3087 O O   . ALA C 3 222 ? 227.473 173.442 218.454 1.00 36.12 ? 222  ALA A O   1 
ATOM   3088 C CB  . ALA C 3 222 ? 227.190 176.072 216.731 1.00 43.40 ? 222  ALA A CB  1 
ATOM   3089 N N   . LEU C 3 223 ? 228.539 175.105 219.536 1.00 36.74 ? 223  LEU A N   1 
ATOM   3090 C CA  . LEU C 3 223 ? 228.321 174.556 220.870 1.00 33.72 ? 223  LEU A CA  1 
ATOM   3091 C C   . LEU C 3 223 ? 227.046 175.104 221.492 1.00 33.98 ? 223  LEU A C   1 
ATOM   3092 O O   . LEU C 3 223 ? 226.701 176.270 221.297 1.00 36.24 ? 223  LEU A O   1 
ATOM   3093 C CB  . LEU C 3 223 ? 229.510 174.887 221.776 1.00 32.74 ? 223  LEU A CB  1 
ATOM   3094 C CG  . LEU C 3 223 ? 230.722 173.944 221.703 1.00 31.47 ? 223  LEU A CG  1 
ATOM   3095 C CD1 . LEU C 3 223 ? 231.322 173.965 220.308 1.00 32.70 ? 223  LEU A CD1 1 
ATOM   3096 C CD2 . LEU C 3 223 ? 231.739 174.386 222.718 1.00 30.82 ? 223  LEU A CD2 1 
ATOM   3097 N N   . GLU C 3 224 ? 226.346 174.259 222.242 1.00 31.86 ? 224  GLU A N   1 
ATOM   3098 C CA  . GLU C 3 224 ? 225.087 174.646 222.865 1.00 31.19 ? 224  GLU A CA  1 
ATOM   3099 C C   . GLU C 3 224 ? 225.268 174.863 224.367 1.00 30.28 ? 224  GLU A C   1 
ATOM   3100 O O   . GLU C 3 224 ? 226.164 174.273 224.964 1.00 29.63 ? 224  GLU A O   1 
ATOM   3101 C CB  . GLU C 3 224 ? 224.034 173.565 222.618 1.00 31.18 ? 224  GLU A CB  1 
ATOM   3102 N N   . PRO C 3 225 ? 224.439 175.701 224.996 1.00 29.85 ? 225  PRO A N   1 
ATOM   3103 C CA  . PRO C 3 225 ? 224.391 175.939 226.426 1.00 28.45 ? 225  PRO A CA  1 
ATOM   3104 C C   . PRO C 3 225 ? 224.217 174.636 227.188 1.00 27.66 ? 225  PRO A C   1 
ATOM   3105 O O   . PRO C 3 225 ? 223.396 173.798 226.818 1.00 29.29 ? 225  PRO A O   1 
ATOM   3106 C CB  . PRO C 3 225 ? 223.151 176.828 226.566 1.00 29.17 ? 225  PRO A CB  1 
ATOM   3107 C CG  . PRO C 3 225 ? 223.042 177.539 225.240 1.00 30.79 ? 225  PRO A CG  1 
ATOM   3108 C CD  . PRO C 3 225 ? 223.510 176.527 224.214 1.00 32.00 ? 225  PRO A CD  1 
ATOM   3109 N N   . LEU C 3 226 ? 224.976 174.480 228.265 1.00 27.20 ? 226  LEU A N   1 
ATOM   3110 C CA  . LEU C 3 226 ? 224.902 173.285 229.093 1.00 25.82 ? 226  LEU A CA  1 
ATOM   3111 C C   . LEU C 3 226 ? 224.341 173.606 230.470 1.00 25.01 ? 226  LEU A C   1 
ATOM   3112 O O   . LEU C 3 226 ? 223.371 172.991 230.913 1.00 25.47 ? 226  LEU A O   1 
ATOM   3113 C CB  . LEU C 3 226 ? 226.297 172.661 229.228 1.00 25.96 ? 226  LEU A CB  1 
ATOM   3114 C CG  . LEU C 3 226 ? 226.411 171.390 230.074 1.00 24.27 ? 226  LEU A CG  1 
ATOM   3115 C CD1 . LEU C 3 226 ? 225.591 170.276 229.449 1.00 23.77 ? 226  LEU A CD1 1 
ATOM   3116 C CD2 . LEU C 3 226 ? 227.873 170.999 230.159 1.00 25.12 ? 226  LEU A CD2 1 
ATOM   3117 N N   . VAL C 3 227 ? 224.965 174.562 231.152 1.00 25.27 ? 227  VAL A N   1 
ATOM   3118 C CA  . VAL C 3 227 ? 224.521 174.948 232.486 1.00 25.10 ? 227  VAL A CA  1 
ATOM   3119 C C   . VAL C 3 227 ? 224.961 176.364 232.855 1.00 25.94 ? 227  VAL A C   1 
ATOM   3120 O O   . VAL C 3 227 ? 226.078 176.781 232.543 1.00 25.95 ? 227  VAL A O   1 
ATOM   3121 C CB  . VAL C 3 227 ? 225.038 173.931 233.530 1.00 24.31 ? 227  VAL A CB  1 
ATOM   3122 C CG1 . VAL C 3 227 ? 226.556 173.903 233.540 1.00 25.40 ? 227  VAL A CG1 1 
ATOM   3123 C CG2 . VAL C 3 227 ? 224.506 174.285 234.916 1.00 24.89 ? 227  VAL A CG2 1 
ATOM   3124 N N   . ASP C 3 228 ? 224.084 177.084 233.551 1.00 25.41 ? 228  ASP A N   1 
ATOM   3125 C CA  . ASP C 3 228 ? 224.391 178.418 234.060 1.00 24.74 ? 228  ASP A CA  1 
ATOM   3126 C C   . ASP C 3 228 ? 224.534 178.376 235.574 1.00 25.15 ? 228  ASP A C   1 
ATOM   3127 O O   . ASP C 3 228 ? 223.562 178.117 236.283 1.00 25.88 ? 228  ASP A O   1 
ATOM   3128 C CB  . ASP C 3 228 ? 223.284 179.409 233.693 1.00 25.70 ? 228  ASP A CB  1 
ATOM   3129 C CG  . ASP C 3 228 ? 223.116 179.623 232.189 1.00 27.63 ? 228  ASP A CG  1 
ATOM   3130 O OD1 . ASP C 3 228 ? 223.992 179.260 231.445 1.00 26.90 ? 228  ASP A OD1 1 
ATOM   3131 O OD2 . ASP C 3 228 ? 222.092 180.144 231.803 1.00 27.40 ? 228  ASP A OD2 1 
ATOM   3132 N N   . LEU C 3 229 ? 225.744 178.597 236.072 1.00 25.54 ? 229  LEU A N   1 
ATOM   3133 C CA  . LEU C 3 229 ? 225.999 178.475 237.503 1.00 25.14 ? 229  LEU A CA  1 
ATOM   3134 C C   . LEU C 3 229 ? 226.163 179.838 238.196 1.00 25.52 ? 229  LEU A C   1 
ATOM   3135 O O   . LEU C 3 229 ? 227.165 180.523 237.986 1.00 25.83 ? 229  LEU A O   1 
ATOM   3136 C CB  . LEU C 3 229 ? 227.266 177.647 237.716 1.00 24.62 ? 229  LEU A CB  1 
ATOM   3137 C CG  . LEU C 3 229 ? 227.284 176.260 237.056 1.00 24.79 ? 229  LEU A CG  1 
ATOM   3138 C CD1 . LEU C 3 229 ? 228.693 175.712 237.099 1.00 23.68 ? 229  LEU A CD1 1 
ATOM   3139 C CD2 . LEU C 3 229 ? 226.329 175.328 237.793 1.00 24.08 ? 229  LEU A CD2 1 
ATOM   3140 N N   . PRO C 3 230 ? 225.214 180.232 239.055 1.00 25.20 ? 230  PRO A N   1 
ATOM   3141 C CA  . PRO C 3 230 ? 225.168 181.483 239.794 1.00 25.50 ? 230  PRO A CA  1 
ATOM   3142 C C   . PRO C 3 230 ? 226.097 181.423 240.998 1.00 25.61 ? 230  PRO A C   1 
ATOM   3143 O O   . PRO C 3 230 ? 225.650 181.180 242.119 1.00 26.13 ? 230  PRO A O   1 
ATOM   3144 C CB  . PRO C 3 230 ? 223.700 181.553 240.216 1.00 25.55 ? 230  PRO A CB  1 
ATOM   3145 C CG  . PRO C 3 230 ? 223.294 180.106 240.388 1.00 25.75 ? 230  PRO A CG  1 
ATOM   3146 C CD  . PRO C 3 230 ? 224.081 179.340 239.328 1.00 25.02 ? 230  PRO A CD  1 
ATOM   3147 N N   . ILE C 3 231 ? 227.396 181.543 240.750 1.00 25.25 ? 231  ILE A N   1 
ATOM   3148 C CA  . ILE C 3 231 ? 228.385 181.282 241.788 1.00 24.46 ? 231  ILE A CA  1 
ATOM   3149 C C   . ILE C 3 231 ? 228.937 182.538 242.460 1.00 25.12 ? 231  ILE A C   1 
ATOM   3150 O O   . ILE C 3 231 ? 228.985 182.610 243.688 1.00 25.38 ? 231  ILE A O   1 
ATOM   3151 C CB  . ILE C 3 231 ? 229.536 180.451 241.224 1.00 24.95 ? 231  ILE A CB  1 
ATOM   3152 C CG1 . ILE C 3 231 ? 229.016 179.084 240.796 1.00 25.08 ? 231  ILE A CG1 1 
ATOM   3153 C CG2 . ILE C 3 231 ? 230.601 180.320 242.268 1.00 26.18 ? 231  ILE A CG2 1 
ATOM   3154 C CD1 . ILE C 3 231 ? 229.987 178.302 239.955 1.00 24.94 ? 231  ILE A CD1 1 
ATOM   3155 N N   . GLY C 3 232 ? 229.379 183.511 241.668 1.00 24.96 ? 232  GLY A N   1 
ATOM   3156 C CA  . GLY C 3 232 ? 229.909 184.756 242.225 1.00 25.79 ? 232  GLY A CA  1 
ATOM   3157 C C   . GLY C 3 232 ? 231.348 184.679 242.757 1.00 25.99 ? 232  GLY A C   1 
ATOM   3158 O O   . GLY C 3 232 ? 231.647 185.254 243.803 1.00 25.26 ? 232  GLY A O   1 
ATOM   3159 N N   . ILE C 3 233 ? 232.244 183.990 242.047 1.00 25.95 ? 233  ILE A N   1 
ATOM   3160 C CA  . ILE C 3 233 ? 233.642 183.921 242.488 1.00 25.94 ? 233  ILE A CA  1 
ATOM   3161 C C   . ILE C 3 233 ? 234.619 184.423 241.423 1.00 27.25 ? 233  ILE A C   1 
ATOM   3162 O O   . ILE C 3 233 ? 234.270 184.527 240.243 1.00 27.61 ? 233  ILE A O   1 
ATOM   3163 C CB  . ILE C 3 233 ? 234.050 182.492 242.904 1.00 25.42 ? 233  ILE A CB  1 
ATOM   3164 C CG1 . ILE C 3 233 ? 233.895 181.538 241.702 1.00 25.33 ? 233  ILE A CG1 1 
ATOM   3165 C CG2 . ILE C 3 233 ? 233.255 182.052 244.134 1.00 26.07 ? 233  ILE A CG2 1 
ATOM   3166 C CD1 . ILE C 3 233 ? 234.462 180.153 241.928 1.00 25.98 ? 233  ILE A CD1 1 
ATOM   3167 N N   . ASN C 3 234 ? 235.843 184.732 241.870 1.00 26.64 ? 234  ASN A N   1 
ATOM   3168 C CA  . ASN C 3 234 ? 236.950 185.193 241.036 1.00 26.97 ? 234  ASN A CA  1 
ATOM   3169 C C   . ASN C 3 234 ? 237.754 184.011 240.495 1.00 27.05 ? 234  ASN A C   1 
ATOM   3170 O O   . ASN C 3 234 ? 238.242 183.182 241.266 1.00 26.92 ? 234  ASN A O   1 
ATOM   3171 C CB  . ASN C 3 234 ? 237.844 186.139 241.832 1.00 28.79 ? 234  ASN A CB  1 
ATOM   3172 C CG  . ASN C 3 234 ? 238.888 186.867 240.988 1.00 29.18 ? 234  ASN A CG  1 
ATOM   3173 O OD1 . ASN C 3 234 ? 238.790 186.922 239.753 1.00 28.94 ? 234  ASN A OD1 1 
ATOM   3174 N ND2 . ASN C 3 234 ? 239.879 187.428 241.655 1.00 29.82 ? 234  ASN A ND2 1 
ATOM   3175 N N   . ILE C 3 235 ? 237.872 183.923 239.164 1.00 26.83 ? 235  ILE A N   1 
ATOM   3176 C CA  . ILE C 3 235 ? 238.627 182.865 238.487 1.00 26.54 ? 235  ILE A CA  1 
ATOM   3177 C C   . ILE C 3 235 ? 239.710 183.460 237.598 1.00 26.88 ? 235  ILE A C   1 
ATOM   3178 O O   . ILE C 3 235 ? 239.421 184.272 236.720 1.00 27.72 ? 235  ILE A O   1 
ATOM   3179 C CB  . ILE C 3 235 ? 237.691 181.979 237.642 1.00 25.17 ? 235  ILE A CB  1 
ATOM   3180 C CG1 . ILE C 3 235 ? 236.657 181.297 238.559 1.00 25.87 ? 235  ILE A CG1 1 
ATOM   3181 C CG2 . ILE C 3 235 ? 238.503 180.948 236.860 1.00 25.82 ? 235  ILE A CG2 1 
ATOM   3182 C CD1 . ILE C 3 235 ? 235.533 180.601 237.823 1.00 27.10 ? 235  ILE A CD1 1 
ATOM   3183 N N   . THR C 3 236 ? 240.956 183.055 237.828 1.00 26.46 ? 236  THR A N   1 
ATOM   3184 C CA  . THR C 3 236 ? 242.077 183.540 237.032 1.00 26.11 ? 236  THR A CA  1 
ATOM   3185 C C   . THR C 3 236 ? 242.895 182.397 236.444 1.00 26.34 ? 236  THR A C   1 
ATOM   3186 O O   . THR C 3 236 ? 243.627 182.591 235.472 1.00 26.24 ? 236  THR A O   1 
ATOM   3187 C CB  . THR C 3 236 ? 242.996 184.456 237.858 1.00 26.02 ? 236  THR A CB  1 
ATOM   3188 O OG1 . THR C 3 236 ? 243.516 183.733 238.980 1.00 27.26 ? 236  THR A OG1 1 
ATOM   3189 C CG2 . THR C 3 236 ? 242.229 185.668 238.351 1.00 28.16 ? 236  THR A CG2 1 
ATOM   3190 N N   . ARG C 3 237 ? 242.784 181.216 237.048 1.00 26.06 ? 237  ARG A N   1 
ATOM   3191 C CA  . ARG C 3 237 ? 243.541 180.038 236.633 1.00 25.58 ? 237  ARG A CA  1 
ATOM   3192 C C   . ARG C 3 237 ? 242.674 178.786 236.693 1.00 25.31 ? 237  ARG A C   1 
ATOM   3193 O O   . ARG C 3 237 ? 241.702 178.735 237.449 1.00 25.25 ? 237  ARG A O   1 
ATOM   3194 C CB  . ARG C 3 237 ? 244.754 179.832 237.525 1.00 25.53 ? 237  ARG A CB  1 
ATOM   3195 C CG  . ARG C 3 237 ? 245.747 180.976 237.545 1.00 25.59 ? 237  ARG A CG  1 
ATOM   3196 C CD  . ARG C 3 237 ? 247.007 180.586 238.218 1.00 25.45 ? 237  ARG A CD  1 
ATOM   3197 N NE  . ARG C 3 237 ? 246.797 180.254 239.620 1.00 25.54 ? 237  ARG A NE  1 
ATOM   3198 C CZ  . ARG C 3 237 ? 247.657 179.553 240.383 1.00 25.88 ? 237  ARG A CZ  1 
ATOM   3199 N NH1 . ARG C 3 237 ? 247.358 179.321 241.640 1.00 26.30 ? 237  ARG A NH1 1 
ATOM   3200 N NH2 . ARG C 3 237 ? 248.792 179.102 239.874 1.00 25.13 ? 237  ARG A NH2 1 
ATOM   3201 N N   . PHE C 3 238 ? 243.061 177.750 235.952 1.00 25.00 ? 238  PHE A N   1 
ATOM   3202 C CA  . PHE C 3 238 ? 242.361 176.479 236.048 1.00 24.57 ? 238  PHE A CA  1 
ATOM   3203 C C   . PHE C 3 238 ? 243.292 175.297 235.814 1.00 24.20 ? 238  PHE A C   1 
ATOM   3204 O O   . PHE C 3 238 ? 244.371 175.442 235.242 1.00 24.67 ? 238  PHE A O   1 
ATOM   3205 C CB  . PHE C 3 238 ? 241.212 176.423 235.048 1.00 24.23 ? 238  PHE A CB  1 
ATOM   3206 C CG  . PHE C 3 238 ? 241.628 176.176 233.643 1.00 23.87 ? 238  PHE A CG  1 
ATOM   3207 C CD1 . PHE C 3 238 ? 241.553 174.900 233.114 1.00 23.59 ? 238  PHE A CD1 1 
ATOM   3208 C CD2 . PHE C 3 238 ? 242.094 177.198 232.844 1.00 25.25 ? 238  PHE A CD2 1 
ATOM   3209 C CE1 . PHE C 3 238 ? 241.930 174.651 231.817 1.00 24.00 ? 238  PHE A CE1 1 
ATOM   3210 C CE2 . PHE C 3 238 ? 242.475 176.950 231.543 1.00 25.86 ? 238  PHE A CE2 1 
ATOM   3211 C CZ  . PHE C 3 238 ? 242.390 175.675 231.031 1.00 25.44 ? 238  PHE A CZ  1 
ATOM   3212 N N   . GLN C 3 239 ? 242.863 174.121 236.255 1.00 23.69 ? 239  GLN A N   1 
ATOM   3213 C CA  . GLN C 3 239 ? 243.654 172.905 236.102 1.00 23.30 ? 239  GLN A CA  1 
ATOM   3214 C C   . GLN C 3 239 ? 242.786 171.730 235.671 1.00 23.24 ? 239  GLN A C   1 
ATOM   3215 O O   . GLN C 3 239 ? 241.627 171.629 236.068 1.00 22.96 ? 239  GLN A O   1 
ATOM   3216 C CB  . GLN C 3 239 ? 244.369 172.581 237.413 1.00 23.99 ? 239  GLN A CB  1 
ATOM   3217 C CG  . GLN C 3 239 ? 245.357 171.439 237.326 1.00 24.57 ? 239  GLN A CG  1 
ATOM   3218 C CD  . GLN C 3 239 ? 246.168 171.305 238.586 1.00 23.87 ? 239  GLN A CD  1 
ATOM   3219 O OE1 . GLN C 3 239 ? 245.703 171.651 239.676 1.00 24.30 ? 239  GLN A OE1 1 
ATOM   3220 N NE2 . GLN C 3 239 ? 247.389 170.808 238.454 1.00 24.20 ? 239  GLN A NE2 1 
ATOM   3221 N N   . THR C 3 240 ? 243.344 170.848 234.848 1.00 22.64 ? 240  THR A N   1 
ATOM   3222 C CA  . THR C 3 240 ? 242.613 169.678 234.370 1.00 21.99 ? 240  THR A CA  1 
ATOM   3223 C C   . THR C 3 240 ? 242.814 168.475 235.290 1.00 23.80 ? 240  THR A C   1 
ATOM   3224 O O   . THR C 3 240 ? 243.943 168.141 235.649 1.00 24.55 ? 240  THR A O   1 
ATOM   3225 C CB  . THR C 3 240 ? 243.056 169.320 232.939 1.00 22.86 ? 240  THR A CB  1 
ATOM   3226 O OG1 . THR C 3 240 ? 242.805 170.434 232.076 1.00 24.83 ? 240  THR A OG1 1 
ATOM   3227 C CG2 . THR C 3 240 ? 242.288 168.112 232.423 1.00 23.80 ? 240  THR A CG2 1 
ATOM   3228 N N   . LEU C 3 241 ? 241.713 167.822 235.661 1.00 23.71 ? 241  LEU A N   1 
ATOM   3229 C CA  . LEU C 3 241 ? 241.759 166.628 236.502 1.00 23.57 ? 241  LEU A CA  1 
ATOM   3230 C C   . LEU C 3 241 ? 241.670 165.343 235.692 1.00 24.35 ? 241  LEU A C   1 
ATOM   3231 O O   . LEU C 3 241 ? 240.717 165.131 234.936 1.00 23.88 ? 241  LEU A O   1 
ATOM   3232 C CB  . LEU C 3 241 ? 240.619 166.641 237.528 1.00 22.15 ? 241  LEU A CB  1 
ATOM   3233 C CG  . LEU C 3 241 ? 240.717 167.677 238.638 1.00 23.07 ? 241  LEU A CG  1 
ATOM   3234 C CD1 . LEU C 3 241 ? 239.412 167.698 239.409 1.00 23.02 ? 241  LEU A CD1 1 
ATOM   3235 C CD2 . LEU C 3 241 ? 241.871 167.314 239.565 1.00 26.58 ? 241  LEU A CD2 1 
ATOM   3236 N N   . LEU C 3 242 ? 242.660 164.480 235.883 1.00 25.10 ? 242  LEU A N   1 
ATOM   3237 C CA  . LEU C 3 242 ? 242.739 163.201 235.192 1.00 24.87 ? 242  LEU A CA  1 
ATOM   3238 C C   . LEU C 3 242 ? 242.422 162.051 236.140 1.00 26.42 ? 242  LEU A C   1 
ATOM   3239 O O   . LEU C 3 242 ? 242.672 162.146 237.342 1.00 26.83 ? 242  LEU A O   1 
ATOM   3240 C CB  . LEU C 3 242 ? 244.152 163.003 234.631 1.00 25.58 ? 242  LEU A CB  1 
ATOM   3241 C CG  . LEU C 3 242 ? 244.708 164.146 233.763 1.00 24.37 ? 242  LEU A CG  1 
ATOM   3242 C CD1 . LEU C 3 242 ? 246.146 163.824 233.378 1.00 26.15 ? 242  LEU A CD1 1 
ATOM   3243 C CD2 . LEU C 3 242 ? 243.844 164.322 232.529 1.00 24.72 ? 242  LEU A CD2 1 
ATOM   3244 N N   . ALA C 3 243 ? 241.928 160.949 235.590 1.00 26.32 ? 243  ALA A N   1 
ATOM   3245 C CA  . ALA C 3 243 ? 241.784 159.715 236.349 1.00 27.23 ? 243  ALA A CA  1 
ATOM   3246 C C   . ALA C 3 243 ? 242.989 158.824 236.100 1.00 28.57 ? 243  ALA A C   1 
ATOM   3247 O O   . ALA C 3 243 ? 243.181 158.320 234.993 1.00 28.65 ? 243  ALA A O   1 
ATOM   3248 C CB  . ALA C 3 243 ? 240.503 158.997 235.970 1.00 26.98 ? 243  ALA A CB  1 
ATOM   3249 N N   . LEU C 3 244 ? 243.821 158.668 237.119 1.00 29.05 ? 244  LEU A N   1 
ATOM   3250 C CA  . LEU C 3 244 ? 245.066 157.922 236.996 1.00 29.36 ? 244  LEU A CA  1 
ATOM   3251 C C   . LEU C 3 244 ? 244.944 156.576 237.684 1.00 29.81 ? 244  LEU A C   1 
ATOM   3252 O O   . LEU C 3 244 ? 244.097 156.399 238.561 1.00 29.58 ? 244  LEU A O   1 
ATOM   3253 C CB  . LEU C 3 244 ? 246.228 158.705 237.614 1.00 29.68 ? 244  LEU A CB  1 
ATOM   3254 C CG  . LEU C 3 244 ? 246.433 160.140 237.111 1.00 29.15 ? 244  LEU A CG  1 
ATOM   3255 C CD1 . LEU C 3 244 ? 247.592 160.761 237.866 1.00 30.27 ? 244  LEU A CD1 1 
ATOM   3256 C CD2 . LEU C 3 244 ? 246.706 160.135 235.621 1.00 28.52 ? 244  LEU A CD2 1 
ATOM   3257 N N   . HIS C 3 245 ? 245.801 155.636 237.309 1.00 30.74 ? 245  HIS A N   1 
ATOM   3258 C CA  . HIS C 3 245 ? 245.781 154.322 237.939 1.00 30.73 ? 245  HIS A CA  1 
ATOM   3259 C C   . HIS C 3 245 ? 247.187 153.818 238.255 1.00 30.77 ? 245  HIS A C   1 
ATOM   3260 O O   . HIS C 3 245 ? 248.140 154.121 237.537 1.00 31.38 ? 245  HIS A O   1 
ATOM   3261 C CB  . HIS C 3 245 ? 245.061 153.312 237.038 1.00 30.47 ? 245  HIS A CB  1 
ATOM   3262 C CG  . HIS C 3 245 ? 245.753 153.042 235.732 1.00 30.60 ? 245  HIS A CG  1 
ATOM   3263 N ND1 . HIS C 3 245 ? 245.616 153.863 234.629 1.00 30.44 ? 245  HIS A ND1 1 
ATOM   3264 C CD2 . HIS C 3 245 ? 246.573 152.036 235.352 1.00 30.32 ? 245  HIS A CD2 1 
ATOM   3265 C CE1 . HIS C 3 245 ? 246.325 153.372 233.629 1.00 30.45 ? 245  HIS A CE1 1 
ATOM   3266 N NE2 . HIS C 3 245 ? 246.914 152.264 234.041 1.00 30.18 ? 245  HIS A NE2 1 
ATOM   3267 N N   . ARG C 3 246 ? 247.306 153.036 239.332 1.00 31.80 ? 246  ARG A N   1 
ATOM   3268 C CA  . ARG C 3 246 ? 248.579 152.477 239.782 1.00 32.09 ? 246  ARG A CA  1 
ATOM   3269 C C   . ARG C 3 246 ? 248.746 151.047 239.272 1.00 31.96 ? 246  ARG A C   1 
ATOM   3270 O O   . ARG C 3 246 ? 247.799 150.259 239.274 1.00 31.09 ? 246  ARG A O   1 
ATOM   3271 C CB  . ARG C 3 246 ? 248.658 152.516 241.314 1.00 33.11 ? 246  ARG A CB  1 
ATOM   3272 C CG  . ARG C 3 246 ? 250.001 152.058 241.947 1.00 34.30 ? 246  ARG A CG  1 
ATOM   3273 C CD  . ARG C 3 246 ? 250.014 152.245 243.448 1.00 33.59 ? 246  ARG A CD  1 
ATOM   3274 N NE  . ARG C 3 246 ? 251.305 151.855 244.050 1.00 35.15 ? 246  ARG A NE  1 
ATOM   3275 C CZ  . ARG C 3 246 ? 251.597 151.843 245.387 1.00 35.29 ? 246  ARG A CZ  1 
ATOM   3276 N NH1 . ARG C 3 246 ? 250.698 152.192 246.288 1.00 35.60 ? 246  ARG A NH1 1 
ATOM   3277 N NH2 . ARG C 3 246 ? 252.800 151.476 245.788 1.00 36.09 ? 246  ARG A NH2 1 
ATOM   3278 N N   . GLY C 3 257 ? 254.509 155.744 239.981 1.00 33.92 ? 257  GLY A N   1 
ATOM   3279 C CA  . GLY C 3 257 ? 253.504 154.900 240.611 1.00 33.36 ? 257  GLY A CA  1 
ATOM   3280 C C   . GLY C 3 257 ? 252.198 154.892 239.817 1.00 33.84 ? 257  GLY A C   1 
ATOM   3281 O O   . GLY C 3 257 ? 251.706 153.829 239.438 1.00 34.00 ? 257  GLY A O   1 
ATOM   3282 N N   . TRP C 3 258 ? 251.640 156.084 239.586 1.00 32.93 ? 258  TRP A N   1 
ATOM   3283 C CA  . TRP C 3 258 ? 250.375 156.264 238.874 1.00 32.30 ? 258  TRP A CA  1 
ATOM   3284 C C   . TRP C 3 258 ? 250.626 156.686 237.431 1.00 31.89 ? 258  TRP A C   1 
ATOM   3285 O O   . TRP C 3 258 ? 251.533 157.470 237.151 1.00 32.28 ? 258  TRP A O   1 
ATOM   3286 C CB  . TRP C 3 258 ? 249.513 157.310 239.586 1.00 31.70 ? 258  TRP A CB  1 
ATOM   3287 C CG  . TRP C 3 258 ? 248.911 156.833 240.888 1.00 32.10 ? 258  TRP A CG  1 
ATOM   3288 C CD1 . TRP C 3 258 ? 247.614 156.467 241.097 1.00 31.26 ? 258  TRP A CD1 1 
ATOM   3289 C CD2 . TRP C 3 258 ? 249.578 156.669 242.166 1.00 32.43 ? 258  TRP A CD2 1 
ATOM   3290 N NE1 . TRP C 3 258 ? 247.432 156.100 242.410 1.00 31.43 ? 258  TRP A NE1 1 
ATOM   3291 C CE2 . TRP C 3 258 ? 248.618 156.215 243.073 1.00 31.99 ? 258  TRP A CE2 1 
ATOM   3292 C CE3 . TRP C 3 258 ? 250.890 156.870 242.607 1.00 33.41 ? 258  TRP A CE3 1 
ATOM   3293 C CZ2 . TRP C 3 258 ? 248.925 155.958 244.397 1.00 32.61 ? 258  TRP A CZ2 1 
ATOM   3294 C CZ3 . TRP C 3 258 ? 251.196 156.606 243.934 1.00 33.39 ? 258  TRP A CZ3 1 
ATOM   3295 C CH2 . TRP C 3 258 ? 250.239 156.163 244.805 1.00 32.64 ? 258  TRP A CH2 1 
ATOM   3296 N N   . THR C 3 259 ? 249.819 156.161 236.518 1.00 31.42 ? 259  THR A N   1 
ATOM   3297 C CA  . THR C 3 259 ? 249.956 156.469 235.101 1.00 30.86 ? 259  THR A CA  1 
ATOM   3298 C C   . THR C 3 259 ? 248.604 156.690 234.433 1.00 30.39 ? 259  THR A C   1 
ATOM   3299 O O   . THR C 3 259 ? 247.571 156.764 235.099 1.00 31.40 ? 259  THR A O   1 
ATOM   3300 C CB  . THR C 3 259 ? 250.728 155.356 234.373 1.00 31.52 ? 259  THR A CB  1 
ATOM   3301 O OG1 . THR C 3 259 ? 251.054 155.792 233.049 1.00 31.59 ? 259  THR A OG1 1 
ATOM   3302 C CG2 . THR C 3 259 ? 249.898 154.085 234.302 1.00 31.42 ? 259  THR A CG2 1 
ATOM   3303 N N   . ALA C 3 260 ? 248.619 156.820 233.110 1.00 30.47 ? 260  ALA A N   1 
ATOM   3304 C CA  . ALA C 3 260 ? 247.411 157.106 232.343 1.00 30.51 ? 260  ALA A CA  1 
ATOM   3305 C C   . ALA C 3 260 ? 247.473 156.449 230.972 1.00 30.11 ? 260  ALA A C   1 
ATOM   3306 O O   . ALA C 3 260 ? 248.550 156.106 230.484 1.00 30.00 ? 260  ALA A O   1 
ATOM   3307 C CB  . ALA C 3 260 ? 247.226 158.609 232.186 1.00 29.39 ? 260  ALA A CB  1 
ATOM   3308 N N   . GLY C 3 261 ? 246.314 156.293 230.343 1.00 29.30 ? 261  GLY A N   1 
ATOM   3309 C CA  . GLY C 3 261 ? 246.250 155.765 228.987 1.00 29.10 ? 261  GLY A CA  1 
ATOM   3310 C C   . GLY C 3 261 ? 246.475 156.882 227.977 1.00 29.27 ? 261  GLY A C   1 
ATOM   3311 O O   . GLY C 3 261 ? 246.882 157.983 228.345 1.00 28.80 ? 261  GLY A O   1 
ATOM   3312 N N   . ALA C 3 262 ? 246.226 156.595 226.704 1.00 28.50 ? 262  ALA A N   1 
ATOM   3313 C CA  . ALA C 3 262 ? 246.477 157.572 225.650 1.00 28.19 ? 262  ALA A CA  1 
ATOM   3314 C C   . ALA C 3 262 ? 245.317 158.547 225.497 1.00 28.07 ? 262  ALA A C   1 
ATOM   3315 O O   . ALA C 3 262 ? 244.187 158.147 225.215 1.00 28.25 ? 262  ALA A O   1 
ATOM   3316 C CB  . ALA C 3 262 ? 246.733 156.862 224.330 1.00 28.59 ? 262  ALA A CB  1 
ATOM   3317 N N   . ALA C 3 263 ? 245.612 159.831 225.672 1.00 27.78 ? 263  ALA A N   1 
ATOM   3318 C CA  . ALA C 3 263 ? 244.629 160.902 225.532 1.00 28.08 ? 263  ALA A CA  1 
ATOM   3319 C C   . ALA C 3 263 ? 245.340 162.234 225.364 1.00 28.54 ? 263  ALA A C   1 
ATOM   3320 O O   . ALA C 3 263 ? 246.516 162.360 225.708 1.00 29.14 ? 263  ALA A O   1 
ATOM   3321 C CB  . ALA C 3 263 ? 243.702 160.944 226.736 1.00 27.52 ? 263  ALA A CB  1 
ATOM   3322 N N   . ALA C 3 264 ? 244.627 163.233 224.855 1.00 28.17 ? 264  ALA A N   1 
ATOM   3323 C CA  . ALA C 3 264 ? 245.186 164.575 224.733 1.00 28.30 ? 264  ALA A CA  1 
ATOM   3324 C C   . ALA C 3 264 ? 244.100 165.632 224.835 1.00 28.24 ? 264  ALA A C   1 
ATOM   3325 O O   . ALA C 3 264 ? 242.926 165.354 224.591 1.00 28.28 ? 264  ALA A O   1 
ATOM   3326 C CB  . ALA C 3 264 ? 245.928 164.721 223.416 1.00 29.79 ? 264  ALA A CB  1 
ATOM   3327 N N   . TYR C 3 265 ? 244.497 166.850 225.184 1.00 28.05 ? 265  TYR A N   1 
ATOM   3328 C CA  . TYR C 3 265 ? 243.549 167.952 225.259 1.00 27.91 ? 265  TYR A CA  1 
ATOM   3329 C C   . TYR C 3 265 ? 244.159 169.260 224.786 1.00 27.38 ? 265  TYR A C   1 
ATOM   3330 O O   . TYR C 3 265 ? 245.379 169.418 224.743 1.00 34.66 ? 265  TYR A O   1 
ATOM   3331 C CB  . TYR C 3 265 ? 242.986 168.085 226.672 1.00 27.03 ? 265  TYR A CB  1 
ATOM   3332 C CG  . TYR C 3 265 ? 243.988 168.457 227.722 1.00 26.54 ? 265  TYR A CG  1 
ATOM   3333 C CD1 . TYR C 3 265 ? 244.159 169.783 228.065 1.00 27.24 ? 265  TYR A CD1 1 
ATOM   3334 C CD2 . TYR C 3 265 ? 244.728 167.474 228.355 1.00 26.28 ? 265  TYR A CD2 1 
ATOM   3335 C CE1 . TYR C 3 265 ? 245.064 170.131 229.040 1.00 26.99 ? 265  TYR A CE1 1 
ATOM   3336 C CE2 . TYR C 3 265 ? 245.636 167.819 229.331 1.00 26.61 ? 265  TYR A CE2 1 
ATOM   3337 C CZ  . TYR C 3 265 ? 245.802 169.145 229.675 1.00 26.62 ? 265  TYR A CZ  1 
ATOM   3338 O OH  . TYR C 3 265 ? 246.706 169.498 230.646 1.00 27.27 ? 265  TYR A OH  1 
ATOM   3339 N N   . TYR C 3 266 ? 243.293 170.184 224.396 1.00 28.79 ? 266  TYR A N   1 
ATOM   3340 C CA  . TYR C 3 266 ? 243.706 171.432 223.786 1.00 29.15 ? 266  TYR A CA  1 
ATOM   3341 C C   . TYR C 3 266 ? 243.102 172.620 224.522 1.00 29.31 ? 266  TYR A C   1 
ATOM   3342 O O   . TYR C 3 266 ? 241.941 172.579 224.931 1.00 28.83 ? 266  TYR A O   1 
ATOM   3343 C CB  . TYR C 3 266 ? 243.261 171.432 222.324 1.00 29.87 ? 266  TYR A CB  1 
ATOM   3344 C CG  . TYR C 3 266 ? 243.709 170.210 221.573 1.00 30.94 ? 266  TYR A CG  1 
ATOM   3345 C CD1 . TYR C 3 266 ? 242.983 169.040 221.681 1.00 30.57 ? 266  TYR A CD1 1 
ATOM   3346 C CD2 . TYR C 3 266 ? 244.839 170.250 220.782 1.00 32.16 ? 266  TYR A CD2 1 
ATOM   3347 C CE1 . TYR C 3 266 ? 243.387 167.913 221.013 1.00 31.28 ? 266  TYR A CE1 1 
ATOM   3348 C CE2 . TYR C 3 266 ? 245.243 169.116 220.104 1.00 32.34 ? 266  TYR A CE2 1 
ATOM   3349 C CZ  . TYR C 3 266 ? 244.521 167.950 220.224 1.00 32.42 ? 266  TYR A CZ  1 
ATOM   3350 O OH  . TYR C 3 266 ? 244.922 166.815 219.562 1.00 33.54 ? 266  TYR A OH  1 
ATOM   3351 N N   . VAL C 3 267 ? 243.883 173.682 224.688 1.00 29.92 ? 267  VAL A N   1 
ATOM   3352 C CA  . VAL C 3 267 ? 243.386 174.877 225.358 1.00 29.15 ? 267  VAL A CA  1 
ATOM   3353 C C   . VAL C 3 267 ? 243.617 176.147 224.550 1.00 31.06 ? 267  VAL A C   1 
ATOM   3354 O O   . VAL C 3 267 ? 244.746 176.467 224.173 1.00 32.12 ? 267  VAL A O   1 
ATOM   3355 C CB  . VAL C 3 267 ? 244.039 175.020 226.742 1.00 28.97 ? 267  VAL A CB  1 
ATOM   3356 C CG1 . VAL C 3 267 ? 243.552 176.294 227.426 1.00 28.97 ? 267  VAL A CG1 1 
ATOM   3357 C CG2 . VAL C 3 267 ? 243.693 173.799 227.581 1.00 28.72 ? 267  VAL A CG2 1 
ATOM   3358 N N   . GLY C 3 268 ? 242.538 176.881 224.309 1.00 30.96 ? 268  GLY A N   1 
ATOM   3359 C CA  . GLY C 3 268 ? 242.603 178.148 223.593 1.00 31.40 ? 268  GLY A CA  1 
ATOM   3360 C C   . GLY C 3 268 ? 241.955 179.239 224.429 1.00 30.56 ? 268  GLY A C   1 
ATOM   3361 O O   . GLY C 3 268 ? 241.440 178.971 225.514 1.00 30.22 ? 268  GLY A O   1 
ATOM   3362 N N   . TYR C 3 269 ? 241.962 180.469 223.932 1.00 31.48 ? 269  TYR A N   1 
ATOM   3363 C CA  . TYR C 3 269 ? 241.361 181.560 224.685 1.00 32.27 ? 269  TYR A CA  1 
ATOM   3364 C C   . TYR C 3 269 ? 240.438 182.411 223.836 1.00 35.58 ? 269  TYR A C   1 
ATOM   3365 O O   . TYR C 3 269 ? 240.673 182.604 222.643 1.00 38.09 ? 269  TYR A O   1 
ATOM   3366 C CB  . TYR C 3 269 ? 242.447 182.400 225.343 1.00 31.54 ? 269  TYR A CB  1 
ATOM   3367 C CG  . TYR C 3 269 ? 243.220 181.603 226.348 1.00 29.75 ? 269  TYR A CG  1 
ATOM   3368 C CD1 . TYR C 3 269 ? 244.396 180.968 225.984 1.00 29.76 ? 269  TYR A CD1 1 
ATOM   3369 C CD2 . TYR C 3 269 ? 242.729 181.473 227.627 1.00 28.60 ? 269  TYR A CD2 1 
ATOM   3370 C CE1 . TYR C 3 269 ? 245.077 180.207 226.909 1.00 28.34 ? 269  TYR A CE1 1 
ATOM   3371 C CE2 . TYR C 3 269 ? 243.404 180.719 228.544 1.00 27.61 ? 269  TYR A CE2 1 
ATOM   3372 C CZ  . TYR C 3 269 ? 244.574 180.083 228.194 1.00 26.89 ? 269  TYR A CZ  1 
ATOM   3373 O OH  . TYR C 3 269 ? 245.246 179.321 229.118 1.00 26.82 ? 269  TYR A OH  1 
ATOM   3374 N N   . LEU C 3 270 ? 239.392 182.922 224.470 1.00 36.08 ? 270  LEU A N   1 
ATOM   3375 C CA  . LEU C 3 270 ? 238.380 183.702 223.776 1.00 40.10 ? 270  LEU A CA  1 
ATOM   3376 C C   . LEU C 3 270 ? 238.793 185.161 223.655 1.00 41.52 ? 270  LEU A C   1 
ATOM   3377 O O   . LEU C 3 270 ? 239.477 185.697 224.527 1.00 40.62 ? 270  LEU A O   1 
ATOM   3378 C CB  . LEU C 3 270 ? 237.054 183.633 224.537 1.00 39.49 ? 270  LEU A CB  1 
ATOM   3379 C CG  . LEU C 3 270 ? 236.517 182.233 224.874 1.00 36.29 ? 270  LEU A CG  1 
ATOM   3380 C CD1 . LEU C 3 270 ? 235.227 182.390 225.664 1.00 35.85 ? 270  LEU A CD1 1 
ATOM   3381 C CD2 . LEU C 3 270 ? 236.282 181.437 223.603 1.00 37.48 ? 270  LEU A CD2 1 
ATOM   3382 N N   . GLN C 3 271 ? 238.348 185.806 222.583 1.00 43.28 ? 271  GLN A N   1 
ATOM   3383 C CA  . GLN C 3 271 ? 238.584 187.228 222.382 1.00 45.34 ? 271  GLN A CA  1 
ATOM   3384 C C   . GLN C 3 271 ? 237.290 187.923 221.962 1.00 46.16 ? 271  GLN A C   1 
ATOM   3385 O O   . GLN C 3 271 ? 236.437 187.303 221.327 1.00 46.28 ? 271  GLN A O   1 
ATOM   3386 C CB  . GLN C 3 271 ? 239.667 187.436 221.319 1.00 46.13 ? 271  GLN A CB  1 
ATOM   3387 C CG  . GLN C 3 271 ? 241.030 186.903 221.713 1.00 44.88 ? 271  GLN A CG  1 
ATOM   3388 C CD  . GLN C 3 271 ? 242.091 187.214 220.682 1.00 46.59 ? 271  GLN A CD  1 
ATOM   3389 O OE1 . GLN C 3 271 ? 241.782 187.646 219.567 1.00 47.16 ? 271  GLN A OE1 1 
ATOM   3390 N NE2 . GLN C 3 271 ? 243.350 186.997 221.046 1.00 46.60 ? 271  GLN A NE2 1 
ATOM   3391 N N   . PRO C 3 272 ? 237.131 189.206 222.295 1.00 46.92 ? 272  PRO A N   1 
ATOM   3392 C CA  . PRO C 3 272 ? 236.028 190.067 221.912 1.00 48.14 ? 272  PRO A CA  1 
ATOM   3393 C C   . PRO C 3 272 ? 236.101 190.402 220.432 1.00 49.47 ? 272  PRO A C   1 
ATOM   3394 O O   . PRO C 3 272 ? 236.845 191.293 220.023 1.00 50.39 ? 272  PRO A O   1 
ATOM   3395 C CB  . PRO C 3 272 ? 236.242 191.296 222.802 1.00 48.01 ? 272  PRO A CB  1 
ATOM   3396 C CG  . PRO C 3 272 ? 237.732 191.314 223.082 1.00 47.83 ? 272  PRO A CG  1 
ATOM   3397 C CD  . PRO C 3 272 ? 238.142 189.853 223.139 1.00 46.69 ? 272  PRO A CD  1 
ATOM   3398 N N   . ARG C 3 273 ? 235.368 189.640 219.630 1.00 50.12 ? 273  ARG A N   1 
ATOM   3399 C CA  . ARG C 3 273 ? 235.412 189.774 218.182 1.00 51.61 ? 273  ARG A CA  1 
ATOM   3400 C C   . ARG C 3 273 ? 234.018 189.735 217.573 1.00 53.01 ? 273  ARG A C   1 
ATOM   3401 O O   . ARG C 3 273 ? 233.064 189.262 218.197 1.00 52.64 ? 273  ARG A O   1 
ATOM   3402 C CB  . ARG C 3 273 ? 236.275 188.686 217.562 1.00 51.64 ? 273  ARG A CB  1 
ATOM   3403 C CG  . ARG C 3 273 ? 237.765 188.843 217.799 1.00 50.60 ? 273  ARG A CG  1 
ATOM   3404 C CD  . ARG C 3 273 ? 238.562 187.892 216.976 1.00 51.07 ? 273  ARG A CD  1 
ATOM   3405 N NE  . ARG C 3 273 ? 239.985 188.178 217.067 1.00 50.53 ? 273  ARG A NE  1 
ATOM   3406 C CZ  . ARG C 3 273 ? 240.928 187.737 216.206 1.00 51.85 ? 273  ARG A CZ  1 
ATOM   3407 N NH1 . ARG C 3 273 ? 240.609 186.971 215.177 1.00 52.15 ? 273  ARG A NH1 1 
ATOM   3408 N NH2 . ARG C 3 273 ? 242.190 188.080 216.398 1.00 50.40 ? 273  ARG A NH2 1 
ATOM   3409 N N   . THR C 3 274 ? 233.906 190.246 216.354 1.00 53.97 ? 274  THR A N   1 
ATOM   3410 C CA  . THR C 3 274 ? 232.633 190.264 215.647 1.00 55.15 ? 274  THR A CA  1 
ATOM   3411 C C   . THR C 3 274 ? 232.528 189.072 214.709 1.00 54.40 ? 274  THR A C   1 
ATOM   3412 O O   . THR C 3 274 ? 233.475 188.757 213.986 1.00 55.78 ? 274  THR A O   1 
ATOM   3413 C CB  . THR C 3 274 ? 232.463 191.569 214.846 1.00 56.14 ? 274  THR A CB  1 
ATOM   3414 N N   . PHE C 3 275 ? 231.388 188.392 214.760 1.00 55.72 ? 275  PHE A N   1 
ATOM   3415 C CA  . PHE C 3 275 ? 231.126 187.252 213.892 1.00 55.50 ? 275  PHE A CA  1 
ATOM   3416 C C   . PHE C 3 275 ? 229.808 187.367 213.147 1.00 56.78 ? 275  PHE A C   1 
ATOM   3417 O O   . PHE C 3 275 ? 228.807 187.834 213.692 1.00 57.19 ? 275  PHE A O   1 
ATOM   3418 C CB  . PHE C 3 275 ? 231.132 185.946 214.691 1.00 54.99 ? 275  PHE A CB  1 
ATOM   3419 C CG  . PHE C 3 275 ? 232.496 185.467 215.057 1.00 54.03 ? 275  PHE A CG  1 
ATOM   3420 C CD1 . PHE C 3 275 ? 233.211 186.043 216.089 1.00 52.71 ? 275  PHE A CD1 1 
ATOM   3421 C CD2 . PHE C 3 275 ? 233.069 184.418 214.358 1.00 53.74 ? 275  PHE A CD2 1 
ATOM   3422 C CE1 . PHE C 3 275 ? 234.472 185.586 216.405 1.00 52.01 ? 275  PHE A CE1 1 
ATOM   3423 C CE2 . PHE C 3 275 ? 234.322 183.962 214.678 1.00 52.21 ? 275  PHE A CE2 1 
ATOM   3424 C CZ  . PHE C 3 275 ? 235.027 184.546 215.702 1.00 51.53 ? 275  PHE A CZ  1 
ATOM   3425 N N   . LEU C 3 276 ? 229.797 186.863 211.919 1.00 56.97 ? 276  LEU A N   1 
ATOM   3426 C CA  . LEU C 3 276 ? 228.556 186.714 211.172 1.00 58.66 ? 276  LEU A CA  1 
ATOM   3427 C C   . LEU C 3 276 ? 228.141 185.247 211.201 1.00 57.42 ? 276  LEU A C   1 
ATOM   3428 O O   . LEU C 3 276 ? 228.862 184.382 210.704 1.00 57.58 ? 276  LEU A O   1 
ATOM   3429 C CB  . LEU C 3 276 ? 228.731 187.196 209.722 1.00 59.17 ? 276  LEU A CB  1 
ATOM   3430 N N   . LEU C 3 277 ? 227.008 184.963 211.834 1.00 58.59 ? 277  LEU A N   1 
ATOM   3431 C CA  . LEU C 3 277 ? 226.564 183.586 212.021 1.00 58.30 ? 277  LEU A CA  1 
ATOM   3432 C C   . LEU C 3 277 ? 225.453 183.217 211.049 1.00 58.54 ? 277  LEU A C   1 
ATOM   3433 O O   . LEU C 3 277 ? 224.470 183.945 210.904 1.00 59.34 ? 277  LEU A O   1 
ATOM   3434 C CB  . LEU C 3 277 ? 226.072 183.386 213.461 1.00 57.40 ? 277  LEU A CB  1 
ATOM   3435 C CG  . LEU C 3 277 ? 227.068 183.764 214.582 1.00 57.25 ? 277  LEU A CG  1 
ATOM   3436 C CD1 . LEU C 3 277 ? 226.398 183.552 215.931 1.00 55.46 ? 277  LEU A CD1 1 
ATOM   3437 C CD2 . LEU C 3 277 ? 228.330 182.917 214.464 1.00 56.19 ? 277  LEU A CD2 1 
ATOM   3438 N N   . LYS C 3 278 ? 225.610 182.075 210.388 1.00 58.01 ? 278  LYS A N   1 
ATOM   3439 C CA  . LYS C 3 278 ? 224.622 181.606 209.427 1.00 58.87 ? 278  LYS A CA  1 
ATOM   3440 C C   . LYS C 3 278 ? 223.717 180.531 210.009 1.00 57.33 ? 278  LYS A C   1 
ATOM   3441 O O   . LYS C 3 278 ? 224.157 179.408 210.271 1.00 58.15 ? 278  LYS A O   1 
ATOM   3442 C CB  . LYS C 3 278 ? 225.314 181.073 208.172 1.00 58.83 ? 278  LYS A CB  1 
ATOM   3443 C CG  . LYS C 3 278 ? 224.367 180.572 207.088 1.00 59.27 ? 278  LYS A CG  1 
ATOM   3444 C CD  . LYS C 3 278 ? 225.132 180.145 205.845 1.00 59.27 ? 278  LYS A CD  1 
ATOM   3445 C CE  . LYS C 3 278 ? 224.193 179.648 204.758 1.00 59.02 ? 278  LYS A CE  1 
ATOM   3446 N NZ  . LYS C 3 278 ? 224.934 179.230 203.535 1.00 61.39 ? 278  LYS A NZ  1 
ATOM   3447 N N   . TYR C 3 279 ? 222.439 180.878 210.169 1.00 59.06 ? 279  TYR A N   1 
ATOM   3448 C CA  . TYR C 3 279 ? 221.428 179.959 210.684 1.00 60.18 ? 279  TYR A CA  1 
ATOM   3449 C C   . TYR C 3 279 ? 220.647 179.337 209.534 1.00 59.92 ? 279  TYR A C   1 
ATOM   3450 O O   . TYR C 3 279 ? 220.125 180.050 208.674 1.00 60.83 ? 279  TYR A O   1 
ATOM   3451 C CB  . TYR C 3 279 ? 220.456 180.693 211.609 1.00 62.26 ? 279  TYR A CB  1 
ATOM   3452 C CG  . TYR C 3 279 ? 221.054 181.180 212.904 1.00 59.40 ? 279  TYR A CG  1 
ATOM   3453 C CD1 . TYR C 3 279 ? 221.754 182.376 212.942 1.00 58.69 ? 279  TYR A CD1 1 
ATOM   3454 C CD2 . TYR C 3 279 ? 220.881 180.442 214.061 1.00 57.90 ? 279  TYR A CD2 1 
ATOM   3455 C CE1 . TYR C 3 279 ? 222.282 182.826 214.134 1.00 58.31 ? 279  TYR A CE1 1 
ATOM   3456 C CE2 . TYR C 3 279 ? 221.407 180.894 215.252 1.00 57.82 ? 279  TYR A CE2 1 
ATOM   3457 C CZ  . TYR C 3 279 ? 222.106 182.082 215.291 1.00 57.72 ? 279  TYR A CZ  1 
ATOM   3458 O OH  . TYR C 3 279 ? 222.632 182.534 216.479 1.00 56.86 ? 279  TYR A OH  1 
ATOM   3459 N N   . ASN C 3 280 ? 220.530 178.013 209.537 1.00 59.34 ? 280  ASN A N   1 
ATOM   3460 C CA  . ASN C 3 280 ? 219.793 177.314 208.490 1.00 60.54 ? 280  ASN A CA  1 
ATOM   3461 C C   . ASN C 3 280 ? 218.300 177.305 208.792 1.00 57.62 ? 280  ASN A C   1 
ATOM   3462 O O   . ASN C 3 280 ? 217.840 177.977 209.716 1.00 64.69 ? 280  ASN A O   1 
ATOM   3463 C CB  . ASN C 3 280 ? 220.319 175.902 208.293 1.00 60.28 ? 280  ASN A CB  1 
ATOM   3464 N N   . GLU C 3 281 ? 217.539 176.568 207.992 1.00 63.97 ? 281  GLU A N   1 
ATOM   3465 C CA  . GLU C 3 281 ? 216.083 176.539 208.121 1.00 61.56 ? 281  GLU A CA  1 
ATOM   3466 C C   . GLU C 3 281 ? 215.601 176.048 209.493 1.00 61.12 ? 281  GLU A C   1 
ATOM   3467 O O   . GLU C 3 281 ? 214.572 176.509 209.988 1.00 61.69 ? 281  GLU A O   1 
ATOM   3468 C CB  . GLU C 3 281 ? 215.480 175.661 207.020 1.00 62.57 ? 281  GLU A CB  1 
ATOM   3469 N N   . ASN C 3 282 ? 216.352 175.123 210.106 1.00 61.79 ? 282  ASN A N   1 
ATOM   3470 C CA  . ASN C 3 282 ? 215.997 174.537 211.403 1.00 61.65 ? 282  ASN A CA  1 
ATOM   3471 C C   . ASN C 3 282 ? 216.544 175.354 212.580 1.00 60.55 ? 282  ASN A C   1 
ATOM   3472 O O   . ASN C 3 282 ? 216.389 174.956 213.738 1.00 61.13 ? 282  ASN A O   1 
ATOM   3473 C CB  . ASN C 3 282 ? 216.487 173.095 211.485 1.00 62.08 ? 282  ASN A CB  1 
ATOM   3474 C CG  . ASN C 3 282 ? 215.819 172.172 210.471 1.00 63.48 ? 282  ASN A CG  1 
ATOM   3475 O OD1 . ASN C 3 282 ? 214.584 172.093 210.410 1.00 63.94 ? 282  ASN A OD1 1 
ATOM   3476 N ND2 . ASN C 3 282 ? 216.619 171.476 209.689 1.00 63.47 ? 282  ASN A ND2 1 
ATOM   3477 N N   . GLY C 3 283 ? 217.187 176.496 212.296 1.00 61.93 ? 283  GLY A N   1 
ATOM   3478 C CA  . GLY C 3 283 ? 217.730 177.390 213.318 1.00 61.60 ? 283  GLY A CA  1 
ATOM   3479 C C   . GLY C 3 283 ? 219.076 176.936 213.869 1.00 57.98 ? 283  GLY A C   1 
ATOM   3480 O O   . GLY C 3 283 ? 219.490 177.362 214.947 1.00 57.71 ? 283  GLY A O   1 
ATOM   3481 N N   . THR C 3 284 ? 219.760 176.077 213.129 1.00 60.44 ? 284  THR A N   1 
ATOM   3482 C CA  . THR C 3 284 ? 221.067 175.586 213.536 1.00 57.01 ? 284  THR A CA  1 
ATOM   3483 C C   . THR C 3 284 ? 222.159 176.383 212.843 1.00 59.76 ? 284  THR A C   1 
ATOM   3484 O O   . THR C 3 284 ? 222.068 176.662 211.647 1.00 56.11 ? 284  THR A O   1 
ATOM   3485 C CB  . THR C 3 284 ? 221.217 174.086 213.215 1.00 57.77 ? 284  THR A CB  1 
ATOM   3486 O OG1 . THR C 3 284 ? 220.252 173.342 213.969 1.00 58.83 ? 284  THR A OG1 1 
ATOM   3487 C CG2 . THR C 3 284 ? 222.615 173.592 213.557 1.00 56.81 ? 284  THR A CG2 1 
ATOM   3488 N N   . ILE C 3 285 ? 223.194 176.759 213.586 1.00 54.67 ? 285  ILE A N   1 
ATOM   3489 C CA  . ILE C 3 285 ? 224.292 177.484 212.964 1.00 55.20 ? 285  ILE A CA  1 
ATOM   3490 C C   . ILE C 3 285 ? 225.143 176.498 212.182 1.00 55.01 ? 285  ILE A C   1 
ATOM   3491 O O   . ILE C 3 285 ? 225.633 175.515 212.736 1.00 53.64 ? 285  ILE A O   1 
ATOM   3492 C CB  . ILE C 3 285 ? 225.170 178.211 213.999 1.00 53.54 ? 285  ILE A CB  1 
ATOM   3493 C CG1 . ILE C 3 285 ? 224.340 179.207 214.790 1.00 53.82 ? 285  ILE A CG1 1 
ATOM   3494 C CG2 . ILE C 3 285 ? 226.295 178.954 213.276 1.00 53.55 ? 285  ILE A CG2 1 
ATOM   3495 C CD1 . ILE C 3 285 ? 225.029 179.720 216.043 1.00 50.83 ? 285  ILE A CD1 1 
ATOM   3496 N N   . THR C 3 286 ? 225.296 176.752 210.889 1.00 55.17 ? 286  THR A N   1 
ATOM   3497 C CA  . THR C 3 286 ? 226.038 175.848 210.023 1.00 54.78 ? 286  THR A CA  1 
ATOM   3498 C C   . THR C 3 286 ? 227.339 176.473 209.555 1.00 54.07 ? 286  THR A C   1 
ATOM   3499 O O   . THR C 3 286 ? 228.235 175.775 209.079 1.00 53.68 ? 286  THR A O   1 
ATOM   3500 C CB  . THR C 3 286 ? 225.196 175.434 208.806 1.00 56.12 ? 286  THR A CB  1 
ATOM   3501 O OG1 . THR C 3 286 ? 224.869 176.597 208.033 1.00 56.86 ? 286  THR A OG1 1 
ATOM   3502 C CG2 . THR C 3 286 ? 223.913 174.756 209.267 1.00 57.56 ? 286  THR A CG2 1 
ATOM   3503 N N   . ASP C 3 287 ? 227.447 177.787 209.703 1.00 54.01 ? 287  ASP A N   1 
ATOM   3504 C CA  . ASP C 3 287 ? 228.661 178.489 209.305 1.00 53.72 ? 287  ASP A CA  1 
ATOM   3505 C C   . ASP C 3 287 ? 228.866 179.753 210.126 1.00 54.49 ? 287  ASP A C   1 
ATOM   3506 O O   . ASP C 3 287 ? 227.934 180.258 210.756 1.00 55.12 ? 287  ASP A O   1 
ATOM   3507 C CB  . ASP C 3 287 ? 228.620 178.836 207.813 1.00 55.15 ? 287  ASP A CB  1 
ATOM   3508 N N   . ALA C 3 288 ? 230.091 180.261 210.113 1.00 53.88 ? 288  ALA A N   1 
ATOM   3509 C CA  . ALA C 3 288 ? 230.412 181.501 210.807 1.00 54.44 ? 288  ALA A CA  1 
ATOM   3510 C C   . ALA C 3 288 ? 231.613 182.186 210.172 1.00 55.11 ? 288  ALA A C   1 
ATOM   3511 O O   . ALA C 3 288 ? 232.564 181.531 209.746 1.00 54.88 ? 288  ALA A O   1 
ATOM   3512 C CB  . ALA C 3 288 ? 230.686 181.226 212.277 1.00 53.33 ? 288  ALA A CB  1 
ATOM   3513 N N   . VAL C 3 289 ? 231.590 183.513 210.161 1.00 55.50 ? 289  VAL A N   1 
ATOM   3514 C CA  . VAL C 3 289 ? 232.703 184.289 209.635 1.00 55.92 ? 289  VAL A CA  1 
ATOM   3515 C C   . VAL C 3 289 ? 233.357 185.140 210.711 1.00 57.15 ? 289  VAL A C   1 
ATOM   3516 O O   . VAL C 3 289 ? 232.699 185.952 211.359 1.00 55.65 ? 289  VAL A O   1 
ATOM   3517 C CB  . VAL C 3 289 ? 232.222 185.206 208.492 1.00 56.93 ? 289  VAL A CB  1 
ATOM   3518 C CG1 . VAL C 3 289 ? 233.378 186.046 207.957 1.00 58.87 ? 289  VAL A CG1 1 
ATOM   3519 C CG2 . VAL C 3 289 ? 231.615 184.360 207.386 1.00 58.09 ? 289  VAL A CG2 1 
ATOM   3520 N N   . ASP C 3 290 ? 234.667 184.976 210.871 1.00 55.02 ? 290  ASP A N   1 
ATOM   3521 C CA  . ASP C 3 290 ? 235.434 185.801 211.800 1.00 55.57 ? 290  ASP A CA  1 
ATOM   3522 C C   . ASP C 3 290 ? 235.811 187.109 211.111 1.00 55.53 ? 290  ASP A C   1 
ATOM   3523 O O   . ASP C 3 290 ? 236.658 187.121 210.215 1.00 59.43 ? 290  ASP A O   1 
ATOM   3524 C CB  . ASP C 3 290 ? 236.691 185.065 212.284 1.00 53.83 ? 290  ASP A CB  1 
ATOM   3525 C CG  . ASP C 3 290 ? 237.512 185.885 213.292 1.00 53.53 ? 290  ASP A CG  1 
ATOM   3526 O OD1 . ASP C 3 290 ? 237.316 187.080 213.347 1.00 55.77 ? 290  ASP A OD1 1 
ATOM   3527 O OD2 . ASP C 3 290 ? 238.327 185.312 213.994 1.00 52.99 ? 290  ASP A OD2 1 
ATOM   3528 N N   . CYS C 3 291 ? 235.143 188.200 211.499 1.00 56.69 ? 291  CYS A N   1 
ATOM   3529 C CA  . CYS C 3 291 ? 235.217 189.477 210.797 1.00 59.28 ? 291  CYS A CA  1 
ATOM   3530 C C   . CYS C 3 291 ? 236.569 190.154 210.999 1.00 57.94 ? 291  CYS A C   1 
ATOM   3531 O O   . CYS C 3 291 ? 236.864 191.172 210.374 1.00 59.35 ? 291  CYS A O   1 
ATOM   3532 C CB  . CYS C 3 291 ? 234.106 190.418 211.283 1.00 57.69 ? 291  CYS A CB  1 
ATOM   3533 S SG  . CYS C 3 291 ? 232.422 189.761 211.085 1.00 59.57 ? 291  CYS A SG  1 
ATOM   3534 N N   . ALA C 3 292 ? 237.381 189.609 211.901 1.00 57.31 ? 292  ALA A N   1 
ATOM   3535 C CA  . ALA C 3 292 ? 238.689 190.183 212.193 1.00 57.94 ? 292  ALA A CA  1 
ATOM   3536 C C   . ALA C 3 292 ? 239.821 189.318 211.645 1.00 57.57 ? 292  ALA A C   1 
ATOM   3537 O O   . ALA C 3 292 ? 240.993 189.580 211.914 1.00 57.78 ? 292  ALA A O   1 
ATOM   3538 C CB  . ALA C 3 292 ? 238.857 190.358 213.694 1.00 56.17 ? 292  ALA A CB  1 
ATOM   3539 N N   . LEU C 3 293 ? 239.474 188.277 210.895 1.00 57.73 ? 293  LEU A N   1 
ATOM   3540 C CA  . LEU C 3 293 ? 240.475 187.342 210.391 1.00 58.98 ? 293  LEU A CA  1 
ATOM   3541 C C   . LEU C 3 293 ? 241.300 187.915 209.241 1.00 59.81 ? 293  LEU A C   1 
ATOM   3542 O O   . LEU C 3 293 ? 242.530 187.863 209.264 1.00 60.56 ? 293  LEU A O   1 
ATOM   3543 C CB  . LEU C 3 293 ? 239.788 186.053 209.928 1.00 58.55 ? 293  LEU A CB  1 
ATOM   3544 C CG  . LEU C 3 293 ? 240.693 184.970 209.318 1.00 57.74 ? 293  LEU A CG  1 
ATOM   3545 C CD1 . LEU C 3 293 ? 241.686 184.471 210.367 1.00 55.28 ? 293  LEU A CD1 1 
ATOM   3546 C CD2 . LEU C 3 293 ? 239.823 183.838 208.804 1.00 56.11 ? 293  LEU A CD2 1 
ATOM   3547 N N   . ASP C 3 294 ? 240.622 188.431 208.221 1.00 60.50 ? 294  ASP A N   1 
ATOM   3548 C CA  . ASP C 3 294 ? 241.294 188.948 207.034 1.00 61.93 ? 294  ASP A CA  1 
ATOM   3549 C C   . ASP C 3 294 ? 240.332 189.881 206.275 1.00 63.83 ? 294  ASP A C   1 
ATOM   3550 O O   . ASP C 3 294 ? 239.148 189.929 206.612 1.00 63.03 ? 294  ASP A O   1 
ATOM   3551 C CB  . ASP C 3 294 ? 241.770 187.763 206.171 1.00 62.13 ? 294  ASP A CB  1 
ATOM   3552 N N   . PRO C 3 295 ? 240.809 190.632 205.265 1.00 62.78 ? 295  PRO A N   1 
ATOM   3553 C CA  . PRO C 3 295 ? 240.041 191.544 204.425 1.00 60.89 ? 295  PRO A CA  1 
ATOM   3554 C C   . PRO C 3 295 ? 238.873 190.890 203.683 1.00 63.50 ? 295  PRO A C   1 
ATOM   3555 O O   . PRO C 3 295 ? 237.923 191.575 203.300 1.00 61.22 ? 295  PRO A O   1 
ATOM   3556 C CB  . PRO C 3 295 ? 241.105 192.055 203.443 1.00 63.74 ? 295  PRO A CB  1 
ATOM   3557 C CG  . PRO C 3 295 ? 242.412 191.914 204.188 1.00 63.33 ? 295  PRO A CG  1 
ATOM   3558 C CD  . PRO C 3 295 ? 242.258 190.646 204.985 1.00 63.32 ? 295  PRO A CD  1 
ATOM   3559 N N   . LEU C 3 296 ? 238.940 189.579 203.459 1.00 63.48 ? 296  LEU A N   1 
ATOM   3560 C CA  . LEU C 3 296 ? 237.863 188.901 202.747 1.00 63.44 ? 296  LEU A CA  1 
ATOM   3561 C C   . LEU C 3 296 ? 236.678 188.721 203.675 1.00 60.26 ? 296  LEU A C   1 
ATOM   3562 O O   . LEU C 3 296 ? 235.530 188.972 203.299 1.00 70.05 ? 296  LEU A O   1 
ATOM   3563 C CB  . LEU C 3 296 ? 238.330 187.541 202.209 1.00 62.88 ? 296  LEU A CB  1 
ATOM   3564 C CG  . LEU C 3 296 ? 237.271 186.705 201.449 1.00 64.56 ? 296  LEU A CG  1 
ATOM   3565 C CD1 . LEU C 3 296 ? 236.754 187.485 200.241 1.00 64.50 ? 296  LEU A CD1 1 
ATOM   3566 C CD2 . LEU C 3 296 ? 237.900 185.389 201.012 1.00 64.11 ? 296  LEU A CD2 1 
ATOM   3567 N N   . SER C 3 297 ? 236.971 188.324 204.906 1.00 67.73 ? 297  SER A N   1 
ATOM   3568 C CA  . SER C 3 297 ? 235.950 188.181 205.928 1.00 66.13 ? 297  SER A CA  1 
ATOM   3569 C C   . SER C 3 297 ? 235.348 189.537 206.257 1.00 56.44 ? 297  SER A C   1 
ATOM   3570 O O   . SER C 3 297 ? 234.139 189.652 206.455 1.00 65.07 ? 297  SER A O   1 
ATOM   3571 C CB  . SER C 3 297 ? 236.535 187.554 207.174 1.00 59.87 ? 297  SER A CB  1 
ATOM   3572 N N   . GLU C 3 298 ? 236.183 190.577 206.266 1.00 67.30 ? 298  GLU A N   1 
ATOM   3573 C CA  . GLU C 3 298 ? 235.697 191.923 206.541 1.00 67.01 ? 298  GLU A CA  1 
ATOM   3574 C C   . GLU C 3 298 ? 234.661 192.332 205.505 1.00 65.00 ? 298  GLU A C   1 
ATOM   3575 O O   . GLU C 3 298 ? 233.618 192.891 205.848 1.00 62.84 ? 298  GLU A O   1 
ATOM   3576 C CB  . GLU C 3 298 ? 236.848 192.932 206.528 1.00 61.28 ? 298  GLU A CB  1 
ATOM   3577 N N   . THR C 3 299 ? 234.934 192.020 204.240 1.00 65.49 ? 299  THR A N   1 
ATOM   3578 C CA  . THR C 3 299 ? 234.005 192.330 203.162 1.00 65.42 ? 299  THR A CA  1 
ATOM   3579 C C   . THR C 3 299 ? 232.696 191.570 203.333 1.00 60.09 ? 299  THR A C   1 
ATOM   3580 O O   . THR C 3 299 ? 231.614 192.148 203.220 1.00 67.94 ? 299  THR A O   1 
ATOM   3581 C CB  . THR C 3 299 ? 234.619 192.000 201.788 1.00 64.02 ? 299  THR A CB  1 
ATOM   3582 N N   . LYS C 3 300 ? 232.796 190.275 203.621 1.00 64.86 ? 300  LYS A N   1 
ATOM   3583 C CA  . LYS C 3 300 ? 231.608 189.447 203.803 1.00 65.53 ? 300  LYS A CA  1 
ATOM   3584 C C   . LYS C 3 300 ? 230.741 189.923 204.971 1.00 64.48 ? 300  LYS A C   1 
ATOM   3585 O O   . LYS C 3 300 ? 229.514 189.950 204.861 1.00 63.97 ? 300  LYS A O   1 
ATOM   3586 C CB  . LYS C 3 300 ? 232.003 187.982 204.004 1.00 63.90 ? 300  LYS A CB  1 
ATOM   3587 N N   . CYS C 3 301 ? 231.378 190.315 206.083 1.00 64.91 ? 301  CYS A N   1 
ATOM   3588 C CA  . CYS C 3 301 ? 230.671 190.812 207.262 1.00 64.43 ? 301  CYS A CA  1 
ATOM   3589 C C   . CYS C 3 301 ? 230.014 192.162 206.981 1.00 64.10 ? 301  CYS A C   1 
ATOM   3590 O O   . CYS C 3 301 ? 228.859 192.390 207.346 1.00 64.42 ? 301  CYS A O   1 
ATOM   3591 C CB  . CYS C 3 301 ? 231.631 190.939 208.454 1.00 62.93 ? 301  CYS A CB  1 
ATOM   3592 S SG  . CYS C 3 301 ? 232.198 189.348 209.119 1.00 62.43 ? 301  CYS A SG  1 
ATOM   3593 N N   . THR C 3 302 ? 230.736 193.043 206.297 1.00 63.23 ? 302  THR A N   1 
ATOM   3594 C CA  . THR C 3 302 ? 230.220 194.368 205.974 1.00 66.02 ? 302  THR A CA  1 
ATOM   3595 C C   . THR C 3 302 ? 228.959 194.272 205.126 1.00 65.12 ? 302  THR A C   1 
ATOM   3596 O O   . THR C 3 302 ? 227.990 194.999 205.349 1.00 65.49 ? 302  THR A O   1 
ATOM   3597 C CB  . THR C 3 302 ? 231.276 195.210 205.229 1.00 64.37 ? 302  THR A CB  1 
ATOM   3598 N N   . LEU C 3 303 ? 228.979 193.367 204.154 1.00 64.72 ? 303  LEU A N   1 
ATOM   3599 C CA  . LEU C 3 303 ? 227.874 193.203 203.220 1.00 65.41 ? 303  LEU A CA  1 
ATOM   3600 C C   . LEU C 3 303 ? 226.842 192.193 203.710 1.00 65.52 ? 303  LEU A C   1 
ATOM   3601 O O   . LEU C 3 303 ? 225.884 191.886 203.001 1.00 65.45 ? 303  LEU A O   1 
ATOM   3602 C CB  . LEU C 3 303 ? 228.413 192.744 201.860 1.00 65.15 ? 303  LEU A CB  1 
ATOM   3603 N N   . LYS C 3 304 ? 227.055 191.652 204.907 1.00 64.28 ? 304  LYS A N   1 
ATOM   3604 C CA  . LYS C 3 304 ? 226.162 190.644 205.475 1.00 65.25 ? 304  LYS A CA  1 
ATOM   3605 C C   . LYS C 3 304 ? 225.939 189.468 204.523 1.00 66.31 ? 304  LYS A C   1 
ATOM   3606 O O   . LYS C 3 304 ? 224.800 189.053 204.305 1.00 64.62 ? 304  LYS A O   1 
ATOM   3607 C CB  . LYS C 3 304 ? 224.817 191.269 205.844 1.00 64.94 ? 304  LYS A CB  1 
ATOM   3608 N N   . SER C 3 305 ? 227.034 188.943 203.961 1.00 63.97 ? 305  SER A N   1 
ATOM   3609 C CA  . SER C 3 305 ? 227.009 187.816 203.032 1.00 64.86 ? 305  SER A CA  1 
ATOM   3610 C C   . SER C 3 305 ? 228.385 187.158 202.968 1.00 64.96 ? 305  SER A C   1 
ATOM   3611 O O   . SER C 3 305 ? 228.661 186.189 203.679 1.00 65.45 ? 305  SER A O   1 
ATOM   3612 C CB  . SER C 3 305 ? 226.577 188.276 201.643 1.00 64.95 ? 305  SER A CB  1 
HETATM 3613 C C1  . NAG D 4 .   ? 228.587 160.453 242.226 1.00 25.55 ? 1    NAG B C1  1 
HETATM 3614 C C2  . NAG D 4 .   ? 228.360 159.216 243.166 1.00 25.70 ? 1    NAG B C2  1 
HETATM 3615 C C3  . NAG D 4 .   ? 226.895 159.238 243.651 1.00 26.71 ? 1    NAG B C3  1 
HETATM 3616 C C4  . NAG D 4 .   ? 226.607 160.557 244.387 1.00 27.12 ? 1    NAG B C4  1 
HETATM 3617 C C5  . NAG D 4 .   ? 226.882 161.722 243.415 1.00 26.45 ? 1    NAG B C5  1 
HETATM 3618 C C6  . NAG D 4 .   ? 226.646 163.070 244.072 1.00 26.71 ? 1    NAG B C6  1 
HETATM 3619 C C7  . NAG D 4 .   ? 229.267 156.978 242.900 1.00 26.42 ? 1    NAG B C7  1 
HETATM 3620 C C8  . NAG D 4 .   ? 229.458 155.715 242.119 1.00 26.46 ? 1    NAG B C8  1 
HETATM 3621 N N2  . NAG D 4 .   ? 228.561 157.983 242.396 1.00 25.86 ? 1    NAG B N2  1 
HETATM 3622 O O3  . NAG D 4 .   ? 226.663 158.140 244.540 1.00 27.41 ? 1    NAG B O3  1 
HETATM 3623 O O4  . NAG D 4 .   ? 225.220 160.573 244.760 1.00 27.70 ? 1    NAG B O4  1 
HETATM 3624 O O5  . NAG D 4 .   ? 228.269 161.666 242.948 1.00 25.83 ? 1    NAG B O5  1 
HETATM 3625 O O6  . NAG D 4 .   ? 227.568 163.315 245.128 1.00 25.65 ? 1    NAG B O6  1 
HETATM 3626 O O7  . NAG D 4 .   ? 229.776 157.077 244.023 1.00 26.13 ? 1    NAG B O7  1 
HETATM 3627 C C1  . NAG D 4 .   ? 225.022 160.798 246.220 1.00 28.13 ? 2    NAG B C1  1 
HETATM 3628 C C2  . NAG D 4 .   ? 223.509 161.056 246.496 1.00 28.35 ? 2    NAG B C2  1 
HETATM 3629 C C3  . NAG D 4 .   ? 223.347 161.336 248.003 1.00 29.05 ? 2    NAG B C3  1 
HETATM 3630 C C4  . NAG D 4 .   ? 223.879 160.130 248.814 1.00 29.22 ? 2    NAG B C4  1 
HETATM 3631 C C5  . NAG D 4 .   ? 225.368 159.915 248.442 1.00 28.73 ? 2    NAG B C5  1 
HETATM 3632 C C6  . NAG D 4 .   ? 225.950 158.714 249.164 1.00 29.78 ? 2    NAG B C6  1 
HETATM 3633 C C7  . NAG D 4 .   ? 222.415 162.103 244.597 1.00 27.52 ? 2    NAG B C7  1 
HETATM 3634 C C8  . NAG D 4 .   ? 221.977 163.313 243.828 1.00 26.20 ? 2    NAG B C8  1 
HETATM 3635 N N2  . NAG D 4 .   ? 223.076 162.237 245.740 1.00 28.10 ? 2    NAG B N2  1 
HETATM 3636 O O3  . NAG D 4 .   ? 221.958 161.546 248.280 1.00 29.66 ? 2    NAG B O3  1 
HETATM 3637 O O4  . NAG D 4 .   ? 223.798 160.421 250.225 1.00 29.91 ? 2    NAG B O4  1 
HETATM 3638 O O5  . NAG D 4 .   ? 225.505 159.687 247.000 1.00 28.38 ? 2    NAG B O5  1 
HETATM 3639 O O6  . NAG D 4 .   ? 227.343 158.584 248.908 1.00 28.97 ? 2    NAG B O6  1 
HETATM 3640 O O7  . NAG D 4 .   ? 222.155 160.976 244.157 1.00 27.48 ? 2    NAG B O7  1 
HETATM 3641 C C1  . BMA D 4 .   ? 222.530 159.955 250.880 1.00 30.47 ? 3    BMA B C1  1 
HETATM 3642 C C2  . BMA D 4 .   ? 222.886 159.321 252.260 1.00 30.71 ? 3    BMA B C2  1 
HETATM 3643 C C3  . BMA D 4 .   ? 221.578 158.826 252.910 1.00 30.76 ? 3    BMA B C3  1 
HETATM 3644 C C4  . BMA D 4 .   ? 220.604 160.014 253.059 1.00 30.68 ? 3    BMA B C4  1 
HETATM 3645 C C5  . BMA D 4 .   ? 220.329 160.610 251.658 1.00 30.44 ? 3    BMA B C5  1 
HETATM 3646 C C6  . BMA D 4 .   ? 219.416 161.820 251.735 1.00 30.77 ? 3    BMA B C6  1 
HETATM 3647 O O2  . BMA D 4 .   ? 223.530 160.283 253.091 1.00 30.75 ? 3    BMA B O2  1 
HETATM 3648 O O3  . BMA D 4 .   ? 221.864 158.264 254.198 1.00 30.46 ? 3    BMA B O3  1 
HETATM 3649 O O4  . BMA D 4 .   ? 219.389 159.552 253.639 1.00 30.40 ? 3    BMA B O4  1 
HETATM 3650 O O5  . BMA D 4 .   ? 221.590 161.038 251.045 1.00 30.36 ? 3    BMA B O5  1 
HETATM 3651 O O6  . BMA D 4 .   ? 218.972 162.213 250.443 1.00 31.23 ? 3    BMA B O6  1 
HETATM 3652 C C1  . NAG E 5 .   ? 251.100 180.024 214.998 1.00 47.28 ? 1301 NAG A C1  1 
HETATM 3653 C C2  . NAG E 5 .   ? 251.089 181.421 214.290 1.00 47.76 ? 1301 NAG A C2  1 
HETATM 3654 C C3  . NAG E 5 .   ? 251.963 181.333 213.021 1.00 48.77 ? 1301 NAG A C3  1 
HETATM 3655 C C4  . NAG E 5 .   ? 253.393 180.922 213.430 1.00 49.26 ? 1301 NAG A C4  1 
HETATM 3656 C C5  . NAG E 5 .   ? 253.333 179.558 214.156 1.00 48.47 ? 1301 NAG A C5  1 
HETATM 3657 C C6  . NAG E 5 .   ? 254.705 179.118 214.632 1.00 49.46 ? 1301 NAG A C6  1 
HETATM 3658 C C7  . NAG E 5 .   ? 248.961 182.517 214.698 1.00 47.84 ? 1301 NAG A C7  1 
HETATM 3659 C C8  . NAG E 5 .   ? 247.550 182.839 214.315 1.00 48.04 ? 1301 NAG A C8  1 
HETATM 3660 N N2  . NAG E 5 .   ? 249.708 181.746 213.914 1.00 47.87 ? 1301 NAG A N2  1 
HETATM 3661 O O3  . NAG E 5 .   ? 251.995 182.608 212.367 1.00 48.65 ? 1301 NAG A O3  1 
HETATM 3662 O O4  . NAG E 5 .   ? 254.203 180.820 212.265 1.00 49.42 ? 1301 NAG A O4  1 
HETATM 3663 O O5  . NAG E 5 .   ? 252.460 179.659 215.329 1.00 47.28 ? 1301 NAG A O5  1 
HETATM 3664 O O6  . NAG E 5 .   ? 254.668 177.797 215.157 1.00 50.56 ? 1301 NAG A O6  1 
HETATM 3665 O O7  . NAG E 5 .   ? 249.426 182.972 215.753 1.00 47.23 ? 1301 NAG A O7  1 
HETATM 3666 C C1  . NAG F 5 .   ? 216.058 170.539 208.668 1.00 64.33 ? 1302 NAG A C1  1 
HETATM 3667 C C2  . NAG F 5 .   ? 217.219 170.001 207.763 1.00 64.68 ? 1302 NAG A C2  1 
HETATM 3668 C C3  . NAG F 5 .   ? 216.624 169.008 206.741 1.00 65.04 ? 1302 NAG A C3  1 
HETATM 3669 C C4  . NAG F 5 .   ? 215.931 167.861 207.504 1.00 65.78 ? 1302 NAG A C4  1 
HETATM 3670 C C5  . NAG F 5 .   ? 214.824 168.457 208.402 1.00 64.73 ? 1302 NAG A C5  1 
HETATM 3671 C C6  . NAG F 5 .   ? 214.134 167.383 209.222 1.00 65.49 ? 1302 NAG A C6  1 
HETATM 3672 C C7  . NAG F 5 .   ? 219.127 171.354 207.104 1.00 64.39 ? 1302 NAG A C7  1 
HETATM 3673 C C8  . NAG F 5 .   ? 219.727 172.510 206.366 1.00 63.30 ? 1302 NAG A C8  1 
HETATM 3674 N N2  . NAG F 5 .   ? 217.819 171.132 207.045 1.00 64.16 ? 1302 NAG A N2  1 
HETATM 3675 O O3  . NAG F 5 .   ? 217.671 168.475 205.918 1.00 64.63 ? 1302 NAG A O3  1 
HETATM 3676 O O4  . NAG F 5 .   ? 215.365 166.950 206.570 1.00 65.39 ? 1302 NAG A O4  1 
HETATM 3677 O O5  . NAG F 5 .   ? 215.410 169.428 209.330 1.00 64.23 ? 1302 NAG A O5  1 
HETATM 3678 O O6  . NAG F 5 .   ? 213.005 167.906 209.909 1.00 64.83 ? 1302 NAG A O6  1 
HETATM 3679 O O7  . NAG F 5 .   ? 219.860 170.608 207.767 1.00 63.84 ? 1302 NAG A O7  1 
HETATM 3680 C C1  . NAG G 5 .   ? 233.610 179.320 257.807 1.00 34.20 ? 1303 NAG A C1  1 
HETATM 3681 C C2  . NAG G 5 .   ? 234.537 178.280 258.526 1.00 34.65 ? 1303 NAG A C2  1 
HETATM 3682 C C3  . NAG G 5 .   ? 234.885 178.830 259.926 1.00 35.18 ? 1303 NAG A C3  1 
HETATM 3683 C C4  . NAG G 5 .   ? 235.586 180.197 259.769 1.00 35.50 ? 1303 NAG A C4  1 
HETATM 3684 C C5  . NAG G 5 .   ? 234.638 181.160 259.019 1.00 35.12 ? 1303 NAG A C5  1 
HETATM 3685 C C6  . NAG G 5 .   ? 235.283 182.513 258.782 1.00 35.23 ? 1303 NAG A C6  1 
HETATM 3686 C C7  . NAG G 5 .   ? 234.513 175.814 258.608 1.00 35.38 ? 1303 NAG A C7  1 
HETATM 3687 C C8  . NAG G 5 .   ? 233.775 174.510 258.685 1.00 35.40 ? 1303 NAG A C8  1 
HETATM 3688 N N2  . NAG G 5 .   ? 233.812 177.012 258.675 1.00 34.66 ? 1303 NAG A N2  1 
HETATM 3689 O O3  . NAG G 5 .   ? 235.755 177.912 260.600 1.00 34.66 ? 1303 NAG A O3  1 
HETATM 3690 O O4  . NAG G 5 .   ? 235.894 180.718 261.057 1.00 35.00 ? 1303 NAG A O4  1 
HETATM 3691 O O5  . NAG G 5 .   ? 234.290 180.594 257.711 1.00 34.15 ? 1303 NAG A O5  1 
HETATM 3692 O O6  . NAG G 5 .   ? 234.350 183.438 258.240 1.00 33.72 ? 1303 NAG A O6  1 
HETATM 3693 O O7  . NAG G 5 .   ? 235.752 175.844 258.520 1.00 34.57 ? 1303 NAG A O7  1 
HETATM 3694 C C1  . NAG H 5 .   ? 240.949 188.195 240.943 1.00 30.63 ? 1304 NAG A C1  1 
HETATM 3695 C C2  . NAG H 5 .   ? 240.575 189.719 240.902 1.00 31.22 ? 1304 NAG A C2  1 
HETATM 3696 C C3  . NAG H 5 .   ? 241.711 190.484 240.189 1.00 31.66 ? 1304 NAG A C3  1 
HETATM 3697 C C4  . NAG H 5 .   ? 243.026 190.254 240.959 1.00 31.89 ? 1304 NAG A C4  1 
HETATM 3698 C C5  . NAG H 5 .   ? 243.322 188.739 241.003 1.00 31.33 ? 1304 NAG A C5  1 
HETATM 3699 C C6  . NAG H 5 .   ? 244.585 188.449 241.795 1.00 31.70 ? 1304 NAG A C6  1 
HETATM 3700 C C7  . NAG H 5 .   ? 238.185 190.136 240.774 1.00 31.39 ? 1304 NAG A C7  1 
HETATM 3701 C C8  . NAG H 5 .   ? 236.917 190.306 239.996 1.00 31.01 ? 1304 NAG A C8  1 
HETATM 3702 N N2  . NAG H 5 .   ? 239.329 189.891 240.144 1.00 31.10 ? 1304 NAG A N2  1 
HETATM 3703 O O3  . NAG H 5 .   ? 241.409 191.885 240.161 1.00 31.71 ? 1304 NAG A O3  1 
HETATM 3704 O O4  . NAG H 5 .   ? 244.085 190.935 240.296 1.00 32.42 ? 1304 NAG A O4  1 
HETATM 3705 O O5  . NAG H 5 .   ? 242.207 188.034 241.643 1.00 30.41 ? 1304 NAG A O5  1 
HETATM 3706 O O6  . NAG H 5 .   ? 244.813 187.052 241.924 1.00 30.65 ? 1304 NAG A O6  1 
HETATM 3707 O O7  . NAG H 5 .   ? 238.158 190.224 242.009 1.00 30.38 ? 1304 NAG A O7  1 
HETATM 3708 C C1  . NAG I 5 .   ? 243.761 145.002 228.318 1.00 34.33 ? 1305 NAG A C1  1 
HETATM 3709 C C2  . NAG I 5 .   ? 243.669 143.565 227.690 1.00 34.52 ? 1305 NAG A C2  1 
HETATM 3710 C C3  . NAG I 5 .   ? 244.975 142.806 228.017 1.00 34.89 ? 1305 NAG A C3  1 
HETATM 3711 C C4  . NAG I 5 .   ? 246.172 143.590 227.445 1.00 36.16 ? 1305 NAG A C4  1 
HETATM 3712 C C5  . NAG I 5 .   ? 246.184 145.003 228.068 1.00 36.41 ? 1305 NAG A C5  1 
HETATM 3713 C C6  . NAG I 5 .   ? 247.318 145.849 227.516 1.00 35.84 ? 1305 NAG A C6  1 
HETATM 3714 C C7  . NAG I 5 .   ? 241.789 142.031 227.538 1.00 34.75 ? 1305 NAG A C7  1 
HETATM 3715 C C8  . NAG I 5 .   ? 240.631 141.286 228.134 1.00 33.90 ? 1305 NAG A C8  1 
HETATM 3716 N N2  . NAG I 5 .   ? 242.532 142.846 228.284 1.00 34.19 ? 1305 NAG A N2  1 
HETATM 3717 O O3  . NAG I 5 .   ? 244.938 141.498 227.431 1.00 35.27 ? 1305 NAG A O3  1 
HETATM 3718 O O4  . NAG I 5 .   ? 247.377 142.906 227.770 1.00 36.36 ? 1305 NAG A O4  1 
HETATM 3719 O O5  . NAG I 5 .   ? 244.919 145.686 227.778 1.00 35.35 ? 1305 NAG A O5  1 
HETATM 3720 O O6  . NAG I 5 .   ? 247.231 145.996 226.103 1.00 36.38 ? 1305 NAG A O6  1 
HETATM 3721 O O7  . NAG I 5 .   ? 242.048 141.879 226.336 1.00 34.94 ? 1305 NAG A O7  1 
HETATM 3722 C C1  . NAG J 5 .   ? 254.528 168.018 248.140 1.00 39.64 ? 1306 NAG A C1  1 
HETATM 3723 C C2  . NAG J 5 .   ? 254.268 168.187 249.677 1.00 40.42 ? 1306 NAG A C2  1 
HETATM 3724 C C3  . NAG J 5 .   ? 254.123 169.692 249.983 1.00 41.53 ? 1306 NAG A C3  1 
HETATM 3725 C C4  . NAG J 5 .   ? 255.409 170.421 249.543 1.00 41.53 ? 1306 NAG A C4  1 
HETATM 3726 C C5  . NAG J 5 .   ? 255.622 170.187 248.030 1.00 40.31 ? 1306 NAG A C5  1 
HETATM 3727 C C6  . NAG J 5 .   ? 256.899 170.841 247.534 1.00 41.41 ? 1306 NAG A C6  1 
HETATM 3728 C C7  . NAG J 5 .   ? 253.039 166.254 250.488 1.00 41.16 ? 1306 NAG A C7  1 
HETATM 3729 C C8  . NAG J 5 .   ? 251.760 165.553 250.834 1.00 40.04 ? 1306 NAG A C8  1 
HETATM 3730 N N2  . NAG J 5 .   ? 253.017 167.499 250.022 1.00 40.81 ? 1306 NAG A N2  1 
HETATM 3731 O O3  . NAG J 5 .   ? 253.917 169.877 251.389 1.00 41.58 ? 1306 NAG A O3  1 
HETATM 3732 O O4  . NAG J 5 .   ? 255.276 171.812 249.811 1.00 42.01 ? 1306 NAG A O4  1 
HETATM 3733 O O5  . NAG J 5 .   ? 255.718 168.749 247.763 1.00 39.56 ? 1306 NAG A O5  1 
HETATM 3734 O O6  . NAG J 5 .   ? 256.921 170.909 246.114 1.00 40.47 ? 1306 NAG A O6  1 
HETATM 3735 O O7  . NAG J 5 .   ? 254.116 165.664 250.636 1.00 40.57 ? 1306 NAG A O7  1 
# 
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    SER 1    1    1   SER SER L . n 
A 1 2    TYR 2    2    2   TYR TYR L . n 
A 1 3    GLU 3    3    3   GLU GLU L . n 
A 1 4    LEU 4    4    4   LEU LEU L . n 
A 1 5    THR 5    5    5   THR THR L . n 
A 1 6    GLN 6    6    6   GLN GLN L . n 
A 1 7    PRO 7    7    7   PRO PRO L . n 
A 1 8    PRO 8    8    8   PRO PRO L . n 
A 1 9    SER 9    9    9   SER SER L . n 
A 1 10   VAL 10   10   10  VAL VAL L . n 
A 1 11   SER 11   11   11  SER SER L . n 
A 1 12   VAL 12   12   12  VAL VAL L . n 
A 1 13   SER 13   13   13  SER SER L . n 
A 1 14   PRO 14   14   14  PRO PRO L . n 
A 1 15   GLY 15   15   15  GLY GLY L . n 
A 1 16   GLN 16   16   16  GLN GLN L . n 
A 1 17   THR 17   17   17  THR THR L . n 
A 1 18   ALA 18   18   18  ALA ALA L . n 
A 1 19   SER 19   19   19  SER SER L . n 
A 1 20   ILE 20   20   20  ILE ILE L . n 
A 1 21   THR 21   21   21  THR THR L . n 
A 1 22   CYS 22   22   22  CYS CYS L . n 
A 1 23   SER 23   23   23  SER SER L . n 
A 1 24   GLY 24   24   24  GLY GLY L . n 
A 1 25   ASP 25   25   25  ASP ASP L . n 
A 1 26   LYS 26   26   26  LYS LYS L . n 
A 1 27   LEU 27   27   27  LEU LEU L . n 
A 1 28   GLY 28   28   28  GLY GLY L . n 
A 1 29   GLU 29   29   29  GLU GLU L . n 
A 1 30   THR 30   30   30  THR THR L . n 
A 1 31   TYR 31   31   31  TYR TYR L . n 
A 1 32   ALA 32   32   32  ALA ALA L . n 
A 1 33   SER 33   33   33  SER SER L . n 
A 1 34   TRP 34   34   34  TRP TRP L . n 
A 1 35   TYR 35   35   35  TYR TYR L . n 
A 1 36   GLN 36   36   36  GLN GLN L . n 
A 1 37   GLN 37   37   37  GLN GLN L . n 
A 1 38   LYS 38   38   38  LYS LYS L . n 
A 1 39   PRO 39   39   39  PRO PRO L . n 
A 1 40   GLY 40   40   40  GLY GLY L . n 
A 1 41   GLN 41   41   41  GLN GLN L . n 
A 1 42   SER 42   42   42  SER SER L . n 
A 1 43   PRO 43   43   43  PRO PRO L . n 
A 1 44   ILE 44   44   44  ILE ILE L . n 
A 1 45   LEU 45   45   45  LEU LEU L . n 
A 1 46   VAL 46   46   46  VAL VAL L . n 
A 1 47   ILE 47   47   47  ILE ILE L . n 
A 1 48   TYR 48   48   48  TYR TYR L . n 
A 1 49   GLN 49   49   49  GLN GLN L . n 
A 1 50   ASP 50   50   50  ASP ASP L . n 
A 1 51   ASN 51   51   51  ASN ASN L . n 
A 1 52   LYS 52   52   52  LYS LYS L . n 
A 1 53   ARG 53   53   53  ARG ARG L . n 
A 1 54   PRO 54   54   54  PRO PRO L . n 
A 1 55   SER 55   55   55  SER SER L . n 
A 1 56   GLY 56   56   56  GLY GLY L . n 
A 1 57   ILE 57   57   57  ILE ILE L . n 
A 1 58   PRO 58   58   58  PRO PRO L . n 
A 1 59   GLU 59   59   59  GLU GLU L . n 
A 1 60   ARG 60   60   60  ARG ARG L . n 
A 1 61   PHE 61   61   61  PHE PHE L . n 
A 1 62   SER 62   62   62  SER SER L . n 
A 1 63   GLY 63   63   63  GLY GLY L . n 
A 1 64   SER 64   64   64  SER SER L . n 
A 1 65   ASN 65   65   65  ASN ASN L . n 
A 1 66   SER 66   66   66  SER SER L . n 
A 1 67   GLU 67   67   67  GLU GLU L . n 
A 1 68   ASN 68   68   68  ASN ASN L . n 
A 1 69   THR 69   69   69  THR THR L . n 
A 1 70   ALA 70   70   70  ALA ALA L . n 
A 1 71   THR 71   71   71  THR THR L . n 
A 1 72   LEU 72   72   72  LEU LEU L . n 
A 1 73   THR 73   73   73  THR THR L . n 
A 1 74   ILE 74   74   74  ILE ILE L . n 
A 1 75   SER 75   75   75  SER SER L . n 
A 1 76   GLY 76   76   76  GLY GLY L . n 
A 1 77   THR 77   77   77  THR THR L . n 
A 1 78   GLN 78   78   78  GLN GLN L . n 
A 1 79   THR 79   79   79  THR THR L . n 
A 1 80   MET 80   80   80  MET MET L . n 
A 1 81   ASP 81   81   81  ASP ASP L . n 
A 1 82   GLU 82   82   82  GLU GLU L . n 
A 1 83   ALA 83   83   83  ALA ALA L . n 
A 1 84   ASP 84   84   84  ASP ASP L . n 
A 1 85   TYR 85   85   85  TYR TYR L . n 
A 1 86   TYR 86   86   86  TYR TYR L . n 
A 1 87   CYS 87   87   87  CYS CYS L . n 
A 1 88   GLN 88   88   88  GLN GLN L . n 
A 1 89   ALA 89   89   89  ALA ALA L . n 
A 1 90   TRP 90   90   90  TRP TRP L . n 
A 1 91   ASP 91   91   91  ASP ASP L . n 
A 1 92   LYS 92   92   92  LYS LYS L . n 
A 1 93   THR 93   93   93  THR THR L . n 
A 1 94   ILE 94   94   94  ILE ILE L . n 
A 1 95   ALA 95   95   95  ALA ALA L . n 
A 1 96   GLY 96   96   96  GLY GLY L . n 
A 1 97   PHE 97   97   97  PHE PHE L . n 
A 1 98   GLY 98   98   98  GLY GLY L . n 
A 1 99   GLY 99   99   99  GLY GLY L . n 
A 1 100  GLY 100  100  100 GLY GLY L . n 
A 1 101  THR 101  101  101 THR THR L . n 
A 1 102  LYS 102  102  102 LYS LYS L . n 
A 1 103  LEU 103  103  103 LEU LEU L . n 
A 1 104  THR 104  104  104 THR THR L . n 
A 1 105  VAL 105  105  105 VAL VAL L . n 
B 2 1    GLN 1    1    1   GLN GLN H . n 
B 2 2    ILE 2    2    2   ILE ILE H . n 
B 2 3    THR 3    3    3   THR THR H . n 
B 2 4    LEU 4    4    4   LEU LEU H . n 
B 2 5    LYS 5    5    5   LYS LYS H . n 
B 2 6    GLU 6    6    6   GLU GLU H . n 
B 2 7    SER 7    7    7   SER SER H . n 
B 2 8    GLY 8    8    8   GLY GLY H . n 
B 2 9    PRO 9    9    9   PRO PRO H . n 
B 2 10   THR 10   10   10  THR THR H . n 
B 2 11   LEU 11   11   11  LEU LEU H . n 
B 2 12   VAL 12   12   12  VAL VAL H . n 
B 2 13   LYS 13   13   13  LYS LYS H . n 
B 2 14   PRO 14   14   14  PRO PRO H . n 
B 2 15   THR 15   15   15  THR THR H . n 
B 2 16   GLN 16   16   16  GLN GLN H . n 
B 2 17   THR 17   17   17  THR THR H . n 
B 2 18   LEU 18   18   18  LEU LEU H . n 
B 2 19   THR 19   19   19  THR THR H . n 
B 2 20   LEU 20   20   20  LEU LEU H . n 
B 2 21   THR 21   21   21  THR THR H . n 
B 2 22   CYS 22   22   22  CYS CYS H . n 
B 2 23   LYS 23   23   23  LYS LYS H . n 
B 2 24   LEU 24   24   24  LEU LEU H . n 
B 2 25   SER 25   25   25  SER SER H . n 
B 2 26   GLY 26   26   26  GLY GLY H . n 
B 2 27   PHE 27   27   27  PHE PHE H . n 
B 2 28   SER 28   28   28  SER SER H . n 
B 2 29   VAL 29   29   29  VAL VAL H . n 
B 2 30   ASN 30   30   30  ASN ASN H . n 
B 2 31   THR 31   31   31  THR THR H . n 
B 2 32   GLY 32   32   32  GLY GLY H . n 
B 2 33   GLY 33   33   33  GLY GLY H . n 
B 2 34   VAL 34   34   34  VAL VAL H . n 
B 2 35   GLY 35   35   35  GLY GLY H . n 
B 2 36   VAL 36   36   36  VAL VAL H . n 
B 2 37   GLY 37   37   37  GLY GLY H . n 
B 2 38   TRP 38   38   38  TRP TRP H . n 
B 2 39   ILE 39   39   39  ILE ILE H . n 
B 2 40   ARG 40   40   40  ARG ARG H . n 
B 2 41   GLN 41   41   41  GLN GLN H . n 
B 2 42   PRO 42   42   42  PRO PRO H . n 
B 2 43   PRO 43   43   43  PRO PRO H . n 
B 2 44   GLY 44   44   44  GLY GLY H . n 
B 2 45   LYS 45   45   45  LYS LYS H . n 
B 2 46   ALA 46   46   46  ALA ALA H . n 
B 2 47   LEU 47   47   47  LEU LEU H . n 
B 2 48   GLU 48   48   48  GLU GLU H . n 
B 2 49   TRP 49   49   49  TRP TRP H . n 
B 2 50   LEU 50   50   50  LEU LEU H . n 
B 2 51   ALA 51   51   51  ALA ALA H . n 
B 2 52   LEU 52   52   52  LEU LEU H . n 
B 2 53   ILE 53   53   53  ILE ILE H . n 
B 2 54   TYR 54   54   54  TYR TYR H . n 
B 2 55   TRP 55   55   55  TRP TRP H . n 
B 2 56   ASN 56   56   56  ASN ASN H . n 
B 2 57   ASP 57   57   57  ASP ASP H . n 
B 2 58   ASP 58   58   58  ASP ASP H . n 
B 2 59   LYS 59   59   59  LYS LYS H . n 
B 2 60   LEU 60   60   60  LEU LEU H . n 
B 2 61   TYR 61   61   61  TYR TYR H . n 
B 2 62   SER 62   62   62  SER SER H . n 
B 2 63   PRO 63   63   63  PRO PRO H . n 
B 2 64   SER 64   64   64  SER SER H . n 
B 2 65   LEU 65   65   65  LEU LEU H . n 
B 2 66   LYS 66   66   66  LYS LYS H . n 
B 2 67   SER 67   67   67  SER SER H . n 
B 2 68   ARG 68   68   68  ARG ARG H . n 
B 2 69   LEU 69   69   69  LEU LEU H . n 
B 2 70   THR 70   70   70  THR THR H . n 
B 2 71   VAL 71   71   71  VAL VAL H . n 
B 2 72   THR 72   72   72  THR THR H . n 
B 2 73   LYS 73   73   73  LYS LYS H . n 
B 2 74   ASP 74   74   74  ASP ASP H . n 
B 2 75   THR 75   75   75  THR THR H . n 
B 2 76   SER 76   76   76  SER SER H . n 
B 2 77   LYS 77   77   77  LYS LYS H . n 
B 2 78   ASN 78   78   78  ASN ASN H . n 
B 2 79   GLN 79   79   79  GLN GLN H . n 
B 2 80   VAL 80   80   80  VAL VAL H . n 
B 2 81   VAL 81   81   81  VAL VAL H . n 
B 2 82   LEU 82   82   82  LEU LEU H . n 
B 2 83   THR 83   83   83  THR THR H . n 
B 2 84   MET 84   84   84  MET MET H . n 
B 2 85   THR 85   85   85  THR THR H . n 
B 2 86   ASN 86   86   86  ASN ASN H . n 
B 2 87   MET 87   87   87  MET MET H . n 
B 2 88   ASP 88   88   88  ASP ASP H . n 
B 2 89   PRO 89   89   89  PRO PRO H . n 
B 2 90   VAL 90   90   90  VAL VAL H . n 
B 2 91   ASP 91   91   91  ASP ASP H . n 
B 2 92   THR 92   92   92  THR THR H . n 
B 2 93   ALA 93   93   93  ALA ALA H . n 
B 2 94   THR 94   94   94  THR THR H . n 
B 2 95   TYR 95   95   95  TYR TYR H . n 
B 2 96   TYR 96   96   96  TYR TYR H . n 
B 2 97   CYS 97   97   97  CYS CYS H . n 
B 2 98   ALA 98   98   98  ALA ALA H . n 
B 2 99   HIS 99   99   99  HIS HIS H . n 
B 2 100  VAL 100  100  100 VAL VAL H . n 
B 2 101  LEU 101  101  101 LEU LEU H . n 
B 2 102  VAL 102  102  102 VAL VAL H . n 
B 2 103  TRP 103  103  103 TRP TRP H . n 
B 2 104  PHE 104  104  104 PHE PHE H . n 
B 2 105  GLY 105  105  105 GLY GLY H . n 
B 2 106  GLU 106  106  106 GLU GLU H . n 
B 2 107  VAL 107  107  107 VAL VAL H . n 
B 2 108  LEU 108  108  108 LEU LEU H . n 
B 2 109  PRO 109  109  109 PRO PRO H . n 
B 2 110  ASP 110  110  110 ASP ASP H . n 
B 2 111  ALA 111  111  111 ALA ALA H . n 
B 2 112  PHE 112  112  112 PHE PHE H . n 
B 2 113  ASP 113  113  113 ASP ASP H . n 
B 2 114  VAL 114  114  114 VAL VAL H . n 
B 2 115  TRP 115  115  115 TRP TRP H . n 
B 2 116  GLY 116  116  116 GLY GLY H . n 
B 2 117  GLN 117  117  117 GLN GLN H . n 
B 2 118  GLY 118  118  118 GLY GLY H . n 
B 2 119  THR 119  119  119 THR THR H . n 
B 2 120  MET 120  120  120 MET MET H . n 
B 2 121  VAL 121  121  121 VAL VAL H . n 
B 2 122  THR 122  122  122 THR THR H . n 
B 2 123  VAL 123  123  123 VAL VAL H . n 
B 2 124  SER 124  124  124 SER SER H . n 
B 2 125  SER 125  125  125 SER SER H . n 
C 3 1    MET 1    1    ?   ?   ?   A . n 
C 3 2    PHE 2    2    ?   ?   ?   A . n 
C 3 3    VAL 3    3    ?   ?   ?   A . n 
C 3 4    PHE 4    4    ?   ?   ?   A . n 
C 3 5    LEU 5    5    ?   ?   ?   A . n 
C 3 6    VAL 6    6    ?   ?   ?   A . n 
C 3 7    LEU 7    7    ?   ?   ?   A . n 
C 3 8    LEU 8    8    ?   ?   ?   A . n 
C 3 9    PRO 9    9    ?   ?   ?   A . n 
C 3 10   LEU 10   10   ?   ?   ?   A . n 
C 3 11   VAL 11   11   ?   ?   ?   A . n 
C 3 12   SER 12   12   ?   ?   ?   A . n 
C 3 13   SER 13   13   ?   ?   ?   A . n 
C 3 14   GLN 14   14   14  GLN GLN A . n 
C 3 15   CYS 15   15   15  CYS CYS A . n 
C 3 16   VAL 16   16   16  VAL VAL A . n 
C 3 17   ASN 17   17   17  ASN ASN A . n 
C 3 18   LEU 18   18   18  LEU LEU A . n 
C 3 19   THR 19   19   19  THR THR A . n 
C 3 20   THR 20   20   20  THR THR A . n 
C 3 21   ARG 21   21   ?   ?   ?   A . n 
C 3 22   THR 22   22   ?   ?   ?   A . n 
C 3 23   GLN 23   23   ?   ?   ?   A . n 
C 3 24   LEU 24   24   ?   ?   ?   A . n 
C 3 25   PRO 25   25   ?   ?   ?   A . n 
C 3 26   PRO 26   26   26  PRO PRO A . n 
C 3 27   ALA 27   27   27  ALA ALA A . n 
C 3 28   TYR 28   28   28  TYR TYR A . n 
C 3 29   THR 29   29   29  THR THR A . n 
C 3 30   ASN 30   30   30  ASN ASN A . n 
C 3 31   SER 31   31   31  SER SER A . n 
C 3 32   PHE 32   32   32  PHE PHE A . n 
C 3 33   THR 33   33   33  THR THR A . n 
C 3 34   ARG 34   34   34  ARG ARG A . n 
C 3 35   GLY 35   35   35  GLY GLY A . n 
C 3 36   VAL 36   36   36  VAL VAL A . n 
C 3 37   TYR 37   37   37  TYR TYR A . n 
C 3 38   TYR 38   38   38  TYR TYR A . n 
C 3 39   PRO 39   39   39  PRO PRO A . n 
C 3 40   ASP 40   40   40  ASP ASP A . n 
C 3 41   LYS 41   41   41  LYS LYS A . n 
C 3 42   VAL 42   42   42  VAL VAL A . n 
C 3 43   PHE 43   43   43  PHE PHE A . n 
C 3 44   ARG 44   44   44  ARG ARG A . n 
C 3 45   SER 45   45   45  SER SER A . n 
C 3 46   SER 46   46   46  SER SER A . n 
C 3 47   VAL 47   47   47  VAL VAL A . n 
C 3 48   LEU 48   48   48  LEU LEU A . n 
C 3 49   HIS 49   49   49  HIS HIS A . n 
C 3 50   SER 50   50   50  SER SER A . n 
C 3 51   THR 51   51   51  THR THR A . n 
C 3 52   GLN 52   52   52  GLN GLN A . n 
C 3 53   ASP 53   53   53  ASP ASP A . n 
C 3 54   LEU 54   54   54  LEU LEU A . n 
C 3 55   PHE 55   55   55  PHE PHE A . n 
C 3 56   LEU 56   56   56  LEU LEU A . n 
C 3 57   PRO 57   57   57  PRO PRO A . n 
C 3 58   PHE 58   58   58  PHE PHE A . n 
C 3 59   PHE 59   59   59  PHE PHE A . n 
C 3 60   SER 60   60   60  SER SER A . n 
C 3 61   ASN 61   61   61  ASN ASN A . n 
C 3 62   VAL 62   62   62  VAL VAL A . n 
C 3 63   THR 63   63   63  THR THR A . n 
C 3 64   TRP 64   64   64  TRP TRP A . n 
C 3 65   PHE 65   65   65  PHE PHE A . n 
C 3 66   HIS 66   66   66  HIS HIS A . n 
C 3 67   ALA 67   67   67  ALA ALA A . n 
C 3 68   ILE 68   68   ?   ?   ?   A . n 
C 3 69   HIS 69   69   ?   ?   ?   A . n 
C 3 70   VAL 70   70   ?   ?   ?   A . n 
C 3 71   SER 71   71   ?   ?   ?   A . n 
C 3 72   GLY 72   72   ?   ?   ?   A . n 
C 3 73   THR 73   73   ?   ?   ?   A . n 
C 3 74   ASN 74   74   ?   ?   ?   A . n 
C 3 75   GLY 75   75   ?   ?   ?   A . n 
C 3 76   THR 76   76   ?   ?   ?   A . n 
C 3 77   LYS 77   77   ?   ?   ?   A . n 
C 3 78   ARG 78   78   78  ARG ARG A . n 
C 3 79   PHE 79   79   79  PHE PHE A . n 
C 3 80   ASP 80   80   80  ASP ASP A . n 
C 3 81   ASN 81   81   81  ASN ASN A . n 
C 3 82   PRO 82   82   82  PRO PRO A . n 
C 3 83   VAL 83   83   83  VAL VAL A . n 
C 3 84   LEU 84   84   84  LEU LEU A . n 
C 3 85   PRO 85   85   85  PRO PRO A . n 
C 3 86   PHE 86   86   86  PHE PHE A . n 
C 3 87   ASN 87   87   87  ASN ASN A . n 
C 3 88   ASP 88   88   88  ASP ASP A . n 
C 3 89   GLY 89   89   89  GLY GLY A . n 
C 3 90   VAL 90   90   90  VAL VAL A . n 
C 3 91   TYR 91   91   91  TYR TYR A . n 
C 3 92   PHE 92   92   92  PHE PHE A . n 
C 3 93   ALA 93   93   93  ALA ALA A . n 
C 3 94   SER 94   94   94  SER SER A . n 
C 3 95   ILE 95   95   95  ILE ILE A . n 
C 3 96   GLU 96   96   96  GLU GLU A . n 
C 3 97   LYS 97   97   97  LYS LYS A . n 
C 3 98   SER 98   98   98  SER SER A . n 
C 3 99   ASN 99   99   99  ASN ASN A . n 
C 3 100  ILE 100  100  100 ILE ILE A . n 
C 3 101  ILE 101  101  101 ILE ILE A . n 
C 3 102  ARG 102  102  102 ARG ARG A . n 
C 3 103  GLY 103  103  103 GLY GLY A . n 
C 3 104  TRP 104  104  104 TRP TRP A . n 
C 3 105  ILE 105  105  105 ILE ILE A . n 
C 3 106  PHE 106  106  106 PHE PHE A . n 
C 3 107  GLY 107  107  107 GLY GLY A . n 
C 3 108  THR 108  108  108 THR THR A . n 
C 3 109  THR 109  109  109 THR THR A . n 
C 3 110  LEU 110  110  110 LEU LEU A . n 
C 3 111  ASP 111  111  111 ASP ASP A . n 
C 3 112  SER 112  112  112 SER SER A . n 
C 3 113  LYS 113  113  113 LYS LYS A . n 
C 3 114  THR 114  114  114 THR THR A . n 
C 3 115  GLN 115  115  115 GLN GLN A . n 
C 3 116  SER 116  116  116 SER SER A . n 
C 3 117  LEU 117  117  117 LEU LEU A . n 
C 3 118  LEU 118  118  118 LEU LEU A . n 
C 3 119  ILE 119  119  119 ILE ILE A . n 
C 3 120  VAL 120  120  120 VAL VAL A . n 
C 3 121  ASN 121  121  121 ASN ASN A . n 
C 3 122  ASN 122  122  122 ASN ASN A . n 
C 3 123  ALA 123  123  123 ALA ALA A . n 
C 3 124  THR 124  124  124 THR THR A . n 
C 3 125  ASN 125  125  125 ASN ASN A . n 
C 3 126  VAL 126  126  126 VAL VAL A . n 
C 3 127  VAL 127  127  127 VAL VAL A . n 
C 3 128  ILE 128  128  128 ILE ILE A . n 
C 3 129  LYS 129  129  129 LYS LYS A . n 
C 3 130  VAL 130  130  130 VAL VAL A . n 
C 3 131  CYS 131  131  131 CYS CYS A . n 
C 3 132  GLU 132  132  132 GLU GLU A . n 
C 3 133  PHE 133  133  133 PHE PHE A . n 
C 3 134  GLN 134  134  134 GLN GLN A . n 
C 3 135  PHE 135  135  135 PHE PHE A . n 
C 3 136  CYS 136  136  136 CYS CYS A . n 
C 3 137  ASN 137  137  137 ASN ASN A . n 
C 3 138  ASP 138  138  138 ASP ASP A . n 
C 3 139  PRO 139  139  139 PRO PRO A . n 
C 3 140  PHE 140  140  140 PHE PHE A . n 
C 3 141  LEU 141  141  141 LEU LEU A . n 
C 3 142  ASP 142  142  142 ASP ASP A . n 
C 3 143  VAL 143  143  143 VAL VAL A . n 
C 3 144  TYR 144  144  144 TYR TYR A . n 
C 3 145  TYR 145  145  145 TYR TYR A . n 
C 3 146  HIS 146  146  146 HIS HIS A . n 
C 3 147  LYS 147  147  147 LYS LYS A . n 
C 3 148  ASN 148  148  148 ASN ASN A . n 
C 3 149  ASN 149  149  149 ASN ASN A . n 
C 3 150  LYS 150  150  150 LYS LYS A . n 
C 3 151  SER 151  151  151 SER SER A . n 
C 3 152  TRP 152  152  152 TRP TRP A . n 
C 3 153  MET 153  153  153 MET MET A . n 
C 3 154  LYS 154  154  154 LYS LYS A . n 
C 3 155  SER 155  155  155 SER SER A . n 
C 3 156  GLU 156  156  156 GLU GLU A . n 
C 3 157  PHE 157  157  157 PHE PHE A . n 
C 3 158  ARG 158  158  158 ARG ARG A . n 
C 3 159  VAL 159  159  159 VAL VAL A . n 
C 3 160  TYR 160  160  160 TYR TYR A . n 
C 3 161  SER 161  161  161 SER SER A . n 
C 3 162  SER 162  162  162 SER SER A . n 
C 3 163  ALA 163  163  163 ALA ALA A . n 
C 3 164  ASN 164  164  164 ASN ASN A . n 
C 3 165  ASN 165  165  165 ASN ASN A . n 
C 3 166  CYS 166  166  166 CYS CYS A . n 
C 3 167  THR 167  167  167 THR THR A . n 
C 3 168  PHE 168  168  168 PHE PHE A . n 
C 3 169  GLU 169  169  169 GLU GLU A . n 
C 3 170  TYR 170  170  170 TYR TYR A . n 
C 3 171  VAL 171  171  171 VAL VAL A . n 
C 3 172  SER 172  172  172 SER SER A . n 
C 3 173  GLN 173  173  173 GLN GLN A . n 
C 3 174  PRO 174  174  174 PRO PRO A . n 
C 3 175  PHE 175  175  175 PHE PHE A . n 
C 3 176  LEU 176  176  176 LEU LEU A . n 
C 3 177  MET 177  177  ?   ?   ?   A . n 
C 3 178  ASP 178  178  ?   ?   ?   A . n 
C 3 179  LEU 179  179  ?   ?   ?   A . n 
C 3 180  GLU 180  180  ?   ?   ?   A . n 
C 3 181  GLY 181  181  ?   ?   ?   A . n 
C 3 182  LYS 182  182  ?   ?   ?   A . n 
C 3 183  GLN 183  183  ?   ?   ?   A . n 
C 3 184  GLY 184  184  ?   ?   ?   A . n 
C 3 185  ASN 185  185  ?   ?   ?   A . n 
C 3 186  PHE 186  186  186 PHE PHE A . n 
C 3 187  LYS 187  187  187 LYS LYS A . n 
C 3 188  ASN 188  188  188 ASN ASN A . n 
C 3 189  LEU 189  189  189 LEU LEU A . n 
C 3 190  ARG 190  190  190 ARG ARG A . n 
C 3 191  GLU 191  191  191 GLU GLU A . n 
C 3 192  PHE 192  192  192 PHE PHE A . n 
C 3 193  VAL 193  193  193 VAL VAL A . n 
C 3 194  PHE 194  194  194 PHE PHE A . n 
C 3 195  LYS 195  195  195 LYS LYS A . n 
C 3 196  ASN 196  196  196 ASN ASN A . n 
C 3 197  ILE 197  197  197 ILE ILE A . n 
C 3 198  ASP 198  198  198 ASP ASP A . n 
C 3 199  GLY 199  199  199 GLY GLY A . n 
C 3 200  TYR 200  200  200 TYR TYR A . n 
C 3 201  PHE 201  201  201 PHE PHE A . n 
C 3 202  LYS 202  202  202 LYS LYS A . n 
C 3 203  ILE 203  203  203 ILE ILE A . n 
C 3 204  TYR 204  204  204 TYR TYR A . n 
C 3 205  SER 205  205  205 SER SER A . n 
C 3 206  LYS 206  206  206 LYS LYS A . n 
C 3 207  HIS 207  207  207 HIS HIS A . n 
C 3 208  THR 208  208  208 THR THR A . n 
C 3 209  PRO 209  209  209 PRO PRO A . n 
C 3 210  ILE 210  210  210 ILE ILE A . n 
C 3 211  ASN 211  211  211 ASN ASN A . n 
C 3 212  LEU 212  212  212 LEU LEU A . n 
C 3 213  VAL 213  213  213 VAL VAL A . n 
C 3 214  ARG 214  214  214 ARG ARG A . n 
C 3 215  ASP 215  215  215 ASP ASP A . n 
C 3 216  LEU 216  216  216 LEU LEU A . n 
C 3 217  PRO 217  217  217 PRO PRO A . n 
C 3 218  GLN 218  218  218 GLN GLN A . n 
C 3 219  GLY 219  219  219 GLY GLY A . n 
C 3 220  PHE 220  220  220 PHE PHE A . n 
C 3 221  SER 221  221  221 SER SER A . n 
C 3 222  ALA 222  222  222 ALA ALA A . n 
C 3 223  LEU 223  223  223 LEU LEU A . n 
C 3 224  GLU 224  224  224 GLU GLU A . n 
C 3 225  PRO 225  225  225 PRO PRO A . n 
C 3 226  LEU 226  226  226 LEU LEU A . n 
C 3 227  VAL 227  227  227 VAL VAL A . n 
C 3 228  ASP 228  228  228 ASP ASP A . n 
C 3 229  LEU 229  229  229 LEU LEU A . n 
C 3 230  PRO 230  230  230 PRO PRO A . n 
C 3 231  ILE 231  231  231 ILE ILE A . n 
C 3 232  GLY 232  232  232 GLY GLY A . n 
C 3 233  ILE 233  233  233 ILE ILE A . n 
C 3 234  ASN 234  234  234 ASN ASN A . n 
C 3 235  ILE 235  235  235 ILE ILE A . n 
C 3 236  THR 236  236  236 THR THR A . n 
C 3 237  ARG 237  237  237 ARG ARG A . n 
C 3 238  PHE 238  238  238 PHE PHE A . n 
C 3 239  GLN 239  239  239 GLN GLN A . n 
C 3 240  THR 240  240  240 THR THR A . n 
C 3 241  LEU 241  241  241 LEU LEU A . n 
C 3 242  LEU 242  242  242 LEU LEU A . n 
C 3 243  ALA 243  243  243 ALA ALA A . n 
C 3 244  LEU 244  244  244 LEU LEU A . n 
C 3 245  HIS 245  245  245 HIS HIS A . n 
C 3 246  ARG 246  246  246 ARG ARG A . n 
C 3 247  SER 247  247  ?   ?   ?   A . n 
C 3 248  TYR 248  248  ?   ?   ?   A . n 
C 3 249  LEU 249  249  ?   ?   ?   A . n 
C 3 250  THR 250  250  ?   ?   ?   A . n 
C 3 251  PRO 251  251  ?   ?   ?   A . n 
C 3 252  GLY 252  252  ?   ?   ?   A . n 
C 3 253  ASP 253  253  ?   ?   ?   A . n 
C 3 254  SER 254  254  ?   ?   ?   A . n 
C 3 255  SER 255  255  ?   ?   ?   A . n 
C 3 256  SER 256  256  ?   ?   ?   A . n 
C 3 257  GLY 257  257  257 GLY GLY A . n 
C 3 258  TRP 258  258  258 TRP TRP A . n 
C 3 259  THR 259  259  259 THR THR A . n 
C 3 260  ALA 260  260  260 ALA ALA A . n 
C 3 261  GLY 261  261  261 GLY GLY A . n 
C 3 262  ALA 262  262  262 ALA ALA A . n 
C 3 263  ALA 263  263  263 ALA ALA A . n 
C 3 264  ALA 264  264  264 ALA ALA A . n 
C 3 265  TYR 265  265  265 TYR TYR A . n 
C 3 266  TYR 266  266  266 TYR TYR A . n 
C 3 267  VAL 267  267  267 VAL VAL A . n 
C 3 268  GLY 268  268  268 GLY GLY A . n 
C 3 269  TYR 269  269  269 TYR TYR A . n 
C 3 270  LEU 270  270  270 LEU LEU A . n 
C 3 271  GLN 271  271  271 GLN GLN A . n 
C 3 272  PRO 272  272  272 PRO PRO A . n 
C 3 273  ARG 273  273  273 ARG ARG A . n 
C 3 274  THR 274  274  274 THR THR A . n 
C 3 275  PHE 275  275  275 PHE PHE A . n 
C 3 276  LEU 276  276  276 LEU LEU A . n 
C 3 277  LEU 277  277  277 LEU LEU A . n 
C 3 278  LYS 278  278  278 LYS LYS A . n 
C 3 279  TYR 279  279  279 TYR TYR A . n 
C 3 280  ASN 280  280  280 ASN ASN A . n 
C 3 281  GLU 281  281  281 GLU GLU A . n 
C 3 282  ASN 282  282  282 ASN ASN A . n 
C 3 283  GLY 283  283  283 GLY GLY A . n 
C 3 284  THR 284  284  284 THR THR A . n 
C 3 285  ILE 285  285  285 ILE ILE A . n 
C 3 286  THR 286  286  286 THR THR A . n 
C 3 287  ASP 287  287  287 ASP ASP A . n 
C 3 288  ALA 288  288  288 ALA ALA A . n 
C 3 289  VAL 289  289  289 VAL VAL A . n 
C 3 290  ASP 290  290  290 ASP ASP A . n 
C 3 291  CYS 291  291  291 CYS CYS A . n 
C 3 292  ALA 292  292  292 ALA ALA A . n 
C 3 293  LEU 293  293  293 LEU LEU A . n 
C 3 294  ASP 294  294  294 ASP ASP A . n 
C 3 295  PRO 295  295  295 PRO PRO A . n 
C 3 296  LEU 296  296  296 LEU LEU A . n 
C 3 297  SER 297  297  297 SER SER A . n 
C 3 298  GLU 298  298  298 GLU GLU A . n 
C 3 299  THR 299  299  299 THR THR A . n 
C 3 300  LYS 300  300  300 LYS LYS A . n 
C 3 301  CYS 301  301  301 CYS CYS A . n 
C 3 302  THR 302  302  302 THR THR A . n 
C 3 303  LEU 303  303  303 LEU LEU A . n 
C 3 304  LYS 304  304  304 LYS LYS A . n 
C 3 305  SER 305  305  305 SER SER A . n 
C 3 306  PHE 306  306  ?   ?   ?   A . n 
C 3 307  THR 307  307  ?   ?   ?   A . n 
C 3 308  VAL 308  308  ?   ?   ?   A . n 
C 3 309  GLU 309  309  ?   ?   ?   A . n 
C 3 310  LYS 310  310  ?   ?   ?   A . n 
C 3 311  GLY 311  311  ?   ?   ?   A . n 
C 3 312  ILE 312  312  ?   ?   ?   A . n 
C 3 313  TYR 313  313  ?   ?   ?   A . n 
C 3 314  GLN 314  314  ?   ?   ?   A . n 
C 3 315  THR 315  315  ?   ?   ?   A . n 
C 3 316  SER 316  316  ?   ?   ?   A . n 
C 3 317  ASN 317  317  ?   ?   ?   A . n 
C 3 318  PHE 318  318  ?   ?   ?   A . n 
C 3 319  ARG 319  319  ?   ?   ?   A . n 
C 3 320  VAL 320  320  ?   ?   ?   A . n 
C 3 321  GLN 321  321  ?   ?   ?   A . n 
C 3 322  PRO 322  322  ?   ?   ?   A . n 
C 3 323  THR 323  323  ?   ?   ?   A . n 
C 3 324  GLU 324  324  ?   ?   ?   A . n 
C 3 325  SER 325  325  ?   ?   ?   A . n 
C 3 326  ILE 326  326  ?   ?   ?   A . n 
C 3 327  VAL 327  327  ?   ?   ?   A . n 
C 3 328  ARG 328  328  ?   ?   ?   A . n 
C 3 329  PHE 329  329  ?   ?   ?   A . n 
C 3 330  PRO 330  330  ?   ?   ?   A . n 
C 3 331  ASN 331  331  ?   ?   ?   A . n 
C 3 332  ILE 332  332  ?   ?   ?   A . n 
C 3 333  THR 333  333  ?   ?   ?   A . n 
C 3 334  ASN 334  334  ?   ?   ?   A . n 
C 3 335  LEU 335  335  ?   ?   ?   A . n 
C 3 336  CYS 336  336  ?   ?   ?   A . n 
C 3 337  PRO 337  337  ?   ?   ?   A . n 
C 3 338  PHE 338  338  ?   ?   ?   A . n 
C 3 339  GLY 339  339  ?   ?   ?   A . n 
C 3 340  GLU 340  340  ?   ?   ?   A . n 
C 3 341  VAL 341  341  ?   ?   ?   A . n 
C 3 342  PHE 342  342  ?   ?   ?   A . n 
C 3 343  ASN 343  343  ?   ?   ?   A . n 
C 3 344  ALA 344  344  ?   ?   ?   A . n 
C 3 345  THR 345  345  ?   ?   ?   A . n 
C 3 346  ARG 346  346  ?   ?   ?   A . n 
C 3 347  PHE 347  347  ?   ?   ?   A . n 
C 3 348  ALA 348  348  ?   ?   ?   A . n 
C 3 349  SER 349  349  ?   ?   ?   A . n 
C 3 350  VAL 350  350  ?   ?   ?   A . n 
C 3 351  TYR 351  351  ?   ?   ?   A . n 
C 3 352  ALA 352  352  ?   ?   ?   A . n 
C 3 353  TRP 353  353  ?   ?   ?   A . n 
C 3 354  ASN 354  354  ?   ?   ?   A . n 
C 3 355  ARG 355  355  ?   ?   ?   A . n 
C 3 356  LYS 356  356  ?   ?   ?   A . n 
C 3 357  ARG 357  357  ?   ?   ?   A . n 
C 3 358  ILE 358  358  ?   ?   ?   A . n 
C 3 359  SER 359  359  ?   ?   ?   A . n 
C 3 360  ASN 360  360  ?   ?   ?   A . n 
C 3 361  CYS 361  361  ?   ?   ?   A . n 
C 3 362  VAL 362  362  ?   ?   ?   A . n 
C 3 363  ALA 363  363  ?   ?   ?   A . n 
C 3 364  ASP 364  364  ?   ?   ?   A . n 
C 3 365  TYR 365  365  ?   ?   ?   A . n 
C 3 366  SER 366  366  ?   ?   ?   A . n 
C 3 367  VAL 367  367  ?   ?   ?   A . n 
C 3 368  LEU 368  368  ?   ?   ?   A . n 
C 3 369  TYR 369  369  ?   ?   ?   A . n 
C 3 370  ASN 370  370  ?   ?   ?   A . n 
C 3 371  SER 371  371  ?   ?   ?   A . n 
C 3 372  ALA 372  372  ?   ?   ?   A . n 
C 3 373  SER 373  373  ?   ?   ?   A . n 
C 3 374  PHE 374  374  ?   ?   ?   A . n 
C 3 375  SER 375  375  ?   ?   ?   A . n 
C 3 376  THR 376  376  ?   ?   ?   A . n 
C 3 377  PHE 377  377  ?   ?   ?   A . n 
C 3 378  LYS 378  378  ?   ?   ?   A . n 
C 3 379  CYS 379  379  ?   ?   ?   A . n 
C 3 380  TYR 380  380  ?   ?   ?   A . n 
C 3 381  GLY 381  381  ?   ?   ?   A . n 
C 3 382  VAL 382  382  ?   ?   ?   A . n 
C 3 383  CYS 383  383  ?   ?   ?   A . n 
C 3 384  PRO 384  384  ?   ?   ?   A . n 
C 3 385  THR 385  385  ?   ?   ?   A . n 
C 3 386  LYS 386  386  ?   ?   ?   A . n 
C 3 387  LEU 387  387  ?   ?   ?   A . n 
C 3 388  ASN 388  388  ?   ?   ?   A . n 
C 3 389  ASP 389  389  ?   ?   ?   A . n 
C 3 390  LEU 390  390  ?   ?   ?   A . n 
C 3 391  CYS 391  391  ?   ?   ?   A . n 
C 3 392  PHE 392  392  ?   ?   ?   A . n 
C 3 393  THR 393  393  ?   ?   ?   A . n 
C 3 394  ASN 394  394  ?   ?   ?   A . n 
C 3 395  VAL 395  395  ?   ?   ?   A . n 
C 3 396  TYR 396  396  ?   ?   ?   A . n 
C 3 397  ALA 397  397  ?   ?   ?   A . n 
C 3 398  ASP 398  398  ?   ?   ?   A . n 
C 3 399  SER 399  399  ?   ?   ?   A . n 
C 3 400  PHE 400  400  ?   ?   ?   A . n 
C 3 401  VAL 401  401  ?   ?   ?   A . n 
C 3 402  ILE 402  402  ?   ?   ?   A . n 
C 3 403  ARG 403  403  ?   ?   ?   A . n 
C 3 404  GLY 404  404  ?   ?   ?   A . n 
C 3 405  ASP 405  405  ?   ?   ?   A . n 
C 3 406  GLU 406  406  ?   ?   ?   A . n 
C 3 407  VAL 407  407  ?   ?   ?   A . n 
C 3 408  ARG 408  408  ?   ?   ?   A . n 
C 3 409  GLN 409  409  ?   ?   ?   A . n 
C 3 410  ILE 410  410  ?   ?   ?   A . n 
C 3 411  ALA 411  411  ?   ?   ?   A . n 
C 3 412  PRO 412  412  ?   ?   ?   A . n 
C 3 413  GLY 413  413  ?   ?   ?   A . n 
C 3 414  GLN 414  414  ?   ?   ?   A . n 
C 3 415  THR 415  415  ?   ?   ?   A . n 
C 3 416  GLY 416  416  ?   ?   ?   A . n 
C 3 417  LYS 417  417  ?   ?   ?   A . n 
C 3 418  ILE 418  418  ?   ?   ?   A . n 
C 3 419  ALA 419  419  ?   ?   ?   A . n 
C 3 420  ASP 420  420  ?   ?   ?   A . n 
C 3 421  TYR 421  421  ?   ?   ?   A . n 
C 3 422  ASN 422  422  ?   ?   ?   A . n 
C 3 423  TYR 423  423  ?   ?   ?   A . n 
C 3 424  LYS 424  424  ?   ?   ?   A . n 
C 3 425  LEU 425  425  ?   ?   ?   A . n 
C 3 426  PRO 426  426  ?   ?   ?   A . n 
C 3 427  ASP 427  427  ?   ?   ?   A . n 
C 3 428  ASP 428  428  ?   ?   ?   A . n 
C 3 429  PHE 429  429  ?   ?   ?   A . n 
C 3 430  THR 430  430  ?   ?   ?   A . n 
C 3 431  GLY 431  431  ?   ?   ?   A . n 
C 3 432  CYS 432  432  ?   ?   ?   A . n 
C 3 433  VAL 433  433  ?   ?   ?   A . n 
C 3 434  ILE 434  434  ?   ?   ?   A . n 
C 3 435  ALA 435  435  ?   ?   ?   A . n 
C 3 436  TRP 436  436  ?   ?   ?   A . n 
C 3 437  ASN 437  437  ?   ?   ?   A . n 
C 3 438  SER 438  438  ?   ?   ?   A . n 
C 3 439  ASN 439  439  ?   ?   ?   A . n 
C 3 440  ASN 440  440  ?   ?   ?   A . n 
C 3 441  LEU 441  441  ?   ?   ?   A . n 
C 3 442  ASP 442  442  ?   ?   ?   A . n 
C 3 443  SER 443  443  ?   ?   ?   A . n 
C 3 444  LYS 444  444  ?   ?   ?   A . n 
C 3 445  VAL 445  445  ?   ?   ?   A . n 
C 3 446  GLY 446  446  ?   ?   ?   A . n 
C 3 447  GLY 447  447  ?   ?   ?   A . n 
C 3 448  ASN 448  448  ?   ?   ?   A . n 
C 3 449  TYR 449  449  ?   ?   ?   A . n 
C 3 450  ASN 450  450  ?   ?   ?   A . n 
C 3 451  TYR 451  451  ?   ?   ?   A . n 
C 3 452  ARG 452  452  ?   ?   ?   A . n 
C 3 453  TYR 453  453  ?   ?   ?   A . n 
C 3 454  ARG 454  454  ?   ?   ?   A . n 
C 3 455  LEU 455  455  ?   ?   ?   A . n 
C 3 456  PHE 456  456  ?   ?   ?   A . n 
C 3 457  ARG 457  457  ?   ?   ?   A . n 
C 3 458  LYS 458  458  ?   ?   ?   A . n 
C 3 459  SER 459  459  ?   ?   ?   A . n 
C 3 460  ASN 460  460  ?   ?   ?   A . n 
C 3 461  LEU 461  461  ?   ?   ?   A . n 
C 3 462  LYS 462  462  ?   ?   ?   A . n 
C 3 463  PRO 463  463  ?   ?   ?   A . n 
C 3 464  PHE 464  464  ?   ?   ?   A . n 
C 3 465  GLU 465  465  ?   ?   ?   A . n 
C 3 466  ARG 466  466  ?   ?   ?   A . n 
C 3 467  ASP 467  467  ?   ?   ?   A . n 
C 3 468  ILE 468  468  ?   ?   ?   A . n 
C 3 469  SER 469  469  ?   ?   ?   A . n 
C 3 470  THR 470  470  ?   ?   ?   A . n 
C 3 471  GLU 471  471  ?   ?   ?   A . n 
C 3 472  ILE 472  472  ?   ?   ?   A . n 
C 3 473  TYR 473  473  ?   ?   ?   A . n 
C 3 474  GLN 474  474  ?   ?   ?   A . n 
C 3 475  ALA 475  475  ?   ?   ?   A . n 
C 3 476  GLY 476  476  ?   ?   ?   A . n 
C 3 477  SER 477  477  ?   ?   ?   A . n 
C 3 478  THR 478  478  ?   ?   ?   A . n 
C 3 479  PRO 479  479  ?   ?   ?   A . n 
C 3 480  CYS 480  480  ?   ?   ?   A . n 
C 3 481  ASN 481  481  ?   ?   ?   A . n 
C 3 482  GLY 482  482  ?   ?   ?   A . n 
C 3 483  VAL 483  483  ?   ?   ?   A . n 
C 3 484  GLN 484  484  ?   ?   ?   A . n 
C 3 485  GLY 485  485  ?   ?   ?   A . n 
C 3 486  PHE 486  486  ?   ?   ?   A . n 
C 3 487  ASN 487  487  ?   ?   ?   A . n 
C 3 488  CYS 488  488  ?   ?   ?   A . n 
C 3 489  TYR 489  489  ?   ?   ?   A . n 
C 3 490  PHE 490  490  ?   ?   ?   A . n 
C 3 491  PRO 491  491  ?   ?   ?   A . n 
C 3 492  LEU 492  492  ?   ?   ?   A . n 
C 3 493  GLN 493  493  ?   ?   ?   A . n 
C 3 494  SER 494  494  ?   ?   ?   A . n 
C 3 495  TYR 495  495  ?   ?   ?   A . n 
C 3 496  GLY 496  496  ?   ?   ?   A . n 
C 3 497  PHE 497  497  ?   ?   ?   A . n 
C 3 498  GLN 498  498  ?   ?   ?   A . n 
C 3 499  PRO 499  499  ?   ?   ?   A . n 
C 3 500  THR 500  500  ?   ?   ?   A . n 
C 3 501  ASN 501  501  ?   ?   ?   A . n 
C 3 502  GLY 502  502  ?   ?   ?   A . n 
C 3 503  VAL 503  503  ?   ?   ?   A . n 
C 3 504  GLY 504  504  ?   ?   ?   A . n 
C 3 505  TYR 505  505  ?   ?   ?   A . n 
C 3 506  GLN 506  506  ?   ?   ?   A . n 
C 3 507  PRO 507  507  ?   ?   ?   A . n 
C 3 508  TYR 508  508  ?   ?   ?   A . n 
C 3 509  ARG 509  509  ?   ?   ?   A . n 
C 3 510  VAL 510  510  ?   ?   ?   A . n 
C 3 511  VAL 511  511  ?   ?   ?   A . n 
C 3 512  VAL 512  512  ?   ?   ?   A . n 
C 3 513  LEU 513  513  ?   ?   ?   A . n 
C 3 514  SER 514  514  ?   ?   ?   A . n 
C 3 515  PHE 515  515  ?   ?   ?   A . n 
C 3 516  GLU 516  516  ?   ?   ?   A . n 
C 3 517  LEU 517  517  ?   ?   ?   A . n 
C 3 518  LEU 518  518  ?   ?   ?   A . n 
C 3 519  HIS 519  519  ?   ?   ?   A . n 
C 3 520  ALA 520  520  ?   ?   ?   A . n 
C 3 521  PRO 521  521  ?   ?   ?   A . n 
C 3 522  ALA 522  522  ?   ?   ?   A . n 
C 3 523  THR 523  523  ?   ?   ?   A . n 
C 3 524  VAL 524  524  ?   ?   ?   A . n 
C 3 525  CYS 525  525  ?   ?   ?   A . n 
C 3 526  GLY 526  526  ?   ?   ?   A . n 
C 3 527  PRO 527  527  ?   ?   ?   A . n 
C 3 528  LYS 528  528  ?   ?   ?   A . n 
C 3 529  LYS 529  529  ?   ?   ?   A . n 
C 3 530  SER 530  530  ?   ?   ?   A . n 
C 3 531  THR 531  531  ?   ?   ?   A . n 
C 3 532  ASN 532  532  ?   ?   ?   A . n 
C 3 533  LEU 533  533  ?   ?   ?   A . n 
C 3 534  VAL 534  534  ?   ?   ?   A . n 
C 3 535  LYS 535  535  ?   ?   ?   A . n 
C 3 536  ASN 536  536  ?   ?   ?   A . n 
C 3 537  LYS 537  537  ?   ?   ?   A . n 
C 3 538  CYS 538  538  ?   ?   ?   A . n 
C 3 539  VAL 539  539  ?   ?   ?   A . n 
C 3 540  ASN 540  540  ?   ?   ?   A . n 
C 3 541  PHE 541  541  ?   ?   ?   A . n 
C 3 542  ASN 542  542  ?   ?   ?   A . n 
C 3 543  PHE 543  543  ?   ?   ?   A . n 
C 3 544  ASN 544  544  ?   ?   ?   A . n 
C 3 545  GLY 545  545  ?   ?   ?   A . n 
C 3 546  LEU 546  546  ?   ?   ?   A . n 
C 3 547  THR 547  547  ?   ?   ?   A . n 
C 3 548  GLY 548  548  ?   ?   ?   A . n 
C 3 549  THR 549  549  ?   ?   ?   A . n 
C 3 550  GLY 550  550  ?   ?   ?   A . n 
C 3 551  VAL 551  551  ?   ?   ?   A . n 
C 3 552  LEU 552  552  ?   ?   ?   A . n 
C 3 553  THR 553  553  ?   ?   ?   A . n 
C 3 554  GLU 554  554  ?   ?   ?   A . n 
C 3 555  SER 555  555  ?   ?   ?   A . n 
C 3 556  ASN 556  556  ?   ?   ?   A . n 
C 3 557  LYS 557  557  ?   ?   ?   A . n 
C 3 558  LYS 558  558  ?   ?   ?   A . n 
C 3 559  PHE 559  559  ?   ?   ?   A . n 
C 3 560  LEU 560  560  ?   ?   ?   A . n 
C 3 561  PRO 561  561  ?   ?   ?   A . n 
C 3 562  PHE 562  562  ?   ?   ?   A . n 
C 3 563  GLN 563  563  ?   ?   ?   A . n 
C 3 564  GLN 564  564  ?   ?   ?   A . n 
C 3 565  PHE 565  565  ?   ?   ?   A . n 
C 3 566  GLY 566  566  ?   ?   ?   A . n 
C 3 567  ARG 567  567  ?   ?   ?   A . n 
C 3 568  ASP 568  568  ?   ?   ?   A . n 
C 3 569  ILE 569  569  ?   ?   ?   A . n 
C 3 570  ALA 570  570  ?   ?   ?   A . n 
C 3 571  ASP 571  571  ?   ?   ?   A . n 
C 3 572  THR 572  572  ?   ?   ?   A . n 
C 3 573  THR 573  573  ?   ?   ?   A . n 
C 3 574  ASP 574  574  ?   ?   ?   A . n 
C 3 575  ALA 575  575  ?   ?   ?   A . n 
C 3 576  VAL 576  576  ?   ?   ?   A . n 
C 3 577  ARG 577  577  ?   ?   ?   A . n 
C 3 578  ASP 578  578  ?   ?   ?   A . n 
C 3 579  PRO 579  579  ?   ?   ?   A . n 
C 3 580  GLN 580  580  ?   ?   ?   A . n 
C 3 581  THR 581  581  ?   ?   ?   A . n 
C 3 582  LEU 582  582  ?   ?   ?   A . n 
C 3 583  GLU 583  583  ?   ?   ?   A . n 
C 3 584  ILE 584  584  ?   ?   ?   A . n 
C 3 585  LEU 585  585  ?   ?   ?   A . n 
C 3 586  ASP 586  586  ?   ?   ?   A . n 
C 3 587  ILE 587  587  ?   ?   ?   A . n 
C 3 588  THR 588  588  ?   ?   ?   A . n 
C 3 589  PRO 589  589  ?   ?   ?   A . n 
C 3 590  CYS 590  590  ?   ?   ?   A . n 
C 3 591  SER 591  591  ?   ?   ?   A . n 
C 3 592  PHE 592  592  ?   ?   ?   A . n 
C 3 593  GLY 593  593  ?   ?   ?   A . n 
C 3 594  GLY 594  594  ?   ?   ?   A . n 
C 3 595  VAL 595  595  ?   ?   ?   A . n 
C 3 596  SER 596  596  ?   ?   ?   A . n 
C 3 597  VAL 597  597  ?   ?   ?   A . n 
C 3 598  ILE 598  598  ?   ?   ?   A . n 
C 3 599  THR 599  599  ?   ?   ?   A . n 
C 3 600  PRO 600  600  ?   ?   ?   A . n 
C 3 601  GLY 601  601  ?   ?   ?   A . n 
C 3 602  THR 602  602  ?   ?   ?   A . n 
C 3 603  ASN 603  603  ?   ?   ?   A . n 
C 3 604  THR 604  604  ?   ?   ?   A . n 
C 3 605  SER 605  605  ?   ?   ?   A . n 
C 3 606  ASN 606  606  ?   ?   ?   A . n 
C 3 607  GLN 607  607  ?   ?   ?   A . n 
C 3 608  VAL 608  608  ?   ?   ?   A . n 
C 3 609  ALA 609  609  ?   ?   ?   A . n 
C 3 610  VAL 610  610  ?   ?   ?   A . n 
C 3 611  LEU 611  611  ?   ?   ?   A . n 
C 3 612  TYR 612  612  ?   ?   ?   A . n 
C 3 613  GLN 613  613  ?   ?   ?   A . n 
C 3 614  GLY 614  614  ?   ?   ?   A . n 
C 3 615  VAL 615  615  ?   ?   ?   A . n 
C 3 616  ASN 616  616  ?   ?   ?   A . n 
C 3 617  CYS 617  617  ?   ?   ?   A . n 
C 3 618  THR 618  618  ?   ?   ?   A . n 
C 3 619  GLU 619  619  ?   ?   ?   A . n 
C 3 620  VAL 620  620  ?   ?   ?   A . n 
C 3 621  PRO 621  621  ?   ?   ?   A . n 
C 3 622  VAL 622  622  ?   ?   ?   A . n 
C 3 623  ALA 623  623  ?   ?   ?   A . n 
C 3 624  ILE 624  624  ?   ?   ?   A . n 
C 3 625  HIS 625  625  ?   ?   ?   A . n 
C 3 626  ALA 626  626  ?   ?   ?   A . n 
C 3 627  ASP 627  627  ?   ?   ?   A . n 
C 3 628  GLN 628  628  ?   ?   ?   A . n 
C 3 629  LEU 629  629  ?   ?   ?   A . n 
C 3 630  THR 630  630  ?   ?   ?   A . n 
C 3 631  PRO 631  631  ?   ?   ?   A . n 
C 3 632  THR 632  632  ?   ?   ?   A . n 
C 3 633  TRP 633  633  ?   ?   ?   A . n 
C 3 634  ARG 634  634  ?   ?   ?   A . n 
C 3 635  VAL 635  635  ?   ?   ?   A . n 
C 3 636  TYR 636  636  ?   ?   ?   A . n 
C 3 637  SER 637  637  ?   ?   ?   A . n 
C 3 638  THR 638  638  ?   ?   ?   A . n 
C 3 639  GLY 639  639  ?   ?   ?   A . n 
C 3 640  SER 640  640  ?   ?   ?   A . n 
C 3 641  ASN 641  641  ?   ?   ?   A . n 
C 3 642  VAL 642  642  ?   ?   ?   A . n 
C 3 643  PHE 643  643  ?   ?   ?   A . n 
C 3 644  GLN 644  644  ?   ?   ?   A . n 
C 3 645  THR 645  645  ?   ?   ?   A . n 
C 3 646  ARG 646  646  ?   ?   ?   A . n 
C 3 647  ALA 647  647  ?   ?   ?   A . n 
C 3 648  GLY 648  648  ?   ?   ?   A . n 
C 3 649  CYS 649  649  ?   ?   ?   A . n 
C 3 650  LEU 650  650  ?   ?   ?   A . n 
C 3 651  ILE 651  651  ?   ?   ?   A . n 
C 3 652  GLY 652  652  ?   ?   ?   A . n 
C 3 653  ALA 653  653  ?   ?   ?   A . n 
C 3 654  GLU 654  654  ?   ?   ?   A . n 
C 3 655  HIS 655  655  ?   ?   ?   A . n 
C 3 656  VAL 656  656  ?   ?   ?   A . n 
C 3 657  ASN 657  657  ?   ?   ?   A . n 
C 3 658  ASN 658  658  ?   ?   ?   A . n 
C 3 659  SER 659  659  ?   ?   ?   A . n 
C 3 660  TYR 660  660  ?   ?   ?   A . n 
C 3 661  GLU 661  661  ?   ?   ?   A . n 
C 3 662  CYS 662  662  ?   ?   ?   A . n 
C 3 663  ASP 663  663  ?   ?   ?   A . n 
C 3 664  ILE 664  664  ?   ?   ?   A . n 
C 3 665  PRO 665  665  ?   ?   ?   A . n 
C 3 666  ILE 666  666  ?   ?   ?   A . n 
C 3 667  GLY 667  667  ?   ?   ?   A . n 
C 3 668  ALA 668  668  ?   ?   ?   A . n 
C 3 669  GLY 669  669  ?   ?   ?   A . n 
C 3 670  ILE 670  670  ?   ?   ?   A . n 
C 3 671  CYS 671  671  ?   ?   ?   A . n 
C 3 672  ALA 672  672  ?   ?   ?   A . n 
C 3 673  SER 673  673  ?   ?   ?   A . n 
C 3 674  TYR 674  674  ?   ?   ?   A . n 
C 3 675  GLN 675  675  ?   ?   ?   A . n 
C 3 676  THR 676  676  ?   ?   ?   A . n 
C 3 677  GLN 677  677  ?   ?   ?   A . n 
C 3 678  THR 678  678  ?   ?   ?   A . n 
C 3 679  ASN 679  679  ?   ?   ?   A . n 
C 3 680  SER 680  680  ?   ?   ?   A . n 
C 3 681  ARG 681  681  ?   ?   ?   A . n 
C 3 682  ARG 682  682  ?   ?   ?   A . n 
C 3 683  ARG 683  683  ?   ?   ?   A . n 
C 3 684  ALA 684  684  ?   ?   ?   A . n 
C 3 685  ARG 685  685  ?   ?   ?   A . n 
C 3 686  SER 686  686  ?   ?   ?   A . n 
C 3 687  VAL 687  687  ?   ?   ?   A . n 
C 3 688  ALA 688  688  ?   ?   ?   A . n 
C 3 689  SER 689  689  ?   ?   ?   A . n 
C 3 690  GLN 690  690  ?   ?   ?   A . n 
C 3 691  SER 691  691  ?   ?   ?   A . n 
C 3 692  ILE 692  692  ?   ?   ?   A . n 
C 3 693  ILE 693  693  ?   ?   ?   A . n 
C 3 694  ALA 694  694  ?   ?   ?   A . n 
C 3 695  TYR 695  695  ?   ?   ?   A . n 
C 3 696  THR 696  696  ?   ?   ?   A . n 
C 3 697  MET 697  697  ?   ?   ?   A . n 
C 3 698  SER 698  698  ?   ?   ?   A . n 
C 3 699  LEU 699  699  ?   ?   ?   A . n 
C 3 700  GLY 700  700  ?   ?   ?   A . n 
C 3 701  ALA 701  701  ?   ?   ?   A . n 
C 3 702  GLU 702  702  ?   ?   ?   A . n 
C 3 703  ASN 703  703  ?   ?   ?   A . n 
C 3 704  SER 704  704  ?   ?   ?   A . n 
C 3 705  VAL 705  705  ?   ?   ?   A . n 
C 3 706  ALA 706  706  ?   ?   ?   A . n 
C 3 707  TYR 707  707  ?   ?   ?   A . n 
C 3 708  SER 708  708  ?   ?   ?   A . n 
C 3 709  ASN 709  709  ?   ?   ?   A . n 
C 3 710  ASN 710  710  ?   ?   ?   A . n 
C 3 711  SER 711  711  ?   ?   ?   A . n 
C 3 712  ILE 712  712  ?   ?   ?   A . n 
C 3 713  ALA 713  713  ?   ?   ?   A . n 
C 3 714  ILE 714  714  ?   ?   ?   A . n 
C 3 715  PRO 715  715  ?   ?   ?   A . n 
C 3 716  THR 716  716  ?   ?   ?   A . n 
C 3 717  ASN 717  717  ?   ?   ?   A . n 
C 3 718  PHE 718  718  ?   ?   ?   A . n 
C 3 719  THR 719  719  ?   ?   ?   A . n 
C 3 720  ILE 720  720  ?   ?   ?   A . n 
C 3 721  SER 721  721  ?   ?   ?   A . n 
C 3 722  VAL 722  722  ?   ?   ?   A . n 
C 3 723  THR 723  723  ?   ?   ?   A . n 
C 3 724  THR 724  724  ?   ?   ?   A . n 
C 3 725  GLU 725  725  ?   ?   ?   A . n 
C 3 726  ILE 726  726  ?   ?   ?   A . n 
C 3 727  LEU 727  727  ?   ?   ?   A . n 
C 3 728  PRO 728  728  ?   ?   ?   A . n 
C 3 729  VAL 729  729  ?   ?   ?   A . n 
C 3 730  SER 730  730  ?   ?   ?   A . n 
C 3 731  MET 731  731  ?   ?   ?   A . n 
C 3 732  THR 732  732  ?   ?   ?   A . n 
C 3 733  LYS 733  733  ?   ?   ?   A . n 
C 3 734  THR 734  734  ?   ?   ?   A . n 
C 3 735  SER 735  735  ?   ?   ?   A . n 
C 3 736  VAL 736  736  ?   ?   ?   A . n 
C 3 737  ASP 737  737  ?   ?   ?   A . n 
C 3 738  CYS 738  738  ?   ?   ?   A . n 
C 3 739  THR 739  739  ?   ?   ?   A . n 
C 3 740  MET 740  740  ?   ?   ?   A . n 
C 3 741  TYR 741  741  ?   ?   ?   A . n 
C 3 742  ILE 742  742  ?   ?   ?   A . n 
C 3 743  CYS 743  743  ?   ?   ?   A . n 
C 3 744  GLY 744  744  ?   ?   ?   A . n 
C 3 745  ASP 745  745  ?   ?   ?   A . n 
C 3 746  SER 746  746  ?   ?   ?   A . n 
C 3 747  THR 747  747  ?   ?   ?   A . n 
C 3 748  GLU 748  748  ?   ?   ?   A . n 
C 3 749  CYS 749  749  ?   ?   ?   A . n 
C 3 750  SER 750  750  ?   ?   ?   A . n 
C 3 751  ASN 751  751  ?   ?   ?   A . n 
C 3 752  LEU 752  752  ?   ?   ?   A . n 
C 3 753  LEU 753  753  ?   ?   ?   A . n 
C 3 754  LEU 754  754  ?   ?   ?   A . n 
C 3 755  GLN 755  755  ?   ?   ?   A . n 
C 3 756  TYR 756  756  ?   ?   ?   A . n 
C 3 757  GLY 757  757  ?   ?   ?   A . n 
C 3 758  SER 758  758  ?   ?   ?   A . n 
C 3 759  PHE 759  759  ?   ?   ?   A . n 
C 3 760  CYS 760  760  ?   ?   ?   A . n 
C 3 761  THR 761  761  ?   ?   ?   A . n 
C 3 762  GLN 762  762  ?   ?   ?   A . n 
C 3 763  LEU 763  763  ?   ?   ?   A . n 
C 3 764  ASN 764  764  ?   ?   ?   A . n 
C 3 765  ARG 765  765  ?   ?   ?   A . n 
C 3 766  ALA 766  766  ?   ?   ?   A . n 
C 3 767  LEU 767  767  ?   ?   ?   A . n 
C 3 768  THR 768  768  ?   ?   ?   A . n 
C 3 769  GLY 769  769  ?   ?   ?   A . n 
C 3 770  ILE 770  770  ?   ?   ?   A . n 
C 3 771  ALA 771  771  ?   ?   ?   A . n 
C 3 772  VAL 772  772  ?   ?   ?   A . n 
C 3 773  GLU 773  773  ?   ?   ?   A . n 
C 3 774  GLN 774  774  ?   ?   ?   A . n 
C 3 775  ASP 775  775  ?   ?   ?   A . n 
C 3 776  LYS 776  776  ?   ?   ?   A . n 
C 3 777  ASN 777  777  ?   ?   ?   A . n 
C 3 778  THR 778  778  ?   ?   ?   A . n 
C 3 779  GLN 779  779  ?   ?   ?   A . n 
C 3 780  GLU 780  780  ?   ?   ?   A . n 
C 3 781  VAL 781  781  ?   ?   ?   A . n 
C 3 782  PHE 782  782  ?   ?   ?   A . n 
C 3 783  ALA 783  783  ?   ?   ?   A . n 
C 3 784  GLN 784  784  ?   ?   ?   A . n 
C 3 785  VAL 785  785  ?   ?   ?   A . n 
C 3 786  LYS 786  786  ?   ?   ?   A . n 
C 3 787  GLN 787  787  ?   ?   ?   A . n 
C 3 788  ILE 788  788  ?   ?   ?   A . n 
C 3 789  TYR 789  789  ?   ?   ?   A . n 
C 3 790  LYS 790  790  ?   ?   ?   A . n 
C 3 791  THR 791  791  ?   ?   ?   A . n 
C 3 792  PRO 792  792  ?   ?   ?   A . n 
C 3 793  PRO 793  793  ?   ?   ?   A . n 
C 3 794  ILE 794  794  ?   ?   ?   A . n 
C 3 795  LYS 795  795  ?   ?   ?   A . n 
C 3 796  ASP 796  796  ?   ?   ?   A . n 
C 3 797  PHE 797  797  ?   ?   ?   A . n 
C 3 798  GLY 798  798  ?   ?   ?   A . n 
C 3 799  GLY 799  799  ?   ?   ?   A . n 
C 3 800  PHE 800  800  ?   ?   ?   A . n 
C 3 801  ASN 801  801  ?   ?   ?   A . n 
C 3 802  PHE 802  802  ?   ?   ?   A . n 
C 3 803  SER 803  803  ?   ?   ?   A . n 
C 3 804  GLN 804  804  ?   ?   ?   A . n 
C 3 805  ILE 805  805  ?   ?   ?   A . n 
C 3 806  LEU 806  806  ?   ?   ?   A . n 
C 3 807  PRO 807  807  ?   ?   ?   A . n 
C 3 808  ASP 808  808  ?   ?   ?   A . n 
C 3 809  PRO 809  809  ?   ?   ?   A . n 
C 3 810  SER 810  810  ?   ?   ?   A . n 
C 3 811  LYS 811  811  ?   ?   ?   A . n 
C 3 812  PRO 812  812  ?   ?   ?   A . n 
C 3 813  SER 813  813  ?   ?   ?   A . n 
C 3 814  LYS 814  814  ?   ?   ?   A . n 
C 3 815  ARG 815  815  ?   ?   ?   A . n 
C 3 816  SER 816  816  ?   ?   ?   A . n 
C 3 817  PRO 817  817  ?   ?   ?   A . n 
C 3 818  ILE 818  818  ?   ?   ?   A . n 
C 3 819  GLU 819  819  ?   ?   ?   A . n 
C 3 820  ASP 820  820  ?   ?   ?   A . n 
C 3 821  LEU 821  821  ?   ?   ?   A . n 
C 3 822  LEU 822  822  ?   ?   ?   A . n 
C 3 823  PHE 823  823  ?   ?   ?   A . n 
C 3 824  ASN 824  824  ?   ?   ?   A . n 
C 3 825  LYS 825  825  ?   ?   ?   A . n 
C 3 826  VAL 826  826  ?   ?   ?   A . n 
C 3 827  THR 827  827  ?   ?   ?   A . n 
C 3 828  LEU 828  828  ?   ?   ?   A . n 
C 3 829  ALA 829  829  ?   ?   ?   A . n 
C 3 830  ASP 830  830  ?   ?   ?   A . n 
C 3 831  ALA 831  831  ?   ?   ?   A . n 
C 3 832  GLY 832  832  ?   ?   ?   A . n 
C 3 833  PHE 833  833  ?   ?   ?   A . n 
C 3 834  ILE 834  834  ?   ?   ?   A . n 
C 3 835  LYS 835  835  ?   ?   ?   A . n 
C 3 836  GLN 836  836  ?   ?   ?   A . n 
C 3 837  TYR 837  837  ?   ?   ?   A . n 
C 3 838  GLY 838  838  ?   ?   ?   A . n 
C 3 839  ASP 839  839  ?   ?   ?   A . n 
C 3 840  CYS 840  840  ?   ?   ?   A . n 
C 3 841  LEU 841  841  ?   ?   ?   A . n 
C 3 842  GLY 842  842  ?   ?   ?   A . n 
C 3 843  ASP 843  843  ?   ?   ?   A . n 
C 3 844  ILE 844  844  ?   ?   ?   A . n 
C 3 845  ALA 845  845  ?   ?   ?   A . n 
C 3 846  ALA 846  846  ?   ?   ?   A . n 
C 3 847  ARG 847  847  ?   ?   ?   A . n 
C 3 848  ASP 848  848  ?   ?   ?   A . n 
C 3 849  LEU 849  849  ?   ?   ?   A . n 
C 3 850  ILE 850  850  ?   ?   ?   A . n 
C 3 851  CYS 851  851  ?   ?   ?   A . n 
C 3 852  ALA 852  852  ?   ?   ?   A . n 
C 3 853  GLN 853  853  ?   ?   ?   A . n 
C 3 854  LYS 854  854  ?   ?   ?   A . n 
C 3 855  PHE 855  855  ?   ?   ?   A . n 
C 3 856  ASN 856  856  ?   ?   ?   A . n 
C 3 857  GLY 857  857  ?   ?   ?   A . n 
C 3 858  LEU 858  858  ?   ?   ?   A . n 
C 3 859  THR 859  859  ?   ?   ?   A . n 
C 3 860  VAL 860  860  ?   ?   ?   A . n 
C 3 861  LEU 861  861  ?   ?   ?   A . n 
C 3 862  PRO 862  862  ?   ?   ?   A . n 
C 3 863  PRO 863  863  ?   ?   ?   A . n 
C 3 864  LEU 864  864  ?   ?   ?   A . n 
C 3 865  LEU 865  865  ?   ?   ?   A . n 
C 3 866  THR 866  866  ?   ?   ?   A . n 
C 3 867  ASP 867  867  ?   ?   ?   A . n 
C 3 868  GLU 868  868  ?   ?   ?   A . n 
C 3 869  MET 869  869  ?   ?   ?   A . n 
C 3 870  ILE 870  870  ?   ?   ?   A . n 
C 3 871  ALA 871  871  ?   ?   ?   A . n 
C 3 872  GLN 872  872  ?   ?   ?   A . n 
C 3 873  TYR 873  873  ?   ?   ?   A . n 
C 3 874  THR 874  874  ?   ?   ?   A . n 
C 3 875  SER 875  875  ?   ?   ?   A . n 
C 3 876  ALA 876  876  ?   ?   ?   A . n 
C 3 877  LEU 877  877  ?   ?   ?   A . n 
C 3 878  LEU 878  878  ?   ?   ?   A . n 
C 3 879  ALA 879  879  ?   ?   ?   A . n 
C 3 880  GLY 880  880  ?   ?   ?   A . n 
C 3 881  THR 881  881  ?   ?   ?   A . n 
C 3 882  ILE 882  882  ?   ?   ?   A . n 
C 3 883  THR 883  883  ?   ?   ?   A . n 
C 3 884  SER 884  884  ?   ?   ?   A . n 
C 3 885  GLY 885  885  ?   ?   ?   A . n 
C 3 886  TRP 886  886  ?   ?   ?   A . n 
C 3 887  THR 887  887  ?   ?   ?   A . n 
C 3 888  PHE 888  888  ?   ?   ?   A . n 
C 3 889  GLY 889  889  ?   ?   ?   A . n 
C 3 890  ALA 890  890  ?   ?   ?   A . n 
C 3 891  GLY 891  891  ?   ?   ?   A . n 
C 3 892  PRO 892  892  ?   ?   ?   A . n 
C 3 893  ALA 893  893  ?   ?   ?   A . n 
C 3 894  LEU 894  894  ?   ?   ?   A . n 
C 3 895  GLN 895  895  ?   ?   ?   A . n 
C 3 896  ILE 896  896  ?   ?   ?   A . n 
C 3 897  PRO 897  897  ?   ?   ?   A . n 
C 3 898  PHE 898  898  ?   ?   ?   A . n 
C 3 899  PRO 899  899  ?   ?   ?   A . n 
C 3 900  MET 900  900  ?   ?   ?   A . n 
C 3 901  GLN 901  901  ?   ?   ?   A . n 
C 3 902  MET 902  902  ?   ?   ?   A . n 
C 3 903  ALA 903  903  ?   ?   ?   A . n 
C 3 904  TYR 904  904  ?   ?   ?   A . n 
C 3 905  ARG 905  905  ?   ?   ?   A . n 
C 3 906  PHE 906  906  ?   ?   ?   A . n 
C 3 907  ASN 907  907  ?   ?   ?   A . n 
C 3 908  GLY 908  908  ?   ?   ?   A . n 
C 3 909  ILE 909  909  ?   ?   ?   A . n 
C 3 910  GLY 910  910  ?   ?   ?   A . n 
C 3 911  VAL 911  911  ?   ?   ?   A . n 
C 3 912  THR 912  912  ?   ?   ?   A . n 
C 3 913  GLN 913  913  ?   ?   ?   A . n 
C 3 914  ASN 914  914  ?   ?   ?   A . n 
C 3 915  VAL 915  915  ?   ?   ?   A . n 
C 3 916  LEU 916  916  ?   ?   ?   A . n 
C 3 917  TYR 917  917  ?   ?   ?   A . n 
C 3 918  GLU 918  918  ?   ?   ?   A . n 
C 3 919  ASN 919  919  ?   ?   ?   A . n 
C 3 920  GLN 920  920  ?   ?   ?   A . n 
C 3 921  LYS 921  921  ?   ?   ?   A . n 
C 3 922  LEU 922  922  ?   ?   ?   A . n 
C 3 923  ILE 923  923  ?   ?   ?   A . n 
C 3 924  ALA 924  924  ?   ?   ?   A . n 
C 3 925  ASN 925  925  ?   ?   ?   A . n 
C 3 926  GLN 926  926  ?   ?   ?   A . n 
C 3 927  PHE 927  927  ?   ?   ?   A . n 
C 3 928  ASN 928  928  ?   ?   ?   A . n 
C 3 929  SER 929  929  ?   ?   ?   A . n 
C 3 930  ALA 930  930  ?   ?   ?   A . n 
C 3 931  ILE 931  931  ?   ?   ?   A . n 
C 3 932  GLY 932  932  ?   ?   ?   A . n 
C 3 933  LYS 933  933  ?   ?   ?   A . n 
C 3 934  ILE 934  934  ?   ?   ?   A . n 
C 3 935  GLN 935  935  ?   ?   ?   A . n 
C 3 936  ASP 936  936  ?   ?   ?   A . n 
C 3 937  SER 937  937  ?   ?   ?   A . n 
C 3 938  LEU 938  938  ?   ?   ?   A . n 
C 3 939  SER 939  939  ?   ?   ?   A . n 
C 3 940  SER 940  940  ?   ?   ?   A . n 
C 3 941  THR 941  941  ?   ?   ?   A . n 
C 3 942  PRO 942  942  ?   ?   ?   A . n 
C 3 943  SER 943  943  ?   ?   ?   A . n 
C 3 944  ALA 944  944  ?   ?   ?   A . n 
C 3 945  LEU 945  945  ?   ?   ?   A . n 
C 3 946  GLY 946  946  ?   ?   ?   A . n 
C 3 947  LYS 947  947  ?   ?   ?   A . n 
C 3 948  LEU 948  948  ?   ?   ?   A . n 
C 3 949  GLN 949  949  ?   ?   ?   A . n 
C 3 950  ASP 950  950  ?   ?   ?   A . n 
C 3 951  VAL 951  951  ?   ?   ?   A . n 
C 3 952  VAL 952  952  ?   ?   ?   A . n 
C 3 953  ASN 953  953  ?   ?   ?   A . n 
C 3 954  GLN 954  954  ?   ?   ?   A . n 
C 3 955  ASN 955  955  ?   ?   ?   A . n 
C 3 956  ALA 956  956  ?   ?   ?   A . n 
C 3 957  GLN 957  957  ?   ?   ?   A . n 
C 3 958  ALA 958  958  ?   ?   ?   A . n 
C 3 959  LEU 959  959  ?   ?   ?   A . n 
C 3 960  ASN 960  960  ?   ?   ?   A . n 
C 3 961  THR 961  961  ?   ?   ?   A . n 
C 3 962  LEU 962  962  ?   ?   ?   A . n 
C 3 963  VAL 963  963  ?   ?   ?   A . n 
C 3 964  LYS 964  964  ?   ?   ?   A . n 
C 3 965  GLN 965  965  ?   ?   ?   A . n 
C 3 966  LEU 966  966  ?   ?   ?   A . n 
C 3 967  SER 967  967  ?   ?   ?   A . n 
C 3 968  SER 968  968  ?   ?   ?   A . n 
C 3 969  ASN 969  969  ?   ?   ?   A . n 
C 3 970  PHE 970  970  ?   ?   ?   A . n 
C 3 971  GLY 971  971  ?   ?   ?   A . n 
C 3 972  ALA 972  972  ?   ?   ?   A . n 
C 3 973  ILE 973  973  ?   ?   ?   A . n 
C 3 974  SER 974  974  ?   ?   ?   A . n 
C 3 975  SER 975  975  ?   ?   ?   A . n 
C 3 976  VAL 976  976  ?   ?   ?   A . n 
C 3 977  LEU 977  977  ?   ?   ?   A . n 
C 3 978  ASN 978  978  ?   ?   ?   A . n 
C 3 979  ASP 979  979  ?   ?   ?   A . n 
C 3 980  ILE 980  980  ?   ?   ?   A . n 
C 3 981  LEU 981  981  ?   ?   ?   A . n 
C 3 982  SER 982  982  ?   ?   ?   A . n 
C 3 983  ARG 983  983  ?   ?   ?   A . n 
C 3 984  LEU 984  984  ?   ?   ?   A . n 
C 3 985  CYS 985  985  ?   ?   ?   A . n 
C 3 986  PRO 986  986  ?   ?   ?   A . n 
C 3 987  PRO 987  987  ?   ?   ?   A . n 
C 3 988  GLU 988  988  ?   ?   ?   A . n 
C 3 989  ALA 989  989  ?   ?   ?   A . n 
C 3 990  GLU 990  990  ?   ?   ?   A . n 
C 3 991  VAL 991  991  ?   ?   ?   A . n 
C 3 992  GLN 992  992  ?   ?   ?   A . n 
C 3 993  ILE 993  993  ?   ?   ?   A . n 
C 3 994  ASP 994  994  ?   ?   ?   A . n 
C 3 995  ARG 995  995  ?   ?   ?   A . n 
C 3 996  LEU 996  996  ?   ?   ?   A . n 
C 3 997  ILE 997  997  ?   ?   ?   A . n 
C 3 998  THR 998  998  ?   ?   ?   A . n 
C 3 999  GLY 999  999  ?   ?   ?   A . n 
C 3 1000 ARG 1000 1000 ?   ?   ?   A . n 
C 3 1001 LEU 1001 1001 ?   ?   ?   A . n 
C 3 1002 GLN 1002 1002 ?   ?   ?   A . n 
C 3 1003 SER 1003 1003 ?   ?   ?   A . n 
C 3 1004 LEU 1004 1004 ?   ?   ?   A . n 
C 3 1005 GLN 1005 1005 ?   ?   ?   A . n 
C 3 1006 THR 1006 1006 ?   ?   ?   A . n 
C 3 1007 TYR 1007 1007 ?   ?   ?   A . n 
C 3 1008 VAL 1008 1008 ?   ?   ?   A . n 
C 3 1009 THR 1009 1009 ?   ?   ?   A . n 
C 3 1010 GLN 1010 1010 ?   ?   ?   A . n 
C 3 1011 GLN 1011 1011 ?   ?   ?   A . n 
C 3 1012 LEU 1012 1012 ?   ?   ?   A . n 
C 3 1013 ILE 1013 1013 ?   ?   ?   A . n 
C 3 1014 ARG 1014 1014 ?   ?   ?   A . n 
C 3 1015 ALA 1015 1015 ?   ?   ?   A . n 
C 3 1016 ALA 1016 1016 ?   ?   ?   A . n 
C 3 1017 GLU 1017 1017 ?   ?   ?   A . n 
C 3 1018 ILE 1018 1018 ?   ?   ?   A . n 
C 3 1019 ARG 1019 1019 ?   ?   ?   A . n 
C 3 1020 ALA 1020 1020 ?   ?   ?   A . n 
C 3 1021 SER 1021 1021 ?   ?   ?   A . n 
C 3 1022 ALA 1022 1022 ?   ?   ?   A . n 
C 3 1023 ASN 1023 1023 ?   ?   ?   A . n 
C 3 1024 LEU 1024 1024 ?   ?   ?   A . n 
C 3 1025 ALA 1025 1025 ?   ?   ?   A . n 
C 3 1026 ALA 1026 1026 ?   ?   ?   A . n 
C 3 1027 THR 1027 1027 ?   ?   ?   A . n 
C 3 1028 LYS 1028 1028 ?   ?   ?   A . n 
C 3 1029 MET 1029 1029 ?   ?   ?   A . n 
C 3 1030 SER 1030 1030 ?   ?   ?   A . n 
C 3 1031 GLU 1031 1031 ?   ?   ?   A . n 
C 3 1032 CYS 1032 1032 ?   ?   ?   A . n 
C 3 1033 VAL 1033 1033 ?   ?   ?   A . n 
C 3 1034 LEU 1034 1034 ?   ?   ?   A . n 
C 3 1035 GLY 1035 1035 ?   ?   ?   A . n 
C 3 1036 GLN 1036 1036 ?   ?   ?   A . n 
C 3 1037 SER 1037 1037 ?   ?   ?   A . n 
C 3 1038 LYS 1038 1038 ?   ?   ?   A . n 
C 3 1039 ARG 1039 1039 ?   ?   ?   A . n 
C 3 1040 VAL 1040 1040 ?   ?   ?   A . n 
C 3 1041 ASP 1041 1041 ?   ?   ?   A . n 
C 3 1042 PHE 1042 1042 ?   ?   ?   A . n 
C 3 1043 CYS 1043 1043 ?   ?   ?   A . n 
C 3 1044 GLY 1044 1044 ?   ?   ?   A . n 
C 3 1045 LYS 1045 1045 ?   ?   ?   A . n 
C 3 1046 GLY 1046 1046 ?   ?   ?   A . n 
C 3 1047 TYR 1047 1047 ?   ?   ?   A . n 
C 3 1048 HIS 1048 1048 ?   ?   ?   A . n 
C 3 1049 LEU 1049 1049 ?   ?   ?   A . n 
C 3 1050 MET 1050 1050 ?   ?   ?   A . n 
C 3 1051 SER 1051 1051 ?   ?   ?   A . n 
C 3 1052 PHE 1052 1052 ?   ?   ?   A . n 
C 3 1053 PRO 1053 1053 ?   ?   ?   A . n 
C 3 1054 GLN 1054 1054 ?   ?   ?   A . n 
C 3 1055 SER 1055 1055 ?   ?   ?   A . n 
C 3 1056 ALA 1056 1056 ?   ?   ?   A . n 
C 3 1057 PRO 1057 1057 ?   ?   ?   A . n 
C 3 1058 HIS 1058 1058 ?   ?   ?   A . n 
C 3 1059 GLY 1059 1059 ?   ?   ?   A . n 
C 3 1060 VAL 1060 1060 ?   ?   ?   A . n 
C 3 1061 VAL 1061 1061 ?   ?   ?   A . n 
C 3 1062 PHE 1062 1062 ?   ?   ?   A . n 
C 3 1063 LEU 1063 1063 ?   ?   ?   A . n 
C 3 1064 HIS 1064 1064 ?   ?   ?   A . n 
C 3 1065 VAL 1065 1065 ?   ?   ?   A . n 
C 3 1066 THR 1066 1066 ?   ?   ?   A . n 
C 3 1067 TYR 1067 1067 ?   ?   ?   A . n 
C 3 1068 VAL 1068 1068 ?   ?   ?   A . n 
C 3 1069 PRO 1069 1069 ?   ?   ?   A . n 
C 3 1070 ALA 1070 1070 ?   ?   ?   A . n 
C 3 1071 HIS 1071 1071 ?   ?   ?   A . n 
C 3 1072 GLU 1072 1072 ?   ?   ?   A . n 
C 3 1073 LYS 1073 1073 ?   ?   ?   A . n 
C 3 1074 ASN 1074 1074 ?   ?   ?   A . n 
C 3 1075 PHE 1075 1075 ?   ?   ?   A . n 
C 3 1076 THR 1076 1076 ?   ?   ?   A . n 
C 3 1077 THR 1077 1077 ?   ?   ?   A . n 
C 3 1078 ALA 1078 1078 ?   ?   ?   A . n 
C 3 1079 PRO 1079 1079 ?   ?   ?   A . n 
C 3 1080 ALA 1080 1080 ?   ?   ?   A . n 
C 3 1081 ILE 1081 1081 ?   ?   ?   A . n 
C 3 1082 CYS 1082 1082 ?   ?   ?   A . n 
C 3 1083 HIS 1083 1083 ?   ?   ?   A . n 
C 3 1084 ASP 1084 1084 ?   ?   ?   A . n 
C 3 1085 GLY 1085 1085 ?   ?   ?   A . n 
C 3 1086 LYS 1086 1086 ?   ?   ?   A . n 
C 3 1087 ALA 1087 1087 ?   ?   ?   A . n 
C 3 1088 HIS 1088 1088 ?   ?   ?   A . n 
C 3 1089 PHE 1089 1089 ?   ?   ?   A . n 
C 3 1090 PRO 1090 1090 ?   ?   ?   A . n 
C 3 1091 ARG 1091 1091 ?   ?   ?   A . n 
C 3 1092 GLU 1092 1092 ?   ?   ?   A . n 
C 3 1093 GLY 1093 1093 ?   ?   ?   A . n 
C 3 1094 VAL 1094 1094 ?   ?   ?   A . n 
C 3 1095 PHE 1095 1095 ?   ?   ?   A . n 
C 3 1096 VAL 1096 1096 ?   ?   ?   A . n 
C 3 1097 SER 1097 1097 ?   ?   ?   A . n 
C 3 1098 ASN 1098 1098 ?   ?   ?   A . n 
C 3 1099 GLY 1099 1099 ?   ?   ?   A . n 
C 3 1100 THR 1100 1100 ?   ?   ?   A . n 
C 3 1101 HIS 1101 1101 ?   ?   ?   A . n 
C 3 1102 TRP 1102 1102 ?   ?   ?   A . n 
C 3 1103 PHE 1103 1103 ?   ?   ?   A . n 
C 3 1104 VAL 1104 1104 ?   ?   ?   A . n 
C 3 1105 THR 1105 1105 ?   ?   ?   A . n 
C 3 1106 GLN 1106 1106 ?   ?   ?   A . n 
C 3 1107 ARG 1107 1107 ?   ?   ?   A . n 
C 3 1108 ASN 1108 1108 ?   ?   ?   A . n 
C 3 1109 PHE 1109 1109 ?   ?   ?   A . n 
C 3 1110 TYR 1110 1110 ?   ?   ?   A . n 
C 3 1111 GLU 1111 1111 ?   ?   ?   A . n 
C 3 1112 PRO 1112 1112 ?   ?   ?   A . n 
C 3 1113 GLN 1113 1113 ?   ?   ?   A . n 
C 3 1114 ILE 1114 1114 ?   ?   ?   A . n 
C 3 1115 ILE 1115 1115 ?   ?   ?   A . n 
C 3 1116 THR 1116 1116 ?   ?   ?   A . n 
C 3 1117 THR 1117 1117 ?   ?   ?   A . n 
C 3 1118 ASP 1118 1118 ?   ?   ?   A . n 
C 3 1119 ASN 1119 1119 ?   ?   ?   A . n 
C 3 1120 THR 1120 1120 ?   ?   ?   A . n 
C 3 1121 PHE 1121 1121 ?   ?   ?   A . n 
C 3 1122 VAL 1122 1122 ?   ?   ?   A . n 
C 3 1123 SER 1123 1123 ?   ?   ?   A . n 
C 3 1124 GLY 1124 1124 ?   ?   ?   A . n 
C 3 1125 ASN 1125 1125 ?   ?   ?   A . n 
C 3 1126 CYS 1126 1126 ?   ?   ?   A . n 
C 3 1127 ASP 1127 1127 ?   ?   ?   A . n 
C 3 1128 VAL 1128 1128 ?   ?   ?   A . n 
C 3 1129 VAL 1129 1129 ?   ?   ?   A . n 
C 3 1130 ILE 1130 1130 ?   ?   ?   A . n 
C 3 1131 GLY 1131 1131 ?   ?   ?   A . n 
C 3 1132 ILE 1132 1132 ?   ?   ?   A . n 
C 3 1133 VAL 1133 1133 ?   ?   ?   A . n 
C 3 1134 ASN 1134 1134 ?   ?   ?   A . n 
C 3 1135 ASN 1135 1135 ?   ?   ?   A . n 
C 3 1136 THR 1136 1136 ?   ?   ?   A . n 
C 3 1137 VAL 1137 1137 ?   ?   ?   A . n 
C 3 1138 TYR 1138 1138 ?   ?   ?   A . n 
C 3 1139 ASP 1139 1139 ?   ?   ?   A . n 
C 3 1140 PRO 1140 1140 ?   ?   ?   A . n 
C 3 1141 LEU 1141 1141 ?   ?   ?   A . n 
C 3 1142 GLN 1142 1142 ?   ?   ?   A . n 
C 3 1143 PRO 1143 1143 ?   ?   ?   A . n 
C 3 1144 GLU 1144 1144 ?   ?   ?   A . n 
C 3 1145 LEU 1145 1145 ?   ?   ?   A . n 
C 3 1146 ASP 1146 1146 ?   ?   ?   A . n 
C 3 1147 SER 1147 1147 ?   ?   ?   A . n 
C 3 1148 PHE 1148 1148 ?   ?   ?   A . n 
C 3 1149 LYS 1149 1149 ?   ?   ?   A . n 
C 3 1150 GLU 1150 1150 ?   ?   ?   A . n 
C 3 1151 GLU 1151 1151 ?   ?   ?   A . n 
C 3 1152 LEU 1152 1152 ?   ?   ?   A . n 
C 3 1153 ASP 1153 1153 ?   ?   ?   A . n 
C 3 1154 LYS 1154 1154 ?   ?   ?   A . n 
C 3 1155 TYR 1155 1155 ?   ?   ?   A . n 
C 3 1156 PHE 1156 1156 ?   ?   ?   A . n 
C 3 1157 LYS 1157 1157 ?   ?   ?   A . n 
C 3 1158 ASN 1158 1158 ?   ?   ?   A . n 
C 3 1159 HIS 1159 1159 ?   ?   ?   A . n 
C 3 1160 THR 1160 1160 ?   ?   ?   A . n 
C 3 1161 SER 1161 1161 ?   ?   ?   A . n 
C 3 1162 PRO 1162 1162 ?   ?   ?   A . n 
C 3 1163 ASP 1163 1163 ?   ?   ?   A . n 
C 3 1164 VAL 1164 1164 ?   ?   ?   A . n 
C 3 1165 ASP 1165 1165 ?   ?   ?   A . n 
C 3 1166 LEU 1166 1166 ?   ?   ?   A . n 
C 3 1167 GLY 1167 1167 ?   ?   ?   A . n 
C 3 1168 ASP 1168 1168 ?   ?   ?   A . n 
C 3 1169 ILE 1169 1169 ?   ?   ?   A . n 
C 3 1170 SER 1170 1170 ?   ?   ?   A . n 
C 3 1171 GLY 1171 1171 ?   ?   ?   A . n 
C 3 1172 ILE 1172 1172 ?   ?   ?   A . n 
C 3 1173 ASN 1173 1173 ?   ?   ?   A . n 
C 3 1174 ALA 1174 1174 ?   ?   ?   A . n 
C 3 1175 SER 1175 1175 ?   ?   ?   A . n 
C 3 1176 VAL 1176 1176 ?   ?   ?   A . n 
C 3 1177 VAL 1177 1177 ?   ?   ?   A . n 
C 3 1178 ASN 1178 1178 ?   ?   ?   A . n 
C 3 1179 ILE 1179 1179 ?   ?   ?   A . n 
C 3 1180 GLN 1180 1180 ?   ?   ?   A . n 
C 3 1181 LYS 1181 1181 ?   ?   ?   A . n 
C 3 1182 GLU 1182 1182 ?   ?   ?   A . n 
C 3 1183 ILE 1183 1183 ?   ?   ?   A . n 
C 3 1184 ASP 1184 1184 ?   ?   ?   A . n 
C 3 1185 ARG 1185 1185 ?   ?   ?   A . n 
C 3 1186 LEU 1186 1186 ?   ?   ?   A . n 
C 3 1187 ASN 1187 1187 ?   ?   ?   A . n 
C 3 1188 GLU 1188 1188 ?   ?   ?   A . n 
C 3 1189 VAL 1189 1189 ?   ?   ?   A . n 
C 3 1190 ALA 1190 1190 ?   ?   ?   A . n 
C 3 1191 LYS 1191 1191 ?   ?   ?   A . n 
C 3 1192 ASN 1192 1192 ?   ?   ?   A . n 
C 3 1193 LEU 1193 1193 ?   ?   ?   A . n 
C 3 1194 ASN 1194 1194 ?   ?   ?   A . n 
C 3 1195 GLU 1195 1195 ?   ?   ?   A . n 
C 3 1196 SER 1196 1196 ?   ?   ?   A . n 
C 3 1197 LEU 1197 1197 ?   ?   ?   A . n 
C 3 1198 ILE 1198 1198 ?   ?   ?   A . n 
C 3 1199 ASP 1199 1199 ?   ?   ?   A . n 
C 3 1200 LEU 1200 1200 ?   ?   ?   A . n 
C 3 1201 GLN 1201 1201 ?   ?   ?   A . n 
C 3 1202 GLU 1202 1202 ?   ?   ?   A . n 
C 3 1203 LEU 1203 1203 ?   ?   ?   A . n 
C 3 1204 GLY 1204 1204 ?   ?   ?   A . n 
C 3 1205 LYS 1205 1205 ?   ?   ?   A . n 
C 3 1206 TYR 1206 1206 ?   ?   ?   A . n 
C 3 1207 GLU 1207 1207 ?   ?   ?   A . n 
C 3 1208 GLN 1208 1208 ?   ?   ?   A . n 
C 3 1209 GLY 1209 1209 ?   ?   ?   A . n 
C 3 1210 SER 1210 1210 ?   ?   ?   A . n 
C 3 1211 GLY 1211 1211 ?   ?   ?   A . n 
C 3 1212 TYR 1212 1212 ?   ?   ?   A . n 
C 3 1213 ILE 1213 1213 ?   ?   ?   A . n 
C 3 1214 PRO 1214 1214 ?   ?   ?   A . n 
C 3 1215 GLU 1215 1215 ?   ?   ?   A . n 
C 3 1216 ALA 1216 1216 ?   ?   ?   A . n 
C 3 1217 PRO 1217 1217 ?   ?   ?   A . n 
C 3 1218 ARG 1218 1218 ?   ?   ?   A . n 
C 3 1219 ASP 1219 1219 ?   ?   ?   A . n 
C 3 1220 GLY 1220 1220 ?   ?   ?   A . n 
C 3 1221 GLN 1221 1221 ?   ?   ?   A . n 
C 3 1222 ALA 1222 1222 ?   ?   ?   A . n 
C 3 1223 TYR 1223 1223 ?   ?   ?   A . n 
C 3 1224 VAL 1224 1224 ?   ?   ?   A . n 
C 3 1225 ARG 1225 1225 ?   ?   ?   A . n 
C 3 1226 LYS 1226 1226 ?   ?   ?   A . n 
C 3 1227 ASP 1227 1227 ?   ?   ?   A . n 
C 3 1228 GLY 1228 1228 ?   ?   ?   A . n 
C 3 1229 GLU 1229 1229 ?   ?   ?   A . n 
C 3 1230 TRP 1230 1230 ?   ?   ?   A . n 
C 3 1231 VAL 1231 1231 ?   ?   ?   A . n 
C 3 1232 LEU 1232 1232 ?   ?   ?   A . n 
C 3 1233 LEU 1233 1233 ?   ?   ?   A . n 
C 3 1234 SER 1234 1234 ?   ?   ?   A . n 
C 3 1235 THR 1235 1235 ?   ?   ?   A . n 
C 3 1236 PHE 1236 1236 ?   ?   ?   A . n 
C 3 1237 LEU 1237 1237 ?   ?   ?   A . n 
C 3 1238 GLY 1238 1238 ?   ?   ?   A . n 
C 3 1239 ARG 1239 1239 ?   ?   ?   A . n 
C 3 1240 SER 1240 1240 ?   ?   ?   A . n 
C 3 1241 LEU 1241 1241 ?   ?   ?   A . n 
C 3 1242 GLU 1242 1242 ?   ?   ?   A . n 
C 3 1243 VAL 1243 1243 ?   ?   ?   A . n 
C 3 1244 LEU 1244 1244 ?   ?   ?   A . n 
C 3 1245 PHE 1245 1245 ?   ?   ?   A . n 
C 3 1246 GLN 1246 1246 ?   ?   ?   A . n 
C 3 1247 GLY 1247 1247 ?   ?   ?   A . n 
C 3 1248 PRO 1248 1248 ?   ?   ?   A . n 
C 3 1249 GLY 1249 1249 ?   ?   ?   A . n 
C 3 1250 SER 1250 1250 ?   ?   ?   A . n 
C 3 1251 GLY 1251 1251 ?   ?   ?   A . n 
C 3 1252 GLY 1252 1252 ?   ?   ?   A . n 
C 3 1253 LEU 1253 1253 ?   ?   ?   A . n 
C 3 1254 ASN 1254 1254 ?   ?   ?   A . n 
C 3 1255 ASP 1255 1255 ?   ?   ?   A . n 
C 3 1256 ILE 1256 1256 ?   ?   ?   A . n 
C 3 1257 PHE 1257 1257 ?   ?   ?   A . n 
C 3 1258 GLU 1258 1258 ?   ?   ?   A . n 
C 3 1259 ALA 1259 1259 ?   ?   ?   A . n 
C 3 1260 GLN 1260 1260 ?   ?   ?   A . n 
C 3 1261 LYS 1261 1261 ?   ?   ?   A . n 
C 3 1262 ILE 1262 1262 ?   ?   ?   A . n 
C 3 1263 GLU 1263 1263 ?   ?   ?   A . n 
C 3 1264 TRP 1264 1264 ?   ?   ?   A . n 
C 3 1265 HIS 1265 1265 ?   ?   ?   A . n 
C 3 1266 GLU 1266 1266 ?   ?   ?   A . n 
C 3 1267 GLY 1267 1267 ?   ?   ?   A . n 
C 3 1268 SER 1268 1268 ?   ?   ?   A . n 
C 3 1269 GLY 1269 1269 ?   ?   ?   A . n 
C 3 1270 HIS 1270 1270 ?   ?   ?   A . n 
C 3 1271 HIS 1271 1271 ?   ?   ?   A . n 
C 3 1272 HIS 1272 1272 ?   ?   ?   A . n 
C 3 1273 HIS 1273 1273 ?   ?   ?   A . n 
C 3 1274 HIS 1274 1274 ?   ?   ?   A . n 
C 3 1275 HIS 1275 1275 ?   ?   ?   A . n 
C 3 1276 HIS 1276 1276 ?   ?   ?   A . n 
C 3 1277 HIS 1277 1277 ?   ?   ?   A . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dveesler@uw.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Veesler 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6019-8675 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 5 NAG 1 1301 796 NAG NAG A . 
F 5 NAG 1 1302 804 NAG NAG A . 
G 5 NAG 1 1303 810 NAG NAG A . 
H 5 NAG 1 1304 811 NAG NAG A . 
I 5 NAG 1 1305 812 NAG NAG A . 
J 5 NAG 1 1306 813 NAG NAG A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4960  ? 
1 MORE         4     ? 
1 'SSA (A^2)'  22480 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2021-11-17 
2 'Structure model' 1 1 2021-11-24 
3 'Structure model' 1 2 2021-12-01 
4 'Structure model' 1 3 2022-01-05 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
3 4 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
5 4 'Structure model' citation        
6 4 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2  2 'Structure model' '_citation.title'                   
3  2 'Structure model' '_citation_author.name'             
4  3 'Structure model' '_citation.page_first'              
5  3 'Structure model' '_citation.page_last'               
6  3 'Structure model' '_citation_author.identifier_ORCID' 
7  4 'Structure model' '_citation.journal_volume'          
8  4 'Structure model' '_citation.page_first'              
9  4 'Structure model' '_citation.page_last'               
10 4 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_entry_details.entry_id                 7SOF 
_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         ? 
# 
_em_3d_fitting.entry_id          7SOF 
_em_3d_fitting.id                1 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_protocol      ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.method            ? 
# 
_em_3d_reconstruction.entry_id                    7SOF 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.num_particles               80186 
_em_3d_reconstruction.resolution                  3.6 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.symmetry_type               POINT 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.magnification_calibration   ? 
# 
_em_buffer.id            1 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.details              ? 
_em_entity_assembly.name                 'SARS-CoV-2 S NTD B.1.617.1 Kappa variant + S2X303 Fab' 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
# 
_em_imaging.id                              1 
_em_imaging.entry_id                        7SOF 
_em_imaging.accelerating_voltage            300 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.cryogen                         ? 
_em_imaging.details                         ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_max             ? 
_em_imaging.nominal_defocus_min             ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.specimen_id                     1 
_em_imaging.citation_id                     ? 
_em_imaging.date                            ? 
_em_imaging.temperature                     ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.astigmatism                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.specimen_holder_type            ? 
# 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.details               ? 
_em_vitrification.humidity              ? 
_em_vitrification.instrument            ? 
_em_vitrification.entry_id              7SOF 
_em_vitrification.citation_id           ? 
_em_vitrification.method                ? 
_em_vitrification.temp                  ? 
_em_vitrification.time_resolved_state   ? 
# 
_em_experiment.entry_id                7SOF 
_em_experiment.id                      1 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.entity_assembly_id      1 
# 
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 ASP L 50  ? ? 73.57   -58.30  
2 1 THR L 93  ? ? 83.75   3.12    
3 1 THR H 15  ? ? 73.02   -1.48   
4 1 ASP H 110 ? ? -119.81 -73.71  
5 1 PHE A 32  ? ? -68.11  -70.79  
6 1 ASN A 87  ? ? 53.05   -124.91 
7 1 THR A 108 ? ? -115.18 -80.38  
8 1 ARG A 158 ? ? -119.40 52.05   
9 1 ARG A 214 ? ? -154.38 44.95   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 L SER 1   ? OG  ? A SER 1   OG  
2   1 Y 1 L GLU 3   ? CG  ? A GLU 3   CG  
3   1 Y 1 L GLU 3   ? CD  ? A GLU 3   CD  
4   1 Y 1 L GLU 3   ? OE1 ? A GLU 3   OE1 
5   1 Y 1 L GLU 3   ? OE2 ? A GLU 3   OE2 
6   1 Y 1 L SER 9   ? OG  ? A SER 9   OG  
7   1 Y 1 L SER 11  ? OG  ? A SER 11  OG  
8   1 Y 1 L VAL 12  ? CG1 ? A VAL 12  CG1 
9   1 Y 1 L VAL 12  ? CG2 ? A VAL 12  CG2 
10  1 Y 1 L SER 13  ? OG  ? A SER 13  OG  
11  1 Y 1 L GLN 16  ? CG  ? A GLN 16  CG  
12  1 Y 1 L GLN 16  ? CD  ? A GLN 16  CD  
13  1 Y 1 L GLN 16  ? OE1 ? A GLN 16  OE1 
14  1 Y 1 L GLN 16  ? NE2 ? A GLN 16  NE2 
15  1 Y 1 L THR 21  ? OG1 ? A THR 21  OG1 
16  1 Y 1 L THR 21  ? CG2 ? A THR 21  CG2 
17  1 Y 1 L SER 23  ? OG  ? A SER 23  OG  
18  1 Y 1 L ASP 25  ? CG  ? A ASP 25  CG  
19  1 Y 1 L ASP 25  ? OD1 ? A ASP 25  OD1 
20  1 Y 1 L ASP 25  ? OD2 ? A ASP 25  OD2 
21  1 Y 1 L LYS 26  ? CG  ? A LYS 26  CG  
22  1 Y 1 L LYS 26  ? CD  ? A LYS 26  CD  
23  1 Y 1 L LYS 26  ? CE  ? A LYS 26  CE  
24  1 Y 1 L LYS 26  ? NZ  ? A LYS 26  NZ  
25  1 Y 1 L GLU 29  ? CG  ? A GLU 29  CG  
26  1 Y 1 L GLU 29  ? CD  ? A GLU 29  CD  
27  1 Y 1 L GLU 29  ? OE1 ? A GLU 29  OE1 
28  1 Y 1 L GLU 29  ? OE2 ? A GLU 29  OE2 
29  1 Y 1 L SER 42  ? OG  ? A SER 42  OG  
30  1 Y 1 L SER 55  ? OG  ? A SER 55  OG  
31  1 Y 1 L GLU 59  ? CG  ? A GLU 59  CG  
32  1 Y 1 L GLU 59  ? CD  ? A GLU 59  CD  
33  1 Y 1 L GLU 59  ? OE1 ? A GLU 59  OE1 
34  1 Y 1 L GLU 59  ? OE2 ? A GLU 59  OE2 
35  1 Y 1 L SER 64  ? OG  ? A SER 64  OG  
36  1 Y 1 L SER 66  ? OG  ? A SER 66  OG  
37  1 Y 1 L GLU 67  ? CG  ? A GLU 67  CG  
38  1 Y 1 L GLU 67  ? CD  ? A GLU 67  CD  
39  1 Y 1 L GLU 67  ? OE1 ? A GLU 67  OE1 
40  1 Y 1 L GLU 67  ? OE2 ? A GLU 67  OE2 
41  1 Y 1 L SER 75  ? OG  ? A SER 75  OG  
42  1 Y 1 L THR 77  ? OG1 ? A THR 77  OG1 
43  1 Y 1 L THR 77  ? CG2 ? A THR 77  CG2 
44  1 Y 1 L GLN 78  ? CG  ? A GLN 78  CG  
45  1 Y 1 L GLN 78  ? CD  ? A GLN 78  CD  
46  1 Y 1 L GLN 78  ? OE1 ? A GLN 78  OE1 
47  1 Y 1 L GLN 78  ? NE2 ? A GLN 78  NE2 
48  1 Y 1 L THR 79  ? OG1 ? A THR 79  OG1 
49  1 Y 1 L THR 79  ? CG2 ? A THR 79  CG2 
50  1 Y 1 L MET 80  ? CG  ? A MET 80  CG  
51  1 Y 1 L MET 80  ? SD  ? A MET 80  SD  
52  1 Y 1 L MET 80  ? CE  ? A MET 80  CE  
53  1 Y 1 L ASP 91  ? CG  ? A ASP 91  CG  
54  1 Y 1 L ASP 91  ? OD1 ? A ASP 91  OD1 
55  1 Y 1 L ASP 91  ? OD2 ? A ASP 91  OD2 
56  1 Y 1 L THR 93  ? OG1 ? A THR 93  OG1 
57  1 Y 1 L THR 93  ? CG2 ? A THR 93  CG2 
58  1 Y 1 L THR 104 ? OG1 ? A THR 104 OG1 
59  1 Y 1 L THR 104 ? CG2 ? A THR 104 CG2 
60  1 Y 1 L VAL 105 ? CG1 ? A VAL 105 CG1 
61  1 Y 1 L VAL 105 ? CG2 ? A VAL 105 CG2 
62  1 Y 1 H GLN 1   ? CG  ? B GLN 1   CG  
63  1 Y 1 H GLN 1   ? CD  ? B GLN 1   CD  
64  1 Y 1 H GLN 1   ? OE1 ? B GLN 1   OE1 
65  1 Y 1 H GLN 1   ? NE2 ? B GLN 1   NE2 
66  1 Y 1 H LYS 13  ? CG  ? B LYS 13  CG  
67  1 Y 1 H LYS 13  ? CD  ? B LYS 13  CD  
68  1 Y 1 H LYS 13  ? CE  ? B LYS 13  CE  
69  1 Y 1 H LYS 13  ? NZ  ? B LYS 13  NZ  
70  1 Y 1 H GLN 16  ? CG  ? B GLN 16  CG  
71  1 Y 1 H GLN 16  ? CD  ? B GLN 16  CD  
72  1 Y 1 H GLN 16  ? OE1 ? B GLN 16  OE1 
73  1 Y 1 H GLN 16  ? NE2 ? B GLN 16  NE2 
74  1 Y 1 H LYS 23  ? CG  ? B LYS 23  CG  
75  1 Y 1 H LYS 23  ? CD  ? B LYS 23  CD  
76  1 Y 1 H LYS 23  ? CE  ? B LYS 23  CE  
77  1 Y 1 H LYS 23  ? NZ  ? B LYS 23  NZ  
78  1 Y 1 H SER 25  ? OG  ? B SER 25  OG  
79  1 Y 1 H SER 28  ? OG  ? B SER 28  OG  
80  1 Y 1 H ASP 58  ? CG  ? B ASP 58  CG  
81  1 Y 1 H ASP 58  ? OD1 ? B ASP 58  OD1 
82  1 Y 1 H ASP 58  ? OD2 ? B ASP 58  OD2 
83  1 Y 1 H SER 64  ? OG  ? B SER 64  OG  
84  1 Y 1 H SER 67  ? OG  ? B SER 67  OG  
85  1 Y 1 H THR 70  ? OG1 ? B THR 70  OG1 
86  1 Y 1 H THR 70  ? CG2 ? B THR 70  CG2 
87  1 Y 1 H THR 72  ? OG1 ? B THR 72  OG1 
88  1 Y 1 H THR 72  ? CG2 ? B THR 72  CG2 
89  1 Y 1 H THR 75  ? OG1 ? B THR 75  OG1 
90  1 Y 1 H THR 75  ? CG2 ? B THR 75  CG2 
91  1 Y 1 H SER 76  ? OG  ? B SER 76  OG  
92  1 Y 1 H ASP 88  ? CG  ? B ASP 88  CG  
93  1 Y 1 H ASP 88  ? OD1 ? B ASP 88  OD1 
94  1 Y 1 H ASP 88  ? OD2 ? B ASP 88  OD2 
95  1 Y 1 H VAL 90  ? CG1 ? B VAL 90  CG1 
96  1 Y 1 H VAL 90  ? CG2 ? B VAL 90  CG2 
97  1 Y 1 H GLU 106 ? CG  ? B GLU 106 CG  
98  1 Y 1 H GLU 106 ? CD  ? B GLU 106 CD  
99  1 Y 1 H GLU 106 ? OE1 ? B GLU 106 OE1 
100 1 Y 1 H GLU 106 ? OE2 ? B GLU 106 OE2 
101 1 Y 1 H GLN 117 ? CG  ? B GLN 117 CG  
102 1 Y 1 H GLN 117 ? CD  ? B GLN 117 CD  
103 1 Y 1 H GLN 117 ? OE1 ? B GLN 117 OE1 
104 1 Y 1 H GLN 117 ? NE2 ? B GLN 117 NE2 
105 1 Y 1 H THR 119 ? OG1 ? B THR 119 OG1 
106 1 Y 1 H THR 119 ? CG2 ? B THR 119 CG2 
107 1 Y 1 H MET 120 ? CG  ? B MET 120 CG  
108 1 Y 1 H MET 120 ? SD  ? B MET 120 SD  
109 1 Y 1 H MET 120 ? CE  ? B MET 120 CE  
110 1 Y 1 H SER 125 ? OG  ? B SER 125 OG  
111 1 Y 1 A GLN 14  ? CG  ? C GLN 14  CG  
112 1 Y 1 A GLN 14  ? CD  ? C GLN 14  CD  
113 1 Y 1 A GLN 14  ? OE1 ? C GLN 14  OE1 
114 1 Y 1 A GLN 14  ? NE2 ? C GLN 14  NE2 
115 1 Y 1 A THR 19  ? OG1 ? C THR 19  OG1 
116 1 Y 1 A THR 19  ? CG2 ? C THR 19  CG2 
117 1 Y 1 A THR 20  ? OG1 ? C THR 20  OG1 
118 1 Y 1 A THR 20  ? CG2 ? C THR 20  CG2 
119 1 Y 1 A ASN 30  ? CG  ? C ASN 30  CG  
120 1 Y 1 A ASN 30  ? OD1 ? C ASN 30  OD1 
121 1 Y 1 A ASN 30  ? ND2 ? C ASN 30  ND2 
122 1 Y 1 A PHE 32  ? CG  ? C PHE 32  CG  
123 1 Y 1 A PHE 32  ? CD1 ? C PHE 32  CD1 
124 1 Y 1 A PHE 32  ? CD2 ? C PHE 32  CD2 
125 1 Y 1 A PHE 32  ? CE1 ? C PHE 32  CE1 
126 1 Y 1 A PHE 32  ? CE2 ? C PHE 32  CE2 
127 1 Y 1 A PHE 32  ? CZ  ? C PHE 32  CZ  
128 1 Y 1 A THR 33  ? OG1 ? C THR 33  OG1 
129 1 Y 1 A THR 33  ? CG2 ? C THR 33  CG2 
130 1 Y 1 A ASP 40  ? CG  ? C ASP 40  CG  
131 1 Y 1 A ASP 40  ? OD1 ? C ASP 40  OD1 
132 1 Y 1 A ASP 40  ? OD2 ? C ASP 40  OD2 
133 1 Y 1 A LYS 41  ? CG  ? C LYS 41  CG  
134 1 Y 1 A LYS 41  ? CD  ? C LYS 41  CD  
135 1 Y 1 A LYS 41  ? CE  ? C LYS 41  CE  
136 1 Y 1 A LYS 41  ? NZ  ? C LYS 41  NZ  
137 1 Y 1 A VAL 42  ? CG1 ? C VAL 42  CG1 
138 1 Y 1 A VAL 42  ? CG2 ? C VAL 42  CG2 
139 1 Y 1 A ARG 44  ? CG  ? C ARG 44  CG  
140 1 Y 1 A ARG 44  ? CD  ? C ARG 44  CD  
141 1 Y 1 A ARG 44  ? NE  ? C ARG 44  NE  
142 1 Y 1 A ARG 44  ? CZ  ? C ARG 44  CZ  
143 1 Y 1 A ARG 44  ? NH1 ? C ARG 44  NH1 
144 1 Y 1 A ARG 44  ? NH2 ? C ARG 44  NH2 
145 1 Y 1 A SER 45  ? OG  ? C SER 45  OG  
146 1 Y 1 A SER 46  ? OG  ? C SER 46  OG  
147 1 Y 1 A LEU 48  ? CG  ? C LEU 48  CG  
148 1 Y 1 A LEU 48  ? CD1 ? C LEU 48  CD1 
149 1 Y 1 A LEU 48  ? CD2 ? C LEU 48  CD2 
150 1 Y 1 A SER 50  ? OG  ? C SER 50  OG  
151 1 Y 1 A THR 51  ? OG1 ? C THR 51  OG1 
152 1 Y 1 A THR 51  ? CG2 ? C THR 51  CG2 
153 1 Y 1 A GLN 52  ? CG  ? C GLN 52  CG  
154 1 Y 1 A GLN 52  ? CD  ? C GLN 52  CD  
155 1 Y 1 A GLN 52  ? OE1 ? C GLN 52  OE1 
156 1 Y 1 A GLN 52  ? NE2 ? C GLN 52  NE2 
157 1 Y 1 A ASP 53  ? CG  ? C ASP 53  CG  
158 1 Y 1 A ASP 53  ? OD1 ? C ASP 53  OD1 
159 1 Y 1 A ASP 53  ? OD2 ? C ASP 53  OD2 
160 1 Y 1 A SER 60  ? OG  ? C SER 60  OG  
161 1 Y 1 A ASP 88  ? CG  ? C ASP 88  CG  
162 1 Y 1 A ASP 88  ? OD1 ? C ASP 88  OD1 
163 1 Y 1 A ASP 88  ? OD2 ? C ASP 88  OD2 
164 1 Y 1 A LYS 113 ? CG  ? C LYS 113 CG  
165 1 Y 1 A LYS 113 ? CD  ? C LYS 113 CD  
166 1 Y 1 A LYS 113 ? CE  ? C LYS 113 CE  
167 1 Y 1 A LYS 113 ? NZ  ? C LYS 113 NZ  
168 1 Y 1 A GLU 132 ? CG  ? C GLU 132 CG  
169 1 Y 1 A GLU 132 ? CD  ? C GLU 132 CD  
170 1 Y 1 A GLU 132 ? OE1 ? C GLU 132 OE1 
171 1 Y 1 A GLU 132 ? OE2 ? C GLU 132 OE2 
172 1 Y 1 A ASN 137 ? CG  ? C ASN 137 CG  
173 1 Y 1 A ASN 137 ? OD1 ? C ASN 137 OD1 
174 1 Y 1 A ASN 137 ? ND2 ? C ASN 137 ND2 
175 1 Y 1 A LEU 176 ? CG  ? C LEU 176 CG  
176 1 Y 1 A LEU 176 ? CD1 ? C LEU 176 CD1 
177 1 Y 1 A LEU 176 ? CD2 ? C LEU 176 CD2 
178 1 Y 1 A ILE 197 ? CG1 ? C ILE 197 CG1 
179 1 Y 1 A ILE 197 ? CG2 ? C ILE 197 CG2 
180 1 Y 1 A ILE 197 ? CD1 ? C ILE 197 CD1 
181 1 Y 1 A ASP 198 ? CG  ? C ASP 198 CG  
182 1 Y 1 A ASP 198 ? OD1 ? C ASP 198 OD1 
183 1 Y 1 A ASP 198 ? OD2 ? C ASP 198 OD2 
184 1 Y 1 A ASN 211 ? CG  ? C ASN 211 CG  
185 1 Y 1 A ASN 211 ? OD1 ? C ASN 211 OD1 
186 1 Y 1 A ASN 211 ? ND2 ? C ASN 211 ND2 
187 1 Y 1 A VAL 213 ? CG1 ? C VAL 213 CG1 
188 1 Y 1 A VAL 213 ? CG2 ? C VAL 213 CG2 
189 1 Y 1 A ARG 214 ? CG  ? C ARG 214 CG  
190 1 Y 1 A ARG 214 ? CD  ? C ARG 214 CD  
191 1 Y 1 A ARG 214 ? NE  ? C ARG 214 NE  
192 1 Y 1 A ARG 214 ? CZ  ? C ARG 214 CZ  
193 1 Y 1 A ARG 214 ? NH1 ? C ARG 214 NH1 
194 1 Y 1 A ARG 214 ? NH2 ? C ARG 214 NH2 
195 1 Y 1 A ASP 215 ? CG  ? C ASP 215 CG  
196 1 Y 1 A ASP 215 ? OD1 ? C ASP 215 OD1 
197 1 Y 1 A ASP 215 ? OD2 ? C ASP 215 OD2 
198 1 Y 1 A GLN 218 ? CG  ? C GLN 218 CG  
199 1 Y 1 A GLN 218 ? CD  ? C GLN 218 CD  
200 1 Y 1 A GLN 218 ? OE1 ? C GLN 218 OE1 
201 1 Y 1 A GLN 218 ? NE2 ? C GLN 218 NE2 
202 1 Y 1 A GLU 224 ? CG  ? C GLU 224 CG  
203 1 Y 1 A GLU 224 ? CD  ? C GLU 224 CD  
204 1 Y 1 A GLU 224 ? OE1 ? C GLU 224 OE1 
205 1 Y 1 A GLU 224 ? OE2 ? C GLU 224 OE2 
206 1 Y 1 A THR 274 ? OG1 ? C THR 274 OG1 
207 1 Y 1 A THR 274 ? CG2 ? C THR 274 CG2 
208 1 Y 1 A LEU 276 ? CG  ? C LEU 276 CG  
209 1 Y 1 A LEU 276 ? CD1 ? C LEU 276 CD1 
210 1 Y 1 A LEU 276 ? CD2 ? C LEU 276 CD2 
211 1 Y 1 A ASN 280 ? CG  ? C ASN 280 CG  
212 1 Y 1 A ASN 280 ? OD1 ? C ASN 280 OD1 
213 1 Y 1 A ASN 280 ? ND2 ? C ASN 280 ND2 
214 1 Y 1 A GLU 281 ? CG  ? C GLU 281 CG  
215 1 Y 1 A GLU 281 ? CD  ? C GLU 281 CD  
216 1 Y 1 A GLU 281 ? OE1 ? C GLU 281 OE1 
217 1 Y 1 A GLU 281 ? OE2 ? C GLU 281 OE2 
218 1 Y 1 A ASP 287 ? CG  ? C ASP 287 CG  
219 1 Y 1 A ASP 287 ? OD1 ? C ASP 287 OD1 
220 1 Y 1 A ASP 287 ? OD2 ? C ASP 287 OD2 
221 1 Y 1 A ASP 294 ? CG  ? C ASP 294 CG  
222 1 Y 1 A ASP 294 ? OD1 ? C ASP 294 OD1 
223 1 Y 1 A ASP 294 ? OD2 ? C ASP 294 OD2 
224 1 Y 1 A SER 297 ? OG  ? C SER 297 OG  
225 1 Y 1 A GLU 298 ? CG  ? C GLU 298 CG  
226 1 Y 1 A GLU 298 ? CD  ? C GLU 298 CD  
227 1 Y 1 A GLU 298 ? OE1 ? C GLU 298 OE1 
228 1 Y 1 A GLU 298 ? OE2 ? C GLU 298 OE2 
229 1 Y 1 A THR 299 ? OG1 ? C THR 299 OG1 
230 1 Y 1 A THR 299 ? CG2 ? C THR 299 CG2 
231 1 Y 1 A LYS 300 ? CG  ? C LYS 300 CG  
232 1 Y 1 A LYS 300 ? CD  ? C LYS 300 CD  
233 1 Y 1 A LYS 300 ? CE  ? C LYS 300 CE  
234 1 Y 1 A LYS 300 ? NZ  ? C LYS 300 NZ  
235 1 Y 1 A THR 302 ? OG1 ? C THR 302 OG1 
236 1 Y 1 A THR 302 ? CG2 ? C THR 302 CG2 
237 1 Y 1 A LEU 303 ? CG  ? C LEU 303 CG  
238 1 Y 1 A LEU 303 ? CD1 ? C LEU 303 CD1 
239 1 Y 1 A LEU 303 ? CD2 ? C LEU 303 CD2 
240 1 Y 1 A LYS 304 ? CG  ? C LYS 304 CG  
241 1 Y 1 A LYS 304 ? CD  ? C LYS 304 CD  
242 1 Y 1 A LYS 304 ? CE  ? C LYS 304 CE  
243 1 Y 1 A LYS 304 ? NZ  ? C LYS 304 NZ  
244 1 Y 1 A SER 305 ? OG  ? C SER 305 OG  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? C MET 1    
2    1 Y 1 A PHE 2    ? C PHE 2    
3    1 Y 1 A VAL 3    ? C VAL 3    
4    1 Y 1 A PHE 4    ? C PHE 4    
5    1 Y 1 A LEU 5    ? C LEU 5    
6    1 Y 1 A VAL 6    ? C VAL 6    
7    1 Y 1 A LEU 7    ? C LEU 7    
8    1 Y 1 A LEU 8    ? C LEU 8    
9    1 Y 1 A PRO 9    ? C PRO 9    
10   1 Y 1 A LEU 10   ? C LEU 10   
11   1 Y 1 A VAL 11   ? C VAL 11   
12   1 Y 1 A SER 12   ? C SER 12   
13   1 Y 1 A SER 13   ? C SER 13   
14   1 Y 1 A ARG 21   ? C ARG 21   
15   1 Y 1 A THR 22   ? C THR 22   
16   1 Y 1 A GLN 23   ? C GLN 23   
17   1 Y 1 A LEU 24   ? C LEU 24   
18   1 Y 1 A PRO 25   ? C PRO 25   
19   1 Y 1 A ILE 68   ? C ILE 68   
20   1 Y 1 A HIS 69   ? C HIS 69   
21   1 Y 1 A VAL 70   ? C VAL 70   
22   1 Y 1 A SER 71   ? C SER 71   
23   1 Y 1 A GLY 72   ? C GLY 72   
24   1 Y 1 A THR 73   ? C THR 73   
25   1 Y 1 A ASN 74   ? C ASN 74   
26   1 Y 1 A GLY 75   ? C GLY 75   
27   1 Y 1 A THR 76   ? C THR 76   
28   1 Y 1 A LYS 77   ? C LYS 77   
29   1 Y 1 A MET 177  ? C MET 177  
30   1 Y 1 A ASP 178  ? C ASP 178  
31   1 Y 1 A LEU 179  ? C LEU 179  
32   1 Y 1 A GLU 180  ? C GLU 180  
33   1 Y 1 A GLY 181  ? C GLY 181  
34   1 Y 1 A LYS 182  ? C LYS 182  
35   1 Y 1 A GLN 183  ? C GLN 183  
36   1 Y 1 A GLY 184  ? C GLY 184  
37   1 Y 1 A ASN 185  ? C ASN 185  
38   1 Y 1 A SER 247  ? C SER 247  
39   1 Y 1 A TYR 248  ? C TYR 248  
40   1 Y 1 A LEU 249  ? C LEU 249  
41   1 Y 1 A THR 250  ? C THR 250  
42   1 Y 1 A PRO 251  ? C PRO 251  
43   1 Y 1 A GLY 252  ? C GLY 252  
44   1 Y 1 A ASP 253  ? C ASP 253  
45   1 Y 1 A SER 254  ? C SER 254  
46   1 Y 1 A SER 255  ? C SER 255  
47   1 Y 1 A SER 256  ? C SER 256  
48   1 Y 1 A PHE 306  ? C PHE 306  
49   1 Y 1 A THR 307  ? C THR 307  
50   1 Y 1 A VAL 308  ? C VAL 308  
51   1 Y 1 A GLU 309  ? C GLU 309  
52   1 Y 1 A LYS 310  ? C LYS 310  
53   1 Y 1 A GLY 311  ? C GLY 311  
54   1 Y 1 A ILE 312  ? C ILE 312  
55   1 Y 1 A TYR 313  ? C TYR 313  
56   1 Y 1 A GLN 314  ? C GLN 314  
57   1 Y 1 A THR 315  ? C THR 315  
58   1 Y 1 A SER 316  ? C SER 316  
59   1 Y 1 A ASN 317  ? C ASN 317  
60   1 Y 1 A PHE 318  ? C PHE 318  
61   1 Y 1 A ARG 319  ? C ARG 319  
62   1 Y 1 A VAL 320  ? C VAL 320  
63   1 Y 1 A GLN 321  ? C GLN 321  
64   1 Y 1 A PRO 322  ? C PRO 322  
65   1 Y 1 A THR 323  ? C THR 323  
66   1 Y 1 A GLU 324  ? C GLU 324  
67   1 Y 1 A SER 325  ? C SER 325  
68   1 Y 1 A ILE 326  ? C ILE 326  
69   1 Y 1 A VAL 327  ? C VAL 327  
70   1 Y 1 A ARG 328  ? C ARG 328  
71   1 Y 1 A PHE 329  ? C PHE 329  
72   1 Y 1 A PRO 330  ? C PRO 330  
73   1 Y 1 A ASN 331  ? C ASN 331  
74   1 Y 1 A ILE 332  ? C ILE 332  
75   1 Y 1 A THR 333  ? C THR 333  
76   1 Y 1 A ASN 334  ? C ASN 334  
77   1 Y 1 A LEU 335  ? C LEU 335  
78   1 Y 1 A CYS 336  ? C CYS 336  
79   1 Y 1 A PRO 337  ? C PRO 337  
80   1 Y 1 A PHE 338  ? C PHE 338  
81   1 Y 1 A GLY 339  ? C GLY 339  
82   1 Y 1 A GLU 340  ? C GLU 340  
83   1 Y 1 A VAL 341  ? C VAL 341  
84   1 Y 1 A PHE 342  ? C PHE 342  
85   1 Y 1 A ASN 343  ? C ASN 343  
86   1 Y 1 A ALA 344  ? C ALA 344  
87   1 Y 1 A THR 345  ? C THR 345  
88   1 Y 1 A ARG 346  ? C ARG 346  
89   1 Y 1 A PHE 347  ? C PHE 347  
90   1 Y 1 A ALA 348  ? C ALA 348  
91   1 Y 1 A SER 349  ? C SER 349  
92   1 Y 1 A VAL 350  ? C VAL 350  
93   1 Y 1 A TYR 351  ? C TYR 351  
94   1 Y 1 A ALA 352  ? C ALA 352  
95   1 Y 1 A TRP 353  ? C TRP 353  
96   1 Y 1 A ASN 354  ? C ASN 354  
97   1 Y 1 A ARG 355  ? C ARG 355  
98   1 Y 1 A LYS 356  ? C LYS 356  
99   1 Y 1 A ARG 357  ? C ARG 357  
100  1 Y 1 A ILE 358  ? C ILE 358  
101  1 Y 1 A SER 359  ? C SER 359  
102  1 Y 1 A ASN 360  ? C ASN 360  
103  1 Y 1 A CYS 361  ? C CYS 361  
104  1 Y 1 A VAL 362  ? C VAL 362  
105  1 Y 1 A ALA 363  ? C ALA 363  
106  1 Y 1 A ASP 364  ? C ASP 364  
107  1 Y 1 A TYR 365  ? C TYR 365  
108  1 Y 1 A SER 366  ? C SER 366  
109  1 Y 1 A VAL 367  ? C VAL 367  
110  1 Y 1 A LEU 368  ? C LEU 368  
111  1 Y 1 A TYR 369  ? C TYR 369  
112  1 Y 1 A ASN 370  ? C ASN 370  
113  1 Y 1 A SER 371  ? C SER 371  
114  1 Y 1 A ALA 372  ? C ALA 372  
115  1 Y 1 A SER 373  ? C SER 373  
116  1 Y 1 A PHE 374  ? C PHE 374  
117  1 Y 1 A SER 375  ? C SER 375  
118  1 Y 1 A THR 376  ? C THR 376  
119  1 Y 1 A PHE 377  ? C PHE 377  
120  1 Y 1 A LYS 378  ? C LYS 378  
121  1 Y 1 A CYS 379  ? C CYS 379  
122  1 Y 1 A TYR 380  ? C TYR 380  
123  1 Y 1 A GLY 381  ? C GLY 381  
124  1 Y 1 A VAL 382  ? C VAL 382  
125  1 Y 1 A CYS 383  ? C CYS 383  
126  1 Y 1 A PRO 384  ? C PRO 384  
127  1 Y 1 A THR 385  ? C THR 385  
128  1 Y 1 A LYS 386  ? C LYS 386  
129  1 Y 1 A LEU 387  ? C LEU 387  
130  1 Y 1 A ASN 388  ? C ASN 388  
131  1 Y 1 A ASP 389  ? C ASP 389  
132  1 Y 1 A LEU 390  ? C LEU 390  
133  1 Y 1 A CYS 391  ? C CYS 391  
134  1 Y 1 A PHE 392  ? C PHE 392  
135  1 Y 1 A THR 393  ? C THR 393  
136  1 Y 1 A ASN 394  ? C ASN 394  
137  1 Y 1 A VAL 395  ? C VAL 395  
138  1 Y 1 A TYR 396  ? C TYR 396  
139  1 Y 1 A ALA 397  ? C ALA 397  
140  1 Y 1 A ASP 398  ? C ASP 398  
141  1 Y 1 A SER 399  ? C SER 399  
142  1 Y 1 A PHE 400  ? C PHE 400  
143  1 Y 1 A VAL 401  ? C VAL 401  
144  1 Y 1 A ILE 402  ? C ILE 402  
145  1 Y 1 A ARG 403  ? C ARG 403  
146  1 Y 1 A GLY 404  ? C GLY 404  
147  1 Y 1 A ASP 405  ? C ASP 405  
148  1 Y 1 A GLU 406  ? C GLU 406  
149  1 Y 1 A VAL 407  ? C VAL 407  
150  1 Y 1 A ARG 408  ? C ARG 408  
151  1 Y 1 A GLN 409  ? C GLN 409  
152  1 Y 1 A ILE 410  ? C ILE 410  
153  1 Y 1 A ALA 411  ? C ALA 411  
154  1 Y 1 A PRO 412  ? C PRO 412  
155  1 Y 1 A GLY 413  ? C GLY 413  
156  1 Y 1 A GLN 414  ? C GLN 414  
157  1 Y 1 A THR 415  ? C THR 415  
158  1 Y 1 A GLY 416  ? C GLY 416  
159  1 Y 1 A LYS 417  ? C LYS 417  
160  1 Y 1 A ILE 418  ? C ILE 418  
161  1 Y 1 A ALA 419  ? C ALA 419  
162  1 Y 1 A ASP 420  ? C ASP 420  
163  1 Y 1 A TYR 421  ? C TYR 421  
164  1 Y 1 A ASN 422  ? C ASN 422  
165  1 Y 1 A TYR 423  ? C TYR 423  
166  1 Y 1 A LYS 424  ? C LYS 424  
167  1 Y 1 A LEU 425  ? C LEU 425  
168  1 Y 1 A PRO 426  ? C PRO 426  
169  1 Y 1 A ASP 427  ? C ASP 427  
170  1 Y 1 A ASP 428  ? C ASP 428  
171  1 Y 1 A PHE 429  ? C PHE 429  
172  1 Y 1 A THR 430  ? C THR 430  
173  1 Y 1 A GLY 431  ? C GLY 431  
174  1 Y 1 A CYS 432  ? C CYS 432  
175  1 Y 1 A VAL 433  ? C VAL 433  
176  1 Y 1 A ILE 434  ? C ILE 434  
177  1 Y 1 A ALA 435  ? C ALA 435  
178  1 Y 1 A TRP 436  ? C TRP 436  
179  1 Y 1 A ASN 437  ? C ASN 437  
180  1 Y 1 A SER 438  ? C SER 438  
181  1 Y 1 A ASN 439  ? C ASN 439  
182  1 Y 1 A ASN 440  ? C ASN 440  
183  1 Y 1 A LEU 441  ? C LEU 441  
184  1 Y 1 A ASP 442  ? C ASP 442  
185  1 Y 1 A SER 443  ? C SER 443  
186  1 Y 1 A LYS 444  ? C LYS 444  
187  1 Y 1 A VAL 445  ? C VAL 445  
188  1 Y 1 A GLY 446  ? C GLY 446  
189  1 Y 1 A GLY 447  ? C GLY 447  
190  1 Y 1 A ASN 448  ? C ASN 448  
191  1 Y 1 A TYR 449  ? C TYR 449  
192  1 Y 1 A ASN 450  ? C ASN 450  
193  1 Y 1 A TYR 451  ? C TYR 451  
194  1 Y 1 A ARG 452  ? C ARG 452  
195  1 Y 1 A TYR 453  ? C TYR 453  
196  1 Y 1 A ARG 454  ? C ARG 454  
197  1 Y 1 A LEU 455  ? C LEU 455  
198  1 Y 1 A PHE 456  ? C PHE 456  
199  1 Y 1 A ARG 457  ? C ARG 457  
200  1 Y 1 A LYS 458  ? C LYS 458  
201  1 Y 1 A SER 459  ? C SER 459  
202  1 Y 1 A ASN 460  ? C ASN 460  
203  1 Y 1 A LEU 461  ? C LEU 461  
204  1 Y 1 A LYS 462  ? C LYS 462  
205  1 Y 1 A PRO 463  ? C PRO 463  
206  1 Y 1 A PHE 464  ? C PHE 464  
207  1 Y 1 A GLU 465  ? C GLU 465  
208  1 Y 1 A ARG 466  ? C ARG 466  
209  1 Y 1 A ASP 467  ? C ASP 467  
210  1 Y 1 A ILE 468  ? C ILE 468  
211  1 Y 1 A SER 469  ? C SER 469  
212  1 Y 1 A THR 470  ? C THR 470  
213  1 Y 1 A GLU 471  ? C GLU 471  
214  1 Y 1 A ILE 472  ? C ILE 472  
215  1 Y 1 A TYR 473  ? C TYR 473  
216  1 Y 1 A GLN 474  ? C GLN 474  
217  1 Y 1 A ALA 475  ? C ALA 475  
218  1 Y 1 A GLY 476  ? C GLY 476  
219  1 Y 1 A SER 477  ? C SER 477  
220  1 Y 1 A THR 478  ? C THR 478  
221  1 Y 1 A PRO 479  ? C PRO 479  
222  1 Y 1 A CYS 480  ? C CYS 480  
223  1 Y 1 A ASN 481  ? C ASN 481  
224  1 Y 1 A GLY 482  ? C GLY 482  
225  1 Y 1 A VAL 483  ? C VAL 483  
226  1 Y 1 A GLN 484  ? C GLN 484  
227  1 Y 1 A GLY 485  ? C GLY 485  
228  1 Y 1 A PHE 486  ? C PHE 486  
229  1 Y 1 A ASN 487  ? C ASN 487  
230  1 Y 1 A CYS 488  ? C CYS 488  
231  1 Y 1 A TYR 489  ? C TYR 489  
232  1 Y 1 A PHE 490  ? C PHE 490  
233  1 Y 1 A PRO 491  ? C PRO 491  
234  1 Y 1 A LEU 492  ? C LEU 492  
235  1 Y 1 A GLN 493  ? C GLN 493  
236  1 Y 1 A SER 494  ? C SER 494  
237  1 Y 1 A TYR 495  ? C TYR 495  
238  1 Y 1 A GLY 496  ? C GLY 496  
239  1 Y 1 A PHE 497  ? C PHE 497  
240  1 Y 1 A GLN 498  ? C GLN 498  
241  1 Y 1 A PRO 499  ? C PRO 499  
242  1 Y 1 A THR 500  ? C THR 500  
243  1 Y 1 A ASN 501  ? C ASN 501  
244  1 Y 1 A GLY 502  ? C GLY 502  
245  1 Y 1 A VAL 503  ? C VAL 503  
246  1 Y 1 A GLY 504  ? C GLY 504  
247  1 Y 1 A TYR 505  ? C TYR 505  
248  1 Y 1 A GLN 506  ? C GLN 506  
249  1 Y 1 A PRO 507  ? C PRO 507  
250  1 Y 1 A TYR 508  ? C TYR 508  
251  1 Y 1 A ARG 509  ? C ARG 509  
252  1 Y 1 A VAL 510  ? C VAL 510  
253  1 Y 1 A VAL 511  ? C VAL 511  
254  1 Y 1 A VAL 512  ? C VAL 512  
255  1 Y 1 A LEU 513  ? C LEU 513  
256  1 Y 1 A SER 514  ? C SER 514  
257  1 Y 1 A PHE 515  ? C PHE 515  
258  1 Y 1 A GLU 516  ? C GLU 516  
259  1 Y 1 A LEU 517  ? C LEU 517  
260  1 Y 1 A LEU 518  ? C LEU 518  
261  1 Y 1 A HIS 519  ? C HIS 519  
262  1 Y 1 A ALA 520  ? C ALA 520  
263  1 Y 1 A PRO 521  ? C PRO 521  
264  1 Y 1 A ALA 522  ? C ALA 522  
265  1 Y 1 A THR 523  ? C THR 523  
266  1 Y 1 A VAL 524  ? C VAL 524  
267  1 Y 1 A CYS 525  ? C CYS 525  
268  1 Y 1 A GLY 526  ? C GLY 526  
269  1 Y 1 A PRO 527  ? C PRO 527  
270  1 Y 1 A LYS 528  ? C LYS 528  
271  1 Y 1 A LYS 529  ? C LYS 529  
272  1 Y 1 A SER 530  ? C SER 530  
273  1 Y 1 A THR 531  ? C THR 531  
274  1 Y 1 A ASN 532  ? C ASN 532  
275  1 Y 1 A LEU 533  ? C LEU 533  
276  1 Y 1 A VAL 534  ? C VAL 534  
277  1 Y 1 A LYS 535  ? C LYS 535  
278  1 Y 1 A ASN 536  ? C ASN 536  
279  1 Y 1 A LYS 537  ? C LYS 537  
280  1 Y 1 A CYS 538  ? C CYS 538  
281  1 Y 1 A VAL 539  ? C VAL 539  
282  1 Y 1 A ASN 540  ? C ASN 540  
283  1 Y 1 A PHE 541  ? C PHE 541  
284  1 Y 1 A ASN 542  ? C ASN 542  
285  1 Y 1 A PHE 543  ? C PHE 543  
286  1 Y 1 A ASN 544  ? C ASN 544  
287  1 Y 1 A GLY 545  ? C GLY 545  
288  1 Y 1 A LEU 546  ? C LEU 546  
289  1 Y 1 A THR 547  ? C THR 547  
290  1 Y 1 A GLY 548  ? C GLY 548  
291  1 Y 1 A THR 549  ? C THR 549  
292  1 Y 1 A GLY 550  ? C GLY 550  
293  1 Y 1 A VAL 551  ? C VAL 551  
294  1 Y 1 A LEU 552  ? C LEU 552  
295  1 Y 1 A THR 553  ? C THR 553  
296  1 Y 1 A GLU 554  ? C GLU 554  
297  1 Y 1 A SER 555  ? C SER 555  
298  1 Y 1 A ASN 556  ? C ASN 556  
299  1 Y 1 A LYS 557  ? C LYS 557  
300  1 Y 1 A LYS 558  ? C LYS 558  
301  1 Y 1 A PHE 559  ? C PHE 559  
302  1 Y 1 A LEU 560  ? C LEU 560  
303  1 Y 1 A PRO 561  ? C PRO 561  
304  1 Y 1 A PHE 562  ? C PHE 562  
305  1 Y 1 A GLN 563  ? C GLN 563  
306  1 Y 1 A GLN 564  ? C GLN 564  
307  1 Y 1 A PHE 565  ? C PHE 565  
308  1 Y 1 A GLY 566  ? C GLY 566  
309  1 Y 1 A ARG 567  ? C ARG 567  
310  1 Y 1 A ASP 568  ? C ASP 568  
311  1 Y 1 A ILE 569  ? C ILE 569  
312  1 Y 1 A ALA 570  ? C ALA 570  
313  1 Y 1 A ASP 571  ? C ASP 571  
314  1 Y 1 A THR 572  ? C THR 572  
315  1 Y 1 A THR 573  ? C THR 573  
316  1 Y 1 A ASP 574  ? C ASP 574  
317  1 Y 1 A ALA 575  ? C ALA 575  
318  1 Y 1 A VAL 576  ? C VAL 576  
319  1 Y 1 A ARG 577  ? C ARG 577  
320  1 Y 1 A ASP 578  ? C ASP 578  
321  1 Y 1 A PRO 579  ? C PRO 579  
322  1 Y 1 A GLN 580  ? C GLN 580  
323  1 Y 1 A THR 581  ? C THR 581  
324  1 Y 1 A LEU 582  ? C LEU 582  
325  1 Y 1 A GLU 583  ? C GLU 583  
326  1 Y 1 A ILE 584  ? C ILE 584  
327  1 Y 1 A LEU 585  ? C LEU 585  
328  1 Y 1 A ASP 586  ? C ASP 586  
329  1 Y 1 A ILE 587  ? C ILE 587  
330  1 Y 1 A THR 588  ? C THR 588  
331  1 Y 1 A PRO 589  ? C PRO 589  
332  1 Y 1 A CYS 590  ? C CYS 590  
333  1 Y 1 A SER 591  ? C SER 591  
334  1 Y 1 A PHE 592  ? C PHE 592  
335  1 Y 1 A GLY 593  ? C GLY 593  
336  1 Y 1 A GLY 594  ? C GLY 594  
337  1 Y 1 A VAL 595  ? C VAL 595  
338  1 Y 1 A SER 596  ? C SER 596  
339  1 Y 1 A VAL 597  ? C VAL 597  
340  1 Y 1 A ILE 598  ? C ILE 598  
341  1 Y 1 A THR 599  ? C THR 599  
342  1 Y 1 A PRO 600  ? C PRO 600  
343  1 Y 1 A GLY 601  ? C GLY 601  
344  1 Y 1 A THR 602  ? C THR 602  
345  1 Y 1 A ASN 603  ? C ASN 603  
346  1 Y 1 A THR 604  ? C THR 604  
347  1 Y 1 A SER 605  ? C SER 605  
348  1 Y 1 A ASN 606  ? C ASN 606  
349  1 Y 1 A GLN 607  ? C GLN 607  
350  1 Y 1 A VAL 608  ? C VAL 608  
351  1 Y 1 A ALA 609  ? C ALA 609  
352  1 Y 1 A VAL 610  ? C VAL 610  
353  1 Y 1 A LEU 611  ? C LEU 611  
354  1 Y 1 A TYR 612  ? C TYR 612  
355  1 Y 1 A GLN 613  ? C GLN 613  
356  1 Y 1 A GLY 614  ? C GLY 614  
357  1 Y 1 A VAL 615  ? C VAL 615  
358  1 Y 1 A ASN 616  ? C ASN 616  
359  1 Y 1 A CYS 617  ? C CYS 617  
360  1 Y 1 A THR 618  ? C THR 618  
361  1 Y 1 A GLU 619  ? C GLU 619  
362  1 Y 1 A VAL 620  ? C VAL 620  
363  1 Y 1 A PRO 621  ? C PRO 621  
364  1 Y 1 A VAL 622  ? C VAL 622  
365  1 Y 1 A ALA 623  ? C ALA 623  
366  1 Y 1 A ILE 624  ? C ILE 624  
367  1 Y 1 A HIS 625  ? C HIS 625  
368  1 Y 1 A ALA 626  ? C ALA 626  
369  1 Y 1 A ASP 627  ? C ASP 627  
370  1 Y 1 A GLN 628  ? C GLN 628  
371  1 Y 1 A LEU 629  ? C LEU 629  
372  1 Y 1 A THR 630  ? C THR 630  
373  1 Y 1 A PRO 631  ? C PRO 631  
374  1 Y 1 A THR 632  ? C THR 632  
375  1 Y 1 A TRP 633  ? C TRP 633  
376  1 Y 1 A ARG 634  ? C ARG 634  
377  1 Y 1 A VAL 635  ? C VAL 635  
378  1 Y 1 A TYR 636  ? C TYR 636  
379  1 Y 1 A SER 637  ? C SER 637  
380  1 Y 1 A THR 638  ? C THR 638  
381  1 Y 1 A GLY 639  ? C GLY 639  
382  1 Y 1 A SER 640  ? C SER 640  
383  1 Y 1 A ASN 641  ? C ASN 641  
384  1 Y 1 A VAL 642  ? C VAL 642  
385  1 Y 1 A PHE 643  ? C PHE 643  
386  1 Y 1 A GLN 644  ? C GLN 644  
387  1 Y 1 A THR 645  ? C THR 645  
388  1 Y 1 A ARG 646  ? C ARG 646  
389  1 Y 1 A ALA 647  ? C ALA 647  
390  1 Y 1 A GLY 648  ? C GLY 648  
391  1 Y 1 A CYS 649  ? C CYS 649  
392  1 Y 1 A LEU 650  ? C LEU 650  
393  1 Y 1 A ILE 651  ? C ILE 651  
394  1 Y 1 A GLY 652  ? C GLY 652  
395  1 Y 1 A ALA 653  ? C ALA 653  
396  1 Y 1 A GLU 654  ? C GLU 654  
397  1 Y 1 A HIS 655  ? C HIS 655  
398  1 Y 1 A VAL 656  ? C VAL 656  
399  1 Y 1 A ASN 657  ? C ASN 657  
400  1 Y 1 A ASN 658  ? C ASN 658  
401  1 Y 1 A SER 659  ? C SER 659  
402  1 Y 1 A TYR 660  ? C TYR 660  
403  1 Y 1 A GLU 661  ? C GLU 661  
404  1 Y 1 A CYS 662  ? C CYS 662  
405  1 Y 1 A ASP 663  ? C ASP 663  
406  1 Y 1 A ILE 664  ? C ILE 664  
407  1 Y 1 A PRO 665  ? C PRO 665  
408  1 Y 1 A ILE 666  ? C ILE 666  
409  1 Y 1 A GLY 667  ? C GLY 667  
410  1 Y 1 A ALA 668  ? C ALA 668  
411  1 Y 1 A GLY 669  ? C GLY 669  
412  1 Y 1 A ILE 670  ? C ILE 670  
413  1 Y 1 A CYS 671  ? C CYS 671  
414  1 Y 1 A ALA 672  ? C ALA 672  
415  1 Y 1 A SER 673  ? C SER 673  
416  1 Y 1 A TYR 674  ? C TYR 674  
417  1 Y 1 A GLN 675  ? C GLN 675  
418  1 Y 1 A THR 676  ? C THR 676  
419  1 Y 1 A GLN 677  ? C GLN 677  
420  1 Y 1 A THR 678  ? C THR 678  
421  1 Y 1 A ASN 679  ? C ASN 679  
422  1 Y 1 A SER 680  ? C SER 680  
423  1 Y 1 A ARG 681  ? C ARG 681  
424  1 Y 1 A ARG 682  ? C ARG 682  
425  1 Y 1 A ARG 683  ? C ARG 683  
426  1 Y 1 A ALA 684  ? C ALA 684  
427  1 Y 1 A ARG 685  ? C ARG 685  
428  1 Y 1 A SER 686  ? C SER 686  
429  1 Y 1 A VAL 687  ? C VAL 687  
430  1 Y 1 A ALA 688  ? C ALA 688  
431  1 Y 1 A SER 689  ? C SER 689  
432  1 Y 1 A GLN 690  ? C GLN 690  
433  1 Y 1 A SER 691  ? C SER 691  
434  1 Y 1 A ILE 692  ? C ILE 692  
435  1 Y 1 A ILE 693  ? C ILE 693  
436  1 Y 1 A ALA 694  ? C ALA 694  
437  1 Y 1 A TYR 695  ? C TYR 695  
438  1 Y 1 A THR 696  ? C THR 696  
439  1 Y 1 A MET 697  ? C MET 697  
440  1 Y 1 A SER 698  ? C SER 698  
441  1 Y 1 A LEU 699  ? C LEU 699  
442  1 Y 1 A GLY 700  ? C GLY 700  
443  1 Y 1 A ALA 701  ? C ALA 701  
444  1 Y 1 A GLU 702  ? C GLU 702  
445  1 Y 1 A ASN 703  ? C ASN 703  
446  1 Y 1 A SER 704  ? C SER 704  
447  1 Y 1 A VAL 705  ? C VAL 705  
448  1 Y 1 A ALA 706  ? C ALA 706  
449  1 Y 1 A TYR 707  ? C TYR 707  
450  1 Y 1 A SER 708  ? C SER 708  
451  1 Y 1 A ASN 709  ? C ASN 709  
452  1 Y 1 A ASN 710  ? C ASN 710  
453  1 Y 1 A SER 711  ? C SER 711  
454  1 Y 1 A ILE 712  ? C ILE 712  
455  1 Y 1 A ALA 713  ? C ALA 713  
456  1 Y 1 A ILE 714  ? C ILE 714  
457  1 Y 1 A PRO 715  ? C PRO 715  
458  1 Y 1 A THR 716  ? C THR 716  
459  1 Y 1 A ASN 717  ? C ASN 717  
460  1 Y 1 A PHE 718  ? C PHE 718  
461  1 Y 1 A THR 719  ? C THR 719  
462  1 Y 1 A ILE 720  ? C ILE 720  
463  1 Y 1 A SER 721  ? C SER 721  
464  1 Y 1 A VAL 722  ? C VAL 722  
465  1 Y 1 A THR 723  ? C THR 723  
466  1 Y 1 A THR 724  ? C THR 724  
467  1 Y 1 A GLU 725  ? C GLU 725  
468  1 Y 1 A ILE 726  ? C ILE 726  
469  1 Y 1 A LEU 727  ? C LEU 727  
470  1 Y 1 A PRO 728  ? C PRO 728  
471  1 Y 1 A VAL 729  ? C VAL 729  
472  1 Y 1 A SER 730  ? C SER 730  
473  1 Y 1 A MET 731  ? C MET 731  
474  1 Y 1 A THR 732  ? C THR 732  
475  1 Y 1 A LYS 733  ? C LYS 733  
476  1 Y 1 A THR 734  ? C THR 734  
477  1 Y 1 A SER 735  ? C SER 735  
478  1 Y 1 A VAL 736  ? C VAL 736  
479  1 Y 1 A ASP 737  ? C ASP 737  
480  1 Y 1 A CYS 738  ? C CYS 738  
481  1 Y 1 A THR 739  ? C THR 739  
482  1 Y 1 A MET 740  ? C MET 740  
483  1 Y 1 A TYR 741  ? C TYR 741  
484  1 Y 1 A ILE 742  ? C ILE 742  
485  1 Y 1 A CYS 743  ? C CYS 743  
486  1 Y 1 A GLY 744  ? C GLY 744  
487  1 Y 1 A ASP 745  ? C ASP 745  
488  1 Y 1 A SER 746  ? C SER 746  
489  1 Y 1 A THR 747  ? C THR 747  
490  1 Y 1 A GLU 748  ? C GLU 748  
491  1 Y 1 A CYS 749  ? C CYS 749  
492  1 Y 1 A SER 750  ? C SER 750  
493  1 Y 1 A ASN 751  ? C ASN 751  
494  1 Y 1 A LEU 752  ? C LEU 752  
495  1 Y 1 A LEU 753  ? C LEU 753  
496  1 Y 1 A LEU 754  ? C LEU 754  
497  1 Y 1 A GLN 755  ? C GLN 755  
498  1 Y 1 A TYR 756  ? C TYR 756  
499  1 Y 1 A GLY 757  ? C GLY 757  
500  1 Y 1 A SER 758  ? C SER 758  
501  1 Y 1 A PHE 759  ? C PHE 759  
502  1 Y 1 A CYS 760  ? C CYS 760  
503  1 Y 1 A THR 761  ? C THR 761  
504  1 Y 1 A GLN 762  ? C GLN 762  
505  1 Y 1 A LEU 763  ? C LEU 763  
506  1 Y 1 A ASN 764  ? C ASN 764  
507  1 Y 1 A ARG 765  ? C ARG 765  
508  1 Y 1 A ALA 766  ? C ALA 766  
509  1 Y 1 A LEU 767  ? C LEU 767  
510  1 Y 1 A THR 768  ? C THR 768  
511  1 Y 1 A GLY 769  ? C GLY 769  
512  1 Y 1 A ILE 770  ? C ILE 770  
513  1 Y 1 A ALA 771  ? C ALA 771  
514  1 Y 1 A VAL 772  ? C VAL 772  
515  1 Y 1 A GLU 773  ? C GLU 773  
516  1 Y 1 A GLN 774  ? C GLN 774  
517  1 Y 1 A ASP 775  ? C ASP 775  
518  1 Y 1 A LYS 776  ? C LYS 776  
519  1 Y 1 A ASN 777  ? C ASN 777  
520  1 Y 1 A THR 778  ? C THR 778  
521  1 Y 1 A GLN 779  ? C GLN 779  
522  1 Y 1 A GLU 780  ? C GLU 780  
523  1 Y 1 A VAL 781  ? C VAL 781  
524  1 Y 1 A PHE 782  ? C PHE 782  
525  1 Y 1 A ALA 783  ? C ALA 783  
526  1 Y 1 A GLN 784  ? C GLN 784  
527  1 Y 1 A VAL 785  ? C VAL 785  
528  1 Y 1 A LYS 786  ? C LYS 786  
529  1 Y 1 A GLN 787  ? C GLN 787  
530  1 Y 1 A ILE 788  ? C ILE 788  
531  1 Y 1 A TYR 789  ? C TYR 789  
532  1 Y 1 A LYS 790  ? C LYS 790  
533  1 Y 1 A THR 791  ? C THR 791  
534  1 Y 1 A PRO 792  ? C PRO 792  
535  1 Y 1 A PRO 793  ? C PRO 793  
536  1 Y 1 A ILE 794  ? C ILE 794  
537  1 Y 1 A LYS 795  ? C LYS 795  
538  1 Y 1 A ASP 796  ? C ASP 796  
539  1 Y 1 A PHE 797  ? C PHE 797  
540  1 Y 1 A GLY 798  ? C GLY 798  
541  1 Y 1 A GLY 799  ? C GLY 799  
542  1 Y 1 A PHE 800  ? C PHE 800  
543  1 Y 1 A ASN 801  ? C ASN 801  
544  1 Y 1 A PHE 802  ? C PHE 802  
545  1 Y 1 A SER 803  ? C SER 803  
546  1 Y 1 A GLN 804  ? C GLN 804  
547  1 Y 1 A ILE 805  ? C ILE 805  
548  1 Y 1 A LEU 806  ? C LEU 806  
549  1 Y 1 A PRO 807  ? C PRO 807  
550  1 Y 1 A ASP 808  ? C ASP 808  
551  1 Y 1 A PRO 809  ? C PRO 809  
552  1 Y 1 A SER 810  ? C SER 810  
553  1 Y 1 A LYS 811  ? C LYS 811  
554  1 Y 1 A PRO 812  ? C PRO 812  
555  1 Y 1 A SER 813  ? C SER 813  
556  1 Y 1 A LYS 814  ? C LYS 814  
557  1 Y 1 A ARG 815  ? C ARG 815  
558  1 Y 1 A SER 816  ? C SER 816  
559  1 Y 1 A PRO 817  ? C PRO 817  
560  1 Y 1 A ILE 818  ? C ILE 818  
561  1 Y 1 A GLU 819  ? C GLU 819  
562  1 Y 1 A ASP 820  ? C ASP 820  
563  1 Y 1 A LEU 821  ? C LEU 821  
564  1 Y 1 A LEU 822  ? C LEU 822  
565  1 Y 1 A PHE 823  ? C PHE 823  
566  1 Y 1 A ASN 824  ? C ASN 824  
567  1 Y 1 A LYS 825  ? C LYS 825  
568  1 Y 1 A VAL 826  ? C VAL 826  
569  1 Y 1 A THR 827  ? C THR 827  
570  1 Y 1 A LEU 828  ? C LEU 828  
571  1 Y 1 A ALA 829  ? C ALA 829  
572  1 Y 1 A ASP 830  ? C ASP 830  
573  1 Y 1 A ALA 831  ? C ALA 831  
574  1 Y 1 A GLY 832  ? C GLY 832  
575  1 Y 1 A PHE 833  ? C PHE 833  
576  1 Y 1 A ILE 834  ? C ILE 834  
577  1 Y 1 A LYS 835  ? C LYS 835  
578  1 Y 1 A GLN 836  ? C GLN 836  
579  1 Y 1 A TYR 837  ? C TYR 837  
580  1 Y 1 A GLY 838  ? C GLY 838  
581  1 Y 1 A ASP 839  ? C ASP 839  
582  1 Y 1 A CYS 840  ? C CYS 840  
583  1 Y 1 A LEU 841  ? C LEU 841  
584  1 Y 1 A GLY 842  ? C GLY 842  
585  1 Y 1 A ASP 843  ? C ASP 843  
586  1 Y 1 A ILE 844  ? C ILE 844  
587  1 Y 1 A ALA 845  ? C ALA 845  
588  1 Y 1 A ALA 846  ? C ALA 846  
589  1 Y 1 A ARG 847  ? C ARG 847  
590  1 Y 1 A ASP 848  ? C ASP 848  
591  1 Y 1 A LEU 849  ? C LEU 849  
592  1 Y 1 A ILE 850  ? C ILE 850  
593  1 Y 1 A CYS 851  ? C CYS 851  
594  1 Y 1 A ALA 852  ? C ALA 852  
595  1 Y 1 A GLN 853  ? C GLN 853  
596  1 Y 1 A LYS 854  ? C LYS 854  
597  1 Y 1 A PHE 855  ? C PHE 855  
598  1 Y 1 A ASN 856  ? C ASN 856  
599  1 Y 1 A GLY 857  ? C GLY 857  
600  1 Y 1 A LEU 858  ? C LEU 858  
601  1 Y 1 A THR 859  ? C THR 859  
602  1 Y 1 A VAL 860  ? C VAL 860  
603  1 Y 1 A LEU 861  ? C LEU 861  
604  1 Y 1 A PRO 862  ? C PRO 862  
605  1 Y 1 A PRO 863  ? C PRO 863  
606  1 Y 1 A LEU 864  ? C LEU 864  
607  1 Y 1 A LEU 865  ? C LEU 865  
608  1 Y 1 A THR 866  ? C THR 866  
609  1 Y 1 A ASP 867  ? C ASP 867  
610  1 Y 1 A GLU 868  ? C GLU 868  
611  1 Y 1 A MET 869  ? C MET 869  
612  1 Y 1 A ILE 870  ? C ILE 870  
613  1 Y 1 A ALA 871  ? C ALA 871  
614  1 Y 1 A GLN 872  ? C GLN 872  
615  1 Y 1 A TYR 873  ? C TYR 873  
616  1 Y 1 A THR 874  ? C THR 874  
617  1 Y 1 A SER 875  ? C SER 875  
618  1 Y 1 A ALA 876  ? C ALA 876  
619  1 Y 1 A LEU 877  ? C LEU 877  
620  1 Y 1 A LEU 878  ? C LEU 878  
621  1 Y 1 A ALA 879  ? C ALA 879  
622  1 Y 1 A GLY 880  ? C GLY 880  
623  1 Y 1 A THR 881  ? C THR 881  
624  1 Y 1 A ILE 882  ? C ILE 882  
625  1 Y 1 A THR 883  ? C THR 883  
626  1 Y 1 A SER 884  ? C SER 884  
627  1 Y 1 A GLY 885  ? C GLY 885  
628  1 Y 1 A TRP 886  ? C TRP 886  
629  1 Y 1 A THR 887  ? C THR 887  
630  1 Y 1 A PHE 888  ? C PHE 888  
631  1 Y 1 A GLY 889  ? C GLY 889  
632  1 Y 1 A ALA 890  ? C ALA 890  
633  1 Y 1 A GLY 891  ? C GLY 891  
634  1 Y 1 A PRO 892  ? C PRO 892  
635  1 Y 1 A ALA 893  ? C ALA 893  
636  1 Y 1 A LEU 894  ? C LEU 894  
637  1 Y 1 A GLN 895  ? C GLN 895  
638  1 Y 1 A ILE 896  ? C ILE 896  
639  1 Y 1 A PRO 897  ? C PRO 897  
640  1 Y 1 A PHE 898  ? C PHE 898  
641  1 Y 1 A PRO 899  ? C PRO 899  
642  1 Y 1 A MET 900  ? C MET 900  
643  1 Y 1 A GLN 901  ? C GLN 901  
644  1 Y 1 A MET 902  ? C MET 902  
645  1 Y 1 A ALA 903  ? C ALA 903  
646  1 Y 1 A TYR 904  ? C TYR 904  
647  1 Y 1 A ARG 905  ? C ARG 905  
648  1 Y 1 A PHE 906  ? C PHE 906  
649  1 Y 1 A ASN 907  ? C ASN 907  
650  1 Y 1 A GLY 908  ? C GLY 908  
651  1 Y 1 A ILE 909  ? C ILE 909  
652  1 Y 1 A GLY 910  ? C GLY 910  
653  1 Y 1 A VAL 911  ? C VAL 911  
654  1 Y 1 A THR 912  ? C THR 912  
655  1 Y 1 A GLN 913  ? C GLN 913  
656  1 Y 1 A ASN 914  ? C ASN 914  
657  1 Y 1 A VAL 915  ? C VAL 915  
658  1 Y 1 A LEU 916  ? C LEU 916  
659  1 Y 1 A TYR 917  ? C TYR 917  
660  1 Y 1 A GLU 918  ? C GLU 918  
661  1 Y 1 A ASN 919  ? C ASN 919  
662  1 Y 1 A GLN 920  ? C GLN 920  
663  1 Y 1 A LYS 921  ? C LYS 921  
664  1 Y 1 A LEU 922  ? C LEU 922  
665  1 Y 1 A ILE 923  ? C ILE 923  
666  1 Y 1 A ALA 924  ? C ALA 924  
667  1 Y 1 A ASN 925  ? C ASN 925  
668  1 Y 1 A GLN 926  ? C GLN 926  
669  1 Y 1 A PHE 927  ? C PHE 927  
670  1 Y 1 A ASN 928  ? C ASN 928  
671  1 Y 1 A SER 929  ? C SER 929  
672  1 Y 1 A ALA 930  ? C ALA 930  
673  1 Y 1 A ILE 931  ? C ILE 931  
674  1 Y 1 A GLY 932  ? C GLY 932  
675  1 Y 1 A LYS 933  ? C LYS 933  
676  1 Y 1 A ILE 934  ? C ILE 934  
677  1 Y 1 A GLN 935  ? C GLN 935  
678  1 Y 1 A ASP 936  ? C ASP 936  
679  1 Y 1 A SER 937  ? C SER 937  
680  1 Y 1 A LEU 938  ? C LEU 938  
681  1 Y 1 A SER 939  ? C SER 939  
682  1 Y 1 A SER 940  ? C SER 940  
683  1 Y 1 A THR 941  ? C THR 941  
684  1 Y 1 A PRO 942  ? C PRO 942  
685  1 Y 1 A SER 943  ? C SER 943  
686  1 Y 1 A ALA 944  ? C ALA 944  
687  1 Y 1 A LEU 945  ? C LEU 945  
688  1 Y 1 A GLY 946  ? C GLY 946  
689  1 Y 1 A LYS 947  ? C LYS 947  
690  1 Y 1 A LEU 948  ? C LEU 948  
691  1 Y 1 A GLN 949  ? C GLN 949  
692  1 Y 1 A ASP 950  ? C ASP 950  
693  1 Y 1 A VAL 951  ? C VAL 951  
694  1 Y 1 A VAL 952  ? C VAL 952  
695  1 Y 1 A ASN 953  ? C ASN 953  
696  1 Y 1 A GLN 954  ? C GLN 954  
697  1 Y 1 A ASN 955  ? C ASN 955  
698  1 Y 1 A ALA 956  ? C ALA 956  
699  1 Y 1 A GLN 957  ? C GLN 957  
700  1 Y 1 A ALA 958  ? C ALA 958  
701  1 Y 1 A LEU 959  ? C LEU 959  
702  1 Y 1 A ASN 960  ? C ASN 960  
703  1 Y 1 A THR 961  ? C THR 961  
704  1 Y 1 A LEU 962  ? C LEU 962  
705  1 Y 1 A VAL 963  ? C VAL 963  
706  1 Y 1 A LYS 964  ? C LYS 964  
707  1 Y 1 A GLN 965  ? C GLN 965  
708  1 Y 1 A LEU 966  ? C LEU 966  
709  1 Y 1 A SER 967  ? C SER 967  
710  1 Y 1 A SER 968  ? C SER 968  
711  1 Y 1 A ASN 969  ? C ASN 969  
712  1 Y 1 A PHE 970  ? C PHE 970  
713  1 Y 1 A GLY 971  ? C GLY 971  
714  1 Y 1 A ALA 972  ? C ALA 972  
715  1 Y 1 A ILE 973  ? C ILE 973  
716  1 Y 1 A SER 974  ? C SER 974  
717  1 Y 1 A SER 975  ? C SER 975  
718  1 Y 1 A VAL 976  ? C VAL 976  
719  1 Y 1 A LEU 977  ? C LEU 977  
720  1 Y 1 A ASN 978  ? C ASN 978  
721  1 Y 1 A ASP 979  ? C ASP 979  
722  1 Y 1 A ILE 980  ? C ILE 980  
723  1 Y 1 A LEU 981  ? C LEU 981  
724  1 Y 1 A SER 982  ? C SER 982  
725  1 Y 1 A ARG 983  ? C ARG 983  
726  1 Y 1 A LEU 984  ? C LEU 984  
727  1 Y 1 A CYS 985  ? C CYS 985  
728  1 Y 1 A PRO 986  ? C PRO 986  
729  1 Y 1 A PRO 987  ? C PRO 987  
730  1 Y 1 A GLU 988  ? C GLU 988  
731  1 Y 1 A ALA 989  ? C ALA 989  
732  1 Y 1 A GLU 990  ? C GLU 990  
733  1 Y 1 A VAL 991  ? C VAL 991  
734  1 Y 1 A GLN 992  ? C GLN 992  
735  1 Y 1 A ILE 993  ? C ILE 993  
736  1 Y 1 A ASP 994  ? C ASP 994  
737  1 Y 1 A ARG 995  ? C ARG 995  
738  1 Y 1 A LEU 996  ? C LEU 996  
739  1 Y 1 A ILE 997  ? C ILE 997  
740  1 Y 1 A THR 998  ? C THR 998  
741  1 Y 1 A GLY 999  ? C GLY 999  
742  1 Y 1 A ARG 1000 ? C ARG 1000 
743  1 Y 1 A LEU 1001 ? C LEU 1001 
744  1 Y 1 A GLN 1002 ? C GLN 1002 
745  1 Y 1 A SER 1003 ? C SER 1003 
746  1 Y 1 A LEU 1004 ? C LEU 1004 
747  1 Y 1 A GLN 1005 ? C GLN 1005 
748  1 Y 1 A THR 1006 ? C THR 1006 
749  1 Y 1 A TYR 1007 ? C TYR 1007 
750  1 Y 1 A VAL 1008 ? C VAL 1008 
751  1 Y 1 A THR 1009 ? C THR 1009 
752  1 Y 1 A GLN 1010 ? C GLN 1010 
753  1 Y 1 A GLN 1011 ? C GLN 1011 
754  1 Y 1 A LEU 1012 ? C LEU 1012 
755  1 Y 1 A ILE 1013 ? C ILE 1013 
756  1 Y 1 A ARG 1014 ? C ARG 1014 
757  1 Y 1 A ALA 1015 ? C ALA 1015 
758  1 Y 1 A ALA 1016 ? C ALA 1016 
759  1 Y 1 A GLU 1017 ? C GLU 1017 
760  1 Y 1 A ILE 1018 ? C ILE 1018 
761  1 Y 1 A ARG 1019 ? C ARG 1019 
762  1 Y 1 A ALA 1020 ? C ALA 1020 
763  1 Y 1 A SER 1021 ? C SER 1021 
764  1 Y 1 A ALA 1022 ? C ALA 1022 
765  1 Y 1 A ASN 1023 ? C ASN 1023 
766  1 Y 1 A LEU 1024 ? C LEU 1024 
767  1 Y 1 A ALA 1025 ? C ALA 1025 
768  1 Y 1 A ALA 1026 ? C ALA 1026 
769  1 Y 1 A THR 1027 ? C THR 1027 
770  1 Y 1 A LYS 1028 ? C LYS 1028 
771  1 Y 1 A MET 1029 ? C MET 1029 
772  1 Y 1 A SER 1030 ? C SER 1030 
773  1 Y 1 A GLU 1031 ? C GLU 1031 
774  1 Y 1 A CYS 1032 ? C CYS 1032 
775  1 Y 1 A VAL 1033 ? C VAL 1033 
776  1 Y 1 A LEU 1034 ? C LEU 1034 
777  1 Y 1 A GLY 1035 ? C GLY 1035 
778  1 Y 1 A GLN 1036 ? C GLN 1036 
779  1 Y 1 A SER 1037 ? C SER 1037 
780  1 Y 1 A LYS 1038 ? C LYS 1038 
781  1 Y 1 A ARG 1039 ? C ARG 1039 
782  1 Y 1 A VAL 1040 ? C VAL 1040 
783  1 Y 1 A ASP 1041 ? C ASP 1041 
784  1 Y 1 A PHE 1042 ? C PHE 1042 
785  1 Y 1 A CYS 1043 ? C CYS 1043 
786  1 Y 1 A GLY 1044 ? C GLY 1044 
787  1 Y 1 A LYS 1045 ? C LYS 1045 
788  1 Y 1 A GLY 1046 ? C GLY 1046 
789  1 Y 1 A TYR 1047 ? C TYR 1047 
790  1 Y 1 A HIS 1048 ? C HIS 1048 
791  1 Y 1 A LEU 1049 ? C LEU 1049 
792  1 Y 1 A MET 1050 ? C MET 1050 
793  1 Y 1 A SER 1051 ? C SER 1051 
794  1 Y 1 A PHE 1052 ? C PHE 1052 
795  1 Y 1 A PRO 1053 ? C PRO 1053 
796  1 Y 1 A GLN 1054 ? C GLN 1054 
797  1 Y 1 A SER 1055 ? C SER 1055 
798  1 Y 1 A ALA 1056 ? C ALA 1056 
799  1 Y 1 A PRO 1057 ? C PRO 1057 
800  1 Y 1 A HIS 1058 ? C HIS 1058 
801  1 Y 1 A GLY 1059 ? C GLY 1059 
802  1 Y 1 A VAL 1060 ? C VAL 1060 
803  1 Y 1 A VAL 1061 ? C VAL 1061 
804  1 Y 1 A PHE 1062 ? C PHE 1062 
805  1 Y 1 A LEU 1063 ? C LEU 1063 
806  1 Y 1 A HIS 1064 ? C HIS 1064 
807  1 Y 1 A VAL 1065 ? C VAL 1065 
808  1 Y 1 A THR 1066 ? C THR 1066 
809  1 Y 1 A TYR 1067 ? C TYR 1067 
810  1 Y 1 A VAL 1068 ? C VAL 1068 
811  1 Y 1 A PRO 1069 ? C PRO 1069 
812  1 Y 1 A ALA 1070 ? C ALA 1070 
813  1 Y 1 A HIS 1071 ? C HIS 1071 
814  1 Y 1 A GLU 1072 ? C GLU 1072 
815  1 Y 1 A LYS 1073 ? C LYS 1073 
816  1 Y 1 A ASN 1074 ? C ASN 1074 
817  1 Y 1 A PHE 1075 ? C PHE 1075 
818  1 Y 1 A THR 1076 ? C THR 1076 
819  1 Y 1 A THR 1077 ? C THR 1077 
820  1 Y 1 A ALA 1078 ? C ALA 1078 
821  1 Y 1 A PRO 1079 ? C PRO 1079 
822  1 Y 1 A ALA 1080 ? C ALA 1080 
823  1 Y 1 A ILE 1081 ? C ILE 1081 
824  1 Y 1 A CYS 1082 ? C CYS 1082 
825  1 Y 1 A HIS 1083 ? C HIS 1083 
826  1 Y 1 A ASP 1084 ? C ASP 1084 
827  1 Y 1 A GLY 1085 ? C GLY 1085 
828  1 Y 1 A LYS 1086 ? C LYS 1086 
829  1 Y 1 A ALA 1087 ? C ALA 1087 
830  1 Y 1 A HIS 1088 ? C HIS 1088 
831  1 Y 1 A PHE 1089 ? C PHE 1089 
832  1 Y 1 A PRO 1090 ? C PRO 1090 
833  1 Y 1 A ARG 1091 ? C ARG 1091 
834  1 Y 1 A GLU 1092 ? C GLU 1092 
835  1 Y 1 A GLY 1093 ? C GLY 1093 
836  1 Y 1 A VAL 1094 ? C VAL 1094 
837  1 Y 1 A PHE 1095 ? C PHE 1095 
838  1 Y 1 A VAL 1096 ? C VAL 1096 
839  1 Y 1 A SER 1097 ? C SER 1097 
840  1 Y 1 A ASN 1098 ? C ASN 1098 
841  1 Y 1 A GLY 1099 ? C GLY 1099 
842  1 Y 1 A THR 1100 ? C THR 1100 
843  1 Y 1 A HIS 1101 ? C HIS 1101 
844  1 Y 1 A TRP 1102 ? C TRP 1102 
845  1 Y 1 A PHE 1103 ? C PHE 1103 
846  1 Y 1 A VAL 1104 ? C VAL 1104 
847  1 Y 1 A THR 1105 ? C THR 1105 
848  1 Y 1 A GLN 1106 ? C GLN 1106 
849  1 Y 1 A ARG 1107 ? C ARG 1107 
850  1 Y 1 A ASN 1108 ? C ASN 1108 
851  1 Y 1 A PHE 1109 ? C PHE 1109 
852  1 Y 1 A TYR 1110 ? C TYR 1110 
853  1 Y 1 A GLU 1111 ? C GLU 1111 
854  1 Y 1 A PRO 1112 ? C PRO 1112 
855  1 Y 1 A GLN 1113 ? C GLN 1113 
856  1 Y 1 A ILE 1114 ? C ILE 1114 
857  1 Y 1 A ILE 1115 ? C ILE 1115 
858  1 Y 1 A THR 1116 ? C THR 1116 
859  1 Y 1 A THR 1117 ? C THR 1117 
860  1 Y 1 A ASP 1118 ? C ASP 1118 
861  1 Y 1 A ASN 1119 ? C ASN 1119 
862  1 Y 1 A THR 1120 ? C THR 1120 
863  1 Y 1 A PHE 1121 ? C PHE 1121 
864  1 Y 1 A VAL 1122 ? C VAL 1122 
865  1 Y 1 A SER 1123 ? C SER 1123 
866  1 Y 1 A GLY 1124 ? C GLY 1124 
867  1 Y 1 A ASN 1125 ? C ASN 1125 
868  1 Y 1 A CYS 1126 ? C CYS 1126 
869  1 Y 1 A ASP 1127 ? C ASP 1127 
870  1 Y 1 A VAL 1128 ? C VAL 1128 
871  1 Y 1 A VAL 1129 ? C VAL 1129 
872  1 Y 1 A ILE 1130 ? C ILE 1130 
873  1 Y 1 A GLY 1131 ? C GLY 1131 
874  1 Y 1 A ILE 1132 ? C ILE 1132 
875  1 Y 1 A VAL 1133 ? C VAL 1133 
876  1 Y 1 A ASN 1134 ? C ASN 1134 
877  1 Y 1 A ASN 1135 ? C ASN 1135 
878  1 Y 1 A THR 1136 ? C THR 1136 
879  1 Y 1 A VAL 1137 ? C VAL 1137 
880  1 Y 1 A TYR 1138 ? C TYR 1138 
881  1 Y 1 A ASP 1139 ? C ASP 1139 
882  1 Y 1 A PRO 1140 ? C PRO 1140 
883  1 Y 1 A LEU 1141 ? C LEU 1141 
884  1 Y 1 A GLN 1142 ? C GLN 1142 
885  1 Y 1 A PRO 1143 ? C PRO 1143 
886  1 Y 1 A GLU 1144 ? C GLU 1144 
887  1 Y 1 A LEU 1145 ? C LEU 1145 
888  1 Y 1 A ASP 1146 ? C ASP 1146 
889  1 Y 1 A SER 1147 ? C SER 1147 
890  1 Y 1 A PHE 1148 ? C PHE 1148 
891  1 Y 1 A LYS 1149 ? C LYS 1149 
892  1 Y 1 A GLU 1150 ? C GLU 1150 
893  1 Y 1 A GLU 1151 ? C GLU 1151 
894  1 Y 1 A LEU 1152 ? C LEU 1152 
895  1 Y 1 A ASP 1153 ? C ASP 1153 
896  1 Y 1 A LYS 1154 ? C LYS 1154 
897  1 Y 1 A TYR 1155 ? C TYR 1155 
898  1 Y 1 A PHE 1156 ? C PHE 1156 
899  1 Y 1 A LYS 1157 ? C LYS 1157 
900  1 Y 1 A ASN 1158 ? C ASN 1158 
901  1 Y 1 A HIS 1159 ? C HIS 1159 
902  1 Y 1 A THR 1160 ? C THR 1160 
903  1 Y 1 A SER 1161 ? C SER 1161 
904  1 Y 1 A PRO 1162 ? C PRO 1162 
905  1 Y 1 A ASP 1163 ? C ASP 1163 
906  1 Y 1 A VAL 1164 ? C VAL 1164 
907  1 Y 1 A ASP 1165 ? C ASP 1165 
908  1 Y 1 A LEU 1166 ? C LEU 1166 
909  1 Y 1 A GLY 1167 ? C GLY 1167 
910  1 Y 1 A ASP 1168 ? C ASP 1168 
911  1 Y 1 A ILE 1169 ? C ILE 1169 
912  1 Y 1 A SER 1170 ? C SER 1170 
913  1 Y 1 A GLY 1171 ? C GLY 1171 
914  1 Y 1 A ILE 1172 ? C ILE 1172 
915  1 Y 1 A ASN 1173 ? C ASN 1173 
916  1 Y 1 A ALA 1174 ? C ALA 1174 
917  1 Y 1 A SER 1175 ? C SER 1175 
918  1 Y 1 A VAL 1176 ? C VAL 1176 
919  1 Y 1 A VAL 1177 ? C VAL 1177 
920  1 Y 1 A ASN 1178 ? C ASN 1178 
921  1 Y 1 A ILE 1179 ? C ILE 1179 
922  1 Y 1 A GLN 1180 ? C GLN 1180 
923  1 Y 1 A LYS 1181 ? C LYS 1181 
924  1 Y 1 A GLU 1182 ? C GLU 1182 
925  1 Y 1 A ILE 1183 ? C ILE 1183 
926  1 Y 1 A ASP 1184 ? C ASP 1184 
927  1 Y 1 A ARG 1185 ? C ARG 1185 
928  1 Y 1 A LEU 1186 ? C LEU 1186 
929  1 Y 1 A ASN 1187 ? C ASN 1187 
930  1 Y 1 A GLU 1188 ? C GLU 1188 
931  1 Y 1 A VAL 1189 ? C VAL 1189 
932  1 Y 1 A ALA 1190 ? C ALA 1190 
933  1 Y 1 A LYS 1191 ? C LYS 1191 
934  1 Y 1 A ASN 1192 ? C ASN 1192 
935  1 Y 1 A LEU 1193 ? C LEU 1193 
936  1 Y 1 A ASN 1194 ? C ASN 1194 
937  1 Y 1 A GLU 1195 ? C GLU 1195 
938  1 Y 1 A SER 1196 ? C SER 1196 
939  1 Y 1 A LEU 1197 ? C LEU 1197 
940  1 Y 1 A ILE 1198 ? C ILE 1198 
941  1 Y 1 A ASP 1199 ? C ASP 1199 
942  1 Y 1 A LEU 1200 ? C LEU 1200 
943  1 Y 1 A GLN 1201 ? C GLN 1201 
944  1 Y 1 A GLU 1202 ? C GLU 1202 
945  1 Y 1 A LEU 1203 ? C LEU 1203 
946  1 Y 1 A GLY 1204 ? C GLY 1204 
947  1 Y 1 A LYS 1205 ? C LYS 1205 
948  1 Y 1 A TYR 1206 ? C TYR 1206 
949  1 Y 1 A GLU 1207 ? C GLU 1207 
950  1 Y 1 A GLN 1208 ? C GLN 1208 
951  1 Y 1 A GLY 1209 ? C GLY 1209 
952  1 Y 1 A SER 1210 ? C SER 1210 
953  1 Y 1 A GLY 1211 ? C GLY 1211 
954  1 Y 1 A TYR 1212 ? C TYR 1212 
955  1 Y 1 A ILE 1213 ? C ILE 1213 
956  1 Y 1 A PRO 1214 ? C PRO 1214 
957  1 Y 1 A GLU 1215 ? C GLU 1215 
958  1 Y 1 A ALA 1216 ? C ALA 1216 
959  1 Y 1 A PRO 1217 ? C PRO 1217 
960  1 Y 1 A ARG 1218 ? C ARG 1218 
961  1 Y 1 A ASP 1219 ? C ASP 1219 
962  1 Y 1 A GLY 1220 ? C GLY 1220 
963  1 Y 1 A GLN 1221 ? C GLN 1221 
964  1 Y 1 A ALA 1222 ? C ALA 1222 
965  1 Y 1 A TYR 1223 ? C TYR 1223 
966  1 Y 1 A VAL 1224 ? C VAL 1224 
967  1 Y 1 A ARG 1225 ? C ARG 1225 
968  1 Y 1 A LYS 1226 ? C LYS 1226 
969  1 Y 1 A ASP 1227 ? C ASP 1227 
970  1 Y 1 A GLY 1228 ? C GLY 1228 
971  1 Y 1 A GLU 1229 ? C GLU 1229 
972  1 Y 1 A TRP 1230 ? C TRP 1230 
973  1 Y 1 A VAL 1231 ? C VAL 1231 
974  1 Y 1 A LEU 1232 ? C LEU 1232 
975  1 Y 1 A LEU 1233 ? C LEU 1233 
976  1 Y 1 A SER 1234 ? C SER 1234 
977  1 Y 1 A THR 1235 ? C THR 1235 
978  1 Y 1 A PHE 1236 ? C PHE 1236 
979  1 Y 1 A LEU 1237 ? C LEU 1237 
980  1 Y 1 A GLY 1238 ? C GLY 1238 
981  1 Y 1 A ARG 1239 ? C ARG 1239 
982  1 Y 1 A SER 1240 ? C SER 1240 
983  1 Y 1 A LEU 1241 ? C LEU 1241 
984  1 Y 1 A GLU 1242 ? C GLU 1242 
985  1 Y 1 A VAL 1243 ? C VAL 1243 
986  1 Y 1 A LEU 1244 ? C LEU 1244 
987  1 Y 1 A PHE 1245 ? C PHE 1245 
988  1 Y 1 A GLN 1246 ? C GLN 1246 
989  1 Y 1 A GLY 1247 ? C GLY 1247 
990  1 Y 1 A PRO 1248 ? C PRO 1248 
991  1 Y 1 A GLY 1249 ? C GLY 1249 
992  1 Y 1 A SER 1250 ? C SER 1250 
993  1 Y 1 A GLY 1251 ? C GLY 1251 
994  1 Y 1 A GLY 1252 ? C GLY 1252 
995  1 Y 1 A LEU 1253 ? C LEU 1253 
996  1 Y 1 A ASN 1254 ? C ASN 1254 
997  1 Y 1 A ASP 1255 ? C ASP 1255 
998  1 Y 1 A ILE 1256 ? C ILE 1256 
999  1 Y 1 A PHE 1257 ? C PHE 1257 
1000 1 Y 1 A GLU 1258 ? C GLU 1258 
1001 1 Y 1 A ALA 1259 ? C ALA 1259 
1002 1 Y 1 A GLN 1260 ? C GLN 1260 
1003 1 Y 1 A LYS 1261 ? C LYS 1261 
1004 1 Y 1 A ILE 1262 ? C ILE 1262 
1005 1 Y 1 A GLU 1263 ? C GLU 1263 
1006 1 Y 1 A TRP 1264 ? C TRP 1264 
1007 1 Y 1 A HIS 1265 ? C HIS 1265 
1008 1 Y 1 A GLU 1266 ? C GLU 1266 
1009 1 Y 1 A GLY 1267 ? C GLY 1267 
1010 1 Y 1 A SER 1268 ? C SER 1268 
1011 1 Y 1 A GLY 1269 ? C GLY 1269 
1012 1 Y 1 A HIS 1270 ? C HIS 1270 
1013 1 Y 1 A HIS 1271 ? C HIS 1271 
1014 1 Y 1 A HIS 1272 ? C HIS 1272 
1015 1 Y 1 A HIS 1273 ? C HIS 1273 
1016 1 Y 1 A HIS 1274 ? C HIS 1274 
1017 1 Y 1 A HIS 1275 ? C HIS 1275 
1018 1 Y 1 A HIS 1276 ? C HIS 1276 
1019 1 Y 1 A HIS 1277 ? C HIS 1277 
# 
_em_ctf_correction.id                       1 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
_em_ctf_correction.details                  ? 
# 
loop_
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
2 1 ? ? 2697049 ? ? 'Severe acute respiratory syndrome coronavirus 2' ? ? 
3 1 ? ? 9606    ? ? 'Homo sapiens'                                    ? ? 
# 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
_em_image_processing.details              ? 
# 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.avg_electron_dose_per_image         63 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
# 
loop_
_em_software.id 
_em_software.category 
_em_software.details 
_em_software.name 
_em_software.version 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
1  'PARTICLE SELECTION'       ? ? ? 1 ? ? 
2  'IMAGE ACQUISITION'        ? ? ? ? ? 1 
3  MASKING                    ? ? ? ? ? ? 
4  'CTF CORRECTION'           ? ? ? 1 ? ? 
5  'LAYERLINE INDEXING'       ? ? ? ? ? ? 
6  'DIFFRACTION INDEXING'     ? ? ? ? ? ? 
7  'MODEL FITTING'            ? ? ? ? ? ? 
8  'MODEL REFINEMENT'         ? ? ? ? ? ? 
9  OTHER                      ? ? ? ? ? ? 
10 'INITIAL EULER ASSIGNMENT' ? ? ? 1 ? ? 
11 'FINAL EULER ASSIGNMENT'   ? ? ? 1 ? ? 
12 CLASSIFICATION             ? ? ? 1 ? ? 
13 RECONSTRUCTION             ? ? ? 1 ? ? 
# 
_em_specimen.id                      1 
_em_specimen.experiment_id           1 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
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 
D 4 NAG 1 B NAG 1 A NAG 807 n 
D 4 NAG 2 B NAG 2 A NAG 808 n 
D 4 BMA 3 B BMA 3 A BMA 809 n 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
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                         
# 
_pdbx_entity_branch.entity_id   4 
_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 4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-                                             'Glycam Condensed Sequence' GMML       1.0   
2 4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
3 4 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}'        LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
_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                ? 
# 
